data_5793 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Backbone 1H, 15N, 13C and side chain 13Cb assignment of a 42 kDa RecR homodimer ; _BMRB_accession_number 5793 _BMRB_flat_file_name bmr5793.str _Entry_type original _Submission_date 2003-05-07 _Accession_date 2003-05-07 _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 Honda Masayoshi . . 2 Ito Yutaka . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 177 "13C chemical shifts" 549 "15N chemical shifts" 177 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2004-02-11 original author . stop_ _Original_release_date 2004-02-11 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title 'Letter to the Editor: Backbone 1H, 13C, 15N assignments of a 42 kDa RecR homodimer' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID ? loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Honda Masayoshi . . 2 Rajesh Sundaresan . . 3 Nietlispach Daniel . . 4 Mikawa Tsutomu . . 5 Shibata Takehiko . . 6 Ito Yutaka . . stop_ _Journal_abbreviation 'J. Biomol. NMR' _Journal_volume 28 _Journal_issue 2 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 199 _Page_last 200 _Year 2004 _Details . save_ ################################## # Molecular system description # ################################## save_system_RecR _Saveframe_category molecular_system _Mol_system_name 'RecR dimer' _Abbreviation_common RecR _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'RecR subunit 1' $RecR_monomer 'RecR subunit 2' $RecR_monomer stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state dimer _System_paramagnetic no _System_thiol_state 'not reported' loop_ _Magnetic_equivalence_ID _Magnetically_equivalent_system_component 1 'RecR subunit 1' 1 'RecR subunit 2' stop_ _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_RecR_monomer _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'Thermus thermophilus HB8 RecR' _Abbreviation_common ttRecR _Molecular_mass 21192.5 _Mol_thiol_state 'not reported' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 194 _Mol_residue_sequence ; MRYPESLLKLTRALSRLPGI GPKTAQRLALHLAFHKEEAE ALAEALEGIKRVRACRECGN LAEGELCPICQDEDRDRSLL AVVESVADLYALERSGEFRG LYHVLGGALNPLEGIGPKEL NLEGLFRRLEGVEEVVLATS MTVEGEATALYLAEELKKRG VRVTRPAYGLPVGGSLEYAD EVTLGRALEGRRPV ; loop_ _Residue_seq_code _Residue_label 1 MET 2 ARG 3 TYR 4 PRO 5 GLU 6 SER 7 LEU 8 LEU 9 LYS 10 LEU 11 THR 12 ARG 13 ALA 14 LEU 15 SER 16 ARG 17 LEU 18 PRO 19 GLY 20 ILE 21 GLY 22 PRO 23 LYS 24 THR 25 ALA 26 GLN 27 ARG 28 LEU 29 ALA 30 LEU 31 HIS 32 LEU 33 ALA 34 PHE 35 HIS 36 LYS 37 GLU 38 GLU 39 ALA 40 GLU 41 ALA 42 LEU 43 ALA 44 GLU 45 ALA 46 LEU 47 GLU 48 GLY 49 ILE 50 LYS 51 ARG 52 VAL 53 ARG 54 ALA 55 CYS 56 ARG 57 GLU 58 CYS 59 GLY 60 ASN 61 LEU 62 ALA 63 GLU 64 GLY 65 GLU 66 LEU 67 CYS 68 PRO 69 ILE 70 CYS 71 GLN 72 ASP 73 GLU 74 ASP 75 ARG 76 ASP 77 ARG 78 SER 79 LEU 80 LEU 81 ALA 82 VAL 83 VAL 84 GLU 85 SER 86 VAL 87 ALA 88 ASP 89 LEU 90 TYR 91 ALA 92 LEU 93 GLU 94 ARG 95 SER 96 GLY 97 GLU 98 PHE 99 ARG 100 GLY 101 LEU 102 TYR 103 HIS 104 VAL 105 LEU 106 GLY 107 GLY 108 ALA 109 LEU 110 ASN 111 PRO 112 LEU 113 GLU 114 GLY 115 ILE 116 GLY 117 PRO 118 LYS 119 GLU 120 LEU 121 ASN 122 LEU 123 GLU 124 GLY 125 LEU 126 PHE 127 ARG 128 ARG 129 LEU 130 GLU 131 GLY 132 VAL 133 GLU 134 GLU 135 VAL 136 VAL 137 LEU 138 ALA 139 THR 140 SER 141 MET 142 THR 143 VAL 144 GLU 145 GLY 146 GLU 147 ALA 148 THR 149 ALA 150 LEU 151 TYR 152 LEU 153 ALA 154 GLU 155 GLU 156 LEU 157 LYS 158 LYS 159 ARG 160 GLY 161 VAL 162 ARG 163 VAL 164 THR 165 ARG 166 PRO 167 ALA 168 TYR 169 GLY 170 LEU 171 PRO 172 VAL 173 GLY 174 GLY 175 SER 176 LEU 177 GLU 178 TYR 179 ALA 180 ASP 181 GLU 182 VAL 183 THR 184 LEU 185 GLY 186 ARG 187 ALA 188 LEU 189 GLU 190 GLY 191 ARG 192 ARG 193 PRO 194 VAL stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2014-11-16 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 DBJ BAD71423 "RecR protein [Thermus thermophilus HB8]" 100.00 194 100.00 100.00 3.19e-130 GB AAS81578 "recombination protein recR [Thermus thermophilus HB27]" 100.00 194 99.48 100.00 1.11e-129 GB AEG34015 "recombination protein RecR [Thermus thermophilus SG0.5JP17-16]" 100.00 194 99.48 100.00 1.11e-129 GB AFH38354 "recombination protein RecR [Thermus thermophilus JL-18]" 100.00 194 98.97 100.00 2.57e-129 GB EIA38760 "recombination protein RecR [Thermus sp. RL]" 100.00 194 99.48 100.00 1.11e-129 REF WP_008633233 "MULTISPECIES: recombinase RecR [Thermus]" 100.00 194 99.48 100.00 1.11e-129 REF WP_011228798 "recombinase RecR [Thermus thermophilus]" 100.00 194 100.00 100.00 3.19e-130 REF WP_014629118 "recombinase RecR [Thermus thermophilus]" 100.00 194 98.97 100.00 2.57e-129 REF YP_005205 "recombination protein RecR [Thermus thermophilus HB27]" 100.00 194 99.48 100.00 1.11e-129 REF YP_005641142 "recombination protein RecR [Thermus thermophilus SG0.5JP17-16]" 100.00 194 99.48 100.00 1.11e-129 SP Q5SHY0 "RecName: Full=Recombination protein RecR [Thermus thermophilus HB8]" 100.00 194 100.00 100.00 3.19e-130 SP Q72I96 "RecName: Full=Recombination protein RecR [Thermus thermophilus HB27]" 100.00 194 99.48 100.00 1.11e-129 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 $RecR_monomer 'Thermus thermophilus' 274 Eubacteria . 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 $RecR_monomer '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 $RecR_monomer 0.6 mM '[U-98% 2H; U-98% 13C; U-98% 15N]' stop_ save_ ############################ # Computer software used # ############################ save_AZARA _Saveframe_category software _Name AZARA _Version 2.7 loop_ _Task 'data processing' stop_ _Details . save_ save_ANSIG_for_OpenGL _Saveframe_category software _Name 'ANSIG for OpenGL' _Version 1.0.5 loop_ _Task 'peak assignments' stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer _Saveframe_category NMR_spectrometer _Manufacturer BRUKER _Model DRX _Field_strength 600 _Details . save_ ############################# # NMR applied experiments # ############################# save_1H-15N_HSQC_1 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-15N HSQC' _Sample_label . save_ save_3D_HNCA_2 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCA' _Sample_label . save_ save_3D_HN(CO)CA_3 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HN(CO)CA' _Sample_label . save_ save_3D_HN(CA)CB_4 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HN(CA)CB' _Sample_label . save_ save_3D_HN(COCA)CB_5 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HN(COCA)CB' _Sample_label . save_ save_3D_HN(CA)CO_6 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HN(CA)CO' _Sample_label . save_ save_3D_HNCO_7 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCO' _Sample_label . save_ save_NMR_spec_expt__0_1 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-15N HSQC' _BMRB_pulse_sequence_accession_number . _Details 'All 3D experiments for backbone assignments are TROSY versions.' save_ save_NMR_spec_expt__0_2 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCA' _BMRB_pulse_sequence_accession_number . _Details 'All 3D experiments for backbone assignments are TROSY versions.' save_ save_NMR_spec_expt__0_3 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HN(CO)CA' _BMRB_pulse_sequence_accession_number . _Details 'All 3D experiments for backbone assignments are TROSY versions.' save_ save_NMR_spec_expt__0_4 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HN(CA)CB' _BMRB_pulse_sequence_accession_number . _Details 'All 3D experiments for backbone assignments are TROSY versions.' save_ save_NMR_spec_expt__0_5 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HN(COCA)CB' _BMRB_pulse_sequence_accession_number . _Details 'All 3D experiments for backbone assignments are TROSY versions.' save_ save_NMR_spec_expt__0_6 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HN(CA)CO' _BMRB_pulse_sequence_accession_number . _Details 'All 3D experiments for backbone assignments are TROSY versions.' save_ save_NMR_spec_expt__0_7 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCO' _BMRB_pulse_sequence_accession_number . _Details 'All 3D experiments for backbone assignments are TROSY versions.' save_ ####################### # Sample conditions # ####################### save_cond_set_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 7.2 0.2 na temperature 318 1 K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference _Saveframe_category chemical_shift_reference _Details . loop_ _Mol_common_name _Atom_type _Atom_isotope_number _Atom_group _Chem_shift_units _Chem_shift_value _Reference_method _Reference_type _External_reference_sample_geometry _External_reference_location _External_reference_axis _Indirect_shift_ratio DSS C 13 'methyl protons' ppm 0.0 . indirect . . . 0.251449530 DSS H 1 'methyl protons' ppm 0.0 internal direct . . . 1.000000000 DSS N 15 'methyl protons' ppm 0.0 . 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_shift_set_1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Experiment_label '1H-15N HSQC' '3D HNCA' '3D HN(CO)CA' '3D HN(CA)CB' '3D HN(COCA)CB' '3D HN(CA)CO' '3D HNCO' stop_ loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $cond_set_1 _Chem_shift_reference_set_label $chemical_shift_reference _Mol_system_component_name 'RecR subunit 1' _Text_data_format . _Text_data . loop_ _Atom_shift_assign_ID _Residue_author_seq_code _Residue_seq_code _Residue_label _Atom_name _Atom_type _Chem_shift_value _Chem_shift_value_error _Chem_shift_ambiguity_code 1 . 2 ARG CA C 54.97 0.025 1 2 . 2 ARG C C 174.65 0.025 1 3 . 2 ARG CB C 30.14 0.025 1 4 . 3 TYR H H 7.97 0.025 1 5 . 3 TYR N N 123.86 0.025 1 6 . 3 TYR CA C 55.07 0.025 1 7 . 3 TYR C C 174.06 0.025 1 8 . 3 TYR CB C 38.62 0.025 1 9 . 4 PRO CA C 62.62 0.025 1 10 . 4 PRO C C 177.61 0.025 1 11 . 4 PRO CB C 30.60 0.025 1 12 . 5 GLU H H 9.03 0.025 1 13 . 5 GLU N N 131.12 0.025 1 14 . 5 GLU CA C 59.72 0.025 1 15 . 5 GLU C C 178.95 0.025 1 16 . 5 GLU CB C 28.75 0.025 1 17 . 6 SER CA C 61.45 0.025 1 18 . 6 SER C C 177.92 0.025 1 19 . 7 LEU H H 6.75 0.025 1 20 . 7 LEU N N 125.38 0.025 1 21 . 7 LEU CA C 56.71 0.025 1 22 . 7 LEU C C 179.45 0.025 1 23 . 7 LEU CB C 41.76 0.025 1 24 . 8 LEU H H 7.72 0.025 1 25 . 8 LEU N N 125.96 0.025 1 26 . 8 LEU CA C 57.74 0.025 1 27 . 8 LEU C C 179.12 0.025 1 28 . 8 LEU CB C 40.12 0.025 1 29 . 9 LYS H H 8.25 0.025 1 30 . 9 LYS N N 121.39 0.025 1 31 . 9 LYS CA C 59.72 0.025 1 32 . 9 LYS C C 179.66 0.025 1 33 . 9 LYS CB C 31.39 0.025 1 34 . 10 LEU H H 7.26 0.025 1 35 . 10 LEU N N 121.99 0.025 1 36 . 10 LEU CA C 57.24 0.025 1 37 . 10 LEU C C 177.23 0.025 1 38 . 10 LEU CB C 40.56 0.025 1 39 . 11 THR H H 8.21 0.025 1 40 . 11 THR N N 118.87 0.025 1 41 . 11 THR CA C 67.26 0.025 1 42 . 11 THR C C 176.88 0.025 1 43 . 12 ARG H H 8.17 0.025 1 44 . 12 ARG N N 123.70 0.025 1 45 . 12 ARG CA C 59.23 0.025 1 46 . 12 ARG C C 178.69 0.025 1 47 . 12 ARG CB C 29.11 0.025 1 48 . 13 ALA H H 7.46 0.025 1 49 . 13 ALA N N 123.02 0.025 1 50 . 13 ALA CA C 54.56 0.025 1 51 . 13 ALA C C 180.26 0.025 1 52 . 13 ALA CB C 17.12 0.025 1 53 . 14 LEU H H 7.85 0.025 1 54 . 14 LEU N N 118.97 0.025 1 55 . 14 LEU CA C 57.02 0.025 1 56 . 14 LEU C C 178.04 0.025 1 57 . 14 LEU CB C 41.81 0.025 1 58 . 15 SER H H 7.76 0.025 1 59 . 15 SER N N 113.78 0.025 1 60 . 15 SER CA C 60.34 0.025 1 61 . 15 SER C C 174.42 0.025 1 62 . 15 SER CB C 62.51 0.025 1 63 . 16 ARG H H 6.75 0.025 1 64 . 16 ARG N N 119.62 0.025 1 65 . 16 ARG CA C 55.85 0.025 1 66 . 16 ARG C C 176.81 0.025 1 67 . 16 ARG CB C 29.89 0.025 1 68 . 17 LEU H H 7.25 0.025 1 69 . 17 LEU N N 123.45 0.025 1 70 . 17 LEU CA C 52.27 0.025 1 71 . 17 LEU C C 174.47 0.025 1 72 . 17 LEU CB C 38.62 0.025 1 73 . 18 PRO CA C 63.05 0.025 1 74 . 18 PRO C C 177.11 0.025 1 75 . 18 PRO CB C 30.33 0.025 1 76 . 19 GLY H H 8.15 0.025 1 77 . 19 GLY N N 111.98 0.025 1 78 . 19 GLY CA C 44.85 0.025 1 79 . 19 GLY C C 174.19 0.025 1 80 . 20 ILE H H 7.24 0.025 1 81 . 20 ILE N N 123.97 0.025 1 82 . 20 ILE CA C 59.41 0.025 1 83 . 20 ILE C C 175.46 0.025 1 84 . 20 ILE CB C 34.03 0.025 1 85 . 21 GLY H H 7.67 0.025 1 86 . 21 GLY N N 112.68 0.025 1 87 . 21 GLY CA C 44.32 0.025 1 88 . 21 GLY C C 172.51 0.025 1 89 . 24 THR H H 7.09 0.025 1 90 . 24 THR N N 110.72 0.025 1 91 . 24 THR CA C 65.61 0.025 1 92 . 24 THR C C 175.94 0.025 1 93 . 24 THR CB C 67.60 0.025 1 94 . 25 ALA H H 8.35 0.025 1 95 . 25 ALA N N 125.27 0.025 1 96 . 25 ALA CA C 55.48 0.025 1 97 . 25 ALA C C 178.55 0.025 1 98 . 25 ALA CB C 18.52 0.025 1 99 . 26 GLN H H 7.36 0.025 1 100 . 26 GLN N N 118.05 0.025 1 101 . 26 GLN CA C 58.64 0.025 1 102 . 26 GLN C C 177.88 0.025 1 103 . 26 GLN CB C 28.20 0.025 1 104 . 27 ARG H H 7.37 0.025 1 105 . 27 ARG N N 121.71 0.025 1 106 . 27 ARG CA C 59.09 0.025 1 107 . 27 ARG C C 180.08 0.025 1 108 . 27 ARG CB C 29.20 0.025 1 109 . 28 LEU H H 8.41 0.025 1 110 . 28 LEU N N 122.47 0.025 1 111 . 28 LEU CA C 57.10 0.025 1 112 . 28 LEU C C 178.27 0.025 1 113 . 28 LEU CB C 41.83 0.025 1 114 . 29 ALA H H 8.21 0.025 1 115 . 29 ALA N N 124.80 0.025 1 116 . 29 ALA CA C 55.08 0.025 1 117 . 29 ALA C C 178.78 0.025 1 118 . 29 ALA CB C 18.18 0.025 1 119 . 30 LEU H H 7.49 0.025 1 120 . 30 LEU N N 118.47 0.025 1 121 . 30 LEU CA C 57.35 0.025 1 122 . 30 LEU C C 178.53 0.025 1 123 . 30 LEU CB C 40.96 0.025 1 124 . 31 HIS H H 7.82 0.025 1 125 . 31 HIS N N 120.22 0.025 1 126 . 31 HIS CA C 60.90 0.025 1 127 . 31 HIS C C 179.61 0.025 1 128 . 31 HIS CB C 30.61 0.025 1 129 . 32 LEU H H 8.32 0.025 1 130 . 32 LEU N N 122.26 0.025 1 131 . 32 LEU CA C 57.57 0.025 1 132 . 32 LEU C C 176.81 0.025 1 133 . 32 LEU CB C 41.24 0.025 1 134 . 33 ALA H H 7.64 0.025 1 135 . 33 ALA N N 120.52 0.025 1 136 . 33 ALA CA C 54.01 0.025 1 137 . 33 ALA C C 177.99 0.025 1 138 . 33 ALA CB C 17.53 0.025 1 139 . 34 PHE H H 7.12 0.025 1 140 . 34 PHE N N 114.43 0.025 1 141 . 34 PHE CA C 57.97 0.025 1 142 . 34 PHE C C 175.60 0.025 1 143 . 34 PHE CB C 39.31 0.025 1 144 . 35 HIS H H 7.60 0.025 1 145 . 35 HIS N N 123.65 0.025 1 146 . 35 HIS CA C 54.75 0.025 1 147 . 35 HIS C C 174.83 0.025 1 148 . 35 HIS CB C 26.32 0.025 1 149 . 36 LYS H H 8.05 0.025 1 150 . 36 LYS N N 124.91 0.025 1 151 . 36 LYS CA C 59.28 0.025 1 152 . 36 LYS C C 178.94 0.025 1 153 . 36 LYS CB C 31.36 0.025 1 154 . 37 GLU H H 9.17 0.025 1 155 . 37 GLU N N 121.89 0.025 1 156 . 37 GLU CA C 59.50 0.025 1 157 . 37 GLU C C 180.06 0.025 1 158 . 37 GLU CB C 27.46 0.025 1 159 . 38 GLU H H 7.63 0.025 1 160 . 38 GLU N N 123.51 0.025 1 161 . 38 GLU CA C 58.75 0.025 1 162 . 38 GLU C C 179.46 0.025 1 163 . 38 GLU CB C 28.34 0.025 1 164 . 39 ALA H H 7.65 0.025 1 165 . 39 ALA N N 125.41 0.025 1 166 . 39 ALA CA C 55.31 0.025 1 167 . 39 ALA C C 179.29 0.025 1 168 . 39 ALA CB C 17.14 0.025 1 169 . 40 GLU H H 8.26 0.025 1 170 . 40 GLU N N 120.49 0.025 1 171 . 40 GLU CA C 58.86 0.025 1 172 . 40 GLU C C 179.18 0.025 1 173 . 40 GLU CB C 28.70 0.025 1 174 . 41 ALA H H 7.60 0.025 1 175 . 41 ALA N N 124.17 0.025 1 176 . 41 ALA CA C 54.44 0.025 1 177 . 41 ALA C C 181.42 0.025 1 178 . 41 ALA CB C 17.28 0.025 1 179 . 42 LEU H H 7.85 0.025 1 180 . 42 LEU N N 123.14 0.025 1 181 . 42 LEU CA C 57.34 0.025 1 182 . 42 LEU C C 177.52 0.025 1 183 . 42 LEU CB C 40.09 0.025 1 184 . 43 ALA H H 8.30 0.025 1 185 . 43 ALA N N 124.86 0.025 1 186 . 43 ALA CA C 55.54 0.025 1 187 . 43 ALA C C 180.64 0.025 1 188 . 43 ALA CB C 17.23 0.025 1 189 . 44 GLU H H 8.13 0.025 1 190 . 44 GLU N N 121.45 0.025 1 191 . 44 GLU CA C 58.97 0.025 1 192 . 44 GLU C C 179.66 0.025 1 193 . 44 GLU CB C 28.68 0.025 1 194 . 45 ALA H H 7.72 0.025 1 195 . 45 ALA N N 124.39 0.025 1 196 . 45 ALA CA C 53.64 0.025 1 197 . 45 ALA C C 180.88 0.025 1 198 . 45 ALA CB C 17.40 0.025 1 199 . 46 LEU H H 8.30 0.025 1 200 . 46 LEU N N 122.66 0.025 1 201 . 46 LEU CA C 57.03 0.025 1 202 . 46 LEU C C 178.97 0.025 1 203 . 46 LEU CB C 40.55 0.025 1 204 . 47 GLU H H 7.60 0.025 1 205 . 47 GLU N N 122.82 0.025 1 206 . 47 GLU CA C 58.63 0.025 1 207 . 47 GLU C C 179.97 0.025 1 208 . 47 GLU CB C 27.95 0.025 1 209 . 48 GLY H H 7.51 0.025 1 210 . 48 GLY N N 106.78 0.025 1 211 . 48 GLY CA C 46.55 0.025 1 212 . 48 GLY C C 176.30 0.025 1 213 . 49 ILE H H 7.26 0.025 1 214 . 49 ILE N N 119.48 0.025 1 215 . 49 ILE CA C 60.14 0.025 1 216 . 49 ILE C C 176.95 0.025 1 217 . 49 ILE CB C 37.94 0.025 1 218 . 50 LYS H H 7.20 0.025 1 219 . 50 LYS N N 123.07 0.025 1 220 . 50 LYS CA C 58.96 0.025 1 221 . 50 LYS C C 177.50 0.025 1 222 . 50 LYS CB C 31.63 0.025 1 223 . 51 ARG H H 7.26 0.025 1 224 . 51 ARG N N 116.98 0.025 1 225 . 51 ARG CA C 56.04 0.025 1 226 . 51 ARG C C 176.73 0.025 1 227 . 51 ARG CB C 29.89 0.025 1 228 . 52 VAL H H 7.07 0.025 1 229 . 52 VAL N N 119.27 0.025 1 230 . 52 VAL CA C 61.91 0.025 1 231 . 52 VAL C C 175.13 0.025 1 232 . 52 VAL CB C 31.28 0.025 1 233 . 53 ARG H H 8.77 0.025 1 234 . 53 ARG N N 125.23 0.025 1 235 . 53 ARG CA C 53.83 0.025 1 236 . 53 ARG C C 173.94 0.025 1 237 . 53 ARG CB C 31.66 0.025 1 238 . 54 ALA H H 8.02 0.025 1 239 . 54 ALA N N 123.98 0.025 1 240 . 54 ALA CA C 51.15 0.025 1 241 . 54 ALA C C 177.48 0.025 1 242 . 54 ALA CB C 18.58 0.025 1 243 . 55 CYS H H 9.36 0.025 1 244 . 55 CYS N N 128.72 0.025 1 245 . 55 CYS CA C 59.09 0.025 1 246 . 55 CYS C C 177.30 0.025 1 247 . 55 CYS CB C 30.91 0.025 1 248 . 56 ARG H H 8.86 0.025 1 249 . 56 ARG N N 132.50 0.025 1 250 . 56 ARG CA C 58.33 0.025 1 251 . 56 ARG C C 176.36 0.025 1 252 . 56 ARG CB C 29.30 0.025 1 253 . 57 GLU H H 8.47 0.025 1 254 . 57 GLU N N 121.43 0.025 1 255 . 57 GLU CA C 57.58 0.025 1 256 . 57 GLU C C 178.18 0.025 1 257 . 57 GLU CB C 30.67 0.025 1 258 . 58 CYS H H 7.74 0.025 1 259 . 58 CYS N N 118.90 0.025 1 260 . 58 CYS CA C 58.76 0.025 1 261 . 58 CYS C C 175.61 0.025 1 262 . 58 CYS CB C 35.64 0.025 1 263 . 59 GLY H H 7.52 0.025 1 264 . 59 GLY N N 111.87 0.025 1 265 . 59 GLY CA C 45.58 0.025 1 266 . 59 GLY C C 172.80 0.025 1 267 . 60 ASN H H 9.06 0.025 1 268 . 60 ASN N N 122.03 0.025 1 269 . 60 ASN CA C 52.28 0.025 1 270 . 60 ASN C C 174.85 0.025 1 271 . 60 ASN CB C 40.34 0.025 1 272 . 61 LEU H H 7.31 0.025 1 273 . 61 LEU N N 126.94 0.025 1 274 . 61 LEU CA C 56.50 0.025 1 275 . 61 LEU C C 175.89 0.025 1 276 . 61 LEU CB C 41.60 0.025 1 277 . 62 ALA H H 8.88 0.025 1 278 . 62 ALA N N 127.69 0.025 1 279 . 62 ALA CA C 50.51 0.025 1 280 . 62 ALA C C 175.61 0.025 1 281 . 62 ALA CB C 21.86 0.025 1 282 . 63 GLU H H 8.84 0.025 1 283 . 63 GLU N N 123.23 0.025 1 284 . 63 GLU CA C 55.09 0.025 1 285 . 63 GLU C C 176.13 0.025 1 286 . 63 GLU CB C 29.24 0.025 1 287 . 64 GLY H H 7.03 0.025 1 288 . 64 GLY N N 111.11 0.025 1 289 . 64 GLY CA C 43.88 0.025 1 290 . 64 GLY C C 171.83 0.025 1 291 . 65 GLU H H 8.05 0.025 1 292 . 65 GLU N N 120.44 0.025 1 293 . 65 GLU CA C 59.03 0.025 1 294 . 65 GLU C C 175.76 0.025 1 295 . 65 GLU CB C 29.98 0.025 1 296 . 66 LEU H H 7.39 0.025 1 297 . 66 LEU N N 116.31 0.025 1 298 . 66 LEU CA C 51.92 0.025 1 299 . 66 LEU C C 177.76 0.025 1 300 . 66 LEU CB C 45.40 0.025 1 301 . 67 CYS H H 9.20 0.025 1 302 . 67 CYS N N 126.31 0.025 1 303 . 67 CYS CA C 57.12 0.025 1 304 . 67 CYS C C 173.20 0.025 1 305 . 67 CYS CB C 29.12 0.025 1 306 . 68 PRO CA C 64.37 0.025 1 307 . 68 PRO C C 178.48 0.025 1 308 . 68 PRO CB C 31.81 0.025 1 309 . 69 ILE H H 7.62 0.025 1 310 . 69 ILE N N 120.35 0.025 1 311 . 69 ILE CA C 63.61 0.025 1 312 . 69 ILE C C 177.88 0.025 1 313 . 69 ILE CB C 36.19 0.025 1 314 . 70 CYS H H 8.26 0.025 1 315 . 70 CYS N N 124.69 0.025 1 316 . 70 CYS CA C 64.79 0.025 1 317 . 70 CYS C C 177.58 0.025 1 318 . 70 CYS CB C 29.28 0.025 1 319 . 71 GLN H H 7.29 0.025 1 320 . 71 GLN N N 115.89 0.025 1 321 . 71 GLN CA C 56.07 0.025 1 322 . 71 GLN C C 175.37 0.025 1 323 . 71 GLN CB C 29.98 0.025 1 324 . 72 ASP H H 7.03 0.025 1 325 . 72 ASP N N 122.80 0.025 1 326 . 72 ASP CA C 54.08 0.025 1 327 . 72 ASP C C 177.39 0.025 1 328 . 72 ASP CB C 40.67 0.025 1 329 . 73 GLU H H 8.71 0.025 1 330 . 73 GLU N N 130.06 0.025 1 331 . 73 GLU CA C 57.77 0.025 1 332 . 73 GLU C C 176.75 0.025 1 333 . 73 GLU CB C 28.85 0.025 1 334 . 74 ASP H H 8.48 0.025 1 335 . 74 ASP N N 121.56 0.025 1 336 . 74 ASP CA C 54.10 0.025 1 337 . 74 ASP C C 176.81 0.025 1 338 . 74 ASP CB C 40.61 0.025 1 339 . 75 ARG H H 6.80 0.025 1 340 . 75 ARG N N 119.13 0.025 1 341 . 75 ARG CA C 53.56 0.025 1 342 . 75 ARG C C 175.52 0.025 1 343 . 75 ARG CB C 28.40 0.025 1 344 . 76 ASP H H 8.26 0.025 1 345 . 76 ASP N N 122.86 0.025 1 346 . 76 ASP CA C 52.37 0.025 1 347 . 76 ASP C C 176.02 0.025 1 348 . 76 ASP CB C 39.38 0.025 1 349 . 77 ARG H H 7.94 0.025 1 350 . 77 ARG N N 124.94 0.025 1 351 . 77 ARG CA C 57.06 0.025 1 352 . 77 ARG C C 175.93 0.025 1 353 . 77 ARG CB C 27.77 0.025 1 354 . 78 SER H H 8.34 0.025 1 355 . 78 SER N N 116.74 0.025 1 356 . 78 SER CA C 58.97 0.025 1 357 . 78 SER C C 173.03 0.025 1 358 . 78 SER CB C 64.08 0.025 1 359 . 79 LEU H H 7.13 0.025 1 360 . 79 LEU N N 127.83 0.025 1 361 . 79 LEU CA C 53.48 0.025 1 362 . 79 LEU C C 174.42 0.025 1 363 . 79 LEU CB C 45.38 0.025 1 364 . 80 LEU H H 8.10 0.025 1 365 . 80 LEU N N 128.10 0.025 1 366 . 80 LEU CA C 52.91 0.025 1 367 . 80 LEU C C 174.57 0.025 1 368 . 80 LEU CB C 46.09 0.025 1 369 . 81 ALA H H 9.16 0.025 1 370 . 81 ALA N N 129.76 0.025 1 371 . 81 ALA CA C 49.77 0.025 1 372 . 81 ALA C C 175.94 0.025 1 373 . 81 ALA CB C 18.83 0.025 1 374 . 82 VAL H H 8.63 0.025 1 375 . 82 VAL N N 126.05 0.025 1 376 . 82 VAL CA C 61.11 0.025 1 377 . 82 VAL C C 174.57 0.025 1 378 . 82 VAL CB C 32.26 0.025 1 379 . 83 VAL H H 8.34 0.025 1 380 . 83 VAL N N 118.01 0.025 1 381 . 83 VAL CA C 57.24 0.025 1 382 . 83 VAL C C 176.19 0.025 1 383 . 83 VAL CB C 35.51 0.025 1 384 . 84 GLU H H 10.24 0.025 1 385 . 84 GLU N N 122.72 0.025 1 386 . 84 GLU CA C 59.51 0.025 1 387 . 84 GLU C C 177.72 0.025 1 388 . 84 GLU CB C 30.12 0.025 1 389 . 85 SER H H 7.08 0.025 1 390 . 85 SER N N 110.66 0.025 1 391 . 85 SER CA C 55.38 0.025 1 392 . 85 SER C C 174.38 0.025 1 393 . 85 SER CB C 67.36 0.025 1 394 . 86 VAL H H 8.59 0.025 1 395 . 86 VAL N N 124.07 0.025 1 396 . 86 VAL CA C 65.45 0.025 1 397 . 86 VAL C C 176.80 0.025 1 398 . 86 VAL CB C 30.70 0.025 1 399 . 87 ALA H H 7.85 0.025 1 400 . 87 ALA N N 123.74 0.025 1 401 . 87 ALA CA C 55.09 0.025 1 402 . 87 ALA C C 180.44 0.025 1 403 . 87 ALA CB C 17.05 0.025 1 404 . 88 ASP H H 7.45 0.025 1 405 . 88 ASP N N 122.63 0.025 1 406 . 88 ASP CA C 56.92 0.025 1 407 . 88 ASP C C 177.43 0.025 1 408 . 88 ASP CB C 39.86 0.025 1 409 . 89 LEU H H 7.25 0.025 1 410 . 89 LEU N N 125.47 0.025 1 411 . 89 LEU CA C 59.83 0.025 1 412 . 89 LEU C C 178.69 0.025 1 413 . 89 LEU CB C 40.74 0.025 1 414 . 90 TYR H H 8.27 0.025 1 415 . 90 TYR N N 120.32 0.025 1 416 . 90 TYR CA C 60.70 0.025 1 417 . 90 TYR C C 178.20 0.025 1 418 . 90 TYR CB C 36.22 0.025 1 419 . 91 ALA H H 7.46 0.025 1 420 . 91 ALA N N 124.34 0.025 1 421 . 91 ALA CA C 54.95 0.025 1 422 . 91 ALA C C 179.64 0.025 1 423 . 91 ALA CB C 17.55 0.025 1 424 . 92 LEU H H 7.74 0.025 1 425 . 92 LEU N N 120.71 0.025 1 426 . 92 LEU CA C 58.11 0.025 1 427 . 92 LEU C C 181.31 0.025 1 428 . 92 LEU CB C 40.79 0.025 1 429 . 93 GLU H H 8.89 0.025 1 430 . 93 GLU N N 125.97 0.025 1 431 . 93 GLU CA C 58.21 0.025 1 432 . 93 GLU C C 179.97 0.025 1 433 . 93 GLU CB C 28.45 0.025 1 434 . 94 ARG H H 8.14 0.025 1 435 . 94 ARG N N 121.55 0.025 1 436 . 94 ARG CA C 58.39 0.025 1 437 . 94 ARG C C 177.84 0.025 1 438 . 94 ARG CB C 29.81 0.025 1 439 . 95 SER H H 7.50 0.025 1 440 . 95 SER N N 116.20 0.025 1 441 . 95 SER CA C 61.09 0.025 1 442 . 95 SER C C 175.57 0.025 1 443 . 95 SER CB C 63.98 0.025 1 444 . 96 GLY H H 7.31 0.025 1 445 . 96 GLY N N 111.35 0.025 1 446 . 96 GLY CA C 45.93 0.025 1 447 . 96 GLY C C 174.72 0.025 1 448 . 97 GLU H H 7.48 0.025 1 449 . 97 GLU N N 119.94 0.025 1 450 . 97 GLU CA C 55.28 0.025 1 451 . 97 GLU C C 175.22 0.025 1 452 . 97 GLU CB C 29.89 0.025 1 453 . 98 PHE H H 8.33 0.025 1 454 . 98 PHE N N 122.95 0.025 1 455 . 98 PHE CA C 57.99 0.025 1 456 . 98 PHE C C 174.79 0.025 1 457 . 98 PHE CB C 40.83 0.025 1 458 . 99 ARG H H 8.03 0.025 1 459 . 99 ARG N N 127.13 0.025 1 460 . 99 ARG CA C 53.79 0.025 1 461 . 99 ARG C C 176.07 0.025 1 462 . 99 ARG CB C 29.47 0.025 1 463 . 100 GLY CA C 44.94 0.025 1 464 . 100 GLY C C 172.93 0.025 1 465 . 101 LEU H H 7.87 0.025 1 466 . 101 LEU N N 120.94 0.025 1 467 . 101 LEU CA C 52.67 0.025 1 468 . 101 LEU C C 175.72 0.025 1 469 . 101 LEU CB C 43.55 0.025 1 470 . 102 TYR H H 8.32 0.025 1 471 . 102 TYR N N 117.56 0.025 1 472 . 102 TYR CA C 56.90 0.025 1 473 . 102 TYR C C 177.16 0.025 1 474 . 102 TYR CB C 44.42 0.025 1 475 . 103 HIS H H 8.57 0.025 1 476 . 103 HIS N N 120.97 0.025 1 477 . 103 HIS CA C 58.83 0.025 1 478 . 103 HIS C C 173.48 0.025 1 479 . 103 HIS CB C 35.20 0.025 1 480 . 104 VAL H H 8.07 0.025 1 481 . 104 VAL N N 130.06 0.025 1 482 . 104 VAL CA C 61.12 0.025 1 483 . 104 VAL C C 176.43 0.025 1 484 . 104 VAL CB C 30.71 0.025 1 485 . 105 LEU H H 8.98 0.025 1 486 . 105 LEU N N 128.98 0.025 1 487 . 105 LEU CA C 56.60 0.025 1 488 . 105 LEU C C 177.63 0.025 1 489 . 105 LEU CB C 42.98 0.025 1 490 . 106 GLY H H 7.46 0.025 1 491 . 106 GLY N N 107.48 0.025 1 492 . 106 GLY CA C 44.86 0.025 1 493 . 106 GLY C C 173.76 0.025 1 494 . 107 GLY H H 7.48 0.025 1 495 . 107 GLY N N 110.47 0.025 1 496 . 107 GLY CA C 43.96 0.025 1 497 . 107 GLY C C 169.07 0.025 1 498 . 108 ALA H H 7.01 0.025 1 499 . 108 ALA N N 119.60 0.025 1 500 . 108 ALA CA C 49.77 0.025 1 501 . 108 ALA C C 176.40 0.025 1 502 . 108 ALA CB C 20.68 0.025 1 503 . 109 LEU H H 7.59 0.025 1 504 . 109 LEU N N 121.03 0.025 1 505 . 109 LEU CA C 55.30 0.025 1 506 . 109 LEU C C 176.84 0.025 1 507 . 109 LEU CB C 41.27 0.025 1 508 . 110 ASN H H 8.35 0.025 1 509 . 110 ASN N N 116.72 0.025 1 510 . 110 ASN CA C 50.70 0.025 1 511 . 110 ASN C C 174.03 0.025 1 512 . 110 ASN CB C 37.66 0.025 1 513 . 111 PRO CA C 64.28 0.025 1 514 . 111 PRO C C 179.19 0.025 1 515 . 111 PRO CB C 31.15 0.025 1 516 . 112 LEU H H 7.58 0.025 1 517 . 112 LEU N N 120.74 0.025 1 518 . 112 LEU CA C 56.82 0.025 1 519 . 112 LEU C C 178.47 0.025 1 520 . 112 LEU CB C 40.30 0.025 1 521 . 113 GLU H H 6.89 0.025 1 522 . 113 GLU N N 118.26 0.025 1 523 . 113 GLU CA C 54.77 0.025 1 524 . 113 GLU C C 176.28 0.025 1 525 . 113 GLU CB C 29.86 0.025 1 526 . 114 GLY H H 7.41 0.025 1 527 . 114 GLY N N 109.44 0.025 1 528 . 114 GLY CA C 45.70 0.025 1 529 . 114 GLY C C 174.06 0.025 1 530 . 115 ILE H H 7.42 0.025 1 531 . 115 ILE N N 122.84 0.025 1 532 . 115 ILE CA C 59.96 0.025 1 533 . 115 ILE C C 175.34 0.025 1 534 . 115 ILE CB C 36.19 0.025 1 535 . 116 GLY H H 8.92 0.025 1 536 . 116 GLY N N 121.06 0.025 1 537 . 116 GLY CA C 43.58 0.025 1 538 . 116 GLY C C 171.89 0.025 1 539 . 117 PRO CA C 65.13 0.025 1 540 . 117 PRO C C 178.48 0.025 1 541 . 117 PRO CB C 31.35 0.025 1 542 . 118 LYS H H 8.10 0.025 1 543 . 118 LYS N N 116.86 0.025 1 544 . 118 LYS CA C 57.68 0.025 1 545 . 118 LYS C C 177.98 0.025 1 546 . 118 LYS CB C 30.96 0.025 1 547 . 119 GLU H H 7.58 0.025 1 548 . 119 GLU N N 121.06 0.025 1 549 . 119 GLU CA C 58.53 0.025 1 550 . 119 GLU C C 176.55 0.025 1 551 . 119 GLU CB C 29.08 0.025 1 552 . 120 LEU H H 7.07 0.025 1 553 . 120 LEU N N 120.36 0.025 1 554 . 120 LEU CA C 53.05 0.025 1 555 . 120 LEU C C 176.47 0.025 1 556 . 120 LEU CB C 42.85 0.025 1 557 . 121 ASN H H 8.39 0.025 1 558 . 121 ASN N N 120.61 0.025 1 559 . 121 ASN CA C 52.27 0.025 1 560 . 121 ASN C C 176.44 0.025 1 561 . 121 ASN CB C 36.13 0.025 1 562 . 122 LEU H H 7.91 0.025 1 563 . 122 LEU N N 124.23 0.025 1 564 . 122 LEU CA C 56.40 0.025 1 565 . 122 LEU C C 177.98 0.025 1 566 . 122 LEU CB C 41.27 0.025 1 567 . 123 GLU H H 8.50 0.025 1 568 . 123 GLU N N 122.23 0.025 1 569 . 123 GLU CA C 59.57 0.025 1 570 . 123 GLU C C 179.49 0.025 1 571 . 123 GLU CB C 28.25 0.025 1 572 . 124 GLY H H 7.98 0.025 1 573 . 124 GLY N N 106.57 0.025 1 574 . 124 GLY CA C 46.13 0.025 1 575 . 124 GLY C C 175.01 0.025 1 576 . 125 LEU H H 6.66 0.025 1 577 . 125 LEU N N 123.51 0.025 1 578 . 125 LEU CA C 56.81 0.025 1 579 . 125 LEU C C 177.85 0.025 1 580 . 125 LEU CB C 39.58 0.025 1 581 . 126 PHE H H 7.01 0.025 1 582 . 126 PHE N N 116.19 0.025 1 583 . 126 PHE CA C 58.41 0.025 1 584 . 126 PHE C C 177.81 0.025 1 585 . 126 PHE CB C 36.47 0.025 1 586 . 127 ARG H H 7.30 0.025 1 587 . 127 ARG N N 118.46 0.025 1 588 . 127 ARG CA C 56.92 0.025 1 589 . 127 ARG C C 177.13 0.025 1 590 . 127 ARG CB C 29.19 0.025 1 591 . 128 ARG H H 7.29 0.025 1 592 . 128 ARG N N 122.01 0.025 1 593 . 128 ARG CA C 56.02 0.025 1 594 . 128 ARG C C 175.73 0.025 1 595 . 128 ARG CB C 29.86 0.025 1 596 . 129 LEU H H 6.91 0.025 1 597 . 129 LEU N N 116.62 0.025 1 598 . 129 LEU CA C 54.99 0.025 1 599 . 129 LEU C C 178.02 0.025 1 600 . 129 LEU CB C 40.62 0.025 1 601 . 130 GLU H H 7.69 0.025 1 602 . 130 GLU N N 125.16 0.025 1 603 . 130 GLU CA C 58.33 0.025 1 604 . 130 GLU C C 177.74 0.025 1 605 . 130 GLU CB C 27.98 0.025 1 606 . 131 GLY H H 8.60 0.025 1 607 . 131 GLY N N 117.30 0.025 1 608 . 131 GLY CA C 45.06 0.025 1 609 . 131 GLY C C 173.80 0.025 1 610 . 132 VAL H H 7.52 0.025 1 611 . 132 VAL N N 123.75 0.025 1 612 . 132 VAL CA C 62.96 0.025 1 613 . 132 VAL C C 175.50 0.025 1 614 . 132 VAL CB C 31.09 0.025 1 615 . 133 GLU H H 9.28 0.025 1 616 . 133 GLU N N 129.19 0.025 1 617 . 133 GLU CA C 56.28 0.025 1 618 . 133 GLU C C 176.30 0.025 1 619 . 133 GLU CB C 30.98 0.025 1 620 . 134 GLU H H 7.42 0.025 1 621 . 134 GLU N N 122.98 0.025 1 622 . 134 GLU CA C 54.54 0.025 1 623 . 134 GLU C C 173.34 0.025 1 624 . 134 GLU CB C 32.00 0.025 1 625 . 135 VAL H H 8.56 0.025 1 626 . 135 VAL N N 128.11 0.025 1 627 . 135 VAL CA C 59.38 0.025 1 628 . 135 VAL C C 174.51 0.025 1 629 . 135 VAL CB C 32.83 0.025 1 630 . 136 VAL H H 9.17 0.025 1 631 . 136 VAL N N 128.81 0.025 1 632 . 136 VAL CA C 59.49 0.025 1 633 . 136 VAL C C 176.38 0.025 1 634 . 136 VAL CB C 31.85 0.025 1 635 . 137 LEU H H 9.37 0.025 1 636 . 137 LEU N N 131.09 0.025 1 637 . 137 LEU CA C 52.80 0.025 1 638 . 137 LEU C C 174.58 0.025 1 639 . 137 LEU CB C 39.54 0.025 1 640 . 138 ALA H H 8.34 0.025 1 641 . 138 ALA N N 136.31 0.025 1 642 . 138 ALA CA C 50.37 0.025 1 643 . 138 ALA C C 176.39 0.025 1 644 . 138 ALA CB C 16.42 0.025 1 645 . 139 THR H H 6.25 0.025 1 646 . 139 THR N N 106.27 0.025 1 647 . 139 THR CA C 61.45 0.025 1 648 . 139 THR C C 174.99 0.025 1 649 . 139 THR CB C 67.88 0.025 1 650 . 140 SER H H 9.16 0.025 1 651 . 140 SER N N 120.16 0.025 1 652 . 140 SER CA C 59.59 0.025 1 653 . 140 SER C C 174.26 0.025 1 654 . 140 SER CB C 63.58 0.025 1 655 . 141 MET H H 8.02 0.025 1 656 . 141 MET N N 121.81 0.025 1 657 . 141 MET CA C 53.45 0.025 1 658 . 141 MET C C 176.91 0.025 1 659 . 141 MET CB C 30.00 0.025 1 660 . 142 THR H H 7.28 0.025 1 661 . 142 THR N N 112.21 0.025 1 662 . 142 THR CA C 59.85 0.025 1 663 . 142 THR C C 175.03 0.025 1 664 . 142 THR CB C 72.15 0.025 1 665 . 143 VAL H H 8.60 0.025 1 666 . 143 VAL N N 124.21 0.025 1 667 . 143 VAL CA C 66.48 0.025 1 668 . 143 VAL C C 179.41 0.025 1 669 . 143 VAL CB C 30.77 0.025 1 670 . 144 GLU H H 9.08 0.025 1 671 . 144 GLU N N 122.48 0.025 1 672 . 144 GLU CA C 59.74 0.025 1 673 . 144 GLU C C 180.79 0.025 1 674 . 144 GLU CB C 27.19 0.025 1 675 . 145 GLY H H 8.73 0.025 1 676 . 145 GLY N N 118.72 0.025 1 677 . 145 GLY CA C 47.64 0.025 1 678 . 145 GLY C C 178.84 0.025 1 679 . 146 GLU H H 8.76 0.025 1 680 . 146 GLU N N 128.74 0.025 1 681 . 146 GLU CA C 58.89 0.025 1 682 . 146 GLU C C 178.71 0.025 1 683 . 146 GLU CB C 28.72 0.025 1 684 . 147 ALA H H 8.12 0.025 1 685 . 147 ALA N N 124.77 0.025 1 686 . 147 ALA CA C 55.06 0.025 1 687 . 147 ALA C C 181.72 0.025 1 688 . 147 ALA CB C 17.34 0.025 1 689 . 148 THR H H 8.10 0.025 1 690 . 148 THR N N 117.77 0.025 1 691 . 148 THR CA C 67.18 0.025 1 692 . 148 THR C C 175.40 0.025 1 693 . 148 THR CB C 68.13 0.025 1 694 . 149 ALA H H 7.85 0.025 1 695 . 149 ALA N N 126.39 0.025 1 696 . 149 ALA CA C 55.32 0.025 1 697 . 149 ALA C C 178.87 0.025 1 698 . 149 ALA CB C 16.38 0.025 1 699 . 150 LEU H H 8.18 0.025 1 700 . 150 LEU N N 120.86 0.025 1 701 . 150 LEU CA C 58.08 0.025 1 702 . 150 LEU C C 179.70 0.025 1 703 . 150 LEU CB C 40.55 0.025 1 704 . 151 TYR H H 7.63 0.025 1 705 . 151 TYR N N 122.30 0.025 1 706 . 151 TYR CA C 60.79 0.025 1 707 . 151 TYR C C 177.95 0.025 1 708 . 151 TYR CB C 38.32 0.025 1 709 . 152 LEU H H 8.24 0.025 1 710 . 152 LEU N N 119.47 0.025 1 711 . 152 LEU CA C 57.02 0.025 1 712 . 152 LEU C C 178.72 0.025 1 713 . 152 LEU CB C 41.72 0.025 1 714 . 153 ALA H H 8.74 0.025 1 715 . 153 ALA N N 123.34 0.025 1 716 . 153 ALA CA C 55.63 0.025 1 717 . 153 ALA C C 179.01 0.025 1 718 . 153 ALA CB C 17.55 0.025 1 719 . 154 GLU H H 7.12 0.025 1 720 . 154 GLU N N 118.17 0.025 1 721 . 154 GLU CA C 58.85 0.025 1 722 . 154 GLU C C 179.54 0.025 1 723 . 154 GLU CB C 28.48 0.025 1 724 . 155 GLU H H 7.16 0.025 1 725 . 155 GLU N N 119.08 0.025 1 726 . 155 GLU CA C 58.00 0.025 1 727 . 155 GLU C C 179.57 0.025 1 728 . 155 GLU CB C 29.14 0.025 1 729 . 156 LEU H H 8.66 0.025 1 730 . 156 LEU N N 122.15 0.025 1 731 . 156 LEU CA C 57.39 0.025 1 732 . 156 LEU C C 179.60 0.025 1 733 . 156 LEU CB C 40.28 0.025 1 734 . 157 LYS H H 8.26 0.025 1 735 . 157 LYS N N 122.95 0.025 1 736 . 157 LYS CA C 60.01 0.025 1 737 . 157 LYS C C 181.29 0.025 1 738 . 157 LYS CB C 30.91 0.025 1 739 . 158 LYS H H 7.10 0.025 1 740 . 158 LYS N N 120.71 0.025 1 741 . 158 LYS CA C 58.53 0.025 1 742 . 158 LYS C C 177.70 0.025 1 743 . 158 LYS CB C 31.32 0.025 1 744 . 159 ARG H H 7.04 0.025 1 745 . 159 ARG N N 119.08 0.025 1 746 . 159 ARG CA C 55.21 0.025 1 747 . 159 ARG C C 176.50 0.025 1 748 . 159 ARG CB C 29.36 0.025 1 749 . 160 GLY H H 7.54 0.025 1 750 . 160 GLY N N 109.21 0.025 1 751 . 160 GLY CA C 45.82 0.025 1 752 . 160 GLY C C 173.96 0.025 1 753 . 161 VAL H H 6.90 0.025 1 754 . 161 VAL N N 119.33 0.025 1 755 . 161 VAL CA C 60.06 0.025 1 756 . 161 VAL C C 175.21 0.025 1 757 . 161 VAL CB C 32.70 0.025 1 758 . 162 ARG H H 7.57 0.025 1 759 . 162 ARG N N 127.37 0.025 1 760 . 162 ARG CA C 56.62 0.025 1 761 . 162 ARG C C 174.98 0.025 1 762 . 162 ARG CB C 29.83 0.025 1 763 . 163 VAL H H 8.00 0.025 1 764 . 163 VAL N N 123.40 0.025 1 765 . 163 VAL CA C 59.03 0.025 1 766 . 163 VAL C C 176.23 0.025 1 767 . 163 VAL CB C 33.66 0.025 1 768 . 164 THR H H 8.66 0.025 1 769 . 164 THR N N 117.76 0.025 1 770 . 164 THR CA C 58.97 0.025 1 771 . 164 THR C C 173.42 0.025 1 772 . 164 THR CB C 72.70 0.025 1 773 . 165 ARG H H 8.65 0.025 1 774 . 165 ARG N N 122.36 0.025 1 775 . 165 ARG CA C 51.65 0.025 1 776 . 165 ARG C C 174.25 0.025 1 777 . 165 ARG CB C 33.25 0.025 1 778 . 166 PRO CA C 62.30 0.025 1 779 . 166 PRO C C 173.97 0.025 1 780 . 166 PRO CB C 31.12 0.025 1 781 . 167 ALA H H 7.92 0.025 1 782 . 167 ALA N N 128.70 0.025 1 783 . 167 ALA CA C 50.26 0.025 1 784 . 167 ALA C C 176.30 0.025 1 785 . 167 ALA CB C 17.20 0.025 1 786 . 168 TYR H H 7.23 0.025 1 787 . 168 TYR N N 121.13 0.025 1 788 . 168 TYR CA C 58.29 0.025 1 789 . 168 TYR C C 176.74 0.025 1 790 . 168 TYR CB C 38.31 0.025 1 791 . 169 GLY CA C 45.07 0.025 1 792 . 169 GLY C C 173.76 0.025 1 793 . 170 LEU H H 7.28 0.025 1 794 . 170 LEU N N 123.36 0.025 1 795 . 170 LEU CA C 52.62 0.025 1 796 . 170 LEU C C 175.01 0.025 1 797 . 170 LEU CB C 41.09 0.025 1 798 . 171 PRO CA C 62.71 0.025 1 799 . 171 PRO C C 176.75 0.025 1 800 . 171 PRO CB C 30.83 0.025 1 801 . 172 VAL H H 7.71 0.025 1 802 . 172 VAL N N 122.07 0.025 1 803 . 172 VAL CA C 62.42 0.025 1 804 . 172 VAL C C 176.80 0.025 1 805 . 172 VAL CB C 31.23 0.025 1 806 . 173 GLY H H 8.11 0.025 1 807 . 173 GLY N N 114.74 0.025 1 808 . 173 GLY CA C 44.92 0.025 1 809 . 173 GLY C C 174.45 0.025 1 810 . 174 GLY H H 7.74 0.025 1 811 . 174 GLY N N 110.58 0.025 1 812 . 174 GLY CA C 44.97 0.025 1 813 . 174 GLY C C 172.97 0.025 1 814 . 175 SER H H 7.77 0.025 1 815 . 175 SER N N 117.69 0.025 1 816 . 175 SER CA C 57.55 0.025 1 817 . 175 SER C C 175.21 0.025 1 818 . 176 LEU H H 8.31 0.025 1 819 . 176 LEU N N 125.99 0.025 1 820 . 176 LEU CA C 57.12 0.025 1 821 . 176 LEU C C 178.21 0.025 1 822 . 176 LEU CB C 40.04 0.025 1 823 . 177 GLU H H 7.82 0.025 1 824 . 177 GLU N N 118.93 0.025 1 825 . 177 GLU CA C 57.77 0.025 1 826 . 177 GLU C C 176.34 0.025 1 827 . 177 GLU CB C 28.49 0.025 1 828 . 178 TYR H H 7.14 0.025 1 829 . 178 TYR N N 119.60 0.025 1 830 . 178 TYR CA C 57.36 0.025 1 831 . 178 TYR C C 175.61 0.025 1 832 . 178 TYR CB C 37.58 0.025 1 833 . 179 ALA H H 7.46 0.025 1 834 . 179 ALA N N 126.13 0.025 1 835 . 179 ALA CA C 51.39 0.025 1 836 . 179 ALA C C 176.72 0.025 1 837 . 179 ALA CB C 18.80 0.025 1 838 . 180 ASP H H 8.01 0.025 1 839 . 180 ASP N N 122.43 0.025 1 840 . 180 ASP CA C 53.68 0.025 1 841 . 180 ASP C C 176.16 0.025 1 842 . 180 ASP CB C 41.65 0.025 1 843 . 181 GLU CA C 60.18 0.025 1 844 . 181 GLU C C 178.82 0.025 1 845 . 181 GLU CB C 28.45 0.025 1 846 . 182 VAL H H 7.88 0.025 1 847 . 182 VAL N N 122.76 0.025 1 848 . 182 VAL CA C 65.09 0.025 1 849 . 182 VAL C C 178.70 0.025 1 850 . 182 VAL CB C 30.70 0.025 1 851 . 183 THR H H 7.92 0.025 1 852 . 183 THR N N 120.79 0.025 1 853 . 183 THR CA C 63.60 0.025 1 854 . 183 THR CB C 65.71 0.025 1 855 . 184 LEU CA C 57.26 0.025 1 856 . 184 LEU C C 178.66 0.025 1 857 . 184 LEU CB C 40.52 0.025 1 858 . 185 GLY H H 8.16 0.025 1 859 . 185 GLY N N 109.53 0.025 1 860 . 185 GLY CA C 47.09 0.025 1 861 . 185 GLY C C 176.08 0.025 1 862 . 186 ARG H H 7.95 0.025 1 863 . 186 ARG N N 123.48 0.025 1 864 . 186 ARG CA C 58.22 0.025 1 865 . 186 ARG C C 179.44 0.025 1 866 . 186 ARG CB C 29.09 0.025 1 867 . 187 ALA H H 7.88 0.025 1 868 . 187 ALA N N 125.30 0.025 1 869 . 187 ALA CA C 53.74 0.025 1 870 . 187 ALA C C 180.37 0.025 1 871 . 187 ALA CB C 17.60 0.025 1 872 . 188 LEU H H 7.78 0.025 1 873 . 188 LEU N N 120.52 0.025 1 874 . 188 LEU CA C 57.01 0.025 1 875 . 188 LEU C C 179.96 0.025 1 876 . 188 LEU CB C 40.82 0.025 1 877 . 189 GLU H H 8.15 0.025 1 878 . 189 GLU N N 124.80 0.025 1 879 . 189 GLU CA C 58.77 0.025 1 880 . 189 GLU C C 178.25 0.025 1 881 . 189 GLU CB C 28.97 0.025 1 882 . 190 GLY H H 7.67 0.025 1 883 . 190 GLY N N 107.16 0.025 1 884 . 190 GLY CA C 44.36 0.025 1 885 . 190 GLY C C 173.54 0.025 1 886 . 191 ARG H H 6.70 0.025 1 887 . 191 ARG N N 120.81 0.025 1 888 . 191 ARG CA C 55.63 0.025 1 889 . 191 ARG C C 174.33 0.025 1 890 . 191 ARG CB C 29.51 0.025 1 891 . 192 ARG H H 7.75 0.025 1 892 . 192 ARG N N 122.75 0.025 1 893 . 192 ARG CA C 52.28 0.025 1 894 . 192 ARG C C 173.67 0.025 1 895 . 192 ARG CB C 31.34 0.025 1 896 . 193 PRO CA C 62.74 0.025 1 897 . 193 PRO C C 176.15 0.025 1 898 . 193 PRO CB C 31.39 0.025 1 899 . 194 VAL H H 7.46 0.025 1 900 . 194 VAL N N 127.05 0.025 1 901 . 194 VAL CA C 62.40 0.025 1 902 . 194 VAL C C 180.63 0.025 1 903 . 194 VAL CB C 32.46 0.025 1 stop_ save_