data_440 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Secondary structure of complement component C3a anaphylatoxin in solution as determined by NMR spectroscopy: Differences between crystal and solution conformations ; _BMRB_accession_number 440 _BMRB_flat_file_name bmr440.str _Entry_type update _Submission_date 1995-07-31 _Accession_date 1996-03-25 _Entry_origination BMRB _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 Nettesheim David G. . 2 Edalji Rohinton P. . 3 Mollison Karl W. . 4 Greer Jonathan . . 5 Zuiderweg Erik R.P. . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 322 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2010-06-11 revision BMRB 'Complete natural source information' 1999-06-14 revision BMRB 'Converted to BMRB NMR-STAR V 2.1 format' 1996-03-25 reformat BMRB 'Converted to the BMRB 1996-03-01 STAR flat-file format' 1995-07-31 original BMRB 'Last release in original BMRB flat-file format' stop_ save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full ; Nettesheim, David G., Edalji, Rohinton P., Mollison, Karl W., Greer, Jonathan, Zuiderweg, Erik R. P., "Secondary structure of complement component C3a anaphylatoxin in solution as determined by NMR spectroscopy: Differences between crystal and solution conformations," Proc. Natl. Acad. Sci. U.S.A. 85, 5036-5040 (1988). ; _Citation_title ; Secondary structure of complement component C3a anaphylatoxin in solution as determined by NMR spectroscopy: Differences between crystal and solution conformations ; _Citation_status published _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 Nettesheim David G. . 2 Edalji Rohinton P. . 3 Mollison Karl W. . 4 Greer Jonathan . . 5 Zuiderweg Erik R.P. . stop_ _Journal_abbreviation 'Proc. Natl. Acad. Sci. U.S.A.' _Journal_volume 85 _Journal_issue . _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 5036 _Page_last 5040 _Year 1988 _Details . save_ ################################## # Molecular system description # ################################## save_system_complement_protein_C3a _Saveframe_category molecular_system _Mol_system_name 'complement protein C3a' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'complement protein C3a' $complement_protein_C3a stop_ _System_molecular_weight . _System_oligomer_state ? _System_paramagnetic ? _System_thiol_state . _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_complement_protein_C3a _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'complement protein C3a' _Name_variant 'residues 1-76' _Molecular_mass . _Mol_thiol_state . _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 76 _Mol_residue_sequence ; SVQLTEKRMNKVGKYPKELR KCCEDGMRQNPMRFSCERRT RFISLGEACKKVFLDCCNYI TELRRQHARASHLGLA ; loop_ _Residue_seq_code _Residue_label 1 SER 2 VAL 3 GLN 4 LEU 5 THR 6 GLU 7 LYS 8 ARG 9 MET 10 ASN 11 LYS 12 VAL 13 GLY 14 LYS 15 TYR 16 PRO 17 LYS 18 GLU 19 LEU 20 ARG 21 LYS 22 CYS 23 CYS 24 GLU 25 ASP 26 GLY 27 MET 28 ARG 29 GLN 30 ASN 31 PRO 32 MET 33 ARG 34 PHE 35 SER 36 CYS 37 GLU 38 ARG 39 ARG 40 THR 41 ARG 42 PHE 43 ILE 44 SER 45 LEU 46 GLY 47 GLU 48 ALA 49 CYS 50 LYS 51 LYS 52 VAL 53 PHE 54 LEU 55 ASP 56 CYS 57 CYS 58 ASN 59 TYR 60 ILE 61 THR 62 GLU 63 LEU 64 ARG 65 ARG 66 GLN 67 HIS 68 ALA 69 ARG 70 ALA 71 SER 72 HIS 73 LEU 74 GLY 75 LEU 76 ALA stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2014-05-12 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 GB AAA72712 "synthetic human C3a gene [synthetic construct]" 100.00 78 98.68 100.00 9.60e-48 GB AAA73037 "C3a [synthetic construct]" 100.00 78 97.37 100.00 4.22e-47 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species _Strain _Fraction $complement_protein_C3a human 9606 Eukaryota Metazoa Homo sapiens generic serum 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 $complement_protein_C3a 'not available' . . . . . stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_one _Saveframe_category sample _Sample_type solution _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_list _Saveframe_category NMR_spectrometer _Manufacturer unknown _Model unknown _Field_strength 0 _Details 'spectrometer information not available' save_ ############################# # NMR applied experiments # ############################# save__1 _Saveframe_category NMR_applied_experiment _Sample_label $sample_one save_ ####################### # Sample conditions # ####################### save_sample_condition_set_one _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 3 . na temperature 293 . K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chem_shift_reference_par_set_one _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_citation_label _Correction_value_citation_label H2O/HDO H . . ppm 4.85 . . . . . $entry_citation $entry_citation 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_chemical_shift_assignment_data_set_one _Saveframe_category assigned_chemical_shifts _Details . loop_ _Sample_label $sample_one stop_ _Sample_conditions_label $sample_condition_set_one _Chem_shift_reference_set_label $chem_shift_reference_par_set_one _Mol_system_component_name 'complement protein C3a' _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 SER HA H 4.25 . 1 2 . 1 SER HB2 H 4.04 . 1 3 . 1 SER HB3 H 4.04 . 1 4 . 2 VAL H H 8.79 . 1 5 . 2 VAL HA H 4.12 . 1 6 . 2 VAL HB H 2.06 . 1 7 . 2 VAL HG1 H .98 . 1 8 . 2 VAL HG2 H .98 . 1 9 . 3 GLN H H 8.62 . 1 10 . 3 GLN HA H 4.29 . 1 11 . 3 GLN HB2 H 2.01 . 2 12 . 3 GLN HB3 H 2.1 . 2 13 . 3 GLN HG2 H 2.4 . 1 14 . 3 GLN HG3 H 2.4 . 1 15 . 3 GLN HE21 H 7.51 . 2 16 . 3 GLN HE22 H 6.89 . 2 17 . 4 LEU H H 8.32 . 1 18 . 4 LEU HA H 4.26 . 1 19 . 4 LEU HD1 H .82 . 2 20 . 4 LEU HD2 H .86 . 2 21 . 5 THR H H 8.02 . 1 22 . 5 THR HA H 4.04 . 1 23 . 5 THR HB H 4.27 . 1 24 . 5 THR HG2 H 1.25 . 1 25 . 6 GLU H H 8.25 . 1 26 . 6 GLU HA H 4.16 . 1 27 . 6 GLU HB2 H 2.13 . 1 28 . 6 GLU HB3 H 2.13 . 1 29 . 6 GLU HG2 H 2.46 . 2 30 . 6 GLU HG3 H 2.53 . 2 31 . 7 LYS H H 8.17 . 1 32 . 7 LYS HA H 4.17 . 1 33 . 7 LYS HB2 H 1.95 . 1 34 . 7 LYS HB3 H 1.95 . 1 35 . 8 ARG H H 8.29 . 1 36 . 8 ARG HA H 4.05 . 1 37 . 8 ARG HB2 H 1.95 . 1 38 . 8 ARG HB3 H 1.95 . 1 39 . 9 MET H H 8.29 . 1 40 . 9 MET HA H 4.27 . 1 41 . 9 MET HB2 H 2.11 . 1 42 . 9 MET HB3 H 2.11 . 1 43 . 9 MET HG2 H 2.57 . 2 44 . 9 MET HG3 H 2.69 . 2 45 . 10 ASN H H 8.47 . 1 46 . 10 ASN HA H 4.43 . 1 47 . 10 ASN HB2 H 2.9 . 2 48 . 10 ASN HB3 H 2.81 . 2 49 . 11 LYS H H 7.59 . 1 50 . 11 LYS HA H 4.02 . 1 51 . 12 VAL H H 7.84 . 1 52 . 12 VAL HA H 3.76 . 1 53 . 12 VAL HB H 2.1 . 1 54 . 12 VAL HG1 H .99 . 2 55 . 12 VAL HG2 H 1.02 . 2 56 . 13 GLY H H 7.77 . 1 57 . 13 GLY HA2 H 3.85 . 1 58 . 13 GLY HA3 H 3.85 . 1 59 . 14 LYS H H 7.43 . 1 60 . 14 LYS HA H 4.06 . 1 61 . 15 TYR H H 7.56 . 1 62 . 15 TYR HA H 4.67 . 1 63 . 15 TYR HB2 H 2.65 . 2 64 . 15 TYR HB3 H 2.92 . 2 65 . 15 TYR HD2 H 7.22 . 1 66 . 15 TYR HE2 H 6.66 . 1 67 . 16 PRO HA H 4.54 . 1 68 . 16 PRO HB2 H 1.95 . 1 69 . 16 PRO HB3 H 1.95 . 1 70 . 16 PRO HD2 H 3.76 . 2 71 . 16 PRO HD3 H 4.09 . 2 72 . 17 LYS H H 8.95 . 1 73 . 17 LYS HA H 3.65 . 1 74 . 18 GLU H H 9.18 . 1 75 . 18 GLU HA H 4.29 . 1 76 . 18 GLU HB2 H 2.16 . 1 77 . 18 GLU HB3 H 2.16 . 1 78 . 18 GLU HG2 H 2.48 . 2 79 . 18 GLU HG3 H 2.57 . 2 80 . 19 LEU H H 7.98 . 1 81 . 19 LEU HA H 4.67 . 1 82 . 19 LEU HD1 H .89 . 2 83 . 19 LEU HD2 H 1.01 . 2 84 . 20 ARG H H 7.7 . 1 85 . 20 ARG HA H 3.67 . 1 86 . 21 LYS H H 8.68 . 1 87 . 21 LYS HA H 4.03 . 1 88 . 22 CYS H H 7.28 . 1 89 . 22 CYS HA H 4.31 . 1 90 . 22 CYS HB2 H 3.4 . 2 91 . 22 CYS HB3 H 3.85 . 2 92 . 23 CYS H H 7.13 . 1 93 . 23 CYS HA H 3.96 . 1 94 . 23 CYS HB2 H 2.5 . 2 95 . 23 CYS HB3 H 3.04 . 2 96 . 24 GLU H H 8.43 . 1 97 . 24 GLU HA H 3.74 . 1 98 . 24 GLU HB2 H 2.08 . 1 99 . 24 GLU HB3 H 2.08 . 1 100 . 24 GLU HG2 H 2.38 . 2 101 . 24 GLU HG3 H 2.49 . 2 102 . 25 ASP H H 8.71 . 1 103 . 25 ASP HA H 4.36 . 1 104 . 25 ASP HB2 H 3.04 . 2 105 . 25 ASP HB3 H 3.24 . 2 106 . 26 GLY H H 7.48 . 1 107 . 26 GLY HA2 H 2.4 . 2 108 . 26 GLY HA3 H 2.98 . 2 109 . 27 MET H H 7.33 . 1 110 . 27 MET HA H 4.35 . 1 111 . 27 MET HE H 2.17 . 1 112 . 28 ARG H H 7.05 . 1 113 . 28 ARG HA H 4.18 . 1 114 . 29 GLN H H 8.71 . 1 115 . 29 GLN HA H 4.18 . 1 116 . 30 ASN H H 8.81 . 1 117 . 30 ASN HA H 5.21 . 1 118 . 30 ASN HB2 H 2.54 . 2 119 . 30 ASN HB3 H 2.84 . 2 120 . 30 ASN HD21 H 7.47 . 2 121 . 30 ASN HD22 H 7.73 . 2 122 . 31 PRO HA H 4.35 . 1 123 . 31 PRO HD2 H 3.62 . 2 124 . 31 PRO HD3 H 3.81 . 2 125 . 32 MET H H 8.02 . 1 126 . 32 MET HA H 4.23 . 1 127 . 33 ARG H H 7.89 . 1 128 . 33 ARG HA H 3.88 . 1 129 . 34 PHE H H 7.72 . 1 130 . 34 PHE HA H 4.99 . 1 131 . 34 PHE HB2 H 2.85 . 2 132 . 34 PHE HB3 H 3.22 . 2 133 . 34 PHE HD1 H 7.19 . 1 134 . 34 PHE HD2 H 7.19 . 1 135 . 34 PHE HE1 H 7.19 . 1 136 . 34 PHE HE2 H 7.19 . 1 137 . 34 PHE HZ H 7.34 . 1 138 . 35 SER H H 9.08 . 1 139 . 35 SER HA H 4.48 . 1 140 . 35 SER HB2 H 4.17 . 1 141 . 35 SER HB3 H 4.17 . 1 142 . 36 CYS H H 9.21 . 1 143 . 36 CYS HA H 4.4 . 1 144 . 36 CYS HB2 H 2.9 . 2 145 . 36 CYS HB3 H 2.99 . 2 146 . 37 GLU H H 8.9 . 1 147 . 37 GLU HA H 3.95 . 1 148 . 37 GLU HB2 H 2.01 . 2 149 . 37 GLU HB3 H 2.1 . 2 150 . 37 GLU HG2 H 2.39 . 2 151 . 37 GLU HG3 H 2.46 . 2 152 . 38 ARG H H 8.11 . 1 153 . 39 ARG H H 8.12 . 1 154 . 39 ARG HA H 4.06 . 1 155 . 39 ARG HG2 H 2.23 . 2 156 . 39 ARG HG3 H 2.39 . 2 157 . 39 ARG HD2 H 2.86 . 2 158 . 39 ARG HD3 H 3.01 . 2 159 . 40 THR H H 7.65 . 1 160 . 40 THR HA H 3.6 . 1 161 . 40 THR HB H 4.12 . 1 162 . 40 THR HG2 H 1.27 . 1 163 . 41 ARG H H 7.25 . 1 164 . 41 ARG HA H 3.93 . 1 165 . 42 PHE H H 7.44 . 1 166 . 42 PHE HA H 4.6 . 1 167 . 42 PHE HB2 H 2.85 . 2 168 . 42 PHE HB3 H 3.43 . 2 169 . 42 PHE HD1 H 7.28 . 1 170 . 42 PHE HD2 H 7.28 . 1 171 . 42 PHE HE1 H 7.28 . 1 172 . 42 PHE HE2 H 7.28 . 1 173 . 42 PHE HZ H 7.16 . 1 174 . 43 ILE H H 7.2 . 1 175 . 43 ILE HA H 4.23 . 1 176 . 43 ILE HB H 1.82 . 1 177 . 43 ILE HG12 H 1.01 . 2 178 . 43 ILE HG13 H 1.12 . 2 179 . 43 ILE HG2 H .77 . 1 180 . 43 ILE HD1 H .47 . 1 181 . 44 SER H H 8.7 . 1 182 . 44 SER HA H 4.59 . 1 183 . 44 SER HB2 H 3.83 . 2 184 . 44 SER HB3 H 3.88 . 2 185 . 45 LEU H H 7.22 . 1 186 . 45 LEU HA H 4.46 . 1 187 . 45 LEU HD1 H .78 . 2 188 . 45 LEU HD2 H .89 . 2 189 . 46 GLY H H 8.38 . 1 190 . 46 GLY HA2 H 3.97 . 2 191 . 46 GLY HA3 H 4.18 . 2 192 . 47 GLU H H 8.6 . 1 193 . 47 GLU HA H 3.92 . 1 194 . 47 GLU HG2 H 2.52 . 1 195 . 47 GLU HG3 H 2.52 . 1 196 . 48 ALA H H 8.68 . 1 197 . 48 ALA HA H 4.15 . 1 198 . 48 ALA HB H 1.48 . 1 199 . 49 CYS H H 8.06 . 1 200 . 49 CYS HA H 4.31 . 1 201 . 49 CYS HB2 H 2.94 . 2 202 . 49 CYS HB3 H 3.14 . 2 203 . 50 LYS H H 8.56 . 1 204 . 50 LYS HA H 3.76 . 1 205 . 51 LYS H H 8.06 . 1 206 . 51 LYS HA H 4.01 . 1 207 . 52 VAL H H 7.59 . 1 208 . 52 VAL HA H 3.56 . 1 209 . 52 VAL HB H 1.98 . 1 210 . 52 VAL HG1 H .27 . 2 211 . 52 VAL HG2 H 1.12 . 2 212 . 53 PHE H H 8.94 . 1 213 . 53 PHE HA H 3.98 . 1 214 . 53 PHE HB2 H 2.94 . 2 215 . 53 PHE HB3 H 3.49 . 2 216 . 53 PHE HD1 H 7.15 . 1 217 . 53 PHE HD2 H 7.15 . 1 218 . 53 PHE HE1 H 7.15 . 1 219 . 53 PHE HE2 H 7.15 . 1 220 . 53 PHE HZ H 7.15 . 1 221 . 54 LEU H H 8.7 . 1 222 . 54 LEU HA H 3.88 . 1 223 . 54 LEU HD1 H .89 . 2 224 . 54 LEU HD2 H .96 . 2 225 . 55 ASP H H 8.38 . 1 226 . 55 ASP HA H 4.47 . 1 227 . 55 ASP HB2 H 2.94 . 2 228 . 55 ASP HB3 H 3.04 . 2 229 . 56 CYS H H 8.9 . 1 230 . 56 CYS HA H 4.21 . 1 231 . 56 CYS HB2 H 3.08 . 2 232 . 56 CYS HB3 H 3.68 . 2 233 . 57 CYS H H 8.94 . 1 234 . 57 CYS HA H 4.14 . 1 235 . 57 CYS HB2 H 2.66 . 2 236 . 57 CYS HB3 H 3.04 . 2 237 . 58 ASN H H 9.36 . 1 238 . 58 ASN HA H 4.47 . 1 239 . 58 ASN HB2 H 2.85 . 2 240 . 58 ASN HB3 H 3.03 . 2 241 . 58 ASN HD21 H 6.75 . 2 242 . 58 ASN HD22 H 7.63 . 2 243 . 59 TYR H H 8.01 . 1 244 . 59 TYR HA H 4.35 . 1 245 . 59 TYR HB2 H 3.24 . 2 246 . 59 TYR HB3 H 3.35 . 2 247 . 59 TYR HD1 H 7.11 . 1 248 . 59 TYR HD2 H 7.11 . 1 249 . 59 TYR HE1 H 6.72 . 1 250 . 59 TYR HE2 H 6.72 . 1 251 . 60 ILE H H 8.09 . 1 252 . 60 ILE HA H 3.96 . 1 253 . 60 ILE HB H 2.02 . 1 254 . 60 ILE HG12 H 1.47 . 2 255 . 60 ILE HG13 H 1.62 . 2 256 . 60 ILE HG2 H 1.2 . 1 257 . 60 ILE HD1 H 1 . 1 258 . 61 THR H H 8.12 . 1 259 . 61 THR HA H 3.88 . 1 260 . 61 THR HB H 4.43 . 1 261 . 61 THR HG2 H 1.29 . 1 262 . 62 GLU H H 7.87 . 1 263 . 62 GLU HA H 4.09 . 1 264 . 62 GLU HB2 H 2.15 . 2 265 . 62 GLU HB3 H 2.19 . 2 266 . 62 GLU HG2 H 2.52 . 1 267 . 62 GLU HG3 H 2.52 . 1 268 . 63 LEU H H 7.75 . 1 269 . 63 LEU HA H 3.96 . 1 270 . 63 LEU HB2 H 1.42 . 1 271 . 63 LEU HB3 H 1.42 . 1 272 . 63 LEU HG H 1.57 . 1 273 . 63 LEU HD1 H .63 . 2 274 . 63 LEU HD2 H .73 . 2 275 . 64 ARG H H 8.38 . 1 276 . 64 ARG HA H 3.98 . 1 277 . 65 ARG H H 7.76 . 1 278 . 65 ARG HA H 4.13 . 1 279 . 66 GLN H H 8.12 . 1 280 . 66 GLN HA H 4.11 . 1 281 . 66 GLN HB2 H 2.13 . 1 282 . 66 GLN HB3 H 2.13 . 1 283 . 66 GLN HG2 H 2.39 . 2 284 . 66 GLN HG3 H 2.53 . 2 285 . 66 GLN HE21 H 6.79 . 2 286 . 66 GLN HE22 H 7.42 . 2 287 . 67 HIS H H 8.31 . 1 288 . 67 HIS HA H 4.53 . 1 289 . 67 HIS HB2 H 3.24 . 2 290 . 67 HIS HB3 H 3.35 . 2 291 . 67 HIS HD2 H 7.35 . 1 292 . 67 HIS HE1 H 8.6 . 1 293 . 68 ALA H H 8.12 . 1 294 . 68 ALA HA H 4.23 . 1 295 . 68 ALA HB H 1.49 . 1 296 . 69 ARG H H 8.08 . 1 297 . 69 ARG HA H 4.22 . 1 298 . 70 ALA H H 8.1 . 1 299 . 70 ALA HA H 4.26 . 1 300 . 70 ALA HB H 1.42 . 1 301 . 71 SER H H 8.09 . 1 302 . 71 SER HA H 4.36 . 1 303 . 71 SER HB2 H 3.82 . 1 304 . 71 SER HB3 H 3.82 . 1 305 . 72 HIS H H 8.35 . 1 306 . 72 HIS HA H 4.68 . 1 307 . 72 HIS HB2 H 3.23 . 2 308 . 72 HIS HB3 H 3.34 . 2 309 . 72 HIS HD2 H 7.28 . 1 310 . 72 HIS HE1 H 8.57 . 1 311 . 73 LEU H H 8.24 . 1 312 . 73 LEU HA H 4.34 . 1 313 . 73 LEU HD1 H .88 . 2 314 . 73 LEU HD2 H .93 . 2 315 . 74 GLY H H 8.42 . 1 316 . 74 GLY HA2 H 3.98 . 1 317 . 74 GLY HA3 H 3.98 . 1 318 . 75 LEU H H 8.08 . 1 319 . 75 LEU HA H 4.38 . 1 320 . 76 ALA H H 8.3 . 1 321 . 76 ALA HA H 4.31 . 1 322 . 76 ALA HB H 1.4 . 1 stop_ save_