data_25745 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Structure of the N-terminal domain of the metalloprotease PrtV from Vibrio cholerae ; _BMRB_accession_number 25745 _BMRB_flat_file_name bmr25745.str _Entry_type original _Submission_date 2015-08-07 _Accession_date 2015-08-07 _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 Persson Cecilia . . 2 Mayzel M. . . 3 Edwin A. . . 4 Wai S. N. . 5 Ohman A. . . 6 Sauer-eriksson A. E. . 7 Karlsson G. . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 449 "13C chemical shifts" 357 "15N chemical shifts" 79 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2016-10-20 update BMRB 'update entry citation' 2015-08-24 original author 'original release' stop_ _Original_release_date 2015-08-24 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; Structure of the N-terminal domain of the metalloprotease PrtV from Vibrio cholerae ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 26434928 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Edwin A. . . 2 Mayzel M. . . 3 Persson Cecilia . . 4 Wai S. N. . 5 Ohman A. . . 6 Karlsson G. . . 7 Sauer-eriksson A. E. . stop_ _Journal_abbreviation 'Protein Sci.' _Journal_volume 24 _Journal_issue 12 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 2076 _Page_last 2080 _Year 2015 _Details . save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name 'N-terminal domain of the metalloprotease PrtV from Vibrio cholerae' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label METALLOPROTEASE $METALLOPROTEASE stop_ _System_molecular_weight 9348.8769 _System_physical_state native _System_oligomer_state ? _System_paramagnetic no _System_thiol_state 'not present' _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_METALLOPROTEASE _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common METALLOPROTEASE _Molecular_mass 9348.8769 _Mol_thiol_state 'not present' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 84 _Mol_residue_sequence ; GAMAQTPIDLGVVNEDKLIE MLVRTGQIPADASDVDKRIA LERYLEEKIRSGFKGDAQFG KKALEQRAKILKVIDKQKGP HKAR ; loop_ _Residue_seq_code _Residue_label 1 GLY 2 ALA 3 MET 4 ALA 5 GLN 6 THR 7 PRO 8 ILE 9 ASP 10 LEU 11 GLY 12 VAL 13 VAL 14 ASN 15 GLU 16 ASP 17 LYS 18 LEU 19 ILE 20 GLU 21 MET 22 LEU 23 VAL 24 ARG 25 THR 26 GLY 27 GLN 28 ILE 29 PRO 30 ALA 31 ASP 32 ALA 33 SER 34 ASP 35 VAL 36 ASP 37 LYS 38 ARG 39 ILE 40 ALA 41 LEU 42 GLU 43 ARG 44 TYR 45 LEU 46 GLU 47 GLU 48 LYS 49 ILE 50 ARG 51 SER 52 GLY 53 PHE 54 LYS 55 GLY 56 ASP 57 ALA 58 GLN 59 PHE 60 GLY 61 LYS 62 LYS 63 ALA 64 LEU 65 GLU 66 GLN 67 ARG 68 ALA 69 LYS 70 ILE 71 LEU 72 LYS 73 VAL 74 ILE 75 ASP 76 LYS 77 GLN 78 LYS 79 GLY 80 PRO 81 HIS 82 LYS 83 ALA 84 ARG stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date . save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $METALLOPROTEASE 'Vibrio cholerae' 666 Bacteria . Vibrio cholerae 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 $METALLOPROTEASE 'recombinant technology' 'Escherichia coli' Escherichia coli BL21(DE3) pET1a-TrxA stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Saveframe_category sample _Sample_type solution _Details '0.7 mM PrtV' loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $METALLOPROTEASE 0.7 mM '[U-13C; U-15N]' Pi 20 mM 'natural abundance' stop_ save_ ############################ # Computer software used # ############################ save_AutoDep _Saveframe_category software _Name AutoDep _Version 4.3 loop_ _Vendor _Address _Electronic_address PDBe . . stop_ loop_ _Task 'chemical shift assignment' stop_ _Details . save_ save_ccpn _Saveframe_category software _Name ccpn _Version any loop_ _Vendor _Address _Electronic_address CCPN . . stop_ loop_ _Task 'chemical shift assignment' stop_ _Details . save_ save_x-plor _Saveframe_category software _Name x-plor _Version any loop_ _Vendor _Address _Electronic_address Brunger . . stop_ loop_ _Task 'chemical shift assignment' stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_Bruker_Avance-800 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model Avance _Field_strength 800 _Details . save_ ############################# # NMR applied experiments # ############################# save_Backbone_exps_1 _Saveframe_category NMR_applied_experiment _Experiment_name 'Backbone exps' _Sample_label $sample_1 save_ save_NOE_exps_2 _Saveframe_category NMR_applied_experiment _Experiment_name 'NOE exps' _Sample_label $sample_1 save_ ####################### # Sample conditions # ####################### save_sample_conditions_1 _Saveframe_category sample_conditions _Details 'pH [7.0], temp [283], pressure [0.0], ionStrength [0.0]' loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 7.000 . pH pressure 1 . atm temperature 283.000 . 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 H 1 'methyl protons' ppm 0.0 external indirect . . . 1 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 _Saveframe_category assigned_chemical_shifts _Details 'Origin nmrStar file /ebi/msd/pdb_root/Processing/prepare/5abk/ebi/prtv.star.csh' loop_ _Software_label $x-plor stop_ loop_ _Experiment_label 'Backbone exps' 'NOE exps' 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 METALLOPROTEASE _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 ALA HA H 4.119 . 1 2 2 2 ALA HB H 1.169 . 1 3 2 2 ALA C C 175.076 . 1 4 2 2 ALA CA C 49.743 . 1 5 2 2 ALA CB C 16.523 . 1 6 3 3 MET H H 8.359 0.001 1 7 3 3 MET HA H 4.232 0.004 1 8 3 3 MET HB2 H 1.786 0.009 2 9 3 3 MET HB3 H 1.851 0.003 2 10 3 3 MET HG2 H 2.352 . 2 11 3 3 MET HG3 H 2.410 . 2 12 3 3 MET C C 173.209 . 1 13 3 3 MET CA C 52.456 0.039 1 14 3 3 MET CB C 29.939 0.001 1 15 3 3 MET CG C 29.037 . 1 16 3 3 MET N N 120.053 0.015 1 17 4 4 ALA H H 8.251 0.006 1 18 4 4 ALA HA H 4.076 0.002 1 19 4 4 ALA HB H 1.169 0.007 1 20 4 4 ALA C C 174.690 . 1 21 4 4 ALA CA C 49.616 0.024 1 22 4 4 ALA CB C 16.389 0.009 1 23 4 4 ALA N N 125.817 0.013 1 24 5 5 GLN H H 8.274 0.002 1 25 5 5 GLN HA H 4.157 0.004 1 26 5 5 GLN HB2 H 1.742 0.002 2 27 5 5 GLN HB3 H 1.867 0.006 2 28 5 5 GLN HG2 H 2.140 . 1 29 5 5 GLN C C 173.064 . 1 30 5 5 GLN CA C 52.647 0.049 1 31 5 5 GLN CB C 26.852 0.019 1 32 5 5 GLN CG C 30.964 0.021 1 33 5 5 GLN N N 119.839 0.019 1 34 6 6 THR H H 8.181 0.005 1 35 6 6 THR HA H 4.348 0.001 1 36 6 6 THR HB H 3.931 0.004 1 37 6 6 THR HG2 H 1.039 0.002 1 38 6 6 THR C C 169.911 . 1 39 6 6 THR CA C 57.258 0.074 1 40 6 6 THR CB C 66.793 0.019 1 41 6 6 THR CG2 C 18.694 0.021 1 42 6 6 THR N N 118.689 0.019 1 43 7 7 PRO HA H 4.212 0.001 1 44 7 7 PRO HB2 H 2.080 0.002 2 45 7 7 PRO HB3 H 1.666 0.003 2 46 7 7 PRO HG2 H 1.768 0.002 2 47 7 7 PRO HG3 H 1.830 0.001 2 48 7 7 PRO HD2 H 3.666 0.003 2 49 7 7 PRO HD3 H 3.485 0.002 2 50 7 7 PRO C C 174.097 . 1 51 7 7 PRO CA C 60.421 0.018 1 52 7 7 PRO CB C 29.323 0.013 1 53 7 7 PRO CG C 24.664 0.019 1 54 7 7 PRO CD C 48.271 0.022 1 55 8 8 ILE H H 8.070 0.002 1 56 8 8 ILE HA H 3.851 0.002 1 57 8 8 ILE HB H 1.584 0.003 1 58 8 8 ILE HG12 H 0.959 0.003 2 59 8 8 ILE HG13 H 1.267 0.004 2 60 8 8 ILE HG2 H 0.654 . 1 61 8 8 ILE HD1 H 0.639 0.01 1 62 8 8 ILE C C 172.844 . 1 63 8 8 ILE CA C 58.473 0.033 1 64 8 8 ILE CB C 36.029 0.005 1 65 8 8 ILE CG1 C 24.665 0.015 1 66 8 8 ILE CG2 C 14.671 0.027 1 67 8 8 ILE CD1 C 10.184 0.033 1 68 8 8 ILE N N 121.072 0.006 1 69 9 9 ASP H H 8.188 0.002 1 70 9 9 ASP HA H 4.416 0.001 1 71 9 9 ASP HB2 H 2.545 0.003 2 72 9 9 ASP HB3 H 2.376 0.005 2 73 9 9 ASP C C 173.471 . 1 74 9 9 ASP CA C 50.956 0.034 1 75 9 9 ASP CB C 38.335 0.025 1 76 9 9 ASP N N 124.397 0.005 1 77 10 10 LEU H H 8.301 0.002 1 78 10 10 LEU HA H 4.043 0.005 1 79 10 10 LEU HB2 H 1.461 0.001 2 80 10 10 LEU HB3 H 1.395 0.004 2 81 10 10 LEU HG H 1.451 0.002 1 82 10 10 LEU HD1 H 0.691 0.002 2 83 10 10 LEU HD2 H 0.617 0.002 2 84 10 10 LEU C C 175.196 . 1 85 10 10 LEU CA C 52.756 0.034 1 86 10 10 LEU CB C 39.238 0.017 1 87 10 10 LEU CG C 24.182 0.039 1 88 10 10 LEU CD1 C 22.316 0.099 2 89 10 10 LEU CD2 C 20.387 0.011 2 90 10 10 LEU N N 123.979 0.011 1 91 11 11 GLY H H 8.320 0.009 1 92 11 11 GLY HA2 H 3.704 . 1 93 11 11 GLY C C 171.483 . 1 94 11 11 GLY CA C 42.718 0.02 1 95 11 11 GLY N N 108.391 0.014 1 96 12 12 VAL H H 7.692 0.002 1 97 12 12 VAL HA H 3.889 0.001 1 98 12 12 VAL HB H 1.873 0.008 1 99 12 12 VAL HG1 H 0.717 0.005 2 100 12 12 VAL HG2 H 0.700 0.007 2 101 12 12 VAL C C 173.536 . 1 102 12 12 VAL CA C 59.751 0.003 1 103 12 12 VAL CB C 29.737 0.026 1 104 12 12 VAL CG1 C 17.915 0.021 2 105 12 12 VAL CG2 C 18.367 0.022 2 106 12 12 VAL N N 119.210 0.023 1 107 13 13 VAL H H 8.022 0.002 1 108 13 13 VAL HA H 3.833 0.006 1 109 13 13 VAL HB H 1.850 0.003 1 110 13 13 VAL HG1 H 0.724 0.011 2 111 13 13 VAL HG2 H 0.704 0.011 2 112 13 13 VAL C C 172.859 . 1 113 13 13 VAL CA C 59.908 . 1 114 13 13 VAL CB C 29.793 . 1 115 13 13 VAL CG1 C 18.283 . 1 116 13 13 VAL CG2 C 18.283 . 1 117 13 13 VAL N N 123.239 0.014 1 118 14 14 ASN H H 8.175 0.004 1 119 14 14 ASN HA H 4.495 0.005 1 120 14 14 ASN HB2 H 2.695 0.006 2 121 14 14 ASN HB3 H 2.610 0.003 2 122 14 14 ASN C C 172.873 . 1 123 14 14 ASN CA C 50.249 . 1 124 14 14 ASN CB C 35.751 0.028 1 125 14 14 ASN N N 122.101 0.019 1 126 15 15 GLU H H 8.555 0.005 1 127 15 15 GLU HA H 3.595 0.003 1 128 15 15 GLU HB2 H 1.858 0.002 2 129 15 15 GLU HB3 H 1.768 0.003 2 130 15 15 GLU HG2 H 2.157 0.005 2 131 15 15 GLU HG3 H 1.958 0.002 2 132 15 15 GLU C C 174.460 . 1 133 15 15 GLU CA C 57.400 0.055 1 134 15 15 GLU CB C 26.876 0.036 1 135 15 15 GLU CG C 34.185 0.024 1 136 15 15 GLU N N 122.909 0.015 1 137 16 16 ASP H H 8.110 0.002 1 138 16 16 ASP HA H 4.139 0.003 1 139 16 16 ASP HB2 H 2.473 0.025 2 140 16 16 ASP HB3 H 2.507 . 2 141 16 16 ASP C C 176.422 . 1 142 16 16 ASP CA C 54.583 0.04 1 143 16 16 ASP CB C 37.077 . 1 144 16 16 ASP N N 117.900 0.008 1 145 17 17 LYS H H 7.698 0.003 1 146 17 17 LYS HA H 3.884 0.003 1 147 17 17 LYS HB2 H 1.651 0.007 2 148 17 17 LYS HB3 H 1.628 0.006 2 149 17 17 LYS HG2 H 1.347 0.002 2 150 17 17 LYS HG3 H 1.212 0.002 2 151 17 17 LYS HD2 H 1.464 . 1 152 17 17 LYS C C 176.851 . 1 153 17 17 LYS CA C 55.484 0.001 1 154 17 17 LYS CB C 29.430 . 1 155 17 17 LYS CG C 22.257 0.012 1 156 17 17 LYS CD C 25.873 . 1 157 17 17 LYS CE C 39.274 . 1 158 17 17 LYS N N 120.238 0.01 1 159 18 18 LEU H H 7.805 0.003 1 160 18 18 LEU HA H 3.868 0.005 1 161 18 18 LEU HB2 H 1.667 0.004 2 162 18 18 LEU HB3 H 1.041 0.005 2 163 18 18 LEU HG H 1.446 0.004 1 164 18 18 LEU HD1 H 0.661 0.002 2 165 18 18 LEU HD2 H 0.589 0.002 2 166 18 18 LEU C C 176.037 . 1 167 18 18 LEU CA C 55.100 0.039 1 168 18 18 LEU CB C 39.357 0.026 1 169 18 18 LEU CG C 24.279 0.037 1 170 18 18 LEU CD1 C 22.831 . 2 171 18 18 LEU CD2 C 20.954 0.03 2 172 18 18 LEU N N 121.912 0.013 1 173 19 19 ILE H H 8.218 0.004 1 174 19 19 ILE HA H 3.269 0.001 1 175 19 19 ILE HB H 1.763 0.004 1 176 19 19 ILE HG12 H 1.614 0.001 1 177 19 19 ILE HG2 H 0.663 0.002 1 178 19 19 ILE HD1 H 0.599 0.004 1 179 19 19 ILE C C 174.456 . 1 180 19 19 ILE CA C 62.916 0.002 1 181 19 19 ILE CB C 34.366 0.051 1 182 19 19 ILE CG1 C 27.881 0.02 1 183 19 19 ILE CG2 C 15.002 0.029 1 184 19 19 ILE CD1 C 9.869 0.017 1 185 19 19 ILE N N 119.554 0.016 1 186 20 20 GLU H H 7.653 0.003 1 187 20 20 GLU HA H 3.725 0.003 1 188 20 20 GLU HB2 H 1.997 0.003 2 189 20 20 GLU HB3 H 1.894 0.008 2 190 20 20 GLU HG2 H 2.213 0.009 2 191 20 20 GLU HG3 H 2.000 0.004 2 192 20 20 GLU C C 176.336 . 1 193 20 20 GLU CA C 56.936 0.057 1 194 20 20 GLU CB C 26.392 0.025 1 195 20 20 GLU CG C 33.451 0.043 1 196 20 20 GLU N N 117.916 0.012 1 197 21 21 MET H H 7.515 0.002 1 198 21 21 MET HA H 3.824 0.006 1 199 21 21 MET HB2 H 1.960 0.003 1 200 21 21 MET HG2 H 2.211 0.011 2 201 21 21 MET HG3 H 2.534 0.004 2 202 21 21 MET HE H 1.549 0.002 1 203 21 21 MET C C 176.169 . 1 204 21 21 MET CA C 56.331 0.017 1 205 21 21 MET CB C 27.355 0.052 1 206 21 21 MET CG C 28.590 0.017 1 207 21 21 MET CE C 13.220 0.009 1 208 21 21 MET N N 120.409 0.013 1 209 22 22 LEU H H 8.279 0.004 1 210 22 22 LEU HA H 3.591 0.005 1 211 22 22 LEU HB2 H 1.821 0.004 2 212 22 22 LEU HB3 H 0.822 0.004 2 213 22 22 LEU HG H 1.410 0.001 1 214 22 22 LEU HD1 H 0.245 0.003 2 215 22 22 LEU HD2 H 0.130 0.004 2 216 22 22 LEU C C 176.167 . 1 217 22 22 LEU CA C 54.888 0.001 1 218 22 22 LEU CB C 38.278 0.036 1 219 22 22 LEU CG C 23.426 0.052 1 220 22 22 LEU CD1 C 22.442 0.014 2 221 22 22 LEU CD2 C 19.004 0.01 2 222 22 22 LEU N N 123.911 0.018 1 223 23 23 VAL H H 8.234 0.001 1 224 23 23 VAL HA H 4.012 0.003 1 225 23 23 VAL HB H 1.953 0.004 1 226 23 23 VAL HG1 H 0.707 0.004 2 227 23 23 VAL HG2 H 0.716 0.004 2 228 23 23 VAL C C 178.170 . 1 229 23 23 VAL CA C 62.358 0.037 1 230 23 23 VAL CB C 29.218 0.047 1 231 23 23 VAL CG1 C 19.357 0.018 2 232 23 23 VAL CG2 C 18.453 0.002 2 233 23 23 VAL N N 120.864 0.007 1 234 24 24 ARG H H 8.450 0.002 1 235 24 24 ARG HA H 3.906 0.001 1 236 24 24 ARG HB2 H 1.815 0.004 1 237 24 24 ARG HG2 H 1.551 0.002 2 238 24 24 ARG HG3 H 1.482 . 2 239 24 24 ARG HD2 H 3.031 0.007 1 240 24 24 ARG C C 175.876 . 1 241 24 24 ARG CA C 56.841 0.014 1 242 24 24 ARG CB C 27.359 . 1 243 24 24 ARG CG C 24.683 0.03 1 244 24 24 ARG CD C 40.482 . 1 245 24 24 ARG N N 122.848 0.014 1 246 25 25 THR H H 7.888 0.002 1 247 25 25 THR HA H 4.205 0.001 1 248 25 25 THR HB H 4.399 0.002 1 249 25 25 THR HG2 H 1.119 0.003 1 250 25 25 THR C C 172.886 . 1 251 25 25 THR CA C 58.953 0.022 1 252 25 25 THR CB C 67.256 0.095 1 253 25 25 THR CG2 C 18.848 0.011 1 254 25 25 THR N N 105.314 0.007 1 255 26 26 GLY H H 7.607 0.002 1 256 26 26 GLY HA2 H 3.893 0.002 2 257 26 26 GLY HA3 H 3.784 0.003 2 258 26 26 GLY C C 172.151 . 1 259 26 26 GLY CA C 43.269 0.016 1 260 26 26 GLY N N 109.587 0.014 1 261 27 27 GLN H H 8.350 0.001 1 262 27 27 GLN HA H 3.952 0.002 1 263 27 27 GLN HB2 H 1.662 0.003 2 264 27 27 GLN HB3 H 1.971 0.006 2 265 27 27 GLN HG2 H 2.160 0.003 2 266 27 27 GLN HG3 H 2.026 0.004 2 267 27 27 GLN C C 172.895 . 1 268 27 27 GLN CA C 54.531 0.034 1 269 27 27 GLN CB C 26.821 0.008 1 270 27 27 GLN CG C 31.657 0.029 1 271 27 27 GLN N N 118.799 0.009 1 272 28 28 ILE H H 6.963 0.003 1 273 28 28 ILE HA H 4.347 0.004 1 274 28 28 ILE HB H 1.278 0.003 1 275 28 28 ILE HG12 H 1.108 0.003 2 276 28 28 ILE HG13 H 0.580 0.001 2 277 28 28 ILE HG2 H 0.589 0.003 1 278 28 28 ILE HD1 H 0.579 0.002 1 279 28 28 ILE C C 169.935 . 1 280 28 28 ILE CA C 54.765 0.023 1 281 28 28 ILE CB C 38.635 0.038 1 282 28 28 ILE CG1 C 24.264 0.047 1 283 28 28 ILE CG2 C 15.327 0.035 1 284 28 28 ILE CD1 C 12.318 0.02 1 285 28 28 ILE N N 115.792 0.013 1 286 29 29 PRO HA H 4.223 0.003 1 287 29 29 PRO HB2 H 2.164 0.001 2 288 29 29 PRO HB3 H 1.763 0.003 2 289 29 29 PRO HG2 H 1.793 0.002 2 290 29 29 PRO HG3 H 1.742 0.002 2 291 29 29 PRO HD2 H 3.571 0.006 2 292 29 29 PRO HD3 H 3.319 0.003 2 293 29 29 PRO C C 174.313 . 1 294 29 29 PRO CA C 59.663 0.016 1 295 29 29 PRO CB C 29.869 0.014 1 296 29 29 PRO CG C 24.766 0.001 1 297 29 29 PRO CD C 48.417 0.022 1 298 30 30 ALA H H 8.556 0.002 1 299 30 30 ALA HA H 3.739 0.002 1 300 30 30 ALA HB H 1.181 0.001 1 301 30 30 ALA C C 175.720 . 1 302 30 30 ALA CA C 51.761 0.015 1 303 30 30 ALA CB C 15.521 0.013 1 304 30 30 ALA N N 122.872 0.021 1 305 31 31 ASP H H 8.020 0.004 1 306 31 31 ASP HA H 4.369 0.002 1 307 31 31 ASP HB2 H 2.651 0.004 2 308 31 31 ASP HB3 H 2.345 0.002 2 309 31 31 ASP C C 173.074 . 1 310 31 31 ASP CA C 49.705 0.017 1 311 31 31 ASP CB C 36.535 0.024 1 312 31 31 ASP N N 113.381 0.009 1 313 32 32 ALA H H 7.049 0.002 1 314 32 32 ALA HA H 4.088 0.001 1 315 32 32 ALA HB H 1.196 0.001 1 316 32 32 ALA C C 174.605 . 1 317 32 32 ALA CA C 49.472 0.01 1 318 32 32 ALA CB C 17.117 0.011 1 319 32 32 ALA N N 121.809 0.009 1 320 33 33 SER H H 9.110 0.002 1 321 33 33 SER HA H 4.168 0.01 1 322 33 33 SER HB2 H 3.884 0.005 2 323 33 33 SER HB3 H 4.142 0.001 2 324 33 33 SER C C 171.437 . 1 325 33 33 SER CA C 54.282 0.052 1 326 33 33 SER CB C 62.080 0.03 1 327 33 33 SER N N 118.137 0.024 1 328 34 34 ASP H H 8.790 0.004 1 329 34 34 ASP HA H 4.074 0.003 1 330 34 34 ASP HB2 H 2.494 0.003 2 331 34 34 ASP HB3 H 2.486 0.008 2 332 34 34 ASP C C 176.305 . 1 333 34 34 ASP CA C 55.377 0.047 1 334 34 34 ASP CB C 36.960 0.005 1 335 34 34 ASP N N 121.259 0.016 1 336 35 35 VAL H H 7.794 0.002 1 337 35 35 VAL HA H 3.497 0.003 1 338 35 35 VAL HB H 1.691 0.006 1 339 35 35 VAL HG1 H 0.733 0.001 2 340 35 35 VAL HG2 H 0.842 0.001 2 341 35 35 VAL C C 174.814 . 1 342 35 35 VAL CA C 63.236 0.024 1 343 35 35 VAL CB C 29.363 0.034 1 344 35 35 VAL CG1 C 17.857 0.033 2 345 35 35 VAL CG2 C 19.756 0.013 2 346 35 35 VAL N N 119.462 0.014 1 347 36 36 ASP H H 7.511 0.003 1 348 36 36 ASP HA H 4.279 0.003 1 349 36 36 ASP HB2 H 2.650 0.004 2 350 36 36 ASP HB3 H 2.315 0.003 2 351 36 36 ASP C C 177.702 . 1 352 36 36 ASP CA C 54.554 0.009 1 353 36 36 ASP CB C 37.044 0.004 1 354 36 36 ASP N N 121.543 0.013 1 355 37 37 LYS H H 8.542 0.002 1 356 37 37 LYS HA H 3.588 0.002 1 357 37 37 LYS HB2 H 1.818 0.002 1 358 37 37 LYS HG2 H 0.829 0.003 1 359 37 37 LYS HD2 H 1.522 0.023 2 360 37 37 LYS HD3 H 1.409 0.002 2 361 37 37 LYS C C 174.496 . 1 362 37 37 LYS CA C 57.990 0.019 1 363 37 37 LYS CB C 29.888 . 1 364 37 37 LYS CG C 24.548 . 1 365 37 37 LYS CD C 27.388 . 1 366 37 37 LYS N N 121.843 0.023 1 367 38 38 ARG H H 7.591 0.003 1 368 38 38 ARG HA H 3.760 0.003 1 369 38 38 ARG HB2 H 1.807 0.007 2 370 38 38 ARG HB3 H 1.755 0.004 2 371 38 38 ARG HG2 H 1.545 . 2 372 38 38 ARG HG3 H 1.461 . 2 373 38 38 ARG HD2 H 2.946 . 2 374 38 38 ARG HD3 H 3.009 . 2 375 38 38 ARG C C 176.190 . 1 376 38 38 ARG CA C 56.662 . 1 377 38 38 ARG CB C 26.104 . 1 378 38 38 ARG CG C 24.532 . 1 379 38 38 ARG CD C 39.949 0.003 1 380 38 38 ARG N N 118.495 0.015 1 381 39 39 ILE H H 7.887 0.002 1 382 39 39 ILE HA H 3.560 0.006 1 383 39 39 ILE HB H 1.645 0.005 1 384 39 39 ILE HG12 H 1.573 0.003 2 385 39 39 ILE HG13 H 0.918 0.003 2 386 39 39 ILE HG2 H 0.713 0.013 1 387 39 39 ILE HD1 H 0.672 0.014 1 388 39 39 ILE C C 175.705 . 1 389 39 39 ILE CA C 62.211 0.004 1 390 39 39 ILE CB C 35.593 0.061 1 391 39 39 ILE CG1 C 26.627 0.011 1 392 39 39 ILE CG2 C 14.052 0.022 1 393 39 39 ILE CD1 C 10.565 0.018 1 394 39 39 ILE N N 120.778 0.017 1 395 40 40 ALA H H 7.688 0.003 1 396 40 40 ALA HA H 3.907 0.003 1 397 40 40 ALA HB H 1.272 0.006 1 398 40 40 ALA C C 177.965 . 1 399 40 40 ALA CA C 52.100 0.05 1 400 40 40 ALA CB C 15.688 0.008 1 401 40 40 ALA N N 121.774 0.01 1 402 41 41 LEU H H 8.202 0.003 1 403 41 41 LEU HA H 3.788 0.008 1 404 41 41 LEU HB2 H 1.836 0.006 2 405 41 41 LEU HB3 H 1.318 0.003 2 406 41 41 LEU HG H 1.446 0.003 1 407 41 41 LEU HD1 H 0.728 0.007 2 408 41 41 LEU HD2 H 0.717 0.001 2 409 41 41 LEU C C 174.973 . 1 410 41 41 LEU CA C 55.454 0.028 1 411 41 41 LEU CB C 38.366 0.024 1 412 41 41 LEU CD1 C 22.283 0.011 1 413 41 41 LEU CD2 C 22.283 0.011 1 414 41 41 LEU N N 121.144 0.013 1 415 42 42 GLU H H 8.122 0.006 1 416 42 42 GLU HA H 3.731 0.004 1 417 42 42 GLU HB2 H 1.996 0.002 2 418 42 42 GLU HB3 H 1.900 0.004 2 419 42 42 GLU HG2 H 2.305 0.007 2 420 42 42 GLU HG3 H 2.062 0.03 2 421 42 42 GLU C C 176.729 . 1 422 42 42 GLU CA C 57.146 0.048 1 423 42 42 GLU CB C 26.240 0.029 1 424 42 42 GLU CG C 33.787 0.104 1 425 42 42 GLU N N 118.871 0.013 1 426 43 43 ARG H H 7.974 0.003 1 427 43 43 ARG HA H 3.918 0.004 1 428 43 43 ARG HB2 H 1.762 0.004 1 429 43 43 ARG HG2 H 1.616 0.005 2 430 43 43 ARG HG3 H 1.475 0.001 2 431 43 43 ARG HD2 H 3.004 0.003 1 432 43 43 ARG C C 175.763 . 1 433 43 43 ARG CA C 56.414 0.023 1 434 43 43 ARG CB C 27.276 . 1 435 43 43 ARG CG C 24.402 0.032 1 436 43 43 ARG CD C 40.636 0.015 1 437 43 43 ARG N N 118.933 0.019 1 438 44 44 TYR H H 7.977 0.003 1 439 44 44 TYR HA H 4.002 0.006 1 440 44 44 TYR HB2 H 3.089 0.004 2 441 44 44 TYR HB3 H 2.930 0.003 2 442 44 44 TYR HD1 H 6.826 0.004 1 443 44 44 TYR HD2 H 6.826 0.004 1 444 44 44 TYR HE1 H 6.504 0.002 1 445 44 44 TYR HE2 H 6.504 0.002 1 446 44 44 TYR C C 175.013 . 1 447 44 44 TYR CA C 58.515 0.027 1 448 44 44 TYR CB C 35.510 0.025 1 449 44 44 TYR N N 121.528 0.012 1 450 45 45 LEU H H 8.438 0.003 1 451 45 45 LEU HA H 3.614 0.003 1 452 45 45 LEU HB2 H 1.753 0.003 2 453 45 45 LEU HB3 H 1.232 0.006 2 454 45 45 LEU HG H 1.830 0.003 1 455 45 45 LEU HD1 H 0.704 0.001 2 456 45 45 LEU HD2 H 0.713 0.002 2 457 45 45 LEU C C 176.484 . 1 458 45 45 LEU CA C 54.742 0.015 1 459 45 45 LEU CB C 38.650 0.023 1 460 45 45 LEU CG C 24.076 . 1 461 45 45 LEU CD1 C 23.178 0.002 2 462 45 45 LEU CD2 C 19.637 0.035 2 463 45 45 LEU N N 119.074 0.012 1 464 46 46 GLU H H 7.939 0.002 1 465 46 46 GLU HA H 3.769 0.004 1 466 46 46 GLU HB2 H 1.965 0.003 2 467 46 46 GLU HB3 H 1.858 0.005 2 468 46 46 GLU HG2 H 2.177 0.006 2 469 46 46 GLU HG3 H 2.049 0.004 2 470 46 46 GLU C C 175.991 . 1 471 46 46 GLU CA C 56.397 0.015 1 472 46 46 GLU CB C 26.669 0.014 1 473 46 46 GLU CG C 33.411 . 1 474 46 46 GLU N N 119.014 0.011 1 475 47 47 GLU H H 7.757 0.003 1 476 47 47 GLU HA H 3.792 0.003 1 477 47 47 GLU HB2 H 1.819 0.027 2 478 47 47 GLU HB3 H 1.850 . 2 479 47 47 GLU HG2 H 2.013 0.003 2 480 47 47 GLU HG3 H 2.139 0.001 2 481 47 47 GLU C C 175.861 . 1 482 47 47 GLU CA C 55.801 0.034 1 483 47 47 GLU CB C 26.260 . 1 484 47 47 GLU CG C 33.402 . 1 485 47 47 GLU N N 118.911 0.014 1 486 48 48 LYS H H 7.711 0.002 1 487 48 48 LYS HA H 3.716 0.003 1 488 48 48 LYS HB2 H 1.379 0.005 2 489 48 48 LYS HB3 H 1.391 0.006 2 490 48 48 LYS HG2 H 0.927 0.005 1 491 48 48 LYS HD2 H 1.232 0.001 1 492 48 48 LYS C C 176.172 . 1 493 48 48 LYS CA C 54.976 0.012 1 494 48 48 LYS CB C 29.055 0.001 1 495 48 48 LYS CG C 21.321 0.016 1 496 48 48 LYS CD C 25.669 0.011 1 497 48 48 LYS CE C 39.103 . 1 498 48 48 LYS N N 119.567 0.029 1 499 49 49 ILE H H 7.706 0.003 1 500 49 49 ILE HA H 3.664 0.002 1 501 49 49 ILE HB H 1.744 0.001 1 502 49 49 ILE HG12 H 1.395 0.002 2 503 49 49 ILE HG13 H 0.961 0.006 2 504 49 49 ILE HG2 H 0.686 0.003 1 505 49 49 ILE HD1 H 0.623 0.006 1 506 49 49 ILE C C 175.404 . 1 507 49 49 ILE CA C 60.618 0.037 1 508 49 49 ILE CB C 35.160 0.023 1 509 49 49 ILE CG1 C 25.823 0.012 1 510 49 49 ILE CG2 C 14.592 0.03 1 511 49 49 ILE CD1 C 10.131 0.021 1 512 49 49 ILE N N 119.548 0.008 1 513 50 50 ARG H H 7.850 0.003 1 514 50 50 ARG HA H 3.921 0.004 1 515 50 50 ARG HB2 H 1.668 0.003 1 516 50 50 ARG HG2 H 1.498 0.003 2 517 50 50 ARG HG3 H 1.408 0.002 2 518 50 50 ARG HD2 H 2.964 0.005 1 519 50 50 ARG C C 174.964 . 1 520 50 50 ARG CA C 55.256 0.006 1 521 50 50 ARG CB C 27.521 0.008 1 522 50 50 ARG CG C 24.630 . 1 523 50 50 ARG CD C 40.512 0.011 1 524 50 50 ARG N N 120.898 0.019 1 525 51 51 SER H H 7.938 0.003 1 526 51 51 SER HA H 4.148 0.001 1 527 51 51 SER HB2 H 3.732 0.007 2 528 51 51 SER HB3 H 3.692 0.004 2 529 51 51 SER C C 172.480 . 1 530 51 51 SER CA C 56.666 0.011 1 531 51 51 SER CB C 60.850 0.019 1 532 51 51 SER N N 113.995 0.009 1 533 52 52 GLY H H 7.825 0.005 1 534 52 52 GLY HA2 H 3.706 0.007 1 535 52 52 GLY C C 171.142 . 1 536 52 52 GLY CA C 42.591 . 1 537 52 52 GLY N N 109.741 0.006 1 538 53 53 PHE H H 7.836 0.001 1 539 53 53 PHE HA H 4.352 0.002 1 540 53 53 PHE HB2 H 2.844 0.005 1 541 53 53 PHE HD1 H 7.027 0.001 1 542 53 53 PHE HD2 H 7.027 0.001 1 543 53 53 PHE HE1 H 7.079 . 1 544 53 53 PHE HE2 H 7.079 . 1 545 53 53 PHE C C 173.061 . 1 546 53 53 PHE CA C 55.222 0.025 1 547 53 53 PHE CB C 36.569 0.012 1 548 53 53 PHE N N 119.983 0.005 1 549 54 54 LYS H H 8.105 0.002 1 550 54 54 LYS HA H 4.037 0.001 1 551 54 54 LYS HB2 H 1.590 0.001 1 552 54 54 LYS HB3 H 1.590 . 1 553 54 54 LYS HG2 H 1.180 . 2 554 54 54 LYS HG3 H 1.134 . 2 555 54 54 LYS HD2 H 1.479 . 2 556 54 54 LYS HD3 H 1.434 . 2 557 54 54 LYS HE2 H 2.761 . 1 558 54 54 LYS HE3 H 2.761 . 1 559 54 54 LYS C C 174.023 . 1 560 54 54 LYS CA C 53.499 0.045 1 561 54 54 LYS CB C 30.071 . 1 562 54 54 LYS CG C 21.812 . 1 563 54 54 LYS CD C 26.161 . 1 564 54 54 LYS CE C 39.300 . 1 565 54 54 LYS N N 123.359 0.024 1 566 55 55 GLY H H 7.626 0.002 1 567 55 55 GLY HA2 H 3.662 0.004 1 568 55 55 GLY HA3 H 3.662 0.004 1 569 55 55 GLY C C 170.979 . 1 570 55 55 GLY CA C 42.548 . 1 571 55 55 GLY N N 109.068 0.005 1 572 56 56 ASP H H 8.083 0.005 1 573 56 56 ASP HA H 4.375 0.004 1 574 56 56 ASP HB2 H 2.451 0.006 2 575 56 56 ASP HB3 H 2.504 0.003 2 576 56 56 ASP C C 173.744 . 1 577 56 56 ASP CA C 51.535 . 1 578 56 56 ASP CB C 38.455 0.007 1 579 56 56 ASP N N 120.522 0.015 1 580 57 57 ALA H H 8.175 0.002 1 581 57 57 ALA HA H 4.003 0.002 1 582 57 57 ALA HB H 1.155 0.003 1 583 57 57 ALA C C 175.216 . 1 584 57 57 ALA CA C 50.365 0.012 1 585 57 57 ALA CB C 16.073 0.021 1 586 57 57 ALA N N 124.412 0.006 1 587 58 58 GLN H H 8.120 0.007 1 588 58 58 GLN HA H 3.950 0.002 1 589 58 58 GLN HB2 H 1.652 0.002 2 590 58 58 GLN HB3 H 1.700 0.002 2 591 58 58 GLN HG2 H 1.905 0.003 1 592 58 58 GLN C C 173.163 . 1 593 58 58 GLN CA C 53.413 0.018 1 594 58 58 GLN CB C 26.251 0.014 1 595 58 58 GLN CG C 30.821 . 1 596 58 58 GLN N N 117.943 0.01 1 597 59 59 PHE H H 7.932 0.005 1 598 59 59 PHE HA H 4.347 0.002 1 599 59 59 PHE HB2 H 2.969 0.003 2 600 59 59 PHE HB3 H 2.797 0.001 2 601 59 59 PHE HD1 H 7.023 0.004 1 602 59 59 PHE HD2 H 7.023 0.004 1 603 59 59 PHE HE1 H 7.088 0.001 1 604 59 59 PHE HE2 H 7.088 0.001 1 605 59 59 PHE C C 173.575 . 1 606 59 59 PHE CA C 55.341 . 1 607 59 59 PHE CB C 36.667 0.035 1 608 59 59 PHE N N 119.838 0.008 1 609 60 60 GLY H H 8.123 0.002 1 610 60 60 GLY HA2 H 3.680 0.006 2 611 60 60 GLY HA3 H 3.689 0.007 2 612 60 60 GLY C C 171.386 . 1 613 60 60 GLY CA C 42.559 . 1 614 60 60 GLY N N 109.820 0.035 1 615 61 61 LYS H H 7.968 0.001 1 616 61 61 LYS HA H 3.960 0.001 1 617 61 61 LYS HB2 H 1.596 0.003 1 618 61 61 LYS HG2 H 1.250 0.012 2 619 61 61 LYS HG3 H 1.166 0.003 2 620 61 61 LYS HD2 H 1.464 . 1 621 61 61 LYS HE2 H 2.767 0.001 1 622 61 61 LYS C C 174.728 . 1 623 61 61 LYS CA C 54.728 . 1 624 61 61 LYS CB C 30.089 . 1 625 61 61 LYS CG C 21.990 0.015 1 626 61 61 LYS CD C 26.356 . 1 627 61 61 LYS CE C 39.319 . 1 628 61 61 LYS N N 120.832 0.006 1 629 62 62 LYS H H 8.159 0.003 1 630 62 62 LYS HA H 3.989 . 1 631 62 62 LYS HB2 H 1.579 . 1 632 62 62 LYS HG2 H 1.268 . 2 633 62 62 LYS HG3 H 1.199 . 2 634 62 62 LYS HD2 H 1.454 . 1 635 62 62 LYS HE2 H 2.763 0.001 1 636 62 62 LYS C C 174.525 . 1 637 62 62 LYS CA C 54.480 . 1 638 62 62 LYS CB C 29.657 . 1 639 62 62 LYS CG C 22.065 . 1 640 62 62 LYS CD C 26.175 . 1 641 62 62 LYS CE C 39.311 . 1 642 62 62 LYS N N 121.242 0.003 1 643 63 63 ALA H H 8.012 0.002 1 644 63 63 ALA HA H 3.966 0.001 1 645 63 63 ALA HB H 1.139 0.001 1 646 63 63 ALA C C 176.064 . 1 647 63 63 ALA CA C 50.576 . 1 648 63 63 ALA CB C 15.908 . 1 649 63 63 ALA N N 124.167 0.005 1 650 64 64 LEU H H 7.976 0.005 1 651 64 64 LEU HA H 3.953 0.005 1 652 64 64 LEU HB2 H 1.500 0.007 2 653 64 64 LEU HB3 H 1.359 . 2 654 64 64 LEU HG H 1.466 0.002 1 655 64 64 LEU HD1 H 0.652 . 2 656 64 64 LEU HD2 H 0.683 0.011 2 657 64 64 LEU C C 175.684 . 1 658 64 64 LEU CA C 53.481 0.01 1 659 64 64 LEU CB C 39.103 0.007 1 660 64 64 LEU CG C 24.205 0.005 1 661 64 64 LEU CD1 C 20.664 0.006 2 662 64 64 LEU CD2 C 22.155 0.014 2 663 64 64 LEU N N 120.341 0.008 1 664 65 65 GLU H H 8.092 0.003 1 665 65 65 GLU HA H 3.950 0.004 1 666 65 65 GLU HB2 H 1.821 0.003 2 667 65 65 GLU HB3 H 1.968 0.002 2 668 65 65 GLU HG2 H 2.011 0.004 2 669 65 65 GLU HG3 H 2.136 0.002 2 670 65 65 GLU C C 174.622 . 1 671 65 65 GLU CA C 54.682 0.08 1 672 65 65 GLU CB C 26.872 0.158 1 673 65 65 GLU CG C 33.488 0.038 1 674 65 65 GLU N N 120.942 0.014 1 675 66 66 GLN H H 8.091 0.004 1 676 66 66 GLN HA H 4.013 0.002 1 677 66 66 GLN HB2 H 1.884 0.003 2 678 66 66 GLN HB3 H 1.831 0.003 2 679 66 66 GLN HG2 H 2.177 0.001 1 680 66 66 GLN C C 173.965 . 1 681 66 66 GLN CA C 53.915 . 1 682 66 66 GLN CB C 26.230 0.001 1 683 66 66 GLN CG C 30.948 . 1 684 66 66 GLN N N 120.476 0.002 1 685 67 67 ARG H H 8.035 0.001 1 686 67 67 ARG HA H 3.970 . 1 687 67 67 ARG HB2 H 1.658 0.002 2 688 67 67 ARG HB3 H 1.595 0.005 2 689 67 67 ARG HG2 H 1.447 0.002 1 690 67 67 ARG HD2 H 2.950 . 1 691 67 67 ARG C C 173.749 . 1 692 67 67 ARG CA C 54.280 . 1 693 67 67 ARG CB C 27.635 0.029 1 694 67 67 ARG CG C 24.225 . 1 695 67 67 ARG CD C 40.574 . 1 696 67 67 ARG N N 121.250 0.008 1 697 68 68 ALA H H 8.009 0.001 1 698 68 68 ALA HA H 3.997 0.002 1 699 68 68 ALA HB H 1.199 0.001 1 700 68 68 ALA C C 175.527 . 1 701 68 68 ALA CA C 50.368 0.012 1 702 68 68 ALA CB C 16.018 0.01 1 703 68 68 ALA N N 123.389 0.007 1 704 69 69 LYS H H 7.911 0.002 1 705 69 69 LYS HA H 3.983 . 1 706 69 69 LYS HB2 H 1.628 0.023 1 707 69 69 LYS HG2 H 1.299 . 2 708 69 69 LYS HG3 H 1.183 . 2 709 69 69 LYS HD2 H 1.468 . 1 710 69 69 LYS HE2 H 2.762 . 1 711 69 69 LYS C C 174.299 . 1 712 69 69 LYS CA C 54.325 . 1 713 69 69 LYS CB C 30.045 . 1 714 69 69 LYS CG C 22.189 . 1 715 69 69 LYS CD C 26.328 . 1 716 69 69 LYS CE C 39.348 . 1 717 69 69 LYS N N 119.870 0.008 1 718 70 70 ILE H H 7.866 0.003 1 719 70 70 ILE HA H 3.833 0.002 1 720 70 70 ILE HB H 1.657 0.004 1 721 70 70 ILE HG12 H 1.311 0.004 1 722 70 70 ILE HG2 H 0.670 0.004 1 723 70 70 ILE HD1 H 0.639 0.008 1 724 70 70 ILE C C 173.667 . 1 725 70 70 ILE CA C 58.806 0.048 1 726 70 70 ILE CB C 35.515 0.028 1 727 70 70 ILE CG1 C 24.874 0.052 1 728 70 70 ILE CG2 C 14.665 0.008 1 729 70 70 ILE CD1 C 9.989 . 1 730 70 70 ILE N N 121.689 0.017 1 731 71 71 LEU H H 8.077 0.002 1 732 71 71 LEU HA H 4.077 0.002 1 733 71 71 LEU HB2 H 1.330 0.004 2 734 71 71 LEU HB3 H 1.444 0.003 2 735 71 71 LEU HG H 1.433 0.001 1 736 71 71 LEU HD1 H 0.633 0.001 2 737 71 71 LEU HD2 H 0.692 0.004 2 738 71 71 LEU C C 174.411 . 1 739 71 71 LEU CA C 52.544 0.016 1 740 71 71 LEU CB C 39.295 0.012 1 741 71 71 LEU CG C 24.201 . 1 742 71 71 LEU CD1 C 20.668 . 2 743 71 71 LEU CD2 C 22.160 . 2 744 71 71 LEU N N 125.382 0.009 1 745 72 72 LYS H H 7.981 0.003 1 746 72 72 LYS HA H 4.067 . 1 747 72 72 LYS HB2 H 1.575 0.006 1 748 72 72 LYS HG2 H 1.255 . 2 749 72 72 LYS HG3 H 1.168 . 2 750 72 72 LYS HD2 H 1.461 . 1 751 72 72 LYS HE2 H 2.763 . 1 752 72 72 LYS C C 173.789 . 1 753 72 72 LYS CA C 53.757 . 1 754 72 72 LYS CB C 30.032 . 1 755 72 72 LYS CG C 22.008 0.015 1 756 72 72 LYS CD C 26.259 . 1 757 72 72 LYS N N 122.192 0.008 1 758 73 73 VAL H H 7.968 0.004 1 759 73 73 VAL HA H 3.802 0.007 1 760 73 73 VAL HB H 1.850 0.002 1 761 73 73 VAL HG1 H 0.745 0.002 2 762 73 73 VAL HG2 H 0.690 0.002 2 763 73 73 VAL C C 173.662 . 1 764 73 73 VAL CA C 60.174 0.051 1 765 73 73 VAL CB C 29.765 0.028 1 766 73 73 VAL CG1 C 18.206 . 2 767 73 73 VAL CG2 C 18.434 . 2 768 73 73 VAL N N 122.356 0.023 1 769 74 74 ILE H H 8.082 0.002 1 770 74 74 ILE HA H 3.881 0.003 1 771 74 74 ILE HB H 1.640 0.006 1 772 74 74 ILE HG12 H 1.119 . 1 773 74 74 ILE HG2 H 0.665 0.003 1 774 74 74 ILE HD1 H 0.629 . 1 775 74 74 ILE C C 173.240 . 1 776 74 74 ILE CA C 58.553 0.001 1 777 74 74 ILE CB C 35.702 0.061 1 778 74 74 ILE CG1 C 24.595 . 1 779 74 74 ILE CG2 C 14.603 . 1 780 74 74 ILE CD1 C 10.101 . 1 781 74 74 ILE N N 124.593 0.01 1 782 75 75 ASP H H 8.215 0.002 1 783 75 75 ASP HA H 4.360 0.002 1 784 75 75 ASP HB2 H 2.500 0.002 2 785 75 75 ASP HB3 H 2.386 0.003 2 786 75 75 ASP C C 173.648 . 1 787 75 75 ASP CA C 51.664 . 1 788 75 75 ASP CB C 38.373 . 1 789 75 75 ASP N N 124.492 0.01 1 790 76 76 LYS H H 8.128 0.003 1 791 76 76 LYS HA H 4.023 0.001 1 792 76 76 LYS HB2 H 1.562 0.001 2 793 76 76 LYS HB3 H 1.655 0.004 2 794 76 76 LYS HG2 H 1.208 . 2 795 76 76 LYS HG3 H 1.257 . 2 796 76 76 LYS HD2 H 1.471 . 1 797 76 76 LYS HE2 H 2.785 . 1 798 76 76 LYS C C 174.072 . 1 799 76 76 LYS CA C 53.811 . 1 800 76 76 LYS CB C 29.930 . 1 801 76 76 LYS CG C 21.981 0.015 1 802 76 76 LYS CD C 26.226 . 1 803 76 76 LYS CE C 39.264 . 1 804 76 76 LYS N N 122.158 0.007 1 805 77 77 GLN H H 8.215 0.001 1 806 77 77 GLN HA H 4.054 0.002 1 807 77 77 GLN HB2 H 1.901 0.001 2 808 77 77 GLN HB3 H 1.811 0.004 2 809 77 77 GLN HG2 H 2.161 0.001 2 810 77 77 GLN HG3 H 2.157 0.003 2 811 77 77 GLN C C 173.284 . 1 812 77 77 GLN CA C 53.247 0.002 1 813 77 77 GLN CB C 26.301 . 1 814 77 77 GLN CG C 31.025 . 1 815 77 77 GLN N N 120.468 0.008 1 816 78 78 LYS H H 8.116 0.001 1 817 78 78 LYS HA H 4.131 0.004 1 818 78 78 LYS HB2 H 1.662 . 2 819 78 78 LYS HB3 H 1.564 . 2 820 78 78 LYS HG2 H 1.215 . 2 821 78 78 LYS HG3 H 1.264 . 2 822 78 78 LYS HD2 H 1.468 . 1 823 78 78 LYS HE2 H 2.779 . 1 824 78 78 LYS C C 173.961 . 1 825 78 78 LYS CA C 53.520 . 1 826 78 78 LYS CB C 30.362 . 1 827 78 78 LYS CG C 21.944 . 1 828 78 78 LYS CD C 26.239 . 1 829 78 78 LYS CE C 39.302 . 1 830 78 78 LYS N N 122.146 0.015 1 831 79 79 GLY H H 8.091 . 1 832 79 79 GLY HA2 H 3.866 . 2 833 79 79 GLY HA3 H 3.914 0.004 2 834 79 79 GLY C C 168.980 . 1 835 79 79 GLY CA C 41.787 0.018 1 836 79 79 GLY N N 109.938 0.005 1 837 80 80 PRO HA H 4.196 0.002 1 838 80 80 PRO HB2 H 2.014 0.003 2 839 80 80 PRO HB3 H 1.610 0.002 2 840 80 80 PRO HG2 H 1.778 . 2 841 80 80 PRO HG3 H 1.665 . 2 842 80 80 PRO HD2 H 3.391 0.001 1 843 80 80 PRO HD3 H 3.391 . 1 844 80 80 PRO C C 174.109 . 1 845 80 80 PRO CA C 60.431 0.001 1 846 80 80 PRO CB C 29.273 0.009 1 847 80 80 PRO CG C 24.233 . 1 848 80 80 PRO CD C 46.922 . 1 849 81 81 HIS H H 8.284 0.001 1 850 81 81 HIS HA H 4.366 0.003 1 851 81 81 HIS HB2 H 2.878 . 1 852 81 81 HIS HB3 H 2.879 0.001 1 853 81 81 HIS C C 172.358 . 1 854 81 81 HIS CA C 53.361 . 1 855 81 81 HIS CB C 27.771 . 1 856 81 81 HIS N N 120.044 0.019 1 857 82 82 LYS H H 8.034 . 1 858 82 82 LYS HA H 4.057 . 1 859 82 82 LYS HB2 H 1.564 . 1 860 82 82 LYS HB3 H 1.564 . 1 861 82 82 LYS HG2 H 1.159 . 1 862 82 82 LYS HG3 H 1.159 . 1 863 82 82 LYS HD2 H 1.471 . 1 864 82 82 LYS HD3 H 1.471 . 1 865 82 82 LYS HE2 H 2.769 . 1 866 82 82 LYS HE3 H 2.771 0.001 1 867 82 82 LYS C C 172.957 . 1 868 82 82 LYS CA C 53.091 . 1 869 82 82 LYS CB C 30.337 . 1 870 82 82 LYS CG C 21.683 . 1 871 82 82 LYS CD C 26.225 . 1 872 82 82 LYS CE C 39.320 . 1 873 82 82 LYS N N 123.552 0.007 1 874 83 83 ALA H H 8.258 . 1 875 83 83 ALA HA H 4.066 0.001 1 876 83 83 ALA HB H 1.183 0.001 1 877 83 83 ALA C C 173.999 . 1 878 83 83 ALA CA C 49.798 0.01 1 879 83 83 ALA CB C 16.373 . 1 880 83 83 ALA N N 126.536 0.008 1 881 84 84 ARG H H 7.810 0.002 1 882 84 84 ARG C C 178.310 . 1 883 84 84 ARG CA C 54.613 . 1 884 84 84 ARG CB C 28.513 . 1 885 84 84 ARG N N 125.395 0.008 1 stop_ save_