data_6713 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Backbone 1H, 13C, and 15N Chemical Shift Assignments for PB1 domain of P40phox ; _BMRB_accession_number 6713 _BMRB_flat_file_name bmr6713.str _Entry_type original _Submission_date 2005-06-30 _Accession_date 2005-06-30 _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 Chenavas Sylvie . . 2 Simorre Jean-Pierre . . 3 Dubosclard Virginie . . 4 Pebay-Peyroula Eva . . 5 Gans Pierre . . 6 Brutscher Bernhard . . 7 Fieschi Franck . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 86 "13C chemical shifts" 269 "15N chemical shifts" 85 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2007-04-11 original author . stop_ _Original_release_date 2007-04-11 save_ ############################# # Citation for this entry # ############################# save_1 _Saveframe_category entry_citation _Citation_full . _Citation_title ; NMR characterization of free and complexed p67phox and p40phox PB1 domains in solution ; _Citation_status 'in preparation' _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID ? loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 chenavas sylvie . . 2 simorre jean-pierre . . 3 dubosclard virginie . . 4 pebay-peyroula eva . . 5 gans pierre . . 6 brutscher bernhard . . 7 fieschi franck . . stop_ _Journal_abbreviation 'Eur. J. Biochem.' _Journal_volume . _Journal_issue . _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first . _Page_last . _Year . _Details . loop_ _Keyword 'NADPH oxidase' 'PB1 domains' stop_ save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name 'PB1 domain of p40phox' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'PB1 domain of p40phox' $PB1_p40phox_polypeptide stop_ _System_molecular_weight 13000 _System_physical_state native _System_oligomer_state protein _System_paramagnetic no _System_thiol_state 'all free' loop_ _Biological_function 'Activation NADPH oxidase' 'Signal transduction' stop_ _Database_query_date . _Details 'Scaffolding domain' save_ ######################## # Monomeric polymers # ######################## save_PB1_p40phox_polypeptide _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'PB1 p40' _Molecular_mass . _Mol_thiol_state 'all free' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 109 _Mol_residue_sequence ; PEEDDPTNWLRCYYYEDTIS TIKDIAVEEDLSSTPLLKDL LELTRREFQREDIALNYRDA EGDLVRLLSDEDVALMVRQA RGLPSQKRLFPWKLHITQKD NYRVYNTMP ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 231 PRO 2 232 GLU 3 233 GLU 4 234 ASP 5 235 ASP 6 236 PRO 7 237 THR 8 238 ASN 9 239 TRP 10 240 LEU 11 241 ARG 12 242 CYS 13 243 TYR 14 244 TYR 15 245 TYR 16 246 GLU 17 247 ASP 18 248 THR 19 249 ILE 20 250 SER 21 251 THR 22 252 ILE 23 253 LYS 24 254 ASP 25 255 ILE 26 256 ALA 27 257 VAL 28 258 GLU 29 259 GLU 30 260 ASP 31 261 LEU 32 262 SER 33 263 SER 34 264 THR 35 265 PRO 36 266 LEU 37 267 LEU 38 268 LYS 39 269 ASP 40 270 LEU 41 271 LEU 42 272 GLU 43 273 LEU 44 274 THR 45 275 ARG 46 276 ARG 47 277 GLU 48 278 PHE 49 279 GLN 50 280 ARG 51 281 GLU 52 282 ASP 53 283 ILE 54 284 ALA 55 285 LEU 56 286 ASN 57 287 TYR 58 288 ARG 59 289 ASP 60 290 ALA 61 291 GLU 62 292 GLY 63 293 ASP 64 294 LEU 65 295 VAL 66 296 ARG 67 297 LEU 68 298 LEU 69 299 SER 70 300 ASP 71 301 GLU 72 302 ASP 73 303 VAL 74 304 ALA 75 305 LEU 76 306 MET 77 307 VAL 78 308 ARG 79 309 GLN 80 310 ALA 81 311 ARG 82 312 GLY 83 313 LEU 84 314 PRO 85 315 SER 86 316 GLN 87 317 LYS 88 318 ARG 89 319 LEU 90 320 PHE 91 321 PRO 92 322 TRP 93 323 LYS 94 324 LEU 95 325 HIS 96 326 ILE 97 327 THR 98 328 GLN 99 329 LYS 100 330 ASP 101 331 ASN 102 332 TYR 103 333 ARG 104 334 VAL 105 335 TYR 106 336 ASN 107 337 THR 108 338 MET 109 339 PRO stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-01-28 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 PDB 1OEY "Heterodimer Of P40phox And P67phox Pb1 Domains From Human Nadph Oxidase" 94.50 107 97.09 97.09 2.34e-64 PDB 2DYB "The Crystal Structure Of Human P40(Phox)" 100.00 341 100.00 100.00 6.19e-71 DBJ BAA89792 "p40phox [Homo sapiens]" 100.00 339 100.00 100.00 6.81e-71 DBJ BAD97044 "neutrophil cytosolic factor 4 (40kD) isoform 1 variant [Homo sapiens]" 100.00 339 99.08 99.08 4.18e-70 DBJ BAG72652 "neutrophil cytosolic factor 4 [synthetic construct]" 100.00 339 100.00 100.00 6.81e-71 EMBL CAA54372 "p40phox protein [Homo sapiens]" 100.00 339 100.00 100.00 7.19e-71 EMBL CAG30414 "NCF4 [Homo sapiens]" 100.00 339 100.00 100.00 6.81e-71 EMBL CAG46875 "NCF4 [Homo sapiens]" 100.00 339 100.00 100.00 7.27e-71 EMBL CAK54559 "NCF4 [synthetic construct]" 100.00 339 100.00 100.00 6.81e-71 EMBL CAK54858 "NCF4 [synthetic construct]" 100.00 339 100.00 100.00 6.81e-71 GB AAB39970 "p40-phox [Homo sapiens]" 100.00 339 100.00 100.00 7.19e-71 GB EAW60123 "neutrophil cytosolic factor 4, 40kDa, isoform CRA_b [Homo sapiens]" 100.00 339 100.00 100.00 6.81e-71 REF NP_000622 "neutrophil cytosol factor 4 isoform 1 [Homo sapiens]" 100.00 339 100.00 100.00 6.81e-71 REF XP_002831119 "PREDICTED: neutrophil cytosol factor 4 [Pongo abelii]" 100.00 339 98.17 98.17 4.85e-69 REF XP_003821585 "PREDICTED: neutrophil cytosol factor 4 isoform X2 [Pan paniscus]" 100.00 339 99.08 100.00 2.44e-70 REF XP_004063463 "PREDICTED: neutrophil cytosol factor 4 [Gorilla gorilla gorilla]" 100.00 339 100.00 100.00 6.81e-71 REF XP_009436715 "PREDICTED: neutrophil cytosol factor 4 [Pan troglodytes]" 100.00 388 99.08 100.00 8.68e-70 SP Q15080 "RecName: Full=Neutrophil cytosol factor 4; Short=NCF-4; AltName: Full=Neutrophil NADPH oxidase factor 4; AltName: Full=SH3 and " 100.00 339 100.00 100.00 6.81e-71 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species _Tissue $PB1_p40phox_polypeptide Human 9606 Eukaryota Metazoa Homo sapiens lymphoid 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 $PB1_p40phox_polypeptide 'recombinant technology' 'E. coli' . . BL21(DE3) . stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_15N_PB1_p40 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $PB1_p40phox_polypeptide 0.3 mM '[U-98% 15N]' HEPES 50 mM . NaCl 30 mM . stop_ save_ save_15N_13C_PB1_p40 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $PB1_p40phox_polypeptide 0.3 mM '[U-98% 15N; U-97% 13C]' HEPES 50 mM . NaCl 30 mM . stop_ save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_600MHz_spectrometer _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model Inova _Field_strength 600 _Details . save_ save_800MHz_spectrometer _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model Inova _Field_strength 800 _Details . save_ ############################# # NMR applied experiments # ############################# save_3D-HNCA_1 _Saveframe_category NMR_applied_experiment _Experiment_name 3D-HNCA _Sample_label . save_ save_3D-HNCO_2 _Saveframe_category NMR_applied_experiment _Experiment_name 3D-HNCO _Sample_label . save_ save_3D-HNCACB_3 _Saveframe_category NMR_applied_experiment _Experiment_name 3D-HNCACB _Sample_label . save_ save_3D-DEPT-CBCA(CO)NH_4 _Saveframe_category NMR_applied_experiment _Experiment_name 3D-DEPT-CBCA(CO)NH _Sample_label . save_ save_3D-HNCA _Saveframe_category NMR_applied_experiment _Experiment_name 3D-HNCA _BMRB_pulse_sequence_accession_number . _Details . save_ ####################### # Sample conditions # ####################### save_conditions_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 7.5 0.1 pH temperature 298 0.3 K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_referencing _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 0.0 . indirect . . . 0.251449530 water H 1 protons ppm 4.773 internal direct . . . 1.0 DSS N 15 'methyl protons' ppm 0.0 . 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_chem_shift_list_1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Sample_label $15N_13C_PB1_p40 stop_ _Sample_conditions_label $conditions_1 _Chem_shift_reference_set_label $chemical_shift_referencing _Mol_system_component_name 'PB1 domain of p40phox' _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 1 231 1 PRO C C 173.1 0.2 1 2 231 1 PRO CA C 62.7 0.2 1 3 231 1 PRO CB C 33.9 0.2 1 4 232 2 GLU H H 8.61 0.02 1 5 232 2 GLU C C 174.5 0.2 1 6 232 2 GLU CA C 57.1 0.2 1 7 232 2 GLU CB C 30.3 0.2 1 8 232 2 GLU N N 122.5 0.2 1 9 233 3 GLU H H 8.32 0.02 1 10 233 3 GLU C C 176 0.2 1 11 233 3 GLU CA C 56.6 0.2 1 12 233 3 GLU CB C 31.1 0.2 1 13 233 3 GLU N N 122.5 0.2 1 14 234 4 ASP H H 8.95 0.02 1 15 234 4 ASP C C 175 0.2 1 16 234 4 ASP CA C 56.3 0.2 1 17 234 4 ASP CB C 40.1 0.2 1 18 234 4 ASP N N 122.2 0.2 1 19 235 5 ASP H H 9.07 0.02 1 20 235 5 ASP N N 125.5 0.2 1 21 236 6 PRO C C 172.9 0.2 1 22 236 6 PRO CA C 63.2 0.2 1 23 236 6 PRO CB C 31.8 0.2 1 24 237 7 THR H H 7.69 0.02 1 25 237 7 THR C C 176.2 0.2 1 26 237 7 THR CA C 64.2 0.2 1 27 237 7 THR CB C 69.1 0.2 1 28 237 7 THR N N 117.7 0.2 1 29 238 8 ASN H H 7.95 0.02 1 30 238 8 ASN C C 175.8 0.2 1 31 238 8 ASN CA C 52.2 0.2 1 32 238 8 ASN CB C 41.2 0.2 1 33 238 8 ASN N N 123.3 0.2 1 34 239 9 TRP H H 8.39 0.02 1 35 239 9 TRP C C 175.4 0.2 1 36 239 9 TRP CA C 56 0.2 1 37 239 9 TRP CB C 32.1 0.2 1 38 239 9 TRP N N 119.2 0.2 1 39 240 10 LEU H H 9.45 0.02 1 40 240 10 LEU C C 171 0.2 1 41 240 10 LEU CA C 53 0.2 1 42 240 10 LEU CB C 45.2 0.2 1 43 240 10 LEU N N 125.9 0.2 1 44 241 11 ARG H H 8.42 0.02 1 45 241 11 ARG CA C 58 0.2 1 46 241 11 ARG CB C 37.4 0.2 1 47 241 11 ARG N N 123.7 0.2 1 48 244 14 TYR C C 174.4 0.2 1 49 244 14 TYR CA C 56.4 0.2 1 50 244 14 TYR CB C 40.9 0.2 1 51 245 15 TYR H H 7.95 0.02 1 52 245 15 TYR C C 174 0.2 1 53 245 15 TYR CA C 57.4 0.2 1 54 245 15 TYR CB C 38.9 0.2 1 55 245 15 TYR N N 127.6 0.2 1 56 246 16 GLU H H 8.07 0.02 1 57 246 16 GLU C C 173.3 0.2 1 58 246 16 GLU CA C 55.9 0.2 1 59 246 16 GLU CB C 30.8 0.2 1 60 246 16 GLU N N 123.8 0.2 1 61 247 17 ASP H H 8.64 0.02 1 62 247 17 ASP C C 172.8 0.2 1 63 247 17 ASP CA C 56.9 0.2 1 64 247 17 ASP CB C 40.4 0.2 1 65 247 17 ASP N N 123.6 0.2 1 66 248 18 THR H H 7.8 0.02 1 67 248 18 THR C C 174.8 0.2 1 68 248 18 THR CA C 62.1 0.2 1 69 248 18 THR CB C 69.4 0.2 1 70 248 18 THR N N 110.1 0.2 1 71 249 19 ILE H H 7.79 0.02 1 72 249 19 ILE C C 173.8 0.2 1 73 249 19 ILE CA C 60.5 0.2 1 74 249 19 ILE CB C 39.6 0.2 1 75 249 19 ILE N N 121.7 0.2 1 76 250 20 SER H H 8.27 0.02 1 77 250 20 SER C C 174.8 0.2 1 78 250 20 SER CA C 56.7 0.2 1 79 250 20 SER CB C 65.1 0.2 1 80 250 20 SER N N 120.2 0.2 1 81 251 21 THR H H 8.4 0.02 1 82 251 21 THR C C 176.2 0.2 1 83 251 21 THR CA C 60.9 0.2 1 84 251 21 THR CB C 71.5 0.2 1 85 251 21 THR N N 116.9 0.2 1 86 252 22 ILE H H 8.14 0.02 1 87 252 22 ILE C C 172.9 0.2 1 88 252 22 ILE CA C 61 0.2 1 89 252 22 ILE CB C 39.9 0.2 1 90 252 22 ILE N N 124 0.2 1 91 253 23 LYS H H 8.98 0.02 1 92 253 23 LYS C C 175.7 0.2 1 93 253 23 LYS CA C 55.5 0.2 1 94 253 23 LYS CB C 36.1 0.2 1 95 253 23 LYS N N 129.4 0.2 1 96 254 24 ASP H H 8.22 0.02 1 97 254 24 ASP C C 172.9 0.2 1 98 254 24 ASP CA C 53 0.2 1 99 254 24 ASP CB C 40.9 0.2 1 100 254 24 ASP N N 126.8 0.2 1 101 255 25 ILE H H 9.32 0.02 1 102 255 25 ILE C C 174.3 0.2 1 103 255 25 ILE CA C 60.3 0.2 1 104 255 25 ILE CB C 40.9 0.2 1 105 255 25 ILE N N 123.7 0.2 1 106 256 26 ALA H H 8.44 0.02 1 107 256 26 ALA C C 171.7 0.2 1 108 256 26 ALA CA C 52.1 0.2 1 109 256 26 ALA CB C 18.4 0.2 1 110 256 26 ALA N N 131 0.2 1 111 257 27 VAL H H 8.25 0.02 1 112 257 27 VAL C C 173.3 0.2 1 113 257 27 VAL CA C 60.9 0.2 1 114 257 27 VAL CB C 35.1 0.2 1 115 257 27 VAL N N 121.2 0.2 1 116 258 28 GLU H H 8.69 0.02 1 117 258 28 GLU C C 172.8 0.2 1 118 258 28 GLU CA C 55.8 0.2 1 119 258 28 GLU CB C 29 0.2 1 120 258 28 GLU N N 127.2 0.2 1 121 259 29 GLU H H 7.53 0.02 1 122 259 29 GLU C C 174 0.2 1 123 259 29 GLU CA C 55.8 0.2 1 124 259 29 GLU CB C 32.1 0.2 1 125 259 29 GLU N N 119.4 0.2 1 126 260 30 ASP H H 8.47 0.02 1 127 260 30 ASP C C 171.7 0.2 1 128 260 30 ASP CA C 54.6 0.2 1 129 260 30 ASP CB C 42.4 0.2 1 130 260 30 ASP N N 119.6 0.2 1 131 261 31 LEU H H 8.01 0.02 1 132 261 31 LEU C C 170.9 0.2 1 133 261 31 LEU CA C 56.7 0.2 1 134 261 31 LEU CB C 42.4 0.2 1 135 261 31 LEU N N 123.7 0.2 1 136 262 32 SER H H 8.36 0.02 1 137 262 32 SER C C 174.1 0.2 1 138 262 32 SER CA C 58.8 0.2 1 139 262 32 SER CB C 63.8 0.2 1 140 262 32 SER N N 113.4 0.2 1 141 263 33 SER H H 7.85 0.02 1 142 263 33 SER C C 175 0.2 1 143 263 33 SER CA C 59.3 0.2 1 144 263 33 SER CB C 64.6 0.2 1 145 263 33 SER N N 117.9 0.2 1 146 264 34 THR H H 8.3 0.02 1 147 264 34 THR CA C 59.5 0.2 1 148 264 34 THR CB C 69.4 0.2 1 149 264 34 THR N N 118 0.2 1 150 265 35 PRO C C 174 0.2 1 151 265 35 PRO CA C 61.9 0.2 1 152 265 35 PRO CB C 32.3 0.2 1 153 266 36 LEU H H 8.4 0.02 1 154 266 36 LEU C C 169.8 0.2 1 155 266 36 LEU CA C 53.6 0.2 1 156 266 36 LEU CB C 41.9 0.2 1 157 266 36 LEU N N 118.4 0.2 1 158 267 37 LEU H H 9.35 0.02 1 159 267 37 LEU C C 169.9 0.2 1 160 267 37 LEU CB C 40.4 0.2 1 161 267 37 LEU N N 125.1 0.2 1 162 268 38 LYS H H 9.14 0.02 1 163 268 38 LYS C C 170.7 0.2 1 164 268 38 LYS CA C 59.4 0.2 1 165 268 38 LYS CB C 31.8 0.2 1 166 268 38 LYS N N 116.1 0.2 1 167 269 39 ASP H H 6.66 0.02 1 168 269 39 ASP C C 169.9 0.2 1 169 269 39 ASP CA C 57.1 0.2 1 170 269 39 ASP CB C 40.4 0.2 1 171 269 39 ASP N N 119.1 0.2 1 172 270 40 LEU H H 7.62 0.02 1 173 270 40 LEU C C 168.6 0.2 1 174 270 40 LEU CA C 57.4 0.2 1 175 270 40 LEU CB C 42.2 0.2 1 176 270 40 LEU N N 120.2 0.2 1 177 271 41 LEU H H 8.7 0.02 1 178 271 41 LEU C C 170.9 0.2 1 179 271 41 LEU CA C 58 0.2 1 180 271 41 LEU CB C 41.9 0.2 1 181 271 41 LEU N N 122.4 0.2 1 182 272 42 GLU H H 7.73 0.02 1 183 272 42 GLU C C 169.8 0.2 1 184 272 42 GLU CA C 59.8 0.2 1 185 272 42 GLU CB C 29.3 0.2 1 186 272 42 GLU N N 118.7 0.2 1 187 273 43 LEU H H 7.75 0.02 1 188 273 43 LEU C C 170 0.2 1 189 273 43 LEU CA C 58.3 0.2 1 190 273 43 LEU CB C 43.2 0.2 1 191 273 43 LEU N N 118.6 0.2 1 192 274 44 THR H H 7.89 0.02 1 193 274 44 THR C C 171.5 0.2 1 194 274 44 THR CA C 66 0.2 1 195 274 44 THR CB C 68.9 0.2 1 196 274 44 THR N N 109 0.2 1 197 275 45 ARG H H 8.48 0.02 1 198 275 45 ARG C C 169 0.2 1 199 275 45 ARG CA C 60 0.2 1 200 275 45 ARG CB C 30.5 0.2 1 201 275 45 ARG N N 123.6 0.2 1 202 276 46 ARG H H 7.46 0.02 1 203 276 46 ARG C C 169.7 0.2 1 204 276 46 ARG CA C 59.2 0.2 1 205 276 46 ARG CB C 30.3 0.2 1 206 276 46 ARG N N 117.6 0.2 1 207 277 47 GLU H H 7.85 0.02 1 208 277 47 GLU C C 170.9 0.2 1 209 277 47 GLU CA C 58.6 0.2 1 210 277 47 GLU CB C 29.8 0.2 1 211 277 47 GLU N N 117.9 0.2 1 212 278 48 PHE H H 8.23 0.02 1 213 278 48 PHE C C 174.7 0.2 1 214 278 48 PHE CA C 59.3 0.2 1 215 278 48 PHE CB C 37.6 0.2 1 216 278 48 PHE N N 113.6 0.2 1 217 279 49 GLN H H 7.54 0.02 1 218 279 49 GLN C C 174.4 0.2 1 219 279 49 GLN CA C 56.6 0.2 1 220 279 49 GLN CB C 26 0.2 1 221 279 49 GLN N N 115.9 0.2 1 222 280 50 ARG H H 7.46 0.02 1 223 280 50 ARG C C 174.7 0.2 1 224 280 50 ARG CA C 55 0.2 1 225 280 50 ARG CB C 33.8 0.2 1 226 280 50 ARG N N 114.7 0.2 1 227 281 51 GLU H H 8.51 0.02 1 228 281 51 GLU C C 171 0.2 1 229 281 51 GLU CA C 56.7 0.2 1 230 281 51 GLU CB C 31.1 0.2 1 231 281 51 GLU N N 117.3 0.2 1 232 282 52 ASP H H 9.18 0.02 1 233 282 52 ASP C C 173.3 0.2 1 234 282 52 ASP CA C 53.6 0.2 1 235 282 52 ASP CB C 38.4 0.2 1 236 282 52 ASP N N 121.2 0.2 1 237 283 53 ILE H H 7.18 0.02 1 238 283 53 ILE C C 174.7 0.2 1 239 283 53 ILE CA C 59.4 0.2 1 240 283 53 ILE CB C 41.6 0.2 1 241 283 53 ILE N N 112.2 0.2 1 242 284 54 ALA H H 9 0.02 1 243 284 54 ALA C C 174.2 0.2 1 244 284 54 ALA CA C 50.4 0.2 1 245 284 54 ALA CB C 21.2 0.2 1 246 284 54 ALA N N 124.3 0.2 1 247 285 55 LEU H H 8.74 0.02 1 248 285 55 LEU C C 173.4 0.2 1 249 285 55 LEU CA C 54.2 0.2 1 250 285 55 LEU CB C 44.1 0.2 1 251 285 55 LEU N N 119.2 0.2 1 252 286 56 ASN H H 7.97 0.02 1 253 286 56 ASN C C 176.1 0.2 1 254 286 56 ASN CA C 51.7 0.2 1 255 286 56 ASN CB C 44.4 0.2 1 256 286 56 ASN N N 118.1 0.2 1 257 287 57 TYR H H 9.07 0.02 1 258 287 57 TYR C C 176.9 0.2 1 259 287 57 TYR CA C 55.9 0.2 1 260 287 57 TYR CB C 41.1 0.2 1 261 287 57 TYR N N 118.4 0.2 1 262 288 58 ARG H H 8.83 0.02 1 263 288 58 ARG C C 172.9 0.2 1 264 288 58 ARG CA C 54.3 0.2 1 265 288 58 ARG CB C 31.1 0.2 1 266 288 58 ARG N N 121 0.2 1 267 289 59 ASP H H 8.61 0.02 1 268 289 59 ASP C C 171.4 0.2 1 269 289 59 ASP CA C 52.8 0.2 1 270 289 59 ASP CB C 41.2 0.2 1 271 289 59 ASP N N 127 0.2 1 272 290 60 ALA H H 8.09 0.02 1 273 290 60 ALA C C 169.8 0.2 1 274 290 60 ALA CA C 54.7 0.2 1 275 290 60 ALA CB C 18.7 0.2 1 276 290 60 ALA N N 120.4 0.2 1 277 291 61 GLU H H 7.76 0.02 1 278 291 61 GLU C C 172.1 0.2 1 279 291 61 GLU CA C 55.8 0.2 1 280 291 61 GLU CB C 29.5 0.2 1 281 291 61 GLU N N 115.6 0.2 1 282 292 62 GLY H H 7.92 0.02 1 283 292 62 GLY C C 174.9 0.2 1 284 292 62 GLY CA C 44.9 0.2 1 285 292 62 GLY N N 107.7 0.2 1 286 293 63 ASP C C 174 0.2 1 287 293 63 ASP CA C 54 0.2 1 288 293 63 ASP CB C 41.4 0.2 1 289 294 64 LEU C C 172.6 0.2 1 290 294 64 LEU CA C 54.5 0.2 1 291 294 64 LEU CB C 42.4 0.2 1 292 295 65 VAL H H 8.84 0.02 1 293 295 65 VAL C C 174.1 0.2 1 294 295 65 VAL CA C 61.4 0.2 1 295 295 65 VAL CB C 33.3 0.2 1 296 295 65 VAL N N 126.7 0.2 1 297 296 66 ARG H H 8.22 0.02 1 298 296 66 ARG C C 172.6 0.2 1 299 296 66 ARG CA C 56.3 0.2 1 300 296 66 ARG CB C 31.1 0.2 1 301 296 66 ARG N N 126.3 0.2 1 302 297 67 LEU H H 8.34 0.02 1 303 297 67 LEU C C 173.9 0.2 1 304 297 67 LEU CA C 53.9 0.2 1 305 297 67 LEU CB C 42.7 0.2 1 306 297 67 LEU N N 123.5 0.2 1 307 298 68 LEU H H 9.01 0.02 1 308 298 68 LEU C C 171.9 0.2 1 309 298 68 LEU CA C 54.6 0.2 1 310 298 68 LEU CB C 43.9 0.2 1 311 298 68 LEU N N 123.5 0.2 1 312 299 69 SER H H 8.07 0.02 1 313 299 69 SER CA C 56.4 0.2 1 314 299 69 SER CB C 67.6 0.2 1 315 299 69 SER N N 114.8 0.2 1 316 300 70 ASP CA C 58.6 0.2 1 317 300 70 ASP CB C 40.7 0.2 1 318 301 71 GLU H H 8.46 0.02 1 319 301 71 GLU C C 170 0.2 1 320 301 71 GLU CA C 59.9 0.2 1 321 301 71 GLU CB C 28.8 0.2 1 322 301 71 GLU N N 122 0.2 1 323 302 72 ASP H H 7.58 0.02 1 324 302 72 ASP C C 170.8 0.2 1 325 302 72 ASP CA C 57.4 0.2 1 326 302 72 ASP CB C 41.9 0.2 1 327 302 72 ASP N N 120.7 0.2 1 328 303 73 VAL H H 7.16 0.02 1 329 303 73 VAL C C 172.3 0.2 1 330 303 73 VAL CA C 65.8 0.2 1 331 303 73 VAL CB C 31.5 0.2 1 332 303 73 VAL N N 119.1 0.2 1 333 304 74 ALA H H 7.68 0.02 1 334 304 74 ALA C C 169 0.2 1 335 304 74 ALA CA C 55.3 0.2 1 336 304 74 ALA CB C 17.4 0.2 1 337 304 74 ALA N N 120.4 0.2 1 338 305 75 LEU H H 7.5 0.02 1 339 305 75 LEU C C 171.1 0.2 1 340 305 75 LEU CA C 58.1 0.2 1 341 305 75 LEU CB C 41.2 0.2 1 342 305 75 LEU N N 120.2 0.2 1 343 306 76 MET H H 7.32 0.02 1 344 306 76 MET C C 170.1 0.2 1 345 306 76 MET CA C 59.1 0.2 1 346 306 76 MET CB C 31 0.2 1 347 306 76 MET N N 120.4 0.2 1 348 307 77 VAL H H 7.76 0.02 1 349 307 77 VAL C C 170.3 0.2 1 350 307 77 VAL CB C 31.5 0.2 1 351 307 77 VAL N N 117.9 0.2 1 352 308 78 ARG H H 7.95 0.02 1 353 308 78 ARG C C 169.5 0.2 1 354 308 78 ARG CA C 59.6 0.2 1 355 308 78 ARG CB C 30.3 0.2 1 356 308 78 ARG N N 119.8 0.2 1 357 309 79 GLN H H 8.06 0.02 1 358 309 79 GLN C C 172.1 0.2 1 359 309 79 GLN CA C 57.5 0.2 1 360 309 79 GLN CB C 28.8 0.2 1 361 309 79 GLN N N 116.3 0.2 1 362 310 80 ALA H H 7.34 0.02 1 363 310 80 ALA CA C 52.6 0.2 1 364 310 80 ALA CB C 19.5 0.2 1 365 310 80 ALA N N 121.8 0.2 1 366 311 81 ARG H H 7.92 0.02 1 367 311 81 ARG N N 119.6 0.2 1 368 312 82 GLY C C 175 0.2 1 369 312 82 GLY CA C 45 0.2 1 370 313 83 LEU H H 7.69 0.02 1 371 313 83 LEU C C 173.8 0.2 1 372 313 83 LEU CA C 53 0.2 1 373 313 83 LEU CB C 41.4 0.2 1 374 313 83 LEU N N 122.8 0.2 1 375 321 91 PRO CA C 63.2 0.2 1 376 321 91 PRO CB C 32.1 0.2 1 377 322 92 TRP H H 8.45 0.02 1 378 322 92 TRP C C 172 0.2 1 379 322 92 TRP CA C 56.9 0.2 1 380 322 92 TRP CB C 30.3 0.2 1 381 322 92 TRP N N 119.8 0.2 1 382 323 93 LYS H H 7.95 0.02 1 383 323 93 LYS C C 173.4 0.2 1 384 323 93 LYS CA C 55.2 0.2 1 385 323 93 LYS CB C 39.2 0.2 1 386 324 94 LEU H H 7.79 0.02 1 387 324 94 LEU C C 173.2 0.2 1 388 324 94 LEU CB C 45.3 0.2 1 389 324 94 LEU N N 118.1 0.2 1 390 325 95 HIS H H 8.97 0.02 1 391 325 95 HIS C C 173.8 0.2 1 392 325 95 HIS CA C 55.9 0.2 1 393 325 95 HIS CB C 33.6 0.2 1 394 325 95 HIS N N 122.1 0.2 1 395 326 96 ILE H H 10 0.02 1 396 326 96 ILE C C 174.8 0.2 1 397 326 96 ILE CA C 61 0.2 1 398 326 96 ILE CB C 39.1 0.2 1 399 326 96 ILE N N 129.1 0.2 1 400 327 97 THR H H 8.34 0.02 1 401 327 97 THR C C 175.1 0.2 1 402 327 97 THR CA C 58.6 0.2 1 403 327 97 THR CB C 70.9 0.2 1 404 327 97 THR N N 115.8 0.2 1 405 328 98 GLN H H 8.69 0.02 1 406 328 98 GLN CA C 57 0.2 1 407 328 98 GLN CB C 28.3 0.2 1 408 328 98 GLN N N 121.1 0.2 1 409 330 100 ASP H H 8.13 0.02 1 410 330 100 ASP C C 173.6 0.2 1 411 330 100 ASP CA C 54.2 0.2 1 412 330 100 ASP CB C 40.9 0.2 1 413 330 100 ASP N N 118.3 0.2 1 414 331 101 ASN H H 7.89 0.02 1 415 331 101 ASN CA C 51.8 0.2 1 416 331 101 ASN CB C 41.7 0.2 1 417 331 101 ASN N N 122 0.2 1 418 333 103 ARG C C 172.1 0.2 1 419 333 103 ARG CA C 55.1 0.2 1 420 334 104 VAL H H 8.03 0.02 1 421 334 104 VAL C C 173.3 0.2 1 422 334 104 VAL CA C 60.8 0.2 1 423 334 104 VAL CB C 38.6 0.2 1 424 334 104 VAL N N 123.1 0.2 1 425 335 105 TYR H H 8.28 0.02 1 426 335 105 TYR CA C 56.2 0.2 1 427 335 105 TYR CB C 33.3 0.2 1 428 335 105 TYR N N 126.3 0.2 1 429 336 106 ASN C C 174 0.2 1 430 336 106 ASN CA C 53.3 0.2 1 431 336 106 ASN CB C 39 0.2 1 432 337 107 THR H H 7.87 0.02 1 433 337 107 THR C C 174.8 0.2 1 434 337 107 THR CA C 61.7 0.2 1 435 337 107 THR CB C 69.9 0.2 1 436 337 107 THR N N 114.1 0.2 1 437 338 108 MET H H 8.17 0.02 1 438 338 108 MET CA C 53.2 0.2 1 439 338 108 MET CB C 32.3 0.2 1 440 338 108 MET N N 124.3 0.2 1 stop_ save_