data_4309 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Backbone NMR Assignment and Secondary Structure of the 19 kDa Hemophore HasA ; _BMRB_accession_number 4309 _BMRB_flat_file_name bmr4309.str _Entry_type original _Submission_date 1999-02-18 _Accession_date 1999-02-18 _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 Izadi-Pruneyre Nadia . . 2 Wolff Nicolas . . 3 Castagne Claire . . 4 Czisch Michael . . 5 Wandersman Cecile . . 6 Delepierre Muriel . . 7 Lecroisey Anne . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 369 "13C chemical shifts" 337 "15N chemical shifts" 172 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 1999-08-12 original author . stop_ _Original_release_date 1999-08-12 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full ; Izadi-Pruneyre, N., Wolff, N., Castagne, C., Czisch, M., Wandersman, C., Delepierre, M., and Lecroisey, A., "Backbone NMR Assignment and Secondary Structure of the 19 kDa Hemophore HasA," J. Biomol. NMR 14, 193-194 (1999). ; _Citation_title 'Backbone NMR Assignment and Secondary Structure of the 19 kDa Hemophore HasA' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code 99356755 _PubMed_ID ? loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Izadi-Pruneyre Nadia . . 2 Wolff Nicolas . . 3 Castagne Claire . . 4 Czisch Michael . . 5 Wandersman Cecile . . 6 Delepierre Muriel . . 7 Lecroisey Anne . . stop_ _Journal_abbreviation 'J. Biomol. NMR' _Journal_name_full 'Journal of Biomolecular NMR' _Journal_volume 14 _Journal_issue . _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 193 _Page_last 194 _Year 1999 _Details . loop_ _Keyword 'HasA protein' 'nmr assignment' stop_ save_ ################################## # Molecular system description # ################################## save_system_HasA _Saveframe_category molecular_system _Mol_system_name HasA _Abbreviation_common HasA _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label HasA $HasA stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state monomer _System_paramagnetic no _System_thiol_state . _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_HasA _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common HasA _Abbreviation_common HasA _Molecular_mass 18284.7 _Mol_thiol_state . _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 178 _Mol_residue_sequence ; AFSVNYDSSFGGYSIHDYLG QWASTFGDVNHTNGNVTDAN SGGFYGGSLSGSQYAISSTA NQVTAFVAGGNLTYTLFNEP AHTLYGQLDSLSFGDGLSGG DTSPYSIQVPDVSFGGLNLS SLQAQGHDGVVHQVVYGLMS GDTGALETALNGILDDYGLS VNSTFDQVAAATAVGVQH ; loop_ _Residue_seq_code _Residue_label 1 ALA 2 PHE 3 SER 4 VAL 5 ASN 6 TYR 7 ASP 8 SER 9 SER 10 PHE 11 GLY 12 GLY 13 TYR 14 SER 15 ILE 16 HIS 17 ASP 18 TYR 19 LEU 20 GLY 21 GLN 22 TRP 23 ALA 24 SER 25 THR 26 PHE 27 GLY 28 ASP 29 VAL 30 ASN 31 HIS 32 THR 33 ASN 34 GLY 35 ASN 36 VAL 37 THR 38 ASP 39 ALA 40 ASN 41 SER 42 GLY 43 GLY 44 PHE 45 TYR 46 GLY 47 GLY 48 SER 49 LEU 50 SER 51 GLY 52 SER 53 GLN 54 TYR 55 ALA 56 ILE 57 SER 58 SER 59 THR 60 ALA 61 ASN 62 GLN 63 VAL 64 THR 65 ALA 66 PHE 67 VAL 68 ALA 69 GLY 70 GLY 71 ASN 72 LEU 73 THR 74 TYR 75 THR 76 LEU 77 PHE 78 ASN 79 GLU 80 PRO 81 ALA 82 HIS 83 THR 84 LEU 85 TYR 86 GLY 87 GLN 88 LEU 89 ASP 90 SER 91 LEU 92 SER 93 PHE 94 GLY 95 ASP 96 GLY 97 LEU 98 SER 99 GLY 100 GLY 101 ASP 102 THR 103 SER 104 PRO 105 TYR 106 SER 107 ILE 108 GLN 109 VAL 110 PRO 111 ASP 112 VAL 113 SER 114 PHE 115 GLY 116 GLY 117 LEU 118 ASN 119 LEU 120 SER 121 SER 122 LEU 123 GLN 124 ALA 125 GLN 126 GLY 127 HIS 128 ASP 129 GLY 130 VAL 131 VAL 132 HIS 133 GLN 134 VAL 135 VAL 136 TYR 137 GLY 138 LEU 139 MET 140 SER 141 GLY 142 ASP 143 THR 144 GLY 145 ALA 146 LEU 147 GLU 148 THR 149 ALA 150 LEU 151 ASN 152 GLY 153 ILE 154 LEU 155 ASP 156 ASP 157 TYR 158 GLY 159 LEU 160 SER 161 VAL 162 ASN 163 SER 164 THR 165 PHE 166 ASP 167 GLN 168 VAL 169 ALA 170 ALA 171 ALA 172 THR 173 ALA 174 VAL 175 GLY 176 VAL 177 GLN 178 HIS stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-10-06 loop_ _Database_name _Database_accession_code _Database_entry_mol_name _Sequence_query_to_submitted_percentage _Sequence_subject_length _Sequence_identity _Sequence_positive _Sequence_homology_expectation_value PDB 1B2V "Heme-binding Protein A" 100.00 188 100.00 100.00 2.27e-118 PDB 1DK0 "Crystal Structure Of The Hemophore Hasa From Serratia Marcescens Crystal Form P2(1), Ph8" 100.00 188 100.00 100.00 2.27e-118 PDB 1DKH "Crystal Structure Of The Hemophore Hasa, Ph 6.5" 100.00 188 100.00 100.00 2.27e-118 PDB 1YBJ "Structural And Dynamics Studies Of Both Apo And Holo Forms Of The Hemophore Hasa" 100.00 178 100.00 100.00 2.54e-118 PDB 2CN4 "The Crystal Structure Of The Secreted Dimeric Form Of The Hemophore Hasa Reveals A Domain Swapping With An Exchanged Heme Ligan" 97.19 173 100.00 100.00 2.19e-114 PDB 2UYD "Crystal Structure Of The Smhasa Mutant H83a" 100.00 188 99.44 99.44 2.59e-117 PDB 3CSL "Structure Of The Serratia Marcescens Hemophore Receptor Hasr In Complex With Its Hemophore Hasa And Heme" 100.00 206 100.00 100.00 2.01e-118 PDB 3CSN "Structure Of The Serratia Marcescens Hemophore Receptor Hasr In Complex With Its Hemophore Hasa" 100.00 206 100.00 100.00 2.01e-118 PDB 3DDR "Structure Of The Serratia Marcescens Hemophore Receptor Hasr-Ile671gly Mutant In Complex With Its Hemophore Hasa And Heme" 100.00 206 100.00 100.00 2.01e-118 EMBL CAA57068 "hasA [Serratia marcescens]" 100.00 188 100.00 100.00 2.27e-118 GB KFD10589 "hemophore [Serratia marcescens subsp. marcescens ATCC 13880]" 100.00 188 100.00 100.00 2.27e-118 GB KFL05309 "hemophore HasA [Serratia marcescens]" 100.00 188 100.00 100.00 2.27e-118 REF WP_016928898 "MULTISPECIES: hemophore HasA [Serratia]" 100.00 188 100.00 100.00 2.27e-118 SP Q54450 "RecName: Full=Hemophore HasA; AltName: Full=Heme acquisition system protein A" 100.00 188 100.00 100.00 2.27e-118 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $HasA Enterobacteria 615 Eubacteria . Serratia marcescens 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 $HasA 'recombinant technology' 'E. Coli' Escherichia coli Pop3 plasmid pSYC34 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 $HasA 2.0 mM '[U-95% 15N]' stop_ save_ save_sample_2 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $HasA 2.0 mM '[15N 95%]-Leu' stop_ save_ save_sample_3 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $HasA 2.0 mM '[U-95% 13C; U-95% 15N]' stop_ save_ ############################ # Computer software used # ############################ save_XEASY _Saveframe_category software _Name XEASY _Version 1.2 _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model Unity _Field_strength 500 _Details . save_ ############################# # NMR applied experiments # ############################# save_1H-15N_HSQC_1 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-15N HSQC' _Sample_label . save_ save_1H-15N_TOCSY-HSQC_2 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-15N TOCSY-HSQC' _Sample_label . save_ save_1H-15N_NOESY-HSQC_3 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-15N NOESY-HSQC' _Sample_label . save_ save_HNCACB_4 _Saveframe_category NMR_applied_experiment _Experiment_name HNCACB _Sample_label . save_ save_CBCA(CO)NH_5 _Saveframe_category NMR_applied_experiment _Experiment_name CBCA(CO)NH _Sample_label . save_ save_HNCO_6 _Saveframe_category NMR_applied_experiment _Experiment_name HNCO _Sample_label . save_ save_1H-15N_HMQC-J_7 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-15N HMQC-J' _Sample_label . save_ save_NMR_spec_expt__0_1 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-15N HSQC' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_2 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-15N TOCSY-HSQC' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_3 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-15N NOESY-HSQC' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_4 _Saveframe_category NMR_applied_experiment _Experiment_name HNCACB _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_5 _Saveframe_category NMR_applied_experiment _Experiment_name CBCA(CO)NH _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_6 _Saveframe_category NMR_applied_experiment _Experiment_name HNCO _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_7 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-15N HMQC-J' _BMRB_pulse_sequence_accession_number . _Details . save_ ####################### # Sample conditions # ####################### save_Ex-condition _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 5.6 0.1 na temperature 303 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 _Indirect_shift_ratio_citation_label _Correction_value_citation_label DSS C 13 'methyl protons' ppm 0.0 . indirect . . . 0.251449530 $entry_citation $entry_citation TMS H 1 'methyl protons' ppm 0 external direct cylindrical external_to_the_sample parallel_to_Bo . $entry_citation $entry_citation DSS N 15 'methyl protons' ppm 0.0 . indirect . . . 0.101329118 $entry_citation $entry_citation 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_shift_set _Saveframe_category assigned_chemical_shifts _Details . loop_ _Sample_label $sample_1 $sample_2 $sample_3 stop_ _Sample_conditions_label $Ex-condition _Chem_shift_reference_set_label $chemical_shift_reference _Mol_system_component_name HasA _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 ALA H H 8.14 . 1 2 . 1 ALA HA H 4.85 . 1 3 . 1 ALA C C 173.2 . 1 4 . 1 ALA CA C 51.7 . 1 5 . 1 ALA N N 121.9 . 1 6 . 2 PHE H H 8.73 . 1 7 . 2 PHE HA H 5.14 . 1 8 . 2 PHE C C 180.3 . 1 9 . 2 PHE CA C 58.0 . 1 10 . 2 PHE N N 125.4 . 1 11 . 3 SER H H 8.02 . 1 12 . 3 SER HA H 4.45 . 1 13 . 3 SER C C 171.7 . 1 14 . 3 SER CA C 56.5 . 1 15 . 3 SER N N 122.67 . 1 16 . 4 VAL H H 8.39 . 1 17 . 4 VAL HA H 5.08 . 1 18 . 4 VAL C C 173.1 . 1 19 . 4 VAL CA C 58.7 . 1 20 . 4 VAL N N 115.8 . 1 21 . 5 ASN H H 8.57 . 1 22 . 5 ASN HA H 4.86 . 1 23 . 5 ASN C C 173.0 . 1 24 . 5 ASN CA C 52.3 . 1 25 . 5 ASN N N 124.3 . 1 26 . 6 TYR H H 7.86 . 1 27 . 6 TYR HA H 5.10 . 1 28 . 6 TYR C C 173.8 . 1 29 . 6 TYR CA C 54.7 . 1 30 . 6 TYR N N 120.1 . 1 31 . 7 ASP H H 8.33 . 1 32 . 7 ASP HA H 4.41 . 1 33 . 7 ASP C C 178.0 . 1 34 . 7 ASP CA C 54.9 . 1 35 . 7 ASP N N 123.7 . 1 36 . 8 SER H H 8.83 . 1 37 . 8 SER HA H 4.05 . 1 38 . 8 SER C C 176.4 . 1 39 . 8 SER CA C 61.8 . 1 40 . 8 SER N N 124.2 . 1 41 . 9 SER H H 8.76 . 1 42 . 9 SER HA H 4.08 . 1 43 . 9 SER C C 176.0 . 1 44 . 9 SER CA C 62.6 . 1 45 . 9 SER N N 121.8 . 1 46 . 10 PHE H H 8.29 . 1 47 . 10 PHE HA H 4.64 . 1 48 . 10 PHE C C 176.8 . 1 49 . 10 PHE CA C 58.0 . 1 50 . 10 PHE N N 120.8 . 1 51 . 11 GLY H H 8.01 . 1 52 . 11 GLY HA2 H 3.67 . 2 53 . 11 GLY HA3 H 4.24 . 2 54 . 11 GLY C C 173.8 . 1 55 . 11 GLY CA C 49.4 . 1 56 . 11 GLY N N 108.4 . 1 57 . 12 GLY H H 8.61 . 1 58 . 12 GLY HA2 H 3.68 . 2 59 . 12 GLY HA3 H 4.53 . 2 60 . 12 GLY C C 175.6 . 1 61 . 12 GLY CA C 44.6 . 1 62 . 12 GLY N N 104.3 . 1 63 . 13 TYR H H 8.40 . 1 64 . 13 TYR HA H 4.80 . 1 65 . 13 TYR C C 176.6 . 1 66 . 13 TYR CA C 57.4 . 1 67 . 13 TYR N N 125.0 . 1 68 . 14 SER H H 9.11 . 1 69 . 14 SER HA H 4.85 . 1 70 . 14 SER C C 175.5 . 1 71 . 14 SER CA C 56.4 . 1 72 . 14 SER N N 116.3 . 1 73 . 15 ILE H H 7.55 . 1 74 . 15 ILE HA H 3.61 . 1 75 . 15 ILE C C 177.6 . 1 76 . 15 ILE CA C 65.1 . 1 77 . 15 ILE N N 124.0 . 1 78 . 16 HIS H H 8.99 . 1 79 . 16 HIS HA H 4.73 . 1 80 . 16 HIS C C 179.7 . 1 81 . 16 HIS CA C 57.3 . 1 82 . 16 HIS N N 118.6 . 1 83 . 17 ASP H H 8.68 . 1 84 . 17 ASP HA H 3.93 . 1 85 . 17 ASP N N 122.8 . 1 86 . 18 TYR C C 176.1 . 1 87 . 18 TYR CA C 63.3 . 1 88 . 19 LEU H H 8.54 . 1 89 . 19 LEU HA H 3.58 . 1 90 . 19 LEU C C 178.6 . 1 91 . 19 LEU CA C 57.7 . 1 92 . 19 LEU N N 120.8 . 1 93 . 20 GLY H H 8.01 . 1 94 . 20 GLY HA2 H 3.85 . 2 95 . 20 GLY HA3 H 3.67 . 2 96 . 20 GLY C C 176.5 . 1 97 . 20 GLY CA C 46.6 . 1 98 . 20 GLY N N 107.1 . 1 99 . 21 GLN H H 7.65 . 1 100 . 21 GLN HA H 4.11 . 1 101 . 21 GLN C C 176.2 . 1 102 . 21 GLN CA C 59.0 . 1 103 . 21 GLN N N 126.9 . 1 104 . 22 TRP H H 8.89 . 1 105 . 22 TRP HA H 4.17 . 1 106 . 22 TRP C C 176.6 . 1 107 . 22 TRP CA C 62.7 . 1 108 . 22 TRP N N 126.6 . 1 109 . 23 ALA H H 8.73 . 1 110 . 23 ALA HA H 4.33 . 1 111 . 23 ALA C C 180.8 . 1 112 . 23 ALA CA C 55.6 . 1 113 . 23 ALA N N 122.8 . 1 114 . 24 SER H H 7.97 . 1 115 . 24 SER HA H 4.08 . 1 116 . 24 SER C C 177.5 . 1 117 . 24 SER CA C 61.2 . 1 118 . 24 SER N N 115.6 . 1 119 . 25 THR H H 8.10 . 1 120 . 25 THR HA H 3.77 . 1 121 . 25 THR C C 176.5 . 1 122 . 25 THR CA C 66.3 . 1 123 . 25 THR N N 120.7 . 1 124 . 26 PHE H H 8.89 . 1 125 . 26 PHE C C 176.4 . 1 126 . 26 PHE CA C 61.4 . 1 127 . 26 PHE N N 124.5 . 1 128 . 27 GLY H H 7.27 . 1 129 . 27 GLY HA2 H 3.67 . 1 130 . 27 GLY HA3 H 4.10 . 1 131 . 27 GLY C C 172.7 . 1 132 . 27 GLY CA C 44.6 . 1 133 . 27 GLY N N 105.0 . 1 134 . 28 ASP H H 7.21 . 1 135 . 28 ASP HA H 4.67 . 1 136 . 28 ASP C C 178.2 . 1 137 . 28 ASP CA C 53.1 . 1 138 . 28 ASP N N 121.7 . 1 139 . 29 VAL H H 8.64 . 1 140 . 29 VAL HA H 3.80 . 1 141 . 29 VAL C C 175.8 . 1 142 . 29 VAL CA C 63.3 . 1 143 . 29 VAL N N 127.1 . 1 144 . 30 ASN H H 8.50 . 1 145 . 30 ASN HA H 4.77 . 1 146 . 30 ASN C C 175.2 . 1 147 . 30 ASN CA C 53.1 . 1 148 . 30 ASN N N 117.5 . 1 149 . 31 HIS H H 7.13 . 1 150 . 31 HIS HA H 4.54 . 1 151 . 31 HIS C C 179.9 . 1 152 . 31 HIS CA C 57.2 . 1 153 . 31 HIS N N 120.5 . 1 154 . 32 THR H H 7.64 . 1 155 . 32 THR HA H 4.11 . 1 156 . 32 THR C C 172.2 . 1 157 . 32 THR CA C 59.1 . 1 158 . 32 THR N N 118.7 . 1 159 . 33 ASN H H 8.72 . 1 160 . 33 ASN HA H 4.48 . 1 161 . 33 ASN CA C 53.4 . 1 162 . 33 ASN N N 118.3 . 1 163 . 34 GLY H H 8.93 . 1 164 . 34 GLY HA2 H 3.99 . 1 165 . 34 GLY HA3 H 3.82 . 1 166 . 34 GLY C C 174.2 . 1 167 . 34 GLY CA C 46.3 . 1 168 . 34 GLY N N 115.8 . 1 169 . 35 ASN H H 8.59 . 1 170 . 35 ASN HA H 4.35 . 1 171 . 35 ASN C C 174.4 . 1 172 . 35 ASN CA C 53.4 . 1 173 . 35 ASN N N 117.8 . 1 174 . 36 VAL H H 7.53 . 1 175 . 36 VAL HA H 4.23 . 1 176 . 36 VAL C C 175.6 . 1 177 . 36 VAL CA C 61.6 . 1 178 . 36 VAL N N 121.5 . 1 179 . 37 THR H H 8.83 . 1 180 . 37 THR HA H 4.45 . 1 181 . 37 THR C C 173.9 . 1 182 . 37 THR CA C 61.0 . 1 183 . 37 THR N N 120.6 . 1 184 . 38 ASP H H 8.38 . 1 185 . 38 ASP HA H 4.57 . 1 186 . 38 ASP C C 174.6 . 1 187 . 38 ASP CA C 54.3 . 1 188 . 38 ASP N N 124.7 . 1 189 . 39 ALA H H 8.39 . 1 190 . 39 ALA HA H 4.17 . 1 191 . 39 ALA C C 175.1 . 1 192 . 39 ALA CA C 51.8 . 1 193 . 39 ALA N N 125.4 . 1 194 . 40 ASN H H 8.14 . 1 195 . 40 ASN HA H 4.85 . 1 196 . 40 ASN C C 176.4 . 1 197 . 40 ASN CA C 53.4 . 1 198 . 40 ASN N N 121.9 . 1 199 . 41 SER H H 8.62 . 1 200 . 41 SER HA H 4.35 . 1 201 . 41 SER C C 173.5 . 1 202 . 41 SER N N 118.3 . 1 203 . 42 GLY H H 8.38 . 1 204 . 42 GLY HA2 H 3.22 . 2 205 . 42 GLY HA3 H 3.69 . 2 206 . 42 GLY C C 172.6 . 1 207 . 42 GLY CA C 44.4 . 1 208 . 42 GLY N N 110.9 . 1 209 . 43 GLY H H 8.40 . 1 210 . 43 GLY HA2 H 3.43 . 2 211 . 43 GLY HA3 H 4.60 . 2 212 . 43 GLY C C 172.7 . 1 213 . 43 GLY CA C 43.8 . 1 214 . 43 GLY N N 109.1 . 1 215 . 44 PHE H H 8.65 . 1 216 . 44 PHE HA H 5.42 . 1 217 . 44 PHE CA C 58.5 . 1 218 . 44 PHE N N 119.2 . 1 219 . 45 TYR H H 8.67 . 1 220 . 45 TYR HA H 3.54 . 1 221 . 45 TYR C C 175.0 . 1 222 . 45 TYR CA C 58.0 . 1 223 . 45 TYR N N 123.1 . 1 224 . 46 GLY H H 8.48 . 1 225 . 46 GLY HA2 H 3.29 . 2 226 . 46 GLY HA3 H 4.42 . 2 227 . 46 GLY C C 173.6 . 1 228 . 46 GLY CA C 44.6 . 1 229 . 46 GLY N N 116.9 . 1 230 . 47 GLY H H 7.61 . 1 231 . 47 GLY HA2 H 4.00 . 2 232 . 47 GLY HA3 H 4.13 . 2 233 . 47 GLY C C 171.9 . 1 234 . 47 GLY CA C 45.1 . 1 235 . 47 GLY N N 111.8 . 1 236 . 48 SER H H 8.25 . 1 237 . 48 SER HA H 4.66 . 1 238 . 48 SER C C 175.1 . 1 239 . 48 SER CA C 59.8 . 1 240 . 48 SER N N 114.7 . 1 241 . 49 LEU H H 8.14 . 1 242 . 49 LEU HA H 4.48 . 1 243 . 49 LEU N N 121.83 . 1 244 . 49 LEU CA C 52.4 . 1 245 . 50 SER HA H 4.43 . 1 246 . 50 SER C C 172.0 . 1 247 . 50 SER CA C 56.0 . 1 248 . 51 GLY H H 8.52 . 1 249 . 51 GLY HA2 H 4.04 . 1 250 . 51 GLY HA3 H 4.76 . 1 251 . 51 GLY C C 172.5 . 1 252 . 51 GLY CA C 45.5 . 1 253 . 51 GLY N N 105.4 . 1 254 . 52 SER H H 8.43 . 1 255 . 52 SER HA H 5.26 . 1 256 . 52 SER C C 176.5 . 1 257 . 52 SER CA C 57.8 . 1 258 . 52 SER N N 114.2 . 1 259 . 53 GLN H H 8.12 . 1 260 . 53 GLN HA H 5.73 . 1 261 . 53 GLN C C 174.7 . 1 262 . 53 GLN CA C 54.2 . 1 263 . 53 GLN N N 119.1 . 1 264 . 54 TYR H H 9.04 . 1 265 . 54 TYR HA H 4.60 . 1 266 . 54 TYR C C 172.0 . 1 267 . 54 TYR CA C 56.5 . 1 268 . 54 TYR N N 123.5 . 1 269 . 55 ALA H H 8.25 . 1 270 . 55 ALA HA H 4.41 . 1 271 . 55 ALA C C 174.1 . 1 272 . 55 ALA CA C 49.4 . 1 273 . 55 ALA N N 132.4 . 1 274 . 56 ILE H H 7.46 . 1 275 . 56 ILE HA H 4.04 . 1 276 . 56 ILE C C 174.4 . 1 277 . 56 ILE CA C 57.7 . 1 278 . 56 ILE N N 122.2 . 1 279 . 57 SER H H 7.64 . 1 280 . 57 SER HA H 3.49 . 1 281 . 57 SER C C 174.3 . 1 282 . 57 SER CA C 55.1 . 1 283 . 57 SER N N 118.7 . 1 284 . 58 SER H H 8.65 . 1 285 . 58 SER HA H 3.18 . 1 286 . 58 SER C C 177.4 . 1 287 . 58 SER CA C 57.6 . 1 288 . 58 SER N N 117.8 . 1 289 . 59 THR H H 8.43 . 1 290 . 59 THR HA H 4.18 . 1 291 . 59 THR C C 175.0 . 1 292 . 59 THR CA C 63.8 . 1 293 . 59 THR N N 125.6 . 1 294 . 60 ALA H H 7.90 . 1 295 . 60 ALA HA H 4.17 . 1 296 . 60 ALA C C 178.3 . 1 297 . 60 ALA CA C 54.0 . 1 298 . 60 ALA N N 126.4 . 1 299 . 61 ASN H H 7.52 . 1 300 . 61 ASN HA H 4.94 . 1 301 . 61 ASN C C 174.6 . 1 302 . 61 ASN CA C 52.0 . 1 303 . 61 ASN N N 109.9 . 1 304 . 62 GLN H H 7.72 . 1 305 . 62 GLN HA H 4.83 . 1 306 . 62 GLN C C 175.0 . 1 307 . 62 GLN CA C 58.1 . 1 308 . 62 GLN N N 114.4 . 1 309 . 63 VAL H H 9.05 . 1 310 . 63 VAL HA H 4.33 . 1 311 . 63 VAL C C 175.8 . 1 312 . 63 VAL CA C 64.5 . 1 313 . 63 VAL N N 118.9 . 1 314 . 64 THR H H 8.81 . 1 315 . 64 THR HA H 4.89 . 1 316 . 64 THR C C 174.0 . 1 317 . 64 THR CA C 66.5 . 1 318 . 64 THR N N 126.4 . 1 319 . 65 ALA H H 9.60 . 1 320 . 65 ALA HA H 5.81 . 1 321 . 65 ALA C C 177.0 . 1 322 . 65 ALA CA C 52.2 . 1 323 . 65 ALA N N 129.5 . 1 324 . 66 PHE H H 8.37 . 1 325 . 66 PHE HA H 5.42 . 1 326 . 66 PHE C C 172.6 . 1 327 . 66 PHE CA C 56.8 . 1 328 . 66 PHE N N 114.9 . 1 329 . 67 VAL H H 8.44 . 1 330 . 67 VAL HA H 4.08 . 1 331 . 67 VAL C C 175.5 . 1 332 . 67 VAL CA C 61.4 . 1 333 . 67 VAL N N 118.0 . 1 334 . 68 ALA H H 9.50 . 1 335 . 68 ALA HA H 5.31 . 1 336 . 68 ALA C C 175.3 . 1 337 . 68 ALA CA C 50.0 . 1 338 . 68 ALA N N 136.4 . 1 339 . 69 GLY H H 9.14 . 1 340 . 69 GLY HA2 H 3.70 . 2 341 . 69 GLY HA3 H 5.35 . 2 342 . 69 GLY C C 173.5 . 1 343 . 69 GLY CA C 43.5 . 1 344 . 69 GLY N N 112.0 . 1 345 . 70 GLY H H 8.63 . 1 346 . 70 GLY HA2 H 3.82 . 2 347 . 70 GLY HA3 H 4.79 . 2 348 . 70 GLY C C 172.0 . 1 349 . 70 GLY CA C 46.4 . 1 350 . 70 GLY N N 113.7 . 1 351 . 71 ASN H H 9.39 . 1 352 . 71 ASN HA H 4.97 . 1 353 . 71 ASN C C 174.1 . 1 354 . 71 ASN CA C 53.8 . 1 355 . 71 ASN N N 127.6 . 1 356 . 72 LEU H H 8.73 . 1 357 . 72 LEU HA H 5.05 . 1 358 . 72 LEU C C 177.8 . 1 359 . 72 LEU CA C 54.2 . 1 360 . 72 LEU N N 128.5 . 1 361 . 73 THR H H 8.40 . 1 362 . 73 THR HA H 4.36 . 1 363 . 73 THR C C 170.5 . 1 364 . 73 THR CA C 62.4 . 1 365 . 73 THR N N 118.5 . 1 366 . 74 TYR H H 8.83 . 1 367 . 74 TYR HA H 5.98 . 1 368 . 74 TYR C C 176.8 . 1 369 . 74 TYR CA C 54.4 . 1 370 . 74 TYR N N 128.3 . 1 371 . 75 THR H H 9.08 . 1 372 . 75 THR HA H 4.02 . 1 373 . 75 THR C C 175.7 . 1 374 . 75 THR CA C 63.0 . 1 375 . 75 THR N N 117.4 . 1 376 . 76 LEU H H 5.99 . 1 377 . 76 LEU HA H 3.10 . 1 378 . 76 LEU CA C 57.5 . 1 379 . 76 LEU N N 120.8 . 1 380 . 77 PHE C C 176.7 . 1 381 . 77 PHE CA C 57.8 . 1 382 . 78 ASN H H 8.12 . 1 383 . 78 ASN HA H 4.48 . 1 384 . 78 ASN C C 173.2 . 1 385 . 78 ASN CA C 54.4 . 1 386 . 78 ASN N N 122.4 . 1 387 . 79 GLU H H 8.16 . 1 388 . 79 GLU HA H 4.27 . 1 389 . 79 GLU CA C 54.0 . 1 390 . 79 GLU N N 120.3 . 1 391 . 80 PRO C C 177.4 . 1 392 . 80 PRO CA C 61.8 . 1 393 . 81 ALA H H 8.49 . 1 394 . 81 ALA HA H 3.99 . 1 395 . 81 ALA C C 177.6 . 1 396 . 81 ALA CA C 53.1 . 1 397 . 81 ALA N N 134.3 . 1 398 . 82 HIS H H 9.15 . 1 399 . 82 HIS HA H 3.57 . 1 400 . 82 HIS C C 173.9 . 1 401 . 82 HIS CA C 57.4 . 1 402 . 82 HIS N N 120.3 . 1 403 . 83 THR H H 8.23 . 1 404 . 83 THR HA H 4.01 . 1 405 . 83 THR C C 173.3 . 1 406 . 83 THR CA C 62.8 . 1 407 . 83 THR N N 117.5 . 1 408 . 84 LEU H H 11.10 . 1 409 . 84 LEU HA H 5.64 . 1 410 . 84 LEU C C 175.2 . 1 411 . 84 LEU CA C 53.6 . 1 412 . 84 LEU N N 136.0 . 1 413 . 85 TYR H H 9.51 . 1 414 . 85 TYR HA H 4.86 . 1 415 . 85 TYR C C 171.2 . 1 416 . 85 TYR CA C 55.8 . 1 417 . 85 TYR N N 125.7 . 1 418 . 86 GLY H H 7.64 . 1 419 . 86 GLY HA2 H 3.72 . 2 420 . 86 GLY HA3 H 5.20 . 2 421 . 86 GLY C C 171.5 . 1 422 . 86 GLY CA C 43.9 . 1 423 . 86 GLY N N 107.5 . 1 424 . 87 GLN H H 8.74 . 1 425 . 87 GLN HA H 4.98 . 1 426 . 87 GLN C C 173.7 . 1 427 . 87 GLN CA C 54.7 . 1 428 . 87 GLN N N 124.3 . 1 429 . 88 LEU H H 9.29 . 1 430 . 88 LEU HA H 4.67 . 1 431 . 88 LEU C C 172.7 . 1 432 . 88 LEU CA C 53.9 . 1 433 . 88 LEU N N 129.1 . 1 434 . 89 ASP H H 9.40 . 1 435 . 89 ASP HA H 5.17 . 1 436 . 89 ASP C C 175.9 . 1 437 . 89 ASP CA C 55.1 . 1 438 . 89 ASP N N 126.8 . 1 439 . 90 SER H H 8.57 . 1 440 . 90 SER HA H 5.57 . 1 441 . 90 SER C C 171.5 . 1 442 . 90 SER CA C 56.3 . 1 443 . 90 SER N N 113.3 . 1 444 . 91 LEU H H 8.75 . 1 445 . 91 LEU HA H 5.17 . 1 446 . 91 LEU C C 174.7 . 1 447 . 91 LEU CA C 53.9 . 1 448 . 91 LEU N N 123.4 . 1 449 . 92 SER H H 8.29 . 1 450 . 92 SER HA H 5.05 . 1 451 . 92 SER C C 171.9 . 1 452 . 92 SER CA C 56.9 . 1 453 . 92 SER N N 119.0 . 1 454 . 93 PHE H H 8.92 . 1 455 . 93 PHE HA H 5.07 . 1 456 . 93 PHE C C 176.2 . 1 457 . 93 PHE CA C 57.8 . 1 458 . 93 PHE N N 122.6 . 1 459 . 94 GLY H H 8.29 . 1 460 . 94 GLY HA2 H 4.22 . 2 461 . 94 GLY HA3 H 4.77 . 2 462 . 94 GLY C C 176.7 . 1 463 . 94 GLY CA C 46.4 . 1 464 . 94 GLY N N 110.0 . 1 465 . 95 ASP H H 7.95 . 1 466 . 95 ASP HA H 5.44 . 1 467 . 95 ASP C C 175.4 . 1 468 . 95 ASP CA C 52.9 . 1 469 . 95 ASP N N 123.2 . 1 470 . 96 GLY H H 9.02 . 1 471 . 96 GLY HA2 H 3.70 . 2 472 . 96 GLY HA3 H 4.04 . 2 473 . 96 GLY C C 172.1 . 1 474 . 96 GLY CA C 46.0 . 1 475 . 96 GLY N N 111.95 . 1 476 . 97 LEU H H 8.57 . 1 477 . 97 LEU HA H 4.95 . 1 478 . 97 LEU C C 176.3 . 1 479 . 97 LEU CA C 54.1 . 1 480 . 97 LEU N N 126.7 . 1 481 . 98 SER H H 8.94 . 1 482 . 98 SER HA H 4.79 . 1 483 . 98 SER C C 173.5 . 1 484 . 98 SER CA C 56.5 . 1 485 . 98 SER N N 121.6 . 1 486 . 99 GLY H H 8.38 . 1 487 . 99 GLY HA2 H 3.50 . 2 488 . 99 GLY HA3 H 3.92 . 2 489 . 99 GLY C C 173.3 . 1 490 . 99 GLY CA C 44.8 . 1 491 . 99 GLY N N 110.7 . 1 492 . 100 GLY H H 6.93 . 1 493 . 100 GLY HA2 H 2.35 . 1 494 . 100 GLY HA3 H 3.18 . 1 495 . 100 GLY C C 173.9 . 1 496 . 100 GLY CA C 44.1 . 1 497 . 100 GLY N N 110.0 . 1 498 . 101 ASP H H 8.33 . 1 499 . 101 ASP HA H 4.75 . 1 500 . 101 ASP C C 175.7 . 1 501 . 101 ASP CA C 55.3 . 1 502 . 101 ASP N N 119.4 . 1 503 . 102 THR H H 8.32 . 1 504 . 102 THR HA H 4.38 . 1 505 . 102 THR C C 173.7 . 1 506 . 102 THR CA C 61.3 . 1 507 . 102 THR N N 111.5 . 1 508 . 103 SER H H 7.61 . 1 509 . 103 SER HA H 4.73 . 1 510 . 103 SER CA C 55.9 . 1 511 . 103 SER N N 119.7 . 1 512 . 104 PRO C C 176.9 . 1 513 . 104 PRO CA C 61.9 . 1 514 . 105 TYR H H 9.78 . 1 515 . 105 TYR HA H 4.91 . 1 516 . 105 TYR C C 177.8 . 1 517 . 105 TYR CA C 59.3 . 1 518 . 105 TYR N N 122.5 . 1 519 . 106 SER H H 8.73 . 1 520 . 106 SER HA H 4.33 . 1 521 . 106 SER C C 171.8 . 1 522 . 106 SER CA C 56.8 . 1 523 . 106 SER N N 116.1 . 1 524 . 107 ILE H H 8.10 . 1 525 . 107 ILE HA H 4.70 . 1 526 . 107 ILE C C 176.9 . 1 527 . 107 ILE CA C 57.6 . 1 528 . 107 ILE N N 123.5 . 1 529 . 108 GLN H H 8.82 . 1 530 . 108 GLN HA H 3.93 . 1 531 . 108 GLN C C 177.2 . 1 532 . 108 GLN CA C 59.8 . 1 533 . 108 GLN N N 130.3 . 1 534 . 109 VAL H H 8.42 . 1 535 . 109 VAL HA H 4.44 . 1 536 . 109 VAL CA C 59.2 . 1 537 . 109 VAL N N 120.7 . 1 538 . 110 PRO HA H 4.21 . 1 539 . 110 PRO C C 176.10 . 1 540 . 110 PRO CA C 63.3 . 1 541 . 111 ASP H H 8.89 . 1 542 . 111 ASP HA H 4.94 . 1 543 . 111 ASP CA C 55.6 . 1 544 . 111 ASP N N 125.0 . 1 545 . 112 VAL H H 6.71 . 1 546 . 112 VAL HA H 4.51 . 1 547 . 112 VAL C C 173.9 . 1 548 . 112 VAL CA C 59.6 . 1 549 . 112 VAL N N 114.6 . 1 550 . 113 SER H H 8.92 . 1 551 . 113 SER HA H 5.26 . 1 552 . 113 SER C C 172.2 . 1 553 . 113 SER CA C 56.9 . 1 554 . 113 SER N N 119.4 . 1 555 . 114 PHE H H 9.34 . 1 556 . 114 PHE HA H 5.33 . 1 557 . 114 PHE C C 175.2 . 1 558 . 114 PHE CA C 55.8 . 1 559 . 114 PHE N N 122.4 . 1 560 . 115 GLY H H 8.89 . 1 561 . 115 GLY HA2 H 3.52 . 2 562 . 115 GLY HA3 H 4.90 . 2 563 . 115 GLY C C 173.1 . 1 564 . 115 GLY CA C 43.5 . 1 565 . 115 GLY N N 112.9 . 1 566 . 116 GLY H H 7.90 . 1 567 . 116 GLY HA2 H 3.82 . 2 568 . 116 GLY HA3 H 4.01 . 2 569 . 116 GLY C C 177.0 . 1 570 . 116 GLY CA C 47.2 . 1 571 . 116 GLY N N 109.5 . 1 572 . 117 LEU H H 9.10 . 1 573 . 117 LEU HA H 3.91 . 1 574 . 117 LEU C C 175.3 . 1 575 . 117 LEU CA C 57.5 . 1 576 . 117 LEU N N 119.3 . 1 577 . 118 ASN H H 8.76 . 1 578 . 118 ASN HA H 4.28 . 1 579 . 118 ASN C C 173.4 . 1 580 . 118 ASN CA C 53.5 . 1 581 . 118 ASN N N 114.4 . 1 582 . 119 LEU H H 7.64 . 1 583 . 119 LEU HA H 4.78 . 1 584 . 119 LEU C C 178.5 . 1 585 . 119 LEU CA C 53.4 . 1 586 . 119 LEU N N 118.7 . 1 587 . 120 SER H H 8.62 . 1 588 . 120 SER HA H 5.60 . 1 589 . 120 SER C C 173.1 . 1 590 . 120 SER CA C 56.9 . 1 591 . 120 SER N N 118.3 . 1 592 . 121 SER H H 9.21 . 1 593 . 121 SER HA H 5.03 . 1 594 . 121 SER C C 173.8 . 1 595 . 121 SER CA C 57.3 . 1 596 . 121 SER N N 117.6 . 1 597 . 122 LEU H H 8.53 . 1 598 . 122 LEU HA H 4.69 . 1 599 . 122 LEU C C 178.6 . 1 600 . 122 LEU CA C 53.1 . 1 601 . 122 LEU N N 122.5 . 1 602 . 123 GLN H H 8.75 . 1 603 . 123 GLN HA H 4.67 . 1 604 . 123 GLN C C 177.4 . 1 605 . 123 GLN CA C 60.1 . 1 606 . 123 GLN N N 129.3 . 1 607 . 124 ALA H H 8.02 . 1 608 . 124 ALA HA H 3.85 . 1 609 . 124 ALA C C 178.8 . 1 610 . 124 ALA CA C 53.9 . 1 611 . 124 ALA N N 116.5 . 1 612 . 125 GLN H H 7.27 . 1 613 . 125 GLN HA H 4.17 . 1 614 . 125 GLN C C 177.70 . 1 615 . 125 GLN CA C 56.6 . 1 616 . 125 GLN N N 115.4 . 1 617 . 126 GLY H H 8.10 . 1 618 . 126 GLY HA2 H 3.65 . 2 619 . 126 GLY HA3 H 3.87 . 2 620 . 126 GLY CA C 46.4 . 1 621 . 126 GLY N N 107.1 . 1 622 . 127 HIS H H 9.31 . 1 623 . 127 HIS HA H 4.67 . 1 624 . 127 HIS C C 173.9 . 1 625 . 127 HIS CA C 54.6 . 1 626 . 127 HIS N N 123.8 . 1 627 . 128 ASP H H 7.63 . 1 628 . 128 ASP HA H 4.75 . 1 629 . 128 ASP CA C 45.7 . 1 630 . 128 ASP N N 116.9 . 1 631 . 129 GLY H H 7.60 . 1 632 . 129 GLY C C 174.5 . 1 633 . 129 GLY CA C 45.2 . 1 634 . 129 GLY N N 109.4 . 1 635 . 130 VAL H H 8.73 . 1 636 . 130 VAL HA H 4.70 . 1 637 . 130 VAL C C 175.8 . 1 638 . 130 VAL CA C 65.6 . 1 639 . 130 VAL N N 125.4 . 1 640 . 131 VAL H H 7.38 . 1 641 . 131 VAL HA H 3.18 . 1 642 . 131 VAL C C 176.1 . 1 643 . 131 VAL CA C 67.8 . 1 644 . 131 VAL N N 122.1 . 1 645 . 132 HIS H H 7.88 . 1 646 . 132 HIS HA H 3.93 . 1 647 . 132 HIS C C 176.4 . 1 648 . 132 HIS CA C 62.1 . 1 649 . 132 HIS N N 122.0 . 1 650 . 133 GLN H H 8.49 . 1 651 . 133 GLN HA H 4.14 . 1 652 . 133 GLN C C 180.5 . 1 653 . 133 GLN CA C 59.8 . 1 654 . 133 GLN N N 116.4 . 1 655 . 134 VAL H H 8.79 . 1 656 . 134 VAL HA H 3.42 . 1 657 . 134 VAL C C 177.9 . 1 658 . 134 VAL CA C 67.0 . 1 659 . 134 VAL N N 119.3 . 1 660 . 135 VAL H H 8.33 . 1 661 . 135 VAL HA H 3.27 . 1 662 . 135 VAL C C 176.9 . 1 663 . 135 VAL CA C 67.5 . 1 664 . 135 VAL N N 120.4 . 1 665 . 136 TYR H H 9.24 . 1 666 . 136 TYR HA H 4.17 . 1 667 . 136 TYR C C 180.1 . 1 668 . 136 TYR CA C 62.2 . 1 669 . 136 TYR N N 121.1 . 1 670 . 137 GLY H H 7.60 . 1 671 . 137 GLY HA2 H 3.90 . 2 672 . 137 GLY HA3 H 4.70 . 2 673 . 137 GLY C C 176.8 . 1 674 . 137 GLY CA C 48.0 . 1 675 . 137 GLY N N 109.4 . 1 676 . 138 LEU H H 7.74 . 1 677 . 138 LEU HA H 3.61 . 1 678 . 138 LEU C C 179.3 . 1 679 . 138 LEU CA C 58.6 . 1 680 . 138 LEU N N 125.5 . 1 681 . 139 MET H H 8.05 . 1 682 . 139 MET HA H 4.11 . 1 683 . 139 MET CA C 58.4 . 1 684 . 139 MET N N 116.9 . 1 685 . 140 SER H H 7.73 . 1 686 . 140 SER C C 180.9 . 1 687 . 140 SER CA C 59.4 . 1 688 . 140 SER N N 114.2 . 1 689 . 141 GLY H H 8.12 . 1 690 . 141 GLY HA2 H 3.26 . 1 691 . 141 GLY HA3 H 3.26 . 1 692 . 141 GLY C C 172.0 . 1 693 . 141 GLY CA C 46.1 . 1 694 . 141 GLY N N 119.1 . 1 695 . 142 ASP H H 8.48 . 1 696 . 142 ASP HA H 4.91 . 1 697 . 142 ASP C C 178.0 . 1 698 . 142 ASP CA C 52.7 . 1 699 . 142 ASP N N 122.3 . 1 700 . 143 THR H H 8.48 . 1 701 . 143 THR HA H 4.61 . 1 702 . 143 THR C C 176.8 . 1 703 . 143 THR CA C 61.8 . 1 704 . 143 THR N N 116.4 . 1 705 . 144 GLY H H 8.76 . 1 706 . 144 GLY HA2 H 3.22 . 2 707 . 144 GLY HA3 H 3.67 . 2 708 . 144 GLY C C 178.7 . 1 709 . 144 GLY CA C 48.5 . 1 710 . 144 GLY N N 114.4 . 1 711 . 145 ALA H H 8.89 . 1 712 . 145 ALA HA H 4.14 . 1 713 . 145 ALA C C 180.9 . 1 714 . 145 ALA CA C 55.1 . 1 715 . 145 ALA N N 126.6 . 1 716 . 146 LEU H H 7.99 . 1 717 . 146 LEU HA H 3.92 . 1 718 . 146 LEU C C 177.4 . 1 719 . 146 LEU CA C 57.5 . 1 720 . 146 LEU N N 121.1 . 1 721 . 147 GLU H H 8.79 . 1 722 . 147 GLU HA H 3.57 . 1 723 . 147 GLU C C 177.8 . 1 724 . 147 GLU CA C 61.9 . 1 725 . 147 GLU N N 120.8 . 1 726 . 148 THR H H 8.40 . 1 727 . 148 THR HA H 4.38 . 1 728 . 148 THR C C 177.0 . 1 729 . 148 THR CA C 62.0 . 1 730 . 148 THR N N 118.5 . 1 731 . 149 ALA H H 7.84 . 1 732 . 149 ALA HA H 4.11 . 1 733 . 149 ALA C C 181.3 . 1 734 . 149 ALA CA C 54.8 . 1 735 . 149 ALA N N 126.5 . 1 736 . 150 LEU H H 9.02 . 1 737 . 150 LEU HA H 3.71 . 1 738 . 150 LEU C C 178.8 . 1 739 . 150 LEU CA C 57.3 . 1 740 . 150 LEU N N 119.9 . 1 741 . 151 ASN H H 8.68 . 1 742 . 151 ASN HA H 4.52 . 1 743 . 151 ASN C C 178.8 . 1 744 . 151 ASN CA C 58.8 . 1 745 . 151 ASN N N 121.5 . 1 746 . 152 GLY H H 7.59 . 1 747 . 152 GLY HA2 H 3.91 . 2 748 . 152 GLY HA3 H 3.91 . 2 749 . 152 GLY CA C 46.9 . 1 750 . 152 GLY N N 108.6 . 1 751 . 153 ILE H H 7.20 . 1 752 . 153 ILE HA H 3.80 . 1 753 . 153 ILE C C 178.5 . 1 754 . 153 ILE CA C 53.4 . 1 755 . 153 ILE N N 123.8 . 1 756 . 154 LEU H H 8.62 . 1 757 . 154 LEU HA H 3.83 . 1 758 . 154 LEU C C 179.0 . 1 759 . 154 LEU CA C 55.5 . 1 760 . 154 LEU N N 118.3 . 1 761 . 155 ASP H H 7.91 . 1 762 . 155 ASP HA H 4.54 . 1 763 . 155 ASP C C 179.2 . 1 764 . 155 ASP CA C 56.6 . 1 765 . 155 ASP N N 123.5 . 1 766 . 156 ASP H H 7.44 . 1 767 . 156 ASP HA H 4.35 . 1 768 . 156 ASP C C 176.5 . 1 769 . 156 ASP CA C 56.7 . 1 770 . 156 ASP N N 119.3 . 1 771 . 157 TYR H H 7.79 . 1 772 . 157 TYR HA H 4.57 . 1 773 . 157 TYR C C 175.9 . 1 774 . 157 TYR CA C 56.9 . 1 775 . 157 TYR N N 117.0 . 1 776 . 158 GLY H H 8.03 . 1 777 . 158 GLY HA2 H 4.05 . 2 778 . 158 GLY HA3 H 4.54 . 2 779 . 158 GLY C C 174.3 . 1 780 . 158 GLY CA C 45.9 . 1 781 . 158 GLY N N 110.1 . 1 782 . 159 LEU H H 7.34 . 1 783 . 159 LEU HA H 4.76 . 1 784 . 159 LEU C C 174.5 . 1 785 . 159 LEU CA C 52.9 . 1 786 . 159 LEU N N 120.1 . 1 787 . 160 SER H H 8.51 . 1 788 . 160 SER HA H 4.63 . 1 789 . 160 SER C C 175.4 . 1 790 . 160 SER CA C 58.7 . 1 791 . 160 SER N N 115.1 . 1 792 . 161 VAL H H 9.31 . 1 793 . 161 VAL HA H 4.01 . 1 794 . 161 VAL C C 177.2 . 1 795 . 161 VAL CA C 64.1 . 1 796 . 161 VAL N N 112.6 . 1 797 . 162 ASN H H 8.43 . 1 798 . 162 ASN HA H 4.80 . 1 799 . 162 ASN C C 175.3 . 1 800 . 162 ASN CA C 54.2 . 1 801 . 162 ASN N N 119.7 . 1 802 . 163 SER H H 8.02 . 1 803 . 163 SER HA H 4.60 . 1 804 . 163 SER C C 172.1 . 1 805 . 163 SER CA C 58.9 . 1 806 . 163 SER N N 121.8 . 1 807 . 164 THR H H 8.44 . 1 808 . 164 THR HA H 5.01 . 1 809 . 164 THR CA C 59.9 . 1 810 . 164 THR N N 113.0 . 1 811 . 165 PHE H H 7.86 . 1 812 . 165 PHE HA H 4.80 . 1 813 . 165 PHE N N 120.1 . 1 814 . 166 ASP H H 8.99 . 1 815 . 166 ASP HA H 4.71 . 1 816 . 166 ASP C C 174.2 . 1 817 . 166 ASP CA C 57.254 . 1 818 . 166 ASP N N 118.61 . 1 819 . 167 GLN H H 7.97 . 1 820 . 167 GLN HA H 4.05 . 1 821 . 167 GLN C C 177.9 . 1 822 . 167 GLN CA C 59.0 . 1 823 . 167 GLN N N 122.2 . 1 824 . 168 VAL H H 8.70 . 1 825 . 168 VAL HA H 5.10 . 1 826 . 168 VAL C C 179.1 . 1 827 . 168 VAL CA C 65.9 . 1 828 . 168 VAL N N 123.5 . 1 829 . 169 ALA H H 9.32 . 1 830 . 169 ALA HA H 4.00 . 1 831 . 169 ALA C C 180.0 . 1 832 . 169 ALA CA C 55.3 . 1 833 . 169 ALA N N 126.9 . 1 834 . 170 ALA H H 7.69 . 1 835 . 170 ALA HA H 4.14 . 1 836 . 170 ALA C C 179.9 . 1 837 . 170 ALA CA C 54.7 . 1 838 . 170 ALA N N 120.2 . 1 839 . 171 ALA H H 7.61 . 1 840 . 171 ALA HA H 4.48 . 1 841 . 171 ALA C C 179.1 . 1 842 . 171 ALA CA C 54.1 . 1 843 . 171 ALA N N 120.0 . 1 844 . 172 THR H H 7.80 . 1 845 . 172 THR HA H 4.24 . 1 846 . 172 THR C C 175.4 . 1 847 . 172 THR CA C 62.1 . 1 848 . 172 THR N N 106.9 . 1 849 . 173 ALA H H 7.45 . 1 850 . 173 ALA HA H 4.39 . 1 851 . 173 ALA C C 178.1 . 1 852 . 173 ALA CA C 53.3 . 1 853 . 173 ALA N N 126.9 . 1 854 . 174 VAL H H 7.83 . 1 855 . 174 VAL HA H 4.13 . 1 856 . 174 VAL C C 177.0 . 1 857 . 174 VAL CA C 63.0 . 1 858 . 174 VAL N N 119.6 . 1 859 . 175 GLY H H 8.35 . 1 860 . 175 GLY HA2 H 4.05 . 2 861 . 175 GLY HA3 H 4.71 . 2 862 . 175 GLY C C 176.5 . 1 863 . 175 GLY CA C 45.2 . 1 864 . 175 GLY N N 112.9 . 1 865 . 176 VAL H H 7.95 . 1 866 . 176 VAL HA H 4.05 . 1 867 . 176 VAL C C 176.0 . 1 868 . 176 VAL CA C 62.3 . 1 869 . 176 VAL N N 120.6 . 1 870 . 177 GLN H H 8.40 . 1 871 . 177 GLN HA H 4.32 . 1 872 . 177 GLN C C 174.9 . 1 873 . 177 GLN CA C 55.6 . 1 874 . 177 GLN N N 126.9 . 1 875 . 178 HIS H H 8.13 . 1 876 . 178 HIS HA H 4.29 . 1 877 . 178 HIS CA C 56.7 . 1 878 . 178 HIS N N 127.2 . 1 stop_ save_