data_11177 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Backbone chemical shift assignments for Thermus thermophilus RecO ; _BMRB_accession_number 11177 _BMRB_flat_file_name bmr11177.str _Entry_type original _Submission_date 2010-07-08 _Accession_date 2010-07-08 _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 Inoue Jin . . 2 Nagae Takayuki . . 3 Mishima Masaki . . 4 Ito Yutaka . . 5 Shibata Takehiko . . 6 Mikawa Tsutomu . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 189 "15N chemical shifts" 189 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2011-06-03 original author . stop_ _Original_release_date 2011-06-03 save_ ############################# # Citation for this entry # ############################# save_citation_1 _Saveframe_category entry_citation _Citation_full . _Citation_title 'A mechanism for single-stranded DNA-binding protein (SSB) displacement from single-stranded DNA upon SSB-RecO interaction.' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 21169364 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Inoue Jin . . 2 Nagae Takayuki . . 3 Mishima Masaki . . 4 Ito Yutaka . . 5 Shibata Takehiko . . 6 Mikawa Tsutomu . . stop_ _Journal_abbreviation 'J. Biol. Chem.' _Journal_name_full 'The Journal of biological chemistry' _Journal_volume 286 _Journal_issue 8 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 6720 _Page_last 6732 _Year 2011 _Details . save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name RecO _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label RecO $RecO 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_RecO _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common RecO _Molecular_mass . _Mol_thiol_state 'not present' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 229 _Mol_residue_sequence ; MAPAYTGKVERYRLEEGIVV GRKPLPQGDLLLRLVTPRGS LEAVVRKGQRPTGRTGRLSL FHHVRFQLYAKGEGLPTLTQ AELLGRLHGLEAPRRFLLAA FLAELAYRLASPEAAPRIYP LLVSGLRGIAKHEDPLLPLV WAGWRVAKAGGIGPNLEGEG LRLKRGRLGEEGVYLGREGV EALKATLRLPGAQALPHLEG APLNRLFLALKAHAEEALGP LRSAEAIGV ; loop_ _Residue_seq_code _Residue_label 1 MET 2 ALA 3 PRO 4 ALA 5 TYR 6 THR 7 GLY 8 LYS 9 VAL 10 GLU 11 ARG 12 TYR 13 ARG 14 LEU 15 GLU 16 GLU 17 GLY 18 ILE 19 VAL 20 VAL 21 GLY 22 ARG 23 LYS 24 PRO 25 LEU 26 PRO 27 GLN 28 GLY 29 ASP 30 LEU 31 LEU 32 LEU 33 ARG 34 LEU 35 VAL 36 THR 37 PRO 38 ARG 39 GLY 40 SER 41 LEU 42 GLU 43 ALA 44 VAL 45 VAL 46 ARG 47 LYS 48 GLY 49 GLN 50 ARG 51 PRO 52 THR 53 GLY 54 ARG 55 THR 56 GLY 57 ARG 58 LEU 59 SER 60 LEU 61 PHE 62 HIS 63 HIS 64 VAL 65 ARG 66 PHE 67 GLN 68 LEU 69 TYR 70 ALA 71 LYS 72 GLY 73 GLU 74 GLY 75 LEU 76 PRO 77 THR 78 LEU 79 THR 80 GLN 81 ALA 82 GLU 83 LEU 84 LEU 85 GLY 86 ARG 87 LEU 88 HIS 89 GLY 90 LEU 91 GLU 92 ALA 93 PRO 94 ARG 95 ARG 96 PHE 97 LEU 98 LEU 99 ALA 100 ALA 101 PHE 102 LEU 103 ALA 104 GLU 105 LEU 106 ALA 107 TYR 108 ARG 109 LEU 110 ALA 111 SER 112 PRO 113 GLU 114 ALA 115 ALA 116 PRO 117 ARG 118 ILE 119 TYR 120 PRO 121 LEU 122 LEU 123 VAL 124 SER 125 GLY 126 LEU 127 ARG 128 GLY 129 ILE 130 ALA 131 LYS 132 HIS 133 GLU 134 ASP 135 PRO 136 LEU 137 LEU 138 PRO 139 LEU 140 VAL 141 TRP 142 ALA 143 GLY 144 TRP 145 ARG 146 VAL 147 ALA 148 LYS 149 ALA 150 GLY 151 GLY 152 ILE 153 GLY 154 PRO 155 ASN 156 LEU 157 GLU 158 GLY 159 GLU 160 GLY 161 LEU 162 ARG 163 LEU 164 LYS 165 ARG 166 GLY 167 ARG 168 LEU 169 GLY 170 GLU 171 GLU 172 GLY 173 VAL 174 TYR 175 LEU 176 GLY 177 ARG 178 GLU 179 GLY 180 VAL 181 GLU 182 ALA 183 LEU 184 LYS 185 ALA 186 THR 187 LEU 188 ARG 189 LEU 190 PRO 191 GLY 192 ALA 193 GLN 194 ALA 195 LEU 196 PRO 197 HIS 198 LEU 199 GLU 200 GLY 201 ALA 202 PRO 203 LEU 204 ASN 205 ARG 206 LEU 207 PHE 208 LEU 209 ALA 210 LEU 211 LYS 212 ALA 213 HIS 214 ALA 215 GLU 216 GLU 217 ALA 218 LEU 219 GLY 220 PRO 221 LEU 222 ARG 223 SER 224 ALA 225 GLU 226 ALA 227 ILE 228 GLY 229 VAL stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-02-27 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 11047 ttRecO 100.00 229 100.00 100.00 1.73e-151 DBJ BAD70446 "DNA repair protein RecO [Thermus thermophilus HB8]" 100.00 229 100.00 100.00 1.73e-151 GB AAS80606 "hypothetical conserved protein [Thermus thermophilus HB27]" 100.00 291 98.69 99.56 6.82e-150 GB AEG33049 "DNA repair protein RecO [Thermus thermophilus SG0.5JP17-16]" 96.51 221 98.64 99.55 1.50e-142 GB AFH39328 "recombinational DNA repair protein (RecF pathway) [Thermus thermophilus JL-18]" 96.51 221 98.64 99.55 3.99e-143 GB EIA39541 "hypothetical protein RLTM_04716 [Thermus sp. RL]" 95.63 221 98.17 99.54 3.16e-141 REF WP_008632002 "DNA repair protein RecO [Thermus sp. RL]" 95.63 221 98.17 99.54 3.16e-141 REF WP_011228077 "DNA repair protein RecO [Thermus thermophilus]" 100.00 229 100.00 100.00 1.73e-151 REF WP_014510042 "DNA repair protein RecO [Thermus thermophilus]" 96.51 221 98.64 99.55 1.50e-142 REF WP_014629934 "DNA repair protein RecO [Thermus thermophilus]" 96.51 221 98.64 99.55 3.99e-143 REF WP_024119227 "DNA repair protein RecO [Thermus thermophilus]" 96.51 221 98.64 99.55 3.86e-143 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species _Strain $RecO 'Thermus thermophilus HB8' 300852 Bacteria . Thermus thermophilus HB8 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 $RecO 'recombinant technology' . Escherichia coli . pET11a 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 $RecO 0.4 mM '[U-100% 13C; U-100% 15N]' TRIS 20 mM 'natural abundance' DTT 2 mM 'natural abundance' EDTA 2 mM 'natural abundance' 'Magnesium chloride' 10 mM 'natural abundance' D2O 10 % 'natural abundance' H2O 90 % 'natural abundance' stop_ save_ ############################ # Computer software used # ############################ save_ANSIG _Saveframe_category software _Name ANSIG _Version . loop_ _Vendor _Address _Electronic_address Kraulis . . stop_ loop_ _Task 'chemical shift assignment' stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model Avance _Field_strength 600 _Details . save_ ############################# # NMR applied experiments # ############################# save_2D_1H-15N_HSQC_1 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-15N HSQC' _Sample_label $sample_1 save_ ####################### # Sample conditions # ####################### save_sample_conditions_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 7.5 . pH temperature 313 . 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 protons' ppm 0 na indirect . . . 0.251449530 DSS H 1 'methyl protons' ppm 0 na indirect . . . 1 DSS N 15 'methyl protons' ppm 0 na 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-15N HSQC' stop_ loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $sample_conditions_1 _Chem_shift_reference_set_label $chemical_shift_reference_1 _Mol_system_component_name RecO _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 5 TYR H H 8.04 0.02 1 2 5 5 TYR N N 123.7 0.02 1 3 6 6 THR H H 7.96 0.02 1 4 6 6 THR N N 118 0.02 1 5 7 7 GLY H H 7.56 0.02 1 6 7 7 GLY N N 112.1 0.02 1 7 8 8 LYS H H 7.99 0.02 1 8 8 8 LYS N N 122.5 0.02 1 9 9 9 VAL H H 8 0.02 1 10 9 9 VAL N N 123.5 0.02 1 11 10 10 GLU H H 8.35 0.02 1 12 10 10 GLU N N 126.9 0.02 1 13 11 11 ARG H H 8.23 0.02 1 14 11 11 ARG N N 123.7 0.02 1 15 12 12 TYR H H 7.8 0.02 1 16 12 12 TYR N N 120.7 0.02 1 17 13 13 ARG H H 8.37 0.02 1 18 13 13 ARG N N 122.5 0.02 1 19 14 14 LEU H H 8.17 0.02 1 20 14 14 LEU N N 127.1 0.02 1 21 15 15 GLU H H 8.46 0.02 1 22 15 15 GLU N N 127.8 0.02 1 23 16 16 GLU H H 8.9 0.02 1 24 16 16 GLU N N 121.4 0.02 1 25 17 17 GLY H H 9.03 0.02 1 26 17 17 GLY N N 130.3 0.02 1 27 18 18 ILE H H 8.51 0.02 1 28 18 18 ILE N N 120.4 0.02 1 29 19 19 VAL H H 8.4 0.02 1 30 19 19 VAL N N 128.5 0.02 1 31 21 21 GLY H H 7.52 0.02 1 32 21 21 GLY N N 111.1 0.02 1 33 22 22 ARG H H 8.4 0.02 1 34 22 22 ARG N N 123 0.02 1 35 23 23 LYS H H 7.43 0.02 1 36 23 23 LYS N N 113.8 0.02 1 37 27 27 GLN H H 8.42 0.02 1 38 27 27 GLN N N 115.2 0.02 1 39 28 28 GLY H H 7.96 0.02 1 40 28 28 GLY N N 107 0.02 1 41 29 29 ASP H H 6.91 0.02 1 42 29 29 ASP N N 122.2 0.02 1 43 30 30 LEU H H 8.45 0.02 1 44 30 30 LEU N N 123.1 0.02 1 45 31 31 LEU H H 8.83 0.02 1 46 31 31 LEU N N 129.6 0.02 1 47 32 32 LEU H H 9.32 0.02 1 48 32 32 LEU N N 129.3 0.02 1 49 33 33 ARG H H 7.94 0.02 1 50 33 33 ARG N N 121.4 0.02 1 51 34 34 LEU H H 9.56 0.02 1 52 34 34 LEU N N 124.9 0.02 1 53 35 35 VAL H H 8.34 0.02 1 54 35 35 VAL N N 120.5 0.02 1 55 36 36 THR H H 7.07 0.02 1 56 36 36 THR N N 120.5 0.02 1 57 38 38 ARG H H 7.42 0.02 1 58 38 38 ARG N N 115.3 0.02 1 59 39 39 GLY H H 7.33 0.02 1 60 39 39 GLY N N 110.5 0.02 1 61 40 40 SER H H 8.62 0.02 1 62 40 40 SER N N 122.1 0.02 1 63 41 41 LEU H H 8.99 0.02 1 64 41 41 LEU N N 124.9 0.02 1 65 42 42 GLU H H 7.6 0.02 1 66 42 42 GLU N N 124.2 0.02 1 67 43 43 ALA H H 8.73 0.02 1 68 43 43 ALA N N 124.7 0.02 1 69 44 44 VAL H H 8.58 0.02 1 70 44 44 VAL N N 120.4 0.02 1 71 45 45 VAL H H 9.16 0.02 1 72 45 45 VAL N N 128 0.02 1 73 46 46 ARG H H 9.09 0.02 1 74 46 46 ARG N N 131 0.02 1 75 47 47 LYS H H 9.16 0.02 1 76 47 47 LYS N N 124.6 0.02 1 77 48 48 GLY H H 8.26 0.02 1 78 48 48 GLY N N 109.5 0.02 1 79 49 49 GLN H H 8.05 0.02 1 80 49 49 GLN N N 120.4 0.02 1 81 50 50 ARG H H 7.88 0.02 1 82 50 50 ARG N N 122.7 0.02 1 83 52 52 THR H H 8.02 0.02 1 84 52 52 THR N N 114.3 0.02 1 85 53 53 GLY H H 8.25 0.02 1 86 53 53 GLY N N 112.4 0.02 1 87 55 55 THR H H 7.87 0.02 1 88 55 55 THR N N 113.9 0.02 1 89 56 56 GLY H H 8.07 0.02 1 90 56 56 GLY N N 111.8 0.02 1 91 60 60 LEU H H 7.76 0.02 1 92 60 60 LEU N N 121.5 0.02 1 93 62 62 HIS H H 7.8 0.02 1 94 62 62 HIS N N 121.1 0.02 1 95 63 63 HIS H H 8.48 0.02 1 96 63 63 HIS N N 125.8 0.02 1 97 64 64 VAL H H 9.35 0.02 1 98 64 64 VAL N N 123 0.02 1 99 65 65 ARG H H 8.73 0.02 1 100 65 65 ARG N N 123.7 0.02 1 101 67 67 GLN H H 8.39 0.02 1 102 67 67 GLN N N 119.5 0.02 1 103 68 68 LEU H H 8.99 0.02 1 104 68 68 LEU N N 126.5 0.02 1 105 70 70 ALA H H 8.39 0.02 1 106 70 70 ALA N N 131.7 0.02 1 107 71 71 LYS H H 7.81 0.02 1 108 71 71 LYS N N 123.4 0.02 1 109 72 72 GLY H H 8.23 0.02 1 110 72 72 GLY N N 112.8 0.02 1 111 73 73 GLU H H 8.07 0.02 1 112 73 73 GLU N N 122.1 0.02 1 113 74 74 GLY H H 8.16 0.02 1 114 74 74 GLY N N 111.4 0.02 1 115 75 75 LEU H H 8.11 0.02 1 116 75 75 LEU N N 124.1 0.02 1 117 77 77 THR H H 8.5 0.02 1 118 77 77 THR N N 116.3 0.02 1 119 78 78 LEU H H 8.72 0.02 1 120 78 78 LEU N N 130.8 0.02 1 121 79 79 THR H H 8.82 0.02 1 122 79 79 THR N N 119.7 0.02 1 123 83 83 LEU H H 8.72 0.02 1 124 83 83 LEU N N 127.5 0.02 1 125 85 85 GLY H H 7.71 0.02 1 126 85 85 GLY N N 107.5 0.02 1 127 86 86 ARG H H 8.21 0.02 1 128 86 86 ARG N N 122.9 0.02 1 129 87 87 LEU H H 8.95 0.02 1 130 87 87 LEU N N 127.4 0.02 1 131 90 90 LEU H H 7.39 0.02 1 132 90 90 LEU N N 117.5 0.02 1 133 91 91 GLU H H 8.08 0.02 1 134 91 91 GLU N N 116.2 0.02 1 135 92 92 ALA H H 7.33 0.02 1 136 92 92 ALA N N 127 0.02 1 137 94 94 ARG H H 8.56 0.02 1 138 94 94 ARG N N 117.1 0.02 1 139 95 95 ARG H H 6.94 0.02 1 140 95 95 ARG N N 117.8 0.02 1 141 96 96 PHE H H 8.58 0.02 1 142 96 96 PHE N N 123 0.02 1 143 97 97 LEU H H 7.89 0.02 1 144 97 97 LEU N N 118 0.02 1 145 98 98 LEU H H 7.34 0.02 1 146 98 98 LEU N N 120.5 0.02 1 147 99 99 ALA H H 8.24 0.02 1 148 99 99 ALA N N 123.6 0.02 1 149 100 100 ALA H H 8.39 0.02 1 150 100 100 ALA N N 120.7 0.02 1 151 101 101 PHE H H 7.36 0.02 1 152 101 101 PHE N N 121.2 0.02 1 153 102 102 LEU H H 7.54 0.02 1 154 102 102 LEU N N 121.1 0.02 1 155 103 103 ALA H H 8.69 0.02 1 156 103 103 ALA N N 119.7 0.02 1 157 104 104 GLU H H 7.79 0.02 1 158 104 104 GLU N N 121 0.02 1 159 105 105 LEU H H 7.82 0.02 1 160 105 105 LEU N N 121.1 0.02 1 161 106 106 ALA H H 8.25 0.02 1 162 106 106 ALA N N 118 0.02 1 163 107 107 TYR H H 8.54 0.02 1 164 107 107 TYR N N 118.5 0.02 1 165 108 108 ARG H H 8.14 0.02 1 166 108 108 ARG N N 117.4 0.02 1 167 109 109 LEU H H 7.18 0.02 1 168 109 109 LEU N N 116.7 0.02 1 169 110 110 ALA H H 7.51 0.02 1 170 110 110 ALA N N 126.9 0.02 1 171 111 111 SER H H 8.08 0.02 1 172 111 111 SER N N 122 0.02 1 173 113 113 GLU H H 7.95 0.02 1 174 113 113 GLU N N 114.7 0.02 1 175 114 114 ALA H H 7.53 0.02 1 176 114 114 ALA N N 121.6 0.02 1 177 115 115 ALA H H 8.75 0.02 1 178 115 115 ALA N N 125.4 0.02 1 179 117 117 ARG H H 7.26 0.02 1 180 117 117 ARG N N 112.9 0.02 1 181 118 118 ILE H H 7.96 0.02 1 182 118 118 ILE N N 120.8 0.02 1 183 119 119 TYR H H 9.14 0.02 1 184 119 119 TYR N N 122.2 0.02 1 185 121 121 LEU H H 6.52 0.02 1 186 121 121 LEU N N 119.8 0.02 1 187 122 122 LEU H H 8.12 0.02 1 188 122 122 LEU N N 122.7 0.02 1 189 123 123 VAL H H 7.64 0.02 1 190 123 123 VAL N N 119.4 0.02 1 191 124 124 SER H H 8.02 0.02 1 192 124 124 SER N N 115.2 0.02 1 193 125 125 GLY H H 8.95 0.02 1 194 125 125 GLY N N 114 0.02 1 195 126 126 LEU H H 8.43 0.02 1 196 126 126 LEU N N 122.9 0.02 1 197 127 127 ARG H H 7.68 0.02 1 198 127 127 ARG N N 118.9 0.02 1 199 128 128 GLY H H 8.02 0.02 1 200 128 128 GLY N N 107.4 0.02 1 201 129 129 ILE H H 8.82 0.02 1 202 129 129 ILE N N 127 0.02 1 203 130 130 ALA H H 7.84 0.02 1 204 130 130 ALA N N 120.6 0.02 1 205 131 131 LYS H H 7.17 0.02 1 206 131 131 LYS N N 114.7 0.02 1 207 132 132 HIS H H 9.03 0.02 1 208 132 132 HIS N N 123.6 0.02 1 209 133 133 GLU H H 8.4 0.02 1 210 133 133 GLU N N 128.2 0.02 1 211 139 139 LEU H H 6.82 0.02 1 212 139 139 LEU N N 119 0.02 1 213 140 140 VAL H H 8.5 0.02 1 214 140 140 VAL N N 121 0.02 1 215 141 141 TRP H H 7.99 0.02 1 216 141 141 TRP N N 120.6 0.02 1 217 142 142 ALA H H 8.85 0.02 1 218 142 142 ALA N N 120.3 0.02 1 219 143 143 GLY H H 9.12 0.02 1 220 143 143 GLY N N 107.8 0.02 1 221 144 144 TRP H H 7.75 0.02 1 222 144 144 TRP N N 121.7 0.02 1 223 145 145 ARG H H 7.57 0.02 1 224 145 145 ARG N N 119.1 0.02 1 225 146 146 VAL H H 9.05 0.02 1 226 146 146 VAL N N 126.5 0.02 1 227 147 147 ALA H H 7.86 0.02 1 228 147 147 ALA N N 123.5 0.02 1 229 148 148 LYS H H 7.84 0.02 1 230 148 148 LYS N N 118.1 0.02 1 231 149 149 ALA H H 8.51 0.02 1 232 149 149 ALA N N 125.2 0.02 1 233 150 150 GLY H H 8.35 0.02 1 234 150 150 GLY N N 130 0.02 1 235 151 151 GLY H H 7.53 0.02 1 236 151 151 GLY N N 107.5 0.02 1 237 152 152 ILE H H 7.93 0.02 1 238 152 152 ILE N N 114.2 0.02 1 239 153 153 GLY H H 9.01 0.02 1 240 153 153 GLY N N 114.1 0.02 1 241 155 155 ASN H H 8.68 0.02 1 242 155 155 ASN N N 121.6 0.02 1 243 156 156 LEU H H 8.4 0.02 1 244 156 156 LEU N N 125.6 0.02 1 245 157 157 GLU H H 7.77 0.02 1 246 157 157 GLU N N 120.3 0.02 1 247 158 158 GLY H H 8.19 0.02 1 248 158 158 GLY N N 110.5 0.02 1 249 159 159 GLU H H 8.08 0.02 1 250 159 159 GLU N N 119.1 0.02 1 251 160 160 GLY H H 7.97 0.02 1 252 160 160 GLY N N 110.4 0.02 1 253 161 161 LEU H H 7.91 0.02 1 254 161 161 LEU N N 117.1 0.02 1 255 162 162 ARG H H 7.97 0.02 1 256 162 162 ARG N N 120.4 0.02 1 257 163 163 LEU H H 8.37 0.02 1 258 163 163 LEU N N 124.2 0.02 1 259 164 164 LYS H H 8.72 0.02 1 260 164 164 LYS N N 130.7 0.02 1 261 165 165 ARG H H 10.2 0.02 1 262 165 165 ARG N N 130.8 0.02 1 263 166 166 GLY H H 9.53 0.02 1 264 166 166 GLY N N 132.1 0.02 1 265 167 167 ARG H H 8 0.02 1 266 167 167 ARG N N 121.4 0.02 1 267 168 168 LEU H H 8.31 0.02 1 268 168 168 LEU N N 124.2 0.02 1 269 169 169 GLY H H 8.87 0.02 1 270 169 169 GLY N N 113.4 0.02 1 271 170 170 GLU H H 8.58 0.02 1 272 170 170 GLU N N 120.6 0.02 1 273 171 171 GLU H H 7.36 0.02 1 274 171 171 GLU N N 118.4 0.02 1 275 172 172 GLY H H 8.64 0.02 1 276 172 172 GLY N N 109.6 0.02 1 277 173 173 VAL H H 7.97 0.02 1 278 173 173 VAL N N 123.8 0.02 1 279 174 174 TYR H H 8.89 0.02 1 280 174 174 TYR N N 129.2 0.02 1 281 176 176 GLY H H 6.64 0.02 1 282 176 176 GLY N N 131.9 0.02 1 283 177 177 ARG H H 9.15 0.02 1 284 177 177 ARG N N 124.5 0.02 1 285 178 178 GLU H H 9.65 0.02 1 286 178 178 GLU N N 118 0.02 1 287 179 179 GLY H H 7.03 0.02 1 288 179 179 GLY N N 109.1 0.02 1 289 180 180 VAL H H 8.13 0.02 1 290 180 180 VAL N N 124.9 0.02 1 291 181 181 GLU H H 7.99 0.02 1 292 181 181 GLU N N 119.3 0.02 1 293 182 182 ALA H H 7.5 0.02 1 294 182 182 ALA N N 122.2 0.02 1 295 183 183 LEU H H 8.2 0.02 1 296 183 183 LEU N N 124.8 0.02 1 297 184 184 LYS H H 8.27 0.02 1 298 184 184 LYS N N 120 0.02 1 299 185 185 ALA H H 7.44 0.02 1 300 185 185 ALA N N 121.3 0.02 1 301 186 186 THR H H 7.73 0.02 1 302 186 186 THR N N 115.4 0.02 1 303 187 187 LEU H H 7.48 0.02 1 304 187 187 LEU N N 117.9 0.02 1 305 188 188 ARG H H 7.75 0.02 1 306 188 188 ARG N N 118.8 0.02 1 307 189 189 LEU H H 7.77 0.02 1 308 189 189 LEU N N 122.4 0.02 1 309 191 191 GLY H H 8.68 0.02 1 310 191 191 GLY N N 111.3 0.02 1 311 192 192 ALA H H 8.73 0.02 1 312 192 192 ALA N N 126.3 0.02 1 313 193 193 GLN H H 7.83 0.02 1 314 193 193 GLN N N 117.9 0.02 1 315 194 194 ALA H H 8.46 0.02 1 316 194 194 ALA N N 121.8 0.02 1 317 195 195 LEU H H 7.36 0.02 1 318 195 195 LEU N N 118.5 0.02 1 319 197 197 HIS H H 7.19 0.02 1 320 197 197 HIS N N 116.5 0.02 1 321 198 198 LEU H H 7.63 0.02 1 322 198 198 LEU N N 120.5 0.02 1 323 199 199 GLU H H 7.19 0.02 1 324 199 199 GLU N N 121.6 0.02 1 325 200 200 GLY H H 8.43 0.02 1 326 200 200 GLY N N 113.4 0.02 1 327 201 201 ALA H H 7.56 0.02 1 328 201 201 ALA N N 124.8 0.02 1 329 204 204 ASN H H 8.74 0.02 1 330 204 204 ASN N N 118.2 0.02 1 331 205 205 ARG H H 7.56 0.02 1 332 205 205 ARG N N 120.3 0.02 1 333 206 206 LEU H H 7.76 0.02 1 334 206 206 LEU N N 119.1 0.02 1 335 207 207 PHE H H 8.67 0.02 1 336 207 207 PHE N N 123.8 0.02 1 337 208 208 LEU H H 8.4 0.02 1 338 208 208 LEU N N 123 0.02 1 339 209 209 ALA H H 8.45 0.02 1 340 209 209 ALA N N 121.2 0.02 1 341 210 210 LEU H H 7.54 0.02 1 342 210 210 LEU N N 123.4 0.02 1 343 211 211 LYS H H 8.07 0.02 1 344 211 211 LYS N N 120.1 0.02 1 345 212 212 ALA H H 7.75 0.02 1 346 212 212 ALA N N 121.2 0.02 1 347 213 213 HIS H H 8.67 0.02 1 348 213 213 HIS N N 121.3 0.02 1 349 214 214 ALA H H 8.8 0.02 1 350 214 214 ALA N N 121.4 0.02 1 351 215 215 GLU H H 8.04 0.02 1 352 215 215 GLU N N 117.8 0.02 1 353 216 216 GLU H H 7.9 0.02 1 354 216 216 GLU N N 123.3 0.02 1 355 217 217 ALA H H 7.19 0.02 1 356 217 217 ALA N N 120.1 0.02 1 357 218 218 LEU H H 8.51 0.02 1 358 218 218 LEU N N 116.4 0.02 1 359 219 219 GLY H H 7.78 0.02 1 360 219 219 GLY N N 113 0.02 1 361 221 221 LEU H H 9.09 0.02 1 362 221 221 LEU N N 128.8 0.02 1 363 222 222 ARG H H 9.35 0.02 1 364 222 222 ARG N N 128.6 0.02 1 365 223 223 SER H H 8.84 0.02 1 366 223 223 SER N N 116.7 0.02 1 367 224 224 ALA H H 7.51 0.02 1 368 224 224 ALA N N 125.5 0.02 1 369 225 225 GLU H H 7.64 0.02 1 370 225 225 GLU N N 119.2 0.02 1 371 226 226 ALA H H 7.52 0.02 1 372 226 226 ALA N N 121.6 0.02 1 373 227 227 ILE H H 7.14 0.02 1 374 227 227 ILE N N 118.6 0.02 1 375 228 228 GLY H H 8 0.02 1 376 228 228 GLY N N 114.1 0.02 1 377 229 229 VAL H H 7.41 0.02 1 378 229 229 VAL N N 124.6 0.02 1 stop_ save_