data_27274 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Backbone 1H, 13C, and 15N Chemical Shift Assignments of phosphorylated (T183 and Y185) p38 alpha in complex with an MKK3bKIM peptide ; _BMRB_accession_number 27274 _BMRB_flat_file_name bmr27274.str _Entry_type original _Submission_date 2017-10-04 _Accession_date 2017-10-04 _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 Ganesan 'Senthil Kumar' . . 2 Page Rebecca . . 3 Peti Wolfgang . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 265 "13C chemical shifts" 532 "15N chemical shifts" 265 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2018-05-22 original BMRB . stop_ loop_ _Related_BMRB_accession_number _Relationship 17471 'Backbone 1H, 13C, and 15N Chemical Shift Assignments for non-phosphorylated p38 alpha MAPK' 19934 'Dual-phospholyrated apo Human p38 alpha ILVM methyl resonance assignments' 27273 'phosphorylated (T183 and Y185) p38 alpha' stop_ _Original_release_date 2017-10-04 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; Dynamic activation and regulation of the mitogen-activated protein kinase p38 ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 29666261 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Kumar 'Ganesan Senthil' S. . 2 Clarkson Michael W. . 3 Kunze Micha . . 4 Granata Daniele . . 5 Wand 'A Joshua' J. . 6 Lindorff-Larsen Kresten . . 7 Page Rebecca . . 8 Peti Wolfgang . . stop_ _Journal_abbreviation 'Proc. Natl. Acad. Sci. U.S.A.' _Journal_name_full 'Proceedings of the National Academy of Sciences of the United States of America' _Journal_volume 115 _Journal_issue 18 _Journal_ISSN 1091-6490 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 4655 _Page_last 4660 _Year 2018 _Details . loop_ _Keyword MAPK p38 stop_ save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name 'dp-p38a MKK3bKIM Complex' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'dp-p38 alpha' $dp-p38_alpha 'MKK3b KIM' $MKK3b_KIM_peptide stop_ _System_molecular_weight 42470 _System_physical_state native _System_oligomer_state ? _System_paramagnetic no _System_thiol_state . loop_ _Biological_function kinase stop_ _Database_query_date . _Details 'doubly phosphorylated (T183 and Y185)MAPK p38 alpha in complex with MKK3bKIM peptide' save_ ######################## # Monomeric polymers # ######################## save_dp-p38_alpha _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common dp-p38_alpha _Molecular_mass 40450 _Mol_thiol_state 'all free' loop_ _Biological_function Kinase stop_ _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 352 _Mol_residue_sequence ; GHMGSQERPTFYRQELNKTI WEVPERYQNLSPVGSGAYGS VCAAFDTKTGLRVAVKKLSR PFQSIIHAKRTYRELRLLKH MKHENVIGLLDVFTPARSLE EFNDVYLVTHLMGADLNNIV KCQKLTDDHVQFLIYQILRG LKYIHSADIIHRDLKPSNLA VNEDCELKILDFGLARHTDD EMXGXVATRWYRAPEIMLNW MHYNQTVDIWSVGCIMAELL TGRTLFPGTDHIDQLKLILR LVGTPGAELLKKISSESARN YIQSLTQMPKMNFANVFIGA NPLAVDLLEKMLVLDSDKRI TAAQALAHAYFAQYHDPDDE PVADPYDQSFESRDLLIDEW KSLTYDEVISFV ; loop_ _Residue_seq_code _Residue_label 1 GLY 2 HIS 3 MET 4 GLY 5 SER 6 GLN 7 GLU 8 ARG 9 PRO 10 THR 11 PHE 12 TYR 13 ARG 14 GLN 15 GLU 16 LEU 17 ASN 18 LYS 19 THR 20 ILE 21 TRP 22 GLU 23 VAL 24 PRO 25 GLU 26 ARG 27 TYR 28 GLN 29 ASN 30 LEU 31 SER 32 PRO 33 VAL 34 GLY 35 SER 36 GLY 37 ALA 38 TYR 39 GLY 40 SER 41 VAL 42 CYS 43 ALA 44 ALA 45 PHE 46 ASP 47 THR 48 LYS 49 THR 50 GLY 51 LEU 52 ARG 53 VAL 54 ALA 55 VAL 56 LYS 57 LYS 58 LEU 59 SER 60 ARG 61 PRO 62 PHE 63 GLN 64 SER 65 ILE 66 ILE 67 HIS 68 ALA 69 LYS 70 ARG 71 THR 72 TYR 73 ARG 74 GLU 75 LEU 76 ARG 77 LEU 78 LEU 79 LYS 80 HIS 81 MET 82 LYS 83 HIS 84 GLU 85 ASN 86 VAL 87 ILE 88 GLY 89 LEU 90 LEU 91 ASP 92 VAL 93 PHE 94 THR 95 PRO 96 ALA 97 ARG 98 SER 99 LEU 100 GLU 101 GLU 102 PHE 103 ASN 104 ASP 105 VAL 106 TYR 107 LEU 108 VAL 109 THR 110 HIS 111 LEU 112 MET 113 GLY 114 ALA 115 ASP 116 LEU 117 ASN 118 ASN 119 ILE 120 VAL 121 LYS 122 CYS 123 GLN 124 LYS 125 LEU 126 THR 127 ASP 128 ASP 129 HIS 130 VAL 131 GLN 132 PHE 133 LEU 134 ILE 135 TYR 136 GLN 137 ILE 138 LEU 139 ARG 140 GLY 141 LEU 142 LYS 143 TYR 144 ILE 145 HIS 146 SER 147 ALA 148 ASP 149 ILE 150 ILE 151 HIS 152 ARG 153 ASP 154 LEU 155 LYS 156 PRO 157 SER 158 ASN 159 LEU 160 ALA 161 VAL 162 ASN 163 GLU 164 ASP 165 CYS 166 GLU 167 LEU 168 LYS 169 ILE 170 LEU 171 ASP 172 PHE 173 GLY 174 LEU 175 ALA 176 ARG 177 HIS 178 THR 179 ASP 180 ASP 181 GLU 182 MET 183 TPO 184 GLY 185 PTR 186 VAL 187 ALA 188 THR 189 ARG 190 TRP 191 TYR 192 ARG 193 ALA 194 PRO 195 GLU 196 ILE 197 MET 198 LEU 199 ASN 200 TRP 201 MET 202 HIS 203 TYR 204 ASN 205 GLN 206 THR 207 VAL 208 ASP 209 ILE 210 TRP 211 SER 212 VAL 213 GLY 214 CYS 215 ILE 216 MET 217 ALA 218 GLU 219 LEU 220 LEU 221 THR 222 GLY 223 ARG 224 THR 225 LEU 226 PHE 227 PRO 228 GLY 229 THR 230 ASP 231 HIS 232 ILE 233 ASP 234 GLN 235 LEU 236 LYS 237 LEU 238 ILE 239 LEU 240 ARG 241 LEU 242 VAL 243 GLY 244 THR 245 PRO 246 GLY 247 ALA 248 GLU 249 LEU 250 LEU 251 LYS 252 LYS 253 ILE 254 SER 255 SER 256 GLU 257 SER 258 ALA 259 ARG 260 ASN 261 TYR 262 ILE 263 GLN 264 SER 265 LEU 266 THR 267 GLN 268 MET 269 PRO 270 LYS 271 MET 272 ASN 273 PHE 274 ALA 275 ASN 276 VAL 277 PHE 278 ILE 279 GLY 280 ALA 281 ASN 282 PRO 283 LEU 284 ALA 285 VAL 286 ASP 287 LEU 288 LEU 289 GLU 290 LYS 291 MET 292 LEU 293 VAL 294 LEU 295 ASP 296 SER 297 ASP 298 LYS 299 ARG 300 ILE 301 THR 302 ALA 303 ALA 304 GLN 305 ALA 306 LEU 307 ALA 308 HIS 309 ALA 310 TYR 311 PHE 312 ALA 313 GLN 314 TYR 315 HIS 316 ASP 317 PRO 318 ASP 319 ASP 320 GLU 321 PRO 322 VAL 323 ALA 324 ASP 325 PRO 326 TYR 327 ASP 328 GLN 329 SER 330 PHE 331 GLU 332 SER 333 ARG 334 ASP 335 LEU 336 LEU 337 ILE 338 ASP 339 GLU 340 TRP 341 LYS 342 SER 343 LEU 344 THR 345 TYR 346 ASP 347 GLU 348 VAL 349 ILE 350 SER 351 PHE 352 VAL 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 BMRB 17471 'p38 alpha' . . . . . PDB 3PY3 'phosphorylated p38 alpha' . . . . . PDB 3P4K 'Phosphorylated p38 alpha bound to MKK3b' . . . . . stop_ save_ save_MKK3b_KIM_peptide _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common MKK3b_KIM_peptide _Molecular_mass 2020.42 _Mol_thiol_state 'all free' loop_ _Biological_function Kinase stop_ _Details . _Residue_count 18 _Mol_residue_sequence ; SKGKSKRKKDLRISCASK ; loop_ _Residue_seq_code _Residue_label 1 SER 2 LYS 3 GLY 4 LYS 5 SER 6 LYS 7 ARG 8 LYS 9 LYS 10 ASP 11 LEU 12 ARG 13 ILE 14 SER 15 CYS 16 ALA 17 SER 18 LYS stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date . save_ ###################### # Polymer residues # ###################### save_chem_comp_TPO _Saveframe_category polymer_residue _Mol_type 'L-PEPTIDE LINKING' _Name_common PHOSPHOTHREONINE _BMRB_code TPO _PDB_code TPO _Standard_residue_derivative . _Molecular_mass 199.099 _Mol_paramagnetic . _Details . loop_ _Atom_name _PDB_atom_name _Atom_type _Atom_chirality _Atom_charge _Atom_oxidation_number _Atom_unpaired_electrons N N N . 0 . ? CA CA C . 0 . ? CB CB C . 0 . ? CG2 CG2 C . 0 . ? OG1 OG1 O . 0 . ? P P P . 0 . ? O1P O1P O . 0 . ? O2P O2P O . 0 . ? O3P O3P O . 0 . ? C C C . 0 . ? O O O . 0 . ? OXT OXT O . 0 . ? H H H . 0 . ? H2 H2 H . 0 . ? HA HA H . 0 . ? HB HB H . 0 . ? HG21 HG21 H . 0 . ? HG22 HG22 H . 0 . ? HG23 HG23 H . 0 . ? HOP2 HOP2 H . 0 . ? HOP3 HOP3 H . 0 . ? HXT HXT H . 0 . ? stop_ loop_ _Bond_order _Bond_atom_one_atom_name _Bond_atom_two_atom_name _PDB_bond_atom_one_atom_name _PDB_bond_atom_two_atom_name SING N CA ? ? SING N H ? ? SING N H2 ? ? SING CA CB ? ? SING CA C ? ? SING CA HA ? ? SING CB CG2 ? ? SING CB OG1 ? ? SING CB HB ? ? SING CG2 HG21 ? ? SING CG2 HG22 ? ? SING CG2 HG23 ? ? SING OG1 P ? ? DOUB P O1P ? ? SING P O2P ? ? SING P O3P ? ? SING O2P HOP2 ? ? SING O3P HOP3 ? ? DOUB C O ? ? SING C OXT ? ? SING OXT HXT ? ? stop_ save_ save_chem_comp_PTR _Saveframe_category polymer_residue _Mol_type 'L-PEPTIDE LINKING' _Name_common O-PHOSPHOTYROSINE _BMRB_code PTR _PDB_code PTR _Standard_residue_derivative . _Molecular_mass 261.168 _Mol_paramagnetic . _Details . loop_ _Atom_name _PDB_atom_name _Atom_type _Atom_chirality _Atom_charge _Atom_oxidation_number _Atom_unpaired_electrons N N N . 0 . ? CA CA C . 0 . ? C C C . 0 . ? O O O . 0 . ? OXT OXT O . 0 . ? CB CB C . 0 . ? CG CG C . 0 . ? CD1 CD1 C . 0 . ? CD2 CD2 C . 0 . ? CE1 CE1 C . 0 . ? CE2 CE2 C . 0 . ? CZ CZ C . 0 . ? OH OH O . 0 . ? P P P . 0 . ? O1P O1P O . 0 . ? O2P O2P O . 0 . ? O3P O3P O . 0 . ? H H H . 0 . ? HN2 HN2 H . 0 . ? HA HA H . 0 . ? HXT HXT H . 0 . ? HB2 HB2 H . 0 . ? HB3 HB3 H . 0 . ? HD1 HD1 H . 0 . ? HD2 HD2 H . 0 . ? HE1 HE1 H . 0 . ? HE2 HE2 H . 0 . ? HO2P HO2P H . 0 . ? HO3P HO3P H . 0 . ? stop_ loop_ _Bond_order _Bond_atom_one_atom_name _Bond_atom_two_atom_name _PDB_bond_atom_one_atom_name _PDB_bond_atom_two_atom_name SING N CA ? ? SING N H ? ? SING N HN2 ? ? SING CA C ? ? SING CA CB ? ? SING CA HA ? ? DOUB C O ? ? SING C OXT ? ? SING OXT HXT ? ? SING CB CG ? ? SING CB HB2 ? ? SING CB HB3 ? ? DOUB CG CD1 ? ? SING CG CD2 ? ? SING CD1 CE1 ? ? SING CD1 HD1 ? ? DOUB CD2 CE2 ? ? SING CD2 HD2 ? ? DOUB CE1 CZ ? ? SING CE1 HE1 ? ? SING CE2 CZ ? ? SING CE2 HE2 ? ? SING CZ OH ? ? SING OH P ? ? DOUB P O1P ? ? SING P O2P ? ? SING P O3P ? ? SING O2P HO2P ? ? SING O3P HO3P ? ? stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $dp-p38_alpha 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 $dp-p38_alpha 'recombinant technology' . Escherichia coli . RP1B stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $dp-p38_alpha 0.35 mM '[U-2H; U-13C; U-15N]' $MKK3b_KIM_peptide 0.35 mM '[U-2H; U-13C; U-15N]' HEPES 10 mM 'natural abundance' 'Sodium Chloride' 150 mM 'natural abundance' DTT 5 mM 'natural abundance' stop_ save_ ############################ # Computer software used # ############################ save_TOPSPIN _Saveframe_category software _Name TOPSPIN _Version 3.2 loop_ _Vendor _Address _Electronic_address 'Bruker Biospin' . . stop_ loop_ _Task collection processing stop_ _Details . save_ save_SPARKY _Saveframe_category software _Name SPARKY _Version NMRFAM loop_ _Vendor _Address _Electronic_address Goddard . . stop_ loop_ _Task 'chemical shift assignment' 'data analysis' stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model Avance _Field_strength 850 _Details . save_ ############################# # NMR applied experiments # ############################# save_2D_1H-15N_HSQC_1 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-15N HSQC' _Sample_label $sample_1 save_ save_3D_HNCA_2 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCA' _Sample_label $sample_1 save_ save_3D_HN(CO)CA_3 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HN(CO)CA' _Sample_label $sample_1 save_ save_3D_HNCACB_4 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCACB' _Sample_label $sample_1 save_ ####################### # Sample conditions # ####################### save_sample_conditions_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units 'ionic strength' 0.15 . M pH 7.4 . pH pressure 1 . atm temperature 293 . 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 na indirect . . . 0.251449530 DSS H 1 'methyl protons' ppm 0 internal direct . . . 1.0 DSS N 15 'methyl protons' ppm 0 na indirect . . . 0.101329118 stop_ save_ ################################### # Assigned chemical shift lists # ################################### ################################################################### # Chemical Shift Ambiguity Index Value Definitions # # # # The values other than 1 are used for those atoms with different # # chemical shifts that cannot be assigned to stereospecific atoms # # or to specific residues or chains. # # # # Index Value Definition # # # # 1 Unique (including isolated methyl protons, # # geminal atoms, and geminal methyl # # groups with identical chemical shifts) # # (e.g. ILE HD11, HD12, HD13 protons) # # 2 Ambiguity of geminal atoms or geminal methyl # # proton groups (e.g. ASP HB2 and HB3 # # protons, LEU CD1 and CD2 carbons, or # # LEU HD11, HD12, HD13 and HD21, HD22, # # HD23 methyl protons) # # 3 Aromatic atoms on opposite sides of # # symmetrical rings (e.g. TYR HE1 and HE2 # # protons) # # 4 Intraresidue ambiguities (e.g. LYS HG and # # HD protons or TRP HZ2 and HZ3 protons) # # 5 Interresidue ambiguities (LYS 12 vs. LYS 27) # # 6 Intermolecular ambiguities (e.g. ASP 31 CA # # in monomer 1 and ASP 31 CA in monomer 2 # # of an asymmetrical homodimer, duplex # # DNA assignments, or other assignments # # that may apply to atoms in one or more # # molecule in the molecular assembly) # # 9 Ambiguous, specific ambiguity not defined # # # ################################################################### save_assigned_chem_shift_list_1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Experiment_label '2D 1H-15N HSQC' '3D HNCA' '3D HN(CO)CA' '3D HNCACB' 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 'dp-p38 alpha' _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 3 MET CA C 55.09 0.20 1 2 3 3 MET CB C 31.68 0.20 1 3 4 4 GLY H H 8.36 0.03 1 4 4 4 GLY CA C 44.77 0.20 1 5 4 4 GLY N N 111.00 0.30 1 6 5 5 SER H H 8.14 0.03 1 7 5 5 SER CA C 58.03 0.20 1 8 5 5 SER CB C 63.16 0.20 1 9 5 5 SER N N 116.11 0.30 1 10 6 6 GLN H H 8.39 0.03 1 11 6 6 GLN CA C 55.30 0.20 1 12 6 6 GLN CB C 28.77 0.20 1 13 6 6 GLN N N 122.25 0.30 1 14 7 7 GLU H H 8.27 0.03 1 15 7 7 GLU CA C 55.64 0.20 1 16 7 7 GLU CB C 29.28 0.20 1 17 7 7 GLU N N 122.61 0.30 1 18 8 8 ARG H H 8.34 0.03 1 19 8 8 ARG CA C 53.57 0.20 1 20 8 8 ARG CB C 29.74 0.20 1 21 8 8 ARG N N 125.48 0.30 1 22 9 9 PRO CA C 62.22 0.20 1 23 9 9 PRO CB C 31.60 0.20 1 24 10 10 THR H H 8.42 0.03 1 25 10 10 THR CA C 62.68 0.20 1 26 10 10 THR CB C 68.81 0.20 1 27 10 10 THR N N 117.49 0.30 1 28 11 11 PHE H H 8.73 0.03 1 29 11 11 PHE CA C 56.51 0.20 1 30 11 11 PHE CB C 41.38 0.20 1 31 11 11 PHE N N 127.38 0.30 1 32 12 12 TYR H H 9.07 0.03 1 33 12 12 TYR CA C 55.47 0.20 1 34 12 12 TYR CB C 40.26 0.20 1 35 12 12 TYR N N 120.17 0.30 1 36 13 13 ARG H H 8.38 0.03 1 37 13 13 ARG CA C 54.05 0.20 1 38 13 13 ARG CB C 32.83 0.20 1 39 13 13 ARG N N 120.19 0.30 1 40 14 14 GLN H H 8.90 0.03 1 41 14 14 GLN CA C 54.33 0.20 1 42 14 14 GLN CB C 32.47 0.20 1 43 14 14 GLN N N 122.55 0.30 1 44 15 15 GLU H H 8.79 0.03 1 45 15 15 GLU CA C 54.92 0.20 1 46 15 15 GLU CB C 29.76 0.20 1 47 15 15 GLU N N 125.66 0.30 1 48 16 16 LEU H H 8.93 0.03 1 49 16 16 LEU CA C 53.51 0.20 1 50 16 16 LEU CB C 43.74 0.20 1 51 16 16 LEU N N 128.62 0.30 1 52 17 17 ASN H H 7.21 0.03 1 53 17 17 ASN CA C 53.89 0.20 1 54 17 17 ASN CB C 36.68 0.20 1 55 17 17 ASN N N 116.60 0.30 1 56 18 18 LYS H H 8.81 0.03 1 57 18 18 LYS CA C 57.15 0.20 1 58 18 18 LYS CB C 28.82 0.20 1 59 18 18 LYS N N 110.05 0.30 1 60 19 19 THR H H 7.78 0.03 1 61 19 19 THR CA C 60.90 0.20 1 62 19 19 THR CB C 70.65 0.20 1 63 19 19 THR N N 115.90 0.30 1 64 20 20 ILE H H 8.54 0.03 1 65 20 20 ILE CA C 59.70 0.20 1 66 20 20 ILE CB C 35.95 0.20 1 67 20 20 ILE N N 125.60 0.30 1 68 21 21 TRP H H 9.20 0.03 1 69 21 21 TRP CA C 56.40 0.20 1 70 21 21 TRP CB C 28.48 0.20 1 71 21 21 TRP N N 131.12 0.30 1 72 22 22 GLU H H 8.20 0.03 1 73 22 22 GLU CA C 54.39 0.20 1 74 22 22 GLU CB C 30.55 0.20 1 75 22 22 GLU N N 128.29 0.30 1 76 23 23 VAL H H 7.58 0.03 1 77 23 23 VAL CA C 55.73 0.20 1 78 23 23 VAL CB C 33.55 0.20 1 79 23 23 VAL N N 112.42 0.30 1 80 24 24 PRO CA C 61.43 0.20 1 81 24 24 PRO CB C 31.71 0.20 1 82 25 25 GLU H H 8.05 0.03 1 83 25 25 GLU CA C 58.12 0.20 1 84 25 25 GLU CB C 29.07 0.20 1 85 25 25 GLU N N 119.05 0.30 1 86 26 26 ARG H H 7.41 0.03 1 87 26 26 ARG CA C 57.36 0.20 1 88 26 26 ARG CB C 29.61 0.20 1 89 26 26 ARG N N 117.59 0.30 1 90 27 27 TYR H H 7.71 0.03 1 91 27 27 TYR CA C 56.83 0.20 1 92 27 27 TYR CB C 37.19 0.20 1 93 27 27 TYR N N 118.24 0.30 1 94 28 28 GLN H H 9.12 0.03 1 95 28 28 GLN CA C 53.15 0.20 1 96 28 28 GLN CB C 32.38 0.20 1 97 28 28 GLN N N 122.68 0.30 1 98 29 29 ASN H H 8.76 0.03 1 99 29 29 ASN CA C 53.14 0.20 1 100 29 29 ASN CB C 36.17 0.20 1 101 29 29 ASN N N 117.59 0.30 1 102 30 30 LEU H H 8.48 0.03 1 103 30 30 LEU CA C 56.57 0.20 1 104 30 30 LEU CB C 40.77 0.20 1 105 30 30 LEU N N 120.33 0.30 1 106 31 31 SER H H 8.70 0.03 1 107 31 31 SER CA C 54.12 0.20 1 108 31 31 SER CB C 64.17 0.20 1 109 31 31 SER N N 116.18 0.30 1 110 32 32 PRO CA C 63.99 0.20 1 111 32 32 PRO CB C 31.80 0.20 1 112 33 33 VAL H H 8.52 0.03 1 113 33 33 VAL CA C 61.61 0.20 1 114 33 33 VAL CB C 33.41 0.20 1 115 33 33 VAL N N 121.02 0.30 1 116 34 34 GLY H H 7.79 0.03 1 117 34 34 GLY CA C 45.07 0.20 1 118 34 34 GLY N N 109.03 0.30 1 119 35 35 SER H H 8.34 0.03 1 120 35 35 SER CA C 57.55 0.20 1 121 35 35 SER CB C 64.20 0.20 1 122 35 35 SER N N 115.42 0.30 1 123 36 36 GLY H H 8.11 0.03 1 124 36 36 GLY CA C 44.43 0.20 1 125 36 36 GLY N N 110.51 0.30 1 126 37 37 ALA H H 8.40 0.03 1 127 37 37 ALA CA C 53.48 0.20 1 128 37 37 ALA CB C 17.81 0.20 1 129 37 37 ALA N N 124.18 0.30 1 130 38 38 TYR H H 7.98 0.03 1 131 38 38 TYR CA C 56.58 0.20 1 132 38 38 TYR CB C 37.16 0.20 1 133 38 38 TYR N N 114.00 0.30 1 134 39 39 GLY H H 7.30 0.03 1 135 39 39 GLY CA C 45.00 0.20 1 136 39 39 GLY N N 108.64 0.30 1 137 40 40 SER H H 8.09 0.03 1 138 40 40 SER CA C 57.47 0.20 1 139 40 40 SER N N 116.10 0.30 1 140 41 41 VAL H H 8.60 0.03 1 141 41 41 VAL CA C 60.99 0.20 1 142 41 41 VAL CB C 33.93 0.20 1 143 41 41 VAL N N 122.55 0.30 1 144 42 42 CYS H H 9.18 0.03 1 145 42 42 CYS CA C 57.52 0.20 1 146 42 42 CYS CB C 30.70 0.20 1 147 42 42 CYS N N 125.34 0.30 1 148 43 43 ALA H H 8.72 0.03 1 149 43 43 ALA CA C 50.18 0.20 1 150 43 43 ALA CB C 19.88 0.20 1 151 43 43 ALA N N 125.69 0.30 1 152 44 44 ALA H H 8.96 0.03 1 153 44 44 ALA CA C 50.16 0.20 1 154 44 44 ALA CB C 22.21 0.20 1 155 44 44 ALA N N 120.70 0.30 1 156 45 45 PHE H H 9.14 0.03 1 157 45 45 PHE CA C 56.77 0.20 1 158 45 45 PHE CB C 40.53 0.20 1 159 45 45 PHE N N 122.36 0.30 1 160 46 46 ASP H H 8.24 0.03 1 161 46 46 ASP CA C 51.42 0.20 1 162 46 46 ASP CB C 40.72 0.20 1 163 46 46 ASP N N 125.98 0.30 1 164 47 47 THR H H 8.89 0.03 1 165 47 47 THR CA C 63.38 0.20 1 166 47 47 THR CB C 68.49 0.20 1 167 47 47 THR N N 117.50 0.30 1 168 48 48 LYS H H 7.82 0.03 1 169 48 48 LYS CA C 58.20 0.20 1 170 48 48 LYS CB C 31.98 0.20 1 171 48 48 LYS N N 121.79 0.30 1 172 49 49 THR H H 6.52 0.03 1 173 49 49 THR CA C 61.29 0.20 1 174 49 49 THR CB C 70.44 0.20 1 175 49 49 THR N N 105.09 0.30 1 176 50 50 GLY H H 8.29 0.03 1 177 50 50 GLY CA C 45.48 0.20 1 178 50 50 GLY N N 112.42 0.30 1 179 51 51 LEU H H 7.03 0.03 1 180 51 51 LEU CA C 53.14 0.20 1 181 51 51 LEU CB C 43.06 0.20 1 182 51 51 LEU N N 119.69 0.30 1 183 52 52 ARG H H 8.17 0.03 1 184 52 52 ARG CA C 55.53 0.20 1 185 52 52 ARG CB C 29.48 0.20 1 186 52 52 ARG N N 119.88 0.30 1 187 53 53 VAL H H 8.76 0.03 1 188 53 53 VAL CA C 59.03 0.20 1 189 53 53 VAL CB C 34.63 0.20 1 190 53 53 VAL N N 116.79 0.30 1 191 54 54 ALA H H 8.75 0.03 1 192 54 54 ALA CA C 49.66 0.20 1 193 54 54 ALA CB C 19.12 0.20 1 194 54 54 ALA N N 122.54 0.30 1 195 55 55 VAL H H 9.17 0.03 1 196 55 55 VAL CA C 60.27 0.20 1 197 55 55 VAL N N 122.60 0.30 1 198 56 56 LYS H H 9.49 0.03 1 199 56 56 LYS CA C 53.58 0.20 1 200 56 56 LYS CB C 34.21 0.20 1 201 56 56 LYS N N 129.20 0.30 1 202 57 57 LYS H H 8.51 0.03 1 203 57 57 LYS CA C 53.88 0.20 1 204 57 57 LYS CB C 33.34 0.20 1 205 57 57 LYS N N 128.37 0.30 1 206 58 58 LEU H H 8.01 0.03 1 207 58 58 LEU CA C 54.62 0.20 1 208 58 58 LEU CB C 39.30 0.20 1 209 58 58 LEU N N 128.49 0.30 1 210 59 59 SER H H 7.97 0.03 1 211 59 59 SER CA C 56.73 0.20 1 212 59 59 SER CB C 62.67 0.20 1 213 59 59 SER N N 117.94 0.30 1 214 60 60 ARG H H 8.69 0.03 1 215 60 60 ARG CA C 55.70 0.20 1 216 60 60 ARG CB C 28.59 0.20 1 217 60 60 ARG N N 123.25 0.30 1 218 61 61 PRO CA C 63.84 0.20 1 219 62 62 PHE H H 7.85 0.03 1 220 62 62 PHE CA C 53.95 0.20 1 221 62 62 PHE CB C 37.40 0.20 1 222 62 62 PHE N N 112.67 0.30 1 223 63 63 GLN H H 6.99 0.03 1 224 63 63 GLN CA C 57.09 0.20 1 225 63 63 GLN CB C 28.83 0.20 1 226 63 63 GLN N N 115.72 0.30 1 227 64 64 SER H H 7.34 0.03 1 228 64 64 SER CA C 56.03 0.20 1 229 64 64 SER CB C 65.95 0.20 1 230 64 64 SER N N 110.22 0.30 1 231 65 65 ILE H H 9.14 0.03 1 232 65 65 ILE CA C 65.23 0.20 1 233 65 65 ILE CB C 37.25 0.20 1 234 65 65 ILE N N 123.44 0.30 1 235 66 66 ILE H H 7.56 0.03 1 236 66 66 ILE CA C 63.80 0.20 1 237 66 66 ILE CB C 37.09 0.20 1 238 66 66 ILE N N 118.69 0.30 1 239 67 67 HIS CA C 60.07 0.20 1 240 68 68 ALA H H 8.57 0.03 1 241 68 68 ALA CA C 54.70 0.20 1 242 68 68 ALA CB C 18.49 0.20 1 243 68 68 ALA N N 123.82 0.30 1 244 69 69 LYS H H 7.81 0.03 1 245 69 69 LYS CA C 59.10 0.20 1 246 69 69 LYS CB C 31.35 0.20 1 247 69 69 LYS N N 118.50 0.30 1 248 70 70 ARG H H 7.40 0.03 1 249 70 70 ARG CA C 58.73 0.20 1 250 70 70 ARG CB C 28.71 0.20 1 251 70 70 ARG N N 119.14 0.30 1 252 71 71 THR H H 8.33 0.03 1 253 71 71 THR CA C 66.59 0.20 1 254 71 71 THR N N 119.92 0.30 1 255 72 72 TYR H H 7.54 0.03 1 256 72 72 TYR CA C 62.25 0.20 1 257 72 72 TYR CB C 36.95 0.20 1 258 72 72 TYR N N 121.53 0.30 1 259 81 81 MET CA C 55.20 0.20 1 260 81 81 MET CB C 32.91 0.20 1 261 82 82 LYS H H 8.45 0.03 1 262 82 82 LYS CA C 54.10 0.20 1 263 82 82 LYS CB C 31.97 0.20 1 264 82 82 LYS N N 128.90 0.30 1 265 83 83 HIS H H 8.63 0.03 1 266 83 83 HIS CA C 56.65 0.20 1 267 83 83 HIS CB C 32.66 0.20 1 268 83 83 HIS N N 124.49 0.30 1 269 84 84 GLU H H 7.94 0.03 1 270 84 84 GLU CA C 59.10 0.20 1 271 84 84 GLU CB C 29.62 0.20 1 272 84 84 GLU N N 125.66 0.30 1 273 85 85 ASN H H 11.38 0.03 1 274 85 85 ASN CA C 53.13 0.20 1 275 85 85 ASN CB C 40.80 0.20 1 276 85 85 ASN N N 118.24 0.30 1 277 86 86 VAL H H 7.64 0.03 1 278 86 86 VAL CA C 61.05 0.20 1 279 86 86 VAL CB C 35.20 0.20 1 280 86 86 VAL N N 119.86 0.30 1 281 87 87 ILE H H 8.31 0.03 1 282 87 87 ILE CA C 60.92 0.20 1 283 87 87 ILE N N 129.47 0.30 1 284 88 88 GLY H H 7.64 0.03 1 285 88 88 GLY CA C 43.19 0.20 1 286 88 88 GLY N N 110.33 0.30 1 287 89 89 LEU H H 8.25 0.03 1 288 89 89 LEU CA C 54.01 0.20 1 289 89 89 LEU N N 121.14 0.30 1 290 90 90 LEU H H 8.89 0.03 1 291 90 90 LEU CA C 55.24 0.20 1 292 90 90 LEU CB C 42.17 0.20 1 293 90 90 LEU N N 126.72 0.30 1 294 91 91 ASP CA C 52.50 0.20 1 295 91 91 ASP CB C 41.53 0.20 1 296 92 92 VAL H H 7.72 0.03 1 297 92 92 VAL CA C 59.09 0.20 1 298 92 92 VAL CB C 32.83 0.20 1 299 92 92 VAL N N 120.59 0.30 1 300 93 93 PHE H H 8.19 0.03 1 301 93 93 PHE CA C 55.46 0.20 1 302 93 93 PHE CB C 41.09 0.20 1 303 93 93 PHE N N 119.05 0.30 1 304 94 94 THR H H 8.88 0.03 1 305 94 94 THR CA C 56.92 0.20 1 306 94 94 THR CB C 71.71 0.20 1 307 94 94 THR N N 113.66 0.30 1 308 95 95 PRO CA C 62.09 0.20 1 309 95 95 PRO CB C 30.48 0.20 1 310 96 96 ALA H H 7.63 0.03 1 311 96 96 ALA CA C 52.33 0.20 1 312 96 96 ALA CB C 19.96 0.20 1 313 96 96 ALA N N 122.43 0.30 1 314 97 97 ARG H H 9.21 0.03 1 315 97 97 ARG CA C 55.54 0.20 1 316 97 97 ARG CB C 29.48 0.20 1 317 97 97 ARG N N 121.30 0.30 1 318 98 98 SER H H 7.31 0.03 1 319 98 98 SER CA C 56.16 0.20 1 320 98 98 SER CB C 65.03 0.20 1 321 98 98 SER N N 111.41 0.30 1 322 99 99 LEU H H 8.42 0.03 1 323 99 99 LEU CA C 56.54 0.20 1 324 99 99 LEU CB C 40.41 0.20 1 325 99 99 LEU N N 122.91 0.30 1 326 100 100 GLU H H 8.23 0.03 1 327 100 100 GLU CA C 58.98 0.20 1 328 100 100 GLU CB C 28.03 0.20 1 329 100 100 GLU N N 117.38 0.30 1 330 101 101 GLU H H 6.95 0.03 1 331 101 101 GLU CA C 54.42 0.20 1 332 101 101 GLU CB C 30.25 0.20 1 333 101 101 GLU N N 115.47 0.30 1 334 102 102 PHE H H 7.22 0.03 1 335 102 102 PHE CA C 56.47 0.20 1 336 102 102 PHE CB C 37.96 0.20 1 337 102 102 PHE N N 122.25 0.30 1 338 103 103 ASN H H 8.47 0.03 1 339 103 103 ASN CA C 53.75 0.20 1 340 103 103 ASN CB C 41.46 0.20 1 341 103 103 ASN N N 125.56 0.30 1 342 104 104 ASP H H 7.57 0.03 1 343 104 104 ASP CA C 52.85 0.20 1 344 104 104 ASP CB C 43.99 0.20 1 345 104 104 ASP N N 115.89 0.30 1 346 105 105 VAL H H 8.38 0.03 1 347 105 105 VAL CA C 61.15 0.20 1 348 105 105 VAL CB C 35.09 0.20 1 349 105 105 VAL N N 121.21 0.30 1 350 106 106 TYR H H 8.06 0.03 1 351 106 106 TYR CA C 54.65 0.20 1 352 106 106 TYR CB C 39.19 0.20 1 353 106 106 TYR N N 124.73 0.30 1 354 107 107 LEU H H 8.77 0.03 1 355 107 107 LEU CA C 52.95 0.20 1 356 107 107 LEU CB C 43.59 0.20 1 357 107 107 LEU N N 119.46 0.30 1 358 108 108 VAL CA C 60.52 0.20 1 359 109 109 THR H H 8.95 0.03 1 360 109 109 THR CA C 59.09 0.20 1 361 109 109 THR CB C 72.72 0.20 1 362 109 109 THR N N 118.20 0.30 1 363 110 110 HIS H H 8.82 0.03 1 364 110 110 HIS CA C 58.46 0.20 1 365 110 110 HIS CB C 31.16 0.20 1 366 110 110 HIS N N 119.47 0.30 1 367 111 111 LEU H H 8.12 0.03 1 368 111 111 LEU CA C 53.91 0.20 1 369 111 111 LEU CB C 41.49 0.20 1 370 111 111 LEU N N 125.54 0.30 1 371 112 112 MET CA C 54.37 0.20 1 372 112 112 MET CB C 31.39 0.20 1 373 113 113 GLY H H 8.10 0.03 1 374 113 113 GLY CA C 45.86 0.20 1 375 113 113 GLY N N 108.71 0.30 1 376 114 114 ALA H H 8.08 0.03 1 377 114 114 ALA CA C 50.93 0.20 1 378 114 114 ALA CB C 21.10 0.20 1 379 114 114 ALA N N 123.13 0.30 1 380 115 115 ASP H H 8.03 0.03 1 381 115 115 ASP CA C 51.91 0.20 1 382 115 115 ASP CB C 42.13 0.20 1 383 115 115 ASP N N 118.11 0.30 1 384 116 116 LEU CA C 56.66 0.20 1 385 117 117 ASN H H 7.69 0.03 1 386 117 117 ASN CA C 55.40 0.20 1 387 117 117 ASN CB C 37.71 0.20 1 388 117 117 ASN N N 117.23 0.30 1 389 118 118 ASN H H 7.89 0.03 1 390 118 118 ASN CA C 55.70 0.20 1 391 118 118 ASN N N 118.17 0.30 1 392 119 119 ILE CA C 63.31 0.20 1 393 120 120 VAL H H 7.59 0.03 1 394 120 120 VAL CA C 64.01 0.20 1 395 120 120 VAL CB C 31.01 0.20 1 396 120 120 VAL N N 115.90 0.30 1 397 121 121 LYS H H 7.15 0.03 1 398 121 121 LYS CA C 57.28 0.20 1 399 121 121 LYS CB C 31.50 0.20 1 400 121 121 LYS N N 117.46 0.30 1 401 122 122 CYS H H 7.43 0.03 1 402 122 122 CYS CA C 58.88 0.20 1 403 122 122 CYS CB C 28.65 0.20 1 404 122 122 CYS N N 113.83 0.30 1 405 123 123 GLN H H 7.99 0.03 1 406 123 123 GLN CA C 54.53 0.20 1 407 123 123 GLN CB C 30.33 0.20 1 408 123 123 GLN N N 120.03 0.30 1 409 124 124 LYS H H 8.25 0.03 1 410 124 124 LYS CA C 54.70 0.20 1 411 124 124 LYS CB C 31.07 0.20 1 412 124 124 LYS N N 122.77 0.30 1 413 125 125 LEU H H 8.67 0.03 1 414 125 125 LEU CA C 53.81 0.20 1 415 125 125 LEU CB C 41.34 0.20 1 416 125 125 LEU N N 127.56 0.30 1 417 126 126 THR CA C 60.70 0.20 1 418 126 126 THR CB C 71.75 0.20 1 419 127 127 ASP H H 9.10 0.03 1 420 127 127 ASP CA C 58.00 0.20 1 421 127 127 ASP CB C 42.32 0.20 1 422 127 127 ASP N N 121.17 0.30 1 423 128 128 ASP H H 7.76 0.03 1 424 128 128 ASP CA C 57.28 0.20 1 425 128 128 ASP CB C 40.26 0.20 1 426 128 128 ASP N N 115.10 0.30 1 427 130 130 VAL H H 8.06 0.03 1 428 130 130 VAL CA C 68.15 0.20 1 429 130 130 VAL CB C 29.86 0.20 1 430 130 130 VAL N N 119.67 0.30 1 431 131 131 GLN H H 8.46 0.03 1 432 131 131 GLN CA C 58.93 0.20 1 433 131 131 GLN CB C 29.70 0.20 1 434 131 131 GLN N N 118.61 0.30 1 435 132 132 PHE H H 7.24 0.03 1 436 132 132 PHE CA C 57.87 0.20 1 437 132 132 PHE CB C 38.98 0.20 1 438 132 132 PHE N N 115.45 0.30 1 439 133 133 LEU H H 8.87 0.03 1 440 133 133 LEU CA C 58.10 0.20 1 441 133 133 LEU CB C 41.53 0.20 1 442 133 133 LEU N N 120.80 0.30 1 443 135 135 TYR H H 8.90 0.03 1 444 135 135 TYR CA C 51.34 0.20 1 445 135 135 TYR CB C 39.33 0.20 1 446 135 135 TYR N N 120.16 0.30 1 447 136 136 GLN H H 8.47 0.03 1 448 136 136 GLN CA C 51.22 0.20 1 449 136 136 GLN N N 116.32 0.30 1 450 139 139 ARG CA C 59.95 0.20 1 451 139 139 ARG CB C 29.17 0.20 1 452 140 140 GLY H H 8.10 0.03 1 453 140 140 GLY CA C 46.42 0.20 1 454 140 140 GLY N N 107.41 0.30 1 455 141 141 LEU H H 8.62 0.03 1 456 141 141 LEU CA C 56.33 0.20 1 457 141 141 LEU CB C 40.68 0.20 1 458 141 141 LEU N N 121.68 0.30 1 459 142 142 LYS H H 8.59 0.03 1 460 142 142 LYS CA C 59.37 0.20 1 461 142 142 LYS CB C 31.55 0.20 1 462 142 142 LYS N N 119.43 0.30 1 463 143 143 TYR H H 6.74 0.03 1 464 143 143 TYR CA C 61.30 0.20 1 465 143 143 TYR CB C 37.64 0.20 1 466 143 143 TYR N N 118.22 0.30 1 467 144 144 ILE H H 8.42 0.03 1 468 144 144 ILE CA C 66.40 0.20 1 469 144 144 ILE N N 120.69 0.30 1 470 145 145 HIS H H 9.45 0.03 1 471 145 145 HIS CA C 56.90 0.20 1 472 145 145 HIS CB C 30.34 0.20 1 473 145 145 HIS N N 119.68 0.30 1 474 146 146 SER H H 7.78 0.03 1 475 146 146 SER CA C 60.82 0.20 1 476 146 146 SER CB C 62.05 0.20 1 477 146 146 SER N N 116.40 0.30 1 478 147 147 ALA H H 7.34 0.03 1 479 147 147 ALA CA C 50.98 0.20 1 480 147 147 ALA CB C 17.20 0.20 1 481 147 147 ALA N N 126.41 0.30 1 482 148 148 ASP H H 8.12 0.03 1 483 148 148 ASP CA C 55.18 0.20 1 484 148 148 ASP CB C 38.48 0.20 1 485 148 148 ASP N N 115.31 0.30 1 486 149 149 ILE H H 7.17 0.03 1 487 149 149 ILE CA C 58.85 0.20 1 488 149 149 ILE CB C 38.44 0.20 1 489 149 149 ILE N N 119.27 0.30 1 490 150 150 ILE H H 7.79 0.03 1 491 150 150 ILE CA C 59.75 0.20 1 492 150 150 ILE N N 123.50 0.30 1 493 151 151 HIS H H 7.33 0.03 1 494 151 151 HIS CA C 62.48 0.20 1 495 151 151 HIS N N 121.10 0.30 1 496 157 157 SER H H 7.71 0.03 1 497 157 157 SER CA C 59.22 0.20 1 498 157 157 SER N N 106.83 0.30 1 499 158 158 ASN H H 7.70 0.03 1 500 158 158 ASN CA C 52.29 0.20 1 501 158 158 ASN N N 118.69 0.30 1 502 159 159 LEU H H 7.05 0.03 1 503 159 159 LEU CA C 52.74 0.20 1 504 159 159 LEU N N 119.62 0.30 1 505 160 160 ALA H H 8.43 0.03 1 506 160 160 ALA CA C 50.21 0.20 1 507 160 160 ALA CB C 21.32 0.20 1 508 160 160 ALA N N 125.63 0.30 1 509 161 161 VAL H H 8.07 0.03 1 510 161 161 VAL CA C 58.70 0.20 1 511 161 161 VAL CB C 35.78 0.20 1 512 161 161 VAL N N 118.14 0.30 1 513 162 162 ASN H H 7.79 0.03 1 514 162 162 ASN CA C 49.94 0.20 1 515 162 162 ASN CB C 39.96 0.20 1 516 162 162 ASN N N 121.25 0.30 1 517 163 163 GLU H H 8.57 0.03 1 518 163 163 GLU CA C 58.52 0.20 1 519 163 163 GLU CB C 28.60 0.20 1 520 163 163 GLU N N 116.64 0.30 1 521 164 164 ASP H H 7.32 0.03 1 522 164 164 ASP CA C 53.58 0.20 1 523 164 164 ASP CB C 40.62 0.20 1 524 164 164 ASP N N 117.24 0.30 1 525 165 165 CYS H H 8.35 0.03 1 526 165 165 CYS CA C 60.99 0.20 1 527 165 165 CYS N N 114.74 0.30 1 528 166 166 GLU H H 7.58 0.03 1 529 166 166 GLU CA C 55.51 0.20 1 530 166 166 GLU CB C 28.08 0.20 1 531 166 166 GLU N N 118.78 0.30 1 532 167 167 LEU H H 7.85 0.03 1 533 167 167 LEU CA C 52.89 0.20 1 534 167 167 LEU CB C 45.29 0.20 1 535 167 167 LEU N N 125.84 0.30 1 536 168 168 LYS H H 8.89 0.03 1 537 168 168 LYS CA C 54.93 0.20 1 538 168 168 LYS CB C 37.46 0.20 1 539 168 168 LYS N N 122.78 0.30 1 540 169 169 ILE H H 8.12 0.03 1 541 169 169 ILE CA C 62.11 0.20 1 542 169 169 ILE CB C 38.76 0.20 1 543 169 169 ILE N N 122.18 0.30 1 544 174 174 LEU CA C 54.45 0.20 1 545 175 175 ALA H H 8.00 0.03 1 546 175 175 ALA CA C 59.66 0.20 1 547 175 175 ALA N N 119.30 0.30 1 548 176 176 ARG H H 8.34 0.03 1 549 176 176 ARG CA C 55.26 0.20 1 550 176 176 ARG CB C 37.37 0.20 1 551 176 176 ARG N N 117.10 0.30 1 552 177 177 HIS CA C 59.01 0.20 1 553 178 178 THR H H 7.19 0.03 1 554 178 178 THR CA C 55.98 0.20 1 555 178 178 THR N N 115.39 0.30 1 556 179 179 ASP CA C 54.70 0.20 1 557 180 180 ASP H H 8.07 0.03 1 558 180 180 ASP CA C 54.37 0.20 1 559 180 180 ASP CB C 40.76 0.20 1 560 180 180 ASP N N 119.75 0.30 1 561 181 181 GLU H H 8.09 0.03 1 562 181 181 GLU CA C 56.77 0.20 1 563 181 181 GLU CB C 29.25 0.20 1 564 181 181 GLU N N 120.81 0.30 1 565 182 182 MET H H 8.08 0.03 1 566 182 182 MET CA C 55.46 0.20 1 567 182 182 MET N N 120.12 0.30 1 568 183 183 TPO H H 8.59 0.03 1 569 183 183 TPO CA C 62.18 0.20 1 570 183 183 TPO CB C 69.28 0.20 1 571 183 183 TPO N N 113.86 0.30 1 572 184 184 GLY H H 8.22 0.03 1 573 184 184 GLY CA C 44.94 0.20 1 574 184 184 GLY N N 111.62 0.30 1 575 185 185 PTR H H 7.72 0.03 1 576 185 185 PTR CA C 57.93 0.20 1 577 185 185 PTR N N 121.56 0.30 1 578 186 186 VAL H H 7.73 0.03 1 579 186 186 VAL CA C 61.92 0.20 1 580 186 186 VAL N N 123.26 0.30 1 581 191 191 TYR CA C 56.57 0.20 1 582 192 192 ARG H H 7.28 0.03 1 583 192 192 ARG CA C 55.39 0.20 1 584 192 192 ARG CB C 30.93 0.20 1 585 192 192 ARG N N 122.58 0.30 1 586 193 193 ALA H H 8.80 0.03 1 587 193 193 ALA CA C 49.72 0.20 1 588 193 193 ALA N N 126.16 0.30 1 589 197 197 MET CA C 59.16 0.20 1 590 198 198 LEU H H 9.16 0.03 1 591 198 198 LEU CA C 57.66 0.20 1 592 198 198 LEU CB C 41.22 0.20 1 593 198 198 LEU N N 126.40 0.30 1 594 199 199 ASN H H 7.82 0.03 1 595 199 199 ASN CA C 53.27 0.20 1 596 199 199 ASN CB C 40.21 0.20 1 597 199 199 ASN N N 115.40 0.30 1 598 200 200 TRP H H 8.50 0.03 1 599 200 200 TRP CA C 54.28 0.20 1 600 200 200 TRP CB C 27.80 0.20 1 601 200 200 TRP N N 125.22 0.30 1 602 201 201 MET H H 8.58 0.03 1 603 201 201 MET CA C 61.80 0.20 1 604 201 201 MET N N 119.89 0.30 1 605 202 202 HIS H H 7.09 0.03 1 606 202 202 HIS CA C 59.11 0.20 1 607 202 202 HIS CB C 32.65 0.20 1 608 202 202 HIS N N 115.12 0.30 1 609 203 203 TYR H H 10.05 0.03 1 610 203 203 TYR CA C 52.50 0.20 1 611 203 203 TYR N N 127.16 0.30 1 612 204 204 ASN H H 8.71 0.03 1 613 204 204 ASN CA C 56.48 0.20 1 614 204 204 ASN CB C 41.06 0.20 1 615 204 204 ASN N N 124.76 0.30 1 616 206 206 THR H H 8.29 0.03 1 617 206 206 THR CA C 58.96 0.20 1 618 206 206 THR N N 115.47 0.30 1 619 208 208 ASP CA C 56.40 0.20 1 620 209 209 ILE H H 7.22 0.03 1 621 209 209 ILE CA C 60.59 0.20 1 622 209 209 ILE CB C 34.30 0.20 1 623 209 209 ILE N N 119.34 0.30 1 624 210 210 TRP H H 7.44 0.03 1 625 210 210 TRP CA C 61.02 0.20 1 626 210 210 TRP CB C 27.80 0.20 1 627 210 210 TRP N N 121.02 0.30 1 628 211 211 SER H H 7.52 0.03 1 629 211 211 SER CA C 61.91 0.20 1 630 211 211 SER CB C 63.04 0.20 1 631 211 211 SER N N 112.68 0.30 1 632 212 212 VAL H H 7.95 0.03 1 633 212 212 VAL CA C 67.16 0.20 1 634 212 212 VAL CB C 29.90 0.20 1 635 212 212 VAL N N 120.06 0.30 1 636 213 213 GLY H H 8.45 0.03 1 637 213 213 GLY CA C 47.60 0.20 1 638 213 213 GLY N N 110.42 0.30 1 639 214 214 CYS H H 7.81 0.03 1 640 214 214 CYS CA C 63.52 0.20 1 641 214 214 CYS CB C 27.44 0.20 1 642 214 214 CYS N N 119.33 0.30 1 643 215 215 ILE H H 8.43 0.03 1 644 215 215 ILE CA C 65.44 0.20 1 645 215 215 ILE CB C 37.41 0.20 1 646 215 215 ILE N N 124.03 0.30 1 647 216 216 MET H H 9.26 0.03 1 648 216 216 MET CA C 60.12 0.20 1 649 216 216 MET CB C 30.68 0.20 1 650 216 216 MET N N 120.58 0.30 1 651 217 217 ALA H H 8.03 0.03 1 652 217 217 ALA CA C 54.94 0.20 1 653 217 217 ALA CB C 19.99 0.20 1 654 217 217 ALA N N 118.24 0.30 1 655 218 218 GLU H H 7.01 0.03 1 656 218 218 GLU CA C 57.85 0.20 1 657 218 218 GLU CB C 29.21 0.20 1 658 218 218 GLU N N 120.22 0.30 1 659 219 219 LEU H H 7.22 0.03 1 660 219 219 LEU CA C 57.02 0.20 1 661 219 219 LEU CB C 41.98 0.20 1 662 219 219 LEU N N 116.40 0.30 1 663 220 220 LEU H H 8.45 0.03 1 664 220 220 LEU CA C 56.66 0.20 1 665 220 220 LEU CB C 39.93 0.20 1 666 220 220 LEU N N 118.57 0.30 1 667 221 221 THR H H 7.93 0.03 1 668 221 221 THR CA C 61.74 0.20 1 669 221 221 THR CB C 71.00 0.20 1 670 221 221 THR N N 106.36 0.30 1 671 222 222 GLY H H 8.45 0.03 1 672 222 222 GLY CA C 45.13 0.20 1 673 222 222 GLY N N 112.84 0.30 1 674 223 223 ARG H H 8.01 0.03 1 675 223 223 ARG CA C 53.57 0.20 1 676 223 223 ARG CB C 31.89 0.20 1 677 223 223 ARG N N 119.50 0.30 1 678 224 224 THR H H 7.87 0.03 1 679 224 224 THR CA C 63.31 0.20 1 680 224 224 THR CB C 68.28 0.20 1 681 224 224 THR N N 120.03 0.30 1 682 225 225 LEU H H 7.77 0.03 1 683 225 225 LEU CA C 52.66 0.20 1 684 225 225 LEU CB C 40.84 0.20 1 685 225 225 LEU N N 117.88 0.30 1 686 227 227 PRO CA C 60.46 0.20 1 687 227 227 PRO CB C 26.73 0.20 1 688 228 228 GLY H H 8.30 0.03 1 689 228 228 GLY CA C 45.09 0.20 1 690 228 228 GLY N N 114.01 0.30 1 691 229 229 THR H H 10.06 0.03 1 692 229 229 THR CA C 63.23 0.20 1 693 229 229 THR N N 116.96 0.30 1 694 230 230 ASP H H 8.60 0.03 1 695 230 230 ASP CA C 57.59 0.20 1 696 230 230 ASP N N 130.84 0.30 1 697 231 231 HIS H H 8.49 0.03 1 698 231 231 HIS CA C 51.74 0.20 1 699 231 231 HIS CB C 40.03 0.20 1 700 231 231 HIS N N 114.38 0.30 1 701 239 239 LEU CA C 57.51 0.20 1 702 239 239 LEU CB C 41.38 0.20 1 703 240 240 ARG H H 8.12 0.03 1 704 240 240 ARG CA C 58.91 0.20 1 705 240 240 ARG CB C 31.73 0.20 1 706 240 240 ARG N N 116.99 0.30 1 707 241 241 LEU H H 7.53 0.03 1 708 241 241 LEU CA C 57.19 0.20 1 709 241 241 LEU CB C 40.42 0.20 1 710 241 241 LEU N N 117.81 0.30 1 711 242 242 VAL H H 8.45 0.03 1 712 242 242 VAL CA C 59.98 0.20 1 713 242 242 VAL N N 122.58 0.30 1 714 243 243 GLY CA C 44.89 0.20 1 715 244 244 THR H H 7.75 0.03 1 716 244 244 THR CA C 59.08 0.20 1 717 244 244 THR N N 121.19 0.30 1 718 245 245 PRO CA C 62.31 0.20 1 719 245 245 PRO CB C 31.94 0.20 1 720 246 246 GLY H H 8.22 0.03 1 721 246 246 GLY CA C 43.30 0.20 1 722 246 246 GLY N N 108.68 0.30 1 723 247 247 ALA H H 8.30 0.03 1 724 247 247 ALA CA C 54.81 0.20 1 725 247 247 ALA CB C 18.07 0.20 1 726 247 247 ALA N N 121.46 0.30 1 727 248 248 GLU H H 8.52 0.03 1 728 248 248 GLU CA C 58.69 0.20 1 729 248 248 GLU CB C 27.86 0.20 1 730 248 248 GLU N N 116.14 0.30 1 731 249 249 LEU H H 7.41 0.03 1 732 249 249 LEU CA C 56.45 0.20 1 733 249 249 LEU CB C 40.35 0.20 1 734 249 249 LEU N N 120.46 0.30 1 735 250 250 LEU H H 7.83 0.03 1 736 250 250 LEU CA C 57.45 0.20 1 737 250 250 LEU CB C 41.14 0.20 1 738 250 250 LEU N N 118.35 0.30 1 739 251 251 LYS H H 7.54 0.03 1 740 251 251 LYS CA C 55.61 0.20 1 741 251 251 LYS N N 120.18 0.30 1 742 252 252 LYS H H 7.45 0.03 1 743 252 252 LYS CA C 55.48 0.20 1 744 252 252 LYS N N 120.99 0.30 1 745 256 256 GLU CA C 59.27 0.20 1 746 257 257 SER H H 8.30 0.03 1 747 257 257 SER CA C 60.60 0.20 1 748 257 257 SER N N 114.30 0.30 1 749 258 258 ALA H H 7.63 0.03 1 750 258 258 ALA CA C 54.34 0.20 1 751 258 258 ALA CB C 18.22 0.20 1 752 258 258 ALA N N 125.80 0.30 1 753 259 259 ARG H H 8.79 0.03 1 754 259 259 ARG CA C 54.95 0.20 1 755 259 259 ARG CB C 29.80 0.20 1 756 259 259 ARG N N 126.38 0.30 1 757 262 262 ILE CA C 62.91 0.20 1 758 263 263 GLN H H 7.97 0.03 1 759 263 263 GLN CA C 57.68 0.20 1 760 263 263 GLN CB C 28.22 0.20 1 761 263 263 GLN N N 118.13 0.30 1 762 264 264 SER H H 7.36 0.03 1 763 264 264 SER CA C 58.97 0.20 1 764 264 264 SER CB C 63.29 0.20 1 765 264 264 SER N N 113.99 0.30 1 766 265 265 LEU H H 6.80 0.03 1 767 265 265 LEU CA C 53.97 0.20 1 768 265 265 LEU N N 123.00 0.30 1 769 266 266 THR CA C 63.22 0.20 1 770 267 267 GLN H H 8.44 0.03 1 771 267 267 GLN CA C 56.50 0.20 1 772 267 267 GLN N N 126.83 0.30 1 773 268 268 MET H H 8.69 0.03 1 774 268 268 MET CB C 32.36 0.20 1 775 268 268 MET N N 123.87 0.30 1 776 269 269 PRO CA C 61.20 0.20 1 777 270 270 LYS H H 8.21 0.03 1 778 270 270 LYS CA C 56.33 0.20 1 779 270 270 LYS CB C 32.02 0.20 1 780 270 270 LYS N N 120.52 0.30 1 781 271 271 MET H H 8.34 0.03 1 782 271 271 MET CA C 55.58 0.20 1 783 271 271 MET CB C 32.50 0.20 1 784 271 271 MET N N 126.19 0.30 1 785 272 272 ASN H H 8.50 0.03 1 786 272 272 ASN CA C 52.50 0.20 1 787 272 272 ASN CB C 37.25 0.20 1 788 272 272 ASN N N 120.40 0.30 1 789 273 273 PHE H H 9.32 0.03 1 790 273 273 PHE CA C 59.51 0.20 1 791 273 273 PHE CB C 36.88 0.20 1 792 273 273 PHE N N 129.90 0.30 1 793 274 274 ALA H H 8.47 0.03 1 794 274 274 ALA CA C 54.22 0.20 1 795 274 274 ALA CB C 16.61 0.20 1 796 274 274 ALA N N 122.36 0.30 1 797 275 275 ASN H H 7.40 0.03 1 798 275 275 ASN CA C 53.31 0.20 1 799 275 275 ASN CB C 38.15 0.20 1 800 275 275 ASN N N 112.92 0.30 1 801 276 276 VAL H H 7.13 0.03 1 802 276 276 VAL CA C 63.95 0.20 1 803 276 276 VAL CB C 32.30 0.20 1 804 276 276 VAL N N 120.10 0.30 1 805 277 277 PHE H H 7.53 0.03 1 806 277 277 PHE CA C 55.58 0.20 1 807 277 277 PHE CB C 36.37 0.20 1 808 277 277 PHE N N 120.87 0.30 1 809 278 278 ILE H H 6.83 0.03 1 810 278 278 ILE CA C 61.91 0.20 1 811 278 278 ILE CB C 36.42 0.20 1 812 278 278 ILE N N 121.03 0.30 1 813 279 279 GLY H H 8.95 0.03 1 814 279 279 GLY CA C 44.58 0.20 1 815 279 279 GLY N N 116.42 0.30 1 816 280 280 ALA H H 7.33 0.03 1 817 280 280 ALA CA C 50.75 0.20 1 818 280 280 ALA CB C 18.82 0.20 1 819 280 280 ALA N N 122.03 0.30 1 820 281 281 ASN H H 9.09 0.03 1 821 281 281 ASN CA C 50.76 0.20 1 822 281 281 ASN CB C 38.50 0.20 1 823 281 281 ASN N N 123.16 0.30 1 824 282 282 PRO CA C 64.77 0.20 1 825 282 282 PRO CB C 31.45 0.20 1 826 283 283 LEU H H 8.36 0.03 1 827 283 283 LEU CA C 56.68 0.20 1 828 283 283 LEU CB C 41.87 0.20 1 829 283 283 LEU N N 117.03 0.30 1 830 284 284 ALA H H 7.00 0.03 1 831 284 284 ALA CA C 53.58 0.20 1 832 284 284 ALA CB C 16.96 0.20 1 833 284 284 ALA N N 121.18 0.30 1 834 285 285 VAL H H 6.99 0.03 1 835 285 285 VAL CA C 66.36 0.20 1 836 285 285 VAL CB C 30.51 0.20 1 837 285 285 VAL N N 116.43 0.30 1 838 286 286 ASP H H 7.42 0.03 1 839 286 286 ASP CA C 57.34 0.20 1 840 286 286 ASP CB C 42.85 0.20 1 841 286 286 ASP N N 117.99 0.30 1 842 287 287 LEU H H 7.01 0.03 1 843 287 287 LEU CA C 57.25 0.20 1 844 287 287 LEU CB C 38.99 0.20 1 845 287 287 LEU N N 117.55 0.30 1 846 288 288 LEU H H 8.03 0.03 1 847 288 288 LEU CA C 58.44 0.20 1 848 288 288 LEU CB C 40.82 0.20 1 849 288 288 LEU N N 120.38 0.30 1 850 289 289 GLU H H 7.87 0.03 1 851 289 289 GLU CA C 58.19 0.20 1 852 289 289 GLU CB C 28.08 0.20 1 853 289 289 GLU N N 117.48 0.30 1 854 290 290 LYS H H 7.26 0.03 1 855 290 290 LYS CA C 56.83 0.20 1 856 290 290 LYS CB C 31.94 0.20 1 857 290 290 LYS N N 116.36 0.30 1 858 291 291 MET H H 7.47 0.03 1 859 291 291 MET CA C 58.17 0.20 1 860 291 291 MET CB C 34.16 0.20 1 861 291 291 MET N N 118.36 0.30 1 862 292 292 LEU H H 7.79 0.03 1 863 292 292 LEU CA C 59.06 0.20 1 864 292 292 LEU CB C 38.17 0.20 1 865 292 292 LEU N N 119.00 0.30 1 866 296 296 SER CA C 60.98 0.20 1 867 297 297 ASP H H 8.40 0.03 1 868 297 297 ASP CA C 56.08 0.20 1 869 297 297 ASP CB C 40.24 0.20 1 870 297 297 ASP N N 121.09 0.30 1 871 298 298 LYS H H 7.54 0.03 1 872 298 298 LYS CA C 54.39 0.20 1 873 298 298 LYS CB C 32.42 0.20 1 874 298 298 LYS N N 117.64 0.30 1 875 299 299 ARG H H 7.00 0.03 1 876 299 299 ARG CA C 57.03 0.20 1 877 299 299 ARG CB C 29.61 0.20 1 878 299 299 ARG N N 122.76 0.30 1 879 300 300 ILE H H 6.95 0.03 1 880 300 300 ILE CA C 61.98 0.20 1 881 300 300 ILE CB C 39.27 0.20 1 882 300 300 ILE N N 125.28 0.30 1 883 301 301 THR H H 7.32 0.03 1 884 301 301 THR CA C 59.89 0.20 1 885 301 301 THR CB C 70.71 0.20 1 886 301 301 THR N N 109.36 0.30 1 887 302 302 ALA H H 9.41 0.03 1 888 302 302 ALA CA C 55.86 0.20 1 889 302 302 ALA CB C 16.00 0.20 1 890 302 302 ALA N N 122.15 0.30 1 891 303 303 ALA H H 8.52 0.03 1 892 303 303 ALA CA C 54.83 0.20 1 893 303 303 ALA CB C 17.54 0.20 1 894 303 303 ALA N N 116.26 0.30 1 895 304 304 GLN H H 7.35 0.03 1 896 304 304 GLN CA C 57.68 0.20 1 897 304 304 GLN CB C 28.02 0.20 1 898 304 304 GLN N N 116.04 0.30 1 899 305 305 ALA H H 8.62 0.03 1 900 305 305 ALA CA C 54.60 0.20 1 901 305 305 ALA CB C 18.50 0.20 1 902 305 305 ALA N N 123.90 0.30 1 903 306 306 LEU H H 7.58 0.03 1 904 306 306 LEU CA C 57.33 0.20 1 905 306 306 LEU CB C 41.00 0.20 1 906 306 306 LEU N N 116.80 0.30 1 907 307 307 ALA H H 6.61 0.03 1 908 307 307 ALA CA C 50.65 0.20 1 909 307 307 ALA CB C 18.16 0.20 1 910 307 307 ALA N N 115.57 0.30 1 911 308 308 HIS H H 7.89 0.03 1 912 308 308 HIS CA C 58.40 0.20 1 913 308 308 HIS CB C 32.17 0.20 1 914 308 308 HIS N N 122.65 0.30 1 915 309 309 ALA H H 8.30 0.03 1 916 309 309 ALA CA C 54.92 0.20 1 917 309 309 ALA CB C 18.37 0.20 1 918 309 309 ALA N N 132.97 0.30 1 919 310 310 TYR H H 11.61 0.03 1 920 310 310 TYR CA C 59.79 0.20 1 921 310 310 TYR CB C 38.24 0.20 1 922 310 310 TYR N N 125.18 0.30 1 923 311 311 PHE H H 7.62 0.03 1 924 311 311 PHE CA C 55.54 0.20 1 925 311 311 PHE CB C 38.22 0.20 1 926 311 311 PHE N N 110.61 0.30 1 927 312 312 ALA H H 7.49 0.03 1 928 312 312 ALA CA C 55.49 0.20 1 929 312 312 ALA CB C 18.13 0.20 1 930 312 312 ALA N N 123.92 0.30 1 931 313 313 GLN H H 8.53 0.03 1 932 313 313 GLN CA C 56.85 0.20 1 933 313 313 GLN CB C 27.57 0.20 1 934 313 313 GLN N N 113.72 0.30 1 935 314 314 TYR H H 7.35 0.03 1 936 314 314 TYR CA C 58.23 0.20 1 937 314 314 TYR CB C 39.94 0.20 1 938 314 314 TYR N N 115.13 0.30 1 939 315 315 HIS H H 7.80 0.03 1 940 315 315 HIS CA C 55.57 0.20 1 941 315 315 HIS CB C 28.85 0.20 1 942 315 315 HIS N N 115.80 0.30 1 943 316 316 ASP H H 7.36 0.03 1 944 316 316 ASP CA C 50.50 0.20 1 945 316 316 ASP CB C 41.49 0.20 1 946 316 316 ASP N N 124.79 0.30 1 947 317 317 PRO CA C 63.89 0.20 1 948 317 317 PRO CB C 31.17 0.20 1 949 318 318 ASP H H 7.85 0.03 1 950 318 318 ASP CA C 54.90 0.20 1 951 318 318 ASP CB C 40.24 0.20 1 952 318 318 ASP N N 117.09 0.30 1 953 319 319 ASP H H 7.94 0.03 1 954 319 319 ASP CA C 52.18 0.20 1 955 319 319 ASP CB C 41.78 0.20 1 956 319 319 ASP N N 120.95 0.30 1 957 320 320 GLU H H 7.76 0.03 1 958 320 320 GLU CA C 53.25 0.20 1 959 320 320 GLU CB C 28.82 0.20 1 960 320 320 GLU N N 121.63 0.30 1 961 321 321 PRO CA C 63.22 0.20 1 962 322 322 VAL H H 7.78 0.03 1 963 322 322 VAL CA C 59.25 0.20 1 964 322 322 VAL CB C 33.35 0.20 1 965 322 322 VAL N N 108.68 0.30 1 966 323 323 ALA H H 8.41 0.03 1 967 323 323 ALA CA C 50.52 0.20 1 968 323 323 ALA CB C 19.38 0.20 1 969 323 323 ALA N N 123.47 0.30 1 970 324 324 ASP H H 8.01 0.03 1 971 324 324 ASP CA C 52.66 0.20 1 972 324 324 ASP CB C 38.80 0.20 1 973 324 324 ASP N N 121.06 0.30 1 974 326 326 TYR CA C 58.82 0.20 1 975 327 327 ASP H H 6.90 0.03 1 976 327 327 ASP CA C 53.88 0.20 1 977 327 327 ASP CB C 41.10 0.20 1 978 327 327 ASP N N 123.00 0.30 1 979 331 331 GLU H H 9.79 0.03 1 980 331 331 GLU CA C 58.24 0.20 1 981 331 331 GLU N N 114.74 0.30 1 982 332 332 SER H H 7.39 0.03 1 983 332 332 SER CA C 57.77 0.20 1 984 332 332 SER CB C 62.78 0.20 1 985 332 332 SER N N 111.91 0.30 1 986 333 333 ARG H H 7.55 0.03 1 987 333 333 ARG CA C 55.87 0.20 1 988 333 333 ARG CB C 30.30 0.20 1 989 333 333 ARG N N 121.97 0.30 1 990 334 334 ASP H H 8.49 0.03 1 991 334 334 ASP CA C 53.04 0.20 1 992 334 334 ASP CB C 40.45 0.20 1 993 334 334 ASP N N 124.61 0.30 1 994 335 335 LEU H H 7.73 0.03 1 995 335 335 LEU CA C 52.42 0.20 1 996 335 335 LEU CB C 41.14 0.20 1 997 335 335 LEU N N 123.12 0.30 1 998 336 336 LEU H H 8.69 0.03 1 999 336 336 LEU CA C 53.65 0.20 1 1000 336 336 LEU CB C 41.32 0.20 1 1001 336 336 LEU N N 119.87 0.30 1 1002 337 337 ILE H H 8.89 0.03 1 1003 337 337 ILE CA C 66.56 0.20 1 1004 337 337 ILE CB C 37.49 0.20 1 1005 337 337 ILE N N 121.75 0.30 1 1006 338 338 ASP H H 8.31 0.03 1 1007 338 338 ASP CA C 56.86 0.20 1 1008 338 338 ASP CB C 39.53 0.20 1 1009 338 338 ASP N N 115.96 0.30 1 1010 339 339 GLU H H 7.03 0.03 1 1011 339 339 GLU CA C 58.09 0.20 1 1012 339 339 GLU CB C 29.21 0.20 1 1013 339 339 GLU N N 120.53 0.30 1 1014 340 340 TRP H H 7.62 0.03 1 1015 340 340 TRP CA C 59.78 0.20 1 1016 340 340 TRP CB C 29.88 0.20 1 1017 340 340 TRP N N 119.63 0.30 1 1018 341 341 LYS H H 8.68 0.03 1 1019 341 341 LYS CA C 59.99 0.20 1 1020 341 341 LYS CB C 31.36 0.20 1 1021 341 341 LYS N N 121.44 0.30 1 1022 342 342 SER H H 7.57 0.03 1 1023 342 342 SER CA C 60.86 0.20 1 1024 342 342 SER CB C 61.88 0.20 1 1025 342 342 SER N N 114.64 0.30 1 1026 343 343 LEU H H 7.87 0.03 1 1027 343 343 LEU CA C 57.28 0.20 1 1028 343 343 LEU CB C 41.18 0.20 1 1029 343 343 LEU N N 120.42 0.30 1 1030 344 344 THR CA C 67.98 0.20 1 1031 345 345 TYR H H 8.74 0.03 1 1032 345 345 TYR CA C 61.65 0.20 1 1033 345 345 TYR CB C 37.28 0.20 1 1034 345 345 TYR N N 124.93 0.30 1 1035 346 346 ASP H H 7.99 0.03 1 1036 346 346 ASP CA C 56.84 0.20 1 1037 346 346 ASP CB C 39.74 0.20 1 1038 346 346 ASP N N 117.45 0.30 1 1039 347 347 GLU H H 7.43 0.03 1 1040 347 347 GLU CA C 57.51 0.20 1 1041 347 347 GLU CB C 28.84 0.20 1 1042 347 347 GLU N N 118.39 0.30 1 1043 348 348 VAL H H 8.00 0.03 1 1044 348 348 VAL CA C 65.75 0.20 1 1045 348 348 VAL CB C 31.19 0.20 1 1046 348 348 VAL N N 121.22 0.30 1 1047 349 349 ILE H H 8.04 0.03 1 1048 349 349 ILE CA C 62.87 0.20 1 1049 349 349 ILE CB C 36.22 0.20 1 1050 349 349 ILE N N 114.73 0.30 1 1051 350 350 SER H H 7.33 0.03 1 1052 350 350 SER CA C 57.76 0.20 1 1053 350 350 SER CB C 63.15 0.20 1 1054 350 350 SER N N 113.27 0.30 1 1055 351 351 PHE H H 7.22 0.03 1 1056 351 351 PHE CA C 60.23 0.20 1 1057 351 351 PHE CB C 39.23 0.20 1 1058 351 351 PHE N N 124.97 0.30 1 1059 352 352 VAL H H 6.83 0.03 1 1060 352 352 VAL CA C 63.14 0.20 1 1061 352 352 VAL CB C 33.64 0.20 1 1062 352 352 VAL N N 130.06 0.30 1 stop_ save_