data_28073 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Backbone resonances of the nSH2 domain of SHP2 in complex with the ITSM of PD-1 ; _BMRB_accession_number 28073 _BMRB_flat_file_name bmr28073.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 Kirkpatrick John P. . 3 Carlomagno Teresa . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 98 "13C chemical shifts" 200 "15N chemical shifts" 98 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2020-11-13 original BMRB . stop_ loop_ _Related_BMRB_accession_number _Relationship 28069 'nSH2 domain of SHP2' 28070 'cSH2 domain of SHP2' 28071 'tandem SH2 domain of SHP2' 28072 'cSH2 domain of SHP2 in complex with the ITIM 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 domain of SHP2 in complex with the ITSM of PD-1' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label nSH2 $nSH2 ITSM $ITSM 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_ save_ITSM _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common ITSM _Molecular_mass . _Mol_thiol_state 'not present' _Details . _Residue_count 11 _Mol_residue_sequence ; EQTEXATIVFP ; loop_ _Residue_seq_code _Residue_label 1 GLU 2 GLN 3 THR 4 GLU 5 PTR 6 ALA 7 THR 8 ILE 9 VAL 10 PHE 11 PRO stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date . save_ ###################### # Polymer residues # ###################### save_chem_comp_PTR _Saveframe_category polymer_residue _Mol_type 'L-PEPTIDE LINKING' _Name_common O-PHOSPHOTYROSINE _BMRB_code PTR _PDB_code PTR _Standard_residue_derivative . _Molecular_mass 261.168 _Mol_paramagnetic . _Details . loop_ _Atom_name _PDB_atom_name _Atom_type _Atom_chirality _Atom_charge _Atom_oxidation_number _Atom_unpaired_electrons N N N . 0 . ? CA CA C . 0 . ? C C C . 0 . ? O O O . 0 . ? OXT OXT O . 0 . ? CB CB C . 0 . ? CG CG C . 0 . ? CD1 CD1 C . 0 . ? CD2 CD2 C . 0 . ? CE1 CE1 C . 0 . ? CE2 CE2 C . 0 . ? CZ CZ C . 0 . ? OH OH O . 0 . ? P P P . 0 . ? O1P O1P O . 0 . ? O2P O2P O . 0 . ? O3P O3P O . 0 . ? H H H . 0 . ? HN2 HN2 H . 0 . ? HA HA H . 0 . ? HXT HXT H . 0 . ? HB2 HB2 H . 0 . ? HB3 HB3 H . 0 . ? HD1 HD1 H . 0 . ? HD2 HD2 H . 0 . ? HE1 HE1 H . 0 . ? HE2 HE2 H . 0 . ? HO2P HO2P H . 0 . ? HO3P HO3P H . 0 . ? stop_ loop_ _Bond_order _Bond_atom_one_atom_name _Bond_atom_two_atom_name _PDB_bond_atom_one_atom_name _PDB_bond_atom_two_atom_name SING N CA ? ? SING N H ? ? SING N HN2 ? ? SING CA C ? ? SING CA CB ? ? SING CA HA ? ? DOUB C O ? ? SING C OXT ? ? SING OXT HXT ? ? SING CB CG ? ? SING CB HB2 ? ? SING CB HB3 ? ? DOUB CG CD1 ? ? SING CG CD2 ? ? SING CD1 CE1 ? ? SING CD1 HD1 ? ? DOUB CD2 CE2 ? ? SING CD2 HD2 ? ? DOUB CE1 CZ ? ? SING CE1 HE1 ? ? SING CE2 CZ ? ? SING CE2 HE2 ? ? SING CZ OH ? ? SING OH P ? ? DOUB P O1P ? ? SING P O2P ? ? SING P O3P ? ? SING O2P HO2P ? ? SING O3P HO3P ? ? stop_ 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-ITSM_1 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $nSH2 0.8 mM '[U-13C; U-15N]' $ITSM 1.6 mM 'natural abundance' 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_2D_1H-15N_HSQC/HMQC_1 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-15N HSQC/HMQC' _Sample_label $nSH2-ITSM_1 save_ save_3D_HNCACB_2 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCACB' _Sample_label $nSH2-ITSM_1 save_ save_HNCOCACB_(H[N[co[{CA|ca[C]}]]])_3 _Saveframe_category NMR_applied_experiment _Experiment_name 'HNCOCACB (H[N[co[{CA|ca[C]}]]])' _Sample_label $nSH2-ITSM_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 '2D 1H-15N HSQC/HMQC' '3D HNCACB' 'HNCOCACB (H[N[co[{CA|ca[C]}]]])' stop_ loop_ _Sample_label $nSH2-ITSM_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 55.744 . 1 2 3 3 MET CB C 32.701 . 1 3 4 4 ALA H H 8.228 0.004 1 4 4 4 ALA CA C 53.094 0.003 1 5 4 4 ALA CB C 19.128 0.001 1 6 4 4 ALA N N 124.885 0.01 1 7 5 5 SER H H 7.975 0.004 1 8 5 5 SER CA C 58.577 0.021 1 9 5 5 SER CB C 63.656 0.008 1 10 5 5 SER N N 113.654 0.011 1 11 6 6 ARG H H 8.133 0.004 1 12 6 6 ARG CA C 55.178 0.014 1 13 6 6 ARG CB C 29.438 0.001 1 14 6 6 ARG N N 121.102 0.011 1 15 7 7 ARG H H 8.353 0.003 1 16 7 7 ARG CA C 58.105 0.001 1 17 7 7 ARG CB C 29.843 0.044 1 18 7 7 ARG N N 119.449 0.005 1 19 8 8 TRP H H 6.383 0.002 1 20 8 8 TRP CA C 54.562 0.002 1 21 8 8 TRP CB C 29.485 0.015 1 22 8 8 TRP N N 110.898 0.01 1 23 9 9 PHE H H 7.643 0.003 1 24 9 9 PHE CA C 57.018 0.004 1 25 9 9 PHE CB C 39.366 0.021 1 26 9 9 PHE N N 123.936 0.006 1 27 10 10 HIS H H 8.752 0.002 1 28 10 10 HIS CA C 52.437 . 1 29 10 10 HIS CB C 33.406 . 1 30 10 10 HIS N N 129.967 0.003 1 31 11 11 PRO CA C 63.525 . 1 32 11 11 PRO CB C 32.813 . 1 33 12 12 ASN H H 8.467 0.003 1 34 12 12 ASN CA C 53.973 0.002 1 35 12 12 ASN CB C 39.259 0.002 1 36 12 12 ASN N N 113.330 0.009 1 37 13 13 ILE H H 6.813 0.002 1 38 13 13 ILE CA C 60.570 0.002 1 39 13 13 ILE CB C 41.620 0.001 1 40 13 13 ILE N N 113.050 0.009 1 41 14 14 THR H H 8.376 0.003 1 42 14 14 THR CA C 60.211 0.024 1 43 14 14 THR CB C 71.739 0.012 1 44 14 14 THR N N 112.907 0.009 1 45 15 15 GLY H H 9.418 0.003 1 46 15 15 GLY CA C 48.002 0.0 1 47 15 15 GLY N N 109.516 0.009 1 48 16 16 VAL H H 7.959 0.003 1 49 16 16 VAL CA C 65.884 0.008 1 50 16 16 VAL CB C 31.933 0.005 1 51 16 16 VAL N N 120.582 0.012 1 52 17 17 GLU H H 7.479 0.002 1 53 17 17 GLU CA C 59.282 0.004 1 54 17 17 GLU CB C 29.958 0.001 1 55 17 17 GLU N N 120.880 0.007 1 56 18 18 ALA H H 8.660 0.002 1 57 18 18 ALA CA C 55.167 0.006 1 58 18 18 ALA CB C 18.931 0.0 1 59 18 18 ALA N N 121.294 0.004 1 60 19 19 GLU H H 8.301 0.003 1 61 19 19 GLU CA C 60.301 0.003 1 62 19 19 GLU CB C 28.625 0.012 1 63 19 19 GLU N N 116.881 0.002 1 64 20 20 ASN H H 7.704 0.004 1 65 20 20 ASN CA C 57.035 0.0 1 66 20 20 ASN CB C 38.798 0.003 1 67 20 20 ASN N N 116.057 0.005 1 68 21 21 LEU H H 8.481 0.002 1 69 21 21 LEU CA C 58.451 0.001 1 70 21 21 LEU CB C 42.728 0.004 1 71 21 21 LEU N N 121.866 0.007 1 72 22 22 LEU H H 8.327 0.002 1 73 22 22 LEU CA C 58.199 0.024 1 74 22 22 LEU CB C 42.509 0.021 1 75 22 22 LEU N N 118.600 0.002 1 76 23 23 LEU H H 8.380 0.002 1 77 23 23 LEU CA C 56.943 0.01 1 78 23 23 LEU CB C 41.289 0.003 1 79 23 23 LEU N N 117.072 0.006 1 80 24 24 THR H H 7.739 0.003 1 81 24 24 THR CA C 63.730 0.002 1 82 24 24 THR CB C 70.562 0.002 1 83 24 24 THR N N 109.170 0.008 1 84 25 25 ARG H H 8.460 0.002 1 85 25 25 ARG CA C 55.725 0.0 1 86 25 25 ARG CB C 31.946 0.006 1 87 25 25 ARG N N 118.967 0.008 1 88 26 26 GLY H H 7.061 0.003 1 89 26 26 GLY CA C 43.853 0.001 1 90 26 26 GLY N N 106.790 0.007 1 91 27 27 VAL H H 8.956 0.003 1 92 27 27 VAL CA C 59.126 0.01 1 93 27 27 VAL CB C 35.984 0.01 1 94 27 27 VAL N N 109.949 0.004 1 95 28 28 ASP H H 8.951 0.003 1 96 28 28 ASP CA C 57.866 0.003 1 97 28 28 ASP CB C 39.035 0.0 1 98 28 28 ASP N N 123.049 0.008 1 99 29 29 GLY H H 8.721 0.003 1 100 29 29 GLY CA C 44.886 0.01 1 101 29 29 GLY N N 113.140 0.008 1 102 30 30 SER H H 9.390 0.003 1 103 30 30 SER CA C 60.753 0.006 1 104 30 30 SER CB C 64.385 0.007 1 105 30 30 SER N N 122.559 0.004 1 106 31 31 PHE H H 8.145 0.002 1 107 31 31 PHE CA C 55.793 0.001 1 108 31 31 PHE CB C 44.246 0.007 1 109 31 31 PHE N N 116.768 0.005 1 110 32 32 LEU H H 9.259 0.003 1 111 32 32 LEU CA C 54.198 0.004 1 112 32 32 LEU CB C 45.009 0.002 1 113 32 32 LEU N N 115.182 0.014 1 114 33 33 ALA H H 9.605 0.003 1 115 33 33 ALA CA C 50.016 0.002 1 116 33 33 ALA CB C 23.482 0.002 1 117 33 33 ALA N N 121.910 0.009 1 118 34 34 ARG H H 9.229 0.003 1 119 34 34 ARG CA C 54.100 . 1 120 34 34 ARG CB C 30.126 . 1 121 34 34 ARG N N 117.316 0.005 1 122 35 35 PRO CA C 63.291 . 1 123 35 35 PRO CB C 32.510 . 1 124 36 36 SER H H 7.740 0.001 1 125 36 36 SER CA C 57.757 0.003 1 126 36 36 SER CB C 64.050 0.025 1 127 36 36 SER N N 116.777 0.008 1 128 37 37 LYS H H 9.943 0.003 1 129 37 37 LYS CA C 57.178 0.048 1 130 37 37 LYS CB C 33.167 0.016 1 131 37 37 LYS N N 131.303 0.006 1 132 38 38 SER H H 9.205 0.003 1 133 38 38 SER CA C 61.035 0.0 1 134 38 38 SER CB C 62.966 0.002 1 135 38 38 SER N N 116.482 0.011 1 136 39 39 ASN H H 8.146 0.003 1 137 39 39 ASN CA C 50.570 . 1 138 39 39 ASN CB C 39.426 . 1 139 39 39 ASN N N 121.586 0.005 1 140 40 40 PRO CA C 64.495 . 1 141 40 40 PRO CB C 31.550 . 1 142 41 41 GLY H H 8.929 0.003 1 143 41 41 GLY CA C 45.440 0.005 1 144 41 41 GLY N N 115.778 0.006 1 145 42 42 ASP H H 8.082 0.003 1 146 42 42 ASP CA C 53.764 0.0 1 147 42 42 ASP CB C 41.869 0.008 1 148 42 42 ASP N N 119.509 0.005 1 149 43 43 PHE H H 8.885 0.002 1 150 43 43 PHE CA C 57.086 0.004 1 151 43 43 PHE CB C 44.484 0.003 1 152 43 43 PHE N N 117.011 0.006 1 153 44 44 THR H H 9.663 0.003 1 154 44 44 THR CA C 62.132 0.006 1 155 44 44 THR CB C 72.953 0.005 1 156 44 44 THR N N 117.448 0.012 1 157 45 45 LEU H H 9.556 0.003 1 158 45 45 LEU CA C 53.447 0.002 1 159 45 45 LEU CB C 45.184 0.006 1 160 45 45 LEU N N 126.107 0.008 1 161 46 46 SER H H 9.271 0.002 1 162 46 46 SER CA C 58.841 0.008 1 163 46 46 SER CB C 65.080 0.004 1 164 46 46 SER N N 122.049 0.006 1 165 47 47 VAL H H 9.049 0.002 1 166 47 47 VAL CA C 60.013 0.002 1 167 47 47 VAL CB C 35.873 0.003 1 168 47 47 VAL N N 123.667 0.005 1 169 48 48 ARG H H 9.244 0.003 1 170 48 48 ARG CA C 54.739 0.002 1 171 48 48 ARG CB C 31.788 0.001 1 172 48 48 ARG N N 127.507 0.006 1 173 49 49 ARG H H 9.453 0.003 1 174 49 49 ARG CA C 55.402 0.01 1 175 49 49 ARG CB C 32.208 0.029 1 176 49 49 ARG N N 130.466 0.004 1 177 50 50 ASN H H 9.309 0.003 1 178 50 50 ASN CA C 54.451 0.007 1 179 50 50 ASN CB C 37.515 0.0 1 180 50 50 ASN N N 124.892 0.007 1 181 51 51 GLY H H 9.536 0.003 1 182 51 51 GLY CA C 46.042 0.003 1 183 51 51 GLY N N 106.094 0.009 1 184 52 52 ALA H H 7.999 0.003 1 185 52 52 ALA CA C 50.468 0.005 1 186 52 52 ALA CB C 22.134 0.001 1 187 52 52 ALA N N 123.060 0.009 1 188 53 53 VAL H H 8.637 0.002 1 189 53 53 VAL CA C 61.213 0.001 1 190 53 53 VAL CB C 34.064 0.003 1 191 53 53 VAL N N 119.694 0.006 1 192 54 54 THR H H 8.934 0.002 1 193 54 54 THR CA C 60.475 0.012 1 194 54 54 THR CB C 71.090 0.001 1 195 54 54 THR N N 124.453 0.002 1 196 55 55 HIS H H 8.444 0.003 1 197 55 55 HIS CA C 54.627 0.007 1 198 55 55 HIS CB C 33.514 0.002 1 199 55 55 HIS N N 124.600 0.011 1 200 56 56 ILE H H 9.773 0.002 1 201 56 56 ILE CA C 60.319 0.001 1 202 56 56 ILE CB C 42.357 0.028 1 203 56 56 ILE N N 123.558 0.004 1 204 57 57 LYS H H 9.027 0.002 1 205 57 57 LYS CA C 58.581 0.001 1 206 57 57 LYS CB C 34.073 0.006 1 207 57 57 LYS N N 127.749 0.005 1 208 58 58 ILE H H 8.808 0.002 1 209 58 58 ILE CA C 60.226 0.016 1 210 58 58 ILE CB C 39.842 0.002 1 211 58 58 ILE N N 121.268 0.009 1 212 59 59 GLN H H 8.707 0.003 1 213 59 59 GLN CA C 55.753 0.003 1 214 59 59 GLN CB C 28.082 0.003 1 215 59 59 GLN N N 129.105 0.012 1 216 60 60 ASN H H 8.296 0.003 1 217 60 60 ASN CA C 50.492 0.001 1 218 60 60 ASN CB C 40.019 0.002 1 219 60 60 ASN N N 122.917 0.006 1 220 61 61 THR H H 8.026 0.002 1 221 61 61 THR CA C 61.505 0.003 1 222 61 61 THR CB C 70.026 0.001 1 223 61 61 THR N N 113.623 0.006 1 224 62 62 GLY H H 7.993 0.003 1 225 62 62 GLY CA C 45.671 0.005 1 226 62 62 GLY N N 112.979 0.008 1 227 63 63 ASP H H 7.410 0.003 1 228 63 63 ASP CA C 54.662 0.004 1 229 63 63 ASP CB C 42.963 0.002 1 230 63 63 ASP N N 117.129 0.002 1 231 64 64 TYR H H 7.167 0.003 1 232 64 64 TYR CA C 56.787 0.006 1 233 64 64 TYR CB C 39.950 0.001 1 234 64 64 TYR N N 114.013 0.007 1 235 65 65 TYR H H 9.659 0.002 1 236 65 65 TYR CA C 56.011 0.001 1 237 65 65 TYR CB C 41.998 0.006 1 238 65 65 TYR N N 117.835 0.007 1 239 66 66 ASP H H 9.088 0.003 1 240 66 66 ASP CA C 53.777 0.007 1 241 66 66 ASP CB C 42.491 0.006 1 242 66 66 ASP N N 121.053 0.006 1 243 67 67 LEU H H 7.408 0.002 1 244 67 67 LEU CA C 53.061 0.005 1 245 67 67 LEU CB C 40.500 0.0 1 246 67 67 LEU N N 118.192 0.005 1 247 68 68 TYR H H 8.433 0.002 1 248 68 68 TYR CA C 61.706 0.004 1 249 68 68 TYR CB C 34.451 0.006 1 250 68 68 TYR N N 115.904 0.008 1 251 69 69 GLY H H 6.765 0.003 1 252 69 69 GLY CA C 43.827 0.003 1 253 69 69 GLY N N 104.280 0.019 1 254 70 70 GLY H H 7.995 0.003 1 255 70 70 GLY CA C 44.447 0.003 1 256 70 70 GLY N N 107.052 0.005 1 257 71 71 GLU H H 8.285 0.003 1 258 71 71 GLU CA C 56.399 0.012 1 259 71 71 GLU CB C 30.095 0.005 1 260 71 71 GLU N N 122.174 0.006 1 261 72 72 LYS H H 7.616 0.003 1 262 72 72 LYS CA C 54.820 0.005 1 263 72 72 LYS CB C 35.289 0.004 1 264 72 72 LYS N N 118.668 0.007 1 265 73 73 PHE H H 9.135 0.002 1 266 73 73 PHE CA C 57.045 0.003 1 267 73 73 PHE CB C 44.502 0.006 1 268 73 73 PHE N N 117.671 0.007 1 269 74 74 ALA H H 9.389 0.002 1 270 74 74 ALA CA C 54.506 0.001 1 271 74 74 ALA CB C 19.928 0.001 1 272 74 74 ALA N N 122.911 0.002 1 273 75 75 THR H H 7.188 0.002 1 274 75 75 THR CA C 58.895 0.01 1 275 75 75 THR CB C 73.537 0.003 1 276 75 75 THR N N 101.874 0.006 1 277 76 76 LEU H H 7.867 0.002 1 278 76 76 LEU CA C 57.048 0.004 1 279 76 76 LEU CB C 41.221 0.005 1 280 76 76 LEU N N 122.405 0.004 1 281 77 77 ALA H H 8.441 0.003 1 282 77 77 ALA CA C 55.523 0.009 1 283 77 77 ALA CB C 18.142 0.002 1 284 77 77 ALA N N 118.817 0.005 1 285 78 78 GLU H H 7.727 0.003 1 286 78 78 GLU CA C 59.444 0.006 1 287 78 78 GLU CB C 31.063 0.005 1 288 78 78 GLU N N 116.802 0.004 1 289 79 79 LEU H H 6.914 0.002 1 290 79 79 LEU CA C 58.554 0.001 1 291 79 79 LEU CB C 41.735 0.003 1 292 79 79 LEU N N 122.609 0.008 1 293 80 80 VAL H H 7.875 0.003 1 294 80 80 VAL CA C 67.469 0.002 1 295 80 80 VAL CB C 31.551 0.001 1 296 80 80 VAL N N 118.856 0.007 1 297 81 81 GLN H H 7.998 0.002 1 298 81 81 GLN CA C 59.167 0.01 1 299 81 81 GLN CB C 28.083 0.002 1 300 81 81 GLN N N 117.297 0.01 1 301 82 82 TYR H H 7.838 0.002 1 302 82 82 TYR CA C 62.270 0.0 1 303 82 82 TYR CB C 39.110 0.01 1 304 82 82 TYR N N 118.386 0.005 1 305 83 83 TYR H H 7.820 0.002 1 306 83 83 TYR CA C 62.777 0.001 1 307 83 83 TYR CB C 38.007 0.003 1 308 83 83 TYR N N 117.222 0.01 1 309 84 84 MET H H 8.239 0.002 1 310 84 84 MET CA C 59.231 0.005 1 311 84 84 MET CB C 34.180 0.002 1 312 84 84 MET N N 119.872 0.006 1 313 85 85 GLU H H 7.480 0.002 1 314 85 85 GLU CA C 57.057 0.001 1 315 85 85 GLU CB C 30.643 0.01 1 316 85 85 GLU N N 115.196 0.004 1 317 86 86 HIS H H 7.506 0.003 1 318 86 86 HIS CA C 54.864 0.053 1 319 86 86 HIS CB C 27.033 0.012 1 320 86 86 HIS N N 118.259 0.009 1 321 87 87 HIS H H 8.140 0.004 1 322 87 87 HIS CA C 57.421 . 1 323 87 87 HIS CB C 30.758 . 1 324 87 87 HIS N N 122.355 0.007 1 325 88 88 GLY CA C 45.744 . 1 326 89 89 GLN H H 7.900 0.003 1 327 89 89 GLN CA C 56.274 0.002 1 328 89 89 GLN CB C 29.442 0.004 1 329 89 89 GLN N N 116.044 0.004 1 330 90 90 LEU H H 8.220 0.003 1 331 90 90 LEU CA C 53.526 0.006 1 332 90 90 LEU CB C 42.539 0.004 1 333 90 90 LEU N N 120.964 0.008 1 334 91 91 LYS H H 8.066 0.003 1 335 91 91 LYS CA C 54.667 0.008 1 336 91 91 LYS CB C 35.910 0.009 1 337 91 91 LYS N N 123.978 0.002 1 338 92 92 GLU H H 8.403 0.003 1 339 92 92 GLU CA C 55.737 0.001 1 340 92 92 GLU CB C 31.967 0.008 1 341 92 92 GLU N N 121.109 0.006 1 342 93 93 LYS H H 8.606 0.003 1 343 93 93 LYS CA C 59.444 . 1 344 93 93 LYS CB C 32.476 . 1 345 93 93 LYS N N 123.782 0.012 1 346 94 94 ASN CA C 53.469 . 1 347 94 94 ASN CB C 37.546 . 1 348 95 95 GLY H H 8.150 0.003 1 349 95 95 GLY CA C 45.016 0.002 1 350 95 95 GLY N N 108.715 0.008 1 351 96 96 ASP H H 8.298 0.003 1 352 96 96 ASP CA C 54.577 0.0 1 353 96 96 ASP CB C 41.302 0.004 1 354 96 96 ASP N N 122.586 0.006 1 355 97 97 VAL H H 8.292 0.003 1 356 97 97 VAL CA C 61.908 0.011 1 357 97 97 VAL CB C 33.518 0.0 1 358 97 97 VAL N N 119.449 0.003 1 359 98 98 ILE H H 8.411 0.003 1 360 98 98 ILE CA C 60.732 0.001 1 361 98 98 ILE CB C 38.649 0.0 1 362 98 98 ILE N N 127.712 0.005 1 363 99 99 GLU H H 8.308 0.003 1 364 99 99 GLU CA C 54.781 0.002 1 365 99 99 GLU CB C 32.182 0.003 1 366 99 99 GLU N N 125.131 0.003 1 367 100 100 LEU H H 8.769 0.002 1 368 100 100 LEU CA C 53.313 0.007 1 369 100 100 LEU CB C 40.022 0.004 1 370 100 100 LEU N N 125.351 0.004 1 371 101 101 LYS H H 8.102 0.003 1 372 101 101 LYS CA C 58.482 0.001 1 373 101 101 LYS CB C 34.560 0.006 1 374 101 101 LYS N N 120.240 0.004 1 375 102 102 TYR H H 7.801 0.002 1 376 102 102 TYR CA C 52.735 . 1 377 102 102 TYR CB C 40.708 . 1 378 102 102 TYR N N 116.517 0.004 1 379 103 103 PRO CA C 62.656 . 1 380 103 103 PRO CB C 32.060 . 1 381 104 104 LEU H H 8.784 0.002 1 382 104 104 LEU CA C 54.420 0.002 1 383 104 104 LEU CB C 41.893 0.001 1 384 104 104 LEU N N 128.558 0.005 1 385 105 105 ASN H H 8.555 0.002 1 386 105 105 ASN CA C 53.392 0.0 1 387 105 105 ASN CB C 39.140 0.002 1 388 105 105 ASN N N 125.839 0.01 1 389 106 106 CYS H H 8.635 0.002 1 390 106 106 CYS CA C 59.049 0.004 1 391 106 106 CYS CB C 27.165 0.001 1 392 106 106 CYS N N 121.843 0.003 1 393 107 107 ALA H H 8.063 0.002 1 394 107 107 ALA CA C 54.027 . 1 395 107 107 ALA CB C 20.240 . 1 396 107 107 ALA N N 133.307 0.002 1 stop_ save_