data_18608 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Backbone resonance assignment of ASC pyrin domain ; _BMRB_accession_number 18608 _BMRB_flat_file_name bmr18608.str _Entry_type original _Submission_date 2012-07-23 _Accession_date 2012-07-23 _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 Vajjhala Parimala R. . 2 Mirams Ruth E. . 3 Hill Justine M. . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 88 "13C chemical shifts" 266 "15N chemical shifts" 89 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2013-02-18 update BMRB 'update entry citation' 2012-10-18 original author 'original release' stop_ save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title 'Multiple binding sites on the pyrin domain of ASC protein allow self-association and interaction with NLRP3 protein.' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 23066025 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Vajjhala Parimala R. . 2 Mirams Ruth E. . 3 Hill Justine M. . stop_ _Journal_abbreviation 'J. Biol. Chem.' _Journal_name_full 'The Journal of biological chemistry' _Journal_volume 287 _Journal_issue 50 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 41732 _Page_last 41743 _Year 2012 _Details . loop_ _Keyword 'death domain' Inflammasome 'NOD-like receptor' 'protein-protein interaction' stop_ save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name 'ASC PYD' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'ASC PYD' $ASC_PYD 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_ASC_PYD _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common ASC_PYD _Molecular_mass . _Mol_thiol_state 'all free' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 108 _Mol_residue_sequence ; MRGSHHHHHHGSMGRARDAI LDALENLTAEELKKFKLKLL SVPLREGYGRIPRGALLSMD SLDLTDKLVSFYLETYGAEL TANVLRDMGLQEMAGQLQAA THQGSGAA ; loop_ _Residue_seq_code _Residue_label 1 MET 2 ARG 3 GLY 4 SER 5 HIS 6 HIS 7 HIS 8 HIS 9 HIS 10 HIS 11 GLY 12 SER 13 MET 14 GLY 15 ARG 16 ALA 17 ARG 18 ASP 19 ALA 20 ILE 21 LEU 22 ASP 23 ALA 24 LEU 25 GLU 26 ASN 27 LEU 28 THR 29 ALA 30 GLU 31 GLU 32 LEU 33 LYS 34 LYS 35 PHE 36 LYS 37 LEU 38 LYS 39 LEU 40 LEU 41 SER 42 VAL 43 PRO 44 LEU 45 ARG 46 GLU 47 GLY 48 TYR 49 GLY 50 ARG 51 ILE 52 PRO 53 ARG 54 GLY 55 ALA 56 LEU 57 LEU 58 SER 59 MET 60 ASP 61 SER 62 LEU 63 ASP 64 LEU 65 THR 66 ASP 67 LYS 68 LEU 69 VAL 70 SER 71 PHE 72 TYR 73 LEU 74 GLU 75 THR 76 TYR 77 GLY 78 ALA 79 GLU 80 LEU 81 THR 82 ALA 83 ASN 84 VAL 85 LEU 86 ARG 87 ASP 88 MET 89 GLY 90 LEU 91 GLN 92 GLU 93 MET 94 ALA 95 GLY 96 GLN 97 LEU 98 GLN 99 ALA 100 ALA 101 THR 102 HIS 103 GLN 104 GLY 105 SER 106 GLY 107 ALA 108 ALA stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-06-02 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 1UCP "Nmr Structure Of The Pyrin Domain Of Human Asc" 84.26 91 98.90 100.00 3.94e-56 PDB 3J63 "Unified Assembly Mechanism Of Asc-dependent Inflammasomes" 84.26 91 98.90 100.00 3.94e-56 DBJ BAA87339 "apoptosis-associated speck-like protein containing a CARD [Homo sapiens]" 88.89 195 98.96 100.00 7.70e-59 DBJ BAG37041 "unnamed protein product [Homo sapiens]" 88.89 195 97.92 100.00 3.33e-58 DBJ BAG73625 "PYD and CARD domain containing [synthetic construct]" 88.89 195 98.96 100.00 7.70e-59 GB AAF99665 "target of methylation-induced silencing-1 [Homo sapiens]" 85.19 176 98.91 100.00 2.15e-56 GB AAG01187 "target of methylation-induced silencing 1 [Homo sapiens]" 88.89 195 98.96 100.00 7.70e-59 GB AAG01188 "target of methylation-induced silencing 1 [Homo sapiens]" 88.89 195 98.96 100.00 7.70e-59 GB AAG30286 "PYCARD [Homo sapiens]" 88.89 195 98.96 100.00 7.70e-59 GB AAH13569 "PYCARD protein, partial [Homo sapiens]" 86.11 192 98.92 100.00 2.05e-56 REF NP_037390 "apoptosis-associated speck-like protein containing a CARD isoform a [Homo sapiens]" 88.89 195 98.96 100.00 7.70e-59 REF NP_660183 "apoptosis-associated speck-like protein containing a CARD isoform b [Homo sapiens]" 85.19 176 98.91 100.00 2.15e-56 REF XP_001158625 "PREDICTED: apoptosis-associated speck-like protein containing a CARD isoform X2 [Pan troglodytes]" 85.19 176 98.91 100.00 1.77e-56 REF XP_001158687 "PREDICTED: apoptosis-associated speck-like protein containing a CARD isoform X1 [Pan troglodytes]" 87.96 195 98.95 100.00 2.80e-58 REF XP_003280507 "PREDICTED: LOW QUALITY PROTEIN: apoptosis-associated speck-like protein containing a CARD [Nomascus leucogenys]" 88.89 195 97.92 98.96 4.14e-58 SP Q9ULZ3 "RecName: Full=Apoptosis-associated speck-like protein containing a CARD; Short=hASC; AltName: Full=Caspase recruitment domain-c" 88.89 195 98.96 100.00 7.70e-59 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $ASC_PYD 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 $ASC_PYD 'recombinant technology' . Escherichia coli . pQE-30 stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Saveframe_category sample _Sample_type solution _Details 'pH 4.0' loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $ASC_PYD 0.3 mM '[U-99% 15N]' 'sodium phosphate' 50 mM 'natural abundance' 'sodium chloride' 150 mM 'natural abundance' D2O 10 % '[U-99% 2H]' H2O 90 % 'natural abundance' stop_ save_ save_sample_2 _Saveframe_category sample _Sample_type solution _Details 'pH 4.0' loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $ASC_PYD 0.9 mM '[U-99% 13C; U-99% 15N]' 'sodium phosphate' 50 mM 'natural abundance' 'sodium chloride' 150 mM 'natural abundance' D2O 10 % '[U-99% 2H]' H2O 90 % 'natural abundance' stop_ save_ ############################ # Computer software used # ############################ save_TOPSPIN _Saveframe_category software _Name TOPSPIN _Version . loop_ _Vendor _Address _Electronic_address 'Bruker Biospin' . . stop_ loop_ _Task collection stop_ _Details . save_ 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_NMRDraw _Saveframe_category software _Name NMRDraw _Version . loop_ _Vendor _Address _Electronic_address 'Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax' . . stop_ loop_ _Task processing stop_ _Details . save_ save_Analysis _Saveframe_category software _Name Analysis _Version . loop_ _Vendor _Address _Electronic_address CCPN . . stop_ loop_ _Task processing stop_ _Details . save_ save_HADDOCK _Saveframe_category software _Name HADDOCK _Version . loop_ _Vendor _Address _Electronic_address 'Alexandre Bonvin' . . stop_ loop_ _Task 'structure solution' stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model Avance _Field_strength 750 _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_HNCO_2 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCO' _Sample_label $sample_2 save_ save_3D_HNCACB_3 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCACB' _Sample_label $sample_2 save_ save_3D_HN(CA)CO_4 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HN(CA)CO' _Sample_label $sample_2 save_ save_3D_CBCA(CO)NH_5 _Saveframe_category NMR_applied_experiment _Experiment_name '3D CBCA(CO)NH' _Sample_label $sample_2 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' 150 . mM pH 4 . 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 na indirect . . . 0.251449530 DSS H 1 'methyl protons' ppm 0.00 internal direct . . . 1.000000000 DSS N 15 'methyl protons' ppm 0.00 na 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 HNCO' '3D HNCACB' '3D HN(CA)CO' '3D CBCA(CO)NH' stop_ loop_ _Sample_label $sample_1 $sample_2 stop_ _Sample_conditions_label $sample_conditions_1 _Chem_shift_reference_set_label $chemical_shift_reference_1 _Mol_system_component_name 'ASC PYD' _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 MET C C 176.750 0.014 1 2 1 1 MET CA C 56.064 0.103 1 3 1 1 MET CB C 32.840 0.113 1 4 1 1 MET N N 122.744 0.012 1 5 3 2 ARG H H 8.267 0.004 1 6 3 2 ARG C C 178.531 0.011 1 7 3 2 ARG CA C 57.967 0.033 1 8 3 2 ARG CB C 30.527 0.060 1 9 3 2 ARG N N 120.405 0.012 1 10 2 3 GLY H H 8.569 0.002 1 11 2 3 GLY C C 174.400 0.021 1 12 2 3 GLY CA C 45.809 0.060 1 13 2 3 GLY N N 110.500 0.009 1 14 4 16 ALA H H 8.561 0.002 1 15 4 16 ALA C C 178.864 0.015 1 16 4 16 ALA CA C 55.583 0.055 1 17 4 16 ALA CB C 18.275 0.068 1 18 4 16 ALA N N 123.312 0.010 1 19 5 17 ARG H H 8.479 0.002 1 20 5 17 ARG C C 177.589 0.015 1 21 5 17 ARG CA C 60.285 0.087 1 22 5 17 ARG CB C 29.683 0.049 1 23 5 17 ARG N N 117.242 0.008 1 24 6 18 ASP H H 7.912 0.003 1 25 6 18 ASP C C 177.294 0.011 1 26 6 18 ASP CA C 56.738 0.022 1 27 6 18 ASP CB C 39.385 0.093 1 28 6 18 ASP N N 117.208 0.013 1 29 7 19 ALA H H 7.787 0.005 1 30 7 19 ALA C C 180.531 0.021 1 31 7 19 ALA CA C 55.043 0.014 1 32 7 19 ALA CB C 18.645 0.043 1 33 7 19 ALA N N 122.527 0.002 1 34 8 20 ILE H H 8.234 0.006 1 35 8 20 ILE C C 176.620 0.017 1 36 8 20 ILE CA C 66.350 0.090 1 37 8 20 ILE CB C 38.799 0.082 1 38 8 20 ILE N N 120.765 0.013 1 39 9 21 LEU H H 8.065 0.004 1 40 9 21 LEU C C 178.367 0.013 1 41 9 21 LEU CA C 57.916 0.030 1 42 9 21 LEU CB C 41.693 0.059 1 43 9 21 LEU N N 119.915 0.006 1 44 10 22 ASP H H 8.101 0.003 1 45 10 22 ASP C C 177.679 0.012 1 46 10 22 ASP CA C 56.372 0.003 1 47 10 22 ASP CB C 38.870 0.132 1 48 10 22 ASP N N 115.770 0.052 1 49 11 23 ALA H H 7.468 0.009 1 50 11 23 ALA C C 179.252 0.013 1 51 11 23 ALA CA C 54.915 0.010 1 52 11 23 ALA CB C 17.998 0.078 1 53 11 23 ALA N N 120.275 0.012 1 54 12 24 LEU H H 8.352 0.006 1 55 12 24 LEU C C 180.709 0.016 1 56 12 24 LEU CA C 57.853 0.048 1 57 12 24 LEU CB C 41.331 0.083 1 58 12 24 LEU N N 114.850 0.004 1 59 13 25 GLU H H 8.879 0.004 1 60 13 25 GLU C C 176.331 0.009 1 61 13 25 GLU CA C 57.866 0.050 1 62 13 25 GLU CB C 27.930 0.043 1 63 13 25 GLU N N 116.432 0.006 1 64 14 26 ASN H H 7.386 0.004 1 65 14 26 ASN C C 175.212 0.001 1 66 14 26 ASN CA C 53.536 0.014 1 67 14 26 ASN CB C 39.843 0.052 1 68 14 26 ASN N N 116.242 0.006 1 69 15 27 LEU H H 7.004 0.009 1 70 15 27 LEU C C 178.521 0.012 1 71 15 27 LEU CA C 54.663 0.007 1 72 15 27 LEU CB C 41.377 0.078 1 73 15 27 LEU N N 119.530 0.014 1 74 16 28 THR H H 8.227 0.004 1 75 16 28 THR C C 174.659 0.032 1 76 16 28 THR CA C 61.094 0.021 1 77 16 28 THR CB C 70.847 0.015 1 78 16 28 THR N N 112.969 0.025 1 79 17 29 ALA H H 9.005 0.002 1 80 17 29 ALA C C 181.494 0.015 1 81 17 29 ALA CA C 56.027 0.068 1 82 17 29 ALA CB C 17.775 0.057 1 83 17 29 ALA N N 123.633 0.011 1 84 18 30 GLU H H 8.665 0.003 1 85 18 30 GLU C C 179.364 0.009 1 86 18 30 GLU CA C 59.283 0.041 1 87 18 30 GLU CB C 28.685 0.065 1 88 18 30 GLU N N 117.655 0.015 1 89 19 31 GLU H H 7.750 0.002 1 90 19 31 GLU C C 178.117 0.037 1 91 19 31 GLU CA C 58.454 0.089 1 92 19 31 GLU CB C 29.719 0.047 1 93 19 31 GLU N N 119.351 0.056 1 94 20 32 LEU H H 9.123 0.004 1 95 20 32 LEU C C 178.500 0.019 1 96 20 32 LEU CA C 58.114 0.021 1 97 20 32 LEU CB C 40.596 0.073 1 98 20 32 LEU N N 122.035 0.015 1 99 21 33 LYS H H 7.632 0.009 1 100 21 33 LYS C C 178.535 0.013 1 101 21 33 LYS CA C 60.446 0.089 1 102 21 33 LYS CB C 32.100 0.063 1 103 21 33 LYS N N 118.817 0.007 1 104 22 34 LYS H H 7.705 0.008 1 105 22 34 LYS C C 178.125 0.016 1 106 22 34 LYS CA C 59.924 0.110 1 107 22 34 LYS CB C 32.491 0.043 1 108 22 34 LYS N N 118.806 0.061 1 109 23 35 PHE H H 8.896 0.007 1 110 23 35 PHE C C 176.720 0.015 1 111 23 35 PHE CA C 61.643 0.086 1 112 23 35 PHE CB C 39.554 0.058 1 113 23 35 PHE N N 122.317 0.011 1 114 24 36 LYS H H 8.152 0.007 1 115 24 36 LYS C C 177.674 0.013 1 116 24 36 LYS CA C 60.669 0.016 1 117 24 36 LYS CB C 33.346 0.063 1 118 24 36 LYS N N 117.291 0.009 1 119 25 37 LEU H H 7.772 0.010 1 120 25 37 LEU C C 181.593 0.018 1 121 25 37 LEU CA C 57.954 0.002 1 122 25 37 LEU CB C 41.329 0.031 1 123 25 37 LEU N N 115.906 0.015 1 124 26 38 LYS H H 8.245 0.009 1 125 26 38 LYS C C 179.399 0.024 1 126 26 38 LYS CA C 57.945 0.010 1 127 26 38 LYS CB C 31.844 0.062 1 128 26 38 LYS N N 120.805 0.008 1 129 27 39 LEU H H 7.989 0.008 1 130 27 39 LEU C C 178.514 0.030 1 131 27 39 LEU CA C 57.269 0.111 1 132 27 39 LEU CB C 41.320 0.087 1 133 27 39 LEU N N 120.816 0.006 1 134 28 40 LEU H H 7.389 0.010 1 135 28 40 LEU C C 176.972 0.013 1 136 28 40 LEU CA C 56.216 0.055 1 137 28 40 LEU CB C 41.768 0.056 1 138 28 40 LEU N N 116.248 0.002 1 139 29 41 SER H H 7.565 0.008 1 140 29 41 SER C C 174.985 0.001 1 141 29 41 SER CA C 58.119 0.048 1 142 29 41 SER CB C 65.544 0.057 1 143 29 41 SER N N 110.955 0.005 1 144 30 42 VAL H H 7.921 0.002 1 145 30 42 VAL C C 173.221 0.000 1 146 30 42 VAL CA C 60.348 0.000 1 147 30 42 VAL CB C 31.794 0.000 1 148 30 42 VAL N N 123.936 0.031 1 149 31 43 PRO C C 176.015 0.000 1 150 31 43 PRO CA C 63.779 0.000 1 151 31 43 PRO CB C 31.818 0.000 1 152 32 44 LEU H H 8.301 0.001 1 153 32 44 LEU C C 178.028 0.011 1 154 32 44 LEU CA C 52.816 0.116 1 155 32 44 LEU CB C 46.120 0.015 1 156 32 44 LEU N N 122.718 0.130 1 157 33 45 ARG H H 7.673 0.003 1 158 33 45 ARG C C 175.999 0.013 1 159 33 45 ARG CA C 56.528 0.027 1 160 33 45 ARG CB C 31.676 0.070 1 161 33 45 ARG N N 121.812 0.012 1 162 34 46 GLU H H 8.537 0.001 1 163 34 46 GLU C C 176.854 0.013 1 164 34 46 GLU CA C 57.900 0.034 1 165 34 46 GLU CB C 28.528 0.058 1 166 34 46 GLU N N 122.354 0.010 1 167 35 47 GLY H H 8.774 0.003 1 168 35 47 GLY C C 174.154 0.016 1 169 35 47 GLY CA C 44.834 0.059 1 170 35 47 GLY N N 111.611 0.011 1 171 36 48 TYR H H 7.533 0.007 1 172 36 48 TYR C C 175.745 0.015 1 173 36 48 TYR CA C 58.167 0.049 1 174 36 48 TYR CB C 40.739 0.079 1 175 36 48 TYR N N 118.280 0.011 1 176 37 49 GLY H H 9.011 0.003 1 177 37 49 GLY C C 172.468 0.014 1 178 37 49 GLY CA C 43.671 0.069 1 179 37 49 GLY N N 109.000 0.009 1 180 38 50 ARG H H 8.537 0.001 1 181 38 50 ARG C C 176.076 0.012 1 182 38 50 ARG CA C 53.987 0.070 1 183 38 50 ARG CB C 31.374 0.067 1 184 38 50 ARG N N 118.620 0.003 1 185 39 51 ILE H H 8.249 0.003 1 186 39 51 ILE C C 173.778 0.000 1 187 39 51 ILE CA C 60.030 0.000 1 188 39 51 ILE CB C 38.862 0.000 1 189 39 51 ILE N N 128.302 0.031 1 190 40 52 PRO C C 177.505 0.000 1 191 40 52 PRO CA C 63.339 0.000 1 192 40 52 PRO CB C 32.491 0.000 1 193 41 53 ARG H H 8.390 0.003 1 194 41 53 ARG C C 177.594 0.018 1 195 41 53 ARG CA C 60.271 0.094 1 196 41 53 ARG CB C 30.681 0.064 1 197 41 53 ARG N N 124.447 0.014 1 198 42 54 GLY H H 8.842 0.007 1 199 42 54 GLY C C 176.236 0.014 1 200 42 54 GLY CA C 46.956 0.037 1 201 42 54 GLY N N 105.185 0.008 1 202 43 55 ALA H H 7.288 0.003 1 203 43 55 ALA C C 179.268 0.015 1 204 43 55 ALA CA C 53.720 0.001 1 205 43 55 ALA CB C 18.362 0.068 1 206 43 55 ALA N N 122.304 0.003 1 207 44 56 LEU H H 7.959 0.006 1 208 44 56 LEU C C 179.701 0.016 1 209 44 56 LEU CA C 57.516 0.125 1 210 44 56 LEU CB C 43.161 0.078 1 211 44 56 LEU N N 117.500 0.004 1 212 45 57 LEU H H 7.960 0.008 1 213 45 57 LEU C C 179.264 0.009 1 214 45 57 LEU CA C 58.849 0.110 1 215 45 57 LEU CB C 40.960 0.082 1 216 45 57 LEU N N 115.806 0.007 1 217 46 58 SER H H 7.705 0.006 1 218 46 58 SER C C 175.071 0.011 1 219 46 58 SER CA C 58.943 0.088 1 220 46 58 SER CB C 64.099 0.066 1 221 46 58 SER N N 112.489 0.004 1 222 47 59 MET H H 7.313 0.007 1 223 47 59 MET C C 176.744 0.012 1 224 47 59 MET CA C 58.013 0.025 1 225 47 59 MET CB C 34.587 0.093 1 226 47 59 MET N N 120.347 0.005 1 227 48 60 ASP H H 8.765 0.003 1 228 48 60 ASP C C 174.669 0.024 1 229 48 60 ASP CA C 51.140 0.089 1 230 48 60 ASP CB C 38.832 0.070 1 231 48 60 ASP N N 121.758 0.016 1 232 49 61 SER H H 8.658 0.004 1 233 49 61 SER C C 179.309 0.013 1 234 49 61 SER CA C 56.276 0.012 1 235 49 61 SER CB C 18.190 0.038 1 236 49 61 SER N N 118.807 0.004 1 237 50 62 LEU H H 7.986 0.003 1 238 50 62 LEU C C 177.826 0.012 1 239 50 62 LEU CA C 58.710 0.156 1 240 50 62 LEU CB C 41.479 0.071 1 241 50 62 LEU N N 121.651 0.022 1 242 51 63 ASP H H 8.275 0.006 1 243 51 63 ASP C C 179.025 0.002 1 244 51 63 ASP CA C 57.035 0.081 1 245 51 63 ASP CB C 39.323 0.082 1 246 51 63 ASP N N 118.718 0.025 1 247 52 64 LEU H H 8.795 0.002 1 248 52 64 LEU C C 177.745 0.018 1 249 52 64 LEU CA C 57.668 0.031 1 250 52 64 LEU CB C 41.961 0.039 1 251 52 64 LEU N N 120.891 0.042 1 252 53 65 THR H H 8.067 0.007 1 253 53 65 THR C C 175.660 0.000 1 254 53 65 THR CA C 69.125 0.000 1 255 53 65 THR CB C 68.077 0.029 1 256 53 65 THR N N 118.045 0.017 1 257 54 66 ASP H H 7.816 0.004 1 258 54 66 ASP C C 178.757 0.016 1 259 54 66 ASP CA C 56.794 0.053 1 260 54 66 ASP CB C 38.817 0.082 1 261 54 66 ASP N N 118.147 0.006 1 262 55 67 LYS H H 8.434 0.006 1 263 55 67 LYS C C 178.301 0.021 1 264 55 67 LYS CA C 57.686 0.001 1 265 55 67 LYS CB C 31.425 0.069 1 266 55 67 LYS N N 122.775 0.014 1 267 56 68 LEU H H 9.047 0.005 1 268 56 68 LEU C C 179.342 0.016 1 269 56 68 LEU CA C 59.002 0.093 1 270 56 68 LEU CB C 42.637 0.086 1 271 56 68 LEU N N 120.705 0.007 1 272 57 69 VAL H H 7.997 0.007 1 273 57 69 VAL C C 178.642 0.021 1 274 57 69 VAL CA C 65.906 0.058 1 275 57 69 VAL CB C 31.296 0.081 1 276 57 69 VAL N N 115.153 0.031 1 277 58 70 SER H H 8.281 0.003 1 278 58 70 SER C C 175.713 0.000 1 279 58 70 SER CA C 61.563 0.074 1 280 58 70 SER CB C 63.616 0.363 1 281 58 70 SER N N 116.913 0.016 1 282 59 71 PHE H H 8.555 0.005 1 283 59 71 PHE C C 178.008 0.008 1 284 59 71 PHE CA C 60.843 0.078 1 285 59 71 PHE CB C 39.022 0.038 1 286 59 71 PHE N N 120.078 0.014 1 287 60 72 TYR H H 8.090 0.006 1 288 60 72 TYR C C 175.605 0.027 1 289 60 72 TYR CA C 58.000 0.018 1 290 60 72 TYR CB C 38.863 0.019 1 291 60 72 TYR N N 115.787 0.016 1 292 61 73 LEU H H 7.463 0.006 1 293 61 73 LEU C C 176.838 0.014 1 294 61 73 LEU CA C 57.327 0.132 1 295 61 73 LEU CB C 40.510 0.078 1 296 61 73 LEU N N 112.119 0.005 1 297 62 74 GLU H H 8.608 0.003 1 298 62 74 GLU C C 177.607 0.034 1 299 62 74 GLU CA C 61.284 0.058 1 300 62 74 GLU CB C 29.399 0.051 1 301 62 74 GLU N N 116.196 0.004 1 302 63 75 THR H H 8.057 0.002 1 303 63 75 THR C C 176.678 0.012 1 304 63 75 THR CA C 65.924 0.004 1 305 63 75 THR CB C 67.884 0.071 1 306 63 75 THR N N 112.562 0.034 1 307 64 76 TYR H H 8.772 0.003 1 308 64 76 TYR C C 177.183 0.028 1 309 64 76 TYR CA C 58.538 0.097 1 310 64 76 TYR CB C 35.957 0.065 1 311 64 76 TYR N N 122.726 0.005 1 312 65 77 GLY H H 8.024 0.007 1 313 65 77 GLY C C 176.241 0.004 1 314 65 77 GLY CA C 47.831 0.030 1 315 65 77 GLY N N 106.851 0.021 1 316 66 78 ALA H H 7.774 0.005 1 317 66 78 ALA C C 178.815 0.011 1 318 66 78 ALA CA C 55.638 0.068 1 319 66 78 ALA CB C 18.169 0.065 1 320 66 78 ALA N N 124.234 0.015 1 321 67 79 GLU H H 7.815 0.007 1 322 67 79 GLU C C 178.440 0.015 1 323 67 79 GLU CA C 59.306 0.040 1 324 67 79 GLU CB C 28.945 0.065 1 325 67 79 GLU N N 120.827 0.027 1 326 68 80 LEU H H 9.023 0.005 1 327 68 80 LEU C C 178.651 0.010 1 328 68 80 LEU CA C 57.861 0.036 1 329 68 80 LEU CB C 42.006 0.059 1 330 68 80 LEU N N 121.196 0.006 1 331 69 81 THR H H 7.547 0.006 1 332 69 81 THR C C 175.966 0.000 1 333 69 81 THR CA C 68.788 0.000 1 334 69 81 THR CB C 67.814 0.026 1 335 69 81 THR N N 114.535 0.009 1 336 70 82 ALA H H 8.146 0.010 1 337 70 82 ALA C C 178.513 0.019 1 338 70 82 ALA CA C 56.039 0.078 1 339 70 82 ALA CB C 17.822 0.071 1 340 70 82 ALA N N 122.272 0.014 1 341 71 83 ASN H H 8.419 0.005 1 342 71 83 ASN C C 178.290 0.020 1 343 71 83 ASN CA C 56.188 0.000 1 344 71 83 ASN CB C 37.805 0.076 1 345 71 83 ASN N N 117.613 0.013 1 346 72 84 VAL H H 8.461 0.005 1 347 72 84 VAL C C 178.218 0.026 1 348 72 84 VAL CA C 67.400 0.073 1 349 72 84 VAL CB C 30.896 0.084 1 350 72 84 VAL N N 121.869 0.007 1 351 73 85 LEU H H 8.411 0.007 1 352 73 85 LEU C C 179.847 0.029 1 353 73 85 LEU CA C 58.411 0.072 1 354 73 85 LEU CB C 41.285 0.114 1 355 73 85 LEU N N 118.655 0.007 1 356 74 86 ARG H H 8.538 0.004 1 357 74 86 ARG C C 180.316 0.011 1 358 74 86 ARG CA C 60.967 0.013 1 359 74 86 ARG CB C 29.319 0.033 1 360 74 86 ARG N N 119.418 0.006 1 361 75 87 ASP H H 8.213 0.006 1 362 75 87 ASP C C 177.436 0.028 1 363 75 87 ASP CA C 56.314 0.039 1 364 75 87 ASP CB C 39.159 0.081 1 365 75 87 ASP N N 121.889 0.013 1 366 76 88 MET H H 7.925 0.004 1 367 76 88 MET C C 175.846 0.013 1 368 76 88 MET CA C 56.674 0.014 1 369 76 88 MET CB C 34.981 0.064 1 370 76 88 MET N N 116.850 0.006 1 371 77 89 GLY H H 8.017 0.006 1 372 77 89 GLY C C 174.824 0.017 1 373 77 89 GLY CA C 45.411 0.067 1 374 77 89 GLY N N 107.441 0.007 1 375 78 90 LEU H H 8.129 0.006 1 376 78 90 LEU C C 177.182 0.016 1 377 78 90 LEU CA C 52.932 0.081 1 378 78 90 LEU CB C 38.839 0.077 1 379 78 90 LEU N N 124.735 0.003 1 380 79 91 GLN H H 7.889 0.007 1 381 79 91 GLN C C 178.936 0.006 1 382 79 91 GLN CA C 59.864 0.057 1 383 79 91 GLN CB C 28.027 0.017 1 384 79 91 GLN N N 118.987 0.012 1 385 80 92 GLU H H 8.805 0.009 1 386 80 92 GLU C C 179.326 0.009 1 387 80 92 GLU CA C 59.487 0.065 1 388 80 92 GLU CB C 27.538 0.096 1 389 80 92 GLU N N 121.241 0.008 1 390 81 93 MET H H 8.108 0.003 1 391 81 93 MET C C 179.069 0.005 1 392 81 93 MET CA C 59.092 0.128 1 393 81 93 MET CB C 33.470 0.092 1 394 81 93 MET N N 119.918 0.013 1 395 82 94 ALA H H 8.112 0.005 1 396 82 94 ALA C C 179.167 0.007 1 397 82 94 ALA CA C 55.490 0.063 1 398 82 94 ALA CB C 19.150 0.051 1 399 82 94 ALA N N 121.548 0.018 1 400 83 95 GLY H H 8.331 0.005 1 401 83 95 GLY C C 177.101 0.014 1 402 83 95 GLY CA C 47.087 0.055 1 403 83 95 GLY N N 105.061 0.009 1 404 84 96 GLN H H 7.991 0.007 1 405 84 96 GLN C C 178.419 0.021 1 406 84 96 GLN CA C 58.558 0.084 1 407 84 96 GLN CB C 28.186 0.041 1 408 84 96 GLN N N 122.340 0.007 1 409 85 97 LEU H H 7.718 0.006 1 410 85 97 LEU C C 179.202 0.008 1 411 85 97 LEU CA C 58.107 0.076 1 412 85 97 LEU CB C 41.767 0.074 1 413 85 97 LEU N N 122.573 0.021 1 414 86 98 GLN H H 8.346 0.002 1 415 86 98 GLN C C 178.557 0.015 1 416 86 98 GLN CA C 59.202 0.078 1 417 86 98 GLN CB C 28.590 0.059 1 418 86 98 GLN N N 119.184 0.062 1 419 87 99 ALA H H 8.083 0.003 1 420 87 99 ALA C C 179.899 0.013 1 421 87 99 ALA CA C 54.805 0.038 1 422 87 99 ALA CB C 17.919 0.043 1 423 87 99 ALA N N 121.549 0.007 1 424 88 100 ALA H H 7.883 0.006 1 425 88 100 ALA C C 178.916 0.028 1 426 88 100 ALA CA C 54.020 0.079 1 427 88 100 ALA CB C 19.055 0.041 1 428 88 100 ALA N N 119.409 0.013 1 429 89 101 THR H H 7.542 0.008 1 430 89 101 THR C C 174.419 0.018 1 431 89 101 THR CA C 62.041 0.111 1 432 89 101 THR CB C 69.712 0.085 1 433 89 101 THR N N 105.387 0.027 1 434 90 102 HIS H H 7.772 0.009 1 435 90 102 HIS C C 174.177 0.035 1 436 90 102 HIS CA C 56.101 0.082 1 437 90 102 HIS CB C 28.242 0.030 1 438 90 102 HIS N N 119.242 0.007 1 439 91 103 GLN H H 8.302 0.002 1 440 91 103 GLN C C 176.341 0.012 1 441 91 103 GLN CA C 56.167 0.058 1 442 91 103 GLN CB C 29.618 0.085 1 443 91 103 GLN N N 120.953 0.006 1 stop_ save_