data_27020 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Backbone 1H, 13C, and 15N Chemical Shift Assignments for Human BetaB2-crystallin ; _BMRB_accession_number 27020 _BMRB_flat_file_name bmr27020.str _Entry_type original _Submission_date 2017-02-01 _Accession_date 2017-02-01 _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 Xi Zhaoyong . . 2 Whitley Matthew J. . 3 Gronenborn Angela M. . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 162 "13C chemical shifts" 322 "15N chemical shifts" 162 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2017-03-31 original BMRB . stop_ _Original_release_date 2017-02-01 save_ ############################# # Citation for this entry # ############################# save_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; Human betaB2-Crystallin Forms a Face-en-Face Dimer in Solution: An Integrated NMR and SAXS Study ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 28238532 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Xi Zhaoyong . . 2 Whitley Matthew J. . 3 Gronenborn Angela M. . stop_ _Journal_abbreviation Structure _Journal_name_full 'Structure (London, England : 1993)' _Journal_volume 25 _Journal_issue 3 _Journal_ISSN 1878-4186 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 496 _Page_last 505 _Year 2017 _Details . save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name 'human betaB2-crystallin dimer' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'human betaB2-crystallin, chain 1' $human_betaB2-crystallin 'human betaB2-crystallin, chain 2' $human_betaB2-crystallin 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_human_betaB2-crystallin _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common human_betaB2-crystallin _Molecular_mass . _Mol_thiol_state 'all free' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 204 _Mol_residue_sequence ; ASDHQTQAGKPQSLNPKIII FEQENFQGHSHELNGPCPNL KETGVEKAGSVLVQAGPWVG YEQANCKGEQFVFEKGEYPR WDSWTSSRRTDSLSSLRPIK VDSQEHKIILYENPNFTGKK MEIIDDDVPSFHAHGYQEKV SSVRVQSGTWVGYQYPGYRG LQYLLEKGDYKDSSDFGAPH PQVQSVRRIRDMQWHQRGAF HPSN ; loop_ _Residue_seq_code _Residue_label 1 ALA 2 SER 3 ASP 4 HIS 5 GLN 6 THR 7 GLN 8 ALA 9 GLY 10 LYS 11 PRO 12 GLN 13 SER 14 LEU 15 ASN 16 PRO 17 LYS 18 ILE 19 ILE 20 ILE 21 PHE 22 GLU 23 GLN 24 GLU 25 ASN 26 PHE 27 GLN 28 GLY 29 HIS 30 SER 31 HIS 32 GLU 33 LEU 34 ASN 35 GLY 36 PRO 37 CYS 38 PRO 39 ASN 40 LEU 41 LYS 42 GLU 43 THR 44 GLY 45 VAL 46 GLU 47 LYS 48 ALA 49 GLY 50 SER 51 VAL 52 LEU 53 VAL 54 GLN 55 ALA 56 GLY 57 PRO 58 TRP 59 VAL 60 GLY 61 TYR 62 GLU 63 GLN 64 ALA 65 ASN 66 CYS 67 LYS 68 GLY 69 GLU 70 GLN 71 PHE 72 VAL 73 PHE 74 GLU 75 LYS 76 GLY 77 GLU 78 TYR 79 PRO 80 ARG 81 TRP 82 ASP 83 SER 84 TRP 85 THR 86 SER 87 SER 88 ARG 89 ARG 90 THR 91 ASP 92 SER 93 LEU 94 SER 95 SER 96 LEU 97 ARG 98 PRO 99 ILE 100 LYS 101 VAL 102 ASP 103 SER 104 GLN 105 GLU 106 HIS 107 LYS 108 ILE 109 ILE 110 LEU 111 TYR 112 GLU 113 ASN 114 PRO 115 ASN 116 PHE 117 THR 118 GLY 119 LYS 120 LYS 121 MET 122 GLU 123 ILE 124 ILE 125 ASP 126 ASP 127 ASP 128 VAL 129 PRO 130 SER 131 PHE 132 HIS 133 ALA 134 HIS 135 GLY 136 TYR 137 GLN 138 GLU 139 LYS 140 VAL 141 SER 142 SER 143 VAL 144 ARG 145 VAL 146 GLN 147 SER 148 GLY 149 THR 150 TRP 151 VAL 152 GLY 153 TYR 154 GLN 155 TYR 156 PRO 157 GLY 158 TYR 159 ARG 160 GLY 161 LEU 162 GLN 163 TYR 164 LEU 165 LEU 166 GLU 167 LYS 168 GLY 169 ASP 170 TYR 171 LYS 172 ASP 173 SER 174 SER 175 ASP 176 PHE 177 GLY 178 ALA 179 PRO 180 HIS 181 PRO 182 GLN 183 VAL 184 GLN 185 SER 186 VAL 187 ARG 188 ARG 189 ILE 190 ARG 191 ASP 192 MET 193 GLN 194 TRP 195 HIS 196 GLN 197 ARG 198 GLY 199 ALA 200 PHE 201 HIS 202 PRO 203 SER 204 ASN 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 $human_betaB2-crystallin 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 $human_betaB2-crystallin 'recombinant technology' . Escherichia coli . pET-21a 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 $human_betaB2-crystallin 0.625 mM 0.35 0.9 '[U-13C; U-15N; U-2H]' 'sodium phosphate buffer' 25 mM . . 'natural abundance' EDTA 1 mM . . 'natural abundance' DTT 5 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_NMRDraw _Saveframe_category software _Name NMRDraw _Version . loop_ _Vendor _Address _Electronic_address 'Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax' . . stop_ loop_ _Task processing 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_Analysis _Saveframe_category software _Name Analysis _Version . loop_ _Vendor _Address _Electronic_address CCPN . . 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_HNCA_2 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCA' _Sample_label $sample_1 save_ save_3D_HNCACB_3 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCACB' _Sample_label $sample_1 save_ save_3D_CBCA(CO)NH_4 _Saveframe_category NMR_applied_experiment _Experiment_name '3D CBCA(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' 0.025 . M pH 6.5 . pH pressure 1 . atm temperature 308 . 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 H 1 protons ppm 4.7 internal direct . . . 1.0 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 HNCA' '3D HNCACB' '3D CBCA(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 'human betaB2-crystallin, chain 1' _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 5 5 GLN CA C 55.750 0.023 1 2 5 5 GLN CB C 28.642 0.000 1 3 6 6 THR H H 8.121 0.001 1 4 6 6 THR CA C 61.824 0.041 1 5 6 6 THR CB C 69.216 0.000 1 6 6 6 THR N N 116.082 0.127 1 7 7 7 GLN H H 8.288 0.002 1 8 7 7 GLN CA C 55.427 0.025 1 9 7 7 GLN CB C 28.497 0.003 1 10 7 7 GLN N N 123.096 0.113 1 11 8 8 ALA H H 8.187 0.001 1 12 8 8 ALA CA C 52.233 0.018 1 13 8 8 ALA CB C 18.386 0.008 1 14 8 8 ALA N N 125.668 0.126 1 15 9 9 GLY H H 8.201 0.001 1 16 9 9 GLY CA C 44.647 0.006 1 17 9 9 GLY N N 108.557 0.113 1 18 10 10 LYS H H 7.947 0.001 1 19 10 10 LYS CA C 53.656 0.007 1 20 10 10 LYS CB C 31.527 0.000 1 21 10 10 LYS N N 122.303 0.114 1 22 11 11 PRO CA C 62.782 0.021 1 23 11 11 PRO CB C 31.059 0.000 1 24 12 12 GLN H H 8.405 0.000 1 25 12 12 GLN CA C 55.445 0.035 1 26 12 12 GLN CB C 29.020 0.000 1 27 12 12 GLN N N 121.388 0.123 1 28 13 13 SER H H 8.244 0.004 1 29 13 13 SER CA C 57.805 0.039 1 30 13 13 SER CB C 63.204 0.060 1 31 13 13 SER N N 117.315 0.121 1 32 14 14 LEU H H 8.177 0.001 1 33 14 14 LEU CA C 54.431 0.037 1 34 14 14 LEU CB C 41.515 0.006 1 35 14 14 LEU N N 124.736 0.116 1 36 15 15 ASN H H 8.154 0.001 1 37 15 15 ASN CA C 51.077 0.004 1 38 15 15 ASN CB C 38.071 0.000 1 39 15 15 ASN N N 122.088 0.109 1 40 16 16 PRO CA C 62.771 0.057 1 41 17 17 LYS H H 9.098 0.001 1 42 17 17 LYS CA C 57.262 0.042 1 43 17 17 LYS CB C 34.781 0.000 1 44 17 17 LYS N N 120.456 0.137 1 45 18 18 ILE H H 8.488 0.003 1 46 18 18 ILE CA C 58.524 0.050 1 47 18 18 ILE CB C 40.485 0.001 1 48 18 18 ILE N N 131.490 0.109 1 49 19 19 ILE H H 8.725 0.002 1 50 19 19 ILE CA C 59.683 0.034 1 51 19 19 ILE CB C 38.966 0.000 1 52 19 19 ILE N N 126.525 0.110 1 53 20 20 ILE H H 8.500 0.004 1 54 20 20 ILE CA C 59.245 0.070 1 55 20 20 ILE CB C 38.669 0.000 1 56 20 20 ILE N N 126.188 0.131 1 57 21 21 PHE H H 9.005 0.002 1 58 21 21 PHE CA C 56.296 0.015 1 59 21 21 PHE CB C 39.222 0.000 1 60 21 21 PHE N N 126.494 0.132 1 61 22 22 GLU H H 8.613 0.001 1 62 22 22 GLU CA C 58.010 0.044 1 63 22 22 GLU CB C 30.710 0.025 1 64 22 22 GLU N N 120.635 0.128 1 65 23 23 GLN H H 7.726 0.001 1 66 23 23 GLN CA C 52.636 0.042 1 67 23 23 GLN CB C 31.140 0.016 1 68 23 23 GLN N N 112.841 0.125 1 69 24 24 GLU H H 8.540 0.001 1 70 24 24 GLU CA C 55.906 0.018 1 71 24 24 GLU CB C 29.357 0.000 1 72 24 24 GLU N N 119.809 0.129 1 73 25 25 ASN H H 9.343 0.002 1 74 25 25 ASN CA C 53.938 0.064 1 75 25 25 ASN CB C 36.285 0.023 1 76 25 25 ASN N N 114.311 0.115 1 77 26 26 PHE H H 7.720 0.001 1 78 26 26 PHE CA C 56.016 0.035 1 79 26 26 PHE CB C 33.909 0.010 1 80 26 26 PHE N N 112.791 0.130 1 81 27 27 GLN H H 6.136 0.002 1 82 27 27 GLN CA C 53.172 0.006 1 83 27 27 GLN CB C 31.104 0.001 1 84 27 27 GLN N N 116.515 0.094 1 85 28 28 GLY H H 8.203 0.002 1 86 28 28 GLY CA C 43.759 0.029 1 87 28 28 GLY N N 105.613 0.131 1 88 29 29 HIS H H 8.522 0.001 1 89 29 29 HIS CA C 56.431 0.015 1 90 29 29 HIS CB C 29.018 0.005 1 91 29 29 HIS N N 118.132 0.113 1 92 30 30 SER H H 7.917 0.001 1 93 30 30 SER CA C 55.138 0.017 1 94 30 30 SER CB C 66.391 0.006 1 95 30 30 SER N N 116.200 0.111 1 96 31 31 HIS H H 8.321 0.002 1 97 31 31 HIS CA C 54.834 0.015 1 98 31 31 HIS CB C 31.955 0.007 1 99 31 31 HIS N N 118.953 0.087 1 100 32 32 GLU H H 8.380 0.002 1 101 32 32 GLU CA C 54.452 0.087 1 102 32 32 GLU CB C 30.450 0.042 1 103 32 32 GLU N N 126.594 0.101 1 104 33 33 LEU H H 8.871 0.002 1 105 33 33 LEU CA C 53.749 0.034 1 106 33 33 LEU CB C 42.922 0.009 1 107 33 33 LEU N N 125.782 0.127 1 108 34 34 ASN H H 8.687 0.001 1 109 34 34 ASN CA C 51.845 0.038 1 110 34 34 ASN CB C 40.676 0.025 1 111 34 34 ASN N N 118.102 0.123 1 112 35 35 GLY H H 7.571 0.002 1 113 35 35 GLY CA C 44.203 0.026 1 114 35 35 GLY N N 107.165 0.128 1 115 36 36 PRO CA C 63.003 0.008 1 116 36 36 PRO CB C 31.943 0.000 1 117 37 37 CYS H H 9.016 0.001 1 118 37 37 CYS CA C 55.432 0.025 1 119 37 37 CYS CB C 28.882 0.000 1 120 37 37 CYS N N 122.028 0.122 1 121 38 38 PRO CA C 63.956 0.027 1 122 38 38 PRO CB C 31.549 0.000 1 123 39 39 ASN H H 7.434 0.001 1 124 39 39 ASN CA C 52.578 0.027 1 125 39 39 ASN CB C 37.767 0.018 1 126 39 39 ASN N N 116.005 0.116 1 127 40 40 LEU H H 8.763 0.003 1 128 40 40 LEU CA C 57.708 0.032 1 129 40 40 LEU CB C 40.617 0.014 1 130 40 40 LEU N N 129.096 0.134 1 131 41 41 LYS H H 8.413 0.006 1 132 41 41 LYS CA C 58.968 0.028 1 133 41 41 LYS CB C 30.821 0.000 1 134 41 41 LYS N N 121.354 0.128 1 135 42 42 GLU H H 7.449 0.001 1 136 42 42 GLU CA C 57.579 0.029 1 137 42 42 GLU CB C 28.733 0.023 1 138 42 42 GLU N N 118.658 0.108 1 139 43 43 THR H H 7.342 0.002 1 140 43 43 THR CA C 61.618 0.028 1 141 43 43 THR CB C 69.648 0.001 1 142 43 43 THR N N 111.152 0.107 1 143 44 44 GLY H H 7.398 0.001 1 144 44 44 GLY CA C 44.363 0.007 1 145 44 44 GLY N N 107.795 0.120 1 146 45 45 VAL H H 7.235 0.001 1 147 45 45 VAL CA C 60.850 0.026 1 148 45 45 VAL CB C 29.929 0.006 1 149 45 45 VAL N N 121.526 0.118 1 150 46 46 GLU H H 8.484 0.001 1 151 46 46 GLU CA C 57.673 0.016 1 152 46 46 GLU CB C 29.753 0.090 1 153 46 46 GLU N N 126.971 0.113 1 154 47 47 LYS H H 7.535 0.002 1 155 47 47 LYS CA C 54.655 0.011 1 156 47 47 LYS CB C 34.237 0.004 1 157 47 47 LYS N N 116.836 0.118 1 158 48 48 ALA H H 8.370 0.001 1 159 48 48 ALA CA C 50.010 0.042 1 160 48 48 ALA CB C 18.485 0.000 1 161 48 48 ALA N N 124.733 0.108 1 162 49 49 GLY H H 8.985 0.003 1 163 49 49 GLY CA C 45.380 0.054 1 164 49 49 GLY N N 112.657 0.154 1 165 50 50 SER H H 8.006 0.004 1 166 50 50 SER CA C 58.400 0.065 1 167 50 50 SER CB C 63.617 0.000 1 168 50 50 SER N N 108.784 0.115 1 169 51 51 VAL H H 9.123 0.006 1 170 51 51 VAL CA C 61.010 0.039 1 171 51 51 VAL CB C 36.035 0.000 1 172 51 51 VAL N N 118.885 0.087 1 173 52 52 LEU H H 9.310 0.001 1 174 52 52 LEU CA C 53.251 0.044 1 175 52 52 LEU CB C 44.881 0.000 1 176 52 52 LEU N N 128.904 0.123 1 177 53 53 VAL H H 8.801 0.002 1 178 53 53 VAL CA C 61.427 0.040 1 179 53 53 VAL CB C 30.873 0.000 1 180 53 53 VAL N N 125.854 0.128 1 181 54 54 GLN H H 7.621 0.001 1 182 54 54 GLN CA C 57.067 0.070 1 183 54 54 GLN CB C 28.815 0.000 1 184 54 54 GLN N N 127.804 0.100 1 185 55 55 ALA H H 8.437 0.005 1 186 55 55 ALA CA C 52.940 0.013 1 187 55 55 ALA CB C 20.014 0.000 1 188 55 55 ALA N N 120.688 0.110 1 189 57 57 PRO CA C 63.881 0.000 1 190 58 58 TRP H H 9.047 0.000 1 191 58 58 TRP CA C 56.206 0.062 1 192 58 58 TRP CB C 32.336 0.000 1 193 58 58 TRP N N 117.596 0.029 1 194 59 59 VAL H H 9.447 0.003 1 195 59 59 VAL CA C 58.856 0.013 1 196 59 59 VAL CB C 34.041 0.000 1 197 59 59 VAL N N 120.702 0.123 1 198 60 60 GLY H H 9.652 0.002 1 199 60 60 GLY CA C 43.424 0.058 1 200 60 60 GLY N N 114.780 0.141 1 201 61 61 TYR H H 8.417 0.002 1 202 61 61 TYR CA C 55.726 0.059 1 203 61 61 TYR CB C 40.207 0.000 1 204 61 61 TYR N N 115.614 0.105 1 205 62 62 GLU H H 9.004 0.002 1 206 62 62 GLU CA C 57.560 0.042 1 207 62 62 GLU CB C 32.215 0.037 1 208 62 62 GLU N N 123.836 0.125 1 209 63 63 GLN H H 8.197 0.002 1 210 63 63 GLN CA C 53.066 0.018 1 211 63 63 GLN CB C 30.477 0.012 1 212 63 63 GLN N N 114.162 0.130 1 213 64 64 ALA H H 8.563 0.001 1 214 64 64 ALA CA C 51.915 0.026 1 215 64 64 ALA CB C 17.886 0.007 1 216 64 64 ALA N N 122.926 0.117 1 217 65 65 ASN H H 9.759 0.011 1 218 65 65 ASN CA C 54.078 0.055 1 219 65 65 ASN CB C 36.081 0.013 1 220 65 65 ASN N N 112.691 0.117 1 221 66 66 CYS H H 8.248 0.002 1 222 66 66 CYS CA C 57.377 0.017 1 223 66 66 CYS CB C 23.815 0.001 1 224 66 66 CYS N N 109.040 0.134 1 225 67 67 LYS H H 6.077 0.002 1 226 67 67 LYS CA C 53.466 0.014 1 227 67 67 LYS CB C 34.687 0.011 1 228 67 67 LYS N N 117.579 0.106 1 229 68 68 GLY H H 8.217 0.001 1 230 68 68 GLY CA C 43.865 0.011 1 231 68 68 GLY N N 106.706 0.140 1 232 69 69 GLU H H 8.640 0.002 1 233 69 69 GLU CA C 57.996 0.037 1 234 69 69 GLU CB C 29.310 0.000 1 235 69 69 GLU N N 122.596 0.116 1 236 72 72 VAL CA C 62.568 0.000 1 237 72 72 VAL CB C 30.817 0.000 1 238 73 73 PHE H H 9.451 0.002 1 239 73 73 PHE CA C 56.594 0.029 1 240 73 73 PHE CB C 40.722 0.000 1 241 73 73 PHE N N 128.591 0.149 1 242 75 75 LYS CA C 58.600 0.000 1 243 76 76 GLY H H 8.446 0.004 1 244 76 76 GLY CA C 43.796 0.000 1 245 76 76 GLY N N 113.428 0.149 1 246 77 77 GLU H H 8.263 0.004 1 247 77 77 GLU CA C 55.696 0.000 1 248 77 77 GLU N N 119.062 0.099 1 249 82 82 ASP H H 8.449 0.005 1 250 82 82 ASP CA C 53.380 0.000 1 251 82 82 ASP CB C 41.423 0.000 1 252 82 82 ASP N N 121.681 0.105 1 253 83 83 SER H H 7.800 0.006 1 254 83 83 SER CA C 57.418 0.028 1 255 83 83 SER CB C 64.176 0.000 1 256 83 83 SER N N 114.689 0.128 1 257 84 84 TRP H H 8.230 0.001 1 258 84 84 TRP CA C 56.317 0.000 1 259 84 84 TRP N N 122.147 0.095 1 260 88 88 ARG CA C 53.398 0.000 1 261 89 89 ARG H H 8.591 0.003 1 262 89 89 ARG CA C 54.928 0.000 1 263 89 89 ARG CB C 30.403 0.000 1 264 89 89 ARG N N 121.510 0.130 1 265 91 91 ASP CA C 53.034 0.002 1 266 91 91 ASP CB C 39.359 0.000 1 267 92 92 SER H H 7.881 0.001 1 268 92 92 SER CA C 58.870 0.017 1 269 92 92 SER CB C 64.007 0.000 1 270 92 92 SER N N 115.297 0.140 1 271 93 93 LEU H H 7.799 0.001 1 272 93 93 LEU CA C 54.788 0.052 1 273 93 93 LEU CB C 42.853 0.000 1 274 93 93 LEU N N 124.282 0.096 1 275 94 94 SER H H 8.816 0.003 1 276 94 94 SER CA C 59.413 0.096 1 277 94 94 SER CB C 65.495 0.000 1 278 94 94 SER N N 117.683 0.142 1 279 95 95 SER H H 7.952 0.002 1 280 95 95 SER CA C 58.064 0.041 1 281 95 95 SER CB C 65.089 0.003 1 282 95 95 SER N N 112.526 0.116 1 283 96 96 LEU H H 8.466 0.003 1 284 96 96 LEU CA C 54.619 0.020 1 285 96 96 LEU CB C 49.069 0.052 1 286 96 96 LEU N N 120.552 0.113 1 287 97 97 ARG H H 9.568 0.002 1 288 97 97 ARG CA C 54.462 0.002 1 289 97 97 ARG CB C 30.128 0.000 1 290 97 97 ARG N N 116.928 0.136 1 291 99 99 ILE H H 7.767 0.001 1 292 99 99 ILE N N 122.238 0.048 1 293 100 100 LYS H H 8.982 0.003 1 294 100 100 LYS N N 129.951 0.105 1 295 101 101 VAL H H 8.273 0.003 1 296 101 101 VAL N N 125.448 0.045 1 297 102 102 ASP H H 8.475 0.002 1 298 102 102 ASP N N 124.868 0.126 1 299 106 106 HIS H H 9.033 0.003 1 300 106 106 HIS CA C 55.673 0.049 1 301 106 106 HIS CB C 32.130 0.000 1 302 106 106 HIS N N 124.535 0.125 1 303 107 107 LYS H H 9.244 0.002 1 304 107 107 LYS CA C 56.278 0.071 1 305 107 107 LYS CB C 34.971 0.024 1 306 107 107 LYS N N 127.145 0.123 1 307 108 108 ILE H H 8.889 0.003 1 308 108 108 ILE CA C 58.723 0.026 1 309 108 108 ILE CB C 40.888 0.062 1 310 108 108 ILE N N 128.910 0.135 1 311 109 109 ILE H H 8.628 0.004 1 312 109 109 ILE CA C 60.194 0.032 1 313 109 109 ILE CB C 39.318 0.006 1 314 109 109 ILE N N 125.545 0.132 1 315 110 110 LEU H H 8.487 0.004 1 316 110 110 LEU CA C 54.242 0.048 1 317 110 110 LEU CB C 40.950 0.022 1 318 110 110 LEU N N 127.472 0.166 1 319 111 111 TYR H H 8.626 0.001 1 320 111 111 TYR CA C 56.630 0.026 1 321 111 111 TYR CB C 39.902 0.004 1 322 111 111 TYR N N 117.498 0.121 1 323 112 112 GLU H H 8.930 0.001 1 324 112 112 GLU CA C 57.275 0.071 1 325 112 112 GLU CB C 31.764 0.048 1 326 112 112 GLU N N 123.300 0.127 1 327 113 113 ASN H H 8.253 0.001 1 328 113 113 ASN CA C 50.191 0.018 1 329 113 113 ASN CB C 38.256 0.000 1 330 113 113 ASN N N 114.933 0.109 1 331 114 114 PRO CA C 62.429 0.036 1 332 114 114 PRO CB C 31.402 0.000 1 333 115 115 ASN H H 9.314 0.001 1 334 115 115 ASN CA C 53.887 0.038 1 335 115 115 ASN CB C 36.480 0.015 1 336 115 115 ASN N N 115.021 0.129 1 337 116 116 PHE H H 7.637 0.002 1 338 116 116 PHE CA C 55.385 0.036 1 339 116 116 PHE CB C 34.057 0.003 1 340 116 116 PHE N N 112.407 0.121 1 341 117 117 THR H H 6.348 0.002 1 342 117 117 THR CA C 59.495 0.042 1 343 117 117 THR CB C 72.414 0.002 1 344 117 117 THR N N 107.913 0.124 1 345 118 118 GLY H H 8.215 0.001 1 346 118 118 GLY CA C 43.729 0.013 1 347 118 118 GLY N N 106.070 0.158 1 348 119 119 LYS H H 8.844 0.001 1 349 119 119 LYS CA C 57.824 0.009 1 350 119 119 LYS CB C 32.486 0.001 1 351 119 119 LYS N N 122.576 0.115 1 352 120 120 LYS H H 7.909 0.001 1 353 120 120 LYS CA C 53.204 0.005 1 354 120 120 LYS CB C 35.691 0.051 1 355 120 120 LYS N N 117.496 0.121 1 356 121 121 MET H H 8.551 0.002 1 357 121 121 MET CA C 54.450 0.028 1 358 121 121 MET CB C 34.905 0.004 1 359 121 121 MET N N 122.464 0.139 1 360 122 122 GLU H H 8.415 0.001 1 361 122 122 GLU CA C 54.094 0.078 1 362 122 122 GLU CB C 31.195 0.018 1 363 122 122 GLU N N 127.620 0.123 1 364 123 123 ILE H H 8.754 0.002 1 365 123 123 ILE CA C 60.147 0.039 1 366 123 123 ILE CB C 38.358 0.013 1 367 123 123 ILE N N 126.553 0.111 1 368 124 124 ILE H H 8.420 0.002 1 369 124 124 ILE CA C 59.174 0.024 1 370 124 124 ILE CB C 39.783 0.010 1 371 124 124 ILE N N 126.903 0.116 1 372 125 125 ASP H H 9.566 0.002 1 373 125 125 ASP CA C 56.513 0.034 1 374 125 125 ASP CB C 39.486 0.088 1 375 125 125 ASP N N 122.268 0.129 1 376 126 126 ASP H H 6.854 0.004 1 377 126 126 ASP CA C 52.263 0.041 1 378 126 126 ASP CB C 43.089 0.000 1 379 126 126 ASP N N 112.267 0.095 1 380 127 127 ASP H H 8.152 0.001 1 381 127 127 ASP CA C 53.071 0.015 1 382 127 127 ASP CB C 43.026 0.000 1 383 127 127 ASP N N 117.025 0.109 1 384 128 128 VAL H H 8.905 0.003 1 385 128 128 VAL CA C 59.088 0.005 1 386 128 128 VAL CB C 33.868 0.000 1 387 128 128 VAL N N 120.758 0.111 1 388 129 129 PRO CA C 62.922 0.001 1 389 130 130 SER H H 7.508 0.008 1 390 130 130 SER CA C 56.001 0.012 1 391 130 130 SER CB C 61.877 0.011 1 392 130 130 SER N N 112.550 0.128 1 393 131 131 PHE H H 9.226 0.004 1 394 131 131 PHE CA C 59.724 0.052 1 395 131 131 PHE CB C 35.307 0.057 1 396 131 131 PHE N N 135.767 0.114 1 397 132 132 HIS H H 9.712 0.002 1 398 132 132 HIS CA C 59.734 0.044 1 399 132 132 HIS CB C 31.566 0.053 1 400 132 132 HIS N N 120.638 0.153 1 401 133 133 ALA H H 8.371 0.004 1 402 133 133 ALA CA C 54.174 0.086 1 403 133 133 ALA CB C 17.389 0.014 1 404 133 133 ALA N N 122.658 0.105 1 405 134 134 HIS H H 7.597 0.001 1 406 134 134 HIS CA C 55.113 0.072 1 407 134 134 HIS CB C 30.459 0.026 1 408 134 134 HIS N N 117.625 0.113 1 409 135 135 GLY H H 7.646 0.002 1 410 135 135 GLY CA C 45.159 0.010 1 411 135 135 GLY N N 106.239 0.122 1 412 136 136 TYR H H 7.951 0.003 1 413 136 136 TYR CA C 57.474 0.022 1 414 136 136 TYR CB C 39.326 0.037 1 415 136 136 TYR N N 124.937 0.119 1 416 137 137 GLN H H 7.899 0.001 1 417 137 137 GLN CA C 54.198 0.038 1 418 137 137 GLN CB C 27.772 0.000 1 419 137 137 GLN N N 125.529 0.110 1 420 138 138 GLU H H 6.401 0.003 1 421 138 138 GLU CA C 55.419 0.039 1 422 138 138 GLU CB C 29.797 0.030 1 423 138 138 GLU N N 119.899 0.121 1 424 139 139 LYS H H 8.013 0.002 1 425 139 139 LYS CA C 56.603 0.018 1 426 139 139 LYS CB C 32.505 0.008 1 427 139 139 LYS N N 118.279 0.138 1 428 140 140 VAL H H 7.637 0.001 1 429 140 140 VAL CA C 62.294 0.057 1 430 140 140 VAL CB C 32.878 0.084 1 431 140 140 VAL N N 119.901 0.119 1 432 141 141 SER H H 8.390 0.003 1 433 141 141 SER CA C 57.905 0.045 1 434 141 141 SER CB C 64.269 0.004 1 435 141 141 SER N N 117.147 0.177 1 436 142 142 SER H H 7.918 0.001 1 437 142 142 SER CA C 58.209 0.059 1 438 142 142 SER CB C 64.475 0.035 1 439 142 142 SER N N 108.132 0.132 1 440 143 143 VAL H H 9.017 0.002 1 441 143 143 VAL CA C 60.778 0.042 1 442 143 143 VAL CB C 37.522 0.044 1 443 143 143 VAL N N 118.110 0.123 1 444 144 144 ARG H H 9.657 0.002 1 445 144 144 ARG CA C 55.445 0.028 1 446 144 144 ARG CB C 31.632 0.000 1 447 144 144 ARG N N 127.378 0.118 1 448 145 145 VAL H H 9.285 0.001 1 449 145 145 VAL CA C 61.931 0.032 1 450 145 145 VAL CB C 29.827 0.029 1 451 145 145 VAL N N 127.394 0.103 1 452 146 146 GLN H H 7.887 0.002 1 453 146 146 GLN CA C 57.667 0.025 1 454 146 146 GLN CB C 28.733 0.004 1 455 146 146 GLN N N 128.671 0.110 1 456 147 147 SER H H 8.341 0.001 1 457 147 147 SER CA C 58.232 0.088 1 458 147 147 SER CB C 64.183 0.033 1 459 147 147 SER N N 110.884 0.129 1 460 148 148 GLY H H 9.037 0.002 1 461 148 148 GLY CA C 43.636 0.019 1 462 148 148 GLY N N 115.497 0.116 1 463 149 149 THR H H 6.972 0.002 1 464 149 149 THR CA C 62.686 0.054 1 465 149 149 THR CB C 69.606 0.000 1 466 149 149 THR N N 113.522 0.148 1 467 150 150 TRP H H 8.930 0.004 1 468 150 150 TRP CA C 55.084 0.019 1 469 150 150 TRP CB C 32.276 0.032 1 470 150 150 TRP N N 128.417 0.120 1 471 151 151 VAL H H 9.360 0.002 1 472 151 151 VAL CA C 60.564 0.037 1 473 151 151 VAL CB C 33.585 0.000 1 474 151 151 VAL N N 119.441 0.125 1 475 152 152 GLY H H 9.236 0.008 1 476 152 152 GLY CA C 43.112 0.011 1 477 152 152 GLY N N 113.572 0.105 1 478 153 153 TYR H H 8.516 0.003 1 479 153 153 TYR CA C 55.624 0.020 1 480 153 153 TYR CB C 39.585 0.000 1 481 153 153 TYR N N 116.070 0.135 1 482 154 154 GLN H H 8.161 0.007 1 483 154 154 GLN CA C 53.475 0.000 1 484 154 154 GLN N N 120.301 0.084 1 485 155 155 TYR H H 7.953 0.001 1 486 155 155 TYR N N 112.942 0.080 1 487 156 156 PRO CA C 61.729 0.022 1 488 156 156 PRO CB C 30.843 0.000 1 489 157 157 GLY H H 9.608 0.007 1 490 157 157 GLY CA C 45.501 0.016 1 491 157 157 GLY N N 106.555 0.122 1 492 158 158 TYR H H 7.451 0.003 1 493 158 158 TYR CA C 54.833 0.000 1 494 158 158 TYR N N 112.887 0.072 1 495 159 159 ARG H H 6.159 0.002 1 496 159 159 ARG CA C 54.240 0.021 1 497 159 159 ARG CB C 33.629 0.000 1 498 159 159 ARG N N 117.658 0.111 1 499 160 160 GLY H H 8.365 0.003 1 500 160 160 GLY CA C 44.162 0.023 1 501 160 160 GLY N N 106.845 0.135 1 502 161 161 LEU H H 8.045 0.005 1 503 161 161 LEU CA C 56.193 0.036 1 504 161 161 LEU CB C 41.327 0.000 1 505 161 161 LEU N N 121.327 0.111 1 506 162 162 GLN H H 7.543 0.005 1 507 162 162 GLN CA C 52.281 0.062 1 508 162 162 GLN CB C 31.075 0.000 1 509 162 162 GLN N N 116.181 0.142 1 510 163 163 TYR H H 8.485 0.004 1 511 163 163 TYR CA C 53.189 0.072 1 512 163 163 TYR CB C 39.502 0.066 1 513 163 163 TYR N N 118.974 0.131 1 514 164 164 LEU H H 8.723 0.004 1 515 164 164 LEU CA C 55.684 0.027 1 516 164 164 LEU CB C 40.780 0.002 1 517 164 164 LEU N N 127.394 0.121 1 518 165 165 LEU H H 9.038 0.003 1 519 165 165 LEU CA C 52.935 0.043 1 520 165 165 LEU CB C 41.713 0.050 1 521 165 165 LEU N N 132.817 0.114 1 522 166 166 GLU H H 8.007 0.001 1 523 166 166 GLU CA C 55.096 0.020 1 524 166 166 GLU CB C 31.968 0.000 1 525 166 166 GLU N N 122.231 0.119 1 526 167 167 LYS H H 8.478 0.003 1 527 167 167 LYS CA C 58.437 0.042 1 528 167 167 LYS CB C 31.727 0.054 1 529 167 167 LYS N N 121.790 0.133 1 530 168 168 GLY H H 8.607 0.001 1 531 168 168 GLY CA C 43.791 0.033 1 532 168 168 GLY N N 115.846 0.126 1 533 169 169 ASP H H 7.957 0.000 1 534 169 169 ASP CA C 53.129 0.017 1 535 169 169 ASP CB C 42.518 0.004 1 536 169 169 ASP N N 118.661 0.107 1 537 170 170 TYR H H 9.354 0.002 1 538 170 170 TYR CA C 56.152 0.007 1 539 170 170 TYR CB C 38.070 0.011 1 540 170 170 TYR N N 122.214 0.117 1 541 171 171 LYS H H 8.696 0.001 1 542 171 171 LYS CA C 58.991 0.021 1 543 171 171 LYS CB C 31.507 0.035 1 544 171 171 LYS N N 124.151 0.118 1 545 172 172 ASP H H 7.988 0.001 1 546 172 172 ASP CA C 53.043 0.012 1 547 172 172 ASP CB C 45.147 0.018 1 548 172 172 ASP N N 117.937 0.133 1 549 173 173 SER H H 7.683 0.005 1 550 173 173 SER CA C 59.999 0.024 1 551 173 173 SER CB C 60.830 0.033 1 552 173 173 SER N N 119.620 0.120 1 553 174 174 SER H H 8.118 0.001 1 554 174 174 SER CA C 60.389 0.069 1 555 174 174 SER CB C 61.595 0.011 1 556 174 174 SER N N 118.374 0.105 1 557 175 175 ASP H H 7.922 0.001 1 558 175 175 ASP CA C 56.885 0.022 1 559 175 175 ASP CB C 40.837 0.000 1 560 175 175 ASP N N 123.051 0.142 1 561 176 176 PHE H H 6.929 0.004 1 562 176 176 PHE CA C 55.002 0.039 1 563 176 176 PHE CB C 36.768 0.051 1 564 176 176 PHE N N 113.443 0.132 1 565 177 177 GLY H H 7.206 0.002 1 566 177 177 GLY CA C 44.986 0.015 1 567 177 177 GLY N N 106.450 0.158 1 568 178 178 ALA H H 6.872 0.001 1 569 178 178 ALA CA C 48.901 0.014 1 570 178 178 ALA CB C 18.377 0.000 1 571 178 178 ALA N N 124.767 0.118 1 572 179 179 PRO CA C 63.076 0.042 1 573 180 180 HIS H H 6.858 0.001 1 574 180 180 HIS CA C 52.694 0.046 1 575 180 180 HIS N N 114.035 0.126 1 576 181 181 PRO CA C 63.282 0.005 1 577 181 181 PRO CB C 29.067 0.000 1 578 182 182 GLN H H 8.145 0.002 1 579 182 182 GLN CA C 54.949 0.056 1 580 182 182 GLN CB C 30.545 0.000 1 581 182 182 GLN N N 125.946 0.125 1 582 183 183 VAL H H 7.742 0.004 1 583 183 183 VAL CA C 61.335 0.016 1 584 183 183 VAL CB C 35.110 0.000 1 585 183 183 VAL N N 126.954 0.173 1 586 185 185 SER CA C 58.831 0.000 1 587 186 186 VAL H H 9.061 0.001 1 588 186 186 VAL CA C 59.838 0.011 1 589 186 186 VAL CB C 34.926 0.000 1 590 186 186 VAL N N 117.423 0.103 1 591 187 187 ARG H H 9.424 0.012 1 592 187 187 ARG CA C 53.185 0.035 1 593 187 187 ARG CB C 32.074 0.078 1 594 187 187 ARG N N 121.380 0.202 1 595 188 188 ARG H H 8.715 0.003 1 596 188 188 ARG CA C 54.915 0.012 1 597 188 188 ARG CB C 30.279 0.012 1 598 188 188 ARG N N 121.748 0.117 1 599 189 189 ILE H H 8.391 0.009 1 600 189 189 ILE CA C 60.147 0.017 1 601 189 189 ILE CB C 35.246 0.000 1 602 189 189 ILE N N 123.801 0.217 1 603 191 191 ASP CA C 53.167 0.000 1 604 191 191 ASP CB C 42.564 0.000 1 605 192 192 MET H H 8.465 0.001 1 606 192 192 MET CA C 55.248 0.031 1 607 192 192 MET CB C 33.140 0.021 1 608 192 192 MET N N 121.483 0.127 1 609 193 193 GLN H H 8.325 0.001 1 610 193 193 GLN CA C 56.039 0.019 1 611 193 193 GLN CB C 28.185 0.000 1 612 193 193 GLN N N 119.774 0.105 1 613 194 194 TRP H H 7.908 0.002 1 614 194 194 TRP CA C 57.413 0.006 1 615 194 194 TRP CB C 28.769 0.000 1 616 194 194 TRP N N 121.838 0.095 1 617 196 196 GLN CB C 28.475 0.000 1 618 197 197 ARG H H 8.238 0.003 1 619 197 197 ARG CA C 56.139 0.077 1 620 197 197 ARG CB C 29.789 0.001 1 621 197 197 ARG N N 122.520 0.140 1 622 198 198 GLY H H 8.319 0.001 1 623 198 198 GLY CA C 44.761 0.036 1 624 198 198 GLY N N 110.672 0.120 1 625 199 199 ALA H H 7.974 0.003 1 626 199 199 ALA CA C 51.832 0.008 1 627 199 199 ALA CB C 18.530 0.003 1 628 199 199 ALA N N 123.935 0.092 1 629 200 200 PHE H H 8.061 0.000 1 630 200 200 PHE CA C 57.143 0.015 1 631 200 200 PHE CB C 38.878 0.014 1 632 200 200 PHE N N 120.052 0.114 1 633 201 201 HIS H H 8.068 0.001 1 634 201 201 HIS CA C 52.963 0.019 1 635 201 201 HIS CB C 29.337 0.000 1 636 201 201 HIS N N 123.530 0.133 1 637 202 202 PRO CA C 62.736 0.002 1 638 202 202 PRO CB C 31.305 0.006 1 639 203 203 SER H H 8.395 0.002 1 640 203 203 SER CA C 57.953 0.044 1 641 203 203 SER CB C 63.411 0.019 1 642 203 203 SER N N 117.073 0.102 1 643 204 204 ASN H H 7.937 0.017 1 644 204 204 ASN CA C 54.534 0.001 1 645 204 204 ASN CB C 39.745 0.000 1 646 204 204 ASN N N 126.150 0.266 1 stop_ save_