data_5348 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Solution structure of ascidian trypsin inhibitor determined by nuclear magnetic resonance spectroscopy ; _BMRB_accession_number 5348 _BMRB_flat_file_name bmr5348.str _Entry_type original _Submission_date 2002-04-18 _Accession_date 2002-04-22 _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 Hemmi Hikaru . . 2 Yoshida Takuya . . 3 Kumazaki Takashi . . 4 Nemoto Nobuaki . . 5 Hasegawa Jun . . 6 Nishioka Fujio . . 7 Kyogoku Yoshimasa . . 8 Yokosawa Hideyoshi . . 9 Kobayashi Yuji . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 307 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2002-08-22 original BMRB . stop_ _Original_release_date 2002-04-22 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; Solution structure of ascidian trypsin inhibitor determined by nuclear magnetic resonance spectroscopy ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID ? loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Hemmi Hikaru . . 2 Yoshida Takuya . . 3 Kumazaki Takashi . . 4 Nemoto Nobuaki . . 5 Hasegawa Jun . . 6 Nishioka Fujio . . 7 Kyogoku Yoshimasa . . 8 Yokosawa Hideyoshi . . 9 Kobayashi Yuji . . stop_ _Journal_abbreviation Biochemistry _Journal_volume 41 _Journal_issue . _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 10657 _Page_last 10664 _Year 2002 _Details . save_ ################################## # Molecular system description # ################################## save_system_ati _Saveframe_category molecular_system _Mol_system_name 'ati monomer' _Abbreviation_common ati _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'ati monomer' $ati stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state monomer _System_paramagnetic no _System_thiol_state 'all disulfide bound' _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_ati _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'ascidian trypsin inhibitor' _Abbreviation_common ati _Molecular_mass . _Mol_thiol_state 'all disulfide bound' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 55 _Mol_residue_sequence ; AHMDCTEFNPLCRCNKMLGD LICAVIGDAKEEHRNMCALC CEHPGGFEYSNGPCE ; loop_ _Residue_seq_code _Residue_label 1 ALA 2 HIS 3 MET 4 ASP 5 CYS 6 THR 7 GLU 8 PHE 9 ASN 10 PRO 11 LEU 12 CYS 13 ARG 14 CYS 15 ASN 16 LYS 17 MET 18 LEU 19 GLY 20 ASP 21 LEU 22 ILE 23 CYS 24 ALA 25 VAL 26 ILE 27 GLY 28 ASP 29 ALA 30 LYS 31 GLU 32 GLU 33 HIS 34 ARG 35 ASN 36 MET 37 CYS 38 ALA 39 LEU 40 CYS 41 CYS 42 GLU 43 HIS 44 PRO 45 GLY 46 GLY 47 PHE 48 GLU 49 TYR 50 SER 51 ASN 52 GLY 53 PRO 54 CYS 55 GLU stop_ _Sequence_homology_query_date 2008-08-19 _Sequence_homology_query_revised_last_date 2008-08-19 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 1IW4 'Solution Structure Of Ascidian Trypsin Inhibitor' 100.00 55 100.00 100.00 2.19e-24 SWISS-PROT P16589 'Trypsin inhibitor (ATI)' 100.00 55 100.00 100.00 2.19e-24 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $ati 'Halocynthia roretzi' 7729 Eukaryota Metazoa Halocynthia roretzi 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 $ati 'purified from the natural source' . . . . . 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 _Concentration_min_value _Concentration_max_value _Isotopic_labeling $ati . mM 1.5 2.0 . stop_ save_ ############################ # Computer software used # ############################ save_NMRPipe _Saveframe_category software _Name NMRPipe _Version . loop_ _Task processing stop_ _Details . save_ save_NMRPIPP _Saveframe_category software _Name PIPP _Version . loop_ _Task assignment 'peak picking' stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model Avance _Field_strength 500 _Details . save_ save_NMR_spectrometer_2 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model DRX _Field_strength 600 _Details . save_ save_NMR_spectrometer_3 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model DMX _Field_strength 750 _Details . save_ save_NMR_spectrometer_4 _Saveframe_category NMR_spectrometer _Manufacturer JEOL _Model alpha _Field_strength 600 _Details . save_ ############################# # NMR applied experiments # ############################# save_1H-1H_NOESY_1 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-1H NOESY' _Sample_label . save_ save_1H-1H_TOCSY_2 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-1H TOCSY' _Sample_label . save_ save_1H-1H_DQFCOSY_3 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-1H DQFCOSY' _Sample_label . save_ save_1H-1H_ECOSY_4 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-1H ECOSY' _Sample_label . save_ ####################### # Sample conditions # ####################### save_Ex-cond_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 3.7 0.1 n/a temperature 303 1 K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference _Saveframe_category chemical_shift_reference _Details . loop_ _Mol_common_name _Atom_type _Atom_isotope_number _Atom_group _Chem_shift_units _Chem_shift_value _Reference_method _Reference_type _External_reference_sample_geometry _External_reference_location _External_reference_axis _Indirect_shift_ratio DSS H 1 'methyl protons' ppm 0.0 internal direct . . . 1.0 stop_ save_ ################################### # Assigned chemical shift lists # ################################### ################################################################### # Chemical Shift Ambiguity Index Value Definitions # # # # The values other than 1 are used for those atoms with different # # chemical shifts that cannot be assigned to stereospecific atoms # # or to specific residues or chains. # # # # Index Value Definition # # # # 1 Unique (including isolated methyl protons, # # geminal atoms, and geminal methyl # # groups with identical chemical shifts) # # (e.g. ILE HD11, HD12, HD13 protons) # # 2 Ambiguity of geminal atoms or geminal methyl # # proton groups (e.g. ASP HB2 and HB3 # # protons, LEU CD1 and CD2 carbons, or # # LEU HD11, HD12, HD13 and HD21, HD22, # # HD23 methyl protons) # # 3 Aromatic atoms on opposite sides of # # symmetrical rings (e.g. TYR HE1 and HE2 # # protons) # # 4 Intraresidue ambiguities (e.g. LYS HG and # # HD protons or TRP HZ2 and HZ3 protons) # # 5 Interresidue ambiguities (LYS 12 vs. LYS 27) # # 6 Intermolecular ambiguities (e.g. ASP 31 CA # # in monomer 1 and ASP 31 CA in monomer 2 # # of an asymmetrical homodimer, duplex # # DNA assignments, or other assignments # # that may apply to atoms in one or more # # molecule in the molecular assembly) # # 9 Ambiguous, specific ambiguity not defined # # # ################################################################### save_shift_set_1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Experiment_label '1H-1H NOESY' '1H-1H TOCSY' '1H-1H DQFCOSY' '1H-1H ECOSY' stop_ loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $Ex-cond_1 _Chem_shift_reference_set_label $chemical_shift_reference _Mol_system_component_name 'ati monomer' _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 ALA HA H 4.04 . 1 2 . 1 ALA HB H 0.92 . 1 3 . 2 HIS H H 9.08 . 1 4 . 2 HIS HA H 5.03 . 1 5 . 2 HIS HB2 H 3.18 . 1 6 . 2 HIS HB3 H 3.18 . 1 7 . 2 HIS HD2 H 8.66 . 1 8 . 2 HIS HE1 H 7.05 . 1 9 . 3 MET H H 8.63 . 1 10 . 3 MET HA H 4.80 . 1 11 . 3 MET HB2 H 0.91 . 2 12 . 3 MET HB3 H 1.48 . 2 13 . 3 MET HG2 H 1.85 . 2 14 . 3 MET HG3 H 2.70 . 2 15 . 4 ASP H H 8.01 . 1 16 . 4 ASP HA H 4.38 . 1 17 . 4 ASP HB2 H 2.20 . 1 18 . 4 ASP HB3 H 2.20 . 1 19 . 5 CYS H H 8.61 . 1 20 . 5 CYS HA H 4.45 . 1 21 . 5 CYS HB2 H 3.74 . 1 22 . 5 CYS HB3 H 3.74 . 1 23 . 6 THR H H 8.43 . 1 24 . 6 THR HA H 4.14 . 1 25 . 6 THR HB H 4.23 . 1 26 . 6 THR HG2 H 1.29 . 1 27 . 7 GLU H H 8.25 . 1 28 . 7 GLU HA H 4.05 . 1 29 . 7 GLU HB2 H 2.12 . 2 30 . 7 GLU HB3 H 2.29 . 2 31 . 7 GLU HG2 H 2.59 . 1 32 . 7 GLU HG3 H 2.59 . 1 33 . 8 PHE H H 7.36 . 1 34 . 8 PHE HA H 4.56 . 1 35 . 8 PHE HB2 H 3.01 . 2 36 . 8 PHE HB3 H 3.40 . 2 37 . 8 PHE HD1 H 7.31 . 1 38 . 8 PHE HD2 H 7.31 . 1 39 . 8 PHE HE1 H 7.08 . 1 40 . 8 PHE HE2 H 7.08 . 1 41 . 9 ASN H H 7.71 . 1 42 . 9 ASN HA H 4.89 . 1 43 . 9 ASN HB2 H 2.68 . 2 44 . 9 ASN HB3 H 2.81 . 2 45 . 9 ASN HD21 H 6.82 . 2 46 . 9 ASN HD22 H 7.55 . 2 47 . 10 PRO HA H 4.89 . 1 48 . 10 PRO HB2 H 2.04 . 1 49 . 10 PRO HB3 H 2.04 . 1 50 . 10 PRO HG2 H 1.81 . 1 51 . 10 PRO HG3 H 1.81 . 1 52 . 10 PRO HD2 H 3.54 . 1 53 . 10 PRO HD3 H 3.54 . 1 54 . 11 LEU H H 8.55 . 1 55 . 11 LEU HA H 4.22 . 1 56 . 11 LEU HB2 H 1.65 . 2 57 . 11 LEU HB3 H 1.74 . 2 58 . 11 LEU HG H 1.97 . 1 59 . 11 LEU HD1 H 1.07 . 1 60 . 11 LEU HD2 H 1.07 . 1 61 . 12 CYS H H 9.08 . 1 62 . 12 CYS HA H 3.91 . 1 63 . 12 CYS HB2 H 3.42 . 1 64 . 12 CYS HB3 H 3.42 . 1 65 . 13 ARG H H 8.39 . 1 66 . 13 ARG HA H 4.68 . 1 67 . 13 ARG HB2 H 1.66 . 2 68 . 13 ARG HB3 H 1.90 . 2 69 . 13 ARG HG2 H 1.54 . 1 70 . 13 ARG HG3 H 1.54 . 1 71 . 13 ARG HD2 H 3.17 . 1 72 . 13 ARG HD3 H 3.17 . 1 73 . 13 ARG HE H 7.19 . 1 74 . 14 CYS H H 7.96 . 1 75 . 14 CYS HA H 5.05 . 1 76 . 14 CYS HB2 H 2.58 . 2 77 . 14 CYS HB3 H 3.26 . 2 78 . 15 ASN H H 8.75 . 1 79 . 15 ASN HA H 4.81 . 1 80 . 15 ASN HB2 H 2.88 . 1 81 . 15 ASN HB3 H 3.04 . 1 82 . 15 ASN HD21 H 6.99 . 2 83 . 15 ASN HD22 H 7.69 . 2 84 . 16 LYS H H 8.39 . 1 85 . 16 LYS HA H 4.28 . 1 86 . 16 LYS HB2 H 1.98 . 1 87 . 16 LYS HB3 H 1.98 . 1 88 . 16 LYS HG2 H 1.43 . 1 89 . 16 LYS HG3 H 1.43 . 1 90 . 16 LYS HD2 H 1.71 . 1 91 . 16 LYS HD3 H 1.71 . 1 92 . 16 LYS HE2 H 3.00 . 1 93 . 16 LYS HE3 H 3.00 . 1 94 . 16 LYS HZ H 7.51 . 1 95 . 17 MET H H 7.83 . 1 96 . 17 MET HA H 4.35 . 1 97 . 17 MET HB2 H 2.03 . 1 98 . 17 MET HB3 H 2.03 . 1 99 . 17 MET HG2 H 2.54 . 1 100 . 17 MET HG3 H 2.54 . 1 101 . 18 LEU H H 8.44 . 1 102 . 18 LEU HA H 4.45 . 1 103 . 18 LEU HB2 H 1.44 . 1 104 . 18 LEU HB3 H 1.85 . 1 105 . 18 LEU HG H 1.75 . 1 106 . 18 LEU HD1 H 0.86 . 2 107 . 18 LEU HD2 H 0.95 . 2 108 . 19 GLY H H 8.54 . 1 109 . 19 GLY HA2 H 3.79 . 2 110 . 19 GLY HA3 H 4.52 . 2 111 . 20 ASP H H 8.31 . 1 112 . 20 ASP HA H 4.55 . 1 113 . 20 ASP HB2 H 2.64 . 1 114 . 20 ASP HB3 H 2.83 . 1 115 . 21 LEU H H 8.22 . 1 116 . 21 LEU HA H 4.39 . 1 117 . 21 LEU HB2 H 1.57 . 1 118 . 21 LEU HB3 H 1.57 . 1 119 . 21 LEU HG H 1.33 . 1 120 . 21 LEU HD1 H 0.82 . 1 121 . 21 LEU HD2 H 0.74 . 1 122 . 22 ILE H H 8.87 . 1 123 . 22 ILE HA H 5.03 . 1 124 . 22 ILE HB H 1.94 . 1 125 . 22 ILE HG12 H 1.04 . 2 126 . 22 ILE HG13 H 1.47 . 2 127 . 22 ILE HG2 H 0.92 . 1 128 . 22 ILE HD1 H 0.64 . 1 129 . 23 CYS H H 8.97 . 1 130 . 23 CYS HA H 5.12 . 1 131 . 23 CYS HB2 H 2.64 . 2 132 . 23 CYS HB3 H 3.22 . 2 133 . 24 ALA H H 9.48 . 1 134 . 24 ALA HA H 5.18 . 1 135 . 24 ALA HB H 1.06 . 1 136 . 25 VAL H H 8.69 . 1 137 . 25 VAL HA H 4.52 . 1 138 . 25 VAL HB H 2.11 . 1 139 . 25 VAL HG1 H 0.90 . 1 140 . 25 VAL HG2 H 0.90 . 1 141 . 26 ILE H H 8.48 . 1 142 . 26 ILE HA H 4.28 . 1 143 . 26 ILE HB H 1.72 . 1 144 . 26 ILE HG12 H 0.94 . 1 145 . 26 ILE HG13 H 0.94 . 1 146 . 26 ILE HG2 H 0.43 . 1 147 . 26 ILE HD1 H 0.01 . 1 148 . 27 GLY H H 8.86 . 1 149 . 27 GLY HA2 H 3.70 . 2 150 . 27 GLY HA3 H 3.99 . 2 151 . 28 ASP H H 8.68 . 1 152 . 28 ASP HA H 4.65 . 1 153 . 28 ASP HB2 H 2.90 . 2 154 . 28 ASP HB3 H 2.95 . 2 155 . 29 ALA H H 7.94 . 1 156 . 29 ALA HA H 4.69 . 1 157 . 29 ALA HB H 1.48 . 1 158 . 30 LYS H H 8.17 . 1 159 . 30 LYS HA H 5.06 . 1 160 . 30 LYS HB2 H 1.65 . 2 161 . 30 LYS HB3 H 1.81 . 2 162 . 30 LYS HG2 H 1.30 . 2 163 . 30 LYS HG3 H 1.48 . 2 164 . 30 LYS HD2 H 1.65 . 1 165 . 30 LYS HD3 H 1.65 . 1 166 . 30 LYS HE2 H 2.92 . 1 167 . 30 LYS HE3 H 2.92 . 1 168 . 30 LYS HZ H 7.52 . 1 169 . 31 GLU H H 9.34 . 1 170 . 31 GLU HA H 4.75 . 1 171 . 31 GLU HB2 H 1.81 . 2 172 . 31 GLU HB3 H 1.96 . 2 173 . 31 GLU HG2 H 2.25 . 1 174 . 31 GLU HG3 H 2.25 . 1 175 . 32 GLU H H 8.73 . 1 176 . 32 GLU HA H 5.41 . 1 177 . 32 GLU HB2 H 1.96 . 1 178 . 32 GLU HB3 H 1.96 . 1 179 . 32 GLU HG2 H 2.40 . 2 180 . 32 GLU HG3 H 2.65 . 2 181 . 33 HIS H H 9.05 . 1 182 . 33 HIS HA H 4.85 . 1 183 . 33 HIS HB2 H 2.52 . 2 184 . 33 HIS HB3 H 3.46 . 2 185 . 33 HIS HD2 H 8.62 . 1 186 . 33 HIS HE1 H 6.73 . 1 187 . 34 ARG H H 8.68 . 1 188 . 34 ARG HA H 4.99 . 1 189 . 34 ARG HB2 H 1.47 . 1 190 . 34 ARG HB3 H 1.47 . 1 191 . 34 ARG HG2 H 1.41 . 2 192 . 34 ARG HG3 H 1.71 . 2 193 . 34 ARG HD2 H 3.20 . 1 194 . 34 ARG HD3 H 3.20 . 1 195 . 34 ARG HE H 7.43 . 1 196 . 35 ASN H H 7.65 . 1 197 . 35 ASN HA H 5.02 . 1 198 . 35 ASN HB2 H 2.98 . 1 199 . 35 ASN HB3 H 2.62 . 1 200 . 35 ASN HD21 H 6.66 . 2 201 . 35 ASN HD22 H 7.58 . 2 202 . 36 MET H H 8.99 . 1 203 . 36 MET HA H 4.02 . 1 204 . 36 MET HB2 H 2.12 . 1 205 . 36 MET HB3 H 2.12 . 1 206 . 36 MET HG2 H 2.65 . 1 207 . 36 MET HG3 H 2.65 . 1 208 . 37 CYS H H 8.24 . 1 209 . 37 CYS HA H 2.32 . 1 210 . 37 CYS HB2 H 3.28 . 1 211 . 37 CYS HB3 H 3.28 . 1 212 . 38 ALA H H 8.26 . 1 213 . 38 ALA HA H 3.79 . 1 214 . 38 ALA HB H 1.28 . 1 215 . 39 LEU H H 7.45 . 1 216 . 39 LEU HA H 3.89 . 1 217 . 39 LEU HB2 H 1.27 . 1 218 . 39 LEU HB3 H 1.41 . 1 219 . 39 LEU HG H 1.00 . 1 220 . 39 LEU HD1 H -0.10 . 1 221 . 39 LEU HD2 H 0.13 . 1 222 . 40 CYS H H 8.18 . 1 223 . 40 CYS HA H 4.67 . 1 224 . 40 CYS HB2 H 2.79 . 1 225 . 40 CYS HB3 H 2.79 . 1 226 . 41 CYS H H 7.63 . 1 227 . 41 CYS HA H 4.26 . 1 228 . 41 CYS HB2 H 3.03 . 1 229 . 41 CYS HB3 H 3.29 . 1 230 . 42 GLU H H 7.20 . 1 231 . 42 GLU HA H 3.98 . 1 232 . 42 GLU HB2 H 1.58 . 2 233 . 42 GLU HB3 H 1.86 . 2 234 . 42 GLU HG2 H 2.16 . 2 235 . 42 GLU HG3 H 2.36 . 2 236 . 43 HIS H H 8.07 . 1 237 . 43 HIS HA H 5.14 . 1 238 . 43 HIS HB2 H 3.25 . 1 239 . 43 HIS HB3 H 3.25 . 1 240 . 43 HIS HD2 H 8.69 . 1 241 . 43 HIS HE1 H 6.85 . 1 242 . 44 PRO HA H 4.89 . 1 243 . 44 PRO HB2 H 2.45 . 1 244 . 44 PRO HB3 H 2.45 . 1 245 . 44 PRO HG2 H 1.95 . 2 246 . 44 PRO HG3 H 2.08 . 2 247 . 44 PRO HD2 H 3.42 . 2 248 . 44 PRO HD3 H 3.58 . 2 249 . 45 GLY H H 8.66 . 1 250 . 45 GLY HA2 H 3.86 . 2 251 . 45 GLY HA3 H 4.23 . 2 252 . 46 GLY H H 8.20 . 1 253 . 46 GLY HA2 H 3.57 . 2 254 . 46 GLY HA3 H 4.63 . 2 255 . 47 PHE H H 6.89 . 1 256 . 47 PHE HA H 5.03 . 1 257 . 47 PHE HB2 H 3.23 . 2 258 . 47 PHE HB3 H 3.42 . 2 259 . 47 PHE HD1 H 6.87 . 1 260 . 47 PHE HD2 H 6.87 . 1 261 . 47 PHE HE1 H 7.14 . 1 262 . 47 PHE HE2 H 7.14 . 1 263 . 47 PHE HZ H 6.84 . 1 264 . 48 GLU H H 9.05 . 1 265 . 48 GLU HA H 5.29 . 1 266 . 48 GLU HB2 H 2.15 . 2 267 . 48 GLU HB3 H 2.24 . 2 268 . 48 GLU HG2 H 2.53 . 1 269 . 48 GLU HG3 H 2.53 . 1 270 . 49 TYR H H 9.04 . 1 271 . 49 TYR HA H 5.70 . 1 272 . 49 TYR HB2 H 3.15 . 1 273 . 49 TYR HB3 H 2.88 . 1 274 . 49 TYR HD1 H 6.79 . 1 275 . 49 TYR HD2 H 6.79 . 1 276 . 49 TYR HE1 H 6.52 . 1 277 . 49 TYR HE2 H 6.52 . 1 278 . 50 SER H H 8.60 . 1 279 . 50 SER HA H 4.62 . 1 280 . 50 SER HB2 H 3.83 . 1 281 . 50 SER HB3 H 3.83 . 1 282 . 51 ASN H H 8.86 . 1 283 . 51 ASN HA H 4.97 . 1 284 . 51 ASN HB2 H 2.78 . 2 285 . 51 ASN HB3 H 2.92 . 2 286 . 51 ASN HD21 H 6.99 . 2 287 . 51 ASN HD22 H 7.62 . 2 288 . 52 GLY H H 8.52 . 1 289 . 52 GLY HA2 H 3.64 . 2 290 . 52 GLY HA3 H 4.50 . 2 291 . 53 PRO HA H 4.22 . 1 292 . 53 PRO HB2 H 2.25 . 1 293 . 53 PRO HB3 H 2.25 . 1 294 . 53 PRO HG2 H 1.95 . 1 295 . 53 PRO HG3 H 1.95 . 1 296 . 53 PRO HD2 H 3.49 . 2 297 . 53 PRO HD3 H 3.63 . 2 298 . 54 CYS H H 8.75 . 1 299 . 54 CYS HA H 4.75 . 1 300 . 54 CYS HB2 H 2.82 . 2 301 . 54 CYS HB3 H 3.06 . 2 302 . 55 GLU H H 8.07 . 1 303 . 55 GLU HA H 4.28 . 1 304 . 55 GLU HB2 H 1.92 . 2 305 . 55 GLU HB3 H 2.14 . 2 306 . 55 GLU HG2 H 2.36 . 1 307 . 55 GLU HG3 H 2.36 . 1 stop_ save_