data_34105 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Dehydroascorbate reductase 3A from Populus trichocarpa complexed with GSH. ; _BMRB_accession_number 34105 _BMRB_flat_file_name bmr34105.str _Entry_type original _Submission_date 2017-02-27 _Accession_date 2017-02-27 _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" 376 "15N chemical shifts" 376 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2017-03-09 original BMRB . stop_ _Original_release_date 2017-03-07 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 0264-6021 _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_GSH 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 24364.195 _Mol_thiol_state 'other bound and free' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 218 _Mol_residue_sequence ; MALEICVKAAVGAPNILGDC 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 CYS 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_GSH _Saveframe_category ligand _Mol_type "non-polymer (NON-POLYMER)" _Name_common "entity_GSH (GLUTATHIONE)" _BMRB_code GSH _PDB_code GSH _Molecular_mass 307.323 _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 N1 N1 N . 0 . ? CA1 CA1 C . 0 . ? C1 C1 C . 0 . ? O11 O11 O . 0 . ? O12 O12 O . 0 . ? CB1 CB1 C . 0 . ? CG1 CG1 C . 0 . ? CD1 CD1 C . 0 . ? OE1 OE1 O . 0 . ? N2 N2 N . 0 . ? CA2 CA2 C . 0 . ? C2 C2 C . 0 . ? O2 O2 O . 0 . ? CB2 CB2 C . 0 . ? SG2 SG2 S . 0 . ? N3 N3 N . 0 . ? CA3 CA3 C . 0 . ? C3 C3 C . 0 . ? O31 O31 O . 0 . ? O32 O32 O . 0 . ? HN11 HN11 H . 0 . ? HN12 HN12 H . 0 . ? HA1 HA1 H . 0 . ? H12 H12 H . 0 . ? HB12 HB12 H . 0 . ? HB13 HB13 H . 0 . ? HG12 HG12 H . 0 . ? HG13 HG13 H . 0 . ? HN2 HN2 H . 0 . ? HA2 HA2 H . 0 . ? HB22 HB22 H . 0 . ? HB23 HB23 H . 0 . ? HSG HSG H . 0 . ? HN3 HN3 H . 0 . ? HA31 HA31 H . 0 . ? HA32 HA32 H . 0 . ? H32 H32 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 SING N1 CA1 ? ? SING N1 HN11 ? ? SING N1 HN12 ? ? SING CA1 C1 ? ? SING CA1 CB1 ? ? SING CA1 HA1 ? ? DOUB C1 O11 ? ? SING C1 O12 ? ? SING O12 H12 ? ? SING CB1 CG1 ? ? SING CB1 HB12 ? ? SING CB1 HB13 ? ? SING CG1 CD1 ? ? SING CG1 HG12 ? ? SING CG1 HG13 ? ? DOUB CD1 OE1 ? ? SING CD1 N2 ? ? SING N2 CA2 ? ? SING N2 HN2 ? ? SING CA2 C2 ? ? SING CA2 CB2 ? ? SING CA2 HA2 ? ? DOUB C2 O2 ? ? SING C2 N3 ? ? SING CB2 SG2 ? ? SING CB2 HB22 ? ? SING CB2 HB23 ? ? SING SG2 HSG ? ? SING N3 CA3 ? ? SING N3 HN3 ? ? SING CA3 C3 ? ? SING CA3 HA31 ? ? SING CA3 HA32 ? ? DOUB C3 O31 ? ? SING C3 O32 ? ? SING O32 H32 ? ? 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 'Western balsam poplar' 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, 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, 74.0 mM GLUTATHIONE, 90% H2O/10% D2O' loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $entity_1 0.37 mM '[U-100% 15N]' $entity_GSH 74.0 mM 'natural abundance' stop_ save_ ############################ # Computer software used # ############################ save_software_1 _Saveframe_category software _Name YASARA _Version . loop_ _Vendor _Address _Electronic_address YASARA . . stop_ loop_ _Task refinement stop_ _Details . save_ save_software_2 _Saveframe_category software _Name AutoDock _Version . loop_ _Vendor _Address _Electronic_address AutoDock . . stop_ loop_ _Task 'structure calculation' stop_ _Details . save_ save_software_3 _Saveframe_category software _Name CcpNMR _Version . loop_ _Vendor _Address _Electronic_address CCPN . . stop_ loop_ _Task 'chemical shift assignment' 'peak picking' stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model Avance _Field_strength 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_ ####################### # 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 8.19 . 1 2 3 3 LEU N N 122.27 . 1 3 4 4 GLU H H 7.54 . 1 4 4 4 GLU N N 122.23 . 1 5 5 5 ILE H H 8.89 . 1 6 5 5 ILE N N 118.71 . 1 7 6 6 CYS H H 9.18 . 1 8 6 6 CYS N N 124.25 . 1 9 7 7 VAL H H 8.61 . 1 10 7 7 VAL N N 113.11 . 1 11 8 8 LYS H H 7.03 . 1 12 8 8 LYS N N 122.1 . 1 13 9 9 ALA H H 8.5 . 1 14 9 9 ALA N N 131.13 . 1 15 10 10 ALA H H 8.28 . 1 16 10 10 ALA N N 123.99 . 1 17 11 11 VAL H H 8.86 . 1 18 11 11 VAL N N 127.22 . 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 7.46 . 1 22 13 13 ALA N N 122.79 . 1 23 15 15 ASN H H 8.08 . 1 24 15 15 ASN N N 123.2 . 1 25 16 16 ILE H H 8.08 . 1 26 16 16 ILE N N 123.2 . 1 27 17 17 LEU H H 8.15 . 1 28 17 17 LEU N N 127.38 . 1 29 18 18 GLY H H 7.75 . 1 30 18 18 GLY N N 111.5 . 1 31 19 19 ASP H H 8.3 . 1 32 19 19 ASP N N 111.34 . 1 33 20 20 CYS H H 7.84 . 1 34 20 20 CYS N N 125.17 . 1 35 22 22 PHE H H 9.12 . 1 36 22 22 PHE N N 130.42 . 1 37 23 23 CYS H H 10.17 . 1 38 23 23 CYS N N 126.25 . 1 39 24 24 GLN H H 8.46 . 1 40 24 24 GLN N N 119.58 . 1 41 25 25 ARG H H 7.44 . 1 42 25 25 ARG N N 118.41 . 1 43 26 26 VAL H H 7.13 . 1 44 26 26 VAL N N 118.84 . 1 45 27 27 LEU H H 8.11 . 1 46 27 27 LEU N N 119.84 . 1 47 28 28 LEU H H 9.14 . 1 48 28 28 LEU N N 117.53 . 1 49 29 29 SER H H 7.22 . 1 50 29 29 SER N N 114.73 . 1 51 30 30 LEU H H 7.79 . 1 52 30 30 LEU N N 120.56 . 1 53 31 31 GLU H H 8.28 . 1 54 31 31 GLU N N 116.07 . 1 55 32 32 GLU H H 8.72 . 1 56 32 32 GLU N N 118.75 . 1 57 33 33 LYS H H 7.46 . 1 58 33 33 LYS N N 114.67 . 1 59 34 34 LYS H H 7.63 . 1 60 34 34 LYS N N 116.74 . 1 61 35 35 ILE H H 8.05 . 1 62 35 35 ILE N N 122.13 . 1 63 37 37 TYR H H 7.79 . 1 64 37 37 TYR N N 116.16 . 1 65 38 38 LYS H H 8.47 . 1 66 38 38 LYS N N 121.96 . 1 67 39 39 SER H H 8.57 . 1 68 39 39 SER N N 120.11 . 1 69 40 40 HIS H H 9.14 . 1 70 40 40 HIS N N 122.27 . 1 71 41 41 LEU H H 8.98 . 1 72 41 41 LEU N N 125.04 . 1 73 42 42 ILE H H 9.03 . 1 74 42 42 ILE N N 125.49 . 1 75 43 43 ASN H H 8.87 . 1 76 43 43 ASN N N 127.62 . 1 77 44 44 LEU H H 8.3 . 1 78 44 44 LEU N N 125.83 . 1 79 45 45 GLY H H 8.02 . 1 80 45 45 GLY N N 105.24 . 1 81 46 46 ASP H H 7.32 . 1 82 46 46 ASP N N 122.7 . 1 83 47 47 LYS H H 8.41 . 1 84 47 47 LYS N N 123.21 . 1 85 49 49 GLN H H 8.86 . 1 86 49 49 GLN N N 123.62 . 1 87 50 50 TRP H H 7.96 . 1 88 50 50 TRP N N 115.01 . 1 89 51 51 PHE H H 5.85 . 1 90 51 51 PHE N N 122.49 . 1 91 52 52 LEU H H 6.99 . 1 92 52 52 LEU N N 120.49 . 1 93 53 53 GLU H H 7.16 . 1 94 53 53 GLU N N 115.09 . 1 95 54 54 ILE H H 6.57 . 1 96 54 54 ILE N N 115.75 . 1 97 55 55 SER H H 7.32 . 1 98 55 55 SER N N 113.14 . 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 8.4 . 1 102 58 58 GLY N N 109.46 . 1 103 59 59 LYS H H 6.71 . 1 104 59 59 LYS N N 117.03 . 1 105 60 60 VAL H H 7.87 . 1 106 60 60 VAL N N 109.9 . 1 107 62 62 VAL H H 7.54 . 1 108 62 62 VAL N N 112.89 . 1 109 63 63 VAL H H 9.08 . 1 110 63 63 VAL N N 123.88 . 1 111 64 64 LYS H H 8.17 . 1 112 64 64 LYS N N 130.36 . 1 113 65 65 ILE H H 8.6 . 1 114 65 65 ILE N N 128.96 . 1 115 66 66 ASP H H 8.87 . 1 116 66 66 ASP N N 127.72 . 1 117 67 67 ASP H H 8.41 . 1 118 67 67 ASP N N 113.86 . 1 119 68 68 LYS H H 7.54 . 1 120 68 68 LYS N N 119.97 . 1 121 69 69 TRP H H 8.68 . 1 122 69 69 TRP N N 122.87 . 1 123 70 70 VAL H H 9.52 . 1 124 70 70 VAL N N 128.12 . 1 125 71 71 ALA H H 8.23 . 1 126 71 71 ALA N N 129.57 . 1 127 72 72 ASP H H 8.00 . 1 128 72 72 ASP N N 111.48 . 1 129 73 73 SER H H 9.23 . 1 130 73 73 SER N N 121.84 . 1 131 74 74 ASP H H 8.07 . 1 132 74 74 ASP N N 120.67 . 1 133 75 75 VAL H H 7.32 . 1 134 75 75 VAL N N 122.7 . 1 135 76 76 ILE H H 8.72 . 1 136 76 76 ILE N N 118.75 . 1 137 77 77 VAL H H 7.9 . 1 138 77 77 VAL N N 112.35 . 1 139 78 78 GLY H H 7.34 . 1 140 78 78 GLY N N 108.13 . 1 141 79 79 ILE H H 7.85 . 1 142 79 79 ILE N N 124.37 . 1 143 80 80 LEU H H 8.3 . 1 144 80 80 LEU N N 117.49 . 1 145 81 81 GLU H H 7.41 . 1 146 81 81 GLU N N 117.86 . 1 147 82 82 GLU H H 7.32 . 1 148 82 82 GLU N N 117.07 . 1 149 83 83 LYS H H 8.16 . 1 150 83 83 LYS N N 114.99 . 1 151 84 84 ASN H H 7.51 . 1 152 84 84 ASN N N 115.75 . 1 153 89 89 LEU H H 9.69 . 1 154 89 89 LEU N N 122.58 . 1 155 90 90 ALA H H 7.13 . 1 156 90 90 ALA N N 122.72 . 1 157 91 91 THR H H 8.72 . 1 158 91 91 THR N N 122.92 . 1 159 94 94 GLU H H 9.58 . 1 160 94 94 GLU N N 117.73 . 1 161 95 95 PHE H H 7.86 . 1 162 95 95 PHE N N 117.54 . 1 163 96 96 ALA H H 7.16 . 1 164 96 96 ALA N N 119.9 . 1 165 97 97 SER H H 8.36 . 1 166 97 97 SER N N 109.68 . 1 167 98 98 VAL H H 7.15 . 1 168 98 98 VAL N N 126.42 . 1 169 99 99 GLY H H 8.61 . 1 170 99 99 GLY N N 113.11 . 1 171 100 100 SER H H 7.87 . 1 172 100 100 SER N N 116.28 . 1 173 101 101 LYS H H 9.00 . 1 174 101 101 LYS N N 119.84 . 1 175 102 102 ILE H H 7.86 . 1 176 102 102 ILE N N 123.08 . 1 177 103 103 PHE H H 9.66 . 1 178 103 103 PHE N N 119.72 . 1 179 105 105 SER H H 7.15 . 1 180 105 105 SER N N 113.14 . 1 181 106 106 PHE H H 8.74 . 1 182 106 106 PHE N N 128.24 . 1 183 107 107 VAL H H 7.62 . 1 184 107 107 VAL N N 122.69 . 1 185 108 108 LYS H H 7.08 . 1 186 108 108 LYS N N 115.5 . 1 187 109 109 PHE H H 7.21 . 1 188 109 109 PHE N N 118.04 . 1 189 110 110 LEU H H 8.65 . 1 190 110 110 LEU N N 121.37 . 1 191 111 111 LYS H H 7.07 . 1 192 111 111 LYS N N 111.14 . 1 193 112 112 SER H H 6.91 . 1 194 112 112 SER N N 114.78 . 1 195 113 113 LYS H H 8.91 . 1 196 113 113 LYS N N 128.33 . 1 197 114 114 ASP H H 7.94 . 1 198 114 114 ASP N N 120.96 . 1 199 116 116 ASN H H 8.28 . 1 200 116 116 ASN N N 115.61 . 1 201 117 117 ASP H H 7.6 . 1 202 117 117 ASP N N 118.95 . 1 203 118 118 GLY H H 8.59 . 1 204 118 118 GLY N N 108.75 . 1 205 119 119 THR H H 8.79 . 1 206 119 119 THR N N 116.37 . 1 207 120 120 GLU H H 8.71 . 1 208 120 120 GLU N N 127.18 . 1 209 121 121 GLN H H 7.8 . 1 210 121 121 GLN N N 116.78 . 1 211 122 122 ALA H H 7.74 . 1 212 122 122 ALA N N 121.11 . 1 213 123 123 LEU H H 7.21 . 1 214 123 123 LEU N N 118.04 . 1 215 124 124 LEU H H 8.48 . 1 216 124 124 LEU N N 120.26 . 1 217 125 125 GLU H H 8.36 . 1 218 125 125 GLU N N 118.22 . 1 219 126 126 GLU H H 7.44 . 1 220 126 126 GLU N N 118.41 . 1 221 127 127 LEU H H 8.58 . 1 222 127 127 LEU N N 121.69 . 1 223 128 128 LYS H H 9.00 . 1 224 128 128 LYS N N 121.12 . 1 225 129 129 ALA H H 7.86 . 1 226 129 129 ALA N N 123.08 . 1 227 130 130 LEU H H 7.52 . 1 228 130 130 LEU N N 120.99 . 1 229 131 131 ASP H H 8.4 . 1 230 131 131 ASP N N 120.64 . 1 231 132 132 GLY H H 8.32 . 1 232 132 132 GLY N N 102.71 . 1 233 133 133 HIS H H 7.82 . 1 234 133 133 HIS N N 122.28 . 1 235 134 134 LEU H H 8.23 . 1 236 134 134 LEU N N 119.45 . 1 237 135 135 LYS H H 7.64 . 1 238 135 135 LYS N N 119.99 . 1 239 136 136 VAL H H 6.39 . 1 240 136 136 VAL N N 112.5 . 1 241 137 137 HIS H H 8.01 . 1 242 137 137 HIS N N 117.1 . 1 243 138 138 GLY H H 7.29 . 1 244 138 138 GLY N N 104.24 . 1 245 140 140 PHE H H 8.33 . 1 246 140 140 PHE N N 117.73 . 1 247 141 141 ILE H H 9.23 . 1 248 141 141 ILE N N 119.5 . 1 249 142 142 ALA H H 9.15 . 1 250 142 142 ALA N N 117.09 . 1 251 143 143 GLY H H 7.5 . 1 252 143 143 GLY N N 111.55 . 1 253 144 144 GLU H H 8.58 . 1 254 144 144 GLU N N 121.69 . 1 255 145 145 LYS H H 7.8 . 1 256 145 145 LYS N N 116.78 . 1 257 146 146 ILE H H 7.63 . 1 258 146 146 ILE N N 124.24 . 1 259 147 147 THR H H 9.22 . 1 260 147 147 THR N N 115.52 . 1 261 148 148 ALA H H 9.4 . 1 262 148 148 ALA N N 122.99 . 1 263 149 149 VAL H H 8.36 . 1 264 149 149 VAL N N 118.22 . 1 265 150 150 ASP H H 7.4 . 1 266 150 150 ASP N N 120.13 . 1 267 151 151 LEU H H 7.12 . 1 268 151 151 LEU N N 114.85 . 1 269 152 152 SER H H 7.45 . 1 270 152 152 SER N N 108.58 . 1 271 153 153 LEU H H 8.23 . 1 272 153 153 LEU N N 119.45 . 1 273 154 154 ALA H H 8.77 . 1 274 154 154 ALA N N 120.67 . 1 275 156 156 LYS H H 6.57 . 1 276 156 156 LYS N N 113.93 . 1 277 157 157 LEU H H 8.63 . 1 278 157 157 LEU N N 118.39 . 1 279 158 158 TYR H H 8.18 . 1 280 158 158 TYR N N 120.99 . 1 281 159 159 HIS H H 7.86 . 1 282 159 159 HIS N N 117.54 . 1 283 160 160 LEU H H 7.44 . 1 284 160 160 LEU N N 118.41 . 1 285 161 161 GLU H H 8.28 . 1 286 161 161 GLU N N 118.35 . 1 287 162 162 VAL H H 8.37 . 1 288 162 162 VAL N N 119.17 . 1 289 163 163 ALA H H 9.25 . 1 290 163 163 ALA N N 120.77 . 1 291 164 164 LEU H H 8.5 . 1 292 164 164 LEU N N 115.49 . 1 293 165 165 GLY H H 7.68 . 1 294 165 165 GLY N N 107.54 . 1 295 166 166 HIS H H 7.72 . 1 296 166 166 HIS N N 117.35 . 1 297 167 167 PHE H H 8.74 . 1 298 167 167 PHE N N 112.27 . 1 299 168 168 LYS H H 7.00 . 1 300 168 168 LYS N N 112.8 . 1 301 169 169 ASN H H 7.07 . 1 302 169 169 ASN N N 117.89 . 1 303 170 170 TRP H H 7.56 . 1 304 170 170 TRP N N 121.73 . 1 305 174 174 ASP H H 7.77 . 1 306 174 174 ASP N N 119.6 . 1 307 175 175 ASN H H 7.65 . 1 308 175 175 ASN N N 112.32 . 1 309 176 176 LEU H H 7.58 . 1 310 176 176 LEU N N 125.66 . 1 311 177 177 THR H H 7.45 . 1 312 177 177 THR N N 110.6 . 1 313 178 178 HIS H H 9.02 . 1 314 178 178 HIS N N 122.13 . 1 315 179 179 VAL H H 8.3 . 1 316 179 179 VAL N N 123.42 . 1 317 180 180 LEU H H 8.07 . 1 318 180 180 LEU N N 118.6 . 1 319 181 181 ASN H H 7.76 . 1 320 181 181 ASN N N 118.4 . 1 321 182 182 TYR H H 7.78 . 1 322 182 182 TYR N N 123.07 . 1 323 183 183 ILE H H 8.02 . 1 324 183 183 ILE N N 115.73 . 1 325 184 184 LYS H H 7.17 . 1 326 184 184 LYS N N 118.43 . 1 327 185 185 LEU H H 7.7 . 1 328 185 185 LEU N N 119.9 . 1 329 186 186 LEU H H 8.11 . 1 330 186 186 LEU N N 119.84 . 1 331 187 187 PHE H H 8.34 . 1 332 187 187 PHE N N 114.73 . 1 333 188 188 SER H H 7.19 . 1 334 188 188 SER N N 110.01 . 1 335 189 189 ARG H H 7.22 . 1 336 189 189 ARG N N 122.61 . 1 337 190 190 GLU H H 8.98 . 1 338 190 190 GLU N N 125.04 . 1 339 191 191 SER H H 8.43 . 1 340 191 191 SER N N 112.47 . 1 341 192 192 PHE H H 6.8 . 1 342 192 192 PHE N N 126.1 . 1 343 193 193 LYS H H 8.15 . 1 344 193 193 LYS N N 118.63 . 1 345 194 194 LYS H H 7.95 . 1 346 194 194 LYS N N 113.96 . 1 347 195 195 THR H H 6.88 . 1 348 195 195 THR N N 105.03 . 1 349 196 196 ARG H H 6.81 . 1 350 196 196 ARG N N 120.98 . 1 351 197 197 ALA H H 8.13 . 1 352 197 197 ALA N N 126.00 . 1 353 198 198 ALA H H 9.1 . 1 354 198 198 ALA N N 125.21 . 1 355 199 199 GLU H H 9.85 . 1 356 199 199 GLU N N 125.06 . 1 357 200 200 GLU H H 9.26 . 1 358 200 200 GLU N N 114.7 . 1 359 201 201 HIS H H 7.37 . 1 360 201 201 HIS N N 121.06 . 1 361 202 202 VAL H H 7.57 . 1 362 202 202 VAL N N 124.68 . 1 363 203 203 ILE H H 8.07 . 1 364 203 203 ILE N N 118.6 . 1 365 204 204 ALA H H 7.77 . 1 366 204 204 ALA N N 119.6 . 1 367 205 205 GLY H H 7.6 . 1 368 205 205 GLY N N 103.1 . 1 369 206 206 TRP H H 7.58 . 1 370 206 206 TRP N N 118.59 . 1 371 209 209 LYS H H 7.61 . 1 372 209 209 LYS N N 115.89 . 1 373 211 211 ASN H H 8.28 . 1 374 211 211 ASN N N 115.61 . 1 375 212 212 ALA H H 7.71 . 1 376 212 212 ALA N N 123.33 . 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_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 8.21 . 1 2 3 3 LEU N N 122.29 . 1 3 4 4 GLU H H 7.42 . 1 4 4 4 GLU N N 121.99 . 1 5 5 5 ILE H H 8.93 . 1 6 5 5 ILE N N 118.76 . 1 7 6 6 CYS H H 9.23 . 1 8 6 6 CYS N N 124.46 . 1 9 7 7 VAL H H 8.60 . 1 10 7 7 VAL N N 113.01 . 1 11 8 8 LYS H H 7.05 . 1 12 8 8 LYS N N 122.12 . 1 13 9 9 ALA H H 8.49 . 1 14 9 9 ALA N N 131.28 . 1 15 10 10 ALA H H 8.29 . 1 16 10 10 ALA N N 124.1 . 1 17 11 11 VAL H H 8.9 . 1 18 11 11 VAL N N 127.15 . 1 19 12 12 GLY H H 8.72 . 1 20 12 12 GLY N N 115.38 . 1 21 13 13 ALA H H 7.47 . 1 22 13 13 ALA N N 122.79 . 1 23 15 15 ASN H H 8.1 . 1 24 15 15 ASN N N 123.25 . 1 25 16 16 ILE H H 8.1 . 1 26 16 16 ILE N N 123.25 . 1 27 17 17 LEU H H 8.15 . 1 28 17 17 LEU N N 127.35 . 1 29 18 18 GLY H H 7.79 . 1 30 18 18 GLY N N 111.72 . 1 31 19 19 ASP H H 8.35 . 1 32 19 19 ASP N N 111.86 . 1 33 20 20 CYS H H 7.89 . 1 34 20 20 CYS N N 125.48 . 1 35 22 22 PHE H H 9.15 . 1 36 22 22 PHE N N 130.7 . 1 37 23 23 CYS H H 10.24 . 1 38 23 23 CYS N N 126.49 . 1 39 24 24 GLN H H 8.47 . 1 40 24 24 GLN N N 119.62 . 1 41 25 25 ARG H H 7.43 . 1 42 25 25 ARG N N 118.59 . 1 43 26 26 VAL H H 7.13 . 1 44 26 26 VAL N N 118.86 . 1 45 27 27 LEU H H 8.15 . 1 46 27 27 LEU N N 120.00 . 1 47 28 28 LEU H H 9.14 . 1 48 28 28 LEU N N 117.54 . 1 49 29 29 SER H H 7.22 . 1 50 29 29 SER N N 114.75 . 1 51 30 30 LEU H H 7.85 . 1 52 30 30 LEU N N 120.6 . 1 53 31 31 GLU H H 8.32 . 1 54 31 31 GLU N N 116.24 . 1 55 32 32 GLU H H 8.74 . 1 56 32 32 GLU N N 118.85 . 1 57 33 33 LYS H H 7.47 . 1 58 33 33 LYS N N 114.72 . 1 59 34 34 LYS H H 7.64 . 1 60 34 34 LYS N N 116.86 . 1 61 35 35 ILE H H 8.09 . 1 62 35 35 ILE N N 122.22 . 1 63 37 37 TYR H H 7.76 . 1 64 37 37 TYR N N 115.8 . 1 65 38 38 LYS H H 8.42 . 1 66 38 38 LYS N N 121.74 . 1 67 39 39 SER H H 8.57 . 1 68 39 39 SER N N 120.13 . 1 69 40 40 HIS H H 9.18 . 1 70 40 40 HIS N N 122.29 . 1 71 41 41 LEU H H 8.99 . 1 72 41 41 LEU N N 125.17 . 1 73 42 42 ILE H H 8.99 . 1 74 42 42 ILE N N 125.17 . 1 75 43 43 ASN H H 8.89 . 1 76 43 43 ASN N N 127.83 . 1 77 44 44 LEU H H 8.34 . 1 78 44 44 LEU N N 125.7 . 1 79 45 45 GLY H H 8.04 . 1 80 45 45 GLY N N 105.27 . 1 81 46 46 ASP H H 7.35 . 1 82 46 46 ASP N N 122.66 . 1 83 47 47 LYS H H 8.46 . 1 84 47 47 LYS N N 123.62 . 1 85 49 49 GLN H H 8.86 . 1 86 49 49 GLN N N 123.65 . 1 87 50 50 TRP H H 7.94 . 1 88 50 50 TRP N N 114.85 . 1 89 51 51 PHE H H 5.87 . 1 90 51 51 PHE N N 122.54 . 1 91 52 52 LEU H H 6.97 . 1 92 52 52 LEU N N 120.22 . 1 93 53 53 GLU H H 7.2 . 1 94 53 53 GLU N N 114.87 . 1 95 54 54 ILE H H 6.63 . 1 96 54 54 ILE N N 115.88 . 1 97 55 55 SER H H 7.2 . 1 98 55 55 SER N N 112.99 . 1 99 57 57 GLU H H 8.36 . 1 100 57 57 GLU N N 114.87 . 1 101 58 58 GLY H H 8.24 . 1 102 58 58 GLY N N 108.31 . 1 103 59 59 LYS H H 6.87 . 1 104 59 59 LYS N N 116.64 . 1 105 60 60 VAL H H 8.34 . 1 106 60 60 VAL N N 110.25 . 1 107 62 62 VAL H H 7.54 . 1 108 62 62 VAL N N 112.88 . 1 109 63 63 VAL H H 9.23 . 1 110 63 63 VAL N N 124.46 . 1 111 64 64 LYS H H 8.25 . 1 112 64 64 LYS N N 130.07 . 1 113 65 65 ILE H H 8.6 . 1 114 65 65 ILE N N 128.8 . 1 115 66 66 ASP H H 8.89 . 1 116 66 66 ASP N N 127.83 . 1 117 67 67 ASP H H 8.41 . 1 118 67 67 ASP N N 113.98 . 1 119 68 68 LYS H H 7.54 . 1 120 68 68 LYS N N 120.05 . 1 121 69 69 TRP H H 8.68 . 1 122 69 69 TRP N N 123.00 . 1 123 70 70 VAL H H 9.61 . 1 124 70 70 VAL N N 128.06 . 1 125 71 71 ALA H H 8.3 . 1 126 71 71 ALA N N 129.95 . 1 127 72 72 ASP H H 7.72 . 1 128 72 72 ASP N N 110.79 . 1 129 73 73 SER H H 9.73 . 1 130 73 73 SER N N 123.54 . 1 131 74 74 ASP H H 7.87 . 1 132 74 74 ASP N N 120.66 . 1 133 75 75 VAL H H 7.26 . 1 134 75 75 VAL N N 121.63 . 1 135 76 76 ILE H H 8.8 . 1 136 76 76 ILE N N 119.14 . 1 137 77 77 VAL H H 7.96 . 1 138 77 77 VAL N N 111.49 . 1 139 78 78 GLY H H 7.23 . 1 140 78 78 GLY N N 108.24 . 1 141 79 79 ILE H H 7.71 . 1 142 79 79 ILE N N 124.23 . 1 143 80 80 LEU H H 8.32 . 1 144 80 80 LEU N N 117.62 . 1 145 81 81 GLU H H 7.36 . 1 146 81 81 GLU N N 117.76 . 1 147 82 82 GLU H H 7.31 . 1 148 82 82 GLU N N 117.00 . 1 149 83 83 LYS H H 8.13 . 1 150 83 83 LYS N N 115.03 . 1 151 84 84 ASN H H 7.53 . 1 152 84 84 ASN N N 115.77 . 1 153 89 89 LEU H H 9.7 . 1 154 89 89 LEU N N 122.46 . 1 155 90 90 ALA H H 7.11 . 1 156 90 90 ALA N N 122.67 . 1 157 91 91 THR H H 8.73 . 1 158 91 91 THR N N 122.95 . 1 159 94 94 GLU H H 9.58 . 1 160 94 94 GLU N N 117.75 . 1 161 95 95 PHE H H 7.86 . 1 162 95 95 PHE N N 117.6 . 1 163 96 96 ALA H H 7.16 . 1 164 96 96 ALA N N 119.86 . 1 165 97 97 SER H H 8.36 . 1 166 97 97 SER N N 109.67 . 1 167 98 98 VAL H H 7.15 . 1 168 98 98 VAL N N 126.4 . 1 169 99 99 GLY H H 8.6 . 1 170 99 99 GLY N N 113.01 . 1 171 100 100 SER H H 7.86 . 1 172 100 100 SER N N 116.3 . 1 173 101 101 LYS H H 8.99 . 1 174 101 101 LYS N N 119.77 . 1 175 102 102 ILE H H 7.86 . 1 176 102 102 ILE N N 123.04 . 1 177 103 103 PHE H H 9.69 . 1 178 103 103 PHE N N 119.72 . 1 179 105 105 SER H H 7.15 . 1 180 105 105 SER N N 113.18 . 1 181 106 106 PHE H H 8.75 . 1 182 106 106 PHE N N 128.2 . 1 183 107 107 VAL H H 7.63 . 1 184 107 107 VAL N N 122.67 . 1 185 108 108 LYS H H 7.09 . 1 186 108 108 LYS N N 115.5 . 1 187 109 109 PHE H H 7.22 . 1 188 109 109 PHE N N 118.03 . 1 189 110 110 LEU H H 8.64 . 1 190 110 110 LEU N N 121.37 . 1 191 111 111 LYS H H 7.07 . 1 192 111 111 LYS N N 111.12 . 1 193 112 112 SER H H 6.91 . 1 194 112 112 SER N N 114.78 . 1 195 113 113 LYS H H 8.91 . 1 196 113 113 LYS N N 128.28 . 1 197 114 114 ASP H H 7.94 . 1 198 114 114 ASP N N 120.91 . 1 199 116 116 ASN H H 8.28 . 1 200 116 116 ASN N N 115.64 . 1 201 117 117 ASP H H 7.59 . 1 202 117 117 ASP N N 118.78 . 1 203 118 118 GLY H H 8.59 . 1 204 118 118 GLY N N 108.75 . 1 205 119 119 THR H H 8.79 . 1 206 119 119 THR N N 116.36 . 1 207 120 120 GLU H H 8.7 . 1 208 120 120 GLU N N 127.15 . 1 209 121 121 GLN H H 7.8 . 1 210 121 121 GLN N N 116.8 . 1 211 122 122 ALA H H 7.74 . 1 212 122 122 ALA N N 121.08 . 1 213 123 123 LEU H H 7.22 . 1 214 123 123 LEU N N 118.03 . 1 215 124 124 LEU H H 8.48 . 1 216 124 124 LEU N N 120.27 . 1 217 125 125 GLU H H 8.36 . 1 218 125 125 GLU N N 118.27 . 1 219 126 126 GLU H H 7.43 . 1 220 126 126 GLU N N 118.59 . 1 221 127 127 LEU H H 8.58 . 1 222 127 127 LEU N N 121.68 . 1 223 128 128 LYS H H 9.00 . 1 224 128 128 LYS N N 121.09 . 1 225 129 129 ALA H H 7.88 . 1 226 129 129 ALA N N 123.4 . 1 227 130 130 LEU H H 7.53 . 1 228 130 130 LEU N N 121.01 . 1 229 131 131 ASP H H 8.4 . 1 230 131 131 ASP N N 120.66 . 1 231 132 132 GLY H H 8.32 . 1 232 132 132 GLY N N 102.66 . 1 233 133 133 HIS H H 7.82 . 1 234 133 133 HIS N N 122.26 . 1 235 134 134 LEU H H 8.24 . 1 236 134 134 LEU N N 119.51 . 1 237 135 135 LYS H H 7.65 . 1 238 135 135 LYS N N 119.99 . 1 239 136 136 VAL H H 6.39 . 1 240 136 136 VAL N N 112.52 . 1 241 137 137 HIS H H 8.01 . 1 242 137 137 HIS N N 117.07 . 1 243 138 138 GLY H H 7.29 . 1 244 138 138 GLY N N 104.22 . 1 245 140 140 PHE H H 8.32 . 1 246 140 140 PHE N N 117.62 . 1 247 141 141 ILE H H 9.23 . 1 248 141 141 ILE N N 119.54 . 1 249 142 142 ALA H H 9.19 . 1 250 142 142 ALA N N 117.13 . 1 251 143 143 GLY H H 7.5 . 1 252 143 143 GLY N N 111.58 . 1 253 144 144 GLU H H 8.58 . 1 254 144 144 GLU N N 121.68 . 1 255 145 145 LYS H H 7.8 . 1 256 145 145 LYS N N 116.8 . 1 257 146 146 ILE H H 7.63 . 1 258 146 146 ILE N N 124.2 . 1 259 147 147 THR H H 9.24 . 1 260 147 147 THR N N 115.51 . 1 261 148 148 ALA H H 9.41 . 1 262 148 148 ALA N N 122.99 . 1 263 149 149 VAL H H 8.36 . 1 264 149 149 VAL N N 118.27 . 1 265 150 150 ASP H H 7.4 . 1 266 150 150 ASP N N 120.1 . 1 267 151 151 LEU H H 7.13 . 1 268 151 151 LEU N N 114.92 . 1 269 152 152 SER H H 7.45 . 1 270 152 152 SER N N 108.55 . 1 271 153 153 LEU H H 8.24 . 1 272 153 153 LEU N N 119.51 . 1 273 154 154 ALA H H 8.78 . 1 274 154 154 ALA N N 120.74 . 1 275 156 156 LYS H H 6.57 . 1 276 156 156 LYS N N 114.01 . 1 277 157 157 LEU H H 8.63 . 1 278 157 157 LEU N N 118.4 . 1 279 158 158 TYR H H 8.17 . 1 280 158 158 TYR N N 121.00 . 1 281 159 159 HIS H H 7.86 . 1 282 159 159 HIS N N 117.6 . 1 283 160 160 LEU H H 7.43 . 1 284 160 160 LEU N N 118.59 . 1 285 161 161 GLU H H 8.29 . 1 286 161 161 GLU N N 118.38 . 1 287 162 162 VAL H H 8.36 . 1 288 162 162 VAL N N 119.05 . 1 289 163 163 ALA H H 9.26 . 1 290 163 163 ALA N N 120.75 . 1 291 164 164 LEU H H 8.5 . 1 292 164 164 LEU N N 115.49 . 1 293 165 165 GLY H H 7.67 . 1 294 165 165 GLY N N 107.5 . 1 295 166 166 HIS H H 7.71 . 1 296 166 166 HIS N N 117.39 . 1 297 167 167 PHE H H 8.74 . 1 298 167 167 PHE N N 112.27 . 1 299 168 168 LYS H H 6.98 . 1 300 168 168 LYS N N 112.87 . 1 301 169 169 ASN H H 7.06 . 1 302 169 169 ASN N N 117.88 . 1 303 170 170 TRP H H 7.56 . 1 304 170 170 TRP N N 121.74 . 1 305 174 174 ASP H H 7.79 . 1 306 174 174 ASP N N 119.6 . 1 307 175 175 ASN H H 7.65 . 1 308 175 175 ASN N N 112.31 . 1 309 176 176 LEU H H 7.58 . 1 310 176 176 LEU N N 125.66 . 1 311 177 177 THR H H 7.45 . 1 312 177 177 THR N N 110.62 . 1 313 178 178 HIS H H 9.02 . 1 314 178 178 HIS N N 122.14 . 1 315 179 179 VAL H H 8.29 . 1 316 179 179 VAL N N 123.44 . 1 317 180 180 LEU H H 8.06 . 1 318 180 180 LEU N N 118.64 . 1 319 181 181 ASN H H 7.76 . 1 320 181 181 ASN N N 118.39 . 1 321 182 182 TYR H H 7.78 . 1 322 182 182 TYR N N 123.06 . 1 323 183 183 ILE H H 8.01 . 1 324 183 183 ILE N N 115.66 . 1 325 184 184 LYS H H 7.17 . 1 326 184 184 LYS N N 118.44 . 1 327 185 185 LEU H H 7.7 . 1 328 185 185 LEU N N 119.9 . 1 329 186 186 LEU H H 8.1 . 1 330 186 186 LEU N N 119.76 . 1 331 187 187 PHE H H 8.36 . 1 332 187 187 PHE N N 114.87 . 1 333 188 188 SER H H 7.19 . 1 334 188 188 SER N N 109.97 . 1 335 189 189 ARG H H 7.22 . 1 336 189 189 ARG N N 122.64 . 1 337 190 190 GLU H H 8.99 . 1 338 190 190 GLU N N 125.17 . 1 339 191 191 SER H H 8.42 . 1 340 191 191 SER N N 112.38 . 1 341 192 192 PHE H H 6.8 . 1 342 192 192 PHE N N 126.07 . 1 343 193 193 LYS H H 8.14 . 1 344 193 193 LYS N N 118.59 . 1 345 194 194 LYS H H 7.94 . 1 346 194 194 LYS N N 113.92 . 1 347 195 195 THR H H 6.88 . 1 348 195 195 THR N N 105.01 . 1 349 196 196 ARG H H 6.81 . 1 350 196 196 ARG N N 120.91 . 1 351 197 197 ALA H H 8.1 . 1 352 197 197 ALA N N 125.84 . 1 353 198 198 ALA H H 9.1 . 1 354 198 198 ALA N N 125.25 . 1 355 199 199 GLU H H 9.84 . 1 356 199 199 GLU N N 125.1 . 1 357 200 200 GLU H H 9.25 . 1 358 200 200 GLU N N 114.67 . 1 359 201 201 HIS H H 7.38 . 1 360 201 201 HIS N N 121.13 . 1 361 202 202 VAL H H 7.57 . 1 362 202 202 VAL N N 124.96 . 1 363 203 203 ILE H H 8.06 . 1 364 203 203 ILE N N 118.64 . 1 365 204 204 ALA H H 7.79 . 1 366 204 204 ALA N N 119.6 . 1 367 205 205 GLY H H 7.61 . 1 368 205 205 GLY N N 103.1 . 1 369 206 206 TRP H H 7.59 . 1 370 206 206 TRP N N 118.78 . 1 371 209 209 LYS H H 7.61 . 1 372 209 209 LYS N N 115.89 . 1 373 211 211 ASN H H 8.28 . 1 374 211 211 ASN N N 115.64 . 1 375 212 212 ALA H H 7.71 . 1 376 212 212 ALA N N 123.34 . 1 stop_ save_