data_18871 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Solution structure of a chaperone in type III secretion system ; _BMRB_accession_number 18871 _BMRB_flat_file_name bmr18871.str _Entry_type original _Submission_date 2012-12-03 _Accession_date 2012-12-03 _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 Chen Li . . 2 Economou Anastassios . . 3 Kalodimos 'Charalampos G.' . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 60 "13C chemical shifts" 203 "15N chemical shifts" 60 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2013-04-08 original author . stop_ _Original_release_date 2013-04-08 save_ ############################# # Citation for this entry # ############################# save_Citation_1 _Saveframe_category entry_citation _Citation_full . _Citation_title 'Substrate-Activated Conformational Switch on Chaperones Encodes a Targeting Signal in Type III Secretion' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 23523349 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Chen Li . . 2 Ai Xuanjun . . 3 Portaliou Athina . . 4 Minetti 'Conceicao A.S.A.' . . 5 Remeta 'David P.' . . 6 Economou Anastassios . . 7 Kalodimos 'Charalampos G.' . . stop_ _Journal_abbreviation 'Cell. Rep.' _Journal_volume 3 _Journal_issue 3 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 709 _Page_last 715 _Year 2013 _Details . save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name 'chaperone in type III secretion system' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'chaperone in type III secretion system, 1' $CesAB 'chaperone in type III secretion system, 2' $CesAB 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_CesAB _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common CesAB _Molecular_mass 12260.241 _Mol_thiol_state 'not present' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 107 _Mol_residue_sequence ; MSIVSQTRNKELLLKKIDSL IEAIKKIIAEFDVVKESVNE LSEKAKTDPQAAEKLNKLIE GYTYGEERKLYDSALSKIEK LIETLSPARSKSQSTMNQRN RNNRKIV ; loop_ _Residue_seq_code _Residue_label 1 MET 2 SER 3 ILE 4 VAL 5 SER 6 GLN 7 THR 8 ARG 9 ASN 10 LYS 11 GLU 12 LEU 13 LEU 14 LEU 15 LYS 16 LYS 17 ILE 18 ASP 19 SER 20 LEU 21 ILE 22 GLU 23 ALA 24 ILE 25 LYS 26 LYS 27 ILE 28 ILE 29 ALA 30 GLU 31 PHE 32 ASP 33 VAL 34 VAL 35 LYS 36 GLU 37 SER 38 VAL 39 ASN 40 GLU 41 LEU 42 SER 43 GLU 44 LYS 45 ALA 46 LYS 47 THR 48 ASP 49 PRO 50 GLN 51 ALA 52 ALA 53 GLU 54 LYS 55 LEU 56 ASN 57 LYS 58 LEU 59 ILE 60 GLU 61 GLY 62 TYR 63 THR 64 TYR 65 GLY 66 GLU 67 GLU 68 ARG 69 LYS 70 LEU 71 TYR 72 ASP 73 SER 74 ALA 75 LEU 76 SER 77 LYS 78 ILE 79 GLU 80 LYS 81 LEU 82 ILE 83 GLU 84 THR 85 LEU 86 SER 87 PRO 88 ALA 89 ARG 90 SER 91 LYS 92 SER 93 GLN 94 SER 95 THR 96 MET 97 ASN 98 GLN 99 ARG 100 ASN 101 ARG 102 ASN 103 ASN 104 ARG 105 LYS 106 ILE 107 VAL stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-04-07 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 17856 CesAB_(Type_III_secretion_system,_chaperone_for_EspA_and_EspB,_LEE_associated) 100.00 107 97.20 97.20 2.22e-63 PDB 2LHK "Structural Analysis Of A Chaperone In Type Iii Secretion System" 100.00 107 97.20 97.20 2.22e-63 PDB 2M1N "Solution Structure Of A Chaperone In Type Iii Secretion System" 100.00 107 100.00 100.00 2.96e-67 DBJ BAB38009 "hypothetical protein [Escherichia coli O157:H7 str. Sakai]" 100.00 107 97.20 97.20 2.22e-63 DBJ BAI37555 "T3SS component [Escherichia coli O111:H- str. 11128]" 100.00 107 97.20 97.20 2.22e-63 EMBL CAG17512 "hypothetical protein [Escherichia coli]" 100.00 107 97.20 97.20 2.22e-63 EMBL CAS11514 "component of T3SS [Escherichia coli O127:H6 str. E2348/69]" 100.00 107 97.20 97.20 2.22e-63 EMBL CAX18596 "Type III secretion system, chaperone for EspA and EspB, LEE associated [Escherichia coli]" 100.00 107 97.20 97.20 2.22e-63 EMBL CAX18671 "Type III secretion system, chaperone for EspA and EspB, LEE associated [Escherichia coli]" 100.00 107 97.20 97.20 2.22e-63 EMBL CAX18751 "Type III secretion system, chaperone for EspA and EspB, LEE associated [Escherichia coli]" 100.00 107 97.20 97.20 2.22e-63 GB AAC31531 "L0052 [Escherichia coli O157:H7 str. EDL933]" 100.00 107 97.20 97.20 2.22e-63 GB AAC38366 "Orf3 [Escherichia coli]" 100.00 107 97.20 97.20 2.22e-63 GB AAG58850 "hypothetical protein Z5138 [Escherichia coli O157:H7 str. EDL933]" 100.00 107 97.20 97.20 2.22e-63 GB ACG59648 "conserved hypothetical protein [Escherichia coli O157:H7]" 100.00 107 97.20 97.20 2.22e-63 GB ACG59706 "conserved hypothetical protein [Escherichia coli]" 100.00 107 97.20 97.20 2.22e-63 REF NP_312613 "hypothetical protein ECs4586 [Escherichia coli O157:H7 str. Sakai]" 100.00 107 97.20 97.20 2.22e-63 REF WP_000029559 "hypothetical protein [Escherichia coli]" 100.00 107 97.20 97.20 2.22e-63 REF WP_032306487 "hypothetical protein, partial [Escherichia coli]" 68.22 73 100.00 100.00 1.24e-42 REF WP_032310654 "hypothetical protein, partial [Escherichia coli]" 73.83 79 100.00 100.00 1.09e-47 REF WP_032316691 "hypothetical protein, partial [Escherichia coli]" 92.52 99 96.97 96.97 3.46e-57 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species _Details $CesAB 'E. coli' 562 Bacteria . Escherichia coli 'Enteropathogenic 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 $CesAB 'recombinant technology' . Escherichia coli . pETDuet-1 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 $CesAB 500 mM '[U-13C; U-15N; U-2H], 13CH3-Ala, Ile, Val, Leu' KPi 50 mM 'natural abundance' KCl 300 mM 'natural abundance' stop_ save_ ############################ # Computer software used # ############################ save_CNS _Saveframe_category software _Name CNS _Version . loop_ _Vendor _Address _Electronic_address 'Brunger, Adams, Clore, Gros, Nilges and Read' . . stop_ loop_ _Task 'structure solution' stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model Avance _Field_strength 700 _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_2D_1H-13C_HSQC_aliphatic_2 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-13C HSQC aliphatic' _Sample_label $sample_1 save_ save_3D_HNCO_3 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCO' _Sample_label $sample_1 save_ save_3D_HNCA_4 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCA' _Sample_label $sample_1 save_ save_3D_HNCACB_5 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCACB' _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_1H-15N_NOESY_7 _Saveframe_category NMR_applied_experiment _Experiment_name '3D 1H-15N NOESY' _Sample_label $sample_1 save_ save_3D_HMQC-NOESY-HMQC_8 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HMQC-NOESY-HMQC' _Sample_label $sample_1 save_ save_NMR_spectrometer_expt _Saveframe_category NMR_applied_experiment _Experiment_name . _BMRB_pulse_sequence_accession_number . _Details . 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' 0.3 . M pH 6.5 . pH pressure 1 . atm temperature 321 . 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 na indirect . . . 0.251449530 DSS H 1 'methyl protons' ppm 0.00 internal direct . . . 1.000000000 DSS N 15 'methyl protons' ppm 0.00 na 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' '2D 1H-13C HSQC aliphatic' '3D HNCO' '3D HNCA' '3D HNCACB' '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 'chaperone in type III secretion system, 1' _Text_data_format . _Text_data . loop_ _Atom_shift_assign_ID _Residue_author_seq_code _Residue_seq_code _Residue_label _Atom_name _Atom_type _Chem_shift_value _Chem_shift_value_error _Chem_shift_ambiguity_code 1 2 2 SER C C 175.116 . . 2 2 2 SER CA C 58.724 . . 3 2 2 SER CB C 63.35 . . 4 3 3 ILE H H 7.879 . . 5 3 3 ILE C C 177.161 . . 6 3 3 ILE CA C 63.327 . . 7 3 3 ILE CB C 37.515 . . 8 3 3 ILE N N 121.831 . . 9 4 4 VAL H H 7.865 . . 10 4 4 VAL CA C 63.551 . . 11 4 4 VAL CB C 31.312 . . 12 4 4 VAL N N 121.833 . . 13 9 9 ASN C C 176.669 . . 14 9 9 ASN CA C 54.393 . . 15 10 10 LYS H H 8.283 . . 16 10 10 LYS C C 178.083 . . 17 10 10 LYS CA C 59.382 . . 18 10 10 LYS CB C 30.722 . . 19 10 10 LYS N N 120.745 . . 20 11 11 GLU H H 8.194 . . 21 11 11 GLU C C 178.993 . . 22 11 11 GLU CA C 59.182 . . 23 11 11 GLU CB C 28.648 . . 24 11 11 GLU N N 118.409 . . 25 12 12 LEU H H 7.911 . . 26 12 12 LEU CA C 57.650 . . 27 12 12 LEU CB C 40.880 . . 28 12 12 LEU N N 119.122 . . 29 13 13 LEU C C 178.370 . . 30 13 13 LEU CA C 57.221 . . 31 13 13 LEU CB C 41.098 . . 32 14 14 LEU H H 8.182 . . 33 14 14 LEU C C 178.800 . . 34 14 14 LEU CA C 58.142 . . 35 14 14 LEU CB C 39.913 . . 36 14 14 LEU N N 117.947 . . 37 15 15 LYS H H 8.016 . . 38 15 15 LYS C C 178.890 . . 39 15 15 LYS CA C 59.034 . . 40 15 15 LYS CB C 31.015 . . 41 15 15 LYS N N 117.826 . . 42 16 16 LYS H H 7.743 . . 43 16 16 LYS CA C 58.395 . . 44 16 16 LYS N N 119.743 . . 45 17 17 ILE H H 8.197 . . 46 17 17 ILE C C 177.354 . . 47 17 17 ILE CA C 65.323 . . 48 17 17 ILE CB C 36.470 . . 49 17 17 ILE N N 120.972 . . 50 18 18 ASP H H 8.528 . . 51 18 18 ASP C C 179.507 . . 52 18 18 ASP CA C 57.800 . . 53 18 18 ASP CB C 39.368 . . 54 18 18 ASP N N 120.128 . . 55 19 19 SER H H 8.034 . . 56 19 19 SER C C 176.851 . . 57 19 19 SER CA C 61.650 . . 58 19 19 SER N N 115.707 . . 59 20 20 LEU H H 7.673 . . 60 20 20 LEU C C 179.036 . . 61 20 20 LEU CA C 57.250 . . 62 20 20 LEU CB C 39.828 . . 63 20 20 LEU N N 124.274 . . 64 21 21 ILE H H 8.234 . . 65 21 21 ILE CA C 65.880 . . 66 21 21 ILE CB C 37.130 . . 67 21 21 ILE N N 119.928 . . 68 22 22 GLU C C 176.187 . . 69 22 22 GLU CA C 59.220 . . 70 22 22 GLU CB C 28.710 . . 71 23 23 ALA H H 7.552 . . 72 23 23 ALA CA C 54.776 . . 73 23 23 ALA CB C 17.269 . . 74 23 23 ALA N N 120.687 . . 75 24 24 ILE C C 178.800 . . 76 24 24 ILE CA C 64.460 . . 77 24 24 ILE CB C 36.228 . . 78 25 25 LYS H H 8.624 . . 79 25 25 LYS C C 178.897 . . 80 25 25 LYS CA C 60.480 . . 81 25 25 LYS CB C 31.340 . . 82 25 25 LYS N N 120.633 . . 83 26 26 LYS H H 7.744 . . 84 26 26 LYS CA C 59.290 . . 85 26 26 LYS CB C 31.410 . . 86 26 26 LYS N N 119.711 . . 87 28 28 ILE C C 177.780 . . 88 28 28 ILE CA C 66.300 . . 89 28 28 ILE CB C 36.820 . . 90 29 29 ALA H H 7.549 . . 91 29 29 ALA C C 181.050 . . 92 29 29 ALA CA C 54.758 . . 93 29 29 ALA CB C 17.138 . . 94 29 29 ALA N N 120.160 . . 95 30 30 GLU H H 7.949 . . 96 30 30 GLU C C 179.960 . . 97 30 30 GLU CA C 58.376 . . 98 30 30 GLU CB C 28.056 . . 99 30 30 GLU N N 118.889 . . 100 31 31 PHE H H 8.446 . . 101 31 31 PHE C C 180.110 . . 102 31 31 PHE CA C 58.42 . . 103 31 31 PHE CB C 31.42 . . 104 31 31 PHE N N 118.579 . . 105 32 32 ASP H H 8.145 . . 106 32 32 ASP C C 179.529 . . 107 32 32 ASP CA C 58.110 . . 108 32 32 ASP CB C 39.697 . . 109 32 32 ASP N N 120.756 . . 110 33 33 VAL H H 7.382 . . 111 33 33 VAL CA C 65.870 . . 112 33 33 VAL CB C 30.620 . . 113 33 33 VAL N N 120.860 . . 114 34 34 VAL C C 178.790 . . 115 34 34 VAL CA C 66.630 . . 116 34 34 VAL CB C 30.700 . . 117 35 35 LYS H H 8.503 . . 118 35 35 LYS C C 178.650 . . 119 35 35 LYS CA C 61.270 . . 120 35 35 LYS CB C 31.029 . . 121 35 35 LYS N N 118.960 . . 122 36 36 GLU H H 7.635 . . 123 36 36 GLU C C 179.507 . . 124 36 36 GLU CA C 59.297 . . 125 36 36 GLU CB C 28.319 . . 126 36 36 GLU N N 118.266 . . 127 37 37 SER H H 8.315 . . 128 37 37 SER C C 177.020 . . 129 37 37 SER CA C 61.270 . . 130 37 37 SER CB C 62.454 . . 131 37 37 SER N N 116.774 . . 132 38 38 VAL H H 8.513 . . 133 38 38 VAL C C 178.115 . . 134 38 38 VAL CA C 66.460 . . 135 38 38 VAL CB C 30.358 . . 136 38 38 VAL N N 122.756 . . 137 39 39 ASN H H 8.074 . . 138 39 39 ASN CA C 56.730 . . 139 39 39 ASN CB C 37.790 . . 140 39 39 ASN N N 119.801 . . 141 41 41 LEU C C 178.720 . . 142 41 41 LEU CA C 57.747 . . 143 41 41 LEU CB C 41.620 . . 144 42 42 SER H H 8.288 . . 145 42 42 SER CA C 61.270 . . 146 42 42 SER CB C 62.388 . . 147 42 42 SER N N 112.233 . . 148 43 43 GLU C C 178.560 . . 149 43 43 GLU CA C 58.076 . . 150 43 43 GLU CB C 28.790 . . 151 44 44 LYS H H 8.146 . . 152 44 44 LYS C C 178.560 . . 153 44 44 LYS CA C 58.405 . . 154 44 44 LYS CB C 31.819 . . 155 44 44 LYS N N 120.772 . . 156 45 45 ALA H H 8.461 . . 157 45 45 ALA C C 177.160 . . 158 45 45 ALA CA C 53.536 . . 159 45 45 ALA CB C 17.604 . . 160 45 45 ALA N N 119.546 . . 161 46 46 LYS H H 7.254 . . 162 46 46 LYS C C 177.940 . . 163 46 46 LYS CA C 59.064 . . 164 46 46 LYS CB C 32.214 . . 165 46 46 LYS N N 115.143 . . 166 47 47 THR H H 7.385 . . 167 47 47 THR C C 173.800 . . 168 47 47 THR CA C 61.038 . . 169 47 47 THR CB C 70.514 . . 170 47 47 THR N N 103.581 . . 171 48 48 ASP H H 8.008 . . 172 48 48 ASP CA C 50.418 . . 173 48 48 ASP CB C 42.328 . . 174 48 48 ASP N N 122.666 . . 175 49 49 PRO C C 179.640 . . 176 49 49 PRO CA C 64.197 . . 177 49 49 PRO CB C 31.621 . . 178 50 50 GLN H H 8.305 . . 179 50 50 GLN C C 179.180 . . 180 50 50 GLN CA C 58.537 . . 181 50 50 GLN CB C 27.476 . . 182 50 50 GLN N N 118.077 . . 183 51 51 ALA H H 7.550 . . 184 51 51 ALA CA C 54.391 . . 185 51 51 ALA CB C 17.209 . . 186 51 51 ALA N N 123.795 . . 187 52 52 ALA H H 7.691 . . 188 52 52 ALA C C 179.710 . . 189 52 52 ALA CA C 55.181 . . 190 52 52 ALA CB C 17.144 . . 191 52 52 ALA N N 119.621 . . 192 53 53 GLU H H 7.900 . . 193 53 53 GLU CA C 59.099 . . 194 53 53 GLU CB C 28.648 . . 195 53 53 GLU N N 118.436 . . 196 56 56 ASN C C 177.900 . . 197 56 56 ASN CA C 56.430 . . 198 56 56 ASN CB C 37.807 . . 199 57 57 LYS H H 8.211 . . 200 57 57 LYS C C 176.070 . . 201 57 57 LYS CA C 58.669 . . 202 57 57 LYS CB C 36.161 . . 203 57 57 LYS N N 119.673 . . 204 58 58 LEU H H 8.039 . . 205 58 58 LEU C C 178.800 . . 206 58 58 LEU CA C 58.170 . . 207 58 58 LEU CB C 42.060 . . 208 58 58 LEU N N 122.397 . . 209 59 59 ILE H H 8.181 . . 210 59 59 ILE CA C 65.740 . . 211 59 59 ILE CB C 37.000 . . 212 59 59 ILE N N 118.483 . . 213 60 60 GLU H H 8.255 . . 214 60 60 GLU C C 179.640 . . 215 60 60 GLU CA C 59.720 . . 216 60 60 GLU CB C 28.920 . . 217 60 60 GLU N N 121.209 . . 218 61 61 GLY H H 8.532 . . 219 61 61 GLY CA C 48.050 . . 220 61 61 GLY N N 109.751 . . 221 62 62 TYR H H 8.153 . . 222 62 62 TYR C C 175.430 . . 223 62 62 TYR CA C 61.560 . . 224 62 62 TYR CB C 37.810 . . 225 62 62 TYR N N 116.869 . . 226 63 63 THR H H 7.701 . . 227 63 63 THR C C 174.950 . . 228 63 63 THR CA C 64.850 . . 229 63 63 THR CB C 68.770 . . 230 63 63 THR N N 114.262 . . 231 64 64 TYR H H 8.111 . . 232 64 64 TYR C C 175.670 . . 233 64 64 TYR CA C 57.155 . . 234 64 64 TYR CB C 39.320 . . 235 64 64 TYR N N 116.321 . . 236 65 65 GLY H H 7.732 . . 237 65 65 GLY C C 174.440 . . 238 65 65 GLY CA C 44.760 . . 239 65 65 GLY N N 110.079 . . 240 66 66 GLU H H 8.646 . . 241 66 66 GLU N N 121.587 . . 242 68 68 ARG C C 179.340 . . 243 68 68 ARG CA C 59.800 . . 244 68 68 ARG CB C 28.594 . . 245 69 69 LYS H H 7.692 . . 246 69 69 LYS CA C 58.040 . . 247 69 69 LYS CB C 30.818 . . 248 69 69 LYS N N 118.590 . . 249 72 72 ASP C C 179.930 . . 250 72 72 ASP CA C 57.089 . . 251 72 72 ASP CB C 39.650 . . 252 73 73 SER H H 8.091 . . 253 73 73 SER C C 177.130 . . 254 73 73 SER CA C 61.001 . . 255 73 73 SER CB C 62.783 . . 256 73 73 SER N N 115.050 . . 257 74 74 ALA H H 8.338 . . 258 74 74 ALA CA C 55.285 . . 259 74 74 ALA CB C 16.743 . . 260 74 74 ALA N N 122.962 . . 261 75 75 LEU C C 179.350 . . 262 75 75 LEU CA C 58.076 . . 263 75 75 LEU CB C 39.847 . . 264 76 76 SER H H 7.978 . . 265 76 76 SER CA C 61.073 . . 266 76 76 SER CB C 62.322 . . 267 76 76 SER N N 113.256 . . 268 77 77 LYS C C 179.000 . . 269 77 77 LYS CA C 58.210 . . 270 77 77 LYS CB C 31.230 . . 271 78 78 ILE H H 8.215 . . 272 78 78 ILE C C 179.980 . . 273 78 78 ILE CA C 65.936 . . 274 78 78 ILE CB C 37.350 . . 275 78 78 ILE N N 119.678 . . 276 79 79 GLU H H 8.196 . . 277 79 79 GLU C C 180.107 . . 278 79 79 GLU CA C 59.195 . . 279 79 79 GLU CB C 28.714 . . 280 79 79 GLU N N 118.412 . . 281 80 80 LYS H H 7.743 . . 282 80 80 LYS C C 179.000 . . 283 80 80 LYS CA C 59.195 . . 284 80 80 LYS CB C 31.424 . . 285 80 80 LYS N N 119.743 . . 286 81 81 LEU H H 8.196 . . 287 81 81 LEU C C 179.110 . . 288 81 81 LEU CA C 58.113 . . 289 81 81 LEU CB C 40.550 . . 290 81 81 LEU N N 119.713 . . 291 82 82 ILE H H 8.345 . . 292 82 82 ILE C C 178.100 . . 293 82 82 ILE CA C 65.810 . . 294 82 82 ILE CB C 36.672 . . 295 82 82 ILE N N 119.985 . . 296 83 83 GLU H H 7.764 . . 297 83 83 GLU CA C 59.100 . . 298 83 83 GLU CB C 28.780 . . 299 83 83 GLU N N 118.503 . . 300 87 87 PRO C C 177.200 . . 301 87 87 PRO CA C 63.800 . . 302 87 87 PRO CB C 31.230 . . 303 88 88 ALA H H 8.054 . . 304 88 88 ALA C C 179.750 . . 305 88 88 ALA CA C 52.588 . . 306 88 88 ALA CB C 18.124 . . 307 88 88 ALA N N 120.979 . . 308 89 89 ARG H H 7.903 . . 309 89 89 ARG CA C 55.810 . . 310 89 89 ARG CB C 29.042 . . 311 89 89 ARG N N 118.479 . . 312 105 105 LYS C C 176.040 . . 313 105 105 LYS CA C 56.102 . . 314 105 105 LYS CB C 31.950 . . 315 106 106 ILE H H 8.066 . . 316 106 106 ILE C C 175.260 . . 317 106 106 ILE CA C 61.169 . . 318 106 106 ILE CB C 37.807 . . 319 106 106 ILE N N 123.032 . . 320 107 107 VAL H H 7.530 . . 321 107 107 VAL CA C 63.177 . . 322 107 107 VAL CB C 32.462 . . 323 107 107 VAL N N 127.461 . . stop_ save_