data_16741 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Backbone assignments for Paracoccus denitrificans amicyanin-CuI. ; _BMRB_accession_number 16741 _BMRB_flat_file_name bmr16741.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" 97 "13C chemical shifts" 285 "15N chemical shifts" 97 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 16740 'Amide assignments for Paracoccus denitrificans amicyanin-ZnII.' 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 holo-amicyanin _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label polypeptide $amicyanin 'copper(I) ion' $CU1 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 16740 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_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 Tue Jun 9 13:36:26 2009 ; 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 _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_HNCACB_2 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCACB' _Sample_label $sample_1 save_ save_3D_HNCO_3 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCO' _Sample_label $sample_1 save_ save_3D_C(CO)NH_4 _Saveframe_category NMR_applied_experiment _Experiment_name '3D C(CO)NH' _Sample_label $sample_1 save_ save_3D_HN(CA)CO_5 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HN(CA)CO' _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' 0.01 . M pH 6.8 . 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 DSS C 13 'methyl protons' ppm 0 na indirect . . . 0.251449530 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 HNCACB' '3D HNCO' '3D C(CO)NH' '3D HN(CA)CO' 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 C C 173.17 . . 3 1 2 ASP CA C 57.21 . . 4 1 2 ASP CB C 41.03 . . 5 1 2 ASP N N 121.32 . . 6 2 3 LYS H H 7.97 . . 7 2 3 LYS C C 175.52 . . 8 2 3 LYS CA C 55.75 . . 9 2 3 LYS CB C 33.2 . . 10 2 3 LYS N N 113.36 . . 11 3 4 ALA H H 6.8 . . 12 3 4 ALA C C 174.64 . . 13 3 4 ALA CA C 51.12 . . 14 3 4 ALA CB C 22.84 . . 15 3 4 ALA N N 116.19 . . 16 4 5 THR H H 8.92 . . 17 4 5 THR C C 177.94 . . 18 4 5 THR CA C 60.25 . . 19 4 5 THR CB C 70.71 . . 20 4 5 THR N N 113.6 . . 21 5 6 ILE H H 8.25 . . 22 5 6 ILE C C 174.95 . . 23 5 6 ILE CA C 59.15 . . 24 5 6 ILE CB C 39.85 . . 25 5 6 ILE N N 122.47 . . 26 6 7 PRO C C 173.43 . . 27 6 7 PRO CA C 60.89 . . 28 6 7 PRO CB C 32.37 . . 29 7 8 SER H H 7.69 . . 30 7 8 SER C C 175.92 . . 31 7 8 SER CA C 56.17 . . 32 7 8 SER CB C 64.27 . . 33 7 8 SER N N 109.32 . . 34 8 9 GLU H H 9.04 . . 35 8 9 GLU C C 172.82 . . 36 8 9 GLU CA C 59.27 . . 37 8 9 GLU CB C 29.84 . . 38 8 9 GLU N N 127.81 . . 39 9 10 SER H H 7.86 . . 40 9 10 SER C C 178.85 . . 41 9 10 SER CA C 55.69 . . 42 9 10 SER CB C 63.5 . . 43 9 10 SER N N 111.98 . . 44 10 11 PRO C C 174.99 . . 45 10 11 PRO CA C 63.07 . . 46 10 11 PRO CB C 32.75 . . 47 11 12 PHE H H 8.55 . . 48 11 12 PHE C C 176.56 . . 49 11 12 PHE CA C 54.25 . . 50 11 12 PHE CB C 41.43 . . 51 11 12 PHE N N 119.93 . . 52 12 13 ALA H H 8.62 . . 53 12 13 ALA C C 171.83 . . 54 12 13 ALA CA C 53.26 . . 55 12 13 ALA CB C 18.75 . . 56 12 13 ALA N N 122.42 . . 57 13 14 ALA H H 8.19 . . 58 13 14 ALA C C 170.95 . . 59 13 14 ALA CA C 54.74 . . 60 13 14 ALA N N 123.64 . . 61 14 15 ALA H H 8.29 . . 62 14 15 ALA C C 171.92 . . 63 14 15 ALA CA C 53.99 . . 64 14 15 ALA CB C 18.79 . . 65 14 15 ALA N N 117.75 . . 66 15 16 GLU H H 7.9 . . 67 15 16 GLU C C 173.73 . . 68 15 16 GLU CA C 56.35 . . 69 15 16 GLU CB C 29.73 . . 70 15 16 GLU N N 114.74 . . 71 16 17 VAL H H 7.41 . . 72 16 17 VAL C C 174.82 . . 73 16 17 VAL CA C 63.64 . . 74 16 17 VAL CB C 31.67 . . 75 16 17 VAL N N 121.73 . . 76 17 18 ALA H H 8.6 . . 77 17 18 ALA C C 172.24 . . 78 17 18 ALA CA C 52.15 . . 79 17 18 ALA CB C 19.49 . . 80 17 18 ALA N N 131.95 . . 81 18 19 ASP H H 8.4 . . 82 18 19 ASP C C 172.62 . . 83 18 19 ASP CA C 56.09 . . 84 18 19 ASP CB C 40.66 . . 85 18 19 ASP N N 120.99 . . 86 19 20 GLY H H 8.59 . . 87 19 20 GLY C C 174.98 . . 88 19 20 GLY CA C 45.14 . . 89 19 20 GLY N N 112.25 . . 90 20 21 ALA H H 7.27 . . 91 20 21 ALA C C 173.27 . . 92 20 21 ALA CA C 52.5 . . 93 20 21 ALA CB C 19.55 . . 94 20 21 ALA N N 122.79 . . 95 21 22 ILE H H 8.43 . . 96 21 22 ILE C C 174.9 . . 97 21 22 ILE CA C 62.55 . . 98 21 22 ILE CB C 37.37 . . 99 21 22 ILE N N 123.43 . . 100 22 23 VAL H H 8.05 . . 101 22 23 VAL C C 174.01 . . 102 22 23 VAL CA C 60.4 . . 103 22 23 VAL CB C 35.96 . . 104 22 23 VAL N N 129.18 . . 105 23 24 VAL H H 8.71 . . 106 23 24 VAL C C 175.65 . . 107 23 24 VAL CA C 61.39 . . 108 23 24 VAL CB C 32.91 . . 109 23 24 VAL N N 127.95 . . 110 24 25 ASP H H 8.55 . . 111 24 25 ASP C C 174.51 . . 112 24 25 ASP CA C 55.12 . . 113 24 25 ASP CB C 43.28 . . 114 24 25 ASP N N 127.15 . . 115 25 26 ILE H H 8.52 . . 116 25 26 ILE C C 175.91 . . 117 25 26 ILE CA C 60.61 . . 118 25 26 ILE CB C 39.06 . . 119 25 26 ILE N N 120.13 . . 120 26 27 ALA H H 8.17 . . 121 26 27 ALA C C 173.86 . . 122 26 27 ALA CA C 52.04 . . 123 26 27 ALA CB C 22.15 . . 124 26 27 ALA N N 124.17 . . 125 27 28 LYS H H 9.03 . . 126 27 28 LYS C C 174.17 . . 127 27 28 LYS CA C 56.51 . . 128 27 28 LYS CB C 29.31 . . 129 27 28 LYS N N 119.62 . . 130 28 29 MET H H 8.96 . . 131 28 29 MET C C 175.99 . . 132 28 29 MET CA C 55.14 . . 133 28 29 MET CB C 28.17 . . 134 28 29 MET N N 108.89 . . 135 29 30 LYS H H 7.2 . . 136 29 30 LYS C C 175.72 . . 137 29 30 LYS CA C 55.42 . . 138 29 30 LYS CB C 35.83 . . 139 29 30 LYS N N 113.48 . . 140 30 31 TYR H H 7.89 . . 141 30 31 TYR C C 172.69 . . 142 30 31 TYR CA C 57.61 . . 143 30 31 TYR CB C 37.82 . . 144 30 31 TYR N N 119.13 . . 145 31 32 GLU H H 9.25 . . 146 31 32 GLU C C 173.81 . . 147 31 32 GLU CA C 60.56 . . 148 31 32 GLU CB C 29.99 . . 149 31 32 GLU N N 123.17 . . 150 32 33 THR H H 6.22 . . 151 32 33 THR CA C 58.83 . . 152 32 33 THR CB C 69.7 . . 153 32 33 THR N N 110.09 . . 154 34 35 GLU H H 8.17 . . 155 34 35 GLU C C 177.33 . . 156 34 35 GLU CA C 56.01 . . 157 34 35 GLU CB C 30.35 . . 158 34 35 GLU N N 122.25 . . 159 35 36 LEU H H 7.67 . . 160 35 36 LEU C C 175.52 . . 161 35 36 LEU CA C 53.83 . . 162 35 36 LEU CB C 45.84 . . 163 35 36 LEU N N 128.51 . . 164 36 37 HIS H H 9.08 . . 165 36 37 HIS C C 176.11 . . 166 36 37 HIS CA C 54.71 . . 167 36 37 HIS CB C 28.83 . . 168 36 37 HIS N N 126.62 . . 169 37 38 VAL H H 9.05 . . 170 37 38 VAL C C 176.01 . . 171 37 38 VAL CA C 58.67 . . 172 37 38 VAL CB C 34.09 . . 173 37 38 VAL N N 117.05 . . 174 38 39 LYS H H 9.19 . . 175 38 39 LYS C C 173.07 . . 176 38 39 LYS CA C 53.59 . . 177 38 39 LYS CB C 34.2 . . 178 38 39 LYS N N 121.05 . . 179 39 40 VAL H H 7.88 . . 180 39 40 VAL C C 173.11 . . 181 39 40 VAL CA C 66.21 . . 182 39 40 VAL CB C 31.37 . . 183 39 40 VAL N N 119.3 . . 184 40 41 GLY H H 8.86 . . 185 40 41 GLY C C 175.99 . . 186 40 41 GLY CA C 44.64 . . 187 40 41 GLY N N 117.04 . . 188 41 42 ASP H H 8.34 . . 189 41 42 ASP C C 174.84 . . 190 41 42 ASP CA C 55.25 . . 191 41 42 ASP CB C 41.32 . . 192 41 42 ASP N N 121.7 . . 193 42 43 THR H H 8.46 . . 194 42 43 THR C C 176.67 . . 195 42 43 THR CA C 62.09 . . 196 42 43 THR CB C 70.33 . . 197 42 43 THR N N 116.53 . . 198 43 44 VAL H H 9.27 . . 199 43 44 VAL C C 176.65 . . 200 43 44 VAL CA C 64.22 . . 201 43 44 VAL CB C 34.33 . . 202 43 44 VAL N N 129.77 . . 203 44 45 THR H H 8.05 . . 204 44 45 THR C C 177.75 . . 205 44 45 THR CA C 61.7 . . 206 44 45 THR CB C 71.19 . . 207 44 45 THR N N 122.64 . . 208 45 46 TRP H H 9.58 . . 209 45 46 TRP C C 174.74 . . 210 45 46 TRP CA C 58.53 . . 211 45 46 TRP CB C 31.8 . . 212 45 46 TRP N N 129.85 . . 213 46 47 ILE H H 8.3 . . 214 46 47 ILE C C 174.88 . . 215 46 47 ILE CA C 60.72 . . 216 46 47 ILE CB C 41.25 . . 217 46 47 ILE N N 117.52 . . 218 47 48 ASN H H 8.51 . . 219 47 48 ASN C C 174.09 . . 220 47 48 ASN CA C 52.94 . . 221 47 48 ASN CB C 37.82 . . 222 47 48 ASN N N 123.65 . . 223 48 49 ARG H H 9.36 . . 224 48 49 ARG C C 173.36 . . 225 48 49 ARG CA C 53.53 . . 226 48 49 ARG CB C 30.13 . . 227 48 49 ARG N N 125.05 . . 228 49 50 GLU H H 8.68 . . 229 49 50 GLU C C 177.98 . . 230 49 50 GLU CA C 54.01 . . 231 49 50 GLU CB C 33.79 . . 232 49 50 GLU N N 121.57 . . 233 50 51 ALA H H 7.89 . . 234 50 51 ALA C C 171.02 . . 235 50 51 ALA CA C 53.1 . . 236 50 51 ALA CB C 18.54 . . 237 50 51 ALA N N 117.2 . . 238 51 52 MET H H 7.47 . . 239 51 52 MET C C 178.32 . . 240 51 52 MET CA C 52.9 . . 241 51 52 MET CB C 32.6 . . 242 51 52 MET N N 120.07 . . 243 53 54 HIS H H 7.36 . . 244 53 54 HIS N N 117.47 . . 245 55 56 VAL H H 6.47 . . 246 55 56 VAL C C 176.21 . . 247 55 56 VAL CA C 60.98 . . 248 55 56 VAL CB C 33.83 . . 249 55 56 VAL N N 106.72 . . 250 56 57 HIS H H 8.48 . . 251 56 57 HIS C C 174.04 . . 252 56 57 HIS CA C 52.98 . . 253 56 57 HIS CB C 33.57 . . 254 56 57 HIS N N 123.86 . . 255 57 58 PHE H H 9.21 . . 256 57 58 PHE C C 174.27 . . 257 57 58 PHE CA C 55.24 . . 258 57 58 PHE CB C 40.68 . . 259 57 58 PHE N N 125.19 . . 260 58 59 VAL H H 8.85 . . 261 58 59 VAL C C 174.9 . . 262 58 59 VAL CA C 62.35 . . 263 58 59 VAL CB C 32.38 . . 264 58 59 VAL N N 117.97 . . 265 59 60 ALA H H 8.68 . . 266 59 60 ALA C C 172.71 . . 267 59 60 ALA CA C 54.64 . . 268 59 60 ALA CB C 18.1 . . 269 59 60 ALA N N 123.71 . . 270 60 61 GLY H H 7.63 . . 271 60 61 GLY C C 174.94 . . 272 60 61 GLY CA C 45.88 . . 273 60 61 GLY N N 111.5 . . 274 61 62 VAL H H 7.8 . . 275 61 62 VAL C C 173.75 . . 276 61 62 VAL CA C 66.58 . . 277 61 62 VAL CB C 32.93 . . 278 61 62 VAL N N 120.91 . . 279 62 63 LEU H H 9.18 . . 280 62 63 LEU C C 174.94 . . 281 62 63 LEU CA C 53.56 . . 282 62 63 LEU CB C 42.61 . . 283 62 63 LEU N N 115.35 . . 284 63 64 GLY H H 7.43 . . 285 63 64 GLY C C 178.51 . . 286 63 64 GLY CA C 44.08 . . 287 63 64 GLY N N 105.07 . . 288 64 65 GLU H H 8.65 . . 289 64 65 GLU C C 172.49 . . 290 64 65 GLU CA C 59.79 . . 291 64 65 GLU CB C 29.96 . . 292 64 65 GLU N N 119.22 . . 293 65 66 ALA H H 7.95 . . 294 65 66 ALA C C 172.83 . . 295 65 66 ALA CA C 50.52 . . 296 65 66 ALA CB C 20.4 . . 297 65 66 ALA N N 119.28 . . 298 66 67 ALA H H 8.48 . . 299 66 67 ALA C C 173.44 . . 300 66 67 ALA CA C 52.45 . . 301 66 67 ALA CB C 19.93 . . 302 66 67 ALA N N 120.64 . . 303 67 68 LEU H H 8.87 . . 304 67 68 LEU C C 176.77 . . 305 67 68 LEU CA C 54.6 . . 306 67 68 LEU CB C 43.47 . . 307 67 68 LEU N N 123.48 . . 308 68 69 LYS H H 8.5 . . 309 68 69 LYS C C 175.22 . . 310 68 69 LYS CA C 55.09 . . 311 68 69 LYS CB C 31.42 . . 312 68 69 LYS N N 128.97 . . 313 69 70 GLY H H 8.9 . . 314 69 70 GLY CA C 44.54 . . 315 69 70 GLY N N 116.65 . . 316 70 71 PRO C C 173.74 . . 317 70 71 PRO CA C 61.94 . . 318 70 71 PRO CB C 31.75 . . 319 71 72 MET H H 8.25 . . 320 71 72 MET C C 174.08 . . 321 71 72 MET CA C 54.54 . . 322 71 72 MET CB C 29.19 . . 323 71 72 MET N N 117.1 . . 324 72 73 MET H H 9.02 . . 325 72 73 MET C C 173.47 . . 326 72 73 MET CA C 55.2 . . 327 72 73 MET CB C 37.42 . . 328 72 73 MET N N 122.96 . . 329 73 74 LYS H H 8.58 . . 330 73 74 LYS C C 175.79 . . 331 73 74 LYS CA C 54.97 . . 332 73 74 LYS CB C 33.19 . . 333 73 74 LYS N N 123.11 . . 334 74 75 LYS H H 7.91 . . 335 74 75 LYS C C 172.98 . . 336 74 75 LYS CA C 59.09 . . 337 74 75 LYS CB C 33.28 . . 338 74 75 LYS N N 119.73 . . 339 75 76 GLU H H 9.36 . . 340 75 76 GLU C C 174.73 . . 341 75 76 GLU CA C 58.3 . . 342 75 76 GLU CB C 26.33 . . 343 75 76 GLU N N 118.11 . . 344 76 77 GLN H H 7.89 . . 345 76 77 GLN C C 177.4 . . 346 76 77 GLN CA C 55.13 . . 347 76 77 GLN CB C 31.89 . . 348 76 77 GLN N N 116.67 . . 349 77 78 ALA H H 8.8 . . 350 77 78 ALA C C 175.05 . . 351 77 78 ALA CA C 49.85 . . 352 77 78 ALA CB C 25.02 . . 353 77 78 ALA N N 122.05 . . 354 78 79 TYR H H 8.41 . . 355 78 79 TYR C C 176.72 . . 356 78 79 TYR CA C 59.51 . . 357 78 79 TYR CB C 43.51 . . 358 78 79 TYR N N 117.13 . . 359 79 80 SER H H 7.62 . . 360 79 80 SER C C 177.65 . . 361 79 80 SER CA C 57.47 . . 362 79 80 SER CB C 67.23 . . 363 79 80 SER N N 121.65 . . 364 80 81 LEU H H 8.84 . . 365 80 81 LEU C C 175.97 . . 366 80 81 LEU CA C 54.61 . . 367 80 81 LEU CB C 48.18 . . 368 80 81 LEU N N 119.69 . . 369 81 82 THR H H 8.51 . . 370 81 82 THR C C 176.23 . . 371 81 82 THR CA C 61.54 . . 372 81 82 THR CB C 69.33 . . 373 81 82 THR N N 119.61 . . 374 82 83 PHE H H 8.11 . . 375 82 83 PHE C C 173.55 . . 376 82 83 PHE CA C 59.58 . . 377 82 83 PHE CB C 41.55 . . 378 82 83 PHE N N 125.08 . . 379 83 84 THR H H 8.14 . . 380 83 84 THR C C 176.23 . . 381 83 84 THR CA C 62.1 . . 382 83 84 THR CB C 69.06 . . 383 83 84 THR N N 112.02 . . 384 84 85 GLU H H 7.67 . . 385 84 85 GLU C C 174.58 . . 386 84 85 GLU CA C 55.31 . . 387 84 85 GLU CB C 33.82 . . 388 84 85 GLU N N 119.92 . . 389 85 86 ALA H H 9.04 . . 390 85 86 ALA C C 173.67 . . 391 85 86 ALA CA C 52.93 . . 392 85 86 ALA CB C 18.54 . . 393 85 86 ALA N N 131.29 . . 394 86 87 GLY H H 8.74 . . 395 86 87 GLY C C 179.82 . . 396 86 87 GLY CA C 44.88 . . 397 86 87 GLY N N 109.01 . . 398 87 88 THR H H 7.74 . . 399 87 88 THR C C 177.06 . . 400 87 88 THR CA C 62.26 . . 401 87 88 THR CB C 70.39 . . 402 87 88 THR N N 114.57 . . 403 88 89 TYR H H 9.12 . . 404 88 89 TYR C C 176.15 . . 405 88 89 TYR CA C 56.57 . . 406 88 89 TYR CB C 39.92 . . 407 88 89 TYR N N 127.28 . . 408 89 90 ASP H H 8.58 . . 409 89 90 ASP C C 175.19 . . 410 89 90 ASP CA C 54.53 . . 411 89 90 ASP CB C 42.94 . . 412 89 90 ASP N N 126.65 . . 413 90 91 TYR H H 8.36 . . 414 90 91 TYR C C 175.98 . . 415 90 91 TYR CA C 56.31 . . 416 90 91 TYR CB C 39.45 . . 417 90 91 TYR N N 116.89 . . 418 91 92 HIS H H 8.64 . . 419 91 92 HIS C C 179.71 . . 420 91 92 HIS CA C 54.62 . . 421 91 92 HIS CB C 33.18 . . 422 91 92 HIS N N 117.11 . . 423 92 93 CYS H H 7.02 . . 424 92 93 CYS CA C 58.03 . . 425 92 93 CYS CB C 30.48 . . 426 92 93 CYS N N 122.62 . . 427 93 94 THR H H 10.39 . . 428 93 94 THR CA C 69.55 . . 429 93 94 THR CB C 65.15 . . 430 93 94 THR N N 128.25 . . 431 94 95 PRO C C 174.3 . . 432 94 95 PRO CA C 64.08 . . 433 95 96 HIS H H 7.23 . . 434 95 96 HIS CA C 52.73 . . 435 95 96 HIS CB C 29.47 . . 436 95 96 HIS N N 118.29 . . 437 97 98 PHE H H 6.62 . . 438 97 98 PHE C C 173.56 . . 439 97 98 PHE CA C 56.81 . . 440 97 98 PHE CB C 37.48 . . 441 97 98 PHE N N 113.69 . . 442 98 99 MET H H 8.47 . . 443 98 99 MET CA C 56.62 . . 444 98 99 MET CB C 31.52 . . 445 98 99 MET N N 126.35 . . 446 99 100 ARG H H 7.73 . . 447 99 100 ARG C C 174.74 . . 448 99 100 ARG CA C 54.66 . . 449 99 100 ARG CB C 34.81 . . 450 99 100 ARG N N 121.34 . . 451 100 101 GLY H H 7.67 . . 452 100 101 GLY C C 179.03 . . 453 100 101 GLY CA C 43.78 . . 454 100 101 GLY N N 108.97 . . 455 101 102 LYS H H 8.44 . . 456 101 102 LYS C C 174.48 . . 457 101 102 LYS CA C 55.91 . . 458 101 102 LYS CB C 36.78 . . 459 101 102 LYS N N 116.97 . . 460 102 103 VAL H H 9.1 . . 461 102 103 VAL C C 176.67 . . 462 102 103 VAL CA C 61.83 . . 463 102 103 VAL CB C 34.35 . . 464 102 103 VAL N N 126.61 . . 465 103 104 VAL H H 9.27 . . 466 103 104 VAL C C 176.84 . . 467 103 104 VAL CA C 61.87 . . 468 103 104 VAL CB C 32.04 . . 469 103 104 VAL N N 129.75 . . 470 104 105 VAL H H 9.22 . . 471 104 105 VAL C C 174.58 . . 472 104 105 VAL CA C 60.85 . . 473 104 105 VAL CB C 32.15 . . 474 104 105 VAL N N 128.95 . . 475 105 106 GLU H H 8.85 . . 476 105 106 GLU C C 170.05 . . 477 105 106 GLU CA C 57.39 . . 478 105 106 GLU CB C 32.63 . . 479 105 106 GLU N N 133.54 . . stop_ save_