data_6021 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Backbone 1H, 15N and 13C assignments for the subunit a of the E.coli ATP Synthase ; _BMRB_accession_number 6021 _BMRB_flat_file_name bmr6021.str _Entry_type original _Submission_date 2003-11-24 _Accession_date 2003-11-25 _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 Dmitriev Oleg Y. . 2 Abildgaard Frits . . 3 Markley John L. . 4 Fillingame Robert H. . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 244 "13C chemical shifts" 753 "15N chemical shifts" 244 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2004-07-06 original author . stop_ _Original_release_date 2004-07-06 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; Letter to the Editor: Backbone 1H, 15N and 13C assignments for the subunit a of the E.coli ATP Synthase ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 15213458 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Dmitriev Oleg Y. . 2 Abildgaard Frits . . 3 Markley John L.. . 4 Fillingame Robert H . stop_ _Journal_abbreviation 'J. Biomol. NMR' _Journal_volume 29 _Journal_issue 3 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 439 _Page_last 440 _Year 2004 _Details . loop_ _Keyword 'Membrane protein' 'chemical shift assignments' TROSY 'ATP synthase' stop_ save_ ################################## # Molecular system description # ################################## save_system_subunit_a_of_the_ATP_synthase _Saveframe_category molecular_system _Mol_system_name 'subunit a of the ATP synthase' _Abbreviation_common 'subunit a of the ATP synthase' _Enzyme_commission_number 3.6.3.14 loop_ _Mol_system_component_name _Mol_label 'sibunit a' $subunit_a stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state monomer _System_paramagnetic no _System_thiol_state 'not present' _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_subunit_a _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'subunit a of the ATP synthase' _Abbreviation_common none _Molecular_mass . _Mol_thiol_state 'not present' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 277 _Mol_residue_sequence ; MHHHHHHASENMTPQDYIGH HLNNLQLDLRTFSLVDPQNP PATFWTINIDSMFFSVVLGL LFLVLFRSVAKKATSGVPGK FQTAIELVIGFVNGSVKDMY HGKSKLIAPLALTIFVWVFL MNLMDLLPIDLLPYIAEHVL GLPALRVVPSADVNVTLSMA LGVFILILFYSIKMKGIGGF TKELTLQPFNHWAFIPVNLI LEGVSLLSKPVSLGLRLFGN MYAGELIFILIAGLLPWWSQ WILNVPWAIFHILIITLQAF IFMVLTIVYLSMASEEH ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 -6 MET 2 -5 HIS 3 -4 HIS 4 -3 HIS 5 -2 HIS 6 -1 HIS 7 1 HIS 8 2 ALA 9 3 SER 10 4 GLU 11 5 ASN 12 6 MET 13 7 THR 14 8 PRO 15 9 GLN 16 10 ASP 17 11 TYR 18 12 ILE 19 13 GLY 20 14 HIS 21 15 HIS 22 16 LEU 23 17 ASN 24 18 ASN 25 19 LEU 26 20 GLN 27 21 LEU 28 22 ASP 29 23 LEU 30 24 ARG 31 25 THR 32 26 PHE 33 27 SER 34 28 LEU 35 29 VAL 36 30 ASP 37 31 PRO 38 32 GLN 39 33 ASN 40 34 PRO 41 35 PRO 42 36 ALA 43 37 THR 44 38 PHE 45 39 TRP 46 40 THR 47 41 ILE 48 42 ASN 49 43 ILE 50 44 ASP 51 45 SER 52 46 MET 53 47 PHE 54 48 PHE 55 49 SER 56 50 VAL 57 51 VAL 58 52 LEU 59 53 GLY 60 54 LEU 61 55 LEU 62 56 PHE 63 57 LEU 64 58 VAL 65 59 LEU 66 60 PHE 67 61 ARG 68 62 SER 69 63 VAL 70 64 ALA 71 65 LYS 72 66 LYS 73 67 ALA 74 68 THR 75 69 SER 76 70 GLY 77 71 VAL 78 72 PRO 79 73 GLY 80 74 LYS 81 75 PHE 82 76 GLN 83 77 THR 84 78 ALA 85 79 ILE 86 80 GLU 87 81 LEU 88 82 VAL 89 83 ILE 90 84 GLY 91 85 PHE 92 86 VAL 93 87 ASN 94 88 GLY 95 89 SER 96 90 VAL 97 91 LYS 98 92 ASP 99 93 MET 100 94 TYR 101 95 HIS 102 96 GLY 103 97 LYS 104 98 SER 105 99 LYS 106 100 LEU 107 101 ILE 108 102 ALA 109 103 PRO 110 104 LEU 111 105 ALA 112 106 LEU 113 107 THR 114 108 ILE 115 109 PHE 116 110 VAL 117 111 TRP 118 112 VAL 119 113 PHE 120 114 LEU 121 115 MET 122 116 ASN 123 117 LEU 124 118 MET 125 119 ASP 126 120 LEU 127 121 LEU 128 122 PRO 129 123 ILE 130 124 ASP 131 125 LEU 132 126 LEU 133 127 PRO 134 128 TYR 135 129 ILE 136 130 ALA 137 131 GLU 138 132 HIS 139 133 VAL 140 134 LEU 141 135 GLY 142 136 LEU 143 137 PRO 144 138 ALA 145 139 LEU 146 140 ARG 147 141 VAL 148 142 VAL 149 143 PRO 150 144 SER 151 145 ALA 152 146 ASP 153 147 VAL 154 148 ASN 155 149 VAL 156 150 THR 157 151 LEU 158 152 SER 159 153 MET 160 154 ALA 161 155 LEU 162 156 GLY 163 157 VAL 164 158 PHE 165 159 ILE 166 160 LEU 167 161 ILE 168 162 LEU 169 163 PHE 170 164 TYR 171 165 SER 172 166 ILE 173 167 LYS 174 168 MET 175 169 LYS 176 170 GLY 177 171 ILE 178 172 GLY 179 173 GLY 180 174 PHE 181 175 THR 182 176 LYS 183 177 GLU 184 178 LEU 185 179 THR 186 180 LEU 187 181 GLN 188 182 PRO 189 183 PHE 190 184 ASN 191 185 HIS 192 186 TRP 193 187 ALA 194 188 PHE 195 189 ILE 196 190 PRO 197 191 VAL 198 192 ASN 199 193 LEU 200 194 ILE 201 195 LEU 202 196 GLU 203 197 GLY 204 198 VAL 205 199 SER 206 200 LEU 207 201 LEU 208 202 SER 209 203 LYS 210 204 PRO 211 205 VAL 212 206 SER 213 207 LEU 214 208 GLY 215 209 LEU 216 210 ARG 217 211 LEU 218 212 PHE 219 213 GLY 220 214 ASN 221 215 MET 222 216 TYR 223 217 ALA 224 218 GLY 225 219 GLU 226 220 LEU 227 221 ILE 228 222 PHE 229 223 ILE 230 224 LEU 231 225 ILE 232 226 ALA 233 227 GLY 234 228 LEU 235 229 LEU 236 230 PRO 237 231 TRP 238 232 TRP 239 233 SER 240 234 GLN 241 235 TRP 242 236 ILE 243 237 LEU 244 238 ASN 245 239 VAL 246 240 PRO 247 241 TRP 248 242 ALA 249 243 ILE 250 244 PHE 251 245 HIS 252 246 ILE 253 247 LEU 254 248 ILE 255 249 ILE 256 250 THR 257 251 LEU 258 252 GLN 259 253 ALA 260 254 PHE 261 255 ILE 262 256 PHE 263 257 MET 264 258 VAL 265 259 LEU 266 260 THR 267 261 ILE 268 262 VAL 269 263 TYR 270 264 LEU 271 265 SER 272 266 MET 273 267 ALA 274 268 SER 275 269 GLU 276 270 GLU 277 271 HIS stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-01-28 loop_ _Database_name _Database_accession_code _Database_entry_mol_name _Sequence_query_to_submitted_percentage _Sequence_subject_length _Sequence_identity _Sequence_positive _Sequence_homology_expectation_value PDB 1C17 "A1c12 Subcomplex Of F1fo Atp Synthase" 63.90 177 100.00 100.00 8.70e-117 DBJ BAB38103 "membrane-bound ATP synthase subunit a AtpB [Escherichia coli O157:H7 str. Sakai]" 97.47 271 99.63 99.63 0.00e+00 DBJ BAE77550 "F0 sector of membrane-bound ATP synthase, subunit a [Escherichia coli str. K-12 substr. W3110]" 97.47 271 100.00 100.00 0.00e+00 DBJ BAG79552 "ATP synthase subunit A [Escherichia coli SE11]" 97.47 271 100.00 100.00 0.00e+00 DBJ BAI27998 "F0 sector of membrane-bound ATP synthase, subunit a AtpB [Escherichia coli O26:H11 str. 11368]" 97.47 271 100.00 100.00 0.00e+00 DBJ BAI33121 "F0 sector of membrane-bound ATP synthase, subunit a AtpB [Escherichia coli O103:H2 str. 12009]" 97.47 271 100.00 100.00 0.00e+00 EMBL CAA23514 "unnamed protein product [Escherichia coli]" 97.47 271 100.00 100.00 0.00e+00 EMBL CAA23520 "atpB [Escherichia coli]" 97.47 271 100.00 100.00 0.00e+00 EMBL CAA23521 "atpB [Escherichia coli]" 72.56 201 99.50 100.00 4.46e-135 EMBL CAA23590 "unnamed protein product [Escherichia coli]" 97.47 271 98.52 98.52 0.00e+00 EMBL CAA25776 "unnamed protein product [Escherichia coli]" 97.47 271 100.00 100.00 0.00e+00 GB AAA24731 "ATP synthase a subunit [Escherichia coli]" 97.47 271 100.00 100.00 0.00e+00 GB AAA24740 "ATPase, a subunit (EC 3.6.1.3) [Escherichia coli]" 97.47 271 99.63 99.63 0.00e+00 GB AAA62090 "ATP synthase F0 subunit a [Escherichia coli]" 97.47 271 100.00 100.00 0.00e+00 GB AAA83869 "integral membrane proton channel F0 subunit A [Escherichia coli]" 97.47 271 100.00 100.00 0.00e+00 GB AAC76761 "F0 sector of membrane-bound ATP synthase, subunit a [Escherichia coli str. K-12 substr. MG1655]" 97.47 271 100.00 100.00 0.00e+00 REF NP_290377 "ATP synthase F0F1 subunit A [Escherichia coli O157:H7 str. EDL933]" 97.47 271 100.00 100.00 0.00e+00 REF NP_312707 "ATP synthase F0F1 subunit A [Escherichia coli O157:H7 str. Sakai]" 97.47 271 99.63 99.63 0.00e+00 REF NP_418194 "F0 sector of membrane-bound ATP synthase, subunit a [Escherichia coli str. K-12 substr. MG1655]" 97.47 271 100.00 100.00 0.00e+00 REF NP_709551 "ATP synthase F0F1 subunit A [Shigella flexneri 2a str. 301]" 97.47 271 99.63 100.00 0.00e+00 REF NP_756524 "F0F1 ATP synthase subunit A [Escherichia coli CFT073]" 97.47 271 99.63 99.63 0.00e+00 SP A1AHR8 "RecName: Full=ATP synthase subunit a; AltName: Full=ATP synthase F0 sector subunit a; AltName: Full=F-ATPase subunit 6 [Escheri" 97.47 271 99.63 99.63 0.00e+00 SP A7ZTV0 "RecName: Full=ATP synthase subunit a; AltName: Full=ATP synthase F0 sector subunit a; AltName: Full=F-ATPase subunit 6 [Escheri" 97.47 271 100.00 100.00 0.00e+00 SP A8A6K1 "RecName: Full=ATP synthase subunit a; AltName: Full=ATP synthase F0 sector subunit a; AltName: Full=F-ATPase subunit 6 [Escheri" 97.47 271 100.00 100.00 0.00e+00 SP B1IX00 "RecName: Full=ATP synthase subunit a; AltName: Full=ATP synthase F0 sector subunit a; AltName: Full=F-ATPase subunit 6 [Escheri" 97.47 271 100.00 100.00 0.00e+00 SP B1LL65 "RecName: Full=ATP synthase subunit a; AltName: Full=ATP synthase F0 sector subunit a; AltName: Full=F-ATPase subunit 6 [Escheri" 97.47 271 99.63 99.63 0.00e+00 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $subunit_a 'E. coli' 562 Eubacteria . Escherichia coli 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 $subunit_a 'recombinant technology' 'E. coli' . . . plasmid pBWU13 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 $subunit_a 0.3 mM '[U-13C; U-15N; non-exchangeable 90% 2H]' CD3COONa 25 mM . 'CHCl3:CD3OH:H2O (4:4:1)' 100 % . stop_ save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model DMX _Field_strength 750 _Details . save_ ############################# # NMR applied experiments # ############################# save_HNCO_1 _Saveframe_category NMR_applied_experiment _Experiment_name HNCO _Sample_label . save_ save_HNCA_2 _Saveframe_category NMR_applied_experiment _Experiment_name HNCA _Sample_label . save_ save_HN(CO)CACB_3 _Saveframe_category NMR_applied_experiment _Experiment_name HN(CO)CACB _Sample_label . save_ save_HN(CA)CB_4 _Saveframe_category NMR_applied_experiment _Experiment_name HN(CA)CB _Sample_label . save_ save_HNCOCA_5 _Saveframe_category NMR_applied_experiment _Experiment_name HNCOCA _Sample_label . save_ save_HNCACO_6 _Saveframe_category NMR_applied_experiment _Experiment_name HNCACO _Sample_label . save_ save_NMR_spec_expt__0_1 _Saveframe_category NMR_applied_experiment _Experiment_name HNCO _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_2 _Saveframe_category NMR_applied_experiment _Experiment_name HNCA _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_3 _Saveframe_category NMR_applied_experiment _Experiment_name HN(CO)CACB _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_4 _Saveframe_category NMR_applied_experiment _Experiment_name HN(CA)CB _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_5 _Saveframe_category NMR_applied_experiment _Experiment_name HNCOCA _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_6 _Saveframe_category NMR_applied_experiment _Experiment_name HNCACO _BMRB_pulse_sequence_accession_number . _Details . save_ ####################### # Sample conditions # ####################### save_conditions _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH* 5.5 0.2 n/a temperature 300 0.2 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_shift_set _Saveframe_category assigned_chemical_shifts _Details . loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $conditions _Chem_shift_reference_set_label $chemical_shift_reference _Mol_system_component_name 'sibunit a' _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 . 8 ALA H H 8.56 0.02 1 2 . 8 ALA N N 124.3 0.1 1 3 . 8 ALA CA C 52.9 0.1 1 4 . 8 ALA C C 177.7 0.1 1 5 . 8 ALA CB C 19.0 0.1 1 6 . 9 SER H H 8.23 0.02 1 7 . 9 SER N N 113.7 0.1 1 8 . 9 SER CA C 58.7 0.1 1 9 . 9 SER C C 174.9 0.1 1 10 . 9 SER CB C 64.3 0.1 1 11 . 10 GLU H H 8.42 0.02 1 12 . 10 GLU N N 118.7 0.1 1 13 . 10 GLU CA C 56.0 0.1 1 14 . 10 GLU C C 175.6 0.1 1 15 . 10 GLU CB C 28.4 0.1 1 16 . 11 ASN H H 8.32 0.02 1 17 . 11 ASN N N 116.0 0.1 1 18 . 11 ASN CA C 53.5 0.1 1 19 . 11 ASN C C 175.1 0.1 1 20 . 11 ASN CB C 39.0 0.1 1 21 . 12 MET H H 8.14 0.02 1 22 . 12 MET N N 118.9 0.1 1 23 . 12 MET CA C 55.4 0.1 1 24 . 12 MET C C 175.9 0.1 1 25 . 12 MET CB C 33.0 0.1 1 26 . 13 THR H H 7.80 0.02 1 27 . 13 THR N N 111.7 0.1 1 28 . 13 THR CA C 60.4 0.1 1 29 . 13 THR C C 174.4 0.1 1 30 . 13 THR CB C 69.0 0.1 1 31 . 14 PRO CA C 65.7 0.1 1 32 . 14 PRO C C 178.3 0.1 1 33 . 14 PRO CB C 31.5 0.1 1 34 . 15 GLN H H 8.96 0.02 1 35 . 15 GLN N N 115.6 0.1 1 36 . 15 GLN CA C 59.6 0.1 1 37 . 15 GLN C C 178.2 0.1 1 38 . 15 GLN CB C 27.6 0.1 1 39 . 16 ASP H H 8.01 0.02 1 40 . 16 ASP N N 118.3 0.1 1 41 . 16 ASP CA C 55.4 0.1 1 42 . 16 ASP C C 177.3 0.1 1 43 . 16 ASP CB C 37.8 0.1 1 44 . 17 TYR H H 8.16 0.02 1 45 . 17 TYR N N 120.7 0.1 1 46 . 17 TYR CA C 61.9 0.1 1 47 . 17 TYR C C 178.8 0.1 1 48 . 17 TYR CB C 38.6 0.1 1 49 . 18 ILE H H 8.56 0.02 1 50 . 18 ILE N N 120.2 0.1 1 51 . 18 ILE CA C 64.8 0.1 1 52 . 18 ILE C C 178.6 0.1 1 53 . 18 ILE CB C 37.7 0.1 1 54 . 19 GLY H H 8.46 0.02 1 55 . 19 GLY N N 106.9 0.1 1 56 . 19 GLY CA C 47.4 0.1 1 57 . 19 GLY C C 175.8 0.1 1 58 . 20 HIS H H 8.23 0.02 1 59 . 20 HIS N N 117.1 0.1 1 60 . 20 HIS CA C 58.4 0.1 1 61 . 20 HIS C C 176.6 0.1 1 62 . 20 HIS CB C 28.2 0.1 1 63 . 21 HIS H H 8.28 0.02 1 64 . 21 HIS N N 115.4 0.1 1 65 . 21 HIS CA C 58.8 0.1 1 66 . 21 HIS C C 176.6 0.1 1 67 . 21 HIS CB C 28.2 0.1 1 68 . 22 LEU H H 8.51 0.02 1 69 . 22 LEU N N 119.8 0.1 1 70 . 22 LEU CA C 57.7 0.1 1 71 . 22 LEU C C 178.9 0.1 1 72 . 22 LEU CB C 41.2 0.1 1 73 . 23 ASN H H 8.26 0.02 1 74 . 23 ASN N N 117.4 0.1 1 75 . 23 ASN CA C 55.9 0.1 1 76 . 23 ASN C C 177.3 0.1 1 77 . 23 ASN CB C 38.6 0.1 1 78 . 24 ASN H H 8.03 0.02 1 79 . 24 ASN N N 118.1 0.1 1 80 . 24 ASN CA C 55.9 0.1 1 81 . 24 ASN C C 177.3 0.1 1 82 . 24 ASN CB C 38.2 0.1 1 83 . 25 LEU H H 8.01 0.02 1 84 . 25 LEU N N 120.4 0.1 1 85 . 25 LEU CA C 58.3 0.1 1 86 . 25 LEU C C 179.0 0.1 1 87 . 25 LEU CB C 41.3 0.1 1 88 . 26 GLN H H 8.13 0.02 1 89 . 26 GLN N N 117.0 0.1 1 90 . 26 GLN CA C 59.7 0.1 1 91 . 26 GLN C C 178.8 0.1 1 92 . 26 GLN CB C 28.0 0.1 1 93 . 27 LEU H H 8.03 0.02 1 94 . 27 LEU N N 119.6 0.1 1 95 . 27 LEU CA C 58.2 0.1 1 96 . 27 LEU C C 180.3 0.1 1 97 . 27 LEU CB C 41.0 0.1 1 98 . 28 ASP H H 8.52 0.02 1 99 . 28 ASP N N 120.6 0.1 1 100 . 28 ASP CA C 56.5 0.1 1 101 . 28 ASP C C 177.5 0.1 1 102 . 28 ASP CB C 37.1 0.1 1 103 . 29 LEU H H 8.46 0.02 1 104 . 29 LEU N N 119.7 0.1 1 105 . 29 LEU CA C 58.3 0.1 1 106 . 29 LEU C C 180.0 0.1 1 107 . 29 LEU CB C 41.3 0.1 1 108 . 30 ARG H H 8.30 0.02 1 109 . 30 ARG N N 118.3 0.1 1 110 . 30 ARG CA C 59.2 0.1 1 111 . 30 ARG C C 179.1 0.1 1 112 . 30 ARG CB C 29.7 0.1 1 113 . 31 THR H H 8.17 0.02 1 114 . 31 THR N N 115.2 0.1 1 115 . 31 THR CA C 67.1 0.1 1 116 . 31 THR C C 176.2 0.1 1 117 . 31 THR CB C 68.5 0.1 1 118 . 32 PHE H H 8.33 0.02 1 119 . 32 PHE N N 119.8 0.1 1 120 . 32 PHE CA C 60.7 0.1 1 121 . 32 PHE C C 177.5 0.1 1 122 . 32 PHE CB C 38.7 0.1 1 123 . 33 SER H H 7.94 0.02 1 124 . 33 SER N N 112.2 0.1 1 125 . 33 SER CA C 61.4 0.1 1 126 . 33 SER C C 174.8 0.1 1 127 . 33 SER CB C 64.0 0.1 1 128 . 34 LEU H H 7.49 0.02 1 129 . 34 LEU N N 119.2 0.1 1 130 . 34 LEU CA C 56.6 0.1 1 131 . 34 LEU C C 178.0 0.1 1 132 . 34 LEU CB C 42.2 0.1 1 133 . 35 VAL H H 7.45 0.02 1 134 . 35 VAL N N 111.7 0.1 1 135 . 35 VAL CA C 62.2 0.1 1 136 . 35 VAL C C 175.5 0.1 1 137 . 35 VAL CB C 32.0 0.1 1 138 . 36 ASP H H 7.69 0.02 1 139 . 36 ASP N N 117.8 0.1 1 140 . 36 ASP CA C 50.8 0.1 1 141 . 36 ASP C C 173.9 0.1 1 142 . 36 ASP CB C 38.1 0.1 1 143 . 37 PRO CA C 64.0 0.1 1 144 . 37 PRO C C 176.7 0.1 1 145 . 37 PRO CB C 31.5 0.1 1 146 . 38 GLN H H 7.86 0.02 1 147 . 38 GLN N N 115.8 0.1 1 148 . 38 GLN CA C 55.8 0.1 1 149 . 38 GLN C C 175.6 0.1 1 150 . 38 GLN CB C 28.9 0.1 1 151 . 39 ASN H H 8.01 0.02 1 152 . 39 ASN N N 116.9 0.1 1 153 . 39 ASN CA C 52.2 0.1 1 154 . 39 ASN C C 174.0 0.1 1 155 . 39 ASN CB C 38.5 0.1 1 156 . 41 PRO CA C 66.2 0.1 1 157 . 41 PRO C C 178.2 0.1 1 158 . 41 PRO CB C 30.1 0.1 1 159 . 42 ALA H H 8.00 0.02 1 160 . 42 ALA N N 118.5 0.1 1 161 . 42 ALA CA C 55.3 0.1 1 162 . 42 ALA C C 179.7 0.1 1 163 . 42 ALA CB C 18.4 0.1 1 164 . 43 THR H H 8.23 0.02 1 165 . 43 THR N N 114.0 0.1 1 166 . 43 THR CA C 58.6 0.1 1 167 . 43 THR C C 175.1 0.1 1 168 . 43 THR CB C 64.3 0.1 1 169 . 44 PHE H H 8.39 0.02 1 170 . 44 PHE N N 120.0 0.1 1 171 . 44 PHE CA C 58.5 0.1 1 172 . 44 PHE C C 179.4 0.1 1 173 . 44 PHE CB C 38.9 0.1 1 174 . 45 TRP H H 8.51 0.02 1 175 . 45 TRP N N 118.0 0.1 1 176 . 45 TRP CA C 61.1 0.1 1 177 . 45 TRP C C 178.1 0.1 1 178 . 45 TRP CB C 29.7 0.1 1 179 . 46 THR H H 8.15 0.02 1 180 . 46 THR N N 114.8 0.1 1 181 . 46 THR CA C 67.6 0.1 1 182 . 46 THR C C 176.2 0.1 1 183 . 46 THR CB C 68.7 0.1 1 184 . 47 ILE H H 8.20 0.02 1 185 . 47 ILE N N 119.7 0.1 1 186 . 47 ILE CA C 65.2 0.1 1 187 . 47 ILE C C 179.1 0.1 1 188 . 47 ILE CB C 37.3 0.1 1 189 . 48 ASN H H 7.79 0.02 1 190 . 48 ASN N N 119.5 0.1 1 191 . 48 ASN CA C 57.6 0.1 1 192 . 48 ASN C C 177.5 0.1 1 193 . 48 ASN CB C 39.1 0.1 1 194 . 49 ILE H H 8.49 0.02 1 195 . 49 ILE N N 120.3 0.1 1 196 . 49 ILE CA C 64.7 0.1 1 197 . 49 ILE C C 178.4 0.1 1 198 . 49 ILE CB C 36.8 0.1 1 199 . 50 ASP H H 8.61 0.02 1 200 . 50 ASP N N 118.7 0.1 1 201 . 50 ASP CA C 56.5 0.1 1 202 . 50 ASP C C 178.0 0.1 1 203 . 50 ASP CB C 36.9 0.1 1 204 . 51 SER H H 8.30 0.02 1 205 . 51 SER N N 114.9 0.1 1 206 . 51 SER CA C 62.8 0.1 1 207 . 51 SER C C 177.2 0.1 1 208 . 51 SER CB C 63.7 0.1 1 209 . 52 MET H H 8.13 0.02 1 210 . 52 MET N N 122.9 0.1 1 211 . 52 MET CA C 59.3 0.1 1 212 . 52 MET C C 178.2 0.1 1 213 . 52 MET CB C 32.2 0.1 1 214 . 53 PHE H H 8.50 0.02 1 215 . 53 PHE N N 119.3 0.1 1 216 . 53 PHE CA C 61.8 0.1 1 217 . 53 PHE C C 177.7 0.1 1 218 . 53 PHE CB C 38.9 0.1 1 219 . 54 PHE H H 8.63 0.02 1 220 . 54 PHE N N 116.8 0.1 1 221 . 54 PHE CA C 61.3 0.1 1 222 . 54 PHE C C 177.8 0.1 1 223 . 54 PHE CB C 38.8 0.1 1 224 . 55 SER H H 8.10 0.02 1 225 . 55 SER N N 113.7 0.1 1 226 . 55 SER CA C 63.1 0.1 1 227 . 55 SER C C 176.6 0.1 1 228 . 55 SER CB C 63.6 0.1 1 229 . 56 VAL H H 7.87 0.02 1 230 . 56 VAL N N 122.5 0.1 1 231 . 56 VAL CA C 66.5 0.1 1 232 . 56 VAL C C 178.0 0.1 1 233 . 56 VAL CB C 31.3 0.1 1 234 . 57 VAL H H 7.85 0.02 1 235 . 57 VAL N N 118.9 0.1 1 236 . 57 VAL CA C 67.2 0.1 1 237 . 57 VAL C C 178.1 0.1 1 238 . 57 VAL CB C 31.0 0.1 1 239 . 58 LEU H H 8.25 0.02 1 240 . 58 LEU N N 118.0 0.1 1 241 . 58 LEU CA C 58.0 0.1 1 242 . 58 LEU C C 179.4 0.1 1 243 . 58 LEU CB C 41.0 0.1 1 244 . 59 GLY H H 8.08 0.02 1 245 . 59 GLY N N 105.4 0.1 1 246 . 59 GLY CA C 47.8 0.1 1 247 . 59 GLY C C 176.1 0.1 1 248 . 60 LEU H H 8.30 0.02 1 249 . 60 LEU N N 121.6 0.1 1 250 . 60 LEU CA C 58.2 0.1 1 251 . 60 LEU C C 179.2 0.1 1 252 . 60 LEU CB C 41.4 0.1 1 253 . 61 LEU H H 8.13 0.02 1 254 . 61 LEU N N 117.0 0.1 1 255 . 61 LEU CA C 56.9 0.1 1 256 . 61 LEU C C 178.3 0.1 1 257 . 61 LEU CB C 41.7 0.1 1 258 . 62 PHE H H 7.68 0.02 1 259 . 62 PHE N N 114.0 0.1 1 260 . 62 PHE CA C 55.1 0.1 1 261 . 62 PHE C C 177.0 0.1 1 262 . 62 PHE CB C 41.6 0.1 1 263 . 63 LEU H H 8.01 0.02 1 264 . 63 LEU N N 120.4 0.1 1 265 . 63 LEU CA C 58.3 0.1 1 266 . 63 LEU C C 179.0 0.1 1 267 . 63 LEU CB C 41.3 0.1 1 268 . 64 VAL H H 8.15 0.02 1 269 . 64 VAL N N 121.3 0.1 1 270 . 64 VAL CA C 66.9 0.1 1 271 . 64 VAL C C 179.7 0.1 1 272 . 64 VAL CB C 31.3 0.1 1 273 . 65 LEU H H 8.47 0.02 1 274 . 65 LEU N N 122.6 0.1 1 275 . 65 LEU CA C 58.6 0.1 1 276 . 65 LEU C C 179.2 0.1 1 277 . 65 LEU CB C 41.0 0.1 1 278 . 66 PHE H H 8.99 0.02 1 279 . 66 PHE N N 119.4 0.1 1 280 . 66 PHE CA C 61.5 0.1 1 281 . 66 PHE C C 178.2 0.1 1 282 . 66 PHE CB C 38.7 0.1 1 283 . 67 ARG H H 8.55 0.02 1 284 . 67 ARG N N 117.2 0.1 1 285 . 67 ARG CA C 59.6 0.1 1 286 . 67 ARG C C 178.8 0.1 1 287 . 67 ARG CB C 29.6 0.1 1 288 . 68 SER H H 8.11 0.02 1 289 . 68 SER N N 114.6 0.1 1 290 . 68 SER CA C 62.6 0.1 1 291 . 68 SER C C 176.8 0.1 1 292 . 68 SER CB C 63.6 0.1 1 293 . 69 VAL H H 8.22 0.02 1 294 . 69 VAL N N 122.3 0.1 1 295 . 69 VAL CA C 66.6 0.1 1 296 . 69 VAL C C 178.1 0.1 1 297 . 69 VAL CB C 31.3 0.1 1 298 . 70 ALA H H 8.32 0.02 1 299 . 70 ALA N N 121.3 0.1 1 300 . 70 ALA CA C 55.3 0.1 1 301 . 70 ALA C C 180.8 0.1 1 302 . 70 ALA CB C 17.9 0.1 1 303 . 71 LYS H H 8.21 0.02 1 304 . 71 LYS N N 117.7 0.1 1 305 . 71 LYS CA C 59.1 0.1 1 306 . 71 LYS C C 179.3 0.1 1 307 . 71 LYS CB C 31.9 0.1 1 308 . 72 LYS H H 7.95 0.02 1 309 . 72 LYS N N 119.6 0.1 1 310 . 72 LYS CA C 59.1 0.1 1 311 . 72 LYS C C 179.4 0.1 1 312 . 72 LYS CB C 31.8 0.1 1 313 . 73 ALA H H 8.59 0.02 1 314 . 73 ALA N N 120.2 0.1 1 315 . 73 ALA CA C 54.8 0.1 1 316 . 73 ALA C C 179.4 0.1 1 317 . 73 ALA CB C 18.6 0.1 1 318 . 74 THR H H 7.76 0.02 1 319 . 74 THR N N 106.6 0.1 1 320 . 74 THR CA C 63.5 0.1 1 321 . 74 THR C C 175.9 0.1 1 322 . 74 THR CB C 69.6 0.1 1 323 . 75 SER H H 7.72 0.02 1 324 . 75 SER N N 115.1 0.1 1 325 . 75 SER CA C 60.3 0.1 1 326 . 75 SER C C 175.3 0.1 1 327 . 75 SER CB C 64.3 0.1 1 328 . 76 GLY H H 8.08 0.02 1 329 . 76 GLY N N 108.1 0.1 1 330 . 76 GLY CA C 45.5 0.1 1 331 . 76 GLY C C 174.4 0.1 1 332 . 77 VAL H H 8.13 0.02 1 333 . 77 VAL N N 119.9 0.1 1 334 . 77 VAL CA C 65.2 0.1 1 335 . 77 VAL CB C 30.5 0.1 1 336 . 78 PRO CA C 65.6 0.1 1 337 . 78 PRO C C 178.4 0.1 1 338 . 78 PRO CB C 30.9 0.1 1 339 . 79 GLY H H 8.24 0.02 1 340 . 79 GLY N N 105.3 0.1 1 341 . 79 GLY CA C 46.7 0.1 1 342 . 79 GLY C C 176.9 0.1 1 343 . 80 LYS H H 8.23 0.02 1 344 . 80 LYS N N 122.5 0.1 1 345 . 80 LYS CA C 59.7 0.1 1 346 . 80 LYS C C 178.7 0.1 1 347 . 80 LYS CB C 32.1 0.1 1 348 . 81 PHE H H 8.42 0.02 1 349 . 81 PHE N N 119.2 0.1 1 350 . 81 PHE CA C 61.2 0.1 1 351 . 81 PHE C C 177.5 0.1 1 352 . 81 PHE CB C 39.0 0.1 1 353 . 82 GLN H H 8.48 0.02 1 354 . 82 GLN N N 117.3 0.1 1 355 . 82 GLN CA C 59.7 0.1 1 356 . 82 GLN C C 178.5 0.1 1 357 . 82 GLN CB C 28.3 0.1 1 358 . 83 THR H H 7.98 0.02 1 359 . 83 THR N N 114.1 0.1 1 360 . 83 THR CA C 67.1 0.1 1 361 . 83 THR C C 175.7 0.1 1 362 . 83 THR CB C 68.6 0.1 1 363 . 84 ALA H H 7.90 0.02 1 364 . 84 ALA N N 122.6 0.1 1 365 . 84 ALA CA C 55.9 0.1 1 366 . 84 ALA C C 179.4 0.1 1 367 . 84 ALA CB C 18.3 0.1 1 368 . 85 ILE H H 7.96 0.02 1 369 . 85 ILE N N 115.7 0.1 1 370 . 85 ILE CA C 64.4 0.1 1 371 . 85 ILE C C 178.3 0.1 1 372 . 85 ILE CB C 37.0 0.1 1 373 . 86 GLU H H 7.98 0.02 1 374 . 86 GLU N N 117.6 0.1 1 375 . 86 GLU CA C 59.6 0.1 1 376 . 86 GLU C C 179.2 0.1 1 377 . 86 GLU CB C 27.6 0.1 1 378 . 87 LEU H H 8.24 0.02 1 379 . 87 LEU N N 119.5 0.1 1 380 . 87 LEU CA C 58.3 0.1 1 381 . 87 LEU C C 179.5 0.1 1 382 . 87 LEU CB C 41.3 0.1 1 383 . 88 VAL H H 8.07 0.02 1 384 . 88 VAL N N 119.5 0.1 1 385 . 88 VAL CA C 67.4 0.1 1 386 . 88 VAL C C 176.3 0.1 1 387 . 88 VAL CB C 31.2 0.1 1 388 . 89 ILE H H 7.99 0.02 1 389 . 89 ILE N N 119.9 0.1 1 390 . 89 ILE CA C 65.5 0.1 1 391 . 89 ILE C C 179.4 0.1 1 392 . 89 ILE CB C 37.3 0.1 1 393 . 90 GLY H H 8.52 0.02 1 394 . 90 GLY N N 106.8 0.1 1 395 . 90 GLY CA C 47.6 0.1 1 396 . 90 GLY C C 176.8 0.1 1 397 . 91 PHE H H 8.63 0.02 1 398 . 91 PHE N N 123.6 0.1 1 399 . 91 PHE CA C 61.5 0.1 1 400 . 91 PHE C C 179.2 0.1 1 401 . 91 PHE CB C 39.4 0.1 1 402 . 92 VAL H H 8.96 0.02 1 403 . 92 VAL N N 122.2 0.1 1 404 . 92 VAL CA C 67.3 0.1 1 405 . 92 VAL C C 178.1 0.1 1 406 . 92 VAL CB C 31.4 0.1 1 407 . 93 ASN H H 8.72 0.02 1 408 . 93 ASN N N 117.1 0.1 1 409 . 93 ASN CA C 57.1 0.1 1 410 . 93 ASN C C 178.2 0.1 1 411 . 93 ASN CB C 39.2 0.1 1 412 . 94 GLY H H 8.43 0.02 1 413 . 94 GLY N N 105.3 0.1 1 414 . 94 GLY CA C 47.3 0.1 1 415 . 94 GLY C C 175.8 0.1 1 416 . 95 SER H H 8.10 0.02 1 417 . 95 SER N N 117.9 0.1 1 418 . 95 SER CA C 62.8 0.1 1 419 . 95 SER C C 176.8 0.1 1 420 . 95 SER CB C 63.6 0.1 1 421 . 96 VAL H H 8.15 0.02 1 422 . 96 VAL N N 121.7 0.1 1 423 . 96 VAL CA C 66.7 0.1 1 424 . 96 VAL C C 178.5 0.1 1 425 . 96 VAL CB C 31.4 0.1 1 426 . 97 LYS H H 7.99 0.02 1 427 . 97 LYS N N 118.5 0.1 1 428 . 97 LYS CA C 60.0 0.1 1 429 . 97 LYS C C 179.2 0.1 1 430 . 97 LYS CB C 31.7 0.1 1 431 . 98 ASP H H 8.27 0.02 1 432 . 98 ASP N N 117.1 0.1 1 433 . 98 ASP CA C 55.9 0.1 1 434 . 98 ASP C C 177.9 0.1 1 435 . 98 ASP CB C 37.3 0.1 1 436 . 99 MET H H 8.21 0.02 1 437 . 99 MET N N 119.2 0.1 1 438 . 99 MET CA C 58.5 0.1 1 439 . 99 MET C C 178.1 0.1 1 440 . 99 MET CB C 31.0 0.1 1 441 . 100 TYR H H 8.25 0.02 1 442 . 100 TYR N N 118.0 0.1 1 443 . 100 TYR CA C 60.8 0.1 1 444 . 100 TYR C C 177.9 0.1 1 445 . 100 TYR CB C 38.2 0.1 1 446 . 101 HIS H H 8.40 0.02 1 447 . 101 HIS N N 117.1 0.1 1 448 . 101 HIS CA C 57.5 0.1 1 449 . 101 HIS C C 176.6 0.1 1 450 . 101 HIS CB C 28.3 0.1 1 451 . 102 GLY H H 8.43 0.02 1 452 . 102 GLY N N 107.7 0.1 1 453 . 102 GLY CA C 47.0 0.1 1 454 . 102 GLY C C 175.4 0.1 1 455 . 103 LYS H H 8.23 0.02 1 456 . 103 LYS N N 119.6 0.1 1 457 . 103 LYS CA C 58.8 0.1 1 458 . 103 LYS C C 178.3 0.1 1 459 . 103 LYS CB C 32.1 0.1 1 460 . 104 SER H H 8.10 0.02 1 461 . 104 SER N N 113.8 0.1 1 462 . 104 SER CA C 61.5 0.1 1 463 . 104 SER C C 176.1 0.1 1 464 . 104 SER CB C 63.1 0.1 1 465 . 105 LYS H H 7.77 0.02 1 466 . 105 LYS N N 119.6 0.1 1 467 . 105 LYS CA C 58.4 0.1 1 468 . 105 LYS C C 177.5 0.1 1 469 . 105 LYS CB C 31.9 0.1 1 470 . 106 LEU H H 7.60 0.02 1 471 . 106 LEU N N 116.2 0.1 1 472 . 106 LEU CA C 56.4 0.1 1 473 . 106 LEU C C 177.8 0.1 1 474 . 106 LEU CB C 42.0 0.1 1 475 . 107 ILE H H 7.47 0.02 1 476 . 107 ILE N N 113.8 0.1 1 477 . 107 ILE CA C 62.4 0.1 1 478 . 107 ILE C C 177.2 0.1 1 479 . 107 ILE CB C 38.3 0.1 1 480 . 108 ALA H H 8.02 0.02 1 481 . 108 ALA N N 122.2 0.1 1 482 . 108 ALA CA C 56.6 0.1 1 483 . 108 ALA C C 176.1 0.1 1 484 . 108 ALA CB C 16.4 0.1 1 485 . 109 PRO CA C 66.1 0.1 1 486 . 109 PRO C C 179.3 0.1 1 487 . 109 PRO CB C 30.8 0.1 1 488 . 110 LEU H H 7.48 0.02 1 489 . 110 LEU N N 118.6 0.1 1 490 . 110 LEU CA C 58.1 0.1 1 491 . 110 LEU C C 178.3 0.1 1 492 . 110 LEU CB C 41.3 0.1 1 493 . 111 ALA H H 8.28 0.02 1 494 . 111 ALA N N 120.7 0.1 1 495 . 111 ALA CA C 55.5 0.1 1 496 . 111 ALA C C 179.7 0.1 1 497 . 111 ALA CB C 18.3 0.1 1 498 . 112 LEU H H 8.26 0.02 1 499 . 112 LEU N N 116.1 0.1 1 500 . 112 LEU CA C 58.0 0.1 1 501 . 112 LEU C C 178.4 0.1 1 502 . 112 LEU CB C 41.5 0.1 1 503 . 113 THR H H 7.68 0.02 1 504 . 113 THR N N 114.0 0.1 1 505 . 113 THR CA C 67.7 0.1 1 506 . 113 THR C C 176.3 0.1 1 507 . 113 THR CB C 68.7 0.1 1 508 . 114 ILE H H 8.44 0.02 1 509 . 114 ILE N N 120.8 0.1 1 510 . 114 ILE CA C 61.5 0.1 1 511 . 114 ILE C C 178.5 0.1 1 512 . 115 PHE H H 8.88 0.02 1 513 . 115 PHE N N 118.9 0.1 1 514 . 115 PHE CA C 62.3 0.1 1 515 . 115 PHE C C 178.3 0.1 1 516 . 115 PHE CB C 38.3 0.1 1 517 . 116 VAL H H 8.63 0.02 1 518 . 116 VAL N N 115.5 0.1 1 519 . 116 VAL CA C 61.0 0.1 1 520 . 116 VAL C C 175.5 0.1 1 521 . 117 TRP H H 7.61 0.02 1 522 . 117 TRP N N 118.0 0.1 1 523 . 117 TRP CA C 56.8 0.1 1 524 . 117 TRP C C 178.0 0.1 1 525 . 118 VAL H H 7.57 0.02 1 526 . 118 VAL N N 110.5 0.1 1 527 . 118 VAL CA C 62.2 0.1 1 528 . 118 VAL C C 175.6 0.1 1 529 . 118 VAL CB C 32.0 0.1 1 530 . 120 LEU CA C 59.0 0.1 1 531 . 120 LEU C C 175.0 0.1 1 532 . 121 MET H H 8.35 0.02 1 533 . 121 MET N N 118.7 0.1 1 534 . 121 MET CA C 56.2 0.1 1 535 . 121 MET C C 175.7 0.1 1 536 . 121 MET CB C 28.3 0.1 1 537 . 122 ASN H H 8.16 0.02 1 538 . 122 ASN N N 117.1 0.1 1 539 . 122 ASN CA C 56.0 0.1 1 540 . 122 ASN C C 177.3 0.1 1 541 . 122 ASN CB C 39.1 0.1 1 542 . 123 LEU H H 8.03 0.02 1 543 . 123 LEU N N 118.1 0.1 1 544 . 123 LEU CA C 55.9 0.1 1 545 . 123 LEU C C 177.3 0.1 1 546 . 123 LEU CB C 41.6 0.1 1 547 . 124 MET H H 8.14 0.02 1 548 . 124 MET N N 116.9 0.1 1 549 . 124 MET CA C 56.0 0.1 1 550 . 124 MET C C 175.6 0.1 1 551 . 124 MET CB C 28.4 0.1 1 552 . 125 ASP H H 8.20 0.02 1 553 . 125 ASP N N 117.2 0.1 1 554 . 125 ASP CA C 53.5 0.1 1 555 . 125 ASP C C 175.0 0.1 1 556 . 125 ASP CB C 39.0 0.1 1 557 . 126 LEU H H 8.26 0.02 1 558 . 126 LEU N N 117.6 0.1 1 559 . 126 LEU CA C 56.0 0.1 1 560 . 126 LEU C C 177.3 0.1 1 561 . 126 LEU CB C 41.1 0.1 1 562 . 127 LEU H H 8.13 0.02 1 563 . 127 LEU N N 117.0 0.1 1 564 . 127 LEU CA C 56.9 0.1 1 565 . 127 LEU C C 178.8 0.1 1 566 . 127 LEU CB C 41.5 0.1 1 567 . 128 PRO CA C 66.0 0.1 1 568 . 128 PRO C C 178.1 0.1 1 569 . 128 PRO CB C 31.3 0.1 1 570 . 129 ILE H H 7.35 0.02 1 571 . 129 ILE N N 114.0 0.1 1 572 . 129 ILE CA C 63.6 0.1 1 573 . 129 ILE C C 177.4 0.1 1 574 . 129 ILE CB C 37.6 0.1 1 575 . 130 ASP H H 8.03 0.02 1 576 . 130 ASP N N 116.4 0.1 1 577 . 130 ASP CA C 55.0 0.1 1 578 . 130 ASP C C 176.7 0.1 1 579 . 130 ASP CB C 38.3 0.1 1 580 . 131 LEU H H 7.95 0.02 1 581 . 131 LEU N N 117.0 0.1 1 582 . 131 LEU CA C 56.5 0.1 1 583 . 131 LEU C C 178.7 0.1 1 584 . 131 LEU CB C 42.5 0.1 1 585 . 132 LEU H H 7.98 0.02 1 586 . 132 LEU N N 118.7 0.1 1 587 . 132 LEU CA C 59.0 0.1 1 588 . 132 LEU C C 179.0 0.1 1 589 . 132 LEU CB C 38.8 0.1 1 590 . 133 PRO CA C 66.4 0.1 1 591 . 133 PRO C C 178.2 0.1 1 592 . 133 PRO CB C 30.6 0.1 1 593 . 134 TYR H H 7.28 0.02 1 594 . 134 TYR N N 115.7 0.1 1 595 . 134 TYR CA C 61.6 0.1 1 596 . 134 TYR C C 179.5 0.1 1 597 . 134 TYR CB C 38.4 0.1 1 598 . 135 ILE H H 8.47 0.02 1 599 . 135 ILE N N 121.7 0.1 1 600 . 135 ILE CA C 65.6 0.1 1 601 . 135 ILE C C 178.8 0.1 1 602 . 135 ILE CB C 37.6 0.1 1 603 . 136 ALA H H 8.79 0.02 1 604 . 136 ALA N N 121.3 0.1 1 605 . 136 ALA CA C 55.7 0.1 1 606 . 136 ALA C C 179.7 0.1 1 607 . 136 ALA CB C 18.5 0.1 1 608 . 137 GLU H H 8.19 0.02 1 609 . 137 GLU N N 113.8 0.1 1 610 . 137 GLU CA C 58.8 0.1 1 611 . 137 GLU C C 178.2 0.1 1 612 . 137 GLU CB C 27.5 0.1 1 613 . 138 HIS H H 7.73 0.02 1 614 . 138 HIS N N 113.5 0.1 1 615 . 138 HIS CA C 59.2 0.1 1 616 . 138 HIS C C 176.1 0.1 1 617 . 138 HIS CB C 28.5 0.1 1 618 . 139 VAL H H 8.20 0.02 1 619 . 139 VAL N N 117.9 0.1 1 620 . 139 VAL CA C 65.4 0.1 1 621 . 139 VAL C C 177.2 0.1 1 622 . 139 VAL CB C 38.8 0.1 1 623 . 140 LEU H H 8.00 0.02 1 624 . 140 LEU N N 116.5 0.1 1 625 . 140 LEU CA C 56.3 0.1 1 626 . 140 LEU C C 178.0 0.1 1 627 . 140 LEU CB C 41.8 0.1 1 628 . 141 GLY H H 7.57 0.02 1 629 . 141 GLY N N 103.2 0.1 1 630 . 141 GLY CA C 45.9 0.1 1 631 . 141 GLY C C 174.6 0.1 1 632 . 142 LEU H H 7.69 0.02 1 633 . 142 LEU N N 119.9 0.1 1 634 . 142 LEU CA C 57.2 0.1 1 635 . 142 LEU C C 176.5 0.1 1 636 . 142 LEU CB C 40.1 0.1 1 637 . 143 PRO CA C 65.6 0.1 1 638 . 143 PRO C C 178.0 0.1 1 639 . 143 PRO CB C 30.9 0.1 1 640 . 144 ALA H H 7.79 0.02 1 641 . 144 ALA N N 117.7 0.1 1 642 . 144 ALA CA C 54.3 0.1 1 643 . 144 ALA C C 178.9 0.1 1 644 . 144 ALA CB C 18.5 0.1 1 645 . 145 LEU H H 7.82 0.02 1 646 . 145 LEU N N 115.9 0.1 1 647 . 145 LEU CA C 56.6 0.1 1 648 . 145 LEU C C 178.0 0.1 1 649 . 145 LEU CB C 41.5 0.1 1 650 . 146 ARG H H 7.70 0.02 1 651 . 146 ARG N N 114.9 0.1 1 652 . 146 ARG CA C 56.9 0.1 1 653 . 146 ARG C C 177.3 0.1 1 654 . 146 ARG CB C 30.4 0.1 1 655 . 147 VAL H H 7.70 0.02 1 656 . 147 VAL N N 116.3 0.1 1 657 . 147 VAL CA C 63.8 0.1 1 658 . 147 VAL C C 176.4 0.1 1 659 . 147 VAL CB C 32.4 0.1 1 660 . 148 VAL H H 7.95 0.02 1 661 . 148 VAL N N 119.8 0.1 1 662 . 148 VAL CA C 65.3 0.1 1 663 . 148 VAL CB C 32.5 0.1 1 664 . 149 PRO CA C 65.5 0.1 1 665 . 149 PRO C C 178.2 0.1 1 666 . 149 PRO CB C 31.0 0.1 1 667 . 150 SER H H 7.70 0.02 1 668 . 150 SER N N 111.7 0.1 1 669 . 150 SER CA C 61.4 0.1 1 670 . 150 SER C C 176.3 0.1 1 671 . 150 SER CB C 63.2 0.1 1 672 . 151 ALA H H 8.35 0.02 1 673 . 151 ALA N N 124.7 0.1 1 674 . 151 ALA CA C 55.1 0.1 1 675 . 151 ALA C C 179.2 0.1 1 676 . 151 ALA CB C 18.0 0.1 1 677 . 152 ASP H H 8.33 0.02 1 678 . 152 ASP N N 115.3 0.1 1 679 . 152 ASP CA C 56.0 0.1 1 680 . 152 ASP C C 178.7 0.1 1 681 . 152 ASP CB C 37.5 0.1 1 682 . 153 VAL H H 8.15 0.02 1 683 . 153 VAL N N 121.4 0.1 1 684 . 153 VAL CA C 66.7 0.1 1 685 . 153 VAL C C 177.2 0.1 1 686 . 153 VAL CB C 31.6 0.1 1 687 . 154 ASN H H 8.10 0.02 1 688 . 154 ASN N N 117.7 0.1 1 689 . 154 ASN CA C 57.0 0.1 1 690 . 154 ASN C C 179.0 0.1 1 691 . 154 ASN CB C 38.6 0.1 1 692 . 155 VAL H H 8.58 0.02 1 693 . 155 VAL N N 120.4 0.1 1 694 . 155 VAL CA C 66.9 0.1 1 695 . 155 VAL C C 177.9 0.1 1 696 . 155 VAL CB C 31.6 0.1 1 697 . 156 THR H H 7.87 0.02 1 698 . 156 THR N N 116.3 0.1 1 699 . 156 THR CA C 67.8 0.1 1 700 . 156 THR C C 176.5 0.1 1 701 . 156 THR CB C 68.5 0.1 1 702 . 157 LEU H H 8.27 0.02 1 703 . 157 LEU N N 121.7 0.1 1 704 . 157 LEU CA C 58.3 0.1 1 705 . 157 LEU C C 179.2 0.1 1 706 . 157 LEU CB C 41.4 0.1 1 707 . 158 SER H H 8.03 0.02 1 708 . 158 SER N N 114.0 0.1 1 709 . 158 SER CA C 63.0 0.1 1 710 . 158 SER C C 177.0 0.1 1 711 . 158 SER CB C 63.6 0.1 1 712 . 159 MET H H 8.26 0.02 1 713 . 159 MET N N 121.0 0.1 1 714 . 159 MET CA C 59.0 0.1 1 715 . 159 MET C C 178.2 0.1 1 716 . 159 MET CB C 32.5 0.1 1 717 . 160 ALA H H 8.24 0.02 1 718 . 160 ALA N N 121.0 0.1 1 719 . 160 ALA CA C 55.6 0.1 1 720 . 160 ALA C C 180.1 0.1 1 721 . 160 ALA CB C 18.3 0.1 1 722 . 161 LEU H H 8.33 0.02 1 723 . 161 LEU N N 117.6 0.1 1 724 . 161 LEU CA C 58.0 0.1 1 725 . 161 LEU C C 179.1 0.1 1 726 . 161 LEU CB C 41.2 0.1 1 727 . 162 GLY H H 8.15 0.02 1 728 . 162 GLY N N 105.0 0.1 1 729 . 162 GLY CA C 47.9 0.1 1 730 . 162 GLY C C 175.8 0.1 1 731 . 163 VAL H H 8.18 0.02 1 732 . 163 VAL N N 120.6 0.1 1 733 . 163 VAL CA C 67.0 0.1 1 734 . 163 VAL C C 178.2 0.1 1 735 . 163 VAL CB C 31.2 0.1 1 736 . 164 PHE H H 8.26 0.02 1 737 . 164 PHE N N 117.9 0.1 1 738 . 164 PHE CA C 60.7 0.1 1 739 . 164 PHE C C 177.8 0.1 1 740 . 164 PHE CB C 38.2 0.1 1 741 . 170 TYR H H 8.48 0.02 1 742 . 170 TYR N N 117.8 0.1 1 743 . 170 TYR CA C 61.9 0.1 1 744 . 170 TYR C C 177.8 0.1 1 745 . 170 TYR CB C 38.5 0.1 1 746 . 171 SER H H 7.51 0.02 1 747 . 171 SER N N 118.3 0.1 1 748 . 171 SER CA C 58.3 0.1 1 749 . 171 SER C C 179.2 0.1 1 750 . 172 ILE H H 8.06 0.02 1 751 . 172 ILE N N 117.3 0.1 1 752 . 172 ILE CA C 65.0 0.1 1 753 . 172 ILE C C 178.9 0.1 1 754 . 172 ILE CB C 37.2 0.1 1 755 . 173 LYS H H 8.03 0.02 1 756 . 173 LYS N N 119.9 0.1 1 757 . 173 LYS CA C 59.4 0.1 1 758 . 173 LYS C C 179.4 0.1 1 759 . 173 LYS CB C 31.6 0.1 1 760 . 174 MET H H 8.40 0.02 1 761 . 174 MET N N 116.3 0.1 1 762 . 174 MET CA C 57.7 0.1 1 763 . 174 MET C C 179.4 0.1 1 764 . 174 MET CB C 31.5 0.1 1 765 . 175 LYS H H 8.14 0.02 1 766 . 175 LYS N N 119.5 0.1 1 767 . 175 LYS CA C 59.1 0.1 1 768 . 175 LYS C C 179.7 0.1 1 769 . 175 LYS CB C 31.7 0.1 1 770 . 176 GLY H H 8.31 0.02 1 771 . 176 GLY N N 107.3 0.1 1 772 . 176 GLY CA C 47.2 0.1 1 773 . 176 GLY C C 175.9 0.1 1 774 . 177 ILE H H 8.32 0.02 1 775 . 177 ILE N N 121.5 0.1 1 776 . 177 ILE CA C 64.6 0.1 1 777 . 177 ILE C C 179.8 0.1 1 778 . 177 ILE CB C 37.6 0.1 1 779 . 178 GLY H H 8.70 0.02 1 780 . 178 GLY N N 110.2 0.1 1 781 . 178 GLY CA C 47.5 0.1 1 782 . 178 GLY C C 176.2 0.1 1 783 . 179 GLY H H 8.44 0.02 1 784 . 179 GLY N N 109.1 0.1 1 785 . 179 GLY CA C 47.3 0.1 1 786 . 179 GLY C C 175.8 0.1 1 787 . 180 PHE H H 8.35 0.02 1 788 . 180 PHE N N 121.5 0.1 1 789 . 180 PHE CA C 61.1 0.1 1 790 . 180 PHE C C 177.6 0.1 1 791 . 180 PHE CB C 39.5 0.1 1 792 . 181 THR H H 8.33 0.02 1 793 . 181 THR N N 112.9 0.1 1 794 . 181 THR CA C 67.0 0.1 1 795 . 181 THR C C 177.4 0.1 1 796 . 181 THR CB C 68.5 0.1 1 797 . 182 LYS H H 8.11 0.02 1 798 . 182 LYS N N 121.4 0.1 1 799 . 182 LYS CA C 59.7 0.1 1 800 . 182 LYS C C 178.9 0.1 1 801 . 182 LYS CB C 31.8 0.1 1 802 . 183 GLU H H 8.05 0.02 1 803 . 183 GLU N N 117.6 0.1 1 804 . 183 GLU CA C 59.1 0.1 1 805 . 183 GLU C C 178.6 0.1 1 806 . 183 GLU CB C 27.5 0.1 1 807 . 184 LEU H H 8.02 0.02 1 808 . 184 LEU N N 118.0 0.1 1 809 . 184 LEU CA C 57.7 0.1 1 810 . 184 LEU C C 179.4 0.1 1 811 . 184 LEU CB C 41.7 0.1 1 812 . 185 THR H H 7.70 0.02 1 813 . 185 THR N N 109.1 0.1 1 814 . 185 THR CA C 64.7 0.1 1 815 . 185 THR C C 175.5 0.1 1 816 . 185 THR CB C 69.6 0.1 1 817 . 186 LEU H H 7.51 0.02 1 818 . 186 LEU N N 118.5 0.1 1 819 . 186 LEU CA C 55.4 0.1 1 820 . 186 LEU C C 177.6 0.1 1 821 . 186 LEU CB C 41.8 0.1 1 822 . 187 GLN H H 7.63 0.02 1 823 . 187 GLN N N 117.5 0.1 1 824 . 187 GLN CA C 56.4 0.1 1 825 . 187 GLN C C 175.6 0.1 1 826 . 187 GLN CB C 27.4 0.1 1 827 . 188 PRO CA C 65.1 0.1 1 828 . 188 PRO C C 177.4 0.1 1 829 . 188 PRO CB C 31.1 0.1 1 830 . 189 PHE H H 7.80 0.02 1 831 . 189 PHE N N 114.5 0.1 1 832 . 189 PHE CA C 59.0 0.1 1 833 . 189 PHE C C 176.4 0.1 1 834 . 189 PHE CB C 38.7 0.1 1 835 . 190 ASN H H 7.97 0.02 1 836 . 190 ASN N N 116.4 0.1 1 837 . 190 ASN CA C 54.2 0.1 1 838 . 190 ASN C C 176.4 0.1 1 839 . 190 ASN CB C 38.5 0.1 1 840 . 191 HIS H H 8.23 0.02 1 841 . 191 HIS N N 116.3 0.1 1 842 . 191 HIS CA C 56.9 0.1 1 843 . 191 HIS C C 175.4 0.1 1 844 . 191 HIS CB C 28.3 0.1 1 845 . 192 TRP H H 7.92 0.02 1 846 . 192 TRP N N 118.6 0.1 1 847 . 192 TRP CA C 58.7 0.1 1 848 . 192 TRP C C 177.1 0.1 1 849 . 192 TRP CB C 29.5 0.1 1 850 . 193 ALA H H 7.78 0.02 1 851 . 193 ALA N N 120.0 0.1 1 852 . 193 ALA CA C 53.7 0.1 1 853 . 193 ALA C C 177.2 0.1 1 854 . 193 ALA CB C 18.7 0.1 1 855 . 194 PHE H H 7.60 0.02 1 856 . 194 PHE N N 114.1 0.1 1 857 . 194 PHE CA C 59.3 0.1 1 858 . 194 PHE C C 176.7 0.1 1 859 . 194 PHE CB C 39.3 0.1 1 860 . 195 ILE H H 8.01 0.02 1 861 . 195 ILE N N 119.3 0.1 1 862 . 195 ILE CA C 64.6 0.1 1 863 . 195 ILE C C 175.4 0.1 1 864 . 195 ILE CB C 31.6 0.1 1 865 . 196 PRO CA C 65.6 0.1 1 866 . 196 PRO C C 177.9 0.1 1 867 . 196 PRO CB C 30.8 0.1 1 868 . 197 VAL H H 7.55 0.02 1 869 . 197 VAL N N 115.4 0.1 1 870 . 197 VAL CA C 66.3 0.1 1 871 . 197 VAL C C 177.4 0.1 1 872 . 197 VAL CB C 31.5 0.1 1 873 . 198 ASN H H 7.98 0.02 1 874 . 198 ASN N N 117.0 0.1 1 875 . 198 ASN CA C 57.0 0.1 1 876 . 198 ASN C C 177.8 0.1 1 877 . 198 ASN CB C 38.6 0.1 1 878 . 199 LEU H H 8.02 0.02 1 879 . 199 LEU N N 119.2 0.1 1 880 . 199 LEU CA C 58.3 0.1 1 881 . 199 LEU C C 179.8 0.1 1 882 . 199 LEU CB C 41.3 0.1 1 883 . 200 ILE H H 7.92 0.02 1 884 . 200 ILE N N 119.4 0.1 1 885 . 200 ILE CA C 65.0 0.1 1 886 . 200 ILE C C 178.5 0.1 1 887 . 200 ILE CB C 37.3 0.1 1 888 . 201 LEU H H 8.21 0.02 1 889 . 201 LEU N N 118.4 0.1 1 890 . 201 LEU CA C 58.2 0.1 1 891 . 201 LEU C C 180.5 0.1 1 892 . 201 LEU CB C 41.0 0.1 1 893 . 202 GLU H H 8.45 0.02 1 894 . 202 GLU N N 118.9 0.1 1 895 . 202 GLU CA C 59.3 0.1 1 896 . 202 GLU C C 178.9 0.1 1 897 . 202 GLU CB C 27.7 0.1 1 898 . 203 GLY H H 8.40 0.02 1 899 . 203 GLY N N 107.5 0.1 1 900 . 203 GLY CA C 48.1 0.1 1 901 . 203 GLY C C 175.9 0.1 1 902 . 204 VAL H H 8.66 0.02 1 903 . 204 VAL N N 120.1 0.1 1 904 . 204 VAL CA C 66.6 0.1 1 905 . 204 VAL C C 179.4 0.1 1 906 . 204 VAL CB C 31.3 0.1 1 907 . 205 SER H H 8.13 0.02 1 908 . 205 SER N N 116.0 0.1 1 909 . 205 SER CA C 62.5 0.1 1 910 . 205 SER C C 177.2 0.1 1 911 . 205 SER CB C 63.5 0.1 1 912 . 206 LEU H H 8.08 0.02 1 913 . 206 LEU N N 121.4 0.1 1 914 . 206 LEU CA C 58.1 0.1 1 915 . 206 LEU C C 179.3 0.1 1 916 . 206 LEU CB C 41.8 0.1 1 917 . 207 LEU H H 8.13 0.02 1 918 . 207 LEU N N 117.0 0.1 1 919 . 207 LEU CA C 57.0 0.1 1 920 . 207 LEU C C 178.2 0.1 1 921 . 207 LEU CB C 41.7 0.1 1 922 . 208 SER H H 7.92 0.02 1 923 . 208 SER N N 110.3 0.1 1 924 . 208 SER CA C 60.9 0.1 1 925 . 208 SER C C 176.5 0.1 1 926 . 208 SER CB C 64.4 0.1 1 927 . 209 LYS H H 7.84 0.02 1 928 . 209 LYS N N 121.8 0.1 1 929 . 209 LYS CA C 60.1 0.1 1 930 . 209 LYS C C 175.7 0.1 1 931 . 209 LYS CB C 29.5 0.1 1 932 . 210 PRO CA C 66.2 0.1 1 933 . 210 PRO C C 178.9 0.1 1 934 . 210 PRO CB C 31.0 0.1 1 935 . 211 VAL H H 7.40 0.02 1 936 . 211 VAL N N 116.0 0.1 1 937 . 211 VAL CA C 66.2 0.1 1 938 . 211 VAL C C 177.8 0.1 1 939 . 211 VAL CB C 31.4 0.1 1 940 . 212 SER H H 8.13 0.02 1 941 . 212 SER N N 114.9 0.1 1 942 . 212 SER CA C 62.2 0.1 1 943 . 212 SER C C 177.1 0.1 1 944 . 212 SER CB C 63.4 0.1 1 945 . 213 LEU H H 8.12 0.02 1 946 . 213 LEU N N 121.4 0.1 1 947 . 213 LEU CA C 58.2 0.1 1 948 . 213 LEU C C 179.2 0.1 1 949 . 213 LEU CB C 41.4 0.1 1 950 . 214 GLY H H 8.28 0.02 1 951 . 214 GLY N N 106.1 0.1 1 952 . 214 GLY CA C 47.9 0.1 1 953 . 214 GLY C C 175.8 0.1 1 954 . 215 LEU H H 8.42 0.02 1 955 . 215 LEU N N 120.7 0.1 1 956 . 215 LEU CA C 58.2 0.1 1 957 . 215 LEU C C 180.1 0.1 1 958 . 215 LEU CB C 41.6 0.1 1 959 . 216 ARG H H 7.97 0.02 1 960 . 216 ARG N N 118.6 0.1 1 961 . 216 ARG CA C 59.0 0.1 1 962 . 216 ARG C C 179.1 0.1 1 963 . 216 ARG CB C 29.7 0.1 1 964 . 217 LEU H H 8.40 0.02 1 965 . 217 LEU N N 120.0 0.1 1 966 . 217 LEU CA C 58.5 0.1 1 967 . 217 LEU C C 179.4 0.1 1 968 . 217 LEU CB C 41.3 0.1 1 969 . 218 PHE H H 8.52 0.02 1 970 . 218 PHE N N 118.0 0.1 1 971 . 218 PHE CA C 61.5 0.1 1 972 . 218 PHE C C 178.4 0.1 1 973 . 218 PHE CB C 38.9 0.1 1 974 . 219 GLY H H 8.67 0.02 1 975 . 219 GLY N N 106.1 0.1 1 976 . 219 GLY CA C 47.8 0.1 1 977 . 219 GLY C C 175.9 0.1 1 978 . 220 ASN H H 8.20 0.02 1 979 . 220 ASN N N 119.2 0.1 1 980 . 220 ASN CA C 56.3 0.1 1 981 . 220 ASN C C 178.2 0.1 1 982 . 220 ASN CB C 38.7 0.1 1 983 . 221 MET H H 8.16 0.02 1 984 . 221 MET N N 119.6 0.1 1 985 . 221 MET CA C 59.1 0.1 1 986 . 221 MET C C 178.2 0.1 1 987 . 221 MET CB C 32.2 0.1 1 988 . 222 TYR H H 8.44 0.02 1 989 . 222 TYR N N 119.6 0.1 1 990 . 222 TYR CA C 61.1 0.1 1 991 . 222 TYR C C 177.8 0.1 1 992 . 222 TYR CB C 38.0 0.1 1 993 . 223 ALA H H 8.28 0.02 1 994 . 223 ALA N N 119.4 0.1 1 995 . 223 ALA CA C 55.5 0.1 1 996 . 223 ALA C C 179.9 0.1 1 997 . 223 ALA CB C 18.1 0.1 1 998 . 224 GLY H H 8.16 0.02 1 999 . 224 GLY N N 102.6 0.1 1 1000 . 224 GLY CA C 47.5 0.1 1 1001 . 224 GLY C C 175.9 0.1 1 1002 . 225 GLU H H 8.10 0.02 1 1003 . 225 GLU N N 120.7 0.1 1 1004 . 225 GLU CA C 59.2 0.1 1 1005 . 225 GLU C C 178.0 0.1 1 1006 . 225 GLU CB C 27.8 0.1 1 1007 . 226 LEU H H 7.97 0.02 1 1008 . 226 LEU N N 118.4 0.1 1 1009 . 226 LEU CA C 58.3 0.1 1 1010 . 226 LEU C C 180.0 0.1 1 1011 . 226 LEU CB C 38.7 0.1 1 1012 . 227 ILE H H 7.88 0.02 1 1013 . 227 ILE N N 119.3 0.1 1 1014 . 227 ILE CA C 65.0 0.1 1 1015 . 227 ILE CB C 37.2 0.1 1 1016 . 230 LEU CA C 57.0 0.1 1 1017 . 230 LEU C C 179.1 0.1 1 1018 . 230 LEU CB C 38.6 0.1 1 1019 . 231 ILE H H 8.56 0.02 1 1020 . 231 ILE N N 120.1 0.1 1 1021 . 231 ILE CA C 64.9 0.1 1 1022 . 231 ILE C C 178.4 0.1 1 1023 . 231 ILE CB C 37.3 0.1 1 1024 . 232 ALA H H 8.46 0.02 1 1025 . 232 ALA N N 120.7 0.1 1 1026 . 232 ALA CA C 54.9 0.1 1 1027 . 232 ALA C C 180.1 0.1 1 1028 . 232 ALA CB C 17.8 0.1 1 1029 . 233 GLY H H 8.02 0.02 1 1030 . 233 GLY N N 102.3 0.1 1 1031 . 233 GLY CA C 46.5 0.1 1 1032 . 233 GLY C C 175.3 0.1 1 1033 . 234 LEU H H 7.95 0.02 1 1034 . 234 LEU N N 119.0 0.1 1 1035 . 234 LEU CA C 56.3 0.1 1 1036 . 234 LEU C C 178.9 0.1 1 1037 . 234 LEU CB C 42.4 0.1 1 1038 . 235 LEU H H 8.10 0.02 1 1039 . 235 LEU N N 119.9 0.1 1 1040 . 235 LEU CA C 59.2 0.1 1 1041 . 235 LEU C C 176.8 0.1 1 1042 . 235 LEU CB C 39.6 0.1 1 1043 . 236 PRO CA C 66.1 0.1 1 1044 . 236 PRO C C 178.2 0.1 1 1045 . 236 PRO CB C 29.1 0.1 1 1046 . 237 TRP H H 7.47 0.02 1 1047 . 237 TRP N N 117.4 0.1 1 1048 . 237 TRP CA C 60.1 0.1 1 1049 . 237 TRP C C 178.6 0.1 1 1050 . 237 TRP CB C 30.7 0.1 1 1051 . 238 TRP H H 8.40 0.02 1 1052 . 238 TRP N N 119.1 0.1 1 1053 . 238 TRP CA C 60.1 0.1 1 1054 . 238 TRP C C 178.5 0.1 1 1055 . 238 TRP CB C 31.5 0.1 1 1056 . 239 SER H H 8.40 0.02 1 1057 . 239 SER N N 112.6 0.1 1 1058 . 239 SER CA C 62.2 0.1 1 1059 . 239 SER C C 175.7 0.1 1 1060 . 239 SER CB C 63.8 0.1 1 1061 . 240 GLN H H 7.51 0.02 1 1062 . 240 GLN N N 118.3 0.1 1 1063 . 240 GLN CA C 58.4 0.1 1 1064 . 240 GLN C C 177.9 0.1 1 1065 . 240 GLN CB C 28.4 0.1 1 1066 . 241 TRP H H 7.91 0.02 1 1067 . 241 TRP N N 119.7 0.1 1 1068 . 241 TRP CA C 60.6 0.1 1 1069 . 241 TRP C C 178.4 0.1 1 1070 . 241 TRP CB C 29.2 0.1 1 1071 . 242 ILE H H 7.89 0.02 1 1072 . 242 ILE N N 116.6 0.1 1 1073 . 242 ILE CA C 63.6 0.1 1 1074 . 242 ILE C C 177.7 0.1 1 1075 . 242 ILE CB C 37.6 0.1 1 1076 . 243 LEU H H 7.65 0.02 1 1077 . 243 LEU N N 116.7 0.1 1 1078 . 243 LEU CA C 56.6 0.1 1 1079 . 243 LEU C C 178.0 0.1 1 1080 . 243 LEU CB C 41.7 0.1 1 1081 . 244 ASN H H 7.68 0.02 1 1082 . 244 ASN N N 113.9 0.1 1 1083 . 244 ASN CA C 55.1 0.1 1 1084 . 244 ASN C C 176.9 0.1 1 1085 . 244 ASN CB C 40.2 0.1 1 1086 . 245 VAL H H 8.02 0.02 1 1087 . 245 VAL N N 120.3 0.1 1 1088 . 245 VAL CA C 68.4 0.1 1 1089 . 245 VAL CB C 29.5 0.1 1 1090 . 246 PRO CA C 66.4 0.1 1 1091 . 246 PRO C C 178.1 0.1 1 1092 . 246 PRO CB C 30.6 0.1 1 1093 . 247 TRP H H 7.26 0.02 1 1094 . 247 TRP N N 115.7 0.1 1 1095 . 247 TRP CA C 60.2 0.1 1 1096 . 247 TRP C C 179.2 0.1 1 1097 . 247 TRP CB C 29.8 0.1 1 1098 . 248 ALA H H 8.38 0.02 1 1099 . 248 ALA N N 123.5 0.1 1 1100 . 248 ALA CA C 55.8 0.1 1 1101 . 248 ALA C C 180.2 0.1 1 1102 . 248 ALA CB C 18.2 0.1 1 1103 . 249 ILE H H 8.35 0.02 1 1104 . 249 ILE N N 117.3 0.1 1 1105 . 249 ILE CA C 65.1 0.1 1 1106 . 249 ILE C C 178.1 0.1 1 1107 . 249 ILE CB C 37.0 0.1 1 1108 . 250 PHE H H 8.40 0.02 1 1109 . 250 PHE N N 118.6 0.1 1 1110 . 250 PHE CA C 61.3 0.1 1 1111 . 250 PHE C C 177.3 0.1 1 1112 . 250 PHE CB C 39.1 0.1 1 1113 . 251 HIS H H 8.13 0.02 1 1114 . 251 HIS N N 113.6 0.1 1 1115 . 251 HIS CA C 59.9 0.1 1 1116 . 251 HIS C C 176.6 0.1 1 1117 . 251 HIS CB C 28.1 0.1 1 1118 . 252 ILE H H 8.19 0.02 1 1119 . 252 ILE N N 118.9 0.1 1 1120 . 252 ILE CA C 64.9 0.1 1 1121 . 252 ILE C C 179.4 0.1 1 1122 . 252 ILE CB C 37.3 0.1 1 1123 . 253 LEU H H 8.53 0.02 1 1124 . 253 LEU N N 123.3 0.1 1 1125 . 253 LEU CA C 58.8 0.1 1 1126 . 253 LEU C C 178.7 0.1 1 1127 . 253 LEU CB C 40.9 0.1 1 1128 . 254 ILE H H 7.90 0.02 1 1129 . 254 ILE N N 117.4 0.1 1 1130 . 254 ILE CA C 64.2 0.1 1 1131 . 254 ILE C C 178.7 0.1 1 1132 . 254 ILE CB C 36.5 0.1 1 1133 . 255 ILE H H 7.86 0.02 1 1134 . 255 ILE N N 118.7 0.1 1 1135 . 255 ILE CA C 64.9 0.1 1 1136 . 255 ILE C C 178.4 0.1 1 1137 . 255 ILE CB C 37.2 0.1 1 1138 . 256 THR H H 8.07 0.02 1 1139 . 256 THR N N 116.5 0.1 1 1140 . 256 THR CA C 67.8 0.1 1 1141 . 256 THR C C 176.9 0.1 1 1142 . 256 THR CB C 68.4 0.1 1 1143 . 257 LEU H H 8.50 0.02 1 1144 . 257 LEU N N 120.1 0.1 1 1145 . 257 LEU CA C 58.3 0.1 1 1146 . 257 LEU C C 179.2 0.1 1 1147 . 257 LEU CB C 41.1 0.1 1 1148 . 258 GLN H H 8.34 0.02 1 1149 . 258 GLN N N 116.7 0.1 1 1150 . 258 GLN CA C 59.7 0.1 1 1151 . 258 GLN C C 178.5 0.1 1 1152 . 258 GLN CB C 28.6 0.1 1 1153 . 259 ALA H H 8.39 0.02 1 1154 . 259 ALA N N 121.0 0.1 1 1155 . 259 ALA CA C 55.6 0.1 1 1156 . 259 ALA C C 179.6 0.1 1 1157 . 259 ALA CB C 18.3 0.1 1 1158 . 260 PHE H H 8.43 0.02 1 1159 . 260 PHE N N 118.6 0.1 1 1160 . 260 PHE CA C 61.7 0.1 1 1161 . 260 PHE C C 177.5 0.1 1 1162 . 260 PHE CB C 39.2 0.1 1 1163 . 261 ILE H H 8.48 0.02 1 1164 . 261 ILE N N 121.7 0.1 1 1165 . 261 ILE CA C 65.5 0.1 1 1166 . 261 ILE CB C 37.7 0.1 1 1167 . 263 MET H H 8.03 0.02 1 1168 . 263 MET N N 118.1 0.1 1 1169 . 263 MET CA C 55.9 0.1 1 1170 . 263 MET C C 177.2 0.1 1 1171 . 263 MET CB C 30.8 0.1 1 1172 . 264 VAL H H 8.01 0.02 1 1173 . 264 VAL N N 118.5 0.1 1 1174 . 264 VAL CA C 66.2 0.1 1 1175 . 264 VAL C C 178.2 0.1 1 1176 . 264 VAL CB C 30.8 0.1 1 1177 . 265 LEU H H 8.00 0.02 1 1178 . 265 LEU N N 118.5 0.1 1 1179 . 265 LEU CA C 55.2 0.1 1 1180 . 265 LEU C C 180.9 0.1 1 1181 . 265 LEU CB C 38.5 0.1 1 1182 . 266 THR H H 8.25 0.02 1 1183 . 266 THR N N 116.4 0.1 1 1184 . 266 THR CA C 66.9 0.1 1 1185 . 266 THR C C 176.2 0.1 1 1186 . 266 THR CB C 68.6 0.1 1 1187 . 267 ILE H H 8.46 0.02 1 1188 . 267 ILE N N 118.6 0.1 1 1189 . 267 ILE CA C 65.3 0.1 1 1190 . 267 ILE C C 179.9 0.1 1 1191 . 267 ILE CB C 37.1 0.1 1 1192 . 268 VAL H H 8.60 0.02 1 1193 . 268 VAL N N 122.8 0.1 1 1194 . 268 VAL CA C 67.7 0.1 1 1195 . 268 VAL C C 178.2 0.1 1 1196 . 268 VAL CB C 31.1 0.1 1 1197 . 269 TYR H H 8.65 0.02 1 1198 . 269 TYR N N 120.4 0.1 1 1199 . 269 TYR CA C 62.3 0.1 1 1200 . 269 TYR C C 178.4 0.1 1 1201 . 269 TYR CB C 38.1 0.1 1 1202 . 270 LEU H H 8.82 0.02 1 1203 . 270 LEU N N 117.7 0.1 1 1204 . 270 LEU CA C 57.9 0.1 1 1205 . 270 LEU C C 180.7 0.1 1 1206 . 270 LEU CB C 41.5 0.1 1 1207 . 271 SER H H 8.41 0.02 1 1208 . 271 SER N N 116.5 0.1 1 1209 . 271 SER CA C 62.8 0.1 1 1210 . 271 SER C C 176.6 0.1 1 1211 . 271 SER CB C 63.5 0.1 1 1212 . 272 MET H H 8.28 0.02 1 1213 . 272 MET N N 121.4 0.1 1 1214 . 272 MET CA C 58.9 0.1 1 1215 . 272 MET C C 178.9 0.1 1 1216 . 272 MET CB C 32.4 0.1 1 1217 . 273 ALA H H 8.52 0.02 1 1218 . 273 ALA N N 120.4 0.1 1 1219 . 273 ALA CA C 54.9 0.1 1 1220 . 273 ALA C C 180.3 0.1 1 1221 . 273 ALA CB C 17.9 0.1 1 1222 . 274 SER H H 7.88 0.02 1 1223 . 274 SER N N 111.6 0.1 1 1224 . 274 SER CA C 61.3 0.1 1 1225 . 274 SER C C 175.3 0.1 1 1226 . 274 SER CB C 64.1 0.1 1 1227 . 275 GLU H H 7.58 0.02 1 1228 . 275 GLU N N 118.0 0.1 1 1229 . 275 GLU CA C 56.9 0.1 1 1230 . 275 GLU C C 176.6 0.1 1 1231 . 275 GLU CB C 28.4 0.1 1 1232 . 276 GLU H H 7.76 0.02 1 1233 . 276 GLU N N 115.4 0.1 1 1234 . 276 GLU CA C 56.2 0.1 1 1235 . 276 GLU C C 175.8 0.1 1 1236 . 276 GLU CB C 28.3 0.1 1 1237 . 277 HIS H H 7.97 0.02 1 1238 . 277 HIS N N 114.0 0.1 1 1239 . 277 HIS CA C 54.6 0.1 1 1240 . 277 HIS C C 174.0 0.1 1 1241 . 277 HIS CB C 28.3 0.1 1 stop_ save_