data_19411 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Conformation and dynamics of the periplasmic membrane-protein chaperone complexes OmpX Skp and tOmpA Skp ; _BMRB_accession_number 19411 _BMRB_flat_file_name bmr19411.str _Entry_type original _Submission_date 2013-08-03 _Accession_date 2013-08-03 _Entry_origination author _NMR_STAR_version 2.1.1 _Experimental_method NMR _Details 'OmpX backbone chemical shifts when bound to the Skp chaperone' loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Burmann Bjoern M. . 2 Wang Congwei . . 3 Hiller Sebastian . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 129 "13C chemical shifts" 236 "15N chemical shifts" 129 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2015-07-16 update author 'update entry citation' 2013-09-10 original author 'original release' stop_ loop_ _Related_BMRB_accession_number _Relationship 19407 'Corresponding chemical shifts of Skp when bound to its substrate OmpX' 19408 'Corresponding chemical shifts of apo-SKP' 19409 'Trimeric Skp with bound tOmpA' 19410 'tOmpA within the trimeric chaperone Skp' stop_ _Original_release_date 2015-07-16 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; Conformation and dynamics of the periplasmic membrane-protein-chaperone complexes OmpX-Skp and tOmpA-Skp ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 24077225 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Burmann Bjoern M. . 2 Wang Congwei . . 3 Hiller Sebastian . . stop_ _Journal_abbreviation 'Nat. Struct. Mol. Biol.' _Journal_name_full 'Nature Structural and Molecular Biology' _Journal_volume 20 _Journal_issue 11 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 1265 _Page_last 1272 _Year 2013 _Details . save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name 'OmpX within the trimeric chaperone Skp' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label OmpX $Escherichia_Coli_OmpX 'Skp, chain 1' $Escherichia_Coli_Skp 'Skp, chain 2' $Escherichia_Coli_Skp 'Skp, chain 3' $Escherichia_Coli_Skp stop_ _System_molecular_weight 64100 _System_physical_state unfolded _System_oligomer_state ? _System_paramagnetic no _System_thiol_state . _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_Escherichia_Coli_OmpX _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common Escherichia_Coli_OmpX _Molecular_mass . _Mol_thiol_state 'not present' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 149 _Mol_residue_sequence ; MATSTVTGGYAQSDMQGVMN KTNGFNLKYRYEQQNNPLGV IGSFTYTEKDRTASSGDYNK NQYYGITAGPAYRINDWASI YGVVGVGYGKFQTTEYPTYK HDTSDYGFSYGAGLQFNPME NVALDFSYEQSRIRSVDVGT WIAGVGYRF ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 0 MET 2 1 ALA 3 2 THR 4 3 SER 5 4 THR 6 5 VAL 7 6 THR 8 7 GLY 9 8 GLY 10 9 TYR 11 10 ALA 12 11 GLN 13 12 SER 14 13 ASP 15 14 MET 16 15 GLN 17 16 GLY 18 17 VAL 19 18 MET 20 19 ASN 21 20 LYS 22 21 THR 23 22 ASN 24 23 GLY 25 24 PHE 26 25 ASN 27 26 LEU 28 27 LYS 29 28 TYR 30 29 ARG 31 30 TYR 32 31 GLU 33 32 GLN 34 33 GLN 35 34 ASN 36 35 ASN 37 36 PRO 38 37 LEU 39 38 GLY 40 39 VAL 41 40 ILE 42 41 GLY 43 42 SER 44 43 PHE 45 44 THR 46 45 TYR 47 46 THR 48 47 GLU 49 48 LYS 50 49 ASP 51 50 ARG 52 51 THR 53 52 ALA 54 53 SER 55 54 SER 56 55 GLY 57 56 ASP 58 57 TYR 59 58 ASN 60 59 LYS 61 60 ASN 62 61 GLN 63 62 TYR 64 63 TYR 65 64 GLY 66 65 ILE 67 66 THR 68 67 ALA 69 68 GLY 70 69 PRO 71 70 ALA 72 71 TYR 73 72 ARG 74 73 ILE 75 74 ASN 76 75 ASP 77 76 TRP 78 77 ALA 79 78 SER 80 79 ILE 81 80 TYR 82 81 GLY 83 82 VAL 84 83 VAL 85 84 GLY 86 85 VAL 87 86 GLY 88 87 TYR 89 88 GLY 90 89 LYS 91 90 PHE 92 91 GLN 93 92 THR 94 93 THR 95 94 GLU 96 95 TYR 97 96 PRO 98 97 THR 99 98 TYR 100 99 LYS 101 100 HIS 102 101 ASP 103 102 THR 104 103 SER 105 104 ASP 106 105 TYR 107 106 GLY 108 107 PHE 109 108 SER 110 109 TYR 111 110 GLY 112 111 ALA 113 112 GLY 114 113 LEU 115 114 GLN 116 115 PHE 117 116 ASN 118 117 PRO 119 118 MET 120 119 GLU 121 120 ASN 122 121 VAL 123 122 ALA 124 123 LEU 125 124 ASP 126 125 PHE 127 126 SER 128 127 TYR 129 128 GLU 130 129 GLN 131 130 SER 132 131 ARG 133 132 ILE 134 133 ARG 135 134 SER 136 135 VAL 137 136 ASP 138 137 VAL 139 138 GLY 140 139 THR 141 140 TRP 142 141 ILE 143 142 ALA 144 143 GLY 145 144 VAL 146 145 GLY 147 146 TYR 148 147 ARG 149 148 PHE stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-11-04 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 EMBL CSY35436 "outer membrane protein X [Shigella sonnei]" 73.83 110 98.18 99.09 3.37e-71 GB KFS26214 "membrane protein, partial [Salmonella enterica subsp. enterica serovar Bareilly str. CFSAN000952]" 59.06 89 97.73 100.00 6.76e-55 stop_ save_ save_Escherichia_Coli_Skp _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common Escherichia_Coli_Skp _Molecular_mass . _Mol_thiol_state 'not present' _Details . _Residue_count 234 _Mol_residue_sequence ; MGSSHHHHHHSSGLVPRGSH MADKIAIVNMGSLFQQVAQK TGVSNTLENEFKGRASELQR METDLQAKMKKLQSMKAGSD RTKLEKDVMAQRQTFAQKAQ AFEQDRARRSNEERGKLVTR IQTAVKSVANSQDIDLVVDA NAVAYNSSDVKDITADVLKQ VKIYGVVGVGYGKFQQTENQ GLNRTASNSDYGFSYGAGMQ FNPIENVALDFSYEQSRIRN VDVGTWIAGVGYRF ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 0 MET 2 1 GLY 3 2 SER 4 3 SER 5 4 HIS 6 5 HIS 7 6 HIS 8 7 HIS 9 8 HIS 10 9 HIS 11 10 SER 12 11 SER 13 12 GLY 14 13 LEU 15 14 VAL 16 15 PRO 17 16 ARG 18 17 GLY 19 18 SER 20 19 HIS 21 20 MET 22 21 ALA 23 22 ASP 24 23 LYS 25 24 ILE 26 25 ALA 27 26 ILE 28 27 VAL 29 28 ASN 30 29 MET 31 30 GLY 32 31 SER 33 32 LEU 34 33 PHE 35 34 GLN 36 35 GLN 37 36 VAL 38 37 ALA 39 38 GLN 40 39 LYS 41 40 THR 42 41 GLY 43 42 VAL 44 43 SER 45 44 ASN 46 45 THR 47 46 LEU 48 47 GLU 49 48 ASN 50 49 GLU 51 50 PHE 52 51 LYS 53 52 GLY 54 53 ARG 55 54 ALA 56 55 SER 57 56 GLU 58 57 LEU 59 58 GLN 60 59 ARG 61 60 MET 62 61 GLU 63 62 THR 64 63 ASP 65 64 LEU 66 65 GLN 67 66 ALA 68 67 LYS 69 68 MET 70 69 LYS 71 70 LYS 72 71 LEU 73 72 GLN 74 73 SER 75 74 MET 76 75 LYS 77 76 ALA 78 77 GLY 79 78 SER 80 79 ASP 81 80 ARG 82 81 THR 83 82 LYS 84 83 LEU 85 84 GLU 86 85 LYS 87 86 ASP 88 87 VAL 89 88 MET 90 89 ALA 91 90 GLN 92 91 ARG 93 92 GLN 94 93 THR 95 94 PHE 96 95 ALA 97 96 GLN 98 97 LYS 99 98 ALA 100 99 GLN 101 100 ALA 102 101 PHE 103 102 GLU 104 103 GLN 105 104 ASP 106 105 ARG 107 106 ALA 108 107 ARG 109 108 ARG 110 109 SER 111 110 ASN 112 111 GLU 113 112 GLU 114 113 ARG 115 114 GLY 116 115 LYS 117 116 LEU 118 117 VAL 119 118 THR 120 119 ARG 121 120 ILE 122 121 GLN 123 122 THR 124 123 ALA 125 124 VAL 126 125 LYS 127 126 SER 128 127 VAL 129 128 ALA 130 129 ASN 131 130 SER 132 131 GLN 133 132 ASP 134 133 ILE 135 134 ASP 136 135 LEU 137 136 VAL 138 137 VAL 139 138 ASP 140 139 ALA 141 140 ASN 142 141 ALA 143 142 VAL 144 143 ALA 145 144 TYR 146 145 ASN 147 146 SER 148 147 SER 149 148 ASP 150 149 VAL 151 150 LYS 152 151 ASP 153 152 ILE 154 153 THR 155 154 ALA 156 155 ASP 157 156 VAL 158 157 LEU 159 158 LYS 160 159 GLN 161 160 VAL 162 161 LYS 163 162 ILE 164 163 TYR 165 164 GLY 166 165 VAL 167 166 VAL 168 167 GLY 169 168 VAL 170 169 GLY 171 170 TYR 172 171 GLY 173 172 LYS 174 173 PHE 175 174 GLN 176 175 GLN 177 176 THR 178 177 GLU 179 178 ASN 180 179 GLN 181 180 GLY 182 181 LEU 183 182 ASN 184 183 ARG 185 184 THR 186 185 ALA 187 186 SER 188 187 ASN 189 188 SER 190 189 ASP 191 190 TYR 192 191 GLY 193 192 PHE 194 193 SER 195 194 TYR 196 195 GLY 197 196 ALA 198 197 GLY 199 198 MET 200 199 GLN 201 200 PHE 202 201 ASN 203 202 PRO 204 203 ILE 205 204 GLU 206 205 ASN 207 206 VAL 208 207 ALA 209 208 LEU 210 209 ASP 211 210 PHE 212 211 SER 213 212 TYR 214 213 GLU 215 214 GLN 216 215 SER 217 216 ARG 218 217 ILE 219 218 ARG 220 219 ASN 221 220 VAL 222 221 ASP 223 222 VAL 224 223 GLY 225 224 THR 226 225 TRP 227 226 ILE 228 227 ALA 229 228 GLY 230 229 VAL 231 230 GLY 232 231 TYR 233 232 ARG 234 233 PHE stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date . 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 UNP P0AEU7 . . . . . . stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species _Strain $Escherichia_Coli_OmpX 'E. coli' 562 Bacteria . Escherichia coli K12 $Escherichia_Coli_Skp 'E. coli' 562 Bacteria . Escherichia coli K12 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 $Escherichia_Coli_OmpX 'recombinant technology' . Escherichia coli 'BL21 (DE3)' pET28B-OmpX $Escherichia_Coli_Skp 'recombinant technology' . Escherichia coli 'BL21 (DE3)' pET28B-Skp stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Saveframe_category sample _Sample_type solution _Details 'Protein samples were produced as a 3:1 ratio (Skp monomer per OmpX)' loop_ _Mol_label _Concentration_value _Concentration_value_units _Concentration_min_value _Concentration_max_value _Isotopic_labeling $Escherichia_Coli_OmpX . mM 0.6 1.05 '[U-13C; U-15N; U-2H]' $Escherichia_Coli_Skp . mM 0.6 1.05 '[U-99% 2H]' H2O 95 % . . 'natural abundance' D2O 5 % . . 'natural abundance' MES 25 mM . . 'natural abundance' NaCl 150 mM . . 'natural abundance' stop_ save_ ############################ # Computer software used # ############################ save_TOPSPIN _Saveframe_category software _Name TOPSPIN _Version 3.2 loop_ _Vendor _Address _Electronic_address 'Bartels et al.' . . 'Bruker Biospin' . . Guntert . . 'Keller and Wuthrich' . . stop_ loop_ _Task 'chemical shift assignment' collection 'data analysis' processing stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model AscendII _Field_strength 700 _Details . save_ save_spectrometer_2 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model Avance _Field_strength 800 _Details . save_ ############################# # NMR applied experiments # ############################# save_2D_1H-15N_HSQC_1 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-15N HSQC' _Sample_label $sample_1 save_ save_3D_HNCA_2 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCA' _Sample_label $sample_1 save_ save_3D_HNCO_3 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCO' _Sample_label $sample_1 save_ save_3D_HNCACB_4 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCACB' _Sample_label $sample_1 save_ ####################### # Sample conditions # ####################### save_sample_conditions_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units 'ionic strength' 0.150 . M pH 6.5 . pH pressure 1 . atm temperature 310 . K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference_1 _Saveframe_category chemical_shift_reference _Details . loop_ _Mol_common_name _Atom_type _Atom_isotope_number _Atom_group _Chem_shift_units _Chem_shift_value _Reference_method _Reference_type _External_reference_sample_geometry _External_reference_location _External_reference_axis _Indirect_shift_ratio DSS C 13 'methyl protons' ppm 0.00 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 HSQC' '3D HNCA' '3D HNCO' '3D HNCACB' 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 OmpX _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 3 4 SER H H 8.02 0.02 1 2 3 4 SER CA C 57.9 0.3 1 3 3 4 SER CB C 63.8 0.3 1 4 3 4 SER N N 115.6 0.3 1 5 4 5 THR H H 7.98 0.02 1 6 4 5 THR CA C 61.3 0.3 1 7 4 5 THR CB C 69.2 0.3 1 8 4 5 THR N N 115.6 0.3 1 9 5 6 VAL H H 8.13 0.02 1 10 5 6 VAL CA C 61.9 0.3 1 11 5 6 VAL CB C 31.6 0.3 1 12 5 6 VAL N N 122.4 0.3 1 13 6 7 THR H H 8.13 0.02 1 14 6 7 THR CA C 61.5 0.3 1 15 6 7 THR CB C 69.5 0.3 1 16 6 7 THR N N 117.4 0.3 1 17 7 8 GLY H H 8.28 0.02 1 18 7 8 GLY CA C 44.9 0.3 1 19 7 8 GLY N N 111.5 0.3 1 20 8 9 GLY H H 8.14 0.02 1 21 8 9 GLY CA C 44.8 0.3 1 22 8 9 GLY N N 108.9 0.3 1 23 9 10 TYR H H 7.98 0.02 1 24 9 10 TYR CA C 57.5 0.3 1 25 9 10 TYR CB C 38.0 0.3 1 26 9 10 TYR N N 120.3 0.3 1 27 10 11 ALA H H 8.18 0.02 1 28 10 11 ALA CA C 51.9 0.3 1 29 10 11 ALA CB C 18.3 0.3 1 30 10 11 ALA N N 125.7 0.3 1 31 11 12 GLN H H 8.17 0.02 1 32 11 12 GLN CA C 55.6 0.3 1 33 11 12 GLN CB C 28.5 0.3 1 34 11 12 GLN N N 119.9 0.3 1 35 12 13 SER H H 8.23 0.02 1 36 12 13 SER CA C 58.1 0.3 1 37 12 13 SER CB C 63.2 0.3 1 38 12 13 SER N N 116.8 0.3 1 39 13 14 ASP H H 8.30 0.02 1 40 13 14 ASP CA C 54.1 0.3 1 41 13 14 ASP CB C 40.5 0.3 1 42 13 14 ASP N N 122.7 0.3 1 43 14 15 MET H H 8.14 0.02 1 44 14 15 MET CA C 52.7 0.3 1 45 14 15 MET CB C 18.0 0.3 1 46 14 15 MET N N 124.2 0.3 1 47 15 16 GLN H H 8.22 0.02 1 48 15 16 GLN CA C 55.9 0.3 1 49 15 16 GLN CB C 28.3 0.3 1 50 15 16 GLN N N 118.6 0.3 1 51 16 17 GLY H H 8.24 0.02 1 52 16 17 GLY CA C 45.2 0.3 1 53 16 17 GLY N N 109.4 0.3 1 54 17 18 VAL H H 8.16 0.02 1 55 17 18 VAL CA C 55.7 0.3 1 56 17 18 VAL CB C 28.5 0.3 1 57 17 18 VAL N N 119.9 0.3 1 58 18 19 MET H H 8.30 0.02 1 59 18 19 MET CA C 55.6 0.3 1 60 18 19 MET CB C 31.9 0.3 1 61 18 19 MET N N 120.8 0.3 1 62 19 20 ASN H H 8.31 0.02 1 63 19 20 ASN CA C 53.1 0.3 1 64 19 20 ASN CB C 38.4 0.3 1 65 19 20 ASN N N 119.6 0.3 1 66 20 21 LYS H H 8.15 0.02 1 67 20 21 LYS CA C 56.2 0.3 1 68 20 21 LYS CB C 31.9 0.3 1 69 20 21 LYS N N 121.5 0.3 1 70 21 22 THR H H 8.26 0.02 1 71 21 22 THR CA C 55.2 0.3 1 72 21 22 THR CB C 31.9 0.3 1 73 21 22 THR N N 120.6 0.3 1 74 22 23 ASN H H 8.23 0.02 1 75 22 23 ASN CA C 45.1 0.3 1 76 22 23 ASN N N 109.7 0.3 1 77 23 24 GLY H H 8.13 0.02 1 78 23 24 GLY CA C 45.0 0.3 1 79 23 24 GLY N N 108.7 0.3 1 80 24 25 PHE H H 8.18 0.02 1 81 24 25 PHE CA C 57.4 0.3 1 82 24 25 PHE CB C 38.3 0.3 1 83 24 25 PHE N N 120.1 0.3 1 84 25 26 ASN H H 7.96 0.02 1 85 25 26 ASN CA C 54.8 0.3 1 86 25 26 ASN CB C 40.0 0.3 1 87 25 26 ASN N N 125.3 0.3 1 88 26 27 LEU H H 8.15 0.02 1 89 26 27 LEU CA C 56.2 0.3 1 90 26 27 LEU CB C 41.4 0.3 1 91 26 27 LEU N N 121.6 0.3 1 92 27 28 LYS H H 8.30 0.02 1 93 27 28 LYS CA C 56.2 0.3 1 94 27 28 LYS CB C 32.0 0.3 1 95 27 28 LYS N N 122.1 0.3 1 96 29 30 ARG H H 8.06 0.02 1 97 29 30 ARG CA C 55.1 0.3 1 98 29 30 ARG CB C 31.0 0.3 1 99 29 30 ARG N N 117.3 0.3 1 100 30 31 TYR H H 8.08 0.02 1 101 30 31 TYR CA C 57.8 0.3 1 102 30 31 TYR CB C 37.9 0.3 1 103 30 31 TYR N N 121.7 0.3 1 104 31 32 GLU H H 8.17 0.02 1 105 31 32 GLU CA C 53.0 0.3 1 106 31 32 GLU CB C 28.5 0.3 1 107 31 32 GLU N N 119.9 0.3 1 108 32 33 GLN H H 8.23 0.02 1 109 32 33 GLN CA C 55.9 0.3 1 110 32 33 GLN CB C 28.4 0.3 1 111 32 33 GLN N N 118.7 0.3 1 112 34 35 ASN H H 8.23 0.02 1 113 34 35 ASN CA C 52.7 0.3 1 114 34 35 ASN CB C 38.3 0.3 1 115 34 35 ASN N N 119.6 0.3 1 116 35 36 ASN H H 8.16 0.02 1 117 35 36 ASN CA C 56.4 0.3 1 118 35 36 ASN CB C 62.8 0.3 1 119 35 36 ASN N N 117.2 0.3 1 120 37 38 LEU H H 8.06 0.02 1 121 37 38 LEU CA C 55.0 0.3 1 122 37 38 LEU CB C 41.0 0.3 1 123 37 38 LEU N N 120.2 0.3 1 124 38 39 GLY H H 8.08 0.02 1 125 38 39 GLY CA C 45.0 0.3 1 126 38 39 GLY N N 108.7 0.3 1 127 39 40 VAL H H 7.85 0.02 1 128 39 40 VAL CA C 62.0 0.3 1 129 39 40 VAL CB C 31.5 0.3 1 130 39 40 VAL N N 119.1 0.3 1 131 40 41 ILE H H 8.07 0.02 1 132 40 41 ILE CA C 61.0 0.3 1 133 40 41 ILE CB C 37.4 0.3 1 134 40 41 ILE N N 123.4 0.3 1 135 41 42 GLY H H 8.25 0.02 1 136 41 42 GLY CA C 44.9 0.3 1 137 41 42 GLY N N 112.2 0.3 1 138 42 43 SER H H 7.97 0.02 1 139 42 43 SER CA C 57.9 0.3 1 140 42 43 SER CB C 63.3 0.3 1 141 42 43 SER N N 115.6 0.3 1 142 43 44 PHE H H 8.00 0.02 1 143 43 44 PHE CA C 55.4 0.3 1 144 43 44 PHE CB C 37.7 0.3 1 145 43 44 PHE N N 121.5 0.3 1 146 44 45 THR H H 8.14 0.02 1 147 44 45 THR CA C 61.3 0.3 1 148 44 45 THR CB C 69.2 0.3 1 149 44 45 THR N N 115.1 0.3 1 150 45 46 TYR H H 8.02 0.02 1 151 45 46 TYR CA C 57.3 0.3 1 152 45 46 TYR CB C 37.8 0.3 1 153 45 46 TYR N N 121.8 0.3 1 154 46 47 THR H H 7.94 0.02 1 155 46 47 THR CA C 61.3 0.3 1 156 46 47 THR CB C 69.4 0.3 1 157 46 47 THR N N 115.4 0.3 1 158 47 48 GLU H H 8.28 0.02 1 159 47 48 GLU CA C 56.5 0.3 1 160 47 48 GLU CB C 29.4 0.3 1 161 47 48 GLU N N 123.6 0.3 1 162 48 49 LYS H H 8.21 0.02 1 163 48 49 LYS CA C 56.3 0.3 1 164 48 49 LYS CB C 31.9 0.3 1 165 48 49 LYS N N 122.2 0.3 1 166 49 50 ASP H H 8.16 0.02 1 167 49 50 ASP CA C 58.2 0.3 1 168 49 50 ASP CB C 63.2 0.3 1 169 49 50 ASP N N 116.3 0.3 1 170 50 51 ARG H H 8.24 0.02 1 171 50 51 ARG CA C 56.0 0.3 1 172 50 51 ARG CB C 29.7 0.3 1 173 50 51 ARG N N 123.0 0.3 1 174 51 52 THR H H 8.02 0.02 1 175 51 52 THR CA C 61.4 0.3 1 176 51 52 THR CB C 69.4 0.3 1 177 51 52 THR N N 114.4 0.3 1 178 52 53 ALA H H 8.18 0.02 1 179 52 53 ALA CA C 52.3 0.3 1 180 52 53 ALA CB C 18.3 0.3 1 181 52 53 ALA N N 126.1 0.3 1 182 53 54 SER H H 8.20 0.02 1 183 53 54 SER CA C 57.8 0.3 1 184 53 54 SER CB C 63.1 0.3 1 185 53 54 SER N N 115.0 0.3 1 186 54 55 SER H H 8.17 0.02 1 187 54 55 SER CA C 56.5 0.3 1 188 54 55 SER CB C 63.1 0.3 1 189 54 55 SER N N 116.9 0.3 1 190 55 56 GLY H H 8.27 0.02 1 191 55 56 GLY CA C 45.1 0.3 1 192 55 56 GLY N N 110.6 0.3 1 193 56 57 ASP H H 8.04 0.02 1 194 56 57 ASP CA C 54.0 0.3 1 195 56 57 ASP CB C 40.6 0.3 1 196 56 57 ASP N N 120.6 0.3 1 197 57 58 TYR H H 7.99 0.02 1 198 57 58 TYR CA C 57.8 0.3 1 199 57 58 TYR CB C 37.7 0.3 1 200 57 58 TYR N N 120.1 0.3 1 201 58 59 ASN H H 7.95 0.02 1 202 58 59 ASN CA C 54.5 0.3 1 203 58 59 ASN CB C 41.5 0.3 1 204 58 59 ASN N N 121.0 0.3 1 205 60 61 ASN H H 8.16 0.02 1 206 60 61 ASN CA C 55.2 0.3 1 207 60 61 ASN CB C 38.3 0.3 1 208 60 61 ASN N N 121.3 0.3 1 209 61 62 GLN H H 8.17 0.02 1 210 61 62 GLN CA C 57.4 0.3 1 211 61 62 GLN CB C 28.7 0.3 1 212 61 62 GLN N N 120.2 0.3 1 213 63 64 TYR H H 7.95 0.02 1 214 63 64 TYR CA C 57.7 0.3 1 215 63 64 TYR CB C 37.9 0.3 1 216 63 64 TYR N N 120.9 0.3 1 217 64 65 GLY H H 7.79 0.02 1 218 64 65 GLY CA C 45.0 0.3 1 219 64 65 GLY N N 109.2 0.3 1 220 65 66 ILE H H 7.93 0.02 1 221 65 66 ILE CA C 60.9 0.3 1 222 65 66 ILE CB C 37.7 0.3 1 223 65 66 ILE N N 119.6 0.3 1 224 66 67 THR H H 8.02 0.02 1 225 66 67 THR CA C 61.1 0.3 1 226 66 67 THR CB C 69.3 0.3 1 227 66 67 THR N N 116.4 0.3 1 228 67 68 ALA H H 8.05 0.02 1 229 67 68 ALA CA C 51.8 0.3 1 230 67 68 ALA CB C 18.8 0.3 1 231 67 68 ALA N N 125.8 0.3 1 232 68 69 GLY H H 7.98 0.02 1 233 68 69 GLY CA C 44.1 0.3 1 234 68 69 GLY N N 107.9 0.3 1 235 70 71 ALA H H 8.28 0.02 1 236 70 71 ALA CA C 52.2 0.3 1 237 70 71 ALA CB C 18.2 0.3 1 238 70 71 ALA N N 123.3 0.3 1 239 71 72 TYR H H 7.75 0.02 1 240 71 72 TYR CA C 57.3 0.3 1 241 71 72 TYR CB C 37.5 0.3 1 242 71 72 TYR N N 117.7 0.3 1 243 72 73 ARG H H 8.30 0.02 1 244 72 73 ARG CA C 55.6 0.3 1 245 72 73 ARG CB C 32.0 0.3 1 246 72 73 ARG N N 121.1 0.3 1 247 73 74 ILE H H 8.00 0.02 1 248 73 74 ILE CA C 61.7 0.3 1 249 73 74 ILE CB C 39.7 0.3 1 250 73 74 ILE N N 121.9 0.3 1 251 75 76 ASP H H 8.18 0.02 1 252 75 76 ASP CA C 55.6 0.3 1 253 75 76 ASP CB C 41.1 0.3 1 254 75 76 ASP N N 120.3 0.3 1 255 76 77 TRP H H 7.81 0.02 1 256 76 77 TRP CA C 56.6 0.3 1 257 76 77 TRP CB C 29.3 0.3 1 258 76 77 TRP N N 120.5 0.3 1 259 77 78 ALA H H 8.13 0.02 1 260 77 78 ALA CA C 52.7 0.3 1 261 77 78 ALA CB C 18.2 0.3 1 262 77 78 ALA N N 123.8 0.3 1 263 78 79 SER H H 7.80 0.02 1 264 78 79 SER CA C 58.8 0.3 1 265 78 79 SER CB C 62.9 0.3 1 266 78 79 SER N N 113.6 0.3 1 267 79 80 ILE H H 7.72 0.02 1 268 79 80 ILE CA C 61.9 0.3 1 269 79 80 ILE CB C 39.2 0.3 1 270 79 80 ILE N N 120.8 0.3 1 271 81 82 GLY H H 7.83 0.02 1 272 81 82 GLY CA C 45.1 0.3 1 273 81 82 GLY N N 108.5 0.3 1 274 82 83 VAL H H 7.79 0.02 1 275 82 83 VAL CA C 61.9 0.3 1 276 82 83 VAL CB C 31.8 0.3 1 277 82 83 VAL N N 118.8 0.3 1 278 83 84 VAL H H 7.83 0.02 1 279 83 84 VAL CA C 61.8 0.3 1 280 83 84 VAL CB C 31.8 0.3 1 281 83 84 VAL N N 119.6 0.3 1 282 84 85 GLY H H 8.20 0.02 1 283 84 85 GLY CA C 44.9 0.3 1 284 84 85 GLY N N 111.7 0.3 1 285 85 86 VAL H H 7.84 0.02 1 286 85 86 VAL CA C 61.6 0.3 1 287 85 86 VAL CB C 31.8 0.3 1 288 85 86 VAL N N 118.5 0.3 1 289 86 87 GLY H H 8.31 0.02 1 290 86 87 GLY CA C 44.8 0.3 1 291 86 87 GLY N N 111.5 0.3 1 292 87 88 TYR H H 8.03 0.02 1 293 87 88 TYR CA C 57.8 0.3 1 294 87 88 TYR CB C 38.0 0.3 1 295 87 88 TYR N N 120.0 0.3 1 296 88 89 GLY H H 8.10 0.02 1 297 88 89 GLY CA C 44.9 0.3 1 298 88 89 GLY N N 108.9 0.3 1 299 89 90 LYS H H 7.89 0.02 1 300 89 90 LYS CA C 55.9 0.3 1 301 89 90 LYS CB C 32.1 0.3 1 302 89 90 LYS N N 120.6 0.3 1 303 92 93 THR H H 7.86 0.02 1 304 92 93 THR CA C 61.3 0.3 1 305 92 93 THR CB C 69.7 0.3 1 306 92 93 THR N N 115.5 0.3 1 307 93 94 THR H H 8.00 0.02 1 308 93 94 THR CA C 61.4 0.3 1 309 93 94 THR CB C 69.4 0.3 1 310 93 94 THR N N 113.8 0.3 1 311 94 95 GLU H H 8.25 0.02 1 312 94 95 GLU CA C 56.0 0.3 1 313 94 95 GLU CB C 29.7 0.3 1 314 94 95 GLU N N 123.1 0.3 1 315 95 96 TYR H H 8.00 0.02 1 316 95 96 TYR CA C 55.5 0.3 1 317 95 96 TYR CB C 37.5 0.3 1 318 95 96 TYR N N 121.4 0.3 1 319 99 100 LYS H H 8.25 0.02 1 320 99 100 LYS CA C 57.0 0.3 1 321 99 100 LYS CB C 33.4 0.3 1 322 99 100 LYS N N 121.3 0.3 1 323 100 101 HIS H H 8.22 0.02 1 324 100 101 HIS CA C 56.3 0.3 1 325 100 101 HIS CB C 29.4 0.3 1 326 100 101 HIS N N 121.4 0.3 1 327 101 102 ASP H H 8.33 0.02 1 328 101 102 ASP CA C 53.9 0.3 1 329 101 102 ASP CB C 40.7 0.3 1 330 101 102 ASP N N 121.5 0.3 1 331 102 103 THR H H 8.05 0.02 1 332 102 103 THR CA C 61.6 0.3 1 333 102 103 THR CB C 69.0 0.3 1 334 102 103 THR N N 114.1 0.3 1 335 103 104 SER H H 8.28 0.02 1 336 103 104 SER CA C 58.5 0.3 1 337 103 104 SER CB C 63.2 0.3 1 338 103 104 SER N N 117.9 0.3 1 339 104 105 ASP H H 8.10 0.02 1 340 104 105 ASP CA C 54.1 0.3 1 341 104 105 ASP CB C 40.7 0.3 1 342 104 105 ASP N N 122.0 0.3 1 343 105 106 TYR H H 8.22 0.02 1 344 105 106 TYR CA C 56.3 0.3 1 345 105 106 TYR CB C 37.4 0.3 1 346 105 106 TYR N N 121.2 0.3 1 347 106 107 GLY H H 8.21 0.02 1 348 106 107 GLY CA C 45.0 0.3 1 349 106 107 GLY N N 110.2 0.3 1 350 107 108 PHE H H 8.03 0.02 1 351 107 108 PHE CA C 57.3 0.3 1 352 107 108 PHE CB C 38.4 0.3 1 353 107 108 PHE N N 120.0 0.3 1 354 108 109 SER H H 8.08 0.02 1 355 108 109 SER CA C 57.7 0.3 1 356 108 109 SER CB C 63.5 0.3 1 357 108 109 SER N N 117.0 0.3 1 358 109 110 TYR H H 8.06 0.02 1 359 109 110 TYR CA C 58.1 0.3 1 360 109 110 TYR CB C 37.8 0.3 1 361 109 110 TYR N N 122.2 0.3 1 362 110 111 GLY H H 8.15 0.02 1 363 110 111 GLY CA C 45.1 0.3 1 364 110 111 GLY N N 110.0 0.3 1 365 111 112 ALA H H 7.96 0.02 1 366 111 112 ALA CA C 52.2 0.3 1 367 111 112 ALA CB C 18.3 0.3 1 368 111 112 ALA N N 123.8 0.3 1 369 112 113 GLY H H 8.23 0.02 1 370 112 113 GLY CA C 45.0 0.3 1 371 112 113 GLY N N 107.6 0.3 1 372 113 114 LEU H H 7.88 0.02 1 373 113 114 LEU CA C 54.7 0.3 1 374 113 114 LEU CB C 41.3 0.3 1 375 113 114 LEU N N 121.3 0.3 1 376 115 116 PHE H H 8.13 0.02 1 377 115 116 PHE CA C 57.1 0.3 1 378 115 116 PHE CB C 38.3 0.3 1 379 115 116 PHE N N 121.4 0.3 1 380 116 117 ASN H H 8.29 0.02 1 381 116 117 ASN CA C 53.9 0.3 1 382 116 117 ASN CB C 40.7 0.3 1 383 116 117 ASN N N 121.9 0.3 1 384 118 119 MET H H 7.95 0.02 1 385 118 119 MET CA C 57.4 0.3 1 386 118 119 MET CB C 33.1 0.3 1 387 118 119 MET N N 120.1 0.3 1 388 119 120 GLU H H 8.00 0.02 1 389 119 120 GLU CA C 55.7 0.3 1 390 119 120 GLU CB C 28.4 0.3 1 391 119 120 GLU N N 120.5 0.3 1 392 120 121 ASN H H 8.26 0.02 1 393 120 121 ASN CA C 53.1 0.3 1 394 120 121 ASN CB C 38.2 0.3 1 395 120 121 ASN N N 118.8 0.3 1 396 121 122 VAL H H 7.83 0.02 1 397 121 122 VAL CA C 61.9 0.3 1 398 121 122 VAL CB C 31.6 0.3 1 399 121 122 VAL N N 119.9 0.3 1 400 122 123 ALA H H 8.17 0.02 1 401 122 123 ALA CA C 52.5 0.3 1 402 122 123 ALA CB C 18.3 0.3 1 403 122 123 ALA N N 124.0 0.3 1 404 123 124 LEU H H 7.94 0.02 1 405 123 124 LEU CA C 53.0 0.3 1 406 123 124 LEU N N 122.5 0.3 1 407 125 126 PHE H H 8.00 0.02 1 408 125 126 PHE CA C 57.9 0.3 1 409 125 126 PHE CB C 37.7 0.3 1 410 125 126 PHE N N 120.5 0.3 1 411 127 128 TYR H H 8.17 0.02 1 412 127 128 TYR CA C 57.9 0.3 1 413 127 128 TYR CB C 38.0 0.3 1 414 127 128 TYR N N 122.7 0.3 1 415 128 129 GLU H H 8.27 0.02 1 416 128 129 GLU CA C 56.1 0.3 1 417 128 129 GLU CB C 29.5 0.3 1 418 128 129 GLU N N 122.4 0.3 1 419 129 130 GLN H H 8.45 0.02 1 420 129 130 GLN CA C 56.2 0.3 1 421 129 130 GLN CB C 29.4 0.3 1 422 129 130 GLN N N 122.2 0.3 1 423 130 131 SER H H 8.06 0.02 1 424 130 131 SER CA C 58.7 0.3 1 425 130 131 SER CB C 63.0 0.3 1 426 130 131 SER N N 115.7 0.3 1 427 131 132 ARG H H 8.23 0.02 1 428 131 132 ARG CA C 56.1 0.3 1 429 131 132 ARG CB C 31.6 0.3 1 430 131 132 ARG N N 122.2 0.3 1 431 132 133 ILE H H 7.91 0.02 1 432 132 133 ILE CA C 61.0 0.3 1 433 132 133 ILE CB C 37.6 0.3 1 434 132 133 ILE N N 120.6 0.3 1 435 133 134 ARG H H 8.07 0.02 1 436 133 134 ARG CA C 55.0 0.3 1 437 133 134 ARG CB C 31.5 0.3 1 438 133 134 ARG N N 123.1 0.3 1 439 134 135 SER H H 8.21 0.02 1 440 134 135 SER CA C 56.2 0.3 1 441 134 135 SER CB C 62.9 0.3 1 442 134 135 SER N N 117.7 0.3 1 443 135 136 VAL H H 8.05 0.02 1 444 135 136 VAL CA C 61.6 0.3 1 445 135 136 VAL CB C 31.6 0.3 1 446 135 136 VAL N N 121.3 0.3 1 447 136 137 ASP H H 8.17 0.02 1 448 136 137 ASP CA C 53.8 0.3 1 449 136 137 ASP CB C 40.8 0.3 1 450 136 137 ASP N N 123.3 0.3 1 451 137 138 VAL H H 8.04 0.02 1 452 137 138 VAL CA C 62.5 0.3 1 453 137 138 VAL CB C 31.5 0.3 1 454 137 138 VAL N N 120.0 0.3 1 455 138 139 GLY H H 8.33 0.02 1 456 138 139 GLY CA C 45.2 0.3 1 457 138 139 GLY N N 110.4 0.3 1 458 139 140 THR H H 7.85 0.02 1 459 139 140 THR CA C 61.8 0.3 1 460 139 140 THR N N 114.3 0.3 1 461 140 141 TRP H H 8.10 0.02 1 462 140 141 TRP CA C 56.0 0.3 1 463 140 141 TRP CB C 29.7 0.3 1 464 140 141 TRP N N 122.6 0.3 1 465 141 142 ILE H H 7.72 0.02 1 466 141 142 ILE CA C 60.6 0.3 1 467 141 142 ILE CB C 37.7 0.3 1 468 141 142 ILE N N 122.2 0.3 1 469 142 143 ALA H H 7.94 0.02 1 470 142 143 ALA CA C 52.5 0.3 1 471 142 143 ALA CB C 18.3 0.3 1 472 142 143 ALA N N 126.5 0.3 1 473 143 144 GLY H H 8.08 0.02 1 474 143 144 GLY CA C 45.0 0.3 1 475 143 144 GLY N N 107.7 0.3 1 476 144 145 VAL H H 7.75 0.02 1 477 144 145 VAL CA C 62.0 0.3 1 478 144 145 VAL CB C 31.9 0.3 1 479 144 145 VAL N N 118.8 0.3 1 480 145 146 GLY H H 8.20 0.02 1 481 145 146 GLY CA C 44.5 0.3 1 482 145 146 GLY N N 110.9 0.3 1 483 146 147 TYR H H 7.85 0.02 1 484 146 147 TYR CA C 57.4 0.3 1 485 146 147 TYR CB C 38.3 0.3 1 486 146 147 TYR N N 120.1 0.3 1 487 147 148 ARG H H 7.96 0.02 1 488 147 148 ARG CA C 55.3 0.3 1 489 147 148 ARG CB C 30.3 0.3 1 490 147 148 ARG N N 122.9 0.3 1 491 148 149 PHE H H 7.62 0.02 1 492 148 149 PHE CA C 58.8 0.3 1 493 148 149 PHE CB C 39.4 0.3 1 494 148 149 PHE N N 126.1 0.3 1 stop_ save_