data_5409 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Backbone Chemical Shift Assignments for 2H, 13C, 15N-labeled Human PTB1 Protein ; _BMRB_accession_number 5409 _BMRB_flat_file_name bmr5409.str _Entry_type original _Submission_date 2002-06-28 _Accession_date 2002-07-03 _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 Simpson Peter J . 2 Natalia Davydova . . 3 Curry Stephen . . 4 Matthews Stephen . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 181 "13C chemical shifts" 571 "15N chemical shifts" 181 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2002-08-22 original author . stop_ _Original_release_date 2002-08-22 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; Letter to the Editor: Resonance Assignment and Topology of the 2H, 13C, 15N labeled 29 kDa N-terminal Fragment of the Polypyrimidine Tract Binding Protein (PTB) ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID ? loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Simpson Peter J. . 2 Davydova Natalia . . 3 Curry Stephen . . 4 Matthews Stephen . . stop_ _Journal_abbreviation 'J. Biomol. NMR' _Journal_volume 24 _Journal_issue 1 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 79 _Page_last 80 _Year 2002 _Details . loop_ _Keyword 'polypyrimidine tract binding protein' RNP 'RNA binding' 'splicing regulation' NMR stop_ save_ ################################## # Molecular system description # ################################## save_system_PTB1 _Saveframe_category molecular_system _Mol_system_name PTB1-12 _Abbreviation_common PTB1 _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'PTB1 domains 1 and 2' $PTB1-12 stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state monomer _System_paramagnetic no _System_thiol_state 'all free' loop_ _Biological_function 'RNA binding' stop_ _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_PTB1-12 _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'Human Polypyrimidine Tract Binding Protein' _Name_variant 'Isoform 1' _Abbreviation_common PTB1 _Molecular_mass 28680 _Mol_thiol_state 'all free' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 263 _Mol_residue_sequence ; MRGSHHHHHHGSSRSSGVPS RVIHIRKLPIDVTEGEVISL GLPFGKVTNLLMLKGKNQAF IEMNTEEAANTMVNYYTSVT PVLRGQPIYIQFSNHKELKT DSSPNQARAQAALQAVNSVQ SGNLALAASAAAVDAGMAMA GQSPVLRIIVENLFYPVTLD VLHQIFSKFGTVLKIITFTK NNQFQALLQYADPVSAQHAK LSLDGQNIYNACCTLRIDFS KLTSLNVKYNNDKSRDYTRP DLPSGDSQPSLDQTMAAAFG LSV ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 39 MET 2 40 ARG 3 41 GLY 4 42 SER 5 43 HIS 6 44 HIS 7 45 HIS 8 46 HIS 9 47 HIS 10 48 HIS 11 49 GLY 12 50 SER 13 51 SER 14 52 ARG 15 53 SER 16 54 SER 17 55 GLY 18 56 VAL 19 57 PRO 20 58 SER 21 59 ARG 22 60 VAL 23 61 ILE 24 62 HIS 25 63 ILE 26 64 ARG 27 65 LYS 28 66 LEU 29 67 PRO 30 68 ILE 31 69 ASP 32 70 VAL 33 71 THR 34 72 GLU 35 73 GLY 36 74 GLU 37 75 VAL 38 76 ILE 39 77 SER 40 78 LEU 41 79 GLY 42 80 LEU 43 81 PRO 44 82 PHE 45 83 GLY 46 84 LYS 47 85 VAL 48 86 THR 49 87 ASN 50 88 LEU 51 89 LEU 52 90 MET 53 91 LEU 54 92 LYS 55 93 GLY 56 94 LYS 57 95 ASN 58 96 GLN 59 97 ALA 60 98 PHE 61 99 ILE 62 100 GLU 63 101 MET 64 102 ASN 65 103 THR 66 104 GLU 67 105 GLU 68 106 ALA 69 107 ALA 70 108 ASN 71 109 THR 72 110 MET 73 111 VAL 74 112 ASN 75 113 TYR 76 114 TYR 77 115 THR 78 116 SER 79 117 VAL 80 118 THR 81 119 PRO 82 120 VAL 83 121 LEU 84 122 ARG 85 123 GLY 86 124 GLN 87 125 PRO 88 126 ILE 89 127 TYR 90 128 ILE 91 129 GLN 92 130 PHE 93 131 SER 94 132 ASN 95 133 HIS 96 134 LYS 97 135 GLU 98 136 LEU 99 137 LYS 100 138 THR 101 139 ASP 102 140 SER 103 141 SER 104 142 PRO 105 143 ASN 106 144 GLN 107 145 ALA 108 146 ARG 109 147 ALA 110 148 GLN 111 149 ALA 112 150 ALA 113 151 LEU 114 152 GLN 115 153 ALA 116 154 VAL 117 155 ASN 118 156 SER 119 157 VAL 120 158 GLN 121 159 SER 122 160 GLY 123 161 ASN 124 162 LEU 125 163 ALA 126 164 LEU 127 165 ALA 128 166 ALA 129 167 SER 130 168 ALA 131 169 ALA 132 170 ALA 133 171 VAL 134 172 ASP 135 173 ALA 136 174 GLY 137 175 MET 138 176 ALA 139 177 MET 140 178 ALA 141 179 GLY 142 180 GLN 143 181 SER 144 182 PRO 145 183 VAL 146 184 LEU 147 185 ARG 148 186 ILE 149 187 ILE 150 188 VAL 151 189 GLU 152 190 ASN 153 191 LEU 154 192 PHE 155 193 TYR 156 194 PRO 157 195 VAL 158 196 THR 159 197 LEU 160 198 ASP 161 199 VAL 162 200 LEU 163 201 HIS 164 202 GLN 165 203 ILE 166 204 PHE 167 205 SER 168 206 LYS 169 207 PHE 170 208 GLY 171 209 THR 172 210 VAL 173 211 LEU 174 212 LYS 175 213 ILE 176 214 ILE 177 215 THR 178 216 PHE 179 217 THR 180 218 LYS 181 219 ASN 182 220 ASN 183 221 GLN 184 222 PHE 185 223 GLN 186 224 ALA 187 225 LEU 188 226 LEU 189 227 GLN 190 228 TYR 191 229 ALA 192 230 ASP 193 231 PRO 194 232 VAL 195 233 SER 196 234 ALA 197 235 GLN 198 236 HIS 199 237 ALA 200 238 LYS 201 239 LEU 202 240 SER 203 241 LEU 204 242 ASP 205 243 GLY 206 244 GLN 207 245 ASN 208 246 ILE 209 247 TYR 210 248 ASN 211 249 ALA 212 250 CYS 213 251 CYS 214 252 THR 215 253 LEU 216 254 ARG 217 255 ILE 218 256 ASP 219 257 PHE 220 258 SER 221 259 LYS 222 260 LEU 223 261 THR 224 262 SER 225 263 LEU 226 264 ASN 227 265 VAL 228 266 LYS 229 267 TYR 230 268 ASN 231 269 ASN 232 270 ASP 233 271 LYS 234 272 SER 235 273 ARG 236 274 ASP 237 275 TYR 238 276 THR 239 277 ARG 240 278 PRO 241 279 ASP 242 280 LEU 243 281 PRO 244 282 SER 245 283 GLY 246 284 ASP 247 285 SER 248 286 GLN 249 287 PRO 250 288 SER 251 289 LEU 252 290 ASP 253 291 GLN 254 292 THR 255 293 MET 256 294 ALA 257 295 ALA 258 296 ALA 259 297 PHE 260 298 GLY 261 299 LEU 262 300 SER 263 301 VAL 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 BMRB 6177 PTB1-2 58.94 164 100.00 100.00 1.67e-105 PDB 1SJR "Nmr Structure Of Rrm2 From Human Polypyrimidine Tract Binding Protein Isoform 1 (Ptb1)" 58.94 164 100.00 100.00 1.67e-105 DBJ BAC29560 "unnamed protein product [Mus musculus]" 85.55 489 99.11 99.11 2.00e-156 GB EDL31647 "mCG13402, isoform CRA_d [Mus musculus]" 85.55 489 99.11 99.11 2.00e-156 GB EDL89385 "polypyrimidine tract binding protein 1, isoform CRA_b [Rattus norvegicus]" 85.55 490 98.67 99.11 1.18e-155 GB EDL89387 "polypyrimidine tract binding protein 1, isoform CRA_d [Rattus norvegicus]" 96.20 500 97.23 98.81 4.71e-159 REF NP_001269942 "polypyrimidine tract-binding protein 1 isoform 3 [Mus musculus]" 85.55 489 99.11 99.11 2.00e-156 REF XP_008985119 "PREDICTED: polypyrimidine tract-binding protein 1 isoform X3 [Callithrix jacchus]" 71.86 448 99.47 99.47 2.43e-129 REF XP_008985120 "PREDICTED: polypyrimidine tract-binding protein 1 isoform X3 [Callithrix jacchus]" 71.86 448 99.47 99.47 2.43e-129 REF XP_010330760 "PREDICTED: polypyrimidine tract-binding protein 1 [Saimiri boliviensis boliviensis]" 95.06 651 98.80 99.20 1.33e-156 REF XP_010805519 "PREDICTED: polypyrimidine tract-binding protein 1 isoform X1 [Bos taurus]" 95.06 527 98.40 99.20 2.01e-157 SP Q00438 "RecName: Full=Polypyrimidine tract-binding protein 1; Short=PTB; AltName: Full=Heterogeneous nuclear ribonucleoprotein I; Short" 95.06 555 97.20 98.80 5.00e-156 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $PTB1-12 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 $PTB1-12 'recombinant technology' . . . . . 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 $PTB1-12 0.5 mM '[U-80% 2H; U-13C; U-15N]' DTT 10 mM . stop_ save_ ############################ # Computer software used # ############################ save_Aurelia _Saveframe_category software _Name Aurelia _Version 2.8.11 loop_ _Task 'Strip-based backbone assignment' stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model DRX _Field_strength 500 _Details . save_ ############################# # NMR applied experiments # ############################# save_1H-15N_HSQC_1 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-15N HSQC' _Sample_label . save_ save_CT-HNCA_2 _Saveframe_category NMR_applied_experiment _Experiment_name CT-HNCA _Sample_label . save_ save_2H-dec_CT-HN(CO)CA_3 _Saveframe_category NMR_applied_experiment _Experiment_name '2H-dec CT-HN(CO)CA' _Sample_label . save_ save_2H-dec_HNCO_4 _Saveframe_category NMR_applied_experiment _Experiment_name '2H-dec HNCO' _Sample_label . save_ save_HN(CA)CO_5 _Saveframe_category NMR_applied_experiment _Experiment_name HN(CA)CO _Sample_label . save_ save_2H-dec_CT-HNCACB_6 _Saveframe_category NMR_applied_experiment _Experiment_name '2H-dec CT-HNCACB' _Sample_label . save_ save_CBCA(CO)NH_7 _Saveframe_category NMR_applied_experiment _Experiment_name CBCA(CO)NH _Sample_label . save_ save_NMR_spec_expt__0_1 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-15N HSQC' _BMRB_pulse_sequence_accession_number . _Details 'The CBCA expt. started with steady-state Ca,Cb magnetisation.' save_ save_NMR_spec_expt__0_2 _Saveframe_category NMR_applied_experiment _Experiment_name CT-HNCA _BMRB_pulse_sequence_accession_number . _Details 'The CBCA expt. started with steady-state Ca,Cb magnetisation.' save_ save_NMR_spec_expt__0_3 _Saveframe_category NMR_applied_experiment _Experiment_name '2H-dec CT-HN(CO)CA' _BMRB_pulse_sequence_accession_number . _Details 'The CBCA expt. started with steady-state Ca,Cb magnetisation.' save_ save_NMR_spec_expt__0_4 _Saveframe_category NMR_applied_experiment _Experiment_name '2H-dec HNCO' _BMRB_pulse_sequence_accession_number . _Details 'The CBCA expt. started with steady-state Ca,Cb magnetisation.' save_ save_NMR_spec_expt__0_5 _Saveframe_category NMR_applied_experiment _Experiment_name HN(CA)CO _BMRB_pulse_sequence_accession_number . _Details 'The CBCA expt. started with steady-state Ca,Cb magnetisation.' save_ save_NMR_spec_expt__0_6 _Saveframe_category NMR_applied_experiment _Experiment_name '2H-dec CT-HNCACB' _BMRB_pulse_sequence_accession_number . _Details 'The CBCA expt. started with steady-state Ca,Cb magnetisation.' save_ save_NMR_spec_expt__0_7 _Saveframe_category NMR_applied_experiment _Experiment_name CBCA(CO)NH _BMRB_pulse_sequence_accession_number . _Details 'The CBCA expt. started with steady-state Ca,Cb magnetisation.' save_ ####################### # Sample conditions # ####################### save_Cond_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH* 6.0 0.2 n/a temperature 298 2 K 'ionic strength' 0.2 0.02 M 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 H 1 'methyl protons' ppm 0.0 internal direct . . . 1.0 DSS N 15 'methyl protons' ppm 0.0 . indirect . . . 0.101329118 DSS C 13 'methyl protons' ppm 0.0 . indirect . . . 0.251449530 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 ; The unstructured region linking domains 1 and 2 could not be assigned due to spectral overlap. ; loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $Cond_1 _Chem_shift_reference_set_label $chemical_shift_reference _Mol_system_component_name 'PTB1 domains 1 and 2' _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 54 16 SER C C 174.71 0.1 1 2 54 16 SER CA C 57.90 0.1 1 3 54 16 SER CB C 63.34 0.1 1 4 55 17 GLY C C 173.33 0.1 1 5 55 17 GLY CA C 44.26 0.1 1 6 55 17 GLY N N 111.63 0.1 1 7 55 17 GLY H H 8.38 0.02 1 8 56 18 VAL C C 174.50 0.1 1 9 56 18 VAL CA C 58.97 0.1 1 10 56 18 VAL CB C 32.15 0.1 1 11 56 18 VAL N N 123.44 0.1 1 12 56 18 VAL H H 8.12 0.02 1 13 57 19 PRO C C 175.30 0.1 1 14 57 19 PRO CA C 62.42 0.1 1 15 57 19 PRO CB C 30.77 0.1 1 16 58 20 SER C C 173.08 0.1 1 17 58 20 SER CA C 55.91 0.1 1 18 58 20 SER CB C 63.95 0.1 1 19 58 20 SER N N 116.44 0.1 1 20 58 20 SER H H 7.33 0.02 1 21 59 21 ARG C C 174.66 0.1 1 22 59 21 ARG CA C 56.06 0.1 1 23 59 21 ARG CB C 30.85 0.1 1 24 59 21 ARG N N 120.55 0.1 1 25 59 21 ARG H H 8.51 0.02 1 26 60 22 VAL C C 174.36 0.1 1 27 60 22 VAL CA C 61.42 0.1 1 28 60 22 VAL CB C 31.54 0.1 1 29 60 22 VAL N N 120.94 0.1 1 30 60 22 VAL H H 8.56 0.02 1 31 61 23 ILE C C 173.73 0.1 1 32 61 23 ILE CA C 58.82 0.1 1 33 61 23 ILE CB C 39.66 0.1 1 34 61 23 ILE N N 131.02 0.1 1 35 61 23 ILE H H 9.44 0.02 1 36 62 24 HIS C C 173.30 0.1 1 37 62 24 HIS CA C 52.53 0.1 1 38 62 24 HIS CB C 34.53 0.1 1 39 62 24 HIS N N 130.25 0.1 1 40 62 24 HIS H H 9.34 0.02 1 41 63 25 ILE C C 174.47 0.1 1 42 63 25 ILE CA C 59.35 0.1 1 43 63 25 ILE CB C 38.82 0.1 1 44 63 25 ILE N N 129.54 0.1 1 45 63 25 ILE H H 9.18 0.02 1 46 64 26 ARG C C 174.01 0.1 1 47 64 26 ARG CA C 53.76 0.1 1 48 64 26 ARG CB C 33.99 0.1 1 49 64 26 ARG N N 125.05 0.1 1 50 64 26 ARG H H 8.82 0.02 1 51 65 27 LYS C C 175.10 0.1 1 52 65 27 LYS CA C 56.14 0.1 1 53 65 27 LYS CB C 28.78 0.1 1 54 65 27 LYS N N 115.93 0.1 1 55 65 27 LYS H H 8.55 0.02 1 56 66 28 LEU C C 175.01 0.1 1 57 66 28 LEU CA C 52.69 0.1 1 58 66 28 LEU CB C 41.27 0.1 1 59 66 28 LEU N N 117.34 0.1 1 60 66 28 LEU H H 7.79 0.02 1 61 67 29 PRO C C 177.55 0.1 1 62 67 29 PRO CA C 61.65 0.1 1 63 67 29 PRO CB C 31.31 0.1 1 64 68 30 ILE C C 175.48 0.1 1 65 68 30 ILE CA C 62.42 0.1 1 66 68 30 ILE CB C 37.75 0.1 1 67 68 30 ILE N N 122.67 0.1 1 68 68 30 ILE H H 8.40 0.02 1 69 69 31 ASP C C 175.48 0.1 1 70 69 31 ASP CA C 52.84 0.1 1 71 69 31 ASP CB C 38.89 0.1 1 72 69 31 ASP N N 119.39 0.1 1 73 69 31 ASP H H 8.30 0.02 1 74 70 32 VAL C C 173.53 0.1 1 75 70 32 VAL CA C 61.42 0.1 1 76 70 32 VAL CB C 31.31 0.1 1 77 70 32 VAL N N 119.39 0.1 1 78 70 32 VAL H H 6.94 0.02 1 79 71 33 THR C C 175.59 0.1 1 80 71 33 THR CA C 59.43 0.1 1 81 71 33 THR CB C 71.54 0.1 1 82 71 33 THR N N 117.34 0.1 1 83 71 33 THR H H 8.11 0.02 1 84 72 34 GLU C C 178.76 0.1 1 85 72 34 GLU CA C 60.20 0.1 1 86 72 34 GLU CB C 28.70 0.1 1 87 72 34 GLU N N 122.86 0.1 1 88 72 34 GLU H H 9.28 0.02 1 89 73 35 GLY C C 177.01 0.1 1 90 73 35 GLY CA C 46.48 0.1 1 91 73 35 GLY N N 105.59 0.1 1 92 73 35 GLY H H 8.67 0.02 1 93 74 36 GLU C C 178.55 0.1 1 94 74 36 GLU CA C 58.36 0.1 1 95 74 36 GLU CB C 30.31 0.1 1 96 74 36 GLU N N 122.73 0.1 1 97 74 36 GLU H H 7.63 0.02 1 98 75 37 VAL C C 177.77 0.1 1 99 75 37 VAL CA C 66.10 0.1 1 100 75 37 VAL CB C 30.54 0.1 1 101 75 37 VAL N N 120.61 0.1 1 102 75 37 VAL H H 7.41 0.02 1 103 76 38 ILE C C 178.97 0.1 1 104 76 38 ILE CA C 65.18 0.1 1 105 76 38 ILE CB C 37.75 0.1 1 106 76 38 ILE N N 120.04 0.1 1 107 76 38 ILE H H 8.47 0.02 1 108 77 39 SER C C 175.30 0.1 1 109 77 39 SER CA C 62.19 0.1 1 110 77 39 SER CB C 62.34 0.1 1 111 77 39 SER N N 115.67 0.1 1 112 77 39 SER H H 7.86 0.02 1 113 78 40 LEU C C 179.58 0.1 1 114 78 40 LEU CA C 56.06 0.1 1 115 78 40 LEU CB C 42.11 0.1 1 116 78 40 LEU N N 121.26 0.1 1 117 78 40 LEU H H 7.48 0.02 1 118 79 41 GLY C C 173.55 0.1 1 119 79 41 GLY CA C 45.41 0.1 1 120 79 41 GLY N N 103.28 0.1 1 121 79 41 GLY H H 7.92 0.02 1 122 80 42 LEU C C 175.37 0.1 1 123 80 42 LEU CA C 57.29 0.1 1 124 80 42 LEU CB C 39.51 0.1 1 125 80 42 LEU N N 121.64 0.1 1 126 80 42 LEU H H 7.16 0.02 1 127 81 43 PRO C C 176.45 0.1 1 128 81 43 PRO CA C 64.03 0.1 1 129 81 43 PRO CB C 29.93 0.1 1 130 82 44 PHE C C 175.05 0.1 1 131 82 44 PHE CA C 57.29 0.1 1 132 82 44 PHE CB C 40.04 0.1 1 133 82 44 PHE N N 113.74 0.1 1 134 82 44 PHE H H 7.74 0.02 1 135 83 45 GLY C C 170.12 0.1 1 136 83 45 GLY CA C 45.02 0.1 1 137 83 45 GLY N N 107.52 0.1 1 138 83 45 GLY H H 7.57 0.02 1 139 84 46 LYS C C 174.97 0.1 1 140 84 46 LYS CA C 54.30 0.1 1 141 84 46 LYS CB C 33.53 0.1 1 142 84 46 LYS N N 120.16 0.1 1 143 84 46 LYS H H 7.51 0.02 1 144 85 47 VAL C C 177.12 0.1 1 145 85 47 VAL CA C 61.27 0.1 1 146 85 47 VAL CB C 31.61 0.1 1 147 85 47 VAL N N 126.40 0.1 1 148 85 47 VAL H H 8.03 0.02 1 149 86 48 THR C C 175.07 0.1 1 150 86 48 THR CA C 61.96 0.1 1 151 86 48 THR CB C 67.71 0.1 1 152 86 48 THR N N 122.54 0.1 1 153 86 48 THR H H 9.17 0.02 1 154 87 49 ASN C C 171.92 0.1 1 155 87 49 ASN CA C 52.69 0.1 1 156 87 49 ASN CB C 41.73 0.1 1 157 87 49 ASN N N 119.46 0.1 1 158 87 49 ASN H H 7.72 0.02 1 159 88 50 LEU C C 173.86 0.1 1 160 88 50 LEU CA C 53.84 0.1 1 161 88 50 LEU CB C 44.79 0.1 1 162 88 50 LEU N N 124.08 0.1 1 163 88 50 LEU H H 8.33 0.02 1 164 89 51 LEU C C 174.88 0.1 1 165 89 51 LEU CA C 53.53 0.1 1 166 89 51 LEU CB C 44.72 0.1 1 167 89 51 LEU N N 129.41 0.1 1 168 89 51 LEU H H 9.10 0.02 1 169 90 52 MET C C 175.19 0.1 1 170 90 52 MET CA C 53.76 0.1 1 171 90 52 MET CB C 32.46 0.1 1 172 90 52 MET N N 127.55 0.1 1 173 90 52 MET H H 9.11 0.02 1 174 91 53 LEU C C 176.96 0.1 1 175 91 53 LEU CA C 52.92 0.1 1 176 91 53 LEU CB C 40.43 0.1 1 177 91 53 LEU N N 128.84 0.1 1 178 91 53 LEU H H 8.40 0.02 1 179 92 54 LYS CA C 58.82 0.1 1 180 92 54 LYS CB C 31.69 0.1 1 181 92 54 LYS N N 125.44 0.1 1 182 92 54 LYS H H 8.39 0.02 1 183 93 55 GLY C C 174.37 0.1 1 184 93 55 GLY CA C 45.33 0.1 1 185 93 55 GLY N N 110.28 0.1 1 186 93 55 GLY H H 8.91 0.02 1 187 94 56 LYS C C 175.84 0.1 1 188 94 56 LYS CA C 54.07 0.1 1 189 94 56 LYS CB C 33.15 0.1 1 190 94 56 LYS N N 117.85 0.1 1 191 94 56 LYS H H 7.44 0.02 1 192 95 57 ASN C C 173.91 0.1 1 193 95 57 ASN CA C 53.76 0.1 1 194 95 57 ASN CB C 36.29 0.1 1 195 95 57 ASN N N 117.92 0.1 1 196 95 57 ASN H H 8.22 0.02 1 197 96 58 GLN C C 174.14 0.1 1 198 96 58 GLN CA C 52.99 0.1 1 199 96 58 GLN CB C 34.91 0.1 1 200 96 58 GLN N N 114.38 0.1 1 201 96 58 GLN H H 7.38 0.02 1 202 97 59 ALA C C 174.36 0.1 1 203 97 59 ALA CA C 50.77 0.1 1 204 97 59 ALA CB C 23.95 0.1 1 205 97 59 ALA N N 121.32 0.1 1 206 97 59 ALA H H 8.86 0.02 1 207 98 60 PHE C C 175.08 0.1 1 208 98 60 PHE CA C 55.68 0.1 1 209 98 60 PHE CB C 41.88 0.1 1 210 98 60 PHE N N 119.14 0.1 1 211 98 60 PHE H H 9.18 0.02 1 212 99 61 ILE C C 172.60 0.1 1 213 99 61 ILE CA C 58.66 0.1 1 214 99 61 ILE CB C 41.65 0.1 1 215 99 61 ILE N N 120.55 0.1 1 216 99 61 ILE H H 9.18 0.02 1 217 100 62 GLU C C 174.95 0.1 1 218 100 62 GLU CA C 53.76 0.1 1 219 100 62 GLU CB C 33.07 0.1 1 220 100 62 GLU N N 128.45 0.1 1 221 100 62 GLU H H 8.58 0.02 1 222 101 63 MET C C 177.68 0.1 1 223 101 63 MET CA C 51.31 0.1 1 224 101 63 MET CB C 31.92 0.1 1 225 101 63 MET N N 124.28 0.1 1 226 101 63 MET H H 8.75 0.02 1 227 102 64 ASN C C 175.01 0.1 1 228 102 64 ASN CA C 55.91 0.1 1 229 102 64 ASN CB C 37.06 0.1 1 230 102 64 ASN N N 118.17 0.1 1 231 102 64 ASN H H 9.07 0.02 1 232 103 65 THR C C 174.26 0.1 1 233 103 65 THR CA C 58.20 0.1 1 234 103 65 THR CB C 72.84 0.1 1 235 103 65 THR N N 106.16 0.1 1 236 103 65 THR H H 7.24 0.02 1 237 104 66 GLU C C 178.64 0.1 1 238 104 66 GLU CA C 59.12 0.1 1 239 104 66 GLU CB C 28.70 0.1 1 240 104 66 GLU N N 124.08 0.1 1 241 104 66 GLU H H 9.30 0.02 1 242 105 67 GLU C C 178.90 0.1 1 243 105 67 GLU CA C 59.73 0.1 1 244 105 67 GLU CB C 28.55 0.1 1 245 105 67 GLU N N 122.35 0.1 1 246 105 67 GLU H H 8.78 0.02 1 247 106 68 ALA C C 179.29 0.1 1 248 106 68 ALA CA C 54.76 0.1 1 249 106 68 ALA CB C 19.43 0.1 1 250 106 68 ALA N N 125.88 0.1 1 251 106 68 ALA H H 8.38 0.02 1 252 107 69 ALA C C 178.28 0.1 1 253 107 69 ALA CA C 54.99 0.1 1 254 107 69 ALA CB C 18.82 0.1 1 255 107 69 ALA N N 119.91 0.1 1 256 107 69 ALA H H 7.45 0.02 1 257 108 70 ASN C C 177.57 0.1 1 258 108 70 ASN CA C 56.37 0.1 1 259 108 70 ASN CB C 38.97 0.1 1 260 108 70 ASN N N 117.79 0.1 1 261 108 70 ASN H H 8.84 0.02 1 262 109 71 THR C C 175.78 0.1 1 263 109 71 THR CA C 66.25 0.1 1 264 109 71 THR CB C 67.71 0.1 1 265 109 71 THR N N 118.43 0.1 1 266 109 71 THR H H 8.60 0.02 1 267 110 72 MET C C 176.45 0.1 1 268 110 72 MET CA C 58.36 0.1 1 269 110 72 MET CB C 32.00 0.1 1 270 110 72 MET N N 124.60 0.1 1 271 110 72 MET H H 7.78 0.02 1 272 111 73 VAL C C 179.00 0.1 1 273 111 73 VAL CA C 66.71 0.1 1 274 111 73 VAL CB C 31.08 0.1 1 275 111 73 VAL N N 119.65 0.1 1 276 111 73 VAL H H 8.12 0.02 1 277 112 74 ASN C C 178.25 0.1 1 278 112 74 ASN CA C 55.98 0.1 1 279 112 74 ASN CB C 37.52 0.1 1 280 112 74 ASN N N 120.10 0.1 1 281 112 74 ASN H H 8.34 0.02 1 282 113 75 TYR C C 177.96 0.1 1 283 113 75 TYR CA C 61.73 0.1 1 284 113 75 TYR CB C 37.97 0.1 1 285 113 75 TYR N N 125.05 0.1 1 286 113 75 TYR H H 8.29 0.02 1 287 114 76 TYR C C 175.59 0.1 1 288 114 76 TYR CA C 58.66 0.1 1 289 114 76 TYR CB C 36.67 0.1 1 290 114 76 TYR N N 117.34 0.1 1 291 114 76 TYR H H 7.79 0.02 1 292 115 77 THR C C 175.03 0.1 1 293 115 77 THR CA C 64.26 0.1 1 294 115 77 THR CB C 68.47 0.1 1 295 115 77 THR N N 114.96 0.1 1 296 115 77 THR H H 7.59 0.02 1 297 116 78 SER C C 173.49 0.1 1 298 116 78 SER CA C 59.12 0.1 1 299 116 78 SER CB C 63.57 0.1 1 300 116 78 SER N N 117.66 0.1 1 301 116 78 SER H H 7.30 0.02 1 302 117 79 VAL C C 174.08 0.1 1 303 117 79 VAL CA C 60.23 0.1 1 304 117 79 VAL CB C 32.61 0.1 1 305 117 79 VAL N N 124.79 0.1 1 306 117 79 VAL H H 7.68 0.02 1 307 118 80 THR C C 172.95 0.1 1 308 118 80 THR CA C 60.27 0.1 1 309 118 80 THR CB C 69.16 0.1 1 310 118 80 THR N N 122.99 0.1 1 311 118 80 THR H H 8.10 0.02 1 312 119 81 PRO C C 173.60 0.1 1 313 119 81 PRO CA C 61.81 0.1 1 314 119 81 PRO CB C 30.01 0.1 1 315 120 82 VAL C C 175.23 0.1 1 316 120 82 VAL CA C 59.12 0.1 1 317 120 82 VAL CB C 35.37 0.1 1 318 120 82 VAL N N 119.46 0.1 1 319 120 82 VAL H H 7.72 0.02 1 320 121 83 LEU C C 175.65 0.1 1 321 121 83 LEU CA C 53.38 0.1 1 322 121 83 LEU CB C 46.17 0.1 1 323 121 83 LEU N N 125.30 0.1 1 324 121 83 LEU H H 8.42 0.02 1 325 122 84 ARG C C 176.68 0.1 1 326 122 84 ARG CA C 55.98 0.1 1 327 122 84 ARG CB C 27.40 0.1 1 328 122 84 ARG N N 123.95 0.1 1 329 122 84 ARG H H 9.45 0.02 1 330 123 85 GLY C C 173.27 0.1 1 331 123 85 GLY CA C 44.87 0.1 1 332 123 85 GLY N N 103.99 0.1 1 333 123 85 GLY H H 8.34 0.02 1 334 124 86 GLN C C 172.27 0.1 1 335 124 86 GLN CA C 51.38 0.1 1 336 124 86 GLN CB C 29.93 0.1 1 337 124 86 GLN N N 123.31 0.1 1 338 124 86 GLN H H 7.96 0.02 1 339 125 87 PRO C C 176.27 0.1 1 340 125 87 PRO CA C 62.04 0.1 1 341 125 87 PRO CB C 31.54 0.1 1 342 126 88 ILE C C 173.62 0.1 1 343 126 88 ILE CA C 58.43 0.1 1 344 126 88 ILE CB C 39.12 0.1 1 345 126 88 ILE N N 118.82 0.1 1 346 126 88 ILE H H 7.72 0.02 1 347 127 89 TYR C C 174.14 0.1 1 348 127 89 TYR CA C 56.06 0.1 1 349 127 89 TYR CB C 40.50 0.1 1 350 127 89 TYR N N 120.23 0.1 1 351 127 89 TYR H H 7.68 0.02 1 352 128 90 ILE C C 173.44 0.1 1 353 128 90 ILE CA C 59.66 0.1 1 354 128 90 ILE CB C 40.20 0.1 1 355 128 90 ILE N N 126.07 0.1 1 356 128 90 ILE H H 8.28 0.02 1 357 129 91 GLN C C 174.65 0.1 1 358 129 91 GLN CA C 53.45 0.1 1 359 129 91 GLN CB C 32.76 0.1 1 360 129 91 GLN N N 123.89 0.1 1 361 129 91 GLN H H 8.39 0.02 1 362 130 92 PHE C C 177.10 0.1 1 363 130 92 PHE CA C 60.04 0.1 1 364 130 92 PHE CB C 39.35 0.1 1 365 130 92 PHE N N 121.51 0.1 1 366 130 92 PHE H H 8.85 0.02 1 367 131 93 SER C C 174.95 0.1 1 368 131 93 SER CA C 56.60 0.1 1 369 131 93 SER CB C 63.95 0.1 1 370 131 93 SER N N 116.82 0.1 1 371 131 93 SER H H 8.79 0.02 1 372 132 94 ASN C C 175.16 0.1 1 373 132 94 ASN CA C 53.15 0.1 1 374 132 94 ASN CB C 37.97 0.1 1 375 132 94 ASN N N 123.38 0.1 1 376 132 94 ASN H H 8.75 0.02 1 377 133 95 HIS CA C 55.91 0.1 1 378 133 95 HIS CB C 30.24 0.1 1 379 133 95 HIS N N 120.30 0.1 1 380 133 95 HIS H H 8.28 0.02 1 381 134 96 LYS C C 176.01 0.1 1 382 134 96 LYS CA C 56.44 0.1 1 383 134 96 LYS CB C 32.38 0.1 1 384 134 96 LYS N N 123.44 0.1 1 385 134 96 LYS H H 8.49 0.02 1 386 135 97 GLU C C 175.21 0.1 1 387 135 97 GLU CA C 54.99 0.1 1 388 135 97 GLU CB C 30.47 0.1 1 389 135 97 GLU N N 119.07 0.1 1 390 135 97 GLU H H 7.89 0.02 1 391 136 98 LEU C C 176.06 0.1 1 392 136 98 LEU CA C 53.91 0.1 1 393 136 98 LEU CB C 41.65 0.1 1 394 136 98 LEU N N 124.15 0.1 1 395 136 98 LEU H H 8.40 0.02 1 396 137 99 LYS C C 176.23 0.1 1 397 137 99 LYS CA C 55.14 0.1 1 398 137 99 LYS CB C 32.46 0.1 1 399 137 99 LYS N N 124.15 0.1 1 400 137 99 LYS H H 8.07 0.02 1 401 138 100 THR C C 174.15 0.1 1 402 138 100 THR CA C 60.81 0.1 1 403 138 100 THR CB C 68.93 0.1 1 404 138 100 THR N N 116.89 0.1 1 405 138 100 THR H H 8.17 0.02 1 406 139 101 ASP C C 175.94 0.1 1 407 139 101 ASP CA C 53.61 0.1 1 408 139 101 ASP CB C 40.58 0.1 1 409 139 101 ASP N N 124.08 0.1 1 410 139 101 ASP H H 8.33 0.02 1 411 140 102 SER C C 174.14 0.1 1 412 140 102 SER CA C 57.59 0.1 1 413 140 102 SER CB C 63.11 0.1 1 414 140 102 SER N N 117.60 0.1 1 415 140 102 SER H H 8.18 0.02 1 416 141 103 SER C C 175.20 0.1 1 417 141 103 SER CA C 56.14 0.1 1 418 141 103 SER CB C 62.73 0.1 1 419 141 103 SER N N 120.87 0.1 1 420 141 103 SER H H 8.28 0.02 1 421 142 104 PRO C C 176.69 0.1 1 422 142 104 PRO CA C 62.73 0.1 1 423 142 104 PRO CB C 31.38 0.1 1 424 143 105 ASN C C 175.04 0.1 1 425 143 105 ASN CA C 52.84 0.1 1 426 143 105 ASN CB C 37.90 0.1 1 427 143 105 ASN N N 119.65 0.1 1 428 143 105 ASN H H 8.36 0.02 1 429 144 106 GLN C C 175.35 0.1 1 430 144 106 GLN CA C 55.37 0.1 1 431 144 106 GLN CB C 28.93 0.1 1 432 144 106 GLN N N 122.16 0.1 1 433 144 106 GLN H H 8.16 0.02 1 434 145 107 ALA C C 177.32 0.1 1 435 145 107 ALA CA C 51.92 0.1 1 436 145 107 ALA CB C 18.89 0.1 1 437 145 107 ALA N N 126.78 0.1 1 438 145 107 ALA H H 8.24 0.02 1 439 146 108 ARG C C 174.82 0.1 1 440 146 108 ARG CA C 55.29 0.1 1 441 146 108 ARG CB C 30.39 0.1 1 442 146 108 ARG N N 122.41 0.1 1 443 146 108 ARG H H 8.19 0.02 1 444 178 140 ALA C C 178.45 0.1 1 445 178 140 ALA CA C 52.54 0.1 1 446 178 140 ALA CB C 18.40 0.1 1 447 179 141 GLY C C 173.92 0.1 1 448 179 141 GLY CA C 44.96 0.1 1 449 179 141 GLY N N 109.96 0.1 1 450 179 141 GLY H H 8.15 0.02 1 451 180 142 GLN C C 175.21 0.1 1 452 180 142 GLN CA C 55.26 0.1 1 453 180 142 GLN CB C 28.86 0.1 1 454 180 142 GLN N N 119.94 0.1 1 455 180 142 GLN H H 7.62 0.02 1 456 181 143 SER C C 173.83 0.1 1 457 181 143 SER CA C 54.38 0.1 1 458 181 143 SER CB C 65.54 0.1 1 459 181 143 SER N N 117.92 0.1 1 460 181 143 SER H H 7.56 0.02 1 461 182 144 PRO CA C 62.05 0.1 1 462 183 145 VAL C C 175.41 0.1 1 463 183 145 VAL CA C 60.34 0.1 1 464 183 145 VAL CB C 31.17 0.1 1 465 183 145 VAL N N 122.41 0.1 1 466 183 145 VAL H H 8.39 0.02 1 467 184 146 LEU C C 175.61 0.1 1 468 184 146 LEU CA C 52.41 0.1 1 469 184 146 LEU CB C 44.38 0.1 1 470 184 146 LEU N N 126.32 0.1 1 471 184 146 LEU H H 9.09 0.02 1 472 185 147 ARG C C 175.03 0.1 1 473 185 147 ARG CA C 55.01 0.1 1 474 185 147 ARG CB C 30.72 0.1 1 475 185 147 ARG N N 123.04 0.1 1 476 185 147 ARG H H 8.97 0.02 1 477 186 148 ILE C C 174.64 0.1 1 478 186 148 ILE CA C 59.62 0.1 1 479 186 148 ILE CB C 40.99 0.1 1 480 186 148 ILE N N 129.90 0.1 1 481 186 148 ILE H H 9.38 0.02 1 482 187 149 ILE C C 175.09 0.1 1 483 187 149 ILE CA C 60.07 0.1 1 484 187 149 ILE CB C 40.43 0.1 1 485 187 149 ILE N N 128.99 0.1 1 486 187 149 ILE H H 9.15 0.02 1 487 188 150 VAL C C 175.50 0.1 1 488 188 150 VAL CA C 60.65 0.1 1 489 188 150 VAL CB C 31.39 0.1 1 490 188 150 VAL N N 125.56 0.1 1 491 188 150 VAL H H 7.96 0.02 1 492 189 151 GLU C C 177.18 0.1 1 493 189 151 GLU CA C 54.69 0.1 1 494 189 151 GLU CB C 31.91 0.1 1 495 189 151 GLU N N 127.34 0.1 1 496 189 151 GLU H H 9.04 0.02 1 497 190 152 ASN C C 176.05 0.1 1 498 190 152 ASN CA C 53.74 0.1 1 499 190 152 ASN CB C 35.87 0.1 1 500 190 152 ASN N N 120.00 0.1 1 501 190 152 ASN H H 8.98 0.02 1 502 191 153 LEU C C 176.61 0.1 1 503 191 153 LEU CA C 54.76 0.1 1 504 191 153 LEU CB C 40.01 0.1 1 505 191 153 LEU N N 125.08 0.1 1 506 191 153 LEU H H 8.30 0.02 1 507 192 154 PHE C C 174.79 0.1 1 508 192 154 PHE CA C 56.47 0.1 1 509 192 154 PHE CB C 38.16 0.1 1 510 192 154 PHE N N 127.27 0.1 1 511 192 154 PHE H H 7.81 0.02 1 512 193 155 TYR C C 172.44 0.1 1 513 193 155 TYR CA C 54.79 0.1 1 514 193 155 TYR CB C 40.09 0.1 1 515 193 155 TYR N N 119.18 0.1 1 516 193 155 TYR H H 7.20 0.02 1 517 194 156 PRO CA C 62.78 0.1 1 518 194 156 PRO CB C 31.39 0.1 1 519 195 157 VAL C C 174.37 0.1 1 520 195 157 VAL CA C 62.27 0.1 1 521 195 157 VAL CB C 32.65 0.1 1 522 195 157 VAL N N 123.54 0.1 1 523 195 157 VAL H H 7.92 0.02 1 524 196 158 THR C C 175.50 0.1 1 525 196 158 THR CA C 59.19 0.1 1 526 196 158 THR CB C 71.63 0.1 1 527 196 158 THR N N 114.64 0.1 1 528 196 158 THR H H 6.62 0.02 1 529 197 159 LEU C C 178.77 0.1 1 530 197 159 LEU CA C 59.29 0.1 1 531 197 159 LEU CB C 41.34 0.1 1 532 197 159 LEU N N 122.53 0.1 1 533 197 159 LEU H H 8.87 0.02 1 534 198 160 ASP C C 179.25 0.1 1 535 198 160 ASP CA C 57.32 0.1 1 536 198 160 ASP CB C 40.37 0.1 1 537 198 160 ASP N N 116.91 0.1 1 538 198 160 ASP H H 8.04 0.02 1 539 199 161 VAL C C 178.40 0.1 1 540 199 161 VAL CA C 66.14 0.1 1 541 199 161 VAL CB C 31.31 0.1 1 542 199 161 VAL N N 122.79 0.1 1 543 199 161 VAL H H 7.49 0.02 1 544 200 162 LEU C C 179.27 0.1 1 545 200 162 LEU CA C 57.86 0.1 1 546 200 162 LEU CB C 40.77 0.1 1 547 200 162 LEU N N 118.49 0.1 1 548 200 162 LEU H H 7.69 0.02 1 549 201 163 HIS C C 178.65 0.1 1 550 201 163 HIS CA C 62.11 0.1 1 551 201 163 HIS CB C 29.31 0.1 1 552 201 163 HIS N N 120.07 0.1 1 553 201 163 HIS H H 9.11 0.02 1 554 202 164 GLN C C 178.96 0.1 1 555 202 164 GLN CA C 59.48 0.1 1 556 202 164 GLN CB C 27.47 0.1 1 557 202 164 GLN N N 122.60 0.1 1 558 202 164 GLN H H 8.39 0.02 1 559 203 165 ILE C C 178.32 0.1 1 560 203 165 ILE CA C 64.46 0.1 1 561 203 165 ILE CB C 38.29 0.1 1 562 203 165 ILE N N 119.12 0.1 1 563 203 165 ILE H H 7.97 0.02 1 564 204 166 PHE C C 181.09 0.1 1 565 205 167 SER C C 174.17 0.1 1 566 205 167 SER CA C 61.73 0.1 1 567 205 167 SER CB C 60.84 0.1 1 568 205 167 SER N N 121.27 0.1 1 569 205 167 SER H H 8.38 0.02 1 570 206 168 LYS C C 177.14 0.1 1 571 206 168 LYS CA C 57.67 0.1 1 572 206 168 LYS CB C 30.94 0.1 1 573 206 168 LYS N N 120.01 0.1 1 574 206 168 LYS H H 6.71 0.02 1 575 207 169 PHE C C 175.05 0.1 1 576 207 169 PHE CA C 57.99 0.1 1 577 207 169 PHE CB C 39.93 0.1 1 578 207 169 PHE N N 113.81 0.1 1 579 207 169 PHE H H 7.03 0.02 1 580 208 170 GLY C C 171.39 0.1 1 581 208 170 GLY CA C 44.80 0.1 1 582 208 170 GLY N N 107.50 0.1 1 583 208 170 GLY H H 7.32 0.02 1 584 209 171 THR C C 174.06 0.1 1 585 209 171 THR CA C 63.06 0.1 1 586 209 171 THR CB C 69.18 0.1 1 587 209 171 THR N N 117.48 0.1 1 588 209 171 THR H H 8.72 0.02 1 589 210 172 VAL C C 175.30 0.1 1 590 210 172 VAL CA C 62.43 0.1 1 591 210 172 VAL CB C 31.17 0.1 1 592 210 172 VAL N N 131.76 0.1 1 593 210 172 VAL H H 9.01 0.02 1 594 211 173 LEU C C 177.30 0.1 1 595 211 173 LEU CA C 56.56 0.1 1 596 211 173 LEU CB C 42.67 0.1 1 597 211 173 LEU N N 127.27 0.1 1 598 211 173 LEU H H 9.12 0.02 1 599 212 174 LYS C C 175.01 0.1 1 600 212 174 LYS CA C 54.69 0.1 1 601 212 174 LYS CB C 39.19 0.1 1 602 212 174 LYS N N 114.45 0.1 1 603 212 174 LYS H H 7.14 0.02 1 604 213 175 ILE CA C 60.81 0.1 1 605 213 175 ILE CB C 42.38 0.1 1 606 213 175 ILE N N 120.45 0.1 1 607 213 175 ILE H H 8.75 0.02 1 608 214 176 ILE C C 174.99 0.1 1 609 214 176 ILE CA C 61.00 0.1 1 610 214 176 ILE CB C 42.15 0.1 1 611 215 177 THR C C 173.12 0.1 1 612 215 177 THR CA C 59.45 0.1 1 613 215 177 THR CB C 71.41 0.1 1 614 215 177 THR N N 117.42 0.1 1 615 215 177 THR H H 8.52 0.02 1 616 216 178 PHE C C 173.26 0.1 1 617 216 178 PHE CA C 56.56 0.1 1 618 216 178 PHE CB C 38.89 0.1 1 619 216 178 PHE N N 117.42 0.1 1 620 216 178 PHE H H 8.32 0.02 1 621 217 179 THR C C 174.63 0.1 1 622 217 179 THR CA C 60.94 0.1 1 623 217 179 THR CB C 70.07 0.1 1 624 217 179 THR N N 115.65 0.1 1 625 217 179 THR H H 8.37 0.02 1 626 218 180 LYS CA C 55.58 0.1 1 627 218 180 LYS CB C 34.80 0.1 1 628 218 180 LYS N N 127.52 0.1 1 629 218 180 LYS H H 8.34 0.02 1 630 219 181 ASN C C 174.94 0.1 1 631 219 181 ASN CA C 54.66 0.1 1 632 219 181 ASN CB C 36.81 0.1 1 633 220 182 ASN C C 174.12 0.1 1 634 220 182 ASN CA C 54.57 0.1 1 635 220 182 ASN CB C 37.55 0.1 1 636 220 182 ASN N N 111.60 0.1 1 637 220 182 ASN H H 8.83 0.02 1 638 221 183 GLN C C 174.72 0.1 1 639 221 183 GLN CA C 54.34 0.1 1 640 221 183 GLN CB C 31.31 0.1 1 641 221 183 GLN N N 119.31 0.1 1 642 221 183 GLN H H 7.75 0.02 1 643 222 184 PHE C C 174.72 0.1 1 644 222 184 PHE CA C 58.62 0.1 1 645 222 184 PHE CB C 40.15 0.1 1 646 222 184 PHE N N 128.98 0.1 1 647 222 184 PHE H H 8.96 0.02 1 648 223 185 GLN C C 172.81 0.1 1 649 223 185 GLN CA C 53.20 0.1 1 650 223 185 GLN CB C 32.35 0.1 1 651 223 185 GLN N N 127.59 0.1 1 652 223 185 GLN H H 8.08 0.02 1 653 224 186 ALA C C 175.99 0.1 1 654 224 186 ALA CA C 49.46 0.1 1 655 224 186 ALA CB C 22.48 0.1 1 656 224 186 ALA N N 120.01 0.1 1 657 224 186 ALA H H 8.98 0.02 1 658 225 187 LEU C C 175.10 0.1 1 659 225 187 LEU CA C 52.98 0.1 1 660 225 187 LEU CB C 44.90 0.1 1 661 225 187 LEU N N 122.15 0.1 1 662 225 187 LEU H H 9.01 0.02 1 663 226 188 LEU C C 173.46 0.1 1 664 226 188 LEU CA C 54.15 0.1 1 665 226 188 LEU CB C 45.37 0.1 1 666 226 188 LEU N N 125.19 0.1 1 667 226 188 LEU H H 8.48 0.02 1 668 227 189 GLN CA C 54.00 0.1 1 669 227 189 GLN CB C 31.02 0.1 1 670 227 189 GLN N N 127.90 0.1 1 671 227 189 GLN H H 8.84 0.02 1 672 228 190 TYR C C 175.61 0.1 1 673 228 190 TYR CA C 58.66 0.1 1 674 228 190 TYR CB C 41.56 0.1 1 675 228 190 TYR N N 128.47 0.1 1 676 228 190 TYR H H 8.86 0.02 1 677 229 191 ALA CA C 54.03 0.1 1 678 229 191 ALA CB C 18.40 0.1 1 679 229 191 ALA N N 120.45 0.1 1 680 229 191 ALA H H 8.26 0.02 1 681 230 192 ASP CA C 50.51 0.1 1 682 230 192 ASP CB C 43.86 0.1 1 683 230 192 ASP N N 116.72 0.1 1 684 230 192 ASP H H 7.72 0.02 1 685 231 193 PRO C C 178.63 0.1 1 686 231 193 PRO CA C 64.77 0.1 1 687 231 193 PRO CB C 31.76 0.1 1 688 232 194 VAL C C 178.72 0.1 1 689 232 194 VAL CA C 65.91 0.1 1 690 232 194 VAL CB C 30.28 0.1 1 691 232 194 VAL N N 122.28 0.1 1 692 232 194 VAL H H 8.47 0.02 1 693 233 195 SER C C 174.99 0.1 1 694 233 195 SER CA C 61.89 0.1 1 695 233 195 SER CB C 65.57 0.1 1 696 233 195 SER N N 118.62 0.1 1 697 233 195 SER H H 7.62 0.02 1 698 234 196 ALA C C 178.80 0.1 1 699 234 196 ALA CA C 54.92 0.1 1 700 234 196 ALA CB C 17.43 0.1 1 701 234 196 ALA N N 121.78 0.1 1 702 234 196 ALA H H 6.41 0.02 1 703 235 197 GLN C C 178.49 0.1 1 704 235 197 GLN CA C 59.13 0.1 1 705 235 197 GLN CB C 27.68 0.1 1 706 235 197 GLN N N 118.49 0.1 1 707 235 197 GLN H H 7.68 0.02 1 708 236 198 HIS C C 177.63 0.1 1 709 236 198 HIS CA C 57.42 0.1 1 710 236 198 HIS CB C 28.94 0.1 1 711 236 198 HIS N N 118.74 0.1 1 712 236 198 HIS H H 8.12 0.02 1 713 237 199 ALA C C 178.96 0.1 1 714 237 199 ALA CA C 54.66 0.1 1 715 237 199 ALA CB C 18.99 0.1 1 716 237 199 ALA N N 123.92 0.1 1 717 237 199 ALA H H 8.29 0.02 1 718 238 200 LYS C C 178.27 0.1 1 719 238 200 LYS CA C 60.34 0.1 1 720 238 200 LYS CB C 31.91 0.1 1 721 238 200 LYS N N 118.62 0.1 1 722 238 200 LYS H H 7.96 0.02 1 723 239 201 LEU C C 180.18 0.1 1 724 239 201 LEU CA C 57.23 0.1 1 725 239 201 LEU CB C 41.41 0.1 1 726 239 201 LEU N N 117.10 0.1 1 727 239 201 LEU H H 7.74 0.02 1 728 240 202 SER C C 176.01 0.1 1 729 240 202 SER CA C 61.35 0.1 1 730 240 202 SER CB C 64.28 0.1 1 731 240 202 SER N N 113.18 0.1 1 732 240 202 SER H H 7.58 0.02 1 733 241 203 LEU C C 177.38 0.1 1 734 241 203 LEU CA C 54.76 0.1 1 735 241 203 LEU CB C 42.75 0.1 1 736 241 203 LEU N N 117.98 0.1 1 737 241 203 LEU H H 8.00 0.02 1 738 242 204 ASP C C 178.29 0.1 1 739 242 204 ASP CA C 57.42 0.1 1 740 242 204 ASP CB C 41.19 0.1 1 741 242 204 ASP N N 120.01 0.1 1 742 242 204 ASP H H 7.45 0.02 1 743 243 205 GLY C C 174.41 0.1 1 744 243 205 GLY CA C 45.50 0.1 1 745 243 205 GLY N N 117.79 0.1 1 746 243 205 GLY H H 9.11 0.02 1 747 244 206 GLN C C 175.14 0.1 1 748 244 206 GLN CA C 54.47 0.1 1 749 244 206 GLN CB C 28.49 0.1 1 750 244 206 GLN N N 120.32 0.1 1 751 244 206 GLN H H 8.06 0.02 1 752 245 207 ASN C C 177.47 0.1 1 753 245 207 ASN CA C 52.16 0.1 1 754 245 207 ASN CB C 38.81 0.1 1 755 245 207 ASN N N 121.08 0.1 1 756 245 207 ASN H H 8.45 0.02 1 757 246 208 ILE C C 175.96 0.1 1 758 246 208 ILE CA C 64.17 0.1 1 759 246 208 ILE CB C 38.37 0.1 1 760 246 208 ILE N N 123.61 0.1 1 761 246 208 ILE H H 8.85 0.02 1 762 247 209 TYR C C 175.25 0.1 1 763 247 209 TYR CA C 55.39 0.1 1 764 247 209 TYR CB C 40.16 0.1 1 765 247 209 TYR N N 116.78 0.1 1 766 247 209 TYR H H 7.10 0.02 1 767 248 210 ASN C C 175.83 0.1 1 768 248 210 ASN CA C 55.80 0.1 1 769 248 210 ASN CB C 37.85 0.1 1 770 248 210 ASN N N 118.74 0.1 1 771 248 210 ASN H H 8.42 0.02 1 772 249 211 ALA C C 176.30 0.1 1 773 249 211 ALA CA C 52.60 0.1 1 774 249 211 ALA CB C 17.88 0.1 1 775 249 211 ALA N N 124.93 0.1 1 776 249 211 ALA H H 8.81 0.02 1 777 250 212 CYS C C 171.70 0.1 1 778 250 212 CYS CA C 57.42 0.1 1 779 250 212 CYS CB C 29.53 0.1 1 780 250 212 CYS N N 114.32 0.1 1 781 250 212 CYS H H 7.84 0.02 1 782 251 213 CYS C C 173.77 0.1 1 783 251 213 CYS CA C 59.80 0.1 1 784 251 213 CYS N N 113.69 0.1 1 785 251 213 CYS H H 8.42 0.02 1 786 252 214 THR C C 174.94 0.1 1 787 252 214 THR CA C 62.46 0.1 1 788 252 214 THR CB C 70.15 0.1 1 789 252 214 THR N N 121.40 0.1 1 790 252 214 THR H H 8.20 0.02 1 791 253 215 LEU C C 176.92 0.1 1 792 253 215 LEU CA C 55.14 0.1 1 793 253 215 LEU CB C 42.44 0.1 1 794 253 215 LEU N N 128.47 0.1 1 795 253 215 LEU H H 8.86 0.02 1 796 254 216 ARG C C 176.74 0.1 1 797 254 216 ARG CA C 53.74 0.1 1 798 254 216 ARG CB C 29.53 0.1 1 799 254 216 ARG N N 124.43 0.1 1 800 254 216 ARG H H 9.00 0.02 1 801 255 217 ILE C C 173.66 0.1 1 802 255 217 ILE CA C 60.34 0.1 1 803 255 217 ILE CB C 41.34 0.1 1 804 255 217 ILE N N 126.32 0.1 1 805 255 217 ILE H H 8.84 0.02 1 806 256 218 ASP C C 175.05 0.1 1 807 256 218 ASP CA C 51.90 0.1 1 808 256 218 ASP CB C 44.16 0.1 1 809 256 218 ASP N N 127.08 0.1 1 810 256 218 ASP H H 8.87 0.02 1 811 257 219 PHE C C 176.76 0.1 1 812 257 219 PHE CA C 58.78 0.1 1 813 257 219 PHE CB C 39.33 0.1 1 814 257 219 PHE N N 120.39 0.1 1 815 257 219 PHE H H 8.79 0.02 1 816 258 220 SER C C 175.45 0.1 1 817 258 220 SER CA C 56.79 0.1 1 818 258 220 SER CB C 63.91 0.1 1 819 258 220 SER N N 118.49 0.1 1 820 258 220 SER H H 8.57 0.02 1 821 260 222 LEU C C 177.30 0.1 1 822 260 222 LEU CA C 54.98 0.1 1 823 260 222 LEU CB C 41.34 0.1 1 824 261 223 THR C C 174.30 0.1 1 825 261 223 THR CA C 61.79 0.1 1 826 261 223 THR CB C 69.18 0.1 1 827 261 223 THR N N 109.77 0.1 1 828 261 223 THR H H 8.32 0.02 1 829 262 224 SER C C 172.48 0.1 1 830 262 224 SER CA C 57.01 0.1 1 831 262 224 SER CB C 64.28 0.1 1 832 262 224 SER N N 113.69 0.1 1 833 262 224 SER H H 7.28 0.02 1 834 263 225 LEU C C 175.54 0.1 1 835 263 225 LEU CA C 52.73 0.1 1 836 263 225 LEU CB C 43.05 0.1 1 837 263 225 LEU N N 121.65 0.1 1 838 263 225 LEU H H 8.01 0.02 1 839 264 226 ASN C C 178.18 0.1 1 840 264 226 ASN CA C 51.90 0.1 1 841 264 226 ASN CB C 38.89 0.1 1 842 264 226 ASN N N 122.91 0.1 1 843 264 226 ASN H H 8.68 0.02 1 844 265 227 VAL C C 175.03 0.1 1 845 265 227 VAL CA C 62.05 0.1 1 846 265 227 VAL CB C 33.27 0.1 1 847 265 227 VAL N N 125.25 0.1 1 848 265 227 VAL H H 8.08 0.02 1 849 266 228 LYS C C 174.77 0.1 1 850 266 228 LYS CA C 56.85 0.1 1 851 266 228 LYS CB C 33.37 0.1 1 852 266 228 LYS N N 128.47 0.1 1 853 266 228 LYS H H 8.34 0.02 1 854 267 229 TYR C C 174.19 0.1 1 855 267 229 TYR CA C 54.57 0.1 1 856 267 229 TYR CB C 42.01 0.1 1 857 267 229 TYR N N 115.58 0.1 1 858 267 229 TYR H H 7.08 0.02 1 859 268 230 ASN C C 174.83 0.1 1 860 268 230 ASN CA C 50.60 0.1 1 861 268 230 ASN CB C 38.59 0.1 1 862 268 230 ASN N N 120.89 0.1 1 863 268 230 ASN H H 7.78 0.02 1 864 269 231 ASN C C 174.63 0.1 1 865 269 231 ASN CA C 52.57 0.1 1 866 269 231 ASN CB C 37.03 0.1 1 867 269 231 ASN N N 124.43 0.1 1 868 269 231 ASN H H 9.42 0.02 1 869 270 232 ASP C C 176.61 0.1 1 870 270 232 ASP CA C 55.77 0.1 1 871 270 232 ASP CB C 39.85 0.1 1 872 270 232 ASP N N 116.72 0.1 1 873 270 232 ASP H H 8.68 0.02 1 874 271 233 LYS C C 176.36 0.1 1 875 271 233 LYS CA C 56.06 0.1 1 876 271 233 LYS CB C 33.32 0.1 1 877 271 233 LYS N N 119.00 0.1 1 878 271 233 LYS H H 8.72 0.02 1 879 272 234 SER C C 171.46 0.1 1 880 272 234 SER CA C 56.56 0.1 1 881 272 234 SER CB C 66.51 0.1 1 882 272 234 SER N N 115.39 0.1 1 883 272 234 SER H H 7.84 0.02 1 884 273 235 ARG C C 173.90 0.1 1 885 273 235 ARG CA C 55.11 0.1 1 886 273 235 ARG CB C 33.25 0.1 1 887 273 235 ARG N N 121.78 0.1 1 888 273 235 ARG H H 8.98 0.02 1 889 274 236 ASP C C 178.27 0.1 1 890 274 236 ASP CA C 52.13 0.1 1 891 274 236 ASP CB C 41.26 0.1 1 892 274 236 ASP N N 126.32 0.1 1 893 274 236 ASP H H 8.91 0.02 1 894 275 237 TYR C C 176.94 0.1 1 895 275 237 TYR CA C 61.57 0.1 1 896 275 237 TYR CB C 36.88 0.1 1 897 275 237 TYR N N 125.57 0.1 1 898 275 237 TYR H H 9.01 0.02 1 899 276 238 THR C C 174.72 0.1 1 900 276 238 THR CA C 61.79 0.1 1 901 276 238 THR CB C 69.33 0.1 1 902 276 238 THR N N 112.74 0.1 1 903 276 238 THR H H 9.23 0.02 1 904 277 239 ARG C C 173.26 0.1 1 905 277 239 ARG CA C 52.38 0.1 1 906 277 239 ARG CB C 30.65 0.1 1 907 277 239 ARG N N 122.60 0.1 1 908 277 239 ARG H H 6.84 0.02 1 909 278 240 PRO C C 177.03 0.1 1 910 278 240 PRO CA C 63.69 0.1 1 911 278 240 PRO CB C 31.17 0.1 1 912 279 241 ASP C C 176.54 0.1 1 913 279 241 ASP CA C 53.46 0.1 1 914 279 241 ASP CB C 39.93 0.1 1 915 279 241 ASP N N 117.48 0.1 1 916 279 241 ASP H H 8.72 0.02 1 917 280 242 LEU C C 175.48 0.1 1 918 280 242 LEU CA C 54.12 0.1 1 919 280 242 LEU CB C 39.33 0.1 1 920 280 242 LEU N N 121.71 0.1 1 921 280 242 LEU H H 6.90 0.02 1 922 281 243 PRO C C 176.43 0.1 1 923 281 243 PRO CA C 62.36 0.1 1 924 281 243 PRO CB C 32.06 0.1 1 925 282 244 SER C C 176.21 0.1 1 926 282 244 SER CA C 58.91 0.1 1 927 282 244 SER CB C 64.13 0.1 1 928 282 244 SER N N 114.76 0.1 1 929 282 244 SER H H 8.56 0.02 1 930 283 245 GLY C C 173.21 0.1 1 931 283 245 GLY CA C 44.49 0.1 1 932 283 245 GLY N N 111.10 0.1 1 933 283 245 GLY H H 7.64 0.02 1 stop_ save_