data_358 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Sequential Resonance Assignment and Secondary Structure Determination of the Ascaris Trypsin Inhibitor, a Member of a Novel Class of Proteinase Inhibitors ; _BMRB_accession_number 358 _BMRB_flat_file_name bmr358.str _Entry_type update _Submission_date 1995-07-31 _Accession_date 1996-03-25 _Entry_origination BMRB _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 Gronenborn Angela M. . 2 Nilges Michael . . 3 Peanasky Robert J. . 4 Clore G. Marius . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 369 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2010-06-11 revision BMRB 'Complete natural source information' 1999-06-14 revision BMRB 'Converted to BMRB NMR-STAR V 2.1 format' 1996-03-25 reformat BMRB 'Converted to the BMRB 1996-03-01 STAR flat-file format' 1995-07-31 original BMRB 'Last release in original BMRB flat-file format' stop_ save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full ; Gronenborn, Angela M., Nilges, Michael, Peanasky, Robert J., Clore, G. Marius, "Sequential Resonance Assignment and Secondary Structure Determination of the Ascaris Trypsin Inhibitor, a Member of a Novel Class of Proteinase Inhibitors," Biochemistry 29, 183-189 (1990). ; _Citation_title ; Sequential Resonance Assignment and Secondary Structure Determination of the Ascaris Trypsin Inhibitor, a Member of a Novel Class of Proteinase Inhibitors ; _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 Gronenborn Angela M. . 2 Nilges Michael . . 3 Peanasky Robert J. . 4 Clore G. Marius . stop_ _Journal_abbreviation Biochemistry _Journal_volume 29 _Journal_issue . _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 183 _Page_last 189 _Year 1990 _Details . save_ ################################## # Molecular system description # ################################## save_system_ascaris_trypsin_inhibitor_1 _Saveframe_category molecular_system _Mol_system_name 'ascaris trypsin inhibitor 1' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'ascaris trypsin inhibitor 1' $ascaris_trypsin_inhibitor_1 stop_ _System_molecular_weight . _System_oligomer_state ? _System_paramagnetic ? _System_thiol_state . _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_ascaris_trypsin_inhibitor_1 _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'ascaris trypsin inhibitor 1' _Molecular_mass . _Mol_thiol_state . _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 62 _Mol_residue_sequence ; EAEKCTKPNEQWTKCGGCEG TCAQKIVPCTRECKPPRCEC IASAGFVRDAQGNCIKFEDD PK ; loop_ _Residue_seq_code _Residue_label 1 GLU 2 ALA 3 GLU 4 LYS 5 CYS 6 THR 7 LYS 8 PRO 9 ASN 10 GLU 11 GLN 12 TRP 13 THR 14 LYS 15 CYS 16 GLY 17 GLY 18 CYS 19 GLU 20 GLY 21 THR 22 CYS 23 ALA 24 GLN 25 LYS 26 ILE 27 VAL 28 PRO 29 CYS 30 THR 31 ARG 32 GLU 33 CYS 34 LYS 35 PRO 36 PRO 37 ARG 38 CYS 39 GLU 40 CYS 41 ILE 42 ALA 43 SER 44 ALA 45 GLY 46 PHE 47 VAL 48 ARG 49 ASP 50 ALA 51 GLN 52 GLY 53 ASN 54 CYS 55 ILE 56 LYS 57 PHE 58 GLU 59 ASP 60 ASP 61 PRO 62 LYS stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-10-14 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 1ATA "High-Resolution Structure Of Ascaris Trypsin Inhibitor In Solution: Direct Evidence For A Ph Induced Conformational Transition " 100.00 62 98.39 98.39 2.25e-33 PDB 1ATB "High-Resolution Structure Of Ascaris Trypsin Inhibitor In Solution: Direct Evidence For A Ph Induced Conformational Transition " 100.00 62 98.39 98.39 2.25e-33 PDB 1ATD "High-Resolution Structure Of Ascaris Trypsin Inhibitor In Solution: Direct Evidence For A Ph Induced Conformational Transition " 100.00 62 98.39 98.39 2.25e-33 PDB 1ATE "High-Resolution Structure Of Ascaris Trypsin Inhibitor In Solution: Direct Evidence For A Ph Induced Conformational Transition " 100.00 62 98.39 98.39 2.25e-33 SP P19398 "RecName: Full=Trypsin inhibitor; AltName: Full=ATI" 100.00 62 98.39 98.39 2.25e-33 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species _Strain _Tissue _Fraction $ascaris_trypsin_inhibitor_1 roundworm 6252 Eukaryota Metazoa Ascaris lumbricoides suum 'whole organism' crude 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 $ascaris_trypsin_inhibitor_1 'not available' pig Sus scrofo generic plasmid . stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_one _Saveframe_category sample _Sample_type solution _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_list _Saveframe_category NMR_spectrometer _Manufacturer unknown _Model unknown _Field_strength 0 _Details 'spectrometer information not available' save_ ############################# # NMR applied experiments # ############################# save__1 _Saveframe_category NMR_applied_experiment _Sample_label $sample_one save_ ####################### # Sample conditions # ####################### save_sample_condition_set_one _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 2.4 . na temperature 313 . K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chem_shift_reference_par_set_one _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_citation_label _Correction_value_citation_label DSS H . . ppm 0 . . . . . $entry_citation $entry_citation 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_chemical_shift_assignment_data_set_one _Saveframe_category assigned_chemical_shifts _Details . loop_ _Sample_label $sample_one stop_ _Sample_conditions_label $sample_condition_set_one _Chem_shift_reference_set_label $chem_shift_reference_par_set_one _Mol_system_component_name 'ascaris trypsin inhibitor 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 . 1 GLU HA H 4.08 . 1 2 . 1 GLU HB2 H 2.17 . 1 3 . 1 GLU HB3 H 2.17 . 1 4 . 1 GLU HG2 H 2.57 . 1 5 . 1 GLU HG3 H 2.57 . 1 6 . 2 ALA H H 8.54 . 1 7 . 2 ALA HA H 4.1 . 1 8 . 2 ALA HB H 1.26 . 1 9 . 3 GLU H H 7.46 . 1 10 . 3 GLU HA H 3.99 . 1 11 . 3 GLU HB2 H 1.51 . 2 12 . 3 GLU HB3 H 1.61 . 2 13 . 3 GLU HG2 H 1.98 . 1 14 . 3 GLU HG3 H 1.98 . 1 15 . 4 LYS H H 8 . 1 16 . 4 LYS HA H 4.3 . 1 17 . 4 LYS HB2 H 1.67 . 2 18 . 4 LYS HB3 H 1.71 . 2 19 . 4 LYS HG2 H 1.28 . 1 20 . 4 LYS HG3 H 1.28 . 1 21 . 4 LYS HD2 H 1.43 . 1 22 . 4 LYS HD3 H 1.43 . 1 23 . 4 LYS HE2 H 2.77 . 1 24 . 4 LYS HE3 H 2.77 . 1 25 . 4 LYS HZ H 7.31 . 1 26 . 5 CYS H H 8.52 . 1 27 . 5 CYS HA H 5.08 . 1 28 . 5 CYS HB2 H 3.41 . 2 29 . 5 CYS HB3 H 2.85 . 2 30 . 6 THR H H 8.39 . 1 31 . 6 THR HA H 4.33 . 1 32 . 6 THR HB H 4.48 . 1 33 . 6 THR HG2 H 1.23 . 1 34 . 7 LYS H H 7.32 . 1 35 . 7 LYS HA H 4.76 . 1 36 . 7 LYS HB2 H 1.42 . 2 37 . 7 LYS HB3 H 1.92 . 2 38 . 7 LYS HG2 H 1.47 . 2 39 . 7 LYS HG3 H 1.56 . 2 40 . 7 LYS HD2 H 1.69 . 2 41 . 7 LYS HD3 H 1.8 . 2 42 . 7 LYS HE2 H 3.05 . 1 43 . 7 LYS HE3 H 3.05 . 1 44 . 7 LYS HZ H 7.56 . 1 45 . 8 PRO HA H 4.27 . 1 46 . 8 PRO HB2 H 1.83 . 2 47 . 8 PRO HB3 H 2.28 . 2 48 . 8 PRO HG2 H 2.03 . 2 49 . 8 PRO HG3 H 2.07 . 2 50 . 8 PRO HD2 H 3.87 . 2 51 . 8 PRO HD3 H 3.66 . 2 52 . 9 ASN H H 8.63 . 1 53 . 9 ASN HA H 3.79 . 1 54 . 9 ASN HB2 H 2.43 . 2 55 . 9 ASN HB3 H 1.19 . 2 56 . 9 ASN HD21 H 6.85 . 2 57 . 9 ASN HD22 H 7.03 . 2 58 . 10 GLU H H 7.24 . 1 59 . 10 GLU HA H 5.02 . 1 60 . 10 GLU HB2 H 1.82 . 2 61 . 10 GLU HB3 H 1.84 . 2 62 . 10 GLU HG2 H 2.12 . 2 63 . 10 GLU HG3 H 2.27 . 2 64 . 11 GLN H H 8.92 . 1 65 . 11 GLN HA H 4.84 . 1 66 . 11 GLN HB2 H 2.05 . 1 67 . 11 GLN HB3 H 2.05 . 1 68 . 11 GLN HG2 H 2.33 . 1 69 . 11 GLN HG3 H 2.33 . 1 70 . 12 TRP H H 9.3 . 1 71 . 12 TRP HA H 4.46 . 1 72 . 12 TRP HB2 H 3.22 . 1 73 . 12 TRP HB3 H 3.22 . 1 74 . 12 TRP HD1 H 7.08 . 1 75 . 12 TRP HE1 H 10.06 . 1 76 . 12 TRP HE3 H 7.55 . 1 77 . 12 TRP HZ2 H 7.38 . 1 78 . 12 TRP HZ3 H 7.1 . 1 79 . 12 TRP HH2 H 7.16 . 1 80 . 13 THR H H 7.9 . 1 81 . 13 THR HA H 4.4 . 1 82 . 13 THR HB H 3.94 . 1 83 . 13 THR HG2 H 1.04 . 1 84 . 14 LYS H H 8.13 . 1 85 . 14 LYS HA H 3.65 . 1 86 . 14 LYS HB2 H 1.82 . 1 87 . 14 LYS HB3 H 1.82 . 1 88 . 14 LYS HG2 H 1.49 . 2 89 . 14 LYS HG3 H 1.55 . 2 90 . 14 LYS HD2 H 1.81 . 1 91 . 14 LYS HD3 H 1.81 . 1 92 . 14 LYS HE2 H 3.12 . 1 93 . 14 LYS HE3 H 3.12 . 1 94 . 14 LYS HZ H 7.58 . 1 95 . 15 CYS H H 7.96 . 1 96 . 15 CYS HA H 4.86 . 1 97 . 15 CYS HB2 H 3.35 . 2 98 . 15 CYS HB3 H 2.92 . 2 99 . 16 GLY H H 7.89 . 1 100 . 16 GLY HA2 H 3.42 . 2 101 . 16 GLY HA3 H 3.76 . 2 102 . 17 GLY H H 8.27 . 1 103 . 17 GLY HA2 H 4.25 . 2 104 . 17 GLY HA3 H 4.12 . 2 105 . 18 CYS H H 8.64 . 1 106 . 18 CYS HA H 4.8 . 1 107 . 18 CYS HB2 H 3.19 . 2 108 . 18 CYS HB3 H 3.1 . 2 109 . 19 GLU H H 8.27 . 1 110 . 19 GLU HA H 4.46 . 1 111 . 19 GLU HB2 H 2.04 . 2 112 . 19 GLU HB3 H 2.18 . 2 113 . 19 GLU HG2 H 2.44 . 2 114 . 19 GLU HG3 H 2.67 . 2 115 . 20 GLY H H 8.68 . 1 116 . 20 GLY HA2 H 4.46 . 2 117 . 20 GLY HA3 H 4.07 . 2 118 . 21 THR H H 8.32 . 1 119 . 21 THR HA H 5.54 . 1 120 . 21 THR HB H 4.74 . 1 121 . 21 THR HG2 H 1.3 . 1 122 . 22 CYS H H 7.86 . 1 123 . 22 CYS HA H 4.74 . 1 124 . 22 CYS HB2 H 3.07 . 2 125 . 22 CYS HB3 H 3.26 . 2 126 . 23 ALA H H 7.98 . 1 127 . 23 ALA HA H 4.35 . 1 128 . 23 ALA HB H 1.43 . 1 129 . 24 GLN H H 7.59 . 1 130 . 24 GLN HA H 4.38 . 1 131 . 24 GLN HB2 H 1.91 . 2 132 . 24 GLN HB3 H 1.99 . 2 133 . 24 GLN HG2 H 1.82 . 2 134 . 24 GLN HG3 H 2.26 . 2 135 . 24 GLN HE21 H 6.85 . 2 136 . 24 GLN HE22 H 7.46 . 2 137 . 25 LYS H H 8.31 . 1 138 . 25 LYS HA H 4.06 . 1 139 . 25 LYS HB2 H 1.43 . 1 140 . 25 LYS HB3 H 1.43 . 1 141 . 25 LYS HG2 H 1.01 . 1 142 . 25 LYS HG3 H 1.01 . 1 143 . 25 LYS HD2 H 1.17 . 1 144 . 25 LYS HD3 H 1.17 . 1 145 . 25 LYS HE2 H 2.7 . 2 146 . 25 LYS HE3 H 2.66 . 2 147 . 25 LYS HZ H 7.41 . 1 148 . 26 ILE H H 7.65 . 1 149 . 26 ILE HA H 4.22 . 1 150 . 26 ILE HB H 1.75 . 1 151 . 26 ILE HG12 H 1.08 . 2 152 . 26 ILE HG13 H 1.36 . 2 153 . 26 ILE HG2 H .79 . 1 154 . 26 ILE HD1 H .79 . 1 155 . 27 VAL H H 8.13 . 1 156 . 27 VAL HA H 4.52 . 1 157 . 27 VAL HB H 2 . 1 158 . 27 VAL HG1 H .9 . 2 159 . 27 VAL HG2 H .97 . 2 160 . 28 PRO HA H 4.4 . 1 161 . 28 PRO HB2 H 1.97 . 2 162 . 28 PRO HB3 H 2.27 . 2 163 . 28 PRO HG2 H 2 . 2 164 . 28 PRO HG3 H 2.14 . 2 165 . 28 PRO HD2 H 3.82 . 2 166 . 28 PRO HD3 H 3.7 . 2 167 . 29 CYS H H 8.43 . 1 168 . 29 CYS HA H 4.92 . 1 169 . 29 CYS HB2 H 3.03 . 2 170 . 29 CYS HB3 H 3.21 . 2 171 . 30 THR H H 8.03 . 1 172 . 30 THR HA H 4.46 . 1 173 . 30 THR HB H 4.46 . 1 174 . 30 THR HG2 H 1.28 . 1 175 . 31 ARG H H 8.33 . 1 176 . 31 ARG HA H 4.29 . 1 177 . 31 ARG HB2 H 1.81 . 2 178 . 31 ARG HB3 H 1.97 . 2 179 . 31 ARG HG2 H 1.69 . 2 180 . 31 ARG HG3 H 1.73 . 2 181 . 31 ARG HD2 H 3.25 . 1 182 . 31 ARG HD3 H 3.25 . 1 183 . 31 ARG HE H 7.16 . 1 184 . 32 GLU H H 7.8 . 1 185 . 32 GLU HA H 4.37 . 1 186 . 32 GLU HB2 H 1.97 . 2 187 . 32 GLU HB3 H 2.04 . 2 188 . 32 GLU HG2 H 2.44 . 1 189 . 32 GLU HG3 H 2.44 . 1 190 . 33 CYS H H 8.56 . 1 191 . 33 CYS HA H 4.56 . 1 192 . 33 CYS HB2 H 2.99 . 2 193 . 33 CYS HB3 H 3.25 . 2 194 . 34 LYS H H 8.45 . 1 195 . 34 LYS HA H 4.59 . 1 196 . 34 LYS HB2 H 1.2 . 2 197 . 34 LYS HB3 H 2.05 . 2 198 . 34 LYS HG2 H 1.49 . 2 199 . 34 LYS HG3 H 1.51 . 2 200 . 34 LYS HD2 H 1.71 . 1 201 . 34 LYS HD3 H 1.71 . 1 202 . 34 LYS HE2 H 3.03 . 1 203 . 34 LYS HE3 H 3.03 . 1 204 . 34 LYS HZ H 7.4 . 1 205 . 35 PRO HA H 4.62 . 1 206 . 35 PRO HB2 H 1.74 . 2 207 . 35 PRO HB3 H 2.54 . 2 208 . 35 PRO HG2 H 2.04 . 2 209 . 35 PRO HG3 H 2.18 . 2 210 . 35 PRO HD2 H 3.83 . 2 211 . 35 PRO HD3 H 3.57 . 2 212 . 36 PRO HA H 4.22 . 1 213 . 36 PRO HB2 H 1.64 . 2 214 . 36 PRO HB3 H 1.96 . 2 215 . 36 PRO HG2 H 2.11 . 2 216 . 36 PRO HG3 H 2.27 . 2 217 . 36 PRO HD2 H 3.93 . 2 218 . 36 PRO HD3 H 3.66 . 2 219 . 37 ARG H H 7.26 . 1 220 . 37 ARG HA H 4.27 . 1 221 . 37 ARG HB2 H 1.69 . 2 222 . 37 ARG HB3 H 2 . 2 223 . 37 ARG HG2 H 1.3 . 2 224 . 37 ARG HG3 H 1.48 . 2 225 . 37 ARG HD2 H 3.21 . 1 226 . 37 ARG HD3 H 3.21 . 1 227 . 37 ARG HE H 6.99 . 1 228 . 38 CYS H H 8.68 . 1 229 . 38 CYS HA H 4.85 . 1 230 . 38 CYS HB2 H 3.19 . 2 231 . 38 CYS HB3 H 2.76 . 2 232 . 39 GLU H H 8.61 . 1 233 . 39 GLU HA H 4.85 . 1 234 . 39 GLU HB2 H 2.02 . 1 235 . 39 GLU HB3 H 2.02 . 1 236 . 39 GLU HG2 H 2.27 . 2 237 . 39 GLU HG3 H 2.35 . 2 238 . 40 CYS H H 9.23 . 1 239 . 40 CYS HA H 5.03 . 1 240 . 40 CYS HB2 H 2.84 . 2 241 . 40 CYS HB3 H 2.56 . 2 242 . 41 ILE H H 7.86 . 1 243 . 41 ILE HA H 4.08 . 1 244 . 41 ILE HB H 1.87 . 1 245 . 41 ILE HG12 H .88 . 2 246 . 41 ILE HG13 H 1.44 . 2 247 . 41 ILE HG2 H 1.06 . 1 248 . 41 ILE HD1 H .77 . 1 249 . 42 ALA H H 8.37 . 1 250 . 42 ALA HA H 4.57 . 1 251 . 42 ALA HB H 1.67 . 1 252 . 43 SER H H 8.9 . 1 253 . 43 SER HA H 4.24 . 1 254 . 43 SER HB2 H 3.98 . 2 255 . 43 SER HB3 H 4.06 . 2 256 . 44 ALA H H 7.13 . 1 257 . 44 ALA HA H 4.74 . 1 258 . 44 ALA HB H 1.65 . 1 259 . 45 GLY H H 8.01 . 1 260 . 45 GLY HA2 H 4.12 . 2 261 . 45 GLY HA3 H 3.75 . 2 262 . 46 PHE H H 7.49 . 1 263 . 46 PHE HA H 5.09 . 1 264 . 46 PHE HB2 H 2.63 . 2 265 . 46 PHE HB3 H 2.94 . 2 266 . 46 PHE HD1 H 7.04 . 1 267 . 46 PHE HD2 H 7.04 . 1 268 . 46 PHE HE1 H 7.32 . 1 269 . 46 PHE HE2 H 7.32 . 1 270 . 46 PHE HZ H 7.25 . 1 271 . 47 VAL H H 9.43 . 1 272 . 47 VAL HA H 4.41 . 1 273 . 47 VAL HB H 1.63 . 1 274 . 47 VAL HG1 H .71 . 2 275 . 47 VAL HG2 H .91 . 2 276 . 48 ARG H H 8.54 . 1 277 . 48 ARG HA H 4.86 . 1 278 . 48 ARG HB2 H 1.82 . 2 279 . 48 ARG HB3 H 1.94 . 2 280 . 48 ARG HG2 H 1.71 . 2 281 . 48 ARG HG3 H 1.82 . 2 282 . 48 ARG HD2 H 2.94 . 2 283 . 48 ARG HD3 H 3.07 . 2 284 . 48 ARG HE H 7.86 . 1 285 . 49 ASP H H 8.98 . 1 286 . 49 ASP HA H 4.92 . 1 287 . 49 ASP HB2 H 2.9 . 2 288 . 49 ASP HB3 H 3.82 . 2 289 . 50 ALA H H 9.03 . 1 290 . 50 ALA HA H 4.16 . 1 291 . 50 ALA HB H 1.5 . 1 292 . 51 GLN H H 7.6 . 1 293 . 51 GLN HA H 4.34 . 1 294 . 51 GLN HB2 H 2.09 . 2 295 . 51 GLN HB3 H 2.25 . 2 296 . 51 GLN HG2 H 2.41 . 2 297 . 51 GLN HG3 H 2.55 . 2 298 . 52 GLY H H 8.17 . 1 299 . 52 GLY HA2 H 4.34 . 2 300 . 52 GLY HA3 H 3.64 . 2 301 . 53 ASN H H 7.85 . 1 302 . 53 ASN HA H 4.95 . 1 303 . 53 ASN HB2 H 2.64 . 2 304 . 53 ASN HB3 H 2.74 . 2 305 . 53 ASN HD21 H 7.13 . 2 306 . 53 ASN HD22 H 7.76 . 2 307 . 54 CYS H H 9.2 . 1 308 . 54 CYS HA H 5.44 . 1 309 . 54 CYS HB2 H 2.9 . 2 310 . 54 CYS HB3 H 2.65 . 2 311 . 55 ILE H H 9.63 . 1 312 . 55 ILE HA H 4.99 . 1 313 . 55 ILE HB H 1.97 . 1 314 . 55 ILE HG12 H .97 . 2 315 . 55 ILE HG13 H 1.4 . 2 316 . 55 ILE HG2 H .89 . 1 317 . 55 ILE HD1 H .88 . 1 318 . 56 LYS H H 8.73 . 1 319 . 56 LYS HA H 3.98 . 1 320 . 56 LYS HB2 H 1.63 . 2 321 . 56 LYS HB3 H 1.69 . 2 322 . 56 LYS HG2 H 1 . 2 323 . 56 LYS HG3 H 1.34 . 2 324 . 56 LYS HD2 H 1.35 . 1 325 . 56 LYS HD3 H 1.35 . 1 326 . 56 LYS HE2 H 2.85 . 1 327 . 56 LYS HE3 H 2.85 . 1 328 . 56 LYS HZ H 7.4 . 1 329 . 57 PHE H H 8.49 . 1 330 . 57 PHE HA H 4.42 . 1 331 . 57 PHE HB2 H 2.96 . 2 332 . 57 PHE HB3 H 3.14 . 2 333 . 57 PHE HD1 H 7.26 . 1 334 . 57 PHE HD2 H 7.26 . 1 335 . 57 PHE HE1 H 7.44 . 1 336 . 57 PHE HE2 H 7.44 . 1 337 . 57 PHE HZ H 7.38 . 1 338 . 58 GLU H H 8.38 . 1 339 . 58 GLU HA H 4.04 . 1 340 . 58 GLU HB2 H 1.97 . 2 341 . 58 GLU HB3 H 2.04 . 2 342 . 58 GLU HG2 H 2.34 . 2 343 . 58 GLU HG3 H 2.44 . 2 344 . 59 ASP H H 8.2 . 1 345 . 59 ASP HA H 4.85 . 1 346 . 59 ASP HB2 H 2.88 . 2 347 . 59 ASP HB3 H 3.2 . 2 348 . 60 ASP H H 7.54 . 1 349 . 60 ASP HA H 4.47 . 1 350 . 60 ASP HB2 H 2.88 . 2 351 . 60 ASP HB3 H 3.06 . 2 352 . 61 PRO HA H 4.47 . 1 353 . 61 PRO HB2 H 1.99 . 2 354 . 61 PRO HB3 H 2.37 . 2 355 . 61 PRO HG2 H 2.15 . 1 356 . 61 PRO HG3 H 2.15 . 1 357 . 61 PRO HD2 H 3.82 . 2 358 . 61 PRO HD3 H 3.93 . 2 359 . 62 LYS H H 8.45 . 1 360 . 62 LYS HA H 4.36 . 1 361 . 62 LYS HB2 H 1.79 . 2 362 . 62 LYS HB3 H 1.95 . 2 363 . 62 LYS HG2 H 1.49 . 1 364 . 62 LYS HG3 H 1.49 . 1 365 . 62 LYS HD2 H 1.62 . 1 366 . 62 LYS HD3 H 1.62 . 1 367 . 62 LYS HE2 H 3.03 . 1 368 . 62 LYS HE3 H 3.03 . 1 369 . 62 LYS HZ H 7.47 . 1 stop_ save_