data_4465 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; The Structural role of the Copper-coordinating and Surface-exposed Histidine Residue in the Blue Copper Protein Azurin ; _BMRB_accession_number 4465 _BMRB_flat_file_name bmr4465.str _Entry_type original _Submission_date 1999-11-24 _Accession_date 1999-11-26 _Entry_origination author _NMR_STAR_version 2.1.1 _Experimental_method NMR _Details . loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Jeuken Lars J.C. . 2 Ubbink Marcellus . . 3 Bitter Johannes H. . 4 'van Vliet' Pieter . . 5 Meyer-Klaucke W. . . 6 Canters Gerard W. . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 245 "15N chemical shifts" 123 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2000-06-19 original author . stop_ _Original_release_date 2000-06-19 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full ; 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 _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 10835281 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Jeuken Lars J.C. . 2 Ubbink Marcellus . . 3 Bitter Johannes H. . 4 'van Vliet' Pieter . . 5 Meyer-Klaucke W. . . 6 Canters Gerard W. . stop_ _Journal_abbreviation 'J. Mol. Biol.' _Journal_name_full 'Journal of Molecular Biology' _Journal_volume 299 _Journal_issue 3 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 737 _Page_last 755 _Year 2000 _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were performed on samples of a variant azurin in which the surface exposed histidine ligand of the copper (His117) had been replaced by a glycine ; save_ ####################################### # Cited references within the entry # ####################################### save_Ref._1 _Saveframe_category citation _Citation_full ; 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 . _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID ? _Journal_abbreviation . _Journal_name_full . _Journal_volume . _Journal_issue . _Journal_CSD . _Book_title . _Book_chapter_title . _Book_volume . _Book_series . _Book_publisher . _Book_publisher_city . _Book_ISBN . _Conference_title . _Conference_site . _Conference_state_province . _Conference_country . _Conference_start_date . _Conference_end_date . _Conference_abstract_number . _Thesis_institution . _Thesis_institution_city . _Thesis_institution_country . _Page_first . _Page_last . _Year . _Details . save_ save_Ref._2 _Saveframe_category citation _Citation_full ; 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 . _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID ? _Journal_abbreviation . _Journal_name_full . _Journal_volume . _Journal_issue . _Journal_CSD . _Book_title . _Book_chapter_title . _Book_volume . _Book_series . _Book_publisher . _Book_publisher_city . _Book_ISBN . _Conference_title . _Conference_site . _Conference_state_province . _Conference_country . _Conference_start_date . _Conference_end_date . _Conference_abstract_number . _Thesis_institution . _Thesis_institution_city . _Thesis_institution_country . _Page_first . _Page_last . _Year . _Details . save_ ################################## # Molecular system description # ################################## save_H117G_azurin _Saveframe_category molecular_system _Mol_system_name 'His117Gly azurin' _Abbreviation_common 'H117G azurin' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'His117Gly azurin' $polymer_H117G_azurin CU $CU1 stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state monomer _System_paramagnetic no _System_thiol_state 'disulfide bound and other bound' _Database_query_date . _Details ; The copper ligand residue His117 has been replaced by a Gly in the azurin studied here. ; save_ ######################## # Monomeric polymers # ######################## save_polymer_H117G_azurin _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'P. Aeruginosa HIs117Gly azurin' _Name_variant His117Gly _Abbreviation_common 'H117G azurin' _Molecular_mass . _Mol_thiol_state 'disulfide bound and other bound' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 128 _Mol_residue_sequence ; AECSVDIQGNDQMQFNTNAI TVDKSCKQFTVNLSHPGNLP KNVMGHNWVLSTAADMQGVV TDGMASGLDKDYLKPDDSRV IAHTKLIGSGEKDSVTFDVS KLKEGEQYMFFCTFPGGSAL MKGTLTLK ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 1 ALA 2 2 GLU 3 3 CYS 4 4 SER 5 5 VAL 6 6 ASP 7 7 ILE 8 8 GLN 9 9 GLY 10 10 ASN 11 11 ASP 12 12 GLN 13 13 MET 14 14 GLN 15 15 PHE 16 16 ASN 17 17 THR 18 18 ASN 19 19 ALA 20 20 ILE 21 21 THR 22 22 VAL 23 23 ASP 24 24 LYS 25 25 SER 26 26 CYS 27 27 LYS 28 28 GLN 29 29 PHE 30 30 THR 31 31 VAL 32 32 ASN 33 33 LEU 34 34 SER 35 35 HIS 36 36 PRO 37 37 GLY 38 38 ASN 39 39 LEU 40 40 PRO 41 41 LYS 42 42 ASN 43 43 VAL 44 44 MET 45 45 GLY 46 46 HIS 47 47 ASN 48 48 TRP 49 49 VAL 50 50 LEU 51 51 SER 52 52 THR 53 53 ALA 54 54 ALA 55 55 ASP 56 56 MET 57 57 GLN 58 58 GLY 59 59 VAL 60 60 VAL 61 61 THR 62 62 ASP 63 63 GLY 64 64 MET 65 65 ALA 66 66 SER 67 67 GLY 68 68 LEU 69 69 ASP 70 70 LYS 71 71 ASP 72 72 TYR 73 73 LEU 74 74 LYS 75 75 PRO 76 76 ASP 77 77 ASP 78 78 SER 79 79 ARG 80 80 VAL 81 81 ILE 82 82 ALA 83 83 HIS 84 84 THR 85 85 LYS 86 86 LEU 87 87 ILE 88 88 GLY 89 89 SER 90 90 GLY 91 91 GLU 92 92 LYS 93 93 ASP 94 94 SER 95 95 VAL 96 96 THR 97 97 PHE 98 98 ASP 99 99 VAL 100 100 SER 101 101 LYS 102 102 LEU 103 103 LYS 104 104 GLU 105 105 GLY 106 106 GLU 107 107 GLN 108 108 TYR 109 109 MET 110 110 PHE 111 111 PHE 112 112 CYS 113 113 THR 114 114 PHE 115 115 PRO 116 116 GLY 117 117 GLY 118 118 SER 119 119 ALA 120 120 LEU 121 121 MET 122 122 LYS 123 123 GLY 124 124 THR 125 125 LEU 126 126 THR 127 127 LEU 128 128 LYS stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-08-11 loop_ _Database_name _Database_accession_code _Database_entry_mol_name _Sequence_query_to_submitted_percentage _Sequence_subject_length _Sequence_identity _Sequence_positive _Sequence_homology_expectation_value BMRB 1210 azurin 100.00 128 99.22 99.22 9.22e-88 BMRB 1211 azurin 100.00 128 99.22 99.22 9.22e-88 BMRB 1212 azurin 100.00 128 99.22 99.22 9.22e-88 BMRB 1213 azurin 100.00 128 99.22 99.22 9.22e-88 BMRB 1214 azurin 100.00 128 99.22 99.22 9.22e-88 BMRB 1215 azurin 100.00 128 99.22 99.22 9.22e-88 BMRB 1216 azurin 100.00 128 99.22 99.22 9.22e-88 BMRB 1217 azurin 100.00 128 99.22 99.22 9.22e-88 BMRB 1218 azurin 100.00 128 99.22 99.22 9.22e-88 BMRB 1219 azurin 100.00 128 99.22 99.22 9.22e-88 BMRB 18254 apo-azurin 100.00 128 99.22 99.22 9.22e-88 PDB 1AG0 "Structure Of Cys 112 Asp Azurin From Pseudomonas Aeruginosa" 100.00 129 98.44 98.44 5.07e-86 PDB 1AZN "Crystal Structure Of The Azurin Mutant Phe114ala From Pseudomonas Aeruginosa At 2.6 Angstroms Resolution" 100.00 128 98.44 98.44 1.34e-86 PDB 1AZR "Crystal Structure Of Pseudomonas Aeruginosa Zinc Azurin Mutant Asp47asp At 2.4 Angstroms Resolution" 100.00 128 97.66 99.22 1.86e-86 PDB 1AZU "Structural Features Of Azurin At 2.7 Angstroms Resolution" 100.00 128 99.22 99.22 9.22e-88 PDB 1BEX "Structure Of Ruthenium-modified Pseudomonas Aeruginosa Azurin" 100.00 128 99.22 99.22 9.22e-88 PDB 1E5Y "Azurin From Pseudomonas Aeruginosa, Reduced Form, Ph 5.5" 100.00 128 99.22 99.22 9.22e-88 PDB 1E5Z "Azurin From Pseudomonas Aeruginosa, Reduced Form, Ph 9.0" 100.00 128 99.22 99.22 9.22e-88 PDB 1E65 "Azurin From Pseudomonas Aeruginosa, Apo Form" 100.00 128 99.22 99.22 9.22e-88 PDB 1E67 "Zn-azurin From Pseudomonas Aeruginosa" 100.00 128 99.22 99.22 9.22e-88 PDB 1ETJ "Azurin Mutant With Met 121 Replaced By Glu" 100.00 128 98.44 98.44 1.23e-86 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 9.05e-86 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 8.84e-87 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 1.68e-86 PDB 1JVL "Azurin Dimer, Covalently Crosslinked Through Bis- Maleimidomethylether" 100.00 128 98.44 98.44 2.88e-86 PDB 1JVO "Azurin Dimer, Crosslinked Via Disulfide Bridge" 100.00 128 98.44 98.44 2.88e-86 PDB 1JZE "Pseudomonas Aeruginosa Azurin Ru(Bpy)2(Im)(His83)" 100.00 128 99.22 99.22 9.22e-88 PDB 1JZF "Pseudomonas Aeruginosa Oxidized Azurin(Cu2+) Ru(Tpy)(Phen) (His83)" 100.00 128 99.22 99.22 9.22e-88 PDB 1JZG "Pseudomonas Aeruginosa Reduced Azurin (Cu1+) Ru(Tpy)(Phen) (His83)" 100.00 128 99.22 99.22 9.22e-88 PDB 1JZH "Pseudomonas Aeruginosa Azurin Ru(tpy)(bpy)(his83)" 100.00 128 99.22 99.22 9.22e-88 PDB 1JZI "Pseudomonas Aeruginosa Azurin Re(Phen)(Co)3(His83)" 100.00 128 99.22 99.22 9.22e-88 PDB 1JZJ "Pseudomonas Aeruginosa Azurin Os(Bpy)2(Im)(His83)" 100.00 128 99.22 99.22 9.22e-88 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 1.86e-85 PDB 1VLX "Structure Of Electron Transfer (cobalt-protein)" 100.00 128 99.22 99.22 9.22e-88 PDB 1XB6 "The K24r Mutant Of Pseudomonas Aeruginosa Azurin" 100.00 128 98.44 99.22 1.61e-87 PDB 1XB8 "Zn Substituted Form Of D62cK74C DOUBLE MUTANT OF PSEUDOMONAS Aeruginosa Azurin" 100.00 128 97.66 97.66 4.86e-85 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 1.37e-85 PDB 2GHZ "Crystal Structure Of Azurin Phe114pro Mutant" 100.00 128 98.44 98.44 3.35e-86 PDB 2GI0 "Crystal Structure Of Cu(I) Phe114pro Azurin Mutant" 100.00 128 98.44 98.44 3.35e-86 PDB 2IDF "P. Aeruginosa Azurin N42c/m64e Double Mutant, Bmme-linked Dimer" 100.00 128 97.66 97.66 3.25e-85 PDB 2IWE "Structure Of A Cavity Mutant (H117g) Of Pseudomonas Aeruginosa Azurin" 100.00 128 100.00 100.00 7.73e-89 PDB 2OJ1 "Disulfide-Linked Dimer Of Azurin N42cM64E DOUBLE MUTANT" 100.00 128 97.66 97.66 3.25e-85 PDB 2TSA "Azurin Mutant M121a" 100.00 128 98.44 98.44 7.67e-87 PDB 2TSB "Azurin Mutant M121a-Azide" 100.00 128 98.44 98.44 7.67e-87 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 4.75e-86 PDB 3FPY "Azurin C112dM121L" 100.00 128 97.66 98.44 1.51e-85 PDB 3FQ1 "Azurin C112dM121I" 100.00 128 97.66 98.44 2.19e-85 PDB 3FQ2 "Azurin C112dM121F" 100.00 128 97.66 97.66 3.70e-85 PDB 3FQY "Azurin C112d" 100.00 128 98.44 98.44 4.91e-86 PDB 3IN0 "Crystal Structure Of The F114pM121Q VARIANT OF PSEUDOMONAS Aeruginosa Azurin In The Cu(Ii) State" 100.00 128 97.66 97.66 2.82e-85 PDB 3IN2 "Crystal Structure Of The N47sM121L VARIANT OF PSEUDOMONAS Aeruginosa Azurin In The Cu(Ii) State" 100.00 128 97.66 99.22 1.76e-86 PDB 3JT2 "Cu(Ii) N47sM121L VARIANT OF PSEUDOMONAS AERUGINOSA AZURIN" 100.00 128 97.66 99.22 1.76e-86 PDB 3JTB "Cu(Ii) N47sF114N VARIANT OF PSEUDOMONAS AERUGINOSA AZURIN" 100.00 128 97.66 98.44 1.39e-85 PDB 3N2J "Azurin H117g, Oxidized Form" 100.00 128 100.00 100.00 7.73e-89 PDB 3NP3 "C112dM121E PSEUDOMONAS AERUGINOSA AZURIN" 100.00 128 97.66 97.66 7.05e-85 PDB 3NP4 "C112dM121E PSEUDOMONAS AERUGINOSA AZURIN" 100.00 128 97.66 97.66 7.05e-85 PDB 3OQR "C112dM121E AZURIN, PH 10.0" 100.00 128 97.66 97.66 7.05e-85 PDB 3UGE "Silver Metallated Pseudomonas Aeruginosa Azurin At 1.70 A" 100.00 128 99.22 99.22 9.22e-88 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 9.22e-88 PDB 4BWW "Crystal Structure Of Spin Labelled Azurin T21r1" 100.00 131 98.44 98.44 6.10e-87 PDB 4HZ1 "Crystal Structure Of Pseudomonas Aeruginosa Azurin With Iron(Ii) At The Copper-Binding Site." 100.00 128 99.22 99.22 9.22e-88 PDB 4JKN "Mercury Metallated Pseudomonas Aeruginosa Azurin At 1.54 A" 100.00 128 99.22 99.22 9.22e-88 PDB 4KO9 "Investigating The Functional Significance Of The Interlocked Pair Structural Determinants In Pseudomonas Aeruginosa Azurin (v95" 100.00 128 97.66 99.22 6.51e-87 PDB 4KOB "Investigating The Functional Significance Of The Interlocked Pair Structural Determinants In Pseudomonas Aeruginosa Azurin (v31" 100.00 128 97.66 99.22 1.88e-87 PDB 4MFH "Crystal Structure Of M121g Azurin" 100.00 128 98.44 98.44 2.81e-86 PDB 4QKT "Azurin Mutant M121em44k With Copper" 100.00 128 97.66 97.66 1.19e-85 PDB 4QLW "Azurin Mutant M121e With Iron" 100.00 128 98.44 98.44 1.23e-86 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 9.22e-88 DBJ BAK87490 "azurin precursor [Pseudomonas aeruginosa NCGM2.S1]" 100.00 148 99.22 99.22 2.09e-88 DBJ BAP24727 "azurin precursor [Pseudomonas aeruginosa]" 100.00 148 99.22 99.22 2.09e-88 DBJ BAP53499 "azurin precursor [Pseudomonas aeruginosa]" 100.00 148 99.22 99.22 2.09e-88 DBJ BAQ42761 "azurin precursor [Pseudomonas aeruginosa]" 100.00 148 99.22 99.22 2.09e-88 DBJ BAR70381 "azurin [Pseudomonas aeruginosa]" 100.00 148 99.22 99.22 2.09e-88 EMBL CAA30279 "unnamed protein product [Pseudomonas aeruginosa]" 100.00 148 99.22 99.22 2.09e-88 EMBL CAW30062 "azurin precursor [Pseudomonas aeruginosa LESB58]" 100.00 148 99.22 99.22 2.09e-88 EMBL CCQ86145 "azurin precursor [Pseudomonas aeruginosa 18A]" 100.00 148 99.22 99.22 2.09e-88 EMBL CDH73668 "Azurin [Pseudomonas aeruginosa MH38]" 100.00 148 99.22 99.22 2.09e-88 EMBL CDH79986 "Azurin [Pseudomonas aeruginosa MH27]" 100.00 148 99.22 99.22 2.09e-88 GB AAA25730 "azurin [Pseudomonas aeruginosa]" 100.00 148 99.22 99.22 2.09e-88 GB AAG08307 "azurin precursor [Pseudomonas aeruginosa PAO1]" 100.00 148 99.22 99.22 2.09e-88 GB AAP03090 "azurin [Burkholderia cepacia]" 100.00 148 97.66 98.44 5.79e-86 GB AAT49489 "PA4922, partial [synthetic construct]" 100.00 149 98.44 98.44 3.70e-87 GB ABJ14307 "azurin precursor [Pseudomonas aeruginosa UCBPP-PA14]" 100.00 148 98.44 99.22 6.81e-88 PRF 671048A azurin 100.00 128 99.22 99.22 9.22e-88 REF NP_253609 "azurin [Pseudomonas aeruginosa PAO1]" 100.00 148 99.22 99.22 2.09e-88 REF WP_003095591 "MULTISPECIES: azurin [Pseudomonas]" 100.00 148 99.22 99.22 2.09e-88 REF WP_003141697 "azurin [Pseudomonas aeruginosa]" 100.00 148 98.44 99.22 6.81e-88 REF WP_031690945 "azurin [Pseudomonas aeruginosa]" 100.00 148 98.44 99.22 4.91e-88 REF WP_033949908 "azurin [Pseudomonas aeruginosa]" 100.00 148 99.22 99.22 2.14e-88 SP B3EWN9 "RecName: Full=Azurin" 100.00 128 98.44 98.44 1.68e-86 SP P00282 "RecName: Full=Azurin; Flags: Precursor" 100.00 148 99.22 99.22 2.09e-88 stop_ save_ ############# # Ligands # ############# save_CU1 _Saveframe_category ligand _Mol_type non-polymer _Name_common "CU1 (COPPER (I) ION)" _BMRB_code . _PDB_code CU1 _Molecular_mass 63.546 _Mol_charge 1 _Mol_paramagnetic . _Mol_aromatic no _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 ; loop_ _Atom_name _PDB_atom_name _Atom_type _Atom_chirality _Atom_charge _Atom_oxidation_number _Atom_unpaired_electrons CU CU CU . 1 . ? stop_ _Mol_thiol_state . _Sequence_homology_query_date . save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species _Fraction $polymer_H117G_azurin 'fluorescent pseudomonads' 287 Eubacteria . Pseudomonas aeruginosa periplasm stop_ save_ ######################### # Experimental source # ######################### save_experimental_source _Saveframe_category experimental_source loop_ _Mol_label _Production_method _Host_organism_name_common _Genus _Species _Strain _Vector_name $polymer_H117G_azurin 'recombinant technology' . . . . . stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_Typical_Sample _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Concentration_min_value _Concentration_max_value _Isotopic_labeling $polymer_H117G_azurin . mM 3 5 [U-15N] stop_ save_ ############################ # Computer software used # ############################ save_azara _Saveframe_category software _Name azara _Version . loop_ _Task 'FID processing' stop_ _Details . _Citation_label $Ref._1 save_ save_ANSIG _Saveframe_category software _Name ANSIG _Version 3.3 loop_ _Task 'peak assignments and peak integration' stop_ _Details . _Citation_label $Ref._2 save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model 'Avance DMX' _Field_strength 600 _Details . save_ ############################# # NMR applied experiments # ############################# save_1H-15N_HSQC_1 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-15N HSQC' _Sample_label $Typical_Sample save_ save_1H-15N_TROSY_2 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-15N TROSY' _Sample_label $Typical_Sample save_ save_1H-15N_TOCSY_3 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-15N TOCSY' _Sample_label $Typical_Sample save_ save_1H-1H_TOCSY_4 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-1H TOCSY' _Sample_label $Typical_Sample save_ save_1H-15N_NOESY_5 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-15N NOESY' _Sample_label $Typical_Sample save_ save_1H-1H_NOESY_6 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-1H NOESY' _Sample_label $Typical_Sample save_ save_NMR_spec_expt__0_1 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-15N HSQC' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_2 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-15N TROSY' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_3 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-15N TOCSY' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_4 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-1H TOCSY' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_5 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-15N NOESY' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_6 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-1H NOESY' _BMRB_pulse_sequence_accession_number . _Details . save_ ####################### # Sample conditions # ####################### save_Typical_Sample_Conditions _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 5.5 0.2 n/a temperature 313 2 K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference _Saveframe_category chemical_shift_reference _Details . loop_ _Mol_common_name _Atom_type _Atom_isotope_number _Atom_group _Chem_shift_units _Chem_shift_value _Reference_method _Reference_type _External_reference_sample_geometry _External_reference_location _External_reference_axis _Indirect_shift_ratio DSS H 1 'methyl protons' ppm 0.0 internal direct . . . 1.0 DSS N 15 'methyl protons' ppm 0.0 . indirect . . . 0.101329118 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 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Experiment_label '1H-15N HSQC' '1H-15N TROSY' '1H-15N TOCSY' '1H-1H TOCSY' '1H-15N NOESY' '1H-1H NOESY' stop_ loop_ _Sample_label $Typical_Sample stop_ _Sample_conditions_label $Typical_Sample_Conditions _Chem_shift_reference_set_label $chemical_shift_reference _Mol_system_component_name 'His117Gly azurin' _Text_data_format . _Text_data . loop_ _Atom_shift_assign_ID _Residue_author_seq_code _Residue_seq_code _Residue_label _Atom_name _Atom_type _Chem_shift_value _Chem_shift_value_error _Chem_shift_ambiguity_code 1 . 2 GLU H H 8.88 0.02 1 2 . 2 GLU HA H 4.48 0.02 1 3 . 2 GLU N N 124.9 0.2 1 4 . 3 CYS H H 8.7 0.02 1 5 . 3 CYS HA H 5.03 0.02 1 6 . 3 CYS N N 120.4 0.2 1 7 . 4 SER H H 7.23 0.02 1 8 . 4 SER HA H 4.65 0.02 1 9 . 4 SER N N 113.1 0.2 1 10 . 5 VAL H H 8.06 0.02 1 11 . 5 VAL HA H 4.42 0.02 1 12 . 5 VAL N N 118.9 0.2 1 13 . 6 ASP H H 8.1 0.02 1 14 . 6 ASP HA H 5.27 0.02 1 15 . 6 ASP N N 126.4 0.2 1 16 . 7 ILE H H 8.97 0.02 1 17 . 7 ILE HA H 4.78 0.02 1 18 . 7 ILE N N 124.1 0.2 1 19 . 8 GLN H H 8.33 0.02 1 20 . 8 GLN HA H 5.26 0.02 1 21 . 8 GLN N N 123.6 0.2 1 22 . 9 GLY H H 8.47 0.02 1 23 . 9 GLY HA2 H 4.99 0.02 1 24 . 9 GLY HA3 H 2.46 0.02 1 25 . 9 GLY N N 108 0.2 1 26 . 10 ASN H H 7.56 0.02 1 27 . 10 ASN HA H 5.15 0.02 1 28 . 10 ASN N N 122.4 0.2 1 29 . 11 ASP H H 8.38 0.02 1 30 . 11 ASP HA H 5.15 0.02 1 31 . 11 ASP N N 119.5 0.2 1 32 . 12 GLN H H 7.70 0.02 1 33 . 12 GLN HA H 4.49 0.02 1 34 . 12 GLN N N 117.2 0.2 1 35 . 13 MET H H 7.56 0.02 1 36 . 13 MET HA H 3.96 0.02 1 37 . 13 MET N N 114.2 0.2 1 38 . 14 GLN H H 6.96 0.02 1 39 . 14 GLN N N 111.5 0.2 1 40 . 15 PHE H H 8.93 0.02 1 41 . 15 PHE HA H 6.09 0.02 1 42 . 15 PHE N N 121.7 0.2 1 43 . 16 ASN H H 8.76 0.02 1 44 . 16 ASN HA H 4.68 0.02 1 45 . 16 ASN N N 116.6 0.2 1 46 . 17 THR H H 7.18 0.02 1 47 . 17 THR HA H 4.77 0.02 1 48 . 17 THR N N 112.4 0.2 1 49 . 18 ASN H H 8.43 0.02 1 50 . 18 ASN HA H 5.14 0.02 1 51 . 18 ASN N N 121.5 0.2 1 52 . 19 ALA H H 8.28 0.02 1 53 . 19 ALA HA H 5.51 0.02 1 54 . 19 ALA N N 123.9 0.2 1 55 . 20 ILE H H 8.98 0.02 1 56 . 20 ILE HA H 4.47 0.02 1 57 . 20 ILE N N 122.5 0.2 1 58 . 21 THR H H 8.71 0.02 1 59 . 21 THR HA H 4.95 0.02 1 60 . 21 THR N N 124.1 0.2 1 61 . 22 VAL H H 8.88 0.02 1 62 . 22 VAL HA H 3.64 0.02 1 63 . 22 VAL N N 128.0 0.2 1 64 . 23 ASP H H 8.12 0.02 1 65 . 23 ASP HA H 4.77 0.02 1 66 . 23 ASP N N 128.1 0.2 1 67 . 24 LYS H H 8.89 0.02 1 68 . 24 LYS HA H 3.94 0.02 1 69 . 24 LYS N N 126.1 0.2 1 70 . 25 SER H H 8.98 0.02 1 71 . 25 SER HA H 4.30 0.02 1 72 . 25 SER N N 115.1 0.2 1 73 . 26 CYS H H 8.28 0.02 1 74 . 26 CYS HA H 4.48 0.02 1 75 . 26 CYS N N 122.7 0.2 1 76 . 27 LYS H H 8.70 0.02 1 77 . 27 LYS HA H 4.26 0.02 1 78 . 27 LYS N N 122.6 0.2 1 79 . 28 GLN H H 7.78 0.02 1 80 . 28 GLN HA H 4.99 0.02 1 81 . 28 GLN N N 116.3 0.2 1 82 . 29 PHE H H 8.40 0.02 1 83 . 29 PHE HA H 4.88 0.02 1 84 . 29 PHE N N 121.8 0.2 1 85 . 30 THR H H 7.06 0.02 1 86 . 30 THR HA H 5.07 0.02 1 87 . 30 THR N N 122.8 0.2 1 88 . 31 VAL H H 8.62 0.02 1 89 . 31 VAL HA H 3.86 0.02 1 90 . 31 VAL N N 125.8 0.2 1 91 . 32 ASN H H 8.37 0.02 1 92 . 32 ASN HA H 5.00 0.02 1 93 . 32 ASN N N 125.0 0.2 1 94 . 33 LEU H H 9.12 0.02 1 95 . 33 LEU HA H 5.38 0.02 1 96 . 33 LEU N N 128.2 0.2 1 97 . 34 SER H H 8.66 0.02 1 98 . 34 SER HA H 5.08 0.02 1 99 . 34 SER N N 119.3 0.2 1 100 . 35 HIS H H 8.62 0.02 1 101 . 35 HIS HA H 6.43 0.02 1 102 . 35 HIS N N 118.6 0.2 1 103 . 37 GLY H H 8.62 0.02 1 104 . 37 GLY N N 110.7 0.2 1 105 . 38 ASN H H 11.46 0.02 1 106 . 38 ASN HA H 4.97 0.02 1 107 . 38 ASN N N 119.9 0.2 1 108 . 39 LEU H H 8.60 0.02 1 109 . 39 LEU N N 123.4 0.2 1 110 . 41 LYS H H 8.93 0.02 1 111 . 41 LYS HA H 3.46 0.02 1 112 . 41 LYS N N 119.2 0.2 1 113 . 42 ASN H H 8.11 0.02 1 114 . 42 ASN HA H 4.69 0.02 1 115 . 42 ASN N N 108.6 0.2 1 116 . 43 VAL H H 7.31 0.02 1 117 . 43 VAL HA H 4.25 0.02 1 118 . 43 VAL N N 118.9 0.2 1 119 . 44 MET H H 7.82 0.02 1 120 . 44 MET HA H 3.72 0.02 1 121 . 44 MET N N 118.9 0.2 1 122 . 45 GLY H H 5.05 0.02 1 123 . 45 GLY HA2 H 4.14 0.02 1 124 . 45 GLY HA3 H 2.94 0.02 1 125 . 45 GLY N N 114.7 0.2 1 126 . 46 HIS H H 8.21 0.02 1 127 . 46 HIS HA H 6.72 0.02 1 128 . 46 HIS N N 110.5 0.2 1 129 . 47 ASN H H 9.48 0.02 1 130 . 47 ASN HA H 4.71 0.02 1 131 . 47 ASN N N 122.4 0.2 1 132 . 48 TRP H H 7.47 0.02 1 133 . 48 TRP N N 114.6 0.2 1 134 . 49 VAL H H 8.24 0.02 1 135 . 49 VAL HA H 4.00 0.02 1 136 . 49 VAL N N 129.2 0.2 1 137 . 50 LEU H H 7.57 0.02 1 138 . 50 LEU HA H 4.87 0.02 1 139 . 50 LEU N N 124.2 0.2 1 140 . 51 SER H H 9.13 0.02 1 141 . 51 SER HA H 5.03 0.02 1 142 . 51 SER N N 122.3 0.2 1 143 . 52 THR H H 9.84 0.02 1 144 . 52 THR HA H 4.79 0.02 1 145 . 52 THR N N 111.5 0.2 1 146 . 53 ALA H H 8.91 0.02 1 147 . 53 ALA HA H 3.89 0.02 1 148 . 53 ALA N N 125.7 0.2 1 149 . 54 ALA H H 8.27 0.02 1 150 . 54 ALA HA H 4.09 0.02 1 151 . 54 ALA N N 118.4 0.2 1 152 . 55 ASP H H 7.31 0.02 1 153 . 55 ASP HA H 4.74 0.02 1 154 . 55 ASP N N 115.9 0.2 1 155 . 56 MET H H 7.01 0.02 1 156 . 56 MET HA H 3.55 0.02 1 157 . 56 MET N N 120.1 0.2 1 158 . 57 GLN H H 8.56 0.02 1 159 . 57 GLN HA H 3.72 0.02 1 160 . 57 GLN N N 115.9 0.2 1 161 . 58 GLY H H 8.37 0.02 1 162 . 58 GLY HA2 H 3.80 0.02 1 163 . 58 GLY HA3 H 3.76 0.02 1 164 . 58 GLY N N 109.5 0.2 1 165 . 59 VAL H H 7.87 0.02 1 166 . 59 VAL HA H 3.61 0.02 1 167 . 59 VAL N N 122.0 0.2 1 168 . 60 VAL H H 8.43 0.02 1 169 . 60 VAL HA H 3.59 0.02 1 170 . 60 VAL N N 120.0 0.2 1 171 . 61 THR H H 8.48 0.02 1 172 . 61 THR HA H 3.89 0.02 1 173 . 61 THR N N 117.1 0.2 1 174 . 62 ASP H H 8.42 0.02 1 175 . 62 ASP N N 121.6 0.2 1 176 . 63 GLY H H 8.69 0.02 1 177 . 63 GLY HA2 H 4.13 0.02 1 178 . 63 GLY HA3 H 3.55 0.02 1 179 . 63 GLY N N 113.7 0.2 1 180 . 64 MET H H 8.50 0.02 1 181 . 64 MET HA H 4.15 0.02 1 182 . 64 MET N N 121.9 0.2 1 183 . 65 ALA H H 7.10 0.02 1 184 . 65 ALA HA H 4.24 0.02 1 185 . 65 ALA N N 117.5 0.2 1 186 . 66 SER H H 7.71 0.02 1 187 . 66 SER HA H 4.28 0.02 1 188 . 66 SER N N 114.9 0.2 1 189 . 67 GLY H H 6.76 0.02 1 190 . 67 GLY HA2 H 4.20 0.02 1 191 . 67 GLY HA3 H 3.59 0.02 1 192 . 67 GLY N N 102.7 0.2 1 193 . 68 LEU H H 7.98 0.02 1 194 . 68 LEU HA H 3.00 0.02 1 195 . 68 LEU N N 122.1 0.2 1 196 . 69 ASP H H 8.54 0.02 1 197 . 69 ASP HA H 4.35 0.02 1 198 . 69 ASP N N 116.8 0.2 1 199 . 70 LYS H H 6.89 0.02 1 200 . 70 LYS HA H 4.50 0.02 1 201 . 70 LYS N N 118.7 0.2 1 202 . 71 ASP H H 8.02 0.02 1 203 . 71 ASP HA H 3.99 0.02 1 204 . 71 ASP N N 115.5 0.2 1 205 . 72 TYR H H 7.70 0.02 1 206 . 72 TYR HA H 3.65 0.02 1 207 . 72 TYR N N 105.4 0.2 1 208 . 73 LEU H H 7.10 0.02 1 209 . 73 LEU N N 117.4 0.2 1 210 . 74 LYS H H 8.85 0.02 1 211 . 74 LYS HA H 4.69 0.02 1 212 . 74 LYS N N 126.8 0.2 1 213 . 75 PRO HA H 4.22 0.02 1 214 . 76 ASP H H 8.68 0.02 1 215 . 76 ASP HA H 4.28 0.02 1 216 . 76 ASP N N 118.5 0.2 1 217 . 77 ASP H H 7.30 0.02 1 218 . 77 ASP HA H 4.29 0.02 1 219 . 77 ASP N N 117.5 0.2 1 220 . 78 SER H H 8.59 0.02 1 221 . 78 SER HA H 4.28 0.02 1 222 . 78 SER N N 124.9 0.2 1 223 . 79 ARG H H 8.56 0.02 1 224 . 79 ARG HA H 4.16 0.02 1 225 . 79 ARG N N 119.8 0.2 1 226 . 80 VAL H H 7.33 0.02 1 227 . 80 VAL HA H 3.90 0.02 1 228 . 80 VAL N N 118.3 0.2 1 229 . 81 ILE H H 8.88 0.02 1 230 . 81 ILE HA H 3.72 0.02 1 231 . 81 ILE N N 131.7 0.2 1 232 . 82 ALA H H 7.19 0.02 1 233 . 82 ALA HA H 4.69 0.02 1 234 . 82 ALA N N 116.5 0.2 1 235 . 83 HIS H H 8.59 0.02 1 236 . 83 HIS HA H 6.15 0.02 1 237 . 83 HIS N N 113.1 0.2 1 238 . 84 THR H H 8.79 0.02 1 239 . 84 THR HA H 4.80 0.02 1 240 . 84 THR N N 110.1 0.2 1 241 . 85 LYS H H 9.32 0.02 1 242 . 85 LYS HA H 4.69 0.02 1 243 . 85 LYS N N 121.5 0.2 1 244 . 86 LEU H H 8.05 0.02 1 245 . 86 LEU HA H 4.70 0.02 1 246 . 86 LEU N N 120.6 0.2 1 247 . 87 ILE H H 9.43 0.02 1 248 . 87 ILE HA H 4.88 0.02 1 249 . 87 ILE N N 120.8 0.2 1 250 . 88 GLY H H 9.31 0.02 1 251 . 88 GLY HA2 H 4.12 0.02 1 252 . 88 GLY HA3 H 3.57 0.02 1 253 . 88 GLY N N 110.9 0.2 1 254 . 89 SER H H 6.87 0.02 1 255 . 89 SER N N 111.3 0.2 1 256 . 90 GLY H H 8.39 0.02 1 257 . 90 GLY N N 111.4 0.2 1 258 . 91 GLU H H 7.64 0.02 1 259 . 91 GLU N N 119.0 0.2 1 260 . 92 LYS H H 8.19 0.02 1 261 . 92 LYS HA H 5.22 0.02 1 262 . 92 LYS N N 117.0 0.2 1 263 . 93 ASP H H 8.96 0.02 1 264 . 93 ASP HA H 5.10 0.02 1 265 . 93 ASP N N 118.0 0.2 1 266 . 94 SER H H 8.03 0.02 1 267 . 94 SER HA H 5.70 0.02 1 268 . 94 SER N N 116.2 0.2 1 269 . 95 VAL H H 8.65 0.02 1 270 . 95 VAL HA H 4.69 0.02 1 271 . 95 VAL N N 121.8 0.2 1 272 . 96 THR H H 8.40 0.02 1 273 . 96 THR HA H 5.37 0.02 1 274 . 96 THR N N 124.7 0.2 1 275 . 97 PHE H H 8.78 0.02 1 276 . 97 PHE HA H 5.28 0.02 1 277 . 97 PHE N N 122.5 0.2 1 278 . 98 ASP H H 8.54 0.02 1 279 . 98 ASP HA H 4.74 0.02 1 280 . 98 ASP N N 120.6 0.2 1 281 . 99 VAL H H 7.88 0.02 1 282 . 99 VAL HA H 3.46 0.02 1 283 . 99 VAL N N 127.2 0.2 1 284 . 100 SER H H 8.61 0.02 1 285 . 100 SER HA H 4.36 0.02 1 286 . 100 SER N N 115.4 0.2 1 287 . 101 LYS H H 7.46 0.02 1 288 . 101 LYS HA H 4.20 0.02 1 289 . 101 LYS N N 119.7 0.2 1 290 . 102 LEU H H 7.91 0.02 1 291 . 102 LEU HA H 4.46 0.02 1 292 . 102 LEU N N 118.4 0.2 1 293 . 103 LYS H H 8.72 0.02 1 294 . 103 LYS HA H 4.68 0.02 1 295 . 103 LYS N N 120.7 0.2 1 296 . 104 GLU H H 8.83 0.02 1 297 . 104 GLU HA H 4.16 0.02 1 298 . 104 GLU N N 124.7 0.2 1 299 . 105 GLY H H 8.90 0.02 1 300 . 105 GLY HA2 H 4.24 0.02 1 301 . 105 GLY HA3 H 3.80 0.02 1 302 . 105 GLY N N 112.4 0.2 1 303 . 106 GLU H H 7.20 0.02 1 304 . 106 GLU HA H 4.48 0.02 1 305 . 106 GLU N N 120.5 0.2 1 306 . 107 GLN H H 9.16 0.02 1 307 . 107 GLN HA H 4.66 0.02 1 308 . 107 GLN N N 124.5 0.2 1 309 . 108 TYR H H 8.63 0.02 1 310 . 108 TYR HA H 4.91 0.02 1 311 . 108 TYR N N 123.9 0.2 1 312 . 109 MET H H 8.99 0.02 1 313 . 109 MET HA H 5.53 0.02 1 314 . 109 MET N N 120.3 0.2 1 315 . 110 PHE H H 8.48 0.02 1 316 . 110 PHE HA H 6.00 0.02 1 317 . 110 PHE N N 117.2 0.2 1 318 . 111 PHE H H 8.11 0.02 1 319 . 111 PHE HA H 5.47 0.02 1 320 . 111 PHE N N 115.4 0.2 1 321 . 112 CYS H H 7.24 0.02 1 322 . 112 CYS HA H 5.64 0.02 1 323 . 112 CYS N N 121.3 0.2 1 324 . 113 THR H H 9.91 0.02 1 325 . 113 THR N N 118.0 0.2 1 326 . 114 PHE H H 9.49 0.02 1 327 . 114 PHE HA H 3.70 0.02 1 328 . 114 PHE N N 128.8 0.2 1 329 . 116 GLY H H 8.81 0.02 1 330 . 116 GLY HA2 H 4.12 0.02 1 331 . 116 GLY N N 109.8 0.2 1 332 . 117 GLY H H 8.12 0.02 1 333 . 117 GLY HA2 H 4.21 0.02 1 334 . 117 GLY HA3 H 3.86 0.02 1 335 . 117 GLY N N 111.6 0.2 1 336 . 118 SER H H 8.40 0.02 1 337 . 118 SER HA H 4.32 0.02 1 338 . 118 SER N N 115.9 0.2 1 339 . 119 ALA H H 7.64 0.02 1 340 . 119 ALA HA H 4.26 0.02 1 341 . 119 ALA N N 122.3 0.2 1 342 . 120 LEU H H 7.66 0.02 1 343 . 120 LEU N N 116.9 0.2 1 344 . 121 MET H H 8.94 0.02 1 345 . 121 MET HA H 4.44 0.02 1 346 . 121 MET N N 123.8 0.2 1 347 . 122 LYS H H 7.52 0.02 1 348 . 122 LYS HA H 5.58 0.02 1 349 . 122 LYS N N 117.1 0.2 1 350 . 123 GLY H H 8.38 0.02 1 351 . 123 GLY HA2 H 4.13 0.02 1 352 . 123 GLY HA3 H 3.08 0.02 1 353 . 123 GLY N N 109.7 0.2 1 354 . 124 THR H H 7.86 0.02 1 355 . 124 THR HA H 5.15 0.02 1 356 . 124 THR N N 109.6 0.2 1 357 . 125 LEU H H 8.07 0.02 1 358 . 125 LEU HA H 5.68 0.02 1 359 . 125 LEU N N 125.3 0.2 1 360 . 126 THR H H 8.44 0.02 1 361 . 126 THR HA H 4.87 0.02 1 362 . 126 THR N N 120.2 0.2 1 363 . 127 LEU H H 8.76 0.02 1 364 . 127 LEU HA H 5.15 0.02 1 365 . 127 LEU N N 127.2 0.2 1 366 . 128 LYS H H 8.55 0.02 1 367 . 128 LYS HA H 4.33 0.02 1 368 . 128 LYS N N 130.2 0.2 1 stop_ save_