data_26752 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Backbone 1H, 13C and 15N resonance assignments of the OB domain of the single stranded DNA binding protein hSSB1 (NABP2/OBFC2B) ; _BMRB_accession_number 26752 _BMRB_flat_file_name bmr26752.str _Entry_type original _Submission_date 2016-03-07 _Accession_date 2016-03-07 _Entry_origination author _NMR_STAR_version 2.1.1 _Experimental_method NMR _Details . loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Kariawasam Ruvini . . 2 Touma Christine . . 3 Cubeddu Liza . . 4 Gamsjaeger Roland . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 116 "13C chemical shifts" 350 "15N chemical shifts" 116 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2016-10-26 update BMRB 'update entry citation' 2016-07-14 original author 'original release' stop_ _Original_release_date 2016-07-14 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; Backbone 1H, 13C and 15N resonance assignments of the OB domain of the single stranded DNA-binding protein hSSB1 (NABP2/OBFC2B) and chemical shift mapping of the DNA-binding interface ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 27193589 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Kariawasam Ruvini . . 2 Touma Christine . . 3 Cubeddu Liza . . 4 Gamsjaeger Roland . . stop_ _Journal_abbreviation 'Biomol. NMR Assign.' _Journal_volume 10 _Journal_issue 2 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 297 _Page_last 300 _Year 2016 _Details . save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name hSSB1 _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'hSSB1 protein' $hSSB1 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_hSSB1 _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common hSSB1 _Molecular_mass . _Mol_thiol_state 'all free' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 128 _Mol_residue_sequence ; GPLGSMTTETFVKDIKPGLK NLNLIFIVLETGRVTKTKDG HEVRTCKVADKTGSINISVW DDVGNLIQPGDIIRLTKGYA SVFKGCLTLYTGRGGDLQKI GEFCMVYSEVPNFSEPNPEY STQQAPNK ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 -4 GLY 2 -3 PRO 3 -2 LEU 4 -1 GLY 5 0 SER 6 1 MET 7 2 THR 8 3 THR 9 4 GLU 10 5 THR 11 6 PHE 12 7 VAL 13 8 LYS 14 9 ASP 15 10 ILE 16 11 LYS 17 12 PRO 18 13 GLY 19 14 LEU 20 15 LYS 21 16 ASN 22 17 LEU 23 18 ASN 24 19 LEU 25 20 ILE 26 21 PHE 27 22 ILE 28 23 VAL 29 24 LEU 30 25 GLU 31 26 THR 32 27 GLY 33 28 ARG 34 29 VAL 35 30 THR 36 31 LYS 37 32 THR 38 33 LYS 39 34 ASP 40 35 GLY 41 36 HIS 42 37 GLU 43 38 VAL 44 39 ARG 45 40 THR 46 41 CYS 47 42 LYS 48 43 VAL 49 44 ALA 50 45 ASP 51 46 LYS 52 47 THR 53 48 GLY 54 49 SER 55 50 ILE 56 51 ASN 57 52 ILE 58 53 SER 59 54 VAL 60 55 TRP 61 56 ASP 62 57 ASP 63 58 VAL 64 59 GLY 65 60 ASN 66 61 LEU 67 62 ILE 68 63 GLN 69 64 PRO 70 65 GLY 71 66 ASP 72 67 ILE 73 68 ILE 74 69 ARG 75 70 LEU 76 71 THR 77 72 LYS 78 73 GLY 79 74 TYR 80 75 ALA 81 76 SER 82 77 VAL 83 78 PHE 84 79 LYS 85 80 GLY 86 81 CYS 87 82 LEU 88 83 THR 89 84 LEU 90 85 TYR 91 86 THR 92 87 GLY 93 88 ARG 94 89 GLY 95 90 GLY 96 91 ASP 97 92 LEU 98 93 GLN 99 94 LYS 100 95 ILE 101 96 GLY 102 97 GLU 103 98 PHE 104 99 CYS 105 100 MET 106 101 VAL 107 102 TYR 108 103 SER 109 104 GLU 110 105 VAL 111 106 PRO 112 107 ASN 113 108 PHE 114 109 SER 115 110 GLU 116 111 PRO 117 112 ASN 118 113 PRO 119 114 GLU 120 115 TYR 121 116 SER 122 117 THR 123 118 GLN 124 119 GLN 125 120 ALA 126 121 PRO 127 122 ASN 128 123 LYS 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 $hSSB1 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 $hSSB1 'recombinant technology' . Escherichia coli . pGex6P 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 _Concentration_min_value _Concentration_max_value _Isotopic_labeling $hSSB1 . uM 200 800 '[U-100% 13C; U-100% 15N]' H2O 90 % . . 'natural abundance' D2O 10 % . . 'natural abundance' NaCl 50 mM . . 'natural abundance' MES 10 mM . . 'natural abundance' TCEP 3 mM . . '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_SPARKY _Saveframe_category software _Name SPARKY _Version . loop_ _Vendor _Address _Electronic_address Goddard . . 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 600 _Details . save_ save_spectrometer_2 _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_HNCACB_2 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCACB' _Sample_label $sample_1 save_ save_3D_CBCA(CO)NH_3 _Saveframe_category NMR_applied_experiment _Experiment_name '3D CBCA(CO)NH' _Sample_label $sample_1 save_ save_3D_HNCO_4 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCO' _Sample_label $sample_1 save_ save_3D_HN(CA)CO_5 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HN(CA)CO' _Sample_label $sample_1 save_ save_3D_1H-15N_NOESY_6 _Saveframe_category NMR_applied_experiment _Experiment_name '3D 1H-15N NOESY' _Sample_label $sample_1 save_ save_2D_1H-13C_HSQC_7 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-13C HSQC' _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' 60 . mM pH 6.0 . pH pressure 1 . atm temperature 298 . 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 na indirect . . . 0.251449530 DSS H 1 'methyl protons' ppm 0.00 internal direct . . . 1.000000000 DSS N 15 'methyl protons' ppm 0.00 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_1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Experiment_label '2D 1H-15N HSQC' '3D HNCACB' '3D CBCA(CO)NH' '3D HNCO' '3D HN(CA)CO' '3D 1H-15N NOESY' '2D 1H-13C HSQC' 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 'hSSB1 protein' _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 1 6 MET H H 8.465 0.001 1 2 1 6 MET C C 176.08 0.027 1 3 1 6 MET CA C 55.538 0.011 1 4 1 6 MET CB C 32.816 0.039 1 5 1 6 MET N N 122.36 0.043 1 6 2 7 THR H H 8.157 0.001 1 7 2 7 THR C C 174.421 0.039 1 8 2 7 THR CA C 61.645 0.114 1 9 2 7 THR CB C 69.921 0.063 1 10 2 7 THR N N 115.384 0.026 1 11 3 8 THR H H 8.263 0.001 1 12 3 8 THR C C 174.107 0.069 1 13 3 8 THR CA C 61.617 0.119 1 14 3 8 THR CB C 69.891 0.072 1 15 3 8 THR N N 117.194 0.008 1 16 4 9 GLU H H 8.426 0.001 1 17 4 9 GLU C C 175.489 0.047 1 18 4 9 GLU CA C 56.579 0.044 1 19 4 9 GLU CB C 30.917 0.051 1 20 4 9 GLU N N 124.277 0.045 1 21 5 10 THR H H 8.168 0.002 1 22 5 10 THR C C 171.674 0.115 1 23 5 10 THR CA C 61.709 0.13 1 24 5 10 THR CB C 70.731 0.033 1 25 5 10 THR N N 119.163 0.059 1 26 6 11 PHE H H 8.937 0.005 1 27 6 11 PHE C C 177.299 0.035 1 28 6 11 PHE CA C 56.723 0.103 1 29 6 11 PHE CB C 42.354 0.069 1 30 6 11 PHE N N 123.497 0.035 1 31 7 12 VAL H H 10.367 0.005 1 32 7 12 VAL C C 178.322 0 1 33 7 12 VAL CA C 67.158 0.074 1 34 7 12 VAL CB C 30.918 0.134 1 35 7 12 VAL N N 124.627 0.097 1 36 8 13 LYS H H 8.084 0.003 1 37 8 13 LYS C C 176.149 0.076 1 38 8 13 LYS CA C 56.871 0.047 1 39 8 13 LYS CB C 32.092 0.008 1 40 8 13 LYS N N 113.268 0.082 1 41 9 14 ASP H H 7.904 0.005 1 42 9 14 ASP C C 176.156 0 1 43 9 14 ASP CA C 54.699 0.112 1 44 9 14 ASP CB C 42.185 0.015 1 45 9 14 ASP N N 119.96 0.061 1 46 10 15 ILE H H 7.418 0.021 1 47 10 15 ILE C C 174.264 0.053 1 48 10 15 ILE CA C 63.525 0.044 1 49 10 15 ILE CB C 36.377 0.005 1 50 10 15 ILE N N 121.011 0.054 1 51 11 16 LYS H H 6.42 0.002 1 52 11 16 LYS C C 172.673 0 1 53 11 16 LYS CA C 52.537 0 1 54 11 16 LYS CB C 34.062 0 1 55 11 16 LYS N N 124.359 0.082 1 56 12 17 PRO C C 177.097 0.053 1 57 12 17 PRO CA C 63.913 0.063 1 58 12 17 PRO CB C 31.697 0.087 1 59 13 18 GLY H H 8.289 0.004 1 60 13 18 GLY C C 174.812 0.034 1 61 13 18 GLY CA C 45.411 0.041 1 62 13 18 GLY N N 111.472 0.039 1 63 14 19 LEU H H 7.336 0.014 1 64 14 19 LEU C C 176.37 0.098 1 65 14 19 LEU CA C 55.537 0.038 1 66 14 19 LEU CB C 43.096 0.026 1 67 14 19 LEU N N 119.926 0.041 1 68 15 20 LYS H H 8.352 0.008 1 69 15 20 LYS C C 174.836 0.086 1 70 15 20 LYS CA C 54.668 0.098 1 71 15 20 LYS CB C 35.649 0.023 1 72 15 20 LYS N N 119.518 0.079 1 73 16 21 ASN H H 8.771 0.003 1 74 16 21 ASN C C 174.525 0.043 1 75 16 21 ASN CA C 54.275 0 1 76 16 21 ASN CB C 37.58 0.046 1 77 16 21 ASN N N 116.517 0.152 1 78 17 22 LEU H H 8.952 0.001 1 79 17 22 LEU C C 175.906 0 1 80 17 22 LEU CA C 54.837 0.055 1 81 17 22 LEU CB C 43.607 0.067 1 82 17 22 LEU N N 118.654 0.038 1 83 18 23 ASN H H 8.496 0.006 1 84 18 23 ASN C C 174.243 0.031 1 85 18 23 ASN CA C 51.477 0.006 1 86 18 23 ASN CB C 40.133 0.019 1 87 18 23 ASN N N 122.249 0.046 1 88 19 24 LEU H H 8.52 0.003 1 89 19 24 LEU C C 174.118 0 1 90 19 24 LEU CA C 54.921 0.021 1 91 19 24 LEU CB C 47.102 0.055 1 92 19 24 LEU N N 122.202 0.042 1 93 20 25 ILE H H 7.798 0.013 1 94 20 25 ILE C C 174.63 0.037 1 95 20 25 ILE CA C 59.856 0.08 1 96 20 25 ILE CB C 40.803 0.078 1 97 20 25 ILE N N 119.233 0.092 1 98 21 26 PHE H H 8.392 0.003 1 99 21 26 PHE C C 172.899 0.011 1 100 21 26 PHE CA C 54.15 0.049 1 101 21 26 PHE CB C 41.027 0.07 1 102 21 26 PHE N N 120.827 0.124 1 103 22 27 ILE H H 9.381 0.014 1 104 22 27 ILE C C 174.59 0.042 1 105 22 27 ILE CA C 57.705 0.101 1 106 22 27 ILE CB C 40.954 0.07 1 107 22 27 ILE N N 118.256 0.062 1 108 23 28 VAL H H 8.72 0.002 1 109 23 28 VAL C C 176.03 0.006 1 110 23 28 VAL CA C 62.956 0.151 1 111 23 28 VAL CB C 31.353 0.058 1 112 23 28 VAL N N 125.921 0.047 1 113 24 29 LEU H H 9.463 0.006 1 114 24 29 LEU C C 177.022 0.03 1 115 24 29 LEU CA C 55.771 0.015 1 116 24 29 LEU CB C 42.442 0 1 117 24 29 LEU N N 128.914 0.069 1 118 25 30 GLU H H 7.679 0.01 1 119 25 30 GLU C C 175.234 0.087 1 120 25 30 GLU CA C 55.072 0.076 1 121 25 30 GLU CB C 34.428 0.052 1 122 25 30 GLU N N 115.453 0.053 1 123 26 31 THR H H 8.989 0.004 1 124 26 31 THR C C 174.507 0.027 1 125 26 31 THR CA C 59.685 0.005 1 126 26 31 THR CB C 69.708 0.093 1 127 26 31 THR N N 114.502 0.018 1 128 27 32 GLY H H 7.848 0.012 1 129 27 32 GLY C C 173.396 0.043 1 130 27 32 GLY CA C 44.884 0.036 1 131 27 32 GLY N N 111.375 0.057 1 132 28 33 ARG H H 8.323 0.001 1 133 28 33 ARG C C 176.683 0 1 134 28 33 ARG CA C 55.851 0.106 1 135 28 33 ARG CB C 31.219 0.021 1 136 28 33 ARG N N 119.376 0.057 1 137 29 34 VAL H H 8.54 0.009 1 138 29 34 VAL C C 176.401 0.049 1 139 29 34 VAL CA C 62.597 0.063 1 140 29 34 VAL CB C 32.999 0.088 1 141 29 34 VAL N N 123.94 0.075 1 142 30 35 THR H H 8.986 0.002 1 143 30 35 THR C C 172.848 0.01 1 144 30 35 THR CA C 61.181 0.052 1 145 30 35 THR CB C 71.205 0.046 1 146 30 35 THR N N 122.551 0.044 1 147 31 36 LYS H H 8.547 0.01 1 148 31 36 LYS C C 177.769 0.039 1 149 31 36 LYS CA C 54.97 0.028 1 150 31 36 LYS CB C 33.811 0.02 1 151 31 36 LYS N N 124.052 0.04 1 152 32 37 THR H H 8.955 0.002 1 153 32 37 THR C C 177.09 0.025 1 154 32 37 THR CA C 60.85 0.045 1 155 32 37 THR CB C 70.97 0.07 1 156 32 37 THR N N 116.17 0.076 1 157 33 38 LYS H H 9.055 0.009 1 158 33 38 LYS C C 176.939 0.088 1 159 33 38 LYS CA C 58.676 0.092 1 160 33 38 LYS CB C 32.142 0.003 1 161 33 38 LYS N N 122.003 0.089 1 162 34 39 ASP H H 8.212 0.001 1 163 34 39 ASP C C 176.436 0.087 1 164 34 39 ASP CA C 52.972 0.051 1 165 34 39 ASP CB C 39.807 0 1 166 34 39 ASP N N 115.143 0.051 1 167 35 40 GLY H H 7.844 0.001 1 168 35 40 GLY C C 174.804 0.052 1 169 35 40 GLY CA C 46.349 0.045 1 170 35 40 GLY N N 106.446 0.059 1 171 36 41 HIS H H 7.781 0.001 1 172 36 41 HIS C C 173.879 0.057 1 173 36 41 HIS CA C 55.269 0.03 1 174 36 41 HIS CB C 30.293 0.115 1 175 36 41 HIS N N 117.704 0.038 1 176 37 42 GLU H H 8.954 0.004 1 177 37 42 GLU C C 174.835 0.079 1 178 37 42 GLU CA C 55.577 0.049 1 179 37 42 GLU CB C 32.619 0.014 1 180 37 42 GLU N N 121.479 0.076 1 181 38 43 VAL H H 8.817 0.002 1 182 38 43 VAL C C 173.789 0.071 1 183 38 43 VAL CA C 59.966 0.096 1 184 38 43 VAL CB C 34.823 0.021 1 185 38 43 VAL N N 121.764 0.049 1 186 39 44 ARG H H 8.504 0.002 1 187 39 44 ARG C C 174.395 0.031 1 188 39 44 ARG CA C 54.32 0.072 1 189 39 44 ARG CB C 34.287 0.079 1 190 39 44 ARG N N 124.057 0.068 1 191 40 45 THR H H 8.978 0.002 1 192 40 45 THR C C 175.113 0.088 1 193 40 45 THR CA C 61.963 0.067 1 194 40 45 THR CB C 69.383 0.019 1 195 40 45 THR N N 120.967 0.048 1 196 41 46 CYS H H 9.285 0.003 1 197 41 46 CYS C C 171.895 0.021 1 198 41 46 CYS CA C 56.63 0.015 1 199 41 46 CYS CB C 29.509 0.056 1 200 41 46 CYS N N 124.434 0.049 1 201 42 47 LYS H H 8.415 0.003 1 202 42 47 LYS C C 175.489 0.065 1 203 42 47 LYS CA C 55.899 0.038 1 204 42 47 LYS CB C 35.123 0.023 1 205 42 47 LYS N N 125.645 0.035 1 206 43 48 VAL H H 9.267 0.023 1 207 43 48 VAL C C 173.885 0.057 1 208 43 48 VAL CA C 58.631 0.102 1 209 43 48 VAL CB C 34.888 0.021 1 210 43 48 VAL N N 123.266 0.031 1 211 44 49 ALA H H 8.844 0.002 1 212 44 49 ALA C C 175.901 0.024 1 213 44 49 ALA CA C 51.923 0.087 1 214 44 49 ALA CB C 25.455 0.039 1 215 44 49 ALA N N 119.596 0.075 1 216 45 50 ASP H H 9.189 0.003 1 217 45 50 ASP C C 178.461 0.025 1 218 45 50 ASP CA C 53.098 0.135 1 219 45 50 ASP CB C 42.78 0.064 1 220 45 50 ASP N N 119.821 0.056 1 221 46 51 LYS H H 9.025 0.019 1 222 46 51 LYS C C 176.071 0.038 1 223 46 51 LYS CA C 59.684 0.006 1 224 46 51 LYS CB C 31.539 0.069 1 225 46 51 LYS N N 117.459 0.078 1 226 47 52 THR H H 9.847 0.009 1 227 47 52 THR C C 172.954 0.004 1 228 47 52 THR CA C 62.198 0.055 1 229 47 52 THR CB C 69.774 0.027 1 230 47 52 THR N N 112.909 0.107 1 231 48 53 GLY H H 7.702 0.001 1 232 48 53 GLY C C 171.341 0 1 233 48 53 GLY CA C 45.175 0.007 1 234 48 53 GLY N N 109.979 0.063 1 235 49 54 SER H H 8.907 0.002 1 236 49 54 SER C C 172.643 0.032 1 237 49 54 SER CA C 56.056 0.135 1 238 49 54 SER CB C 68.874 0.045 1 239 49 54 SER N N 108.349 0.047 1 240 50 55 ILE H H 9.17 0.001 1 241 50 55 ILE C C 171.808 0.058 1 242 50 55 ILE CA C 60.667 0.002 1 243 50 55 ILE CB C 41.712 0.089 1 244 50 55 ILE N N 118.805 0.029 1 245 51 56 ASN H H 8.71 0.003 1 246 51 56 ASN C C 175.124 0.038 1 247 51 56 ASN CA C 51.45 0.043 1 248 51 56 ASN CB C 39.082 0.056 1 249 51 56 ASN N N 122.004 0.092 1 250 52 57 ILE H H 8.98 0.003 1 251 52 57 ILE C C 173.188 0.039 1 252 52 57 ILE CA C 57.4 0.077 1 253 52 57 ILE CB C 41.633 0 1 254 52 57 ILE N N 117.488 0.072 1 255 53 58 SER H H 7.995 0.004 1 256 53 58 SER C C 173.282 0.013 1 257 53 58 SER CA C 57.166 0.054 1 258 53 58 SER CB C 64.034 0.031 1 259 53 58 SER N N 122.255 0.089 1 260 54 59 VAL H H 8.888 0.003 1 261 54 59 VAL C C 175.278 0 1 262 54 59 VAL CA C 60.785 0.003 1 263 54 59 VAL CB C 34.356 0.018 1 264 54 59 VAL N N 123.51 0.083 1 265 55 60 TRP H H 8.842 0.01 1 266 55 60 TRP C C 176.969 0.087 1 267 55 60 TRP CA C 56.869 0.034 1 268 55 60 TRP CB C 31.465 0.104 1 269 55 60 TRP N N 127.032 0.09 1 270 56 61 ASP H H 9.443 0.008 1 271 56 61 ASP C C 176.372 0.051 1 272 56 61 ASP CA C 56.198 0.046 1 273 56 61 ASP CB C 40.458 0.032 1 274 56 61 ASP N N 120.139 0.088 1 275 57 62 ASP H H 8.534 0.013 1 276 57 62 ASP C C 178.026 0.072 1 277 57 62 ASP CA C 56.665 0.095 1 278 57 62 ASP CB C 40.275 0.041 1 279 57 62 ASP N N 120.991 0.099 1 280 58 63 VAL H H 8.014 0.001 1 281 58 63 VAL C C 177.916 0.028 1 282 58 63 VAL CA C 64.823 0.015 1 283 58 63 VAL CB C 31.769 0 1 284 58 63 VAL N N 119.189 0.101 1 285 59 64 GLY H H 7.902 0.004 1 286 59 64 GLY C C 174.453 0 1 287 59 64 GLY CA C 46.507 0.034 1 288 59 64 GLY N N 107.132 0.054 1 289 60 65 ASN H H 7.75 0.004 1 290 60 65 ASN C C 175.65 0.009 1 291 60 65 ASN CA C 54.564 0.043 1 292 60 65 ASN CB C 38.822 0.044 1 293 60 65 ASN N N 116.966 0.033 1 294 61 66 LEU H H 7.828 0.003 1 295 61 66 LEU C C 177.709 0.065 1 296 61 66 LEU CA C 55.464 0.012 1 297 61 66 LEU CB C 42.935 0.05 1 298 61 66 LEU N N 119.442 0.053 1 299 62 67 ILE H H 7.22 0.014 1 300 62 67 ILE C C 174.448 0.016 1 301 62 67 ILE CA C 61.976 0.108 1 302 62 67 ILE CB C 39.151 0.079 1 303 62 67 ILE N N 119.366 0.062 1 304 63 68 GLN H H 8.746 0.003 1 305 63 68 GLN CA C 52.463 0 1 306 63 68 GLN CB C 30.979 0 1 307 63 68 GLN N N 125.232 0.08 1 308 64 69 PRO C C 177.067 0.042 1 309 64 69 PRO CA C 63.663 0.036 1 310 64 69 PRO CB C 31.198 0.007 1 311 65 70 GLY H H 9.391 0.002 1 312 65 70 GLY C C 173.512 0 1 313 65 70 GLY CA C 44.65 0.011 1 314 65 70 GLY N N 114.893 0.043 1 315 66 71 ASP H H 7.907 0.002 1 316 66 71 ASP C C 174.706 0.032 1 317 66 71 ASP CA C 56.177 0.046 1 318 66 71 ASP CB C 41.459 0.112 1 319 66 71 ASP N N 121.684 0.029 1 320 67 72 ILE H H 8.389 0.003 1 321 67 72 ILE C C 175.286 0 1 322 67 72 ILE CA C 60.321 0.121 1 323 67 72 ILE CB C 37.576 0.098 1 324 67 72 ILE N N 122.603 0.084 1 325 68 73 ILE H H 9.131 0.005 1 326 68 73 ILE C C 172.706 0 1 327 68 73 ILE CA C 57.41 0 1 328 68 73 ILE CB C 40.808 0.072 1 329 68 73 ILE N N 128.465 0.07 1 330 69 74 ARG H H 8.894 0.005 1 331 69 74 ARG C C 175.136 0 1 332 69 74 ARG CA C 54.164 0.015 1 333 69 74 ARG CB C 32.916 0.021 1 334 69 74 ARG N N 123.395 0.115 1 335 70 75 LEU H H 9.123 0.004 1 336 70 75 LEU C C 175.262 0.131 1 337 70 75 LEU CA C 53.435 0.087 1 338 70 75 LEU CB C 45.327 0.008 1 339 70 75 LEU N N 133.476 0.013 1 340 71 76 THR H H 8.716 0.003 1 341 71 76 THR C C 173.202 0.035 1 342 71 76 THR CA C 60.039 0.095 1 343 71 76 THR CB C 71.314 0.069 1 344 71 76 THR N N 117.992 0.14 1 345 72 77 LYS H H 8.19 0.002 1 346 72 77 LYS C C 177.118 0.049 1 347 72 77 LYS CA C 57.766 0.021 1 348 72 77 LYS CB C 30.593 0.033 1 349 72 77 LYS N N 117.06 0.089 1 350 73 78 GLY H H 9.591 0.014 1 351 73 78 GLY C C 172.517 0.019 1 352 73 78 GLY CA C 45.3 0.002 1 353 73 78 GLY N N 108.107 0.053 1 354 74 79 TYR H H 8.765 0.001 1 355 74 79 TYR C C 172.03 0.041 1 356 74 79 TYR CA C 56.609 0.058 1 357 74 79 TYR CB C 40.97 0.113 1 358 74 79 TYR N N 115.675 0.034 1 359 75 80 ALA H H 8.223 0.007 1 360 75 80 ALA C C 177.631 0.02 1 361 75 80 ALA CA C 49.982 0.014 1 362 75 80 ALA CB C 23.426 0.046 1 363 75 80 ALA N N 121.257 0.059 1 364 76 81 SER H H 9.164 0.002 1 365 76 81 SER C C 172.29 0.044 1 366 76 81 SER CA C 56.548 0.017 1 367 76 81 SER CB C 65.74 0.056 1 368 76 81 SER N N 117.806 0.078 1 369 77 82 VAL H H 8.741 0.002 1 370 77 82 VAL C C 175.107 0.039 1 371 77 82 VAL CA C 62.608 0.072 1 372 77 82 VAL CB C 32.379 0.043 1 373 77 82 VAL N N 122.93 0.036 1 374 78 83 PHE H H 8.731 0.013 1 375 78 83 PHE C C 175.041 0.006 1 376 78 83 PHE CA C 56.891 0.084 1 377 78 83 PHE CB C 41.175 0.045 1 378 78 83 PHE N N 129.745 0.079 1 379 79 84 LYS H H 9.313 0.012 1 380 79 84 LYS C C 176.394 0.049 1 381 79 84 LYS CA C 57.09 0.043 1 382 79 84 LYS CB C 29.918 0.022 1 383 79 84 LYS N N 129.85 0.056 1 384 80 85 GLY H H 8.152 0.006 1 385 80 85 GLY C C 173.594 0.13 1 386 80 85 GLY CA C 45.418 0.065 1 387 80 85 GLY N N 102.702 0.036 1 388 81 86 CYS H H 7.717 0.002 1 389 81 86 CYS C C 175.902 0.01 1 390 81 86 CYS CA C 57.389 0.13 1 391 81 86 CYS CB C 30.15 0.092 1 392 81 86 CYS N N 117.726 0.032 1 393 82 87 LEU H H 9.735 0.003 1 394 82 87 LEU C C 174.595 0.095 1 395 82 87 LEU CA C 57.035 0.008 1 396 82 87 LEU CB C 41.578 0.072 1 397 82 87 LEU N N 133.725 0.053 1 398 83 88 THR H H 9.035 0.003 1 399 83 88 THR C C 171.105 0.048 1 400 83 88 THR CA C 62.853 0.153 1 401 83 88 THR CB C 72.951 0.128 1 402 83 88 THR N N 125.354 0.094 1 403 84 89 LEU H H 8.486 0.005 1 404 84 89 LEU C C 173.663 0 1 405 84 89 LEU CA C 53.417 0.093 1 406 84 89 LEU CB C 44.757 0.062 1 407 84 89 LEU N N 125.441 0.1 1 408 85 90 TYR H H 8.651 0.005 1 409 85 90 TYR C C 175.546 0.07 1 410 85 90 TYR CA C 56.697 0.025 1 411 85 90 TYR CB C 42.243 0.039 1 412 85 90 TYR N N 118.838 0.082 1 413 86 91 THR H H 8.536 0.003 1 414 86 91 THR C C 175.66 0.027 1 415 86 91 THR CA C 62.464 0.069 1 416 86 91 THR CB C 69.033 0.123 1 417 86 91 THR N N 111.582 0.079 1 418 87 92 GLY H H 8.358 0.002 1 419 87 92 GLY C C 174.209 0 1 420 87 92 GLY CA C 44.639 0.056 1 421 87 92 GLY N N 112.096 0.04 1 422 88 93 ARG H H 8.684 0.001 1 423 88 93 ARG C C 177.993 0.011 1 424 88 93 ARG CA C 57.667 0.05 1 425 88 93 ARG CB C 29.708 0.029 1 426 88 93 ARG N N 122.229 0.016 1 427 89 94 GLY H H 8.993 0.003 1 428 89 94 GLY C C 174.796 0.034 1 429 89 94 GLY CA C 45.364 0.038 1 430 89 94 GLY N N 113.214 0.047 1 431 90 95 GLY H H 8.1 0.002 1 432 90 95 GLY C C 172.481 0.084 1 433 90 95 GLY CA C 45.216 0.019 1 434 90 95 GLY N N 109.124 0.018 1 435 91 96 ASP H H 8.313 0.002 1 436 91 96 ASP C C 173.495 0.017 1 437 91 96 ASP CA C 53.423 0.028 1 438 91 96 ASP CB C 44.11 0.043 1 439 91 96 ASP N N 118.878 0.039 1 440 92 97 LEU H H 8.204 0.001 1 441 92 97 LEU C C 175.281 0.015 1 442 92 97 LEU CA C 54.332 0.004 1 443 92 97 LEU CB C 43.976 0.025 1 444 92 97 LEU N N 121.621 0.024 1 445 93 98 GLN H H 8.391 0.002 1 446 93 98 GLN C C 174.581 0.095 1 447 93 98 GLN CA C 53.943 0.119 1 448 93 98 GLN CB C 32.131 0.038 1 449 93 98 GLN N N 122.014 0.07 1 450 94 99 LYS H H 9.02 0.002 1 451 94 99 LYS C C 177.294 0.07 1 452 94 99 LYS CA C 57.142 0.02 1 453 94 99 LYS CB C 32.418 0.077 1 454 94 99 LYS N N 127.264 0.057 1 455 95 100 ILE H H 9.118 0.006 1 456 95 100 ILE C C 175.685 0 1 457 95 100 ILE CA C 60.813 0.023 1 458 95 100 ILE CB C 39.331 0 1 459 95 100 ILE N N 122.183 0.109 1 460 96 101 GLY H H 7.745 0.018 1 461 96 101 GLY C C 171.246 0.019 1 462 96 101 GLY CA C 45.391 0.071 1 463 96 101 GLY N N 109.906 0.015 1 464 97 102 GLU H H 8.57 0.005 1 465 97 102 GLU C C 176.84 0 1 466 97 102 GLU CA C 55.65 0.096 1 467 97 102 GLU CB C 32.176 0 1 468 97 102 GLU N N 117.828 0.05 1 469 98 103 PHE H H 8.209 0.006 1 470 98 103 PHE C C 176.456 0.069 1 471 98 103 PHE CA C 54.024 0 1 472 98 103 PHE CB C 31.099 0.083 1 473 98 103 PHE N N 115.6 0.061 1 474 99 104 CYS H H 8.807 0.015 1 475 99 104 CYS C C 173.469 0.058 1 476 99 104 CYS CA C 57.859 0.056 1 477 99 104 CYS CB C 26.702 0.023 1 478 99 104 CYS N N 121.427 0.039 1 479 100 105 MET H H 7.951 0.006 1 480 100 105 MET C C 174.498 0.044 1 481 100 105 MET CA C 55.556 0.03 1 482 100 105 MET CB C 36.454 0.015 1 483 100 105 MET N N 123.469 0.053 1 484 101 106 VAL H H 8.49 0.003 1 485 101 106 VAL C C 174.752 0.048 1 486 101 106 VAL CA C 63.113 0.082 1 487 101 106 VAL CB C 31.888 0.056 1 488 101 106 VAL N N 126.771 0.034 1 489 102 107 TYR H H 7.904 0.002 1 490 102 107 TYR C C 173.067 0.039 1 491 102 107 TYR CA C 55.363 0.04 1 492 102 107 TYR CB C 40.784 0.041 1 493 102 107 TYR N N 120.547 0.096 1 494 103 108 SER H H 8.411 0.002 1 495 103 108 SER C C 173.641 0.049 1 496 103 108 SER CA C 56.181 0.087 1 497 103 108 SER CB C 65.483 0.076 1 498 103 108 SER N N 115.79 0.061 1 499 104 109 GLU H H 9.19 0.003 1 500 104 109 GLU C C 176.29 0 1 501 104 109 GLU CA C 58.234 0 1 502 104 109 GLU CB C 30.547 0 1 503 104 109 GLU N N 122.606 0.069 1 504 106 111 PRO C C 173.404 0.016 1 505 106 111 PRO CA C 62.527 0.048 1 506 106 111 PRO CB C 33.838 0.059 1 507 107 112 ASN H H 8.408 0.001 1 508 107 112 ASN C C 177.774 0.003 1 509 107 112 ASN CA C 50.824 0.056 1 510 107 112 ASN CB C 37.999 0.014 1 511 107 112 ASN N N 117.691 0.058 1 512 108 113 PHE H H 9.66 0.004 1 513 108 113 PHE C C 177.119 0.068 1 514 108 113 PHE CA C 61.528 0.141 1 515 108 113 PHE CB C 38.211 0.088 1 516 108 113 PHE N N 125.63 0.057 1 517 109 114 SER H H 8.481 0.004 1 518 109 114 SER C C 173.474 0.032 1 519 109 114 SER CA C 59.525 0.002 1 520 109 114 SER CB C 63.878 0.032 1 521 109 114 SER N N 115.893 0.043 1 522 110 115 GLU H H 7.117 0.019 1 523 110 115 GLU C C 174.871 0 1 524 110 115 GLU CA C 55.302 0 1 525 110 115 GLU CB C 29.138 0 1 526 110 115 GLU N N 122.341 0.036 1 527 111 116 PRO C C 176.7 0.031 1 528 111 116 PRO CA C 63.87 0 1 529 111 116 PRO CB C 31.627 0.013 1 530 112 117 ASN H H 8.457 0.001 1 531 112 117 ASN CA C 50.533 0 1 532 112 117 ASN CB C 39.715 0 1 533 112 117 ASN N N 121.881 0.068 1 534 113 118 PRO C C 177.836 0 1 535 113 118 PRO CA C 64.383 0.154 1 536 113 118 PRO CB C 32.2 0 1 537 114 119 GLU H H 8.305 0.001 1 538 114 119 GLU C C 177.445 0.038 1 539 114 119 GLU CA C 57.528 0.098 1 540 114 119 GLU CB C 29.575 0.062 1 541 114 119 GLU N N 118.213 0.03 1 542 115 120 TYR H H 7.8 0.001 1 543 115 120 TYR C C 176.494 0.018 1 544 115 120 TYR CA C 57.005 0.037 1 545 115 120 TYR CB C 38.214 0.073 1 546 115 120 TYR N N 118.555 0.013 1 547 116 121 SER H H 7.927 0.003 1 548 116 121 SER C C 174.754 0.025 1 549 116 121 SER CA C 58.788 0.13 1 550 116 121 SER CB C 63.869 0.008 1 551 116 121 SER N N 116.141 0.082 1 552 117 122 THR H H 8.072 0.001 1 553 117 122 THR CA C 62.138 0.04 1 554 117 122 THR CB C 69.63 0.04 1 555 117 122 THR N N 115.421 0.02 1 556 118 123 GLN H H 8.248 0 1 557 118 123 GLN C C 175.829 0.005 1 558 118 123 GLN CA C 55.963 0.082 1 559 118 123 GLN CB C 29.426 0.021 1 560 118 123 GLN N N 122.501 0.047 1 561 119 124 GLN H H 8.338 0.001 1 562 119 124 GLN C C 175.478 0.092 1 563 119 124 GLN CA C 55.628 0.061 1 564 119 124 GLN CB C 29.63 0.046 1 565 119 124 GLN N N 121.813 0.014 1 566 120 125 ALA H H 8.383 0.001 1 567 120 125 ALA CA C 50.631 0 1 568 120 125 ALA CB C 18.21 0 1 569 120 125 ALA N N 127.175 0.011 1 570 121 126 PRO C C 176.753 0.005 1 571 121 126 PRO CA C 63.071 0.082 1 572 121 126 PRO CB C 32.115 0.047 1 573 122 127 ASN H H 8.463 0.002 1 574 122 127 ASN C C 174.192 0.015 1 575 122 127 ASN CA C 53.386 0.059 1 576 122 127 ASN CB C 38.908 0.044 1 577 122 127 ASN N N 119.018 0.015 1 578 123 128 LYS H H 7.854 0.001 1 579 123 128 LYS C C 181.098 0 1 580 123 128 LYS CA C 57.693 0 1 581 123 128 LYS CB C 33.814 0 1 582 123 128 LYS N N 126.401 0.01 1 stop_ save_