data_5359 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; 1H, 15N, 13C Backbone Chemical Shift Assignments for Free Bovine Pancreatic Trypsin Inhibitor (BPTI) at pH 5.8 and 36 Degrees ; _BMRB_accession_number 5359 _BMRB_flat_file_name bmr5359.str _Entry_type original _Submission_date 2001-04-30 _Accession_date 2001-04-30 _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 Biamonti Clelia . . 2 Baran Michael C . 3 Montelione Gaetano T . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 197 "13C chemical shifts" 196 "15N chemical shifts" 53 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2002-05-08 original BMRB . stop_ loop_ _Related_BMRB_accession_number _Relationship 5358 'Complex form of BPTI with trypsin.' stop_ _Original_release_date 2002-04-30 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; Structural and Dynamic Investigations of Macromolecular Recognition Processes by Nuclear Magnetic Resonance Spectroscopy ; _Citation_status published _Citation_type thesis _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID ? loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Biamonti Clelia . . stop_ _Journal_abbreviation . _Journal_volume . _Journal_issue . _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Thesis_institution 'Rutgers University' _Thesis_institution_city 'Piscataway, NJ' _Thesis_institution_country 'U. S. A.' _Page_first . _Page_last . _Year 1996 _Details . save_ ################################## # Molecular system description # ################################## save_system_BPTI _Saveframe_category molecular_system _Mol_system_name 'Bovine Pancreatic Trypsin Inhibitor' _Abbreviation_common BPTI _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label BPTI $BPTI stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state monomer _System_paramagnetic no _System_thiol_state 'all disulfide bound' _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_BPTI _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'bovine pancreatic trypsin inhibitor' _Abbreviation_common BPTI _Molecular_mass . _Mol_thiol_state 'all disulfide bound' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 58 _Mol_residue_sequence ; RPDFCLEPPYTGPCKARIIR YFYNAKAGLCQTFVYGGCRA KRNNFKSAEDCMRTCGGA ; loop_ _Residue_seq_code _Residue_label 1 ARG 2 PRO 3 ASP 4 PHE 5 CYS 6 LEU 7 GLU 8 PRO 9 PRO 10 TYR 11 THR 12 GLY 13 PRO 14 CYS 15 LYS 16 ALA 17 ARG 18 ILE 19 ILE 20 ARG 21 TYR 22 PHE 23 TYR 24 ASN 25 ALA 26 LYS 27 ALA 28 GLY 29 LEU 30 CYS 31 GLN 32 THR 33 PHE 34 VAL 35 TYR 36 GLY 37 GLY 38 CYS 39 ARG 40 ALA 41 LYS 42 ARG 43 ASN 44 ASN 45 PHE 46 LYS 47 SER 48 ALA 49 GLU 50 ASP 51 CYS 52 MET 53 ARG 54 THR 55 CYS 56 GLY 57 GLY 58 ALA stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date . save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $BPTI Cow 9913 Eukaryota Metazoa Bos taurus 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 $BPTI 'recombinant technology' E.coli Escherichia coli . . stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_Sample_1 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $BPTI 0.75 mM . CaCl2 25 mM . NaAzide 3 mM . H2O 90 % . D2O 10 % . stop_ save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer _Saveframe_category NMR_spectrometer _Manufacturer VARIAN _Model Unity _Field_strength 500 _Details . save_ ############################# # NMR applied experiments # ############################# save_HSQC_1 _Saveframe_category NMR_applied_experiment _Experiment_name HSQC _Sample_label . save_ save_HNCA_2 _Saveframe_category NMR_applied_experiment _Experiment_name HNCA _Sample_label . save_ save_HNCO_3 _Saveframe_category NMR_applied_experiment _Experiment_name HNCO _Sample_label . save_ ####################### # Sample conditions # ####################### save_BPTI_cond_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 5.8 . n/a temperature 309 . K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference _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 . ppm . . indirect . . . 0.251449537 DSS H 1 . ppm 0.00 external direct cylindrical external . 1.0 DSS N 15 . ppm . . 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_BPTI_shifts_1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Experiment_label HSQC HNCA HNCO stop_ loop_ _Sample_label $Sample_1 stop_ _Sample_conditions_label $BPTI_cond_1 _Chem_shift_reference_set_label $chemical_shift_reference _Mol_system_component_name BPTI _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 . 1 ARG HB2 H 1.89 . 2 2 . 1 ARG HB3 H 1.80 . 2 3 . 2 PRO HA H 4.33 . 1 4 . 2 PRO HB2 H 2.03 . 2 5 . 2 PRO HB3 H 0.92 . 2 6 . 2 PRO C C 177.7 . 1 7 . 2 PRO CA C 63.3 . 1 8 . 2 PRO CB C 33.4 . 1 9 . 2 PRO CG C 28.2 . 1 10 . 2 PRO CD C 51.7 . 1 11 . 3 ASP N N 123.9 . 1 12 . 3 ASP H H 8.70 . 1 13 . 3 ASP HA H 4.25 . 1 14 . 3 ASP HB2 H 2.77 . 2 15 . 3 ASP C C 180.2 . 1 16 . 3 ASP CA C 57.4 . 1 17 . 3 ASP CB C 39.0 . 1 18 . 4 PHE N N 116.9 . 1 19 . 4 PHE H H 7.88 . 1 20 . 4 PHE HA H 4.60 . 1 21 . 4 PHE HB2 H 3.35 . 2 22 . 4 PHE C C 177.7 . 1 23 . 4 PHE CA C 59.3 . 1 24 . 4 PHE CB C 38.0 . 1 25 . 5 CYS N N 121.5 . 1 26 . 5 CYS H H 7.48 . 1 27 . 5 CYS HA H 4.35 . 1 28 . 5 CYS HB2 H 2.86 . 2 29 . 5 CYS HB3 H 2.74 . 2 30 . 5 CYS C C 173.4 . 1 31 . 5 CYS CA C 58.0 . 1 32 . 5 CYS CB C 40.3 . 1 33 . 6 LEU N N 114.2 . 1 34 . 6 LEU H H 7.62 . 1 35 . 6 LEU HA H 4.51 . 1 36 . 6 LEU HB2 H 1.84 . 2 37 . 6 LEU C C 178.6 . 1 38 . 6 LEU CA C 54.8 . 1 39 . 6 LEU CB C 40.8 . 1 40 . 6 LEU CG C 28.9 . 1 41 . 6 LEU CD1 C 23.3 . 2 42 . 6 LEU CD2 C 25.4 . 2 43 . 7 GLU N N 120.8 . 1 44 . 7 GLU H H 7.56 . 1 45 . 7 GLU HA H 4.59 . 1 46 . 7 GLU HB2 H 2.26 . 2 47 . 7 GLU HB3 H 2.17 . 2 48 . 7 GLU CA C 55.1 . 1 49 . 7 GLU CB C 29.8 . 1 50 . 8 PRO HA H 4.63 . 1 51 . 8 PRO HB2 H 2.44 . 2 52 . 8 PRO HB3 H 1.84 . 2 53 . 9 PRO HA H 3.72 . 1 54 . 9 PRO C C 176.1 . 1 55 . 9 PRO CA C 62.7 . 1 56 . 9 PRO CB C 30.5 . 1 57 . 9 PRO CG C 26.4 . 1 58 . 9 PRO CD C 50.4 . 1 59 . 10 TYR N N 123.6 . 1 60 . 10 TYR H H 7.85 . 1 61 . 10 TYR HA H 4.95 . 1 62 . 10 TYR HB2 H 2.96 . 2 63 . 10 TYR C C 175.3 . 1 64 . 10 TYR CA C 56.5 . 1 65 . 11 THR N N 127.7 . 1 66 . 11 THR H H 8.99 . 1 67 . 11 THR HA H 4.53 . 1 68 . 11 THR HB H 4.05 . 1 69 . 11 THR C C 177.1 . 1 70 . 11 THR CA C 67.3 . 1 71 . 11 THR CB C 70.5 . 1 72 . 11 THR CG2 C 22.0 . 1 73 . 12 GLY N N 107.3 . 1 74 . 12 GLY H H 7.19 . 1 75 . 12 GLY HA2 H 3.90 . 2 76 . 12 GLY HA3 H 3.26 . 2 77 . 12 GLY CA C 46.3 . 1 78 . 13 PRO HA H 4.56 . 1 79 . 13 PRO HB2 H 2.17 . 2 80 . 13 PRO HB3 H 2.11 . 2 81 . 13 PRO C C 178.9 . 1 82 . 13 PRO CA C 64.3 . 1 83 . 13 PRO CB C 32.0 . 1 84 . 13 PRO CD C 49.6 . 1 85 . 14 CYS N N 120.3 . 1 86 . 14 CYS H H 8.73 . 1 87 . 14 CYS HA H 4.56 . 1 88 . 14 CYS HB2 H 3.47 . 2 89 . 14 CYS HB3 H 2.79 . 2 90 . 14 CYS C C 171.9 . 1 91 . 14 CYS CA C 60.7 . 1 92 . 14 CYS CB C 46.3 . 1 93 . 15 LYS N N 115.8 . 1 94 . 15 LYS H H 8.00 . 1 95 . 15 LYS HA H 4.41 . 1 96 . 15 LYS HB2 H 2.09 . 2 97 . 15 LYS HB3 H 1.58 . 2 98 . 15 LYS C C 177.7 . 1 99 . 15 LYS CA C 56.4 . 1 100 . 15 LYS CB C 31.7 . 1 101 . 15 LYS CD C 29.2 . 1 102 . 15 LYS CE C 42.9 . 1 103 . 16 ALA N N 124.0 . 1 104 . 16 ALA H H 8.25 . 1 105 . 16 ALA HA H 4.29 . 1 106 . 16 ALA HB H 1.18 . 1 107 . 16 ALA C C 175.2 . 1 108 . 16 ALA CA C 52.0 . 1 109 . 16 ALA CB C 19.9 . 1 110 . 17 ARG N N 118.8 . 1 111 . 17 ARG H H 8.23 . 1 112 . 17 ARG HA H 4.32 . 1 113 . 17 ARG HB2 H 1.60 . 2 114 . 17 ARG C C 174.9 . 1 115 . 17 ARG CA C 55.1 . 1 116 . 17 ARG CB C 29.4 . 1 117 . 17 ARG CD C 44.2 . 1 118 . 18 ILE N N 126.1 . 1 119 . 18 ILE H H 8.17 . 1 120 . 18 ILE HA H 4.20 . 1 121 . 18 ILE HB H 1.87 . 1 122 . 18 ILE C C 175.8 . 1 123 . 18 ILE CA C 60.4 . 1 124 . 18 ILE CB C 40.1 . 1 125 . 18 ILE CG1 C 27.4 . 2 126 . 18 ILE CG2 C 18.9 . 2 127 . 18 ILE CD1 C 14.3 . 1 128 . 19 ILE N N 128.7 . 1 129 . 19 ILE H H 8.73 . 1 130 . 19 ILE HA H 4.31 . 1 131 . 19 ILE HB H 1.95 . 1 132 . 19 ILE C C 176.7 . 1 133 . 19 ILE CA C 61.3 . 1 134 . 19 ILE CB C 35.9 . 1 135 . 19 ILE CG1 C 27.7 . 2 136 . 19 ILE CG2 C 17.6 . 2 137 . 19 ILE CD1 C 10.9 . 1 138 . 20 ARG N N 130.4 . 1 139 . 20 ARG H H 8.43 . 1 140 . 20 ARG HA H 4.70 . 1 141 . 20 ARG HB2 H 1.81 . 2 142 . 20 ARG HB3 H 0.81 . 2 143 . 20 ARG C C 173.6 . 1 144 . 20 ARG CA C 52.0 . 1 145 . 20 ARG CB C 35.4 . 1 146 . 20 ARG CG C 28.5 . 1 147 . 20 ARG CD C 43.2 . 1 148 . 21 TYR N N 115.7 . 1 149 . 21 TYR H H 9.22 . 1 150 . 21 TYR HA H 5.69 . 1 151 . 21 TYR HB2 H 2.70 . 2 152 . 21 TYR C C 175.9 . 1 153 . 21 TYR CA C 57.6 . 1 154 . 21 TYR CB C 41.2 . 1 155 . 22 PHE N N 120.3 . 1 156 . 22 PHE H H 9.82 . 1 157 . 22 PHE HA H 5.27 . 1 158 . 22 PHE HB2 H 2.91 . 2 159 . 22 PHE HB3 H 2.82 . 2 160 . 22 PHE C C 173.1 . 1 161 . 22 PHE CA C 55.3 . 1 162 . 22 PHE CB C 42.9 . 1 163 . 23 TYR N N 125.3 . 1 164 . 23 TYR H H 10.60 . 1 165 . 23 TYR HA H 4.29 . 1 166 . 23 TYR HB2 H 3.47 . 2 167 . 23 TYR HB3 H 2.73 . 2 168 . 23 TYR C C 173.9 . 1 169 . 23 TYR CA C 59.8 . 1 170 . 23 TYR CB C 40.8 . 1 171 . 24 ASN N N 125.7 . 1 172 . 24 ASN H H 7.80 . 1 173 . 24 ASN HA H 4.61 . 1 174 . 24 ASN HB2 H 2.86 . 2 175 . 24 ASN HB3 H 2.17 . 2 176 . 24 ASN C C 175.5 . 1 177 . 24 ASN CA C 50.8 . 1 178 . 24 ASN CB C 38.5 . 1 179 . 25 ALA N N 126.8 . 1 180 . 25 ALA H H 8.84 . 1 181 . 25 ALA HA H 3.76 . 1 182 . 25 ALA HB H 1.56 . 1 183 . 25 ALA C C 179.7 . 1 184 . 25 ALA CA C 55.1 . 1 185 . 25 ALA CB C 19.4 . 1 186 . 26 LYS N N 117.3 . 1 187 . 26 LYS H H 7.96 . 1 188 . 26 LYS HA H 4.07 . 1 189 . 26 LYS HB2 H 1.89 . 2 190 . 26 LYS C C 177.9 . 1 191 . 26 LYS CA C 58.9 . 1 192 . 26 LYS CB C 31.4 . 1 193 . 26 LYS CG C 25.6 . 1 194 . 26 LYS CD C 29.7 . 1 195 . 26 LYS CE C 42.6 . 1 196 . 27 ALA N N 118.9 . 1 197 . 27 ALA H H 6.86 . 1 198 . 27 ALA HA H 4.29 . 1 199 . 27 ALA HB H 1.18 . 1 200 . 27 ALA C C 178.3 . 1 201 . 27 ALA CA C 52.1 . 1 202 . 27 ALA CB C 20.9 . 1 203 . 28 GLY N N 107.1 . 1 204 . 28 GLY H H 8.18 . 1 205 . 28 GLY HA2 H 3.92 . 2 206 . 28 GLY HA3 H 3.61 . 2 207 . 28 GLY C C 173.8 . 1 208 . 28 GLY CA C 46.0 . 1 209 . 29 LEU N N 115.0 . 1 210 . 29 LEU H H 6.86 . 1 211 . 29 LEU HA H 4.74 . 1 212 . 29 LEU HB2 H 1.73 . 2 213 . 29 LEU HB3 H 1.43 . 2 214 . 29 LEU C C 173.8 . 1 215 . 29 LEU CA C 53.9 . 1 216 . 29 LEU CB C 45.7 . 1 217 . 29 LEU CD1 C 25.4 . 1 218 . 30 CYS N N 118.7 . 1 219 . 30 CYS H H 8.44 . 1 220 . 30 CYS HA H 5.61 . 1 221 . 30 CYS HB2 H 3.67 . 2 222 . 30 CYS HB3 H 2.67 . 2 223 . 30 CYS C C 174.0 . 1 224 . 30 CYS CA C 58.0 . 1 225 . 30 CYS CB C 49.3 . 1 226 . 31 GLN N N 123.4 . 1 227 . 31 GLN H H 8.81 . 1 228 . 31 GLN HA H 4.83 . 1 229 . 31 GLN HB2 H 2.15 . 2 230 . 31 GLN HB3 H 1.73 . 2 231 . 31 GLN C C 174.4 . 1 232 . 31 GLN CA C 54.1 . 1 233 . 31 GLN CB C 32.3 . 1 234 . 31 GLN CG C 35.4 . 1 235 . 32 THR N N 108.6 . 1 236 . 32 THR H H 8.08 . 1 237 . 32 THR HA H 5.29 . 1 238 . 32 THR HB H 4.04 . 1 239 . 32 THR C C 175.6 . 1 240 . 32 THR CA C 60.8 . 1 241 . 32 THR CB C 71.2 . 1 242 . 32 THR CG2 C 22.5 . 1 243 . 33 PHE N N 119.4 . 1 244 . 33 PHE H H 9.42 . 1 245 . 33 PHE HA H 4.86 . 1 246 . 33 PHE HB2 H 3.09 . 2 247 . 33 PHE HB3 H 2.96 . 2 248 . 33 PHE C C 171.8 . 1 249 . 33 PHE CA C 55.7 . 1 250 . 33 PHE CB C 41.6 . 1 251 . 34 VAL N N 119.0 . 1 252 . 34 VAL H H 8.41 . 1 253 . 34 VAL HA H 3.92 . 1 254 . 34 VAL HB H 1.95 . 1 255 . 34 VAL C C 173.6 . 1 256 . 34 VAL CA C 62.6 . 1 257 . 34 VAL CB C 31.3 . 1 258 . 34 VAL CG1 C 22.5 . 2 259 . 35 TYR N N 130.0 . 1 260 . 35 TYR H H 9.43 . 1 261 . 35 TYR HA H 4.89 . 1 262 . 35 TYR HB2 H 2.66 . 2 263 . 35 TYR HB3 H 2.51 . 2 264 . 35 TYR C C 174.8 . 1 265 . 35 TYR CA C 55.0 . 1 266 . 35 TYR CB C 44.1 . 1 267 . 36 GLY N N 114.5 . 1 268 . 36 GLY H H 8.64 . 1 269 . 36 GLY HA2 H 4.31 . 2 270 . 36 GLY HA3 H 3.25 . 2 271 . 36 GLY C C 175.3 . 1 272 . 36 GLY CA C 45.7 . 1 273 . 37 GLY N N 98.0 . 1 274 . 37 GLY H H 4.36 . 1 275 . 37 GLY HA2 H 4.23 . 2 276 . 37 GLY HA3 H 2.91 . 2 277 . 37 GLY C C 173.8 . 1 278 . 37 GLY CA C 46.0 . 1 279 . 38 CYS N N 115.3 . 1 280 . 38 CYS H H 7.80 . 1 281 . 38 CYS HA H 4.95 . 1 282 . 38 CYS HB2 H 3.96 . 2 283 . 38 CYS HB3 H 3.03 . 2 284 . 38 CYS C C 173.7 . 1 285 . 38 CYS CA C 55.7 . 1 286 . 38 CYS CB C 45.2 . 1 287 . 39 ARG N N 113.7 . 1 288 . 39 ARG H H 9.12 . 1 289 . 39 ARG HA H 3.94 . 1 290 . 39 ARG HB2 H 2.27 . 2 291 . 39 ARG C C 174.6 . 1 292 . 39 ARG CA C 56.9 . 1 293 . 39 ARG CB C 34.6 . 1 294 . 39 ARG CD C 44.2 . 1 295 . 40 ALA N N 118.3 . 1 296 . 40 ALA H H 7.42 . 1 297 . 40 ALA HA H 4.08 . 1 298 . 40 ALA HB H 1.20 . 1 299 . 40 ALA C C 180.4 . 1 300 . 40 ALA CA C 54.0 . 1 301 . 40 ALA CB C 19.9 . 1 302 . 41 LYS N N 121.5 . 1 303 . 41 LYS H H 8.35 . 1 304 . 41 LYS HA H 4.45 . 1 305 . 41 LYS HB2 H 2.26 . 2 306 . 41 LYS HB3 H 1.65 . 2 307 . 41 LYS C C 176.9 . 1 308 . 41 LYS CA C 55.7 . 1 309 . 41 LYS CB C 33.1 . 1 310 . 41 LYS CD C 29.5 . 1 311 . 41 LYS CE C 42.4 . 1 312 . 42 ARG N N 116.1 . 1 313 . 42 ARG H H 8.40 . 1 314 . 42 ARG HA H 3.67 . 1 315 . 42 ARG HB2 H 1.03 . 2 316 . 42 ARG HB3 H 0.37 . 2 317 . 42 ARG C C 178.1 . 1 318 . 42 ARG CA C 59.1 . 1 319 . 42 ARG CB C 28.5 . 1 320 . 42 ARG CG C 27.7 . 1 321 . 42 ARG CD C 43.9 . 1 322 . 43 ASN N N 116.4 . 1 323 . 43 ASN H H 7.27 . 1 324 . 43 ASN HA H 5.06 . 1 325 . 43 ASN HB2 H 3.34 . 2 326 . 43 ASN HB3 H 3.26 . 2 327 . 43 ASN C C 174.9 . 1 328 . 43 ASN CA C 51.1 . 1 329 . 43 ASN CB C 35.7 . 1 330 . 44 ASN N N 121.1 . 1 331 . 44 ASN H H 6.81 . 1 332 . 44 ASN HA H 4.90 . 1 333 . 44 ASN HB2 H 2.78 . 2 334 . 44 ASN HB3 H 2.51 . 2 335 . 44 ASN C C 174.4 . 1 336 . 44 ASN CA C 54.1 . 1 337 . 44 ASN CB C 39.6 . 1 338 . 45 PHE N N 122.9 . 1 339 . 45 PHE H H 9.98 . 1 340 . 45 PHE HA H 5.13 . 1 341 . 45 PHE HB2 H 3.41 . 2 342 . 45 PHE HB3 H 2.79 . 2 343 . 45 PHE C C 176.7 . 1 344 . 45 PHE CA C 56.3 . 1 345 . 45 PHE CB C 40.8 . 1 346 . 46 LYS N N 120.7 . 1 347 . 46 LYS H H 9.97 . 1 348 . 46 LYS HA H 4.38 . 1 349 . 46 LYS HB2 H 2.10 . 2 350 . 46 LYS HB3 H 1.99 . 2 351 . 46 LYS C C 176.2 . 1 352 . 46 LYS CA C 58.6 . 1 353 . 46 LYS CB C 32.3 . 1 354 . 46 LYS CD C 30.0 . 1 355 . 46 LYS CE C 42.9 . 1 356 . 47 SER N N 108.9 . 1 357 . 47 SER H H 7.50 . 1 358 . 47 SER HA H 4.54 . 1 359 . 47 SER HB2 H 4.12 . 2 360 . 47 SER HB3 H 3.87 . 2 361 . 47 SER C C 173.7 . 1 362 . 47 SER CA C 56.4 . 1 363 . 47 SER CB C 67.9 . 1 364 . 48 ALA N N 125.8 . 1 365 . 48 ALA H H 8.18 . 1 366 . 48 ALA HA H 3.15 . 1 367 . 48 ALA HB H 1.04 . 1 368 . 48 ALA C C 179.7 . 1 369 . 48 ALA CA C 55.4 . 1 370 . 48 ALA CB C 18.1 . 1 371 . 49 GLU N N 117.9 . 1 372 . 49 GLU H H 8.64 . 1 373 . 49 GLU HA H 3.88 . 1 374 . 49 GLU HB2 H 2.02 . 2 375 . 49 GLU HB3 H 1.86 . 2 376 . 49 GLU C C 179.5 . 1 377 . 49 GLU CA C 60.7 . 1 378 . 49 GLU CB C 29.5 . 1 379 . 49 GLU CG C 37.2 . 1 380 . 50 ASP N N 120.7 . 1 381 . 50 ASP H H 7.90 . 1 382 . 50 ASP HA H 4.29 . 1 383 . 50 ASP HB2 H 2.88 . 2 384 . 50 ASP HB3 H 2.73 . 2 385 . 50 ASP C C 178.1 . 1 386 . 50 ASP CA C 57.6 . 1 387 . 50 ASP CB C 40.5 . 1 388 . 51 CYS N N 120.0 . 1 389 . 51 CYS H H 7.05 . 1 390 . 51 CYS HA H 1.70 . 1 391 . 51 CYS HB2 H 3.18 . 2 392 . 51 CYS HB3 H 2.88 . 2 393 . 51 CYS C C 175.6 . 1 394 . 51 CYS CA C 58.9 . 1 395 . 51 CYS CB C 44.2 . 1 396 . 52 MET N N 121.2 . 1 397 . 52 MET H H 8.63 . 1 398 . 52 MET HA H 4.16 . 1 399 . 52 MET HB2 H 2.06 . 2 400 . 52 MET HB3 H 1.97 . 2 401 . 52 MET C C 180.6 . 1 402 . 52 MET CA C 56.7 . 1 403 . 52 MET CB C 33.6 . 1 404 . 53 ARG N N 121.5 . 1 405 . 53 ARG H H 8.32 . 1 406 . 53 ARG HA H 3.98 . 1 407 . 53 ARG HB2 H 1.93 . 2 408 . 53 ARG HB3 H 1.87 . 2 409 . 53 ARG C C 178.6 . 1 410 . 53 ARG CA C 59.6 . 1 411 . 53 ARG CB C 30.8 . 1 412 . 53 ARG CG C 28.7 . 1 413 . 53 ARG CD C 44.2 . 1 414 . 54 THR N N 113.5 . 1 415 . 54 THR H H 7.44 . 1 416 . 54 THR HA H 4.08 . 1 417 . 54 THR HB H 4.00 . 1 418 . 54 THR C C 176.6 . 1 419 . 54 THR CA C 66.4 . 1 420 . 54 THR CB C 69.5 . 1 421 . 54 THR CG2 C 22.77 . 1 422 . 55 CYS N N 115.1 . 1 423 . 55 CYS H H 8.29 . 1 424 . 55 CYS HA H 4.62 . 1 425 . 55 CYS HB2 H 2.25 . 2 426 . 55 CYS HB3 H 2.01 . 2 427 . 55 CYS C C 174.1 . 1 428 . 55 CYS CA C 54.5 . 1 429 . 55 CYS CB C 42.9 . 1 430 . 56 GLY N N 107.8 . 1 431 . 56 GLY H H 8.00 . 1 432 . 56 GLY HA2 H 3.85 . 2 433 . 56 GLY C C 174.5 . 1 434 . 56 GLY CA C 46.7 . 1 435 . 57 GLY N N 109.3 . 1 436 . 57 GLY H H 8.23 . 1 437 . 57 GLY HA2 H 3.97 . 2 438 . 57 GLY HA3 H 3.81 . 2 439 . 57 GLY C C 173.3 . 1 440 . 57 GLY CA C 45.2 . 1 441 . 58 ALA N N 129.7 . 1 442 . 58 ALA H H 7.99 . 1 443 . 58 ALA HA H 4.02 . 1 444 . 58 ALA HB H 1.32 . 1 445 . 58 ALA CA C 54.5 . 1 446 . 58 ALA CB C 18.9 . 1 stop_ save_