data_5700 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Backbone 1H, 13C and 15N resonance assignments for the 25.8 kDa DNA binding domain of the human p63 protein ; _BMRB_accession_number 5700 _BMRB_flat_file_name bmr5700.str _Entry_type original _Submission_date 2003-02-18 _Accession_date 2003-02-18 _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 Furrer Julien . . 2 Enthart Andreas . . 3 Dehner Alexander . . 4 Klein Christian . . 5 Hansen Silke . . 6 Schwaiger Manfred . . 7 Gemmecker Gerd . . 8 Kessler Horst . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 370 "13C chemical shifts" 608 "15N chemical shifts" 200 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2003-03-21 original author . stop_ _Original_release_date 2003-03-21 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title 'Backbone 1H, 13C and 15N resonance assignments for the 25.8 kDa DNA binding domain of the human p63 protein' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 12815266 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Furrer Julien . . 2 Enthart Andreas . . 3 Kuhlewein Angelika . . 4 Dehner Alexander . . 5 Klein Christian . . 6 Hansen Silke . . 7 Schwaiger Manfred . . 8 Gemmecker Gerd . . 9 Kessler Horst . . stop_ _Journal_abbreviation 'J. Biomol. NMR' _Journal_name_full 'Journal of biomolecular NMR' _Journal_volume 26 _Journal_issue 4 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 377 _Page_last 378 _Year 2003 _Details . loop_ _Keyword DNA 'p53 protein homologue' 'resonance assignment' stop_ save_ ################################## # Molecular system description # ################################## save_system_p63 _Saveframe_category molecular_system _Mol_system_name 'p63 DNA-binding domain' _Abbreviation_common p63 _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'p63 DBD' $p63_monomer stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state monomer _System_paramagnetic no _System_thiol_state 'all free' loop_ _Biological_function 'tumor suppressor' stop_ _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_p63_monomer _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common p63 _Abbreviation_common p63 _Molecular_mass 25832 _Mol_thiol_state 'all free' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 233 _Mol_residue_sequence ; GSSTFDALSPSPAIPSNTDY PGPHSFDVSFQQSSTAKSAT WTYSTELKKLYCQIAKTCPI QIKVMTPPPQGAVIRAMPVY KKAEHVTEVVKRCPNHELSR EFNEGQIAPPSHLIRVEGNS HAQYVEDPITGRQSVLVPYE PPQVGTEFTTVLYNFMCNSS CVGGMNRRPILIIVTLETRD GQVLGRRCFEARICACPGRD RKADEDSIRKQQVSDSTKNG DAFRQNTHGIQMT ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 113 GLY 2 114 SER 3 115 SER 4 116 THR 5 117 PHE 6 118 ASP 7 119 ALA 8 120 LEU 9 121 SER 10 122 PRO 11 123 SER 12 124 PRO 13 125 ALA 14 126 ILE 15 127 PRO 16 128 SER 17 129 ASN 18 130 THR 19 131 ASP 20 132 TYR 21 133 PRO 22 134 GLY 23 135 PRO 24 136 HIS 25 137 SER 26 138 PHE 27 139 ASP 28 140 VAL 29 141 SER 30 142 PHE 31 143 GLN 32 144 GLN 33 145 SER 34 146 SER 35 147 THR 36 148 ALA 37 149 LYS 38 150 SER 39 151 ALA 40 152 THR 41 153 TRP 42 154 THR 43 155 TYR 44 156 SER 45 157 THR 46 158 GLU 47 159 LEU 48 160 LYS 49 161 LYS 50 162 LEU 51 163 TYR 52 164 CYS 53 165 GLN 54 166 ILE 55 167 ALA 56 168 LYS 57 169 THR 58 170 CYS 59 171 PRO 60 172 ILE 61 173 GLN 62 174 ILE 63 175 LYS 64 176 VAL 65 177 MET 66 178 THR 67 179 PRO 68 180 PRO 69 181 PRO 70 182 GLN 71 183 GLY 72 184 ALA 73 185 VAL 74 186 ILE 75 187 ARG 76 188 ALA 77 189 MET 78 190 PRO 79 191 VAL 80 192 TYR 81 193 LYS 82 194 LYS 83 195 ALA 84 196 GLU 85 197 HIS 86 198 VAL 87 199 THR 88 200 GLU 89 201 VAL 90 202 VAL 91 203 LYS 92 204 ARG 93 205 CYS 94 206 PRO 95 207 ASN 96 208 HIS 97 209 GLU 98 210 LEU 99 211 SER 100 212 ARG 101 213 GLU 102 214 PHE 103 215 ASN 104 216 GLU 105 217 GLY 106 218 GLN 107 219 ILE 108 220 ALA 109 221 PRO 110 222 PRO 111 223 SER 112 224 HIS 113 225 LEU 114 226 ILE 115 227 ARG 116 228 VAL 117 229 GLU 118 230 GLY 119 231 ASN 120 232 SER 121 233 HIS 122 234 ALA 123 235 GLN 124 236 TYR 125 237 VAL 126 238 GLU 127 239 ASP 128 240 PRO 129 241 ILE 130 242 THR 131 243 GLY 132 244 ARG 133 245 GLN 134 246 SER 135 247 VAL 136 248 LEU 137 249 VAL 138 250 PRO 139 251 TYR 140 252 GLU 141 253 PRO 142 254 PRO 143 255 GLN 144 256 VAL 145 257 GLY 146 258 THR 147 259 GLU 148 260 PHE 149 261 THR 150 262 THR 151 263 VAL 152 264 LEU 153 265 TYR 154 266 ASN 155 267 PHE 156 268 MET 157 269 CYS 158 270 ASN 159 271 SER 160 272 SER 161 273 CYS 162 274 VAL 163 275 GLY 164 276 GLY 165 277 MET 166 278 ASN 167 279 ARG 168 280 ARG 169 281 PRO 170 282 ILE 171 283 LEU 172 284 ILE 173 285 ILE 174 286 VAL 175 287 THR 176 288 LEU 177 289 GLU 178 290 THR 179 291 ARG 180 292 ASP 181 293 GLY 182 294 GLN 183 295 VAL 184 296 LEU 185 297 GLY 186 298 ARG 187 299 ARG 188 300 CYS 189 301 PHE 190 302 GLU 191 303 ALA 192 304 ARG 193 305 ILE 194 306 CYS 195 307 ALA 196 308 CYS 197 309 PRO 198 310 GLY 199 311 ARG 200 312 ASP 201 313 ARG 202 314 LYS 203 315 ALA 204 316 ASP 205 317 GLU 206 318 ASP 207 319 SER 208 320 ILE 209 321 ARG 210 322 LYS 211 323 GLN 212 324 GLN 213 325 VAL 214 326 SER 215 327 ASP 216 328 SER 217 329 THR 218 330 LYS 219 331 ASN 220 332 GLY 221 333 ASP 222 334 ALA 223 335 PHE 224 336 ARG 225 337 GLN 226 338 ASN 227 339 THR 228 340 HIS 229 341 GLY 230 342 ILE 231 343 GLN 232 344 MET 233 345 THR stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-01-28 loop_ _Database_name _Database_accession_code _Database_entry_mol_name _Sequence_query_to_submitted_percentage _Sequence_subject_length _Sequence_identity _Sequence_positive _Sequence_homology_expectation_value PDB 2RMN "The Solution Structure Of The P63 Dna-Binding Domain" 100.00 233 100.00 100.00 7.02e-173 PDB 3QYM "Structure Of P63 Dna Binding Domain In Complex With A 10 Base Pair AT Rich Response Element Half Site" 85.41 203 99.50 99.50 7.57e-145 PDB 3QYN "Structure Of P63 Dna Binding Domain In Complex With A 22 Base Pair AT Rich Response Element Containing 2 Base Pair Spacer Betwe" 85.41 203 99.50 99.50 7.57e-145 PDB 3US0 'Structure Of P63 Dna Binding Domain In Complex With A 22 Base Pair AT Rich Response Element Containing A Two Base Pair "at" Spa' 85.41 203 99.50 99.50 7.57e-145 PDB 3US1 'Structure Of P63 Dna Binding Domain In Complex With A 22 Base Pair Response Element Containing A Two Base Pair "gc" Spacer Betw' 85.41 203 99.50 99.50 7.57e-145 PDB 3US2 "Structure Of P63 Dna Binding Domain In Complex With A 19 Base Pair AT Rich Response Element Containing Two Half Sites With A Si" 85.41 203 99.50 99.50 7.57e-145 DBJ BAA32432 "p73H [Mus musculus]" 101.29 586 97.46 97.46 1.84e-164 DBJ BAA32433 "p73H [Homo sapiens]" 101.29 586 97.03 97.03 3.51e-163 DBJ BAA32592 "p51A [Homo sapiens]" 101.29 448 97.88 97.88 1.32e-166 DBJ BAA32593 "p51B [Homo sapiens]" 101.29 641 97.88 97.88 2.72e-164 DBJ BAB20631 "DN p63 alpha [Gallus gallus]" 99.57 582 99.14 99.14 4.68e-166 EMBL CAA76562 "KET protein [Homo sapiens]" 101.29 680 97.88 97.88 2.12e-163 EMBL CAB88216 "TA2 KET alpha [Rattus norvegicus]" 101.29 680 97.46 97.46 1.02e-162 EMBL CAC37098 "TA1 KET alpha protein [Rattus norvegicus]" 101.29 663 97.46 97.46 6.08e-163 EMBL CAC37099 "DN KET alpha protein [Rattus norvegicus]" 101.29 586 97.46 97.46 1.90e-164 EMBL CAC37100 "TA1 KET gamma protein [Rattus norvegicus]" 101.29 470 97.46 97.46 1.15e-165 GB AAC24830 "p53 homolog [Homo sapiens]" 101.29 356 97.46 97.46 1.07e-167 GB AAC43038 "CUSP [Homo sapiens]" 101.29 586 97.88 97.88 2.26e-165 GB AAC62633 "TA p63 gamma [Homo sapiens]" 101.29 448 97.88 97.88 1.32e-166 GB AAC62634 "DN p63 gamma [Homo sapiens]" 101.29 393 97.88 97.88 4.34e-168 GB AAC62635 "TA p63 alpha [Homo sapiens]" 101.29 641 97.88 97.88 2.39e-164 REF NP_001079107 "tumor protein p63 [Xenopus laevis]" 99.57 365 96.98 99.57 1.23e-167 REF NP_001108450 "tumor protein 63 isoform 2 [Homo sapiens]" 101.29 555 97.88 97.88 4.61e-165 REF NP_001108451 "tumor protein 63 isoform 3 [Homo sapiens]" 101.29 487 97.88 97.88 6.40e-166 REF NP_001108452 "tumor protein 63 isoform 4 [Homo sapiens]" 101.29 586 97.88 97.88 2.26e-165 REF NP_001108453 "tumor protein 63 isoform 5 [Homo sapiens]" 101.29 461 97.88 97.88 2.10e-167 SP O88898 "RecName: Full=Tumor protein 63; Short=p63; AltName: Full=Transformation-related protein 63; Short=TP63; AltName: Full=Tumor pro" 101.29 680 97.46 97.46 9.24e-163 SP Q9H3D4 "RecName: Full=Tumor protein 63; Short=p63; AltName: Full=Chronic ulcerative stomatitis protein; Short=CUSP; AltName: Full=Kerat" 101.29 680 97.88 97.88 2.38e-163 SP Q9JJP6 "RecName: Full=Tumor protein 63; Short=p63; AltName: Full=Keratinocyte transcription factor KET; AltName: Full=Transformation-re" 101.29 680 97.46 97.46 1.02e-162 TPG DAA33389 "TPA: tumor protein p63-like [Bos taurus]" 101.29 680 97.88 97.88 2.00e-163 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species _Tissue $p63_monomer Human 9606 Eukaryota Metazoa Homo sapiens placenta stop_ save_ ######################### # Experimental source # ######################### save_experimental_source _Saveframe_category experimental_source loop_ _Mol_label _Production_method _Host_organism_name_common _Genus _Species _Strain _Variant _Vector_type _Vector_name $p63_monomer 'recombinant technology' 'E. coli' Escherichia coli B BL21 pQE30 . 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 $p63_monomer 0.7 mM '[U-75% 2H; U-98% 13C; U-98% 15N]' stop_ save_ save_sample_2 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $p63_monomer 0.7 mM '[U-98% 15N]' stop_ save_ ############################ # Computer software used # ############################ save_Xwinnmr _Saveframe_category software _Name xwinnmr _Version 3.5 _Details . save_ save_Aurelia _Saveframe_category software _Name AURELIA _Version 2.8.4 _Details . save_ save_PASTA _Saveframe_category software _Name PASTA _Version . loop_ _Task 'automatic assignment program' stop_ _Details 'In-house developed software for automating the peak assignment process.' save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model Avance _Field_strength 600 _Details . save_ save_NMR_spectrometer_2 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model Avance _Field_strength 750 _Details . save_ save_NMR_spectrometer_3 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model Avance _Field_strength 900 _Details . save_ ############################# # NMR applied experiments # ############################# save_1H,15N_HSQC_1 _Saveframe_category NMR_applied_experiment _Experiment_name '1H,15N HSQC' _Sample_label . save_ save_HNHA_2 _Saveframe_category NMR_applied_experiment _Experiment_name HNHA _Sample_label . save_ save_1H,15N_HSQC-TOCSY_3 _Saveframe_category NMR_applied_experiment _Experiment_name '1H,15N HSQC-TOCSY' _Sample_label . save_ save_1H,15N_HSQC-NOESY_4 _Saveframe_category NMR_applied_experiment _Experiment_name '1H,15N HSQC-NOESY' _Sample_label . save_ save_1H,15N_HSQC-NOESY-1H,15N_HSQC_5 _Saveframe_category NMR_applied_experiment _Experiment_name '1H,15N HSQC-NOESY-1H,15N HSQC' _Sample_label . save_ save_HNCO_6 _Saveframe_category NMR_applied_experiment _Experiment_name HNCO _Sample_label . save_ save_tr-HNCA_7 _Saveframe_category NMR_applied_experiment _Experiment_name tr-HNCA _Sample_label . save_ save_tr-HN(CA)CO_8 _Saveframe_category NMR_applied_experiment _Experiment_name tr-HN(CA)CO _Sample_label . save_ save_tr-HN(CO)CACB_9 _Saveframe_category NMR_applied_experiment _Experiment_name tr-HN(CO)CACB _Sample_label . save_ save_tr-HNCACB_10 _Saveframe_category NMR_applied_experiment _Experiment_name tr-HNCACB _Sample_label . save_ ####################### # Sample conditions # ####################### save_Ex_cond_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 6.8 0.2 n/a temperature 303 1 K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference _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 0.0 . indirect . . . 0.251449530 DSS H 1 'methyl protons' ppm 0.0 internal direct . . . 1.0 DSS H 2 'methyl protons' ppm 0.0 . indirect . . . 0.153506088 DSS N 15 'methyl protons' ppm 0.0 . 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_shift_set_1 _Saveframe_category assigned_chemical_shifts _Details 'Due to very poor signal to noise ratio, CB and HA only partially assigned.' loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $Ex_cond_1 _Chem_shift_reference_set_label $chemical_shift_reference _Mol_system_component_name 'p63 DBD' _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 SER C C 177.4 0.1 1 2 . 3 SER CA C 58.0 0.1 1 3 . 4 THR N N 121.7 0.1 1 4 . 4 THR H H 7.94 0.03 1 5 . 4 THR C C 174.3 0.1 1 6 . 4 THR CA C 61.6 0.1 1 7 . 4 THR CB C 69.2 0.1 1 8 . 4 THR HA H 4.37 0.03 1 9 . 5 PHE N N 121.7 0.1 1 10 . 5 PHE H H 8.20 0.03 1 11 . 5 PHE C C 175.2 0.1 1 12 . 5 PHE CA C 57.4 0.1 1 13 . 5 PHE CB C 38.7 0.1 1 14 . 5 PHE HA H 4.55 0.03 1 15 . 6 ASP N N 122.1 0.1 1 16 . 6 ASP H H 8.20 0.03 1 17 . 6 ASP C C 175.7 0.1 1 18 . 6 ASP CA C 53.7 0.1 1 19 . 6 ASP CB C 40.6 0.1 1 20 . 6 ASP HA H 4.55 0.03 1 21 . 7 ALA N N 124.0 0.1 1 22 . 7 ALA H H 8.12 0.03 1 23 . 7 ALA C C 177.5 0.1 1 24 . 7 ALA CA C 52.2 0.1 1 25 . 7 ALA CB C 18.3 0.1 1 26 . 7 ALA HA H 4.23 0.03 1 27 . 8 LEU N N 119.8 0.1 1 28 . 8 LEU H H 8.15 0.03 1 29 . 8 LEU C C 177.2 0.1 1 30 . 8 LEU CA C 54.5 0.1 1 31 . 8 LEU CB C 41.1 0.1 1 32 . 8 LEU HA H 4.35 0.03 1 33 . 9 SER N N 117.4 0.1 1 34 . 9 SER H H 8.11 0.03 1 35 . 9 SER C C 172.4 0.1 1 36 . 9 SER CA C 55.7 0.1 1 37 . 10 PRO C C 175.3 0.1 1 38 . 10 PRO CA C 62.8 0.1 1 39 . 10 PRO CB C 31.1 0.1 1 40 . 11 SER N N 115.3 0.1 1 41 . 11 SER H H 8.07 0.03 1 42 . 11 SER C C 172.9 0.1 1 43 . 11 SER CA C 54.6 0.1 1 44 . 11 SER HA H 4.58 0.03 1 45 . 12 PRO C C 176.3 0.1 1 46 . 12 PRO CA C 62.2 0.1 1 47 . 12 PRO CB C 31.0 0.1 1 48 . 13 ALA N N 123.5 0.1 1 49 . 13 ALA H H 8.32 0.03 1 50 . 13 ALA C C 177.3 0.1 1 51 . 13 ALA CA C 52.0 0.1 1 52 . 13 ALA HA H 4.23 0.03 1 53 . 14 ILE N N 121.6 0.1 1 54 . 14 ILE H H 8.21 0.03 1 55 . 14 ILE CA C 58.2 0.1 1 56 . 15 PRO C C 176.0 0.1 1 57 . 15 PRO CA C 62.2 0.1 1 58 . 15 PRO CB C 31.1 0.1 1 59 . 16 SER N N 116.8 0.1 1 60 . 16 SER H H 8.27 0.03 1 61 . 16 SER C C 174.3 0.1 1 62 . 16 SER CA C 58.0 0.1 1 63 . 16 SER CB C 62.9 0.1 1 64 . 16 SER HA H 4.46 0.03 1 65 . 17 ASN N N 120.1 0.1 1 66 . 17 ASN H H 8.20 0.03 1 67 . 17 ASN C C 174.7 0.1 1 68 . 17 ASN CA C 51.6 0.1 1 69 . 17 ASN CB C 37.6 0.1 1 70 . 17 ASN HA H 4.27 0.03 1 71 . 18 THR N N 112.2 0.1 1 72 . 18 THR H H 7.65 0.03 1 73 . 18 THR C C 174.6 0.1 1 74 . 18 THR CA C 60.9 0.1 1 75 . 18 THR CB C 70.1 0.1 1 76 . 18 THR HA H 4.33 0.03 1 77 . 19 ASP N N 125.8 0.1 1 78 . 19 ASP H H 8.86 0.03 1 79 . 19 ASP C C 176.8 0.1 1 80 . 19 ASP CA C 55.1 0.1 1 81 . 19 ASP CB C 41.2 0.1 1 82 . 20 TYR N N 121.9 0.1 1 83 . 20 TYR H H 9.74 0.03 1 84 . 20 TYR C C 171.9 0.1 1 85 . 20 TYR CA C 53.3 0.1 1 86 . 20 TYR CB C 40.1 0.1 1 87 . 20 TYR HA H 5.31 0.03 1 88 . 21 PRO C C 179.2 0.1 1 89 . 21 PRO CA C 64.4 0.1 1 90 . 22 GLY N N 101.4 0.1 1 91 . 22 GLY H H 7.35 0.03 1 92 . 22 GLY CA C 44.6 0.1 1 93 . 23 PRO C C 177.6 0.1 1 94 . 23 PRO CA C 63.4 0.1 1 95 . 24 HIS N N 116.6 0.1 1 96 . 24 HIS H H 8.95 0.03 1 97 . 24 HIS C C 174.5 0.1 1 98 . 24 HIS CA C 54.5 0.1 1 99 . 24 HIS CB C 26.2 0.1 1 100 . 24 HIS HA H 4.66 0.03 1 101 . 25 SER N N 115.4 0.1 1 102 . 25 SER H H 7.91 0.03 1 103 . 25 SER C C 171.9 0.1 1 104 . 25 SER CA C 58.5 0.1 1 105 . 25 SER CB C 60.3 0.1 1 106 . 25 SER HA H 4.58 0.03 1 107 . 26 PHE N N 121.5 0.1 1 108 . 26 PHE H H 8.53 0.03 1 109 . 26 PHE C C 174.1 0.1 1 110 . 26 PHE CA C 56.7 0.1 1 111 . 26 PHE CB C 39.8 0.1 1 112 . 26 PHE HA H 4.91 0.03 1 113 . 27 ASP N N 129.5 0.1 1 114 . 27 ASP H H 9.07 0.03 1 115 . 27 ASP C C 173.3 0.1 1 116 . 27 ASP CA C 52.7 0.1 1 117 . 27 ASP CB C 44.4 0.1 1 118 . 27 ASP HA H 4.64 0.03 1 119 . 28 VAL N N 118.8 0.1 1 120 . 28 VAL H H 7.95 0.03 1 121 . 28 VAL C C 174.3 0.1 1 122 . 28 VAL CA C 58.9 0.1 1 123 . 28 VAL CB C 33.6 0.1 1 124 . 28 VAL HA H 4.86 0.03 1 125 . 29 SER N N 119.8 0.1 1 126 . 29 SER H H 8.96 0.03 1 127 . 29 SER C C 170.1 0.1 1 128 . 29 SER CA C 56.2 0.1 1 129 . 29 SER CB C 65.4 0.1 1 130 . 29 SER HA H 4.27 0.03 1 131 . 30 PHE N N 116.9 0.1 1 132 . 30 PHE H H 7.97 0.03 1 133 . 30 PHE C C 176.4 0.1 1 134 . 30 PHE CA C 56.1 0.1 1 135 . 30 PHE CB C 40.4 0.1 1 136 . 30 PHE HA H 4.56 0.03 1 137 . 31 GLN N N 122.2 0.1 1 138 . 31 GLN H H 8.90 0.03 1 139 . 31 GLN C C 175.1 0.1 1 140 . 31 GLN CA C 55.3 0.1 1 141 . 31 GLN CB C 28.8 0.1 1 142 . 31 GLN HA H 4.25 0.03 1 143 . 32 GLN N N 121.4 0.1 1 144 . 32 GLN H H 8.63 0.03 1 145 . 32 GLN C C 175.6 0.1 1 146 . 32 GLN CA C 55.7 0.1 1 147 . 32 GLN CB C 28.5 0.1 1 148 . 32 GLN HA H 4.47 0.03 1 149 . 33 SER N N 117.6 0.1 1 150 . 33 SER H H 8.40 0.03 1 151 . 33 SER C C 172.7 0.1 1 152 . 33 SER CA C 57.5 0.1 1 153 . 34 SER N N 120.8 0.1 1 154 . 34 SER H H 7.44 0.03 1 155 . 34 SER C C 174.1 0.1 1 156 . 34 SER CA C 57.5 0.1 1 157 . 35 THR N N 112.3 0.1 1 158 . 35 THR H H 7.65 0.03 1 159 . 35 THR C C 174.1 0.1 1 160 . 35 THR CA C 61.0 0.1 1 161 . 35 THR CB C 68.1 0.1 1 162 . 36 ALA N N 124.9 0.1 1 163 . 36 ALA H H 7.99 0.03 1 164 . 36 ALA C C 178.2 0.1 1 165 . 36 ALA CA C 52.0 0.1 1 166 . 36 ALA HA H 4.53 0.03 1 167 . 37 LYS N N 120.9 0.1 1 168 . 37 LYS H H 8.15 0.03 1 169 . 37 LYS C C 176.9 0.1 1 170 . 37 LYS CA C 56.4 0.1 1 171 . 38 SER N N 112.7 0.1 1 172 . 38 SER H H 7.94 0.03 1 173 . 38 SER C C 174.2 0.1 1 174 . 38 SER CA C 57.1 0.1 1 175 . 39 ALA N N 125.4 0.1 1 176 . 39 ALA H H 7.85 0.03 1 177 . 39 ALA C C 178.3 0.1 1 178 . 39 ALA CA C 52.4 0.1 1 179 . 39 ALA CB C 17.6 0.1 1 180 . 39 ALA HA H 4.46 0.03 1 181 . 40 THR N N 111.6 0.1 1 182 . 40 THR H H 8.49 0.03 1 183 . 40 THR C C 173.2 0.1 1 184 . 40 THR CA C 62.6 0.1 1 185 . 40 THR CB C 69.1 0.1 1 186 . 40 THR HA H 4.27 0.03 1 187 . 41 TRP N N 114.5 0.1 1 188 . 41 TRP H H 7.18 0.03 1 189 . 41 TRP C C 173.6 0.1 1 190 . 41 TRP CA C 54.9 0.1 1 191 . 41 TRP CB C 30.9 0.1 1 192 . 41 TRP HA H 5.48 0.03 1 193 . 42 THR N N 114.6 0.1 1 194 . 42 THR H H 9.70 0.03 1 195 . 42 THR C C 170.1 0.1 1 196 . 42 THR CA C 61.1 0.1 1 197 . 42 THR CB C 68.0 0.1 1 198 . 42 THR HA H 4.17 0.03 1 199 . 43 TYR N N 128.2 0.1 1 200 . 43 TYR H H 8.63 0.03 1 201 . 43 TYR C C 173.8 0.1 1 202 . 43 TYR CA C 56.0 0.1 1 203 . 43 TYR CB C 41.3 0.1 1 204 . 43 TYR HA H 5.40 0.03 1 205 . 44 SER N N 120.1 0.1 1 206 . 44 SER H H 8.57 0.03 1 207 . 44 SER C C 175.1 0.1 1 208 . 44 SER CA C 55.1 0.1 1 209 . 44 SER CB C 63.4 0.1 1 210 . 44 SER HA H 4.52 0.03 1 211 . 45 THR N N 123.8 0.1 1 212 . 45 THR H H 8.38 0.03 1 213 . 45 THR C C 177.2 0.1 1 214 . 45 THR CA C 64.1 0.1 1 215 . 45 THR CB C 68.1 0.1 1 216 . 45 THR HA H 4.33 0.03 1 217 . 46 GLU N N 122.2 0.1 1 218 . 46 GLU H H 8.58 0.03 1 219 . 46 GLU C C 177.9 0.1 1 220 . 46 GLU CA C 58.8 0.1 1 221 . 46 GLU CB C 29.3 0.1 1 222 . 46 GLU HA H 4.08 0.03 1 223 . 47 LEU N N 114.9 0.1 1 224 . 47 LEU H H 7.56 0.03 1 225 . 47 LEU C C 175.8 0.1 1 226 . 47 LEU CA C 53.7 0.1 1 227 . 47 LEU CB C 41.3 0.1 1 228 . 47 LEU HA H 4.31 0.03 1 229 . 48 LYS N N 120.8 0.1 1 230 . 48 LYS H H 7.67 0.03 1 231 . 48 LYS C C 174.5 0.1 1 232 . 48 LYS CA C 56.5 0.1 1 233 . 48 LYS CB C 29.1 0.1 1 234 . 48 LYS HA H 3.94 0.03 1 235 . 49 LYS N N 119.2 0.1 1 236 . 49 LYS H H 7.02 0.03 1 237 . 49 LYS C C 171.8 0.1 1 238 . 49 LYS CA C 54.3 0.1 1 239 . 49 LYS CB C 37.9 0.1 1 240 . 49 LYS HA H 5.01 0.03 1 241 . 50 LEU N N 129.0 0.1 1 242 . 50 LEU H H 9.28 0.03 1 243 . 50 LEU C C 173.1 0.1 1 244 . 50 LEU CA C 53.4 0.1 1 245 . 50 LEU CB C 44.1 0.1 1 246 . 51 TYR N N 124.8 0.1 1 247 . 51 TYR H H 9.28 0.03 1 248 . 51 TYR C C 175.5 0.1 1 249 . 51 TYR CA C 54.9 0.1 1 250 . 51 TYR CB C 39.5 0.1 1 251 . 52 CYS N N 119.7 0.1 1 252 . 52 CYS H H 9.22 0.03 1 253 . 52 CYS C C 171.9 0.1 1 254 . 52 CYS CA C 56.3 0.1 1 255 . 52 CYS CB C 31.2 0.1 1 256 . 52 CYS HA H 5.56 0.03 1 257 . 53 GLN N N 121.1 0.1 1 258 . 53 GLN H H 8.31 0.03 1 259 . 53 GLN C C 176.7 0.1 1 260 . 53 GLN CA C 54.5 0.1 1 261 . 53 GLN CB C 30.9 0.1 1 262 . 53 GLN HA H 4.19 0.03 1 263 . 54 ILE N N 123.7 0.1 1 264 . 54 ILE H H 8.76 0.03 1 265 . 54 ILE C C 174.3 0.1 1 266 . 54 ILE CA C 61.0 0.1 1 267 . 54 ILE CB C 36.9 0.1 1 268 . 55 ALA N N 123.1 0.1 1 269 . 55 ALA H H 8.71 0.03 1 270 . 55 ALA C C 175.7 0.1 1 271 . 55 ALA CA C 54.0 0.1 1 272 . 55 ALA CB C 18.0 0.1 1 273 . 56 LYS N N 117.8 0.1 1 274 . 56 LYS H H 7.49 0.03 1 275 . 56 LYS C C 177.1 0.1 1 276 . 56 LYS CA C 53.7 0.1 1 277 . 56 LYS CB C 33.2 0.1 1 278 . 56 LYS HA H 4.70 0.03 1 279 . 57 THR N N 117.4 0.1 1 280 . 57 THR H H 8.10 0.03 1 281 . 57 THR C C 173.9 0.1 1 282 . 57 THR CA C 65.0 0.1 1 283 . 57 THR HA H 4.58 0.03 1 284 . 58 CYS N N 127.7 0.1 1 285 . 58 CYS H H 9.15 0.03 1 286 . 58 CYS C C 171.6 0.1 1 287 . 58 CYS CA C 55.2 0.1 1 288 . 58 CYS CB C 27.1 0.1 1 289 . 58 CYS HA H 4.54 0.03 1 290 . 59 PRO C C 175.1 0.1 1 291 . 59 PRO CA C 60.9 0.1 1 292 . 60 ILE N N 124.3 0.1 1 293 . 60 ILE H H 8.92 0.03 1 294 . 60 ILE C C 173.9 0.1 1 295 . 60 ILE CA C 60.0 0.1 1 296 . 60 ILE HA H 3.72 0.03 1 297 . 61 GLN N N 121.4 0.1 1 298 . 61 GLN H H 7.83 0.03 1 299 . 61 GLN C C 174.8 0.1 1 300 . 61 GLN CA C 53.7 0.1 1 301 . 61 GLN CB C 28.2 0.1 1 302 . 61 GLN HA H 4.21 0.03 1 303 . 62 ILE N N 123.7 0.1 1 304 . 62 ILE H H 9.51 0.03 1 305 . 62 ILE C C 174.4 0.1 1 306 . 62 ILE CA C 58.8 0.1 1 307 . 62 ILE CB C 39.4 0.1 1 308 . 62 ILE HA H 4.71 0.03 1 309 . 63 LYS N N 127.8 0.1 1 310 . 63 LYS H H 8.75 0.03 1 311 . 63 LYS C C 174.1 0.1 1 312 . 63 LYS CA C 54.0 0.1 1 313 . 63 LYS CB C 36.1 0.1 1 314 . 63 LYS HA H 5.11 0.03 1 315 . 64 VAL N N 113.4 0.1 1 316 . 64 VAL H H 7.94 0.03 1 317 . 64 VAL C C 176.1 0.1 1 318 . 64 VAL CA C 58.5 0.1 1 319 . 64 VAL CB C 34.6 0.1 1 320 . 64 VAL HA H 4.90 0.03 1 321 . 65 MET N N 118.6 0.1 1 322 . 65 MET H H 8.82 0.03 1 323 . 65 MET C C 176.7 0.1 1 324 . 65 MET CA C 55.2 0.1 1 325 . 65 MET CB C 32.6 0.1 1 326 . 65 MET HA H 4.74 0.03 1 327 . 66 THR N N 110.5 0.1 1 328 . 66 THR H H 7.49 0.03 1 329 . 66 THR C C 171.4 0.1 1 330 . 66 THR CA C 57.3 0.1 1 331 . 66 THR HA H 4.77 0.03 1 332 . 69 PRO C C 176.0 0.1 1 333 . 69 PRO CA C 61.6 0.1 1 334 . 69 PRO CB C 31.2 0.1 1 335 . 70 GLN N N 120.1 0.1 1 336 . 70 GLN H H 8.50 0.03 1 337 . 70 GLN C C 177.9 0.1 1 338 . 70 GLN CA C 56.7 0.1 1 339 . 70 GLN CB C 27.5 0.1 1 340 . 71 GLY N N 114.2 0.1 1 341 . 71 GLY H H 9.19 0.03 1 342 . 71 GLY C C 172.9 0.1 1 343 . 71 GLY CA C 44.6 0.1 1 344 . 72 ALA N N 119.4 0.1 1 345 . 72 ALA H H 7.40 0.03 1 346 . 72 ALA C C 177.3 0.1 1 347 . 72 ALA CA C 51.7 0.1 1 348 . 72 ALA CB C 17.7 0.1 1 349 . 72 ALA HA H 4.64 0.03 1 350 . 73 VAL N N 113.8 0.1 1 351 . 73 VAL H H 9.12 0.03 1 352 . 73 VAL C C 173.4 0.1 1 353 . 73 VAL CA C 58.6 0.1 1 354 . 73 VAL CB C 35.6 0.1 1 355 . 73 VAL HA H 5.02 0.03 1 356 . 74 ILE N N 120.1 0.1 1 357 . 74 ILE H H 9.15 0.03 1 358 . 74 ILE C C 176.1 0.1 1 359 . 74 ILE CA C 57.8 0.1 1 360 . 74 ILE CB C 38.5 0.1 1 361 . 74 ILE HA H 5.30 0.03 1 362 . 75 ARG N N 132.2 0.1 1 363 . 75 ARG H H 9.69 0.03 1 364 . 75 ARG C C 173.4 0.1 1 365 . 75 ARG CA C 53.6 0.1 1 366 . 75 ARG CB C 32.2 0.1 1 367 . 75 ARG HA H 5.26 0.03 1 368 . 76 ALA N N 126.8 0.1 1 369 . 76 ALA H H 8.46 0.03 1 370 . 76 ALA C C 175.4 0.1 1 371 . 76 ALA CA C 50.2 0.1 1 372 . 76 ALA CB C 20.2 0.1 1 373 . 76 ALA HA H 5.35 0.03 1 374 . 77 MET N N 120.9 0.1 1 375 . 77 MET H H 8.48 0.03 1 376 . 77 MET C C 172.6 0.1 1 377 . 77 MET CA C 51.3 0.1 1 378 . 78 PRO C C 175.5 0.1 1 379 . 78 PRO CA C 60.3 0.1 1 380 . 78 PRO CB C 30.9 0.1 1 381 . 79 VAL N N 116.7 0.1 1 382 . 79 VAL H H 9.17 0.03 1 383 . 79 VAL C C 174.4 0.1 1 384 . 79 VAL CA C 59.5 0.1 1 385 . 79 VAL CB C 36.7 0.1 1 386 . 79 VAL HA H 4.43 0.03 1 387 . 80 TYR N N 123.2 0.1 1 388 . 80 TYR H H 9.26 0.03 1 389 . 80 TYR C C 175.1 0.1 1 390 . 80 TYR CA C 61.0 0.1 1 391 . 80 TYR CB C 37.3 0.1 1 392 . 81 LYS N N 120.0 0.1 1 393 . 81 LYS H H 8.08 0.03 1 394 . 81 LYS C C 177.3 0.1 1 395 . 81 LYS CA C 57.7 0.1 1 396 . 81 LYS CB C 35.0 0.1 1 397 . 81 LYS HA H 4.33 0.03 1 398 . 82 LYS N N 118.5 0.1 1 399 . 82 LYS H H 9.35 0.03 1 400 . 82 LYS C C 178.0 0.1 1 401 . 82 LYS CA C 56.1 0.1 1 402 . 82 LYS CB C 31.0 0.1 1 403 . 82 LYS HA H 4.28 0.03 1 404 . 83 ALA N N 126.1 0.1 1 405 . 83 ALA H H 8.71 0.03 1 406 . 83 ALA C C 179.6 0.1 1 407 . 83 ALA CA C 54.8 0.1 1 408 . 83 ALA CB C 17.7 0.1 1 409 . 84 GLU N N 114.8 0.1 1 410 . 84 GLU H H 9.36 0.03 1 411 . 84 GLU C C 176.3 0.1 1 412 . 84 GLU CA C 57.7 0.1 1 413 . 84 GLU CB C 27.8 0.1 1 414 . 84 GLU HA H 4.08 0.03 1 415 . 85 HIS N N 116.9 0.1 1 416 . 85 HIS H H 7.70 0.03 1 417 . 85 HIS C C 177.0 0.1 1 418 . 85 HIS CA C 54.2 0.1 1 419 . 85 HIS CB C 32.7 0.1 1 420 . 85 HIS HA H 5.07 0.03 1 421 . 86 VAL N N 117.9 0.1 1 422 . 86 VAL H H 7.39 0.03 1 423 . 86 VAL C C 177.1 0.1 1 424 . 86 VAL CA C 65.5 0.1 1 425 . 86 VAL CB C 31.4 0.1 1 426 . 87 THR N N 112.6 0.1 1 427 . 87 THR H H 8.34 0.03 1 428 . 87 THR C C 174.0 0.1 1 429 . 87 THR CA C 63.2 0.1 1 430 . 87 THR CB C 68.2 0.1 1 431 . 87 THR HA H 4.05 0.03 1 432 . 88 GLU N N 123.8 0.1 1 433 . 88 GLU H H 8.16 0.03 1 434 . 88 GLU C C 175.6 0.1 1 435 . 88 GLU CA C 55.6 0.1 1 436 . 88 GLU CB C 29.6 0.1 1 437 . 88 GLU HA H 4.47 0.03 1 438 . 89 VAL N N 126.2 0.1 1 439 . 89 VAL H H 8.81 0.03 1 440 . 89 VAL C C 176.8 0.1 1 441 . 89 VAL CA C 63.6 0.1 1 442 . 89 VAL CB C 29.6 0.1 1 443 . 89 VAL HA H 3.75 0.03 1 444 . 90 VAL N N 128.7 0.1 1 445 . 90 VAL H H 8.68 0.03 1 446 . 90 VAL C C 174.7 0.1 1 447 . 90 VAL CA C 62.8 0.1 1 448 . 90 VAL CB C 29.8 0.1 1 449 . 91 LYS N N 126.9 0.1 1 450 . 91 LYS H H 7.94 0.03 1 451 . 91 LYS C C 174.6 0.1 1 452 . 91 LYS CA C 54.7 0.1 1 453 . 91 LYS CB C 34.4 0.1 1 454 . 91 LYS HA H 4.86 0.03 1 455 . 92 ARG N N 116.0 0.1 1 456 . 92 ARG H H 8.40 0.03 1 457 . 92 ARG C C 176.0 0.1 1 458 . 92 ARG CA C 56.3 0.1 1 459 . 92 ARG CB C 31.7 0.1 1 460 . 92 ARG HA H 4.51 0.03 1 461 . 93 CYS N N 124.3 0.1 1 462 . 93 CYS H H 8.89 0.03 1 463 . 93 CYS C C 172.3 0.1 1 464 . 93 CYS CA C 55.5 0.1 1 465 . 93 CYS HA H 3.93 0.03 1 466 . 94 PRO C C 178.4 0.1 1 467 . 94 PRO CA C 65.1 0.1 1 468 . 94 PRO CB C 31.1 0.1 1 469 . 95 ASN N N 114.2 0.1 1 470 . 95 ASN H H 8.09 0.03 1 471 . 95 ASN C C 178.1 0.1 1 472 . 95 ASN CA C 55.8 0.1 1 473 . 95 ASN CB C 37.9 0.1 1 474 . 95 ASN HA H 4.34 0.03 1 475 . 96 HIS N N 119.5 0.1 1 476 . 96 HIS H H 8.98 0.03 1 477 . 96 HIS C C 177.9 0.1 1 478 . 96 HIS CA C 61.8 0.1 1 479 . 96 HIS CB C 29.9 0.1 1 480 . 96 HIS HA H 4.45 0.03 1 481 . 97 GLU N N 123.2 0.1 1 482 . 97 GLU H H 9.08 0.03 1 483 . 97 GLU C C 176.6 0.1 1 484 . 97 GLU CA C 59.0 0.1 1 485 . 97 GLU CB C 29.4 0.1 1 486 . 98 LEU N N 113.7 0.1 1 487 . 98 LEU H H 7.79 0.03 1 488 . 98 LEU C C 177.8 0.1 1 489 . 98 LEU CA C 54.5 0.1 1 490 . 98 LEU CB C 41.1 0.1 1 491 . 98 LEU HA H 4.27 0.03 1 492 . 99 SER N N 113.3 0.1 1 493 . 99 SER H H 7.02 0.03 1 494 . 99 SER C C 174.8 0.1 1 495 . 99 SER CA C 57.4 0.1 1 496 . 99 SER HA H 4.42 0.03 1 497 . 100 ARG C C 175.4 0.1 1 498 . 100 ARG CA C 62.2 0.1 1 499 . 101 GLU N N 123.8 0.1 1 500 . 101 GLU H H 8.57 0.03 1 501 . 101 GLU C C 177.4 0.1 1 502 . 101 GLU CA C 52.2 0.1 1 503 . 102 PHE C C 175.3 0.1 1 504 . 102 PHE CA C 58.2 0.1 1 505 . 102 PHE HA H 4.33 0.03 1 506 . 103 ASN N N 118.0 0.1 1 507 . 103 ASN H H 7.85 0.03 1 508 . 103 ASN C C 175.8 0.1 1 509 . 103 ASN CA C 52.8 0.1 1 510 . 103 ASN CB C 39.6 0.1 1 511 . 103 ASN HA H 5.07 0.03 1 512 . 104 GLU N N 122.2 0.1 1 513 . 104 GLU H H 8.30 0.03 1 514 . 104 GLU C C 177.6 0.1 1 515 . 104 GLU CA C 57.1 0.1 1 516 . 104 GLU CB C 29.3 0.1 1 517 . 104 GLU HA H 4.54 0.03 1 518 . 105 GLY N N 113.1 0.1 1 519 . 105 GLY H H 9.04 0.03 1 520 . 105 GLY C C 173.8 0.1 1 521 . 105 GLY CA C 45.5 0.1 1 522 . 105 GLY HA2 H 5.10 0.03 1 523 . 105 GLY HA3 H 5.10 0.03 1 524 . 106 GLN N N 116.9 0.1 1 525 . 106 GLN H H 7.81 0.03 1 526 . 106 GLN C C 175.9 0.1 1 527 . 106 GLN CA C 53.7 0.1 1 528 . 106 GLN CB C 28.2 0.1 1 529 . 107 ILE N N 118.9 0.1 1 530 . 107 ILE H H 8.11 0.03 1 531 . 107 ILE C C 176.4 0.1 1 532 . 107 ILE CA C 61.0 0.1 1 533 . 107 ILE CB C 38.0 0.1 1 534 . 108 ALA N N 125.4 0.1 1 535 . 108 ALA H H 7.95 0.03 1 536 . 108 ALA C C 174.3 0.1 1 537 . 108 ALA CA C 49.8 0.1 1 538 . 108 ALA CB C 16.8 0.1 1 539 . 110 PRO C C 176.7 0.1 1 540 . 110 PRO CA C 62.7 0.1 1 541 . 110 PRO CB C 31.0 0.1 1 542 . 111 SER N N 117.1 0.1 1 543 . 111 SER H H 8.38 0.03 1 544 . 111 SER C C 172.7 0.1 1 545 . 111 SER CA C 55.7 0.1 1 546 . 111 SER HA H 4.74 0.03 1 547 . 115 ARG CA C 53.2 0.1 1 548 . 116 VAL N N 118.9 0.1 1 549 . 116 VAL H H 7.68 0.03 1 550 . 116 VAL C C 175.2 0.1 1 551 . 116 VAL CA C 60.1 0.1 1 552 . 116 VAL CB C 33.0 0.1 1 553 . 116 VAL HA H 4.29 0.03 1 554 . 117 GLU N N 130.2 0.1 1 555 . 117 GLU H H 8.57 0.03 1 556 . 117 GLU C C 175.9 0.1 1 557 . 117 GLU CA C 53.7 0.1 1 558 . 117 GLU CB C 30.5 0.1 1 559 . 117 GLU HA H 4.78 0.03 1 560 . 118 GLY N N 111.0 0.1 1 561 . 118 GLY H H 8.67 0.03 1 562 . 118 GLY C C 174.1 0.1 1 563 . 118 GLY CA C 45.8 0.1 1 564 . 119 ASN N N 115.9 0.1 1 565 . 119 ASN H H 7.97 0.03 1 566 . 119 ASN C C 175.7 0.1 1 567 . 119 ASN CA C 52.1 0.1 1 568 . 119 ASN CB C 39.6 0.1 1 569 . 119 ASN HA H 4.89 0.03 1 570 . 120 SER C C 174.3 0.1 1 571 . 120 SER CA C 59.5 0.1 1 572 . 120 SER CB C 62.2 0.1 1 573 . 121 HIS N N 119.1 0.1 1 574 . 121 HIS H H 8.87 0.03 1 575 . 121 HIS C C 174.2 0.1 1 576 . 121 HIS CA C 54.6 0.1 1 577 . 121 HIS CB C 28.6 0.1 1 578 . 121 HIS HA H 4.75 0.03 1 579 . 122 ALA N N 121.3 0.1 1 580 . 122 ALA H H 7.11 0.03 1 581 . 122 ALA C C 176.7 0.1 1 582 . 122 ALA CA C 52.0 0.1 1 583 . 122 ALA CB C 17.9 0.1 1 584 . 122 ALA HA H 4.70 0.03 1 585 . 123 GLN N N 121.8 0.1 1 586 . 123 GLN H H 9.08 0.03 1 587 . 123 GLN C C 173.2 0.1 1 588 . 123 GLN CA C 53.9 0.1 1 589 . 123 GLN CB C 31.1 0.1 1 590 . 123 GLN HA H 4.70 0.03 1 591 . 124 TYR N N 125.3 0.1 1 592 . 124 TYR H H 8.94 0.03 1 593 . 124 TYR C C 175.8 0.1 1 594 . 124 TYR CA C 58.1 0.1 1 595 . 124 TYR CB C 39.8 0.1 1 596 . 124 TYR HA H 4.79 0.03 1 597 . 125 VAL N N 122.0 0.1 1 598 . 125 VAL H H 9.24 0.03 1 599 . 125 VAL C C 173.9 0.1 1 600 . 125 VAL CA C 60.0 0.1 1 601 . 125 VAL CB C 34.5 0.1 1 602 . 125 VAL HA H 4.72 0.03 1 603 . 126 GLU N N 121.6 0.1 1 604 . 126 GLU H H 8.30 0.03 1 605 . 126 GLU C C 175.4 0.1 1 606 . 126 GLU CA C 53.8 0.1 1 607 . 126 GLU CB C 32.0 0.1 1 608 . 126 GLU HA H 5.07 0.03 1 609 . 127 ASP N N 128.8 0.1 1 610 . 127 ASP H H 8.57 0.03 1 611 . 127 ASP C C 176.0 0.1 1 612 . 127 ASP CA C 51.8 0.1 1 613 . 127 ASP CB C 42.6 0.1 1 614 . 127 ASP HA H 4.84 0.03 1 615 . 128 PRO C C 176.9 0.1 1 616 . 128 PRO CA C 63.8 0.1 1 617 . 128 PRO CB C 31.3 0.1 1 618 . 129 ILE N N 118.2 0.1 1 619 . 129 ILE H H 8.48 0.03 1 620 . 129 ILE C C 178.0 0.1 1 621 . 129 ILE CA C 62.0 0.1 1 622 . 129 ILE HA H 4.14 0.03 1 623 . 130 THR N N 108.2 0.1 1 624 . 130 THR H H 8.39 0.03 1 625 . 130 THR C C 176.6 0.1 1 626 . 130 THR CA C 61.7 0.1 1 627 . 130 THR CB C 70.6 0.1 1 628 . 130 THR HA H 4.33 0.03 1 629 . 131 GLY N N 109.6 0.1 1 630 . 131 GLY H H 8.18 0.03 1 631 . 131 GLY C C 174.1 0.1 1 632 . 131 GLY CA C 45.0 0.1 1 633 . 131 GLY HA2 H 4.22 0.03 1 634 . 131 GLY HA3 H 4.22 0.03 1 635 . 132 ARG N N 116.9 0.1 1 636 . 132 ARG H H 7.90 0.03 1 637 . 132 ARG C C 176.4 0.1 1 638 . 132 ARG CA C 57.7 0.1 1 639 . 132 ARG CB C 29.5 0.1 1 640 . 132 ARG HA H 3.99 0.03 1 641 . 133 GLN N N 124.7 0.1 1 642 . 133 GLN H H 7.98 0.03 1 643 . 133 GLN C C 175.1 0.1 1 644 . 133 GLN CA C 53.7 0.1 1 645 . 133 GLN HA H 4.70 0.03 1 646 . 134 SER N N 114.0 0.1 1 647 . 134 SER H H 9.09 0.03 1 648 . 134 SER C C 174.6 0.1 1 649 . 134 SER CA C 57.7 0.1 1 650 . 134 SER HA H 5.07 0.03 1 651 . 135 VAL N N 112.8 0.1 1 652 . 135 VAL H H 8.02 0.03 1 653 . 135 VAL C C 173.8 0.1 1 654 . 135 VAL CA C 57.4 0.1 1 655 . 135 VAL HA H 5.46 0.03 1 656 . 136 LEU N N 128.7 0.1 1 657 . 136 LEU H H 9.21 0.03 1 658 . 136 LEU C C 176.2 0.1 1 659 . 136 LEU CA C 52.8 0.1 1 660 . 136 LEU CB C 45.5 0.1 1 661 . 136 LEU HA H 5.65 0.03 1 662 . 137 VAL N N 112.5 0.1 1 663 . 137 VAL H H 8.54 0.03 1 664 . 137 VAL C C 172.7 0.1 1 665 . 137 VAL CA C 57.3 0.1 1 666 . 137 VAL HA H 4.73 0.03 1 667 . 138 PRO C C 177.5 0.1 1 668 . 138 PRO CA C 62.3 0.1 1 669 . 138 PRO CB C 30.8 0.1 1 670 . 139 TYR N N 124.5 0.1 1 671 . 139 TYR H H 8.85 0.03 1 672 . 139 TYR C C 174.0 0.1 1 673 . 139 TYR CA C 59.6 0.1 1 674 . 139 TYR CB C 37.1 0.1 1 675 . 139 TYR HA H 3.91 0.03 1 676 . 140 GLU N N 129.7 0.1 1 677 . 140 GLU H H 6.88 0.03 1 678 . 140 GLU C C 170.6 0.1 1 679 . 140 GLU CA C 51.6 0.1 1 680 . 140 GLU CB C 30.6 0.1 1 681 . 140 GLU HA H 4.49 0.03 1 682 . 142 PRO C C 177.2 0.1 1 683 . 142 PRO CA C 62.2 0.1 1 684 . 142 PRO CB C 31.5 0.1 1 685 . 143 GLN N N 121.2 0.1 1 686 . 143 GLN H H 8.30 0.03 1 687 . 143 GLN C C 176.2 0.1 1 688 . 143 GLN CA C 55.2 0.1 1 689 . 143 GLN CB C 28.3 0.1 1 690 . 143 GLN HA H 4.18 0.03 1 691 . 144 VAL N N 122.2 0.1 1 692 . 144 VAL H H 8.36 0.03 1 693 . 144 VAL C C 177.0 0.1 1 694 . 144 VAL CA C 63.8 0.1 1 695 . 144 VAL CB C 30.8 0.1 1 696 . 144 VAL HA H 3.86 0.03 1 697 . 145 GLY N N 114.1 0.1 1 698 . 145 GLY H H 8.85 0.03 1 699 . 145 GLY C C 174.0 0.1 1 700 . 145 GLY CA C 44.3 0.1 1 701 . 145 GLY HA2 H 3.76 0.03 1 702 . 145 GLY HA3 H 3.76 0.03 1 703 . 146 THR N N 113.0 0.1 1 704 . 146 THR H H 8.15 0.03 1 705 . 146 THR C C 173.2 0.1 1 706 . 146 THR CA C 59.9 0.1 1 707 . 146 THR CB C 70.8 0.1 1 708 . 147 GLU N N 118.4 0.1 1 709 . 147 GLU H H 8.39 0.03 1 710 . 147 GLU C C 175.4 0.1 1 711 . 147 GLU CA C 56.0 0.1 1 712 . 147 GLU CB C 30.4 0.1 1 713 . 147 GLU HA H 4.28 0.03 1 714 . 148 PHE N N 114.7 0.1 1 715 . 148 PHE H H 7.47 0.03 1 716 . 148 PHE C C 175.4 0.1 1 717 . 148 PHE CA C 55.4 0.1 1 718 . 148 PHE CB C 41.9 0.1 1 719 . 148 PHE HA H 5.28 0.03 1 720 . 149 THR N N 121.3 0.1 1 721 . 149 THR H H 9.45 0.03 1 722 . 149 THR C C 173.4 0.1 1 723 . 149 THR CA C 62.6 0.1 1 724 . 149 THR CB C 69.8 0.1 1 725 . 149 THR HA H 4.35 0.03 1 726 . 150 THR N N 124.5 0.1 1 727 . 150 THR H H 8.91 0.03 1 728 . 150 THR C C 174.1 0.1 1 729 . 150 THR CA C 61.9 0.1 1 730 . 150 THR HA H 5.10 0.03 1 731 . 151 VAL N N 130.2 0.1 1 732 . 151 VAL H H 8.90 0.03 1 733 . 151 VAL C C 172.4 0.1 1 734 . 151 VAL CA C 61.1 0.1 1 735 . 151 VAL CB C 33.3 0.1 1 736 . 151 VAL HA H 3.83 0.03 1 737 . 152 LEU N N 124.7 0.1 1 738 . 152 LEU H H 8.25 0.03 1 739 . 152 LEU C C 174.7 0.1 1 740 . 152 LEU CA C 52.4 0.1 1 741 . 152 LEU CB C 40.7 0.1 1 742 . 152 LEU HA H 4.50 0.03 1 743 . 153 TYR C C 176.1 0.1 1 744 . 153 TYR CA C 56.3 0.1 1 745 . 154 ASN N N 116.9 0.1 1 746 . 154 ASN H H 8.89 0.03 1 747 . 154 ASN C C 171.9 0.1 1 748 . 154 ASN CA C 50.9 0.1 1 749 . 154 ASN CB C 43.5 0.1 1 750 . 155 PHE N N 121.6 0.1 1 751 . 155 PHE H H 9.94 0.03 1 752 . 155 PHE C C 178.5 0.1 1 753 . 155 PHE CA C 56.7 0.1 1 754 . 155 PHE CB C 43.6 0.1 1 755 . 155 PHE HA H 5.22 0.03 1 756 . 156 MET N N 116.4 0.1 1 757 . 156 MET H H 8.72 0.03 1 758 . 156 MET C C 174.7 0.1 1 759 . 156 MET CA C 54.1 0.1 1 760 . 157 CYS N N 120.1 0.1 1 761 . 157 CYS H H 7.35 0.03 1 762 . 157 CYS C C 173.2 0.1 1 763 . 157 CYS CA C 60.4 0.1 1 764 . 157 CYS HA H 4.03 0.03 1 765 . 158 ASN N N 118.1 0.1 1 766 . 158 ASN H H 8.30 0.03 1 767 . 158 ASN C C 177.2 0.1 1 768 . 158 ASN CA C 53.4 0.1 1 769 . 158 ASN CB C 40.0 0.1 1 770 . 159 SER N N 119.6 0.1 1 771 . 159 SER H H 9.67 0.03 1 772 . 159 SER C C 174.2 0.1 1 773 . 159 SER CA C 63.3 0.1 1 774 . 159 SER HA H 5.62 0.03 1 775 . 160 SER N N 109.1 0.1 1 776 . 160 SER H H 8.15 0.03 1 777 . 160 SER C C 175.4 0.1 1 778 . 160 SER CA C 57.8 0.1 1 779 . 160 SER CB C 63.2 0.1 1 780 . 160 SER HA H 4.22 0.03 1 781 . 161 CYS N N 122.4 0.1 1 782 . 161 CYS H H 7.90 0.03 1 783 . 161 CYS C C 178.4 0.1 1 784 . 161 CYS CA C 64.0 0.1 1 785 . 161 CYS HA H 4.35 0.03 1 786 . 162 VAL N N 129.6 0.1 1 787 . 162 VAL H H 8.76 0.03 1 788 . 162 VAL C C 177.2 0.1 1 789 . 162 VAL CA C 63.9 0.1 1 790 . 162 VAL CB C 38.0 0.1 1 791 . 162 VAL HA H 4.79 0.03 1 792 . 163 GLY N N 110.3 0.1 1 793 . 163 GLY H H 8.77 0.03 1 794 . 163 GLY C C 173.4 0.1 1 795 . 163 GLY CA C 44.4 0.1 1 796 . 164 GLY N N 108.1 0.1 1 797 . 164 GLY H H 7.35 0.03 1 798 . 164 GLY C C 174.5 0.1 1 799 . 164 GLY CA C 43.7 0.1 1 800 . 164 GLY HA2 H 4.62 0.03 1 801 . 164 GLY HA3 H 4.62 0.03 1 802 . 165 MET C C 179.2 0.1 1 803 . 165 MET CA C 59.1 0.1 1 804 . 165 MET CB C 33.6 0.1 1 805 . 166 ASN N N 117.2 0.1 1 806 . 166 ASN H H 8.63 0.03 1 807 . 166 ASN C C 173.6 0.1 1 808 . 166 ASN CA C 54.2 0.1 1 809 . 166 ASN CB C 36.5 0.1 1 810 . 166 ASN HA H 4.07 0.03 1 811 . 167 ARG N N 107.1 0.1 1 812 . 167 ARG H H 9.26 0.03 1 813 . 167 ARG C C 176.0 0.1 1 814 . 167 ARG CA C 57.5 0.1 1 815 . 167 ARG CB C 26.4 0.1 1 816 . 168 ARG N N 123.6 0.1 1 817 . 168 ARG H H 7.97 0.03 1 818 . 168 ARG C C 176.4 0.1 1 819 . 168 ARG CA C 53.7 0.1 1 820 . 168 ARG CB C 30.0 0.1 1 821 . 168 ARG HA H 4.66 0.03 1 822 . 169 PRO C C 177.3 0.1 1 823 . 169 PRO CA C 62.1 0.1 1 824 . 169 PRO CB C 32.8 0.1 1 825 . 170 ILE N N 112.6 0.1 1 826 . 170 ILE H H 7.78 0.03 1 827 . 170 ILE C C 174.2 0.1 1 828 . 170 ILE CA C 58.7 0.1 1 829 . 170 ILE CB C 42.3 0.1 1 830 . 171 LEU N N 118.2 0.1 1 831 . 171 LEU H H 9.45 0.03 1 832 . 171 LEU C C 174.9 0.1 1 833 . 171 LEU CA C 52.0 0.1 1 834 . 171 LEU CB C 43.7 0.1 1 835 . 171 LEU HA H 4.83 0.03 1 836 . 172 ILE C C 173.9 0.1 1 837 . 172 ILE CA C 57.5 0.1 1 838 . 173 ILE N N 125.0 0.1 1 839 . 173 ILE H H 8.80 0.03 1 840 . 173 ILE C C 176.5 0.1 1 841 . 173 ILE CA C 59.8 0.1 1 842 . 173 ILE HA H 4.37 0.03 1 843 . 174 VAL N N 132.0 0.1 1 844 . 174 VAL H H 9.46 0.03 1 845 . 174 VAL C C 176.1 0.1 1 846 . 174 VAL CA C 59.9 0.1 1 847 . 174 VAL CB C 32.3 0.1 1 848 . 174 VAL HA H 5.55 0.03 1 849 . 175 THR N N 115.6 0.1 1 850 . 175 THR H H 9.70 0.03 1 851 . 175 THR C C 172.3 0.1 1 852 . 175 THR CA C 57.3 0.1 1 853 . 175 THR HA H 5.36 0.03 1 854 . 176 LEU N N 123.8 0.1 1 855 . 176 LEU H H 7.71 0.03 1 856 . 176 LEU C C 175.7 0.1 1 857 . 176 LEU CA C 51.9 0.1 1 858 . 176 LEU CB C 41.3 0.1 1 859 . 176 LEU HA H 4.92 0.03 1 860 . 177 GLU N N 125.6 0.1 1 861 . 177 GLU H H 9.51 0.03 1 862 . 177 GLU C C 176.8 0.1 1 863 . 177 GLU CA C 52.7 0.1 1 864 . 177 GLU CB C 33.5 0.1 1 865 . 177 GLU HA H 5.64 0.03 1 866 . 178 THR N N 108.4 0.1 1 867 . 178 THR H H 8.78 0.03 1 868 . 178 THR C C 176.8 0.1 1 869 . 178 THR CA C 60.7 0.1 1 870 . 178 THR CB C 71.2 0.1 1 871 . 178 THR HA H 4.46 0.03 1 872 . 179 ARG N N 121.1 0.1 1 873 . 179 ARG H H 9.31 0.03 1 874 . 179 ARG C C 176.2 0.1 1 875 . 179 ARG CA C 58.0 0.1 1 876 . 179 ARG CB C 28.9 0.1 1 877 . 180 ASP N N 112.8 0.1 1 878 . 180 ASP H H 7.81 0.03 1 879 . 180 ASP C C 176.2 0.1 1 880 . 180 ASP CA C 52.5 0.1 1 881 . 180 ASP CB C 40.0 0.1 1 882 . 180 ASP HA H 4.74 0.03 1 883 . 181 GLY N N 107.4 0.1 1 884 . 181 GLY H H 7.71 0.03 1 885 . 181 GLY C C 174.5 0.1 1 886 . 181 GLY CA C 45.2 0.1 1 887 . 181 GLY HA2 H 4.17 0.03 1 888 . 181 GLY HA3 H 4.17 0.03 1 889 . 182 GLN N N 119.8 0.1 1 890 . 182 GLN H H 7.86 0.03 1 891 . 182 GLN C C 176.3 0.1 1 892 . 182 GLN CA C 54.9 0.1 1 893 . 182 GLN CB C 27.6 0.1 1 894 . 182 GLN HA H 4.34 0.03 1 895 . 183 VAL N N 125.6 0.1 1 896 . 183 VAL H H 8.93 0.03 1 897 . 183 VAL C C 175.7 0.1 1 898 . 183 VAL CA C 64.3 0.1 1 899 . 183 VAL HA H 4.74 0.03 1 900 . 184 LEU N N 128.1 0.1 1 901 . 184 LEU H H 9.69 0.03 1 902 . 184 LEU C C 176.7 0.1 1 903 . 184 LEU CA C 54.0 0.1 1 904 . 185 GLY N N 106.3 0.1 1 905 . 185 GLY H H 7.90 0.03 1 906 . 185 GLY C C 171.2 0.1 1 907 . 185 GLY CA C 44.8 0.1 1 908 . 185 GLY HA2 H 4.62 0.03 1 909 . 185 GLY HA3 H 4.62 0.03 1 910 . 186 ARG N N 125.5 0.1 1 911 . 186 ARG H H 9.91 0.03 1 912 . 186 ARG C C 174.5 0.1 1 913 . 186 ARG CA C 55.7 0.1 1 914 . 186 ARG CB C 34.1 0.1 1 915 . 186 ARG HA H 5.59 0.03 1 916 . 187 ARG N N 127.0 0.1 1 917 . 187 ARG H H 9.82 0.03 1 918 . 187 ARG C C 174.3 0.1 1 919 . 187 ARG CA C 52.9 0.1 1 920 . 187 ARG CB C 34.3 0.1 1 921 . 187 ARG HA H 5.11 0.03 1 922 . 188 CYS N N 117.7 0.1 1 923 . 188 CYS H H 8.58 0.03 1 924 . 188 CYS C C 174.1 0.1 1 925 . 188 CYS CA C 55.2 0.1 1 926 . 188 CYS CB C 30.2 0.1 1 927 . 188 CYS HA H 5.76 0.03 1 928 . 189 PHE N N 119.0 0.1 1 929 . 189 PHE H H 8.11 0.03 1 930 . 189 PHE C C 172.5 0.1 1 931 . 189 PHE CA C 55.3 0.1 1 932 . 189 PHE CB C 39.7 0.1 1 933 . 189 PHE HA H 5.10 0.03 1 934 . 190 GLU N N 122.6 0.1 1 935 . 190 GLU H H 8.77 0.03 1 936 . 190 GLU C C 174.4 0.1 1 937 . 190 GLU CA C 55.4 0.1 1 938 . 190 GLU CB C 29.6 0.1 1 939 . 190 GLU HA H 4.98 0.03 1 940 . 191 ALA N N 124.7 0.1 1 941 . 191 ALA H H 7.93 0.03 1 942 . 191 ALA C C 174.9 0.1 1 943 . 191 ALA CA C 49.8 0.1 1 944 . 191 ALA CB C 20.9 0.1 1 945 . 191 ALA HA H 5.55 0.03 1 946 . 192 ARG N N 123.4 0.1 1 947 . 192 ARG H H 9.01 0.03 1 948 . 192 ARG C C 173.1 0.1 1 949 . 192 ARG CA C 54.3 0.1 1 950 . 192 ARG CB C 32.0 0.1 1 951 . 192 ARG HA H 4.33 0.03 1 952 . 193 ILE N N 129.5 0.1 1 953 . 193 ILE H H 8.53 0.03 1 954 . 193 ILE C C 177.3 0.1 1 955 . 193 ILE CA C 59.3 0.1 1 956 . 193 ILE CB C 36.7 0.1 1 957 . 193 ILE HA H 5.55 0.03 1 958 . 194 CYS N N 123.5 0.1 1 959 . 194 CYS H H 9.62 0.03 1 960 . 194 CYS C C 172.8 0.1 1 961 . 194 CYS CA C 54.6 0.1 1 962 . 194 CYS CB C 31.5 0.1 1 963 . 194 CYS HA H 5.15 0.03 1 964 . 195 ALA N N 122.5 0.1 1 965 . 195 ALA H H 8.58 0.03 1 966 . 195 ALA C C 179.1 0.1 1 967 . 195 ALA CA C 54.6 0.1 1 968 . 195 ALA CB C 18.7 0.1 1 969 . 196 CYS N N 115.9 0.1 1 970 . 196 CYS H H 8.85 0.03 1 971 . 196 CYS C C 171.5 0.1 1 972 . 196 CYS CA C 54.5 0.1 1 973 . 196 CYS CB C 26.9 0.1 1 974 . 196 CYS HA H 4.92 0.03 1 975 . 197 PRO C C 176.5 0.1 1 976 . 197 PRO CA C 65.1 0.1 1 977 . 198 GLY N N 102.8 0.1 1 978 . 198 GLY H H 8.86 0.03 1 979 . 198 GLY C C 176.1 0.1 1 980 . 198 GLY CA C 46.4 0.1 1 981 . 198 GLY HA2 H 3.60 0.03 1 982 . 198 GLY HA3 H 3.60 0.03 1 983 . 199 ARG N N 122.1 0.1 1 984 . 199 ARG H H 7.41 0.03 1 985 . 199 ARG C C 178.7 0.1 1 986 . 199 ARG CA C 58.3 0.1 1 987 . 199 ARG HA H 3.99 0.03 1 988 . 200 ASP N N 122.5 0.1 1 989 . 200 ASP H H 8.00 0.03 1 990 . 200 ASP C C 177.6 0.1 1 991 . 200 ASP CA C 57.0 0.1 1 992 . 200 ASP CB C 39.0 0.1 1 993 . 200 ASP HA H 4.33 0.03 1 994 . 201 ARG N N 120.8 0.1 1 995 . 201 ARG H H 7.81 0.03 1 996 . 201 ARG C C 177.2 0.1 1 997 . 201 ARG CA C 58.7 0.1 1 998 . 201 ARG CB C 27.9 0.1 1 999 . 201 ARG HA H 4.23 0.03 1 1000 . 202 LYS N N 118.4 0.1 1 1001 . 202 LYS H H 7.33 0.03 1 1002 . 202 LYS C C 178.0 0.1 1 1003 . 202 LYS CA C 58.6 0.1 1 1004 . 202 LYS CB C 31.2 0.1 1 1005 . 202 LYS HA H 3.99 0.03 1 1006 . 203 ALA N N 119.8 0.1 1 1007 . 203 ALA H H 7.93 0.03 1 1008 . 203 ALA C C 181.0 0.1 1 1009 . 203 ALA CA C 54.4 0.1 1 1010 . 203 ALA CB C 16.7 0.1 1 1011 . 203 ALA HA H 4.18 0.03 1 1012 . 204 ASP N N 119.5 0.1 1 1013 . 204 ASP H H 8.06 0.03 1 1014 . 204 ASP C C 179.5 0.1 1 1015 . 204 ASP CA C 56.4 0.1 1 1016 . 204 ASP CB C 39.3 0.1 1 1017 . 204 ASP HA H 4.47 0.03 1 1018 . 205 GLU N N 120.3 0.1 1 1019 . 205 GLU H H 8.66 0.03 1 1020 . 205 GLU C C 179.2 0.1 1 1021 . 205 GLU CA C 59.0 0.1 1 1022 . 205 GLU CB C 28.1 0.1 1 1023 . 205 GLU HA H 3.92 0.03 1 1024 . 206 ASP N N 119.9 0.1 1 1025 . 206 ASP H H 8.75 0.03 1 1026 . 206 ASP C C 178.5 0.1 1 1027 . 206 ASP CA C 56.5 0.1 1 1028 . 206 ASP CB C 39.7 0.1 1 1029 . 206 ASP HA H 4.47 0.03 1 1030 . 207 SER N N 114.0 0.1 1 1031 . 207 SER H H 7.84 0.03 1 1032 . 207 SER C C 176.2 0.1 1 1033 . 207 SER CA C 60.6 0.1 1 1034 . 207 SER CB C 62.4 0.1 1 1035 . 207 SER HA H 4.29 0.03 1 1036 . 208 ILE N N 119.9 0.1 1 1037 . 208 ILE H H 7.58 0.03 1 1038 . 208 ILE C C 177.5 0.1 1 1039 . 208 ILE CA C 62.3 0.1 1 1040 . 208 ILE CB C 37.2 0.1 1 1041 . 208 ILE HA H 4.13 0.03 1 1042 . 209 ARG N N 121.5 0.1 1 1043 . 209 ARG H H 7.64 0.03 1 1044 . 209 ARG C C 174.7 0.1 1 1045 . 209 ARG CA C 57.3 0.1 1 1046 . 209 ARG CB C 29.4 0.1 1 1047 . 209 ARG HA H 4.23 0.03 1 1048 . 210 LYS N N 119.6 0.1 1 1049 . 210 LYS H H 8.00 0.03 1 1050 . 210 LYS C C 177.2 0.1 1 1051 . 210 LYS CA C 56.8 0.1 1 1052 . 210 LYS CB C 31.8 0.1 1 1053 . 210 LYS HA H 4.20 0.03 1 1054 . 211 GLN N N 119.5 0.1 1 1055 . 211 GLN H H 8.04 0.03 1 1056 . 211 GLN C C 176.2 0.1 1 1057 . 211 GLN CA C 56.0 0.1 1 1058 . 211 GLN CB C 28.1 0.1 1 1059 . 211 GLN HA H 4.24 0.03 1 1060 . 212 GLN N N 120.3 0.1 1 1061 . 212 GLN H H 8.23 0.03 1 1062 . 212 GLN C C 176.3 0.1 1 1063 . 212 GLN CA C 55.9 0.1 1 1064 . 212 GLN CB C 28.2 0.1 1 1065 . 212 GLN HA H 4.38 0.03 1 1066 . 213 VAL N N 120.4 0.1 1 1067 . 213 VAL H H 8.15 0.03 1 1068 . 213 VAL C C 176.0 0.1 1 1069 . 213 VAL CA C 62.1 0.1 1 1070 . 213 VAL CB C 31.2 0.1 1 1071 . 213 VAL HA H 4.20 0.03 1 1072 . 214 SER N N 116.8 0.1 1 1073 . 214 SER H H 8.27 0.03 1 1074 . 214 SER C C 174.3 0.1 1 1075 . 214 SER CA C 58.0 0.1 1 1076 . 214 SER CB C 63.2 0.1 1 1077 . 214 SER HA H 4.46 0.03 1 1078 . 215 ASP N N 122.4 0.1 1 1079 . 215 ASP H H 8.43 0.03 1 1080 . 215 ASP C C 176.6 0.1 1 1081 . 215 ASP CA C 54.1 0.1 1 1082 . 215 ASP CB C 40.8 0.1 1 1083 . 215 ASP HA H 4.57 0.03 1 1084 . 216 SER N N 116.4 0.1 1 1085 . 216 SER H H 8.40 0.03 1 1086 . 216 SER C C 175.2 0.1 1 1087 . 216 SER CA C 58.7 0.1 1 1088 . 216 SER CB C 62.8 0.1 1 1089 . 216 SER HA H 4.50 0.03 1 1090 . 217 THR N N 115.2 0.1 1 1091 . 217 THR H H 8.23 0.03 1 1092 . 217 THR C C 174.9 0.1 1 1093 . 217 THR CA C 62.2 0.1 1 1094 . 217 THR CB C 69.2 0.1 1 1095 . 217 THR HA H 4.37 0.03 1 1096 . 218 LYS N N 122.6 0.1 1 1097 . 218 LYS H H 8.15 0.03 1 1098 . 218 LYS C C 176.3 0.1 1 1099 . 218 LYS CA C 55.9 0.1 1 1100 . 218 LYS HA H 4.39 0.03 1 1101 . 219 ASN C C 175.8 0.1 1 1102 . 219 ASN CA C 52.8 0.1 1 1103 . 219 ASN CB C 38.3 0.1 1 1104 . 220 GLY N N 109.2 0.1 1 1105 . 220 GLY H H 8.36 0.03 1 1106 . 220 GLY C C 174.1 0.1 1 1107 . 220 GLY CA C 45.1 0.1 1 1108 . 220 GLY HA2 H 4.00 0.03 1 1109 . 220 GLY HA3 H 4.00 0.03 1 1110 . 221 ASP N N 120.5 0.1 1 1111 . 221 ASP H H 8.27 0.03 1 1112 . 221 ASP C C 176.4 0.1 1 1113 . 221 ASP CA C 54.3 0.1 1 1114 . 221 ASP CB C 41.3 0.1 1 1115 . 221 ASP HA H 4.61 0.03 1 1116 . 222 ALA N N 123.3 0.1 1 1117 . 222 ALA H H 8.22 0.03 1 1118 . 222 ALA C C 177.8 0.1 1 1119 . 222 ALA CA C 52.7 0.1 1 1120 . 222 ALA CB C 18.1 0.1 1 1121 . 222 ALA HA H 4.17 0.03 1 1122 . 223 PHE N N 117.9 0.1 1 1123 . 223 PHE H H 8.09 0.03 1 1124 . 223 PHE C C 175.8 0.1 1 1125 . 223 PHE CA C 57.5 0.1 1 1126 . 223 PHE CB C 38.4 0.1 1 1127 . 223 PHE HA H 4.65 0.03 1 1128 . 224 ARG N N 121.7 0.1 1 1129 . 224 ARG H H 7.97 0.03 1 1130 . 224 ARG C C 175.1 0.1 1 1131 . 224 ARG CA C 55.7 0.1 1 1132 . 224 ARG CB C 29.7 0.1 1 1133 . 224 ARG HA H 4.26 0.03 1 1134 . 225 GLN N N 120.6 0.1 1 1135 . 225 GLN H H 8.32 0.03 1 1136 . 225 GLN C C 175.7 0.1 1 1137 . 225 GLN CA C 55.6 0.1 1 1138 . 225 GLN HA H 4.28 0.03 1 1139 . 226 ASN N N 119.5 0.1 1 1140 . 226 ASN H H 8.51 0.03 1 1141 . 226 ASN C C 175.4 0.1 1 1142 . 226 ASN CA C 52.9 0.1 1 1143 . 227 THR N N 113.7 0.1 1 1144 . 227 THR H H 8.15 0.03 1 1145 . 227 THR C C 174.3 0.1 1 1146 . 227 THR CA C 61.7 0.1 1 1147 . 228 HIS N N 123.2 0.1 1 1148 . 228 HIS H H 8.13 0.03 1 1149 . 228 HIS C C 175.2 0.1 1 1150 . 228 HIS CA C 55.6 0.1 1 1151 . 228 HIS HA H 4.36 0.03 1 1152 . 229 GLY N N 109.7 0.1 1 1153 . 229 GLY H H 8.34 0.03 1 1154 . 229 GLY C C 173.8 0.1 1 1155 . 229 GLY CA C 44.7 0.1 1 1156 . 230 ILE N N 119.9 0.1 1 1157 . 230 ILE H H 8.03 0.03 1 1158 . 230 ILE C C 176.0 0.1 1 1159 . 230 ILE CA C 60.6 0.1 1 1160 . 230 ILE CB C 38.0 0.1 1 1161 . 230 ILE HA H 4.22 0.03 1 1162 . 231 GLN N N 124.5 0.1 1 1163 . 231 GLN H H 8.53 0.03 1 1164 . 231 GLN C C 175.5 0.1 1 1165 . 231 GLN CA C 55.1 0.1 1 1166 . 231 GLN CB C 28.6 0.1 1 1167 . 231 GLN HA H 4.42 0.03 1 1168 . 232 MET N N 123.1 0.1 1 1169 . 232 MET H H 8.54 0.03 1 1170 . 232 MET C C 175.5 0.1 1 1171 . 232 MET CA C 55.1 0.1 1 1172 . 232 MET CB C 32.2 0.1 1 1173 . 232 MET HA H 4.57 0.03 1 1174 . 233 THR N N 120.2 0.1 1 1175 . 233 THR H H 7.82 0.03 1 1176 . 233 THR C C 179.0 0.1 1 1177 . 233 THR CA C 62.6 0.1 1 1178 . 233 THR HA H 4.17 0.03 1 stop_ save_