data_6050 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Solution structure of Sso7d mutant (K12L), NMR, 4 structures ; _BMRB_accession_number 6050 _BMRB_flat_file_name bmr6050.str _Entry_type original _Submission_date 2003-12-16 _Accession_date 2003-12-16 _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 Recca T. . . 2 Consonni R. . . 3 Alberti E. . . 4 Arosio I. . . 5 Zetta L. . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 388 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2007-03-22 original author 'original release' 2007-11-05 update BMRB 'complete the entry citation' stop_ save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; Structural determinants responsible for the thermostability of Sso7d and its single point mutants ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 17340638 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Consonni R. . . 2 Arosio I. . . 3 Recca T. . . 4 Fusi P. . . 5 Zetta L. . . stop_ _Journal_abbreviation Proteins _Journal_volume 67 _Journal_issue 3 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 766 _Page_last 775 _Year 2007 _Details . loop_ _Keyword NMR 'RNASE AND DNA-BINDING PROTEIN' 'SINGLE POINT MUTATION' 'SULFOLOBUS SOLFATARICUS' 'THERMOSTABLE RIBONUCLEASE' stop_ save_ ####################################### # Cited references within the entry # ####################################### save_ref_1 _Saveframe_category citation _Citation_full ; The Sso7d DNA-binding protein from sulfolobus solfataricus has ribonuclease activity Febs Lett. V.497, 131, 2001 ; _Citation_title 'The Sso7d DNA-binding protein from Sulfolobus solfataricus has ribonuclease activity.' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 11377427 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Shehi E . . 2 Serina S . . 3 Fumagalli G . . 4 Vanoni M . . 5 Consonni R . . 6 Zetta L . . 7 Deho G . . 8 Tortora P . . 9 Fusi P . . stop_ _Journal_abbreviation 'FEBS Lett.' _Journal_name_full 'FEBS letters' _Journal_volume 497 _Journal_issue 2-3 _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 131 _Page_last 136 _Year 2001 _Details ; Sso7d is a small, basic, abundant protein from the thermoacidophilic archaeon Sulfolobus solfataricus. Previous research has shown that Sso7d can bind double-stranded DNA without sequence specificity by placing its triple-stranded beta-sheet across the minor groove. We previously found RNase activity both in preparations of Sso7d purified from its natural source and in recombinant, purified protein expressed in Escherichia coli. This paper provides conclusive evidence that supports the assignment of RNase activity to Sso7d, shown by the total absence of activity in the single-point mutants E35L and K12L, despite the preservation of their overall structure under the assay conditions. In keeping with our observation that the residues putatively involved in RNase activity and those playing a role in DNA binding are located on different surfaces of the molecule, the activity was not impaired in the presence of DNA. If a small synthetic RNA was used as a substrate, Sso7d attacked both predicted double- and single-stranded RNA stretches, with no evident preference for specific sequences or individual bases. Apparently, the more readily attacked bonds were those intrinsically more unstable. ; save_ ################################## # Molecular system description # ################################## save_system_Rnase_SSO7D _Saveframe_category molecular_system _Mol_system_name 'Endoribonuclease SSO7D single point mutant K12L' _Abbreviation_common 'Rnase SSO7D' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'Endoribounuclease SSO7D' $SSO7D_K12L stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state monomer _System_paramagnetic no _System_thiol_state 'not present' _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_SSO7D_K12L _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common SSO7D _Name_variant K12L _Abbreviation_common K12L _Molecular_mass . _Mol_thiol_state 'not present' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 62 _Mol_residue_sequence ; ATVKFKYKGEELQVDISKIK KVWRVGKMISFTYDEGGGKT GRGAVSEKDAPKKLLQMLEK QK ; loop_ _Residue_seq_code _Residue_label 1 ALA 2 THR 3 VAL 4 LYS 5 PHE 6 LYS 7 TYR 8 LYS 9 GLY 10 GLU 11 GLU 12 LEU 13 GLN 14 VAL 15 ASP 16 ILE 17 SER 18 LYS 19 ILE 20 LYS 21 LYS 22 VAL 23 TRP 24 ARG 25 VAL 26 GLY 27 LYS 28 MET 29 ILE 30 SER 31 PHE 32 THR 33 TYR 34 ASP 35 GLU 36 GLY 37 GLY 38 GLY 39 LYS 40 THR 41 GLY 42 ARG 43 GLY 44 ALA 45 VAL 46 SER 47 GLU 48 LYS 49 ASP 50 ALA 51 PRO 52 LYS 53 LYS 54 LEU 55 LEU 56 GLN 57 MET 58 LEU 59 GLU 60 LYS 61 GLN 62 LYS stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2008-08-19 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 2CVR 'Nmr Solution Structure Of Sso7d Mutant, K12l, 12 Conformers' 100.00 62 98.39 100.00 2.58e-26 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species _Details $SSO7D_K12L 'Sulfolobus solfataricus' 2287 Archaea . Sulfolobus solfataricus archaeobacterium 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 $SSO7D_K12L 'recombinant technology' 'E. coli' Escherichia coli . . 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 $SSO7D_K12L 2 mM . D2O 10 % . H2O 90 % . stop_ save_ save_sample_2 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $SSO7D_K12L 2 mM . D2O 100 % . H2O 90 % . stop_ save_ ############################ # Computer software used # ############################ save_FELIX _Saveframe_category software _Name FELIX _Version 98.0 loop_ _Task 'data analysis' stop_ _Details 'Molecular Simulation Inc.' save_ save_DISCOVER _Saveframe_category software _Name DISCOVER _Version 3.0 loop_ _Task refinement 'structure solution' stop_ _Details Dauber-Osguthorpe save_ save_XWINNMR _Saveframe_category software _Name xwinnmr _Version 2.6 loop_ _Task collection stop_ _Details Bruker save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model DMX _Field_strength 500 _Details . save_ ############################# # NMR applied experiments # ############################# save_DQF-COSY_1 _Saveframe_category NMR_applied_experiment _Experiment_name DQF-COSY _Sample_label . save_ save_2D_TOCSY_2 _Saveframe_category NMR_applied_experiment _Experiment_name '2D TOCSY' _Sample_label . save_ save_2D_NOESY_3 _Saveframe_category NMR_applied_experiment _Experiment_name '2D NOESY' _Sample_label . save_ save_NMR_spec_expt__0_1 _Saveframe_category NMR_applied_experiment _Experiment_name DQF-COSY _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_2 _Saveframe_category NMR_applied_experiment _Experiment_name '2D TOCSY' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_3 _Saveframe_category NMR_applied_experiment _Experiment_name '2D NOESY' _BMRB_pulse_sequence_accession_number . _Details . save_ ####################### # Sample conditions # ####################### save_sample_cond_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 4.5 0.2 pH pressure 1 . atm temperature 300 1 K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference _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 0.0 internal direct . . . 1.0 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_chemical_shift_set_1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $sample_cond_1 _Chem_shift_reference_set_label $chemical_shift_reference _Mol_system_component_name 'Endoribounuclease SSO7D' _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 ALA HA H 4.250 0.03 1 2 . 1 ALA HB H 1.458 0.03 1 3 . 2 THR H H 8.582 0.03 1 4 . 2 THR HA H 4.953 0.03 1 5 . 2 THR HB H 3.828 0.03 1 6 . 2 THR HG2 H 1.047 0.03 1 7 . 3 VAL H H 8.900 0.03 1 8 . 3 VAL HA H 4.360 0.03 1 9 . 3 VAL HB H 1.675 0.03 1 10 . 3 VAL HG1 H 0.663 0.03 1 11 . 3 VAL HG2 H 0.579 0.03 1 12 . 4 LYS H H 8.485 0.03 1 13 . 4 LYS HA H 5.392 0.03 1 14 . 4 LYS HB3 H 1.715 0.03 1 15 . 4 LYS HB2 H 1.830 0.03 1 16 . 4 LYS HG3 H 1.252 0.03 1 17 . 4 LYS HG2 H 1.388 0.03 1 18 . 4 LYS HD2 H 1.623 0.03 1 19 . 4 LYS HD3 H 1.623 0.03 1 20 . 4 LYS HE2 H 2.874 0.03 1 21 . 4 LYS HE3 H 2.874 0.03 1 22 . 5 PHE H H 8.678 0.03 1 23 . 5 PHE HA H 5.055 0.03 1 24 . 5 PHE HB3 H 3.164 0.03 1 25 . 5 PHE HD1 H 7.077 0.03 1 26 . 5 PHE HD2 H 7.077 0.03 1 27 . 5 PHE HE1 H 6.985 0.03 1 28 . 5 PHE HE2 H 6.985 0.03 1 29 . 5 PHE HB2 H 3.237 0.03 1 30 . 6 LYS H H 8.720 0.03 1 31 . 6 LYS HA H 5.212 0.03 1 32 . 6 LYS HB3 H 1.690 0.03 1 33 . 6 LYS HB2 H 1.770 0.03 1 34 . 6 LYS HG3 H 1.251 0.03 1 35 . 6 LYS HG2 H 1.386 0.03 1 36 . 6 LYS HD2 H 1.595 0.03 1 37 . 6 LYS HD3 H 1.595 0.03 1 38 . 6 LYS HE2 H 2.916 0.03 1 39 . 6 LYS HE3 H 2.916 0.03 1 40 . 7 TYR H H 9.000 0.03 1 41 . 7 TYR HA H 4.824 0.03 1 42 . 7 TYR HB3 H 2.906 0.03 1 43 . 7 TYR HB2 H 3.195 0.03 1 44 . 7 TYR HD1 H 7.333 0.03 1 45 . 7 TYR HD2 H 7.333 0.03 1 46 . 7 TYR HE1 H 6.920 0.03 1 47 . 7 TYR HE2 H 6.920 0.03 1 48 . 8 LYS H H 9.152 0.03 1 49 . 8 LYS HA H 3.618 0.03 1 50 . 8 LYS HB2 H 1.518 0.03 1 51 . 8 LYS HB3 H 1.518 0.03 1 52 . 8 LYS HG3 H 0.518 0.03 1 53 . 8 LYS HG2 H 0.815 0.03 1 54 . 8 LYS HD2 H 1.779 0.03 1 55 . 8 LYS HD3 H 1.779 0.03 1 56 . 8 LYS HE2 H 2.894 0.03 1 57 . 8 LYS HE3 H 2.894 0.03 1 58 . 9 GLY H H 8.495 0.03 1 59 . 9 GLY HA3 H 3.596 0.03 1 60 . 9 GLY HA2 H 4.160 0.03 1 61 . 10 GLU H H 7.887 0.03 1 62 . 10 GLU HA H 4.612 0.03 1 63 . 10 GLU HB2 H 2.037 0.03 1 64 . 10 GLU HB3 H 2.037 0.03 1 65 . 10 GLU HG3 H 2.282 0.03 1 66 . 10 GLU HG2 H 2.370 0.03 1 67 . 11 GLU H H 8.667 0.03 1 68 . 11 GLU HA H 4.518 0.03 1 69 . 11 GLU HB3 H 1.832 0.03 1 70 . 11 GLU HG3 H 2.085 0.03 1 71 . 11 GLU HG2 H 2.164 0.03 1 72 . 11 GLU HB2 H 1.970 0.03 1 73 . 12 LEU H H 8.820 0.03 1 74 . 12 LEU HA H 4.510 0.03 1 75 . 12 LEU HB3 H 0.448 0.03 1 76 . 12 LEU HG H 1.340 0.03 1 77 . 12 LEU HB2 H 0.900 0.03 1 78 . 12 LEU HD2 H 0.811 0.03 1 79 . 12 LEU HD1 H 0.860 0.03 1 80 . 13 GLN H H 7.921 0.03 1 81 . 13 GLN HA H 5.349 0.03 1 82 . 13 GLN HB2 H 1.832 0.03 1 83 . 13 GLN HB3 H 1.832 0.03 1 84 . 13 GLN HG2 H 2.148 0.03 1 85 . 13 GLN HG3 H 2.148 0.03 1 86 . 13 GLN HE21 H 7.552 0.03 1 87 . 13 GLN HE22 H 6.843 0.03 1 88 . 14 VAL H H 8.660 0.03 1 89 . 14 VAL HA H 4.320 0.03 1 90 . 14 VAL HB H 1.516 0.03 1 91 . 14 VAL HG1 H 0.460 0.03 1 92 . 14 VAL HG2 H 0.415 0.03 1 93 . 15 ASP H H 8.673 0.03 1 94 . 15 ASP HA H 4.625 0.03 1 95 . 15 ASP HB2 H 2.581 0.03 1 96 . 15 ASP HB3 H 2.581 0.03 1 97 . 16 ILE H H 8.380 0.03 1 98 . 16 ILE HA H 3.633 0.03 1 99 . 16 ILE HB H 1.765 0.03 1 100 . 16 ILE HG12 H 1.065 0.03 1 101 . 16 ILE HG13 H 1.065 0.03 1 102 . 16 ILE HG2 H 0.815 0.03 1 103 . 16 ILE HD1 H 0.560 0.03 1 104 . 17 SER H H 8.926 0.03 1 105 . 17 SER HA H 4.255 0.03 1 106 . 17 SER HB2 H 3.975 0.03 1 107 . 17 SER HB3 H 3.975 0.03 1 108 . 18 LYS H H 8.042 0.03 1 109 . 18 LYS HA H 4.559 0.03 1 110 . 18 LYS HB2 H 2.037 0.03 1 111 . 18 LYS HB3 H 2.037 0.03 1 112 . 18 LYS HG3 H 1.500 0.03 1 113 . 18 LYS HD2 H 2.437 0.03 1 114 . 18 LYS HD3 H 2.437 0.03 1 115 . 18 LYS HE2 H 3.073 0.03 1 116 . 18 LYS HE3 H 3.073 0.03 1 117 . 18 LYS HG2 H 1.686 0.03 1 118 . 19 ILE H H 7.520 0.03 1 119 . 19 ILE HA H 4.160 0.03 1 120 . 19 ILE HB H 1.985 0.03 1 121 . 19 ILE HG13 H 1.060 0.03 1 122 . 19 ILE HG12 H 1.360 0.03 1 123 . 19 ILE HD1 H 0.089 0.03 1 124 . 19 ILE HG2 H 0.822 0.03 1 125 . 20 LYS H H 7.535 0.03 1 126 . 20 LYS HA H 4.505 0.03 1 127 . 20 LYS HB3 H 1.854 0.03 1 128 . 20 LYS HE2 H 3.001 0.03 1 129 . 20 LYS HE3 H 3.001 0.03 1 130 . 20 LYS HB2 H 1.833 0.03 1 131 . 21 LYS HB3 H 1.840 0.03 1 132 . 21 LYS HG2 H 1.467 0.03 1 133 . 21 LYS HG3 H 1.467 0.03 1 134 . 21 LYS HD2 H 1.697 0.03 1 135 . 21 LYS HD3 H 1.697 0.03 1 136 . 21 LYS HE2 H 3.013 0.03 1 137 . 21 LYS HE3 H 3.013 0.03 1 138 . 21 LYS HB2 H 1.940 0.03 1 139 . 22 VAL H H 8.387 0.03 1 140 . 22 VAL HA H 5.275 0.03 1 141 . 22 VAL HB H 1.770 0.03 1 142 . 22 VAL HG1 H 0.915 0.03 1 143 . 22 VAL HG2 H 0.915 0.03 1 144 . 23 TRP H H 9.336 0.03 1 145 . 23 TRP HA H 4.958 0.03 1 146 . 23 TRP HB3 H 3.233 0.03 1 147 . 23 TRP HD1 H 6.998 0.03 1 148 . 23 TRP HE1 H 10.100 0.03 1 149 . 23 TRP HE3 H 7.213 0.03 1 150 . 23 TRP HZ2 H 7.340 0.03 1 151 . 23 TRP HZ3 H 6.924 0.03 1 152 . 23 TRP HH2 H 6.909 0.03 1 153 . 23 TRP HB2 H 3.480 0.03 1 154 . 24 ARG H H 8.835 0.03 1 155 . 24 ARG HA H 4.945 0.03 1 156 . 24 ARG HB3 H 1.723 0.03 1 157 . 24 ARG HG3 H 1.515 0.03 1 158 . 24 ARG HD3 H 3.213 0.03 1 159 . 24 ARG HE H 7.585 0.03 1 160 . 24 ARG HB2 H 1.858 0.03 1 161 . 24 ARG HG2 H 1.590 0.03 1 162 . 24 ARG HD2 H 3.318 0.03 1 163 . 25 VAL H H 8.657 0.03 1 164 . 25 VAL HA H 4.249 0.03 1 165 . 25 VAL HB H 2.020 0.03 1 166 . 25 VAL HG1 H 1.008 0.03 1 167 . 25 VAL HG2 H 0.957 0.03 1 168 . 26 GLY H H 8.930 0.03 1 169 . 26 GLY HA3 H 3.712 0.03 1 170 . 26 GLY HA2 H 4.012 0.03 1 171 . 27 LYS HA H 4.435 0.03 1 172 . 27 LYS HB2 H 1.757 0.03 1 173 . 27 LYS HB3 H 1.757 0.03 1 174 . 27 LYS HG3 H 1.490 0.03 1 175 . 27 LYS HD2 H 2.180 0.03 1 176 . 27 LYS HD3 H 2.180 0.03 1 177 . 27 LYS HE2 H 3.033 0.03 1 178 . 27 LYS HE3 H 3.033 0.03 1 179 . 27 LYS HG2 H 2.473 0.03 1 180 . 28 MET H H 8.185 0.03 1 181 . 28 MET HA H 5.000 0.03 1 182 . 28 MET HB3 H 1.767 0.03 1 183 . 28 MET HG3 H 2.463 0.03 1 184 . 28 MET HB2 H 2.185 0.03 1 185 . 28 MET HG2 H 2.615 0.03 1 186 . 29 ILE H H 9.325 0.03 1 187 . 29 ILE HA H 4.427 0.03 1 188 . 29 ILE HB H 2.019 0.03 1 189 . 29 ILE HG12 H 1.230 0.03 1 190 . 29 ILE HG13 H 1.230 0.03 1 191 . 29 ILE HG2 H 0.710 0.03 1 192 . 30 SER H H 8.767 0.03 1 193 . 30 SER HA H 4.675 0.03 1 194 . 30 SER HB3 H 2.140 0.03 1 195 . 30 SER HB2 H 2.500 0.03 1 196 . 31 PHE H H 7.587 0.03 1 197 . 31 PHE HA H 5.637 0.03 1 198 . 31 PHE HB3 H 3.045 0.03 1 199 . 31 PHE HD1 H 6.542 0.03 1 200 . 31 PHE HD2 H 6.542 0.03 1 201 . 31 PHE HE1 H 6.307 0.03 1 202 . 31 PHE HE2 H 6.307 0.03 1 203 . 31 PHE HZ H 5.630 0.03 1 204 . 31 PHE HB2 H 3.200 0.03 1 205 . 32 THR H H 9.020 0.03 1 206 . 32 THR HA H 5.639 0.03 1 207 . 32 THR HB H 4.329 0.03 1 208 . 32 THR HG2 H 1.390 0.03 1 209 . 33 TYR H H 8.614 0.03 1 210 . 33 TYR HA H 5.506 0.03 1 211 . 33 TYR HB3 H 2.654 0.03 1 212 . 33 TYR HD1 H 6.672 0.03 1 213 . 33 TYR HD2 H 6.672 0.03 1 214 . 33 TYR HE1 H 6.570 0.03 1 215 . 33 TYR HE2 H 6.570 0.03 1 216 . 33 TYR HB2 H 2.882 0.03 1 217 . 34 ASP H H 8.930 0.03 1 218 . 34 ASP HA H 4.760 0.03 1 219 . 34 ASP HB3 H 2.691 0.03 1 220 . 34 ASP HB2 H 2.975 0.03 1 221 . 35 GLU H H 8.435 0.03 1 222 . 35 GLU HA H 4.520 0.03 1 223 . 35 GLU HB2 H 1.812 0.03 1 224 . 35 GLU HB3 H 1.812 0.03 1 225 . 35 GLU HG3 H 2.175 0.03 1 226 . 35 GLU HG2 H 2.407 0.03 1 227 . 36 GLY H H 8.562 0.03 1 228 . 36 GLY HA3 H 3.860 0.03 1 229 . 36 GLY HA2 H 4.502 0.03 1 230 . 37 GLY H H 8.863 0.03 1 231 . 37 GLY HA2 H 3.915 0.03 1 232 . 37 GLY HA3 H 3.915 0.03 1 233 . 38 GLY H H 9.027 0.03 1 234 . 38 GLY HA3 H 3.695 0.03 1 235 . 38 GLY HA2 H 4.170 0.03 1 236 . 39 LYS H H 7.525 0.03 1 237 . 39 LYS HA H 4.150 0.03 1 238 . 39 LYS HB2 H 1.855 0.03 1 239 . 39 LYS HB3 H 1.855 0.03 1 240 . 39 LYS HG2 H 1.473 0.03 1 241 . 39 LYS HG3 H 1.473 0.03 1 242 . 39 LYS HD2 H 1.699 0.03 1 243 . 39 LYS HD3 H 1.699 0.03 1 244 . 39 LYS HE2 H 2.798 0.03 1 245 . 39 LYS HE3 H 2.798 0.03 1 246 . 40 THR H H 8.611 0.03 1 247 . 40 THR HA H 4.899 0.03 1 248 . 40 THR HB H 3.942 0.03 1 249 . 40 THR HG2 H 1.218 0.03 1 250 . 41 GLY H H 8.615 0.03 1 251 . 41 GLY HA3 H 2.551 0.03 1 252 . 41 GLY HA2 H 4.202 0.03 1 253 . 42 ARG H H 7.795 0.03 1 254 . 42 ARG HA H 5.168 0.03 1 255 . 42 ARG HB3 H 1.590 0.03 1 256 . 42 ARG HB2 H 1.727 0.03 1 257 . 42 ARG HG2 H 1.530 0.03 1 258 . 42 ARG HG3 H 1.530 0.03 1 259 . 42 ARG HD2 H 3.210 0.03 1 260 . 42 ARG HD3 H 3.210 0.03 1 261 . 42 ARG HE H 7.213 0.03 1 262 . 43 GLY H H 7.765 0.03 1 263 . 43 GLY HA3 H 2.395 0.03 1 264 . 43 GLY HA2 H 3.900 0.03 1 265 . 44 ALA H H 6.765 0.03 1 266 . 44 ALA HA H 5.060 0.03 1 267 . 44 ALA HB H 1.140 0.03 1 268 . 45 VAL H H 9.102 0.03 1 269 . 45 VAL HA H 4.730 0.03 1 270 . 45 VAL HB H 2.170 0.03 1 271 . 45 VAL HG1 H 1.065 0.03 1 272 . 45 VAL HG2 H 0.990 0.03 1 273 . 46 SER H H 9.100 0.03 1 274 . 46 SER HA H 4.898 0.03 1 275 . 46 SER HB3 H 4.005 0.03 1 276 . 46 SER HB2 H 4.182 0.03 1 277 . 47 GLU H H 8.783 0.03 1 278 . 47 GLU HA H 3.865 0.03 1 279 . 47 GLU HB2 H 2.039 0.03 1 280 . 47 GLU HB3 H 2.039 0.03 1 281 . 47 GLU HG3 H 2.207 0.03 1 282 . 47 GLU HG2 H 2.358 0.03 1 283 . 48 LYS H H 8.116 0.03 1 284 . 48 LYS HA H 4.150 0.03 1 285 . 48 LYS HB2 H 1.830 0.03 1 286 . 48 LYS HB3 H 1.830 0.03 1 287 . 48 LYS HG2 H 1.468 0.03 1 288 . 48 LYS HG3 H 1.468 0.03 1 289 . 48 LYS HD2 H 1.715 0.03 1 290 . 48 LYS HD3 H 1.715 0.03 1 291 . 48 LYS HE2 H 3.043 0.03 1 292 . 48 LYS HE3 H 3.043 0.03 1 293 . 49 ASP H H 7.570 0.03 1 294 . 49 ASP HA H 4.870 0.03 1 295 . 49 ASP HB3 H 2.620 0.03 1 296 . 49 ASP HB2 H 3.008 0.03 1 297 . 50 ALA H H 7.472 0.03 1 298 . 50 ALA HA H 4.382 0.03 1 299 . 50 ALA HB H 1.325 0.03 1 300 . 51 PRO HA H 4.728 0.03 1 301 . 51 PRO HB3 H 2.078 0.03 1 302 . 51 PRO HG3 H 1.880 0.03 1 303 . 51 PRO HD3 H 3.414 0.03 1 304 . 51 PRO HB2 H 2.584 0.03 1 305 . 51 PRO HG2 H 2.280 0.03 1 306 . 51 PRO HD2 H 4.255 0.03 1 307 . 52 LYS H H 9.132 0.03 1 308 . 52 LYS HA H 3.902 0.03 1 309 . 52 LYS HB3 H 1.795 0.03 1 310 . 52 LYS HG2 H 1.447 0.03 1 311 . 52 LYS HE2 H 2.999 0.03 1 312 . 52 LYS HE3 H 2.999 0.03 1 313 . 52 LYS HB2 H 1.917 0.03 1 314 . 53 LYS H H 9.845 0.03 1 315 . 53 LYS HA H 3.935 0.03 1 316 . 53 LYS HB3 H 1.745 0.03 1 317 . 53 LYS HG3 H 2.264 0.03 1 318 . 53 LYS HG2 H 2.500 0.03 1 319 . 53 LYS HB2 H 1.875 0.03 1 320 . 54 LEU H H 7.362 0.03 1 321 . 54 LEU HA H 4.159 0.03 1 322 . 54 LEU HB3 H 1.042 0.03 1 323 . 54 LEU HG H 1.437 0.03 1 324 . 54 LEU HB2 H 1.885 0.03 1 325 . 54 LEU HD2 H 0.592 0.03 1 326 . 54 LEU HD1 H 0.632 0.03 1 327 . 55 LEU H H 7.275 0.03 1 328 . 55 LEU HA H 3.914 0.03 1 329 . 55 LEU HB2 H 1.900 0.03 1 330 . 55 LEU HB3 H 1.900 0.03 1 331 . 55 LEU HG H 1.562 0.03 1 332 . 55 LEU HD1 H 0.937 0.03 1 333 . 55 LEU HD2 H 0.790 0.03 1 334 . 56 GLN H H 8.215 0.03 1 335 . 56 GLN HA H 4.060 0.03 1 336 . 56 GLN HB2 H 2.072 0.03 1 337 . 56 GLN HB3 H 2.072 0.03 1 338 . 56 GLN HG3 H 2.410 0.03 1 339 . 56 GLN HE21 H 7.482 0.03 1 340 . 56 GLN HE22 H 6.837 0.03 1 341 . 56 GLN HG2 H 2.492 0.03 1 342 . 57 MET H H 7.363 0.03 1 343 . 57 MET HA H 4.104 0.03 1 344 . 57 MET HB2 H 2.203 0.03 1 345 . 57 MET HB3 H 2.203 0.03 1 346 . 57 MET HG3 H 2.472 0.03 1 347 . 57 MET HG2 H 2.854 0.03 1 348 . 58 LEU H H 7.467 0.03 1 349 . 58 LEU HA H 4.066 0.03 1 350 . 58 LEU HB3 H 1.730 0.03 1 351 . 58 LEU HG H 1.648 0.03 1 352 . 58 LEU HB2 H 1.840 0.03 1 353 . 58 LEU HD1 H 0.945 0.03 1 354 . 58 LEU HD2 H 0.904 0.03 1 355 . 59 GLU H H 7.837 0.03 1 356 . 59 GLU HA H 4.228 0.03 1 357 . 59 GLU HB2 H 2.093 0.03 1 358 . 59 GLU HB3 H 2.093 0.03 1 359 . 59 GLU HG2 H 2.421 0.03 1 360 . 59 GLU HG3 H 2.421 0.03 1 361 . 60 LYS H H 7.882 0.03 1 362 . 60 LYS HA H 4.323 0.03 1 363 . 60 LYS HB3 H 1.853 0.03 1 364 . 60 LYS HG2 H 1.535 0.03 1 365 . 60 LYS HG3 H 1.535 0.03 1 366 . 60 LYS HD2 H 1.716 0.03 1 367 . 60 LYS HD3 H 1.716 0.03 1 368 . 60 LYS HE2 H 3.027 0.03 1 369 . 60 LYS HE3 H 3.027 0.03 1 370 . 60 LYS HB2 H 1.942 0.03 1 371 . 61 GLN H H 8.074 0.03 1 372 . 61 GLN HA H 4.340 0.03 1 373 . 61 GLN HB3 H 2.079 0.03 1 374 . 61 GLN HG2 H 2.516 0.03 1 375 . 61 GLN HG3 H 2.516 0.03 1 376 . 61 GLN HE21 H 7.630 0.03 1 377 . 61 GLN HE22 H 7.043 0.03 1 378 . 61 GLN HB2 H 2.274 0.03 1 379 . 62 LYS H H 7.946 0.03 1 380 . 62 LYS HA H 4.191 0.03 1 381 . 62 LYS HB2 H 1.784 0.03 1 382 . 62 LYS HB3 H 1.784 0.03 1 383 . 62 LYS HG2 H 1.465 0.03 1 384 . 62 LYS HG3 H 1.465 0.03 1 385 . 62 LYS HD2 H 1.753 0.03 1 386 . 62 LYS HD3 H 1.753 0.03 1 387 . 62 LYS HE2 H 3.046 0.03 1 388 . 62 LYS HE3 H 3.046 0.03 1 stop_ save_