data_6404 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; HN, N, CA, CB Chemical Shift Assignments for the CID domain of Pcf11 ; _BMRB_accession_number 6404 _BMRB_flat_file_name bmr6404.str _Entry_type original _Submission_date 2004-10-25 _Accession_date 2004-11-29 _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 Hollingworth David . . 2 Frenkiel Thomas A. . 3 Kelly Geoff . . 4 Noble Christian G. . 5 Taylor Ian A. . 6 Ramos Andres . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 130 "13C chemical shifts" 258 "15N chemical shifts" 130 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2005-07-26 original author . stop_ _Original_release_date 2005-07-26 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title 'Backbone assignment of PCF11 CTD binding domain' _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 Hollingworth David . . 2 Kelly Geoff . . 3 Frenkiel Thomas A. . 4 Noble Christian G. . 5 Taylor Ian A. . 6 Ramos Andres . . stop_ _Journal_abbreviation 'J. Biomol. NMR' _Journal_volume 31 _Journal_issue 4 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 363 _Page_last 363 _Year 2005 _Details . save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name 'Pcf11 CID' _Abbreviation_common 'Pcf11 CID' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'Pcf11 CID' $Pcf11_CID stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state protein _System_paramagnetic no _System_thiol_state 'all free' _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_Pcf11_CID _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'Pcf11 CID' _Name_variant 'Pcf11 CID' _Abbreviation_common 'Pcf11 CID' _Molecular_mass . _Mol_thiol_state 'all free' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 142 _Mol_residue_sequence ; MDHDTEVIVKDFNSILEELT FNSRPIITTLTKLAEENISC AQYFVDAIESRIEKCMPKQK LYAFYALDSICKNVGSPYTI YFSRNLFNLYKRTYLLVDNT TRTKLINMFKLWLNPNDTGL PLFEGSALEKIEQFLIKASA LH ; loop_ _Residue_seq_code _Residue_label 1 MET 2 ASP 3 HIS 4 ASP 5 THR 6 GLU 7 VAL 8 ILE 9 VAL 10 LYS 11 ASP 12 PHE 13 ASN 14 SER 15 ILE 16 LEU 17 GLU 18 GLU 19 LEU 20 THR 21 PHE 22 ASN 23 SER 24 ARG 25 PRO 26 ILE 27 ILE 28 THR 29 THR 30 LEU 31 THR 32 LYS 33 LEU 34 ALA 35 GLU 36 GLU 37 ASN 38 ILE 39 SER 40 CYS 41 ALA 42 GLN 43 TYR 44 PHE 45 VAL 46 ASP 47 ALA 48 ILE 49 GLU 50 SER 51 ARG 52 ILE 53 GLU 54 LYS 55 CYS 56 MET 57 PRO 58 LYS 59 GLN 60 LYS 61 LEU 62 TYR 63 ALA 64 PHE 65 TYR 66 ALA 67 LEU 68 ASP 69 SER 70 ILE 71 CYS 72 LYS 73 ASN 74 VAL 75 GLY 76 SER 77 PRO 78 TYR 79 THR 80 ILE 81 TYR 82 PHE 83 SER 84 ARG 85 ASN 86 LEU 87 PHE 88 ASN 89 LEU 90 TYR 91 LYS 92 ARG 93 THR 94 TYR 95 LEU 96 LEU 97 VAL 98 ASP 99 ASN 100 THR 101 THR 102 ARG 103 THR 104 LYS 105 LEU 106 ILE 107 ASN 108 MET 109 PHE 110 LYS 111 LEU 112 TRP 113 LEU 114 ASN 115 PRO 116 ASN 117 ASP 118 THR 119 GLY 120 LEU 121 PRO 122 LEU 123 PHE 124 GLU 125 GLY 126 SER 127 ALA 128 LEU 129 GLU 130 LYS 131 ILE 132 GLU 133 GLN 134 PHE 135 LEU 136 ILE 137 LYS 138 ALA 139 SER 140 ALA 141 LEU 142 HIS stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2014-05-25 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 1SZ9 "The Rna Polymerase Ii Ctd In Mrna Processing: Beta-Turn Recognition And Beta-Spiral Model" 98.59 144 100.00 100.00 1.89e-97 PDB 1SZA "The Rna Polymerase Ii Ctd In Mrna Processing: Beta-Turn Recognition And Beta-Spiral Model" 98.59 144 100.00 100.00 1.89e-97 PDB 2BF0 "Crystal Structure Of The Rpr Of Pcf11" 96.48 143 98.54 98.54 1.05e-92 DBJ GAA22455 "K7_Pcf11p [Saccharomyces cerevisiae Kyokai no. 7]" 100.00 627 100.00 100.00 4.88e-95 EMBL CAA88508 "unknown [Saccharomyces cerevisiae]" 100.00 626 100.00 100.00 6.29e-95 EMBL CAY78728 "Pcf11p [Saccharomyces cerevisiae EC1118]" 100.00 626 100.00 100.00 5.65e-95 GB AHY75209 "Pcf11p [Saccharomyces cerevisiae YJM993]" 100.00 626 100.00 100.00 5.65e-95 GB EDN60562 "cleavage and polyadenylation factor CF I component [Saccharomyces cerevisiae YJM789]" 100.00 626 100.00 100.00 5.65e-95 GB EDV08088 "protein PCF11 [Saccharomyces cerevisiae RM11-1a]" 100.00 626 100.00 100.00 5.65e-95 GB EDZ73030 "YDR228Cp-like protein [Saccharomyces cerevisiae AWRI1631]" 100.00 626 100.00 100.00 5.65e-95 GB EEU05243 "Pcf11p [Saccharomyces cerevisiae JAY291]" 100.00 626 100.00 100.00 5.65e-95 REF NP_010514 "Pcf11p [Saccharomyces cerevisiae S288c]" 100.00 626 100.00 100.00 6.29e-95 SP P39081 "RecName: Full=Protein PCF11; AltName: Full=protein 1 of CF I [Saccharomyces cerevisiae S288c]" 100.00 626 100.00 100.00 6.29e-95 TPG DAA12070 "TPA: Pcf11p [Saccharomyces cerevisiae S288c]" 100.00 626 100.00 100.00 6.29e-95 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $Pcf11_CID 'brewer's yeast' 4932 Eukaryota Fungi Saccharomices cerevisiae 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 $Pcf11_CID 'recombinant technology' 'Escherichia 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 $Pcf11_CID 0.8 mM '[U-13C; U-15N; U-2H]' stop_ save_ save_sample_2 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $Pcf11_CID 0.8 mM '[U-13C; U-15N]' stop_ save_ save_sample_3 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $Pcf11_CID 0.8 mM [U-15N] stop_ save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model Inova _Field_strength 800 _Details . save_ ############################# # NMR applied experiments # ############################# save_HNCACB_1 _Saveframe_category NMR_applied_experiment _Experiment_name HNCACB _Sample_label . save_ save_HNCA_2 _Saveframe_category NMR_applied_experiment _Experiment_name HNCA _Sample_label . save_ save_TROSY-HNCACB_3 _Saveframe_category NMR_applied_experiment _Experiment_name TROSY-HNCACB _Sample_label . save_ save_TROSY-HNCA_4 _Saveframe_category NMR_applied_experiment _Experiment_name TROSY-HNCA _Sample_label . save_ save_15N-edited_NOESY_5 _Saveframe_category NMR_applied_experiment _Experiment_name '15N-edited NOESY' _Sample_label . save_ save_NMR_spec_expt__0_1 _Saveframe_category NMR_applied_experiment _Experiment_name HNCACB _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_2 _Saveframe_category NMR_applied_experiment _Experiment_name HNCA _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_3 _Saveframe_category NMR_applied_experiment _Experiment_name TROSY-HNCACB _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_4 _Saveframe_category NMR_applied_experiment _Experiment_name TROSY-HNCA _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_5 _Saveframe_category NMR_applied_experiment _Experiment_name '15N-edited NOESY' _BMRB_pulse_sequence_accession_number . _Details . save_ ####################### # Sample conditions # ####################### save_conditions_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 7.4 0.2 pH temperature 300 1 K 'ionic strength' 0.1 0.001 M 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 _Indirect_shift_ratio_citation_label _Correction_value_citation_label DSS H 1 'methyl protons' ppm 0.0 internal direct . . . 1.0 $entry_citation $entry_citation DSS C 13 'methyl protons' ppm 0.0 . indirect . . . 0.251449530 $entry_citation $entry_citation DSS N 15 'methyl protons' ppm 0.0 . indirect . . . 0.101329118 $entry_citation $entry_citation 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 . loop_ _Sample_label $sample_2 stop_ _Sample_conditions_label $conditions_1 _Chem_shift_reference_set_label $chemical_shift_referencing _Mol_system_component_name 'Pcf11 CID' _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 . 5 THR H H 8 . 1 2 . 5 THR N N 116.3 . 1 3 . 5 THR CA C 66.2 . 1 4 . 5 THR CB C 68.5 . 1 5 . 6 GLU H H 8.18 . 1 6 . 6 GLU N N 120.2 . 1 7 . 6 GLU CA C 60.1 . 1 8 . 6 GLU CB C 29.3 . 1 9 . 7 VAL H H 7.66 . 1 10 . 7 VAL N N 116.9 . 1 11 . 7 VAL CA C 66.5 . 1 12 . 7 VAL CB C 31.9 . 1 13 . 8 ILE H H 7.39 . 1 14 . 8 ILE N N 120.1 . 1 15 . 8 ILE CA C 64.3 . 1 16 . 8 ILE CB C 38.3 . 1 17 . 9 VAL H H 8.41 . 1 18 . 9 VAL N N 119.5 . 1 19 . 9 VAL CA C 67.5 . 1 20 . 9 VAL CB C 31.8 . 1 21 . 10 LYS H H 8.37 . 1 22 . 10 LYS N N 120.7 . 1 23 . 10 LYS CA C 60.2 . 1 24 . 10 LYS CB C 31.9 . 1 25 . 11 ASP H H 8.45 . 1 26 . 11 ASP N N 121 . 1 27 . 11 ASP CA C 57.9 . 1 28 . 11 ASP CB C 40.1 . 1 29 . 12 PHE H H 8.5 . 1 30 . 12 PHE N N 120.5 . 1 31 . 12 PHE CA C 62.2 . 1 32 . 12 PHE CB C 41 . 1 33 . 13 ASN H H 8.63 . 1 34 . 13 ASN N N 114.7 . 1 35 . 13 ASN CA C 57.1 . 1 36 . 13 ASN CB C 39.4 . 1 37 . 14 SER H H 8.45 . 1 38 . 14 SER N N 115.2 . 1 39 . 14 SER CA C 62.1 . 1 40 . 14 SER CB C 63.5 . 1 41 . 15 ILE H H 7.81 . 1 42 . 15 ILE N N 122.3 . 1 43 . 15 ILE CA C 64.3 . 1 44 . 15 ILE CB C 37.8 . 1 45 . 16 LEU H H 7.83 . 1 46 . 16 LEU N N 119 . 1 47 . 16 LEU CA C 57.8 . 1 48 . 16 LEU CB C 41.9 . 1 49 . 17 GLU H H 7.5 . 1 50 . 17 GLU N N 113.5 . 1 51 . 17 GLU CA C 58 . 1 52 . 17 GLU CB C 29.5 . 1 53 . 18 GLU H H 7.5 . 1 54 . 18 GLU N N 114.2 . 1 55 . 18 GLU CA C 55.9 . 1 56 . 18 GLU CB C 29.4 . 1 57 . 19 LEU H H 7.8 . 1 58 . 19 LEU N N 122.5 . 1 59 . 19 LEU CA C 53.6 . 1 60 . 19 LEU CB C 40 . 1 61 . 20 THR H H 8.67 . 1 62 . 20 THR N N 114.2 . 1 63 . 20 THR CA C 61.3 . 1 64 . 20 THR CB C 69.8 . 1 65 . 21 PHE H H 7.67 . 1 66 . 21 PHE N N 116.5 . 1 67 . 21 PHE CA C 54 . 1 68 . 21 PHE CB C 38.5 . 1 69 . 22 ASN H H 8.4 . 1 70 . 22 ASN N N 115.7 . 1 71 . 22 ASN CA C 52 . 1 72 . 22 ASN CB C 36 . 1 73 . 23 SER H H 6.81 . 1 74 . 23 SER N N 118 . 1 75 . 23 SER CA C 55.6 . 1 76 . 23 SER CB C 61.5 . 1 77 . 24 ARG H H 8.97 . 1 78 . 24 ARG N N 127.7 . 1 79 . 24 ARG CA C 59.8 . 1 80 . 24 ARG CB C 25.9 . 1 81 . 25 PRO CA C 66.8 . 1 82 . 26 ILE H H 7.54 . 1 83 . 26 ILE N N 117.5 . 1 84 . 26 ILE CA C 65.5 . 1 85 . 26 ILE CB C 36.8 . 1 86 . 27 ILE H H 8.18 . 1 87 . 27 ILE N N 119.2 . 1 88 . 27 ILE CA C 66.7 . 1 89 . 27 ILE CB C 37.3 . 1 90 . 28 THR H H 9.04 . 1 91 . 28 THR N N 119.3 . 1 92 . 28 THR CA C 67.5 . 1 93 . 28 THR CB C 68.9 . 1 94 . 29 THR H H 8.18 . 1 95 . 29 THR N N 121.2 . 1 96 . 29 THR CA C 67.5 . 1 97 . 29 THR CB C 68.8 . 1 98 . 30 LEU H H 8.59 . 1 99 . 30 LEU N N 119.5 . 1 100 . 30 LEU CA C 58.2 . 1 101 . 30 LEU CB C 41.7 . 1 102 . 31 THR H H 7.88 . 1 103 . 31 THR N N 114 . 1 104 . 31 THR CA C 67.4 . 1 105 . 31 THR CB C 69 . 1 106 . 32 LYS H H 8.12 . 1 107 . 32 LYS N N 122 . 1 108 . 32 LYS CA C 59.1 . 1 109 . 32 LYS CB C 31.9 . 1 110 . 33 LEU H H 8.42 . 1 111 . 33 LEU N N 117.8 . 1 112 . 33 LEU CA C 58.5 . 1 113 . 33 LEU CB C 42.6 . 1 114 . 34 ALA H H 8.1 . 1 115 . 34 ALA N N 119 . 1 116 . 34 ALA CA C 54.4 . 1 117 . 34 ALA CB C 17.7 . 1 118 . 35 GLU H H 8.13 . 1 119 . 35 GLU N N 118.2 . 1 120 . 35 GLU CA C 58.9 . 1 121 . 35 GLU CB C 30.6 . 1 122 . 36 GLU H H 8.43 . 1 123 . 36 GLU N N 115.2 . 1 124 . 36 GLU CA C 58.1 . 1 125 . 36 GLU CB C 31 . 1 126 . 37 ASN H H 7.71 . 1 127 . 37 ASN N N 116 . 1 128 . 37 ASN CA C 51.9 . 1 129 . 37 ASN CB C 39.8 . 1 130 . 38 ILE H H 7.72 . 1 131 . 38 ILE N N 120.5 . 1 132 . 38 ILE CA C 64.6 . 1 133 . 38 ILE CB C 38.1 . 1 134 . 39 SER H H 8.81 . 1 135 . 39 SER N N 117 . 1 136 . 39 SER CA C 61.2 . 1 137 . 39 SER CB C 62.1 . 1 138 . 40 CYS H H 7.97 . 1 139 . 40 CYS N N 117.7 . 1 140 . 40 CYS CA C 59 . 1 141 . 40 CYS CB C 27.5 . 1 142 . 41 ALA H H 7.58 . 1 143 . 41 ALA N N 120.2 . 1 144 . 41 ALA CA C 56.3 . 1 145 . 41 ALA CB C 18.9 . 1 146 . 42 GLN H H 8.7 . 1 147 . 42 GLN N N 113.2 . 1 148 . 42 GLN CA C 58.7 . 1 149 . 42 GLN CB C 27.9 . 1 150 . 43 TYR H H 6.86 . 1 151 . 43 TYR N N 115.7 . 1 152 . 43 TYR CA C 59.7 . 1 153 . 43 TYR CB C 37.8 . 1 154 . 44 PHE H H 7.54 . 1 155 . 44 PHE N N 119.5 . 1 156 . 44 PHE CA C 56.6 . 1 157 . 44 PHE CB C 36.6 . 1 158 . 45 VAL H H 8.29 . 1 159 . 45 VAL N N 120.4 . 1 160 . 45 VAL CA C 56.6 . 1 161 . 45 VAL CB C 38.3 . 1 162 . 46 ASP H H 8.09 . 1 163 . 46 ASP N N 118.5 . 1 164 . 46 ASP CA C 57.6 . 1 165 . 46 ASP CB C 31 . 1 166 . 47 ALA H H 8.09 . 1 167 . 47 ALA N N 121.2 . 1 168 . 47 ALA CA C 55.4 . 1 169 . 47 ALA CB C 18.7 . 1 170 . 48 ILE H H 8.52 . 1 171 . 48 ILE N N 119.3 . 1 172 . 48 ILE CA C 65.7 . 1 173 . 48 ILE CB C 37.4 . 1 174 . 49 GLU H H 9.09 . 1 175 . 49 GLU N N 118.3 . 1 176 . 49 GLU CA C 61.2 . 1 177 . 49 GLU CB C 28.8 . 1 178 . 50 SER H H 8.44 . 1 179 . 50 SER N N 112.7 . 1 180 . 50 SER CA C 61.6 . 1 181 . 50 SER CB C 63 . 1 182 . 51 ARG H H 7.84 . 1 183 . 51 ARG N N 119.2 . 1 184 . 51 ARG CA C 58.7 . 1 185 . 51 ARG CB C 29.1 . 1 186 . 52 ILE H H 8.26 . 1 187 . 52 ILE N N 117.6 . 1 188 . 52 ILE CA C 66.7 . 1 189 . 52 ILE CB C 38 . 1 190 . 53 GLU H H 8.02 . 1 191 . 53 GLU N N 117.5 . 1 192 . 53 GLU CA C 59.7 . 1 193 . 53 GLU CB C 30.2 . 1 194 . 54 LYS H H 8.23 . 1 195 . 54 LYS N N 114.7 . 1 196 . 54 LYS CA C 58.2 . 1 197 . 54 LYS CB C 34.5 . 1 198 . 55 CYS H H 8.48 . 1 199 . 55 CYS N N 115.9 . 1 200 . 55 CYS CA C 58.5 . 1 201 . 55 CYS CB C 28.2 . 1 202 . 56 MET H H 8.61 . 1 203 . 56 MET N N 118.7 . 1 204 . 56 MET CA C 54.4 . 1 205 . 56 MET CB C 31.2 . 1 206 . 58 LYS H H 8.19 . 1 207 . 58 LYS N N 112.7 . 1 208 . 58 LYS CA C 59 . 1 209 . 58 LYS CB C 32 . 1 210 . 59 GLN H H 8.01 . 1 211 . 59 GLN N N 113.5 . 1 212 . 59 GLN CA C 55.9 . 1 213 . 59 GLN CB C 29.5 . 1 214 . 60 LYS H H 7.51 . 1 215 . 60 LYS N N 121.7 . 1 216 . 60 LYS CA C 61.1 . 1 217 . 60 LYS CB C 34.2 . 1 218 . 61 LEU H H 8.5 . 1 219 . 61 LEU N N 115.7 . 1 220 . 61 LEU CA C 57.5 . 1 221 . 61 LEU CB C 41.4 . 1 222 . 62 TYR H H 5.97 . 1 223 . 62 TYR N N 113.2 . 1 224 . 62 TYR CA C 58.6 . 1 225 . 62 TYR CB C 36.3 . 1 226 . 63 ALA H H 7.07 . 1 227 . 63 ALA N N 118.7 . 1 228 . 63 ALA CA C 55.2 . 1 229 . 63 ALA CB C 17.9 . 1 230 . 64 PHE H H 7.81 . 1 231 . 64 PHE N N 118 . 1 232 . 64 PHE CA C 63.5 . 1 233 . 64 PHE CB C 38.5 . 1 234 . 65 TYR H H 8.55 . 1 235 . 65 TYR N N 117.5 . 1 236 . 65 TYR CA C 58.4 . 1 237 . 65 TYR CB C 36 . 1 238 . 66 ALA H H 7.85 . 1 239 . 66 ALA N N 123.2 . 1 240 . 66 ALA CA C 56 . 1 241 . 66 ALA CB C 17.2 . 1 242 . 67 LEU H H 7.75 . 1 243 . 67 LEU N N 120.2 . 1 244 . 67 LEU CA C 60.5 . 1 245 . 67 LEU CB C 43 . 1 246 . 68 ASP H H 9.12 . 1 247 . 68 ASP N N 119.7 . 1 248 . 68 ASP CA C 59 . 1 249 . 68 ASP CB C 44.5 . 1 250 . 69 SER H H 8.09 . 1 251 . 69 SER N N 109.5 . 1 252 . 69 SER CA C 61.1 . 1 253 . 69 SER CB C 63.1 . 1 254 . 70 ILE H H 8.49 . 1 255 . 70 ILE N N 119 . 1 256 . 70 ILE CA C 66.4 . 1 257 . 70 ILE CB C 38 . 1 258 . 71 CYS H H 8.36 . 1 259 . 71 CYS N N 116.5 . 1 260 . 71 CYS CA C 66.2 . 1 261 . 71 CYS CB C 27.4 . 1 262 . 72 LYS H H 8.53 . 1 263 . 72 LYS N N 117.7 . 1 264 . 72 LYS CA C 59.4 . 1 265 . 72 LYS CB C 33.4 . 1 266 . 73 ASN H H 8.22 . 1 267 . 73 ASN N N 111.5 . 1 268 . 73 ASN CA C 55.6 . 1 269 . 73 ASN CB C 39.7 . 1 270 . 74 VAL H H 8.11 . 1 271 . 74 VAL N N 118.5 . 1 272 . 74 VAL CA C 64.4 . 1 273 . 74 VAL CB C 32.2 . 1 274 . 75 GLY H H 7.45 . 1 275 . 75 GLY N N 104.5 . 1 276 . 75 GLY CA C 45.6 . 1 277 . 76 SER H H 8.79 . 1 278 . 76 SER N N 121.7 . 1 279 . 76 SER CA C 57.7 . 1 280 . 76 SER CB C 63.1 . 1 281 . 78 TYR H H 8.28 . 1 282 . 78 TYR N N 126 . 1 283 . 78 TYR CA C 64.3 . 1 284 . 78 TYR CB C 33.2 . 1 285 . 79 THR H H 7.52 . 1 286 . 79 THR N N 106 . 1 287 . 79 THR CA C 64.4 . 1 288 . 79 THR CB C 67.1 . 1 289 . 80 ILE H H 6.74 . 1 290 . 80 ILE N N 120.5 . 1 291 . 80 ILE CA C 64.1 . 1 292 . 80 ILE CB C 37.7 . 1 293 . 81 TYR H H 8.43 . 1 294 . 81 TYR N N 118.7 . 1 295 . 81 TYR CA C 58.6 . 1 296 . 81 TYR CB C 37.8 . 1 297 . 82 PHE H H 9.49 . 1 298 . 82 PHE N N 115.7 . 1 299 . 82 PHE CA C 61.8 . 1 300 . 82 PHE CB C 38.9 . 1 301 . 83 SER H H 7.7 . 1 302 . 83 SER N N 111.2 . 1 303 . 83 SER CA C 63.5 . 1 304 . 84 ARG H H 7.03 . 1 305 . 84 ARG N N 119.2 . 1 306 . 84 ARG CA C 60.2 . 1 307 . 84 ARG CB C 29.3 . 1 308 . 85 ASN H H 8.85 . 1 309 . 85 ASN N N 113.5 . 1 310 . 85 ASN CA C 52.6 . 1 311 . 85 ASN CB C 38.8 . 1 312 . 86 LEU H H 6.8 . 1 313 . 86 LEU N N 120.2 . 1 314 . 86 LEU CA C 58.9 . 1 315 . 86 LEU CB C 42.9 . 1 316 . 87 PHE H H 8.83 . 1 317 . 87 PHE N N 114.5 . 1 318 . 87 PHE CA C 61.2 . 1 319 . 87 PHE CB C 37.6 . 1 320 . 88 ASN H H 8.15 . 1 321 . 88 ASN N N 116.4 . 1 322 . 88 ASN CA C 56.4 . 1 323 . 88 ASN CB C 38 . 1 324 . 89 LEU H H 8.35 . 1 325 . 89 LEU N N 117.5 . 1 326 . 89 LEU CA C 57.9 . 1 327 . 89 LEU CB C 42.4 . 1 328 . 90 TYR H H 9.25 . 1 329 . 90 TYR N N 123.3 . 1 330 . 90 TYR CA C 62.9 . 1 331 . 90 TYR CB C 39.7 . 1 332 . 91 LYS H H 8.69 . 1 333 . 91 LYS N N 118.5 . 1 334 . 91 LYS CA C 59.8 . 1 335 . 91 LYS CB C 31.3 . 1 336 . 92 ARG H H 7.67 . 1 337 . 92 ARG N N 114.3 . 1 338 . 92 ARG CA C 59.4 . 1 339 . 92 ARG CB C 30.4 . 1 340 . 93 THR H H 7.42 . 1 341 . 93 THR N N 112 . 1 342 . 93 THR CA C 68 . 1 343 . 94 TYR H H 8.77 . 1 344 . 94 TYR N N 120.2 . 1 345 . 94 TYR CA C 62.4 . 1 346 . 94 TYR CB C 38.8 . 1 347 . 95 LEU H H 7.88 . 1 348 . 95 LEU N N 113 . 1 349 . 95 LEU CA C 57.4 . 1 350 . 95 LEU CB C 41.9 . 1 351 . 96 LEU H H 7.47 . 1 352 . 96 LEU N N 116.7 . 1 353 . 96 LEU CA C 55.7 . 1 354 . 96 LEU CB C 44.7 . 1 355 . 97 VAL H H 7.1 . 1 356 . 97 VAL N N 110 . 1 357 . 97 VAL CA C 60.4 . 1 358 . 97 VAL CB C 33.5 . 1 359 . 98 ASP H H 7.84 . 1 360 . 98 ASP N N 115 . 1 361 . 98 ASP CA C 52.6 . 1 362 . 98 ASP CB C 41.6 . 1 363 . 99 ASN H H 7.78 . 1 364 . 99 ASN N N 122.8 . 1 365 . 99 ASN CA C 53.4 . 1 366 . 99 ASN CB C 38.1 . 1 367 . 100 THR H H 8.8 . 1 368 . 100 THR N N 113.2 . 1 369 . 100 THR CA C 66.5 . 1 370 . 100 THR CB C 69.6 . 1 371 . 101 THR H H 8.25 . 1 372 . 101 THR N N 120.5 . 1 373 . 101 THR CA C 67.3 . 1 374 . 101 THR CB C 68.6 . 1 375 . 102 ARG H H 8.67 . 1 376 . 102 ARG N N 122.5 . 1 377 . 102 ARG CA C 61.3 . 1 378 . 102 ARG CB C 29.3 . 1 379 . 103 THR H H 7.78 . 1 380 . 103 THR N N 113.2 . 1 381 . 103 THR CA C 67.3 . 1 382 . 103 THR CB C 68.6 . 1 383 . 104 LYS H H 7.29 . 1 384 . 104 LYS N N 119.5 . 1 385 . 104 LYS CA C 59.7 . 1 386 . 104 LYS CB C 32.2 . 1 387 . 105 LEU H H 8.42 . 1 388 . 105 LEU N N 120.5 . 1 389 . 105 LEU CA C 58 . 1 390 . 105 LEU CB C 41 . 1 391 . 106 ILE H H 8.84 . 1 392 . 106 ILE N N 127 . 1 393 . 106 ILE CA C 66.6 . 1 394 . 106 ILE CB C 38 . 1 395 . 107 ASN H H 8.12 . 1 396 . 107 ASN N N 118.2 . 1 397 . 107 ASN CA C 56.3 . 1 398 . 107 ASN CB C 37.6 . 1 399 . 108 MET H H 7.71 . 1 400 . 108 MET N N 118 . 1 401 . 108 MET CA C 58.7 . 1 402 . 108 MET CB C 33.5 . 1 403 . 109 PHE H H 7.2 . 1 404 . 109 PHE N N 118.3 . 1 405 . 109 PHE CA C 59.7 . 1 406 . 109 PHE CB C 38.2 . 1 407 . 110 LYS H H 8.15 . 1 408 . 110 LYS N N 116.7 . 1 409 . 110 LYS CA C 59.9 . 1 410 . 110 LYS CB C 31.8 . 1 411 . 111 LEU H H 7.03 . 1 412 . 111 LEU N N 117 . 1 413 . 111 LEU CA C 56.7 . 1 414 . 111 LEU CB C 41.3 . 1 415 . 112 TRP H H 7.73 . 1 416 . 112 TRP N N 119.2 . 1 417 . 112 TRP CA C 57.1 . 1 418 . 112 TRP CB C 29.3 . 1 419 . 113 LEU H H 7.23 . 1 420 . 113 LEU N N 114.6 . 1 421 . 113 LEU CA C 56.6 . 1 422 . 113 LEU CB C 42.4 . 1 423 . 114 ASN H H 7.24 . 1 424 . 114 ASN N N 111.4 . 1 425 . 114 ASN CA C 51.3 . 1 426 . 114 ASN CB C 38.5 . 1 427 . 118 THR H H 8.04 . 1 428 . 118 THR N N 107.5 . 1 429 . 118 THR CA C 62.7 . 1 430 . 118 THR CB C 70.7 . 1 431 . 119 GLY H H 8.31 . 1 432 . 119 GLY N N 108.7 . 1 433 . 119 GLY CA C 44.6 . 1 434 . 120 LEU H H 7.64 . 1 435 . 120 LEU N N 121 . 1 436 . 120 LEU CA C 51.3 . 1 437 . 120 LEU CB C 42.2 . 1 438 . 121 PRO CA C 62.5 . 1 439 . 121 PRO CB C 33.1 . 1 440 . 122 LEU H H 8.55 . 1 441 . 122 LEU N N 117.8 . 1 442 . 122 LEU CA C 56.8 . 1 443 . 122 LEU CB C 43.9 . 1 444 . 123 PHE H H 6.13 . 1 445 . 123 PHE N N 106.8 . 1 446 . 123 PHE CA C 55.2 . 1 447 . 123 PHE CB C 42.5 . 1 448 . 124 GLU H H 8.23 . 1 449 . 124 GLU N N 118.7 . 1 450 . 124 GLU CA C 55.6 . 1 451 . 124 GLU CB C 30.8 . 1 452 . 125 GLY H H 8.75 . 1 453 . 125 GLY N N 110 . 1 454 . 125 GLY CA C 47.1 . 1 455 . 127 ALA H H 7.78 . 1 456 . 127 ALA N N 123.7 . 1 457 . 127 ALA CA C 56 . 1 458 . 127 ALA CB C 19.2 . 1 459 . 128 LEU H H 7.95 . 1 460 . 128 LEU N N 113.2 . 1 461 . 128 LEU CA C 57.9 . 1 462 . 128 LEU CB C 40.4 . 1 463 . 129 GLU H H 8.5 . 1 464 . 129 GLU N N 120 . 1 465 . 129 GLU CA C 57.9 . 1 466 . 129 GLU CB C 29.3 . 1 467 . 130 LYS H H 7.63 . 1 468 . 130 LYS N N 117.6 . 1 469 . 130 LYS CA C 59.6 . 1 470 . 130 LYS CB C 30.9 . 1 471 . 131 ILE H H 7.96 . 1 472 . 131 ILE N N 119.5 . 1 473 . 131 ILE CA C 66.9 . 1 474 . 131 ILE CB C 37.6 . 1 475 . 132 GLU H H 8.46 . 1 476 . 132 GLU N N 120.1 . 1 477 . 132 GLU CA C 60.5 . 1 478 . 132 GLU CB C 30.1 . 1 479 . 133 GLN H H 8.09 . 1 480 . 133 GLN N N 114 . 1 481 . 133 GLN CA C 58.9 . 1 482 . 133 GLN CB C 28.3 . 1 483 . 134 PHE H H 7.85 . 1 484 . 134 PHE N N 120.6 . 1 485 . 134 PHE CA C 60.8 . 1 486 . 134 PHE CB C 39.1 . 1 487 . 135 LEU H H 8.44 . 1 488 . 135 LEU N N 119.3 . 1 489 . 135 LEU CA C 57.3 . 1 490 . 135 LEU CB C 42 . 1 491 . 136 ILE H H 8.28 . 1 492 . 136 ILE N N 120 . 1 493 . 136 ILE CA C 65.1 . 1 494 . 136 ILE CB C 38.1 . 1 495 . 137 LYS H H 7.75 . 1 496 . 137 LYS N N 120.7 . 1 497 . 137 LYS CA C 58.7 . 1 498 . 137 LYS CB C 31.9 . 1 499 . 138 ALA H H 7.78 . 1 500 . 138 ALA N N 119.7 . 1 501 . 138 ALA CA C 52.5 . 1 502 . 138 ALA CB C 17.5 . 1 503 . 139 SER H H 7.88 . 1 504 . 139 SER N N 112 . 1 505 . 139 SER CA C 59.3 . 1 506 . 139 SER CB C 62 . 1 507 . 140 ALA H H 7.85 . 1 508 . 140 ALA N N 120 . 1 509 . 140 ALA CA C 52.4 . 1 510 . 140 ALA CB C 20.3 . 1 511 . 141 LEU H H 7.44 . 1 512 . 141 LEU N N 117.7 . 1 513 . 141 LEU CA C 54.6 . 1 514 . 141 LEU CB C 43 . 1 515 . 142 HIS H H 7.7 . 1 516 . 142 HIS N N 123.6 . 1 517 . 142 HIS CA C 57.4 . 1 518 . 142 HIS CB C 31 . 1 stop_ save_