data_19407 ####################### # 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 19407 _BMRB_flat_file_name bmr19407.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 'Skp backbone chemical shifts in the apo state' 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" 133 "13C chemical shifts" 257 "15N chemical shifts" 133 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 19408 'Trimeric Skp with bound OmpX' 19409 'Trimeric Skp with bound tOmpA' 19410 'tOmpA within the trimeric chaperone Skp' 19411 'OmpX 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 'trimeric Skp' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'Skp, chain 1' $Escherichia_Coli_Skp 'Skp, chain 2' $Escherichia_Coli_Skp 'Skp, chain 3' $Escherichia_Coli_Skp stop_ _System_molecular_weight 46900 _System_physical_state native _System_oligomer_state ? _System_paramagnetic no _System_thiol_state . _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## 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 . ############################## # Polymer residue sequence # ############################## _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 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 BMRB 19408 Escherichia_Coli_Skp 100.00 234 100.00 100.00 6.42e-171 BMRB 19409 Escherichia_Coli_Skp 69.23 162 100.00 100.00 2.90e-111 BMRB 19730 Escherichia_Coli_Skp 69.23 162 100.00 100.00 2.90e-111 BMRB 19733 Escherichia_Coli_Skp 69.23 162 100.00 100.00 2.90e-111 PDB 1SG2 "Crystal Structure Of The Periplasmic Chaperone Skp" 60.26 153 100.00 100.00 1.37e-91 EMBL CDL25894 "Outer membrane protein H precursor [Escherichia coli ISC7]" 56.84 133 100.00 100.00 2.27e-86 GB ADN44803 "histone-like protein [Escherichia coli ABU 83972]" 56.84 133 100.00 100.00 2.27e-86 GB AFG39053 "Chaperone protein skp precursor [Escherichia coli P12b]" 56.84 133 100.00 100.00 2.27e-86 GB EDZ78162 "chaperone protein Skp [Escherichia coli O157:H7 str. EC4206]" 56.84 133 100.00 100.00 2.27e-86 GB EID69435 "outer membrane chaperone Skp (OmpH) [Escherichia coli W26]" 56.84 133 100.00 100.00 2.27e-86 GB EMV37114 "chaperone protein skp [Escherichia coli BCE002_MS12]" 61.54 161 97.92 98.61 2.47e-92 REF WP_001387023 "chaperone protein skp [Escherichia coli]" 61.54 161 97.92 98.61 2.47e-92 REF WP_024201252 "molecular chaperone [Escherichia coli]" 61.97 148 97.24 97.93 1.17e-92 REF WP_050877050 "molecular chaperone [Escherichia coli]" 61.54 161 97.92 98.61 4.69e-92 REF WP_052985403 "molecular chaperone, partial [Shigella sonnei]" 52.99 124 100.00 100.00 1.92e-79 REF WP_052989315 "molecular chaperone, partial [Shigella sonnei]" 53.42 125 100.00 100.00 4.18e-80 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_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_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 . loop_ _Mol_label _Concentration_value _Concentration_value_units _Concentration_min_value _Concentration_max_value _Isotopic_labeling $Escherichia_Coli_Skp . mM 0.6 1.05 '[U-13C; U-15N; U-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_HNCACB_3 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCACB' _Sample_label $sample_1 save_ save_3D_1H-15N_NOESY_4 _Saveframe_category NMR_applied_experiment _Experiment_name '3D 1H-15N NOESY' _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 HNCACB' '3D 1H-15N NOESY' 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 'Skp, chain 1' _Text_data_format . _Text_data . loop_ _Atom_shift_assign_ID _Residue_author_seq_code _Residue_seq_code _Residue_label _Atom_name _Atom_type _Chem_shift_value _Chem_shift_value_error _Chem_shift_ambiguity_code 1 10 11 SER H H 7.82 0.02 1 2 10 11 SER CA C 61.5 0.3 1 3 10 11 SER N N 113.7 0.3 1 4 24 25 ILE H H 7.70 0.02 1 5 24 25 ILE CA C 60.1 0.3 1 6 24 25 ILE CB C 39.4 0.3 1 7 24 25 ILE N N 115.6 0.3 1 8 25 26 ALA H H 8.73 0.02 1 9 25 26 ALA CA C 49.9 0.3 1 10 25 26 ALA CB C 24.3 0.3 1 11 25 26 ALA N N 125.9 0.3 1 12 26 27 ILE H H 8.84 0.02 1 13 26 27 ILE CA C 58.8 0.3 1 14 26 27 ILE CB C 41.2 0.3 1 15 26 27 ILE N N 115.2 0.3 1 16 27 28 VAL H H 8.19 0.02 1 17 27 28 VAL CA C 58.9 0.3 1 18 27 28 VAL CB C 34.7 0.3 1 19 27 28 VAL N N 118.1 0.3 1 20 28 29 ASN H H 8.87 0.02 1 21 28 29 ASN CA C 51.3 0.3 1 22 28 29 ASN CB C 37.0 0.3 1 23 28 29 ASN N N 128.5 0.3 1 24 29 30 MET H H 7.98 0.02 1 25 29 30 MET CA C 57.2 0.3 1 26 29 30 MET CB C 30.5 0.3 1 27 29 30 MET N N 124.3 0.3 1 28 30 31 GLY H H 9.07 0.02 1 29 30 31 GLY CA C 47.1 0.3 1 30 30 31 GLY N N 108.7 0.3 1 31 31 32 SER H H 7.77 0.02 1 32 31 32 SER CA C 60.3 0.3 1 33 31 32 SER CB C 62.9 0.3 1 34 31 32 SER N N 117.4 0.3 1 35 32 33 LEU H H 8.03 0.02 1 36 32 33 LEU CA C 58.1 0.3 1 37 32 33 LEU CB C 41.4 0.3 1 38 32 33 LEU N N 121.3 0.3 1 39 33 34 PHE H H 8.60 0.02 1 40 33 34 PHE CA C 62.7 0.3 1 41 33 34 PHE CB C 38.2 0.3 1 42 33 34 PHE N N 118.3 0.3 1 43 34 35 GLN H H 7.63 0.02 1 44 34 35 GLN CA C 58.8 0.3 1 45 34 35 GLN CB C 27.9 0.3 1 46 34 35 GLN N N 117.0 0.3 1 47 35 36 GLN H H 8.44 0.02 1 48 35 36 GLN CA C 59.1 0.3 1 49 35 36 GLN CB C 29.0 0.3 1 50 35 36 GLN N N 118.0 0.3 1 51 36 37 VAL H H 8.98 0.02 1 52 36 37 VAL CA C 66.4 0.3 1 53 36 37 VAL CB C 30.6 0.3 1 54 36 37 VAL N N 120.8 0.3 1 55 37 38 ALA H H 8.59 0.02 1 56 37 38 ALA CA C 55.6 0.3 1 57 37 38 ALA CB C 17.2 0.3 1 58 37 38 ALA N N 122.2 0.3 1 59 38 39 GLN H H 7.64 0.02 1 60 38 39 GLN CA C 58.6 0.3 1 61 38 39 GLN CB C 27.9 0.3 1 62 38 39 GLN N N 117.6 0.3 1 63 39 40 LYS H H 8.15 0.02 1 64 39 40 LYS CA C 58.9 0.3 1 65 39 40 LYS CB C 32.5 0.3 1 66 39 40 LYS N N 120.8 0.3 1 67 40 41 THR H H 8.01 0.02 1 68 40 41 THR CA C 62.6 0.3 1 69 40 41 THR CB C 70.2 0.3 1 70 40 41 THR N N 107.8 0.3 1 71 41 42 GLY H H 7.63 0.02 1 72 41 42 GLY CA C 46.3 0.3 1 73 41 42 GLY N N 110.3 0.3 1 74 42 43 VAL H H 7.59 0.02 1 75 42 43 VAL CA C 65.5 0.3 1 76 42 43 VAL CB C 31.4 0.3 1 77 42 43 VAL N N 121.0 0.3 1 78 45 46 THR H H 8.29 0.02 1 79 45 46 THR CA C 66.3 0.3 1 80 45 46 THR CB C 68.3 0.3 1 81 45 46 THR N N 118.4 0.3 1 82 46 47 LEU H H 8.00 0.02 1 83 46 47 LEU CA C 57.4 0.3 1 84 46 47 LEU CB C 40.8 0.3 1 85 46 47 LEU N N 122.5 0.3 1 86 47 48 GLU H H 8.20 0.02 1 87 47 48 GLU CA C 59.5 0.3 1 88 47 48 GLU CB C 27.7 0.3 1 89 47 48 GLU N N 119.8 0.3 1 90 48 49 ASN H H 8.19 0.02 1 91 48 49 ASN CA C 56.3 0.3 1 92 48 49 ASN CB C 38.1 0.3 1 93 48 49 ASN N N 117.2 0.3 1 94 49 50 GLU H H 8.50 0.02 1 95 49 50 GLU CA C 59.1 0.3 1 96 49 50 GLU CB C 29.1 0.3 1 97 49 50 GLU N N 123.0 0.3 1 98 50 51 PHE H H 7.72 0.02 1 99 50 51 PHE CA C 58.0 0.3 1 100 50 51 PHE CB C 40.7 0.3 1 101 50 51 PHE N N 120.3 0.3 1 102 51 52 LYS H H 8.13 0.02 1 103 51 52 LYS CA C 59.4 0.3 1 104 51 52 LYS CB C 28.9 0.3 1 105 51 52 LYS N N 120.0 0.3 1 106 52 53 GLY H H 8.08 0.02 1 107 52 53 GLY CA C 47.0 0.3 1 108 52 53 GLY N N 106.0 0.3 1 109 53 54 ARG H H 8.20 0.02 1 110 53 54 ARG CA C 58.6 0.3 1 111 53 54 ARG CB C 30.8 0.3 1 112 53 54 ARG N N 123.9 0.3 1 113 54 55 ALA H H 8.87 0.02 1 114 54 55 ALA CA C 54.9 0.3 1 115 54 55 ALA CB C 17.5 0.3 1 116 54 55 ALA N N 123.8 0.3 1 117 55 56 SER H H 8.35 0.02 1 118 55 56 SER CA C 61.5 0.3 1 119 55 56 SER CB C 63.5 0.3 1 120 55 56 SER N N 115.7 0.3 1 121 56 57 GLU H H 7.80 0.02 1 122 56 57 GLU CA C 59.1 0.3 1 123 56 57 GLU CB C 28.9 0.3 1 124 56 57 GLU N N 123.5 0.3 1 125 57 58 LEU H H 7.95 0.02 1 126 57 58 LEU CA C 59.6 0.3 1 127 57 58 LEU CB C 41.6 0.3 1 128 57 58 LEU N N 122.3 0.3 1 129 58 59 GLN H H 8.21 0.02 1 130 58 59 GLN CA C 58.8 0.3 1 131 58 59 GLN CB C 27.9 0.3 1 132 58 59 GLN N N 119.3 0.3 1 133 59 60 ARG H H 7.82 0.02 1 134 59 60 ARG CA C 59.4 0.3 1 135 59 60 ARG CB C 28.3 0.3 1 136 59 60 ARG N N 123.2 0.3 1 137 61 62 GLU H H 8.38 0.02 1 138 61 62 GLU CA C 59.7 0.3 1 139 61 62 GLU CB C 28.7 0.3 1 140 61 62 GLU N N 121.7 0.3 1 141 62 63 THR H H 8.15 0.02 1 142 62 63 THR CA C 66.5 0.3 1 143 62 63 THR CB C 68.7 0.3 1 144 62 63 THR N N 116.1 0.3 1 145 63 64 ASP H H 8.04 0.02 1 146 63 64 ASP CA C 57.5 0.3 1 147 63 64 ASP CB C 41.2 0.3 1 148 63 64 ASP N N 124.2 0.3 1 149 64 65 LEU H H 8.58 0.02 1 150 64 65 LEU CA C 57.3 0.3 1 151 64 65 LEU CB C 39.9 0.3 1 152 64 65 LEU N N 122.5 0.3 1 153 65 66 GLN H H 8.42 0.02 1 154 65 66 GLN CA C 59.8 0.3 1 155 65 66 GLN CB C 28.9 0.3 1 156 65 66 GLN N N 121.5 0.3 1 157 66 67 ALA H H 9.07 0.02 1 158 66 67 ALA CA C 55.1 0.3 1 159 66 67 ALA CB C 16.8 0.3 1 160 66 67 ALA N N 125.3 0.3 1 161 67 68 LYS H H 8.37 0.02 1 162 67 68 LYS CA C 56.4 0.3 1 163 67 68 LYS N N 125.2 0.3 1 164 68 69 MET H H 8.11 0.02 1 165 68 69 MET CA C 59.8 0.3 1 166 68 69 MET CB C 32.3 0.3 1 167 68 69 MET N N 120.9 0.3 1 168 69 70 LYS H H 8.48 0.02 1 169 69 70 LYS CA C 58.5 0.3 1 170 69 70 LYS CB C 31.1 0.3 1 171 69 70 LYS N N 118.5 0.3 1 172 70 71 LYS H H 7.87 0.02 1 173 70 71 LYS CA C 59.0 0.3 1 174 70 71 LYS CB C 31.2 0.3 1 175 70 71 LYS N N 120.4 0.3 1 176 71 72 LEU H H 8.26 0.02 1 177 71 72 LEU CA C 58.0 0.3 1 178 71 72 LEU CB C 41.7 0.3 1 179 71 72 LEU N N 120.4 0.3 1 180 72 73 GLN H H 7.64 0.02 1 181 72 73 GLN CA C 57.9 0.3 1 182 72 73 GLN CB C 27.9 0.3 1 183 72 73 GLN N N 115.4 0.3 1 184 73 74 SER H H 7.45 0.02 1 185 73 74 SER CA C 58.1 0.3 1 186 73 74 SER CB C 64.2 0.3 1 187 73 74 SER N N 111.8 0.3 1 188 74 75 MET H H 7.43 0.02 1 189 74 75 MET CA C 56.2 0.3 1 190 74 75 MET CB C 34.2 0.3 1 191 74 75 MET N N 122.9 0.3 1 192 75 76 LYS H H 8.49 0.02 1 193 75 76 LYS CA C 55.6 0.3 1 194 75 76 LYS CB C 32.3 0.3 1 195 75 76 LYS N N 124.7 0.3 1 196 76 77 ALA H H 8.25 0.02 1 197 76 77 ALA CA C 53.1 0.3 1 198 76 77 ALA CB C 18.3 0.3 1 199 76 77 ALA N N 123.5 0.3 1 200 77 78 GLY H H 8.33 0.02 1 201 77 78 GLY CA C 44.4 0.3 1 202 77 78 GLY N N 109.6 0.3 1 203 80 81 ARG H H 7.84 0.02 1 204 80 81 ARG CA C 59.7 0.3 1 205 80 81 ARG CB C 29.6 0.3 1 206 80 81 ARG N N 121.2 0.3 1 207 81 82 THR H H 7.99 0.02 1 208 81 82 THR CA C 66.7 0.3 1 209 81 82 THR CB C 68.4 0.3 1 210 81 82 THR N N 115.8 0.3 1 211 82 83 LYS H H 8.31 0.02 1 212 82 83 LYS CA C 59.5 0.3 1 213 82 83 LYS CB C 31.8 0.3 1 214 82 83 LYS N N 121.3 0.3 1 215 83 84 LEU H H 7.79 0.02 1 216 83 84 LEU CA C 57.7 0.3 1 217 83 84 LEU CB C 41.2 0.3 1 218 83 84 LEU N N 120.5 0.3 1 219 84 85 GLU H H 7.90 0.02 1 220 84 85 GLU CA C 58.7 0.3 1 221 84 85 GLU CB C 27.7 0.3 1 222 84 85 GLU N N 119.4 0.3 1 223 85 86 LYS H H 7.66 0.02 1 224 85 86 LYS CA C 59.1 0.3 1 225 85 86 LYS CB C 31.3 0.3 1 226 85 86 LYS N N 121.3 0.3 1 227 86 87 ASP H H 8.17 0.02 1 228 86 87 ASP CA C 57.8 0.3 1 229 86 87 ASP CB C 40.8 0.3 1 230 86 87 ASP N N 122.3 0.3 1 231 87 88 VAL H H 8.85 0.02 1 232 87 88 VAL CA C 66.9 0.3 1 233 87 88 VAL CB C 30.6 0.3 1 234 87 88 VAL N N 120.7 0.3 1 235 88 89 MET H H 8.19 0.02 1 236 88 89 MET CA C 58.7 0.3 1 237 88 89 MET CB C 30.9 0.3 1 238 88 89 MET N N 119.4 0.3 1 239 89 90 ALA H H 7.82 0.02 1 240 89 90 ALA CA C 54.8 0.3 1 241 89 90 ALA CB C 17.3 0.3 1 242 89 90 ALA N N 122.8 0.3 1 243 90 91 GLN H H 7.83 0.02 1 244 90 91 GLN CA C 58.8 0.3 1 245 90 91 GLN CB C 27.6 0.3 1 246 90 91 GLN N N 117.8 0.3 1 247 91 92 ARG H H 8.07 0.02 1 248 91 92 ARG CA C 59.4 0.3 1 249 91 92 ARG CB C 29.0 0.3 1 250 91 92 ARG N N 121.0 0.3 1 251 92 93 GLN H H 7.71 0.02 1 252 92 93 GLN CA C 59.1 0.3 1 253 92 93 GLN CB C 27.5 0.3 1 254 92 93 GLN N N 120.2 0.3 1 255 93 94 THR H H 8.20 0.02 1 256 93 94 THR CA C 66.6 0.3 1 257 93 94 THR CB C 68.4 0.3 1 258 93 94 THR N N 118.3 0.3 1 259 94 95 PHE H H 8.74 0.02 1 260 94 95 PHE CA C 61.5 0.3 1 261 94 95 PHE CB C 38.7 0.3 1 262 94 95 PHE N N 123.1 0.3 1 263 95 96 ALA H H 8.22 0.02 1 264 95 96 ALA CA C 55.0 0.3 1 265 95 96 ALA CB C 17.3 0.3 1 266 95 96 ALA N N 120.9 0.3 1 267 96 97 GLN H H 8.61 0.02 1 268 96 97 GLN CA C 58.9 0.3 1 269 96 97 GLN CB C 27.7 0.3 1 270 96 97 GLN N N 120.7 0.3 1 271 97 98 LYS H H 9.07 0.02 1 272 97 98 LYS CA C 60.0 0.3 1 273 97 98 LYS CB C 29.4 0.3 1 274 97 98 LYS N N 121.5 0.3 1 275 98 99 ALA H H 7.81 0.02 1 276 98 99 ALA CA C 54.8 0.3 1 277 98 99 ALA CB C 17.5 0.3 1 278 98 99 ALA N N 122.5 0.3 1 279 99 100 GLN H H 8.00 0.02 1 280 99 100 GLN CA C 59.6 0.3 1 281 99 100 GLN CB C 29.2 0.3 1 282 99 100 GLN N N 120.2 0.3 1 283 100 101 ALA H H 7.87 0.02 1 284 100 101 ALA CA C 55.0 0.3 1 285 100 101 ALA CB C 17.3 0.3 1 286 100 101 ALA N N 122.8 0.3 1 287 101 102 PHE H H 8.00 0.02 1 288 101 102 PHE CA C 61.3 0.3 1 289 101 102 PHE CB C 39.1 0.3 1 290 101 102 PHE N N 119.1 0.3 1 291 102 103 GLU H H 7.99 0.02 1 292 102 103 GLU CA C 59.1 0.3 1 293 102 103 GLU CB C 27.6 0.3 1 294 102 103 GLU N N 119.9 0.3 1 295 103 104 GLN H H 7.80 0.02 1 296 103 104 GLN CA C 59.6 0.3 1 297 103 104 GLN CB C 31.6 0.3 1 298 103 104 GLN N N 119.2 0.3 1 299 104 105 ASP H H 7.71 0.02 1 300 104 105 ASP CA C 57.3 0.3 1 301 104 105 ASP CB C 40.3 0.3 1 302 104 105 ASP N N 121.5 0.3 1 303 105 106 ARG H H 8.95 0.02 1 304 105 106 ARG CA C 59.8 0.3 1 305 105 106 ARG CB C 29.1 0.3 1 306 105 106 ARG N N 120.4 0.3 1 307 106 107 ALA H H 7.87 0.02 1 308 106 107 ALA CA C 54.9 0.3 1 309 106 107 ALA CB C 17.5 0.3 1 310 106 107 ALA N N 122.1 0.3 1 311 108 109 ARG H H 8.49 0.02 1 312 108 109 ARG CA C 57.1 0.3 1 313 108 109 ARG CB C 26.7 0.3 1 314 108 109 ARG N N 119.4 0.3 1 315 109 110 SER H H 8.40 0.02 1 316 109 110 SER CA C 62.2 0.3 1 317 109 110 SER CB C 65.6 0.3 1 318 109 110 SER N N 115.2 0.3 1 319 110 111 ASN H H 8.13 0.02 1 320 110 111 ASN CA C 55.7 0.3 1 321 110 111 ASN CB C 39.1 0.3 1 322 110 111 ASN N N 118.7 0.3 1 323 111 112 GLU H H 8.03 0.02 1 324 111 112 GLU CA C 58.8 0.3 1 325 111 112 GLU CB C 28.6 0.3 1 326 111 112 GLU N N 118.7 0.3 1 327 112 113 GLU H H 8.47 0.02 1 328 112 113 GLU CA C 58.6 0.3 1 329 112 113 GLU CB C 28.3 0.3 1 330 112 113 GLU N N 118.2 0.3 1 331 113 114 ARG H H 7.60 0.02 1 332 113 114 ARG CA C 58.9 0.3 1 333 113 114 ARG CB C 31.7 0.3 1 334 113 114 ARG N N 121.3 0.3 1 335 114 115 GLY H H 8.49 0.02 1 336 114 115 GLY N N 110.8 0.3 1 337 115 116 LYS H H 7.83 0.02 1 338 115 116 LYS CA C 55.4 0.3 1 339 115 116 LYS N N 115.0 0.3 1 340 116 117 LEU H H 8.19 0.02 1 341 116 117 LEU CA C 57.0 0.3 1 342 116 117 LEU CB C 40.9 0.3 1 343 116 117 LEU N N 121.4 0.3 1 344 117 118 VAL H H 8.23 0.02 1 345 117 118 VAL CA C 59.7 0.3 1 346 117 118 VAL CB C 29.2 0.3 1 347 117 118 VAL N N 124.7 0.3 1 348 118 119 THR H H 8.33 0.02 1 349 118 119 THR CA C 66.7 0.3 1 350 118 119 THR CB C 68.7 0.3 1 351 118 119 THR N N 116.8 0.3 1 352 119 120 ARG H H 7.81 0.02 1 353 119 120 ARG CA C 59.7 0.3 1 354 119 120 ARG CB C 31.9 0.3 1 355 119 120 ARG N N 121.2 0.3 1 356 120 121 ILE H H 8.36 0.02 1 357 120 121 ILE CA C 65.9 0.3 1 358 120 121 ILE CB C 37.2 0.3 1 359 120 121 ILE N N 121.3 0.3 1 360 121 122 GLN H H 8.96 0.02 1 361 121 122 GLN CA C 59.8 0.3 1 362 121 122 GLN CB C 27.6 0.3 1 363 121 122 GLN N N 120.5 0.3 1 364 122 123 THR H H 8.27 0.02 1 365 122 123 THR CA C 66.7 0.3 1 366 122 123 THR CB C 68.7 0.3 1 367 122 123 THR N N 116.5 0.3 1 368 123 124 ALA H H 7.39 0.02 1 369 123 124 ALA CA C 55.0 0.3 1 370 123 124 ALA CB C 19.4 0.3 1 371 123 124 ALA N N 126.2 0.3 1 372 124 125 VAL H H 8.60 0.02 1 373 124 125 VAL CA C 66.6 0.3 1 374 124 125 VAL CB C 30.4 0.3 1 375 124 125 VAL N N 119.2 0.3 1 376 125 126 LYS H H 7.67 0.02 1 377 125 126 LYS CA C 59.1 0.3 1 378 125 126 LYS CB C 33.5 0.3 1 379 125 126 LYS N N 118.9 0.3 1 380 126 127 SER H H 7.68 0.02 1 381 126 127 SER CA C 59.1 0.3 1 382 126 127 SER CB C 61.1 0.3 1 383 126 127 SER N N 119.2 0.3 1 384 127 128 VAL H H 7.94 0.02 1 385 127 128 VAL CA C 66.1 0.3 1 386 127 128 VAL CB C 31.9 0.3 1 387 127 128 VAL N N 122.2 0.3 1 388 128 129 ALA H H 8.58 0.02 1 389 128 129 ALA CA C 55.5 0.3 1 390 128 129 ALA CB C 17.1 0.3 1 391 128 129 ALA N N 122.1 0.3 1 392 129 130 ASN H H 8.52 0.02 1 393 129 130 ASN CA C 55.7 0.3 1 394 129 130 ASN CB C 38.6 0.3 1 395 129 130 ASN N N 115.0 0.3 1 396 130 131 SER H H 7.85 0.02 1 397 130 131 SER CA C 61.3 0.3 1 398 130 131 SER CB C 63.6 0.3 1 399 130 131 SER N N 115.6 0.3 1 400 131 132 GLN H H 7.54 0.02 1 401 131 132 GLN CA C 55.3 0.3 1 402 131 132 GLN CB C 28.7 0.3 1 403 131 132 GLN N N 118.5 0.3 1 404 132 133 ASP H H 7.79 0.02 1 405 132 133 ASP CA C 55.5 0.3 1 406 132 133 ASP CB C 39.4 0.3 1 407 132 133 ASP N N 119.7 0.3 1 408 133 134 ILE H H 8.20 0.02 1 409 133 134 ILE CA C 61.2 0.3 1 410 133 134 ILE CB C 39.4 0.3 1 411 133 134 ILE N N 118.4 0.3 1 412 134 135 ASP H H 8.32 0.02 1 413 134 135 ASP CA C 55.6 0.3 1 414 134 135 ASP CB C 41.9 0.3 1 415 134 135 ASP N N 125.0 0.3 1 416 135 136 LEU H H 7.63 0.02 1 417 135 136 LEU CA C 53.8 0.3 1 418 135 136 LEU CB C 45.8 0.3 1 419 135 136 LEU N N 120.3 0.3 1 420 136 137 VAL H H 9.02 0.02 1 421 136 137 VAL CA C 59.6 0.3 1 422 136 137 VAL CB C 32.0 0.3 1 423 136 137 VAL N N 125.3 0.3 1 424 137 138 VAL H H 9.10 0.02 1 425 137 138 VAL CA C 60.3 0.3 1 426 137 138 VAL CB C 33.6 0.3 1 427 137 138 VAL N N 127.5 0.3 1 428 138 139 ASP H H 8.63 0.02 1 429 138 139 ASP CA C 54.2 0.3 1 430 138 139 ASP CB C 42.1 0.3 1 431 138 139 ASP N N 125.1 0.3 1 432 139 140 ALA H H 8.83 0.02 1 433 139 140 ALA CA C 54.5 0.3 1 434 139 140 ALA CB C 18.2 0.3 1 435 139 140 ALA N N 129.4 0.3 1 436 140 141 ASN H H 8.82 0.02 1 437 140 141 ASN CA C 55.6 0.3 1 438 140 141 ASN CB C 38.1 0.3 1 439 140 141 ASN N N 116.3 0.3 1 440 141 142 ALA H H 8.19 0.02 1 441 141 142 ALA CA C 51.8 0.3 1 442 141 142 ALA CB C 18.9 0.3 1 443 141 142 ALA N N 120.8 0.3 1 444 142 143 VAL H H 7.52 0.02 1 445 142 143 VAL CA C 62.3 0.3 1 446 142 143 VAL CB C 32.6 0.3 1 447 142 143 VAL N N 119.6 0.3 1 448 143 144 ALA H H 8.70 0.02 1 449 143 144 ALA CA C 52.2 0.3 1 450 143 144 ALA CB C 20.5 0.3 1 451 143 144 ALA N N 129.6 0.3 1 452 144 145 TYR H H 7.64 0.02 1 453 144 145 TYR CA C 58.8 0.3 1 454 144 145 TYR CB C 41.4 0.3 1 455 144 145 TYR N N 116.9 0.3 1 456 145 146 ASN H H 6.87 0.02 1 457 145 146 ASN CA C 51.8 0.3 1 458 145 146 ASN CB C 40.8 0.3 1 459 145 146 ASN N N 123.5 0.3 1 460 146 147 SER H H 8.88 0.02 1 461 146 147 SER CA C 56.8 0.3 1 462 146 147 SER CB C 64.9 0.3 1 463 146 147 SER N N 119.2 0.3 1 464 147 148 SER H H 8.64 0.02 1 465 147 148 SER CA C 60.0 0.3 1 466 147 148 SER CB C 62.9 0.3 1 467 147 148 SER N N 114.2 0.3 1 468 148 149 ASP H H 7.71 0.02 1 469 148 149 ASP CA C 55.4 0.3 1 470 148 149 ASP CB C 39.2 0.3 1 471 148 149 ASP N N 119.7 0.3 1 472 149 150 VAL H H 7.38 0.02 1 473 149 150 VAL CA C 61.7 0.3 1 474 149 150 VAL CB C 31.2 0.3 1 475 149 150 VAL N N 122.3 0.3 1 476 150 151 LYS H H 9.06 0.02 1 477 150 151 LYS CA C 56.9 0.3 1 478 150 151 LYS CB C 32.7 0.3 1 479 150 151 LYS N N 128.0 0.3 1 480 151 152 ASP H H 8.20 0.02 1 481 151 152 ASP CA C 52.2 0.3 1 482 151 152 ASP CB C 40.9 0.3 1 483 151 152 ASP N N 121.4 0.3 1 484 152 153 ILE H H 8.66 0.02 1 485 152 153 ILE CA C 61.6 0.3 1 486 152 153 ILE CB C 37.3 0.3 1 487 152 153 ILE N N 118.3 0.3 1 488 153 154 THR H H 8.86 0.02 1 489 153 154 THR CA C 69.6 0.3 1 490 153 154 THR CB C 71.8 0.3 1 491 153 154 THR N N 121.5 0.3 1 492 154 155 ALA H H 8.70 0.02 1 493 154 155 ALA CA C 55.2 0.3 1 494 154 155 ALA CB C 17.3 0.3 1 495 154 155 ALA N N 121.8 0.3 1 496 155 156 ASP H H 7.70 0.02 1 497 155 156 ASP CA C 57.1 0.3 1 498 155 156 ASP CB C 40.7 0.3 1 499 155 156 ASP N N 118.9 0.3 1 500 156 157 VAL H H 8.38 0.02 1 501 156 157 VAL CA C 66.4 0.3 1 502 156 157 VAL CB C 30.2 0.3 1 503 156 157 VAL N N 120.6 0.3 1 504 157 158 LEU H H 8.07 0.02 1 505 157 158 LEU CA C 58.0 0.3 1 506 157 158 LEU CB C 40.7 0.3 1 507 157 158 LEU N N 120.1 0.3 1 508 158 159 LYS H H 7.21 0.02 1 509 158 159 LYS CA C 58.3 0.3 1 510 158 159 LYS CB C 32.1 0.3 1 511 158 159 LYS N N 115.4 0.3 1 512 159 160 GLN H H 7.48 0.02 1 513 159 160 GLN CA C 55.2 0.3 1 514 159 160 GLN CB C 28.6 0.3 1 515 159 160 GLN N N 115.8 0.3 1 516 160 161 VAL H H 7.33 0.02 1 517 160 161 VAL CA C 63.8 0.3 1 518 160 161 VAL CB C 30.8 0.3 1 519 160 161 VAL N N 121.2 0.3 1 520 161 162 LYS H H 7.87 0.02 1 521 161 162 LYS CA C 57.1 0.3 1 522 161 162 LYS CB C 33.4 0.3 1 523 161 162 LYS N N 132.6 0.3 1 stop_ save_