data_16133 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Backbone 1H, 13C, and 15N Chemical Shift Assignments for TolAIII residues 296-421 ; _BMRB_accession_number 16133 _BMRB_flat_file_name bmr16133.str _Entry_type original _Submission_date 2009-01-23 _Accession_date 2009-01-23 _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 Hecht Oliver . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 77 "13C chemical shifts" 145 "15N chemical shifts" 77 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2009-05-05 update BMRB 'complete entry citation' 2009-04-22 original author 'original release' stop_ loop_ _Related_BMRB_accession_number _Relationship 16130 'Tdom 40-76 TolAIII complex' 16131 Tdom40-76 16134 TolAIII+tdom stop_ save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title 'A common interaction for the entry of colicin N and filamentous phage into Escherichia coli' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 19306883 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Hecht Oliver . . 2 Ridley Helen . . 3 Lakey Jeremy H. . 4 Moore Geoffrey R. . stop_ _Journal_abbreviation 'J. Mol. Biol.' _Journal_name_full 'Journal of molecular biology' _Journal_volume 388 _Journal_issue 4 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 880 _Page_last 893 _Year 2009 _Details . save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name TolAIII _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label TolAIII $TolAIII stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state ? _System_paramagnetic no _System_thiol_state . _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_TolAIII _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common TolAIII _Molecular_mass . _Mol_thiol_state 'all disulfide bound' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 135 _Mol_residue_sequence ; HHHHHHSSQIFSVTLSSGKN APKTGGGAKGNNASPAGSGN TKNNGASGADINNYAGQIKS AIESKFYDASSYAGKTCTLR IKLAPDGMLLDIKPEGGDPA LCQAALAAAKLAKIPKPPSQ AVYEVFKNAPLDFKP ; loop_ _Residue_seq_code _Residue_label 1 HIS 2 HIS 3 HIS 4 HIS 5 HIS 6 HIS 7 SER 8 SER 9 GLN 10 ILE 11 PHE 12 SER 13 VAL 14 THR 15 LEU 16 SER 17 SER 18 GLY 19 LYS 20 ASN 21 ALA 22 PRO 23 LYS 24 THR 25 GLY 26 GLY 27 GLY 28 ALA 29 LYS 30 GLY 31 ASN 32 ASN 33 ALA 34 SER 35 PRO 36 ALA 37 GLY 38 SER 39 GLY 40 ASN 41 THR 42 LYS 43 ASN 44 ASN 45 GLY 46 ALA 47 SER 48 GLY 49 ALA 50 ASP 51 ILE 52 ASN 53 ASN 54 TYR 55 ALA 56 GLY 57 GLN 58 ILE 59 LYS 60 SER 61 ALA 62 ILE 63 GLU 64 SER 65 LYS 66 PHE 67 TYR 68 ASP 69 ALA 70 SER 71 SER 72 TYR 73 ALA 74 GLY 75 LYS 76 THR 77 CYS 78 THR 79 LEU 80 ARG 81 ILE 82 LYS 83 LEU 84 ALA 85 PRO 86 ASP 87 GLY 88 MET 89 LEU 90 LEU 91 ASP 92 ILE 93 LYS 94 PRO 95 GLU 96 GLY 97 GLY 98 ASP 99 PRO 100 ALA 101 LEU 102 CYS 103 GLN 104 ALA 105 ALA 106 LEU 107 ALA 108 ALA 109 ALA 110 LYS 111 LEU 112 ALA 113 LYS 114 ILE 115 PRO 116 LYS 117 PRO 118 PRO 119 SER 120 GLN 121 ALA 122 VAL 123 TYR 124 GLU 125 VAL 126 PHE 127 LYS 128 ASN 129 ALA 130 PRO 131 LEU 132 ASP 133 PHE 134 LYS 135 PRO 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 BMRB 16134 TolAIII 100.00 135 100.00 100.00 6.36e-91 PDB 1S62 "Solution Structure Of The Escherichia Coli Tola C-Terminal Domain" 71.85 106 100.00 100.00 1.51e-61 PDB 1TOL "Fusion Of N-Terminal Domain Of The Minor Coat Protein From Gene Iii In Phage M13, And C-Terminal Domain Of E. Coli Protein-Tola" 89.63 222 100.00 100.00 1.66e-77 PDB 2X9A "Crystal Structure Of G3p From Phage If1 In Complex With Its Coreceptor, The C-Terminal Domain Of Tola" 89.63 136 100.00 100.00 5.80e-78 EMBL CTW32328 "cell envelope integrity inner membrane protein TolA [Escherichia coli]" 93.33 421 97.62 97.62 4.82e-83 GB AHA63696 "TolA protein [Shigella dysenteriae 1617]" 83.70 116 99.12 99.12 1.07e-71 GB AHG07456 "TolA protein [Escherichia coli O145:H28 str. RM13514]" 93.33 368 97.62 97.62 8.74e-85 GB AHY69283 "TolA protein [Escherichia coli O145:H28 str. RM12581]" 93.33 368 97.62 97.62 8.74e-85 GB EGB67246 "TonB family protein domain-containing protein [Escherichia coli TA007]" 81.48 115 99.09 99.09 6.55e-70 GB EGC08283 "TonB family protein domain-containing protein [Escherichia fergusonii B253]" 71.85 98 96.91 97.94 3.54e-60 REF WP_000030617 "cell envelope integrity/translocation protein TolA [Escherichia coli]" 93.33 421 97.62 97.62 7.26e-83 REF WP_000030621 "cell envelope integrity/translocation protein TolA [Escherichia sp. TW09231]" 93.33 422 97.62 97.62 3.29e-83 REF WP_000030643 "cell envelope integrity/translocation protein TolA [Escherichia coli]" 93.33 437 97.62 97.62 2.62e-83 REF WP_000030697 "MULTISPECIES: cell envelope integrity/translocation protein TolA [Escherichia]" 93.33 422 97.62 97.62 4.04e-83 REF WP_000030705 "cell envelope integrity/translocation protein TolA [Escherichia sp. TW14182]" 93.33 425 97.62 97.62 2.25e-83 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $TolAIII '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 $TolAIII 'recombinant technology' . Escherichia coli . pet8c 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 $TolAIII 0.6 mM '[U-100% 13C; U-100% 15N]' H2O 90 % 'natural abundance' D2O 10 % 'natural abundance' stop_ save_ ############################ # Computer software used # ############################ save_NMRView _Saveframe_category software _Name NMRView _Version . loop_ _Vendor _Address _Electronic_address 'Johnson, One Moon Scientific' . . stop_ loop_ _Task 'chemical shift assignment' stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model INOVA _Field_strength 500 _Details . save_ save_spectrometer_2 _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model INOVA _Field_strength 600 _Details . save_ ############################# # NMR applied experiments # ############################# save_2D_1H-15N_HSQC_1 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-15N HSQC' _Sample_label $sample_1 save_ save_3D_HNCACB_2 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCACB' _Sample_label $sample_1 save_ save_3D_CBCA(CO)NH_3 _Saveframe_category NMR_applied_experiment _Experiment_name '3D CBCA(CO)NH' _Sample_label $sample_1 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' 0.35 . M pH 6.8 . pH pressure 1 . atm temperature 300 . K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference_1 _Saveframe_category chemical_shift_reference _Details . loop_ _Mol_common_name _Atom_type _Atom_isotope_number _Atom_group _Chem_shift_units _Chem_shift_value _Reference_method _Reference_type _External_reference_sample_geometry _External_reference_location _External_reference_axis _Indirect_shift_ratio DSS C 13 'methyl protons' ppm 0.00 . indirect . . . 0.251449530 DSS H 1 'methyl protons' ppm 0.00 internal direct . . . 1.000000000 DSS N 15 'methyl protons' ppm 0.00 . indirect . . . 0.101329118 stop_ save_ ################################### # Assigned chemical shift lists # ################################### ################################################################### # Chemical Shift Ambiguity Index Value Definitions # # # # The values other than 1 are used for those atoms with different # # chemical shifts that cannot be assigned to stereospecific atoms # # or to specific residues or chains. # # # # Index Value Definition # # # # 1 Unique (including isolated methyl protons, # # geminal atoms, and geminal methyl # # groups with identical chemical shifts) # # (e.g. ILE HD11, HD12, HD13 protons) # # 2 Ambiguity of geminal atoms or geminal methyl # # proton groups (e.g. ASP HB2 and HB3 # # protons, LEU CD1 and CD2 carbons, or # # LEU HD11, HD12, HD13 and HD21, HD22, # # HD23 methyl protons) # # 3 Aromatic atoms on opposite sides of # # symmetrical rings (e.g. TYR HE1 and HE2 # # protons) # # 4 Intraresidue ambiguities (e.g. LYS HG and # # HD protons or TRP HZ2 and HZ3 protons) # # 5 Interresidue ambiguities (LYS 12 vs. LYS 27) # # 6 Intermolecular ambiguities (e.g. ASP 31 CA # # in monomer 1 and ASP 31 CA in monomer 2 # # of an asymmetrical homodimer, duplex # # DNA assignments, or other assignments # # that may apply to atoms in one or more # # molecule in the molecular assembly) # # 9 Ambiguous, specific ambiguity not defined # # # ################################################################### save_assigned_chem_shift_list_1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Experiment_label '2D 1H-15N HSQC' '3D CBCA(CO)NH' stop_ loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $sample_conditions_1 _Chem_shift_reference_set_label $chemical_shift_reference_1 _Mol_system_component_name TolAIII _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 43 43 ASN CA C 54.826 . 1 2 43 43 ASN CB C 41.001 . 1 3 44 44 ASN H H 8.256 . 1 4 44 44 ASN N N 113.804 . 1 5 49 49 ALA CB C 18.617 . 1 6 50 50 ASP H H 8.073 . 1 7 50 50 ASP CA C 57.081 . 1 8 50 50 ASP CB C 40.432 . 1 9 50 50 ASP N N 119.224 . 1 10 51 51 ILE H H 8.150 . 1 11 51 51 ILE CA C 65.404 . 1 12 51 51 ILE CB C 38.315 . 1 13 51 51 ILE N N 121.637 . 1 14 52 52 ASN H H 8.433 . 1 15 52 52 ASN CA C 56.278 . 1 16 52 52 ASN CB C 38.330 . 1 17 52 52 ASN N N 118.269 . 1 18 53 53 ASN H H 8.725 . 1 19 53 53 ASN CA C 56.167 . 1 20 53 53 ASN CB C 38.378 . 1 21 53 53 ASN N N 119.413 . 1 22 54 54 TYR H H 8.098 . 1 23 54 54 TYR CA C 61.367 . 1 24 54 54 TYR CB C 37.970 . 1 25 54 54 TYR N N 121.993 . 1 26 55 55 ALA H H 8.565 . 1 27 55 55 ALA CA C 55.723 . 1 28 55 55 ALA CB C 18.100 . 1 29 55 55 ALA N N 121.231 . 1 30 56 56 GLY H H 7.908 . 1 31 56 56 GLY CA C 47.147 . 1 32 56 56 GLY N N 103.515 . 1 33 57 57 GLN H H 7.794 . 1 34 57 57 GLN CA C 59.173 . 1 35 57 57 GLN CB C 28.815 . 1 36 57 57 GLN N N 122.930 . 1 37 58 58 ILE H H 8.051 . 1 38 58 58 ILE CA C 66.369 . 1 39 58 58 ILE CB C 37.789 . 1 40 58 58 ILE N N 121.397 . 1 41 59 59 LYS H H 8.154 . 1 42 59 59 LYS CA C 61.290 . 1 43 59 59 LYS CB C 32.244 . 1 44 59 59 LYS N N 118.623 . 1 45 60 60 SER H H 8.438 . 1 46 60 60 SER CA C 61.833 . 1 47 60 60 SER CB C 63.059 . 1 48 60 60 SER N N 113.643 . 1 49 61 61 ALA H H 7.863 . 1 50 61 61 ALA CA C 55.339 . 1 51 61 61 ALA CB C 18.275 . 1 52 61 61 ALA N N 125.108 . 1 53 62 62 ILE H H 7.919 . 1 54 62 62 ILE CA C 66.145 . 1 55 62 62 ILE CB C 38.271 . 1 56 62 62 ILE N N 118.678 . 1 57 63 63 GLU H H 8.979 . 1 58 63 63 GLU CA C 60.246 . 1 59 63 63 GLU CB C 29.948 . 1 60 63 63 GLU N N 119.012 . 1 61 64 64 SER H H 7.988 . 1 62 64 64 SER CA C 61.679 . 1 63 64 64 SER CB C 63.415 . 1 64 64 64 SER N N 113.105 . 1 65 65 65 LYS H H 7.355 . 1 66 65 65 LYS CA C 53.111 . 1 67 65 65 LYS CB C 32.334 . 1 68 65 65 LYS N N 117.978 . 1 69 66 66 PHE H H 7.716 . 1 70 66 66 PHE CA C 55.356 . 1 71 66 66 PHE CB C 38.672 . 1 72 66 66 PHE N N 122.737 . 1 73 67 67 TYR H H 7.996 . 1 74 67 67 TYR CA C 59.665 . 1 75 67 67 TYR CB C 38.143 . 1 76 67 67 TYR N N 123.654 . 1 77 68 68 ASP H H 8.564 . 1 78 68 68 ASP CB C 39.743 . 1 79 68 68 ASP N N 118.579 . 1 80 69 69 ALA H H 7.950 . 1 81 69 69 ALA CA C 55.862 . 1 82 69 69 ALA CB C 18.202 . 1 83 69 69 ALA N N 123.996 . 1 84 70 70 SER H H 8.455 . 1 85 70 70 SER CA C 61.260 . 1 86 70 70 SER CB C 62.648 . 1 87 70 70 SER N N 110.998 . 1 88 71 71 SER H H 7.884 . 1 89 71 71 SER CA C 60.805 . 1 90 71 71 SER CB C 62.807 . 1 91 71 71 SER N N 118.288 . 1 92 72 72 TYR H H 7.881 . 1 93 72 72 TYR CA C 56.949 . 1 94 72 72 TYR CB C 40.023 . 1 95 72 72 TYR N N 119.275 . 1 96 73 73 ALA H H 6.999 . 1 97 73 73 ALA CA C 54.227 . 1 98 73 73 ALA CB C 18.562 . 1 99 73 73 ALA N N 121.442 . 1 100 74 74 GLY H H 8.789 . 1 101 74 74 GLY CA C 45.507 . 1 102 74 74 GLY N N 112.396 . 1 103 75 75 LYS H H 8.117 . 1 104 75 75 LYS CA C 54.831 . 1 105 75 75 LYS CB C 34.855 . 1 106 75 75 LYS N N 120.707 . 1 107 76 76 THR H H 8.335 . 1 108 76 76 THR CA C 60.960 . 1 109 76 76 THR CB C 72.058 . 1 110 76 76 THR N N 111.385 . 1 111 77 77 CYS H H 8.618 . 1 112 77 77 CYS CA C 57.029 . 1 113 77 77 CYS CB C 49.067 . 1 114 77 77 CYS N N 121.221 . 1 115 78 78 THR H H 9.021 . 1 116 78 78 THR CA C 62.653 . 1 117 78 78 THR CB C 70.076 . 1 118 78 78 THR N N 128.758 . 1 119 79 79 LEU H H 9.315 . 1 120 79 79 LEU CA C 53.168 . 1 121 79 79 LEU CB C 44.812 . 1 122 79 79 LEU N N 127.835 . 1 123 80 80 ARG H H 9.254 . 1 124 80 80 ARG CA C 54.851 . 1 125 80 80 ARG CB C 30.218 . 1 126 80 80 ARG N N 123.155 . 1 127 81 81 ILE H H 6.425 . 1 128 81 81 ILE CA C 60.223 . 1 129 81 81 ILE CB C 41.571 . 1 130 81 81 ILE N N 126.539 . 1 131 82 82 LYS H H 8.011 . 1 132 82 82 LYS CA C 55.445 . 1 133 82 82 LYS CB C 35.381 . 1 134 82 82 LYS N N 121.903 . 1 135 83 83 LEU H H 8.310 . 1 136 83 83 LEU CA C 53.441 . 1 137 83 83 LEU CB C 46.055 . 1 138 83 83 LEU N N 124.409 . 1 139 84 84 ALA H H 9.175 . 1 140 84 84 ALA N N 126.471 . 1 141 85 85 PRO CA C 65.000 . 1 142 85 85 PRO CB C 31.303 . 1 143 86 86 ASP H H 7.598 . 1 144 86 86 ASP CA C 52.737 . 1 145 86 86 ASP CB C 40.147 . 1 146 86 86 ASP N N 111.908 . 1 147 87 87 GLY H H 8.535 . 1 148 87 87 GLY CA C 45.039 . 1 149 87 87 GLY N N 109.014 . 1 150 88 88 MET H H 7.506 . 1 151 88 88 MET CA C 56.731 . 1 152 88 88 MET CB C 32.768 . 1 153 88 88 MET N N 117.486 . 1 154 89 89 LEU H H 8.705 . 1 155 89 89 LEU CA C 55.505 . 1 156 89 89 LEU CB C 42.337 . 1 157 89 89 LEU N N 125.392 . 1 158 90 90 LEU H H 9.064 . 1 159 90 90 LEU CA C 56.067 . 1 160 90 90 LEU CB C 42.680 . 1 161 90 90 LEU N N 128.912 . 1 162 91 91 ASP H H 7.863 . 1 163 91 91 ASP CA C 53.942 . 1 164 91 91 ASP CB C 44.796 . 1 165 91 91 ASP N N 115.250 . 1 166 92 92 ILE H H 8.056 . 1 167 92 92 ILE CA C 59.902 . 1 168 92 92 ILE CB C 40.510 . 1 169 92 92 ILE N N 119.401 . 1 170 93 93 LYS H H 8.457 . 1 171 93 93 LYS N N 124.674 . 1 172 94 94 PRO CA C 62.901 . 1 173 94 94 PRO CB C 31.996 . 1 174 95 95 GLU H H 9.407 . 1 175 95 95 GLU CA C 56.397 . 1 176 95 95 GLU CB C 31.854 . 1 177 95 95 GLU N N 123.941 . 1 178 96 96 GLY H H 7.699 . 1 179 96 96 GLY CA C 45.312 . 1 180 96 96 GLY N N 107.036 . 1 181 97 97 GLY H H 8.346 . 1 182 97 97 GLY CA C 44.080 . 1 183 97 97 GLY N N 106.913 . 1 184 98 98 ASP H H 8.643 . 1 185 98 98 ASP N N 122.709 . 1 186 99 99 PRO CA C 66.094 . 1 187 99 99 PRO CB C 32.399 . 1 188 100 100 ALA H H 8.003 . 1 189 100 100 ALA CA C 55.473 . 1 190 100 100 ALA CB C 18.439 . 1 191 100 100 ALA N N 120.954 . 1 192 101 101 LEU H H 8.768 . 1 193 101 101 LEU CA C 57.635 . 1 194 101 101 LEU CB C 40.445 . 1 195 101 101 LEU N N 121.815 . 1 196 102 102 CYS H H 9.095 . 1 197 102 102 CYS CA C 56.242 . 1 198 102 102 CYS CB C 37.504 . 1 199 102 102 CYS N N 115.098 . 1 200 103 103 GLN H H 8.102 . 1 201 103 103 GLN CA C 59.148 . 1 202 103 103 GLN CB C 28.382 . 1 203 103 103 GLN N N 118.506 . 1 204 104 104 ALA H H 7.695 . 1 205 104 104 ALA CA C 54.728 . 1 206 104 104 ALA CB C 18.822 . 1 207 104 104 ALA N N 123.443 . 1 208 105 105 ALA H H 8.930 . 1 209 105 105 ALA CA C 54.559 . 1 210 105 105 ALA CB C 17.474 . 1 211 105 105 ALA N N 122.272 . 1 212 106 106 LEU H H 8.049 . 1 213 106 106 LEU CA C 58.702 . 1 214 106 106 LEU CB C 42.260 . 1 215 106 106 LEU N N 118.779 . 1 216 107 107 ALA H H 7.231 . 1 217 107 107 ALA CA C 54.900 . 1 218 107 107 ALA CB C 17.883 . 1 219 107 107 ALA N N 119.297 . 1 220 108 108 ALA H H 7.330 . 1 221 108 108 ALA CA C 54.671 . 1 222 108 108 ALA CB C 18.879 . 1 223 108 108 ALA N N 119.869 . 1 224 109 109 ALA H H 8.404 . 1 225 109 109 ALA CA C 55.237 . 1 226 109 109 ALA CB C 18.443 . 1 227 109 109 ALA N N 118.552 . 1 228 110 110 LYS H H 7.364 . 1 229 110 110 LYS CA C 58.710 . 1 230 110 110 LYS CB C 32.617 . 1 231 110 110 LYS N N 113.674 . 1 232 111 111 LEU H H 7.242 . 1 233 111 111 LEU CA C 54.502 . 1 234 111 111 LEU CB C 43.769 . 1 235 111 111 LEU N N 117.014 . 1 236 112 112 ALA H H 7.206 . 1 237 112 112 ALA CA C 52.318 . 1 238 112 112 ALA CB C 20.454 . 1 239 112 112 ALA N N 121.712 . 1 240 113 113 LYS H H 8.574 . 1 241 113 113 LYS CA C 54.547 . 1 242 113 113 LYS CB C 31.678 . 1 243 113 113 LYS N N 123.382 . 1 244 114 114 ILE H H 8.580 . 1 245 114 114 ILE N N 129.542 . 1 246 115 115 PRO CA C 62.135 . 1 247 115 115 PRO CB C 32.044 . 1 248 116 116 LYS H H 8.471 . 1 249 116 116 LYS N N 122.966 . 1 250 118 118 PRO CA C 63.902 . 1 251 118 118 PRO CB C 32.179 . 1 252 119 119 SER H H 6.874 . 1 253 119 119 SER N N 108.792 . 1 254 120 120 GLN CA C 56.931 . 1 255 120 120 GLN CB C 29.640 . 1 256 121 121 ALA H H 5.668 . 1 257 121 121 ALA CA C 55.170 . 1 258 121 121 ALA CB C 18.304 . 1 259 121 121 ALA N N 120.285 . 1 260 122 122 VAL H H 12.585 . 1 261 122 122 VAL CA C 66.357 . 1 262 122 122 VAL CB C 31.950 . 1 263 122 122 VAL N N 116.579 . 1 264 123 123 TYR H H 4.156 . 1 265 123 123 TYR CA C 61.675 . 1 266 123 123 TYR N N 121.283 . 1 267 124 124 GLU H H 8.220 . 1 268 124 124 GLU CA C 59.256 . 1 269 124 124 GLU CB C 29.256 . 1 270 124 124 GLU N N 114.658 . 1 271 125 125 VAL H H 7.064 . 1 272 125 125 VAL CA C 65.382 . 1 273 125 125 VAL CB C 32.050 . 1 274 125 125 VAL N N 116.438 . 1 275 126 126 PHE H H 7.575 . 1 276 126 126 PHE CA C 60.735 . 1 277 126 126 PHE CB C 39.625 . 1 278 126 126 PHE N N 116.128 . 1 279 127 127 LYS H H 7.543 . 1 280 127 127 LYS CA C 59.089 . 1 281 127 127 LYS CB C 31.590 . 1 282 127 127 LYS N N 117.760 . 1 283 128 128 ASN H H 7.392 . 1 284 128 128 ASN CA C 53.241 . 1 285 128 128 ASN N N 115.622 . 1 286 129 129 ALA H H 8.482 . 1 287 129 129 ALA N N 125.962 . 1 288 130 130 PRO CA C 61.246 . 1 289 130 130 PRO CB C 31.637 . 1 290 131 131 LEU H H 9.212 . 1 291 131 131 LEU CA C 54.250 . 1 292 131 131 LEU CB C 46.186 . 1 293 131 131 LEU N N 122.960 . 1 294 132 132 ASP H H 8.698 . 1 295 132 132 ASP CA C 53.985 . 1 296 132 132 ASP CB C 41.545 . 1 297 132 132 ASP N N 125.372 . 1 298 133 133 PHE H H 9.279 . 1 299 133 133 PHE N N 125.112 . 1 stop_ save_