data_19408 ####################### # 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 19408 _BMRB_flat_file_name bmr19408.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 when bound to its substrate OmpX' 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" 149 "13C chemical shifts" 283 "15N chemical shifts" 149 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 'Trimeric Skp' 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 with bound OmpX' _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 OmpX $Escherichia_Coli_OmpX stop_ _System_molecular_weight 64100 _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 19407 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_ 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 . _Residue_count 150 _Mol_residue_sequence ; MATSTVTGGYAQSDMQGVMN KTNGFNLKYRYEQDNNPLGV IGSFTYTEKDRTENGSYNKG QYYGITAGPAYRLNDWASIY GVVGVGYGKFQQTENQGLNR TASNSDYGFSYGAGMQFNPI ENVALDFSYEQSRIRNVDVG TWIAGVGYRF ; 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 ASP 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 GLU 54 53 ASN 55 54 GLY 56 55 SER 57 56 TYR 58 57 ASN 59 58 LYS 60 59 GLY 61 60 GLN 62 61 TYR 63 62 TYR 64 63 GLY 65 64 ILE 66 65 THR 67 66 ALA 68 67 GLY 69 68 PRO 70 69 ALA 71 70 TYR 72 71 ARG 73 72 LEU 74 73 ASN 75 74 ASP 76 75 TRP 77 76 ALA 78 77 SER 79 78 ILE 80 79 TYR 81 80 GLY 82 81 VAL 83 82 VAL 84 83 GLY 85 84 VAL 86 85 GLY 87 86 TYR 88 87 GLY 89 88 LYS 90 89 PHE 91 90 GLN 92 91 GLN 93 92 THR 94 93 GLU 95 94 ASN 96 95 GLN 97 96 GLY 98 97 LEU 99 98 ASN 100 99 ARG 101 100 THR 102 101 ALA 103 102 SER 104 103 ASN 105 104 SER 106 105 ASP 107 106 TYR 108 107 GLY 109 108 PHE 110 109 SER 111 110 TYR 112 111 GLY 113 112 ALA 114 113 GLY 115 114 MET 116 115 GLN 117 116 PHE 118 117 ASN 119 118 PRO 120 119 ILE 121 120 GLU 122 121 ASN 123 122 VAL 124 123 ALA 125 124 LEU 126 125 ASP 127 126 PHE 128 127 SER 129 128 TYR 130 129 GLU 131 130 GLN 132 131 SER 133 132 ARG 134 133 ILE 135 134 ARG 136 135 ASN 137 136 VAL 138 137 ASP 139 138 VAL 140 139 GLY 141 140 THR 142 141 TRP 143 142 ILE 144 143 ALA 145 144 GLY 146 145 VAL 147 146 GLY 148 147 TYR 149 148 ARG 150 149 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 P25253 . . . . . . 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 $Escherichia_Coli_OmpX '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 $Escherichia_Coli_OmpX 'recombinant technology' . Escherichia coli 'BL21 (DE3)' pET28B-OmpX 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 0.2 0.35 '[U-100% 2H]' $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_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_ save_3D_1H-15N_NOESY_5 _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 HNCO' '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 1 2 GLY H H 8.29 0.02 1 2 1 2 GLY CA C 44.9 0.3 1 3 1 2 GLY N N 110.8 0.3 1 4 3 4 SER H H 7.94 0.02 1 5 3 4 SER CA C 58.8 0.3 1 6 3 4 SER CB C 62.3 0.3 1 7 3 4 SER N N 119.0 0.3 1 8 10 11 SER H H 7.75 0.02 1 9 10 11 SER CA C 61.2 0.3 1 10 10 11 SER CB C 62.6 0.3 1 11 10 11 SER N N 113.6 0.3 1 12 12 13 GLY H H 8.19 0.02 1 13 12 13 GLY CA C 45.2 0.3 1 14 12 13 GLY N N 114.7 0.3 1 15 13 14 LEU H H 7.96 0.02 1 16 13 14 LEU CA C 55.0 0.3 1 17 13 14 LEU CB C 41.7 0.3 1 18 13 14 LEU N N 122.0 0.3 1 19 14 15 VAL H H 8.00 0.02 1 20 14 15 VAL CA C 59.6 0.3 1 21 14 15 VAL CB C 32.0 0.3 1 22 14 15 VAL N N 122.5 0.3 1 23 16 17 ARG H H 8.37 0.02 1 24 16 17 ARG CA C 56.2 0.3 1 25 16 17 ARG CB C 30.2 0.3 1 26 16 17 ARG N N 122.2 0.3 1 27 17 18 GLY H H 8.48 0.02 1 28 17 18 GLY CA C 45.0 0.3 1 29 17 18 GLY N N 110.8 0.3 1 30 18 19 SER H H 8.13 0.02 1 31 18 19 SER CA C 58.1 0.3 1 32 18 19 SER CB C 63.8 0.3 1 33 18 19 SER N N 115.7 0.3 1 34 19 20 HIS H H 8.51 0.02 1 35 19 20 HIS CA C 58.4 0.3 1 36 19 20 HIS CB C 28.2 0.3 1 37 19 20 HIS N N 118.1 0.3 1 38 21 22 ALA H H 8.25 0.02 1 39 21 22 ALA CA C 55.0 0.3 1 40 21 22 ALA CB C 17.4 0.3 1 41 21 22 ALA N N 120.8 0.3 1 42 22 23 ASP H H 8.15 0.02 1 43 22 23 ASP CA C 58.1 0.3 1 44 22 23 ASP CB C 41.3 0.3 1 45 22 23 ASP N N 120.8 0.3 1 46 23 24 LYS H H 8.09 0.02 1 47 23 24 LYS CA C 58.9 0.3 1 48 23 24 LYS CB C 29.7 0.3 1 49 23 24 LYS N N 121.0 0.3 1 50 24 25 ILE H H 8.54 0.02 1 51 24 25 ILE CA C 59.3 0.3 1 52 24 25 ILE N N 122.7 0.3 1 53 25 26 ALA H H 8.76 0.02 1 54 25 26 ALA CA C 50.1 0.3 1 55 25 26 ALA CB C 24.3 0.3 1 56 25 26 ALA N N 126.2 0.3 1 57 26 27 ILE H H 8.84 0.02 1 58 26 27 ILE CA C 58.9 0.3 1 59 26 27 ILE CB C 41.6 0.3 1 60 26 27 ILE N N 115.0 0.3 1 61 27 28 VAL H H 8.17 0.02 1 62 27 28 VAL CA C 59.0 0.3 1 63 27 28 VAL CB C 34.9 0.3 1 64 27 28 VAL N N 117.8 0.3 1 65 28 29 ASN H H 8.86 0.02 1 66 28 29 ASN CA C 51.5 0.3 1 67 28 29 ASN CB C 36.8 0.3 1 68 28 29 ASN N N 128.6 0.3 1 69 29 30 MET H H 7.99 0.02 1 70 29 30 MET CA C 57.1 0.3 1 71 29 30 MET CB C 30.5 0.3 1 72 29 30 MET N N 124.3 0.3 1 73 30 31 GLY H H 9.03 0.02 1 74 30 31 GLY CA C 47.3 0.3 1 75 30 31 GLY N N 108.4 0.3 1 76 31 32 SER H H 7.73 0.02 1 77 31 32 SER CA C 60.3 0.3 1 78 31 32 SER CB C 62.8 0.3 1 79 31 32 SER N N 117.1 0.3 1 80 32 33 LEU H H 8.01 0.02 1 81 32 33 LEU CA C 58.1 0.3 1 82 32 33 LEU CB C 41.7 0.3 1 83 32 33 LEU N N 121.1 0.3 1 84 33 34 PHE H H 8.66 0.02 1 85 33 34 PHE CA C 62.6 0.3 1 86 33 34 PHE CB C 37.1 0.3 1 87 33 34 PHE N N 118.8 0.3 1 88 34 35 GLN H H 7.72 0.02 1 89 34 35 GLN CA C 59.3 0.3 1 90 34 35 GLN CB C 28.2 0.3 1 91 34 35 GLN N N 116.6 0.3 1 92 35 36 GLN H H 8.40 0.02 1 93 35 36 GLN CB C 29.1 0.3 1 94 35 36 GLN N N 117.9 0.3 1 95 36 37 VAL H H 8.95 0.02 1 96 36 37 VAL CA C 66.3 0.3 1 97 36 37 VAL CB C 30.7 0.3 1 98 36 37 VAL N N 120.9 0.3 1 99 37 38 ALA H H 8.64 0.02 1 100 37 38 ALA CA C 55.6 0.3 1 101 37 38 ALA CB C 17.2 0.3 1 102 37 38 ALA N N 122.2 0.3 1 103 38 39 GLN H H 7.74 0.02 1 104 38 39 GLN CA C 58.7 0.3 1 105 38 39 GLN CB C 27.9 0.3 1 106 38 39 GLN N N 117.7 0.3 1 107 39 40 LYS H H 8.19 0.02 1 108 39 40 LYS CA C 58.9 0.3 1 109 39 40 LYS CB C 32.2 0.3 1 110 39 40 LYS N N 120.8 0.3 1 111 40 41 THR H H 8.00 0.02 1 112 40 41 THR CA C 62.7 0.3 1 113 40 41 THR CB C 70.2 0.3 1 114 40 41 THR N N 107.4 0.3 1 115 41 42 GLY H H 7.60 0.02 1 116 41 42 GLY CA C 46.2 0.3 1 117 41 42 GLY N N 110.4 0.3 1 118 42 43 VAL H H 7.43 0.02 1 119 42 43 VAL CA C 65.9 0.3 1 120 42 43 VAL CB C 31.1 0.3 1 121 42 43 VAL N N 120.5 0.3 1 122 43 44 SER H H 8.48 0.02 1 123 43 44 SER CA C 61.9 0.3 1 124 43 44 SER N N 115.4 0.3 1 125 44 45 ASN H H 7.76 0.02 1 126 44 45 ASN CA C 56.1 0.3 1 127 44 45 ASN CB C 38.2 0.3 1 128 44 45 ASN N N 120.4 0.3 1 129 45 46 THR H H 8.28 0.02 1 130 45 46 THR CA C 66.7 0.3 1 131 45 46 THR CB C 68.4 0.3 1 132 45 46 THR N N 118.5 0.3 1 133 46 47 LEU H H 8.10 0.02 1 134 46 47 LEU CA C 57.9 0.3 1 135 46 47 LEU CB C 40.9 0.3 1 136 46 47 LEU N N 122.3 0.3 1 137 47 48 GLU H H 8.13 0.02 1 138 47 48 GLU CA C 59.4 0.3 1 139 47 48 GLU CB C 27.8 0.3 1 140 47 48 GLU N N 119.8 0.3 1 141 48 49 ASN H H 8.19 0.02 1 142 48 49 ASN CA C 56.2 0.3 1 143 48 49 ASN CB C 38.1 0.3 1 144 48 49 ASN N N 117.0 0.3 1 145 49 50 GLU H H 8.52 0.02 1 146 49 50 GLU CA C 59.1 0.3 1 147 49 50 GLU CB C 29.2 0.3 1 148 49 50 GLU N N 122.7 0.3 1 149 50 51 PHE H H 7.65 0.02 1 150 50 51 PHE CA C 58.1 0.3 1 151 50 51 PHE CB C 40.4 0.3 1 152 50 51 PHE N N 120.5 0.3 1 153 51 52 LYS H H 8.21 0.02 1 154 51 52 LYS CA C 60.2 0.3 1 155 51 52 LYS CB C 33.6 0.3 1 156 51 52 LYS N N 120.1 0.3 1 157 52 53 GLY H H 8.16 0.02 1 158 52 53 GLY CA C 47.2 0.3 1 159 52 53 GLY N N 105.9 0.3 1 160 53 54 ARG H H 8.19 0.02 1 161 53 54 ARG CA C 58.7 0.3 1 162 53 54 ARG CB C 30.9 0.3 1 163 53 54 ARG N N 123.8 0.3 1 164 54 55 ALA H H 8.81 0.02 1 165 54 55 ALA CA C 54.9 0.3 1 166 54 55 ALA CB C 17.6 0.3 1 167 54 55 ALA N N 123.7 0.3 1 168 55 56 SER H H 8.34 0.02 1 169 55 56 SER CA C 61.5 0.3 1 170 55 56 SER CB C 63.4 0.3 1 171 55 56 SER N N 115.1 0.3 1 172 56 57 GLU H H 7.75 0.02 1 173 56 57 GLU CA C 59.2 0.3 1 174 56 57 GLU CB C 28.9 0.3 1 175 56 57 GLU N N 123.1 0.3 1 176 57 58 LEU H H 7.94 0.02 1 177 57 58 LEU CA C 59.5 0.3 1 178 57 58 LEU CB C 41.4 0.3 1 179 57 58 LEU N N 122.3 0.3 1 180 58 59 GLN H H 8.22 0.02 1 181 58 59 GLN CA C 59.4 0.3 1 182 58 59 GLN CB C 28.9 0.3 1 183 58 59 GLN N N 119.9 0.3 1 184 59 60 ARG H H 7.89 0.02 1 185 59 60 ARG CA C 54.8 0.3 1 186 59 60 ARG CB C 28.6 0.3 1 187 59 60 ARG N N 123.6 0.3 1 188 61 62 GLU H H 8.49 0.02 1 189 61 62 GLU CA C 59.8 0.3 1 190 61 62 GLU CB C 28.8 0.3 1 191 61 62 GLU N N 121.5 0.3 1 192 62 63 THR H H 8.12 0.02 1 193 62 63 THR CA C 66.3 0.3 1 194 62 63 THR CB C 68.5 0.3 1 195 62 63 THR N N 116.0 0.3 1 196 63 64 ASP H H 8.02 0.02 1 197 63 64 ASP CA C 57.4 0.3 1 198 63 64 ASP CB C 41.2 0.3 1 199 63 64 ASP N N 124.1 0.3 1 200 64 65 LEU H H 8.54 0.02 1 201 64 65 LEU CA C 57.5 0.3 1 202 64 65 LEU CB C 39.9 0.3 1 203 64 65 LEU N N 122.2 0.3 1 204 65 66 GLN H H 8.52 0.02 1 205 65 66 GLN CA C 59.7 0.3 1 206 65 66 GLN CB C 28.8 0.3 1 207 65 66 GLN N N 121.5 0.3 1 208 66 67 ALA H H 9.06 0.02 1 209 66 67 ALA CA C 55.1 0.3 1 210 66 67 ALA CB C 16.8 0.3 1 211 66 67 ALA N N 125.4 0.3 1 212 67 68 LYS H H 8.55 0.02 1 213 67 68 LYS CA C 55.1 0.3 1 214 67 68 LYS CB C 29.1 0.3 1 215 67 68 LYS N N 125.3 0.3 1 216 68 69 MET H H 8.13 0.02 1 217 68 69 MET CA C 59.8 0.3 1 218 68 69 MET CB C 32.3 0.3 1 219 68 69 MET N N 120.8 0.3 1 220 69 70 LYS H H 8.49 0.02 1 221 69 70 LYS CA C 58.6 0.3 1 222 69 70 LYS CB C 31.1 0.3 1 223 69 70 LYS N N 118.6 0.3 1 224 70 71 LYS H H 7.89 0.02 1 225 70 71 LYS CA C 59.1 0.3 1 226 70 71 LYS CB C 31.4 0.3 1 227 70 71 LYS N N 120.3 0.3 1 228 71 72 LEU H H 8.26 0.02 1 229 71 72 LEU CA C 58.0 0.3 1 230 71 72 LEU CB C 41.6 0.3 1 231 71 72 LEU N N 120.4 0.3 1 232 72 73 GLN H H 7.63 0.02 1 233 72 73 GLN CA C 58.0 0.3 1 234 72 73 GLN CB C 28.0 0.3 1 235 72 73 GLN N N 115.4 0.3 1 236 73 74 SER H H 7.44 0.02 1 237 73 74 SER CA C 58.1 0.3 1 238 73 74 SER CB C 64.3 0.3 1 239 73 74 SER N N 111.8 0.3 1 240 74 75 MET H H 7.42 0.02 1 241 74 75 MET CA C 56.0 0.3 1 242 74 75 MET CB C 34.4 0.3 1 243 74 75 MET N N 122.8 0.3 1 244 75 76 LYS H H 8.49 0.02 1 245 75 76 LYS CA C 55.6 0.3 1 246 75 76 LYS CB C 32.4 0.3 1 247 75 76 LYS N N 124.7 0.3 1 248 76 77 ALA H H 8.25 0.02 1 249 76 77 ALA CA C 53.1 0.3 1 250 76 77 ALA CB C 18.2 0.3 1 251 76 77 ALA N N 123.4 0.3 1 252 77 78 GLY H H 8.33 0.02 1 253 77 78 GLY CA C 44.4 0.3 1 254 77 78 GLY N N 109.6 0.3 1 255 78 79 SER H H 8.26 0.02 1 256 78 79 SER N N 113.6 0.3 1 257 80 81 ARG H H 7.86 0.02 1 258 80 81 ARG CA C 59.6 0.3 1 259 80 81 ARG N N 121.2 0.3 1 260 81 82 THR H H 8.07 0.02 1 261 81 82 THR CA C 67.0 0.3 1 262 81 82 THR CB C 68.6 0.3 1 263 81 82 THR N N 116.1 0.3 1 264 82 83 LYS H H 8.35 0.02 1 265 82 83 LYS CA C 59.4 0.3 1 266 82 83 LYS CB C 31.9 0.3 1 267 82 83 LYS N N 121.3 0.3 1 268 83 84 LEU H H 7.79 0.02 1 269 83 84 LEU CA C 57.9 0.3 1 270 83 84 LEU CB C 41.4 0.3 1 271 83 84 LEU N N 120.6 0.3 1 272 84 85 GLU H H 8.02 0.02 1 273 84 85 GLU CA C 59.5 0.3 1 274 84 85 GLU CB C 27.7 0.3 1 275 84 85 GLU N N 120.0 0.3 1 276 85 86 LYS H H 7.66 0.02 1 277 85 86 LYS CA C 59.3 0.3 1 278 85 86 LYS CB C 31.7 0.3 1 279 85 86 LYS N N 121.7 0.3 1 280 86 87 ASP H H 7.94 0.02 1 281 86 87 ASP CA C 57.4 0.3 1 282 86 87 ASP CB C 40.5 0.3 1 283 86 87 ASP N N 122.4 0.3 1 284 87 88 VAL H H 8.85 0.02 1 285 87 88 VAL CA C 66.9 0.3 1 286 87 88 VAL CB C 30.8 0.3 1 287 87 88 VAL N N 120.7 0.3 1 288 88 89 MET H H 8.23 0.02 1 289 88 89 MET CA C 58.7 0.3 1 290 88 89 MET CB C 30.8 0.3 1 291 88 89 MET N N 119.4 0.3 1 292 89 90 ALA H H 7.84 0.02 1 293 89 90 ALA CA C 55.0 0.3 1 294 89 90 ALA CB C 17.4 0.3 1 295 89 90 ALA N N 122.7 0.3 1 296 90 91 GLN H H 7.82 0.02 1 297 90 91 GLN CA C 58.9 0.3 1 298 90 91 GLN CB C 27.8 0.3 1 299 90 91 GLN N N 117.5 0.3 1 300 91 92 ARG H H 8.04 0.02 1 301 91 92 ARG CA C 59.1 0.3 1 302 91 92 ARG CB C 29.1 0.3 1 303 91 92 ARG N N 120.9 0.3 1 304 92 93 GLN H H 7.68 0.02 1 305 92 93 GLN CA C 59.0 0.3 1 306 92 93 GLN CB C 27.7 0.3 1 307 92 93 GLN N N 120.0 0.3 1 308 93 94 THR H H 8.16 0.02 1 309 93 94 THR CA C 66.7 0.3 1 310 93 94 THR CB C 68.3 0.3 1 311 93 94 THR N N 118.1 0.3 1 312 94 95 PHE H H 8.72 0.02 1 313 94 95 PHE CA C 61.5 0.3 1 314 94 95 PHE CB C 38.8 0.3 1 315 94 95 PHE N N 123.0 0.3 1 316 95 96 ALA H H 8.23 0.02 1 317 95 96 ALA CA C 54.9 0.3 1 318 95 96 ALA CB C 17.4 0.3 1 319 95 96 ALA N N 120.8 0.3 1 320 96 97 GLN H H 8.60 0.02 1 321 96 97 GLN CA C 58.9 0.3 1 322 96 97 GLN CB C 27.8 0.3 1 323 96 97 GLN N N 120.6 0.3 1 324 97 98 LYS H H 9.07 0.02 1 325 97 98 LYS CA C 59.8 0.3 1 326 97 98 LYS CB C 29.4 0.3 1 327 97 98 LYS N N 121.5 0.3 1 328 98 99 ALA H H 7.81 0.02 1 329 98 99 ALA CA C 54.8 0.3 1 330 98 99 ALA CB C 17.4 0.3 1 331 98 99 ALA N N 122.5 0.3 1 332 99 100 GLN H H 8.03 0.02 1 333 99 100 GLN CA C 59.6 0.3 1 334 99 100 GLN CB C 29.4 0.3 1 335 99 100 GLN N N 120.1 0.3 1 336 100 101 ALA H H 7.84 0.02 1 337 100 101 ALA CA C 55.0 0.3 1 338 100 101 ALA CB C 17.3 0.3 1 339 100 101 ALA N N 122.6 0.3 1 340 101 102 PHE H H 7.99 0.02 1 341 101 102 PHE CA C 61.3 0.3 1 342 101 102 PHE CB C 39.2 0.3 1 343 101 102 PHE N N 119.3 0.3 1 344 102 103 GLU H H 8.11 0.02 1 345 102 103 GLU CA C 59.4 0.3 1 346 102 103 GLU CB C 27.2 0.3 1 347 102 103 GLU N N 120.2 0.3 1 348 103 104 GLN H H 7.78 0.02 1 349 103 104 GLN CA C 59.4 0.3 1 350 103 104 GLN CB C 31.4 0.3 1 351 103 104 GLN N N 119.0 0.3 1 352 104 105 ASP H H 7.69 0.02 1 353 104 105 ASP CA C 57.5 0.3 1 354 104 105 ASP CB C 40.3 0.3 1 355 104 105 ASP N N 121.5 0.3 1 356 105 106 ARG H H 8.96 0.02 1 357 105 106 ARG CA C 60.0 0.3 1 358 105 106 ARG CB C 29.3 0.3 1 359 105 106 ARG N N 120.5 0.3 1 360 106 107 ALA H H 8.70 0.02 1 361 106 107 ALA CA C 55.1 0.3 1 362 106 107 ALA CB C 17.3 0.3 1 363 106 107 ALA N N 122.2 0.3 1 364 107 108 ARG H H 7.80 0.02 1 365 107 108 ARG CA C 57.3 0.3 1 366 107 108 ARG CB C 30.2 0.3 1 367 107 108 ARG N N 121.8 0.3 1 368 108 109 ARG H H 8.64 0.02 1 369 108 109 ARG CA C 56.8 0.3 1 370 108 109 ARG CB C 30.5 0.3 1 371 108 109 ARG N N 119.2 0.3 1 372 109 110 SER H H 8.36 0.02 1 373 109 110 SER CA C 62.3 0.3 1 374 109 110 SER CB C 64.9 0.3 1 375 109 110 SER N N 115.2 0.3 1 376 110 111 ASN H H 8.17 0.02 1 377 110 111 ASN CA C 56.8 0.3 1 378 110 111 ASN CB C 39.0 0.3 1 379 110 111 ASN N N 118.8 0.3 1 380 111 112 GLU H H 8.25 0.02 1 381 111 112 GLU CA C 58.8 0.3 1 382 111 112 GLU CB C 28.0 0.3 1 383 111 112 GLU N N 119.3 0.3 1 384 112 113 GLU H H 8.26 0.02 1 385 112 113 GLU CA C 58.9 0.3 1 386 112 113 GLU CB C 27.5 0.3 1 387 112 113 GLU N N 118.3 0.3 1 388 113 114 ARG H H 7.66 0.02 1 389 113 114 ARG CA C 58.9 0.3 1 390 113 114 ARG CB C 31.3 0.3 1 391 113 114 ARG N N 121.3 0.3 1 392 114 115 GLY H H 8.41 0.02 1 393 114 115 GLY CA C 44.9 0.3 1 394 114 115 GLY N N 110.3 0.3 1 395 115 116 LYS H H 7.92 0.02 1 396 115 116 LYS CA C 55.0 0.3 1 397 115 116 LYS N N 115.8 0.3 1 398 116 117 LEU H H 8.09 0.02 1 399 116 117 LEU CA C 56.4 0.3 1 400 116 117 LEU CB C 38.0 0.3 1 401 116 117 LEU N N 120.5 0.3 1 402 117 118 VAL H H 8.22 0.02 1 403 117 118 VAL CA C 59.5 0.3 1 404 117 118 VAL CB C 29.1 0.3 1 405 117 118 VAL N N 124.8 0.3 1 406 118 119 THR H H 8.33 0.02 1 407 118 119 THR CA C 66.5 0.3 1 408 118 119 THR CB C 68.9 0.3 1 409 118 119 THR N N 116.8 0.3 1 410 119 120 ARG H H 7.80 0.02 1 411 119 120 ARG CA C 59.6 0.3 1 412 119 120 ARG CB C 31.7 0.3 1 413 119 120 ARG N N 121.2 0.3 1 414 120 121 ILE H H 8.38 0.02 1 415 120 121 ILE CA C 65.9 0.3 1 416 120 121 ILE CB C 37.4 0.3 1 417 120 121 ILE N N 121.0 0.3 1 418 121 122 GLN H H 9.08 0.02 1 419 121 122 GLN CA C 59.8 0.3 1 420 121 122 GLN CB C 28.0 0.3 1 421 121 122 GLN N N 120.5 0.3 1 422 122 123 THR H H 8.26 0.02 1 423 122 123 THR CA C 66.7 0.3 1 424 122 123 THR CB C 68.9 0.3 1 425 122 123 THR N N 116.6 0.3 1 426 123 124 ALA H H 7.35 0.02 1 427 123 124 ALA CA C 55.1 0.3 1 428 123 124 ALA CB C 19.3 0.3 1 429 123 124 ALA N N 126.2 0.3 1 430 124 125 VAL H H 8.61 0.02 1 431 124 125 VAL CA C 66.5 0.3 1 432 124 125 VAL CB C 30.7 0.3 1 433 124 125 VAL N N 119.2 0.3 1 434 125 126 LYS H H 7.72 0.02 1 435 125 126 LYS CA C 59.4 0.3 1 436 125 126 LYS CB C 33.4 0.3 1 437 125 126 LYS N N 119.0 0.3 1 438 126 127 SER H H 7.68 0.02 1 439 126 127 SER CA C 59.3 0.3 1 440 126 127 SER CB C 61.0 0.3 1 441 126 127 SER N N 119.2 0.3 1 442 127 128 VAL H H 7.93 0.02 1 443 127 128 VAL CA C 66.2 0.3 1 444 127 128 VAL CB C 32.0 0.3 1 445 127 128 VAL N N 122.2 0.3 1 446 128 129 ALA H H 8.60 0.02 1 447 128 129 ALA CA C 55.6 0.3 1 448 128 129 ALA CB C 17.3 0.3 1 449 128 129 ALA N N 122.1 0.3 1 450 129 130 ASN H H 8.49 0.02 1 451 129 130 ASN CA C 55.9 0.3 1 452 129 130 ASN CB C 38.5 0.3 1 453 129 130 ASN N N 115.0 0.3 1 454 130 131 SER H H 7.82 0.02 1 455 130 131 SER CA C 61.2 0.3 1 456 130 131 SER CB C 62.9 0.3 1 457 130 131 SER N N 115.5 0.3 1 458 131 132 GLN H H 7.55 0.02 1 459 131 132 GLN CA C 55.5 0.3 1 460 131 132 GLN CB C 28.7 0.3 1 461 131 132 GLN N N 118.4 0.3 1 462 132 133 ASP H H 7.70 0.02 1 463 132 133 ASP CA C 55.4 0.3 1 464 132 133 ASP CB C 38.9 0.3 1 465 132 133 ASP N N 119.5 0.3 1 466 133 134 ILE H H 8.15 0.02 1 467 133 134 ILE CA C 61.2 0.3 1 468 133 134 ILE CB C 39.0 0.3 1 469 133 134 ILE N N 118.5 0.3 1 470 134 135 ASP H H 8.43 0.02 1 471 134 135 ASP CA C 56.3 0.3 1 472 134 135 ASP CB C 43.2 0.3 1 473 134 135 ASP N N 125.1 0.3 1 474 135 136 LEU H H 7.60 0.02 1 475 135 136 LEU CA C 54.0 0.3 1 476 135 136 LEU CB C 45.6 0.3 1 477 135 136 LEU N N 120.2 0.3 1 478 136 137 VAL H H 9.00 0.02 1 479 136 137 VAL CA C 59.6 0.3 1 480 136 137 VAL CB C 31.8 0.3 1 481 136 137 VAL N N 125.3 0.3 1 482 137 138 VAL H H 9.08 0.02 1 483 137 138 VAL CA C 60.2 0.3 1 484 137 138 VAL CB C 33.6 0.3 1 485 137 138 VAL N N 127.5 0.3 1 486 138 139 ASP H H 8.62 0.02 1 487 138 139 ASP CA C 54.3 0.3 1 488 138 139 ASP CB C 42.2 0.3 1 489 138 139 ASP N N 125.1 0.3 1 490 139 140 ALA H H 8.84 0.02 1 491 139 140 ALA CA C 54.4 0.3 1 492 139 140 ALA CB C 18.3 0.3 1 493 139 140 ALA N N 129.5 0.3 1 494 140 141 ASN H H 8.84 0.02 1 495 140 141 ASN CA C 55.5 0.3 1 496 140 141 ASN CB C 38.1 0.3 1 497 140 141 ASN N N 116.0 0.3 1 498 141 142 ALA H H 8.18 0.02 1 499 141 142 ALA CA C 51.7 0.3 1 500 141 142 ALA CB C 18.6 0.3 1 501 141 142 ALA N N 120.3 0.3 1 502 142 143 VAL H H 7.53 0.02 1 503 142 143 VAL CA C 62.2 0.3 1 504 142 143 VAL CB C 32.9 0.3 1 505 142 143 VAL N N 119.6 0.3 1 506 143 144 ALA H H 8.67 0.02 1 507 143 144 ALA CA C 52.3 0.3 1 508 143 144 ALA CB C 20.3 0.3 1 509 143 144 ALA N N 129.3 0.3 1 510 144 145 TYR H H 7.60 0.02 1 511 144 145 TYR CA C 58.9 0.3 1 512 144 145 TYR CB C 41.2 0.3 1 513 144 145 TYR N N 116.7 0.3 1 514 145 146 ASN H H 6.88 0.02 1 515 145 146 ASN CA C 52.0 0.3 1 516 145 146 ASN CB C 40.8 0.3 1 517 145 146 ASN N N 123.6 0.3 1 518 146 147 SER H H 8.86 0.02 1 519 146 147 SER CA C 56.7 0.3 1 520 146 147 SER CB C 64.8 0.3 1 521 146 147 SER N N 119.2 0.3 1 522 147 148 SER H H 8.63 0.02 1 523 147 148 SER CA C 60.3 0.3 1 524 147 148 SER CB C 62.6 0.3 1 525 147 148 SER N N 114.2 0.3 1 526 148 149 ASP H H 7.82 0.02 1 527 148 149 ASP CA C 55.5 0.3 1 528 148 149 ASP CB C 39.7 0.3 1 529 148 149 ASP N N 119.7 0.3 1 530 149 150 VAL H H 7.42 0.02 1 531 149 150 VAL CA C 61.4 0.3 1 532 149 150 VAL CB C 31.4 0.3 1 533 149 150 VAL N N 122.6 0.3 1 534 150 151 LYS H H 8.93 0.02 1 535 150 151 LYS CA C 56.7 0.3 1 536 150 151 LYS CB C 32.6 0.3 1 537 150 151 LYS N N 127.7 0.3 1 538 151 152 ASP H H 8.23 0.02 1 539 151 152 ASP CA C 52.3 0.3 1 540 151 152 ASP CB C 40.8 0.3 1 541 151 152 ASP N N 121.5 0.3 1 542 152 153 ILE H H 8.66 0.02 1 543 152 153 ILE CA C 61.4 0.3 1 544 152 153 ILE CB C 37.3 0.3 1 545 152 153 ILE N N 118.4 0.3 1 546 153 154 THR H H 8.86 0.02 1 547 153 154 THR CA C 69.6 0.3 1 548 153 154 THR CB C 72.0 0.3 1 549 153 154 THR N N 121.6 0.3 1 550 154 155 ALA H H 8.71 0.02 1 551 154 155 ALA CA C 55.2 0.3 1 552 154 155 ALA CB C 17.2 0.3 1 553 154 155 ALA N N 121.8 0.3 1 554 155 156 ASP H H 7.69 0.02 1 555 155 156 ASP CA C 57.0 0.3 1 556 155 156 ASP CB C 40.5 0.3 1 557 155 156 ASP N N 118.8 0.3 1 558 156 157 VAL H H 8.37 0.02 1 559 156 157 VAL CA C 66.3 0.3 1 560 156 157 VAL CB C 30.2 0.3 1 561 156 157 VAL N N 120.5 0.3 1 562 157 158 LEU H H 8.09 0.02 1 563 157 158 LEU CA C 57.9 0.3 1 564 157 158 LEU CB C 40.6 0.3 1 565 157 158 LEU N N 120.2 0.3 1 566 158 159 LYS H H 7.18 0.02 1 567 158 159 LYS CA C 58.2 0.3 1 568 158 159 LYS CB C 32.1 0.3 1 569 158 159 LYS N N 115.3 0.3 1 570 159 160 GLN H H 7.49 0.02 1 571 159 160 GLN CA C 55.1 0.3 1 572 159 160 GLN CB C 28.6 0.3 1 573 159 160 GLN N N 115.7 0.3 1 574 160 161 VAL H H 7.31 0.02 1 575 160 161 VAL CA C 63.6 0.3 1 576 160 161 VAL CB C 30.8 0.3 1 577 160 161 VAL N N 121.3 0.3 1 578 161 162 LYS H H 7.89 0.02 1 579 161 162 LYS CA C 57.2 0.3 1 580 161 162 LYS CB C 33.4 0.3 1 581 161 162 LYS N N 132.9 0.3 1 stop_ save_