data_6184 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Model for the Catalytic Domain of the Proofreading Epsilon Subunit of E.coli DNA Polymerase III Based on NMR Structural Data ; _BMRB_accession_number 6184 _BMRB_flat_file_name bmr6184.str _Entry_type original _Submission_date 2004-04-20 _Accession_date 2004-04-21 _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 DeRose Eugene F. . 2 Li Dawei . . 3 Darden Thomas . . 4 Harvey Scott . . 5 Perrino Fred W. . 6 Schaaper Roel M. . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 225 "13C chemical shifts" 534 "15N chemical shifts" 157 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2004-06-25 original author . stop_ _Original_release_date 2004-06-25 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; Model for the Catalytic Domain of the Proofreading Epsilon Subunit of Escherichia coli DNA Polymerase III Based on NMR Structural Data ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 11772007 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 DeRose Eugene F . stop_ _Journal_abbreviation Biochemistry _Journal_volume 41 _Journal_issue . _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 94 _Page_last 110 _Year 2002 _Details . save_ ####################################### # Cited references within the entry # ####################################### save_ref-1 _Saveframe_category citation _Citation_full ; DeRose, E.F., Darden, T., Harvey, S., Gabel, S., Perrino, F. W., Schaaper, R. M., and London, R. E. Elucidation of the Epsilon-Theta Subunit Interface of Escherichia coli DNA Polymerase III by NMR Spectroscopy, Biochemistry 42, 3635-3644 (2003). Biochemistry. 2003 Apr 8;42(13):3635-44. ; _Citation_title . _Citation_status . _Citation_type . _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 12667053 _Journal_abbreviation . _Journal_name_full . _Journal_volume . _Journal_issue . _Journal_CSD . _Book_title . _Book_chapter_title . _Book_volume . _Book_series . _Book_publisher . _Book_publisher_city . _Book_ISBN . _Conference_title . _Conference_site . _Conference_state_province . _Conference_country . _Conference_start_date . _Conference_end_date . _Conference_abstract_number . _Thesis_institution . _Thesis_institution_city . _Thesis_institution_country . _Page_first . _Page_last . _Year . _Details . save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name 'N-terminal domain of the epsilon subunit of E. coli DNA polymerase III' _Abbreviation_common 'N-terminal domain of the epsilon subunit of E. coli DNA polymerase III' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'N-terminal domain of the epsilon subunit of E. coli DNA polymerase III' $polymerase_III stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state monomer _System_paramagnetic no _System_thiol_state 'all free' _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_polymerase_III _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common epsilon-186 _Molecular_mass . _Mol_thiol_state 'all free' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 186 _Mol_residue_sequence ; MSTAITRQIVLDTETTGMNQ IGAHYEGHKIIEIGAVEVVN RRLTGNNFHVYLKPDRLVDP EAFGVHGIADEFLLDKPTFA EVADEFMDYIRGAELVIHNA AFDIGFMDYEFSLLKRDIPK TNTFCKVTDSLAVARKMFPG KRNSLDALCARYEIDNSKRT LHGALLDAQILAEVYLAMTG GQTSMA ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 -3 MET 2 -2 SER 3 -1 THR 4 1 ALA 5 2 ILE 6 3 THR 7 4 ARG 8 5 GLN 9 6 ILE 10 7 VAL 11 8 LEU 12 9 ASP 13 10 THR 14 11 GLU 15 12 THR 16 13 THR 17 14 GLY 18 15 MET 19 16 ASN 20 17 GLN 21 18 ILE 22 19 GLY 23 20 ALA 24 21 HIS 25 22 TYR 26 23 GLU 27 24 GLY 28 25 HIS 29 26 LYS 30 27 ILE 31 28 ILE 32 29 GLU 33 30 ILE 34 31 GLY 35 32 ALA 36 33 VAL 37 34 GLU 38 35 VAL 39 36 VAL 40 37 ASN 41 38 ARG 42 39 ARG 43 40 LEU 44 41 THR 45 42 GLY 46 43 ASN 47 44 ASN 48 45 PHE 49 46 HIS 50 47 VAL 51 48 TYR 52 49 LEU 53 50 LYS 54 51 PRO 55 52 ASP 56 53 ARG 57 54 LEU 58 55 VAL 59 56 ASP 60 57 PRO 61 58 GLU 62 59 ALA 63 60 PHE 64 61 GLY 65 62 VAL 66 63 HIS 67 64 GLY 68 65 ILE 69 66 ALA 70 67 ASP 71 68 GLU 72 69 PHE 73 70 LEU 74 71 LEU 75 72 ASP 76 73 LYS 77 74 PRO 78 75 THR 79 76 PHE 80 77 ALA 81 78 GLU 82 79 VAL 83 80 ALA 84 81 ASP 85 82 GLU 86 83 PHE 87 84 MET 88 85 ASP 89 86 TYR 90 87 ILE 91 88 ARG 92 89 GLY 93 90 ALA 94 91 GLU 95 92 LEU 96 93 VAL 97 94 ILE 98 95 HIS 99 96 ASN 100 97 ALA 101 98 ALA 102 99 PHE 103 100 ASP 104 101 ILE 105 102 GLY 106 103 PHE 107 104 MET 108 105 ASP 109 106 TYR 110 107 GLU 111 108 PHE 112 109 SER 113 110 LEU 114 111 LEU 115 112 LYS 116 113 ARG 117 114 ASP 118 115 ILE 119 116 PRO 120 117 LYS 121 118 THR 122 119 ASN 123 120 THR 124 121 PHE 125 122 CYS 126 123 LYS 127 124 VAL 128 125 THR 129 126 ASP 130 127 SER 131 128 LEU 132 129 ALA 133 130 VAL 134 131 ALA 135 132 ARG 136 133 LYS 137 134 MET 138 135 PHE 139 136 PRO 140 137 GLY 141 138 LYS 142 139 ARG 143 140 ASN 144 141 SER 145 142 LEU 146 143 ASP 147 144 ALA 148 145 LEU 149 146 CYS 150 147 ALA 151 148 ARG 152 149 TYR 153 150 GLU 154 151 ILE 155 152 ASP 156 153 ASN 157 154 SER 158 155 LYS 159 156 ARG 160 157 THR 161 158 LEU 162 159 HIS 163 160 GLY 164 161 ALA 165 162 LEU 166 163 LEU 167 164 ASP 168 165 ALA 169 166 GLN 170 167 ILE 171 168 LEU 172 169 ALA 173 170 GLU 174 171 VAL 175 172 TYR 176 173 LEU 177 174 ALA 178 175 MET 179 176 THR 180 177 GLY 181 178 GLY 182 179 GLN 183 180 THR 184 181 SER 185 182 MET 186 183 ALA stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-01-28 loop_ _Database_name _Database_accession_code _Database_entry_mol_name _Sequence_query_to_submitted_percentage _Sequence_subject_length _Sequence_identity _Sequence_positive _Sequence_homology_expectation_value PDB 1J53 "Structure Of The N-Terminal Exonuclease Domain Of The Epsilon Subunit Of E.Coli Dna Polymerase Iii At Ph 8.5" 100.00 186 100.00 100.00 5.44e-134 PDB 1J54 "Structure Of The N-Terminal Exonuclease Domain Of The Epsilon Subunit Of E.Coli Dna Polymerase Iii At Ph 5.8" 100.00 186 100.00 100.00 5.44e-134 PDB 2GUI "Structure And Function Of Cyclized Versions Of The Proofread Exonuclease Subunit Of E. Coli Dna Polymerase Iii" 99.46 194 100.00 100.00 3.72e-133 PDB 2IDO "Structure Of The E. Coli Pol Iii Epsilon-Hot Proofreading Complex" 100.00 186 100.00 100.00 5.44e-134 PDB 2XY8 "Paramagnetic-Based Nmr Structure Of The Complex Between The N-Terminal Epsilon Domain And The Theta Domain Of The Dna Polymeras" 100.00 186 100.00 100.00 5.44e-134 DBJ BAA77886 "DNA polymerase III epsilon subunit [Escherichia coli str. K-12 substr. W3110]" 100.00 243 100.00 100.00 2.76e-134 DBJ BAB33634 "DNA polymerase III epsilon subunit [Escherichia coli O157:H7 str. Sakai]" 100.00 243 100.00 100.00 2.85e-134 DBJ BAG75735 "DNA polymerase III epsilon subunit [Escherichia coli SE11]" 100.00 243 100.00 100.00 2.76e-134 DBJ BAI23571 "DNA polymerase III, epsilon subunit DnaQ [Escherichia coli O26:H11 str. 11368]" 100.00 243 100.00 100.00 2.76e-134 DBJ BAI29085 "DNA polymerase III, epsilon subunit DnaQ [Escherichia coli O103:H2 str. 12009]" 100.00 243 100.00 100.00 2.76e-134 EMBL CAA27661 "unnamed protein product [Escherichia coli]" 100.00 243 100.00 100.00 2.76e-134 EMBL CAP74779 "DNA polymerase III subunit epsilon [Escherichia coli LF82]" 100.00 243 99.46 99.46 1.00e-133 EMBL CAQ30730 "DNA polymerase III, epsilon subunit, subunit of DNA polymerase III, core enzyme and DNA polymerase III, holoenzyme [Escherichia" 100.00 243 100.00 100.00 2.58e-134 EMBL CAQ87813 "DNA polymerase III epsilon subunit [Escherichia fergusonii ATCC 35469]" 100.00 243 100.00 100.00 2.53e-134 EMBL CAQ97098 "DNA polymerase III epsilon subunit [Escherichia coli IAI1]" 100.00 243 100.00 100.00 2.76e-134 GB AAA24564 "DNA polymerase III epsilon subunit [Escherichia coli]" 100.00 243 100.00 100.00 2.76e-134 GB AAB08637 "DNA polymerase III epsilon chain [Escherichia coli]" 100.00 246 100.00 100.00 2.16e-134 GB AAC73320 "DNA polymerase III epsilon subunit [Escherichia coli str. K-12 substr. MG1655]" 100.00 243 100.00 100.00 2.76e-134 GB AAG54511 "DNA polymerase III, epsilon subunit [Escherichia coli O157:H7 str. EDL933]" 100.00 243 100.00 100.00 2.85e-134 GB AAN41863 "DNA polymerase III, epsilon subunit [Shigella flexneri 2a str. 301]" 100.00 243 100.00 100.00 2.53e-134 REF NP_285903 "DNA polymerase III subunit epsilon [Escherichia coli O157:H7 str. EDL933]" 100.00 243 100.00 100.00 2.85e-134 REF NP_308238 "DNA polymerase III subunit epsilon [Escherichia coli O157:H7 str. Sakai]" 100.00 243 100.00 100.00 2.85e-134 REF NP_414751 "DNA polymerase III epsilon subunit [Escherichia coli str. K-12 substr. MG1655]" 100.00 243 100.00 100.00 2.76e-134 REF NP_706156 "DNA polymerase III subunit epsilon [Shigella flexneri 2a str. 301]" 100.00 243 100.00 100.00 2.53e-134 REF NP_752198 "DNA polymerase III subunit epsilon [Escherichia coli CFT073]" 100.00 246 100.00 100.00 2.93e-134 SP P03007 "RecName: Full=DNA polymerase III subunit epsilon [Escherichia coli K-12]" 100.00 243 100.00 100.00 2.76e-134 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $polymerase_III 'Escherichia coli' 562 Bacteria . Escherichia coli 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 $polymerase_III 'recombinant technology' 'E. coli' Escherichia coli . . 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 $polymerase_III 0.72 mM '[U-2H; U-13C; U-15N]' stop_ save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_INOVA_600 _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model INOVA _Field_strength 600 _Details . save_ save_UnityPlus_500 _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model UnityPlus _Field_strength 500 _Details . save_ ############################# # NMR applied experiments # ############################# save_HNCA_1 _Saveframe_category NMR_applied_experiment _Experiment_name HNCA _Sample_label $sample_1 save_ save_HN(CO)CA_2 _Saveframe_category NMR_applied_experiment _Experiment_name HN(CO)CA _Sample_label $sample_1 save_ save_HN(CA)CB_3 _Saveframe_category NMR_applied_experiment _Experiment_name HN(CA)CB _Sample_label $sample_1 save_ save_HN(COCA)CB_4 _Saveframe_category NMR_applied_experiment _Experiment_name HN(COCA)CB _Sample_label $sample_1 save_ save_HNCO_5 _Saveframe_category NMR_applied_experiment _Experiment_name HNCO _Sample_label $sample_1 save_ save_H(CCO)NH-TOCSY_6 _Saveframe_category NMR_applied_experiment _Experiment_name H(CCO)NH-TOCSY _Sample_label $sample_1 save_ save_(H)C(CO)NH-TOCSY_7 _Saveframe_category NMR_applied_experiment _Experiment_name (H)C(CO)NH-TOCSY _Sample_label $sample_1 save_ save_3D_15N-separated_NOESY_8 _Saveframe_category NMR_applied_experiment _Experiment_name '3D 15N-separated NOESY' _Sample_label $sample_1 save_ ####################### # Sample conditions # ####################### save_Ex-cond_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 7.0 0.2 pH temperature 293 0.1 K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference _Saveframe_category chemical_shift_reference _Details . loop_ _Mol_common_name _Atom_type _Atom_isotope_number _Atom_group _Chem_shift_units _Chem_shift_value _Reference_method _Reference_type _External_reference_sample_geometry _External_reference_location _External_reference_axis _Indirect_shift_ratio DSS H 1 'methyl protons' ppm 0 internal direct . . . 1.0 DSS C 13 'methyl protons' ppm 0 internal indirect . . . 0.251449530 DSS N 15 'methyl protons' ppm 0 internal 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_1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $Ex-cond_1 _Chem_shift_reference_set_label $chemical_shift_reference _Mol_system_component_name 'N-terminal domain of the epsilon subunit of E. coli DNA polymerase III' _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 1 4 ALA CA C 52.028 0.3 1 2 1 4 ALA CB C 18.411 0.3 1 3 1 4 ALA C C 177.274 0.3 1 4 2 5 ILE N N 121.057 0.3 1 5 2 5 ILE H H 8.198 0.03 1 6 2 5 ILE CA C 60.425 0.3 1 7 2 5 ILE CB C 38.010 0.3 1 8 2 5 ILE CD1 C 12.698 0.3 1 9 2 5 ILE HD1 H 0.826 0.03 1 10 2 5 ILE C C 176.619 0.3 1 11 3 6 THR N N 119.713 0.3 1 12 3 6 THR H H 8.476 0.03 1 13 3 6 THR CA C 61.552 0.3 1 14 3 6 THR CB C 69.400 0.3 1 15 3 6 THR C C 173.463 0.3 1 16 4 7 ARG N N 125.395 0.3 1 17 4 7 ARG H H 8.194 0.03 1 18 4 7 ARG CA C 55.027 0.3 1 19 4 7 ARG CB C 31.584 0.3 1 20 4 7 ARG C C 174.212 0.3 1 21 5 8 GLN N N 124.677 0.3 1 22 5 8 GLN H H 9.262 0.03 1 23 5 8 GLN CA C 53.641 0.3 1 24 5 8 GLN CB C 31.133 0.3 1 25 5 8 GLN C C 174.419 0.3 1 26 6 9 ILE N N 122.525 0.3 1 27 6 9 ILE H H 9.115 0.03 1 28 6 9 ILE CA C 57.611 0.3 1 29 6 9 ILE CB C 37.950 0.3 1 30 6 9 ILE CD1 C 11.153 0.3 1 31 6 9 ILE HD1 H 0.331 0.03 1 32 6 9 ILE C C 174.270 0.3 1 33 7 10 VAL N N 129.755 0.3 1 34 7 10 VAL H H 8.961 0.03 1 35 7 10 VAL CA C 60.803 0.3 1 36 7 10 VAL CB C 30.646 0.3 1 37 7 10 VAL CG2 C 22.548 0.3 2 38 7 10 VAL HG2 H 0.918 0.03 4 39 7 10 VAL CG1 C 19.550 0.3 2 40 7 10 VAL HG1 H 0.662 0.03 4 41 7 10 VAL C C 175.494 0.3 1 42 8 11 LEU N N 127.865 0.3 1 43 8 11 LEU H H 8.393 0.03 1 44 8 11 LEU CA C 54.260 0.3 1 45 8 11 LEU CB C 47.332 0.3 1 46 8 11 LEU CD1 C 26.956 0.3 2 47 8 11 LEU HD1 H 0.983 0.03 4 48 8 11 LEU C C 173.690 0.3 1 49 9 12 ASP N N 121.821 0.3 1 50 9 12 ASP H H 9.298 0.03 1 51 9 12 ASP CA C 53.262 0.3 1 52 9 12 ASP CB C 43.656 0.3 1 53 9 12 ASP C C 173.722 0.3 1 54 10 13 THR N N 114.431 0.3 1 55 10 13 THR H H 8.142 0.03 1 56 10 13 THR CA C 59.933 0.3 1 57 10 13 THR CB C 72.235 0.3 1 58 10 13 THR C C 174.034 0.3 1 59 11 14 GLU N N 116.134 0.3 1 60 11 14 GLU H H 8.520 0.03 1 61 11 14 GLU CA C 53.364 0.3 1 62 11 14 GLU CB C 31.281 0.3 1 63 11 14 GLU C C 177.661 0.3 1 64 12 15 THR N N 111.611 0.3 1 65 12 15 THR H H 9.014 0.03 1 66 12 15 THR CA C 60.407 0.3 1 67 12 15 THR CB C 73.124 0.3 1 68 12 15 THR C C 174.114 0.3 1 69 13 16 THR N N 107.499 0.3 1 70 13 16 THR H H 8.895 0.03 1 71 13 16 THR CA C 63.963 0.3 1 72 13 16 THR CB C 69.212 0.3 1 73 13 16 THR C C 172.028 0.3 1 74 14 17 GLY N N 104.784 0.3 1 75 14 17 GLY H H 7.568 0.03 1 76 14 17 GLY CA C 43.569 0.3 1 77 14 17 GLY C C 170.760 0.3 1 78 15 18 MET N N 113.650 0.3 1 79 15 18 MET H H 7.819 0.03 1 80 15 18 MET CA C 54.501 0.3 1 81 15 18 MET CB C 33.684 0.3 1 82 15 18 MET C C 173.664 0.3 1 83 16 19 ASN N N 119.143 0.3 1 84 16 19 ASN H H 8.998 0.03 1 85 16 19 ASN CA C 51.812 0.3 1 86 16 19 ASN CB C 39.448 0.3 1 87 17 20 GLN CA C 56.582 0.3 1 88 17 20 GLN CB C 28.600 0.3 1 89 18 21 ILE N N 117.126 0.3 1 90 18 21 ILE H H 7.489 0.03 1 91 18 21 ILE CA C 59.602 0.3 1 92 18 21 ILE CB C 38.894 0.3 1 93 18 21 ILE CD1 C 12.698 0.3 1 94 18 21 ILE HD1 H 0.826 0.03 1 95 18 21 ILE C C 175.447 0.3 1 96 19 22 GLY N N 111.938 0.3 1 97 19 22 GLY H H 8.167 0.03 1 98 19 22 GLY CA C 43.749 0.3 1 99 19 22 GLY C C 176.098 0.3 1 100 20 23 ALA N N 124.466 0.3 1 101 20 23 ALA H H 8.252 0.03 1 102 20 23 ALA CA C 51.943 0.3 1 103 20 23 ALA CB C 16.408 0.3 1 104 20 23 ALA C C 181.151 0.3 1 105 21 24 HIS N N 121.331 0.3 1 106 21 24 HIS H H 8.225 0.03 1 107 21 24 HIS CA C 59.042 0.3 1 108 21 24 HIS CB C 30.258 0.3 1 109 22 25 TYR C C 174.783 0.3 1 110 23 26 GLU N N 120.437 0.3 1 111 23 26 GLU H H 5.545 0.03 1 112 23 26 GLU CA C 58.459 0.3 1 113 23 26 GLU CB C 28.615 0.3 1 114 23 26 GLU C C 177.471 0.3 1 115 24 27 GLY N N 111.680 0.3 1 116 24 27 GLY H H 8.088 0.03 1 117 24 27 GLY CA C 45.406 0.3 1 118 24 27 GLY C C 173.262 0.3 1 119 25 28 HIS N N 120.883 0.3 1 120 25 28 HIS H H 8.437 0.03 1 121 25 28 HIS CA C 56.853 0.3 1 122 25 28 HIS CB C 35.423 0.3 1 123 25 28 HIS C C 173.640 0.3 1 124 26 29 LYS N N 113.637 0.3 1 125 26 29 LYS H H 8.485 0.03 1 126 26 29 LYS CA C 52.417 0.3 1 127 26 29 LYS CB C 34.216 0.3 1 128 26 29 LYS C C 177.169 0.3 1 129 27 30 ILE N N 121.419 0.3 1 130 27 30 ILE H H 9.606 0.03 1 131 27 30 ILE CA C 62.799 0.3 1 132 27 30 ILE CB C 37.754 0.3 1 133 27 30 ILE CD1 C 13.230 0.3 1 134 27 30 ILE HD1 H 0.642 0.03 1 135 27 30 ILE C C 175.571 0.3 1 136 28 31 ILE N N 117.483 0.3 1 137 28 31 ILE H H 8.869 0.03 1 138 28 31 ILE CA C 60.571 0.3 1 139 28 31 ILE CB C 38.538 0.3 1 140 28 31 ILE CD1 C 14.645 0.3 1 141 28 31 ILE HD1 H 0.352 0.03 1 142 28 31 ILE C C 174.598 0.3 1 143 29 32 GLU N N 123.047 0.3 1 144 29 32 GLU H H 7.506 0.03 1 145 29 32 GLU CA C 55.456 0.3 1 146 29 32 GLU CB C 32.579 0.3 1 147 29 32 GLU C C 174.595 0.3 1 148 30 33 ILE N N 124.011 0.3 1 149 30 33 ILE H H 8.478 0.03 1 150 30 33 ILE CA C 60.725 0.3 1 151 30 33 ILE CB C 41.284 0.3 1 152 30 33 ILE CD1 C 12.158 0.3 1 153 30 33 ILE HD1 H 0.056 0.03 1 154 30 33 ILE C C 174.422 0.3 1 155 31 34 GLY N N 114.573 0.3 1 156 31 34 GLY H H 9.154 0.03 1 157 31 34 GLY CA C 43.361 0.3 1 158 31 34 GLY C C 170.676 0.3 1 159 32 35 ALA N N 125.367 0.3 1 160 32 35 ALA H H 9.486 0.03 1 161 32 35 ALA CA C 50.528 0.3 1 162 32 35 ALA CB C 23.089 0.3 1 163 32 35 ALA C C 175.374 0.3 1 164 33 36 VAL N N 113.618 0.3 1 165 33 36 VAL H H 8.827 0.03 1 166 33 36 VAL CA C 58.119 0.3 1 167 33 36 VAL CB C 34.697 0.3 1 168 33 36 VAL CG2 C 21.313 0.3 2 169 33 36 VAL HG2 H 0.756 0.03 4 170 33 36 VAL CG1 C 20.978 0.3 2 171 33 36 VAL HG1 H 0.688 0.03 4 172 33 36 VAL C C 174.477 0.3 1 173 34 37 GLU N N 121.744 0.3 1 174 34 37 GLU H H 6.455 0.03 1 175 34 37 GLU CA C 55.697 0.3 1 176 34 37 GLU CB C 32.423 0.3 1 177 34 37 GLU C C 175.276 0.3 1 178 35 38 VAL N N 130.067 0.3 1 179 35 38 VAL H H 9.512 0.03 1 180 35 38 VAL CA C 60.594 0.3 1 181 35 38 VAL CB C 33.818 0.3 1 182 35 38 VAL CG2 C 21.953 0.3 2 183 35 38 VAL HG2 H 0.827 0.03 4 184 35 38 VAL CG1 C 20.730 0.3 2 185 35 38 VAL HG1 H 0.824 0.03 4 186 35 38 VAL C C 175.239 0.3 1 187 36 39 VAL N N 125.489 0.3 1 188 36 39 VAL H H 8.848 0.03 1 189 36 39 VAL CA C 61.038 0.3 1 190 36 39 VAL CB C 34.291 0.3 1 191 36 39 VAL CG2 C 22.068 0.3 2 192 36 39 VAL HG2 H 0.958 0.03 4 193 36 39 VAL CG1 C 21.316 0.3 2 194 36 39 VAL HG1 H 0.928 0.03 4 195 36 39 VAL C C 176.992 0.3 1 196 37 40 ASN N N 128.423 0.3 1 197 37 40 ASN H H 9.377 0.03 1 198 37 40 ASN CA C 53.990 0.3 1 199 37 40 ASN CB C 36.130 0.3 1 200 37 40 ASN C C 174.298 0.3 1 201 38 41 ARG N N 106.329 0.3 1 202 38 41 ARG H H 8.830 0.03 1 203 38 41 ARG CA C 57.988 0.3 1 204 38 41 ARG CB C 25.684 0.3 1 205 38 41 ARG C C 173.208 0.3 1 206 39 42 ARG N N 117.222 0.3 1 207 39 42 ARG H H 7.598 0.03 1 208 39 42 ARG CA C 53.927 0.3 1 209 39 42 ARG CB C 32.012 0.3 1 210 39 42 ARG C C 175.202 0.3 1 211 40 43 LEU N N 125.182 0.3 1 212 40 43 LEU H H 8.667 0.03 1 213 40 43 LEU CA C 55.644 0.3 1 214 40 43 LEU CB C 39.792 0.3 1 215 40 43 LEU CD1 C 25.414 0.3 2 216 40 43 LEU HD1 H 0.933 0.03 4 217 40 43 LEU C C 178.714 0.3 1 218 41 44 THR N N 114.708 0.3 1 219 41 44 THR H H 7.787 0.03 1 220 41 44 THR CA C 62.232 0.3 1 221 41 44 THR CB C 69.414 0.3 1 222 41 44 THR C C 177.168 0.3 1 223 42 45 GLY N N 111.510 0.3 1 224 42 45 GLY H H 9.847 0.03 1 225 42 45 GLY CA C 44.612 0.3 1 226 42 45 GLY C C 173.821 0.3 1 227 43 46 ASN N N 119.803 0.3 1 228 43 46 ASN H H 7.954 0.03 1 229 43 46 ASN CA C 51.946 0.3 1 230 43 46 ASN CB C 35.897 0.3 1 231 43 46 ASN C C 173.264 0.3 1 232 44 47 ASN N N 123.483 0.3 1 233 44 47 ASN H H 7.638 0.03 1 234 44 47 ASN CA C 51.991 0.3 1 235 44 47 ASN CB C 40.903 0.3 1 236 44 47 ASN C C 173.874 0.3 1 237 45 48 PHE N N 121.699 0.3 1 238 45 48 PHE H H 9.072 0.03 1 239 45 48 PHE CA C 57.354 0.3 1 240 45 48 PHE CB C 43.320 0.3 1 241 46 49 HIS N N 127.008 0.3 1 242 46 49 HIS H H 7.504 0.03 1 243 46 49 HIS CA C 53.161 0.3 1 244 46 49 HIS CB C 35.358 0.3 1 245 46 49 HIS C C 172.670 0.3 1 246 47 50 VAL N N 120.108 0.3 1 247 47 50 VAL H H 8.464 0.03 1 248 47 50 VAL CA C 59.837 0.3 1 249 47 50 VAL CB C 35.466 0.3 1 250 47 50 VAL CG2 C 22.279 0.3 2 251 47 50 VAL HG2 H 0.585 0.03 4 252 47 50 VAL CG1 C 20.110 0.3 2 253 47 50 VAL HG1 H 0.684 0.03 4 254 47 50 VAL C C 172.677 0.3 1 255 48 51 TYR N N 119.361 0.3 1 256 48 51 TYR H H 7.933 0.03 1 257 48 51 TYR CA C 57.086 0.3 1 258 48 51 TYR CB C 40.749 0.3 1 259 48 51 TYR C C 176.357 0.3 1 260 49 52 LEU N N 119.569 0.3 1 261 49 52 LEU H H 8.226 0.03 1 262 49 52 LEU CA C 51.716 0.3 1 263 49 52 LEU CB C 44.251 0.3 1 264 49 52 LEU CD1 C 24.982 0.3 2 265 49 52 LEU HD1 H 0.567 0.03 4 266 49 52 LEU CD2 C 26.234 0.3 2 267 49 52 LEU HD2 H 0.655 0.03 4 268 49 52 LEU C C 174.373 0.3 1 269 50 53 LYS N N 120.663 0.3 1 270 50 53 LYS H H 8.194 0.03 1 271 50 53 LYS CA C 53.216 0.3 1 272 50 53 LYS CB C 33.295 0.3 1 273 52 55 ASP C C 174.323 0.3 1 274 53 56 ARG N N 110.830 0.3 1 275 53 56 ARG H H 7.142 0.03 1 276 53 56 ARG CA C 54.243 0.3 1 277 53 56 ARG CB C 29.301 0.3 1 278 53 56 ARG C C 174.564 0.3 1 279 54 57 LEU N N 119.848 0.3 1 280 54 57 LEU H H 8.619 0.03 1 281 54 57 LEU CA C 54.102 0.3 1 282 54 57 LEU CB C 40.999 0.3 1 283 54 57 LEU CD1 C 21.879 0.3 2 284 54 57 LEU HD1 H 0.848 0.03 4 285 54 57 LEU CD2 C 25.866 0.3 2 286 54 57 LEU HD2 H 0.726 0.03 4 287 54 57 LEU C C 178.496 0.3 1 288 55 58 VAL N N 125.358 0.3 1 289 55 58 VAL H H 10.658 0.03 1 290 55 58 VAL CA C 63.248 0.3 1 291 55 58 VAL CB C 33.447 0.3 1 292 55 58 VAL CG2 C 22.395 0.3 2 293 55 58 VAL HG2 H 1.180 0.03 4 294 55 58 VAL CG1 C 21.670 0.3 2 295 55 58 VAL HG1 H 1.296 0.03 4 296 55 58 VAL C C 175.973 0.3 1 297 56 59 ASP N N 128.690 0.3 1 298 56 59 ASP H H 9.221 0.03 1 299 56 59 ASP CA C 52.895 0.3 1 300 56 59 ASP CB C 42.107 0.3 1 301 57 60 PRO CA C 65.159 0.3 1 302 57 60 PRO CB C 30.474 0.3 1 303 57 60 PRO C C 178.666 0.3 1 304 58 61 GLU N N 117.993 0.3 1 305 58 61 GLU H H 9.108 0.03 1 306 58 61 GLU CA C 58.846 0.3 1 307 58 61 GLU CB C 28.633 0.3 1 308 58 61 GLU C C 179.202 0.3 1 309 59 62 ALA N N 123.853 0.3 1 310 59 62 ALA H H 7.463 0.03 1 311 59 62 ALA CA C 54.082 0.3 1 312 59 62 ALA CB C 17.808 0.3 1 313 59 62 ALA C C 179.662 0.3 1 314 60 63 PHE N N 118.646 0.3 1 315 60 63 PHE H H 7.955 0.03 1 316 61 64 GLY N N 105.630 0.3 1 317 61 64 GLY H H 7.677 0.03 1 318 61 64 GLY CA C 46.057 0.3 1 319 61 64 GLY C C 173.117 0.3 1 320 62 65 VAL N N 118.883 0.3 1 321 62 65 VAL H H 7.035 0.03 1 322 62 65 VAL CA C 64.155 0.3 1 323 62 65 VAL CB C 32.008 0.3 1 324 62 65 VAL CG1 C 21.105 0.3 2 325 62 65 VAL HG1 H 0.913 0.03 4 326 62 65 VAL C C 177.075 0.3 1 327 63 66 HIS N N 113.194 0.3 1 328 63 66 HIS H H 7.157 0.03 1 329 63 66 HIS CA C 54.943 0.3 1 330 63 66 HIS CB C 31.148 0.3 1 331 63 66 HIS C C 177.315 0.3 1 332 64 67 GLY N N 111.191 0.3 1 333 64 67 GLY H H 8.374 0.03 1 334 64 67 GLY CA C 45.662 0.3 1 335 64 67 GLY C C 174.349 0.3 1 336 65 68 ILE N N 125.439 0.3 1 337 65 68 ILE H H 10.521 0.03 1 338 65 68 ILE CA C 61.980 0.3 1 339 65 68 ILE CB C 36.125 0.3 1 340 65 68 ILE CD1 C 13.800 0.3 1 341 65 68 ILE HD1 H 0.512 0.03 1 342 65 68 ILE C C 173.177 0.3 1 343 66 69 ALA N N 125.297 0.3 1 344 66 69 ALA H H 7.731 0.03 1 345 66 69 ALA CA C 50.734 0.3 1 346 66 69 ALA CB C 22.847 0.3 1 347 68 71 GLU CA C 61.593 0.3 1 348 68 71 GLU CB C 28.219 0.3 1 349 68 71 GLU C C 177.809 0.3 1 350 69 72 PHE N N 114.538 0.3 1 351 69 72 PHE H H 6.839 0.03 1 352 69 72 PHE CA C 58.621 0.3 1 353 69 72 PHE CB C 39.113 0.3 1 354 70 73 LEU N N 115.977 0.3 1 355 70 73 LEU H H 7.210 0.03 1 356 70 73 LEU CA C 54.404 0.3 1 357 70 73 LEU CB C 41.010 0.3 1 358 70 73 LEU CD1 C 21.237 0.3 2 359 70 73 LEU HD1 H 0.978 0.03 4 360 70 73 LEU CD2 C 25.525 0.3 2 361 70 73 LEU HD2 H 0.960 0.03 4 362 70 73 LEU C C 177.396 0.3 1 363 71 74 LEU N N 114.562 0.3 1 364 71 74 LEU H H 6.754 0.03 1 365 71 74 LEU CA C 57.474 0.3 1 366 71 74 LEU CB C 41.171 0.3 1 367 71 74 LEU CD1 C 22.467 0.3 2 368 71 74 LEU HD1 H 0.855 0.03 4 369 71 74 LEU CD2 C 26.032 0.3 2 370 71 74 LEU HD2 H 0.994 0.03 4 371 71 74 LEU C C 177.561 0.3 1 372 72 75 ASP N N 115.455 0.3 1 373 72 75 ASP H H 7.709 0.03 1 374 72 75 ASP CA C 52.240 0.3 1 375 72 75 ASP CB C 39.645 0.3 1 376 72 75 ASP C C 176.605 0.3 1 377 73 76 LYS N N 120.435 0.3 1 378 73 76 LYS H H 7.056 0.03 1 379 73 76 LYS CA C 52.409 0.3 1 380 73 76 LYS CB C 28.745 0.3 1 381 74 77 PRO CA C 61.681 0.3 1 382 74 77 PRO CB C 31.431 0.3 1 383 74 77 PRO C C 176.370 0.3 1 384 75 78 THR N N 108.348 0.3 1 385 75 78 THR H H 8.362 0.03 1 386 75 78 THR CA C 60.138 0.3 1 387 75 78 THR CB C 71.598 0.3 1 388 76 79 PHE CA C 62.029 0.3 1 389 77 80 ALA N N 117.376 0.3 1 390 77 80 ALA H H 8.439 0.03 1 391 77 80 ALA CA C 54.910 0.3 1 392 77 80 ALA CB C 18.008 0.3 1 393 77 80 ALA C C 179.991 0.3 1 394 78 81 GLU N N 115.331 0.3 1 395 78 81 GLU H H 7.552 0.03 1 396 78 81 GLU CA C 57.771 0.3 1 397 78 81 GLU CB C 30.052 0.3 1 398 78 81 GLU C C 177.503 0.3 1 399 79 82 VAL N N 112.177 0.3 1 400 79 82 VAL H H 7.334 0.03 1 401 79 82 VAL CA C 60.414 0.3 1 402 79 82 VAL CB C 32.982 0.3 1 403 79 82 VAL CG2 C 20.861 0.3 2 404 79 82 VAL HG2 H 0.820 0.03 4 405 79 82 VAL CG1 C 20.608 0.3 2 406 79 82 VAL HG1 H 0.727 0.03 4 407 79 82 VAL C C 176.070 0.3 1 408 80 83 ALA N N 123.642 0.3 1 409 80 83 ALA H H 7.602 0.03 1 410 80 83 ALA CA C 56.008 0.3 1 411 80 83 ALA CB C 18.537 0.3 1 412 80 83 ALA C C 178.340 0.3 1 413 81 84 ASP N N 116.483 0.3 1 414 81 84 ASP H H 8.533 0.03 1 415 81 84 ASP CA C 57.986 0.3 1 416 81 84 ASP CB C 39.307 0.3 1 417 81 84 ASP C C 178.042 0.3 1 418 82 85 GLU N N 121.571 0.3 1 419 82 85 GLU H H 8.336 0.03 1 420 82 85 GLU CA C 59.180 0.3 1 421 82 85 GLU CB C 28.895 0.3 1 422 82 85 GLU C C 179.669 0.3 1 423 83 86 PHE N N 120.050 0.3 1 424 83 86 PHE H H 8.725 0.03 1 425 83 86 PHE CB C 38.491 0.3 1 426 84 87 MET N N 117.801 0.3 1 427 84 87 MET H H 8.872 0.03 1 428 84 87 MET CA C 59.556 0.3 1 429 84 87 MET CB C 32.181 0.3 1 430 84 87 MET C C 177.477 0.3 1 431 85 88 ASP N N 116.718 0.3 1 432 85 88 ASP H H 8.081 0.03 1 433 85 88 ASP CA C 56.519 0.3 1 434 85 88 ASP CB C 39.770 0.3 1 435 85 88 ASP C C 177.863 0.3 1 436 86 89 TYR N N 119.810 0.3 1 437 86 89 TYR H H 7.521 0.03 1 438 86 89 TYR CA C 60.578 0.3 1 439 86 89 TYR CB C 37.588 0.3 1 440 87 90 ILE N N 108.344 0.3 1 441 87 90 ILE H H 7.390 0.03 1 442 87 90 ILE CA C 62.249 0.3 1 443 87 90 ILE CB C 37.829 0.3 1 444 87 90 ILE CD1 C 12.915 0.3 1 445 87 90 ILE HD1 H 0.508 0.03 1 446 87 90 ILE C C 176.243 0.3 1 447 88 91 ARG N N 120.229 0.3 1 448 88 91 ARG H H 7.869 0.03 1 449 88 91 ARG CA C 59.157 0.3 1 450 88 91 ARG CB C 28.588 0.3 1 451 88 91 ARG C C 177.732 0.3 1 452 89 92 GLY N N 114.082 0.3 1 453 89 92 GLY H H 8.515 0.03 1 454 89 92 GLY CA C 45.101 0.3 1 455 89 92 GLY C C 173.762 0.3 1 456 90 93 ALA N N 123.500 0.3 1 457 90 93 ALA H H 8.146 0.03 1 458 90 93 ALA CA C 50.929 0.3 1 459 90 93 ALA CB C 19.995 0.3 1 460 90 93 ALA C C 176.105 0.3 1 461 91 94 GLU N N 119.183 0.3 1 462 91 94 GLU H H 7.902 0.03 1 463 91 94 GLU CA C 54.190 0.3 1 464 91 94 GLU CB C 29.971 0.3 1 465 91 94 GLU C C 174.895 0.3 1 466 92 95 LEU N N 129.173 0.3 1 467 92 95 LEU H H 9.336 0.03 1 468 92 95 LEU CA C 52.769 0.3 1 469 92 95 LEU CB C 42.309 0.3 1 470 92 95 LEU CD1 C 23.406 0.3 2 471 92 95 LEU HD1 H 0.783 0.03 4 472 92 95 LEU CD2 C 25.371 0.3 2 473 92 95 LEU HD2 H 0.760 0.03 4 474 93 96 VAL N N 125.749 0.3 1 475 93 96 VAL H H 8.984 0.03 1 476 93 96 VAL CA C 61.222 0.3 1 477 93 96 VAL CB C 32.259 0.3 1 478 93 96 VAL CG2 C 19.471 0.3 2 479 93 96 VAL HG2 H 0.179 0.03 4 480 93 96 VAL CG1 C 19.062 0.3 2 481 93 96 VAL HG1 H 0.326 0.03 4 482 93 96 VAL C C 174.443 0.3 1 483 94 97 ILE N N 123.072 0.3 1 484 94 97 ILE H H 8.208 0.03 1 485 94 97 ILE CA C 59.144 0.3 1 486 94 97 ILE CB C 42.788 0.3 1 487 94 97 ILE CD1 C 15.106 0.3 1 488 94 97 ILE HD1 H 0.872 0.03 1 489 94 97 ILE C C 175.273 0.3 1 490 95 98 HIS N N 132.590 0.3 1 491 95 98 HIS H H 9.121 0.03 1 492 95 98 HIS CA C 57.692 0.3 1 493 95 98 HIS CB C 30.309 0.3 1 494 95 98 HIS C C 176.329 0.3 1 495 96 99 ASN N N 125.783 0.3 1 496 96 99 ASN H H 8.292 0.03 1 497 96 99 ASN CA C 53.261 0.3 1 498 96 99 ASN CB C 35.623 0.3 1 499 96 99 ASN C C 174.715 0.3 1 500 97 100 ALA N N 118.485 0.3 1 501 97 100 ALA H H 6.759 0.03 1 502 97 100 ALA CA C 54.839 0.3 1 503 97 100 ALA CB C 19.135 0.3 1 504 97 100 ALA C C 176.906 0.3 1 505 98 101 ALA N N 116.120 0.3 1 506 98 101 ALA H H 8.690 0.03 1 507 98 101 ALA CA C 54.789 0.3 1 508 98 101 ALA CB C 17.453 0.3 1 509 98 101 ALA C C 180.972 0.3 1 510 99 102 PHE N N 118.822 0.3 1 511 99 102 PHE H H 7.891 0.03 1 512 99 102 PHE CA C 60.019 0.3 1 513 99 102 PHE CB C 38.336 0.3 1 514 100 103 ASP N N 122.375 0.3 1 515 100 103 ASP H H 8.782 0.03 1 516 100 103 ASP CA C 57.215 0.3 1 517 100 103 ASP CB C 39.911 0.3 1 518 100 103 ASP C C 178.889 0.3 1 519 101 104 ILE N N 118.576 0.3 1 520 101 104 ILE H H 9.145 0.03 1 521 101 104 ILE CA C 61.846 0.3 1 522 101 104 ILE CB C 34.408 0.3 1 523 101 104 ILE CD1 C 10.328 0.3 1 524 101 104 ILE HD1 H 0.701 0.03 1 525 101 104 ILE C C 177.852 0.3 1 526 102 105 GLY N N 105.101 0.3 1 527 102 105 GLY H H 7.757 0.03 1 528 102 105 GLY CA C 46.882 0.3 1 529 103 106 PHE CA C 62.885 0.3 1 530 103 106 PHE CB C 39.190 0.3 1 531 103 106 PHE C C 177.727 0.3 1 532 104 107 MET N N 119.310 0.3 1 533 104 107 MET H H 8.672 0.03 1 534 104 107 MET CA C 59.615 0.3 1 535 104 107 MET CB C 32.537 0.3 1 536 104 107 MET C C 176.221 0.3 1 537 105 108 ASP N N 116.555 0.3 1 538 105 108 ASP H H 8.941 0.03 1 539 105 108 ASP CA C 57.118 0.3 1 540 105 108 ASP CB C 38.975 0.3 1 541 106 109 TYR CA C 59.353 0.3 1 542 106 109 TYR CB C 37.663 0.3 1 543 107 110 GLU N N 120.218 0.3 1 544 107 110 GLU H H 8.238 0.03 1 545 107 110 GLU CA C 59.072 0.3 1 546 107 110 GLU CB C 25.962 0.3 1 547 107 110 GLU C C 181.050 0.3 1 548 108 111 PHE N N 117.692 0.3 1 549 108 111 PHE H H 8.920 0.03 1 550 108 111 PHE CA C 60.156 0.3 1 551 108 111 PHE CB C 37.194 0.3 1 552 108 111 PHE C C 180.767 0.3 1 553 109 112 SER N N 118.846 0.3 1 554 109 112 SER H H 8.518 0.03 1 555 109 112 SER CA C 61.398 0.3 1 556 109 112 SER CB C 62.012 0.3 1 557 109 112 SER C C 177.617 0.3 1 558 110 113 LEU N N 123.719 0.3 1 559 110 113 LEU H H 7.661 0.03 1 560 110 113 LEU CA C 56.098 0.3 1 561 110 113 LEU CB C 40.685 0.3 1 562 110 113 LEU CD1 C 21.414 0.3 2 563 110 113 LEU HD1 H 0.644 0.03 4 564 110 113 LEU CD2 C 24.403 0.3 2 565 110 113 LEU HD2 H 0.345 0.03 4 566 110 113 LEU C C 178.497 0.3 1 567 111 114 LEU N N 114.561 0.3 1 568 111 114 LEU H H 7.444 0.03 1 569 111 114 LEU CA C 55.149 0.3 1 570 111 114 LEU CB C 39.983 0.3 1 571 111 114 LEU CD1 C 22.390 0.3 2 572 111 114 LEU HD1 H 1.008 0.03 4 573 111 114 LEU CD2 C 26.032 0.3 2 574 111 114 LEU HD2 H 1.216 0.03 4 575 111 114 LEU C C 177.014 0.3 1 576 112 115 LYS N N 112.762 0.3 1 577 112 115 LYS H H 7.761 0.03 1 578 112 115 LYS CA C 56.801 0.3 1 579 112 115 LYS CB C 28.184 0.3 1 580 112 115 LYS C C 175.934 0.3 1 581 113 116 ARG N N 117.659 0.3 1 582 113 116 ARG H H 8.642 0.03 1 583 113 116 ARG CA C 54.583 0.3 1 584 113 116 ARG CB C 31.535 0.3 1 585 113 116 ARG C C 175.171 0.3 1 586 114 117 ASP N N 117.987 0.3 1 587 114 117 ASP H H 8.442 0.03 1 588 114 117 ASP CA C 54.783 0.3 1 589 114 117 ASP CB C 38.708 0.3 1 590 114 117 ASP C C 175.211 0.3 1 591 115 118 ILE N N 121.420 0.3 1 592 115 118 ILE H H 7.615 0.03 1 593 115 118 ILE CA C 59.295 0.3 1 594 115 118 ILE CB C 38.265 0.3 1 595 115 118 ILE CD1 C 13.107 0.3 1 596 115 118 ILE HD1 H 0.842 0.03 1 597 116 119 PRO CA C 61.729 0.3 1 598 116 119 PRO CB C 31.989 0.3 1 599 116 119 PRO C C 175.355 0.3 1 600 117 120 LYS N N 115.843 0.3 1 601 117 120 LYS H H 8.180 0.03 1 602 117 120 LYS CA C 56.439 0.3 1 603 117 120 LYS CB C 31.655 0.3 1 604 118 121 THR CA C 67.411 0.3 1 605 118 121 THR CB C 68.015 0.3 1 606 118 121 THR C C 175.469 0.3 1 607 119 122 ASN N N 115.850 0.3 1 608 119 122 ASN H H 8.866 0.03 1 609 119 122 ASN CA C 53.737 0.3 1 610 119 122 ASN CB C 36.679 0.3 1 611 119 122 ASN C C 176.086 0.3 1 612 120 123 THR N N 109.547 0.3 1 613 120 123 THR H H 8.173 0.03 1 614 120 123 THR CA C 62.746 0.3 1 615 120 123 THR CB C 69.900 0.3 1 616 121 124 PHE CA C 56.068 0.3 1 617 121 124 PHE CB C 38.792 0.3 1 618 122 125 CYS N N 123.049 0.3 1 619 122 125 CYS H H 7.968 0.03 1 620 122 125 CYS CA C 58.767 0.3 1 621 122 125 CYS CB C 31.120 0.3 1 622 122 125 CYS C C 173.437 0.3 1 623 123 126 LYS N N 121.243 0.3 1 624 123 126 LYS H H 7.709 0.03 1 625 123 126 LYS CA C 55.038 0.3 1 626 123 126 LYS CB C 32.835 0.3 1 627 124 127 VAL N N 124.984 0.3 1 628 124 127 VAL H H 8.562 0.03 1 629 124 127 VAL CA C 62.456 0.3 1 630 124 127 VAL CB C 32.928 0.3 1 631 124 127 VAL CG2 C 21.539 0.3 2 632 124 127 VAL HG2 H 0.788 0.03 4 633 124 127 VAL CG1 C 20.608 0.3 2 634 124 127 VAL HG1 H 0.727 0.03 4 635 124 127 VAL C C 175.185 0.3 1 636 125 128 THR N N 129.801 0.3 1 637 125 128 THR H H 9.765 0.03 1 638 125 128 THR CA C 61.518 0.3 1 639 125 128 THR CB C 69.832 0.3 1 640 125 128 THR C C 171.446 0.3 1 641 126 129 ASP N N 124.885 0.3 1 642 126 129 ASP H H 8.496 0.03 1 643 126 129 ASP CA C 50.822 0.3 1 644 126 129 ASP CB C 41.450 0.3 1 645 126 129 ASP C C 178.176 0.3 1 646 127 130 SER N N 121.489 0.3 1 647 127 130 SER H H 8.816 0.03 1 648 127 130 SER CA C 61.970 0.3 1 649 127 130 SER CB C 61.517 0.3 1 650 127 130 SER C C 177.217 0.3 1 651 128 131 LEU N N 125.496 0.3 1 652 128 131 LEU H H 8.395 0.03 1 653 128 131 LEU CA C 57.155 0.3 1 654 128 131 LEU CB C 39.653 0.3 1 655 128 131 LEU CD1 C 22.917 0.3 2 656 128 131 LEU HD1 H 0.809 0.03 4 657 128 131 LEU CD2 C 25.866 0.3 2 658 128 131 LEU HD2 H 0.726 0.03 4 659 128 131 LEU C C 177.854 0.3 1 660 129 132 ALA N N 121.946 0.3 1 661 129 132 ALA H H 6.799 0.03 1 662 129 132 ALA CA C 54.375 0.3 1 663 129 132 ALA CB C 17.184 0.3 1 664 129 132 ALA C C 181.192 0.3 1 665 130 133 VAL N N 117.868 0.3 1 666 130 133 VAL H H 7.497 0.03 1 667 130 133 VAL CA C 66.063 0.3 1 668 130 133 VAL CB C 31.358 0.3 1 669 130 133 VAL CG2 C 21.989 0.3 2 670 130 133 VAL HG2 H 1.174 0.03 4 671 130 133 VAL CG1 C 21.237 0.3 2 672 130 133 VAL HG1 H 0.978 0.03 4 673 130 133 VAL C C 177.983 0.3 1 674 131 134 ALA N N 122.144 0.3 1 675 131 134 ALA H H 8.101 0.03 1 676 131 134 ALA CA C 55.455 0.3 1 677 131 134 ALA CB C 17.684 0.3 1 678 132 135 ARG N N 115.672 0.3 1 679 132 135 ARG H H 8.567 0.03 1 680 132 135 ARG CA C 59.102 0.3 1 681 132 135 ARG CB C 29.685 0.3 1 682 132 135 ARG C C 178.277 0.3 1 683 133 136 LYS N N 117.280 0.3 1 684 133 136 LYS H H 7.322 0.03 1 685 133 136 LYS CA C 57.808 0.3 1 686 133 136 LYS CB C 31.383 0.3 1 687 134 137 MET N N 117.443 0.3 1 688 134 137 MET H H 7.611 0.03 1 689 134 137 MET CA C 57.709 0.3 1 690 134 137 MET CB C 32.759 0.3 1 691 134 137 MET C C 176.325 0.3 1 692 135 138 PHE N N 117.037 0.3 1 693 135 138 PHE H H 8.461 0.03 1 694 137 140 GLY CA C 45.192 0.3 1 695 137 140 GLY C C 174.075 0.3 1 696 138 141 LYS N N 117.929 0.3 1 697 138 141 LYS H H 7.242 0.03 1 698 138 141 LYS CA C 53.277 0.3 1 699 138 141 LYS CB C 32.741 0.3 1 700 140 143 ASN CA C 53.634 0.3 1 701 140 143 ASN CB C 39.840 0.3 1 702 140 143 ASN C C 173.796 0.3 1 703 141 144 SER N N 110.424 0.3 1 704 141 144 SER H H 6.915 0.03 1 705 141 144 SER CA C 57.092 0.3 1 706 141 144 SER CB C 63.747 0.3 1 707 141 144 SER C C 174.674 0.3 1 708 142 145 LEU N N 121.993 0.3 1 709 142 145 LEU H H 9.050 0.03 1 710 142 145 LEU CA C 58.286 0.3 1 711 142 145 LEU CB C 40.411 0.3 1 712 142 145 LEU CD1 C 24.030 0.3 2 713 142 145 LEU HD1 H 0.701 0.03 4 714 142 145 LEU CD2 C 24.201 0.3 2 715 142 145 LEU HD2 H 0.634 0.03 4 716 142 145 LEU C C 178.816 0.3 1 717 143 146 ASP N N 116.041 0.3 1 718 143 146 ASP H H 8.594 0.03 1 719 143 146 ASP CA C 56.755 0.3 1 720 143 146 ASP CB C 39.166 0.3 1 721 143 146 ASP C C 178.715 0.3 1 722 144 147 ALA N N 124.133 0.3 1 723 144 147 ALA H H 7.465 0.03 1 724 144 147 ALA CA C 54.225 0.3 1 725 144 147 ALA CB C 17.700 0.3 1 726 144 147 ALA C C 181.276 0.3 1 727 145 148 LEU N N 120.016 0.3 1 728 145 148 LEU H H 8.356 0.03 1 729 145 148 LEU CA C 57.461 0.3 1 730 145 148 LEU CB C 41.485 0.3 1 731 145 148 LEU CD1 C 23.327 0.3 2 732 145 148 LEU HD1 H 1.124 0.03 4 733 145 148 LEU CD2 C 26.194 0.3 2 734 145 148 LEU HD2 H 0.914 0.03 4 735 145 148 LEU C C 178.978 0.3 1 736 146 149 CYS N N 117.140 0.3 1 737 146 149 CYS H H 8.562 0.03 1 738 146 149 CYS CA C 63.900 0.3 1 739 146 149 CYS CB C 25.463 0.3 1 740 146 149 CYS C C 176.860 0.3 1 741 147 150 ALA N N 119.926 0.3 1 742 147 150 ALA H H 7.336 0.03 1 743 147 150 ALA CA C 54.164 0.3 1 744 147 150 ALA CB C 16.911 0.3 1 745 147 150 ALA C C 180.690 0.3 1 746 148 151 ARG N N 119.487 0.3 1 747 148 151 ARG H H 7.750 0.03 1 748 148 151 ARG CA C 58.729 0.3 1 749 148 151 ARG CB C 29.124 0.3 1 750 149 152 TYR N N 113.988 0.3 1 751 149 152 TYR H H 7.541 0.03 1 752 150 153 GLU CA C 56.733 0.3 1 753 150 153 GLU CB C 26.049 0.3 1 754 150 153 GLU C C 175.516 0.3 1 755 151 154 ILE N N 119.946 0.3 1 756 151 154 ILE H H 8.211 0.03 1 757 151 154 ILE CA C 59.687 0.3 1 758 151 154 ILE CB C 36.895 0.3 1 759 151 154 ILE CD1 C 11.472 0.3 1 760 151 154 ILE HD1 H 0.717 0.03 1 761 151 154 ILE C C 175.456 0.3 1 762 152 155 ASP N N 127.079 0.3 1 763 152 155 ASP H H 8.597 0.03 1 764 152 155 ASP CA C 53.323 0.3 1 765 152 155 ASP CB C 41.044 0.3 1 766 153 156 ASN CA C 52.663 0.3 1 767 153 156 ASN CB C 38.271 0.3 1 768 153 156 ASN C C 176.238 0.3 1 769 154 157 SER N N 117.180 0.3 1 770 154 157 SER H H 8.610 0.03 1 771 154 157 SER CA C 60.688 0.3 1 772 154 157 SER CB C 63.324 0.3 1 773 154 157 SER C C 175.112 0.3 1 774 155 158 LYS N N 121.325 0.3 1 775 155 158 LYS H H 8.423 0.03 1 776 155 158 LYS CA C 54.887 0.3 1 777 155 158 LYS CB C 30.848 0.3 1 778 155 158 LYS C C 176.428 0.3 1 779 156 159 ARG N N 118.910 0.3 1 780 156 159 ARG H H 7.460 0.03 1 781 156 159 ARG CA C 54.848 0.3 1 782 156 159 ARG CB C 30.368 0.3 1 783 157 160 THR CA C 61.227 0.3 1 784 157 160 THR CB C 68.688 0.3 1 785 157 160 THR C C 174.370 0.3 1 786 158 161 LEU N N 119.260 0.3 1 787 158 161 LEU H H 6.568 0.03 1 788 158 161 LEU CA C 53.316 0.3 1 789 158 161 LEU CB C 42.092 0.3 1 790 158 161 LEU CD1 C 21.953 0.3 2 791 158 161 LEU HD1 H 0.827 0.03 4 792 158 161 LEU CD2 C 24.840 0.3 2 793 158 161 LEU HD2 H 0.721 0.03 4 794 158 161 LEU C C 174.438 0.3 1 795 159 162 HIS N N 114.510 0.3 1 796 159 162 HIS H H 8.072 0.03 1 797 159 162 HIS CA C 54.063 0.3 1 798 159 162 HIS CB C 32.763 0.3 1 799 159 162 HIS C C 175.654 0.3 1 800 160 163 GLY N N 108.063 0.3 1 801 160 163 GLY H H 8.594 0.03 1 802 160 163 GLY CA C 46.607 0.3 1 803 160 163 GLY C C 175.137 0.3 1 804 161 164 ALA N N 128.262 0.3 1 805 161 164 ALA H H 10.433 0.03 1 806 161 164 ALA CA C 53.498 0.3 1 807 161 164 ALA CB C 17.706 0.3 1 808 161 164 ALA C C 179.323 0.3 1 809 162 165 LEU N N 116.590 0.3 1 810 162 165 LEU H H 6.491 0.03 1 811 162 165 LEU CA C 56.630 0.3 1 812 162 165 LEU CB C 39.066 0.3 1 813 162 165 LEU CD1 C 24.130 0.3 2 814 162 165 LEU HD1 H 0.876 0.03 4 815 162 165 LEU CD2 C 26.835 0.3 2 816 162 165 LEU HD2 H 1.014 0.03 4 817 162 165 LEU C C 176.671 0.3 1 818 163 166 LEU N N 118.583 0.3 1 819 163 166 LEU H H 6.351 0.03 1 820 163 166 LEU CA C 57.040 0.3 1 821 163 166 LEU CB C 38.208 0.3 1 822 163 166 LEU CD1 C 23.019 0.3 2 823 163 166 LEU HD1 H 0.745 0.03 4 824 163 166 LEU CD2 C 24.878 0.3 2 825 163 166 LEU HD2 H 0.861 0.03 4 826 164 167 ASP N N 117.126 0.3 1 827 164 167 ASP H H 7.489 0.03 1 828 164 167 ASP CA C 57.264 0.3 1 829 164 167 ASP CB C 38.911 0.3 1 830 164 167 ASP C C 178.361 0.3 1 831 165 168 ALA N N 122.407 0.3 1 832 165 168 ALA H H 8.083 0.03 1 833 165 168 ALA CA C 54.893 0.3 1 834 165 168 ALA CB C 16.483 0.3 1 835 165 168 ALA C C 178.082 0.3 1 836 166 169 GLN N N 119.194 0.3 1 837 166 169 GLN H H 7.950 0.03 1 838 166 169 GLN CA C 59.426 0.3 1 839 166 169 GLN CB C 27.448 0.3 1 840 166 169 GLN C C 177.795 0.3 1 841 167 170 ILE N N 118.297 0.3 1 842 167 170 ILE H H 8.407 0.03 1 843 167 170 ILE CA C 65.066 0.3 1 844 167 170 ILE CB C 36.672 0.3 1 845 167 170 ILE CD1 C 12.775 0.3 1 846 167 170 ILE HD1 H 0.674 0.03 1 847 167 170 ILE C C 178.149 0.3 1 848 168 171 LEU N N 119.196 0.3 1 849 168 171 LEU H H 8.414 0.03 1 850 168 171 LEU CA C 57.020 0.3 1 851 168 171 LEU CB C 38.850 0.3 1 852 168 171 LEU CD1 C 21.292 0.3 2 853 168 171 LEU HD1 H 0.833 0.03 4 854 168 171 LEU CD2 C 27.085 0.3 2 855 168 171 LEU HD2 H 0.985 0.03 4 856 168 171 LEU C C 177.797 0.3 1 857 169 172 ALA N N 121.883 0.3 1 858 169 172 ALA H H 8.658 0.03 1 859 169 172 ALA CA C 55.443 0.3 1 860 169 172 ALA CB C 17.713 0.3 1 861 169 172 ALA C C 179.077 0.3 1 862 170 173 GLU N N 116.392 0.3 1 863 170 173 GLU H H 7.828 0.03 1 864 170 173 GLU CA C 59.966 0.3 1 865 170 173 GLU CB C 28.541 0.3 1 866 170 173 GLU C C 180.758 0.3 1 867 171 174 VAL N N 121.594 0.3 1 868 171 174 VAL H H 8.661 0.03 1 869 171 174 VAL CA C 66.050 0.3 1 870 171 174 VAL CB C 31.439 0.3 1 871 171 174 VAL CG2 C 24.881 0.3 2 872 171 174 VAL HG2 H 0.984 0.03 4 873 171 174 VAL CG1 C 22.897 0.3 2 874 171 174 VAL HG1 H 0.956 0.03 4 875 171 174 VAL C C 176.783 0.3 1 876 172 175 TYR N N 122.243 0.3 1 877 172 175 TYR H H 9.757 0.03 1 878 172 175 TYR CA C 61.965 0.3 1 879 172 175 TYR CB C 37.596 0.3 1 880 173 176 LEU N N 120.615 0.3 1 881 173 176 LEU H H 8.590 0.03 1 882 173 176 LEU CA C 57.480 0.3 1 883 173 176 LEU CB C 40.120 0.3 1 884 173 176 LEU CD1 C 22.008 0.3 2 885 173 176 LEU HD1 H 0.706 0.03 4 886 173 176 LEU CD2 C 24.840 0.3 2 887 173 176 LEU HD2 H 0.721 0.03 4 888 173 176 LEU C C 179.301 0.3 1 889 174 177 ALA N N 122.970 0.3 1 890 174 177 ALA H H 7.514 0.03 1 891 174 177 ALA CA C 54.587 0.3 1 892 174 177 ALA CB C 16.102 0.3 1 893 175 178 MET N N 117.376 0.3 1 894 175 178 MET H H 8.439 0.03 1 895 175 178 MET CA C 58.375 0.3 1 896 175 178 MET CB C 34.123 0.3 1 897 175 178 MET C C 177.701 0.3 1 898 176 179 THR N N 104.194 0.3 1 899 176 179 THR H H 7.263 0.03 1 900 176 179 THR CA C 60.975 0.3 1 901 176 179 THR CB C 69.470 0.3 1 902 176 179 THR C C 175.443 0.3 1 903 177 180 GLY N N 109.435 0.3 1 904 177 180 GLY H H 7.368 0.03 1 905 177 180 GLY CA C 45.402 0.3 1 906 177 180 GLY C C 174.647 0.3 1 907 178 181 GLY N N 108.543 0.3 1 908 178 181 GLY H H 8.192 0.03 1 909 178 181 GLY CA C 45.054 0.3 1 910 182 185 MET CA C 55.063 0.3 1 911 182 185 MET CB C 32.230 0.3 1 912 182 185 MET C C 174.906 0.3 1 913 183 186 ALA N N 130.318 0.3 1 914 183 186 ALA H H 7.878 0.03 1 915 183 186 ALA CA C 53.424 0.3 1 916 183 186 ALA CB C 19.365 0.3 1 stop_ loop_ _Atom_shift_assign_ID_ambiguity 40 '40,40,38,38,38' '47,47,47' '171,171,171,169,169,169' '185,185,185,183,183,183' '194,194,194,192,192,192' '216,216,216' '253,253,253,251,251,251' '267,267,267,265,265,265' '286,286,286,284,284,284' '295,295,295,293,293,293' '325,325,325' '361,361,361,359,359,359' '370,370,370,368,368,368' '406,406,406,404,404,404' '473,473,473,471,471,471' '481,481,481,479,479,479' '565,565,565,563,563,563' '574,574,574,572,572,572' '634,634,634,632,632,632' '658,658,658,656,656,656' '672,672,672,670,670,670' '715,715,715,713,713,713' '734,734,734,732,732,732' '793,793,793,791,791,791' '816,816,816,814,814,814' '825,825,825,823,823,823' '855,855,855,853,853,853' '874,874,874,872,872,872' '887,887,887,885,885,885' stop_ save_