data_5458 #Corrected using PDB structure: 1EH1A # #N.B. (Observed* = Observed shift + Offset correction) # #After reference correction, the following residues still #have a CA chemical shift difference (obs*-pred) greater than 5.0ppm: #NUM AA CS Observed* Predicted # 84 R CA 60.11 54.64 # #After reference correction, the following residues still #have a CO chemical shift difference (obs*-pred) greater than 5.0ppm: #NUM AA CS Observed* Predicted #185 G C 178.88 173.66 # #After reference correction, the following residues still #have a N chemical shift difference (obs*-pred) greater than 10.0ppm: #NUM AA CS Observed* Predicted # 30 T N 110.52 123.47 # #The average CS difference between predicted and observed: #HA CA CB CO N HN #N/A -0.49 -0.39 -0.22 -0.68 -0.22 # #bmr5458.str.corr chemical shifts have been re-referenced with the following #offsets (these values have been added to the original bmr5458.str file): #HA CA CB CO N HN #N/A -0.44 -0.44 -0.22 -0.68 N/A # #The 95% confidence intervals for the above recommended offsets are: # HA CA CB CO N HN # N/A +/-0.11 +/-0.12 +/-0.11 +/-0.24 +/-0.05 # #The Correlation Coefficients between predicted and observed #chemical shifts are: #HA CA CB CO N HN #N/A 0.967 0.996 0.842 0.792 0.570 # #The RMSD between predicted and observed* (reference #corrected) chemical shifts are: #HA CA CB CO N HN #N/A 0.766 0.787 0.747 1.619 0.309 # ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Backbone 1H, 13C, and 15N assignments of the ribosome recycling factor from Thermus thermophillus ; loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Blake Brain K. . 2 Ito Koichi . . 3 Nakamura Yoshikazu . . 4 Alam Steven L. . stop_ _BMRB_accession_number 5458 _BMRB_flat_file_name bmr5458.str _Entry_type new _Submission_date 2002-07-09 _Accession_date 2002-07-09 _Entry_origination author _NMR_STAR_version 2.1.1 _Experimental_method NMR loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count '1H chemical shifts' 178 '15N chemical shifts' 178 '13C chemical shifts' 541 stop_ save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_title ; Letter to the Editor: Backbone 1H, 13C, and 15N assignments of the ribosome recycling factor from Thermus thermophillus ; _Citation_status published _Citation_type journal _MEDLINE_UI_code . _PubMed_ID . loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Blake Brain K. . 2 Ito Koichi . . 3 Nakamura Yoshikazu . . 4 Alam Steven L . stop_ _Journal_abbreviation "J. Biomol. NMR" _Journal_volume 24 _Journal_issue 1 _Page_first 81 _Page_last 82 _Year 2002 loop_ _Keyword "Ribosome" "recycling RRF" "translation" "termination" stop_ 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 RRF $RRF stop_ _System_physical_state native _System_oligomer_state monomer _System_paramagnetic no _System_thiol_state "not present" loop_ _Biological_function "dissociates protein translational posttermination complex" stop_ loop_ _Database_name _Database_accession_code _Database_entry_mol_name _Database_entry_details Genbank AB016498.1 ? . stop_ save_ ######################## # Monomeric polymers # ######################## save_RRF _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common "ribosome recycling factor" _Name_variant . _Abbreviation_common RRF _Mol_thiol_state "not present" ############################## # Polymer residue sequence # ############################## _Residue_count 185 _Mol_residue_sequence ; MTLKELYAETRSHMQKSLEV LEHNLAGLRTGRANPALLLH LKVEYYGAHVPLNQIATVTA PDPRTLVVQSWDQNALKAIE KAIRDSDLGLNPSNKGDALY INIPPLTEERRKDLVRAVRQ YAEEGRVAIRNIRREALDKL KKLAKELHLSEDETKRAEAE IQKITDEFIAKADQLAEKKE QEILG ; loop_ _Residue_seq_code _Residue_label 1 MET 2 THR 3 LEU 4 LYS 5 GLU 6 LEU 7 TYR 8 ALA 9 GLU 10 THR 11 ARG 12 SER 13 HIS 14 MET 15 GLN 16 LYS 17 SER 18 LEU 19 GLU 20 VAL 21 LEU 22 GLU 23 HIS 24 ASN 25 LEU 26 ALA 27 GLY 28 LEU 29 ARG 30 THR 31 GLY 32 ARG 33 ALA 34 ASN 35 PRO 36 ALA 37 LEU 38 LEU 39 LEU 40 HIS 41 LEU 42 LYS 43 VAL 44 GLU 45 TYR 46 TYR 47 GLY 48 ALA 49 HIS 50 VAL 51 PRO 52 LEU 53 ASN 54 GLN 55 ILE 56 ALA 57 THR 58 VAL 59 THR 60 ALA 61 PRO 62 ASP 63 PRO 64 ARG 65 THR 66 LEU 67 VAL 68 VAL 69 GLN 70 SER 71 TRP 72 ASP 73 GLN 74 ASN 75 ALA 76 LEU 77 LYS 78 ALA 79 ILE 80 GLU 81 LYS 82 ALA 83 ILE 84 ARG 85 ASP 86 SER 87 ASP 88 LEU 89 GLY 90 LEU 91 ASN 92 PRO 93 SER 94 ASN 95 LYS 96 GLY 97 ASP 98 ALA 99 LEU 100 TYR 101 ILE 102 ASN 103 ILE 104 PRO 105 PRO 106 LEU 107 THR 108 GLU 109 GLU 110 ARG 111 ARG 112 LYS 113 ASP 114 LEU 115 VAL 116 ARG 117 ALA 118 VAL 119 ARG 120 GLN 121 TYR 122 ALA 123 GLU 124 GLU 125 GLY 126 ARG 127 VAL 128 ALA 129 ILE 130 ARG 131 ASN 132 ILE 133 ARG 134 ARG 135 GLU 136 ALA 137 LEU 138 ASP 139 LYS 140 LEU 141 LYS 142 LYS 143 LEU 144 ALA 145 LYS 146 GLU 147 LEU 148 HIS 149 LEU 150 SER 151 GLU 152 ASP 153 GLU 154 THR 155 LYS 156 ARG 157 ALA 158 GLU 159 ALA 160 GLU 161 ILE 162 GLN 163 LYS 164 ILE 165 THR 166 ASP 167 GLU 168 PHE 169 ILE 170 ALA 171 LYS 172 ALA 173 ASP 174 GLN 175 LEU 176 ALA 177 GLU 178 LYS 179 LYS 180 GLU 181 GLN 182 GLU 183 ILE 184 LEU 185 GLY stop_ _Sequence_homology_query_date 2004-07-29 _Sequence_homology_query_revised_last_date 2004-05-13 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 1EH1 "A Chain A, Ribosome Recycling Factor FromThermus Thermophilus" 100.00 185 100 100 8e-99 DBJ BAA76865.1 "ribosome recycling factor gene (RRF)[Thermus thermophilus]" 100.00 185 100 100 8e-99 GenBank AAS80854.1 "ribosome recycling factor (rrf) [Thermusthermophilus HB27]" 100.00 185 100 100 8e-99 REF YP_004481.1 "ribosome recycling factor (rrf)[Thermus thermophilus HB27]" 100.00 185 100 100 8e-99 SWISS-PROT Q9WX76 "RRF_THETH Ribosome recycling factor (Ribosomereleasing factor) (RRF)" 100.00 185 100 100 8e-99 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species _Gene_mnemonic $RRF . 274 Eubacteria . Thermus thermophillus frr 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 loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $RRF 1.05 mM "[U-98% 13C; U-98% 15N]" NH4Cl 50 mM . D2O 10 % . stop_ save_ save_sample_2 _Saveframe_category sample _Sample_type solution loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $RRF 1.05 mM "[U-98% 15N]" NH4Cl 50 mM . D2O 10 % . stop_ save_ save_sample_3 _Saveframe_category sample _Sample_type solution loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $RRF 1.05 mM "[U-98% 2H; U-98% 13C; U-98% 15N]" NH4Cl 50 mM . D2O 10 % . stop_ save_ ############################ # Computer software used # ############################ save_SPARKY _Saveframe_category software _Name SPARKY _Version 1.1 loop_ _Task "peak picking" "peak assignment" stop_ save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer1 _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model INOVA _Field_strength 750 save_ save_NMR_spectrometer2 _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model INOVA _Field_strength 600 save_ save_NMR_spectrometer3 _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model UNITY _Field_strength 500 save_ ############################# # NMR applied experiments # ############################# save_NMR_applied_experiment _Saveframe_category NMR_applied_experiment _Experiment_name ; 1H-15N HSQC HNCA HN(CO)CA HNCO HN(CA)CO CBCA(CO)NH HNCACB (H)C(CO)NH 1H-15N NOESY 1H-15N TOCSY ; save_ ####################### # Sample conditions # ####################### save_Ex-cond _Saveframe_category sample_conditions loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 6.4 .1 n/a temperature 310 0.1 K 'ionic strength' 0.10 0.02 M stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference _Saveframe_category chemical_shift_reference 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 # # # # Index Value Definition # # # # 1 Unique # # 2 Ambiguity of geminal atoms or geminal methyl # # proton groups # # 3 Aromatic atoms on opposite sides of the ring # # (e.g. Tyr HE1 and HE2 protons) # # 4 Intraresidue ambiguities (e.g. Lys HG and # # HD protons) # # 5 Interresidue ambiguities (Lys 12 vs. Lys 27) # # 9 Ambiguous, specific ambiguity not defined # # # ################################################################### save_shift_set_1 _Saveframe_category assigned_chemical_shifts loop_ _Sample_label $sample_1 $sample_2 $sample_3 stop_ _Sample_conditions_label $Ex-cond _Chem_shift_reference_set_label $chemical_shift_reference _Mol_system_component_name RRF loop_ _Atom_shift_assign_ID _Residue_seq_code _Residue_label _Atom_name _Atom_type _Chem_shift_value _Chem_shift_value_error _Chem_shift_ambiguity_code 1 1 MET CA C 55.06 0.05 1 2 1 MET CB C 34.26 0.05 1 3 2 THR N N 113.22 0.05 1 4 2 THR H H 8.38 0.01 1 5 2 THR CA C 59.66 0.05 1 6 2 THR CB C 71.36 0.05 1 7 2 THR C C 175.18 0.05 1 8 3 LEU N N 119.92 0.05 1 9 3 LEU H H 8.76 0.01 1 10 3 LEU CA C 57.86 0.05 1 11 3 LEU CB C 40.66 0.05 1 12 3 LEU C C 177.28 0.05 1 13 4 LYS N N 114.92 0.05 1 14 4 LYS H H 8.03 0.01 1 15 4 LYS CA C 59.96 0.05 1 16 4 LYS CB C 32.16 0.05 1 17 4 LYS C C 180.18 0.05 1 18 5 GLU N N 118.72 0.05 1 19 5 GLU H H 7.68 0.01 1 20 5 GLU CA C 58.86 0.05 1 21 5 GLU CB C 30.06 0.05 1 22 5 GLU C C 178.78 0.05 1 23 6 LEU N N 123.12 0.05 1 24 6 LEU H H 8.08 0.01 1 25 6 LEU CA C 58.06 0.05 1 26 6 LEU CB C 40.56 0.05 1 27 6 LEU C C 181.08 0.05 1 28 7 TYR N N 122.62 0.05 1 29 7 TYR H H 8.75 0.01 1 30 7 TYR CA C 58.56 0.05 1 31 7 TYR CB C 36.06 0.05 1 32 7 TYR C C 178.18 0.05 1 33 8 ALA N N 121.02 0.05 1 34 8 ALA H H 8.13 0.01 1 35 8 ALA CA C 55.26 0.05 1 36 8 ALA CB C 18.06 0.05 1 37 8 ALA C C 180.58 0.05 1 38 9 GLU N N 120.02 0.05 1 39 9 GLU H H 8.79 0.01 1 40 9 GLU CA C 59.26 0.05 1 41 9 GLU CB C 29.76 0.05 1 42 9 GLU C C 177.88 0.05 1 43 10 THR N N 116.62 0.05 1 44 10 THR H H 8.26 0.01 1 45 10 THR CA C 67.96 0.05 1 46 10 THR C C 175.68 0.05 1 47 11 ARG N N 119.22 0.05 1 48 11 ARG H H 8.33 0.01 1 49 11 ARG CA C 60.26 0.05 1 50 11 ARG CB C 30.26 0.05 1 51 11 ARG C C 177.38 0.05 1 52 12 SER N N 113.32 0.05 1 53 12 SER H H 8.32 0.01 1 54 12 SER CA C 61.66 0.05 1 55 12 SER CB C 62.56 0.05 1 56 12 SER C C 177.68 0.05 1 57 13 HIS N N 119.22 0.05 1 58 13 HIS H H 8.59 0.01 1 59 13 HIS CA C 58.26 0.05 1 60 13 HIS CB C 30.06 0.05 1 61 13 HIS C C 178.68 0.05 1 62 14 MET N N 120.52 0.05 1 63 14 MET H H 8.38 0.01 1 64 14 MET CA C 60.66 0.05 1 65 14 MET CB C 29.76 0.05 1 66 14 MET C C 177.08 0.05 1 67 15 GLN N N 120.32 0.05 1 68 15 GLN H H 8.63 0.01 1 69 15 GLN CA C 58.86 0.05 1 70 15 GLN CB C 27.46 0.05 1 71 15 GLN C C 178.28 0.05 1 72 16 LYS N N 118.62 0.05 1 73 16 LYS H H 7.87 0.01 1 74 16 LYS CA C 58.96 0.05 1 75 16 LYS CB C 31.36 0.05 1 76 16 LYS C C 179.28 0.05 1 77 17 SER N N 114.92 0.05 1 78 17 SER H H 7.72 0.01 1 79 17 SER CA C 62.76 0.05 1 80 17 SER C C 177.28 0.05 1 81 18 LEU N N 124.22 0.05 1 82 18 LEU H H 8.45 0.01 1 83 18 LEU CA C 57.26 0.05 1 84 18 LEU CB C 41.76 0.05 1 85 18 LEU C C 178.58 0.05 1 86 19 GLU N N 119.52 0.05 1 87 19 GLU H H 8.37 0.01 1 88 19 GLU CA C 59.36 0.05 1 89 19 GLU CB C 28.96 0.05 1 90 19 GLU C C 179.48 0.05 1 91 20 VAL N N 121.12 0.05 1 92 20 VAL H H 7.94 0.01 1 93 20 VAL CA C 66.56 0.05 1 94 20 VAL CB C 31.76 0.05 1 95 20 VAL C C 177.98 0.05 1 96 21 LEU N N 120.52 0.05 1 97 21 LEU H H 7.65 0.01 1 98 21 LEU CA C 58.36 0.05 1 99 21 LEU CB C 40.86 0.05 1 100 21 LEU C C 178.08 0.05 1 101 22 GLU N N 118.62 0.05 1 102 22 GLU H H 8.98 0.01 1 103 22 GLU CA C 60.46 0.05 1 104 22 GLU CB C 29.46 0.05 1 105 22 GLU C C 179.08 0.05 1 106 23 HIS N N 118.02 0.05 1 107 23 HIS H H 8.45 0.01 1 108 23 HIS CA C 58.86 0.05 1 109 23 HIS CB C 28.66 0.05 1 110 23 HIS C C 177.68 0.05 1 111 24 ASN N N 119.62 0.05 1 112 24 ASN H H 8.60 0.01 1 113 24 ASN CA C 55.16 0.05 1 114 24 ASN CB C 36.06 0.05 1 115 24 ASN C C 178.08 0.05 1 116 25 LEU N N 117.42 0.05 1 117 25 LEU H H 8.54 0.01 1 118 25 LEU CA C 57.16 0.05 1 119 25 LEU CB C 41.06 0.05 1 120 25 LEU C C 178.78 0.05 1 121 26 ALA N N 120.22 0.05 1 122 26 ALA H H 8.26 0.01 1 123 26 ALA CA C 54.16 0.05 1 124 26 ALA CB C 18.06 0.05 1 125 26 ALA C C 178.88 0.05 1 126 27 GLY N N 101.52 0.05 1 127 27 GLY H H 7.35 0.01 1 128 27 GLY CA C 45.06 0.05 1 129 27 GLY C C 173.98 0.05 1 130 28 LEU N N 118.92 0.05 1 131 28 LEU H H 7.19 0.01 1 132 28 LEU CA C 53.86 0.05 1 133 28 LEU CB C 41.96 0.05 1 134 28 LEU C C 176.38 0.05 1 135 29 ARG N N 124.62 0.05 1 136 29 ARG H H 8.65 0.01 1 137 29 ARG CA C 56.06 0.05 1 138 29 ARG CB C 29.76 0.05 1 139 29 ARG C C 175.08 0.05 1 140 30 THR N N 110.52 0.05 1 141 30 THR H H 8.15 0.01 1 142 30 THR CA C 60.96 0.05 1 143 30 THR CB C 69.56 0.05 1 144 30 THR C C 174.58 0.05 1 145 31 GLY N N 107.62 0.05 1 146 31 GLY H H 8.59 0.01 1 147 31 GLY CA C 45.66 0.05 1 148 31 GLY C C 173.18 0.05 1 149 32 ARG N N 117.52 0.05 1 150 32 ARG H H 7.77 0.01 1 151 32 ARG CA C 54.26 0.05 1 152 32 ARG CB C 32.26 0.05 1 153 32 ARG C C 175.58 0.05 1 154 33 ALA N N 124.62 0.05 1 155 33 ALA H H 8.76 0.01 1 156 33 ALA CA C 53.16 0.05 1 157 33 ALA CB C 18.96 0.05 1 158 33 ALA C C 175.88 0.05 1 159 34 ASN N N 120.12 0.05 1 160 34 ASN H H 7.86 0.01 1 161 34 ASN CA C 49.76 0.05 1 162 34 ASN CB C 40.16 0.05 1 163 34 ASN C C 173.68 0.05 1 164 35 PRO CA C 65.16 0.05 1 165 35 PRO CB C 32.46 0.05 1 166 35 PRO C C 176.48 0.05 1 167 36 ALA N N 116.52 0.05 1 168 36 ALA H H 8.11 0.01 1 169 36 ALA CA C 54.56 0.05 1 170 36 ALA CB C 18.26 0.05 1 171 36 ALA C C 178.18 0.05 1 172 37 LEU N N 116.02 0.05 1 173 37 LEU H H 7.83 0.01 1 174 37 LEU CA C 57.06 0.05 1 175 37 LEU CB C 43.16 0.05 1 176 37 LEU C C 177.08 0.05 1 177 38 LEU N N 110.82 0.05 1 178 38 LEU H H 7.34 0.01 1 179 38 LEU CA C 54.06 0.05 1 180 38 LEU CB C 44.16 0.05 1 181 38 LEU C C 177.58 0.05 1 182 39 LEU N N 115.02 0.05 1 183 39 LEU H H 7.38 0.01 1 184 39 LEU CA C 58.46 0.05 1 185 39 LEU CB C 42.46 0.05 1 186 39 LEU C C 176.28 0.05 1 187 40 HIS N N 112.02 0.05 1 188 40 HIS H H 8.14 0.01 1 189 40 HIS CA C 54.96 0.05 1 190 40 HIS CB C 29.76 0.05 1 191 40 HIS C C 175.48 0.05 1 192 41 LEU N N 122.62 0.05 1 193 41 LEU H H 7.40 0.01 1 194 41 LEU CA C 55.56 0.05 1 195 41 LEU CB C 42.86 0.05 1 196 41 LEU C C 175.88 0.05 1 197 42 LYS N N 122.72 0.05 1 198 42 LYS H H 8.43 0.01 1 199 42 LYS CA C 55.56 0.05 1 200 42 LYS CB C 33.06 0.05 1 201 42 LYS C C 175.68 0.05 1 202 43 VAL N N 123.02 0.05 1 203 43 VAL H H 9.27 0.01 1 204 43 VAL CA C 60.36 0.05 1 205 43 VAL CB C 34.56 0.05 1 206 43 VAL C C 174.58 0.05 1 207 44 GLU N N 126.92 0.05 1 208 44 GLU H H 8.55 0.01 1 209 44 GLU CA C 56.26 0.05 1 210 44 GLU CB C 29.06 0.05 1 211 44 GLU C C 174.68 0.05 1 212 45 TYR N N 129.52 0.05 1 213 45 TYR H H 9.10 0.01 1 214 45 TYR CA C 56.86 0.05 1 215 45 TYR CB C 41.06 0.05 1 216 45 TYR C C 173.88 0.05 1 217 46 TYR N N 124.32 0.05 1 218 46 TYR H H 8.72 0.01 1 219 46 TYR CA C 59.06 0.05 1 220 46 TYR CB C 35.66 0.05 1 221 46 TYR C C 176.08 0.05 1 222 47 GLY N N 103.82 0.05 1 223 47 GLY H H 8.50 0.01 1 224 47 GLY CA C 45.46 0.05 1 225 47 GLY C C 173.18 0.05 1 226 48 ALA N N 122.92 0.05 1 227 48 ALA H H 7.76 0.01 1 228 48 ALA CA C 50.16 0.05 1 229 48 ALA CB C 21.36 0.05 1 230 48 ALA C C 175.38 0.05 1 231 49 HIS N N 119.12 0.05 1 232 49 HIS H H 8.61 0.01 1 233 49 HIS CA C 55.76 0.05 1 234 49 HIS CB C 30.56 0.05 1 235 49 HIS C C 175.38 0.05 1 236 50 VAL N N 120.62 0.05 1 237 50 VAL H H 9.24 0.01 1 238 50 VAL CA C 57.66 0.05 1 239 50 VAL CB C 33.76 0.05 1 240 50 VAL C C 172.48 0.05 1 241 51 PRO CA C 62.26 0.05 1 242 51 PRO CB C 31.96 0.05 1 243 51 PRO C C 178.38 0.05 1 244 52 LEU N N 124.72 0.05 1 245 52 LEU H H 8.81 0.01 1 246 52 LEU CA C 59.66 0.05 1 247 52 LEU CB C 41.36 0.05 1 248 52 LEU C C 177.78 0.05 1 249 53 ASN N N 111.02 0.05 1 250 53 ASN H H 8.21 0.01 1 251 53 ASN CA C 54.56 0.05 1 252 53 ASN CB C 38.06 0.05 1 253 53 ASN C C 175.48 0.05 1 254 54 GLN N N 116.92 0.05 1 255 54 GLN H H 8.18 0.01 1 256 54 GLN CA C 57.06 0.05 1 257 54 GLN CB C 29.46 0.05 1 258 54 GLN C C 177.08 0.05 1 259 55 ILE N N 109.22 0.05 1 260 55 ILE H H 7.73 0.01 1 261 55 ILE CA C 60.06 0.05 1 262 55 ILE CB C 40.56 0.05 1 263 55 ILE C C 173.08 0.05 1 264 56 ALA N N 123.62 0.05 1 265 56 ALA H H 7.95 0.01 1 266 56 ALA CA C 51.06 0.05 1 267 56 ALA CB C 22.76 0.05 1 268 56 ALA C C 175.08 0.05 1 269 57 THR N N 110.12 0.05 1 270 57 THR H H 8.71 0.01 1 271 57 THR CA C 60.16 0.05 1 272 57 THR CB C 71.06 0.05 1 273 57 THR C C 173.68 0.05 1 274 58 VAL N N 122.92 0.05 1 275 58 VAL H H 8.66 0.01 1 276 58 VAL CA C 60.36 0.05 1 277 58 VAL CB C 34.06 0.05 1 278 58 VAL C C 174.58 0.05 1 279 59 THR N N 117.82 0.05 1 280 59 THR H H 9.01 0.01 1 281 59 THR CA C 59.56 0.05 1 282 59 THR CB C 72.16 0.05 1 283 59 THR C C 172.18 0.05 1 284 60 ALA N N 122.82 0.05 1 285 60 ALA H H 8.70 0.01 1 286 60 ALA CA C 48.16 0.05 1 287 60 ALA CB C 19.96 0.05 1 288 60 ALA C C 174.98 0.05 1 289 61 PRO CA C 64.06 0.05 1 290 61 PRO CB C 31.96 0.05 1 291 61 PRO C C 175.68 0.05 1 292 62 ASP N N 114.52 0.05 1 293 62 ASP H H 7.90 0.01 1 294 62 ASP CA C 52.36 0.05 1 295 62 ASP CB C 40.96 0.05 1 296 62 ASP C C 173.98 0.05 1 297 63 PRO CA C 64.66 0.05 1 298 63 PRO CB C 32.66 0.05 1 299 63 PRO C C 176.58 0.05 1 300 64 ARG N N 115.02 0.05 1 301 64 ARG H H 8.56 0.01 1 302 64 ARG CA C 54.66 0.05 1 303 64 ARG CB C 31.76 0.05 1 304 64 ARG C C 175.48 0.05 1 305 65 THR N N 117.62 0.05 1 306 65 THR H H 7.52 0.01 1 307 65 THR CA C 62.46 0.05 1 308 65 THR CB C 71.36 0.05 1 309 65 THR C C 172.68 0.05 1 310 66 LEU N N 121.22 0.05 1 311 66 LEU H H 8.84 0.01 1 312 66 LEU CA C 52.56 0.05 1 313 66 LEU CB C 46.26 0.05 1 314 66 LEU C C 174.98 0.05 1 315 67 VAL N N 120.82 0.05 1 316 67 VAL H H 9.03 0.01 1 317 67 VAL CA C 60.46 0.05 1 318 67 VAL CB C 33.56 0.05 1 319 67 VAL C C 175.48 0.05 1 320 68 VAL N N 126.82 0.05 1 321 68 VAL H H 9.07 0.01 1 322 68 VAL CA C 60.06 0.05 1 323 68 VAL CB C 33.46 0.05 1 324 68 VAL C C 174.48 0.05 1 325 69 GLN N N 124.32 0.05 1 326 69 GLN H H 8.69 0.01 1 327 69 GLN CA C 54.56 0.05 1 328 69 GLN CB C 32.96 0.05 1 329 69 GLN C C 173.98 0.05 1 330 70 SER N N 113.92 0.05 1 331 70 SER H H 8.36 0.01 1 332 70 SER CA C 57.06 0.05 1 333 70 SER CB C 64.36 0.05 1 334 70 SER C C 173.58 0.05 1 335 71 TRP N N 123.02 0.05 1 336 71 TRP H H 7.68 0.01 1 337 71 TRP CA C 57.86 0.05 1 338 71 TRP CB C 28.26 0.05 1 339 71 TRP NE1 N 129.90 0.05 1 340 71 TRP HE1 H 10.30 0.01 1 341 71 TRP C C 175.48 0.05 1 342 72 ASP N N 119.22 0.05 1 343 72 ASP H H 7.86 0.01 1 344 72 ASP CA C 52.16 0.05 1 345 72 ASP CB C 41.36 0.05 1 346 72 ASP C C 176.98 0.05 1 347 73 GLN N N 125.92 0.05 1 348 73 GLN H H 9.24 0.01 1 349 73 GLN CA C 58.96 0.05 1 350 73 GLN CB C 28.26 0.05 1 351 73 GLN C C 178.48 0.05 1 352 74 ASN N N 116.52 0.05 1 353 74 ASN H H 8.66 0.01 1 354 74 ASN CA C 55.66 0.05 1 355 74 ASN CB C 37.96 0.05 1 356 74 ASN C C 177.88 0.05 1 357 75 ALA N N 122.42 0.05 1 358 75 ALA H H 7.96 0.01 1 359 75 ALA CA C 54.06 0.05 1 360 75 ALA CB C 18.06 0.05 1 361 75 ALA C C 178.78 0.05 1 362 76 LEU N N 116.02 0.05 1 363 76 LEU H H 7.52 0.01 1 364 76 LEU CA C 58.36 0.05 1 365 76 LEU CB C 41.16 0.05 1 366 76 LEU C C 178.88 0.05 1 367 77 LYS N N 117.32 0.05 1 368 77 LYS H H 7.89 0.01 1 369 77 LYS CA C 59.16 0.05 1 370 77 LYS CB C 31.86 0.05 1 371 77 LYS C C 178.88 0.05 1 372 78 ALA N N 122.82 0.05 1 373 78 ALA H H 7.65 0.01 1 374 78 ALA CA C 54.76 0.05 1 375 78 ALA CB C 18.16 0.05 1 376 78 ALA C C 180.98 0.05 1 377 79 ILE N N 120.62 0.05 1 378 79 ILE H H 8.58 0.01 1 379 79 ILE CA C 65.36 0.05 1 380 79 ILE CB C 37.96 0.05 1 381 79 ILE C C 176.58 0.05 1 382 80 GLU N N 120.32 0.05 1 383 80 GLU H H 8.63 0.01 1 384 80 GLU CA C 60.66 0.05 1 385 80 GLU CB C 29.26 0.05 1 386 80 GLU C C 177.68 0.05 1 387 81 LYS N N 117.72 0.05 1 388 81 LYS H H 7.67 0.01 1 389 81 LYS CA C 59.46 0.05 1 390 81 LYS CB C 32.56 0.05 1 391 81 LYS C C 177.18 0.05 1 392 82 ALA N N 119.52 0.05 1 393 82 ALA H H 7.96 0.01 1 394 82 ALA CA C 54.86 0.05 1 395 82 ALA CB C 18.96 0.05 1 396 82 ALA C C 180.78 0.05 1 397 83 ILE N N 115.62 0.05 1 398 83 ILE H H 8.54 0.01 1 399 83 ILE CA C 65.36 0.05 1 400 83 ILE CB C 38.36 0.05 1 401 83 ILE C C 179.58 0.05 1 402 84 ARG N N 122.52 0.05 1 403 84 ARG H H 8.68 0.01 1 404 84 ARG CA C 60.16 0.05 1 405 84 ARG CB C 29.76 0.05 1 406 84 ARG C C 177.58 0.05 1 407 85 ASP N N 116.82 0.05 1 408 85 ASP H H 8.53 0.01 1 409 85 ASP CA C 54.96 0.05 1 410 85 ASP CB C 40.46 0.05 1 411 85 ASP C C 176.58 0.05 1 412 86 SER N N 115.22 0.05 1 413 86 SER H H 7.60 0.01 1 414 86 SER CA C 59.16 0.05 1 415 86 SER CB C 64.76 0.05 1 416 86 SER C C 173.58 0.05 1 417 87 ASP N N 117.92 0.05 1 418 87 ASP H H 8.51 0.01 1 419 87 ASP CA C 53.86 0.05 1 420 87 ASP CB C 39.96 0.05 1 421 87 ASP C C 177.08 0.05 1 422 88 LEU N N 117.42 0.05 1 423 88 LEU H H 8.18 0.01 1 424 88 LEU CA C 56.46 0.05 1 425 88 LEU CB C 43.26 0.05 1 426 88 LEU C C 177.98 0.05 1 427 89 GLY N N 107.22 0.05 1 428 89 GLY H H 8.50 0.01 1 429 89 GLY CA C 46.36 0.05 1 430 89 GLY C C 174.28 0.05 1 431 90 LEU N N 116.52 0.05 1 432 90 LEU H H 7.54 0.01 1 433 90 LEU CA C 52.86 0.05 1 434 90 LEU CB C 44.26 0.05 1 435 90 LEU C C 175.58 0.05 1 436 91 ASN N N 117.92 0.05 1 437 91 ASN H H 8.91 0.01 1 438 91 ASN CA C 49.96 0.05 1 439 91 ASN CB C 39.56 0.05 1 440 91 ASN C C 172.58 0.05 1 441 92 PRO CA C 62.26 0.05 1 442 92 PRO CB C 33.16 0.05 1 443 92 PRO C C 174.78 0.05 1 444 93 SER N N 115.62 0.05 1 445 93 SER H H 9.00 0.01 1 446 93 SER CA C 56.76 0.05 1 447 93 SER CB C 64.36 0.05 1 448 93 SER C C 173.78 0.05 1 449 94 ASN N N 125.52 0.05 1 450 94 ASN H H 9.28 0.01 1 451 94 ASN CA C 53.26 0.05 1 452 94 ASN CB C 38.76 0.05 1 453 94 ASN C C 175.48 0.05 1 454 95 LYS N N 125.92 0.05 1 455 95 LYS H H 8.61 0.01 1 456 95 LYS CA C 55.06 0.05 1 457 95 LYS CB C 32.46 0.05 1 458 95 LYS C C 176.38 0.05 1 459 96 GLY N N 112.52 0.05 1 460 96 GLY H H 9.07 0.01 1 461 96 GLY CA C 46.76 0.05 1 462 96 GLY C C 174.18 0.05 1 463 97 ASP N N 119.12 0.05 1 464 97 ASP H H 8.52 0.01 1 465 97 ASP CA C 53.36 0.05 1 466 97 ASP CB C 40.16 0.05 1 467 97 ASP C C 174.88 0.05 1 468 98 ALA N N 118.42 0.05 1 469 98 ALA H H 7.60 0.01 1 470 98 ALA CA C 51.06 0.05 1 471 98 ALA CB C 22.16 0.05 1 472 98 ALA C C 175.68 0.05 1 473 99 LEU N N 116.62 0.05 1 474 99 LEU H H 8.88 0.01 1 475 99 LEU CA C 52.66 0.05 1 476 99 LEU CB C 44.06 0.05 1 477 99 LEU C C 175.08 0.05 1 478 100 TYR N N 122.72 0.05 1 479 100 TYR H H 9.23 0.01 1 480 100 TYR CA C 57.46 0.05 1 481 100 TYR CB C 40.36 0.05 1 482 100 TYR C C 175.88 0.05 1 483 101 ILE N N 123.92 0.05 1 484 101 ILE H H 9.51 0.01 1 485 101 ILE CA C 60.26 0.05 1 486 101 ILE CB C 40.36 0.05 1 487 101 ILE C C 173.58 0.05 1 488 102 ASN N N 125.42 0.05 1 489 102 ASN H H 8.87 0.01 1 490 102 ASN CA C 52.86 0.05 1 491 102 ASN CB C 39.86 0.05 1 492 102 ASN C C 174.18 0.05 1 493 103 ILE N N 126.62 0.05 1 494 103 ILE H H 8.81 0.01 1 495 103 ILE CA C 56.16 0.05 1 496 103 ILE CB C 36.96 0.05 1 497 103 ILE C C 173.68 0.05 1 498 105 PRO CA C 62.06 0.05 1 499 105 PRO CB C 32.06 0.05 1 500 105 PRO C C 177.28 0.05 1 501 106 LEU N N 120.52 0.05 1 502 106 LEU H H 8.69 0.01 1 503 106 LEU CA C 54.46 0.05 1 504 106 LEU CB C 43.46 0.05 1 505 106 LEU C C 177.88 0.05 1 506 107 THR N N 111.42 0.05 1 507 107 THR H H 7.71 0.01 1 508 107 THR CA C 60.26 0.05 1 509 107 THR CB C 70.66 0.05 1 510 107 THR C C 175.38 0.05 1 511 108 GLU N N 121.52 0.05 1 512 108 GLU H H 9.11 0.01 1 513 108 GLU CA C 59.86 0.05 1 514 108 GLU CB C 29.16 0.05 1 515 108 GLU C C 178.78 0.05 1 516 109 GLU N N 117.12 0.05 1 517 109 GLU H H 8.89 0.01 1 518 109 GLU CA C 59.76 0.05 1 519 109 GLU CB C 28.96 0.05 1 520 109 GLU C C 178.58 0.05 1 521 110 ARG N N 118.82 0.05 1 522 110 ARG H H 7.67 0.01 1 523 110 ARG CA C 57.96 0.05 1 524 110 ARG CB C 29.96 0.05 1 525 110 ARG C C 178.68 0.05 1 526 111 ARG N N 118.52 0.05 1 527 111 ARG H H 8.59 0.01 1 528 111 ARG CA C 60.56 0.05 1 529 111 ARG CB C 30.36 0.05 1 530 111 ARG C C 177.78 0.05 1 531 112 LYS N N 116.42 0.05 1 532 112 LYS H H 8.01 0.01 1 533 112 LYS CA C 59.76 0.05 1 534 112 LYS CB C 31.96 0.05 1 535 112 LYS C C 179.58 0.05 1 536 113 ASP N N 119.72 0.05 1 537 113 ASP H H 7.90 0.01 1 538 113 ASP CA C 57.26 0.05 1 539 113 ASP CB C 40.96 0.05 1 540 113 ASP C C 179.08 0.05 1 541 114 LEU N N 121.32 0.05 1 542 114 LEU H H 8.54 0.01 1 543 114 LEU CA C 57.76 0.05 1 544 114 LEU CB C 42.66 0.05 1 545 114 LEU C C 178.88 0.05 1 546 115 VAL N N 119.02 0.05 1 547 115 VAL H H 8.44 0.01 1 548 115 VAL CA C 67.66 0.05 1 549 115 VAL CB C 31.36 0.05 1 550 115 VAL C C 177.68 0.05 1 551 116 ARG N N 118.62 0.05 1 552 116 ARG H H 7.83 0.01 1 553 116 ARG CA C 59.76 0.05 1 554 116 ARG CB C 29.26 0.05 1 555 116 ARG C C 178.88 0.05 1 556 117 ALA N N 121.62 0.05 1 557 117 ALA H H 7.92 0.01 1 558 117 ALA CA C 54.96 0.05 1 559 117 ALA CB C 17.86 0.05 1 560 117 ALA C C 179.38 0.05 1 561 118 VAL N N 118.02 0.05 1 562 118 VAL H H 8.49 0.01 1 563 118 VAL CA C 67.16 0.05 1 564 118 VAL CB C 31.36 0.05 1 565 118 VAL C C 177.68 0.05 1 566 119 ARG N N 116.62 0.05 1 567 119 ARG H H 8.31 0.01 1 568 119 ARG CA C 59.56 0.05 1 569 119 ARG CB C 29.46 0.05 1 570 119 ARG C C 179.58 0.05 1 571 120 GLN N N 121.32 0.05 1 572 120 GLN H H 8.44 0.01 1 573 120 GLN CA C 58.86 0.05 1 574 120 GLN CB C 27.86 0.05 1 575 120 GLN C C 178.78 0.05 1 576 121 TYR N N 118.62 0.05 1 577 121 TYR H H 8.72 0.01 1 578 121 TYR CA C 59.76 0.05 1 579 121 TYR CB C 36.76 0.05 1 580 121 TYR C C 179.78 0.05 1 581 122 ALA N N 122.32 0.05 1 582 122 ALA H H 9.25 0.01 1 583 122 ALA CA C 55.66 0.05 1 584 122 ALA CB C 18.16 0.05 1 585 122 ALA C C 178.78 0.05 1 586 123 GLU N N 118.62 0.05 1 587 123 GLU H H 8.17 0.01 1 588 123 GLU CA C 59.06 0.05 1 589 123 GLU CB C 28.46 0.05 1 590 123 GLU C C 178.38 0.05 1 591 124 GLU N N 118.32 0.05 1 592 124 GLU H H 8.34 0.01 1 593 124 GLU CA C 59.66 0.05 1 594 124 GLU CB C 29.26 0.05 1 595 124 GLU C C 180.38 0.05 1 596 125 GLY N N 107.72 0.05 1 597 125 GLY H H 8.52 0.01 1 598 125 GLY CA C 46.96 0.05 1 599 125 GLY C C 174.98 0.05 1 600 126 ARG N N 121.22 0.05 1 601 126 ARG H H 8.72 0.01 1 602 126 ARG CA C 60.76 0.05 1 603 126 ARG CB C 29.96 0.05 1 604 126 ARG C C 178.58 0.05 1 605 127 VAL N N 119.62 0.05 1 606 127 VAL H H 8.87 0.01 1 607 127 VAL CA C 66.76 0.05 1 608 127 VAL CB C 31.66 0.05 1 609 127 VAL C C 178.38 0.05 1 610 128 ALA N N 121.82 0.05 1 611 128 ALA H H 8.08 0.01 1 612 128 ALA CA C 55.46 0.05 1 613 128 ALA CB C 17.66 0.05 1 614 128 ALA C C 181.08 0.05 1 615 129 ILE N N 119.12 0.05 1 616 129 ILE H H 8.36 0.01 1 617 129 ILE CA C 65.96 0.05 1 618 129 ILE CB C 38.16 0.05 1 619 129 ILE C C 178.18 0.05 1 620 130 ARG N N 119.22 0.05 1 621 130 ARG H H 8.87 0.01 1 622 130 ARG CA C 60.56 0.05 1 623 130 ARG CB C 29.56 0.05 1 624 130 ARG C C 179.68 0.05 1 625 131 ASN N N 121.52 0.05 1 626 131 ASN H H 8.88 0.01 1 627 131 ASN CA C 55.96 0.05 1 628 131 ASN CB C 37.66 0.05 1 629 131 ASN C C 177.68 0.05 1 630 132 ILE N N 123.12 0.05 1 631 132 ILE H H 8.17 0.01 1 632 132 ILE CA C 64.76 0.05 1 633 132 ILE CB C 37.16 0.05 1 634 132 ILE C C 178.18 0.05 1 635 133 ARG N N 120.92 0.05 1 636 133 ARG H H 8.21 0.01 1 637 133 ARG CA C 59.96 0.05 1 638 133 ARG CB C 28.06 0.05 1 639 133 ARG C C 176.88 0.05 1 640 134 ARG N N 117.92 0.05 1 641 134 ARG H H 7.87 0.01 1 642 134 ARG CA C 59.76 0.05 1 643 134 ARG CB C 29.66 0.05 1 644 134 ARG C C 178.78 0.05 1 645 135 GLU N N 119.02 0.05 1 646 135 GLU H H 8.18 0.01 1 647 135 GLU CA C 59.36 0.05 1 648 135 GLU CB C 29.56 0.05 1 649 135 GLU C C 179.28 0.05 1 650 136 ALA N N 123.42 0.05 1 651 136 ALA H H 8.96 0.01 1 652 136 ALA CA C 55.26 0.05 1 653 136 ALA CB C 19.16 0.05 1 654 136 ALA C C 179.88 0.05 1 655 137 LEU N N 117.52 0.05 1 656 137 LEU H H 8.66 0.01 1 657 137 LEU CA C 57.46 0.05 1 658 137 LEU CB C 40.96 0.05 1 659 137 LEU C C 180.18 0.05 1 660 138 ASP N N 121.82 0.05 1 661 138 ASP H H 8.26 0.01 1 662 138 ASP CA C 57.56 0.05 1 663 138 ASP CB C 40.26 0.05 1 664 138 ASP C C 179.58 0.05 1 665 139 LYS N N 120.92 0.05 1 666 139 LYS H H 8.34 0.01 1 667 139 LYS CA C 59.86 0.05 1 668 139 LYS CB C 34.56 0.05 1 669 139 LYS C C 179.48 0.05 1 670 140 LEU N N 120.92 0.05 1 671 140 LEU H H 8.91 0.01 1 672 140 LEU CA C 57.76 0.05 1 673 140 LEU CB C 41.26 0.05 1 674 140 LEU C C 177.08 0.05 1 675 141 LYS N N 117.32 0.05 1 676 141 LYS H H 7.87 0.01 1 677 141 LYS CA C 59.66 0.05 1 678 141 LYS CB C 32.06 0.05 1 679 141 LYS C C 179.38 0.05 1 680 142 LYS N N 117.62 0.05 1 681 142 LYS H H 7.28 0.01 1 682 142 LYS CA C 59.06 0.05 1 683 142 LYS CB C 32.56 0.05 1 684 142 LYS C C 179.08 0.05 1 685 143 LEU N N 121.52 0.05 1 686 143 LEU H H 8.67 0.01 1 687 143 LEU CA C 57.66 0.05 1 688 143 LEU CB C 42.26 0.05 1 689 143 LEU C C 178.48 0.05 1 690 144 ALA N N 119.72 0.05 1 691 144 ALA H H 9.35 0.01 1 692 144 ALA CA C 55.16 0.05 1 693 144 ALA CB C 18.46 0.05 1 694 144 ALA C C 180.18 0.05 1 695 145 LYS N N 115.12 0.05 1 696 145 LYS H H 7.17 0.01 1 697 145 LYS CA C 58.26 0.05 1 698 145 LYS CB C 32.36 0.05 1 699 145 LYS C C 179.08 0.05 1 700 146 GLU N N 119.92 0.05 1 701 146 GLU H H 7.94 0.01 1 702 146 GLU CA C 58.96 0.05 1 703 146 GLU CB C 30.06 0.05 1 704 146 GLU C C 178.28 0.05 1 705 147 LEU N N 114.42 0.05 1 706 147 LEU H H 8.65 0.01 1 707 147 LEU CA C 54.16 0.05 1 708 147 LEU CB C 41.76 0.05 1 709 147 LEU C C 176.48 0.05 1 710 148 HIS N N 114.92 0.05 1 711 148 HIS H H 7.59 0.01 1 712 148 HIS CA C 55.96 0.05 1 713 148 HIS CB C 25.86 0.05 1 714 148 HIS C C 174.98 0.05 1 715 149 LEU N N 116.32 0.05 1 716 149 LEU H H 8.14 0.01 1 717 149 LEU CA C 54.86 0.05 1 718 149 LEU CB C 42.26 0.05 1 719 149 LEU C C 178.38 0.05 1 720 150 SER N N 118.42 0.05 1 721 150 SER H H 9.36 0.01 1 722 150 SER CA C 57.16 0.05 1 723 150 SER CB C 65.26 0.05 1 724 150 SER C C 175.98 0.05 1 725 151 GLU N N 123.52 0.05 1 726 151 GLU H H 9.35 0.01 1 727 151 GLU CA C 60.16 0.05 1 728 151 GLU CB C 29.16 0.05 1 729 151 GLU C C 178.78 0.05 1 730 152 ASP N N 117.52 0.05 1 731 152 ASP H H 8.64 0.01 1 732 152 ASP CA C 57.46 0.05 1 733 152 ASP CB C 40.96 0.05 1 734 152 ASP C C 178.98 0.05 1 735 153 GLU N N 118.92 0.05 1 736 153 GLU H H 8.02 0.01 1 737 153 GLU CA C 59.16 0.05 1 738 153 GLU CB C 30.76 0.05 1 739 153 GLU C C 179.68 0.05 1 740 154 THR N N 117.42 0.05 1 741 154 THR H H 8.61 0.01 1 742 154 THR CA C 67.56 0.05 1 743 154 THR C C 176.18 0.05 1 744 155 LYS N N 121.52 0.05 1 745 155 LYS H H 8.46 0.01 1 746 155 LYS CA C 59.26 0.05 1 747 155 LYS CB C 31.86 0.05 1 748 155 LYS C C 180.18 0.05 1 749 156 ARG N N 119.82 0.05 1 750 156 ARG H H 8.10 0.01 1 751 156 ARG CA C 59.26 0.05 1 752 156 ARG CB C 29.86 0.05 1 753 156 ARG C C 178.68 0.05 1 754 157 ALA N N 123.72 0.05 1 755 157 ALA H H 8.00 0.01 1 756 157 ALA CA C 54.56 0.05 1 757 157 ALA CB C 20.66 0.05 1 758 157 ALA C C 180.08 0.05 1 759 158 GLU N N 119.02 0.05 1 760 158 GLU H H 8.67 0.01 1 761 158 GLU CA C 60.06 0.05 1 762 158 GLU CB C 29.36 0.05 1 763 158 GLU C C 179.48 0.05 1 764 159 ALA N N 120.92 0.05 1 765 159 ALA H H 8.09 0.01 1 766 159 ALA CA C 54.66 0.05 1 767 159 ALA CB C 17.56 0.05 1 768 159 ALA C C 180.58 0.05 1 769 160 GLU N N 121.52 0.05 1 770 160 GLU H H 8.25 0.01 1 771 160 GLU CA C 58.86 0.05 1 772 160 GLU CB C 28.56 0.05 1 773 160 GLU C C 179.18 0.05 1 774 161 ILE N N 118.62 0.05 1 775 161 ILE H H 8.33 0.01 1 776 161 ILE CA C 64.56 0.05 1 777 161 ILE CB C 36.96 0.05 1 778 161 ILE C C 179.58 0.05 1 779 162 GLN N N 123.32 0.05 1 780 162 GLN H H 8.65 0.01 1 781 162 GLN CA C 58.86 0.05 1 782 162 GLN CB C 27.76 0.05 1 783 162 GLN C C 176.58 0.05 1 784 163 LYS N N 120.72 0.05 1 785 163 LYS H H 8.36 0.01 1 786 163 LYS CA C 59.86 0.05 1 787 163 LYS CB C 32.16 0.05 1 788 163 LYS C C 179.98 0.05 1 789 164 ILE N N 120.22 0.05 1 790 164 ILE H H 8.32 0.01 1 791 164 ILE CA C 65.86 0.05 1 792 164 ILE CB C 39.26 0.05 1 793 164 ILE C C 177.38 0.05 1 794 165 THR N N 115.32 0.05 1 795 165 THR H H 8.11 0.01 1 796 165 THR CA C 67.96 0.05 1 797 165 THR CB C 72.56 0.05 1 798 165 THR C C 175.98 0.05 1 799 166 ASP N N 120.52 0.05 1 800 166 ASP H H 8.97 0.01 1 801 166 ASP CA C 57.56 0.05 1 802 166 ASP CB C 40.06 0.05 1 803 166 ASP C C 179.38 0.05 1 804 167 GLU N N 121.52 0.05 1 805 167 GLU H H 8.20 0.01 1 806 167 GLU CA C 59.06 0.05 1 807 167 GLU CB C 29.16 0.05 1 808 167 GLU C C 179.08 0.05 1 809 168 PHE N N 118.02 0.05 1 810 168 PHE H H 8.30 0.01 1 811 168 PHE CA C 64.06 0.05 1 812 168 PHE CB C 39.06 0.05 1 813 168 PHE C C 178.08 0.05 1 814 169 ILE N N 121.72 0.05 1 815 169 ILE H H 9.26 0.01 1 816 169 ILE CA C 63.66 0.05 1 817 169 ILE CB C 35.66 0.05 1 818 169 ILE C C 177.18 0.05 1 819 170 ALA N N 119.32 0.05 1 820 170 ALA H H 7.96 0.01 1 821 170 ALA CA C 55.06 0.05 1 822 170 ALA CB C 17.46 0.05 1 823 170 ALA C C 181.18 0.05 1 824 171 LYS N N 117.52 0.05 1 825 171 LYS H H 7.84 0.01 1 826 171 LYS CA C 59.66 0.05 1 827 171 LYS CB C 33.06 0.05 1 828 171 LYS C C 178.98 0.05 1 829 172 ALA N N 124.12 0.05 1 830 172 ALA H H 8.56 0.01 1 831 172 ALA CA C 55.56 0.05 1 832 172 ALA CB C 16.76 0.05 1 833 172 ALA C C 178.68 0.05 1 834 173 ASP N N 117.62 0.05 1 835 173 ASP H H 8.86 0.01 1 836 173 ASP CA C 57.46 0.05 1 837 173 ASP CB C 39.76 0.05 1 838 173 ASP C C 179.68 0.05 1 839 174 GLN N N 119.32 0.05 1 840 174 GLN H H 8.27 0.01 1 841 174 GLN CA C 58.86 0.05 1 842 174 GLN CB C 28.66 0.05 1 843 174 GLN C C 178.78 0.05 1 844 175 LEU N N 120.22 0.05 1 845 175 LEU H H 8.20 0.01 1 846 175 LEU CA C 57.96 0.05 1 847 175 LEU CB C 42.16 0.05 1 848 175 LEU C C 179.88 0.05 1 849 176 ALA N N 120.72 0.05 1 850 176 ALA H H 8.25 0.01 1 851 176 ALA CA C 55.16 0.05 1 852 176 ALA CB C 18.56 0.05 1 853 176 ALA C C 178.98 0.05 1 854 177 GLU N N 119.02 0.05 1 855 177 GLU H H 8.59 0.01 1 856 177 GLU CA C 59.46 0.05 1 857 177 GLU CB C 29.46 0.05 1 858 177 GLU C C 179.08 0.05 1 859 178 LYS N N 117.92 0.05 1 860 178 LYS H H 8.24 0.01 1 861 178 LYS CA C 59.06 0.05 1 862 178 LYS CB C 32.06 0.05 1 863 178 LYS C C 179.48 0.05 1 864 179 LYS N N 119.22 0.05 1 865 179 LYS H H 7.90 0.01 1 866 179 LYS CA C 56.56 0.05 1 867 179 LYS CB C 30.16 0.05 1 868 179 LYS C C 178.48 0.05 1 869 180 GLU N N 119.02 0.05 1 870 180 GLU H H 8.70 0.01 1 871 180 GLU CA C 61.16 0.05 1 872 180 GLU CB C 29.16 0.05 1 873 180 GLU C C 178.28 0.05 1 874 181 GLN N N 115.92 0.05 1 875 181 GLN H H 8.26 0.01 1 876 181 GLN CA C 58.76 0.05 1 877 181 GLN CB C 27.86 0.05 1 878 181 GLN C C 178.98 0.05 1 879 182 GLU N N 119.22 0.05 1 880 182 GLU H H 7.92 0.01 1 881 182 GLU CA C 58.86 0.05 1 882 182 GLU CB C 30.16 0.05 1 883 182 GLU C C 178.88 0.05 1 884 183 ILE N N 118.92 0.05 1 885 183 ILE H H 8.01 0.01 1 886 183 ILE CA C 64.66 0.05 1 887 183 ILE CB C 38.66 0.05 1 888 183 ILE C C 176.58 0.05 1 889 184 LEU N N 117.32 0.05 1 890 184 LEU H H 8.14 0.01 1 891 184 LEU CA C 55.96 0.05 1 892 184 LEU CB C 42.36 0.05 1 893 184 LEU C C 177.28 0.05 1 894 185 GLY N N 112.62 0.05 1 895 185 GLY H H 7.72 0.01 1 896 185 GLY CA C 46.46 0.05 1 897 185 GLY C C 178.88 0.05 1 stop_ save_ ####################################### # Cited references within the entry # ####################################### save_ref_1 _Saveframe_category citation _MEDLINE_UI_code 12086623 _Citation_full ; Ito K, Fujiwara T, Toyoda T, Nakamura Y. Elongation Factor G Paricipates in Ribosome Disassembly by Interacting with Ribosome Recycling Factor at Their tRNA-Mimicry Domains. Mol Cell. 2002 Jun;9(6):1263-72 ; save_ save_ref_2 _Saveframe_category citation _MEDLINE_UI_code 11214182 _Citation_full ; Fujiwara T, Ito K, Nakamura Y. Functional mapping of ribosome-contact sites in the ribosome recycling factor: a structural view from a tRNA mimic. RNA. 2001 Jan;7(1):64-70 ; save_ save_ref_3 _Saveframe_category citation _MEDLINE_UI_code 11073219 _Citation_full ; Toyoda T, Tin OF, Ito K, Fujiwara T, Kumasaka T, Yamamoto M, Garber MB, Nakamura Y. Crystal structure combined with genetic analysis of the Thermus thermophilus ribosome recycling factor shows that a flexible hinge may act as a functional switch. RNA. 2000 Oct;6(10):1432-44 ; save_