data_27244 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Chemical shifts assignments of Escherichia coli aquaporin (AqpZ) by solid-state NMR ; _BMRB_accession_number 27244 _BMRB_flat_file_name bmr27244.str _Entry_type original _Submission_date 2017-09-06 _Accession_date 2017-09-06 _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 Xie 'Hua yong' . . 2 Zhao 'Yong xiang' . . 3 yang Jun . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "13C chemical shifts" 840 "15N chemical shifts" 220 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2018-10-02 original BMRB . stop_ _Original_release_date 2017-09-06 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; Chemical shifts assignments of Escherichia coli aquaporin (AqpZ) by solid-state NMR ; _Citation_status 'in preparation' _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID ? loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Xie 'Hua yong' . . 2 Zhao 'Yong xiang' . . stop_ _Journal_abbreviation 'Angew. Chem. Int. Ed. Engl.' _Journal_name_full 'Angewandte Chemie (International ed. in English)' _Journal_volume . _Journal_issue . _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first . _Page_last . _Year . _Details . save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name AqpZ _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label AqpZ $AqpZ stop_ _System_molecular_weight 24302 _System_physical_state native _System_oligomer_state ? _System_paramagnetic no _System_thiol_state . _Database_query_date . _Details ; The AqpZ proteoliposome was prepared by dialysis of protein, detergent and lipid mixtures. In details, the 10mg/ml liposome stock was prepared by hydration and Ultrasonic bath methods. The POPC/POPG lipids was dissolved by 2%DPC and mixed with AqpZ in elution buffer (20mM Tris, PH8.0, 100mM NaCl, 10% glycerol, 250mM imidazole, 0.5%DPC). The final AqpZ protein concentration is 0.6-0.7mg/ml, the mass ratio of lipid to protein is 1.25. After incubated 2h in 291K, the protein, detergent and lipids mixture was put into 8KD dialysis bag against a 1000 20mM Tris (pH8.0,291K), 50mM NaCl buffer. The dialysis buffer was changed every 24hours, after 7 days the AqpZ POPC/POPG proteoliposome was collected by centrifugation at 80,000rpm for 2h. ; save_ ######################## # Monomeric polymers # ######################## save_AqpZ _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common AqpZ _Molecular_mass . _Mol_thiol_state unknown _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 243 _Mol_residue_sequence ; MGSSHHHHHHEFMFRKLAAE CFGTFWLVFGGCGSAVLAAG FPELGIGFAGVALAFGLTVL TMAFAVGHISGGHFNPAVTI GLWAGGRFPAKEVVGYVIAQ VVGGIVAAALLYLIASGKTG FDAAASGFASNGYGEHSPGG YSMLSALVVELVLSAGFLLV IHGATDKFAPAGFAPIAIGL ALTLIHLISIPVTNTSVNPA RSTAVAIFQGGWALEQLWFF WVVPIVGGIIGGLIYRTLLE KRD ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 -11 MET 2 -10 GLY 3 -9 SER 4 -8 SER 5 -7 HIS 6 -6 HIS 7 -5 HIS 8 -4 HIS 9 -3 HIS 10 -2 HIS 11 -1 GLU 12 0 PHE 13 1 MET 14 2 PHE 15 3 ARG 16 4 LYS 17 5 LEU 18 6 ALA 19 7 ALA 20 8 GLU 21 9 CYS 22 10 PHE 23 11 GLY 24 12 THR 25 13 PHE 26 14 TRP 27 15 LEU 28 16 VAL 29 17 PHE 30 18 GLY 31 19 GLY 32 20 CYS 33 21 GLY 34 22 SER 35 23 ALA 36 24 VAL 37 25 LEU 38 26 ALA 39 27 ALA 40 28 GLY 41 29 PHE 42 30 PRO 43 31 GLU 44 32 LEU 45 33 GLY 46 34 ILE 47 35 GLY 48 36 PHE 49 37 ALA 50 38 GLY 51 39 VAL 52 40 ALA 53 41 LEU 54 42 ALA 55 43 PHE 56 44 GLY 57 45 LEU 58 46 THR 59 47 VAL 60 48 LEU 61 49 THR 62 50 MET 63 51 ALA 64 52 PHE 65 53 ALA 66 54 VAL 67 55 GLY 68 56 HIS 69 57 ILE 70 58 SER 71 59 GLY 72 60 GLY 73 61 HIS 74 62 PHE 75 63 ASN 76 64 PRO 77 65 ALA 78 66 VAL 79 67 THR 80 68 ILE 81 69 GLY 82 70 LEU 83 71 TRP 84 72 ALA 85 73 GLY 86 74 GLY 87 75 ARG 88 76 PHE 89 77 PRO 90 78 ALA 91 79 LYS 92 80 GLU 93 81 VAL 94 82 VAL 95 83 GLY 96 84 TYR 97 85 VAL 98 86 ILE 99 87 ALA 100 88 GLN 101 89 VAL 102 90 VAL 103 91 GLY 104 92 GLY 105 93 ILE 106 94 VAL 107 95 ALA 108 96 ALA 109 97 ALA 110 98 LEU 111 99 LEU 112 100 TYR 113 101 LEU 114 102 ILE 115 103 ALA 116 104 SER 117 105 GLY 118 106 LYS 119 107 THR 120 108 GLY 121 109 PHE 122 110 ASP 123 111 ALA 124 112 ALA 125 113 ALA 126 114 SER 127 115 GLY 128 116 PHE 129 117 ALA 130 118 SER 131 119 ASN 132 120 GLY 133 121 TYR 134 122 GLY 135 123 GLU 136 124 HIS 137 125 SER 138 126 PRO 139 127 GLY 140 128 GLY 141 129 TYR 142 130 SER 143 131 MET 144 132 LEU 145 133 SER 146 134 ALA 147 135 LEU 148 136 VAL 149 137 VAL 150 138 GLU 151 139 LEU 152 140 VAL 153 141 LEU 154 142 SER 155 143 ALA 156 144 GLY 157 145 PHE 158 146 LEU 159 147 LEU 160 148 VAL 161 149 ILE 162 150 HIS 163 151 GLY 164 152 ALA 165 153 THR 166 154 ASP 167 155 LYS 168 156 PHE 169 157 ALA 170 158 PRO 171 159 ALA 172 160 GLY 173 161 PHE 174 162 ALA 175 163 PRO 176 164 ILE 177 165 ALA 178 166 ILE 179 167 GLY 180 168 LEU 181 169 ALA 182 170 LEU 183 171 THR 184 172 LEU 185 173 ILE 186 174 HIS 187 175 LEU 188 176 ILE 189 177 SER 190 178 ILE 191 179 PRO 192 180 VAL 193 181 THR 194 182 ASN 195 183 THR 196 184 SER 197 185 VAL 198 186 ASN 199 187 PRO 200 188 ALA 201 189 ARG 202 190 SER 203 191 THR 204 192 ALA 205 193 VAL 206 194 ALA 207 195 ILE 208 196 PHE 209 197 GLN 210 198 GLY 211 199 GLY 212 200 TRP 213 201 ALA 214 202 LEU 215 203 GLU 216 204 GLN 217 205 LEU 218 206 TRP 219 207 PHE 220 208 PHE 221 209 TRP 222 210 VAL 223 211 VAL 224 212 PRO 225 213 ILE 226 214 VAL 227 215 GLY 228 216 GLY 229 217 ILE 230 218 ILE 231 219 GLY 232 220 GLY 233 221 LEU 234 222 ILE 235 223 TYR 236 224 ARG 237 225 THR 238 226 LEU 239 227 LEU 240 228 GLU 241 229 LYS 242 230 ARG 243 231 ASP stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date . loop_ _Database_name _Database_accession_code _Database_entry_mol_name _Sequence_query_to_submitted_percentage _Sequence_subject_length _Sequence_identity _Sequence_positive _Sequence_homology_expectation_value NCBI 'GenBank: CCI77899.1' aqpZ . . . . . NCBI 'GenBank: CDO13762.1' aqpZ . . . . . stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $AqpZ 'E. coli' 562 Bacteria . Escherichia coli 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 $AqpZ 'recombinant technology' . Escherichia coli 'Escherichia coli' pSD005 stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Saveframe_category sample _Sample_type solid _Details ; U-13C,15N labeled AqpZ in POPC/POPG lipids; The POPC/POPG lipids was dissolved by 2%DPC and mixed with AqpZ in elution buffer (20mM Tris, PH8.0, 100mM NaCl, 10% glycerol, 250mM imidazole, 0.5%DPC). ; loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $AqpZ 70 '% w/w' '[U-13C; U-15N]' 'POPC/POPG lipids' . '% w/w' 'natural abundance' stop_ save_ ############################ # Computer software used # ############################ save_NMRPipe _Saveframe_category software _Name NMRPipe _Version . loop_ _Vendor _Address _Electronic_address 'Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax' . . stop_ loop_ _Task 'data analysis' processing 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_SPARKY _Saveframe_category software _Name SPARKY _Version . loop_ _Vendor _Address _Electronic_address Goddard . . stop_ loop_ _Task 'chemical shift assignment' stop_ _Details . save_ save_VNMRJ _Saveframe_category software _Name VNMRJ _Version 2.31A loop_ _Vendor _Address _Electronic_address Varian . . stop_ loop_ _Task collection stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model 'Uniform NMR System' _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_3D_NCACX_1 _Saveframe_category NMR_applied_experiment _Experiment_name '3D NCACX' _Sample_label $sample_1 save_ save_3D_NCOCX_2 _Saveframe_category NMR_applied_experiment _Experiment_name '3D NCOCX' _Sample_label $sample_1 save_ save_3D_CONCA_3 _Saveframe_category NMR_applied_experiment _Experiment_name '3D CONCA' _Sample_label $sample_1 save_ save_3D_CANCOCX_4 _Saveframe_category NMR_applied_experiment _Experiment_name '3D CANCOCX' _Sample_label $sample_1 save_ save_3D_NCACB_5 _Saveframe_category NMR_applied_experiment _Experiment_name '3D NCACB' _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 pH 7.4 0.3 pH pressure 1 0.01 atm temperature 277 3 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 external indirect . . . 0.251449530 DSS N 15 'methyl protons' ppm 0.00 external indirect . . . 0.101329120 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 '3D NCACX' '3D NCOCX' '3D CONCA' '3D CANCOCX' '3D NCACB' 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 AqpZ _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 17 LEU C C 179.514 0.3 1 2 5 17 LEU CA C 57.434 0.3 1 3 5 17 LEU CB C 41.788 0.3 1 4 5 17 LEU N N 116 0.5 1 5 6 18 ALA C C 178.214 0.3 1 6 6 18 ALA CA C 55.014 0.3 1 7 6 18 ALA CB C 17.289 0.3 1 8 6 18 ALA N N 120.883 0.5 1 9 7 19 ALA C C 179.897 0.3 1 10 7 19 ALA CA C 56.198 0.3 1 11 7 19 ALA CB C 17.595 0.3 1 12 7 19 ALA N N 120.467 0.5 1 13 8 20 GLU C C 179.521 0.3 1 14 8 20 GLU CA C 59.512 0.3 1 15 8 20 GLU CB C 30.712 0.3 1 16 8 20 GLU CG C 37.112 0.3 1 17 8 20 GLU CD C 182.007 0.3 1 18 8 20 GLU N N 116.414 0.5 1 19 9 21 CYS C C 177.097 0.3 1 20 9 21 CYS CA C 62.373 0.3 1 21 9 21 CYS CB C 27.476 0.3 1 22 9 21 CYS N N 123.589 0.5 1 23 10 22 PHE C C 178.467 0.3 1 24 10 22 PHE CA C 60.261 0.3 1 25 10 22 PHE CB C 40.309 0.3 1 26 10 22 PHE N N 121.66 0.5 1 27 11 23 GLY C C 175.122 0.3 1 28 11 23 GLY CA C 47.414 0.3 1 29 11 23 GLY N N 107.38 0.5 1 30 14 26 TRP C C 174.733 0.3 1 31 14 26 TRP CA C 59.497 0.3 1 32 14 26 TRP CB C 31.359 0.3 1 33 14 26 TRP N N 122.014 0.5 1 34 15 27 LEU C C 179.257 0.3 1 35 15 27 LEU CA C 58.323 0.3 1 36 15 27 LEU CB C 43.181 0.3 1 37 15 27 LEU CG C 28.186 0.3 1 38 15 27 LEU CD1 C 25.534 0.3 2 39 15 27 LEU CD2 C 24.667 0.3 2 40 15 27 LEU N N 120.774 0.5 1 41 16 28 VAL C C 177.393 0.3 1 42 16 28 VAL CA C 66.773 0.3 1 43 16 28 VAL CB C 31.648 0.3 1 44 16 28 VAL CG1 C 23.988 0.3 2 45 16 28 VAL CG2 C 20.069 0.3 2 46 16 28 VAL N N 118.778 0.5 1 47 17 29 PHE C C 176.922 0.3 1 48 17 29 PHE CA C 62.354 0.3 1 49 17 29 PHE CB C 40.043 0.3 1 50 17 29 PHE CD1 C 131.87 0.3 1 51 17 29 PHE N N 119.377 0.5 1 52 18 30 GLY C C 175.365 0.3 1 53 18 30 GLY CA C 45.832 0.3 1 54 18 30 GLY N N 101.301 0.5 1 55 19 31 GLY C C 175.68 0.3 1 56 19 31 GLY CA C 45.124 0.3 1 57 19 31 GLY N N 111.34 0.5 1 58 20 32 CYS C C 176.753 0.3 1 59 20 32 CYS CA C 62.225 0.3 1 60 20 32 CYS CB C 25.05 0.3 1 61 20 32 CYS N N 119.104 0.5 1 62 21 33 GLY C C 175.228 0.3 1 63 21 33 GLY CA C 47.774 0.3 1 64 21 33 GLY N N 107.5 0.5 1 65 22 34 SER C C 176.6 0.3 1 66 22 34 SER CA C 62.71 0.3 1 67 22 34 SER CB C 61.48 0.3 1 68 22 34 SER N N 118.189 0.5 1 69 23 35 ALA C C 179.232 0.3 1 70 23 35 ALA CA C 54.779 0.3 1 71 23 35 ALA CB C 18.427 0.3 1 72 23 35 ALA N N 125.725 0.5 1 73 24 36 VAL C C 177.782 0.3 1 74 24 36 VAL CA C 65.333 0.3 1 75 24 36 VAL CB C 33.695 0.3 1 76 24 36 VAL CG1 C 22.547 0.3 2 77 24 36 VAL CG2 C 21.029 0.3 2 78 24 36 VAL N N 117.517 0.5 1 79 25 37 LEU C C 178.948 0.3 1 80 25 37 LEU CA C 56.004 0.3 1 81 25 37 LEU CB C 41.535 0.3 1 82 25 37 LEU CG C 26.87 0.3 1 83 25 37 LEU CD1 C 24.392 0.3 2 84 25 37 LEU CD2 C 22.294 0.3 2 85 25 37 LEU N N 114.371 0.5 1 86 26 38 ALA C C 180.453 0.3 1 87 26 38 ALA CA C 53.213 0.3 1 88 26 38 ALA CB C 24.215 0.3 1 89 26 38 ALA N N 117.356 0.5 1 90 27 39 ALA C C 178.589 0.3 1 91 27 39 ALA CA C 55.942 0.3 1 92 27 39 ALA CB C 19.514 0.3 1 93 27 39 ALA N N 125.26 0.5 1 94 28 40 GLY C C 173.774 0.3 1 95 28 40 GLY CA C 44.146 0.3 1 96 28 40 GLY N N 102.251 0.5 1 97 29 41 PHE C C 174.354 0.3 1 98 29 41 PHE CA C 57.195 0.3 1 99 29 41 PHE CB C 40.054 0.3 1 100 29 41 PHE N N 124.073 0.5 1 101 30 42 PRO C C 179.192 0.3 1 102 30 42 PRO CA C 64.32 0.3 1 103 30 42 PRO CB C 32.184 0.3 1 104 30 42 PRO CG C 27.955 0.3 1 105 30 42 PRO CD C 50.183 0.3 1 106 30 42 PRO N N 145.024 0.5 1 107 31 43 GLU C C 178.442 0.3 1 108 31 43 GLU CA C 61.806 0.3 1 109 31 43 GLU CB C 31.41 0.3 1 110 31 43 GLU CG C 35.839 0.3 1 111 31 43 GLU N N 118.262 0.5 1 112 32 44 LEU C C 176.987 0.3 1 113 32 44 LEU CA C 54.097 0.3 1 114 32 44 LEU CB C 42.147 0.3 1 115 32 44 LEU CG C 27.314 0.3 1 116 32 44 LEU CD1 C 23.986 0.3 2 117 32 44 LEU CD2 C 22.101 0.3 2 118 32 44 LEU N N 121.06 0.5 1 119 33 45 GLY C C 174.428 0.3 1 120 33 45 GLY CA C 46.819 0.3 1 121 33 45 GLY N N 103.691 0.5 1 122 34 46 ILE C C 177.032 0.3 1 123 34 46 ILE CA C 63.141 0.3 1 124 34 46 ILE CB C 38.93 0.3 1 125 34 46 ILE CG1 C 26.536 0.3 1 126 34 46 ILE CG2 C 18.284 0.3 1 127 34 46 ILE CD1 C 14.838 0.3 1 128 34 46 ILE N N 110.02 0.5 1 129 35 47 GLY C C 172.512 0.3 1 130 35 47 GLY CA C 44.974 0.3 1 131 35 47 GLY N N 109.076 0.5 1 132 36 48 PHE C C 179.519 0.3 1 133 36 48 PHE CA C 56.339 0.3 1 134 36 48 PHE CB C 37.814 0.3 1 135 36 48 PHE N N 117.083 0.5 1 136 40 52 ALA C C 176.389 0.3 1 137 40 52 ALA CA C 55.122 0.3 1 138 40 52 ALA CB C 18.124 0.3 1 139 40 52 ALA N N 117.071 0.5 1 140 41 53 LEU C C 176.891 0.3 1 141 41 53 LEU CA C 57.578 0.3 1 142 41 53 LEU CB C 40.916 0.3 1 143 41 53 LEU CG C 26.264 0.3 1 144 41 53 LEU CD1 C 24.351 0.3 2 145 41 53 LEU CD2 C 22.405 0.3 2 146 41 53 LEU N N 120.795 0.5 1 147 42 54 ALA C C 179.611 0.3 1 148 42 54 ALA CA C 55.921 0.3 1 149 42 54 ALA CB C 18.262 0.3 1 150 42 54 ALA N N 121.607 0.5 1 151 43 55 PHE C C 179.442 0.3 1 152 43 55 PHE CA C 64.111 0.3 1 153 43 55 PHE CB C 39.413 0.3 1 154 43 55 PHE N N 112.94 0.5 1 155 44 56 GLY C C 176.803 0.3 1 156 44 56 GLY CA C 48.322 0.3 1 157 44 56 GLY N N 104.843 0.5 1 158 45 57 LEU C C 181.847 0.3 1 159 45 57 LEU CA C 57.386 0.3 1 160 45 57 LEU CB C 40.382 0.3 1 161 45 57 LEU CG C 26.414 0.3 1 162 45 57 LEU CD1 C 25.132 0.3 2 163 45 57 LEU CD2 C 23.128 0.3 2 164 45 57 LEU N N 117.319 0.5 1 165 46 58 THR C C 175.879 0.3 1 166 46 58 THR CA C 65.87 0.3 1 167 46 58 THR CB C 68.066 0.3 1 168 46 58 THR CG2 C 24 0.3 1 169 46 58 THR N N 117.291 0.5 1 170 47 59 VAL C C 176.532 0.3 1 171 47 59 VAL CA C 66.041 0.3 1 172 47 59 VAL CB C 32.955 0.3 1 173 47 59 VAL CG1 C 25.878 0.3 2 174 47 59 VAL CG2 C 22.036 0.3 2 175 47 59 VAL N N 123.315 0.5 1 176 48 60 LEU C C 178.868 0.3 1 177 48 60 LEU CA C 59.803 0.3 1 178 48 60 LEU CB C 45.362 0.3 1 179 48 60 LEU CG C 28.502 0.3 1 180 48 60 LEU CD1 C 27.539 0.3 2 181 48 60 LEU CD2 C 25.674 0.3 2 182 48 60 LEU N N 120.743 0.5 1 183 49 61 THR C C 177.38 0.3 1 184 49 61 THR CA C 65.719 0.3 1 185 49 61 THR CB C 69.728 0.3 1 186 49 61 THR CG2 C 24.025 0.3 1 187 49 61 THR N N 105.68 0.5 1 188 50 62 MET C C 178.678 0.3 1 189 50 62 MET CA C 56.666 0.3 1 190 50 62 MET CB C 31.544 0.3 1 191 50 62 MET CG C 31.609 0.3 1 192 50 62 MET CE C 19.69 0.3 1 193 50 62 MET N N 119.702 0.5 1 194 51 63 ALA C C 181.471 0.3 1 195 51 63 ALA CA C 55.897 0.3 1 196 51 63 ALA CB C 16.57 0.3 1 197 51 63 ALA N N 124.569 0.5 1 198 52 64 PHE C C 177.322 0.3 1 199 52 64 PHE CA C 63.114 0.3 1 200 52 64 PHE CB C 39.962 0.3 1 201 52 64 PHE N N 116.411 0.5 1 202 53 65 ALA C C 177.364 0.3 1 203 53 65 ALA CA C 54.872 0.3 1 204 53 65 ALA CB C 22.51 0.3 1 205 53 65 ALA N N 118.353 0.5 1 206 54 66 VAL C C 178.822 0.3 1 207 54 66 VAL CA C 59.035 0.3 1 208 54 66 VAL CB C 33.859 0.3 1 209 54 66 VAL CG1 C 19.637 0.3 2 210 54 66 VAL CG2 C 19.7 0.3 2 211 54 66 VAL N N 100.393 0.5 1 212 55 67 GLY C C 176.323 0.3 1 213 55 67 GLY CA C 47.38 0.3 1 214 55 67 GLY N N 116.243 0.5 1 215 56 68 HIS C C 175.132 0.3 1 216 56 68 HIS CA C 56.94 0.3 1 217 56 68 HIS CB C 32.23 0.3 1 218 56 68 HIS N N 116.6 0.5 1 219 56 68 HIS ND1 N 164.047 0.5 1 220 57 69 ILE C C 176.876 0.3 1 221 57 69 ILE CA C 63.228 0.3 1 222 57 69 ILE CB C 38.273 0.3 1 223 57 69 ILE CG1 C 27.268 0.3 1 224 57 69 ILE CG2 C 17.59 0.3 1 225 57 69 ILE CD1 C 14.496 0.3 1 226 57 69 ILE N N 120.048 0.5 1 227 58 70 SER C C 176.359 0.3 1 228 58 70 SER CA C 58.47 0.3 1 229 58 70 SER CB C 66.944 0.3 1 230 58 70 SER N N 107.22 0.5 1 231 59 71 GLY C C 174.822 0.3 1 232 59 71 GLY CA C 45.128 0.3 1 233 59 71 GLY N N 114.895 0.5 1 234 60 72 GLY C C 170.8 0.3 1 235 60 72 GLY CA C 47.994 0.3 1 236 60 72 GLY N N 110.751 0.5 1 237 61 73 HIS C C 175.882 0.3 1 238 61 73 HIS CA C 56.937 0.3 1 239 61 73 HIS CB C 32.078 0.3 1 240 61 73 HIS CD2 C 112.769 0.3 1 241 61 73 HIS CE1 C 136.195 0.3 1 242 61 73 HIS N N 123.862 0.5 1 243 62 74 PHE C C 176.588 0.3 1 244 62 74 PHE CA C 54.813 0.3 1 245 62 74 PHE CB C 38.161 0.3 1 246 62 74 PHE N N 117.365 0.5 1 247 63 75 ASN C C 174.904 0.3 1 248 63 75 ASN CA C 51.427 0.3 1 249 63 75 ASN CB C 40.567 0.3 1 250 63 75 ASN CG C 178.159 0.3 1 251 63 75 ASN N N 119.564 0.5 1 252 64 76 PRO C C 177.832 0.3 1 253 64 76 PRO CA C 65.055 0.3 1 254 64 76 PRO CB C 33.801 0.3 1 255 64 76 PRO CG C 26.462 0.3 1 256 64 76 PRO CD C 51.899 0.3 1 257 64 76 PRO N N 138.329 0.5 1 258 65 77 ALA C C 180.404 0.3 1 259 65 77 ALA CA C 54.301 0.3 1 260 65 77 ALA CB C 17.731 0.3 1 261 65 77 ALA N N 113.998 0.5 1 262 66 78 VAL C C 176.613 0.3 1 263 66 78 VAL CA C 64.439 0.3 1 264 66 78 VAL CB C 32.194 0.3 1 265 66 78 VAL CG1 C 23.142 0.3 2 266 66 78 VAL CG2 C 21.271 0.3 2 267 66 78 VAL N N 118.603 0.5 1 268 67 79 THR C C 176.364 0.3 1 269 67 79 THR CA C 66.501 0.3 1 270 67 79 THR CB C 69.031 0.3 1 271 67 79 THR CG2 C 25.367 0.3 1 272 67 79 THR N N 117.569 0.5 1 273 68 80 ILE C C 177.823 0.3 1 274 68 80 ILE CA C 65.447 0.3 1 275 68 80 ILE CB C 38.035 0.3 1 276 68 80 ILE CG1 C 31.435 0.3 1 277 68 80 ILE CG2 C 18.288 0.3 1 278 68 80 ILE CD1 C 14.293 0.3 1 279 68 80 ILE N N 117.489 0.5 1 280 69 81 GLY C C 175.777 0.3 1 281 69 81 GLY CA C 47.773 0.3 1 282 69 81 GLY N N 110.686 0.5 1 283 70 82 LEU C C 180.173 0.3 1 284 70 82 LEU CA C 56.842 0.3 1 285 70 82 LEU CB C 42.407 0.3 1 286 70 82 LEU CG C 27.061 0.3 1 287 70 82 LEU CD1 C 25.797 0.3 2 288 70 82 LEU CD2 C 20.841 0.3 2 289 70 82 LEU N N 121.782 0.5 1 290 71 83 TRP C C 179.791 0.3 1 291 71 83 TRP CA C 60.536 0.3 1 292 71 83 TRP CB C 27.07 0.3 1 293 71 83 TRP N N 123.167 0.5 1 294 72 84 ALA C C 177.861 0.3 1 295 72 84 ALA CA C 54.679 0.3 1 296 72 84 ALA CB C 18.241 0.3 1 297 72 84 ALA N N 125.924 0.5 1 298 73 85 GLY C C 175.429 0.3 1 299 73 85 GLY CA C 45.169 0.3 1 300 73 85 GLY N N 102.575 0.5 1 301 74 86 GLY C C 175.279 0.3 1 302 74 86 GLY CA C 45.45 0.3 1 303 74 86 GLY N N 108.643 0.5 1 304 75 87 ARG C C 177.605 0.3 1 305 75 87 ARG CA C 54.222 0.3 1 306 75 87 ARG CB C 32.862 0.3 1 307 75 87 ARG CG C 25.859 0.3 1 308 75 87 ARG CD C 42.368 0.3 1 309 75 87 ARG N N 115.519 0.5 1 310 76 88 PHE C C 172.609 0.3 1 311 76 88 PHE CA C 55.204 0.3 1 312 76 88 PHE CB C 38.243 0.3 1 313 76 88 PHE N N 123.009 0.5 1 314 77 89 PRO C C 177.287 0.3 1 315 77 89 PRO CA C 62.301 0.3 1 316 77 89 PRO CB C 32.462 0.3 1 317 77 89 PRO CG C 27.276 0.3 1 318 77 89 PRO CD C 50.819 0.3 1 319 77 89 PRO N N 142.447 0.5 1 320 78 90 ALA C C 180.681 0.3 1 321 78 90 ALA CA C 54.717 0.3 1 322 78 90 ALA CB C 18.931 0.3 1 323 78 90 ALA N N 126.717 0.5 1 324 79 91 LYS C C 176.936 0.3 1 325 79 91 LYS CA C 58.468 0.3 1 326 79 91 LYS CB C 32.078 0.3 1 327 79 91 LYS N N 112.463 0.5 1 328 80 92 GLU C C 176.649 0.3 1 329 80 92 GLU CA C 56.7 0.3 1 330 80 92 GLU CB C 30.4 0.3 1 331 80 92 GLU CG C 37.135 0.3 1 332 80 92 GLU CD C 179.661 0.3 1 333 80 92 GLU N N 117.031 0.5 1 334 81 93 VAL C C 177.413 0.3 1 335 81 93 VAL CA C 66.518 0.3 1 336 81 93 VAL CB C 31.953 0.3 1 337 81 93 VAL CG1 C 22.525 0.3 2 338 81 93 VAL CG2 C 20.995 0.3 2 339 81 93 VAL N N 119.479 0.5 1 340 82 94 VAL C C 176.587 0.3 1 341 82 94 VAL CA C 67.26 0.3 1 342 82 94 VAL CB C 31.623 0.3 1 343 82 94 VAL CG1 C 23.81 0.3 2 344 82 94 VAL CG2 C 21.46 0.3 2 345 82 94 VAL N N 118.594 0.5 1 346 83 95 GLY C C 175.188 0.3 1 347 83 95 GLY CA C 47.902 0.3 1 348 83 95 GLY N N 105.524 0.5 1 349 84 96 TYR C C 179.195 0.3 1 350 84 96 TYR CA C 62.944 0.3 1 351 84 96 TYR CB C 38.448 0.3 1 352 84 96 TYR N N 123.014 0.5 1 353 85 97 VAL C C 179.053 0.3 1 354 85 97 VAL CA C 65.806 0.3 1 355 85 97 VAL CB C 31.583 0.3 1 356 85 97 VAL CG1 C 23.517 0.3 2 357 85 97 VAL CG2 C 21.625 0.3 2 358 85 97 VAL N N 117.862 0.5 1 359 86 98 ILE C C 180.193 0.3 1 360 86 98 ILE CA C 64.705 0.3 1 361 86 98 ILE CB C 39.056 0.3 1 362 86 98 ILE CG1 C 29.498 0.3 1 363 86 98 ILE CG2 C 17.895 0.3 1 364 86 98 ILE CD1 C 16.252 0.3 1 365 86 98 ILE N N 119.178 0.5 1 366 87 99 ALA C C 180.317 0.3 1 367 87 99 ALA CA C 56.114 0.3 1 368 87 99 ALA CB C 19.638 0.3 1 369 87 99 ALA N N 124.765 0.5 1 370 88 100 GLN C C 179.1 0.3 1 371 88 100 GLN CA C 58.437 0.3 1 372 88 100 GLN CB C 27.503 0.3 1 373 88 100 GLN CG C 32.71 0.3 1 374 88 100 GLN CD C 177.264 0.3 1 375 88 100 GLN N N 116.979 0.5 1 376 89 101 VAL C C 179.208 0.3 1 377 89 101 VAL CA C 66.994 0.3 1 378 89 101 VAL CB C 31.901 0.3 1 379 89 101 VAL CG1 C 23.851 0.3 2 380 89 101 VAL CG2 C 21.709 0.3 2 381 89 101 VAL N N 118.929 0.5 1 382 90 102 VAL C C 177.692 0.3 1 383 90 102 VAL CA C 67.262 0.3 1 384 90 102 VAL CB C 31.801 0.3 1 385 90 102 VAL CG1 C 23.972 0.3 2 386 90 102 VAL CG2 C 21.465 0.3 2 387 90 102 VAL N N 118.904 0.5 1 388 91 103 GLY C C 176.424 0.3 1 389 91 103 GLY CA C 49.071 0.3 1 390 91 103 GLY N N 106.515 0.5 1 391 95 107 ALA C C 181.467 0.3 1 392 95 107 ALA CA C 54.813 0.3 1 393 95 107 ALA CB C 19.336 0.3 1 394 95 107 ALA N N 121.142 0.5 1 395 96 108 ALA C C 178.112 0.3 1 396 96 108 ALA CA C 54.986 0.3 1 397 96 108 ALA CB C 19.892 0.3 1 398 96 108 ALA N N 120.973 0.5 1 399 97 109 ALA C C 179.5 0.3 1 400 97 109 ALA CA C 55.31 0.3 1 401 97 109 ALA CB C 20.039 0.3 1 402 97 109 ALA N N 120.614 0.5 1 403 98 110 LEU C C 176.156 0.3 1 404 98 110 LEU CA C 57.248 0.3 1 405 98 110 LEU CB C 40.937 0.3 1 406 98 110 LEU CG C 26.554 0.3 1 407 98 110 LEU N N 120.6 0.5 1 408 99 111 LEU C C 176.351 0.3 1 409 99 111 LEU CA C 57.715 0.3 1 410 99 111 LEU CB C 38.59 0.3 1 411 99 111 LEU CG C 27.472 0.3 1 412 99 111 LEU N N 115.225 0.5 1 413 100 112 TYR C C 178.467 0.3 1 414 100 112 TYR CA C 57.59 0.3 1 415 100 112 TYR CB C 37.715 0.3 1 416 100 112 TYR N N 120.826 0.5 1 417 101 113 LEU C C 179.238 0.3 1 418 101 113 LEU CA C 58.333 0.3 1 419 101 113 LEU CB C 43.279 0.3 1 420 101 113 LEU CG C 28.237 0.3 1 421 101 113 LEU CD1 C 25.432 0.3 2 422 101 113 LEU CD2 C 24.565 0.3 2 423 101 113 LEU N N 120.134 0.5 1 424 102 114 ILE C C 179.561 0.3 1 425 102 114 ILE CA C 64.597 0.3 1 426 102 114 ILE CB C 39.057 0.3 1 427 102 114 ILE CG1 C 31.543 0.3 1 428 102 114 ILE CG2 C 17.782 0.3 1 429 102 114 ILE CD1 C 16.15 0.3 1 430 102 114 ILE N N 119.007 0.5 1 431 103 115 ALA C C 178.259 0.3 1 432 103 115 ALA CA C 54.685 0.3 1 433 103 115 ALA CB C 16.656 0.3 1 434 103 115 ALA N N 124.532 0.5 1 435 104 116 SER C C 173.825 0.3 1 436 104 116 SER CA C 60.169 0.3 1 437 104 116 SER CB C 63.278 0.3 1 438 104 116 SER N N 109.48 0.5 1 439 105 117 GLY C C 172.168 0.3 1 440 105 117 GLY CA C 45.54 0.3 1 441 105 117 GLY N N 109.119 0.5 1 442 106 118 LYS C C 175.512 0.3 1 443 106 118 LYS CA C 54.206 0.3 1 444 106 118 LYS CB C 35.136 0.3 1 445 106 118 LYS CG C 24.139 0.3 1 446 106 118 LYS CD C 28.893 0.3 1 447 106 118 LYS CE C 42.395 0.3 1 448 106 118 LYS N N 122.004 0.5 1 449 107 119 THR C C 175.944 0.3 1 450 107 119 THR CA C 64.545 0.3 1 451 107 119 THR CB C 68.739 0.3 1 452 107 119 THR CG2 C 22.421 0.3 1 453 107 119 THR N N 123.068 0.5 1 454 108 120 GLY C C 174.444 0.3 1 455 108 120 GLY CA C 45.097 0.3 1 456 108 120 GLY N N 116.978 0.5 1 457 109 121 PHE C C 174.99 0.3 1 458 109 121 PHE CA C 59.055 0.3 1 459 109 121 PHE CB C 39.931 0.3 1 460 109 121 PHE N N 121.678 0.5 1 461 110 122 ASP C C 176.132 0.3 1 462 110 122 ASP CA C 52.571 0.3 1 463 110 122 ASP CB C 42.676 0.3 1 464 110 122 ASP CG C 180.991 0.3 1 465 110 122 ASP N N 129.626 0.5 1 466 111 123 ALA C C 178.233 0.3 1 467 111 123 ALA CA C 55.232 0.3 1 468 111 123 ALA CB C 19.43 0.3 1 469 111 123 ALA N N 131.16 0.5 1 470 112 124 ALA C C 181.439 0.3 1 471 112 124 ALA CA C 54.567 0.3 1 472 112 124 ALA CB C 19.4 0.3 1 473 112 124 ALA N N 117.786 0.5 1 474 113 125 ALA C C 179.734 0.3 1 475 113 125 ALA CA C 54.306 0.3 1 476 113 125 ALA CB C 19.177 0.3 1 477 113 125 ALA N N 121.228 0.5 1 478 114 126 SER C C 176.645 0.3 1 479 114 126 SER CA C 59.851 0.3 1 480 114 126 SER CB C 64.65 0.3 1 481 114 126 SER N N 109.228 0.5 1 482 115 127 GLY C C 173.817 0.3 1 483 115 127 GLY CA C 45.962 0.3 1 484 115 127 GLY N N 112.102 0.5 1 485 116 128 PHE C C 172.597 0.3 1 486 116 128 PHE CA C 57.508 0.3 1 487 116 128 PHE CB C 39.248 0.3 1 488 116 128 PHE N N 124.459 0.5 1 489 117 129 ALA C C 178.035 0.3 1 490 117 129 ALA CA C 52.169 0.3 1 491 117 129 ALA CB C 17.172 0.3 1 492 117 129 ALA N N 108.72 0.5 1 493 118 130 SER C C 175.341 0.3 1 494 118 130 SER CA C 61.144 0.3 1 495 118 130 SER CB C 64.758 0.3 1 496 118 130 SER N N 116.706 0.5 1 497 119 131 ASN C C 172.067 0.3 1 498 119 131 ASN CA C 54.664 0.3 1 499 119 131 ASN CB C 38.199 0.3 1 500 119 131 ASN CG C 177.292 0.3 1 501 119 131 ASN N N 122.909 0.5 1 502 120 132 GLY C C 170.152 0.3 1 503 120 132 GLY CA C 45.422 0.3 1 504 120 132 GLY N N 107.56 0.5 1 505 121 133 TYR C C 177.273 0.3 1 506 121 133 TYR CA C 54.606 0.3 1 507 121 133 TYR CB C 43.257 0.3 1 508 121 133 TYR N N 111.666 0.5 1 509 122 134 GLY C C 176.62 0.3 1 510 122 134 GLY CA C 46.946 0.3 1 511 122 134 GLY N N 113.61 0.5 1 512 123 135 GLU C C 176.62 0.3 1 513 123 135 GLU CA C 57.631 0.3 1 514 123 135 GLU CB C 29.221 0.3 1 515 123 135 GLU CG C 35.807 0.3 1 516 123 135 GLU N N 126.452 0.5 1 517 124 136 HIS C C 173.558 0.3 1 518 124 136 HIS CA C 52.849 0.3 1 519 124 136 HIS CB C 27.67 0.3 1 520 124 136 HIS CG C 131.136 0.3 1 521 124 136 HIS CD2 C 118.984 0.3 1 522 124 136 HIS CE1 C 132.972 0.3 1 523 124 136 HIS N N 112.84 0.5 1 524 125 137 SER C C 176.129 0.3 1 525 125 137 SER CA C 54.147 0.3 1 526 125 137 SER CB C 64.162 0.3 1 527 125 137 SER N N 121.555 0.5 1 528 126 138 PRO C C 177.8 0.3 1 529 126 138 PRO CA C 65.606 0.3 1 530 126 138 PRO CB C 31.958 0.3 1 531 126 138 PRO CG C 27.508 0.3 1 532 126 138 PRO CD C 50.445 0.3 1 533 126 138 PRO N N 144.155 0.5 1 534 127 139 GLY C C 173.709 0.3 1 535 127 139 GLY CA C 44.973 0.3 1 536 127 139 GLY N N 102.209 0.5 1 537 128 140 GLY C C 175.111 0.3 1 538 128 140 GLY CA C 46.344 0.3 1 539 128 140 GLY N N 108.473 0.5 1 540 129 141 TYR C C 176.274 0.3 1 541 129 141 TYR CA C 59.537 0.3 1 542 129 141 TYR CB C 40.72 0.3 1 543 129 141 TYR CG C 123.196 0.3 1 544 129 141 TYR CD1 C 128.865 0.3 1 545 129 141 TYR CD2 C 128.865 0.3 1 546 129 141 TYR CE1 C 117.059 0.3 1 547 129 141 TYR CE2 C 117.059 0.3 1 548 129 141 TYR N N 117.417 0.5 1 549 130 142 SER C C 174.525 0.3 1 550 130 142 SER CA C 57.212 0.3 1 551 130 142 SER CB C 65.932 0.3 1 552 130 142 SER N N 114.966 0.5 1 553 131 143 MET C C 177.882 0.3 1 554 131 143 MET CA C 59.671 0.3 1 555 131 143 MET CB C 32.66 0.3 1 556 131 143 MET N N 120.6 0.5 1 557 132 144 LEU C C 178.59 0.3 1 558 132 144 LEU CA C 58.268 0.3 1 559 132 144 LEU CB C 41.129 0.3 1 560 132 144 LEU CG C 27.131 0.3 1 561 132 144 LEU CD1 C 23.621 0.3 2 562 132 144 LEU CD2 C 22.418 0.3 2 563 132 144 LEU N N 119.148 0.5 1 564 133 145 SER C C 175.37 0.3 1 565 133 145 SER CA C 64.396 0.3 1 566 133 145 SER CB C 62.645 0.3 1 567 133 145 SER N N 116.491 0.5 1 568 134 146 ALA C C 177.844 0.3 1 569 134 146 ALA CA C 54.525 0.3 1 570 134 146 ALA CB C 20.25 0.3 1 571 134 146 ALA N N 123.2 0.5 1 572 135 147 LEU C C 177.732 0.3 1 573 135 147 LEU CA C 58.461 0.3 1 574 135 147 LEU CB C 42.008 0.3 1 575 135 147 LEU CG C 27.502 0.3 1 576 135 147 LEU CD1 C 25.91 0.3 2 577 135 147 LEU CD2 C 23.078 0.3 2 578 135 147 LEU N N 119.13 0.5 1 579 136 148 VAL C C 177.809 0.3 1 580 136 148 VAL CA C 67.353 0.3 1 581 136 148 VAL CB C 31.598 0.3 1 582 136 148 VAL CG1 C 22.852 0.3 2 583 136 148 VAL CG2 C 21.064 0.3 2 584 136 148 VAL N N 115.81 0.5 1 585 137 149 VAL C C 176.949 0.3 1 586 137 149 VAL CA C 66.28 0.3 1 587 137 149 VAL CB C 31.484 0.3 1 588 137 149 VAL CG1 C 23.937 0.3 2 589 137 149 VAL CG2 C 21.485 0.3 2 590 137 149 VAL N N 118.8 0.5 1 591 138 150 GLU C C 180.215 0.3 1 592 138 150 GLU CA C 59.931 0.3 1 593 138 150 GLU CB C 29.145 0.3 1 594 138 150 GLU CG C 37.979 0.3 1 595 138 150 GLU N N 120.778 0.5 1 596 139 151 LEU C C 178.33 0.3 1 597 139 151 LEU CA C 58.867 0.3 1 598 139 151 LEU CB C 43.406 0.3 1 599 139 151 LEU N N 122.7 0.5 1 600 140 152 VAL C C 178.493 0.3 1 601 140 152 VAL CA C 66.218 0.3 1 602 140 152 VAL CB C 31.756 0.3 1 603 140 152 VAL N N 115.89 0.5 1 604 141 153 LEU C C 179.094 0.3 1 605 141 153 LEU CA C 57.538 0.3 1 606 141 153 LEU CB C 39.713 0.3 1 607 141 153 LEU CG C 28.081 0.3 1 608 141 153 LEU CD1 C 26.182 0.3 2 609 141 153 LEU CD2 C 22.483 0.3 2 610 141 153 LEU N N 114.75 0.5 1 611 142 154 SER C C 175.867 0.3 1 612 142 154 SER CA C 63.288 0.3 1 613 142 154 SER CB C 62.306 0.3 1 614 142 154 SER N N 117.09 0.5 1 615 143 155 ALA C C 180.55 0.3 1 616 143 155 ALA CA C 55.301 0.3 1 617 143 155 ALA CB C 18.168 0.3 1 618 143 155 ALA N N 123.659 0.5 1 619 144 156 GLY C C 174.612 0.3 1 620 144 156 GLY CA C 47.039 0.3 1 621 144 156 GLY N N 105.165 0.5 1 622 145 157 PHE C C 177.434 0.3 1 623 145 157 PHE CA C 58.273 0.3 1 624 145 157 PHE CB C 38.531 0.3 1 625 145 157 PHE N N 121.233 0.5 1 626 146 158 LEU C C 181.077 0.3 1 627 146 158 LEU CA C 53.7 0.3 1 628 146 158 LEU CB C 40.37 0.3 1 629 146 158 LEU CG C 28.177 0.3 1 630 146 158 LEU CD1 C 23.605 0.3 2 631 146 158 LEU CD2 C 20.598 0.3 2 632 146 158 LEU N N 119.133 0.5 1 633 147 159 LEU C C 178.57 0.3 1 634 147 159 LEU CA C 60.181 0.3 1 635 147 159 LEU CB C 42.24 0.3 1 636 147 159 LEU CG C 28.364 0.3 1 637 147 159 LEU CD1 C 26.061 0.3 2 638 147 159 LEU CD2 C 21.957 0.3 2 639 147 159 LEU N N 127.181 0.5 1 640 148 160 VAL C C 177.389 0.3 1 641 148 160 VAL CA C 65.61 0.3 1 642 148 160 VAL CB C 31.303 0.3 1 643 148 160 VAL CG1 C 22.387 0.3 2 644 148 160 VAL CG2 C 20.906 0.3 2 645 148 160 VAL N N 119.573 0.5 1 646 149 161 ILE C C 178.969 0.3 1 647 149 161 ILE CA C 65.712 0.3 1 648 149 161 ILE CB C 38.12 0.3 1 649 149 161 ILE CG1 C 29.489 0.3 1 650 149 161 ILE CG2 C 17.147 0.3 1 651 149 161 ILE CD1 C 14.036 0.3 1 652 149 161 ILE N N 118.597 0.5 1 653 150 162 HIS C C 178.608 0.3 1 654 150 162 HIS CA C 61.732 0.3 1 655 150 162 HIS CB C 28.651 0.3 1 656 150 162 HIS CG C 129.573 0.3 1 657 150 162 HIS CE1 C 137.694 0.3 1 658 150 162 HIS N N 118.396 0.5 1 659 151 163 GLY C C 175.993 0.3 1 660 151 163 GLY CA C 48.889 0.3 1 661 151 163 GLY N N 108.52 0.5 1 662 152 164 ALA C C 177.99 0.3 1 663 152 164 ALA CA C 53.481 0.3 1 664 152 164 ALA CB C 18.021 0.3 1 665 152 164 ALA N N 119.376 0.5 1 666 153 165 THR C C 173.841 0.3 1 667 153 165 THR CA C 60.327 0.3 1 668 153 165 THR CB C 69.094 0.3 1 669 153 165 THR CG2 C 21.561 0.3 1 670 153 165 THR N N 102.149 0.5 1 671 154 166 ASP C C 177.104 0.3 1 672 154 166 ASP CA C 54.279 0.3 1 673 154 166 ASP CB C 42.874 0.3 1 674 154 166 ASP CG C 180.069 0.3 1 675 154 166 ASP N N 126.78 0.5 1 676 155 167 LYS C C 175.959 0.3 1 677 155 167 LYS CA C 57.971 0.3 1 678 155 167 LYS CB C 29.17 0.3 1 679 155 167 LYS CD C 29.287 0.3 1 680 155 167 LYS N N 128.861 0.5 1 681 156 168 PHE C C 175.705 0.3 1 682 156 168 PHE CA C 63.799 0.3 1 683 156 168 PHE CB C 39.538 0.3 1 684 156 168 PHE N N 110.688 0.5 1 685 157 169 ALA C C 176.405 0.3 1 686 157 169 ALA CA C 50.943 0.3 1 687 157 169 ALA CB C 18.175 0.3 1 688 157 169 ALA N N 124.209 0.5 1 689 158 170 PRO C C 177.524 0.3 1 690 158 170 PRO CA C 65.933 0.3 1 691 158 170 PRO CB C 31.91 0.3 1 692 158 170 PRO CD C 50.576 0.3 1 693 158 170 PRO N N 145.739 0.5 1 694 160 172 GLY C C 171.672 0.3 1 695 160 172 GLY CA C 45.522 0.3 1 696 160 172 GLY N N 108.159 0.5 1 697 161 173 PHE C C 177.972 0.3 1 698 161 173 PHE CA C 59.166 0.3 1 699 161 173 PHE CB C 41.334 0.3 1 700 161 173 PHE N N 110.438 0.5 1 701 162 174 ALA C C 175.019 0.3 1 702 162 174 ALA CA C 56.931 0.3 1 703 162 174 ALA CB C 15.937 0.3 1 704 162 174 ALA N N 123.766 0.5 1 705 163 175 PRO C C 179.518 0.3 1 706 163 175 PRO CA C 66.111 0.3 1 707 163 175 PRO CB C 31.71 0.3 1 708 163 175 PRO CG C 28.98 0.3 1 709 163 175 PRO CD C 49.798 0.3 1 710 163 175 PRO N N 130.94 0.5 1 711 164 176 ILE C C 176.689 0.3 1 712 164 176 ILE CA C 64.088 0.3 1 713 164 176 ILE CB C 38.414 0.3 1 714 164 176 ILE CG1 C 29.715 0.3 1 715 164 176 ILE CG2 C 18.262 0.3 1 716 164 176 ILE CD1 C 14.876 0.3 1 717 164 176 ILE N N 112.203 0.5 1 718 165 177 ALA C C 178.351 0.3 1 719 165 177 ALA CA C 55.411 0.3 1 720 165 177 ALA CB C 18.557 0.3 1 721 165 177 ALA N N 120.681 0.5 1 722 166 178 ILE C C 178.781 0.3 1 723 166 178 ILE CA C 65.871 0.3 1 724 166 178 ILE CB C 39.278 0.3 1 725 166 178 ILE CG1 C 29.155 0.3 1 726 166 178 ILE CG2 C 17.272 0.3 1 727 166 178 ILE CD1 C 14.263 0.3 1 728 166 178 ILE N N 115.389 0.5 1 729 167 179 GLY C C 176.146 0.3 1 730 167 179 GLY CA C 48.513 0.3 1 731 167 179 GLY N N 105.706 0.5 1 732 168 180 LEU C C 179.661 0.3 1 733 168 180 LEU CA C 57.316 0.3 1 734 168 180 LEU CB C 38.627 0.3 1 735 168 180 LEU CG C 27.451 0.3 1 736 168 180 LEU N N 116.076 0.5 1 737 169 181 ALA C C 178.902 0.3 1 738 169 181 ALA CA C 55.82 0.3 1 739 169 181 ALA CB C 17.377 0.3 1 740 169 181 ALA N N 123.433 0.5 1 741 170 182 LEU C C 181.544 0.3 1 742 170 182 LEU CA C 57.384 0.3 1 743 170 182 LEU CB C 41.32 0.3 1 744 170 182 LEU N N 119.72 0.5 1 745 171 183 THR C C 176.111 0.3 1 746 171 183 THR CA C 67.522 0.3 1 747 171 183 THR CB C 68.757 0.3 1 748 171 183 THR CG2 C 22.42 0.3 1 749 171 183 THR N N 122.712 0.5 1 750 172 184 LEU C C 176.287 0.3 1 751 172 184 LEU CA C 58.276 0.3 1 752 172 184 LEU CB C 41.155 0.3 1 753 172 184 LEU CG C 22.423 0.3 1 754 172 184 LEU N N 123.524 0.5 1 755 173 185 ILE C C 178.953 0.3 1 756 173 185 ILE CA C 65.334 0.3 1 757 173 185 ILE CB C 38.779 0.3 1 758 173 185 ILE N N 117.661 0.5 1 759 174 186 HIS C C 176.278 0.3 1 760 174 186 HIS CA C 60.372 0.3 1 761 174 186 HIS CB C 30.233 0.3 1 762 174 186 HIS N N 120.309 0.5 1 763 174 186 HIS ND1 N 162.881 0.5 1 764 175 187 LEU C C 176.065 0.3 1 765 175 187 LEU CA C 57.599 0.3 1 766 175 187 LEU CB C 40.668 0.3 1 767 175 187 LEU CG C 26.01 0.3 1 768 175 187 LEU CD1 C 22.496 0.3 2 769 175 187 LEU N N 121.028 0.5 1 770 176 188 ILE C C 175.463 0.3 1 771 176 188 ILE CA C 63.503 0.3 1 772 176 188 ILE CB C 40.094 0.3 1 773 176 188 ILE CG1 C 26.188 0.3 1 774 176 188 ILE CG2 C 18.197 0.3 1 775 176 188 ILE CD1 C 15.028 0.3 1 776 176 188 ILE N N 109.943 0.5 1 777 177 189 SER C C 176.521 0.3 1 778 177 189 SER CA C 59.619 0.3 1 779 177 189 SER CB C 67.657 0.3 1 780 177 189 SER N N 99.938 0.5 1 781 178 190 ILE C C 175.779 0.3 1 782 178 190 ILE CA C 66.726 0.3 1 783 178 190 ILE CB C 35.358 0.3 1 784 178 190 ILE CG1 C 29.944 0.3 1 785 178 190 ILE CG2 C 17.503 0.3 1 786 178 190 ILE CD1 C 14.848 0.3 1 787 178 190 ILE N N 129.419 0.5 1 788 179 191 PRO C C 175.81 0.3 1 789 179 191 PRO CA C 65.059 0.3 1 790 179 191 PRO CB C 33.148 0.3 1 791 179 191 PRO CG C 28.383 0.3 1 792 179 191 PRO CD C 49.57 0.3 1 793 179 191 PRO N N 129.372 0.5 1 794 180 192 VAL C C 179.661 0.3 1 795 180 192 VAL CA C 63.827 0.3 1 796 180 192 VAL CB C 31.925 0.3 1 797 180 192 VAL CG1 C 22.174 0.3 2 798 180 192 VAL CG2 C 20.518 0.3 2 799 180 192 VAL N N 111.01 0.5 1 800 181 193 THR C C 177.399 0.3 1 801 181 193 THR CA C 60.413 0.3 1 802 181 193 THR CB C 69.739 0.3 1 803 181 193 THR CG2 C 24.671 0.3 1 804 181 193 THR N N 104.906 0.5 1 805 182 194 ASN C C 172.243 0.3 1 806 182 194 ASN CA C 54.077 0.3 1 807 182 194 ASN CB C 39.365 0.3 1 808 182 194 ASN CG C 177.533 0.3 1 809 182 194 ASN N N 124.453 0.5 1 810 184 196 SER C C 174.181 0.3 1 811 184 196 SER CA C 58.417 0.3 1 812 184 196 SER CB C 64.068 0.3 1 813 184 196 SER N N 129.118 0.5 1 814 185 197 VAL C C 174.997 0.3 1 815 185 197 VAL CA C 62.232 0.3 1 816 185 197 VAL CB C 33.467 0.3 1 817 185 197 VAL CG1 C 22.349 0.3 2 818 185 197 VAL CG2 C 21.278 0.3 2 819 185 197 VAL N N 111.751 0.5 1 820 186 198 ASN C C 173.983 0.3 1 821 186 198 ASN CA C 52.038 0.3 1 822 186 198 ASN CB C 39.384 0.3 1 823 186 198 ASN CG C 178.669 0.3 1 824 186 198 ASN N N 110.933 0.5 1 825 187 199 PRO C C 180.774 0.3 1 826 187 199 PRO CA C 63.601 0.3 1 827 187 199 PRO CB C 31.494 0.3 1 828 187 199 PRO CG C 26.685 0.3 1 829 187 199 PRO CD C 50.64 0.3 1 830 187 199 PRO N N 134.085 0.5 1 831 188 200 ALA C C 178.466 0.3 1 832 188 200 ALA CA C 54.91 0.3 1 833 188 200 ALA CB C 18.161 0.3 1 834 188 200 ALA N N 116.985 0.5 1 835 189 201 ARG C C 179.085 0.3 1 836 189 201 ARG CA C 57.68 0.3 1 837 189 201 ARG CB C 28.564 0.3 1 838 189 201 ARG CG C 26.136 0.3 1 839 189 201 ARG CD C 43.76 0.3 1 840 189 201 ARG CZ C 159.26 0.3 1 841 189 201 ARG N N 120.811 0.5 1 842 190 202 SER C C 175.907 0.3 1 843 190 202 SER CA C 62.29 0.3 1 844 190 202 SER CB C 63.201 0.3 1 845 190 202 SER N N 115.186 0.5 1 846 191 203 THR C C 174.18 0.3 1 847 191 203 THR CA C 66.628 0.3 1 848 191 203 THR CB C 69.525 0.3 1 849 191 203 THR CG2 C 21.991 0.3 1 850 191 203 THR N N 118.377 0.5 1 851 192 204 ALA C C 176.172 0.3 1 852 192 204 ALA CA C 55.855 0.3 1 853 192 204 ALA CB C 19.78 0.3 1 854 192 204 ALA N N 118.966 0.5 1 855 193 205 VAL C C 178.71 0.3 1 856 193 205 VAL CA C 62.289 0.3 1 857 193 205 VAL CB C 30.511 0.3 1 858 193 205 VAL CG1 C 23.001 0.3 2 859 193 205 VAL CG2 C 18.855 0.3 2 860 193 205 VAL N N 97.614 0.5 1 861 194 206 ALA C C 179.668 0.3 1 862 194 206 ALA CA C 54.609 0.3 1 863 194 206 ALA CB C 19.739 0.3 1 864 194 206 ALA N N 125.453 0.5 1 865 195 207 ILE C C 176.683 0.3 1 866 195 207 ILE CA C 64.488 0.3 1 867 195 207 ILE CB C 38.779 0.3 1 868 195 207 ILE CG1 C 28.287 0.3 1 869 195 207 ILE CG2 C 20.069 0.3 1 870 195 207 ILE CD1 C 16.657 0.3 1 871 195 207 ILE N N 111.259 0.5 1 872 196 208 PHE C C 177.352 0.3 1 873 196 208 PHE CA C 57.568 0.3 1 874 196 208 PHE CB C 41.484 0.3 1 875 196 208 PHE N N 120.694 0.5 1 876 197 209 GLN C C 179.55 0.3 1 877 197 209 GLN CA C 60.45 0.3 1 878 197 209 GLN CB C 30.526 0.3 1 879 197 209 GLN CG C 31.676 0.3 1 880 197 209 GLN N N 122.584 0.5 1 881 198 210 GLY C C 176.165 0.3 1 882 198 210 GLY CA C 46.81 0.3 1 883 198 210 GLY N N 98.703 0.5 1 884 199 211 GLY C C 175.823 0.3 1 885 199 211 GLY CA C 45.48 0.3 1 886 199 211 GLY N N 109.739 0.5 1 887 200 212 TRP C C 177.741 0.3 1 888 200 212 TRP CA C 58.628 0.3 1 889 200 212 TRP CB C 28.058 0.3 1 890 200 212 TRP N N 132.325 0.5 1 891 201 213 ALA C C 181.381 0.3 1 892 201 213 ALA CA C 55.801 0.3 1 893 201 213 ALA CB C 19.816 0.3 1 894 201 213 ALA N N 124.476 0.5 1 895 202 214 LEU C C 178.081 0.3 1 896 202 214 LEU CA C 56.596 0.3 1 897 202 214 LEU CB C 42.064 0.3 1 898 202 214 LEU CG C 26.212 0.3 1 899 202 214 LEU CD1 C 23.239 0.3 2 900 202 214 LEU CD2 C 24.106 0.3 2 901 202 214 LEU N N 115.151 0.5 1 902 203 215 GLU C C 178.543 0.3 1 903 203 215 GLU CA C 59.198 0.3 1 904 203 215 GLU CB C 29.625 0.3 1 905 203 215 GLU CG C 36.555 0.3 1 906 203 215 GLU CD C 182.619 0.3 1 907 203 215 GLU N N 120.021 0.5 1 908 204 216 GLN C C 176.612 0.3 1 909 204 216 GLN CA C 56.746 0.3 1 910 204 216 GLN CB C 29.169 0.3 1 911 204 216 GLN CG C 33.672 0.3 1 912 204 216 GLN CD C 178.794 0.3 1 913 204 216 GLN N N 112.853 0.5 1 914 205 217 LEU C C 178.517 0.3 1 915 205 217 LEU CA C 58.216 0.3 1 916 205 217 LEU CB C 41.206 0.3 1 917 205 217 LEU CG C 27.523 0.3 1 918 205 217 LEU CD1 C 25.891 0.3 2 919 205 217 LEU CD2 C 23.647 0.3 2 920 205 217 LEU N N 119.44 0.5 1 921 206 218 TRP C C 176.825 0.3 1 922 206 218 TRP CA C 59.413 0.3 1 923 206 218 TRP CB C 27.428 0.3 1 924 206 218 TRP N N 116.707 0.5 1 925 207 219 PHE C C 175.48 0.3 1 926 207 219 PHE CA C 61.086 0.3 1 927 207 219 PHE CB C 40.245 0.3 1 928 207 219 PHE N N 126.828 0.5 1 929 208 220 PHE C C 173.687 0.3 1 930 208 220 PHE CA C 59.787 0.3 1 931 208 220 PHE CB C 38.183 0.3 1 932 208 220 PHE N N 115.687 0.5 1 933 209 221 TRP C C 176.95 0.3 1 934 209 221 TRP CA C 60.421 0.3 1 935 209 221 TRP CB C 29.767 0.3 1 936 209 221 TRP CD1 C 126.154 0.3 1 937 209 221 TRP CE2 C 139.34 0.3 1 938 209 221 TRP CZ2 C 114.372 0.3 1 939 209 221 TRP N N 113.985 0.5 1 940 210 222 VAL C C 176.423 0.3 1 941 210 222 VAL CA C 66.612 0.3 1 942 210 222 VAL CB C 33.166 0.3 1 943 210 222 VAL CG1 C 23.203 0.3 2 944 210 222 VAL CG2 C 21.737 0.3 2 945 210 222 VAL N N 113.678 0.5 1 946 211 223 VAL C C 174.614 0.3 1 947 211 223 VAL CA C 69.741 0.3 1 948 211 223 VAL CB C 31.21 0.3 1 949 211 223 VAL CG1 C 23.857 0.3 2 950 211 223 VAL CG2 C 22.834 0.3 2 951 211 223 VAL N N 115.731 0.5 1 952 212 224 PRO C C 179.08 0.3 1 953 212 224 PRO CA C 64.871 0.3 1 954 212 224 PRO CB C 34.886 0.3 1 955 212 224 PRO CG C 32.598 0.3 1 956 212 224 PRO CD C 50.045 0.3 1 957 212 224 PRO N N 132.75 0.5 1 958 213 225 ILE C C 177.658 0.3 1 959 213 225 ILE CA C 65.629 0.3 1 960 213 225 ILE CB C 37.085 0.3 1 961 213 225 ILE CG1 C 27.532 0.3 1 962 213 225 ILE CG2 C 17.68 0.3 1 963 213 225 ILE CD1 C 14.212 0.3 1 964 213 225 ILE N N 112.37 0.5 1 965 214 226 VAL C C 177.32 0.3 1 966 214 226 VAL CA C 67.403 0.3 1 967 214 226 VAL CB C 31.337 0.3 1 968 214 226 VAL CG1 C 24.146 0.3 2 969 214 226 VAL CG2 C 21.727 0.3 2 970 214 226 VAL N N 119.943 0.5 1 971 215 227 GLY C C 174.92 0.3 1 972 215 227 GLY CA C 47.955 0.3 1 973 215 227 GLY N N 105.638 0.5 1 974 216 228 GLY C C 175.439 0.3 1 975 216 228 GLY CA C 47.265 0.3 1 976 216 228 GLY N N 109.979 0.5 1 977 217 229 ILE C C 177.248 0.3 1 978 217 229 ILE CA C 65.789 0.3 1 979 217 229 ILE CB C 37.894 0.3 1 980 217 229 ILE CG1 C 30.328 0.3 1 981 217 229 ILE CG2 C 17.017 0.3 1 982 217 229 ILE CD1 C 14.569 0.3 1 983 217 229 ILE N N 121.467 0.5 1 984 218 230 ILE C C 177.944 0.3 1 985 218 230 ILE CA C 66.017 0.3 1 986 218 230 ILE CB C 37.312 0.3 1 987 218 230 ILE CG1 C 30.316 0.3 1 988 218 230 ILE CG2 C 16.827 0.3 1 989 218 230 ILE CD1 C 14.059 0.3 1 990 218 230 ILE N N 118.805 0.5 1 991 219 231 GLY C C 175.057 0.3 1 992 219 231 GLY CA C 48.088 0.3 1 993 219 231 GLY N N 105.826 0.5 1 994 220 232 GLY C C 175.234 0.3 1 995 220 232 GLY CA C 46.959 0.3 1 996 220 232 GLY N N 107.005 0.5 1 997 221 233 LEU C C 177.517 0.3 1 998 221 233 LEU CA C 57.475 0.3 1 999 221 233 LEU CB C 41.889 0.3 1 1000 221 233 LEU CG C 26.364 0.3 1 1001 221 233 LEU CD1 C 23.12 0.3 2 1002 221 233 LEU CD2 C 21.716 0.3 2 1003 221 233 LEU N N 119.348 0.5 1 1004 222 234 ILE C C 178.484 0.3 1 1005 222 234 ILE CA C 61.705 0.3 1 1006 222 234 ILE CB C 37.817 0.3 1 1007 222 234 ILE CG1 C 26.389 0.3 1 1008 222 234 ILE CG2 C 18.106 0.3 1 1009 222 234 ILE N N 122.306 0.5 1 1010 223 235 TYR C C 178.41 0.3 1 1011 223 235 TYR CA C 57.438 0.3 1 1012 223 235 TYR CB C 37.571 0.3 1 1013 223 235 TYR CG C 123.967 0.3 1 1014 223 235 TYR CD1 C 132.522 0.3 1 1015 223 235 TYR CD2 C 129.914 0.3 1 1016 223 235 TYR N N 120.8 0.5 1 1017 224 236 ARG C C 178.969 0.3 1 1018 224 236 ARG CA C 57.602 0.3 1 1019 224 236 ARG CB C 28.462 0.3 1 1020 224 236 ARG CG C 26.228 0.3 1 1021 224 236 ARG CD C 43.76 0.3 1 1022 224 236 ARG CZ C 160.179 0.3 1 1023 224 236 ARG N N 120.873 0.5 1 1024 224 236 ARG NH1 N 70.234 0.5 1 1025 225 237 THR C C 175.911 0.3 1 1026 225 237 THR CA C 62.267 0.3 1 1027 225 237 THR CB C 63.252 0.3 1 1028 225 237 THR CG2 C 19.51 0.3 1 1029 225 237 THR N N 115.189 0.5 1 1030 226 238 LEU C C 176.4 0.3 1 1031 226 238 LEU CA C 58.26 0.3 1 1032 226 238 LEU CB C 41.21 0.3 1 1033 226 238 LEU CG C 27.48 0.3 1 1034 226 238 LEU CD1 C 22.39 0.3 2 1035 226 238 LEU N N 123.5 0.5 1 1036 227 239 LEU C C 176.7 0.3 1 1037 227 239 LEU CA C 57.36 0.3 1 1038 227 239 LEU CB C 41.08 0.3 1 1039 227 239 LEU N N 117.3 0.5 1 1040 228 240 GLU C C 180.139 0.3 1 1041 228 240 GLU CA C 59.902 0.3 1 1042 228 240 GLU CB C 29.1 0.3 1 1043 228 240 GLU CG C 33.58 0.3 1 1044 228 240 GLU N N 120.91 0.5 1 1045 229 241 LYS C C 178.209 0.3 1 1046 229 241 LYS CA C 59.149 0.3 1 1047 229 241 LYS CB C 32.011 0.3 1 1048 229 241 LYS CD C 26.273 0.3 1 1049 229 241 LYS CE C 43.334 0.3 1 1050 229 241 LYS N N 122.737 0.5 1 1051 230 242 ARG C C 177.945 0.3 1 1052 230 242 ARG CA C 56.9 0.3 1 1053 230 242 ARG CB C 30.33 0.3 1 1054 230 242 ARG CG C 26.27 0.3 1 1055 230 242 ARG CD C 41.906 0.3 1 1056 230 242 ARG N N 115.682 0.5 1 1057 231 243 ASP C C 178.641 0.3 1 1058 231 243 ASP CA C 58.56 0.3 1 1059 231 243 ASP CB C 40.98 0.3 1 1060 231 243 ASP N N 119.144 0.5 1 stop_ save_