data_26943 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; mini monomeric TGF-b2 ; _BMRB_accession_number 26943 _BMRB_flat_file_name bmr26943.str _Entry_type original _Submission_date 2016-11-15 _Accession_date 2016-11-15 _Entry_origination author _NMR_STAR_version 2.1.1 _Experimental_method NMR _Details 'Assigned backbone chemical shifts for an engineered TGF-b2 monomer lacking the interfacial a-helix.' loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Hinck Andrew . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 86 "13C chemical shifts" 272 "15N chemical shifts" 86 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2017-06-08 update BMRB 'update entry citation' 2017-04-26 original author 'original release' stop_ loop_ _Related_BMRB_accession_number _Relationship 26944 'mini monomeric TGF-b2-7m' stop_ _Original_release_date 2016-11-15 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; An engineered TGF-beta monomer that functions as a dominant negative to block TGF-beta signaling ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 28228478 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Kim Sun-Kyung . . 2 Myers Lindsey . . 3 Hinck Cynthia S. . 4 Can Kristin . . 5 Thirangala Avi . . 6 Iskra Brian . . 7 Brothers Molly . . 8 Vonberg Machell . . 9 Leal Belinda . . 10 Richter Blair . . 11 Kodak Ravindra . . 12 Taylor Alex B. . 13 Du Shoucheng . . 14 Barnes Christopher . . 15 Calero Guillermo . . 16 Hart Peter J. . 17 Hart Matthew J. . 18 Demeler Borries . . 19 Hinck Andrew P. . stop_ _Journal_abbreviation 'J. Biol. Chem.' _Journal_volume 292 _Journal_issue 17 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 7173 _Page_last 7188 _Year 2017 _Details . loop_ _Keyword Cancer Fibrosis Inhibitor NMR Signaling TGF stop_ save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name mmTGF-b2 _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label mmTGF-b2 $mmTGF-b2 stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state ? _System_paramagnetic no _System_thiol_state . loop_ _Biological_function 'signaling protein' stop_ _Database_query_date . _Details 'Monomeric protein, no oligomers are formed, either covalently or non-covalently' save_ ######################## # Monomeric polymers # ######################## save_mmTGF-b2 _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common mmTGF-b2 _Molecular_mass . _Mol_thiol_state 'all disulfide bound' loop_ _Biological_function 'Signaling protein' stop_ _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 93 _Mol_residue_sequence ; MALDAAYCFRNVQDNCCLRP LYIDFKRDCGWKWIHEPKGY NANFCAGACPYRNSKSPSCV SQDLEPLTILYYIGKTPKIE QLSNMIVKSCKCS ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 0 MET 2 1 ALA 3 2 LEU 4 3 ASP 5 4 ALA 6 5 ALA 7 6 TYR 8 7 CYS 9 8 PHE 10 9 ARG 11 10 ASN 12 11 VAL 13 12 GLN 14 13 ASP 15 14 ASN 16 15 CYS 17 16 CYS 18 17 LEU 19 18 ARG 20 19 PRO 21 20 LEU 22 21 TYR 23 22 ILE 24 23 ASP 25 24 PHE 26 25 LYS 27 26 ARG 28 27 ASP 29 28 CYS 30 29 GLY 31 30 TRP 32 31 LYS 33 32 TRP 34 33 ILE 35 34 HIS 36 35 GLU 37 36 PRO 38 37 LYS 39 38 GLY 40 39 TYR 41 40 ASN 42 41 ALA 43 42 ASN 44 43 PHE 45 44 CYS 46 45 ALA 47 46 GLY 48 47 ALA 49 48 CYS 50 49 PRO 51 50 TYR 52 51 ARG 53 52 ASN 54 53 SER 55 54 LYS 56 55 SER 57 56 PRO 58 57 SER 59 58 CYS 60 59 VAL 61 60 SER 62 61 GLN 63 62 ASP 64 63 LEU 65 64 GLU 66 65 PRO 67 66 LEU 68 67 THR 69 68 ILE 70 69 LEU 71 70 TYR 72 71 TYR 73 72 ILE 74 73 GLY 75 74 LYS 76 75 THR 77 76 PRO 78 77 LYS 79 78 ILE 80 79 GLU 81 80 GLN 82 81 LEU 83 82 SER 84 83 ASN 85 84 MET 86 85 ILE 87 86 VAL 88 87 LYS 89 88 SER 90 89 CYS 91 90 LYS 92 91 CYS 93 92 SER 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 _Details $mmTGF-b2 Human 9606 Eukaryota Metazoa Homo sapiens ; This is an engineered variant of the mature growth factor domain of human TGF-b2. Because it is engineered, it does not naturally exist ; 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 _Details $mmTGF-b2 'recombinant technology' . Escherichia coli BL21(DE3) pET32a 'Protein is produced using pET32a, but not as a thioredoxin fusion (the thioredoxin part was removed from the coding construct)' 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 $mmTGF-b2 0.2 mM '[U-99% 13C; U-99% 15N]' D2O 5 % '[U-99% 2H]' H2O 95 % 'natural abundance' 'dibasic sodium phosphate' 10 mM 'natural abundance' CHAPS 10 mM 'natural abundance' stop_ save_ ############################ # Computer software used # ############################ save_NMRPipe _Saveframe_category software _Name NMRPipe _Version . loop_ _Vendor _Address _Electronic_address 'Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax' . . stop_ loop_ _Task processing stop_ _Details 'Used for data processing' save_ save_SPARKY _Saveframe_category software _Name SPARKY _Version NMRFAM-SPARKY loop_ _Vendor _Address _Electronic_address Goddard . . stop_ loop_ _Task 'chemical shift assignment' stop_ _Details . save_ save_PINE _Saveframe_category software _Name PINE _Version . loop_ _Vendor _Address _Electronic_address 'Bahrami, Markley, Assadi, and Eghbalnia' . . stop_ loop_ _Task 'chemical shift assignment' stop_ _Details . save_ save_TOPSPIN _Saveframe_category software _Name TOPSPIN _Version 3.1 loop_ _Vendor _Address _Electronic_address 'Bruker Biospin' . . stop_ loop_ _Task collection stop_ _Details 'Used NUS option to generate sampling schedules for triple-resonance data collection' save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model Avance _Field_strength 800 _Details AV-II 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_ save_3D_HNCO_4 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCO' _Sample_label $sample_1 save_ save_3D_HN(CA)CO_5 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HN(CA)CO' _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' 0.06 . M pH 4.7 . pH pressure 1 . atm temperature 310 . K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference_1 _Saveframe_category chemical_shift_reference _Details '1H DSS, with IUPAC indirect referencing ratios used to reference 13C and 15N' 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 0.0 internal indirect . . . 0.251449530 DSS H 1 'methyl protons' ppm 0.0 internal direct . . . 1 DSS N 15 'methyl protons' ppm 0.0 internal indirect . . . 0.10132918 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 $NMRPipe $SPARKY $PINE $TOPSPIN stop_ loop_ _Experiment_label '2D 1H-15N HSQC' '3D CBCA(CO)NH' '3D HNCACB' '3D HNCO' '3D HN(CA)CO' 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 mmTGF-b2 _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 2 ALA H H 8.098 0.00 . 2 1 2 ALA C C 173.343 0.01 . 3 1 2 ALA CA C 51.706 0.10 . 4 1 2 ALA CB C 19.562 0.07 . 5 1 2 ALA N N 125.168 0.00 . 6 2 3 LEU H H 8.704 0.03 . 7 2 3 LEU C C 174.879 0.01 . 8 2 3 LEU CA C 53.357 0.06 . 9 2 3 LEU CB C 39.734 0.06 . 10 2 3 LEU N N 121.176 0.03 . 11 3 4 ASP H H 7.778 0.01 . 12 3 4 ASP C C 175.984 0.01 . 13 3 4 ASP CA C 51.497 0.04 . 14 3 4 ASP CB C 42.994 0.02 . 15 3 4 ASP N N 121.429 0.08 . 16 4 5 ALA H H 8.550 0.03 . 17 4 5 ALA C C 179.241 0.01 . 18 4 5 ALA CA C 55.576 0.17 . 19 4 5 ALA CB C 18.843 0.11 . 20 4 5 ALA N N 122.998 0.01 . 21 5 6 ALA H H 7.684 0.02 . 22 5 6 ALA C C 179.179 0.01 . 23 5 6 ALA CA C 54.778 0.06 . 24 5 6 ALA CB C 18.198 0.10 . 25 5 6 ALA N N 119.292 0.04 . 26 6 7 TYR H H 7.669 0.00 . 27 6 7 TYR C C 178.333 0.02 . 28 6 7 TYR CA C 60.415 0.06 . 29 6 7 TYR CB C 40.385 0.02 . 30 6 7 TYR N N 115.415 0.12 . 31 7 8 CYS H H 8.883 0.02 . 32 7 8 CYS C C 176.412 0.01 . 33 7 8 CYS CA C 57.487 0.33 . 34 7 8 CYS CB C 40.508 0.01 . 35 7 8 CYS N N 115.148 0.06 . 36 8 9 PHE H H 8.465 0.02 . 37 8 9 PHE C C 176.676 0.03 . 38 8 9 PHE CA C 56.340 0.04 . 39 8 9 PHE CB C 35.925 0.08 . 40 8 9 PHE N N 117.153 0.18 . 41 9 10 ARG H H 7.141 0.03 . 42 9 10 ARG C C 175.044 0.01 . 43 9 10 ARG CA C 56.614 0.14 . 44 9 10 ARG CB C 31.102 0.05 . 45 9 10 ARG N N 116.452 0.14 . 46 10 11 ASN H H 7.407 0.03 . 47 10 11 ASN C C 173.384 0.00 . 48 10 11 ASN CA C 52.610 0.08 . 49 10 11 ASN CB C 39.595 0.03 . 50 10 11 ASN N N 117.951 0.01 . 51 11 12 VAL H H 8.163 0.07 . 52 11 12 VAL C C 175.744 0.72 . 53 11 12 VAL CA C 63.695 0.02 . 54 11 12 VAL CB C 31.498 0.03 . 55 11 12 VAL N N 121.920 0.17 . 56 12 13 GLN H H 8.478 0.03 . 57 12 13 GLN C C 175.599 0.01 . 58 12 13 GLN CA C 54.616 0.09 . 59 12 13 GLN CB C 31.349 0.06 . 60 12 13 GLN N N 124.416 0.17 . 61 13 14 ASP H H 8.707 0.03 . 62 13 14 ASP C C 177.048 0.01 . 63 13 14 ASP CA C 55.434 0.04 . 64 13 14 ASP CB C 41.098 0.06 . 65 13 14 ASP N N 120.949 0.02 . 66 14 15 ASN H H 7.637 0.01 . 67 14 15 ASN C C 174.074 0.01 . 68 14 15 ASN CA C 53.696 0.12 . 69 14 15 ASN CB C 39.485 0.04 . 70 14 15 ASN N N 117.393 0.04 . 71 15 16 CYS H H 8.590 0.03 . 72 15 16 CYS C C 172.228 0.02 . 73 15 16 CYS CA C 55.469 0.09 . 74 15 16 CYS CB C 35.279 0.06 . 75 15 16 CYS N N 116.153 0.09 . 76 16 17 CYS H H 8.090 0.00 . 77 16 17 CYS C C 171.253 0.02 . 78 16 17 CYS CA C 59.374 0.07 . 79 16 17 CYS CB C 39.611 0.07 . 80 16 17 CYS N N 124.890 0.06 . 81 17 18 LEU H H 7.633 0.00 . 82 17 18 LEU C C 174.558 0.01 . 83 17 18 LEU CA C 55.696 0.04 . 84 17 18 LEU CB C 43.979 0.06 . 85 17 18 LEU N N 125.468 0.02 . 86 18 19 ARG H H 9.140 0.01 . 87 18 19 ARG C C 172.983 0.00 . 88 18 19 ARG CA C 50.712 0.00 . 89 18 19 ARG CB C 29.838 0.00 . 90 18 19 ARG N N 125.742 0.02 . 91 19 20 PRO C C 176.968 0.00 . 92 19 20 PRO CA C 62.186 0.00 . 93 19 20 PRO CB C 31.885 0.03 . 94 20 21 LEU H H 7.700 0.00 . 95 20 21 LEU C C 173.395 0.01 . 96 20 21 LEU CA C 56.853 0.07 . 97 20 21 LEU CB C 44.845 0.09 . 98 20 21 LEU N N 119.040 0.01 . 99 21 22 TYR H H 8.658 0.03 . 100 21 22 TYR C C 173.738 0.01 . 101 21 22 TYR CA C 57.096 0.06 . 102 21 22 TYR CB C 39.721 0.04 . 103 21 22 TYR N N 131.314 0.03 . 104 22 23 ILE H H 7.798 0.01 . 105 22 23 ILE C C 172.420 0.01 . 106 22 23 ILE CA C 58.147 0.19 . 107 22 23 ILE CB C 39.295 0.16 . 108 22 23 ILE N N 127.766 0.02 . 109 23 24 ASP H H 9.073 0.01 . 110 23 24 ASP C C 177.235 0.01 . 111 23 24 ASP CA C 52.685 0.09 . 112 23 24 ASP CB C 44.370 0.07 . 113 23 24 ASP N N 127.766 0.02 . 114 24 25 PHE H H 8.210 0.00 . 115 24 25 PHE C C 178.093 0.01 . 116 24 25 PHE CA C 63.876 0.06 . 117 24 25 PHE CB C 38.605 0.05 . 118 24 25 PHE N N 125.227 0.03 . 119 25 26 LYS H H 8.789 0.02 . 120 25 26 LYS C C 178.401 0.01 . 121 25 26 LYS CA C 60.689 0.05 . 122 25 26 LYS CB C 32.805 0.05 . 123 25 26 LYS N N 120.297 0.05 . 124 26 27 ARG H H 8.872 0.01 . 125 26 27 ARG C C 177.552 0.00 . 126 26 27 ARG CA C 59.021 0.07 . 127 26 27 ARG CB C 31.490 0.07 . 128 26 27 ARG N N 119.557 0.01 . 129 27 28 ASP H H 8.389 0.01 . 130 27 28 ASP C C 176.757 0.00 . 131 27 28 ASP CA C 56.717 0.08 . 132 27 28 ASP CB C 41.626 0.04 . 133 27 28 ASP N N 113.395 0.07 . 134 28 29 CYS H H 6.563 0.02 . 135 28 29 CYS C C 176.730 0.05 . 136 28 29 CYS CA C 54.273 0.01 . 137 28 29 CYS CB C 41.706 0.02 . 138 28 29 CYS N N 113.666 0.03 . 139 29 30 GLY H H 7.248 0.00 . 140 29 30 GLY C C 175.707 0.02 . 141 29 30 GLY CA C 46.376 0.05 . 142 29 30 GLY N N 106.528 0.02 . 143 30 31 TRP H H 7.967 0.00 . 144 30 31 TRP C C 176.175 0.00 . 145 30 31 TRP CA C 54.343 0.06 . 146 30 31 TRP CB C 29.069 0.06 . 147 30 31 TRP N N 122.890 0.07 . 148 31 32 LYS H H 8.557 0.06 . 149 31 32 LYS C C 175.886 0.01 . 150 31 32 LYS CA C 57.455 0.00 . 151 31 32 LYS CB C 32.675 0.09 . 152 31 32 LYS N N 121.412 0.02 . 153 32 33 TRP H H 7.160 0.01 . 154 32 33 TRP C C 175.878 0.00 . 155 32 33 TRP CA C 56.281 0.06 . 156 32 33 TRP CB C 29.058 0.04 . 157 32 33 TRP N N 114.958 0.02 . 158 33 34 ILE H H 6.759 0.01 . 159 33 34 ILE C C 175.625 0.01 . 160 33 34 ILE CA C 62.802 0.05 . 161 33 34 ILE CB C 37.885 0.10 . 162 33 34 ILE N N 121.605 0.10 . 163 34 35 HIS H H 9.015 0.01 . 164 34 35 HIS C C 174.669 0.00 . 165 34 35 HIS CA C 58.608 0.20 . 166 34 35 HIS CB C 31.424 0.15 . 167 34 35 HIS N N 127.291 0.02 . 168 35 36 GLU H H 7.997 0.00 . 169 35 36 GLU C C 173.302 0.00 . 170 35 36 GLU CA C 53.933 0.00 . 171 35 36 GLU CB C 34.646 0.00 . 172 35 36 GLU N N 116.121 0.12 . 173 36 37 PRO C C 175.483 0.01 . 174 36 37 PRO CA C 62.814 0.00 . 175 36 37 PRO CB C 34.797 0.05 . 176 37 38 LYS H H 8.804 0.03 . 177 37 38 LYS C C 177.230 0.00 . 178 37 38 LYS CA C 57.931 0.10 . 179 37 38 LYS CB C 32.520 0.11 . 180 37 38 LYS N N 116.489 0.03 . 181 38 39 GLY H H 7.714 0.00 . 182 38 39 GLY C C 170.429 0.00 . 183 38 39 GLY CA C 46.083 0.01 . 184 38 39 GLY N N 105.837 0.03 . 185 39 40 TYR H H 8.237 0.00 . 186 39 40 TYR C C 171.515 0.02 . 187 39 40 TYR CA C 55.942 0.10 . 188 39 40 TYR CB C 40.797 0.05 . 189 39 40 TYR N N 116.968 0.06 . 190 40 41 ASN H H 8.560 0.02 . 191 40 41 ASN C C 171.854 0.00 . 192 40 41 ASN CA C 53.368 0.05 . 193 40 41 ASN CB C 38.482 0.04 . 194 40 41 ASN N N 119.827 0.07 . 195 41 42 ALA H H 7.313 0.01 . 196 41 42 ALA C C 177.112 0.01 . 197 41 42 ALA CA C 55.340 0.04 . 198 41 42 ALA CB C 21.823 0.07 . 199 41 42 ALA N N 130.963 0.03 . 200 42 43 ASN H H 7.679 0.02 . 201 42 43 ASN C C 170.889 0.01 . 202 42 43 ASN CA C 55.263 0.08 . 203 42 43 ASN CB C 40.612 0.03 . 204 42 43 ASN N N 131.377 0.03 . 205 43 44 PHE H H 8.145 0.00 . 206 43 44 PHE C C 172.609 0.01 . 207 43 44 PHE CA C 57.473 0.04 . 208 43 44 PHE CB C 40.108 0.08 . 209 43 44 PHE N N 107.250 0.05 . 210 44 45 CYS H H 8.783 0.04 . 211 44 45 CYS C C 173.446 0.01 . 212 44 45 CYS CA C 54.559 0.07 . 213 44 45 CYS CB C 42.618 0.07 . 214 44 45 CYS N N 118.889 0.07 . 215 45 46 ALA H H 24.890 50.51 . 216 45 46 ALA C C 177.271 0.62 . 217 45 46 ALA CA C 52.962 0.04 . 218 45 46 ALA CB C 23.661 0.08 . 219 45 46 ALA N N 121.051 0.08 . 220 46 47 GLY H H 9.034 0.03 . 221 46 47 GLY C C 172.683 0.78 . 222 46 47 GLY CA C 43.889 0.04 . 223 46 47 GLY N N 99.811 28.09 . 224 47 48 ALA H H 7.998 0.01 . 225 47 48 ALA C C 178.271 0.00 . 226 47 48 ALA CA C 53.641 0.07 . 227 47 48 ALA CB C 19.958 0.08 . 228 47 48 ALA N N 120.335 0.05 . 229 48 49 CYS H H 8.519 0.03 . 230 48 49 CYS C C 171.702 0.00 . 231 48 49 CYS CA C 53.898 0.00 . 232 48 49 CYS CB C 44.070 0.00 . 233 48 49 CYS N N 120.356 0.02 . 234 49 50 PRO C C 175.786 0.00 . 235 49 50 PRO CA C 63.196 0.07 . 236 49 50 PRO CB C 31.963 0.01 . 237 50 51 TYR H H 8.227 0.04 . 238 50 51 TYR C C 175.830 0.01 . 239 50 51 TYR CA C 58.818 0.03 . 240 50 51 TYR CB C 38.908 0.03 . 241 50 51 TYR N N 121.143 0.05 . 242 51 52 ARG H H 7.825 0.01 . 243 51 52 ARG C C 174.659 0.00 . 244 51 52 ARG CA C 55.392 0.04 . 245 51 52 ARG CB C 32.457 0.07 . 246 51 52 ARG N N 124.145 0.14 . 247 52 53 ASN H H 8.352 0.03 . 248 52 53 ASN C C 177.515 0.00 . 249 52 53 ASN CA C 53.636 0.09 . 250 52 53 ASN CB C 18.717 0.12 . 251 52 53 ASN N N 125.075 0.05 . 252 53 54 SER H H 8.037 0.02 . 253 53 54 SER C C 173.888 0.01 . 254 53 54 SER CA C 59.420 0.08 . 255 53 54 SER CB C 63.388 0.05 . 256 53 54 SER N N 111.695 0.09 . 257 54 55 LYS H H 7.847 0.01 . 258 54 55 LYS C C 175.276 0.01 . 259 54 55 LYS CA C 55.928 0.08 . 260 54 55 LYS CB C 33.665 0.05 . 261 54 55 LYS N N 120.743 0.01 . 262 55 56 SER H H 8.407 0.03 . 263 55 56 SER C C 172.628 0.00 . 264 55 56 SER CA C 56.359 0.00 . 265 55 56 SER CB C 63.409 0.00 . 266 55 56 SER N N 118.586 0.04 . 267 56 57 PRO C C 175.899 0.00 . 268 56 57 PRO CA C 62.831 0.10 . 269 56 57 PRO CB C 32.880 0.07 . 270 57 58 SER H H 8.718 0.01 . 271 57 58 SER C C 172.057 0.01 . 272 57 58 SER CA C 57.765 0.07 . 273 57 58 SER CB C 65.947 0.01 . 274 57 58 SER N N 115.700 0.02 . 275 58 59 CYS H H 8.518 0.02 . 276 58 59 CYS C C 173.821 0.00 . 277 58 59 CYS CA C 54.938 0.06 . 278 58 59 CYS CB C 37.020 0.00 . 279 58 59 CYS N N 124.500 0.06 . 280 59 60 VAL H H 9.267 0.02 . 281 59 60 VAL C C 174.488 0.01 . 282 59 60 VAL CA C 59.168 0.06 . 283 59 60 VAL CB C 36.944 0.11 . 284 59 60 VAL N N 122.653 0.03 . 285 60 61 SER H H 8.271 0.03 . 286 60 61 SER C C 173.536 0.01 . 287 60 61 SER CA C 59.365 0.01 . 288 60 61 SER CB C 64.605 0.03 . 289 60 61 SER N N 114.809 0.03 . 290 61 62 GLN H H 8.752 0.01 . 291 61 62 GLN C C 173.503 0.03 . 292 61 62 GLN CA C 56.338 0.00 . 293 61 62 GLN CB C 29.241 0.00 . 294 61 62 GLN N N 122.844 0.04 . 295 62 63 ASP H H 7.430 0.01 . 296 62 63 ASP C C 174.197 0.01 . 297 62 63 ASP CA C 54.575 0.01 . 298 62 63 ASP CB C 42.455 0.02 . 299 62 63 ASP N N 117.993 0.04 . 300 63 64 LEU H H 8.499 0.03 . 301 63 64 LEU C C 176.611 0.00 . 302 63 64 LEU CA C 53.967 0.08 . 303 63 64 LEU CB C 46.685 0.04 . 304 63 64 LEU N N 123.442 0.02 . 305 64 65 GLU H H 9.499 0.01 . 306 64 65 GLU C C 174.008 0.00 . 307 64 65 GLU CA C 53.548 0.00 . 308 64 65 GLU CB C 33.335 0.00 . 309 64 65 GLU N N 121.059 0.06 . 310 65 66 PRO C C 174.679 0.00 . 311 65 66 PRO CA C 62.017 0.05 . 312 65 66 PRO CB C 34.157 0.00 . 313 66 67 LEU H H 8.432 0.01 . 314 66 67 LEU C C 175.423 0.01 . 315 66 67 LEU CA C 53.665 0.02 . 316 66 67 LEU CB C 47.568 0.03 . 317 66 67 LEU N N 118.975 0.04 . 318 67 68 THR H H 8.502 0.03 . 319 67 68 THR C C 173.476 0.01 . 320 67 68 THR CA C 63.440 0.13 . 321 67 68 THR CB C 68.793 0.04 . 322 67 68 THR N N 125.128 0.07 . 323 68 69 ILE H H 8.935 0.01 . 324 68 69 ILE C C 172.848 0.02 . 325 68 69 ILE CA C 59.146 0.05 . 326 68 69 ILE CB C 42.578 0.09 . 327 68 69 ILE N N 119.266 0.04 . 328 69 70 LEU H H 8.807 0.01 . 329 69 70 LEU C C 175.585 0.02 . 330 69 70 LEU CA C 53.858 0.11 . 331 69 70 LEU CB C 46.485 0.06 . 332 69 70 LEU N N 121.362 0.10 . 333 70 71 TYR H H 9.233 0.02 . 334 70 71 TYR C C 170.570 0.01 . 335 70 71 TYR CA C 55.765 0.05 . 336 70 71 TYR CB C 41.645 0.11 . 337 70 71 TYR N N 125.707 0.06 . 338 71 72 TYR H H 8.998 0.04 . 339 71 72 TYR C C 176.327 0.01 . 340 71 72 TYR CA C 57.486 0.08 . 341 71 72 TYR CB C 41.449 0.06 . 342 71 72 TYR N N 118.581 0.03 . 343 72 73 ILE H H 8.268 0.00 . 344 72 73 ILE C C 177.370 0.01 . 345 72 73 ILE CA C 60.347 0.02 . 346 72 73 ILE CB C 38.417 0.11 . 347 72 73 ILE N N 121.664 0.03 . 348 73 74 GLY H H 8.960 0.03 . 349 73 74 GLY C C 174.653 0.04 . 350 73 74 GLY CA C 47.362 0.04 . 351 73 74 GLY N N 118.805 0.08 . 352 74 75 LYS H H 8.789 0.03 . 353 74 75 LYS C C 175.171 0.01 . 354 74 75 LYS CA C 53.143 0.10 . 355 74 75 LYS CB C 39.094 0.10 . 356 74 75 LYS N N 124.107 0.07 . 357 75 76 THR H H 8.316 0.02 . 358 75 76 THR C C 171.372 0.00 . 359 75 76 THR CA C 60.453 0.00 . 360 75 76 THR CB C 70.833 0.00 . 361 75 76 THR N N 119.131 0.11 . 362 76 77 PRO C C 175.433 0.00 . 363 76 77 PRO CA C 61.861 0.10 . 364 76 77 PRO CB C 32.109 0.05 . 365 77 78 LYS H H 8.673 0.01 . 366 77 78 LYS C C 173.495 0.00 . 367 77 78 LYS CA C 54.202 0.07 . 368 77 78 LYS CB C 34.191 0.03 . 369 77 78 LYS N N 122.701 0.09 . 370 78 79 ILE H H 7.851 0.03 . 371 78 79 ILE C C 176.220 0.00 . 372 78 79 ILE CA C 59.406 0.04 . 373 78 79 ILE CB C 39.652 0.03 . 374 78 79 ILE N N 121.673 0.02 . 375 79 80 GLU H H 8.695 0.00 . 376 79 80 GLU C C 173.630 0.00 . 377 79 80 GLU CA C 54.572 0.06 . 378 79 80 GLU CB C 34.977 0.03 . 379 79 80 GLU N N 125.840 0.03 . 380 80 81 GLN H H 8.832 0.03 . 381 80 81 GLN C C 175.201 0.01 . 382 80 81 GLN CA C 55.128 0.09 . 383 80 81 GLN CB C 30.923 0.02 . 384 80 81 GLN N N 121.437 0.13 . 385 81 82 LEU H H 9.184 0.02 . 386 81 82 LEU C C 176.083 0.03 . 387 81 82 LEU CA C 53.546 0.09 . 388 81 82 LEU CB C 42.720 0.09 . 389 81 82 LEU N N 126.618 0.06 . 390 82 83 SER H H 8.560 0.03 . 391 82 83 SER C C 174.368 0.00 . 392 82 83 SER CA C 59.594 0.09 . 393 82 83 SER CB C 63.922 0.04 . 394 82 83 SER N N 119.308 0.06 . 395 83 84 ASN H H 8.652 0.02 . 396 83 84 ASN C C 173.162 0.01 . 397 83 84 ASN CA C 54.715 0.07 . 398 83 84 ASN CB C 36.340 0.05 . 399 83 84 ASN N N 115.272 0.02 . 400 84 85 MET H H 7.133 0.01 . 401 84 85 MET C C 175.916 0.01 . 402 84 85 MET CA C 55.281 0.05 . 403 84 85 MET CB C 34.542 0.11 . 404 84 85 MET N N 113.699 0.05 . 405 85 86 ILE H H 8.578 0.02 . 406 85 86 ILE C C 175.275 0.02 . 407 85 86 ILE CA C 60.657 0.02 . 408 85 86 ILE CB C 41.737 0.13 . 409 85 86 ILE N N 120.432 0.02 . 410 86 87 VAL H H 9.490 0.01 . 411 86 87 VAL C C 174.918 0.00 . 412 86 87 VAL CA C 63.353 0.14 . 413 86 87 VAL CB C 31.797 0.03 . 414 86 87 VAL N N 127.757 0.06 . 415 87 88 LYS H H 8.815 0.01 . 416 87 88 LYS C C 176.202 0.01 . 417 87 88 LYS CA C 55.466 0.10 . 418 87 88 LYS CB C 34.401 0.03 . 419 87 88 LYS N N 125.559 0.02 . 420 88 89 SER H H 7.939 0.01 . 421 88 89 SER C C 173.638 0.01 . 422 88 89 SER CA C 57.517 0.11 . 423 88 89 SER CB C 65.679 0.03 . 424 88 89 SER N N 110.812 0.03 . 425 89 90 CYS H H 7.987 0.02 . 426 89 90 CYS C C 172.094 0.01 . 427 89 90 CYS CA C 53.955 0.07 . 428 89 90 CYS CB C 44.474 0.06 . 429 89 90 CYS N N 117.471 0.09 . 430 90 91 LYS H H 9.425 0.01 . 431 90 91 LYS C C 173.334 0.01 . 432 90 91 LYS CA C 55.630 0.07 . 433 90 91 LYS CB C 35.433 0.01 . 434 90 91 LYS N N 117.207 0.09 . 435 91 92 CYS H H 8.396 0.03 . 436 91 92 CYS C C 175.195 0.01 . 437 91 92 CYS CA C 56.208 0.07 . 438 91 92 CYS CB C 42.562 0.06 . 439 91 92 CYS N N 118.387 0.02 . 440 92 93 SER H H 9.185 0.01 . 441 92 93 SER C C 178.389 0.00 . 442 92 93 SER CA C 59.891 0.00 . 443 92 93 SER CB C 66.108 0.00 . 444 92 93 SER N N 125.607 0.02 . stop_ save_