data_6520 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; 1H, 15N Chemical shift assignments for recombinant elicitor protein PcF from the oomycete pathogen P. cactorum ; _BMRB_accession_number 6520 _BMRB_flat_file_name bmr6520.str _Entry_type original _Submission_date 2005-02-21 _Accession_date 2005-02-21 _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 Nicastro Giuseppe . . 2 Orsomando Giuseppe . . 3 Desario F. . . 4 Ferrari Elena . . 5 Manconi L. . . 6 Spisni Alberto . . 7 Ruggeri Silverio . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 281 "15N chemical shifts" 49 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2009-05-27 original author . stop_ save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; The solution structure of the recombinant elicitor protein PcF from the oomycete pathogen P. cactorum displays a helix-loop-helix fold and reveals calcium binding ability ; _Citation_status 'in preparation' _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID ? loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Nicastro G. . . 2 Orsomando Giuseppe . . 3 Desario F. . . 4 Ferrari E. . . 5 Manconi L. . . 6 Spisni Alberto . . 7 Ruggeri Silverio . . stop_ _Journal_abbreviation . _Journal_volume . _Journal_issue . _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first . _Page_last . _Year . _Details . save_ ####################################### # Cited references within the entry # ####################################### save_Phytophthora_cactorum _Saveframe_category citation _Citation_full ; PcF protein from Phytophthora cactorum and its recombinant homologue elicit phenylalanine ammonia lyase activation in tomato. Cell Mol Life Sci. 2003 Jul;60(7):1470-6. ; _Citation_title 'PcF protein from Phytophthora cactorum and its recombinant homologue elicit phenylalanine ammonia lyase activation in tomato.' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 12943233 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Orsomando Giuseppe . . 2 Lorenzi M. . . 3 Ferrari E. . . 4 'de Chiara' C. . . 5 Spisni Alberto . . 6 Ruggeri Silverio . . stop_ _Journal_abbreviation 'Cell. Mol. Life Sci.' _Journal_name_full . _Journal_volume 60 _Journal_issue 7 _Journal_CSD . _Book_title . _Book_chapter_title . _Book_volume . _Book_series . _Book_publisher . _Book_publisher_city . _Book_ISBN . _Conference_title . _Conference_site . _Conference_state_province . _Conference_country . _Conference_start_date . _Conference_end_date . _Conference_abstract_number . _Thesis_institution . _Thesis_institution_city . _Thesis_institution_country . _Page_first 1470 _Page_last 1476 _Year 2003 _Details . loop_ _Keyword NMR stop_ save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name 'Pcf monomer' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'Pcf monomer' $elicitor_protein stop_ _System_molecular_weight 6214 _System_physical_state native _System_oligomer_state ? _System_paramagnetic no _System_thiol_state 'all disulfide bound' _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_elicitor_protein _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'elicitor protein Pcf from the oomycete pathogen P. cactorum' _Molecular_mass 6214 _Mol_thiol_state 'all disulfide bound' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 52 _Mol_residue_sequence ; EDPLYCQAIGCPTLYSEANL AVSKECRDQGKLGDDFHRCC EEQCGSTTPASA ; loop_ _Residue_seq_code _Residue_label 1 GLU 2 ASP 3 PRO 4 LEU 5 TYR 6 CYS 7 GLN 8 ALA 9 ILE 10 GLY 11 CYS 12 PRO 13 THR 14 LEU 15 TYR 16 SER 17 GLU 18 ALA 19 ASN 20 LEU 21 ALA 22 VAL 23 SER 24 LYS 25 GLU 26 CYS 27 ARG 28 ASP 29 GLN 30 GLY 31 LYS 32 LEU 33 GLY 34 ASP 35 ASP 36 PHE 37 HIS 38 ARG 39 CYS 40 CYS 41 GLU 42 GLU 43 GLN 44 CYS 45 GLY 46 SER 47 THR 48 THR 49 PRO 50 ALA 51 SER 52 ALA stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date . save_ ######################################## # Molecular bond linkage definitions # ######################################## save_crosslink_bonds _Saveframe_category crosslink_bonds loop_ _Bond_order _Bond_type _Atom_one_mol_system_component_name _Atom_one_residue_seq_code _Atom_one_residue_label _Atom_one_atom_name _Atom_two_mol_system_component_name _Atom_two_residue_seq_code _Atom_two_residue_label _Atom_two_atom_name single disulfide 'Pcf monomer' 6 CYS SG 'Pcf monomer' 40 CYS SG single disulfide 'Pcf monomer' 11 CYS SG 'Pcf monomer' 44 CYS SG single disulfide 'Pcf monomer' 26 CYS SG 'Pcf monomer' 39 CYS SG stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $elicitor_protein 'Pichia Pastoris' 4922 Eukaryota Fungi Phytophthora cactorum 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 $elicitor_protein 'recombinant technology' 'Pichia pastoris' . . . . 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 $elicitor_protein 0.65 mM [U-15N] stop_ save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model INOVA _Field_strength 600 _Details . save_ ############################# # NMR applied experiments # ############################# save_3D-TOCSY-HSQC_1 _Saveframe_category NMR_applied_experiment _Experiment_name 3D-TOCSY-HSQC _Sample_label . save_ save_3D-NOESY-HSQC_2 _Saveframe_category NMR_applied_experiment _Experiment_name 3D-NOESY-HSQC _Sample_label . save_ save_2D-NOESY_3 _Saveframe_category NMR_applied_experiment _Experiment_name 2D-NOESY _Sample_label . save_ save_2D-TOSCY_4 _Saveframe_category NMR_applied_experiment _Experiment_name 2D-TOSCY _Sample_label . save_ save_2D-HSQC-15N_5 _Saveframe_category NMR_applied_experiment _Experiment_name 2D-HSQC-15N _Sample_label . save_ ####################### # Sample conditions # ####################### save_conditions_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 5.0 0.1 pH temperature 293 0.5 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 DSS H 1 'methyl protons' ppm 0 internal direct . . . 1 DSS N 15 'methyl protons' ppm 0 . indirect . . . 0.101329118 DSS C 13 'methyl protons' ppm 0 . indirect . . . 0.251449530 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 '1H and 15N assignments' loop_ _Experiment_label NMR_experiment_list stop_ loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $conditions_1 _Chem_shift_reference_set_label $chemical_shift_referencing _Mol_system_component_name 'Pcf monomer' _Text_data_format . _Text_data . loop_ _Atom_shift_assign_ID _Residue_author_seq_code _Residue_seq_code _Residue_label _Atom_name _Atom_type _Chem_shift_value _Chem_shift_value_error _Chem_shift_ambiguity_code 1 . 1 GLU H H 8.22 . . 2 . 1 GLU HA H 4.21 . . 3 . 1 GLU HB2 H 1.96 . . 4 . 1 GLU HB3 H 1.36 . . 5 . 1 GLU HG2 H 2.44 . . 6 . 1 GLU HG3 H 2.10 . . 7 . 1 GLU N N 128.4 . . 8 . 2 ASP H H 8.22 . . 9 . 2 ASP HA H 4.51 . . 10 . 2 ASP HB2 H 2.85 . . 11 . 2 ASP HB3 H 2.85 . . 12 . 2 ASP N N 124.9 . . 13 . 3 PRO HA H 4.20 . . 14 . 3 PRO HB2 H 2.17 . . 15 . 3 PRO HB3 H 1.38 . . 16 . 3 PRO HG2 H 2.42 . . 17 . 3 PRO HG3 H 1.97 . . 18 . 3 PRO HD2 H 3.63 . . 19 . 3 PRO HD3 H 3.74 . . 20 . 4 LEU H H 8.11 . . 21 . 4 LEU HA H 4.05 . . 22 . 4 LEU HB2 H 1.11 . . 23 . 4 LEU HB3 H 1.11 . . 24 . 4 LEU HG H 0.66 . . 25 . 4 LEU HD1 H 0.5 . . 26 . 4 LEU HD2 H 0.37 . . 27 . 4 LEU N N 120.36 . . 28 . 5 TYR H H 8.24 . . 29 . 5 TYR HA H 5.19 . . 30 . 5 TYR HB2 H 3.22 . . 31 . 5 TYR HB3 H 2.49 . . 32 . 5 TYR HD1 H 7.09 . . 33 . 5 TYR HD2 H 7.09 . . 34 . 5 TYR HE1 H 6.88 . . 35 . 5 TYR HE2 H 6.88 . . 36 . 5 TYR N N 119.11 . . 37 . 6 CYS H H 9.1 . . 38 . 6 CYS HA H 4.92 . . 39 . 6 CYS HB2 H 3.11 . . 40 . 6 CYS HB3 H 2.47 . . 41 . 6 CYS N N 120.36 . . 42 . 7 GLN H H 9.20 . . 43 . 7 GLN HA H 4.54 . . 44 . 7 GLN HB2 H 1.98 . . 45 . 7 GLN HB3 H 1.98 . . 46 . 7 GLN HG2 H 2.40 . . 47 . 7 GLN HG3 H 2.40 . . 48 . 7 GLN HE21 H 7.61 . . 49 . 7 GLN HE22 H 6.97 . . 50 . 7 GLN N N 123.48 . . 51 . 8 ALA H H 6.80 . . 52 . 8 ALA HA H 4.36 . . 53 . 8 ALA HB H 1.33 . . 54 . 8 ALA N N 123.9 . . 55 . 9 ILE H H 8.50 . . 56 . 9 ILE HA H 3.85 . . 57 . 9 ILE HB H 1.80 . . 58 . 9 ILE HG12 H 1.65 . . 59 . 9 ILE HG13 H 1.65 . . 60 . 9 ILE HG2 H 0.95 . . 61 . 9 ILE HD1 H 1.30 . . 62 . 9 ILE N N 123.06 . . 63 . 10 GLY H H 8.82 . . 64 . 10 GLY HA2 H 4.41 . . 65 . 10 GLY HA3 H 3.65 . . 66 . 10 GLY N N 115.17 . . 67 . 11 CYS H H 8.15 . . 68 . 11 CYS HA H 4.90 . . 69 . 11 CYS HB2 H 3.14 . . 70 . 11 CYS HB3 H 2.79 . . 71 . 11 CYS N N 118.07 . . 72 . 12 PRO HA H 4.56 . . 73 . 12 PRO HB2 H 2.50 . . 74 . 12 PRO HB3 H 1.76 . . 75 . 12 PRO HG2 H 2.06 . . 76 . 12 PRO HG3 H 1.63 . . 77 . 12 PRO HD2 H 3.57 . . 78 . 12 PRO HD3 H 4.08 . . 79 . 13 THR H H 8.41 . . 80 . 13 THR HA H 3.96 . . 81 . 13 THR HB H 4.01 . . 82 . 13 THR HG2 H 1.34 . . 83 . 13 THR N N 116.0 . . 84 . 14 LEU H H 8.52 . . 85 . 14 LEU HA H 3.46 . . 86 . 14 LEU HB2 H 1.28 . . 87 . 14 LEU HB3 H 1.28 . . 88 . 14 LEU HG H 0.82 . . 89 . 14 LEU HD1 H 0.62 . . 90 . 14 LEU HD2 H 0.55 . . 91 . 14 LEU N N 128.05 . . 92 . 15 TYR H H 8.38 . . 93 . 15 TYR HA H 4.81 . . 94 . 15 TYR HB2 H 3.24 . . 95 . 15 TYR HB3 H 3.24 . . 96 . 15 TYR HD1 H 6.66 . . 97 . 15 TYR HD2 H 6.66 . . 98 . 15 TYR HE1 H 6.83 . . 99 . 15 TYR HE2 H 6.83 . . 100 . 15 TYR N N 115.37 . . 101 . 16 SER H H 7.91 . . 102 . 16 SER HA H 4.50 . . 103 . 16 SER HB2 H 4.31 . . 104 . 16 SER HB3 H 4.03 . . 105 . 16 SER N N 114.95 . . 106 . 17 GLU H H 9.21 . . 107 . 17 GLU HA H 4.07 . . 108 . 17 GLU HB2 H 2.19 . . 109 . 17 GLU HB3 H 2.19 . . 110 . 17 GLU HG2 H 2.53 . . 111 . 17 GLU HG3 H 2.59 . . 112 . 17 GLU N N 123.48 . . 113 . 18 ALA H H 8.84 . . 114 . 18 ALA HA H 4.30 . . 115 . 18 ALA HB H 1.49 . . 116 . 18 ALA N N 120.15 . . 117 . 19 ASN H H 7.90 . . 118 . 19 ASN HA H 4.14 . . 119 . 19 ASN HB2 H 2.64 . . 120 . 19 ASN HB3 H 2.405 . . 121 . 19 ASN HD21 H 7.43 . . 122 . 19 ASN HD22 H 7.70 . . 123 . 19 ASN N N 118.7 . . 124 . 20 LEU H H 8.81 . . 125 . 20 LEU HA H 4.11 . . 126 . 20 LEU HB2 H 2.02 . . 127 . 20 LEU HB3 H 1.80 . . 128 . 20 LEU HG H 1.65 . . 129 . 20 LEU HD1 H 0.98 . . 130 . 20 LEU HD2 H 0.92 . . 131 . 20 LEU N N 123.27 . . 132 . 21 ALA H H 8.09 . . 133 . 21 ALA HA H 4.23 . . 134 . 21 ALA HB H 1.54 . . 135 . 21 ALA N N 121.2 . . 136 . 22 VAL H H 7.82 . . 137 . 22 VAL HA H 4.11 . . 138 . 22 VAL HB H 2.13 . . 139 . 22 VAL HG1 H 1.13 . . 140 . 22 VAL HG2 H 1.09 . . 141 . 22 VAL N N 118.9 . . 142 . 23 SER H H 8.55 . . 143 . 23 SER HA H 4.55 . . 144 . 23 SER HB2 H 4.38 . . 145 . 23 SER HB3 H 4.38 . . 146 . 23 SER N N 118.07 . . 147 . 24 LYS H H 8.10 . . 148 . 24 LYS HA H 3.94 . . 149 . 24 LYS HB2 H 2.08 . . 150 . 24 LYS HB3 H 2.08 . . 151 . 24 LYS HG2 H 1.49 . . 152 . 24 LYS HG3 H 1.49 . . 153 . 24 LYS N N 122.23 . . 154 . 25 GLU H H 7.77 . . 155 . 25 GLU HA H 4.14 . . 156 . 25 GLU HB2 H 2.27 . . 157 . 25 GLU HB3 H 2.27 . . 158 . 25 GLU HG2 H 2.48 . . 159 . 25 GLU HG3 H 2.43 . . 160 . 25 GLU N N 118.49 . . 161 . 26 CYS H H 8.07 . . 162 . 26 CYS HA H 4.67 . . 163 . 26 CYS HB2 H 2.62 . . 164 . 26 CYS HB3 H 2.62 . . 165 . 26 CYS N N 116.2 . . 166 . 27 ARG H H 8.92 . . 167 . 27 ARG HA H 4.37 . . 168 . 27 ARG HB2 H 2.09 . . 169 . 27 ARG HB3 H 1.93 . . 170 . 27 ARG HG2 H 1.51 . . 171 . 27 ARG HG3 H 1.51 . . 172 . 27 ARG HD2 H 3.40 . . 173 . 27 ARG HD3 H 3.17 . . 174 . 27 ARG HE H 7.30 . . 175 . 27 ARG N N 123.06 . . 176 . 28 ASP H H 8.74 . . 177 . 28 ASP HA H 4.56 . . 178 . 28 ASP HB2 H 3.00 . . 179 . 28 ASP HB3 H 2.88 . . 180 . 28 ASP N N 120.36 . . 181 . 29 GLN H H 7.65 . . 182 . 29 GLN HA H 4.33 . . 183 . 29 GLN HB2 H 2.38 . . 184 . 29 GLN HB3 H 2.15 . . 185 . 29 GLN HG2 H 2.66 . . 186 . 29 GLN HG3 H 2.44 . . 187 . 29 GLN HE21 H 7.38 . . 188 . 29 GLN HE22 H 6.78 . . 189 . 29 GLN N N 117.87 . . 190 . 30 GLY H H 8.33 . . 191 . 30 GLY HA2 H 4.03 . . 192 . 30 GLY HA3 H 4.03 . . 193 . 30 GLY N N 108.5 . . 194 . 31 LYS H H 7.40 . . 195 . 31 LYS HA H 4.41 . . 196 . 31 LYS HB2 H 1.92 . . 197 . 31 LYS HB3 H 1.92 . . 198 . 31 LYS HG2 H 1.62 . . 199 . 31 LYS HG3 H 1.62 . . 200 . 31 LYS HD2 H 1.48 . . 201 . 31 LYS HD3 H 1.48 . . 202 . 31 LYS HE2 H 3.00 . . 203 . 31 LYS HE3 H 3.00 . . 204 . 31 LYS N N 118.91 . . 205 . 32 LEU H H 8.33 . . 206 . 32 LEU HA H 4.54 . . 207 . 32 LEU HB2 H 1.77 . . 208 . 32 LEU HB3 H 1.77 . . 209 . 32 LEU HG H 1.63 . . 210 . 32 LEU HD1 H 0.9 . . 211 . 32 LEU HD2 H 0.9 . . 212 . 32 LEU N N 122.4 . . 213 . 33 GLY H H 8.35 . . 214 . 33 GLY HA2 H 4.07 . . 215 . 33 GLY HA3 H 3.81 . . 216 . 33 GLY N N 108.52 . . 217 . 34 ASP H H 8.83 . . 218 . 34 ASP HA H 4.64 . . 219 . 34 ASP HB2 H 2.78 . . 220 . 34 ASP HB3 H 2.78 . . 221 . 34 ASP N N 124.72 . . 222 . 35 ASP H H 7.98 . . 223 . 35 ASP HA H 3.90 . . 224 . 35 ASP HB2 H 3.02 . . 225 . 35 ASP HB3 H 2.94 . . 226 . 35 ASP N N 125.14 . . 227 . 36 PHE H H 8.38 . . 228 . 36 PHE HA H 4.55 . . 229 . 36 PHE HB2 H 3.06 . . 230 . 36 PHE HB3 H 2.76 . . 231 . 36 PHE HD1 H 6.82 . . 232 . 36 PHE HD2 H 6.82 . . 233 . 36 PHE HE1 H 7.17 . . 234 . 36 PHE HE2 H 7.17 . . 235 . 36 PHE HZ H 6.90 . . 236 . 36 PHE N N 120.15 . . 237 . 37 HIS H H 8.13 . . 238 . 37 HIS HA H 4.35 . . 239 . 37 HIS HB2 H 3.45 . . 240 . 37 HIS HB3 H 3.45 . . 241 . 37 HIS HD2 H 7.48 . . 242 . 37 HIS HE1 H 8.75 . . 243 . 37 HIS N N 117.24 . . 244 . 38 ARG H H 8.34 . . 245 . 38 ARG HA H 3.96 . . 246 . 38 ARG HB2 H 1.89 . . 247 . 38 ARG HB3 H 1.76 . . 248 . 38 ARG HG2 H 1.64 . . 249 . 38 ARG HG3 H 1.64 . . 250 . 38 ARG HD2 H 3.24 . . 251 . 38 ARG HD3 H 3.24 . . 252 . 38 ARG HE H 7.34 . . 253 . 38 ARG N N 119.74 . . 254 . 39 CYS H H 7.88 . . 255 . 39 CYS HA H 4.26 . . 256 . 39 CYS HB2 H 3.18 . . 257 . 39 CYS HB3 H 3.03 . . 258 . 39 CYS N N 120.36 . . 259 . 40 CYS H H 8.32 . . 260 . 40 CYS HA H 3.93 . . 261 . 40 CYS HB2 H 3.09 . . 262 . 40 CYS HB3 H 2.50 . . 263 . 40 CYS N N 120.98 . . 264 . 41 GLU H H 8.08 . . 265 . 41 GLU HA H 3.70 . . 266 . 41 GLU HB2 H 2.15 . . 267 . 41 GLU HB3 H 2.15 . . 268 . 41 GLU HG2 H 2.31 . . 269 . 41 GLU HG3 H 2.31 . . 270 . 41 GLU N N 118.5 . . 271 . 42 GLU H H 8.03 . . 272 . 42 GLU HA H 4.05 . . 273 . 42 GLU HB2 H 2.24 . . 274 . 42 GLU HB3 H 2.15 . . 275 . 42 GLU HG2 H 2.57 . . 276 . 42 GLU HG3 H 2.43 . . 277 . 42 GLU N N 117.6 . . 278 . 43 GLN H H 8.81 . . 279 . 43 GLN HA H 4.14 . . 280 . 43 GLN HB2 H 2.11 . . 281 . 43 GLN HB3 H 1.85 . . 282 . 43 GLN HG2 H 2.64 . . 283 . 43 GLN HG3 H 2.32 . . 284 . 43 GLN HE21 H 7.24 . . 285 . 43 GLN HE22 H 6.84 . . 286 . 43 GLN N N 116.83 . . 287 . 44 CYS H H 8.76 . . 288 . 44 CYS HA H 4.55 . . 289 . 44 CYS HB2 H 3.37 . . 290 . 44 CYS HB3 H 3.06 . . 291 . 44 CYS N N 113.92 . . 292 . 45 GLY H H 7.67 . . 293 . 45 GLY HA2 H 4.18 . . 294 . 45 GLY HA3 H 3.89 . . 295 . 45 GLY N N 107.9 . . 296 . 46 SER H H 8.18 . . 297 . 46 SER HA H 4.57 . . 298 . 46 SER HB2 H 3.90 . . 299 . 46 SER HB3 H 3.90 . . 300 . 46 SER N N 115.37 . . 301 . 47 THR H H 8.20 . . 302 . 47 THR HA H 4.42 . . 303 . 47 THR HB H 4.27 . . 304 . 47 THR HG2 H 1.20 . . 305 . 47 THR N N 115.79 . . 306 . 48 THR H H 8.25 . . 307 . 48 THR HA H 4.65 . . 308 . 48 THR HB H 4.14 . . 309 . 48 THR HG2 H 1.25 . . 310 . 48 THR N N 119.53 . . 311 . 49 PRO HA H 4.39 . . 312 . 49 PRO HB2 H 2.30 . . 313 . 49 PRO HB3 H 2.30 . . 314 . 49 PRO HG2 H 2.03 . . 315 . 49 PRO HG3 H 1.95 . . 316 . 49 PRO HD2 H 3.87 . . 317 . 49 PRO HD3 H 3.69 . . 318 . 50 ALA H H 8.45 . . 319 . 50 ALA HA H 4.31 . . 320 . 50 ALA HB H 1.41 . . 321 . 50 ALA N N 124.7 . . 322 . 51 SER H H 8.24 . . 323 . 51 SER HA H 3.97 . . 324 . 51 SER HB2 H 3.85 . . 325 . 51 SER HB3 H 3.60 . . 326 . 51 SER N N 122.4 . . 327 . 52 ALA H H 8.12 . . 328 . 52 ALA HA H 4.23 . . 329 . 52 ALA HB H 1.4 . . 330 . 52 ALA N N 129.95 . . stop_ save_