data_4794 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Chemical Shift Assignments for Human WT Gelsolin Domain 2 ; _BMRB_accession_number 4794 _BMRB_flat_file_name bmr4794.str _Entry_type original _Submission_date 2000-07-25 _Accession_date 2000-07-25 _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 Kazmirski Steven L. . 2 Howard Mark J. . 3 Isaacson Rivka L. . 4 Fersht Alan R. . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 352 "13C chemical shifts" 215 "15N chemical shifts" 105 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2000-11-13 original author . stop_ loop_ _Related_BMRB_accession_number _Relationship 4795 'human D187N gelsolin domain 2' stop_ _Original_release_date 2000-11-13 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; Elucidating the Mechanism of Familial Amyloidosis--Finnish Type: NMR Studies of Human Gelsolin Domain 2 ; _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 Kazmirski Steven L. . 2 Howard Mark J. . 3 Isaacson Rivka L. . 4 Fersht Alan R. . stop_ _Journal_abbreviation 'Proc. Natl. Acad. Sci. U.S.A.' _Journal_volume 97 _Journal_issue . _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 10706 _Page_last 10711 _Year 2000 _Details . save_ ################################## # Molecular system description # ################################## save_gelsolin _Saveframe_category molecular_system _Mol_system_name 'human wild type gelsolin domain 2' _Abbreviation_common gelsolin _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'gelsolin domain 2' $Gelsolin_Domain_2 stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state monomer _System_paramagnetic no _System_thiol_state 'all disulfide bound' loop_ _Biological_function 'Actin binding protein' stop_ _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_Gelsolin_Domain_2 _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'Gelsolin Domain 2' _Abbreviation_common 'Gelsolin Domain 2' _Molecular_mass . _Mol_thiol_state 'all disulfide bound' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 116 _Mol_residue_sequence ; HVVPNEVVVQRLFQVKGRRV VRATEVPVSWESFNNGDCFI LDLGNNIHQWCGSNSNRYER LKATQVSKGIRDNERSGRAR VHVSEEGTEPEAMLQVLGPK PALPAGTEDTAKEDAA ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 151 HIS 2 152 VAL 3 153 VAL 4 154 PRO 5 155 ASN 6 156 GLU 7 157 VAL 8 158 VAL 9 159 VAL 10 160 GLN 11 161 ARG 12 161 LEU 13 163 PHE 14 164 GLN 15 165 VAL 16 166 LYS 17 167 GLY 18 168 ARG 19 169 ARG 20 170 VAL 21 171 VAL 22 172 ARG 23 273 ALA 24 274 THR 25 275 GLU 26 176 VAL 27 177 PRO 28 178 VAL 29 179 SER 30 180 TRP 31 181 GLU 32 182 SER 33 183 PHE 34 184 ASN 35 185 ASN 36 186 GLY 37 187 ASP 38 188 CYS 39 189 PHE 40 190 ILE 41 191 LEU 42 192 ASP 43 193 LEU 44 194 GLY 45 195 ASN 46 196 ASN 47 197 ILE 48 198 HIS 49 199 GLN 50 200 TRP 51 201 CYS 52 202 GLY 53 203 SER 54 204 ASN 55 205 SER 56 206 ASN 57 207 ARG 58 208 TYR 59 209 GLU 60 210 ARG 61 211 LEU 62 212 LYS 63 213 ALA 64 214 THR 65 215 GLN 66 216 VAL 67 217 SER 68 218 LYS 69 219 GLY 70 220 ILE 71 221 ARG 72 222 ASP 73 223 ASN 74 224 GLU 75 225 ARG 76 226 SER 77 227 GLY 78 228 ARG 79 229 ALA 80 230 ARG 81 231 VAL 82 232 HIS 83 233 VAL 84 234 SER 85 235 GLU 86 236 GLU 87 237 GLY 88 238 THR 89 239 GLU 90 240 PRO 91 241 GLU 92 242 ALA 93 243 MET 94 244 LEU 95 245 GLN 96 246 VAL 97 247 LEU 98 248 GLY 99 249 PRO 100 250 LYS 101 251 PRO 102 252 ALA 103 253 LEU 104 254 PRO 105 255 ALA 106 256 GLY 107 257 THR 108 258 GLU 109 259 ASP 110 260 THR 111 261 ALA 112 262 LYS 113 263 GLU 114 264 ASP 115 265 ALA 116 266 ALA stop_ _Sequence_homology_query_date 2008-08-19 _Sequence_homology_query_revised_last_date 2008-08-19 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 EMBL CAI14414 'gelsolin (amyloidosis, Finnish type) [Homo sapiens]' 78.45 228 100.00 100.00 2.55e-47 EMBL CAI14415 'gelsolin (amyloidosis, Finnish type) [Homo sapiens]' 100.00 260 100.00 100.00 6.36e-63 BMRB 4795 'Gelsolin Domain 2' 100.00 116 99.14 100.00 1.21e-61 PDB 1KCQ 'Human Gelsolin Domain 2 With A Cd2+ Bound' 89.66 104 100.00 100.00 4.10e-55 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $Gelsolin_Domain_2 Human 9606 Eukaryota Metazoa Homo sapien 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 $Gelsolin_Domain_2 'recombinant technology' . . . . . 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 $Gelsolin_Domain_2 0.5 mM '[U-13C; U-15N]' stop_ save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model AMX _Field_strength 500 _Details . save_ save_NMR_spectrometer_2 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model DRX _Field_strength 600 _Details . save_ ############################# # NMR applied experiments # ############################# save_1H-15N_HSQC_1 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-15N HSQC' _Sample_label . save_ save_1H-15N_TOCSY_2 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-15N TOCSY' _Sample_label . save_ save_1H-15N_NOESY_3 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-15N NOESY' _Sample_label . save_ save_HNCACB_4 _Saveframe_category NMR_applied_experiment _Experiment_name HNCACB _Sample_label . save_ save_CBCA(CO)NH_5 _Saveframe_category NMR_applied_experiment _Experiment_name CBCA(CO)NH _Sample_label . save_ save_NMR_spec_expt__0_1 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-15N HSQC' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_2 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-15N TOCSY' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_3 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-15N NOESY' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_4 _Saveframe_category NMR_applied_experiment _Experiment_name HNCACB _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_5 _Saveframe_category NMR_applied_experiment _Experiment_name CBCA(CO)NH _BMRB_pulse_sequence_accession_number . _Details . save_ ####################### # Sample conditions # ####################### save_Cond_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 7.2 0.2 n/a temperature 298 0.2 K 'ionic strength' 20 . mM 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 H 1 'methyl protons' ppm 0.0 internal direct . . . . DSS N 15 'methyl protons' ppm 0.0 . indirect . . . 0.101329118 DSS C 13 'methyl protons' ppm 0.0 . indirect . . . 0.251449530 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_shift_set_1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $Cond_1 _Chem_shift_reference_set_label $chemical_shift_reference _Mol_system_component_name 'gelsolin domain 2' _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 HIS CA C 54.10 0.1 1 2 . 1 HIS CB C 31.13 0.1 1 3 . 2 VAL N N 119.20 0.1 1 4 . 2 VAL H H 7.90 0.01 1 5 . 2 VAL CA C 59.86 0.1 1 6 . 2 VAL HA H 4.08 0.01 1 7 . 2 VAL CB C 29.72 0.1 1 8 . 2 VAL HB H 1.95 0.01 1 9 . 3 VAL N N 125.88 0.1 1 10 . 3 VAL H H 8.32 0.01 1 11 . 3 VAL CA C 59.30 0.1 1 12 . 3 VAL HA H 4.37 0.01 1 13 . 3 VAL CB C 31.87 0.1 1 14 . 3 VAL HB H 2.01 0.01 1 15 . 3 VAL HG1 H 0.90 0.01 1 16 . 3 VAL HG2 H 0.90 0.01 1 17 . 4 PRO CA C 62.58 0.1 1 18 . 4 PRO CB C 31.53 0.1 1 19 . 5 ASN N N 118.68 0.1 1 20 . 5 ASN H H 8.44 0.01 1 21 . 5 ASN CA C 52.83 0.1 1 22 . 5 ASN HA H 4.59 0.01 1 23 . 5 ASN CB C 38.15 0.1 1 24 . 5 ASN HB2 H 2.75 0.01 1 25 . 5 ASN HB3 H 2.75 0.01 1 26 . 6 GLU N N 121.20 0.1 1 27 . 6 GLU H H 8.27 0.01 1 28 . 6 GLU CA C 55.76 0.1 1 29 . 6 GLU HA H 4.26 0.01 1 30 . 6 GLU CB C 29.84 0.1 1 31 . 6 GLU HB2 H 1.92 0.01 1 32 . 6 GLU HB3 H 1.92 0.01 1 33 . 6 GLU HG2 H 2.19 0.01 1 34 . 6 GLU HG3 H 2.19 0.01 1 35 . 7 VAL N N 122.66 0.1 1 36 . 7 VAL H H 8.20 0.01 1 37 . 7 VAL CA C 61.74 0.1 1 38 . 7 VAL HA H 4.04 0.01 1 39 . 7 VAL CB C 31.79 0.1 1 40 . 7 VAL HB H 1.99 0.01 1 41 . 7 VAL HG1 H 0.89 0.01 1 42 . 7 VAL HG2 H 0.89 0.01 1 43 . 8 VAL N N 126.51 0.1 1 44 . 8 VAL H H 8.28 0.01 1 45 . 8 VAL CA C 61.66 0.1 1 46 . 8 VAL HA H 4.05 0.01 1 47 . 8 VAL CB C 32.00 0.1 1 48 . 8 VAL HB H 1.99 0.01 1 49 . 8 VAL HG1 H 0.92 0.01 1 50 . 8 VAL HG2 H 0.92 0.01 1 51 . 9 VAL N N 127.31 0.1 1 52 . 9 VAL H H 8.21 0.01 1 53 . 9 VAL CA C 61.30 0.1 1 54 . 9 VAL HA H 3.96 0.01 1 55 . 9 VAL CB C 32.90 0.1 1 56 . 9 VAL HB H 1.66 0.01 1 57 . 10 GLN N N 123.99 0.1 1 58 . 10 GLN H H 8.24 0.01 1 59 . 10 GLN CA C 55.17 0.1 1 60 . 10 GLN HA H 4.90 0.01 1 61 . 10 GLN CB C 29.85 0.1 1 62 . 10 GLN HB2 H 1.86 0.01 1 63 . 10 GLN HB3 H 1.86 0.01 1 64 . 10 GLN HG2 H 2.14 0.01 1 65 . 10 GLN HG3 H 2.14 0.01 1 66 . 11 ARG N N 121.25 0.1 1 67 . 11 ARG H H 8.61 0.01 1 68 . 11 ARG CA C 53.74 0.1 1 69 . 11 ARG HA H 4.65 0.01 1 70 . 11 ARG CB C 34.18 0.1 1 71 . 11 ARG HB2 H 1.63 0.01 1 72 . 11 ARG HB3 H 1.63 0.01 1 73 . 12 LEU N N 124.07 0.1 1 74 . 12 LEU H H 8.81 0.01 1 75 . 12 LEU CA C 52.31 0.1 1 76 . 12 LEU HA H 5.55 0.01 1 77 . 12 LEU CB C 45.95 0.1 1 78 . 12 LEU HB2 H 1.96 0.01 1 79 . 12 LEU HB3 H 1.96 0.01 1 80 . 13 PHE N N 121.49 0.1 1 81 . 13 PHE H H 9.14 0.01 1 82 . 13 PHE CA C 55.18 0.1 1 83 . 13 PHE HA H 5.31 0.01 1 84 . 13 PHE CB C 41.13 0.1 1 85 . 13 PHE HB2 H 2.75 0.01 1 86 . 13 PHE HB3 H 2.75 0.01 1 87 . 14 GLN N N 124.39 0.1 1 88 . 14 GLN H H 9.55 0.01 1 89 . 14 GLN CA C 54.15 0.1 1 90 . 14 GLN HA H 4.01 0.01 1 91 . 14 GLN CB C 29.42 0.1 1 92 . 15 VAL N N 129.54 0.1 1 93 . 15 VAL H H 8.87 0.01 1 94 . 15 VAL CA C 61.03 0.1 1 95 . 15 VAL HA H 4.66 0.01 1 96 . 15 VAL CB C 31.40 0.1 1 97 . 15 VAL HB H 1.59 0.01 1 98 . 15 VAL HG1 H 0.63 0.01 1 99 . 15 VAL HG2 H 0.63 0.01 1 100 . 16 LYS N N 125.98 0.1 1 101 . 16 LYS H H 8.07 0.01 1 102 . 16 LYS CA C 53.75 0.1 1 103 . 16 LYS HA H 5.35 0.01 1 104 . 16 LYS CB C 38.23 0.1 1 105 . 16 LYS HB2 H 1.50 0.01 1 106 . 16 LYS HB3 H 1.50 0.01 1 107 . 17 GLY N N 119.81 0.1 1 108 . 17 GLY H H 10.62 0.01 1 109 . 17 GLY CA C 44.31 0.1 1 110 . 17 GLY HA2 H 3.83 0.01 1 111 . 17 GLY HA3 H 3.83 0.01 1 112 . 18 ARG N N 120.13 0.1 1 113 . 18 ARG H H 8.15 0.01 1 114 . 18 ARG CA C 56.78 0.1 1 115 . 18 ARG HA H 4.25 0.01 1 116 . 18 ARG CB C 30.48 0.1 1 117 . 18 ARG HB2 H 1.68 0.01 1 118 . 18 ARG HB3 H 1.68 0.01 1 119 . 21 VAL N N 127.82 0.1 1 120 . 21 VAL H H 8.47 0.01 1 121 . 21 VAL CA C 60.79 0.1 1 122 . 21 VAL HA H 4.17 0.01 1 123 . 21 VAL CB C 31.46 0.1 1 124 . 21 VAL HB H 1.60 0.01 1 125 . 21 VAL HG1 H 0.68 0.01 1 126 . 21 VAL HG2 H 0.68 0.01 1 127 . 22 ARG N N 125.85 0.1 1 128 . 22 ARG H H 8.13 0.01 1 129 . 22 ARG CA C 53.66 0.1 1 130 . 22 ARG HA H 4.59 0.01 1 131 . 22 ARG CB C 32.84 0.1 1 132 . 22 ARG HB2 H 1.75 0.01 1 133 . 22 ARG HB3 H 1.75 0.01 1 134 . 23 ALA N N 125.20 0.1 1 135 . 23 ALA H H 8.68 0.01 1 136 . 23 ALA CA C 49.25 0.1 1 137 . 23 ALA HA H 5.64 0.01 1 138 . 23 ALA CB C 20.04 0.1 1 139 . 24 THR N N 117.83 0.1 1 140 . 24 THR H H 9.02 0.01 1 141 . 24 THR CA C 59.83 0.1 1 142 . 24 THR HA H 3.99 0.01 1 143 . 24 THR CB C 70.97 0.1 1 144 . 24 THR HB H 3.99 0.01 1 145 . 24 THR HG2 H 1.23 0.01 1 146 . 25 GLU N N 127.73 0.1 1 147 . 25 GLU H H 9.08 0.01 1 148 . 25 GLU CA C 56.71 0.1 1 149 . 25 GLU HA H 4.53 0.01 1 150 . 25 GLU CB C 28.03 0.1 1 151 . 25 GLU HB2 H 1.80 0.01 1 152 . 25 GLU HB3 H 1.80 0.01 1 153 . 26 VAL N N 120.38 0.1 1 154 . 26 VAL H H 8.68 0.01 1 155 . 26 VAL CA C 58.04 0.1 1 156 . 26 VAL HA H 5.26 0.01 1 157 . 26 VAL CB C 32.59 0.1 1 158 . 27 PRO CA C 62.34 0.1 1 159 . 27 PRO CB C 28.77 0.1 1 160 . 28 VAL N N 123.53 0.1 1 161 . 28 VAL H H 8.77 0.01 1 162 . 28 VAL CA C 62.26 0.1 1 163 . 28 VAL HA H 3.45 0.01 1 164 . 28 VAL CB C 28.77 0.1 1 165 . 28 VAL HB H 2.05 0.01 1 166 . 28 VAL HG1 H 1.07 0.01 1 167 . 28 VAL HG2 H 1.07 0.01 1 168 . 29 SER N N 121.33 0.1 1 169 . 29 SER H H 7.27 0.01 1 170 . 29 SER CA C 55.77 0.1 1 171 . 29 SER HA H 4.52 0.01 1 172 . 29 SER CB C 62.98 0.1 1 173 . 29 SER HB2 H 3.12 0.01 1 174 . 29 SER HB3 H 3.12 0.01 1 175 . 30 TRP N N 128.65 0.1 1 176 . 30 TRP H H 9.78 0.01 1 177 . 30 TRP CA C 59.81 0.1 1 178 . 30 TRP CB C 29.98 0.1 1 179 . 31 GLU N N 117.85 0.1 1 180 . 31 GLU H H 8.82 0.01 1 181 . 31 GLU CA C 58.10 0.1 1 182 . 31 GLU HA H 4.08 0.01 1 183 . 31 GLU CB C 28.80 0.1 1 184 . 31 GLU HB2 H 2.31 0.01 2 185 . 31 GLU HB3 H 1.93 0.01 2 186 . 32 SER N N 112.96 0.1 1 187 . 32 SER H H 7.58 0.01 1 188 . 32 SER CA C 58.10 0.1 1 189 . 32 SER HA H 4.38 0.01 1 190 . 32 SER CB C 63.44 0.1 1 191 . 32 SER HB2 H 3.95 0.01 1 192 . 32 SER HB3 H 3.95 0.01 1 193 . 33 PHE N N 119.20 0.1 1 194 . 33 PHE H H 7.76 0.01 1 195 . 33 PHE CA C 58.21 0.1 1 196 . 33 PHE HA H 3.25 0.01 1 197 . 33 PHE CB C 41.36 0.1 1 198 . 34 ASN N N 111.89 0.1 1 199 . 34 ASN H H 7.24 0.01 1 200 . 34 ASN CA C 52.93 0.1 1 201 . 34 ASN CB C 41.49 0.1 1 202 . 35 ASN N N 114.60 0.1 1 203 . 35 ASN H H 8.83 0.01 1 204 . 35 ASN CA C 53.24 0.1 1 205 . 35 ASN HA H 5.13 0.01 1 206 . 35 ASN CB C 38.60 0.1 1 207 . 36 GLY N N 107.57 0.1 1 208 . 36 GLY H H 9.70 0.01 1 209 . 36 GLY CA C 44.55 0.1 1 210 . 36 GLY HA2 H 4.26 0.01 2 211 . 36 GLY HA3 H 3.77 0.01 2 212 . 37 ASP N N 123.99 0.1 1 213 . 37 ASP H H 7.17 0.01 1 214 . 37 ASP CA C 52.62 0.1 1 215 . 37 ASP HA H 5.50 0.01 1 216 . 37 ASP CB C 43.92 0.1 1 217 . 37 ASP HB2 H 3.16 0.01 2 218 . 37 ASP HB3 H 2.53 0.01 2 219 . 38 CYS N N 114.02 0.1 1 220 . 38 CYS H H 7.66 0.01 1 221 . 38 CYS CA C 57.17 0.1 1 222 . 38 CYS HA H 6.04 0.01 1 223 . 38 CYS CB C 48.87 0.1 1 224 . 38 CYS HB2 H 2.87 0.01 1 225 . 38 CYS HB3 H 2.87 0.01 1 226 . 39 PHE N N 119.75 0.1 1 227 . 39 PHE H H 10.51 0.01 1 228 . 39 PHE CA C 56.57 0.1 1 229 . 39 PHE HA H 5.47 0.01 1 230 . 39 PHE CB C 43.88 0.1 1 231 . 40 ILE N N 120.36 0.1 1 232 . 40 ILE H H 9.21 0.01 1 233 . 40 ILE CA C 57.99 0.1 1 234 . 40 ILE HA H 5.22 0.01 1 235 . 40 ILE CB C 39.72 0.1 1 236 . 40 ILE HB H 1.98 0.01 1 237 . 41 LEU N N 130.91 0.1 1 238 . 41 LEU H H 9.84 0.01 1 239 . 41 LEU CA C 52.74 0.1 1 240 . 41 LEU HA H 5.17 0.01 1 241 . 41 LEU CB C 42.55 0.1 1 242 . 42 ASP N N 129.85 0.1 1 243 . 42 ASP H H 9.61 0.01 1 244 . 42 ASP CA C 53.11 0.1 1 245 . 42 ASP CB C 42.05 0.1 1 246 . 42 ASP HB2 H 3.07 0.01 1 247 . 42 ASP HB3 H 3.07 0.01 1 248 . 43 LEU N N 122.63 0.1 1 249 . 43 LEU H H 8.17 0.01 1 250 . 43 LEU CA C 52.22 0.1 1 251 . 43 LEU HA H 5.20 0.01 1 252 . 43 LEU CB C 41.17 0.1 1 253 . 43 LEU HB2 H 2.02 0.01 1 254 . 43 LEU HB3 H 2.02 0.01 1 255 . 44 GLY N N 111.42 0.1 1 256 . 44 GLY H H 8.62 0.01 1 257 . 44 GLY CA C 45.48 0.1 1 258 . 44 GLY HA2 H 4.47 0.01 2 259 . 44 GLY HA3 H 3.28 0.01 2 260 . 45 ASN CA C 53.23 0.1 1 261 . 45 ASN CB C 37.33 0.1 1 262 . 46 ASN N N 116.54 0.1 1 263 . 46 ASN H H 7.08 0.01 1 264 . 46 ASN CA C 52.18 0.1 1 265 . 46 ASN HA H 5.52 0.01 1 266 . 46 ASN CB C 44.23 0.1 1 267 . 46 ASN HB2 H 2.71 0.01 2 268 . 46 ASN HB3 H 2.35 0.01 2 269 . 47 ILE N N 123.33 0.1 1 270 . 47 ILE H H 9.12 0.01 1 271 . 47 ILE CA C 59.64 0.1 1 272 . 47 ILE HA H 4.68 0.01 1 273 . 47 ILE CB C 40.71 0.1 1 274 . 47 ILE HB H 1.57 0.01 1 275 . 48 HIS N N 128.04 0.1 1 276 . 48 HIS H H 9.64 0.01 1 277 . 48 HIS CA C 55.53 0.1 1 278 . 48 HIS HA H 5.11 0.01 1 279 . 48 HIS CB C 32.19 0.1 1 280 . 48 HIS HB2 H 3.22 0.01 1 281 . 48 HIS HB3 H 3.22 0.01 1 282 . 49 GLN N N 127.62 0.1 1 283 . 49 GLN H H 9.20 0.01 1 284 . 49 GLN CA C 54.07 0.1 1 285 . 49 GLN HA H 4.92 0.01 1 286 . 49 GLN CB C 29.96 0.1 1 287 . 49 GLN HB2 H 1.98 0.01 1 288 . 49 GLN HB3 H 1.98 0.01 1 289 . 50 TRP N N 130.92 0.1 1 290 . 50 TRP H H 9.51 0.01 1 291 . 50 TRP CA C 55.76 0.1 1 292 . 50 TRP HA H 5.55 0.01 1 293 . 50 TRP CB C 33.84 0.1 1 294 . 50 TRP HB2 H 3.56 0.01 2 295 . 50 TRP HB3 H 3.05 0.01 2 296 . 51 CYS N N 122.92 0.1 1 297 . 51 CYS H H 7.33 0.01 1 298 . 51 CYS CA C 55.83 0.1 1 299 . 51 CYS HA H 5.41 0.01 1 300 . 51 CYS CB C 44.78 0.1 1 301 . 51 CYS HB2 H 3.23 0.01 2 302 . 51 CYS HB3 H 2.93 0.01 2 303 . 52 GLY N N 122.92 0.1 1 304 . 52 GLY H H 7.33 0.01 1 305 . 52 GLY CA C 44.77 0.1 1 306 . 52 GLY HA2 H 3.63 0.01 1 307 . 52 GLY HA3 H 3.63 0.01 1 308 . 53 SER N N 122.01 0.1 1 309 . 53 SER H H 9.86 0.01 1 310 . 53 SER CA C 60.91 0.1 1 311 . 53 SER HA H 5.64 0.01 1 312 . 53 SER CB C 61.75 0.1 1 313 . 54 ASN N N 116.71 0.1 1 314 . 54 ASN H H 8.72 0.01 1 315 . 54 ASN CA C 51.82 0.1 1 316 . 54 ASN HA H 5.25 0.01 1 317 . 54 ASN CB C 38.73 0.1 1 318 . 54 ASN HB2 H 3.16 0.01 2 319 . 54 ASN HB3 H 2.60 0.01 2 320 . 55 SER N N 118.23 0.1 1 321 . 55 SER H H 7.62 0.01 1 322 . 55 SER CA C 58.40 0.1 1 323 . 55 SER CB C 63.49 0.1 1 324 . 56 ASN N N 121.73 0.1 1 325 . 56 ASN H H 8.86 0.01 1 326 . 56 ASN CA C 51.24 0.1 1 327 . 56 ASN HA H 5.10 0.01 1 328 . 56 ASN CB C 40.23 0.1 1 329 . 57 ARG N N 116.68 0.1 1 330 . 57 ARG H H 8.77 0.01 1 331 . 57 ARG CA C 58.53 0.1 1 332 . 57 ARG HA H 5.13 0.01 1 333 . 57 ARG CB C 28.90 0.1 1 334 . 57 ARG HB2 H 2.51 0.01 1 335 . 57 ARG HB3 H 2.51 0.01 1 336 . 58 TYR N N 121.46 0.1 1 337 . 58 TYR H H 8.06 0.01 1 338 . 58 TYR CA C 59.95 0.1 1 339 . 58 TYR HA H 4.14 0.01 1 340 . 58 TYR CB C 36.19 0.1 1 341 . 58 TYR HB2 H 3.05 0.01 1 342 . 58 TYR HB3 H 3.05 0.01 1 343 . 59 GLU N N 123.82 0.1 1 344 . 59 GLU H H 8.48 0.01 1 345 . 59 GLU CA C 58.83 0.1 1 346 . 59 GLU HA H 3.68 0.01 1 347 . 59 GLU CB C 28.08 0.1 1 348 . 60 ARG N N 118.80 0.1 1 349 . 60 ARG H H 7.96 0.01 1 350 . 60 ARG CA C 59.22 0.1 1 351 . 60 ARG HA H 4.17 0.01 1 352 . 60 ARG CB C 29.30 0.1 1 353 . 60 ARG HB2 H 2.07 0.01 1 354 . 60 ARG HB3 H 2.07 0.01 1 355 . 61 LEU N N 119.82 0.1 1 356 . 61 LEU H H 7.69 0.01 1 357 . 61 LEU CA C 57.18 0.1 1 358 . 61 LEU HA H 4.10 0.01 1 359 . 61 LEU CB C 41.56 0.1 1 360 . 61 LEU HB2 H 1.72 0.01 1 361 . 61 LEU HB3 H 1.72 0.01 1 362 . 62 LYS N N 120.13 0.1 1 363 . 62 LYS H H 8.08 0.01 1 364 . 62 LYS CA C 56.46 0.1 1 365 . 62 LYS HA H 4.19 0.01 1 366 . 62 LYS CB C 30.44 0.1 1 367 . 62 LYS HB2 H 1.84 0.01 1 368 . 62 LYS HB3 H 1.84 0.01 1 369 . 63 ALA N N 121.31 0.1 1 370 . 63 ALA H H 8.91 0.01 1 371 . 63 ALA CA C 55.18 0.1 1 372 . 63 ALA HA H 3.75 0.01 1 373 . 63 ALA CB C 16.32 0.1 1 374 . 63 ALA HB H 1.38 0.01 1 375 . 64 THR N N 114.68 0.1 1 376 . 64 THR H H 7.45 0.01 1 377 . 64 THR CA C 64.94 0.1 1 378 . 64 THR HA H 4.31 0.01 1 379 . 64 THR CB C 68.57 0.1 1 380 . 65 GLN N N 120.80 0.1 1 381 . 65 GLN H H 7.53 0.01 1 382 . 65 GLN CA C 58.28 0.1 1 383 . 65 GLN HA H 3.95 0.01 1 384 . 65 GLN CB C 27.71 0.1 1 385 . 65 GLN HB2 H 2.31 0.01 1 386 . 65 GLN HB3 H 2.31 0.01 1 387 . 66 VAL N N 121.83 0.1 1 388 . 66 VAL H H 8.89 0.01 1 389 . 66 VAL CA C 65.02 0.1 1 390 . 66 VAL HA H 3.61 0.01 1 391 . 66 VAL CB C 30.72 0.1 1 392 . 66 VAL HB H 1.90 0.01 1 393 . 67 SER N N 118.01 0.1 1 394 . 67 SER H H 8.55 0.01 1 395 . 67 SER CA C 62.66 0.1 1 396 . 67 SER HA H 3.75 0.01 1 397 . 68 LYS N N 120.80 0.1 1 398 . 68 LYS H H 7.84 0.01 1 399 . 68 LYS CA C 59.37 0.1 1 400 . 68 LYS HA H 3.65 0.01 1 401 . 68 LYS CB C 31.73 0.1 1 402 . 68 LYS HB2 H 1.81 0.01 1 403 . 68 LYS HB3 H 1.81 0.01 1 404 . 69 GLY N N 106.98 0.1 1 405 . 69 GLY H H 7.99 0.01 1 406 . 69 GLY CA C 46.37 0.1 1 407 . 69 GLY HA2 H 3.81 0.01 1 408 . 69 GLY HA3 H 4.28 0.01 1 409 . 70 ILE N N 122.53 0.1 1 410 . 70 ILE H H 7.98 0.01 1 411 . 70 ILE CA C 65.16 0.1 1 412 . 70 ILE HA H 3.53 0.01 1 413 . 70 ILE CB C 38.02 0.1 1 414 . 71 ARG N N 118.38 0.1 1 415 . 71 ARG H H 7.64 0.01 1 416 . 71 ARG CA C 59.47 0.1 1 417 . 71 ARG CB C 29.34 0.1 1 418 . 72 ASP N N 116.51 0.1 1 419 . 72 ASP H H 8.98 0.01 1 420 . 72 ASP CA C 56.58 0.1 1 421 . 72 ASP HA H 4.32 0.01 1 422 . 72 ASP CB C 39.70 0.1 1 423 . 72 ASP HB2 H 2.57 0.01 1 424 . 72 ASP HB3 H 2.57 0.01 1 425 . 73 ASN N N 116.20 0.1 1 426 . 73 ASN H H 8.56 0.01 1 427 . 73 ASN CA C 53.79 0.1 1 428 . 73 ASN HA H 4.86 0.01 1 429 . 73 ASN CB C 37.99 0.1 1 430 . 73 ASN HB2 H 3.05 0.01 2 431 . 73 ASN HB3 H 2.84 0.01 2 432 . 74 GLU N N 117.08 0.1 1 433 . 74 GLU H H 7.81 0.01 1 434 . 74 GLU CA C 57.13 0.1 1 435 . 74 GLU HA H 4.55 0.01 1 436 . 74 GLU CB C 29.72 0.1 1 437 . 74 GLU HB2 H 2.31 0.01 1 438 . 74 GLU HB3 H 2.31 0.01 1 439 . 75 ARG N N 114.55 0.1 1 440 . 75 ARG H H 7.14 0.01 1 441 . 75 ARG CA C 52.24 0.1 1 442 . 75 ARG HA H 4.87 0.01 1 443 . 75 ARG HB2 H 2.17 0.01 1 444 . 75 ARG HB3 H 2.17 0.01 1 445 . 76 SER N N 114.24 0.1 1 446 . 76 SER H H 8.07 0.01 1 447 . 76 SER CA C 58.61 0.1 1 448 . 76 SER HA H 4.30 0.01 1 449 . 76 SER HB2 H 4.13 0.01 1 450 . 76 SER HB3 H 4.13 0.01 1 451 . 77 GLY N N 105.82 0.1 1 452 . 77 GLY H H 8.92 0.01 1 453 . 77 GLY CA C 44.77 0.1 1 454 . 77 GLY HA2 H 4.33 0.01 2 455 . 77 GLY HA3 H 3.65 0.01 2 456 . 78 ARG N N 121.06 0.1 1 457 . 78 ARG H H 7.95 0.01 1 458 . 78 ARG CA C 55.19 0.1 1 459 . 78 ARG HA H 4.36 0.01 1 460 . 78 ARG CB C 28.83 0.1 1 461 . 78 ARG HB2 H 1.86 0.01 1 462 . 78 ARG HB3 H 1.86 0.01 1 463 . 79 ALA N N 119.07 0.1 1 464 . 79 ALA H H 6.91 0.01 1 465 . 79 ALA CA C 50.76 0.1 1 466 . 79 ALA HA H 4.58 0.01 1 467 . 79 ALA CB C 20.86 0.1 1 468 . 79 ALA HB H 1.17 0.01 1 469 . 80 ARG N N 119.66 0.1 1 470 . 80 ARG H H 7.71 0.01 1 471 . 80 ARG CA C 54.07 0.1 1 472 . 80 ARG HA H 4.40 0.01 1 473 . 80 ARG CB C 31.83 0.1 1 474 . 80 ARG HB2 H 1.95 0.01 1 475 . 80 ARG HB3 H 1.95 0.01 1 476 . 81 VAL N N 124.25 0.1 1 477 . 81 VAL H H 8.41 0.01 1 478 . 81 VAL CA C 60.50 0.1 1 479 . 81 VAL HA H 4.63 0.01 1 480 . 81 VAL CB C 31.80 0.1 1 481 . 81 VAL HB H 1.81 0.01 1 482 . 81 VAL HG1 H 0.76 0.01 1 483 . 81 VAL HG2 H 0.76 0.01 1 484 . 82 HIS N N 129.45 0.1 1 485 . 82 HIS H H 9.21 0.01 1 486 . 82 HIS CA C 53.54 0.1 1 487 . 82 HIS HA H 4.78 0.01 1 488 . 82 HIS CB C 31.98 0.1 1 489 . 82 HIS HB2 H 2.95 0.01 2 490 . 82 HIS HB3 H 2.72 0.01 2 491 . 83 VAL N N 129.21 0.1 1 492 . 83 VAL H H 9.19 0.01 1 493 . 83 VAL CA C 61.83 0.1 1 494 . 83 VAL HA H 4.99 0.01 1 495 . 83 VAL HB H 2.01 0.01 1 496 . 83 VAL HG1 H 0.93 0.01 1 497 . 83 VAL HG2 H 0.93 0.01 1 498 . 84 SER N N 123.36 0.1 1 499 . 84 SER H H 9.66 0.01 1 500 . 84 SER CA C 57.18 0.1 1 501 . 84 SER CB C 65.95 0.1 1 502 . 85 GLU N N 117.08 0.1 1 503 . 85 GLU H H 7.79 0.01 1 504 . 85 GLU CA C 52.84 0.1 1 505 . 85 GLU HA H 4.15 0.01 1 506 . 85 GLU CB C 32.15 0.1 1 507 . 85 GLU HB2 H 1.66 0.01 1 508 . 85 GLU HB3 H 1.66 0.01 1 509 . 86 GLU N N 119.60 0.1 1 510 . 86 GLU H H 7.44 0.01 1 511 . 86 GLU CA C 57.48 0.1 1 512 . 86 GLU CB C 29.25 0.1 1 513 . 87 GLY N N 118.29 0.1 1 514 . 87 GLY H H 9.87 0.01 1 515 . 87 GLY CA C 44.92 0.1 1 516 . 87 GLY HA2 H 3.88 0.01 1 517 . 87 GLY HA3 H 3.88 0.01 1 518 . 88 THR N N 113.60 0.1 1 519 . 88 THR H H 8.58 0.01 1 520 . 88 THR CA C 58.72 0.1 1 521 . 88 THR CB C 67.80 0.1 1 522 . 89 GLU N N 123.01 0.1 1 523 . 89 GLU H H 8.95 0.01 1 524 . 89 GLU CA C 56.79 0.1 1 525 . 89 GLU HA H 4.43 0.01 1 526 . 89 GLU CB C 27.46 0.1 1 527 . 89 GLU HB2 H 2.55 0.01 2 528 . 89 GLU HB3 H 2.34 0.01 2 529 . 90 PRO CA C 61.08 0.1 1 530 . 90 PRO CB C 32.02 0.1 1 531 . 91 GLU N N 123.51 0.1 1 532 . 91 GLU H H 8.91 0.01 1 533 . 91 GLU CA C 59.14 0.1 1 534 . 91 GLU CB C 28.60 0.1 1 535 . 92 ALA N N 118.12 0.1 1 536 . 92 ALA H H 8.62 0.01 1 537 . 92 ALA CA C 54.26 0.1 1 538 . 92 ALA CB C 19.13 0.1 1 539 . 93 MET N N 112.90 0.1 1 540 . 93 MET H H 6.89 0.01 1 541 . 93 MET CA C 58.57 0.1 1 542 . 93 MET HA H 3.38 0.01 1 543 . 93 MET CB C 32.79 0.1 1 544 . 93 MET HB2 H 1.84 0.01 1 545 . 93 MET HB3 H 1.84 0.01 1 546 . 94 LEU N N 118.80 0.1 1 547 . 94 LEU H H 7.12 0.01 1 548 . 94 LEU CA C 56.18 0.1 1 549 . 94 LEU HA H 4.07 0.01 1 550 . 94 LEU CB C 39.70 0.1 1 551 . 94 LEU HB2 H 1.83 0.01 1 552 . 94 LEU HB3 H 1.83 0.01 1 553 . 95 GLN N N 119.47 0.1 1 554 . 95 GLN H H 8.40 0.01 1 555 . 95 GLN CA C 57.82 0.1 1 556 . 95 GLN HA H 3.88 0.01 1 557 . 95 GLN CB C 27.72 0.1 1 558 . 95 GLN HB2 H 2.05 0.01 1 559 . 95 GLN HB3 H 2.05 0.01 1 560 . 96 VAL N N 116.41 0.1 1 561 . 96 VAL H H 6.78 0.01 1 562 . 96 VAL CA C 64.11 0.1 1 563 . 96 VAL HA H 3.77 0.01 1 564 . 96 VAL CB C 32.26 0.1 1 565 . 96 VAL HB H 1.75 0.01 1 566 . 96 VAL HG1 H 0.67 0.01 1 567 . 96 VAL HG2 H 0.67 0.01 1 568 . 97 LEU N N 116.41 0.1 1 569 . 97 LEU H H 7.60 0.01 1 570 . 97 LEU CA C 54.69 0.1 1 571 . 97 LEU HA H 3.88 0.01 1 572 . 97 LEU CB C 40.48 0.1 1 573 . 97 LEU HB2 H 0.93 0.01 1 574 . 97 LEU HB3 H 0.93 0.01 1 575 . 98 GLY N N 108.97 0.1 1 576 . 98 GLY H H 7.83 0.01 1 577 . 98 GLY CA C 43.49 0.1 1 578 . 98 GLY HA2 H 4.45 0.01 2 579 . 98 GLY HA3 H 3.85 0.01 2 580 . 99 PRO CA C 62.42 0.1 1 581 . 99 PRO CB C 31.02 0.1 1 582 . 100 LYS N N 126.25 0.1 1 583 . 100 LYS H H 8.15 0.01 1 584 . 100 LYS CA C 53.28 0.1 1 585 . 100 LYS CB C 33.15 0.1 1 586 . 101 PRO CA C 60.97 0.1 1 587 . 101 PRO CB C 31.77 0.1 1 588 . 102 ALA N N 120.40 0.1 1 589 . 102 ALA H H 7.94 0.01 1 590 . 102 ALA CA C 51.87 0.1 1 591 . 102 ALA HA H 4.09 0.01 1 592 . 102 ALA CB C 17.00 0.1 1 593 . 102 ALA HB H 1.23 0.01 1 594 . 103 LEU N N 124.92 0.1 1 595 . 103 LEU H H 8.26 0.01 1 596 . 103 LEU CA C 51.61 0.1 1 597 . 103 LEU HA H 4.55 0.01 1 598 . 103 LEU CB C 41.99 0.1 1 599 . 103 LEU HB2 H 1.82 0.01 1 600 . 103 LEU HB3 H 1.82 0.01 1 601 . 104 PRO CA C 61.25 0.1 1 602 . 104 PRO CB C 32.10 0.1 1 603 . 105 ALA N N 121.86 0.1 1 604 . 105 ALA H H 8.44 0.01 1 605 . 105 ALA CA C 52.34 0.1 1 606 . 105 ALA HA H 4.32 0.01 1 607 . 105 ALA CB C 18.70 0.1 1 608 . 105 ALA HB H 1.47 0.01 1 609 . 106 GLY N N 104.98 0.1 1 610 . 106 GLY H H 8.19 0.01 1 611 . 106 GLY CA C 44.01 0.1 1 612 . 106 GLY HA2 H 3.81 0.01 2 613 . 106 GLY HA3 H 4.03 0.01 2 614 . 107 THR N N 112.03 0.1 1 615 . 107 THR H H 8.23 0.01 1 616 . 107 THR CA C 59.89 0.1 1 617 . 107 THR HA H 4.42 0.01 1 618 . 107 THR CB C 70.29 0.1 1 619 . 108 GLU N N 122.22 0.1 1 620 . 108 GLU H H 8.68 0.01 1 621 . 108 GLU CA C 56.38 0.1 1 622 . 108 GLU HA H 4.15 0.01 1 623 . 108 GLU CB C 29.30 0.1 1 624 . 108 GLU HB2 H 2.02 0.01 1 625 . 108 GLU HB3 H 2.02 0.01 1 626 . 109 ASP CA C 54.23 0.1 1 627 . 109 ASP CB C 40.58 0.1 1 628 . 110 THR N N 114.08 0.1 1 629 . 110 THR H H 8.05 0.01 1 630 . 110 THR CA C 61.20 0.1 1 631 . 110 THR CB C 69.18 0.1 1 632 . 111 ALA N N 126.86 0.1 1 633 . 111 ALA H H 8.41 0.01 1 634 . 111 ALA CA C 51.98 0.1 1 635 . 111 ALA HA H 4.36 0.01 1 636 . 111 ALA CB C 18.90 0.1 1 637 . 111 ALA HB H 1.40 0.01 1 638 . 112 LYS N N 120.89 0.1 1 639 . 112 LYS H H 8.32 0.01 1 640 . 112 LYS CA C 56.03 0.1 1 641 . 112 LYS HA H 4.21 0.01 1 642 . 112 LYS CB C 32.08 0.1 1 643 . 112 LYS HB2 H 1.75 0.01 1 644 . 112 LYS HB3 H 1.75 0.01 1 645 . 113 GLU N N 121.21 0.1 1 646 . 113 GLU H H 8.50 0.01 1 647 . 113 GLU CA C 56.17 0.1 1 648 . 113 GLU HA H 4.21 0.01 1 649 . 113 GLU CB C 29.43 0.1 1 650 . 113 GLU HB2 H 1.96 0.01 1 651 . 113 GLU HB3 H 1.96 0.01 1 652 . 113 GLU HG2 H 2.24 0.01 1 653 . 113 GLU HG3 H 2.24 0.01 1 654 . 114 ASP N N 120.93 0.1 1 655 . 114 ASP H H 8.22 0.01 1 656 . 114 ASP CA C 53.76 0.1 1 657 . 114 ASP HA H 4.52 0.01 1 658 . 114 ASP CB C 40.60 0.1 1 659 . 114 ASP HB2 H 2.61 0.01 1 660 . 114 ASP HB3 H 2.61 0.01 1 661 . 115 ALA N N 124.25 0.1 1 662 . 115 ALA H H 7.99 0.01 1 663 . 115 ALA CA C 51.61 0.1 1 664 . 115 ALA HA H 4.26 0.01 1 665 . 115 ALA CB C 18.79 0.1 1 666 . 115 ALA HB H 1.35 0.01 1 667 . 116 ALA N N 129.17 0.1 1 668 . 116 ALA H H 7.84 0.01 1 669 . 116 ALA CA C 53.23 0.1 1 670 . 116 ALA HA H 4.06 0.01 1 671 . 116 ALA CB C 19.29 0.1 1 672 . 116 ALA HB H 1.27 0.01 1 stop_ save_