data_18933 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; ASFV Pol X structure ; _BMRB_accession_number 18933 _BMRB_flat_file_name bmr18933.str _Entry_type original _Submission_date 2013-01-03 _Accession_date 2013-01-03 _Entry_origination author _NMR_STAR_version 2.1.1 _Experimental_method NMR _Details 'SFV Pol X structure' loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Wu Wen-Jin . . 2 Su Mei-I . . 3 Tsai Ming-Daw . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 154 "13C chemical shifts" 430 "15N chemical shifts" 154 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2014-05-05 update BMRB 'update entry citation' 2014-03-31 original author 'original release' stop_ loop_ _Related_BMRB_accession_number _Relationship 18934 'Binary complex of African Swine Fever Virus Pol X with MgdGTP' 18935 'Ternary complex of African Swine Fever Virus Pol X with MgdGTP and DNA' stop_ save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title 'How a low-fidelity DNA polymerase chooses non-watson-crick from watson-crick incorporation.' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 24617852 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Wu Wen-Jin . . 2 Su Mei-I . . 3 Wu Jian-Li . . 4 Kumar Sandeep . . 5 Lim Liang-Hin . . 6 Wang 'Chun-Wei Eric' . . 7 Nelissen Frank H.T. . 8 Chen 'Ming-Chuan Chad' . . 9 Doreleijers Jurgen F. . 10 Wijmenga Sybren S. . 11 Tsai Ming-Daw . . stop_ _Journal_abbreviation 'J. Am. Chem. Soc.' _Journal_name_full 'Journal of the American Chemical Society' _Journal_volume 136 _Journal_issue 13 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 4927 _Page_last 4937 _Year 2014 _Details . save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name 'ASFV Pol X' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'ASFV Pol X' $entity stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state ? _System_paramagnetic no _System_thiol_state . _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_entity _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common entity _Molecular_mass 20351.670 _Mol_thiol_state 'all free' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 174 _Mol_residue_sequence ; MLTLIQGKKIVNHLRSRLAF EYNGQLIKILSKNIVAVGSL RREEKMLNDVDLLIIVPEKK LLKHVLPNIRIKGLSFSVKV CGERKCVLFIEWEKKTYQLD LFTALAEEKPYAIFHFTGPV SYLIRIRAALKKKNYKLNQY GLFKNQTLVPLKITTEKELI KELGFTYRIPKKRL ; loop_ _Residue_seq_code _Residue_label 1 MET 2 LEU 3 THR 4 LEU 5 ILE 6 GLN 7 GLY 8 LYS 9 LYS 10 ILE 11 VAL 12 ASN 13 HIS 14 LEU 15 ARG 16 SER 17 ARG 18 LEU 19 ALA 20 PHE 21 GLU 22 TYR 23 ASN 24 GLY 25 GLN 26 LEU 27 ILE 28 LYS 29 ILE 30 LEU 31 SER 32 LYS 33 ASN 34 ILE 35 VAL 36 ALA 37 VAL 38 GLY 39 SER 40 LEU 41 ARG 42 ARG 43 GLU 44 GLU 45 LYS 46 MET 47 LEU 48 ASN 49 ASP 50 VAL 51 ASP 52 LEU 53 LEU 54 ILE 55 ILE 56 VAL 57 PRO 58 GLU 59 LYS 60 LYS 61 LEU 62 LEU 63 LYS 64 HIS 65 VAL 66 LEU 67 PRO 68 ASN 69 ILE 70 ARG 71 ILE 72 LYS 73 GLY 74 LEU 75 SER 76 PHE 77 SER 78 VAL 79 LYS 80 VAL 81 CYS 82 GLY 83 GLU 84 ARG 85 LYS 86 CYS 87 VAL 88 LEU 89 PHE 90 ILE 91 GLU 92 TRP 93 GLU 94 LYS 95 LYS 96 THR 97 TYR 98 GLN 99 LEU 100 ASP 101 LEU 102 PHE 103 THR 104 ALA 105 LEU 106 ALA 107 GLU 108 GLU 109 LYS 110 PRO 111 TYR 112 ALA 113 ILE 114 PHE 115 HIS 116 PHE 117 THR 118 GLY 119 PRO 120 VAL 121 SER 122 TYR 123 LEU 124 ILE 125 ARG 126 ILE 127 ARG 128 ALA 129 ALA 130 LEU 131 LYS 132 LYS 133 LYS 134 ASN 135 TYR 136 LYS 137 LEU 138 ASN 139 GLN 140 TYR 141 GLY 142 LEU 143 PHE 144 LYS 145 ASN 146 GLN 147 THR 148 LEU 149 VAL 150 PRO 151 LEU 152 LYS 153 ILE 154 THR 155 THR 156 GLU 157 LYS 158 GLU 159 LEU 160 ILE 161 LYS 162 GLU 163 LEU 164 GLY 165 PHE 166 THR 167 TYR 168 ARG 169 ILE 170 PRO 171 LYS 172 LYS 173 ARG 174 LEU stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-11-25 loop_ _Database_name _Database_accession_code _Database_entry_mol_name _Sequence_query_to_submitted_percentage _Sequence_subject_length _Sequence_identity _Sequence_positive _Sequence_homology_expectation_value BMRB 18934 entity_1 100.00 174 100.00 100.00 1.99e-119 BMRB 18935 entity 100.00 174 100.00 100.00 1.99e-119 PDB 1JAJ "Solution Structure Of Dna Polymerase X From The African Swine Fever Virus" 100.00 174 100.00 100.00 1.99e-119 PDB 1JQR "Nmr Structure Of The African Swine Fever Virus Dna Polymerase X" 100.00 174 100.00 100.00 1.99e-119 PDB 2M2T "Asfv Pol X Structure" 100.00 174 100.00 100.00 1.99e-119 PDB 2M2U "Binary Complex Of African Swine Fever Virus Pol X With Mgdgtp" 100.00 174 100.00 100.00 1.99e-119 PDB 2M2V "African Swine Fever Virus Pol X In The Ternary Complex With Mgdgtp And Dna" 100.00 174 100.00 100.00 1.99e-119 PDB 2M2W "Ternary Complex Of Asfv Pol X With Dna And Mgdgtp" 100.00 174 100.00 100.00 1.99e-119 EMBL CAN10196 "DNA polymerase beta-like protein [African swine fever virus Benin 97/1]" 100.00 174 100.00 100.00 1.99e-119 EMBL CAN10446 "DNA polymerase beta-like protein [African swine fever virus OURT 88/3]" 100.00 174 100.00 100.00 1.99e-119 EMBL CBH29197 "BA71V-O174L [African swine fever virus E75]" 100.00 174 100.00 100.00 1.99e-119 GB AAA65326 "DNA polymerase beta-like protein [African swine fever virus]" 100.00 174 100.00 100.00 1.99e-119 GB AIY22288 "DNA polymerase beta-like protein [African swine fever virus]" 100.00 174 100.00 100.00 1.99e-119 GB AIY22446 "DNA polymerase beta-like protein [African swine fever virus]" 100.00 174 100.00 100.00 1.99e-119 GB AKO62778 "pO174L [African swine fever virus]" 100.00 174 100.00 100.00 1.99e-119 PRF 2113434DC "DNA polymerase beta-like protein" 100.00 174 100.00 100.00 1.99e-119 REF NP_042790 "DNA polymerase beta-like protein [African swine fever virus]" 100.00 174 100.00 100.00 1.99e-119 SP P0C984 "RecName: Full=Repair DNA polymerase X; Short=Pol X [African swine fever virus Malawi LIL 20/1]" 100.00 174 98.85 99.43 1.25e-117 SP P42494 "RecName: Full=Repair DNA polymerase X; Short=Pol X" 100.00 174 100.00 100.00 1.99e-119 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $entity 'African Swine Fever Virus' 10497 Viruses . Asfivirus 'African Swine Fever Virus' 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 $entity 'recombinant technology' . Escherichia coli . pET-17b 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 $entity 1.0 mM '[U-100% 13C; U-100% 15N; U-80% 2H]' DTT 10 mM [U-2H] 'potassium chloride' 50 mM 'natural abundance' borate 50 mM 'natural abundance' stop_ save_ save_sample_2 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $entity 1.0 mM '[U-100% 13C; U-100% 15N]' DTT 10 mM [U-2H] 'potassium chloride' 50 mM 'natural abundance' borate 50 mM 'natural abundance' stop_ save_ ############################ # Computer software used # ############################ save_Haddock _Saveframe_category software _Name HADDOCK _Version . loop_ _Vendor _Address _Electronic_address 'Dr. Alexandre Bonvin' . . stop_ loop_ _Task refinement stop_ _Details . save_ save_CYANA _Saveframe_category software _Name CYANA _Version . loop_ _Vendor _Address _Electronic_address 'Guntert, Mumenthaler and Wuthrich' . . stop_ loop_ _Task 'structure solution' stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model Avance _Field_strength 800 _Details . save_ save_spectrometer_2 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model Avance _Field_strength 600 _Details . save_ ############################# # NMR applied experiments # ############################# save_2D_1H-15N_HSQC_1 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-15N HSQC' _Sample_label $sample_1 save_ save_2D_1H-13C_HSQC_2 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-13C HSQC' _Sample_label $sample_2 save_ save_3D_HNCO_3 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCO' _Sample_label $sample_1 save_ save_3D_HNCA_4 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCA' _Sample_label $sample_1 save_ save_3D_HNCACB_5 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCACB' _Sample_label $sample_1 save_ save_3D_1H-15N_NOESY_6 _Saveframe_category NMR_applied_experiment _Experiment_name '3D 1H-15N NOESY' _Sample_label $sample_2 save_ save_3D_1H-13C_NOESY_7 _Saveframe_category NMR_applied_experiment _Experiment_name '3D 1H-13C NOESY' _Sample_label $sample_2 save_ save_3D_HCCH-TOCSY_8 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HCCH-TOCSY' _Sample_label $sample_2 save_ ####################### # Sample conditions # ####################### save_sample_conditions_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units 'ionic strength' 100 . mM pH 6.5 . pH pressure 1 . atm temperature 293 . K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference_1 _Saveframe_category chemical_shift_reference _Details . loop_ _Mol_common_name _Atom_type _Atom_isotope_number _Atom_group _Chem_shift_units _Chem_shift_value _Reference_method _Reference_type _External_reference_sample_geometry _External_reference_location _External_reference_axis _Indirect_shift_ratio DSS C 13 'methyl protons' ppm 0.00 na indirect . . . 0.251449530 DSS H 1 'methyl protons' ppm 0.00 internal direct . . . 1.000000000 DSS N 15 'methyl protons' ppm 0.00 na indirect . . . 0.101329118 stop_ save_ ################################### # Assigned chemical shift lists # ################################### ################################################################### # Chemical Shift Ambiguity Index Value Definitions # # # # The values other than 1 are used for those atoms with different # # chemical shifts that cannot be assigned to stereospecific atoms # # or to specific residues or chains. # # # # Index Value Definition # # # # 1 Unique (including isolated methyl protons, # # geminal atoms, and geminal methyl # # groups with identical chemical shifts) # # (e.g. ILE HD11, HD12, HD13 protons) # # 2 Ambiguity of geminal atoms or geminal methyl # # proton groups (e.g. ASP HB2 and HB3 # # protons, LEU CD1 and CD2 carbons, or # # LEU HD11, HD12, HD13 and HD21, HD22, # # HD23 methyl protons) # # 3 Aromatic atoms on opposite sides of # # symmetrical rings (e.g. TYR HE1 and HE2 # # protons) # # 4 Intraresidue ambiguities (e.g. LYS HG and # # HD protons or TRP HZ2 and HZ3 protons) # # 5 Interresidue ambiguities (LYS 12 vs. LYS 27) # # 6 Intermolecular ambiguities (e.g. ASP 31 CA # # in monomer 1 and ASP 31 CA in monomer 2 # # of an asymmetrical homodimer, duplex # # DNA assignments, or other assignments # # that may apply to atoms in one or more # # molecule in the molecular assembly) # # 9 Ambiguous, specific ambiguity not defined # # # ################################################################### save_assigned_chem_shift_list_1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Experiment_label '2D 1H-15N HSQC' '2D 1H-13C HSQC' '3D HNCO' '3D HNCA' '3D HNCACB' stop_ loop_ _Sample_label $sample_1 $sample_2 stop_ _Sample_conditions_label $sample_conditions_1 _Chem_shift_reference_set_label $chemical_shift_reference_1 _Mol_system_component_name 'ASFV Pol X' _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 2 LEU H H 8.756 0.020 1 2 2 2 LEU C C 175.742 0.3 1 3 2 2 LEU CA C 54.134 0.3 1 4 2 2 LEU CB C 42.842 0.3 1 5 2 2 LEU N N 122.812 0.3 1 6 3 3 THR H H 8.428 0.020 1 7 3 3 THR C C 175.938 0.3 1 8 3 3 THR CA C 60.550 0.3 1 9 3 3 THR CB C 70.781 0.3 1 10 3 3 THR N N 113.000 0.3 1 11 4 4 LEU H H 7.731 0.020 1 12 4 4 LEU C C 178.463 0.3 1 13 4 4 LEU CA C 58.129 0.3 1 14 4 4 LEU CB C 39.534 0.3 1 15 4 4 LEU N N 122.531 0.3 1 16 5 5 ILE H H 7.645 0.020 1 17 5 5 ILE C C 178.573 0.3 1 18 5 5 ILE CA C 63.738 0.3 1 19 5 5 ILE CB C 36.872 0.3 1 20 5 5 ILE N N 115.505 0.3 1 21 6 6 GLN H H 7.645 0.020 1 22 6 6 GLN C C 179.014 0.3 1 23 6 6 GLN CA C 58.331 0.3 1 24 6 6 GLN CB C 28.189 0.3 1 25 6 6 GLN N N 121.626 0.3 1 26 7 7 GLY H H 8.660 0.020 1 27 7 7 GLY C C 174.749 0.3 1 28 7 7 GLY CA C 46.790 0.3 1 29 7 7 GLY N N 107.684 0.3 1 30 8 8 LYS H H 8.518 0.020 1 31 8 8 LYS C C 179.455 0.3 1 32 8 8 LYS CA C 59.905 0.3 1 33 8 8 LYS CB C 31.422 0.3 1 34 8 8 LYS N N 120.942 0.3 1 35 9 9 LYS H H 7.731 0.020 1 36 9 9 LYS C C 179.823 0.3 1 37 9 9 LYS CA C 59.622 0.3 1 38 9 9 LYS CB C 31.295 0.3 1 39 9 9 LYS N N 120.710 0.3 1 40 10 10 ILE H H 7.711 0.020 1 41 10 10 ILE C C 177.789 0.3 1 42 10 10 ILE CA C 64.465 0.3 1 43 10 10 ILE CB C 36.365 0.3 1 44 10 10 ILE N N 121.345 0.3 1 45 11 11 VAL H H 7.918 0.020 1 46 11 11 VAL C C 177.372 0.3 1 47 11 11 VAL CA C 67.451 0.3 1 48 11 11 VAL CB C 30.534 0.3 1 49 11 11 VAL N N 120.258 0.3 1 50 12 12 ASN H H 7.993 0.020 1 51 12 12 ASN C C 177.445 0.3 1 52 12 12 ASN CA C 56.112 0.3 1 53 12 12 ASN CB C 37.633 0.3 1 54 12 12 ASN N N 116.971 0.3 1 55 13 13 HIS H H 7.741 0.020 1 56 13 13 HIS C C 177.862 0.3 1 57 13 13 HIS CA C 59.098 0.3 1 58 13 13 HIS CB C 31.232 0.3 1 59 13 13 HIS N N 120.258 0.3 1 60 14 14 LEU H H 8.221 0.020 1 61 14 14 LEU C C 179.186 0.3 1 62 14 14 LEU CA C 56.757 0.3 1 63 14 14 LEU CB C 41.119 0.3 1 64 14 14 LEU N N 116.641 0.3 1 65 15 15 ARG H H 7.968 0.020 1 66 15 15 ARG C C 176.330 0.3 1 67 15 15 ARG CA C 59.703 0.3 1 68 15 15 ARG CB C 29.077 0.3 1 69 15 15 ARG N N 115.957 0.3 1 70 16 16 SER H H 6.963 0.020 1 71 16 16 SER C C 176.024 0.3 1 72 16 16 SER CA C 57.282 0.3 1 73 16 16 SER CB C 63.683 0.3 1 74 16 16 SER N N 109.395 0.3 1 75 17 17 ARG H H 7.781 0.020 1 76 17 17 ARG C C 174.590 0.3 1 77 17 17 ARG CA C 56.273 0.3 1 78 17 17 ARG CB C 31.802 0.3 1 79 17 17 ARG N N 122.775 0.3 1 80 18 18 LEU H H 8.650 0.020 1 81 18 18 LEU C C 176.281 0.3 1 82 18 18 LEU CA C 54.780 0.3 1 83 18 18 LEU CB C 43.211 0.3 1 84 18 18 LEU N N 122.421 0.3 1 85 19 19 ALA H H 8.609 0.020 1 86 19 19 ALA C C 173.904 0.3 1 87 19 19 ALA CA C 50.866 0.3 1 88 19 19 ALA CB C 22.865 0.3 1 89 19 19 ALA N N 126.441 0.3 1 90 20 20 PHE H H 8.801 0.020 1 91 20 20 PHE C C 172.592 0.3 1 92 20 20 PHE CA C 55.789 0.3 1 93 20 20 PHE CB C 41.689 0.3 1 94 20 20 PHE N N 114.600 0.3 1 95 21 21 GLU H H 7.847 0.020 1 96 21 21 GLU C C 174.872 0.3 1 97 21 21 GLU CA C 55.062 0.3 1 98 21 21 GLU CB C 30.725 0.3 1 99 21 21 GLU N N 122.873 0.3 1 100 22 22 TYR H H 8.806 0.020 1 101 22 22 TYR C C 174.872 0.3 1 102 22 22 TYR CA C 55.748 0.3 1 103 22 22 TYR CB C 40.105 0.3 1 104 22 22 TYR N N 126.270 0.3 1 105 23 23 ASN H H 8.943 0.020 1 106 23 23 ASN C C 175.435 0.3 1 107 23 23 ASN CA C 53.005 0.3 1 108 23 23 ASN CB C 36.365 0.3 1 109 23 23 ASN N N 128.420 0.3 1 110 24 24 GLY H H 8.534 0.020 1 111 24 24 GLY C C 173.707 0.3 1 112 24 24 GLY CA C 44.934 0.3 1 113 24 24 GLY N N 104.067 0.3 1 114 25 25 GLN H H 7.595 0.020 1 115 25 25 GLN C C 173.744 0.3 1 116 25 25 GLN CA C 53.327 0.3 1 117 25 25 GLN CB C 30.661 0.3 1 118 25 25 GLN N N 120.038 0.3 1 119 26 26 LEU H H 8.382 0.020 1 120 26 26 LEU C C 175.987 0.3 1 121 26 26 LEU CA C 54.013 0.3 1 122 26 26 LEU CB C 40.865 0.3 1 123 26 26 LEU N N 124.681 0.3 1 124 27 27 ILE H H 8.882 0.020 1 125 27 27 ILE C C 175.215 0.3 1 126 27 27 ILE CA C 59.259 0.3 1 127 27 27 ILE CB C 35.732 0.3 1 128 27 27 ILE N N 130.779 0.3 1 129 28 28 LYS H H 8.165 0.020 1 130 28 28 LYS C C 176.771 0.3 1 131 28 28 LYS CA C 56.838 0.3 1 132 28 28 LYS CB C 31.739 0.3 1 133 28 28 LYS N N 126.160 0.3 1 134 29 29 ILE H H 8.019 0.020 1 135 29 29 ILE C C 175.877 0.3 1 136 29 29 ILE CA C 60.308 0.3 1 137 29 29 ILE CB C 37.063 0.3 1 138 29 29 ILE N N 126.380 0.3 1 139 30 30 LEU H H 8.917 0.020 1 140 30 30 LEU C C 178.867 0.3 1 141 30 30 LEU CA C 54.619 0.3 1 142 30 30 LEU CB C 40.865 0.3 1 143 30 30 LEU N N 129.215 0.3 1 144 31 31 SER H H 8.594 0.020 1 145 31 31 SER C C 177.396 0.3 1 146 31 31 SER CA C 61.236 0.3 1 147 31 31 SER CB C 62.035 0.3 1 148 31 31 SER N N 117.997 0.3 1 149 32 32 LYS H H 8.029 0.020 1 150 32 32 LYS C C 176.244 0.3 1 151 32 32 LYS CA C 57.403 0.3 1 152 32 32 LYS CB C 30.281 0.3 1 153 32 32 LYS N N 116.189 0.3 1 154 33 33 ASN H H 7.902 0.020 1 155 33 33 ASN C C 172.384 0.3 1 156 33 33 ASN CA C 52.157 0.3 1 157 33 33 ASN CB C 38.267 0.3 1 158 33 33 ASN N N 119.061 0.3 1 159 34 34 ILE H H 7.443 0.020 1 160 34 34 ILE C C 175.607 0.3 1 161 34 34 ILE CA C 60.550 0.3 1 162 34 34 ILE CB C 38.964 0.3 1 163 34 34 ILE N N 120.038 0.3 1 164 35 35 VAL H H 9.533 0.020 1 165 35 35 VAL C C 175.386 0.3 1 166 35 35 VAL CA C 60.026 0.3 1 167 35 35 VAL CB C 34.781 0.3 1 168 35 35 VAL N N 129.435 0.3 1 169 36 36 ALA H H 8.665 0.020 1 170 36 36 ALA C C 177.347 0.3 1 171 36 36 ALA CA C 52.399 0.3 1 172 36 36 ALA CB C 17.858 0.3 1 173 36 36 ALA N N 130.571 0.3 1 174 37 37 VAL H H 8.079 0.020 1 175 37 37 VAL C C 174.455 0.3 1 176 37 37 VAL CA C 59.380 0.3 1 177 37 37 VAL CB C 32.943 0.3 1 178 37 37 VAL N N 115.395 0.3 1 179 38 38 GLY H H 7.579 0.020 1 180 38 38 GLY C C 173.364 0.3 1 181 38 38 GLY CA C 46.185 0.3 1 182 38 38 GLY N N 107.672 0.3 1 183 39 39 SER H H 8.953 0.020 1 184 39 39 SER C C 175.570 0.3 1 185 39 39 SER CA C 61.801 0.3 1 186 39 39 SER CB C 62.478 0.3 1 187 39 39 SER N N 121.052 0.3 1 188 40 40 LEU H H 8.195 0.020 1 189 40 40 LEU C C 180.203 0.3 1 190 40 40 LEU CA C 58.129 0.3 1 191 40 40 LEU CB C 41.753 0.3 1 192 40 40 LEU N N 121.553 0.3 1 193 41 41 ARG H H 6.873 0.020 1 194 41 41 ARG C C 177.323 0.3 1 195 41 41 ARG CA C 58.331 0.3 1 196 41 41 ARG CB C 28.443 0.3 1 197 41 41 ARG N N 121.956 0.3 1 198 42 42 ARG H H 7.438 0.020 1 199 42 42 ARG C C 172.911 0.3 1 200 42 42 ARG CA C 57.242 0.3 1 201 42 42 ARG CB C 29.140 0.3 1 202 42 42 ARG N N 114.600 0.3 1 203 43 43 GLU H H 7.564 0.020 1 204 43 43 GLU C C 175.999 0.3 1 205 43 43 GLU CA C 56.556 0.3 1 206 43 43 GLU CB C 25.337 0.3 1 207 43 43 GLU N N 113.354 0.3 1 208 44 44 GLU H H 7.261 0.020 1 209 44 44 GLU C C 175.423 0.3 1 210 44 44 GLU CA C 56.838 0.3 1 211 44 44 GLU CB C 28.696 0.3 1 212 44 44 GLU N N 119.696 0.3 1 213 45 45 LYS H H 7.938 0.020 1 214 45 45 LYS C C 177.715 0.3 1 215 45 45 LYS CA C 59.219 0.3 1 216 45 45 LYS CB C 32.119 0.3 1 217 45 45 LYS N N 117.435 0.3 1 218 46 46 MET H H 7.595 0.020 1 219 46 46 MET CA C 52.520 0.3 1 220 46 46 MET CB C 33.450 0.3 1 221 46 46 MET N N 115.847 0.3 1 222 47 47 LEU H H 9.220 0.020 1 223 47 47 LEU CA C 53.126 0.3 1 224 47 47 LEU CB C 43.070 0.3 1 225 47 47 LEU N N 121.627 0.3 1 226 49 49 ASP H H 7.761 0.020 1 227 49 49 ASP C C 173.340 0.3 1 228 49 49 ASP CA C 51.794 0.3 1 229 49 49 ASP CB C 43.006 0.3 1 230 49 49 ASP N N 117.093 0.3 1 231 50 50 VAL H H 8.089 0.020 1 232 50 50 VAL C C 173.070 0.3 1 233 50 50 VAL CA C 61.842 0.3 1 234 50 50 VAL CB C 32.563 0.3 1 235 50 50 VAL N N 119.012 0.3 1 236 51 51 ASP H H 8.069 0.020 1 237 51 51 ASP C C 174.565 0.3 1 238 51 51 ASP CA C 52.157 0.3 1 239 51 51 ASP CB C 42.640 0.3 1 240 51 51 ASP N N 127.064 0.3 1 241 52 52 LEU H H 8.852 0.020 1 242 52 52 LEU C C 174.063 0.3 1 243 52 52 LEU CA C 52.682 0.3 1 244 52 52 LEU CB C 44.351 0.3 1 245 52 52 LEU N N 121.627 0.3 1 246 53 53 LEU H H 9.362 0.020 1 247 53 53 LEU CA C 55.991 0.3 1 248 53 53 LEU CB C 42.133 0.3 1 249 53 53 LEU N N 123.093 0.3 1 250 54 54 ILE H H 8.907 0.020 1 251 54 54 ILE CA C 55.062 0.3 1 252 54 54 ILE CB C 33.070 0.3 1 253 54 54 ILE N N 123.777 0.3 1 254 58 58 GLU H H 6.716 0.020 1 255 58 58 GLU CA C 54.377 0.3 1 256 58 58 GLU CB C 31.422 0.3 1 257 58 58 GLU N N 114.710 0.3 1 258 61 61 LEU H H 7.307 0.020 1 259 61 61 LEU C C 178.512 0.3 1 260 61 61 LEU CA C 54.780 0.3 1 261 61 61 LEU CB C 41.119 0.3 1 262 61 61 LEU N N 115.957 0.3 1 263 62 62 LEU H H 7.327 0.020 1 264 62 62 LEU C C 177.874 0.3 1 265 62 62 LEU CA C 58.936 0.3 1 266 62 62 LEU CB C 40.739 0.3 1 267 62 62 LEU N N 120.038 0.3 1 268 63 63 LYS H H 7.973 0.020 1 269 63 63 LYS C C 175.460 0.3 1 270 63 63 LYS CA C 57.564 0.3 1 271 63 63 LYS CB C 30.725 0.3 1 272 63 63 LYS N N 114.600 0.3 1 273 64 64 HIS H H 7.544 0.020 1 274 64 64 HIS CA C 56.112 0.3 1 275 64 64 HIS CB C 32.436 0.3 1 276 64 64 HIS N N 115.273 0.3 1 277 65 65 VAL H H 6.787 0.020 1 278 65 65 VAL CA C 66.038 0.3 1 279 65 65 VAL CB C 30.027 0.3 1 280 65 65 VAL N N 118.682 0.3 1 281 68 68 ASN H H 7.009 0.020 1 282 68 68 ASN C C 174.884 0.3 1 283 68 68 ASN CA C 51.027 0.3 1 284 68 68 ASN CB C 40.232 0.3 1 285 68 68 ASN N N 112.108 0.3 1 286 69 69 ILE H H 7.150 0.020 1 287 69 69 ILE C C 174.394 0.3 1 288 69 69 ILE CA C 60.107 0.3 1 289 69 69 ILE CB C 38.267 0.3 1 290 69 69 ILE N N 123.325 0.3 1 291 70 70 ARG H H 8.902 0.020 1 292 70 70 ARG C C 174.590 0.3 1 293 70 70 ARG CA C 53.247 0.3 1 294 70 70 ARG CB C 32.372 0.3 1 295 70 70 ARG N N 126.722 0.3 1 296 71 71 ILE H H 7.491 0.020 1 297 71 71 ILE C C 175.583 0.3 1 298 71 71 ILE CA C 59.824 0.3 1 299 71 71 ILE CB C 37.760 0.3 1 300 71 71 ILE N N 119.978 0.3 1 301 72 72 LYS H H 8.523 0.020 1 302 72 72 LYS C C 177.703 0.3 1 303 72 72 LYS CA C 57.201 0.3 1 304 72 72 LYS CB C 31.485 0.3 1 305 72 72 LYS N N 128.530 0.3 1 306 73 73 GLY H H 8.791 0.020 1 307 73 73 GLY C C 173.781 0.3 1 308 73 73 GLY CA C 45.822 0.3 1 309 73 73 GLY N N 113.806 0.3 1 310 74 74 LEU H H 7.393 0.020 1 311 74 74 LEU C C 175.840 0.3 1 312 74 74 LEU CA C 53.691 0.3 1 313 74 74 LEU CB C 44.161 0.3 1 314 74 74 LEU N N 120.490 0.3 1 315 75 75 SER H H 8.917 0.020 1 316 75 75 SER C C 173.205 0.3 1 317 75 75 SER CA C 57.887 0.3 1 318 75 75 SER CB C 63.049 0.3 1 319 75 75 SER N N 120.038 0.3 1 320 76 76 PHE H H 8.003 0.020 1 321 76 76 PHE C C 173.536 0.3 1 322 76 76 PHE CA C 55.426 0.3 1 323 76 76 PHE CB C 42.006 0.3 1 324 76 76 PHE N N 119.586 0.3 1 325 77 77 SER H H 8.907 0.020 1 326 77 77 SER C C 173.438 0.3 1 327 77 77 SER CA C 56.152 0.3 1 328 77 77 SER CB C 65.204 0.3 1 329 77 77 SER N N 114.943 0.3 1 330 78 78 VAL H H 8.892 0.020 1 331 78 78 VAL CA C 62.044 0.3 1 332 78 78 VAL CB C 32.182 0.3 1 333 78 78 VAL N N 124.791 0.3 1 334 79 79 LYS H H 9.049 0.020 1 335 79 79 LYS CA C 56.192 0.3 1 336 79 79 LYS CB C 32.372 0.3 1 337 79 79 LYS N N 129.667 0.3 1 338 82 82 GLY H H 8.044 0.020 1 339 82 82 GLY C C 171.710 0.3 1 340 82 82 GLY CA C 43.925 0.3 1 341 82 82 GLY N N 117.263 0.3 1 342 83 83 GLU H H 8.296 0.020 1 343 83 83 GLU C C 178.695 0.3 1 344 83 83 GLU CA C 58.977 0.3 1 345 83 83 GLU CB C 29.837 0.3 1 346 83 83 GLU N N 117.203 0.3 1 347 84 84 ARG H H 8.342 0.020 1 348 84 84 ARG C C 175.877 0.3 1 349 84 84 ARG CA C 53.731 0.3 1 350 84 84 ARG CB C 31.295 0.3 1 351 84 84 ARG N N 113.818 0.3 1 352 85 85 LYS H H 6.822 0.020 1 353 85 85 LYS C C 174.516 0.3 1 354 85 85 LYS CA C 54.740 0.3 1 355 85 85 LYS CB C 34.844 0.3 1 356 85 85 LYS N N 119.354 0.3 1 357 86 86 CYS H H 9.084 0.020 1 358 86 86 CYS C C 171.600 0.3 1 359 86 86 CYS CA C 55.627 0.3 1 360 86 86 CYS CB C 30.344 0.3 1 361 86 86 CYS N N 125.928 0.3 1 362 87 87 VAL H H 8.705 0.020 1 363 87 87 VAL C C 174.431 0.3 1 364 87 87 VAL CA C 61.317 0.3 1 365 87 87 VAL CB C 33.196 0.3 1 366 87 87 VAL N N 126.612 0.3 1 367 88 88 LEU H H 9.417 0.020 1 368 88 88 LEU C C 175.227 0.3 1 369 88 88 LEU CA C 52.520 0.3 1 370 88 88 LEU CB C 44.605 0.3 1 371 88 88 LEU N N 127.748 0.3 1 372 89 89 PHE H H 8.937 0.020 1 373 89 89 PHE C C 176.906 0.3 1 374 89 89 PHE CA C 55.587 0.3 1 375 89 89 PHE CB C 38.901 0.3 1 376 89 89 PHE N N 120.981 0.3 1 377 90 90 ILE H H 9.230 0.020 1 378 90 90 ILE C C 173.781 0.3 1 379 90 90 ILE CA C 58.654 0.3 1 380 90 90 ILE CB C 40.612 0.3 1 381 90 90 ILE N N 119.928 0.3 1 382 91 91 GLU H H 8.175 0.020 1 383 91 91 GLU C C 175.607 0.3 1 384 91 91 GLU CA C 54.619 0.3 1 385 91 91 GLU CB C 29.837 0.3 1 386 91 91 GLU N N 124.339 0.3 1 387 92 92 TRP H H 9.306 0.020 1 388 92 92 TRP C C 175.203 0.3 1 389 92 92 TRP CA C 56.233 0.3 1 390 92 92 TRP CB C 30.661 0.3 1 391 92 92 TRP N N 127.516 0.3 1 392 93 93 GLU H H 8.796 0.020 1 393 93 93 GLU C C 175.668 0.3 1 394 93 93 GLU CA C 56.878 0.3 1 395 93 93 GLU CB C 26.034 0.3 1 396 93 93 GLU N N 127.834 0.3 1 397 94 94 LYS H H 8.498 0.020 1 398 94 94 LYS C C 175.423 0.3 1 399 94 94 LYS CA C 57.443 0.3 1 400 94 94 LYS CB C 28.633 0.3 1 401 94 94 LYS N N 108.931 0.3 1 402 95 95 LYS H H 7.761 0.020 1 403 95 95 LYS C C 174.443 0.3 1 404 95 95 LYS CA C 54.417 0.3 1 405 95 95 LYS CB C 34.464 0.3 1 406 95 95 LYS N N 121.737 0.3 1 407 96 96 THR H H 7.761 0.020 1 408 96 96 THR C C 174.296 0.3 1 409 96 96 THR CA C 61.115 0.3 1 410 96 96 THR CB C 69.450 0.3 1 411 96 96 THR N N 116.067 0.3 1 412 97 97 TYR H H 9.018 0.020 1 413 97 97 TYR C C 173.536 0.3 1 414 97 97 TYR CA C 55.950 0.3 1 415 97 97 TYR CB C 41.182 0.3 1 416 97 97 TYR N N 124.229 0.3 1 417 98 98 GLN H H 8.781 0.020 1 418 98 98 GLN C C 173.266 0.3 1 419 98 98 GLN CA C 55.143 0.3 1 420 98 98 GLN CB C 29.013 0.3 1 421 98 98 GLN N N 123.435 0.3 1 422 99 99 LEU H H 9.104 0.020 1 423 99 99 LEU C C 173.867 0.3 1 424 99 99 LEU CA C 52.520 0.3 1 425 99 99 LEU CB C 44.605 0.3 1 426 99 99 LEU N N 130.119 0.3 1 427 100 100 ASP H H 9.089 0.020 1 428 100 100 ASP C C 172.837 0.3 1 429 100 100 ASP CA C 51.754 0.3 1 430 100 100 ASP CB C 39.344 0.3 1 431 100 100 ASP N N 125.182 0.3 1 432 101 101 LEU H H 8.458 0.020 1 433 101 101 LEU C C 174.529 0.3 1 434 101 101 LEU CA C 51.915 0.3 1 435 101 101 LEU CB C 43.908 0.3 1 436 101 101 LEU N N 121.174 0.3 1 437 102 102 PHE H H 8.281 0.020 1 438 102 102 PHE C C 176.293 0.3 1 439 102 102 PHE CA C 54.054 0.3 1 440 102 102 PHE CB C 41.880 0.3 1 441 102 102 PHE N N 119.464 0.3 1 442 103 103 THR H H 7.872 0.020 1 443 103 103 THR C C 174.933 0.3 1 444 103 103 THR CA C 57.726 0.3 1 445 103 103 THR CB C 71.288 0.3 1 446 103 103 THR N N 108.576 0.3 1 447 104 104 ALA H H 8.660 0.020 1 448 104 104 ALA C C 175.754 0.3 1 449 104 104 ALA CA C 50.018 0.3 1 450 104 104 ALA CB C 22.485 0.3 1 451 104 104 ALA N N 122.885 0.3 1 452 105 105 LEU H H 8.226 0.020 1 453 105 105 LEU C C 179.504 0.3 1 454 105 105 LEU CA C 53.247 0.3 1 455 105 105 LEU CB C 41.753 0.3 1 456 105 105 LEU N N 120.881 0.3 1 457 106 106 ALA H H 8.392 0.020 1 458 106 106 ALA C C 181.269 0.3 1 459 106 106 ALA CA C 56.313 0.3 1 460 106 106 ALA CB C 17.224 0.3 1 461 106 106 ALA N N 124.901 0.3 1 462 107 107 GLU H H 9.664 0.020 1 463 107 107 GLU C C 177.764 0.3 1 464 107 107 GLU CA C 58.533 0.3 1 465 107 107 GLU CB C 27.936 0.3 1 466 107 107 GLU N N 116.409 0.3 1 467 108 108 GLU H H 7.589 0.020 1 468 108 108 GLU CA C 55.143 0.3 1 469 108 108 GLU CB C 29.837 0.3 1 470 108 108 GLU N N 116.189 0.3 1 471 109 109 LYS H H 7.514 0.020 1 472 109 109 LYS CA C 62.851 0.3 1 473 109 109 LYS CB C 30.471 0.3 1 474 109 109 LYS N N 119.928 0.3 1 475 111 111 TYR H H 6.393 0.020 1 476 111 111 TYR C C 179.504 0.3 1 477 111 111 TYR CA C 59.017 0.3 1 478 111 111 TYR CB C 35.668 0.3 1 479 111 111 TYR N N 114.930 0.3 1 480 112 112 ALA H H 8.554 0.020 1 481 112 112 ALA C C 179.173 0.3 1 482 112 112 ALA CA C 54.901 0.3 1 483 112 112 ALA CB C 18.112 0.3 1 484 112 112 ALA N N 124.901 0.3 1 485 113 113 ILE H H 8.680 0.020 1 486 113 113 ILE C C 178.499 0.3 1 487 113 113 ILE CA C 66.281 0.3 1 488 113 113 ILE CB C 37.316 0.3 1 489 113 113 ILE N N 119.464 0.3 1 490 114 114 PHE H H 7.721 0.020 1 491 114 114 PHE C C 178.217 0.3 1 492 114 114 PHE CA C 61.559 0.3 1 493 114 114 PHE CB C 39.471 0.3 1 494 114 114 PHE N N 122.922 0.3 1 495 115 115 HIS H H 8.155 0.020 1 496 115 115 HIS C C 177.286 0.3 1 497 115 115 HIS CA C 59.380 0.3 1 498 115 115 HIS CB C 31.865 0.3 1 499 115 115 HIS N N 118.560 0.3 1 500 116 116 PHE H H 8.564 0.020 1 501 116 116 PHE C C 179.026 0.3 1 502 116 116 PHE CA C 59.461 0.3 1 503 116 116 PHE CB C 37.189 0.3 1 504 116 116 PHE N N 111.472 0.3 1 505 117 117 THR H H 7.620 0.020 1 506 117 117 THR C C 172.935 0.3 1 507 117 117 THR CA C 67.088 0.3 1 508 117 117 THR CB C 67.126 0.3 1 509 117 117 THR N N 119.012 0.3 1 510 118 118 GLY H H 6.666 0.020 1 511 118 118 GLY CA C 44.167 0.3 1 512 118 118 GLY N N 107.917 0.3 1 513 121 121 SER H H 8.322 0.020 1 514 121 121 SER C C 176.061 0.3 1 515 121 121 SER CA C 61.035 0.3 1 516 121 121 SER N N 113.354 0.3 1 517 122 122 TYR H H 6.514 0.020 1 518 122 122 TYR C C 176.293 0.3 1 519 122 122 TYR CA C 59.057 0.3 1 520 122 122 TYR CB C 38.711 0.3 1 521 122 122 TYR N N 124.681 0.3 1 522 123 123 LEU H H 7.428 0.020 1 523 123 123 LEU C C 179.774 0.3 1 524 123 123 LEU CA C 56.878 0.3 1 525 123 123 LEU CB C 39.978 0.3 1 526 123 123 LEU N N 117.997 0.3 1 527 124 124 ILE H H 8.453 0.020 1 528 124 124 ILE C C 178.830 0.3 1 529 124 124 ILE CA C 65.151 0.3 1 530 124 124 ILE CB C 37.063 0.3 1 531 124 124 ILE N N 119.012 0.3 1 532 125 125 ARG H H 7.004 0.020 1 533 125 125 ARG C C 179.762 0.3 1 534 125 125 ARG CA C 59.057 0.3 1 535 125 125 ARG CB C 28.950 0.3 1 536 125 125 ARG N N 121.174 0.3 1 537 126 126 ILE H H 7.579 0.020 1 538 126 126 ILE C C 178.352 0.3 1 539 126 126 ILE CA C 62.205 0.3 1 540 126 126 ILE CB C 35.415 0.3 1 541 126 126 ILE N N 122.299 0.3 1 542 127 127 ARG H H 8.715 0.020 1 543 127 127 ARG C C 179.786 0.3 1 544 127 127 ARG CA C 59.986 0.3 1 545 127 127 ARG CB C 29.330 0.3 1 546 127 127 ARG N N 119.354 0.3 1 547 128 128 ALA H H 7.978 0.020 1 548 128 128 ALA C C 180.325 0.3 1 549 128 128 ALA CA C 54.740 0.3 1 550 128 128 ALA CB C 17.161 0.3 1 551 128 128 ALA N N 122.873 0.3 1 552 129 129 ALA H H 7.519 0.020 1 553 129 129 ALA C C 181.539 0.3 1 554 129 129 ALA CA C 54.498 0.3 1 555 129 129 ALA CB C 17.478 0.3 1 556 129 129 ALA N N 121.846 0.3 1 557 130 130 LEU H H 8.296 0.020 1 558 130 130 LEU C C 179.909 0.3 1 559 130 130 LEU CA C 56.999 0.3 1 560 130 130 LEU CB C 40.422 0.3 1 561 130 130 LEU N N 119.134 0.3 1 562 131 131 LYS H H 8.281 0.020 1 563 131 131 LYS C C 180.289 0.3 1 564 131 131 LYS CA C 59.017 0.3 1 565 131 131 LYS CB C 31.232 0.3 1 566 131 131 LYS N N 122.299 0.3 1 567 132 132 LYS H H 7.317 0.020 1 568 132 132 LYS C C 177.482 0.3 1 569 132 132 LYS CA C 58.492 0.3 1 570 132 132 LYS CB C 31.232 0.3 1 571 132 132 LYS N N 118.743 0.3 1 572 133 133 LYS H H 7.327 0.020 1 573 133 133 LYS C C 174.614 0.3 1 574 133 133 LYS CA C 54.780 0.3 1 575 133 133 LYS CB C 32.182 0.3 1 576 133 133 LYS N N 117.093 0.3 1 577 134 134 ASN H H 7.938 0.020 1 578 134 134 ASN C C 173.965 0.3 1 579 134 134 ASN CA C 54.296 0.3 1 580 134 134 ASN CB C 36.175 0.3 1 581 134 134 ASN N N 113.012 0.3 1 582 135 135 TYR H H 7.741 0.020 1 583 135 135 TYR C C 176.342 0.3 1 584 135 135 TYR CA C 55.668 0.3 1 585 135 135 TYR CB C 41.563 0.3 1 586 135 135 TYR N N 115.725 0.3 1 587 136 136 LYS H H 9.296 0.020 1 588 136 136 LYS C C 173.475 0.3 1 589 136 136 LYS CA C 54.901 0.3 1 590 136 136 LYS CB C 34.718 0.3 1 591 136 136 LYS N N 122.641 0.3 1 592 137 137 LEU H H 8.776 0.020 1 593 137 137 LEU C C 175.423 0.3 1 594 137 137 LEU CA C 53.126 0.3 1 595 137 137 LEU CB C 45.746 0.3 1 596 137 137 LEU N N 127.284 0.3 1 597 138 138 ASN H H 8.811 0.020 1 598 138 138 ASN C C 174.933 0.3 1 599 138 138 ASN CA C 52.117 0.3 1 600 138 138 ASN CB C 37.506 0.3 1 601 138 138 ASN N N 125.818 0.3 1 602 139 139 GLN H H 9.220 0.020 1 603 139 139 GLN CA C 56.838 0.3 1 604 139 139 GLN CB C 25.717 0.3 1 605 139 139 GLN N N 116.861 0.3 1 606 140 140 TYR H H 8.549 0.020 1 607 140 140 TYR CA C 56.757 0.3 1 608 140 140 TYR CB C 37.570 0.3 1 609 140 140 TYR N N 120.600 0.3 1 610 141 141 GLY H H 7.186 0.020 1 611 141 141 GLY CA C 43.844 0.3 1 612 141 141 GLY N N 105.986 0.3 1 613 142 142 LEU H H 7.539 0.020 1 614 142 142 LEU C C 173.340 0.3 1 615 142 142 LEU CA C 52.520 0.3 1 616 142 142 LEU CB C 44.351 0.3 1 617 142 142 LEU N N 120.038 0.3 1 618 143 143 PHE H H 9.084 0.020 1 619 143 143 PHE C C 173.977 0.3 1 620 143 143 PHE CA C 52.641 0.3 1 621 143 143 PHE CB C 44.668 0.3 1 622 143 143 PHE N N 124.229 0.3 1 623 144 144 LYS H H 9.281 0.020 1 624 144 144 LYS C C 175.092 0.3 1 625 144 144 LYS CA C 58.856 0.3 1 626 144 144 LYS CB C 38.584 0.3 1 627 144 144 LYS N N 127.858 0.3 1 628 145 145 ASN H H 9.205 0.020 1 629 145 145 ASN C C 175.779 0.3 1 630 145 145 ASN CA C 57.726 0.3 1 631 145 145 ASN CB C 34.654 0.3 1 632 145 145 ASN N N 128.188 0.3 1 633 146 146 GLN H H 8.983 0.020 1 634 146 146 GLN C C 175.399 0.3 1 635 146 146 GLN CA C 58.815 0.3 1 636 146 146 GLN CB C 32.626 0.3 1 637 146 146 GLN N N 129.655 0.3 1 638 147 147 THR H H 8.029 0.020 1 639 147 147 THR C C 173.254 0.3 1 640 147 147 THR CA C 61.721 0.3 1 641 147 147 THR CB C 70.274 0.3 1 642 147 147 THR N N 117.936 0.3 1 643 148 148 LEU H H 8.635 0.020 1 644 148 148 LEU CA C 55.466 0.3 1 645 148 148 LEU CB C 41.689 0.3 1 646 148 148 LEU N N 130.681 0.3 1 647 149 149 VAL H H 8.968 0.020 1 648 149 149 VAL CA C 59.178 0.3 1 649 149 149 VAL CB C 31.675 0.3 1 650 149 149 VAL N N 130.803 0.3 1 651 151 151 LEU H H 7.872 0.020 1 652 151 151 LEU CA C 54.013 0.3 1 653 151 151 LEU CB C 44.098 0.3 1 654 151 151 LEU N N 124.290 0.3 1 655 153 153 ILE H H 7.125 0.020 1 656 153 153 ILE C C 175.877 0.3 1 657 153 153 ILE CA C 58.694 0.3 1 658 153 153 ILE CB C 41.689 0.3 1 659 153 153 ILE N N 114.943 0.3 1 660 154 154 THR H H 9.286 0.020 1 661 154 154 THR C C 174.945 0.3 1 662 154 154 THR CA C 62.124 0.3 1 663 154 154 THR CB C 70.718 0.3 1 664 154 154 THR N N 111.766 0.3 1 665 155 155 THR H H 7.645 0.020 1 666 155 155 THR CA C 58.936 0.3 1 667 155 155 THR CB C 72.683 0.3 1 668 155 155 THR N N 111.766 0.3 1 669 157 157 LYS H H 8.175 0.020 1 670 157 157 LYS C C 178.781 0.3 1 671 157 157 LYS CA C 60.026 0.3 1 672 157 157 LYS CB C 31.422 0.3 1 673 157 157 LYS N N 119.464 0.3 1 674 158 158 GLU H H 7.519 0.020 1 675 158 158 GLU C C 178.867 0.3 1 676 158 158 GLU CA C 58.492 0.3 1 677 158 158 GLU CB C 29.330 0.3 1 678 158 158 GLU N N 118.340 0.3 1 679 159 159 LEU H H 7.524 0.020 1 680 159 159 LEU C C 176.526 0.3 1 681 159 159 LEU CA C 58.170 0.3 1 682 159 159 LEU CB C 39.915 0.3 1 683 159 159 LEU N N 120.710 0.3 1 684 160 160 ILE H H 7.741 0.020 1 685 160 160 ILE C C 177.213 0.3 1 686 160 160 ILE CA C 65.030 0.3 1 687 160 160 ILE CB C 37.506 0.3 1 688 160 160 ILE N N 118.217 0.3 1 689 161 161 LYS H H 7.382 0.020 1 690 161 161 LYS C C 180.999 0.3 1 691 161 161 LYS CA C 58.815 0.3 1 692 161 161 LYS CB C 30.978 0.3 1 693 161 161 LYS N N 118.450 0.3 1 694 162 162 GLU H H 8.210 0.020 1 695 162 162 GLU C C 178.818 0.3 1 696 162 162 GLU CA C 58.049 0.3 1 697 162 162 GLU CB C 27.936 0.3 1 698 162 162 GLU N N 121.846 0.3 1 699 163 163 LEU H H 7.796 0.020 1 700 163 163 LEU C C 176.784 0.3 1 701 163 163 LEU CA C 55.022 0.3 1 702 163 163 LEU CB C 41.309 0.3 1 703 163 163 LEU N N 116.751 0.3 1 704 164 164 GLY H H 7.589 0.020 1 705 164 164 GLY C C 174.492 0.3 1 706 164 164 GLY CA C 44.732 0.3 1 707 164 164 GLY N N 104.849 0.3 1 708 165 165 PHE H H 7.251 0.020 1 709 165 165 PHE CA C 55.668 0.3 1 710 165 165 PHE CB C 40.485 0.3 1 711 165 165 PHE N N 118.902 0.3 1 712 166 166 THR H H 8.407 0.020 1 713 166 166 THR CA C 62.245 0.3 1 714 166 166 THR CB C 69.323 0.3 1 715 166 166 THR N N 117.093 0.3 1 716 168 168 ARG H H 7.160 0.020 1 717 168 168 ARG CA C 52.238 0.3 1 718 168 168 ARG CB C 31.992 0.3 1 719 168 168 ARG N N 127.431 0.3 1 720 171 171 LYS H H 8.210 0.020 1 721 171 171 LYS C C 176.416 0.3 1 722 171 171 LYS CA C 57.605 0.3 1 723 171 171 LYS CB C 31.929 0.3 1 724 171 171 LYS N N 113.574 0.3 1 725 172 172 LYS H H 7.761 0.020 1 726 172 172 LYS C C 175.717 0.3 1 727 172 172 LYS CA C 54.175 0.3 1 728 172 172 LYS CB C 31.612 0.3 1 729 172 172 LYS N N 117.313 0.3 1 730 173 173 ARG H H 6.885 0.020 1 731 173 173 ARG C C 172.850 0.3 1 732 173 173 ARG CA C 56.878 0.3 1 733 173 173 ARG CB C 28.506 0.3 1 734 173 173 ARG N N 122.056 0.3 1 735 174 174 LEU H H 7.150 0.020 1 736 174 174 LEU CA C 56.878 0.3 1 737 174 174 LEU CB C 44.098 0.3 1 738 174 174 LEU N N 128.640 0.3 1 stop_ save_