data_6522 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Characterization of an amyloid fibril intermediate ; _BMRB_accession_number 6522 _BMRB_flat_file_name bmr6522.str _Entry_type original _Submission_date 2005-02-23 _Accession_date 2005-02-23 _Entry_origination author _NMR_STAR_version 2.1.1 _Experimental_method NMR _Details 'Backbone residue assignments were used for H/D exchange, pKa and stability studies of p53tet-R337H' loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Galea Charles A. . 2 Bowman Prentice . . 3 Kriwacki Richard W. . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 2 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 95 "13C chemical shifts" 105 "15N chemical shifts" 95 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2007-01-29 original BMRB . stop_ loop_ _Related_BMRB_accession_number _Relationship 4048 'Data were collected at a different pH for this molecular system.' 6521 'p53 tetramer' stop_ _Original_release_date 2005-02-23 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; Disruption of an intermonomer salt bridge in the p53 tetramerization domain results in an increased propensity to form amyloid fibrils. ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 16260757 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Galea Charles A. . 2 Bowman Prentice . . 3 Kriwacki Richard W. . stop_ _Journal_abbreviation 'Protein Sci.' _Journal_volume 14 _Journal_issue 12 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 2993 _Page_last 3003 _Year 2005 _Details . loop_ _Keyword 'H/D exchange' 'Mutant p53 tetramerization domain' R337H 'amyloid fibril intermediate' p53tet-R337H 'pKa studies' 'tumor supressor protein' stop_ save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name 'Mutant p53 tetramerization domain (p53tet-R337H)' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'subunit A' $Mutant_p53_tetramerization_domain_polypeptide 'subunit B' $Mutant_p53_tetramerization_domain_polypeptide 'subunit C' $Mutant_p53_tetramerization_domain_polypeptide 'subunit D' $Mutant_p53_tetramerization_domain_polypeptide stop_ _System_molecular_weight 24527 _System_physical_state native _System_oligomer_state 'protein-protein complex' _System_paramagnetic no _System_thiol_state 'not present' loop_ _Magnetic_equivalence_ID _Magnetically_equivalent_system_component 1 'subunit A' 1 'subunit B' 1 'subunit C' 1 'subunit D' stop_ loop_ _Biological_function 'Transcription factor' stop_ _Database_query_date . _Details Homotetramer save_ ######################## # Monomeric polymers # ######################## save_Mutant_p53_tetramerization_domain_polypeptide _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common Mutant_p53_tetramerization_domain_polypeptide _Molecular_mass 6131.8 _Mol_thiol_state 'not present' loop_ _Biological_function 'transcription factor' stop_ _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 54 _Mol_residue_sequence ; GSHMNTSSSPQPKKKPLDGE YFTLQIRGRERFEMFRELNE ALELKDAQAGKEPG ; loop_ _Residue_seq_code _Residue_label 1 GLY 2 SER 3 HIS 4 MET 5 ASN 6 THR 7 SER 8 SER 9 SER 10 PRO 11 GLN 12 PRO 13 LYS 14 LYS 15 LYS 16 PRO 17 LEU 18 ASP 19 GLY 20 GLU 21 TYR 22 PHE 23 THR 24 LEU 25 GLN 26 ILE 27 ARG 28 GLY 29 ARG 30 GLU 31 ARG 32 PHE 33 GLU 34 MET 35 PHE 36 ARG 37 GLU 38 LEU 39 ASN 40 GLU 41 ALA 42 LEU 43 GLU 44 LEU 45 LYS 46 ASP 47 ALA 48 GLN 49 ALA 50 GLY 51 LYS 52 GLU 53 PRO 54 GLY 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 $Mutant_p53_tetramerization_domain_polypeptide 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 _Variant _Vector_name $Mutant_p53_tetramerization_domain_polypeptide 'recombinant technology' 'E. coli' Escherichia coli BL21 DE3 . 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 $Mutant_p53_tetramerization_domain_polypeptide 4.0 mM [U-15N] Na2HPO4 10.0 mM . NaCl 50.0 mM . NaN3 0.02 % . stop_ save_ save_sample_2 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $Mutant_p53_tetramerization_domain_polypeptide 4.0 mM 'U-13C; U-15N' Na2HPO4 10.0 mM . NaCl 50.0 mM . NaN3 0.02 % . stop_ save_ ############################ # Computer software used # ############################ save_software_1 _Saveframe_category software _Name Felix _Version . loop_ _Vendor _Address _Electronic_address Accelrys 'Accelrys, Inc. 10188 Telesis Court, Suite 100 San Diego, CA 92121 USA Phone: +1 858 799 5000 Fax: +1 858 799 5100' http://www.accelrys.com/ stop_ loop_ _Task 'Chemical Shift Assignments' stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_600MHz_spectrometer _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model 'INOVA 600' _Field_strength 600 _Details . save_ ############################# # NMR applied experiments # ############################# save_1H15N_HSQC_1 _Saveframe_category NMR_applied_experiment _Experiment_name 1H15N_HSQC _Sample_label . save_ save_HNCA_2 _Saveframe_category NMR_applied_experiment _Experiment_name HNCA _Sample_label . save_ save_HN(CO)CA_3 _Saveframe_category NMR_applied_experiment _Experiment_name HN(CO)CA _Sample_label . save_ save_HNCACB_4 _Saveframe_category NMR_applied_experiment _Experiment_name HNCACB _Sample_label . save_ save_CBCA(CO)NH_5 _Saveframe_category NMR_applied_experiment _Experiment_name CBCA(CO)NH _Sample_label . save_ save_1H15N_NOESY_6 _Saveframe_category NMR_applied_experiment _Experiment_name 1H15N_NOESY _Sample_label . save_ ####################### # Sample conditions # ####################### save_conditions_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 6.0 0.05 pH temperature 293.0 0.1 K stop_ save_ save_conditions_2 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 4.0 0.05 pH temperature 293.0 0.1 K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_referencing _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 TSP H 1 'methyl protons' ppm 0.00 external indirect . . . 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_chem_shift_list_1 _Saveframe_category assigned_chemical_shifts _Details 'Chemical shift assignments for p53tet-R337H at pH 6.0' loop_ _Software_label $software_1 stop_ loop_ _Experiment_label 1H15N_HSQC HNCA HN(CO)CA HNCACB CBCA(CO)NH 1H15N_NOESY stop_ _Sample_conditions_label $conditions_1 _Chem_shift_reference_set_label $chemical_shift_referencing _Mol_system_component_name 'subunit A' _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 10 4 MET H H 8.313 . . 2 10 4 MET CA C 55.11147 . . 3 10 4 MET N N 123.176 . . 4 11 5 ASN H H 8.469 . . 5 11 5 ASN CA C 52.97075 . . 6 11 5 ASN N N 121.892 . . 7 12 6 THR H H 8.064 . . 8 12 6 THR CA C 61.20434 . . 9 12 6 THR N N 115.726 . . 10 13 7 SER H H 8.135 . . 11 13 7 SER CA C 57.95821 . . 12 13 7 SER N N 119.074 . . 13 14 8 SER H H 8.195 . . 14 14 8 SER CA C 57.85863 . . 15 14 8 SER N N 118.953 . . 16 15 9 SER H H 8.117 . . 17 15 9 SER CA C 56.04787 . . 18 15 9 SER N N 120.146 . . 19 16 10 PRO CA C 63.13255 . . 20 17 11 GLN H H 7.934 . . 21 17 11 GLN CA C 52.77706 . . 22 17 11 GLN N N 120.431 . . 23 18 12 PRO CA C 62.80736 . . 24 19 13 LYS H H 8.27 . . 25 19 13 LYS CA C 56.26735 . . 26 19 13 LYS N N 123.212 . . 27 20 14 LYS H H 8.181 . . 28 20 14 LYS CA C 56 . . 29 20 14 LYS N N 124.416 . . 30 21 15 LYS H H 8.281 . . 31 21 15 LYS CA C 53.94794 . . 32 21 15 LYS N N 126.174 . . 33 22 16 PRO CA C 62.80927 . . 34 23 17 LEU H H 8.22 . . 35 23 17 LEU CA C 54.79747 . . 36 23 17 LEU N N 123.325 . . 37 24 18 ASP H H 8.13 . . 38 24 18 ASP CA C 53.85928 . . 39 24 18 ASP N N 122.758 . . 40 25 19 GLY H H 8.086 . . 41 25 19 GLY CA C 44.61739 . . 42 25 19 GLY N N 110.413 . . 43 26 20 GLU H H 7.84 . . 44 26 20 GLU CA C 56.67536 . . 45 26 20 GLU N N 122.063 . . 46 27 21 TYR H H 7.911 . . 47 27 21 TYR CA C 57.03203 . . 48 27 21 TYR N N 121.631 . . 49 28 22 PHE H H 9.067 . . 50 28 22 PHE CA C 56.24717 . . 51 28 22 PHE N N 122.586 . . 52 29 23 THR H H 8.324 . . 53 29 23 THR CA C 61.1375 . . 54 29 23 THR N N 116.38 . . 55 30 24 LEU H H 8.812 . . 56 30 24 LEU CA C 53.01972 . . 57 30 24 LEU N N 128.06 . . 58 31 25 GLN H H 8.502 . . 59 31 25 GLN CA C 54.6095 . . 60 31 25 GLN N N 125.88 . . 61 32 26 ILE H H 9.29 . . 62 32 26 ILE CA C 59.0805 . . 63 32 26 ILE N N 127.644 . . 64 33 27 ARG H H 9.513 . . 65 33 27 ARG CA C 55.81449 . . 66 33 27 ARG N N 130.477 . . 67 34 28 GLY H H 8.842 . . 68 34 28 GLY CA C 44.61617 . . 69 34 28 GLY N N 118.23 . . 70 35 29 ARG H H 8.627 . . 71 35 29 ARG CA C 58.61677 . . 72 35 29 ARG N N 125.516 . . 73 36 30 GLU H H 8.702 . . 74 36 30 GLU CA C 60.10957 . . 75 36 30 GLU N N 120.007 . . 76 37 31 ARG H H 8.918 . . 77 37 31 ARG CA C 55.90561 . . 78 37 31 ARG N N 118.612 . . 79 38 32 PHE H H 8.058 . . 80 38 32 PHE CA C 61.6898 . . 81 38 32 PHE N N 122.598 . . 82 39 33 GLU H H 8.47 . . 83 39 33 GLU CA C 58.7117 . . 84 39 33 GLU N N 118.893 . . 85 40 34 MET H H 7.246 . . 86 40 34 MET CA C 58.66151 . . 87 40 34 MET N N 121.086 . . 88 41 35 PHE H H 7.822 . . 89 41 35 PHE CA C 60.47758 . . 90 41 35 PHE N N 118.118 . . 91 42 36 ARG H H 8.938 . . 92 42 36 ARG CA C 59.54486 . . 93 42 36 ARG N N 122.555 . . 94 43 37 GLU H H 7.438 . . 95 43 37 GLU CA C 59.17438 . . 96 43 37 GLU N N 121.298 . . 97 44 38 LEU H H 7.699 . . 98 44 38 LEU CA C 57.68349 . . 99 44 38 LEU N N 118.892 . . 100 45 39 ASN H H 8.78 . . 101 45 39 ASN CA C 56.933 . . 102 45 39 ASN N N 119.109 . . 103 46 40 GLU H H 8.259 . . 104 46 40 GLU CA C 58.99051 . . 105 46 40 GLU N N 119.582 . . 106 47 41 ALA H H 7.946 . . 107 47 41 ALA CA C 54.97206 . . 108 47 41 ALA N N 122.503 . . 109 48 42 LEU H H 8.192 . . 110 48 42 LEU CA C 57.63275 . . 111 48 42 LEU N N 120.827 . . 112 49 43 GLU H H 8.209 . . 113 49 43 GLU CA C 59.48402 . . 114 49 43 GLU N N 119.756 . . 115 50 44 LEU CA C 57.43578 . . 116 51 45 LYS H H 7.986 . . 117 51 45 LYS CA C 59.17493 . . 118 51 45 LYS N N 122.187 . . 119 52 46 ASP H H 8.309 . . 120 52 46 ASP CA C 56.46623 . . 121 52 46 ASP N N 121.246 . . 122 53 47 ALA H H 7.749 . . 123 53 47 ALA CA C 53.60693 . . 124 53 47 ALA N N 123.27 . . 125 54 48 GLN H H 7.725 . . 126 54 48 GLN CA C 56.23407 . . 127 54 48 GLN N N 118.02 . . 128 55 49 ALA H H 7.69 . . 129 55 49 ALA CA C 52.82521 . . 130 55 49 ALA N N 123.99 . . 131 56 50 GLY H H 8.061 . . 132 56 50 GLY CA C 45.08553 . . 133 56 50 GLY N N 108.675 . . 134 57 51 LYS H H 7.772 . . 135 57 51 LYS CA C 55.54168 . . 136 57 51 LYS N N 121.654 . . 137 58 52 GLU H H 8.325 . . 138 58 52 GLU CA C 54.04124 . . 139 58 52 GLU N N 125.135 . . 140 59 53 PRO CA C 62.90543 . . 141 60 54 GLY H H 8.025 . . 142 60 54 GLY CA C 46.0188 . . 143 60 54 GLY N N 118.225 . . stop_ save_ save_chem_shift_list_2 _Saveframe_category assigned_chemical_shifts _Details 'Chemical shift assignments for p53tet-R337H at pH 4.0' loop_ _Software_label $software_1 stop_ loop_ _Experiment_label 1H15N_HSQC HNCA HN(CO)CA HNCACB CBCA(CO)NH 1H15N_NOESY stop_ _Sample_conditions_label $conditions_2 _Chem_shift_reference_set_label $chemical_shift_referencing _Mol_system_component_name 'subunit A' _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 6 1 GLY CA C 43.32244 . . 2 7 2 SER H H 8.494 . . 3 7 2 SER CA C 58.2537 . . 4 7 2 SER N N 116.78 . . 5 8 3 HIS H H 8.56 . . 6 8 3 HIS CA C 55.34199 . . 7 8 3 HIS N N 121.816 . . 8 9 4 MET H H 8.305 . . 9 9 4 MET CA C 55.45112 . . 10 9 4 MET N N 123.232 . . 11 10 5 ASN H H 8.481 . . 12 10 5 ASN CA C 53.21523 . . 13 10 5 ASN N N 122.078 . . 14 12 6 THR H H 8.065 . . 15 12 6 THR CA C 61.70045 . . 16 12 6 THR N N 115.85 . . 17 13 7 SER H H 8.195 . . 18 13 7 SER CA C 58.44032 . . 19 13 7 SER N N 119.041 . . 20 14 8 SER H H 8.156 . . 21 14 8 SER CA C 58.24934 . . 22 14 8 SER N N 119.129 . . 23 15 9 SER H H 8.131 . . 24 15 9 SER CA C 56.57248 . . 25 15 9 SER N N 120.24 . . 26 16 10 PRO CA C 63.4758 . . 27 17 11 GLN H H 7.934 . . 28 17 11 GLN CA C 52.89492 . . 29 17 11 GLN N N 120.543 . . 30 18 12 PRO CA C 62.91949 . . 31 19 13 LYS H H 8.273 . . 32 19 13 LYS CA C 56.20251 . . 33 19 13 LYS N N 123.285 . . 34 20 14 LYS H H 8.169 . . 35 20 14 LYS CA C 56.01453 . . 36 20 14 LYS N N 124.404 . . 37 21 15 LYS H H 8.273 . . 38 21 15 LYS CA C 54.33304 . . 39 21 15 LYS N N 126.183 . . 40 22 16 PRO CA C 63.10583 . . 41 23 17 LEU H H 8.207 . . 42 23 17 LEU CA C 55.26614 . . 43 23 17 LEU N N 123.499 . . 44 24 18 ASP H H 8.176 . . 45 24 18 ASP CA C 54.14478 . . 46 24 18 ASP N N 122.243 . . 47 25 19 GLY H H 8.091 . . 48 25 19 GLY CA C 45.09724 . . 49 25 19 GLY N N 110.445 . . 50 26 20 GLU H H 7.791 . . 51 26 20 GLU CA C 55.82436 . . 52 26 20 GLU N N 121.368 . . 53 27 21 TYR H H 7.87 . . 54 27 21 TYR CA C 57.40764 . . 55 27 21 TYR N N 121.173 . . 56 28 22 PHE H H 8.997 . . 57 28 22 PHE CA C 56.57576 . . 58 28 22 PHE N N 122.563 . . 59 29 23 THR H H 8.329 . . 60 29 23 THR CA C 61.60469 . . 61 29 23 THR N N 116.528 . . 62 30 24 LEU H H 8.792 . . 63 30 24 LEU CA C 53.39939 . . 64 30 24 LEU N N 127.918 . . 65 31 25 GLN H H 8.482 . . 66 31 25 GLN CA C 55.07897 . . 67 31 25 GLN N N 126.063 . . 68 32 26 ILE H H 9.262 . . 69 32 26 ILE CA C 59.37342 . . 70 32 26 ILE N N 127.659 . . 71 33 27 ARG H H 9.192 . . 72 33 27 ARG CA C 56.0099 . . 73 33 27 ARG N N 130.085 . . 74 34 28 GLY H H 8.826 . . 75 34 28 GLY CA C 45.00147 . . 76 34 28 GLY N N 117.952 . . 77 35 29 ARG H H 8.632 . . 78 35 29 ARG CA C 59.36088 . . 79 35 29 ARG N N 126.461 . . 80 36 30 GLU H H 8.598 . . 81 36 30 GLU CA C 60.121 . . 82 36 30 GLU N N 120.186 . . 83 37 31 ARG H H 8.687 . . 84 37 31 ARG CA C 56.56675 . . 85 37 31 ARG N N 118.556 . . 86 38 32 PHE H H 8.092 . . 87 38 32 PHE CA C 61.79622 . . 88 38 32 PHE N N 122.301 . . 89 39 33 GLU H H 8.409 . . 90 39 33 GLU CA C 58.99855 . . 91 39 33 GLU N N 118.863 . . 92 40 34 MET H H 7.316 . . 93 40 34 MET CA C 58.99964 . . 94 40 34 MET N N 120.733 . . 95 41 35 PHE H H 7.885 . . 96 41 35 PHE CA C 61.05301 . . 97 41 35 PHE N N 118.263 . . 98 42 36 ARG H H 8.855 . . 99 42 36 ARG CA C 60.02578 . . 100 42 36 ARG N N 122.603 . . 101 43 37 GLU H H 7.497 . . 102 43 37 GLU CA C 59.36633 . . 103 43 37 GLU N N 120.826 . . 104 44 38 LEU H H 7.79 . . 105 44 38 LEU CA C 58.0649 . . 106 44 38 LEU N N 119.342 . . 107 45 39 ASN H H 8.765 . . 108 45 39 ASN CA C 57.31487 . . 109 45 39 ASN N N 119.31 . . 110 46 40 GLU H H 8.234 . . 111 46 40 GLU CA C 59.09022 . . 112 46 40 GLU N N 119.019 . . 113 47 41 ALA H H 7.882 . . 114 47 41 ALA CA C 55.35836 . . 115 47 41 ALA N N 122.631 . . 116 48 42 LEU H H 8.195 . . 117 48 42 LEU CA C 58.44169 . . 118 48 42 LEU N N 120.666 . . 119 49 43 GLU H H 8.156 . . 120 49 43 GLU CA C 59.55786 . . 121 49 43 GLU N N 119.402 . . 122 50 44 LEU H H 7.655 . . 123 50 44 LEU CA C 57.87473 . . 124 50 44 LEU N N 122.912 . . 125 51 45 LYS H H 7.959 . . 126 51 45 LYS CA C 59.3707 . . 127 51 45 LYS N N 122.036 . . 128 52 46 ASP H H 8.339 . . 129 52 46 ASP CA C 56.57412 . . 130 52 46 ASP N N 120.768 . . 131 53 47 ALA H H 7.723 . . 132 53 47 ALA CA C 53.95816 . . 133 53 47 ALA N N 123.535 . . 134 54 48 GLN H H 7.758 . . 135 54 48 GLN CA C 56.75992 . . 136 54 48 GLN N N 118.46 . . 137 55 49 ALA H H 7.737 . . 138 55 49 ALA CA C 53.21605 . . 139 55 49 ALA N N 123.947 . . 140 56 50 GLY H H 8.026 . . 141 56 50 GLY CA C 45.5627 . . 142 56 50 GLY N N 108.689 . . 143 57 51 LYS H H 7.804 . . 144 57 51 LYS CA C 55.82791 . . 145 57 51 LYS N N 121.477 . . 146 58 52 GLU H H 8.245 . . 147 58 52 GLU CA C 53.96034 . . 148 58 52 GLU N N 124.209 . . 149 59 53 PRO CA C 63.28536 . . 150 60 54 GLY H H 8.039 . . 151 60 54 GLY CA C 46.12011 . . 152 60 54 GLY N N 116.673 . . stop_ save_