data_26944 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; mini monomeric TGF-b2-7m ; _BMRB_accession_number 26944 _BMRB_flat_file_name bmr26944.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 and bearing seven single amino acid substitutions that engender the protein with high affinity TbRII binding. ; loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Hinck Andrew P. . 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" 271 "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 26943 'engineered TGF-b2 monomer' 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 Cano 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-b2-7m _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label mmTGF-b2-7m $mmTGF-b2-7M 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-b2-7M _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common mmTGF-b2-7M _Molecular_mass . _Mol_thiol_state 'all disulfide bound' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 93 _Mol_residue_sequence ; MALDAAYCFRNVQDNCCLRP LYIDFRKDLGWKWIHEPKGY NANFCAGACPYRNSKSPSCV SQDLEPLTIVYYVGRKPKVE 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 ARG 27 26 LYS 28 27 ASP 29 28 LEU 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 VAL 71 70 TYR 72 71 TYR 73 72 VAL 74 73 GLY 75 74 ARG 76 75 LYS 77 76 PRO 78 77 LYS 79 78 VAL 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-b2-7M 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 existThis 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-b2-7M '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-b2-7M 0.2 mM '[U-99% 13C; U-99% 15N]' D2O 5 mM '[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 . save_ save_TOPSPIN _Saveframe_category software _Name TOPSPIN _Version . loop_ _Vendor _Address _Electronic_address 'Bruker Biospin' . . stop_ loop_ _Task collection stop_ _Details . save_ save_SPARKY _Saveframe_category software _Name SPARKY _Version NMRFAM-SPARKY loop_ _Vendor _Address _Electronic_address Goddard . . stop_ loop_ _Task 'data analysis' 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_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model Avance _Field_strength 700 _Details AV-I 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 . 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 . . . 1.0 DSS N 15 'methyl protons' ppm 0.0 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_ _Software_label $NMRPipe $TOPSPIN $SPARKY $PINE 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-b2-7m _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 8.758 0.01 . 2 1 2 ALA C C 173.376 0.01 . 3 1 2 ALA CA C 51.654 0.09 . 4 1 2 ALA CB C 19.503 0.02 . 5 1 2 ALA N N 120.946 0.00 . 6 2 3 LEU H H 8.717 0.00 . 7 2 3 LEU C C 174.925 0.01 . 8 2 3 LEU CA C 53.145 0.02 . 9 2 3 LEU CB C 39.627 0.03 . 10 2 3 LEU N N 121.225 0.01 . 11 3 4 ASP H H 7.808 0.00 . 12 3 4 ASP C C 176.038 0.01 . 13 3 4 ASP CA C 51.392 0.04 . 14 3 4 ASP CB C 42.922 0.02 . 15 3 4 ASP N N 121.489 0.01 . 16 4 5 ALA H H 8.558 0.00 . 17 4 5 ALA C C 179.135 0.02 . 18 4 5 ALA CA C 55.541 0.04 . 19 4 5 ALA CB C 18.732 0.01 . 20 4 5 ALA N N 123.071 0.01 . 21 5 6 ALA H H 7.705 0.00 . 22 5 6 ALA C C 179.119 0.01 . 23 5 6 ALA CA C 54.660 0.02 . 24 5 6 ALA CB C 18.126 0.02 . 25 5 6 ALA N N 119.384 0.01 . 26 6 7 TYR H H 7.690 0.00 . 27 6 7 TYR C C 178.236 0.01 . 28 6 7 TYR CA C 60.281 0.04 . 29 6 7 TYR CB C 40.282 0.01 . 30 6 7 TYR N N 115.540 0.01 . 31 7 8 CYS H H 8.891 0.00 . 32 7 8 CYS C C 176.341 0.02 . 33 7 8 CYS CA C 57.218 0.02 . 34 7 8 CYS CB C 40.467 0.02 . 35 7 8 CYS N N 115.253 0.01 . 36 8 9 PHE H H 8.467 0.00 . 37 8 9 PHE C C 176.673 0.01 . 38 8 9 PHE CA C 56.246 0.08 . 39 8 9 PHE CB C 35.923 0.01 . 40 8 9 PHE N N 117.297 0.01 . 41 9 10 ARG H H 7.193 0.00 . 42 9 10 ARG C C 175.141 0.00 . 43 9 10 ARG CA C 56.541 0.06 . 44 9 10 ARG CB C 30.999 0.00 . 45 9 10 ARG N N 116.655 0.01 . 46 10 11 ASN H H 7.445 0.00 . 47 10 11 ASN C C 173.543 0.00 . 48 10 11 ASN CA C 52.541 0.05 . 49 10 11 ASN CB C 39.509 0.03 . 50 10 11 ASN N N 117.981 0.02 . 51 11 12 VAL H H 8.148 0.00 . 52 11 12 VAL C C 134.153 72.75 . 53 11 12 VAL CA C 63.693 0.06 . 54 11 12 VAL CB C 31.367 0.02 . 55 11 12 VAL N N 121.890 0.01 . 56 12 13 GLN H H 8.500 0.00 . 57 12 13 GLN C C 175.653 0.01 . 58 12 13 GLN CA C 54.491 0.04 . 59 12 13 GLN CB C 31.245 0.04 . 60 12 13 GLN N N 124.453 0.03 . 61 13 14 ASP H H 8.697 0.00 . 62 13 14 ASP C C 176.966 0.01 . 63 13 14 ASP CA C 55.446 0.05 . 64 13 14 ASP CB C 40.954 0.03 . 65 13 14 ASP N N 120.889 0.01 . 66 14 15 ASN H H 7.668 0.00 . 67 14 15 ASN C C 174.053 0.01 . 68 14 15 ASN CA C 53.450 0.02 . 69 14 15 ASN CB C 39.400 0.03 . 70 14 15 ASN N N 117.507 0.01 . 71 15 16 CYS H H 8.592 0.00 . 72 15 16 CYS C C 172.307 0.01 . 73 15 16 CYS CA C 55.419 0.02 . 74 15 16 CYS CB C 35.210 0.02 . 75 15 16 CYS N N 116.245 0.01 . 76 16 17 CYS H H 8.142 0.00 . 77 16 17 CYS C C 171.262 0.01 . 78 16 17 CYS CA C 59.275 0.05 . 79 16 17 CYS CB C 39.686 0.03 . 80 16 17 CYS N N 125.056 0.02 . 81 17 18 LEU H H 7.657 0.00 . 82 17 18 LEU C C 174.636 0.01 . 83 17 18 LEU CA C 55.632 0.03 . 84 17 18 LEU CB C 43.840 0.03 . 85 17 18 LEU N N 125.399 0.01 . 86 18 19 ARG H H 9.170 0.00 . 87 18 19 ARG C C 173.071 0.00 . 88 18 19 ARG CA C 50.634 0.00 . 89 18 19 ARG CB C 29.897 0.00 . 90 18 19 ARG N N 125.881 0.01 . 91 19 20 PRO C C 177.034 0.01 . 92 19 20 PRO CA C 62.126 0.06 . 93 19 20 PRO CB C 31.856 0.02 . 94 20 21 LEU H H 7.756 0.00 . 95 20 21 LEU C C 173.411 0.01 . 96 20 21 LEU CA C 56.713 0.01 . 97 20 21 LEU CB C 44.739 0.03 . 98 20 21 LEU N N 119.380 0.02 . 99 21 22 TYR H H 8.724 0.00 . 100 21 22 TYR C C 173.837 0.01 . 101 21 22 TYR CA C 56.800 0.04 . 102 21 22 TYR CB C 39.693 0.02 . 103 21 22 TYR N N 131.325 0.01 . 104 22 23 ILE H H 7.855 0.00 . 105 22 23 ILE C C 172.299 0.00 . 106 22 23 ILE CA C 58.264 0.04 . 107 22 23 ILE CB C 39.082 0.03 . 108 22 23 ILE N N 128.067 0.02 . 109 23 24 ASP H H 9.265 0.00 . 110 23 24 ASP C C 177.380 0.01 . 111 23 24 ASP CA C 52.682 0.04 . 112 23 24 ASP CB C 44.429 0.03 . 113 23 24 ASP N N 127.811 0.02 . 114 24 25 PHE H H 8.281 0.00 . 115 24 25 PHE C C 177.868 0.01 . 116 24 25 PHE CA C 63.370 0.10 . 117 24 25 PHE CB C 38.480 0.00 . 118 24 25 PHE N N 125.316 0.02 . 119 25 26 ARG H H 8.748 0.00 . 120 25 26 ARG C C 178.544 0.00 . 121 25 26 ARG CA C 59.945 0.04 . 122 25 26 ARG CB C 30.589 0.01 . 123 25 26 ARG N N 119.294 0.01 . 124 26 27 LYS H H 8.871 0.00 . 125 26 27 LYS C C 177.618 0.01 . 126 26 27 LYS CA C 59.220 0.08 . 127 26 27 LYS CB C 33.508 0.07 . 128 26 27 LYS N N 107.008 28.87 . 129 27 28 ASP H H 8.197 0.45 . 130 27 28 ASP C C 176.891 0.00 . 131 27 28 ASP CA C 56.637 0.04 . 132 27 28 ASP CB C 41.550 0.02 . 133 27 28 ASP N N 114.069 0.04 . 134 28 29 LEU H H 6.553 0.00 . 135 28 29 LEU CA C 115.689 50.02 . 136 28 29 LEU CB C 41.487 0.00 . 137 28 29 LEU N N 113.558 0.05 . 138 29 30 GLY H H 7.230 0.00 . 139 29 30 GLY C C 175.629 0.01 . 140 29 30 GLY CA C 46.352 0.03 . 141 29 30 GLY N N 106.665 0.02 . 142 30 31 TRP H H 8.087 0.00 . 143 30 31 TRP C C 176.348 0.01 . 144 30 31 TRP CA C 54.435 0.03 . 145 30 31 TRP CB C 29.263 0.02 . 146 30 31 TRP N N 122.613 0.02 . 147 31 32 LYS H H 8.605 0.00 . 148 31 32 LYS C C 175.925 0.00 . 149 31 32 LYS CA C 57.355 0.04 . 150 31 32 LYS CB C 32.680 0.01 . 151 31 32 LYS N N 121.610 0.03 . 152 32 33 TRP H H 7.158 0.00 . 153 32 33 TRP C C 175.848 0.01 . 154 32 33 TRP CA C 55.847 0.02 . 155 32 33 TRP CB C 29.118 0.01 . 156 32 33 TRP N N 114.770 0.00 . 157 33 34 ILE H H 6.917 0.00 . 158 33 34 ILE C C 175.440 0.01 . 159 33 34 ILE CA C 62.291 0.05 . 160 33 34 ILE CB C 37.889 0.05 . 161 33 34 ILE N N 121.885 0.01 . 162 34 35 HIS H H 9.092 0.01 . 163 34 35 HIS C C 174.313 0.01 . 164 34 35 HIS CA C 58.057 0.05 . 165 34 35 HIS CB C 30.995 0.02 . 166 34 35 HIS N N 127.360 0.03 . 167 35 36 GLU H H 7.917 0.00 . 168 35 36 GLU C C 172.952 0.00 . 169 35 36 GLU CA C 53.816 0.00 . 170 35 36 GLU CB C 33.769 0.00 . 171 35 36 GLU N N 117.405 0.02 . 172 36 37 PRO C C 175.469 0.01 . 173 36 37 PRO CA C 62.725 0.03 . 174 36 37 PRO CB C 34.768 0.00 . 175 37 38 LYS H H 8.784 0.00 . 176 37 38 LYS C C 177.127 0.01 . 177 37 38 LYS CA C 57.874 0.04 . 178 37 38 LYS CB C 32.564 0.01 . 179 37 38 LYS N N 116.311 0.01 . 180 38 39 GLY H H 7.714 0.00 . 181 38 39 GLY C C 170.498 0.00 . 182 38 39 GLY CA C 46.015 0.04 . 183 38 39 GLY N N 105.999 0.00 . 184 39 40 TYR H H 8.230 0.00 . 185 39 40 TYR C C 171.526 0.01 . 186 39 40 TYR CA C 55.870 0.04 . 187 39 40 TYR CB C 40.762 0.02 . 188 39 40 TYR N N 117.077 0.01 . 189 40 41 ASN H H 8.575 0.00 . 190 40 41 ASN C C 171.981 0.01 . 191 40 41 ASN CA C 53.189 0.03 . 192 40 41 ASN CB C 38.416 0.04 . 193 40 41 ASN N N 119.928 0.02 . 194 41 42 ALA H H 7.315 0.00 . 195 41 42 ALA C C 177.190 0.01 . 196 41 42 ALA CA C 55.133 0.03 . 197 41 42 ALA CB C 21.589 0.04 . 198 41 42 ALA N N 130.957 0.02 . 199 42 43 ASN H H 7.680 0.00 . 200 42 43 ASN C C 170.775 0.00 . 201 42 43 ASN CA C 54.986 0.05 . 202 42 43 ASN CB C 40.532 0.01 . 203 42 43 ASN N N 131.426 0.00 . 204 43 44 PHE H H 8.161 0.00 . 205 43 44 PHE C C 172.718 0.00 . 206 43 44 PHE CA C 57.394 0.05 . 207 43 44 PHE CB C 40.025 0.05 . 208 43 44 PHE N N 107.352 0.02 . 209 44 45 CYS H H 8.745 0.00 . 210 44 45 CYS C C 173.458 0.01 . 211 44 45 CYS CA C 54.443 0.04 . 212 44 45 CYS CB C 42.564 0.03 . 213 44 45 CYS N N 118.914 0.01 . 214 45 46 ALA H H 8.087 0.00 . 215 45 46 ALA C C 176.382 0.00 . 216 45 46 ALA CA C 52.931 0.04 . 217 45 46 ALA CB C 23.522 0.00 . 218 45 46 ALA N N 121.377 0.02 . 219 46 47 GLY H H 8.994 0.00 . 220 46 47 GLY C C 172.254 0.00 . 221 46 47 GLY CA C 43.740 0.02 . 222 46 47 GLY N N 111.944 0.01 . 223 47 48 ALA H H 8.003 0.00 . 224 47 48 ALA C C 178.298 0.01 . 225 47 48 ALA CA C 53.518 0.03 . 226 47 48 ALA CB C 19.850 0.03 . 227 47 48 ALA N N 120.362 0.01 . 228 48 49 CYS H H 8.528 0.00 . 229 48 49 CYS C C 171.811 0.00 . 230 48 49 CYS CA C 53.867 0.00 . 231 48 49 CYS CB C 44.006 0.00 . 232 48 49 CYS N N 120.381 0.01 . 233 49 50 PRO C C 175.812 0.00 . 234 49 50 PRO CA C 63.048 0.04 . 235 49 50 PRO CB C 31.968 0.00 . 236 50 51 TYR H H 8.248 0.00 . 237 50 51 TYR C C 175.837 0.01 . 238 50 51 TYR CA C 58.686 0.03 . 239 50 51 TYR CB C 38.809 0.03 . 240 50 51 TYR N N 121.209 0.01 . 241 51 52 ARG H H 7.844 0.00 . 242 51 52 ARG C C 174.763 0.00 . 243 51 52 ARG CA C 55.265 0.05 . 244 51 52 ARG CB C 32.443 0.02 . 245 51 52 ARG N N 124.197 0.01 . 246 52 53 ASN H H 8.370 0.00 . 247 52 53 ASN C C 177.496 0.00 . 248 52 53 ASN CA C 53.478 0.03 . 249 52 53 ASN CB C 18.551 0.01 . 250 52 53 ASN N N 125.149 0.01 . 251 53 54 SER H H 8.054 0.00 . 252 53 54 SER C C 173.930 0.00 . 253 53 54 SER CA C 60.283 1.55 . 254 53 54 SER CB C 63.226 0.03 . 255 53 54 SER N N 111.717 0.01 . 256 54 55 LYS H H 7.867 0.00 . 257 54 55 LYS C C 175.323 0.01 . 258 54 55 LYS CA C 55.858 0.04 . 259 54 55 LYS CB C 33.639 0.00 . 260 54 55 LYS N N 120.801 0.01 . 261 55 56 SER H H 8.422 0.00 . 262 55 56 SER C C 172.624 0.00 . 263 55 56 SER CA C 56.146 0.00 . 264 55 56 SER CB C 63.263 0.00 . 265 55 56 SER N N 118.618 0.01 . 266 56 57 PRO C C 175.930 0.01 . 267 56 57 PRO CA C 62.683 0.03 . 268 56 57 PRO CB C 32.839 0.01 . 269 57 58 SER H H 8.738 0.00 . 270 57 58 SER C C 172.111 0.01 . 271 57 58 SER CA C 57.611 0.04 . 272 57 58 SER CB C 65.732 0.03 . 273 57 58 SER N N 115.744 0.01 . 274 58 59 CYS H H 8.534 0.00 . 275 58 59 CYS C C 173.848 0.00 . 276 58 59 CYS CA C 54.738 0.02 . 277 58 59 CYS CB C 36.983 0.03 . 278 58 59 CYS N N 124.543 0.01 . 279 59 60 VAL H H 9.284 0.00 . 280 59 60 VAL C C 174.533 0.01 . 281 59 60 VAL CA C 59.057 0.05 . 282 59 60 VAL CB C 36.890 0.05 . 283 59 60 VAL N N 122.751 0.01 . 284 60 61 SER H H 8.281 0.00 . 285 60 61 SER C C 173.597 0.00 . 286 60 61 SER CA C 59.282 0.04 . 287 60 61 SER CB C 64.439 0.03 . 288 60 61 SER N N 114.850 0.01 . 289 61 62 GLN H H 8.774 0.00 . 290 61 62 GLN C C 173.571 0.00 . 291 61 62 GLN CA C 56.168 0.00 . 292 61 62 GLN CB C 36.006 10.36 . 293 61 62 GLN N N 122.886 0.02 . 294 62 63 ASP H H 7.434 0.00 . 295 62 63 ASP C C 174.220 0.01 . 296 62 63 ASP CA C 54.452 0.03 . 297 62 63 ASP CB C 42.287 0.03 . 298 62 63 ASP N N 118.005 0.01 . 299 63 64 LEU H H 8.501 0.00 . 300 63 64 LEU C C 176.622 0.00 . 301 63 64 LEU CA C 51.487 3.03 . 302 63 64 LEU CB C 49.046 2.99 . 303 63 64 LEU N N 123.606 0.02 . 304 64 65 GLU H H 9.521 0.00 . 305 64 65 GLU C C 174.049 0.00 . 306 64 65 GLU CA C 53.213 0.00 . 307 64 65 GLU CB C 33.178 0.00 . 308 64 65 GLU N N 121.047 0.01 . 309 65 66 PRO C C 174.690 0.01 . 310 65 66 PRO CA C 61.901 0.04 . 311 65 66 PRO CB C 34.031 0.03 . 312 66 67 LEU H H 8.468 0.00 . 313 66 67 LEU C C 175.528 0.02 . 314 66 67 LEU CA C 53.344 0.04 . 315 66 67 LEU CB C 47.497 0.02 . 316 66 67 LEU N N 119.102 0.02 . 317 67 68 THR H H 8.574 0.00 . 318 67 68 THR C C 173.780 0.00 . 319 67 68 THR CA C 63.564 0.08 . 320 67 68 THR CB C 68.953 0.06 . 321 67 68 THR N N 125.040 0.02 . 322 68 69 ILE H H 9.071 0.00 . 323 68 69 ILE C C 173.743 0.00 . 324 68 69 ILE CA C 58.797 0.04 . 325 68 69 ILE CB C 42.500 0.02 . 326 68 69 ILE N N 120.803 0.01 . 327 69 70 VAL H H 8.798 0.00 . 328 69 70 VAL C C 175.839 0.01 . 329 69 70 VAL CA C 60.630 0.06 . 330 69 70 VAL CB C 34.944 0.01 . 331 69 70 VAL N N 118.976 0.02 . 332 70 71 TYR H H 9.020 0.00 . 333 70 71 TYR C C 171.586 0.00 . 334 70 71 TYR CA C 55.624 0.05 . 335 70 71 TYR CB C 41.492 0.02 . 336 70 71 TYR N N 125.624 0.02 . 337 71 72 TYR H H 9.181 0.01 . 338 71 72 TYR C C 176.296 0.00 . 339 71 72 TYR CA C 57.751 0.05 . 340 71 72 TYR CB C 40.425 0.01 . 341 71 72 TYR N N 119.895 0.01 . 342 72 73 VAL H H 8.455 0.00 . 343 72 73 VAL C C 177.305 0.01 . 344 72 73 VAL CA C 61.820 0.06 . 345 72 73 VAL CB C 32.515 0.03 . 346 72 73 VAL N N 122.491 0.01 . 347 73 74 GLY H H 8.984 0.00 . 348 73 74 GLY C C 174.837 0.01 . 349 73 74 GLY CA C 47.139 0.02 . 350 73 74 GLY N N 118.628 0.01 . 351 74 75 ARG H H 8.821 0.00 . 352 74 75 ARG C C 175.564 0.01 . 353 74 75 ARG CA C 56.289 0.04 . 354 74 75 ARG CB C 29.867 0.03 . 355 74 75 ARG N N 121.388 0.02 . 356 75 76 LYS H H 7.871 0.00 . 357 75 76 LYS C C 173.305 0.00 . 358 75 76 LYS CA C 53.229 0.00 . 359 75 76 LYS CB C 34.102 0.00 . 360 75 76 LYS N N 121.269 0.01 . 361 76 77 PRO C C 176.004 0.00 . 362 76 77 PRO CA C 61.955 0.06 . 363 76 77 PRO CB C 31.601 0.02 . 364 77 78 LYS H H 8.840 0.00 . 365 77 78 LYS C C 173.342 0.01 . 366 77 78 LYS CA C 54.658 0.04 . 367 77 78 LYS CB C 34.344 0.03 . 368 77 78 LYS N N 124.849 0.01 . 369 78 79 VAL H H 7.927 0.00 . 370 78 79 VAL C C 176.428 0.01 . 371 78 79 VAL CA C 60.927 0.05 . 372 78 79 VAL CB C 33.091 0.06 . 373 78 79 VAL N N 122.738 0.01 . 374 79 80 GLU H H 9.039 0.00 . 375 79 80 GLU C C 173.645 0.00 . 376 79 80 GLU CA C 54.578 0.04 . 377 79 80 GLU CB C 34.496 0.01 . 378 79 80 GLU N N 127.213 0.02 . 379 80 81 GLN H H 8.755 0.00 . 380 80 81 GLN C C 175.273 0.01 . 381 80 81 GLN CA C 54.976 0.04 . 382 80 81 GLN CB C 30.584 0.01 . 383 80 81 GLN N N 121.877 0.01 . 384 81 82 LEU H H 9.196 0.00 . 385 81 82 LEU C C 176.131 0.00 . 386 81 82 LEU CA C 53.296 0.02 . 387 81 82 LEU CB C 42.701 0.02 . 388 81 82 LEU N N 126.814 0.01 . 389 82 83 SER H H 8.568 0.00 . 390 82 83 SER C C 174.327 0.02 . 391 82 83 SER CA C 59.512 0.08 . 392 82 83 SER CB C 63.839 0.05 . 393 82 83 SER N N 119.245 0.01 . 394 83 84 ASN H H 8.680 0.00 . 395 83 84 ASN C C 173.172 0.01 . 396 83 84 ASN CA C 54.606 0.07 . 397 83 84 ASN CB C 36.316 0.02 . 398 83 84 ASN N N 115.378 0.01 . 399 84 85 MET H H 7.181 0.00 . 400 84 85 MET C C 175.909 0.01 . 401 84 85 MET CA C 55.159 0.03 . 402 84 85 MET CB C 34.675 0.05 . 403 84 85 MET N N 113.720 0.02 . 404 85 86 ILE H H 8.573 0.00 . 405 85 86 ILE C C 175.347 0.01 . 406 85 86 ILE CA C 60.578 0.01 . 407 85 86 ILE CB C 41.859 0.02 . 408 85 86 ILE N N 120.439 0.01 . 409 86 87 VAL H H 9.513 0.00 . 410 86 87 VAL C C 174.983 0.01 . 411 86 87 VAL CA C 63.086 0.06 . 412 86 87 VAL CB C 31.928 0.03 . 413 86 87 VAL N N 127.805 0.00 . 414 87 88 LYS H H 8.836 0.00 . 415 87 88 LYS C C 176.197 0.01 . 416 87 88 LYS CA C 55.290 0.01 . 417 87 88 LYS CB C 34.407 0.01 . 418 87 88 LYS N N 125.546 0.02 . 419 88 89 SER H H 7.945 0.00 . 420 88 89 SER C C 173.625 0.00 . 421 88 89 SER CA C 57.477 0.06 . 422 88 89 SER CB C 65.564 0.03 . 423 88 89 SER N N 110.783 0.01 . 424 89 90 CYS H H 8.024 0.00 . 425 89 90 CYS C C 172.171 0.00 . 426 89 90 CYS CA C 53.888 0.03 . 427 89 90 CYS CB C 44.402 0.03 . 428 89 90 CYS N N 117.553 0.01 . 429 90 91 LYS H H 9.437 0.00 . 430 90 91 LYS C C 173.384 0.01 . 431 90 91 LYS CA C 55.550 0.01 . 432 90 91 LYS CB C 35.320 0.02 . 433 90 91 LYS N N 117.274 0.00 . 434 91 92 CYS H H 8.410 0.00 . 435 91 92 CYS C C 175.182 0.01 . 436 91 92 CYS CA C 56.037 0.03 . 437 91 92 CYS CB C 42.495 0.01 . 438 91 92 CYS N N 118.452 0.01 . 439 92 93 SER H H 9.199 0.00 . 440 92 93 SER C C 178.365 0.00 . 441 92 93 SER CA C 59.869 0.00 . 442 92 93 SER CB C 65.893 0.00 . 443 92 93 SER N N 125.644 0.00 . stop_ save_