data_16470 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Backbone 1H, 13C, and 15N Chemical Shift Assignments for ShcA PTB Domain ; _BMRB_accession_number 16470 _BMRB_flat_file_name bmr16470.str _Entry_type original _Submission_date 2009-08-27 _Accession_date 2009-08-27 _Entry_origination author _NMR_STAR_version 2.1.1 _Experimental_method NMR _Details 'Bound to PTP-PEST NPLH peptide' loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Smith Matthew J. . 2 Ikura Mitsu . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 153 "13C chemical shifts" 264 "15N chemical shifts" 153 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2010-03-05 update BMRB 'completed entry citation' 2010-01-28 original BMRB 'original release' stop_ save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title 'The PTB domain of ShcA couples receptor activation to the cytoskeletal regulator IQGAP1.' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 20075861 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Smith Matthew J. . 2 Hardy 'W. Rod' . . 3 Li Guang-Yao . . 4 Goudreault Marilyn . . 5 Hersch Steven . . 6 Metalnikov Pavel . . 7 Starostine Andrei . . 8 Pawson Tony . . 9 Ikura Mitsuhiko . . stop_ _Journal_abbreviation 'EMBO J.' _Journal_name_full 'The EMBO journal' _Journal_volume 29 _Journal_issue 5 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 884 _Page_last 896 _Year 2010 _Details . loop_ _Keyword ErbB2 IQGAP1 'PTB Domain' PTP-PEST ShcA stop_ save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name 'ShcA PTB domain-NPLH peptide' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'peptide ligand' $PTP-PEST_peptide 'binding domain' $ShcA_PTB_domain stop_ _System_molecular_weight 22635 _System_physical_state native _System_oligomer_state ? _System_paramagnetic no _System_thiol_state . _Database_query_date . _Details 'NPLH peptide bound to isotopically labeled ShcA PTB domain' save_ ######################## # Monomeric polymers # ######################## save_PTP-PEST_peptide _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common PTP-PEST_peptide _Molecular_mass 1665.7 _Mol_thiol_state 'not present' loop_ _Biological_function phosphatase stop_ _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 14 _Mol_residue_sequence PLSFTNPLHSDDWH loop_ _Residue_seq_code _Residue_label 1 PRO 2 LEU 3 SER 4 PHE 5 THR 6 ASN 7 PRO 8 LEU 9 HIS 10 SER 11 ASP 12 ASP 13 TRP 14 HIS stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date . 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 SWS P35831 PTP-PEST . . . . . stop_ save_ save_ShcA_PTB_domain _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common ShcA_PTB_domain _Molecular_mass 20969 _Mol_thiol_state unknown loop_ _Biological_function 'adaptor protein' stop_ _Details . _Residue_count 191 _Mol_residue_sequence ; GQLGGEEWTRHGSFVNKPTR GWLHPNDKVMGPGVSYLVRY MGCVEVLQSMRALDFNTRTQ VTREAISLVCEAVPGAKGAT RRRKPCSRPLSSILGRSNLK FAGMPITLTVSTSSLNLMAA DCKQIIANHHMQSISFASGG DPDTAEYVAYVAKDPVNQRA CHILECPEGLAQDVISTIGQ AFELRFKQYLR ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 17 GLY 2 18 GLN 3 19 LEU 4 20 GLY 5 21 GLY 6 22 GLU 7 23 GLU 8 24 TRP 9 25 THR 10 26 ARG 11 27 HIS 12 28 GLY 13 29 SER 14 30 PHE 15 31 VAL 16 32 ASN 17 33 LYS 18 34 PRO 19 35 THR 20 36 ARG 21 37 GLY 22 38 TRP 23 39 LEU 24 40 HIS 25 41 PRO 26 42 ASN 27 43 ASP 28 44 LYS 29 45 VAL 30 46 MET 31 47 GLY 32 48 PRO 33 49 GLY 34 50 VAL 35 51 SER 36 52 TYR 37 53 LEU 38 54 VAL 39 55 ARG 40 56 TYR 41 57 MET 42 58 GLY 43 59 CYS 44 60 VAL 45 61 GLU 46 62 VAL 47 63 LEU 48 64 GLN 49 65 SER 50 66 MET 51 67 ARG 52 68 ALA 53 69 LEU 54 70 ASP 55 71 PHE 56 72 ASN 57 73 THR 58 74 ARG 59 75 THR 60 76 GLN 61 77 VAL 62 78 THR 63 79 ARG 64 80 GLU 65 81 ALA 66 82 ILE 67 83 SER 68 84 LEU 69 85 VAL 70 86 CYS 71 87 GLU 72 88 ALA 73 89 VAL 74 90 PRO 75 91 GLY 76 92 ALA 77 93 LYS 78 94 GLY 79 95 ALA 80 96 THR 81 97 ARG 82 98 ARG 83 99 ARG 84 100 LYS 85 101 PRO 86 102 CYS 87 103 SER 88 104 ARG 89 105 PRO 90 106 LEU 91 107 SER 92 108 SER 93 109 ILE 94 110 LEU 95 111 GLY 96 112 ARG 97 113 SER 98 114 ASN 99 115 LEU 100 116 LYS 101 117 PHE 102 118 ALA 103 119 GLY 104 120 MET 105 121 PRO 106 122 ILE 107 123 THR 108 124 LEU 109 125 THR 110 126 VAL 111 127 SER 112 128 THR 113 129 SER 114 130 SER 115 131 LEU 116 132 ASN 117 133 LEU 118 134 MET 119 135 ALA 120 136 ALA 121 137 ASP 122 138 CYS 123 139 LYS 124 140 GLN 125 141 ILE 126 142 ILE 127 143 ALA 128 144 ASN 129 145 HIS 130 146 HIS 131 147 MET 132 148 GLN 133 149 SER 134 150 ILE 135 151 SER 136 152 PHE 137 153 ALA 138 154 SER 139 155 GLY 140 156 GLY 141 157 ASP 142 158 PRO 143 159 ASP 144 160 THR 145 161 ALA 146 162 GLU 147 163 TYR 148 164 VAL 149 165 ALA 150 166 TYR 151 167 VAL 152 168 ALA 153 169 LYS 154 170 ASP 155 171 PRO 156 172 VAL 157 173 ASN 158 174 GLN 159 175 ARG 160 176 ALA 161 177 CYS 162 178 HIS 163 179 ILE 164 180 LEU 165 181 GLU 166 182 CYS 167 183 PRO 168 184 GLU 169 185 GLY 170 186 LEU 171 187 ALA 172 188 GLN 173 189 ASP 174 190 VAL 175 191 ILE 176 192 SER 177 193 THR 178 194 ILE 179 195 GLY 180 196 GLN 181 197 ALA 182 198 PHE 183 199 GLU 184 200 LEU 185 201 ARG 186 202 PHE 187 203 LYS 188 204 GLN 189 205 TYR 190 206 LEU 191 207 ARG stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-01-30 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 17080 Shc-PTB 100.00 211 100.00 100.00 6.02e-140 BMRB 5566 Shc_PTB_Domain 100.00 207 100.00 100.00 4.95e-140 PDB 1N3H "Coupling Of Folding And Binding In The Ptb Domain Of The Signaling Protein Shc" 100.00 207 100.00 100.00 4.95e-140 PDB 1OY2 "Coupling Of Folding And Binding In The Ptb Domain Of The Signaling Protein Shc" 100.00 207 100.00 100.00 4.95e-140 PDB 1SHC "Shc Ptb Domain Complexed With A Trka Receptor Phosphopeptide, Nmr, Minimized Average Structure" 100.00 195 100.00 100.00 3.58e-140 PDB 2L1C "Shc-Ptb:biphosphorylated Integrin Beta3 Cytoplasmic Tail Complex (1:1)" 100.00 211 100.00 100.00 6.02e-140 DBJ BAA74950 "shc transforming protein [Rattus norvegicus]" 72.25 138 100.00 100.00 8.52e-96 DBJ BAC33706 "unnamed protein product [Mus musculus]" 100.00 469 100.00 100.00 8.91e-136 DBJ BAD92086 "SHC (Src homology 2 domain containing) transforming protein 1 isoform p66Shc variant [Homo sapiens]" 50.26 377 100.00 100.00 2.15e-59 DBJ BAE33083 "unnamed protein product [Mus musculus]" 100.00 579 100.00 100.00 3.23e-135 DBJ BAF84832 "unnamed protein product [Homo sapiens]" 100.00 474 100.00 100.00 5.68e-136 EMBL CAA48251 "SHC transforming protein [Homo sapiens]" 100.00 473 100.00 100.00 6.14e-136 EMBL CAA70977 "shc p66 [Homo sapiens]" 100.00 583 100.00 100.00 3.12e-135 EMBL CAH92143 "hypothetical protein [Pongo abelii]" 100.00 583 100.00 100.00 4.05e-135 GB AAA91777 "src homology collagen protein 66 kDa isoform [Mus musculus]" 100.00 579 100.00 100.00 3.23e-135 GB AAB49972 "p66shc [Homo sapiens]" 100.00 583 100.00 100.00 3.09e-135 GB AAC52146 "Shcp52 [Mus musculus]" 100.00 469 100.00 100.00 8.91e-136 GB AAH14158 "SHC (Src homology 2 domain containing) transforming protein 1 [Homo sapiens]" 100.00 474 100.00 100.00 5.68e-136 GB AAH33925 "SHC1 protein [Homo sapiens]" 50.26 369 100.00 100.00 2.62e-59 REF NP_001068773 "SHC-transforming protein 1 isoform b [Bos taurus]" 100.00 473 100.00 100.00 3.60e-136 REF NP_001106802 "SHC-transforming protein 1 isoform a [Mus musculus]" 100.00 579 100.00 100.00 3.23e-135 REF NP_001123512 "SHC-transforming protein 1 isoform 3 [Homo sapiens]" 100.00 584 100.00 100.00 3.43e-135 REF NP_001123513 "SHC-transforming protein 1 isoform 4 [Homo sapiens]" 100.00 473 100.00 100.00 6.14e-136 REF NP_001126253 "SHC-transforming protein 1 [Pongo abelii]" 100.00 583 100.00 100.00 4.05e-135 SP P29353 "RecName: Full=SHC-transforming protein 1; AltName: Full=SHC-transforming protein 3; AltName: Full=SHC-transforming protein A; A" 100.00 583 100.00 100.00 3.33e-135 SP P98083 "RecName: Full=SHC-transforming protein 1; AltName: Full=SHC-transforming protein A; AltName: Full=Src homology 2 domain-contain" 100.00 579 100.00 100.00 3.23e-135 SP Q0IIE2 "RecName: Full=SHC-transforming protein 1; AltName: Full=Src homology 2 domain-containing-transforming protein C1; Short=SH2 dom" 100.00 473 100.00 100.00 3.60e-136 SP Q5M824 "RecName: Full=SHC-transforming protein 1; AltName: Full=Src homology 2 domain-containing-transforming protein C1; Short=SH2 dom" 100.00 469 99.48 99.48 4.45e-135 SP Q5R7W7 "RecName: Full=SHC-transforming protein 1; AltName: Full=Src homology 2 domain-containing-transforming protein C1; Short=SH2 dom" 100.00 583 100.00 100.00 4.05e-135 TPG DAA31779 "TPA: SHC-transforming protein 1 isoform b [Bos taurus]" 100.00 473 100.00 100.00 3.60e-136 TPG DAA31780 "TPA: SHC-transforming protein 1 isoform a [Bos taurus]" 100.00 583 100.00 100.00 1.30e-135 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $ShcA_PTB_domain Mouse 10090 Eukaryota Metazoa Mus musculus 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 $ShcA_PTB_domain 'recombinant technology' . Escherichia coli . pET15b stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Saveframe_category sample _Sample_type solution _Details 'ShcA PTB domain-PTP-PEST peptide' loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $ShcA_PTB_domain 200 uM '[U-13C; U-15N]' $PTP-PEST_peptide 2 mM 'natural abundance' D2O 10 % 'natural abundance' H2O 90 % 'natural abundance' NaCl 100 mM 'natural abundance' stop_ save_ ############################ # Computer software used # ############################ save_NMRPipe _Saveframe_category software _Name NMRPipe _Version . loop_ _Vendor _Address _Electronic_address 'Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax' . . stop_ loop_ _Task processing stop_ _Details . save_ save_NMRView _Saveframe_category software _Name NMRView _Version . loop_ _Vendor _Address _Electronic_address 'Johnson, One Moon Scientific' . . stop_ loop_ _Task 'chemical shift assignment' stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model Avance _Field_strength 800 _Details . save_ ############################# # NMR applied experiments # ############################# save_2D_1H-15N_HSQC_1 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-15N HSQC' _Sample_label $sample_1 save_ save_3D_CBCA(CO)NH_2 _Saveframe_category NMR_applied_experiment _Experiment_name '3D CBCA(CO)NH' _Sample_label $sample_1 save_ save_3D_HNCA_3 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCA' _Sample_label $sample_1 save_ save_3D_HNCACB_4 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCACB' _Sample_label $sample_1 save_ ####################### # Sample conditions # ####################### save_sample_conditions_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units 'ionic strength' 150 . mM pH 7.5 . pH pressure 1 . atm temperature 303 . K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference_1 _Saveframe_category chemical_shift_reference _Details . loop_ _Mol_common_name _Atom_type _Atom_isotope_number _Atom_group _Chem_shift_units _Chem_shift_value _Reference_method _Reference_type _External_reference_sample_geometry _External_reference_location _External_reference_axis _Indirect_shift_ratio DSS C 13 'methyl protons' ppm 0.00 . indirect . . . 0.251449530 DSS H 1 'methyl protons' ppm 0.00 internal direct . . . 1.000000000 DSS N 15 'methyl protons' ppm 0.00 . indirect . . . 0.101329118 stop_ save_ ################################### # Assigned chemical shift lists # ################################### ################################################################### # Chemical Shift Ambiguity Index Value Definitions # # # # The values other than 1 are used for those atoms with different # # chemical shifts that cannot be assigned to stereospecific atoms # # or to specific residues or chains. # # # # Index Value Definition # # # # 1 Unique (including isolated methyl protons, # # geminal atoms, and geminal methyl # # groups with identical chemical shifts) # # (e.g. ILE HD11, HD12, HD13 protons) # # 2 Ambiguity of geminal atoms or geminal methyl # # proton groups (e.g. ASP HB2 and HB3 # # protons, LEU CD1 and CD2 carbons, or # # LEU HD11, HD12, HD13 and HD21, HD22, # # HD23 methyl protons) # # 3 Aromatic atoms on opposite sides of # # symmetrical rings (e.g. TYR HE1 and HE2 # # protons) # # 4 Intraresidue ambiguities (e.g. LYS HG and # # HD protons or TRP HZ2 and HZ3 protons) # # 5 Interresidue ambiguities (LYS 12 vs. LYS 27) # # 6 Intermolecular ambiguities (e.g. ASP 31 CA # # in monomer 1 and ASP 31 CA in monomer 2 # # of an asymmetrical homodimer, duplex # # DNA assignments, or other assignments # # that may apply to atoms in one or more # # molecule in the molecular assembly) # # 9 Ambiguous, specific ambiguity not defined # # # ################################################################### save_assigned_chem_shift_list_1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Experiment_label '2D 1H-15N HSQC' '3D CBCA(CO)NH' '3D HNCA' '3D HNCACB' 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 'binding domain' _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 17 1 GLY H H 8.449 . 1 2 17 1 GLY CA C 45.42 . 1 3 17 1 GLY N N 110.05 . 1 4 18 2 GLN H H 8.234 . 1 5 18 2 GLN CA C 56.19 . 1 6 18 2 GLN CB C 29.5 . 1 7 18 2 GLN N N 119.782 . 1 8 19 3 LEU H H 8.354 . 1 9 19 3 LEU CA C 55.72 . 1 10 19 3 LEU CB C 42.4 . 1 11 19 3 LEU N N 123.106 . 1 12 20 4 GLY H H 8.408 . 1 13 20 4 GLY CA C 45.49 . 1 14 20 4 GLY N N 109.712 . 1 15 21 5 GLY H H 8.245 . 1 16 21 5 GLY CA C 45.42 . 1 17 21 5 GLY N N 108.775 . 1 18 22 6 GLU H H 8.458 . 1 19 22 6 GLU CA C 57.28 . 1 20 22 6 GLU CB C 29.89 . 1 21 22 6 GLU N N 119.835 . 1 22 23 7 GLU H H 8.125 . 1 23 23 7 GLU N N 126.43 . 1 24 25 9 THR H H 7.675 . 1 25 25 9 THR N N 119.65 . 1 26 28 12 GLY H H 8.214 . 1 27 28 12 GLY CA C 46.12 . 1 28 28 12 GLY N N 109.29 . 1 29 31 15 VAL H H 8.058 . 1 30 31 15 VAL CA C 59.93 . 1 31 31 15 VAL CB C 32.62 . 1 32 31 15 VAL N N 122.237 . 1 33 32 16 ASN H H 7.777 . 1 34 32 16 ASN N N 117.43 . 1 35 37 21 GLY H H 7.744 . 1 36 37 21 GLY CA C 43.86 . 1 37 37 21 GLY N N 107.96 . 1 38 38 22 TRP H H 8.021 . 1 39 38 22 TRP CA C 55.56 . 1 40 38 22 TRP CB C 30.44 . 1 41 38 22 TRP N N 117.436 . 1 42 39 23 LEU H H 8.967 . 1 43 39 23 LEU CA C 56.19 . 1 44 39 23 LEU CB C 43.08 . 1 45 39 23 LEU N N 119.301 . 1 46 40 24 HIS H H 7.054 . 1 47 40 24 HIS CA C 53.77 . 1 48 40 24 HIS CB C 32.15 . 1 49 40 24 HIS N N 114.8 . 1 50 42 26 ASN H H 8.661 . 1 51 42 26 ASN CA C 56.73 . 1 52 42 26 ASN CB C 37.79 . 1 53 42 26 ASN N N 121.777 . 1 54 43 27 ASP H H 8.776 . 1 55 43 27 ASP CA C 56.59 . 1 56 43 27 ASP CB C 39.65 . 1 57 43 27 ASP N N 115.33 . 1 58 44 28 LYS H H 7.226 . 1 59 44 28 LYS CA C 58.61 . 1 60 44 28 LYS CB C 33.01 . 1 61 44 28 LYS N N 119.389 . 1 62 45 29 VAL H H 6.931 . 1 63 45 29 VAL CA C 66.25 . 1 64 45 29 VAL CB C 31.61 . 1 65 45 29 VAL N N 118.11 . 1 66 46 30 MET H H 7.824 . 1 67 46 30 MET CA C 56.58 . 1 68 46 30 MET CB C 34.42 . 1 69 46 30 MET N N 113.52 . 1 70 47 31 GLY H H 7.138 . 1 71 47 31 GLY CA C 43.63 . 1 72 47 31 GLY N N 107.31 . 1 73 49 33 GLY H H 7.949 . 1 74 49 33 GLY CA C 44.48 . 1 75 49 33 GLY N N 106.67 . 1 76 50 34 VAL H H 8.307 . 1 77 50 34 VAL CA C 61.49 . 1 78 50 34 VAL CB C 33.87 . 1 79 50 34 VAL N N 118.155 . 1 80 51 35 SER H H 8.172 . 1 81 51 35 SER CA C 57.28 . 1 82 51 35 SER CB C 66.02 . 1 83 51 35 SER N N 121.03 . 1 84 52 36 TYR H H 9.26 . 1 85 52 36 TYR CA C 57.05 . 1 86 52 36 TYR CB C 44.17 . 1 87 52 36 TYR N N 120.29 . 1 88 53 37 LEU H H 8.57 . 1 89 53 37 LEU CA C 54.86 . 1 90 53 37 LEU CB C 41.36 . 1 91 53 37 LEU N N 125.758 . 1 92 54 38 VAL H H 8.513 . 1 93 54 38 VAL CA C 58.84 . 1 94 54 38 VAL CB C 34.96 . 1 95 54 38 VAL N N 116.638 . 1 96 55 39 ARG H H 8.803 . 1 97 55 39 ARG CA C 55.49 . 1 98 55 39 ARG CB C 33.64 . 1 99 55 39 ARG N N 119.94 . 1 100 56 40 TYR H H 9.168 . 1 101 56 40 TYR CA C 58.52 . 1 102 56 40 TYR CB C 39.88 . 1 103 56 40 TYR N N 128.442 . 1 104 57 41 MET H H 8.81 . 1 105 57 41 MET N N 123.321 . 1 106 58 42 GLY H H 5.395 . 1 107 58 42 GLY CA C 42.84 . 1 108 58 42 GLY N N 132.05 . 1 109 59 43 CYS H H 7.751 . 1 110 59 43 CYS CA C 54.23 . 1 111 59 43 CYS CB C 32.08 . 1 112 59 43 CYS N N 107.3 . 1 113 60 44 VAL H H 8.09 . 1 114 60 44 VAL CA C 60.23 . 1 115 60 44 VAL CB C 35.43 . 1 116 60 44 VAL N N 117.818 . 1 117 61 45 GLU H H 8.532 . 1 118 61 45 GLU CA C 58.14 . 1 119 61 45 GLU CB C 31.99 . 1 120 61 45 GLU N N 127.955 . 1 121 62 46 VAL H H 8.437 . 1 122 62 46 VAL CA C 61.57 . 1 123 62 46 VAL CB C 31.37 . 1 124 62 46 VAL N N 124.455 . 1 125 63 47 LEU H H 9.366 . 1 126 63 47 LEU CA C 56.27 . 1 127 63 47 LEU CB C 42.14 . 1 128 63 47 LEU N N 126.281 . 1 129 64 48 GLN H H 7.035 . 1 130 64 48 GLN CA C 53.69 . 1 131 64 48 GLN CB C 33.09 . 1 132 64 48 GLN N N 115.89 . 1 133 65 49 SER H H 8.246 . 1 134 65 49 SER CA C 58.14 . 1 135 65 49 SER CB C 63.91 . 1 136 65 49 SER N N 112.597 . 1 137 66 50 MET H H 8.328 . 1 138 66 50 MET CA C 54.94 . 1 139 66 50 MET CB C 29.97 . 1 140 66 50 MET N N 123.523 . 1 141 68 52 ALA H H 7.363 . 1 142 68 52 ALA CA C 52.59 . 1 143 68 52 ALA CB C 18.97 . 1 144 68 52 ALA N N 119.273 . 1 145 69 53 LEU H H 7.219 . 1 146 69 53 LEU CA C 52.76 . 1 147 69 53 LEU CB C 43.7 . 1 148 69 53 LEU N N 118.71 . 1 149 70 54 ASP H H 8.234 . 1 150 70 54 ASP CA C 52.91 . 1 151 70 54 ASP CB C 41.05 . 1 152 70 54 ASP N N 119.782 . 1 153 71 55 PHE H H 8.874 . 1 154 71 55 PHE CA C 63.02 . 1 155 71 55 PHE CB C 39.43 . 1 156 71 55 PHE N N 121.059 . 1 157 72 56 ASN H H 8.694 . 1 158 72 56 ASN CA C 56.42 . 1 159 72 56 ASN CB C 38.01 . 1 160 72 56 ASN N N 116.651 . 1 161 73 57 THR H H 8.338 . 1 162 73 57 THR CA C 67.27 . 1 163 73 57 THR N N 119.646 . 1 164 74 58 ARG H H 8.294 . 1 165 74 58 ARG CA C 60.87 . 1 166 74 58 ARG CB C 29.19 . 1 167 74 58 ARG N N 121.831 . 1 168 75 59 THR H H 7.33 . 1 169 75 59 THR CA C 65.86 . 1 170 75 59 THR N N 110.579 . 1 171 76 60 GLN H H 7.776 . 1 172 76 60 GLN CA C 58.99 . 1 173 76 60 GLN CB C 27.94 . 1 174 76 60 GLN N N 123.139 . 1 175 77 61 VAL H H 8.298 . 1 176 77 61 VAL CA C 67.27 . 1 177 77 61 VAL CB C 31.37 . 1 178 77 61 VAL N N 120.306 . 1 179 78 62 THR H H 7.492 . 1 180 78 62 THR CA C 65.79 . 1 181 78 62 THR CB C 68.44 . 1 182 78 62 THR N N 108.1 . 1 183 79 63 ARG H H 7.718 . 1 184 79 63 ARG CA C 59.93 . 1 185 79 63 ARG CB C 30.28 . 1 186 79 63 ARG N N 121.61 . 1 187 80 64 GLU H H 8.423 . 1 188 80 64 GLU CA C 58.99 . 1 189 80 64 GLU CB C 29.03 . 1 190 80 64 GLU N N 120.453 . 1 191 81 65 ALA H H 8.301 . 1 192 81 65 ALA CA C 58.84 . 1 193 81 65 ALA CB C 18.49 . 1 194 81 65 ALA N N 122.813 . 1 195 82 66 ILE H H 7.929 . 1 196 82 66 ILE CA C 66.18 . 1 197 82 66 ILE CB C 38.71 . 1 198 82 66 ILE N N 116.16 . 1 199 83 67 SER H H 7.617 . 1 200 83 67 SER N N 114.01 . 1 201 84 68 LEU H H 8.172 . 1 202 84 68 LEU CA C 58.45 . 1 203 84 68 LEU CB C 42.61 . 1 204 84 68 LEU N N 121.03 . 1 205 85 69 VAL H H 7.759 . 1 206 85 69 VAL CA C 66.02 . 1 207 85 69 VAL CB C 30.83 . 1 208 85 69 VAL N N 115.48 . 1 209 86 70 CYS H H 8.061 . 1 210 86 70 CYS CA C 63.76 . 1 211 86 70 CYS CB C 26.61 . 1 212 86 70 CYS N N 117.418 . 1 213 87 71 GLU H H 7.495 . 1 214 87 71 GLU CA C 57.91 . 1 215 87 71 GLU CB C 29.81 . 1 216 87 71 GLU N N 116.65 . 1 217 88 72 ALA H H 7.372 . 1 218 88 72 ALA CA C 52.91 . 1 219 88 72 ALA CB C 21.15 . 1 220 88 72 ALA N N 120.03 . 1 221 89 73 VAL H H 7.718 . 1 222 89 73 VAL CA C 60.32 . 1 223 89 73 VAL CB C 33.25 . 1 224 89 73 VAL N N 120.476 . 1 225 91 75 GLY H H 8.577 . 1 226 91 75 GLY CA C 45.26 . 1 227 91 75 GLY N N 109.88 . 1 228 92 76 ALA H H 8.146 . 1 229 92 76 ALA CA C 53.3 . 1 230 92 76 ALA CB C 19.04 . 1 231 92 76 ALA N N 124.184 . 1 232 93 77 LYS H H 8.777 . 1 233 93 77 LYS CA C 57.92 . 1 234 93 77 LYS CB C 31.97 . 1 235 93 77 LYS N N 122.278 . 1 236 94 78 GLY H H 8.627 . 1 237 94 78 GLY CA C 45.65 . 1 238 94 78 GLY N N 106.561 . 1 239 95 79 ALA H H 7.792 . 1 240 95 79 ALA CA C 53.07 . 1 241 95 79 ALA CB C 19.67 . 1 242 95 79 ALA N N 122.677 . 1 243 96 80 THR H H 8.129 . 1 244 96 80 THR CA C 61.96 . 1 245 96 80 THR CB C 69.69 . 1 246 96 80 THR N N 111.39 . 1 247 97 81 ARG H H 7.934 . 1 248 97 81 ARG CA C 56.19 . 1 249 97 81 ARG CB C 30.83 . 1 250 97 81 ARG N N 122.06 . 1 251 98 82 ARG H H 7.617 . 1 252 98 82 ARG CA C 56.18 . 1 253 98 82 ARG CB C 30.6 . 1 254 98 82 ARG N N 118.631 . 1 255 99 83 ARG H H 8.442 . 1 256 99 83 ARG CA C 56.11 . 1 257 99 83 ARG CB C 30.98 . 1 258 99 83 ARG N N 123.487 . 1 259 100 84 LYS H H 8.437 . 1 260 100 84 LYS CA C 54.47 . 1 261 100 84 LYS CB C 32.54 . 1 262 100 84 LYS N N 124.455 . 1 263 102 86 CYS H H 8.458 . 1 264 102 86 CYS CA C 58.29 . 1 265 102 86 CYS CB C 28.25 . 1 266 102 86 CYS N N 119.835 . 1 267 103 87 SER H H 8.246 . 1 268 103 87 SER CA C 58.68 . 1 269 103 87 SER CB C 63.91 . 1 270 103 87 SER N N 112.597 . 1 271 104 88 ARG H H 8.315 . 1 272 104 88 ARG CA C 56.27 . 1 273 104 88 ARG CB C 30.59 . 1 274 104 88 ARG N N 122.38 . 1 275 106 90 LEU H H 8.503 . 1 276 106 90 LEU CA C 55.09 . 1 277 106 90 LEU CB C 41.15 . 1 278 106 90 LEU N N 121.43 . 1 279 107 91 SER H H 8.326 . 1 280 107 91 SER CA C 60.32 . 1 281 107 91 SER CB C 63.52 . 1 282 107 91 SER N N 116.134 . 1 283 108 92 SER H H 8.225 . 1 284 108 92 SER CA C 58.61 . 1 285 108 92 SER CB C 63.99 . 1 286 108 92 SER N N 115.371 . 1 287 109 93 ILE H H 7.905 . 1 288 109 93 ILE CA C 62.67 . 1 289 109 93 ILE CB C 39.72 . 1 290 109 93 ILE N N 119.68 . 1 291 110 94 LEU H H 7.718 . 1 292 110 94 LEU CA C 53.77 . 1 293 110 94 LEU CB C 42.84 . 1 294 110 94 LEU N N 120.476 . 1 295 111 95 GLY H H 8.518 . 1 296 111 95 GLY CA C 43.94 . 1 297 111 95 GLY N N 110.872 . 1 298 112 96 ARG H H 9.064 . 1 299 112 96 ARG CA C 56.42 . 1 300 112 96 ARG CB C 31.37 . 1 301 112 96 ARG N N 124.955 . 1 302 113 97 SER H H 8.602 . 1 303 113 97 SER CA C 57.67 . 1 304 113 97 SER CB C 65.01 . 1 305 113 97 SER N N 117.392 . 1 306 114 98 ASN H H 9.188 . 1 307 114 98 ASN CA C 52.76 . 1 308 114 98 ASN CB C 38.86 . 1 309 114 98 ASN N N 121.001 . 1 310 115 99 LEU H H 9.084 . 1 311 115 99 LEU CA C 52.71 . 1 312 115 99 LEU N N 125.5 . 1 313 119 103 GLY H H 9.87 . 1 314 119 103 GLY CA C 45.18 . 1 315 119 103 GLY N N 111.745 . 1 316 120 104 MET H H 7.976 . 1 317 120 104 MET CA C 54.63 . 1 318 120 104 MET CB C 34.89 . 1 319 120 104 MET N N 122.577 . 1 320 122 106 ILE H H 9.261 . 1 321 122 106 ILE CA C 59.31 . 1 322 122 106 ILE CB C 43.78 . 1 323 122 106 ILE N N 119.123 . 1 324 123 107 THR H H 9.29 . 1 325 123 107 THR CA C 59.08 . 1 326 123 107 THR CB C 69.3 . 1 327 123 107 THR N N 116.927 . 1 328 124 108 LEU H H 9.668 . 1 329 124 108 LEU CA C 52.91 . 1 330 124 108 LEU CB C 45.19 . 1 331 124 108 LEU N N 132.994 . 1 332 125 109 THR H H 9.356 . 1 333 125 109 THR CA C 62.27 . 1 334 125 109 THR CB C 69.84 . 1 335 125 109 THR N N 123.758 . 1 336 126 110 VAL H H 9.417 . 1 337 126 110 VAL CA C 62.04 . 1 338 126 110 VAL CB C 33.48 . 1 339 126 110 VAL N N 129.158 . 1 340 127 111 SER H H 8.301 . 1 341 127 111 SER CA C 58.84 . 1 342 127 111 SER CB C 68.36 . 1 343 127 111 SER N N 122.813 . 1 344 128 112 THR H H 7.848 . 1 345 128 112 THR CA C 64.46 . 1 346 128 112 THR CB C 68.67 . 1 347 128 112 THR N N 103.13 . 1 348 129 113 SER H H 8.172 . 1 349 129 113 SER CA C 61.02 . 1 350 129 113 SER N N 114.424 . 1 351 130 114 SER H H 7.587 . 1 352 130 114 SER CA C 58.14 . 1 353 130 114 SER CB C 65.47 . 1 354 130 114 SER N N 114.99 . 1 355 131 115 LEU H H 8.37 . 1 356 131 115 LEU CA C 55.01 . 1 357 131 115 LEU CB C 41.99 . 1 358 131 115 LEU N N 117.735 . 1 359 132 116 ASN H H 8.503 . 1 360 132 116 ASN CA C 52.99 . 1 361 132 116 ASN CB C 42.69 . 1 362 132 116 ASN N N 121.43 . 1 363 133 117 LEU H H 8.76 . 1 364 133 117 LEU CA C 52.99 . 1 365 133 117 LEU CB C 42.84 . 1 366 133 117 LEU N N 126.6 . 1 367 134 118 MET H H 8.328 . 1 368 134 118 MET CA C 53.54 . 1 369 134 118 MET CB C 36.29 . 1 370 134 118 MET N N 123.523 . 1 371 135 119 ALA H H 8.867 . 1 372 135 119 ALA CA C 53.38 . 1 373 135 119 ALA CB C 20.21 . 1 374 135 119 ALA N N 128.043 . 1 375 136 120 ALA H H 8.41 . 1 376 136 120 ALA CA C 54.63 . 1 377 136 120 ALA CB C 18.58 . 1 378 136 120 ALA N N 125.156 . 1 379 137 121 ASP H H 8.284 . 1 380 137 121 ASP CA C 54.55 . 1 381 137 121 ASP CB C 40.11 . 1 382 137 121 ASP N N 114.77 . 1 383 138 122 CYS H H 8.041 . 1 384 138 122 CYS CA C 55.64 . 1 385 138 122 CYS CB C 32.08 . 1 386 138 122 CYS N N 125.3 . 1 387 139 123 LYS H H 8.691 . 1 388 139 123 LYS CA C 57.75 . 1 389 139 123 LYS CB C 30.59 . 1 390 139 123 LYS N N 125.454 . 1 391 140 124 GLN H H 7.455 . 1 392 140 124 GLN CA C 55.49 . 1 393 140 124 GLN CB C 30.6 . 1 394 140 124 GLN N N 118.059 . 1 395 141 125 ILE H H 8.712 . 1 396 141 125 ILE CA C 61.18 . 1 397 141 125 ILE CB C 37.93 . 1 398 141 125 ILE N N 126.697 . 1 399 142 126 ILE H H 8.336 . 1 400 142 126 ILE CA C 62.51 . 1 401 142 126 ILE CB C 37.77 . 1 402 142 126 ILE N N 129.301 . 1 403 143 127 ALA H H 7.455 . 1 404 143 127 ALA CA C 52.44 . 1 405 143 127 ALA CB C 20.92 . 1 406 143 127 ALA N N 118.059 . 1 407 145 129 HIS H H 8.786 . 1 408 145 129 HIS CA C 55.01 . 1 409 145 129 HIS CB C 31.69 . 1 410 145 129 HIS N N 125.252 . 1 411 146 130 HIS H H 8.501 . 1 412 146 130 HIS N N 120.345 . 1 413 148 132 GLN H H 9.535 . 1 414 148 132 GLN N N 116.909 . 1 415 150 134 ILE H H 7.617 . 1 416 150 134 ILE CA C 64.46 . 1 417 150 134 ILE CB C 39.49 . 1 418 150 134 ILE N N 124.87 . 1 419 154 138 SER H H 9.477 . 1 420 154 138 SER CA C 57.19 . 1 421 154 138 SER CB C 66.64 . 1 422 154 138 SER N N 113.89 . 1 423 155 139 GLY H H 8.625 . 1 424 155 139 GLY CA C 45.34 . 1 425 155 139 GLY N N 109.994 . 1 426 156 140 GLY H H 8.512 . 1 427 156 140 GLY CA C 45.11 . 1 428 156 140 GLY N N 106.141 . 1 429 157 141 ASP H H 7.874 . 1 430 157 141 ASP CA C 53.69 . 1 431 157 141 ASP CB C 41.13 . 1 432 157 141 ASP N N 121.376 . 1 433 159 143 ASP H H 8.333 . 1 434 159 143 ASP CA C 55.41 . 1 435 159 143 ASP CB C 40.89 . 1 436 159 143 ASP N N 113.426 . 1 437 160 144 THR H H 8.043 . 1 438 160 144 THR CA C 59.78 . 1 439 160 144 THR CB C 68.83 . 1 440 160 144 THR N N 113.5 . 1 441 161 145 ALA H H 7.509 . 1 442 161 145 ALA CA C 56.19 . 1 443 161 145 ALA CB C 19.04 . 1 444 161 145 ALA N N 123.69 . 1 445 162 146 GLU H H 9.455 . 1 446 162 146 GLU CA C 56.89 . 1 447 162 146 GLU CB C 28.33 . 1 448 162 146 GLU N N 117.391 . 1 449 163 147 TYR H H 7.972 . 1 450 163 147 TYR CA C 58.45 . 1 451 163 147 TYR CB C 41.83 . 1 452 163 147 TYR N N 117.953 . 1 453 164 148 VAL H H 9.052 . 1 454 164 148 VAL CA C 60.94 . 1 455 164 148 VAL CB C 35.91 . 1 456 164 148 VAL N N 121.045 . 1 457 165 149 ALA H H 9.262 . 1 458 165 149 ALA CA C 49.63 . 1 459 165 149 ALA CB C 24.35 . 1 460 165 149 ALA N N 127.934 . 1 461 166 150 TYR H H 8.765 . 1 462 166 150 TYR CA C 56.89 . 1 463 166 150 TYR N N 116.099 . 1 464 167 151 VAL H H 9.02 . 1 465 167 151 VAL CA C 61.49 . 1 466 167 151 VAL CB C 32.4 . 1 467 167 151 VAL N N 122.473 . 1 468 168 152 ALA H H 8.936 . 1 469 168 152 ALA CA C 49.71 . 1 470 168 152 ALA CB C 23.73 . 1 471 168 152 ALA N N 128.361 . 1 472 169 153 LYS H H 7.317 . 1 473 169 153 LYS CA C 55.09 . 1 474 169 153 LYS CB C 35.83 . 1 475 169 153 LYS N N 118.039 . 1 476 170 154 ASP H H 8.269 . 1 477 170 154 ASP N N 122.38 . 1 478 172 156 VAL H H 8.548 . 1 479 172 156 VAL CA C 64.45 . 1 480 172 156 VAL CB C 33.02 . 1 481 172 156 VAL N N 117.65 . 1 482 173 157 ASN H H 9.426 . 1 483 173 157 ASN CA C 54.08 . 1 484 173 157 ASN CB C 40.27 . 1 485 173 157 ASN N N 117.552 . 1 486 174 158 GLN H H 7.876 . 1 487 174 158 GLN CA C 56.81 . 1 488 174 158 GLN CB C 25.53 . 1 489 174 158 GLN N N 113.141 . 1 490 175 159 ARG H H 7.982 . 1 491 175 159 ARG CA C 56.34 . 1 492 175 159 ARG CB C 29.97 . 1 493 175 159 ARG N N 124.43 . 1 494 176 160 ALA H H 9.254 . 1 495 176 160 ALA CA C 51.35 . 1 496 176 160 ALA CB C 22.48 . 1 497 176 160 ALA N N 129.257 . 1 498 177 161 CYS H H 9.243 . 1 499 177 161 CYS CA C 56.57 . 1 500 177 161 CYS CB C 27.07 . 1 501 177 161 CYS N N 121.209 . 1 502 178 162 HIS H H 9.363 . 1 503 178 162 HIS CA C 56.42 . 1 504 178 162 HIS N N 131.061 . 1 505 179 163 ILE H H 7.912 . 1 506 179 163 ILE CA C 60.16 . 1 507 179 163 ILE CB C 39.34 . 1 508 179 163 ILE N N 120.03 . 1 509 180 164 LEU H H 9.532 . 1 510 180 164 LEU CA C 52.52 . 1 511 180 164 LEU CB C 43.94 . 1 512 180 164 LEU N N 126.082 . 1 513 181 165 GLU H H 9.556 . 1 514 181 165 GLU CA C 55.72 . 1 515 181 165 GLU CB C 33.79 . 1 516 181 165 GLU N N 124.553 . 1 517 182 166 CYS H H 9.12 . 1 518 182 166 CYS CA C 56.27 . 1 519 182 166 CYS CB C 28.41 . 1 520 182 166 CYS N N 127.686 . 1 521 184 168 GLU H H 8.843 . 1 522 184 168 GLU CA C 58.53 . 1 523 184 168 GLU CB C 28.91 . 1 524 184 168 GLU N N 120.631 . 1 525 185 169 GLY H H 8.885 . 1 526 185 169 GLY CA C 45.81 . 1 527 185 169 GLY N N 111.054 . 1 528 186 170 LEU H H 7.926 . 1 529 186 170 LEU CA C 55.79 . 1 530 186 170 LEU CB C 44.41 . 1 531 186 170 LEU N N 120.591 . 1 532 187 171 ALA H H 8.665 . 1 533 187 171 ALA CA C 56.66 . 1 534 187 171 ALA CB C 18.65 . 1 535 187 171 ALA N N 123.697 . 1 536 188 172 GLN H H 8.259 . 1 537 188 172 GLN CA C 58.99 . 1 538 188 172 GLN CB C 27.78 . 1 539 188 172 GLN N N 113.715 . 1 540 189 173 ASP H H 7.425 . 1 541 189 173 ASP CA C 56.73 . 1 542 189 173 ASP CB C 40.66 . 1 543 189 173 ASP N N 122.78 . 1 544 190 174 VAL H H 8.08 . 1 545 190 174 VAL CA C 67.58 . 1 546 190 174 VAL CB C 30.83 . 1 547 190 174 VAL N N 121.532 . 1 548 191 175 ILE H H 8.286 . 1 549 191 175 ILE N N 115.504 . 1 550 195 179 GLY H H 7.584 . 1 551 195 179 GLY CA C 47.21 . 1 552 195 179 GLY N N 105.11 . 1 553 197 181 ALA H H 7.834 . 1 554 197 181 ALA CA C 55.49 . 1 555 197 181 ALA CB C 17.56 . 1 556 197 181 ALA N N 121.189 . 1 557 198 182 PHE H H 8.361 . 1 558 198 182 PHE CA C 57.74 . 1 559 198 182 PHE CB C 42.3 . 1 560 198 182 PHE N N 115.202 . 1 561 199 183 GLU H H 8.114 . 1 562 199 183 GLU CA C 58.92 . 1 563 199 183 GLU CB C 29.89 . 1 564 199 183 GLU N N 118.37 . 1 565 203 187 LYS H H 7.522 . 1 566 203 187 LYS N N 120 . 1 567 207 191 ARG H H 7.357 . 1 568 207 191 ARG CA C 58.29 . 1 569 207 191 ARG CB C 31.22 . 1 570 207 191 ARG N N 124.78 . 1 stop_ save_