data_15666 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Mutant Collision E7 protein IM7 with an extended helix III in M Urea ; _BMRB_accession_number 15666 _BMRB_flat_file_name bmr15666.str _Entry_type original _Submission_date 2008-02-20 _Accession_date 2008-02-20 _Entry_origination author _NMR_STAR_version 2.1.1 _Experimental_method NMR _Details . loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Figueiredo Angelo MMP . 2 Whittaker Sara B. . 3 Knowling Stuart . . 4 Radford Sheena E. . 5 Moore Geoffrey R. . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 88 "13C chemical shifts" 175 "15N chemical shifts" 88 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2009-11-10 original author . stop_ _Original_release_date 2009-11-10 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title 'Amino acid insertion reveals a necessary three-helical intermediate in the folding pathway of the colicin E7 immunity protein Im7.' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 19651139 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Knowling Stuart E. . 2 Figueiredo 'Angelo Miguel' . . 3 Whittaker 'Sara B-M' . . 4 Moore Geoffrey R. . 5 Radford Sheena E. . stop_ _Journal_abbreviation 'J. Mol. Biol.' _Journal_name_full 'Journal of molecular biology' _Journal_volume 392 _Journal_issue 4 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 1074 _Page_last 1086 _Year 2009 _Details . save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name 'Im7 mutant' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'Im7 mutant' $Im7_mutant stop_ _System_molecular_weight . _System_physical_state unfolded _System_oligomer_state ? _System_paramagnetic no _System_thiol_state . _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_Im7_mutant _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common Im7_mutant _Molecular_mass . _Mol_thiol_state 'not present' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 101 _Mol_residue_sequence ; MEHHHHHHELKNSISDYTEA EFVQLLKEIEKENVAATDDV LDVLLEHFVKITEHPDGTAL IYEAAARAAANPGGDGGGPE GIVKEIKEWRAANGKPGFKQ G ; loop_ _Residue_seq_code _Residue_label 1 MET 2 GLU 3 HIS 4 HIS 5 HIS 6 HIS 7 HIS 8 HIS 9 GLU 10 LEU 11 LYS 12 ASN 13 SER 14 ILE 15 SER 16 ASP 17 TYR 18 THR 19 GLU 20 ALA 21 GLU 22 PHE 23 VAL 24 GLN 25 LEU 26 LEU 27 LYS 28 GLU 29 ILE 30 GLU 31 LYS 32 GLU 33 ASN 34 VAL 35 ALA 36 ALA 37 THR 38 ASP 39 ASP 40 VAL 41 LEU 42 ASP 43 VAL 44 LEU 45 LEU 46 GLU 47 HIS 48 PHE 49 VAL 50 LYS 51 ILE 52 THR 53 GLU 54 HIS 55 PRO 56 ASP 57 GLY 58 THR 59 ALA 60 LEU 61 ILE 62 TYR 63 GLU 64 ALA 65 ALA 66 ALA 67 ARG 68 ALA 69 ALA 70 ALA 71 ASN 72 PRO 73 GLY 74 GLY 75 ASP 76 GLY 77 GLY 78 GLY 79 PRO 80 GLU 81 GLY 82 ILE 83 VAL 84 LYS 85 GLU 86 ILE 87 LYS 88 GLU 89 TRP 90 ARG 91 ALA 92 ALA 93 ASN 94 GLY 95 LYS 96 PRO 97 GLY 98 PHE 99 LYS 100 GLN 101 GLY stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-09-09 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 15645 Im7_mutant 100.00 101 100.00 100.00 1.69e-65 PDB 2K0D "Nmr Structure Of A Mutant Colicin E7 Immunity Protein Im7 With An Extended Helix Iii" 100.00 101 100.00 100.00 1.69e-65 GB EYB47026 "colicin immunity protein, partial [Escherichia coli]" 51.49 53 98.08 98.08 1.60e-25 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $Im7_mutant 'Escherichia coli' 562 Bacteria . Escherichia coli 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 $Im7_mutant 'recombinant technology' . Escherichia coli . JM109 stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Saveframe_category sample _Sample_type solution _Details 'Im7 mutant in 6 M UREA' loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $Im7_mutant 1 mM '[U-13C; U-15N]' H2O 95 % . D2O 5 % . 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_NMRView _Saveframe_category software _Name NMRView _Version 5.1.1 loop_ _Vendor _Address _Electronic_address 'Johnson, One Moon Scientific' . . stop_ loop_ _Task 'chemical shift assignment' 'peak picking' stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model Avance _Field_strength 800 _Details . save_ save_spectrometer_2 _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model INOVA _Field_strength 500 _Details . save_ ############################# # NMR applied experiments # ############################# save_3D_CBCANH_1 _Saveframe_category NMR_applied_experiment _Experiment_name '3D CBCANH' _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_HNN_3 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNN' _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' 50 . mM pH* 7 . pH pressure 1 . atm temperature 298 . K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference_1 _Saveframe_category chemical_shift_reference _Details . loop_ _Mol_common_name _Atom_type _Atom_isotope_number _Atom_group _Chem_shift_units _Chem_shift_value _Reference_method _Reference_type _External_reference_sample_geometry _External_reference_location _External_reference_axis _Indirect_shift_ratio DSS C 13 'methyl protons' ppm 0.00 . indirect . . . 0.251449530 DSS H 1 'methyl protons' ppm 0.00 internal direct . . . 1.000000000 DSS N 15 'methyl protons' ppm 0.00 . 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 $NMRView stop_ loop_ _Experiment_label '3D CBCANH' '3D CBCA(CO)NH' '3D HNN' 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 'Im7 mutant' _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 2 9 GLU H H 8.547 0.002 1 2 2 9 GLU CA C 56.489 0.002 1 3 2 9 GLU CB C 30.633 0.002 1 4 2 9 GLU N N 121.671 0.002 1 5 3 10 LEU H H 8.447 0.002 1 6 3 10 LEU CA C 55.226 0.002 1 7 3 10 LEU CB C 42.312 0.002 1 8 3 10 LEU N N 124.123 0.002 1 9 4 11 LYS H H 8.506 0.002 1 10 4 11 LYS CA C 56.400 0.002 1 11 4 11 LYS CB C 33.217 0.002 1 12 4 11 LYS N N 122.749 0.002 1 13 5 12 ASN H H 8.601 0.002 1 14 5 12 ASN CA C 53.340 0.002 1 15 5 12 ASN CB C 39.145 0.002 1 16 5 12 ASN N N 120.321 0.002 1 17 6 13 SER H H 8.424 0.002 1 18 6 13 SER CA C 58.362 0.002 1 19 6 13 SER CB C 64.191 0.002 1 20 6 13 SER N N 116.523 0.002 1 21 7 14 ILE H H 8.310 0.002 1 22 7 14 ILE CA C 61.491 0.002 1 23 7 14 ILE CB C 38.868 0.002 1 24 7 14 ILE N N 122.421 0.002 1 25 8 15 SER H H 8.385 0.002 1 26 8 15 SER CA C 58.364 0.002 1 27 8 15 SER CB C 64.224 0.002 1 28 8 15 SER N N 119.295 0.002 1 29 9 16 ASP H H 8.359 0.002 1 30 9 16 ASP CA C 54.507 0.002 1 31 9 16 ASP CB C 41.422 0.002 1 32 9 16 ASP N N 122.637 0.002 1 33 10 17 TYR H H 8.203 0.002 1 34 10 17 TYR CA C 58.128 0.002 1 35 10 17 TYR CB C 38.853 0.002 1 36 10 17 TYR N N 120.699 0.002 1 37 11 18 THR H H 8.200 0.002 1 38 11 18 THR CA C 61.966 0.002 1 39 11 18 THR CB C 70.279 0.002 1 40 11 18 THR N N 116.796 0.002 1 41 12 19 GLU H H 8.455 0.002 1 42 12 19 GLU CA C 56.896 0.002 1 43 12 19 GLU CB C 30.328 0.002 1 44 12 19 GLU N N 123.580 0.002 1 45 13 20 ALA H H 8.328 0.002 1 46 13 20 ALA CA C 52.935 0.002 1 47 13 20 ALA CB C 19.296 0.002 1 48 13 20 ALA N N 124.705 0.002 1 49 14 21 GLU H H 8.367 0.002 1 50 14 21 GLU CA C 57.028 0.002 1 51 14 21 GLU CB C 30.535 0.002 1 52 14 21 GLU N N 119.973 0.002 1 53 15 22 PHE H H 8.319 0.002 1 54 15 22 PHE CA C 57.959 0.002 1 55 15 22 PHE CB C 39.588 0.002 1 56 15 22 PHE N N 121.436 0.002 1 57 16 23 VAL H H 8.094 0.002 1 58 16 23 VAL CA C 62.621 0.002 1 59 16 23 VAL CB C 32.913 0.002 1 60 16 23 VAL N N 122.807 0.002 1 61 17 24 GLN H H 8.394 0.002 1 62 17 24 GLN CA C 56.016 0.002 1 63 17 24 GLN CB C 29.516 0.002 1 64 17 24 GLN N N 124.277 0.002 1 65 18 25 LEU H H 8.373 0.002 1 66 18 25 LEU CA C 55.326 0.002 1 67 18 25 LEU CB C 42.455 0.002 1 68 18 25 LEU N N 124.658 0.002 1 69 19 26 LEU H H 8.389 0.002 1 70 19 26 LEU CA C 55.278 0.002 1 71 19 26 LEU CB C 42.372 0.002 1 72 19 26 LEU N N 123.655 0.002 1 73 20 27 LYS H H 8.426 0.002 1 74 20 27 LYS CA C 56.668 0.002 1 75 20 27 LYS CB C 33.323 0.002 1 76 20 27 LYS N N 122.788 0.002 1 77 21 28 GLU H H 8.553 0.002 1 78 21 28 GLU CA C 56.783 0.002 1 79 21 28 GLU CB C 30.352 0.002 1 80 21 28 GLU N N 122.813 0.002 1 81 22 29 ILE H H 8.284 0.002 1 82 22 29 ILE CA C 61.497 0.002 1 83 22 29 ILE CB C 38.837 0.002 1 84 22 29 ILE N N 121.997 0.002 1 85 23 30 GLU H H 8.567 0.002 1 86 23 30 GLU CA C 56.831 0.002 1 87 23 30 GLU CB C 30.332 0.002 1 88 23 30 GLU N N 125.286 0.002 1 89 24 31 LYS H H 8.407 0.002 1 90 24 31 LYS CA C 56.709 0.002 1 91 24 31 LYS CB C 33.322 0.002 1 92 24 31 LYS N N 122.815 0.002 1 93 25 32 GLU H H 8.576 0.002 1 94 25 32 GLU CA C 56.744 0.002 1 95 25 32 GLU CB C 30.533 0.002 1 96 25 32 GLU N N 122.081 0.002 1 97 26 33 ASN H H 8.646 0.002 1 98 26 33 ASN CA C 53.271 0.002 1 99 26 33 ASN CB C 38.993 0.002 1 100 26 33 ASN N N 120.751 0.002 1 101 27 34 VAL H H 8.175 0.002 1 102 27 34 VAL CA C 62.209 0.002 1 103 27 34 VAL CB C 32.884 0.002 1 104 27 34 VAL N N 120.898 0.002 1 105 28 35 ALA H H 8.441 0.002 1 106 28 35 ALA CA C 52.375 0.002 1 107 28 35 ALA CB C 19.369 0.002 1 108 28 35 ALA N N 127.907 0.002 1 109 29 36 ALA H H 8.386 0.002 1 110 29 36 ALA CA C 52.522 0.002 1 111 29 36 ALA CB C 19.346 0.002 1 112 29 36 ALA N N 124.154 0.002 1 113 30 37 THR H H 8.169 0.002 1 114 30 37 THR CA C 61.583 0.002 1 115 30 37 THR CB C 70.126 0.002 1 116 30 37 THR N N 112.661 0.002 1 117 31 38 ASP H H 8.420 0.002 1 118 31 38 ASP CA C 54.526 0.002 1 119 31 38 ASP CB C 41.371 0.002 1 120 31 38 ASP N N 122.161 0.002 1 121 32 39 ASP H H 8.376 0.002 1 122 32 39 ASP CA C 54.570 0.002 1 123 32 39 ASP CB C 41.412 0.002 1 124 32 39 ASP N N 120.921 0.002 1 125 33 40 VAL H H 8.138 0.002 1 126 33 40 VAL CA C 62.540 0.002 1 127 33 40 VAL CB C 32.622 0.002 1 128 33 40 VAL N N 120.301 0.002 1 129 34 41 LEU H H 8.357 0.002 1 130 34 41 LEU CA C 55.251 0.002 1 131 34 41 LEU CB C 42.602 0.002 1 132 34 41 LEU N N 125.651 0.002 1 133 35 42 ASP H H 8.419 0.002 1 134 35 42 ASP CA C 54.537 0.002 1 135 35 42 ASP CB C 41.330 0.002 1 136 35 42 ASP N N 121.788 0.002 1 137 36 43 VAL H H 8.055 0.002 1 138 36 43 VAL CA C 62.524 0.002 1 139 36 43 VAL CB C 32.775 0.002 1 140 36 43 VAL N N 120.025 0.002 1 141 37 44 LEU H H 8.361 0.002 1 142 37 44 LEU CA C 55.234 0.002 1 143 37 44 LEU CB C 42.164 0.002 1 144 37 44 LEU N N 125.410 0.002 1 145 38 45 LEU H H 8.258 0.002 1 146 38 45 LEU CA C 55.219 0.002 1 147 38 45 LEU CB C 42.451 0.002 1 148 38 45 LEU N N 123.601 0.002 1 149 39 46 GLU H H 8.423 0.002 1 150 39 46 GLU CA C 56.833 0.002 1 151 39 46 GLU CB C 30.545 0.002 1 152 39 46 GLU N N 121.502 0.002 1 153 40 47 HIS H H 8.358 0.002 1 154 40 47 HIS CA C 56.181 0.002 1 155 40 47 HIS CB C 30.800 0.002 1 156 40 47 HIS N N 120.225 0.002 1 157 41 48 PHE H H 8.216 0.002 1 158 41 48 PHE CA C 57.640 0.002 1 159 41 48 PHE CB C 39.778 0.002 1 160 41 48 PHE N N 121.846 0.002 1 161 42 49 VAL H H 8.204 0.002 1 162 42 49 VAL CA C 62.248 0.002 1 163 42 49 VAL CB C 33.014 0.002 1 164 42 49 VAL N N 123.100 0.002 1 165 43 50 LYS H H 8.451 0.002 1 166 43 50 LYS CA C 56.246 0.002 1 167 43 50 LYS CB C 33.265 0.002 1 168 43 50 LYS N N 126.375 0.002 1 169 44 51 ILE H H 8.492 0.002 1 170 44 51 ILE CA C 61.169 0.002 1 171 44 51 ILE CB C 38.801 0.002 1 172 44 51 ILE N N 124.301 0.002 1 173 45 52 THR H H 8.371 0.002 1 174 45 52 THR CA C 61.852 0.002 1 175 45 52 THR CB C 69.982 0.002 1 176 45 52 THR N N 119.032 0.002 1 177 46 53 GLU H H 8.462 0.002 1 178 46 53 GLU CA C 56.533 0.002 1 179 46 53 GLU CB C 30.753 0.002 1 180 46 53 GLU N N 123.820 0.002 1 181 47 54 HIS H H 8.576 0.002 1 182 47 54 HIS CA C 56.550 0.002 1 183 47 54 HIS CB C 30.553 0.002 1 184 47 54 HIS N N 122.574 0.002 1 185 48 55 PRO CA C 63.878 0.002 1 186 48 55 PRO CB C 32.130 0.002 1 187 49 56 ASP H H 8.922 0.002 1 188 49 56 ASP CA C 54.524 0.002 1 189 49 56 ASP CB C 41.392 0.002 1 190 49 56 ASP N N 120.756 0.002 1 191 50 57 GLY H H 8.448 0.002 1 192 50 57 GLY CA C 45.763 0.002 1 193 50 57 GLY N N 109.501 0.002 1 194 51 58 THR H H 8.194 0.002 1 195 51 58 THR CA C 62.418 0.002 1 196 51 58 THR CB C 70.085 0.002 1 197 51 58 THR N N 113.900 0.002 1 198 52 59 ALA H H 8.343 0.002 1 199 52 59 ALA CA C 52.648 0.002 1 200 52 59 ALA CB C 19.289 0.002 1 201 52 59 ALA N N 126.339 0.002 1 202 53 60 LEU H H 8.219 0.002 1 203 53 60 LEU CA C 55.300 0.002 1 204 53 60 LEU CB C 42.333 0.002 1 205 53 60 LEU N N 121.998 0.002 1 206 54 61 ILE H H 8.158 0.002 1 207 54 61 ILE CA C 61.129 0.002 1 208 54 61 ILE CB C 38.816 0.002 1 209 54 61 ILE N N 121.859 0.002 1 210 55 62 TYR H H 8.359 0.002 1 211 55 62 TYR CA C 57.899 0.002 1 212 55 62 TYR CB C 38.853 0.002 1 213 55 62 TYR N N 124.818 0.002 1 214 56 63 GLU H H 8.424 0.002 1 215 56 63 GLU CA C 56.516 0.002 1 216 56 63 GLU CB C 30.666 0.002 1 217 56 63 GLU N N 123.649 0.002 1 218 57 64 ALA H H 8.331 0.002 1 219 57 64 ALA CA C 52.870 0.002 1 220 57 64 ALA CB C 19.108 0.002 1 221 57 64 ALA N N 125.553 0.002 1 222 58 65 ALA H H 8.290 0.002 1 223 58 65 ALA CA C 52.655 0.002 1 224 58 65 ALA CB C 19.129 0.002 1 225 58 65 ALA N N 123.001 0.002 1 226 59 66 ALA H H 8.251 0.002 1 227 59 66 ALA CA C 52.699 0.002 1 228 59 66 ALA CB C 19.097 0.002 1 229 59 66 ALA N N 123.260 0.002 1 230 60 67 ARG H H 8.308 0.002 1 231 60 67 ARG CA C 56.254 0.002 1 232 60 67 ARG CB C 31.020 0.002 1 233 60 67 ARG N N 120.512 0.002 1 234 61 68 ALA H H 8.364 0.002 1 235 61 68 ALA CA C 52.532 0.002 1 236 61 68 ALA CB C 19.269 0.002 1 237 61 68 ALA N N 125.465 0.002 1 238 62 69 ALA H H 8.306 0.002 1 239 62 69 ALA CA C 52.427 0.002 1 240 62 69 ALA CB C 19.310 0.002 1 241 62 69 ALA N N 123.546 0.002 1 242 63 70 ALA H H 8.288 0.002 1 243 63 70 ALA CA C 52.473 0.002 1 244 63 70 ALA CB C 19.298 0.002 1 245 63 70 ALA N N 123.183 0.002 1 246 64 71 ASN H H 8.517 0.002 1 247 64 71 ASN CA C 51.413 0.002 1 248 64 71 ASN CB C 38.944 0.002 1 249 64 71 ASN N N 118.773 0.002 1 250 65 72 PRO CA C 63.940 0.002 1 251 65 72 PRO CB C 32.102 0.002 1 252 66 73 GLY H H 8.521 0.002 1 253 66 73 GLY CA C 45.354 0.002 1 254 66 73 GLY N N 108.891 0.002 1 255 67 74 GLY H H 8.250 0.002 1 256 67 74 GLY CA C 45.424 0.002 1 257 67 74 GLY N N 108.793 0.002 1 258 68 75 ASP H H 8.446 0.002 1 259 68 75 ASP CA C 54.437 0.002 1 260 68 75 ASP CB C 41.585 0.002 1 261 68 75 ASP N N 120.469 0.002 1 262 69 76 GLY H H 8.531 0.002 1 263 69 76 GLY CA C 45.650 0.002 1 264 69 76 GLY N N 109.595 0.002 1 265 70 77 GLY H H 8.427 0.002 1 266 70 77 GLY CA C 45.330 0.002 1 267 70 77 GLY N N 108.876 0.002 1 268 71 78 GLY H H 8.278 0.002 1 269 71 78 GLY CA C 44.708 0.002 1 270 71 78 GLY N N 108.975 0.002 1 271 72 79 PRO CA C 63.613 0.002 1 272 72 79 PRO CB C 32.169 0.002 1 273 73 80 GLU H H 8.739 0.002 1 274 73 80 GLU CA C 57.028 0.002 1 275 73 80 GLU CB C 30.286 0.002 1 276 73 80 GLU N N 120.865 0.002 1 277 74 81 GLY H H 8.372 0.002 1 278 74 81 GLY CA C 45.459 0.002 1 279 74 81 GLY N N 109.622 0.002 1 280 75 82 ILE H H 8.009 0.002 1 281 75 82 ILE CA C 61.182 0.002 1 282 75 82 ILE CB C 38.859 0.002 1 283 75 82 ILE N N 120.287 0.002 1 284 76 83 VAL H H 8.361 0.002 1 285 76 83 VAL CA C 62.480 0.002 1 286 76 83 VAL CB C 32.643 0.002 1 287 76 83 VAL N N 125.510 0.002 1 288 77 84 LYS H H 8.528 0.002 1 289 77 84 LYS CA C 56.318 0.002 1 290 77 84 LYS CB C 33.317 0.002 1 291 77 84 LYS N N 126.498 0.002 1 292 78 85 GLU H H 8.520 0.002 1 293 78 85 GLU CA C 56.455 0.002 1 294 78 85 GLU CB C 30.663 0.002 1 295 78 85 GLU N N 122.993 0.002 1 296 79 86 ILE H H 8.433 0.002 1 297 79 86 ILE CA C 61.121 0.002 1 298 79 86 ILE CB C 38.620 0.002 1 299 79 86 ILE N N 123.771 0.002 1 300 80 87 LYS H H 8.540 0.002 1 301 80 87 LYS CB C 33.202 0.002 1 302 80 87 LYS N N 126.461 0.002 1 303 81 88 GLU H H 8.507 0.002 1 304 81 88 GLU CA C 56.485 0.002 1 305 81 88 GLU CB C 30.578 0.002 1 306 81 88 GLU N N 122.619 0.002 1 307 82 89 TRP H H 8.441 0.002 1 308 82 89 TRP CA C 57.702 0.002 1 309 82 89 TRP CB C 29.765 0.002 1 310 82 89 TRP N N 123.927 0.002 1 311 83 90 ARG H H 8.140 0.002 1 312 83 90 ARG CA C 55.735 0.002 1 313 83 90 ARG CB C 31.423 0.002 1 314 83 90 ARG N N 123.977 0.002 1 315 84 91 ALA H H 8.205 0.002 1 316 84 91 ALA CA C 52.456 0.002 1 317 84 91 ALA CB C 19.220 0.002 1 318 84 91 ALA N N 125.451 0.002 1 319 85 92 ALA CA C 52.735 0.002 1 320 85 92 ALA CB C 19.108 0.002 1 321 86 93 ASN H H 8.376 0.002 1 322 86 93 ASN CA C 53.282 0.002 1 323 86 93 ASN CB C 39.031 0.002 1 324 86 93 ASN N N 117.613 0.002 1 325 87 94 GLY H H 8.331 0.002 1 326 87 94 GLY CA C 45.301 0.002 1 327 87 94 GLY N N 109.017 0.002 1 328 88 95 LYS H H 8.232 0.002 1 329 88 95 LYS CA C 54.388 0.002 1 330 88 95 LYS CB C 32.680 0.002 1 331 88 95 LYS N N 121.973 0.002 1 332 89 96 PRO CA C 63.489 0.002 1 333 89 96 PRO CB C 32.165 0.002 1 334 90 97 GLY H H 8.514 0.002 1 335 90 97 GLY CA C 45.199 0.002 1 336 90 97 GLY N N 109.266 0.002 1 337 91 98 PHE H H 8.169 0.002 1 338 91 98 PHE CA C 57.752 0.002 1 339 91 98 PHE CB C 39.923 0.002 1 340 91 98 PHE N N 120.443 0.002 1 341 92 99 LYS H H 8.419 0.002 1 342 92 99 LYS CA C 56.336 0.002 1 343 92 99 LYS CB C 33.365 0.002 1 344 92 99 LYS N N 124.422 0.002 1 345 93 100 GLN H H 8.506 0.002 1 346 93 100 GLN CA C 56.007 0.002 1 347 93 100 GLN CB C 29.959 0.002 1 348 93 100 GLN N N 123.235 0.002 1 349 94 101 GLY H H 8.188 0.002 1 350 94 101 GLY CA C 46.415 0.002 1 351 94 101 GLY N N 117.327 0.002 1 stop_ save_