data_4306 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Backbone NMR asignment of a cyanobacterial transcriptional factor, SmtB, that has bound zinc ions ; _BMRB_accession_number 4306 _BMRB_flat_file_name bmr4306.str _Entry_type revised _Submission_date 1999-02-03 _Accession_date 1999-02-03 _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 Kosada Takashi . . 2 Morita Hayato Eugene . 3 Miura Akira . . 4 Yamazaki Toshio . . 5 Hayashi Hidenori . . 6 Kyogoku Yoshimasa . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 114 "13C chemical shifts" 119 "15N chemical shifts" 114 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2000-07-14 update BMRB 'update NMR-STAR version' 2000-07-14 update author 'Chemical shift values of 15N are revised' stop_ save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; Backbone NMR assignments of a cyanobacterial transcriptional factor, SmtB, that binds zinc ions ; _Citation_status published _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 Kosada Takashi . . 2 Morita Hayato Eugene . 3 Miura Akira . . 4 Yamazaki Toshio . . 5 Hayashi Hidenori . . 6 Kyogoku Yoshimasa . . stop_ _Journal_abbreviation 'J. Biomol. NMR' _Journal_volume 14 _Journal_issue 2 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 191 _Page_last 192 _Year 1999 _Details . loop_ _Keyword 'backbone assignments' 'heavy metal ion sensing' SmtB 'transcriptional factor' 'zinc ion binding' stop_ save_ ####################################### # Cited references within the entry # ####################################### save_ref_1 _Saveframe_category citation _Citation_full 'Morita HE, Kosada T, Yamazaki T, Kyogoku Y, Hayashi H, J. Biomol. NMR 1998; 12:453-4' _Citation_title . _Citation_status . _Citation_type . _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID ? _Journal_abbreviation . _Journal_name_full . _Journal_volume . _Journal_issue . _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 . _Page_last . _Year . _Details . save_ ################################## # Molecular system description # ################################## save_ZnSmtB _Saveframe_category molecular_system _Mol_system_name 'Polyandrocarpa lectin' _Abbreviation_common SmtB _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'SmtB subunit 1' $SmtB 'SmtB subunit 2' $SmtB Zn1 $ZN Zn2 $ZN Zn3 $ZN Zn4 $ZN stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state dimer _System_paramagnetic no _System_thiol_state 'not reported' loop_ _Magnetic_equivalence_ID _Magnetically_equivalent_system_component 1 'SmtB subunit 1' 2 'SmtB subunit 2' stop_ _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_SmtB _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'transcriptional repressor' _Abbreviation_common SmtB _Molecular_mass 13395.2 _Mol_thiol_state 'not reported' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 121 _Mol_residue_sequence ; TKPVLQDGETVVCQGTHAAI ASELQAIAPEVAQSLAEFFA VLADPNRLRLLSLLARSELC VGDLAQAIGVSESAVSHQLR SLRNLRLVSYRKQGRHVYYQ LQDHHIVALYQNALDHLQEC R ; loop_ _Residue_seq_code _Residue_label 1 THR 2 LYS 3 PRO 4 VAL 5 LEU 6 GLN 7 ASP 8 GLY 9 GLU 10 THR 11 VAL 12 VAL 13 CYS 14 GLN 15 GLY 16 THR 17 HIS 18 ALA 19 ALA 20 ILE 21 ALA 22 SER 23 GLU 24 LEU 25 GLN 26 ALA 27 ILE 28 ALA 29 PRO 30 GLU 31 VAL 32 ALA 33 GLN 34 SER 35 LEU 36 ALA 37 GLU 38 PHE 39 PHE 40 ALA 41 VAL 42 LEU 43 ALA 44 ASP 45 PRO 46 ASN 47 ARG 48 LEU 49 ARG 50 LEU 51 LEU 52 SER 53 LEU 54 LEU 55 ALA 56 ARG 57 SER 58 GLU 59 LEU 60 CYS 61 VAL 62 GLY 63 ASP 64 LEU 65 ALA 66 GLN 67 ALA 68 ILE 69 GLY 70 VAL 71 SER 72 GLU 73 SER 74 ALA 75 VAL 76 SER 77 HIS 78 GLN 79 LEU 80 ARG 81 SER 82 LEU 83 ARG 84 ASN 85 LEU 86 ARG 87 LEU 88 VAL 89 SER 90 TYR 91 ARG 92 LYS 93 GLN 94 GLY 95 ARG 96 HIS 97 VAL 98 TYR 99 TYR 100 GLN 101 LEU 102 GLN 103 ASP 104 HIS 105 HIS 106 ILE 107 VAL 108 ALA 109 LEU 110 TYR 111 GLN 112 ASN 113 ALA 114 LEU 115 ASP 116 HIS 117 LEU 118 GLN 119 GLU 120 CYS 121 ARG stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-08-11 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 BMRB 4128 "cyanobacterial metallothionein gene repressor" 100.00 121 100.00 100.00 9.24e-80 PDB 1R1T "Crystal Structure Of The Cyanobacterial Metallothionein Repressor Smtb In The Apo-Form" 100.00 122 100.00 100.00 1.01e-79 PDB 1R22 "Crystal Structure Of The Cyanobacterial Metallothionein Repressor Smtb (C14sC61SC121S MUTANT) IN THE ZN2ALPHA5- Form" 100.00 122 97.52 97.52 8.85e-77 PDB 1R23 "Crystal Structure Of The Cyanobacterial Metallothionein Repressor Smtb In The Zn1-Form (One Zn(Ii) Per Dimer)" 100.00 122 100.00 100.00 1.01e-79 PDB 1SMT "Smtb Repressor From Synechococcus Pcc7942" 100.00 122 100.00 100.00 1.01e-79 DBJ BAD78452 "zinc-responsive repressor ZiaR [Synechococcus elongatus PCC 6301]" 100.00 122 100.00 100.00 1.01e-79 EMBL CAA45872 "SmtB [Synechococcus elongatus PCC 7942]" 100.00 122 100.00 100.00 1.01e-79 GB AAT01609 "hypothetical metal-binding protein [Desulfomicrobium norvegicum]" 76.03 106 100.00 100.00 3.94e-56 GB AAT01610 "hypothetical metal-binding protein, partial [uncultured sulfate-reducing bacterium]" 76.03 106 100.00 100.00 3.94e-56 GB AAT01611 "hypothetical metal-binding protein, partial [Desulfovibrio vulgaris]" 76.03 106 100.00 100.00 3.94e-56 GB AAT01612 "hypothetical metal-binding protein [Desulfovibrio desulfuricans]" 64.46 78 100.00 100.00 3.98e-44 GB AAT01613 "hypothetical metal-binding protein, partial [Desulfococcus multivorans]" 76.03 106 100.00 100.00 3.94e-56 REF WP_011242576 "MULTISPECIES: transcriptional regulator [Synechococcus]" 100.00 122 100.00 100.00 1.01e-79 SP P30340 "RecName: Full=Transcriptional repressor SmtB" 100.00 122 100.00 100.00 1.01e-79 stop_ save_ ############# # Ligands # ############# save_ZN _Saveframe_category ligand _Mol_type non-polymer _Name_common "ZN (ZINC ION)" _BMRB_code . _PDB_code ZN _Molecular_mass 65.409 _Mol_charge 2 _Mol_paramagnetic . _Mol_aromatic no _Details ; Information obtained from PDB's Chemical Component Dictionary at http://wwpdb-remediation.rutgers.edu/downloads.html Downloaded on Wed Jul 13 13:29:39 2011 ; loop_ _Atom_name _PDB_atom_name _Atom_type _Atom_chirality _Atom_charge _Atom_oxidation_number _Atom_unpaired_electrons ZN ZN ZN . 2 . ? 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 $SmtB . . . . . . 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 $SmtB 'recombinant technology' 'E. coli' Escherichia coli BL21(DE3) T-21d stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_one _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $SmtB 0.6 mM '[U-15N; U-13C]' H2O 90 % . D2O 10 % . stop_ save_ save_sample_two _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $SmtB 0.6 mM [U-15N]-A,V,L,H,R H2O 90 % . D2O 10 % . stop_ save_ ############################# # Purity of the molecules # ############################# save_mol_purity_list _Saveframe_category sample_mol_purity _Sample_label $sample_one loop_ _Mol_label _Mol_purity_value _Mol_purity_value_units _Mol_purity_measurement_method $SmtB 95 % 'SDS gel electrophoresis' stop_ save_ ############################ # Computer software used # ############################ save_NMR-PIPE _Saveframe_category software _Name NMR-PIPE _Version 1.6 loop_ _Task 'peak picking and assignments' stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model DMX _Field_strength 500 _Details . save_ ############################# # NMR applied experiments # ############################# save_2D_1H-15N_HSQC_1 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-15N HSQC' _Sample_label . save_ save_3D_HNCACB_2 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCACB' _Sample_label . save_ save_3D_CBCA(CO)NH_3 _Saveframe_category NMR_applied_experiment _Experiment_name '3D CBCA(CO)NH' _Sample_label . save_ save_3D_HNCA_4 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCA' _Sample_label . save_ save_3D_HN(CO)CA_5 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HN(CO)CA' _Sample_label . save_ save_NMR_spec_expt__0_1 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-15N HSQC' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_2 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCACB' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_3 _Saveframe_category NMR_applied_experiment _Experiment_name '3D CBCA(CO)NH' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_4 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCA' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_5 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HN(CO)CA' _BMRB_pulse_sequence_accession_number . _Details . save_ ####################### # Sample conditions # ####################### save_Ex-cond_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 6.0 0.05 n/a temperature 313 0.1 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 C 13 'methyl protons' ppm 0.0 . indirect . . . 0.2514495 DSS H 1 'methyl protons' ppm 0.00 internal direct . . . . DSS N 15 'methyl protons' ppm 0.0 . indirect . . . 0.1013291 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_assignment_SmtB _Saveframe_category assigned_chemical_shifts _Details . loop_ _Sample_label $sample_one $sample_two stop_ _Sample_conditions_label $Ex-cond_1 _Chem_shift_reference_set_label $chemical_shift_reference _Mol_system_component_name 'SmtB subunit 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 PRO CA C 63.35 0.35 1 2 . 4 VAL H H 8.23 0.04 1 3 . 4 VAL CA C 62.59 0.35 1 4 . 4 VAL N N 120.78 0.05 1 5 . 5 LEU H H 8.3 0.04 1 6 . 5 LEU CA C 55.2 0.35 1 7 . 5 LEU N N 126.11 0.05 1 8 . 6 GLN H H 8.43 0.04 1 9 . 6 GLN CA C 55.89 0.35 1 10 . 6 GLN N N 121.63 0.05 1 11 . 7 ASP H H 8.4 0.04 1 12 . 7 ASP CA C 54.81 0.35 1 13 . 7 ASP N N 121.96 0.05 1 14 . 8 GLY H H 8.37 0.04 1 15 . 8 GLY CA C 45.71 0.35 1 16 . 8 GLY N N 109.01 0.05 1 17 . 9 GLU H H 8.27 0.04 1 18 . 9 GLU CA C 56.87 0.35 1 19 . 9 GLU N N 120.27 0.05 1 20 . 10 THR H H 8.31 0.04 1 21 . 10 THR CA C 62.24 0.35 1 22 . 10 THR N N 116.64 0.05 1 23 . 11 VAL H H 8.02 0.04 1 24 . 11 VAL CA C 61.99 0.35 1 25 . 11 VAL N N 121.26 0.05 1 26 . 12 VAL H H 7.71 0.04 1 27 . 12 VAL CA C 59.64 0.35 1 28 . 12 VAL N N 115.41 0.05 1 29 . 13 CYS H H 7.47 0.04 1 30 . 13 CYS CA C 60.79 0.35 1 31 . 13 CYS N N 117.97 0.05 1 32 . 14 GLN H H 8.38 0.04 1 33 . 14 GLN CA C 55.42 0.35 1 34 . 14 GLN N N 120.07 0.05 1 35 . 15 GLY H H 8.03 0.04 1 36 . 15 GLY CA C 44.68 0.35 1 37 . 15 GLY N N 107.29 0.05 1 38 . 16 THR H H 8 0.04 1 39 . 16 THR CA C 62.35 0.35 1 40 . 16 THR N N 111.37 0.05 1 41 . 17 HIS H H 8.65 0.04 1 42 . 17 HIS CA C 57.13 0.35 1 43 . 17 HIS N N 120.18 0.05 1 44 . 18 ALA H H 8.76 0.04 1 45 . 18 ALA CA C 51.75 0.35 1 46 . 18 ALA N N 126.95 0.05 1 47 . 19 ALA H H 8.33 0.04 1 48 . 19 ALA CA C 53.05 0.35 1 49 . 19 ALA N N 123.6 0.05 1 50 . 20 ILE H H 8.01 0.04 1 51 . 20 ILE CA C 60.86 0.35 1 52 . 20 ILE N N 119.11 0.05 1 53 . 21 ALA H H 8.42 0.04 1 54 . 21 ALA CA C 53.15 0.35 1 55 . 21 ALA N N 127.16 0.05 1 56 . 22 SER H H 8.34 0.04 1 57 . 22 SER CA C 60.13 0.35 1 58 . 22 SER N N 115.73 0.05 1 59 . 23 GLU H H 8.49 0.04 1 60 . 23 GLU CA C 57.51 0.35 1 61 . 23 GLU N N 119.28 0.05 1 62 . 24 LEU H H 7.7 0.04 1 63 . 24 LEU CA C 54.97 0.35 1 64 . 24 LEU N N 122.7 0.05 1 65 . 25 GLN H H 7.75 0.04 1 66 . 25 GLN CA C 54.72 0.35 1 67 . 25 GLN N N 121.28 0.05 1 68 . 26 ALA H H 8.68 0.04 1 69 . 26 ALA CA C 50.83 0.35 1 70 . 26 ALA N N 126.43 0.05 1 71 . 27 ILE H H 7.84 0.04 1 72 . 27 ILE CA C 62.47 0.35 1 73 . 27 ILE N N 114.01 0.05 1 74 . 28 ALA H H 8.6 0.04 1 75 . 28 ALA CA C 51.07 0.35 1 76 . 28 ALA N N 125.56 0.05 1 77 . 29 PRO CA C 66.72 0.35 1 78 . 30 GLU H H 9.78 0.04 1 79 . 30 GLU CA C 60.32 0.35 1 80 . 30 GLU N N 116.75 0.05 1 81 . 31 VAL H H 7.11 0.04 1 82 . 31 VAL CA C 65.71 0.35 1 83 . 31 VAL N N 122.22 0.05 1 84 . 32 ALA H H 8.4 0.04 1 85 . 32 ALA CA C 55.93 0.35 1 86 . 32 ALA N N 121.92 0.05 1 87 . 33 GLN H H 8.57 0.04 1 88 . 33 GLN CA C 59.41 0.35 1 89 . 33 GLN N N 117.01 0.05 1 90 . 34 SER H H 7.67 0.04 1 91 . 34 SER CA C 62.45 0.35 1 92 . 34 SER N N 116.41 0.05 1 93 . 35 LEU H H 8.77 0.04 1 94 . 35 LEU CA C 57.38 0.35 1 95 . 35 LEU N N 123.96 0.05 1 96 . 36 ALA H H 8.6 0.04 1 97 . 36 ALA CA C 56.28 0.35 1 98 . 36 ALA N N 123.14 0.05 1 99 . 37 GLU H H 7.87 0.04 1 100 . 37 GLU CA C 59.28 0.35 1 101 . 37 GLU N N 117.47 0.05 1 102 . 38 PHE H H 7.61 0.04 1 103 . 38 PHE CA C 61.44 0.35 1 104 . 38 PHE N N 120.6 0.05 1 105 . 39 PHE H H 8.29 0.04 1 106 . 39 PHE CA C 62.41 0.35 1 107 . 39 PHE N N 115.83 0.05 1 108 . 40 ALA H H 8.57 0.04 1 109 . 40 ALA CA C 55.4 0.35 1 110 . 40 ALA N N 119.95 0.05 1 111 . 41 VAL H H 7.38 0.04 1 112 . 41 VAL CA C 64.86 0.35 1 113 . 41 VAL N N 116.99 0.05 1 114 . 42 LEU H H 6.94 0.04 1 115 . 42 LEU CA C 55.32 0.35 1 116 . 42 LEU N N 118.69 0.05 1 117 . 43 ALA H H 7.16 0.04 1 118 . 43 ALA CA C 51.41 0.35 1 119 . 43 ALA N N 120.46 0.05 1 120 . 44 ASP H H 7.98 0.04 1 121 . 44 ASP CA C 51.47 0.35 1 122 . 44 ASP N N 120.85 0.05 1 123 . 45 PRO CA C 65.36 0.35 1 124 . 46 ASN H H 8.16 0.04 1 125 . 46 ASN CA C 56.97 0.35 1 126 . 46 ASN N N 116.64 0.05 1 127 . 47 ARG H H 8.53 0.04 1 128 . 47 ARG CA C 61.17 0.35 1 129 . 47 ARG N N 120.61 0.05 1 130 . 48 LEU H H 7.99 0.04 1 131 . 48 LEU CA C 58.27 0.35 1 132 . 48 LEU N N 117.78 0.05 1 133 . 49 ARG H H 8.23 0.04 1 134 . 49 ARG CA C 61.13 0.35 1 135 . 49 ARG N N 119.2 0.05 1 136 . 50 LEU H H 7.64 0.04 1 137 . 50 LEU CA C 59.21 0.35 1 138 . 50 LEU N N 119.72 0.05 1 139 . 51 LEU H H 8.18 0.04 1 140 . 51 LEU CA C 58.73 0.35 1 141 . 51 LEU N N 118.53 0.05 1 142 . 52 SER H H 8.36 0.04 1 143 . 52 SER CA C 61.48 0.35 1 144 . 52 SER N N 113.13 0.05 1 145 . 53 LEU H H 7.13 0.04 1 146 . 53 LEU CA C 57.75 0.35 1 147 . 53 LEU N N 124.11 0.05 1 148 . 54 LEU H H 7.37 0.04 1 149 . 54 LEU CA C 55.52 0.35 1 150 . 54 LEU N N 118.45 0.05 1 151 . 55 ALA H H 8.12 0.04 1 152 . 55 ALA CA C 54.08 0.35 1 153 . 55 ALA N N 119.41 0.05 1 154 . 56 ARG H H 7.53 0.04 1 155 . 56 ARG CA C 57.12 0.35 1 156 . 56 ARG N N 115.65 0.05 1 157 . 57 SER H H 7.88 0.04 1 158 . 57 SER CA C 57.93 0.35 1 159 . 57 SER N N 113.04 0.05 1 160 . 58 GLU H H 8.12 0.04 1 161 . 58 GLU CA C 57.5 0.35 1 162 . 58 GLU N N 122.39 0.05 1 163 . 59 LEU H H 8.25 0.04 1 164 . 59 LEU CA C 54.44 0.35 1 165 . 59 LEU N N 127.5 0.05 1 166 . 60 CYS H H 9.38 0.04 1 167 . 60 CYS CA C 56.85 0.35 1 168 . 60 CYS N N 119.54 0.05 1 169 . 61 VAL H H 7.8 0.04 1 170 . 61 VAL CA C 67.75 0.35 1 171 . 61 VAL N N 118.15 0.05 1 172 . 62 GLY H H 8.6 0.04 1 173 . 62 GLY CA C 46.19 0.35 1 174 . 62 GLY N N 108.3 0.05 1 175 . 63 ASP H H 8.09 0.04 1 176 . 63 ASP CA C 57.78 0.35 1 177 . 63 ASP N N 127.17 0.05 1 178 . 64 LEU H H 8.58 0.04 1 179 . 64 LEU CA C 58.59 0.35 1 180 . 64 LEU N N 121.28 0.05 1 181 . 65 ALA H H 8.26 0.04 1 182 . 65 ALA CA C 55.77 0.35 1 183 . 65 ALA N N 118.69 0.05 1 184 . 66 GLN H H 7.59 0.04 1 185 . 66 GLN CA C 58.75 0.35 1 186 . 66 GLN N N 115.46 0.05 1 187 . 67 ALA H H 8.21 0.04 1 188 . 67 ALA CA C 55.04 0.35 1 189 . 67 ALA N N 121.11 0.05 1 190 . 68 ILE H H 7.71 0.04 1 191 . 68 ILE CA C 60.65 0.35 1 192 . 68 ILE N N 110.73 0.05 1 193 . 69 GLY H H 8.12 0.04 1 194 . 69 GLY CA C 47.03 0.35 1 195 . 69 GLY N N 111.82 0.05 1 196 . 70 VAL H H 7.73 0.04 1 197 . 70 VAL CA C 59.18 0.35 1 198 . 70 VAL N N 113.06 0.05 1 199 . 71 SER H H 8.23 0.04 1 200 . 71 SER CA C 57.85 0.35 1 201 . 71 SER N N 114.94 0.05 1 202 . 72 GLU H H 9.17 0.04 1 203 . 72 GLU CA C 61.05 0.35 1 204 . 72 GLU N N 120.82 0.05 1 205 . 73 SER H H 8.45 0.04 1 206 . 73 SER CA C 61.54 0.35 1 207 . 73 SER N N 113.71 0.05 1 208 . 74 ALA H H 7.86 0.04 1 209 . 74 ALA CA C 55.49 0.35 1 210 . 74 ALA N N 126.01 0.05 1 211 . 75 VAL H H 8.08 0.04 1 212 . 75 VAL CA C 66.72 0.35 1 213 . 75 VAL N N 118.41 0.05 1 214 . 76 SER H H 8.47 0.04 1 215 . 76 SER CA C 62.15 0.35 1 216 . 76 SER N N 115.64 0.05 1 217 . 77 HIS H H 7.92 0.04 1 218 . 77 HIS CA C 59.70 0.35 1 219 . 77 HIS N N 120.07 0.05 1 220 . 78 GLN H H 7.72 0.04 1 221 . 78 GLN CA C 58.59 0.35 1 222 . 78 GLN N N 118.77 0.05 1 223 . 79 LEU H H 8.41 0.04 1 224 . 79 LEU CA C 57.35 0.35 1 225 . 79 LEU N N 117.57 0.05 1 226 . 80 ARG H H 7.83 0.04 1 227 . 80 ARG CA C 60.46 0.35 1 228 . 80 ARG N N 120.84 0.05 1 229 . 81 SER H H 7.72 0.04 1 230 . 81 SER CA C 62.25 0.35 1 231 . 81 SER N N 114.06 0.05 1 232 . 82 LEU H H 7.26 0.04 1 233 . 82 LEU CA C 57.48 0.35 1 234 . 82 LEU N N 118.22 0.05 1 235 . 83 ARG H H 8.87 0.04 1 236 . 83 ARG CA C 59.56 0.35 1 237 . 83 ARG N N 123.03 0.05 1 238 . 84 ASN H H 8.52 0.04 1 239 . 84 ASN CA C 56.22 0.35 1 240 . 84 ASN N N 120.66 0.05 1 241 . 85 LEU H H 7.32 0.04 1 242 . 85 LEU CA C 53.77 0.35 1 243 . 85 LEU N N 118.94 0.05 1 244 . 86 ARG H H 8.14 0.04 1 245 . 86 ARG CA C 57.74 0.35 1 246 . 86 ARG N N 111.26 0.05 1 247 . 87 LEU H H 8.7 0.04 1 248 . 87 LEU CA C 57.86 0.35 1 249 . 87 LEU N N 115.98 0.05 1 250 . 88 VAL H H 7.15 0.04 1 251 . 88 VAL CA C 57.81 0.35 1 252 . 88 VAL N N 106.94 0.05 1 253 . 89 SER H H 9.03 0.04 1 254 . 89 SER CA C 56.65 0.35 1 255 . 89 SER N N 116.02 0.05 1 256 . 90 TYR H H 7.9 0.04 1 257 . 90 TYR CA C 55.38 0.35 1 258 . 90 TYR N N 115.51 0.05 1 259 . 91 ARG H H 8.98 0.04 1 260 . 91 ARG CA C 54.93 0.35 1 261 . 91 ARG N N 118.49 0.05 1 262 . 92 LYS H H 9 0.04 1 263 . 92 LYS CA C 56.07 0.35 1 264 . 92 LYS N N 124.45 0.05 1 265 . 93 GLN H H 8.8 0.04 1 266 . 93 GLN CA C 56.19 0.35 1 267 . 93 GLN N N 126.25 0.05 1 268 . 94 GLY CA C 47.37 0.35 1 269 . 95 ARG H H 8.91 0.04 1 270 . 95 ARG CA C 55.94 0.35 1 271 . 95 ARG N N 124.08 0.05 1 272 . 96 HIS H H 7.93 0.04 1 273 . 96 HIS CA C 55.47 0.35 1 274 . 96 HIS N N 116.83 0.05 1 275 . 97 VAL H H 8.75 0.04 1 276 . 97 VAL CA C 62.29 0.35 1 277 . 97 VAL N N 125.01 0.05 1 278 . 98 TYR H H 8.95 0.04 1 279 . 98 TYR CA C 59.18 0.35 1 280 . 98 TYR N N 124.83 0.05 1 281 . 99 TYR H H 9.24 0.04 1 282 . 99 TYR CA C 57.67 0.35 1 283 . 99 TYR N N 123.78 0.05 1 284 . 100 GLN H H 8.43 0.04 1 285 . 100 GLN CA C 54.13 0.35 1 286 . 100 GLN N N 111.84 0.05 1 287 . 101 LEU H H 9.02 0.04 1 288 . 101 LEU CA C 56 0.35 1 289 . 101 LEU N N 120.26 0.05 1 290 . 102 GLN H H 8.05 0.04 1 291 . 102 GLN CA C 61.09 0.35 1 292 . 102 GLN N N 120.67 0.05 1 293 . 103 ASP H H 7.12 0.04 1 294 . 103 ASP CA C 52.94 0.35 1 295 . 103 ASP N N 106.45 0.05 1 296 . 104 HIS CA C 58.78 0.35 1 297 . 105 HIS H H 7.66 0.04 1 298 . 105 HIS CA C 59.60 0.35 1 299 . 105 HIS N N 119.66 0.05 1 300 . 106 ILE H H 7.60 0.04 1 301 . 106 ILE CA C 61.55 0.35 1 302 . 106 ILE N N 120.61 0.05 1 303 . 107 VAL H H 7.11 0.04 1 304 . 107 VAL CA C 66.83 0.35 1 305 . 107 VAL N N 119.07 0.05 1 306 . 108 ALA H H 7.99 0.04 1 307 . 108 ALA CA C 55.09 0.35 1 308 . 108 ALA N N 118.83 0.05 1 309 . 109 LEU H H 8.51 0.04 1 310 . 109 LEU CA C 59.95 0.35 1 311 . 109 LEU N N 122.13 0.05 1 312 . 110 TYR H H 8.14 0.04 1 313 . 110 TYR CA C 62.7 0.35 1 314 . 110 TYR N N 118.37 0.05 1 315 . 111 GLN H H 8.78 0.04 1 316 . 111 GLN CA C 59.05 0.35 1 317 . 111 GLN N N 116.86 0.05 1 318 . 112 ASN H H 8.37 0.04 1 319 . 112 ASN CA C 58.15 0.35 1 320 . 112 ASN N N 114.54 0.05 1 321 . 113 ALA H H 7.64 0.04 1 322 . 113 ALA CA C 55.52 0.35 1 323 . 113 ALA N N 120.52 0.05 1 324 . 114 LEU H H 8.08 0.04 1 325 . 114 LEU CA C 58.29 0.35 1 326 . 114 LEU N N 119.13 0.05 1 327 . 115 ASP H H 8.61 0.04 1 328 . 115 ASP CA C 57.21 0.35 1 329 . 115 ASP N N 118.23 0.05 1 330 . 116 HIS H H 7.29 0.04 1 331 . 116 HIS CA C 58.29 0.35 1 332 . 116 HIS N N 117.59 0.05 1 333 . 117 LEU H H 7.71 0.04 1 334 . 117 LEU CA C 57.61 0.35 1 335 . 117 LEU N N 120.75 0.05 1 336 . 118 GLN H H 7.65 0.04 1 337 . 118 GLN CA C 57.03 0.35 1 338 . 118 GLN N N 114.54 0.05 1 339 . 119 GLU H H 7.15 0.04 1 340 . 119 GLU CA C 57.42 0.35 1 341 . 119 GLU N N 118.4 0.05 1 342 . 120 CYS H H 7.83 0.04 1 343 . 120 CYS CA C 58.86 0.35 1 344 . 120 CYS N N 117.42 0.05 1 345 . 121 ARG H H 7.77 0.04 1 346 . 121 ARG CA C 57.69 0.35 1 347 . 121 ARG N N 127.93 0.05 1 stop_ save_