data_4478 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; PKD domain 1 from Human polycystein-1 ; _BMRB_accession_number 4478 _BMRB_flat_file_name bmr4478.str _Entry_type original _Submission_date 1998-12-30 _Accession_date 1999-12-06 _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 Bycroft M. . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 406 "13C chemical shifts" 176 "15N chemical shifts" 80 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2000-05-25 original author . stop_ _Original_release_date 2000-05-25 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; The Structure of a PKD Domain from Polycystin-1: Implications for Polycystic Kidney Diseas ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code 99107746 _PubMed_ID ? loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Bycroft M. . . 2 Bateman A. . . 3 Clarke J. . . 4 Hamill S. J. . 5 Sandford R. . . 6 Thomas R. L. . 7 Chothia C. . . stop_ _Journal_abbreviation 'EMBO J.' _Journal_volume 18 _Journal_issue . _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 297 _Page_last 305 _Year 1999 _Details . save_ ################################## # Molecular system description # ################################## save_system_PKD1 _Saveframe_category molecular_system _Mol_system_name 'PKD1 HUMAN' _Abbreviation_common 'PKD1 HUMAN' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'PKD1 HUMAN' $PKD1 stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state monomer _System_paramagnetic no _System_thiol_state 'not present' _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_PKD1 _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'PKD1 HUMAN' _Name_variant none _Abbreviation_common 'PKD1 HUMAN' _Molecular_mass . _Mol_thiol_state 'not present' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 91 _Mol_residue_sequence ; GSVFPASPGATLVGPHGPLA SGQLAAFHIAAPLPVTATRW DFGDGSAEVDAAGPAASHRY VLPGRYHVTAVLALGAGSAL LGTDVQVEAAP ; loop_ _Residue_seq_code _Residue_label 1 GLY 2 SER 3 VAL 4 PHE 5 PRO 6 ALA 7 SER 8 PRO 9 GLY 10 ALA 11 THR 12 LEU 13 VAL 14 GLY 15 PRO 16 HIS 17 GLY 18 PRO 19 LEU 20 ALA 21 SER 22 GLY 23 GLN 24 LEU 25 ALA 26 ALA 27 PHE 28 HIS 29 ILE 30 ALA 31 ALA 32 PRO 33 LEU 34 PRO 35 VAL 36 THR 37 ALA 38 THR 39 ARG 40 TRP 41 ASP 42 PHE 43 GLY 44 ASP 45 GLY 46 SER 47 ALA 48 GLU 49 VAL 50 ASP 51 ALA 52 ALA 53 GLY 54 PRO 55 ALA 56 ALA 57 SER 58 HIS 59 ARG 60 TYR 61 VAL 62 LEU 63 PRO 64 GLY 65 ARG 66 TYR 67 HIS 68 VAL 69 THR 70 ALA 71 VAL 72 LEU 73 ALA 74 LEU 75 GLY 76 ALA 77 GLY 78 SER 79 ALA 80 LEU 81 LEU 82 GLY 83 THR 84 ASP 85 VAL 86 GLN 87 VAL 88 GLU 89 ALA 90 ALA 91 PRO stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-03-25 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 1B4R "Pkd Domain 1 From Human Polycystein-1" 86.81 80 100.00 100.00 9.20e-46 GB AAB59488 "polycystic kidney disease-associated protein [Homo sapiens]" 91.21 3638 100.00 100.00 1.24e-43 REF XP_003804194 "PREDICTED: polycystin-1-like, partial [Pan paniscus]" 97.80 587 97.75 98.88 1.11e-47 REF XP_009439072 "PREDICTED: polycystin-1 [Pan troglodytes]" 97.80 546 97.75 97.75 1.49e-47 REF XP_011521097 "PREDICTED: polycystin-1-like [Homo sapiens]" 97.80 471 97.75 97.75 6.99e-48 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $PKD1 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 _Variant _Vector_name $PKD1 'recombinant technology' 'Escherichia coli' Escherichia coli BL21 DE3 . 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 _Concentration_min_value _Concentration_max_value _Isotopic_labeling $PKD1 . mM 1 3 '[U-13C; U-15N]' 'acetate buffer' . mM . . [U-2H] stop_ save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model AMX _Field_strength 500 _Details . save_ ####################### # Sample conditions # ####################### save_sample_cond_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 3.0 . n/a temperature 298 . K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chem_shift_ref _Saveframe_category chemical_shift_reference _Details . 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_set_1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $sample_cond_1 _Chem_shift_reference_set_label $chem_shift_ref _Mol_system_component_name 'PKD1 HUMAN' _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 . 3 VAL H H 8.05 . 1 2 . 3 VAL HA H 3.98 . 1 3 . 3 VAL HB H 1.84 . 1 4 . 3 VAL HG1 H 0.70 . 1 5 . 3 VAL HG2 H 0.70 . 1 6 . 3 VAL CA C 59.3 . 1 7 . 3 VAL CB C 30.0 . 1 8 . 3 VAL N N 121.5 . 1 9 . 4 PHE H H 8.26 . 1 10 . 4 PHE HA H 4.81 . 1 11 . 4 PHE HB2 H 3.04 . 2 12 . 4 PHE HB3 H 2.77 . 2 13 . 4 PHE N N 125.0 . 1 14 . 5 PRO HA H 4.31 . 1 15 . 5 PRO HB2 H 2.15 . 1 16 . 5 PRO HB3 H 2.15 . 1 17 . 5 PRO CA C 60.3 . 1 18 . 5 PRO CB C 29.3 . 1 19 . 6 ALA H H 8.21 . 1 20 . 6 ALA HA H 4.23 . 1 21 . 6 ALA HB H 1.28 . 1 22 . 6 ALA CA C 49.6 . 1 23 . 6 ALA CB C 16.6 . 1 24 . 6 ALA N N 124.1 . 1 25 . 7 SER H H 8.18 . 1 26 . 7 SER HA H 4.65 . 1 27 . 7 SER HB2 H 3.72 . 1 28 . 7 SER HB3 H 3.72 . 1 29 . 7 SER N N 115.9 . 1 30 . 8 PRO HA H 4.33 . 1 31 . 8 PRO HB2 H 2.15 . 2 32 . 8 PRO HB3 H 1.80 . 2 33 . 9 GLY H H 8.20 . 1 34 . 9 GLY HA2 H 3.78 . 1 35 . 9 GLY HA3 H 3.78 . 1 36 . 9 GLY CA C 42.4 . 1 37 . 9 GLY N N 108.1 . 1 38 . 10 ALA H H 7.82 . 1 39 . 10 ALA HA H 4.97 . 1 40 . 10 ALA HB H 1.13 . 1 41 . 10 ALA CA C 48.7 . 1 42 . 10 ALA CB C 18.3 . 1 43 . 10 ALA N N 121.9 . 1 44 . 11 THR H H 8.72 . 1 45 . 11 THR HA H 4.45 . 1 46 . 11 THR HB H 3.87 . 1 47 . 11 THR HG2 H 1.08 . 1 48 . 11 THR CA C 58.3 . 1 49 . 11 THR CB C 69.6 . 1 50 . 11 THR CG2 C 19.2 . 1 51 . 11 THR N N 113.9 . 1 52 . 12 LEU H H 8.73 . 1 53 . 12 LEU HA H 4.53 . 1 54 . 12 LEU HB2 H 1.14 . 1 55 . 12 LEU HB3 H 1.60 . 1 56 . 12 LEU HG H 1.35 . 1 57 . 12 LEU HD1 H 0.50 . 1 58 . 12 LEU HD2 H 0.64 . 1 59 . 12 LEU CG C 24.2 . 1 60 . 12 LEU CD1 C 24.4 . 1 61 . 12 LEU CD2 C 22.9 . 1 62 . 12 LEU N N 127.2 . 1 63 . 13 VAL H H 9.02 . 1 64 . 13 VAL HA H 4.06 . 1 65 . 13 VAL HB H 1.22 . 1 66 . 13 VAL HG1 H 0.88 . 2 67 . 13 VAL HG2 H 0.71 . 2 68 . 13 VAL CA C 59.8 . 1 69 . 13 VAL CB C 29.0 . 1 70 . 13 VAL N N 129.1 . 1 71 . 14 GLY H H 8.23 . 1 72 . 14 GLY HA2 H 4.60 . 2 73 . 14 GLY HA3 H 3.61 . 2 74 . 14 GLY CA C 41.9 . 1 75 . 14 GLY N N 115.1 . 1 76 . 15 PRO HA H 4.26 . 1 77 . 15 PRO HB2 H 2.30 . 2 78 . 15 PRO HB3 H 1.80 . 2 79 . 15 PRO HG2 H 1.73 . 1 80 . 15 PRO HG3 H 1.73 . 1 81 . 15 PRO HD2 H 3.13 . 2 82 . 15 PRO HD3 H 2.62 . 2 83 . 15 PRO CA C 60.2 . 1 84 . 15 PRO CB C 29.4 . 1 85 . 16 HIS H H 8.83 . 1 86 . 16 HIS HA H 4.76 . 1 87 . 16 HIS HB2 H 3.19 . 1 88 . 16 HIS HB3 H 3.19 . 1 89 . 16 HIS HD2 H 7.23 . 1 90 . 16 HIS HE1 H 8.52 . 1 91 . 16 HIS CA C 52.6 . 1 92 . 16 HIS CB C 26.2 . 1 93 . 16 HIS N N 121.4 . 1 94 . 17 GLY H H 7.95 . 1 95 . 17 GLY HA2 H 4.00 . 1 96 . 17 GLY HA3 H 4.00 . 1 97 . 17 GLY N N 110.9 . 1 98 . 18 PRO HA H 4.50 . 1 99 . 18 PRO HB2 H 1.94 . 2 100 . 18 PRO HB3 H 1.61 . 2 101 . 18 PRO CA C 60.3 . 1 102 . 18 PRO CB C 29.6 . 1 103 . 19 LEU H H 8.70 . 1 104 . 19 LEU HA H 4.53 . 1 105 . 19 LEU HB2 H 1.59 . 1 106 . 19 LEU HB3 H 1.59 . 1 107 . 19 LEU HG H 1.63 . 1 108 . 19 LEU HD1 H 0.81 . 1 109 . 19 LEU HD2 H 0.76 . 1 110 . 19 LEU CA C 50.7 . 1 111 . 19 LEU CB C 42.2 . 1 112 . 19 LEU CG C 24.6 . 1 113 . 19 LEU CD1 C 23.3 . 1 114 . 19 LEU CD2 C 24.6 . 1 115 . 19 LEU N N 124.0 . 1 116 . 20 ALA H H 8.30 . 1 117 . 20 ALA HA H 4.80 . 1 118 . 20 ALA HB H 1.24 . 1 119 . 20 ALA CA C 47.8 . 1 120 . 20 ALA CB C 17.8 . 1 121 . 20 ALA N N 124.2 . 1 122 . 21 SER H H 8.19 . 1 123 . 21 SER HA H 3.72 . 1 124 . 21 SER HB2 H 3.53 . 1 125 . 21 SER HB3 H 3.53 . 1 126 . 21 SER CA C 57.3 . 1 127 . 21 SER CB C 60.4 . 1 128 . 21 SER N N 116.9 . 1 129 . 22 GLY H H 9.09 . 1 130 . 22 GLY HA2 H 4.22 . 2 131 . 22 GLY HA3 H 3.34 . 2 132 . 22 GLY CA C 42.7 . 1 133 . 22 GLY N N 113.4 . 1 134 . 23 GLN H H 7.75 . 1 135 . 23 GLN HA H 4.20 . 1 136 . 23 GLN HB2 H 2.10 . 1 137 . 23 GLN HB3 H 2.10 . 1 138 . 23 GLN HG2 H 2.34 . 1 139 . 23 GLN HG3 H 2.34 . 1 140 . 23 GLN CA C 52.5 . 1 141 . 23 GLN CB C 27.0 . 1 142 . 23 GLN N N 121.1 . 1 143 . 24 LEU H H 8.49 . 1 144 . 24 LEU HA H 3.78 . 1 145 . 24 LEU HB2 H 1.50 . 2 146 . 24 LEU HB3 H 1.14 . 2 147 . 24 LEU HG H 1.07 . 1 148 . 24 LEU HD1 H 0.52 . 1 149 . 24 LEU HD2 H 0.58 . 1 150 . 24 LEU CA C 53.1 . 1 151 . 24 LEU CB C 40.6 . 1 152 . 24 LEU CG C 24.2 . 1 153 . 24 LEU CD1 C 21.5 . 1 154 . 24 LEU CD2 C 22.4 . 1 155 . 24 LEU N N 124.5 . 1 156 . 25 ALA H H 8.67 . 1 157 . 25 ALA HA H 4.30 . 1 158 . 25 ALA HB H 1.35 . 1 159 . 25 ALA CA C 48.0 . 1 160 . 25 ALA CB C 18.6 . 1 161 . 25 ALA N N 132.1 . 1 162 . 26 ALA H H 7.87 . 1 163 . 26 ALA HA H 4.54 . 1 164 . 26 ALA HB H 1.10 . 1 165 . 26 ALA CA C 48.4 . 1 166 . 26 ALA CB C 17.9 . 1 167 . 26 ALA N N 125.3 . 1 168 . 27 PHE H H 8.37 . 1 169 . 27 PHE HA H 5.27 . 1 170 . 27 PHE HB2 H 2.34 . 1 171 . 27 PHE HB3 H 2.93 . 1 172 . 27 PHE HD1 H 6.98 . 1 173 . 27 PHE HD2 H 6.98 . 1 174 . 27 PHE HE1 H 7.35 . 1 175 . 27 PHE HE2 H 7.35 . 1 176 . 27 PHE HZ H 6.23 . 1 177 . 27 PHE CA C 53.3 . 1 178 . 27 PHE CB C 42.0 . 1 179 . 27 PHE N N 118.7 . 1 180 . 28 HIS H H 9.01 . 1 181 . 28 HIS HA H 5.72 . 1 182 . 28 HIS HB2 H 3.28 . 2 183 . 28 HIS HB3 H 3.03 . 2 184 . 28 HIS HD2 H 6.86 . 1 185 . 28 HIS HE1 H 8.59 . 1 186 . 28 HIS CA C 53.2 . 1 187 . 28 HIS CB C 28.9 . 1 188 . 28 HIS N N 113.9 . 1 189 . 29 ILE H H 8.92 . 1 190 . 29 ILE HA H 4.72 . 1 191 . 29 ILE HB H 1.81 . 1 192 . 29 ILE HG12 H 1.34 . 2 193 . 29 ILE HG13 H 1.22 . 2 194 . 29 ILE HG2 H 0.65 . 1 195 . 29 ILE HD1 H 0.43 . 1 196 . 29 ILE CA C 56.5 . 1 197 . 29 ILE CB C 35.9 . 1 198 . 29 ILE CG1 C 25.1 . 1 199 . 29 ILE CG2 C 15.6 . 1 200 . 29 ILE CD1 C 10.5 . 1 201 . 29 ILE N N 122.2 . 1 202 . 30 ALA H H 9.00 . 1 203 . 30 ALA HA H 4.72 . 1 204 . 30 ALA HB H 1.25 . 1 205 . 30 ALA CA C 48.1 . 1 206 . 30 ALA CB C 17.0 . 1 207 . 30 ALA N N 132.7 . 1 208 . 31 ALA H H 8.33 . 1 209 . 31 ALA HA H 4.74 . 1 210 . 31 ALA HB H 1.28 . 1 211 . 31 ALA CA C 48.4 . 1 212 . 31 ALA CB C 18.8 . 1 213 . 31 ALA N N 124.8 . 1 214 . 32 PRO HA H 4.44 . 1 215 . 32 PRO HB2 H 2.10 . 1 216 . 32 PRO HB3 H 1.97 . 1 217 . 32 PRO HD2 H 3.50 . 1 218 . 32 PRO CA C 60.9 . 1 219 . 32 PRO CB C 28.8 . 1 220 . 33 LEU H H 6.89 . 1 221 . 33 LEU HA H 4.72 . 1 222 . 33 LEU HB2 H 1.40 . 1 223 . 33 LEU HB3 H 1.40 . 1 224 . 33 LEU HG H 1.42 . 1 225 . 33 LEU HD1 H 0.75 . 2 226 . 33 LEU HD2 H 0.81 . 2 227 . 33 LEU N N 119.1 . 1 228 . 34 PRO HA H 4.20 . 1 229 . 34 PRO HB2 H 2.15 . 1 230 . 34 PRO HB3 H 2.15 . 1 231 . 35 VAL H H 8.32 . 1 232 . 35 VAL HA H 4.12 . 1 233 . 35 VAL HB H 1.81 . 1 234 . 35 VAL HG1 H 0.64 . 1 235 . 35 VAL HG2 H 0.78 . 1 236 . 35 VAL CA C 60.8 . 1 237 . 35 VAL CB C 29.3 . 1 238 . 35 VAL CG1 C 20.2 . 1 239 . 35 VAL CG2 C 18.4 . 1 240 . 35 VAL N N 124.8 . 1 241 . 36 THR H H 8.46 . 1 242 . 36 THR HA H 4.20 . 1 243 . 36 THR HB H 4.20 . 1 244 . 36 THR HG2 H 1.04 . 1 245 . 36 THR CA C 59.5 . 1 246 . 36 THR CB C 66.5 . 1 247 . 36 THR CG2 C 38.9 . 1 248 . 36 THR N N 118.0 . 1 249 . 37 ALA H H 7.32 . 1 250 . 37 ALA HA H 4.91 . 1 251 . 37 ALA HB H 1.32 . 1 252 . 37 ALA CA C 50.2 . 1 253 . 37 ALA CB C 18.4 . 1 254 . 37 ALA N N 122.9 . 1 255 . 38 THR H H 8.79 . 1 256 . 38 THR HA H 4.81 . 1 257 . 38 THR HB H 3.34 . 1 258 . 38 THR HG2 H 0.72 . 1 259 . 38 THR CA C 57.2 . 1 260 . 38 THR CB C 69.8 . 1 261 . 38 THR CG2 C 21.7 . 1 262 . 38 THR N N 112.7 . 1 263 . 39 ARG H H 7.99 . 1 264 . 39 ARG HA H 5.26 . 1 265 . 39 ARG HB2 H 1.41 . 1 266 . 39 ARG HB3 H 1.41 . 1 267 . 39 ARG HG2 H 1.40 . 1 268 . 39 ARG HG3 H 1.40 . 1 269 . 39 ARG HD2 H 2.93 . 1 270 . 39 ARG HD3 H 2.93 . 1 271 . 39 ARG HE H 7.19 . 1 272 . 39 ARG CA C 52.4 . 1 273 . 39 ARG CB C 30.0 . 1 274 . 39 ARG N N 122.2 . 1 275 . 40 TRP H H 9.33 . 1 276 . 40 TRP HA H 4.44 . 1 277 . 40 TRP HB2 H 2.43 . 2 278 . 40 TRP HB3 H 1.69 . 2 279 . 40 TRP HD1 H 6.79 . 1 280 . 40 TRP HE1 H 10.23 . 1 281 . 40 TRP HE3 H 6.31 . 1 282 . 40 TRP HZ2 H 6.98 . 1 283 . 40 TRP HZ3 H 6.18 . 1 284 . 40 TRP HH2 H 6.41 . 1 285 . 40 TRP CA C 54.0 . 1 286 . 40 TRP CB C 29.2 . 1 287 . 40 TRP N N 127.1 . 1 288 . 40 TRP NE1 N 128.8 . 1 289 . 41 ASP H H 8.36 . 1 290 . 41 ASP HA H 4.73 . 1 291 . 41 ASP HB2 H 2.88 . 1 292 . 41 ASP HB3 H 2.28 . 1 293 . 41 ASP CA C 48.8 . 1 294 . 41 ASP CB C 38.2 . 1 295 . 41 ASP N N 119.9 . 1 296 . 42 PHE H H 8.95 . 1 297 . 42 PHE HA H 4.11 . 1 298 . 42 PHE HB2 H 1.47 . 1 299 . 42 PHE HB3 H 2.53 . 1 300 . 42 PHE HD1 H 6.63 . 1 301 . 42 PHE HD2 H 6.63 . 1 302 . 42 PHE HE1 H 6.94 . 1 303 . 42 PHE HE2 H 6.94 . 1 304 . 42 PHE HZ H 6.14 . 1 305 . 42 PHE CA C 58.0 . 1 306 . 42 PHE CB C 34.7 . 1 307 . 42 PHE N N 121.2 . 1 308 . 43 GLY H H 8.46 . 1 309 . 43 GLY HA2 H 4.51 . 2 310 . 43 GLY HA3 H 3.90 . 2 311 . 43 GLY CA C 44.5 . 1 312 . 43 GLY N N 105.4 . 1 313 . 44 ASP H H 8.32 . 1 314 . 44 ASP HA H 4.93 . 1 315 . 44 ASP HB2 H 3.10 . 2 316 . 44 ASP HB3 H 1.99 . 2 317 . 44 ASP CA C 49.4 . 1 318 . 44 ASP CB C 38.7 . 1 319 . 44 ASP N N 117.3 . 1 320 . 45 GLY H H 8.77 . 1 321 . 45 GLY HA2 H 4.28 . 2 322 . 45 GLY HA3 H 3.65 . 2 323 . 45 GLY CA C 42.6 . 1 324 . 45 GLY N N 111.0 . 1 325 . 46 SER H H 7.52 . 1 326 . 46 SER HA H 4.30 . 1 327 . 46 SER HB2 H 4.02 . 1 328 . 46 SER HB3 H 4.02 . 1 329 . 46 SER CA C 61.5 . 1 330 . 46 SER CB C 55.5 . 1 331 . 46 SER N N 115.4 . 1 332 . 47 ALA H H 8.42 . 1 333 . 47 ALA HA H 4.13 . 1 334 . 47 ALA HB H 1.35 . 1 335 . 47 ALA CA C 49.9 . 1 336 . 47 ALA CB C 16.3 . 1 337 . 47 ALA N N 123.7 . 1 338 . 48 GLU H H 8.43 . 1 339 . 48 GLU HA H 4.46 . 1 340 . 48 GLU HB2 H 1.90 . 2 341 . 48 GLU HB3 H 1.72 . 2 342 . 48 GLU HG2 H 2.38 . 2 343 . 48 GLU HG3 H 2.15 . 2 344 . 48 GLU CA C 54.2 . 1 345 . 48 GLU CB C 26.5 . 1 346 . 48 GLU N N 121.3 . 1 347 . 49 VAL H H 8.48 . 1 348 . 49 VAL HA H 4.29 . 1 349 . 49 VAL HB H 1.92 . 1 350 . 49 VAL HG1 H 0.95 . 1 351 . 49 VAL HG2 H 1.15 . 1 352 . 49 VAL CA C 58.8 . 1 353 . 49 VAL CB C 33.0 . 1 354 . 49 VAL CG1 C 18.0 . 1 355 . 49 VAL CG2 C 18.8 . 1 356 . 49 VAL N N 123.5 . 1 357 . 50 ASP H H 8.83 . 1 358 . 50 ASP HA H 5.45 . 1 359 . 50 ASP HB2 H 2.78 . 1 360 . 50 ASP HB3 H 2.61 . 1 361 . 50 ASP CA C 49.7 . 1 362 . 50 ASP CB C 36.6 . 1 363 . 50 ASP N N 127.4 . 1 364 . 51 ALA H H 9.13 . 1 365 . 51 ALA HA H 4.72 . 1 366 . 51 ALA HB H 1.47 . 1 367 . 51 ALA CA C 48.5 . 1 368 . 51 ALA CB C 19.1 . 1 369 . 51 ALA N N 127.1 . 1 370 . 52 ALA H H 8.56 . 1 371 . 52 ALA HA H 4.78 . 1 372 . 52 ALA HB H 1.35 . 1 373 . 52 ALA CA C 48.7 . 1 374 . 52 ALA CB C 15.3 . 1 375 . 52 ALA N N 127.2 . 1 376 . 53 GLY H H 7.64 . 1 377 . 53 GLY HA2 H 4.00 . 1 378 . 53 GLY HA3 H 4.00 . 1 379 . 53 GLY N N 107.4 . 1 380 . 54 PRO HA H 4.49 . 1 381 . 54 PRO HB2 H 2.01 . 1 382 . 54 PRO HB3 H 2.01 . 1 383 . 54 PRO HG2 H 1.87 . 1 384 . 54 PRO HG3 H 1.87 . 1 385 . 54 PRO HD2 H 3.49 . 1 386 . 54 PRO HD3 H 3.49 . 1 387 . 54 PRO CA C 61.1 . 1 388 . 54 PRO CB C 30.6 . 1 389 . 54 PRO CD C 46.5 . 1 390 . 55 ALA H H 8.00 . 1 391 . 55 ALA HA H 5.33 . 1 392 . 55 ALA HB H 1.35 . 1 393 . 55 ALA CA C 48.8 . 1 394 . 55 ALA CB C 20.7 . 1 395 . 55 ALA N N 123.2 . 1 396 . 56 ALA H H 7.77 . 1 397 . 56 ALA HA H 4.13 . 1 398 . 56 ALA HB H 0.01 . 1 399 . 56 ALA CA C 49.2 . 1 400 . 56 ALA CB C 17.4 . 1 401 . 56 ALA N N 120.3 . 1 402 . 57 SER H H 9.09 . 1 403 . 57 SER HA H 5.52 . 1 404 . 57 SER HB2 H 3.51 . 2 405 . 57 SER HB3 H 3.35 . 2 406 . 57 SER CA C 53.8 . 1 407 . 57 SER CB C 63.7 . 1 408 . 57 SER N N 113.4 . 1 409 . 58 HIS H H 8.64 . 1 410 . 58 HIS HA H 4.03 . 1 411 . 58 HIS HB2 H 1.47 . 1 412 . 58 HIS HB3 H 0.70 . 1 413 . 58 HIS HE1 H 8.30 . 1 414 . 58 HIS CA C 52.0 . 1 415 . 58 HIS CB C 28.5 . 1 416 . 58 HIS N N 117.4 . 1 417 . 59 ARG H H 7.53 . 1 418 . 59 ARG HA H 4.46 . 1 419 . 59 ARG HB2 H 1.04 . 1 420 . 59 ARG HB3 H 1.04 . 1 421 . 59 ARG HG2 H 0.78 . 2 422 . 59 ARG HG3 H 1.00 . 2 423 . 59 ARG HD2 H 2.94 . 2 424 . 59 ARG HD3 H 2.77 . 2 425 . 59 ARG HE H 6.96 . 1 426 . 59 ARG CA C 52.1 . 1 427 . 59 ARG CB C 26.74 . 1 428 . 59 ARG N N 126.0 . 1 429 . 60 TYR H H 8.08 . 1 430 . 60 TYR HA H 4.23 . 1 431 . 60 TYR HB2 H 2.78 . 1 432 . 60 TYR HB3 H 2.54 . 1 433 . 60 TYR HD1 H 7.00 . 1 434 . 60 TYR HD2 H 7.00 . 1 435 . 60 TYR HE1 H 7.29 . 1 436 . 60 TYR HE2 H 7.29 . 1 437 . 60 TYR CA C 55.45 . 1 438 . 60 TYR CB C 37.5 . 1 439 . 60 TYR N N 122.9 . 1 440 . 61 VAL H H 8.60 . 1 441 . 61 VAL HA H 3.91 . 1 442 . 61 VAL HB H 1.97 . 1 443 . 61 VAL HG1 H 0.76 . 2 444 . 61 VAL HG2 H 0.73 . 2 445 . 61 VAL CA C 61.0 . 1 446 . 61 VAL CB C 29.8 . 1 447 . 61 VAL N N 118.8 . 1 448 . 62 LEU H H 7.77 . 1 449 . 62 LEU HA H 4.20 . 1 450 . 62 LEU HB2 H 2.34 . 2 451 . 62 LEU HB3 H 2.10 . 2 452 . 62 LEU HG H 1.58 . 1 453 . 62 LEU HD1 H 0.90 . 1 454 . 62 LEU HD2 H 0.90 . 1 455 . 62 LEU N N 120.3 . 1 456 . 63 PRO HA H 4.03 . 1 457 . 63 PRO HB2 H 2.05 . 1 458 . 63 PRO HB3 H 1.84 . 2 459 . 63 PRO HG2 H 1.84 . 2 460 . 63 PRO CA C 59.9 . 1 461 . 63 PRO CB C 29.8 . 1 462 . 64 GLY H H 8.54 . 1 463 . 64 GLY HA2 H 3.82 . 2 464 . 64 GLY HA3 H 3.56 . 2 465 . 64 GLY CA C 41.8 . 1 466 . 64 GLY N N 108.3 . 1 467 . 65 ARG H H 7.65 . 1 468 . 65 ARG HA H 4.85 . 1 469 . 65 ARG HB2 H 1.45 . 1 470 . 65 ARG HB3 H 1.45 . 1 471 . 65 ARG HG2 H 1.22 . 2 472 . 65 ARG HG3 H 1.36 . 2 473 . 65 ARG HD2 H 2.98 . 1 474 . 65 ARG HD3 H 2.98 . 1 475 . 65 ARG HE H 7.12 . 1 476 . 65 ARG CA C 51.5 . 1 477 . 65 ARG CB C 28.3 . 1 478 . 65 ARG N N 119.9 . 1 479 . 66 TYR H H 8.58 . 1 480 . 66 TYR HA H 4.77 . 1 481 . 66 TYR HB2 H 3.06 . 1 482 . 66 TYR HB3 H 2.22 . 1 483 . 66 TYR HD1 H 6.52 . 1 484 . 66 TYR HD2 H 6.52 . 1 485 . 66 TYR CA C 54.1 . 1 486 . 66 TYR CB C 38.9 . 1 487 . 66 TYR N N 123.2 . 1 488 . 67 HIS H H 9.34 . 1 489 . 67 HIS HA H 5.25 . 1 490 . 67 HIS HB2 H 3.23 . 2 491 . 67 HIS HB3 H 2.91 . 2 492 . 67 HIS HD2 H 6.96 . 1 493 . 67 HIS HE1 H 8.43 . 1 494 . 67 HIS CA C 51.9 . 1 495 . 67 HIS CB C 26.6 . 1 496 . 67 HIS N N 122.9 . 1 497 . 68 VAL H H 8.59 . 1 498 . 68 VAL HA H 4.28 . 1 499 . 68 VAL HB H 1.44 . 1 500 . 68 VAL HG1 H 0.21 . 1 501 . 68 VAL HG2 H 0.84 . 1 502 . 68 VAL CA C 58.1 . 1 503 . 68 VAL CB C 30.7 . 1 504 . 68 VAL CG1 C 17.2 . 1 505 . 68 VAL CG2 C 20.0 . 1 506 . 68 VAL N N 130.2 . 1 507 . 69 THR H H 8.63 . 1 508 . 69 THR HA H 4.88 . 1 509 . 69 THR HB H 3.74 . 2 510 . 69 THR HG2 H 0.90 . 1 511 . 69 THR CA C 56.7 . 1 512 . 69 THR CB C 69.5 . 1 513 . 69 THR CG2 C 19.6 . 1 514 . 69 THR N N 117.0 . 1 515 . 70 ALA H H 8.32 . 1 516 . 70 ALA HA H 4.35 . 1 517 . 70 ALA HB H -0.31 . 1 518 . 70 ALA CA C 46.9 . 1 519 . 70 ALA CB C 18.0 . 1 520 . 70 ALA N N 123.8 . 1 521 . 71 VAL H H 8.29 . 1 522 . 71 VAL HA H 4.56 . 1 523 . 71 VAL HB H 1.57 . 1 524 . 71 VAL HG1 H 0.66 . 1 525 . 71 VAL HG2 H 0.66 . 1 526 . 71 VAL CA C 58.1 . 1 527 . 71 VAL CB C 30.8 . 1 528 . 71 VAL N N 120.7 . 1 529 . 72 LEU H H 8.66 . 1 530 . 72 LEU HA H 4.55 . 1 531 . 72 LEU HB2 H 1.41 . 1 532 . 72 LEU HB3 H 1.41 . 1 533 . 72 LEU HG H 1.40 . 1 534 . 72 LEU HD1 H 0.61 . 1 535 . 72 LEU HD2 H 0.50 . 1 536 . 72 LEU CG C 25.0 . 1 537 . 72 LEU CD1 C 24.5 . 1 538 . 72 LEU CD2 C 24.0 . 1 539 . 72 LEU N N 126.7 . 1 540 . 73 ALA H H 8.17 . 1 541 . 73 ALA HA H 4.46 . 1 542 . 73 ALA HB H 1.22 . 1 543 . 73 ALA CA C 49.4 . 1 544 . 73 ALA CB C 16.43 . 1 545 . 73 ALA N N 125.6 . 1 546 . 74 LEU H H 7.79 . 1 547 . 74 LEU HA H 4.47 . 1 548 . 74 LEU HB2 H 1.36 . 2 549 . 74 LEU HB3 H 1.14 . 2 550 . 74 LEU CA C 50.9 . 1 551 . 74 LEU CB C 40.7 . 1 552 . 74 LEU N N 124.1 . 1 553 . 75 GLY H H 8.67 . 1 554 . 75 GLY HA2 H 3.53 . 2 555 . 75 GLY HA3 H 3.83 . 2 556 . 75 GLY CA C 44.1 . 1 557 . 75 GLY N N 113.7 . 1 558 . 76 ALA H H 8.44 . 1 559 . 76 ALA HA H 4.30 . 1 560 . 76 ALA HB H 1.28 . 1 561 . 76 ALA CA C 49.6 . 1 562 . 76 ALA CB C 16.0 . 1 563 . 76 ALA N N 127.2 . 1 564 . 77 GLY H H 7.71 . 1 565 . 77 GLY HA2 H 4.16 . 2 566 . 77 GLY HA3 H 3.78 . 2 567 . 77 GLY CA C 41.9 . 1 568 . 77 GLY N N 107.2 . 1 569 . 78 SER H H 8.18 . 1 570 . 78 SER HA H 5.03 . 1 571 . 78 SER HB2 H 3.52 . 1 572 . 78 SER HB3 H 3.52 . 1 573 . 78 SER CA C 54.9 . 1 574 . 78 SER CB C 62.9 . 1 575 . 78 SER N N 115.4 . 1 576 . 79 ALA H H 8.58 . 1 577 . 79 ALA HA H 4.53 . 1 578 . 79 ALA HB H 1.15 . 1 579 . 79 ALA CA C 50.1 . 1 580 . 79 ALA CB C 16.3 . 1 581 . 79 ALA N N 124.4 . 1 582 . 80 LEU H H 8.04 . 1 583 . 80 LEU HA H 4.88 . 1 584 . 80 LEU HB2 H 1.46 . 2 585 . 80 LEU HB3 H 1.28 . 2 586 . 80 LEU CA C 51.8 . 1 587 . 80 LEU CB C 41.3 . 1 588 . 80 LEU N N 122.6 . 1 589 . 81 LEU H H 8.89 . 1 590 . 81 LEU HA H 4.67 . 1 591 . 81 LEU HB2 H 1.42 . 2 592 . 81 LEU HB3 H 1.24 . 2 593 . 81 LEU HG H 1.32 . 1 594 . 81 LEU HD1 H 0.64 . 1 595 . 81 LEU HD2 H 0.61 . 1 596 . 81 LEU CA C 50.5 . 1 597 . 81 LEU CB C 43.5 . 1 598 . 81 LEU CG C 24.0 . 1 599 . 81 LEU CD1 C 23.2 . 1 600 . 81 LEU CD2 C 22.8 . 1 601 . 81 LEU N N 126.8 . 1 602 . 82 GLY H H 8.15 . 1 603 . 82 GLY HA2 H 5.16 . 2 604 . 82 GLY HA3 H 3.52 . 2 605 . 82 GLY CA C 42.5 . 1 606 . 82 GLY N N 106.1 . 1 607 . 83 THR H H 8.37 . 1 608 . 83 THR HA H 4.53 . 1 609 . 83 THR HB H 4.15 . 1 610 . 83 THR HG2 H 0.96 . 1 611 . 83 THR CA C 57.3 . 1 612 . 83 THR CB C 70.0 . 1 613 . 83 THR CG2 C 16.4 . 1 614 . 83 THR N N 113.5 . 1 615 . 84 ASP H H 7.98 . 1 616 . 84 ASP HA H 5.98 . 1 617 . 84 ASP HB2 H 2.47 . 1 618 . 84 ASP HB3 H 2.47 . 1 619 . 84 ASP CA C 50.5 . 1 620 . 84 ASP CB C 40.8 . 1 621 . 84 ASP N N 121.8 . 1 622 . 85 VAL H H 9.19 . 1 623 . 85 VAL HA H 4.59 . 1 624 . 85 VAL HB H 1.97 . 1 625 . 85 VAL HG1 H 0.93 . 1 626 . 85 VAL HG2 H 0.86 . 1 627 . 85 VAL CA C 57.0 . 1 628 . 85 VAL CB C 32.9 . 1 629 . 85 VAL CG1 C 19.4 . 1 630 . 85 VAL CG2 C 18.0 . 1 631 . 85 VAL N N 117.5 . 1 632 . 86 GLN H H 8.64 . 1 633 . 86 GLN HA H 4.75 . 1 634 . 86 GLN HB2 H 1.84 . 1 635 . 86 GLN HB3 H 1.84 . 1 636 . 86 GLN HG2 H 2.05 . 1 637 . 86 GLN HG3 H 2.05 . 1 638 . 86 GLN CA C 51.9 . 1 639 . 86 GLN CB C 28.1 . 1 640 . 86 GLN N N 125.0 . 1 641 . 87 VAL H H 9.10 . 1 642 . 87 VAL HA H 4.60 . 1 643 . 87 VAL HB H 2.12 . 1 644 . 87 VAL HG1 H 0.63 . 1 645 . 87 VAL HG2 H 0.55 . 1 646 . 87 VAL CA C 58.0 . 1 647 . 87 VAL CB C 30.6 . 1 648 . 87 VAL CG1 C 19.0 . 1 649 . 87 VAL N N 126.6 . 1 650 . 88 GLU H H 9.26 . 1 651 . 88 GLU HA H 4.60 . 1 652 . 88 GLU HB2 H 2.04 . 2 653 . 88 GLU HB3 H 1.85 . 2 654 . 88 GLU HG2 H 2.27 . 1 655 . 88 GLU HG3 H 2.27 . 1 656 . 88 GLU CA C 51.5 . 1 657 . 88 GLU CB C 28.3 . 1 658 . 88 GLU N N 127.3 . 1 659 . 89 ALA H H 8.61 . 1 660 . 89 ALA HA H 4.16 . 1 661 . 89 ALA HB H 1.28 . 1 662 . 89 ALA N N 123.4 . 1 stop_ save_