data_5563 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Assignment of backbone 1H, 13C and 15N resonances of ParG, a protein required for active partition of bacterial plasmids ; _BMRB_accession_number 5563 _BMRB_flat_file_name bmr5563.str _Entry_type original _Submission_date 2002-10-18 _Accession_date 2002-10-18 _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 Golovanov Alexander P. . 2 Barilla Daniela . . 3 Golovanova Marina . . 4 Hayes Finbarr . . 5 Lian Lu-Yun . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 435 "13C chemical shifts" 317 "15N chemical shifts" 83 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2019-10-30 update BMRB 'update entry etc.' 2003-12-08 original author 'original release' stop_ _Original_release_date 2002-10-18 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; ParG, a protein required for active partition of bacterial plasmids, has a dimeric ribbon-helix-helix structure ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 14622405 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Golovanov Alexander P. . 2 Barilla Daniela . . 3 Golovanova Marina . . 4 Hayes Finbarr . . 5 Lian Lu-Yun . . stop_ _Journal_abbreviation 'Mol. Microbiol.' _Journal_volume 50 _Journal_issue 4 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 1141 _Page_last 1153 _Year 2003 _Details . loop_ _Keyword 'active partition' 'bacterial plasmids' stop_ save_ ####################################### # Cited references within the entry # ####################################### save_reference_1 _Saveframe_category citation _Citation_full ; Hayes F. The partition system of multidrug resistance plasmid TP228 includes a novel protein that epitomizes an evolutionarily distinct subgroup of the ParA superfamily. Mol Microbiol. 2000 Aug;37(3):528-41. ; _Citation_title ; The partition system of multidrug resistance plasmid TP228 includes a novel protein that epitomizes an evolutionarily distinct subgroup of the ParA superfamily. ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 10931346 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Hayes F . . stop_ _Journal_abbreviation 'Mol. Microbiol.' _Journal_name_full 'Molecular microbiology' _Journal_volume 37 _Journal_issue 3 _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 528 _Page_last 541 _Year 2000 _Details ; The segregational stability of bacterial, low-copy-number plasmids is promoted primarily by active partition. The plasmid-specified components of the prototypical P1 plasmid partition system consist of two proteins, ParA (44.3 kDa) and ParB (38.5 kDa), which, in conjunction with integration host factor, form a nucleoprotein complex at the plasmid partition site, parS. This complex is the probable substrate for the directed temporal and spatial intracellular movement of plasmids before cell division. The genetic organization of the partition cassette of the multidrug resistance plasmid TP228 differs markedly from that of the P1 paradigm. The TP228 system includes a novel member (ParF; 22.0 kDa) of the ParA superfamily of ATPases, of which the P1 ParA protein is the archetype. However, the ParF protein and its immediate relatives form a discrete subgroup of the ParA superfamily, which evolutionarily is more related to the MinD subgroup of cell division proteins than to ParA of P1. The TP228 and P1 partition modules differ further in that the former does not include a parB homologue, but does specify a protein (ParG; 8.6 kDa) unrelated to ParB. Homologues of the parF gene are widely disseminated on eubacterial genomes, suggesting that ParF-mediated partition may be a common mechanism by which plasmid segregational stability is achieved. ; save_ ################################## # Molecular system description # ################################## save_system_ParG _Saveframe_category molecular_system _Mol_system_name 'ParG dimer' _Abbreviation_common ParG _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'ParG subunit_1' $ParG 'ParG subunit_2' $ParG stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state dimer _System_paramagnetic no _System_thiol_state 'not reported' loop_ _Magnetic_equivalence_ID _Magnetically_equivalent_system_component 1 'ParG subunit_1' 1 'ParG subunit_2' stop_ loop_ _Biological_function 'required for active partition of bacterial plasmids' stop_ _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_ParG _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common ParG _Abbreviation_common ParG _Molecular_mass 8625 _Mol_thiol_state 'not reported' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 76 _Mol_residue_sequence ; MSLEKAHTSVKKMTFGENRD LERVVTAPVSSGKIKRVNVN FDEEKHTRFKAACARKGTSI TDVVNQLVDNWLKENE ; loop_ _Residue_seq_code _Residue_label 1 MET 2 SER 3 LEU 4 GLU 5 LYS 6 ALA 7 HIS 8 THR 9 SER 10 VAL 11 LYS 12 LYS 13 MET 14 THR 15 PHE 16 GLY 17 GLU 18 ASN 19 ARG 20 ASP 21 LEU 22 GLU 23 ARG 24 VAL 25 VAL 26 THR 27 ALA 28 PRO 29 VAL 30 SER 31 SER 32 GLY 33 LYS 34 ILE 35 LYS 36 ARG 37 VAL 38 ASN 39 VAL 40 ASN 41 PHE 42 ASP 43 GLU 44 GLU 45 LYS 46 HIS 47 THR 48 ARG 49 PHE 50 LYS 51 ALA 52 ALA 53 CYS 54 ALA 55 ARG 56 LYS 57 GLY 58 THR 59 SER 60 ILE 61 THR 62 ASP 63 VAL 64 VAL 65 ASN 66 GLN 67 LEU 68 VAL 69 ASP 70 ASN 71 TRP 72 LEU 73 LYS 74 GLU 75 ASN 76 GLU stop_ _Sequence_homology_query_date 2008-08-19 _Sequence_homology_query_revised_last_date 2008-08-19 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 1P94 'Nmr Structure Of Parg Symmetric Dimer' 100.00 76 100.00 100.00 6.89e-37 GenBank AAF74218 'plasmid partition protein ParG [Salmonella enterica subsp. enterica serovar Newport]' 100.00 76 100.00 100.00 6.89e-37 GenBank ABZ89622 'plasmid partitioning protein ParG [Escherichia coli]' 100.00 76 100.00 100.00 6.89e-37 GenBank ACA51142 'partitioning protein ParB [Salmonella enterica subsp. enterica serovar Dublin]' 100.00 76 100.00 100.00 6.89e-37 REF YP_001693222 'plasmid partitioning protein ParG [Escherichia coli]' 100.00 76 100.00 100.00 6.89e-37 REF YP_001716185 'partitioning protein ParB [Salmonella enterica subsp. enterica serovar Dublin]' 100.00 76 100.00 100.00 6.89e-37 REF ZP_02351781 'hypothetical protein Sententeri_18255 [Salmonella enterica subsp. enterica serovar Dublin str. CT_02021853]' 100.00 76 100.00 100.00 6.89e-37 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 $ParG 'Salmonella enterica subsp. enterica serovar Newport' 108619 Eubacteria . Salmonella enterica TP228 parG 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 $ParG 'recombinant technology' . . . . . stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Concentration_min_value _Concentration_max_value _Isotopic_labeling $ParG . mM 1.0 2.0 '[U-95% 15N]' stop_ save_ save_sample_2 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Concentration_min_value _Concentration_max_value _Isotopic_labeling $ParG . mM 1.0 2.0 '[U-95% 13C; U-95% 15N]' stop_ save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model DRX _Field_strength 600 _Details . save_ ############################# # NMR applied experiments # ############################# save_2D_1H-15N_HSQC_1 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-15N HSQC' _Sample_label . save_ save_2D_1H-13C_HSQC_2 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-13C HSQC' _Sample_label . save_ save_2D_1H-1H_COSY_(in_D2O)_3 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-1H COSY (in D2O)' _Sample_label . save_ save_2D_1H-1H_TOCSY_(in_D2O)_4 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-1H TOCSY (in D2O)' _Sample_label . save_ save_2D_1H-1H_NOESY_(in_D2O)_5 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-1H NOESY (in D2O)' _Sample_label . save_ save_3D_HNHA_6 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNHA' _Sample_label . save_ save_3D_HNCO_7 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCO' _Sample_label . save_ save_3D_HN(CA)CO_8 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HN(CA)CO' _Sample_label . save_ save_3D_HNCA_9 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCA' _Sample_label . save_ save_3D_HN(CO)CA_10 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HN(CO)CA' _Sample_label . save_ save_3D_CBCA(CO)NH_11 _Saveframe_category NMR_applied_experiment _Experiment_name '3D CBCA(CO)NH' _Sample_label . save_ save_3D_CBCANH_12 _Saveframe_category NMR_applied_experiment _Experiment_name '3D CBCANH' _Sample_label . save_ save_3D_HAHB(CO)NH_13 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HAHB(CO)NH' _Sample_label . save_ save_3D_15N_NOESY-HSQC_14 _Saveframe_category NMR_applied_experiment _Experiment_name '3D 15N NOESY-HSQC' _Sample_label . save_ save_3D_1H-13C-1H_HCCH-TOCSY_15 _Saveframe_category NMR_applied_experiment _Experiment_name '3D 1H-13C-1H HCCH-TOCSY' _Sample_label . save_ save_3D_15N_TOCSY-HSQC_16 _Saveframe_category NMR_applied_experiment _Experiment_name '3D 15N TOCSY-HSQC' _Sample_label . save_ ####################### # Sample conditions # ####################### save_ex-cond_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 5.5 0.1 na 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 C 13 'methyl protons' ppm 0.0 . indirect . . . 0.251449530 DSS H 1 'methyl protons' ppm 0.0 internal direct . . . 1.000000000 DSS N 15 'methyl protons' ppm 0.0 . indirect . . . 0.101329118 stop_ save_ ################################### # Assigned chemical shift lists # ################################### ################################################################### # Chemical Shift Ambiguity Index Value Definitions # # # # The values other than 1 are used for those atoms with different # # chemical shifts that cannot be assigned to stereospecific atoms # # or to specific residues or chains. # # # # Index Value Definition # # # # 1 Unique (including isolated methyl protons, # # geminal atoms, and geminal methyl # # groups with identical chemical shifts) # # (e.g. ILE HD11, HD12, HD13 protons) # # 2 Ambiguity of geminal atoms or geminal methyl # # proton groups (e.g. ASP HB2 and HB3 # # protons, LEU CD1 and CD2 carbons, or # # LEU HD11, HD12, HD13 and HD21, HD22, # # HD23 methyl protons) # # 3 Aromatic atoms on opposite sides of # # symmetrical rings (e.g. TYR HE1 and HE2 # # protons) # # 4 Intraresidue ambiguities (e.g. LYS HG and # # HD protons or TRP HZ2 and HZ3 protons) # # 5 Interresidue ambiguities (LYS 12 vs. LYS 27) # # 6 Intermolecular ambiguities (e.g. ASP 31 CA # # in monomer 1 and ASP 31 CA in monomer 2 # # of an asymmetrical homodimer, duplex # # DNA assignments, or other assignments # # that may apply to atoms in one or more # # molecule in the molecular assembly) # # 9 Ambiguous, specific ambiguity not defined # # # ################################################################### save_shift_set_1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Experiment_label '2D 1H-15N HSQC' '2D 1H-13C HSQC' '2D 1H-1H COSY (in D2O)' '2D 1H-1H TOCSY (in D2O)' '2D 1H-1H NOESY (in D2O)' '3D HNHA' '3D HNCO' '3D HN(CA)CO' '3D HNCA' '3D HN(CO)CA' '3D CBCA(CO)NH' '3D CBCANH' '3D HAHB(CO)NH' '3D 15N NOESY-HSQC' '3D 1H-13C-1H HCCH-TOCSY' '3D 15N TOCSY-HSQC' stop_ _Sample_conditions_label $ex-cond_1 _Chem_shift_reference_set_label $chemical_shift_reference _Mol_system_component_name 'ParG subunit_1' _Text_data_format . _Text_data . loop_ _Atom_shift_assign_ID _Residue_author_seq_code _Residue_seq_code _Residue_label _Atom_name _Atom_type _Chem_shift_value _Chem_shift_value_error _Chem_shift_ambiguity_code 1 . 2 SER N N 119.419 . 1 2 . 2 SER H H 8.461 . 1 3 . 3 LEU N N 122.833 . 1 4 . 3 LEU H H 8.703 . 1 5 . 3 LEU CA C 55.476 . 1 6 . 3 LEU HA H 4.368 . 1 7 . 3 LEU CB C 42.220 . 1 8 . 3 LEU HB3 H 1.593 . 1 9 . 3 LEU HB2 H 1.593 . 1 10 . 3 LEU C C 177.133 . 1 11 . 4 GLU N N 122.734 . 1 12 . 4 GLU H H 8.552 . 1 13 . 4 GLU CA C 56.683 . 1 14 . 4 GLU HA H 4.228 . 1 15 . 4 GLU CB C 30.169 . 1 16 . 4 GLU HB3 H 1.930 . 1 17 . 4 GLU HB2 H 1.930 . 1 18 . 4 GLU CG C 36.110 . 1 19 . 4 GLU HG3 H 2.254 . 1 20 . 4 GLU HG2 H 2.254 . 1 21 . 4 GLU C C 176.464 . 1 22 . 5 LYS N N 123.165 . 1 23 . 5 LYS H H 8.397 . 1 24 . 5 LYS CA C 56.328 . 1 25 . 5 LYS HA H 4.241 . 1 26 . 5 LYS CB C 32.925 . 1 27 . 5 LYS HB3 H 1.721 . 1 28 . 5 LYS HB2 H 1.721 . 1 29 . 5 LYS CG C 24.800 . 1 30 . 5 LYS HG3 H 1.406 . 1 31 . 5 LYS HG2 H 1.406 . 1 32 . 5 LYS CD C 29.198 . 1 33 . 5 LYS HD3 H 1.818 . 1 34 . 5 LYS HD2 H 1.818 . 1 35 . 5 LYS CE C 42.132 . 1 36 . 5 LYS HE3 H 3.008 . 1 37 . 5 LYS HE2 H 3.008 . 1 38 . 5 LYS C C 176.325 . 1 39 . 6 ALA N N 124.977 . 1 40 . 6 ALA H H 8.331 . 1 41 . 6 ALA CA C 52.507 . 1 42 . 6 ALA HA H 4.241 . 1 43 . 6 ALA CB C 19.200 . 1 44 . 6 ALA HB H 1.359 . 1 45 . 6 ALA C C 177.729 . 1 46 . 7 HIS N N 118.325 . 1 47 . 7 HIS H H 8.586 . 1 48 . 7 HIS CA C 55.348 . 1 49 . 7 HIS HA H 4.771 . 1 50 . 7 HIS CB C 29.190 . 1 51 . 7 HIS HB3 H 3.209 . 2 52 . 7 HIS HB2 H 3.292 . 2 53 . 7 HIS CD2 C 120.124 . 1 54 . 7 HIS HD2 H 7.275 . 2 55 . 7 HIS CE1 C 136.621 . 1 56 . 7 HIS HE1 H 8.505 . 4 57 . 7 HIS C C 174.754 . 1 58 . 8 THR N N 115.897 . 1 59 . 8 THR H H 8.231 . 1 60 . 8 THR CA C 61.839 . 1 61 . 8 THR HA H 4.357 . 1 62 . 8 THR CB C 69.910 . 1 63 . 8 THR HB H 4.176 . 1 64 . 8 THR CG2 C 21.568 . 1 65 . 8 THR HG2 H 1.136 . 1 66 . 8 THR C C 174.292 . 1 67 . 9 SER N N 118.902 . 1 68 . 9 SER H H 8.479 . 1 69 . 9 SER CA C 58.124 . 1 70 . 9 SER HA H 4.544 . 1 71 . 9 SER CB C 63.978 . 1 72 . 9 SER HB3 H 3.877 . 2 73 . 9 SER HB2 H 3.928 . 2 74 . 9 SER C C 174.461 . 1 75 . 10 VAL N N 122.467 . 1 76 . 10 VAL H H 8.242 . 1 77 . 10 VAL CA C 62.398 . 1 78 . 10 VAL HA H 4.125 . 1 79 . 10 VAL CB C 32.775 . 1 80 . 10 VAL HB H 2.082 . 1 81 . 10 VAL CG2 C 20.922 . 1 82 . 10 VAL HG2 H 0.927 . 1 83 . 10 VAL CG1 C 20.922 . 1 84 . 10 VAL HG1 H 0.927 . 1 85 . 10 VAL C C 176.088 . 1 86 . 11 LYS N N 125.884 . 1 87 . 11 LYS H H 8.397 . 1 88 . 11 LYS CA C 56.255 . 1 89 . 11 LYS HA H 4.307 . 1 90 . 11 LYS CB C 33.150 . 1 91 . 11 LYS HB3 H 1.751 . 2 92 . 11 LYS HB2 H 1.811 . 2 93 . 11 LYS CG C 24.840 . 1 94 . 11 LYS HG3 H 1.402 . 2 95 . 11 LYS HG2 H 1.460 . 2 96 . 11 LYS CD C 29.147 . 1 97 . 11 LYS HD3 H 1.708 . 1 98 . 11 LYS HD2 H 1.708 . 1 99 . 11 LYS CE C 42.113 . 1 100 . 11 LYS HE3 H 3.008 . 1 101 . 11 LYS HE2 H 3.008 . 1 102 . 11 LYS C C 176.257 . 1 103 . 12 LYS N N 123.782 . 1 104 . 12 LYS H H 8.390 . 1 105 . 12 LYS CA C 56.303 . 1 106 . 12 LYS HA H 4.280 . 1 107 . 12 LYS CB C 33.194 . 1 108 . 12 LYS HB3 H 1.744 . 1 109 . 12 LYS HB2 H 1.744 . 1 110 . 12 LYS CG C 24.840 . 1 111 . 12 LYS HG3 H 1.417 . 2 112 . 12 LYS HG2 H 1.458 . 2 113 . 12 LYS CD C 29.122 . 1 114 . 12 LYS HD3 H 1.701 . 1 115 . 12 LYS HD2 H 1.701 . 1 116 . 12 LYS CE C 42.123 . 1 117 . 12 LYS HE3 H 3.010 . 1 118 . 12 LYS HE2 H 3.010 . 1 119 . 12 LYS C C 176.393 . 1 120 . 13 MET N N 122.768 . 1 121 . 13 MET H H 8.498 . 1 122 . 13 MET CA C 55.405 . 1 123 . 13 MET HA H 4.510 . 1 124 . 13 MET CB C 33.020 . 1 125 . 13 MET HB3 H 1.987 . 1 126 . 13 MET HB2 H 1.987 . 1 127 . 13 MET CG C 32.030 . 1 128 . 13 MET HG3 H 2.490 . 2 129 . 13 MET HG2 H 2.549 . 2 130 . 13 MET C C 176.088 . 1 131 . 14 THR N N 115.660 . 1 132 . 14 THR H H 8.119 . 1 133 . 14 THR CA C 61.536 . 1 134 . 14 THR HA H 4.324 . 1 135 . 14 THR CB C 70.000 . 1 136 . 14 THR HB H 4.151 . 1 137 . 14 THR CG2 C 21.605 . 1 138 . 14 THR HG2 H 1.128 . 1 139 . 14 THR C C 174.003 . 1 140 . 15 PHE N N 122.371 . 1 141 . 15 PHE H H 8.408 . 1 142 . 15 PHE CA C 58.017 . 1 143 . 15 PHE HA H 4.650 . 1 144 . 15 PHE CB C 39.953 . 1 145 . 15 PHE HB3 H 3.187 . 2 146 . 15 PHE HB2 H 3.031 . 2 147 . 15 PHE CD1 C 131.658 . 3 148 . 15 PHE HD1 H 7.361 . 3 149 . 15 PHE CE1 C 131.786 . 3 150 . 15 PHE HE1 H 7.276 . 3 151 . 15 PHE CZ C 131.786 . 1 152 . 15 PHE HZ H 7.319 . 1 153 . 15 PHE C C 176.223 . 1 154 . 16 GLY N N 110.752 . 1 155 . 16 GLY H H 8.412 . 1 156 . 16 GLY CA C 45.355 . 1 157 . 16 GLY HA3 H 3.870 . 2 158 . 16 GLY HA2 H 3.964 . 2 159 . 16 GLY C C 174.070 . 1 160 . 17 GLU N N 120.521 . 1 161 . 17 GLU H H 8.299 . 1 162 . 17 GLU CA C 56.640 . 1 163 . 17 GLU HA H 4.275 . 1 164 . 17 GLU CB C 30.230 . 1 165 . 17 GLU HB3 H 1.950 . 1 166 . 17 GLU HB2 H 1.950 . 1 167 . 17 GLU CG C 32.830 . 1 168 . 17 GLU HG3 H 2.248 . 1 169 . 17 GLU HG2 H 2.248 . 1 170 . 17 GLU C C 176.342 . 1 171 . 18 ASN N N 119.788 . 1 172 . 18 ASN H H 8.575 . 1 173 . 18 ASN CA C 53.350 . 1 174 . 18 ASN HA H 4.696 . 1 175 . 18 ASN CB C 38.690 . 1 176 . 18 ASN HB3 H 2.763 . 2 177 . 18 ASN HB2 H 2.865 . 2 178 . 18 ASN ND2 N 113.124 . 1 179 . 18 ASN HD21 H 7.647 . 2 180 . 18 ASN HD22 H 6.970 . 2 181 . 18 ASN C C 175.370 . 1 182 . 19 ARG N N 121.908 . 1 183 . 19 ARG H H 8.391 . 1 184 . 19 ARG CA C 56.484 . 1 185 . 19 ARG HA H 4.330 . 1 186 . 19 ARG CB C 30.500 . 1 187 . 19 ARG HB3 H 1.750 . 2 188 . 19 ARG HB2 H 1.850 . 2 189 . 19 ARG CG C 27.051 . 1 190 . 19 ARG HG3 H 1.616 . 1 191 . 19 ARG HG2 H 1.616 . 1 192 . 19 ARG CD C 43.373 . 1 193 . 19 ARG HD3 H 3.189 . 1 194 . 19 ARG HD2 H 3.189 . 1 195 . 19 ARG C C 176.237 . 1 196 . 20 ASP N N 120.697 . 1 197 . 20 ASP H H 8.374 . 1 198 . 20 ASP CA C 54.758 . 1 199 . 20 ASP HA H 4.572 . 1 200 . 20 ASP CB C 40.873 . 1 201 . 20 ASP HB3 H 2.745 . 2 202 . 20 ASP HB2 H 2.616 . 2 203 . 20 ASP C C 176.428 . 1 204 . 21 LEU N N 121.911 . 1 205 . 21 LEU H H 8.085 . 1 206 . 21 LEU CA C 55.456 . 1 207 . 21 LEU HA H 4.285 . 1 208 . 21 LEU CB C 42.220 . 1 209 . 21 LEU HB3 H 1.637 . 1 210 . 21 LEU HB2 H 1.637 . 1 211 . 21 LEU CD1 C 24.947 . 1 212 . 21 LEU HD1 H 0.935 . 2 213 . 21 LEU CD2 C 23.223 . 1 214 . 21 LEU HD2 H 0.859 . 2 215 . 21 LEU C C 177.637 . 1 216 . 22 GLU N N 120.691 . 1 217 . 22 GLU H H 8.267 . 1 218 . 22 GLU CA C 56.694 . 1 219 . 22 GLU HA H 4.268 . 1 220 . 22 GLU CB C 30.093 . 1 221 . 22 GLU HB3 H 1.951 . 2 222 . 22 GLU HB2 H 2.043 . 2 223 . 22 GLU CG C 36.146 . 1 224 . 22 GLU HG3 H 2.258 . 2 225 . 22 GLU HG2 H 2.289 . 2 226 . 22 GLU C C 176.376 . 1 227 . 23 ARG N N 121.601 . 1 228 . 23 ARG H H 8.145 . 1 229 . 23 ARG CA C 56.065 . 1 230 . 23 ARG HA H 4.294 . 1 231 . 23 ARG CB C 30.694 . 1 232 . 23 ARG HB3 H 1.758 . 1 233 . 23 ARG HB2 H 1.758 . 1 234 . 23 ARG CG C 27.050 . 1 235 . 23 ARG HG3 H 1.608 . 1 236 . 23 ARG HG2 H 1.608 . 1 237 . 23 ARG CD C 43.390 . 1 238 . 23 ARG HD3 H 3.185 . 1 239 . 23 ARG HD2 H 3.185 . 1 240 . 23 ARG C C 176.020 . 1 241 . 24 VAL N N 122.671 . 1 242 . 24 VAL H H 8.196 . 1 243 . 24 VAL CA C 62.450 . 1 244 . 24 VAL HA H 4.123 . 1 245 . 24 VAL CB C 32.655 . 1 246 . 24 VAL HB H 2.077 . 1 247 . 24 VAL CG2 C 20.950 . 1 248 . 24 VAL HG2 H 0.947 . 2 249 . 24 VAL CG1 C 20.950 . 1 250 . 24 VAL HG1 H 0.974 . 2 251 . 24 VAL C C 176.223 . 1 252 . 25 VAL N N 125.334 . 1 253 . 25 VAL H H 8.393 . 1 254 . 25 VAL CA C 62.364 . 1 255 . 25 VAL HA H 4.194 . 1 256 . 25 VAL CB C 32.640 . 1 257 . 25 VAL HB H 2.074 . 1 258 . 25 VAL CG2 C 21.034 . 1 259 . 25 VAL HG2 H 0.961 . 1 260 . 25 VAL CG1 C 21.034 . 1 261 . 25 VAL HG1 H 0.961 . 1 262 . 25 VAL C C 176.342 . 1 263 . 26 THR N N 119.336 . 1 264 . 26 THR H H 8.258 . 1 265 . 26 THR CA C 61.483 . 1 266 . 26 THR HA H 4.320 . 1 267 . 26 THR CB C 69.826 . 1 268 . 26 THR HB H 4.212 . 1 269 . 26 THR CG2 C 21.623 . 1 270 . 26 THR HG2 H 1.205 . 1 271 . 26 THR C C 173.728 . 1 272 . 27 ALA N N 128.383 . 1 273 . 27 ALA H H 8.338 . 1 274 . 27 ALA CA C 50.500 . 1 275 . 27 ALA HA H 4.607 . 1 276 . 27 ALA CB C 18.103 . 1 277 . 27 ALA HB H 1.370 . 1 278 . 27 ALA C C 175.321 . 1 279 . 28 PRO CA C 62.856 . 1 280 . 28 PRO HA H 4.473 . 1 281 . 28 PRO CB C 32.015 . 1 282 . 28 PRO HB3 H 2.301 . 2 283 . 28 PRO HB2 H 1.908 . 2 284 . 28 PRO CG C 27.402 . 1 285 . 28 PRO HG3 H 2.032 . 1 286 . 28 PRO HG2 H 2.032 . 1 287 . 28 PRO CD C 50.490 . 1 288 . 28 PRO HD3 H 3.651 . 2 289 . 28 PRO HD2 H 3.811 . 2 290 . 28 PRO C C 176.996 . 1 291 . 29 VAL N N 120.712 . 1 292 . 29 VAL H H 8.322 . 1 293 . 29 VAL CA C 62.400 . 1 294 . 29 VAL HA H 4.125 . 1 295 . 29 VAL CB C 32.789 . 1 296 . 29 VAL HB H 2.078 . 1 297 . 29 VAL HG2 H 0.964 . 1 298 . 29 VAL HG1 H 0.964 . 1 299 . 29 VAL C C 176.411 . 1 300 . 30 SER N N 119.592 . 1 301 . 30 SER H H 8.467 . 1 302 . 30 SER CA C 57.983 . 1 303 . 30 SER HA H 4.540 . 1 304 . 30 SER CB C 64.000 . 1 305 . 30 SER HB3 H 3.924 . 1 306 . 30 SER HB2 H 3.924 . 1 307 . 30 SER C C 174.671 . 1 308 . 31 SER N N 118.902 . 1 309 . 31 SER H H 8.624 . 1 310 . 31 SER CA C 58.761 . 1 311 . 31 SER HA H 4.510 . 1 312 . 31 SER CB C 64.240 . 1 313 . 31 SER HB3 H 3.928 . 2 314 . 31 SER HB2 H 3.960 . 2 315 . 31 SER C C 175.173 . 1 316 . 32 GLY N N 111.041 . 1 317 . 32 GLY H H 8.554 . 1 318 . 32 GLY CA C 45.350 . 1 319 . 32 GLY HA3 H 4.000 . 1 320 . 32 GLY HA2 H 4.000 . 1 321 . 32 GLY C C 173.953 . 1 322 . 33 LYS N N 121.324 . 1 323 . 33 LYS H H 8.350 . 1 324 . 33 LYS CA C 56.134 . 1 325 . 33 LYS HA H 4.390 . 1 326 . 33 LYS CB C 33.078 . 1 327 . 33 LYS HB3 H 1.747 . 2 328 . 33 LYS HB2 H 1.810 . 2 329 . 33 LYS CG C 24.840 . 1 330 . 33 LYS HG3 H 1.434 . 1 331 . 33 LYS HG2 H 1.434 . 1 332 . 33 LYS CD C 29.136 . 1 333 . 33 LYS HD3 H 1.707 . 1 334 . 33 LYS HD2 H 1.707 . 1 335 . 33 LYS CE C 42.147 . 1 336 . 33 LYS HE3 H 3.011 . 1 337 . 33 LYS HE2 H 3.011 . 1 338 . 33 LYS C C 175.869 . 1 339 . 34 ILE N N 122.270 . 1 340 . 34 ILE H H 8.227 . 1 341 . 34 ILE CA C 59.622 . 1 342 . 34 ILE HA H 4.500 . 1 343 . 34 ILE CB C 39.556 . 1 344 . 34 ILE HB H 1.757 . 1 345 . 34 ILE CG1 C 27.164 . 2 346 . 34 ILE HG13 H 1.417 . 1 347 . 34 ILE HG12 H 1.203 . 1 348 . 34 ILE CD1 C 12.025 . 1 349 . 34 ILE HD1 H 0.737 . 1 350 . 34 ILE CG2 C 17.926 . 1 351 . 34 ILE HG2 H 0.714 . 1 352 . 34 ILE C C 175.715 . 1 353 . 35 LYS N N 128.204 . 1 354 . 35 LYS H H 9.421 . 1 355 . 35 LYS CA C 53.767 . 1 356 . 35 LYS HA H 4.533 . 1 357 . 35 LYS CB C 34.249 . 1 358 . 35 LYS HB3 H 1.474 . 1 359 . 35 LYS HB2 H 1.474 . 1 360 . 35 LYS CG C 24.014 . 1 361 . 35 LYS HG3 H 1.206 . 2 362 . 35 LYS HG2 H 0.960 . 2 363 . 35 LYS CD C 28.260 . 1 364 . 35 LYS HD3 H 1.528 . 2 365 . 35 LYS HD2 H 1.435 . 2 366 . 35 LYS CE C 41.910 . 1 367 . 35 LYS HE3 H 2.800 . 1 368 . 35 LYS HE2 H 2.800 . 1 369 . 35 LYS C C 174.468 . 1 370 . 36 ARG N N 125.839 . 1 371 . 36 ARG H H 8.454 . 1 372 . 36 ARG CA C 56.451 . 1 373 . 36 ARG HA H 4.601 . 1 374 . 36 ARG CB C 30.125 . 1 375 . 36 ARG HB3 H 1.819 . 1 376 . 36 ARG HB2 H 1.819 . 1 377 . 36 ARG CG C 27.510 . 1 378 . 36 ARG HG3 H 1.605 . 1 379 . 36 ARG HG2 H 1.605 . 1 380 . 36 ARG CD C 43.624 . 1 381 . 36 ARG HD3 H 3.189 . 2 382 . 36 ARG HD2 H 3.100 . 2 383 . 36 ARG C C 176.122 . 1 384 . 37 VAL N N 126.997 . 1 385 . 37 VAL H H 8.585 . 1 386 . 37 VAL CA C 61.224 . 1 387 . 37 VAL HA H 4.143 . 1 388 . 37 VAL CB C 34.440 . 1 389 . 37 VAL HB H 2.203 . 1 390 . 37 VAL CG2 C 21.048 . 1 391 . 37 VAL HG2 H 0.824 . 2 392 . 37 VAL CG1 C 22.055 . 1 393 . 37 VAL HG1 H 0.662 . 2 394 . 37 VAL C C 173.834 . 1 395 . 38 ASN N N 124.221 . 1 396 . 38 ASN H H 8.464 . 1 397 . 38 ASN CA C 53.651 . 1 398 . 38 ASN HA H 5.102 . 1 399 . 38 ASN CB C 40.560 . 1 400 . 38 ASN HB3 H 2.460 . 1 401 . 38 ASN HB2 H 2.460 . 1 402 . 38 ASN ND2 N 112.571 . 1 403 . 38 ASN HD21 H 7.281 . 2 404 . 38 ASN HD22 H 6.619 . 2 405 . 38 ASN C C 174.595 . 1 406 . 39 VAL N N 125.145 . 1 407 . 39 VAL H H 9.190 . 1 408 . 39 VAL CA C 61.204 . 1 409 . 39 VAL HA H 3.979 . 1 410 . 39 VAL CB C 34.560 . 1 411 . 39 VAL HB H 1.805 . 1 412 . 39 VAL CG2 C 20.975 . 1 413 . 39 VAL HG2 H 0.772 . 2 414 . 39 VAL CG1 C 21.964 . 1 415 . 39 VAL HG1 H 0.473 . 2 416 . 39 VAL C C 174.004 . 1 417 . 40 ASN N N 123.527 . 1 418 . 40 ASN H H 7.713 . 1 419 . 40 ASN CA C 52.374 . 1 420 . 40 ASN HA H 5.174 . 1 421 . 40 ASN CB C 39.042 . 1 422 . 40 ASN HB3 H 2.589 . 2 423 . 40 ASN HB2 H 2.329 . 2 424 . 40 ASN ND2 N 111.766 . 1 425 . 40 ASN HD21 H 7.405 . 2 426 . 40 ASN HD22 H 6.700 . 2 427 . 40 ASN C C 174.954 . 1 428 . 41 PHE N N 122.140 . 1 429 . 41 PHE H H 9.067 . 1 430 . 41 PHE CA C 55.900 . 1 431 . 41 PHE HA H 5.118 . 1 432 . 41 PHE CB C 43.980 . 1 433 . 41 PHE HB3 H 2.814 . 2 434 . 41 PHE HB2 H 3.259 . 2 435 . 41 PHE CD1 C 129.853 . 3 436 . 41 PHE HD1 H 7.327 . 3 437 . 41 PHE CE1 C 129.880 . 3 438 . 41 PHE HE1 H 6.953 . 3 439 . 41 PHE CZ C 128.161 . 1 440 . 41 PHE HZ H 6.883 . 1 441 . 41 PHE C C 175.342 . 1 442 . 42 ASP N N 122.602 . 1 443 . 42 ASP H H 9.210 . 1 444 . 42 ASP CA C 55.013 . 1 445 . 42 ASP HA H 4.810 . 1 446 . 42 ASP CB C 42.511 . 1 447 . 42 ASP HB3 H 2.734 . 2 448 . 42 ASP HB2 H 2.850 . 2 449 . 42 ASP C C 177.511 . 1 450 . 43 GLU N N 125.826 . 1 451 . 43 GLU H H 8.814 . 1 452 . 43 GLU CA C 61.000 . 1 453 . 43 GLU HA H 3.885 . 1 454 . 43 GLU CB C 30.191 . 1 455 . 43 GLU HB3 H 2.100 . 1 456 . 43 GLU HB2 H 2.100 . 1 457 . 43 GLU CG C 36.183 . 1 458 . 43 GLU HG3 H 2.301 . 1 459 . 43 GLU HG2 H 2.301 . 1 460 . 43 GLU C C 177.918 . 1 461 . 44 GLU N N 119.468 . 1 462 . 44 GLU H H 8.706 . 1 463 . 44 GLU CA C 59.784 . 1 464 . 44 GLU HA H 4.184 . 1 465 . 44 GLU CB C 28.768 . 1 466 . 44 GLU HB3 H 2.160 . 1 467 . 44 GLU HB2 H 2.160 . 1 468 . 44 GLU CG C 32.838 . 1 469 . 44 GLU HG3 H 2.393 . 1 470 . 44 GLU HG2 H 2.393 . 1 471 . 44 GLU C C 178.928 . 1 472 . 45 LYS N N 121.508 . 1 473 . 45 LYS H H 7.913 . 1 474 . 45 LYS CA C 59.692 . 1 475 . 45 LYS HA H 3.960 . 1 476 . 45 LYS CB C 32.150 . 1 477 . 45 LYS HB3 H 2.014 . 1 478 . 45 LYS HB2 H 2.014 . 1 479 . 45 LYS CG C 25.307 . 1 480 . 45 LYS HG3 H 1.434 . 1 481 . 45 LYS HG2 H 1.434 . 1 482 . 45 LYS CD C 29.270 . 1 483 . 45 LYS HD3 H 1.822 . 1 484 . 45 LYS HD2 H 1.822 . 1 485 . 45 LYS CE C 41.603 . 1 486 . 45 LYS HE3 H 3.164 . 2 487 . 45 LYS HE2 H 2.891 . 2 488 . 45 LYS C C 178.494 . 1 489 . 46 HIS N N 118.534 . 1 490 . 46 HIS H H 8.839 . 1 491 . 46 HIS CA C 61.503 . 1 492 . 46 HIS HA H 3.863 . 1 493 . 46 HIS CB C 30.100 . 1 494 . 46 HIS HB3 H 3.350 . 2 495 . 46 HIS HB2 H 2.975 . 2 496 . 46 HIS CD2 C 119.770 . 1 497 . 46 HIS HD2 H 6.326 . 1 498 . 46 HIS CE1 C 138.031 . 1 499 . 46 HIS HE1 H 7.705 . 1 500 . 46 HIS C C 176.505 . 1 501 . 47 THR N N 116.759 . 1 502 . 47 THR H H 8.707 . 1 503 . 47 THR CA C 67.006 . 1 504 . 47 THR HA H 3.654 . 1 505 . 47 THR CB C 68.788 . 1 506 . 47 THR HB H 4.428 . 1 507 . 47 THR CG2 C 21.676 . 1 508 . 47 THR HG2 H 1.298 . 1 509 . 47 THR C C 177.172 . 1 510 . 48 ARG N N 120.998 . 1 511 . 48 ARG H H 8.028 . 1 512 . 48 ARG CA C 59.369 . 1 513 . 48 ARG HA H 4.156 . 1 514 . 48 ARG CB C 31.483 . 1 515 . 48 ARG HB3 H 2.120 . 2 516 . 48 ARG HB2 H 1.927 . 2 517 . 48 ARG CG C 28.488 . 1 518 . 48 ARG HG3 H 1.923 . 2 519 . 48 ARG HG2 H 1.660 . 2 520 . 48 ARG CD C 44.056 . 1 521 . 48 ARG HD3 H 3.267 . 2 522 . 48 ARG HD2 H 3.388 . 2 523 . 48 ARG NE N 86.820 . 1 524 . 48 ARG HE H 7.465 . 1 525 . 48 ARG C C 179.594 . 1 526 . 49 PHE N N 121.996 . 1 527 . 49 PHE H H 9.059 . 1 528 . 49 PHE CA C 57.684 . 1 529 . 49 PHE HA H 4.888 . 1 530 . 49 PHE CB C 38.987 . 1 531 . 49 PHE HB3 H 3.242 . 2 532 . 49 PHE HB2 H 3.097 . 2 533 . 49 PHE CD1 C 129.994 . 3 534 . 49 PHE HD1 H 6.958 . 3 535 . 49 PHE CE1 C 131.827 . 3 536 . 49 PHE HE1 H 6.508 . 3 537 . 49 PHE CZ C 128.443 . 1 538 . 49 PHE HZ H 6.616 . 1 539 . 49 PHE C C 177.299 . 1 540 . 50 LYS N N 120.654 . 1 541 . 50 LYS H H 9.058 . 1 542 . 50 LYS CA C 60.301 . 1 543 . 50 LYS HA H 3.442 . 1 544 . 50 LYS CB C 32.354 . 1 545 . 50 LYS HB3 H 1.663 . 2 546 . 50 LYS HB2 H 1.394 . 2 547 . 50 LYS CG C 24.840 . 1 548 . 50 LYS HG3 H 1.260 . 1 549 . 50 LYS HG2 H 1.260 . 1 550 . 50 LYS CD C 29.777 . 1 551 . 50 LYS HD3 H 1.553 . 1 552 . 50 LYS HD2 H 1.553 . 1 553 . 50 LYS CE C 41.683 . 1 554 . 50 LYS HE3 H 2.946 . 2 555 . 50 LYS HE2 H 2.859 . 2 556 . 50 LYS C C 179.391 . 1 557 . 51 ALA N N 120.653 . 1 558 . 51 ALA H H 7.802 . 1 559 . 51 ALA CA C 55.162 . 1 560 . 51 ALA HA H 4.218 . 1 561 . 51 ALA CB C 18.066 . 1 562 . 51 ALA HB H 1.553 . 1 563 . 51 ALA C C 180.244 . 1 564 . 52 ALA N N 121.499 . 1 565 . 52 ALA H H 8.264 . 1 566 . 52 ALA CA C 55.185 . 1 567 . 52 ALA HA H 4.310 . 1 568 . 52 ALA CB C 19.540 . 1 569 . 52 ALA HB H 1.815 . 1 570 . 52 ALA C C 180.696 . 1 571 . 53 CYS N N 115.800 . 1 572 . 53 CYS H H 8.436 . 1 573 . 53 CYS CA C 64.871 . 1 574 . 53 CYS HA H 3.977 . 1 575 . 53 CYS CB C 26.027 . 1 576 . 53 CYS HB3 H 2.796 . 2 577 . 53 CYS HB2 H 2.247 . 2 578 . 53 CYS C C 177.059 . 1 579 . 54 ALA N N 122.148 . 1 580 . 54 ALA H H 7.894 . 1 581 . 54 ALA CA C 55.260 . 1 582 . 54 ALA HA H 4.230 . 1 583 . 54 ALA CB C 17.584 . 1 584 . 54 ALA HB H 1.533 . 1 585 . 54 ALA C C 181.783 . 1 586 . 55 ARG N N 118.921 . 1 587 . 55 ARG H H 7.998 . 1 588 . 55 ARG CA C 59.472 . 1 589 . 55 ARG HA H 4.146 . 1 590 . 55 ARG CB C 30.670 . 1 591 . 55 ARG HB3 H 2.124 . 2 592 . 55 ARG HB2 H 1.948 . 2 593 . 55 ARG CG C 28.477 . 1 594 . 55 ARG HG3 H 1.925 . 1 595 . 55 ARG HG2 H 1.925 . 1 596 . 55 ARG CD C 43.980 . 1 597 . 55 ARG HD3 H 3.395 . 2 598 . 55 ARG HD2 H 3.270 . 2 599 . 55 ARG C C 178.283 . 1 600 . 56 LYS N N 115.992 . 1 601 . 56 LYS H H 7.529 . 1 602 . 56 LYS CA C 55.416 . 1 603 . 56 LYS HA H 4.421 . 1 604 . 56 LYS CB C 32.930 . 1 605 . 56 LYS HB3 H 1.926 . 2 606 . 56 LYS HB2 H 2.256 . 2 607 . 56 LYS HG3 H 1.695 . 4 608 . 56 LYS HG2 H 1.695 . 4 609 . 56 LYS HE3 H 2.764 . 4 610 . 56 LYS C C 176.726 . 1 611 . 57 GLY N N 109.148 . 1 612 . 57 GLY H H 7.895 . 1 613 . 57 GLY CA C 46.772 . 1 614 . 57 GLY HA3 H 3.970 . 2 615 . 57 GLY HA2 H 4.026 . 2 616 . 57 GLY C C 174.250 . 1 617 . 58 THR N N 114.972 . 1 618 . 58 THR H H 8.039 . 1 619 . 58 THR CA C 57.825 . 1 620 . 58 THR HA H 4.964 . 1 621 . 58 THR CB C 70.264 . 1 622 . 58 THR HB H 3.971 . 1 623 . 58 THR CG2 C 19.313 . 1 624 . 58 THR HG2 H 1.182 . 1 625 . 58 THR C C 171.954 . 1 626 . 59 SER N N 116.821 . 1 627 . 59 SER H H 8.863 . 1 628 . 59 SER CA C 55.787 . 1 629 . 59 SER HA H 4.728 . 1 630 . 59 SER CB C 67.336 . 1 631 . 59 SER HB3 H 4.107 . 1 632 . 59 SER HB2 H 4.107 . 1 633 . 59 SER C C 173.216 . 1 634 . 60 ILE N N 122.833 . 1 635 . 60 ILE H H 8.725 . 1 636 . 60 ILE CA C 65.710 . 1 637 . 60 ILE HA H 3.141 . 1 638 . 60 ILE CB C 37.566 . 1 639 . 60 ILE HB H 1.637 . 1 640 . 60 ILE CG1 C 28.328 . 2 641 . 60 ILE HG13 H 1.276 . 1 642 . 60 ILE HG12 H -0.244 . 1 643 . 60 ILE CD1 C 13.658 . 1 644 . 60 ILE HD1 H 0.511 . 1 645 . 60 ILE CG2 C 15.754 . 1 646 . 60 ILE HG2 H 0.628 . 1 647 . 60 ILE C C 177.894 . 1 648 . 61 THR N N 114.363 . 1 649 . 61 THR H H 8.269 . 1 650 . 61 THR CA C 67.117 . 1 651 . 61 THR HA H 3.830 . 1 652 . 61 THR CB C 69.115 . 1 653 . 61 THR HB H 4.080 . 1 654 . 61 THR CG2 C 21.639 . 1 655 . 61 THR HG2 H 1.263 . 1 656 . 61 THR C C 176.393 . 1 657 . 62 ASP N N 124.224 . 1 658 . 62 ASP H H 7.661 . 1 659 . 62 ASP CA C 57.847 . 1 660 . 62 ASP HA H 4.421 . 1 661 . 62 ASP CB C 39.967 . 1 662 . 62 ASP HB3 H 2.588 . 2 663 . 62 ASP HB2 H 2.670 . 2 664 . 62 ASP C C 178.829 . 1 665 . 63 VAL N N 121.934 . 1 666 . 63 VAL H H 8.228 . 1 667 . 63 VAL CA C 67.000 . 1 668 . 63 VAL HA H 3.518 . 1 669 . 63 VAL CB C 31.635 . 1 670 . 63 VAL HB H 1.643 . 1 671 . 63 VAL CG2 C 24.732 . 1 672 . 63 VAL HG2 H 0.831 . 2 673 . 63 VAL CG1 C 19.178 . 1 674 . 63 VAL HG1 H -0.199 . 2 675 . 63 VAL C C 178.290 . 1 676 . 64 VAL N N 117.338 . 1 677 . 64 VAL H H 8.942 . 1 678 . 64 VAL CA C 68.067 . 1 679 . 64 VAL HA H 3.391 . 1 680 . 64 VAL CB C 30.959 . 1 681 . 64 VAL HB H 2.108 . 1 682 . 64 VAL CG2 C 24.012 . 1 683 . 64 VAL HG2 H 1.140 . 2 684 . 64 VAL CG1 C 23.097 . 1 685 . 64 VAL HG1 H 0.953 . 2 686 . 64 VAL C C 177.555 . 1 687 . 65 ASN N N 116.330 . 1 688 . 65 ASN H H 7.909 . 1 689 . 65 ASN CA C 59.176 . 1 690 . 65 ASN HA H 3.904 . 1 691 . 65 ASN CB C 39.679 . 1 692 . 65 ASN HB3 H 2.971 . 2 693 . 65 ASN HB2 H 2.663 . 2 694 . 65 ASN ND2 N 113.008 . 1 695 . 65 ASN HD21 H 7.429 . 2 696 . 65 ASN C C 176.756 . 1 697 . 66 GLN N N 119.834 . 1 698 . 66 GLN H H 7.785 . 1 699 . 66 GLN CA C 59.388 . 1 700 . 66 GLN HA H 4.152 . 1 701 . 66 GLN CB C 28.619 . 1 702 . 66 GLN HB3 H 2.243 . 1 703 . 66 GLN HB2 H 2.243 . 1 704 . 66 GLN CG C 33.989 . 1 705 . 66 GLN HG3 H 2.430 . 2 706 . 66 GLN HG2 H 2.574 . 2 707 . 66 GLN NE2 N 111.650 . 1 708 . 66 GLN HE21 H 7.437 . 2 709 . 66 GLN HE22 H 6.928 . 2 710 . 66 GLN C C 178.694 . 1 711 . 67 LEU N N 119.360 . 1 712 . 67 LEU H H 8.571 . 1 713 . 67 LEU CA C 57.690 . 1 714 . 67 LEU HA H 4.168 . 1 715 . 67 LEU CB C 41.651 . 1 716 . 67 LEU HB3 H 1.914 . 1 717 . 67 LEU HB2 H 1.914 . 1 718 . 67 LEU CG C 25.973 . 1 719 . 67 LEU HG H 2.009 . 1 720 . 67 LEU CD1 C 25.667 . 1 721 . 67 LEU HD1 H 0.562 . 2 722 . 67 LEU CD2 C 21.911 . 1 723 . 67 LEU HD2 H 1.075 . 2 724 . 67 LEU C C 180.425 . 1 725 . 68 VAL N N 120.766 . 1 726 . 68 VAL H H 8.664 . 1 727 . 68 VAL CA C 66.812 . 1 728 . 68 VAL HA H 3.289 . 1 729 . 68 VAL CB C 31.246 . 1 730 . 68 VAL HB H 1.935 . 1 731 . 68 VAL CG2 C 24.480 . 1 732 . 68 VAL HG2 H 0.610 . 2 733 . 68 VAL CG1 C 19.347 . 1 734 . 68 VAL HG1 H 0.053 . 2 735 . 68 VAL C C 177.110 . 1 736 . 69 ASP N N 121.510 . 1 737 . 69 ASP H H 8.179 . 1 738 . 69 ASP CA C 58.148 . 1 739 . 69 ASP HA H 4.374 . 1 740 . 69 ASP CB C 39.831 . 1 741 . 69 ASP HB3 H 2.961 . 2 742 . 69 ASP HB2 H 2.669 . 2 743 . 69 ASP C C 179.614 . 1 744 . 70 ASN N N 117.969 . 1 745 . 70 ASN H H 7.708 . 1 746 . 70 ASN CA C 56.275 . 1 747 . 70 ASN HA H 4.486 . 1 748 . 70 ASN CB C 38.195 . 1 749 . 70 ASN HB3 H 3.064 . 2 750 . 70 ASN HB2 H 3.085 . 2 751 . 70 ASN ND2 N 112.353 . 1 752 . 70 ASN HD21 H 7.806 . 2 753 . 70 ASN HD22 H 7.098 . 2 754 . 70 ASN C C 177.122 . 1 755 . 71 TRP N N 123.521 . 1 756 . 71 TRP H H 8.511 . 1 757 . 71 TRP CA C 62.584 . 1 758 . 71 TRP HA H 4.182 . 1 759 . 71 TRP CB C 29.859 . 1 760 . 71 TRP HB3 H 3.311 . 1 761 . 71 TRP HB2 H 3.311 . 1 762 . 71 TRP CD1 C 128.090 . 1 763 . 71 TRP HD1 H 7.397 . 1 764 . 71 TRP NE1 N 132.162 . 1 765 . 71 TRP HE1 H 10.500 . 1 766 . 71 TRP CZ2 C 114.700 . 1 767 . 71 TRP HZ2 H 7.304 . 1 768 . 71 TRP CH2 C 123.720 . 1 769 . 71 TRP HH2 H 6.801 . 1 770 . 71 TRP CZ3 C 120.970 . 1 771 . 71 TRP HZ3 H 7.122 . 1 772 . 71 TRP CE3 C 118.997 . 1 773 . 71 TRP HE3 H 7.262 . 1 774 . 71 TRP C C 180.493 . 1 775 . 72 LEU N N 120.827 . 1 776 . 72 LEU H H 9.431 . 1 777 . 72 LEU CA C 58.232 . 1 778 . 72 LEU HA H 3.865 . 1 779 . 72 LEU CB C 41.552 . 1 780 . 72 LEU HB3 H 2.082 . 2 781 . 72 LEU HB2 H 1.577 . 2 782 . 72 LEU CG C 27.105 . 1 783 . 72 LEU HG H 1.996 . 1 784 . 72 LEU CD1 C 23.654 . 1 785 . 72 LEU HD1 H 1.057 . 2 786 . 72 LEU CD2 C 26.062 . 1 787 . 72 LEU HD2 H 0.873 . 2 788 . 72 LEU C C 178.655 . 1 789 . 73 LYS N N 117.495 . 1 790 . 73 LYS H H 7.454 . 1 791 . 73 LYS CA C 59.355 . 1 792 . 73 LYS HA H 4.045 . 1 793 . 73 LYS CB C 32.220 . 1 794 . 73 LYS HB3 H 1.960 . 1 795 . 73 LYS HB2 H 1.960 . 1 796 . 73 LYS CG C 24.947 . 1 797 . 73 LYS HG3 H 1.508 . 2 798 . 73 LYS HG2 H 1.669 . 2 799 . 73 LYS CD C 29.460 . 1 800 . 73 LYS HD3 H 1.765 . 1 801 . 73 LYS HD2 H 1.765 . 1 802 . 73 LYS C C 178.562 . 1 803 . 74 GLU N N 114.271 . 1 804 . 74 GLU H H 7.100 . 1 805 . 74 GLU CA C 56.866 . 1 806 . 74 GLU HA H 4.260 . 1 807 . 74 GLU CB C 31.173 . 1 808 . 74 GLU HB3 H 1.867 . 2 809 . 74 GLU HB2 H 1.771 . 2 810 . 74 GLU CG C 36.147 . 1 811 . 74 GLU HG3 H 2.274 . 1 812 . 74 GLU HG2 H 2.274 . 1 813 . 74 GLU C C 177.240 . 1 814 . 75 ASN N N 115.509 . 1 815 . 75 ASN H H 7.487 . 1 816 . 75 ASN CA C 54.212 . 1 817 . 75 ASN HA H 4.543 . 1 818 . 75 ASN CB C 40.292 . 1 819 . 75 ASN HB3 H 1.711 . 2 820 . 75 ASN HB2 H 0.796 . 2 821 . 75 ASN ND2 N 116.455 . 1 822 . 75 ASN HD21 H 6.711 . 2 823 . 75 ASN HD22 H 6.048 . 2 824 . 75 ASN C C 173.547 . 1 825 . 76 GLU N N 126.070 . 1 826 . 76 GLU H H 7.947 . 1 827 . 76 GLU CA C 59.908 . 1 828 . 76 GLU HA H 3.889 . 1 829 . 76 GLU CB C 30.519 . 1 830 . 76 GLU HB3 H 2.012 . 1 831 . 76 GLU HB2 H 2.012 . 1 832 . 76 GLU CG C 37.115 . 1 833 . 76 GLU HG3 H 2.301 . 1 834 . 76 GLU HG2 H 2.301 . 1 835 . 76 GLU C C 181.073 . 1 stop_ loop_ _Atom_shift_assign_ID_ambiguity 56 '607,608,609' stop_ save_