data_27273 ####################### # 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 ; _BMRB_accession_number 27273 _BMRB_flat_file_name bmr27273.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" 268 "13C chemical shifts" 550 "15N chemical shifts" 268 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' 27274 'phosphorylated (T183 and Y185) p38 alpha in complex with an MKK3bKIM peptide' 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-p38 alpha' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'dp-p38 alpha' $dp-p38_alpha stop_ _System_molecular_weight 40450 _System_physical_state native _System_oligomer_state ? _System_paramagnetic no _System_thiol_state . loop_ _Biological_function kinase stop_ _Database_query_date . _Details 'Monomer; No ligand bound' 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' . . . . . stop_ 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]' 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_ _Software_label $TOPSPIN $Sparky stop_ 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 55.11 0.20 1 2 3 3 MET CB C 31.65 0.20 1 3 4 4 GLY H H 8.32 0.03 1 4 4 4 GLY CA C 44.73 0.20 1 5 4 4 GLY N N 110.75 0.30 1 6 5 5 SER H H 8.12 0.03 1 7 5 5 SER CA C 57.82 0.20 1 8 5 5 SER CB C 63.33 0.20 1 9 5 5 SER N N 116.29 0.30 1 10 6 6 GLN H H 8.38 0.03 1 11 6 6 GLN CA C 55.34 0.20 1 12 6 6 GLN CB C 28.47 0.20 1 13 6 6 GLN N N 122.28 0.30 1 14 7 7 GLU H H 8.27 0.03 1 15 7 7 GLU CA C 55.78 0.20 1 16 7 7 GLU CB C 29.10 0.20 1 17 7 7 GLU N N 122.64 0.30 1 18 8 8 ARG H H 8.34 0.03 1 19 8 8 ARG CA C 53.61 0.20 1 20 8 8 ARG CB C 29.57 0.20 1 21 8 8 ARG N N 125.43 0.30 1 22 9 9 PRO CA C 62.23 0.20 1 23 9 9 PRO CB C 31.42 0.20 1 24 10 10 THR H H 8.43 0.03 1 25 10 10 THR CA C 62.76 0.20 1 26 10 10 THR CB C 69.01 0.20 1 27 10 10 THR N N 117.58 0.30 1 28 11 11 PHE H H 8.74 0.03 1 29 11 11 PHE CA C 56.52 0.20 1 30 11 11 PHE CB C 41.03 0.20 1 31 11 11 PHE N N 127.39 0.30 1 32 12 12 TYR H H 9.07 0.03 1 33 12 12 TYR CA C 55.55 0.20 1 34 12 12 TYR CB C 40.14 0.20 1 35 12 12 TYR N N 120.24 0.30 1 36 13 13 ARG H H 8.39 0.03 1 37 13 13 ARG CA C 53.97 0.20 1 38 13 13 ARG CB C 32.80 0.20 1 39 13 13 ARG N N 120.22 0.30 1 40 14 14 GLN H H 8.90 0.03 1 41 14 14 GLN CA C 54.42 0.20 1 42 14 14 GLN CB C 32.20 0.20 1 43 14 14 GLN N N 122.50 0.30 1 44 15 15 GLU H H 8.79 0.03 1 45 15 15 GLU CA C 54.94 0.20 1 46 15 15 GLU CB C 29.70 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 53.53 0.20 1 50 16 16 LEU CB C 43.68 0.20 1 51 16 16 LEU N N 128.75 0.30 1 52 17 17 ASN H H 7.24 0.03 1 53 17 17 ASN CA C 53.82 0.20 1 54 17 17 ASN CB C 36.46 0.20 1 55 17 17 ASN N N 116.34 0.30 1 56 18 18 LYS H H 8.82 0.03 1 57 18 18 LYS CA C 57.38 0.20 1 58 18 18 LYS CB C 28.87 0.20 1 59 18 18 LYS N N 110.08 0.30 1 60 19 19 THR H H 7.79 0.03 1 61 19 19 THR CA C 60.97 0.20 1 62 19 19 THR CB C 70.87 0.20 1 63 19 19 THR N N 115.84 0.30 1 64 20 20 ILE H H 8.55 0.03 1 65 20 20 ILE CA C 59.77 0.20 1 66 20 20 ILE CB C 35.78 0.20 1 67 20 20 ILE N N 125.56 0.30 1 68 21 21 TRP H H 9.22 0.03 1 69 21 21 TRP CA C 56.51 0.20 1 70 21 21 TRP CB C 28.49 0.20 1 71 21 21 TRP N N 131.19 0.30 1 72 22 22 GLU H H 8.22 0.03 1 73 22 22 GLU CA C 54.47 0.20 1 74 22 22 GLU CB C 30.44 0.20 1 75 22 22 GLU N N 128.36 0.30 1 76 23 23 VAL H H 7.58 0.03 1 77 23 23 VAL CA C 55.84 0.20 1 78 23 23 VAL CB C 33.32 0.20 1 79 23 23 VAL N N 112.53 0.30 1 80 24 24 PRO CA C 61.44 0.20 1 81 24 24 PRO CB C 31.33 0.20 1 82 25 25 GLU H H 8.06 0.03 1 83 25 25 GLU CA C 58.12 0.20 1 84 25 25 GLU CB C 28.73 0.20 1 85 25 25 GLU N N 119.04 0.30 1 86 26 26 ARG H H 7.41 0.03 1 87 26 26 ARG CA C 57.52 0.20 1 88 26 26 ARG CB C 29.55 0.20 1 89 26 26 ARG N N 117.71 0.30 1 90 27 27 TYR H H 7.72 0.03 1 91 27 27 TYR CA C 56.97 0.20 1 92 27 27 TYR CB C 36.87 0.20 1 93 27 27 TYR N N 118.29 0.30 1 94 28 28 GLN H H 9.13 0.03 1 95 28 28 GLN CA C 53.16 0.20 1 96 28 28 GLN CB C 32.48 0.20 1 97 28 28 GLN N N 122.61 0.30 1 98 29 29 ASN H H 8.76 0.03 1 99 29 29 ASN CA C 53.15 0.20 1 100 29 29 ASN CB C 36.26 0.20 1 101 29 29 ASN N N 117.63 0.30 1 102 30 30 LEU H H 8.49 0.03 1 103 30 30 LEU CA C 56.62 0.20 1 104 30 30 LEU CB C 40.68 0.20 1 105 30 30 LEU N N 120.39 0.30 1 106 31 31 SER H H 8.69 0.03 1 107 31 31 SER CA C 54.18 0.20 1 108 31 31 SER CB C 64.27 0.20 1 109 31 31 SER N N 116.18 0.30 1 110 32 32 PRO CA C 64.03 0.20 1 111 32 32 PRO CB C 31.49 0.20 1 112 33 33 VAL H H 8.56 0.03 1 113 33 33 VAL CA C 61.65 0.20 1 114 33 33 VAL CB C 33.26 0.20 1 115 33 33 VAL N N 121.08 0.30 1 116 34 34 GLY H H 7.74 0.03 1 117 34 34 GLY CA C 45.01 0.20 1 118 34 34 GLY N N 108.69 0.30 1 119 35 35 SER H H 8.35 0.03 1 120 35 35 SER CA C 57.61 0.20 1 121 35 35 SER CB C 64.43 0.20 1 122 35 35 SER N N 115.52 0.30 1 123 36 36 GLY H H 8.11 0.03 1 124 36 36 GLY CA C 44.28 0.20 1 125 36 36 GLY N N 110.65 0.30 1 126 37 37 ALA H H 8.38 0.03 1 127 37 37 ALA CA C 53.42 0.20 1 128 37 37 ALA CB C 17.64 0.20 1 129 37 37 ALA N N 124.35 0.30 1 130 38 38 TYR H H 8.00 0.03 1 131 38 38 TYR CA C 56.83 0.20 1 132 38 38 TYR N N 113.98 0.30 1 133 39 39 GLY H H 7.26 0.03 1 134 39 39 GLY CA C 45.07 0.20 1 135 39 39 GLY N N 108.52 0.30 1 136 40 40 SER H H 8.07 0.03 1 137 40 40 SER CA C 57.54 0.20 1 138 40 40 SER CB C 64.76 0.20 1 139 40 40 SER N N 116.11 0.30 1 140 41 41 VAL H H 8.61 0.03 1 141 41 41 VAL CA C 61.08 0.20 1 142 41 41 VAL CB C 34.41 0.20 1 143 41 41 VAL N N 122.73 0.30 1 144 42 42 CYS H H 9.20 0.03 1 145 42 42 CYS CA C 57.60 0.20 1 146 42 42 CYS CB C 30.44 0.20 1 147 42 42 CYS N N 125.46 0.30 1 148 43 43 ALA H H 8.73 0.03 1 149 43 43 ALA CA C 50.20 0.20 1 150 43 43 ALA CB C 19.86 0.20 1 151 43 43 ALA N N 125.78 0.30 1 152 44 44 ALA H H 8.96 0.03 1 153 44 44 ALA CA C 50.10 0.20 1 154 44 44 ALA CB C 22.28 0.20 1 155 44 44 ALA N N 120.73 0.30 1 156 45 45 PHE H H 9.15 0.03 1 157 45 45 PHE CA C 56.81 0.20 1 158 45 45 PHE CB C 40.27 0.20 1 159 45 45 PHE N N 122.42 0.30 1 160 46 46 ASP H H 8.26 0.03 1 161 46 46 ASP CA C 51.37 0.20 1 162 46 46 ASP CB C 40.80 0.20 1 163 46 46 ASP N N 126.10 0.30 1 164 47 47 THR H H 8.86 0.03 1 165 47 47 THR CA C 63.41 0.20 1 166 47 47 THR CB C 68.85 0.20 1 167 47 47 THR N N 117.46 0.30 1 168 48 48 LYS H H 7.83 0.03 1 169 48 48 LYS CA C 58.28 0.20 1 170 48 48 LYS CB C 31.58 0.20 1 171 48 48 LYS N N 121.91 0.30 1 172 49 49 THR H H 6.51 0.03 1 173 49 49 THR CA C 61.28 0.20 1 174 49 49 THR CB C 70.50 0.20 1 175 49 49 THR N N 105.12 0.30 1 176 50 50 GLY H H 8.31 0.03 1 177 50 50 GLY CA C 45.41 0.20 1 178 50 50 GLY N N 112.46 0.30 1 179 51 51 LEU H H 7.04 0.03 1 180 51 51 LEU CA C 53.20 0.20 1 181 51 51 LEU CB C 43.15 0.20 1 182 51 51 LEU N N 119.76 0.30 1 183 52 52 ARG H H 8.16 0.03 1 184 52 52 ARG CA C 55.56 0.20 1 185 52 52 ARG CB C 29.35 0.20 1 186 52 52 ARG N N 119.80 0.30 1 187 53 53 VAL H H 8.75 0.03 1 188 53 53 VAL CA C 59.12 0.20 1 189 53 53 VAL CB C 34.51 0.20 1 190 53 53 VAL N N 116.89 0.30 1 191 54 54 ALA H H 8.75 0.03 1 192 54 54 ALA CA C 49.50 0.20 1 193 54 54 ALA CB C 19.40 0.20 1 194 54 54 ALA N N 122.80 0.30 1 195 55 55 VAL H H 9.19 0.03 1 196 55 55 VAL CA C 60.40 0.20 1 197 55 55 VAL CB C 31.90 0.20 1 198 55 55 VAL N N 122.61 0.30 1 199 56 56 LYS H H 9.50 0.03 1 200 56 56 LYS CA C 53.54 0.20 1 201 56 56 LYS CB C 34.22 0.20 1 202 56 56 LYS N N 129.37 0.30 1 203 57 57 LYS H H 8.52 0.03 1 204 57 57 LYS CA C 53.89 0.20 1 205 57 57 LYS CB C 32.75 0.20 1 206 57 57 LYS N N 128.45 0.30 1 207 58 58 LEU H H 7.93 0.03 1 208 58 58 LEU CA C 54.77 0.20 1 209 58 58 LEU CB C 39.10 0.20 1 210 58 58 LEU N N 128.63 0.30 1 211 59 59 SER H H 7.98 0.03 1 212 59 59 SER CA C 57.05 0.20 1 213 59 59 SER CB C 62.73 0.20 1 214 59 59 SER N N 118.02 0.30 1 215 60 60 ARG H H 8.65 0.03 1 216 60 60 ARG CA C 55.59 0.20 1 217 60 60 ARG CB C 28.59 0.20 1 218 60 60 ARG N N 122.93 0.30 1 219 61 61 PRO CA C 63.90 0.20 1 220 61 61 PRO CB C 30.82 0.20 1 221 62 62 PHE H H 7.84 0.03 1 222 62 62 PHE CA C 53.99 0.20 1 223 62 62 PHE CB C 37.28 0.20 1 224 62 62 PHE N N 112.26 0.30 1 225 63 63 GLN H H 6.91 0.03 1 226 63 63 GLN CA C 57.25 0.20 1 227 63 63 GLN CB C 28.76 0.20 1 228 63 63 GLN N N 116.02 0.30 1 229 64 64 SER H H 7.38 0.03 1 230 64 64 SER CA C 56.34 0.20 1 231 64 64 SER CB C 65.89 0.20 1 232 64 64 SER N N 110.38 0.30 1 233 65 65 ILE H H 9.13 0.03 1 234 65 65 ILE CA C 65.33 0.20 1 235 65 65 ILE CB C 36.96 0.20 1 236 65 65 ILE N N 122.68 0.30 1 237 66 66 ILE H H 7.51 0.03 1 238 66 66 ILE CA C 63.78 0.20 1 239 66 66 ILE CB C 36.63 0.20 1 240 66 66 ILE N N 119.06 0.30 1 241 67 67 HIS CA C 60.44 0.20 1 242 68 68 ALA H H 8.54 0.03 1 243 68 68 ALA CA C 54.62 0.20 1 244 68 68 ALA CB C 18.38 0.20 1 245 68 68 ALA N N 123.40 0.30 1 246 69 69 LYS H H 7.76 0.03 1 247 69 69 LYS CA C 59.12 0.20 1 248 69 69 LYS CB C 31.13 0.20 1 249 69 69 LYS N N 118.34 0.30 1 250 70 70 ARG H H 7.40 0.03 1 251 70 70 ARG CA C 59.02 0.20 1 252 70 70 ARG CB C 28.77 0.20 1 253 70 70 ARG N N 119.42 0.30 1 254 71 71 THR H H 8.38 0.03 1 255 71 71 THR CA C 66.59 0.20 1 256 71 71 THR CB C 67.81 0.20 1 257 71 71 THR N N 120.38 0.30 1 258 72 72 TYR H H 7.51 0.03 1 259 72 72 TYR CA C 62.11 0.20 1 260 72 72 TYR CB C 37.18 0.20 1 261 72 72 TYR N N 121.55 0.30 1 262 81 81 MET CA C 55.18 0.20 1 263 82 82 LYS H H 8.44 0.03 1 264 82 82 LYS CA C 54.20 0.20 1 265 82 82 LYS CB C 31.90 0.20 1 266 82 82 LYS N N 128.68 0.30 1 267 83 83 HIS H H 8.64 0.03 1 268 83 83 HIS CA C 56.94 0.20 1 269 83 83 HIS CB C 32.53 0.20 1 270 83 83 HIS N N 124.67 0.30 1 271 84 84 GLU H H 7.97 0.03 1 272 84 84 GLU CA C 59.11 0.20 1 273 84 84 GLU CB C 29.15 0.20 1 274 84 84 GLU N N 125.64 0.30 1 275 85 85 ASN H H 11.29 0.03 1 276 85 85 ASN CA C 53.21 0.20 1 277 85 85 ASN CB C 40.33 0.20 1 278 85 85 ASN N N 118.08 0.30 1 279 86 86 VAL H H 7.62 0.03 1 280 86 86 VAL CA C 61.17 0.20 1 281 86 86 VAL CB C 35.26 0.20 1 282 86 86 VAL N N 119.95 0.30 1 283 87 87 ILE H H 8.32 0.03 1 284 87 87 ILE CA C 61.04 0.20 1 285 87 87 ILE CB C 37.82 0.20 1 286 87 87 ILE N N 129.61 0.30 1 287 88 88 GLY H H 7.54 0.03 1 288 88 88 GLY CA C 43.04 0.20 1 289 88 88 GLY N N 109.54 0.30 1 290 89 89 LEU H H 8.16 0.03 1 291 89 89 LEU CA C 54.09 0.20 1 292 89 89 LEU N N 121.35 0.30 1 293 90 90 LEU H H 8.91 0.03 1 294 90 90 LEU CA C 55.31 0.20 1 295 90 90 LEU CB C 42.28 0.20 1 296 90 90 LEU N N 126.65 0.30 1 297 91 91 ASP CA C 52.39 0.20 1 298 91 91 ASP CB C 41.66 0.20 1 299 92 92 VAL H H 7.78 0.03 1 300 92 92 VAL CA C 59.23 0.20 1 301 92 92 VAL CB C 32.80 0.20 1 302 92 92 VAL N N 120.44 0.30 1 303 93 93 PHE H H 8.18 0.03 1 304 93 93 PHE CA C 55.57 0.20 1 305 93 93 PHE CB C 40.87 0.20 1 306 93 93 PHE N N 119.17 0.30 1 307 94 94 THR H H 8.88 0.03 1 308 94 94 THR CA C 56.90 0.20 1 309 94 94 THR CB C 71.85 0.20 1 310 94 94 THR N N 113.58 0.30 1 311 95 95 PRO CA C 62.20 0.20 1 312 95 95 PRO CB C 30.42 0.20 1 313 96 96 ALA H H 7.63 0.03 1 314 96 96 ALA CA C 52.38 0.20 1 315 96 96 ALA CB C 19.90 0.20 1 316 96 96 ALA N N 122.45 0.30 1 317 97 97 ARG H H 9.20 0.03 1 318 97 97 ARG CA C 55.58 0.20 1 319 97 97 ARG CB C 29.68 0.20 1 320 97 97 ARG N N 121.26 0.30 1 321 98 98 SER H H 7.31 0.03 1 322 98 98 SER CA C 56.14 0.20 1 323 98 98 SER CB C 65.14 0.20 1 324 98 98 SER N N 111.46 0.30 1 325 99 99 LEU H H 8.41 0.03 1 326 99 99 LEU CA C 56.54 0.20 1 327 99 99 LEU CB C 40.16 0.20 1 328 99 99 LEU N N 122.53 0.30 1 329 100 100 GLU H H 8.24 0.03 1 330 100 100 GLU CA C 59.10 0.20 1 331 100 100 GLU CB C 27.98 0.20 1 332 100 100 GLU N N 117.50 0.30 1 333 101 101 GLU H H 6.95 0.03 1 334 101 101 GLU CA C 54.40 0.20 1 335 101 101 GLU CB C 30.10 0.20 1 336 101 101 GLU N N 115.50 0.30 1 337 102 102 PHE H H 7.22 0.03 1 338 102 102 PHE CA C 56.43 0.20 1 339 102 102 PHE CB C 37.90 0.20 1 340 102 102 PHE N N 122.29 0.30 1 341 103 103 ASN H H 8.47 0.03 1 342 103 103 ASN CA C 53.66 0.20 1 343 103 103 ASN CB C 41.46 0.20 1 344 103 103 ASN N N 125.67 0.30 1 345 104 104 ASP H H 7.56 0.03 1 346 104 104 ASP CA C 52.79 0.20 1 347 104 104 ASP CB C 43.86 0.20 1 348 104 104 ASP N N 115.95 0.30 1 349 105 105 VAL H H 8.40 0.03 1 350 105 105 VAL CA C 61.38 0.20 1 351 105 105 VAL CB C 34.81 0.20 1 352 105 105 VAL N N 121.29 0.30 1 353 106 106 TYR H H 8.01 0.03 1 354 106 106 TYR CA C 54.61 0.20 1 355 106 106 TYR CB C 39.25 0.20 1 356 106 106 TYR N N 124.78 0.30 1 357 107 107 LEU H H 8.77 0.03 1 358 107 107 LEU CA C 52.97 0.20 1 359 107 107 LEU CB C 43.73 0.20 1 360 107 107 LEU N N 119.72 0.30 1 361 108 108 VAL CA C 60.60 0.20 1 362 108 108 VAL CB C 32.24 0.20 1 363 109 109 THR H H 8.96 0.03 1 364 109 109 THR CA C 59.17 0.20 1 365 109 109 THR CB C 72.99 0.20 1 366 109 109 THR N N 118.24 0.30 1 367 110 110 HIS H H 8.84 0.03 1 368 110 110 HIS CA C 58.69 0.20 1 369 110 110 HIS CB C 31.08 0.20 1 370 110 110 HIS N N 119.72 0.30 1 371 111 111 LEU H H 8.12 0.03 1 372 111 111 LEU CA C 54.07 0.20 1 373 111 111 LEU CB C 41.41 0.20 1 374 111 111 LEU N N 125.34 0.30 1 375 112 112 MET H H 8.68 0.03 1 376 112 112 MET CA C 54.84 0.20 1 377 112 112 MET N N 126.43 0.30 1 378 113 113 GLY H H 8.05 0.03 1 379 113 113 GLY CA C 45.31 0.20 1 380 113 113 GLY N N 108.51 0.30 1 381 114 114 ALA H H 7.79 0.03 1 382 114 114 ALA CA C 50.92 0.20 1 383 114 114 ALA CB C 20.09 0.20 1 384 114 114 ALA N N 123.91 0.30 1 385 115 115 ASP H H 7.91 0.03 1 386 115 115 ASP CA C 51.89 0.20 1 387 115 115 ASP CB C 41.81 0.20 1 388 115 115 ASP N N 118.44 0.30 1 389 116 116 LEU H H 7.74 0.03 1 390 116 116 LEU CA C 56.97 0.20 1 391 116 116 LEU CB C 41.17 0.20 1 392 116 116 LEU N N 117.87 0.30 1 393 117 117 ASN H H 7.57 0.03 1 394 117 117 ASN CA C 55.67 0.20 1 395 117 117 ASN CB C 37.40 0.20 1 396 117 117 ASN N N 115.84 0.30 1 397 118 118 ASN H H 7.90 0.03 1 398 118 118 ASN CA C 56.05 0.20 1 399 118 118 ASN CB C 38.97 0.20 1 400 118 118 ASN N N 118.36 0.30 1 401 119 119 ILE H H 7.42 0.03 1 402 119 119 ILE CA C 62.85 0.20 1 403 119 119 ILE CB C 36.12 0.20 1 404 119 119 ILE N N 118.83 0.30 1 405 120 120 VAL H H 7.47 0.03 1 406 120 120 VAL CA C 64.20 0.20 1 407 120 120 VAL CB C 30.98 0.20 1 408 120 120 VAL N N 116.64 0.30 1 409 121 121 LYS H H 7.31 0.03 1 410 121 121 LYS CA C 57.29 0.20 1 411 121 121 LYS CB C 31.61 0.20 1 412 121 121 LYS N N 117.49 0.30 1 413 122 122 CYS H H 7.57 0.03 1 414 122 122 CYS CA C 59.52 0.20 1 415 122 122 CYS CB C 28.62 0.20 1 416 122 122 CYS N N 114.53 0.30 1 417 123 123 GLN H H 7.95 0.03 1 418 123 123 GLN CA C 54.44 0.20 1 419 123 123 GLN CB C 29.90 0.20 1 420 123 123 GLN N N 119.69 0.30 1 421 124 124 LYS H H 8.17 0.03 1 422 124 124 LYS CA C 54.77 0.20 1 423 124 124 LYS CB C 30.81 0.20 1 424 124 124 LYS N N 122.01 0.30 1 425 125 125 LEU H H 8.49 0.03 1 426 125 125 LEU CA C 54.07 0.20 1 427 125 125 LEU CB C 41.67 0.20 1 428 125 125 LEU N N 126.86 0.30 1 429 126 126 THR CA C 60.21 0.20 1 430 127 127 ASP H H 8.90 0.03 1 431 127 127 ASP CA C 58.08 0.20 1 432 127 127 ASP CB C 41.99 0.20 1 433 127 127 ASP N N 120.83 0.30 1 434 128 128 ASP H H 7.88 0.03 1 435 128 128 ASP CA C 57.05 0.20 1 436 128 128 ASP CB C 39.66 0.20 1 437 128 128 ASP N N 115.51 0.30 1 438 129 129 HIS H H 7.44 0.03 1 439 129 129 HIS CA C 59.67 0.20 1 440 129 129 HIS CB C 31.37 0.20 1 441 129 129 HIS N N 119.53 0.30 1 442 130 130 VAL H H 8.08 0.03 1 443 130 130 VAL CA C 68.18 0.20 1 444 130 130 VAL CB C 29.89 0.20 1 445 130 130 VAL N N 120.16 0.30 1 446 131 131 GLN H H 8.33 0.03 1 447 131 131 GLN CA C 59.02 0.20 1 448 131 131 GLN CB C 29.30 0.20 1 449 131 131 GLN N N 118.33 0.30 1 450 132 132 PHE H H 7.37 0.03 1 451 132 132 PHE CA C 58.12 0.20 1 452 132 132 PHE CB C 39.00 0.20 1 453 132 132 PHE N N 116.38 0.30 1 454 133 133 LEU H H 8.72 0.03 1 455 133 133 LEU CA C 58.20 0.20 1 456 133 133 LEU CB C 41.59 0.20 1 457 133 133 LEU N N 120.78 0.30 1 458 139 139 ARG CA C 59.97 0.20 1 459 139 139 ARG CB C 28.97 0.20 1 460 140 140 GLY H H 8.05 0.03 1 461 140 140 GLY CA C 46.45 0.20 1 462 140 140 GLY N N 107.23 0.30 1 463 141 141 LEU H H 8.61 0.03 1 464 141 141 LEU CA C 56.32 0.20 1 465 141 141 LEU CB C 40.44 0.20 1 466 141 141 LEU N N 121.69 0.30 1 467 142 142 LYS H H 8.62 0.03 1 468 142 142 LYS CA C 59.41 0.20 1 469 142 142 LYS CB C 31.35 0.20 1 470 142 142 LYS N N 119.45 0.30 1 471 143 143 TYR H H 6.75 0.03 1 472 143 143 TYR CA C 61.45 0.20 1 473 143 143 TYR CB C 37.23 0.20 1 474 143 143 TYR N N 118.27 0.30 1 475 144 144 ILE H H 8.37 0.03 1 476 144 144 ILE CA C 66.42 0.20 1 477 144 144 ILE CB C 37.31 0.20 1 478 144 144 ILE N N 120.28 0.30 1 479 145 145 HIS H H 9.44 0.03 1 480 145 145 HIS CA C 56.90 0.20 1 481 145 145 HIS CB C 30.26 0.20 1 482 145 145 HIS N N 119.69 0.30 1 483 146 146 SER H H 7.79 0.03 1 484 146 146 SER CA C 60.89 0.20 1 485 146 146 SER CB C 62.12 0.20 1 486 146 146 SER N N 116.63 0.30 1 487 147 147 ALA H H 7.35 0.03 1 488 147 147 ALA CA C 50.91 0.20 1 489 147 147 ALA CB C 17.25 0.20 1 490 147 147 ALA N N 126.39 0.30 1 491 148 148 ASP H H 8.14 0.03 1 492 148 148 ASP CA C 55.12 0.20 1 493 148 148 ASP CB C 38.45 0.20 1 494 148 148 ASP N N 115.24 0.30 1 495 149 149 ILE H H 7.17 0.03 1 496 149 149 ILE CA C 58.89 0.20 1 497 149 149 ILE CB C 38.36 0.20 1 498 149 149 ILE N N 119.09 0.30 1 499 150 150 ILE H H 7.77 0.03 1 500 150 150 ILE CA C 59.74 0.20 1 501 150 150 ILE CB C 39.86 0.20 1 502 150 150 ILE N N 123.19 0.30 1 503 151 151 HIS H H 7.31 0.03 1 504 151 151 HIS CA C 62.34 0.20 1 505 151 151 HIS CB C 35.34 0.20 1 506 151 151 HIS N N 121.10 0.30 1 507 157 157 SER H H 7.65 0.03 1 508 157 157 SER CA C 59.42 0.20 1 509 157 157 SER N N 106.89 0.30 1 510 158 158 ASN H H 7.72 0.03 1 511 158 158 ASN CA C 51.95 0.20 1 512 158 158 ASN CB C 37.35 0.20 1 513 158 158 ASN N N 119.06 0.30 1 514 159 159 LEU H H 6.99 0.03 1 515 159 159 LEU CA C 52.60 0.20 1 516 159 159 LEU CB C 42.40 0.20 1 517 159 159 LEU N N 119.25 0.30 1 518 160 160 ALA H H 8.47 0.03 1 519 160 160 ALA CA C 50.21 0.20 1 520 160 160 ALA CB C 20.82 0.20 1 521 160 160 ALA N N 125.58 0.30 1 522 161 161 VAL H H 8.11 0.03 1 523 161 161 VAL CA C 59.15 0.20 1 524 161 161 VAL CB C 35.15 0.20 1 525 161 161 VAL N N 117.83 0.30 1 526 162 162 ASN H H 7.83 0.03 1 527 162 162 ASN CA C 49.97 0.20 1 528 162 162 ASN CB C 39.08 0.20 1 529 162 162 ASN N N 122.32 0.30 1 530 163 163 GLU H H 8.76 0.03 1 531 163 163 GLU CA C 58.71 0.20 1 532 163 163 GLU CB C 28.10 0.20 1 533 163 163 GLU N N 117.55 0.30 1 534 164 164 ASP H H 7.45 0.03 1 535 164 164 ASP CA C 53.96 0.20 1 536 164 164 ASP CB C 40.73 0.20 1 537 164 164 ASP N N 118.75 0.30 1 538 165 165 CYS H H 8.23 0.03 1 539 165 165 CYS CA C 62.20 0.20 1 540 165 165 CYS CB C 24.47 0.20 1 541 165 165 CYS N N 111.42 0.30 1 542 166 166 GLU H H 7.59 0.03 1 543 166 166 GLU CA C 55.74 0.20 1 544 166 166 GLU CB C 28.18 0.20 1 545 166 166 GLU N N 117.77 0.30 1 546 167 167 LEU H H 7.90 0.03 1 547 167 167 LEU CA C 53.25 0.20 1 548 167 167 LEU CB C 45.38 0.20 1 549 167 167 LEU N N 125.38 0.30 1 550 168 168 LYS H H 8.91 0.03 1 551 168 168 LYS CA C 54.59 0.20 1 552 168 168 LYS CB C 37.22 0.20 1 553 168 168 LYS N N 122.69 0.30 1 554 169 169 ILE H H 8.15 0.03 1 555 169 169 ILE CA C 62.22 0.20 1 556 169 169 ILE CB C 39.03 0.20 1 557 169 169 ILE N N 122.09 0.30 1 558 170 170 LEU H H 8.42 0.03 1 559 170 170 LEU CA C 54.00 0.20 1 560 170 170 LEU N N 125.31 0.30 1 561 174 174 LEU CA C 54.27 0.20 1 562 174 174 LEU CB C 40.15 0.20 1 563 175 175 ALA H H 8.02 0.03 1 564 175 175 ALA CA C 59.68 0.20 1 565 175 175 ALA N N 119.20 0.30 1 566 176 176 ARG H H 8.35 0.03 1 567 176 176 ARG CA C 55.25 0.20 1 568 176 176 ARG CB C 37.00 0.20 1 569 176 176 ARG N N 117.14 0.30 1 570 178 178 THR H H 7.22 0.03 1 571 178 178 THR CA C 56.04 0.20 1 572 178 178 THR CB C 63.37 0.20 1 573 178 178 THR N N 115.66 0.30 1 574 179 179 ASP CA C 54.72 0.20 1 575 180 180 ASP H H 8.08 0.03 1 576 180 180 ASP CA C 54.52 0.20 1 577 180 180 ASP CB C 40.66 0.20 1 578 180 180 ASP N N 120.23 0.30 1 579 181 181 GLU H H 8.02 0.03 1 580 181 181 GLU CA C 57.56 0.20 1 581 181 181 GLU CB C 29.22 0.20 1 582 181 181 GLU N N 121.20 0.30 1 583 182 182 MET H H 7.99 0.03 1 584 182 182 MET CA C 55.95 0.20 1 585 182 182 MET N N 120.22 0.30 1 586 183 183 TPO H H 8.66 0.03 1 587 183 183 TPO CA C 62.62 0.20 1 588 183 183 TPO N N 113.52 0.30 1 589 184 184 GLY H H 8.27 0.03 1 590 184 184 GLY CA C 44.94 0.20 1 591 184 184 GLY N N 111.46 0.30 1 592 185 185 PTR H H 7.74 0.03 1 593 185 185 PTR CA C 57.66 0.20 1 594 185 185 PTR CB C 38.48 0.20 1 595 185 185 PTR N N 121.71 0.30 1 596 186 186 VAL H H 7.73 0.03 1 597 186 186 VAL CA C 61.86 0.20 1 598 186 186 VAL N N 123.19 0.30 1 599 191 191 TYR CA C 56.71 0.20 1 600 192 192 ARG H H 7.30 0.03 1 601 192 192 ARG CA C 55.49 0.20 1 602 192 192 ARG CB C 30.80 0.20 1 603 192 192 ARG N N 122.51 0.30 1 604 193 193 ALA H H 8.79 0.03 1 605 193 193 ALA CA C 49.54 0.20 1 606 193 193 ALA N N 126.43 0.30 1 607 197 197 MET CA C 59.21 0.20 1 608 197 197 MET CB C 33.86 0.20 1 609 198 198 LEU H H 9.17 0.03 1 610 198 198 LEU CA C 57.91 0.20 1 611 198 198 LEU N N 126.68 0.30 1 612 199 199 ASN H H 7.82 0.03 1 613 199 199 ASN CA C 53.33 0.20 1 614 199 199 ASN CB C 40.11 0.20 1 615 199 199 ASN N N 115.41 0.30 1 616 200 200 TRP H H 8.50 0.03 1 617 200 200 TRP CA C 54.03 0.20 1 618 200 200 TRP CB C 27.62 0.20 1 619 200 200 TRP N N 124.96 0.30 1 620 201 201 MET H H 8.61 0.03 1 621 201 201 MET CA C 61.74 0.20 1 622 201 201 MET CB C 37.33 0.20 1 623 201 201 MET N N 120.30 0.30 1 624 202 202 HIS H H 7.14 0.03 1 625 202 202 HIS CA C 59.34 0.20 1 626 202 202 HIS CB C 32.29 0.20 1 627 202 202 HIS N N 115.33 0.30 1 628 203 203 TYR H H 10.10 0.03 1 629 203 203 TYR CA C 52.36 0.20 1 630 203 203 TYR CB C 40.94 0.20 1 631 203 203 TYR N N 127.17 0.30 1 632 204 204 ASN H H 8.72 0.03 1 633 204 204 ASN CB C 41.33 0.20 1 634 204 204 ASN N N 125.09 0.30 1 635 205 205 GLN H H 7.14 0.03 1 636 205 205 GLN CA C 57.23 0.20 1 637 205 205 GLN CB C 27.72 0.20 1 638 205 205 GLN N N 118.41 0.30 1 639 206 206 THR H H 8.29 0.03 1 640 206 206 THR CA C 59.16 0.20 1 641 206 206 THR N N 115.53 0.30 1 642 208 208 ASP CA C 56.23 0.20 1 643 208 208 ASP CB C 41.45 0.20 1 644 209 209 ILE H H 7.21 0.03 1 645 209 209 ILE CA C 60.70 0.20 1 646 209 209 ILE CB C 34.23 0.20 1 647 209 209 ILE N N 119.42 0.30 1 648 210 210 TRP H H 7.44 0.03 1 649 210 210 TRP CA C 61.07 0.20 1 650 210 210 TRP CB C 27.45 0.20 1 651 210 210 TRP N N 120.88 0.30 1 652 211 211 SER H H 7.50 0.03 1 653 211 211 SER CA C 61.84 0.20 1 654 211 211 SER CB C 62.89 0.20 1 655 211 211 SER N N 112.80 0.30 1 656 212 212 VAL H H 7.93 0.03 1 657 212 212 VAL CA C 67.24 0.20 1 658 212 212 VAL CB C 29.81 0.20 1 659 212 212 VAL N N 119.95 0.30 1 660 213 213 GLY H H 8.43 0.03 1 661 213 213 GLY CA C 47.59 0.20 1 662 213 213 GLY N N 110.35 0.30 1 663 214 214 CYS H H 7.83 0.03 1 664 214 214 CYS CA C 63.65 0.20 1 665 214 214 CYS CB C 27.17 0.20 1 666 214 214 CYS N N 119.39 0.30 1 667 215 215 ILE H H 8.36 0.03 1 668 215 215 ILE CA C 65.45 0.20 1 669 215 215 ILE CB C 37.56 0.20 1 670 215 215 ILE N N 124.35 0.30 1 671 216 216 MET H H 9.23 0.03 1 672 216 216 MET CA C 60.02 0.20 1 673 216 216 MET CB C 30.90 0.20 1 674 216 216 MET N N 120.60 0.30 1 675 217 217 ALA H H 8.09 0.03 1 676 217 217 ALA CA C 55.08 0.20 1 677 217 217 ALA CB C 19.40 0.20 1 678 217 217 ALA N N 118.38 0.30 1 679 218 218 GLU H H 7.04 0.03 1 680 218 218 GLU CA C 57.71 0.20 1 681 218 218 GLU CB C 29.07 0.20 1 682 218 218 GLU N N 119.92 0.30 1 683 219 219 LEU H H 7.23 0.03 1 684 219 219 LEU CA C 57.11 0.20 1 685 219 219 LEU CB C 42.15 0.20 1 686 219 219 LEU N N 116.53 0.30 1 687 220 220 LEU H H 8.46 0.03 1 688 220 220 LEU CA C 56.68 0.20 1 689 220 220 LEU CB C 39.94 0.20 1 690 220 220 LEU N N 118.55 0.30 1 691 221 221 THR H H 7.89 0.03 1 692 221 221 THR CA C 61.80 0.20 1 693 221 221 THR CB C 71.19 0.20 1 694 221 221 THR N N 106.16 0.30 1 695 222 222 GLY H H 8.37 0.03 1 696 222 222 GLY CA C 45.19 0.20 1 697 222 222 GLY N N 112.77 0.30 1 698 223 223 ARG H H 7.94 0.03 1 699 223 223 ARG CA C 53.61 0.20 1 700 223 223 ARG CB C 32.08 0.20 1 701 223 223 ARG N N 119.21 0.30 1 702 224 224 THR H H 7.88 0.03 1 703 224 224 THR CA C 63.27 0.20 1 704 224 224 THR CB C 68.60 0.20 1 705 224 224 THR N N 120.01 0.30 1 706 225 225 LEU H H 7.76 0.03 1 707 225 225 LEU CA C 52.48 0.20 1 708 225 225 LEU CB C 40.84 0.20 1 709 225 225 LEU N N 117.94 0.30 1 710 227 227 PRO CA C 60.57 0.20 1 711 228 228 GLY H H 8.29 0.03 1 712 228 228 GLY CA C 44.92 0.20 1 713 228 228 GLY N N 113.45 0.30 1 714 229 229 THR H H 10.09 0.03 1 715 229 229 THR CA C 63.21 0.20 1 716 229 229 THR CB C 68.87 0.20 1 717 229 229 THR N N 117.11 0.30 1 718 230 230 ASP H H 8.58 0.03 1 719 230 230 ASP CA C 57.70 0.20 1 720 230 230 ASP CB C 39.71 0.20 1 721 230 230 ASP N N 130.72 0.30 1 722 231 231 HIS H H 8.49 0.03 1 723 231 231 HIS CA C 51.89 0.20 1 724 231 231 HIS CB C 39.59 0.20 1 725 231 231 HIS N N 114.41 0.30 1 726 239 239 LEU CA C 57.35 0.20 1 727 240 240 ARG H H 8.15 0.03 1 728 240 240 ARG CA C 58.91 0.20 1 729 240 240 ARG CB C 31.93 0.20 1 730 240 240 ARG N N 117.43 0.30 1 731 241 241 LEU H H 7.54 0.03 1 732 241 241 LEU CA C 57.42 0.20 1 733 241 241 LEU CB C 40.12 0.20 1 734 241 241 LEU N N 117.81 0.30 1 735 242 242 VAL H H 8.51 0.03 1 736 242 242 VAL CA C 59.91 0.20 1 737 242 242 VAL CB C 40.31 0.20 1 738 242 242 VAL N N 122.73 0.30 1 739 245 245 PRO CA C 62.24 0.20 1 740 245 245 PRO CB C 31.60 0.20 1 741 246 246 GLY H H 8.22 0.03 1 742 246 246 GLY CA C 43.20 0.20 1 743 246 246 GLY N N 108.72 0.30 1 744 247 247 ALA H H 8.31 0.03 1 745 247 247 ALA CA C 54.89 0.20 1 746 247 247 ALA CB C 17.70 0.20 1 747 247 247 ALA N N 121.44 0.30 1 748 248 248 GLU H H 8.54 0.03 1 749 248 248 GLU CA C 58.79 0.20 1 750 248 248 GLU CB C 27.55 0.20 1 751 248 248 GLU N N 116.36 0.30 1 752 249 249 LEU H H 7.40 0.03 1 753 249 249 LEU CA C 56.39 0.20 1 754 249 249 LEU CB C 40.19 0.20 1 755 249 249 LEU N N 120.43 0.30 1 756 250 250 LEU H H 7.91 0.03 1 757 250 250 LEU CA C 57.57 0.20 1 758 250 250 LEU CB C 41.41 0.20 1 759 250 250 LEU N N 118.35 0.30 1 760 251 251 LYS H H 7.56 0.03 1 761 251 251 LYS CA C 55.73 0.20 1 762 251 251 LYS CB C 36.05 0.20 1 763 251 251 LYS N N 120.18 0.30 1 764 257 257 SER H H 8.30 0.03 1 765 257 257 SER CA C 60.62 0.20 1 766 257 257 SER N N 113.76 0.30 1 767 258 258 ALA H H 7.63 0.03 1 768 258 258 ALA CA C 54.44 0.20 1 769 258 258 ALA CB C 17.84 0.20 1 770 258 258 ALA N N 125.82 0.30 1 771 259 259 ARG H H 8.78 0.03 1 772 259 259 ARG CA C 55.03 0.20 1 773 259 259 ARG CB C 29.83 0.20 1 774 259 259 ARG N N 126.42 0.30 1 775 262 262 ILE CA C 63.34 0.20 1 776 263 263 GLN H H 8.04 0.03 1 777 263 263 GLN CA C 57.80 0.20 1 778 263 263 GLN CB C 28.03 0.20 1 779 263 263 GLN N N 118.20 0.30 1 780 264 264 SER H H 7.37 0.03 1 781 264 264 SER CA C 58.87 0.20 1 782 264 264 SER CB C 63.36 0.20 1 783 264 264 SER N N 114.04 0.30 1 784 265 265 LEU H H 6.78 0.03 1 785 265 265 LEU CA C 54.00 0.20 1 786 265 265 LEU CB C 41.21 0.20 1 787 265 265 LEU N N 122.98 0.30 1 788 266 266 THR H H 9.25 0.03 1 789 266 266 THR CA C 63.48 0.20 1 790 266 266 THR CB C 71.60 0.20 1 791 266 266 THR N N 122.40 0.30 1 792 267 267 GLN H H 8.44 0.03 1 793 267 267 GLN CA C 56.25 0.20 1 794 267 267 GLN CB C 27.42 0.20 1 795 267 267 GLN N N 126.97 0.30 1 796 268 268 MET H H 8.65 0.03 1 797 268 268 MET CA C 51.88 0.20 1 798 268 268 MET CB C 32.52 0.20 1 799 268 268 MET N N 124.16 0.30 1 800 269 269 PRO CA C 61.29 0.20 1 801 270 270 LYS H H 8.21 0.03 1 802 270 270 LYS CA C 56.43 0.20 1 803 270 270 LYS CB C 31.92 0.20 1 804 270 270 LYS N N 120.45 0.30 1 805 271 271 MET H H 8.34 0.03 1 806 271 271 MET CA C 55.74 0.20 1 807 271 271 MET CB C 32.27 0.20 1 808 271 271 MET N N 126.31 0.30 1 809 272 272 ASN H H 8.51 0.03 1 810 272 272 ASN CA C 52.39 0.20 1 811 272 272 ASN CB C 37.28 0.20 1 812 272 272 ASN N N 120.44 0.30 1 813 273 273 PHE H H 9.34 0.03 1 814 273 273 PHE CA C 59.55 0.20 1 815 273 273 PHE CB C 36.73 0.20 1 816 273 273 PHE N N 129.97 0.30 1 817 274 274 ALA H H 8.49 0.03 1 818 274 274 ALA CA C 54.29 0.20 1 819 274 274 ALA CB C 17.02 0.20 1 820 274 274 ALA N N 122.43 0.30 1 821 275 275 ASN H H 7.39 0.03 1 822 275 275 ASN CA C 53.26 0.20 1 823 275 275 ASN CB C 37.92 0.20 1 824 275 275 ASN N N 112.64 0.30 1 825 276 276 VAL H H 7.13 0.03 1 826 276 276 VAL CA C 63.94 0.20 1 827 276 276 VAL CB C 32.44 0.20 1 828 276 276 VAL N N 120.12 0.30 1 829 277 277 PHE H H 7.55 0.03 1 830 277 277 PHE CA C 55.64 0.20 1 831 277 277 PHE CB C 36.17 0.20 1 832 277 277 PHE N N 120.94 0.30 1 833 278 278 ILE H H 6.82 0.03 1 834 278 278 ILE CA C 61.95 0.20 1 835 278 278 ILE CB C 36.53 0.20 1 836 278 278 ILE N N 120.97 0.30 1 837 279 279 GLY H H 8.94 0.03 1 838 279 279 GLY CA C 44.52 0.20 1 839 279 279 GLY N N 116.43 0.30 1 840 280 280 ALA H H 7.32 0.03 1 841 280 280 ALA CA C 50.70 0.20 1 842 280 280 ALA CB C 18.87 0.20 1 843 280 280 ALA N N 122.06 0.30 1 844 281 281 ASN H H 9.03 0.03 1 845 281 281 ASN CA C 50.92 0.20 1 846 281 281 ASN CB C 38.49 0.20 1 847 281 281 ASN N N 122.60 0.30 1 848 282 282 PRO CA C 64.94 0.20 1 849 282 282 PRO CB C 31.44 0.20 1 850 283 283 LEU H H 8.37 0.03 1 851 283 283 LEU CA C 56.85 0.20 1 852 283 283 LEU CB C 41.87 0.20 1 853 283 283 LEU N N 117.19 0.30 1 854 284 284 ALA H H 7.03 0.03 1 855 284 284 ALA CA C 53.52 0.20 1 856 284 284 ALA CB C 17.01 0.20 1 857 284 284 ALA N N 121.21 0.30 1 858 285 285 VAL H H 7.02 0.03 1 859 285 285 VAL CA C 66.50 0.20 1 860 285 285 VAL CB C 30.90 0.20 1 861 285 285 VAL N N 116.54 0.30 1 862 286 286 ASP H H 7.42 0.03 1 863 286 286 ASP CA C 57.50 0.20 1 864 286 286 ASP CB C 42.51 0.20 1 865 286 286 ASP N N 117.98 0.30 1 866 287 287 LEU H H 7.04 0.03 1 867 287 287 LEU CA C 57.47 0.20 1 868 287 287 LEU CB C 39.05 0.20 1 869 287 287 LEU N N 117.60 0.30 1 870 288 288 LEU H H 8.07 0.03 1 871 288 288 LEU CA C 58.60 0.20 1 872 288 288 LEU CB C 40.70 0.20 1 873 288 288 LEU N N 120.39 0.30 1 874 289 289 GLU H H 7.91 0.03 1 875 289 289 GLU CA C 58.27 0.20 1 876 289 289 GLU CB C 28.41 0.20 1 877 289 289 GLU N N 117.67 0.30 1 878 290 290 LYS H H 7.26 0.03 1 879 290 290 LYS CA C 56.95 0.20 1 880 290 290 LYS CB C 31.82 0.20 1 881 290 290 LYS N N 116.48 0.30 1 882 291 291 MET H H 7.49 0.03 1 883 291 291 MET CA C 58.24 0.20 1 884 291 291 MET CB C 34.13 0.20 1 885 291 291 MET N N 118.48 0.30 1 886 292 292 LEU H H 7.79 0.03 1 887 292 292 LEU CA C 59.21 0.20 1 888 292 292 LEU CB C 38.20 0.20 1 889 292 292 LEU N N 119.01 0.30 1 890 296 296 SER CA C 61.05 0.20 1 891 297 297 ASP H H 8.39 0.03 1 892 297 297 ASP CA C 55.91 0.20 1 893 297 297 ASP CB C 40.18 0.20 1 894 297 297 ASP N N 121.08 0.30 1 895 298 298 LYS H H 7.57 0.03 1 896 298 298 LYS CA C 54.43 0.20 1 897 298 298 LYS CB C 32.70 0.20 1 898 298 298 LYS N N 117.80 0.30 1 899 299 299 ARG H H 6.99 0.03 1 900 299 299 ARG CA C 57.00 0.20 1 901 299 299 ARG CB C 29.61 0.20 1 902 299 299 ARG N N 122.58 0.30 1 903 300 300 ILE H H 7.02 0.03 1 904 300 300 ILE CA C 61.99 0.20 1 905 300 300 ILE CB C 38.98 0.20 1 906 300 300 ILE N N 125.16 0.30 1 907 301 301 THR H H 7.31 0.03 1 908 301 301 THR CA C 59.95 0.20 1 909 301 301 THR CB C 70.79 0.20 1 910 301 301 THR N N 109.48 0.30 1 911 302 302 ALA H H 9.43 0.03 1 912 302 302 ALA CA C 55.99 0.20 1 913 302 302 ALA CB C 15.94 0.20 1 914 302 302 ALA N N 122.21 0.30 1 915 303 303 ALA H H 8.56 0.03 1 916 303 303 ALA CA C 54.84 0.20 1 917 303 303 ALA CB C 17.57 0.20 1 918 303 303 ALA N N 116.00 0.30 1 919 304 304 GLN H H 7.35 0.03 1 920 304 304 GLN CA C 57.80 0.20 1 921 304 304 GLN CB C 27.97 0.20 1 922 304 304 GLN N N 116.03 0.30 1 923 305 305 ALA H H 8.61 0.03 1 924 305 305 ALA CA C 54.62 0.20 1 925 305 305 ALA CB C 18.43 0.20 1 926 305 305 ALA N N 123.95 0.30 1 927 306 306 LEU H H 7.59 0.03 1 928 306 306 LEU CA C 57.47 0.20 1 929 306 306 LEU CB C 41.26 0.20 1 930 306 306 LEU N N 116.65 0.30 1 931 307 307 ALA H H 6.50 0.03 1 932 307 307 ALA CA C 50.59 0.20 1 933 307 307 ALA CB C 18.05 0.20 1 934 307 307 ALA N N 115.05 0.30 1 935 308 308 HIS H H 7.89 0.03 1 936 308 308 HIS CA C 58.47 0.20 1 937 308 308 HIS CB C 32.07 0.20 1 938 308 308 HIS N N 122.80 0.30 1 939 309 309 ALA H H 8.27 0.03 1 940 309 309 ALA CA C 54.95 0.20 1 941 309 309 ALA CB C 18.16 0.20 1 942 309 309 ALA N N 132.80 0.30 1 943 310 310 TYR H H 11.57 0.03 1 944 310 310 TYR CA C 60.01 0.20 1 945 310 310 TYR CB C 37.99 0.20 1 946 310 310 TYR N N 125.12 0.30 1 947 311 311 PHE H H 7.59 0.03 1 948 311 311 PHE CA C 55.99 0.20 1 949 311 311 PHE CB C 38.05 0.20 1 950 311 311 PHE N N 110.56 0.30 1 951 312 312 ALA H H 7.45 0.03 1 952 312 312 ALA CA C 55.50 0.20 1 953 312 312 ALA CB C 18.02 0.20 1 954 312 312 ALA N N 123.56 0.30 1 955 313 313 GLN H H 8.60 0.03 1 956 313 313 GLN CA C 56.93 0.20 1 957 313 313 GLN CB C 27.46 0.20 1 958 313 313 GLN N N 114.16 0.30 1 959 314 314 TYR H H 7.37 0.03 1 960 314 314 TYR CA C 58.27 0.20 1 961 314 314 TYR CB C 39.03 0.20 1 962 314 314 TYR N N 116.11 0.30 1 963 315 315 HIS H H 7.76 0.03 1 964 315 315 HIS CA C 55.91 0.20 1 965 315 315 HIS CB C 28.91 0.20 1 966 315 315 HIS N N 115.48 0.30 1 967 316 316 ASP H H 7.50 0.03 1 968 316 316 ASP CA C 50.62 0.20 1 969 316 316 ASP CB C 40.91 0.20 1 970 316 316 ASP N N 125.20 0.30 1 971 317 317 PRO CA C 63.78 0.20 1 972 317 317 PRO CB C 31.26 0.20 1 973 318 318 ASP H H 7.89 0.03 1 974 318 318 ASP CA C 55.07 0.20 1 975 318 318 ASP CB C 40.03 0.20 1 976 318 318 ASP N N 117.48 0.30 1 977 319 319 ASP H H 7.96 0.03 1 978 319 319 ASP CA C 52.30 0.20 1 979 319 319 ASP CB C 41.50 0.20 1 980 319 319 ASP N N 121.31 0.30 1 981 320 320 GLU H H 7.69 0.03 1 982 320 320 GLU CA C 53.24 0.20 1 983 320 320 GLU CB C 28.83 0.20 1 984 320 320 GLU N N 121.56 0.30 1 985 321 321 PRO CA C 63.20 0.20 1 986 322 322 VAL H H 7.80 0.03 1 987 322 322 VAL CA C 59.32 0.20 1 988 322 322 VAL CB C 33.19 0.20 1 989 322 322 VAL N N 109.22 0.30 1 990 323 323 ALA H H 8.38 0.03 1 991 323 323 ALA CA C 50.47 0.20 1 992 323 323 ALA CB C 19.34 0.20 1 993 323 323 ALA N N 123.67 0.30 1 994 324 324 ASP H H 8.01 0.03 1 995 324 324 ASP CA C 52.75 0.20 1 996 324 324 ASP CB C 38.97 0.20 1 997 324 324 ASP N N 120.98 0.30 1 998 326 326 TYR CA C 58.97 0.20 1 999 327 327 ASP H H 6.89 0.03 1 1000 327 327 ASP CA C 53.97 0.20 1 1001 327 327 ASP CB C 40.93 0.20 1 1002 327 327 ASP N N 123.03 0.30 1 1003 331 331 GLU H H 9.85 0.03 1 1004 331 331 GLU CA C 58.20 0.20 1 1005 331 331 GLU N N 114.94 0.30 1 1006 332 332 SER H H 7.37 0.03 1 1007 332 332 SER CA C 57.74 0.20 1 1008 332 332 SER CB C 63.22 0.20 1 1009 332 332 SER N N 111.94 0.30 1 1010 333 333 ARG H H 7.54 0.03 1 1011 333 333 ARG CA C 55.87 0.20 1 1012 333 333 ARG CB C 30.25 0.20 1 1013 333 333 ARG N N 121.95 0.30 1 1014 334 334 ASP H H 8.50 0.03 1 1015 334 334 ASP CA C 53.18 0.20 1 1016 334 334 ASP CB C 40.21 0.20 1 1017 334 334 ASP N N 124.99 0.30 1 1018 335 335 LEU H H 7.76 0.03 1 1019 335 335 LEU CA C 52.43 0.20 1 1020 335 335 LEU CB C 41.15 0.20 1 1021 335 335 LEU N N 123.17 0.30 1 1022 336 336 LEU H H 8.72 0.03 1 1023 336 336 LEU CA C 53.87 0.20 1 1024 336 336 LEU CB C 41.47 0.20 1 1025 336 336 LEU N N 119.92 0.30 1 1026 337 337 ILE H H 8.91 0.03 1 1027 337 337 ILE CA C 66.54 0.20 1 1028 337 337 ILE CB C 37.27 0.20 1 1029 337 337 ILE N N 121.85 0.30 1 1030 338 338 ASP H H 8.32 0.03 1 1031 338 338 ASP CA C 56.93 0.20 1 1032 338 338 ASP CB C 39.39 0.20 1 1033 338 338 ASP N N 115.95 0.30 1 1034 339 339 GLU H H 7.03 0.03 1 1035 339 339 GLU CA C 58.24 0.20 1 1036 339 339 GLU CB C 29.20 0.20 1 1037 339 339 GLU N N 120.56 0.30 1 1038 340 340 TRP H H 7.65 0.03 1 1039 340 340 TRP CA C 59.76 0.20 1 1040 340 340 TRP CB C 30.11 0.20 1 1041 340 340 TRP N N 119.85 0.30 1 1042 341 341 LYS H H 8.69 0.03 1 1043 341 341 LYS CA C 60.06 0.20 1 1044 341 341 LYS CB C 31.23 0.20 1 1045 341 341 LYS N N 121.49 0.30 1 1046 342 342 SER H H 7.56 0.03 1 1047 342 342 SER CA C 60.85 0.20 1 1048 342 342 SER CB C 62.11 0.20 1 1049 342 342 SER N N 114.57 0.30 1 1050 343 343 LEU H H 7.85 0.03 1 1051 343 343 LEU CA C 57.47 0.20 1 1052 343 343 LEU CB C 41.45 0.20 1 1053 343 343 LEU N N 120.39 0.30 1 1054 344 344 THR CA C 68.02 0.20 1 1055 345 345 TYR H H 8.76 0.03 1 1056 345 345 TYR CA C 61.68 0.20 1 1057 345 345 TYR CB C 37.23 0.20 1 1058 345 345 TYR N N 124.85 0.30 1 1059 346 346 ASP H H 8.01 0.03 1 1060 346 346 ASP CA C 56.96 0.20 1 1061 346 346 ASP CB C 39.53 0.20 1 1062 346 346 ASP N N 117.48 0.30 1 1063 347 347 GLU H H 7.43 0.03 1 1064 347 347 GLU CA C 57.60 0.20 1 1065 347 347 GLU CB C 28.64 0.20 1 1066 347 347 GLU N N 118.49 0.30 1 1067 348 348 VAL H H 8.01 0.03 1 1068 348 348 VAL CA C 65.81 0.20 1 1069 348 348 VAL CB C 30.99 0.20 1 1070 348 348 VAL N N 121.24 0.30 1 1071 349 349 ILE H H 8.04 0.03 1 1072 349 349 ILE CA C 62.92 0.20 1 1073 349 349 ILE CB C 36.07 0.20 1 1074 349 349 ILE N N 114.65 0.30 1 1075 350 350 SER H H 7.33 0.03 1 1076 350 350 SER CA C 57.88 0.20 1 1077 350 350 SER CB C 63.35 0.20 1 1078 350 350 SER N N 113.39 0.30 1 1079 351 351 PHE H H 7.21 0.03 1 1080 351 351 PHE CA C 60.25 0.20 1 1081 351 351 PHE CB C 39.00 0.20 1 1082 351 351 PHE N N 125.03 0.30 1 1083 352 352 VAL H H 6.83 0.03 1 1084 352 352 VAL CA C 63.31 0.20 1 1085 352 352 VAL CB C 33.32 0.20 1 1086 352 352 VAL N N 130.13 0.30 1 stop_ save_