data_16740 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Amide assignments for Paracoccus denitrificans amicyanin-ZnII. ; _BMRB_accession_number 16740 _BMRB_flat_file_name bmr16740.str _Entry_type original _Submission_date 2010-02-21 _Accession_date 2010-02-21 _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 Ubbink Marcellus . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 98 "15N chemical shifts" 96 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2010-10-14 update BMRB 'update entry citation' 2010-10-05 original author 'original release' stop_ loop_ _Related_BMRB_accession_number _Relationship 16741 'Backbone assignments for Paracoccus denitrificans amicyanin-CuI.' stop_ save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _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 _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 20873742 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Meschi Francesca . . 2 Wiertz Frank . . 3 Klauss Linda . . 4 Cavalieri Chiara . . 5 Blok Anneloes . . 6 Ludwig Bernd . . 7 Heering Hendrik A. . 8 Merli Angelo . . 9 Rossi 'Gian Luigi' . . 10 Ubbink Marcellus . . stop_ _Journal_abbreviation 'J. Am. Chem. Soc.' _Journal_name_full 'Journal of the American Chemical Society' _Journal_volume 132 _Journal_issue 41 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 14537 _Page_last 14545 _Year 2010 _Details . loop_ _Keyword 'electron transfer' kinetics stop_ save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name Zn-amicyanin _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label polypeptide $amicyanin 'zinc(II) ion' $ZN stop_ _System_molecular_weight . _System_physical_state metal-substituted _System_oligomer_state ? _System_paramagnetic no _System_thiol_state . _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_amicyanin _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common amicyanin _Molecular_mass . _Mol_thiol_state 'all other bound' loop_ _Biological_function 'Electron transfer' stop_ _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 106 _Mol_residue_sequence ; GDKATIPSESPFAAAEVADG AIVVDIAKMKYETPELHVKV GDTVTWINREAMPHNVHFVA GVLGEAALKGPMMKKEQAYS LTFTEAGTYDYHCTPHPFMR GKVVVE ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 0 GLY 2 1 ASP 3 2 LYS 4 3 ALA 5 4 THR 6 5 ILE 7 6 PRO 8 7 SER 9 8 GLU 10 9 SER 11 10 PRO 12 11 PHE 13 12 ALA 14 13 ALA 15 14 ALA 16 15 GLU 17 16 VAL 18 17 ALA 19 18 ASP 20 19 GLY 21 20 ALA 22 21 ILE 23 22 VAL 24 23 VAL 25 24 ASP 26 25 ILE 27 26 ALA 28 27 LYS 29 28 MET 30 29 LYS 31 30 TYR 32 31 GLU 33 32 THR 34 33 PRO 35 34 GLU 36 35 LEU 37 36 HIS 38 37 VAL 39 38 LYS 40 39 VAL 41 40 GLY 42 41 ASP 43 42 THR 44 43 VAL 45 44 THR 46 45 TRP 47 46 ILE 48 47 ASN 49 48 ARG 50 49 GLU 51 50 ALA 52 51 MET 53 52 PRO 54 53 HIS 55 54 ASN 56 55 VAL 57 56 HIS 58 57 PHE 59 58 VAL 60 59 ALA 61 60 GLY 62 61 VAL 63 62 LEU 64 63 GLY 65 64 GLU 66 65 ALA 67 66 ALA 68 67 LEU 69 68 LYS 70 69 GLY 71 70 PRO 72 71 MET 73 72 MET 74 73 LYS 75 74 LYS 76 75 GLU 77 76 GLN 78 77 ALA 79 78 TYR 80 79 SER 81 80 LEU 82 81 THR 83 82 PHE 84 83 THR 85 84 GLU 86 85 ALA 87 86 GLY 88 87 THR 89 88 TYR 90 89 ASP 91 90 TYR 92 91 HIS 93 92 CYS 94 93 THR 95 94 PRO 96 95 HIS 97 96 PRO 98 97 PHE 99 98 MET 100 99 ARG 101 100 GLY 102 101 LYS 103 102 VAL 104 103 VAL 105 104 VAL 106 105 GLU stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-10-07 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 16741 amicyanin 100.00 106 100.00 100.00 5.27e-71 PDB 1AAC "Amicyanin Oxidized, 1.31 Angstroms" 99.06 105 100.00 100.00 3.98e-70 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 3.98e-70 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 3.98e-70 PDB 1BXA "Amicyanin Reduced, Ph 4.4, 1.3 Angstroms" 99.06 105 100.00 100.00 3.98e-70 PDB 1MDA "Crystal Structure Of An Electron-Transfer Complex Between Methylamine Dehydrogenase And Amicyanin" 97.17 103 100.00 100.00 1.43e-68 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 3.98e-70 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 3.98e-70 PDB 1SF3 "Structure Of The Reduced Form Of The P94a Mutant Of Amicyanin" 99.06 105 99.05 99.05 3.72e-69 PDB 1SF5 "Structure Of Oxidized State Of The P94a Mutant Of Amicyanin" 99.06 105 98.10 98.10 3.93e-68 PDB 1SFD "Oxidized Form Of Amicyanin Mutant P94f" 99.06 105 99.05 99.05 1.12e-68 PDB 1SFH "Reduced State Of Amicyanin Mutant P94f" 99.06 105 99.05 99.05 1.12e-68 PDB 1T5K "Crystal Structure Of Amicyanin Substituted With Cobalt" 99.06 105 100.00 100.00 3.98e-70 PDB 2GB2 "The P52g Mutant Of Amicyanin In The Cu(Ii) State." 99.06 105 99.05 99.05 7.73e-69 PDB 2GBA "Reduced Cu(I) Form At Ph 4 Of P52g Mutant Of Amicyanin" 99.06 105 99.05 99.05 7.73e-69 PDB 2GC4 "Structural Comparison Of The Oxidized Ternary Electron Transfer Complex Of Methylamine Dehydrogenase, Amicyanin And Cytochrome " 99.06 105 100.00 100.00 3.98e-70 PDB 2GC7 "Substrate Reduced, Copper Free Complex Of Methylamine Dehydrogenase, Amicyanin And Cytochrome C551i From Paracoccus Denitrifica" 99.06 105 100.00 100.00 3.98e-70 PDB 2IDQ "Structure Of M98a Mutant Of Amicyanin, Cu(Ii)" 99.06 105 99.05 99.05 3.60e-69 PDB 2IDS "Structure Of M98a Mutant Of Amicyanin, Cu(I)" 99.06 105 99.05 99.05 3.60e-69 PDB 2IDT "Structure Of M98q Mutant Of Amicyanin, Cu(Ii)" 99.06 105 98.10 98.10 1.91e-68 PDB 2IDU "Structure Of M98q Mutant Of Amicyanin, Cu(I)" 99.06 105 98.10 98.10 1.91e-68 PDB 2J55 "X-ray Reduced Paraccocus Denitrificans Methylamine Dehydrogenase O-quinone In Complex With Amicyanin." 99.06 105 100.00 100.00 3.98e-70 PDB 2J56 "X-Ray Reduced Paraccocus Denitrificans Methylamine Dehydrogenase N-Semiquinone In Complex With Amicyanin." 99.06 105 100.00 100.00 3.98e-70 PDB 2J57 "X-Ray Reduced Paraccocus Denitrificans Methylamine Dehydrogenase N-Quinol In Complex With Amicyanin." 99.06 105 100.00 100.00 3.98e-70 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 3.98e-70 PDB 2OV0 "Structure Of The Blue Copper Protein Amicyanin To 0.75 A Resolution" 99.06 105 100.00 100.00 3.98e-70 PDB 2QDV "Structure Of The Cu(Ii) Form Of The M51a Mutant Of Amicyanin" 100.00 106 98.11 98.11 2.45e-67 PDB 2QDW "Structure Of Cu(I) Form Of The M51a Mutant Of Amicyanin" 100.00 106 98.11 98.11 2.45e-67 PDB 2RAC "Amicyanin Reduced, Ph 7.7, 1.3 Angstroms" 99.06 105 100.00 100.00 3.98e-70 PDB 3IE9 "Structure Of Oxidized M98l Mutant Of Amicyanin" 99.06 105 99.05 100.00 1.12e-69 PDB 3IEA "Structure Of Reduced M98l Mutant Of Amicyanin" 99.06 105 99.05 100.00 1.12e-69 PDB 3L45 "A Joint Neutron And X-Ray Structure Of Oxidized Amicyanin" 99.06 105 100.00 100.00 3.98e-70 PDB 3PLY "Structure Of Oxidized P96g Mutant Of Amicyanin" 99.06 105 99.05 99.05 7.73e-69 PDB 3RYM "Structure Of Oxidized M98k Mutant Of Amicyanin" 99.06 105 99.05 99.05 4.15e-69 PDB 4P5R "Structure Of Oxidized W45y Mutant Of Amicyanin" 99.06 105 99.05 100.00 2.80e-69 PDB 4P5S "Structure Of Reduced W45y Mutant Of Amicyanin" 99.06 105 99.05 100.00 2.80e-69 EMBL CAA39199 "amicyanin [Paracoccus denitrificans]" 100.00 131 99.06 99.06 1.08e-70 GB ABL72795 "amicyanin [Paracoccus denitrificans PD1222]" 100.00 131 99.06 99.06 1.08e-70 PRF 1702223A amicyanin 100.00 131 99.06 99.06 1.08e-70 REF WP_041530795 "amicyanin [Paracoccus denitrificans]" 99.06 125 100.00 100.00 1.83e-70 SP P22364 "RecName: Full=Amicyanin; Flags: Precursor" 100.00 131 99.06 99.06 1.08e-70 stop_ save_ ############# # Ligands # ############# save_ZN _Saveframe_category ligand _Mol_type non-polymer _Name_common "ZN (ZINC ION)" _BMRB_code . _PDB_code ZN _Molecular_mass 65.409 _Mol_charge 2 _Mol_paramagnetic . _Mol_aromatic no _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 ; loop_ _Atom_name _PDB_atom_name _Atom_type _Atom_chirality _Atom_charge _Atom_oxidation_number _Atom_unpaired_electrons ZN ZN ZN . 2 . ? 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 _Strain _Gene_mnemonic $amicyanin 'Paracoccus denitrificans' 266 Bacteria . Paracoccus denitrificans Pd1222 mauC 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 $amicyanin 'recombinant technology' . Escherichia coli . pET28ami stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $amicyanin 1.2 mM [U-15N] stop_ save_ ############################ # Computer software used # ############################ save_AZARA _Saveframe_category software _Name AZARA _Version . loop_ _Vendor _Address _Electronic_address Boucher . . stop_ loop_ _Task processing stop_ _Details . save_ save_ANSIG _Saveframe_category software _Name ANSIG _Version . loop_ _Vendor _Address _Electronic_address Kraulis . . stop_ loop_ _Task 'chemical shift assignment' stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model DMX _Field_strength 600 _Details . save_ ############################# # NMR applied experiments # ############################# save_2D_1H-15N_HSQC_1 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-15N HSQC' _Sample_label $sample_1 save_ save_3D_1H-15N_NOESY_2 _Saveframe_category NMR_applied_experiment _Experiment_name '3D 1H-15N NOESY' _Sample_label $sample_1 save_ save_3D_1H-15N_TOCSY_3 _Saveframe_category NMR_applied_experiment _Experiment_name '3D 1H-15N TOCSY' _Sample_label $sample_1 save_ ####################### # Sample conditions # ####################### save_sample_conditions_1 _Saveframe_category sample_conditions _Details '20 mM KPi' loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units 'ionic strength' 0.08 . M pH 7.9 . pH pressure 1 . atm temperature 300 . K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference_1 _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 water H 1 protons ppm 4.70 internal direct . . . 1.0 DSS N 15 'methyl protons' ppm 0 na 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_assigned_chem_shift_list_1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Experiment_label '2D 1H-15N HSQC' '3D 1H-15N NOESY' '3D 1H-15N TOCSY' stop_ loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $sample_conditions_1 _Chem_shift_reference_set_label $chemical_shift_reference_1 _Mol_system_component_name polypeptide _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 1 2 ASP H H 8.38 . . 2 1 2 ASP N N 121.39 . . 3 2 3 LYS H H 7.94 . . 4 2 3 LYS N N 114.37 . . 5 3 4 ALA H H 6.87 . . 6 3 4 ALA N N 116.44 . . 7 4 5 THR H H 8.85 . . 8 4 5 THR N N 112.86 . . 9 5 6 ILE H H 8.25 . . 10 5 6 ILE N N 122.46 . . 11 7 8 SER H H 7.69 . . 12 7 8 SER N N 109.47 . . 13 8 9 GLU H H 9.02 . . 14 8 9 GLU N N 127.93 . . 15 9 10 SER H H 7.85 . . 16 9 10 SER N N 112.1 . . 17 11 12 PHE H H 8.57 . . 18 11 12 PHE N N 120.07 . . 19 12 13 ALA H H 8.62 . . 20 12 13 ALA N N 122.53 . . 21 13 14 ALA H H 8.17 . . 22 13 14 ALA N N 123.68 . . 23 14 15 ALA H H 8.28 . . 24 14 15 ALA N N 117.84 . . 25 15 16 GLU H H 7.89 . . 26 15 16 GLU N N 114.87 . . 27 16 17 VAL H H 7.41 . . 28 16 17 VAL N N 121.89 . . 29 17 18 ALA H H 8.59 . . 30 17 18 ALA N N 132.06 . . 31 18 19 ASP H H 8.4 . . 32 18 19 ASP N N 121.08 . . 33 19 20 GLY H H 8.59 . . 34 19 20 GLY N N 112.36 . . 35 20 21 ALA H H 7.27 . . 36 20 21 ALA N N 122.86 . . 37 21 22 ILE H H 8.4 . . 38 21 22 ILE N N 123.53 . . 39 22 23 VAL H H 8.05 . . 40 22 23 VAL N N 129.35 . . 41 23 24 VAL H H 8.7 . . 42 23 24 VAL N N 128.06 . . 43 24 25 ASP H H 8.62 . . 44 24 25 ASP N N 127.33 . . 45 25 26 ILE H H 8.58 . . 46 25 26 ILE N N 120.29 . . 47 26 27 ALA H H 8.3 . . 48 26 27 ALA N N 124.5 . . 49 27 28 LYS H H 8.9 . . 50 27 28 LYS N N 119.65 . . 51 28 29 MET H H 8.88 . . 52 28 29 MET N N 108.4 . . 53 29 30 LYS H H 7.33 . . 54 29 30 LYS N N 113.78 . . 55 30 31 TYR H H 8.17 . . 56 30 31 TYR N N 118.55 . . 57 31 32 GLU H H 9.3 . . 58 31 32 GLU N N 123.2 . . 59 32 33 THR H H 6.23 . . 60 32 33 THR N N 110.19 . . 61 34 35 GLU H H 8.09 . . 62 34 35 GLU N N 121.99 . . 63 35 36 LEU H H 7.69 . . 64 35 36 LEU N N 128.59 . . 65 36 37 HIS H H 8.93 . . 66 36 37 HIS N N 127.22 . . 67 37 38 VAL H H 9.1 . . 68 37 38 VAL N N 117.18 . . 69 38 39 LYS H H 9.19 . . 70 38 39 LYS N N 121.13 . . 71 39 40 VAL H H 7.92 . . 72 39 40 VAL N N 119.45 . . 73 40 41 GLY H H 8.87 . . 74 40 41 GLY N N 117.11 . . 75 41 42 ASP H H 8.36 . . 76 41 42 ASP N N 121.88 . . 77 42 43 THR H H 8.45 . . 78 42 43 THR N N 116.62 . . 79 43 44 VAL H H 9.27 . . 80 43 44 VAL N N 129.77 . . 81 44 45 THR H H 8.05 . . 82 44 45 THR N N 122.75 . . 83 45 46 TRP H H 9.58 . . 84 45 46 TRP N N 129.91 . . 85 46 47 ILE H H 8.31 . . 86 46 47 ILE N N 117.67 . . 87 47 48 ASN H H 8.53 . . 88 47 48 ASN N N 123.81 . . 89 47 48 ASN HD21 H 7.46 . . 90 47 48 ASN HD22 H 6.82 . . 91 47 48 ASN ND2 N 110.38 . . 92 48 49 ARG H H 9.49 . . 93 48 49 ARG N N 125.12 . . 94 49 50 GLU H H 8.35 . . 95 49 50 GLU N N 120.68 . . 96 50 51 ALA H H 7.94 . . 97 50 51 ALA N N 117.5 . . 98 51 52 MET H H 7.46 . . 99 51 52 MET N N 119.66 . . 100 55 56 VAL H H 6.55 . . 101 55 56 VAL N N 107.59 . . 102 56 57 HIS H H 8.48 . . 103 56 57 HIS N N 124.47 . . 104 58 59 VAL H H 9 . . 105 58 59 VAL N N 118.25 . . 106 59 60 ALA H H 8.68 . . 107 59 60 ALA N N 123.59 . . 108 60 61 GLY H H 7.66 . . 109 60 61 GLY N N 111.58 . . 110 61 62 VAL H H 7.84 . . 111 61 62 VAL N N 121.09 . . 112 62 63 LEU H H 9.16 . . 113 62 63 LEU N N 115.37 . . 114 63 64 GLY H H 7.42 . . 115 63 64 GLY N N 114.78 . . 116 64 65 GLU H H 8.66 . . 117 64 65 GLU N N 119.34 . . 118 65 66 ALA H H 7.98 . . 119 65 66 ALA N N 119.44 . . 120 66 67 ALA H H 8.48 . . 121 66 67 ALA N N 120.86 . . 122 67 68 LEU H H 8.94 . . 123 67 68 LEU N N 123.97 . . 124 68 69 LYS H H 8.44 . . 125 68 69 LYS N N 128.75 . . 126 69 70 GLY H H 8.85 . . 127 69 70 GLY N N 116.32 . . 128 71 72 MET H H 8.31 . . 129 71 72 MET N N 117.22 . . 130 72 73 MET H H 8.77 . . 131 72 73 MET N N 122.8 . . 132 73 74 LYS H H 8.56 . . 133 73 74 LYS N N 123.2 . . 134 74 75 LYS H H 7.94 . . 135 74 75 LYS N N 119.79 . . 136 75 76 GLU H H 9.35 . . 137 75 76 GLU N N 118.22 . . 138 76 77 GLN H H 7.89 . . 139 76 77 GLN N N 116.81 . . 140 76 77 GLN HE21 H 7.72 . . 141 76 77 GLN HE22 H 6.65 . . 142 76 77 GLN NE2 N 112.33 . . 143 77 78 ALA H H 8.82 . . 144 77 78 ALA N N 122.28 . . 145 78 79 TYR H H 8.43 . . 146 78 79 TYR N N 117.27 . . 147 79 80 SER H H 7.62 . . 148 79 80 SER N N 121.73 . . 149 80 81 LEU H H 8.84 . . 150 80 81 LEU N N 119.8 . . 151 81 82 THR H H 8.49 . . 152 81 82 THR N N 119.67 . . 153 82 83 PHE H H 8.09 . . 154 82 83 PHE N N 125.1 . . 155 83 84 THR H H 8.15 . . 156 83 84 THR N N 112.24 . . 157 84 85 GLU H H 7.67 . . 158 84 85 GLU N N 120.15 . . 159 85 86 ALA H H 9.03 . . 160 85 86 ALA N N 131.34 . . 161 86 87 GLY H H 8.74 . . 162 86 87 GLY N N 109.08 . . 163 87 88 THR H H 7.72 . . 164 87 88 THR N N 114.63 . . 165 88 89 TYR H H 9.13 . . 166 88 89 TYR N N 127.44 . . 167 89 90 ASP H H 8.53 . . 168 89 90 ASP N N 126.89 . . 169 90 91 TYR H H 8.3 . . 170 90 91 TYR N N 116.85 . . 171 91 92 HIS H H 8.68 . . 172 91 92 HIS N N 118.64 . . 173 92 93 CYS H H 6.78 . . 174 92 93 CYS N N 120.76 . . 175 93 94 THR H H 10.23 . . 176 93 94 THR N N 128.84 . . 177 97 98 PHE H H 6.41 . . 178 97 98 PHE N N 111.11 . . 179 98 99 MET H H 8.41 . . 180 98 99 MET N N 125.63 . . 181 99 100 ARG H H 7.76 . . 182 99 100 ARG N N 121.3 . . 183 100 101 GLY H H 7.71 . . 184 100 101 GLY N N 109.08 . . 185 101 102 LYS H H 8.38 . . 186 101 102 LYS N N 117.44 . . 187 102 103 VAL H H 9.1 . . 188 102 103 VAL N N 126.89 . . 189 103 104 VAL H H 9.28 . . 190 103 104 VAL N N 130.03 . . 191 104 105 VAL H H 9.18 . . 192 104 105 VAL N N 128.81 . . 193 105 106 GLU H H 8.77 . . 194 105 106 GLU N N 133.61 . . stop_ save_