data_26742 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Backbone and Partial Side-Chain Chemical Shift Assignments and Dynamics Measurements for The Catalytic Domain of Human Prolyl Hydroxylase Domain 2 (PHD2) With Zn(II), 2-Oxoglutarate (2OG) and Hypoxia Inducible Factor-alpha (HIF-alpha) Peptide ; _BMRB_accession_number 26742 _BMRB_flat_file_name bmr26742.str _Entry_type original _Submission_date 2016-02-04 _Accession_date 2016-02-04 _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 Leung Ivanhoe KH . 2 Cantrelle Francois-Xavier . . 3 Hardy Adam P. . 4 Landrieu Isabelle . . 5 Schofield Christopher J. . 6 Claridge Timothy DW . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 heteronucl_NOE 1 T1_relaxation 1 T2_relaxation 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 170 "13C chemical shifts" 543 "15N chemical shifts" 170 "T1 relaxation values" 163 "T2 relaxation values" 163 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2018-07-11 update BMRB 'update entry citation' 2016-08-26 original author 'original release' stop_ loop_ _Related_BMRB_accession_number _Relationship 26741 'PHD2 Zn(II) 2OG' stop_ _Original_release_date 2016-08-26 save_ ############################# # Citation for this entry # ############################# save_Manuscript_in_Preparation _Saveframe_category entry_citation _Citation_full . _Citation_title ; 2-Oxoglutarate regulates binding of hydroxylated hypoxia-inducible factor to prolyl hydroxylase domain 2. ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 29522057 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Abboud Martine I. . 2 McAllister Tom E. . 3 Leung Ivanhoe . . 4 Chowdhury Rasheduzzaman . . 5 Jorgensen Christian . . 6 Domene Carmen . . 7 Mecinovic Jasmin . . 8 Lippl Kerstin . . 9 Hancock Rebecca L. . 10 Hopkinson Richard J. . 11 Kawamura Akane . . 12 Claridge Timothy . . 13 Schofield Christopher J. . stop_ _Journal_abbreviation 'Chem. Commun. (Camb.)' _Journal_name_full 'Chemical communications (Cambridge, England)' _Journal_volume 54 _Journal_issue 25 _Journal_ISSN 1364-548X _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 3130 _Page_last 3133 _Year 2018 _Details . save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name PHD2-Zn(II)-2OG-CODD _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label PHD2 $PHD2 'ZINC ION' $entity_ZN Co-substrate $entity_AKG Substrate $CODD 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_PHD2 _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common PHD2 _Molecular_mass . _Mol_thiol_state unknown _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 228 _Mol_residue_sequence ; GSHMASPNGQTKPLPALKLA LEYIVPCMNKHGICVVDDFL GKETGQQIGDEVRALHDTGK FTDGQLVSQKSDSSKDIRGD KITWIEGKEPGCETIGLLMS SMDDLIRHCNGKLGSYKING RTKAMVACYPGNGTGYVRHV DNPNGDGRCVTCIYYLNKDW DAKVSGGILRIFPEGKAQFA DIEPKFDRLLFFWSDRRNPH EVQPAYATRYAITVWYFDAD ERARAKVK ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 -6 GLY 2 -5 SER 3 -4 HIS 4 -3 MET 5 -2 ALA 6 -1 SER 7 181 PRO 8 182 ASN 9 183 GLY 10 184 GLN 11 185 THR 12 186 LYS 13 187 PRO 14 188 LEU 15 189 PRO 16 190 ALA 17 191 LEU 18 192 LYS 19 193 LEU 20 194 ALA 21 195 LEU 22 196 GLU 23 197 TYR 24 198 ILE 25 199 VAL 26 200 PRO 27 201 CYS 28 202 MET 29 203 ASN 30 204 LYS 31 205 HIS 32 206 GLY 33 207 ILE 34 208 CYS 35 209 VAL 36 210 VAL 37 211 ASP 38 212 ASP 39 213 PHE 40 214 LEU 41 215 GLY 42 216 LYS 43 217 GLU 44 218 THR 45 219 GLY 46 220 GLN 47 221 GLN 48 222 ILE 49 223 GLY 50 224 ASP 51 225 GLU 52 226 VAL 53 227 ARG 54 228 ALA 55 229 LEU 56 230 HIS 57 231 ASP 58 232 THR 59 233 GLY 60 234 LYS 61 235 PHE 62 236 THR 63 237 ASP 64 238 GLY 65 239 GLN 66 240 LEU 67 241 VAL 68 242 SER 69 243 GLN 70 244 LYS 71 245 SER 72 246 ASP 73 247 SER 74 248 SER 75 249 LYS 76 250 ASP 77 251 ILE 78 252 ARG 79 253 GLY 80 254 ASP 81 255 LYS 82 256 ILE 83 257 THR 84 258 TRP 85 259 ILE 86 260 GLU 87 261 GLY 88 262 LYS 89 263 GLU 90 264 PRO 91 265 GLY 92 266 CYS 93 267 GLU 94 268 THR 95 269 ILE 96 270 GLY 97 271 LEU 98 272 LEU 99 273 MET 100 274 SER 101 275 SER 102 276 MET 103 277 ASP 104 278 ASP 105 279 LEU 106 280 ILE 107 281 ARG 108 282 HIS 109 283 CYS 110 284 ASN 111 285 GLY 112 286 LYS 113 287 LEU 114 288 GLY 115 289 SER 116 290 TYR 117 291 LYS 118 292 ILE 119 293 ASN 120 294 GLY 121 295 ARG 122 296 THR 123 297 LYS 124 298 ALA 125 299 MET 126 300 VAL 127 301 ALA 128 302 CYS 129 303 TYR 130 304 PRO 131 305 GLY 132 306 ASN 133 307 GLY 134 308 THR 135 309 GLY 136 310 TYR 137 311 VAL 138 312 ARG 139 313 HIS 140 314 VAL 141 315 ASP 142 316 ASN 143 317 PRO 144 318 ASN 145 319 GLY 146 320 ASP 147 321 GLY 148 322 ARG 149 323 CYS 150 324 VAL 151 325 THR 152 326 CYS 153 327 ILE 154 328 TYR 155 329 TYR 156 330 LEU 157 331 ASN 158 332 LYS 159 333 ASP 160 334 TRP 161 335 ASP 162 336 ALA 163 337 LYS 164 338 VAL 165 339 SER 166 340 GLY 167 341 GLY 168 342 ILE 169 343 LEU 170 344 ARG 171 345 ILE 172 346 PHE 173 347 PRO 174 348 GLU 175 349 GLY 176 350 LYS 177 351 ALA 178 352 GLN 179 353 PHE 180 354 ALA 181 355 ASP 182 356 ILE 183 357 GLU 184 358 PRO 185 359 LYS 186 360 PHE 187 361 ASP 188 362 ARG 189 363 LEU 190 364 LEU 191 365 PHE 192 366 PHE 193 367 TRP 194 368 SER 195 369 ASP 196 370 ARG 197 371 ARG 198 372 ASN 199 373 PRO 200 374 HIS 201 375 GLU 202 376 VAL 203 377 GLN 204 378 PRO 205 379 ALA 206 380 TYR 207 381 ALA 208 382 THR 209 383 ARG 210 384 TYR 211 385 ALA 212 386 ILE 213 387 THR 214 388 VAL 215 389 TRP 216 390 TYR 217 391 PHE 218 392 ASP 219 393 ALA 220 394 ASP 221 395 GLU 222 396 ARG 223 397 ALA 224 398 ARG 225 399 ALA 226 400 LYS 227 401 VAL 228 402 LYS stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date . save_ save_CODD _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common CODD _Molecular_mass . _Mol_thiol_state 'not present' _Details 'Hypoxia Inducible Factor-Alpha (HIF-alpha) Peptide. Substrate' _Residue_count 19 _Mol_residue_sequence ; DLDLEMLAPYIPMDDDFQL ; loop_ _Residue_seq_code _Residue_label 1 ASP 2 LEU 3 ASP 4 LEU 5 GLU 6 MET 7 LEU 8 ALA 9 PRO 10 TYR 11 ILE 12 PRO 13 MET 14 ASP 15 ASP 16 ASP 17 PHE 18 GLN 19 LEU stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date . save_ ############# # Ligands # ############# save_ZN _Saveframe_category ligand _Mol_type "non-polymer (NON-POLYMER)" _Name_common "entity_ZN (ZINC ION)" _BMRB_code ZN _PDB_code ZN _Molecular_mass 65.409 _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 ZN ZN ZN . 2 . ? stop_ _Mol_thiol_state . _Sequence_homology_query_date . save_ save_AKG _Saveframe_category ligand _Mol_type "non-polymer (NON-POLYMER)" _Name_common "entity_AKG (2-OXOGLUTARIC ACID)" _BMRB_code AKG _PDB_code AKG _Molecular_mass 146.098 _Mol_charge 0 _Mol_paramagnetic . _Mol_aromatic no _Details . loop_ _Atom_name _PDB_atom_name _Atom_type _Atom_chirality _Atom_charge _Atom_oxidation_number _Atom_unpaired_electrons C1 C1 C . 0 . ? O1 O1 O . 0 . ? O2 O2 O . 0 . ? C2 C2 C . 0 . ? O5 O5 O . 0 . ? C3 C3 C . 0 . ? C4 C4 C . 0 . ? C5 C5 C . 0 . ? O3 O3 O . 0 . ? O4 O4 O . 0 . ? HO2 HO2 H . 0 . ? H31 H31 H . 0 . ? H32 H32 H . 0 . ? H41 H41 H . 0 . ? H42 H42 H . 0 . ? HO4 HO4 H . 0 . ? stop_ loop_ _Bond_order _Bond_atom_one_atom_name _Bond_atom_two_atom_name _PDB_bond_atom_one_atom_name _PDB_bond_atom_two_atom_name DOUB C1 O1 ? ? SING C1 O2 ? ? SING C1 C2 ? ? SING O2 HO2 ? ? DOUB C2 O5 ? ? SING C2 C3 ? ? SING C3 C4 ? ? SING C3 H31 ? ? SING C3 H32 ? ? SING C4 C5 ? ? SING C4 H41 ? ? SING C4 H42 ? ? DOUB C5 O3 ? ? SING C5 O4 ? ? SING O4 HO4 ? ? 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 $PHD2 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 $PHD2 'recombinant technology' . Escherichia coli . pET28 stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_assignment _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $PHD2 0.4 mM '[U-13C; U-15N; U-2H]' $entity_ZN 0.6875 mM 'natural abundance' $entity_AKG 0.9167 mM 'natural abundance' $CODD 0.8 mM 'natural abundance' TRIS 50 mM [U-2H] DSS 0.0667 mM 'natural abundance' 'sodium azide' 0.02 % 'natural abundance' stop_ save_ save_sample_t1t2noe _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $PHD2 0.4 mM [U-15N] $entity_ZN 0.6 mM 'natural abundance' $entity_AKG 0.8 mM 'natural abundance' $CODD 0.8 mM 'natural abundance' TRIS 50 mM [U-2H] 'sodium azide' 0.02 % '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_Analysis _Saveframe_category software _Name 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_assignment _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model Avance _Field_strength 700 _Details . save_ save_spectrometer_t1t2noe _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model Avance _Field_strength 900 _Details . save_ ############################# # NMR applied experiments # ############################# save_2D_1H-15N_HSQC_1 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-15N HSQC' _Sample_label $sample_assignment save_ save_3D_HNCO_2 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCO' _Sample_label $sample_assignment save_ save_3D_HNCA_3 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCA' _Sample_label $sample_assignment save_ save_3D_HNCACB_4 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCACB' _Sample_label $sample_assignment save_ save_3D_HNCOCACB_5 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCOCACB' _Sample_label $sample_assignment save_ save_3D_HNCACO_6 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCACO' _Sample_label $sample_assignment save_ save_3D_HNCOCA_7 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCOCA' _Sample_label $sample_assignment save_ save_3D_Heteronuclear_NOE_8 _Saveframe_category NMR_applied_experiment _Experiment_name '3D Heteronuclear NOE' _Sample_label $sample_t1t2noe save_ save_3D_T1_9 _Saveframe_category NMR_applied_experiment _Experiment_name '3D T1' _Sample_label $sample_t1t2noe save_ save_3D_T2_10 _Saveframe_category NMR_applied_experiment _Experiment_name '3D T2' _Sample_label $sample_t1t2noe save_ save_2D_1H-15N_HSQC_11 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-15N HSQC' _Sample_label $sample_t1t2noe save_ ####################### # Sample conditions # ####################### save_sample_conditions_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 6.6 . pH temperature 310 . K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference_1 _Saveframe_category chemical_shift_reference _Details . loop_ _Mol_common_name _Atom_type _Atom_isotope_number _Atom_group _Chem_shift_units _Chem_shift_value _Reference_method _Reference_type _External_reference_sample_geometry _External_reference_location _External_reference_axis _Indirect_shift_ratio DSS C 13 'methyl protons' ppm 0.00 na indirect . . . 0.251449530 DSS H 1 'methyl protons' ppm 0.00 internal direct . . . 1.000000000 DSS N 15 'methyl protons' ppm 0.00 na indirect . . . 0.101329118 stop_ save_ ################################### # Assigned chemical shift lists # ################################### ################################################################### # Chemical Shift Ambiguity Index Value Definitions # # # # The values other than 1 are used for those atoms with different # # chemical shifts that cannot be assigned to stereospecific atoms # # or to specific residues or chains. # # # # Index Value Definition # # # # 1 Unique (including isolated methyl protons, # # geminal atoms, and geminal methyl # # groups with identical chemical shifts) # # (e.g. ILE HD11, HD12, HD13 protons) # # 2 Ambiguity of geminal atoms or geminal methyl # # proton groups (e.g. ASP HB2 and HB3 # # protons, LEU CD1 and CD2 carbons, or # # LEU HD11, HD12, HD13 and HD21, HD22, # # HD23 methyl protons) # # 3 Aromatic atoms on opposite sides of # # symmetrical rings (e.g. TYR HE1 and HE2 # # protons) # # 4 Intraresidue ambiguities (e.g. LYS HG and # # HD protons or TRP HZ2 and HZ3 protons) # # 5 Interresidue ambiguities (LYS 12 vs. LYS 27) # # 6 Intermolecular ambiguities (e.g. ASP 31 CA # # in monomer 1 and ASP 31 CA in monomer 2 # # of an asymmetrical homodimer, duplex # # DNA assignments, or other assignments # # that may apply to atoms in one or more # # molecule in the molecular assembly) # # 9 Ambiguous, specific ambiguity not defined # # # ################################################################### save_assigned_chem_shift_list_1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Experiment_label '2D 1H-15N HSQC' '3D HNCO' '3D HNCA' '3D HNCACB' '3D HNCOCACB' '3D HNCACO' '3D HNCOCA' stop_ loop_ _Sample_label $sample_assignment stop_ _Sample_conditions_label $sample_conditions_1 _Chem_shift_reference_set_label $chemical_shift_reference_1 _Mol_system_component_name PHD2 _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 1 181 7 PRO C C 174.2 0.5 . 2 181 7 PRO CA C 60.68 0.5 . 3 181 7 PRO CB C 28.37 0.5 . 4 182 8 ASN H H 8.29 0.05 . 5 182 8 ASN C C 173.14 0.5 . 6 182 8 ASN CA C 50.44 0.5 . 7 182 8 ASN CB C 35.82 0.5 . 8 182 8 ASN N N 117.81 0.1 . 9 183 9 GLY H H 8.32 0.05 . 10 183 9 GLY C C 171.48 0.5 . 11 183 9 GLY CA C 42.53 0.5 . 12 183 9 GLY N N 109.08 0.1 . 13 184 10 GLN H H 8.17 0.05 . 14 184 10 GLN C C 173.45 0.5 . 15 184 10 GLN CA C 52.69 0.5 . 16 184 10 GLN CB C 26.23 0.5 . 17 184 10 GLN N N 119.47 0.1 . 18 185 11 THR H H 8.14 0.05 . 19 185 11 THR C C 170.64 0.5 . 20 185 11 THR CA C 59.39 0.5 . 21 185 11 THR CB C 66.75 0.5 . 22 185 11 THR N N 116.44 0.1 . 23 186 12 LYS H H 8.02 0.05 . 24 186 12 LYS C C 172.26 0.5 . 25 186 12 LYS CA C 49.96 0.5 . 26 186 12 LYS CB C 30.47 0.5 . 27 186 12 LYS N N 121.9 0.1 . 28 187 13 PRO C C 174 0.5 . 29 187 13 PRO CA C 59.85 0.5 . 30 187 13 PRO CB C 28.56 0.5 . 31 188 14 LEU H H 8.35 0.05 . 32 188 14 LEU C C 172.93 0.5 . 33 188 14 LEU CA C 50.17 0.5 . 34 188 14 LEU CB C 39.03 0.5 . 35 188 14 LEU N N 123.25 0.1 . 36 189 15 PRO C C 174.93 0.5 . 37 189 15 PRO CA C 60.4 0.5 . 38 189 15 PRO CB C 27.99 0.5 . 39 190 16 ALA H H 8.43 0.05 . 40 190 16 ALA C C 175.78 0.5 . 41 190 16 ALA CA C 52.03 0.5 . 42 190 16 ALA CB C 15.62 0.5 . 43 190 16 ALA N N 123.44 0.1 . 44 191 17 LEU H H 7.99 0.05 . 45 191 17 LEU C C 175.61 0.5 . 46 191 17 LEU CA C 55.31 0.5 . 47 191 17 LEU CB C 38.4 0.5 . 48 191 17 LEU N N 116.77 0.1 . 49 192 18 LYS H H 7.31 0.05 . 50 192 18 LYS C C 175.61 0.5 . 51 192 18 LYS CA C 55.92 0.5 . 52 192 18 LYS CB C 29.22 0.5 . 53 192 18 LYS N N 117.22 0.1 . 54 193 19 LEU H H 8.11 0.05 . 55 193 19 LEU C C 176.87 0.5 . 56 193 19 LEU CA C 54.63 0.5 . 57 193 19 LEU CB C 38.82 0.5 . 58 193 19 LEU N N 118.94 0.1 . 59 194 20 ALA H H 8.24 0.05 . 60 194 20 ALA C C 174.94 0.5 . 61 194 20 ALA CA C 52.65 0.5 . 62 194 20 ALA CB C 16 0.5 . 63 194 20 ALA N N 119.62 0.1 . 64 195 21 LEU H H 8.12 0.05 . 65 195 21 LEU C C 176.6 0.5 . 66 195 21 LEU CA C 54.4 0.5 . 67 195 21 LEU CB C 38.31 0.5 . 68 195 21 LEU N N 112.79 0.1 . 69 196 22 GLU H H 8.47 0.05 . 70 196 22 GLU C C 171.3 0.5 . 71 196 22 GLU CA C 53.67 0.5 . 72 196 22 GLU CB C 26.24 0.5 . 73 196 22 GLU N N 112.84 0.1 . 74 197 23 TYR H H 7.38 0.05 . 75 197 23 TYR C C 171.77 0.5 . 76 197 23 TYR CA C 57.43 0.5 . 77 197 23 TYR CB C 37.48 0.5 . 78 197 23 TYR N N 117.18 0.1 . 79 198 24 ILE H H 8.76 0.05 . 80 198 24 ILE C C 174.9 0.5 . 81 198 24 ILE CA C 62.65 0.5 . 82 198 24 ILE CB C 33.88 0.5 . 83 198 24 ILE N N 120.88 0.1 . 84 199 25 VAL H H 8.56 0.05 . 85 199 25 VAL C C 172.8 0.5 . 86 199 25 VAL CA C 65.7 0.5 . 87 199 25 VAL CB C 26.4 0.5 . 88 199 25 VAL N N 116.06 0.1 . 89 200 26 PRO C C 177.14 0.5 . 90 200 26 PRO CA C 62.55 0.5 . 91 200 26 PRO CB C 26.81 0.5 . 92 201 27 CYS H H 7.76 0.05 . 93 201 27 CYS C C 175.36 0.5 . 94 201 27 CYS CA C 61.18 0.5 . 95 201 27 CYS CB C 24.03 0.5 . 96 201 27 CYS N N 115.62 0.1 . 97 202 28 MET H H 8.71 0.05 . 98 202 28 MET C C 176.75 0.5 . 99 202 28 MET CA C 53.28 0.5 . 100 202 28 MET CB C 26.17 0.5 . 101 202 28 MET N N 117.61 0.1 . 102 203 29 ASN H H 8.51 0.05 . 103 203 29 ASN C C 174.4 0.5 . 104 203 29 ASN CA C 53.5 0.5 . 105 203 29 ASN CB C 34.71 0.5 . 106 203 29 ASN N N 116.48 0.1 . 107 204 30 LYS H H 7.93 0.05 . 108 204 30 LYS C C 174.93 0.5 . 109 204 30 LYS CA C 55.52 0.5 . 110 204 30 LYS CB C 30 0.5 . 111 204 30 LYS N N 117.22 0.1 . 112 205 31 HIS H H 8.48 0.05 . 113 205 31 HIS C C 174.4 0.5 . 114 205 31 HIS CA C 52.89 0.5 . 115 205 31 HIS CB C 29.27 0.5 . 116 205 31 HIS N N 113.09 0.1 . 117 206 32 GLY H H 8.53 0.05 . 118 206 32 GLY C C 168.37 0.5 . 119 206 32 GLY CA C 44.21 0.5 . 120 206 32 GLY N N 110.44 0.1 . 121 207 33 ILE H H 6.76 0.05 . 122 207 33 ILE C C 172.84 0.5 . 123 207 33 ILE CA C 56.94 0.5 . 124 207 33 ILE CB C 40.8 0.5 . 125 207 33 ILE N N 115.52 0.1 . 126 208 34 CYS C C 169.05 0.5 . 127 208 34 CYS CA C 56 0.5 . 128 208 34 CYS CB C 26.58 0.5 . 129 209 35 VAL H H 8.79 0.05 . 130 209 35 VAL C C 172.52 0.5 . 131 209 35 VAL CA C 58.69 0.5 . 132 209 35 VAL CB C 30.26 0.5 . 133 209 35 VAL N N 130.09 0.1 . 134 210 36 VAL C C 171.53 0.5 . 135 210 36 VAL CA C 58.42 0.5 . 136 210 36 VAL CB C 30.24 0.5 . 137 211 37 ASP H H 8.44 0.05 . 138 211 37 ASP C C 173.11 0.5 . 139 211 37 ASP CA C 51.44 0.5 . 140 211 37 ASP CB C 40.03 0.5 . 141 211 37 ASP N N 125.57 0.1 . 142 212 38 ASP H H 8.71 0.05 . 143 212 38 ASP C C 174.41 0.5 . 144 212 38 ASP CA C 51.83 0.5 . 145 212 38 ASP CB C 35.79 0.5 . 146 212 38 ASP N N 117.61 0.1 . 147 213 39 PHE H H 8.49 0.05 . 148 213 39 PHE C C 173.64 0.5 . 149 213 39 PHE CA C 57.38 0.5 . 150 213 39 PHE CB C 36.07 0.5 . 151 213 39 PHE N N 117.07 0.1 . 152 214 40 LEU C C 176.68 0.5 . 153 214 40 LEU CA C 51.45 0.5 . 154 214 40 LEU CB C 40.47 0.5 . 155 215 41 GLY H H 10.32 0.05 . 156 215 41 GLY C C 171.31 0.5 . 157 215 41 GLY CA C 40.79 0.5 . 158 215 41 GLY N N 115.16 0.1 . 159 216 42 LYS H H 8.19 0.05 . 160 216 42 LYS C C 175.85 0.5 . 161 216 42 LYS CA C 57.18 0.5 . 162 216 42 LYS CB C 29.21 0.5 . 163 216 42 LYS N N 117.89 0.1 . 164 217 43 GLU H H 8.63 0.05 . 165 217 43 GLU C C 176.96 0.5 . 166 217 43 GLU CA C 57.37 0.5 . 167 217 43 GLU CB C 25.27 0.5 . 168 217 43 GLU N N 118.84 0.1 . 169 218 44 THR H H 8.67 0.05 . 170 218 44 THR C C 174.06 0.5 . 171 218 44 THR CA C 63.47 0.5 . 172 218 44 THR CB C 64.35 0.5 . 173 218 44 THR N N 118.14 0.1 . 174 219 45 GLY H H 8.63 0.05 . 175 219 45 GLY C C 173.95 0.5 . 176 219 45 GLY CA C 45.23 0.5 . 177 219 45 GLY N N 108.38 0.1 . 178 220 46 GLN H H 8.59 0.05 . 179 220 46 GLN C C 175.45 0.5 . 180 220 46 GLN CA C 55.88 0.5 . 181 220 46 GLN N N 120.56 0.1 . 182 221 47 GLN H H 7.63 0.05 . 183 221 47 GLN C C 176.52 0.5 . 184 221 47 GLN CA C 56.21 0.5 . 185 221 47 GLN CB C 25 0.5 . 186 221 47 GLN N N 120.01 0.1 . 187 222 48 ILE H H 8.11 0.05 . 188 222 48 ILE C C 175.51 0.5 . 189 222 48 ILE CA C 63.11 0.5 . 190 222 48 ILE CB C 33.57 0.5 . 191 222 48 ILE N N 119.58 0.1 . 192 223 49 GLY H H 8.45 0.05 . 193 223 49 GLY C C 173.37 0.5 . 194 223 49 GLY CA C 44.94 0.5 . 195 223 49 GLY N N 106.85 0.1 . 196 224 50 ASP H H 8.52 0.05 . 197 224 50 ASP C C 176.93 0.5 . 198 224 50 ASP CA C 54.54 0.5 . 199 224 50 ASP CB C 36.51 0.5 . 200 224 50 ASP N N 122.72 0.1 . 201 225 51 GLU H H 8.23 0.05 . 202 225 51 GLU C C 177.96 0.5 . 203 225 51 GLU CA C 56.72 0.5 . 204 225 51 GLU CB C 25.53 0.5 . 205 225 51 GLU N N 122.31 0.1 . 206 226 52 VAL H H 8.66 0.05 . 207 226 52 VAL C C 175.04 0.5 . 208 226 52 VAL CA C 63.88 0.5 . 209 226 52 VAL CB C 27.67 0.5 . 210 226 52 VAL N N 119.62 0.1 . 211 227 53 ARG H H 8.3 0.05 . 212 227 53 ARG C C 175.95 0.5 . 213 227 53 ARG CA C 56.93 0.5 . 214 227 53 ARG CB C 26.21 0.5 . 215 227 53 ARG N N 120.23 0.1 . 216 228 54 ALA H H 7.92 0.05 . 217 228 54 ALA C C 178.6 0.5 . 218 228 54 ALA CA C 52.3 0.5 . 219 228 54 ALA CB C 14.27 0.5 . 220 228 54 ALA N N 120.86 0.1 . 221 229 55 LEU H H 7.83 0.05 . 222 229 55 LEU C C 176.47 0.5 . 223 229 55 LEU CA C 54.71 0.5 . 224 229 55 LEU CB C 39.18 0.5 . 225 229 55 LEU N N 119.13 0.1 . 226 230 56 HIS H H 8.4 0.05 . 227 230 56 HIS C C 176.25 0.5 . 228 230 56 HIS CA C 55.79 0.5 . 229 230 56 HIS CB C 25.46 0.5 . 230 230 56 HIS N N 119.19 0.1 . 231 231 57 ASP H H 8.93 0.05 . 232 231 57 ASP C C 174.58 0.5 . 233 231 57 ASP CA C 53.64 0.5 . 234 231 57 ASP CB C 37 0.5 . 235 231 57 ASP N N 121.1 0.1 . 236 232 58 THR H H 7.57 0.05 . 237 232 58 THR C C 173.44 0.5 . 238 232 58 THR CA C 59.76 0.5 . 239 232 58 THR CB C 67.11 0.5 . 240 232 58 THR N N 108.07 0.1 . 241 233 59 GLY H H 7.63 0.05 . 242 233 59 GLY C C 173.17 0.5 . 243 233 59 GLY CA C 43.59 0.5 . 244 233 59 GLY N N 108.11 0.1 . 245 234 60 LYS H H 7.61 0.05 . 246 234 60 LYS C C 174.44 0.5 . 247 234 60 LYS CA C 53.29 0.5 . 248 234 60 LYS CB C 29.01 0.5 . 249 234 60 LYS N N 115.98 0.1 . 250 235 61 PHE H H 8.53 0.05 . 251 235 61 PHE C C 174.06 0.5 . 252 235 61 PHE CA C 53.85 0.5 . 253 235 61 PHE CB C 35.11 0.5 . 254 235 61 PHE N N 119.92 0.1 . 255 236 62 THR H H 9.51 0.05 . 256 236 62 THR C C 171.49 0.5 . 257 236 62 THR CA C 56.95 0.5 . 258 236 62 THR CB C 68.68 0.5 . 259 236 62 THR N N 113.75 0.1 . 260 237 63 ASP H H 8.48 0.05 . 261 237 63 ASP C C 175.05 0.5 . 262 237 63 ASP CA C 53.24 0.5 . 263 237 63 ASP CB C 35.78 0.5 . 264 237 63 ASP N N 120.99 0.1 . 265 238 64 GLY H H 8.21 0.05 . 266 238 64 GLY C C 178.56 0.5 . 267 238 64 GLY CA C 42.46 0.5 . 268 238 64 GLY N N 108.81 0.1 . 269 241 67 VAL C C 173.61 0.5 . 270 241 67 VAL CA C 59.38 0.5 . 271 241 67 VAL CB C 29.19 0.5 . 272 242 68 SER H H 8.25 0.05 . 273 242 68 SER C C 171.9 0.5 . 274 242 68 SER CA C 55.27 0.5 . 275 242 68 SER CB C 60.54 0.5 . 276 242 68 SER N N 118.46 0.1 . 277 243 69 GLN H H 8.336 0.05 . 278 243 69 GLN C C 173.25 0.5 . 279 243 69 GLN CA C 53.29 0.5 . 280 243 69 GLN CB C 26.11 0.5 . 281 243 69 GLN N N 122.01 0.1 . 282 244 70 LYS C C 174.15 0.5 . 283 244 70 LYS CA C 53.13 0.5 . 284 244 70 LYS CB C 29.61 0.5 . 285 245 71 SER H H 8.23 0.05 . 286 245 71 SER C C 171.9 0.5 . 287 245 71 SER CA C 55.53 0.5 . 288 245 71 SER CB C 60.63 0.5 . 289 245 71 SER N N 115.97 0.1 . 290 246 72 ASP H H 8.48 0.05 . 291 246 72 ASP C C 173.79 0.5 . 292 246 72 ASP CA C 51.94 0.5 . 293 246 72 ASP CB C 37.33 0.5 . 294 246 72 ASP N N 120.91 0.1 . 295 247 73 SER H H 8.1 0.05 . 296 247 73 SER C C 172.64 0.5 . 297 247 73 SER CA C 55.2 0.5 . 298 247 73 SER CB C 60.47 0.5 . 299 247 73 SER N N 113.78 0.1 . 300 248 74 SER H H 8.49 0.05 . 301 248 74 SER C C 172.85 0.5 . 302 248 74 SER CA C 56.51 0.5 . 303 248 74 SER CB C 60.47 0.5 . 304 248 74 SER N N 119.01 0.1 . 305 249 75 LYS H H 8.03 0.05 . 306 249 75 LYS C C 173.74 0.5 . 307 249 75 LYS CA C 54.39 0.5 . 308 249 75 LYS CB C 28.48 0.5 . 309 249 75 LYS N N 121.64 0.1 . 310 250 76 ASP H H 8.17 0.05 . 311 250 76 ASP C C 173.16 0.5 . 312 250 76 ASP CA C 52.01 0.5 . 313 250 76 ASP CB C 36.77 0.5 . 314 250 76 ASP N N 117.17 0.1 . 315 251 77 ILE H H 7.87 0.05 . 316 251 77 ILE C C 172.12 0.5 . 317 251 77 ILE CA C 59.52 0.5 . 318 251 77 ILE CB C 35.5 0.5 . 319 251 77 ILE N N 121.36 0.1 . 320 252 78 ARG H H 7.99 0.05 . 321 252 78 ARG C C 172.72 0.5 . 322 252 78 ARG CA C 50.93 0.5 . 323 252 78 ARG CB C 28.36 0.5 . 324 252 78 ARG N N 113.93 0.1 . 325 253 79 GLY H H 8.82 0.05 . 326 253 79 GLY C C 170.41 0.5 . 327 253 79 GLY CA C 42.15 0.5 . 328 253 79 GLY N N 110.37 0.1 . 329 254 80 ASP H H 9.48 0.05 . 330 254 80 ASP C C 173.53 0.5 . 331 254 80 ASP CA C 49.17 0.5 . 332 254 80 ASP CB C 34.82 0.5 . 333 254 80 ASP N N 116.35 0.1 . 334 255 81 LYS H H 8.46 0.05 . 335 255 81 LYS C C 173.33 0.5 . 336 255 81 LYS CA C 50.45 0.5 . 337 255 81 LYS CB C 31.31 0.5 . 338 255 81 LYS N N 119.68 0.1 . 339 256 82 ILE H H 9.67 0.05 . 340 256 82 ILE C C 175.12 0.5 . 341 256 82 ILE CA C 55.31 0.5 . 342 256 82 ILE CB C 40.79 0.5 . 343 256 82 ILE N N 114.71 0.1 . 344 257 83 THR H H 8.14 0.05 . 345 257 83 THR C C 168.11 0.5 . 346 257 83 THR CA C 58.52 0.5 . 347 257 83 THR CB C 67.17 0.5 . 348 257 83 THR N N 113.3 0.1 . 349 258 84 TRP H H 7.96 0.05 . 350 258 84 TRP C C 174.16 0.5 . 351 258 84 TRP CA C 52.54 0.5 . 352 258 84 TRP CB C 27.89 0.5 . 353 258 84 TRP N N 124.52 0.1 . 354 259 85 ILE H H 9.86 0.05 . 355 259 85 ILE C C 172.22 0.5 . 356 259 85 ILE CA C 53.91 0.5 . 357 259 85 ILE CB C 36.93 0.5 . 358 259 85 ILE N N 125.54 0.1 . 359 260 86 GLU H H 11.33 0.05 . 360 260 86 GLU C C 175.08 0.5 . 361 260 86 GLU CA C 54.54 0.5 . 362 260 86 GLU CB C 27.68 0.5 . 363 260 86 GLU N N 128.54 0.1 . 364 261 87 GLY H H 10.02 0.05 . 365 261 87 GLY C C 169.59 0.5 . 366 261 87 GLY CA C 41.55 0.5 . 367 261 87 GLY N N 109.31 0.1 . 368 262 88 LYS H H 6.78 0.05 . 369 262 88 LYS C C 173.48 0.5 . 370 262 88 LYS CA C 52.09 0.5 . 371 262 88 LYS CB C 29.73 0.5 . 372 262 88 LYS N N 116.32 0.1 . 373 263 89 GLU H H 10.65 0.05 . 374 263 89 GLU C C 171.93 0.5 . 375 263 89 GLU CA C 53.74 0.5 . 376 263 89 GLU CB C 23.65 0.5 . 377 263 89 GLU N N 126.42 0.1 . 378 264 90 PRO C C 175.6 0.5 . 379 264 90 PRO CA C 60.68 0.5 . 380 264 90 PRO CB C 27.88 0.5 . 381 265 91 GLY H H 9.12 0.05 . 382 265 91 GLY C C 172.32 0.5 . 383 265 91 GLY CA C 42.58 0.5 . 384 265 91 GLY N N 113.78 0.1 . 385 266 92 CYS H H 7.77 0.05 . 386 266 92 CYS C C 172.89 0.5 . 387 266 92 CYS CA C 54.94 0.5 . 388 266 92 CYS CB C 25.38 0.5 . 389 266 92 CYS N N 115.16 0.1 . 390 267 93 GLU H H 9.11 0.05 . 391 267 93 GLU C C 177.01 0.5 . 392 267 93 GLU CA C 57.85 0.5 . 393 267 93 GLU N N 120.09 0.1 . 394 268 94 THR H H 10.3 0.05 . 395 268 94 THR C C 172.82 0.5 . 396 268 94 THR CA C 63.11 0.5 . 397 268 94 THR N N 121.57 0.1 . 398 269 95 ILE H H 8.32 0.05 . 399 269 95 ILE C C 176.18 0.5 . 400 269 95 ILE CA C 63.57 0.5 . 401 269 95 ILE CB C 34.03 0.5 . 402 269 95 ILE N N 125.55 0.1 . 403 270 96 GLY H H 8.43 0.05 . 404 270 96 GLY C C 173.77 0.5 . 405 270 96 GLY CA C 44.94 0.5 . 406 270 96 GLY N N 106.6 0.1 . 407 271 97 LEU H H 7.71 0.05 . 408 271 97 LEU C C 177.73 0.5 . 409 271 97 LEU CA C 55.2 0.5 . 410 271 97 LEU CB C 37.64 0.5 . 411 271 97 LEU N N 125.53 0.1 . 412 283 109 CYS C C 172.15 0.5 . 413 283 109 CYS CA C 58.03 0.5 . 414 283 109 CYS CB C 24.55 0.5 . 415 284 110 ASN H H 7.66 0.05 . 416 284 110 ASN C C 173.13 0.5 . 417 284 110 ASN CA C 52.08 0.5 . 418 284 110 ASN CB C 35.14 0.5 . 419 284 110 ASN N N 117.76 0.1 . 420 285 111 GLY H H 8.79 0.05 . 421 285 111 GLY C C 172.5 0.5 . 422 285 111 GLY CA C 42.78 0.5 . 423 285 111 GLY N N 113.43 0.1 . 424 286 112 LYS H H 8.1 0.05 . 425 286 112 LYS C C 173.62 0.5 . 426 286 112 LYS CA C 52.38 0.5 . 427 286 112 LYS CB C 30.91 0.5 . 428 286 112 LYS N N 116.47 0.1 . 429 287 113 LEU H H 7.66 0.05 . 430 287 113 LEU C C 172.48 0.5 . 431 287 113 LEU CA C 50.16 0.5 . 432 287 113 LEU CB C 37.6 0.5 . 433 287 113 LEU N N 120.37 0.1 . 434 288 114 GLY H H 8.71 0.05 . 435 288 114 GLY C C 170.87 0.5 . 436 288 114 GLY CA C 43.85 0.5 . 437 288 114 GLY N N 113.19 0.1 . 438 289 115 SER H H 7.79 0.05 . 439 289 115 SER C C 172.09 0.5 . 440 289 115 SER CA C 54.02 0.5 . 441 289 115 SER CB C 59.79 0.5 . 442 289 115 SER N N 118.86 0.1 . 443 290 116 TYR H H 7.3 0.05 . 444 290 116 TYR C C 173.77 0.5 . 445 290 116 TYR CA C 55.23 0.5 . 446 290 116 TYR CB C 36.36 0.5 . 447 290 116 TYR N N 119.88 0.1 . 448 291 117 LYS H H 9.22 0.05 . 449 291 117 LYS C C 172.48 0.5 . 450 291 117 LYS CA C 52.28 0.5 . 451 291 117 LYS CB C 28.93 0.5 . 452 291 117 LYS N N 125.83 0.1 . 453 292 118 ILE H H 8.6 0.05 . 454 292 118 ILE C C 174.1 0.5 . 455 292 118 ILE CA C 58.58 0.5 . 456 292 118 ILE CB C 33.84 0.5 . 457 292 118 ILE N N 125.04 0.1 . 458 293 119 ASN CA C 49.28 0.5 . 459 293 119 ASN CB C 36.73 0.5 . 460 294 120 GLY H H 7.92 0.05 . 461 294 120 GLY C C 168.31 0.5 . 462 294 120 GLY CA C 43.45 0.5 . 463 294 120 GLY N N 108.32 0.1 . 464 295 121 ARG H H 9.14 0.05 . 465 295 121 ARG C C 172.97 0.5 . 466 295 121 ARG CA C 52.17 0.5 . 467 295 121 ARG CB C 28.48 0.5 . 468 295 121 ARG N N 115.22 0.1 . 469 296 122 THR H H 7.99 0.05 . 470 296 122 THR C C 174.23 0.5 . 471 296 122 THR CA C 58.67 0.5 . 472 296 122 THR CB C 70.27 0.5 . 473 296 122 THR N N 108.51 0.1 . 474 297 123 LYS H H 8.02 0.05 . 475 297 123 LYS C C 172.61 0.5 . 476 297 123 LYS CA C 54.91 0.5 . 477 297 123 LYS CB C 30.6 0.5 . 478 297 123 LYS N N 115.25 0.1 . 479 298 124 ALA H H 8.46 0.05 . 480 298 124 ALA C C 175.05 0.5 . 481 298 124 ALA CA C 48.81 0.5 . 482 298 124 ALA CB C 15.7 0.5 . 483 298 124 ALA N N 120.87 0.1 . 484 299 125 MET H H 9.82 0.05 . 485 299 125 MET C C 172.43 0.5 . 486 299 125 MET CA C 51.02 0.5 . 487 299 125 MET CB C 30.11 0.5 . 488 299 125 MET N N 124.97 0.1 . 489 300 126 VAL H H 8.62 0.05 . 490 300 126 VAL C C 171.27 0.5 . 491 300 126 VAL CA C 59.16 0.5 . 492 300 126 VAL CB C 27.62 0.5 . 493 300 126 VAL N N 129.59 0.1 . 494 301 127 ALA H H 9.04 0.05 . 495 301 127 ALA C C 173.41 0.5 . 496 301 127 ALA CA C 47.65 0.5 . 497 301 127 ALA CB C 21.34 0.5 . 498 301 127 ALA N N 127.58 0.1 . 499 302 128 CYS H H 9.24 0.05 . 500 302 128 CYS C C 172.91 0.5 . 501 302 128 CYS CA C 52.92 0.5 . 502 302 128 CYS CB C 27.61 0.5 . 503 302 128 CYS N N 119.91 0.1 . 504 303 129 TYR H H 9.17 0.05 . 505 303 129 TYR C C 173.45 0.5 . 506 303 129 TYR CA C 54.68 0.5 . 507 303 129 TYR CB C 33.9 0.5 . 508 303 129 TYR N N 129.69 0.1 . 509 304 130 PRO C C 173.95 0.5 . 510 304 130 PRO CA C 60.48 0.5 . 511 304 130 PRO CB C 26.78 0.5 . 512 305 131 GLY H H 8.09 0.05 . 513 305 131 GLY C C 171.41 0.5 . 514 305 131 GLY CA C 42.55 0.5 . 515 305 131 GLY N N 107.29 0.1 . 516 306 132 ASN H H 8.75 0.05 . 517 306 132 ASN C C 172.58 0.5 . 518 306 132 ASN CA C 50.46 0.5 . 519 306 132 ASN CB C 34.6 0.5 . 520 306 132 ASN N N 117.12 0.1 . 521 307 133 GLY H H 8.18 0.05 . 522 307 133 GLY C C 171.55 0.5 . 523 307 133 GLY CA C 43.29 0.5 . 524 307 133 GLY N N 105.82 0.1 . 525 308 134 THR H H 7.41 0.05 . 526 308 134 THR C C 171.55 0.5 . 527 308 134 THR CA C 58.23 0.5 . 528 308 134 THR CB C 68.82 0.5 . 529 308 134 THR N N 110.62 0.1 . 530 309 135 GLY H H 8.17 0.05 . 531 309 135 GLY C C 169.12 0.5 . 532 309 135 GLY CA C 42.28 0.5 . 533 309 135 GLY N N 107.37 0.1 . 534 310 136 TYR H H 9.152 0.05 . 535 310 136 TYR CA C 53.064 0.5 . 536 310 136 TYR N N 128.463 0.1 . 537 311 137 VAL C C 173.51 0.5 . 538 311 137 VAL CA C 59.2 0.5 . 539 311 137 VAL CB C 29.39 0.5 . 540 312 138 ARG H H 8.14 0.05 . 541 312 138 ARG C C 172.52 0.5 . 542 312 138 ARG CA C 53.72 0.5 . 543 312 138 ARG CB C 26.33 0.5 . 544 312 138 ARG N N 120.35 0.1 . 545 313 139 HIS H H 8.8 0.05 . 546 313 139 HIS C C 168.69 0.5 . 547 313 139 HIS CA C 52.37 0.5 . 548 313 139 HIS CB C 28.35 0.5 . 549 313 139 HIS N N 121.48 0.1 . 550 314 140 VAL H H 8.34 0.05 . 551 314 140 VAL C C 174.19 0.5 . 552 314 140 VAL CA C 56.76 0.5 . 553 314 140 VAL CB C 31.81 0.5 . 554 314 140 VAL N N 116.86 0.1 . 555 315 141 ASP H H 9.16 0.05 . 556 315 141 ASP C C 171.26 0.5 . 557 315 141 ASP CA C 55.04 0.5 . 558 315 141 ASP CB C 37.11 0.5 . 559 315 141 ASP N N 128.51 0.1 . 560 316 142 ASN H H 7.3 0.05 . 561 316 142 ASN C C 171.7 0.5 . 562 316 142 ASN CA C 45.92 0.5 . 563 316 142 ASN CB C 36.5 0.5 . 564 316 142 ASN N N 106.36 0.1 . 565 318 144 ASN C C 172.26 0.5 . 566 318 144 ASN CA C 49.89 0.5 . 567 318 144 ASN CB C 36.56 0.5 . 568 319 145 GLY H H 8.33 0.05 . 569 319 145 GLY C C 172.65 0.5 . 570 319 145 GLY CA C 44.54 0.5 . 571 319 145 GLY N N 112.58 0.1 . 572 320 146 ASP H H 8.98 0.05 . 573 320 146 ASP CA C 50.77 0.5 . 574 320 146 ASP CB C 37.52 0.5 . 575 320 146 ASP N N 119.32 0.1 . 576 321 147 GLY H H 9.34 0.05 . 577 321 147 GLY CA C 41.73 0.5 . 578 321 147 GLY N N 106.72 0.1 . 579 322 148 ARG C C 173.53 0.5 . 580 322 148 ARG CA C 55.63 0.5 . 581 322 148 ARG CB C 29.05 0.5 . 582 323 149 CYS H H 9.8 0.05 . 583 323 149 CYS C C 172.33 0.5 . 584 323 149 CYS CA C 53.73 0.5 . 585 323 149 CYS CB C 26.09 0.5 . 586 323 149 CYS N N 121.08 0.1 . 587 324 150 VAL H H 7.46 0.05 . 588 324 150 VAL CA C 59.49 0.5 . 589 324 150 VAL CB C 33.66 0.5 . 590 324 150 VAL N N 125.21 0.1 . 591 325 151 THR H H 8.96 0.05 . 592 325 151 THR CA C 58.7 0.5 . 593 325 151 THR N N 124.85 0.1 . 594 329 155 TYR C C 174.12 0.5 . 595 329 155 TYR CA C 55.68 0.5 . 596 329 155 TYR CB C 37.82 0.5 . 597 330 156 LEU H H 6.02 0.05 . 598 330 156 LEU C C 173.5 0.5 . 599 330 156 LEU CA C 51.7 0.5 . 600 330 156 LEU CB C 40.27 0.5 . 601 330 156 LEU N N 113.64 0.1 . 602 331 157 ASN H H 6.6 0.05 . 603 331 157 ASN C C 170.63 0.5 . 604 331 157 ASN CA C 40.59 0.5 . 605 331 157 ASN CB C 36.06 0.5 . 606 331 157 ASN N N 115.57 0.1 . 607 332 158 LYS H H 9.07 0.05 . 608 332 158 LYS C C 173.61 0.5 . 609 332 158 LYS CA C 54.87 0.5 . 610 332 158 LYS CB C 29.23 0.5 . 611 332 158 LYS N N 129.64 0.1 . 612 333 159 ASP H H 9.04 0.05 . 613 333 159 ASP C C 172.16 0.5 . 614 333 159 ASP CA C 52.27 0.5 . 615 333 159 ASP CB C 36.07 0.5 . 616 333 159 ASP N N 121.81 0.1 . 617 334 160 TRP H H 7.67 0.05 . 618 334 160 TRP C C 173.18 0.5 . 619 334 160 TRP CA C 55.65 0.5 . 620 334 160 TRP CB C 25.88 0.5 . 621 334 160 TRP N N 119.22 0.1 . 622 335 161 ASP H H 8.15 0.05 . 623 335 161 ASP C C 173.63 0.5 . 624 335 161 ASP CA C 48.8 0.5 . 625 335 161 ASP N N 129.13 0.1 . 626 336 162 ALA C C 177.01 0.5 . 627 336 162 ALA CA C 51.36 0.5 . 628 336 162 ALA CB C 15.66 0.5 . 629 337 163 LYS H H 8.29 0.05 . 630 337 163 LYS C C 175.06 0.5 . 631 337 163 LYS CA C 56.1 0.5 . 632 337 163 LYS CB C 28.06 0.5 . 633 337 163 LYS N N 117.96 0.1 . 634 338 164 VAL H H 6.96 0.05 . 635 338 164 VAL CA C 60.05 0.5 . 636 338 164 VAL CB C 29.98 0.5 . 637 338 164 VAL N N 113.51 0.1 . 638 339 165 SER H H 8.33 0.05 . 639 339 165 SER C C 171.93 0.5 . 640 339 165 SER CA C 56.31 0.5 . 641 339 165 SER CB C 59.42 0.5 . 642 339 165 SER N N 113.6 0.1 . 643 340 166 GLY H H 8.25 0.05 . 644 340 166 GLY C C 172.82 0.5 . 645 340 166 GLY CA C 42.93 0.5 . 646 340 166 GLY N N 111.74 0.1 . 647 341 167 GLY H H 7.88 0.05 . 648 341 167 GLY C C 171.44 0.5 . 649 341 167 GLY CA C 44.11 0.5 . 650 341 167 GLY N N 108.36 0.1 . 651 342 168 ILE H H 7.45 0.05 . 652 342 168 ILE C C 172.29 0.5 . 653 342 168 ILE CA C 58.84 0.5 . 654 342 168 ILE CB C 34.79 0.5 . 655 342 168 ILE N N 119.57 0.1 . 656 343 169 LEU H H 7.81 0.05 . 657 343 169 LEU C C 171 0.5 . 658 343 169 LEU CA C 50.79 0.5 . 659 343 169 LEU CB C 37.98 0.5 . 660 343 169 LEU N N 126.93 0.1 . 661 344 170 ARG H H 8.99 0.05 . 662 344 170 ARG C C 171.88 0.5 . 663 344 170 ARG CA C 51.3 0.5 . 664 344 170 ARG CB C 28.54 0.5 . 665 344 170 ARG N N 130.65 0.1 . 666 345 171 ILE H H 8.95 0.05 . 667 345 171 ILE C C 0 0.5 . 668 345 171 ILE CA C 56.71 0.5 . 669 345 171 ILE CB C 36.57 0.5 . 670 345 171 ILE N N 125.87 0.1 . 671 346 172 PHE H H 8.61 0.05 . 672 346 172 PHE C C 170.18 0.5 . 673 346 172 PHE CA C 51.24 0.5 . 674 346 172 PHE CB C 35.06 0.5 . 675 346 172 PHE N N 125.4 0.1 . 676 347 173 PRO C C 176.87 0.5 . 677 347 173 PRO CA C 60.43 0.5 . 678 347 173 PRO CB C 28.5 0.5 . 679 348 174 GLU H H 9.31 0.05 . 680 348 174 GLU C C 175.2 0.5 . 681 348 174 GLU CA C 55.11 0.5 . 682 348 174 GLU CB C 26.21 0.5 . 683 348 174 GLU N N 123.91 0.1 . 684 349 175 GLY H H 8.98 0.05 . 685 349 175 GLY C C 171.67 0.5 . 686 349 175 GLY CA C 42.66 0.5 . 687 349 175 GLY N N 111.62 0.1 . 688 350 176 LYS H H 7.71 0.05 . 689 350 176 LYS C C 173.47 0.5 . 690 350 176 LYS CA C 51.65 0.5 . 691 350 176 LYS CB C 29.91 0.5 . 692 350 176 LYS N N 118.98 0.1 . 693 351 177 ALA H H 8.35 0.05 . 694 351 177 ALA C C 174.97 0.5 . 695 351 177 ALA CA C 50.11 0.5 . 696 351 177 ALA CB C 15.59 0.5 . 697 351 177 ALA N N 122.08 0.1 . 698 352 178 GLN H H 7.46 0.05 . 699 352 178 GLN C C 172.39 0.5 . 700 352 178 GLN CA C 52.18 0.5 . 701 352 178 GLN CB C 26.76 0.5 . 702 352 178 GLN N N 115.57 0.1 . 703 353 179 PHE H H 7.09 0.05 . 704 353 179 PHE C C 171.67 0.5 . 705 353 179 PHE CA C 51.99 0.5 . 706 353 179 PHE CB C 36.67 0.5 . 707 353 179 PHE N N 118.78 0.1 . 708 354 180 ALA H H 9.1 0.05 . 709 354 180 ALA CA C 47.97 0.5 . 710 354 180 ALA CB C 17.35 0.5 . 711 354 180 ALA N N 124.23 0.1 . 712 355 181 ASP H H 8.29 0.05 . 713 355 181 ASP C C 173.54 0.5 . 714 355 181 ASP CA C 50.36 0.5 . 715 355 181 ASP CB C 38.45 0.5 . 716 355 181 ASP N N 123.21 0.1 . 717 356 182 ILE H H 9.8 0.05 . 718 356 182 ILE C C 172.61 0.5 . 719 356 182 ILE CA C 55.66 0.5 . 720 356 182 ILE CB C 34.18 0.5 . 721 356 182 ILE N N 126.25 0.1 . 722 357 183 GLU H H 8.44 0.05 . 723 357 183 GLU C C 173.88 0.5 . 724 357 183 GLU CA C 52.33 0.5 . 725 357 183 GLU CB C 25.79 0.5 . 726 357 183 GLU N N 125.54 0.1 . 727 358 184 PRO C C 173.13 0.5 . 728 358 184 PRO CA C 58.85 0.5 . 729 358 184 PRO CB C 25.06 0.5 . 730 359 185 LYS H H 7.57 0.05 . 731 359 185 LYS C C 170.37 0.5 . 732 359 185 LYS CA C 53.53 0.5 . 733 359 185 LYS CB C 31.02 0.5 . 734 359 185 LYS N N 122.22 0.1 . 735 360 186 PHE H H 7.23 0.05 . 736 360 186 PHE C C 172.7 0.5 . 737 360 186 PHE CA C 56.15 0.5 . 738 360 186 PHE CB C 36.29 0.5 . 739 360 186 PHE N N 118.96 0.1 . 740 361 187 ASP H H 7.78 0.05 . 741 361 187 ASP C C 169.35 0.5 . 742 361 187 ASP CA C 51.9 0.5 . 743 361 187 ASP CB C 37.37 0.5 . 744 361 187 ASP N N 125.51 0.1 . 745 366 192 PHE C C 172.82 0.5 . 746 366 192 PHE CA C 54.71 0.5 . 747 366 192 PHE CB C 37.19 0.5 . 748 367 193 TRP H H 7.27 0.05 . 749 367 193 TRP C C 175.9 0.5 . 750 367 193 TRP CA C 53.79 0.5 . 751 367 193 TRP CB C 27.82 0.5 . 752 367 193 TRP N N 117.56 0.1 . 753 368 194 SER H H 7.74 0.05 . 754 368 194 SER C C 171.2 0.5 . 755 368 194 SER CA C 57.26 0.5 . 756 368 194 SER CB C 61.2 0.5 . 757 368 194 SER N N 114.22 0.1 . 758 369 195 ASP H H 7.89 0.05 . 759 369 195 ASP C C 173.29 0.5 . 760 369 195 ASP CA C 50.04 0.5 . 761 369 195 ASP CB C 36.75 0.5 . 762 369 195 ASP N N 119.28 0.1 . 763 370 196 ARG H H 7.73 0.05 . 764 370 196 ARG C C 173.56 0.5 . 765 370 196 ARG CA C 54.98 0.5 . 766 370 196 ARG CB C 26.19 0.5 . 767 370 196 ARG N N 110.8 0.1 . 768 371 197 ARG H H 8.41 0.05 . 769 371 197 ARG C C 173.35 0.5 . 770 371 197 ARG CA C 56.56 0.5 . 771 371 197 ARG CB C 28.25 0.5 . 772 371 197 ARG N N 118.78 0.1 . 773 372 198 ASN H H 7.55 0.05 . 774 372 198 ASN C C 171.05 0.5 . 775 372 198 ASN CA C 47.86 0.5 . 776 372 198 ASN CB C 37.56 0.5 . 777 372 198 ASN N N 110.75 0.1 . 778 373 199 PRO C C 173.36 0.5 . 779 373 199 PRO CA C 61.01 0.5 . 780 373 199 PRO CB C 27.68 0.5 . 781 374 200 HIS H H 9.06 0.05 . 782 374 200 HIS C C 168.53 0.5 . 783 374 200 HIS CA C 52.25 0.5 . 784 374 200 HIS CB C 28.25 0.5 . 785 374 200 HIS N N 118.14 0.1 . 786 375 201 GLU H H 9.18 0.05 . 787 375 201 GLU C C 171.23 0.5 . 788 375 201 GLU CA C 50.25 0.5 . 789 375 201 GLU CB C 30.81 0.5 . 790 375 201 GLU N N 116.57 0.1 . 791 376 202 VAL H H 9.33 0.05 . 792 376 202 VAL C C 174.48 0.5 . 793 376 202 VAL CA C 59.28 0.5 . 794 376 202 VAL CB C 28.26 0.5 . 795 376 202 VAL N N 123.09 0.1 . 796 377 203 GLN H H 8.8 0.05 . 797 377 203 GLN C C 169.13 0.5 . 798 377 203 GLN CA C 52.39 0.5 . 799 377 203 GLN CB C 23.03 0.5 . 800 377 203 GLN N N 127.7 0.1 . 801 380 206 TYR C C 171.09 0.5 . 802 380 206 TYR CA C 54.84 0.5 . 803 380 206 TYR CB C 34.94 0.5 . 804 381 207 ALA H H 7.79 0.05 . 805 381 207 ALA C C 172.64 0.5 . 806 381 207 ALA CA C 47.43 0.5 . 807 381 207 ALA CB C 18.56 0.5 . 808 381 207 ALA N N 121.55 0.1 . 809 382 208 THR H H 8.24 0.05 . 810 382 208 THR C C 170.58 0.5 . 811 382 208 THR CA C 61.73 0.5 . 812 382 208 THR CB C 65.32 0.5 . 813 382 208 THR N N 115.68 0.1 . 814 383 209 ARG H H 8.49 0.05 . 815 383 209 ARG C C 172.26 0.5 . 816 383 209 ARG CA C 51.18 0.5 . 817 383 209 ARG CB C 31.37 0.5 . 818 383 209 ARG N N 130.26 0.1 . 819 384 210 TYR H H 9.88 0.05 . 820 384 210 TYR C C 173.94 0.5 . 821 384 210 TYR CA C 54.3 0.5 . 822 384 210 TYR CB C 41.07 0.5 . 823 384 210 TYR N N 126.85 0.1 . 824 385 211 ALA H H 8.7 0.05 . 825 385 211 ALA C C 172.61 0.5 . 826 385 211 ALA CA C 49.34 0.5 . 827 385 211 ALA CB C 19.43 0.5 . 828 385 211 ALA N N 121.86 0.1 . 829 391 217 PHE C C 173.14 0.5 . 830 391 217 PHE CA C 52.73 0.5 . 831 392 218 ASP H H 8.51 0.05 . 832 392 218 ASP C C 173.85 0.5 . 833 392 218 ASP CA C 50.02 0.5 . 834 392 218 ASP CB C 41.55 0.5 . 835 392 218 ASP N N 119.39 0.1 . 836 393 219 ALA H H 9.48 0.05 . 837 393 219 ALA C C 178.13 0.5 . 838 393 219 ALA CA C 52.45 0.5 . 839 393 219 ALA CB C 16.3 0.5 . 840 393 219 ALA N N 128.48 0.1 . 841 394 220 ASP H H 8.31 0.05 . 842 394 220 ASP C C 175.84 0.5 . 843 394 220 ASP CA C 54.1 0.5 . 844 394 220 ASP CB C 37.43 0.5 . 845 394 220 ASP N N 117.79 0.1 . 846 395 221 GLU H H 8.95 0.05 . 847 395 221 GLU C C 176.36 0.5 . 848 395 221 GLU CA C 56.95 0.5 . 849 395 221 GLU CB C 27.36 0.5 . 850 395 221 GLU N N 121.93 0.1 . 851 396 222 ARG H H 8.87 0.05 . 852 396 222 ARG C C 174.3 0.5 . 853 396 222 ARG CA C 53.93 0.5 . 854 396 222 ARG N N 117.89 0.1 . 855 397 223 ALA H H 7.51 0.05 . 856 397 223 ALA C C 176.79 0.5 . 857 397 223 ALA CA C 51.9 0.5 . 858 397 223 ALA CB C 14.53 0.5 . 859 397 223 ALA N N 118.35 0.1 . 860 398 224 ARG H H 7.55 0.05 . 861 398 224 ARG C C 175.59 0.5 . 862 398 224 ARG CA C 55.43 0.5 . 863 398 224 ARG CB C 26.63 0.5 . 864 398 224 ARG N N 116.67 0.1 . 865 399 225 ALA H H 7.78 0.05 . 866 399 225 ALA CA C 50.79 0.5 . 867 399 225 ALA CB C 15.28 0.5 . 868 399 225 ALA N N 121.17 0.1 . 869 400 226 LYS H H 7.24 0.05 . 870 400 226 LYS C C 174.01 0.5 . 871 400 226 LYS CA C 53.94 0.5 . 872 400 226 LYS CB C 29.58 0.5 . 873 400 226 LYS N N 114.84 0.1 . 874 401 227 VAL H H 7.37 0.05 . 875 401 227 VAL C C 172.52 0.5 . 876 401 227 VAL CA C 59.44 0.5 . 877 401 227 VAL CB C 28.65 0.5 . 878 401 227 VAL N N 117.92 0.1 . 879 402 228 LYS H H 7.65 0.05 . 880 402 228 LYS C C 178.52 0.5 . 881 402 228 LYS CA C 54.71 0.5 . 882 402 228 LYS CB C 30.1 0.5 . 883 402 228 LYS N N 129.11 0.1 . stop_ save_ save_heteronuclear_T1_list_1 _Saveframe_category T1_relaxation _Details . loop_ _Sample_label $sample_t1t2noe stop_ _Sample_conditions_label $sample_conditions_1 _Spectrometer_frequency_1H 900 _T1_coherence_type Iz _T1_value_units s _Mol_system_component_name PHD2 _Text_data_format . _Text_data . loop_ _T1_ID _Residue_seq_code _Residue_label _Atom_name _T1_value _T1_value_error 1 8 ASN H 1.05717 . 2 9 GLY H 0.82476 . 3 10 GLN H 0.80212 . 4 11 THR H 0.9126 . 5 12 LYS H 1.05105 . 6 14 LEU H 0.99992 . 7 16 ALA H 1.23999 . 8 17 LEU H 1.32721 . 9 18 LYS H 1.33144 . 10 19 LEU H 1.39388 . 11 20 ALA H 1.31712 . 12 21 LEU H 1.49717 . 13 22 GLU H 1.62453 . 14 23 TYR H 1.424 . 15 24 ILE H 1.45536 . 16 25 VAL H 1.44987 . 17 27 CYS H 1.47977 . 18 28 MET H 1.57299 . 19 29 ASN H 1.50039 . 20 30 LYS H 1.5355 . 21 31 HIS H 1.54251 . 22 32 GLY H 1.57495 . 23 33 ILE H 1.44387 . 24 35 VAL H 1.48814 . 25 38 ASP H 1.57299 . 26 39 PHE H 1.4556 . 27 41 GLY H 1.58791 . 28 42 LYS H 1.50142 . 29 43 GLU H 1.47219 . 30 44 THR H 1.50174 . 31 45 GLY H 1.42874 . 32 46 GLN H 1.45582 . 33 47 GLN H 1.5007 . 34 48 ILE H 1.49994 . 35 49 GLY H 1.52343 . 36 50 ASP H 1.49609 . 37 51 GLU H 1.48721 . 38 52 VAL H 1.55617 . 39 53 ARG H 1.51109 . 40 54 ALA H 1.44436 . 41 55 LEU H 1.52293 . 42 56 HIS H 1.434 . 43 57 ASP H 1.4366 . 44 58 THR H 1.47634 . 45 59 GLY H 1.27832 . 46 60 LYS H 1.34327 . 47 61 PHE H 1.40446 . 48 62 THR H 1.54123 . 49 63 ASP H 1.47053 . 50 64 GLY H 1.10492 . 51 69 GLN H 1.25196 . 52 71 SER H 0.96806 . 53 72 ASP H 0.94507 . 54 73 SER H 0.89539 . 55 74 SER H 0.88421 . 56 75 LYS H 1.03808 . 57 76 ASP H 1.11183 . 58 77 ILE H 1.30618 . 59 78 ARG H 1.54138 . 60 79 GLY H 1.67739 . 61 80 ASP H 1.293 . 62 81 LYS H 1.52211 . 63 82 ILE H 1.52147 . 64 83 THR H 1.50942 . 65 84 TRP H 1.60187 . 66 85 ILE H 1.61599 . 67 86 GLU H 1.48857 . 68 87 GLY H 1.51182 . 69 88 LYS H 1.52477 . 70 89 GLU H 1.48794 . 71 91 GLY H 1.61451 . 72 92 CYS H 1.52899 . 73 93 GLU H 1.34575 . 74 95 ILE H 1.46337 . 75 96 GLY H 1.52088 . 76 97 LEU H 1.41856 . 77 104 ASP H 1.34906 . 78 110 ASN H 1.30621 . 79 111 GLY H 1.33584 . 80 112 LYS H 1.19346 . 81 113 LEU H 1.5007 . 82 114 GLY H 0.96694 . 83 115 SER H 1.50503 . 84 116 TYR H 1.50779 . 85 117 LYS H 1.58509 . 86 118 ILE H 1.68163 . 87 120 GLY H 1.31411 . 88 121 ARG H 1.15304 . 89 122 THR H 1.4801 . 90 123 LYS H 1.636 . 91 124 ALA H 1.47053 . 92 125 MET H 1.58111 . 93 126 VAL H 1.50679 . 94 127 ALA H 1.53355 . 95 128 CYS H 1.61181 . 96 129 TYR H 1.56629 . 97 131 GLY H 1.63886 . 98 132 ASN H 1.59229 . 99 133 GLY H 1.59318 . 100 134 THR H 1.53433 . 101 135 GLY H 1.75105 . 102 136 TYR H 1.47629 . 103 138 ARG H 1.33003 . 104 139 HIS H 1.47143 . 105 141 ASP H 1.47629 . 106 142 ASN H 1.48942 . 107 145 GLY H 1.5824 . 108 146 ASP H 1.44695 . 109 147 GLY H 1.101 . 110 150 VAL H 1.47317 . 111 151 THR H 1.47577 . 112 156 LEU H 1.63223 . 113 157 ASN H 1.50995 . 114 158 LYS H 1.53237 . 115 159 ASP H 1.3589 . 116 160 TRP H 1.57855 . 117 161 ASP H 1.68963 . 118 163 LYS H 1.39385 . 119 164 VAL H 1.59582 . 120 165 SER H 1.57295 . 121 166 GLY H 1.4077 . 122 168 ILE H 1.28664 . 123 169 LEU H 1.56359 . 124 170 ARG H 1.47798 . 125 171 ILE H 1.57947 . 126 172 PHE H 1.54726 . 127 174 GLU H 1.45576 . 128 175 GLY H 1.3914 . 129 176 LYS H 1.30772 . 130 177 ALA H 1.25196 . 131 178 GLN H 1.48332 . 132 179 PHE H 1.42819 . 133 180 ALA H 1.50817 . 134 181 ASP H 1.69128 . 135 182 ILE H 1.71649 . 136 185 LYS H 1.48426 . 137 186 PHE H 1.53598 . 138 187 ASP H 1.44472 . 139 193 TRP H 1.44598 . 140 194 SER H 1.57735 . 141 195 ASP H 1.50189 . 142 196 ARG H 1.56369 . 143 197 ARG H 1.36387 . 144 198 ASN H 1.069 . 145 200 HIS H 1.31307 . 146 201 GLU H 1.5612 . 147 202 VAL H 1.57341 . 148 203 GLN H 1.54107 . 149 207 ALA H 1.58649 . 150 208 THR H 1.60724 . 151 209 ARG H 1.60215 . 152 210 TYR H 1.49565 . 153 211 ALA H 1.56566 . 154 219 ALA H 1.397 . 155 220 ASP H 1.05717 . 156 221 GLU H 1.56397 . 157 222 ARG H 1.51643 . 158 223 ALA H 1.28128 . 159 224 ARG H 1.43728 . 160 225 ALA H 1.33401 . 161 226 LYS H 1.34619 . 162 227 VAL H 0.92315 . 163 228 LYS H 0.84591 . stop_ save_ save_heteronuclear_T2_list_1 _Saveframe_category T2_relaxation _Details . loop_ _Sample_label $sample_t1t2noe stop_ _Sample_conditions_label $sample_conditions_1 _Spectrometer_frequency_1H 900 _T2_coherence_type I(+,-) _T2_value_units ms _Mol_system_component_name PHD2 _Text_data_format . _Text_data . loop_ _T2_ID _Residue_seq_code _Residue_label _Atom_name _T2_value _T2_value_error _Rex_value _Rex_error 1 8 ASN H 116.40213 . . . 2 9 GLY H 210.65616 . . . 3 10 GLN H 225.65928 . . . 4 11 THR H 143.31008 . . . 5 12 LYS H 107.20944 . . . 6 14 LEU H 86.44546 . . . 7 16 ALA H 51.44398 . . . 8 17 LEU H 51.43217 . . . 9 18 LYS H 51.844 . . . 10 19 LEU H 48.343 . . . 11 20 ALA H 47.99304 . . . 12 21 LEU H 54.08712 . . . 13 22 GLU H 53.62943 . . . 14 23 TYR H 53.002 . . . 15 24 ILE H 45.598 . . . 16 25 VAL H 48.23255 . . . 17 27 CYS H 49.07643 . . . 18 28 MET H 48.83413 . . . 19 29 ASN H 46.58392 . . . 20 30 LYS H 48.00285 . . . 21 31 HIS H 57.416 . . . 22 32 GLY H 49.744 . . . 23 33 ILE H 49.39493 . . . 24 35 VAL H 49.431 . . . 25 38 ASP H 48.83413 . . . 26 39 PHE H 47.622 . . . 27 41 GLY H 49.88 . . . 28 42 LYS H 45.52215 . . . 29 43 GLU H 50.10384 . . . 30 44 THR H 49.29069 . . . 31 45 GLY H 48.32198 . . . 32 46 GLN H 44.38211 . . . 33 47 GLN H 47.54467 . . . 34 48 ILE H 47.94929 . . . 35 49 GLY H 43.642 . . . 36 50 ASP H 46.63685 . . . 37 51 GLU H 48.08901 . . . 38 52 VAL H 45.75824 . . . 39 53 ARG H 44.90151 . . . 40 54 ALA H 46.5714 . . . 41 55 LEU H 46.79503 . . . 42 56 HIS H 43.69 . . . 43 57 ASP H 47.429 . . . 44 58 THR H 51.85651 . . . 45 59 GLY H 51.44019 . . . 46 60 LYS H 53.23756 . . . 47 61 PHE H 42.867 . . . 48 62 THR H 50.847 . . . 49 63 ASP H 59.11848 . . . 50 64 GLY H 42.072 . . . 51 69 GLN H 73.72635 . . . 52 71 SER H 98.79173 . . . 53 72 ASP H 94.37469 . . . 54 73 SER H 94.16006 . . . 55 74 SER H 55.45241 . . . 56 75 LYS H 71.5609 . . . 57 76 ASP H 29.56349 . . . 58 77 ILE H 59.174 . . . 59 78 ARG H 24.142 . . . 60 79 GLY H 49.081 . . . 61 80 ASP H 33.935 . . . 62 81 LYS H 57.447 . . . 63 82 ILE H 49.594 . . . 64 83 THR H 50.395 . . . 65 84 TRP H 57.93219 . . . 66 85 ILE H 56.72609 . . . 67 86 GLU H 55.095 . . . 68 87 GLY H 54.812 . . . 69 88 LYS H 56.471 . . . 70 89 GLU H 53.672 . . . 71 91 GLY H 57.46043 . . . 72 92 CYS H 56.32398 . . . 73 93 GLU H 49.67923 . . . 74 95 ILE H 53.51499 . . . 75 96 GLY H 47.946 . . . 76 97 LEU H 52.08578 . . . 77 104 ASP H 40.627 . . . 78 110 ASN H 53.92058 . . . 79 111 GLY H 66.313 . . . 80 112 LYS H 58.72628 . . . 81 113 LEU H 58.005 . . . 82 114 GLY H 65.258 . . . 83 115 SER H 49.497 . . . 84 116 TYR H 51.36767 . . . 85 117 LYS H 55.355 . . . 86 118 ILE H 58.426 . . . 87 120 GLY H 44.35619 . . . 88 123 LYS H 51.084 . . . 89 124 ALA H 59.11848 . . . 90 125 MET H 51.679 . . . 91 126 VAL H 46.909 . . . 92 127 ALA H 47.54649 . . . 93 128 CYS H 49.027 . . . 94 129 TYR H 39.015 . . . 95 131 GLY H 44.335 . . . 96 132 ASN H 45.84081 . . . 97 133 GLY H 43.75775 . . . 98 134 THR H 24.359 . . . 99 135 GLY H 11.586 . . . 100 136 TYR H 47.343 . . . 101 138 ARG H 51.43 . . . 102 139 HIS H 31.22698 . . . 103 140 VAL H 27.61721 . . . 104 141 ASP H 35.91287 . . . 105 142 ASN H 28.60743 . . . 106 145 GLY H 57.23998 . . . 107 146 ASP H 50.24229 . . . 108 147 GLY H 25.93984 . . . 109 149 CYS H 41.716 . . . 110 150 VAL H 53.39933 . . . 111 151 THR H 58.69818 . . . 112 156 LEU H 50.2626 . . . 113 157 ASN H 54.80442 . . . 114 158 LYS H 41.16066 . . . 115 159 ASP H 20.9564 . . . 116 160 TRP H 37.53823 . . . 117 161 ASP H 42.67508 . . . 118 163 LYS H 50.13243 . . . 119 164 VAL H 48.47364 . . . 120 165 SER H 55.29033 . . . 121 166 GLY H 47.42846 . . . 122 167 GLY H 46.242 . . . 123 168 ILE H 44.07763 . . . 124 169 LEU H 42.59222 . . . 125 170 ARG H 43.47 . . . 126 171 ILE H 52.77445 . . . 127 172 PHE H 57.962 . . . 128 174 GLU H 54.9684 . . . 129 175 GLY H 65.35472 . . . 130 176 LYS H 61.48385 . . . 131 177 ALA H 73.72635 . . . 132 178 GLN H 86.08288 . . . 133 179 PHE H 64.41538 . . . 134 180 ALA H 52.44141 . . . 135 181 ASP H 58.39911 . . . 136 182 ILE H 51.821 . . . 137 185 LYS H 44.74066 . . . 138 186 PHE H 37.9929 . . . 139 187 ASP H 49.63345 . . . 140 193 TRP H 49.545 . . . 141 194 SER H 43.66798 . . . 142 195 ASP H 43.6225 . . . 143 196 ARG H 51.74409 . . . 144 197 ARG H 37.80942 . . . 145 200 HIS H 37.50552 . . . 146 201 GLU H 47.788 . . . 147 202 VAL H 47.63782 . . . 148 203 GLN H 47.29032 . . . 149 207 ALA H 44.56589 . . . 150 208 THR H 44.76325 . . . 151 209 ARG H 35.995 . . . 152 210 TYR H 45.827 . . . 153 211 ALA H 50.65237 . . . 154 218 ASP H 55.223 . . . 155 219 ALA H 36.67544 . . . 156 221 GLU H 45.65115 . . . 157 222 ARG H 43.26397 . . . 158 223 ALA H 43.33514 . . . 159 224 ARG H 52.9565 . . . 160 225 ALA H 49.32 . . . 161 226 LYS H 31.7919 . . . 162 227 VAL H 73.77 . . . 163 228 LYS H 194.378 . . . stop_ save_ save_heteronuclear_noe_list_1 _Saveframe_category heteronuclear_NOE _Details . loop_ _Experiment_label '3D Heteronuclear NOE' '2D 1H-15N HSQC' stop_ loop_ _Sample_label $sample_t1t2noe stop_ _Sample_conditions_label $sample_conditions_1 _Spectrometer_frequency_1H 900 _Mol_system_component_name PHD2 _Atom_one_atom_name N _Atom_two_atom_name H _Heteronuclear_NOE_value_type 'peak height' _NOE_reference_value 20000000 _NOE_reference_description . _Text_data_format . _Text_data . loop_ _Residue_seq_code _Residue_label _Heteronuclear_NOE_value _Heteronuclear_NOE_value_error 8 ASN 0.2743 . 9 GLY 0.2037 . 10 GLN 0.172 . 11 THR 0.2396 . 12 LYS 0.4211 . 14 LEU 0.4572 . 16 ALA 0.762 . 17 LEU 0.7934 . 18 LYS 0.7604 . 19 LEU 0.8149 . 20 ALA 0.896 . 21 LEU 0.8442 . 22 GLU 0.8392 . 23 TYR 0.8563 . 24 ILE 0.8463 . 25 VAL 0.8395 . 27 CYS 0.8753 . 28 MET 0.9014 . 29 ASN 0.8716 . 30 LYS 0.9219 . 31 HIS 0.849 . 32 GLY 0.8691 . 33 ILE 0.8815 . 35 VAL 0.8729 . 38 ASP 0.9014 . 39 PHE 0.9077 . 41 GLY 0.7668 . 42 LYS 0.8829 . 43 GLU 0.7893 . 44 THR 0.8495 . 45 GLY 0.8608 . 46 GLN 0.8624 . 47 GLN 0.8658 . 48 ILE 0.8837 . 49 GLY 0.8723 . 50 ASP 0.8756 . 51 GLU 0.8745 . 52 VAL 0.8307 . 53 ARG 0.889 . 54 ALA 0.8762 . 55 LEU 0.8658 . 56 HIS 0.8511 . 57 ASP 0.8815 . 58 THR 0.8179 . 59 GLY 0.764 . 60 LYS 0.7029 . 61 PHE 0.767 . 62 THR 0.8208 . 63 ASP 0.7486 . 64 GLY 0.8039 . 69 GLN 0.6529 . 71 SER 0.5714 . 72 ASP 0.5951 . 73 SER 0.5464 . 74 SER 0.5783 . 75 LYS 0.6813 . 76 ASP 0.6918 . 77 ILE 0.6919 . 78 ARG 0.862 . 79 GLY 0.9151 . 80 ASP 0.9032 . 81 LYS 0.9032 . 82 ILE 0.8477 . 83 THR 0.8477 . 84 TRP 0.883 . 85 ILE 0.8376 . 86 GLU 0.8771 . 87 GLY 0.8972 . 88 LYS 0.7492 . 89 GLU 0.8673 . 91 GLY 0.8275 . 92 CYS 0.8682 . 93 GLU 0.8895 . 94 THR 0.908 . 95 ILE 0.8567 . 96 GLY 0.873 . 97 LEU 0.8699 . 104 ASP 0.8792 . 110 ASN 0.8554 . 111 GLY 0.7455 . 112 LYS 0.8611 . 113 LEU 0.8011 . 114 GLY 0.8101 . 115 SER 0.8132 . 116 TYR 0.8469 . 117 LYS 0.8162 . 118 ILE 0.8443 . 120 GLY 0.826 . 121 ARG 0.892 . 122 THR 0.8432 . 123 LYS 0.8989 . 124 ALA 0.7868 . 125 MET 0.8352 . 126 VAL 0.8724 . 127 ALA 0.8834 . 128 CYS 0.8749 . 129 TYR 0.8235 . 131 GLY 0.8117 . 132 ASN 0.859 . 133 GLY 0.8996 . 134 THR 0.9152 . 135 GLY 0.8171 . 136 TYR 0.9193 . 138 ARG 0.8203 . 139 HIS 0.8999 . 140 VAL 0.8909 . 141 ASP 0.9193 . 142 ASN 0.9044 . 145 GLY 0.757 . 146 ASP 0.917 . 147 GLY 0.9441 . 149 CYS 0.8954 . 150 VAL 0.9078 . 151 THR 0.8671 . 156 LEU 0.8251 . 157 ASN 0.8498 . 158 LYS 0.8194 . 159 ASP 0.7484 . 160 TRP 0.7317 . 161 ASP 0.8326 . 163 LYS 0.8978 . 164 VAL 0.8353 . 165 SER 0.8543 . 166 GLY 0.9328 . 167 GLY 0.8303 . 168 ILE 0.989 . 169 LEU 0.8739 . 170 ARG 0.9248 . 171 ILE 0.8759 . 172 PHE 0.8692 . 174 GLU 0.8229 . 175 GLY 0.6807 . 176 LYS 0.6819 . 177 ALA 0.6529 . 178 GLN 0.4647 . 179 PHE 0.576 . 180 ALA 0.8261 . 181 ASP 0.9276 . 182 ILE 0.8905 . 185 LYS 0.8872 . 186 PHE 0.8281 . 187 ASP 0.8792 . 193 TRP 0.8884 . 194 SER 0.8884 . 195 ASP 0.8725 . 196 ARG 0.8796 . 197 ARG 0.883 . 200 HIS 0.9123 . 201 GLU 0.9022 . 202 VAL 0.8281 . 203 GLN 0.9098 . 207 ALA 0.9021 . 208 THR 0.8932 . 209 ARG 0.8652 . 210 TYR 0.9541 . 211 ALA 0.9003 . 218 ASP 0.8968 . 219 ALA 0.8294 . 220 ASP 0.6801 . 221 GLU 0.8654 . 222 ARG 0.8851 . 223 ALA 0.855 . 224 ARG 0.8194 . 225 ALA 0.7457 . 226 LYS 0.6751 . 227 VAL 0.5308 . 228 LYS 0.284 . stop_ save_