data_19237 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Solution structure of AhPDF1 from Arabidopsis halleri ; _BMRB_accession_number 19237 _BMRB_flat_file_name bmr19237.str _Entry_type original _Submission_date 2013-05-13 _Accession_date 2013-05-13 _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 Meindre Fanny . . 2 Paquet Francoise . . 3 Landon Celine . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 306 "13C chemical shifts" 128 "15N chemical shifts" 30 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2014-05-12 original author . stop_ _Original_release_date 2014-05-12 save_ ############################# # Citation for this entry # ############################# save_Citation_1 _Saveframe_category entry_citation _Citation_full . _Citation_title 'Folding and structural studies of the protein AhPDF1' _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 Meindre Fanny . . 2 Paquet Francoise . . 3 Landon Celine . . 4 Meindre Fanny . . 5 Paquet Francoise . . 6 Landon Celine . . stop_ _Journal_abbreviation 'Not known' _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_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name 'AhPDF1 from Arabidopsis halleri' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'AhPDF1 from Arabidopsis halleri' $AhPDF1 stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state ? _System_paramagnetic no _System_thiol_state . _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_AhPDF1 _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common AhPDF1 _Molecular_mass 5699.622 _Mol_thiol_state . _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 51 _Mol_residue_sequence ; XRLCEKPSGTWSGVCGNNGA CRNQCIRLEKARHGSCNYVF PAHKCICYFPC ; loop_ _Residue_seq_code _Residue_label 1 PCA 2 ARG 3 LEU 4 CYS 5 GLU 6 LYS 7 PRO 8 SER 9 GLY 10 THR 11 TRP 12 SER 13 GLY 14 VAL 15 CYS 16 GLY 17 ASN 18 ASN 19 GLY 20 ALA 21 CYS 22 ARG 23 ASN 24 GLN 25 CYS 26 ILE 27 ARG 28 LEU 29 GLU 30 LYS 31 ALA 32 ARG 33 HIS 34 GLY 35 SER 36 CYS 37 ASN 38 TYR 39 VAL 40 PHE 41 PRO 42 ALA 43 HIS 44 LYS 45 CYS 46 ILE 47 CYS 48 TYR 49 PHE 50 PRO 51 CYS stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2014-11-09 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 PDB 2M8B "Solution Structure Of Ahpdf1 From Arabidopsis Halleri" 98.04 51 100.00 100.00 6.67e-28 EMBL CCN97877 "defensin [Arabidopsis halleri subsp. halleri]" 98.04 80 100.00 100.00 3.44e-29 GB AAY27736 "putative plant defensin PDF1.1 [Arabidopsis halleri]" 98.04 80 100.00 100.00 3.44e-29 stop_ save_ ###################### # Polymer residues # ###################### save_chem_comp_PCA _Saveframe_category polymer_residue _Mol_type 'L-PEPTIDE LINKING' _Name_common 'PYROGLUTAMIC ACID' _BMRB_code PCA _PDB_code PCA _Standard_residue_derivative . _Molecular_mass 129.114 _Mol_paramagnetic no _Details . loop_ _Atom_name _PDB_atom_name _Atom_type _Atom_chirality _Atom_charge _Atom_oxidation_number _Atom_unpaired_electrons N N N . 0 . ? CA CA C . 0 . ? CB CB C . 0 . ? CG CG C . 0 . ? CD CD C . 0 . ? OE OE O . 0 . ? C C C . 0 . ? O O O . 0 . ? OXT OXT O . 0 . ? H H H . 0 . ? HA HA H . 0 . ? HB2 HB2 H . 0 . ? HB3 HB3 H . 0 . ? HG2 HG2 H . 0 . ? HG3 HG3 H . 0 . ? HXT HXT 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 N CA ? ? SING N CD ? ? SING N H ? ? SING CA CB ? ? SING CA C ? ? SING CA HA ? ? SING CB CG ? ? SING CB HB2 ? ? SING CB HB3 ? ? SING CG CD ? ? SING CG HG2 ? ? SING CG HG3 ? ? DOUB CD OE ? ? DOUB C O ? ? SING C OXT ? ? SING OXT HXT ? ? stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $AhPDF1 Eudicots 81970 Eukaryota Metazoa Arabidopsis halleri 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 $AhPDF1 'chemical synthesis' . . . . . 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 $AhPDF1 1.3 mM 'natural abundance' H2O 90 % 'natural abundance' D2O 10 % 'natural abundance' stop_ save_ save_sample_2 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $AhPDF1 1.3 mM 'natural abundance' D2O 100 % 'natural abundance' stop_ save_ ############################ # Computer software used # ############################ save_CCPNMR _Saveframe_category software _Name CcpNMR _Version 2.2.2 loop_ _Vendor _Address _Electronic_address CCPN . . stop_ loop_ _Task 'chemical shift assignment' 'peak picking' stop_ _Details . save_ save_NMRPipe _Saveframe_category software _Name NMRPipe _Version . loop_ _Vendor _Address _Electronic_address 'Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax' . . stop_ loop_ _Task processing stop_ _Details . save_ save_ARIA _Saveframe_category software _Name ARIA _Version 2.3 loop_ _Vendor _Address _Electronic_address 'Linge, O'Donoghue and Nilges' . . stop_ loop_ _Task refinement 'structure solution' stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model INOVA _Field_strength 600 _Details . save_ ############################# # NMR applied experiments # ############################# save_2D_1H-1H_COSY_1 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-1H COSY' _Sample_label $sample_1 save_ save_2D_1H-1H_TOCSY_2 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-1H TOCSY' _Sample_label $sample_1 save_ save_2D_1H-1H_NOESY_3 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-1H NOESY' _Sample_label $sample_1 save_ save_2D_1H-15N_HSQC_4 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-15N HSQC' _Sample_label $sample_1 save_ save_2D_1H-13C_HSQC_5 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-13C HSQC' _Sample_label $sample_1 save_ save_2D_1H-1H_TOCSY_6 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-1H TOCSY' _Sample_label $sample_2 save_ save_2D_1H-1H_NOESY_7 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-1H NOESY' _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 pH 4.5 . pH pressure 1 . atm temperature 273 . K stop_ save_ save_sample_conditions_2 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 4.5 . pH pressure 1 . atm temperature 273 . K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_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 C 13 'methyl carbon' ppm 0 internal direct . . . 0.251449530 DSS H 1 'methyl protons' ppm 0 internal direct . . . 1.0 water N 15 protons ppm 0 internal indirect . . . 0.101329118 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_chem_shift_list_1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Experiment_label '2D 1H-1H COSY' '2D 1H-1H TOCSY' '2D 1H-1H NOESY' '2D 1H-15N HSQC' '2D 1H-13C HSQC' stop_ loop_ _Sample_label $sample_1 $sample_2 stop_ _Sample_conditions_label $sample_conditions_1 _Chem_shift_reference_set_label $chemical_shift_reference_1 _Mol_system_component_name 'AhPDF1 from Arabidopsis halleri' _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 PCA CA C 63.042 . . 2 1 1 PCA HA H 3.734 . . 3 1 1 PCA HB2 H 1.936 . . 4 1 1 PCA HB3 H 1.937 . . 5 1 1 PCA HG2 H 0.867 . . 6 1 1 PCA HG3 H 0.574 . . 7 2 2 ARG H H 8.372 . . 8 2 2 ARG HA H 4.361 . . 9 2 2 ARG HB2 H 1.924 . . 10 2 2 ARG HB3 H 1.796 . . 11 2 2 ARG HG2 H 1.924 . . 12 2 2 ARG HG3 H 1.703 . . 13 2 2 ARG HD2 H 3.243 . . 14 2 2 ARG HD3 H 3.243 . . 15 2 2 ARG HE H 7.206 . . 16 3 3 LEU H H 8.460 . . 17 3 3 LEU HA H 5.129 . . 18 3 3 LEU HB2 H 1.369 . . 19 3 3 LEU HB3 H 1.818 . . 20 3 3 LEU HG H 1.681 . . 21 3 3 LEU HD1 H 0.682 . . 22 3 3 LEU HD2 H 0.694 . . 23 3 3 LEU CA C 54.667 . . 24 3 3 LEU CB C 46.077 . . 25 3 3 LEU CD1 C 24.055 . . 26 3 3 LEU CD2 C 24.055 . . 27 4 4 CYS H H 9.717 . . 28 4 4 CYS HA H 5.134 . . 29 4 4 CYS HB2 H 2.996 . . 30 4 4 CYS HB3 H 2.996 . . 31 4 4 CYS CA C 60.428 . . 32 4 4 CYS N N 122.129 . . 33 5 5 GLU H H 8.801 . . 34 5 5 GLU HA H 4.479 . . 35 5 5 GLU HB2 H 1.666 . . 36 5 5 GLU HB3 H 1.666 . . 37 5 5 GLU HG2 H 2.050 . . 38 5 5 GLU HG3 H 1.865 . . 39 5 5 GLU CG C 36.907 . . 40 5 5 GLU N N 122.663 . . 41 6 6 LYS H H 9.057 . . 42 6 6 LYS HA H 4.762 . . 43 6 6 LYS HB2 H 1.882 . . 44 6 6 LYS HB3 H 1.789 . . 45 6 6 LYS HG2 H 1.476 . . 46 6 6 LYS HG3 H 1.410 . . 47 6 6 LYS HD2 H 1.566 . . 48 6 6 LYS HD3 H 1.475 . . 49 6 6 LYS HE2 H 2.769 . . 50 6 6 LYS HE3 H 2.769 . . 51 6 6 LYS HZ H 7.384 . . 52 6 6 LYS CB C 36.955 . . 53 6 6 LYS CG C 25.673 . . 54 6 6 LYS CD C 30.109 . . 55 7 7 PRO HA H 4.468 . . 56 7 7 PRO HB2 H 2.308 . . 57 7 7 PRO HB3 H 1.914 . . 58 7 7 PRO HG2 H 2.154 . . 59 7 7 PRO HG3 H 1.916 . . 60 7 7 PRO HD2 H 3.634 . . 61 7 7 PRO HD3 H 3.869 . . 62 7 7 PRO CA C 64.390 . . 63 7 7 PRO CB C 32.996 . . 64 7 7 PRO CG C 28.879 . . 65 7 7 PRO CD C 51.658 . . 66 8 8 SER H H 8.628 . . 67 8 8 SER HA H 4.751 . . 68 8 8 SER HB2 H 4.110 . . 69 8 8 SER HB3 H 3.704 . . 70 8 8 SER CA C 59.388 . . 71 8 8 SER CB C 65.016 . . 72 9 9 GLY H H 10.642 . . 73 9 9 GLY HA2 H 4.416 . . 74 9 9 GLY HA3 H 3.912 . . 75 9 9 GLY CA C 46.276 . . 76 9 9 GLY N N 119.742 . . 77 10 10 THR H H 8.204 . . 78 10 10 THR HA H 4.506 . . 79 10 10 THR HB H 4.161 . . 80 10 10 THR HG1 H 1.144 . . 81 10 10 THR HG2 H 1.142 . . 82 10 10 THR CA C 63.146 . . 83 10 10 THR CB C 71.462 . . 84 10 10 THR CG2 C 22.443 . . 85 10 10 THR N N 109.252 . . 86 11 11 TRP H H 8.151 . . 87 11 11 TRP HA H 4.126 . . 88 11 11 TRP HB2 H 3.262 . . 89 11 11 TRP HB3 H 3.104 . . 90 11 11 TRP HD1 H 7.099 . . 91 11 11 TRP HE1 H 8.608 . . 92 11 11 TRP HE3 H 7.360 . . 93 11 11 TRP HZ2 H 7.833 . . 94 11 11 TRP HZ3 H 6.807 . . 95 11 11 TRP HH2 H 7.248 . . 96 11 11 TRP CA C 59.332 . . 97 11 11 TRP CB C 30.028 . . 98 11 11 TRP CE3 C 115.540 . . 99 11 11 TRP CZ2 C 121.369 . . 100 11 11 TRP CZ3 C 120.473 . . 101 11 11 TRP CH2 C 122.032 . . 102 11 11 TRP N N 125.850 . . 103 12 12 SER H H 7.364 . . 104 12 12 SER HA H 4.642 . . 105 12 12 SER HB2 H 3.572 . . 106 12 12 SER HB3 H 3.572 . . 107 12 12 SER CA C 57.769 . . 108 12 12 SER CB C 65.589 . . 109 12 12 SER N N 123.082 . . 110 13 13 GLY H H 8.403 . . 111 13 13 GLY HA2 H 3.888 . . 112 13 13 GLY HA3 H 4.188 . . 113 13 13 GLY CA C 44.984 . . 114 13 13 GLY N N 111.342 . . 115 14 14 VAL H H 8.540 . . 116 14 14 VAL HA H 4.065 . . 117 14 14 VAL HB H 2.150 . . 118 14 14 VAL HG1 H 1.096 . . 119 14 14 VAL HG2 H 0.989 . . 120 14 14 VAL CA C 64.423 . . 121 14 14 VAL CB C 33.537 . . 122 14 14 VAL CG1 C 22.470 . . 123 14 14 VAL CG2 C 21.865 . . 124 14 14 VAL N N 119.976 . . 125 15 15 CYS H H 8.289 . . 126 15 15 CYS HA H 4.946 . . 127 15 15 CYS HB2 H 1.890 . . 128 15 15 CYS HB3 H 2.924 . . 129 15 15 CYS CA C 57.919 . . 130 15 15 CYS CB C 39.661 . . 131 16 16 GLY H H 8.610 . . 132 16 16 GLY HA2 H 3.706 . . 133 16 16 GLY HA3 H 4.402 . . 134 16 16 GLY CA C 45.808 . . 135 16 16 GLY N N 114.030 . . 136 17 17 ASN H H 7.335 . . 137 17 17 ASN HA H 4.876 . . 138 17 17 ASN HB2 H 2.792 . . 139 17 17 ASN HB3 H 3.050 . . 140 17 17 ASN HD21 H 7.902 . . 141 17 17 ASN HD22 H 7.024 . . 142 17 17 ASN CA C 53.355 . . 143 17 17 ASN ND2 N 113.318 . . 144 18 18 ASN H H 9.056 . . 145 18 18 ASN HA H 4.252 . . 146 18 18 ASN HB2 H 3.159 . . 147 18 18 ASN HB3 H 2.734 . . 148 18 18 ASN HD21 H 7.042 . . 149 18 18 ASN HD22 H 7.626 . . 150 18 18 ASN CB C 39.481 . . 151 18 18 ASN ND2 N 112.928 . . 152 19 19 GLY H H 8.565 . . 153 19 19 GLY HA2 H 3.966 . . 154 19 19 GLY HA3 H 3.789 . . 155 19 19 GLY CA C 47.970 . . 156 19 19 GLY N N 107.723 . . 157 20 20 ALA H H 7.949 . . 158 20 20 ALA HA H 4.358 . . 159 20 20 ALA HB H 1.758 . . 160 20 20 ALA CA C 55.758 . . 161 20 20 ALA CB C 19.534 . . 162 20 20 ALA N N 124.931 . . 163 21 21 CYS H H 7.335 . . 164 21 21 CYS HA H 4.174 . . 165 21 21 CYS HB2 H 2.244 . . 166 21 21 CYS HB3 H 2.066 . . 167 21 21 CYS CA C 59.283 . . 168 21 21 CYS CB C 37.802 . . 169 22 22 ARG H H 8.494 . . 170 22 22 ARG HA H 3.249 . . 171 22 22 ARG HB2 H 1.919 . . 172 22 22 ARG HB3 H 1.924 . . 173 22 22 ARG HG2 H 1.501 . . 174 22 22 ARG HG3 H 1.501 . . 175 22 22 ARG HD2 H 3.315 . . 176 22 22 ARG HD3 H 3.478 . . 177 22 22 ARG HE H 7.723 . . 178 22 22 ARG CA C 54.049 . . 179 22 22 ARG CB C 29.748 . . 180 22 22 ARG CG C 30.402 . . 181 22 22 ARG CD C 44.619 . . 182 22 22 ARG N N 122.243 . . 183 23 23 ASN H H 8.271 . . 184 23 23 ASN HA H 4.399 . . 185 23 23 ASN HB2 H 2.928 . . 186 23 23 ASN HB3 H 2.848 . . 187 23 23 ASN HD21 H 7.696 . . 188 23 23 ASN HD22 H 6.976 . . 189 23 23 ASN N N 114.938 . . 190 23 23 ASN ND2 N 112.295 . . 191 24 24 GLN H H 8.221 . . 192 24 24 GLN HA H 4.107 . . 193 24 24 GLN HB2 H 2.405 . . 194 24 24 GLN HB3 H 2.589 . . 195 24 24 GLN HG2 H 2.584 . . 196 24 24 GLN HG3 H 2.582 . . 197 24 24 GLN HE21 H 6.568 . . 198 24 24 GLN HE22 H 7.814 . . 199 24 24 GLN CB C 28.964 . . 200 24 24 GLN CG C 28.964 . . 201 24 24 GLN N N 120.890 . . 202 24 24 GLN NE2 N 110.324 . . 203 25 25 CYS H H 8.747 . . 204 25 25 CYS HA H 4.241 . . 205 25 25 CYS HB2 H 2.545 . . 206 25 25 CYS HB3 H 2.863 . . 207 25 25 CYS CA C 60.365 . . 208 25 25 CYS CB C 38.032 . . 209 26 26 ILE H H 8.198 . . 210 26 26 ILE HA H 3.852 . . 211 26 26 ILE HB H 1.732 . . 212 26 26 ILE HG12 H 1.448 . . 213 26 26 ILE HG13 H 1.732 . . 214 26 26 ILE HG2 H 0.889 . . 215 26 26 ILE HD1 H 0.814 . . 216 26 26 ILE CA C 66.031 . . 217 26 26 ILE CB C 40.352 . . 218 26 26 ILE CG2 C 17.436 . . 219 26 26 ILE CD1 C 15.411 . . 220 26 26 ILE N N 119.696 . . 221 27 27 ARG H H 8.736 . . 222 27 27 ARG HA H 4.141 . . 223 27 27 ARG HB2 H 1.909 . . 224 27 27 ARG HB3 H 1.654 . . 225 27 27 ARG HG2 H 1.824 . . 226 27 27 ARG HG3 H 1.990 . . 227 27 27 ARG HD2 H 3.207 . . 228 27 27 ARG HD3 H 3.264 . . 229 27 27 ARG HE H 7.320 . . 230 27 27 ARG CA C 60.507 . . 231 27 27 ARG CB C 32.042 . . 232 28 28 LEU H H 8.572 . . 233 28 28 LEU HA H 4.721 . . 234 28 28 LEU HB2 H 1.673 . . 235 28 28 LEU HB3 H 2.210 . . 236 28 28 LEU HG H 1.778 . . 237 28 28 LEU HD1 H 1.003 . . 238 28 28 LEU HD2 H 0.930 . . 239 28 28 LEU CA C 56.621 . . 240 28 28 LEU CB C 43.722 . . 241 28 28 LEU CG C 28.828 . . 242 28 28 LEU CD1 C 25.859 . . 243 28 28 LEU CD2 C 23.619 . . 244 29 29 GLU H H 7.032 . . 245 29 29 GLU HA H 4.810 . . 246 29 29 GLU HB2 H 2.759 . . 247 29 29 GLU HB3 H 2.661 . . 248 29 29 GLU HG2 H 2.380 . . 249 29 29 GLU HG3 H 2.270 . . 250 29 29 GLU CA C 56.943 . . 251 29 29 GLU CB C 31.048 . . 252 29 29 GLU CG C 39.629 . . 253 29 29 GLU N N 115.746 . . 254 30 30 LYS H H 7.475 . . 255 30 30 LYS HA H 4.246 . . 256 30 30 LYS HB2 H 2.164 . . 257 30 30 LYS HB3 H 2.265 . . 258 30 30 LYS HG2 H 1.437 . . 259 30 30 LYS HG3 H 1.437 . . 260 30 30 LYS HD2 H 1.743 . . 261 30 30 LYS HD3 H 1.741 . . 262 30 30 LYS HE2 H 3.066 . . 263 30 30 LYS HE3 H 3.066 . . 264 30 30 LYS HZ H 7.566 . . 265 30 30 LYS CA C 58.203 . . 266 30 30 LYS CG C 26.251 . . 267 31 31 ALA H H 7.974 . . 268 31 31 ALA HA H 4.009 . . 269 31 31 ALA HB H 0.829 . . 270 31 31 ALA CA C 51.807 . . 271 31 31 ALA CB C 14.022 . . 272 31 31 ALA N N 120.618 . . 273 32 32 ARG H H 8.230 . . 274 32 32 ARG HA H 4.482 . . 275 32 32 ARG HB2 H 1.622 . . 276 32 32 ARG HB3 H 1.835 . . 277 32 32 ARG HG2 H 1.769 . . 278 32 32 ARG HG3 H 1.714 . . 279 32 32 ARG HD2 H 3.253 . . 280 32 32 ARG HD3 H 3.253 . . 281 32 32 ARG HE H 7.463 . . 282 32 32 ARG N N 113.739 . . 283 33 33 HIS H H 7.683 . . 284 33 33 HIS HA H 4.750 . . 285 33 33 HIS HB2 H 3.220 . . 286 33 33 HIS HB3 H 2.393 . . 287 33 33 HIS HD2 H 6.003 . . 288 33 33 HIS HE1 H 7.802 . . 289 33 33 HIS CB C 34.441 . . 290 33 33 HIS CD2 C 119.297 . . 291 33 33 HIS CE1 C 141.284 . . 292 34 34 GLY H H 6.313 . . 293 34 34 GLY HA2 H 3.825 . . 294 34 34 GLY HA3 H 5.317 . . 295 34 34 GLY CA C 47.457 . . 296 34 34 GLY N N 110.723 . . 297 35 35 SER H H 9.075 . . 298 35 35 SER HA H 4.118 . . 299 35 35 SER HB2 H 3.714 . . 300 35 35 SER HB3 H 3.720 . . 301 35 35 SER CA C 61.816 . . 302 35 35 SER CB C 73.315 . . 303 36 36 CYS H H 8.552 . . 304 36 36 CYS HA H 5.455 . . 305 36 36 CYS HB2 H 2.872 . . 306 36 36 CYS HB3 H 2.728 . . 307 36 36 CYS CA C 52.833 . . 308 36 36 CYS CB C 37.259 . . 309 37 37 ASN H H 9.079 . . 310 37 37 ASN HA H 4.999 . . 311 37 37 ASN HB2 H 2.759 . . 312 37 37 ASN HB3 H 2.760 . . 313 37 37 ASN HD21 H 6.790 . . 314 37 37 ASN HD22 H 7.399 . . 315 37 37 ASN CA C 52.088 . . 316 37 37 ASN CB C 42.750 . . 317 37 37 ASN ND2 N 110.690 . . 318 38 38 TYR H H 8.829 . . 319 38 38 TYR HA H 4.208 . . 320 38 38 TYR HB2 H 2.558 . . 321 38 38 TYR HB3 H 3.011 . . 322 38 38 TYR HD1 H 6.599 . . 323 38 38 TYR HD2 H 6.599 . . 324 38 38 TYR HE1 H 6.701 . . 325 38 38 TYR HE2 H 6.701 . . 326 38 38 TYR CD1 C 133.647 . . 327 38 38 TYR CD2 C 133.647 . . 328 38 38 TYR CE1 C 118.754 . . 329 38 38 TYR CE2 C 118.754 . . 330 39 39 VAL H H 7.680 . . 331 39 39 VAL HA H 3.887 . . 332 39 39 VAL HB H 1.881 . . 333 39 39 VAL HG1 H 0.873 . . 334 39 39 VAL HG2 H 0.873 . . 335 39 39 VAL CA C 64.862 . . 336 39 39 VAL CG1 C 21.990 . . 337 39 39 VAL CG2 C 21.209 . . 338 40 40 PHE H H 8.441 . . 339 40 40 PHE HA H 3.956 . . 340 40 40 PHE HB2 H 3.036 . . 341 40 40 PHE HB3 H 2.884 . . 342 40 40 PHE HD1 H 7.312 . . 343 40 40 PHE HD2 H 7.312 . . 344 40 40 PHE HE1 H 7.423 . . 345 40 40 PHE HE2 H 7.423 . . 346 40 40 PHE HZ H 7.381 . . 347 40 40 PHE CA C 57.565 . . 348 40 40 PHE CD1 C 133.203 . . 349 40 40 PHE CD2 C 133.203 . . 350 40 40 PHE CE1 C 132.768 . . 351 40 40 PHE CE2 C 132.768 . . 352 40 40 PHE CZ C 131.536 . . 353 41 41 PRO HA H 3.868 . . 354 41 41 PRO HB2 H 1.981 . . 355 41 41 PRO HB3 H 0.969 . . 356 41 41 PRO HG2 H 1.497 . . 357 41 41 PRO HG3 H 1.716 . . 358 41 41 PRO HD2 H 3.353 . . 359 41 41 PRO HD3 H 3.281 . . 360 41 41 PRO CA C 62.617 . . 361 41 41 PRO CG C 24.910 . . 362 41 41 PRO CD C 49.877 . . 363 42 42 ALA H H 8.286 . . 364 42 42 ALA HA H 4.777 . . 365 42 42 ALA HB H 1.340 . . 366 42 42 ALA CA C 52.598 . . 367 42 42 ALA CB C 23.268 . . 368 43 43 HIS H H 8.588 . . 369 43 43 HIS HA H 4.954 . . 370 43 43 HIS HB2 H 3.120 . . 371 43 43 HIS HB3 H 3.305 . . 372 43 43 HIS HD2 H 8.253 . . 373 43 43 HIS HE1 H 7.284 . . 374 43 43 HIS CA C 56.597 . . 375 43 43 HIS CB C 31.205 . . 376 43 43 HIS CD2 C 125.229 . . 377 43 43 HIS CE1 C 138.211 . . 378 44 44 LYS H H 8.825 . . 379 44 44 LYS HA H 4.667 . . 380 44 44 LYS HB2 H 1.553 . . 381 44 44 LYS HB3 H 1.877 . . 382 44 44 LYS HG2 H 1.508 . . 383 44 44 LYS HG3 H 1.408 . . 384 44 44 LYS HD2 H 1.495 . . 385 44 44 LYS HD3 H 1.676 . . 386 44 44 LYS HE2 H 2.986 . . 387 44 44 LYS HE3 H 2.986 . . 388 44 44 LYS HZ H 7.656 . . 389 44 44 LYS CA C 55.564 . . 390 44 44 LYS CB C 37.018 . . 391 44 44 LYS CE C 42.838 . . 392 45 45 CYS H H 9.154 . . 393 45 45 CYS HA H 4.714 . . 394 45 45 CYS HB2 H 2.208 . . 395 45 45 CYS HB3 H 1.618 . . 396 45 45 CYS CB C 36.420 . . 397 45 45 CYS N N 120.533 . . 398 46 46 ILE H H 8.773 . . 399 46 46 ILE HA H 4.159 . . 400 46 46 ILE HB H 2.052 . . 401 46 46 ILE HG12 H 1.309 . . 402 46 46 ILE HG13 H 1.549 . . 403 46 46 ILE HG2 H 0.390 . . 404 46 46 ILE HD1 H 0.598 . . 405 46 46 ILE CA C 58.950 . . 406 46 46 ILE CB C 38.351 . . 407 46 46 ILE CG1 C 27.803 . . 408 46 46 ILE CG2 C 18.314 . . 409 46 46 ILE CD1 C 10.433 . . 410 46 46 ILE N N 133.530 . . 411 47 47 CYS H H 8.520 . . 412 47 47 CYS HA H 5.341 . . 413 47 47 CYS HB2 H 2.734 . . 414 47 47 CYS HB3 H 3.008 . . 415 47 47 CYS CA C 52.088 . . 416 47 47 CYS N N 120.445 . . 417 48 48 TYR H H 7.870 . . 418 48 48 TYR HA H 5.280 . . 419 48 48 TYR HB2 H 2.744 . . 420 48 48 TYR HB3 H 2.433 . . 421 48 48 TYR HD1 H 6.661 . . 422 48 48 TYR HD2 H 6.661 . . 423 48 48 TYR HE1 H 6.738 . . 424 48 48 TYR HE2 H 6.738 . . 425 48 48 TYR CA C 57.903 . . 426 48 48 TYR CB C 42.520 . . 427 48 48 TYR CD1 C 133.354 . . 428 48 48 TYR CD2 C 133.354 . . 429 48 48 TYR CE1 C 119.915 . . 430 48 48 TYR CE2 C 119.915 . . 431 48 48 TYR N N 116.569 . . 432 49 49 PHE H H 9.162 . . 433 49 49 PHE HA H 4.961 . . 434 49 49 PHE HB2 H 3.312 . . 435 49 49 PHE HB3 H 2.769 . . 436 49 49 PHE HD1 H 7.270 . . 437 49 49 PHE HD2 H 7.270 . . 438 49 49 PHE HE1 H 7.482 . . 439 49 49 PHE HE2 H 7.482 . . 440 49 49 PHE HZ H 7.346 . . 441 49 49 PHE CD1 C 133.044 . . 442 49 49 PHE CD2 C 133.044 . . 443 49 49 PHE CE1 C 133.453 . . 444 49 49 PHE CE2 C 133.453 . . 445 49 49 PHE CZ C 131.266 . . 446 49 49 PHE N N 122.029 . . 447 50 50 PRO HA H 4.894 . . 448 50 50 PRO HB2 H 2.109 . . 449 50 50 PRO HB3 H 2.386 . . 450 50 50 PRO HG2 H 1.952 . . 451 50 50 PRO HG3 H 2.385 . . 452 50 50 PRO HD2 H 3.816 . . 453 50 50 PRO HD3 H 4.123 . . 454 50 50 PRO CA C 64.668 . . 455 50 50 PRO CB C 32.918 . . 456 50 50 PRO CG C 29.079 . . 457 50 50 PRO CD C 51.958 . . 458 51 51 CYS H H 8.348 . . 459 51 51 CYS HA H 4.565 . . 460 51 51 CYS HB2 H 3.401 . . 461 51 51 CYS HB3 H 3.201 . . 462 51 51 CYS CA C 57.632 . . 463 51 51 CYS CB C 44.537 . . 464 51 51 CYS N N 126.422 . . stop_ save_