data_34093 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Solution structure of C20S variant of Dehydroascorbate reductase 3A from Populus trichocarpa in complex with dehydroascorbic acid. ; _BMRB_accession_number 34093 _BMRB_flat_file_name bmr34093.str _Entry_type original _Submission_date 2017-01-26 _Accession_date 2017-01-26 _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 Roret T. . . 2 Tsan P. . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 2 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 374 "15N chemical shifts" 374 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2017-03-16 original BMRB . stop_ _Original_release_date 2017-03-15 save_ ############################# # Citation for this entry # ############################# save_citation_1 _Saveframe_category entry_citation _Citation_full . _Citation_title ; Insights into ascorbate regeneration in plants: investigating the redox and structural properties of dehydroascorbate reductases from Populus trichocarpa. ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 26699905 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Lallement P. A. . 2 Roret T. . . 3 Tsan P. . . 4 Gualberto J. M. . 5 Girardet J. M. . 6 Didierjean C. . . 7 Rouhier N. . . 8 Hecker A. . . stop_ _Journal_abbreviation 'Biochem. J.' _Journal_volume 473 _Journal_issue 6 _Journal_ASTM BIJOAK _Journal_ISSN 1470-8728 _Journal_CSD 0043 _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 717 _Page_last 731 _Year 2016 _Details . save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name 'Dehydroascorbate reductase family protein' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label entity_1 $entity_1 entity_2 $entity_UU3 stop_ _System_molecular_weight . _System_oligomer_state ? _System_paramagnetic no _System_thiol_state . _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_entity_1 _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common entity_1 _Molecular_mass 24348.131 _Mol_thiol_state 'all free' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 218 _Mol_residue_sequence ; MALEICVKAAVGAPNILGDS PFCQRVLLSLEEKKIPYKSH LINLGDKPQWFLEISPEGKV PVVKIDDKWVADSDVIVGIL EEKNPEPPLATPPEFASVGS KIFPSFVKFLKSKDPNDGTE QALLEELKALDGHLKVHGPF IAGEKITAVDLSLAPKLYHL EVALGHFKNWPIPDNLTHVL NYIKLLFSRESFKKTRAAEE HVIAGWEPKVNAHHHHHH ; loop_ _Residue_seq_code _Residue_label 1 MET 2 ALA 3 LEU 4 GLU 5 ILE 6 CYS 7 VAL 8 LYS 9 ALA 10 ALA 11 VAL 12 GLY 13 ALA 14 PRO 15 ASN 16 ILE 17 LEU 18 GLY 19 ASP 20 SER 21 PRO 22 PHE 23 CYS 24 GLN 25 ARG 26 VAL 27 LEU 28 LEU 29 SER 30 LEU 31 GLU 32 GLU 33 LYS 34 LYS 35 ILE 36 PRO 37 TYR 38 LYS 39 SER 40 HIS 41 LEU 42 ILE 43 ASN 44 LEU 45 GLY 46 ASP 47 LYS 48 PRO 49 GLN 50 TRP 51 PHE 52 LEU 53 GLU 54 ILE 55 SER 56 PRO 57 GLU 58 GLY 59 LYS 60 VAL 61 PRO 62 VAL 63 VAL 64 LYS 65 ILE 66 ASP 67 ASP 68 LYS 69 TRP 70 VAL 71 ALA 72 ASP 73 SER 74 ASP 75 VAL 76 ILE 77 VAL 78 GLY 79 ILE 80 LEU 81 GLU 82 GLU 83 LYS 84 ASN 85 PRO 86 GLU 87 PRO 88 PRO 89 LEU 90 ALA 91 THR 92 PRO 93 PRO 94 GLU 95 PHE 96 ALA 97 SER 98 VAL 99 GLY 100 SER 101 LYS 102 ILE 103 PHE 104 PRO 105 SER 106 PHE 107 VAL 108 LYS 109 PHE 110 LEU 111 LYS 112 SER 113 LYS 114 ASP 115 PRO 116 ASN 117 ASP 118 GLY 119 THR 120 GLU 121 GLN 122 ALA 123 LEU 124 LEU 125 GLU 126 GLU 127 LEU 128 LYS 129 ALA 130 LEU 131 ASP 132 GLY 133 HIS 134 LEU 135 LYS 136 VAL 137 HIS 138 GLY 139 PRO 140 PHE 141 ILE 142 ALA 143 GLY 144 GLU 145 LYS 146 ILE 147 THR 148 ALA 149 VAL 150 ASP 151 LEU 152 SER 153 LEU 154 ALA 155 PRO 156 LYS 157 LEU 158 TYR 159 HIS 160 LEU 161 GLU 162 VAL 163 ALA 164 LEU 165 GLY 166 HIS 167 PHE 168 LYS 169 ASN 170 TRP 171 PRO 172 ILE 173 PRO 174 ASP 175 ASN 176 LEU 177 THR 178 HIS 179 VAL 180 LEU 181 ASN 182 TYR 183 ILE 184 LYS 185 LEU 186 LEU 187 PHE 188 SER 189 ARG 190 GLU 191 SER 192 PHE 193 LYS 194 LYS 195 THR 196 ARG 197 ALA 198 ALA 199 GLU 200 GLU 201 HIS 202 VAL 203 ILE 204 ALA 205 GLY 206 TRP 207 GLU 208 PRO 209 LYS 210 VAL 211 ASN 212 ALA 213 HIS 214 HIS 215 HIS 216 HIS 217 HIS 218 HIS stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date . save_ ############# # Ligands # ############# save_UU3 _Saveframe_category ligand _Mol_type "non-polymer (NON-POLYMER)" _Name_common "entity_UU3 ((5R)-5-[(1S)-1,2-bis(oxidanyl)ethyl]oxolane-2,3,4-trione)" _BMRB_code UU3 _PDB_code UU3 _Molecular_mass 174.108 _Mol_charge 0 _Mol_paramagnetic . _Mol_aromatic no _Details . loop_ _Atom_name _PDB_atom_name _Atom_type _Atom_chirality _Atom_charge _Atom_oxidation_number _Atom_unpaired_electrons C01 C01 C . 0 . ? C02 C02 C . 0 . ? C03 C03 C . 0 . ? C04 C04 C . 0 . ? O05 O05 O . 0 . ? C06 C06 C . 0 . ? O07 O07 O . 0 . ? C08 C08 C . 0 . ? O09 O09 O . 0 . ? O10 O10 O . 0 . ? O11 O11 O . 0 . ? O12 O12 O . 0 . ? H1 H1 H . 0 . ? H2 H2 H . 0 . ? H3 H3 H . 0 . ? H4 H4 H . 0 . ? H5 H5 H . 0 . ? H6 H6 H . 0 . ? stop_ loop_ _Bond_order _Bond_atom_one_atom_name _Bond_atom_two_atom_name _PDB_bond_atom_one_atom_name _PDB_bond_atom_two_atom_name DOUB O07 C06 ? ? DOUB O09 C08 ? ? SING C06 C08 ? ? SING C06 C04 ? ? SING C08 O10 ? ? SING O12 C01 ? ? DOUB C04 O05 ? ? SING C04 C03 ? ? SING O10 C03 ? ? SING C01 C02 ? ? SING C03 C02 ? ? SING C02 O11 ? ? SING C01 H1 ? ? SING C01 H2 ? ? SING C02 H3 ? ? SING C03 H4 ? ? SING O11 H5 ? ? SING O12 H6 ? ? stop_ _Mol_thiol_state . _Sequence_homology_query_date . save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species _Gene_mnemonic $entity_1 'Black cottonwood' 3694 Eukaryota Viridiplantae Populus trichocarpa POPTR_0008s04920g 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 $entity_1 'recombinant technology' . Escherichia coli . . stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Saveframe_category sample _Sample_type solution _Details '0.37 mM [U-100% 15N] dehydroascorbate reductase 3A, 90% H2O/10% D2O' loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $entity_1 0.37 mM '[U-100% 15N]' stop_ save_ save_sample_2 _Saveframe_category sample _Sample_type solution _Details '0.37 mM [U-100% 15N] dehydroascorbate reductase 3A, 47 mM Dehydroascorbic acid, 90% H2O/10% D2O' loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling 'Dehydroascorbic acid' 47 mM 'natural abundance' $entity_1 0.37 mM '[U-100% 15N]' stop_ save_ ############################ # Computer software used # ############################ save_software_1 _Saveframe_category software _Name CcpNMR _Version . loop_ _Vendor _Address _Electronic_address CCPN . . stop_ loop_ _Task 'chemical shift assignment' 'peak picking' stop_ _Details . save_ save_software_2 _Saveframe_category software _Name 'PELE web server' _Version . loop_ _Vendor _Address _Electronic_address PELE . . stop_ loop_ _Task 'structure calculation' stop_ _Details . save_ save_software_3 _Saveframe_category software _Name 'UCSF Chimera' _Version . loop_ _Vendor _Address _Electronic_address 'UCSF Chimera' . . stop_ loop_ _Task refinement stop_ _Details . save_ save_software_4 _Saveframe_category software _Name YASARA _Version . loop_ _Vendor _Address _Electronic_address YASARA . . stop_ loop_ _Task refinement stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model Avance _Field_strength 600 _Details . save_ ############################# # NMR applied experiments # ############################# save_2D_1H-15N_HSQC_1 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-15N HSQC' _Sample_label $sample_1 save_ save_2D_1H-15N_HSQC_2 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-15N HSQC' _Sample_label $sample_2 save_ ####################### # Sample conditions # ####################### save_sample_conditions_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units 'ionic strength' 50 . mM pH 8.0 . pH pressure 1 . atm temperature 298 . K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chem_shift_reference_1 _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 0.000 internal direct . . . 1.0 DSS N 15 'methyl protons' ppm 0.000 internal indirect . . . 0.10132912 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_1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Experiment_label '2D 1H-15N HSQC' stop_ loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $sample_conditions_1 _Chem_shift_reference_set_label $chem_shift_reference_1 _Mol_system_component_name entity_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 3 3 LEU H H 8.2 . 1 2 3 3 LEU N N 121.88 . 1 3 4 4 GLU H H 7.5 . 1 4 4 4 GLU N N 122.4 . 1 5 5 5 ILE H H 8.96 . 1 6 5 5 ILE N N 118.89 . 1 7 6 6 CYS H H 9.23 . 1 8 6 6 CYS N N 124.45 . 1 9 7 7 VAL H H 8.59 . 1 10 7 7 VAL N N 113.05 . 1 11 8 8 LYS H H 8.31 . 1 12 8 8 LYS N N 118.18 . 1 13 9 9 ALA H H 8.54 . 1 14 9 9 ALA N N 131.48 . 1 15 10 10 ALA H H 8.26 . 1 16 10 10 ALA N N 123.92 . 1 17 11 11 VAL H H 8.91 . 1 18 11 11 VAL N N 127.21 . 1 19 12 12 GLY H H 8.72 . 1 20 12 12 GLY N N 115.4 . 1 21 13 13 ALA H H 7.47 . 1 22 13 13 ALA N N 122.88 . 1 23 15 15 ASN H H 8.1 . 1 24 15 15 ASN N N 113.05 . 1 25 16 16 ILE H H 8.09 . 1 26 16 16 ILE N N 123.24 . 1 27 17 17 LEU H H 8.15 . 1 28 17 17 LEU N N 127.32 . 1 29 18 18 GLY H H 7.75 . 1 30 18 18 GLY N N 111.45 . 1 31 19 19 ASP H H 8.3 . 1 32 19 19 ASP N N 111.54 . 1 33 20 20 SER H H 7.79 . 1 34 20 20 SER N N 124.71 . 1 35 22 22 PHE H H 8.67 . 1 36 22 22 PHE N N 128.41 . 1 37 23 23 CYS H H 8.32 . 1 38 23 23 CYS N N 126.62 . 1 39 24 24 GLN H H 8.49 . 1 40 24 24 GLN N N 120.17 . 1 41 25 25 ARG H H 7.46 . 1 42 25 25 ARG N N 118.47 . 1 43 26 26 VAL H H 6.92 . 1 44 26 26 VAL N N 118.28 . 1 45 27 27 LEU H H 8.11 . 1 46 27 27 LEU N N 119.74 . 1 47 28 28 LEU H H 9.11 . 1 48 28 28 LEU N N 116.96 . 1 49 29 29 SER H H 7.01 . 1 50 29 29 SER N N 115.16 . 1 51 30 30 LEU H H 7.77 . 1 52 30 30 LEU N N 120.73 . 1 53 31 31 GLU H H 8.29 . 1 54 31 31 GLU N N 115.66 . 1 55 32 32 GLU H H 8.68 . 1 56 32 32 GLU N N 118.88 . 1 57 33 33 LYS H H 7.46 . 1 58 33 33 LYS N N 114.65 . 1 59 34 34 LYS H H 7.64 . 1 60 34 34 LYS N N 116.83 . 1 61 35 35 ILE H H 8.06 . 1 62 35 35 ILE N N 122.19 . 1 63 37 37 TYR H H 7.74 . 1 64 37 37 TYR N N 115.79 . 1 65 38 38 LYS H H 8.52 . 1 66 38 38 LYS N N 122.31 . 1 67 39 39 SER H H 8.49 . 1 68 39 39 SER N N 120.17 . 1 69 40 40 HIS H H 9.26 . 1 70 40 40 HIS N N 123.91 . 1 71 41 41 LEU H H 8.88 . 1 72 41 41 LEU N N 124.64 . 1 73 42 42 ILE H H 8.99 . 1 74 42 42 ILE N N 125.71 . 1 75 43 43 ASN H H 8.91 . 1 76 43 43 ASN N N 127.21 . 1 77 44 44 LEU H H 8.34 . 1 78 44 44 LEU N N 125.85 . 1 79 45 45 GLY H H 8.03 . 1 80 45 45 GLY N N 105.3 . 1 81 46 46 ASP H H 7.34 . 1 82 46 46 ASP N N 122.78 . 1 83 47 47 LYS H H 8.42 . 1 84 47 47 LYS N N 123.19 . 1 85 49 49 GLN H H 9.05 . 1 86 49 49 GLN N N 123.74 . 1 87 50 50 TRP H H 7.98 . 1 88 50 50 TRP N N 115.1 . 1 89 51 51 PHE H H 5.84 . 1 90 51 51 PHE N N 122.53 . 1 91 52 52 LEU H H 7.02 . 1 92 52 52 LEU N N 120.5 . 1 93 53 53 GLU H H 7.16 . 1 94 53 53 GLU N N 114.99 . 1 95 54 54 ILE H H 6.59 . 1 96 54 54 ILE N N 115.86 . 1 97 55 55 SER H H 7.31 . 1 98 55 55 SER N N 113.04 . 1 99 57 57 GLU H H 8.39 . 1 100 57 57 GLU N N 115.07 . 1 101 58 58 GLY H H 8.33 . 1 102 58 58 GLY N N 109.16 . 1 103 59 59 LYS H H 6.74 . 1 104 59 59 LYS N N 117.02 . 1 105 60 60 VAL H H 7.85 . 1 106 60 60 VAL N N 109.84 . 1 107 62 62 VAL H H 7.55 . 1 108 62 62 VAL N N 113.51 . 1 109 63 63 VAL H H 9.12 . 1 110 63 63 VAL N N 124.23 . 1 111 64 64 LYS H H 8.24 . 1 112 64 64 LYS N N 130.54 . 1 113 65 65 ILE H H 8.62 . 1 114 65 65 ILE N N 128.8 . 1 115 66 66 ASP H H 8.85 . 1 116 66 66 ASP N N 127.7 . 1 117 67 67 ASP H H 8.44 . 1 118 67 67 ASP N N 113.41 . 1 119 68 68 LYS H H 7.54 . 1 120 68 68 LYS N N 120.00 . 1 121 69 69 TRP H H 8.66 . 1 122 69 69 TRP N N 122.84 . 1 123 70 70 VAL H H 9.56 . 1 124 70 70 VAL N N 128.08 . 1 125 71 71 ALA H H 8.26 . 1 126 71 71 ALA N N 129.6 . 1 127 72 72 ASP H H 7.95 . 1 128 72 72 ASP N N 111.92 . 1 129 74 74 ASP H H 8.09 . 1 130 74 74 ASP N N 120.57 . 1 131 75 75 VAL H H 7.36 . 1 132 75 75 VAL N N 122.39 . 1 133 76 76 ILE H H 8.68 . 1 134 76 76 ILE N N 118.88 . 1 135 77 77 VAL H H 7.92 . 1 136 77 77 VAL N N 112.53 . 1 137 78 78 GLY H H 7.36 . 1 138 78 78 GLY N N 108.06 . 1 139 79 79 ILE H H 7.89 . 1 140 79 79 ILE N N 124.38 . 1 141 80 80 LEU H H 8.32 . 1 142 80 80 LEU N N 117.66 . 1 143 81 81 GLU H H 7.42 . 1 144 81 81 GLU N N 117.85 . 1 145 82 82 GLU H H 7.33 . 1 146 82 82 GLU N N 117.1 . 1 147 83 83 LYS H H 8.17 . 1 148 83 83 LYS N N 115.24 . 1 149 84 84 ASN H H 7.52 . 1 150 84 84 ASN N N 115.69 . 1 151 89 89 LEU H H 9.69 . 1 152 89 89 LEU N N 122.57 . 1 153 90 90 ALA H H 7.14 . 1 154 90 90 ALA N N 122.73 . 1 155 91 91 THR H H 8.72 . 1 156 91 91 THR N N 123.01 . 1 157 94 94 GLU H H 9.72 . 1 158 94 94 GLU N N 117.9 . 1 159 95 95 PHE H H 7.89 . 1 160 95 95 PHE N N 118.02 . 1 161 96 96 ALA H H 7.16 . 1 162 96 96 ALA N N 119.8 . 1 163 97 97 SER H H 8.33 . 1 164 97 97 SER N N 108.75 . 1 165 98 98 VAL H H 7.15 . 1 166 98 98 VAL N N 126.47 . 1 167 99 99 GLY H H 8.67 . 1 168 99 99 GLY N N 113.24 . 1 169 100 100 SER H H 7.86 . 1 170 100 100 SER N N 116.15 . 1 171 101 101 LYS H H 8.95 . 1 172 101 101 LYS N N 119.59 . 1 173 102 102 ILE H H 7.88 . 1 174 102 102 ILE N N 123.43 . 1 175 103 103 PHE H H 9.7 . 1 176 103 103 PHE N N 119.83 . 1 177 105 105 SER H H 7.14 . 1 178 105 105 SER N N 113.05 . 1 179 106 106 PHE H H 8.74 . 1 180 106 106 PHE N N 128.34 . 1 181 107 107 VAL H H 7.64 . 1 182 107 107 VAL N N 122.69 . 1 183 108 108 LYS H H 7.09 . 1 184 108 108 LYS N N 115.53 . 1 185 109 109 PHE H H 7.21 . 1 186 109 109 PHE N N 118.07 . 1 187 110 110 LEU H H 8.66 . 1 188 110 110 LEU N N 121.45 . 1 189 111 111 LYS H H 7.08 . 1 190 111 111 LYS N N 111.17 . 1 191 112 112 SER H H 6.91 . 1 192 112 112 SER N N 114.96 . 1 193 113 113 LYS H H 8.91 . 1 194 113 113 LYS N N 128.11 . 1 195 114 114 ASP H H 7.95 . 1 196 114 114 ASP N N 120.91 . 1 197 116 116 ASN H H 8.29 . 1 198 116 116 ASN N N 115.66 . 1 199 117 117 ASP H H 7.61 . 1 200 117 117 ASP N N 119.07 . 1 201 118 118 GLY H H 8.57 . 1 202 118 118 GLY N N 108.65 . 1 203 119 119 THR H H 8.81 . 1 204 119 119 THR N N 116.4 . 1 205 120 120 GLU H H 8.71 . 1 206 120 120 GLU N N 127.15 . 1 207 121 121 GLN H H 7.82 . 1 208 121 121 GLN N N 117.42 . 1 209 122 122 ALA H H 7.75 . 1 210 122 122 ALA N N 121.12 . 1 211 123 123 LEU H H 7.17 . 1 212 123 123 LEU N N 118.5 . 1 213 124 124 LEU H H 8.49 . 1 214 124 124 LEU N N 120.17 . 1 215 125 125 GLU H H 8.36 . 1 216 125 125 GLU N N 118.39 . 1 217 126 126 GLU H H 7.42 . 1 218 126 126 GLU N N 118.87 . 1 219 127 127 LEU H H 8.55 . 1 220 127 127 LEU N N 121.95 . 1 221 128 128 LYS H H 8.99 . 1 222 128 128 LYS N N 121.03 . 1 223 129 129 ALA H H 7.88 . 1 224 129 129 ALA N N 123.43 . 1 225 130 130 LEU H H 7.51 . 1 226 130 130 LEU N N 120.98 . 1 227 131 131 ASP H H 8.37 . 1 228 131 131 ASP N N 120.89 . 1 229 132 132 GLY H H 8.3 . 1 230 132 132 GLY N N 102.36 . 1 231 133 133 HIS H H 7.78 . 1 232 133 133 HIS N N 122.17 . 1 233 134 134 LEU H H 8.2 . 1 234 134 134 LEU N N 119.58 . 1 235 135 135 LYS H H 7.69 . 1 236 135 135 LYS N N 120.34 . 1 237 136 136 VAL H H 6.3 . 1 238 136 136 VAL N N 113.98 . 1 239 137 137 HIS H H 8.07 . 1 240 137 137 HIS N N 117.8 . 1 241 138 138 GLY H H 7.26 . 1 242 138 138 GLY N N 103.53 . 1 243 140 140 PHE H H 8.32 . 1 244 140 140 PHE N N 117.66 . 1 245 141 141 ILE H H 9.22 . 1 246 141 141 ILE N N 119.42 . 1 247 142 142 ALA H H 9.02 . 1 248 142 142 ALA N N 117.25 . 1 249 143 143 GLY H H 7.49 . 1 250 143 143 GLY N N 111.79 . 1 251 144 144 GLU H H 8.58 . 1 252 144 144 GLU N N 121.39 . 1 253 145 145 LYS H H 7.8 . 1 254 145 145 LYS N N 116.83 . 1 255 146 146 ILE H H 7.65 . 1 256 146 146 ILE N N 124.08 . 1 257 147 147 THR H H 9.27 . 1 258 147 147 THR N N 115.47 . 1 259 148 148 ALA H H 9.42 . 1 260 148 148 ALA N N 123.03 . 1 261 149 149 VAL H H 8.36 . 1 262 149 149 VAL N N 118.39 . 1 263 150 150 ASP H H 7.39 . 1 264 150 150 ASP N N 120.11 . 1 265 151 151 LEU H H 7.16 . 1 266 151 151 LEU N N 114.99 . 1 267 152 152 SER H H 7.44 . 1 268 152 152 SER N N 108.72 . 1 269 153 153 LEU H H 8.31 . 1 270 153 153 LEU N N 119.28 . 1 271 154 154 ALA H H 8.81 . 1 272 154 154 ALA N N 120.76 . 1 273 156 156 LYS H H 6.6 . 1 274 156 156 LYS N N 113.99 . 1 275 157 157 LEU H H 8.63 . 1 276 157 157 LEU N N 118.43 . 1 277 158 158 TYR H H 8.14 . 1 278 158 158 TYR N N 121.13 . 1 279 159 159 HIS H H 8.03 . 1 280 159 159 HIS N N 118.16 . 1 281 160 160 LEU H H 7.46 . 1 282 160 160 LEU N N 118.47 . 1 283 161 161 GLU H H 8.31 . 1 284 161 161 GLU N N 118.18 . 1 285 163 163 ALA H H 9.24 . 1 286 163 163 ALA N N 120.61 . 1 287 164 164 LEU H H 8.51 . 1 288 164 164 LEU N N 115.28 . 1 289 165 165 GLY H H 7.7 . 1 290 165 165 GLY N N 107.65 . 1 291 166 166 HIS H H 7.82 . 1 292 166 166 HIS N N 117.42 . 1 293 167 167 PHE H H 8.69 . 1 294 167 167 PHE N N 112.21 . 1 295 168 168 LYS H H 6.98 . 1 296 168 168 LYS N N 112.71 . 1 297 169 169 ASN H H 7.07 . 1 298 169 169 ASN N N 118.1 . 1 299 170 170 TRP H H 7.6 . 1 300 170 170 TRP N N 122.00 . 1 301 174 174 ASP H H 7.77 . 1 302 174 174 ASP N N 119.42 . 1 303 175 175 ASN H H 7.66 . 1 304 175 175 ASN N N 112.4 . 1 305 176 176 LEU H H 7.51 . 1 306 176 176 LEU N N 125.41 . 1 307 177 177 THR H H 8.49 . 1 308 177 177 THR N N 120.17 . 1 309 178 178 HIS H H 9.00 . 1 310 178 178 HIS N N 123.32 . 1 311 179 179 VAL H H 8.26 . 1 312 179 179 VAL N N 123.92 . 1 313 180 180 LEU H H 8.1 . 1 314 180 180 LEU N N 118.66 . 1 315 181 181 ASN H H 7.76 . 1 316 181 181 ASN N N 118.22 . 1 317 182 182 TYR H H 7.85 . 1 318 182 182 TYR N N 122.93 . 1 319 183 183 ILE H H 7.98 . 1 320 183 183 ILE N N 115.1 . 1 321 184 184 LYS H H 7.13 . 1 322 184 184 LYS N N 119.36 . 1 323 185 185 LEU H H 7.74 . 1 324 185 185 LEU N N 119.9 . 1 325 186 186 LEU H H 8.11 . 1 326 186 186 LEU N N 119.74 . 1 327 187 187 PHE H H 8.31 . 1 328 187 187 PHE N N 114.61 . 1 329 188 188 SER H H 7.17 . 1 330 188 188 SER N N 109.7 . 1 331 189 189 ARG H H 7.22 . 1 332 189 189 ARG N N 122.73 . 1 333 190 190 GLU H H 8.99 . 1 334 190 190 GLU N N 125.71 . 1 335 191 191 SER H H 8.43 . 1 336 191 191 SER N N 112.43 . 1 337 192 192 PHE H H 6.82 . 1 338 192 192 PHE N N 126.16 . 1 339 193 193 LYS H H 8.18 . 1 340 193 193 LYS N N 118.61 . 1 341 194 194 LYS H H 7.94 . 1 342 194 194 LYS N N 114.02 . 1 343 195 195 THR H H 6.89 . 1 344 195 195 THR N N 105.00 . 1 345 196 196 ARG H H 6.79 . 1 346 196 196 ARG N N 120.94 . 1 347 197 197 ALA H H 8.04 . 1 348 197 197 ALA N N 125.9 . 1 349 198 198 ALA H H 9.16 . 1 350 198 198 ALA N N 125.54 . 1 351 199 199 GLU H H 9.97 . 1 352 199 199 GLU N N 125.29 . 1 353 200 200 GLU H H 9.25 . 1 354 200 200 GLU N N 114.4 . 1 355 201 201 HIS H H 8.53 . 1 356 201 201 HIS N N 116.12 . 1 357 202 202 VAL H H 7.62 . 1 358 202 202 VAL N N 124.77 . 1 359 203 203 ILE H H 7.76 . 1 360 203 203 ILE N N 118.22 . 1 361 204 204 ALA H H 7.72 . 1 362 204 204 ALA N N 119.03 . 1 363 205 205 GLY H H 7.6 . 1 364 205 205 GLY N N 103.05 . 1 365 206 206 TRP H H 7.62 . 1 366 206 206 TRP N N 118.54 . 1 367 207 207 GLU H H 7.67 . 1 368 207 207 GLU N N 117.71 . 1 369 209 209 LYS H H 7.61 . 1 370 209 209 LYS N N 115.88 . 1 371 211 211 ASN H H 8.29 . 1 372 211 211 ASN N N 115.66 . 1 373 212 212 ALA H H 7.85 . 1 374 212 212 ALA N N 122.93 . 1 stop_ save_ save_assigned_chemical_shifts_2 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Experiment_label '2D 1H-15N HSQC' stop_ loop_ _Sample_label $sample_2 stop_ _Sample_conditions_label $sample_conditions_1 _Chem_shift_reference_set_label $chem_shift_reference_1 _Mol_system_component_name entity_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 3 3 LEU H H 8.2 . 1 2 3 3 LEU N N 121.82 . 1 3 4 4 GLU H H 7.5 . 1 4 4 4 GLU N N 122.88 . 1 5 5 5 ILE H H 8.99 . 1 6 5 5 ILE N N 118.81 . 1 7 6 6 CYS H H 9.21 . 1 8 6 6 CYS N N 124.48 . 1 9 7 7 VAL H H 8.61 . 1 10 7 7 VAL N N 113.08 . 1 11 8 8 LYS H H 8.36 . 1 12 8 8 LYS N N 118.04 . 1 13 9 9 ALA H H 8.58 . 1 14 9 9 ALA N N 131.98 . 1 15 10 10 ALA H H 8.23 . 1 16 10 10 ALA N N 123.9 . 1 17 11 11 VAL H H 8.89 . 1 18 11 11 VAL N N 127.32 . 1 19 12 12 GLY H H 8.72 . 1 20 12 12 GLY N N 115.39 . 1 21 13 13 ALA H H 7.5 . 1 22 13 13 ALA N N 122.88 . 1 23 15 15 ASN H H 8.1 . 1 24 15 15 ASN N N 113.06 . 1 25 16 16 ILE H H 8.23 . 1 26 16 16 ILE N N 123.9 . 1 27 17 17 LEU H H 8.19 . 1 28 17 17 LEU N N 127.4 . 1 29 18 18 GLY H H 7.67 . 1 30 18 18 GLY N N 112.35 . 1 31 19 19 ASP H H 8.2 . 1 32 19 19 ASP N N 113.17 . 1 33 20 20 SER H H 7.78 . 1 34 20 20 SER N N 124.42 . 1 35 22 22 PHE H H 8.67 . 1 36 22 22 PHE N N 128.4 . 1 37 23 23 CYS H H 8.32 . 1 38 23 23 CYS N N 126.67 . 1 39 24 24 GLN H H 8.47 . 1 40 24 24 GLN N N 120.22 . 1 41 25 25 ARG H H 7.48 . 1 42 25 25 ARG N N 118.56 . 1 43 26 26 VAL H H 6.85 . 1 44 26 26 VAL N N 118.11 . 1 45 27 27 LEU H H 8.14 . 1 46 27 27 LEU N N 119.43 . 1 47 28 28 LEU H H 9.06 . 1 48 28 28 LEU N N 116.91 . 1 49 29 29 SER H H 7.01 . 1 50 29 29 SER N N 115.17 . 1 51 30 30 LEU H H 7.8 . 1 52 30 30 LEU N N 120.62 . 1 53 31 31 GLU H H 8.29 . 1 54 31 31 GLU N N 115.65 . 1 55 32 32 GLU H H 8.67 . 1 56 32 32 GLU N N 118.84 . 1 57 33 33 LYS H H 7.45 . 1 58 33 33 LYS N N 114.63 . 1 59 34 34 LYS H H 7.64 . 1 60 34 34 LYS N N 116.88 . 1 61 35 35 ILE H H 8.09 . 1 62 35 35 ILE N N 122.26 . 1 63 37 37 TYR H H 7.76 . 1 64 37 37 TYR N N 115.84 . 1 65 38 38 LYS H H 8.48 . 1 66 38 38 LYS N N 122.05 . 1 67 39 39 SER H H 8.47 . 1 68 39 39 SER N N 120.22 . 1 69 40 40 HIS H H 9.22 . 1 70 40 40 HIS N N 123.38 . 1 71 41 41 LEU H H 8.96 . 1 72 41 41 LEU N N 124.7 . 1 73 42 42 ILE H H 8.92 . 1 74 42 42 ILE N N 125.64 . 1 75 43 43 ASN H H 8.89 . 1 76 43 43 ASN N N 127.32 . 1 77 44 44 LEU H H 8.33 . 1 78 44 44 LEU N N 125.97 . 1 79 45 45 GLY H H 8.03 . 1 80 45 45 GLY N N 105.31 . 1 81 46 46 ASP H H 7.37 . 1 82 46 46 ASP N N 122.82 . 1 83 47 47 LYS H H 8.43 . 1 84 47 47 LYS N N 123.2 . 1 85 49 49 GLN H H 9.06 . 1 86 49 49 GLN N N 123.44 . 1 87 50 50 TRP H H 8 . 1 88 50 50 TRP N N 115.11 . 1 89 51 51 PHE H H 5.83 . 1 90 51 51 PHE N N 122.43 . 1 91 52 52 LEU H H 7.01 . 1 92 52 52 LEU N N 120.54 . 1 93 53 53 GLU H H 7.16 . 1 94 53 53 GLU N N 115.01 . 1 95 54 54 ILE H H 6.59 . 1 96 54 54 ILE N N 115.86 . 1 97 55 55 SER H H 7.29 . 1 98 55 55 SER N N 112.9 . 1 99 57 57 GLU H H 8.38 . 1 100 57 57 GLU N N 115.04 . 1 101 58 58 GLY H H 8.27 . 1 102 58 58 GLY N N 108.73 . 1 103 59 59 LYS H H 6.76 . 1 104 59 59 LYS N N 116.94 . 1 105 60 60 VAL H H 8.02 . 1 106 60 60 VAL N N 109.55 . 1 107 62 62 VAL H H 7.55 . 1 108 62 62 VAL N N 113.52 . 1 109 63 63 VAL H H 9.17 . 1 110 63 63 VAL N N 124.43 . 1 111 64 64 LYS H H 8.27 . 1 112 64 64 LYS N N 130.62 . 1 113 65 65 ILE H H 8.61 . 1 114 65 65 ILE N N 128.81 . 1 115 66 66 ASP H H 8.88 . 1 116 66 66 ASP N N 127.74 . 1 117 67 67 ASP H H 8.42 . 1 118 67 67 ASP N N 113.56 . 1 119 68 68 LYS H H 7.54 . 1 120 68 68 LYS N N 120.01 . 1 121 69 69 TRP H H 8.66 . 1 122 69 69 TRP N N 122.86 . 1 123 70 70 VAL H H 9.57 . 1 124 70 70 VAL N N 127.88 . 1 125 71 71 ALA H H 8.27 . 1 126 71 71 ALA N N 129.65 . 1 127 72 72 ASP H H 7.94 . 1 128 72 72 ASP N N 111.79 . 1 129 74 74 ASP H H 8.05 . 1 130 74 74 ASP N N 120.55 . 1 131 75 75 VAL H H 7.37 . 1 132 75 75 VAL N N 122.43 . 1 133 76 76 ILE H H 8.67 . 1 134 76 76 ILE N N 118.84 . 1 135 77 77 VAL H H 7.93 . 1 136 77 77 VAL N N 112.69 . 1 137 78 78 GLY H H 7.37 . 1 138 78 78 GLY N N 108.03 . 1 139 79 79 ILE H H 7.89 . 1 140 79 79 ILE N N 124.38 . 1 141 80 80 LEU H H 8.3 . 1 142 80 80 LEU N N 117.64 . 1 143 81 81 GLU H H 7.45 . 1 144 81 81 GLU N N 118.01 . 1 145 82 82 GLU H H 7.34 . 1 146 82 82 GLU N N 117.14 . 1 147 83 83 LYS H H 8.17 . 1 148 83 83 LYS N N 115.19 . 1 149 84 84 ASN H H 7.51 . 1 150 84 84 ASN N N 115.68 . 1 151 89 89 LEU H H 9.67 . 1 152 89 89 LEU N N 122.61 . 1 153 90 90 ALA H H 7.14 . 1 154 90 90 ALA N N 122.68 . 1 155 91 91 THR H H 8.71 . 1 156 91 91 THR N N 123.02 . 1 157 94 94 GLU H H 9.65 . 1 158 94 94 GLU N N 117.86 . 1 159 95 95 PHE H H 7.87 . 1 160 95 95 PHE N N 117.85 . 1 161 96 96 ALA H H 7.15 . 1 162 96 96 ALA N N 119.86 . 1 163 97 97 SER H H 8.3 . 1 164 97 97 SER N N 109.03 . 1 165 98 98 VAL H H 7.15 . 1 166 98 98 VAL N N 126.43 . 1 167 99 99 GLY H H 8.7 . 1 168 99 99 GLY N N 112.8 . 1 169 100 100 SER H H 7.86 . 1 170 100 100 SER N N 115.91 . 1 171 101 101 LYS H H 8.95 . 1 172 101 101 LYS N N 119.59 . 1 173 102 102 ILE H H 7.91 . 1 174 102 102 ILE N N 123.12 . 1 175 103 103 PHE H H 9.68 . 1 176 103 103 PHE N N 119.93 . 1 177 105 105 SER H H 7.18 . 1 178 105 105 SER N N 113.14 . 1 179 106 106 PHE H H 8.75 . 1 180 106 106 PHE N N 128.34 . 1 181 107 107 VAL H H 7.66 . 1 182 107 107 VAL N N 122.63 . 1 183 108 108 LYS H H 7.09 . 1 184 108 108 LYS N N 115.41 . 1 185 109 109 PHE H H 7.21 . 1 186 109 109 PHE N N 118.12 . 1 187 110 110 LEU H H 8.64 . 1 188 110 110 LEU N N 121.31 . 1 189 111 111 LYS H H 7.06 . 1 190 111 111 LYS N N 111.16 . 1 191 112 112 SER H H 6.92 . 1 192 112 112 SER N N 114.91 . 1 193 113 113 LYS H H 8.91 . 1 194 113 113 LYS N N 128.31 . 1 195 114 114 ASP H H 7.95 . 1 196 114 114 ASP N N 120.92 . 1 197 116 116 ASN H H 8.29 . 1 198 116 116 ASN N N 115.65 . 1 199 117 117 ASP H H 7.61 . 1 200 117 117 ASP N N 119.05 . 1 201 118 118 GLY H H 8.56 . 1 202 118 118 GLY N N 108.68 . 1 203 119 119 THR H H 8.81 . 1 204 119 119 THR N N 116.35 . 1 205 120 120 GLU H H 8.7 . 1 206 120 120 GLU N N 127.13 . 1 207 121 121 GLN H H 7.82 . 1 208 121 121 GLN N N 117.42 . 1 209 122 122 ALA H H 7.74 . 1 210 122 122 ALA N N 121.11 . 1 211 123 123 LEU H H 7.16 . 1 212 123 123 LEU N N 118.38 . 1 213 124 124 LEU H H 8.47 . 1 214 124 124 LEU N N 120.22 . 1 215 125 125 GLU H H 8.43 . 1 216 125 125 GLU N N 118.27 . 1 217 126 126 GLU H H 7.38 . 1 218 126 126 GLU N N 118.49 . 1 219 127 127 LEU H H 8.55 . 1 220 127 127 LEU N N 121.98 . 1 221 128 128 LYS H H 9.02 . 1 222 128 128 LYS N N 121 . 1 223 129 129 ALA H H 7.88 . 1 224 129 129 ALA N N 123.43 . 1 225 130 130 LEU H H 7.51 . 1 226 130 130 LEU N N 120.92 . 1 227 131 131 ASP H H 8.36 . 1 228 131 131 ASP N N 120.84 . 1 229 132 132 GLY H H 8.29 . 1 230 132 132 GLY N N 102.47 . 1 231 133 133 HIS H H 7.78 . 1 232 133 133 HIS N N 122.12 . 1 233 134 134 LEU H H 8.27 . 1 234 134 134 LEU N N 119.07 . 1 235 135 135 LYS H H 7.67 . 1 236 135 135 LYS N N 120.15 . 1 237 136 136 VAL H H 6.31 . 1 238 136 136 VAL N N 113.15 . 1 239 137 137 HIS H H 8.09 . 1 240 137 137 HIS N N 117 . 1 241 138 138 GLY H H 7.28 . 1 242 138 138 GLY N N 103.89 . 1 243 140 140 PHE H H 8.3 . 1 244 140 140 PHE N N 117.64 . 1 245 141 141 ILE H H 9.25 . 1 246 141 141 ILE N N 119.45 . 1 247 142 142 ALA H H 9.04 . 1 248 142 142 ALA N N 117.29 . 1 249 143 143 GLY H H 7.5 . 1 250 143 143 GLY N N 111.66 . 1 251 144 144 GLU H H 8.58 . 1 252 144 144 GLU N N 121.58 . 1 253 145 145 LYS H H 7.8 . 1 254 145 145 LYS N N 116.76 . 1 255 146 146 ILE H H 7.64 . 1 256 146 146 ILE N N 124.2 . 1 257 147 147 THR H H 9.25 . 1 258 147 147 THR N N 115.55 . 1 259 148 148 ALA H H 9.41 . 1 260 148 148 ALA N N 123.01 . 1 261 149 149 VAL H H 8.36 . 1 262 149 149 VAL N N 118.04 . 1 263 150 150 ASP H H 7.4 . 1 264 150 150 ASP N N 120.11 . 1 265 151 151 LEU H H 7.16 . 1 266 151 151 LEU N N 115.01 . 1 267 152 152 SER H H 7.44 . 1 268 152 152 SER N N 108.73 . 1 269 153 153 LEU H H 8.27 . 1 270 153 153 LEU N N 119.07 . 1 271 154 154 ALA H H 8.83 . 1 272 154 154 ALA N N 120.66 . 1 273 156 156 LYS H H 6.58 . 1 274 156 156 LYS N N 114.36 . 1 275 157 157 LEU H H 8.66 . 1 276 157 157 LEU N N 118.47 . 1 277 158 158 TYR H H 8.14 . 1 278 158 158 TYR N N 121.14 . 1 279 159 159 HIS H H 8 . 1 280 159 159 HIS N N 117.8 . 1 281 160 160 LEU H H 7.48 . 1 282 160 160 LEU N N 118.56 . 1 283 161 161 GLU H H 8.36 . 1 284 161 161 GLU N N 118.04 . 1 285 163 163 ALA H H 9.31 . 1 286 163 163 ALA N N 120.76 . 1 287 164 164 LEU H H 8.48 . 1 288 164 164 LEU N N 115.3 . 1 289 165 165 GLY H H 7.68 . 1 290 165 165 GLY N N 107.6 . 1 291 166 166 HIS H H 7.82 . 1 292 166 166 HIS N N 117.42 . 1 293 167 167 PHE H H 8.74 . 1 294 167 167 PHE N N 112.45 . 1 295 168 168 LYS H H 7.03 . 1 296 168 168 LYS N N 112.93 . 1 297 169 169 ASN H H 7.03 . 1 298 169 169 ASN N N 117.95 . 1 299 170 170 TRP H H 7.58 . 1 300 170 170 TRP N N 121.91 . 1 301 174 174 ASP H H 7.78 . 1 302 174 174 ASP N N 119.5 . 1 303 175 175 ASN H H 7.67 . 1 304 175 175 ASN N N 112.35 . 1 305 176 176 LEU H H 7.53 . 1 306 176 176 LEU N N 125.47 . 1 307 177 177 THR H H 8.47 . 1 308 177 177 THR N N 120.22 . 1 309 178 178 HIS H H 9 . 1 310 178 178 HIS N N 122.94 . 1 311 179 179 VAL H H 8.23 . 1 312 179 179 VAL N N 123.9 . 1 313 180 180 LEU H H 8.09 . 1 314 180 180 LEU N N 118.66 . 1 315 181 181 ASN H H 7.77 . 1 316 181 181 ASN N N 118.2 . 1 317 182 182 TYR H H 7.84 . 1 318 182 182 TYR N N 122.97 . 1 319 183 183 ILE H H 8 . 1 320 183 183 ILE N N 115.11 . 1 321 184 184 LYS H H 7.11 . 1 322 184 184 LYS N N 119.38 . 1 323 185 185 LEU H H 7.68 . 1 324 185 185 LEU N N 119.62 . 1 325 186 186 LEU H H 8.14 . 1 326 186 186 LEU N N 119.43 . 1 327 187 187 PHE H H 8.32 . 1 328 187 187 PHE N N 114.67 . 1 329 188 188 SER H H 7.16 . 1 330 188 188 SER N N 109.75 . 1 331 189 189 ARG H H 7.22 . 1 332 189 189 ARG N N 122.75 . 1 333 190 190 GLU H H 9.02 . 1 334 190 190 GLU N N 125.39 . 1 335 191 191 SER H H 8.44 . 1 336 191 191 SER N N 112.41 . 1 337 192 192 PHE H H 6.83 . 1 338 192 192 PHE N N 126.1 . 1 339 193 193 LYS H H 8.18 . 1 340 193 193 LYS N N 118.73 . 1 341 194 194 LYS H H 7.94 . 1 342 194 194 LYS N N 114.06 . 1 343 195 195 THR H H 6.89 . 1 344 195 195 THR N N 104.88 . 1 345 196 196 ARG H H 6.76 . 1 346 196 196 ARG N N 121.23 . 1 347 197 197 ALA H H 7.86 . 1 348 197 197 ALA N N 125.44 . 1 349 198 198 ALA H H 9.15 . 1 350 198 198 ALA N N 125.75 . 1 351 199 199 GLU H H 9.95 . 1 352 199 199 GLU N N 125.17 . 1 353 200 200 GLU H H 9.25 . 1 354 200 200 GLU N N 114.31 . 1 355 201 201 HIS H H 8.53 . 1 356 201 201 HIS N N 116.11 . 1 357 202 202 VAL H H 7.53 . 1 358 202 202 VAL N N 125.47 . 1 359 203 203 ILE H H 7.77 . 1 360 203 203 ILE N N 118.2 . 1 361 204 204 ALA H H 7.73 . 1 362 204 204 ALA N N 119.13 . 1 363 205 205 GLY H H 7.7 . 1 364 205 205 GLY N N 104.15 . 1 365 206 206 TRP H H 7.67 . 1 366 206 206 TRP N N 118.89 . 1 367 207 207 GLU H H 7.77 . 1 368 207 207 GLU N N 118.2 . 1 369 209 209 LYS H H 7.61 . 1 370 209 209 LYS N N 115.92 . 1 371 211 211 ASN H H 8.29 . 1 372 211 211 ASN N N 115.65 . 1 373 212 212 ALA H H 7.91 . 1 374 212 212 ALA N N 123.12 . 1 stop_ save_