data_16134 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Backbone 1H, 13C, and 15N Chemical Shift Assignments for tolaIII residues296-421in complex with unlabelled colicin N Tdomain ; _BMRB_accession_number 16134 _BMRB_flat_file_name bmr16134.str _Entry_type original _Submission_date 2009-01-23 _Accession_date 2009-01-23 _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 Hecht Oliver . . 2 Moore Geoffrey . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 70 "13C chemical shifts" 148 "15N chemical shifts" 71 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2009-05-05 update BMRB 'complete entry citation' 2009-04-17 original author 'original release' stop_ loop_ _Related_BMRB_accession_number _Relationship 16130 'Tdom 40-76 TolAIII complex' 16131 Tdom40-76 16133 TolAIII stop_ save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title 'A common interation for the entry of colicin N and filamentous phage into Escherichia Coli' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 19306883 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Hecht Oliver . . 2 Ridley Helen . . 3 Lakey Jeremy . . 4 Moore Geoffrey . . stop_ _Journal_abbreviation 'J. Mol. Biol.' _Journal_name_full 'Journal of Molecular Biology' _Journal_volume 388 _Journal_issue 4 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 880 _Page_last 893 _Year 2009 _Details . save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name TolAIII+tdom _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label TolAIII $TolAIII Tdom40-76 $Tdom40-76 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_TolAIII _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common TolAIII _Molecular_mass . _Mol_thiol_state 'all disulfide bound' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 135 _Mol_residue_sequence ; HHHHHHSSQIFSVTLSSGKN APKTGGGAKGNNASPAGSGN TKNNGASGADINNYAGQIKS AIESKFYDASSYAGKTCTLR IKLAPDGMLLDIKPEGGDPA LCQAALAAAKLAKIPKPPSQ AVYEVFKNAPLDFKP ; loop_ _Residue_seq_code _Residue_label 1 HIS 2 HIS 3 HIS 4 HIS 5 HIS 6 HIS 7 SER 8 SER 9 GLN 10 ILE 11 PHE 12 SER 13 VAL 14 THR 15 LEU 16 SER 17 SER 18 GLY 19 LYS 20 ASN 21 ALA 22 PRO 23 LYS 24 THR 25 GLY 26 GLY 27 GLY 28 ALA 29 LYS 30 GLY 31 ASN 32 ASN 33 ALA 34 SER 35 PRO 36 ALA 37 GLY 38 SER 39 GLY 40 ASN 41 THR 42 LYS 43 ASN 44 ASN 45 GLY 46 ALA 47 SER 48 GLY 49 ALA 50 ASP 51 ILE 52 ASN 53 ASN 54 TYR 55 ALA 56 GLY 57 GLN 58 ILE 59 LYS 60 SER 61 ALA 62 ILE 63 GLU 64 SER 65 LYS 66 PHE 67 TYR 68 ASP 69 ALA 70 SER 71 SER 72 TYR 73 ALA 74 GLY 75 LYS 76 THR 77 CYS 78 THR 79 LEU 80 ARG 81 ILE 82 LYS 83 LEU 84 ALA 85 PRO 86 ASP 87 GLY 88 MET 89 LEU 90 LEU 91 ASP 92 ILE 93 LYS 94 PRO 95 GLU 96 GLY 97 GLY 98 ASP 99 PRO 100 ALA 101 LEU 102 CYS 103 GLN 104 ALA 105 ALA 106 LEU 107 ALA 108 ALA 109 ALA 110 LYS 111 LEU 112 ALA 113 LYS 114 ILE 115 PRO 116 LYS 117 PRO 118 PRO 119 SER 120 GLN 121 ALA 122 VAL 123 TYR 124 GLU 125 VAL 126 PHE 127 LYS 128 ASN 129 ALA 130 PRO 131 LEU 132 ASP 133 PHE 134 LYS 135 PRO 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 BMRB 16133 TolAIII 100.00 135 100.00 100.00 6.36e-91 PDB 1S62 "Solution Structure Of The Escherichia Coli Tola C-Terminal Domain" 71.85 106 100.00 100.00 1.51e-61 PDB 1TOL "Fusion Of N-Terminal Domain Of The Minor Coat Protein From Gene Iii In Phage M13, And C-Terminal Domain Of E. Coli Protein-Tola" 89.63 222 100.00 100.00 1.66e-77 PDB 2X9A "Crystal Structure Of G3p From Phage If1 In Complex With Its Coreceptor, The C-Terminal Domain Of Tola" 89.63 136 100.00 100.00 5.80e-78 EMBL CTW32328 "cell envelope integrity inner membrane protein TolA [Escherichia coli]" 93.33 421 97.62 97.62 4.82e-83 GB AHA63696 "TolA protein [Shigella dysenteriae 1617]" 83.70 116 99.12 99.12 1.07e-71 GB AHG07456 "TolA protein [Escherichia coli O145:H28 str. RM13514]" 93.33 368 97.62 97.62 8.74e-85 GB AHY69283 "TolA protein [Escherichia coli O145:H28 str. RM12581]" 93.33 368 97.62 97.62 8.74e-85 GB EGB67246 "TonB family protein domain-containing protein [Escherichia coli TA007]" 81.48 115 99.09 99.09 6.55e-70 GB EGC08283 "TonB family protein domain-containing protein [Escherichia fergusonii B253]" 71.85 98 96.91 97.94 3.54e-60 REF WP_000030617 "cell envelope integrity/translocation protein TolA [Escherichia coli]" 93.33 421 97.62 97.62 7.26e-83 REF WP_000030621 "cell envelope integrity/translocation protein TolA [Escherichia sp. TW09231]" 93.33 422 97.62 97.62 3.29e-83 REF WP_000030643 "cell envelope integrity/translocation protein TolA [Escherichia coli]" 93.33 437 97.62 97.62 2.62e-83 REF WP_000030697 "MULTISPECIES: cell envelope integrity/translocation protein TolA [Escherichia]" 93.33 422 97.62 97.62 4.04e-83 REF WP_000030705 "cell envelope integrity/translocation protein TolA [Escherichia sp. TW14182]" 93.33 425 97.62 97.62 2.25e-83 stop_ save_ save_Tdom40-76 _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common Tdom40-76 _Molecular_mass . _Mol_thiol_state 'not present' _Details . _Residue_count 90 _Mol_residue_sequence ; MGSNGADNAHNNAFGGGKNP GIGNTSGAGSNGSASSNRGN SNGWSWSNKPHKNDGFHSDG SYHITFHGDNNSKPKPGGNS GNRGNNGDGA ; loop_ _Residue_seq_code _Residue_label 1 MET 2 GLY 3 SER 4 ASN 5 GLY 6 ALA 7 ASP 8 ASN 9 ALA 10 HIS 11 ASN 12 ASN 13 ALA 14 PHE 15 GLY 16 GLY 17 GLY 18 LYS 19 ASN 20 PRO 21 GLY 22 ILE 23 GLY 24 ASN 25 THR 26 SER 27 GLY 28 ALA 29 GLY 30 SER 31 ASN 32 GLY 33 SER 34 ALA 35 SER 36 SER 37 ASN 38 ARG 39 GLY 40 ASN 41 SER 42 ASN 43 GLY 44 TRP 45 SER 46 TRP 47 SER 48 ASN 49 LYS 50 PRO 51 HIS 52 LYS 53 ASN 54 ASP 55 GLY 56 PHE 57 HIS 58 SER 59 ASP 60 GLY 61 SER 62 TYR 63 HIS 64 ILE 65 THR 66 PHE 67 HIS 68 GLY 69 ASP 70 ASN 71 ASN 72 SER 73 LYS 74 PRO 75 LYS 76 PRO 77 GLY 78 GLY 79 ASN 80 SER 81 GLY 82 ASN 83 ARG 84 GLY 85 ASN 86 ASN 87 GLY 88 ASP 89 GLY 90 ALA stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-01-30 loop_ _Database_name _Database_accession_code _Database_entry_mol_name _Sequence_query_to_submitted_percentage _Sequence_subject_length _Sequence_identity _Sequence_positive _Sequence_homology_expectation_value BMRB 15506 Colicin_N_T_domain 98.89 90 100.00 100.00 2.88e-49 BMRB 16130 Tdom40-76 100.00 90 100.00 100.00 2.00e-50 BMRB 16131 Tdom40-47 100.00 90 100.00 100.00 2.00e-50 EMBL CAA68592 "unnamed protein product [Escherichia coli]" 100.00 387 100.00 100.00 2.30e-51 GB EMX27764 "colicin-N [Escherichia coli MP021561.2]" 100.00 387 100.00 100.00 2.33e-51 GB EMZ96444 "colicin-N [Escherichia coli P0299917.1]" 100.00 387 100.00 100.00 2.35e-51 GB KHH25654 "colicin-N [Escherichia coli]" 100.00 387 98.89 100.00 6.87e-51 GB KHH41883 "colicin-N [Escherichia coli]" 100.00 387 100.00 100.00 2.30e-51 GB KHH74941 "colicin-N [Escherichia coli]" 100.00 387 100.00 100.00 2.30e-51 REF WP_001749638 "colicin-N [Escherichia coli]" 100.00 387 100.00 100.00 2.35e-51 REF WP_004026235 "colicin-N [Escherichia coli]" 100.00 387 100.00 100.00 2.33e-51 REF WP_024139131 "colicin-N [Salmonella enterica]" 100.00 387 98.89 100.00 7.97e-51 REF WP_032488335 "unnamed protein product [Escherichia coli]" 100.00 387 100.00 100.00 2.30e-51 REF YP_009073784 "unnamed protein product [Escherichia coli]" 100.00 387 100.00 100.00 2.30e-51 SP P08083 "RecName: Full=Colicin-N [Escherichia coli]" 100.00 387 100.00 100.00 2.30e-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 $TolAIII 'E. coli' 562 Bacteria . Escherichia coli stop_ save_ ######################### # Experimental source # ######################### save_experimental_source _Saveframe_category experimental_source loop_ _Mol_label _Production_method _Host_organism_name_common _Genus _Species _Strain _Vector_name $TolAIII 'recombinant technology' . Escherichia coli . pet8c 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 $TolAIII 0.8 mM '[U-100% 13C; U-100% 15N]' $Tdom40-76 0.8 mM 'natural abundance' H2O 90 % 'natural abundance' D2O 10 % 'natural abundance' stop_ save_ ############################ # Computer software used # ############################ save_NMRView _Saveframe_category software _Name NMRView _Version . loop_ _Vendor _Address _Electronic_address 'Johnson, One Moon Scientific' . . stop_ loop_ _Task 'chemical shift assignment' stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model INOVA _Field_strength 500 _Details . save_ save_spectrometer_2 _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model INOVA _Field_strength 600 _Details . save_ ############################# # NMR applied experiments # ############################# save_2D_1H-15N_HSQC_1 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-15N HSQC' _Sample_label $sample_1 save_ save_3D_CBCA(CO)NH_2 _Saveframe_category NMR_applied_experiment _Experiment_name '3D CBCA(CO)NH' _Sample_label $sample_1 save_ save_3D_HNCACB_3 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCACB' _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' 0.35 . M pH 6.8 . pH pressure 1 . atm temperature 300 . 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 '2D 1H-15N HSQC' '3D CBCA(CO)NH' '3D HNCACB' 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 TolAIII _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 49 49 ALA CA C 54.943 . 1 2 49 49 ALA CB C 18.558 . 1 3 50 50 ASP H H 8.107 . 1 4 50 50 ASP CA C 57.255 . 1 5 50 50 ASP CB C 40.523 . 1 6 50 50 ASP N N 118.872 . 1 7 51 51 ILE H H 8.117 . 1 8 51 51 ILE CA C 65.830 . 1 9 51 51 ILE CB C 45.745 . 1 10 51 51 ILE N N 121.296 . 1 11 52 52 ASN H H 8.354 . 1 12 52 52 ASN CA C 56.420 . 1 13 52 52 ASN CB C 38.448 . 1 14 52 52 ASN N N 117.625 . 1 15 53 53 ASN H H 8.762 . 1 16 53 53 ASN CA C 56.223 . 1 17 53 53 ASN CB C 38.686 . 1 18 53 53 ASN N N 118.869 . 1 19 54 54 TYR H H 8.107 . 1 20 54 54 TYR CA C 61.671 . 1 21 54 54 TYR CB C 38.062 . 1 22 54 54 TYR N N 122.071 . 1 23 55 55 ALA H H 8.138 . 1 24 55 55 ALA CA C 55.534 . 1 25 55 55 ALA CB C 18.597 . 1 26 55 55 ALA N N 121.089 . 1 27 56 56 GLY H H 7.683 . 1 28 56 56 GLY CA C 47.027 . 1 29 56 56 GLY N N 101.628 . 1 30 57 57 GLN H H 7.717 . 1 31 57 57 GLN CA C 58.910 . 1 32 57 57 GLN CB C 28.675 . 1 33 57 57 GLN N N 122.674 . 1 34 58 58 ILE H H 7.840 . 1 35 58 58 ILE CA C 66.502 . 1 36 58 58 ILE CB C 37.971 . 1 37 58 58 ILE N N 121.817 . 1 38 60 60 SER CA C 61.651 . 1 39 60 60 SER CB C 63.140 . 1 40 61 61 ALA H H 7.821 . 1 41 61 61 ALA CA C 55.347 . 1 42 61 61 ALA CB C 18.774 . 1 43 61 61 ALA N N 123.603 . 1 44 62 62 ILE H H 7.873 . 1 45 62 62 ILE CA C 64.973 . 1 46 62 62 ILE CB C 37.785 . 1 47 62 62 ILE N N 117.626 . 1 48 63 63 GLU H H 4.244 . 1 49 63 63 GLU CA C 60.400 . 1 50 63 63 GLU CB C 30.092 . 1 51 63 63 GLU N N 120.894 . 1 52 64 64 SER H H 7.802 . 1 53 64 64 SER CA C 61.603 . 1 54 64 64 SER CB C 63.601 . 1 55 64 64 SER N N 110.122 . 1 56 65 65 LYS H H 7.184 . 1 57 65 65 LYS CA C 54.128 . 1 58 65 65 LYS CB C 33.382 . 1 59 65 65 LYS N N 116.503 . 1 60 66 66 PHE H H 8.326 . 1 61 66 66 PHE CA C 52.479 . 1 62 66 66 PHE CB C 36.823 . 1 63 66 66 PHE N N 123.875 . 1 64 67 67 TYR H H 7.472 . 1 65 67 67 TYR CA C 59.987 . 1 66 67 67 TYR CB C 38.741 . 1 67 67 67 TYR N N 118.973 . 1 68 68 68 ASP H H 8.297 . 1 69 68 68 ASP CA C 53.426 . 1 70 68 68 ASP CB C 41.547 . 1 71 68 68 ASP N N 117.239 . 1 72 71 71 SER CA C 60.503 . 1 73 71 71 SER CB C 62.373 . 1 74 72 72 TYR H H 7.519 . 1 75 72 72 TYR CA C 55.773 . 1 76 72 72 TYR CB C 40.521 . 1 77 72 72 TYR N N 118.390 . 1 78 73 73 ALA H H 6.829 . 1 79 73 73 ALA CA C 54.149 . 1 80 73 73 ALA CB C 18.443 . 1 81 73 73 ALA N N 121.414 . 1 82 74 74 GLY H H 9.014 . 1 83 74 74 GLY CA C 45.791 . 1 84 74 74 GLY N N 112.627 . 1 85 75 75 LYS H H 8.406 . 1 86 75 75 LYS CA C 54.533 . 1 87 75 75 LYS CB C 34.271 . 1 88 75 75 LYS N N 120.310 . 1 89 76 76 THR H H 8.539 . 1 90 76 76 THR CA C 60.169 . 1 91 76 76 THR CB C 72.799 . 1 92 76 76 THR N N 108.496 . 1 93 77 77 CYS H H 8.461 . 1 94 77 77 CYS CA C 58.047 . 1 95 77 77 CYS CB C 49.853 . 1 96 77 77 CYS N N 117.607 . 1 97 78 78 THR H H 8.795 . 1 98 78 78 THR CA C 62.947 . 1 99 78 78 THR CB C 72.351 . 1 100 78 78 THR N N 128.209 . 1 101 79 79 LEU H H 9.652 . 1 102 79 79 LEU CA C 52.824 . 1 103 79 79 LEU CB C 45.260 . 1 104 79 79 LEU N N 125.755 . 1 105 80 80 ARG H H 9.208 . 1 106 80 80 ARG CA C 54.330 . 1 107 80 80 ARG CB C 31.847 . 1 108 80 80 ARG N N 122.904 . 1 109 81 81 ILE H H 8.426 . 1 110 81 81 ILE CA C 60.476 . 1 111 81 81 ILE CB C 40.600 . 1 112 81 81 ILE N N 122.254 . 1 113 82 82 LYS H H 7.921 . 1 114 82 82 LYS CA C 55.709 . 1 115 82 82 LYS CB C 35.180 . 1 116 82 82 LYS N N 120.339 . 1 117 83 83 LEU H H 8.997 . 1 118 83 83 LEU CA C 53.659 . 1 119 83 83 LEU CB C 46.709 . 1 120 83 83 LEU N N 127.051 . 1 121 84 84 ALA H H 9.503 . 1 122 84 84 ALA CA C 50.771 . 1 123 84 84 ALA CB C 19.584 . 1 124 84 84 ALA N N 129.613 . 1 125 85 85 PRO CA C 64.685 . 1 126 85 85 PRO CB C 31.463 . 1 127 86 86 ASP H H 7.581 . 1 128 86 86 ASP CA C 52.867 . 1 129 86 86 ASP CB C 40.245 . 1 130 86 86 ASP N N 111.988 . 1 131 87 87 GLY H H 8.585 . 1 132 87 87 GLY CA C 45.094 . 1 133 87 87 GLY N N 108.481 . 1 134 88 88 MET H H 7.620 . 1 135 88 88 MET CA C 56.443 . 1 136 88 88 MET CB C 33.033 . 1 137 88 88 MET N N 117.635 . 1 138 89 89 LEU H H 8.720 . 1 139 89 89 LEU CA C 55.004 . 1 140 89 89 LEU CB C 41.799 . 1 141 89 89 LEU N N 124.796 . 1 142 90 90 LEU H H 9.106 . 1 143 90 90 LEU CA C 56.138 . 1 144 90 90 LEU CB C 43.021 . 1 145 90 90 LEU N N 128.118 . 1 146 91 91 ASP H H 7.915 . 1 147 91 91 ASP CA C 53.511 . 1 148 91 91 ASP CB C 44.656 . 1 149 91 91 ASP N N 114.490 . 1 150 92 92 ILE H H 8.216 . 1 151 92 92 ILE CA C 60.923 . 1 152 92 92 ILE CB C 40.533 . 1 153 92 92 ILE N N 118.921 . 1 154 93 93 LYS H H 8.566 . 1 155 93 93 LYS CA C 52.709 . 1 156 93 93 LYS CB C 36.047 . 1 157 93 93 LYS N N 125.167 . 1 158 94 94 PRO CB C 31.743 . 1 159 94 94 PRO N N 126.470 . 1 160 95 95 GLU H H 9.270 . 1 161 95 95 GLU CA C 56.364 . 1 162 95 95 GLU CB C 31.425 . 1 163 95 95 GLU N N 124.846 . 1 164 96 96 GLY H H 7.616 . 1 165 96 96 GLY CA C 45.326 . 1 166 96 96 GLY N N 106.770 . 1 167 97 97 GLY H H 8.223 . 1 168 97 97 GLY CA C 44.666 . 1 169 97 97 GLY N N 106.502 . 1 170 98 98 ASP H H 8.795 . 1 171 98 98 ASP CA C 52.713 . 1 172 98 98 ASP CB C 44.198 . 1 173 98 98 ASP N N 122.302 . 1 174 99 99 PRO CA C 66.060 . 1 175 99 99 PRO CB C 32.443 . 1 176 100 100 ALA H H 7.993 . 1 177 100 100 ALA CA C 55.390 . 1 178 100 100 ALA CB C 18.638 . 1 179 100 100 ALA N N 120.541 . 1 180 101 101 LEU H H 8.538 . 1 181 101 101 LEU CA C 57.479 . 1 182 101 101 LEU CB C 29.379 . 1 183 101 101 LEU N N 121.437 . 1 184 102 102 CYS H H 9.028 . 1 185 102 102 CYS CA C 56.098 . 1 186 102 102 CYS CB C 36.979 . 1 187 102 102 CYS N N 114.397 . 1 188 103 103 GLN H H 8.173 . 1 189 103 103 GLN CA C 59.077 . 1 190 103 103 GLN CB C 28.236 . 1 191 103 103 GLN N N 118.590 . 1 192 104 104 ALA H H 7.625 . 1 193 104 104 ALA CA C 54.788 . 1 194 104 104 ALA CB C 18.574 . 1 195 104 104 ALA N N 123.859 . 1 196 105 105 ALA H H 8.372 . 1 197 105 105 ALA CA C 54.152 . 1 198 105 105 ALA CB C 16.418 . 1 199 105 105 ALA N N 121.426 . 1 200 106 106 LEU H H 3.012 . 1 201 106 106 LEU CA C 58.871 . 1 202 106 106 LEU CB C 42.731 . 1 203 106 106 LEU N N 119.280 . 1 204 107 107 ALA H H 7.523 . 1 205 107 107 ALA CA C 54.891 . 1 206 107 107 ALA CB C 17.941 . 1 207 107 107 ALA N N 119.002 . 1 208 108 108 ALA H H 7.076 . 1 209 108 108 ALA CA C 54.556 . 1 210 108 108 ALA CB C 18.818 . 1 211 108 108 ALA N N 118.052 . 1 212 109 109 ALA H H 8.371 . 1 213 109 109 ALA CA C 55.338 . 1 214 109 109 ALA CB C 17.896 . 1 215 109 109 ALA N N 118.346 . 1 216 110 110 LYS H H 11.420 . 1 217 110 110 LYS CA C 59.023 . 1 218 110 110 LYS CB C 32.777 . 1 219 110 110 LYS N N 113.397 . 1 220 111 111 LEU H H 7.370 . 1 221 111 111 LEU CA C 54.686 . 1 222 111 111 LEU CB C 43.488 . 1 223 111 111 LEU N N 117.383 . 1 224 112 112 ALA H H 7.393 . 1 225 112 112 ALA CA C 52.395 . 1 226 112 112 ALA CB C 20.582 . 1 227 112 112 ALA N N 121.801 . 1 228 113 113 LYS H H 8.627 . 1 229 113 113 LYS CA C 54.343 . 1 230 113 113 LYS CB C 31.711 . 1 231 113 113 LYS N N 123.332 . 1 232 114 114 ILE H H 8.581 . 1 233 114 114 ILE CA C 58.584 . 1 234 114 114 ILE CB C 37.667 . 1 235 114 114 ILE N N 129.050 . 1 236 120 120 GLN CA C 58.880 . 1 237 120 120 GLN CB C 28.003 . 1 238 121 121 ALA H H 8.446 . 1 239 121 121 ALA CA C 55.208 . 1 240 121 121 ALA CB C 18.498 . 1 241 121 121 ALA N N 120.425 . 1 242 122 122 VAL H H 7.526 . 1 243 122 122 VAL CA C 66.474 . 1 244 122 122 VAL CB C 31.964 . 1 245 122 122 VAL N N 116.331 . 1 246 123 123 TYR H H 8.177 . 1 247 123 123 TYR CA C 61.621 . 1 248 123 123 TYR CB C 37.681 . 1 249 123 123 TYR N N 120.704 . 1 250 124 124 GLU H H 8.220 . 1 251 124 124 GLU CA C 59.306 . 1 252 124 124 GLU CB C 29.617 . 1 253 124 124 GLU N N 114.428 . 1 254 125 125 VAL H H 7.212 . 1 255 125 125 VAL CA C 65.609 . 1 256 125 125 VAL CB C 32.126 . 1 257 125 125 VAL N N 116.874 . 1 258 126 126 PHE H H 7.273 . 1 259 126 126 PHE CA C 60.084 . 1 260 126 126 PHE CB C 41.098 . 1 261 126 126 PHE N N 115.410 . 1 262 127 127 LYS H H 7.604 . 1 263 127 127 LYS CA C 59.863 . 1 264 127 127 LYS CB C 36.213 . 1 265 127 127 LYS N N 117.690 . 1 266 128 128 ASN H H 8.059 . 1 267 128 128 ASN CA C 51.628 . 1 268 128 128 ASN CB C 40.378 . 1 269 128 128 ASN N N 118.491 . 1 270 129 129 ALA H H 7.274 . 1 271 129 129 ALA CA C 51.728 . 1 272 129 129 ALA CB C 19.409 . 1 273 129 129 ALA N N 123.769 . 1 274 130 130 PRO CA C 61.603 . 1 275 130 130 PRO CB C 31.391 . 1 276 131 131 LEU H H 9.212 . 1 277 131 131 LEU CA C 52.679 . 1 278 131 131 LEU CB C 43.091 . 1 279 131 131 LEU N N 121.547 . 1 280 132 132 ASP H H 9.207 . 1 281 132 132 ASP CA C 53.890 . 1 282 132 132 ASP CB C 42.244 . 1 283 132 132 ASP N N 123.915 . 1 284 133 133 PHE H H 9.996 . 1 285 133 133 PHE CA C 58.897 . 1 286 133 133 PHE CB C 40.925 . 1 287 133 133 PHE N N 123.077 . 1 288 134 134 LYS H H 10.037 . 1 289 134 134 LYS N N 125.528 . 1 stop_ save_