data_18756 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Backbone 15N, 1H, and CA Chemical Shift Assignments for WT IkappaBalpha (67-287) ; _BMRB_accession_number 18756 _BMRB_flat_file_name bmr18756.str _Entry_type original _Submission_date 2012-10-02 _Accession_date 2012-10-02 _Entry_origination author _NMR_STAR_version 2.1.1 _Experimental_method NMR _Details ; The effects of consensus mutations, Y254L/T257A and C186P/A220P, on the structure and dynamics of the AR domain of IkappaBalpha were investigated by NMR. ; loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Cervantes Carla F. . 2 Handley Lindsey D. . 3 Komives Elizabeth A. . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 139 "13C chemical shifts" 163 "15N chemical shifts" 139 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2013-02-22 update BMRB 'update entry citation' 2013-02-12 original author 'original release' stop_ loop_ _Related_BMRB_accession_number _Relationship 18759 'C186P/A220P IkappaBalpha (67-287)' 18760 'Y254L/T257A IkappaBalpha (67-287)' stop_ save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title 'Long-Range Effects and Functional Consequences of Stabilizing Mutations in the Ankyrin Repeat Domain of IB.' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 23274114 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Cervantes Carla F. . 2 Handley Lindsey D. . 3 Sue Shih-Che . . 4 Dyson 'H. Jane' . . 5 Komives Elizabeth A. . stop_ _Journal_abbreviation 'J. Mol. Biol.' _Journal_name_full 'Journal of molecular biology' _Journal_volume 425 _Journal_issue 5 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 902 _Page_last 913 _Year 2013 _Details . loop_ _Keyword 'ankyrin repeat' 'chemical shift difference' PEST proteasome relaxation stop_ save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name 'WT IkappaBalpha' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'WT IkappaBalpha' $WT_IkappaBalpha stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state ? _System_paramagnetic no _System_thiol_state . _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_WT_IkappaBalpha _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common WT_IkappaBalpha _Molecular_mass . _Mol_thiol_state 'all free' loop_ _Biological_function 'Inhibitor of transcription factor NFkappaB' stop_ _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 221 _Mol_residue_sequence ; KQQLTEDGDSFLHLAIIHEE KALTMEVIRQVKGDLAFLNF QNNLQQTPLHLAVITNQPEI AEALLGAGCDPELRDFRGNT PLHLACEQGCLASVGVLTQS CTTPHLHSILKATNYNGHTC LHLASIHGYLGIVELLVSLG ADVNAQEPCNGRTALHLAVD LQNPDLVSLLLKCGADVNRV TYQGYSPYQLTWGRPSTRIQ QQLGQLTLENLQMLPESEDE E ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 67 LYS 2 68 GLN 3 69 GLN 4 70 LEU 5 71 THR 6 72 GLU 7 73 ASP 8 74 GLY 9 75 ASP 10 76 SER 11 77 PHE 12 78 LEU 13 79 HIS 14 80 LEU 15 81 ALA 16 82 ILE 17 83 ILE 18 84 HIS 19 85 GLU 20 86 GLU 21 87 LYS 22 88 ALA 23 89 LEU 24 90 THR 25 91 MET 26 92 GLU 27 93 VAL 28 94 ILE 29 95 ARG 30 96 GLN 31 97 VAL 32 98 LYS 33 99 GLY 34 100 ASP 35 101 LEU 36 102 ALA 37 103 PHE 38 104 LEU 39 105 ASN 40 106 PHE 41 107 GLN 42 108 ASN 43 109 ASN 44 110 LEU 45 111 GLN 46 112 GLN 47 113 THR 48 114 PRO 49 115 LEU 50 116 HIS 51 117 LEU 52 118 ALA 53 119 VAL 54 120 ILE 55 121 THR 56 122 ASN 57 123 GLN 58 124 PRO 59 125 GLU 60 126 ILE 61 127 ALA 62 128 GLU 63 129 ALA 64 130 LEU 65 131 LEU 66 132 GLY 67 133 ALA 68 134 GLY 69 135 CYS 70 136 ASP 71 137 PRO 72 138 GLU 73 139 LEU 74 140 ARG 75 141 ASP 76 142 PHE 77 143 ARG 78 144 GLY 79 145 ASN 80 146 THR 81 147 PRO 82 148 LEU 83 149 HIS 84 150 LEU 85 151 ALA 86 152 CYS 87 153 GLU 88 154 GLN 89 155 GLY 90 156 CYS 91 157 LEU 92 158 ALA 93 159 SER 94 160 VAL 95 161 GLY 96 162 VAL 97 163 LEU 98 164 THR 99 165 GLN 100 166 SER 101 167 CYS 102 168 THR 103 169 THR 104 170 PRO 105 171 HIS 106 172 LEU 107 173 HIS 108 174 SER 109 175 ILE 110 176 LEU 111 177 LYS 112 178 ALA 113 179 THR 114 180 ASN 115 181 TYR 116 182 ASN 117 183 GLY 118 184 HIS 119 185 THR 120 186 CYS 121 187 LEU 122 188 HIS 123 189 LEU 124 190 ALA 125 191 SER 126 192 ILE 127 193 HIS 128 194 GLY 129 195 TYR 130 196 LEU 131 197 GLY 132 198 ILE 133 199 VAL 134 200 GLU 135 201 LEU 136 202 LEU 137 203 VAL 138 204 SER 139 205 LEU 140 206 GLY 141 207 ALA 142 208 ASP 143 209 VAL 144 210 ASN 145 211 ALA 146 212 GLN 147 213 GLU 148 214 PRO 149 215 CYS 150 216 ASN 151 217 GLY 152 218 ARG 153 219 THR 154 220 ALA 155 221 LEU 156 222 HIS 157 223 LEU 158 224 ALA 159 225 VAL 160 226 ASP 161 227 LEU 162 228 GLN 163 229 ASN 164 230 PRO 165 231 ASP 166 232 LEU 167 233 VAL 168 234 SER 169 235 LEU 170 236 LEU 171 237 LEU 172 238 LYS 173 239 CYS 174 240 GLY 175 241 ALA 176 242 ASP 177 243 VAL 178 244 ASN 179 245 ARG 180 246 VAL 181 247 THR 182 248 TYR 183 249 GLN 184 250 GLY 185 251 TYR 186 252 SER 187 253 PRO 188 254 TYR 189 255 GLN 190 256 LEU 191 257 THR 192 258 TRP 193 259 GLY 194 260 ARG 195 261 PRO 196 262 SER 197 263 THR 198 264 ARG 199 265 ILE 200 266 GLN 201 267 GLN 202 268 GLN 203 269 LEU 204 270 GLY 205 271 GLN 206 272 LEU 207 273 THR 208 274 LEU 209 275 GLU 210 276 ASN 211 277 LEU 212 278 GLN 213 279 MET 214 280 LEU 215 281 PRO 216 282 GLU 217 283 SER 218 284 GLU 219 285 ASP 220 286 GLU 221 287 GLU stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-01-30 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 18759 CPAP_IkappaBalpha 100.00 221 99.10 99.10 3.91e-156 BMRB 18760 YLTA_IkappaBalpha 100.00 221 99.10 99.10 8.74e-157 PDB 1IKN "IkappabalphaNF-Kappab Complex" 100.00 236 100.00 100.00 6.30e-159 PDB 1NFI "I-Kappa-B-AlphaNF-Kappa-B Complex" 96.38 213 100.00 100.00 1.92e-152 DBJ BAE89638 "unnamed protein product [Macaca fascicularis]" 100.00 317 100.00 100.00 1.12e-157 DBJ BAG36213 "unnamed protein product [Homo sapiens]" 100.00 317 100.00 100.00 9.42e-158 DBJ BAI46793 "nuclear factor of kappa light polypeptide gene enhancer in B-cells inhibitor, alpha [synthetic construct]" 100.00 317 100.00 100.00 9.42e-158 EMBL CAB65556 "IkBa [Homo sapiens]" 100.00 317 100.00 100.00 9.42e-158 GB AAA16489 "MAD3 [Homo sapiens]" 100.00 317 100.00 100.00 9.42e-158 GB AAH02601 "Nuclear factor of kappa light polypeptide gene enhancer in B-cells inhibitor, alpha [Homo sapiens]" 100.00 317 100.00 100.00 9.42e-158 GB AAH04983 "Nuclear factor of kappa light polypeptide gene enhancer in B-cells inhibitor, alpha [Homo sapiens]" 100.00 317 100.00 100.00 9.42e-158 GB AAK51149 "NFKBIA [Homo sapiens]" 100.00 317 100.00 100.00 9.42e-158 GB AAP35754 "nuclear factor of kappa light polypeptide gene enhancer in B-cells inhibitor, alpha [Homo sapiens]" 100.00 317 100.00 100.00 9.42e-158 REF NP_001244679 "NF-kappa-B inhibitor alpha [Macaca mulatta]" 100.00 317 100.00 100.00 1.12e-157 REF NP_001271861 "uncharacterized protein LOC101867458 [Macaca fascicularis]" 100.00 317 100.00 100.00 1.12e-157 REF NP_065390 "NF-kappa-B inhibitor alpha [Homo sapiens]" 100.00 317 100.00 100.00 9.42e-158 REF XP_002753867 "PREDICTED: NF-kappa-B inhibitor alpha [Callithrix jacchus]" 100.00 310 99.10 100.00 2.03e-157 REF XP_002824720 "PREDICTED: NF-kappa-B inhibitor alpha [Pongo abelii]" 100.00 317 99.55 99.55 1.60e-156 SP P25963 "RecName: Full=NF-kappa-B inhibitor alpha; AltName: Full=I-kappa-B-alpha; Short=IkB-alpha; Short=IkappaBalpha; AltName: Full=Maj" 100.00 317 100.00 100.00 9.42e-158 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $WT_IkappaBalpha Human 9606 Eukaryota Metazoa Homo sapiens 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 $WT_IkappaBalpha 'recombinant technology' . Escherichia coli BL21(DE3) pET11a stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_WT_IkappaBalpha_3x-labelled _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $WT_IkappaBalpha 0.1 mM '[U-13C; U-15N; U-2H]' 2H-Tris 25 mM '[U-99% 2H]' 'sodium chloride' 50 mM 'natural abundance' EDTA 1 mM 'natural abundance' CHAPS 5 mM 'natural abundance' 'sodium azide' 2 mM 'natural abundance' DTT 2 mM 'natural abundance' D2O 10 % '[U-100% 2H]' 'protease inhibitor cocktail' 1 % 'natural abundance' stop_ save_ save_WT_IkappaBalpha_Gly_15N-labelled _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $WT_IkappaBalpha 0.1 mM [U-15N]-Gly 2H-Tris 25 mM '[U-99% 2H]' 'sodium chloride' 50 mM 'natural abundance' EDTA 1 mM 'natural abundance' CHAPS 5 mM 'natural abundance' 'sodium azide' 2 mM 'natural abundance' DTT 2 mM 'natural abundance' D2O 10 % '[U-100% 2H]' 'protease inhibitor cocktail' 1 % 'natural abundance' stop_ save_ save_WT_IkappaBalpha_Thr_15N-labelled _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $WT_IkappaBalpha 0.1 mM [U-15N]-Thr 2H-Tris 25 mM '[U-99% 2H]' 'sodium chloride' 50 mM 'natural abundance' EDTA 1 mM 'natural abundance' CHAPS 5 mM 'natural abundance' 'sodium azide' 2 mM 'natural abundance' DTT 2 mM 'natural abundance' D2O 10 % '[U-100% 2H]' 'protease inhibitor cocktail' 1 % 'natural abundance' stop_ save_ save_WT_IkappaBalpha_Ala_15N-labelled _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $WT_IkappaBalpha 0.1 mM [U-15N]-Ala 2H-Tris 25 mM '[U-99% 2H]' 'sodium chloride' 50 mM 'natural abundance' EDTA 1 mM 'natural abundance' CHAPS 5 mM 'natural abundance' 'sodium azide' 2 mM 'natural abundance' DTT 2 mM 'natural abundance' D2O 10 % '[U-100% 2H]' 'protease inhibitor cocktail' 1 % 'natural abundance' stop_ save_ save_WT_IkappaBalpha_Leu_15N-labelled _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $WT_IkappaBalpha 0.1 mM [U-15N]-Leu 2H-Tris 25 mM '[U-99% 2H]' 'sodium chloride' 50 mM 'natural abundance' EDTA 1 mM 'natural abundance' CHAPS 5 mM 'natural abundance' 'sodium azide' 2 mM 'natural abundance' DTT 2 mM 'natural abundance' D2O 10 % '[U-100% 2H]' 'protease inhibitor cocktail' 1 % 'natural abundance' stop_ save_ save_WT_IkappaBalpha_Val_15N-labelled _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $WT_IkappaBalpha 0.1 mM [U-15N]-Val 2H-Tris 25 mM '[U-99% 2H]' 'sodium chloride' 50 mM 'natural abundance' EDTA 1 mM 'natural abundance' CHAPS 5 mM 'natural abundance' 'sodium azide' 2 mM 'natural abundance' DTT 2 mM 'natural abundance' D2O 10 % '[U-100% 2H]' 'protease inhibitor cocktail' 1 % 'natural abundance' stop_ save_ ############################ # Computer software used # ############################ save_NMRView _Saveframe_category software _Name NMRView _Version . loop_ _Vendor _Address _Electronic_address 'One Moon Scientific, Inc.' ; 839 Grant Ave. Westfield, NJ 07090 ; http://www.onemoonscientific.com/index.html stop_ loop_ _Task 'chemical shift assignment' 'peak picking' stop_ _Details . save_ save_NMRPipe _Saveframe_category software _Name NMRPipe _Version . loop_ _Vendor _Address _Electronic_address 'Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax' ; 31 Center Drive, MSC 2560 Bethesda, MD 20892-2560 ; http://spin.niddk.nih.gov/NMRPipe/ stop_ loop_ _Task processing stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model DRX _Field_strength 600 _Details . save_ save_spectrometer_2 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model Avance _Field_strength 800 _Details . save_ ############################# # NMR applied experiments # ############################# save_3D_HN(CO)CA_1 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HN(CO)CA' _Sample_label $WT_IkappaBalpha_3x-labelled save_ save_3D_HNCO_2 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCO' _Sample_label $WT_IkappaBalpha_3x-labelled save_ save_3D_HNCA_3 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCA' _Sample_label $WT_IkappaBalpha_3x-labelled save_ save_3D_HNCACB_4 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCACB' _Sample_label $WT_IkappaBalpha_3x-labelled save_ save_2D_1H-15N_HSQC_5 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-15N HSQC' _Sample_label $WT_IkappaBalpha_Gly_15N-labelled save_ save_2D_1H-15N_HSQC_6 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-15N HSQC' _Sample_label $WT_IkappaBalpha_Thr_15N-labelled save_ save_2D_1H-15N_HSQC_7 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-15N HSQC' _Sample_label $WT_IkappaBalpha_Ala_15N-labelled save_ save_2D_1H-15N_HSQC_8 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-15N HSQC' _Sample_label $WT_IkappaBalpha_Leu_15N-labelled save_ save_2D_1H-15N_HSQC_9 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-15N HSQC' _Sample_label $WT_IkappaBalpha_Val_15N-labelled save_ ####################### # Sample conditions # ####################### save_sample_conditions_1 _Saveframe_category sample_conditions _Details 'These sample conditions were used for all NMR samples.' loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 7.5 . pH pressure 1 . atm temperature 273 . 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_WT_shift_list _Saveframe_category assigned_chemical_shifts _Details . loop_ _Experiment_label '3D HN(CO)CA' '3D HNCO' '3D HNCA' '3D HNCACB' '2D 1H-15N HSQC' stop_ loop_ _Sample_label $WT_IkappaBalpha_3x-labelled $WT_IkappaBalpha_Gly_15N-labelled $WT_IkappaBalpha_Thr_15N-labelled $WT_IkappaBalpha_Ala_15N-labelled $WT_IkappaBalpha_Leu_15N-labelled $WT_IkappaBalpha_Val_15N-labelled stop_ _Sample_conditions_label $sample_conditions_1 _Chem_shift_reference_set_label $chemical_shift_reference_1 _Mol_system_component_name 'WT IkappaBalpha' _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 69 3 GLN CA C 55.441 0.46 . 2 70 4 LEU H H 8.382 0.0059 . 3 70 4 LEU CA C 53.21 0.46 . 4 70 4 LEU N N 122.592 0.14 . 5 71 5 THR H H 8.17 0.0059 . 6 71 5 THR CA C 60.092 0.46 . 7 71 5 THR N N 109.377 0.14 . 8 72 6 GLU H H 9.454 0.0059 . 9 72 6 GLU CA C 58.059 0.46 . 10 72 6 GLU N N 121.388 0.14 . 11 73 7 ASP H H 7.766 0.0059 . 12 73 7 ASP CA C 53.745 0.46 . 13 73 7 ASP N N 115.518 0.14 . 14 74 8 GLY H H 8.4 0.0059 . 15 74 8 GLY CA C 45.712 0.46 . 16 74 8 GLY N N 110.666 0.14 . 17 75 9 ASP H H 7.202 0.0059 . 18 75 9 ASP CA C 55.311 0.46 . 19 75 9 ASP N N 115.432 0.14 . 20 76 10 SER CA C 57.134 0.46 . 21 77 11 PHE H H 9.879 0.0059 . 22 77 11 PHE CA C 61.479 0.46 . 23 77 11 PHE N N 120.29 0.14 . 24 78 12 LEU H H 8.016 0.0059 . 25 78 12 LEU CA C 56.761 0.46 . 26 78 12 LEU N N 116.407 0.14 . 27 80 14 LEU H H 8.152 0.0059 . 28 80 14 LEU CA C 57.099 0.46 . 29 80 14 LEU N N 114.621 0.14 . 30 81 15 ALA H H 8.375 0.0059 . 31 81 15 ALA CA C 55.319 0.46 . 32 81 15 ALA N N 122.564 0.14 . 33 82 16 ILE H H 7.468 0.0059 . 34 82 16 ILE CA C 65.074 0.46 . 35 82 16 ILE N N 116.116 0.14 . 36 83 17 ILE H H 8.71 0.0059 . 37 83 17 ILE CA C 65.125 0.46 . 38 83 17 ILE N N 123.189 0.14 . 39 84 18 HIS H H 7.951 0.0059 . 40 84 18 HIS CA C 57.135 0.46 . 41 84 18 HIS N N 114.738 0.14 . 42 85 19 GLU H H 8.288 0.0059 . 43 85 19 GLU CA C 57.078 0.46 . 44 85 19 GLU N N 116.766 0.14 . 45 86 20 GLU H H 8.217 0.0059 . 46 86 20 GLU CA C 53.809 0.46 . 47 86 20 GLU N N 119.357 0.14 . 48 87 21 LYS H H 8.039 0.0059 . 49 87 21 LYS CA C 60.836 0.46 . 50 87 21 LYS N N 126.566 0.14 . 51 88 22 ALA H H 8.611 0.0059 . 52 88 22 ALA CA C 54.944 0.46 . 53 88 22 ALA N N 121.206 0.14 . 54 89 23 LEU H H 8.502 0.0059 . 55 89 23 LEU CA C 57.523 0.46 . 56 89 23 LEU N N 120.476 0.14 . 57 90 24 THR H H 8.495 0.0059 . 58 90 24 THR CA C 68.451 0.46 . 59 90 24 THR N N 116.45 0.14 . 60 91 25 MET H H 8.32 0.0059 . 61 91 25 MET CA C 57.845 0.46 . 62 91 25 MET N N 118.503 0.14 . 63 92 26 GLU H H 7.871 0.0059 . 64 92 26 GLU CA C 58.079 0.46 . 65 92 26 GLU N N 120.845 0.14 . 66 93 27 VAL H H 8.637 0.0059 . 67 93 27 VAL CA C 66.95 0.46 . 68 93 27 VAL N N 120.016 0.14 . 69 94 28 ILE H H 8.373 0.0059 . 70 94 28 ILE CA C 65.91 0.46 . 71 94 28 ILE N N 117.195 0.14 . 72 95 29 ARG H H 7.793 0.0059 . 73 95 29 ARG CA C 59.373 0.46 . 74 95 29 ARG N N 117.216 0.14 . 75 96 30 GLN H H 8.102 0.0059 . 76 96 30 GLN CA C 57.775 0.46 . 77 96 30 GLN N N 116.019 0.14 . 78 97 31 VAL H H 8.021 0.0059 . 79 97 31 VAL CA C 60.934 0.46 . 80 97 31 VAL N N 112.106 0.14 . 81 98 32 LYS H H 7.325 0.0059 . 82 98 32 LYS CA C 57.896 0.46 . 83 98 32 LYS N N 120.173 0.14 . 84 99 33 GLY H H 8.905 0.0059 . 85 99 33 GLY CA C 45.123 0.46 . 86 99 33 GLY N N 110.556 0.14 . 87 100 34 ASP H H 8.266 0.0059 . 88 100 34 ASP CA C 52.448 0.46 . 89 100 34 ASP N N 122.607 0.14 . 90 101 35 LEU H H 8.346 0.0059 . 91 101 35 LEU CA C 57.277 0.46 . 92 101 35 LEU N N 124.97 0.14 . 93 102 36 ALA H H 8.389 0.0059 . 94 102 36 ALA CA C 54.369 0.46 . 95 102 36 ALA N N 120.313 0.14 . 96 103 37 PHE H H 7.703 0.0059 . 97 103 37 PHE CA C 60.105 0.46 . 98 103 37 PHE N N 116.384 0.14 . 99 104 38 LEU H H 8.218 0.0059 . 100 104 38 LEU CA C 56.834 0.46 . 101 104 38 LEU N N 117.282 0.14 . 102 105 39 ASN H H 7.905 0.0059 . 103 105 39 ASN CA C 51.576 0.46 . 104 105 39 ASN N N 111.266 0.14 . 105 106 40 PHE H H 7.123 0.0059 . 106 106 40 PHE CA C 60.347 0.46 . 107 106 40 PHE N N 122.575 0.14 . 108 107 41 GLN H H 7.44 0.0059 . 109 107 41 GLN CA C 53.815 0.46 . 110 107 41 GLN N N 124.953 0.14 . 111 108 42 ASN H H 7.506 0.0059 . 112 108 42 ASN CA C 51.25 0.46 . 113 108 42 ASN N N 119.525 0.14 . 114 109 43 ASN H H 8.103 0.0059 . 115 109 43 ASN CA C 55.45 0.46 . 116 109 43 ASN N N 116.182 0.14 . 117 110 44 LEU H H 7.499 0.0059 . 118 110 44 LEU CA C 54.741 0.46 . 119 110 44 LEU N N 121.681 0.14 . 120 111 45 GLN H H 8.604 0.0059 . 121 111 45 GLN CA C 57.22 0.46 . 122 111 45 GLN N N 113.244 0.14 . 123 112 46 GLN H H 8.376 0.0059 . 124 112 46 GLN CA C 55.098 0.46 . 125 112 46 GLN N N 116.022 0.14 . 126 113 47 THR H H 9.993 0.0059 . 127 113 47 THR CA C 60.086 0.46 . 128 113 47 THR N N 120.94 0.14 . 129 114 48 PRO CA C 65.644 0.46 . 130 115 49 LEU H H 8.65 0.0059 . 131 115 49 LEU CA C 57.56 0.46 . 132 115 49 LEU N N 117.97 0.14 . 133 116 50 HIS CA C 63.597 0.46 . 134 117 51 LEU H H 7.757 0.0059 . 135 117 51 LEU CA C 56.978 0.46 . 136 117 51 LEU N N 115.815 0.14 . 137 118 52 ALA H H 9.002 0.0059 . 138 118 52 ALA CA C 54.882 0.46 . 139 118 52 ALA N N 125.179 0.14 . 140 119 53 VAL H H 7.453 0.0059 . 141 119 53 VAL CA C 65.524 0.46 . 142 119 53 VAL N N 116.103 0.14 . 143 120 54 ILE CA C 64.987 0.46 . 144 121 55 THR H H 7.629 0.0059 . 145 121 55 THR CA C 61.099 0.46 . 146 121 55 THR N N 104.591 0.14 . 147 122 56 ASN H H 7.919 0.0059 . 148 122 56 ASN CA C 53.736 0.46 . 149 122 56 ASN N N 117.604 0.14 . 150 123 57 GLN H H 8.375 0.0059 . 151 123 57 GLN CA C 53.45 0.46 . 152 123 57 GLN N N 114.362 0.14 . 153 124 58 PRO CA C 64.517 0.46 . 154 125 59 GLU H H 9.601 0.0059 . 155 125 59 GLU CA C 58.622 0.46 . 156 125 59 GLU N N 119.177 0.14 . 157 126 60 ILE CA C 62.292 0.46 . 158 127 61 ALA H H 7.585 0.0059 . 159 127 61 ALA CA C 55.079 0.46 . 160 127 61 ALA N N 122.194 0.14 . 161 128 62 GLU H H 8.425 0.0059 . 162 128 62 GLU CA C 59.649 0.46 . 163 128 62 GLU N N 116.75 0.14 . 164 129 63 ALA H H 7.447 0.0059 . 165 129 63 ALA CA C 54.376 0.46 . 166 129 63 ALA N N 122.307 0.14 . 167 130 64 LEU H H 8.516 0.0059 . 168 130 64 LEU CA C 57.508 0.46 . 169 130 64 LEU N N 120.04 0.14 . 170 131 65 LEU CA C 57.931 0.46 . 171 132 66 GLY H H 8.635 0.0059 . 172 132 66 GLY CA C 46.426 0.46 . 173 132 66 GLY N N 109.267 0.14 . 174 133 67 ALA H H 7.609 0.0059 . 175 133 67 ALA CA C 51.721 0.46 . 176 133 67 ALA N N 121.137 0.14 . 177 134 68 GLY H H 7.664 0.0059 . 178 134 68 GLY CA C 44.355 0.46 . 179 134 68 GLY N N 102.308 0.14 . 180 135 69 CYS H H 7.803 0.0059 . 181 135 69 CYS CA C 59.397 0.46 . 182 135 69 CYS N N 117.608 0.14 . 183 136 70 ASP H H 8.972 0.0059 . 184 136 70 ASP CA C 50.719 0.46 . 185 136 70 ASP N N 122.005 0.14 . 186 137 71 PRO CA C 62.846 0.46 . 187 138 72 GLU H H 8.887 0.0059 . 188 138 72 GLU CA C 56.354 0.46 . 189 138 72 GLU N N 118.082 0.14 . 190 139 73 LEU H H 6.429 0.0059 . 191 139 73 LEU CA C 55.559 0.46 . 192 139 73 LEU N N 118.454 0.14 . 193 140 74 ARG H H 8.523 0.0059 . 194 140 74 ARG CA C 52.963 0.46 . 195 140 74 ARG N N 117.45 0.14 . 196 141 75 ASP H H 7.718 0.0059 . 197 141 75 ASP CA C 52.321 0.46 . 198 141 75 ASP N N 118.832 0.14 . 199 142 76 PHE H H 7.837 0.0059 . 200 142 76 PHE CA C 58.876 0.46 . 201 142 76 PHE N N 115.81 0.14 . 202 143 77 ARG H H 7.804 0.0059 . 203 143 77 ARG CA C 55.1 0.46 . 204 143 77 ARG N N 120.63 0.14 . 205 144 78 GLY H H 8.291 0.0059 . 206 144 78 GLY CA C 44.968 0.46 . 207 144 78 GLY N N 112.741 0.14 . 208 145 79 ASN H H 8.605 0.0059 . 209 145 79 ASN CA C 53.386 0.46 . 210 145 79 ASN N N 119.518 0.14 . 211 147 81 PRO CA C 65.882 0.46 . 212 148 82 LEU H H 8.016 0.0059 . 213 148 82 LEU CA C 57.18 0.46 . 214 148 82 LEU N N 116.411 0.14 . 215 149 83 HIS H H 8.108 0.0059 . 216 149 83 HIS CA C 62.352 0.46 . 217 149 83 HIS N N 121.044 0.14 . 218 150 84 LEU H H 7.47 0.0059 . 219 150 84 LEU CA C 57.149 0.46 . 220 150 84 LEU N N 114.795 0.14 . 221 151 85 ALA H H 8.147 0.0059 . 222 151 85 ALA CA C 54.848 0.46 . 223 151 85 ALA N N 121.175 0.14 . 224 152 86 CYS H H 7.937 0.0059 . 225 152 86 CYS CA C 63.955 0.46 . 226 152 86 CYS N N 114.723 0.14 . 227 153 87 GLU H H 8.152 0.0059 . 228 153 87 GLU CA C 58.067 0.46 . 229 153 87 GLU N N 117.629 0.14 . 230 154 88 GLN CA C 55.863 0.46 . 231 155 89 GLY H H 7.302 0.0059 . 232 155 89 GLY CA C 44.608 0.46 . 233 155 89 GLY N N 108.567 0.14 . 234 156 90 CYS CA C 57.372 0.46 . 235 157 91 LEU H H 8.42 0.0059 . 236 157 91 LEU CA C 57.911 0.46 . 237 157 91 LEU N N 131.029 0.14 . 238 158 92 ALA H H 8.915 0.0059 . 239 158 92 ALA CA C 54.458 0.46 . 240 158 92 ALA N N 122.12 0.14 . 241 159 93 SER CA C 62.847 0.46 . 242 160 94 VAL H H 8.194 0.0059 . 243 160 94 VAL CA C 66.685 0.46 . 244 160 94 VAL N N 121.748 0.14 . 245 161 95 GLY H H 8.573 0.0059 . 246 161 95 GLY CA C 47.076 0.46 . 247 161 95 GLY N N 107.61 0.14 . 248 162 96 VAL H H 7.785 0.0059 . 249 162 96 VAL CA C 65.439 0.46 . 250 162 96 VAL N N 119.942 0.14 . 251 163 97 LEU H H 8.217 0.0059 . 252 163 97 LEU CA C 57.103 0.46 . 253 163 97 LEU N N 117.252 0.14 . 254 164 98 THR H H 7.656 0.0059 . 255 164 98 THR CA C 62.695 0.46 . 256 164 98 THR N N 104.329 0.14 . 257 165 99 GLN H H 8.054 0.0059 . 258 165 99 GLN CA C 56.87 0.46 . 259 165 99 GLN N N 119.837 0.14 . 260 166 100 SER CA C 58.605 0.46 . 261 167 101 CYS H H 7.248 0.0059 . 262 167 101 CYS CA C 56.989 0.46 . 263 167 101 CYS N N 116.864 0.14 . 264 168 102 THR CA C 61.444 0.46 . 265 169 103 THR H H 9.015 0.0059 . 266 169 103 THR CA C 67.456 0.46 . 267 169 103 THR N N 117.919 0.14 . 268 170 104 PRO CA C 65.611 0.46 . 269 171 105 HIS H H 7.295 0.0059 . 270 171 105 HIS CA C 58.074 0.46 . 271 171 105 HIS N N 115.574 0.14 . 272 172 106 LEU H H 8.592 0.0059 . 273 172 106 LEU CA C 57.559 0.46 . 274 172 106 LEU N N 121.725 0.14 . 275 173 107 HIS H H 8.338 0.0059 . 276 173 107 HIS CA C 58.731 0.46 . 277 173 107 HIS N N 115.576 0.14 . 278 174 108 SER H H 7.712 0.0059 . 279 174 108 SER CA C 60.905 0.46 . 280 174 108 SER N N 112.356 0.14 . 281 175 109 ILE H H 8.861 0.0059 . 282 175 109 ILE CA C 65.208 0.46 . 283 175 109 ILE N N 122.21 0.14 . 284 176 110 LEU H H 8.334 0.0059 . 285 176 110 LEU CA C 56.719 0.46 . 286 176 110 LEU N N 117.791 0.14 . 287 177 111 LYS H H 7.422 0.0059 . 288 177 111 LYS CA C 55.738 0.46 . 289 177 111 LYS N N 116.117 0.14 . 290 178 112 ALA H H 7.44 0.0059 . 291 178 112 ALA CA C 52.655 0.46 . 292 178 112 ALA N N 122.918 0.14 . 293 179 113 THR H H 9.114 0.0059 . 294 179 113 THR CA C 58.331 0.46 . 295 179 113 THR N N 113.181 0.14 . 296 180 114 ASN H H 8.173 0.0059 . 297 180 114 ASN CA C 50.427 0.46 . 298 180 114 ASN N N 121.478 0.14 . 299 181 115 TYR H H 8.009 0.0059 . 300 181 115 TYR CA C 57.415 0.46 . 301 181 115 TYR N N 116.411 0.14 . 302 182 116 ASN H H 7.692 0.0059 . 303 182 116 ASN CA C 52.573 0.46 . 304 182 116 ASN N N 117.245 0.14 . 305 183 117 GLY H H 8.252 0.0059 . 306 183 117 GLY CA C 44.87 0.46 . 307 183 117 GLY N N 106.542 0.14 . 308 184 118 HIS H H 7.587 0.0059 . 309 184 118 HIS CA C 54.661 0.46 . 310 184 118 HIS N N 116.518 0.14 . 311 185 119 THR CA C 59.618 0.46 . 312 186 120 CYS H H 9.666 0.0059 . 313 186 120 CYS CA C 64.312 0.46 . 314 186 120 CYS N N 119.945 0.14 . 315 187 121 LEU H H 8.395 0.0059 . 316 187 121 LEU CA C 57.841 0.46 . 317 187 121 LEU N N 121.461 0.14 . 318 188 122 HIS H H 7.955 0.0059 . 319 188 122 HIS CA C 60.492 0.46 . 320 188 122 HIS N N 121.531 0.14 . 321 189 123 LEU H H 8.017 0.0059 . 322 189 123 LEU CA C 57.69 0.46 . 323 189 123 LEU N N 116.34 0.14 . 324 190 124 ALA H H 8.261 0.0059 . 325 190 124 ALA CA C 54.47 0.46 . 326 190 124 ALA N N 118.389 0.14 . 327 192 126 ILE CA C 64.159 0.46 . 328 193 127 HIS H H 7.944 0.0059 . 329 193 127 HIS CA C 56.731 0.46 . 330 193 127 HIS N N 118.664 0.14 . 331 194 128 GLY H H 7.567 0.0059 . 332 194 128 GLY CA C 45.93 0.46 . 333 194 128 GLY N N 107.868 0.14 . 334 195 129 TYR H H 8.196 0.0059 . 335 195 129 TYR CA C 54.707 0.46 . 336 195 129 TYR N N 120.255 0.14 . 337 196 130 LEU H H 8.192 0.0059 . 338 196 130 LEU CA C 58.539 0.46 . 339 196 130 LEU N N 124.378 0.14 . 340 197 131 GLY H H 8.783 0.0059 . 341 197 131 GLY CA C 46.471 0.46 . 342 197 131 GLY N N 106.603 0.14 . 343 198 132 ILE H H 7.383 0.0059 . 344 198 132 ILE CA C 64.981 0.46 . 345 198 132 ILE N N 121.485 0.14 . 346 199 133 VAL H H 8.107 0.0059 . 347 199 133 VAL CA C 67.379 0.46 . 348 199 133 VAL N N 120.154 0.14 . 349 200 134 GLU H H 7.945 0.0059 . 350 200 134 GLU CA C 59.602 0.46 . 351 200 134 GLU N N 116.079 0.14 . 352 201 135 LEU H H 7.651 0.0059 . 353 201 135 LEU CA C 57.457 0.46 . 354 201 135 LEU N N 120.117 0.14 . 355 202 136 LEU H H 8.87 0.0059 . 356 202 136 LEU CA C 57.703 0.46 . 357 202 136 LEU N N 118.082 0.14 . 358 203 137 VAL CA C 66.61 0.46 . 359 204 138 SER H H 8.216 0.0059 . 360 204 138 SER CA C 61.495 0.46 . 361 204 138 SER N N 118.796 0.14 . 362 205 139 LEU H H 7.651 0.0059 . 363 205 139 LEU CA C 54.856 0.46 . 364 205 139 LEU N N 120.098 0.14 . 365 206 140 GLY H H 7.772 0.0059 . 366 206 140 GLY CA C 44.331 0.46 . 367 206 140 GLY N N 103.707 0.14 . 368 207 141 ALA H H 8.345 0.0059 . 369 207 141 ALA CA C 52.363 0.46 . 370 207 141 ALA N N 124.275 0.14 . 371 208 142 ASP H H 8.461 0.0059 . 372 208 142 ASP CA C 53.099 0.46 . 373 208 142 ASP N N 119.768 0.14 . 374 209 143 VAL H H 9.062 0.0059 . 375 209 143 VAL CA C 62.842 0.46 . 376 209 143 VAL N N 129.805 0.14 . 377 210 144 ASN H H 8.753 0.0059 . 378 210 144 ASN CA C 52.697 0.46 . 379 210 144 ASN N N 118.926 0.14 . 380 211 145 ALA H H 7.061 0.0059 . 381 211 145 ALA CA C 53.335 0.46 . 382 211 145 ALA N N 121.209 0.14 . 383 212 146 GLN H H 9.174 0.0059 . 384 212 146 GLN CA C 53.507 0.46 . 385 212 146 GLN N N 122.494 0.14 . 386 230 164 PRO CA C 67.34 0.46 . 387 231 165 ASP H H 7.967 0.0059 . 388 231 165 ASP CA C 56.89 0.46 . 389 231 165 ASP N N 119.117 0.14 . 390 232 166 LEU H H 7.526 0.0059 . 391 232 166 LEU CA C 56.31 0.46 . 392 232 166 LEU N N 122.33 0.14 . 393 233 167 VAL CA C 67.351 0.46 . 394 234 168 SER H H 8.069 0.0059 . 395 234 168 SER CA C 61.565 0.46 . 396 234 168 SER N N 111.472 0.14 . 397 235 169 LEU H H 7.789 0.0059 . 398 235 169 LEU CA C 57.159 0.46 . 399 235 169 LEU N N 122.179 0.14 . 400 237 171 LEU CA C 57.621 0.46 . 401 238 172 LYS H H 8.085 0.0059 . 402 238 172 LYS CA C 59.067 0.46 . 403 238 172 LYS N N 123.427 0.14 . 404 239 173 CYS H H 8.052 0.0059 . 405 239 173 CYS CA C 60.305 0.46 . 406 239 173 CYS N N 115.136 0.14 . 407 240 174 GLY H H 7.718 0.0059 . 408 240 174 GLY CA C 45.165 0.46 . 409 240 174 GLY N N 105.358 0.14 . 410 241 175 ALA H H 8.245 0.0059 . 411 241 175 ALA CA C 52.606 0.46 . 412 241 175 ALA N N 122.276 0.14 . 413 242 176 ASP H H 8.964 0.0059 . 414 242 176 ASP CA C 52.606 0.46 . 415 242 176 ASP N N 120.769 0.14 . 416 243 177 VAL H H 8.463 0.0059 . 417 243 177 VAL CA C 62.416 0.46 . 418 243 177 VAL N N 122.449 0.14 . 419 279 213 MET CA C 55.194 0.46 . 420 280 214 LEU H H 8.384 0.0059 . 421 280 214 LEU CA C 52.569 0.46 . 422 280 214 LEU N N 125.001 0.14 . 423 281 215 PRO CA C 62.546 0.46 . 424 282 216 GLU H H 8.555 0.0059 . 425 282 216 GLU CA C 56.056 0.46 . 426 282 216 GLU N N 121.015 0.14 . 427 283 217 SER H H 8.452 0.0059 . 428 283 217 SER CA C 57.732 0.46 . 429 283 217 SER N N 116.754 0.14 . 430 284 218 GLU H H 8.681 0.0059 . 431 284 218 GLU CA C 56.041 0.46 . 432 284 218 GLU N N 122.948 0.14 . 433 285 219 ASP H H 8.442 0.0059 . 434 285 219 ASP CA C 54.137 0.46 . 435 285 219 ASP N N 121.468 0.14 . 436 286 220 GLU H H 8.434 0.0059 . 437 286 220 GLU CA C 56.068 0.46 . 438 286 220 GLU N N 121.461 0.14 . 439 287 221 GLU H H 8.157 0.0059 . 440 287 221 GLU CA C 57.693 0.46 . 441 287 221 GLU N N 127.273 0.14 . stop_ save_