data_4062 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; 1H and 15N Resonance Assignments and Secondary Structure of the Carbon Monoxide Complex of Sperm Whale Myoglobin ; _BMRB_accession_number 4062 _BMRB_flat_file_name bmr4062.str _Entry_type original _Submission_date 1997-09-26 _Accession_date 1997-09-26 _Entry_origination BMRB _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 Theriault Yves . . 2 Pochapsky Thomas C. . 3 Dalvit Claudio . . 4 Chiu Mark L. . 5 Sligar Stephen G. . 6 Wright Peter E. . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 690 "15N chemical shifts" 148 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 1998-02-25 reformat BMRB 'converted to NMR-STAR version 2.1' stop_ _Original_release_date 1997-09-26 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full ; Theriault, Y., Pochapsky T. C., Dalvit, C., Chiu, M., Sligar, S. G., and Wright, P. E., "1H and 15N Resonance Assignments and Secondary Structure of the Carbon Monoxide Complex of Sperm Whale Myoglobin," J. Biomol. NMR 4, 491-504 (1994). ; _Citation_title ; 1H and 15N Resonance Assignments and Secondary Structure of the Carbon Monoxide Complex of Sperm Whale Myoglobin ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code 94355813 _PubMed_ID ? loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Theriault Yves . . 2 Pochapsky Thomas C. . 3 Dalvit Claudio . . 4 Chiu Mark L. . 5 Sligar Stephen G. . 6 Wright Peter E. . stop_ _Journal_abbreviation 'J. Biomol. NMR' _Journal_name_full 'Journal of Biomolecular NMR' _Journal_volume 4 _Journal_issue . _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 491 _Page_last 504 _Year 1994 _Details . loop_ _Keyword 'Heme protein' 'Iron protoporphyrin IX' 'MbCO, myoglobin complexed with carbon monoxide' NMR stop_ save_ ################################## # Molecular system description # ################################## save_MbCO _Saveframe_category molecular_system _Mol_system_name 'myoglobin carbon monoxide complex' _Abbreviation_common MbCO _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label apomyoglobin $apoMb 'Iron protoporphyrin IX' $entity_PP9 'Carbon monoxide' $entity_CMO stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state monomer _System_paramagnetic no _System_thiol_state . loop_ _Biological_function 'Oxygen storage protein' stop_ _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_apoMb _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common apomyoglobin _Abbreviation_common apoMb _Molecular_mass . _Mol_thiol_state . _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 154 _Mol_residue_sequence ; MVLSEGEWQLVLHVWAKVEA DVAGHGQDILIRLFKSHPET LEKFDRFKHLKTEAEMKASE DLKKHGVTVLTALGAILKKK GHHEAELKPLAQSHATKHKI PIKYLEFISEAIIHVLHSRH PGDFGADAQGAMNKALELFR KDIAAKYKELGYQG ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 0 MET 2 1 VAL 3 2 LEU 4 3 SER 5 4 GLU 6 5 GLY 7 6 GLU 8 7 TRP 9 8 GLN 10 9 LEU 11 10 VAL 12 11 LEU 13 12 HIS 14 13 VAL 15 14 TRP 16 15 ALA 17 16 LYS 18 17 VAL 19 18 GLU 20 19 ALA 21 20 ASP 22 21 VAL 23 22 ALA 24 23 GLY 25 24 HIS 26 25 GLY 27 26 GLN 28 27 ASP 29 28 ILE 30 29 LEU 31 30 ILE 32 31 ARG 33 32 LEU 34 33 PHE 35 34 LYS 36 35 SER 37 36 HIS 38 37 PRO 39 38 GLU 40 39 THR 41 40 LEU 42 41 GLU 43 42 LYS 44 43 PHE 45 44 ASP 46 45 ARG 47 46 PHE 48 47 LYS 49 48 HIS 50 49 LEU 51 50 LYS 52 51 THR 53 52 GLU 54 53 ALA 55 54 GLU 56 55 MET 57 56 LYS 58 57 ALA 59 58 SER 60 59 GLU 61 60 ASP 62 61 LEU 63 62 LYS 64 63 LYS 65 64 HIS 66 65 GLY 67 66 VAL 68 67 THR 69 68 VAL 70 69 LEU 71 70 THR 72 71 ALA 73 72 LEU 74 73 GLY 75 74 ALA 76 75 ILE 77 76 LEU 78 77 LYS 79 78 LYS 80 79 LYS 81 80 GLY 82 81 HIS 83 82 HIS 84 83 GLU 85 84 ALA 86 85 GLU 87 86 LEU 88 87 LYS 89 88 PRO 90 89 LEU 91 90 ALA 92 91 GLN 93 92 SER 94 93 HIS 95 94 ALA 96 95 THR 97 96 LYS 98 97 HIS 99 98 LYS 100 99 ILE 101 100 PRO 102 101 ILE 103 102 LYS 104 103 TYR 105 104 LEU 106 105 GLU 107 106 PHE 108 107 ILE 109 108 SER 110 109 GLU 111 110 ALA 112 111 ILE 113 112 ILE 114 113 HIS 115 114 VAL 116 115 LEU 117 116 HIS 118 117 SER 119 118 ARG 120 119 HIS 121 120 PRO 122 121 GLY 123 122 ASP 124 123 PHE 125 124 GLY 126 125 ALA 127 126 ASP 128 127 ALA 129 128 GLN 130 129 GLY 131 130 ALA 132 131 MET 133 132 ASN 134 133 LYS 135 134 ALA 136 135 LEU 137 136 GLU 138 137 LEU 139 138 PHE 140 139 ARG 141 140 LYS 142 141 ASP 143 142 ILE 144 143 ALA 145 144 ALA 146 145 LYS 147 146 TYR 148 147 LYS 149 148 GLU 150 149 LEU 151 150 GLY 152 151 TYR 153 152 GLN 154 153 GLY stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date . save_ ############# # Ligands # ############# save_PP9 _Saveframe_category ligand _Mol_type "non-polymer (NON-POLYMER)" _Name_common 'PROTOPORPHYRIN IX' _BMRB_code PP9 _PDB_code PP9 _Molecular_mass 562.658 _Mol_charge 0 _Mol_paramagnetic . _Mol_aromatic yes _Details . loop_ _Atom_name _PDB_atom_name _Atom_type _Atom_chirality _Atom_charge _Atom_oxidation_number _Atom_unpaired_electrons CHA CHA C . 0 . ? CHB CHB C . 0 . ? CHC CHC C . 0 . ? CHD CHD C . 0 . ? NA NA N . 0 . ? C1A C1A C . 0 . ? C2A C2A C . 0 . ? C3A C3A C . 0 . ? C4A C4A C . 0 . ? CMA CMA C . 0 . ? CAA CAA C . 0 . ? CBA CBA C . 0 . ? CGA CGA C . 0 . ? O1A O1A O . 0 . ? O2A O2A O . 0 . ? NB NB N . 0 . ? C1B C1B C . 0 . ? C2B C2B C . 0 . ? C3B C3B C . 0 . ? C4B C4B C . 0 . ? CMB CMB C . 0 . ? CAB CAB C . 0 . ? CBB CBB C . 0 . ? NC NC N . 0 . ? C1C C1C C . 0 . ? C2C C2C C . 0 . ? C3C C3C C . 0 . ? C4C C4C C . 0 . ? CMC CMC C . 0 . ? CAC CAC C . 0 . ? CBC CBC C . 0 . ? ND ND N . 0 . ? C1D C1D C . 0 . ? C2D C2D C . 0 . ? C3D C3D C . 0 . ? C4D C4D C . 0 . ? CMD CMD C . 0 . ? CAD CAD C . 0 . ? CBD CBD C . 0 . ? CGD CGD C . 0 . ? O1D O1D O . 0 . ? O2D O2D O . 0 . ? HHA HHA H . 0 . ? HHB HHB H . 0 . ? HHC HHC H . 0 . ? HHD HHD H . 0 . ? HNA HNA H . 0 . ? HMA1 HMA1 H . 0 . ? HMA2 HMA2 H . 0 . ? HMA3 HMA3 H . 0 . ? HAA1 HAA1 H . 0 . ? HAA2 HAA2 H . 0 . ? HBA1 HBA1 H . 0 . ? HBA2 HBA2 H . 0 . ? H2A H2A H . 0 . ? HMB1 HMB1 H . 0 . ? HMB2 HMB2 H . 0 . ? HMB3 HMB3 H . 0 . ? HAB HAB H . 0 . ? HBB1 HBB1 H . 0 . ? HBB2 HBB2 H . 0 . ? HNC HNC H . 0 . ? HMC1 HMC1 H . 0 . ? HMC2 HMC2 H . 0 . ? HMC3 HMC3 H . 0 . ? HAC HAC H . 0 . ? HBC1 HBC1 H . 0 . ? HBC2 HBC2 H . 0 . ? HMD1 HMD1 H . 0 . ? HMD2 HMD2 H . 0 . ? HMD3 HMD3 H . 0 . ? HAD1 HAD1 H . 0 . ? HAD2 HAD2 H . 0 . ? HBD1 HBD1 H . 0 . ? HBD2 HBD2 H . 0 . ? H2D H2D H . 0 . ? stop_ loop_ _Bond_order _Bond_atom_one_atom_name _Bond_atom_two_atom_name _PDB_bond_atom_one_atom_name _PDB_bond_atom_two_atom_name SING CHA C1A ? ? DOUB CHA C4D ? ? SING CHA HHA ? ? SING CHB C4A ? ? DOUB CHB C1B ? ? SING CHB HHB ? ? SING CHC C4B ? ? DOUB CHC C1C ? ? SING CHC HHC ? ? DOUB CHD C4C ? ? SING CHD C1D ? ? SING CHD HHD ? ? SING NA C1A ? ? SING NA C4A ? ? SING NA HNA ? ? DOUB C1A C2A ? ? SING C2A C3A ? ? SING C2A CAA ? ? DOUB C3A C4A ? ? SING C3A CMA ? ? SING CMA HMA1 ? ? SING CMA HMA2 ? ? SING CMA HMA3 ? ? SING CAA CBA ? ? SING CAA HAA1 ? ? SING CAA HAA2 ? ? SING CBA CGA ? ? SING CBA HBA1 ? ? SING CBA HBA2 ? ? DOUB CGA O1A ? ? SING CGA O2A ? ? SING O2A H2A ? ? SING NB C1B ? ? DOUB NB C4B ? ? SING C1B C2B ? ? DOUB C2B C3B ? ? SING C2B CMB ? ? SING C3B C4B ? ? SING C3B CAB ? ? SING CMB HMB1 ? ? SING CMB HMB2 ? ? SING CMB HMB3 ? ? DOUB CAB CBB ? ? SING CAB HAB ? ? SING CBB HBB1 ? ? SING CBB HBB2 ? ? SING NC C1C ? ? SING NC C4C ? ? SING NC HNC ? ? SING C1C C2C ? ? DOUB C2C C3C ? ? SING C2C CMC ? ? SING C3C C4C ? ? SING C3C CAC ? ? SING CMC HMC1 ? ? SING CMC HMC2 ? ? SING CMC HMC3 ? ? DOUB CAC CBC ? ? SING CAC HAC ? ? SING CBC HBC1 ? ? SING CBC HBC2 ? ? DOUB ND C1D ? ? SING ND C4D ? ? SING C1D C2D ? ? DOUB C2D C3D ? ? SING C2D CMD ? ? SING C3D C4D ? ? SING C3D CAD ? ? SING CMD HMD1 ? ? SING CMD HMD2 ? ? SING CMD HMD3 ? ? SING CAD CBD ? ? SING CAD HAD1 ? ? SING CAD HAD2 ? ? SING CBD CGD ? ? SING CBD HBD1 ? ? SING CBD HBD2 ? ? DOUB CGD O1D ? ? SING CGD O2D ? ? SING O2D H2D ? ? stop_ _Mol_thiol_state . _Sequence_homology_query_date . save_ save_CMO _Saveframe_category ligand _Mol_type "non-polymer (NON-POLYMER)" _Name_common 'CARBON MONOXIDE' _BMRB_code CMO _PDB_code CMO _Molecular_mass 28.010 _Mol_charge 0 _Mol_paramagnetic . _Mol_aromatic no _Details . loop_ _Atom_name _PDB_atom_name _Atom_type _Atom_chirality _Atom_charge _Atom_oxidation_number _Atom_unpaired_electrons C C C . -1 . ? O O O . 1 . ? stop_ loop_ _Bond_order _Bond_atom_one_atom_name _Bond_atom_two_atom_name _PDB_bond_atom_one_atom_name _PDB_bond_atom_two_atom_name TRIP C O ? ? 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 $apoMb 'sperm whale' 9755 Eukaryota Metazoa Physeter catodon stop_ save_ ######################### # Experimental source # ######################### save_experimental_source _Saveframe_category experimental_source loop_ _Mol_label _Production_method _Host_organism_name_common _Genus _Species _Strain _Vector_type _Vector_name $apoMb 'recombinant technology' 'E. Coli' Escherichia coli NCM533 plasmid pCKR102 stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_one _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $MbCO . mM [U-15N] 'potassium phosphate' 0.05 mM . D20 100 % . stop_ save_ save_sample_two _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $MbCO . mM [U-15N] 'potassium phosphate' 0.05 mM . D20 10 % . H2O 90 % . stop_ save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer_one _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model AM-500 _Field_strength 500 _Details . save_ save_NMR_spectrometer_two _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model AMX-600 _Field_strength 600MHz _Details . save_ ############################# # NMR applied experiments # ############################# save__1 _Saveframe_category NMR_applied_experiment _Sample_label . save_ ####################### # Sample conditions # ####################### save_experimental_conditions_MbCO _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 5.6 . n/a temperature 308 . K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chem_shift_reference_MbCO _Saveframe_category chemical_shift_reference _Details ; All 1H chemical shifts were referenced to the VAL68 CGH3 resonance at -2.32 ppm relative to water at 4.68 ppm N15 chemical shifts were indirectly referenced to liquid NH3 by using the H1 frequency of the H2O resonance ; 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 H2O H 1 . ppm 4.68 . . . . . 'liquid ammonia' N 15 . . 0. indirectly . . . . 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_chemical_shift_assignment_MbCO _Saveframe_category assigned_chemical_shifts _Details . loop_ _Sample_label $sample_two stop_ _Sample_conditions_label $experimental_conditions_MbCO _Chem_shift_reference_set_label $chem_shift_reference_MbCO _Mol_system_component_name apomyoglobin _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 VAL HA H 4.31 . 1 2 . 2 VAL HB H 2.15 . 1 3 . 2 VAL HG1 H 0.91 . 2 4 . 2 VAL HG2 H 0.95 . 2 5 . 3 LEU H H 8.35 . 1 6 . 3 LEU HA H 4.51 . 1 7 . 3 LEU HB2 H 0.66 . 1 8 . 3 LEU HB3 H 0.66 . 1 9 . 3 LEU HG H 1.13 . 1 10 . 3 LEU HD1 H -0.37 . 2 11 . 3 LEU HD2 H 0.35 . 2 12 . 3 LEU N N 126.2 . 1 13 . 4 SER H H 9.14 . 1 14 . 4 SER HA H 4.59 . 1 15 . 4 SER N N 117.7 . 1 16 . 5 GLU H H 9.14 . 1 17 . 5 GLU HA H 4.44 . 1 18 . 5 GLU HB2 H 2.06 . 2 19 . 5 GLU HB3 H 2.23 . 2 20 . 5 GLU N N 121.4 . 1 21 . 6 GLY H H 8.66 . 1 22 . 6 GLY HA2 H 3.87 . 1 23 . 6 GLY HA3 H 3.87 . 1 24 . 6 GLY N N 106.0 . 1 25 . 7 GLU H H 7.81 . 1 26 . 7 GLU HA H 3.90 . 1 27 . 7 GLU HB2 H 2.06 . 2 28 . 7 GLU HB3 H 2.33 . 2 29 . 7 GLU N N 122.8 . 1 30 . 8 TRP H H 8.56 . 1 31 . 8 TRP HA H 4.58 . 1 32 . 8 TRP HB2 H 3.12 . 2 33 . 8 TRP HB3 H 3.40 . 2 34 . 8 TRP HD1 H 6.97 . 1 35 . 8 TRP HE1 H 7.44 . 1 36 . 8 TRP HE3 H 9.67 . 1 37 . 8 TRP HZ2 H 7.16 . 1 38 . 8 TRP HZ3 H 7.06 . 1 39 . 8 TRP HH2 H 7.28 . 1 40 . 8 TRP N N 119.0 . 1 41 . 8 TRP NE1 N 129.4 . 1 42 . 9 GLN H H 8.52 . 1 43 . 9 GLN HA H 4.11 . 1 44 . 9 GLN HB2 H 2.26 . 1 45 . 9 GLN HB3 H 2.26 . 1 46 . 9 GLN N N 116.9 . 1 47 . 10 LEU H H 7.63 . 1 48 . 10 LEU HA H 4.26 . 1 49 . 10 LEU HB2 H 1.37 . 1 50 . 10 LEU HB3 H 1.37 . 1 51 . 10 LEU HG H 1.87 . 1 52 . 10 LEU HD1 H 0.77 . 2 53 . 10 LEU HD2 H 0.84 . 2 54 . 10 LEU N N 120.3 . 1 55 . 11 VAL H H 8.00 . 1 56 . 11 VAL HA H 3.70 . 1 57 . 11 VAL HB H 2.66 . 1 58 . 11 VAL HG1 H 0.90 . 2 59 . 11 VAL HG2 H 1.10 . 2 60 . 11 VAL N N 120.3 . 1 61 . 12 LEU H H 8.81 . 1 62 . 12 LEU HA H 4.29 . 1 63 . 12 LEU HB2 H 1.66 . 2 64 . 12 LEU HB3 H 1.97 . 2 65 . 12 LEU HG H 2.10 . 1 66 . 12 LEU HD1 H 0.85 . 2 67 . 12 LEU HD2 H 0.95 . 2 68 . 12 LEU N N 118.1 . 1 69 . 13 HIS H H 8.60 . 1 70 . 13 HIS HA H 4.51 . 1 71 . 13 HIS HB2 H 3.48 . 1 72 . 13 HIS HB3 H 3.48 . 1 73 . 13 HIS HD2 H 7.26 . 1 74 . 13 HIS HE1 H 8.46 . 1 75 . 13 HIS N N 121.2 . 1 76 . 14 VAL H H 7.93 . 1 77 . 14 VAL HA H 3.60 . 1 78 . 14 VAL HB H 2.44 . 1 79 . 14 VAL HG1 H 0.96 . 2 80 . 14 VAL HG2 H 1.19 . 2 81 . 14 VAL N N 118.5 . 1 82 . 15 TRP H H 9.04 . 1 83 . 15 TRP HA H 3.83 . 1 84 . 15 TRP HB2 H 3.20 . 2 85 . 15 TRP HB3 H 3.44 . 2 86 . 15 TRP HD1 H 7.03 . 1 87 . 15 TRP HE1 H 10.27 . 1 88 . 15 TRP HE3 H 7.13 . 1 89 . 15 TRP HZ2 H 7.51 . 3 90 . 15 TRP HZ3 H 6.68 . 3 91 . 15 TRP HH2 H 6.92 . 1 92 . 15 TRP N N 122.2 . 1 93 . 15 TRP NE1 N 128.0 . 1 94 . 16 ALA H H 7.61 . 1 95 . 16 ALA HA H 4.14 . 1 96 . 16 ALA HB H 1.45 . 1 97 . 16 ALA N N 118.6 . 1 98 . 17 LYS H H 7.17 . 1 99 . 17 LYS HA H 3.84 . 1 100 . 17 LYS HB2 H 1.46 . 1 101 . 17 LYS HB3 H 1.46 . 1 102 . 17 LYS N N 115.4 . 1 103 . 18 VAL H H 6.72 . 1 104 . 18 VAL HA H 1.56 . 1 105 . 18 VAL HB H 0.87 . 1 106 . 18 VAL HG1 H -0.47 . 2 107 . 18 VAL HG2 H -0.10 . 2 108 . 18 VAL N N 121.2 . 1 109 . 19 GLU H H 7.44 . 1 110 . 19 GLU HA H 3.49 . 1 111 . 19 GLU HB2 H 1.90 . 1 112 . 19 GLU HB3 H 1.90 . 1 113 . 19 GLU N N 114.4 . 1 114 . 20 ALA H H 6.85 . 1 115 . 20 ALA HA H 4.22 . 1 116 . 20 ALA HB H 1.43 . 1 117 . 20 ALA N N 119.6 . 1 118 . 21 ASP H H 7.55 . 1 119 . 21 ASP HA H 4.84 . 1 120 . 21 ASP HB2 H 2.44 . 2 121 . 21 ASP HB3 H 2.84 . 2 122 . 21 ASP N N 115.5 . 1 123 . 22 VAL H H 8.72 . 1 124 . 22 VAL HA H 3.49 . 1 125 . 22 VAL HB H 2.03 . 1 126 . 22 VAL HG1 H 0.97 . 1 127 . 22 VAL HG2 H 0.97 . 1 128 . 22 VAL N N 129.9 . 1 129 . 23 ALA H H 8.49 . 1 130 . 23 ALA HA H 3.87 . 1 131 . 23 ALA HB H 1.20 . 1 132 . 23 ALA N N 122.2 . 1 133 . 24 GLY H H 8.04 . 1 134 . 24 GLY HA2 H 3.75 . 2 135 . 24 GLY HA3 H 3.83 . 2 136 . 24 GLY N N 105.6 . 1 137 . 25 HIS H H 7.56 . 1 138 . 25 HIS HA H 3.69 . 1 139 . 25 HIS HB2 H 2.50 . 2 140 . 25 HIS HB3 H 2.69 . 2 141 . 25 HIS HD2 H 6.28 . 1 142 . 25 HIS HE1 H 7.91 . 1 143 . 25 HIS N N 116.0 . 1 144 . 26 GLY H H 8.69 . 1 145 . 26 GLY HA2 H 3.10 . 2 146 . 26 GLY HA3 H 3.27 . 2 147 . 26 GLY N N 107.8 . 1 148 . 27 GLN H H 7.93 . 1 149 . 27 GLN HA H 3.42 . 1 150 . 27 GLN HB2 H 1.90 . 1 151 . 27 GLN HB3 H 1.90 . 1 152 . 27 GLN N N 120.3 . 1 153 . 28 ASP H H 7.47 . 1 154 . 28 ASP HA H 4.06 . 1 155 . 28 ASP HB2 H 2.41 . 2 156 . 28 ASP HB3 H 2.57 . 2 157 . 28 ASP N N 117.0 . 1 158 . 29 ILE H H 8.16 . 1 159 . 29 ILE HA H 3.31 . 1 160 . 29 ILE HB H 1.52 . 1 161 . 29 ILE HG12 H 0.97 . 2 162 . 29 ILE HG13 H 0.49 . 2 163 . 29 ILE HD1 H 0.74 . 1 164 . 29 ILE N N 119.8 . 1 165 . 30 LEU H H 7.20 . 1 166 . 30 LEU HA H 3.00 . 1 167 . 30 LEU HB2 H 0.17 . 2 168 . 30 LEU HB3 H 1.03 . 2 169 . 30 LEU HG H 0.86 . 1 170 . 30 LEU HD1 H -0.69 . 2 171 . 30 LEU HD2 H -0.29 . 2 172 . 30 LEU N N 118.2 . 1 173 . 31 ILE H H 7.86 . 1 174 . 31 ILE HA H 3.31 . 1 175 . 31 ILE HB H 1.56 . 1 176 . 31 ILE HG12 H 1.60 . 2 177 . 31 ILE HG13 H 0.74 . 2 178 . 31 ILE HD1 H 0.49 . 1 179 . 31 ILE N N 115.8 . 1 180 . 32 ARG H H 7.72 . 1 181 . 32 ARG HA H 3.88 . 1 182 . 32 ARG N N 118.0 . 1 183 . 33 LEU H H 7.92 . 1 184 . 33 LEU HA H 3.94 . 1 185 . 33 LEU HG H 1.94 . 1 186 . 33 LEU HD1 H 0.60 . 2 187 . 33 LEU HD2 H 0.96 . 2 188 . 33 LEU N N 122.6 . 1 189 . 34 PHE H H 7.93 . 1 190 . 34 PHE HA H 4.36 . 1 191 . 34 PHE HB2 H 2.89 . 2 192 . 34 PHE HB3 H 2.97 . 2 193 . 34 PHE HD1 H 7.00 . 1 194 . 34 PHE HD2 H 7.00 . 1 195 . 34 PHE HE1 H 6.46 . 1 196 . 34 PHE HE2 H 6.46 . 1 197 . 34 PHE HZ H 5.21 . 1 198 . 34 PHE N N 116.4 . 1 199 . 35 LYS H H 8.56 . 1 200 . 35 LYS HA H 4.03 . 1 201 . 35 LYS HB2 H 1.73 . 1 202 . 35 LYS HB3 H 1.73 . 1 203 . 35 LYS N N 116.7 . 1 204 . 36 SER H H 8.15 . 1 205 . 36 SER HA H 4.02 . 1 206 . 36 SER HB2 H 3.41 . 2 207 . 36 SER HB3 H 3.68 . 2 208 . 36 SER N N 113.0 . 1 209 . 37 HIS H H 8.05 . 1 210 . 37 HIS HA H 4.84 . 1 211 . 37 HIS HB2 H 2.94 . 1 212 . 37 HIS HB3 H 2.94 . 1 213 . 37 HIS HD2 H 7.10 . 1 214 . 37 HIS HE1 H 8.15 . 1 215 . 37 HIS N N 117.1 . 1 216 . 39 GLU H H 11.03 . 1 217 . 39 GLU HA H 4.48 . 1 218 . 39 GLU HB2 H 2.74 . 1 219 . 39 GLU HB3 H 2.74 . 1 220 . 39 GLU N N 121.8 . 1 221 . 40 THR H H 8.73 . 1 222 . 40 THR HA H 4.19 . 1 223 . 40 THR HG2 H 1.14 . 1 224 . 40 THR N N 113.3 . 1 225 . 41 LEU H H 7.32 . 1 226 . 41 LEU HA H 3.85 . 1 227 . 41 LEU HB2 H 1.02 . 2 228 . 41 LEU HB3 H 1.81 . 2 229 . 41 LEU HG H 1.24 . 1 230 . 41 LEU HD1 H -0.08 . 2 231 . 41 LEU HD2 H 0.47 . 2 232 . 41 LEU N N 123.4 . 1 233 . 42 GLU H H 7.22 . 1 234 . 42 GLU HA H 4.04 . 1 235 . 42 GLU N N 113.0 . 1 236 . 43 LYS H H 7.69 . 1 237 . 43 LYS HA H 4.07 . 1 238 . 43 LYS HB2 H 2.28 . 2 239 . 43 LYS HB3 H 2.90 . 2 240 . 43 LYS N N 113.2 . 1 241 . 44 PHE H H 8.32 . 1 242 . 44 PHE HA H 5.01 . 1 243 . 44 PHE HB2 H 2.69 . 2 244 . 44 PHE HB3 H 3.29 . 2 245 . 44 PHE HD1 H 7.29 . 1 246 . 44 PHE HD2 H 7.29 . 1 247 . 44 PHE HE1 H 6.07 . 1 248 . 44 PHE HE2 H 6.07 . 1 249 . 44 PHE HZ H 4.73 . 1 250 . 44 PHE N N 118.8 . 1 251 . 45 ASP H H 8.83 . 1 252 . 45 ASP HA H 4.28 . 1 253 . 45 ASP HB2 H 2.74 . 1 254 . 45 ASP HB3 H 2.74 . 1 255 . 45 ASP N N 126.4 . 1 256 . 46 ARG H H 8.98 . 1 257 . 46 ARG HA H 4.12 . 1 258 . 46 ARG HB2 H 1.12 . 1 259 . 46 ARG HB3 H 1.12 . 1 260 . 46 ARG N N 114.0 . 1 261 . 47 PHE H H 7.07 . 1 262 . 47 PHE HA H 5.11 . 1 263 . 47 PHE HB2 H 2.29 . 2 264 . 47 PHE HB3 H 3.27 . 2 265 . 47 PHE HD1 H 6.76 . 1 266 . 47 PHE HD2 H 6.76 . 1 267 . 47 PHE HE1 H 6.49 . 1 268 . 47 PHE HE2 H 6.49 . 1 269 . 47 PHE HZ H 6.58 . 1 270 . 47 PHE N N 112.3 . 1 271 . 48 LYS H H 7.59 . 1 272 . 48 LYS HA H 3.91 . 1 273 . 48 LYS N N 116.6 . 1 274 . 49 HIS HA H 3.91 . 1 275 . 49 HIS HB2 H 3.04 . 2 276 . 49 HIS HB3 H 3.16 . 2 277 . 49 HIS HD2 H 7.17 . 1 278 . 49 HIS HE1 H 8.32 . 1 279 . 50 LEU H H 7.54 . 1 280 . 50 LEU HA H 4.04 . 1 281 . 50 LEU HB2 H 1.92 . 2 282 . 50 LEU HB3 H 0.76 . 2 283 . 50 LEU HG H 1.15 . 1 284 . 50 LEU HD1 H 0.63 . 2 285 . 50 LEU HD2 H 0.87 . 2 286 . 50 LEU N N 123.9 . 1 287 . 51 LYS H H 8.23 . 1 288 . 51 LYS HA H 4.28 . 1 289 . 51 LYS HB2 H 1.90 . 1 290 . 51 LYS HB3 H 1.90 . 1 291 . 51 LYS N N 119.1 . 1 292 . 52 THR H H 7.58 . 1 293 . 52 THR HG2 H 1.18 . 1 294 . 52 THR N N 107.1 . 1 295 . 54 ALA H H 8.33 . 1 296 . 54 ALA HA H 3.94 . 1 297 . 54 ALA HB H 1.34 . 1 298 . 54 ALA N N 120.1 . 1 299 . 55 GLU H H 7.66 . 1 300 . 55 GLU HA H 3.92 . 1 301 . 55 GLU HB2 H 1.94 . 1 302 . 55 GLU HB3 H 1.94 . 1 303 . 55 GLU N N 117.9 . 1 304 . 56 MET H H 8.04 . 1 305 . 56 MET HA H 3.82 . 1 306 . 56 MET HB2 H 2.10 . 2 307 . 56 MET HB3 H 1.75 . 2 308 . 56 MET HE H 1.75 . 1 309 . 56 MET N N 118.2 . 1 310 . 57 LYS H H 8.49 . 1 311 . 57 LYS HA H 3.63 . 1 312 . 57 LYS HB2 H 1.72 . 1 313 . 57 LYS HB3 H 1.72 . 1 314 . 57 LYS N N 118.5 . 1 315 . 58 ALA H H 7.08 . 1 316 . 58 ALA HA H 4.23 . 1 317 . 58 ALA HB H 1.40 . 1 318 . 58 ALA N N 117.5 . 1 319 . 59 SER H H 6.81 . 1 320 . 59 SER HA H 4.44 . 1 321 . 59 SER HB2 H 3.87 . 2 322 . 59 SER HB3 H 3.96 . 2 323 . 59 SER N N 110.9 . 1 324 . 60 GLU H H 9.13 . 1 325 . 60 GLU HA H 4.06 . 1 326 . 60 GLU HB2 H 2.06 . 2 327 . 60 GLU HB3 H 2.34 . 2 328 . 60 GLU N N 134.5 . 1 329 . 61 ASP H H 8.35 . 1 330 . 61 ASP HA H 4.48 . 1 331 . 61 ASP HB2 H 2.66 . 1 332 . 61 ASP HB3 H 2.66 . 1 333 . 61 ASP N N 119.0 . 1 334 . 62 LEU H H 8.08 . 1 335 . 62 LEU HA H 3.28 . 1 336 . 62 LEU HB2 H 0.72 . 2 337 . 62 LEU HB3 H 1.63 . 2 338 . 62 LEU HG H 0.85 . 1 339 . 62 LEU HD1 H -0.14 . 2 340 . 62 LEU HD2 H 0.47 . 2 341 . 62 LEU N N 123.7 . 1 342 . 63 LYS H H 7.12 . 1 343 . 63 LYS HA H 3.56 . 1 344 . 63 LYS HB2 H 1.73 . 1 345 . 63 LYS HB3 H 1.73 . 1 346 . 63 LYS N N 119.8 . 1 347 . 64 LYS H H 8.13 . 1 348 . 64 LYS HA H 3.85 . 1 349 . 64 LYS HB2 H 1.94 . 1 350 . 64 LYS HB3 H 1.94 . 1 351 . 64 LYS N N 117.6 . 1 352 . 65 HIS H H 7.97 . 1 353 . 65 HIS HA H 4.17 . 1 354 . 65 HIS HB2 H 2.41 . 2 355 . 65 HIS HB3 H 2.91 . 2 356 . 65 HIS HD2 H 4.92 . 1 357 . 65 HIS HE1 H 7.13 . 1 358 . 65 HIS N N 120.1 . 1 359 . 66 GLY H H 8.06 . 1 360 . 66 GLY HA2 H 2.61 . 2 361 . 66 GLY HA3 H 3.24 . 2 362 . 66 GLY N N 106.1 . 1 363 . 67 VAL H H 7.32 . 1 364 . 67 VAL HA H 3.38 . 1 365 . 67 VAL HB H 2.30 . 1 366 . 67 VAL HG1 H 0.87 . 2 367 . 67 VAL HG2 H 0.95 . 2 368 . 67 VAL N N 120.4 . 1 369 . 68 THR H H 7.89 . 1 370 . 68 THR HA H 3.84 . 1 371 . 68 THR HB H 4.01 . 1 372 . 68 THR HG2 H 1.50 . 1 373 . 68 THR N N 123.1 . 1 374 . 69 VAL H H 7.66 . 1 375 . 69 VAL HA H 3.26 . 1 376 . 69 VAL HB H 0.86 . 1 377 . 69 VAL HG1 H -0.59 . 2 378 . 69 VAL HG2 H -2.32 . 2 379 . 69 VAL N N 121.2 . 1 380 . 70 LEU H H 7.91 . 1 381 . 70 LEU HA H 4.25 . 1 382 . 70 LEU HB2 H 1.47 . 1 383 . 70 LEU HB3 H 1.47 . 1 384 . 70 LEU HG H 1.76 . 1 385 . 70 LEU HD1 H 0.62 . 2 386 . 70 LEU HD2 H 0.76 . 2 387 . 70 LEU N N 116.4 . 1 388 . 71 THR H H 8.79 . 1 389 . 71 THR HA H 4.18 . 1 390 . 71 THR HB H 4.46 . 1 391 . 71 THR HG2 H 1.43 . 1 392 . 71 THR N N 117.7 . 1 393 . 72 ALA H H 7.78 . 1 394 . 72 ALA HA H 4.62 . 1 395 . 72 ALA HB H 2.40 . 1 396 . 72 ALA N N 124.8 . 1 397 . 73 LEU H H 8.68 . 1 398 . 73 LEU HA H 4.13 . 1 399 . 73 LEU HB2 H 1.71 . 2 400 . 73 LEU HB3 H 2.03 . 2 401 . 73 LEU HG H 1.15 . 1 402 . 73 LEU HD1 H 0.42 . 2 403 . 73 LEU HD2 H 0.90 . 2 404 . 73 LEU N N 118.1 . 1 405 . 74 GLY H H 9.02 . 1 406 . 74 GLY HA2 H 2.64 . 2 407 . 74 GLY HA3 H 4.02 . 2 408 . 74 GLY N N 107.6 . 1 409 . 75 ALA H H 7.56 . 1 410 . 75 ALA HA H 4.06 . 1 411 . 75 ALA HB H 1.62 . 1 412 . 75 ALA N N 121.4 . 1 413 . 76 ILE H H 7.26 . 1 414 . 76 ILE HA H 3.58 . 1 415 . 76 ILE HB H 2.12 . 1 416 . 76 ILE HG12 H 0.82 . 1 417 . 76 ILE HG13 H 0.82 . 1 418 . 76 ILE N N 116.4 . 1 419 . 77 LEU H H 8.61 . 1 420 . 77 LEU HA H 4.06 . 1 421 . 77 LEU HB2 H 1.03 . 2 422 . 77 LEU HB3 H 1.96 . 2 423 . 77 LEU HG H 1.45 . 1 424 . 77 LEU HD1 H -0.14 . 2 425 . 77 LEU HD2 H 0.79 . 2 426 . 77 LEU N N 121.9 . 1 427 . 78 LYS H H 7.86 . 1 428 . 78 LYS HA H 3.84 . 1 429 . 78 LYS HB2 H 1.60 . 1 430 . 78 LYS HB3 H 1.60 . 1 431 . 78 LYS N N 113.3 . 1 432 . 79 LYS H H 7.30 . 1 433 . 79 LYS HA H 4.08 . 1 434 . 79 LYS HB2 H 1.83 . 2 435 . 79 LYS HB3 H 1.97 . 2 436 . 79 LYS N N 114.7 . 1 437 . 80 LYS H H 7.96 . 1 438 . 80 LYS HA H 0.92 . 1 439 . 80 LYS N N 120.0 . 1 440 . 81 GLY H H 9.31 . 1 441 . 81 GLY HA2 H 3.24 . 2 442 . 81 GLY HA3 H 4.11 . 2 443 . 81 GLY N N 106.1 . 1 444 . 82 HIS H H 7.36 . 1 445 . 82 HIS HA H 4.84 . 1 446 . 82 HIS HB2 H 3.07 . 2 447 . 82 HIS HB3 H 3.35 . 2 448 . 82 HIS HD2 H 7.14 . 1 449 . 82 HIS HE1 H 8.51 . 1 450 . 82 HIS N N 122.3 . 1 451 . 83 HIS H H 6.82 . 1 452 . 83 HIS HA H 5.32 . 1 453 . 83 HIS HB2 H 2.78 . 2 454 . 83 HIS HB3 H 3.74 . 2 455 . 83 HIS HD2 H 6.69 . 1 456 . 83 HIS HE1 H 7.63 . 1 457 . 83 HIS N N 114.2 . 1 458 . 84 GLU H H 8.75 . 1 459 . 84 GLU HA H 3.97 . 1 460 . 84 GLU HB2 H 1.99 . 1 461 . 84 GLU HB3 H 1.99 . 1 462 . 84 GLU N N 123.8 . 1 463 . 85 ALA H H 8.52 . 1 464 . 85 ALA HA H 4.03 . 1 465 . 85 ALA HB H 1.38 . 1 466 . 85 ALA N N 118.2 . 1 467 . 86 GLU H H 8.40 . 1 468 . 86 GLU HA H 4.06 . 1 469 . 86 GLU HB2 H 2.23 . 1 470 . 86 GLU HB3 H 2.23 . 1 471 . 86 GLU N N 117.8 . 1 472 . 87 LEU H H 8.18 . 1 473 . 87 LEU HA H 3.97 . 1 474 . 87 LEU HB2 H 2.37 . 1 475 . 87 LEU HB3 H 2.37 . 1 476 . 87 LEU N N 124.8 . 1 477 . 89 PRO HA H 4.29 . 1 478 . 89 PRO HD2 H 3.51 . 1 479 . 89 PRO HD3 H 3.51 . 1 480 . 90 LEU H H 6.34 . 1 481 . 90 LEU HA H 3.77 . 1 482 . 90 LEU HB2 H 1.18 . 2 483 . 90 LEU HB3 H 1.47 . 2 484 . 90 LEU HG H 0.58 . 1 485 . 90 LEU HD1 H 0.29 . 2 486 . 90 LEU HD2 H 0.42 . 2 487 . 90 LEU N N 119.7 . 1 488 . 91 ALA H H 8.34 . 1 489 . 91 ALA HA H 3.44 . 1 490 . 91 ALA HB H 1.19 . 1 491 . 91 ALA N N 120.8 . 1 492 . 92 GLN H H 7.86 . 1 493 . 92 GLN HA H 3.56 . 1 494 . 92 GLN HB2 H 1.90 . 2 495 . 92 GLN HB3 H 2.13 . 2 496 . 92 GLN N N 114.4 . 1 497 . 93 SER H H 7.96 . 1 498 . 93 SER HA H 3.54 . 1 499 . 93 SER N N 115.4 . 1 500 . 94 HIS H H 7.70 . 1 501 . 94 HIS HA H 2.55 . 1 502 . 94 HIS HB2 H 1.77 . 1 503 . 94 HIS HB3 H 1.77 . 1 504 . 94 HIS HD1 H 9.38 . 1 505 . 94 HIS HD2 H 1.11 . 1 506 . 94 HIS HE1 H 1.63 . 1 507 . 94 HIS N N 121.5 . 1 508 . 94 HIS ND1 N 64.9 . 1 509 . 95 ALA H H 7.79 . 1 510 . 95 ALA HA H 3.11 . 1 511 . 95 ALA HB H 0.30 . 1 512 . 95 ALA N N 119.3 . 1 513 . 96 THR H H 6.85 . 1 514 . 96 THR HA H 3.85 . 1 515 . 96 THR HB H 4.01 . 1 516 . 96 THR HG2 H 0.99 . 1 517 . 96 THR N N 103.0 . 1 518 . 97 LYS H H 7.00 . 1 519 . 97 LYS HA H 4.23 . 1 520 . 97 LYS HB2 H 0.99 . 2 521 . 97 LYS HB3 H 1.18 . 2 522 . 97 LYS N N 121.3 . 1 523 . 98 HIS H H 7.14 . 1 524 . 98 HIS HA H 4.24 . 1 525 . 98 HIS HB2 H 1.65 . 2 526 . 98 HIS HB3 H 2.75 . 2 527 . 98 HIS HD2 H 2.34 . 1 528 . 98 HIS HE1 H 8.54 . 1 529 . 98 HIS N N 114.7 . 1 530 . 99 LYS H H 6.19 . 1 531 . 99 LYS HA H 3.27 . 1 532 . 99 LYS HB2 H 1.92 . 1 533 . 99 LYS HB3 H 1.92 . 1 534 . 99 LYS N N 112.8 . 1 535 . 100 ILE H H 7.92 . 1 536 . 100 ILE HA H 4.40 . 1 537 . 100 ILE HB H 1.40 . 1 538 . 100 ILE N N 120.1 . 1 539 . 101 PRO HA H 4.44 . 1 540 . 102 ILE H H 9.06 . 1 541 . 102 ILE HA H 3.56 . 1 542 . 102 ILE HB H 1.84 . 1 543 . 102 ILE HG12 H 1.23 . 2 544 . 102 ILE HG13 H 1.30 . 2 545 . 102 ILE HG2 H 0.77 . 1 546 . 102 ILE HD1 H 0.22 . 1 547 . 102 ILE N N 123.8 . 1 548 . 103 LYS H H 8.69 . 1 549 . 103 LYS HA H 3.94 . 1 550 . 103 LYS HB2 H 1.43 . 2 551 . 103 LYS HB3 H 1.79 . 2 552 . 103 LYS N N 119.6 . 1 553 . 104 TYR H H 7.67 . 1 554 . 104 TYR HA H 4.52 . 1 555 . 104 TYR HD1 H 7.30 . 1 556 . 104 TYR HD2 H 7.30 . 1 557 . 104 TYR HE1 H 7.20 . 1 558 . 104 TYR HE2 H 7.20 . 1 559 . 104 TYR N N 115.5 . 1 560 . 105 LEU H H 8.06 . 1 561 . 105 LEU HA H 5.03 . 1 562 . 105 LEU HB2 H 2.41 . 1 563 . 105 LEU HB3 H 2.41 . 1 564 . 105 LEU HG H 1.90 . 1 565 . 105 LEU HD1 H 0.73 . 2 566 . 105 LEU HD2 H 1.08 . 2 567 . 105 LEU N N 120.0 . 1 568 . 107 PHE H H 7.81 . 1 569 . 107 PHE HA H 4.81 . 1 570 . 107 PHE HB2 H 2.94 . 2 571 . 107 PHE HB3 H 3.52 . 2 572 . 107 PHE HD1 H 6.81 . 1 573 . 107 PHE HD2 H 6.81 . 1 574 . 107 PHE HE1 H 7.44 . 1 575 . 107 PHE HE2 H 7.44 . 1 576 . 107 PHE HZ H 7.44 . 1 577 . 107 PHE N N 118.5 . 1 578 . 108 ILE H H 8.74 . 1 579 . 108 ILE HA H 4.39 . 1 580 . 108 ILE HB H 2.16 . 1 581 . 108 ILE HG12 H 1.39 . 2 582 . 108 ILE HG13 H 1.46 . 2 583 . 108 ILE HG2 H 1.02 . 1 584 . 108 ILE HD1 H 0.31 . 1 585 . 108 ILE N N 119.1 . 1 586 . 109 SER H H 7.89 . 1 587 . 109 SER HA H 4.50 . 1 588 . 109 SER N N 120.8 . 1 589 . 110 GLU H H 7.92 . 1 590 . 110 GLU HA H 4.12 . 1 591 . 110 GLU HB2 H 2.40 . 1 592 . 110 GLU HB3 H 2.40 . 1 593 . 110 GLU N N 120.8 . 1 594 . 111 ALA H H 7.77 . 1 595 . 111 ALA HA H 4.15 . 1 596 . 111 ALA HB H 1.60 . 1 597 . 111 ALA N N 122.2 . 1 598 . 112 ILE H H 8.40 . 1 599 . 112 ILE HA H 3.48 . 1 600 . 112 ILE N N 117.8 . 1 601 . 113 ILE H H 7.87 . 1 602 . 113 ILE HA H 3.72 . 1 603 . 113 ILE HB H 2.25 . 1 604 . 113 ILE HG12 H 1.14 . 1 605 . 113 ILE HG13 H 1.14 . 1 606 . 113 ILE N N 118.3 . 1 607 . 114 HIS H H 8.46 . 1 608 . 114 HIS HA H 4.27 . 1 609 . 114 HIS HB2 H 3.22 . 2 610 . 114 HIS HB3 H 3.30 . 2 611 . 114 HIS HD2 H 6.82 . 1 612 . 114 HIS HE1 H 8.00 . 1 613 . 114 HIS N N 117.9 . 1 614 . 115 VAL H H 8.43 . 1 615 . 115 VAL HA H 3.61 . 1 616 . 115 VAL HB H 2.02 . 1 617 . 115 VAL HG1 H 0.98 . 1 618 . 115 VAL HG2 H 0.98 . 1 619 . 115 VAL N N 120.3 . 1 620 . 116 LEU H H 8.39 . 1 621 . 116 LEU HA H 3.75 . 1 622 . 116 LEU HB2 H 1.34 . 1 623 . 116 LEU HB3 H 1.34 . 1 624 . 116 LEU HG H 1.77 . 1 625 . 116 LEU HD1 H 0.51 . 2 626 . 116 LEU HD2 H 0.69 . 2 627 . 116 LEU N N 120.4 . 1 628 . 117 HIS H H 8.13 . 1 629 . 117 HIS HA H 4.32 . 1 630 . 117 HIS HB2 H 3.34 . 1 631 . 117 HIS HB3 H 3.34 . 1 632 . 117 HIS HD2 H 7.45 . 1 633 . 117 HIS HE1 H 8.46 . 1 634 . 117 HIS N N 115.7 . 1 635 . 118 SER H H 8.00 . 1 636 . 118 SER HA H 3.90 . 1 637 . 118 SER HB2 H 3.74 . 1 638 . 118 SER HB3 H 3.74 . 1 639 . 118 SER N N 112.6 . 1 640 . 119 ARG H H 8.13 . 1 641 . 119 ARG HA H 3.87 . 1 642 . 119 ARG HB2 H 1.14 . 1 643 . 119 ARG HB3 H 1.14 . 1 644 . 119 ARG HD2 H 2.55 . 1 645 . 119 ARG HD3 H 2.55 . 1 646 . 119 ARG HE H 6.66 . 1 647 . 119 ARG N N 115.8 . 1 648 . 119 ARG NE N 96.9 . 1 649 . 120 HIS H H 7.40 . 1 650 . 120 HIS HA H 5.23 . 1 651 . 120 HIS HB2 H 3.14 . 2 652 . 120 HIS HB3 H 3.24 . 2 653 . 120 HIS HD2 H 6.92 . 1 654 . 120 HIS HE1 H 8.61 . 1 655 . 120 HIS N N 114.6 . 1 656 . 123 ASP H H 7.58 . 1 657 . 123 ASP HA H 5.02 . 1 658 . 123 ASP HB2 H 2.40 . 2 659 . 123 ASP HB3 H 2.80 . 2 660 . 123 ASP N N 117.7 . 1 661 . 124 PHE H H 8.11 . 1 662 . 124 PHE HA H 5.01 . 1 663 . 124 PHE HB2 H 2.71 . 2 664 . 124 PHE HB3 H 3.36 . 2 665 . 124 PHE HD1 H 7.10 . 1 666 . 124 PHE HD2 H 7.10 . 1 667 . 124 PHE HE1 H 7.32 . 1 668 . 124 PHE HE2 H 7.32 . 1 669 . 124 PHE HZ H 7.19 . 1 670 . 124 PHE N N 123.3 . 1 671 . 125 GLY H H 8.00 . 1 672 . 125 GLY HA2 H 3.85 . 2 673 . 125 GLY HA3 H 4.31 . 2 674 . 125 GLY N N 109.6 . 1 675 . 126 ALA H H 8.51 . 1 676 . 126 ALA HA H 3.77 . 1 677 . 126 ALA HB H 1.39 . 1 678 . 126 ALA N N 121.0 . 1 679 . 127 ASP H H 8.60 . 1 680 . 127 ASP HA H 4.29 . 1 681 . 127 ASP HB2 H 2.53 . 2 682 . 127 ASP HB3 H 2.66 . 2 683 . 127 ASP N N 117.4 . 1 684 . 128 ALA H H 8.24 . 1 685 . 128 ALA HA H 3.97 . 1 686 . 128 ALA HB H 1.52 . 1 687 . 128 ALA N N 126.5 . 1 688 . 129 GLN H H 8.55 . 1 689 . 129 GLN HA H 3.41 . 1 690 . 129 GLN HB2 H 1.73 . 1 691 . 129 GLN HB3 H 1.73 . 1 692 . 129 GLN N N 118.4 . 1 693 . 130 GLY H H 8.08 . 1 694 . 130 GLY HA2 H 3.87 . 1 695 . 130 GLY HA3 H 3.87 . 1 696 . 130 GLY N N 106.8 . 1 697 . 131 ALA H H 7.77 . 1 698 . 131 ALA HA H 3.93 . 1 699 . 131 ALA HB H 1.51 . 1 700 . 131 ALA N N 124.4 . 1 701 . 132 MET H H 8.54 . 1 702 . 132 MET HA H 4.47 . 1 703 . 132 MET HB2 H 2.36 . 1 704 . 132 MET HB3 H 2.36 . 1 705 . 132 MET HE H 2.25 . 1 706 . 132 MET N N 116.5 . 1 707 . 133 ASN H H 8.75 . 1 708 . 133 ASN HA H 4.47 . 1 709 . 133 ASN HB2 H 2.90 . 2 710 . 133 ASN HB3 H 2.99 . 2 711 . 133 ASN HD21 H 6.93 . 2 712 . 133 ASN HD22 H 7.39 . 2 713 . 133 ASN N N 117.6 . 1 714 . 133 ASN ND2 N 112.32 . 1 715 . 134 LYS H H 7.94 . 1 716 . 134 LYS HA H 4.06 . 1 717 . 134 LYS HB2 H 1.84 . 1 718 . 134 LYS HB3 H 1.84 . 1 719 . 134 LYS N N 120.1 . 1 720 . 135 ALA H H 8.41 . 1 721 . 135 ALA HA H 3.85 . 1 722 . 135 ALA HB H 1.40 . 1 723 . 135 ALA N N 122.6 . 1 724 . 136 LEU H H 8.48 . 1 725 . 136 LEU HA H 4.39 . 1 726 . 136 LEU HB2 H 1.63 . 1 727 . 136 LEU HB3 H 1.63 . 1 728 . 136 LEU N N 116.1 . 1 729 . 137 GLU H H 8.47 . 1 730 . 137 GLU HA H 3.87 . 1 731 . 137 GLU HB2 H 2.22 . 1 732 . 137 GLU HB3 H 2.22 . 1 733 . 137 GLU N N 123.2 . 1 734 . 138 LEU H H 8.30 . 1 735 . 138 LEU HA H 4.08 . 1 736 . 138 LEU HB2 H 1.56 . 1 737 . 138 LEU HB3 H 1.56 . 1 738 . 138 LEU HG H 1.80 . 1 739 . 138 LEU HD1 H 1.10 . 2 740 . 138 LEU HD2 H 1.23 . 2 741 . 138 LEU N N 122.0 . 1 742 . 139 PHE H H 7.87 . 1 743 . 139 PHE HA H 4.04 . 1 744 . 139 PHE HB2 H 3.29 . 2 745 . 139 PHE HB3 H 3.50 . 2 746 . 139 PHE HD1 H 7.09 . 1 747 . 139 PHE HD2 H 7.09 . 1 748 . 139 PHE HE1 H 7.14 . 1 749 . 139 PHE HE2 H 7.14 . 1 750 . 139 PHE HZ H 6.99 . 1 751 . 139 PHE N N 118.3 . 1 752 . 140 ARG H H 8.46 . 1 753 . 140 ARG HA H 3.47 . 1 754 . 140 ARG HB2 H 1.61 . 1 755 . 140 ARG HB3 H 1.61 . 1 756 . 140 ARG N N 116.9 . 1 757 . 141 LYS H H 8.78 . 1 758 . 141 LYS HA H 3.90 . 1 759 . 141 LYS HB2 H 2.00 . 1 760 . 141 LYS HB3 H 2.00 . 1 761 . 141 LYS N N 121.6 . 1 762 . 142 ASP H H 8.47 . 1 763 . 142 ASP HA H 3.89 . 1 764 . 142 ASP HB2 H 2.52 . 2 765 . 142 ASP HB3 H 2.71 . 2 766 . 142 ASP N N 122.1 . 1 767 . 143 ILE H H 8.30 . 1 768 . 143 ILE HA H 3.37 . 1 769 . 143 ILE HB H 1.27 . 1 770 . 143 ILE HG12 H 0.56 . 2 771 . 143 ILE HG13 H 0.73 . 2 772 . 143 ILE HG2 H -0.03 . 1 773 . 143 ILE HD1 H -0.13 . 1 774 . 143 ILE N N 122.7 . 1 775 . 144 ALA H H 8.16 . 1 776 . 144 ALA HA H 3.58 . 1 777 . 144 ALA HB H 1.39 . 1 778 . 144 ALA N N 123.2 . 1 779 . 145 ALA H H 7.65 . 1 780 . 145 ALA HA H 4.14 . 1 781 . 145 ALA HB H 1.55 . 1 782 . 145 ALA N N 120.6 . 1 783 . 146 LYS H H 7.53 . 1 784 . 146 LYS HA H 4.13 . 1 785 . 146 LYS HB2 H 1.96 . 1 786 . 146 LYS HB3 H 1.96 . 1 787 . 146 LYS N N 119.0 . 1 788 . 147 TYR H H 9.03 . 1 789 . 147 TYR HA H 3.87 . 1 790 . 147 TYR HB2 H 3.06 . 2 791 . 147 TYR HB3 H 3.48 . 2 792 . 147 TYR HD1 H 6.60 . 1 793 . 147 TYR HD2 H 6.60 . 1 794 . 147 TYR HE1 H 6.41 . 1 795 . 147 TYR HE2 H 6.41 . 1 796 . 147 TYR N N 121.4 . 1 797 . 148 LYS H H 7.64 . 1 798 . 148 LYS HA H 4.06 . 1 799 . 148 LYS HB2 H 1.94 . 1 800 . 148 LYS HB3 H 1.94 . 1 801 . 148 LYS N N 117.7 . 1 802 . 149 GLU H H 7.64 . 1 803 . 149 GLU HA H 4.01 . 1 804 . 149 GLU HB2 H 2.19 . 1 805 . 149 GLU HB3 H 2.19 . 1 806 . 149 GLU N N 121.0 . 1 807 . 150 LEU H H 7.70 . 1 808 . 150 LEU HA H 4.18 . 1 809 . 150 LEU HB2 H 1.40 . 2 810 . 150 LEU HB3 H 1.74 . 2 811 . 150 LEU HG H 1.74 . 1 812 . 150 LEU HD1 H 0.53 . 2 813 . 150 LEU HD2 H 0.76 . 2 814 . 150 LEU N N 117.1 . 1 815 . 151 GLY H H 7.75 . 1 816 . 151 GLY HA2 H 3.69 . 2 817 . 151 GLY HA3 H 4.04 . 2 818 . 151 GLY N N 107.0 . 1 819 . 152 TYR H H 7.96 . 1 820 . 152 TYR HA H 4.53 . 1 821 . 152 TYR HB2 H 2.43 . 1 822 . 152 TYR HB3 H 2.43 . 1 823 . 152 TYR HD1 H 6.47 . 1 824 . 152 TYR HD2 H 6.47 . 1 825 . 152 TYR HE1 H 6.41 . 1 826 . 152 TYR HE2 H 6.41 . 1 827 . 152 TYR N N 121.4 . 1 828 . 153 GLN H H 8.19 . 1 829 . 153 GLN HA H 4.06 . 1 830 . 153 GLN HB2 H 1.81 . 2 831 . 153 GLN HB3 H 2.01 . 2 832 . 153 GLN HG2 H 2.26 . 1 833 . 153 GLN HG3 H 2.26 . 1 834 . 153 GLN N N 124.3 . 1 835 . 154 GLY H H 6.53 . 1 836 . 154 GLY HA2 H 3.43 . 2 837 . 154 GLY HA3 H 3.50 . 2 838 . 154 GLY N N 113.1 . 1 stop_ save_