data_16516 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Backbone and 13Cb chemical shifts for human AP endonuclease 1 (APE1) residues 39-318 ; _BMRB_accession_number 16516 _BMRB_flat_file_name bmr16516.str _Entry_type original _Submission_date 2009-09-23 _Accession_date 2009-09-23 _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 Manvilla Brittney A. . 2 Drohat Alex C. . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 237 "13C chemical shifts" 766 "15N chemical shifts" 237 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2010-05-20 update BMRB 'complete entry citation' 2009-11-20 original author 'original release' stop_ save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title 'Chemical shift assignments for human apurinic/apyrimidinic endonuclease 1.' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 19888678 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Manvilla Brittney A. . 2 Varney Kristen M. . 3 Drohat Alexander C. . stop_ _Journal_abbreviation 'Biomol. NMR Assignments' _Journal_name_full 'Biomolecular NMR assignments' _Journal_volume 4 _Journal_issue 1 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 5 _Page_last 8 _Year 2010 _Details . loop_ _Keyword APE1 'apurinic/apyrimidinic endonuclease' 'DNA base excision repair' Ref-1 stop_ save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name 'APE1 (39-318)' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label APE1 $APE1 stop_ _System_molecular_weight 32100 _System_physical_state native _System_oligomer_state ? _System_paramagnetic no _System_thiol_state . loop_ _Biological_function 3'-phosphodiesterase 'apyrinic/apyrimidinic endonuclease' stop_ _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_APE1 _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common APE1 _Molecular_mass . _Mol_thiol_state 'free and other bound' loop_ _Biological_function 'DNA repair; transcriptional regulation' stop_ _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 286 _Mol_residue_sequence ; GSHMASGEGPALYEDPPDQK TSPSGKPATLKICSWNVDGL RAWIKKKGLDWVKEEAPDIL CLQETKCSENKLPAELQELP GLSHQYWSAPSDKEGYSGVG LLSRQCPLKVSYGIGDEEHD QEGRVIVAEFDSFVLVTAYV PNAGRGLVRLEYRQRWDEAF RKFLKGLASRKPLVLCGDLN VAHEEIDLRNPKGNKKNAGF TPQERQGFGELLQAVPLADS FRHLYPNTPYAYTFWTYMMN ARSKNVGWRLDYFLLSHSLL PALCDSKIRSKALGSDHCPI TLYLAL ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 -6 GLY 2 -5 SER 3 -4 HIS 4 -3 MET 5 -2 ALA 6 -1 SER 7 39 GLY 8 40 GLU 9 41 GLY 10 42 PRO 11 43 ALA 12 44 LEU 13 45 TYR 14 46 GLU 15 47 ASP 16 48 PRO 17 49 PRO 18 50 ASP 19 51 GLN 20 52 LYS 21 53 THR 22 54 SER 23 55 PRO 24 56 SER 25 57 GLY 26 58 LYS 27 59 PRO 28 60 ALA 29 61 THR 30 62 LEU 31 63 LYS 32 64 ILE 33 65 CYS 34 66 SER 35 67 TRP 36 68 ASN 37 69 VAL 38 70 ASP 39 71 GLY 40 72 LEU 41 73 ARG 42 74 ALA 43 75 TRP 44 76 ILE 45 77 LYS 46 78 LYS 47 79 LYS 48 80 GLY 49 81 LEU 50 82 ASP 51 83 TRP 52 84 VAL 53 85 LYS 54 86 GLU 55 87 GLU 56 88 ALA 57 89 PRO 58 90 ASP 59 91 ILE 60 92 LEU 61 93 CYS 62 94 LEU 63 95 GLN 64 96 GLU 65 97 THR 66 98 LYS 67 99 CYS 68 100 SER 69 101 GLU 70 102 ASN 71 103 LYS 72 104 LEU 73 105 PRO 74 106 ALA 75 107 GLU 76 108 LEU 77 109 GLN 78 110 GLU 79 111 LEU 80 112 PRO 81 113 GLY 82 114 LEU 83 115 SER 84 116 HIS 85 117 GLN 86 118 TYR 87 119 TRP 88 120 SER 89 121 ALA 90 122 PRO 91 123 SER 92 124 ASP 93 125 LYS 94 126 GLU 95 127 GLY 96 128 TYR 97 129 SER 98 130 GLY 99 131 VAL 100 132 GLY 101 133 LEU 102 134 LEU 103 135 SER 104 136 ARG 105 137 GLN 106 138 CYS 107 139 PRO 108 140 LEU 109 141 LYS 110 142 VAL 111 143 SER 112 144 TYR 113 145 GLY 114 146 ILE 115 147 GLY 116 148 ASP 117 149 GLU 118 150 GLU 119 151 HIS 120 152 ASP 121 153 GLN 122 154 GLU 123 155 GLY 124 156 ARG 125 157 VAL 126 158 ILE 127 159 VAL 128 160 ALA 129 161 GLU 130 162 PHE 131 163 ASP 132 164 SER 133 165 PHE 134 166 VAL 135 167 LEU 136 168 VAL 137 169 THR 138 170 ALA 139 171 TYR 140 172 VAL 141 173 PRO 142 174 ASN 143 175 ALA 144 176 GLY 145 177 ARG 146 178 GLY 147 179 LEU 148 180 VAL 149 181 ARG 150 182 LEU 151 183 GLU 152 184 TYR 153 185 ARG 154 186 GLN 155 187 ARG 156 188 TRP 157 189 ASP 158 190 GLU 159 191 ALA 160 192 PHE 161 193 ARG 162 194 LYS 163 195 PHE 164 196 LEU 165 197 LYS 166 198 GLY 167 199 LEU 168 200 ALA 169 201 SER 170 202 ARG 171 203 LYS 172 204 PRO 173 205 LEU 174 206 VAL 175 207 LEU 176 208 CYS 177 209 GLY 178 210 ASP 179 211 LEU 180 212 ASN 181 213 VAL 182 214 ALA 183 215 HIS 184 216 GLU 185 217 GLU 186 218 ILE 187 219 ASP 188 220 LEU 189 221 ARG 190 222 ASN 191 223 PRO 192 224 LYS 193 225 GLY 194 226 ASN 195 227 LYS 196 228 LYS 197 229 ASN 198 230 ALA 199 231 GLY 200 232 PHE 201 233 THR 202 234 PRO 203 235 GLN 204 236 GLU 205 237 ARG 206 238 GLN 207 239 GLY 208 240 PHE 209 241 GLY 210 242 GLU 211 243 LEU 212 244 LEU 213 245 GLN 214 246 ALA 215 247 VAL 216 248 PRO 217 249 LEU 218 250 ALA 219 251 ASP 220 252 SER 221 253 PHE 222 254 ARG 223 255 HIS 224 256 LEU 225 257 TYR 226 258 PRO 227 259 ASN 228 260 THR 229 261 PRO 230 262 TYR 231 263 ALA 232 264 TYR 233 265 THR 234 266 PHE 235 267 TRP 236 268 THR 237 269 TYR 238 270 MET 239 271 MET 240 272 ASN 241 273 ALA 242 274 ARG 243 275 SER 244 276 LYS 245 277 ASN 246 278 VAL 247 279 GLY 248 280 TRP 249 281 ARG 250 282 LEU 251 283 ASP 252 284 TYR 253 285 PHE 254 286 LEU 255 287 LEU 256 288 SER 257 289 HIS 258 290 SER 259 291 LEU 260 292 LEU 261 293 PRO 262 294 ALA 263 295 LEU 264 296 CYS 265 297 ASP 266 298 SER 267 299 LYS 268 300 ILE 269 301 ARG 270 302 SER 271 303 LYS 272 304 ALA 273 305 LEU 274 306 GLY 275 307 SER 276 308 ASP 277 309 HIS 278 310 CYS 279 311 PRO 280 312 ILE 281 313 THR 282 314 LEU 283 315 TYR 284 316 LEU 285 317 ALA 286 318 LEU stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-10-28 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 PDB 1BIX "The Crystal Structure Of The Human Dna Repair Endonuclease Hap1 Suggests The Recognition Of Extra-Helical Deoxyribose At Dna Ab" 98.60 287 99.65 100.00 0.00e+00 PDB 1DE8 "Human ApurinicAPYRIMIDINIC ENDONUCLEASE-1 (Ape1) Bound To Abasic Dna" 96.50 276 99.64 99.64 0.00e+00 PDB 1DE9 "Human Ape1 Endonuclease With Bound Abasic Dna And Mn2+ Ion" 96.50 276 99.64 99.64 0.00e+00 PDB 1DEW "Crystal Structure Of Human Ape1 Bound To Abasic Dna" 97.55 279 99.64 99.64 0.00e+00 PDB 1E9N "A Second Divalent Metal Ion In The Active Site Of A New Crystal Form Of Human ApurinicAPYRIMIDINIC ENDONUCLEASE, Ape1, And Its " 98.60 318 99.65 100.00 0.00e+00 PDB 1HD7 "A Second Divalent Metal Ion In The Active Site Of A New Crystal Form Of Human ApurinicAPYRIDINIMIC ENDONUCLEASE, Ape1, And Its " 98.60 318 99.65 100.00 0.00e+00 PDB 2ISI "Crystal Structure Of Ape1 From Homo Sapiens In A New Crystal Form Complexed With A Ligand" 98.60 317 99.65 100.00 0.00e+00 PDB 2O3H "Crystal Structure Of The Human C65a Ape" 100.00 285 99.30 99.30 0.00e+00 PDB 3U8U "Crystal Structure Of Human ApurinicAPYRIDINIMIC ENDONUCLEASE, APE1 IN A New Crystal Form" 98.60 318 99.65 100.00 0.00e+00 PDB 4IEM "Human Apurinic/apyrimidinic Endonuclease (ape1) With Product Dna And Mg2+" 98.60 317 99.65 100.00 0.00e+00 PDB 4LND "Crystal Structure Of Human Apurinic/apyrimidinic Endonuclease 1 With Essential Mg2+ Cofactor" 100.00 286 100.00 100.00 0.00e+00 PDB 4QH9 "Crystal Structure Of Mn2+ Bound Human Ape1" 100.00 285 99.30 99.30 0.00e+00 PDB 4QHD "Crystal Structure Of Apo Human Ape1" 100.00 285 99.30 99.30 0.00e+00 PDB 4QHE "Crystal Structure Of Mg2+ Bound Human Ape1" 100.00 285 99.30 99.30 0.00e+00 PDB 5DFF "Human Ape1 Product Complex" 96.50 276 100.00 100.00 0.00e+00 PDB 5DFH "Human Ape1 Mismatch Product Complex" 96.50 276 100.00 100.00 0.00e+00 PDB 5DFI "Human Ape1 Phosphorothioate Substrate Complex" 96.50 276 100.00 100.00 0.00e+00 PDB 5DFJ "Human Ape1 E96q/d210n Mismatch Substrate Complex" 96.50 276 99.28 100.00 0.00e+00 PDB 5DG0 "Human Ape1 Phosphorothioate Substrate Complex With Mn2+" 96.50 276 100.00 100.00 0.00e+00 DBJ BAA02633 "APEX nuclease [Homo sapiens]" 98.60 318 99.29 100.00 0.00e+00 DBJ BAA07270 "APEX nuclease [Mus musculus]" 98.60 317 97.16 98.58 0.00e+00 DBJ BAA14381 "apurinic/apyrimidinic endonuclease [Homo sapiens]" 98.60 318 99.29 99.65 0.00e+00 DBJ BAA14382 "APEX nuclease precursor [Mus musculus]" 98.60 317 97.16 98.58 0.00e+00 DBJ BAB28774 "unnamed protein product [Mus musculus]" 98.60 317 97.16 98.58 0.00e+00 EMBL CAA42437 "HAP1 [Homo sapiens]" 98.60 318 99.29 99.65 0.00e+00 EMBL CAA46925 "AP endonuclease 1 [Homo sapiens]" 98.60 318 99.65 100.00 0.00e+00 EMBL CAD61917 "unnamed protein product [Homo sapiens]" 98.60 318 99.65 100.00 0.00e+00 GB AAA58371 "apurinic endonuclease [Homo sapiens]" 98.60 318 98.94 99.29 0.00e+00 GB AAA58372 "apurinic/apyrimidinic endonuclease [Homo sapiens]" 98.60 318 99.65 100.00 0.00e+00 GB AAA58629 "apurinic/apyrimidinic endonuclease [Homo sapiens]" 98.60 318 99.65 100.00 0.00e+00 GB AAB22977 "Ref-1 [Homo sapiens]" 98.60 318 99.65 100.00 0.00e+00 GB AAB26054 "APEX nuclease=major apurinic/apyrimidinic endonuclease [human, Peptide, 317 aa]" 98.60 317 99.29 99.65 0.00e+00 PRF 2019234A "APEX nuclease" 98.60 318 99.29 100.00 0.00e+00 REF NP_001074954 "DNA-(apurinic or apyrimidinic site) lyase [Pan troglodytes]" 98.60 318 99.29 100.00 0.00e+00 REF NP_001138591 "DNA-(apurinic or apyrimidinic site) lyase [Canis lupus familiaris]" 98.60 318 97.52 98.94 0.00e+00 REF NP_001231178 "DNA-(apurinic or apyrimidinic site) lyase [Homo sapiens]" 98.60 318 99.65 100.00 0.00e+00 REF NP_001245038 "DNA-(apurinic or apyrimidinic site) lyase [Macaca mulatta]" 98.60 318 98.58 99.29 0.00e+00 REF NP_001277543 "APEX nuclease (multifunctional DNA repair enzyme) 1 [Panthera tigris altaica]" 98.60 318 97.87 98.94 0.00e+00 SP A1YES6 "RecName: Full=DNA-(apurinic or apyrimidinic site) lyase; AltName: Full=APEX nuclease; Short=APEN; AltName: Full=Apurinic-apyrim" 98.60 318 97.87 99.29 0.00e+00 SP A1YFZ3 "RecName: Full=DNA-(apurinic or apyrimidinic site) lyase; AltName: Full=APEX nuclease; Short=APEN; AltName: Full=Apurinic-apyrim" 98.60 318 99.29 100.00 0.00e+00 SP A2T6Y4 "RecName: Full=DNA-(apurinic or apyrimidinic site) lyase; AltName: Full=APEX nuclease; Short=APEN; AltName: Full=Apurinic-apyrim" 98.60 318 99.29 100.00 0.00e+00 SP A2T7I6 "RecName: Full=DNA-(apurinic or apyrimidinic site) lyase; AltName: Full=APEX nuclease; Short=APEN; AltName: Full=Apurinic-apyrim" 98.60 318 98.58 99.65 0.00e+00 SP P27695 "RecName: Full=DNA-(apurinic or apyrimidinic site) lyase; AltName: Full=APEX nuclease; Short=APEN; AltName: Full=Apurinic-apyrim" 98.60 318 99.65 100.00 0.00e+00 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $APE1 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 $APE1 'recombinant technology' . Escherichia coli . pET28a stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_2H_13C_15N-APE1_delta_N38 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $APE1 0.8 mM '[U-13C; U-15N; U-2H]' D2O 10 % '[U-99% 2H]' 'sodium phosphate' 20 mM 'natural abundance' 'sodium chloride' 100 mM 'natural abundance' DTT 0.5 mM 'natural abundance' EDTA 0.2 mM 'natural abundance' H2O 90 % 'natural abundance' D2O 10 % 'natural abundance' stop_ save_ ############################ # Computer software used # ############################ save_SPARKY _Saveframe_category software _Name SPARKY _Version . loop_ _Vendor _Address _Electronic_address Goddard . . stop_ loop_ _Task 'chemical shift assignment' 'data analysis' 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 'data analysis' 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_TROSY_1 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-15N TROSY' _Sample_label $2H_13C_15N-APE1_delta_N38 save_ save_3D_TROSY_HNCO_2 _Saveframe_category NMR_applied_experiment _Experiment_name '3D TROSY HNCO' _Sample_label $2H_13C_15N-APE1_delta_N38 save_ save_3D_TROSY_HNCACO_3 _Saveframe_category NMR_applied_experiment _Experiment_name '3D TROSY HNCACO' _Sample_label $2H_13C_15N-APE1_delta_N38 save_ save_3D_TROSY_HNCA_4 _Saveframe_category NMR_applied_experiment _Experiment_name '3D TROSY HNCA' _Sample_label $2H_13C_15N-APE1_delta_N38 save_ save_3D_TROSY_HNCOCA_5 _Saveframe_category NMR_applied_experiment _Experiment_name '3D TROSY HNCOCA' _Sample_label $2H_13C_15N-APE1_delta_N38 save_ save_3D_TROSY_HNCACB_6 _Saveframe_category NMR_applied_experiment _Experiment_name '3D TROSY HNCACB' _Sample_label $2H_13C_15N-APE1_delta_N38 save_ save_3D_TROSY_HNCOCACB_7 _Saveframe_category NMR_applied_experiment _Experiment_name '3D TROSY HNCOCACB' _Sample_label $2H_13C_15N-APE1_delta_N38 save_ save_3D_1H-15N_NOESY_8 _Saveframe_category NMR_applied_experiment _Experiment_name '3D 1H-15N NOESY' _Sample_label $2H_13C_15N-APE1_delta_N38 save_ ####################### # Sample conditions # ####################### save_sample_conditions_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 6.5 0.05 pH pressure 1.0 . atm temperature 298 0.1 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 _Indirect_shift_ratio_citation_label _Correction_value_citation_label DSS C 13 'methyl protons' ppm 0.00 . indirect . . . 0.251449530 $entry_citation $entry_citation DSS H 1 'methyl protons' ppm 0.00 external direct . 'separate tube (no insert) similar to the experimental sample tube' . 1.000000000 $entry_citation $entry_citation DSS N 15 'methyl protons' ppm 0.00 . indirect . . . 0.101329118 $entry_citation $entry_citation 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 TROSY' '3D TROSY HNCO' '3D TROSY HNCACO' '3D TROSY HNCA' '3D TROSY HNCOCA' '3D TROSY HNCACB' '3D TROSY HNCOCACB' stop_ loop_ _Sample_label $2H_13C_15N-APE1_delta_N38 stop_ _Sample_conditions_label $sample_conditions_1 _Chem_shift_reference_set_label $chemical_shift_reference_1 _Mol_system_component_name APE1 _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 -3 4 MET C C 175.838 0.000 1 2 -3 4 MET CA C 54.930 0.055 1 3 -3 4 MET CB C 32.047 0.039 1 4 -2 5 ALA H H 8.381 0.002 1 5 -2 5 ALA C C 177.810 0.012 1 6 -2 5 ALA CA C 52.108 0.051 1 7 -2 5 ALA CB C 18.401 0.021 1 8 -2 5 ALA N N 126.329 0.040 1 9 -1 6 SER H H 8.297 0.002 1 10 -1 6 SER C C 175.298 0.000 1 11 -1 6 SER CA C 58.043 0.086 1 12 -1 6 SER CB C 63.129 0.095 1 13 -1 6 SER N N 115.680 0.024 1 14 39 7 GLY H H 8.364 0.004 1 15 39 7 GLY C C 174.122 0.018 1 16 39 7 GLY CA C 44.983 0.032 1 17 39 7 GLY N N 111.317 0.006 1 18 40 8 GLU H H 8.221 0.002 1 19 40 8 GLU C C 176.753 0.014 1 20 40 8 GLU CA C 55.937 0.063 1 21 40 8 GLU CB C 29.815 0.047 1 22 40 8 GLU N N 120.751 0.061 1 23 41 9 GLY H H 8.259 0.002 1 24 41 9 GLY C C 171.698 0.000 1 25 41 9 GLY CA C 44.090 0.006 1 26 41 9 GLY N N 110.278 0.202 1 27 42 10 PRO C C 176.354 0.000 1 28 42 10 PRO CA C 62.810 0.068 1 29 42 10 PRO CB C 31.302 0.036 1 30 43 11 ALA H H 7.983 0.001 1 31 43 11 ALA C C 175.831 0.057 1 32 43 11 ALA CA C 50.703 0.036 1 33 43 11 ALA CB C 16.491 0.010 1 34 43 11 ALA N N 125.906 0.066 1 35 44 12 LEU H H 7.625 0.008 1 36 44 12 LEU C C 176.128 0.024 1 37 44 12 LEU CA C 54.476 0.090 1 38 44 12 LEU CB C 41.766 0.210 1 39 44 12 LEU N N 122.232 0.079 1 40 45 13 TYR H H 8.320 0.003 1 41 45 13 TYR C C 173.707 0.118 1 42 45 13 TYR CA C 57.689 0.044 1 43 45 13 TYR CB C 41.369 0.021 1 44 45 13 TYR N N 123.094 0.079 1 45 46 14 GLU H H 7.679 0.001 1 46 46 14 GLU C C 173.432 0.023 1 47 46 14 GLU CA C 53.445 0.044 1 48 46 14 GLU CB C 30.248 0.011 1 49 46 14 GLU N N 129.732 0.066 1 50 47 15 ASP H H 8.438 0.003 1 51 47 15 ASP C C 174.892 0.000 1 52 47 15 ASP CA C 52.383 0.006 1 53 47 15 ASP CB C 41.623 0.000 1 54 47 15 ASP N N 131.403 0.039 1 55 49 16 PRO C C 175.938 0.000 1 56 49 16 PRO CA C 62.866 0.067 1 57 49 16 PRO CB C 31.360 0.038 1 58 50 18 ASP H H 8.463 0.001 1 59 50 18 ASP C C 175.401 0.024 1 60 50 18 ASP CA C 55.000 0.049 1 61 50 18 ASP CB C 39.464 0.030 1 62 50 18 ASP N N 122.491 0.050 1 63 51 19 GLN H H 10.246 0.001 1 64 51 19 GLN C C 174.474 0.007 1 65 51 19 GLN CA C 54.623 0.087 1 66 51 19 GLN CB C 27.723 0.015 1 67 51 19 GLN N N 130.203 0.038 1 68 52 20 LYS H H 7.746 0.002 1 69 52 20 LYS C C 175.293 0.013 1 70 52 20 LYS CA C 55.257 0.070 1 71 52 20 LYS CB C 30.962 0.031 1 72 52 20 LYS N N 120.494 0.040 1 73 53 21 THR H H 7.338 0.001 1 74 53 21 THR C C 173.500 0.018 1 75 53 21 THR CA C 60.243 0.077 1 76 53 21 THR CB C 70.583 0.011 1 77 53 21 THR N N 113.758 0.085 1 78 54 22 SER H H 9.138 0.002 1 79 54 22 SER C C 175.222 0.000 1 80 54 22 SER CA C 56.900 0.078 1 81 54 22 SER CB C 62.445 0.000 1 82 54 22 SER N N 123.627 0.045 1 83 55 23 PRO C C 177.750 0.000 1 84 55 23 PRO CA C 65.306 0.031 1 85 55 23 PRO CB C 30.779 0.015 1 86 56 24 SER H H 7.748 0.003 1 87 56 24 SER C C 174.983 0.031 1 88 56 24 SER CA C 57.687 0.075 1 89 56 24 SER CB C 62.868 0.058 1 90 56 24 SER N N 109.350 0.049 1 91 57 25 GLY H H 8.357 0.004 1 92 57 25 GLY C C 174.212 0.016 1 93 57 25 GLY CA C 44.809 0.033 1 94 57 25 GLY N N 111.566 0.054 1 95 58 26 LYS H H 7.452 0.001 1 96 58 26 LYS CA C 53.295 0.058 1 97 58 26 LYS CB C 31.335 0.000 1 98 58 26 LYS N N 122.056 0.022 1 99 59 27 PRO C C 176.694 0.048 1 100 59 27 PRO CA C 61.732 0.065 1 101 60 28 ALA H H 8.221 0.004 1 102 60 28 ALA C C 178.164 0.016 1 103 60 28 ALA CA C 52.858 0.062 1 104 60 28 ALA CB C 18.702 0.078 1 105 60 28 ALA N N 121.056 0.227 1 106 61 29 THR H H 9.142 0.002 1 107 61 29 THR C C 173.721 0.016 1 108 61 29 THR CA C 60.481 0.027 1 109 61 29 THR CB C 70.158 0.103 1 110 61 29 THR N N 113.414 0.037 1 111 62 30 LEU H H 8.134 0.005 1 112 62 30 LEU C C 173.415 0.000 1 113 62 30 LEU CA C 54.189 0.074 1 114 62 30 LEU CB C 45.305 0.042 1 115 62 30 LEU N N 125.919 0.058 1 116 63 31 LYS H H 9.657 0.003 1 117 63 31 LYS C C 175.828 0.006 1 118 63 31 LYS CA C 53.745 0.087 1 119 63 31 LYS CB C 34.739 0.110 1 120 63 31 LYS N N 130.158 0.033 1 121 64 32 ILE H H 9.024 0.008 1 122 64 32 ILE C C 173.827 0.013 1 123 64 32 ILE CA C 59.159 0.061 1 124 64 32 ILE CB C 39.672 0.022 1 125 64 32 ILE N N 127.683 0.105 1 126 65 33 CYS H H 9.278 0.001 1 127 65 33 CYS C C 172.734 0.013 1 128 65 33 CYS CA C 56.308 0.026 1 129 65 33 CYS CB C 30.650 0.029 1 130 65 33 CYS N N 127.104 0.031 1 131 66 34 SER H H 9.370 0.004 1 132 66 34 SER C C 172.691 0.000 1 133 66 34 SER CA C 55.800 0.175 1 134 66 34 SER CB C 64.192 0.070 1 135 66 34 SER N N 124.599 0.048 1 136 67 35 TRP H H 8.958 0.003 1 137 67 35 TRP C C 173.930 0.003 1 138 67 35 TRP CA C 54.297 0.036 1 139 67 35 TRP CB C 32.870 0.052 1 140 67 35 TRP N N 129.453 0.037 1 141 68 36 ASN H H 9.366 0.003 1 142 68 36 ASN C C 175.620 0.010 1 143 68 36 ASN CA C 52.095 0.029 1 144 68 36 ASN CB C 35.055 0.034 1 145 68 36 ASN N N 126.466 0.029 1 146 69 37 VAL H H 7.216 0.004 1 147 69 37 VAL C C 173.694 0.006 1 148 69 37 VAL CA C 60.681 0.099 1 149 69 37 VAL CB C 30.134 0.000 1 150 69 37 VAL N N 116.699 0.083 1 151 70 38 ASP H H 7.556 0.007 1 152 70 38 ASP C C 175.416 0.000 1 153 70 38 ASP CA C 55.751 0.092 1 154 70 38 ASP CB C 39.477 0.017 1 155 70 38 ASP N N 115.343 0.125 1 156 71 39 GLY H H 8.328 0.003 1 157 71 39 GLY C C 172.666 0.003 1 158 71 39 GLY CA C 44.294 0.032 1 159 71 39 GLY N N 106.530 0.060 1 160 72 40 LEU H H 8.849 0.002 1 161 72 40 LEU C C 178.314 0.018 1 162 72 40 LEU CA C 58.281 0.014 1 163 72 40 LEU CB C 43.443 0.091 1 164 72 40 LEU N N 126.397 0.046 1 165 73 41 ARG H H 8.349 0.007 1 166 73 41 ARG C C 179.090 0.008 1 167 73 41 ARG CA C 60.103 0.071 1 168 73 41 ARG CB C 28.397 0.016 1 169 73 41 ARG N N 115.563 0.060 1 170 74 42 ALA H H 7.981 0.004 1 171 74 42 ALA C C 179.088 0.008 1 172 74 42 ALA CA C 54.753 0.041 1 173 74 42 ALA CB C 17.522 0.044 1 174 74 42 ALA N N 125.585 0.097 1 175 75 43 TRP H H 8.700 0.006 1 176 75 43 TRP C C 179.739 0.011 1 177 75 43 TRP CA C 60.129 0.083 1 178 75 43 TRP CB C 27.340 0.047 1 179 75 43 TRP N N 123.346 0.091 1 180 76 44 ILE H H 8.427 0.002 1 181 76 44 ILE C C 181.554 0.009 1 182 76 44 ILE CA C 64.507 0.040 1 183 76 44 ILE CB C 37.173 0.013 1 184 76 44 ILE N N 119.875 0.062 1 185 77 45 LYS H H 7.727 0.001 1 186 77 45 LYS C C 178.040 0.007 1 187 77 45 LYS CA C 58.763 0.044 1 188 77 45 LYS CB C 30.841 0.064 1 189 77 45 LYS N N 123.692 0.068 1 190 78 46 LYS H H 7.634 0.004 1 191 78 46 LYS C C 174.663 0.022 1 192 78 46 LYS CA C 56.311 0.062 1 193 78 46 LYS CB C 31.315 0.040 1 194 78 46 LYS N N 119.545 0.097 1 195 79 47 LYS H H 7.463 0.003 1 196 79 47 LYS C C 178.427 0.000 1 197 79 47 LYS CA C 57.034 0.008 1 198 79 47 LYS CB C 26.567 0.000 1 199 79 47 LYS N N 110.016 0.047 1 200 84 52 VAL C C 177.755 0.030 1 201 84 52 VAL CA C 66.525 0.046 1 202 84 52 VAL CB C 30.909 0.015 1 203 85 53 LYS H H 7.983 0.007 1 204 85 53 LYS C C 178.606 0.008 1 205 85 53 LYS CA C 59.347 0.018 1 206 85 53 LYS CB C 31.574 0.016 1 207 85 53 LYS N N 118.348 0.065 1 208 86 54 GLU H H 6.927 0.002 1 209 86 54 GLU C C 177.605 0.000 1 210 86 54 GLU CA C 57.724 0.031 1 211 86 54 GLU CB C 28.606 0.000 1 212 86 54 GLU N N 118.345 0.066 1 213 87 55 GLU C C 176.046 0.000 1 214 87 55 GLU CA C 56.750 0.092 1 215 87 55 GLU CB C 29.446 0.000 1 216 88 56 ALA H H 8.266 0.007 1 217 88 56 ALA C C 174.521 0.000 1 218 88 56 ALA CA C 51.653 0.067 1 219 88 56 ALA CB C 16.551 0.000 1 220 88 56 ALA N N 117.180 0.104 1 221 90 58 ASP C C 175.871 0.000 1 222 90 58 ASP CA C 57.046 0.071 1 223 90 58 ASP CB C 42.995 0.000 1 224 91 59 ILE H H 7.485 0.011 1 225 91 59 ILE C C 173.071 0.006 1 226 91 59 ILE CA C 60.048 0.044 1 227 91 59 ILE CB C 42.291 0.068 1 228 91 59 ILE N N 115.087 0.044 1 229 92 60 LEU H H 9.905 0.002 1 230 92 60 LEU C C 173.625 0.001 1 231 92 60 LEU CA C 52.362 0.055 1 232 92 60 LEU CB C 45.529 0.086 1 233 92 60 LEU N N 130.583 0.027 1 234 93 61 CYS H H 9.537 0.003 1 235 93 61 CYS C C 172.687 0.007 1 236 93 61 CYS CA C 56.485 0.067 1 237 93 61 CYS CB C 29.720 0.021 1 238 93 61 CYS N N 126.731 0.062 1 239 94 62 LEU H H 9.002 0.008 1 240 94 62 LEU C C 177.275 0.040 1 241 94 62 LEU CA C 51.932 0.121 1 242 94 62 LEU CB C 45.092 0.081 1 243 94 62 LEU N N 122.532 0.156 1 244 95 63 GLN H H 8.075 0.005 1 245 95 63 GLN C C 174.500 0.020 1 246 95 63 GLN CA C 54.204 0.063 1 247 95 63 GLN CB C 29.639 0.039 1 248 95 63 GLN N N 115.980 0.038 1 249 96 64 GLU H H 8.358 0.021 1 250 96 64 GLU C C 175.822 0.000 1 251 96 64 GLU CA C 57.677 0.055 1 252 96 64 GLU N N 122.983 0.083 1 253 97 65 THR H H 7.749 0.008 1 254 97 65 THR C C 177.551 0.025 1 255 97 65 THR CA C 63.539 0.079 1 256 97 65 THR CB C 66.540 0.031 1 257 97 65 THR N N 110.411 0.108 1 258 98 66 LYS H H 9.319 0.003 1 259 98 66 LYS C C 175.114 0.008 1 260 98 66 LYS CA C 57.076 0.068 1 261 98 66 LYS CB C 29.960 0.060 1 262 98 66 LYS N N 118.115 0.121 1 263 99 67 CYS H H 7.508 0.008 1 264 99 67 CYS C C 172.450 0.005 1 265 99 67 CYS CA C 57.586 0.075 1 266 99 67 CYS CB C 29.664 0.017 1 267 99 67 CYS N N 116.097 0.285 1 268 100 68 SER H H 8.363 0.005 1 269 100 68 SER C C 174.966 0.000 1 270 100 68 SER CA C 57.165 0.045 1 271 100 68 SER CB C 63.966 0.005 1 272 100 68 SER N N 119.616 0.081 1 273 101 69 GLU C C 176.482 0.000 1 274 101 69 GLU CA C 57.856 0.056 1 275 102 70 ASN H H 8.099 0.003 1 276 102 70 ASN C C 175.190 0.023 1 277 102 70 ASN CA C 53.534 0.082 1 278 102 70 ASN CB C 37.669 0.010 1 279 102 70 ASN N N 115.350 0.052 1 280 103 71 LYS H H 7.349 0.002 1 281 103 71 LYS CA C 54.141 0.046 1 282 103 71 LYS CB C 31.952 0.000 1 283 103 71 LYS N N 120.451 0.048 1 284 105 73 PRO C C 177.773 0.000 1 285 105 73 PRO CA C 62.356 0.041 1 286 105 73 PRO CB C 31.425 0.000 1 287 106 74 ALA H H 8.774 0.001 1 288 106 74 ALA C C 179.905 0.005 1 289 106 74 ALA CA C 54.261 0.020 1 290 106 74 ALA CB C 17.701 0.026 1 291 106 74 ALA N N 129.250 0.040 1 292 107 75 GLU H H 10.051 0.004 1 293 107 75 GLU C C 178.492 0.015 1 294 107 75 GLU CA C 59.972 0.043 1 295 107 75 GLU CB C 28.299 0.032 1 296 107 75 GLU N N 118.154 0.056 1 297 108 76 LEU H H 7.143 0.002 1 298 108 76 LEU C C 178.131 0.047 1 299 108 76 LEU CA C 56.012 0.022 1 300 108 76 LEU CB C 40.176 0.019 1 301 108 76 LEU N N 116.862 0.051 1 302 109 77 GLN H H 7.680 0.001 1 303 109 77 GLN C C 176.747 0.033 1 304 109 77 GLN CA C 56.767 0.037 1 305 109 77 GLN CB C 27.711 0.038 1 306 109 77 GLN N N 116.845 0.044 1 307 110 78 GLU H H 7.410 0.006 1 308 110 78 GLU C C 175.751 0.004 1 309 110 78 GLU CA C 54.808 0.020 1 310 110 78 GLU CB C 28.483 0.035 1 311 110 78 GLU N N 117.138 0.029 1 312 111 79 LEU H H 6.972 0.001 1 313 111 79 LEU C C 174.854 0.000 1 314 111 79 LEU CA C 52.034 0.002 1 315 111 79 LEU CB C 41.684 0.000 1 316 111 79 LEU N N 121.692 0.029 1 317 112 80 PRO C C 178.142 0.022 1 318 112 80 PRO CA C 63.416 0.055 1 319 112 80 PRO CB C 30.789 0.009 1 320 113 81 GLY H H 8.666 0.001 1 321 113 81 GLY C C 174.389 0.006 1 322 113 81 GLY CA C 45.515 0.029 1 323 113 81 GLY N N 110.086 0.032 1 324 114 82 LEU H H 7.188 0.002 1 325 114 82 LEU C C 176.179 0.000 1 326 114 82 LEU CA C 52.246 0.016 1 327 114 82 LEU CB C 40.663 0.015 1 328 114 82 LEU N N 123.382 0.064 1 329 115 83 SER H H 7.649 0.001 1 330 115 83 SER C C 174.808 0.000 1 331 115 83 SER CA C 60.106 0.088 1 332 115 83 SER CB C 63.331 0.046 1 333 115 83 SER N N 113.200 0.049 1 334 116 84 HIS H H 7.909 0.004 1 335 116 84 HIS C C 173.177 0.009 1 336 116 84 HIS CA C 55.490 0.042 1 337 116 84 HIS CB C 27.027 0.075 1 338 116 84 HIS N N 123.226 0.054 1 339 117 85 GLN H H 7.928 0.006 1 340 117 85 GLN C C 173.604 0.024 1 341 117 85 GLN CA C 54.065 0.043 1 342 117 85 GLN CB C 29.555 0.028 1 343 117 85 GLN N N 122.889 0.079 1 344 118 86 TYR H H 8.613 0.005 1 345 118 86 TYR C C 172.916 0.007 1 346 118 86 TYR CA C 56.920 0.054 1 347 118 86 TYR CB C 39.979 0.022 1 348 118 86 TYR N N 123.606 0.064 1 349 119 87 TRP H H 8.630 0.002 1 350 119 87 TRP C C 175.201 0.000 1 351 119 87 TRP CA C 55.403 0.007 1 352 119 87 TRP CB C 32.758 0.000 1 353 119 87 TRP N N 120.588 0.033 1 354 120 88 SER C C 173.106 0.000 1 355 120 88 SER CA C 56.669 0.084 1 356 121 89 ALA H H 8.391 0.003 1 357 121 89 ALA C C 177.809 0.000 1 358 121 89 ALA CA C 50.306 0.067 1 359 121 89 ALA CB C 18.872 0.000 1 360 121 89 ALA N N 128.998 0.139 1 361 130 98 GLY C C 175.182 0.000 1 362 130 98 GLY CA C 45.197 0.085 1 363 131 99 VAL H H 8.340 0.002 1 364 131 99 VAL C C 174.743 0.017 1 365 131 99 VAL CA C 58.598 0.033 1 366 131 99 VAL CB C 36.533 0.059 1 367 131 99 VAL N N 117.619 0.046 1 368 132 100 GLY H H 8.891 0.002 1 369 132 100 GLY C C 170.847 0.004 1 370 132 100 GLY CA C 44.524 0.074 1 371 132 100 GLY N N 108.147 0.089 1 372 133 101 LEU H H 8.677 0.003 1 373 133 101 LEU C C 173.398 0.010 1 374 133 101 LEU CA C 54.809 0.134 1 375 133 101 LEU CB C 45.332 0.095 1 376 133 101 LEU N N 124.009 0.115 1 377 134 102 LEU H H 9.615 0.002 1 378 134 102 LEU C C 175.526 0.022 1 379 134 102 LEU CA C 54.194 0.040 1 380 134 102 LEU CB C 43.240 0.038 1 381 134 102 LEU N N 127.641 0.040 1 382 135 103 SER H H 9.591 0.002 1 383 135 103 SER C C 174.766 0.008 1 384 135 103 SER CA C 56.867 0.042 1 385 135 103 SER CB C 65.881 0.031 1 386 135 103 SER N N 116.054 0.044 1 387 136 104 ARG H H 8.964 0.001 1 388 136 104 ARG C C 178.855 0.026 1 389 136 104 ARG CA C 58.762 0.051 1 390 136 104 ARG CB C 30.277 0.112 1 391 136 104 ARG N N 129.331 0.057 1 392 137 105 GLN H H 8.631 0.002 1 393 137 105 GLN C C 175.977 0.001 1 394 137 105 GLN CA C 53.489 0.038 1 395 137 105 GLN CB C 29.535 0.058 1 396 137 105 GLN N N 117.342 0.043 1 397 138 106 CYS H H 8.916 0.002 1 398 138 106 CYS C C 173.114 0.000 1 399 138 106 CYS CA C 57.261 0.019 1 400 138 106 CYS CB C 26.375 0.000 1 401 138 106 CYS N N 127.268 0.050 1 402 139 107 PRO C C 175.811 0.000 1 403 139 107 PRO CA C 62.161 0.051 1 404 139 107 PRO CB C 30.628 0.000 1 405 140 108 LEU H H 8.427 0.004 1 406 140 108 LEU C C 177.993 0.002 1 407 140 108 LEU CA C 56.565 0.025 1 408 140 108 LEU CB C 41.194 0.015 1 409 140 108 LEU N N 122.307 0.039 1 410 141 109 LYS H H 6.738 0.002 1 411 141 109 LYS C C 173.782 0.003 1 412 141 109 LYS CA C 55.519 0.031 1 413 141 109 LYS CB C 34.774 0.027 1 414 141 109 LYS N N 114.230 0.031 1 415 142 110 VAL H H 8.221 0.002 1 416 142 110 VAL C C 174.856 0.007 1 417 142 110 VAL CA C 60.476 0.040 1 418 142 110 VAL CB C 33.363 0.045 1 419 142 110 VAL N N 126.180 0.022 1 420 143 111 SER H H 9.006 0.004 1 421 143 111 SER C C 171.004 0.016 1 422 143 111 SER CA C 56.352 0.087 1 423 143 111 SER CB C 64.799 0.011 1 424 143 111 SER N N 122.140 0.031 1 425 144 112 TYR H H 8.478 0.004 1 426 144 112 TYR C C 176.414 0.021 1 427 144 112 TYR CA C 56.513 0.066 1 428 144 112 TYR CB C 39.853 0.071 1 429 144 112 TYR N N 119.578 0.039 1 430 145 113 GLY H H 7.673 0.004 1 431 145 113 GLY C C 171.408 0.011 1 432 145 113 GLY CA C 43.916 0.065 1 433 145 113 GLY N N 109.646 0.055 1 434 146 114 ILE H H 9.988 0.003 1 435 146 114 ILE C C 176.749 0.101 1 436 146 114 ILE CA C 59.025 0.125 1 437 146 114 ILE CB C 38.346 0.001 1 438 146 114 ILE N N 111.473 0.043 1 439 147 115 GLY H H 9.029 0.005 1 440 147 115 GLY C C 173.915 0.005 1 441 147 115 GLY CA C 45.441 0.059 1 442 147 115 GLY N N 114.826 0.093 1 443 148 116 ASP H H 7.489 0.002 1 444 148 116 ASP C C 175.698 0.043 1 445 148 116 ASP CA C 52.786 0.184 1 446 148 116 ASP CB C 43.595 0.040 1 447 148 116 ASP N N 120.033 0.028 1 448 149 117 GLU H H 8.901 0.011 1 449 149 117 GLU C C 178.545 0.003 1 450 149 117 GLU CA C 59.731 0.080 1 451 149 117 GLU CB C 28.903 0.106 1 452 149 117 GLU N N 127.012 0.120 1 453 150 118 GLU H H 8.364 0.007 1 454 150 118 GLU C C 178.068 0.008 1 455 150 118 GLU CA C 58.298 0.044 1 456 150 118 GLU CB C 28.807 0.074 1 457 150 118 GLU N N 118.545 0.084 1 458 151 119 HIS H H 7.467 0.005 1 459 151 119 HIS C C 176.777 0.008 1 460 151 119 HIS CA C 56.286 0.087 1 461 151 119 HIS CB C 31.916 0.064 1 462 151 119 HIS N N 115.078 0.130 1 463 152 120 ASP H H 7.530 0.008 1 464 152 120 ASP CA C 54.669 0.025 1 465 152 120 ASP CB C 40.702 0.000 1 466 152 120 ASP N N 120.583 0.169 1 467 156 124 ARG C C 176.367 0.000 1 468 156 124 ARG CA C 58.136 0.062 1 469 156 124 ARG CB C 33.269 0.061 1 470 157 125 VAL H H 7.587 0.001 1 471 157 125 VAL C C 176.889 0.016 1 472 157 125 VAL CA C 61.098 0.030 1 473 157 125 VAL CB C 37.637 0.020 1 474 157 125 VAL N N 116.326 0.101 1 475 158 126 ILE H H 8.502 0.006 1 476 158 126 ILE C C 172.707 0.001 1 477 158 126 ILE CA C 61.299 0.067 1 478 158 126 ILE CB C 41.325 0.008 1 479 158 126 ILE N N 129.172 0.048 1 480 159 127 VAL H H 8.611 0.004 1 481 159 127 VAL C C 174.166 0.018 1 482 159 127 VAL CA C 60.434 0.055 1 483 159 127 VAL CB C 32.252 0.052 1 484 159 127 VAL N N 127.457 0.032 1 485 160 128 ALA H H 9.779 0.002 1 486 160 128 ALA C C 173.514 0.022 1 487 160 128 ALA CA C 49.304 0.062 1 488 160 128 ALA CB C 21.322 0.019 1 489 160 128 ALA N N 130.320 0.064 1 490 161 129 GLU H H 8.539 0.001 1 491 161 129 GLU C C 173.633 0.017 1 492 161 129 GLU CA C 55.527 0.047 1 493 161 129 GLU CB C 29.695 0.043 1 494 161 129 GLU N N 124.408 0.043 1 495 162 130 PHE H H 8.316 0.004 1 496 162 130 PHE C C 174.843 0.012 1 497 162 130 PHE CA C 56.746 0.042 1 498 162 130 PHE CB C 39.436 0.113 1 499 162 130 PHE N N 125.475 0.064 1 500 163 131 ASP H H 8.821 0.001 1 501 163 131 ASP C C 178.335 0.007 1 502 163 131 ASP CA C 58.698 0.050 1 503 163 131 ASP CB C 40.022 0.073 1 504 163 131 ASP N N 120.935 0.049 1 505 164 132 SER H H 8.457 0.003 1 506 164 132 SER C C 173.500 0.029 1 507 164 132 SER CA C 57.745 0.068 1 508 164 132 SER CB C 64.357 0.026 1 509 164 132 SER N N 108.508 0.028 1 510 165 133 PHE H H 7.071 0.002 1 511 165 133 PHE C C 171.030 0.008 1 512 165 133 PHE CA C 55.596 0.074 1 513 165 133 PHE CB C 38.928 0.050 1 514 165 133 PHE N N 114.913 0.099 1 515 166 134 VAL H H 9.184 0.002 1 516 166 134 VAL C C 172.088 0.009 1 517 166 134 VAL CA C 60.290 0.041 1 518 166 134 VAL CB C 33.098 0.020 1 519 166 134 VAL N N 120.508 0.057 1 520 167 135 LEU H H 9.137 0.001 1 521 167 135 LEU C C 174.282 0.008 1 522 167 135 LEU CA C 52.295 0.044 1 523 167 135 LEU CB C 44.745 0.107 1 524 167 135 LEU N N 130.205 0.036 1 525 168 136 VAL H H 9.543 0.004 1 526 168 136 VAL C C 175.870 0.012 1 527 168 136 VAL CA C 59.925 0.156 1 528 168 136 VAL CB C 33.532 0.030 1 529 168 136 VAL N N 126.891 0.102 1 530 169 137 THR H H 9.012 0.004 1 531 169 137 THR C C 171.476 0.020 1 532 169 137 THR CA C 58.020 0.049 1 533 169 137 THR CB C 70.814 0.078 1 534 169 137 THR N N 121.930 0.128 1 535 170 138 ALA H H 8.232 0.003 1 536 170 138 ALA C C 174.697 0.036 1 537 170 138 ALA CA C 49.295 0.070 1 538 170 138 ALA CB C 24.755 0.024 1 539 170 138 ALA N N 128.056 0.063 1 540 171 139 TYR H H 8.458 0.003 1 541 171 139 TYR C C 174.932 0.008 1 542 171 139 TYR CA C 52.283 0.023 1 543 171 139 TYR CB C 38.247 0.090 1 544 171 139 TYR N N 120.488 0.126 1 545 172 140 VAL H H 7.974 0.006 1 546 172 140 VAL C C 172.794 0.000 1 547 172 140 VAL CA C 60.605 0.026 1 548 172 140 VAL CB C 32.678 0.000 1 549 172 140 VAL N N 130.244 0.053 1 550 173 141 PRO C C 174.655 0.000 1 551 173 141 PRO CA C 62.516 0.011 1 552 173 141 PRO CB C 30.486 0.054 1 553 174 142 ASN H H 7.743 0.003 1 554 174 142 ASN C C 176.285 0.013 1 555 174 142 ASN CA C 52.774 0.057 1 556 174 142 ASN CB C 39.948 0.009 1 557 174 142 ASN N N 124.854 0.041 1 558 175 143 ALA H H 9.442 0.003 1 559 175 143 ALA C C 176.681 0.012 1 560 175 143 ALA CA C 54.243 0.026 1 561 175 143 ALA CB C 17.904 0.028 1 562 175 143 ALA N N 128.160 0.028 1 563 176 144 GLY H H 8.442 0.003 1 564 176 144 GLY C C 175.117 0.000 1 565 176 144 GLY CA C 43.610 0.042 1 566 176 144 GLY N N 104.710 0.035 1 567 177 145 ARG H H 8.659 0.002 1 568 177 145 ARG C C 179.483 0.000 1 569 177 145 ARG CA C 57.236 0.010 1 570 177 145 ARG CB C 28.397 0.000 1 571 177 145 ARG N N 125.005 0.023 1 572 178 146 GLY C C 173.921 0.000 1 573 178 146 GLY CA C 46.038 0.028 1 574 179 147 LEU H H 8.050 0.002 1 575 179 147 LEU C C 179.434 0.000 1 576 179 147 LEU CA C 54.947 0.140 1 577 179 147 LEU CB C 37.169 0.030 1 578 179 147 LEU N N 112.096 0.032 1 579 180 148 VAL H H 6.965 0.005 1 580 180 148 VAL C C 176.784 0.024 1 581 180 148 VAL CA C 64.067 0.037 1 582 180 148 VAL CB C 30.863 0.022 1 583 180 148 VAL N N 114.563 0.038 1 584 181 149 ARG H H 8.552 0.004 1 585 181 149 ARG C C 177.244 0.110 1 586 181 149 ARG CA C 54.216 0.039 1 587 181 149 ARG CB C 30.246 0.068 1 588 181 149 ARG N N 121.672 0.070 1 589 182 150 LEU H H 7.524 0.002 1 590 182 150 LEU C C 177.911 0.012 1 591 182 150 LEU CA C 58.001 0.038 1 592 182 150 LEU CB C 41.818 0.020 1 593 182 150 LEU N N 123.252 0.067 1 594 183 151 GLU H H 8.682 0.001 1 595 183 151 GLU C C 179.608 0.006 1 596 183 151 GLU CA C 59.899 0.045 1 597 183 151 GLU CB C 27.752 0.016 1 598 183 151 GLU N N 120.262 0.054 1 599 184 152 TYR H H 8.071 0.001 1 600 184 152 TYR C C 176.932 0.033 1 601 184 152 TYR CA C 61.648 0.085 1 602 184 152 TYR CB C 37.192 0.005 1 603 184 152 TYR N N 120.752 0.062 1 604 185 153 ARG H H 8.527 0.002 1 605 185 153 ARG C C 176.983 0.026 1 606 185 153 ARG CA C 57.256 0.137 1 607 185 153 ARG CB C 27.782 0.019 1 608 185 153 ARG N N 121.230 0.060 1 609 186 154 GLN H H 8.124 0.005 1 610 186 154 GLN C C 179.147 0.031 1 611 186 154 GLN CA C 59.404 0.061 1 612 186 154 GLN CB C 29.211 0.121 1 613 186 154 GLN N N 118.283 0.205 1 614 187 155 ARG H H 7.376 0.005 1 615 187 155 ARG C C 179.611 0.032 1 616 187 155 ARG CA C 59.447 0.052 1 617 187 155 ARG CB C 29.107 0.022 1 618 187 155 ARG N N 120.895 0.053 1 619 188 156 TRP H H 8.675 0.010 1 620 188 156 TRP C C 176.493 0.010 1 621 188 156 TRP CA C 60.183 0.080 1 622 188 156 TRP CB C 25.936 0.027 1 623 188 156 TRP N N 122.197 0.178 1 624 189 157 ASP H H 9.155 0.004 1 625 189 157 ASP C C 179.621 0.019 1 626 189 157 ASP CA C 57.566 0.152 1 627 189 157 ASP CB C 38.715 0.087 1 628 189 157 ASP N N 119.711 0.092 1 629 190 158 GLU H H 7.156 0.003 1 630 190 158 GLU C C 177.385 0.008 1 631 190 158 GLU CA C 59.043 0.063 1 632 190 158 GLU CB C 28.855 0.004 1 633 190 158 GLU N N 119.204 0.110 1 634 191 159 ALA H H 7.573 0.004 1 635 191 159 ALA C C 180.972 0.013 1 636 191 159 ALA CA C 54.329 0.046 1 637 191 159 ALA CB C 17.874 0.027 1 638 191 159 ALA N N 122.700 0.051 1 639 192 160 PHE H H 9.168 0.005 1 640 192 160 PHE C C 177.043 0.035 1 641 192 160 PHE CA C 58.051 0.123 1 642 192 160 PHE CB C 37.902 0.047 1 643 192 160 PHE N N 121.263 0.190 1 644 193 161 ARG H H 7.770 0.004 1 645 193 161 ARG C C 177.330 0.035 1 646 193 161 ARG CA C 59.190 0.080 1 647 193 161 ARG CB C 28.827 0.035 1 648 193 161 ARG N N 118.341 0.077 1 649 194 162 LYS H H 7.460 0.007 1 650 194 162 LYS C C 179.556 0.008 1 651 194 162 LYS CA C 59.517 0.073 1 652 194 162 LYS CB C 31.197 0.117 1 653 194 162 LYS N N 119.095 0.074 1 654 195 163 PHE H H 7.758 0.005 1 655 195 163 PHE C C 178.029 0.003 1 656 195 163 PHE CA C 59.515 0.116 1 657 195 163 PHE CB C 38.920 0.885 1 658 195 163 PHE N N 121.738 0.044 1 659 196 164 LEU H H 8.156 0.139 1 660 196 164 LEU C C 178.216 0.027 1 661 196 164 LEU CA C 56.843 0.086 1 662 196 164 LEU CB C 40.873 0.149 1 663 196 164 LEU N N 120.671 0.124 1 664 197 165 LYS H H 8.131 0.002 1 665 197 165 LYS C C 179.272 0.040 1 666 197 165 LYS CA C 59.475 0.073 1 667 197 165 LYS CB C 31.463 0.106 1 668 197 165 LYS N N 118.831 0.123 1 669 198 166 GLY H H 7.383 0.003 1 670 198 166 GLY C C 176.889 0.008 1 671 198 166 GLY CA C 46.462 0.023 1 672 198 166 GLY N N 105.129 0.122 1 673 199 167 LEU H H 7.283 0.002 1 674 199 167 LEU C C 178.877 0.004 1 675 199 167 LEU CA C 57.058 0.023 1 676 199 167 LEU CB C 41.899 0.018 1 677 199 167 LEU N N 123.841 0.035 1 678 200 168 ALA H H 8.040 0.003 1 679 200 168 ALA C C 178.222 0.001 1 680 200 168 ALA CA C 52.272 0.015 1 681 200 168 ALA CB C 17.741 0.014 1 682 200 168 ALA N N 119.490 0.090 1 683 201 169 SER H H 7.309 0.001 1 684 201 169 SER C C 174.782 0.000 1 685 201 169 SER CA C 59.845 0.070 1 686 201 169 SER CB C 62.694 0.066 1 687 201 169 SER N N 112.105 0.072 1 688 202 170 ARG H H 7.577 0.018 1 689 202 170 ARG C C 175.850 0.042 1 690 202 170 ARG CA C 56.638 0.071 1 691 202 170 ARG CB C 31.015 0.059 1 692 202 170 ARG N N 120.298 0.150 1 693 203 171 LYS H H 7.621 0.004 1 694 203 171 LYS C C 171.627 0.000 1 695 203 171 LYS CA C 54.000 0.059 1 696 203 171 LYS CB C 36.529 0.000 1 697 203 171 LYS N N 122.028 0.146 1 698 204 172 PRO C C 174.613 0.010 1 699 204 172 PRO CA C 62.518 0.006 1 700 204 172 PRO CB C 31.851 0.043 1 701 205 173 LEU H H 8.689 0.003 1 702 205 173 LEU C C 175.712 0.014 1 703 205 173 LEU CA C 53.445 0.030 1 704 205 173 LEU CB C 45.560 0.050 1 705 205 173 LEU N N 120.846 0.076 1 706 206 174 VAL H H 8.855 0.001 1 707 206 174 VAL C C 173.421 0.005 1 708 206 174 VAL CA C 61.176 0.050 1 709 206 174 VAL CB C 33.164 0.014 1 710 206 174 VAL N N 122.091 0.076 1 711 207 175 LEU H H 9.484 0.002 1 712 207 175 LEU C C 175.120 0.002 1 713 207 175 LEU CA C 52.000 0.020 1 714 207 175 LEU CB C 43.615 0.045 1 715 207 175 LEU N N 128.943 0.033 1 716 208 176 CYS H H 9.603 0.005 1 717 208 176 CYS C C 172.426 0.004 1 718 208 176 CYS CA C 53.034 0.029 1 719 208 176 CYS CB C 34.786 0.017 1 720 208 176 CYS N N 121.896 0.045 1 721 209 177 GLY H H 7.488 0.002 1 722 209 177 GLY C C 171.704 0.000 1 723 209 177 GLY CA C 43.805 0.000 1 724 209 177 GLY N N 106.771 0.045 1 725 210 178 ASP C C 175.858 0.000 1 726 210 178 ASP CA C 52.021 0.029 1 727 210 178 ASP CB C 39.443 0.006 1 728 211 179 LEU H H 8.726 0.002 1 729 211 179 LEU C C 176.991 0.025 1 730 211 179 LEU CA C 52.631 0.048 1 731 211 179 LEU CB C 37.177 0.023 1 732 211 179 LEU N N 122.627 0.057 1 733 212 180 ASN H H 9.105 0.007 1 734 212 180 ASN C C 172.471 0.007 1 735 212 180 ASN CA C 55.322 0.044 1 736 212 180 ASN CB C 38.224 0.028 1 737 212 180 ASN N N 117.391 0.140 1 738 213 181 VAL H H 6.690 0.002 1 739 213 181 VAL C C 171.820 0.001 1 740 213 181 VAL CA C 59.309 0.020 1 741 213 181 VAL CB C 32.994 0.013 1 742 213 181 VAL N N 108.421 0.050 1 743 214 182 ALA H H 8.934 0.001 1 744 214 182 ALA C C 174.675 0.003 1 745 214 182 ALA CA C 49.473 0.036 1 746 214 182 ALA CB C 19.702 0.036 1 747 214 182 ALA N N 133.117 0.100 1 748 215 183 HIS H H 6.841 0.001 1 749 215 183 HIS C C 175.294 0.011 1 750 215 183 HIS CA C 58.816 0.050 1 751 215 183 HIS CB C 30.871 0.027 1 752 215 183 HIS N N 120.308 0.036 1 753 216 184 GLU H H 9.813 0.002 1 754 216 184 GLU C C 177.406 0.018 1 755 216 184 GLU CA C 53.475 0.016 1 756 216 184 GLU CB C 37.802 9.042 1 757 216 184 GLU N N 117.144 0.050 1 758 217 185 GLU H H 8.995 0.001 1 759 217 185 GLU C C 177.555 0.022 1 760 217 185 GLU CA C 60.347 0.073 1 761 217 185 GLU CB C 27.943 0.026 1 762 217 185 GLU N N 120.292 0.044 1 763 218 186 ILE H H 7.628 0.002 1 764 218 186 ILE C C 177.033 0.011 1 765 218 186 ILE CA C 62.421 0.054 1 766 218 186 ILE CB C 38.260 0.006 1 767 218 186 ILE N N 112.326 0.072 1 768 219 187 ASP H H 8.330 0.003 1 769 219 187 ASP C C 171.438 0.003 1 770 219 187 ASP CA C 55.841 0.055 1 771 219 187 ASP CB C 41.794 0.078 1 772 219 187 ASP N N 122.857 0.060 1 773 220 188 LEU H H 7.572 0.001 1 774 220 188 LEU C C 173.235 0.002 1 775 220 188 LEU CA C 55.813 0.066 1 776 220 188 LEU CB C 40.709 0.013 1 777 220 188 LEU N N 119.829 0.035 1 778 221 189 ARG H H 6.998 0.002 1 779 221 189 ARG C C 176.616 0.102 1 780 221 189 ARG CA C 55.840 0.005 1 781 221 189 ARG CB C 29.474 0.000 1 782 221 189 ARG N N 118.813 0.053 1 783 222 190 ASN H H 8.218 0.002 1 784 222 190 ASN N N 110.239 0.049 1 785 223 191 PRO C C 179.243 0.000 1 786 223 191 PRO CA C 64.637 0.070 1 787 223 191 PRO CB C 31.174 0.000 1 788 224 192 LYS H H 8.008 0.002 1 789 224 192 LYS C C 179.270 0.019 1 790 224 192 LYS CA C 59.230 0.045 1 791 224 192 LYS CB C 30.907 0.016 1 792 224 192 LYS N N 115.566 0.039 1 793 225 193 GLY H H 7.389 0.004 1 794 225 193 GLY C C 175.186 0.011 1 795 225 193 GLY CA C 44.939 0.041 1 796 225 193 GLY N N 104.099 0.079 1 797 226 194 ASN H H 7.242 0.001 1 798 226 194 ASN C C 174.456 0.003 1 799 226 194 ASN CA C 53.965 0.033 1 800 226 194 ASN CB C 41.245 0.029 1 801 226 194 ASN N N 118.051 0.027 1 802 227 195 LYS H H 7.426 0.003 1 803 227 195 LYS C C 176.007 0.002 1 804 227 195 LYS CA C 58.959 0.040 1 805 227 195 LYS CB C 31.783 0.094 1 806 227 195 LYS N N 118.601 0.042 1 807 228 196 LYS H H 8.029 0.005 1 808 228 196 LYS C C 174.198 0.014 1 809 228 196 LYS CA C 54.023 0.047 1 810 228 196 LYS CB C 31.390 0.022 1 811 228 196 LYS N N 116.113 0.048 1 812 229 197 ASN H H 7.584 0.003 1 813 229 197 ASN C C 173.292 0.011 1 814 229 197 ASN CA C 50.789 0.029 1 815 229 197 ASN CB C 41.155 0.054 1 816 229 197 ASN N N 117.889 0.084 1 817 230 198 ALA H H 8.293 0.008 1 818 230 198 ALA C C 176.719 0.038 1 819 230 198 ALA CA C 53.242 0.066 1 820 230 198 ALA CB C 17.746 0.027 1 821 230 198 ALA N N 122.308 0.059 1 822 231 199 GLY H H 6.230 0.002 1 823 231 199 GLY C C 174.964 0.006 1 824 231 199 GLY CA C 44.606 0.069 1 825 231 199 GLY N N 118.300 0.056 1 826 232 200 PHE H H 8.758 0.001 1 827 232 200 PHE C C 175.443 0.050 1 828 232 200 PHE CA C 56.889 0.091 1 829 232 200 PHE CB C 40.018 0.047 1 830 232 200 PHE N N 121.812 0.037 1 831 233 201 THR H H 7.505 0.005 1 832 233 201 THR C C 174.719 0.000 1 833 233 201 THR CA C 60.465 0.016 1 834 233 201 THR CB C 68.767 0.000 1 835 233 201 THR N N 110.500 0.034 1 836 234 202 PRO C C 179.827 0.000 1 837 234 202 PRO CA C 64.716 0.038 1 838 234 202 PRO CB C 30.686 0.026 1 839 235 203 GLN H H 8.860 0.002 1 840 235 203 GLN C C 180.581 0.009 1 841 235 203 GLN CA C 60.189 0.048 1 842 235 203 GLN CB C 26.698 0.089 1 843 235 203 GLN N N 115.962 0.046 1 844 236 204 GLU H H 8.267 0.004 1 845 236 204 GLU C C 180.565 0.002 1 846 236 204 GLU CA C 59.370 0.062 1 847 236 204 GLU CB C 31.204 0.157 1 848 236 204 GLU N N 122.009 0.089 1 849 237 205 ARG H H 8.487 0.006 1 850 237 205 ARG C C 179.465 0.009 1 851 237 205 ARG CA C 60.408 0.042 1 852 237 205 ARG CB C 30.813 0.017 1 853 237 205 ARG N N 122.055 0.104 1 854 238 206 GLN H H 8.741 0.002 1 855 238 206 GLN C C 179.489 0.021 1 856 238 206 GLN CA C 58.302 0.023 1 857 238 206 GLN CB C 27.037 0.025 1 858 238 206 GLN N N 121.021 0.067 1 859 239 207 GLY H H 7.951 0.003 1 860 239 207 GLY C C 176.354 0.007 1 861 239 207 GLY CA C 46.523 0.024 1 862 239 207 GLY N N 107.023 0.045 1 863 240 208 PHE H H 7.897 0.001 1 864 240 208 PHE C C 177.037 0.006 1 865 240 208 PHE CA C 61.117 0.052 1 866 240 208 PHE CB C 38.711 0.025 1 867 240 208 PHE N N 126.121 0.034 1 868 241 209 GLY H H 8.204 0.003 1 869 241 209 GLY C C 177.245 0.015 1 870 241 209 GLY CA C 47.198 0.042 1 871 241 209 GLY N N 105.423 0.041 1 872 242 210 GLU H H 8.239 0.003 1 873 242 210 GLU C C 178.404 0.058 1 874 242 210 GLU CA C 58.575 0.063 1 875 242 210 GLU CB C 28.442 0.047 1 876 242 210 GLU N N 121.117 0.028 1 877 243 211 LEU H H 7.606 0.003 1 878 243 211 LEU C C 177.430 0.016 1 879 243 211 LEU CA C 58.630 0.076 1 880 243 211 LEU CB C 39.607 0.045 1 881 243 211 LEU N N 123.281 0.042 1 882 244 212 LEU H H 7.444 0.002 1 883 244 212 LEU C C 180.524 0.004 1 884 244 212 LEU CA C 57.047 0.059 1 885 244 212 LEU CB C 39.566 0.013 1 886 244 212 LEU N N 113.807 0.063 1 887 245 213 GLN H H 7.602 0.008 1 888 245 213 GLN C C 177.811 0.006 1 889 245 213 GLN CA C 57.290 0.060 1 890 245 213 GLN CB C 28.802 0.033 1 891 245 213 GLN N N 114.729 0.052 1 892 246 214 ALA H H 8.512 0.003 1 893 246 214 ALA C C 179.139 0.009 1 894 246 214 ALA CA C 53.800 0.056 1 895 246 214 ALA CB C 19.273 0.051 1 896 246 214 ALA N N 119.224 0.061 1 897 247 215 VAL H H 6.803 0.003 1 898 247 215 VAL C C 173.548 0.000 1 899 247 215 VAL CA C 68.847 0.000 1 900 247 215 VAL CB C 29.839 0.000 1 901 247 215 VAL N N 114.371 0.066 1 902 248 216 PRO C C 176.342 0.008 1 903 248 216 PRO CA C 61.181 0.034 1 904 248 216 PRO CB C 34.370 0.008 1 905 249 217 LEU H H 9.229 0.002 1 906 249 217 LEU C C 174.429 0.029 1 907 249 217 LEU CA C 52.895 0.076 1 908 249 217 LEU CB C 48.039 0.035 1 909 249 217 LEU N N 117.817 0.108 1 910 250 218 ALA H H 9.036 0.002 1 911 250 218 ALA C C 177.045 0.016 1 912 250 218 ALA CA C 49.405 0.050 1 913 250 218 ALA CB C 21.014 0.068 1 914 250 218 ALA N N 120.264 0.059 1 915 251 219 ASP H H 9.165 0.001 1 916 251 219 ASP C C 176.918 0.066 1 917 251 219 ASP CA C 52.764 0.082 1 918 251 219 ASP CB C 40.094 0.036 1 919 251 219 ASP N N 121.803 0.076 1 920 252 220 SER H H 8.601 0.005 1 921 252 220 SER C C 173.967 0.000 1 922 252 220 SER CA C 62.240 0.046 1 923 252 220 SER CB C 63.570 0.089 1 924 252 220 SER N N 123.132 0.045 1 925 253 221 PHE H H 8.023 0.003 1 926 253 221 PHE C C 176.616 0.005 1 927 253 221 PHE CA C 62.616 0.069 1 928 253 221 PHE CB C 39.904 0.019 1 929 253 221 PHE N N 122.298 0.089 1 930 254 222 ARG H H 7.010 0.001 1 931 254 222 ARG C C 177.270 0.006 1 932 254 222 ARG CA C 54.065 0.036 1 933 254 222 ARG CB C 28.046 0.075 1 934 254 222 ARG N N 116.604 0.050 1 935 255 223 HIS H H 8.558 0.002 1 936 255 223 HIS C C 176.886 0.018 1 937 255 223 HIS CA C 59.306 0.014 1 938 255 223 HIS CB C 30.030 0.009 1 939 255 223 HIS N N 118.782 0.049 1 940 256 224 LEU H H 6.661 0.001 1 941 256 224 LEU C C 177.015 0.015 1 942 256 224 LEU CA C 55.452 0.074 1 943 256 224 LEU CB C 42.534 0.027 1 944 256 224 LEU N N 115.895 0.041 1 945 257 225 TYR H H 7.960 0.002 1 946 257 225 TYR C C 174.325 0.000 1 947 257 225 TYR CA C 54.201 0.026 1 948 257 225 TYR CB C 34.958 0.000 1 949 257 225 TYR N N 118.035 0.028 1 950 258 226 PRO C C 177.441 0.000 1 951 258 226 PRO CA C 64.740 0.067 1 952 258 226 PRO CB C 31.428 0.052 1 953 259 227 ASN H H 8.417 0.002 1 954 259 227 ASN C C 175.353 0.029 1 955 259 227 ASN CA C 51.534 0.070 1 956 259 227 ASN CB C 39.450 0.015 1 957 259 227 ASN N N 112.775 0.046 1 958 260 228 THR H H 6.665 0.001 1 959 260 228 THR C C 171.457 0.000 1 960 260 228 THR CA C 61.588 0.042 1 961 260 228 THR CB C 70.220 0.000 1 962 260 228 THR N N 118.838 0.042 1 963 261 229 PRO C C 175.202 0.000 1 964 261 229 PRO CA C 60.805 0.034 1 965 261 229 PRO CB C 31.187 0.026 1 966 262 230 TYR H H 8.335 0.002 1 967 262 230 TYR C C 171.549 0.000 1 968 262 230 TYR CA C 55.903 0.035 1 969 262 230 TYR CB C 34.084 0.012 1 970 262 230 TYR N N 108.785 0.057 1 971 263 231 ALA H H 7.055 0.001 1 972 263 231 ALA C C 173.079 0.001 1 973 263 231 ALA CA C 50.203 0.026 1 974 263 231 ALA CB C 17.726 0.015 1 975 263 231 ALA N N 123.709 0.019 1 976 264 232 TYR H H 6.785 0.001 1 977 264 232 TYR C C 172.013 0.030 1 978 264 232 TYR CA C 52.732 0.068 1 979 264 232 TYR CB C 39.931 0.062 1 980 264 232 TYR N N 122.198 0.054 1 981 265 233 THR H H 7.899 0.002 1 982 265 233 THR C C 171.874 0.086 1 983 265 233 THR CA C 60.479 0.045 1 984 265 233 THR CB C 68.772 0.043 1 985 265 233 THR N N 106.582 0.055 1 986 266 234 PHE H H 7.050 0.007 1 987 266 234 PHE C C 171.736 0.000 1 988 266 234 PHE CA C 55.478 0.039 1 989 266 234 PHE CB C 41.520 0.069 1 990 266 234 PHE N N 121.041 0.116 1 991 267 235 TRP H H 7.517 0.005 1 992 267 235 TRP C C 174.434 0.000 1 993 267 235 TRP CA C 55.284 0.015 1 994 267 235 TRP CB C 31.168 0.000 1 995 267 235 TRP N N 127.249 0.027 1 996 268 236 THR C C 176.013 0.000 1 997 268 236 THR CA C 60.734 0.058 1 998 268 236 THR CB C 68.309 0.009 1 999 269 237 TYR H H 8.834 0.003 1 1000 269 237 TYR C C 178.864 0.001 1 1001 269 237 TYR CA C 59.762 0.086 1 1002 269 237 TYR CB C 37.655 0.069 1 1003 269 237 TYR N N 122.962 0.101 1 1004 270 238 MET H H 8.008 0.007 1 1005 270 238 MET C C 176.007 0.002 1 1006 270 238 MET CA C 55.976 0.032 1 1007 270 238 MET CB C 32.215 0.030 1 1008 270 238 MET N N 116.772 0.092 1 1009 271 239 MET H H 8.852 0.001 1 1010 271 239 MET C C 175.995 0.003 1 1011 271 239 MET CA C 55.881 0.044 1 1012 271 239 MET CB C 29.083 0.034 1 1013 271 239 MET N N 115.465 0.060 1 1014 272 240 ASN H H 8.796 0.002 1 1015 272 240 ASN C C 176.001 0.002 1 1016 272 240 ASN CA C 53.539 0.026 1 1017 272 240 ASN CB C 36.746 0.032 1 1018 272 240 ASN N N 115.700 0.045 1 1019 273 241 ALA H H 7.024 0.001 1 1020 273 241 ALA C C 180.085 0.046 1 1021 273 241 ALA CA C 56.040 0.033 1 1022 273 241 ALA CB C 17.859 0.009 1 1023 273 241 ALA N N 120.456 0.072 1 1024 274 242 ARG H H 9.062 0.003 1 1025 274 242 ARG C C 179.998 0.030 1 1026 274 242 ARG CA C 59.591 0.028 1 1027 274 242 ARG CB C 28.431 0.020 1 1028 274 242 ARG N N 120.300 0.033 1 1029 275 243 SER H H 7.880 0.003 1 1030 275 243 SER C C 175.963 0.000 1 1031 275 243 SER CA C 60.593 0.088 1 1032 275 243 SER CB C 62.091 0.041 1 1033 275 243 SER N N 115.680 0.063 1 1034 276 244 LYS H H 7.113 0.001 1 1035 276 244 LYS C C 175.415 0.004 1 1036 276 244 LYS CA C 55.470 0.031 1 1037 276 244 LYS CB C 32.385 0.043 1 1038 276 244 LYS N N 118.699 0.033 1 1039 277 245 ASN H H 8.006 0.002 1 1040 277 245 ASN C C 174.927 0.004 1 1041 277 245 ASN CA C 53.420 0.039 1 1042 277 245 ASN CB C 37.118 0.032 1 1043 277 245 ASN N N 119.058 0.034 1 1044 278 246 VAL H H 8.669 0.004 1 1045 278 246 VAL C C 174.136 0.000 1 1046 278 246 VAL CA C 61.328 0.013 1 1047 278 246 VAL CB C 29.036 0.000 1 1048 278 246 VAL N N 121.943 0.049 1 1049 279 247 GLY C C 170.841 0.000 1 1050 279 247 GLY CA C 44.708 0.046 1 1051 280 248 TRP H H 8.743 0.001 1 1052 280 248 TRP C C 175.865 0.017 1 1053 280 248 TRP CA C 54.798 0.045 1 1054 280 248 TRP CB C 32.368 0.023 1 1055 280 248 TRP N N 116.094 0.040 1 1056 281 249 ARG H H 10.226 0.008 1 1057 281 249 ARG C C 171.127 0.014 1 1058 281 249 ARG CA C 56.751 0.032 1 1059 281 249 ARG CB C 28.703 0.053 1 1060 281 249 ARG N N 129.662 0.147 1 1061 282 250 LEU H H 6.591 0.003 1 1062 282 250 LEU C C 173.812 0.015 1 1063 282 250 LEU CA C 53.920 0.066 1 1064 282 250 LEU CB C 43.890 0.055 1 1065 282 250 LEU N N 120.641 0.058 1 1066 283 251 ASP H H 6.950 0.001 1 1067 283 251 ASP C C 174.458 0.011 1 1068 283 251 ASP CA C 52.462 0.083 1 1069 283 251 ASP CB C 41.876 0.035 1 1070 283 251 ASP N N 117.902 0.052 1 1071 284 252 TYR H H 8.044 0.004 1 1072 284 252 TYR C C 175.618 0.017 1 1073 284 252 TYR CA C 56.881 0.069 1 1074 284 252 TYR CB C 43.730 0.027 1 1075 284 252 TYR N N 118.648 0.048 1 1076 285 253 PHE H H 8.754 0.002 1 1077 285 253 PHE C C 176.310 0.004 1 1078 285 253 PHE CA C 58.548 0.043 1 1079 285 253 PHE CB C 41.867 0.022 1 1080 285 253 PHE N N 114.480 0.035 1 1081 286 254 LEU H H 10.245 0.005 1 1082 286 254 LEU C C 175.193 0.017 1 1083 286 254 LEU CA C 52.096 0.067 1 1084 286 254 LEU CB C 42.774 0.059 1 1085 286 254 LEU N N 126.805 0.047 1 1086 287 255 LEU H H 9.068 0.003 1 1087 287 255 LEU C C 177.569 0.016 1 1088 287 255 LEU CA C 52.748 0.052 1 1089 287 255 LEU CB C 45.244 0.012 1 1090 287 255 LEU N N 121.392 0.051 1 1091 288 256 SER H H 8.954 0.003 1 1092 288 256 SER C C 175.311 0.006 1 1093 288 256 SER CA C 60.809 0.029 1 1094 288 256 SER CB C 63.357 0.034 1 1095 288 256 SER N N 119.441 0.088 1 1096 289 257 HIS H H 8.589 0.006 1 1097 289 257 HIS C C 179.253 0.006 1 1098 289 257 HIS CA C 58.973 0.041 1 1099 289 257 HIS CB C 29.617 0.057 1 1100 289 257 HIS N N 123.768 0.062 1 1101 290 258 SER H H 8.428 0.010 1 1102 290 258 SER C C 175.450 0.000 1 1103 290 258 SER CA C 59.446 0.085 1 1104 290 258 SER CB C 61.704 0.028 1 1105 290 258 SER N N 114.806 0.043 1 1106 291 259 LEU H H 7.619 0.002 1 1107 291 259 LEU C C 177.692 0.031 1 1108 291 259 LEU CA C 53.792 0.062 1 1109 291 259 LEU CB C 42.507 0.026 1 1110 291 259 LEU N N 120.167 0.120 1 1111 292 260 LEU H H 7.540 0.002 1 1112 292 260 LEU C C 177.736 0.000 1 1113 292 260 LEU CA C 58.977 0.034 1 1114 292 260 LEU CB C 37.469 0.000 1 1115 292 260 LEU N N 121.437 0.047 1 1116 293 261 PRO C C 176.195 0.023 1 1117 293 261 PRO CA C 64.818 0.032 1 1118 293 261 PRO CB C 30.137 0.042 1 1119 294 262 ALA H H 7.376 0.002 1 1120 294 262 ALA C C 176.882 0.008 1 1121 294 262 ALA CA C 50.768 0.021 1 1122 294 262 ALA CB C 19.082 0.025 1 1123 294 262 ALA N N 117.027 0.051 1 1124 295 263 LEU H H 7.681 0.002 1 1125 295 263 LEU C C 174.904 0.002 1 1126 295 263 LEU CA C 55.801 0.039 1 1127 295 263 LEU CB C 40.513 0.078 1 1128 295 263 LEU N N 123.057 0.037 1 1129 296 264 CYS H H 8.182 0.001 1 1130 296 264 CYS C C 173.160 0.003 1 1131 296 264 CYS CA C 59.166 0.056 1 1132 296 264 CYS CB C 27.738 0.075 1 1133 296 264 CYS N N 124.880 0.039 1 1134 297 265 ASP H H 7.370 0.001 1 1135 297 265 ASP C C 174.538 0.019 1 1136 297 265 ASP CA C 52.487 0.070 1 1137 297 265 ASP CB C 45.312 0.016 1 1138 297 265 ASP N N 111.142 0.097 1 1139 298 266 SER H H 9.229 0.003 1 1140 298 266 SER C C 172.981 0.013 1 1141 298 266 SER CA C 56.358 0.038 1 1142 298 266 SER CB C 65.230 0.009 1 1143 298 266 SER N N 117.361 0.107 1 1144 299 267 LYS H H 10.539 0.002 1 1145 299 267 LYS C C 177.490 0.000 1 1146 299 267 LYS CA C 52.359 0.019 1 1147 299 267 LYS CB C 29.604 0.012 1 1148 299 267 LYS N N 124.119 0.035 1 1149 300 268 ILE H H 9.067 0.002 1 1150 300 268 ILE C C 174.992 0.016 1 1151 300 268 ILE CA C 61.864 0.064 1 1152 300 268 ILE CB C 38.950 0.010 1 1153 300 268 ILE N N 125.144 0.020 1 1154 301 269 ARG H H 7.995 0.003 1 1155 301 269 ARG C C 178.123 0.032 1 1156 301 269 ARG CA C 51.751 0.059 1 1157 301 269 ARG CB C 26.031 0.025 1 1158 301 269 ARG N N 124.553 0.127 1 1159 302 270 SER H H 8.131 0.002 1 1160 302 270 SER C C 175.954 0.017 1 1161 302 270 SER CA C 61.130 0.061 1 1162 302 270 SER CB C 63.434 0.004 1 1163 302 270 SER N N 113.562 0.024 1 1164 303 271 LYS H H 8.762 0.003 1 1165 303 271 LYS C C 176.755 0.034 1 1166 303 271 LYS CA C 55.352 0.032 1 1167 303 271 LYS CB C 31.286 0.062 1 1168 303 271 LYS N N 118.689 0.065 1 1169 304 272 ALA H H 7.173 0.007 1 1170 304 272 ALA C C 177.854 0.001 1 1171 304 272 ALA CA C 52.205 0.075 1 1172 304 272 ALA CB C 16.427 0.019 1 1173 304 272 ALA N N 123.365 0.051 1 1174 305 273 LEU H H 8.561 0.001 1 1175 305 273 LEU C C 176.270 0.004 1 1176 305 273 LEU CA C 54.390 0.085 1 1177 305 273 LEU CB C 41.677 0.049 1 1178 305 273 LEU N N 128.895 0.042 1 1179 306 274 GLY H H 8.628 0.002 1 1180 306 274 GLY C C 171.877 0.001 1 1181 306 274 GLY CA C 45.303 0.033 1 1182 306 274 GLY N N 104.777 0.039 1 1183 307 275 SER H H 8.617 0.008 1 1184 307 275 SER C C 173.563 0.011 1 1185 307 275 SER CA C 54.878 0.043 1 1186 307 275 SER CB C 63.267 0.062 1 1187 307 275 SER N N 115.674 0.040 1 1188 308 276 ASP H H 9.053 0.005 1 1189 308 276 ASP C C 175.822 0.003 1 1190 308 276 ASP CA C 54.539 0.068 1 1191 308 276 ASP CB C 36.581 0.056 1 1192 308 276 ASP N N 122.371 0.069 1 1193 309 277 HIS H H 8.665 0.001 1 1194 309 277 HIS C C 178.012 0.005 1 1195 309 277 HIS CA C 53.367 0.087 1 1196 309 277 HIS CB C 32.358 0.025 1 1197 309 277 HIS N N 115.356 0.065 1 1198 310 278 CYS H H 9.470 0.004 1 1199 310 278 CYS C C 169.013 0.000 1 1200 310 278 CYS CA C 53.602 0.046 1 1201 310 278 CYS CB C 27.742 0.000 1 1202 310 278 CYS N N 123.340 0.038 1 1203 311 279 PRO C C 175.984 0.008 1 1204 311 279 PRO CA C 61.463 0.046 1 1205 311 279 PRO CB C 30.509 0.036 1 1206 312 280 ILE H H 8.616 0.003 1 1207 312 280 ILE C C 175.419 0.013 1 1208 312 280 ILE CA C 59.255 0.017 1 1209 312 280 ILE CB C 40.413 0.058 1 1210 312 280 ILE N N 113.141 0.062 1 1211 313 281 THR H H 7.896 0.001 1 1212 313 281 THR C C 170.479 0.001 1 1213 313 281 THR CA C 61.136 0.045 1 1214 313 281 THR CB C 72.402 0.021 1 1215 313 281 THR N N 118.119 0.039 1 1216 314 282 LEU H H 9.476 0.002 1 1217 314 282 LEU C C 174.837 0.023 1 1218 314 282 LEU CA C 52.156 0.068 1 1219 314 282 LEU CB C 43.453 0.083 1 1220 314 282 LEU N N 131.604 0.052 1 1221 315 283 TYR H H 8.227 0.003 1 1222 315 283 TYR C C 174.895 0.051 1 1223 315 283 TYR CA C 56.483 0.058 1 1224 315 283 TYR CB C 41.329 0.003 1 1225 315 283 TYR N N 121.892 0.101 1 1226 316 284 LEU H H 9.017 0.006 1 1227 316 284 LEU C C 175.304 0.017 1 1228 316 284 LEU CA C 52.278 0.079 1 1229 316 284 LEU CB C 45.930 0.029 1 1230 316 284 LEU N N 122.186 0.050 1 1231 317 285 ALA H H 9.789 0.002 1 1232 317 285 ALA C C 173.756 0.011 1 1233 317 285 ALA CA C 50.892 0.029 1 1234 317 285 ALA CB C 18.708 0.054 1 1235 317 285 ALA N N 129.492 0.021 1 1236 318 286 LEU H H 6.998 0.001 1 1237 318 286 LEU C C 182.456 0.000 1 1238 318 286 LEU CA C 55.305 0.009 1 1239 318 286 LEU CB C 43.336 0.000 1 1240 318 286 LEU N N 127.269 0.032 1 stop_ save_