data_28069 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Backbone resonances of the nSH2 domain of SHP2 ; _BMRB_accession_number 28069 _BMRB_flat_file_name bmr28069.str _Entry_type original _Submission_date 2020-02-09 _Accession_date 2020-02-09 _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 Marasco Michelangelo . . 2 Carlomagno Teresa . . 3 Kirkpatrick John P. . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 94 "13C chemical shifts" 187 "15N chemical shifts" 94 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2020-11-13 original BMRB . stop_ loop_ _Related_BMRB_accession_number _Relationship 28070 'cSH2 domain of SHP2' 28071 'tandem SH2 domain of SHP2' 28072 'cSH2 domain of SHP2 in complex with the ITIM of PD-1' 28073 'nSH2 domain of SHP2 in complex with the ITSM of PD-1' 28074 'nSH2 domain of SHP2 in complex with the ITIM of PD-1' 28075 'tSH2 domain in complex with the bidentate ITIM-ITSM peptide of PD-1, ITIM-bound state' 28076 'tSH2 domain in complex with the bidentate ITIM-ITSM peptide of PD-1, ITSM-bound state' stop_ _Original_release_date 2020-02-10 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; 1H, 13C, 15N chemical shift assignments of SHP2 SH2 domains in complex with PD-1 immune-tyrosine motifs ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 32236803 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Marasco Michelangelo . . 2 Kirkpatrick John P. . 3 Carlomagno Teresa . . stop_ _Journal_abbreviation 'Biomol. NMR Assign.' _Journal_name_full 'Biomolecular NMR assignments' _Journal_volume 14 _Journal_issue 2 _Journal_ISSN 1874-270X _Journal_CSD 0353 _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 179 _Page_last 188 _Year 2020 _Details . save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name nSH2 _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label nSH2 $nSH2 stop_ _System_molecular_weight 12003.5316 _System_physical_state native _System_oligomer_state ? _System_paramagnetic no _System_thiol_state 'all free' _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_nSH2 _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common nSH2 _Molecular_mass 12003.5316 _Mol_thiol_state 'all free' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 107 _Mol_residue_sequence ; GPMASRRWFHPNITGVEAEN LLLTRGVDGSFLARPSKSNP GDFTLSVRRNGAVTHIKIQN TGDYYDLYGGEKFATLAELV QYYMEHHGQLKEKNGDVIEL KYPLNCA ; loop_ _Residue_seq_code _Residue_label 1 GLY 2 PRO 3 MET 4 ALA 5 SER 6 ARG 7 ARG 8 TRP 9 PHE 10 HIS 11 PRO 12 ASN 13 ILE 14 THR 15 GLY 16 VAL 17 GLU 18 ALA 19 GLU 20 ASN 21 LEU 22 LEU 23 LEU 24 THR 25 ARG 26 GLY 27 VAL 28 ASP 29 GLY 30 SER 31 PHE 32 LEU 33 ALA 34 ARG 35 PRO 36 SER 37 LYS 38 SER 39 ASN 40 PRO 41 GLY 42 ASP 43 PHE 44 THR 45 LEU 46 SER 47 VAL 48 ARG 49 ARG 50 ASN 51 GLY 52 ALA 53 VAL 54 THR 55 HIS 56 ILE 57 LYS 58 ILE 59 GLN 60 ASN 61 THR 62 GLY 63 ASP 64 TYR 65 TYR 66 ASP 67 LEU 68 TYR 69 GLY 70 GLY 71 GLU 72 LYS 73 PHE 74 ALA 75 THR 76 LEU 77 ALA 78 GLU 79 LEU 80 VAL 81 GLN 82 TYR 83 TYR 84 MET 85 GLU 86 HIS 87 HIS 88 GLY 89 GLN 90 LEU 91 LYS 92 GLU 93 LYS 94 ASN 95 GLY 96 ASP 97 VAL 98 ILE 99 GLU 100 LEU 101 LYS 102 TYR 103 PRO 104 LEU 105 ASN 106 CYS 107 ALA 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 _Gene_mnemonic $nSH2 Human 9606 Eukaryota Metazoa Homo sapiens ptpn11 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 $nSH2 'recombinant technology' 'Escherichia coli' Escherichia coli 'Tuner (DE3)' pETM22 stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_nSH2_1 _Saveframe_category sample _Sample_type solution _Details '100mM MES, 150mM NaCl, 3mM TCEP, pH 6.8' loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $nSH2 0.8 mM '[U-13C; U-15N]' MES 100.0 mM 'natural abundance' NaCl 150.0 mM 'natural abundance' TCEP 3.0 mM 'natural abundance' stop_ save_ ############################ # Computer software used # ############################ save_CcpNmr_Analysis _Saveframe_category software _Name CcpNmr_Analysis _Version 2.4 loop_ _Vendor _Address _Electronic_address CCPN 'Department of Biochemistry, Cambridge CB2 1GA, UK' http://www.ccpn.ac.uk stop_ loop_ _Task 'peak picking, chemical shift assignment' stop_ _Details 'The CCPN NMR assignment and data analysis application' save_ save_NMRPipe _Saveframe_category software _Name NMRPipe _Version 8.7 loop_ _Vendor _Address _Electronic_address 'F. Delaglio, S. Grzesiek, G. Vuister, G. Zhu, J. Pfeifer, A. Bax' . . stop_ loop_ _Task 'data processing' stop_ _Details . save_ save_TOPSPIN _Saveframe_category software _Name TOPSPIN _Version 3.2 loop_ _Vendor _Address _Electronic_address 'Bruker Biospin' . . stop_ loop_ _Task 'data collection' stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_850 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model 'Avance III HD' _Field_strength 850 _Details . save_ ############################# # NMR applied experiments # ############################# save_3D_HNCACB_1 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCACB' _Sample_label $nSH2_1 save_ save_HNCOCACB_(H[N[co[{CA|ca[C]}]]])_2 _Saveframe_category NMR_applied_experiment _Experiment_name 'HNCOCACB (H[N[co[{CA|ca[C]}]]])' _Sample_label $nSH2_1 save_ save_2D_1H-15N_HSQC/HMQC_3 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-15N HSQC/HMQC' _Sample_label $nSH2_1 save_ ####################### # Sample conditions # ####################### save_Standard _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units 'ionic strength' 0.150 . M pH 6.800 . pH pressure 1.000 . atm temperature 298.000 . 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 HDO C 13 'hydroxyl proton' ppm 4.78 na indirect . . . 0.251449530 HDO H 1 'hydroxyl proton' ppm 4.78 internal indirect . . . 1.000000000 HDO N 15 'hydroxyl proton' ppm 4.78 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 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Software_label $CcpNmr_Analysis stop_ loop_ _Experiment_label '3D HNCACB' 'HNCOCACB (H[N[co[{CA|ca[C]}]]])' '2D 1H-15N HSQC/HMQC' stop_ loop_ _Sample_label $nSH2_1 stop_ _Sample_conditions_label $Standard _Chem_shift_reference_set_label $chemical_shift_reference_1 _Mol_system_component_name nSH2 _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 3 3 MET CA C 55.727 . 1 2 3 3 MET CB C 32.677 . 1 3 4 4 ALA H H 8.221 0.002 1 4 4 4 ALA CA C 53.070 0.009 1 5 4 4 ALA CB C 19.093 0.008 1 6 4 4 ALA N N 124.854 0.006 1 7 5 5 SER H H 7.972 0.006 1 8 5 5 SER CA C 58.524 0.005 1 9 5 5 SER CB C 63.699 0.01 1 10 5 5 SER N N 113.613 0.006 1 11 6 6 ARG H H 8.118 0.003 1 12 6 6 ARG CA C 54.968 0.012 1 13 6 6 ARG CB C 29.422 0.002 1 14 6 6 ARG N N 121.355 0.022 1 15 7 7 ARG H H 8.396 0.002 1 16 7 7 ARG CA C 58.189 0.007 1 17 7 7 ARG CB C 29.781 0.045 1 18 7 7 ARG N N 119.619 0.011 1 19 8 8 TRP H H 6.391 0.001 1 20 8 8 TRP CA C 54.529 0.001 1 21 8 8 TRP CB C 29.442 0.013 1 22 8 8 TRP N N 110.929 0.002 1 23 9 9 PHE H H 7.615 0.002 1 24 9 9 PHE CA C 56.967 0.004 1 25 9 9 PHE CB C 39.484 0.002 1 26 9 9 PHE N N 124.312 0.006 1 27 10 10 HIS H H 8.633 0.001 1 28 10 10 HIS CA C 52.572 . 1 29 10 10 HIS CB C 33.285 . 1 30 10 10 HIS N N 129.524 0.001 1 31 11 11 PRO CA C 63.840 . 1 32 11 11 PRO CB C 32.796 . 1 33 12 12 ASN H H 8.529 0.001 1 34 12 12 ASN CA C 53.246 0.002 1 35 12 12 ASN CB C 39.504 0.0 1 36 12 12 ASN N N 114.055 0.004 1 37 13 13 ILE H H 6.897 0.001 1 38 13 13 ILE CA C 60.723 0.005 1 39 13 13 ILE CB C 41.509 0.003 1 40 13 13 ILE N N 114.845 0.008 1 41 14 14 THR H H 8.454 0.002 1 42 14 14 THR CA C 60.314 0.022 1 43 14 14 THR CB C 71.701 0.003 1 44 14 14 THR N N 114.238 0.005 1 45 15 15 GLY H H 8.917 0.002 1 46 15 15 GLY CA C 47.818 0.002 1 47 15 15 GLY N N 109.686 0.002 1 48 16 16 VAL H H 7.888 0.002 1 49 16 16 VAL CA C 65.687 0.005 1 50 16 16 VAL CB C 31.959 0.003 1 51 16 16 VAL N N 120.393 0.004 1 52 17 17 GLU H H 7.417 0.001 1 53 17 17 GLU CA C 59.017 0.004 1 54 17 17 GLU CB C 30.274 0.003 1 55 17 17 GLU N N 120.765 0.005 1 56 18 18 ALA H H 8.542 0.002 1 57 18 18 ALA CA C 55.292 0.002 1 58 18 18 ALA CB C 18.644 0.001 1 59 18 18 ALA N N 121.646 0.006 1 60 19 19 GLU H H 8.177 0.001 1 61 19 19 GLU CA C 60.274 0.001 1 62 19 19 GLU CB C 28.732 0.001 1 63 19 19 GLU N N 116.416 0.006 1 64 20 20 ASN H H 8.013 0.001 1 65 20 20 ASN CA C 56.962 0.002 1 66 20 20 ASN CB C 38.669 0.005 1 67 20 20 ASN N N 116.195 0.005 1 68 21 21 LEU H H 8.640 0.001 1 69 21 21 LEU CA C 58.459 0.001 1 70 21 21 LEU CB C 42.581 0.006 1 71 21 21 LEU N N 122.379 0.005 1 72 22 22 LEU H H 8.093 0.001 1 73 22 22 LEU CA C 58.230 0.022 1 74 22 22 LEU CB C 42.532 0.006 1 75 22 22 LEU N N 118.496 0.005 1 76 23 23 LEU H H 8.340 0.001 1 77 23 23 LEU CA C 56.952 0.0 1 78 23 23 LEU CB C 41.490 0.001 1 79 23 23 LEU N N 116.841 0.006 1 80 24 24 THR H H 7.848 0.001 1 81 24 24 THR CA C 63.615 0.004 1 82 24 24 THR CB C 70.592 0.001 1 83 24 24 THR N N 109.188 0.004 1 84 25 25 ARG H H 8.434 0.001 1 85 25 25 ARG CA C 55.667 0.005 1 86 25 25 ARG CB C 31.769 0.001 1 87 25 25 ARG N N 119.427 0.007 1 88 26 26 GLY H H 7.061 0.001 1 89 26 26 GLY CA C 43.885 0.001 1 90 26 26 GLY N N 106.871 0.005 1 91 27 27 VAL H H 8.933 0.002 1 92 27 27 VAL CA C 59.099 0.001 1 93 27 27 VAL CB C 35.960 0.004 1 94 27 27 VAL N N 109.899 0.002 1 95 28 28 ASP H H 8.936 0.002 1 96 28 28 ASP CA C 57.825 0.006 1 97 28 28 ASP CB C 39.021 0.0 1 98 28 28 ASP N N 123.026 0.004 1 99 29 29 GLY H H 8.765 0.001 1 100 29 29 GLY CA C 44.785 0.005 1 101 29 29 GLY N N 112.901 0.004 1 102 30 30 SER H H 9.358 0.002 1 103 30 30 SER CA C 60.709 0.002 1 104 30 30 SER CB C 64.353 0.003 1 105 30 30 SER N N 122.516 0.005 1 106 31 31 PHE H H 8.025 0.001 1 107 31 31 PHE CA C 55.805 0.001 1 108 31 31 PHE CB C 44.357 0.004 1 109 31 31 PHE N N 116.357 0.001 1 110 32 32 LEU H H 9.252 0.001 1 111 32 32 LEU CA C 54.434 0.002 1 112 32 32 LEU CB C 44.769 0.017 1 113 32 32 LEU N N 114.837 0.002 1 114 33 33 ALA H H 9.673 0.001 1 115 33 33 ALA CA C 50.069 0.005 1 116 33 33 ALA CB C 23.717 0.002 1 117 33 33 ALA N N 121.868 0.007 1 118 34 34 ARG H H 9.144 0.001 1 119 34 34 ARG CA C 53.318 . 1 120 34 34 ARG CB C 30.538 . 1 121 34 34 ARG N N 116.895 0.005 1 122 40 40 PRO CA C 64.309 . 1 123 40 40 PRO CB C 31.799 . 1 124 41 41 GLY H H 8.559 0.002 1 125 41 41 GLY CA C 45.340 0.005 1 126 41 41 GLY N N 112.241 0.002 1 127 42 42 ASP H H 7.689 0.002 1 128 42 42 ASP CA C 53.507 0.002 1 129 42 42 ASP CB C 42.059 0.001 1 130 42 42 ASP N N 119.554 0.004 1 131 43 43 PHE H H 8.984 0.001 1 132 43 43 PHE CA C 57.215 0.001 1 133 43 43 PHE CB C 44.485 0.004 1 134 43 43 PHE N N 118.055 0.004 1 135 44 44 THR H H 9.501 0.001 1 136 44 44 THR CA C 62.317 0.0 1 137 44 44 THR CB C 72.476 0.001 1 138 44 44 THR N N 117.606 0.004 1 139 45 45 LEU H H 9.574 0.001 1 140 45 45 LEU CA C 53.451 0.001 1 141 45 45 LEU CB C 44.842 0.002 1 142 45 45 LEU N N 128.355 0.005 1 143 46 46 SER H H 9.389 0.002 1 144 46 46 SER CA C 58.947 0.006 1 145 46 46 SER CB C 64.960 0.002 1 146 46 46 SER N N 123.848 0.006 1 147 47 47 VAL H H 8.995 0.001 1 148 47 47 VAL CA C 59.976 0.005 1 149 47 47 VAL CB C 35.806 0.005 1 150 47 47 VAL N N 123.503 0.003 1 151 48 48 ARG H H 9.126 0.002 1 152 48 48 ARG CA C 54.638 0.004 1 153 48 48 ARG CB C 31.927 0.007 1 154 48 48 ARG N N 127.184 0.005 1 155 49 49 ARG H H 9.440 0.001 1 156 49 49 ARG CA C 55.597 0.004 1 157 49 49 ARG CB C 32.372 0.035 1 158 49 49 ARG N N 130.917 0.005 1 159 50 50 ASN H H 9.312 0.002 1 160 50 50 ASN CA C 54.452 0.005 1 161 50 50 ASN CB C 37.472 0.002 1 162 50 50 ASN N N 125.496 0.005 1 163 51 51 GLY H H 9.593 0.002 1 164 51 51 GLY CA C 46.032 0.004 1 165 51 51 GLY N N 105.989 0.005 1 166 52 52 ALA H H 7.979 0.001 1 167 52 52 ALA CA C 50.442 0.002 1 168 52 52 ALA CB C 22.194 0.002 1 169 52 52 ALA N N 122.756 0.002 1 170 53 53 VAL H H 8.663 0.002 1 171 53 53 VAL CA C 61.281 0.001 1 172 53 53 VAL CB C 33.948 0.002 1 173 53 53 VAL N N 119.764 0.003 1 174 54 54 THR H H 8.939 0.001 1 175 54 54 THR CA C 60.325 0.003 1 176 54 54 THR CB C 71.278 0.003 1 177 54 54 THR N N 124.526 0.005 1 178 55 55 HIS H H 8.509 0.001 1 179 55 55 HIS CA C 54.708 0.008 1 180 55 55 HIS CB C 32.457 0.0 1 181 55 55 HIS N N 125.512 0.002 1 182 56 56 ILE H H 9.821 0.001 1 183 56 56 ILE CA C 60.436 0.005 1 184 56 56 ILE CB C 40.780 0.001 1 185 56 56 ILE N N 127.187 0.004 1 186 57 57 LYS H H 8.654 0.002 1 187 57 57 LYS CA C 58.064 0.0 1 188 57 57 LYS CB C 33.265 0.0 1 189 57 57 LYS N N 128.278 0.007 1 190 58 58 ILE H H 8.631 0.001 1 191 58 58 ILE CA C 60.278 0.007 1 192 58 58 ILE CB C 39.732 0.003 1 193 58 58 ILE N N 123.346 0.006 1 194 59 59 GLN H H 8.877 0.002 1 195 59 59 GLN CA C 55.517 0.002 1 196 59 59 GLN CB C 29.175 0.002 1 197 59 59 GLN N N 128.917 0.005 1 198 60 60 ASN H H 8.632 0.002 1 199 60 60 ASN CA C 51.126 0.015 1 200 60 60 ASN CB C 40.041 0.008 1 201 60 60 ASN N N 123.033 0.006 1 202 61 61 THR H H 8.317 0.002 1 203 61 61 THR CA C 61.316 0.004 1 204 61 61 THR CB C 69.753 0.002 1 205 61 61 THR N N 116.881 0.008 1 206 62 62 GLY H H 8.266 0.002 1 207 62 62 GLY CA C 46.104 0.01 1 208 62 62 GLY N N 114.011 0.008 1 209 63 63 ASP H H 7.753 0.002 1 210 63 63 ASP CA C 54.716 0.004 1 211 63 63 ASP CB C 42.233 0.001 1 212 63 63 ASP N N 118.634 0.006 1 213 64 64 TYR H H 7.243 0.001 1 214 64 64 TYR CA C 56.765 0.001 1 215 64 64 TYR CB C 40.852 0.001 1 216 64 64 TYR N N 114.413 0.007 1 217 65 65 TYR H H 9.622 0.001 1 218 65 65 TYR CA C 56.543 0.027 1 219 65 65 TYR CB C 41.816 0.001 1 220 65 65 TYR N N 118.499 0.007 1 221 66 66 ASP H H 9.127 0.002 1 222 66 66 ASP CA C 53.705 0.001 1 223 66 66 ASP CB C 43.806 0.003 1 224 66 66 ASP N N 120.461 0.008 1 225 67 67 LEU H H 8.164 0.002 1 226 67 67 LEU CA C 53.559 0.043 1 227 67 67 LEU CB C 41.228 0.004 1 228 67 67 LEU N N 118.682 0.004 1 229 68 68 TYR H H 8.617 0.002 1 230 68 68 TYR CA C 60.014 0.007 1 231 68 68 TYR CB C 35.322 0.029 1 232 68 68 TYR N N 118.706 0.01 1 233 69 69 GLY H H 7.661 0.008 1 234 69 69 GLY CA C 44.743 0.005 1 235 69 69 GLY N N 107.442 0.025 1 236 70 70 GLY H H 8.365 0.002 1 237 70 70 GLY CA C 44.830 0.011 1 238 70 70 GLY N N 107.775 0.004 1 239 71 71 GLU H H 8.237 0.002 1 240 71 71 GLU CA C 56.835 0.002 1 241 71 71 GLU CB C 30.032 0.001 1 242 71 71 GLU N N 122.214 0.005 1 243 72 72 LYS H H 7.709 0.002 1 244 72 72 LYS CA C 54.960 0.009 1 245 72 72 LYS CB C 34.803 0.001 1 246 72 72 LYS N N 118.513 0.004 1 247 73 73 PHE H H 9.134 0.002 1 248 73 73 PHE CA C 57.217 0.002 1 249 73 73 PHE CB C 44.074 0.001 1 250 73 73 PHE N N 118.159 0.006 1 251 74 74 ALA H H 9.452 0.002 1 252 74 74 ALA CA C 54.507 0.0 1 253 74 74 ALA CB C 19.932 0.004 1 254 74 74 ALA N N 123.498 0.005 1 255 75 75 THR H H 7.186 0.002 1 256 75 75 THR CA C 58.781 0.001 1 257 75 75 THR CB C 73.627 0.002 1 258 75 75 THR N N 101.467 0.01 1 259 76 76 LEU H H 7.998 0.002 1 260 76 76 LEU CA C 57.033 0.003 1 261 76 76 LEU CB C 41.001 0.0 1 262 76 76 LEU N N 122.248 0.009 1 263 77 77 ALA H H 8.415 0.002 1 264 77 77 ALA CA C 55.551 0.002 1 265 77 77 ALA CB C 18.033 0.0 1 266 77 77 ALA N N 118.862 0.003 1 267 78 78 GLU H H 7.809 0.002 1 268 78 78 GLU CA C 59.485 0.005 1 269 78 78 GLU CB C 31.000 0.003 1 270 78 78 GLU N N 117.142 0.005 1 271 79 79 LEU H H 6.972 0.002 1 272 79 79 LEU CA C 58.689 0.006 1 273 79 79 LEU CB C 41.812 0.003 1 274 79 79 LEU N N 122.566 0.005 1 275 80 80 VAL H H 7.925 0.002 1 276 80 80 VAL CA C 67.406 0.003 1 277 80 80 VAL CB C 31.562 0.006 1 278 80 80 VAL N N 118.706 0.004 1 279 81 81 GLN H H 8.047 0.002 1 280 81 81 GLN CA C 59.115 0.005 1 281 81 81 GLN CB C 28.067 0.008 1 282 81 81 GLN N N 117.455 0.007 1 283 82 82 TYR H H 7.837 0.002 1 284 82 82 TYR CA C 62.261 0.009 1 285 82 82 TYR CB C 38.893 0.001 1 286 82 82 TYR N N 118.405 0.006 1 287 83 83 TYR H H 7.747 0.002 1 288 83 83 TYR CA C 62.797 0.011 1 289 83 83 TYR CB C 37.981 0.0 1 290 83 83 TYR N N 117.415 0.014 1 291 84 84 MET H H 8.310 0.002 1 292 84 84 MET CA C 59.324 0.002 1 293 84 84 MET CB C 34.011 0.008 1 294 84 84 MET N N 120.108 0.012 1 295 85 85 GLU H H 7.441 0.001 1 296 85 85 GLU CA C 56.843 0.008 1 297 85 85 GLU CB C 30.538 0.024 1 298 85 85 GLU N N 114.944 0.009 1 299 86 86 HIS H H 7.446 0.002 1 300 86 86 HIS CB C 26.975 . 1 301 86 86 HIS N N 118.280 0.022 1 302 88 88 GLY CA C 45.396 . 1 303 89 89 GLN H H 7.992 0.004 1 304 89 89 GLN CA C 56.312 0.001 1 305 89 89 GLN CB C 29.610 0.034 1 306 89 89 GLN N N 116.088 0.01 1 307 90 90 LEU H H 8.499 0.002 1 308 90 90 LEU CA C 54.723 0.0 1 309 90 90 LEU CB C 41.471 0.001 1 310 90 90 LEU N N 124.258 0.013 1 311 91 91 LYS H H 8.076 0.002 1 312 91 91 LYS CA C 54.513 0.02 1 313 91 91 LYS CB C 36.876 0.005 1 314 91 91 LYS N N 123.811 0.001 1 315 92 92 GLU H H 8.759 0.001 1 316 92 92 GLU CA C 55.523 0.008 1 317 92 92 GLU CB C 31.421 0.001 1 318 92 92 GLU N N 120.096 0.006 1 319 93 93 LYS H H 9.028 0.002 1 320 93 93 LYS CA C 59.285 0.001 1 321 93 93 LYS CB C 31.935 0.021 1 322 93 93 LYS N N 122.987 0.005 1 323 94 94 ASN H H 7.998 0.002 1 324 94 94 ASN CA C 52.997 0.004 1 325 94 94 ASN CB C 37.628 0.002 1 326 94 94 ASN N N 115.036 0.003 1 327 95 95 GLY H H 8.130 0.002 1 328 95 95 GLY CA C 44.975 0.003 1 329 95 95 GLY N N 108.697 0.006 1 330 96 96 ASP H H 8.075 0.001 1 331 96 96 ASP CA C 54.913 0.004 1 332 96 96 ASP CB C 40.528 0.006 1 333 96 96 ASP N N 121.989 0.006 1 334 97 97 VAL H H 8.343 0.002 1 335 97 97 VAL CA C 63.193 0.002 1 336 97 97 VAL CB C 32.930 0.001 1 337 97 97 VAL N N 121.820 0.006 1 338 98 98 ILE H H 8.507 0.001 1 339 98 98 ILE CA C 59.823 0.001 1 340 98 98 ILE CB C 39.043 0.001 1 341 98 98 ILE N N 127.677 0.005 1 342 99 99 GLU H H 8.196 0.001 1 343 99 99 GLU CA C 55.191 0.007 1 344 99 99 GLU CB C 31.746 0.002 1 345 99 99 GLU N N 124.481 0.001 1 346 100 100 LEU H H 8.635 0.002 1 347 100 100 LEU CA C 53.181 0.006 1 348 100 100 LEU CB C 40.191 0.003 1 349 100 100 LEU N N 124.965 0.005 1 350 101 101 LYS H H 8.210 0.001 1 351 101 101 LYS CA C 58.409 0.002 1 352 101 101 LYS CB C 35.006 0.002 1 353 101 101 LYS N N 120.637 0.004 1 354 102 102 TYR H H 7.799 0.001 1 355 102 102 TYR CA C 52.833 . 1 356 102 102 TYR CB C 40.739 . 1 357 102 102 TYR N N 116.456 0.002 1 358 103 103 PRO CA C 62.627 . 1 359 103 103 PRO CB C 32.184 . 1 360 104 104 LEU H H 8.733 0.001 1 361 104 104 LEU CA C 54.492 0.002 1 362 104 104 LEU CB C 41.710 0.005 1 363 104 104 LEU N N 128.659 0.004 1 364 105 105 ASN H H 8.505 0.002 1 365 105 105 ASN CA C 53.352 0.002 1 366 105 105 ASN CB C 39.220 0.002 1 367 105 105 ASN N N 125.381 0.01 1 368 106 106 CYS H H 8.623 0.001 1 369 106 106 CYS CA C 58.907 0.001 1 370 106 106 CYS CB C 27.226 0.001 1 371 106 106 CYS N N 121.615 0.006 1 372 107 107 ALA H H 8.081 0.002 1 373 107 107 ALA CA C 54.036 . 1 374 107 107 ALA CB C 20.205 . 1 375 107 107 ALA N N 133.192 0.005 1 stop_ save_