data_7136 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Assignments of 2SSbeta in 8M urea, pH 2, 293 K ; _BMRB_accession_number 7136 _BMRB_flat_file_name bmr7136.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" 189 "13C chemical shifts" 76 "15N chemical shifts" 96 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(beta) _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 2SS(beta) $2SS(beta) 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(beta) _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 2SS(beta) _Molecular_mass . _Mol_thiol_state unknown _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 129 _Mol_residue_sequence ; KVFGRSELAAAMKRHGLDNY RGYSLGNWVAAAKFESNFNT EATNRNTDGSTDYGILQINS RWWCNDGRTPGSRNLCNIPC SALLSSDITASVNCAKKIVS DGNGMNAWVAWRNRAKGTDV QAWIRGARL ; 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 SER 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 ALA 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 CYS 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 CYS 77 77 ASN 78 78 ILE 79 79 PRO 80 80 CYS 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 CYS 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 ALA 116 116 LYS 117 117 GLY 118 118 THR 119 119 ASP 120 120 VAL 121 121 GLN 122 122 ALA 123 123 TRP 124 124 ILE 125 125 ARG 126 126 GLY 127 127 ALA 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 11461 1SS[64-80] 100.00 130 97.67 98.45 2.39e-85 BMRB 11462 1SS[76-94] 100.00 130 97.67 98.45 2.39e-85 BMRB 4831 lysozyme 100.00 129 96.90 96.90 9.37e-85 BMRB 6415 C30A/C115A 100.00 130 97.67 98.45 9.89e-86 BMRB 7143 HEWL 100.00 129 96.90 96.90 9.37e-85 BMRB 7144 HEWL 100.00 129 96.90 96.90 9.37e-85 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $2SS(beta) Hen 9031 Eukaryota Metazoa Gallus gallus 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(beta) '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(beta) 300 uM . 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(beta) _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 1 LYS H H 8.7 . . 2 1 1 LYS HA H 4.35 . . 3 1 1 LYS CA C 56.55 . . 4 1 1 LYS N N 125.42 . . 5 2 2 VAL H H 8.27 . . 6 2 2 VAL HA H 4.08 . . 7 2 2 VAL CA C 62.17 . . 8 2 2 VAL N N 123.17 . . 9 3 3 PHE H H 8.53 . . 10 3 3 PHE HA H 4.61 . . 11 3 3 PHE CA C 58.00 . . 12 3 3 PHE N N 125.79 . . 13 4 4 GLY H H 8.37 . . 14 4 4 GLY HA2 H 3.92 . . 15 4 4 GLY N N 111.30 . . 16 5 5 ARG H H 8.32 . . 17 5 5 ARG HA H 4.32 . . 18 5 5 ARG CA C 56.87 . . 19 5 5 ARG N N 121.33 . . 20 6 6 SER H H 8.17 . . 21 6 6 SER HA H 4.32 . . 22 6 6 SER CA C 59.22 . . 23 6 6 SER N N 123.39 . . 24 7 7 GLU H H 8.42 . . 25 7 7 GLU HA H 4.39 . . 26 7 7 GLU CA C 56.69 . . 27 7 7 GLU N N 123.30 . . 28 8 8 LEU H H 8.17 . . 29 8 8 LEU HA H 4.30 . . 30 8 8 LEU CA C 56.06 . . 31 8 8 LEU N N 123.35 . . 32 9 9 ALA H H 8.19 . . 33 9 9 ALA HA H 4.24 . . 34 9 9 ALA CA C 53.55 . . 35 9 9 ALA N N 124.45 . . 36 10 10 ALA H H 8.15 . . 37 10 10 ALA HA H 4.18 . . 38 10 10 ALA CA C 53.55 . . 39 10 10 ALA N N 122.70 . . 40 12 12 MET H H 8.10 . . 41 12 12 MET HA H 4.35 . . 42 12 12 MET CA C 56.32 . . 43 12 12 MET N N 119.11 . . 44 13 13 LYS H H 8.19 . . 45 13 13 LYS HA H 4.21 . . 46 13 13 LYS CA C 56.94 . . 47 13 13 LYS N N 120.82 . . 48 14 14 ARG H H 8.19 . . 49 14 14 ARG HA H 4.25 . . 50 14 14 ARG CA C 56.55 . . 51 14 14 ARG N N 121.80 . . 52 15 15 HIS H H 8.49 . . 53 15 15 HIS HA H 4.66 . . 54 15 15 HIS CA C 55.64 . . 55 15 15 HIS N N 119.72 . . 56 16 16 GLY H H 8.44 . . 57 16 16 GLY HA2 H 3.95 . . 58 16 16 GLY N N 110.59 . . 59 17 17 LEU H H 8.21 . . 60 17 17 LEU HA H 4.32 . . 61 17 17 LEU CA C 55.45 . . 62 17 17 LEU N N 122.08 . . 63 18 18 ASP H H 8.55 . . 64 18 18 ASP HA H 4.63 . . 65 18 18 ASP CA C 53.25 . . 66 18 18 ASP N N 119.93 . . 67 19 19 ASN H H 8.29 . . 68 19 19 ASN HA H 4.64 . . 69 19 19 ASN CA C 53.34 . . 70 19 19 ASN N N 119.63 . . 71 20 20 TYR H H 8.05 . . 72 20 20 TYR HA H 4.49 . . 73 20 20 TYR CA C 58.41 . . 74 20 20 TYR N N 121.18 . . 75 21 21 ARG H H 8.23 . . 76 21 21 ARG HA H 4.20 . . 77 21 21 ARG CA C 56.44 . . 78 21 21 ARG N N 124.02 . . 79 22 22 GLY H H 7.76 . . 80 22 22 GLY HA2 H 3.82 . . 81 22 22 GLY N N 109.31 . . 82 23 23 TYR H H 7.96 . . 83 23 23 TYR HA H 4.57 . . 84 23 23 TYR CA C 58.11 . . 85 23 23 TYR N N 120.39 . . 86 24 24 SER H H 8.25 . . 87 24 24 SER HA H 4.42 . . 88 24 24 SER CA C 58.27 . . 89 24 24 SER N N 118.22 . . 90 25 25 LEU H H 8.22 . . 91 25 25 LEU HA H 4.25 . . 92 25 25 LEU CA C 55.82 . . 93 25 25 LEU N N 124.59 . . 94 26 26 GLY H H 8.25 . . 95 26 26 GLY HA2 H 3.82 . . 96 26 26 GLY N N 109.03 . . 97 27 27 ASN H H 8.20 . . 98 27 27 ASN HA H 4.67 . . 99 27 27 ASN CA C 53.41 . . 100 27 27 ASN N N 119.32 . . 101 28 28 TRP H H 8.09 . . 102 28 28 TRP HA H 4.58 . . 103 28 28 TRP CA C 58.23 . . 104 28 28 TRP N N 122.37 . . 105 29 29 VAL H H 7.74 . . 106 29 29 VAL HA H 3.83 . . 107 29 29 VAL CA C 62.81 . . 108 29 29 VAL N N 122.96 . . 109 30 30 ALA H H 8.05 . . 110 30 30 ALA HA H 4.07 . . 111 30 30 ALA CA C 53.00 . . 112 30 30 ALA N N 127.07 . . 113 31 31 ALA H H 8.06 . . 114 31 31 ALA HA H 4.08 . . 115 31 31 ALA CA C 53.00 . . 116 31 31 ALA N N 123.17 . . 117 32 32 ALA H H 8.12 . . 118 32 32 ALA HA H 4.17 . . 119 32 32 ALA CA C 53.05 . . 120 32 32 ALA N N 123.26 . . 121 33 33 LYS H H 8.08 . . 122 33 33 LYS HA H 4.34 . . 123 33 33 LYS CA C 56.87 . . 124 33 33 LYS N N 120.17 . . 125 34 34 PHE H H 8.12 . . 126 34 34 PHE HA H 4.57 . . 127 34 34 PHE CA C 58.17 . . 128 34 34 PHE N N 121.08 . . 129 35 35 GLU H H 8.19 . . 130 35 35 GLU HA H 4.33 . . 131 35 35 GLU CA C 55.89 . . 132 35 35 GLU N N 122.20 . . 133 36 36 SER H H 8.29 . . 134 36 36 SER HA H 4.32 . . 135 36 36 SER CA C 58.82 . . 136 36 36 SER N N 117.18 . . 137 37 37 ASN H H 8.35 . . 138 37 37 ASN HA H 4.68 . . 139 37 37 ASN CA C 53.57 . . 140 37 37 ASN N N 120.68 . . 141 38 38 PHE H H 8.14 . . 142 38 38 PHE HA H 4.58 . . 143 38 38 PHE CA C 58.32 . . 144 38 38 PHE N N 120.91 . . 145 39 39 ASN H H 8.34 . . 146 39 39 ASN HA H 4.71 . . 147 39 39 ASN CA C 53.57 . . 148 39 39 ASN N N 120.63 . . 149 40 40 THR H H 8.13 . . 150 40 40 THR HA H 4.27 . . 151 40 40 THR CA C 52.56 . . 152 40 40 THR N N 115.02 . . 153 41 41 GLU H H 8.32 . . 154 41 41 GLU HA H 4.26 . . 155 41 41 GLU CA C 56.35 . . 156 41 41 GLU N N 122.59 . . 157 42 42 ALA H H 8.3 . . 158 42 42 ALA HA H 4.30 . . 159 42 42 ALA CA C 53.07 . . 160 42 42 ALA N N 125.35 . . 161 43 43 THR H H 8.11 . . 162 43 43 THR HA H 4.29 . . 163 43 43 THR CA C 62.26 . . 164 43 43 THR N N 113.35 . . 165 44 44 ASN H H 8.37 . . 166 44 44 ASN HA H 4.70 . . 167 44 44 ASN CA C 53.48 . . 168 44 44 ASN N N 121.48 . . 169 45 45 ARG H H 8.36 . . 170 45 45 ARG HA H 4.30 . . 171 45 45 ARG CA C 56.51 . . 172 45 45 ARG N N 121.94 . . 173 46 46 ASN H H 8.5 . . 174 46 46 ASN HA H 4.75 . . 175 46 46 ASN CA C 53.63 . . 176 46 46 ASN N N 120.10 . . 177 47 47 THR H H 8.17 . . 178 47 47 THR HA H 4.31 . . 179 47 47 THR CA C 62.22 . . 180 47 47 THR N N 114.57 . . 181 48 48 ASP H H 8.48 . . 182 48 48 ASP HA H 4.73 . . 183 48 48 ASP CA C 53.50 . . 184 48 48 ASP N N 121.39 . . 185 49 49 GLY H H 8.41 . . 186 49 49 GLY HA2 H 3.97 . . 187 49 49 GLY N N 110.00 . . 188 50 50 SER H H 8.17 . . 189 50 50 SER HA H 4.48 . . 190 50 50 SER CA C 58.73 . . 191 50 50 SER N N 116.03 . . 192 51 51 THR H H 8.20 . . 193 51 51 THR HA H 4.28 . . 194 51 51 THR CA C 62.22 . . 195 51 51 THR N N 116.16 . . 196 52 52 ASP H H 8.36 . . 197 52 52 ASP HA H 4.69 . . 198 52 52 ASP CA C 53.05 . . 199 52 52 ASP N N 121.51 . . 200 53 53 TYR H H 8.13 . . 201 53 53 TYR HA H 4.46 . . 202 53 53 TYR CA C 58.82 . . 203 53 53 TYR N N 121.28 . . 204 54 54 GLY H H 8.28 . . 205 54 54 GLY HA2 H 3.87 . . 206 54 54 GLY N N 110.08 . . 207 55 55 ILE H H 7.85 . . 208 55 55 ILE HA H 4.12 . . 209 55 55 ILE CA C 61.76 . . 210 55 55 ILE N N 120.16 . . 211 56 56 LEU H H 8.22 . . 212 56 56 LEU HA H 4.28 . . 213 56 56 LEU N N 125.11 . . 214 57 57 GLN H H 8.26 . . 215 57 57 GLN HA H 4.30 . . 216 57 57 GLN CA C 56.26 . . 217 57 57 GLN N N 121.61 . . 218 58 58 ILE H H 8.14 . . 219 58 58 ILE HA H 4.01 . . 220 58 58 ILE N N 121.96 . . 221 67 67 GLY H H 8.39 . . 222 67 67 GLY HA2 H 3.91 . . 223 67 67 GLY N N 109.12 . . 224 68 68 ARG H H 8.08 . . 225 68 68 ARG HA H 4.18 . . 226 68 68 ARG N N 120.18 . . 227 69 69 THR H H 8.04 . . 228 69 69 THR HA H 4.39 . . 229 69 69 THR N N 116.80 . . 230 71 71 GLY H H 8.54 . . 231 71 71 GLY HA2 H 3.91 . . 232 71 71 GLY N N 110.00 . . 233 72 72 SER H H 8.03 . . 234 72 72 SER HA H 4.41 . . 235 72 72 SER CA C 58.82 . . 236 72 72 SER N N 115.85 . . 237 73 73 ARG H H 8.41 . . 238 73 73 ARG HA H 4.27 . . 239 73 73 ARG CA C 56.44 . . 240 73 73 ARG N N 122.76 . . 241 74 74 ASN H H 8.28 . . 242 74 74 ASN HA H 4.75 . . 243 74 74 ASN CA C 53.46 . . 244 74 74 ASN N N 120.80 . . 245 75 75 LEU HA H 4.27 . . 246 89 89 THR H H 8.11 . . 247 89 89 THR N N 116.13 . . 248 90 90 ALA H H 8.15 . . 249 90 90 ALA N N 122.72 . . 250 91 91 SER H H 8.08 . . 251 91 91 SER N N 117.20 . . 252 92 92 VAL H H 7.67 . . 253 92 92 VAL CA C 62.52 . . 254 92 92 VAL N N 121.57 . . 255 99 99 VAL HA H 4.11 . . 256 100 100 SER H H 8.33 . . 257 100 100 SER HA H 4.46 . . 258 100 100 SER CA C 58.75 . . 259 100 100 SER N N 119.34 . . 260 101 101 ASP H H 8.49 . . 261 101 101 ASP HA H 4.78 . . 262 101 101 ASP CA C 53.25 . . 263 101 101 ASP N N 121.59 . . 264 102 102 GLY H H 8.37 . . 265 102 102 GLY HA2 H 3.94 . . 266 102 102 GLY N N 109.64 . . 267 103 103 ASN H H 8.35 . . 268 103 103 ASN HA H 4.74 . . 269 103 103 ASN CA C 53.55 . . 270 103 103 ASN N N 119.09 . . 271 104 104 GLY H H 8.46 . . 272 104 104 GLY HA2 H 3.93 . . 273 104 104 GLY N N 109.69 . . 274 105 105 MET H H 8.22 . . 275 105 105 MET HA H 4.40 . . 276 105 105 MET CA C 56.28 . . 277 105 105 MET N N 120.37 . . 278 106 106 ASN H H 8.39 . . 279 106 106 ASN HA H 4.58 . . 280 106 106 ASN CA C 54.19 . . 281 106 106 ASN N N 119.64 . . 282 107 107 ALA H H 8.21 . . 283 107 107 ALA HA H 4.18 . . 284 107 107 ALA CA C 53.78 . . 285 107 107 ALA N N 124.16 . . 286 108 108 TRP H H 8.04 . . 287 108 108 TRP HA H 4.50 . . 288 108 108 TRP CA C 58.75 . . 289 108 108 TRP N N 120.28 . . 290 109 109 VAL H H 7.83 . . 291 109 109 VAL HA H 3.70 . . 292 109 109 VAL CA C 50.16 . . 293 109 109 VAL N N 121.38 . . 294 110 110 ALA H H 8.00 . . 295 110 110 ALA HA H 4.10 . . 296 110 110 ALA N N 124.72 . . 297 111 111 TRP H H 7.94 . . 298 111 111 TRP HA H 4.41 . . 299 111 111 TRP CA C 58.75 . . 300 111 111 TRP N N 119.80 . . 301 112 112 ARG H H 7.99 . . 302 112 112 ARG HA H 4.11 . . 303 112 112 ARG CA C 57.45 . . 304 112 112 ARG N N 121.46 . . 305 113 113 ASN H H 8.11 . . 306 113 113 ASN HA H 4.56 . . 307 113 113 ASN CA C 53.80 . . 308 113 113 ASN N N 118.47 . . 309 114 114 ARG H H 7.89 . . 310 114 114 ARG HA H 4.18 . . 311 114 114 ARG CA C 56.81 . . 312 114 114 ARG N N 121.44 . . 313 117 117 GLY H H 8.35 . . 314 117 117 GLY HA2 H 3.98 . . 315 117 117 GLY N N 110.24 . . 316 118 118 THR H H 8.05 . . 317 118 118 THR HA H 4.32 . . 318 118 118 THR CA C 62.19 . . 319 118 118 THR N N 113.73 . . 320 119 119 ASP H H 8.57 . . 321 119 119 ASP HA H 4.75 . . 322 119 119 ASP CA C 53.14 . . 323 119 119 ASP N N 122.09 . . 324 120 120 VAL H H 8.11 . . 325 120 120 VAL HA H 3.95 . . 326 120 120 VAL CA C 63.20 . . 327 120 120 VAL N N 121.45 . . 328 121 121 GLN H H 8.37 . . 329 121 121 GLN HA H 4.18 . . 330 121 121 GLN CA C 56.51 . . 331 121 121 GLN N N 123.64 . . 332 122 122 ALA H H 8.17 . . 333 122 122 ALA HA H 4.17 . . 334 122 122 ALA CA C 53.16 . . 335 122 122 ALA N N 124.79 . . 336 123 123 TRP H H 7.99 . . 337 123 123 TRP HA H 4.61 . . 338 123 123 TRP CA C 57.63 . . 339 123 123 TRP N N 120.33 . . 340 124 124 ILE H H 7.87 . . 341 124 124 ILE HA H 3.98 . . 342 124 124 ILE CA C 61.58 . . 343 124 124 ILE N N 123.30 . . 344 125 125 ARG H H 8.16 . . 345 125 125 ARG HA H 4.19 . . 346 125 125 ARG CA C 56.87 . . 347 125 125 ARG N N 124.76 . . 348 126 126 GLY H H 8.3 . . 349 126 126 GLY HA2 H 3.91 . . 350 126 126 GLY N N 110.45 . . 351 127 127 ALA H H 8.05 . . 352 127 127 ALA HA H 4.27 . . 353 127 127 ALA CA C 52.61 . . 354 127 127 ALA N N 124.01 . . 355 128 128 ARG H H 8.28 . . 356 128 128 ARG HA H 4.28 . . 357 128 128 ARG CA C 56.14 . . 358 128 128 ARG N N 120.82 . . 359 129 129 LEU H H 8.35 . . 360 129 129 LEU CA C 54.56 . . 361 129 129 LEU N N 125.42 . . stop_ save_