data_4457 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Sequence-specific assignments and partial unfolding of extracellular domains II and III of E-cadherin. ; _BMRB_accession_number 4457 _BMRB_flat_file_name bmr4457.str _Entry_type original _Submission_date 1999-11-15 _Accession_date 1999-11-11 _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 Alattia Jean-Rene . . 2 Tong Frances K. . 3 Tong Kit I. . 4 Ikura Mitsuhiko . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 332 "13C chemical shifts" 321 "15N chemical shifts" 167 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2000-03-17 original author . stop_ _Original_release_date 2000-03-17 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; Letter to the Editor: Sequence-specific resonance assignments and partial unfolding of extracellular domains II and III of E-cadherin ; _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 Alattia Jean-Rene . . 2 Tong Frances K. . 3 Tong Kit I. . 4 Ikura Mitsuhiko . . stop_ _Journal_abbreviation 'J. Biomol. NMR' _Journal_volume 16 _Journal_issue . _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 181 _Page_last 182 _Year 2000 _Details . loop_ _Keyword 'NMR assignments' 'cell adhesion' calcium stop_ save_ ################################## # Molecular system description # ################################## save_EC23 _Saveframe_category molecular_system _Mol_system_name E-cadherin _Abbreviation_common EC23 _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'E-cadherin domains 2-3' $E-cadherin stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state monomer _System_paramagnetic no _System_thiol_state 'not reported' loop_ _Biological_function 'cell-cell adhesion' stop_ _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_E-cadherin _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'Epithelial Cadherin' _Abbreviation_common E-cadherin _Molecular_mass 24355 _Mol_thiol_state 'not reported' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 227 _Mol_residue_sequence ; GSMTQEVFEGSVAEGAVPGT SVMKVSATDADDDVNTYNAA IAYTIVSQDPELPHKNMFTV NRDTGVISVLTSGLDRESYP TYTLVVQAADLQGEGLSTTA KAVITVKDINDNAPVFNPST YQGQVPENEVNARIATLKVT DDDAPNTPAWKAVYTVVNDP DQQFVVVTDPTTNDGILKTA KGLDFEAKQQYILHVRVENE EPFEGSLVPSTATVTVDVVD VNEAPIF ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 106 GLY 2 107 SER 3 108 MET 4 109 THR 5 110 GLN 6 111 GLU 7 112 VAL 8 113 PHE 9 114 GLU 10 115 GLY 11 116 SER 12 117 VAL 13 118 ALA 14 119 GLU 15 120 GLY 16 121 ALA 17 122 VAL 18 123 PRO 19 124 GLY 20 125 THR 21 126 SER 22 127 VAL 23 128 MET 24 129 LYS 25 130 VAL 26 131 SER 27 132 ALA 28 133 THR 29 134 ASP 30 135 ALA 31 136 ASP 32 137 ASP 33 138 ASP 34 139 VAL 35 140 ASN 36 141 THR 37 142 TYR 38 143 ASN 39 144 ALA 40 145 ALA 41 146 ILE 42 147 ALA 43 148 TYR 44 149 THR 45 150 ILE 46 151 VAL 47 152 SER 48 153 GLN 49 154 ASP 50 155 PRO 51 156 GLU 52 157 LEU 53 158 PRO 54 159 HIS 55 160 LYS 56 161 ASN 57 162 MET 58 163 PHE 59 164 THR 60 165 VAL 61 166 ASN 62 167 ARG 63 168 ASP 64 169 THR 65 170 GLY 66 171 VAL 67 172 ILE 68 173 SER 69 174 VAL 70 175 LEU 71 176 THR 72 177 SER 73 178 GLY 74 179 LEU 75 180 ASP 76 181 ARG 77 182 GLU 78 183 SER 79 184 TYR 80 185 PRO 81 186 THR 82 187 TYR 83 188 THR 84 189 LEU 85 190 VAL 86 191 VAL 87 192 GLN 88 193 ALA 89 194 ALA 90 195 ASP 91 196 LEU 92 197 GLN 93 198 GLY 94 199 GLU 95 200 GLY 96 201 LEU 97 202 SER 98 203 THR 99 204 THR 100 205 ALA 101 206 LYS 102 207 ALA 103 208 VAL 104 209 ILE 105 210 THR 106 211 VAL 107 212 LYS 108 213 ASP 109 214 ILE 110 215 ASN 111 216 ASP 112 217 ASN 113 218 ALA 114 219 PRO 115 220 VAL 116 221 PHE 117 222 ASN 118 223 PRO 119 224 SER 120 225 THR 121 226 TYR 122 227 GLN 123 228 GLY 124 229 GLN 125 230 VAL 126 231 PRO 127 232 GLU 128 233 ASN 129 234 GLU 130 235 VAL 131 236 ASN 132 237 ALA 133 238 ARG 134 239 ILE 135 240 ALA 136 241 THR 137 242 LEU 138 243 LYS 139 244 VAL 140 245 THR 141 246 ASP 142 247 ASP 143 248 ASP 144 249 ALA 145 250 PRO 146 251 ASN 147 252 THR 148 253 PRO 149 254 ALA 150 255 TRP 151 256 LYS 152 257 ALA 153 258 VAL 154 259 TYR 155 260 THR 156 261 VAL 157 262 VAL 158 263 ASN 159 264 ASP 160 265 PRO 161 266 ASP 162 267 GLN 163 268 GLN 164 269 PHE 165 270 VAL 166 271 VAL 167 272 VAL 168 273 THR 169 274 ASP 170 275 PRO 171 276 THR 172 277 THR 173 278 ASN 174 279 ASP 175 280 GLY 176 281 ILE 177 282 LEU 178 283 LYS 179 284 THR 180 285 ALA 181 286 LYS 182 287 GLY 183 288 LEU 184 289 ASP 185 290 PHE 186 291 GLU 187 292 ALA 188 293 LYS 189 294 GLN 190 295 GLN 191 296 TYR 192 297 ILE 193 298 LEU 194 299 HIS 195 300 VAL 196 301 ARG 197 302 VAL 198 303 GLU 199 304 ASN 200 305 GLU 201 306 GLU 202 307 PRO 203 308 PHE 204 309 GLU 205 310 GLY 206 311 SER 207 312 LEU 208 313 VAL 209 314 PRO 210 315 SER 211 316 THR 212 317 ALA 213 318 THR 214 319 VAL 215 320 THR 216 321 VAL 217 322 ASP 218 323 VAL 219 324 VAL 220 325 ASP 221 326 VAL 222 327 ASN 223 328 GLU 224 329 ALA 225 330 PRO 226 331 ILE 227 332 PHE stop_ _Sequence_homology_query_date 2008-08-19 _Sequence_homology_query_revised_last_date 2008-01-16 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 REF NP_033994.1 'cadherin 1 [Mus musculus]' 25.68 884 99 99 10e-123 SWISS-PROT P09803 'CADH1_MOUSE Epithelial cadherin precursor(E-cadherin) (Uvomorulin) (Cadherin-1) (ARC-1) (CD324antigen) [Contains: E-Cad/' 25.68 884 100 100 10e-124 GenBank EDL11373.1 'cadherin 1, isoform CRA_b [Musmusculus]' 25.68 884 99 99 10e-123 PRF 1312359A 'cadherin E' 25.68 884 100 100 10e-124 GenBank AAH98501.1 'Cdh1 protein [Mus musculus]' 25.68 884 100 100 10e-124 GenBank EDL11372.1 'cadherin 1, isoform CRA_a [Musmusculus]' 25.68 884 100 100 10e-124 EMBL CAA29488.1 'unnamed protein product [Mus musculus]' 25.68 884 100 100 10e-124 EMBL CAA43292.1 'uvomorulin [Mus musculus]' 25.68 884 99 99 10e-123 PDB 1EDH 'A Chain A, E-Cadherin Domains 1 And 2 InComplex With Calcium' 100.44 226 100 100 1e-58 EMBL CAA29645.1 'uvomorulin (711 AA) [Mus musculus]' 31.93 711 100 100 10e-124 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 $E-cadherin Mouse 10090 Eukaryota Metazoa Mus musculus epithelium stop_ save_ ######################### # Experimental source # ######################### save_experimental_source _Saveframe_category experimental_source loop_ _Mol_label _Production_method _Host_organism_name_common _Genus _Species _Strain _Vector_type _Vector_name $E-cadherin 'recombinant technology' 'E. coli' Escherichia coli 'BL21 (DE3)' plasmid 'pET 15b (modified)' stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_ec23_274c _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $E-cadherin 2.0 mM . stop_ save_ ############################ # Computer software used # ############################ save_nmrPipe _Saveframe_category software _Name nmrPipe _Version . loop_ _Task 'Data processing' stop_ _Details . save_ save_nmrview _Saveframe_category software _Name nmrview _Version 3.0b4 loop_ _Task Assignment stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer1 _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model Inova _Field_strength 500 _Details . save_ save_NMR_spectrometer2 _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model Inova _Field_strength 600 _Details . save_ ############################# # NMR applied experiments # ############################# save_1H-15N_NOESY_1 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-15N NOESY' _Sample_label . save_ save_1H-15N_DIPSI_2 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-15N DIPSI' _Sample_label . save_ save_HBCBCACONNH_3 _Saveframe_category NMR_applied_experiment _Experiment_name HBCBCACONNH _Sample_label . save_ save_HNCACB_4 _Saveframe_category NMR_applied_experiment _Experiment_name HNCACB _Sample_label . save_ save_HNCO_5 _Saveframe_category NMR_applied_experiment _Experiment_name HNCO _Sample_label . save_ save_HBCBCACOCAHA_6 _Saveframe_category NMR_applied_experiment _Experiment_name HBCBCACOCAHA _Sample_label . save_ save_HCCH-TOCSY_7 _Saveframe_category NMR_applied_experiment _Experiment_name HCCH-TOCSY _Sample_label . save_ save_CCCTOCSY_NNH_8 _Saveframe_category NMR_applied_experiment _Experiment_name CCCTOCSY_NNH _Sample_label . save_ save_15N-13C_NOESY_9 _Saveframe_category NMR_applied_experiment _Experiment_name '15N-13C NOESY' _Sample_label . save_ save_NMR_spec_expt__0_1 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-15N NOESY' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_2 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-15N DIPSI' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_3 _Saveframe_category NMR_applied_experiment _Experiment_name HBCBCACONNH _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_4 _Saveframe_category NMR_applied_experiment _Experiment_name HNCACB _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_5 _Saveframe_category NMR_applied_experiment _Experiment_name HNCO _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_6 _Saveframe_category NMR_applied_experiment _Experiment_name HBCBCACOCAHA _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_7 _Saveframe_category NMR_applied_experiment _Experiment_name HCCH-TOCSY _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_8 _Saveframe_category NMR_applied_experiment _Experiment_name CCCTOCSY_NNH _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_9 _Saveframe_category NMR_applied_experiment _Experiment_name '15N-13C NOESY' _BMRB_pulse_sequence_accession_number . _Details . save_ ####################### # Sample conditions # ####################### save_cond_274c _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 7.4 0.2 n/a temperature 298 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 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_curr_side_assign.16 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Sample_label $ec23_274c stop_ _Sample_conditions_label $cond_274c _Chem_shift_reference_set_label $chemical_shift_reference _Mol_system_component_name 'E-cadherin domains 2-3' _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 . 5 GLN N N 117.48 0.20 1 2 . 5 GLN H H 7.33 0.02 1 3 . 5 GLN CA C 53.88 0.20 1 4 . 5 GLN HA H 4.46 0.02 1 5 . 5 GLN CB C 30.60 0.20 1 6 . 8 PHE N N 125.25 0.20 1 7 . 8 PHE H H 8.34 0.02 1 8 . 8 PHE CA C 57.30 0.20 1 9 . 8 PHE HA H 4.65 0.02 1 10 . 8 PHE CB C 39.76 0.20 1 11 . 9 GLU N N 124.18 0.20 1 12 . 9 GLU H H 8.39 0.02 1 13 . 9 GLU CA C 56.71 0.20 1 14 . 9 GLU HA H 4.26 0.02 1 15 . 9 GLU CB C 30.16 0.20 1 16 . 10 GLY N N 110.03 0.20 1 17 . 10 GLY H H 7.88 0.02 1 18 . 10 GLY CA C 45.18 0.20 1 19 . 10 GLY HA2 H 3.95 0.02 1 20 . 10 GLY HA3 H 3.95 0.02 1 21 . 11 SER N N 113.65 0.20 1 22 . 11 SER H H 8.63 0.02 1 23 . 11 SER CA C 56.87 0.20 1 24 . 11 SER HA H 5.74 0.02 1 25 . 11 SER CB C 66.65 0.20 1 26 . 12 VAL N N 119.86 0.20 1 27 . 12 VAL H H 8.68 0.02 1 28 . 12 VAL CA C 58.82 0.20 1 29 . 12 VAL HA H 4.56 0.02 1 30 . 12 VAL CB C 35.49 0.20 1 31 . 13 ALA N N 130.94 0.20 1 32 . 13 ALA H H 8.68 0.02 1 33 . 13 ALA CA C 51.78 0.20 1 34 . 13 ALA HA H 4.46 0.02 1 35 . 13 ALA CB C 19.44 0.20 1 36 . 14 GLU N N 119.66 0.20 1 37 . 14 GLU H H 8.53 0.02 1 38 . 14 GLU CA C 57.52 0.20 1 39 . 14 GLU HA H 3.89 0.02 1 40 . 14 GLU CB C 29.50 0.20 1 41 . 15 GLY N N 108.26 0.20 1 42 . 15 GLY H H 8.08 0.02 1 43 . 15 GLY CA C 44.84 0.20 1 44 . 16 ALA N N 122.89 0.20 1 45 . 16 ALA H H 7.56 0.02 1 46 . 16 ALA CA C 52.82 0.20 1 47 . 16 ALA HA H 4.29 0.02 1 48 . 16 ALA CB C 19.62 0.20 1 49 . 17 VAL N N 115.45 0.20 1 50 . 17 VAL H H 7.73 0.02 1 51 . 17 VAL CA C 59.12 0.20 1 52 . 17 VAL HA H 4.49 0.02 1 53 . 17 VAL CB C 30.99 0.20 1 54 . 19 GLY N N 113.26 0.20 1 55 . 19 GLY H H 9.10 0.02 1 56 . 19 GLY CA C 44.24 0.20 1 57 . 19 GLY HA2 H 4.51 0.02 1 58 . 19 GLY HA3 H 4.51 0.02 1 59 . 20 THR N N 118.94 0.20 1 60 . 20 THR H H 7.76 0.02 1 61 . 20 THR CA C 64.40 0.20 1 62 . 20 THR HA H 4.07 0.02 1 63 . 20 THR CB C 69.63 0.20 1 64 . 21 SER N N 125.87 0.20 1 65 . 21 SER H H 9.10 0.02 1 66 . 21 SER CA C 59.41 0.20 1 67 . 21 SER HA H 4.35 0.02 1 68 . 21 SER CB C 63.31 0.20 1 69 . 22 VAL N N 123.46 0.20 1 70 . 22 VAL H H 9.33 0.02 1 71 . 22 VAL CA C 64.31 0.20 1 72 . 22 VAL HA H 4.13 0.02 1 73 . 22 VAL CB C 34.26 0.20 1 74 . 23 MET N N 110.87 0.20 1 75 . 23 MET H H 7.52 0.02 1 76 . 23 MET CA C 54.67 0.20 1 77 . 23 MET HA H 4.63 0.02 1 78 . 23 MET CB C 34.27 0.20 1 79 . 26 SER N N 112.05 0.20 1 80 . 26 SER H H 6.14 0.02 1 81 . 26 SER CA C 56.67 0.20 1 82 . 26 SER HA H 4.82 0.02 1 83 . 26 SER CB C 65.51 0.20 1 84 . 27 ALA N N 127.00 0.20 1 85 . 27 ALA H H 8.38 0.02 1 86 . 27 ALA CA C 51.22 0.20 1 87 . 27 ALA HA H 4.97 0.02 1 88 . 27 ALA CB C 20.97 0.20 1 89 . 28 THR N N 112.17 0.20 1 90 . 28 THR H H 8.18 0.02 1 91 . 28 THR CA C 60.20 0.20 1 92 . 28 THR HA H 4.54 0.02 1 93 . 28 THR CB C 70.39 0.20 1 94 . 30 ALA N N 125.50 0.20 1 95 . 30 ALA H H 8.38 0.02 1 96 . 30 ALA CA C 52.83 0.20 1 97 . 30 ALA HA H 4.33 0.02 1 98 . 30 ALA CB C 19.38 0.20 1 99 . 31 ASP N N 120.00 0.20 1 100 . 31 ASP H H 8.25 0.02 1 101 . 31 ASP CA C 54.41 0.20 1 102 . 31 ASP CB C 40.94 0.20 1 103 . 34 VAL N N 120.20 0.20 1 104 . 34 VAL H H 8.03 0.02 1 105 . 34 VAL CA C 62.73 0.20 1 106 . 34 VAL HA H 4.09 0.02 1 107 . 34 VAL CB C 32.30 0.20 1 108 . 35 ASN N N 120.72 0.20 1 109 . 35 ASN H H 8.43 0.02 1 110 . 35 ASN CA C 53.38 0.20 1 111 . 35 ASN HA H 4.77 0.02 1 112 . 35 ASN CB C 38.80 0.20 1 113 . 36 THR N N 114.34 0.20 1 114 . 36 THR H H 7.96 0.02 1 115 . 36 THR CA C 61.93 0.20 1 116 . 36 THR HA H 4.27 0.02 1 117 . 36 THR CB C 69.48 0.20 1 118 . 37 TYR N N 122.42 0.20 1 119 . 37 TYR H H 8.12 0.02 1 120 . 37 TYR CA C 57.74 0.20 1 121 . 37 TYR HA H 4.60 0.02 1 122 . 37 TYR CB C 38.32 0.20 1 123 . 39 ALA N N 125.09 0.20 1 124 . 39 ALA H H 8.09 0.02 1 125 . 39 ALA CA C 52.39 0.20 1 126 . 39 ALA HA H 4.29 0.02 1 127 . 39 ALA CB C 19.39 0.20 1 128 . 40 ALA N N 124.70 0.20 1 129 . 40 ALA H H 8.39 0.02 1 130 . 40 ALA CA C 51.72 0.20 1 131 . 40 ALA HA H 4.51 0.02 1 132 . 40 ALA CB C 19.31 0.20 1 133 . 41 ILE N N 121.74 0.20 1 134 . 41 ILE H H 7.60 0.02 1 135 . 41 ILE CA C 58.99 0.20 1 136 . 41 ILE HA H 4.55 0.02 1 137 . 41 ILE CB C 40.20 0.20 1 138 . 42 ALA N N 127.61 0.20 1 139 . 42 ALA H H 8.63 0.02 1 140 . 42 ALA CA C 49.69 0.20 1 141 . 42 ALA HA H 5.25 0.02 1 142 . 42 ALA CB C 21.57 0.20 1 143 . 43 TYR N N 125.99 0.20 1 144 . 43 TYR H H 9.56 0.02 1 145 . 43 TYR CA C 57.42 0.20 1 146 . 43 TYR HA H 5.63 0.02 1 147 . 43 TYR CB C 40.65 0.20 1 148 . 44 THR N N 112.28 0.20 1 149 . 44 THR H H 8.90 0.02 1 150 . 44 THR CA C 60.46 0.20 1 151 . 44 THR HA H 4.47 0.02 1 152 . 44 THR CB C 72.62 0.20 1 153 . 45 ILE N N 123.36 0.20 1 154 . 45 ILE H H 8.80 0.02 1 155 . 45 ILE CA C 61.91 0.20 1 156 . 45 ILE HA H 4.44 0.02 1 157 . 45 ILE CB C 38.70 0.20 1 158 . 46 VAL N N 127.86 0.20 1 159 . 46 VAL H H 9.26 0.02 1 160 . 46 VAL CA C 63.04 0.20 1 161 . 46 VAL HA H 4.09 0.02 1 162 . 46 VAL CB C 32.74 0.20 1 163 . 47 SER N N 111.94 0.20 1 164 . 47 SER H H 7.49 0.02 1 165 . 47 SER CA C 57.53 0.20 1 166 . 47 SER HA H 4.68 0.02 1 167 . 47 SER CB C 64.98 0.20 1 168 . 48 GLN N N 122.02 0.20 1 169 . 48 GLN H H 8.60 0.02 1 170 . 48 GLN CA C 55.39 0.20 1 171 . 48 GLN HA H 4.83 0.02 1 172 . 48 GLN CB C 34.18 0.20 1 173 . 49 ASP N N 126.41 0.20 1 174 . 49 ASP H H 8.59 0.02 1 175 . 49 ASP CA C 55.38 0.20 1 176 . 49 ASP HA H 5.24 0.02 1 177 . 49 ASP CB C 44.91 0.20 1 178 . 51 GLU N N 122.44 0.20 1 179 . 51 GLU H H 9.19 0.02 1 180 . 51 GLU CA C 55.93 0.20 1 181 . 51 GLU HA H 4.26 0.02 1 182 . 51 GLU CB C 28.14 0.20 1 183 . 52 LEU N N 115.38 0.20 1 184 . 52 LEU H H 6.33 0.02 1 185 . 52 LEU CA C 51.55 0.20 1 186 . 52 LEU HA H 4.21 0.02 1 187 . 52 LEU CB C 45.14 0.20 1 188 . 54 HIS N N 118.47 0.20 1 189 . 54 HIS H H 6.93 0.02 1 190 . 54 HIS CA C 54.20 0.20 1 191 . 54 HIS HA H 4.77 0.02 1 192 . 54 HIS CB C 33.80 0.20 1 193 . 56 ASN N N 116.33 0.20 1 194 . 56 ASN H H 8.59 0.02 1 195 . 56 ASN CA C 51.59 0.20 1 196 . 56 ASN HA H 5.07 0.02 1 197 . 56 ASN CB C 39.10 0.20 1 198 . 57 MET N N 118.98 0.20 1 199 . 57 MET H H 9.29 0.02 1 200 . 57 MET CA C 54.86 0.20 1 201 . 57 MET HA H 4.24 0.02 1 202 . 57 MET CB C 29.55 0.20 1 203 . 58 PHE N N 116.00 0.20 1 204 . 58 PHE H H 8.19 0.02 1 205 . 58 PHE CA C 55.68 0.20 1 206 . 58 PHE HA H 5.14 0.02 1 207 . 58 PHE CB C 42.17 0.20 1 208 . 59 THR N N 112.98 0.20 1 209 . 59 THR H H 8.77 0.02 1 210 . 59 THR CA C 58.84 0.20 1 211 . 59 THR HA H 4.71 0.02 1 212 . 59 THR CB C 69.58 0.20 1 213 . 60 VAL N N 123.59 0.20 1 214 . 60 VAL H H 8.11 0.02 1 215 . 60 VAL CA C 57.03 0.20 1 216 . 60 VAL HA H 5.23 0.02 1 217 . 60 VAL CB C 35.47 0.20 1 218 . 61 ASN N N 128.39 0.20 1 219 . 61 ASN H H 8.17 0.02 1 220 . 61 ASN CA C 53.81 0.20 1 221 . 61 ASN HA H 4.64 0.02 1 222 . 61 ASN CB C 39.35 0.20 1 223 . 62 ARG N N 130.27 0.20 1 224 . 62 ARG H H 8.95 0.02 1 225 . 62 ARG CA C 58.30 0.20 1 226 . 62 ARG HA H 4.83 0.02 1 227 . 62 ARG CB C 31.40 0.20 1 228 . 63 ASP N N 112.08 0.20 1 229 . 63 ASP H H 8.09 0.02 1 230 . 63 ASP CA C 55.38 0.20 1 231 . 63 ASP HA H 5.12 0.02 1 232 . 63 ASP CB C 42.75 0.20 1 233 . 64 THR N N 108.33 0.20 1 234 . 64 THR H H 8.17 0.02 1 235 . 64 THR CA C 61.70 0.20 1 236 . 64 THR HA H 4.55 0.02 1 237 . 64 THR CB C 70.96 0.20 1 238 . 65 GLY N N 110.40 0.20 1 239 . 65 GLY H H 8.09 0.02 1 240 . 65 GLY CA C 44.84 0.20 1 241 . 65 GLY HA2 H 3.26 0.02 1 242 . 65 GLY HA3 H 3.26 0.02 1 243 . 66 VAL N N 118.86 0.20 1 244 . 66 VAL H H 7.17 0.02 1 245 . 66 VAL CA C 63.55 0.20 1 246 . 66 VAL HA H 4.04 0.02 1 247 . 66 VAL CB C 32.43 0.20 1 248 . 67 ILE N N 110.44 0.20 1 249 . 67 ILE H H 9.46 0.02 1 250 . 67 ILE CA C 60.01 0.20 1 251 . 67 ILE HA H 5.03 0.02 1 252 . 67 ILE CB C 38.64 0.20 1 253 . 68 SER N N 121.70 0.20 1 254 . 68 SER H H 9.06 0.02 1 255 . 68 SER CA C 56.17 0.20 1 256 . 68 SER HA H 5.49 0.02 1 257 . 68 SER CB C 66.24 0.20 1 258 . 69 VAL N N 122.06 0.20 1 259 . 69 VAL H H 8.58 0.02 1 260 . 69 VAL CA C 63.90 0.20 1 261 . 69 VAL HA H 4.20 0.02 1 262 . 69 VAL CB C 32.78 0.20 1 263 . 71 THR N N 114.41 0.20 1 264 . 71 THR H H 8.88 0.02 1 265 . 71 THR CA C 63.88 0.20 1 266 . 71 THR HA H 4.10 0.02 1 267 . 71 THR CB C 68.94 0.20 1 268 . 72 SER N N 118.34 0.20 1 269 . 72 SER H H 8.14 0.02 1 270 . 72 SER CA C 58.73 0.20 1 271 . 72 SER HA H 4.46 0.02 1 272 . 72 SER CB C 63.85 0.20 1 273 . 73 GLY N N 131.25 0.20 1 274 . 73 GLY H H 8.33 0.02 1 275 . 73 GLY CA C 44.86 0.20 1 276 . 74 LEU N N 121.86 0.20 1 277 . 74 LEU H H 8.09 0.02 1 278 . 74 LEU CA C 54.97 0.20 1 279 . 74 LEU HA H 4.35 0.02 1 280 . 74 LEU CB C 42.29 0.20 1 281 . 76 ARG N N 127.31 0.20 1 282 . 76 ARG H H 9.50 0.02 1 283 . 76 ARG CA C 58.82 0.20 1 284 . 76 ARG HA H 3.79 0.02 1 285 . 76 ARG CB C 30.05 0.20 1 286 . 77 GLU N N 116.81 0.20 1 287 . 77 GLU H H 8.16 0.02 1 288 . 77 GLU CA C 58.41 0.20 1 289 . 77 GLU HA H 3.95 0.02 1 290 . 77 GLU CB C 29.59 0.20 1 291 . 78 SER N N 112.83 0.20 1 292 . 78 SER H H 7.18 0.02 1 293 . 78 SER CA C 60.24 0.20 1 294 . 78 SER HA H 4.08 0.02 1 295 . 78 SER CB C 63.10 0.20 1 296 . 79 TYR N N 117.90 0.20 1 297 . 79 TYR H H 7.73 0.02 1 298 . 79 TYR CA C 53.90 0.20 1 299 . 79 TYR HA H 5.10 0.02 1 300 . 79 TYR CB C 37.78 0.20 1 301 . 81 THR N N 111.94 0.20 1 302 . 81 THR H H 7.31 0.02 1 303 . 81 THR CA C 60.28 0.20 1 304 . 81 THR HA H 5.42 0.02 1 305 . 81 THR CB C 72.14 0.20 1 306 . 82 TYR N N 122.73 0.20 1 307 . 82 TYR H H 9.24 0.02 1 308 . 82 TYR CA C 57.11 0.20 1 309 . 82 TYR HA H 5.35 0.02 1 310 . 82 TYR CB C 43.48 0.20 1 311 . 83 THR N N 117.55 0.20 1 312 . 83 THR H H 9.41 0.02 1 313 . 83 THR CA C 61.98 0.20 1 314 . 83 THR HA H 5.12 0.02 1 315 . 83 THR CB C 69.76 0.20 1 316 . 84 LEU N N 130.92 0.20 1 317 . 84 LEU H H 10.04 0.02 1 318 . 84 LEU CA C 52.13 0.20 1 319 . 84 LEU HA H 5.55 0.02 1 320 . 84 LEU CB C 43.55 0.20 1 321 . 85 VAL N N 122.26 0.20 1 322 . 85 VAL H H 8.00 0.02 1 323 . 85 VAL CA C 62.53 0.20 1 324 . 85 VAL HA H 4.72 0.02 1 325 . 85 VAL CB C 32.38 0.20 1 326 . 86 VAL N N 127.61 0.20 1 327 . 86 VAL H H 9.20 0.02 1 328 . 86 VAL CA C 59.72 0.20 1 329 . 86 VAL HA H 4.96 0.02 1 330 . 86 VAL CB C 34.16 0.20 1 331 . 87 GLN N N 126.23 0.20 1 332 . 87 GLN H H 9.38 0.02 1 333 . 87 GLN CA C 53.89 0.20 1 334 . 87 GLN HA H 5.22 0.02 1 335 . 87 GLN CB C 33.54 0.20 1 336 . 88 ALA N N 128.51 0.20 1 337 . 88 ALA H H 8.82 0.02 1 338 . 88 ALA CA C 49.95 0.20 1 339 . 88 ALA HA H 4.82 0.02 1 340 . 88 ALA CB C 21.05 0.20 1 341 . 89 ALA N N 126.31 0.20 1 342 . 89 ALA H H 8.62 0.02 1 343 . 89 ALA CA C 50.32 0.20 1 344 . 89 ALA HA H 4.79 0.02 1 345 . 89 ALA CB C 21.45 0.20 1 346 . 90 ASP N N 122.01 0.20 1 347 . 90 ASP H H 8.35 0.02 1 348 . 90 ASP CA C 53.51 0.20 1 349 . 90 ASP HA H 4.78 0.02 1 350 . 90 ASP CB C 41.52 0.20 1 351 . 91 LEU N N 124.52 0.20 1 352 . 91 LEU H H 8.53 0.02 1 353 . 91 LEU CA C 55.73 0.20 1 354 . 91 LEU HA H 4.25 0.02 1 355 . 91 LEU CB C 41.44 0.20 1 356 . 92 GLN N N 117.55 0.20 1 357 . 92 GLN H H 8.41 0.02 1 358 . 92 GLN CA C 55.40 0.20 1 359 . 92 GLN HA H 4.42 0.02 1 360 . 92 GLN CB C 29.52 0.20 1 361 . 93 GLY N N 108.60 0.20 1 362 . 93 GLY H H 8.08 0.02 1 363 . 93 GLY CA C 45.77 0.20 1 364 . 93 GLY HA2 H 3.97 0.02 1 365 . 93 GLY HA3 H 3.97 0.02 1 366 . 95 GLY N N 108.96 0.20 1 367 . 95 GLY H H 8.32 0.02 1 368 . 95 GLY CA C 45.56 0.20 1 369 . 95 GLY HA2 H 3.96 0.02 1 370 . 95 GLY HA3 H 3.96 0.02 1 371 . 96 LEU N N 122.17 0.20 1 372 . 96 LEU H H 8.30 0.02 1 373 . 96 LEU CA C 54.95 0.20 1 374 . 96 LEU HA H 4.47 0.02 1 375 . 96 LEU CB C 42.23 0.20 1 376 . 97 SER N N 116.45 0.20 1 377 . 97 SER H H 8.25 0.02 1 378 . 97 SER CA C 57.30 0.20 1 379 . 97 SER HA H 5.30 0.02 1 380 . 97 SER CB C 65.36 0.20 1 381 . 98 THR N N 114.20 0.20 1 382 . 98 THR H H 8.46 0.02 1 383 . 98 THR CA C 60.19 0.20 1 384 . 98 THR HA H 4.88 0.02 1 385 . 98 THR CB C 71.74 0.20 1 386 . 99 THR N N 111.69 0.20 1 387 . 99 THR H H 8.27 0.02 1 388 . 99 THR CA C 59.62 0.20 1 389 . 99 THR HA H 5.75 0.02 1 390 . 99 THR CB C 72.48 0.20 1 391 . 100 ALA N N 122.68 0.20 1 392 . 100 ALA H H 9.10 0.02 1 393 . 100 ALA CA C 50.90 0.20 1 394 . 100 ALA HA H 4.92 0.02 1 395 . 100 ALA CB C 23.89 0.20 1 396 . 101 LYS N N 118.55 0.20 1 397 . 101 LYS H H 8.19 0.02 1 398 . 101 LYS CA C 54.83 0.20 1 399 . 101 LYS HA H 5.45 0.02 1 400 . 101 LYS CB C 35.40 0.20 1 401 . 102 ALA N N 126.12 0.20 1 402 . 102 ALA H H 9.39 0.02 1 403 . 102 ALA CA C 49.58 0.20 1 404 . 102 ALA HA H 5.54 0.02 1 405 . 102 ALA CB C 20.32 0.20 1 406 . 103 VAL N N 125.21 0.20 1 407 . 103 VAL H H 8.98 0.02 1 408 . 103 VAL CA C 61.47 0.20 1 409 . 103 VAL HA H 4.92 0.02 1 410 . 103 VAL CB C 32.95 0.20 1 411 . 104 ILE N N 130.51 0.20 1 412 . 104 ILE H H 9.57 0.02 1 413 . 104 ILE CA C 59.61 0.20 1 414 . 104 ILE HA H 4.51 0.02 1 415 . 104 ILE CB C 40.68 0.20 1 416 . 105 THR N N 124.67 0.20 1 417 . 105 THR H H 8.60 0.02 1 418 . 105 THR CA C 62.12 0.20 1 419 . 105 THR HA H 4.89 0.02 1 420 . 105 THR CB C 70.14 0.20 1 421 . 106 VAL N N 129.13 0.20 1 422 . 106 VAL H H 8.97 0.02 1 423 . 106 VAL CA C 61.83 0.20 1 424 . 106 VAL HA H 4.82 0.02 1 425 . 106 VAL CB C 32.05 0.20 1 426 . 107 LYS N N 126.90 0.20 1 427 . 107 LYS H H 9.05 0.02 1 428 . 107 LYS CA C 54.30 0.20 1 429 . 107 LYS HA H 4.73 0.02 1 430 . 107 LYS CB C 35.20 0.20 1 431 . 108 ASP N N 120.70 0.20 1 432 . 108 ASP H H 8.64 0.02 1 433 . 108 ASP CA C 54.06 0.20 1 434 . 108 ASP HA H 4.67 0.02 1 435 . 108 ASP CB C 42.08 0.20 1 436 . 109 ILE N N 122.45 0.20 1 437 . 109 ILE H H 8.57 0.02 1 438 . 109 ILE CA C 62.18 0.20 1 439 . 109 ILE HA H 4.17 0.02 1 440 . 109 ILE CB C 38.96 0.20 1 441 . 110 ASN N N 120.57 0.20 1 442 . 110 ASN H H 8.58 0.02 1 443 . 110 ASN CA C 53.14 0.20 1 444 . 110 ASN HA H 4.81 0.02 1 445 . 110 ASN CB C 38.94 0.20 1 446 . 112 ASN N N 119.54 0.20 1 447 . 112 ASN H H 8.26 0.02 1 448 . 112 ASN CA C 52.81 0.20 1 449 . 112 ASN HA H 4.74 0.02 1 450 . 112 ASN CB C 38.87 0.20 1 451 . 113 ALA N N 125.69 0.20 1 452 . 113 ALA H H 8.11 0.02 1 453 . 113 ALA CA C 50.61 0.20 1 454 . 113 ALA HA H 4.60 0.02 1 455 . 113 ALA CB C 18.06 0.20 1 456 . 115 VAL N N 120.67 0.20 1 457 . 115 VAL H H 8.13 0.02 1 458 . 115 VAL CA C 62.14 0.20 1 459 . 115 VAL HA H 4.10 0.02 1 460 . 115 VAL CB C 32.46 0.20 1 461 . 116 PHE N N 124.85 0.20 1 462 . 116 PHE H H 8.36 0.02 1 463 . 116 PHE CA C 57.35 0.20 1 464 . 116 PHE HA H 4.68 0.02 1 465 . 116 PHE CB C 39.59 0.20 1 466 . 117 ASN N N 123.82 0.20 1 467 . 117 ASN H H 8.32 0.02 1 468 . 117 ASN CA C 55.73 0.20 1 469 . 117 ASN HA H 4.96 0.02 1 470 . 117 ASN CB C 39.30 0.20 1 471 . 120 THR N N 115.05 0.20 1 472 . 120 THR H H 7.88 0.02 1 473 . 120 THR CA C 61.76 0.20 1 474 . 120 THR HA H 4.33 0.02 1 475 . 120 THR CB C 69.56 0.20 1 476 . 121 TYR N N 122.86 0.20 1 477 . 121 TYR H H 8.05 0.02 1 478 . 121 TYR CA C 57.98 0.20 1 479 . 121 TYR HA H 4.58 0.02 1 480 . 121 TYR CB C 38.56 0.20 1 481 . 122 GLN N N 123.52 0.20 1 482 . 122 GLN H H 8.23 0.02 1 483 . 122 GLN CA C 55.67 0.20 1 484 . 122 GLN HA H 4.44 0.02 1 485 . 122 GLN CB C 29.42 0.20 1 486 . 123 GLY N N 109.64 0.20 1 487 . 123 GLY H H 7.75 0.02 1 488 . 123 GLY CA C 45.01 0.20 1 489 . 123 GLY HA2 H 3.92 0.02 1 490 . 123 GLY HA3 H 3.92 0.02 1 491 . 124 GLN N N 120.10 0.20 1 492 . 124 GLN H H 8.18 0.02 1 493 . 124 GLN CA C 55.68 0.20 1 494 . 124 GLN HA H 4.39 0.02 1 495 . 124 GLN CB C 29.53 0.20 1 496 . 125 VAL N N 123.52 0.20 1 497 . 125 VAL H H 8.23 0.02 1 498 . 125 VAL CA C 59.69 0.20 1 499 . 125 VAL HA H 4.41 0.02 1 500 . 125 VAL CB C 32.44 0.20 1 501 . 127 GLU N N 121.67 0.20 1 502 . 127 GLU H H 8.57 0.02 1 503 . 127 GLU CA C 57.26 0.20 1 504 . 127 GLU HA H 4.22 0.02 1 505 . 127 GLU CB C 30.00 0.20 1 506 . 128 ASN N N 118.56 0.20 1 507 . 128 ASN H H 8.38 0.02 1 508 . 128 ASN CA C 53.39 0.20 1 509 . 128 ASN HA H 4.70 0.02 1 510 . 128 ASN CB C 38.69 0.20 1 511 . 130 VAL N N 118.88 0.20 1 512 . 130 VAL H H 7.65 0.02 1 513 . 130 VAL CA C 60.67 0.20 1 514 . 130 VAL HA H 4.91 0.02 1 515 . 130 VAL CB C 34.76 0.20 1 516 . 131 ASN N N 127.54 0.20 1 517 . 131 ASN H H 9.38 0.02 1 518 . 131 ASN CA C 56.27 0.20 1 519 . 131 ASN HA H 4.77 0.02 1 520 . 131 ASN CB C 41.85 0.20 1 521 . 133 ARG N N 119.84 0.20 1 522 . 133 ARG H H 8.14 0.02 1 523 . 133 ARG CA C 56.47 0.20 1 524 . 133 ARG HA H 4.34 0.02 1 525 . 133 ARG CB C 30.40 0.20 1 526 . 134 ILE N N 121.59 0.20 1 527 . 134 ILE H H 7.97 0.02 1 528 . 134 ILE CA C 61.23 0.20 1 529 . 134 ILE HA H 4.18 0.02 1 530 . 134 ILE CB C 38.48 0.20 1 531 . 135 ALA N N 127.49 0.20 1 532 . 135 ALA H H 8.27 0.02 1 533 . 135 ALA CA C 52.48 0.20 1 534 . 135 ALA HA H 4.40 0.02 1 535 . 135 ALA CB C 19.24 0.20 1 536 . 136 THR N N 113.60 0.20 1 537 . 136 THR H H 7.99 0.02 1 538 . 136 THR CA C 61.62 0.20 1 539 . 136 THR HA H 4.32 0.02 1 540 . 136 THR CB C 69.67 0.20 1 541 . 137 LEU N N 125.09 0.20 1 542 . 137 LEU H H 8.09 0.02 1 543 . 137 LEU CA C 55.01 0.20 1 544 . 137 LEU HA H 4.39 0.02 1 545 . 137 LEU CB C 42.41 0.20 1 546 . 138 LYS N N 123.28 0.20 1 547 . 138 LYS H H 8.30 0.02 1 548 . 138 LYS CA C 55.68 0.20 1 549 . 138 LYS HA H 4.42 0.02 1 550 . 138 LYS CB C 32.86 0.20 1 551 . 139 VAL N N 122.61 0.20 1 552 . 139 VAL H H 8.26 0.02 1 553 . 139 VAL CA C 62.05 0.20 1 554 . 139 VAL HA H 4.26 0.02 1 555 . 139 VAL CB C 32.85 0.20 1 556 . 140 THR N N 119.87 0.20 1 557 . 140 THR H H 8.31 0.02 1 558 . 140 THR CA C 61.54 0.20 1 559 . 140 THR HA H 4.44 0.02 1 560 . 140 THR CB C 69.63 0.20 1 561 . 141 ASP N N 122.96 0.20 1 562 . 141 ASP H H 8.33 0.02 1 563 . 141 ASP CA C 54.30 0.20 1 564 . 141 ASP HA H 4.67 0.02 1 565 . 141 ASP CB C 41.12 0.20 1 566 . 142 ASP N N 121.16 0.20 1 567 . 142 ASP H H 8.27 0.02 1 568 . 142 ASP CA C 54.42 0.20 1 569 . 142 ASP HA H 4.63 0.02 1 570 . 142 ASP CB C 41.11 0.20 1 571 . 143 ASP N N 120.59 0.20 1 572 . 143 ASP H H 8.22 0.02 1 573 . 143 ASP CA C 54.08 0.20 1 574 . 143 ASP HA H 4.63 0.02 1 575 . 143 ASP CB C 41.09 0.20 1 576 . 144 ALA N N 125.25 0.20 1 577 . 144 ALA H H 7.99 0.02 1 578 . 144 ALA CA C 50.70 0.20 1 579 . 144 ALA HA H 4.56 0.02 1 580 . 144 ALA CB C 18.15 0.20 1 581 . 147 THR N N 116.72 0.20 1 582 . 147 THR H H 7.97 0.02 1 583 . 147 THR CA C 59.71 0.20 1 584 . 147 THR HA H 4.59 0.02 1 585 . 147 THR CB C 69.57 0.20 1 586 . 150 TRP N N 119.20 0.20 1 587 . 150 TRP H H 7.82 0.02 1 588 . 150 TRP CA C 57.32 0.20 1 589 . 150 TRP HA H 4.59 0.02 1 590 . 150 TRP CB C 29.32 0.20 1 591 . 151 LYS N N 122.84 0.20 1 592 . 151 LYS H H 7.66 0.02 1 593 . 151 LYS CA C 55.94 0.20 1 594 . 151 LYS HA H 4.16 0.02 1 595 . 151 LYS CB C 32.94 0.20 1 596 . 152 ALA N N 124.79 0.20 1 597 . 152 ALA H H 7.89 0.02 1 598 . 152 ALA CA C 52.51 0.20 1 599 . 152 ALA HA H 4.17 0.02 1 600 . 152 ALA CB C 19.23 0.20 1 601 . 153 VAL N N 118.83 0.20 1 602 . 153 VAL H H 7.82 0.02 1 603 . 153 VAL CA C 62.10 0.20 1 604 . 153 VAL HA H 4.09 0.02 1 605 . 153 VAL CB C 33.02 0.20 1 606 . 158 ASN N N 121.27 0.20 1 607 . 158 ASN H H 8.37 0.02 1 608 . 158 ASN CA C 53.35 0.20 1 609 . 158 ASN HA H 4.76 0.02 1 610 . 158 ASN CB C 38.73 0.20 1 611 . 159 ASP N N 121.53 0.20 1 612 . 159 ASP H H 8.25 0.02 1 613 . 159 ASP CA C 53.35 0.20 1 614 . 159 ASP CB C 38.73 0.20 1 615 . 161 ASP N N 119.00 0.20 1 616 . 161 ASP H H 8.34 0.02 1 617 . 161 ASP CA C 54.65 0.20 1 618 . 161 ASP HA H 4.59 0.02 1 619 . 161 ASP CB C 40.94 0.20 1 620 . 162 GLN N N 119.95 0.20 1 621 . 162 GLN H H 7.90 0.02 1 622 . 162 GLN CA C 55.68 0.20 1 623 . 162 GLN HA H 4.31 0.02 1 624 . 162 GLN CB C 29.21 0.20 1 625 . 163 GLN N N 120.86 0.20 1 626 . 163 GLN H H 8.20 0.02 1 627 . 163 GLN CA C 56.16 0.20 1 628 . 163 GLN HA H 4.28 0.02 1 629 . 163 GLN CB C 29.30 0.20 1 630 . 164 PHE N N 121.03 0.20 1 631 . 164 PHE H H 8.18 0.02 1 632 . 164 PHE CA C 54.38 0.20 1 633 . 164 PHE HA H 4.31 0.02 1 634 . 164 PHE CB C 41.17 0.20 1 635 . 165 VAL N N 122.60 0.20 1 636 . 165 VAL H H 7.99 0.02 1 637 . 165 VAL CA C 61.94 0.20 1 638 . 165 VAL CB C 32.62 0.20 1 639 . 166 VAL N N 126.02 0.20 1 640 . 166 VAL H H 8.36 0.02 1 641 . 166 VAL CA C 61.93 0.20 1 642 . 166 VAL HA H 4.24 0.02 1 643 . 166 VAL CB C 32.81 0.20 1 644 . 167 VAL N N 124.46 0.20 1 645 . 167 VAL H H 8.20 0.02 1 646 . 167 VAL CA C 61.93 0.20 1 647 . 167 VAL HA H 4.10 0.02 1 648 . 167 VAL CB C 32.82 0.20 1 649 . 168 THR N N 119.17 0.20 1 650 . 168 THR H H 8.25 0.02 1 651 . 168 THR CA C 61.55 0.20 1 652 . 168 THR HA H 4.36 0.02 1 653 . 168 THR CB C 69.74 0.20 1 654 . 169 ASP N N 123.04 0.20 1 655 . 169 ASP H H 8.43 0.02 1 656 . 169 ASP CA C 53.76 0.20 1 657 . 169 ASP CB C 41.12 0.20 1 658 . 171 THR N N 113.38 0.20 1 659 . 171 THR H H 8.38 0.02 1 660 . 171 THR CA C 62.60 0.20 1 661 . 171 THR HA H 4.38 0.02 1 662 . 171 THR CB C 69.39 0.20 1 663 . 172 THR N N 115.36 0.20 1 664 . 172 THR H H 7.89 0.02 1 665 . 172 THR CA C 61.76 0.20 1 666 . 172 THR HA H 4.40 0.02 1 667 . 172 THR CB C 69.56 0.20 1 668 . 175 GLY N N 108.95 0.20 1 669 . 175 GLY H H 8.29 0.02 1 670 . 175 GLY CA C 45.56 0.20 1 671 . 176 ILE N N 120.66 0.20 1 672 . 176 ILE H H 7.87 0.02 1 673 . 176 ILE CA C 61.15 0.20 1 674 . 176 ILE HA H 4.16 0.02 1 675 . 176 ILE CB C 38.32 0.20 1 676 . 177 LEU N N 125.74 0.20 1 677 . 177 LEU H H 8.24 0.02 1 678 . 177 LEU CA C 55.27 0.20 1 679 . 177 LEU HA H 4.39 0.02 1 680 . 177 LEU CB C 42.04 0.20 1 681 . 178 LYS N N 123.58 0.20 1 682 . 178 LYS H H 8.27 0.02 1 683 . 178 LYS CA C 55.76 0.20 1 684 . 178 LYS HA H 4.32 0.02 1 685 . 178 LYS CB C 32.94 0.20 1 686 . 179 THR N N 114.68 0.20 1 687 . 179 THR H H 8.00 0.02 1 688 . 179 THR CA C 61.55 0.20 1 689 . 179 THR HA H 4.36 0.02 1 690 . 179 THR CB C 69.27 0.20 1 691 . 182 GLY N N 110.44 0.20 1 692 . 182 GLY H H 8.35 0.02 1 693 . 182 GLY CA C 45.04 0.20 1 694 . 182 GLY HA2 H 4.00 0.02 1 695 . 182 GLY HA3 H 4.00 0.02 1 696 . 187 ALA N N 124.72 0.20 1 697 . 187 ALA H H 8.10 0.02 1 698 . 187 ALA CA C 52.83 0.20 1 699 . 187 ALA CB C 19.15 0.20 1 700 . 199 ASN N N 119.58 0.20 1 701 . 199 ASN H H 8.43 0.02 1 702 . 199 ASN CA C 53.22 0.20 1 703 . 199 ASN CB C 38.88 0.20 1 704 . 200 GLU N N 121.43 0.20 1 705 . 200 GLU H H 8.32 0.02 1 706 . 200 GLU CA C 56.37 0.20 1 707 . 200 GLU HA H 4.35 0.02 1 708 . 200 GLU CB C 30.27 0.20 1 709 . 201 GLU N N 123.78 0.20 1 710 . 201 GLU H H 8.39 0.02 1 711 . 201 GLU CA C 54.18 0.20 1 712 . 201 GLU HA H 4.61 0.02 1 713 . 201 GLU CB C 29.85 0.20 1 714 . 204 GLU N N 122.35 0.20 1 715 . 204 GLU H H 8.93 0.02 1 716 . 204 GLU CA C 55.13 0.20 1 717 . 204 GLU HA H 5.38 0.02 1 718 . 204 GLU CB C 32.97 0.20 1 719 . 205 GLY N N 110.14 0.20 1 720 . 205 GLY H H 8.57 0.02 1 721 . 205 GLY CA C 45.27 0.20 1 722 . 205 GLY HA2 H 3.96 0.02 1 723 . 205 GLY HA3 H 3.96 0.02 1 724 . 206 SER N N 115.66 0.20 1 725 . 206 SER H H 8.13 0.02 1 726 . 206 SER CA C 58.27 0.20 1 727 . 206 SER HA H 4.48 0.02 1 728 . 206 SER CB C 63.85 0.20 1 729 . 207 LEU N N 124.41 0.20 1 730 . 207 LEU H H 8.26 0.02 1 731 . 207 LEU CA C 54.96 0.20 1 732 . 207 LEU HA H 4.42 0.02 1 733 . 207 LEU CB C 42.18 0.20 1 734 . 208 VAL N N 123.05 0.20 1 735 . 208 VAL H H 8.08 0.02 1 736 . 208 VAL CA C 59.64 0.20 1 737 . 208 VAL HA H 4.42 0.02 1 738 . 208 VAL CB C 32.54 0.20 1 739 . 210 SER N N 116.76 0.20 1 740 . 210 SER H H 8.46 0.02 1 741 . 210 SER CA C 58.20 0.20 1 742 . 210 SER HA H 4.52 0.02 1 743 . 210 SER CB C 63.77 0.20 1 744 . 211 THR N N 115.98 0.20 1 745 . 211 THR H H 8.16 0.02 1 746 . 211 THR CA C 61.48 0.20 1 747 . 211 THR HA H 4.40 0.02 1 748 . 211 THR CB C 69.58 0.20 1 749 . 212 ALA N N 126.65 0.20 1 750 . 212 ALA H H 8.25 0.02 1 751 . 212 ALA CA C 52.28 0.20 1 752 . 212 ALA HA H 4.41 0.02 1 753 . 212 ALA CB C 19.25 0.20 1 754 . 213 THR N N 115.01 0.20 1 755 . 213 THR H H 8.15 0.02 1 756 . 213 THR CA C 61.75 0.20 1 757 . 213 THR HA H 4.37 0.02 1 758 . 213 THR CB C 69.61 0.20 1 759 . 214 VAL N N 123.65 0.20 1 760 . 214 VAL H H 8.19 0.02 1 761 . 214 VAL CA C 61.96 0.20 1 762 . 214 VAL HA H 4.27 0.02 1 763 . 214 VAL CB C 32.73 0.20 1 764 . 215 THR N N 117.39 0.20 1 765 . 215 THR H H 8.18 0.02 1 766 . 215 THR CA C 61.20 0.20 1 767 . 215 THR HA H 4.45 0.02 1 768 . 215 THR CB C 69.81 0.20 1 769 . 216 VAL N N 122.90 0.20 1 770 . 216 VAL H H 8.18 0.02 1 771 . 216 VAL CA C 61.62 0.20 1 772 . 216 VAL HA H 4.22 0.02 1 773 . 216 VAL CB C 32.93 0.20 1 774 . 217 ASP N N 124.85 0.20 1 775 . 217 ASP H H 8.38 0.02 1 776 . 217 ASP CA C 54.12 0.20 1 777 . 217 ASP HA H 4.73 0.02 1 778 . 217 ASP CB C 41.21 0.20 1 779 . 218 VAL N N 121.15 0.20 1 780 . 218 VAL H H 8.10 0.02 1 781 . 218 VAL CA C 62.00 0.20 1 782 . 218 VAL HA H 4.14 0.02 1 783 . 218 VAL CB C 32.70 0.20 1 784 . 219 VAL N N 125.67 0.20 1 785 . 219 VAL H H 8.26 0.02 1 786 . 219 VAL CA C 61.91 0.20 1 787 . 219 VAL HA H 4.14 0.02 1 788 . 219 VAL CB C 32.74 0.20 1 789 . 220 ASP N N 125.15 0.20 1 790 . 220 ASP H H 8.40 0.02 1 791 . 220 ASP CA C 53.71 0.20 1 792 . 220 ASP HA H 4.70 0.02 1 793 . 220 ASP CB C 41.34 0.20 1 794 . 221 VAL N N 120.94 0.20 1 795 . 221 VAL H H 8.12 0.02 1 796 . 222 ASN N N 121.92 0.20 1 797 . 222 ASN H H 8.49 0.02 1 798 . 222 ASN CA C 53.22 0.20 1 799 . 222 ASN HA H 4.75 0.02 1 800 . 222 ASN CB C 39.12 0.20 1 801 . 223 GLU N N 121.82 0.20 1 802 . 223 GLU H H 8.19 0.02 1 803 . 223 GLU CA C 56.08 0.20 1 804 . 223 GLU HA H 4.30 0.02 1 805 . 223 GLU CB C 30.40 0.20 1 806 . 224 ALA N N 127.07 0.20 1 807 . 224 ALA H H 8.22 0.02 1 808 . 224 ALA CA C 50.22 0.20 1 809 . 224 ALA HA H 4.62 0.02 1 810 . 224 ALA CB C 18.18 0.20 1 811 . 226 ILE N N 120.85 0.20 1 812 . 226 ILE H H 8.06 0.02 1 813 . 226 ILE CA C 60.90 0.20 1 814 . 226 ILE HA H 4.13 0.02 1 815 . 226 ILE CB C 38.78 0.20 1 816 . 227 PHE N N 128.90 0.20 1 817 . 227 PHE H H 7.67 0.02 1 818 . 227 PHE CA C 58.68 0.20 1 819 . 227 PHE HA H 4.50 0.02 1 820 . 227 PHE CB C 40.42 0.20 1 stop_ save_