data_16059 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Paramecium bursaria Chlorella virus 1 (PBCV1) DNA ligase (holo form) ; _BMRB_accession_number 16059 _BMRB_flat_file_name bmr16059.str _Entry_type original _Submission_date 2008-12-13 _Accession_date 2008-12-13 _Entry_origination author _NMR_STAR_version 2.1.1 _Experimental_method NMR _Details 'Lys 27 (..ATPKIDG...) is adenylated' loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Piserchio Andrea . . 2 Nair Pravin A. . 3 Shuman Stewart . . 4 Ghose Ranajeet . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 248 "13C chemical shifts" 733 "15N chemical shifts" 248 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2009-08-20 update BMRB 'added PubMed ID' 2009-06-05 update BMRB 'completed entry citation' 2009-01-15 original author 'original release' stop_ save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title 'Sequence-specific 1H N, 13C, and 15N backbone resonance assignments of the 34 kDa Paramecium bursaria Chlorella virus 1 (PBCV1) DNA ligase' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 19636951 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Piserchio Andrea . . 2 Nair Pravin A. . 3 Shuman Stewart . . 4 Ghose Ranajeet . . stop_ _Journal_abbreviation 'Biomol. NMR Assignments' _Journal_name_full 'Biomolecular NMR Assignments' _Journal_volume 3 _Journal_issue 1 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 77 _Page_last 80 _Year 2009 _Details . save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name 'Chv DNA Ligase Monomer' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'Chv DNA Ligase' $Chv_DNA_Ligase 'adenosine monophosphate' $AMP stop_ _System_molecular_weight 34.2 _System_physical_state native _System_oligomer_state ? _System_paramagnetic no _System_thiol_state . _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_Chv_DNA_Ligase _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common Chv_DNA_Ligase _Molecular_mass . _Mol_thiol_state 'all free' loop_ _Biological_function 'DNA Ligase' stop_ _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 319 _Mol_residue_sequence ; MGHHHHHHHHHHSSGHIEGR HMAITKPLLAATLENIEDVQ FPCLATPKIDGIRSVKQTQM LSRTFKPIRNSVMNRLLTEL LPEGSDGEISIEGATFQDTT SAVMTGHKMYNAKFSYYWFD YVTDDPLKKYIDRVEDMKNY ITVHPHILEHAQVKIIPLIP VEINNITELLQYERDVLSKG FEGVMIRKPDGKYKFGRSTL KEGILLKMKQFKDAEATIIS MTALFKNTNTKTKDNFGYSK RSTHKSGKVEEDVMGSIEVD YDGVVFSIGTGFDADQRRDF WQNKESYIGKMVKFKYFEMG SKDCPRFPVFIGIRHEEDR ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 -20 MET 2 -19 GLY 3 -18 HIS 4 -17 HIS 5 -16 HIS 6 -15 HIS 7 -14 HIS 8 -13 HIS 9 -12 HIS 10 -11 HIS 11 -10 HIS 12 -9 HIS 13 -8 SER 14 -7 SER 15 -6 GLY 16 -5 HIS 17 -4 ILE 18 -3 GLU 19 -2 GLY 20 -1 ARG 21 0 HIS 22 1 MET 23 2 ALA 24 3 ILE 25 4 THR 26 5 LYS 27 6 PRO 28 7 LEU 29 8 LEU 30 9 ALA 31 10 ALA 32 11 THR 33 12 LEU 34 13 GLU 35 14 ASN 36 15 ILE 37 16 GLU 38 17 ASP 39 18 VAL 40 19 GLN 41 20 PHE 42 21 PRO 43 22 CYS 44 23 LEU 45 24 ALA 46 25 THR 47 26 PRO 48 27 LYS 49 28 ILE 50 29 ASP 51 30 GLY 52 31 ILE 53 32 ARG 54 33 SER 55 34 VAL 56 35 LYS 57 36 GLN 58 37 THR 59 38 GLN 60 39 MET 61 40 LEU 62 41 SER 63 42 ARG 64 43 THR 65 44 PHE 66 45 LYS 67 46 PRO 68 47 ILE 69 48 ARG 70 49 ASN 71 50 SER 72 51 VAL 73 52 MET 74 53 ASN 75 54 ARG 76 55 LEU 77 56 LEU 78 57 THR 79 58 GLU 80 59 LEU 81 60 LEU 82 61 PRO 83 62 GLU 84 63 GLY 85 64 SER 86 65 ASP 87 66 GLY 88 67 GLU 89 68 ILE 90 69 SER 91 70 ILE 92 71 GLU 93 72 GLY 94 73 ALA 95 74 THR 96 75 PHE 97 76 GLN 98 77 ASP 99 78 THR 100 79 THR 101 80 SER 102 81 ALA 103 82 VAL 104 83 MET 105 84 THR 106 85 GLY 107 86 HIS 108 87 LYS 109 88 MET 110 89 TYR 111 90 ASN 112 91 ALA 113 92 LYS 114 93 PHE 115 94 SER 116 95 TYR 117 96 TYR 118 97 TRP 119 98 PHE 120 99 ASP 121 100 TYR 122 101 VAL 123 102 THR 124 103 ASP 125 104 ASP 126 105 PRO 127 106 LEU 128 107 LYS 129 108 LYS 130 109 TYR 131 110 ILE 132 111 ASP 133 112 ARG 134 113 VAL 135 114 GLU 136 115 ASP 137 116 MET 138 117 LYS 139 118 ASN 140 119 TYR 141 120 ILE 142 121 THR 143 122 VAL 144 123 HIS 145 124 PRO 146 125 HIS 147 126 ILE 148 127 LEU 149 128 GLU 150 129 HIS 151 130 ALA 152 131 GLN 153 132 VAL 154 133 LYS 155 134 ILE 156 135 ILE 157 136 PRO 158 137 LEU 159 138 ILE 160 139 PRO 161 140 VAL 162 141 GLU 163 142 ILE 164 143 ASN 165 144 ASN 166 145 ILE 167 146 THR 168 147 GLU 169 148 LEU 170 149 LEU 171 150 GLN 172 151 TYR 173 152 GLU 174 153 ARG 175 154 ASP 176 155 VAL 177 156 LEU 178 157 SER 179 158 LYS 180 159 GLY 181 160 PHE 182 161 GLU 183 162 GLY 184 163 VAL 185 164 MET 186 165 ILE 187 166 ARG 188 167 LYS 189 168 PRO 190 169 ASP 191 170 GLY 192 171 LYS 193 172 TYR 194 173 LYS 195 174 PHE 196 175 GLY 197 176 ARG 198 177 SER 199 178 THR 200 179 LEU 201 180 LYS 202 181 GLU 203 182 GLY 204 183 ILE 205 184 LEU 206 185 LEU 207 186 LYS 208 187 MET 209 188 LYS 210 189 GLN 211 190 PHE 212 191 LYS 213 192 ASP 214 193 ALA 215 194 GLU 216 195 ALA 217 196 THR 218 197 ILE 219 198 ILE 220 199 SER 221 200 MET 222 201 THR 223 202 ALA 224 203 LEU 225 204 PHE 226 205 LYS 227 206 ASN 228 207 THR 229 208 ASN 230 209 THR 231 210 LYS 232 211 THR 233 212 LYS 234 213 ASP 235 214 ASN 236 215 PHE 237 216 GLY 238 217 TYR 239 218 SER 240 219 LYS 241 220 ARG 242 221 SER 243 222 THR 244 223 HIS 245 224 LYS 246 225 SER 247 226 GLY 248 227 LYS 249 228 VAL 250 229 GLU 251 230 GLU 252 231 ASP 253 232 VAL 254 233 MET 255 234 GLY 256 235 SER 257 236 ILE 258 237 GLU 259 238 VAL 260 239 ASP 261 240 TYR 262 241 ASP 263 242 GLY 264 243 VAL 265 244 VAL 266 245 PHE 267 246 SER 268 247 ILE 269 248 GLY 270 249 THR 271 250 GLY 272 251 PHE 273 252 ASP 274 253 ALA 275 254 ASP 276 255 GLN 277 256 ARG 278 257 ARG 279 258 ASP 280 259 PHE 281 260 TRP 282 261 GLN 283 262 ASN 284 263 LYS 285 264 GLU 286 265 SER 287 266 TYR 288 267 ILE 289 268 GLY 290 269 LYS 291 270 MET 292 271 VAL 293 272 LYS 294 273 PHE 295 274 LYS 296 275 TYR 297 276 PHE 298 277 GLU 299 278 MET 300 279 GLY 301 280 SER 302 281 LYS 303 282 ASP 304 283 CYS 305 284 PRO 306 285 ARG 307 286 PHE 308 287 PRO 309 288 VAL 310 289 PHE 311 290 ILE 312 291 GLY 313 292 ILE 314 293 ARG 315 294 HIS 316 295 GLU 317 296 GLU 318 297 ASP 319 298 ARG stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2014-03-05 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 1FVI "Crystal Structure Of Chlorella Virus Dna Ligase-Adenylate" 93.10 297 99.66 99.66 0.00e+00 PDB 1P8L "New Crystal Structure Of Chlorella Virus Dna Ligase-Adenylate" 93.42 304 100.00 100.00 0.00e+00 PDB 2Q2T "Structure Of Chlorella Virus Dna Ligase-Adenylate Bound To A 5' Phosphorylated Nick" 100.00 319 100.00 100.00 0.00e+00 PDB 2Q2U "Structure Of Chlorella Virus Dna Ligase-Product Dna Complex" 100.00 319 100.00 100.00 0.00e+00 GB AAC96909 "ATP-dependent DNA ligase [Paramecium bursaria Chlorella virus 1]" 93.42 298 100.00 100.00 0.00e+00 GB AGE48553 "DNA ligase [Paramecium bursaria Chlorella virus AN69C]" 93.42 298 99.33 100.00 0.00e+00 GB AGE51623 "DNA ligase [Paramecium bursaria Chlorella virus CviKI]" 93.10 298 96.97 98.99 0.00e+00 GB AGE52640 "DNA ligase [Paramecium bursaria Chlorella virus CvsA1]" 93.10 298 96.97 98.99 0.00e+00 GB AGE53996 "DNA ligase [Paramecium bursaria Chlorella virus IL-3A]" 93.42 298 99.33 100.00 0.00e+00 REF NP_048900 "ATP-dependent DNA ligase [Paramecium bursaria Chlorella virus 1]" 93.42 298 100.00 100.00 0.00e+00 stop_ save_ ############# # Ligands # ############# save_AMP _Saveframe_category ligand _Mol_type non-polymer _Name_common "AMP (ADENOSINE MONOPHOSPHATE)" _BMRB_code . _PDB_code AMP _Molecular_mass 347.221 _Mol_charge 0 _Mol_paramagnetic . _Mol_aromatic yes _Details ; Information obtained from PDB's Chemical Component Dictionary at http://wwpdb-remediation.rutgers.edu/downloads.html Downloaded on Tue Nov 18 18:13:55 2008 ; loop_ _Atom_name _PDB_atom_name _Atom_type _Atom_chirality _Atom_charge _Atom_oxidation_number _Atom_unpaired_electrons P P P . 0 . ? O1P O1P O . 0 . ? O2P O2P O . 0 . ? O3P O3P O . 0 . ? O5' O5' O . 0 . ? C5' C5' C . 0 . ? C4' C4' C . 0 . ? O4' O4' O . 0 . ? C3' C3' C . 0 . ? O3' O3' O . 0 . ? C2' C2' C . 0 . ? O2' O2' O . 0 . ? C1' C1' C . 0 . ? N9 N9 N . 0 . ? C8 C8 C . 0 . ? N7 N7 N . 0 . ? C5 C5 C . 0 . ? C6 C6 C . 0 . ? N6 N6 N . 0 . ? N1 N1 N . 0 . ? C2 C2 C . 0 . ? N3 N3 N . 0 . ? C4 C4 C . 0 . ? HOP2 HOP2 H . 0 . ? HOP3 HOP3 H . 0 . ? H5'1 H5'1 H . 0 . ? H5'2 H5'2 H . 0 . ? H4' H4' H . 0 . ? H3' H3' H . 0 . ? HO3' HO3' H . 0 . ? H2' H2' H . 0 . ? HO2' HO2' H . 0 . ? H1' H1' H . 0 . ? H8 H8 H . 0 . ? HN61 HN61 H . 0 . ? HN62 HN62 H . 0 . ? H2 H2 H . 0 . ? stop_ loop_ _Bond_order _Bond_atom_one_atom_name _Bond_atom_two_atom_name _PDB_bond_atom_one_atom_name _PDB_bond_atom_two_atom_name DOUB P O1P ? ? SING P O2P ? ? SING P O3P ? ? SING P O5' ? ? SING O2P HOP2 ? ? SING O3P HOP3 ? ? SING O5' C5' ? ? SING C5' C4' ? ? SING C5' H5'1 ? ? SING C5' H5'2 ? ? SING C4' O4' ? ? SING C4' C3' ? ? SING C4' H4' ? ? SING O4' C1' ? ? SING C3' O3' ? ? SING C3' C2' ? ? SING C3' H3' ? ? SING O3' HO3' ? ? SING C2' O2' ? ? SING C2' C1' ? ? SING C2' H2' ? ? SING O2' HO2' ? ? SING C1' N9 ? ? SING C1' H1' ? ? SING N9 C8 ? ? SING N9 C4 ? ? DOUB C8 N7 ? ? SING C8 H8 ? ? SING N7 C5 ? ? SING C5 C6 ? ? DOUB C5 C4 ? ? SING C6 N6 ? ? DOUB C6 N1 ? ? SING N6 HN61 ? ? SING N6 HN62 ? ? SING N1 C2 ? ? DOUB C2 N3 ? ? SING C2 H2 ? ? SING N3 C4 ? ? stop_ _Mol_thiol_state . _Sequence_homology_query_date . save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $Chv_DNA_Ligase 'Chlorella virus' 10507 Viruses . Chlorovirus 'Chlorella virus' 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 $Chv_DNA_Ligase 'recombinant technology' . Escherichia coli . Pet 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 $Chv_DNA_Ligase 0.3 mM '[U-13C; U-15N; U-2H]' $AMP 0.3 mM 'natural abundance' MES 20 mM 'natural abundance' 'sodium chloride' 300 mM 'natural abundance' DTT 2 mM 'natural abundance' EDTA 1 mM 'natural abundance' stop_ save_ ############################ # Computer software used # ############################ save_SPARKY _Saveframe_category software _Name SPARKY _Version . loop_ _Vendor _Address _Electronic_address Goddard . . stop_ loop_ _Task 'chemical shift assignment' stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model Avance _Field_strength 800 _Details . save_ save_spectrometer_2 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model Avance _Field_strength 900 _Details . save_ ############################# # NMR applied experiments # ############################# save_2D_1H-15N_HSQC_1 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-15N HSQC' _Sample_label $sample_1 save_ save_3D_HNCO_2 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCO' _Sample_label $sample_1 save_ save_3D_HNCA_3 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCA' _Sample_label $sample_1 save_ save_3D_HNCACB_4 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCACB' _Sample_label $sample_1 save_ save_3D_HN(CO)CA_5 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HN(CO)CA' _Sample_label $sample_1 save_ save_3D_HN(CO)CACB_6 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HN(CO)CACB' _Sample_label $sample_1 save_ save_3D_1H-15N_NOESY_7 _Saveframe_category NMR_applied_experiment _Experiment_name '3D 1H-15N NOESY' _Sample_label $sample_1 save_ ####################### # Sample conditions # ####################### save_sample_conditions_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units 'ionic strength' 0.302 . M pH 6.5 . pH pressure 1 . atm temperature 298.15 . K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference_1 _Saveframe_category chemical_shift_reference _Details . loop_ _Mol_common_name _Atom_type _Atom_isotope_number _Atom_group _Chem_shift_units _Chem_shift_value _Reference_method _Reference_type _External_reference_sample_geometry _External_reference_location _External_reference_axis _Indirect_shift_ratio DSS C 13 'methyl protons' ppm 0 internal indirect . . . 0.25144952 DSS H 1 'methyl protons' ppm 0 internal direct . . . 1.0 DSS N 15 'methyl protons' ppm 0 internal indirect . . . 0.10132905 stop_ save_ ################################### # Assigned chemical shift lists # ################################### ################################################################### # Chemical Shift Ambiguity Index Value Definitions # # # # The values other than 1 are used for those atoms with different # # chemical shifts that cannot be assigned to stereospecific atoms # # or to specific residues or chains. # # # # Index Value Definition # # # # 1 Unique (including isolated methyl protons, # # geminal atoms, and geminal methyl # # groups with identical chemical shifts) # # (e.g. ILE HD11, HD12, HD13 protons) # # 2 Ambiguity of geminal atoms or geminal methyl # # proton groups (e.g. ASP HB2 and HB3 # # protons, LEU CD1 and CD2 carbons, or # # LEU HD11, HD12, HD13 and HD21, HD22, # # HD23 methyl protons) # # 3 Aromatic atoms on opposite sides of # # symmetrical rings (e.g. TYR HE1 and HE2 # # protons) # # 4 Intraresidue ambiguities (e.g. LYS HG and # # HD protons or TRP HZ2 and HZ3 protons) # # 5 Interresidue ambiguities (LYS 12 vs. LYS 27) # # 6 Intermolecular ambiguities (e.g. ASP 31 CA # # in monomer 1 and ASP 31 CA in monomer 2 # # of an asymmetrical homodimer, duplex # # DNA assignments, or other assignments # # that may apply to atoms in one or more # # molecule in the molecular assembly) # # 9 Ambiguous, specific ambiguity not defined # # # ################################################################### save_assigned_chem_shift_list_1 _Saveframe_category assigned_chemical_shifts _Details ; Please note that the chemical shifts 1H and 15N resonances have been extracted from TROSY-based experiments (no TROSY correction has been performed. ; loop_ _Experiment_label '3D 1H-15N NOESY' stop_ loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $sample_conditions_1 _Chem_shift_reference_set_label $chemical_shift_reference_1 _Mol_system_component_name 'Chv DNA Ligase' _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 1 22 MET C C 174.8 0.1 1 2 1 22 MET CA C 54.67 0.3 1 3 1 22 MET CB C 32.27 0.3 1 4 2 23 ALA H H 8.096 0.006 1 5 2 23 ALA C C 177.5 0.1 1 6 2 23 ALA CA C 52.8 0.3 1 7 2 23 ALA CB C 18.86 0.3 1 8 2 23 ALA N N 125.7 0.05 1 9 3 24 ILE H H 7.816 0.006 1 10 3 24 ILE CA C 60.44 0.3 1 11 3 24 ILE CB C 38.34 0.3 1 12 3 24 ILE N N 117.4 0.05 1 13 4 25 THR H H 5.326 0.006 1 14 4 25 THR C C 174.2 0.1 1 15 4 25 THR CA C 63.65 0.3 1 16 4 25 THR CB C 67.97 0.3 1 17 4 25 THR N N 118 0.05 1 18 5 26 LYS H H 6.658 0.006 1 19 5 26 LYS CA C 53.87 0.3 1 20 5 26 LYS CB C 34.61 0.3 1 21 5 26 LYS N N 117.8 0.05 1 22 6 27 PRO C C 175.5 0.1 1 23 6 27 PRO CA C 62.42 0.3 1 24 6 27 PRO CB C 30.69 0.3 1 25 7 28 LEU H H 7.186 0.006 1 26 7 28 LEU C C 176.8 0.1 1 27 7 28 LEU CA C 55.27 0.3 1 28 7 28 LEU CB C 40.62 0.3 1 29 7 28 LEU N N 122.5 0.05 1 30 8 29 LEU H H 7.697 0.006 1 31 8 29 LEU C C 176.2 0.1 1 32 8 29 LEU CA C 52.48 0.3 1 33 8 29 LEU CB C 44.14 0.3 1 34 8 29 LEU N N 125.7 0.05 1 35 9 30 ALA H H 8.245 0.006 1 36 9 30 ALA C C 178.1 0.1 1 37 9 30 ALA CA C 51.19 0.3 1 38 9 30 ALA CB C 21.46 0.3 1 39 9 30 ALA N N 123.1 0.05 1 40 10 31 ALA H H 8.155 0.006 1 41 10 31 ALA C C 177.2 0.1 1 42 10 31 ALA CA C 50.13 0.3 1 43 10 31 ALA CB C 18.43 0.3 1 44 10 31 ALA N N 124.5 0.05 1 45 11 32 THR H H 8.684 0.006 1 46 11 32 THR C C 173 0.1 1 47 11 32 THR CA C 63.44 0.3 1 48 11 32 THR CB C 68.87 0.3 1 49 11 32 THR N N 119.5 0.05 1 50 12 33 LEU H H 8.266 0.006 1 51 12 33 LEU CA C 54.57 0.3 1 52 12 33 LEU CB C 42.88 0.3 1 53 12 33 LEU N N 129.2 0.05 1 54 14 35 ASN C C 176.1 0.1 1 55 14 35 ASN CA C 51.14 0.3 1 56 15 36 ILE H H 8.881 0.006 1 57 15 36 ILE CA C 63.52 0.3 1 58 15 36 ILE CB C 37.31 0.3 1 59 15 36 ILE N N 125.1 0.05 1 60 16 37 GLU C C 176.7 0.1 1 61 16 37 GLU CA C 58.06 0.3 1 62 16 37 GLU CB C 28.19 0.3 1 63 17 38 ASP H H 7.761 0.006 1 64 17 38 ASP C C 176.6 0.1 1 65 17 38 ASP CA C 55.16 0.3 1 66 17 38 ASP CB C 40.72 0.3 1 67 17 38 ASP N N 117 0.05 1 68 18 39 VAL H H 7.043 0.006 1 69 18 39 VAL C C 174.5 0.1 1 70 18 39 VAL CA C 63.23 0.3 1 71 18 39 VAL CB C 30.85 0.3 1 72 18 39 VAL N N 121.5 0.05 1 73 19 40 GLN H H 8.369 0.006 1 74 19 40 GLN C C 173.9 0.1 1 75 19 40 GLN CA C 53.79 0.3 1 76 19 40 GLN CB C 28.98 0.3 1 77 19 40 GLN N N 126.9 0.05 1 78 20 41 PHE H H 8.259 0.006 1 79 20 41 PHE CA C 55.78 0.3 1 80 20 41 PHE CB C 40.02 0.3 1 81 20 41 PHE N N 120.1 0.05 1 82 21 42 PRO C C 175.6 0.1 1 83 21 42 PRO CA C 62.34 0.3 1 84 22 43 CYS H H 9.101 0.006 1 85 22 43 CYS C C 171.8 0.1 1 86 22 43 CYS CA C 54.95 0.3 1 87 22 43 CYS CB C 30.83 0.3 1 88 22 43 CYS N N 115.6 0.05 1 89 23 44 LEU H H 8.508 0.006 1 90 23 44 LEU C C 176.1 0.1 1 91 23 44 LEU CA C 52.95 0.3 1 92 23 44 LEU CB C 43.72 0.3 1 93 23 44 LEU N N 120.4 0.05 1 94 24 45 ALA H H 9.122 0.006 1 95 24 45 ALA C C 175.9 0.1 1 96 24 45 ALA CA C 50.57 0.3 1 97 24 45 ALA CB C 22.66 0.3 1 98 24 45 ALA N N 129.6 0.05 1 99 25 46 THR H H 8.593 0.006 1 100 25 46 THR CA C 58.44 0.3 1 101 25 46 THR CB C 70.7 0.3 1 102 25 46 THR N N 109.1 0.05 1 103 26 47 PRO C C 175.2 0.1 1 104 26 47 PRO CA C 61.76 0.3 1 105 26 47 PRO CB C 30.84 0.3 1 106 27 48 LYS H H 7.635 0.006 1 107 27 48 LYS C C 174.8 0.1 1 108 27 48 LYS CA C 56.54 0.3 1 109 27 48 LYS CB C 32.95 0.3 1 110 27 48 LYS N N 121.4 0.05 1 111 28 49 ILE H H 9.4 0.006 1 112 28 49 ILE C C 175.7 0.1 1 113 28 49 ILE CA C 58 0.3 1 114 28 49 ILE CB C 36.4 0.3 1 115 28 49 ILE N N 129.8 0.05 1 116 29 50 ASP H H 8.7 0.006 1 117 29 50 ASP C C 175.1 0.1 1 118 29 50 ASP CA C 52.42 0.3 1 119 29 50 ASP CB C 40.96 0.3 1 120 29 50 ASP N N 128.6 0.05 1 121 30 51 GLY H H 7.735 0.006 1 122 30 51 GLY C C 172.1 0.1 1 123 30 51 GLY CA C 45.04 0.3 1 124 30 51 GLY N N 112.1 0.05 1 125 31 52 ILE H H 9.036 0.006 1 126 31 52 ILE C C 175.9 0.1 1 127 31 52 ILE CA C 57.64 0.3 1 128 31 52 ILE CB C 37.56 0.3 1 129 31 52 ILE N N 121.2 0.05 1 130 32 53 ARG H H 8.508 0.006 1 131 32 53 ARG C C 175.7 0.1 1 132 32 53 ARG CA C 55.57 0.3 1 133 32 53 ARG CB C 30.49 0.3 1 134 32 53 ARG N N 131.6 0.05 1 135 33 54 SER H H 8.756 0.006 1 136 33 54 SER C C 173.4 0.1 1 137 33 54 SER CA C 57.22 0.3 1 138 33 54 SER CB C 65.03 0.3 1 139 33 54 SER N N 120 0.05 1 140 34 55 VAL H H 8.19 0.006 1 141 34 55 VAL C C 175 0.1 1 142 34 55 VAL CA C 57.8 0.3 1 143 34 55 VAL CB C 34.17 0.3 1 144 34 55 VAL N N 125.8 0.05 1 145 35 56 LYS H H 8.61 0.006 1 146 35 56 LYS C C 177.1 0.1 1 147 35 56 LYS CA C 55.37 0.3 1 148 35 56 LYS CB C 32.55 0.3 1 149 35 56 LYS N N 124.4 0.05 1 150 36 57 GLN H H 8.306 0.006 1 151 36 57 GLN CA C 55.46 0.3 1 152 36 57 GLN CB C 28.99 0.3 1 153 36 57 GLN N N 133 0.05 1 154 38 59 GLN CA C 52.95 0.3 1 155 38 59 GLN CB C 30.26 0.3 1 156 39 60 MET H H 8.094 0.006 1 157 39 60 MET C C 176.1 0.1 1 158 39 60 MET CA C 53.42 0.3 1 159 39 60 MET CB C 26.82 0.3 1 160 39 60 MET N N 115.9 0.05 1 161 40 61 LEU H H 8.986 0.006 1 162 40 61 LEU C C 178.1 0.1 1 163 40 61 LEU CA C 52.02 0.3 1 164 40 61 LEU CB C 44.67 0.3 1 165 40 61 LEU N N 123.2 0.05 1 166 41 62 SER H H 9.182 0.006 1 167 41 62 SER C C 175.8 0.1 1 168 41 62 SER CA C 56.78 0.3 1 169 41 62 SER CB C 65.17 0.3 1 170 41 62 SER N N 117.9 0.05 1 171 42 63 ARG H H 9.276 0.006 1 172 42 63 ARG C C 176.1 0.1 1 173 42 63 ARG CA C 58.43 0.3 1 174 42 63 ARG CB C 28.91 0.3 1 175 42 63 ARG N N 118 0.05 1 176 43 64 THR H H 7.567 0.006 1 177 43 64 THR C C 177.1 0.1 1 178 43 64 THR CA C 60.94 0.3 1 179 43 64 THR CB C 67.95 0.3 1 180 43 64 THR N N 107.7 0.05 1 181 44 65 PHE H H 8.444 0.006 1 182 44 65 PHE C C 174.1 0.1 1 183 44 65 PHE CA C 58.59 0.3 1 184 44 65 PHE CB C 33.31 0.3 1 185 44 65 PHE N N 118.4 0.05 1 186 45 66 LYS H H 7.164 0.006 1 187 45 66 LYS CA C 52.6 0.3 1 188 45 66 LYS CB C 31.25 0.3 1 189 45 66 LYS N N 117.2 0.05 1 190 46 67 PRO C C 177.7 0.1 1 191 46 67 PRO CA C 62.93 0.3 1 192 46 67 PRO CB C 31.04 0.3 1 193 47 68 ILE H H 7.823 0.006 1 194 47 68 ILE CA C 60.24 0.3 1 195 47 68 ILE CB C 35.63 0.3 1 196 47 68 ILE N N 121.7 0.05 1 197 48 69 ARG H H 7.561 0.006 1 198 48 69 ARG C C 176.3 0.1 1 199 48 69 ARG CA C 57.76 0.3 1 200 48 69 ARG CB C 29.35 0.3 1 201 48 69 ARG N N 125.5 0.05 1 202 49 70 ASN H H 7.224 0.006 1 203 49 70 ASN C C 175.6 0.1 1 204 49 70 ASN CA C 53.65 0.3 1 205 49 70 ASN CB C 36.26 0.3 1 206 49 70 ASN N N 116.9 0.05 1 207 50 71 SER H H 8.294 0.006 1 208 50 71 SER C C 176.3 0.1 1 209 50 71 SER CA C 61.1 0.3 1 210 50 71 SER CB C 62.43 0.3 1 211 50 71 SER N N 125.6 0.05 1 212 51 72 VAL H H 7.605 0.006 1 213 51 72 VAL C C 177.9 0.1 1 214 51 72 VAL CA C 65.88 0.3 1 215 51 72 VAL CB C 31.09 0.3 1 216 51 72 VAL N N 124.3 0.05 1 217 52 73 MET H H 7.126 0.006 1 218 52 73 MET C C 177.6 0.1 1 219 52 73 MET CA C 59.09 0.3 1 220 52 73 MET CB C 32.25 0.3 1 221 52 73 MET N N 117.2 0.05 1 222 53 74 ASN H H 8.1 0.006 1 223 53 74 ASN C C 177.8 0.1 1 224 53 74 ASN CA C 55.79 0.3 1 225 53 74 ASN CB C 38.55 0.3 1 226 53 74 ASN N N 114.3 0.05 1 227 54 75 ARG H H 8.332 0.006 1 228 54 75 ARG C C 178.8 0.1 1 229 54 75 ARG CA C 60.05 0.3 1 230 54 75 ARG CB C 29.12 0.3 1 231 54 75 ARG N N 121.4 0.05 1 232 55 76 LEU H H 8.126 0.006 1 233 55 76 LEU C C 179.1 0.1 1 234 55 76 LEU CA C 57.62 0.3 1 235 55 76 LEU CB C 42.18 0.3 1 236 55 76 LEU N N 118.1 0.05 1 237 56 77 LEU H H 7.682 0.006 1 238 56 77 LEU C C 178.1 0.1 1 239 56 77 LEU CA C 57.35 0.3 1 240 56 77 LEU CB C 39 0.3 1 241 56 77 LEU N N 116.2 0.05 1 242 57 78 THR H H 8.292 0.006 1 243 57 78 THR C C 176.3 0.1 1 244 57 78 THR CA C 67.68 0.3 1 245 57 78 THR N N 115.1 0.05 1 246 58 79 GLU H H 7.495 0.006 1 247 58 79 GLU C C 178.2 0.1 1 248 58 79 GLU CA C 58.25 0.3 1 249 58 79 GLU CB C 29.06 0.3 1 250 58 79 GLU N N 119.2 0.05 1 251 59 80 LEU H H 7.2 0.006 1 252 59 80 LEU C C 177 0.1 1 253 59 80 LEU CA C 56.63 0.3 1 254 59 80 LEU CB C 44.24 0.3 1 255 59 80 LEU N N 118.3 0.05 1 256 60 81 LEU H H 7.589 0.006 1 257 60 81 LEU CA C 51.2 0.3 1 258 60 81 LEU CB C 40.49 0.3 1 259 60 81 LEU N N 117.3 0.05 1 260 61 82 PRO C C 178.4 0.1 1 261 61 82 PRO CA C 60.88 0.3 1 262 61 82 PRO CB C 30.95 0.3 1 263 62 83 GLU H H 8.406 0.006 1 264 62 83 GLU C C 176.4 0.1 1 265 62 83 GLU CA C 57.08 0.3 1 266 62 83 GLU CB C 29.24 0.3 1 267 62 83 GLU N N 123.2 0.05 1 268 63 84 GLY H H 8.29 0.006 1 269 63 84 GLY C C 175.4 0.1 1 270 63 84 GLY CA C 44.82 0.3 1 271 63 84 GLY N N 112.1 0.05 1 272 64 85 SER H H 7.162 0.006 1 273 64 85 SER C C 175.9 0.1 1 274 64 85 SER CA C 61.8 0.3 1 275 64 85 SER CB C 63.74 0.3 1 276 64 85 SER N N 116.7 0.05 1 277 65 86 ASP H H 8.264 0.006 1 278 65 86 ASP C C 174.5 0.1 1 279 65 86 ASP CA C 52.17 0.3 1 280 65 86 ASP CB C 44.42 0.3 1 281 65 86 ASP N N 121.8 0.05 1 282 66 87 GLY H H 7.512 0.006 1 283 66 87 GLY C C 171.9 0.1 1 284 66 87 GLY CA C 45.7 0.3 1 285 66 87 GLY N N 117.9 0.05 1 286 67 88 GLU H H 7.656 0.006 1 287 67 88 GLU C C 174.5 0.1 1 288 67 88 GLU CA C 53.3 0.3 1 289 67 88 GLU CB C 33.2 0.3 1 290 67 88 GLU N N 116.8 0.05 1 291 68 89 ILE H H 9.124 0.006 1 292 68 89 ILE C C 175.4 0.1 1 293 68 89 ILE CA C 61.11 0.3 1 294 68 89 ILE CB C 39.47 0.3 1 295 68 89 ILE N N 124.3 0.05 1 296 69 90 SER H H 8.884 0.006 1 297 69 90 SER C C 172.7 0.1 1 298 69 90 SER CA C 56.96 0.3 1 299 69 90 SER CB C 65.42 0.3 1 300 69 90 SER N N 121.2 0.05 1 301 70 91 ILE H H 8.162 0.006 1 302 70 91 ILE C C 176.4 0.1 1 303 70 91 ILE CA C 60.36 0.3 1 304 70 91 ILE CB C 38.31 0.3 1 305 70 91 ILE N N 126 0.05 1 306 71 92 GLU H H 8.927 0.006 1 307 71 92 GLU C C 178.3 0.1 1 308 71 92 GLU CA C 57.95 0.3 1 309 71 92 GLU CB C 28.42 0.3 1 310 71 92 GLU N N 129.7 0.05 1 311 72 93 GLY H H 8.907 0.006 1 312 72 93 GLY C C 173.5 0.1 1 313 72 93 GLY CA C 45.4 0.3 1 314 72 93 GLY N N 114.2 0.05 1 315 73 94 ALA H H 7.546 0.006 1 316 73 94 ALA C C 178.8 0.1 1 317 73 94 ALA CA C 50.63 0.3 1 318 73 94 ALA CB C 20.34 0.3 1 319 73 94 ALA N N 123.3 0.05 1 320 74 95 THR H H 8.627 0.006 1 321 74 95 THR CA C 60.81 0.3 1 322 74 95 THR CB C 71.11 0.3 1 323 74 95 THR N N 112 0.05 1 324 75 96 PHE H H 9.292 0.006 1 325 75 96 PHE C C 178.9 0.1 1 326 75 96 PHE CA C 61.53 0.3 1 327 75 96 PHE CB C 38.38 0.3 1 328 75 96 PHE N N 125.3 0.05 1 329 76 97 GLN H H 8.742 0.006 1 330 76 97 GLN C C 178.4 0.1 1 331 76 97 GLN CA C 58.87 0.3 1 332 76 97 GLN CB C 27.28 0.3 1 333 76 97 GLN N N 121 0.05 1 334 77 98 ASP H H 7.808 0.006 1 335 77 98 ASP C C 179.4 0.1 1 336 77 98 ASP CA C 56.88 0.3 1 337 77 98 ASP CB C 39.46 0.3 1 338 77 98 ASP N N 121.5 0.05 1 339 78 99 THR H H 8.428 0.006 1 340 78 99 THR C C 175.7 0.1 1 341 78 99 THR CA C 66.66 0.3 1 342 78 99 THR N N 121 0.05 1 343 79 100 THR H H 8.181 0.006 1 344 79 100 THR C C 176 0.1 1 345 79 100 THR CA C 67.27 0.3 1 346 79 100 THR N N 118.2 0.05 1 347 80 101 SER H H 7.843 0.006 1 348 80 101 SER C C 176.5 0.1 1 349 80 101 SER CA C 61.03 0.3 1 350 80 101 SER CB C 62.13 0.3 1 351 80 101 SER N N 115.5 0.05 1 352 81 102 ALA H H 7.672 0.006 1 353 81 102 ALA C C 178.3 0.1 1 354 81 102 ALA CA C 55.08 0.3 1 355 81 102 ALA CB C 18.29 0.3 1 356 81 102 ALA N N 123.3 0.05 1 357 82 103 VAL H H 7.67 0.006 1 358 82 103 VAL C C 176.3 0.1 1 359 82 103 VAL CA C 64.31 0.3 1 360 82 103 VAL CB C 32.55 0.3 1 361 82 103 VAL N N 115.5 0.05 1 362 83 104 MET H H 8.039 0.006 1 363 83 104 MET C C 176 0.1 1 364 83 104 MET CA C 53.66 0.3 1 365 83 104 MET N N 112.5 0.05 1 366 84 105 THR H H 7.001 0.006 1 367 84 105 THR C C 174.2 0.1 1 368 84 105 THR CA C 61.33 0.3 1 369 84 105 THR CB C 69.94 0.3 1 370 84 105 THR N N 114.2 0.05 1 371 85 106 GLY H H 8.544 0.006 1 372 85 106 GLY CA C 46.09 0.3 1 373 85 106 GLY N N 113 0.05 1 374 90 111 ASN C C 174.5 0.1 1 375 91 112 ALA H H 5.753 0.006 1 376 91 112 ALA C C 176.4 0.1 1 377 91 112 ALA CA C 51.6 0.3 1 378 91 112 ALA CB C 18.3 0.3 1 379 91 112 ALA N N 123.1 0.05 1 380 92 113 LYS H H 8.018 0.006 1 381 92 113 LYS C C 177.4 0.1 1 382 92 113 LYS CA C 56.26 0.3 1 383 92 113 LYS CB C 32.15 0.3 1 384 92 113 LYS N N 119.7 0.05 1 385 93 114 PHE H H 7.992 0.006 1 386 93 114 PHE C C 172.5 0.1 1 387 93 114 PHE CA C 55.76 0.3 1 388 93 114 PHE CB C 40.13 0.3 1 389 93 114 PHE N N 116.5 0.05 1 390 94 115 SER H H 9.044 0.006 1 391 94 115 SER C C 172.7 0.1 1 392 94 115 SER CA C 56.39 0.3 1 393 94 115 SER CB C 65.62 0.3 1 394 94 115 SER N N 115.1 0.05 1 395 95 116 TYR H H 8.669 0.006 1 396 95 116 TYR C C 174.3 0.1 1 397 95 116 TYR CA C 56.52 0.3 1 398 95 116 TYR CB C 41.35 0.3 1 399 95 116 TYR N N 122.9 0.05 1 400 96 117 TYR H H 8.845 0.006 1 401 96 117 TYR C C 173.2 0.1 1 402 96 117 TYR CA C 56.85 0.3 1 403 96 117 TYR CB C 38.65 0.3 1 404 96 117 TYR N N 128.4 0.05 1 405 97 118 TRP H H 8.483 0.006 1 406 97 118 TRP C C 174.2 0.1 1 407 97 118 TRP CA C 53.73 0.3 1 408 97 118 TRP CB C 30.51 0.3 1 409 97 118 TRP N N 127.5 0.05 1 410 98 119 PHE H H 8.456 0.006 1 411 98 119 PHE C C 175.7 0.1 1 412 98 119 PHE CA C 53.91 0.3 1 413 98 119 PHE CB C 40.4 0.3 1 414 98 119 PHE N N 120.3 0.05 1 415 99 120 ASP H H 8.784 0.006 1 416 99 120 ASP C C 174.6 0.1 1 417 99 120 ASP CA C 53.43 0.3 1 418 99 120 ASP CB C 44.53 0.3 1 419 99 120 ASP N N 122.7 0.05 1 420 100 121 TYR H H 10.26 0.006 1 421 100 121 TYR C C 173.2 0.1 1 422 100 121 TYR CA C 54.02 0.3 1 423 100 121 TYR CB C 40.08 0.3 1 424 100 121 TYR N N 125.1 0.05 1 425 101 122 VAL H H 8.758 0.006 1 426 101 122 VAL C C 174.4 0.1 1 427 101 122 VAL CA C 61.15 0.3 1 428 101 122 VAL CB C 31.52 0.3 1 429 101 122 VAL N N 131.5 0.05 1 430 102 123 THR H H 8.046 0.006 1 431 102 123 THR C C 175 0.1 1 432 102 123 THR CA C 60.17 0.3 1 433 102 123 THR CB C 68.51 0.3 1 434 102 123 THR N N 117.4 0.05 1 435 103 124 ASP H H 8.571 0.006 1 436 103 124 ASP C C 175.7 0.1 1 437 103 124 ASP CA C 54.63 0.3 1 438 103 124 ASP CB C 40.68 0.3 1 439 103 124 ASP N N 118.5 0.05 1 440 104 125 ASP H H 7.749 0.006 1 441 104 125 ASP CA C 51.14 0.3 1 442 104 125 ASP CB C 42.08 0.3 1 443 104 125 ASP N N 118.1 0.05 1 444 105 126 PRO C C 174.8 0.1 1 445 105 126 PRO CA C 64.16 0.3 1 446 105 126 PRO CB C 31.58 0.3 1 447 106 127 LEU H H 8.187 0.006 1 448 106 127 LEU C C 177.9 0.1 1 449 106 127 LEU CA C 54.41 0.3 1 450 106 127 LEU CB C 39.35 0.3 1 451 106 127 LEU N N 116.6 0.05 1 452 107 128 LYS H H 7.115 0.006 1 453 107 128 LYS C C 175.6 0.1 1 454 107 128 LYS CA C 57.09 0.3 1 455 107 128 LYS CB C 32.4 0.3 1 456 107 128 LYS N N 123.1 0.05 1 457 108 129 LYS H H 8.745 0.006 1 458 108 129 LYS C C 179.2 0.1 1 459 108 129 LYS CA C 57.19 0.3 1 460 108 129 LYS CB C 33.54 0.3 1 461 108 129 LYS N N 125.9 0.05 1 462 109 130 TYR H H 8.255 0.006 1 463 109 130 TYR C C 176.4 0.1 1 464 109 130 TYR CA C 61.63 0.3 1 465 109 130 TYR CB C 37.15 0.3 1 466 109 130 TYR N N 125.7 0.05 1 467 110 131 ILE H H 8.318 0.006 1 468 110 131 ILE C C 176.5 0.1 1 469 110 131 ILE CA C 63.71 0.3 1 470 110 131 ILE CB C 37.52 0.3 1 471 110 131 ILE N N 113.8 0.05 1 472 111 132 ASP H H 6.994 0.006 1 473 111 132 ASP C C 178.7 0.1 1 474 111 132 ASP CA C 56.75 0.3 1 475 111 132 ASP CB C 40.22 0.3 1 476 111 132 ASP N N 122.5 0.05 1 477 112 133 ARG H H 8.266 0.006 1 478 112 133 ARG C C 179.7 0.1 1 479 112 133 ARG CA C 60.56 0.3 1 480 112 133 ARG CB C 26.8 0.3 1 481 112 133 ARG N N 124.8 0.05 1 482 113 134 VAL H H 8.178 0.006 1 483 113 134 VAL C C 178.9 0.1 1 484 113 134 VAL CA C 65.61 0.3 1 485 113 134 VAL CB C 30.2 0.3 1 486 113 134 VAL N N 118.8 0.05 1 487 114 135 GLU H H 7.251 0.006 1 488 114 135 GLU C C 178.9 0.1 1 489 114 135 GLU CA C 59.16 0.3 1 490 114 135 GLU CB C 27.77 0.3 1 491 114 135 GLU N N 121 0.05 1 492 115 136 ASP H H 7.911 0.006 1 493 115 136 ASP C C 180.2 0.1 1 494 115 136 ASP CA C 57.69 0.3 1 495 115 136 ASP CB C 39.31 0.3 1 496 115 136 ASP N N 119.9 0.05 1 497 116 137 MET H H 7.863 0.006 1 498 116 137 MET C C 177.2 0.1 1 499 116 137 MET CA C 59.59 0.3 1 500 116 137 MET CB C 32.5 0.3 1 501 116 137 MET N N 123.6 0.05 1 502 117 138 LYS H H 8.371 0.006 1 503 117 138 LYS C C 180.2 0.1 1 504 117 138 LYS CA C 59.97 0.3 1 505 117 138 LYS CB C 31.41 0.3 1 506 117 138 LYS N N 119 0.05 1 507 118 139 ASN H H 8.886 0.006 1 508 118 139 ASN CA C 55.68 0.3 1 509 118 139 ASN CB C 37.5 0.3 1 510 118 139 ASN N N 118.4 0.05 1 511 119 140 TYR H H 8.186 0.006 1 512 119 140 TYR C C 179.5 0.1 1 513 119 140 TYR CA C 63.03 0.3 1 514 119 140 TYR CB C 38.2 0.3 1 515 119 140 TYR N N 122.5 0.05 1 516 120 141 ILE H H 8.24 0.006 1 517 120 141 ILE C C 177.4 0.1 1 518 120 141 ILE CA C 65.08 0.3 1 519 120 141 ILE CB C 37.28 0.3 1 520 120 141 ILE N N 119.5 0.05 1 521 121 142 THR H H 7.905 0.006 1 522 121 142 THR C C 176.2 0.1 1 523 121 142 THR CA C 66.05 0.3 1 524 121 142 THR CB C 68.34 0.3 1 525 121 142 THR N N 115.8 0.05 1 526 122 143 VAL H H 7.169 0.006 1 527 122 143 VAL C C 175.2 0.1 1 528 122 143 VAL CA C 62.81 0.3 1 529 122 143 VAL CB C 31.45 0.3 1 530 122 143 VAL N N 116.3 0.05 1 531 123 144 HIS H H 7.578 0.006 1 532 123 144 HIS CA C 52.94 0.3 1 533 123 144 HIS CB C 27.59 0.3 1 534 123 144 HIS N N 118.2 0.05 1 535 124 145 PRO C C 179.4 0.1 1 536 124 145 PRO CA C 65.23 0.3 1 537 124 145 PRO CB C 30.72 0.3 1 538 125 146 HIS H H 8.1 0.006 1 539 125 146 HIS C C 178.7 0.1 1 540 125 146 HIS CA C 57.76 0.3 1 541 125 146 HIS CB C 28.37 0.3 1 542 125 146 HIS N N 116.3 0.05 1 543 126 147 ILE H H 7.436 0.006 1 544 126 147 ILE C C 176 0.1 1 545 126 147 ILE CA C 64.02 0.3 1 546 126 147 ILE CB C 36.4 0.3 1 547 126 147 ILE N N 118 0.05 1 548 127 148 LEU H H 7.077 0.006 1 549 127 148 LEU C C 178.1 0.1 1 550 127 148 LEU CA C 54.52 0.3 1 551 127 148 LEU CB C 40.68 0.3 1 552 127 148 LEU N N 116.3 0.05 1 553 128 149 GLU H H 7.432 0.006 1 554 128 149 GLU C C 175.8 0.1 1 555 128 149 GLU CA C 54.5 0.3 1 556 128 149 GLU CB C 29.9 0.3 1 557 128 149 GLU N N 118.2 0.05 1 558 129 150 HIS H H 7.946 0.006 1 559 129 150 HIS C C 176.2 0.1 1 560 129 150 HIS CA C 59.75 0.3 1 561 129 150 HIS CB C 30.68 0.3 1 562 129 150 HIS N N 125.1 0.05 1 563 130 151 ALA H H 7.967 0.006 1 564 130 151 ALA C C 178.3 0.1 1 565 130 151 ALA CA C 53.97 0.3 1 566 130 151 ALA CB C 18.53 0.3 1 567 130 151 ALA N N 126.6 0.05 1 568 131 152 GLN H H 10.05 0.006 1 569 131 152 GLN C C 174.5 0.1 1 570 131 152 GLN CA C 56.88 0.3 1 571 131 152 GLN CB C 30.25 0.3 1 572 131 152 GLN N N 122.2 0.05 1 573 132 153 VAL H H 8.088 0.006 1 574 132 153 VAL C C 173.4 0.1 1 575 132 153 VAL CA C 57.65 0.3 1 576 132 153 VAL CB C 31.78 0.3 1 577 132 153 VAL N N 119.5 0.05 1 578 133 154 LYS H H 8.273 0.006 1 579 133 154 LYS C C 175 0.1 1 580 133 154 LYS CA C 54.45 0.3 1 581 133 154 LYS CB C 31.66 0.3 1 582 133 154 LYS N N 129.7 0.05 1 583 134 155 ILE H H 7.987 0.006 1 584 134 155 ILE C C 175.2 0.1 1 585 134 155 ILE CA C 59.63 0.3 1 586 134 155 ILE CB C 36.07 0.3 1 587 134 155 ILE N N 128.4 0.05 1 588 135 156 ILE H H 8.93 0.006 1 589 135 156 ILE CA C 58.13 0.3 1 590 135 156 ILE CB C 38.91 0.3 1 591 135 156 ILE N N 129.2 0.05 1 592 136 157 PRO C C 176.6 0.1 1 593 136 157 PRO CA C 61.64 0.3 1 594 136 157 PRO CB C 30.43 0.3 1 595 137 158 LEU H H 8.851 0.006 1 596 137 158 LEU C C 173.6 0.1 1 597 137 158 LEU CA C 52.85 0.3 1 598 137 158 LEU CB C 40.55 0.3 1 599 137 158 LEU N N 129.3 0.05 1 600 138 159 ILE H H 7.74 0.006 1 601 138 159 ILE CA C 55.79 0.3 1 602 138 159 ILE CB C 36.05 0.3 1 603 138 159 ILE N N 127.3 0.05 1 604 139 160 PRO C C 176 0.1 1 605 139 160 PRO CA C 62.12 0.3 1 606 140 161 VAL H H 8.657 0.006 1 607 140 161 VAL C C 175.5 0.1 1 608 140 161 VAL CA C 59.88 0.3 1 609 140 161 VAL CB C 33.24 0.3 1 610 140 161 VAL N N 117.6 0.05 1 611 141 162 GLU H H 8.531 0.006 1 612 141 162 GLU C C 174.9 0.1 1 613 141 162 GLU CA C 56.7 0.3 1 614 141 162 GLU CB C 29.75 0.3 1 615 141 162 GLU N N 126.1 0.05 1 616 142 163 ILE H H 8.737 0.006 1 617 142 163 ILE C C 176.5 0.1 1 618 142 163 ILE CA C 58.18 0.3 1 619 142 163 ILE CB C 36.52 0.3 1 620 142 163 ILE N N 127.9 0.05 1 621 143 164 ASN H H 9.109 0.006 1 622 143 164 ASN C C 174.3 0.1 1 623 143 164 ASN CA C 54.81 0.3 1 624 143 164 ASN CB C 41.14 0.3 1 625 143 164 ASN N N 122.7 0.05 1 626 144 165 ASN H H 6.895 0.006 1 627 144 165 ASN C C 174.4 0.1 1 628 144 165 ASN CA C 51.5 0.3 1 629 144 165 ASN CB C 38.98 0.3 1 630 144 165 ASN N N 112.7 0.05 1 631 145 166 ILE H H 8.012 0.006 1 632 145 166 ILE C C 176 0.1 1 633 145 166 ILE CA C 64.06 0.3 1 634 145 166 ILE CB C 37.43 0.3 1 635 145 166 ILE N N 118.4 0.05 1 636 146 167 THR H H 7.668 0.006 1 637 146 167 THR C C 175.2 0.1 1 638 146 167 THR CA C 66.93 0.3 1 639 146 167 THR CB C 67.68 0.3 1 640 146 167 THR N N 119.3 0.05 1 641 147 168 GLU H H 8.191 0.006 1 642 147 168 GLU CA C 58.55 0.3 1 643 147 168 GLU CB C 29.73 0.3 1 644 147 168 GLU N N 120.8 0.05 1 645 154 175 ASP H H 8.31 0.006 1 646 154 175 ASP C C 180.1 0.1 1 647 154 175 ASP CA C 57.14 0.3 1 648 154 175 ASP CB C 40.23 0.3 1 649 154 175 ASP N N 118.9 0.05 1 650 155 176 VAL H H 8.414 0.006 1 651 155 176 VAL CA C 65.7 0.3 1 652 155 176 VAL CB C 30.32 0.3 1 653 155 176 VAL N N 118 0.05 1 654 156 177 LEU H H 8.023 0.006 1 655 156 177 LEU C C 182.55 0.1 1 656 156 177 LEU CA C 56.91 0.3 1 657 156 177 LEU N N 121.9 0.05 1 658 157 178 SER H H 7.88 0.006 1 659 157 178 SER C C 175.1 0.1 1 660 157 178 SER CA C 60.88 0.3 1 661 157 178 SER CB C 62.58 0.3 1 662 157 178 SER N N 116.3 0.05 1 663 158 179 LYS H H 7.264 0.006 1 664 158 179 LYS C C 176.4 0.1 1 665 158 179 LYS CA C 55.64 0.3 1 666 158 179 LYS CB C 32.6 0.3 1 667 158 179 LYS N N 120.5 0.05 1 668 159 180 GLY H H 7.58 0.006 1 669 159 180 GLY C C 174.5 0.1 1 670 159 180 GLY CA C 44.97 0.3 1 671 159 180 GLY N N 106.1 0.05 1 672 160 181 PHE H H 7.455 0.006 1 673 160 181 PHE C C 176 0.1 1 674 160 181 PHE CA C 57.36 0.3 1 675 160 181 PHE CB C 38.52 0.3 1 676 160 181 PHE N N 119.6 0.05 1 677 161 182 GLU H H 9.019 0.006 1 678 161 182 GLU C C 176.2 0.1 1 679 161 182 GLU CA C 56.37 0.3 1 680 161 182 GLU CB C 29.96 0.3 1 681 161 182 GLU N N 117.1 0.05 1 682 162 183 GLY H H 7.116 0.006 1 683 162 183 GLY C C 175 0.1 1 684 162 183 GLY CA C 44.64 0.3 1 685 162 183 GLY N N 103.8 0.05 1 686 163 184 VAL H H 8.408 0.006 1 687 163 184 VAL C C 173.2 0.1 1 688 163 184 VAL CA C 60.69 0.3 1 689 163 184 VAL CB C 35.86 0.3 1 690 163 184 VAL N N 120.2 0.05 1 691 164 185 MET H H 8.964 0.006 1 692 164 185 MET C C 175.2 0.1 1 693 164 185 MET CA C 51.56 0.3 1 694 164 185 MET CB C 29.41 0.3 1 695 164 185 MET N N 123.3 0.05 1 696 165 186 ILE H H 8.917 0.006 1 697 165 186 ILE C C 175.4 0.1 1 698 165 186 ILE CA C 60.23 0.3 1 699 165 186 ILE CB C 40.99 0.3 1 700 165 186 ILE N N 120.9 0.05 1 701 166 187 ARG H H 8.651 0.006 1 702 166 187 ARG C C 176.5 0.1 1 703 166 187 ARG CA C 54.15 0.3 1 704 166 187 ARG CB C 33.9 0.3 1 705 166 187 ARG N N 122.4 0.05 1 706 167 188 LYS H H 6.917 0.006 1 707 167 188 LYS CA C 53.96 0.3 1 708 167 188 LYS CB C 32.36 0.3 1 709 167 188 LYS N N 121.6 0.05 1 710 168 189 PRO C C 175.4 0.1 1 711 168 189 PRO CA C 66.38 0.3 1 712 168 189 PRO CB C 31.47 0.3 1 713 169 190 ASP H H 8.338 0.006 1 714 169 190 ASP C C 176.8 0.1 1 715 169 190 ASP CA C 51.9 0.3 1 716 169 190 ASP CB C 38.58 0.3 1 717 169 190 ASP N N 109.9 0.05 1 718 170 191 GLY H H 7.45 0.006 1 719 170 191 GLY CA C 45.48 0.3 1 720 170 191 GLY N N 105.7 0.05 1 721 171 192 LYS H H 8.15 0.006 1 722 171 192 LYS C C 174.9 0.1 1 723 171 192 LYS CA C 55.19 0.3 1 724 171 192 LYS CB C 32.72 0.3 1 725 171 192 LYS N N 122.7 0.05 1 726 172 193 TYR H H 9.068 0.006 1 727 172 193 TYR C C 173.6 0.1 1 728 172 193 TYR CA C 58.78 0.3 1 729 172 193 TYR CB C 36.44 0.3 1 730 172 193 TYR N N 125 0.05 1 731 173 194 LYS H H 5.564 0.006 1 732 173 194 LYS C C 173.4 0.1 1 733 173 194 LYS CA C 54.96 0.3 1 734 173 194 LYS CB C 34.57 0.3 1 735 173 194 LYS N N 128.3 0.05 1 736 174 195 PHE H H 7.982 0.006 1 737 174 195 PHE C C 175.7 0.1 1 738 174 195 PHE CA C 52.43 0.3 1 739 174 195 PHE CB C 34.97 0.3 1 740 174 195 PHE N N 126 0.05 1 741 175 196 GLY H H 7.576 0.006 1 742 175 196 GLY C C 173.8 0.1 1 743 175 196 GLY CA C 43.51 0.3 1 744 175 196 GLY N N 111.4 0.05 1 745 176 197 ARG H H 8.418 0.006 1 746 176 197 ARG CA C 55.23 0.3 1 747 176 197 ARG CB C 30.02 0.3 1 748 176 197 ARG N N 120.4 0.05 1 749 177 198 SER H H 8.268 0.006 1 750 177 198 SER C C 174.5 0.1 1 751 177 198 SER CA C 58.31 0.3 1 752 177 198 SER CB C 64.2 0.3 1 753 177 198 SER N N 122.1 0.05 1 754 178 199 THR H H 9.342 0.006 1 755 178 199 THR C C 177.3 0.1 1 756 178 199 THR CA C 60.39 0.3 1 757 178 199 THR CB C 70.17 0.3 1 758 178 199 THR N N 117.9 0.05 1 759 179 200 LEU H H 8.745 0.006 1 760 179 200 LEU C C 176 0.1 1 761 179 200 LEU CA C 57.7 0.3 1 762 179 200 LEU CB C 41.01 0.3 1 763 179 200 LEU N N 124.4 0.05 1 764 180 201 LYS H H 8.131 0.006 1 765 180 201 LYS C C 179.5 0.1 1 766 180 201 LYS CA C 58.02 0.3 1 767 180 201 LYS CB C 31.21 0.3 1 768 180 201 LYS N N 118.7 0.05 1 769 181 202 GLU H H 7.667 0.006 1 770 181 202 GLU C C 179.5 0.1 1 771 181 202 GLU CA C 57.86 0.3 1 772 181 202 GLU CB C 29.56 0.3 1 773 181 202 GLU N N 116.8 0.05 1 774 182 203 GLY H H 7.147 0.006 1 775 182 203 GLY C C 173.6 0.1 1 776 182 203 GLY CA C 45.66 0.3 1 777 182 203 GLY N N 101.4 0.05 1 778 183 204 ILE H H 6.667 0.006 1 779 183 204 ILE C C 176.5 0.1 1 780 183 204 ILE CA C 64.78 0.3 1 781 183 204 ILE CB C 38.12 0.3 1 782 183 204 ILE N N 119.3 0.05 1 783 184 205 LEU H H 6.93 0.006 1 784 184 205 LEU C C 172.9 0.1 1 785 184 205 LEU CA C 54.66 0.3 1 786 184 205 LEU CB C 42.97 0.3 1 787 184 205 LEU N N 116.2 0.05 1 788 185 206 LEU H H 9.25 0.006 1 789 185 206 LEU C C 174.8 0.1 1 790 185 206 LEU CA C 52.11 0.3 1 791 185 206 LEU CB C 44.36 0.3 1 792 185 206 LEU N N 127.8 0.05 1 793 186 207 LYS H H 8.71 0.006 1 794 186 207 LYS CA C 54.24 0.3 1 795 186 207 LYS CB C 33.92 0.3 1 796 186 207 LYS N N 122 0.05 1 797 190 211 PHE C C 176.2 0.1 1 798 191 212 LYS H H 7.855 0.006 1 799 191 212 LYS C C 174.6 0.1 1 800 191 212 LYS CA C 54.46 0.3 1 801 191 212 LYS N N 118.1 0.05 1 802 192 213 ASP H H 7.906 0.006 1 803 192 213 ASP C C 175.5 0.1 1 804 192 213 ASP CA C 53.63 0.3 1 805 192 213 ASP CB C 42.94 0.3 1 806 192 213 ASP N N 119.2 0.05 1 807 193 214 ALA H H 8.336 0.006 1 808 193 214 ALA C C 174.4 0.1 1 809 193 214 ALA CA C 51.11 0.3 1 810 193 214 ALA CB C 22.44 0.3 1 811 193 214 ALA N N 123.6 0.05 1 812 194 215 GLU H H 7.805 0.006 1 813 194 215 GLU C C 175.8 0.1 1 814 194 215 GLU CA C 54.23 0.3 1 815 194 215 GLU CB C 32.84 0.3 1 816 194 215 GLU N N 117.3 0.05 1 817 195 216 ALA H H 8.893 0.006 1 818 195 216 ALA C C 175.4 0.1 1 819 195 216 ALA CA C 51.11 0.3 1 820 195 216 ALA CB C 23.84 0.3 1 821 195 216 ALA N N 121.9 0.05 1 822 196 217 THR H H 8.1 0.006 1 823 196 217 THR C C 175.1 0.1 1 824 196 217 THR CA C 62.51 0.3 1 825 196 217 THR CB C 70.39 0.3 1 826 196 217 THR N N 116.9 0.05 1 827 197 218 ILE H H 9.032 0.006 1 828 197 218 ILE C C 176.8 0.1 1 829 197 218 ILE CA C 64.01 0.3 1 830 197 218 ILE CB C 37.09 0.3 1 831 197 218 ILE N N 125.2 0.05 1 832 198 219 ILE H H 9.412 0.006 1 833 198 219 ILE C C 175.9 0.1 1 834 198 219 ILE CA C 61.09 0.3 1 835 198 219 ILE CB C 38.71 0.3 1 836 198 219 ILE N N 126.2 0.05 1 837 199 220 SER H H 7.938 0.006 1 838 199 220 SER C C 172.2 0.1 1 839 199 220 SER CA C 57.47 0.3 1 840 199 220 SER CB C 62.9 0.3 1 841 199 220 SER N N 113.8 0.05 1 842 200 221 MET H H 8.349 0.006 1 843 200 221 MET C C 174.5 0.1 1 844 200 221 MET CA C 55.55 0.3 1 845 200 221 MET CB C 36.67 0.3 1 846 200 221 MET N N 116.5 0.05 1 847 201 222 THR H H 8.829 0.006 1 848 201 222 THR C C 174.3 0.1 1 849 201 222 THR CA C 61.54 0.3 1 850 201 222 THR CB C 67.15 0.3 1 851 201 222 THR N N 118.7 0.05 1 852 202 223 ALA H H 8.887 0.006 1 853 202 223 ALA C C 176.7 0.1 1 854 202 223 ALA CA C 51.94 0.3 1 855 202 223 ALA CB C 17.4 0.3 1 856 202 223 ALA N N 132.1 0.05 1 857 203 224 LEU H H 7.745 0.006 1 858 203 224 LEU C C 176.5 0.1 1 859 203 224 LEU CA C 55.64 0.3 1 860 203 224 LEU CB C 41.75 0.3 1 861 203 224 LEU N N 123.2 0.05 1 862 204 225 PHE H H 8.361 0.006 1 863 204 225 PHE CA C 57.35 0.3 1 864 204 225 PHE CB C 38.39 0.3 1 865 204 225 PHE N N 124.6 0.05 1 866 205 226 LYS H H 8.032 0.006 1 867 205 226 LYS C C 175.7 0.1 1 868 205 226 LYS CA C 55.81 0.3 1 869 205 226 LYS CB C 32.28 0.3 1 870 205 226 LYS N N 123.9 0.05 1 871 206 227 ASN H H 8.218 0.006 1 872 206 227 ASN C C 175.6 0.1 1 873 206 227 ASN CA C 53.08 0.3 1 874 206 227 ASN CB C 38.39 0.3 1 875 206 227 ASN N N 120.2 0.05 1 876 207 228 THR H H 8.007 0.006 1 877 207 228 THR CA C 61.8 0.3 1 878 207 228 THR CB C 69.28 0.3 1 879 207 228 THR N N 114.6 0.05 1 880 208 229 ASN H H 8.367 0.006 1 881 208 229 ASN C C 175.5 0.1 1 882 208 229 ASN CA C 53.12 0.3 1 883 208 229 ASN CB C 38.38 0.3 1 884 208 229 ASN N N 121.4 0.05 1 885 209 230 THR H H 7.98 0.006 1 886 209 230 THR C C 174.7 0.1 1 887 209 230 THR CA C 61.93 0.3 1 888 209 230 THR CB C 69.32 0.3 1 889 209 230 THR N N 114.8 0.05 1 890 210 231 LYS H H 8.237 0.006 1 891 210 231 LYS C C 176.9 0.1 1 892 210 231 LYS CA C 56.25 0.3 1 893 210 231 LYS CB C 31.99 0.3 1 894 210 231 LYS N N 123.7 0.05 1 895 211 232 THR H H 7.966 0.006 1 896 211 232 THR C C 174.6 0.1 1 897 211 232 THR CA C 61.57 0.3 1 898 211 232 THR CB C 69.52 0.3 1 899 211 232 THR N N 115.3 0.05 1 900 212 233 LYS H H 8.192 0.006 1 901 212 233 LYS C C 176.3 0.1 1 902 212 233 LYS CA C 56.27 0.3 1 903 212 233 LYS CB C 32.14 0.3 1 904 212 233 LYS N N 123.3 0.05 1 905 213 234 ASP H H 8.119 0.006 1 906 213 234 ASP C C 179.2 0.1 1 907 213 234 ASP CA C 54.15 0.3 1 908 213 234 ASP CB C 40.8 0.3 1 909 213 234 ASP N N 121 0.05 1 910 214 235 ASN H H 8.131 0.006 1 911 214 235 ASN C C 175.2 0.1 1 912 214 235 ASN CA C 53.14 0.3 1 913 214 235 ASN CB C 38.35 0.3 1 914 214 235 ASN N N 118.8 0.05 1 915 215 236 PHE H H 8.131 0.006 1 916 215 236 PHE C C 176.4 0.1 1 917 215 236 PHE CA C 58 0.3 1 918 215 236 PHE CB C 46.35 0.3 1 919 215 236 PHE N N 120.4 0.05 1 920 216 237 GLY H H 8.139 0.006 1 921 216 237 GLY C C 174.2 0.1 1 922 216 237 GLY CA C 45.15 0.3 1 923 216 237 GLY N N 110 0.05 1 924 217 238 TYR H H 7.903 0.006 1 925 217 238 TYR C C 176.2 0.1 1 926 217 238 TYR CA C 58.01 0.3 1 927 217 238 TYR CB C 38.05 0.3 1 928 217 238 TYR N N 120.6 0.05 1 929 218 239 SER H H 8.122 0.006 1 930 218 239 SER C C 174.5 0.1 1 931 218 239 SER CA C 58.24 0.3 1 932 218 239 SER CB C 63.37 0.3 1 933 218 239 SER N N 117.5 0.05 1 934 219 240 LYS H H 8.117 0.006 1 935 219 240 LYS C C 176.7 0.1 1 936 219 240 LYS CA C 56.26 0.3 1 937 219 240 LYS CB C 31.91 0.3 1 938 219 240 LYS N N 123.4 0.05 1 939 220 241 ARG H H 8.128 0.006 1 940 220 241 ARG C C 176.5 0.1 1 941 220 241 ARG CA C 56.08 0.3 1 942 220 241 ARG CB C 29.91 0.3 1 943 220 241 ARG N N 121.7 0.05 1 944 221 242 SER H H 8.222 0.006 1 945 221 242 SER C C 174.9 0.1 1 946 221 242 SER CA C 58.18 0.3 1 947 221 242 SER CB C 63.38 0.3 1 948 221 242 SER N N 118.8 0.05 1 949 222 243 THR H H 8.032 0.006 1 950 222 243 THR CA C 61.52 0.3 1 951 222 243 THR CB C 69.23 0.3 1 952 222 243 THR N N 115.7 0.05 1 953 224 245 LYS C C 176.6 0.1 1 954 224 245 LYS CA C 56.15 0.3 1 955 224 245 LYS CB C 32.13 0.3 1 956 225 246 SER H H 8.294 0.006 1 957 225 246 SER C C 175.1 0.1 1 958 225 246 SER CA C 58.37 0.3 1 959 225 246 SER CB C 63.39 0.3 1 960 225 246 SER N N 117.3 0.05 1 961 226 247 GLY H H 8.286 0.006 1 962 226 247 GLY C C 173.8 0.1 1 963 226 247 GLY CA C 44.91 0.3 1 964 226 247 GLY N N 111.1 0.05 1 965 227 248 LYS H H 7.999 0.006 1 966 227 248 LYS C C 176.6 0.1 1 967 227 248 LYS CA C 55.72 0.3 1 968 227 248 LYS CB C 32.27 0.3 1 969 227 248 LYS N N 121.6 0.05 1 970 228 249 VAL H H 8.143 0.006 1 971 228 249 VAL C C 176.1 0.1 1 972 228 249 VAL CA C 62.12 0.3 1 973 228 249 VAL CB C 31.96 0.3 1 974 228 249 VAL N N 122.7 0.05 1 975 229 250 GLU H H 8.398 0.006 1 976 229 250 GLU CA C 56.98 0.3 1 977 229 250 GLU CB C 30.42 0.3 1 978 229 250 GLU N N 125.2 0.05 1 979 230 251 GLU H H 8.249 0.006 1 980 230 251 GLU C C 176 0.1 1 981 230 251 GLU CA C 55.82 0.3 1 982 230 251 GLU CB C 29.81 0.3 1 983 230 251 GLU N N 123.8 0.05 1 984 231 252 ASP H H 8.196 0.006 1 985 231 252 ASP CA C 54.16 0.3 1 986 231 252 ASP CB C 41.41 0.3 1 987 231 252 ASP N N 122.5 0.05 1 988 232 253 VAL H H 7.495 0.006 1 989 232 253 VAL C C 173.6 0.1 1 990 232 253 VAL CA C 58.11 0.3 1 991 232 253 VAL CB C 34.66 0.3 1 992 232 253 VAL N N 109.5 0.05 1 993 233 254 MET H H 7.876 0.006 1 994 233 254 MET C C 174.1 0.1 1 995 233 254 MET CA C 57.36 0.3 1 996 233 254 MET CB C 30.32 0.3 1 997 233 254 MET N N 121.4 0.05 1 998 234 255 GLY H H 9.511 0.006 1 999 234 255 GLY C C 173.6 0.1 1 1000 234 255 GLY CA C 45.3 0.3 1 1001 234 255 GLY N N 116.9 0.05 1 1002 235 256 SER H H 7.843 0.006 1 1003 235 256 SER C C 173 0.1 1 1004 235 256 SER CA C 57.93 0.3 1 1005 235 256 SER CB C 65.26 0.3 1 1006 235 256 SER N N 114.6 0.05 1 1007 236 257 ILE H H 8.089 0.006 1 1008 236 257 ILE C C 173.5 0.1 1 1009 236 257 ILE CA C 58.92 0.3 1 1010 236 257 ILE CB C 39.48 0.3 1 1011 236 257 ILE N N 112.1 0.05 1 1012 237 258 GLU H H 8.357 0.006 1 1013 237 258 GLU C C 176 0.1 1 1014 237 258 GLU CA C 55.42 0.3 1 1015 237 258 GLU CB C 29.92 0.3 1 1016 237 258 GLU N N 125.9 0.05 1 1017 238 259 VAL H H 8.615 0.006 1 1018 238 259 VAL C C 172.2 0.1 1 1019 238 259 VAL CA C 56.94 0.3 1 1020 238 259 VAL CB C 33.52 0.3 1 1021 238 259 VAL N N 117.3 0.05 1 1022 239 260 ASP H H 8.502 0.006 1 1023 239 260 ASP C C 176 0.1 1 1024 239 260 ASP CA C 52.4 0.3 1 1025 239 260 ASP CB C 42.83 0.3 1 1026 239 260 ASP N N 118.5 0.05 1 1027 240 261 TYR H H 9.293 0.006 1 1028 240 261 TYR C C 174.2 0.1 1 1029 240 261 TYR CA C 53.9 0.3 1 1030 240 261 TYR CB C 39.29 0.3 1 1031 240 261 TYR N N 128.9 0.05 1 1032 241 262 ASP H H 8.65 0.006 1 1033 241 262 ASP C C 175.2 0.1 1 1034 241 262 ASP CA C 54.75 0.3 1 1035 241 262 ASP CB C 39.35 0.3 1 1036 241 262 ASP N N 127.1 0.05 1 1037 242 263 GLY H H 8.784 0.006 1 1038 242 263 GLY C C 174.6 0.1 1 1039 242 263 GLY CA C 44.89 0.3 1 1040 242 263 GLY N N 106.2 0.05 1 1041 243 264 VAL H H 7.636 0.006 1 1042 243 264 VAL C C 174.5 0.1 1 1043 243 264 VAL CA C 61.59 0.3 1 1044 243 264 VAL CB C 32.25 0.3 1 1045 243 264 VAL N N 123.7 0.05 1 1046 244 265 VAL H H 8.124 0.006 1 1047 244 265 VAL CA C 60.3 0.3 1 1048 244 265 VAL CB C 32.09 0.3 1 1049 244 265 VAL N N 127.2 0.05 1 1050 245 266 PHE C C 172.9 0.1 1 1051 245 266 PHE CA C 55.81 0.3 1 1052 245 266 PHE CB C 39.67 0.3 1 1053 246 267 SER H H 8.38 0.006 1 1054 246 267 SER C C 174.3 0.1 1 1055 246 267 SER CA C 57.65 0.3 1 1056 246 267 SER CB C 64.53 0.3 1 1057 246 267 SER N N 114.8 0.05 1 1058 247 268 ILE H H 9.295 0.006 1 1059 247 268 ILE C C 175.6 0.1 1 1060 247 268 ILE CA C 61.34 0.3 1 1061 247 268 ILE CB C 38.96 0.3 1 1062 247 268 ILE N N 122.5 0.05 1 1063 248 269 GLY H H 8.93 0.006 1 1064 248 269 GLY C C 173.4 0.1 1 1065 248 269 GLY CA C 44.54 0.3 1 1066 248 269 GLY N N 113.9 0.05 1 1067 249 270 THR H H 7.367 0.006 1 1068 249 270 THR C C 172.5 0.1 1 1069 249 270 THR CA C 61.08 0.3 1 1070 249 270 THR CB C 70.38 0.3 1 1071 249 270 THR N N 116 0.05 1 1072 250 271 GLY H H 8.686 0.006 1 1073 250 271 GLY C C 172.2 0.1 1 1074 250 271 GLY CA C 44.42 0.3 1 1075 250 271 GLY N N 112.2 0.05 1 1076 251 272 PHE H H 6.543 0.006 1 1077 251 272 PHE C C 176.4 0.1 1 1078 251 272 PHE CA C 54.88 0.3 1 1079 251 272 PHE CB C 41.53 0.3 1 1080 251 272 PHE N N 116.8 0.05 1 1081 252 273 ASP H H 9.078 0.006 1 1082 252 273 ASP C C 176.4 0.1 1 1083 252 273 ASP CA C 51.92 0.3 1 1084 252 273 ASP CB C 41.27 0.3 1 1085 252 273 ASP N N 124.1 0.05 1 1086 253 274 ALA H H 8.383 0.006 1 1087 253 274 ALA C C 180.9 0.1 1 1088 253 274 ALA CA C 55.68 0.3 1 1089 253 274 ALA CB C 17.95 0.3 1 1090 253 274 ALA N N 120.8 0.05 1 1091 254 275 ASP H H 8.059 0.006 1 1092 254 275 ASP C C 179.3 0.1 1 1093 254 275 ASP CA C 57.21 0.3 1 1094 254 275 ASP CB C 39.76 0.3 1 1095 254 275 ASP N N 119.1 0.05 1 1096 255 276 GLN H H 8.749 0.006 1 1097 255 276 GLN C C 178.9 0.1 1 1098 255 276 GLN CA C 58.39 0.3 1 1099 255 276 GLN CB C 28.22 0.3 1 1100 255 276 GLN N N 121.7 0.05 1 1101 256 277 ARG H H 8.246 0.006 1 1102 256 277 ARG C C 180 0.1 1 1103 256 277 ARG CA C 61.21 0.3 1 1104 256 277 ARG CB C 27.65 0.3 1 1105 256 277 ARG N N 116.9 0.05 1 1106 257 278 ARG H H 7.485 0.006 1 1107 257 278 ARG C C 177.4 0.1 1 1108 257 278 ARG CA C 59.62 0.3 1 1109 257 278 ARG CB C 29.38 0.3 1 1110 257 278 ARG N N 120.4 0.05 1 1111 258 279 ASP H H 8.515 0.006 1 1112 258 279 ASP C C 178.8 0.1 1 1113 258 279 ASP CA C 58.06 0.3 1 1114 258 279 ASP CB C 41.81 0.3 1 1115 258 279 ASP N N 121.1 0.05 1 1116 259 280 PHE H H 9.114 0.006 1 1117 259 280 PHE C C 176.1 0.1 1 1118 259 280 PHE CA C 59.82 0.3 1 1119 259 280 PHE CB C 37.46 0.3 1 1120 259 280 PHE N N 117.6 0.05 1 1121 260 281 TRP H H 6.723 0.006 1 1122 260 281 TRP C C 179.3 0.1 1 1123 260 281 TRP CA C 59.37 0.3 1 1124 260 281 TRP CB C 29.94 0.3 1 1125 260 281 TRP N N 113.4 0.05 1 1126 261 282 GLN H H 8.594 0.006 1 1127 261 282 GLN C C 177.4 0.1 1 1128 261 282 GLN CA C 58.13 0.3 1 1129 261 282 GLN CB C 28 0.3 1 1130 261 282 GLN N N 117.3 0.05 1 1131 262 283 ASN H H 7.656 0.006 1 1132 262 283 ASN C C 175.7 0.1 1 1133 262 283 ASN CA C 51.93 0.3 1 1134 262 283 ASN CB C 38.37 0.3 1 1135 262 283 ASN N N 115.6 0.05 1 1136 263 284 LYS H H 6.724 0.006 1 1137 263 284 LYS C C 178 0.1 1 1138 263 284 LYS CA C 60.71 0.3 1 1139 263 284 LYS CB C 31.96 0.3 1 1140 263 284 LYS N N 121.7 0.05 1 1141 264 285 GLU H H 8.452 0.006 1 1142 264 285 GLU C C 178.7 0.1 1 1143 264 285 GLU CA C 59.1 0.3 1 1144 264 285 GLU CB C 27.94 0.3 1 1145 264 285 GLU N N 116.4 0.05 1 1146 265 286 SER H H 7.752 0.006 1 1147 265 286 SER C C 174.5 0.1 1 1148 265 286 SER CA C 59.51 0.3 1 1149 265 286 SER CB C 62.63 0.3 1 1150 265 286 SER N N 113.5 0.05 1 1151 266 287 TYR H H 7.552 0.006 1 1152 266 287 TYR C C 176.3 0.1 1 1153 266 287 TYR CA C 59.49 0.3 1 1154 266 287 TYR CB C 39.01 0.3 1 1155 266 287 TYR N N 118.8 0.05 1 1156 267 288 ILE H H 7.244 0.006 1 1157 267 288 ILE C C 177.4 0.1 1 1158 267 288 ILE CA C 62.84 0.3 1 1159 267 288 ILE CB C 34.98 0.3 1 1160 267 288 ILE N N 119.6 0.05 1 1161 268 289 GLY H H 8.868 0.006 1 1162 268 289 GLY C C 177.5 0.1 1 1163 268 289 GLY CA C 44.75 0.3 1 1164 268 289 GLY N N 116.8 0.05 1 1165 269 290 LYS H H 7.986 0.006 1 1166 269 290 LYS C C 175.4 0.1 1 1167 269 290 LYS CA C 55.41 0.3 1 1168 269 290 LYS CB C 32.13 0.3 1 1169 269 290 LYS N N 120.3 0.05 1 1170 270 291 MET H H 8.71 0.006 1 1171 270 291 MET C C 176.2 0.1 1 1172 270 291 MET CA C 54.22 0.3 1 1173 270 291 MET CB C 33.1 0.3 1 1174 270 291 MET N N 118.9 0.05 1 1175 271 292 VAL H H 9.364 0.006 1 1176 271 292 VAL C C 174.4 0.1 1 1177 271 292 VAL CA C 58.35 0.3 1 1178 271 292 VAL CB C 33.59 0.3 1 1179 271 292 VAL N N 117 0.05 1 1180 272 293 LYS H H 8.984 0.006 1 1181 272 293 LYS C C 175.4 0.1 1 1182 272 293 LYS CA C 54.53 0.3 1 1183 272 293 LYS CB C 32.8 0.3 1 1184 272 293 LYS N N 122.7 0.05 1 1185 273 294 PHE H H 8.883 0.006 1 1186 273 294 PHE C C 171.7 0.1 1 1187 273 294 PHE CA C 55.27 0.3 1 1188 273 294 PHE CB C 41.77 0.3 1 1189 273 294 PHE N N 121.8 0.05 1 1190 274 295 LYS H H 8.828 0.006 1 1191 274 295 LYS CA C 53.45 0.3 1 1192 274 295 LYS CB C 36.59 0.3 1 1193 274 295 LYS N N 119.4 0.05 1 1194 287 308 PRO C C 177.5 0.1 1 1195 288 309 VAL H H 9.265 0.006 1 1196 288 309 VAL C C 175.1 0.1 1 1197 288 309 VAL CA C 60.14 0.3 1 1198 288 309 VAL CB C 34.72 0.3 1 1199 288 309 VAL N N 119.7 0.05 1 1200 289 310 PHE H H 8.217 0.006 1 1201 289 310 PHE C C 173.2 0.1 1 1202 289 310 PHE CA C 59.28 0.3 1 1203 289 310 PHE N N 127.5 0.05 1 1204 290 311 ILE H H 7.804 0.006 1 1205 290 311 ILE CA C 59.33 0.3 1 1206 290 311 ILE N N 123.2 0.05 1 1207 291 312 GLY H H 6.374 0.006 1 1208 291 312 GLY C C 171.2 0.1 1 1209 291 312 GLY CA C 45.89 0.3 1 1210 291 312 GLY N N 104.7 0.05 1 1211 292 313 ILE H H 8.679 0.006 1 1212 292 313 ILE C C 175.9 0.1 1 1213 292 313 ILE CA C 59.32 0.3 1 1214 292 313 ILE CB C 38.31 0.3 1 1215 292 313 ILE N N 121.2 0.05 1 1216 293 314 ARG H H 8.534 0.006 1 1217 293 314 ARG C C 175.9 0.1 1 1218 293 314 ARG CA C 55.91 0.3 1 1219 293 314 ARG CB C 29.83 0.3 1 1220 293 314 ARG N N 128.2 0.05 1 1221 294 315 HIS H H 8.54 0.006 1 1222 294 315 HIS C C 176.4 0.1 1 1223 294 315 HIS CA C 56.68 0.3 1 1224 294 315 HIS CB C 29.77 0.3 1 1225 294 315 HIS N N 123.6 0.05 1 1226 295 316 GLU H H 8.6 0.006 1 1227 295 316 GLU CA C 56.28 0.3 1 1228 295 316 GLU CB C 29.48 0.3 1 1229 295 316 GLU N N 121.4 0.05 1 stop_ save_