data_27996 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Chemical shift assignments of calcineurin catalytic subunit A residues 27-348 in complex with RCAN1 128-164 ; _BMRB_accession_number 27996 _BMRB_flat_file_name bmr27996.str _Entry_type original _Submission_date 2019-08-09 _Accession_date 2019-08-09 _Entry_origination author _NMR_STAR_version 2.1.1 _Experimental_method NMR _Details . loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Peti Wolfgang . . 2 Li Yang . . 3 Page Rebecca . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 111 "13C chemical shifts" 206 "15N chemical shifts" 111 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2020-09-24 update BMRB 'update entry citation' 2020-07-09 original author 'original release' stop_ loop_ _Related_BMRB_accession_number _Relationship 27994 'RCAN1 residues 89-197' 27995 'phosphorylated RCAN1 residues 89-197' 27997 'RCAN1 residues 128-164 in complex with calcineurin catalytic subunit A residues 27-348' stop_ _Original_release_date 2019-08-09 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; The structure of the RCAN1:CN complex explains the inhibition of and substrate recruitment by calcineurin ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 32936779 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Li Yang . . 2 Sheftic Sarah R. . 3 Grigoriu Simina . . 4 Schwieters Charles D. . 5 Page Rebecca . . 6 Peti Wolfgang . . stop_ _Journal_abbreviation 'Sci. Adv.' _Journal_name_full 'Science Advances' _Journal_volume 6 _Journal_issue 27 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 3681 _Page_last 3681 _Year 2020 _Details . save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name 'Calcineurin catalytic subunit A residues 27-348 in complex with RCAN1 residues 128-164' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label Calcineurin $Calcineurin_catalytic_subunit_A_residues_27-348 RCAN1 $RCAN1_residues_128-164 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_Calcineurin_catalytic_subunit_A_residues_27-348 _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'Calcineurin catalytic subunit A residues 27-348' _Molecular_mass . _Mol_thiol_state 'all free' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 327 _Mol_residue_sequence ; GHMHRLTAKEVFDNDGKPRV DILKAHLMKEGRLEESVALR IITEGASILRQEKNLLDIDA PVTVCGDIHGQFFDLMKLFE VGGSPANTRYLFLGDYVDRG YFSIECVLYLWALKILYPKT LFLLRGNHECRHLTEYFTFK QECKIKYSERVYDACMDAFD CLPLAALMNQQFLCVHGGLS PEINTLDDIRKLDRFKEPPA YGPMCDILWSDPLEDFGNEK TQEHFTHNTVRGCSYFYSYP AVCEFLQHNNLLSILRAHEA QDAGYRMYRKSQTTGFPSLI TIFSAPNYLDVYNNKAAVLK YENNVMNIRQFNCSPHPYWL PNFMDDD ; loop_ _Residue_seq_code _Residue_label 1 GLY 2 HIS 3 MET 4 HIS 5 ARG 6 LEU 7 THR 8 ALA 9 LYS 10 GLU 11 VAL 12 PHE 13 ASP 14 ASN 15 ASP 16 GLY 17 LYS 18 PRO 19 ARG 20 VAL 21 ASP 22 ILE 23 LEU 24 LYS 25 ALA 26 HIS 27 LEU 28 MET 29 LYS 30 GLU 31 GLY 32 ARG 33 LEU 34 GLU 35 GLU 36 SER 37 VAL 38 ALA 39 LEU 40 ARG 41 ILE 42 ILE 43 THR 44 GLU 45 GLY 46 ALA 47 SER 48 ILE 49 LEU 50 ARG 51 GLN 52 GLU 53 LYS 54 ASN 55 LEU 56 LEU 57 ASP 58 ILE 59 ASP 60 ALA 61 PRO 62 VAL 63 THR 64 VAL 65 CYS 66 GLY 67 ASP 68 ILE 69 HIS 70 GLY 71 GLN 72 PHE 73 PHE 74 ASP 75 LEU 76 MET 77 LYS 78 LEU 79 PHE 80 GLU 81 VAL 82 GLY 83 GLY 84 SER 85 PRO 86 ALA 87 ASN 88 THR 89 ARG 90 TYR 91 LEU 92 PHE 93 LEU 94 GLY 95 ASP 96 TYR 97 VAL 98 ASP 99 ARG 100 GLY 101 TYR 102 PHE 103 SER 104 ILE 105 GLU 106 CYS 107 VAL 108 LEU 109 TYR 110 LEU 111 TRP 112 ALA 113 LEU 114 LYS 115 ILE 116 LEU 117 TYR 118 PRO 119 LYS 120 THR 121 LEU 122 PHE 123 LEU 124 LEU 125 ARG 126 GLY 127 ASN 128 HIS 129 GLU 130 CYS 131 ARG 132 HIS 133 LEU 134 THR 135 GLU 136 TYR 137 PHE 138 THR 139 PHE 140 LYS 141 GLN 142 GLU 143 CYS 144 LYS 145 ILE 146 LYS 147 TYR 148 SER 149 GLU 150 ARG 151 VAL 152 TYR 153 ASP 154 ALA 155 CYS 156 MET 157 ASP 158 ALA 159 PHE 160 ASP 161 CYS 162 LEU 163 PRO 164 LEU 165 ALA 166 ALA 167 LEU 168 MET 169 ASN 170 GLN 171 GLN 172 PHE 173 LEU 174 CYS 175 VAL 176 HIS 177 GLY 178 GLY 179 LEU 180 SER 181 PRO 182 GLU 183 ILE 184 ASN 185 THR 186 LEU 187 ASP 188 ASP 189 ILE 190 ARG 191 LYS 192 LEU 193 ASP 194 ARG 195 PHE 196 LYS 197 GLU 198 PRO 199 PRO 200 ALA 201 TYR 202 GLY 203 PRO 204 MET 205 CYS 206 ASP 207 ILE 208 LEU 209 TRP 210 SER 211 ASP 212 PRO 213 LEU 214 GLU 215 ASP 216 PHE 217 GLY 218 ASN 219 GLU 220 LYS 221 THR 222 GLN 223 GLU 224 HIS 225 PHE 226 THR 227 HIS 228 ASN 229 THR 230 VAL 231 ARG 232 GLY 233 CYS 234 SER 235 TYR 236 PHE 237 TYR 238 SER 239 TYR 240 PRO 241 ALA 242 VAL 243 CYS 244 GLU 245 PHE 246 LEU 247 GLN 248 HIS 249 ASN 250 ASN 251 LEU 252 LEU 253 SER 254 ILE 255 LEU 256 ARG 257 ALA 258 HIS 259 GLU 260 ALA 261 GLN 262 ASP 263 ALA 264 GLY 265 TYR 266 ARG 267 MET 268 TYR 269 ARG 270 LYS 271 SER 272 GLN 273 THR 274 THR 275 GLY 276 PHE 277 PRO 278 SER 279 LEU 280 ILE 281 THR 282 ILE 283 PHE 284 SER 285 ALA 286 PRO 287 ASN 288 TYR 289 LEU 290 ASP 291 VAL 292 TYR 293 ASN 294 ASN 295 LYS 296 ALA 297 ALA 298 VAL 299 LEU 300 LYS 301 TYR 302 GLU 303 ASN 304 ASN 305 VAL 306 MET 307 ASN 308 ILE 309 ARG 310 GLN 311 PHE 312 ASN 313 CYS 314 SER 315 PRO 316 HIS 317 PRO 318 TYR 319 TRP 320 LEU 321 PRO 322 ASN 323 PHE 324 MET 325 ASP 326 ASP 327 ASP 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 Q08209 . . . . . . UNP P53805-2 . . . . . . stop_ save_ save_RCAN1_residues_128-164 _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'RCAN1 residues 128-164' _Molecular_mass . _Mol_thiol_state 'all free' _Details . _Residue_count 40 _Mol_residue_sequence ; GHMNYDLLYAISKLGPGEKY ELHAATDTTPSVVITVCESD ; loop_ _Residue_seq_code _Residue_label 1 GLY 2 HIS 3 MET 4 ASN 5 TYR 6 ASP 7 LEU 8 LEU 9 TYR 10 ALA 11 ILE 12 SER 13 LYS 14 LEU 15 GLY 16 PRO 17 GLY 18 GLU 19 LYS 20 TYR 21 GLU 22 LEU 23 HIS 24 ALA 25 ALA 26 THR 27 ASP 28 THR 29 THR 30 PRO 31 SER 32 VAL 33 VAL 34 ILE 35 THR 36 VAL 37 CYS 38 GLU 39 SER 40 ASP 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 P53805-2 RCAN1 . . . . . stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $Calcineurin_catalytic_subunit_A_residues_27-348 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 $Calcineurin_catalytic_subunit_A_residues_27-348 'recombinant technology' . Escherichia coli . RP1B stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $Calcineurin_catalytic_subunit_A_residues_27-348 0.13 mM '[U-13C; U-15N; U-2H]' $RCAN1_residues_128-164 0.65 mM 'natural abundance' 'sodium phosphate' 20 mM 'natural abundance' 'sodium chloride' 50 mM 'natural abundance' TCEP 0.5 mM 'natural abundance' stop_ save_ ############################ # Computer software used # ############################ save_TOPSPIN _Saveframe_category software _Name TOPSPIN _Version . loop_ _Vendor _Address _Electronic_address 'Bruker Biospin' . . stop_ loop_ _Task collection processing stop_ _Details . save_ save_CARA _Saveframe_category software _Name CARA _Version . loop_ _Vendor _Address _Electronic_address 'Keller and Wuthrich' . . stop_ loop_ _Task 'chemical shift assignment' stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model Avance _Field_strength 850 _Details 'equipped with a 5 mm TCI HCN z-gradient cryoprobe' save_ ############################# # NMR applied experiments # ############################# save_2D_1H-15N_TROSY_1 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-15N TROSY' _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_HN(CO)CA_4 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HN(CO)CA' _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' 50 . mM pH 6.8 . pH pressure 1 . atm temperature 298 . K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference_1 _Saveframe_category chemical_shift_reference _Details . loop_ _Mol_common_name _Atom_type _Atom_isotope_number _Atom_group _Chem_shift_units _Chem_shift_value _Reference_method _Reference_type _External_reference_sample_geometry _External_reference_location _External_reference_axis _Indirect_shift_ratio DSS C 13 'methyl protons' ppm 0.00 na indirect . . . 0.251449530 DSS H 1 'methyl protons' ppm 0.00 internal direct . . . 1.000000000 DSS N 15 'methyl protons' ppm 0.00 na indirect . . . 0.101329118 stop_ save_ ################################### # Assigned chemical shift lists # ################################### ################################################################### # Chemical Shift Ambiguity Index Value Definitions # # # # The values other than 1 are used for those atoms with different # # chemical shifts that cannot be assigned to stereospecific atoms # # or to specific residues or chains. # # # # Index Value Definition # # # # 1 Unique (including isolated methyl protons, # # geminal atoms, and geminal methyl # # groups with identical chemical shifts) # # (e.g. ILE HD11, HD12, HD13 protons) # # 2 Ambiguity of geminal atoms or geminal methyl # # proton groups (e.g. ASP HB2 and HB3 # # protons, LEU CD1 and CD2 carbons, or # # LEU HD11, HD12, HD13 and HD21, HD22, # # HD23 methyl protons) # # 3 Aromatic atoms on opposite sides of # # symmetrical rings (e.g. TYR HE1 and HE2 # # protons) # # 4 Intraresidue ambiguities (e.g. LYS HG and # # HD protons or TRP HZ2 and HZ3 protons) # # 5 Interresidue ambiguities (LYS 12 vs. LYS 27) # # 6 Intermolecular ambiguities (e.g. ASP 31 CA # # in monomer 1 and ASP 31 CA in monomer 2 # # of an asymmetrical homodimer, duplex # # DNA assignments, or other assignments # # that may apply to atoms in one or more # # molecule in the molecular assembly) # # 9 Ambiguous, specific ambiguity not defined # # # ################################################################### save_assigned_chem_shift_list_1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Experiment_label '2D 1H-15N TROSY' '3D HNCA' '3D HNCACB' '3D HN(CO)CA' 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 Calcineurin _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 5 5 ARG H H 8.399 0.020 1 2 5 5 ARG CA C 55.244 0.3 1 3 5 5 ARG CB C 30.387 0.3 1 4 5 5 ARG N N 125.854 0.2 1 5 6 6 LEU H H 7.126 0.020 1 6 6 6 LEU CA C 56.102 0.3 1 7 6 6 LEU CB C 42.511 0.3 1 8 6 6 LEU N N 121.157 0.2 1 9 7 7 THR H H 8.39 0.020 1 10 7 7 THR CA C 61.15 0.3 1 11 7 7 THR CB C 73.007 0.3 1 12 7 7 THR N N 113.202 0.2 1 13 8 8 ALA H H 9.124 0.020 1 14 8 8 ALA CA C 56.596 0.3 1 15 8 8 ALA CB C 17.864 0.3 1 16 8 8 ALA N N 123.571 0.2 1 17 9 9 LYS H H 7.954 0.020 1 18 9 9 LYS CA C 58.537 0.3 1 19 9 9 LYS CB C 31.669 0.3 1 20 9 9 LYS N N 115.921 0.2 1 21 10 10 GLU H H 7.15 0.020 1 22 10 10 GLU CA C 58.29 0.3 1 23 10 10 GLU CB C 31.477 0.3 1 24 10 10 GLU N N 116.067 0.2 1 25 11 11 VAL H H 7.416 0.020 1 26 11 11 VAL CA C 64.657 0.3 1 27 11 11 VAL CB C 33.784 0.3 1 28 11 11 VAL N N 116.341 0.2 1 29 12 12 PHE H H 8.054 0.020 1 30 12 12 PHE CA C 57.632 0.3 1 31 12 12 PHE CB C 40.898 0.3 1 32 12 12 PHE N N 117.689 0.2 1 33 13 13 ASP H H 8.754 0.020 1 34 13 13 ASP CA C 52.889 0.3 1 35 13 13 ASP CB C 41.07 0.3 1 36 13 13 ASP N N 122.215 0.2 1 37 15 15 ASP H H 8.157 0.020 1 38 15 15 ASP CA C 54.59 0.3 1 39 15 15 ASP CB C 41.79 0.3 1 40 15 15 ASP N N 118.636 0.2 1 41 16 16 GLY H H 8.085 0.020 1 42 16 16 GLY CA C 45.611 0.3 1 43 16 16 GLY N N 108.545 0.2 1 44 17 17 LYS H H 8.384 0.020 1 45 17 17 LYS CA C 53.788 0.3 1 46 17 17 LYS CB C 31.124 0.3 1 47 17 17 LYS N N 121.932 0.2 1 48 19 19 ARG H H 8.734 0.020 1 49 19 19 ARG CA C 55.022 0.3 1 50 19 19 ARG CB C 27.953 0.3 1 51 19 19 ARG N N 123.346 0.2 1 52 20 20 VAL H H 7.526 0.020 1 53 20 20 VAL CA C 66.502 0.3 1 54 20 20 VAL CB C 30.98 0.3 1 55 20 20 VAL N N 120.056 0.2 1 56 21 21 ASP H H 8.971 0.020 1 57 21 21 ASP CA C 57.398 0.3 1 58 21 21 ASP CB C 38.691 0.3 1 59 21 21 ASP N N 121.674 0.2 1 60 22 22 ILE H H 7.116 0.020 1 61 22 22 ILE CA C 62.517 0.3 1 62 22 22 ILE CB C 36.412 0.3 1 63 22 22 ILE N N 123.814 0.2 1 64 23 23 LEU H H 7.819 0.020 1 65 23 23 LEU CA C 58.756 0.3 1 66 23 23 LEU CB C 42.511 0.3 1 67 23 23 LEU N N 119.373 0.2 1 68 24 24 LYS H H 8.608 0.020 1 69 24 24 LYS CA C 61.309 0.3 1 70 24 24 LYS CB C 32.566 0.3 1 71 24 24 LYS N N 118.791 0.2 1 72 25 25 ALA H H 7.244 0.020 1 73 25 25 ALA CA C 55.19 0.3 1 74 25 25 ALA CB C 17.826 0.3 1 75 25 25 ALA N N 117.672 0.2 1 76 26 26 HIS H H 7.854 0.020 1 77 26 26 HIS CA C 60.019 0.3 1 78 26 26 HIS CB C 36.988 0.3 1 79 26 26 HIS N N 116.959 0.2 1 80 28 28 MET H H 8.223 0.020 1 81 28 28 MET CA C 59.278 0.3 1 82 28 28 MET CB C 37.95 0.3 1 83 28 28 MET N N 116.077 0.2 1 84 29 29 LYS H H 6.91 0.020 1 85 29 29 LYS CA C 55.719 0.3 1 86 29 29 LYS CB C 31.553 0.3 1 87 29 29 LYS N N 117.484 0.2 1 88 31 31 GLY H H 7.781 0.020 1 89 31 31 GLY CA C 44.324 0.3 1 90 31 31 GLY N N 106.174 0.2 1 91 32 32 ARG H H 8.821 0.020 1 92 32 32 ARG CA C 54.092 0.3 1 93 32 32 ARG CB C 33.079 0.3 1 94 32 32 ARG N N 118.115 0.2 1 95 33 33 LEU H H 8.341 0.020 1 96 33 33 LEU CA C 54.096 0.3 1 97 33 33 LEU CB C 42.583 0.3 1 98 33 33 LEU N N 121.37 0.2 1 99 34 34 GLU H H 8.606 0.020 1 100 34 34 GLU CA C 58.818 0.3 1 101 34 34 GLU CB C 29.467 0.3 1 102 34 34 GLU N N 122.72 0.2 1 103 35 35 GLU H H 9.295 0.020 1 104 35 35 GLU CA C 62.242 0.3 1 105 35 35 GLU CB C 29.426 0.3 1 106 35 35 GLU N N 127.996 0.2 1 107 36 36 SER H H 8.837 0.020 1 108 36 36 SER CA C 62.023 0.3 1 109 36 36 SER N N 111.942 0.2 1 110 37 37 VAL H H 7.101 0.020 1 111 37 37 VAL CA C 65.957 0.3 1 112 37 37 VAL CB C 31.028 0.3 1 113 37 37 VAL N N 125.038 0.2 1 114 38 38 ALA H H 6.686 0.020 1 115 38 38 ALA CA C 55.454 0.3 1 116 38 38 ALA CB C 18.368 0.3 1 117 38 38 ALA N N 118.801 0.2 1 118 47 47 SER H H 7.813 0.020 1 119 47 47 SER CA C 62.113 0.3 1 120 47 47 SER CB C 63.285 0.3 1 121 47 47 SER N N 112.535 0.2 1 122 48 48 ILE H H 7.021 0.020 1 123 48 48 ILE CA C 65.102 0.3 1 124 48 48 ILE CB C 38.545 0.3 1 125 48 48 ILE N N 122.2 0.2 1 126 51 51 GLN H H 6.984 0.020 1 127 51 51 GLN CA C 56.04 0.3 1 128 51 51 GLN CB C 29.682 0.3 1 129 51 51 GLN N N 111.839 0.2 1 130 53 53 LYS H H 8.331 0.020 1 131 53 53 LYS CA C 56.195 0.3 1 132 53 53 LYS CB C 33.286 0.3 1 133 53 53 LYS N N 122.401 0.2 1 134 54 54 ASN H H 7.874 0.020 1 135 54 54 ASN CA C 57.33 0.3 1 136 54 54 ASN CB C 40.065 0.3 1 137 54 54 ASN N N 112.826 0.2 1 138 55 55 LEU H H 7.408 0.020 1 139 55 55 LEU CA C 52.225 0.3 1 140 55 55 LEU CB C 44.116 0.3 1 141 55 55 LEU N N 116.337 0.2 1 142 57 57 ASP H H 8.09 0.020 1 143 57 57 ASP CA C 54.868 0.3 1 144 57 57 ASP CB C 42.223 0.3 1 145 57 57 ASP N N 121.879 0.2 1 146 58 58 ILE H H 7.989 0.020 1 147 58 58 ILE CA C 59.558 0.3 1 148 58 58 ILE CB C 41.358 0.3 1 149 58 58 ILE N N 122.511 0.2 1 150 59 59 ASP H H 8.254 0.020 1 151 59 59 ASP CA C 54.556 0.3 1 152 59 59 ASP CB C 41.806 0.3 1 153 59 59 ASP N N 128.063 0.2 1 154 60 60 ALA H H 7.875 0.020 1 155 60 60 ALA CA C 55.114 0.3 1 156 60 60 ALA CB C 17.576 0.3 1 157 60 60 ALA N N 120.194 0.2 1 158 62 62 VAL H H 8.35 0.020 1 159 62 62 VAL CA C 61.225 0.3 1 160 62 62 VAL CB C 33.719 0.3 1 161 62 62 VAL N N 120.422 0.2 1 162 79 79 PHE H H 7.194 0.020 1 163 79 79 PHE CA C 61.657 0.3 1 164 79 79 PHE CB C 38.947 0.3 1 165 79 79 PHE N N 115.814 0.2 1 166 80 80 GLU H H 7.404 0.020 1 167 80 80 GLU CA C 59.713 0.3 1 168 80 80 GLU CB C 29.106 0.3 1 169 80 80 GLU N N 121.365 0.2 1 170 81 81 VAL H H 7.736 0.020 1 171 81 81 VAL CA C 65.051 0.3 1 172 81 81 VAL CB C 31.629 0.3 1 173 81 81 VAL N N 119.068 0.2 1 174 82 82 GLY H H 9.073 0.020 1 175 82 82 GLY CA C 47.011 0.3 1 176 82 82 GLY N N 106.916 0.2 1 177 83 83 GLY H H 7.251 0.020 1 178 83 83 GLY CA C 43.462 0.3 1 179 83 83 GLY N N 107.852 0.2 1 180 84 84 SER H H 8.537 0.020 1 181 84 84 SER CA C 56.452 0.3 1 182 84 84 SER CB C 63.842 0.3 1 183 84 84 SER N N 117.065 0.2 1 184 86 86 ALA H H 7.436 0.020 1 185 86 86 ALA CA C 54.621 0.3 1 186 86 86 ALA CB C 18.44 0.3 1 187 86 86 ALA N N 118.017 0.2 1 188 87 87 ASN H H 7.386 0.020 1 189 87 87 ASN CA C 52.69 0.3 1 190 87 87 ASN CB C 40.001 0.3 1 191 87 87 ASN N N 111.021 0.2 1 192 88 88 THR H H 7.1 0.020 1 193 88 88 THR CA C 62.953 0.3 1 194 88 88 THR CB C 71.482 0.3 1 195 88 88 THR N N 117.913 0.2 1 196 89 89 ARG H H 8.535 0.020 1 197 89 89 ARG CA C 56.087 0.3 1 198 89 89 ARG CB C 31.028 0.3 1 199 89 89 ARG N N 126.811 0.2 1 200 90 90 TYR H H 7.009 0.020 1 201 90 90 TYR CA C 60.669 0.3 1 202 90 90 TYR CB C 38.655 0.3 1 203 90 90 TYR N N 119.179 0.2 1 204 91 91 LEU H H 9.617 0.020 1 205 91 91 LEU CA C 54.613 0.3 1 206 91 91 LEU CB C 42.052 0.3 1 207 91 91 LEU N N 124.925 0.2 1 208 119 119 LYS H H 8.341 0.020 1 209 119 119 LYS CA C 55.766 0.3 1 210 119 119 LYS CB C 32.502 0.3 1 211 119 119 LYS N N 114.978 0.2 1 212 120 120 THR H H 7.075 0.020 1 213 120 120 THR CA C 62.811 0.3 1 214 120 120 THR CB C 70.051 0.3 1 215 120 120 THR N N 106.59 0.2 1 216 149 149 GLU H H 8.835 0.020 1 217 149 149 GLU CA C 60.574 0.3 1 218 149 149 GLU CB C 28.4 0.3 1 219 149 149 GLU N N 124.756 0.2 1 220 150 150 ARG H H 8.031 0.020 1 221 150 150 ARG CA C 59.898 0.3 1 222 150 150 ARG CB C 29.323 0.3 1 223 150 150 ARG N N 119.058 0.2 1 224 151 151 VAL H H 7.197 0.020 1 225 151 151 VAL CA C 66.78 0.3 1 226 151 151 VAL CB C 31.413 0.3 1 227 151 151 VAL N N 119.804 0.2 1 228 152 152 TYR H H 6.929 0.020 1 229 152 152 TYR CA C 63.262 0.3 1 230 152 152 TYR CB C 37.106 0.3 1 231 152 152 TYR N N 121.36 0.2 1 232 153 153 ASP H H 8.7 0.020 1 233 153 153 ASP CA C 58.046 0.3 1 234 153 153 ASP CB C 39.845 0.3 1 235 153 153 ASP N N 120.577 0.2 1 236 154 154 ALA H H 7.555 0.020 1 237 154 154 ALA CA C 55.189 0.3 1 238 154 154 ALA CB C 17.569 0.3 1 239 154 154 ALA N N 121.68 0.2 1 240 169 169 ASN H H 9.92 0.020 1 241 169 169 ASN CA C 54.87 0.3 1 242 169 169 ASN CB C 41.411 0.3 1 243 169 169 ASN N N 131.833 0.2 1 244 170 170 GLN H H 8.765 0.020 1 245 170 170 GLN CA C 58.949 0.3 1 246 170 170 GLN CB C 27.23 0.3 1 247 170 170 GLN N N 109.012 0.2 1 248 171 171 GLN H H 7.781 0.020 1 249 171 171 GLN CA C 57.687 0.3 1 250 171 171 GLN CB C 34.169 0.3 1 251 171 171 GLN N N 115.073 0.2 1 252 186 186 LEU H H 7.256 0.020 1 253 186 186 LEU CA C 58.386 0.3 1 254 186 186 LEU CB C 39.917 0.3 1 255 186 186 LEU N N 117.897 0.2 1 256 187 187 ASP H H 8.048 0.020 1 257 187 187 ASP CA C 58.262 0.3 1 258 187 187 ASP CB C 40.421 0.3 1 259 187 187 ASP N N 119.701 0.2 1 260 188 188 ASP H H 7.57 0.020 1 261 188 188 ASP CA C 58.17 0.3 1 262 188 188 ASP CB C 41.43 0.3 1 263 188 188 ASP N N 118.472 0.2 1 264 189 189 ILE H H 7.233 0.020 1 265 189 189 ILE CA C 64.685 0.3 1 266 189 189 ILE CB C 38.719 0.3 1 267 189 189 ILE N N 116.338 0.2 1 268 190 190 ARG H H 7.422 0.020 1 269 190 190 ARG CA C 60.638 0.3 1 270 190 190 ARG CB C 29.251 0.3 1 271 190 190 ARG N N 119.13 0.2 1 272 191 191 LYS H H 7.274 0.020 1 273 191 191 LYS CA C 57.577 0.3 1 274 191 191 LYS CB C 32.694 0.3 1 275 191 191 LYS N N 113.294 0.2 1 276 192 192 LEU H H 6.58 0.020 1 277 192 192 LEU CA C 55.879 0.3 1 278 192 192 LEU CB C 41.618 0.3 1 279 192 192 LEU N N 117.802 0.2 1 280 194 194 ARG H H 8.298 0.020 1 281 194 194 ARG CA C 55.793 0.3 1 282 194 194 ARG CB C 30.98 0.3 1 283 194 194 ARG N N 123.775 0.2 1 284 195 195 PHE H H 7.222 0.020 1 285 195 195 PHE CA C 56.42 0.3 1 286 195 195 PHE CB C 36.529 0.3 1 287 195 195 PHE N N 120.313 0.2 1 288 200 200 ALA H H 8.242 0.020 1 289 200 200 ALA CA C 53.386 0.3 1 290 200 200 ALA CB C 18.224 0.3 1 291 200 200 ALA N N 120.095 0.2 1 292 201 201 TYR H H 6.89 0.020 1 293 201 201 TYR CA C 55.962 0.3 1 294 201 201 TYR CB C 40.156 0.3 1 295 201 201 TYR N N 111.201 0.2 1 296 202 202 GLY H H 8.938 0.020 1 297 202 202 GLY CA C 44.921 0.3 1 298 202 202 GLY N N 111.445 0.2 1 299 216 216 PHE H H 6.992 0.020 1 300 216 216 PHE N N 119.166 0.2 1 301 217 217 GLY H H 9.56 0.020 1 302 217 217 GLY CA C 45.833 0.3 1 303 217 217 GLY N N 123.459 0.2 1 304 218 218 ASN H H 8.505 0.020 1 305 218 218 ASN CA C 52.461 0.3 1 306 218 218 ASN CB C 39.773 0.3 1 307 218 218 ASN N N 121.127 0.2 1 308 219 219 GLU H H 9.27 0.020 1 309 219 219 GLU CA C 60.176 0.3 1 310 219 219 GLU CB C 29.611 0.3 1 311 219 219 GLU N N 121.583 0.2 1 312 220 220 LYS H H 8.864 0.020 1 313 220 220 LYS CA C 56.925 0.3 1 314 220 220 LYS CB C 32.71 0.3 1 315 220 220 LYS N N 120.623 0.2 1 316 221 221 THR H H 7.387 0.020 1 317 221 221 THR CA C 60.628 0.3 1 318 221 221 THR CB C 70.227 0.3 1 319 221 221 THR N N 110.909 0.2 1 320 247 247 GLN H H 7.926 0.020 1 321 247 247 GLN CA C 59.031 0.3 1 322 247 247 GLN CB C 27.952 0.3 1 323 247 247 GLN N N 117.602 0.2 1 324 248 248 HIS H H 8.261 0.020 1 325 248 248 HIS CA C 58.263 0.3 1 326 248 248 HIS CB C 29.426 0.3 1 327 248 248 HIS N N 117.064 0.2 1 328 249 249 ASN H H 7.035 0.020 1 329 249 249 ASN CA C 53.844 0.3 1 330 249 249 ASN CB C 40.577 0.3 1 331 249 249 ASN N N 111.633 0.2 1 332 250 250 ASN H H 7.43 0.020 1 333 250 250 ASN CA C 54.713 0.3 1 334 250 250 ASN CB C 37.106 0.3 1 335 250 250 ASN N N 117.705 0.2 1 336 254 254 ILE H H 9.161 0.020 1 337 254 254 ILE CA C 62.946 0.3 1 338 254 254 ILE N N 123.052 0.2 1 339 269 269 ARG H H 8.005 0.020 1 340 269 269 ARG CA C 57.83 0.3 1 341 269 269 ARG CB C 30.318 0.3 1 342 269 269 ARG N N 117.759 0.2 1 343 270 270 LYS H H 8.688 0.020 1 344 270 270 LYS CA C 57.369 0.3 1 345 270 270 LYS CB C 32.054 0.3 1 346 270 270 LYS N N 127.754 0.2 1 347 271 271 SER H H 8.416 0.020 1 348 271 271 SER CA C 58.787 0.3 1 349 271 271 SER N N 119.992 0.2 1 350 273 273 THR H H 7.188 0.020 1 351 273 273 THR CA C 62.078 0.3 1 352 273 273 THR CB C 71.393 0.3 1 353 273 273 THR N N 107.961 0.2 1 354 274 274 THR H H 7.103 0.020 1 355 274 274 THR CA C 57.632 0.3 1 356 274 274 THR CB C 66.149 0.3 1 357 274 274 THR N N 114.576 0.2 1 358 275 275 GLY H H 7.652 0.020 1 359 275 275 GLY CA C 46.627 0.3 1 360 275 275 GLY N N 110.583 0.2 1 361 276 276 PHE H H 8.167 0.020 1 362 276 276 PHE CA C 56.781 0.3 1 363 276 276 PHE CB C 43.304 0.3 1 364 276 276 PHE N N 122.296 0.2 1 365 278 278 SER H H 8.044 0.020 1 366 278 278 SER CA C 64.419 0.3 1 367 278 278 SER CB C 69.097 0.3 1 368 278 278 SER N N 110.991 0.2 1 369 301 301 TYR H H 8.751 0.020 1 370 301 301 TYR CA C 55.217 0.3 1 371 301 301 TYR N N 128.591 0.2 1 372 302 302 GLU H H 8.151 0.020 1 373 302 302 GLU CA C 55.793 0.3 1 374 302 302 GLU CB C 31.989 0.3 1 375 302 302 GLU N N 124.923 0.2 1 376 303 303 ASN H H 9.516 0.020 1 377 303 303 ASN CA C 55.08 0.3 1 378 303 303 ASN CB C 37.373 0.3 1 379 303 303 ASN N N 124.401 0.2 1 380 304 304 ASN H H 8.44 0.020 1 381 304 304 ASN CA C 55.272 0.3 1 382 304 304 ASN N N 111.526 0.2 1 383 305 305 VAL H H 7.647 0.020 1 384 305 305 VAL CA C 62.274 0.3 1 385 305 305 VAL CB C 35.16 0.3 1 386 305 305 VAL N N 119.162 0.2 1 387 306 306 MET H H 8.583 0.020 1 388 306 306 MET CA C 55.244 0.3 1 389 306 306 MET N N 124.826 0.2 1 390 307 307 ASN H H 8.985 0.020 1 391 307 307 ASN CA C 51.21 0.3 1 392 307 307 ASN CB C 40.321 0.3 1 393 307 307 ASN N N 124.616 0.2 1 394 308 308 ILE H H 9.01 0.020 1 395 308 308 ILE CA C 62.023 0.3 1 396 308 308 ILE CB C 37.886 0.3 1 397 308 308 ILE N N 129.739 0.2 1 398 309 309 ARG H H 9.236 0.020 1 399 309 309 ARG CA C 55.573 0.3 1 400 309 309 ARG CB C 34.745 0.3 1 401 309 309 ARG N N 126.967 0.2 1 402 310 310 GLN H H 9.299 0.020 1 403 310 310 GLN CA C 55.903 0.3 1 404 310 310 GLN CB C 33.784 0.3 1 405 310 310 GLN N N 131.835 0.2 1 406 311 311 PHE H H 8.962 0.020 1 407 311 311 PHE CA C 57.632 0.3 1 408 311 311 PHE CB C 41.218 0.3 1 409 311 311 PHE N N 117.179 0.2 1 410 312 312 ASN H H 8.597 0.020 1 411 312 312 ASN CA C 51.704 0.3 1 412 312 312 ASN N N 118.008 0.2 1 413 313 313 CYS H H 8.196 0.020 1 414 313 313 CYS CA C 57.577 0.3 1 415 313 313 CYS CB C 29.618 0.3 1 416 313 313 CYS N N 115.073 0.2 1 417 314 314 SER H H 8.735 0.020 1 418 314 314 SER CA C 57.549 0.3 1 419 314 314 SER CB C 63.971 0.3 1 420 314 314 SER N N 118.795 0.2 1 421 326 326 ASP H H 8.118 0.020 1 422 326 326 ASP CA C 54.868 0.3 1 423 326 326 ASP CB C 41.43 0.3 1 424 326 326 ASP N N 121.057 0.2 1 425 327 327 ASP H H 7.816 0.020 1 426 327 327 ASP CA C 56.215 0.3 1 427 327 327 ASP CB C 42.244 0.3 1 428 327 327 ASP N N 126.063 0.2 1 stop_ save_