data_27402 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; chemical shifts for human Axin DIX domain ; _BMRB_accession_number 27402 _BMRB_flat_file_name bmr27402.str _Entry_type original _Submission_date 2018-02-14 _Accession_date 2018-02-14 _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 Ward Meaghan E. . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "13C chemical shifts" 273 "15N chemical shifts" 67 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2020-10-06 original BMRB . stop_ _Original_release_date 2018-02-15 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; Investigations of dynamic amyloid-like structures of the Wnt signalling pathway by solid-state NMR ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 29561051 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Ward Meaghan E. . 2 Daniels Mark . . 3 'van Kappel' Eline C . 4 Maurice Madelon M. . 5 Baldus Marc . . stop_ _Journal_abbreviation 'Chem. Comm.' _Journal_name_full 'Chemical communications (Cambridge, England)' _Journal_volume 54 _Journal_issue 32 _Journal_ISSN 1364-548X _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 3959 _Page_last 3962 _Year 2018 _Details . loop_ _Keyword Axin 'DIX domain' 'solid-state NMR' 'wnt signalling' stop_ save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name 'Axin DIX domain' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'Axin DIX domain, unit 1' $human_Axin_DIX_domain 'Axin DIX domain, unit 2' $human_Axin_DIX_domain stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state ? _System_paramagnetic no _System_thiol_state . loop_ _Biological_function 'Wnt signalling and puncta formation' stop_ _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_human_Axin_DIX_domain _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common human_Axin_DIX_domain _Molecular_mass . _Mol_thiol_state 'not reported' loop_ _Biological_function 'Wnt signalling' stop_ _Details 'The assignment covers residues 778-862. There is a HIS-tag and a TEV cleavage site at the N terminus.' ############################## # Polymer residue sequence # ############################## _Residue_count 96 _Mol_residue_sequence ; HHHHHENLYFQQPCDSIVVA YYFCGEPIPYRTLVRGRAVT LGQFKELLTKKGSYRYYFKK VSDEFDCGVVFEEVREDEAV LPVFEEKIIGKVEKVD ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 767 HIS 2 768 HIS 3 769 HIS 4 770 HIS 5 771 HIS 6 772 GLU 7 773 ASN 8 774 LEU 9 775 TYR 10 776 PHE 11 777 GLN 12 778 GLN 13 779 PRO 14 780 CYS 15 781 ASP 16 782 SER 17 783 ILE 18 784 VAL 19 785 VAL 20 786 ALA 21 787 TYR 22 788 TYR 23 789 PHE 24 790 CYS 25 791 GLY 26 792 GLU 27 793 PRO 28 794 ILE 29 795 PRO 30 796 TYR 31 797 ARG 32 798 THR 33 799 LEU 34 800 VAL 35 801 ARG 36 802 GLY 37 803 ARG 38 804 ALA 39 805 VAL 40 806 THR 41 807 LEU 42 808 GLY 43 809 GLN 44 810 PHE 45 811 LYS 46 812 GLU 47 813 LEU 48 814 LEU 49 815 THR 50 816 LYS 51 817 LYS 52 818 GLY 53 819 SER 54 820 TYR 55 821 ARG 56 822 TYR 57 823 TYR 58 824 PHE 59 825 LYS 60 826 LYS 61 827 VAL 62 828 SER 63 829 ASP 64 830 GLU 65 831 PHE 66 832 ASP 67 833 CYS 68 834 GLY 69 835 VAL 70 836 VAL 71 837 PHE 72 838 GLU 73 839 GLU 74 840 VAL 75 841 ARG 76 842 GLU 77 843 ASP 78 844 GLU 79 845 ALA 80 846 VAL 81 847 LEU 82 848 PRO 83 849 VAL 84 850 PHE 85 851 GLU 86 852 GLU 87 853 LYS 88 854 ILE 89 855 ILE 90 856 GLY 91 857 LYS 92 858 VAL 93 859 GLU 94 860 LYS 95 861 VAL 96 862 ASP stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date . save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $human_Axin_DIX_domain Human 9606 Eukaryota Metazoa Homo sapiens 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 $human_Axin_DIX_domain 'recombinant technology' . Escherichia coli Rosetta2 PET24 stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Saveframe_category sample _Sample_type solid _Details 'purified human Axin DIX domain' loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $human_Axin_DIX_domain solid mM '[U-100% 13C; U-100% 15N]' stop_ save_ ############################ # Computer software used # ############################ save_TOPSPIN _Saveframe_category software _Name TOPSPIN _Version . loop_ _Vendor _Address _Electronic_address 'Bruker Biospin' . . stop_ loop_ _Task collection processing stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model Avance _Field_strength 700 _Details . save_ save_spectrometer_2 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model Avance _Field_strength 950 _Details . save_ ############################# # NMR applied experiments # ############################# save_3D_NCACX_1 _Saveframe_category NMR_applied_experiment _Experiment_name '3D NCACX' _Sample_label $sample_1 save_ save_3D_CANCO_2 _Saveframe_category NMR_applied_experiment _Experiment_name '3D CANCO' _Sample_label $sample_1 save_ save_3D_NCOCX_3 _Saveframe_category NMR_applied_experiment _Experiment_name '3D NCOCX' _Sample_label $sample_1 save_ save_2D_CC_Spin_Diffusion_for_seqentials_4 _Saveframe_category NMR_applied_experiment _Experiment_name '2D CC Spin Diffusion for seqentials' _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' 20 . mM pH 8 . pH pressure 1 . atm temperature 278 2 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 carbons' ppm 40.48 external direct . 'separate tube (no insert) similar to the experimental sample tube' . 1.0 DSS N 15 'methyl carbons' ppm 40.48 external indirect . 'separate tube (no insert) similar to the experimental sample tube' . 0.4029799 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_ _Software_label $TOPSPIN stop_ loop_ _Experiment_label '3D NCACX' '3D CANCO' '3D NCOCX' '2D CC Spin Diffusion for seqentials' 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 'Axin DIX domain, unit 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 1 782 16 SER CA C 57.9 0.3 1 2 782 16 SER CB C 66.3 0.3 1 3 783 17 ILE CA C 60.0 0.3 1 4 783 17 ILE CB C 42.3 0.3 1 5 783 17 ILE CG1 C 28.8 0.3 1 6 783 17 ILE CG2 C 15.9 0.3 1 7 783 17 ILE CD1 C 14.5 0.3 1 8 783 17 ILE N N 122.6 0.3 1 9 784 18 VAL C C 174.2 0.3 1 10 784 18 VAL CA C 63.4 0.3 1 11 784 18 VAL CB C 32.1 0.3 1 12 784 18 VAL CG1 C 22.4 0.3 1 13 784 18 VAL CG2 C 21.5 0.3 1 14 784 18 VAL N N 128.2 0.3 1 15 785 19 VAL C C 173.8 0.3 1 16 785 19 VAL CA C 60.6 0.3 1 17 785 19 VAL CB C 33.9 0.3 1 18 785 19 VAL N N 127.6 0.3 1 19 786 20 ALA C C 176.5 0.3 1 20 786 20 ALA CA C 49.4 0.3 1 21 786 20 ALA CB C 23.2 0.3 1 22 786 20 ALA N N 129.8 0.3 1 23 787 21 TYR C C 172.9 0.3 1 24 787 21 TYR CA C 55.3 0.3 1 25 787 21 TYR CB C 39.5 0.3 1 26 787 21 TYR CZ C 157.8 0.3 1 27 787 21 TYR N N 113.5 0.3 1 28 788 22 TYR CA C 54.7 0.3 1 29 788 22 TYR CB C 41.8 0.3 1 30 788 22 TYR N N 119.1 0.3 1 31 793 27 PRO CA C 64.6 0.3 1 32 793 27 PRO CB C 32.4 0.3 1 33 793 27 PRO CG C 27.4 0.3 1 34 793 27 PRO CD C 51.0 0.3 1 35 793 27 PRO N N 137.1 0.3 1 36 794 28 ILE C C 174.9 0.3 1 37 794 28 ILE CA C 57.9 0.3 1 38 794 28 ILE CB C 37.9 0.3 1 39 794 28 ILE CG1 C 27.1 0.3 1 40 794 28 ILE CG2 C 17.3 0.3 1 41 794 28 ILE CD1 C 12.8 0.3 1 42 794 28 ILE N N 117.1 0.3 1 43 795 29 PRO C C 173.9 0.3 1 44 795 29 PRO CA C 62.1 0.3 1 45 795 29 PRO CB C 30.9 0.3 1 46 795 29 PRO CG C 25.3 0.3 1 47 795 29 PRO CD C 50.9 0.3 1 48 795 29 PRO N N 141.1 0.3 1 49 796 30 TYR CA C 57.2 0.3 1 50 796 30 TYR CB C 40.2 0.3 1 51 796 30 TYR N N 117.7 0.3 1 52 797 31 ARG C C 172.6 0.3 1 53 797 31 ARG CA C 57.5 0.3 1 54 797 31 ARG CG C 27.0 0.3 1 55 797 31 ARG N N 126.8 0.3 1 56 798 32 THR C C 171.8 0.3 1 57 798 32 THR CA C 59.8 0.3 1 58 798 32 THR CB C 69.6 0.3 1 59 798 32 THR CG2 C 20.5 0.3 1 60 798 32 THR N N 122.7 0.3 1 61 799 33 LEU C C 176.4 0.3 1 62 799 33 LEU CA C 54.0 0.3 1 63 799 33 LEU CB C 45.6 0.3 1 64 799 33 LEU N N 124.3 0.3 1 65 800 34 VAL C C 174.3 0.3 1 66 800 34 VAL CA C 60.5 0.3 1 67 800 34 VAL CB C 34.6 0.3 1 68 800 34 VAL N N 124.1 0.3 1 69 801 35 ARG C C 174.8 0.3 1 70 801 35 ARG CA C 53.5 0.3 1 71 801 35 ARG N N 125.3 0.3 1 72 804 38 ALA C C 175.1 0.3 1 73 804 38 ALA CA C 51.1 0.3 1 74 804 38 ALA CB C 20.6 0.3 1 75 804 38 ALA N N 122.2 0.3 1 76 805 39 VAL CA C 61.0 0.3 1 77 805 39 VAL CB C 34.7 0.3 1 78 805 39 VAL N N 123.4 0.3 1 79 806 40 THR C C 176.9 0.3 1 80 806 40 THR CA C 59.2 0.3 1 81 806 40 THR CB C 71.5 0.3 1 82 806 40 THR CG2 C 21.8 0.3 1 83 806 40 THR N N 115.6 0.3 1 84 807 41 LEU C C 179.1 0.3 1 85 807 41 LEU CA C 58.3 0.3 1 86 807 41 LEU CB C 39.5 0.3 1 87 807 41 LEU CD1 C 24.8 0.3 1 88 807 41 LEU CD2 C 22.3 0.3 1 89 807 41 LEU N N 120.9 0.3 1 90 808 42 GLY C C 176.7 0.3 1 91 808 42 GLY CA C 46.8 0.3 1 92 808 42 GLY N N 107.5 0.3 1 93 809 43 GLN C C 179.0 0.3 1 94 809 43 GLN CA C 58.7 0.3 1 95 809 43 GLN CB C 29.7 0.3 1 96 809 43 GLN CG C 35.1 0.3 1 97 809 43 GLN CD C 180.4 0.3 1 98 809 43 GLN N N 120.7 0.3 1 99 810 44 PHE C C 176.8 0.3 1 100 810 44 PHE CA C 61.4 0.3 1 101 810 44 PHE CB C 39.4 0.3 1 102 810 44 PHE CD1 C 131.5 0.3 1 103 810 44 PHE N N 122.5 0.3 1 104 811 45 LYS C C 179.0 0.3 1 105 811 45 LYS CA C 60.2 0.3 1 106 811 45 LYS CB C 32.8 0.3 1 107 811 45 LYS CG C 26.3 0.3 1 108 811 45 LYS CD C 30.4 0.3 1 109 811 45 LYS CE C 41.5 0.3 1 110 811 45 LYS N N 117.3 0.3 1 111 811 45 LYS NZ N 33.3 0.3 1 112 812 46 GLU C C 177.5 0.3 1 113 812 46 GLU CA C 57.5 0.3 1 114 812 46 GLU CB C 29.2 0.3 1 115 812 46 GLU CG C 36.2 0.3 1 116 812 46 GLU CD C 184.0 0.3 1 117 812 46 GLU N N 115.2 0.3 1 118 813 47 LEU C C 177.8 0.3 1 119 813 47 LEU CA C 55.2 0.3 1 120 813 47 LEU CB C 41.4 0.3 1 121 813 47 LEU CG C 25.3 0.3 1 122 813 47 LEU CD1 C 22.4 0.3 1 123 813 47 LEU N N 116.8 0.3 1 124 814 48 LEU CA C 54.5 0.3 1 125 814 48 LEU CG C 26.3 0.3 1 126 814 48 LEU N N 117.9 0.3 1 127 815 49 THR CA C 62.8 0.3 1 128 815 49 THR CB C 67.8 0.3 1 129 815 49 THR CG2 C 22.0 0.3 1 130 818 52 GLY C C 171.2 0.3 1 131 818 52 GLY CA C 44.8 0.3 1 132 818 52 GLY N N 110.0 0.3 1 133 819 53 SER C C 172.6 0.3 1 134 819 53 SER CA C 56.7 0.3 1 135 819 53 SER CB C 62.6 0.3 1 136 819 53 SER N N 116.5 0.3 1 137 820 54 TYR C C 175.4 0.3 1 138 820 54 TYR CA C 54.7 0.3 1 139 820 54 TYR CB C 41.4 0.3 1 140 820 54 TYR CG C 133.1 0.3 1 141 820 54 TYR N N 123.8 0.3 1 142 821 55 ARG C C 173.6 0.3 1 143 821 55 ARG CA C 55.0 0.3 1 144 821 55 ARG CB C 33.2 0.3 1 145 821 55 ARG CG C 27.2 0.3 1 146 821 55 ARG N N 119.1 0.3 1 147 822 56 TYR CA C 56.6 0.3 1 148 822 56 TYR CB C 41.0 0.3 1 149 822 56 TYR CE1 C 117.8 0.3 1 150 822 56 TYR CE2 C 116.8 0.3 1 151 822 56 TYR CZ C 157.4 0.3 1 152 822 56 TYR N N 119.5 0.3 1 153 823 57 TYR C C 174.6 0.3 1 154 823 57 TYR CA C 55.1 0.3 1 155 823 57 TYR CB C 41.5 0.3 1 156 823 57 TYR N N 119.4 0.3 1 157 824 58 PHE C C 174.7 0.3 1 158 824 58 PHE CA C 57.1 0.3 1 159 824 58 PHE CB C 43.2 0.3 1 160 824 58 PHE CD1 C 131.0 0.3 1 161 824 58 PHE N N 118.1 0.3 1 162 825 59 LYS C C 174.9 0.3 1 163 825 59 LYS CA C 57.6 0.3 1 164 825 59 LYS CB C 34.0 0.3 1 165 825 59 LYS CD C 30.5 0.3 1 166 825 59 LYS CE C 41.8 0.3 1 167 825 59 LYS N N 125.4 0.3 1 168 826 60 LYS C C 175.1 0.3 1 169 826 60 LYS CA C 54.6 0.3 1 170 826 60 LYS CB C 37.0 0.3 1 171 826 60 LYS CG C 23.8 0.3 1 172 826 60 LYS CD C 30.1 0.3 1 173 826 60 LYS CE C 42.0 0.3 1 174 826 60 LYS N N 121.3 0.3 1 175 827 61 VAL C C 176.4 0.3 1 176 827 61 VAL CA C 63.8 0.3 1 177 827 61 VAL CB C 32.0 0.3 1 178 827 61 VAL CG1 C 22.5 0.3 1 179 827 61 VAL CG2 C 21.4 0.3 1 180 827 61 VAL N N 124.4 0.3 1 181 828 62 SER C C 174.1 0.3 1 182 828 62 SER CA C 57.5 0.3 1 183 828 62 SER CB C 65.6 0.3 1 184 828 62 SER N N 119.0 0.3 1 185 829 63 ASP C C 176.3 0.3 1 186 829 63 ASP CA C 53.6 0.3 1 187 829 63 ASP CB C 40.5 0.3 1 188 829 63 ASP CG C 180.5 0.3 1 189 829 63 ASP N N 125.5 0.3 1 190 834 68 GLY C C 174.2 0.3 1 191 834 68 GLY CA C 47.0 0.3 1 192 834 68 GLY N N 110.0 0.3 1 193 835 69 VAL C C 171.4 0.3 1 194 835 69 VAL CA C 59.3 0.3 1 195 835 69 VAL CB C 35.5 0.3 1 196 835 69 VAL CG1 C 21.8 0.3 1 197 835 69 VAL N N 119.5 0.3 1 198 836 70 VAL C C 173.3 0.3 1 199 836 70 VAL CA C 58.4 0.3 1 200 836 70 VAL CB C 35.9 0.3 1 201 836 70 VAL CG1 C 21.5 0.3 1 202 836 70 VAL CG2 C 19.9 0.3 1 203 836 70 VAL N N 114.6 0.3 1 204 837 71 PHE C C 175.0 0.3 1 205 837 71 PHE CA C 58.4 0.3 1 206 837 71 PHE CB C 39.3 0.3 1 207 837 71 PHE CG C 141.7 0.3 1 208 837 71 PHE N N 122.3 0.3 1 209 838 72 GLU C C 176.8 0.3 1 210 838 72 GLU CA C 54.9 0.3 1 211 838 72 GLU CB C 32.2 0.3 1 212 838 72 GLU CG C 36.4 0.3 1 213 838 72 GLU CD C 183.6 0.3 1 214 838 72 GLU N N 126.4 0.3 1 215 839 73 GLU C C 176.8 0.3 1 216 839 73 GLU CA C 56.5 0.3 1 217 839 73 GLU CB C 28.3 0.3 1 218 839 73 GLU CG C 36.9 0.3 1 219 839 73 GLU CD C 183.3 0.3 1 220 839 73 GLU N N 129.4 0.3 1 221 840 74 VAL C C 175.0 0.3 1 222 840 74 VAL CA C 62.1 0.3 1 223 840 74 VAL CB C 34.4 0.3 1 224 840 74 VAL CG1 C 22.7 0.3 1 225 840 74 VAL CG2 C 21.6 0.3 1 226 840 74 VAL N N 128.7 0.3 1 227 841 75 ARG C C 175.9 0.3 1 228 841 75 ARG CA C 56.5 0.3 1 229 841 75 ARG CB C 34.2 0.3 1 230 841 75 ARG CG C 27.5 0.3 1 231 841 75 ARG CD C 43.5 0.3 1 232 841 75 ARG CZ C 159.7 0.3 1 233 841 75 ARG N N 123.6 0.3 1 234 842 76 GLU C C 176.1 0.3 1 235 842 76 GLU CA C 55.5 0.3 1 236 842 76 GLU CB C 30.0 0.3 1 237 842 76 GLU CG C 35.9 0.3 1 238 842 76 GLU CD C 183.6 0.3 1 239 842 76 GLU N N 120.6 0.3 1 240 843 77 ASP C C 177.8 0.3 1 241 843 77 ASP CA C 57.0 0.3 1 242 843 77 ASP CB C 40.1 0.3 1 243 843 77 ASP CG C 178.7 0.3 1 244 843 77 ASP N N 124.4 0.3 1 245 844 78 GLU C C 176.2 0.3 1 246 844 78 GLU CA C 56.3 0.3 1 247 844 78 GLU CB C 28.9 0.3 1 248 844 78 GLU CG C 36.0 0.3 1 249 844 78 GLU N N 114.4 0.3 1 250 845 79 ALA C C 176.5 0.3 1 251 845 79 ALA CA C 52.5 0.3 1 252 845 79 ALA CB C 19.4 0.3 1 253 845 79 ALA N N 123.8 0.3 1 254 846 80 VAL C C 177.0 0.3 1 255 846 80 VAL CA C 62.6 0.3 1 256 846 80 VAL CB C 31.7 0.3 1 257 846 80 VAL N N 121.6 0.3 1 258 847 81 LEU C C 174.5 0.3 1 259 847 81 LEU CA C 52.7 0.3 1 260 847 81 LEU CB C 38.7 0.3 1 261 847 81 LEU CG C 25.7 0.3 1 262 847 81 LEU CD1 C 22.1 0.3 1 263 847 81 LEU N N 128.4 0.3 1 264 848 82 PRO CA C 62.3 0.3 1 265 848 82 PRO CB C 32.2 0.3 1 266 848 82 PRO CG C 27.5 0.3 1 267 848 82 PRO CD C 49.5 0.3 1 268 848 82 PRO N N 134.6 0.3 1 269 849 83 VAL C C 175.6 0.3 1 270 849 83 VAL CA C 60.6 0.3 1 271 849 83 VAL CB C 33.8 0.3 1 272 849 83 VAL N N 118.4 0.3 1 273 850 84 PHE C C 173.7 0.3 1 274 850 84 PHE CA C 57.7 0.3 1 275 850 84 PHE CB C 42.1 0.3 1 276 850 84 PHE CG C 138.7 0.3 1 277 850 84 PHE CE1 C 131.9 0.3 1 278 850 84 PHE N N 130.9 0.3 1 279 851 85 GLU C C 176.0 0.3 1 280 851 85 GLU CA C 57.1 0.3 1 281 851 85 GLU CB C 26.3 0.3 1 282 851 85 GLU CG C 36.0 0.3 1 283 851 85 GLU CD C 184.5 0.3 1 284 851 85 GLU N N 125.8 0.3 1 285 852 86 GLU C C 174.8 0.3 1 286 852 86 GLU CA C 58.2 0.3 1 287 852 86 GLU CB C 27.8 0.3 1 288 852 86 GLU CG C 36.8 0.3 1 289 852 86 GLU CD C 184.9 0.3 1 290 852 86 GLU N N 106.8 0.3 1 291 853 87 LYS C C 173.3 0.3 1 292 853 87 LYS CA C 55.3 0.3 1 293 853 87 LYS CB C 36.4 0.3 1 294 853 87 LYS CG C 24.0 0.3 1 295 853 87 LYS CD C 27.9 0.3 1 296 853 87 LYS N N 120.6 0.3 1 297 854 88 ILE C C 175.3 0.3 1 298 854 88 ILE CA C 60.7 0.3 1 299 854 88 ILE CB C 39.2 0.3 1 300 854 88 ILE CG1 C 27.6 0.3 1 301 854 88 ILE CG2 C 18.4 0.3 1 302 854 88 ILE CD1 C 14.2 0.3 1 303 854 88 ILE N N 120.7 0.3 1 304 855 89 ILE C C 175.4 0.3 1 305 855 89 ILE CA C 58.9 0.3 1 306 855 89 ILE CB C 39.6 0.3 1 307 855 89 ILE CG1 C 26.9 0.3 1 308 855 89 ILE CG2 C 17.4 0.3 1 309 855 89 ILE CD1 C 13.6 0.3 1 310 855 89 ILE N N 127.5 0.3 1 311 856 90 GLY C C 172.7 0.3 1 312 856 90 GLY CA C 44.9 0.3 1 313 856 90 GLY N N 111.6 0.3 1 314 857 91 LYS C C 173.6 0.3 1 315 857 91 LYS CA C 56.4 0.3 1 316 857 91 LYS CB C 35.9 0.3 1 317 857 91 LYS CD C 29.3 0.3 1 318 857 91 LYS CE C 41.3 0.3 1 319 857 91 LYS N N 119.9 0.3 1 320 858 92 VAL C C 175.4 0.3 1 321 858 92 VAL CA C 60.9 0.3 1 322 858 92 VAL CB C 34.0 0.3 1 323 858 92 VAL N N 124.4 0.3 1 324 859 93 GLU C C 174.8 0.3 1 325 859 93 GLU CA C 53.7 0.3 1 326 859 93 GLU CB C 33.2 0.3 1 327 859 93 GLU CD C 180.5 0.3 1 328 859 93 GLU N N 125.7 0.3 1 329 860 94 LYS C C 176.1 0.3 1 330 860 94 LYS CA C 56.6 0.3 1 331 860 94 LYS CB C 33.8 0.3 1 332 860 94 LYS CG C 25.0 0.3 1 333 860 94 LYS CD C 29.0 0.3 1 334 860 94 LYS CE C 41.8 0.3 1 335 860 94 LYS N N 123.6 0.3 1 336 861 95 VAL C C 175.0 0.3 1 337 861 95 VAL CA C 62.3 0.3 1 338 861 95 VAL CB C 32.2 0.3 1 339 861 95 VAL CG1 C 20.9 0.3 1 340 861 95 VAL N N 123.5 0.3 1 stop_ save_