data_27404 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; 1H, 15N, 13C backbone resonance assignments of the nuclease core residues 2-336 of K93A human flap endonuclease-1 in complex with dual-hairpin DNA substrate ; _BMRB_accession_number 27404 _BMRB_flat_file_name bmr27404.str _Entry_type original _Submission_date 2018-02-15 _Accession_date 2018-02-15 _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 Bennet Ian A. . 2 Baxter Nicola J. . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 132 "13C chemical shifts" 280 "15N chemical shifts" 132 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2018-11-14 update BMRB 'update entry citation' 2018-05-22 original author 'original release' stop_ loop_ _Related_BMRB_accession_number _Relationship 27160 '1H, 15N, 13C backbone resonance assignments of the nuclease core residues 2-336 of wild-type human flap endonuclease-1.' 27403 '1H, 15N, 13C backbone resonance assignments of the nuclease core residues 2-336 of P188A human flap endonuclease-1' stop_ _Original_release_date 2018-02-15 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; Regional conformational flexibility couples substrate specificity and scissile phosphate diester selectivity in human flap endonuclease 1 ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 29718417 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Bennet Ian A. . 2 Finger 'L David' D. . 3 Baxter Nicola J. . 4 Ambrose Benjamin . . 5 Hounslow Andrea M. . 6 Thompson Mark J. . 7 Exell Jack C. . 8 Shahari 'Nur Nazihah' . . 9 Craggs Timothy D. . 10 Waltho Jonathan P. . 11 Grasby Jane A. . stop_ _Journal_abbreviation 'Nucleic Acids Res.' _Journal_name_full 'Nucleic acids research' _Journal_volume 46 _Journal_issue 11 _Journal_ISSN 1362-4962 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 5618 _Page_last 5633 _Year 2018 _Details . loop_ _Keyword Catalysis 'DNA replication / repair' 'Flap endonuclease 1' 'NMR spectroscopy' 'Protein dynamics' stop_ save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name hFEN1-336-K93A-DNA _Enzyme_commission_number 'EC 3.1.-.-' loop_ _Mol_system_component_name _Mol_label hFEN1-336-K93A-DNA $hFEN1-K93A 'Calcium ion' $entity_CA 'dual-hairpin DNA substrate' $dual-hairpin_DNA_substrate stop_ _System_molecular_weight 51091.44 _System_physical_state native _System_oligomer_state ? _System_paramagnetic no _System_thiol_state . _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_hFEN1-K93A _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common hFEN1-K93A _Molecular_mass 38400.08 _Mol_thiol_state 'all free' loop_ _Biological_function ; Flap endonuclease hydrolyses the phosphodiester of a 5' DNA sequence from a structure called a DNA flap. The DNA flap structure occurs in double-stranded DNA containing a single-stranded break where the 5' portion of the downstream strand is too long and overlaps the 3' end of the upstream strand. Flap endonucleases cleave the downstream strand of the overlap flap structure precisely after the first base-paired nucleotide, creating a ligatable nick." ; stop_ _Details ; The final 6 residues at the C-terminus (LEVLFQ) represent the cleavage recognition site for the human rhinovirus type 14 3C protease. ; ############################## # Polymer residue sequence # ############################## _Residue_count 341 _Mol_residue_sequence ; GIQGLAKLIADVAPSAIREN DIKSYFGRKVAIDASMSIYQ FLIAVRQGGDVLQNEEGETT SHLMGMFYRTIRMMENGIKP VYVFDGKPPQLASGELAKRS ERRAEAEKQLQQAQAAGAEQ EVEKFTKRLVKVTKQHNDEC KHLLSLMGIPYLDAPSEAEA SCAALVKAGKVYAAATEDMD CLTFGSPVLMRHLTASEAKK LPIQEFHLSRILQELGLNQE QFVDLCILLGSDYCESIRGI GPKRAVDLIQKHKSIEEIVR RLDPNKYPVPENWLHKEAHQ LFLEPEVLDPESVELKWSEP NEEELIKFMCGEKQFSEERI RSGVKRLSKSRQGSTLEVLF Q ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 2 GLY 2 3 ILE 3 4 GLN 4 5 GLY 5 6 LEU 6 7 ALA 7 8 LYS 8 9 LEU 9 10 ILE 10 11 ALA 11 12 ASP 12 13 VAL 13 14 ALA 14 15 PRO 15 16 SER 16 17 ALA 17 18 ILE 18 19 ARG 19 20 GLU 20 21 ASN 21 22 ASP 22 23 ILE 23 24 LYS 24 25 SER 25 26 TYR 26 27 PHE 27 28 GLY 28 29 ARG 29 30 LYS 30 31 VAL 31 32 ALA 32 33 ILE 33 34 ASP 34 35 ALA 35 36 SER 36 37 MET 37 38 SER 38 39 ILE 39 40 TYR 40 41 GLN 41 42 PHE 42 43 LEU 43 44 ILE 44 45 ALA 45 46 VAL 46 47 ARG 47 48 GLN 48 49 GLY 49 50 GLY 50 51 ASP 51 52 VAL 52 53 LEU 53 54 GLN 54 55 ASN 55 56 GLU 56 57 GLU 57 58 GLY 58 59 GLU 59 60 THR 60 61 THR 61 62 SER 62 63 HIS 63 64 LEU 64 65 MET 65 66 GLY 66 67 MET 67 68 PHE 68 69 TYR 69 70 ARG 70 71 THR 71 72 ILE 72 73 ARG 73 74 MET 74 75 MET 75 76 GLU 76 77 ASN 77 78 GLY 78 79 ILE 79 80 LYS 80 81 PRO 81 82 VAL 82 83 TYR 83 84 VAL 84 85 PHE 85 86 ASP 86 87 GLY 87 88 LYS 88 89 PRO 89 90 PRO 90 91 GLN 91 92 LEU 92 93 ALA 93 94 SER 94 95 GLY 95 96 GLU 96 97 LEU 97 98 ALA 98 99 LYS 99 100 ARG 100 101 SER 101 102 GLU 102 103 ARG 103 104 ARG 104 105 ALA 105 106 GLU 106 107 ALA 107 108 GLU 108 109 LYS 109 110 GLN 110 111 LEU 111 112 GLN 112 113 GLN 113 114 ALA 114 115 GLN 115 116 ALA 116 117 ALA 117 118 GLY 118 119 ALA 119 120 GLU 120 121 GLN 121 122 GLU 122 123 VAL 123 124 GLU 124 125 LYS 125 126 PHE 126 127 THR 127 128 LYS 128 129 ARG 129 130 LEU 130 131 VAL 131 132 LYS 132 133 VAL 133 134 THR 134 135 LYS 135 136 GLN 136 137 HIS 137 138 ASN 138 139 ASP 139 140 GLU 140 141 CYS 141 142 LYS 142 143 HIS 143 144 LEU 144 145 LEU 145 146 SER 146 147 LEU 147 148 MET 148 149 GLY 149 150 ILE 150 151 PRO 151 152 TYR 152 153 LEU 153 154 ASP 154 155 ALA 155 156 PRO 156 157 SER 157 158 GLU 158 159 ALA 159 160 GLU 160 161 ALA 161 162 SER 162 163 CYS 163 164 ALA 164 165 ALA 165 166 LEU 166 167 VAL 167 168 LYS 168 169 ALA 169 170 GLY 170 171 LYS 171 172 VAL 172 173 TYR 173 174 ALA 174 175 ALA 175 176 ALA 176 177 THR 177 178 GLU 178 179 ASP 179 180 MET 180 181 ASP 181 182 CYS 182 183 LEU 183 184 THR 184 185 PHE 185 186 GLY 186 187 SER 187 188 PRO 188 189 VAL 189 190 LEU 190 191 MET 191 192 ARG 192 193 HIS 193 194 LEU 194 195 THR 195 196 ALA 196 197 SER 197 198 GLU 198 199 ALA 199 200 LYS 200 201 LYS 201 202 LEU 202 203 PRO 203 204 ILE 204 205 GLN 205 206 GLU 206 207 PHE 207 208 HIS 208 209 LEU 209 210 SER 210 211 ARG 211 212 ILE 212 213 LEU 213 214 GLN 214 215 GLU 215 216 LEU 216 217 GLY 217 218 LEU 218 219 ASN 219 220 GLN 220 221 GLU 221 222 GLN 222 223 PHE 223 224 VAL 224 225 ASP 225 226 LEU 226 227 CYS 227 228 ILE 228 229 LEU 229 230 LEU 230 231 GLY 231 232 SER 232 233 ASP 233 234 TYR 234 235 CYS 235 236 GLU 236 237 SER 237 238 ILE 238 239 ARG 239 240 GLY 240 241 ILE 241 242 GLY 242 243 PRO 243 244 LYS 244 245 ARG 245 246 ALA 246 247 VAL 247 248 ASP 248 249 LEU 249 250 ILE 250 251 GLN 251 252 LYS 252 253 HIS 253 254 LYS 254 255 SER 255 256 ILE 256 257 GLU 257 258 GLU 258 259 ILE 259 260 VAL 260 261 ARG 261 262 ARG 262 263 LEU 263 264 ASP 264 265 PRO 265 266 ASN 266 267 LYS 267 268 TYR 268 269 PRO 269 270 VAL 270 271 PRO 271 272 GLU 272 273 ASN 273 274 TRP 274 275 LEU 275 276 HIS 276 277 LYS 277 278 GLU 278 279 ALA 279 280 HIS 280 281 GLN 281 282 LEU 282 283 PHE 283 284 LEU 284 285 GLU 285 286 PRO 286 287 GLU 287 288 VAL 288 289 LEU 289 290 ASP 290 291 PRO 291 292 GLU 292 293 SER 293 294 VAL 294 295 GLU 295 296 LEU 296 297 LYS 297 298 TRP 298 299 SER 299 300 GLU 300 301 PRO 301 302 ASN 302 303 GLU 303 304 GLU 304 305 GLU 305 306 LEU 306 307 ILE 307 308 LYS 308 309 PHE 309 310 MET 310 311 CYS 311 312 GLY 312 313 GLU 313 314 LYS 314 315 GLN 315 316 PHE 316 317 SER 317 318 GLU 318 319 GLU 319 320 ARG 320 321 ILE 321 322 ARG 322 323 SER 323 324 GLY 324 325 VAL 325 326 LYS 326 327 ARG 327 328 LEU 328 329 SER 329 330 LYS 330 331 SER 331 332 ARG 332 333 GLN 333 334 GLY 334 335 SER 335 336 THR 336 337 LEU 337 338 GLU 338 339 VAL 339 340 LEU 340 341 PHE 341 342 GLN stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date . save_ save_dual-hairpin_DNA_substrate _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class DNA _Name_common dual-hairpin_DNA_substrate _Molecular_mass 12611.2 _Mol_thiol_state 'not present' _Details ; Synthetic oligonucleotide with sequence: 5'- TGA AAG GCA GAG CGC TAG CTC TGC CTT TCG AGC GAA GCT CC -3' ; _Residue_count 41 _Mol_residue_sequence ; TGAAAGGCAGAGCGCTAGCT CTGCCTTTCGAGCGAAGCTC C ; loop_ _Residue_seq_code _Residue_label 1 DT 2 DG 3 DA 4 DA 5 DA 6 DG 7 DG 8 DC 9 DA 10 DG 11 DA 12 DG 13 DC 14 DG 15 DC 16 DT 17 DA 18 DG 19 DC 20 DT 21 DC 22 DT 23 DG 24 DC 25 DC 26 DT 27 DT 28 DT 29 DC 30 DG 31 DA 32 DG 33 DC 34 DG 35 DA 36 DA 37 DG 38 DC 39 DT 40 DC 41 DC stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date . save_ ############# # Ligands # ############# save_CA _Saveframe_category ligand _Mol_type "non-polymer (NON-POLYMER)" _Name_common "entity_CA (CALCIUM ION)" _BMRB_code CA _PDB_code CA _Molecular_mass 40.078 _Mol_charge 2 _Mol_paramagnetic . _Mol_aromatic no _Details . loop_ _Atom_name _PDB_atom_name _Atom_type _Atom_chirality _Atom_charge _Atom_oxidation_number _Atom_unpaired_electrons CA CA CA . 2 . ? stop_ _Mol_thiol_state . _Sequence_homology_query_date . save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $hFEN1-K93A 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 $hFEN1-K93A 'recombinant technology' . . . BL21(DE3)-RILP pET-29b $dual-hairpin_DNA_substrate 'chemical synthesis' . . . . . 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 $hFEN1-K93A 0.5 mM '[U-100% 13C; U-100% 15N; U-80% 2H]' HEPES 10 mM 'natural abundance' 'potassium chloride' 6 mM 'natural abundance' 'sodium azide' 4 mM 'natural abundance' D2O 10 % '[U-99% 2H]' H2O 90 % 'natural abundance' TSP 0.05 mM '[U-99% 2H]' beta-mercaptoethanol 100 mM 'natural abundance' 'calcium chloride' 8 mM 'natural abundance' $dual-hairpin_DNA_substrate 0.55 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 stop_ _Details . save_ save_Felix _Saveframe_category software _Name Felix _Version . loop_ _Vendor _Address _Electronic_address 'Accelrys Software Inc.' . . stop_ loop_ _Task processing stop_ _Details . save_ save_CCPN_Analysis _Saveframe_category software _Name CCPN_Analysis _Version . loop_ _Vendor _Address _Electronic_address CCPN . . stop_ loop_ _Task 'chemical shift assignment' 'data analysis' 'peak picking' stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model Avance _Field_strength 600 _Details . 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_TROSY-HNCA_2 _Saveframe_category NMR_applied_experiment _Experiment_name '3D TROSY-HNCA' _Sample_label $sample_1 save_ save_3D_TROSY-HN(CO)CA_3 _Saveframe_category NMR_applied_experiment _Experiment_name '3D TROSY-HN(CO)CA' _Sample_label $sample_1 save_ save_3D_TROSY-HNCACB_4 _Saveframe_category NMR_applied_experiment _Experiment_name '3D TROSY-HNCACB' _Sample_label $sample_1 save_ save_3D_TROSY-HN(CO)CACB_5 _Saveframe_category NMR_applied_experiment _Experiment_name '3D TROSY-HN(CO)CACB' _Sample_label $sample_1 save_ save_3D_TROSY-HN(CA)CO_6 _Saveframe_category NMR_applied_experiment _Experiment_name '3D TROSY-HN(CA)CO' _Sample_label $sample_1 save_ save_3D_TROSY-HNCO_7 _Saveframe_category NMR_applied_experiment _Experiment_name '3D TROSY-HNCO' _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' 60 . mM pH 7.5 . 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 'TROSY offset: amide protons; amide nitrogens.' loop_ _Software_label $TOPSPIN $Felix $CCPN_Analysis stop_ loop_ _Experiment_label '2D 1H-15N TROSY' '3D TROSY-HNCA' '3D TROSY-HN(CO)CA' '3D TROSY-HNCACB' '3D TROSY-HN(CO)CACB' '3D TROSY-HN(CA)CO' '3D TROSY-HNCO' 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 hFEN1-336-K93A-DNA _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 8 7 LYS H H 8.072 0.005 1 2 8 7 LYS CA C 58.354 0.018 1 3 8 7 LYS CB C 31.074 0.148 1 4 8 7 LYS N N 120.496 0.147 1 5 9 8 LEU H H 7.865 0.005 1 6 9 8 LEU CA C 57.869 0.021 1 7 9 8 LEU CB C 41.355 0.000 1 8 9 8 LEU N N 120.637 0.043 1 9 10 9 ILE H H 8.537 0.004 1 10 10 9 ILE CA C 64.625 0.024 1 11 10 9 ILE CB C 36.767 0.000 1 12 10 9 ILE N N 118.523 0.100 1 13 11 10 ALA H H 7.639 0.004 1 14 11 10 ALA C C 178.345 0.014 1 15 11 10 ALA CA C 54.855 0.013 1 16 11 10 ALA CB C 17.170 0.000 1 17 11 10 ALA N N 120.371 0.082 1 18 12 11 ASP H H 7.858 0.006 1 19 12 11 ASP CA C 56.340 0.039 1 20 12 11 ASP CB C 41.553 0.000 1 21 12 11 ASP N N 116.420 0.163 1 22 13 12 VAL H H 8.501 0.002 1 23 13 12 VAL CA C 61.541 0.005 1 24 13 12 VAL N N 112.341 0.094 1 25 14 13 ALA H H 8.832 0.002 1 26 14 13 ALA CA C 49.760 0.000 1 27 14 13 ALA CB C 18.746 0.000 1 28 14 13 ALA N N 125.494 0.132 1 29 16 15 SER H H 8.132 0.003 1 30 16 15 SER CA C 59.799 0.006 1 31 16 15 SER CB C 61.977 0.082 1 32 16 15 SER N N 113.241 0.089 1 33 17 16 ALA H H 8.343 0.002 1 34 17 16 ALA CA C 52.315 0.053 1 35 17 16 ALA CB C 20.440 0.100 1 36 17 16 ALA N N 124.238 0.056 1 37 18 17 ILE H H 7.308 0.003 1 38 18 17 ILE CA C 59.394 0.005 1 39 18 17 ILE CB C 38.637 0.037 1 40 18 17 ILE N N 117.733 0.091 1 41 19 18 ARG H H 8.853 0.002 1 42 19 18 ARG C C 174.641 0.013 1 43 19 18 ARG CA C 53.514 0.023 1 44 19 18 ARG CB C 32.164 0.030 1 45 19 18 ARG N N 126.227 0.053 1 46 20 19 GLU H H 8.363 0.004 1 47 20 19 GLU C C 175.830 0.020 1 48 20 19 GLU CA C 54.371 0.021 1 49 20 19 GLU CB C 30.259 0.064 1 50 20 19 GLU N N 123.138 0.050 1 51 21 20 ASN H H 8.800 0.003 1 52 21 20 ASN C C 173.895 0.001 1 53 21 20 ASN CA C 51.365 0.075 1 54 21 20 ASN CB C 43.140 0.083 1 55 21 20 ASN N N 122.130 0.077 1 56 22 21 ASP H H 8.493 0.004 1 57 22 21 ASP CA C 53.071 0.015 1 58 22 21 ASP CB C 42.895 0.000 1 59 22 21 ASP N N 119.995 0.086 1 60 25 24 SER H H 7.810 0.003 1 61 25 24 SER CA C 60.342 0.038 1 62 25 24 SER CB C 62.648 0.142 1 63 25 24 SER N N 115.267 0.041 1 64 26 25 TYR H H 7.672 0.002 1 65 26 25 TYR CA C 58.284 0.005 1 66 26 25 TYR CB C 37.320 0.099 1 67 26 25 TYR N N 119.162 0.096 1 68 27 26 PHE H H 7.044 0.005 1 69 27 26 PHE C C 177.183 0.015 1 70 27 26 PHE CA C 60.544 0.001 1 71 27 26 PHE CB C 38.327 0.069 1 72 27 26 PHE N N 120.969 0.051 1 73 28 27 GLY H H 8.407 0.001 1 74 28 27 GLY C C 174.309 0.004 1 75 28 27 GLY CA C 44.610 0.029 1 76 28 27 GLY N N 117.881 0.110 1 77 29 28 ARG H H 7.930 0.003 1 78 29 28 ARG C C 175.017 0.018 1 79 29 28 ARG CA C 54.056 0.041 1 80 29 28 ARG CB C 29.695 0.048 1 81 29 28 ARG N N 119.232 0.093 1 82 30 29 LYS H H 8.469 0.002 1 83 30 29 LYS CA C 54.187 0.000 1 84 30 29 LYS CB C 34.188 0.000 1 85 30 29 LYS N N 121.603 0.064 1 86 86 85 ASP H H 9.044 0.004 1 87 86 85 ASP CA C 55.253 0.030 1 88 86 85 ASP CB C 42.258 0.180 1 89 86 85 ASP N N 122.231 0.054 1 90 87 86 GLY H H 8.599 0.002 1 91 87 86 GLY C C 173.729 0.001 1 92 87 86 GLY CA C 44.183 0.009 1 93 87 86 GLY N N 112.721 0.041 1 94 88 87 LYS H H 7.640 0.003 1 95 88 87 LYS C C 174.288 0.000 1 96 88 87 LYS CA C 53.938 0.000 1 97 88 87 LYS CB C 31.568 0.000 1 98 88 87 LYS N N 128.128 0.054 1 99 107 106 ALA H H 7.953 0.002 1 100 107 106 ALA CA C 54.661 0.037 1 101 107 106 ALA CB C 17.185 0.053 1 102 107 106 ALA N N 123.068 0.101 1 103 108 107 GLU H H 8.312 0.007 1 104 108 107 GLU N N 119.112 0.144 1 105 146 145 SER H H 8.298 0.008 1 106 146 145 SER CA C 61.139 0.000 1 107 146 145 SER CB C 62.420 0.000 1 108 146 145 SER N N 114.887 0.126 1 109 149 148 GLY H H 7.561 0.003 1 110 149 148 GLY C C 173.882 0.000 1 111 149 148 GLY CA C 45.167 0.056 1 112 149 148 GLY N N 105.981 0.044 1 113 152 151 TYR H H 7.369 0.002 1 114 152 151 TYR C C 173.611 0.032 1 115 152 151 TYR CA C 54.620 0.012 1 116 152 151 TYR CB C 41.779 0.000 1 117 152 151 TYR N N 113.473 0.078 1 118 153 152 LEU H H 9.116 0.004 1 119 153 152 LEU CA C 52.348 0.055 1 120 153 152 LEU N N 119.853 0.031 1 121 154 153 ASP H H 8.770 0.002 1 122 154 153 ASP CA C 53.503 0.027 1 123 154 153 ASP CB C 41.068 0.081 1 124 154 153 ASP N N 123.746 0.053 1 125 155 154 ALA H H 8.949 0.004 1 126 155 154 ALA CA C 49.597 0.008 1 127 155 154 ALA CB C 17.422 0.000 1 128 155 154 ALA N N 127.580 0.064 1 129 157 156 SER H H 6.513 0.006 1 130 157 156 SER CA C 55.676 0.022 1 131 157 156 SER CB C 61.697 0.022 1 132 157 156 SER N N 114.061 0.094 1 133 158 157 GLU H H 8.194 0.004 1 134 158 157 GLU CA C 56.025 0.000 1 135 158 157 GLU N N 124.356 0.108 1 136 164 163 ALA H H 7.419 0.004 1 137 164 163 ALA C C 178.780 0.013 1 138 164 163 ALA CA C 54.848 0.038 1 139 164 163 ALA CB C 17.692 0.129 1 140 164 163 ALA N N 119.892 0.090 1 141 165 164 ALA H H 7.494 0.002 1 142 165 164 ALA C C 180.193 0.038 1 143 165 164 ALA CA C 54.795 0.061 1 144 165 164 ALA CB C 16.945 0.000 1 145 165 164 ALA N N 120.020 0.082 1 146 166 165 LEU H H 7.743 0.005 1 147 166 165 LEU CA C 57.903 0.030 1 148 166 165 LEU N N 118.102 0.038 1 149 167 166 VAL H H 7.539 0.003 1 150 167 166 VAL CA C 64.355 0.035 1 151 167 166 VAL N N 120.739 0.099 1 152 168 167 LYS H H 8.613 0.004 1 153 168 167 LYS CA C 59.930 0.030 1 154 168 167 LYS CB C 32.265 0.128 1 155 168 167 LYS N N 122.691 0.055 1 156 169 168 ALA H H 7.403 0.008 1 157 169 168 ALA CA C 51.474 0.089 1 158 169 168 ALA CB C 19.482 0.000 1 159 169 168 ALA N N 116.190 0.092 1 160 170 169 GLY H H 8.003 0.003 1 161 170 169 GLY C C 175.085 0.024 1 162 170 169 GLY CA C 45.353 0.032 1 163 170 169 GLY N N 107.538 0.146 1 164 171 170 LYS H H 8.075 0.005 1 165 171 170 LYS CA C 55.406 0.051 1 166 171 170 LYS CB C 31.925 0.025 1 167 171 170 LYS N N 116.637 0.108 1 168 172 171 VAL H H 6.975 0.009 1 169 172 171 VAL CA C 57.841 0.048 1 170 172 171 VAL CB C 33.381 0.011 1 171 172 171 VAL N N 104.680 0.161 1 172 173 172 TYR H H 8.756 0.002 1 173 173 172 TYR CA C 59.542 0.064 1 174 173 172 TYR CB C 39.350 0.000 1 175 173 172 TYR N N 120.942 0.094 1 176 174 173 ALA H H 6.835 0.005 1 177 174 173 ALA CA C 50.818 0.003 1 178 174 173 ALA N N 109.900 0.078 1 179 175 174 ALA H H 6.804 0.002 1 180 175 174 ALA CA C 49.012 0.064 1 181 175 174 ALA CB C 21.865 0.020 1 182 175 174 ALA N N 122.319 0.040 1 183 176 175 ALA H H 9.350 0.002 1 184 176 175 ALA CA C 50.214 0.000 1 185 176 175 ALA CB C 19.869 0.000 1 186 176 175 ALA N N 127.103 0.075 1 187 189 188 VAL H H 6.565 0.005 1 188 189 188 VAL CA C 60.622 0.073 1 189 189 188 VAL CB C 34.733 0.000 1 190 189 188 VAL N N 110.921 0.113 1 191 190 189 LEU H H 8.587 0.003 1 192 190 189 LEU CA C 52.683 0.014 1 193 190 189 LEU CB C 46.158 0.056 1 194 190 189 LEU N N 132.823 0.168 1 195 191 190 MET H H 9.536 0.004 1 196 191 190 MET CA C 54.135 0.076 1 197 191 190 MET CB C 35.892 0.043 1 198 191 190 MET N N 126.379 0.082 1 199 192 191 ARG H H 9.420 0.004 1 200 192 191 ARG CA C 54.927 0.015 1 201 192 191 ARG CB C 31.316 0.000 1 202 192 191 ARG N N 123.422 0.093 1 203 208 207 HIS H H 8.707 0.003 1 204 208 207 HIS CA C 54.664 0.045 1 205 208 207 HIS CB C 31.399 0.127 1 206 208 207 HIS N N 121.901 0.099 1 207 209 208 LEU H H 8.073 0.003 1 208 209 208 LEU CA C 57.830 0.025 1 209 209 208 LEU CB C 42.065 0.000 1 210 209 208 LEU N N 128.766 0.062 1 211 210 209 SER H H 9.525 0.003 1 212 210 209 SER CA C 61.223 0.025 1 213 210 209 SER N N 113.045 0.093 1 214 211 210 ARG H H 6.924 0.003 1 215 211 210 ARG CA C 56.690 0.000 1 216 211 210 ARG CB C 28.957 0.000 1 217 211 210 ARG N N 120.899 0.086 1 218 214 213 GLN H H 7.810 0.003 1 219 214 213 GLN CA C 58.395 0.042 1 220 214 213 GLN CB C 28.309 0.043 1 221 214 213 GLN N N 117.565 0.091 1 222 215 214 GLU H H 8.239 0.003 1 223 215 214 GLU CA C 58.667 0.016 1 224 215 214 GLU CB C 28.612 0.000 1 225 215 214 GLU N N 118.769 0.148 1 226 216 215 LEU H H 7.854 0.005 1 227 216 215 LEU CA C 54.882 0.039 1 228 216 215 LEU N N 115.483 0.121 1 229 217 216 GLY H H 7.746 0.009 1 230 217 216 GLY CA C 46.368 0.090 1 231 217 216 GLY N N 110.831 0.102 1 232 218 217 LEU H H 7.917 0.004 1 233 218 217 LEU C C 176.172 0.054 1 234 218 217 LEU CA C 52.550 0.057 1 235 218 217 LEU CB C 45.165 0.054 1 236 218 217 LEU N N 118.002 0.100 1 237 219 218 ASN H H 7.567 0.003 1 238 219 218 ASN CA C 50.193 0.024 1 239 219 218 ASN CB C 38.573 0.139 1 240 219 218 ASN N N 116.430 0.061 1 241 220 219 GLN H H 8.600 0.002 1 242 220 219 GLN CA C 58.983 0.001 1 243 220 219 GLN CB C 26.609 0.060 1 244 220 219 GLN N N 119.449 0.057 1 245 221 220 GLU H H 8.562 0.004 1 246 221 220 GLU CA C 60.814 0.030 1 247 221 220 GLU N N 119.076 0.098 1 248 222 221 GLN H H 8.202 0.005 1 249 222 221 GLN CA C 57.729 0.030 1 250 222 221 GLN CB C 28.371 0.000 1 251 222 221 GLN N N 119.087 0.132 1 252 223 222 PHE H H 8.592 0.006 1 253 223 222 PHE CA C 60.425 0.012 1 254 223 222 PHE CB C 38.891 0.000 1 255 223 222 PHE N N 121.216 0.218 1 256 224 223 VAL H H 8.744 0.005 1 257 224 223 VAL CA C 67.321 0.063 1 258 224 223 VAL CB C 29.919 0.000 1 259 224 223 VAL N N 123.469 0.058 1 260 225 224 ASP H H 7.409 0.005 1 261 225 224 ASP CA C 57.354 0.019 1 262 225 224 ASP CB C 40.518 0.000 1 263 225 224 ASP N N 120.865 0.068 1 264 226 225 LEU H H 8.435 0.004 1 265 226 225 LEU CA C 57.938 0.013 1 266 226 225 LEU CB C 39.839 0.000 1 267 226 225 LEU N N 121.602 0.063 1 268 227 226 CYS H H 7.817 0.001 1 269 227 226 CYS CA C 63.561 0.000 1 270 227 226 CYS N N 116.566 0.050 1 271 237 236 SER H H 8.351 0.004 1 272 237 236 SER CA C 56.941 0.012 1 273 237 236 SER CB C 63.654 0.105 1 274 237 236 SER N N 116.781 0.056 1 275 238 237 ILE H H 8.908 0.002 1 276 238 237 ILE CA C 60.697 0.023 1 277 238 237 ILE CB C 37.385 0.031 1 278 238 237 ILE N N 119.936 0.056 1 279 239 238 ARG H H 8.810 0.003 1 280 239 238 ARG CA C 57.816 0.015 1 281 239 238 ARG CB C 28.554 0.000 1 282 239 238 ARG N N 132.985 0.100 1 283 244 243 LYS H H 7.904 0.003 1 284 244 243 LYS C C 174.380 0.000 1 285 244 243 LYS CA C 59.070 0.041 1 286 244 243 LYS CB C 30.704 0.000 1 287 244 243 LYS N N 120.847 0.072 1 288 245 244 ARG H H 7.634 0.002 1 289 245 244 ARG CA C 58.691 0.037 1 290 245 244 ARG CB C 32.263 0.000 1 291 245 244 ARG N N 116.587 0.133 1 292 246 245 ALA H H 9.109 0.004 1 293 246 245 ALA CA C 55.386 0.042 1 294 246 245 ALA CB C 18.585 0.000 1 295 246 245 ALA N N 120.908 0.068 1 296 247 246 VAL H H 7.426 0.006 1 297 247 246 VAL CA C 66.298 0.030 1 298 247 246 VAL CB C 31.194 0.000 1 299 247 246 VAL N N 115.728 0.136 1 300 248 247 ASP H H 6.859 0.010 1 301 248 247 ASP CA C 57.318 0.026 1 302 248 247 ASP CB C 41.485 0.027 1 303 248 247 ASP N N 119.034 0.086 1 304 249 248 LEU H H 8.447 0.007 1 305 249 248 LEU CA C 57.366 0.000 1 306 249 248 LEU CB C 41.128 0.000 1 307 249 248 LEU N N 117.138 0.100 1 308 253 252 HIS H H 8.239 0.005 1 309 253 252 HIS CA C 56.280 0.033 1 310 253 252 HIS CB C 31.751 0.016 1 311 253 252 HIS N N 115.108 0.103 1 312 254 253 LYS H H 8.133 0.005 1 313 254 253 LYS CA C 59.753 0.000 1 314 254 253 LYS CB C 29.463 0.069 1 315 254 253 LYS N N 113.994 0.070 1 316 255 254 SER H H 8.021 0.004 1 317 255 254 SER C C 174.571 0.014 1 318 255 254 SER CA C 55.728 0.039 1 319 255 254 SER CB C 66.210 0.098 1 320 255 254 SER N N 112.891 0.073 1 321 256 255 ILE H H 8.495 0.003 1 322 256 255 ILE CA C 65.848 0.029 1 323 256 255 ILE CB C 36.607 0.163 1 324 256 255 ILE N N 122.717 0.066 1 325 257 256 GLU H H 8.852 0.004 1 326 257 256 GLU CA C 59.991 0.023 1 327 257 256 GLU CB C 28.586 0.000 1 328 257 256 GLU N N 118.629 0.093 1 329 258 257 GLU H H 7.441 0.009 1 330 258 257 GLU CA C 57.605 0.018 1 331 258 257 GLU CB C 28.579 0.000 1 332 258 257 GLU N N 118.379 0.097 1 333 259 258 ILE H H 7.989 0.001 1 334 259 258 ILE CA C 65.952 0.031 1 335 259 258 ILE CB C 37.412 0.109 1 336 259 258 ILE N N 121.392 0.077 1 337 260 259 VAL H H 8.588 0.006 1 338 260 259 VAL CA C 66.111 0.052 1 339 260 259 VAL CB C 30.512 0.006 1 340 260 259 VAL N N 116.636 0.054 1 341 261 260 ARG H H 7.076 0.005 1 342 261 260 ARG CA C 58.165 0.012 1 343 261 260 ARG CB C 29.799 0.178 1 344 261 260 ARG N N 117.388 0.096 1 345 262 261 ARG H H 7.399 0.002 1 346 262 261 ARG CA C 54.678 0.047 1 347 262 261 ARG CB C 30.073 0.009 1 348 262 261 ARG N N 116.853 0.104 1 349 263 262 LEU H H 7.435 0.006 1 350 263 262 LEU CA C 54.240 0.019 1 351 263 262 LEU CB C 42.287 0.166 1 352 263 262 LEU N N 121.844 0.105 1 353 264 263 ASP H H 8.618 0.002 1 354 264 263 ASP C C 175.650 0.000 1 355 264 263 ASP CA C 51.315 0.000 1 356 264 263 ASP CB C 41.087 0.000 1 357 264 263 ASP N N 125.606 0.060 1 358 272 271 GLU H H 8.440 0.002 1 359 272 271 GLU C C 177.185 0.018 1 360 272 271 GLU CA C 56.602 0.034 1 361 272 271 GLU CB C 29.306 0.000 1 362 272 271 GLU N N 122.890 0.043 1 363 273 272 ASN H H 9.001 0.005 1 364 273 272 ASN CA C 53.385 0.007 1 365 273 272 ASN CB C 36.985 0.054 1 366 273 272 ASN N N 120.894 0.059 1 367 274 273 TRP H H 7.838 0.005 1 368 274 273 TRP CA C 55.531 0.000 1 369 274 273 TRP N N 118.691 0.115 1 370 287 286 GLU H H 8.378 0.003 1 371 287 286 GLU CB C 28.485 0.098 1 372 287 286 GLU N N 120.651 0.060 1 373 288 287 VAL H H 8.575 0.003 1 374 288 287 VAL C C 174.954 0.003 1 375 288 287 VAL CA C 58.761 0.043 1 376 288 287 VAL CB C 36.940 0.000 1 377 288 287 VAL N N 121.204 0.049 1 378 289 288 LEU H H 7.030 0.003 1 379 289 288 LEU C C 174.485 0.001 1 380 289 288 LEU CA C 53.569 0.038 1 381 289 288 LEU CB C 40.958 0.094 1 382 289 288 LEU N N 119.591 0.066 1 383 290 289 ASP H H 8.325 0.002 1 384 290 289 ASP C C 176.772 0.000 1 385 290 289 ASP CA C 50.422 0.000 1 386 290 289 ASP CB C 40.673 0.000 1 387 290 289 ASP N N 120.309 0.058 1 388 292 291 GLU H H 7.997 0.003 1 389 292 291 GLU CA C 56.582 0.010 1 390 292 291 GLU CB C 28.095 0.000 1 391 292 291 GLU N N 114.213 0.055 1 392 293 292 SER H H 7.596 0.002 1 393 293 292 SER C C 174.070 0.002 1 394 293 292 SER CA C 58.196 0.008 1 395 293 292 SER CB C 64.027 0.068 1 396 293 292 SER N N 113.049 0.065 1 397 294 293 VAL H H 6.825 0.003 1 398 294 293 VAL C C 174.528 0.002 1 399 294 293 VAL CA C 60.970 0.012 1 400 294 293 VAL CB C 32.331 0.000 1 401 294 293 VAL N N 118.868 0.061 1 402 295 294 GLU H H 8.478 0.002 1 403 295 294 GLU C C 175.096 0.000 1 404 295 294 GLU CA C 54.504 0.024 1 405 295 294 GLU CB C 29.934 0.065 1 406 295 294 GLU N N 127.822 0.057 1 407 296 295 LEU H H 8.551 0.002 1 408 296 295 LEU CA C 53.753 0.037 1 409 296 295 LEU CB C 41.353 0.118 1 410 296 295 LEU N N 126.317 0.063 1 411 297 296 LYS H H 7.332 0.002 1 412 297 296 LYS C C 173.298 0.011 1 413 297 296 LYS CA C 54.891 0.028 1 414 297 296 LYS CB C 34.533 0.019 1 415 297 296 LYS N N 123.111 0.066 1 416 298 297 TRP H H 8.823 0.003 1 417 298 297 TRP CA C 58.911 0.009 1 418 298 297 TRP CB C 29.631 0.155 1 419 298 297 TRP N N 127.508 0.073 1 420 299 298 SER H H 9.263 0.003 1 421 299 298 SER C C 172.622 0.002 1 422 299 298 SER CA C 56.809 0.029 1 423 299 298 SER CB C 64.724 0.084 1 424 299 298 SER N N 121.417 0.045 1 425 300 299 GLU H H 8.486 0.002 1 426 300 299 GLU C C 174.635 0.000 1 427 300 299 GLU CA C 54.541 0.000 1 428 300 299 GLU CB C 28.582 0.000 1 429 300 299 GLU N N 121.520 0.045 1 430 302 301 ASN H H 8.530 0.002 1 431 302 301 ASN CA C 50.775 0.061 1 432 302 301 ASN CB C 36.606 0.105 1 433 302 301 ASN N N 121.143 0.067 1 434 303 302 GLU H H 8.287 0.002 1 435 303 302 GLU CA C 61.012 0.015 1 436 303 302 GLU CB C 29.443 0.117 1 437 303 302 GLU N N 124.858 0.066 1 438 304 303 GLU H H 8.807 0.002 1 439 304 303 GLU CA C 59.419 0.069 1 440 304 303 GLU CB C 28.174 0.110 1 441 304 303 GLU N N 116.649 0.050 1 442 305 304 GLU H H 7.551 0.004 1 443 305 304 GLU CA C 57.780 0.050 1 444 305 304 GLU N N 117.880 0.095 1 445 306 305 LEU H H 8.571 0.010 1 446 306 305 LEU CA C 58.516 0.023 1 447 306 305 LEU CB C 41.140 0.104 1 448 306 305 LEU N N 123.039 0.103 1 449 307 306 ILE H H 8.197 0.007 1 450 307 306 ILE CA C 63.764 0.022 1 451 307 306 ILE CB C 35.781 0.000 1 452 307 306 ILE N N 120.722 0.196 1 453 308 307 LYS H H 7.753 0.003 1 454 308 307 LYS CA C 60.111 0.004 1 455 308 307 LYS CB C 31.520 0.002 1 456 308 307 LYS N N 121.975 0.055 1 457 309 308 PHE H H 7.987 0.004 1 458 309 308 PHE CA C 59.137 0.000 1 459 309 308 PHE CB C 40.052 0.000 1 460 309 308 PHE N N 116.645 0.067 1 461 317 316 SER H H 9.391 0.005 1 462 317 316 SER C C 176.419 0.017 1 463 317 316 SER CA C 57.362 0.043 1 464 317 316 SER CB C 62.962 0.089 1 465 317 316 SER N N 119.575 0.088 1 466 318 317 GLU H H 9.073 0.003 1 467 318 317 GLU CA C 60.113 0.017 1 468 318 317 GLU CB C 28.434 0.033 1 469 318 317 GLU N N 132.471 0.066 1 470 319 318 GLU H H 8.535 0.003 1 471 319 318 GLU C C 179.916 0.020 1 472 319 318 GLU CA C 59.248 0.039 1 473 319 318 GLU CB C 28.447 0.088 1 474 319 318 GLU N N 119.034 0.073 1 475 320 319 ARG H H 7.339 0.003 1 476 320 319 ARG CA C 58.842 0.000 1 477 320 319 ARG CB C 29.271 0.000 1 478 320 319 ARG N N 118.877 0.065 1 479 321 320 ILE H H 8.211 0.003 1 480 321 320 ILE CA C 61.187 0.009 1 481 321 320 ILE CB C 33.784 0.105 1 482 321 320 ILE N N 121.085 0.039 1 483 322 321 ARG H H 9.007 0.004 1 484 322 321 ARG C C 179.805 0.019 1 485 322 321 ARG CA C 60.827 0.001 1 486 322 321 ARG CB C 28.482 0.000 1 487 322 321 ARG N N 120.155 0.103 1 488 323 322 SER H H 7.998 0.003 1 489 323 322 SER CA C 61.326 0.085 1 490 323 322 SER N N 115.219 0.125 1 491 324 323 GLY H H 8.311 0.003 1 492 324 323 GLY C C 174.778 0.015 1 493 324 323 GLY CA C 47.283 0.018 1 494 324 323 GLY N N 110.509 0.071 1 495 325 324 VAL H H 8.850 0.005 1 496 325 324 VAL CA C 66.882 0.000 1 497 325 324 VAL CB C 30.341 0.000 1 498 325 324 VAL N N 122.432 0.059 1 499 332 331 ARG H H 7.524 0.002 1 500 332 331 ARG C C 176.961 0.000 1 501 332 331 ARG CA C 56.572 0.003 1 502 332 331 ARG CB C 29.436 0.068 1 503 332 331 ARG N N 121.770 0.046 1 504 333 332 GLN H H 7.868 0.003 1 505 333 332 GLN C C 176.724 0.029 1 506 333 332 GLN CA C 56.132 0.138 1 507 333 332 GLN N N 120.017 0.088 1 508 334 333 GLY H H 8.246 0.007 1 509 334 333 GLY CA C 45.168 0.053 1 510 334 333 GLY N N 109.645 0.089 1 511 336 335 THR H H 8.131 0.003 1 512 336 335 THR CA C 61.737 0.000 1 513 336 335 THR CB C 69.267 0.132 1 514 336 335 THR N N 116.425 0.097 1 515 337 336 LEU H H 8.096 0.002 1 516 337 336 LEU C C 177.206 0.004 1 517 337 336 LEU CA C 54.964 0.006 1 518 337 336 LEU CB C 41.277 0.073 1 519 337 336 LEU N N 124.448 0.049 1 520 338 337 GLU H H 8.224 0.002 1 521 338 337 GLU C C 176.250 0.005 1 522 338 337 GLU CA C 56.205 0.003 1 523 338 337 GLU CB C 29.423 0.080 1 524 338 337 GLU N N 122.340 0.060 1 525 339 338 VAL H H 7.982 0.002 1 526 339 338 VAL C C 175.728 0.001 1 527 339 338 VAL CA C 61.846 0.018 1 528 339 338 VAL CB C 31.735 0.080 1 529 339 338 VAL N N 121.939 0.049 1 530 340 339 LEU H H 8.104 0.003 1 531 340 339 LEU C C 176.790 0.002 1 532 340 339 LEU CA C 54.538 0.004 1 533 340 339 LEU CB C 41.551 0.082 1 534 340 339 LEU N N 125.967 0.034 1 535 341 340 PHE H H 8.092 0.002 1 536 341 340 PHE C C 174.693 0.000 1 537 341 340 PHE CA C 57.155 0.002 1 538 341 340 PHE CB C 38.675 0.085 1 539 341 340 PHE N N 121.413 0.053 1 540 342 341 GLN H H 7.739 0.002 1 541 342 341 GLN C C 180.271 0.000 1 542 342 341 GLN CA C 56.888 0.000 1 543 342 341 GLN CB C 29.853 0.000 1 544 342 341 GLN N N 126.747 0.055 1 stop_ save_