data_4331 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Backbone 1H, 13C, and 15N Resonance Assignments of Streptomyces Subtilisin Inhibitor ; _BMRB_accession_number 4331 _BMRB_flat_file_name bmr4331.str _Entry_type original _Submission_date 1999-04-12 _Accession_date 1999-04-13 _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 Sasakawa Hiroaki . . 2 Tamura Atsuo . . 3 Taguchi Seiichi . . 4 Akasaka Kazuyuki . . 5 Miyake Yoko . . 6 Kainosho Masatsune . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 98 "13C chemical shifts" 198 "15N chemical shifts" 98 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 1999-05-24 original BMRB . stop_ _Original_release_date 1999-04-13 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full ; Sasakawa, H., Tamura, A., Taguchi, S., Akasaka, K., Miyake, Y., Kainosho, M., "Backbone 1H, 13C, and 15N Resonance Assignments of Streptomyces Subtilisin Inhibitor," J. Biomol. NMR, in preparation (1999). ; _Citation_title ; Backbone 1H, 13C, and 15N Resonance Assignments of Streptomyces Subtilisin Inhibitor ; _Citation_status 'in preparation' _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID ? loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Sasakawa Hiroaki . . 2 Tamura Atsuo . . 3 Taguchi Seiichi . . 4 Akasaka Kazuyuki . . 5 Miyake Yoko . . 6 Kainosho Masatsune . . stop_ _Journal_abbreviation 'J. Biomol. NMR' _Journal_volume . _Journal_issue . _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first . _Page_last . _Year 1999 _Details . loop_ _Keyword 'Streptomyces subtilisin inhibitor' 'resonance assignment' stop_ save_ ################################## # Molecular system description # ################################## save_SSI_dimer _Saveframe_category molecular_system _Mol_system_name 'Streptomyces subtilisin inhibitor' _Abbreviation_common SSI _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'SSI subunit 1' $SSI 'SSI subunit 2' $SSI stop_ _System_molecular_weight 23000 _System_physical_state native _System_oligomer_state dimer _System_paramagnetic no _System_thiol_state . loop_ _Biological_function 'protease inhibitor' stop_ _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_SSI _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'Streptomyces subtilisin inhibitor' _Abbreviation_common SSI _Molecular_mass 11500 _Mol_thiol_state . _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 113 _Mol_residue_sequence ; GAPSALYAPSALVLTVGKGV SATTAAPERAVTLTCAPGPS GTHPAAGSACADLAAVGGDL NALTRGEDVMCPMVYDPVLL TVDGVWQGKRVSYERVFSNE CEMNAHGSSVFAF ; loop_ _Residue_seq_code _Residue_label 1 GLY 2 ALA 3 PRO 4 SER 5 ALA 6 LEU 7 TYR 8 ALA 9 PRO 10 SER 11 ALA 12 LEU 13 VAL 14 LEU 15 THR 16 VAL 17 GLY 18 LYS 19 GLY 20 VAL 21 SER 22 ALA 23 THR 24 THR 25 ALA 26 ALA 27 PRO 28 GLU 29 ARG 30 ALA 31 VAL 32 THR 33 LEU 34 THR 35 CYS 36 ALA 37 PRO 38 GLY 39 PRO 40 SER 41 GLY 42 THR 43 HIS 44 PRO 45 ALA 46 ALA 47 GLY 48 SER 49 ALA 50 CYS 51 ALA 52 ASP 53 LEU 54 ALA 55 ALA 56 VAL 57 GLY 58 GLY 59 ASP 60 LEU 61 ASN 62 ALA 63 LEU 64 THR 65 ARG 66 GLY 67 GLU 68 ASP 69 VAL 70 MET 71 CYS 72 PRO 73 MET 74 VAL 75 TYR 76 ASP 77 PRO 78 VAL 79 LEU 80 LEU 81 THR 82 VAL 83 ASP 84 GLY 85 VAL 86 TRP 87 GLN 88 GLY 89 LYS 90 ARG 91 VAL 92 SER 93 TYR 94 GLU 95 ARG 96 VAL 97 PHE 98 SER 99 ASN 100 GLU 101 CYS 102 GLU 103 MET 104 ASN 105 ALA 106 HIS 107 GLY 108 SER 109 SER 110 VAL 111 PHE 112 ALA 113 PHE stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date . save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $SSI 'S. albogriseolus' 1887 Eubacteria . Streptomyces albogriseolus 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 $SSI 'recombinant technology' . . . . . stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_one _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Concentration_max_value _Isotopic_labeling $SSI_dimer . mM 1 '[U-13C; U-15N]' phosphate 25 mM . . 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_HNCA_1 _Saveframe_category NMR_applied_experiment _Experiment_name HNCA _Sample_label . save_ save_HN(CO)CA_2 _Saveframe_category NMR_applied_experiment _Experiment_name HN(CO)CA _Sample_label . save_ save_HNCO_3 _Saveframe_category NMR_applied_experiment _Experiment_name HNCO _Sample_label . save_ ####################### # Sample conditions # ####################### save_sample_conditions _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 6.3 0.05 na temperature 303 0.5 K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference _Saveframe_category chemical_shift_reference _Details . loop_ _Mol_common_name _Atom_type _Atom_isotope_number _Atom_group _Chem_shift_units _Chem_shift_value _Reference_method _Reference_type _External_reference_sample_geometry _External_reference_location _External_reference_axis _Indirect_shift_ratio DSS C 13 'methyl protons' ppm 0.0 . indirect . . . 0.251449530 DSS H 1 'methyl protons' ppm 0.0 internal direct . . . 1.0 DSS N 15 'methyl protons' ppm 0.0 . indirect . . . 0.101329118 stop_ save_ ################################### # Assigned chemical shift lists # ################################### ################################################################### # Chemical Shift Ambiguity Index Value Definitions # # # # The values other than 1 are used for those atoms with different # # chemical shifts that cannot be assigned to stereospecific atoms # # or to specific residues or chains. # # # # Index Value Definition # # # # 1 Unique (including isolated methyl protons, # # geminal atoms, and geminal methyl # # groups with identical chemical shifts) # # (e.g. ILE HD11, HD12, HD13 protons) # # 2 Ambiguity of geminal atoms or geminal methyl # # proton groups (e.g. ASP HB2 and HB3 # # protons, LEU CD1 and CD2 carbons, or # # LEU HD11, HD12, HD13 and HD21, HD22, # # HD23 methyl protons) # # 3 Aromatic atoms on opposite sides of # # symmetrical rings (e.g. TYR HE1 and HE2 # # protons) # # 4 Intraresidue ambiguities (e.g. LYS HG and # # HD protons or TRP HZ2 and HZ3 protons) # # 5 Interresidue ambiguities (LYS 12 vs. LYS 27) # # 6 Intermolecular ambiguities (e.g. ASP 31 CA # # in monomer 1 and ASP 31 CA in monomer 2 # # of an asymmetrical homodimer, duplex # # DNA assignments, or other assignments # # that may apply to atoms in one or more # # molecule in the molecular assembly) # # 9 Ambiguous, specific ambiguity not defined # # # ################################################################### save_assigned_chemical_shifts _Saveframe_category assigned_chemical_shifts _Details . loop_ _Experiment_label HNCA HN(CO)CA HNCO stop_ loop_ _Sample_label $sample_one stop_ _Sample_conditions_label $sample_conditions _Chem_shift_reference_set_label $chemical_shift_reference _Mol_system_component_name 'SSI subunit 1' _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 . 10 SER H H 8.42 . 1 2 . 10 SER C C 173.0 . 1 3 . 10 SER CA C 57.3 . 1 4 . 10 SER N N 116.0 . 1 5 . 11 ALA H H 9.23 . 1 6 . 11 ALA C C 174.3 . 1 7 . 11 ALA CA C 52.9 . 1 8 . 11 ALA N N 129.6 . 1 9 . 12 LEU H H 9.47 . 1 10 . 12 LEU C C 175.6 . 1 11 . 12 LEU CA C 53.9 . 1 12 . 12 LEU N N 122.8 . 1 13 . 13 VAL H H 9.17 . 1 14 . 13 VAL C C 174.6 . 1 15 . 13 VAL CA C 60.8 . 1 16 . 13 VAL N N 117.6 . 1 17 . 14 LEU H H 8.95 . 1 18 . 14 LEU C C 175.7 . 1 19 . 14 LEU CA C 55.4 . 1 20 . 14 LEU N N 130.3 . 1 21 . 15 THR H H 9.16 . 1 22 . 15 THR C C 172.3 . 1 23 . 15 THR CA C 60.4 . 1 24 . 15 THR N N 111.4 . 1 25 . 16 VAL H H 8.65 . 1 26 . 16 VAL C C 174.3 . 1 27 . 16 VAL CA C 60.2 . 1 28 . 16 VAL N N 118.3 . 1 29 . 17 GLY H H 7.94 . 1 30 . 17 GLY C C 171.3 . 1 31 . 17 GLY CA C 45.6 . 1 32 . 17 GLY N N 112.4 . 1 33 . 18 LYS H H 8.98 . 1 34 . 18 LYS C C 175.8 . 1 35 . 18 LYS CA C 56.7 . 1 36 . 18 LYS N N 121.1 . 1 37 . 19 GLY H H 7.98 . 1 38 . 19 GLY C C 171.6 . 1 39 . 19 GLY CA C 44.7 . 1 40 . 19 GLY N N 111.0 . 1 41 . 20 VAL H H 7.48 . 1 42 . 20 VAL C C 175.4 . 1 43 . 20 VAL CA C 60.9 . 1 44 . 20 VAL N N 102.7 . 1 45 . 21 SER H H 7.35 . 1 46 . 21 SER C C 174.3 . 1 47 . 21 SER CA C 56.6 . 1 48 . 21 SER N N 112.6 . 1 49 . 22 ALA H H 9.58 . 1 50 . 22 ALA C C 178.8 . 1 51 . 22 ALA CA C 55.7 . 1 52 . 22 ALA N N 127.5 . 1 53 . 23 THR H H 7.78 . 1 54 . 23 THR C C 175.9 . 1 55 . 23 THR CA C 64.2 . 1 56 . 23 THR N N 105.6 . 1 57 . 24 THR H H 7.22 . 1 58 . 24 THR C C 174.0 . 1 59 . 24 THR CA C 62.1 . 1 60 . 24 THR N N 109.0 . 1 61 . 25 ALA H H 7.95 . 1 62 . 25 ALA C C 175.9 . 1 63 . 25 ALA CA C 50.8 . 1 64 . 25 ALA N N 126.1 . 1 65 . 26 ALA H H 8.66 . 1 66 . 26 ALA CA C 50.4 . 1 67 . 26 ALA N N 130.8 . 1 68 . 27 PRO C C 175.4 . 1 69 . 28 GLU H H 9.50 . 1 70 . 28 GLU C C 176.9 . 1 71 . 28 GLU CA C 57.9 . 1 72 . 28 GLU N N 125.2 . 1 73 . 29 ARG H H 7.85 . 1 74 . 29 ARG C C 174.4 . 1 75 . 29 ARG CA C 55.5 . 1 76 . 29 ARG N N 113.4 . 1 77 . 30 ALA H H 8.69 . 1 78 . 30 ALA C C 175.7 . 1 79 . 30 ALA CA C 51.5 . 1 80 . 30 ALA N N 122.3 . 1 81 . 31 VAL H H 8.74 . 1 82 . 31 VAL C C 174.2 . 1 83 . 31 VAL CA C 58.6 . 1 84 . 31 VAL N N 112.0 . 1 85 . 32 THR H H 8.33 . 1 86 . 32 THR C C 173.9 . 1 87 . 32 THR CA C 58.9 . 1 88 . 32 THR N N 108.7 . 1 89 . 33 LEU H H 9.00 . 1 90 . 33 LEU C C 174.4 . 1 91 . 33 LEU CA C 55.0 . 1 92 . 33 LEU N N 120.8 . 1 93 . 34 THR H H 8.98 . 1 94 . 34 THR C C 174.0 . 1 95 . 34 THR CA C 61.9 . 1 96 . 34 THR N N 122.7 . 1 97 . 35 CYS H H 7.74 . 1 98 . 35 CYS C C 173.2 . 1 99 . 35 CYS CA C 53.4 . 1 100 . 35 CYS N N 115.6 . 1 101 . 36 ALA H H 7.47 . 1 102 . 36 ALA CA C 50.1 . 1 103 . 36 ALA N N 122.7 . 1 104 . 37 PRO C C 175.6 . 1 105 . 37 PRO CA C 65.9 . 1 106 . 38 GLY H H 7.15 . 1 107 . 38 GLY CA C 44.9 . 1 108 . 38 GLY N N 108.7 . 1 109 . 39 PRO C C 177.8 . 1 110 . 39 PRO CA C 62.9 . 1 111 . 40 SER H H 9.20 . 1 112 . 40 SER C C 172.3 . 1 113 . 40 SER CA C 60.3 . 1 114 . 40 SER N N 118.6 . 1 115 . 41 GLY H H 8.08 . 1 116 . 41 GLY C C 174.5 . 1 117 . 41 GLY CA C 44.6 . 1 118 . 41 GLY N N 106.0 . 1 119 . 42 THR H H 8.12 . 1 120 . 42 THR C C 174.4 . 1 121 . 42 THR CA C 62.2 . 1 122 . 42 THR N N 107.7 . 1 123 . 43 HIS H H 8.26 . 1 124 . 43 HIS CA C 50.8 . 1 125 . 43 HIS N N 125.5 . 1 126 . 44 PRO C C 176.9 . 1 127 . 44 PRO CA C 64.8 . 1 128 . 45 ALA H H 11.05 . 1 129 . 45 ALA C C 176.4 . 1 130 . 45 ALA CA C 50.0 . 1 131 . 45 ALA N N 130.8 . 1 132 . 46 ALA H H 7.61 . 1 133 . 46 ALA C C 179.0 . 1 134 . 46 ALA CA C 56.2 . 1 135 . 46 ALA N N 121.2 . 1 136 . 47 GLY H H 8.75 . 1 137 . 47 GLY C C 177.1 . 1 138 . 47 GLY CA C 47.9 . 1 139 . 47 GLY N N 103.5 . 1 140 . 48 SER H H 7.99 . 1 141 . 48 SER C C 175.7 . 1 142 . 48 SER CA C 61.6 . 1 143 . 48 SER N N 119.2 . 1 144 . 49 ALA H H 8.85 . 1 145 . 49 ALA C C 179.8 . 1 146 . 49 ALA CA C 55.5 . 1 147 . 49 ALA N N 125.2 . 1 148 . 50 CYS H H 8.64 . 1 149 . 50 CYS C C 177.4 . 1 150 . 50 CYS CA C 59.4 . 1 151 . 50 CYS N N 114.2 . 1 152 . 51 ALA H H 7.62 . 1 153 . 51 ALA C C 180.7 . 1 154 . 51 ALA CA C 55.7 . 1 155 . 51 ALA N N 123.9 . 1 156 . 52 ASP H H 8.53 . 1 157 . 52 ASP C C 179.2 . 1 158 . 52 ASP CA C 57.6 . 1 159 . 52 ASP N N 121.5 . 1 160 . 53 LEU H H 7.80 . 1 161 . 53 LEU C C 179.5 . 1 162 . 53 LEU CA C 57.3 . 1 163 . 53 LEU N N 117.6 . 1 164 . 54 ALA H H 8.44 . 1 165 . 54 ALA C C 181.6 . 1 166 . 54 ALA CA C 55.4 . 1 167 . 54 ALA N N 122.4 . 1 168 . 55 ALA H H 7.92 . 1 169 . 55 ALA C C 179.4 . 1 170 . 55 ALA CA C 55.2 . 1 171 . 55 ALA N N 120.6 . 1 172 . 56 VAL H H 6.96 . 1 173 . 56 VAL C C 177.7 . 1 174 . 56 VAL CA C 60.1 . 1 175 . 56 VAL N N 105.4 . 1 176 . 57 GLY H H 7.93 . 1 177 . 57 GLY C C 175.6 . 1 178 . 57 GLY CA C 47.9 . 1 179 . 57 GLY N N 113.4 . 1 180 . 58 GLY H H 8.16 . 1 181 . 58 GLY C C 171.5 . 1 182 . 58 GLY CA C 44.8 . 1 183 . 58 GLY N N 104.0 . 1 184 . 59 ASP H H 7.03 . 1 185 . 59 ASP C C 176.1 . 1 186 . 59 ASP CA C 52.5 . 1 187 . 59 ASP N N 117.6 . 1 188 . 60 LEU H H 7.74 . 1 189 . 60 LEU C C 178.6 . 1 190 . 60 LEU CA C 57.9 . 1 191 . 60 LEU N N 125.6 . 1 192 . 61 ASN H H 8.11 . 1 193 . 61 ASN C C 179.0 . 1 194 . 61 ASN CA C 55.4 . 1 195 . 61 ASN N N 114.1 . 1 196 . 62 ALA H H 7.71 . 1 197 . 62 ALA C C 177.7 . 1 198 . 62 ALA CA C 52.2 . 1 199 . 62 ALA N N 120.7 . 1 200 . 63 LEU H H 6.95 . 1 201 . 63 LEU C C 177.4 . 1 202 . 63 LEU CA C 55.7 . 1 203 . 63 LEU N N 118.5 . 1 204 . 64 THR H H 8.06 . 1 205 . 64 THR C C 177.4 . 1 206 . 64 THR CA C 52.6 . 1 207 . 64 THR N N 120.5 . 1 208 . 65 ARG H H 8.06 . 1 209 . 65 ARG C C 177.2 . 1 210 . 65 ARG CA C 55.7 . 1 211 . 65 ARG N N 120.5 . 1 212 . 66 GLY H H 8.58 . 1 213 . 66 GLY C C 175.7 . 1 214 . 66 GLY CA C 47.0 . 1 215 . 66 GLY N N 113.7 . 1 216 . 67 GLU H H 8.66 . 1 217 . 67 GLU C C 176.8 . 1 218 . 67 GLU CA C 58.1 . 1 219 . 67 GLU N N 122.8 . 1 220 . 68 ASP H H 8.61 . 1 221 . 68 ASP C C 175.8 . 1 222 . 68 ASP CA C 54.5 . 1 223 . 68 ASP N N 117.5 . 1 224 . 69 VAL H H 7.26 . 1 225 . 69 VAL C C 175.8 . 1 226 . 69 VAL CA C 63.1 . 1 227 . 69 VAL N N 119.1 . 1 228 . 70 MET H H 8.74 . 1 229 . 70 MET C C 176.9 . 1 230 . 70 MET CA C 54.7 . 1 231 . 70 MET N N 127.8 . 1 232 . 71 CYS H H 8.71 . 1 233 . 71 CYS CA C 51.6 . 1 234 . 71 CYS N N 122.7 . 1 235 . 72 PRO C C 175.8 . 1 236 . 73 MET H H 7.62 . 1 237 . 73 MET C C 175.5 . 1 238 . 73 MET CA C 54.9 . 1 239 . 73 MET N N 117.5 . 1 240 . 74 VAL H H 8.53 . 1 241 . 74 VAL C C 174.4 . 1 242 . 74 VAL CA C 61.4 . 1 243 . 74 VAL N N 120.6 . 1 244 . 75 TYR H H 7.80 . 1 245 . 75 TYR C C 174.1 . 1 246 . 75 TYR CA C 57.9 . 1 247 . 75 TYR N N 129.2 . 1 248 . 76 ASP H H 8.44 . 1 249 . 76 ASP CA C 52.4 . 1 250 . 76 ASP N N 127.0 . 1 251 . 77 PRO C C 177.5 . 1 252 . 77 PRO CA C 63.7 . 1 253 . 78 VAL H H 8.33 . 1 254 . 78 VAL C C 172.5 . 1 255 . 78 VAL CA C 59.4 . 1 256 . 78 VAL N N 114.5 . 1 257 . 79 LEU H H 8.76 . 1 258 . 79 LEU C C 175.5 . 1 259 . 79 LEU CA C 53.1 . 1 260 . 79 LEU N N 125.1 . 1 261 . 80 LEU H H 9.17 . 1 262 . 80 LEU C C 176.3 . 1 263 . 80 LEU CA C 53.0 . 1 264 . 80 LEU N N 133.1 . 1 265 . 81 THR H H 8.99 . 1 266 . 81 THR C C 173.8 . 1 267 . 81 THR CA C 60.2 . 1 268 . 81 THR N N 114.6 . 1 269 . 82 VAL H H 8.86 . 1 270 . 82 VAL C C 174.1 . 1 271 . 82 VAL CA C 62.4 . 1 272 . 82 VAL N N 120.0 . 1 273 . 83 ASP H H 8.73 . 1 274 . 83 ASP C C 174.2 . 1 275 . 83 ASP CA C 53.5 . 1 276 . 83 ASP N N 123.3 . 1 277 . 84 GLY H H 8.37 . 1 278 . 84 GLY C C 172.2 . 1 279 . 84 GLY CA C 45.9 . 1 280 . 84 GLY N N 105.4 . 1 281 . 85 VAL H H 9.52 . 1 282 . 85 VAL C C 173.0 . 1 283 . 85 VAL CA C 59.3 . 1 284 . 85 VAL N N 123.9 . 1 285 . 86 TRP H H 9.55 . 1 286 . 86 TRP C C 174.7 . 1 287 . 86 TRP CA C 56.6 . 1 288 . 86 TRP N N 125.2 . 1 289 . 87 GLN H H 8.33 . 1 290 . 87 GLN C C 176.1 . 1 291 . 87 GLN CA C 56.6 . 1 292 . 87 GLN N N 128.6 . 1 293 . 88 GLY H H 8.31 . 1 294 . 88 GLY C C 177.0 . 1 295 . 88 GLY CA C 46.7 . 1 296 . 88 GLY N N 101.1 . 1 297 . 89 LYS H H 8.10 . 1 298 . 89 LYS C C 176.2 . 1 299 . 89 LYS CA C 54.8 . 1 300 . 89 LYS N N 120.8 . 1 301 . 90 ARG H H 9.00 . 1 302 . 90 ARG C C 176.2 . 1 303 . 90 ARG CA C 58.6 . 1 304 . 90 ARG N N 123.6 . 1 305 . 91 VAL H H 8.87 . 1 306 . 91 VAL C C 174.9 . 1 307 . 91 VAL CA C 61.6 . 1 308 . 91 VAL N N 123.1 . 1 309 . 92 SER H H 8.32 . 1 310 . 92 SER C C 173.3 . 1 311 . 92 SER CA C 58.1 . 1 312 . 92 SER N N 120.6 . 1 313 . 93 TYR H H 9.23 . 1 314 . 93 TYR C C 174.1 . 1 315 . 93 TYR N N 128.9 . 1 316 . 94 GLU H H 7.79 . 1 317 . 94 GLU C C 173.8 . 1 318 . 94 GLU CA C 54.9 . 1 319 . 94 GLU N N 127.5 . 1 320 . 95 ARG H H 8.36 . 1 321 . 95 ARG C C 174.5 . 1 322 . 95 ARG CA C 56.1 . 1 323 . 95 ARG N N 124.0 . 1 324 . 96 VAL H H 8.12 . 1 325 . 96 VAL C C 172.7 . 1 326 . 96 VAL CA C 60.8 . 1 327 . 96 VAL N N 125.4 . 1 328 . 97 PHE H H 9.43 . 1 329 . 97 PHE C C 176.5 . 1 330 . 97 PHE CA C 56.8 . 1 331 . 97 PHE N N 126.4 . 1 332 . 98 SER H H 9.30 . 1 333 . 98 SER C C 176.6 . 1 334 . 98 SER CA C 56.9 . 1 335 . 98 SER N N 116.5 . 1 336 . 99 ASN H H 7.42 . 1 337 . 99 ASN C C 175.7 . 1 338 . 99 ASN CA C 52.8 . 1 339 . 99 ASN N N 106.5 . 1 340 . 100 GLU H H 9.20 . 1 341 . 100 GLU C C 172.1 . 1 342 . 100 GLU CA C 60.3 . 1 343 . 100 GLU N N 118.6 . 1 344 . 101 CYS H H 8.10 . 1 345 . 101 CYS C C 177.2 . 1 346 . 101 CYS CA C 60.4 . 1 347 . 101 CYS N N 120.8 . 1 348 . 102 GLU H H 8.43 . 1 349 . 102 GLU C C 179.2 . 1 350 . 102 GLU CA C 59.4 . 1 351 . 102 GLU N N 121.3 . 1 352 . 103 MET H H 7.27 . 1 353 . 103 MET C C 177.2 . 1 354 . 103 MET CA C 59.5 . 1 355 . 103 MET N N 119.6 . 1 356 . 104 ASN H H 7.99 . 1 357 . 104 ASN C C 176.6 . 1 358 . 104 ASN CA C 56.0 . 1 359 . 104 ASN N N 115.3 . 1 360 . 105 ALA H H 8.17 . 1 361 . 105 ALA C C 178.1 . 1 362 . 105 ALA CA C 53.6 . 1 363 . 105 ALA N N 120.0 . 1 364 . 106 HIS H H 7.78 . 1 365 . 106 HIS C C 175.0 . 1 366 . 106 HIS CA C 58.3 . 1 367 . 106 HIS N N 116.5 . 1 368 . 107 GLY H H 7.77 . 1 369 . 107 GLY C C 173.6 . 1 370 . 107 GLY CA C 47.2 . 1 371 . 107 GLY N N 105.9 . 1 372 . 108 SER H H 8.52 . 1 373 . 108 SER C C 175.8 . 1 374 . 108 SER CA C 60.2 . 1 375 . 108 SER N N 115.7 . 1 376 . 109 SER H H 8.97 . 1 377 . 109 SER C C 175.8 . 1 378 . 109 SER CA C 60.5 . 1 379 . 109 SER N N 119.3 . 1 380 . 110 VAL H H 8.36 . 1 381 . 110 VAL C C 177.0 . 1 382 . 110 VAL CA C 66.7 . 1 383 . 110 VAL N N 121.7 . 1 384 . 111 PHE H H 7.73 . 1 385 . 111 PHE C C 174.2 . 1 386 . 111 PHE CA C 53.5 . 1 387 . 111 PHE N N 116.5 . 1 388 . 112 ALA H H 7.21 . 1 389 . 112 ALA C C 174.6 . 1 390 . 112 ALA CA C 51.0 . 1 391 . 112 ALA N N 123.8 . 1 392 . 113 PHE H H 7.11 . 1 393 . 113 PHE CA C 57.4 . 1 394 . 113 PHE N N 122.0 . 1 stop_ save_