data_4792 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Backbone NMR Assignment and Secondary Structure of the Dimeric ParD Protein ; _BMRB_accession_number 4792 _BMRB_flat_file_name bmr4792.str _Entry_type original _Submission_date 2000-07-21 _Accession_date 2000-07-21 _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 Oberer Monika . . 2 Prytulla Stefan . . 3 Keller Walter . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 370 "13C chemical shifts" 321 "15N chemical shifts" 89 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2002-04-04 original author . stop_ _Original_release_date 2002-04-04 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; The Anti-toxin ParD of Plasmid RK2 Consists of two Structurally Distinct Moieties and Belongs to the Ribbon-helix-helix Family of DNA-binding Proteins ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code 21609805 _PubMed_ID 11743881 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Oberer Monika . . 2 Zangger Klaus . . 3 Prytulla Stefan . . 4 Keller Walter . . stop_ _Journal_abbreviation 'Biochem. J.' _Journal_volume 361 _Journal_issue 'Pt 1' _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 41 _Page_last 47 _Year 2002 _Details . loop_ _Keyword 'plasmid addiction system' antitoxin RK2/RP4 autoregulation NMR stop_ save_ ####################################### # Cited references within the entry # ####################################### save_ref_1 _Saveframe_category citation _Citation_full ; Ch. Bartels, T.-H. Xia, M. Billeter, P. G?ntert and K. W?thrich (1995) The program XEASY for computer-supported NMR spectral analysis of biological macromolecules. J. Biomolecular NMR 5, 1-10 ; _Citation_title . _Citation_status . _Citation_type . _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID ? _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_system_ParD _Saveframe_category molecular_system _Mol_system_name 'ParD dimer' _Abbreviation_common ParD _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'ParD subunit 1' $ParD 'ParD subunit 2' $ParD stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state dimer _System_paramagnetic no _System_thiol_state 'not present' loop_ _Magnetic_equivalence_ID _Magnetically_equivalent_system_component 1 'ParD subunit 1' 1 'ParD subunit 2' stop_ loop_ _Biological_function antitoxin 'plasmid stabilization' DNA-binding autoregulation stop_ _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_ParD _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common ParD _Abbreviation_common ParD _Molecular_mass 9103.18 _Mol_thiol_state 'not present' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 83 _Mol_residue_sequence ; MSRLTIDMTDQQHQSLKALA ALQGKTIKQYALERLFPGDA DADQAWQELKTMLGNRINDG LAGKVSTKSVGEILDEELSG DRA ; loop_ _Residue_seq_code _Residue_label 1 MET 2 SER 3 ARG 4 LEU 5 THR 6 ILE 7 ASP 8 MET 9 THR 10 ASP 11 GLN 12 GLN 13 HIS 14 GLN 15 SER 16 LEU 17 LYS 18 ALA 19 LEU 20 ALA 21 ALA 22 LEU 23 GLN 24 GLY 25 LYS 26 THR 27 ILE 28 LYS 29 GLN 30 TYR 31 ALA 32 LEU 33 GLU 34 ARG 35 LEU 36 PHE 37 PRO 38 GLY 39 ASP 40 ALA 41 ASP 42 ALA 43 ASP 44 GLN 45 ALA 46 TRP 47 GLN 48 GLU 49 LEU 50 LYS 51 THR 52 MET 53 LEU 54 GLY 55 ASN 56 ARG 57 ILE 58 ASN 59 ASP 60 GLY 61 LEU 62 ALA 63 GLY 64 LYS 65 VAL 66 SER 67 THR 68 LYS 69 SER 70 VAL 71 GLY 72 GLU 73 ILE 74 LEU 75 ASP 76 GLU 77 GLU 78 LEU 79 SER 80 GLY 81 ASP 82 ARG 83 ALA stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2014-12-21 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 2AN7 "Solution Structure Of The Bacterial Antidote Pard" 100.00 83 100.00 100.00 1.68e-51 EMBL CAE54490 "plasmid stabilisation protein ParD [Cloning vector pMR10]" 100.00 83 100.00 100.00 1.68e-51 EMBL CAG30890 "ParD protein [uncultured bacterium]" 100.00 83 100.00 100.00 1.68e-51 EMBL CAK12703 "rD antitoxin protein [Pseudomonas aeruginosa]" 100.00 83 100.00 100.00 1.68e-51 GB AAA26418 "parD [Plasmid RP4]" 100.00 83 100.00 100.00 1.68e-51 GB AAA91498 "putative [Escherichia coli]" 100.00 83 100.00 100.00 1.68e-51 GB AAA92774 "parD [Plasmid RK2]" 100.00 83 100.00 100.00 1.68e-51 GB AAA98334 "ParD [Xanthomonas sp. W17]" 100.00 83 100.00 100.00 1.68e-51 GB AAB67690 "ParD [Cloning vector pJB321]" 100.00 83 100.00 100.00 1.68e-51 PIR A47048 "plasmid stabilization protein ParD - plasmid RK2" 100.00 83 100.00 100.00 1.68e-51 REF WP_011205807 "MULTISPECIES: ParD protein [Gammaproteobacteria]" 100.00 83 100.00 100.00 1.68e-51 REF WP_032072691 "ParD [uncultured bacterium]" 100.00 94 100.00 100.00 4.30e-51 REF YP_006941366 "ParD protein [uncultured bacterium]" 100.00 83 100.00 100.00 1.68e-51 REF YP_006941448 "Protein parD [uncultured bacterium]" 100.00 83 100.00 100.00 1.68e-51 REF YP_006941534 "ParD protein [uncultured bacterium]" 100.00 83 100.00 100.00 1.68e-51 SP P22995 "RecName: Full=Antitoxin ParD [Escherichia coli]" 100.00 83 100.00 100.00 1.68e-51 TPE CAJ85710 "TPA: ParD antitoxin protein [Birmingham IncP-alpha plasmid]" 100.00 83 100.00 100.00 1.68e-51 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species _Plasmid _Gene_mnemonic $ParD 'E. coli' 562 Bacteria . Escherichia coli RP4/RK2 parD stop_ save_ ######################### # Experimental source # ######################### save_experimental_source _Saveframe_category experimental_source loop_ _Mol_label _Production_method _Host_organism_name_common _Genus _Species _Strain _Vector_type _Vector_name _Details $ParD 'recombinant technology' 'E. coli' Escherichia coli BL21 plasmid pRR136-6 ; Protein is encoded on the broad-host range plasmid RP4/RK2; Plasmid is transmitted to a wide range of gram-negative bacteria; T7 promotor, heat inducible ; stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Saveframe_category sample _Sample_type solution _Details 'Degradation of the sample was observed after prolonged measurement' loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $ParD 0.6 mM '[U-98% 13C; U-98% 15N]' stop_ save_ save_sample_2 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $ParD 0.5 mM '[U-98% 15N]' stop_ save_ save_sample_3 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $ParD 0.5 mM . stop_ save_ ############################ # Computer software used # ############################ save_XEASY _Saveframe_category software _Name XEASY _Version 1.3 _Details . _Citation_label $ref_1 save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model 'Unity INOVA' _Field_strength 600 _Details . save_ ############################# # NMR applied experiments # ############################# save_2D_1H15N_HSQC_1 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H15N HSQC' _Sample_label . save_ save_2D_NOESY_2 _Saveframe_category NMR_applied_experiment _Experiment_name '2D NOESY' _Sample_label . save_ save_2D_TOCSY_3 _Saveframe_category NMR_applied_experiment _Experiment_name '2D TOCSY' _Sample_label . save_ save_3D_15N_NOESY-HSQC_4 _Saveframe_category NMR_applied_experiment _Experiment_name '3D 15N NOESY-HSQC' _Sample_label . save_ save_3D_15N_TOCSY-HSQC_5 _Saveframe_category NMR_applied_experiment _Experiment_name '3D 15N TOCSY-HSQC' _Sample_label . save_ save_3D_HNCO_6 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCO' _Sample_label . save_ save_3D_HN(CO)CA_7 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HN(CO)CA' _Sample_label . save_ save_3D_CBCA(CO)NH_8 _Saveframe_category NMR_applied_experiment _Experiment_name '3D CBCA(CO)NH' _Sample_label . save_ save_3D_HNCACB_9 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCACB' _Sample_label . save_ save_NMR_spec_expt__0_1 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H15N HSQC' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_2 _Saveframe_category NMR_applied_experiment _Experiment_name '2D NOESY' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_3 _Saveframe_category NMR_applied_experiment _Experiment_name '2D TOCSY' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_4 _Saveframe_category NMR_applied_experiment _Experiment_name '3D 15N NOESY-HSQC' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_5 _Saveframe_category NMR_applied_experiment _Experiment_name '3D 15N TOCSY-HSQC' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_6 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCO' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_7 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HN(CO)CA' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_8 _Saveframe_category NMR_applied_experiment _Experiment_name '3D CBCA(CO)NH' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_9 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCACB' _BMRB_pulse_sequence_accession_number . _Details . save_ ####################### # Sample conditions # ####################### save_Cond1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 6.0 . n/a temperature 306 . K 'ionic strength' 0.11 . M stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference _Saveframe_category chemical_shift_reference _Details . loop_ _Mol_common_name _Atom_type _Atom_isotope_number _Atom_group _Chem_shift_units _Chem_shift_value _Reference_method _Reference_type _External_reference_sample_geometry _External_reference_location _External_reference_axis _Indirect_shift_ratio DSS H 1 'methyl protons' ppm 0.0 internal direct . . . . TMS C 13 'methyl protons' ppm 0.0 . indirect . . . . TMS N 15 'methyl protons' ppm 0.0 . indirect . . . 0.101329144 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 '2D 1H15N HSQC' '2D NOESY' '2D TOCSY' '3D 15N NOESY-HSQC' '3D 15N TOCSY-HSQC' '3D HNCO' '3D HN(CO)CA' '3D CBCA(CO)NH' '3D HNCACB' stop_ _Sample_conditions_label $Cond1 _Chem_shift_reference_set_label $chemical_shift_reference _Mol_system_component_name 'ParD 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 . 4 LEU N N 127.041 0.022 1 2 . 4 LEU H H 8.842 0.008 1 3 . 4 LEU CA C 54.161 0.046 1 4 . 4 LEU HA H 4.711 0 1 5 . 4 LEU CB C 45.779 0.092 1 6 . 4 LEU HB2 H 1.756 0 1 7 . 4 LEU CG C 24.1 0 1 8 . 4 LEU HG H 1.314 0 1 9 . 4 LEU CD1 C 26.545 0 1 10 . 4 LEU HD1 H 0.906 0 1 11 . 4 LEU CD2 C 23.876 0 1 12 . 4 LEU HD2 H 0.703 0 1 13 . 4 LEU C C 177.484 0.007 1 14 . 5 THR N N 122.817 0.01 1 15 . 5 THR H H 8.641 0.001 1 16 . 5 THR CA C 61.746 0.108 1 17 . 5 THR HA H 5.168 0 1 18 . 5 THR CB C 70.489 0.04 1 19 . 5 THR HB H 3.862 0 1 20 . 5 THR CG2 C 22.292 0 1 21 . 5 THR HG2 H 1.045 0 1 22 . 5 THR C C 178.312 0.002 1 23 . 6 ILE N N 125.161 0.022 1 24 . 6 ILE H H 9.117 0.005 1 25 . 6 ILE CA C 60.189 0.078 1 26 . 6 ILE HA H 4.325 0 1 27 . 6 ILE CB C 41.522 0.099 1 28 . 6 ILE HB H 1.776 0 1 29 . 6 ILE CG1 C 27.2 0 1 30 . 6 ILE HG12 H 0.884 0 1 31 . 6 ILE CG2 C 18.455 0 1 32 . 6 ILE HG2 H 0.907 0 1 33 . 6 ILE CD1 C 13.868 0 1 34 . 6 ILE HD1 H 0.698 0 1 35 . 6 ILE C C 177.75 0.009 1 36 . 7 ASP N N 127.191 0.019 1 37 . 7 ASP H H 8.398 0.004 1 38 . 7 ASP CA C 54.881 0.09 1 39 . 7 ASP HA H 5.16 0 1 40 . 7 ASP CB C 42.85 0.061 1 41 . 7 ASP HB2 H 2.608 0 2 42 . 7 ASP HB3 H 2.475 0 2 43 . 7 ASP C C 177.246 0.004 1 44 . 8 MET N N 119.271 0.004 1 45 . 8 MET H H 8.51 0.02 1 46 . 8 MET CA C 54.861 0.1 1 47 . 8 MET HA H 4.915 0 1 48 . 8 MET CB C 36.368 0 1 49 . 8 MET HB2 H 2.367 0 1 50 . 8 MET CG C 31.465 0 1 51 . 8 MET HG2 H 2.571 0 1 52 . 8 MET HE H 2.165 0 1 53 . 8 MET C C 176.323 0.007 1 54 . 9 THR N N 112.615 0.016 1 55 . 9 THR H H 8.883 0.007 1 56 . 9 THR CA C 61.544 0.226 1 57 . 9 THR HA H 4.524 0 1 58 . 9 THR CB C 71.316 0 1 59 . 9 THR HB H 4.28 0 1 60 . 9 THR CG2 C 61.67 0 1 61 . 9 THR HG2 H 1.267 0 1 62 . 9 THR C C 176.357 0.003 1 63 . 10 ASP N N 121.69 0.007 1 64 . 10 ASP H H 9 0.012 1 65 . 10 ASP CA C 58.385 0.076 1 66 . 10 ASP HA H 4.711 0 1 67 . 10 ASP CB C 40.466 0 1 68 . 10 ASP HB2 H 2.694 0 1 69 . 10 ASP C C 173.342 0.022 1 70 . 11 GLN N N 118.824 0.01 1 71 . 11 GLN H H 8.474 0.006 1 72 . 11 GLN CA C 59.971 0.063 1 73 . 11 GLN HA H 3.981 0 1 74 . 11 GLN CB C 28.658 0.173 1 75 . 11 GLN HB2 H 1.94 0 2 76 . 11 GLN HB3 H 2.10 0 2 77 . 11 GLN CG C 34.551 0 1 78 . 11 GLN HG2 H 2.37 0 1 79 . 11 GLN CD C 171.82 0 1 80 . 11 GLN NE2 N 112.34 0 1 81 . 11 GLN HE21 H 6.877 0 2 82 . 11 GLN HE22 H 7.456 0 2 83 . 11 GLN C C 172.804 0 1 84 . 12 GLN N N 121.062 0.011 1 85 . 12 GLN H H 7.855 0.005 1 86 . 12 GLN CA C 59.537 0.024 1 87 . 12 GLN HA H 3.775 0 1 88 . 12 GLN CB C 28.599 0 1 89 . 12 GLN HB2 H 2.29 0 1 90 . 12 GLN CG C 33.133 0 1 91 . 12 GLN HG2 H 2.192 0 1 92 . 12 GLN NE2 N 109.89 0 1 93 . 12 GLN HE21 H 6.37 0 2 94 . 12 GLN HE22 H 6.99 0 2 95 . 12 GLN C C 174.27 0.02 1 96 . 13 HIS N N 119.983 0.011 1 97 . 13 HIS H H 8.487 0.005 1 98 . 13 HIS CA C 60.529 0.086 1 99 . 13 HIS HA H 4.314 0 1 100 . 13 HIS CB C 31.375 0.25 1 101 . 13 HIS HB2 H 3.396 0 2 102 . 13 HIS HB3 H 3.056 0 2 103 . 13 HIS HD2 H 7.856 0 1 104 . 13 HIS C C 174.459 0.021 1 105 . 14 GLN N N 117.194 0.017 1 106 . 14 GLN H H 8.509 0.002 1 107 . 14 GLN CA C 59.239 0.114 1 108 . 14 GLN HA H 4.39 0 1 109 . 14 GLN CB C 28.632 0.057 1 110 . 14 GLN HB2 H 2.06 0 2 111 . 14 GLN HB3 H 2.021 0 2 112 . 14 GLN CG C 34.051 0 1 113 . 14 GLN HG2 H 2.5 0 1 114 . 14 GLN CD C 172.05 0 1 115 . 14 GLN NE2 N 111.69 0 1 116 . 14 GLN HE21 H 6.82 0.001 2 117 . 14 GLN HE22 H 7.431 0 2 118 . 14 GLN C C 172.711 0.011 1 119 . 15 SER N N 116.394 0.011 1 120 . 15 SER H H 8.198 0.012 1 121 . 15 SER CA C 62.645 0.045 1 122 . 15 SER HA H 4.479 0 1 123 . 15 SER CB C 64.414 0 1 124 . 15 SER HB2 H 3.946 0 1 125 . 15 SER C C 176.263 0.007 1 126 . 16 LEU N N 122.576 0.014 1 127 . 16 LEU H H 8.368 0.01 1 128 . 16 LEU CA C 58.353 0.099 1 129 . 16 LEU HA H 3.973 0 1 130 . 16 LEU CB C 42.515 0.079 1 131 . 16 LEU HB2 H 1.896 0 1 132 . 16 LEU CG C 27.26 0 1 133 . 16 LEU HG H 1.772 0 1 134 . 16 LEU CD1 C 25.961 0 1 135 . 16 LEU HD1 H 0.867 0 2 136 . 16 LEU HD2 H 0.928 0 2 137 . 16 LEU C C 174.034 0.026 1 138 . 17 LYS N N 117.363 0.01 1 139 . 17 LYS H H 8.225 0.009 1 140 . 17 LYS CA C 60.426 0.057 1 141 . 17 LYS HA H 3.686 0 1 142 . 17 LYS CB C 33.084 0.051 1 143 . 17 LYS HB2 H 1.863 0 2 144 . 17 LYS HB3 H 1.769 0 2 145 . 17 LYS CG C 25.377 0 1 146 . 17 LYS HG2 H 1.527 0 1 147 . 17 LYS CD C 29.964 0 1 148 . 17 LYS CE C 41.973 0 1 149 . 17 LYS HE2 H 2.812 0 1 150 . 17 LYS C C 172.949 0.001 1 151 . 18 ALA N N 121.275 0.01 1 152 . 18 ALA H H 7.761 0.001 1 153 . 18 ALA CA C 55.309 0.131 1 154 . 18 ALA HA H 4.116 0 1 155 . 18 ALA CB C 18.906 0.086 1 156 . 18 ALA HB H 1.513 0 1 157 . 18 ALA C C 172.15 0 1 158 . 19 LEU N N 120.047 0.006 1 159 . 19 LEU H H 8.199 0.002 1 160 . 19 LEU CA C 58.319 0.034 1 161 . 19 LEU HA H 3.891 0 1 162 . 19 LEU CB C 42.321 0.122 1 163 . 19 LEU HB2 H 1.665 0 1 164 . 19 LEU CG C 67.09 0 1 165 . 19 LEU HG H 1.498 0 1 166 . 19 LEU CD1 C 25.544 0 1 167 . 19 LEU HD1 H 1.125 0 1 168 . 19 LEU CD2 C 23.626 0 1 169 . 19 LEU HD2 H 0.87 0 1 170 . 19 LEU C C 172.762 0.038 1 171 . 20 ALA N N 120.578 0.018 1 172 . 20 ALA H H 7.886 0.004 1 173 . 20 ALA CA C 55.837 0.065 1 174 . 20 ALA HA H 3.454 0 1 175 . 20 ALA CB C 17.859 0.12 1 176 . 20 ALA HB H 1.082 0 1 177 . 20 ALA C C 172.236 0.005 1 178 . 21 ALA N N 119.521 0.001 1 179 . 21 ALA H H 7.841 0.002 1 180 . 21 ALA CA C 55.62 0.033 1 181 . 21 ALA HA H 4.145 0 1 182 . 21 ALA CB C 18.469 0.067 1 183 . 21 ALA HB H 1.526 0 1 184 . 21 ALA C C 169.928 0.005 1 185 . 22 LEU N N 120.102 0.006 1 186 . 22 LEU H H 7.978 0.001 1 187 . 22 LEU CA C 58.107 0.08 1 188 . 22 LEU HA H 4.186 0 1 189 . 22 LEU CB C 42.684 0.072 1 190 . 22 LEU HB2 H 1.878 0 1 191 . 22 LEU HG H 1.671 0 1 192 . 22 LEU CD1 C 25.461 0 1 193 . 22 LEU HD1 H 0.923 0 1 194 . 22 LEU CD2 C 24.043 0 1 195 . 22 LEU C C 173.477 0.013 1 196 . 23 GLN N N 114.257 0.009 1 197 . 23 GLN H H 7.332 0.004 1 198 . 23 GLN CA C 55.561 0.089 1 199 . 23 GLN HA H 4.475 0 1 200 . 23 GLN CB C 30.134 0.123 1 201 . 23 GLN HB2 H 1.907 0 1 202 . 23 GLN CG C 34.301 0 1 203 . 23 GLN HG2 H 2.587 0 2 204 . 23 GLN HG3 H 2.438 0 2 205 . 23 GLN CD C 172.28 0 1 206 . 23 GLN NE2 N 110.65 0 1 207 . 23 GLN HE21 H 6.795 0 2 208 . 23 GLN HE22 H 7.376 0 2 209 . 23 GLN C C 175.949 0.002 1 210 . 24 GLY N N 109.334 5.968 1 211 . 24 GLY H H 8.045 0.087 1 212 . 24 GLY CA C 46.952 0.09 1 213 . 24 GLY HA2 H 3.903 0 1 214 . 24 GLY C C 177.75 0 1 215 . 25 LYS N N 118.683 0.012 1 216 . 25 LYS H H 7.894 0 1 217 . 25 LYS CA C 54.904 0.054 1 218 . 25 LYS HA H 4.83 0 1 219 . 25 LYS CB C 37.984 0.064 1 220 . 25 LYS HB2 H 2.049 0 1 221 . 25 LYS HG2 H 1.57 0 1 222 . 25 LYS HD2 H 1.399 0 1 223 . 25 LYS CE C 42.641 0 1 224 . 25 LYS HE2 H 3.402 0 1 225 . 25 LYS C C 175.66 0.005 1 226 . 26 THR N N 110.169 0.011 1 227 . 26 THR H H 8.201 0.011 1 228 . 26 THR CA C 61.179 0.082 1 229 . 26 THR HA H 4.456 0 1 230 . 26 THR CB C 71.191 0.009 1 231 . 26 THR HB H 3.94 0 1 232 . 26 THR HG2 H 1.343 0 1 233 . 26 THR C C 175.958 0.021 1 234 . 27 ILE N N 120.678 0.056 1 235 . 27 ILE H H 8.951 0.002 1 236 . 27 ILE CA C 66.587 0.056 1 237 . 27 ILE HA H 4.749 0 1 238 . 27 ILE CB C 37.9 0 1 239 . 27 ILE HB H 1.844 0 1 240 . 27 ILE CG2 C 18.789 0 1 241 . 27 ILE HG12 H 1.382 0 1 242 . 27 ILE CD1 C 14.285 0 1 243 . 27 ILE HD1 H 0.979 0 1 244 . 27 ILE C C 175.206 0.015 1 245 . 28 LYS N N 118.816 0.008 1 246 . 28 LYS H H 7.961 0.006 1 247 . 28 LYS CA C 60.91 0.003 1 248 . 28 LYS HA H 3.896 0 1 249 . 28 LYS CB C 33.283 0.154 1 250 . 28 LYS HB2 H 1.824 0 1 251 . 28 LYS CG C 25.961 0 1 252 . 28 LYS HG2 H 1.62 0 1 253 . 28 LYS CD C 29.881 0 1 254 . 28 LYS HD2 H 1.433 0 1 255 . 28 LYS CE C 42.557 0 1 256 . 28 LYS HE2 H 3.11 0 1 257 . 28 LYS C C 174.422 0.022 1 258 . 29 GLN N N 118.036 0.01 1 259 . 29 GLN H H 7.674 0.002 1 260 . 29 GLN CA C 59.206 0.004 1 261 . 29 GLN HA H 3.981 0 1 262 . 29 GLN CB C 29.291 0.108 1 263 . 29 GLN HB2 H 2.24 0 1 264 . 29 GLN CG C 33.634 0 1 265 . 29 GLN HG2 H 2.45 0 1 266 . 29 GLN CD C 172.37 0 1 267 . 29 GLN NE2 N 111.94 0 1 268 . 29 GLN HE21 H 6.915 0 2 269 . 29 GLN HE22 H 7.932 0 2 270 . 29 GLN C C 173.742 0.021 1 271 . 30 TYR N N 118.778 0.011 1 272 . 30 TYR H H 8.556 0.005 1 273 . 30 TYR CA C 61.977 0.031 1 274 . 30 TYR HA H 3.872 0 1 275 . 30 TYR CB C 40.154 0.073 1 276 . 30 TYR HB2 H 3.019 0 2 277 . 30 TYR HB3 H 2.795 0 2 278 . 30 TYR HD1 H 6.747 0 1 279 . 30 TYR HE1 H 6.595 0 1 280 . 30 TYR C C 175.406 0.021 1 281 . 31 ALA N N 119.011 0.005 1 282 . 31 ALA H H 8.714 0.003 1 283 . 31 ALA CA C 55.514 0.024 1 284 . 31 ALA HA H 3.61 0 1 285 . 31 ALA CB C 18.724 0.126 1 286 . 31 ALA HB H 1.358 0 1 287 . 31 ALA C C 173.019 0.019 1 288 . 32 LEU N N 116.707 0.008 1 289 . 32 LEU H H 8.049 0.004 1 290 . 32 LEU CA C 59.14 0.053 1 291 . 32 LEU HA H 3.969 0 1 292 . 32 LEU CB C 42.322 0.156 1 293 . 32 LEU HB2 H 1.901 0 1 294 . 32 LEU CG C 25.627 0 1 295 . 32 LEU HG H 1.709 0 1 296 . 32 LEU CD1 C 21.124 0 1 297 . 32 LEU HD1 H 1.05 0 1 298 . 32 LEU C C 172.886 0.018 1 299 . 33 GLU N N 117.284 0.012 1 300 . 33 GLU H H 7.715 0.009 1 301 . 33 GLU CA C 59.175 0.258 1 302 . 33 GLU HA H 3.997 0 1 303 . 33 GLU CB C 29.603 0.092 1 304 . 33 GLU HB2 H 2.23 0 1 305 . 33 GLU CG C 36.886 0 1 306 . 33 GLU HG2 H 2.56 0 1 307 . 33 GLU C C 173.285 0.025 1 308 . 34 ARG N N 115.209 0.011 1 309 . 34 ARG H H 7.445 0.005 1 310 . 34 ARG CA C 56.207 0.038 1 311 . 34 ARG HA H 3.902 0 1 312 . 34 ARG CB C 29.5 0 1 313 . 34 ARG HB2 H 1.558 0 1 314 . 34 ARG HG2 H 1.448 0 1 315 . 34 ARG HD2 H 2.855 0 1 316 . 34 ARG C C 173.758 0.007 1 317 . 35 LEU N N 117.808 0.008 1 318 . 35 LEU H H 7.904 0.236 1 319 . 35 LEU CA C 57.491 0.101 1 320 . 35 LEU HA H 3.647 0 1 321 . 35 LEU CB C 42.858 0.078 1 322 . 35 LEU HB2 H 1.45 0 1 323 . 35 LEU CG C 25.461 0 1 324 . 35 LEU HG H 1.66 0 1 325 . 35 LEU CD1 C 23.292 0 1 326 . 35 LEU HD1 H 0.587 0 1 327 . 35 LEU C C 176.367 0.004 1 328 . 36 PHE N N 115.013 0.039 1 329 . 36 PHE H H 7.479 0.008 1 330 . 36 PHE CA C 54.996 0.09 1 331 . 36 PHE HA H 4.97 0 1 332 . 36 PHE CB C 39.641 0 1 333 . 36 PHE HB2 H 3.06 0 2 334 . 36 PHE HB3 H 2.9 0 2 335 . 36 PHE HD1 H 7.139 0 1 336 . 36 PHE HE1 H 7.27 0 1 337 . 36 PHE HZ H 7.371 0 1 338 . 36 PHE C C 179.29 0 1 339 . 37 PRO CA C 63.98 0 1 340 . 37 PRO HA H 4.475 0 1 341 . 37 PRO CB C 32.412 0.08 1 342 . 37 PRO HB2 H 2.198 0 1 343 . 37 PRO CG C 27.379 0 1 344 . 37 PRO HG2 H 1.918 0 1 345 . 37 PRO CD C 50.397 0 1 346 . 37 PRO HD2 H 3.556 0 2 347 . 37 PRO HD3 H 3.356 0 2 348 . 37 PRO C C 173.847 0 1 349 . 38 GLY N N 109.502 0.017 1 350 . 38 GLY H H 8.566 0.005 1 351 . 38 GLY CA C 45.935 0.082 1 352 . 38 GLY HA2 H 3.921 0 2 353 . 38 GLY HA3 H 4.003 0 2 354 . 39 ASP N N 120.441 0.012 1 355 . 39 ASP H H 8.181 0 1 356 . 39 ASP CA C 54.955 0.054 1 357 . 39 ASP HA H 4.605 0 1 358 . 39 ASP CB C 41.699 0.122 1 359 . 39 ASP HB2 H 2.655 0 2 360 . 39 ASP HB3 H 2.714 0 2 361 . 39 ASP C C 175.617 0.007 1 362 . 40 ALA N N 123.499 0.001 1 363 . 40 ALA H H 8.233 0.006 1 364 . 40 ALA CA C 53.755 0.014 1 365 . 40 ALA HA H 4.272 0 1 366 . 40 ALA CB C 19.569 0.093 1 367 . 40 ALA HB H 1.399 0 1 368 . 40 ALA C C 174.297 0.004 1 369 . 41 ASP N N 118.305 0.013 1 370 . 41 ASP H H 8.16 0.005 1 371 . 41 ASP CA C 55.15 0.083 1 372 . 41 ASP HA H 4.57 0 1 373 . 41 ASP CB C 41.553 0.094 1 374 . 41 ASP HB2 H 2.65 0 2 375 . 41 ASP HB3 H 2.71 0 2 376 . 41 ASP C C 175.436 0.006 1 377 . 42 ALA N N 123.957 0 1 378 . 42 ALA H H 8.133 0.004 1 379 . 42 ALA CA C 53.88 0.044 1 380 . 42 ALA HA H 4.2 0 1 381 . 42 ALA CB C 19.446 0.108 1 382 . 42 ALA HB H 1.349 0 1 383 . 42 ALA C C 174.048 0.015 1 384 . 43 ASP N N 119.029 0.008 1 385 . 43 ASP H H 8.233 0.001 1 386 . 43 ASP CA C 56.082 0.002 1 387 . 43 ASP HA H 4.576 0 1 388 . 43 ASP CB C 41.761 0.021 1 389 . 43 ASP HB2 H 2.78 0 2 390 . 43 ASP HB3 H 2.631 0 2 391 . 43 ASP C C 174.68 0.01 1 392 . 44 GLN N N 121.037 0.004 1 393 . 44 GLN H H 8.343 0.002 1 394 . 44 GLN CA C 58.026 0.034 1 395 . 44 GLN HA H 4.14 0 1 396 . 44 GLN CB C 29.098 0.123 1 397 . 44 GLN HB2 H 2.075 0 1 398 . 44 GLN CG C 34.051 0 1 399 . 44 GLN HG2 H 2.4 0 1 400 . 44 GLN CD C 171.87 0 1 401 . 44 GLN NE2 N 112.2 0 1 402 . 44 GLN HE21 H 6.792 0 2 403 . 44 GLN HE22 H 7.586 0 2 404 . 44 GLN C C 174.78 0.041 1 405 . 45 ALA N N 122.805 0.016 1 406 . 45 ALA H H 8.261 0 1 407 . 45 ALA CA C 54.763 0.086 1 408 . 45 ALA HA H 4.222 0 1 409 . 45 ALA CB C 18.858 0.136 1 410 . 45 ALA HB H 1.38 0 1 411 . 45 ALA C C 172.858 0.022 1 412 . 46 TRP N N 118.745 0 1 413 . 46 TRP H H 8.038 0 1 414 . 46 TRP CA C 59.275 0.036 1 415 . 46 TRP HA H 4.565 0 1 416 . 46 TRP CB C 29.853 0.105 1 417 . 46 TRP HB2 H 3.342 0 1 418 . 46 TRP HD1 H 7.277 0 1 419 . 46 TRP HE3 H 7.561 0 1 420 . 46 TRP NE1 N 128.936 0 1 421 . 46 TRP HE1 H 10.133 0 1 422 . 46 TRP HZ3 H 6.996 0 1 423 . 46 TRP HZ2 H 7.416 0 1 424 . 46 TRP HH2 H 7.111 0 1 425 . 46 TRP C C 174.854 0.051 1 426 . 47 GLN N N 118.632 0.006 1 427 . 47 GLN H H 7.989 0.003 1 428 . 47 GLN CA C 58.476 0.108 1 429 . 47 GLN HA H 3.897 0 1 430 . 47 GLN CB C 28.808 0.139 1 431 . 47 GLN HB2 H 2.33 0 1 432 . 47 GLN CG C 33.717 0 1 433 . 47 GLN HG2 H 2.659 0 1 434 . 47 GLN CD C 172.04 0 1 435 . 47 GLN NE2 N 112.11 0 1 436 . 47 GLN HE21 H 6.841 0 2 437 . 47 GLN HE22 H 7.443 0 2 438 . 47 GLN C C 174.137 0.034 1 439 . 48 GLU N N 119.617 0.026 1 440 . 48 GLU H H 8.102 0.003 1 441 . 48 GLU CA C 58.8 0 1 442 . 48 GLU HA H 4.111 0 1 443 . 48 GLU CB C 30.037 0.085 1 444 . 48 GLU HB2 H 2.03 0 2 445 . 48 GLU HB3 H 2.097 0 2 446 . 48 GLU CG C 36.469 0 1 447 . 48 GLU HG2 H 2.26 0 2 448 . 48 GLU HG3 H 2.375 0 2 449 . 48 GLU C C 173.95 0 1 450 . 49 LEU N N 121.781 0.001 1 451 . 49 LEU H H 8.014 0.004 1 452 . 49 LEU CA C 57.625 0.091 1 453 . 49 LEU HA H 4.099 0 1 454 . 49 LEU CB C 42.457 0.149 1 455 . 49 LEU HB2 H 1.64 0 1 456 . 49 LEU CG C 27.295 0 1 457 . 49 LEU CD1 C 24.627 0 1 458 . 49 LEU HD1 H 0.87 0 1 459 . 49 LEU C C 173.872 0.007 1 460 . 50 LYS N N 118.944 0.009 1 461 . 50 LYS H H 8.161 0.005 1 462 . 50 LYS CA C 59.256 0.038 1 463 . 50 LYS HA H 3.86 0 1 464 . 50 LYS CB C 32.405 0.087 1 465 . 50 LYS HB2 H 1.662 0 1 466 . 50 LYS CG C 24.877 0 1 467 . 50 LYS HG2 H 1.255 0 1 468 . 50 LYS CD C 29.38 0 1 469 . 50 LYS HD2 H 1.55 0 1 470 . 50 LYS CE C 42.307 0 1 471 . 50 LYS HE2 H 2.85 0 1 472 . 50 LYS C C 173.415 0.031 1 473 . 51 THR N N 114.447 0.066 1 474 . 51 THR H H 7.839 0.003 1 475 . 51 THR CA C 64.838 0.031 1 476 . 51 THR HA H 4.27 0 1 477 . 51 THR CB C 69.654 0.076 1 478 . 51 THR HB H 4.085 0 1 479 . 51 THR CG2 C 21.958 0 1 480 . 51 THR HG2 H 1.29 0 1 481 . 51 THR C C 176.45 0.02 1 482 . 52 MET N N 121.57 0 1 483 . 52 MET H H 8.018 0.003 1 484 . 52 MET CA C 57.935 0.039 1 485 . 52 MET HA H 4.313 0 1 486 . 52 MET CB C 33.35 0.162 1 487 . 52 MET HB2 H 2.145 0 2 488 . 52 MET HB3 H 2.238 0 2 489 . 52 MET CG C 32.216 0 1 490 . 52 MET HG2 H 2.537 0 1 491 . 52 MET C C 174.618 0.002 1 492 . 53 LEU N N 119.893 0.003 1 493 . 53 LEU H H 8.163 0.003 1 494 . 53 LEU CA C 56.637 0.058 1 495 . 53 LEU HA H 4.163 0 1 496 . 53 LEU CB C 42.678 0.056 1 497 . 53 LEU HB2 H 1.709 0 1 498 . 53 LEU CG C 27.129 0 1 499 . 53 LEU HG H 1.532 0 1 500 . 53 LEU CD1 C 25.711 0 1 501 . 53 LEU HD1 H 0.841 0 1 502 . 53 LEU CD2 C 23.626 0 1 503 . 53 LEU C C 173.681 0.009 1 504 . 54 GLY N N 107.503 0.003 1 505 . 54 GLY H H 8.065 0.005 1 506 . 54 GLY CA C 46.417 0.059 1 507 . 54 GLY HA2 H 3.934 0 1 508 . 54 GLY C C 177.632 0.008 1 509 . 55 ASN N N 118.946 0.01 1 510 . 55 ASN H H 8.17 0.007 1 511 . 55 ASN CA C 54.157 0.06 1 512 . 55 ASN HA H 4.71 0 1 513 . 55 ASN CB C 39.224 0.102 1 514 . 55 ASN HB2 H 2.812 0 2 515 . 55 ASN HB3 H 2.865 0 2 516 . 55 ASN CG C 175.18 0 1 517 . 55 ASN ND2 N 112.29 0 1 518 . 55 ASN HD21 H 6.88 0.002 2 519 . 55 ASN HD22 H 7.551 0 2 520 . 55 ASN C C 176.498 0.002 1 521 . 56 ARG N N 120.379 0.007 1 522 . 56 ARG H H 8.111 0.008 1 523 . 56 ARG CA C 57.123 0.038 1 524 . 56 ARG HA H 3.95 0 1 525 . 56 ARG CB C 30.931 0.086 1 526 . 56 ARG HB2 H 1.839 0 1 527 . 56 ARG CG C 27.295 0 1 528 . 56 ARG CD C 43.725 0 1 529 . 56 ARG HD2 H 3.194 0 1 530 . 56 ARG C C 175.448 0.002 1 531 . 57 ILE N N 120.338 0.018 1 532 . 57 ILE H H 8.01 0.006 1 533 . 57 ILE CA C 62.192 0.05 1 534 . 57 ILE HA H 4.108 0 1 535 . 57 ILE CB C 39.022 0.074 1 536 . 57 ILE HB H 1.808 0 1 537 . 57 ILE CG2 C 17.955 0 1 538 . 57 ILE HG2 H 0.951 0 1 539 . 57 ILE CG1 C 27.796 0 1 540 . 57 ILE HG12 H 1.506 0 1 541 . 57 ILE CD1 C 13.285 0 1 542 . 57 ILE HD1 H 0.897 0 1 543 . 57 ILE C C 175.906 0.005 1 544 . 58 ASN N N 121.322 0.007 1 545 . 58 ASN H H 8.333 0.007 1 546 . 58 ASN CA C 53.915 0.144 1 547 . 58 ASN HA H 4.71 0 1 548 . 58 ASN CB C 39.391 0.096 1 549 . 58 ASN HB2 H 2.88 0 2 550 . 58 ASN HB3 H 2.785 0 2 551 . 58 ASN CG C 112.29 0 1 552 . 58 ASN ND2 N 112.82 0 1 553 . 58 ASN HD21 H 6.881 0.001 2 554 . 58 ASN HD22 H 7.605 0 2 555 . 58 ASN C C 176.882 0.002 1 556 . 59 ASP N N 121.272 0.002 1 557 . 59 ASP H H 8.218 0.005 1 558 . 59 ASP CA C 55.313 0.087 1 559 . 59 ASP HA H 4.575 0 1 560 . 59 ASP CB C 41.633 0.105 1 561 . 59 ASP HB2 H 2.72 0 1 562 . 59 ASP C C 175.022 0.008 1 563 . 60 GLY N N 108.681 0.017 1 564 . 60 GLY H H 8.315 0.003 1 565 . 60 GLY CA C 46.267 0.059 1 566 . 60 GLY HA2 H 3.959 0 1 567 . 60 GLY C C 177.378 0.002 1 568 . 61 LEU N N 121.363 0.019 1 569 . 61 LEU H H 8.057 0.004 1 570 . 61 LEU CA C 55.912 0.1 1 571 . 61 LEU HA H 4.32 0 1 572 . 61 LEU CB C 42.663 0.128 1 573 . 61 LEU HB2 H 1.61 0 1 574 . 61 LEU CG C 27.212 0 1 575 . 61 LEU HG H 1.721 0 1 576 . 61 LEU CD1 C 25.294 0 1 577 . 61 LEU HD1 H 0.873 0 1 578 . 61 LEU CD2 C 23.626 0 1 579 . 61 LEU C C 174.557 0.001 1 580 . 62 ALA N N 123.46 0.016 1 581 . 62 ALA H H 8.164 0.004 1 582 . 62 ALA CA C 53.406 0.058 1 583 . 62 ALA HA H 4.294 0 1 584 . 62 ALA CB C 19.425 0.152 1 585 . 62 ALA HB H 1.42 0 1 586 . 62 ALA C C 173.788 0.004 1 587 . 63 GLY N N 107.48 0.015 1 588 . 63 GLY H H 8.24 0.004 1 589 . 63 GLY CA C 45.82 0.092 1 590 . 63 GLY HA2 H 3.95 0 1 591 . 63 GLY C C 177.898 0.022 1 592 . 64 LYS N N 120.633 0.018 1 593 . 64 LYS H H 8.024 0.005 1 594 . 64 LYS CA C 56.668 0.07 1 595 . 64 LYS HA H 4.371 0 1 596 . 64 LYS CB C 33.665 0.029 1 597 . 64 LYS HB2 H 1.774 0 2 598 . 64 LYS HB3 H 1.857 0 2 599 . 64 LYS CG C 25.044 0 1 600 . 64 LYS HG2 H 1.416 0 2 601 . 64 LYS HG3 H 1.347 0 2 602 . 64 LYS CD C 29.38 0 1 603 . 64 LYS HD2 H 1.672 0 1 604 . 64 LYS CE C 42.39 0 1 605 . 64 LYS HE2 H 2.99 0 1 606 . 64 LYS C C 175.477 0.006 1 607 . 65 VAL N N 120.766 0.011 1 608 . 65 VAL H H 8.114 0.003 1 609 . 65 VAL CA C 62.596 0.054 1 610 . 65 VAL HA H 4.185 0 1 611 . 65 VAL CB C 33.346 0.099 1 612 . 65 VAL HB H 2.09 0 1 613 . 65 VAL CG1 C 21.124 0 1 614 . 65 VAL HG1 H 0.953 0 1 615 . 65 VAL C C 175.906 0.004 1 616 . 66 SER N N 119.49 0.011 1 617 . 66 SER H H 8.426 0.005 1 618 . 66 SER CA C 58.711 0.241 1 619 . 66 SER HA H 4.578 0 1 620 . 66 SER CB C 64.376 0.025 1 621 . 66 SER HB2 H 3.899 0 1 622 . 66 SER C C 177.246 0.004 1 623 . 67 THR N N 116.248 0 1 624 . 67 THR H H 8.206 0.006 1 625 . 67 THR CA C 62.34 0.022 1 626 . 67 THR HA H 4.377 0 1 627 . 67 THR CB C 70.105 0.044 1 628 . 67 THR HB H 3.903 0 1 629 . 67 THR CG2 C 21.958 0 1 630 . 67 THR HG2 H 1.22 0 1 631 . 67 THR C C 177.608 0 1 632 . 68 LYS N N 123.354 0.025 1 633 . 68 LYS H H 8.244 0.005 1 634 . 68 LYS CA C 56.789 0.07 1 635 . 68 LYS HA H 4.36 0 1 636 . 68 LYS CB C 33.724 0.11 1 637 . 68 LYS HB2 H 1.8 0 1 638 . 68 LYS CG C 24.877 0 1 639 . 68 LYS HG2 H 1.43 0 1 640 . 68 LYS CD C 29.297 0 1 641 . 68 LYS HD2 H 1.66 0 1 642 . 68 LYS CE C 42.39 0 1 643 . 68 LYS HE2 H 2.979 0 1 644 . 68 LYS C C 175.595 0.016 1 645 . 69 SER N N 117.72 0.021 1 646 . 69 SER H H 8.396 0.004 1 647 . 69 SER CA C 58.614 0.078 1 648 . 69 SER HA H 4.517 0 1 649 . 69 SER CB C 64.502 0.058 1 650 . 69 SER HB2 H 3.896 0 1 651 . 69 SER C C 177.42 0.01 1 652 . 70 VAL N N 121.018 0.009 1 653 . 70 VAL H H 8.219 0.006 1 654 . 70 VAL CA C 63.433 0.102 1 655 . 70 VAL HA H 4.113 0 1 656 . 70 VAL CB C 33.04 0.142 1 657 . 70 VAL HB H 2.125 0 1 658 . 70 VAL CG1 C 21.124 0 1 659 . 70 VAL HG1 H 0.967 0 2 660 . 70 VAL HG2 H 0.904 0 2 661 . 70 VAL C C 175.402 0.007 1 662 . 71 GLY N N 111.293 0.009 1 663 . 71 GLY H H 8.399 0.004 1 664 . 71 GLY CA C 45.801 0.093 1 665 . 71 GLY HA2 H 3.945 0 1 666 . 71 GLY C C 177.992 0.042 1 667 . 72 GLU N N 120.552 0.014 1 668 . 72 GLU H H 8.082 0.004 1 669 . 72 GLU CA C 57.141 0.041 1 670 . 72 GLU HA H 4.306 0 1 671 . 72 GLU CB C 30.949 0.178 1 672 . 72 GLU HB2 H 1.989 0 2 673 . 72 GLU HB3 H 2.039 0 2 674 . 72 GLU CG C 36.636 0 1 675 . 72 GLU HG2 H 2.25 0 1 676 . 72 GLU C C 175.625 0 1 677 . 73 ILE N N 122.181 0.004 1 678 . 73 ILE H H 8.171 0.002 1 679 . 73 ILE CA C 61.867 0.009 1 680 . 73 ILE HA H 4.12 0 1 681 . 73 ILE CB C 38.967 0.094 1 682 . 73 ILE HB H 1.873 0 1 683 . 73 ILE CG2 C 17.871 0 1 684 . 73 ILE HG2 H 0.92 0 1 685 . 73 ILE CG1 C 27.629 0 1 686 . 73 ILE CD1 C 13.118 0 1 687 . 73 ILE C C 175.842 0.003 1 688 . 74 LEU N N 126.183 0.001 1 689 . 74 LEU H H 8.342 0.003 1 690 . 74 LEU CA C 55.653 0 1 691 . 74 LEU HA H 4.381 0 1 692 . 74 LEU CB C 42.895 0.066 1 693 . 74 LEU HB2 H 1.67 0 1 694 . 74 LEU CG C 27.379 0 1 695 . 74 LEU HG H 1.61 0 1 696 . 74 LEU CD1 C 25.21 0 1 697 . 74 LEU HD1 H 0.9 0 1 698 . 74 LEU CD2 C 23.793 0 1 699 . 74 LEU C C 175.054 0 1 700 . 75 ASP N N 121.359 0.001 1 701 . 75 ASP H H 8.241 0.004 1 702 . 75 ASP CA C 55.197 0.027 1 703 . 75 ASP HA H 4.578 0 1 704 . 75 ASP CB C 41.654 0.078 1 705 . 75 ASP HB2 H 2.623 0 2 706 . 75 ASP HB3 H 2.736 0 2 707 . 75 ASP C C 175.472 0.008 1 708 . 76 GLU N N 121.15 0.001 1 709 . 76 GLU H H 8.355 0.002 1 710 . 76 GLU CA C 57.653 0.08 1 711 . 76 GLU HA H 4.246 0 1 712 . 76 GLU CB C 30.947 0.023 1 713 . 76 GLU HB2 H 1.988 0 2 714 . 76 GLU HB3 H 2.071 0 2 715 . 76 GLU CG C 36.553 0 1 716 . 76 GLU HG2 H 2.29 0 2 717 . 76 GLU HG3 H 2.259 0 2 718 . 76 GLU C C 175.231 0.001 1 719 . 77 GLU N N 121.16 0.018 1 720 . 77 GLU H H 8.4 0.002 1 721 . 77 GLU CA C 57.3 0.066 1 722 . 77 GLU HA H 4.263 0 1 723 . 77 GLU CB C 30.625 0.154 1 724 . 77 GLU HB2 H 2.008 0 2 725 . 77 GLU HB3 H 2.067 0 2 726 . 77 GLU CG C 36.636 0 1 727 . 77 GLU HG2 H 2.299 0 2 728 . 77 GLU HG3 H 2.259 0 2 729 . 77 GLU C C 175.299 0.001 1 730 . 78 LEU N N 122.297 0.002 1 731 . 78 LEU H H 8.167 0.004 1 732 . 78 LEU CA C 55.665 0.051 1 733 . 78 LEU HA H 4.382 0 1 734 . 78 LEU CB C 42.637 0.069 1 735 . 78 LEU HB2 H 1.721 0 1 736 . 78 LEU CG C 27.379 0 1 737 . 78 LEU HG H 1.63 0 1 738 . 78 LEU CD1 C 25.377 0 1 739 . 78 LEU HD1 H 0.894 0 1 740 . 78 LEU CD2 C 23.459 0 1 741 . 78 LEU C C 174.547 0.002 1 742 . 79 SER N N 115.94 0.007 1 743 . 79 SER H H 8.188 0.007 1 744 . 79 SER CA C 59.061 0.007 1 745 . 79 SER HA H 4.451 0 1 746 . 79 SER CB C 64.456 0 1 747 . 79 SER HB2 H 3.896 0 1 748 . 79 SER C C 176.883 0.014 1 749 . 80 GLY N N 110.594 0.005 1 750 . 80 GLY H H 8.329 0.04 1 751 . 80 GLY CA C 45.929 0.067 1 752 . 80 GLY HA2 H 4 0 1 753 . 80 GLY C C 178.152 0.003 1 754 . 81 ASP N N 120.45 0.013 1 755 . 81 ASP H H 8.255 0.002 1 756 . 81 ASP CA C 54.949 0.073 1 757 . 81 ASP HA H 4.624 0 1 758 . 81 ASP CB C 41.589 0.079 1 759 . 81 ASP HB2 H 2.623 0 2 760 . 81 ASP HB3 H 2.709 0 2 761 . 81 ASP C C 175.915 0.009 1 762 . 82 ARG N N 121.056 0.002 1 763 . 82 ARG H H 8.152 0.002 1 764 . 82 ARG CA C 56.251 0.069 1 765 . 82 ARG HA H 4.35 0 1 766 . 82 ARG CB C 31.344 0.086 1 767 . 82 ARG HB2 H 1.926 0 1 768 . 82 ARG CG C 27.045 0 1 769 . 82 ARG HG2 H 1.76 0 2 770 . 82 ARG HG3 H 1.66 0 2 771 . 82 ARG CD C 43.725 0 1 772 . 82 ARG HD2 H 3.22 0 1 773 . 82 ARG C C 177.065 0.011 1 774 . 83 ALA N N 130.888 0.026 1 775 . 83 ALA H H 7.912 0.001 1 776 . 83 ALA CA C 54.38 0 1 777 . 83 ALA HA H 4.13 0 1 778 . 83 ALA CB C 20.659 0 1 779 . 83 ALA HB H 1.345 0 1 780 . 83 ALA C C 169.56 0 1 stop_ save_