data_25748 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; ddFLN5+110 ; _BMRB_accession_number 25748 _BMRB_flat_file_name bmr25748.str _Entry_type original _Submission_date 2015-08-10 _Accession_date 2015-08-10 _Entry_origination author _NMR_STAR_version 2.1.1 _Experimental_method NMR _Details 'Structural ensemble of ddFLN5+110 RNC: 3 representative ground state structures' loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Cabrita Lisa D. . 2 Cassaignau Anais ME . 3 Launay Helene MM . 4 Waudby Christopher A. . 5 Camilloni Carlo . . 6 Robertson Amy L. . 7 Wang Xiaolin . . 8 Wlodarski Tomasz . . 9 Wentink Anne S. . 10 Vendruscolo Michele . . 11 Dobson Christopher M. . 12 Christodoulou John . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 204 "13C chemical shifts" 271 "15N chemical shifts" 122 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2016-08-05 update BMRB 'update entry citation' 2016-02-29 original author 'original release' stop_ _Original_release_date 2016-02-29 save_ ############################# # Citation for this entry # ############################# save_citation_1 _Saveframe_category entry_citation _Citation_full . _Citation_title ; A strategy for co-translational folding studies of ribosome-bound nascent chain complexes using NMR spectroscopy ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 27466710 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Cassaignau Anais ME . 2 Launay Helene MM . 3 Karyadi Maria-Evangelia . . 4 Wang Xiaolin . . 5 Waudby Christopher A. . 6 Deckert Annika . . 7 Robertson Amy L. . 8 Christodoulou John . . 9 Cabrita Lisa D. . stop_ _Journal_abbreviation 'Nat. Protoc.' _Journal_volume 11 _Journal_issue 8 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 1492 _Page_last 1507 _Year 2016 _Details . save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name ddFLN5+110 _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label entity $entity stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state ? _System_paramagnetic no _System_thiol_state . _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_entity _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common entity _Molecular_mass 23420.918 _Mol_thiol_state . _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 221 _Mol_residue_sequence ; HHHHHHASKPAPSAEHSYAE GEGLVKVFDNAPAEFTIFAV DTKGVARTDGGDPFEVAING PDGLVVDAKVTDNNDGTYGV VYDAPVEGNYNVNVTLRGNP IKNMPIDVKCIEGANGEDSS FGSFTFTVAAKNKKGEVKTY GGDKFEVSITGPAEEITLDA IDNQDGTYTAAYSLVGNGRF STGVKLNGKHIEGSPFKQVL GNELFSTPVWISQAQGIRAG P ; loop_ _Residue_seq_code _Residue_label 1 HIS 2 HIS 3 HIS 4 HIS 5 HIS 6 HIS 7 ALA 8 SER 9 LYS 10 PRO 11 ALA 12 PRO 13 SER 14 ALA 15 GLU 16 HIS 17 SER 18 TYR 19 ALA 20 GLU 21 GLY 22 GLU 23 GLY 24 LEU 25 VAL 26 LYS 27 VAL 28 PHE 29 ASP 30 ASN 31 ALA 32 PRO 33 ALA 34 GLU 35 PHE 36 THR 37 ILE 38 PHE 39 ALA 40 VAL 41 ASP 42 THR 43 LYS 44 GLY 45 VAL 46 ALA 47 ARG 48 THR 49 ASP 50 GLY 51 GLY 52 ASP 53 PRO 54 PHE 55 GLU 56 VAL 57 ALA 58 ILE 59 ASN 60 GLY 61 PRO 62 ASP 63 GLY 64 LEU 65 VAL 66 VAL 67 ASP 68 ALA 69 LYS 70 VAL 71 THR 72 ASP 73 ASN 74 ASN 75 ASP 76 GLY 77 THR 78 TYR 79 GLY 80 VAL 81 VAL 82 TYR 83 ASP 84 ALA 85 PRO 86 VAL 87 GLU 88 GLY 89 ASN 90 TYR 91 ASN 92 VAL 93 ASN 94 VAL 95 THR 96 LEU 97 ARG 98 GLY 99 ASN 100 PRO 101 ILE 102 LYS 103 ASN 104 MET 105 PRO 106 ILE 107 ASP 108 VAL 109 LYS 110 CYS 111 ILE 112 GLU 113 GLY 114 ALA 115 ASN 116 GLY 117 GLU 118 ASP 119 SER 120 SER 121 PHE 122 GLY 123 SER 124 PHE 125 THR 126 PHE 127 THR 128 VAL 129 ALA 130 ALA 131 LYS 132 ASN 133 LYS 134 LYS 135 GLY 136 GLU 137 VAL 138 LYS 139 THR 140 TYR 141 GLY 142 GLY 143 ASP 144 LYS 145 PHE 146 GLU 147 VAL 148 SER 149 ILE 150 THR 151 GLY 152 PRO 153 ALA 154 GLU 155 GLU 156 ILE 157 THR 158 LEU 159 ASP 160 ALA 161 ILE 162 ASP 163 ASN 164 GLN 165 ASP 166 GLY 167 THR 168 TYR 169 THR 170 ALA 171 ALA 172 TYR 173 SER 174 LEU 175 VAL 176 GLY 177 ASN 178 GLY 179 ARG 180 PHE 181 SER 182 THR 183 GLY 184 VAL 185 LYS 186 LEU 187 ASN 188 GLY 189 LYS 190 HIS 191 ILE 192 GLU 193 GLY 194 SER 195 PRO 196 PHE 197 LYS 198 GLN 199 VAL 200 LEU 201 GLY 202 ASN 203 GLU 204 LEU 205 PHE 206 SER 207 THR 208 PRO 209 VAL 210 TRP 211 ILE 212 SER 213 GLN 214 ALA 215 GLN 216 GLY 217 ILE 218 ARG 219 ALA 220 GLY 221 PRO 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 $entity 'E. 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 $entity 'recombinant technology' . Escherichia coli BL21 pLDC-17 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 $entity 10 uM [U-15N] HEPES 10 mM 'natural abundance' 'ammonium chloride' 30 mM 'natural abundance' MgCl2 12 mM 'natural abundance' BME 2 mM 'natural abundance' EDTA 1 mM 'natural abundance' stop_ save_ save_sample_2 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $entity 10 uM '[U-100% 2H, Ile d1-13CH3]' HEPES 10 mM [U-2H] 'ammonium chloride' 30 mM [U-2H] MgCl2 12 mM [U-2H] BME 2 mM [U-2H] EDTA 1 mM [U-2H] stop_ save_ ############################ # Computer software used # ############################ save_GROMACS _Saveframe_category software _Name GROMACS _Version 5.0.4 loop_ _Vendor _Address _Electronic_address GROMACS . . stop_ loop_ _Task 'structure calculation using molecular dynamics simulations with chemical shifts restraints' stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_UCL _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model Avance _Field_strength 700 _Details . save_ ############################# # NMR applied experiments # ############################# save_2D_1H-15N_SOFAST_HMQC_1 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-15N SOFAST HMQC' _Sample_label $sample_1 save_ save_2D_1H-13C_HMQC_2 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-13C HMQC' _Sample_label $sample_2 save_ ####################### # Sample conditions # ####################### save_sample_conditions_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 7.5 . 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 na indirect . . . 0.251449530 DSS H 1 'methyl protons' ppm 0.00 internal direct . . . 1.000000000 DSS N 15 'methyl protons' ppm 0.00 na 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_ _Experiment_label '2D 1H-15N SOFAST HMQC' '2D 1H-13C HMQC' stop_ loop_ _Sample_label $sample_1 $sample_2 stop_ _Sample_conditions_label $sample_conditions_1 _Chem_shift_reference_set_label $chemical_shift_reference_1 _Mol_system_component_name entity _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 9 9 LYS HA H 4.716 . . 2 9 9 LYS C C 174.2 . . 3 9 9 LYS N N 127.57 . . 4 10 10 PRO HA H 4.311 . . 5 10 10 PRO CA C 63.914 . . 6 10 10 PRO CB C 33.667 . . 7 11 11 ALA HA H 4.75 . . 8 11 11 ALA CA C 49.511 . . 9 11 11 ALA CB C 19.654 . . 10 11 11 ALA N N 125.53 . . 11 12 12 PRO HA H 4.271 . . 12 12 12 PRO CA C 62.896 . . 13 12 12 PRO CB C 32.802 . . 14 13 13 SER H H 9.134 . . 15 13 13 SER HA H 4.79 . . 16 13 13 SER CB C 65.273 . . 17 13 13 SER N N 112.92 . . 18 14 14 ALA HA H 4.123 . . 19 14 14 ALA C C 176.9 . . 20 14 14 ALA CA C 55.869 . . 21 14 14 ALA CB C 18.573 . . 22 15 15 GLU H H 7.961 . . 23 15 15 GLU HA H 3.976 . . 24 15 15 GLU C C 177.4 . . 25 15 15 GLU CA C 59.262 . . 26 15 15 GLU N N 113.92 . . 27 16 16 HIS H H 7.079 . . 28 16 16 HIS HA H 4.801 . . 29 16 16 HIS C C 177.1 . . 30 16 16 HIS CA C 57.21 . . 31 16 16 HIS CB C 34.31 . . 32 16 16 HIS N N 111.76 . . 33 17 17 SER HA H 4.932 . . 34 17 17 SER C C 170.5 . . 35 17 17 SER CA C 62.209 . . 36 17 17 SER N N 117.17 . . 37 18 18 TYR H H 8.434 . . 38 18 18 TYR HA H 5.025 . . 39 18 18 TYR C C 171 . . 40 18 18 TYR CA C 56.719 . . 41 18 18 TYR CB C 41.183 . . 42 18 18 TYR N N 116.81 . . 43 19 19 ALA H H 9.626 . . 44 19 19 ALA C C 175.8 . . 45 19 19 ALA CA C 50.603 . . 46 19 19 ALA CB C 24.198 . . 47 20 20 GLU HA H 4.822 . . 48 20 20 GLU CA C 56.443 . . 49 20 20 GLU CB C 35.93 . . 50 21 21 GLY H H 8.85 . . 51 21 21 GLY C C 174 . . 52 21 21 GLY N N 112.61 . . 53 22 22 GLU HA H 4.17 . . 54 22 22 GLU C C 175.2 . . 55 22 22 GLU CA C 60.141 . . 56 22 22 GLU CB C 29.728 . . 57 22 22 GLU N N 126.71 . . 58 23 23 GLY H H 9.097 . . 59 23 23 GLY C C 171.8 . . 60 23 23 GLY CA C 46.815 . . 61 23 23 GLY N N 104.40 . . 62 24 24 LEU H H 7.691 . . 63 24 24 LEU HA H 4.436 . . 64 24 24 LEU C C 176.2 . . 65 24 24 LEU CA C 54.243 . . 66 24 24 LEU CB C 42.197 . . 67 25 25 VAL H H 8.068 . . 68 25 25 VAL HA H 4.133 . . 69 25 25 VAL C C 175.2 . . 70 25 25 VAL CA C 65.137 . . 71 25 25 VAL CB C 35.26 . . 72 25 25 VAL N N 121.21 . . 73 26 26 LYS H H 8.31 . . 74 26 26 LYS C C 172.8 . . 75 26 26 LYS CA C 57.416 . . 76 26 26 LYS CB C 34.117 . . 77 26 26 LYS N N 121.83 . . 78 27 27 VAL H H 7.924 . . 79 27 27 VAL HA H 4.327 . . 80 27 27 VAL C C 172.7 . . 81 27 27 VAL CB C 35.388 . . 82 27 27 VAL N N 122.63 . . 83 28 28 PHE H H 9.087 . . 84 28 28 PHE HA H 5.794 . . 85 28 28 PHE C C 176.8 . . 86 28 28 PHE CA C 56.27 . . 87 28 28 PHE CB C 43.815 . . 88 28 28 PHE N N 121.77 . . 89 29 29 ASP H H 8.029 . . 90 29 29 ASP C C 177.2 . . 91 29 29 ASP CA C 54.81 . . 92 29 29 ASP N N 119.10 . . 93 30 30 ASN H H 7.76 . . 94 30 30 ASN HA H 4.758 . . 95 30 30 ASN C C 175.2 . . 96 30 30 ASN CA C 51.712 . . 97 30 30 ASN N N 115.82 . . 98 31 31 ALA H H 7.487 . . 99 31 31 ALA HA H 4.879 . . 100 31 31 ALA C C 174.5 . . 101 31 31 ALA CA C 50.67 . . 102 31 31 ALA CB C 21.572 . . 103 31 31 ALA N N 122.14 . . 104 32 32 PRO HA H 4.288 . . 105 32 32 PRO CA C 63.901 . . 106 32 32 PRO CB C 32.711 . . 107 33 33 ALA H H 8.891 . . 108 33 33 ALA HA H 4.557 . . 109 33 33 ALA C C 175.9 . . 110 33 33 ALA CA C 50.95 . . 111 33 33 ALA CB C 21.424 . . 112 33 33 ALA N N 127.97 . . 113 34 34 GLU H H 8.441 . . 114 34 34 GLU HA H 5.733 . . 115 34 34 GLU C C 177 . . 116 34 34 GLU CA C 54.868 . . 117 34 34 GLU N N 117.64 . . 118 35 35 PHE H H 8.822 . . 119 35 35 PHE HA H 5.125 . . 120 35 35 PHE C C 171.4 . . 121 35 35 PHE CA C 57.91 . . 122 35 35 PHE CB C 40.633 . . 123 35 35 PHE N N 116.25 . . 124 36 36 THR H H 8.921 . . 125 36 36 THR HA H 5.215 . . 126 36 36 THR C C 173 . . 127 36 36 THR CA C 61.722 . . 128 36 36 THR CB C 72.286 . . 129 36 36 THR N N 116.75 . . 130 37 37 ILE H H 9.341 . . 131 37 37 ILE HA H 4.117 . . 132 37 37 ILE CA C 61.674 . . 133 37 37 ILE CB C 40.296 . . 134 37 37 ILE N N 125.37 . . 135 38 38 PHE HA H 4.267 . . 136 38 38 PHE C C 173.7 . . 137 38 38 PHE CA C 57.897 . . 138 38 38 PHE CB C 38.901 . . 139 38 38 PHE N N 128.05 . . 140 39 39 ALA H H 8.669 . . 141 39 39 ALA HA H 4.625 . . 142 39 39 ALA C C 177.6 . . 143 39 39 ALA CA C 51.898 . . 144 39 39 ALA CB C 21.666 . . 145 39 39 ALA N N 124.89 . . 146 40 40 VAL H H 9.264 . . 147 40 40 VAL HA H 4.363 . . 148 40 40 VAL C C 174.2 . . 149 40 40 VAL CA C 62.025 . . 150 40 40 VAL CB C 35.713 . . 151 40 40 VAL N N 127.58 . . 152 41 41 ASP H H 9.028 . . 153 41 41 ASP HA H 5.14 . . 154 41 41 ASP C C 177.9 . . 155 41 41 ASP CB C 43.361 . . 156 42 42 THR H H 7.527 . . 157 42 42 THR HA H 4.051 . . 158 42 42 THR C C 175.6 . . 159 42 42 THR CA C 64.46 . . 160 42 42 THR CB C 69.48 . . 161 42 42 THR N N 104.59 . . 162 43 43 LYS HA H 4.475 . . 163 43 43 LYS C C 176.9 . . 164 43 43 LYS CA C 55.375 . . 165 43 43 LYS CB C 32.361 . . 166 43 43 LYS N N 122.01 . . 167 44 44 GLY H H 8.109 . . 168 44 44 GLY C C 173.8 . . 169 44 44 GLY CA C 45.612 . . 170 45 45 VAL HA H 4.021 . . 171 45 45 VAL C C 175.8 . . 172 45 45 VAL CB C 32.407 . . 173 46 46 ALA H H 8.859 . . 174 46 46 ALA HA H 4.553 . . 175 46 46 ALA C C 179.7 . . 176 46 46 ALA CA C 54.602 . . 177 46 46 ALA CB C 18.657 . . 178 46 46 ALA N N 131.52 . . 179 47 47 ARG H H 8.71 . . 180 47 47 ARG HA H 4.454 . . 181 47 47 ARG C C 177 . . 182 47 47 ARG CA C 55.657 . . 183 47 47 ARG CB C 29.619 . . 184 48 48 THR HA H 4.365 . . 185 48 48 THR C C 174 . . 186 48 48 THR CB C 69.834 . . 187 48 48 THR N N 106.99 . . 188 49 49 ASP H H 7.495 . . 189 49 49 ASP HA H 4.266 . . 190 49 49 ASP C C 174.4 . . 191 49 49 ASP CA C 52.969 . . 192 49 49 ASP N N 118.94 . . 193 50 50 GLY C C 175 . . 194 50 50 GLY CA C 45.511 . . 195 50 50 GLY N N 104.09 . . 196 51 51 GLY H H 9.903 . . 197 51 51 GLY C C 175.3 . . 198 51 51 GLY N N 108.58 . . 199 52 52 ASP H H 8.634 . . 200 52 52 ASP HA H 5.165 . . 201 52 52 ASP C C 176.2 . . 202 52 52 ASP CA C 52.296 . . 203 52 52 ASP CB C 41.866 . . 204 52 52 ASP N N 121.97 . . 205 53 53 PRO HA H 4.687 . . 206 53 53 PRO C C 175.3 . . 207 53 53 PRO CA C 63.065 . . 208 53 53 PRO CB C 28.228 . . 209 54 54 PHE H H 7.669 . . 210 54 54 PHE HA H 4.701 . . 211 54 54 PHE C C 175.9 . . 212 54 54 PHE CB C 41.026 . . 213 54 54 PHE N N 123.15 . . 214 55 55 GLU H H 9.012 . . 215 55 55 GLU HA H 4.59 . . 216 55 55 GLU C C 174.5 . . 217 55 55 GLU CA C 55.321 . . 218 55 55 GLU CB C 33.345 . . 219 55 55 GLU N N 121.62 . . 220 56 56 VAL HA H 4.654 . . 221 56 56 VAL C C 173.9 . . 222 56 56 VAL CA C 61.785 . . 223 56 56 VAL CB C 34.428 . . 224 56 56 VAL N N 121.00 . . 225 57 57 ALA H H 8.614 . . 226 57 57 ALA HA H 4.88 . . 227 57 57 ALA C C 176.2 . . 228 57 57 ALA CA C 51.335 . . 229 57 57 ALA CB C 21.544 . . 230 58 58 ILE H H 9.111 . . 231 58 58 ILE HA H 5.154 . . 232 58 58 ILE C C 174.1 . . 233 58 58 ILE CA C 60.77 . . 234 58 58 ILE CB C 40.805 . . 235 58 58 ILE N N 124.67 . . 236 59 59 ASN H H 8.717 . . 237 59 59 ASN C C 175.2 . . 238 59 59 ASN CA C 52.603 . . 239 59 59 ASN CB C 42.648 . . 240 59 59 ASN N N 126.04 . . 241 60 60 GLY H H 9.367 . . 242 60 60 GLY C C 170.2 . . 243 60 60 GLY CA C 45.127 . . 244 60 60 GLY N N 112.22 . . 245 61 61 PRO C C 177.3 . . 246 61 61 PRO CA C 63.778 . . 247 61 61 PRO CB C 32.396 . . 248 62 62 ASP H H 8.907 . . 249 62 62 ASP HA H 4.259 . . 250 62 62 ASP C C 176.1 . . 251 62 62 ASP CA C 55.54 . . 252 62 62 ASP CB C 40.358 . . 253 62 62 ASP N N 119.83 . . 254 63 63 GLY H H 8.129 . . 255 63 63 GLY C C 174.6 . . 256 63 63 GLY CA C 46.091 . . 257 63 63 GLY N N 104.86 . . 258 64 64 LEU H H 7.146 . . 259 64 64 LEU HA H 4.117 . . 260 64 64 LEU C C 176.2 . . 261 64 64 LEU CA C 56.387 . . 262 64 64 LEU CB C 43.874 . . 263 64 64 LEU N N 123.21 . . 264 65 65 VAL H H 8.609 . . 265 65 65 VAL HA H 4.348 . . 266 65 65 VAL C C 176 . . 267 65 65 VAL CA C 63.4 . . 268 65 65 VAL CB C 33.119 . . 269 65 65 VAL N N 129.00 . . 270 66 66 VAL H H 8.049 . . 271 66 66 VAL HA H 4.215 . . 272 66 66 VAL C C 174.6 . . 273 66 66 VAL CA C 61.736 . . 274 66 66 VAL CB C 34.084 . . 275 66 66 VAL N N 128.79 . . 276 67 67 ASP H H 8.931 . . 277 67 67 ASP HA H 4.819 . . 278 67 67 ASP C C 175.1 . . 279 67 67 ASP CA C 54.071 . . 280 67 67 ASP CB C 41.779 . . 281 67 67 ASP N N 127.71 . . 282 68 68 ALA H H 8.733 . . 283 68 68 ALA HA H 4.681 . . 284 68 68 ALA C C 176.4 . . 285 68 68 ALA CA C 51.536 . . 286 68 68 ALA CB C 20.87 . . 287 69 69 LYS H H 8.869 . . 288 69 69 LYS HA H 4.585 . . 289 69 69 LYS C C 175.8 . . 290 69 69 LYS CA C 56.283 . . 291 69 69 LYS CB C 33.495 . . 292 69 69 LYS N N 123.26 . . 293 70 70 VAL H H 8.857 . . 294 70 70 VAL C C 176.3 . . 295 70 70 VAL CA C 61.665 . . 296 70 70 VAL CB C 33.7 . . 297 71 71 THR H H 9.918 . . 298 71 71 THR HA H 4.408 . . 299 71 71 THR C C 172.9 . . 300 71 71 THR CA C 62.228 . . 301 71 71 THR CB C 71.175 . . 302 71 71 THR N N 126.49 . . 303 72 72 ASP H H 8.851 . . 304 72 72 ASP HA H 4.268 . . 305 72 72 ASP C C 176.2 . . 306 72 72 ASP CA C 53.688 . . 307 72 72 ASP CB C 41.427 . . 308 72 72 ASP N N 126.80 . . 309 73 73 ASN H H 7.471 . . 310 73 73 ASN HA H 4.513 . . 311 73 73 ASN C C 174.6 . . 312 73 73 ASN CA C 54.507 . . 313 73 73 ASN CB C 38.008 . . 314 73 73 ASN N N 125.07 . . 315 74 74 ASN H H 9.49 . . 316 74 74 ASN HA H 4.042 . . 317 74 74 ASN C C 173.2 . . 318 74 74 ASN CA C 54.77 . . 319 74 74 ASN CB C 37.65 . . 320 74 74 ASN N N 117.18 . . 321 75 75 ASP H H 7.795 . . 322 75 75 ASP C C 175.6 . . 323 75 75 ASP CA C 53.177 . . 324 75 75 ASP CB C 41.593 . . 325 75 75 ASP N N 116.04 . . 326 76 76 GLY H H 8.17 . . 327 76 76 GLY C C 172.5 . . 328 76 76 GLY CA C 45.63 . . 329 76 76 GLY N N 109.92 . . 330 77 77 THR H H 8.02 . . 331 77 77 THR HA H 5.568 . . 332 77 77 THR C C 175.2 . . 333 77 77 THR CA C 59.855 . . 334 77 77 THR CB C 73.354 . . 335 77 77 THR N N 108.77 . . 336 78 78 TYR H H 8.696 . . 337 78 78 TYR HA H 5.029 . . 338 78 78 TYR C C 175.7 . . 339 78 78 TYR CA C 56.571 . . 340 78 78 TYR CB C 40.641 . . 341 78 78 TYR N N 120.07 . . 342 79 79 GLY H H 9.166 . . 343 79 79 GLY C C 172.8 . . 344 79 79 GLY CA C 46.042 . . 345 79 79 GLY N N 112.43 . . 346 80 80 VAL H H 8.767 . . 347 80 80 VAL HA H 4.872 . . 348 80 80 VAL C C 175.2 . . 349 80 80 VAL CA C 61.315 . . 350 80 80 VAL CB C 33.38 . . 351 80 80 VAL N N 124.09 . . 352 81 81 VAL H H 8.39 . . 353 81 81 VAL HA H 5.345 . . 354 81 81 VAL C C 174.8 . . 355 81 81 VAL CA C 60.478 . . 356 81 81 VAL CB C 35.918 . . 357 81 81 VAL N N 126.33 . . 358 82 82 TYR H H 9.34 . . 359 82 82 TYR HA H 5.041 . . 360 82 82 TYR CA C 56.558 . . 361 82 82 TYR CB C 41.816 . . 362 82 82 TYR N N 124.09 . . 363 83 83 ASP H H 8.211 . . 364 83 83 ASP HA H 4.691 . . 365 83 83 ASP C C 173.7 . . 366 83 83 ASP CA C 53.657 . . 367 83 83 ASP CB C 43.583 . . 368 83 83 ASP N N 119.35 . . 369 84 84 ALA H H 8.782 . . 370 84 84 ALA HA H 3.768 . . 371 84 84 ALA C C 174.8 . . 372 84 84 ALA CA C 51.329 . . 373 84 84 ALA CB C 19.596 . . 374 84 84 ALA N N 127.59 . . 375 85 85 PRO HA H 4.548 . . 376 85 85 PRO C C 176.7 . . 377 85 85 PRO CA C 64.847 . . 378 86 86 VAL H H 6.898 . . 379 86 86 VAL HA H 4.671 . . 380 86 86 VAL C C 175.2 . . 381 86 86 VAL CA C 59.668 . . 382 86 86 VAL CB C 36.21 . . 383 86 86 VAL N N 113.19 . . 384 87 87 GLU H H 9.111 . . 385 87 87 GLU HA H 4.144 . . 386 87 87 GLU C C 174.1 . . 387 87 87 GLU CA C 57.846 . . 388 87 87 GLU CB C 30.466 . . 389 87 87 GLU N N 126.51 . . 390 88 88 GLY H H 8.303 . . 391 88 88 GLY C C 171.9 . . 392 88 88 GLY CA C 44.237 . . 393 89 89 ASN H H 8.517 . . 394 89 89 ASN C C 174.5 . . 395 89 89 ASN CA C 54.688 . . 396 89 89 ASN CB C 41.341 . . 397 89 89 ASN N N 119.44 . . 398 90 90 TYR H H 9.563 . . 399 90 90 TYR HA H 4.725 . . 400 90 90 TYR C C 173.6 . . 401 90 90 TYR CA C 57.468 . . 402 90 90 TYR CB C 39.83 . . 403 90 90 TYR N N 124.87 . . 404 91 91 ASN H H 8.981 . . 405 91 91 ASN C C 173.5 . . 406 91 91 ASN CA C 53.683 . . 407 91 91 ASN CB C 42.515 . . 408 91 91 ASN N N 122.94 . . 409 92 92 VAL H H 9.474 . . 410 92 92 VAL HA H 4.211 . . 411 92 92 VAL C C 173 . . 412 92 92 VAL CA C 62.377 . . 413 92 92 VAL CB C 33.585 . . 414 92 92 VAL N N 128.75 . . 415 93 93 ASN H H 8.921 . . 416 93 93 ASN HA H 5.264 . . 417 93 93 ASN C C 174.9 . . 418 93 93 ASN CA C 51.338 . . 419 93 93 ASN CB C 41.909 . . 420 93 93 ASN N N 123.48 . . 421 94 94 VAL H H 7.569 . . 422 94 94 VAL C C 174.6 . . 423 94 94 VAL CA C 61.483 . . 424 94 94 VAL CB C 33.264 . . 425 94 94 VAL N N 127.74 . . 426 95 95 THR H H 9.229 . . 427 95 95 THR C C 173 . . 428 95 95 THR CA C 59.315 . . 429 95 95 THR CB C 73.581 . . 430 95 95 THR N N 116.06 . . 431 96 96 LEU H H 8.737 . . 432 96 96 LEU HA H 4.351 . . 433 96 96 LEU C C 176.1 . . 434 96 96 LEU CA C 53.956 . . 435 96 96 LEU CB C 44.842 . . 436 96 96 LEU N N 119.77 . . 437 97 97 ARG HA H 3.855 . . 438 97 97 ARG C C 176 . . 439 97 97 ARG CA C 57.361 . . 440 97 97 ARG CB C 28.437 . . 441 97 97 ARG N N 128.72 . . 442 98 98 GLY H H 8.763 . . 443 98 98 GLY C C 173.6 . . 444 98 98 GLY CA C 45.399 . . 445 98 98 GLY N N 102.86 . . 446 99 99 ASN H H 7.665 . . 447 99 99 ASN HA H 5.293 . . 448 99 99 ASN C C 172.3 . . 449 99 99 ASN CB C 40.278 . . 450 99 99 ASN N N 119.97 . . 451 100 100 PRO HA H 4.643 . . 452 100 100 PRO C C 177 . . 453 100 100 PRO CA C 63.506 . . 454 100 100 PRO CB C 32.437 . . 455 101 101 ILE H H 7.672 . . 456 101 101 ILE HA H 4.741 . . 457 101 101 ILE C C 174.3 . . 458 101 101 ILE CA C 60.625 . . 459 101 101 ILE CB C 36.617 . . 460 101 101 ILE N N 113.84 . . 461 102 102 LYS HA H 5.276 . . 462 102 102 LYS C C 177.1 . . 463 102 102 LYS CB C 33.176 . . 464 102 102 LYS N N 119.97 . . 465 103 103 ASN H H 8.902 . . 466 103 103 ASN HA H 4.359 . . 467 103 103 ASN C C 172.2 . . 468 103 103 ASN CA C 54.735 . . 469 103 103 ASN CB C 37.855 . . 470 103 103 ASN N N 117.18 . . 471 104 104 MET H H 7.519 . . 472 104 104 MET HA H 4.822 . . 473 104 104 MET CB C 33.53 . . 474 104 104 MET N N 115.88 . . 475 105 105 PRO HA H 4.931 . . 476 105 105 PRO C C 175.3 . . 477 105 105 PRO CA C 62.332 . . 478 105 105 PRO CB C 36.146 . . 479 106 106 ILE H H 9.06 . . 480 106 106 ILE HA H 4.552 . . 481 106 106 ILE C C 173.3 . . 482 106 106 ILE CA C 60.399 . . 483 106 106 ILE CB C 43.209 . . 484 106 106 ILE N N 119.54 . . 485 107 107 ASP H H 8.157 . . 486 107 107 ASP HA H 5.55 . . 487 107 107 ASP C C 175.4 . . 488 107 107 ASP CA C 54.609 . . 489 107 107 ASP CB C 43.134 . . 490 108 108 VAL H H 9.62 . . 491 108 108 VAL HA H 4.12 . . 492 108 108 VAL CA C 61.445 . . 493 109 109 LYS H H 8.304 . . 494 109 109 LYS HA H 4.731 . . 495 109 109 LYS C C 174.8 . . 496 109 109 LYS CA C 56.086 . . 497 109 109 LYS CB C 33.983 . . 498 109 109 LYS N N 126.76 . . 499 110 110 CYS H H 9.287 . . 500 110 110 CYS HA H 5.043 . . 501 110 110 CYS C C 175.2 . . 502 110 110 CYS CA C 55.178 . . 503 110 110 CYS CB C 29.587 . . 504 110 110 CYS N N 125.24 . . 505 111 111 ILE H H 8.698 . . 506 111 111 ILE HA H 4.732 . . 507 111 111 ILE C C 174.4 . . 508 111 111 ILE CA C 59.727 . . 509 111 111 ILE CB C 41.668 . . 510 111 111 ILE N N 126.5 . . 511 112 112 GLU H H 8.407 . . 512 112 112 GLU HA H 4.177 . . 513 112 112 GLU C C 177 . . 514 112 112 GLU CA C 57.547 . . 515 112 112 GLU N N 121.72 . . 516 113 113 GLY H H 8.792 . . 517 113 113 GLY C C 179.4 . . 518 113 113 GLY CA C 46.332 . . 519 113 113 GLY N N 119.50 . . 520 114 114 ALA H H 8.255 . . 521 114 114 ALA N N 124.44 . . 522 115 115 ASN H H 8.441 . . 523 115 115 ASN N N 118.60 . . 524 116 116 GLY H H 8.352 . . 525 116 116 GLY N N 109.63 . . 526 117 117 GLU H H 8.339 . . 527 117 117 GLU N N 120.44 . . 528 118 118 ASP H H 8.394 . . 529 118 118 ASP N N 121.36 . . 530 119 119 SER H H 8.302 . . 531 119 119 SER N N 116.87 . . 532 122 122 GLY H H 8.198 . . 533 122 122 GLY N N 110.49 . . 534 128 128 VAL H H 8.12 . . 535 128 128 VAL N N 122.63 . . 536 130 130 ALA H H 8.158 . . 537 130 130 ALA N N 122.85 . . 538 131 131 LYS H H 8.193 . . 539 131 131 LYS N N 119.90 . . 540 134 134 LYS H H 8.323 . . 541 134 134 LYS N N 122.35 . . 542 135 135 GLY H H 8.363 . . 543 135 135 GLY N N 109.93 . . 544 136 136 GLU H H 8.152 . . 545 136 136 GLU N N 120.49 . . 546 137 137 VAL H H 8.272 . . 547 137 137 VAL N N 122.20 . . 548 138 138 LYS H H 8.461 . . 549 138 138 LYS N N 125.97 . . 550 139 139 THR H H 8.111 . . 551 139 139 THR N N 115.73 . . 552 144 144 LYS H H 8.19 . . 553 144 144 LYS N N 120.88 . . 554 145 145 PHE H H 8.19 . . 555 145 145 PHE N N 120.88 . . 556 146 146 GLU H H 8.26 . . 557 146 146 GLU N N 122.71 . . 558 148 148 SER H H 8.403 . . 559 148 148 SER N N 119.88 . . 560 149 149 ILE H H 8.285 . . 561 149 149 ILE N N 123.05 . . 562 150 150 THR H H 8.205 . . 563 150 150 THR N N 117.56 . . 564 151 151 GLY H H 8.215 . . 565 151 151 GLY N N 111.72 . . 566 153 153 ALA H H 8.425 . . 567 153 153 ALA N N 124.42 . . 568 155 155 GLU H H 8.383 . . 569 155 155 GLU N N 122.33 . . 570 156 156 ILE H H 8.227 . . 571 156 156 ILE N N 122.86 . . 572 158 158 LEU H H 8.395 . . 573 158 158 LEU N N 125.81 . . 574 159 159 ASP H H 8.293 . . 575 159 159 ASP N N 121.15 . . 576 160 160 ALA H H 8.108 . . 577 160 160 ALA N N 124.15 . . 578 161 161 ILE H H 8.088 . . 579 161 161 ILE N N 120.08 . . 580 162 162 ASP H H 8.332 . . 581 162 162 ASP N N 124.13 . . 582 165 165 ASP H H 8.329 . . 583 165 165 ASP N N 120.58 . . 584 166 166 GLY H H 8.342 . . 585 166 166 GLY N N 109.48 . . 586 167 167 THR H H 8.049 . . 587 167 167 THR N N 113.84 . . 588 168 168 TYR H H 8.259 . . 589 168 168 TYR N N 122.86 . . 590 171 171 ALA H H 8.132 . . 591 171 171 ALA N N 123.91 . . 592 197 197 LYS H H 8.026 . . 593 197 197 LYS N N 123.15 . . 594 198 198 GLN H H 8.314 . . 595 198 198 GLN N N 122.51 . . 596 199 199 VAL H H 8.277 . . 597 199 199 VAL N N 122.61 . . stop_ save_