data_26768 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; 1H, 15N and 13C backbone assignments of the catalytic domain of human NSD2 ; _BMRB_accession_number 26768 _BMRB_flat_file_name bmr26768.str _Entry_type original _Submission_date 2016-03-23 _Accession_date 2016-03-23 _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 Amin Nader . . 2 Nietlispach Daniel . . 3 Coyle Joe . . 4 Williams Glyn . . 5 Chiarparin Elisabetta . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 206 "13C chemical shifts" 629 "15N chemical shifts" 206 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2016-10-26 update BMRB 'update entry citation' 2016-04-22 original author 'original release' stop_ _Original_release_date 2016-09-08 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; NMR backbone resonance assignment and solution secondary structure determination of human NSD1 and NSD2 ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 27356987 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Amin Nader . . 2 Nietlispach Daniel . . 3 Qamar Seema . . 4 Coyle Joe . . 5 Chiarparin Elisabetta . . 6 Williams Glyn . . stop_ _Journal_abbreviation 'Biomol. NMR Assign.' _Journal_volume 10 _Journal_issue 2 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 315 _Page_last 320 _Year 2016 _Details . save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name NSD2 _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label NSD2 $NSD2 stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state ? _System_paramagnetic no _System_thiol_state . _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_NSD2 _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common NSD2 _Molecular_mass . _Mol_thiol_state 'all free' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 235 _Mol_residue_sequence ; GSHMKLQREARETQESERKP PPYKHIKVNKPYGKVQIYTA DISEIPKCNCKPTDENPCGF DSECLNRMLMFECHPQVCPA GEFCQNQCFTKRQYPETKII KTDGKGWGLVAKRDIRKGEF VNEYVGELIDEEECMARIKH AHENDITHFYMLTIDKDRII DAGPKGNYSRFMNHSCQPNC ETLKWTVNGDTRVGLFAVCD IPAGTELTFNYNLDCLGNEK TVCRCGASNCSGFLG ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 969 GLY 2 970 SER 3 971 HIS 4 972 MET 5 973 LYS 6 974 LEU 7 975 GLN 8 976 ARG 9 977 GLU 10 978 ALA 11 979 ARG 12 980 GLU 13 981 THR 14 982 GLN 15 983 GLU 16 984 SER 17 985 GLU 18 986 ARG 19 987 LYS 20 988 PRO 21 989 PRO 22 990 PRO 23 991 TYR 24 992 LYS 25 993 HIS 26 994 ILE 27 995 LYS 28 996 VAL 29 997 ASN 30 998 LYS 31 999 PRO 32 1000 TYR 33 1001 GLY 34 1002 LYS 35 1003 VAL 36 1004 GLN 37 1005 ILE 38 1006 TYR 39 1007 THR 40 1008 ALA 41 1009 ASP 42 1010 ILE 43 1011 SER 44 1012 GLU 45 1013 ILE 46 1014 PRO 47 1015 LYS 48 1016 CYS 49 1017 ASN 50 1018 CYS 51 1019 LYS 52 1020 PRO 53 1021 THR 54 1022 ASP 55 1023 GLU 56 1024 ASN 57 1025 PRO 58 1026 CYS 59 1027 GLY 60 1028 PHE 61 1029 ASP 62 1030 SER 63 1031 GLU 64 1032 CYS 65 1033 LEU 66 1034 ASN 67 1035 ARG 68 1036 MET 69 1037 LEU 70 1038 MET 71 1039 PHE 72 1040 GLU 73 1041 CYS 74 1042 HIS 75 1043 PRO 76 1044 GLN 77 1045 VAL 78 1046 CYS 79 1047 PRO 80 1048 ALA 81 1049 GLY 82 1050 GLU 83 1051 PHE 84 1052 CYS 85 1053 GLN 86 1054 ASN 87 1055 GLN 88 1056 CYS 89 1057 PHE 90 1058 THR 91 1059 LYS 92 1060 ARG 93 1061 GLN 94 1062 TYR 95 1063 PRO 96 1064 GLU 97 1065 THR 98 1066 LYS 99 1067 ILE 100 1068 ILE 101 1069 LYS 102 1070 THR 103 1071 ASP 104 1072 GLY 105 1073 LYS 106 1074 GLY 107 1075 TRP 108 1076 GLY 109 1077 LEU 110 1078 VAL 111 1079 ALA 112 1080 LYS 113 1081 ARG 114 1082 ASP 115 1083 ILE 116 1084 ARG 117 1085 LYS 118 1086 GLY 119 1087 GLU 120 1088 PHE 121 1089 VAL 122 1090 ASN 123 1091 GLU 124 1092 TYR 125 1093 VAL 126 1094 GLY 127 1095 GLU 128 1096 LEU 129 1097 ILE 130 1098 ASP 131 1099 GLU 132 1100 GLU 133 1101 GLU 134 1102 CYS 135 1103 MET 136 1104 ALA 137 1105 ARG 138 1106 ILE 139 1107 LYS 140 1108 HIS 141 1109 ALA 142 1110 HIS 143 1111 GLU 144 1112 ASN 145 1113 ASP 146 1114 ILE 147 1115 THR 148 1116 HIS 149 1117 PHE 150 1118 TYR 151 1119 MET 152 1120 LEU 153 1121 THR 154 1122 ILE 155 1123 ASP 156 1124 LYS 157 1125 ASP 158 1126 ARG 159 1127 ILE 160 1128 ILE 161 1129 ASP 162 1130 ALA 163 1131 GLY 164 1132 PRO 165 1133 LYS 166 1134 GLY 167 1135 ASN 168 1136 TYR 169 1137 SER 170 1138 ARG 171 1139 PHE 172 1140 MET 173 1141 ASN 174 1142 HIS 175 1143 SER 176 1144 CYS 177 1145 GLN 178 1146 PRO 179 1147 ASN 180 1148 CYS 181 1149 GLU 182 1150 THR 183 1151 LEU 184 1152 LYS 185 1153 TRP 186 1154 THR 187 1155 VAL 188 1156 ASN 189 1157 GLY 190 1158 ASP 191 1159 THR 192 1160 ARG 193 1161 VAL 194 1162 GLY 195 1163 LEU 196 1164 PHE 197 1165 ALA 198 1166 VAL 199 1167 CYS 200 1168 ASP 201 1169 ILE 202 1170 PRO 203 1171 ALA 204 1172 GLY 205 1173 THR 206 1174 GLU 207 1175 LEU 208 1176 THR 209 1177 PHE 210 1178 ASN 211 1179 TYR 212 1180 ASN 213 1181 LEU 214 1182 ASP 215 1183 CYS 216 1184 LEU 217 1185 GLY 218 1186 ASN 219 1187 GLU 220 1188 LYS 221 1189 THR 222 1190 VAL 223 1191 CYS 224 1192 ARG 225 1193 CYS 226 1194 GLY 227 1195 ALA 228 1196 SER 229 1197 ASN 230 1198 CYS 231 1199 SER 232 1200 GLY 233 1201 PHE 234 1202 LEU 235 1203 GLY 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 $NSD2 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 _Vector_name $NSD2 'recombinant technology' . Escherichia coli . pET23b 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 $NSD2 0.2 mM '[U-98% 13C; U-98% 15N]' 'potassium phosphate' 50 mM 'natural abundance' 'sodium chloride' 450 mM 'natural abundance' TCEP 2 mM 'natural abundance' 'S-adenosyl methionine' 2 mM 'natural abundance' 'sodium azide' 0.01 '% w/v' 'natural abundance' D2O 10 '% v/v' 'natural abundance' stop_ save_ ############################ # Computer software used # ############################ save_CCPN_Analysis _Saveframe_category software _Name CCPN_Analysis _Version . loop_ _Vendor _Address _Electronic_address CCPN . . stop_ loop_ _Task 'chemical shift assignment' stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model Avance _Field_strength 600 _Details . save_ save_spectrometer_2 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model Avance _Field_strength 500 _Details . save_ ############################# # NMR applied experiments # ############################# save_2D_1H-15N_HSQC_1 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-15N HSQC' _Sample_label $sample_1 save_ save_3D_HNCA_2 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCA' _Sample_label $sample_1 save_ save_3D_HNCO_3 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCO' _Sample_label $sample_1 save_ save_3D_HN(CO)CA_4 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HN(CO)CA' _Sample_label $sample_1 save_ save_3D_HN(CO)CA_5 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HN(CO)CA' _Sample_label $sample_1 save_ save_3D_HN(COCA)CB_6 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HN(COCA)CB' _Sample_label $sample_1 save_ save_3D_1H-15N_NOESY_7 _Saveframe_category NMR_applied_experiment _Experiment_name '3D 1H-15N NOESY' _Sample_label $sample_1 save_ ####################### # Sample conditions # ####################### save_sample_conditions_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units 'ionic strength' 450 . mM pH 7 . pH pressure 1 . atm temperature 310 . K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference_1 _Saveframe_category chemical_shift_reference _Details . loop_ _Mol_common_name _Atom_type _Atom_isotope_number _Atom_group _Chem_shift_units _Chem_shift_value _Reference_method _Reference_type _External_reference_sample_geometry _External_reference_location _External_reference_axis _Indirect_shift_ratio DSS C 13 'methyl protons' ppm 0.00 na indirect . . . 0.251449530 DSS H 1 'methyl protons' ppm 0.00 internal direct . . . 1.000000000 DSS N 15 'methyl protons' ppm 0.00 na 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_assigned_chem_shift_list_1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Experiment_label '2D 1H-15N HSQC' '3D HNCA' '3D HNCO' '3D HN(CO)CA' '3D HN(COCA)CB' '3D 1H-15N NOESY' stop_ loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $sample_conditions_1 _Chem_shift_reference_set_label $chemical_shift_reference_1 _Mol_system_component_name NSD2 _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 1 973 5 LYS C C 176.5 . 1 2 973 5 LYS CA C 56.67 . 1 3 973 5 LYS CB C 32.91 . 1 4 974 6 LEU H H 8.2 . 1 5 974 6 LEU C C 177.42 . 1 6 974 6 LEU CA C 55.4 . 1 7 974 6 LEU CB C 42.5 . 1 8 974 6 LEU N N 122.87 . 1 9 975 7 GLN H H 8.33 . 1 10 975 7 GLN C C 176.09 . 1 11 975 7 GLN CA C 56.1 . 1 12 975 7 GLN CB C 29.44 . 1 13 975 7 GLN N N 121.05 . 1 14 976 8 ARG H H 8.33 . 1 15 976 8 ARG C C 176.62 . 1 16 976 8 ARG CA C 56.52 . 1 17 976 8 ARG CB C 30.83 . 1 18 976 8 ARG N N 121.94 . 1 19 977 9 GLU H H 8.48 . 1 20 977 9 GLU C C 176.41 . 1 21 977 9 GLU CA C 56.85 . 1 22 977 9 GLU CB C 30.33 . 1 23 977 9 GLU N N 121.38 . 1 24 978 10 ALA H H 8.29 . 1 25 978 10 ALA C C 177.84 . 1 26 978 10 ALA CA C 52.81 . 1 27 978 10 ALA CB C 19.26 . 1 28 978 10 ALA N N 124.92 . 1 29 979 11 ARG H H 8.26 . 1 30 979 11 ARG C C 176.62 . 1 31 979 11 ARG CA C 56.51 . 1 32 979 11 ARG CB C 31 . 1 33 979 11 ARG N N 119.8 . 1 34 980 12 GLU H H 8.48 . 1 35 980 12 GLU C C 176.99 . 1 36 980 12 GLU CA C 57.06 . 1 37 980 12 GLU CB C 30.23 . 1 38 980 12 GLU N N 121.34 . 1 39 981 13 THR H H 8.17 . 1 40 981 13 THR C C 174.86 . 1 41 981 13 THR CA C 62.22 . 1 42 981 13 THR CB C 69.88 . 1 43 981 13 THR N N 114.7 . 1 44 982 14 GLN H H 8.43 . 1 45 982 14 GLN C C 176.52 . 1 46 982 14 GLN CA C 56.26 . 1 47 982 14 GLN CB C 29.5 . 1 48 982 14 GLN N N 122.15 . 1 49 983 15 GLU H H 8.51 . 1 50 983 15 GLU C C 177.11 . 1 51 983 15 GLU CA C 57.46 . 1 52 983 15 GLU CB C 30.09 . 1 53 983 15 GLU N N 121.8 . 1 54 984 16 SER H H 8.31 . 1 55 984 16 SER C C 174.87 . 1 56 984 16 SER CA C 59.03 . 1 57 984 16 SER CB C 63.86 . 1 58 984 16 SER N N 115.7 . 1 59 985 17 GLU H H 8.32 . 1 60 985 17 GLU C C 176.62 . 1 61 985 17 GLU CA C 56.78 . 1 62 985 17 GLU CB C 30.43 . 1 63 985 17 GLU N N 121.82 . 1 64 986 18 ARG H H 8.34 . 1 65 986 18 ARG C C 175.74 . 1 66 986 18 ARG CA C 56.67 . 1 67 986 18 ARG CB C 31.1 . 1 68 986 18 ARG N N 121.11 . 1 69 987 19 LYS H H 8.13 . 1 70 987 19 LYS CA C 53.77 . 1 71 987 19 LYS CB C 33.38 . 1 72 987 19 LYS N N 121.26 . 1 73 990 22 PRO C C 175.73 . 1 74 990 22 PRO CA C 63.44 . 1 75 990 22 PRO CB C 32.85 . 1 76 991 23 TYR H H 7.66 . 1 77 991 23 TYR C C 172.64 . 1 78 991 23 TYR CA C 55.82 . 1 79 991 23 TYR CB C 40.35 . 1 80 991 23 TYR N N 117.17 . 1 81 992 24 LYS H H 7.73 . 1 82 992 24 LYS C C 173.78 . 1 83 992 24 LYS CA C 55.18 . 1 84 992 24 LYS CB C 32.54 . 1 85 992 24 LYS N N 121.27 . 1 86 993 25 HIS H H 8.4 . 1 87 993 25 HIS C C 176.67 . 1 88 993 25 HIS CA C 56.1 . 1 89 993 25 HIS CB C 31.44 . 1 90 993 25 HIS N N 129.63 . 1 91 994 26 ILE H H 8.13 . 1 92 994 26 ILE C C 173.96 . 1 93 994 26 ILE CA C 59.74 . 1 94 994 26 ILE CB C 41.83 . 1 95 994 26 ILE N N 123.42 . 1 96 995 27 LYS H H 8.52 . 1 97 995 27 LYS C C 177.76 . 1 98 995 27 LYS CA C 57.09 . 1 99 995 27 LYS CB C 35.48 . 1 100 995 27 LYS N N 114.92 . 1 101 996 28 VAL H H 7.25 . 1 102 996 28 VAL C C 173.36 . 1 103 996 28 VAL CA C 58.51 . 1 104 996 28 VAL CB C 36.21 . 1 105 996 28 VAL N N 113.07 . 1 106 997 29 ASN H H 8.69 . 1 107 997 29 ASN C C 176.01 . 1 108 997 29 ASN CA C 54.24 . 1 109 997 29 ASN CB C 39.19 . 1 110 997 29 ASN N N 118.78 . 1 111 998 30 LYS H H 8.01 . 1 112 998 30 LYS CA C 51.05 . 1 113 998 30 LYS CB C 34.86 . 1 114 998 30 LYS N N 119.47 . 1 115 999 31 PRO C C 175.09 . 1 116 999 31 PRO CA C 63.8 . 1 117 999 31 PRO CB C 32.32 . 1 118 1000 32 TYR H H 8.95 . 1 119 1000 32 TYR C C 176.04 . 1 120 1000 32 TYR CA C 57.52 . 1 121 1000 32 TYR CB C 42.28 . 1 122 1000 32 TYR N N 125.96 . 1 123 1001 33 GLY H H 8.13 . 1 124 1001 33 GLY C C 175.77 . 1 125 1001 33 GLY CA C 46.3 . 1 126 1001 33 GLY N N 115.98 . 1 127 1002 34 LYS H H 9.13 . 1 128 1002 34 LYS C C 176.7 . 1 129 1002 34 LYS CA C 56.51 . 1 130 1002 34 LYS CB C 32.31 . 1 131 1002 34 LYS N N 125.43 . 1 132 1003 35 VAL H H 7.39 . 1 133 1003 35 VAL C C 174.4 . 1 134 1003 35 VAL CA C 63.75 . 1 135 1003 35 VAL CB C 32.44 . 1 136 1003 35 VAL N N 120.94 . 1 137 1004 36 GLN H H 8.29 . 1 138 1004 36 GLN C C 174.79 . 1 139 1004 36 GLN CA C 54.51 . 1 140 1004 36 GLN CB C 32.05 . 1 141 1004 36 GLN N N 123.53 . 1 142 1005 37 ILE H H 8.02 . 1 143 1005 37 ILE C C 175.63 . 1 144 1005 37 ILE CA C 60.32 . 1 145 1005 37 ILE CB C 40.22 . 1 146 1005 37 ILE N N 119.17 . 1 147 1006 38 TYR H H 8.75 . 1 148 1006 38 TYR C C 174.57 . 1 149 1006 38 TYR CA C 57.78 . 1 150 1006 38 TYR CB C 39.77 . 1 151 1006 38 TYR N N 127.9 . 1 152 1007 39 THR H H 7.95 . 1 153 1007 39 THR C C 173.41 . 1 154 1007 39 THR CA C 60.65 . 1 155 1007 39 THR CB C 70.82 . 1 156 1007 39 THR N N 115.58 . 1 157 1008 40 ALA H H 7.61 . 1 158 1008 40 ALA C C 177.5 . 1 159 1008 40 ALA CA C 51.34 . 1 160 1008 40 ALA CB C 20.2 . 1 161 1008 40 ALA N N 125.71 . 1 162 1009 41 ASP H H 8.46 . 1 163 1009 41 ASP C C 177.71 . 1 164 1009 41 ASP CA C 54.08 . 1 165 1009 41 ASP CB C 43.41 . 1 166 1009 41 ASP N N 121.17 . 1 167 1010 42 ILE H H 8.27 . 1 168 1010 42 ILE C C 177.14 . 1 169 1010 42 ILE CA C 64.15 . 1 170 1010 42 ILE CB C 37.72 . 1 171 1010 42 ILE N N 122.71 . 1 172 1011 43 SER H H 8.23 . 1 173 1011 43 SER C C 175.38 . 1 174 1011 43 SER CA C 60.54 . 1 175 1011 43 SER CB C 63.25 . 1 176 1011 43 SER N N 114.43 . 1 177 1012 44 GLU H H 8.01 . 1 178 1012 44 GLU C C 176.57 . 1 179 1012 44 GLU CA C 55.79 . 1 180 1012 44 GLU CB C 30.95 . 1 181 1012 44 GLU N N 119.75 . 1 182 1013 45 ILE H H 7.28 . 1 183 1013 45 ILE CA C 58.8 . 1 184 1013 45 ILE CB C 38.62 . 1 185 1013 45 ILE N N 124.14 . 1 186 1014 46 PRO C C 175.01 . 1 187 1014 46 PRO CA C 63.38 . 1 188 1014 46 PRO CB C 31.81 . 1 189 1015 47 LYS H H 8.22 . 1 190 1015 47 LYS C C 176.45 . 1 191 1015 47 LYS CA C 54.66 . 1 192 1015 47 LYS CB C 35.86 . 1 193 1015 47 LYS N N 121.99 . 1 194 1016 48 CYS H H 8.7 . 1 195 1016 48 CYS C C 172.31 . 1 196 1016 48 CYS CA C 57.69 . 1 197 1016 48 CYS CB C 31.2 . 1 198 1016 48 CYS N N 125.58 . 1 199 1017 49 ASN H H 8.48 . 1 200 1017 49 ASN C C 176.27 . 1 201 1017 49 ASN CA C 52.04 . 1 202 1017 49 ASN CB C 40.19 . 1 203 1017 49 ASN N N 112.8 . 1 204 1018 50 CYS H H 9.42 . 1 205 1018 50 CYS C C 173.82 . 1 206 1018 50 CYS CA C 62.33 . 1 207 1018 50 CYS CB C 31.09 . 1 208 1018 50 CYS N N 125.92 . 1 209 1019 51 LYS H H 8.12 . 1 210 1019 51 LYS CA C 52.87 . 1 211 1019 51 LYS CB C 34.29 . 1 212 1019 51 LYS N N 117.28 . 1 213 1020 52 PRO C C 175.5 . 1 214 1020 52 PRO CA C 64.66 . 1 215 1020 52 PRO CB C 32.36 . 1 216 1021 53 THR H H 6.54 . 1 217 1021 53 THR C C 175.4 . 1 218 1021 53 THR CA C 60.53 . 1 219 1021 53 THR CB C 68.94 . 1 220 1021 53 THR N N 126.58 . 1 221 1022 54 ASP H H 7.35 . 1 222 1022 54 ASP C C 175.34 . 1 223 1022 54 ASP CA C 54.86 . 1 224 1022 54 ASP CB C 40.82 . 1 225 1022 54 ASP N N 123.26 . 1 226 1023 55 GLU H H 8.63 . 1 227 1023 55 GLU C C 177.09 . 1 228 1023 55 GLU CA C 59.11 . 1 229 1023 55 GLU CB C 30 . 1 230 1023 55 GLU N N 120.01 . 1 231 1024 56 ASN H H 8.56 . 1 232 1024 56 ASN CA C 51.92 . 1 233 1024 56 ASN CB C 39.52 . 1 234 1024 56 ASN N N 116.44 . 1 235 1025 57 PRO C C 177.15 . 1 236 1025 57 PRO CA C 63.99 . 1 237 1025 57 PRO CB C 31.56 . 1 238 1026 58 CYS H H 8.44 . 1 239 1026 58 CYS C C 176.4 . 1 240 1026 58 CYS CA C 58.36 . 1 241 1026 58 CYS CB C 32.18 . 1 242 1026 58 CYS N N 118.68 . 1 243 1027 59 GLY H H 8.5 . 1 244 1027 59 GLY C C 176.52 . 1 245 1027 59 GLY CA C 45.07 . 1 246 1027 59 GLY N N 104.75 . 1 247 1028 60 PHE H H 8.81 . 1 248 1028 60 PHE C C 176.09 . 1 249 1028 60 PHE CA C 61.15 . 1 250 1028 60 PHE CB C 39.07 . 1 251 1028 60 PHE N N 120.36 . 1 252 1029 61 ASP H H 8.57 . 1 253 1029 61 ASP C C 175.69 . 1 254 1029 61 ASP CA C 53.73 . 1 255 1029 61 ASP CB C 40.14 . 1 256 1029 61 ASP N N 118.52 . 1 257 1030 62 SER H H 7.63 . 1 258 1030 62 SER C C 174.7 . 1 259 1030 62 SER CA C 58.81 . 1 260 1030 62 SER CB C 66.41 . 1 261 1030 62 SER N N 115.22 . 1 262 1031 63 GLU H H 8.7 . 1 263 1031 63 GLU C C 174.92 . 1 264 1031 63 GLU CA C 55.61 . 1 265 1031 63 GLU CB C 28.46 . 1 266 1031 63 GLU N N 119.39 . 1 267 1032 64 CYS H H 7.47 . 1 268 1032 64 CYS C C 177.9 . 1 269 1032 64 CYS CA C 60.75 . 1 270 1032 64 CYS CB C 32.54 . 1 271 1032 64 CYS N N 120.2 . 1 272 1033 65 LEU H H 8.91 . 1 273 1033 65 LEU C C 178.79 . 1 274 1033 65 LEU CA C 58.14 . 1 275 1033 65 LEU CB C 43.8 . 1 276 1033 65 LEU N N 131.44 . 1 277 1034 66 ASN H H 8.45 . 1 278 1034 66 ASN C C 178.07 . 1 279 1034 66 ASN CA C 55.78 . 1 280 1034 66 ASN CB C 36.63 . 1 281 1034 66 ASN N N 119.02 . 1 282 1035 67 ARG H H 7.8 . 1 283 1035 67 ARG C C 180.04 . 1 284 1035 67 ARG CA C 60.53 . 1 285 1035 67 ARG CB C 30.51 . 1 286 1035 67 ARG N N 122.77 . 1 287 1036 68 MET H H 8.09 . 1 288 1036 68 MET C C 177.33 . 1 289 1036 68 MET CA C 58.83 . 1 290 1036 68 MET CB C 32.86 . 1 291 1036 68 MET N N 117.36 . 1 292 1037 69 LEU H H 7.2 . 1 293 1037 69 LEU C C 174.92 . 1 294 1037 69 LEU CA C 54.16 . 1 295 1037 69 LEU CB C 42.38 . 1 296 1037 69 LEU N N 117.52 . 1 297 1038 70 MET H H 7.47 . 1 298 1038 70 MET C C 174.03 . 1 299 1038 70 MET CA C 56.69 . 1 300 1038 70 MET CB C 27.79 . 1 301 1038 70 MET N N 114.06 . 1 302 1039 71 PHE H H 8.06 . 1 303 1039 71 PHE C C 175.85 . 1 304 1039 71 PHE CA C 55.67 . 1 305 1039 71 PHE CB C 40.9 . 1 306 1039 71 PHE N N 117.55 . 1 307 1040 72 GLU H H 8.04 . 1 308 1040 72 GLU C C 176.78 . 1 309 1040 72 GLU CA C 57.23 . 1 310 1040 72 GLU CB C 32.54 . 1 311 1040 72 GLU N N 123.75 . 1 312 1041 73 CYS H H 8.08 . 1 313 1041 73 CYS C C 174.3 . 1 314 1041 73 CYS CA C 61.79 . 1 315 1041 73 CYS CB C 33.9 . 1 316 1041 73 CYS N N 128.51 . 1 317 1042 74 HIS H H 8.64 . 1 318 1042 74 HIS CA C 53.56 . 1 319 1042 74 HIS CB C 34.91 . 1 320 1042 74 HIS N N 120.58 . 1 321 1043 75 PRO C C 178.71 . 1 322 1043 75 PRO CA C 64.73 . 1 323 1043 75 PRO CB C 32.18 . 1 324 1044 76 GLN H H 10.96 . 1 325 1044 76 GLN C C 175.75 . 1 326 1044 76 GLN CA C 56.83 . 1 327 1044 76 GLN CB C 29.4 . 1 328 1044 76 GLN N N 120.32 . 1 329 1045 77 VAL H H 7.93 . 1 330 1045 77 VAL C C 175.51 . 1 331 1045 77 VAL CA C 63.09 . 1 332 1045 77 VAL CB C 34.9 . 1 333 1045 77 VAL N N 118.36 . 1 334 1046 78 CYS H H 8.13 . 1 335 1046 78 CYS CA C 58.59 . 1 336 1046 78 CYS CB C 30.01 . 1 337 1046 78 CYS N N 122.32 . 1 338 1047 79 PRO C C 178.09 . 1 339 1047 79 PRO CA C 64.66 . 1 340 1047 79 PRO CB C 32.21 . 1 341 1048 80 ALA H H 9.55 . 1 342 1048 80 ALA C C 177.68 . 1 343 1048 80 ALA CA C 52.76 . 1 344 1048 80 ALA CB C 19.09 . 1 345 1048 80 ALA N N 123.82 . 1 346 1049 81 GLY H H 7.91 . 1 347 1049 81 GLY C C 176.64 . 1 348 1049 81 GLY CA C 47.21 . 1 349 1049 81 GLY N N 106.85 . 1 350 1050 82 GLU H H 9.29 . 1 351 1050 82 GLU C C 176.4 . 1 352 1050 82 GLU CA C 57.85 . 1 353 1050 82 GLU CB C 29.18 . 1 354 1050 82 GLU N N 125.33 . 1 355 1051 83 PHE H H 7.95 . 1 356 1051 83 PHE C C 174.65 . 1 357 1051 83 PHE CA C 57.95 . 1 358 1051 83 PHE CB C 39.5 . 1 359 1051 83 PHE N N 117.5 . 1 360 1052 84 CYS H H 7.15 . 1 361 1052 84 CYS C C 178.14 . 1 362 1052 84 CYS CA C 62.02 . 1 363 1052 84 CYS CB C 31.12 . 1 364 1052 84 CYS N N 121.5 . 1 365 1053 85 GLN H H 8.28 . 1 366 1053 85 GLN C C 175.22 . 1 367 1053 85 GLN CA C 55.64 . 1 368 1053 85 GLN CB C 27.94 . 1 369 1053 85 GLN N N 128.2 . 1 370 1054 86 ASN H H 10.02 . 1 371 1054 86 ASN C C 174.29 . 1 372 1054 86 ASN CA C 52.12 . 1 373 1054 86 ASN CB C 39.94 . 1 374 1054 86 ASN N N 125.97 . 1 375 1055 87 GLN H H 7.94 . 1 376 1055 87 GLN C C 175.84 . 1 377 1055 87 GLN CA C 55.09 . 1 378 1055 87 GLN CB C 29.18 . 1 379 1055 87 GLN N N 119.25 . 1 380 1056 88 CYS H H 7.91 . 1 381 1056 88 CYS C C 178.07 . 1 382 1056 88 CYS CA C 62.23 . 1 383 1056 88 CYS CB C 27.46 . 1 384 1056 88 CYS N N 116.81 . 1 385 1057 89 PHE H H 10.58 . 1 386 1057 89 PHE C C 182.08 . 1 387 1057 89 PHE CA C 60.84 . 1 388 1057 89 PHE CB C 38.05 . 1 389 1057 89 PHE N N 118.68 . 1 390 1058 90 THR H H 10.18 . 1 391 1058 90 THR C C 176.46 . 1 392 1058 90 THR CA C 67.23 . 1 393 1058 90 THR CB C 68.63 . 1 394 1058 90 THR N N 120.47 . 1 395 1059 91 LYS H H 8.03 . 1 396 1059 91 LYS C C 175.74 . 1 397 1059 91 LYS CA C 58.05 . 1 398 1059 91 LYS CB C 32.81 . 1 399 1059 91 LYS N N 117.06 . 1 400 1060 92 ARG H H 7.36 . 1 401 1060 92 ARG C C 174.97 . 1 402 1060 92 ARG CA C 57.03 . 1 403 1060 92 ARG CB C 27.3 . 1 404 1060 92 ARG N N 115.1 . 1 405 1061 93 GLN H H 7.8 . 1 406 1061 93 GLN C C 174.61 . 1 407 1061 93 GLN CA C 54.72 . 1 408 1061 93 GLN CB C 27.92 . 1 409 1061 93 GLN N N 118.86 . 1 410 1062 94 TYR H H 7.44 . 1 411 1062 94 TYR CA C 51.93 . 1 412 1062 94 TYR CB C 38 . 1 413 1062 94 TYR N N 123.5 . 1 414 1063 95 PRO C C 175.52 . 1 415 1063 95 PRO CA C 62.73 . 1 416 1063 95 PRO CB C 31.77 . 1 417 1064 96 GLU H H 8.75 . 1 418 1064 96 GLU C C 176.61 . 1 419 1064 96 GLU CA C 58.23 . 1 420 1064 96 GLU CB C 30.47 . 1 421 1064 96 GLU N N 123.17 . 1 422 1065 97 THR H H 8.06 . 1 423 1065 97 THR C C 173.65 . 1 424 1065 97 THR CA C 59.65 . 1 425 1065 97 THR CB C 73.92 . 1 426 1065 97 THR N N 112.79 . 1 427 1066 98 LYS H H 8.72 . 1 428 1066 98 LYS C C 173.77 . 1 429 1066 98 LYS CA C 55.04 . 1 430 1066 98 LYS CB C 36.63 . 1 431 1066 98 LYS N N 117.88 . 1 432 1067 99 ILE H H 8.16 . 1 433 1067 99 ILE C C 176.77 . 1 434 1067 99 ILE CA C 61.11 . 1 435 1067 99 ILE CB C 38.98 . 1 436 1067 99 ILE N N 124.25 . 1 437 1068 100 ILE H H 8.62 . 1 438 1068 100 ILE C C 174.62 . 1 439 1068 100 ILE CA C 58.96 . 1 440 1068 100 ILE CB C 42.75 . 1 441 1068 100 ILE N N 120 . 1 442 1069 101 LYS H H 8.57 . 1 443 1069 101 LYS C C 176.2 . 1 444 1069 101 LYS CA C 56.48 . 1 445 1069 101 LYS CB C 32.48 . 1 446 1069 101 LYS N N 123.81 . 1 447 1070 102 THR H H 7.95 . 1 448 1070 102 THR CA C 59.25 . 1 449 1070 102 THR CB C 70.82 . 1 450 1070 102 THR N N 116.09 . 1 451 1072 104 GLY C C 174.35 . 1 452 1072 104 GLY CA C 45.76 . 1 453 1073 105 LYS H H 7.08 . 1 454 1073 105 LYS C C 175.28 . 1 455 1073 105 LYS CA C 54.94 . 1 456 1073 105 LYS CB C 32 . 1 457 1073 105 LYS N N 115.16 . 1 458 1074 106 GLY H H 8.04 . 1 459 1074 106 GLY C C 174.1 . 1 460 1074 106 GLY CA C 45.14 . 1 461 1074 106 GLY N N 108.01 . 1 462 1075 107 TRP H H 9.8 . 1 463 1075 107 TRP C C 176.85 . 1 464 1075 107 TRP CA C 57.84 . 1 465 1075 107 TRP CB C 30.9 . 1 466 1075 107 TRP N N 130.34 . 1 467 1076 108 GLY H H 9.66 . 1 468 1076 108 GLY C C 171.42 . 1 469 1076 108 GLY CA C 45.09 . 1 470 1076 108 GLY N N 111.23 . 1 471 1077 109 LEU H H 8.68 . 1 472 1077 109 LEU CA C 53.57 . 1 473 1077 109 LEU N N 122.22 . 1 474 1083 115 ILE C C 175.47 . 1 475 1083 115 ILE CA C 60.14 . 1 476 1083 115 ILE CB C 41.51 . 1 477 1084 116 ARG H H 9.58 . 1 478 1084 116 ARG C C 175.41 . 1 479 1084 116 ARG CA C 54.98 . 1 480 1084 116 ARG CB C 32.16 . 1 481 1084 116 ARG N N 129.91 . 1 482 1085 117 LYS H H 8.64 . 1 483 1085 117 LYS C C 176.42 . 1 484 1085 117 LYS CA C 59.37 . 1 485 1085 117 LYS CB C 32.92 . 1 486 1085 117 LYS N N 121.05 . 1 487 1086 118 GLY H H 8.34 . 1 488 1086 118 GLY C C 174.22 . 1 489 1086 118 GLY CA C 44.88 . 1 490 1086 118 GLY N N 114.81 . 1 491 1087 119 GLU H H 8.17 . 1 492 1087 119 GLU C C 176 . 1 493 1087 119 GLU CA C 58.75 . 1 494 1087 119 GLU CB C 31.39 . 1 495 1087 119 GLU N N 118.76 . 1 496 1088 120 PHE H H 7.68 . 1 497 1088 120 PHE C C 174.22 . 1 498 1088 120 PHE CA C 57.73 . 1 499 1088 120 PHE CB C 39.88 . 1 500 1088 120 PHE N N 121.43 . 1 501 1089 121 VAL H H 8.66 . 1 502 1089 121 VAL C C 174.43 . 1 503 1089 121 VAL CA C 62.98 . 1 504 1089 121 VAL CB C 33.33 . 1 505 1089 121 VAL N N 126.11 . 1 506 1090 122 ASN H H 6.67 . 1 507 1090 122 ASN C C 171.48 . 1 508 1090 122 ASN CA C 52.13 . 1 509 1090 122 ASN CB C 42.93 . 1 510 1090 122 ASN N N 113.71 . 1 511 1091 123 GLU H H 7.73 . 1 512 1091 123 GLU C C 174.34 . 1 513 1091 123 GLU CA C 53.88 . 1 514 1091 123 GLU CB C 33.13 . 1 515 1091 123 GLU N N 118.73 . 1 516 1092 124 TYR H H 8.68 . 1 517 1092 124 TYR C C 173.48 . 1 518 1092 124 TYR CA C 58.18 . 1 519 1092 124 TYR CB C 38.55 . 1 520 1092 124 TYR N N 130.12 . 1 521 1093 125 VAL H H 5.9 . 1 522 1093 125 VAL C C 175.28 . 1 523 1093 125 VAL CA C 58.34 . 1 524 1093 125 VAL CB C 35.02 . 1 525 1093 125 VAL N N 123.26 . 1 526 1094 126 GLY H H 8.34 . 1 527 1094 126 GLY C C 172.64 . 1 528 1094 126 GLY CA C 46.78 . 1 529 1094 126 GLY N N 107.25 . 1 530 1095 127 GLU H H 8.25 . 1 531 1095 127 GLU C C 175.33 . 1 532 1095 127 GLU CA C 56.01 . 1 533 1095 127 GLU CB C 31.96 . 1 534 1095 127 GLU N N 120.77 . 1 535 1096 128 LEU H H 8.48 . 1 536 1096 128 LEU C C 174.61 . 1 537 1096 128 LEU CA C 54.19 . 1 538 1096 128 LEU CB C 44.79 . 1 539 1096 128 LEU N N 127.93 . 1 540 1097 129 ILE H H 9.53 . 1 541 1097 129 ILE C C 174.18 . 1 542 1097 129 ILE CA C 59.03 . 1 543 1097 129 ILE CB C 42.22 . 1 544 1097 129 ILE N N 117.74 . 1 545 1098 130 ASP H H 8.23 . 1 546 1098 130 ASP C C 176.61 . 1 547 1098 130 ASP CA C 51.06 . 1 548 1098 130 ASP CB C 41.73 . 1 549 1098 130 ASP N N 118.61 . 1 550 1099 131 GLU H H 8.56 . 1 551 1099 131 GLU C C 178.45 . 1 552 1099 131 GLU CA C 60.64 . 1 553 1099 131 GLU CB C 30.09 . 1 554 1099 131 GLU N N 117.88 . 1 555 1100 132 GLU H H 8.37 . 1 556 1100 132 GLU C C 179.54 . 1 557 1100 132 GLU CA C 60 . 1 558 1100 132 GLU CB C 29.69 . 1 559 1100 132 GLU N N 119.87 . 1 560 1101 133 GLU H H 8.54 . 1 561 1101 133 GLU C C 178.12 . 1 562 1101 133 GLU CA C 58.4 . 1 563 1101 133 GLU CB C 29.14 . 1 564 1101 133 GLU N N 122.55 . 1 565 1102 134 CYS H H 8.84 . 1 566 1102 134 CYS C C 176.44 . 1 567 1102 134 CYS CA C 63.41 . 1 568 1102 134 CYS CB C 26.92 . 1 569 1102 134 CYS N N 120.28 . 1 570 1103 135 MET H H 8.71 . 1 571 1103 135 MET C C 179.53 . 1 572 1103 135 MET CA C 58.31 . 1 573 1103 135 MET CB C 31.75 . 1 574 1103 135 MET N N 116.42 . 1 575 1104 136 ALA H H 7.91 . 1 576 1104 136 ALA C C 181.07 . 1 577 1104 136 ALA CA C 55.52 . 1 578 1104 136 ALA CB C 18.18 . 1 579 1104 136 ALA N N 123.02 . 1 580 1105 137 ARG H H 8.43 . 1 581 1105 137 ARG C C 180.57 . 1 582 1105 137 ARG CA C 60.17 . 1 583 1105 137 ARG CB C 30.65 . 1 584 1105 137 ARG N N 119.9 . 1 585 1106 138 ILE H H 8.79 . 1 586 1106 138 ILE C C 177.23 . 1 587 1106 138 ILE CA C 66.24 . 1 588 1106 138 ILE CB C 38.03 . 1 589 1106 138 ILE N N 122.67 . 1 590 1107 139 LYS H H 8.08 . 1 591 1107 139 LYS C C 179.11 . 1 592 1107 139 LYS CA C 60.1 . 1 593 1107 139 LYS CB C 32.59 . 1 594 1107 139 LYS N N 120.33 . 1 595 1108 140 HIS H H 8.14 . 1 596 1108 140 HIS C C 178.11 . 1 597 1108 140 HIS CA C 59.81 . 1 598 1108 140 HIS CB C 30.34 . 1 599 1108 140 HIS N N 117.26 . 1 600 1109 141 ALA H H 8.29 . 1 601 1109 141 ALA C C 180.66 . 1 602 1109 141 ALA CA C 55.62 . 1 603 1109 141 ALA CB C 18.86 . 1 604 1109 141 ALA N N 122.67 . 1 605 1110 142 HIS H H 8.58 . 1 606 1110 142 HIS C C 179.42 . 1 607 1110 142 HIS CA C 58.37 . 1 608 1110 142 HIS CB C 29.9 . 1 609 1110 142 HIS N N 116.63 . 1 610 1111 143 GLU H H 8.22 . 1 611 1111 143 GLU C C 177.09 . 1 612 1111 143 GLU CA C 58.39 . 1 613 1111 143 GLU CB C 29.9 . 1 614 1111 143 GLU N N 118.64 . 1 615 1112 144 ASN H H 7.55 . 1 616 1112 144 ASN C C 173.07 . 1 617 1112 144 ASN CA C 53.58 . 1 618 1112 144 ASN CB C 39.93 . 1 619 1112 144 ASN N N 115.73 . 1 620 1113 145 ASP H H 7.9 . 1 621 1113 145 ASP C C 174.75 . 1 622 1113 145 ASP CA C 55.89 . 1 623 1113 145 ASP CB C 39.47 . 1 624 1113 145 ASP N N 116.47 . 1 625 1114 146 ILE H H 8.1 . 1 626 1114 146 ILE C C 176.75 . 1 627 1114 146 ILE CA C 61.1 . 1 628 1114 146 ILE CB C 37.56 . 1 629 1114 146 ILE N N 119.96 . 1 630 1115 147 THR H H 8.18 . 1 631 1115 147 THR C C 173.77 . 1 632 1115 147 THR CA C 62.53 . 1 633 1115 147 THR CB C 69.76 . 1 634 1115 147 THR N N 116.39 . 1 635 1116 148 HIS H H 7.06 . 1 636 1116 148 HIS C C 173.01 . 1 637 1116 148 HIS CA C 55.15 . 1 638 1116 148 HIS CB C 33.59 . 1 639 1116 148 HIS N N 118.99 . 1 640 1117 149 PHE H H 7.58 . 1 641 1117 149 PHE C C 175.44 . 1 642 1117 149 PHE CA C 57.88 . 1 643 1117 149 PHE CB C 43.88 . 1 644 1117 149 PHE N N 118.82 . 1 645 1118 150 TYR H H 9.42 . 1 646 1118 150 TYR C C 178.28 . 1 647 1118 150 TYR CA C 56.75 . 1 648 1118 150 TYR CB C 40.28 . 1 649 1118 150 TYR N N 117.41 . 1 650 1119 151 MET H H 8.17 . 1 651 1119 151 MET C C 175.81 . 1 652 1119 151 MET CA C 55.54 . 1 653 1119 151 MET CB C 35.09 . 1 654 1119 151 MET N N 124.65 . 1 655 1120 152 LEU H H 9.56 . 1 656 1120 152 LEU C C 175.53 . 1 657 1120 152 LEU CA C 55.69 . 1 658 1120 152 LEU CB C 46.74 . 1 659 1120 152 LEU N N 128.61 . 1 660 1121 153 THR H H 9.05 . 1 661 1121 153 THR C C 174.19 . 1 662 1121 153 THR CA C 64.72 . 1 663 1121 153 THR CB C 69.85 . 1 664 1121 153 THR N N 123.15 . 1 665 1122 154 ILE H H 8.69 . 1 666 1122 154 ILE C C 175.02 . 1 667 1122 154 ILE CA C 64.03 . 1 668 1122 154 ILE CB C 39.14 . 1 669 1122 154 ILE N N 123.14 . 1 670 1123 155 ASP H H 8.49 . 1 671 1123 155 ASP C C 175.41 . 1 672 1123 155 ASP CA C 52.76 . 1 673 1123 155 ASP CB C 41.84 . 1 674 1123 155 ASP N N 118.77 . 1 675 1124 156 LYS H H 8.42 . 1 676 1124 156 LYS C C 176.37 . 1 677 1124 156 LYS CA C 58.49 . 1 678 1124 156 LYS CB C 31.95 . 1 679 1124 156 LYS N N 116.69 . 1 680 1125 157 ASP H H 8.66 . 1 681 1125 157 ASP C C 175.7 . 1 682 1125 157 ASP CA C 54.86 . 1 683 1125 157 ASP CB C 42.87 . 1 684 1125 157 ASP N N 116.26 . 1 685 1126 158 ARG H H 7.84 . 1 686 1126 158 ARG C C 173.19 . 1 687 1126 158 ARG CA C 56.43 . 1 688 1126 158 ARG CB C 34 . 1 689 1126 158 ARG N N 117.84 . 1 690 1127 159 ILE H H 9.53 . 1 691 1127 159 ILE C C 173.81 . 1 692 1127 159 ILE CA C 60.95 . 1 693 1127 159 ILE CB C 43.18 . 1 694 1127 159 ILE N N 126.63 . 1 695 1128 160 ILE H H 9.33 . 1 696 1128 160 ILE C C 175.13 . 1 697 1128 160 ILE CA C 61.43 . 1 698 1128 160 ILE CB C 39.55 . 1 699 1128 160 ILE N N 125.67 . 1 700 1129 161 ASP H H 9.77 . 1 701 1129 161 ASP C C 176.5 . 1 702 1129 161 ASP CA C 52.77 . 1 703 1129 161 ASP CB C 42.41 . 1 704 1129 161 ASP N N 126.28 . 1 705 1130 162 ALA H H 8.17 . 1 706 1130 162 ALA C C 176.55 . 1 707 1130 162 ALA CA C 51.11 . 1 708 1130 162 ALA CB C 18.73 . 1 709 1130 162 ALA N N 127.91 . 1 710 1131 163 GLY H H 8.8 . 1 711 1131 163 GLY CA C 47.53 . 1 712 1131 163 GLY N N 108.27 . 1 713 1132 164 PRO C C 177.88 . 1 714 1132 164 PRO CA C 63.9 . 1 715 1132 164 PRO CB C 32.95 . 1 716 1133 165 LYS H H 6.67 . 1 717 1133 165 LYS C C 172.8 . 1 718 1133 165 LYS CA C 53.48 . 1 719 1133 165 LYS CB C 36.12 . 1 720 1133 165 LYS N N 113.83 . 1 721 1134 166 GLY H H 8.24 . 1 722 1134 166 GLY C C 171.15 . 1 723 1134 166 GLY CA C 45.9 . 1 724 1134 166 GLY N N 104.09 . 1 725 1135 167 ASN H H 8.66 . 1 726 1135 167 ASN C C 176.41 . 1 727 1135 167 ASN CA C 50.88 . 1 728 1135 167 ASN CB C 38.35 . 1 729 1135 167 ASN N N 121.91 . 1 730 1136 168 TYR H H 7.98 . 1 731 1136 168 TYR C C 178.07 . 1 732 1136 168 TYR CA C 61.46 . 1 733 1136 168 TYR CB C 36.7 . 1 734 1136 168 TYR N N 112.04 . 1 735 1137 169 SER H H 8.29 . 1 736 1137 169 SER C C 175.93 . 1 737 1137 169 SER CA C 62.23 . 1 738 1137 169 SER N N 112.99 . 1 739 1138 170 ARG H H 7.09 . 1 740 1138 170 ARG C C 174.86 . 1 741 1138 170 ARG CA C 57.62 . 1 742 1138 170 ARG CB C 30.02 . 1 743 1138 170 ARG N N 121.48 . 1 744 1139 171 PHE H H 7.75 . 1 745 1139 171 PHE C C 174.3 . 1 746 1139 171 PHE CA C 59.84 . 1 747 1139 171 PHE CB C 39.55 . 1 748 1139 171 PHE N N 114.9 . 1 749 1140 172 MET H H 7.68 . 1 750 1140 172 MET C C 178.01 . 1 751 1140 172 MET CA C 57.74 . 1 752 1140 172 MET CB C 33.62 . 1 753 1140 172 MET N N 114.5 . 1 754 1141 173 ASN H H 9.61 . 1 755 1141 173 ASN C C 172.18 . 1 756 1141 173 ASN CA C 53.5 . 1 757 1141 173 ASN CB C 39.59 . 1 758 1141 173 ASN N N 126.27 . 1 759 1142 174 HIS H H 9.68 . 1 760 1142 174 HIS C C 180.34 . 1 761 1142 174 HIS CA C 56.44 . 1 762 1142 174 HIS CB C 30.77 . 1 763 1142 174 HIS N N 119.26 . 1 764 1143 175 SER H H 6.68 . 1 765 1143 175 SER C C 171.6 . 1 766 1143 175 SER CA C 56.05 . 1 767 1143 175 SER CB C 65.22 . 1 768 1143 175 SER N N 119.02 . 1 769 1144 176 CYS H H 8.9 . 1 770 1144 176 CYS C C 176.09 . 1 771 1144 176 CYS CA C 62.31 . 1 772 1144 176 CYS CB C 29.25 . 1 773 1144 176 CYS N N 127.52 . 1 774 1145 177 GLN H H 8.45 . 1 775 1145 177 GLN CA C 53.2 . 1 776 1145 177 GLN CB C 29.57 . 1 777 1145 177 GLN N N 120.47 . 1 778 1147 179 ASN C C 175.85 . 1 779 1147 179 ASN CA C 52.24 . 1 780 1147 179 ASN CB C 39.14 . 1 781 1148 180 CYS H H 8.68 . 1 782 1148 180 CYS C C 173.5 . 1 783 1148 180 CYS CA C 58.11 . 1 784 1148 180 CYS CB C 32.57 . 1 785 1148 180 CYS N N 118.22 . 1 786 1149 181 GLU H H 9.51 . 1 787 1149 181 GLU C C 174.81 . 1 788 1149 181 GLU CA C 53.94 . 1 789 1149 181 GLU CB C 32.96 . 1 790 1149 181 GLU N N 117.3 . 1 791 1150 182 THR H H 8.56 . 1 792 1150 182 THR C C 175.49 . 1 793 1150 182 THR CA C 59.14 . 1 794 1150 182 THR CB C 70.11 . 1 795 1150 182 THR N N 112 . 1 796 1151 183 LEU H H 9.34 . 1 797 1151 183 LEU C C 176.53 . 1 798 1151 183 LEU CA C 54.44 . 1 799 1151 183 LEU CB C 46.94 . 1 800 1151 183 LEU N N 122.23 . 1 801 1152 184 LYS H H 8.76 . 1 802 1152 184 LYS C C 175.63 . 1 803 1152 184 LYS CA C 56.56 . 1 804 1152 184 LYS CB C 32.13 . 1 805 1152 184 LYS N N 123.74 . 1 806 1153 185 TRP H H 9 . 1 807 1153 185 TRP CA C 56.37 . 1 808 1153 185 TRP N N 126.78 . 1 809 1154 186 THR C C 174.7 . 1 810 1154 186 THR CA C 62.68 . 1 811 1154 186 THR CB C 68.31 . 1 812 1155 187 VAL H H 9.37 . 1 813 1155 187 VAL C C 175.29 . 1 814 1155 187 VAL CA C 61.11 . 1 815 1155 187 VAL CB C 34.24 . 1 816 1155 187 VAL N N 129.14 . 1 817 1156 188 ASN H H 9.9 . 1 818 1156 188 ASN C C 176.12 . 1 819 1156 188 ASN CA C 54.45 . 1 820 1156 188 ASN CB C 38.04 . 1 821 1156 188 ASN N N 128.76 . 1 822 1157 189 GLY H H 9.14 . 1 823 1157 189 GLY C C 172.49 . 1 824 1157 189 GLY CA C 45.86 . 1 825 1157 189 GLY N N 103.00 . 1 826 1158 190 ASP H H 7.81 . 1 827 1158 190 ASP C C 174.98 . 1 828 1158 190 ASP CA C 52 . 1 829 1158 190 ASP CB C 45.01 . 1 830 1158 190 ASP N N 118.93 . 1 831 1159 191 THR H H 9.03 . 1 832 1159 191 THR C C 173.58 . 1 833 1159 191 THR CA C 63.15 . 1 834 1159 191 THR CB C 69.65 . 1 835 1159 191 THR N N 119.49 . 1 836 1160 192 ARG H H 9.04 . 1 837 1160 192 ARG C C 174.92 . 1 838 1160 192 ARG CA C 53.38 . 1 839 1160 192 ARG CB C 35.24 . 1 840 1160 192 ARG N N 124.01 . 1 841 1161 193 VAL H H 9.43 . 1 842 1161 193 VAL C C 175.69 . 1 843 1161 193 VAL CA C 62.67 . 1 844 1161 193 VAL CB C 32.37 . 1 845 1161 193 VAL N N 121.3 . 1 846 1162 194 GLY H H 9.58 . 1 847 1162 194 GLY C C 170.96 . 1 848 1162 194 GLY CA C 44.64 . 1 849 1162 194 GLY N N 114.17 . 1 850 1163 195 LEU H H 8.34 . 1 851 1163 195 LEU C C 175.33 . 1 852 1163 195 LEU CA C 52.56 . 1 853 1163 195 LEU CB C 42.99 . 1 854 1163 195 LEU N N 122.34 . 1 855 1164 196 PHE H H 9.14 . 1 856 1164 196 PHE C C 175.64 . 1 857 1164 196 PHE CA C 55.63 . 1 858 1164 196 PHE CB C 43.44 . 1 859 1164 196 PHE N N 120.17 . 1 860 1165 197 ALA H H 8.74 . 1 861 1165 197 ALA C C 181.26 . 1 862 1165 197 ALA CA C 52.95 . 1 863 1165 197 ALA CB C 19.56 . 1 864 1165 197 ALA N N 125.28 . 1 865 1166 198 VAL H H 9.6 . 1 866 1166 198 VAL C C 174.4 . 1 867 1166 198 VAL CA C 61.58 . 1 868 1166 198 VAL CB C 31.82 . 1 869 1166 198 VAL N N 120.2 . 1 870 1167 199 CYS H H 8.04 . 1 871 1167 199 CYS C C 171.07 . 1 872 1167 199 CYS CA C 54.4 . 1 873 1167 199 CYS CB C 31.08 . 1 874 1167 199 CYS N N 115.73 . 1 875 1168 200 ASP H H 8.39 . 1 876 1168 200 ASP C C 177.12 . 1 877 1168 200 ASP CA C 55.14 . 1 878 1168 200 ASP CB C 40.48 . 1 879 1168 200 ASP N N 118.3 . 1 880 1169 201 ILE H H 9.29 . 1 881 1169 201 ILE CA C 58.99 . 1 882 1169 201 ILE CB C 41.64 . 1 883 1169 201 ILE N N 124.12 . 1 884 1170 202 PRO C C 177.65 . 1 885 1170 202 PRO CA C 62.31 . 1 886 1170 202 PRO CB C 32.24 . 1 887 1171 203 ALA H H 9.28 . 1 888 1171 203 ALA C C 178.22 . 1 889 1171 203 ALA CA C 53.83 . 1 890 1171 203 ALA CB C 18.15 . 1 891 1171 203 ALA N N 126.55 . 1 892 1172 204 GLY H H 8.5 . 1 893 1172 204 GLY C C 173.62 . 1 894 1172 204 GLY CA C 45.37 . 1 895 1172 204 GLY N N 109.95 . 1 896 1173 205 THR H H 7.93 . 1 897 1173 205 THR C C 173.99 . 1 898 1173 205 THR CA C 62.97 . 1 899 1173 205 THR CB C 69.3 . 1 900 1173 205 THR N N 118.99 . 1 901 1174 206 GLU H H 8.86 . 1 902 1174 206 GLU C C 176.19 . 1 903 1174 206 GLU CA C 57.73 . 1 904 1174 206 GLU CB C 29.25 . 1 905 1174 206 GLU N N 127.25 . 1 906 1175 207 LEU H H 9.29 . 1 907 1175 207 LEU C C 175.98 . 1 908 1175 207 LEU CA C 54.29 . 1 909 1175 207 LEU CB C 43.27 . 1 910 1175 207 LEU N N 130.69 . 1 911 1176 208 THR H H 9.41 . 1 912 1176 208 THR C C 173.09 . 1 913 1176 208 THR CA C 58.97 . 1 914 1176 208 THR CB C 73.59 . 1 915 1176 208 THR N N 115.89 . 1 916 1177 209 PHE H H 8.35 . 1 917 1177 209 PHE C C 172.49 . 1 918 1177 209 PHE CA C 55.71 . 1 919 1177 209 PHE CB C 42.56 . 1 920 1177 209 PHE N N 113.37 . 1 921 1178 210 ASN H H 9.06 . 1 922 1178 210 ASN C C 177.06 . 1 923 1178 210 ASN CA C 52.1 . 1 924 1178 210 ASN CB C 39.03 . 1 925 1178 210 ASN N N 118.79 . 1 926 1179 211 TYR H H 12.34 . 1 927 1179 211 TYR C C 177.89 . 1 928 1179 211 TYR CA C 57.53 . 1 929 1179 211 TYR CB C 36.86 . 1 930 1179 211 TYR N N 132.19 . 1 931 1180 212 ASN H H 8.87 . 1 932 1180 212 ASN C C 175.94 . 1 933 1180 212 ASN CA C 55.73 . 1 934 1180 212 ASN CB C 38.8 . 1 935 1180 212 ASN N N 115.79 . 1 936 1181 213 LEU H H 8.01 . 1 937 1181 213 LEU C C 178.11 . 1 938 1181 213 LEU CA C 56.7 . 1 939 1181 213 LEU CB C 41.61 . 1 940 1181 213 LEU N N 118.51 . 1 941 1182 214 ASP H H 8.43 . 1 942 1182 214 ASP C C 176.46 . 1 943 1182 214 ASP CA C 55.8 . 1 944 1182 214 ASP CB C 43.74 . 1 945 1182 214 ASP N N 116.89 . 1 946 1183 215 CYS H H 8.43 . 1 947 1183 215 CYS C C 176.46 . 1 948 1183 215 CYS CA C 55.8 . 1 949 1183 215 CYS CB C 43.74 . 1 950 1183 215 CYS N N 116.89 . 1 951 1184 216 LEU H H 7.15 . 1 952 1184 216 LEU C C 176.52 . 1 953 1184 216 LEU CA C 54.87 . 1 954 1184 216 LEU CB C 44.57 . 1 955 1184 216 LEU N N 121.4 . 1 956 1185 217 GLY H H 8.29 . 1 957 1185 217 GLY C C 174.31 . 1 958 1185 217 GLY CA C 45 . 1 959 1185 217 GLY N N 106.2 . 1 960 1186 218 ASN H H 7.74 . 1 961 1186 218 ASN C C 175.69 . 1 962 1186 218 ASN CA C 53.61 . 1 963 1186 218 ASN CB C 39.85 . 1 964 1186 218 ASN N N 114.88 . 1 965 1187 219 GLU H H 8.99 . 1 966 1187 219 GLU C C 176.85 . 1 967 1187 219 GLU CA C 59.46 . 1 968 1187 219 GLU CB C 29.01 . 1 969 1187 219 GLU N N 120.57 . 1 970 1188 220 LYS H H 8.41 . 1 971 1188 220 LYS C C 176.32 . 1 972 1188 220 LYS CA C 56.23 . 1 973 1188 220 LYS CB C 31.4 . 1 974 1188 220 LYS N N 117.26 . 1 975 1189 221 THR H H 7.9 . 1 976 1189 221 THR C C 173.58 . 1 977 1189 221 THR CA C 63.24 . 1 978 1189 221 THR CB C 69.69 . 1 979 1189 221 THR N N 118.61 . 1 980 1190 222 VAL H H 8.43 . 1 981 1190 222 VAL C C 175.13 . 1 982 1190 222 VAL CA C 63.28 . 1 983 1190 222 VAL CB C 32.51 . 1 984 1190 222 VAL N N 128.12 . 1 985 1191 223 CYS H H 7.39 . 1 986 1191 223 CYS C C 176.57 . 1 987 1191 223 CYS CA C 59.8 . 1 988 1191 223 CYS CB C 31.3 . 1 989 1191 223 CYS N N 127.6 . 1 990 1192 224 ARG H H 10.48 . 1 991 1192 224 ARG C C 177.68 . 1 992 1192 224 ARG CA C 53.67 . 1 993 1192 224 ARG CB C 29.06 . 1 994 1192 224 ARG N N 130.18 . 1 995 1193 225 CYS H H 10.07 . 1 996 1193 225 CYS C C 177.55 . 1 997 1193 225 CYS CA C 62.12 . 1 998 1193 225 CYS CB C 30.2 . 1 999 1193 225 CYS N N 124.92 . 1 1000 1194 226 GLY H H 9.28 . 1 1001 1194 226 GLY C C 173.94 . 1 1002 1194 226 GLY CA C 46.11 . 1 1003 1194 226 GLY N N 112.92 . 1 1004 1195 227 ALA H H 9.29 . 1 1005 1195 227 ALA CA C 52.69 . 1 1006 1195 227 ALA CB C 21.19 . 1 1007 1195 227 ALA N N 126.84 . 1 1008 1196 228 SER C C 174.72 . 1 1009 1196 228 SER CA C 61.12 . 1 1010 1197 229 ASN H H 8.16 . 1 1011 1197 229 ASN C C 174.29 . 1 1012 1197 229 ASN CA C 51.94 . 1 1013 1197 229 ASN CB C 37.54 . 1 1014 1197 229 ASN N N 117.43 . 1 1015 1198 230 CYS H H 7.06 . 1 1016 1198 230 CYS C C 177.77 . 1 1017 1198 230 CYS CA C 58.91 . 1 1018 1198 230 CYS CB C 29.57 . 1 1019 1198 230 CYS N N 121.25 . 1 1020 1199 231 SER H H 9.79 . 1 1021 1199 231 SER C C 175.79 . 1 1022 1199 231 SER CA C 60.08 . 1 1023 1199 231 SER CB C 64.27 . 1 1024 1199 231 SER N N 129.83 . 1 1025 1200 232 GLY H H 9.88 . 1 1026 1200 232 GLY C C 174.1 . 1 1027 1200 232 GLY CA C 44.9 . 1 1028 1200 232 GLY N N 115.82 . 1 1029 1201 233 PHE H H 7.84 . 1 1030 1201 233 PHE C C 173.83 . 1 1031 1201 233 PHE CA C 56.7 . 1 1032 1201 233 PHE CB C 43.32 . 1 1033 1201 233 PHE N N 119.24 . 1 1034 1202 234 LEU H H 8.41 . 1 1035 1202 234 LEU C C 175.47 . 1 1036 1202 234 LEU CA C 55.09 . 1 1037 1202 234 LEU CB C 40.98 . 1 1038 1202 234 LEU N N 121.43 . 1 1039 1203 235 GLY H H 7.32 . 1 1040 1203 235 GLY CA C 46.42 . 1 1041 1203 235 GLY N N 113.96 . 1 stop_ save_