data_11558 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Backbone 1H, 13C, and 15N Chemical Shift Assignments for the peptidyl prolyl cis-trans isomerase domain of C113D mutant human Pin1 without sulfate ion ; _BMRB_accession_number 11558 _BMRB_flat_file_name bmr11558.str _Entry_type original _Submission_date 2014-03-24 _Accession_date 2014-03-24 _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 Xu Ning . . 2 Tamari Yu . . 3 Tochio Naoya . . 4 Tate Shin-ichi . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 107 "13C chemical shifts" 325 "15N chemical shifts" 107 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2018-12-18 original BMRB . stop_ loop_ _Related_BMRB_accession_number _Relationship 11557 ; Backbone 1H, 13C, and 15N Chemical Shift Assignments for the peptidyl prolyl cis-trans isomerase domain of human Pin1 without sulfate ion ; 11559 'Solution structure of the peptidyl prolyl cis-trans isomerase domain of human Pin1 with sulfate ion' 11560 'Solution structure of the peptidyl prolyl cis-trans isomerase domain of C113D mutant with sulfate ion' stop_ _Original_release_date 2014-03-24 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; The C113D mutation in human Pin1 causes allosteric structural changes in the phosphate binding pocket of the PPIase domain through the tug of war in the dual-histidine motif. ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 25100325 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Xu Ning . . 2 Tochio Naoya . . 3 Wang Jong . . 4 Tamari Yu . . 5 Uewaki Jun-ichi . . 6 Utsunomiya-Tate Naoko . . 7 Igarashi Kazuhiko . . 8 Shiraki Takuma . . 9 Kobayashi Naohiro . . 10 Tate Shin-ichi . . stop_ _Journal_abbreviation Biochemistry _Journal_name_full Biochemistry _Journal_volume 53 _Journal_issue 34 _Journal_ISSN 0006-2960 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 5568 _Page_last 5578 _Year 2014 _Details . save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name 'C113D mutant human Pin1 PPIase domain' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label PPIase $C113D_mutant_hPin1_PPIase_domain stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state ? _System_paramagnetic no _System_thiol_state . _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_C113D_mutant_hPin1_PPIase_domain _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common C113D_mutant_hPin1_PPIase_domain _Molecular_mass . _Mol_thiol_state 'all free' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 117 _Mol_residue_sequence ; GSHMEPARVRCSHLLVKHSQ SRRPSSWRQEKITRTKEEAL ELINGYIQKIKSGEEDFESL ASQFSDDSSAKARGDLGAFS RGQMQKPFEDASFALRTGEM SGPVFTDSGIHIILRTE ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 1 GLY 2 2 SER 3 3 HIS 4 4 MET 5 5 GLU 6 6 PRO 7 7 ALA 8 8 ARG 9 9 VAL 10 10 ARG 11 11 CYS 12 12 SER 13 13 HIS 14 14 LEU 15 15 LEU 16 16 VAL 17 17 LYS 18 18 HIS 19 19 SER 20 20 GLN 21 21 SER 22 22 ARG 23 23 ARG 24 24 PRO 25 25 SER 26 26 SER 27 27 TRP 28 28 ARG 29 29 GLN 30 30 GLU 31 31 LYS 32 32 ILE 33 33 THR 34 34 ARG 35 35 THR 36 36 LYS 37 37 GLU 38 38 GLU 39 39 ALA 40 40 LEU 41 41 GLU 42 42 LEU 43 43 ILE 44 44 ASN 45 45 GLY 46 46 TYR 47 47 ILE 48 48 GLN 49 49 LYS 50 50 ILE 51 51 LYS 52 52 SER 53 53 GLY 54 54 GLU 55 55 GLU 56 56 ASP 57 57 PHE 58 58 GLU 59 59 SER 60 60 LEU 61 61 ALA 62 62 SER 63 63 GLN 64 64 PHE 65 65 SER 66 66 ASP 67 67 ASP 68 68 SER 69 69 SER 70 70 ALA 71 71 LYS 72 72 ALA 73 73 ARG 74 74 GLY 75 75 ASP 76 76 LEU 77 77 GLY 78 78 ALA 79 79 PHE 80 80 SER 81 81 ARG 82 82 GLY 83 83 GLN 84 84 MET 85 85 GLN 86 86 LYS 87 87 PRO 88 88 PHE 89 89 GLU 90 90 ASP 91 91 ALA 92 92 SER 93 93 PHE 94 94 ALA 95 95 LEU 96 96 ARG 97 97 THR 98 98 GLY 99 99 GLU 100 100 MET 101 101 SER 102 102 GLY 103 103 PRO 104 104 VAL 105 105 PHE 106 106 THR 107 107 ASP 108 108 SER 109 109 GLY 110 110 ILE 111 111 HIS 112 112 ILE 113 113 ILE 114 114 LEU 115 115 ARG 116 116 THR 117 117 GLU 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 $C113D_mutant_hPin1_PPIase_domain Human 9606 Eukaryota Metazoa Homo sapiens 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 $C113D_mutant_hPin1_PPIase_domain 'recombinant technology' 'E. coli' Escherichia coli . pET28a stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $C113D_mutant_hPin1_PPIase_domain 0.2 mM '[U-13C; U-15N]' TRIS 50 mM 'natural abundance' DTT 1 mM 'natural abundance' 'sodium azide' 0.03 % 'natural abundance' H2O 94.12 % 'natural abundance' D2O 5.88 % 'natural abundance' stop_ save_ ############################ # Computer software used # ############################ save_TOPSPIN _Saveframe_category software _Name TOPSPIN _Version . loop_ _Vendor _Address _Electronic_address 'Bruker Biospin' . . stop_ loop_ _Task collection stop_ _Details . save_ 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_Magro _Saveframe_category software _Name Magro _Version . loop_ _Vendor _Address _Electronic_address Kobayashi . . stop_ loop_ _Task 'data analysis' stop_ _Details . save_ save_NMRView _Saveframe_category software _Name NMRView _Version . loop_ _Vendor _Address _Electronic_address 'Johnson, One Moon Scientific' . . stop_ loop_ _Task 'data analysis' stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model Avance _Field_strength 700 _Details . save_ ############################# # NMR applied experiments # ############################# save_2D_1H-15N_HSQC_1 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-15N HSQC' _Sample_label $sample_1 save_ save_3D_HNCO_2 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCO' _Sample_label $sample_1 save_ save_3D_HN(CA)CO_3 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HN(CA)CO' _Sample_label $sample_1 save_ save_3D_HNCA_4 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCA' _Sample_label $sample_1 save_ save_3D_HN(CO)CA_5 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HN(CO)CA' _Sample_label $sample_1 save_ save_3D_CBCA(CO)NH_6 _Saveframe_category NMR_applied_experiment _Experiment_name '3D CBCA(CO)NH' _Sample_label $sample_1 save_ save_3D_HNCACB_7 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCACB' _Sample_label $sample_1 save_ save_3D_C(CO)NH_8 _Saveframe_category NMR_applied_experiment _Experiment_name '3D C(CO)NH' _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' 0 . M pH 6.8 . pH pressure 1 . atm temperature 299 . 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 water C 13 protons ppm 4.844 internal indirect . . . 0.251449530 water H 1 protons ppm 4.844 internal direct . . . 1.0 water N 15 protons ppm 4.844 internal 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 HNCO' '3D HN(CA)CO' '3D HNCA' '3D HN(CO)CA' '3D CBCA(CO)NH' '3D HNCACB' '3D C(CO)NH' stop_ loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $sample_conditions_1 _Chem_shift_reference_set_label $chemical_shift_reference_1 _Mol_system_component_name PPIase _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 4 4 MET H H 8.296 0.030 1 2 4 4 MET C C 175.435 0.300 1 3 4 4 MET CA C 55.022 0.300 1 4 4 4 MET CB C 32.967 0.300 1 5 4 4 MET N N 122.313 0.300 1 6 5 5 GLU H H 8.365 0.030 1 7 5 5 GLU C C 174.026 0.300 1 8 5 5 GLU CA C 54.354 0.300 1 9 5 5 GLU CB C 30.116 0.300 1 10 5 5 GLU N N 124.232 0.300 1 11 6 6 PRO C C 176.165 0.300 1 12 6 6 PRO CA C 62.486 0.300 1 13 6 6 PRO CB C 32.212 0.300 1 14 7 7 ALA H H 8.581 0.030 1 15 7 7 ALA C C 178.084 0.300 1 16 7 7 ALA CA C 53.681 0.300 1 17 7 7 ALA CB C 19.381 0.300 1 18 7 7 ALA N N 122.607 0.300 1 19 8 8 ARG H H 7.719 0.030 1 20 8 8 ARG C C 174.518 0.300 1 21 8 8 ARG CA C 54.309 0.300 1 22 8 8 ARG CB C 34.309 0.300 1 23 8 8 ARG N N 115.526 0.300 1 24 9 9 VAL H H 7.861 0.030 1 25 9 9 VAL C C 172.103 0.300 1 26 9 9 VAL CA C 58.712 0.300 1 27 9 9 VAL CB C 35.063 0.300 1 28 9 9 VAL N N 113.848 0.300 1 29 10 10 ARG H H 8.213 0.030 1 30 10 10 ARG C C 175.850 0.300 1 31 10 10 ARG CA C 54.771 0.300 1 32 10 10 ARG CB C 34.560 0.300 1 33 10 10 ARG N N 120.810 0.300 1 34 11 11 CYS H H 7.159 0.030 1 35 11 11 CYS C C 173.154 0.300 1 36 11 11 CYS CA C 55.617 0.300 1 37 11 11 CYS CB C 33.722 0.300 1 38 11 11 CYS N N 117.508 0.300 1 39 12 12 SER H H 9.368 0.030 1 40 12 12 SER C C 173.196 0.300 1 41 12 12 SER CA C 55.945 0.300 1 42 12 12 SER CB C 65.840 0.300 1 43 12 12 SER N N 116.398 0.300 1 44 13 13 HIS H H 9.759 0.030 1 45 13 13 HIS C C 171.826 0.300 1 46 13 13 HIS CA C 54.267 0.300 1 47 13 13 HIS CB C 37.076 0.300 1 48 13 13 HIS N N 119.542 0.300 1 49 14 14 LEU H H 8.907 0.030 1 50 14 14 LEU C C 173.526 0.300 1 51 14 14 LEU CA C 55.602 0.300 1 52 14 14 LEU CB C 45.504 0.300 1 53 14 14 LEU N N 125.211 0.300 1 54 15 15 LEU H H 8.078 0.030 1 55 15 15 LEU C C 173.822 0.300 1 56 15 15 LEU CA C 52.576 0.300 1 57 15 15 LEU CB C 45.294 0.300 1 58 15 15 LEU N N 126.870 0.300 1 59 16 16 VAL H H 9.523 0.030 1 60 16 16 VAL C C 176.281 0.300 1 61 16 16 VAL CA C 61.479 0.300 1 62 16 16 VAL CB C 33.135 0.300 1 63 16 16 VAL N N 128.420 0.300 1 64 17 17 LYS H H 9.102 0.030 1 65 17 17 LYS C C 174.240 0.300 1 66 17 17 LYS CA C 56.768 0.300 1 67 17 17 LYS CB C 36.321 0.300 1 68 17 17 LYS N N 125.320 0.300 1 69 18 18 HIS H H 8.254 0.030 1 70 18 18 HIS C C 176.541 0.300 1 71 18 18 HIS CA C 54.567 0.300 1 72 18 18 HIS CB C 33.805 0.300 1 73 18 18 HIS N N 113.941 0.300 1 74 19 19 SER H H 9.480 0.030 1 75 19 19 SER C C 175.533 0.300 1 76 19 19 SER CA C 60.641 0.300 1 77 19 19 SER CB C 62.970 0.300 1 78 19 19 SER N N 113.804 0.300 1 79 20 20 GLN H H 9.147 0.030 1 80 20 20 GLN C C 176.416 0.300 1 81 20 20 GLN CA C 55.045 0.300 1 82 20 20 GLN CB C 29.445 0.300 1 83 20 20 GLN N N 120.282 0.300 1 84 21 21 SER H H 7.846 0.030 1 85 21 21 SER C C 173.020 0.300 1 86 21 21 SER CA C 61.109 0.300 1 87 21 21 SER CB C 63.576 0.300 1 88 21 21 SER N N 121.185 0.300 1 89 22 22 ARG H H 8.099 0.030 1 90 22 22 ARG C C 176.884 0.300 1 91 22 22 ARG CA C 59.027 0.300 1 92 22 22 ARG CB C 29.529 0.300 1 93 22 22 ARG N N 123.023 0.300 1 94 23 23 ARG H H 8.368 0.030 1 95 23 23 ARG C C 174.317 0.300 1 96 23 23 ARG CA C 52.677 0.300 1 97 23 23 ARG CB C 31.122 0.300 1 98 23 23 ARG N N 116.797 0.300 1 99 24 24 PRO C C 173.817 0.300 1 100 24 24 PRO CA C 63.408 0.300 1 101 24 24 PRO CB C 27.516 0.300 1 102 25 25 SER H H 9.000 0.030 1 103 25 25 SER C C 172.529 0.300 1 104 25 25 SER CA C 57.810 0.300 1 105 25 25 SER CB C 65.588 0.300 1 106 25 25 SER N N 120.601 0.300 1 107 26 26 SER H H 8.987 0.030 1 108 26 26 SER C C 174.362 0.300 1 109 26 26 SER CA C 57.035 0.300 1 110 26 26 SER CB C 68.524 0.300 1 111 26 26 SER N N 119.124 0.300 1 112 27 27 TRP H H 8.508 0.030 1 113 27 27 TRP C C 176.258 0.300 1 114 27 27 TRP CA C 58.035 0.300 1 115 27 27 TRP CB C 27.348 0.300 1 116 27 27 TRP N N 118.948 0.300 1 117 28 28 ARG H H 7.023 0.030 1 118 28 28 ARG C C 176.417 0.300 1 119 28 28 ARG CA C 57.030 0.300 1 120 28 28 ARG CB C 29.948 0.300 1 121 28 28 ARG N N 117.840 0.300 1 122 29 29 GLN H H 6.907 0.030 1 123 29 29 GLN N N 118.288 0.300 1 124 30 30 GLU C C 176.529 0.300 1 125 31 31 LYS H H 8.020 0.030 1 126 31 31 LYS C C 174.529 0.300 1 127 31 31 LYS CA C 55.106 0.300 1 128 31 31 LYS CB C 34.057 0.300 1 129 31 31 LYS N N 117.905 0.300 1 130 32 32 ILE H H 7.844 0.030 1 131 32 32 ILE C C 175.612 0.300 1 132 32 32 ILE CA C 60.651 0.300 1 133 32 32 ILE CB C 37.411 0.300 1 134 32 32 ILE N N 125.998 0.300 1 135 33 33 THR H H 8.191 0.030 1 136 33 33 THR C C 175.260 0.300 1 137 33 33 THR CA C 60.547 0.300 1 138 33 33 THR CB C 69.614 0.300 1 139 33 33 THR N N 116.550 0.300 1 140 34 34 ARG H H 7.554 0.030 1 141 34 34 ARG C C 174.569 0.300 1 142 34 34 ARG CA C 55.639 0.300 1 143 34 34 ARG CB C 31.206 0.300 1 144 34 34 ARG N N 123.774 0.300 1 145 35 35 THR H H 9.001 0.030 1 146 35 35 THR C C 176.487 0.300 1 147 35 35 THR CA C 60.808 0.300 1 148 35 35 THR CB C 71.459 0.300 1 149 35 35 THR N N 113.587 0.300 1 150 36 36 LYS H H 8.784 0.030 1 151 36 36 LYS C C 177.755 0.300 1 152 36 36 LYS CA C 60.305 0.300 1 153 36 36 LYS CB C 31.960 0.300 1 154 36 36 LYS N N 122.225 0.300 1 155 37 37 GLU H H 8.555 0.030 1 156 37 37 GLU C C 179.840 0.300 1 157 37 37 GLU CA C 60.725 0.300 1 158 37 37 GLU CB C 28.690 0.300 1 159 37 37 GLU N N 118.415 0.300 1 160 38 38 GLU H H 7.930 0.030 1 161 38 38 GLU C C 179.886 0.300 1 162 38 38 GLU CA C 58.823 0.300 1 163 38 38 GLU CB C 30.200 0.300 1 164 38 38 GLU N N 121.687 0.300 1 165 39 39 ALA H H 8.635 0.030 1 166 39 39 ALA C C 177.889 0.300 1 167 39 39 ALA CA C 54.888 0.300 1 168 39 39 ALA CB C 19.004 0.300 1 169 39 39 ALA N N 121.979 0.300 1 170 40 40 LEU H H 8.180 0.030 1 171 40 40 LEU C C 177.770 0.300 1 172 40 40 LEU CA C 57.338 0.300 1 173 40 40 LEU CB C 41.437 0.300 1 174 40 40 LEU N N 120.160 0.300 1 175 41 41 GLU H H 7.684 0.030 1 176 41 41 GLU C C 180.317 0.300 1 177 41 41 GLU CA C 59.383 0.300 1 178 41 41 GLU CB C 29.445 0.300 1 179 41 41 GLU N N 119.316 0.300 1 180 42 42 LEU H H 7.739 0.030 1 181 42 42 LEU C C 178.634 0.300 1 182 42 42 LEU CA C 57.460 0.300 1 183 42 42 LEU CB C 41.772 0.300 1 184 42 42 LEU N N 121.150 0.300 1 185 43 43 ILE H H 8.057 0.030 1 186 43 43 ILE C C 177.448 0.300 1 187 43 43 ILE CA C 62.368 0.300 1 188 43 43 ILE CB C 35.315 0.300 1 189 43 43 ILE N N 120.208 0.300 1 190 44 44 ASN H H 8.720 0.030 1 191 44 44 ASN C C 179.137 0.300 1 192 44 44 ASN CA C 55.817 0.300 1 193 44 44 ASN CB C 37.621 0.300 1 194 44 44 ASN N N 118.966 0.300 1 195 45 45 GLY H H 7.951 0.030 1 196 45 45 GLY C C 176.755 0.300 1 197 45 45 GLY CA C 46.888 0.300 1 198 45 45 GLY N N 110.189 0.300 1 199 46 46 TYR H H 8.090 0.030 1 200 46 46 TYR C C 178.151 0.300 1 201 46 46 TYR CA C 58.628 0.300 1 202 46 46 TYR CB C 35.986 0.300 1 203 46 46 TYR N N 123.021 0.300 1 204 47 47 ILE H H 8.637 0.030 1 205 47 47 ILE C C 177.918 0.300 1 206 47 47 ILE CA C 67.014 0.300 1 207 47 47 ILE CB C 38.334 0.300 1 208 47 47 ILE N N 118.884 0.300 1 209 48 48 GLN H H 7.778 0.030 1 210 48 48 GLN C C 179.260 0.300 1 211 48 48 GLN CA C 58.964 0.300 1 212 48 48 GLN CB C 28.187 0.300 1 213 48 48 GLN N N 117.508 0.300 1 214 49 49 LYS H H 8.056 0.030 1 215 49 49 LYS C C 178.365 0.300 1 216 49 49 LYS CA C 59.551 0.300 1 217 49 49 LYS CB C 33.470 0.300 1 218 49 49 LYS N N 120.243 0.300 1 219 50 50 ILE H H 8.155 0.030 1 220 50 50 ILE C C 181.287 0.300 1 221 50 50 ILE CA C 63.692 0.300 1 222 50 50 ILE CB C 39.005 0.300 1 223 50 50 ILE N N 119.975 0.300 1 224 51 51 LYS H H 9.022 0.030 1 225 51 51 LYS C C 178.990 0.300 1 226 51 51 LYS CA C 59.586 0.300 1 227 51 51 LYS CB C 32.464 0.300 1 228 51 51 LYS N N 120.975 0.300 1 229 52 52 SER H H 8.145 0.030 1 230 52 52 SER C C 175.637 0.300 1 231 52 52 SER CA C 59.221 0.300 1 232 52 52 SER CB C 63.911 0.300 1 233 52 52 SER N N 111.610 0.300 1 234 53 53 GLY H H 7.823 0.030 1 235 53 53 GLY C C 174.456 0.300 1 236 53 53 GLY CA C 45.378 0.300 1 237 53 53 GLY N N 110.356 0.300 1 238 54 54 GLU H H 8.258 0.030 1 239 54 54 GLU C C 176.734 0.300 1 240 54 54 GLU CA C 58.751 0.300 1 241 54 54 GLU CB C 31.038 0.300 1 242 54 54 GLU N N 121.686 0.300 1 243 55 55 GLU H H 7.378 0.030 1 244 55 55 GLU C C 174.230 0.300 1 245 55 55 GLU CA C 54.183 0.300 1 246 55 55 GLU CB C 34.393 0.300 1 247 55 55 GLU N N 114.372 0.300 1 248 56 56 ASP H H 8.344 0.030 1 249 56 56 ASP C C 175.578 0.300 1 250 56 56 ASP CA C 52.353 0.300 1 251 56 56 ASP CB C 43.156 0.300 1 252 56 56 ASP N N 118.588 0.300 1 253 57 57 PHE H H 9.079 0.030 1 254 57 57 PHE C C 176.666 0.300 1 255 57 57 PHE CA C 62.486 0.300 1 256 57 57 PHE CB C 40.347 0.300 1 257 57 57 PHE N N 122.230 0.300 1 258 58 58 GLU H H 8.968 0.030 1 259 58 58 GLU C C 179.194 0.300 1 260 58 58 GLU CA C 60.389 0.300 1 261 58 58 GLU CB C 29.780 0.300 1 262 58 58 GLU N N 116.640 0.300 1 263 59 59 SER H H 8.084 0.030 1 264 59 59 SER C C 178.084 0.300 1 265 59 59 SER CA C 61.340 0.300 1 266 59 59 SER CB C 62.653 0.300 1 267 59 59 SER N N 115.968 0.300 1 268 60 60 LEU H H 7.699 0.030 1 269 60 60 LEU C C 178.835 0.300 1 270 60 60 LEU CA C 57.312 0.300 1 271 60 60 LEU CB C 41.688 0.300 1 272 60 60 LEU N N 120.766 0.300 1 273 61 61 ALA H H 8.802 0.030 1 274 61 61 ALA C C 178.988 0.300 1 275 61 61 ALA CA C 55.441 0.300 1 276 61 61 ALA CB C 17.285 0.300 1 277 61 61 ALA N N 122.554 0.300 1 278 62 62 SER H H 7.707 0.030 1 279 62 62 SER C C 174.913 0.300 1 280 62 62 SER CA C 60.641 0.300 1 281 62 62 SER CB C 63.408 0.300 1 282 62 62 SER N N 108.802 0.300 1 283 63 63 GLN H H 6.882 0.030 1 284 63 63 GLN C C 177.724 0.300 1 285 63 63 GLN CA C 57.454 0.300 1 286 63 63 GLN CB C 31.374 0.300 1 287 63 63 GLN N N 115.196 0.300 1 288 64 64 PHE H H 8.176 0.030 1 289 64 64 PHE C C 175.204 0.300 1 290 64 64 PHE CA C 57.303 0.300 1 291 64 64 PHE CB C 41.269 0.300 1 292 64 64 PHE N N 112.524 0.300 1 293 65 65 SER H H 7.863 0.030 1 294 65 65 SER C C 176.122 0.300 1 295 65 65 SER CA C 57.035 0.300 1 296 65 65 SER CB C 65.588 0.300 1 297 65 65 SER N N 111.272 0.300 1 298 66 66 ASP H H 9.950 0.030 1 299 66 66 ASP C C 175.600 0.300 1 300 66 66 ASP CA C 55.858 0.300 1 301 66 66 ASP CB C 43.617 0.300 1 302 66 66 ASP N N 125.465 0.300 1 303 67 67 ASP H H 8.232 0.030 1 304 67 67 ASP C C 176.912 0.300 1 305 67 67 ASP CA C 54.354 0.300 1 306 67 67 ASP CB C 45.127 0.300 1 307 67 67 ASP N N 118.464 0.300 1 308 69 69 SER C C 176.652 0.300 1 309 69 69 SER CA C 60.305 0.300 1 310 69 69 SER CB C 63.492 0.300 1 311 70 70 ALA H H 8.255 0.030 1 312 70 70 ALA C C 179.862 0.300 1 313 70 70 ALA CA C 56.553 0.300 1 314 70 70 ALA CB C 20.220 0.300 1 315 70 70 ALA N N 131.471 0.300 1 316 71 71 LYS H H 7.101 0.030 1 317 71 71 LYS C C 176.565 0.300 1 318 71 71 LYS CA C 57.370 0.300 1 319 71 71 LYS CB C 31.709 0.300 1 320 71 71 LYS N N 113.844 0.300 1 321 72 72 ALA H H 7.598 0.030 1 322 72 72 ALA C C 177.346 0.300 1 323 72 72 ALA CA C 50.710 0.300 1 324 72 72 ALA CB C 18.794 0.300 1 325 72 72 ALA N N 123.907 0.300 1 326 73 73 ARG H H 8.106 0.030 1 327 73 73 ARG C C 174.943 0.300 1 328 73 73 ARG CA C 57.530 0.300 1 329 73 73 ARG CB C 26.845 0.300 1 330 73 73 ARG N N 115.478 0.300 1 331 74 74 GLY H H 8.299 0.030 1 332 74 74 GLY C C 174.116 0.300 1 333 74 74 GLY CA C 45.043 0.300 1 334 74 74 GLY N N 103.082 0.300 1 335 75 75 ASP H H 7.225 0.030 1 336 75 75 ASP C C 175.488 0.300 1 337 75 75 ASP CA C 55.853 0.300 1 338 75 75 ASP CB C 42.191 0.300 1 339 75 75 ASP N N 119.278 0.300 1 340 76 76 LEU H H 8.786 0.030 1 341 76 76 LEU C C 178.902 0.300 1 342 76 76 LEU CA C 54.305 0.300 1 343 76 76 LEU CB C 44.288 0.300 1 344 76 76 LEU N N 125.337 0.300 1 345 77 77 GLY H H 8.325 0.030 1 346 77 77 GLY C C 171.067 0.300 1 347 77 77 GLY CA C 44.749 0.300 1 348 77 77 GLY N N 108.964 0.300 1 349 78 78 ALA H H 8.117 0.030 1 350 78 78 ALA C C 179.024 0.300 1 351 78 78 ALA CA C 50.494 0.300 1 352 78 78 ALA CB C 20.472 0.300 1 353 78 78 ALA N N 119.297 0.300 1 354 79 79 PHE H H 8.960 0.030 1 355 79 79 PHE C C 172.801 0.300 1 356 79 79 PHE CA C 55.945 0.300 1 357 79 79 PHE CB C 41.017 0.300 1 358 79 79 PHE N N 117.995 0.300 1 359 80 80 SER H H 8.463 0.030 1 360 80 80 SER C C 175.136 0.300 1 361 80 80 SER CA C 56.615 0.300 1 362 80 80 SER CB C 66.175 0.300 1 363 80 80 SER N N 113.892 0.300 1 364 81 81 ARG H H 8.884 0.030 1 365 81 81 ARG C C 177.845 0.300 1 366 81 81 ARG CA C 58.544 0.300 1 367 81 81 ARG CB C 30.116 0.300 1 368 81 81 ARG N N 121.360 0.300 1 369 82 82 GLY H H 10.340 0.030 1 370 82 82 GLY C C 174.569 0.300 1 371 82 82 GLY CA C 45.294 0.300 1 372 82 82 GLY N N 112.752 0.300 1 373 83 83 GLN H H 7.889 0.030 1 374 83 83 GLN C C 176.202 0.300 1 375 83 83 GLN CA C 57.622 0.300 1 376 83 83 GLN CB C 31.877 0.300 1 377 83 83 GLN N N 119.032 0.300 1 378 84 84 MET H H 9.106 0.030 1 379 84 84 MET C C 175.544 0.300 1 380 84 84 MET CA C 52.422 0.300 1 381 84 84 MET CB C 33.470 0.300 1 382 84 84 MET N N 118.344 0.300 1 383 85 85 GLN H H 8.422 0.030 1 384 85 85 GLN C C 178.627 0.300 1 385 85 85 GLN CA C 56.938 0.300 1 386 85 85 GLN CB C 29.780 0.300 1 387 85 85 GLN N N 118.443 0.300 1 388 86 86 LYS H H 9.170 0.030 1 389 86 86 LYS C C 174.049 0.300 1 390 86 86 LYS CA C 60.885 0.300 1 391 86 86 LYS CB C 29.948 0.300 1 392 86 86 LYS N N 126.179 0.300 1 393 87 87 PRO C C 180.115 0.300 1 394 87 87 PRO CA C 65.672 0.300 1 395 87 87 PRO CB C 31.290 0.300 1 396 88 88 PHE H H 6.998 0.030 1 397 88 88 PHE C C 178.242 0.300 1 398 88 88 PHE CA C 60.557 0.300 1 399 88 88 PHE CB C 40.514 0.300 1 400 88 88 PHE N N 116.404 0.300 1 401 89 89 GLU H H 8.718 0.030 1 402 89 89 GLU C C 177.528 0.300 1 403 89 89 GLU CA C 60.225 0.300 1 404 89 89 GLU CB C 30.703 0.300 1 405 89 89 GLU N N 122.947 0.300 1 406 90 90 ASP H H 9.191 0.030 1 407 90 90 ASP C C 179.308 0.300 1 408 90 90 ASP CA C 57.202 0.300 1 409 90 90 ASP CB C 39.676 0.300 1 410 90 90 ASP N N 118.963 0.300 1 411 91 91 ALA H H 7.109 0.030 1 412 91 91 ALA C C 179.603 0.300 1 413 91 91 ALA CA C 54.365 0.300 1 414 91 91 ALA CB C 20.304 0.300 1 415 91 91 ALA N N 119.016 0.300 1 416 92 92 SER H H 7.900 0.030 1 417 92 92 SER C C 174.897 0.300 1 418 92 92 SER CA C 63.157 0.300 1 419 92 92 SER CB C 63.324 0.300 1 420 92 92 SER N N 113.853 0.300 1 421 93 93 PHE H H 8.265 0.030 1 422 93 93 PHE C C 175.883 0.300 1 423 93 93 PHE CA C 61.060 0.300 1 424 93 93 PHE CB C 38.921 0.300 1 425 93 93 PHE N N 115.149 0.300 1 426 94 94 ALA H H 6.978 0.030 1 427 94 94 ALA C C 177.963 0.300 1 428 94 94 ALA CA C 51.941 0.300 1 429 94 94 ALA CB C 19.927 0.300 1 430 94 94 ALA N N 119.032 0.300 1 431 95 95 LEU H H 6.924 0.030 1 432 95 95 LEU C C 177.873 0.300 1 433 95 95 LEU CA C 54.514 0.300 1 434 95 95 LEU CB C 43.030 0.300 1 435 95 95 LEU N N 119.985 0.300 1 436 96 96 ARG H H 8.864 0.030 1 437 96 96 ARG C C 177.029 0.300 1 438 96 96 ARG CA C 55.022 0.300 1 439 96 96 ARG CB C 30.996 0.300 1 440 96 96 ARG N N 122.096 0.300 1 441 97 97 THR H H 8.473 0.030 1 442 97 97 THR C C 175.748 0.300 1 443 97 97 THR CA C 65.337 0.300 1 444 97 97 THR CB C 67.433 0.300 1 445 97 97 THR N N 117.016 0.300 1 446 98 98 GLY H H 8.934 0.030 1 447 98 98 GLY C C 173.164 0.300 1 448 98 98 GLY CA C 45.043 0.300 1 449 98 98 GLY N N 115.727 0.300 1 450 99 99 GLU H H 8.166 0.030 1 451 99 99 GLU C C 173.028 0.300 1 452 99 99 GLU CA C 55.475 0.300 1 453 99 99 GLU CB C 32.464 0.300 1 454 99 99 GLU N N 122.127 0.300 1 455 100 100 MET H H 8.235 0.030 1 456 100 100 MET C C 176.440 0.300 1 457 100 100 MET CA C 52.842 0.300 1 458 100 100 MET CB C 37.495 0.300 1 459 100 100 MET N N 123.061 0.300 1 460 101 101 SER H H 9.705 0.030 1 461 101 101 SER C C 174.764 0.300 1 462 101 101 SER CA C 59.047 0.300 1 463 101 101 SER CB C 65.085 0.300 1 464 101 101 SER N N 123.529 0.300 1 465 102 102 GLY H H 7.779 0.030 1 466 102 102 GLY CA C 44.707 0.300 1 467 102 102 GLY N N 103.293 0.300 1 468 103 103 PRO C C 177.058 0.300 1 469 103 103 PRO CA C 63.658 0.300 1 470 103 103 PRO CB C 31.625 0.300 1 471 104 104 VAL H H 9.212 0.030 1 472 104 104 VAL C C 174.909 0.300 1 473 104 104 VAL CA C 61.144 0.300 1 474 104 104 VAL CB C 35.315 0.300 1 475 104 104 VAL N N 127.259 0.300 1 476 105 105 PHE H H 9.097 0.030 1 477 105 105 PHE C C 176.009 0.300 1 478 105 105 PHE CA C 57.743 0.300 1 479 105 105 PHE CB C 39.760 0.300 1 480 105 105 PHE N N 127.861 0.300 1 481 106 106 THR H H 9.104 0.030 1 482 106 106 THR C C 175.659 0.300 1 483 106 106 THR CA C 60.473 0.300 1 484 106 106 THR CB C 72.088 0.300 1 485 106 106 THR N N 112.854 0.300 1 486 107 107 ASP H H 9.091 0.030 1 487 107 107 ASP C C 178.207 0.300 1 488 107 107 ASP CA C 56.028 0.300 1 489 107 107 ASP CB C 40.263 0.300 1 490 107 107 ASP N N 118.211 0.300 1 491 108 108 SER H H 8.912 0.030 1 492 108 108 SER C C 175.058 0.300 1 493 108 108 SER CA C 60.054 0.300 1 494 108 108 SER CB C 63.576 0.300 1 495 108 108 SER N N 114.220 0.300 1 496 109 109 GLY H H 7.707 0.030 1 497 109 109 GLY C C 169.286 0.300 1 498 109 109 GLY CA C 45.378 0.300 1 499 109 109 GLY N N 109.967 0.300 1 500 110 110 ILE H H 8.296 0.030 1 501 110 110 ILE C C 173.889 0.300 1 502 110 110 ILE CA C 59.790 0.300 1 503 110 110 ILE CB C 39.424 0.300 1 504 110 110 ILE N N 123.041 0.300 1 505 111 111 HIS H H 9.949 0.030 1 506 111 111 HIS C C 176.973 0.300 1 507 111 111 HIS CA C 53.594 0.300 1 508 111 111 HIS CB C 32.296 0.300 1 509 111 111 HIS N N 124.434 0.300 1 510 112 112 ILE H H 8.507 0.030 1 511 112 112 ILE C C 175.458 0.300 1 512 112 112 ILE CA C 62.160 0.300 1 513 112 112 ILE CB C 41.688 0.300 1 514 112 112 ILE N N 115.427 0.300 1 515 113 113 ILE H H 8.790 0.030 1 516 113 113 ILE C C 172.691 0.300 1 517 113 113 ILE CA C 60.824 0.300 1 518 113 113 ILE CB C 41.688 0.300 1 519 113 113 ILE N N 125.431 0.300 1 520 114 114 LEU H H 8.791 0.030 1 521 114 114 LEU C C 175.488 0.300 1 522 114 114 LEU CA C 52.926 0.300 1 523 114 114 LEU CB C 45.546 0.300 1 524 114 114 LEU N N 128.664 0.300 1 525 115 115 ARG H H 8.106 0.030 1 526 115 115 ARG C C 176.168 0.300 1 527 115 115 ARG CA C 56.196 0.300 1 528 115 115 ARG CB C 29.948 0.300 1 529 115 115 ARG N N 127.356 0.300 1 530 116 116 THR H H 9.069 0.030 1 531 116 116 THR C C 175.420 0.300 1 532 116 116 THR CA C 61.797 0.300 1 533 116 116 THR CB C 69.111 0.300 1 534 116 116 THR N N 120.975 0.300 1 535 117 117 GLU H H 7.974 0.030 1 536 117 117 GLU C C 181.429 0.300 1 537 117 117 GLU CA C 58.041 0.300 1 538 117 117 GLU CB C 33.638 0.300 1 539 117 117 GLU N N 126.294 0.300 1 stop_ save_