data_5191 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Backbone NMR assignments of Ribosome Recycling Factors from Thermotoga maritima ; _BMRB_accession_number 5191 _BMRB_flat_file_name bmr5191.str _Entry_type original _Submission_date 2001-10-30 _Accession_date 2001-10-30 _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 Yoshida Takuya . . 2 Kijima Hiroyuki . . 3 Oka Shinichiro . . 4 Uchiyama Susumu . . 5 Nakano Hiroaki . . 6 Ohkubo Tadayasu . . 7 Kobayashi Yuji . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 167 "13C chemical shifts" 341 "15N chemical shifts" 167 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2002-05-07 original author . stop_ _Original_release_date 2002-05-07 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; Letter to the Editor: Backbone NMR Assignments of Ribosome Recycling Factors from Escherichia coli and Thermotoga maritima ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code 21880670 _PubMed_ID 11883785 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Yoshida Takuya . . 2 Kijima Hiroyuki . . 3 Oka Shinichiro . . 4 Uchiyama Susumu . . 5 Nakano Hiroaki . . 6 Ohkubo Tadayasu . . 7 Kobayashi Yuji . . stop_ _Journal_abbreviation 'J. Biomol. NMR' _Journal_volume 22 _Journal_issue 2 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 195 _Page_last 196 _Year 2002 _Details . save_ ################################## # Molecular system description # ################################## save_system_RRF _Saveframe_category molecular_system _Mol_system_name 'ribosome recycling factor' _Abbreviation_common RRF _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'ribosome recycling factor' $RRF 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_RRF _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'ribosome recycling factor' _Abbreviation_common RRF _Molecular_mass . _Mol_thiol_state 'not present' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 185 _Mol_residue_sequence ; MVNPFIKEAKEKMKRTLEKI EDELRKMRTGKPSPAILEEI KVDYYGVPTPVNQLATISIS EERTLVIKPWDKSVLSLIEK AINASDLGLNPINDGNVIRL VFPSPTTEQREKWVKKAKEI VEEGKIAIRNIRREILKKIK EDQKEGLIPEDDAKRLENEI QKLTDEFIEKLDEVFEIKKE EIMEF ; loop_ _Residue_seq_code _Residue_label 1 MET 2 VAL 3 ASN 4 PRO 5 PHE 6 ILE 7 LYS 8 GLU 9 ALA 10 LYS 11 GLU 12 LYS 13 MET 14 LYS 15 ARG 16 THR 17 LEU 18 GLU 19 LYS 20 ILE 21 GLU 22 ASP 23 GLU 24 LEU 25 ARG 26 LYS 27 MET 28 ARG 29 THR 30 GLY 31 LYS 32 PRO 33 SER 34 PRO 35 ALA 36 ILE 37 LEU 38 GLU 39 GLU 40 ILE 41 LYS 42 VAL 43 ASP 44 TYR 45 TYR 46 GLY 47 VAL 48 PRO 49 THR 50 PRO 51 VAL 52 ASN 53 GLN 54 LEU 55 ALA 56 THR 57 ILE 58 SER 59 ILE 60 SER 61 GLU 62 GLU 63 ARG 64 THR 65 LEU 66 VAL 67 ILE 68 LYS 69 PRO 70 TRP 71 ASP 72 LYS 73 SER 74 VAL 75 LEU 76 SER 77 LEU 78 ILE 79 GLU 80 LYS 81 ALA 82 ILE 83 ASN 84 ALA 85 SER 86 ASP 87 LEU 88 GLY 89 LEU 90 ASN 91 PRO 92 ILE 93 ASN 94 ASP 95 GLY 96 ASN 97 VAL 98 ILE 99 ARG 100 LEU 101 VAL 102 PHE 103 PRO 104 SER 105 PRO 106 THR 107 THR 108 GLU 109 GLN 110 ARG 111 GLU 112 LYS 113 TRP 114 VAL 115 LYS 116 LYS 117 ALA 118 LYS 119 GLU 120 ILE 121 VAL 122 GLU 123 GLU 124 GLY 125 LYS 126 ILE 127 ALA 128 ILE 129 ARG 130 ASN 131 ILE 132 ARG 133 ARG 134 GLU 135 ILE 136 LEU 137 LYS 138 LYS 139 ILE 140 LYS 141 GLU 142 ASP 143 GLN 144 LYS 145 GLU 146 GLY 147 LEU 148 ILE 149 PRO 150 GLU 151 ASP 152 ASP 153 ALA 154 LYS 155 ARG 156 LEU 157 GLU 158 ASN 159 GLU 160 ILE 161 GLN 162 LYS 163 LEU 164 THR 165 ASP 166 GLU 167 PHE 168 ILE 169 GLU 170 LYS 171 LEU 172 ASP 173 GLU 174 VAL 175 PHE 176 GLU 177 ILE 178 LYS 179 LYS 180 GLU 181 GLU 182 ILE 183 MET 184 GLU 185 PHE stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-01-28 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 1DD5 "Crystal Structure Of Thermotoga Maritima Ribosome Recycling Factor, Rrf" 100.00 185 100.00 100.00 1.31e-123 PDB 1T1M "Binding Position Of Ribosome Recycling Factor (Rrf) On The E. Coli 70s Ribosome" 100.00 185 100.00 100.00 1.31e-123 GB AAD36470 "ribosome recycling factor [Thermotoga maritima MSB8]" 100.00 185 100.00 100.00 1.31e-123 GB ACB09774 "ribosome recycling factor [Thermotoga sp. RQ2]" 100.00 185 100.00 100.00 1.31e-123 GB AGL50330 "Ribosome recycling factor [Thermotoga maritima MSB8]" 100.00 185 100.00 100.00 1.31e-123 GB AHD18705 "ribosome recycling factor [Thermotoga maritima MSB8]" 100.00 185 100.00 100.00 1.31e-123 GB AIY86963 "ribosome recycling factor [Thermotoga sp. 2812B]" 100.00 185 99.46 100.00 2.41e-123 REF NP_229200 "ribosome recycling factor [Thermotoga maritima MSB8]" 100.00 185 100.00 100.00 1.31e-123 REF WP_004081616 "MULTISPECIES: ribosome recycling factor [Thermotoga]" 100.00 185 100.00 100.00 1.31e-123 REF WP_008195141 "MULTISPECIES: ribosome recycling factor [Thermotoga]" 100.00 185 99.46 100.00 2.41e-123 REF WP_029682954 "ribosome recycling factor [Thermotoga sp. A7A]" 100.00 185 99.46 100.00 1.54e-123 REF WP_038034460 "MULTISPECIES: ribosome recycling factor [Thermotoga]" 100.00 185 98.92 99.46 1.92e-122 SP B1LBS6 "RecName: Full=Ribosome-recycling factor; Short=RRF; AltName: Full=Ribosome-releasing factor [Thermotoga sp. RQ2]" 100.00 185 100.00 100.00 1.31e-123 SP Q9X1B9 "RecName: Full=Ribosome-recycling factor; Short=RRF; AltName: Full=Ribosome-releasing factor [Thermotoga maritima MSB8]" 100.00 185 100.00 100.00 1.31e-123 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $RRF 'Thermotoga maritima' 2336 Eubacteria . Thermotoga maritima 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 $RRF 'recombinant technology' . . . . . 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 $RRF 0.5 mM . stop_ save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model INOVA _Field_strength 600 _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 7.4 0.1 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 H 1 'methyl protons' ppm 0.0 internal direct . . . 1.0 DSS N 15 'methyl protons' ppm 0.0 . indirect . . . 0.101329118 DSS C 13 'methyl protons' ppm 0.0 . indirect . . . 0.251449530 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_shift_set_1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $Ex-cond_1 _Chem_shift_reference_set_label $chemical_shift_reference _Mol_system_component_name 'ribosome recycling factor' _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 . 4 PRO C C 178.79 0.05 1 2 . 4 PRO CA C 65.33 0.05 1 3 . 5 PHE H H 8.42 0.01 1 4 . 5 PHE C C 177.91 0.05 1 5 . 5 PHE CA C 61.30 0.05 1 6 . 5 PHE N N 117.33 0.05 1 7 . 6 ILE H H 7.54 0.01 1 8 . 6 ILE C C 177.41 0.05 1 9 . 6 ILE CA C 63.22 0.05 1 10 . 6 ILE N N 118.95 0.05 1 11 . 7 LYS H H 7.89 0.01 1 12 . 7 LYS C C 178.47 0.05 1 13 . 7 LYS CA C 60.08 0.05 1 14 . 7 LYS N N 120.17 0.05 1 15 . 8 GLU H H 7.96 0.01 1 16 . 8 GLU C C 178.27 0.05 1 17 . 8 GLU CA C 59.27 0.05 1 18 . 8 GLU N N 118.50 0.05 1 19 . 9 ALA H H 8.03 0.01 1 20 . 9 ALA C C 178.66 0.05 1 21 . 9 ALA CA C 55.64 0.05 1 22 . 9 ALA N N 120.17 0.05 1 23 . 10 LYS H H 8.64 0.01 1 24 . 10 LYS C C 178.53 0.05 1 25 . 10 LYS CA C 60.88 0.05 1 26 . 10 LYS N N 116.65 0.05 1 27 . 11 GLU H H 8.19 0.01 1 28 . 11 GLU C C 179.63 0.05 1 29 . 11 GLU CA C 59.59 0.05 1 30 . 11 GLU N N 117.96 0.05 1 31 . 12 LYS H H 8.21 0.01 1 32 . 12 LYS C C 180.50 0.05 1 33 . 12 LYS CA C 60.27 0.05 1 34 . 12 LYS N N 118.37 0.05 1 35 . 13 MET H H 8.69 0.01 1 36 . 13 MET C C 176.93 0.05 1 37 . 13 MET CA C 61.02 0.05 1 38 . 13 MET N N 121.55 0.05 1 39 . 14 LYS H H 8.31 0.01 1 40 . 14 LYS C C 178.82 0.05 1 41 . 14 LYS CA C 61.02 0.05 1 42 . 14 LYS N N 120.65 0.05 1 43 . 15 ARG H H 7.87 0.01 1 44 . 15 ARG C C 179.38 0.05 1 45 . 15 ARG CA C 59.07 0.05 1 46 . 15 ARG N N 117.88 0.05 1 47 . 16 THR H H 7.56 0.01 1 48 . 16 THR C C 175.48 0.05 1 49 . 16 THR CA C 67.64 0.05 1 50 . 16 THR N N 117.41 0.05 1 51 . 17 LEU H H 8.14 0.01 1 52 . 17 LEU C C 177.81 0.05 1 53 . 17 LEU CA C 58.90 0.05 1 54 . 17 LEU N N 122.84 0.05 1 55 . 18 GLU H H 8.46 0.01 1 56 . 18 GLU C C 179.44 0.05 1 57 . 18 GLU CA C 59.46 0.05 1 58 . 18 GLU N N 117.55 0.05 1 59 . 19 LYS H H 7.84 0.01 1 60 . 19 LYS C C 178.93 0.05 1 61 . 19 LYS CA C 59.35 0.05 1 62 . 19 LYS N N 120.78 0.05 1 63 . 20 ILE H H 8.02 0.01 1 64 . 20 ILE C C 178.22 0.05 1 65 . 20 ILE CA C 63.17 0.05 1 66 . 20 ILE N N 121.26 0.05 1 67 . 21 GLU H H 8.84 0.01 1 68 . 21 GLU C C 179.87 0.05 1 69 . 21 GLU CA C 61.10 0.05 1 70 . 21 GLU N N 119.11 0.05 1 71 . 22 ASP H H 8.13 0.01 1 72 . 22 ASP C C 177.86 0.05 1 73 . 22 ASP CA C 57.79 0.05 1 74 . 22 ASP N N 120.31 0.05 1 75 . 23 GLU H H 8.21 0.01 1 76 . 23 GLU C C 180.47 0.05 1 77 . 23 GLU CA C 59.56 0.05 1 78 . 23 GLU N N 119.17 0.05 1 79 . 24 LEU H H 8.45 0.01 1 80 . 24 LEU C C 179.30 0.05 1 81 . 24 LEU CA C 57.72 0.05 1 82 . 24 LEU N N 117.81 0.05 1 83 . 25 ARG H H 8.04 0.01 1 84 . 25 ARG C C 178.07 0.05 1 85 . 25 ARG CA C 58.88 0.05 1 86 . 25 ARG N N 120.33 0.05 1 87 . 26 LYS H H 7.26 0.01 1 88 . 26 LYS C C 175.85 0.05 1 89 . 26 LYS CA C 57.11 0.05 1 90 . 26 LYS N N 115.56 0.05 1 91 . 27 MET H H 7.03 0.01 1 92 . 27 MET C C 175.36 0.05 1 93 . 27 MET CA C 56.32 0.05 1 94 . 27 MET N N 118.81 0.05 1 95 . 28 ARG H H 8.27 0.01 1 96 . 28 ARG C C 175.09 0.05 1 97 . 28 ARG CA C 56.64 0.05 1 98 . 28 ARG N N 127.68 0.05 1 99 . 29 THR H H 8.38 0.01 1 100 . 29 THR C C 174.40 0.05 1 101 . 29 THR CA C 59.74 0.05 1 102 . 29 THR N N 116.26 0.05 1 103 . 30 GLY H H 8.21 0.01 1 104 . 30 GLY C C 173.09 0.05 1 105 . 30 GLY CA C 46.01 0.05 1 106 . 30 GLY N N 108.79 0.05 1 107 . 31 LYS H H 7.65 0.01 1 108 . 31 LYS CA C 53.26 0.05 1 109 . 31 LYS N N 121.03 0.05 1 110 . 34 PRO C C 178.78 0.05 1 111 . 34 PRO CA C 64.66 0.05 1 112 . 35 ALA H H 7.83 0.01 1 113 . 35 ALA C C 179.43 0.05 1 114 . 35 ALA CA C 54.56 0.05 1 115 . 35 ALA N N 119.77 0.05 1 116 . 36 ILE H H 7.22 0.01 1 117 . 36 ILE C C 176.41 0.05 1 118 . 36 ILE CA C 63.15 0.05 1 119 . 36 ILE N N 112.08 0.05 1 120 . 37 LEU H H 7.39 0.01 1 121 . 37 LEU C C 177.83 0.05 1 122 . 37 LEU CA C 54.23 0.05 1 123 . 37 LEU N N 116.63 0.05 1 124 . 38 GLU H H 7.42 0.01 1 125 . 38 GLU C C 177.27 0.05 1 126 . 38 GLU CA C 59.74 0.05 1 127 . 38 GLU N N 119.02 0.05 1 128 . 39 GLU H H 7.98 0.01 1 129 . 39 GLU C C 176.31 0.05 1 130 . 39 GLU CA C 55.78 0.05 1 131 . 39 GLU N N 113.42 0.05 1 132 . 40 ILE H H 7.37 0.01 1 133 . 40 ILE C C 174.54 0.05 1 134 . 40 ILE CA C 60.52 0.05 1 135 . 40 ILE N N 121.20 0.05 1 136 . 41 LYS H H 8.35 0.01 1 137 . 41 LYS C C 175.30 0.05 1 138 . 41 LYS CA C 54.39 0.05 1 139 . 41 LYS N N 126.10 0.05 1 140 . 42 VAL H H 8.66 0.01 1 141 . 42 VAL C C 175.03 0.05 1 142 . 42 VAL CA C 59.33 0.05 1 143 . 42 VAL N N 118.08 0.05 1 144 . 43 ASP H H 8.51 0.01 1 145 . 43 ASP C C 174.07 0.05 1 146 . 43 ASP CA C 54.39 0.05 1 147 . 43 ASP N N 125.55 0.05 1 148 . 44 TYR H H 7.98 0.01 1 149 . 44 TYR C C 174.60 0.05 1 150 . 44 TYR CA C 56.33 0.05 1 151 . 44 TYR N N 128.26 0.05 1 152 . 45 TYR H H 8.40 0.01 1 153 . 45 TYR C C 175.77 0.05 1 154 . 45 TYR CA C 59.49 0.05 1 155 . 45 TYR N N 124.34 0.05 1 156 . 46 GLY H H 7.90 0.01 1 157 . 46 GLY C C 174.35 0.05 1 158 . 46 GLY CA C 45.30 0.05 1 159 . 46 GLY N N 97.94 0.05 1 160 . 47 VAL H H 7.46 0.01 1 161 . 47 VAL CA C 59.31 0.05 1 162 . 47 VAL N N 121.27 0.05 1 163 . 50 PRO C C 178.17 0.05 1 164 . 50 PRO CA C 62.71 0.05 1 165 . 51 VAL H H 8.37 0.01 1 166 . 51 VAL C C 176.78 0.05 1 167 . 51 VAL CA C 66.59 0.05 1 168 . 51 VAL N N 121.86 0.05 1 169 . 52 ASN H H 8.45 0.01 1 170 . 52 ASN C C 175.76 0.05 1 171 . 52 ASN CA C 54.67 0.05 1 172 . 52 ASN N N 113.97 0.05 1 173 . 53 GLN H H 7.67 0.01 1 174 . 53 GLN C C 175.94 0.05 1 175 . 53 GLN CA C 56.12 0.05 1 176 . 53 GLN N N 116.22 0.05 1 177 . 54 LEU H H 7.50 0.01 1 178 . 54 LEU C C 174.91 0.05 1 179 . 54 LEU CA C 53.89 0.05 1 180 . 54 LEU N N 117.03 0.05 1 181 . 55 ALA H H 7.25 0.01 1 182 . 55 ALA C C 175.03 0.05 1 183 . 55 ALA CA C 51.00 0.05 1 184 . 55 ALA N N 120.21 0.05 1 185 . 56 THR H H 7.67 0.01 1 186 . 56 THR C C 174.13 0.05 1 187 . 56 THR CA C 61.55 0.05 1 188 . 56 THR N N 113.18 0.05 1 189 . 57 ILE H H 8.82 0.01 1 190 . 57 ILE C C 175.03 0.05 1 191 . 57 ILE CA C 60.11 0.05 1 192 . 57 ILE N N 127.49 0.05 1 193 . 58 SER H H 8.91 0.01 1 194 . 58 SER C C 172.36 0.05 1 195 . 58 SER CA C 56.64 0.05 1 196 . 58 SER N N 121.43 0.05 1 197 . 59 ILE H H 8.53 0.01 1 198 . 59 ILE C C 176.22 0.05 1 199 . 59 ILE CA C 60.57 0.05 1 200 . 59 ILE N N 122.35 0.05 1 201 . 60 SER H H 8.77 0.01 1 202 . 60 SER C C 173.82 0.05 1 203 . 60 SER CA C 57.12 0.05 1 204 . 60 SER N N 122.56 0.05 1 205 . 61 GLU H H 8.65 0.01 1 206 . 61 GLU C C 176.29 0.05 1 207 . 61 GLU CA C 56.95 0.05 1 208 . 61 GLU N N 121.35 0.05 1 209 . 62 GLU H H 8.54 0.01 1 210 . 62 GLU C C 177.48 0.05 1 211 . 62 GLU CA C 59.50 0.05 1 212 . 62 GLU N N 115.80 0.05 1 213 . 63 ARG H H 8.57 0.01 1 214 . 63 ARG C C 174.29 0.05 1 215 . 63 ARG CA C 56.47 0.05 1 216 . 63 ARG N N 116.58 0.05 1 217 . 64 THR H H 7.63 0.01 1 218 . 64 THR C C 173.53 0.05 1 219 . 64 THR CA C 61.83 0.05 1 220 . 64 THR N N 113.84 0.05 1 221 . 65 LEU H H 9.08 0.01 1 222 . 65 LEU C C 175.07 0.05 1 223 . 65 LEU CA C 53.53 0.05 1 224 . 65 LEU N N 125.86 0.05 1 225 . 66 VAL H H 9.17 0.01 1 226 . 66 VAL C C 175.01 0.05 1 227 . 66 VAL CA C 61.80 0.05 1 228 . 66 VAL N N 124.05 0.05 1 229 . 67 ILE H H 9.31 0.01 1 230 . 67 ILE C C 174.13 0.05 1 231 . 67 ILE CA C 60.58 0.05 1 232 . 67 ILE N N 127.51 0.05 1 233 . 68 LYS H H 8.74 0.01 1 234 . 68 LYS CA C 52.59 0.05 1 235 . 68 LYS N N 127.85 0.05 1 236 . 69 PRO C C 175.84 0.05 1 237 . 69 PRO CA C 61.91 0.05 1 238 . 70 TRP H H 7.35 0.01 1 239 . 70 TRP C C 176.32 0.05 1 240 . 70 TRP CA C 58.45 0.05 1 241 . 70 TRP N N 121.18 0.05 1 242 . 71 ASP H H 8.34 0.01 1 243 . 71 ASP C C 176.79 0.05 1 244 . 71 ASP CA C 52.10 0.05 1 245 . 71 ASP N N 120.19 0.05 1 246 . 72 LYS H H 8.87 0.01 1 247 . 72 LYS C C 178.68 0.05 1 248 . 72 LYS CA C 59.28 0.05 1 249 . 72 LYS N N 123.78 0.05 1 250 . 73 SER H H 8.79 0.01 1 251 . 73 SER C C 176.03 0.05 1 252 . 73 SER CA C 61.50 0.05 1 253 . 73 SER N N 116.22 0.05 1 254 . 74 VAL H H 7.64 0.01 1 255 . 74 VAL C C 177.22 0.05 1 256 . 74 VAL CA C 61.85 0.05 1 257 . 74 VAL N N 115.59 0.05 1 258 . 75 LEU H H 7.60 0.01 1 259 . 75 LEU C C 178.48 0.05 1 260 . 75 LEU CA C 59.61 0.05 1 261 . 75 LEU N N 123.59 0.05 1 262 . 76 SER H H 8.48 0.01 1 263 . 76 SER C C 176.68 0.05 1 264 . 76 SER CA C 61.49 0.05 1 265 . 76 SER N N 111.64 0.05 1 266 . 77 LEU H H 7.09 0.01 1 267 . 77 LEU C C 180.30 0.05 1 268 . 77 LEU CA C 57.46 0.05 1 269 . 77 LEU N N 120.64 0.05 1 270 . 78 ILE H H 8.11 0.01 1 271 . 78 ILE C C 176.91 0.05 1 272 . 78 ILE CA C 65.84 0.05 1 273 . 78 ILE N N 120.49 0.05 1 274 . 79 GLU H H 8.17 0.01 1 275 . 79 GLU C C 177.55 0.05 1 276 . 79 GLU CA C 60.87 0.05 1 277 . 79 GLU N N 120.65 0.05 1 278 . 80 LYS H H 7.86 0.01 1 279 . 80 LYS C C 178.99 0.05 1 280 . 80 LYS CA C 59.75 0.05 1 281 . 80 LYS N N 117.04 0.05 1 282 . 81 ALA H H 7.79 0.01 1 283 . 81 ALA C C 180.93 0.05 1 284 . 81 ALA CA C 54.89 0.05 1 285 . 81 ALA N N 121.59 0.05 1 286 . 82 ILE H H 8.32 0.01 1 287 . 82 ILE C C 179.97 0.05 1 288 . 82 ILE CA C 65.13 0.05 1 289 . 82 ILE N N 117.59 0.05 1 290 . 83 ASN H H 8.42 0.01 1 291 . 83 ASN C C 176.20 0.05 1 292 . 83 ASN CA C 56.04 0.05 1 293 . 83 ASN N N 121.31 0.05 1 294 . 84 ALA H H 7.69 0.01 1 295 . 84 ALA C C 177.45 0.05 1 296 . 84 ALA CA C 52.57 0.05 1 297 . 84 ALA N N 119.99 0.05 1 298 . 85 SER H H 7.49 0.01 1 299 . 85 SER C C 173.48 0.05 1 300 . 85 SER CA C 59.02 0.05 1 301 . 85 SER N N 115.45 0.05 1 302 . 86 ASP H H 8.35 0.01 1 303 . 86 ASP C C 177.31 0.05 1 304 . 86 ASP CA C 53.48 0.05 1 305 . 86 ASP N N 118.52 0.05 1 306 . 87 LEU H H 8.13 0.01 1 307 . 87 LEU C C 178.52 0.05 1 308 . 87 LEU CA C 57.25 0.05 1 309 . 87 LEU N N 118.57 0.05 1 310 . 88 GLY H H 8.60 0.01 1 311 . 88 GLY C C 174.13 0.05 1 312 . 88 GLY CA C 46.40 0.05 1 313 . 88 GLY N N 106.52 0.05 1 314 . 89 LEU H H 6.92 0.01 1 315 . 89 LEU C C 175.18 0.05 1 316 . 89 LEU CA C 52.76 0.05 1 317 . 89 LEU N N 117.26 0.05 1 318 . 90 ASN H H 8.49 0.01 1 319 . 90 ASN CA C 50.45 0.05 1 320 . 90 ASN N N 119.89 0.05 1 321 . 91 PRO C C 175.59 0.05 1 322 . 91 PRO CA C 62.51 0.05 1 323 . 92 ILE H H 8.61 0.01 1 324 . 92 ILE C C 175.26 0.05 1 325 . 92 ILE CA C 60.78 0.05 1 326 . 92 ILE N N 123.98 0.05 1 327 . 93 ASN H H 9.00 0.01 1 328 . 93 ASN C C 175.61 0.05 1 329 . 93 ASN CA C 51.57 0.05 1 330 . 93 ASN N N 128.28 0.05 1 331 . 94 ASP H H 8.42 0.01 1 332 . 94 ASP C C 177.70 0.05 1 333 . 94 ASP CA C 52.90 0.05 1 334 . 94 ASP N N 126.02 0.05 1 335 . 95 GLY H H 8.97 0.01 1 336 . 95 GLY C C 173.09 0.05 1 337 . 95 GLY CA C 45.43 0.05 1 338 . 95 GLY N N 110.05 0.05 1 339 . 96 ASN H H 8.96 0.01 1 340 . 96 ASN C C 174.10 0.05 1 341 . 96 ASN CA C 55.31 0.05 1 342 . 96 ASN N N 118.95 0.05 1 343 . 97 VAL H H 9.12 0.01 1 344 . 97 VAL C C 174.56 0.05 1 345 . 97 VAL CA C 58.96 0.05 1 346 . 97 VAL N N 112.49 0.05 1 347 . 98 ILE H H 8.17 0.01 1 348 . 98 ILE C C 175.34 0.05 1 349 . 98 ILE CA C 58.23 0.05 1 350 . 98 ILE N N 116.32 0.05 1 351 . 99 ARG H H 8.96 0.01 1 352 . 99 ARG C C 175.34 0.05 1 353 . 99 ARG CA C 54.63 0.05 1 354 . 99 ARG N N 125.61 0.05 1 355 . 100 LEU H H 9.10 0.01 1 356 . 100 LEU C C 174.10 0.05 1 357 . 100 LEU CA C 53.17 0.05 1 358 . 100 LEU N N 122.99 0.05 1 359 . 101 VAL H H 8.90 0.01 1 360 . 101 VAL C C 176.03 0.05 1 361 . 101 VAL CA C 62.18 0.05 1 362 . 101 VAL N N 125.93 0.05 1 363 . 102 PHE H H 9.11 0.01 1 364 . 102 PHE CA C 55.80 0.05 1 365 . 102 PHE N N 129.64 0.05 1 366 . 107 THR C C 176.17 0.05 1 367 . 107 THR CA C 67.03 0.05 1 368 . 108 GLU H H 8.47 0.01 1 369 . 108 GLU C C 178.98 0.05 1 370 . 108 GLU CA C 59.78 0.05 1 371 . 108 GLU N N 120.33 0.05 1 372 . 109 GLN H H 7.48 0.01 1 373 . 109 GLN C C 177.30 0.05 1 374 . 109 GLN CA C 58.52 0.05 1 375 . 109 GLN N N 119.57 0.05 1 376 . 110 ARG H H 7.83 0.01 1 377 . 110 ARG C C 178.36 0.05 1 378 . 110 ARG CA C 60.58 0.05 1 379 . 110 ARG N N 116.70 0.05 1 380 . 111 GLU H H 8.01 0.01 1 381 . 111 GLU C C 179.67 0.05 1 382 . 111 GLU CA C 59.78 0.05 1 383 . 111 GLU N N 116.60 0.05 1 384 . 112 LYS H H 7.65 0.01 1 385 . 112 LYS C C 180.13 0.05 1 386 . 112 LYS CA C 59.77 0.05 1 387 . 112 LYS N N 120.24 0.05 1 388 . 113 TRP H H 8.38 0.01 1 389 . 113 TRP C C 178.53 0.05 1 390 . 113 TRP CA C 58.83 0.05 1 391 . 113 TRP N N 122.12 0.05 1 392 . 114 VAL H H 8.79 0.01 1 393 . 114 VAL C C 177.62 0.05 1 394 . 114 VAL CA C 68.22 0.05 1 395 . 114 VAL N N 120.97 0.05 1 396 . 115 LYS H H 7.91 0.01 1 397 . 115 LYS C C 178.89 0.05 1 398 . 115 LYS CA C 59.74 0.05 1 399 . 115 LYS N N 119.33 0.05 1 400 . 116 LYS H H 8.04 0.01 1 401 . 116 LYS C C 178.15 0.05 1 402 . 116 LYS CA C 58.51 0.05 1 403 . 116 LYS N N 120.39 0.05 1 404 . 117 ALA H H 8.58 0.01 1 405 . 117 ALA C C 178.76 0.05 1 406 . 117 ALA CA C 55.34 0.05 1 407 . 117 ALA N N 121.19 0.05 1 408 . 118 LYS H H 8.64 0.01 1 409 . 118 LYS C C 178.18 0.05 1 410 . 118 LYS CA C 58.89 0.05 1 411 . 118 LYS N N 118.40 0.05 1 412 . 119 GLU H H 8.13 0.01 1 413 . 119 GLU C C 179.79 0.05 1 414 . 119 GLU CA C 59.81 0.05 1 415 . 119 GLU N N 119.78 0.05 1 416 . 120 ILE H H 8.24 0.01 1 417 . 120 ILE C C 179.21 0.05 1 418 . 120 ILE CA C 65.46 0.05 1 419 . 120 ILE N N 120.79 0.05 1 420 . 121 VAL H H 8.11 0.01 1 421 . 121 VAL C C 178.46 0.05 1 422 . 121 VAL CA C 67.74 0.05 1 423 . 121 VAL N N 119.15 0.05 1 424 . 122 GLU H H 9.08 0.01 1 425 . 122 GLU C C 180.07 0.05 1 426 . 122 GLU CA C 59.82 0.05 1 427 . 122 GLU N N 121.41 0.05 1 428 . 123 GLU H H 8.12 0.01 1 429 . 123 GLU C C 180.40 0.05 1 430 . 123 GLU CA C 59.78 0.05 1 431 . 123 GLU N N 120.53 0.05 1 432 . 124 GLY H H 8.03 0.01 1 433 . 124 GLY C C 174.83 0.05 1 434 . 124 GLY CA C 47.84 0.05 1 435 . 124 GLY N N 109.18 0.05 1 436 . 125 LYS H H 8.45 0.01 1 437 . 125 LYS C C 177.20 0.05 1 438 . 125 LYS CA C 60.91 0.05 1 439 . 125 LYS N N 122.16 0.05 1 440 . 126 ILE H H 7.85 0.01 1 441 . 126 ILE C C 178.32 0.05 1 442 . 126 ILE CA C 65.40 0.05 1 443 . 126 ILE N N 119.63 0.05 1 444 . 127 ALA H H 7.74 0.01 1 445 . 127 ALA C C 181.15 0.05 1 446 . 127 ALA CA C 55.63 0.05 1 447 . 127 ALA N N 122.53 0.05 1 448 . 128 ILE H H 8.35 0.01 1 449 . 128 ILE C C 178.26 0.05 1 450 . 128 ILE CA C 63.22 0.05 1 451 . 128 ILE N N 118.89 0.05 1 452 . 129 ARG H H 8.32 0.01 1 453 . 129 ARG C C 179.66 0.05 1 454 . 129 ARG CA C 60.62 0.05 1 455 . 129 ARG N N 118.94 0.05 1 456 . 130 ASN H H 8.69 0.01 1 457 . 130 ASN C C 177.71 0.05 1 458 . 130 ASN CA C 56.05 0.05 1 459 . 130 ASN N N 121.43 0.05 1 460 . 131 ILE H H 8.12 0.01 1 461 . 131 ILE C C 177.73 0.05 1 462 . 131 ILE CA C 65.52 0.05 1 463 . 131 ILE N N 123.91 0.05 1 464 . 132 ARG H H 7.78 0.01 1 465 . 132 ARG C C 177.09 0.05 1 466 . 132 ARG CA C 60.31 0.05 1 467 . 132 ARG N N 118.81 0.05 1 468 . 133 ARG H H 7.88 0.01 1 469 . 133 ARG C C 178.94 0.05 1 470 . 133 ARG CA C 59.96 0.05 1 471 . 133 ARG N N 117.10 0.05 1 472 . 134 GLU H H 8.19 0.01 1 473 . 134 GLU C C 179.37 0.05 1 474 . 134 GLU CA C 59.43 0.05 1 475 . 134 GLU N N 119.12 0.05 1 476 . 135 ILE H H 8.33 0.01 1 477 . 135 ILE C C 177.90 0.05 1 478 . 135 ILE CA C 63.68 0.05 1 479 . 135 ILE N N 120.48 0.05 1 480 . 136 LEU H H 8.55 0.01 1 481 . 136 LEU C C 179.36 0.05 1 482 . 136 LEU CA C 58.30 0.05 1 483 . 136 LEU N N 119.68 0.05 1 484 . 137 LYS H H 7.73 0.01 1 485 . 137 LYS C C 178.47 0.05 1 486 . 137 LYS CA C 59.83 0.05 1 487 . 137 LYS N N 118.92 0.05 1 488 . 138 LYS H H 7.29 0.01 1 489 . 138 LYS C C 178.74 0.05 1 490 . 138 LYS CA C 59.53 0.05 1 491 . 138 LYS N N 119.40 0.05 1 492 . 139 ILE H H 7.97 0.01 1 493 . 139 ILE C C 177.53 0.05 1 494 . 139 ILE CA C 65.70 0.05 1 495 . 139 ILE N N 119.78 0.05 1 496 . 140 LYS H H 7.99 0.01 1 497 . 140 LYS C C 179.92 0.05 1 498 . 140 LYS CA C 58.93 0.05 1 499 . 140 LYS N N 117.88 0.05 1 500 . 141 GLU H H 8.15 0.01 1 501 . 141 GLU C C 178.97 0.05 1 502 . 141 GLU CA C 59.54 0.05 1 503 . 141 GLU N N 121.15 0.05 1 504 . 142 ASP H H 8.23 0.01 1 505 . 142 ASP C C 179.68 0.05 1 506 . 142 ASP CA C 57.56 0.05 1 507 . 142 ASP N N 122.03 0.05 1 508 . 143 GLN H H 8.79 0.01 1 509 . 143 GLN C C 180.31 0.05 1 510 . 143 GLN CA C 59.53 0.05 1 511 . 143 GLN N N 122.75 0.05 1 512 . 144 LYS H H 8.31 0.01 1 513 . 144 LYS C C 178.49 0.05 1 514 . 144 LYS CA C 59.47 0.05 1 515 . 144 LYS N N 122.99 0.05 1 516 . 145 GLU H H 7.67 0.01 1 517 . 145 GLU C C 176.50 0.05 1 518 . 145 GLU CA C 56.30 0.05 1 519 . 145 GLU N N 116.25 0.05 1 520 . 146 GLY H H 7.89 0.01 1 521 . 146 GLY C C 175.35 0.05 1 522 . 146 GLY CA C 45.48 0.05 1 523 . 146 GLY N N 106.54 0.05 1 524 . 147 LEU H H 8.17 0.01 1 525 . 147 LEU C C 177.00 0.05 1 526 . 147 LEU CA C 56.15 0.05 1 527 . 147 LEU N N 118.82 0.05 1 528 . 148 ILE H H 6.78 0.01 1 529 . 148 ILE CA C 57.81 0.05 1 530 . 148 ILE N N 115.12 0.05 1 531 . 149 PRO C C 177.13 0.05 1 532 . 149 PRO CA C 62.59 0.05 1 533 . 150 GLU H H 8.89 0.01 1 534 . 150 GLU C C 178.07 0.05 1 535 . 150 GLU CA C 60.56 0.05 1 536 . 150 GLU N N 123.18 0.05 1 537 . 151 ASP H H 8.93 0.01 1 538 . 151 ASP C C 179.15 0.05 1 539 . 151 ASP CA C 57.48 0.05 1 540 . 151 ASP N N 116.65 0.05 1 541 . 152 ASP H H 7.22 0.01 1 542 . 152 ASP C C 177.93 0.05 1 543 . 152 ASP CA C 57.11 0.05 1 544 . 152 ASP N N 120.11 0.05 1 545 . 153 ALA H H 8.34 0.01 1 546 . 153 ALA C C 179.59 0.05 1 547 . 153 ALA CA C 55.91 0.05 1 548 . 153 ALA N N 122.94 0.05 1 549 . 154 LYS H H 7.99 0.01 1 550 . 154 LYS C C 179.19 0.05 1 551 . 154 LYS CA C 59.10 0.05 1 552 . 154 LYS N N 117.76 0.05 1 553 . 155 ARG H H 7.53 0.01 1 554 . 155 ARG C C 179.56 0.05 1 555 . 155 ARG CA C 59.86 0.05 1 556 . 155 ARG N N 120.13 0.05 1 557 . 156 LEU H H 8.45 0.01 1 558 . 156 LEU C C 178.94 0.05 1 559 . 156 LEU CA C 58.10 0.05 1 560 . 156 LEU N N 120.19 0.05 1 561 . 157 GLU H H 8.35 0.01 1 562 . 157 GLU C C 178.82 0.05 1 563 . 157 GLU CA C 60.26 0.05 1 564 . 157 GLU N N 119.19 0.05 1 565 . 158 ASN H H 7.87 0.01 1 566 . 158 ASN C C 178.07 0.05 1 567 . 158 ASN CA C 56.48 0.05 1 568 . 158 ASN N N 117.88 0.05 1 569 . 159 GLU H H 8.32 0.01 1 570 . 159 GLU C C 179.92 0.05 1 571 . 159 GLU CA C 59.78 0.05 1 572 . 159 GLU N N 120.98 0.05 1 573 . 160 ILE H H 8.67 0.01 1 574 . 160 ILE C C 179.30 0.05 1 575 . 160 ILE CA C 62.75 0.05 1 576 . 160 ILE N N 119.64 0.05 1 577 . 161 GLN H H 8.57 0.01 1 578 . 161 GLN C C 177.18 0.05 1 579 . 161 GLN CA C 59.64 0.05 1 580 . 161 GLN N N 125.46 0.05 1 581 . 162 LYS H H 7.94 0.01 1 582 . 162 LYS C C 179.54 0.05 1 583 . 162 LYS CA C 59.48 0.05 1 584 . 162 LYS N N 119.49 0.05 1 585 . 163 LEU H H 7.96 0.01 1 586 . 163 LEU C C 178.22 0.05 1 587 . 163 LEU CA C 58.09 0.05 1 588 . 163 LEU N N 119.96 0.05 1 589 . 164 THR H H 8.10 0.01 1 590 . 164 THR C C 175.92 0.05 1 591 . 164 THR CA C 67.92 0.05 1 592 . 164 THR N N 115.76 0.05 1 593 . 165 ASP H H 8.23 0.01 1 594 . 165 ASP C C 179.10 0.05 1 595 . 165 ASP CA C 57.93 0.05 1 596 . 165 ASP N N 120.78 0.05 1 597 . 166 GLU H H 8.18 0.01 1 598 . 166 GLU C C 179.80 0.05 1 599 . 166 GLU CA C 59.60 0.05 1 600 . 166 GLU N N 120.92 0.05 1 601 . 167 PHE H H 8.50 0.01 1 602 . 167 PHE C C 178.31 0.05 1 603 . 167 PHE CA C 63.95 0.05 1 604 . 167 PHE N N 118.78 0.05 1 605 . 168 ILE H H 8.70 0.01 1 606 . 168 ILE C C 177.61 0.05 1 607 . 168 ILE CA C 65.02 0.05 1 608 . 168 ILE N N 121.31 0.05 1 609 . 169 GLU H H 7.99 0.01 1 610 . 169 GLU C C 180.04 0.05 1 611 . 169 GLU CA C 59.73 0.05 1 612 . 169 GLU N N 118.98 0.05 1 613 . 170 LYS H H 8.02 0.01 1 614 . 170 LYS C C 179.24 0.05 1 615 . 170 LYS CA C 58.71 0.05 1 616 . 170 LYS N N 119.77 0.05 1 617 . 171 LEU H H 8.11 0.01 1 618 . 171 LEU C C 178.06 0.05 1 619 . 171 LEU CA C 58.45 0.05 1 620 . 171 LEU N N 121.14 0.05 1 621 . 172 ASP H H 8.04 0.01 1 622 . 172 ASP C C 179.09 0.05 1 623 . 172 ASP CA C 58.25 0.05 1 624 . 172 ASP N N 119.59 0.05 1 625 . 173 GLU H H 8.10 0.01 1 626 . 173 GLU C C 178.93 0.05 1 627 . 173 GLU CA C 59.87 0.05 1 628 . 173 GLU N N 121.53 0.05 1 629 . 174 VAL H H 8.35 0.01 1 630 . 174 VAL C C 179.38 0.05 1 631 . 174 VAL CA C 66.14 0.05 1 632 . 174 VAL N N 117.62 0.05 1 633 . 175 PHE H H 8.24 0.01 1 634 . 175 PHE C C 175.63 0.05 1 635 . 175 PHE CA C 61.81 0.05 1 636 . 175 PHE N N 120.40 0.05 1 637 . 176 GLU H H 8.17 0.01 1 638 . 176 GLU C C 179.70 0.05 1 639 . 176 GLU CA C 59.58 0.05 1 640 . 176 GLU N N 119.42 0.05 1 641 . 177 ILE H H 8.08 0.01 1 642 . 177 ILE C C 178.76 0.05 1 643 . 177 ILE CA C 64.90 0.05 1 644 . 177 ILE N N 119.47 0.05 1 645 . 178 LYS H H 7.76 0.01 1 646 . 178 LYS C C 178.14 0.05 1 647 . 178 LYS CA C 56.90 0.05 1 648 . 178 LYS N N 122.34 0.05 1 649 . 179 LYS H H 8.92 0.01 1 650 . 179 LYS C C 177.70 0.05 1 651 . 179 LYS CA C 60.32 0.05 1 652 . 179 LYS N N 120.36 0.05 1 653 . 180 GLU H H 7.78 0.01 1 654 . 180 GLU C C 178.56 0.05 1 655 . 180 GLU CA C 59.69 0.05 1 656 . 180 GLU N N 118.10 0.05 1 657 . 181 GLU H H 7.62 0.01 1 658 . 181 GLU C C 179.46 0.05 1 659 . 181 GLU CA C 59.49 0.05 1 660 . 181 GLU N N 119.74 0.05 1 661 . 182 ILE H H 8.46 0.01 1 662 . 182 ILE C C 177.61 0.05 1 663 . 182 ILE CA C 65.26 0.05 1 664 . 182 ILE N N 119.15 0.05 1 665 . 183 MET H H 8.15 0.01 1 666 . 183 MET C C 177.45 0.05 1 667 . 183 MET CA C 55.56 0.05 1 668 . 183 MET N N 114.26 0.05 1 669 . 184 GLU H H 7.83 0.01 1 670 . 184 GLU C C 176.10 0.05 1 671 . 184 GLU CA C 57.49 0.05 1 672 . 184 GLU N N 118.27 0.05 1 673 . 185 PHE H H 7.51 0.01 1 674 . 185 PHE CA C 60.50 0.05 1 675 . 185 PHE N N 124.61 0.05 1 stop_ save_