data_7135 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Assignments of 2SSalpha in 8M urea, pH 2, 293 K ; _BMRB_accession_number 7135 _BMRB_flat_file_name bmr7135.str _Entry_type original _Submission_date 2006-06-01 _Accession_date 2006-06-01 _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 Collins Emily S. . 2 Wirmer Julia . . 3 Hirai Kenichi . . 4 Tachibana Hideki . . 5 Segawa Shin-ichi . . 6 Dobson Christopher M. . 7 Schwalbe Harald . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 216 "15N chemical shifts" 108 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2008-11-12 original author . stop_ _Original_release_date 2008-11-12 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title 'Characterisation of Disulfide Bond Dynamics in Non-Native States of Lysozyme and its Disulfide Deletion Mutants by NMR' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 16138305 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Collins Emily S. . 2 Wirmer Julia . . 3 Hirai Kenichi . . 4 Tachibana Hideki . . 5 Segawa Shin-ichi . . 6 Dobson Christopher M. . 7 Schwalbe Harald . . stop_ _Journal_abbreviation ChemBioChem _Journal_volume 6 _Journal_issue 9 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 1619 _Page_last 1627 _Year 2005 _Details . save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name 2SS(alpha) _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 2SS(alpha) $2SS(alpha) stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state ? _System_paramagnetic no _System_thiol_state unknown _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_2SS(alpha) _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 2SS(alpha) _Molecular_mass . _Mol_thiol_state unknown _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 129 _Mol_residue_sequence ; KVFGRCELAAAMKRHGLDNY RGYSLGNWVCAAKFESNFNT EATNRNTDGSTDYGILQINS RWWANDGRTPGSRNLANIPA SALLSSDITASVNAAKKIVS DGNGMNAWVAWRNRCKGTDV EAWIRGCRL ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 1 LYS 2 2 VAL 3 3 PHE 4 4 GLY 5 5 ARG 6 6 CYS 7 7 GLU 8 8 LEU 9 9 ALA 10 10 ALA 11 11 ALA 12 12 MET 13 13 LYS 14 14 ARG 15 15 HIS 16 16 GLY 17 17 LEU 18 18 ASP 19 19 ASN 20 20 TYR 21 21 ARG 22 22 GLY 23 23 TYR 24 24 SER 25 25 LEU 26 26 GLY 27 27 ASN 28 28 TRP 29 29 VAL 30 30 CYS 31 31 ALA 32 32 ALA 33 33 LYS 34 34 PHE 35 35 GLU 36 36 SER 37 37 ASN 38 38 PHE 39 39 ASN 40 40 THR 41 41 GLU 42 42 ALA 43 43 THR 44 44 ASN 45 45 ARG 46 46 ASN 47 47 THR 48 48 ASP 49 49 GLY 50 50 SER 51 51 THR 52 52 ASP 53 53 TYR 54 54 GLY 55 55 ILE 56 56 LEU 57 57 GLN 58 58 ILE 59 59 ASN 60 60 SER 61 61 ARG 62 62 TRP 63 63 TRP 64 64 ALA 65 65 ASN 66 66 ASP 67 67 GLY 68 68 ARG 69 69 THR 70 70 PRO 71 71 GLY 72 72 SER 73 73 ARG 74 74 ASN 75 75 LEU 76 76 ALA 77 77 ASN 78 78 ILE 79 79 PRO 80 80 ALA 81 81 SER 82 82 ALA 83 83 LEU 84 84 LEU 85 85 SER 86 86 SER 87 87 ASP 88 88 ILE 89 89 THR 90 90 ALA 91 91 SER 92 92 VAL 93 93 ASN 94 94 ALA 95 95 ALA 96 96 LYS 97 97 LYS 98 98 ILE 99 99 VAL 100 100 SER 101 101 ASP 102 102 GLY 103 103 ASN 104 104 GLY 105 105 MET 106 106 ASN 107 107 ALA 108 108 TRP 109 109 VAL 110 110 ALA 111 111 TRP 112 112 ARG 113 113 ASN 114 114 ARG 115 115 CYS 116 116 LYS 117 117 GLY 118 118 THR 119 119 ASP 120 120 VAL 121 121 GLU 122 122 ALA 123 123 TRP 124 124 ILE 125 125 ARG 126 126 GLY 127 127 CYS 128 128 ARG 129 129 LEU stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2014-05-12 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 BMRB 11459 1SS[6-127] 100.00 130 96.90 98.45 7.78e-85 BMRB 11460 1SS[30-115] 100.00 130 96.90 98.45 8.49e-85 BMRB 5069 2SS(6-127_30-115) 100.00 130 98.45 100.00 7.51e-87 BMRB 5803 HEWL 100.00 130 96.90 98.45 2.73e-85 BMRB 5804 HEWL 100.00 130 96.90 98.45 2.73e-85 BMRB 7159 2SS[6-127,_30-115] 100.00 129 98.45 100.00 1.01e-86 PDB 3ZVQ "Crystal Structure Of Proteolyzed Lysozyme" 54.26 70 97.14 98.57 3.18e-42 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species _Details $2SS(alpha) Hen 9031 Eukaryota Metazoa Gallus gallus egg-white 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 $2SS(alpha) 'recombinant technology' . . . . . 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 $2SS(alpha) 1 mM . urea 8 M . D2O 10 % . stop_ save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer unknown _Model unknown _Field_strength 0 _Details 'spectrometer information not available' save_ ############################# # NMR applied experiments # ############################# save_unknown_1 _Saveframe_category NMR_applied_experiment _Experiment_name unknown _Sample_label $sample_1 save_ save_NMR_spec_expt _Saveframe_category NMR_applied_experiment _Experiment_name unknown _BMRB_pulse_sequence_accession_number . _Details 'experiment information not available' save_ ####################### # Sample conditions # ####################### save_conditions_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 2 0 pH temperature 293 0 K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_referencing _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 _Indirect_shift_ratio_citation_label _Correction_value_citation_label DSS H 1 'methyl protons' ppm 0.0 internal direct . . . 1.000000000 $entry_citation $entry_citation DSS N 15 'methyl protons' ppm 0.0 . indirect . . . 0.101329118 $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_chem_shift_list_1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Experiment_label unknown stop_ loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $conditions_1 _Chem_shift_reference_set_label $chemical_shift_referencing _Mol_system_component_name 2SS(alpha) _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 3 3 PHE HA H 4.57 . . 2 4 4 GLY H H 8.36 . . 3 4 4 GLY HA2 H 3.92 . . 4 4 4 GLY N N 110.75 . . 5 5 5 ARG H H 8.28 . . 6 5 5 ARG HA H 4.29 . . 7 5 5 ARG N N 120.98 . . 8 6 6 CYS H H 8.60 . . 9 6 6 CYS HA H 4.60 . . 10 6 6 CYS N N 120.13 . . 11 8 8 LEU H H 8.27 . . 12 8 8 LEU HA H 4.32 . . 13 8 8 LEU N N 124.25 . . 14 9 9 ALA H H 8.27 . . 15 9 9 ALA HA H 4.22 . . 16 9 9 ALA N N 125.25 . . 17 10 10 ALA H H 8.20 . . 18 10 10 ALA HA H 4.24 . . 19 10 10 ALA N N 124.00 . . 20 11 11 ALA H H 8.12 . . 21 11 11 ALA HA H 4.17 . . 22 11 11 ALA N N 122.81 . . 23 12 12 MET H H 8.17 . . 24 12 12 MET HA H 4.21 . . 25 12 12 MET N N 119.67 . . 26 13 13 LYS H H 8.31 . . 27 13 13 LYS HA H 4.30 . . 28 13 13 LYS N N 123.03 . . 29 14 14 ARG H H 8.30 . . 30 14 14 ARG HA H 4.21 . . 31 14 14 ARG N N 122.54 . . 32 15 15 HIS H H 8.61 . . 33 15 15 HIS HA H 4.66 . . 34 15 15 HIS N N 119.98 . . 35 16 16 GLY H H 8.42 . . 36 16 16 GLY HA2 H 3.92 . . 37 16 16 GLY N N 110.71 . . 38 17 17 LEU H H 8.22 . . 39 17 17 LEU HA H 4.30 . . 40 17 17 LEU N N 122.01 . . 41 18 18 ASP H H 8.55 . . 42 18 18 ASP HA H 4.62 . . 43 18 18 ASP N N 119.85 . . 44 19 19 ASN H H 8.37 . . 45 19 19 ASN HA H 4.62 . . 46 19 19 ASN N N 119.83 . . 47 20 20 TYR H H 8.05 . . 48 20 20 TYR HA H 4.46 . . 49 20 20 TYR N N 121.19 . . 50 21 21 ARG H H 8.27 . . 51 21 21 ARG HA H 4.17 . . 52 21 21 ARG N N 123.91 . . 53 22 22 GLY H H 7.68 . . 54 22 22 GLY HA2 H 3.75 . . 55 22 22 GLY N N 109.28 . . 56 23 23 TYR H H 7.98 . . 57 23 23 TYR HA H 4.53 . . 58 23 23 TYR N N 120.18 . . 59 24 24 SER H H 8.33 . . 60 24 24 SER HA H 4.51 . . 61 24 24 SER N N 118.03 . . 62 25 25 LEU H H 8.22 . . 63 25 25 LEU HA H 4.27 . . 64 25 25 LEU N N 124.68 . . 65 26 26 GLY H H 8.19 . . 66 26 26 GLY HA2 H 3.73 . . 67 26 26 GLY N N 108.97 . . 68 27 27 ASN H H 8.17 . . 69 27 27 ASN HA H 4.60 . . 70 27 27 ASN N N 118.98 . . 71 28 28 TRP H H 8.02 . . 72 28 28 TRP HA H 4.55 . . 73 28 28 TRP N N 121.93 . . 74 29 29 VAL H H 7.98 . . 75 29 29 VAL N N 121.13 . . 76 30 30 CYS H H 8.29 . . 77 30 30 CYS N N 123.74 . . 78 31 31 ALA H H 8.15 . . 79 31 31 ALA HA H 4.25 . . 80 31 31 ALA N N 126.64 . . 81 32 32 ALA H H 8.13 . . 82 32 32 ALA HA H 4.19 . . 83 32 32 ALA N N 123.99 . . 84 33 33 LYS H H 8.19 . . 85 33 33 LYS HA H 4.58 . . 86 33 33 LYS N N 120.69 . . 87 34 34 PHE H H 8.21 . . 88 34 34 PHE HA H 4.53 . . 89 34 34 PHE N N 121.73 . . 90 35 35 GLU H H 8.22 . . 91 35 35 GLU HA H 4.30 . . 92 35 35 GLU N N 122.78 . . 93 36 36 SER H H 8.29 . . 94 36 36 SER HA H 4.33 . . 95 36 36 SER N N 117.48 . . 96 37 37 ASN H H 8.43 . . 97 37 37 ASN HA H 4.65 . . 98 37 37 ASN N N 120.99 . . 99 38 38 PHE H H 8.19 . . 100 38 38 PHE HA H 4.35 . . 101 38 38 PHE N N 120.94 . . 102 39 39 ASN H H 8.39 . . 103 39 39 ASN HA H 4.68 . . 104 39 39 ASN N N 120.90 . . 105 40 40 THR H H 8.12 . . 106 40 40 THR HA H 4.24 . . 107 40 40 THR N N 114.80 . . 108 41 41 GLU H H 8.36 . . 109 41 41 GLU HA H 4.23 . . 110 41 41 GLU N N 122.39 . . 111 42 42 ALA H H 8.27 . . 112 42 42 ALA HA H 4.24 . . 113 42 42 ALA N N 125.47 . . 114 43 43 THR H H 8.09 . . 115 43 43 THR HA H 4.26 . . 116 43 43 THR N N 113.23 . . 117 44 44 ASN H H 8.39 . . 118 44 44 ASN HA H 4.74 . . 119 44 44 ASN N N 121.42 . . 120 45 45 ARG H H 8.35 . . 121 45 45 ARG HA H 4.23 . . 122 45 45 ARG N N 121.98 . . 123 46 46 ASN H H 8.49 . . 124 46 46 ASN HA H 4.71 . . 125 46 46 ASN N N 120.27 . . 126 47 47 THR H H 8.15 . . 127 47 47 THR HA H 4.29 . . 128 47 47 THR N N 114.32 . . 129 48 48 ASP H H 8.48 . . 130 48 48 ASP HA H 4.73 . . 131 48 48 ASP N N 121.14 . . 132 49 49 GLY H H 8.32 . . 133 49 49 GLY HA2 H 3.93 . . 134 49 49 GLY N N 109.70 . . 135 50 50 SER H H 8.17 . . 136 50 50 SER HA H 4.44 . . 137 50 50 SER N N 115.83 . . 138 51 51 THR H H 8.23 . . 139 51 51 THR HA H 4.21 . . 140 51 51 THR N N 116.06 . . 141 52 52 ASP H H 8.37 . . 142 52 52 ASP HA H 4.66 . . 143 52 52 ASP N N 121.54 . . 144 53 53 TYR H H 8.14 . . 145 53 53 TYR HA H 4.43 . . 146 53 53 TYR N N 121.41 . . 147 54 54 GLY H H 8.22 . . 148 54 54 GLY HA2 H 3.83 . . 149 54 54 GLY N N 110.20 . . 150 55 55 ILE H H 7.88 . . 151 55 55 ILE HA H 4.10 . . 152 55 55 ILE N N 120.16 . . 153 56 56 LEU H H 8.23 . . 154 56 56 LEU HA H 4.28 . . 155 56 56 LEU N N 126.35 . . 156 57 57 GLN H H 8.41 . . 157 57 57 GLN HA H 4.28 . . 158 57 57 GLN N N 122.78 . . 159 58 58 ILE H H 8.25 . . 160 58 58 ILE HA H 4.06 . . 161 58 58 ILE N N 122.79 . . 162 59 59 ASN H H 8.44 . . 163 59 59 ASN HA H 4.70 . . 164 59 59 ASN N N 123.24 . . 165 60 60 SER H H 8.25 . . 166 60 60 SER HA H 4.22 . . 167 60 60 SER N N 117.08 . . 168 61 61 ARG H H 8.44 . . 169 61 61 ARG HA H 4.00 . . 170 61 61 ARG N N 122.81 . . 171 62 62 TRP H H 7.86 . . 172 62 62 TRP HA H 4.47 . . 173 62 62 TRP N N 121.51 . . 174 63 63 TRP H H 7.48 . . 175 63 63 TRP HA H 4.43 . . 176 63 63 TRP N N 122.01 . . 177 64 64 ALA H H 7.77 . . 178 64 64 ALA HA H 4.04 . . 179 64 64 ALA N N 125.10 . . 180 65 65 ASN H H 7.99 . . 181 65 65 ASN HA H 4.54 . . 182 65 65 ASN N N 117.92 . . 183 66 66 ASP HA H 4.62 . . 184 67 67 GLY H H 8.29 . . 185 67 67 GLY HA2 H 3.82 . . 186 67 67 GLY N N 108.94 . . 187 71 71 GLY H H 8.37 . . 188 71 71 GLY HA2 H 3.89 . . 189 71 71 GLY N N 109.63 . . 190 72 72 SER H H 8.12 . . 191 72 72 SER HA H 4.38 . . 192 72 72 SER N N 115.85 . . 193 73 73 ARG H H 8.44 . . 194 73 73 ARG HA H 4.33 . . 195 73 73 ARG N N 123.18 . . 196 77 77 ASN HA H 4.60 . . 197 78 78 ILE H H 7.98 . . 198 78 78 ILE HA H 4.36 . . 199 78 78 ILE N N 122.58 . . 200 80 80 ALA H H 8.29 . . 201 80 80 ALA HA H 4.34 . . 202 80 80 ALA N N 116.79 . . 203 81 81 SER H H 8.20 . . 204 81 81 SER HA H 4.18 . . 205 81 81 SER N N 114.10 . . 206 84 84 LEU H H 8.12 . . 207 84 84 LEU HA H 4.40 . . 208 84 84 LEU N N 121.88 . . 209 85 85 SER H H 8.18 . . 210 85 85 SER HA H 4.34 . . 211 85 85 SER N N 115.88 . . 212 88 88 ILE H H 7.98 . . 213 88 88 ILE HA H 4.26 . . 214 88 88 ILE N N 121.13 . . 215 89 89 THR H H 8.27 . . 216 89 89 THR HA H 4.30 . . 217 89 89 THR N N 115.87 . . 218 90 90 ALA H H 8.11 . . 219 90 90 ALA HA H 4.30 . . 220 90 90 ALA N N 126.07 . . 221 91 91 SER H H 8.14 . . 222 91 91 SER HA H 4.30 . . 223 91 91 SER N N 118.13 . . 224 92 92 VAL H H 8.01 . . 225 92 92 VAL HA H 4.14 . . 226 92 92 VAL N N 121.48 . . 227 93 93 ASN H H 8.34 . . 228 93 93 ASN HA H 4.68 . . 229 93 93 ASN N N 121.24 . . 230 97 97 LYS H H 8.13 . . 231 97 97 LYS HA H 4.21 . . 232 97 97 LYS N N 121.20 . . 233 98 98 ILE H H 8.35 . . 234 98 98 ILE HA H 4.23 . . 235 98 98 ILE N N 124.29 . . 236 99 99 VAL H H 8.29 . . 237 99 99 VAL HA H 4.12 . . 238 99 99 VAL N N 125.68 . . 239 100 100 SER H H 8.42 . . 240 100 100 SER HA H 4.45 . . 241 100 100 SER N N 120.20 . . 242 101 101 ASP H H 8.52 . . 243 101 101 ASP HA H 4.69 . . 244 101 101 ASP N N 121.91 . . 245 102 102 GLY H H 8.34 . . 246 102 102 GLY HA2 H 3.88 . . 247 102 102 GLY N N 109.57 . . 248 103 103 ASN H H 8.30 . . 249 103 103 ASN HA H 4.68 . . 250 103 103 ASN N N 118.94 . . 251 104 104 GLY H H 8.38 . . 252 104 104 GLY HA2 H 3.90 . . 253 104 104 GLY N N 109.56 . . 254 105 105 MET H H 8.21 . . 255 105 105 MET HA H 4.35 . . 256 105 105 MET N N 120.10 . . 257 106 106 ASN H H 8.46 . . 258 106 106 ASN HA H 4.57 . . 259 106 106 ASN N N 120.08 . . 260 107 107 ALA H H 8.17 . . 261 107 107 ALA HA H 4.14 . . 262 107 107 ALA N N 124.48 . . 263 108 108 TRP H H 8.09 . . 264 108 108 TRP HA H 4.53 . . 265 108 108 TRP N N 120.53 . . 266 109 109 VAL H H 7.77 . . 267 109 109 VAL HA H 3.80 . . 268 109 109 VAL N N 122.12 . . 269 110 110 ALA H H 8.01 . . 270 110 110 ALA HA H 4.06 . . 271 110 110 ALA N N 126.42 . . 272 111 111 TRP H H 7.96 . . 273 111 111 TRP HA H 4.46 . . 274 111 111 TRP N N 120.35 . . 275 112 112 ARG H H 7.94 . . 276 112 112 ARG HA H 4.00 . . 277 112 112 ARG N N 121.88 . . 278 113 113 ASN H H 8.06 . . 279 113 113 ASN HA H 4.49 . . 280 113 113 ASN N N 119.10 . . 281 114 114 ARG H H 8.36 . . 282 114 114 ARG HA H 4.05 . . 283 114 114 ARG N N 122.02 . . 284 115 115 CYS H H 8.34 . . 285 115 115 CYS HA H 4.61 . . 286 115 115 CYS N N 119.32 . . 287 117 117 GLY H H 8.32 . . 288 117 117 GLY HA2 H 3.92 . . 289 117 117 GLY N N 110.76 . . 290 118 118 THR H H 8.04 . . 291 118 118 THR HA H 4.32 . . 292 118 118 THR N N 113.68 . . 293 119 119 ASP H H 8.51 . . 294 119 119 ASP HA H 4.75 . . 295 119 119 ASP N N 121.93 . . 296 120 120 VAL H H 8.07 . . 297 120 120 VAL HA H 3.99 . . 298 120 120 VAL N N 121.13 . . 299 121 121 GLU H H 8.34 . . 300 121 121 GLU HA H 4.23 . . 301 121 121 GLU N N 123.90 . . 302 122 122 ALA H H 8.15 . . 303 122 122 ALA HA H 4.20 . . 304 122 122 ALA N N 125.04 . . 305 123 123 TRP H H 8.05 . . 306 123 123 TRP HA H 4.67 . . 307 123 123 TRP N N 120.53 . . 308 124 124 ILE H H 8.02 . . 309 124 124 ILE HA H 4.06 . . 310 124 124 ILE N N 123.22 . . 311 125 125 ARG H H 8.25 . . 312 125 125 ARG HA H 4.16 . . 313 125 125 ARG N N 125.33 . . 314 126 126 GLY H H 8.29 . . 315 126 126 GLY HA2 H 3.98 . . 316 126 126 GLY N N 110.05 . . 317 127 127 CYS H H 8.22 . . 318 127 127 CYS HA H 4.61 . . 319 127 127 CYS N N 118.98 . . 320 128 128 ARG H H 8.55 . . 321 128 128 ARG HA H 4.28 . . 322 128 128 ARG N N 124.00 . . 323 129 129 LEU H H 8.42 . . 324 129 129 LEU N N 125.41 . . stop_ save_