data_17404 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Backbone (H,N,CA,HA,CB,HB) assignment of the Escherichia coli peptidyl-tRNA hydrolase ; _BMRB_accession_number 17404 _BMRB_flat_file_name bmr17404.str _Entry_type original _Submission_date 2011-01-11 _Accession_date 2011-01-11 _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 Giorgi Laurent . . 2 Plateau Pierre . . 3 Aubard Caroline . . 4 Fromant Michel . . 5 Blanquet Sylvain . . 6 Bontems Francois . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 635 "13C chemical shifts" 541 "15N chemical shifts" 183 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2012-12-07 update BMRB 'delete outliers: 32 PRO N 1, 58 PRO N 1, 106 PRO N 1, 57 ALA C 1, 105 ASN C 1, 132 GLY C 1, 147 ASN C 1' 2012-03-09 update BMRB 'update entry citation' 2011-07-07 original author 'original release' stop_ save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title 'NMR-based substrate analog docking to Escherichia coli peptidyl-tRNA hydrolase.' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 21718701 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Giorgi Laurent . . 2 Plateau Pierre . . 3 Aubard Gavin . . 4 Fromant Caroline . . 5 Thureau Michel . . 6 Grtli Aurelien . . 7 Blanquet Morten . . 8 Bontems Sylvain . . stop_ _Journal_abbreviation 'J. Mol. Biol.' _Journal_name_full 'Journal of molecular biology' _Journal_volume 412 _Journal_issue 4 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 619 _Page_last 633 _Year 2011 _Details . loop_ _Keyword 'E. coli peptidyl-tRNA hydrolase' Haddock 'solution NMR' 'substrate analog' stop_ save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name 'PTH-HA20 solution' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'PTH-HA20 solution' $PTH-HA20 stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state ? _System_paramagnetic no _System_thiol_state . loop_ _Biological_function 'hydrolyse peptidyl-tRNA prematurely dissociated from the ribosome' stop_ _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_PTH-HA20 _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common PTH-HA20 _Molecular_mass . _Mol_thiol_state 'all free' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 214 _Mol_residue_sequence ; MGSSHHHHHHSSGLVPRGSH MTIKLIVGLANPGAEYAATR ANAGAWFVDLLAERLRAPLR EEAKFFGYTSRVTLGGEDVR LLVPTTFMNLSGKAVAAMAS FFRINPDEILVAHDELDLPP GVAKFKLGGGHGGHNGLKDI ISKLGNNPNFHRLRIGIGHP GDKNKVVGFVLGKPPVSEQK LIDEAIDEAARCTEMWFTDG LTKATNRLHAFKAQ ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 -20 MET 2 -19 GLY 3 -18 SER 4 -17 SER 5 -16 HIS 6 -15 HIS 7 -14 HIS 8 -13 HIS 9 -12 HIS 10 -11 HIS 11 -10 SER 12 -9 SER 13 -8 GLY 14 -7 LEU 15 -6 VAL 16 -5 PRO 17 -4 ARG 18 -3 GLY 19 -2 SER 20 -1 HIS 21 0 MET 22 1 THR 23 2 ILE 24 3 LYS 25 4 LEU 26 5 ILE 27 6 VAL 28 7 GLY 29 8 LEU 30 9 ALA 31 10 ASN 32 11 PRO 33 12 GLY 34 13 ALA 35 14 GLU 36 15 TYR 37 16 ALA 38 17 ALA 39 18 THR 40 19 ARG 41 20 ALA 42 21 ASN 43 22 ALA 44 23 GLY 45 24 ALA 46 25 TRP 47 26 PHE 48 27 VAL 49 28 ASP 50 29 LEU 51 30 LEU 52 31 ALA 53 32 GLU 54 33 ARG 55 34 LEU 56 35 ARG 57 36 ALA 58 37 PRO 59 38 LEU 60 39 ARG 61 40 GLU 62 41 GLU 63 42 ALA 64 43 LYS 65 44 PHE 66 45 PHE 67 46 GLY 68 47 TYR 69 48 THR 70 49 SER 71 50 ARG 72 51 VAL 73 52 THR 74 53 LEU 75 54 GLY 76 55 GLY 77 56 GLU 78 57 ASP 79 58 VAL 80 59 ARG 81 60 LEU 82 61 LEU 83 62 VAL 84 63 PRO 85 64 THR 86 65 THR 87 66 PHE 88 67 MET 89 68 ASN 90 69 LEU 91 70 SER 92 71 GLY 93 72 LYS 94 73 ALA 95 74 VAL 96 75 ALA 97 76 ALA 98 77 MET 99 78 ALA 100 79 SER 101 80 PHE 102 81 PHE 103 82 ARG 104 83 ILE 105 84 ASN 106 85 PRO 107 86 ASP 108 87 GLU 109 88 ILE 110 89 LEU 111 90 VAL 112 91 ALA 113 92 HIS 114 93 ASP 115 94 GLU 116 95 LEU 117 96 ASP 118 97 LEU 119 98 PRO 120 99 PRO 121 100 GLY 122 101 VAL 123 102 ALA 124 103 LYS 125 104 PHE 126 105 LYS 127 106 LEU 128 107 GLY 129 108 GLY 130 109 GLY 131 110 HIS 132 111 GLY 133 112 GLY 134 113 HIS 135 114 ASN 136 115 GLY 137 116 LEU 138 117 LYS 139 118 ASP 140 119 ILE 141 120 ILE 142 121 SER 143 122 LYS 144 123 LEU 145 124 GLY 146 125 ASN 147 126 ASN 148 127 PRO 149 128 ASN 150 129 PHE 151 130 HIS 152 131 ARG 153 132 LEU 154 133 ARG 155 134 ILE 156 135 GLY 157 136 ILE 158 137 GLY 159 138 HIS 160 139 PRO 161 140 GLY 162 141 ASP 163 142 LYS 164 143 ASN 165 144 LYS 166 145 VAL 167 146 VAL 168 147 GLY 169 148 PHE 170 149 VAL 171 150 LEU 172 151 GLY 173 152 LYS 174 153 PRO 175 154 PRO 176 155 VAL 177 156 SER 178 157 GLU 179 158 GLN 180 159 LYS 181 160 LEU 182 161 ILE 183 162 ASP 184 163 GLU 185 164 ALA 186 165 ILE 187 166 ASP 188 167 GLU 189 168 ALA 190 169 ALA 191 170 ARG 192 171 CYS 193 172 THR 194 173 GLU 195 174 MET 196 175 TRP 197 176 PHE 198 177 THR 199 178 ASP 200 179 GLY 201 180 LEU 202 181 THR 203 182 LYS 204 183 ALA 205 184 THR 206 185 ASN 207 186 ARG 208 187 LEU 209 188 HIS 210 189 ALA 211 190 PHE 212 191 LYS 213 192 ALA 214 193 GLN stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-09-09 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 2PTH "Peptidyl-Trna Hydrolase From Escherichia Coli" 90.19 193 99.48 99.48 4.69e-135 PDB 3OFV "Crystal Structure Of Peptidyl-Trna Hydrolase From Escherichia Coli, I222 Crystal Form" 98.60 211 99.05 99.53 5.78e-149 PDB 3VJR "Crystal Structure Of Peptidyl-trna Hydrolase From Escherichia Coli In Complex With The Cca-acceptor-t[psi]c Domain Of Trna" 92.06 197 99.49 99.49 2.08e-138 DBJ BAA36062 "peptidyl-tRNA hydrolase [Escherichia coli str. K12 substr. W3110]" 90.65 194 99.48 99.48 4.53e-136 DBJ BAB35132 "peptidyl-tRNA hydrolase [Escherichia coli O157:H7 str. Sakai]" 90.65 194 99.48 99.48 4.53e-136 DBJ BAG76778 "peptidyl-tRNA hydrolase [Escherichia coli SE11]" 90.65 194 99.48 99.48 4.53e-136 DBJ BAI25016 "peptidyl-tRNA hydrolase [Escherichia coli O26:H11 str. 11368]" 90.65 194 99.48 99.48 4.53e-136 DBJ BAI30140 "peptidyl-tRNA hydrolase [Escherichia coli O103:H2 str. 12009]" 90.65 194 99.48 99.48 4.53e-136 EMBL CAA43945 "peptidyl-tRNA hydrolase [Escherichia coli K-12]" 90.65 194 99.48 99.48 4.53e-136 EMBL CAP75743 "Peptidyl-tRNA hydrolase [Escherichia coli LF82]" 90.65 194 99.48 99.48 4.53e-136 EMBL CAQ31706 "peptidyl-tRNA hydrolase [Escherichia coli BL21(DE3)]" 90.65 194 99.48 99.48 4.53e-136 EMBL CAQ98084 "peptidyl-tRNA hydrolase [Escherichia coli IAI1]" 90.65 194 99.48 99.48 4.53e-136 EMBL CAR02598 "peptidyl-tRNA hydrolase [Escherichia coli S88]" 90.65 194 99.48 99.48 4.53e-136 GB AAC74288 "peptidyl-tRNA hydrolase [Escherichia coli str. K-12 substr. MG1655]" 90.65 194 99.48 99.48 4.53e-136 GB AAG56062 "peptidyl-tRNA hydrolase [Escherichia coli O157:H7 str. EDL933]" 90.65 194 99.48 99.48 4.53e-136 GB AAN42820 "peptidyl-tRNA hydrolase [Shigella flexneri 2a str. 301]" 90.65 194 98.97 98.97 2.36e-135 GB AAN80127 "Peptidyl-tRNA hydrolase [Escherichia coli CFT073]" 90.65 194 99.48 99.48 4.53e-136 GB AAP16706 "peptidyl-tRNA hydrolase [Shigella flexneri 2a str. 2457T]" 90.65 194 98.97 98.97 2.36e-135 PRF 2104267B "peptidyl-tRNA hydrolase" 90.65 194 98.97 99.48 2.49e-135 REF NP_309736 "peptidyl-tRNA hydrolase [Escherichia coli O157:H7 str. Sakai]" 90.65 194 99.48 99.48 4.53e-136 REF NP_415722 "peptidyl-tRNA hydrolase [Escherichia coli str. K-12 substr. MG1655]" 90.65 194 99.48 99.48 4.53e-136 REF NP_707113 "peptidyl-tRNA hydrolase [Shigella flexneri 2a str. 301]" 90.65 194 98.97 98.97 2.36e-135 REF WP_000152925 "peptidyl-tRNA hydrolase [Escherichia coli]" 90.65 194 98.97 99.48 7.49e-136 REF WP_000152927 "peptidyl-tRNA hydrolase [Escherichia coli]" 90.65 194 98.97 98.97 1.15e-134 SP A7ZKX7 "RecName: Full=Peptidyl-tRNA hydrolase; Short=PTH" 90.65 194 99.48 99.48 4.53e-136 SP A7ZZE0 "RecName: Full=Peptidyl-tRNA hydrolase; Short=PTH" 90.65 194 99.48 99.48 4.53e-136 SP B1IU89 "RecName: Full=Peptidyl-tRNA hydrolase; Short=PTH" 90.65 194 99.48 99.48 4.53e-136 SP B1LH96 "RecName: Full=Peptidyl-tRNA hydrolase; Short=PTH" 90.65 194 99.48 99.48 4.53e-136 SP B1XAP5 "RecName: Full=Peptidyl-tRNA hydrolase; Short=PTH" 90.65 194 99.48 99.48 4.53e-136 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $PTH-HA20 'E. coli' 562 Bacteria . Escherichia coli 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 $PTH-HA20 'recombinant technology' . Escherichia coli . pET15b 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 $PTH-HA20 0.5-0.7 mM '[U-98% 13C; U-98% 15N]' 'sodium acetate' 50 mM 'natural abundance' 'sodium chloride' 200 mM 'natural abundance' stop_ save_ save_sample_2 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $PTH-HA20 0.5-0.7 mM '[U-98% 13C; U-98% 15N]' 'sodium acetate' 50 mM 'natural abundance' 'sodium chloride' 200 mM 'natural abundance' stop_ save_ ############################ # Computer software used # ############################ save_SPARKY _Saveframe_category software _Name SPARKY _Version . loop_ _Vendor _Address _Electronic_address Goddard . . stop_ loop_ _Task 'chemical shift assignment' 'peak picking' stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model Avance _Field_strength 600 _Details . save_ save_spectrometer_2 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model Avance _Field_strength 950 _Details . save_ ############################# # NMR applied experiments # ############################# save_2D_1H-15N_HSQC_1 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-15N HSQC' _Sample_label $sample_1 save_ save_3D_HNCO_2 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCO' _Sample_label $sample_1 save_ save_3D_HNCA_3 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCA' _Sample_label $sample_1 save_ save_3D_HNCACB_4 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCACB' _Sample_label $sample_1 save_ save_3D_HN(CO)CA_5 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HN(CO)CA' _Sample_label $sample_1 save_ save_3D_CBCA(CO)NH_6 _Saveframe_category NMR_applied_experiment _Experiment_name '3D CBCA(CO)NH' _Sample_label $sample_1 save_ save_3D_HBHA(CO)NH_7 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HBHA(CO)NH' _Sample_label $sample_1 save_ save_3D_1H-15N_NOESY_8 _Saveframe_category NMR_applied_experiment _Experiment_name '3D 1H-15N NOESY' _Sample_label $sample_1 save_ save_3D_HCCH-TOCSY_9 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HCCH-TOCSY' _Sample_label $sample_2 save_ ####################### # Sample conditions # ####################### save_sample_conditions_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units 'ionic strength' 250 . mM pH 6.0 . pH pressure 1 . atm temperature 290 . K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference_1 _Saveframe_category chemical_shift_reference _Details . loop_ _Mol_common_name _Atom_type _Atom_isotope_number _Atom_group _Chem_shift_units _Chem_shift_value _Reference_method _Reference_type _External_reference_sample_geometry _External_reference_location _External_reference_axis _Indirect_shift_ratio _Indirect_shift_ratio_citation_label _Correction_value_citation_label 'spectrometer frequency' C 13 no ppm 2.5 internal direct . . . 1.0 $entry_citation $entry_citation 'spectrometer frequency' H 1 no ppm 0 internal direct . . . 1.0 $entry_citation $entry_citation 'spectrometer frequency' N 15 no ppm 0 internal direct . . . 1.0 $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_assigned_chem_shift_list_1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Experiment_label '3D HNCO' '3D HNCA' '3D CBCA(CO)NH' '3D HCCH-TOCSY' stop_ loop_ _Sample_label $sample_1 $sample_2 stop_ _Sample_conditions_label $sample_conditions_1 _Chem_shift_reference_set_label $chemical_shift_reference_1 _Mol_system_component_name 'PTH-HA20 solution' _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 22 THR H H 8.10 . 1 2 1 22 THR HA H 4.13 . 1 3 1 22 THR HB H 3.79 . 1 4 1 22 THR C C 176.89 . 1 5 1 22 THR CA C 60.38 . 1 6 1 22 THR CB C 70.22 . 1 7 1 22 THR N N 116.44 . 1 8 2 23 ILE H H 6.88 . 1 9 2 23 ILE HA H 3.81 . 1 10 2 23 ILE HB H 1.25 . 1 11 2 23 ILE C C 179.15 . 1 12 2 23 ILE CA C 57.70 . 1 13 2 23 ILE CB C 36.75 . 1 14 2 23 ILE N N 120.89 . 1 15 3 24 LYS H H 9.34 . 1 16 3 24 LYS HA H 4.53 . 1 17 3 24 LYS HB2 H 1.40 . 2 18 3 24 LYS HB3 H 1.90 . 2 19 3 24 LYS C C 180.04 . 1 20 3 24 LYS CA C 55.98 . 1 21 3 24 LYS CB C 36.70 . 1 22 3 24 LYS N N 121.40 . 1 23 4 25 LEU H H 7.63 . 1 24 4 25 LEU HA H 5.20 . 1 25 4 25 LEU HB2 H 1.18 . 2 26 4 25 LEU HB3 H 1.67 . 2 27 4 25 LEU C C 176.43 . 1 28 4 25 LEU CA C 53.31 . 1 29 4 25 LEU CB C 45.71 . 1 30 4 25 LEU N N 124.49 . 1 31 5 26 ILE H H 9.01 . 1 32 5 26 ILE HA H 5.05 . 1 33 5 26 ILE HB H 1.64 . 1 34 5 26 ILE C C 177.24 . 1 35 5 26 ILE CA C 60.13 . 1 36 5 26 ILE CB C 38.84 . 1 37 5 26 ILE N N 127.42 . 1 38 6 27 VAL H H 9.49 . 1 39 6 27 VAL HA H 5.40 . 1 40 6 27 VAL HB H 2.00 . 1 41 6 27 VAL C C 178.41 . 1 42 6 27 VAL CA C 58.67 . 1 43 6 27 VAL CB C 34.83 . 1 44 6 27 VAL N N 127.15 . 1 45 7 28 GLY H H 9.13 . 1 46 7 28 GLY HA2 H 4.84 . 2 47 7 28 GLY HA3 H 3.10 . 2 48 7 28 GLY C C 175.17 . 1 49 7 28 GLY CA C 44.79 . 1 50 7 28 GLY N N 116.44 . 1 51 8 29 LEU H H 7.26 . 1 52 8 29 LEU C C 179.93 . 1 53 8 29 LEU CA C 55.04 . 1 54 8 29 LEU CB C 40.60 . 1 55 8 29 LEU N N 118.59 . 1 56 9 30 ALA H H 8.38 . 1 57 9 30 ALA HA H 4.59 . 1 58 9 30 ALA HB H 1.18 . 1 59 9 30 ALA C C 180.80 . 1 60 9 30 ALA CA C 51.77 . 1 61 9 30 ALA CB C 24.13 . 1 62 9 30 ALA N N 121.13 . 1 63 10 31 ASN H H 8.31 . 1 64 10 31 ASN HA H 4.83 . 1 65 10 31 ASN HB2 H 1.67 . 2 66 10 31 ASN HB3 H 2.20 . 2 67 10 31 ASN CA C 50.71 . 1 68 10 31 ASN CB C 39.78 . 1 69 10 31 ASN N N 115.69 . 1 70 11 32 PRO HA H 4.41 . 1 71 11 32 PRO HB2 H 1.71 . 2 72 11 32 PRO HB3 H 1.71 . 2 73 11 32 PRO C C 180.72 . 1 74 11 32 PRO CA C 62.92 . 1 75 11 32 PRO CB C 32.29 . 1 76 12 33 GLY H H 8.13 . 1 77 12 33 GLY HA2 H 3.72 . 2 78 12 33 GLY HA3 H 4.53 . 2 79 12 33 GLY C C 180.27 . 1 80 12 33 GLY CA C 44.07 . 1 81 12 33 GLY N N 106.89 . 1 82 13 34 ALA H H 8.80 . 1 83 13 34 ALA HA H 4.02 . 1 84 13 34 ALA HB H 1.36 . 1 85 13 34 ALA C C 184.11 . 1 86 13 34 ALA CA C 55.07 . 1 87 13 34 ALA CB C 18.16 . 1 88 13 34 ALA N N 127.55 . 1 89 14 35 GLU H H 9.53 . 1 90 14 35 GLU HA H 3.95 . 1 91 14 35 GLU HB2 H 1.60 . 2 92 14 35 GLU HB3 H 1.53 . 2 93 14 35 GLU C C 181.23 . 1 94 14 35 GLU CA C 58.07 . 1 95 14 35 GLU CB C 28.05 . 1 96 14 35 GLU N N 116.55 . 1 97 15 36 TYR H H 7.22 . 1 98 15 36 TYR HA H 4.70 . 1 99 15 36 TYR HB2 H 2.33 . 2 100 15 36 TYR HB3 H 3.42 . 2 101 15 36 TYR C C 181.33 . 1 102 15 36 TYR CA C 57.33 . 1 103 15 36 TYR CB C 38.60 . 1 104 15 36 TYR N N 116.21 . 1 105 16 37 ALA H H 7.28 . 1 106 16 37 ALA HA H 4.27 . 1 107 16 37 ALA HB H 1.45 . 1 108 16 37 ALA C C 181.53 . 1 109 16 37 ALA CA C 55.33 . 1 110 16 37 ALA CB C 18.71 . 1 111 16 37 ALA N N 124.56 . 1 112 17 38 ALA H H 8.60 . 1 113 17 38 ALA HA H 4.77 . 1 114 17 38 ALA HB H 1.35 . 1 115 17 38 ALA C C 181.62 . 1 116 17 38 ALA CA C 51.22 . 1 117 17 38 ALA CB C 18.85 . 1 118 17 38 ALA N N 117.58 . 1 119 18 39 THR H H 7.80 . 1 120 18 39 THR HA H 4.53 . 1 121 18 39 THR HB H 4.32 . 1 122 18 39 THR C C 177.99 . 1 123 18 39 THR CA C 60.98 . 1 124 18 39 THR CB C 71.66 . 1 125 18 39 THR N N 109.78 . 1 126 19 40 ARG H H 7.86 . 1 127 19 40 ARG HA H 3.60 . 1 128 19 40 ARG C C 180.18 . 1 129 19 40 ARG CA C 60.58 . 1 130 19 40 ARG CB C 31.00 . 1 131 19 40 ARG N N 117.03 . 1 132 20 41 ALA H H 7.98 . 1 133 20 41 ALA HA H 3.98 . 1 134 20 41 ALA HB H 1.25 . 1 135 20 41 ALA C C 178.54 . 1 136 20 41 ALA CA C 52.69 . 1 137 20 41 ALA CB C 17.63 . 1 138 20 41 ALA N N 116.35 . 1 139 21 42 ASN H H 7.48 . 1 140 21 42 ASN HA H 4.82 . 1 141 21 42 ASN HB2 H 2.64 . 2 142 21 42 ASN HB3 H 2.90 . 2 143 21 42 ASN C C 178.90 . 1 144 21 42 ASN CA C 51.84 . 1 145 21 42 ASN CB C 36.94 . 1 146 21 42 ASN N N 114.55 . 1 147 22 43 ALA H H 7.14 . 1 148 22 43 ALA HA H 2.96 . 1 149 22 43 ALA HB H 0.96 . 1 150 22 43 ALA C C 182.33 . 1 151 22 43 ALA CA C 54.96 . 1 152 22 43 ALA CB C 16.97 . 1 153 22 43 ALA N N 121.01 . 1 154 23 44 GLY H H 9.06 . 1 155 23 44 GLY HA2 H 3.82 . 2 156 23 44 GLY HA3 H 3.44 . 2 157 23 44 GLY C C 180.06 . 1 158 23 44 GLY CA C 47.02 . 1 159 23 44 GLY N N 102.18 . 1 160 24 45 ALA H H 7.19 . 1 161 24 45 ALA HA H 3.90 . 1 162 24 45 ALA HB H 1.38 . 1 163 24 45 ALA C C 183.33 . 1 164 24 45 ALA CA C 55.13 . 1 165 24 45 ALA CB C 18.44 . 1 166 24 45 ALA N N 126.13 . 1 167 25 46 TRP H H 8.43 . 1 168 25 46 TRP HA H 4.60 . 1 169 25 46 TRP HB2 H 3.13 . 2 170 25 46 TRP HB3 H 3.80 . 2 171 25 46 TRP C C 184.30 . 1 172 25 46 TRP CA C 57.74 . 1 173 25 46 TRP CB C 28.33 . 1 174 25 46 TRP N N 119.81 . 1 175 26 47 PHE H H 7.76 . 1 176 26 47 PHE HA H 4.25 . 1 177 26 47 PHE HB2 H 3.50 . 2 178 26 47 PHE HB3 H 3.50 . 2 179 26 47 PHE C C 178.93 . 1 180 26 47 PHE CA C 60.65 . 1 181 26 47 PHE CB C 38.03 . 1 182 26 47 PHE N N 119.39 . 1 183 27 48 VAL H H 7.85 . 1 184 27 48 VAL HA H 2.99 . 1 185 27 48 VAL HB H 1.79 . 1 186 27 48 VAL C C 180.78 . 1 187 27 48 VAL CA C 67.57 . 1 188 27 48 VAL CB C 31.03 . 1 189 27 48 VAL N N 120.69 . 1 190 28 49 ASP H H 9.13 . 1 191 28 49 ASP HA H 4.14 . 1 192 28 49 ASP HB2 H 2.58 . 2 193 28 49 ASP HB3 H 2.77 . 2 194 28 49 ASP C C 181.94 . 1 195 28 49 ASP CA C 56.74 . 1 196 28 49 ASP CB C 39.83 . 1 197 28 49 ASP N N 119.10 . 1 198 29 50 LEU H H 7.49 . 1 199 29 50 LEU HA H 4.05 . 1 200 29 50 LEU HB2 H 1.50 . 2 201 29 50 LEU HB3 H 1.50 . 2 202 29 50 LEU C C 182.92 . 1 203 29 50 LEU CA C 57.67 . 1 204 29 50 LEU CB C 41.07 . 1 205 29 50 LEU N N 120.82 . 1 206 30 51 LEU H H 7.63 . 1 207 30 51 LEU HA H 3.55 . 1 208 30 51 LEU HB2 H 1.40 . 2 209 30 51 LEU HB3 H 1.02 . 2 210 30 51 LEU C C 181.76 . 1 211 30 51 LEU CA C 57.92 . 1 212 30 51 LEU CB C 41.73 . 1 213 30 51 LEU N N 119.48 . 1 214 31 52 ALA H H 8.39 . 1 215 31 52 ALA HA H 3.41 . 1 216 31 52 ALA HB H 1.29 . 1 217 31 52 ALA C C 183.66 . 1 218 31 52 ALA CA C 55.20 . 1 219 31 52 ALA CB C 17.74 . 1 220 31 52 ALA N N 119.87 . 1 221 32 53 GLU H H 7.86 . 1 222 32 53 GLU HA H 3.86 . 1 223 32 53 GLU HB2 H 2.04 . 2 224 32 53 GLU HB3 H 2.04 . 2 225 32 53 GLU C C 184.71 . 1 226 32 53 GLU CA C 58.57 . 1 227 32 53 GLU CB C 29.13 . 1 228 32 53 GLU N N 116.97 . 1 229 33 54 ARG H H 8.74 . 1 230 33 54 ARG HA H 3.85 . 1 231 33 54 ARG HB2 H 1.75 . 2 232 33 54 ARG HB3 H 1.75 . 2 233 33 54 ARG C C 182.31 . 1 234 33 54 ARG CA C 59.16 . 1 235 33 54 ARG CB C 29.91 . 1 236 33 54 ARG N N 121.47 . 1 237 34 55 LEU H H 7.99 . 1 238 34 55 LEU HA H 4.21 . 1 239 34 55 LEU HB2 H 1.59 . 2 240 34 55 LEU HB3 H 1.52 . 2 241 34 55 LEU C C 179.10 . 1 242 34 55 LEU CA C 53.66 . 1 243 34 55 LEU CB C 39.67 . 1 244 34 55 LEU N N 116.48 . 1 245 35 56 ARG H H 7.46 . 1 246 35 56 ARG HA H 3.71 . 1 247 35 56 ARG HB2 H 1.78 . 2 248 35 56 ARG HB3 H 1.97 . 2 249 35 56 ARG C C 178.51 . 1 250 35 56 ARG CA C 56.02 . 1 251 35 56 ARG CB C 26.01 . 1 252 35 56 ARG N N 115.72 . 1 253 36 57 ALA H H 8.39 . 1 254 36 57 ALA HA H 4.73 . 1 255 36 57 ALA HB H 0.96 . 1 256 36 57 ALA CA C 48.77 . 1 257 36 57 ALA CB C 19.85 . 1 258 36 57 ALA N N 122.94 . 1 259 37 58 PRO HA H 3.98 . 1 260 37 58 PRO HB2 H 2.14 . 2 261 37 58 PRO HB3 H 2.14 . 2 262 37 58 PRO C C 180.57 . 1 263 37 58 PRO CA C 62.47 . 1 264 37 58 PRO CB C 31.78 . 1 265 38 59 LEU H H 8.27 . 1 266 38 59 LEU HA H 4.09 . 1 267 38 59 LEU HB2 H 1.18 . 2 268 38 59 LEU HB3 H 1.59 . 2 269 38 59 LEU C C 179.94 . 1 270 38 59 LEU CA C 54.92 . 1 271 38 59 LEU CB C 42.72 . 1 272 38 59 LEU N N 121.78 . 1 273 39 60 ARG H H 8.72 . 1 274 39 60 ARG HA H 4.67 . 1 275 39 60 ARG HB2 H 1.77 . 2 276 39 60 ARG HB3 H 1.77 . 2 277 39 60 ARG C C 179.15 . 1 278 39 60 ARG CA C 54.14 . 1 279 39 60 ARG CB C 33.50 . 1 280 39 60 ARG N N 121.04 . 1 281 40 61 GLU H H 8.83 . 1 282 40 61 GLU HA H 3.50 . 1 283 40 61 GLU HB2 H 1.38 . 2 284 40 61 GLU HB3 H 1.68 . 2 285 40 61 GLU C C 179.79 . 1 286 40 61 GLU CA C 57.99 . 1 287 40 61 GLU CB C 29.27 . 1 288 40 61 GLU N N 125.73 . 1 289 41 62 GLU H H 8.76 . 1 290 41 62 GLU HA H 4.40 . 1 291 41 62 GLU HB2 H 1.75 . 2 292 41 62 GLU HB3 H 1.92 . 2 293 41 62 GLU C C 179.10 . 1 294 41 62 GLU CA C 55.02 . 1 295 41 62 GLU CB C 30.81 . 1 296 41 62 GLU N N 128.99 . 1 297 42 63 ALA H H 8.55 . 1 298 42 63 ALA HA H 3.79 . 1 299 42 63 ALA HB H 1.14 . 1 300 42 63 ALA C C 184.62 . 1 301 42 63 ALA CA C 54.97 . 1 302 42 63 ALA CB C 17.80 . 1 303 42 63 ALA N N 129.34 . 1 304 43 64 LYS H H 8.23 . 1 305 43 64 LYS HA H 3.42 . 1 306 43 64 LYS HB2 H 0.86 . 2 307 43 64 LYS HB3 H 1.16 . 2 308 43 64 LYS C C 178.55 . 1 309 43 64 LYS CA C 57.30 . 1 310 43 64 LYS CB C 30.99 . 1 311 43 64 LYS N N 115.86 . 1 312 44 65 PHE H H 7.06 . 1 313 44 65 PHE HA H 4.73 . 1 314 44 65 PHE HB2 H 2.30 . 2 315 44 65 PHE HB3 H 3.54 . 2 316 44 65 PHE C C 176.77 . 1 317 44 65 PHE CA C 54.01 . 1 318 44 65 PHE CB C 39.38 . 1 319 44 65 PHE N N 114.86 . 1 320 45 66 PHE H H 6.94 . 1 321 45 66 PHE HA H 3.75 . 1 322 45 66 PHE HB2 H 3.02 . 2 323 45 66 PHE HB3 H 3.02 . 2 324 45 66 PHE C C 179.33 . 1 325 45 66 PHE CA C 57.57 . 1 326 45 66 PHE CB C 35.64 . 1 327 45 66 PHE N N 110.07 . 1 328 46 67 GLY H H 6.76 . 1 329 46 67 GLY HA2 H 3.88 . 2 330 46 67 GLY HA3 H 4.60 . 2 331 46 67 GLY C C 175.10 . 1 332 46 67 GLY CA C 46.86 . 1 333 46 67 GLY N N 98.59 . 1 334 47 68 TYR H H 9.07 . 1 335 47 68 TYR HA H 4.75 . 1 336 47 68 TYR HB2 H 2.60 . 2 337 47 68 TYR HB3 H 2.83 . 2 338 47 68 TYR C C 179.60 . 1 339 47 68 TYR CA C 56.09 . 1 340 47 68 TYR CB C 40.23 . 1 341 47 68 TYR N N 120.00 . 1 342 48 69 THR H H 9.27 . 1 343 48 69 THR HA H 5.65 . 1 344 48 69 THR HB H 4.20 . 1 345 48 69 THR C C 178.35 . 1 346 48 69 THR CA C 58.51 . 1 347 48 69 THR CB C 72.42 . 1 348 48 69 THR N N 112.58 . 1 349 49 70 SER H H 7.95 . 1 350 49 70 SER HA H 4.45 . 1 351 49 70 SER HB2 H 3.51 . 2 352 49 70 SER HB3 H 3.71 . 2 353 49 70 SER C C 177.58 . 1 354 49 70 SER CA C 56.87 . 1 355 49 70 SER CB C 64.68 . 1 356 49 70 SER N N 113.76 . 1 357 50 71 ARG H H 8.20 . 1 358 50 71 ARG HA H 4.93 . 1 359 50 71 ARG HB2 H 1.45 . 2 360 50 71 ARG HB3 H 1.62 . 2 361 50 71 ARG C C 177.87 . 1 362 50 71 ARG CA C 55.15 . 1 363 50 71 ARG CB C 32.60 . 1 364 50 71 ARG N N 123.79 . 1 365 51 72 VAL H H 9.02 . 1 366 51 72 VAL HA H 4.55 . 1 367 51 72 VAL HB H 1.88 . 1 368 51 72 VAL C C 177.51 . 1 369 51 72 VAL CA C 58.35 . 1 370 51 72 VAL CB C 35.28 . 1 371 51 72 VAL N N 119.30 . 1 372 52 73 THR H H 8.00 . 1 373 52 73 THR HA H 5.02 . 1 374 52 73 THR HB H 3.68 . 1 375 52 73 THR C C 177.71 . 1 376 52 73 THR CA C 60.68 . 1 377 52 73 THR CB C 69.16 . 1 378 52 73 THR N N 117.65 . 1 379 53 74 LEU H H 8.46 . 1 380 53 74 LEU HA H 4.34 . 1 381 53 74 LEU HB2 H 0.48 . 2 382 53 74 LEU HB3 H 0.50 . 2 383 53 74 LEU C C 179.95 . 1 384 53 74 LEU CA C 52.96 . 1 385 53 74 LEU CB C 44.56 . 1 386 53 74 LEU N N 128.06 . 1 387 54 75 GLY H H 9.15 . 1 388 54 75 GLY HA2 H 3.65 . 2 389 54 75 GLY HA3 H 3.75 . 2 390 54 75 GLY C C 179.00 . 1 391 54 75 GLY CA C 46.92 . 1 392 54 75 GLY N N 113.02 . 1 393 55 76 GLY H H 8.22 . 1 394 55 76 GLY HA2 H 3.38 . 2 395 55 76 GLY HA3 H 4.03 . 2 396 55 76 GLY C C 177.38 . 1 397 55 76 GLY CA C 44.60 . 1 398 55 76 GLY N N 104.17 . 1 399 56 77 GLU H H 7.74 . 1 400 56 77 GLU HA H 4.52 . 1 401 56 77 GLU HB2 H 1.87 . 2 402 56 77 GLU HB3 H 1.87 . 2 403 56 77 GLU C C 178.28 . 1 404 56 77 GLU CA C 53.85 . 1 405 56 77 GLU CB C 31.13 . 1 406 56 77 GLU N N 120.77 . 1 407 57 78 ASP H H 8.42 . 1 408 57 78 ASP HA H 4.73 . 1 409 57 78 ASP HB2 H 2.32 . 2 410 57 78 ASP HB3 H 2.56 . 2 411 57 78 ASP C C 179.90 . 1 412 57 78 ASP CA C 53.95 . 1 413 57 78 ASP CB C 41.35 . 1 414 57 78 ASP N N 121.11 . 1 415 58 79 VAL H H 9.01 . 1 416 58 79 VAL HA H 3.99 . 1 417 58 79 VAL HB H 1.40 . 1 418 58 79 VAL C C 177.59 . 1 419 58 79 VAL CA C 61.28 . 1 420 58 79 VAL CB C 34.57 . 1 421 58 79 VAL N N 127.54 . 1 422 59 80 ARG H H 7.73 . 1 423 59 80 ARG HA H 4.88 . 1 424 59 80 ARG HB2 H 2 . 2 425 59 80 ARG HB3 H 2 . 2 426 59 80 ARG C C 177.62 . 1 427 59 80 ARG CA C 53.99 . 1 428 59 80 ARG CB C 31.64 . 1 429 59 80 ARG N N 124.06 . 1 430 60 81 LEU H H 8.28 . 1 431 60 81 LEU HA H 5.24 . 1 432 60 81 LEU HB2 H 1.47 . 2 433 60 81 LEU HB3 H 1.14 . 2 434 60 81 LEU C C 180.14 . 1 435 60 81 LEU CA C 52.50 . 1 436 60 81 LEU CB C 43.44 . 1 437 60 81 LEU N N 120.93 . 1 438 61 82 LEU H H 8.79 . 1 439 61 82 LEU HA H 5.40 . 1 440 61 82 LEU HB2 H 2.00 . 2 441 61 82 LEU HB3 H 2.00 . 2 442 61 82 LEU C C 178.50 . 1 443 61 82 LEU CA C 53.75 . 1 444 61 82 LEU CB C 46.31 . 1 445 61 82 LEU N N 122.16 . 1 446 62 83 VAL H H 9.16 . 1 447 62 83 VAL HA H 5.19 . 1 448 62 83 VAL HB H 1.96 . 1 449 62 83 VAL C C 1 . 1 450 62 83 VAL CA C 59.02 . 1 451 62 83 VAL CB C 35.17 . 1 452 62 83 VAL N N 127.61 . 1 453 63 84 PRO C C 182.46 . 1 454 63 84 PRO CA C 62.63 . 1 455 63 84 PRO CB C 6.11 . 1 456 64 85 THR H H 9.36 . 1 457 64 85 THR HA H 4.33 . 1 458 64 85 THR HB H 4.46 . 1 459 64 85 THR C C 178.51 . 1 460 64 85 THR CA C 60.20 . 1 461 64 85 THR CB C 67.38 . 1 462 64 85 THR N N 113.10 . 1 463 65 86 THR H H 6.87 . 1 464 65 86 THR HA H 4.12 . 1 465 65 86 THR HB H 4.32 . 1 466 65 86 THR C C 179.93 . 1 467 65 86 THR CA C 60.48 . 1 468 65 86 THR CB C 70.67 . 1 469 65 86 THR N N 110.46 . 1 470 66 87 PHE H H 7.95 . 1 471 66 87 PHE HA H 4.12 . 1 472 66 87 PHE HB2 H 3.06 . 2 473 66 87 PHE HB3 H 3.06 . 2 474 66 87 PHE C C 183.13 . 1 475 66 87 PHE CA C 60.54 . 1 476 66 87 PHE CB C 38.73 . 1 477 66 87 PHE N N 114.98 . 1 478 67 88 MET H H 8.78 . 1 479 67 88 MET HA H 4.13 . 1 480 67 88 MET HB2 H 2.07 . 2 481 67 88 MET HB3 H 2.56 . 2 482 67 88 MET C C 183.25 . 1 483 67 88 MET CA C 58.31 . 1 484 67 88 MET CB C 31.90 . 1 485 67 88 MET N N 123.05 . 1 486 68 89 ASN H H 8.59 . 1 487 68 89 ASN HA H 4.13 . 1 488 68 89 ASN HB2 H 2.62 . 2 489 68 89 ASN HB3 H 2.97 . 2 490 68 89 ASN C C 177.26 . 1 491 68 89 ASN CA C 53.97 . 1 492 68 89 ASN CB C 36.28 . 1 493 68 89 ASN N N 114.90 . 1 494 69 90 LEU H H 7.55 . 1 495 69 90 LEU HA H 4.94 . 1 496 69 90 LEU HB2 H 1.41 . 2 497 69 90 LEU HB3 H 1.41 . 2 498 69 90 LEU C C 182.02 . 1 499 69 90 LEU CA C 53.54 . 1 500 69 90 LEU CB C 43.03 . 1 501 69 90 LEU N N 118.96 . 1 502 70 91 SER H H 7.57 . 1 503 70 91 SER HA H 4.30 . 1 504 70 91 SER HB2 H 3.66 . 2 505 70 91 SER HB3 H 3.66 . 2 506 70 91 SER C C 179.87 . 1 507 70 91 SER CA C 62.89 . 1 508 70 91 SER CB C 65.03 . 1 509 70 91 SER N N 114.19 . 1 510 71 92 GLY H H 10.23 . 1 511 71 92 GLY HA2 H 3.38 . 2 512 71 92 GLY HA3 H 3.33 . 2 513 71 92 GLY C C 178.72 . 1 514 71 92 GLY CA C 47.89 . 1 515 71 92 GLY N N 109.51 . 1 516 72 93 LYS H H 8.07 . 1 517 72 93 LYS HA H 3.87 . 1 518 72 93 LYS HB2 H 1.61 . 2 519 72 93 LYS HB3 H 1.61 . 2 520 72 93 LYS C C 182.89 . 1 521 72 93 LYS CA C 58.94 . 1 522 72 93 LYS CB C 32.32 . 1 523 72 93 LYS N N 120.86 . 1 524 73 94 ALA H H 6.79 . 1 525 73 94 ALA HA H 4.42 . 1 526 73 94 ALA HB H 1.74 . 1 527 73 94 ALA C C 181.92 . 1 528 73 94 ALA CA C 54.56 . 1 529 73 94 ALA CB C 19.80 . 1 530 73 94 ALA N N 120.77 . 1 531 74 95 VAL H H 7.17 . 1 532 74 95 VAL HA H 3.07 . 1 533 74 95 VAL HB H 1.69 . 1 534 74 95 VAL C C 180.95 . 1 535 74 95 VAL CA C 66.85 . 1 536 74 95 VAL CB C 31.72 . 1 537 74 95 VAL N N 114.61 . 1 538 75 96 ALA H H 8.74 . 1 539 75 96 ALA HA H 3.93 . 1 540 75 96 ALA HB H 1.30 . 1 541 75 96 ALA C C 184.07 . 1 542 75 96 ALA CA C 54.68 . 1 543 75 96 ALA CB C 17.94 . 1 544 75 96 ALA N N 118.43 . 1 545 76 97 ALA H H 7.51 . 1 546 76 97 ALA HA H 4.26 . 1 547 76 97 ALA HB H 1.90 . 1 548 76 97 ALA C C 184.53 . 1 549 76 97 ALA CA C 55.18 . 1 550 76 97 ALA CB C 18.10 . 1 551 76 97 ALA N N 119.93 . 1 552 77 98 MET H H 7.82 . 1 553 77 98 MET HA H 3.78 . 1 554 77 98 MET HB2 H 1.85 . 2 555 77 98 MET HB3 H 2.56 . 2 556 77 98 MET C C 181.40 . 1 557 77 98 MET CA C 59.35 . 1 558 77 98 MET CB C 32.80 . 1 559 77 98 MET N N 117.31 . 1 560 78 99 ALA H H 8.95 . 1 561 78 99 ALA HA H 3.92 . 1 562 78 99 ALA HB H 1.31 . 1 563 78 99 ALA C C 184.15 . 1 564 78 99 ALA CA C 55.44 . 1 565 78 99 ALA CB C 16.84 . 1 566 78 99 ALA N N 120.50 . 1 567 79 100 SER H H 8.34 . 1 568 79 100 SER HA H 4.24 . 1 569 79 100 SER HB2 H 3.95 . 2 570 79 100 SER HB3 H 3.95 . 2 571 79 100 SER C C 181.12 . 1 572 79 100 SER CA C 60.76 . 1 573 79 100 SER CB C 62.50 . 1 574 79 100 SER N N 110.76 . 1 575 80 101 PHE H H 7.55 . 1 576 80 101 PHE HA H 3.95 . 1 577 80 101 PHE HB2 H 2.62 . 2 578 80 101 PHE HB3 H 2.62 . 2 579 80 101 PHE C C 180.92 . 1 580 80 101 PHE CA C 61.71 . 1 581 80 101 PHE CB C 39.98 . 1 582 80 101 PHE N N 122.42 . 1 583 81 102 PHE H H 7.63 . 1 584 81 102 PHE HA H 4.43 . 1 585 81 102 PHE HB2 H 2.50 . 2 586 81 102 PHE HB3 H 3.39 . 2 587 81 102 PHE C C 177.73 . 1 588 81 102 PHE CA C 58.51 . 1 589 81 102 PHE CB C 39.17 . 1 590 81 102 PHE N N 112.16 . 1 591 82 103 ARG H H 7.55 . 1 592 82 103 ARG HA H 3.86 . 1 593 82 103 ARG HB2 H 1.76 . 2 594 82 103 ARG HB3 H 2.04 . 2 595 82 103 ARG C C 178.53 . 1 596 82 103 ARG CA C 56.85 . 1 597 82 103 ARG CB C 25.76 . 1 598 82 103 ARG N N 118.90 . 1 599 83 104 ILE H H 8.66 . 1 600 83 104 ILE HA H 3.89 . 1 601 83 104 ILE HB H 1.42 . 1 602 83 104 ILE C C 179.18 . 1 603 83 104 ILE CA C 60.93 . 1 604 83 104 ILE CB C 40.63 . 1 605 83 104 ILE N N 121.69 . 1 606 84 105 ASN H H 9.03 . 1 607 84 105 ASN HA H 4.92 . 1 608 84 105 ASN HB2 H 2.55 . 2 609 84 105 ASN HB3 H 2.80 . 2 610 84 105 ASN CA C 51.68 . 1 611 84 105 ASN CB C 38.24 . 1 612 84 105 ASN N N 126.65 . 1 613 85 106 PRO HA H 4.00 . 1 614 85 106 PRO HB2 H 2.00 . 2 615 85 106 PRO HB3 H 2.00 . 2 616 85 106 PRO C C 179.50 . 1 617 85 106 PRO CA C 66.54 . 1 618 85 106 PRO CB C 31.00 . 1 619 86 107 ASP H H 7.98 . 1 620 86 107 ASP HA H 4.47 . 1 621 86 107 ASP HB2 H 2.55 . 2 622 86 107 ASP HB3 H 2.55 . 2 623 86 107 ASP C C 179.77 . 1 624 86 107 ASP CA C 54.80 . 1 625 86 107 ASP CB C 38.36 . 1 626 86 107 ASP N N 109.99 . 1 627 87 108 GLU H H 8.08 . 1 628 87 108 GLU HA H 4.60 . 1 629 87 108 GLU HB2 H 2.55 . 2 630 87 108 GLU HB3 H 2.55 . 2 631 87 108 GLU C C 179.05 . 1 632 87 108 GLU CA C 54.64 . 1 633 87 108 GLU CB C 30.60 . 1 634 87 108 GLU N N 116.63 . 1 635 88 109 ILE H H 7.98 . 1 636 88 109 ILE HA H 4.83 . 1 637 88 109 ILE HB H 2.07 . 1 638 88 109 ILE C C 177.15 . 1 639 88 109 ILE CA C 60.47 . 1 640 88 109 ILE CB C 39.75 . 1 641 88 109 ILE N N 122.45 . 1 642 89 110 LEU H H 8.87 . 1 643 89 110 LEU HA H 5.10 . 1 644 89 110 LEU HB2 H 1.87 . 2 645 89 110 LEU HB3 H 1.87 . 2 646 89 110 LEU C C 177.92 . 1 647 89 110 LEU CA C 52.77 . 1 648 89 110 LEU CB C 45.68 . 1 649 89 110 LEU N N 127.60 . 1 650 90 111 VAL H H 9.53 . 1 651 90 111 VAL HA H 4.68 . 1 652 90 111 VAL HB H 2.22 . 1 653 90 111 VAL C C 178.25 . 1 654 90 111 VAL CA C 60.73 . 1 655 90 111 VAL CB C 33.06 . 1 656 90 111 VAL N N 127.32 . 1 657 91 112 ALA H H 10.04 . 1 658 91 112 ALA HA H 5.45 . 1 659 91 112 ALA HB H 1.35 . 1 660 91 112 ALA C C 179.58 . 1 661 91 112 ALA CA C 49.90 . 1 662 91 112 ALA CB C 21.42 . 1 663 91 112 ALA N N 132.66 . 1 664 92 113 HIS H H 8.77 . 1 665 92 113 HIS HA H 5.29 . 1 666 92 113 HIS HB2 H 2.62 . 2 667 92 113 HIS HB3 H 2.62 . 2 668 92 113 HIS C C 175.31 . 1 669 92 113 HIS CA C 53.31 . 1 670 92 113 HIS CB C 32.38 . 1 671 92 113 HIS N N 118.43 . 1 672 93 114 ASP H H 10.35 . 1 673 93 114 ASP HA H 4.34 . 1 674 93 114 ASP HB2 H 2.32 . 2 675 93 114 ASP HB3 H 2.82 . 2 676 93 114 ASP C C 181.17 . 1 677 93 114 ASP CA C 53.37 . 1 678 93 114 ASP CB C 39.76 . 1 679 93 114 ASP N N 116.65 . 1 680 94 115 GLU H H 8.86 . 1 681 94 115 GLU HA H 5.07 . 1 682 94 115 GLU C C 178.69 . 1 683 94 115 GLU CA C 53.57 . 1 684 94 115 GLU CB C 32.70 . 1 685 94 115 GLU N N 126.59 . 1 686 95 116 LEU H H 8.53 . 1 687 95 116 LEU HA H 4.73 . 1 688 95 116 LEU HB2 H 1.47 . 2 689 95 116 LEU HB3 H 1.71 . 2 690 95 116 LEU C C 182.52 . 1 691 95 116 LEU CA C 56.39 . 1 692 95 116 LEU CB C 43.95 . 1 693 95 116 LEU N N 131.87 . 1 694 96 117 ASP H H 9.20 . 1 695 96 117 ASP HA H 4.52 . 1 696 96 117 ASP HB2 H 2.39 . 2 697 96 117 ASP HB3 H 2.59 . 2 698 96 117 ASP C C 178.98 . 1 699 96 117 ASP CA C 54.39 . 1 700 96 117 ASP CB C 40.43 . 1 701 96 117 ASP N N 115.41 . 1 702 97 118 LEU H H 7.28 . 1 703 97 118 LEU HA H 4.77 . 1 704 97 118 LEU CA C 50.82 . 1 705 97 118 LEU CB C 44.62 . 1 706 97 118 LEU N N 119.54 . 1 707 99 120 PRO C C 181.59 . 1 708 99 120 PRO CA C 62.63 . 1 709 99 120 PRO CB C 31.21 . 1 710 100 121 GLY H H 9.63 . 1 711 100 121 GLY HA2 H 3.70 . 2 712 100 121 GLY HA3 H 4.40 . 2 713 100 121 GLY C C 176.26 . 1 714 100 121 GLY CA C 45.63 . 1 715 100 121 GLY N N 113.31 . 1 716 101 122 VAL H H 7.53 . 1 717 101 122 VAL HA H 4.66 . 1 718 101 122 VAL HB H 2.06 . 1 719 101 122 VAL C C 178.75 . 1 720 101 122 VAL CA C 59.92 . 1 721 101 122 VAL CB C 34.66 . 1 722 101 122 VAL N N 117.27 . 1 723 102 123 ALA H H 9.17 . 1 724 102 123 ALA HA H 5.20 . 1 725 102 123 ALA HB H 0.98 . 1 726 102 123 ALA C C 181.67 . 1 727 102 123 ALA CA C 50.90 . 1 728 102 123 ALA CB C 21.79 . 1 729 102 123 ALA N N 128.79 . 1 730 103 124 LYS H H 7.94 . 1 731 103 124 LYS HA H 4.70 . 1 732 103 124 LYS C C 178.80 . 1 733 103 124 LYS CA C 54.22 . 1 734 103 124 LYS CB C 39.12 . 1 735 103 124 LYS N N 114.07 . 1 736 104 125 PHE H H 8.31 . 1 737 104 125 PHE HA H 5.85 . 1 738 104 125 PHE HB2 H 3.16 . 2 739 104 125 PHE HB3 H 2.72 . 2 740 104 125 PHE C C 182.29 . 1 741 104 125 PHE CA C 56.10 . 1 742 104 125 PHE CB C 41.00 . 1 743 104 125 PHE N N 122.45 . 1 744 105 126 LYS H H 9.12 . 1 745 105 126 LYS HA H 4.43 . 1 746 105 126 LYS HB2 H 1.80 . 2 747 105 126 LYS HB3 H 1.80 . 2 748 105 126 LYS C C 176.98 . 1 749 105 126 LYS CA C 56.01 . 1 750 105 126 LYS CB C 37.88 . 1 751 105 126 LYS N N 123.41 . 1 752 106 127 LEU H H 8.54 . 1 753 106 127 LEU HA H 4.48 . 1 754 106 127 LEU HB2 H 1.55 . 2 755 106 127 LEU HB3 H 1.55 . 2 756 106 127 LEU C C 180.28 . 1 757 106 127 LEU CA C 53.72 . 1 758 106 127 LEU CB C 41.41 . 1 759 106 127 LEU N N 128.26 . 1 760 107 128 GLY H H 7.29 . 1 761 107 128 GLY HA2 H 3.76 . 2 762 107 128 GLY HA3 H 3.92 . 2 763 107 128 GLY C C 175.34 . 1 764 107 128 GLY CA C 44.03 . 1 765 107 128 GLY N N 113.35 . 1 766 108 129 GLY H H 7.68 . 1 767 108 129 GLY HA2 H 3.50 . 2 768 108 129 GLY HA3 H 4.10 . 2 769 108 129 GLY C C 179.24 . 1 770 108 129 GLY CA C 43.35 . 1 771 108 129 GLY N N 101.91 . 1 772 109 130 GLY H H 7.93 . 1 773 109 130 GLY HA2 H 3.60 . 2 774 109 130 GLY HA3 H 3.98 . 2 775 109 130 GLY C C 178.39 . 1 776 109 130 GLY CA C 44.45 . 1 777 109 130 GLY N N 105.34 . 1 778 110 131 HIS H H 7.43 . 1 779 110 131 HIS HA H 4.49 . 1 780 110 131 HIS HB2 H 3.55 . 2 781 110 131 HIS HB3 H 3.55 . 2 782 110 131 HIS C C 181.60 . 1 783 110 131 HIS CA C 54.82 . 1 784 110 131 HIS CB C 31.62 . 1 785 110 131 HIS N N 115.19 . 1 786 111 132 GLY H H 8.38 . 1 787 111 132 GLY HA2 H 3.73 . 2 788 111 132 GLY HA3 H 3.92 . 2 789 111 132 GLY CA C 46.76 . 1 790 111 132 GLY N N 112.16 . 1 791 112 133 GLY H H 10.94 . 1 792 112 133 GLY HA2 H 3.63 . 2 793 112 133 GLY HA3 H 4.20 . 2 794 112 133 GLY C C 181.20 . 1 795 112 133 GLY CA C 44.43 . 1 796 112 133 GLY N N 112.68 . 1 797 113 134 HIS H H 8.14 . 1 798 113 134 HIS HA H 4.26 . 1 799 113 134 HIS HB2 H 3.04 . 2 800 113 134 HIS HB3 H 3.04 . 2 801 113 134 HIS C C 180.99 . 1 802 113 134 HIS CA C 57.57 . 1 803 113 134 HIS CB C 31.84 . 1 804 113 134 HIS N N 124.50 . 1 805 114 135 ASN H H 8.99 . 1 806 114 135 ASN HA H 4.23 . 1 807 114 135 ASN HB2 H 2.55 . 2 808 114 135 ASN HB3 H 2.55 . 2 809 114 135 ASN C C 180.62 . 1 810 114 135 ASN CA C 55.80 . 1 811 114 135 ASN CB C 38.10 . 1 812 114 135 ASN N N 126.70 . 1 813 115 136 GLY H H 9.36 . 1 814 115 136 GLY HA2 H 3.73 . 2 815 115 136 GLY HA3 H 4.33 . 2 816 115 136 GLY C C 179.06 . 1 817 115 136 GLY CA C 47.04 . 1 818 115 136 GLY N N 113.20 . 1 819 116 137 LEU H H 8.55 . 1 820 116 137 LEU HA H 3.87 . 1 821 116 137 LEU HB2 H 2.20 . 2 822 116 137 LEU HB3 H 2.20 . 2 823 116 137 LEU C C 182.87 . 1 824 116 137 LEU CA C 58.01 . 1 825 116 137 LEU CB C 42.12 . 1 826 116 137 LEU N N 122.38 . 1 827 117 138 LYS H H 8.43 . 1 828 117 138 LYS HA H 3.59 . 1 829 117 138 LYS HB2 H 1.23 . 2 830 117 138 LYS HB3 H 1.61 . 2 831 117 138 LYS C C 182.26 . 1 832 117 138 LYS CA C 60.30 . 1 833 117 138 LYS CB C 32.88 . 1 834 117 138 LYS N N 117.14 . 1 835 118 139 ASP H H 7.11 . 1 836 118 139 ASP HA H 4.50 . 1 837 118 139 ASP HB2 H 2.78 . 2 838 118 139 ASP HB3 H 2.78 . 2 839 118 139 ASP C C 182.39 . 1 840 118 139 ASP CA C 57.78 . 1 841 118 139 ASP CB C 43.03 . 1 842 118 139 ASP N N 117.93 . 1 843 119 140 ILE H H 7.89 . 1 844 119 140 ILE HA H 3.26 . 1 845 119 140 ILE HB H 1.57 . 1 846 119 140 ILE C C 180.18 . 1 847 119 140 ILE CA C 66.45 . 1 848 119 140 ILE CB C 37.60 . 1 849 119 140 ILE N N 119.51 . 1 850 120 141 ILE H H 8.29 . 1 851 120 141 ILE HA H 3.57 . 1 852 120 141 ILE HB H 1.83 . 1 853 120 141 ILE C C 183.19 . 1 854 120 141 ILE CA C 65.31 . 1 855 120 141 ILE CB C 38.65 . 1 856 120 141 ILE N N 117.09 . 1 857 121 142 SER H H 7.40 . 1 858 121 142 SER HA H 4.15 . 1 859 121 142 SER HB2 H 3.95 . 2 860 121 142 SER HB3 H 3.95 . 2 861 121 142 SER C C 182.77 . 1 862 121 142 SER CA C 61.32 . 1 863 121 142 SER CB C 62.80 . 1 864 121 142 SER N N 110.60 . 1 865 122 143 LYS H H 8.57 . 1 866 122 143 LYS HA H 4.06 . 1 867 122 143 LYS HB2 H 1.53 . 2 868 122 143 LYS HB3 H 1.68 . 2 869 122 143 LYS C C 182.12 . 1 870 122 143 LYS CA C 58.42 . 1 871 122 143 LYS CB C 31.38 . 1 872 122 143 LYS N N 120.28 . 1 873 123 144 LEU H H 7.86 . 1 874 123 144 LEU HA H 4.42 . 1 875 123 144 LEU HB2 H 2 . 2 876 123 144 LEU HB3 H 1.68 . 2 877 123 144 LEU C C 179.79 . 1 878 123 144 LEU CA C 54.10 . 1 879 123 144 LEU CB C 40.28 . 1 880 123 144 LEU N N 119.38 . 1 881 124 145 GLY H H 7.76 . 1 882 124 145 GLY HA2 H 3.73 . 2 883 124 145 GLY HA3 H 3.95 . 2 884 124 145 GLY C C 178.86 . 1 885 124 145 GLY CA C 46.16 . 1 886 124 145 GLY N N 107.58 . 1 887 125 146 ASN H H 8.08 . 1 888 125 146 ASN HA H 4.12 . 1 889 125 146 ASN HB2 H 2.78 . 2 890 125 146 ASN HB3 H 2.99 . 2 891 125 146 ASN C C 177.41 . 1 892 125 146 ASN CA C 53.68 . 1 893 125 146 ASN CB C 36.24 . 1 894 125 146 ASN N N 117.58 . 1 895 126 147 ASN H H 7.20 . 1 896 126 147 ASN HA H 5.13 . 1 897 126 147 ASN HB2 H 2.35 . 2 898 126 147 ASN HB3 H 3.05 . 2 899 126 147 ASN CA C 48.76 . 1 900 126 147 ASN CB C 40.72 . 1 901 126 147 ASN N N 116.05 . 1 902 127 148 PRO C C 181.97 . 1 903 127 148 PRO CA C 61.59 . 1 904 127 148 PRO CB C 32.04 . 1 905 128 149 ASN H H 8.44 . 1 906 128 149 ASN HA H 4.23 . 1 907 128 149 ASN HB2 H 2.56 . 2 908 128 149 ASN HB3 H 2.83 . 2 909 128 149 ASN C C 175.95 . 1 910 128 149 ASN CA C 54.29 . 1 911 128 149 ASN CB C 36.85 . 1 912 128 149 ASN N N 124.17 . 1 913 129 150 PHE H H 7.36 . 1 914 129 150 PHE HA H 5.09 . 1 915 129 150 PHE HB2 H 2.80 . 2 916 129 150 PHE HB3 H 3.23 . 2 917 129 150 PHE C C 180.94 . 1 918 129 150 PHE CA C 53.83 . 1 919 129 150 PHE CB C 42.15 . 1 920 129 150 PHE N N 114.46 . 1 921 130 151 HIS H H 8.80 . 1 922 130 151 HIS HA H 4.99 . 1 923 130 151 HIS HB2 H 3.16 . 2 924 130 151 HIS HB3 H 3.16 . 2 925 130 151 HIS C C 179.42 . 1 926 130 151 HIS CA C 56.75 . 1 927 130 151 HIS CB C 32.52 . 1 928 130 151 HIS N N 122.69 . 1 929 131 152 ARG H H 10.02 . 1 930 131 152 ARG HA H 5.92 . 1 931 131 152 ARG HB2 H 2.62 . 2 932 131 152 ARG HB3 H 2.62 . 2 933 131 152 ARG C C 178.66 . 1 934 131 152 ARG CA C 54.83 . 1 935 131 152 ARG CB C 31.82 . 1 936 131 152 ARG N N 120.80 . 1 937 132 153 LEU H H 8.71 . 1 938 132 153 LEU HA H 4.84 . 1 939 132 153 LEU C C 176.68 . 1 940 132 153 LEU CA C 53.33 . 1 941 132 153 LEU CB C 42.68 . 1 942 132 153 LEU N N 124.09 . 1 943 133 154 ARG H H 9.21 . 1 944 133 154 ARG HA H 3.27 . 1 945 133 154 ARG C C 178.40 . 1 946 133 154 ARG CA C 53.45 . 1 947 133 154 ARG CB C 31.49 . 1 948 133 154 ARG N N 125.65 . 1 949 134 155 ILE H H 8.49 . 1 950 134 155 ILE HA H 3.80 . 1 951 134 155 ILE HB H 1.43 . 1 952 134 155 ILE C C 179.08 . 1 953 134 155 ILE CA C 60.91 . 1 954 134 155 ILE CB C 37.62 . 1 955 134 155 ILE N N 124.16 . 1 956 135 156 GLY H H 8.43 . 1 957 135 156 GLY HA2 H 4.16 . 2 958 135 156 GLY HA3 H 3.47 . 2 959 135 156 GLY C C 178.41 . 1 960 135 156 GLY CA C 48.52 . 1 961 135 156 GLY N N 115.73 . 1 962 136 157 ILE H H 7.89 . 1 963 136 157 ILE HA H 4.63 . 1 964 136 157 ILE HB H 0.00 . 1 965 136 157 ILE C C 181.40 . 1 966 136 157 ILE CA C 60.32 . 1 967 136 157 ILE CB C 41.03 . 1 968 136 157 ILE N N 113.60 . 1 969 137 158 GLY H H 8.97 . 1 970 137 158 GLY C C 172.40 . 1 971 137 158 GLY CA C 44.82 . 1 972 137 158 GLY N N 111.61 . 1 973 138 159 HIS H H 7.35 . 1 974 138 159 HIS CA C 52.25 . 1 975 138 159 HIS CB C 30.56 . 1 976 138 159 HIS N N 107.69 . 1 977 139 160 PRO C C 181.50 . 1 978 140 161 GLY H H 8.05 . 1 979 140 161 GLY HA2 H 3.69 . 2 980 140 161 GLY HA3 H 3.83 . 2 981 140 161 GLY C C 177.37 . 1 982 140 161 GLY CA C 45.77 . 1 983 140 161 GLY N N 104.70 . 1 984 141 162 ASP H H 7.24 . 1 985 141 162 ASP HA H 4.65 . 1 986 141 162 ASP HB2 H 2.48 . 2 987 141 162 ASP HB3 H 2.59 . 2 988 141 162 ASP C C 180.84 . 1 989 141 162 ASP CA C 52.39 . 1 990 141 162 ASP CB C 41.98 . 1 991 141 162 ASP N N 118.21 . 1 992 142 163 LYS H H 8.72 . 1 993 142 163 LYS HA H 3.96 . 1 994 142 163 LYS HB2 H 1.79 . 2 995 142 163 LYS HB3 H 1.79 . 2 996 142 163 LYS C C 181.76 . 1 997 142 163 LYS CA C 58.25 . 1 998 142 163 LYS CB C 31.61 . 1 999 142 163 LYS N N 125.41 . 1 1000 143 164 ASN H H 8.70 . 1 1001 143 164 ASN HA H 4.59 . 1 1002 143 164 ASN HB2 H 2.79 . 2 1003 143 164 ASN HB3 H 2.79 . 2 1004 143 164 ASN C C 180.31 . 1 1005 143 164 ASN CA C 54.24 . 1 1006 143 164 ASN CB C 37.94 . 1 1007 143 164 ASN N N 116.94 . 1 1008 144 165 LYS H H 7.85 . 1 1009 144 165 LYS HA H 4.56 . 1 1010 144 165 LYS HB2 H 1.66 . 2 1011 144 165 LYS HB3 H 2.12 . 2 1012 144 165 LYS C C 180.71 . 1 1013 144 165 LYS CA C 55.20 . 1 1014 144 165 LYS CB C 32.56 . 1 1015 144 165 LYS N N 118.90 . 1 1016 145 166 VAL H H 7.24 . 1 1017 145 166 VAL HA H 3.50 . 1 1018 145 166 VAL HB H 2.09 . 1 1019 145 166 VAL C C 180.41 . 1 1020 145 166 VAL CA C 66.97 . 1 1021 145 166 VAL CB C 32.03 . 1 1022 145 166 VAL N N 119.75 . 1 1023 146 167 VAL H H 8.24 . 1 1024 146 167 VAL HA H 3.68 . 1 1025 146 167 VAL HB H 1.93 . 1 1026 146 167 VAL C C 181.51 . 1 1027 146 167 VAL CA C 66.66 . 1 1028 146 167 VAL CB C 30.90 . 1 1029 146 167 VAL N N 120.75 . 1 1030 147 168 GLY H H 8.06 . 1 1031 147 168 GLY HA2 H 3.75 . 2 1032 147 168 GLY HA3 H 3.75 . 2 1033 147 168 GLY C C 179.75 . 1 1034 147 168 GLY CA C 45.70 . 1 1035 147 168 GLY N N 104.72 . 1 1036 148 169 PHE H H 7.91 . 1 1037 148 169 PHE HA H 4.24 . 1 1038 148 169 PHE HB2 H 3.15 . 2 1039 148 169 PHE HB3 H 3.15 . 2 1040 148 169 PHE C C 183.07 . 1 1041 148 169 PHE CA C 60.77 . 1 1042 148 169 PHE CB C 40.35 . 1 1043 148 169 PHE N N 122.12 . 1 1044 149 170 VAL H H 8.60 . 1 1045 149 170 VAL HA H 3.85 . 1 1046 149 170 VAL HB H 2.29 . 1 1047 149 170 VAL C C 179.13 . 1 1048 149 170 VAL CA C 65.37 . 1 1049 149 170 VAL CB C 30.94 . 1 1050 149 170 VAL N N 116.71 . 1 1051 150 171 LEU H H 7.21 . 1 1052 150 171 LEU HA H 4.62 . 1 1053 150 171 LEU HB2 H 1.75 . 2 1054 150 171 LEU HB3 H 1.79 . 2 1055 150 171 LEU C C 179.22 . 1 1056 150 171 LEU CA C 53.12 . 1 1057 150 171 LEU CB C 39.87 . 1 1058 150 171 LEU N N 116.13 . 1 1059 151 172 GLY H H 7.36 . 1 1060 151 172 GLY C C 176.21 . 1 1061 151 172 GLY CA C 43.05 . 1 1062 151 172 GLY N N 107.39 . 1 1063 152 173 LYS H H 8.38 . 1 1064 152 173 LYS HA H 4.94 . 1 1065 152 173 LYS HB2 H 1.82 . 2 1066 152 173 LYS HB3 H 1.82 . 2 1067 152 173 LYS CA C 52.97 . 1 1068 152 173 LYS CB C 33.37 . 1 1069 152 173 LYS N N 122.15 . 1 1070 154 175 PRO C C 181.18 . 1 1071 154 175 PRO CA C 61.96 . 1 1072 154 175 PRO CB C 32.02 . 1 1073 155 176 VAL H H 8.65 . 1 1074 155 176 VAL HA H 3.67 . 1 1075 155 176 VAL HB H 2.02 . 1 1076 155 176 VAL C C 181.46 . 1 1077 155 176 VAL CA C 66.24 . 1 1078 155 176 VAL CB C 31.32 . 1 1079 155 176 VAL N N 122.70 . 1 1080 156 177 SER H H 8.34 . 1 1081 156 177 SER HA H 4.02 . 1 1082 156 177 SER HB2 H 3.67 . 2 1083 156 177 SER HB3 H 3.82 . 2 1084 156 177 SER C C 180.70 . 1 1085 156 177 SER CA C 60.54 . 1 1086 156 177 SER CB C 61.28 . 1 1087 156 177 SER N N 113.27 . 1 1088 157 178 GLU H H 6.86 . 1 1089 157 178 GLU HA H 4.02 . 1 1090 157 178 GLU HB2 H 1.97 . 2 1091 157 178 GLU HB3 H 1.97 . 2 1092 157 178 GLU C C 181.76 . 1 1093 157 178 GLU CA C 58.52 . 1 1094 157 178 GLU CB C 30.68 . 1 1095 157 178 GLU N N 120.97 . 1 1096 158 179 GLN H H 8.59 . 1 1097 158 179 GLN HA H 3.60 . 1 1098 158 179 GLN HB2 H 2.04 . 2 1099 158 179 GLN HB3 H 2.15 . 2 1100 158 179 GLN C C 181.00 . 1 1101 158 179 GLN CA C 58.18 . 1 1102 158 179 GLN CB C 28.70 . 1 1103 158 179 GLN N N 120.30 . 1 1104 159 180 LYS H H 7.88 . 1 1105 159 180 LYS HA H 4.02 . 1 1106 159 180 LYS HB2 H 1.80 . 2 1107 159 180 LYS HB3 H 1.80 . 2 1108 159 180 LYS C C 182.36 . 1 1109 159 180 LYS CA C 59.11 . 1 1110 159 180 LYS CB C 32.31 . 1 1111 159 180 LYS N N 116.02 . 1 1112 160 181 LEU H H 6.75 . 1 1113 160 181 LEU HA H 3.96 . 1 1114 160 181 LEU C C 183.15 . 1 1115 160 181 LEU CA C 57.23 . 1 1116 160 181 LEU CB C 40.88 . 1 1117 160 181 LEU N N 116.38 . 1 1118 161 182 ILE H H 8.15 . 1 1119 161 182 ILE HA H 4.02 . 1 1120 161 182 ILE HB H 1.85 . 1 1121 161 182 ILE C C 182.23 . 1 1122 161 182 ILE CA C 64.97 . 1 1123 161 182 ILE CB C 38.70 . 1 1124 161 182 ILE N N 121.01 . 1 1125 162 183 ASP H H 9.00 . 1 1126 162 183 ASP HA H 4.29 . 1 1127 162 183 ASP HB2 H 2.55 . 2 1128 162 183 ASP HB3 H 2.77 . 2 1129 162 183 ASP C C 184.14 . 1 1130 162 183 ASP CA C 57.50 . 1 1131 162 183 ASP CB C 39.12 . 1 1132 162 183 ASP N N 119.59 . 1 1133 163 184 GLU H H 7.95 . 1 1134 163 184 GLU HA H 4.14 . 1 1135 163 184 GLU HB2 H 2.24 . 2 1136 163 184 GLU HB3 H 2.48 . 2 1137 163 184 GLU C C 183.24 . 1 1138 163 184 GLU CA C 59.14 . 1 1139 163 184 GLU CB C 29.34 . 1 1140 163 184 GLU N N 119.71 . 1 1141 164 185 ALA H H 8.28 . 1 1142 164 185 ALA HA H 4.06 . 1 1143 164 185 ALA HB H 1.38 . 1 1144 164 185 ALA C C 183.15 . 1 1145 164 185 ALA CA C 55.29 . 1 1146 164 185 ALA CB C 16.78 . 1 1147 164 185 ALA N N 124.30 . 1 1148 165 186 ILE H H 9.06 . 1 1149 165 186 ILE HA H 3.56 . 1 1150 165 186 ILE HB H 2.10 . 1 1151 165 186 ILE C C 181.21 . 1 1152 165 186 ILE CA C 66.65 . 1 1153 165 186 ILE CB C 37.38 . 1 1154 165 186 ILE N N 118.66 . 1 1155 166 187 ASP H H 7.89 . 1 1156 166 187 ASP HA H 4.24 . 1 1157 166 187 ASP HB2 H 2.75 . 2 1158 166 187 ASP HB3 H 2.75 . 2 1159 166 187 ASP C C 182.09 . 1 1160 166 187 ASP CA C 57.20 . 1 1161 166 187 ASP CB C 41.43 . 1 1162 166 187 ASP N N 120.83 . 1 1163 167 188 GLU H H 7.51 . 1 1164 167 188 GLU HA H 4.07 . 1 1165 167 188 GLU C C 183.60 . 1 1166 167 188 GLU CA C 58.07 . 1 1167 167 188 GLU CB C 27.64 . 1 1168 167 188 GLU N N 120.01 . 1 1169 168 189 ALA H H 9.20 . 1 1170 168 189 ALA HA H 3.77 . 1 1171 168 189 ALA HB H 1.22 . 1 1172 168 189 ALA C C 185.04 . 1 1173 168 189 ALA CA C 55.34 . 1 1174 168 189 ALA CB C 18.09 . 1 1175 168 189 ALA N N 122.74 . 1 1176 169 190 ALA H H 9.12 . 1 1177 169 190 ALA HA H 4.12 . 1 1178 169 190 ALA HB H 1.42 . 1 1179 169 190 ALA C C 183.70 . 1 1180 169 190 ALA CA C 56.19 . 1 1181 169 190 ALA CB C 17.15 . 1 1182 169 190 ALA N N 125.75 . 1 1183 170 191 ARG H H 7.92 . 1 1184 170 191 ARG HA H 4.10 . 1 1185 170 191 ARG HB2 H 1.79 . 2 1186 170 191 ARG HB3 H 1.97 . 2 1187 170 191 ARG C C 184.96 . 1 1188 170 191 ARG CA C 59.18 . 1 1189 170 191 ARG CB C 29.35 . 1 1190 170 191 ARG N N 120.42 . 1 1191 171 192 CYS H H 8.96 . 1 1192 171 192 CYS HA H 4.32 . 1 1193 171 192 CYS HB2 H 2.82 . 2 1194 171 192 CYS HB3 H 3.00 . 2 1195 171 192 CYS C C 181.47 . 1 1196 171 192 CYS CA C 63.86 . 1 1197 171 192 CYS CB C 27.01 . 1 1198 171 192 CYS N N 118.57 . 1 1199 172 193 THR H H 8.72 . 1 1200 172 193 THR HA H 4.47 . 1 1201 172 193 THR HB H 4.15 . 1 1202 172 193 THR C C 179.73 . 1 1203 172 193 THR CA C 68.64 . 1 1204 172 193 THR CB C 67.27 . 1 1205 172 193 THR N N 121.07 . 1 1206 173 194 GLU H H 7.65 . 1 1207 173 194 GLU HA H 3.88 . 1 1208 173 194 GLU HB2 H 2.01 . 2 1209 173 194 GLU HB3 H 2.10 . 2 1210 173 194 GLU C C 182.54 . 1 1211 173 194 GLU CA C 61.02 . 1 1212 173 194 GLU CB C 29.14 . 1 1213 173 194 GLU N N 120.03 . 1 1214 174 195 MET H H 7.73 . 1 1215 174 195 MET HA H 4.33 . 1 1216 174 195 MET HB2 H 2.18 . 2 1217 174 195 MET HB3 H 2.22 . 2 1218 174 195 MET C C 177.86 . 1 1219 174 195 MET CA C 57.88 . 1 1220 174 195 MET CB C 33.22 . 1 1221 174 195 MET N N 117.15 . 1 1222 175 196 TRP H H 8.14 . 1 1223 175 196 TRP HA H 3.96 . 1 1224 175 196 TRP HB2 H 3.57 . 2 1225 175 196 TRP HB3 H 3.57 . 2 1226 175 196 TRP C C 182.82 . 1 1227 175 196 TRP CA C 57.94 . 1 1228 175 196 TRP CB C 28.44 . 1 1229 175 196 TRP N N 124.40 . 1 1230 176 197 PHE H H 7.41 . 1 1231 176 197 PHE HA H 4.02 . 1 1232 176 197 PHE HB2 H 2.90 . 2 1233 176 197 PHE HB3 H 3.12 . 2 1234 176 197 PHE C C 181.09 . 1 1235 176 197 PHE CA C 61.36 . 1 1236 176 197 PHE CB C 38.92 . 1 1237 176 197 PHE N N 115.00 . 1 1238 177 198 THR H H 7.98 . 1 1239 177 198 THR HA H 4.32 . 1 1240 177 198 THR HB H 4.19 . 1 1241 177 198 THR C C 179.84 . 1 1242 177 198 THR CA C 63.76 . 1 1243 177 198 THR CB C 69.10 . 1 1244 177 198 THR N N 109.05 . 1 1245 178 199 ASP H H 9.21 . 1 1246 178 199 ASP HA H 4.84 . 1 1247 178 199 ASP HB2 H 2.44 . 2 1248 178 199 ASP HB3 H 2.62 . 2 1249 178 199 ASP C C 180.57 . 1 1250 178 199 ASP CA C 54.59 . 1 1251 178 199 ASP CB C 43.55 . 1 1252 178 199 ASP N N 121.13 . 1 1253 179 200 GLY H H 7.72 . 1 1254 179 200 GLY C C 177.00 . 1 1255 179 200 GLY CA C 44.65 . 1 1256 179 200 GLY N N 110.61 . 1 1257 180 201 LEU H H 8.22 . 1 1258 180 201 LEU C C 183.00 . 1 1259 180 201 LEU CA C 57.03 . 1 1260 180 201 LEU CB C 40.80 . 1 1261 180 201 LEU N N 121.10 . 1 1262 181 202 THR H H 8.33 . 1 1263 181 202 THR HA H 3.94 . 1 1264 181 202 THR HB H 3.60 . 1 1265 181 202 THR C C 179.90 . 1 1266 181 202 THR CA C 67.10 . 1 1267 181 202 THR CB C 68.00 . 1 1268 181 202 THR N N 118.90 . 1 1269 182 203 LYS H H 8.23 . 1 1270 182 203 LYS HA H 3.83 . 1 1271 182 203 LYS HB2 H 1.47 . 2 1272 182 203 LYS HB3 H 1.56 . 2 1273 182 203 LYS C C 183.27 . 1 1274 182 203 LYS CA C 59.43 . 1 1275 182 203 LYS CB C 32.04 . 1 1276 182 203 LYS N N 121.40 . 1 1277 183 204 ALA H H 7.54 . 1 1278 183 204 ALA HA H 4.10 . 1 1279 183 204 ALA HB H 1.34 . 1 1280 183 204 ALA C C 182.84 . 1 1281 183 204 ALA CA C 55.33 . 1 1282 183 204 ALA CB C 19.06 . 1 1283 183 204 ALA N N 121.30 . 1 1284 184 205 THR H H 8.40 . 1 1285 184 205 THR HA H 3.50 . 1 1286 184 205 THR HB H 3.90 . 1 1287 184 205 THR C C 179.04 . 1 1288 184 205 THR CA C 66.19 . 1 1289 184 205 THR CB C 68.28 . 1 1290 184 205 THR N N 114.11 . 1 1291 185 206 ASN H H 8.05 . 1 1292 185 206 ASN HA H 4.20 . 1 1293 185 206 ASN HB2 H 2.68 . 2 1294 185 206 ASN HB3 H 2.68 . 2 1295 185 206 ASN C C 182.05 . 1 1296 185 206 ASN CA C 55.25 . 1 1297 185 206 ASN CB C 37.25 . 1 1298 185 206 ASN N N 119.51 . 1 1299 186 207 ARG H H 7.37 . 1 1300 186 207 ARG HA H 4.09 . 1 1301 186 207 ARG HB2 H 1.70 . 2 1302 186 207 ARG HB3 H 1.90 . 2 1303 186 207 ARG C C 182.12 . 1 1304 186 207 ARG CA C 58.90 . 1 1305 186 207 ARG CB C 29.39 . 1 1306 186 207 ARG N N 117.99 . 1 1307 187 208 LEU H H 8.41 . 1 1308 187 208 LEU HA H 4.09 . 1 1309 187 208 LEU HB2 H 1.70 . 2 1310 187 208 LEU HB3 H 1.70 . 2 1311 187 208 LEU C C 183.48 . 1 1312 187 208 LEU CA C 58.33 . 1 1313 187 208 LEU CB C 40.26 . 1 1314 187 208 LEU N N 121.94 . 1 1315 188 209 HIS H H 9.17 . 1 1316 188 209 HIS HA H 4.83 . 1 1317 188 209 HIS HB2 H 3.22 . 2 1318 188 209 HIS HB3 H 3.22 . 2 1319 188 209 HIS C C 180.59 . 1 1320 188 209 HIS CA C 56.47 . 1 1321 188 209 HIS CB C 27.38 . 1 1322 188 209 HIS N N 115.03 . 1 1323 189 210 ALA H H 7.29 . 1 1324 189 210 ALA HA H 4.44 . 1 1325 189 210 ALA HB H 1.48 . 1 1326 189 210 ALA C C 180.89 . 1 1327 189 210 ALA CA C 51.73 . 1 1328 189 210 ALA CB C 19.18 . 1 1329 189 210 ALA N N 121.31 . 1 1330 190 211 PHE H H 7.69 . 1 1331 190 211 PHE HA H 4.34 . 1 1332 190 211 PHE HB2 H 2.24 . 2 1333 190 211 PHE HB3 H 3.40 . 2 1334 190 211 PHE C C 179.48 . 1 1335 190 211 PHE CA C 58.87 . 1 1336 190 211 PHE CB C 39.32 . 1 1337 190 211 PHE N N 121.43 . 1 1338 191 212 LYS H H 7.55 . 1 1339 191 212 LYS HA H 4.12 . 1 1340 191 212 LYS HB2 H 1.41 . 2 1341 191 212 LYS HB3 H 1.41 . 2 1342 191 212 LYS C C 178.01 . 1 1343 191 212 LYS CA C 55.53 . 1 1344 191 212 LYS CB C 34.25 . 1 1345 191 212 LYS N N 129.57 . 1 1346 192 213 ALA H H 8.45 . 1 1347 192 213 ALA HA H 3.90 . 1 1348 192 213 ALA HB H 1.62 . 1 1349 192 213 ALA C C 179.70 . 1 1350 192 213 ALA CA C 52.42 . 1 1351 192 213 ALA CB C 20.86 . 1 1352 192 213 ALA N N 129.85 . 1 1353 193 214 GLN H H 7.98 . 1 1354 193 214 GLN HA H 4.13 . 1 1355 193 214 GLN HB2 H 1.80 . 2 1356 193 214 GLN HB3 H 1.95 . 2 1357 193 214 GLN CA C 56.46 . 1 1358 193 214 GLN CB C 31.57 . 1 1359 193 214 GLN N N 123.39 . 1 stop_ save_