data_18854 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; 1H,15N and 13C backbone chemical shifts of Human Halo S100A6 C3S ; _BMRB_accession_number 18854 _BMRB_flat_file_name bmr18854.str _Entry_type original _Submission_date 2012-11-23 _Accession_date 2012-11-23 _Entry_origination author _NMR_STAR_version 2.1.1 _Experimental_method NMR _Details 'Human S100A6 C3S Ca2+ bound form' loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Gupta Arun A. . 2 Yu Chin . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 83 "13C chemical shifts" 194 "15N chemical shifts" 83 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2014-02-14 original author . stop_ _Original_release_date 2014-02-14 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title '1H, 13C and 15N backbone and side chain resonance assignments of human halo S100A1.' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 22311340 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Gupta Arun A. . 2 Mohan Sepuru K. . 3 Chin Yu . . stop_ _Journal_abbreviation 'Biomol. NMR Assignments' _Journal_name_full 'Biomolecular NMR assignments' _Journal_volume 6 _Journal_issue 2 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 213 _Page_last 215 _Year 2012 _Details . loop_ _Keyword Assignment 'Calcium binding protein' 'Human Halo S100A6 C3S' stop_ save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name 'Human S100A6 C3S' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'Human S100A6 C3S' $Human_S100A6_C3S stop_ _System_molecular_weight 10163.8 _System_physical_state native _System_oligomer_state ? _System_paramagnetic no _System_thiol_state . _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_Human_S100A6_C3S _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common Human_S100A6_C3S _Molecular_mass 10163.8 _Mol_thiol_state 'all free' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 90 _Mol_residue_sequence ; MASPLDQAIGLLVAIFHKYS GREGDKHTLSKKELKELIQK ELTIGSKLQDAEIARLMEDL DRNKDQEVNFQEYVTFLGAL ALIYNEALKG ; loop_ _Residue_seq_code _Residue_label 1 MET 2 ALA 3 SER 4 PRO 5 LEU 6 ASP 7 GLN 8 ALA 9 ILE 10 GLY 11 LEU 12 LEU 13 VAL 14 ALA 15 ILE 16 PHE 17 HIS 18 LYS 19 TYR 20 SER 21 GLY 22 ARG 23 GLU 24 GLY 25 ASP 26 LYS 27 HIS 28 THR 29 LEU 30 SER 31 LYS 32 LYS 33 GLU 34 LEU 35 LYS 36 GLU 37 LEU 38 ILE 39 GLN 40 LYS 41 GLU 42 LEU 43 THR 44 ILE 45 GLY 46 SER 47 LYS 48 LEU 49 GLN 50 ASP 51 ALA 52 GLU 53 ILE 54 ALA 55 ARG 56 LEU 57 MET 58 GLU 59 ASP 60 LEU 61 ASP 62 ARG 63 ASN 64 LYS 65 ASP 66 GLN 67 GLU 68 VAL 69 ASN 70 PHE 71 GLN 72 GLU 73 TYR 74 VAL 75 THR 76 PHE 77 LEU 78 GLY 79 ALA 80 LEU 81 ALA 82 LEU 83 ILE 84 TYR 85 ASN 86 GLU 87 ALA 88 LEU 89 LYS 90 GLY 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 BMRB 18868 entity_1 100.00 90 100.00 100.00 1.86e-56 PDB 1K8U "Crystal Structure Of Calcium-Free (Or Apo) Human S100a6; Cys3met Mutant (Selenomethionine Derivative)" 100.00 90 97.78 97.78 1.47e-54 PDB 1K96 "Crystal Structure Of Calcium Bound Human S100a6" 100.00 90 98.89 98.89 6.66e-56 PDB 1K9K "Crystal Structure Of Calcium Bound Human S100a6" 100.00 90 98.89 98.89 6.66e-56 PDB 1K9P "Crystal Structure Of Calcium Free (or Apo) Human S100a6" 100.00 90 98.89 98.89 6.66e-56 PDB 2M1K "Interaction Of Human S100a6 (c3s) With V Domain Of Receptor For Advanced Glycation End Products (rage)" 100.00 90 100.00 100.00 1.86e-56 DBJ BAG35024 "unnamed protein product [Homo sapiens]" 100.00 90 97.78 97.78 8.91e-55 DBJ BAG74211 "S100 calcium binding protein A6 [synthetic construct]" 100.00 90 98.89 98.89 6.66e-56 GB AAA35886 "2A9 peptide [Homo sapiens]" 100.00 90 98.89 98.89 6.66e-56 GB AAA51905 "calcyclin [Homo sapiens]" 100.00 90 98.89 98.89 6.66e-56 GB AAA51906 "put. calcyclin; putative [Homo sapiens]" 100.00 90 98.89 98.89 6.66e-56 GB AAH01431 "S100 calcium binding protein A6 [Homo sapiens]" 100.00 90 98.89 98.89 6.66e-56 GB AAH09017 "S100A6 protein [Homo sapiens]" 100.00 90 98.89 98.89 6.66e-56 REF NP_001248728 "protein S100-A6 [Macaca mulatta]" 100.00 90 98.89 98.89 6.66e-56 REF NP_055439 "protein S100-A6 [Homo sapiens]" 100.00 90 98.89 98.89 6.66e-56 REF XP_002760026 "PREDICTED: protein S100-A6 [Callithrix jacchus]" 100.00 90 97.78 98.89 2.19e-55 REF XP_002810202 "PREDICTED: protein S100-A6 [Pongo abelii]" 100.00 90 98.89 98.89 6.66e-56 REF XP_003259360 "PREDICTED: protein S100-A6 [Nomascus leucogenys]" 100.00 90 98.89 98.89 6.66e-56 SP P06703 "RecName: Full=Protein S100-A6; AltName: Full=Calcyclin; AltName: Full=Growth factor-inducible protein 2A9; AltName: Full=MLN 4;" 100.00 90 98.89 98.89 6.66e-56 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $Human_S100A6_C3S 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_S100A6_C3S 'recombinant technology' . Escherichia coli 'BL21 (DE3)' pET(20b)+ stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Concentration_min_value _Concentration_max_value _Isotopic_labeling $Human_S100A6_C3S . mM 1 1.5 '[U-100% 13C; U-100% 15N]' TRIS 20 mM . . 'natural abundance' 'Calcium chloride' 10 mM . . 'natural abundance' 'sodium azide' 0.01 % . . 'natural abundance' H2O 90 % . . 'natural abundance' D2O 10 % . . 'natural abundance' stop_ save_ ############################ # Computer software used # ############################ save_VNMRJ _Saveframe_category software _Name VNMRJ _Version 2.3 loop_ _Vendor _Address _Electronic_address Varian . . stop_ loop_ _Task collection processing stop_ _Details . save_ save_SPARKY _Saveframe_category software _Name SPARKY _Version . loop_ _Vendor _Address _Electronic_address Goddard . . stop_ loop_ _Task 'chemical shift assignment' 'data analysis' 'peak picking' stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model INOVA _Field_strength 700 _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_HNCA_2 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCA' _Sample_label $sample_1 save_ save_3D_HN(CO)CA_3 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HN(CO)CA' _Sample_label $sample_1 save_ save_3D_CBCA(CO)NH_4 _Saveframe_category NMR_applied_experiment _Experiment_name '3D CBCA(CO)NH' _Sample_label $sample_1 save_ save_3D_HNCACB_5 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCACB' _Sample_label $sample_1 save_ save_3D_HNCO_6 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCO' _Sample_label $sample_1 save_ save_3D_HCACO_7 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HCACO' _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 . M pH 7.0 . 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 TSP C 13 'methyl protons' ppm 0.00 internal indirect . . . 0.251449530 TSP H 1 'methyl protons' ppm 0.00 internal direct . . . 1.00 TSP N 15 'methyl protons' ppm 0.00 internal 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 HNCA' '3D HN(CO)CA' '3D CBCA(CO)NH' '3D HNCACB' '3D HNCO' '3D HCACO' 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 'Human S100A6 C3S' _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 CB C 33.800 0.200 1 2 2 2 ALA CA C 57.300 0.200 1 3 3 3 SER H H 7.854 0.02 1 4 3 3 SER N N 118.552 0.20 1 5 4 4 PRO C C 180.814 0.20 1 6 4 4 PRO CA C 66.500 0.200 1 7 5 5 LEU H H 9.386 0.02 1 8 5 5 LEU C C 179.272 0.20 1 9 5 5 LEU CA C 58.600 0.200 1 10 5 5 LEU N N 119.501 0.20 1 11 6 6 ASP H H 7.912 0.02 1 12 6 6 ASP C C 179.800 0.20 1 13 6 6 ASP CA C 58.000 0.200 1 14 6 6 ASP N N 119.191 0.20 1 15 7 7 GLN H H 8.065 0.02 1 16 7 7 GLN C C 179.998 0.20 1 17 7 7 GLN CA C 58.900 0.200 1 18 7 7 GLN N N 117.979 0.20 1 19 8 8 ALA H H 8.159 0.02 1 20 8 8 ALA CA C 55.500 0.200 1 21 8 8 ALA N N 124.008 0.20 1 22 9 9 ILE C C 179.258 0.20 1 23 9 9 ILE CA C 64.900 0.200 1 24 10 10 GLY H H 8.062 0.02 1 25 10 10 GLY C C 177.984 0.20 1 26 10 10 GLY CA C 47.300 0.200 1 27 10 10 GLY N N 105.447 0.20 1 28 11 11 LEU H H 8.067 0.02 1 29 11 11 LEU C C 178.346 0.20 1 30 11 11 LEU CA C 58.000 0.200 1 31 11 11 LEU N N 124.755 0.20 1 32 12 12 LEU H H 7.997 0.02 1 33 12 12 LEU C C 182.560 0.20 1 34 12 12 LEU CA C 59.000 0.200 1 35 12 12 LEU N N 121.609 0.20 1 36 13 13 VAL H H 8.087 0.02 1 37 13 13 VAL C C 178.016 0.20 1 38 13 13 VAL CA C 67.100 0.200 1 39 13 13 VAL N N 119.951 0.20 1 40 14 14 ALA H H 8.363 0.02 1 41 14 14 ALA C C 175.380 0.20 1 42 14 14 ALA CA C 55.600 0.200 1 43 14 14 ALA N N 122.867 0.20 1 44 15 15 ILE H H 8.787 0.02 1 45 15 15 ILE C C 178.058 0.20 1 46 15 15 ILE CA C 64.800 0.200 1 47 15 15 ILE N N 118.496 0.20 1 48 16 16 PHE H H 7.171 0.02 1 49 16 16 PHE N N 119.259 0.20 1 50 17 17 HIS C C 178.660 0.20 1 51 17 17 HIS CA C 54.800 0.200 1 52 17 17 HIS CB C 30.000 0.200 1 53 18 18 LYS H H 8.880 0.02 1 54 18 18 LYS C C 180.221 0.20 1 55 18 18 LYS CA C 58.800 0.200 1 56 18 18 LYS CB C 32.810 0.200 1 57 18 18 LYS CE C 42.100 0.200 1 58 18 18 LYS N N 122.924 0.20 1 59 19 19 TYR H H 8.879 0.02 1 60 19 19 TYR C C 178.435 0.20 1 61 19 19 TYR CA C 55.300 0.200 1 62 19 19 TYR N N 120.227 0.20 1 63 20 20 SER H H 7.557 0.02 1 64 20 20 SER C C 178.376 0.20 1 65 20 20 SER CA C 56.900 0.200 1 66 20 20 SER CB C 61.700 0.200 1 67 20 20 SER N N 119.760 0.20 1 68 21 21 GLY H H 7.696 0.02 1 69 21 21 GLY C C 174.862 0.20 1 70 21 21 GLY CA C 45.600 0.200 1 71 21 21 GLY N N 111.202 0.20 1 72 22 22 ARG H H 7.311 0.02 1 73 22 22 ARG C C 178.336 0.20 1 74 22 22 ARG CA C 59.500 0.200 1 75 22 22 ARG CB C 30.500 0.200 1 76 22 22 ARG CD C 43.300 0.200 1 77 22 22 ARG N N 122.200 0.20 1 78 23 23 GLU H H 9.488 0.02 1 79 23 23 GLU C C 177.129 0.20 1 80 23 23 GLU CA C 54.300 0.200 1 81 23 23 GLU CB C 33.200 0.200 1 82 23 23 GLU N N 115.984 0.20 1 83 24 24 GLY H H 9.048 0.02 1 84 24 24 GLY C C 174.499 0.20 1 85 24 24 GLY CA C 45.900 0.200 1 86 24 24 GLY N N 114.031 0.20 1 87 25 25 ASP H H 8.249 0.02 1 88 25 25 ASP C C 177.998 0.20 1 89 25 25 ASP CA C 55.000 0.200 1 90 25 25 ASP N N 125.634 0.20 1 91 26 26 LYS H H 9.043 0.02 1 92 26 26 LYS CA C 57.400 0.200 1 93 26 26 LYS CB C 37.800 0.200 1 94 26 26 LYS CE C 42.100 0.200 1 95 26 26 LYS N N 121.469 0.20 1 96 27 27 HIS H H 8.168 0.02 1 97 27 27 HIS C C 175.067 0.20 1 98 27 27 HIS CA C 55.300 0.200 1 99 27 27 HIS CB C 30.300 0.200 1 100 27 27 HIS N N 121.183 0.20 1 101 28 28 THR H H 7.248 0.02 1 102 28 28 THR C C 174.469 0.20 1 103 28 28 THR CA C 60.000 0.200 1 104 28 28 THR N N 106.447 0.20 1 105 29 29 LEU H H 9.421 0.02 1 106 29 29 LEU C C 180.751 0.20 1 107 29 29 LEU CA C 55.200 0.200 1 108 29 29 LEU CB C 41.800 0.200 1 109 29 29 LEU N N 125.037 0.20 1 110 30 30 SER H H 8.241 0.02 1 111 30 30 SER C C 177.946 0.20 1 112 30 30 SER CA C 57.900 0.200 1 113 30 30 SER N N 112.780 0.20 1 114 31 31 LYS H H 9.659 0.02 1 115 31 31 LYS CA C 55.400 0.200 1 116 31 31 LYS CE C 42.100 0.200 1 117 31 31 LYS N N 117.689 0.20 1 118 32 32 LYS C C 180.677 0.20 1 119 32 32 LYS CA C 59.800 0.200 1 120 32 32 LYS CE C 42.100 0.200 1 121 33 33 GLU H H 7.608 0.02 1 122 33 33 GLU C C 179.654 0.20 1 123 33 33 GLU CA C 59.300 0.200 1 124 33 33 GLU N N 120.336 0.20 1 125 34 34 LEU H H 7.659 0.02 1 126 34 34 LEU C C 179.420 0.20 1 127 34 34 LEU CA C 56.600 0.200 1 128 34 34 LEU N N 117.303 0.20 1 129 35 35 LYS H H 7.731 0.02 1 130 35 35 LYS CA C 60.700 0.200 1 131 35 35 LYS CB C 32.000 0.200 1 132 35 35 LYS CE C 42.100 0.200 1 133 35 35 LYS N N 116.520 0.20 1 134 36 36 GLU H H 7.871 0.02 1 135 36 36 GLU C C 177.868 0.20 1 136 36 36 GLU CA C 59.700 0.200 1 137 36 36 GLU CB C 29.300 0.200 1 138 36 36 GLU N N 118.365 0.20 1 139 37 37 LEU H H 7.513 0.02 1 140 37 37 LEU C C 176.731 0.20 1 141 37 37 LEU CA C 59.500 0.200 1 142 37 37 LEU CB C 42.700 0.200 1 143 37 37 LEU N N 121.068 0.20 1 144 38 38 ILE H H 8.206 0.02 1 145 38 38 ILE C C 178.658 0.20 1 146 38 38 ILE CA C 65.300 0.200 1 147 38 38 ILE N N 117.867 0.20 1 148 39 39 GLN H H 8.238 0.02 1 149 39 39 GLN C C 180.003 0.20 1 150 39 39 GLN CA C 59.500 0.200 1 151 39 39 GLN N N 114.147 0.20 1 152 40 40 LYS H H 8.298 0.02 1 153 40 40 LYS C C 180.483 0.20 1 154 40 40 LYS CA C 57.500 0.200 1 155 40 40 LYS CE C 42.100 0.200 1 156 40 40 LYS N N 115.051 0.20 1 157 41 41 GLU H H 8.328 0.02 1 158 41 41 GLU C C 178.252 0.20 1 159 41 41 GLU CA C 55.700 0.200 1 160 41 41 GLU N N 112.448 0.20 1 161 42 42 LEU H H 7.361 0.02 1 162 42 42 LEU C C 179.377 0.20 1 163 42 42 LEU CA C 53.300 0.200 1 164 42 42 LEU N N 118.693 0.20 1 165 43 43 THR H H 9.926 0.02 1 166 43 43 THR C C 178.543 0.20 1 167 43 43 THR CA C 67.300 0.200 1 168 43 43 THR N N 125.535 0.20 1 169 44 44 ILE H H 8.214 0.02 1 170 44 44 ILE C C 178.107 0.20 1 171 44 44 ILE CA C 62.400 0.200 1 172 44 44 ILE CB C 38.300 0.200 1 173 44 44 ILE N N 116.467 0.20 1 174 45 45 GLY H H 7.750 0.02 1 175 45 45 GLY C C 176.355 0.20 1 176 45 45 GLY CA C 47.400 0.200 1 177 45 45 GLY N N 108.241 0.20 1 178 46 46 SER H H 7.847 0.02 1 179 46 46 SER C C 176.007 0.20 1 180 46 46 SER CA C 60.100 0.200 1 181 46 46 SER N N 113.635 0.20 1 182 47 47 LYS H H 7.709 0.02 1 183 47 47 LYS C C 178.100 0.20 1 184 47 47 LYS CA C 56.000 0.200 1 185 47 47 LYS CB C 33.400 0.200 1 186 47 47 LYS CE C 42.100 0.200 1 187 47 47 LYS N N 119.437 0.20 1 188 48 48 LEU H H 7.139 0.02 1 189 48 48 LEU C C 178.009 0.20 1 190 48 48 LEU CA C 55.000 0.200 1 191 48 48 LEU N N 120.169 0.20 1 192 49 49 GLN H H 7.917 0.02 1 193 49 49 GLN C C 179.051 0.20 1 194 49 49 GLN CA C 58.100 0.200 1 195 49 49 GLN N N 121.739 0.20 1 196 50 50 ASP H H 7.597 0.02 1 197 50 50 ASP C C 178.335 0.20 1 198 50 50 ASP CA C 59.300 0.200 1 199 50 50 ASP N N 119.121 0.20 1 200 51 51 ALA H H 7.560 0.02 1 201 51 51 ALA C C 181.587 0.20 1 202 51 51 ALA CA C 57.700 0.200 1 203 51 51 ALA N N 116.624 0.20 1 204 52 52 GLU H H 8.511 0.02 1 205 52 52 GLU C C 180.495 0.20 1 206 52 52 GLU CA C 58.900 0.200 1 207 52 52 GLU N N 118.931 0.20 1 208 53 53 ILE H H 7.905 0.02 1 209 53 53 ILE CA C 65.400 0.200 1 210 53 53 ILE N N 120.400 0.20 1 211 54 54 ALA C C 181.477 0.20 1 212 54 54 ALA CA C 55.600 0.200 1 213 55 55 ARG H H 7.448 0.02 1 214 55 55 ARG C C 179.468 0.20 1 215 55 55 ARG CA C 59.100 0.200 1 216 55 55 ARG CD C 43.300 0.200 1 217 55 55 ARG N N 118.315 0.20 1 218 56 56 LEU H H 7.672 0.02 1 219 56 56 LEU C C 179.984 0.20 1 220 56 56 LEU CA C 58.000 0.200 1 221 56 56 LEU N N 120.310 0.20 1 222 57 57 MET H H 8.354 0.02 1 223 57 57 MET C C 179.083 0.20 1 224 57 57 MET N N 115.780 0.20 1 225 58 58 GLU H H 7.620 0.02 1 226 58 58 GLU C C 179.161 0.20 1 227 58 58 GLU CA C 59.300 0.200 1 228 58 58 GLU CB C 31.100 0.200 1 229 58 58 GLU N N 117.826 0.20 1 230 59 59 ASP H H 8.693 0.02 1 231 59 59 ASP CA C 57.200 0.200 1 232 59 59 ASP N N 117.801 0.20 1 233 60 60 LEU H H 8.159 0.02 1 234 60 60 LEU C C 179.216 0.20 1 235 60 60 LEU CA C 56.200 0.200 1 236 60 60 LEU N N 117.370 0.20 1 237 61 61 ASP H H 7.559 0.02 1 238 61 61 ASP C C 178.473 0.20 1 239 61 61 ASP CA C 52.800 0.200 1 240 61 61 ASP CB C 39.100 0.200 1 241 61 61 ASP N N 117.835 0.20 1 242 62 62 ARG H H 7.839 0.02 1 243 62 62 ARG C C 178.519 0.20 1 244 62 62 ARG CA C 58.500 0.200 1 245 62 62 ARG CB C 30.200 0.200 1 246 62 62 ARG CD C 43.300 0.200 1 247 62 62 ARG N N 125.783 0.20 1 248 63 63 ASN H H 7.899 0.02 1 249 63 63 ASN C C 175.597 0.20 1 250 63 63 ASN CA C 51.900 0.200 1 251 63 63 ASN CB C 36.700 0.200 1 252 63 63 ASN N N 112.348 0.20 1 253 64 64 LYS H H 7.485 0.02 1 254 64 64 LYS C C 176.731 0.20 1 255 64 64 LYS CA C 59.500 0.200 1 256 64 64 LYS CE C 42.100 0.200 1 257 64 64 LYS N N 114.407 0.20 1 258 65 65 ASP H H 8.184 0.02 1 259 65 65 ASP C C 177.981 0.20 1 260 65 65 ASP CA C 52.900 0.200 1 261 65 65 ASP N N 117.880 0.20 1 262 66 66 GLN H H 9.917 0.02 1 263 66 66 GLN C C 175.374 0.20 1 264 66 66 GLN CA C 57.900 0.200 1 265 66 66 GLN CB C 26.200 0.200 1 266 66 66 GLN N N 114.037 0.20 1 267 67 67 GLU H H 7.800 0.02 1 268 67 67 GLU C C 176.826 0.20 1 269 67 67 GLU CA C 54.000 0.200 1 270 67 67 GLU CB C 33.100 0.200 1 271 67 67 GLU N N 117.611 0.20 1 272 68 68 VAL H H 9.656 0.02 1 273 68 68 VAL C C 177.398 0.20 1 274 68 68 VAL CA C 61.100 0.200 1 275 68 68 VAL CB C 33.300 0.200 1 276 68 68 VAL N N 126.064 0.20 1 277 69 69 ASN H H 9.036 0.02 1 278 69 69 ASN C C 175.438 0.20 1 279 69 69 ASN CA C 51.200 0.200 1 280 69 69 ASN N N 127.002 0.20 1 281 70 70 PHE H H 9.055 0.02 1 282 70 70 PHE C C 177.652 0.20 1 283 70 70 PHE CA C 63.300 0.200 1 284 70 70 PHE N N 119.437 0.20 1 285 71 71 GLN H H 8.273 0.02 1 286 71 71 GLN C C 180.488 0.20 1 287 71 71 GLN CA C 60.100 0.200 1 288 71 71 GLN CB C 27.900 0.200 1 289 71 71 GLN N N 117.576 0.20 1 290 72 72 GLU H H 8.631 0.02 1 291 72 72 GLU C C 179.001 0.20 1 292 72 72 GLU CA C 58.700 0.200 1 293 72 72 GLU N N 119.971 0.20 1 294 73 73 TYR H H 7.721 0.02 1 295 73 73 TYR C C 180.040 0.20 1 296 73 73 TYR N N 120.475 0.20 1 297 74 74 VAL H H 8.147 0.02 1 298 74 74 VAL C C 178.463 0.20 1 299 74 74 VAL CA C 60.200 0.200 1 300 74 74 VAL CB C 33.800 0.200 1 301 74 74 VAL N N 119.604 0.20 1 302 75 75 THR H H 8.234 0.02 1 303 75 75 THR C C 179.971 0.20 1 304 75 75 THR CA C 60.600 0.200 1 305 75 75 THR N N 116.488 0.20 1 306 76 76 PHE H H 7.864 0.02 1 307 76 76 PHE C C 177.695 0.20 1 308 76 76 PHE CA C 60.000 0.200 1 309 76 76 PHE N N 116.963 0.20 1 310 77 77 LEU H H 7.913 0.02 1 311 77 77 LEU C C 180.668 0.20 1 312 77 77 LEU CA C 57.800 0.200 1 313 77 77 LEU N N 117.568 0.20 1 314 78 78 GLY H H 8.057 0.02 1 315 78 78 GLY C C 176.062 0.20 1 316 78 78 GLY CA C 47.600 0.200 1 317 78 78 GLY N N 104.257 0.20 1 318 79 79 ALA H H 7.804 0.02 1 319 79 79 ALA C C 182.313 0.20 1 320 79 79 ALA CA C 55.100 0.200 1 321 79 79 ALA N N 124.122 0.20 1 322 80 80 LEU H H 8.045 0.02 1 323 80 80 LEU C C 178.389 0.20 1 324 80 80 LEU CA C 57.400 0.200 1 325 80 80 LEU N N 117.976 0.20 1 326 81 81 ALA H H 8.152 0.02 1 327 81 81 ALA C C 181.617 0.20 1 328 81 81 ALA CA C 55.300 0.200 1 329 81 81 ALA N N 121.199 0.20 1 330 82 82 LEU H H 7.238 0.02 1 331 82 82 LEU C C 180.828 0.20 1 332 82 82 LEU CA C 58.800 0.200 1 333 82 82 LEU N N 117.392 0.20 1 334 83 83 ILE H H 8.726 0.02 1 335 83 83 ILE C C 177.495 0.20 1 336 83 83 ILE CA C 60.500 0.200 1 337 83 83 ILE N N 124.342 0.20 1 338 84 84 TYR H H 8.241 0.02 1 339 84 84 TYR C C 177.236 0.20 1 340 84 84 TYR CA C 56.900 0.200 1 341 84 84 TYR N N 120.026 0.20 1 342 85 85 ASN H H 7.681 0.02 1 343 85 85 ASN C C 175.508 0.20 1 344 85 85 ASN CA C 56.600 0.200 1 345 85 85 ASN N N 117.125 0.20 1 346 86 86 GLU H H 8.790 0.02 1 347 86 86 GLU C C 177.821 0.20 1 348 86 86 GLU N N 119.756 0.20 1 349 87 87 ALA H H 7.714 0.02 1 350 87 87 ALA N N 124.638 0.20 1 351 88 88 LEU H H 7.854 0.02 1 352 88 88 LEU CA C 57.900 0.200 1 353 88 88 LEU N N 118.552 0.20 1 354 89 89 LYS H H 8.384 0.02 1 355 89 89 LYS C C 177.332 0.20 1 356 89 89 LYS CA C 56.900 0.200 1 357 89 89 LYS CE C 42.100 0.200 1 358 89 89 LYS N N 118.627 0.20 1 359 90 90 GLY H H 7.685 0.02 1 360 90 90 GLY N N 114.718 0.20 1 stop_ save_