data_15784 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; 1H, 13C, and 15N Chemical Shift Assignments for NikA(1-51) ; _BMRB_accession_number 15784 _BMRB_flat_file_name bmr15784.str _Entry_type original _Submission_date 2008-05-28 _Accession_date 2008-05-28 _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 Yoshida Hitoshi . . 2 Furuya Nobuhisa . . 3 Lin Yi-Jan . . 4 Guntert Peter . . 5 Komano Teruya . . 6 Kainosho Masatsune . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 254 "13C chemical shifts" 201 "15N chemical shifts" 51 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2008-11-25 original author . stop_ _Original_release_date 2008-11-25 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title 'Structural basis of the role of the NikA ribbon-helix-helix domain in initiating bacterial conjugation.' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 18929573 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Yoshida Hitoshi . . 2 Furuya Nobuhisa . . 3 Lin Yi-Jan . . 4 Guntert Peter . . 5 Komano Teruya . . 6 Kainosho Masatsune . . stop_ _Journal_abbreviation 'J. Mol. Biol.' _Journal_volume 384 _Journal_issue 3 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 690 _Page_last 701 _Year 2008 _Details . loop_ _Keyword 'bacterial conjugation' homodimer NMR relaxosome 'ribbon-helix-helix fold' stop_ save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name 'NikA(1-51) homodimer' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label NikA(1-51) $NikA(1-51) stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state ? _System_paramagnetic no _System_thiol_state . _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_NikA(1-51) _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common NikA(1-51) _Molecular_mass . _Mol_thiol_state 'not present' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 51 _Mol_residue_sequence ; SDSAVRKKSEVRQKTVVRTL RFSPVEDETIRKKAEDSGLT VSAYIRNAALN ; loop_ _Residue_seq_code _Residue_label 1 SER 2 ASP 3 SER 4 ALA 5 VAL 6 ARG 7 LYS 8 LYS 9 SER 10 GLU 11 VAL 12 ARG 13 GLN 14 LYS 15 THR 16 VAL 17 VAL 18 ARG 19 THR 20 LEU 21 ARG 22 PHE 23 SER 24 PRO 25 VAL 26 GLU 27 ASP 28 GLU 29 THR 30 ILE 31 ARG 32 LYS 33 LYS 34 ALA 35 GLU 36 ASP 37 SER 38 GLY 39 LEU 40 THR 41 VAL 42 SER 43 ALA 44 TYR 45 ILE 46 ARG 47 ASN 48 ALA 49 ALA 50 LEU 51 ASN stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-09-09 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 2BA3 "Nmr Structure Of Nika N-Terminal Fragment" 100.00 51 100.00 100.00 5.11e-26 DBJ BAA75139 "relaxosome component [Shigella sonnei]" 100.00 110 100.00 100.00 8.79e-26 DBJ BAA78022 "nikA [Plasmid R64]" 100.00 110 100.00 100.00 8.79e-26 DBJ BAB91643 "NikA oriT-specific DNA binding protein [Salmonella enterica subsp. enterica serovar Typhimurium]" 100.00 110 100.00 100.00 8.79e-26 DBJ BAG80276 "relaxosome component NikA [Escherichia coli SE11]" 100.00 110 100.00 100.00 8.79e-26 DBJ BAK64475 "NikA oriT-specific DNA-binding protein [Salmonella enterica subsp. enterica serovar Typhimurium]" 100.00 110 100.00 100.00 8.79e-26 EMBL CBL93594 "relaxosome product NikA protein [Escherichia coli ETEC 1392/75]" 100.00 110 100.00 100.00 8.79e-26 EMBL CCE57555 "ribbon-helix-helix protein, copG family protein [Escherichia coli]" 100.00 110 100.00 100.00 8.79e-26 EMBL CCQ26867 "plasmid mobilization protein [Shigella sonnei]" 100.00 110 100.00 100.00 8.79e-26 EMBL CDH80849 "NikA oriT-specific DNA binding protein [Salmonella enterica subsp. enterica serovar Typhimurium str. STM709]" 100.00 110 100.00 100.00 8.79e-26 EMBL CDO67566 "relaxosome component NikA [Escherichia coli]" 100.00 110 100.00 100.00 8.79e-26 GB AAS76382 "relaxosome component [Salmonella enterica subsp. enterica serovar Choleraesuis str. SC-B67]" 100.00 110 100.00 100.00 8.79e-26 GB AAZ05364 "NikA [Salmonella enterica]" 100.00 110 100.00 100.00 8.79e-26 GB ACF56917 "relaxosome component [Salmonella enterica subsp. enterica serovar Kentucky str. CVM29188]" 100.00 110 100.00 100.00 8.79e-26 GB ACF65722 "relaxosome component [Salmonella enterica subsp. enterica serovar Heidelberg str. SL476]" 100.00 126 100.00 100.00 2.15e-25 GB ACQ42156 "plasmid mobilization protein [Escherichia coli]" 100.00 110 100.00 100.00 8.79e-26 REF NP_052500 "relaxosome component [Shigella sonnei]" 100.00 110 100.00 100.00 8.79e-26 REF NP_863435 "hypothetical protein R64_p080 (plasmid) [Salmonella enterica subsp. enterica serovar Typhimurium]" 100.00 110 100.00 100.00 8.79e-26 REF WP_000325007 "hypothetical protein, partial [Escherichia coli]" 80.39 99 100.00 100.00 4.77e-19 REF WP_001283946 "hypothetical protein [Escherichia coli]" 100.00 110 98.04 100.00 3.57e-25 REF WP_001283947 "MULTISPECIES: hypothetical protein [Enterobacteriaceae]" 100.00 110 100.00 100.00 8.79e-26 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species _Strain $NikA(1-51) 'R64 plasmid' 602 Bacteria . Salmonella typhimurium 'R64 plasmid' 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 $NikA(1-51) 'recombinant technology' . Escherichia coli 'BL21 (DE3) Star' pNikA 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 $NikA(1-51) 2 mM '[U-13C; U-15N]' 'phosphate buffer' 50 mM 'natural abundance' 'sodium chloride' 50 mM 'natural abundance' 'sodium azide' 0.02% w/v 'natural abundance' H2O 90 % 'natural abundance' D2O 10 % . stop_ save_ ############################ # Computer software used # ############################ save_NMRPipe _Saveframe_category software _Name NMRPipe _Version . loop_ _Vendor _Address _Electronic_address 'Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax' . . stop_ loop_ _Task processing stop_ _Details . save_ save_NMRView _Saveframe_category software _Name NMRView _Version . loop_ _Vendor _Address _Electronic_address 'Johnson, One Moon Scientific' . . stop_ loop_ _Task 'chemical shift assignment' 'peak picking' stop_ _Details . save_ save_SPARKY _Saveframe_category software _Name SPARKY _Version . loop_ _Vendor _Address _Electronic_address Goddard . . stop_ loop_ _Task 'chemical shift assignment' 'peak picking' stop_ _Details . save_ save_CYANA _Saveframe_category software _Name CYANA _Version . loop_ _Vendor _Address _Electronic_address Guntert . . stop_ loop_ _Task 'structure solution' stop_ _Details . save_ save_OPALp _Saveframe_category software _Name OPALp _Version . loop_ _Vendor _Address _Electronic_address 'Koradi, Billeter, Guntert' . . stop_ loop_ _Task refinement stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model AV _Field_strength 500 _Details . save_ save_spectrometer_2 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model DRX _Field_strength 600 _Details . save_ ############################# # NMR applied experiments # ############################# save_triple_resonance_1 _Saveframe_category NMR_applied_experiment _Experiment_name 'triple resonance' _Sample_label $sample_1 save_ ####################### # Sample conditions # ####################### save_sample_conditions_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units 'ionic strength' 0.05 . M pH 6.8 . pH pressure 1 . atm temperature 298 . K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference_1 _Saveframe_category chemical_shift_reference _Details . loop_ _Mol_common_name _Atom_type _Atom_isotope_number _Atom_group _Chem_shift_units _Chem_shift_value _Reference_method _Reference_type _External_reference_sample_geometry _External_reference_location _External_reference_axis _Indirect_shift_ratio DSS C 13 'methyl protons' ppm 0.00 . indirect . . . 0.251449530 DSS H 1 'methyl protons' ppm 0.00 internal direct . . . 1.000000000 DSS N 15 'methyl protons' ppm 0.00 . indirect . . . 0.101329118 stop_ save_ ################################### # Assigned chemical shift lists # ################################### ################################################################### # Chemical Shift Ambiguity Index Value Definitions # # # # The values other than 1 are used for those atoms with different # # chemical shifts that cannot be assigned to stereospecific atoms # # or to specific residues or chains. # # # # Index Value Definition # # # # 1 Unique (including isolated methyl protons, # # geminal atoms, and geminal methyl # # groups with identical chemical shifts) # # (e.g. ILE HD11, HD12, HD13 protons) # # 2 Ambiguity of geminal atoms or geminal methyl # # proton groups (e.g. ASP HB2 and HB3 # # protons, LEU CD1 and CD2 carbons, or # # LEU HD11, HD12, HD13 and HD21, HD22, # # HD23 methyl protons) # # 3 Aromatic atoms on opposite sides of # # symmetrical rings (e.g. TYR HE1 and HE2 # # protons) # # 4 Intraresidue ambiguities (e.g. LYS HG and # # HD protons or TRP HZ2 and HZ3 protons) # # 5 Interresidue ambiguities (LYS 12 vs. LYS 27) # # 6 Intermolecular ambiguities (e.g. ASP 31 CA # # in monomer 1 and ASP 31 CA in monomer 2 # # of an asymmetrical homodimer, duplex # # DNA assignments, or other assignments # # that may apply to atoms in one or more # # molecule in the molecular assembly) # # 9 Ambiguous, specific ambiguity not defined # # # ################################################################### save_assigned_chem_shift_list_1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Experiment_label 'triple resonance' stop_ loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $sample_conditions_1 _Chem_shift_reference_set_label $chemical_shift_reference_1 _Mol_system_component_name NikA(1-51) _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 1 SER HA H 4.041 0.020 1 2 1 1 SER HB2 H 3.634 0.020 2 3 1 1 SER HB3 H 3.839 0.020 2 4 1 1 SER CA C 59.841 0.400 1 5 1 1 SER CB C 65.150 0.400 1 6 2 2 ASP HA H 4.569 0.020 1 7 2 2 ASP HB2 H 2.599 0.020 2 8 2 2 ASP HB3 H 2.528 0.020 2 9 2 2 ASP C C 176.530 0.400 1 10 2 2 ASP CA C 54.589 0.400 1 11 2 2 ASP CB C 41.462 0.400 1 12 3 3 SER H H 8.267 0.020 1 13 3 3 SER HA H 4.276 0.020 1 14 3 3 SER HB2 H 3.726 0.020 1 15 3 3 SER HB3 H 3.726 0.020 1 16 3 3 SER C C 174.667 0.400 1 17 3 3 SER CA C 58.605 0.400 1 18 3 3 SER CB C 63.763 0.400 1 19 3 3 SER N N 116.529 0.400 1 20 4 4 ALA H H 8.196 0.020 1 21 4 4 ALA HA H 4.179 0.020 1 22 4 4 ALA HB H 1.265 0.020 1 23 4 4 ALA C C 178.021 0.400 1 24 4 4 ALA CA C 52.977 0.400 1 25 4 4 ALA CB C 19.202 0.400 1 26 4 4 ALA N N 125.751 0.400 1 27 5 5 VAL H H 7.811 0.020 1 28 5 5 VAL HA H 3.912 0.020 1 29 5 5 VAL HB H 1.929 0.020 1 30 5 5 VAL HG1 H 0.787 0.020 1 31 5 5 VAL HG2 H 0.787 0.020 1 32 5 5 VAL C C 176.344 0.400 1 33 5 5 VAL CA C 62.506 0.400 1 34 5 5 VAL CB C 32.588 0.400 1 35 5 5 VAL CG1 C 21.198 0.400 1 36 5 5 VAL CG2 C 21.198 0.400 1 37 5 5 VAL N N 118.872 0.400 1 38 6 6 ARG H H 8.146 0.020 1 39 6 6 ARG HA H 4.195 0.020 1 40 6 6 ARG HB2 H 1.695 0.020 2 41 6 6 ARG HB3 H 1.630 0.020 2 42 6 6 ARG HD2 H 3.061 0.020 1 43 6 6 ARG HD3 H 3.061 0.020 1 44 6 6 ARG C C 176.344 0.400 1 45 6 6 ARG CA C 56.173 0.400 1 46 6 6 ARG CB C 30.859 0.400 1 47 6 6 ARG CD C 43.369 0.400 1 48 6 6 ARG N N 124.824 0.400 1 49 7 7 LYS H H 8.207 0.020 1 50 7 7 LYS C C 176.792 0.400 1 51 7 7 LYS N N 123.109 0.400 1 52 8 8 LYS H H 8.258 0.020 1 53 8 8 LYS C C 176.903 0.400 1 54 8 8 LYS N N 122.855 0.400 1 55 9 9 SER H H 8.197 0.020 1 56 9 9 SER HA H 4.243 0.020 1 57 9 9 SER HB2 H 3.726 0.020 1 58 9 9 SER HB3 H 3.726 0.020 1 59 9 9 SER C C 174.667 0.400 1 60 9 9 SER CA C 58.831 0.400 1 61 9 9 SER CB C 63.763 0.400 1 62 9 9 SER N N 116.772 0.400 1 63 10 10 GLU H H 8.280 0.020 1 64 10 10 GLU HA H 4.201 0.020 1 65 10 10 GLU HB2 H 1.917 0.020 2 66 10 10 GLU HB3 H 1.806 0.020 2 67 10 10 GLU C C 176.530 0.400 1 68 10 10 GLU CA C 56.610 0.400 1 69 10 10 GLU CB C 30.511 0.400 1 70 10 10 GLU N N 123.218 0.400 1 71 11 11 VAL H H 8.032 0.020 1 72 11 11 VAL HA H 3.888 0.020 1 73 11 11 VAL HB H 1.941 0.020 1 74 11 11 VAL HG1 H 0.822 0.020 1 75 11 11 VAL HG2 H 0.822 0.020 1 76 11 11 VAL C C 176.344 0.400 1 77 11 11 VAL CA C 62.778 0.400 1 78 11 11 VAL CB C 32.229 0.400 1 79 11 11 VAL CG1 C 20.838 0.400 1 80 11 11 VAL CG2 C 20.838 0.400 1 81 11 11 VAL N N 121.505 0.400 1 82 12 12 ARG H H 8.269 0.020 1 83 12 12 ARG HA H 4.195 0.020 1 84 12 12 ARG HB2 H 1.695 0.020 2 85 12 12 ARG HB3 H 1.630 0.020 2 86 12 12 ARG HD2 H 3.061 0.020 1 87 12 12 ARG HD3 H 3.061 0.020 1 88 12 12 ARG C C 176.344 0.400 1 89 12 12 ARG CA C 56.173 0.400 1 90 12 12 ARG CB C 30.859 0.400 1 91 12 12 ARG CD C 43.369 0.400 1 92 12 12 ARG N N 124.717 0.400 1 93 13 13 GLN H H 8.246 0.020 1 94 13 13 GLN HA H 4.208 0.020 1 95 13 13 GLN HB2 H 1.970 0.020 2 96 13 13 GLN HB3 H 1.854 0.020 2 97 13 13 GLN HE21 H 7.436 0.020 2 98 13 13 GLN HE22 H 6.776 0.020 2 99 13 13 GLN HG2 H 2.257 0.020 1 100 13 13 GLN HG3 H 2.257 0.020 1 101 13 13 GLN C C 175.971 0.400 1 102 13 13 GLN CA C 55.916 0.400 1 103 13 13 GLN CB C 29.864 0.400 1 104 13 13 GLN CG C 34.019 0.400 1 105 13 13 GLN N N 121.386 0.400 1 106 13 13 GLN NE2 N 112.483 0.400 1 107 14 14 LYS H H 8.276 0.020 1 108 14 14 LYS HA H 4.149 0.020 1 109 14 14 LYS HB2 H 1.703 0.020 2 110 14 14 LYS HB3 H 1.655 0.020 2 111 14 14 LYS HD2 H 1.548 0.020 1 112 14 14 LYS HD3 H 1.548 0.020 1 113 14 14 LYS HE2 H 2.856 0.020 1 114 14 14 LYS HE3 H 2.856 0.020 1 115 14 14 LYS HG2 H 1.365 0.020 2 116 14 14 LYS HG3 H 1.246 0.020 2 117 14 14 LYS C C 175.971 0.400 1 118 14 14 LYS CA C 56.518 0.400 1 119 14 14 LYS CB C 33.073 0.400 1 120 14 14 LYS CD C 29.241 0.400 1 121 14 14 LYS CE C 42.194 0.400 1 122 14 14 LYS CG C 25.027 0.400 1 123 14 14 LYS N N 123.021 0.400 1 124 15 15 THR H H 7.720 0.020 1 125 15 15 THR HA H 4.225 0.020 1 126 15 15 THR HB H 3.873 0.020 1 127 15 15 THR HG2 H 0.961 0.020 1 128 15 15 THR C C 173.801 0.400 1 129 15 15 THR CA C 62.211 0.400 1 130 15 15 THR CB C 70.979 0.400 1 131 15 15 THR CG2 C 22.248 0.400 1 132 15 15 THR N N 114.171 0.400 1 133 16 16 VAL H H 9.143 0.020 1 134 16 16 VAL HA H 4.004 0.020 1 135 16 16 VAL HB H 1.872 0.020 1 136 16 16 VAL HG1 H 0.744 0.020 1 137 16 16 VAL HG2 H 0.744 0.020 1 138 16 16 VAL C C 174.853 0.400 1 139 16 16 VAL CA C 62.452 0.400 1 140 16 16 VAL CB C 33.361 0.400 1 141 16 16 VAL CG1 C 20.774 0.400 1 142 16 16 VAL CG2 C 20.774 0.400 1 143 16 16 VAL N N 126.087 0.400 1 144 17 17 VAL H H 8.364 0.020 1 145 17 17 VAL HA H 4.653 0.020 1 146 17 17 VAL HB H 1.778 0.020 1 147 17 17 VAL HG1 H 0.723 0.020 2 148 17 17 VAL HG2 H 0.657 0.020 2 149 17 17 VAL C C 176.716 0.400 1 150 17 17 VAL CA C 61.419 0.400 1 151 17 17 VAL CB C 33.022 0.400 1 152 17 17 VAL CG1 C 21.474 0.400 1 153 17 17 VAL CG2 C 21.564 0.400 1 154 17 17 VAL N N 127.119 0.400 1 155 18 18 ARG H H 9.038 0.020 1 156 18 18 ARG HA H 4.669 0.020 1 157 18 18 ARG HB2 H 1.612 0.020 2 158 18 18 ARG HB3 H 1.694 0.020 2 159 18 18 ARG HD2 H 2.683 0.020 2 160 18 18 ARG HD3 H 3.121 0.020 2 161 18 18 ARG C C 174.480 0.400 1 162 18 18 ARG CA C 54.148 0.400 1 163 18 18 ARG CB C 33.202 0.400 1 164 18 18 ARG CD C 43.236 0.400 1 165 18 18 ARG N N 126.432 0.400 1 166 19 19 THR H H 8.536 0.020 1 167 19 19 THR HA H 4.727 0.020 1 168 19 19 THR HB H 3.747 0.020 1 169 19 19 THR HG2 H 0.913 0.020 1 170 19 19 THR C C 173.644 0.400 1 171 19 19 THR CA C 62.000 0.400 1 172 19 19 THR CB C 69.919 0.400 1 173 19 19 THR CG2 C 22.097 0.400 1 174 19 19 THR N N 118.670 0.400 1 175 20 20 LEU H H 8.972 0.020 1 176 20 20 LEU HA H 4.430 0.020 1 177 20 20 LEU HB2 H 0.951 0.020 2 178 20 20 LEU HB3 H 1.421 0.020 2 179 20 20 LEU HD1 H 0.721 0.020 2 180 20 20 LEU HD2 H 0.779 0.020 2 181 20 20 LEU HG H 1.442 0.020 1 182 20 20 LEU C C 174.294 0.400 1 183 20 20 LEU CA C 52.892 0.400 1 184 20 20 LEU CB C 45.825 0.400 1 185 20 20 LEU CD1 C 24.513 0.400 1 186 20 20 LEU CD2 C 26.679 0.400 1 187 20 20 LEU CG C 27.882 0.400 1 188 20 20 LEU N N 128.320 0.400 1 189 21 21 ARG H H 7.938 0.020 1 190 21 21 ARG HA H 4.945 0.020 1 191 21 21 ARG HB2 H 1.370 0.020 1 192 21 21 ARG HB3 H 1.370 0.020 1 193 21 21 ARG HD2 H 2.972 0.020 1 194 21 21 ARG HD3 H 2.972 0.020 1 195 21 21 ARG HG2 H 1.373 0.020 1 196 21 21 ARG HG3 H 1.373 0.020 1 197 21 21 ARG C C 175.333 0.400 1 198 21 21 ARG CA C 54.721 0.400 1 199 21 21 ARG CB C 32.512 0.400 1 200 21 21 ARG CD C 43.256 0.400 1 201 21 21 ARG CG C 28.445 0.400 1 202 21 21 ARG N N 119.462 0.400 1 203 22 22 PHE H H 9.021 0.020 1 204 22 22 PHE HA H 4.777 0.020 1 205 22 22 PHE HB2 H 2.468 0.020 2 206 22 22 PHE HB3 H 3.359 0.020 2 207 22 22 PHE HD1 H 7.079 0.020 1 208 22 22 PHE HD2 H 7.079 0.020 1 209 22 22 PHE HE1 H 6.845 0.020 1 210 22 22 PHE HE2 H 6.845 0.020 1 211 22 22 PHE HZ H 6.678 0.020 1 212 22 22 PHE C C 175.039 0.400 1 213 22 22 PHE CA C 56.549 0.400 1 214 22 22 PHE CB C 43.356 0.400 1 215 22 22 PHE CD1 C 132.227 0.400 1 216 22 22 PHE CD2 C 132.227 0.400 1 217 22 22 PHE CE1 C 130.762 0.400 1 218 22 22 PHE CE2 C 130.762 0.400 1 219 22 22 PHE CZ C 128.111 0.400 1 220 22 22 PHE N N 120.286 0.400 1 221 23 23 SER H H 9.411 0.020 1 222 23 23 SER HA H 4.937 0.020 1 223 23 23 SER C C 177.544 0.400 1 224 23 23 SER CA C 56.727 0.400 1 225 23 23 SER N N 119.420 0.400 1 226 24 24 PRO HA H 4.095 0.020 1 227 24 24 PRO HB2 H 1.877 0.020 2 228 24 24 PRO HB3 H 2.307 0.020 2 229 24 24 PRO HD2 H 3.851 0.020 1 230 24 24 PRO HD3 H 3.851 0.020 1 231 24 24 PRO HG2 H 2.081 0.020 1 232 24 24 PRO HG3 H 2.081 0.020 1 233 24 24 PRO C C 179.325 0.400 1 234 24 24 PRO CA C 66.570 0.400 1 235 24 24 PRO CB C 31.862 0.400 1 236 24 24 PRO CD C 50.222 0.400 1 237 24 24 PRO CG C 28.654 0.400 1 238 25 25 VAL H H 7.563 0.020 1 239 25 25 VAL HA H 3.779 0.020 1 240 25 25 VAL HB H 1.836 0.020 1 241 25 25 VAL HG1 H 0.822 0.020 2 242 25 25 VAL HG2 H 0.915 0.020 2 243 25 25 VAL C C 178.846 0.400 1 244 25 25 VAL CA C 65.693 0.400 1 245 25 25 VAL CB C 32.040 0.400 1 246 25 25 VAL CG1 C 20.838 0.400 1 247 25 25 VAL CG2 C 22.556 0.400 1 248 25 25 VAL N N 116.405 0.400 1 249 26 26 GLU H H 7.512 0.020 1 250 26 26 GLU HA H 3.838 0.020 1 251 26 26 GLU HB2 H 2.684 0.020 2 252 26 26 GLU HB3 H 1.934 0.020 2 253 26 26 GLU HG2 H 2.408 0.020 2 254 26 26 GLU HG3 H 2.312 0.020 2 255 26 26 GLU C C 178.766 0.400 1 256 26 26 GLU CA C 58.902 0.400 1 257 26 26 GLU CB C 30.798 0.400 1 258 26 26 GLU CG C 36.907 0.400 1 259 26 26 GLU N N 122.557 0.400 1 260 27 27 ASP H H 8.669 0.020 1 261 27 27 ASP HA H 3.900 0.020 1 262 27 27 ASP HB2 H 2.243 0.020 2 263 27 27 ASP HB3 H 2.536 0.020 2 264 27 27 ASP C C 177.586 0.400 1 265 27 27 ASP CA C 57.954 0.400 1 266 27 27 ASP CB C 43.617 0.400 1 267 27 27 ASP N N 118.012 0.400 1 268 28 28 GLU H H 7.875 0.020 1 269 28 28 GLU HA H 3.738 0.020 1 270 28 28 GLU HB2 H 2.017 0.020 1 271 28 28 GLU HB3 H 2.017 0.020 1 272 28 28 GLU C C 178.837 0.400 1 273 28 28 GLU CA C 59.710 0.400 1 274 28 28 GLU CB C 29.550 0.400 1 275 28 28 GLU N N 118.040 0.400 1 276 29 29 THR H H 7.662 0.020 1 277 29 29 THR HA H 3.739 0.020 1 278 29 29 THR HB H 4.293 0.020 1 279 29 29 THR HG2 H 1.087 0.020 1 280 29 29 THR C C 176.344 0.400 1 281 29 29 THR CA C 66.756 0.400 1 282 29 29 THR CB C 68.663 0.400 1 283 29 29 THR CG2 C 21.561 0.400 1 284 29 29 THR N N 116.635 0.400 1 285 30 30 ILE H H 7.875 0.020 1 286 30 30 ILE HA H 3.159 0.020 1 287 30 30 ILE HB H 1.486 0.020 1 288 30 30 ILE HD1 H -0.040 0.020 1 289 30 30 ILE HG12 H 1.267 0.020 2 290 30 30 ILE HG13 H 0.686 0.020 2 291 30 30 ILE HG2 H 0.559 0.020 1 292 30 30 ILE C C 176.903 0.400 1 293 30 30 ILE CA C 65.390 0.400 1 294 30 30 ILE CB C 37.356 0.400 1 295 30 30 ILE CD1 C 14.014 0.400 1 296 30 30 ILE CG1 C 28.801 0.400 1 297 30 30 ILE CG2 C 18.344 0.400 1 298 30 30 ILE N N 121.804 0.400 1 299 31 31 ARG H H 8.502 0.020 1 300 31 31 ARG HA H 3.508 0.020 1 301 31 31 ARG HB2 H 1.602 0.020 2 302 31 31 ARG HB3 H 1.686 0.020 2 303 31 31 ARG HD2 H 2.972 0.020 1 304 31 31 ARG HD3 H 2.972 0.020 1 305 31 31 ARG HG2 H 1.232 0.020 1 306 31 31 ARG HG3 H 1.232 0.020 1 307 31 31 ARG C C 179.262 0.400 1 308 31 31 ARG CA C 60.462 0.400 1 309 31 31 ARG CB C 30.075 0.400 1 310 31 31 ARG CD C 43.765 0.400 1 311 31 31 ARG CG C 28.442 0.400 1 312 31 31 ARG N N 119.175 0.400 1 313 32 32 LYS H H 7.497 0.020 1 314 32 32 LYS HA H 3.884 0.020 1 315 32 32 LYS HB2 H 1.751 0.020 1 316 32 32 LYS HB3 H 1.751 0.020 1 317 32 32 LYS HD2 H 1.572 0.020 2 318 32 32 LYS HD3 H 1.478 0.020 2 319 32 32 LYS HG2 H 1.309 0.020 1 320 32 32 LYS HG3 H 1.309 0.020 1 321 32 32 LYS C C 178.207 0.400 1 322 32 32 LYS CA C 59.176 0.400 1 323 32 32 LYS CB C 32.020 0.400 1 324 32 32 LYS CD C 28.724 0.400 1 325 32 32 LYS CG C 24.890 0.400 1 326 32 32 LYS N N 119.486 0.400 1 327 33 33 LYS H H 7.540 0.020 1 328 33 33 LYS HB2 H 2.018 0.020 1 329 33 33 LYS HB3 H 2.018 0.020 1 330 33 33 LYS C C 179.884 0.400 1 331 33 33 LYS CB C 32.095 0.400 1 332 33 33 LYS N N 119.050 0.400 1 333 34 34 ALA H H 8.208 0.020 1 334 34 34 ALA HA H 3.448 0.020 1 335 34 34 ALA HB H 1.040 0.020 1 336 34 34 ALA C C 179.325 0.400 1 337 34 34 ALA CA C 55.826 0.400 1 338 34 34 ALA CB C 17.665 0.400 1 339 34 34 ALA N N 122.909 0.400 1 340 35 35 GLU H H 7.997 0.020 1 341 35 35 GLU HA H 3.877 0.020 1 342 35 35 GLU HB2 H 2.021 0.020 2 343 35 35 GLU HB3 H 1.994 0.020 2 344 35 35 GLU C C 181.002 0.400 1 345 35 35 GLU CA C 59.737 0.400 1 346 35 35 GLU CB C 29.381 0.400 1 347 35 35 GLU N N 119.482 0.400 1 348 36 36 ASP H H 8.405 0.020 1 349 36 36 ASP HA H 4.279 0.020 1 350 36 36 ASP HB2 H 2.599 0.020 1 351 36 36 ASP HB3 H 2.599 0.020 1 352 36 36 ASP C C 177.834 0.400 1 353 36 36 ASP CA C 57.178 0.400 1 354 36 36 ASP CB C 40.502 0.400 1 355 36 36 ASP N N 120.553 0.400 1 356 37 37 SER H H 7.481 0.020 1 357 37 37 SER HA H 4.450 0.020 1 358 37 37 SER HB2 H 3.969 0.020 1 359 37 37 SER HB3 H 3.969 0.020 1 360 37 37 SER C C 174.294 0.400 1 361 37 37 SER CA C 59.149 0.400 1 362 37 37 SER CB C 64.866 0.400 1 363 37 37 SER N N 112.666 0.400 1 364 38 38 GLY H H 7.871 0.020 1 365 38 38 GLY HA2 H 3.895 0.020 2 366 38 38 GLY HA3 H 3.772 0.020 2 367 38 38 GLY C C 174.108 0.400 1 368 38 38 GLY CA C 46.433 0.400 1 369 38 38 GLY N N 110.893 0.400 1 370 39 39 LEU H H 7.850 0.020 1 371 39 39 LEU HA H 4.782 0.020 1 372 39 39 LEU HB2 H 1.458 0.020 2 373 39 39 LEU HB3 H 1.660 0.020 2 374 39 39 LEU HD1 H 0.764 0.020 1 375 39 39 LEU HD2 H 0.764 0.020 1 376 39 39 LEU HG H 1.456 0.020 1 377 39 39 LEU C C 177.538 0.400 1 378 39 39 LEU CA C 53.141 0.400 1 379 39 39 LEU CB C 47.097 0.400 1 380 39 39 LEU CD1 C 22.817 0.400 1 381 39 39 LEU CD2 C 22.817 0.400 1 382 39 39 LEU CG C 26.361 0.400 1 383 39 39 LEU N N 119.947 0.400 1 384 40 40 THR H H 7.654 0.020 1 385 40 40 THR HA H 4.234 0.020 1 386 40 40 THR HB H 4.570 0.020 1 387 40 40 THR HG2 H 1.231 0.020 1 388 40 40 THR C C 175.658 0.400 1 389 40 40 THR CA C 61.188 0.400 1 390 40 40 THR CB C 70.501 0.400 1 391 40 40 THR CG2 C 22.273 0.400 1 392 40 40 THR N N 109.345 0.400 1 393 41 41 VAL H H 8.721 0.020 1 394 41 41 VAL HA H 3.239 0.020 1 395 41 41 VAL HB H 1.832 0.020 1 396 41 41 VAL HG1 H 0.613 0.020 2 397 41 41 VAL HG2 H 0.830 0.020 2 398 41 41 VAL C C 178.021 0.400 1 399 41 41 VAL CA C 68.189 0.400 1 400 41 41 VAL CB C 31.300 0.400 1 401 41 41 VAL CG1 C 21.453 0.400 1 402 41 41 VAL CG2 C 24.317 0.400 1 403 41 41 VAL N N 121.470 0.400 1 404 42 42 SER H H 8.424 0.020 1 405 42 42 SER HA H 3.742 0.020 1 406 42 42 SER C C 175.785 0.400 1 407 42 42 SER CA C 62.514 0.400 1 408 42 42 SER N N 113.251 0.400 1 409 43 43 ALA H H 7.494 0.020 1 410 43 43 ALA HA H 3.916 0.020 1 411 43 43 ALA HB H 1.374 0.020 1 412 43 43 ALA C C 179.884 0.400 1 413 43 43 ALA CA C 55.172 0.400 1 414 43 43 ALA CB C 19.490 0.400 1 415 43 43 ALA N N 123.328 0.400 1 416 44 44 TYR H H 8.662 0.020 1 417 44 44 TYR HA H 3.742 0.020 1 418 44 44 TYR HB2 H 2.773 0.020 2 419 44 44 TYR HB3 H 3.102 0.020 2 420 44 44 TYR HD1 H 6.749 0.020 1 421 44 44 TYR HD2 H 6.749 0.020 1 422 44 44 TYR HE1 H 6.659 0.020 1 423 44 44 TYR HE2 H 6.659 0.020 1 424 44 44 TYR C C 177.593 0.400 1 425 44 44 TYR CA C 62.514 0.400 1 426 44 44 TYR CB C 39.211 0.400 1 427 44 44 TYR CD1 C 132.769 0.400 1 428 44 44 TYR CD2 C 132.769 0.400 1 429 44 44 TYR CE1 C 118.074 0.400 1 430 44 44 TYR CE2 C 118.074 0.400 1 431 44 44 TYR N N 119.611 0.400 1 432 45 45 ILE H H 8.445 0.020 1 433 45 45 ILE HA H 3.138 0.020 1 434 45 45 ILE HB H 1.667 0.020 1 435 45 45 ILE HD1 H 0.651 0.020 1 436 45 45 ILE HG12 H 2.190 0.020 1 437 45 45 ILE HG13 H 2.190 0.020 1 438 45 45 ILE HG2 H 0.718 0.020 1 439 45 45 ILE C C 177.462 0.400 1 440 45 45 ILE CA C 66.393 0.400 1 441 45 45 ILE CB C 37.810 0.400 1 442 45 45 ILE CD1 C 14.446 0.400 1 443 45 45 ILE CG1 C 29.143 0.400 1 444 45 45 ILE CG2 C 19.038 0.400 1 445 45 45 ILE N N 118.859 0.400 1 446 46 46 ARG H H 8.026 0.020 1 447 46 46 ARG HA H 3.635 0.020 1 448 46 46 ARG HB2 H 1.683 0.020 2 449 46 46 ARG HB3 H 1.618 0.020 2 450 46 46 ARG HD2 H 3.092 0.020 2 451 46 46 ARG HD3 H 2.839 0.020 2 452 46 46 ARG C C 177.462 0.400 1 453 46 46 ARG CA C 60.816 0.400 1 454 46 46 ARG CB C 30.287 0.400 1 455 46 46 ARG CD C 42.590 0.400 1 456 46 46 ARG N N 117.983 0.400 1 457 47 47 ASN H H 8.026 0.020 1 458 47 47 ASN HA H 4.078 0.020 1 459 47 47 ASN HB2 H 2.531 0.020 2 460 47 47 ASN HB3 H 2.586 0.020 2 461 47 47 ASN HD21 H 7.308 0.020 2 462 47 47 ASN HD22 H 6.880 0.020 2 463 47 47 ASN C C 177.648 0.400 1 464 47 47 ASN CA C 56.329 0.400 1 465 47 47 ASN CB C 38.112 0.400 1 466 47 47 ASN N N 115.323 0.400 1 467 47 47 ASN ND2 N 111.936 0.400 1 468 48 48 ALA H H 7.809 0.020 1 469 48 48 ALA HA H 3.792 0.020 1 470 48 48 ALA HB H 0.899 0.020 1 471 48 48 ALA C C 179.325 0.400 1 472 48 48 ALA CA C 54.393 0.400 1 473 48 48 ALA CB C 16.905 0.400 1 474 48 48 ALA N N 121.450 0.400 1 475 49 49 ALA H H 7.863 0.020 1 476 49 49 ALA HA H 3.821 0.020 1 477 49 49 ALA HB H 1.402 0.020 1 478 49 49 ALA C C 178.503 0.400 1 479 49 49 ALA CA C 54.016 0.400 1 480 49 49 ALA CB C 19.693 0.400 1 481 49 49 ALA N N 117.188 0.400 1 482 50 50 LEU H H 7.610 0.020 1 483 50 50 LEU HA H 4.062 0.020 1 484 50 50 LEU HB2 H 1.685 0.020 2 485 50 50 LEU HB3 H 1.431 0.020 2 486 50 50 LEU HD1 H 0.816 0.020 2 487 50 50 LEU HD2 H 0.857 0.020 2 488 50 50 LEU HG H 1.673 0.020 1 489 50 50 LEU C C 176.716 0.400 1 490 50 50 LEU CA C 55.766 0.400 1 491 50 50 LEU CB C 43.320 0.400 1 492 50 50 LEU CD1 C 23.312 0.400 1 493 50 50 LEU CD2 C 25.503 0.400 1 494 50 50 LEU CG C 27.620 0.400 1 495 50 50 LEU N N 116.113 0.400 1 496 51 51 ASN H H 7.277 0.020 1 497 51 51 ASN HA H 4.355 0.020 1 498 51 51 ASN HB2 H 2.599 0.020 1 499 51 51 ASN HB3 H 2.599 0.020 1 500 51 51 ASN HD21 H 7.484 0.020 2 501 51 51 ASN HD22 H 6.630 0.020 2 502 51 51 ASN C C 179.908 0.400 1 503 51 51 ASN CA C 55.505 0.400 1 504 51 51 ASN CB C 40.502 0.400 1 505 51 51 ASN N N 123.881 0.400 1 506 51 51 ASN ND2 N 113.123 0.400 1 stop_ save_