data_7318 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Backbone 1HN, 15N, and 13C Chemical Shift Assignments for wt Im7* (* denotes his-tag) and its variants, Im7*L53AI54A and Im7*YY ; _BMRB_accession_number 7318 _BMRB_flat_file_name bmr7318.str _Entry_type original _Submission_date 2006-10-17 _Accession_date 2006-10-17 _Entry_origination author _NMR_STAR_version 2.1.1 _Experimental_method NMR _Details 'The variants of wt Im7* (L53AI54A and YY) show biochemical and biophysical properties resembling the kinetic protein folding intermediate of wt Im7*. These variants have therefore been studied by NMR to obtain structural and dynamic information of the protein folding intermediate. This entry consists of backbone 1HN, 15N and 13C chemical shifts of the three proteins.' loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Whittaker Sara B.-M. . 2 Spence Graham R. . 3 Grossmann Guenter J. . 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" 101 "13C chemical shifts" 202 "15N chemical shifts" 68 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2007-05-04 original author . stop_ _Original_release_date 2007-05-04 save_ ############################# # Citation for this entry # ############################# save_citation_1 _Saveframe_category entry_citation _Citation_full . _Citation_title ; NMR analysis of the conformational properties of the trapped on-pathway folding intermediate of the bacterial immunity protein Im7. ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 17188712 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Whittaker Sara B.-M. . 2 Spence Graham R. . 3 Grossmann Guenter J. . 4 Radford Sheena E. . 5 Moore Geoffrey R. . stop_ _Journal_abbreviation 'J. Mol. Biol.' _Journal_volume 366 _Journal_issue 3 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 1001 _Page_last 1015 _Year 2007 _Details . loop_ _Keyword Im7 intermediate NMR 'partially folded' 'Protein folding' SAXS stop_ save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name Monomer _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label Monomer $YY_variant_of_Im7* stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state protein _System_paramagnetic no _System_thiol_state 'not present' loop_ _Biological_function 'Inhibitor protein of the endonuclease Colicin E7.' stop_ _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_YY_variant_of_Im7* _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common YY _Molecular_mass . _Mol_thiol_state 'not present' loop_ _Biological_function 'Trapped protein folding intermediate of Im7*' stop_ _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 94 _Mol_residue_sequence ; MEHHHHHHELKNSISDYTEA EFVQLLKEIEKENVAATDDV LDVLLEHFVKITEHPDGGGG GYYPSDNRDDSPEGIVKEIK EWRAANGKPGFKQG ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 -8 MET 2 -7 GLU 3 -6 HIS 4 -5 HIS 5 -4 HIS 6 -3 HIS 7 -2 HIS 8 -1 HIS 9 2 GLU 10 3 LEU 11 4 LYS 12 5 ASN 13 6 SER 14 7 ILE 15 8 SER 16 9 ASP 17 10 TYR 18 11 THR 19 12 GLU 20 13 ALA 21 14 GLU 22 15 PHE 23 16 VAL 24 17 GLN 25 18 LEU 26 19 LEU 27 20 LYS 28 21 GLU 29 22 ILE 30 23 GLU 31 24 LYS 32 25 GLU 33 26 ASN 34 27 VAL 35 28 ALA 36 29 ALA 37 30 THR 38 31 ASP 39 32 ASP 40 33 VAL 41 34 LEU 42 35 ASP 43 36 VAL 44 37 LEU 45 38 LEU 46 39 GLU 47 40 HIS 48 41 PHE 49 42 VAL 50 43 LYS 51 44 ILE 52 45 THR 53 46 GLU 54 47 HIS 55 48 PRO 56 49 ASP 57 50 GLY 58 51 GLY 59 52 GLY 60 53 GLY 61 54 GLY 62 55 TYR 63 56 TYR 64 57 PRO 65 58 SER 66 59 ASP 67 60 ASN 68 61 ARG 69 62 ASP 70 63 ASP 71 64 SER 72 65 PRO 73 66 GLU 74 67 GLY 75 68 ILE 76 69 VAL 77 70 LYS 78 71 GLU 79 72 ILE 80 73 LYS 81 74 GLU 82 75 TRP 83 76 ARG 84 77 ALA 85 78 ALA 86 79 ASN 87 80 GLY 88 81 LYS 89 82 PRO 90 83 GLY 91 84 PHE 92 85 LYS 93 86 GLN 94 87 GLY stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2014-10-18 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 GB EYB47026 "colicin immunity protein, partial [Escherichia coli]" 52.13 53 100.00 100.00 2.60e-24 REF WP_032277812 "colicin transporter, partial [Escherichia coli]" 52.13 53 100.00 100.00 2.60e-24 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $YY_variant_of_Im7* '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 $YY_variant_of_Im7* 'recombinant technology' 'E. coli' Escherichia coli . . stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Saveframe_category sample _Sample_type solution _Details 'doubly-labelled (13C/15N) Im7*YY sample for backbone resonance assignments.' loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $YY_variant_of_Im7* 1 mM '[U-13C; U-15N]' 'potassium phosphate buffer' 50 mM . 'sodium sulphate' 400 mM . H2O 90 % . D2O 10 % . stop_ save_ save_sample_2 _Saveframe_category sample _Sample_type solution _Details 'singly-labelled (15N) Im7* sample for relaxation data measurement and 15N-edited NOESY experiment.' loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $YY_variant_of_Im7* 1 mM '[U-99% 15N]' 'potassium phosphate buffer' 50 mM . 'sodium sulphate' 400 mM . H2O 90 % . D2O 10 % . stop_ save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model Inova _Field_strength 500 _Details . save_ save_spectrometer_2 _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model Inova _Field_strength 600 _Details . save_ save_spectrometer_3 _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model Inova _Field_strength 750 _Details . save_ ############################# # NMR applied experiments # ############################# save_1H15N_HSQC_1 _Saveframe_category NMR_applied_experiment _Experiment_name '1H15N HSQC' _Sample_label . save_ save_HNCO_2 _Saveframe_category NMR_applied_experiment _Experiment_name HNCO _Sample_label $Samples_1_and_3_and_5 save_ save_HNCA_3 _Saveframe_category NMR_applied_experiment _Experiment_name HNCA _Sample_label $Samples_3_and_5 save_ save_HNCOCA_4 _Saveframe_category NMR_applied_experiment _Experiment_name HNCOCA _Sample_label $Samples_3_and_5_again save_ save_CBCACONH_5 _Saveframe_category NMR_applied_experiment _Experiment_name CBCACONH _Sample_label $Samples_3_and_5_again2 save_ save_HNCACB_6 _Saveframe_category NMR_applied_experiment _Experiment_name HNCACB _Sample_label $sample_1 save_ save_1H-1H-15N_NOESY-HSQC_7 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-1H-15N NOESY-HSQC' _Sample_label . save_ ####################### # Sample conditions # ####################### save_conditions_1 _Saveframe_category sample_conditions _Details 'Used for all NMR experiments.' loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 7 0.2 pH temperature 298 0.1 K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_referencing _Saveframe_category chemical_shift_reference _Details '1H chemical shifts referenced directly against external DSS; 15N and 13C referenced indirectly to DSS using absolute frequency ratios at 298K.' 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 _Indirect_shift_ratio_citation_label _Correction_value_citation_label DSS C 13 'methyl protons' ppm 0.0 . indirect . . . 0.251449530 $citation_1 $citation_1 DSS H 1 'methyl protons' ppm 0.0 internal direct . . . 1.000000000 $citation_1 $citation_1 DSS N 15 'methyl protons' ppm 0.0 . indirect . . . 0.101329118 $citation_1 $citation_1 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_Im7*_YY_chemical_shifts _Saveframe_category assigned_chemical_shifts _Details 'Backbone HN, N and C chemical shifts.' loop_ _Software_label $NMRView stop_ loop_ _Experiment_label 1H15N_HSQC HNCO HNCA HNCOCA CBCACONH 1H-1H-15N_NOESY-HSQC stop_ loop_ _Sample_label $sample_1 $sample_2 $Samples_1_and_3_and_5 $Samples_3_and_5 $Samples_3_and_5_again $Samples_3_and_5_again2 stop_ _Sample_conditions_label $conditions_1 _Chem_shift_reference_set_label $chemical_shift_referencing _Mol_system_component_name Monomer _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 HA H 4.270 0.01 1 2 2 9 GLU C C 176.183 0.2 1 3 2 9 GLU CA C 56.241 0.2 1 4 2 9 GLU CB C 30.114 0.2 1 5 3 10 LEU H H 8.337 0.01 1 6 3 10 LEU C C 177.530 0.2 1 7 3 10 LEU CA C 54.770 0.2 1 8 3 10 LEU CB C 42.523 0.2 1 9 3 10 LEU N N 124.169 0.1 1 10 4 11 LYS H H 8.035 0.01 1 11 4 11 LYS C C 175.878 0.2 1 12 4 11 LYS CA C 56.060 0.2 1 13 4 11 LYS CB C 32.950 0.2 1 14 4 11 LYS N N 121.541 0.1 1 15 5 12 ASN H H 8.460 0.01 1 16 5 12 ASN C C 175.221 0.2 1 17 5 12 ASN CA C 55.630 0.2 1 18 5 12 ASN CB C 39.633 0.2 1 19 5 12 ASN N N 116.900 0.1 1 20 6 13 SER H H 8.231 0.01 1 21 6 13 SER CA C 56.330 0.2 1 22 6 13 SER N N 112.083 0.1 1 23 8 15 SER HA H 4.460 0.01 1 24 8 15 SER C C 174.118 0.2 1 25 8 15 SER CA C 59.738 0.2 1 26 8 15 SER CB C 63.102 0.2 1 27 9 16 ASP H H 7.797 0.01 1 28 9 16 ASP C C 175.793 0.2 1 29 9 16 ASP CA C 55.020 0.2 1 30 9 16 ASP CB C 42.480 0.2 1 31 9 16 ASP N N 118.483 0.1 1 32 10 17 TYR H H 8.139 0.01 1 33 10 17 TYR C C 177.422 0.2 1 34 10 17 TYR CA C 57.639 0.2 1 35 10 17 TYR N N 120.072 0.1 1 36 11 18 THR H H 8.795 0.01 1 37 11 18 THR HA H 4.690 0.01 1 38 11 18 THR C C 175.662 0.2 1 39 11 18 THR CA C 60.632 0.2 1 40 11 18 THR CB C 70.552 0.2 1 41 11 18 THR N N 112.243 0.1 1 42 12 19 GLU H H 9.096 0.01 1 43 12 19 GLU C C 178.022 0.2 1 44 12 19 GLU CA C 60.380 0.2 1 45 12 19 GLU CB C 29.539 0.2 1 46 12 19 GLU N N 122.887 0.1 1 47 13 20 ALA H H 8.333 0.01 1 48 13 20 ALA C C 181.484 0.2 1 49 13 20 ALA CA C 54.867 0.2 1 50 13 20 ALA CB C 18.478 0.2 1 51 13 20 ALA N N 118.635 0.1 1 52 14 21 GLU H H 7.985 0.01 1 53 14 21 GLU HA H 4.010 0.01 1 54 14 21 GLU C C 179.436 0.2 1 55 14 21 GLU CA C 58.525 0.2 1 56 14 21 GLU CB C 31.125 0.2 1 57 14 21 GLU N N 118.844 0.1 1 58 15 22 PHE H H 8.526 0.01 1 59 15 22 PHE C C 176.998 0.2 1 60 15 22 PHE CA C 61.937 0.2 1 61 15 22 PHE CB C 40.088 0.2 1 62 15 22 PHE N N 123.545 0.1 1 63 16 23 VAL H H 8.484 0.01 1 64 16 23 VAL HA H 3.330 0.01 1 65 16 23 VAL C C 177.598 0.2 1 66 16 23 VAL CA C 67.199 0.2 1 67 16 23 VAL CB C 31.705 0.2 1 68 16 23 VAL N N 118.289 0.1 1 69 17 24 GLN H H 7.581 0.01 1 70 17 24 GLN HA H 3.890 0.01 1 71 17 24 GLN C C 177.865 0.2 1 72 17 24 GLN CA C 58.808 0.2 1 73 17 24 GLN CB C 28.029 0.2 1 74 17 24 GLN N N 117.691 0.1 1 75 18 25 LEU H H 7.683 0.01 1 76 18 25 LEU HA H 4.010 0.01 1 77 18 25 LEU C C 178.392 0.2 1 78 18 25 LEU CA C 58.073 0.2 1 79 18 25 LEU CB C 41.246 0.2 1 80 18 25 LEU N N 121.467 0.1 1 81 19 26 LEU H H 7.795 0.01 1 82 19 26 LEU C C 179.780 0.2 1 83 19 26 LEU CA C 57.761 0.2 1 84 19 26 LEU CB C 40.983 0.2 1 85 19 26 LEU N N 117.491 0.1 1 86 20 27 LYS H H 8.176 0.01 1 87 20 27 LYS HA H 4.180 0.01 1 88 20 27 LYS C C 179.497 0.2 1 89 20 27 LYS CA C 59.583 0.2 1 90 20 27 LYS CB C 32.453 0.2 1 91 20 27 LYS N N 118.914 0.1 1 92 21 28 GLU H H 8.127 0.01 1 93 21 28 GLU HA H 4.070 0.01 1 94 21 28 GLU C C 179.270 0.2 1 95 21 28 GLU CA C 58.976 0.2 1 96 21 28 GLU CB C 29.483 0.2 1 97 21 28 GLU N N 120.495 0.1 1 98 22 29 ILE H H 8.102 0.01 1 99 22 29 ILE C C 178.330 0.2 1 100 22 29 ILE CA C 64.144 0.2 1 101 22 29 ILE CB C 37.738 0.2 1 102 22 29 ILE N N 119.664 0.1 1 103 23 30 GLU H H 7.978 0.01 1 104 23 30 GLU HA H 4.040 0.01 1 105 23 30 GLU C C 178.179 0.2 1 106 23 30 GLU CA C 58.827 0.2 1 107 23 30 GLU CB C 29.789 0.2 1 108 23 30 GLU N N 120.490 0.1 1 109 24 31 LYS H H 7.677 0.01 1 110 24 31 LYS HA H 4.130 0.01 1 111 24 31 LYS C C 177.878 0.2 1 112 24 31 LYS CA C 57.887 0.2 1 113 24 31 LYS CB C 32.854 0.2 1 114 24 31 LYS N N 118.128 0.1 1 115 25 32 GLU H H 7.933 0.01 1 116 25 32 GLU HA H 4.260 0.01 1 117 25 32 GLU C C 176.753 0.2 1 118 25 32 GLU CA C 56.902 0.2 1 119 25 32 GLU CB C 29.769 0.2 1 120 25 32 GLU N N 117.718 0.1 1 121 26 33 ASN H H 8.055 0.01 1 122 26 33 ASN HA H 4.780 0.01 1 123 26 33 ASN C C 175.427 0.2 1 124 26 33 ASN CA C 53.653 0.2 1 125 26 33 ASN CB C 38.929 0.2 1 126 26 33 ASN N N 117.471 0.1 1 127 27 34 VAL H H 7.962 0.01 1 128 27 34 VAL HA H 4.080 0.01 1 129 27 34 VAL C C 176.027 0.2 1 130 27 34 VAL CA C 62.973 0.2 1 131 27 34 VAL CB C 32.679 0.2 1 132 27 34 VAL N N 119.223 0.1 1 133 28 35 ALA H H 8.272 0.01 1 134 28 35 ALA C C 177.303 0.2 1 135 28 35 ALA CA C 52.370 0.2 1 136 28 35 ALA CB C 19.577 0.2 1 137 28 35 ALA N N 124.923 0.1 1 138 29 36 ALA H H 8.175 0.01 1 139 29 36 ALA C C 177.948 0.2 1 140 29 36 ALA CA C 52.720 0.2 1 141 29 36 ALA CB C 19.295 0.2 1 142 29 36 ALA N N 122.172 0.1 1 143 30 37 THR H H 7.994 0.01 1 144 30 37 THR C C 175.077 0.2 1 145 30 37 THR CA C 62.693 0.2 1 146 30 37 THR CB C 69.167 0.2 1 147 30 37 THR N N 112.010 0.1 1 148 31 38 ASP H H 8.305 0.01 1 149 31 38 ASP N N 121.306 0.1 1 150 32 39 ASP C C 177.493 0.2 1 151 32 39 ASP CA C 55.383 0.2 1 152 32 39 ASP CB C 40.956 0.2 1 153 33 40 VAL H H 7.841 0.01 1 154 33 40 VAL C C 177.337 0.2 1 155 33 40 VAL CA C 65.152 0.2 1 156 33 40 VAL CB C 32.002 0.2 1 157 33 40 VAL N N 119.882 0.1 1 158 34 41 LEU H H 8.247 0.01 1 159 34 41 LEU C C 178.149 0.2 1 160 34 41 LEU CA C 57.617 0.2 1 161 34 41 LEU CB C 41.237 0.2 1 162 34 41 LEU N N 120.649 0.1 1 163 35 42 ASP H H 7.953 0.01 1 164 35 42 ASP C C 178.620 0.2 1 165 35 42 ASP CA C 57.348 0.2 1 166 35 42 ASP CB C 40.763 0.2 1 167 35 42 ASP N N 118.330 0.1 1 168 36 43 VAL H H 7.582 0.01 1 169 36 43 VAL HA H 3.860 0.01 1 170 36 43 VAL C C 178.585 0.2 1 171 36 43 VAL CA C 65.323 0.2 1 172 36 43 VAL CB C 32.089 0.2 1 173 36 43 VAL N N 118.572 0.1 1 174 37 44 LEU H H 7.923 0.01 1 175 37 44 LEU HA H 4.110 0.01 1 176 37 44 LEU C C 178.793 0.2 1 177 37 44 LEU CA C 57.847 0.2 1 178 37 44 LEU CB C 42.486 0.2 1 179 37 44 LEU N N 120.795 0.1 1 180 38 45 LEU H H 8.512 0.01 1 181 38 45 LEU CA C 57.780 0.2 1 182 38 45 LEU CB C 41.530 0.2 1 183 38 45 LEU N N 118.626 0.1 1 184 45 52 THR C C 174.387 0.2 1 185 45 52 THR CA C 61.965 0.2 1 186 45 52 THR CB C 69.437 0.2 1 187 46 53 GLU H H 8.102 0.01 1 188 46 53 GLU CA C 56.620 0.2 1 189 46 53 GLU CB C 30.400 0.2 1 190 46 53 GLU N N 121.931 0.1 1 191 48 55 PRO HA H 4.390 0.01 1 192 48 55 PRO C C 177.103 0.2 1 193 48 55 PRO CA C 63.857 0.2 1 194 48 55 PRO CB C 32.100 0.2 1 195 49 56 ASP H H 8.857 0.01 1 196 49 56 ASP HA H 4.640 0.01 1 197 49 56 ASP C C 177.077 0.2 1 198 49 56 ASP CA C 54.440 0.2 1 199 49 56 ASP CB C 41.129 0.2 1 200 49 56 ASP N N 120.020 0.1 1 201 50 57 GLY H H 8.332 0.01 1 202 50 57 GLY C C 174.848 0.2 1 203 50 57 GLY CA C 45.415 0.2 1 204 50 57 GLY N N 109.390 0.1 1 205 51 58 GLY H H 8.388 0.01 1 206 51 58 GLY N N 108.887 0.1 1 207 53 60 GLY HA2 H 3.960 0.01 2 208 53 60 GLY C C 174.635 0.2 1 209 53 60 GLY CA C 45.371 0.2 1 210 54 61 GLY H H 8.254 0.01 1 211 54 61 GLY HA2 H 3.880 0.01 2 212 54 61 GLY C C 173.094 0.2 1 213 54 61 GLY CA C 45.076 0.2 1 214 54 61 GLY N N 108.422 0.1 1 215 55 62 TYR H H 7.934 0.01 1 216 55 62 TYR C C 174.701 0.2 1 217 55 62 TYR CA C 57.779 0.2 1 218 55 62 TYR CB C 39.082 0.2 1 219 55 62 TYR N N 122.299 0.1 1 220 56 63 TYR H H 8.096 0.01 1 221 56 63 TYR CA C 55.390 0.2 1 222 56 63 TYR CB C 38.860 0.2 1 223 56 63 TYR N N 124.108 0.1 1 224 57 64 PRO HA H 4.270 0.01 1 225 57 64 PRO C C 176.683 0.2 1 226 57 64 PRO CA C 62.914 0.2 1 227 57 64 PRO CB C 31.956 0.2 1 228 58 65 SER H H 8.375 0.01 1 229 58 65 SER HA H 4.380 0.01 1 230 58 65 SER C C 174.735 0.2 1 231 58 65 SER CA C 58.355 0.2 1 232 58 65 SER CB C 63.900 0.2 1 233 58 65 SER N N 116.274 0.1 1 234 59 66 ASP H H 8.418 0.01 1 235 59 66 ASP HA H 4.560 0.01 1 236 59 66 ASP C C 176.073 0.2 1 237 59 66 ASP CA C 54.795 0.2 1 238 59 66 ASP CB C 40.958 0.2 1 239 59 66 ASP N N 121.838 0.1 1 240 60 67 ASN H H 8.286 0.01 1 241 60 67 ASN HA H 4.710 0.01 1 242 60 67 ASN C C 174.822 0.2 1 243 60 67 ASN CA C 53.112 0.2 1 244 60 67 ASN CB C 38.815 0.2 1 245 60 67 ASN N N 117.913 0.1 1 246 61 68 ARG H H 8.006 0.01 1 247 61 68 ARG HA H 4.240 0.01 1 248 61 68 ARG C C 175.695 0.2 1 249 61 68 ARG CA C 56.353 0.2 1 250 61 68 ARG CB C 31.039 0.2 1 251 61 68 ARG N N 121.531 0.1 1 252 62 69 ASP H H 8.425 0.01 1 253 62 69 ASP C C 175.256 0.2 1 254 62 69 ASP CA C 53.789 0.2 1 255 62 69 ASP CB C 41.216 0.2 1 256 62 69 ASP N N 122.613 0.1 1 257 63 70 ASP H H 8.157 0.01 1 258 63 70 ASP HA H 4.650 0.01 1 259 63 70 ASP C C 175.924 0.2 1 260 63 70 ASP CA C 53.464 0.2 1 261 63 70 ASP CB C 40.623 0.2 1 262 63 70 ASP N N 122.542 0.1 1 263 64 71 SER H H 8.262 0.01 1 264 64 71 SER CA C 57.030 0.2 1 265 64 71 SER CB C 63.500 0.2 1 266 64 71 SER N N 116.361 0.1 1 267 65 72 PRO C C 177.470 0.2 1 268 66 73 GLU H H 9.130 0.01 1 269 66 73 GLU C C 179.470 0.2 1 270 66 73 GLU CA C 60.433 0.2 1 271 66 73 GLU CB C 28.564 0.2 1 272 66 73 GLU N N 115.290 0.1 1 273 67 74 GLY H H 8.179 0.01 1 274 67 74 GLY C C 176.788 0.2 1 275 67 74 GLY CA C 46.728 0.2 1 276 67 74 GLY N N 110.880 0.1 1 277 68 75 ILE H H 8.470 0.01 1 278 68 75 ILE C C 178.308 0.2 1 279 68 75 ILE CA C 64.494 0.2 1 280 68 75 ILE N N 124.314 0.1 1 281 69 76 VAL H H 8.074 0.01 1 282 69 76 VAL HA H 3.630 0.01 1 283 69 76 VAL C C 177.287 0.2 1 284 69 76 VAL CA C 67.676 0.2 1 285 69 76 VAL CB C 31.270 0.2 1 286 69 76 VAL N N 119.101 0.1 1 287 70 77 LYS H H 7.734 0.01 1 288 70 77 LYS HA H 4.020 0.01 1 289 70 77 LYS C C 178.585 0.2 1 290 70 77 LYS CA C 60.149 0.2 1 291 70 77 LYS CB C 32.679 0.2 1 292 70 77 LYS N N 119.926 0.1 1 293 71 78 GLU H H 7.861 0.01 1 294 71 78 GLU C C 179.915 0.2 1 295 71 78 GLU CA C 59.413 0.2 1 296 71 78 GLU CB C 29.510 0.2 1 297 71 78 GLU N N 119.015 0.1 1 298 72 79 ILE H H 8.684 0.01 1 299 72 79 ILE C C 177.997 0.2 1 300 72 79 ILE CA C 65.513 0.2 1 301 72 79 ILE N N 120.905 0.1 1 302 73 80 LYS H H 8.769 0.01 1 303 73 80 LYS C C 180.179 0.2 1 304 73 80 LYS CA C 60.404 0.2 1 305 73 80 LYS CB C 32.845 0.2 1 306 73 80 LYS N N 120.103 0.1 1 307 74 81 GLU H H 8.216 0.01 1 308 74 81 GLU HA H 4.120 0.01 1 309 74 81 GLU C C 178.943 0.2 1 310 74 81 GLU CA C 59.232 0.2 1 311 74 81 GLU CB C 29.543 0.2 1 312 74 81 GLU N N 119.492 0.1 1 313 75 82 TRP H H 8.561 0.01 1 314 75 82 TRP C C 179.276 0.2 1 315 75 82 TRP CA C 61.130 0.2 1 316 75 82 TRP N N 123.126 0.1 1 317 76 83 ARG H H 8.830 0.01 1 318 76 83 ARG C C 178.322 0.2 1 319 76 83 ARG CA C 58.670 0.2 1 320 76 83 ARG N N 118.700 0.1 1 321 77 84 ALA H H 7.769 0.01 1 322 77 84 ALA CA C 54.950 0.2 1 323 77 84 ALA CB C 18.030 0.2 1 324 77 84 ALA N N 120.736 0.1 1 325 78 85 ALA H H 8.090 0.01 1 326 78 85 ALA C C 178.490 0.2 1 327 78 85 ALA CA C 54.200 0.2 1 328 78 85 ALA CB C 18.510 0.2 1 329 78 85 ALA N N 121.100 0.1 1 330 79 86 ASN H H 7.200 0.01 1 331 79 86 ASN C C 174.591 0.2 1 332 79 86 ASN CA C 53.150 0.2 1 333 79 86 ASN CB C 39.830 0.2 1 334 79 86 ASN N N 113.650 0.1 1 335 80 87 GLY H H 7.747 0.01 1 336 80 87 GLY HA2 H 3.860 0.01 2 337 80 87 GLY C C 174.438 0.2 1 338 80 87 GLY CA C 46.783 0.2 1 339 80 87 GLY N N 108.827 0.1 1 340 81 88 LYS H H 8.027 0.01 1 341 81 88 LYS CA C 52.500 0.2 1 342 81 88 LYS CB C 32.520 0.2 1 343 81 88 LYS N N 119.493 0.1 1 344 82 89 PRO HA H 4.310 0.01 1 345 82 89 PRO C C 176.670 0.2 1 346 82 89 PRO CA C 62.875 0.2 1 347 82 89 PRO CB C 32.315 0.2 1 348 83 90 GLY H H 8.306 0.01 1 349 83 90 GLY C C 173.952 0.2 1 350 83 90 GLY CA C 43.493 0.2 1 351 83 90 GLY N N 109.905 0.1 1 352 84 91 PHE H H 8.117 0.01 1 353 84 91 PHE C C 176.388 0.2 1 354 84 91 PHE CA C 59.404 0.2 1 355 84 91 PHE CB C 39.817 0.2 1 356 84 91 PHE N N 119.325 0.1 1 357 85 92 LYS H H 8.460 0.01 1 358 85 92 LYS HA H 4.180 0.01 1 359 85 92 LYS C C 176.568 0.2 1 360 85 92 LYS CA C 57.059 0.2 1 361 85 92 LYS CB C 32.905 0.2 1 362 85 92 LYS N N 123.913 0.1 1 363 86 93 GLN H H 8.647 0.01 1 364 86 93 GLN HA H 4.300 0.01 1 365 86 93 GLN C C 175.458 0.2 1 366 86 93 GLN CA C 56.238 0.2 1 367 86 93 GLN CB C 29.693 0.2 1 368 86 93 GLN N N 124.332 0.1 1 369 87 94 GLY H H 8.056 0.01 1 370 87 94 GLY CA C 46.220 0.2 1 371 87 94 GLY N N 116.869 0.1 1 stop_ save_