data_4342 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Assignment of the 1H, 15N, and 13C Resonances of the C-terminal Domain of Frataxin, the Protein Involved in Friedreich Ataxia. ; _BMRB_accession_number 4342 _BMRB_flat_file_name bmr4342.str _Entry_type new _Submission_date 1999-05-04 _Accession_date 1999-05-04 _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 Musco Giovanna . . 2 'de Tommasi' Tina . . 3 Stier Gunter . . 4 Kolmerer Bernhard . . 5 Bottomle Matthew . . 6 Adinolfi Salvatore . . 7 Musket Frederick . . 8 Gibson Toby . . 9 Frenkiel Tom . . 10 Pastore Annalisa . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 721 "13C chemical shifts" 485 "15N chemical shifts" 125 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2000-01-05 original author . stop_ save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full ; Musco, G., de Tommasi, T., Stier, G., Kolmerer, B., Bottomle, M., Adinolfi, S., Musket, F., Gibson, T., Frenkiel, T., and Pastore, A., "Assignment of the 1H, 15N, and 13C Resonances of the C-terminal Domain of Frataxin, the Protein Responsible for Friedreich Ataxia," J. Biomol. NMR 15, 87-88 (1999). ; _Citation_title ; Assignment of the 1H, 15N, and 13C Resonances of the C-terminal Domain of Frataxin, the Protein Involved in Friedreich Ataxia. ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code 20016853 _PubMed_ID ? loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Musco Giovanna . . 2 'de Tommasi' Tina . . 3 Stier Gunter . . 4 Kolmerer Bernhard . . 5 Bottomle Matthew . . 6 Adinolfi Salvatore . . 7 Musket Frederick . . 8 Gibson Toby . . 9 Frenkiel Tom . . 10 Pastore Annalisa . . stop_ _Journal_abbreviation 'J. Biomol. NMR' _Journal_name_full 'Journal of Biomolecular NMR' _Journal_volume 15 _Journal_issue . _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 87 _Page_last 88 _Year 1999 _Details . loop_ _Keyword 'Friedreich ataxia' Frataxin stop_ save_ ################################## # Molecular system description # ################################## save_system_Frataxin _Saveframe_category molecular_system _Mol_system_name Frataxin _Abbreviation_common Frataxin _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label Frataxin $Frataxin stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state monomer _System_paramagnetic no _System_thiol_state 'not present' loop_ _Biological_function 'mitochondrial protein' stop_ _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_Frataxin _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common Frataxin _Abbreviation_common Frataxin _Molecular_mass 14683 _Mol_thiol_state . _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 122 _Mol_residue_sequence ; PMDETTYERLAEETLDSLAE FFEDLADKPYTFEDYDVSFG SGVLTVKLGGDLGTYVINKQ TPNKQIWLSSPSSGPKRYDW TGKNWVYSHDGVSLHELLAA ELTKALKTKLDLSSLAYSGK DA ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 89 PRO 2 90 MET 3 91 ASP 4 92 GLU 5 93 THR 6 94 THR 7 95 TYR 8 96 GLU 9 97 ARG 10 98 LEU 11 99 ALA 12 100 GLU 13 101 GLU 14 102 THR 15 103 LEU 16 104 ASP 17 105 SER 18 106 LEU 19 107 ALA 20 108 GLU 21 109 PHE 22 110 PHE 23 111 GLU 24 112 ASP 25 113 LEU 26 114 ALA 27 115 ASP 28 116 LYS 29 117 PRO 30 118 TYR 31 119 THR 32 120 PHE 33 121 GLU 34 122 ASP 35 123 TYR 36 124 ASP 37 125 VAL 38 126 SER 39 127 PHE 40 128 GLY 41 129 SER 42 130 GLY 43 131 VAL 44 132 LEU 45 133 THR 46 134 VAL 47 135 LYS 48 136 LEU 49 137 GLY 50 138 GLY 51 139 ASP 52 140 LEU 53 141 GLY 54 142 THR 55 143 TYR 56 144 VAL 57 145 ILE 58 146 ASN 59 147 LYS 60 148 GLN 61 149 THR 62 150 PRO 63 151 ASN 64 152 LYS 65 153 GLN 66 154 ILE 67 155 TRP 68 156 LEU 69 157 SER 70 158 SER 71 159 PRO 72 160 SER 73 161 SER 74 162 GLY 75 163 PRO 76 164 LYS 77 165 ARG 78 166 TYR 79 167 ASP 80 168 TRP 81 169 THR 82 170 GLY 83 171 LYS 84 172 ASN 85 173 TRP 86 174 VAL 87 175 TYR 88 176 SER 89 177 HIS 90 178 ASP 91 179 GLY 92 180 VAL 93 181 SER 94 182 LEU 95 183 HIS 96 184 GLU 97 185 LEU 98 186 LEU 99 187 ALA 100 188 ALA 101 189 GLU 102 190 LEU 103 191 THR 104 192 LYS 105 193 ALA 106 194 LEU 107 195 LYS 108 196 THR 109 197 LYS 110 198 LEU 111 199 ASP 112 200 LEU 113 201 SER 114 202 SER 115 203 LEU 116 204 ALA 117 205 TYR 118 206 SER 119 207 GLY 120 208 LYS 121 209 ASP 122 210 ALA stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-01-29 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 15233 hfraG130V 99.18 123 99.17 99.17 2.74e-79 BMRB 15234 hfraD122Y 99.18 123 99.17 99.17 3.76e-79 BMRB 15235 hfraW155R 99.18 123 99.17 99.17 4.38e-79 BMRB 15736 Full-length_Human_frataxin 99.18 187 99.17 100.00 9.69e-80 BMRB 15906 Frataxin 99.18 121 100.00 100.00 1.64e-80 BMRB 16581 Frataxin 99.18 121 100.00 100.00 1.64e-80 PDB 1EKG "Mature Human Frataxin" 99.18 127 99.17 100.00 7.21e-80 PDB 1LY7 "The Solution Structure Of The The C-Terminal Domain Of Frataxin, The Protein Responsible For Friedreich Ataxia" 98.36 121 100.00 100.00 1.71e-79 PDB 3S4M "Crystal Structure Of Wild-Type Human Frataxin" 99.18 129 99.17 100.00 1.48e-79 PDB 3S5D "Crystal Structure Of Human Frataxin Variant W155a" 99.18 129 98.35 99.17 4.31e-78 PDB 3S5E "Crystal Structure Of Human Frataxin Variant W155r, One Of The Friedreich's Ataxia Point Mutations" 99.18 129 98.35 99.17 4.09e-78 PDB 3S5F "Crystal Structure Of Human Frataxin Variant W155f" 99.18 129 98.35 100.00 1.31e-78 PDB 3T3J "1.70 A Structure Of Friedreich's Ataxia Frataxin Variant N146k" 99.18 129 98.35 99.17 1.53e-78 PDB 3T3K "1.24 A Structure Of Friedreich's Ataxia Frataxin Variant Q148r" 99.18 129 98.35 100.00 6.82e-79 PDB 3T3L "1.15 A Structure Of Human Frataxin Variant Q153a" 99.18 129 98.35 99.17 1.34e-78 PDB 3T3T "1.38 A Structure Of Human Frataxin Variant Q148g" 99.18 129 98.35 99.17 2.64e-78 PDB 3T3X "1.57 A Structure Of Friedreich's Ataxia Frataxin Variant R165c" 99.18 129 98.35 99.17 2.19e-78 GB AAA98508 "frataxin [Homo sapiens]" 99.18 210 97.52 99.17 8.10e-78 GB AAA98509 "frataxin [Homo sapiens]" 58.20 171 98.59 100.00 4.50e-41 GB AAA98510 "frataxin [Homo sapiens]" 99.18 210 97.52 99.17 8.10e-78 GB AAH23633 "Frataxin [Homo sapiens]" 99.18 210 99.17 100.00 9.73e-80 GB AAH48097 "Frataxin [Homo sapiens]" 99.18 210 99.17 100.00 9.73e-80 REF NP_000135 "frataxin, mitochondrial isoform 1 preproprotein [Homo sapiens]" 99.18 210 99.17 100.00 9.73e-80 REF NP_001155178 "frataxin, mitochondrial isoform 3 preproprotein [Homo sapiens]" 58.20 171 98.59 100.00 4.50e-41 REF NP_001247670 "frataxin, mitochondrial [Macaca mulatta]" 99.18 210 97.52 99.17 7.06e-79 REF NP_852090 "frataxin, mitochondrial isoform 2 preproprotein [Homo sapiens]" 58.20 196 98.59 100.00 2.03e-41 REF XP_001137864 "PREDICTED: frataxin, mitochondrial [Pan troglodytes]" 95.08 238 99.14 99.14 5.94e-75 SP Q16595 "RecName: Full=Frataxin, mitochondrial; AltName: Full=Friedreich ataxia protein; Short=Fxn; Contains: RecName: Full=Frataxin int" 99.18 210 99.17 100.00 9.73e-80 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species _Organelle _Gene_mnemonic $Frataxin human 9606 Eukaryota Metazoa Homo sapiens mitochondria FRDA 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 $Frataxin 'recombinant technology' . . . . . 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 $Frataxin 1.0 mM '[U-95% 13C; U-90% 15N]' stop_ save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer_one _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model 'Unity plus' _Field_strength 600 _Details . save_ save_NMR_spectrometer_two _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model 'Unity plus' _Field_strength 500 _Details . save_ save_NMR_spectrometer_three _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model DMX _Field_strength 500 _Details . save_ ############################# # NMR applied experiments # ############################# save_1H-1H_-15N_NOESY_1 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-1H -15N NOESY' _Sample_label . save_ save_13C-1H-1H_NOESY_2 _Saveframe_category NMR_applied_experiment _Experiment_name '13C-1H-1H NOESY' _Sample_label . save_ save_3D_1H-13C-1HHCCH-TOCSY_3 _Saveframe_category NMR_applied_experiment _Experiment_name '3D 1H-13C-1HHCCH-TOCSY' _Sample_label . save_ save_3D_HNCA_4 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCA' _Sample_label . save_ save_3D_HN(CO)CA_5 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HN(CO)CA' _Sample_label . save_ save_3D_CBCA(CO)NH_6 _Saveframe_category NMR_applied_experiment _Experiment_name '3D CBCA(CO)NH' _Sample_label . save_ save_3D_HNCACB_7 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCACB' _Sample_label . save_ save_3D_HNHA_8 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNHA' _Sample_label . save_ save_3D_HNHB_9 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNHB' _Sample_label . save_ save_NMR_spec_expt__0_1 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-1H -15N NOESY' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_2 _Saveframe_category NMR_applied_experiment _Experiment_name '13C-1H-1H NOESY' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_3 _Saveframe_category NMR_applied_experiment _Experiment_name '3D 1H-13C-1HHCCH-TOCSY' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_4 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCA' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_5 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HN(CO)CA' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_6 _Saveframe_category NMR_applied_experiment _Experiment_name '3D CBCA(CO)NH' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_7 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCACB' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_8 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNHA' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_9 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNHB' _BMRB_pulse_sequence_accession_number . _Details . save_ ####################### # Sample conditions # ####################### save_sample_conditions _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 6.8 0.3 na temperature 300 1 K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference _Saveframe_category chemical_shift_reference _Details . loop_ _Mol_common_name _Atom_type _Atom_isotope_number _Atom_group _Chem_shift_units _Chem_shift_value _Reference_method _Reference_type _External_reference_sample_geometry _External_reference_location _External_reference_axis _Indirect_shift_ratio DSS H 1 'methyl protons' ppm 0 external direct . . . . DSS N 15 'methyl protons' ppm 0.0 . Indirect . . . 0.101329118 DSS C 13 'methyl protons' ppm 0.0 . Indirect . . . 0.251449530 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_chemical_shifts _Saveframe_category assigned_chemical_shifts _Details . loop_ _Sample_label $sample_one stop_ _Sample_conditions_label $sample_conditions _Chem_shift_reference_set_label $chemical_shift_reference _Mol_system_component_name Frataxin _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 PRO CD C 50.6 . 1 2 . 1 PRO CA C 62.7 . 1 3 . 1 PRO HA H 4.45 . 1 4 . 1 PRO CB C 32.2 . 1 5 . 1 PRO HB2 H 2.30 . 1 6 . 1 PRO HB3 H 2.30 . 1 7 . 1 PRO CG C 27.0 . 1 8 . 1 PRO HG2 H 1.95 . 1 9 . 1 PRO HG3 H 1.95 . 1 10 . 1 PRO HD2 H 3.62 . 2 11 . 1 PRO HD3 H 3.27 . 2 12 . 2 MET N N 123.8 . 1 13 . 2 MET H H 8.67 . 1 14 . 2 MET CA C 55.8 . 1 15 . 2 MET HA H 4.54 . 1 16 . 2 MET CB C 34.9 . 1 17 . 2 MET HB2 H 2.12 . 1 18 . 2 MET HB3 H 2.12 . 1 19 . 2 MET CG C 31.8 . 1 20 . 2 MET HG2 H 2.66 . 2 21 . 2 MET HG3 H 2.51 . 2 22 . 3 ASP N N 124.6 . 1 23 . 3 ASP H H 8.20 . 1 24 . 3 ASP CA C 53.0 . 1 25 . 3 ASP HA H 4.75 . 1 26 . 3 ASP CB C 41.9 . 1 27 . 3 ASP HB2 H 3.09 . 2 28 . 3 ASP HB3 H 2.77 . 2 29 . 4 GLU N N 122.8 . 1 30 . 4 GLU H H 8.84 . 1 31 . 4 GLU CA C 61.1 . 1 32 . 4 GLU HA H 3.97 . 1 33 . 4 GLU CB C 30.1 . 1 34 . 4 GLU HB2 H 2.15 . 1 35 . 4 GLU HB3 H 2.15 . 1 36 . 4 GLU CG C 37.2 . 1 37 . 4 GLU HG2 H 2.35 . 1 38 . 4 GLU HG3 H 2.35 . 1 39 . 5 THR N N 116.9 . 1 40 . 5 THR H H 8.21 . 1 41 . 5 THR CA C 66.1 . 1 42 . 5 THR HA H 4.03 . 1 43 . 5 THR CB C 68.5 . 1 44 . 5 THR HB H 4.19 . 1 45 . 5 THR HG2 H 1.26 . 1 46 . 5 THR CG2 C 21.3 . 1 47 . 5 THR C C 177.7 . 1 48 . 6 THR N N 122.8 . 1 49 . 6 THR H H 8.25 . 1 50 . 6 THR CA C 66.7 . 1 51 . 6 THR HA H 3.84 . 1 52 . 6 THR CB C 68.7 . 1 53 . 6 THR HB H 4.12 . 1 54 . 6 THR HG2 H 1.13 . 1 55 . 6 THR CG2 C 21.5 . 1 56 . 7 TYR N N 122.8 . 1 57 . 7 TYR H H 8.16 . 1 58 . 7 TYR CA C 62.5 . 1 59 . 7 TYR HA H 3.87 . 1 60 . 7 TYR CB C 37.7 . 1 61 . 7 TYR HB2 H 3.19 . 2 62 . 7 TYR HB3 H 3.03 . 2 63 . 7 TYR HD1 H 7.16 . 1 64 . 7 TYR HD2 H 7.16 . 1 65 . 7 TYR HE1 H 6.68 . 1 66 . 7 TYR HE2 H 6.68 . 1 67 . 7 TYR CD1 C 132.5 . 1 68 . 7 TYR CE1 C 117.7 . 1 69 . 8 GLU N N 120.5 . 1 70 . 8 GLU H H 8.36 . 1 71 . 8 GLU CA C 60.1 . 1 72 . 8 GLU HA H 3.47 . 1 73 . 8 GLU CB C 29.4 . 1 74 . 8 GLU HB2 H 2.00 . 1 75 . 8 GLU HB3 H 2.00 . 1 76 . 8 GLU CG C 36.5 . 1 77 . 8 GLU HG2 H 2.42 . 2 78 . 8 GLU HG3 H 2.12 . 2 79 . 8 GLU C C 175.4 . 1 80 . 9 ARG N N 120.0 . 1 81 . 9 ARG H H 7.35 . 1 82 . 9 ARG CA C 59.2 . 1 83 . 9 ARG HA H 4.06 . 1 84 . 9 ARG CB C 30.1 . 1 85 . 9 ARG HB2 H 1.86 . 1 86 . 9 ARG HB3 H 1.86 . 1 87 . 9 ARG CG C 27.7 . 1 88 . 9 ARG HG2 H 1.71 . 2 89 . 9 ARG HG3 H 1.57 . 2 90 . 9 ARG CD C 43.3 . 1 91 . 9 ARG HD2 H 3.27 . 2 92 . 9 ARG HD3 H 3.16 . 2 93 . 9 ARG C C 178.3 . 1 94 . 10 LEU N N 121.4 . 1 95 . 10 LEU H H 7.96 . 1 96 . 10 LEU CA C 57.8 . 1 97 . 10 LEU HA H 3.71 . 1 98 . 10 LEU CB C 42.3 . 1 99 . 10 LEU HB2 H 1.25 . 2 100 . 10 LEU HB3 H 0.45 . 2 101 . 10 LEU CG C 26.4 . 1 102 . 10 LEU HG H 1.20 . 1 103 . 10 LEU HD1 H -0.16 . 2 104 . 10 LEU HD2 H -0.60 . 2 105 . 10 LEU CD1 C 22.3 . 1 106 . 10 LEU CD2 C 24.3 . 1 107 . 10 LEU C C 178.3 . 1 108 . 11 ALA N N 126.3 . 1 109 . 11 ALA H H 9.17 . 1 110 . 11 ALA CA C 55.9 . 1 111 . 11 ALA HA H 3.62 . 1 112 . 11 ALA HB H 0.74 . 1 113 . 11 ALA CB C 17.8 . 1 114 . 11 ALA C C 173.3 . 1 115 . 12 GLU N N 120.5 . 1 116 . 12 GLU H H 8.13 . 1 117 . 12 GLU CA C 60.2 . 1 118 . 12 GLU HA H 3.94 . 1 119 . 12 GLU CB C 29.1 . 1 120 . 12 GLU HB2 H 2.27 . 2 121 . 12 GLU HB3 H 2.14 . 2 122 . 12 GLU CG C 36.2 . 1 123 . 12 GLU HG2 H 2.41 . 1 124 . 12 GLU HG3 H 2.41 . 1 125 . 12 GLU C C 178.9 . 1 126 . 13 GLU N N 120.2 . 1 127 . 13 GLU H H 8.41 . 1 128 . 13 GLU CA C 60.0 . 1 129 . 13 GLU HA H 4.17 . 1 130 . 13 GLU CB C 31.1 . 1 131 . 13 GLU HB2 H 2.39 . 2 132 . 13 GLU HB3 H 2.19 . 2 133 . 13 GLU CG C 37.2 . 1 134 . 13 GLU HG2 H 2.71 . 1 135 . 13 GLU HG3 H 2.71 . 1 136 . 13 GLU C C 176.6 . 1 137 . 14 THR N N 118.3 . 1 138 . 14 THR H H 8.17 . 1 139 . 14 THR CA C 68.3 . 1 140 . 14 THR HA H 3.95 . 1 141 . 14 THR CB C 69.3 . 1 142 . 14 THR HB H 4.27 . 1 143 . 14 THR HG2 H 1.12 . 1 144 . 14 THR HG1 H 5.58 . 1 145 . 14 THR CG2 C 19.7 . 1 146 . 15 LEU N N 125.2 . 1 147 . 15 LEU H H 8.46 . 1 148 . 15 LEU CA C 58.6 . 1 149 . 15 LEU HA H 3.82 . 1 150 . 15 LEU CB C 41.5 . 1 151 . 15 LEU HB2 H 1.98 . 2 152 . 15 LEU HB3 H 1.42 . 2 153 . 15 LEU CG C 27.8 . 1 154 . 15 LEU HG H 1.63 . 1 155 . 15 LEU HD1 H 0.73 . 2 156 . 15 LEU HD2 H 0.61 . 2 157 . 15 LEU CD1 C 26.1 . 1 158 . 15 LEU CD2 C 23.0 . 1 159 . 16 ASP N N 122.4 . 1 160 . 16 ASP H H 9.04 . 1 161 . 16 ASP CA C 57.7 . 1 162 . 16 ASP HA H 4.28 . 1 163 . 16 ASP CB C 41.3 . 1 164 . 16 ASP HB2 H 2.87 . 2 165 . 16 ASP HB3 H 2.68 . 2 166 . 16 ASP C C 177.2 . 1 167 . 17 SER N N 114.6 . 1 168 . 17 SER H H 7.27 . 1 169 . 17 SER CA C 61.2 . 1 170 . 17 SER HA H 4.33 . 1 171 . 17 SER CB C 63.8 . 1 172 . 17 SER HB2 H 4.24 . 2 173 . 17 SER HB3 H 4.14 . 2 174 . 17 SER C C 178.3 . 1 175 . 18 LEU N N 121.3 . 1 176 . 18 LEU H H 7.52 . 1 177 . 18 LEU CA C 58.2 . 1 178 . 18 LEU HA H 4.00 . 1 179 . 18 LEU CB C 42.8 . 1 180 . 18 LEU HB2 H 1.91 . 2 181 . 18 LEU HB3 H 1.19 . 2 182 . 18 LEU CG C 26.9 . 1 183 . 18 LEU HG H 1.77 . 1 184 . 18 LEU HD1 H 0.53 . 2 185 . 18 LEU HD2 H 0.42 . 2 186 . 18 LEU CD1 C 24.8 . 1 187 . 18 LEU CD2 C 25.4 . 1 188 . 18 LEU C C 178.2 . 1 189 . 19 ALA N N 124.7 . 1 190 . 19 ALA H H 8.90 . 1 191 . 19 ALA CA C 56.5 . 1 192 . 19 ALA HA H 3.76 . 1 193 . 19 ALA HB H 0.85 . 1 194 . 19 ALA CB C 17.6 . 1 195 . 20 GLU N N 119.9 . 1 196 . 20 GLU H H 7.75 . 1 197 . 20 GLU CA C 59.6 . 1 198 . 20 GLU HA H 3.99 . 1 199 . 20 GLU CB C 29.7 . 1 200 . 20 GLU HB2 H 2.19 . 1 201 . 20 GLU HB3 H 2.19 . 1 202 . 20 GLU CG C 36.7 . 1 203 . 20 GLU HG2 H 2.45 . 2 204 . 20 GLU HG3 H 2.27 . 2 205 . 20 GLU C C 178.9 . 1 206 . 21 PHE N N 123.3 . 1 207 . 21 PHE H H 7.64 . 1 208 . 21 PHE CA C 61.4 . 1 209 . 21 PHE HA H 4.17 . 1 210 . 21 PHE CB C 39.4 . 1 211 . 21 PHE HB2 H 3.15 . 1 212 . 21 PHE HB3 H 3.15 . 1 213 . 21 PHE HD1 H 6.49 . 1 214 . 21 PHE HD2 H 6.49 . 1 215 . 21 PHE HE1 H 6.76 . 1 216 . 21 PHE HE2 H 6.76 . 1 217 . 21 PHE CD1 C 131.0 . 1 218 . 21 PHE CE1 C 129.5 . 1 219 . 21 PHE CZ C 128.1 . 1 220 . 21 PHE HZ H 6.86 . 1 221 . 21 PHE C C 178.6 . 1 222 . 22 PHE N N 119.1 . 1 223 . 22 PHE H H 8.78 . 1 224 . 22 PHE CA C 63.0 . 1 225 . 22 PHE HA H 4.13 . 1 226 . 22 PHE CB C 38.1 . 1 227 . 22 PHE HB2 H 3.27 . 2 228 . 22 PHE HB3 H 2.81 . 2 229 . 22 PHE HD1 H 7.62 . 1 230 . 22 PHE HD2 H 7.62 . 1 231 . 22 PHE HE1 H 6.99 . 1 232 . 22 PHE HE2 H 6.99 . 1 233 . 22 PHE CD1 C 132.2 . 1 234 . 22 PHE CE1 C 128.8 . 1 235 . 22 PHE CZ C 126.8 . 1 236 . 22 PHE HZ H 6.79 . 1 237 . 22 PHE C C 177.4 . 1 238 . 23 GLU N N 126.9 . 1 239 . 23 GLU H H 9.23 . 1 240 . 23 GLU CA C 60.2 . 1 241 . 23 GLU HA H 4.22 . 1 242 . 23 GLU CB C 29.2 . 1 243 . 23 GLU HB2 H 2.11 . 1 244 . 23 GLU HB3 H 2.11 . 1 245 . 23 GLU CG C 36.1 . 1 246 . 23 GLU HG2 H 2.52 . 2 247 . 23 GLU HG3 H 2.29 . 2 248 . 24 ASP N N 122.4 . 1 249 . 24 ASP H H 7.74 . 1 250 . 24 ASP CA C 56.5 . 1 251 . 24 ASP HA H 4.42 . 1 252 . 24 ASP CB C 41.4 . 1 253 . 24 ASP HB2 H 2.71 . 2 254 . 24 ASP HB3 H 2.58 . 2 255 . 24 ASP C C 179.4 . 1 256 . 25 LEU N N 118.0 . 1 257 . 25 LEU H H 7.23 . 1 258 . 25 LEU CA C 55.8 . 1 259 . 25 LEU HA H 3.81 . 1 260 . 25 LEU CB C 41.3 . 1 261 . 25 LEU HB2 H 1.59 . 2 262 . 25 LEU HB3 H 1.23 . 2 263 . 25 LEU CG C 26.4 . 1 264 . 25 LEU HG H 1.51 . 1 265 . 25 LEU HD1 H 0.70 . 2 266 . 25 LEU HD2 H 0.59 . 2 267 . 25 LEU CD1 C 24.6 . 1 268 . 25 LEU CD2 C 23.3 . 1 269 . 25 LEU C C 177.0 . 1 270 . 26 ALA N N 122.4 . 1 271 . 26 ALA H H 7.23 . 1 272 . 26 ALA CA C 55.4 . 1 273 . 26 ALA HA H 3.63 . 1 274 . 26 ALA HB H 1.63 . 1 275 . 26 ALA CB C 18.7 . 1 276 . 26 ALA C C 178.3 . 1 277 . 27 ASP N N 115.5 . 1 278 . 27 ASP H H 7.49 . 1 279 . 27 ASP CA C 53.4 . 1 280 . 27 ASP HA H 4.58 . 1 281 . 27 ASP CB C 40.7 . 1 282 . 27 ASP HB2 H 2.72 . 2 283 . 27 ASP HB3 H 2.63 . 2 284 . 27 ASP C C 177.4 . 1 285 . 28 LYS N N 121.3 . 1 286 . 28 LYS H H 7.01 . 1 287 . 28 LYS CA C 52.3 . 1 288 . 28 LYS HA H 4.25 . 1 289 . 28 LYS CB C 30.9 . 1 290 . 28 LYS HB2 H 1.18 . 2 291 . 28 LYS HB3 H 0.53 . 2 292 . 28 LYS CG C 24.8 . 1 293 . 28 LYS HG2 H 1.37 . 1 294 . 28 LYS HG3 H 1.37 . 1 295 . 28 LYS CD C 25.3 . 1 296 . 28 LYS HD2 H 1.39 . 1 297 . 28 LYS HD3 H 1.39 . 1 298 . 28 LYS HE2 H 2.98 . 2 299 . 28 LYS HE3 H 2.73 . 2 300 . 28 LYS C C 176.5 . 1 301 . 29 PRO CD C 50.6 . 1 302 . 29 PRO CA C 64.4 . 1 303 . 29 PRO HA H 4.37 . 1 304 . 29 PRO CB C 31.6 . 1 305 . 29 PRO HB2 H 2.32 . 2 306 . 29 PRO HB3 H 1.99 . 2 307 . 29 PRO CG C 27.3 . 1 308 . 29 PRO HG2 H 1.65 . 2 309 . 29 PRO HG3 H 1.46 . 2 310 . 29 PRO HD2 H 3.71 . 2 311 . 29 PRO HD3 H 3.40 . 2 312 . 30 TYR N N 111.9 . 1 313 . 30 TYR H H 5.88 . 1 314 . 30 TYR CA C 54.8 . 1 315 . 30 TYR HA H 4.57 . 1 316 . 30 TYR CB C 37.3 . 1 317 . 30 TYR HB2 H 3.45 . 2 318 . 30 TYR HB3 H 2.81 . 2 319 . 30 TYR HD1 H 6.90 . 1 320 . 30 TYR HD2 H 6.90 . 1 321 . 30 TYR HE1 H 6.70 . 1 322 . 30 TYR HE2 H 6.70 . 1 323 . 30 TYR CD1 C 132.6 . 1 324 . 30 TYR CE1 C 117.7 . 1 325 . 30 TYR C C 176.0 . 1 326 . 31 THR N N 114.0 . 1 327 . 31 THR H H 6.89 . 1 328 . 31 THR CA C 59.6 . 1 329 . 31 THR HA H 4.46 . 1 330 . 31 THR CB C 70.7 . 1 331 . 31 THR HB H 3.77 . 1 332 . 31 THR HG2 H 0.54 . 1 333 . 31 THR CG2 C 23.2 . 1 334 . 31 THR C C 175.3 . 1 335 . 32 PHE N N 125.5 . 1 336 . 32 PHE H H 8.99 . 1 337 . 32 PHE CA C 56.8 . 1 338 . 32 PHE HA H 4.78 . 1 339 . 32 PHE CB C 40.6 . 1 340 . 32 PHE HB2 H 3.69 . 2 341 . 32 PHE HB3 H 3.26 . 2 342 . 32 PHE HD1 H 7.41 . 1 343 . 32 PHE HD2 H 7.41 . 1 344 . 32 PHE HE1 H 7.41 . 1 345 . 32 PHE HE2 H 7.41 . 1 346 . 32 PHE CD1 C 130.2 . 1 347 . 32 PHE CE1 C 130.2 . 1 348 . 32 PHE CZ C 130.2 . 1 349 . 32 PHE HZ H 7.41 . 1 350 . 32 PHE C C 175.4 . 1 351 . 33 GLU N N 122.7 . 1 352 . 33 GLU H H 9.28 . 1 353 . 33 GLU CA C 59.4 . 1 354 . 33 GLU HA H 4.22 . 1 355 . 33 GLU CB C 29.7 . 1 356 . 33 GLU HB2 H 2.15 . 1 357 . 33 GLU HB3 H 2.15 . 1 358 . 33 GLU CG C 36.2 . 1 359 . 33 GLU HG2 H 2.40 . 1 360 . 33 GLU HG3 H 2.40 . 1 361 . 34 ASP N N 116.3 . 1 362 . 34 ASP H H 9.21 . 1 363 . 34 ASP CA C 52.7 . 1 364 . 34 ASP HA H 4.64 . 1 365 . 34 ASP CB C 38.1 . 1 366 . 34 ASP HB2 H 2.92 . 2 367 . 34 ASP HB3 H 2.61 . 2 368 . 34 ASP C C 176.3 . 1 369 . 35 TYR N N 124.7 . 1 370 . 35 TYR H H 7.27 . 1 371 . 35 TYR CA C 58.6 . 1 372 . 35 TYR HA H 4.60 . 1 373 . 35 TYR CB C 40.2 . 1 374 . 35 TYR HB2 H 3.19 . 2 375 . 35 TYR HB3 H 2.92 . 2 376 . 35 TYR HD1 H 7.20 . 1 377 . 35 TYR HD2 H 7.20 . 1 378 . 35 TYR HE1 H 6.53 . 1 379 . 35 TYR HE2 H 6.53 . 1 380 . 35 TYR CD1 C 132.5 . 1 381 . 35 TYR CE1 C 115.8 . 1 382 . 35 TYR HH H 9.03 . 1 383 . 35 TYR C C 174.5 . 1 384 . 36 ASP N N 131.0 . 1 385 . 36 ASP H H 8.82 . 1 386 . 36 ASP CA C 54.6 . 1 387 . 36 ASP HA H 4.78 . 1 388 . 36 ASP CB C 46.2 . 1 389 . 36 ASP HB2 H 2.53 . 2 390 . 36 ASP HB3 H 2.39 . 2 391 . 36 ASP C C 176.0 . 1 392 . 37 VAL N N 126.6 . 1 393 . 37 VAL H H 8.19 . 1 394 . 37 VAL CA C 60.6 . 1 395 . 37 VAL HA H 4.66 . 1 396 . 37 VAL CB C 34.4 . 1 397 . 37 VAL HB H 1.91 . 1 398 . 37 VAL HG1 H 0.85 . 2 399 . 37 VAL HG2 H 0.79 . 2 400 . 37 VAL CG1 C 21.5 . 1 401 . 37 VAL CG2 C 22.8 . 1 402 . 37 VAL C C 172.8 . 1 403 . 38 SER N N 123.8 . 1 404 . 38 SER H H 8.88 . 1 405 . 38 SER CA C 56.9 . 1 406 . 38 SER HA H 4.85 . 1 407 . 38 SER CB C 65.4 . 1 408 . 38 SER HB2 H 3.79 . 1 409 . 38 SER HB3 H 3.79 . 1 410 . 39 PHE N N 128.8 . 1 411 . 39 PHE H H 9.02 . 1 412 . 39 PHE CA C 54.5 . 1 413 . 39 PHE HA H 5.94 . 1 414 . 39 PHE CB C 41.6 . 1 415 . 39 PHE HB2 H 3.06 . 2 416 . 39 PHE HB3 H 2.94 . 2 417 . 39 PHE HD1 H 7.24 . 1 418 . 39 PHE HD2 H 7.24 . 1 419 . 39 PHE HE1 H 7.32 . 1 420 . 39 PHE HE2 H 7.32 . 1 421 . 39 PHE CD1 C 130.1 . 1 422 . 39 PHE CE1 C 129.2 . 1 423 . 39 PHE HZ H 7.42 . 1 424 . 39 PHE C C 172.7 . 1 425 . 40 GLY N N 117.2 . 1 426 . 40 GLY H H 8.14 . 1 427 . 40 GLY CA C 45.7 . 1 428 . 40 GLY HA2 H 3.89 . 2 429 . 40 GLY HA3 H 3.76 . 2 430 . 41 SER N N 120.3 . 1 431 . 41 SER H H 8.72 . 1 432 . 41 SER CA C 58.6 . 1 433 . 41 SER HA H 3.98 . 1 434 . 41 SER CB C 62.0 . 1 435 . 41 SER HB2 H 3.86 . 1 436 . 41 SER HB3 H 3.86 . 1 437 . 42 GLY N N 108.6 . 1 438 . 42 GLY H H 8.71 . 1 439 . 42 GLY CA C 46.0 . 1 440 . 42 GLY HA2 H 4.09 . 2 441 . 42 GLY HA3 H 3.52 . 2 442 . 42 GLY C C 174.5 . 1 443 . 43 VAL N N 121.3 . 1 444 . 43 VAL H H 7.69 . 1 445 . 43 VAL CA C 62.1 . 1 446 . 43 VAL HA H 4.50 . 1 447 . 43 VAL CB C 34.4 . 1 448 . 43 VAL HB H 2.10 . 1 449 . 43 VAL HG1 H 0.87 . 2 450 . 43 VAL HG2 H 0.82 . 2 451 . 43 VAL CG1 C 21.5 . 1 452 . 43 VAL CG2 C 21.5 . 1 453 . 43 VAL C C 172.3 . 1 454 . 44 LEU N N 135.5 . 1 455 . 44 LEU H H 9.61 . 1 456 . 44 LEU CA C 53.7 . 1 457 . 44 LEU HA H 5.34 . 1 458 . 44 LEU CB C 44.7 . 1 459 . 44 LEU HB2 H 2.10 . 2 460 . 44 LEU HB3 H 1.23 . 2 461 . 44 LEU CG C 27.2 . 1 462 . 44 LEU HG H 1.18 . 1 463 . 44 LEU HD1 H 0.70 . 1 464 . 44 LEU HD2 H 0.70 . 1 465 . 44 LEU CD1 C 21.8 . 1 466 . 44 LEU CD2 C 21.8 . 1 467 . 45 THR N N 126.9 . 1 468 . 45 THR H H 9.24 . 1 469 . 45 THR CA C 61.9 . 1 470 . 45 THR HA H 5.05 . 1 471 . 45 THR CB C 69.8 . 1 472 . 45 THR HB H 4.00 . 1 473 . 45 THR HG2 H 1.02 . 1 474 . 45 THR CG2 C 21.5 . 1 475 . 46 VAL N N 130.2 . 1 476 . 46 VAL H H 9.17 . 1 477 . 46 VAL CA C 60.9 . 1 478 . 46 VAL HA H 4.28 . 1 479 . 46 VAL CB C 33.9 . 1 480 . 46 VAL HB H 1.59 . 1 481 . 46 VAL HG1 H 0.43 . 2 482 . 46 VAL HG2 H -0.19 . 2 483 . 46 VAL CG1 C 20.6 . 1 484 . 46 VAL CG2 C 18.3 . 1 485 . 46 VAL C C 173.6 . 1 486 . 47 LYS N N 132.7 . 1 487 . 47 LYS H H 8.90 . 1 488 . 47 LYS CA C 55.2 . 1 489 . 47 LYS HA H 4.57 . 1 490 . 47 LYS CB C 33.3 . 1 491 . 47 LYS HB2 H 1.80 . 1 492 . 47 LYS HB3 H 1.80 . 1 493 . 47 LYS CG C 25.4 . 1 494 . 47 LYS HG2 H 1.35 . 2 495 . 47 LYS HG3 H 1.21 . 2 496 . 47 LYS CD C 30.2 . 1 497 . 47 LYS HD2 H 1.66 . 1 498 . 47 LYS HD3 H 1.66 . 1 499 . 47 LYS CE C 42.6 . 1 500 . 47 LYS HE2 H 3.05 . 1 501 . 47 LYS HE3 H 3.05 . 1 502 . 47 LYS C C 174.0 . 1 503 . 48 LEU N N 126.0 . 1 504 . 48 LEU H H 8.49 . 1 505 . 48 LEU CA C 57.1 . 1 506 . 48 LEU HA H 4.43 . 1 507 . 48 LEU CB C 43.9 . 1 508 . 48 LEU HB2 H 2.27 . 2 509 . 48 LEU HB3 H 1.51 . 2 510 . 48 LEU CG C 27.4 . 1 511 . 48 LEU HG H 1.91 . 1 512 . 48 LEU HD1 H 1.04 . 2 513 . 48 LEU HD2 H 0.92 . 2 514 . 48 LEU CD1 C 23.1 . 1 515 . 48 LEU CD2 C 26.5 . 1 516 . 48 LEU C C 174.8 . 1 517 . 49 GLY N N 105.2 . 1 518 . 49 GLY H H 7.57 . 1 519 . 49 GLY CA C 42.7 . 1 520 . 49 GLY HA2 H 4.42 . 2 521 . 49 GLY HA3 H 3.37 . 2 522 . 49 GLY C C 177.2 . 1 523 . 50 GLY N N 109.4 . 1 524 . 50 GLY H H 9.16 . 1 525 . 50 GLY CA C 47.2 . 1 526 . 50 GLY HA2 H 3.54 . 2 527 . 50 GLY HA3 H 3.18 . 2 528 . 50 GLY C C 173.4 . 1 529 . 51 ASP N N 125.9 . 1 530 . 51 ASP H H 8.67 . 1 531 . 51 ASP CA C 53.8 . 1 532 . 51 ASP HA H 4.66 . 1 533 . 51 ASP CB C 40.3 . 1 534 . 51 ASP HB2 H 2.73 . 1 535 . 51 ASP HB3 H 2.73 . 1 536 . 52 LEU N N 122.4 . 1 537 . 52 LEU H H 8.38 . 1 538 . 52 LEU CA C 56.5 . 1 539 . 52 LEU HA H 4.19 . 1 540 . 52 LEU CB C 44.1 . 1 541 . 52 LEU HB2 H 2.31 . 2 542 . 52 LEU HB3 H 1.55 . 2 543 . 52 LEU CG C 27.7 . 1 544 . 52 LEU HG H 1.95 . 1 545 . 52 LEU HD1 H 1.06 . 2 546 . 52 LEU HD2 H 0.96 . 2 547 . 52 LEU CD1 C 26.9 . 1 548 . 52 LEU CD2 C 22.4 . 1 549 . 53 GLY N N 107.4 . 1 550 . 53 GLY H H 8.05 . 1 551 . 53 GLY CA C 44.4 . 1 552 . 53 GLY HA2 H 4.08 . 2 553 . 53 GLY HA3 H 3.75 . 2 554 . 53 GLY C C 177.7 . 1 555 . 54 THR N N 116.9 . 1 556 . 54 THR H H 7.93 . 1 557 . 54 THR CA C 61.2 . 1 558 . 54 THR HA H 5.34 . 1 559 . 54 THR CB C 72.4 . 1 560 . 54 THR HB H 3.69 . 1 561 . 54 THR HG2 H 0.90 . 1 562 . 54 THR CG2 C 22.8 . 1 563 . 54 THR C C 172.3 . 1 564 . 55 TYR N N 127.4 . 1 565 . 55 TYR H H 9.33 . 1 566 . 55 TYR CA C 57.8 . 1 567 . 55 TYR HA H 4.99 . 1 568 . 55 TYR CB C 41.9 . 1 569 . 55 TYR HB2 H 2.76 . 2 570 . 55 TYR HB3 H 2.48 . 2 571 . 55 TYR HD1 H 6.95 . 1 572 . 55 TYR HD2 H 6.95 . 1 573 . 55 TYR HE1 H 6.78 . 1 574 . 55 TYR HE2 H 6.78 . 1 575 . 55 TYR CD1 C 131.2 . 1 576 . 55 TYR CE1 C 116.4 . 1 577 . 55 TYR HH H 11.08 . 1 578 . 55 TYR C C 174.2 . 1 579 . 56 VAL N N 121.6 . 1 580 . 56 VAL H H 7.92 . 1 581 . 56 VAL CA C 62.0 . 1 582 . 56 VAL HA H 4.95 . 1 583 . 56 VAL CB C 34.7 . 1 584 . 56 VAL HB H 1.89 . 1 585 . 56 VAL HG1 H 0.88 . 1 586 . 56 VAL HG2 H 0.88 . 1 587 . 56 VAL CG1 C 21.8 . 1 588 . 56 VAL CG2 C 21.8 . 1 589 . 56 VAL C C 175.3 . 1 590 . 57 ILE N N 133.3 . 1 591 . 57 ILE H H 9.70 . 1 592 . 57 ILE CA C 60.4 . 1 593 . 57 ILE HA H 5.23 . 1 594 . 57 ILE CB C 40.6 . 1 595 . 57 ILE HB H 1.75 . 1 596 . 57 ILE HG2 H 0.69 . 1 597 . 57 ILE CG2 C 19.4 . 1 598 . 57 ILE CG1 C 28.5 . 1 599 . 57 ILE HG12 H 1.59 . 2 600 . 57 ILE HG13 H 1.00 . 2 601 . 57 ILE HD1 H 0.74 . 1 602 . 57 ILE CD1 C 14.8 . 1 603 . 57 ILE C C 175.5 . 1 604 . 58 ASN N N 123.8 . 1 605 . 58 ASN H H 9.62 . 1 606 . 58 ASN CA C 52.3 . 1 607 . 58 ASN HA H 5.82 . 1 608 . 58 ASN CB C 43.5 . 1 609 . 58 ASN HB2 H 2.90 . 2 610 . 58 ASN HB3 H 2.54 . 2 611 . 58 ASN ND2 N 114.0 . 1 612 . 58 ASN HD21 H 6.78 . 2 613 . 58 ASN HD22 H 6.16 . 2 614 . 59 LYS N N 123.5 . 1 615 . 59 LYS H H 8.45 . 1 616 . 59 LYS CA C 57.3 . 1 617 . 59 LYS HA H 4.10 . 1 618 . 59 LYS CB C 33.6 . 1 619 . 59 LYS HB2 H 1.92 . 1 620 . 59 LYS HB3 H 1.92 . 1 621 . 59 LYS CG C 24.6 . 1 622 . 59 LYS HG2 H 1.46 . 1 623 . 59 LYS HG3 H 1.46 . 1 624 . 59 LYS CD C 30.2 . 1 625 . 59 LYS HD2 H 1.76 . 1 626 . 59 LYS HD3 H 1.76 . 1 627 . 59 LYS CE C 41.5 . 1 628 . 59 LYS HE2 H 2.92 . 1 629 . 59 LYS HE3 H 2.92 . 1 630 . 60 GLN N N 131.6 . 1 631 . 60 GLN H H 7.81 . 1 632 . 60 GLN CA C 54.3 . 1 633 . 60 GLN HA H 4.42 . 1 634 . 60 GLN CB C 27.4 . 1 635 . 60 GLN HB2 H 1.54 . 2 636 . 60 GLN HB3 H 0.61 . 2 637 . 60 GLN CG C 32.5 . 1 638 . 60 GLN HG2 H 1.28 . 2 639 . 60 GLN HG3 H 0.93 . 2 640 . 60 GLN NE2 N 110.8 . 1 641 . 60 GLN HE21 H 7.14 . 2 642 . 60 GLN HE22 H 6.84 . 2 643 . 60 GLN C C 174.7 . 1 644 . 61 THR N N 125.5 . 1 645 . 61 THR H H 8.57 . 1 646 . 61 THR CA C 68.5 . 1 647 . 61 THR HA H 4.01 . 1 648 . 61 THR CB C 66.7 . 1 649 . 61 THR HB H 4.24 . 1 650 . 61 THR HG2 H 1.27 . 1 651 . 61 THR CG2 C 19.4 . 1 652 . 62 PRO CD C 50.6 . 1 653 . 62 PRO CA C 66.2 . 1 654 . 62 PRO HA H 4.23 . 1 655 . 62 PRO CB C 30.9 . 1 656 . 62 PRO HB2 H 2.30 . 2 657 . 62 PRO HB3 H 1.96 . 2 658 . 62 PRO CG C 27.7 . 1 659 . 62 PRO HG2 H 1.89 . 2 660 . 62 PRO HG3 H 1.68 . 2 661 . 62 PRO HD2 H 3.67 . 2 662 . 62 PRO HD3 H 3.38 . 2 663 . 63 ASN N N 113.0 . 1 664 . 63 ASN H H 7.02 . 1 665 . 63 ASN CA C 53.2 . 1 666 . 63 ASN HA H 4.75 . 1 667 . 63 ASN CB C 40.3 . 1 668 . 63 ASN HB2 H 3.06 . 2 669 . 63 ASN HB3 H 2.29 . 2 670 . 63 ASN ND2 N 113.6 . 1 671 . 63 ASN HD21 H 7.67 . 2 672 . 63 ASN HD22 H 7.07 . 2 673 . 63 ASN C C 176.8 . 1 674 . 64 LYS N N 119.7 . 1 675 . 64 LYS H H 7.92 . 1 676 . 64 LYS CA C 57.4 . 1 677 . 64 LYS HA H 2.12 . 1 678 . 64 LYS CB C 28.9 . 1 679 . 64 LYS HB2 H 1.67 . 1 680 . 64 LYS HB3 H 1.67 . 1 681 . 64 LYS CG C 24.9 . 1 682 . 64 LYS HG2 H 0.86 . 1 683 . 64 LYS HG3 H 0.86 . 1 684 . 64 LYS CD C 27.4 . 1 685 . 64 LYS HD2 H 1.25 . 1 686 . 64 LYS HD3 H 1.25 . 1 687 . 64 LYS CE C 42.1 . 1 688 . 64 LYS HE2 H 2.98 . 2 689 . 64 LYS HE3 H 2.76 . 2 690 . 65 GLN N N 113.8 . 1 691 . 65 GLN H H 7.13 . 1 692 . 65 GLN CA C 54.1 . 1 693 . 65 GLN HA H 5.78 . 1 694 . 65 GLN CB C 37.1 . 1 695 . 65 GLN HB2 H 2.34 . 2 696 . 65 GLN HB3 H 1.99 . 2 697 . 65 GLN CG C 34.2 . 1 698 . 65 GLN HG2 H 2.81 . 1 699 . 65 GLN HG3 H 2.81 . 1 700 . 65 GLN NE2 N 111.6 . 1 701 . 65 GLN HE21 H 6.26 . 1 702 . 65 GLN HE22 H 6.26 . 1 703 . 65 GLN C C 174.4 . 1 704 . 66 ILE N N 125.5 . 1 705 . 66 ILE H H 8.52 . 1 706 . 66 ILE CA C 61.2 . 1 707 . 66 ILE HA H 4.66 . 1 708 . 66 ILE CB C 39.8 . 1 709 . 66 ILE HB H 1.17 . 1 710 . 66 ILE HG2 H 0.51 . 1 711 . 66 ILE CG2 C 17.4 . 1 712 . 66 ILE CG1 C 27.7 . 1 713 . 66 ILE HG12 H 0.37 . 2 714 . 66 ILE HG13 H 0.18 . 2 715 . 66 ILE HD1 H -0.43 . 1 716 . 66 ILE CD1 C 11.3 . 1 717 . 67 TRP N N 133.0 . 1 718 . 67 TRP H H 9.50 . 1 719 . 67 TRP CA C 55.5 . 1 720 . 67 TRP HA H 5.67 . 1 721 . 67 TRP CB C 31.1 . 1 722 . 67 TRP HB2 H 3.38 . 1 723 . 67 TRP HB3 H 3.38 . 1 724 . 67 TRP CD2 C 120.2 . 1 725 . 67 TRP CE3 C 120.3 . 1 726 . 67 TRP NE1 N 129.3 . 1 727 . 67 TRP HD1 H 6.81 . 1 728 . 67 TRP HE3 H 7.56 . 1 729 . 67 TRP CZ3 C 121.6 . 1 730 . 67 TRP CZ2 C 112.7 . 1 731 . 67 TRP HE1 H 10.47 . 1 732 . 67 TRP HZ3 H 7.05 . 1 733 . 67 TRP CH2 C 124.7 . 1 734 . 67 TRP HZ2 H 7.29 . 1 735 . 67 TRP HH2 H 7.19 . 1 736 . 67 TRP C C 174.5 . 1 737 . 68 LEU N N 125.2 . 1 738 . 68 LEU H H 8.71 . 1 739 . 68 LEU CA C 53.7 . 1 740 . 68 LEU HA H 5.36 . 1 741 . 68 LEU CB C 48.3 . 1 742 . 68 LEU HB2 H 1.92 . 2 743 . 68 LEU HB3 H 1.53 . 2 744 . 68 LEU CG C 27.1 . 1 745 . 68 LEU HG H 1.59 . 1 746 . 68 LEU HD1 H 0.98 . 1 747 . 68 LEU HD2 H 0.98 . 1 748 . 68 LEU CD1 C 27.1 . 1 749 . 68 LEU CD2 C 27.1 . 1 750 . 69 SER N N 123.3 . 1 751 . 69 SER H H 9.27 . 1 752 . 69 SER CA C 57.3 . 1 753 . 69 SER HA H 4.49 . 1 754 . 69 SER CB C 63.8 . 1 755 . 69 SER HB2 H 3.77 . 2 756 . 69 SER HB3 H 3.67 . 2 757 . 70 SER N N 122.7 . 1 758 . 70 SER H H 7.57 . 1 759 . 70 SER CA C 51.7 . 1 760 . 70 SER HA H 4.84 . 1 761 . 70 SER CB C 63.2 . 1 762 . 70 SER HB2 H 4.15 . 2 763 . 70 SER HB3 H 3.85 . 2 764 . 70 SER C C 173.2 . 1 765 . 71 PRO CD C 49.1 . 1 766 . 71 PRO CA C 64.0 . 1 767 . 71 PRO HA H 4.36 . 1 768 . 71 PRO CB C 32.0 . 1 769 . 71 PRO HB2 H 2.25 . 2 770 . 71 PRO HB3 H 2.10 . 2 771 . 71 PRO CG C 26.9 . 1 772 . 71 PRO HG2 H 1.70 . 2 773 . 71 PRO HG3 H 1.50 . 2 774 . 71 PRO HD2 H 2.66 . 2 775 . 71 PRO HD3 H 2.50 . 2 776 . 72 SER N N 115.2 . 1 777 . 72 SER H H 7.84 . 1 778 . 72 SER CA C 59.1 . 1 779 . 72 SER HA H 4.62 . 1 780 . 72 SER CB C 64.5 . 1 781 . 72 SER HB2 H 3.72 . 2 782 . 72 SER HB3 H 3.66 . 2 783 . 72 SER C C 175.9 . 1 784 . 73 SER N N 116.3 . 1 785 . 73 SER H H 8.23 . 1 786 . 73 SER CA C 58.0 . 1 787 . 73 SER HA H 4.68 . 1 788 . 73 SER CB C 64.0 . 1 789 . 73 SER HB2 H 4.01 . 2 790 . 73 SER HB3 H 3.60 . 2 791 . 73 SER C C 175.7 . 1 792 . 74 GLY N N 115.2 . 1 793 . 74 GLY H H 7.94 . 1 794 . 74 GLY CA C 45.6 . 1 795 . 74 GLY HA2 H 4.38 . 2 796 . 74 GLY HA3 H 3.93 . 2 797 . 74 GLY C C 175.3 . 1 798 . 75 PRO CD C 49.7 . 1 799 . 75 PRO CA C 62.2 . 1 800 . 75 PRO HA H 5.42 . 1 801 . 75 PRO CB C 32.6 . 1 802 . 75 PRO HB2 H 2.13 . 2 803 . 75 PRO HB3 H 1.78 . 2 804 . 75 PRO CG C 27.0 . 1 805 . 75 PRO HG2 H 1.98 . 1 806 . 75 PRO HG3 H 1.98 . 1 807 . 75 PRO HD2 H 3.67 . 2 808 . 75 PRO HD3 H 3.56 . 2 809 . 76 LYS N N 124.1 . 1 810 . 76 LYS H H 9.09 . 1 811 . 76 LYS CA C 55.8 . 1 812 . 76 LYS HA H 3.99 . 1 813 . 76 LYS CB C 39.0 . 1 814 . 76 LYS HB2 H 1.40 . 2 815 . 76 LYS HB3 H 0.66 . 2 816 . 76 LYS CG C 25.5 . 1 817 . 76 LYS HG2 H 1.06 . 1 818 . 76 LYS HG3 H 1.06 . 1 819 . 76 LYS CD C 28.9 . 1 820 . 76 LYS HD2 H 1.19 . 2 821 . 76 LYS HD3 H 0.96 . 2 822 . 76 LYS CE C 42.4 . 1 823 . 76 LYS HE2 H 2.73 . 2 824 . 76 LYS HE3 H 2.62 . 2 825 . 77 ARG N N 121.6 . 1 826 . 77 ARG H H 6.38 . 1 827 . 77 ARG CA C 55.3 . 1 828 . 77 ARG HA H 4.71 . 1 829 . 77 ARG CB C 32.6 . 1 830 . 77 ARG HB2 H 1.67 . 2 831 . 77 ARG HB3 H 1.42 . 2 832 . 77 ARG CG C 25.9 . 1 833 . 77 ARG HG2 H 1.04 . 2 834 . 77 ARG HG3 H -0.09 . 2 835 . 77 ARG CD C 43.4 . 1 836 . 77 ARG HD2 H 2.84 . 2 837 . 77 ARG HD3 H 2.80 . 2 838 . 77 ARG C C 174.4 . 1 839 . 78 TYR N N 123.8 . 1 840 . 78 TYR H H 9.60 . 1 841 . 78 TYR CA C 59.7 . 1 842 . 78 TYR HA H 4.68 . 1 843 . 78 TYR CB C 41.1 . 1 844 . 78 TYR HB2 H 3.41 . 2 845 . 78 TYR HB3 H 3.11 . 2 846 . 78 TYR HD1 H 6.99 . 1 847 . 78 TYR HD2 H 6.99 . 1 848 . 78 TYR HE1 H 6.79 . 1 849 . 78 TYR HE2 H 6.79 . 1 850 . 78 TYR CD1 C 131.1 . 1 851 . 78 TYR CE1 C 118.0 . 1 852 . 79 ASP N N 123.8 . 1 853 . 79 ASP H H 8.92 . 1 854 . 79 ASP CA C 53.8 . 1 855 . 79 ASP HA H 5.70 . 1 856 . 79 ASP CB C 45.4 . 1 857 . 79 ASP HB2 H 2.90 . 2 858 . 79 ASP HB3 H 2.72 . 2 859 . 80 TRP N N 124.9 . 1 860 . 80 TRP H H 9.29 . 1 861 . 80 TRP CA C 56.1 . 1 862 . 80 TRP HA H 4.72 . 1 863 . 80 TRP CB C 30.2 . 1 864 . 80 TRP HB2 H 2.98 . 2 865 . 80 TRP HB3 H 2.39 . 2 866 . 80 TRP CD2 C 125.8 . 1 867 . 80 TRP CE3 C 120.6 . 1 868 . 80 TRP NE1 N 130.0 . 1 869 . 80 TRP HD1 H 6.92 . 1 870 . 80 TRP HE3 H 5.08 . 1 871 . 80 TRP CZ3 C 119.1 . 1 872 . 80 TRP CZ2 C 113.4 . 1 873 . 80 TRP HE1 H 10.05 . 1 874 . 80 TRP HZ3 H 6.13 . 1 875 . 80 TRP CH2 C 123.9 . 1 876 . 80 TRP HZ2 H 6.93 . 1 877 . 80 TRP HH2 H 6.61 . 1 878 . 80 TRP C C 175.5 . 1 879 . 81 THR N N 118.3 . 1 880 . 81 THR H H 8.29 . 1 881 . 81 THR CA C 61.2 . 1 882 . 81 THR HA H 4.20 . 1 883 . 81 THR CB C 72.2 . 1 884 . 81 THR HB H 4.35 . 1 885 . 81 THR HG2 H 1.18 . 1 886 . 81 THR CG2 C 21.5 . 1 887 . 82 GLY N N 110.4 . 1 888 . 82 GLY H H 4.38 . 1 889 . 82 GLY CA C 45.7 . 1 890 . 82 GLY HA2 H 4.26 . 2 891 . 82 GLY HA3 H 3.16 . 2 892 . 83 LYS N N 117.2 . 1 893 . 83 LYS H H 6.67 . 1 894 . 83 LYS CA C 56.0 . 1 895 . 83 LYS HA H 4.16 . 1 896 . 83 LYS CB C 35.7 . 1 897 . 83 LYS HB2 H 1.45 . 1 898 . 83 LYS HB3 H 1.45 . 1 899 . 83 LYS CG C 23.6 . 1 900 . 83 LYS HG2 H 1.04 . 2 901 . 83 LYS HG3 H 0.86 . 2 902 . 83 LYS CD C 29.1 . 1 903 . 83 LYS HD2 H 1.05 . 1 904 . 83 LYS HD3 H 1.05 . 1 905 . 83 LYS CE C 41.9 . 1 906 . 83 LYS HE2 H 2.82 . 1 907 . 83 LYS HE3 H 2.82 . 1 908 . 83 LYS C C 172.7 . 1 909 . 84 ASN N N 118.0 . 1 910 . 84 ASN H H 6.62 . 1 911 . 84 ASN CA C 51.7 . 1 912 . 84 ASN HA H 4.56 . 1 913 . 84 ASN CB C 37.2 . 1 914 . 84 ASN HB2 H 3.34 . 2 915 . 84 ASN HB3 H 2.81 . 2 916 . 84 ASN ND2 N 117.8 . 1 917 . 84 ASN HD21 H 8.84 . 2 918 . 84 ASN HD22 H 6.94 . 2 919 . 84 ASN C C 172.5 . 1 920 . 85 TRP N N 121.9 . 1 921 . 85 TRP H H 9.02 . 1 922 . 85 TRP CA C 55.2 . 1 923 . 85 TRP HA H 5.77 . 1 924 . 85 TRP CB C 30.1 . 1 925 . 85 TRP HB2 H 3.41 . 2 926 . 85 TRP HB3 H 3.21 . 2 927 . 85 TRP CD2 C 125.6 . 1 928 . 85 TRP CE3 C 119.7 . 1 929 . 85 TRP NE1 N 132.0 . 1 930 . 85 TRP HD1 H 7.63 . 1 931 . 85 TRP HE3 H 7.63 . 1 932 . 85 TRP CZ3 C 121.2 . 1 933 . 85 TRP CZ2 C 112.8 . 1 934 . 85 TRP HE1 H 9.90 . 1 935 . 85 TRP HZ3 H 7.56 . 1 936 . 85 TRP CH2 C 122.5 . 1 937 . 85 TRP HZ2 H 6.50 . 1 938 . 85 TRP HH2 H 6.94 . 1 939 . 85 TRP C C 178.0 . 1 940 . 86 VAL N N 124.1 . 1 941 . 86 VAL H H 9.61 . 1 942 . 86 VAL CA C 62.0 . 1 943 . 86 VAL HA H 4.90 . 1 944 . 86 VAL CB C 37.2 . 1 945 . 86 VAL HB H 1.77 . 1 946 . 86 VAL HG1 H 0.80 . 2 947 . 86 VAL HG2 H 0.75 . 2 948 . 86 VAL CG1 C 22.2 . 1 949 . 86 VAL CG2 C 22.2 . 1 950 . 87 TYR N N 133.0 . 1 951 . 87 TYR H H 7.94 . 1 952 . 87 TYR CA C 54.0 . 1 953 . 87 TYR HA H 5.20 . 1 954 . 87 TYR CB C 37.2 . 1 955 . 87 TYR HB2 H 3.67 . 2 956 . 87 TYR HB3 H 2.55 . 2 957 . 87 TYR HD1 H 7.67 . 1 958 . 87 TYR HD2 H 7.67 . 1 959 . 87 TYR HE1 H 6.97 . 1 960 . 87 TYR HE2 H 6.97 . 1 961 . 87 TYR CD1 C 132.4 . 1 962 . 87 TYR CE1 C 117.1 . 1 963 . 87 TYR C C 174.9 . 1 964 . 88 SER N N 129.4 . 1 965 . 88 SER H H 9.45 . 1 966 . 88 SER CA C 61.7 . 1 967 . 88 SER HA H 3.92 . 1 968 . 88 SER CB C 62.4 . 1 969 . 88 SER HB2 H 3.86 . 1 970 . 88 SER HB3 H 3.86 . 1 971 . 88 SER C C 176.2 . 1 972 . 89 HIS N N 118.5 . 1 973 . 89 HIS H H 5.94 . 1 974 . 89 HIS CA C 58.4 . 1 975 . 89 HIS HA H 4.07 . 1 976 . 89 HIS CB C 30.6 . 1 977 . 89 HIS HB2 H 2.38 . 2 978 . 89 HIS HB3 H 2.15 . 2 979 . 89 HIS CD2 C 118.5 . 1 980 . 89 HIS CE1 C 136.0 . 1 981 . 89 HIS HD2 H 6.95 . 1 982 . 89 HIS HE1 H 8.15 . 1 983 . 89 HIS C C 175.4 . 1 984 . 90 ASP N N 115.2 . 1 985 . 90 ASP H H 6.77 . 1 986 . 90 ASP CA C 53.1 . 1 987 . 90 ASP HA H 4.70 . 1 988 . 90 ASP CB C 42.8 . 1 989 . 90 ASP HB2 H 3.04 . 2 990 . 90 ASP HB3 H 2.44 . 2 991 . 90 ASP C C 175.1 . 1 992 . 91 GLY N N 112.2 . 1 993 . 91 GLY H H 8.67 . 1 994 . 91 GLY CA C 46.5 . 1 995 . 91 GLY HA2 H 4.08 . 2 996 . 91 GLY HA3 H 3.56 . 2 997 . 91 GLY C C 177.3 . 1 998 . 92 VAL N N 126.9 . 1 999 . 92 VAL H H 8.70 . 1 1000 . 92 VAL CA C 63.8 . 1 1001 . 92 VAL HA H 4.12 . 1 1002 . 92 VAL CB C 32.3 . 1 1003 . 92 VAL HB H 2.43 . 1 1004 . 92 VAL HG1 H 1.27 . 2 1005 . 92 VAL HG2 H 0.91 . 2 1006 . 92 VAL CG1 C 21.6 . 1 1007 . 92 VAL CG2 C 21.6 . 1 1008 . 92 VAL C C 173.9 . 1 1009 . 93 SER N N 129.9 . 1 1010 . 93 SER H H 9.25 . 1 1011 . 93 SER CA C 57.9 . 1 1012 . 93 SER HA H 5.61 . 1 1013 . 93 SER CB C 66.3 . 1 1014 . 93 SER HB2 H 4.70 . 2 1015 . 93 SER HB3 H 4.11 . 2 1016 . 93 SER C C 177.9 . 1 1017 . 94 LEU N N 125.8 . 1 1018 . 94 LEU H H 8.31 . 1 1019 . 94 LEU CA C 58.0 . 1 1020 . 94 LEU HA H 3.54 . 1 1021 . 94 LEU CB C 42.6 . 1 1022 . 94 LEU HB2 H 1.43 . 2 1023 . 94 LEU HB3 H 0.39 . 2 1024 . 94 LEU CG C 26.1 . 1 1025 . 94 LEU HG H 0.72 . 1 1026 . 94 LEU HD1 H 0.23 . 2 1027 . 94 LEU HD2 H 0.17 . 2 1028 . 94 LEU CD1 C 24.1 . 1 1029 . 94 LEU CD2 C 25.9 . 1 1030 . 95 HIS N N 117.4 . 1 1031 . 95 HIS H H 7.63 . 1 1032 . 95 HIS CA C 62.2 . 1 1033 . 95 HIS HA H 3.64 . 1 1034 . 95 HIS CB C 30.6 . 1 1035 . 95 HIS HB2 H 2.86 . 1 1036 . 95 HIS HB3 H 2.86 . 1 1037 . 95 HIS CD2 C 115.0 . 1 1038 . 95 HIS CE1 C 137.4 . 1 1039 . 95 HIS HD2 H 6.99 . 1 1040 . 95 HIS HE1 H 7.50 . 1 1041 . 95 HIS C C 176.6 . 1 1042 . 96 GLU N N 124.9 . 1 1043 . 96 GLU H H 8.24 . 1 1044 . 96 GLU CA C 59.5 . 1 1045 . 96 GLU HA H 4.00 . 1 1046 . 96 GLU CB C 30.1 . 1 1047 . 96 GLU HB2 H 2.43 . 2 1048 . 96 GLU HB3 H 2.02 . 2 1049 . 96 GLU CG C 37.0 . 1 1050 . 96 GLU HG2 H 2.33 . 1 1051 . 96 GLU HG3 H 2.33 . 1 1052 . 97 LEU N N 126.3 . 1 1053 . 97 LEU H H 8.50 . 1 1054 . 97 LEU CA C 58.6 . 1 1055 . 97 LEU HA H 4.21 . 1 1056 . 97 LEU CB C 40.8 . 1 1057 . 97 LEU HB2 H 2.17 . 2 1058 . 97 LEU HB3 H 1.93 . 2 1059 . 97 LEU CG C 27.9 . 1 1060 . 97 LEU HG H 1.71 . 1 1061 . 97 LEU HD1 H 0.93 . 1 1062 . 97 LEU HD2 H 0.93 . 1 1063 . 97 LEU CD1 C 24.9 . 1 1064 . 97 LEU CD2 C 25.1 . 1 1065 . 97 LEU C C 174.8 . 1 1066 . 98 LEU N N 119.4 . 1 1067 . 98 LEU H H 8.15 . 1 1068 . 98 LEU CA C 57.9 . 1 1069 . 98 LEU HA H 3.81 . 1 1070 . 98 LEU CB C 42.9 . 1 1071 . 98 LEU HB2 H 1.71 . 2 1072 . 98 LEU HB3 H 1.02 . 2 1073 . 98 LEU CG C 26.5 . 1 1074 . 98 LEU HG H 0.87 . 1 1075 . 98 LEU HD1 H 0.55 . 2 1076 . 98 LEU HD2 H 0.48 . 2 1077 . 98 LEU CD1 C 22.5 . 1 1078 . 98 LEU CD2 C 22.5 . 1 1079 . 98 LEU C C 179.6 . 1 1080 . 99 ALA N N 121.6 . 1 1081 . 99 ALA H H 7.97 . 1 1082 . 99 ALA CA C 56.6 . 1 1083 . 99 ALA HA H 3.72 . 1 1084 . 99 ALA HB H 1.60 . 1 1085 . 99 ALA CB C 18.6 . 1 1086 . 99 ALA C C 178.3 . 1 1087 . 100 ALA N N 124.1 . 1 1088 . 100 ALA H H 7.96 . 1 1089 . 100 ALA CA C 55.8 . 1 1090 . 100 ALA HA H 4.19 . 1 1091 . 100 ALA HB H 1.63 . 1 1092 . 100 ALA CB C 18.3 . 1 1093 . 101 GLU N N 119.1 . 1 1094 . 101 GLU H H 8.91 . 1 1095 . 101 GLU CA C 60.4 . 1 1096 . 101 GLU HA H 4.09 . 1 1097 . 101 GLU CB C 29.8 . 1 1098 . 101 GLU HB2 H 2.35 . 2 1099 . 101 GLU HB3 H 2.14 . 2 1100 . 101 GLU CG C 37.0 . 1 1101 . 101 GLU HG2 H 2.96 . 1 1102 . 101 GLU HG3 H 2.96 . 1 1103 . 102 LEU N N 122.7 . 1 1104 . 102 LEU H H 9.27 . 1 1105 . 102 LEU CA C 58.1 . 1 1106 . 102 LEU HA H 4.19 . 1 1107 . 102 LEU CB C 42.2 . 1 1108 . 102 LEU HB2 H 2.00 . 2 1109 . 102 LEU HB3 H 1.39 . 2 1110 . 102 LEU CG C 26.9 . 1 1111 . 102 LEU HD1 H 0.96 . 2 1112 . 102 LEU HD2 H 0.86 . 2 1113 . 102 LEU CD1 C 23.3 . 1 1114 . 102 LEU CD2 C 23.3 . 1 1115 . 103 THR N N 120.0 . 1 1116 . 103 THR H H 7.92 . 1 1117 . 103 THR CA C 66.1 . 1 1118 . 103 THR HA H 4.86 . 1 1119 . 103 THR CB C 69.7 . 1 1120 . 103 THR HB H 4.37 . 1 1121 . 103 THR HG2 H 1.14 . 1 1122 . 103 THR HG1 H 5.60 . 1 1123 . 103 THR CG2 C 21.5 . 1 1124 . 104 LYS N N 121.6 . 1 1125 . 104 LYS H H 7.07 . 1 1126 . 104 LYS CA C 59.1 . 1 1127 . 104 LYS HA H 4.07 . 1 1128 . 104 LYS CB C 32.8 . 1 1129 . 104 LYS HB2 H 1.90 . 1 1130 . 104 LYS HB3 H 1.90 . 1 1131 . 104 LYS CG C 25.1 . 1 1132 . 104 LYS HG2 H 1.44 . 1 1133 . 104 LYS HG3 H 1.44 . 1 1134 . 104 LYS CD C 29.3 . 1 1135 . 104 LYS HD2 H 1.74 . 2 1136 . 104 LYS HD3 H 1.60 . 2 1137 . 104 LYS CE C 42.0 . 1 1138 . 104 LYS HE2 H 3.07 . 1 1139 . 104 LYS HE3 H 3.07 . 1 1140 . 104 LYS C C 177.4 . 1 1141 . 105 ALA N N 122.7 . 1 1142 . 105 ALA H H 8.25 . 1 1143 . 105 ALA CA C 55.3 . 1 1144 . 105 ALA HA H 4.21 . 1 1145 . 105 ALA HB H 1.62 . 1 1146 . 105 ALA CB C 19.5 . 1 1147 . 106 LEU N N 114.4 . 1 1148 . 106 LEU H H 8.68 . 1 1149 . 106 LEU CA C 54.5 . 1 1150 . 106 LEU HA H 4.38 . 1 1151 . 106 LEU CB C 41.1 . 1 1152 . 106 LEU HB2 H 1.79 . 2 1153 . 106 LEU HB3 H 1.52 . 2 1154 . 106 LEU CG C 27.5 . 1 1155 . 106 LEU HG H 1.75 . 1 1156 . 106 LEU HD1 H 0.93 . 1 1157 . 106 LEU HD2 H 0.93 . 1 1158 . 106 LEU CD1 C 22.6 . 1 1159 . 106 LEU CD2 C 26.0 . 1 1160 . 106 LEU C C 178.7 . 1 1161 . 107 LYS N N 117.7 . 1 1162 . 107 LYS H H 7.48 . 1 1163 . 107 LYS CA C 57.3 . 1 1164 . 107 LYS HA H 3.88 . 1 1165 . 107 LYS CB C 29.0 . 1 1166 . 107 LYS HB2 H 2.05 . 2 1167 . 107 LYS HB3 H 1.91 . 2 1168 . 107 LYS CG C 24.9 . 1 1169 . 107 LYS HG2 H 1.35 . 1 1170 . 107 LYS HG3 H 1.35 . 1 1171 . 107 LYS CD C 29.4 . 1 1172 . 107 LYS HD2 H 1.76 . 1 1173 . 107 LYS HD3 H 1.76 . 1 1174 . 107 LYS CE C 42.3 . 1 1175 . 107 LYS HE2 H 3.10 . 1 1176 . 107 LYS HE3 H 3.10 . 1 1177 . 107 LYS C C 176.5 . 1 1178 . 108 THR N N 116.0 . 1 1179 . 108 THR H H 7.36 . 1 1180 . 108 THR CA C 61.0 . 1 1181 . 108 THR HA H 4.19 . 1 1182 . 108 THR CB C 71.3 . 1 1183 . 108 THR HB H 3.16 . 1 1184 . 108 THR HG2 H 0.08 . 1 1185 . 108 THR CG2 C 17.5 . 1 1186 . 108 THR C C 174.5 . 1 1187 . 109 LYS N N 126.0 . 1 1188 . 109 LYS H H 7.95 . 1 1189 . 109 LYS CA C 57.6 . 1 1190 . 109 LYS HA H 4.11 . 1 1191 . 109 LYS CB C 32.1 . 1 1192 . 109 LYS HB2 H 1.69 . 1 1193 . 109 LYS HB3 H 1.69 . 1 1194 . 109 LYS CG C 24.8 . 1 1195 . 109 LYS HG2 H 1.15 . 1 1196 . 109 LYS HG3 H 1.15 . 1 1197 . 109 LYS CD C 29.2 . 1 1198 . 109 LYS HD2 H 1.34 . 1 1199 . 109 LYS HD3 H 1.34 . 1 1200 . 109 LYS CE C 42.1 . 1 1201 . 109 LYS HE2 H 2.94 . 1 1202 . 109 LYS HE3 H 2.94 . 1 1203 . 109 LYS C C 170.6 . 1 1204 . 110 LEU N N 132.7 . 1 1205 . 110 LEU H H 8.08 . 1 1206 . 110 LEU CA C 53.9 . 1 1207 . 110 LEU HA H 4.66 . 1 1208 . 110 LEU CB C 45.7 . 1 1209 . 110 LEU HB2 H 1.52 . 2 1210 . 110 LEU HB3 H 1.24 . 2 1211 . 110 LEU CG C 27.4 . 1 1212 . 110 LEU HG H 0.80 . 1 1213 . 110 LEU HD1 H 0.85 . 1 1214 . 110 LEU HD2 H 0.85 . 1 1215 . 110 LEU CD1 C 23.9 . 1 1216 . 110 LEU CD2 C 23.9 . 1 1217 . 110 LEU C C 175.8 . 1 1218 . 111 ASP N N 121.3 . 1 1219 . 111 ASP H H 8.29 . 1 1220 . 111 ASP CA C 53.8 . 1 1221 . 111 ASP HA H 4.60 . 1 1222 . 111 ASP CB C 43.6 . 1 1223 . 111 ASP HB2 H 2.72 . 2 1224 . 111 ASP HB3 H 2.43 . 2 1225 . 111 ASP C C 174.5 . 1 1226 . 112 LEU N N 131.0 . 1 1227 . 112 LEU H H 8.12 . 1 1228 . 112 LEU CA C 56.5 . 1 1229 . 112 LEU HA H 4.20 . 1 1230 . 112 LEU CB C 41.3 . 1 1231 . 112 LEU HB2 H 2.04 . 2 1232 . 112 LEU HB3 H 1.20 . 2 1233 . 112 LEU CG C 30.6 . 1 1234 . 112 LEU HG H 0.31 . 1 1235 . 112 LEU HD1 H 0.41 . 2 1236 . 112 LEU HD2 H 0.20 . 2 1237 . 112 LEU CD1 C 24.8 . 1 1238 . 112 LEU CD2 C 27.4 . 1 1239 . 112 LEU C C 175.2 . 1 1240 . 113 SER N N 116.6 . 1 1241 . 113 SER H H 8.35 . 1 1242 . 113 SER CA C 62.2 . 1 1243 . 113 SER HA H 3.84 . 1 1244 . 113 SER CB C 63.3 . 1 1245 . 113 SER HB2 H 3.81 . 1 1246 . 113 SER HB3 H 3.81 . 1 1247 . 114 SER N N 118.3 . 1 1248 . 114 SER H H 8.28 . 1 1249 . 114 SER CA C 58.9 . 1 1250 . 114 SER HA H 4.32 . 1 1251 . 114 SER CB C 63.2 . 1 1252 . 114 SER HB2 H 3.88 . 2 1253 . 114 SER HB3 H 3.80 . 2 1254 . 115 LEU N N 124.1 . 1 1255 . 115 LEU H H 7.03 . 1 1256 . 115 LEU CA C 55.0 . 1 1257 . 115 LEU HA H 4.06 . 1 1258 . 115 LEU CB C 41.1 . 1 1259 . 115 LEU HB2 H 2.00 . 2 1260 . 115 LEU HB3 H 1.59 . 2 1261 . 115 LEU CG C 27.9 . 1 1262 . 115 LEU HG H 1.59 . 1 1263 . 115 LEU HD1 H 0.75 . 2 1264 . 115 LEU HD2 H 0.56 . 2 1265 . 115 LEU CD1 C 22.5 . 1 1266 . 115 LEU CD2 C 25.6 . 1 1267 . 115 LEU C C 173.8 . 1 1268 . 116 ALA N N 124.1 . 1 1269 . 116 ALA H H 7.98 . 1 1270 . 116 ALA CA C 53.2 . 1 1271 . 116 ALA HA H 3.84 . 1 1272 . 116 ALA HB H 1.25 . 1 1273 . 116 ALA CB C 19.4 . 1 1274 . 117 TYR N N 115.8 . 1 1275 . 117 TYR H H 8.44 . 1 1276 . 117 TYR CA C 59.9 . 1 1277 . 117 TYR HA H 4.14 . 1 1278 . 117 TYR CB C 34.4 . 1 1279 . 117 TYR HB2 H 3.58 . 1 1280 . 117 TYR HB3 H 3.58 . 1 1281 . 117 TYR HD1 H 7.23 . 1 1282 . 117 TYR HD2 H 7.23 . 1 1283 . 117 TYR HE1 H 6.96 . 1 1284 . 117 TYR HE2 H 6.96 . 1 1285 . 117 TYR CD1 C 132.3 . 1 1286 . 117 TYR CE1 C 116.7 . 1 1287 . 117 TYR C C 177.9 . 1 1288 . 118 SER N N 113.0 . 1 1289 . 118 SER H H 7.50 . 1 1290 . 118 SER CA C 59.2 . 1 1291 . 118 SER HA H 3.39 . 1 1292 . 118 SER CB C 63.3 . 1 1293 . 118 SER HB2 H 3.49 . 2 1294 . 118 SER HB3 H 3.26 . 2 1295 . 118 SER C C 175.0 . 1 1296 . 119 GLY N N 114.1 . 1 1297 . 119 GLY H H 8.87 . 1 1298 . 119 GLY CA C 45.6 . 1 1299 . 119 GLY HA2 H 4.10 . 2 1300 . 119 GLY HA3 H 3.49 . 2 1301 . 119 GLY C C 177.3 . 1 1302 . 120 LYS N N 124.2 . 1 1303 . 120 LYS H H 7.97 . 1 1304 . 120 LYS CA C 56.1 . 1 1305 . 120 LYS HA H 4.26 . 1 1306 . 120 LYS CB C 32.8 . 1 1307 . 120 LYS HB2 H 1.78 . 2 1308 . 120 LYS HB3 H 1.67 . 2 1309 . 120 LYS CG C 24.1 . 1 1310 . 120 LYS HG2 H 1.35 . 1 1311 . 120 LYS HG3 H 1.35 . 1 1312 . 120 LYS CD C 28.7 . 1 1313 . 120 LYS HD2 H 1.58 . 1 1314 . 120 LYS HD3 H 1.58 . 1 1315 . 120 LYS CE C 41.9 . 1 1316 . 120 LYS HE2 H 2.93 . 1 1317 . 120 LYS HE3 H 2.93 . 1 1318 . 121 ASP N N 125.2 . 1 1319 . 121 ASP H H 8.57 . 1 1320 . 121 ASP CA C 54.5 . 1 1321 . 121 ASP HA H 4.50 . 1 1322 . 121 ASP CB C 41.0 . 1 1323 . 121 ASP HB2 H 2.70 . 2 1324 . 121 ASP HB3 H 2.51 . 2 1325 . 122 ALA N N 131.6 . 1 1326 . 122 ALA H H 7.73 . 1 1327 . 122 ALA CA C 53.8 . 1 1328 . 122 ALA HA H 4.07 . 1 1329 . 122 ALA HB H 1.25 . 1 1330 . 122 ALA CB C 20.7 . 1 1331 . 122 ALA C C 174.5 . 1 stop_ save_