data_4465 #Corrected using PDB structure: 1JVOJ # #N.B. (Observed* = Observed shift + Offset correction) # #After reference correction, the following residues still #have a HA chemical shift difference (obs*-pred) greater than 0.7ppm: #NUM AA CS Observed* Predicted # 3 C HA 4.99 4.11 # 13 M HA 3.92 2.99 # 35 H HA 6.39 4.95 # 44 M HA 3.68 4.40 # 46 H HA 6.68 5.51 # 47 N HA 4.67 5.54 #110 F HA 5.96 5.06 # #After reference correction, the following residues still #have a N chemical shift difference (obs*-pred) greater than 10.0ppm: #NUM AA CS Observed* Predicted # 45 G N 114.42 104.00 # 48 W N 114.32 128.77 # #After reference correction, the following residues still #have a HN chemical shift difference (obs*-pred) greater than 2.0ppm: #NUM AA CS Observed* Predicted #112 C H 7.26 9.30 # #The average CS difference between predicted and observed: #HA CA CB CO N HN #-0.04 N/A N/A N/A -0.28 0.02 # #bmr4465.str.corr chemical shifts have been re-referenced with the following #offsets (these values have been added to the original bmr4465.str file): #HA CA CB CO N HN #N/A N/A N/A N/A -0.28 N/A # #The 95% confidence intervals for the above recommended offsets are: # HA CA CB CO N HN #+/-0.03 N/A N/A N/A +/-0.27 +/-0.07 # #The Correlation Coefficients between predicted and observed #chemical shifts are: #HA CA CB CO N HN #0.882 N/A N/A N/A 0.846 0.693 # #The RMSD between predicted and observed* (reference #corrected) chemical shifts are: #HA CA CB CO N HN #0.140 N/A N/A N/A 1.485 0.362 # ####################### # 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 ; 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_ _BMRB_accession_number 4465 _BMRB_flat_file_name bmr4465.str _Entry_type new _Submission_date 1999-11-24 _Accession_date 1999-11-26 _Entry_origination author _NMR_STAR_version 2.1.1 _Experimental_method NMR 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_ 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 _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 _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_ ################################## # 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_physical_state native _System_oligomer_state monomer _System_paramagnetic no _System_thiol_state 'disulfide bound and other bound' _Details ; The copper ligand residue His117 has been replaced by a Gly in the azurin studied here. ; loop_ _Database_name _Database_accession_code _Database_entry_mol_name _Database_entry_details PDB 1E5Y "A Chain A, Aurin From Pseudomonas Aeruginosa, Reduced Form, Ph 5.5" . PDB 1E5Z "A Chain A, Aurin From Pseudomonas Aeruginosa, Reduced Form, Ph 9.0" . PDB 1E65 "A Chain A, Aurin From Pseudomonas Aeruginosa, Apo Form" . PDB 1E67 "A Chain A, Zn-Azurin From Pseudomonas Aeruginosa" . PDB 1VLX "A Chain A, Structure Of Electron Transfer (Cobalt-Protein)" . PDB 1BEX "A Chain A, Structure Of Ruthenium-Modified Pseudomonas Aeruginosa Azurin" . PDB 1AZU Azurin . PDB 4AZU "A Chain A, Azurin (Ph 5.5)" . PDB 5AZU "A Chain A, Azurin (Ph 9.0)" . PDB 1AZN "A Chain A, Azurin Mutant With Phe 114 Replaced By Ala (F114a)" . PDB 1ILU "A Chain A, Electron Transfer Protein Mol_id: 1; Molecule: Azurin; Chain: A, B, C, D, E, F, G, H, I, K, L, M; Engineered: Yes; Mutation: F110s" . PDB 1ETJ "A Chain A, Azurin Mutant With Met 121 Replaced By Glu" . PDB 1ILS "A Chain A, Electron Transfer Protein Mol_id: 1; Molecule: Azurin; Chain: A, B, C, D; Engineered: Yes; Mutation: I7s" . PDB 2TSB "A Chain A, Azurin Mutant M121a-Azide" . PDB 2TSA "A Chain A, Azurin Mutant M121a" . stop_ 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" _Mol_thiol_state 'disulfide bound and other bound' ############################## # 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 2004-07-29 _Sequence_homology_query_revised_last_date 2004-07-16 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 PDB 1AZU Azurin 100.00 128 99 99 3e-69 PDB 1BEX "A Chain A, Structure Of Ruthenium-ModifiedPseudomonas Aeruginosa Azurin" 100.00 128 99 99 3e-69 PDB 1E5Y "A Chain A, Aurin From Pseudomonas Aeruginosa,Reduced Form, Ph 5.5" 100.00 128 99 99 3e-69 PDB 1E5Z "A Chain A, Aurin From Pseudomonas Aeruginosa,Reduced Form, Ph 9.0" 100.00 128 99 99 3e-69 PDB 1E65 "A Chain A, Aurin From Pseudomonas Aeruginosa,Apo Form" 100.00 128 99 99 3e-69 PDB 1E67 "A Chain A, Zn-Azurin From PseudomonasAeruginosa" 100.00 128 99 99 3e-69 PDB 1JZE "A Chain A, Pseudomonas Aeruginosa AzurinRu(Bpy)2(Im)(His83)" 100.00 128 99 99 3e-69 PDB 1JZF "A Chain A, Pseudomonas Aeruginosa OxidizedAzurin(Cu2+) Ru(Tpy)(Phen) (His83)" 100.00 128 99 99 3e-69 PDB 1JZG "A Chain A, Pseudomonas Aeruginosa ReducedAzurin (Cu1+) Ru(Tpy)(Phen) (His83)" 100.00 128 99 99 3e-69 PDB 1JZH "A Chain A, Pseudomonas Aeruginosa AzurinRu(Tpy)(Bpy)(His83)" 100.00 128 99 99 3e-69 PDB 1JZI "A Chain A, Pseudomonas Aeruginosa AzurinRe(Phen)(Co)3(His83)" 100.00 128 99 99 3e-69 PDB 1JZJ "A Chain A, Pseudomonas Aeruginosa AzurinOs(Bpy)2(Im)(His83)" 100.00 128 99 99 3e-69 PDB 1VLX "A Chain A, Structure Of Electron Transfer(Cobalt-Protein)" 100.00 128 99 99 3e-69 PDB 4AZU "A Chain A, Azurin (Ph 5.5)" 100.00 128 99 99 10e-69 PDB 5AZU "A Chain A, Azurin (Ph 9.0)" 100.00 128 99 99 10e-69 PDB 1AZN "A Chain A, Azurin Mutant With Phe 114 ReplacedBy Ala (F114a)" 100.00 128 98 98 2e-68 PDB 1ETJ "A Chain A, Azurin Mutant With Met 121 ReplacedBy Glu" 100.00 128 98 98 2e-68 PDB 1ILS "A Chain A, Electron Transfer Protein Mol_id: 1;Molecule: Azurin; Chain: A, B, C, D; Engineered: Yes;Mutation: I7s" 100.00 128 98 98 10e-69 PDB 1ILU "A Chain A, Electron Transfer Protein Mol_id: 1;Molecule: Azurin; Chain: A, B, C, D, E, F, G, H, I, K,L, M; Engineered: Yes; Mutation: F110s" 100.00 128 98 98 2e-68 PDB 1JVL "A Chain A, Azurin Dimer, CovalentlyCrosslinked Through Bis- Maleimidomethylether" 100.00 128 98 98 3e-68 PDB 1JVO "A Chain A, Azurin Dimer, Crosslinked ViaDisulfide Bridge" 100.00 128 98 98 3e-68 PDB 1NZR "A Chain A, Azurin Mutant With Trp 48 ReplacedBy Met (W48m)" 100.00 128 98 98 2e-67 PDB 2TSA "A Chain A, Azurin Mutant M121a" 100.00 128 98 98 10e-69 PDB 2TSB "A Chain A, Azurin Mutant M121a-Azide" 100.00 128 98 98 10e-69 PDB 1AZR "A Chain A, Azurin Mutant With Asn 47 Replaced ByAsp (N47D)" 100.00 128 98 99 2e-68 PDB 1EZL "A Chain A, Crystal Structure Of The DisulphideBond-Deficient Azurin Mutant C3aC26A: HOW IMPORTANT ISTHE S-S Bond For Folding And Stability?" 100.00 128 98 98 3e-67 PDB 2AZU "A Chain A, Azurin Mutant With His 35 Replaced ByLeu (H35L)" 100.00 128 98 98 1e-67 PDB 3AZU "A Chain A, Azurin Mutant With His 35 Replaced ByGln (H35Q)" 100.00 128 98 98 5e-68 PDB 1AG0 "A Chain A, Structure Of Cys 112 Asp Azurin FromPseudomonas Aeruginosa" 99.22 129 98 98 6e-68 EMBL CAA30279.1 "unnamed protein product [Pseudomonasaeruginosa]" 86.49 148 99 99 3e-69 GenBank AAA25730.1 "azurin [Pseudomonas aeruginosa]" 86.49 148 99 99 3e-69 GenBank AAG08307.1 "azurin precursor [Pseudomonas aeruginosaPAO1]" 86.49 148 99 99 3e-69 GenBank AAP03090.1 "azurin [Burkholderia cepacia]" 86.49 148 98 98 6e-68 GenBank AAT49489.1 "PA4922 [synthetic construct]" 85.91 149 98 98 10e-69 PIR AZPSCA "azurin precursor [validated] - Pseudomonasaeruginosa" 86.49 148 99 99 3e-69 PRF 671048A azurin 100.00 128 99 99 3e-69 REF NP_253609.1 "azurin precursor [Pseudomonasaeruginosa PA01]" 86.49 148 99 99 3e-69 SWISS-PROT P00282 "AZUR_PSEAE Azurin precursor" 86.49 148 99 99 3e-69 stop_ save_ ############# # Ligands # ############# save_CU1 _Saveframe_category ligand _Mol_type non-polymer _Name_common Cu _Abbreviation_common Cu _Name_IUPAC 'COPPER (I) ION' _PDB_code CU1 _Mol_empirical_formula CU1 _Mol_charge 1+ _Mol_paramagnetic no _Mol_aromatic no _Details . loop_ _Atom_name _PDB_atom_name _Atom_type _Atom_chirality _Atom_charge _Atom_oxidation_number _Atom_unpaired_electrons CU CU CU ? 1 ? ? stop_ save_ ######################################## # Molecular bond linkage definitions # ######################################## save_crosslink_bonds _Saveframe_category crosslink_bonds loop_ _Bond_order _Bond_type _Atom_one_mol_system_component_name _Atom_one_residue_seq_code _Atom_one_atom_name _Atom_two_mol_system_component_name _Atom_two_residue_seq_code _Atom_two_atom_name single disulfide azurin 3 SG azurin 26 SG coordinative . azurin 112 SG CU . CU stop_ loop_ _Deleted_atom_mol_system_component_name _Deleted_atom_residue_seq_code _Deleted_atom_residue_label _Deleted_atom_name azurin 3 CYS HG azurin 26 CYS HG azurin 112 CYS HG stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species _Fraction $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 $H117G_azurin 'recombinant technology' . . . . . stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_Typical_Sample _Saveframe_category sample _Sample_type solution 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 loop_ _Task "FID processing" stop_ _Citation_label $Ref._1 save_ save_ANSIG _Saveframe_category software _Name ANSIG _Version 3.3 loop_ _Task "peak assignments and peak integration" stop_ _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 save_ ############################# # NMR applied experiments # ############################# save_NMR_applied_experiment _Saveframe_category NMR_applied_experiment _Details ; 1H-15N HSQC 1H-15N TROSY 1H-15N TOCSY 1H-1H TOCSY 1H-15N NOESY 1H-1H NOESY 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. ; save_ ####################### # Sample conditions # ####################### save_Typical_Sample_Conditions _Saveframe_category sample_conditions 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 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 # # # # Index Value Definition # # # # 1 Unique # # 2 Ambiguity of geminal atoms or geminal methyl # # proton groups # # 3 Aromatic atoms on opposite sides of the ring # # (e.g. Tyr HE1 and HE2 protons) # # 4 Intraresidue ambiguities (e.g. Lys HG and # # HD protons) # # 5 Interresidue ambiguities (Lys 12 vs. Lys 27) # # 9 Ambiguous, specific ambiguity not defined # # # ################################################################### save_H117G1 _Saveframe_category assigned_chemical_shifts 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" loop_ _Atom_shift_assign_ID _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 124.62 0.2 1 4 3 CYS H H 8.70 0.02 1 5 3 CYS HA H 5.03 0.02 1 6 3 CYS N N 120.12 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 112.82 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 118.62 0.2 1 13 6 ASP H H 8.10 0.02 1 14 6 ASP HA H 5.27 0.02 1 15 6 ASP N N 126.12 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 123.82 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 123.32 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 107.72 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 122.12 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 119.22 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 116.92 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 113.92 0.2 1 38 14 GLN H H 6.96 0.02 1 39 14 GLN N N 111.22 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 121.42 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 116.32 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 112.12 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 121.22 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 123.62 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 122.22 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 123.82 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 127.72 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 127.82 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 125.82 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 114.82 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 122.42 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 122.32 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 116.02 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 121.52 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 122.52 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 125.52 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 124.72 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 127.92 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 119.02 0.2 1 100 35 HIS H H 8.62 0.02 1 101 35 HIS HA H 6.43 0.02 1 103 37 GLY H H 8.62 0.02 1 104 37 GLY N N 110.42 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 119.62 0.2 1 108 39 LEU H H 8.60 0.02 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 118.92 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 108.32 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 118.62 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 118.62 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 114.42 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 110.22 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 122.12 0.2 1 132 48 TRP H H 7.47 0.02 1 133 48 TRP N N 114.32 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 128.92 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 123.92 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 122.02 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 111.22 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 125.42 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 118.12 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 115.62 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 119.82 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 115.62 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 109.22 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 121.72 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 119.72 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 116.82 0.2 1 174 62 ASP H H 8.42 0.02 1 175 62 ASP N N 121.32 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 113.42 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 121.62 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 117.22 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 114.62 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 102.42 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 121.82 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 116.52 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 118.42 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 115.22 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 105.12 0.2 1 208 73 LEU H H 7.10 0.02 1 209 73 LEU N N 117.12 0.2 1 210 74 LYS H H 8.85 0.02 1 211 74 LYS HA H 4.69 0.02 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 118.22 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 117.22 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 124.62 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 119.52 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 118.02 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 131.42 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 116.22 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 112.82 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 109.82 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 121.22 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 120.32 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 120.52 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 110.62 0.2 1 254 89 SER H H 6.87 0.02 1 255 89 SER N N 111.02 0.2 1 256 90 GLY H H 8.39 0.02 1 257 90 GLY N N 111.12 0.2 1 258 91 GLU H H 7.64 0.02 1 259 91 GLU N N 118.72 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 116.72 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 117.72 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 115.92 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 121.52 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 124.42 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 122.22 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 120.32 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 126.92 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 115.12 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 119.42 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 118.12 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 120.42 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 124.42 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 112.12 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 120.22 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 124.22 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 123.62 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 120.02 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 116.92 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 115.12 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 121.02 0.2 1 324 113 THR H H 9.91 0.02 1 325 113 THR N N 117.72 0.2 1 326 114 PHE H H 9.49 0.02 1 327 114 PHE HA H 3.70 0.02 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 109.52 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 111.32 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 115.62 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 122.02 0.2 1 342 120 LEU H H 7.66 0.02 1 343 120 LEU N N 116.62 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 123.52 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 116.82 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 109.42 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 109.32 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 125.02 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 119.92 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 126.92 0.2 1 366 128 LYS H H 8.55 0.02 1 367 128 LYS HA H 4.33 0.02 1 stop_ 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 ; 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. ; save_