data_19836 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; NMR structure of E. coli Trigger Factor in complex with unfolded PhoA1-150 ; _BMRB_accession_number 19836 _BMRB_flat_file_name bmr19836.str _Entry_type original _Submission_date 2014-03-05 _Accession_date 2014-03-05 _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 Saio Tomohide . . 2 Guan Xiao . . 3 Rossi Paolo . . 4 Economou Anastassios . . 5 Kalodimos Charalampos G. . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 2 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 1154 "13C chemical shifts" 565 "15N chemical shifts" 479 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2014-05-20 original author . stop_ loop_ _Related_BMRB_accession_number _Relationship 19835 'E. coli Trigger Factor in complex with unfolded PhoA220-310' 19837 'E. coli Trigger Factor in complex with unfolded PhoA365-471' stop_ _Original_release_date 2014-05-20 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title 'Structural basis for protein antiaggregation activity of the trigger factor chaperone' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 24812405 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Saio Tomohide . . 2 Guan Xiao . . 3 Rossi Paolo . . 4 Economou Anastassios . . 5 Kalodimos Charalampos G. . stop_ _Journal_abbreviation Science _Journal_volume 344 _Journal_issue 6184 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 1250494 _Page_last 1250494 _Year 2014 _Details . save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name 'E. coli Trigger Factor in complex with unfolded PhoA1-150' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label entity_1 $entity_1 entity_2 $entity_2 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_entity_1 _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common entity_1 _Molecular_mass 16862.254 _Mol_thiol_state 'not present' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 151 _Mol_residue_sequence ; HMKQSTIALALLPLLFTPVT KARTPEMPVLENRAAQGDIT APGGARRLTGDQTAALRDSL SDKPAKNIILLIGDGMGDSE ITAARNYAEGAGGFFKGIDA LPLTGQYTHYALNKKTGKPD YVTDSAASATAWSTGVKTYN GALGVDIHEKD ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 1000 HIS 2 1001 MET 3 1002 LYS 4 1003 GLN 5 1004 SER 6 1005 THR 7 1006 ILE 8 1007 ALA 9 1008 LEU 10 1009 ALA 11 1010 LEU 12 1011 LEU 13 1012 PRO 14 1013 LEU 15 1014 LEU 16 1015 PHE 17 1016 THR 18 1017 PRO 19 1018 VAL 20 1019 THR 21 1020 LYS 22 1021 ALA 23 1022 ARG 24 1023 THR 25 1024 PRO 26 1025 GLU 27 1026 MET 28 1027 PRO 29 1028 VAL 30 1029 LEU 31 1030 GLU 32 1031 ASN 33 1032 ARG 34 1033 ALA 35 1034 ALA 36 1035 GLN 37 1036 GLY 38 1037 ASP 39 1038 ILE 40 1039 THR 41 1040 ALA 42 1041 PRO 43 1042 GLY 44 1043 GLY 45 1044 ALA 46 1045 ARG 47 1046 ARG 48 1047 LEU 49 1048 THR 50 1049 GLY 51 1050 ASP 52 1051 GLN 53 1052 THR 54 1053 ALA 55 1054 ALA 56 1055 LEU 57 1056 ARG 58 1057 ASP 59 1058 SER 60 1059 LEU 61 1060 SER 62 1061 ASP 63 1062 LYS 64 1063 PRO 65 1064 ALA 66 1065 LYS 67 1066 ASN 68 1067 ILE 69 1068 ILE 70 1069 LEU 71 1070 LEU 72 1071 ILE 73 1072 GLY 74 1073 ASP 75 1074 GLY 76 1075 MET 77 1076 GLY 78 1077 ASP 79 1078 SER 80 1079 GLU 81 1080 ILE 82 1081 THR 83 1082 ALA 84 1083 ALA 85 1084 ARG 86 1085 ASN 87 1086 TYR 88 1087 ALA 89 1088 GLU 90 1089 GLY 91 1090 ALA 92 1091 GLY 93 1092 GLY 94 1093 PHE 95 1094 PHE 96 1095 LYS 97 1096 GLY 98 1097 ILE 99 1098 ASP 100 1099 ALA 101 1100 LEU 102 1101 PRO 103 1102 LEU 104 1103 THR 105 1104 GLY 106 1105 GLN 107 1106 TYR 108 1107 THR 109 1108 HIS 110 1109 TYR 111 1110 ALA 112 1111 LEU 113 1112 ASN 114 1113 LYS 115 1114 LYS 116 1115 THR 117 1116 GLY 118 1117 LYS 119 1118 PRO 120 1119 ASP 121 1120 TYR 122 1121 VAL 123 1122 THR 124 1123 ASP 125 1124 SER 126 1125 ALA 127 1126 ALA 128 1127 SER 129 1128 ALA 130 1129 THR 131 1130 ALA 132 1131 TRP 133 1132 SER 134 1133 THR 135 1134 GLY 136 1135 VAL 137 1136 LYS 138 1137 THR 139 1138 TYR 140 1139 ASN 141 1140 GLY 142 1141 ALA 143 1142 LEU 144 1143 GLY 145 1144 VAL 146 1145 ASP 147 1146 ILE 148 1147 HIS 149 1148 GLU 150 1149 LYS 151 1150 ASP stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-08-05 loop_ _Database_name _Database_accession_code _Database_entry_mol_name _Sequence_query_to_submitted_percentage _Sequence_subject_length _Sequence_identity _Sequence_positive _Sequence_homology_expectation_value PDB 1AJA "Three-Dimensional Structure Of The D153g Mutant Of E. Coli Alkaline Phosphatase: A Mutant With Weaker Magnesium Binding And Inc" 84.77 449 100.00 100.00 3.76e-83 PDB 1AJB "Three-Dimensional Structure Of The D153g Mutant Of E. Coli Alkaline Phosphatase: A Mutant With Weaker Magnesium Binding And Inc" 84.77 449 100.00 100.00 3.76e-83 PDB 1AJC "Three-Dimensional Structure Of The D153g Mutant Of E. Coli Alkaline Phosphatase: A Mutant With Weaker Magnesium Binding And Inc" 84.77 449 100.00 100.00 3.76e-83 PDB 1AJD "Three-Dimensional Structure Of The D153g Mutant Of E. Coli Alkaline Phosphatase: A Mutant With Weaker Magnesium Binding And Inc" 84.77 449 100.00 100.00 3.76e-83 PDB 1ALH "Kinetics And Crystal Structure Of A Mutant E. Coli Alkaline Phosphatase (Asp-369-->asn): A Mechanism Involving One Zinc Per Act" 82.78 446 100.00 100.00 1.28e-80 PDB 1ALI "Alkaline Phosphatase Mutant (H412n)" 84.77 449 100.00 100.00 3.52e-83 PDB 1ALJ "Alkaline Phosphatase Mutant (H412n)" 84.77 449 100.00 100.00 3.52e-83 PDB 1ALK "Reaction Mechanism Of Alkaline Phosphatase Based On Crystal Structures. Two Metal Ion Catalysis" 84.77 449 98.44 100.00 6.95e-82 PDB 1ANI "Alkaline Phosphatase (D153h, K328h)" 82.78 446 100.00 100.00 1.50e-80 PDB 1ANJ "Alkaline Phosphatase (K328h)" 82.78 446 100.00 100.00 1.62e-80 PDB 1B8J "Alkaline Phosphatase Complexed With Vanadate" 84.77 449 99.22 99.22 2.10e-82 PDB 1ED8 "Structure Of E. Coli Alkaline Phosphatase Inhibited By The Inorganic Phosphate At 1.75a Resolution" 84.77 449 100.00 100.00 4.10e-83 PDB 1ED9 "Structure Of E. Coli Alkaline Phosphatase Without The Inorganic Phosphate At 1.75a Resolution" 84.77 449 100.00 100.00 4.10e-83 PDB 1ELX "E. Coli Alkaline Phosphatase Mutant (S102a)" 84.77 449 99.22 100.00 1.20e-82 PDB 1ELY "E. Coli Alkaline Phosphatase Mutant (S102c)" 84.77 449 99.22 99.22 1.37e-82 PDB 1ELZ "E. Coli Alkaline Phosphatase Mutant (S102g)" 84.77 449 99.22 99.22 2.42e-82 PDB 1EW8 "Alkaline Phosphatase (e.c. 3.1.3.1) Complex With Phosphonoacetic Acid" 84.77 449 100.00 100.00 4.10e-83 PDB 1EW9 "Alkaline Phosphatase (E.C. 3.1.3.1) Complex With Mercaptomethyl Phosphonate" 84.77 449 100.00 100.00 4.10e-83 PDB 1HJK "Alkaline Phosphatase Mutant H331q" 84.77 449 99.22 99.22 1.68e-82 PDB 1HQA "Alkaline Phosphatase (H412q)" 84.77 449 100.00 100.00 3.45e-83 PDB 1KH4 "E. Coli Alkaline Phosphatase Mutant (d330n) In Complex With Phosphate" 84.77 449 98.44 100.00 5.08e-82 PDB 1KH5 "E. Coli Alkaline Phosphatase Mutant (d330n) Mimic Of The Transition States With Aluminium Fluoride" 84.77 449 98.44 100.00 5.08e-82 PDB 1KH7 "E. Coli Alkaline Phosphatase Mutant (d153gd330n)" 84.77 449 98.44 100.00 6.30e-82 PDB 1KH9 "E. Coli Alkaline Phosphatase Mutant (d153gd330n) Complex With Phosphate" 84.77 449 98.44 100.00 5.08e-82 PDB 1KHJ "E. Coli Alkaline Phosphatase Mutant (d153hd330n) Mimic Of The Transition States With Aluminium Fluoride" 84.77 449 98.44 100.00 5.48e-82 PDB 1KHK "E. Coli Alkaline Phosphatase Mutant (d153hd330n)" 84.77 449 98.44 100.00 5.48e-82 PDB 1KHL "E. Coli Alkaline Phosphatase Mutant (d153hd330n) Complex With Phosphate" 84.77 449 98.44 100.00 5.48e-82 PDB 1KHN "E. Coli Alkaline Phosphatase Mutant (d153hd330n) Zinc Form" 84.77 449 98.44 100.00 5.48e-82 PDB 1URA "Alkaline Phosphatase (D51zn)" 82.78 446 99.20 100.00 5.94e-80 PDB 1URB "Alkaline Phosphatase (N51mg)" 82.78 446 99.20 100.00 5.94e-80 PDB 1Y6V "Structure Of E. Coli Alkaline Phosphatase In Presence Of Cobalt At 1.60 A Resolution" 84.77 449 100.00 100.00 4.10e-83 PDB 1Y7A "Structure Of D153hK328W E. COLI ALKALINE PHOSPHATASE IN Presence Of Cobalt At 1.77 A Resolution" 84.77 449 100.00 100.00 6.30e-83 PDB 2ANH "Alkaline Phosphatase (D153h)" 82.78 446 100.00 100.00 1.33e-80 PDB 2G9Y "Structure Of S102t E. Coli Alkaline Phosphatase In Presence Of Phosphate At 2.00 A Resolution" 84.77 449 99.22 100.00 1.25e-82 PDB 2GA3 "Structure Of S102t E. Coli Alkaline Phosphatase-Phosphate Intermediate At 2.20a Resolution" 84.77 449 99.22 99.22 2.10e-82 PDB 2MLY "Nmr Structure Of E. Coli Trigger Factor In Complex With Unfolded Phoa1-150" 100.00 151 100.00 100.00 1.11e-103 PDB 3BDF "Crystal Structure Of Metal-Free E. Coli Alkaline Phosphatase (T155v)" 85.43 458 100.00 100.00 7.03e-84 PDB 3BDG "Crystal Structure Of Wild-TypeT155V MIXED DIMER OF E. COLI ALKALINE Phosphatase" 85.43 458 100.00 100.00 4.33e-84 PDB 3BDH "Crystal Structure Of Zinc-Deficient Wild-Type E. Coli Alkaline Phosphatase" 85.43 458 100.00 100.00 6.74e-84 PDB 3CMR "E. Coli Alkaline Phosphatase Mutant R166s In Complex With Phosphate" 84.77 449 100.00 100.00 3.76e-83 PDB 3DPC "Structure Of E.coli Alkaline Phosphatase Mutant In Complex With A Phosphorylated Peptide" 84.77 455 99.22 99.22 5.96e-82 PDB 3DYC "Structure Of E322y Alkaline Phosphatase In Complex With Inorganic Phosphate" 84.77 449 100.00 100.00 5.36e-83 PDB 3TG0 "E. Coli Alkaline Phosphatase With Bound Inorganic Phosphate" 84.77 449 100.00 100.00 4.10e-83 PDB 4KM4 "E. Coli Alkaline Phosphatase Mutant S102g/r166s In Complex With Inorganic Phosphate" 82.78 445 99.20 99.20 8.81e-80 PDB 4YR1 "Crystal Structure Of E. Coli Alkaline Phosphatase D101a/d153a In Complex With Inorganic Phosphate" 79.47 443 99.17 99.17 2.81e-75 DBJ BAB33856 "alkaline phosphatase [Escherichia coli O157:H7 str. Sakai]" 99.34 494 98.67 99.33 1.50e-97 DBJ BAE76164 "alkaline phosphatase [Escherichia coli str. K12 substr. W3110]" 99.34 471 100.00 100.00 1.44e-99 DBJ BAG75928 "alkaline phosphatase [Escherichia coli SE11]" 99.34 494 99.33 100.00 2.36e-98 DBJ BAI23756 "bacterial alkaline phosphatase PhoA [Escherichia coli O26:H11 str. 11368]" 99.34 471 98.67 98.67 3.73e-97 DBJ BAI29227 "bacterial alkaline phosphatase PhoA [Escherichia coli O103:H2 str. 12009]" 99.34 471 98.67 98.67 1.71e-97 EMBL CAA28257 "alkaline phosphatase [Escherichia coli]" 99.34 471 100.00 100.00 1.44e-99 EMBL CAP74918 "alkaline phosphatase [Escherichia coli LF82]" 99.34 471 100.00 100.00 1.79e-99 EMBL CAQ30851 "alkaline phosphatase [Escherichia coli BL21(DE3)]" 99.34 471 99.33 99.33 1.14e-98 EMBL CAQ97255 "bacterial alkaline phosphatase [Escherichia coli IAI1]" 99.34 471 100.00 100.00 1.83e-99 EMBL CAR01727 "bacterial alkaline phosphatase [Escherichia coli S88]" 99.34 471 100.00 100.00 1.79e-99 GB AAA24359 "alkaline phosphatase precursor, partial [Escherichia coli]" 50.99 80 100.00 100.00 8.46e-45 GB AAA24363 "alkaline phosphatase precursor (EC 3.1.3.1) [Escherichia coli]" 99.34 471 99.33 99.33 1.13e-98 GB AAA24364 "alkaline phosphatase precursor (EC 3.1.3.1) [Escherichia coli]" 99.34 471 100.00 100.00 1.44e-99 GB AAA24365 "alkaline phosphatase precursor (EC 3.1.3.1) [Escherichia coli]" 99.34 471 100.00 100.00 1.44e-99 GB AAA24366 "alkaline phosphatase precursor (EC 3.1.3.1) [Escherichia coli]" 99.34 471 100.00 100.00 2.35e-99 REF NP_308460 "alkaline phosphatase [Escherichia coli O157:H7 str. Sakai]" 99.34 494 98.67 99.33 1.50e-97 REF NP_414917 "bacterial alkaline phosphatase [Escherichia coli str. K-12 substr. MG1655]" 99.34 471 100.00 100.00 1.44e-99 REF NP_706185 "alkaline phosphatase [Shigella flexneri 2a str. 301]" 99.34 494 98.67 99.33 3.15e-97 REF WP_000089619 "alkaline phosphatase [Escherichia coli]" 99.34 494 98.67 99.33 1.50e-97 REF WP_000089625 "alkaline phosphatase [Shigella flexneri]" 99.34 494 98.67 99.33 3.15e-97 SP P00634 "RecName: Full=Alkaline phosphatase; Short=APase; Flags: Precursor" 99.34 471 100.00 100.00 1.44e-99 stop_ save_ save_entity_2 _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common entity_2 _Molecular_mass 48256.020 _Mol_thiol_state 'not present' _Details . _Residue_count 443 _Mol_residue_sequence ; MNHKVHHHHHHMQVSVETTQ GLGRRVTITIAADSIETAVK SELVNVAKKVRIDGFRKGKV PMNIVAQRYGASVRQDVLGD LMSRNFIDAIIKEKINPAGA PTYVPGEYKLGEDFTYSVEF EVYPEVELQGLEAIEVEKPI VEVTDADVDGMLDTLRKQQA TWKEKDGAVEAEDRVTIDFT GSVDGEEFEGGKASDFVLAM GQGRMIPGFEDGIKGHKAGE EFTIDVTFPEEYHAENLKGK AAKFAINLKKVEERELPELT AEFIKRFGVEDGSVEGLRAE VRKNMERELKSAIRNRVKSQ AIEGLVKANDIDVPAALIDS EIDVLRRQAAQRFGGNEKQA LELPRELFEEQAKRRVVVGL LLGEVIRTNELKADEERVKG LIEEMASAYEDPKEVIEFYS KNKELMDNMRNVALEEQAVE AVLAKAKVTEKETTFNELMN QQA ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 -10 MET 2 -9 ASN 3 -8 HIS 4 -7 LYS 5 -6 VAL 6 -5 HIS 7 -4 HIS 8 -3 HIS 9 -2 HIS 10 -1 HIS 11 0 HIS 12 1 MET 13 2 GLN 14 3 VAL 15 4 SER 16 5 VAL 17 6 GLU 18 7 THR 19 8 THR 20 9 GLN 21 10 GLY 22 11 LEU 23 12 GLY 24 13 ARG 25 14 ARG 26 15 VAL 27 16 THR 28 17 ILE 29 18 THR 30 19 ILE 31 20 ALA 32 21 ALA 33 22 ASP 34 23 SER 35 24 ILE 36 25 GLU 37 26 THR 38 27 ALA 39 28 VAL 40 29 LYS 41 30 SER 42 31 GLU 43 32 LEU 44 33 VAL 45 34 ASN 46 35 VAL 47 36 ALA 48 37 LYS 49 38 LYS 50 39 VAL 51 40 ARG 52 41 ILE 53 42 ASP 54 43 GLY 55 44 PHE 56 45 ARG 57 46 LYS 58 47 GLY 59 48 LYS 60 49 VAL 61 50 PRO 62 51 MET 63 52 ASN 64 53 ILE 65 54 VAL 66 55 ALA 67 56 GLN 68 57 ARG 69 58 TYR 70 59 GLY 71 60 ALA 72 61 SER 73 62 VAL 74 63 ARG 75 64 GLN 76 65 ASP 77 66 VAL 78 67 LEU 79 68 GLY 80 69 ASP 81 70 LEU 82 71 MET 83 72 SER 84 73 ARG 85 74 ASN 86 75 PHE 87 76 ILE 88 77 ASP 89 78 ALA 90 79 ILE 91 80 ILE 92 81 LYS 93 82 GLU 94 83 LYS 95 84 ILE 96 85 ASN 97 86 PRO 98 87 ALA 99 88 GLY 100 89 ALA 101 90 PRO 102 91 THR 103 92 TYR 104 93 VAL 105 94 PRO 106 95 GLY 107 96 GLU 108 97 TYR 109 98 LYS 110 99 LEU 111 100 GLY 112 101 GLU 113 102 ASP 114 103 PHE 115 104 THR 116 105 TYR 117 106 SER 118 107 VAL 119 108 GLU 120 109 PHE 121 110 GLU 122 111 VAL 123 112 TYR 124 113 PRO 125 114 GLU 126 115 VAL 127 116 GLU 128 117 LEU 129 118 GLN 130 119 GLY 131 120 LEU 132 121 GLU 133 122 ALA 134 123 ILE 135 124 GLU 136 125 VAL 137 126 GLU 138 127 LYS 139 128 PRO 140 129 ILE 141 130 VAL 142 131 GLU 143 132 VAL 144 133 THR 145 134 ASP 146 135 ALA 147 136 ASP 148 137 VAL 149 138 ASP 150 139 GLY 151 140 MET 152 141 LEU 153 142 ASP 154 143 THR 155 144 LEU 156 145 ARG 157 146 LYS 158 147 GLN 159 148 GLN 160 149 ALA 161 150 THR 162 151 TRP 163 152 LYS 164 153 GLU 165 154 LYS 166 155 ASP 167 156 GLY 168 157 ALA 169 158 VAL 170 159 GLU 171 160 ALA 172 161 GLU 173 162 ASP 174 163 ARG 175 164 VAL 176 165 THR 177 166 ILE 178 167 ASP 179 168 PHE 180 169 THR 181 170 GLY 182 171 SER 183 172 VAL 184 173 ASP 185 174 GLY 186 175 GLU 187 176 GLU 188 177 PHE 189 178 GLU 190 179 GLY 191 180 GLY 192 181 LYS 193 182 ALA 194 183 SER 195 184 ASP 196 185 PHE 197 186 VAL 198 187 LEU 199 188 ALA 200 189 MET 201 190 GLY 202 191 GLN 203 192 GLY 204 193 ARG 205 194 MET 206 195 ILE 207 196 PRO 208 197 GLY 209 198 PHE 210 199 GLU 211 200 ASP 212 201 GLY 213 202 ILE 214 203 LYS 215 204 GLY 216 205 HIS 217 206 LYS 218 207 ALA 219 208 GLY 220 209 GLU 221 210 GLU 222 211 PHE 223 212 THR 224 213 ILE 225 214 ASP 226 215 VAL 227 216 THR 228 217 PHE 229 218 PRO 230 219 GLU 231 220 GLU 232 221 TYR 233 222 HIS 234 223 ALA 235 224 GLU 236 225 ASN 237 226 LEU 238 227 LYS 239 228 GLY 240 229 LYS 241 230 ALA 242 231 ALA 243 232 LYS 244 233 PHE 245 234 ALA 246 235 ILE 247 236 ASN 248 237 LEU 249 238 LYS 250 239 LYS 251 240 VAL 252 241 GLU 253 242 GLU 254 243 ARG 255 244 GLU 256 245 LEU 257 246 PRO 258 247 GLU 259 248 LEU 260 249 THR 261 250 ALA 262 251 GLU 263 252 PHE 264 253 ILE 265 254 LYS 266 255 ARG 267 256 PHE 268 257 GLY 269 258 VAL 270 259 GLU 271 260 ASP 272 261 GLY 273 262 SER 274 263 VAL 275 264 GLU 276 265 GLY 277 266 LEU 278 267 ARG 279 268 ALA 280 269 GLU 281 270 VAL 282 271 ARG 283 272 LYS 284 273 ASN 285 274 MET 286 275 GLU 287 276 ARG 288 277 GLU 289 278 LEU 290 279 LYS 291 280 SER 292 281 ALA 293 282 ILE 294 283 ARG 295 284 ASN 296 285 ARG 297 286 VAL 298 287 LYS 299 288 SER 300 289 GLN 301 290 ALA 302 291 ILE 303 292 GLU 304 293 GLY 305 294 LEU 306 295 VAL 307 296 LYS 308 297 ALA 309 298 ASN 310 299 ASP 311 300 ILE 312 301 ASP 313 302 VAL 314 303 PRO 315 304 ALA 316 305 ALA 317 306 LEU 318 307 ILE 319 308 ASP 320 309 SER 321 310 GLU 322 311 ILE 323 312 ASP 324 313 VAL 325 314 LEU 326 315 ARG 327 316 ARG 328 317 GLN 329 318 ALA 330 319 ALA 331 320 GLN 332 321 ARG 333 322 PHE 334 323 GLY 335 324 GLY 336 325 ASN 337 326 GLU 338 327 LYS 339 328 GLN 340 329 ALA 341 330 LEU 342 331 GLU 343 332 LEU 344 333 PRO 345 334 ARG 346 335 GLU 347 336 LEU 348 337 PHE 349 338 GLU 350 339 GLU 351 340 GLN 352 341 ALA 353 342 LYS 354 343 ARG 355 344 ARG 356 345 VAL 357 346 VAL 358 347 VAL 359 348 GLY 360 349 LEU 361 350 LEU 362 351 LEU 363 352 GLY 364 353 GLU 365 354 VAL 366 355 ILE 367 356 ARG 368 357 THR 369 358 ASN 370 359 GLU 371 360 LEU 372 361 LYS 373 362 ALA 374 363 ASP 375 364 GLU 376 365 GLU 377 366 ARG 378 367 VAL 379 368 LYS 380 369 GLY 381 370 LEU 382 371 ILE 383 372 GLU 384 373 GLU 385 374 MET 386 375 ALA 387 376 SER 388 377 ALA 389 378 TYR 390 379 GLU 391 380 ASP 392 381 PRO 393 382 LYS 394 383 GLU 395 384 VAL 396 385 ILE 397 386 GLU 398 387 PHE 399 388 TYR 400 389 SER 401 390 LYS 402 391 ASN 403 392 LYS 404 393 GLU 405 394 LEU 406 395 MET 407 396 ASP 408 397 ASN 409 398 MET 410 399 ARG 411 400 ASN 412 401 VAL 413 402 ALA 414 403 LEU 415 404 GLU 416 405 GLU 417 406 GLN 418 407 ALA 419 408 VAL 420 409 GLU 421 410 ALA 422 411 VAL 423 412 LEU 424 413 ALA 425 414 LYS 426 415 ALA 427 416 LYS 428 417 VAL 429 418 THR 430 419 GLU 431 420 LYS 432 421 GLU 433 422 THR 434 423 THR 435 424 PHE 436 425 ASN 437 426 GLU 438 427 LEU 439 428 MET 440 429 ASN 441 430 GLN 442 431 GLN 443 432 ALA stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-01-29 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 BMRB 19835 entity_2 100.00 443 100.00 100.00 0.00e+00 BMRB 19837 entity_2 100.00 443 100.00 100.00 0.00e+00 PDB 1W26 "Trigger Factor In Complex With The Ribosome Forms A Molecular Cradle For Nascent Proteins" 97.29 432 97.68 97.68 0.00e+00 PDB 2MLX "Nmr Structure Of E. Coli Trigger Factor In Complex With Unfolded Phoa220-310" 100.00 443 100.00 100.00 0.00e+00 PDB 2MLY "Nmr Structure Of E. Coli Trigger Factor In Complex With Unfolded Phoa1-150" 100.00 443 100.00 100.00 0.00e+00 PDB 2MLZ "Nmr Structure Of E. Coli Trigger Factor In Complex With Unfolded Phoa365-471" 100.00 443 100.00 100.00 0.00e+00 PDB 2VRH "Structure Of The E. Coli Trigger Factor Bound To A Translating Ribosome" 97.29 432 97.68 97.68 0.00e+00 DBJ BAB33913 "trigger factor [Escherichia coli O157:H7 str. Sakai]" 97.52 432 100.00 100.00 0.00e+00 DBJ BAD98926 "trigger factor tag [Expression vector pColdTF]" 100.00 489 100.00 100.00 0.00e+00 DBJ BAE76216 "peptidyl-prolyl cis/trans isomerase [Escherichia coli str. K-12 substr. W3110]" 97.52 432 100.00 100.00 0.00e+00 DBJ BAG75986 "trigger factor [Escherichia coli SE11]" 97.52 432 99.77 100.00 0.00e+00 DBJ BAI23810 "peptidyl-prolyl cis/trans isomerase [Escherichia coli O26:H11 str. 11368]" 97.52 432 99.77 99.77 0.00e+00 EMBL CAP74970 "Trigger factor [Escherichia coli LF82]" 97.52 432 99.77 99.77 0.00e+00 EMBL CAQ30908 "trigger factor; a molecular chaperone involved in cell division [Escherichia coli BL21(DE3)]" 97.52 432 100.00 100.00 0.00e+00 EMBL CAQ97312 "peptidyl-prolyl cis/trans isomerase (trigger factor) [Escherichia coli IAI1]" 97.52 432 100.00 100.00 0.00e+00 EMBL CAR01780 "peptidyl-prolyl cis/trans isomerase (trigger factor) [Escherichia coli S88]" 96.84 429 100.00 100.00 0.00e+00 EMBL CAR06670 "peptidyl-prolyl cis/trans isomerase (trigger factor) [Escherichia coli ED1a]" 97.52 432 100.00 100.00 0.00e+00 GB AAA62791 "trigger factor [Escherichia coli]" 97.52 432 97.69 98.61 0.00e+00 GB AAB40192 "trigger factor [Escherichia coli]" 97.52 432 100.00 100.00 0.00e+00 GB AAC73539 "peptidyl-prolyl cis/trans isomerase (trigger factor) [Escherichia coli str. K-12 substr. MG1655]" 97.52 432 100.00 100.00 0.00e+00 GB AAG54786 "trigger factor; a molecular chaperone involved in cell division [Escherichia coli O157:H7 str. EDL933]" 97.52 432 100.00 100.00 0.00e+00 GB AAN42037 "trigger factor [Shigella flexneri 2a str. 301]" 97.52 432 100.00 100.00 0.00e+00 REF NP_286178 "trigger factor [Escherichia coli O157:H7 str. EDL933]" 97.52 432 100.00 100.00 0.00e+00 REF NP_308517 "trigger factor [Escherichia coli O157:H7 str. Sakai]" 97.52 432 100.00 100.00 0.00e+00 REF NP_414970 "peptidyl-prolyl cis/trans isomerase (trigger factor) [Escherichia coli str. K-12 substr. MG1655]" 97.52 432 100.00 100.00 0.00e+00 REF NP_706330 "trigger factor [Shigella flexneri 2a str. 301]" 97.52 432 100.00 100.00 0.00e+00 REF NP_752485 "trigger factor [Escherichia coli CFT073]" 97.52 432 99.77 99.77 0.00e+00 SP A1A8A5 "RecName: Full=Trigger factor; Short=TF; AltName: Full=PPIase [Escherichia coli APEC O1]" 96.84 429 100.00 100.00 0.00e+00 SP A7ZIJ4 "RecName: Full=Trigger factor; Short=TF; AltName: Full=PPIase [Escherichia coli E24377A]" 97.52 432 99.77 100.00 0.00e+00 SP A7ZX94 "RecName: Full=Trigger factor; Short=TF; AltName: Full=PPIase [Escherichia coli HS]" 97.52 432 100.00 100.00 0.00e+00 SP B1J012 "RecName: Full=Trigger factor; Short=TF; AltName: Full=PPIase [Escherichia coli ATCC 8739]" 97.52 432 100.00 100.00 0.00e+00 SP B1LJJ3 "RecName: Full=Trigger factor; Short=TF; AltName: Full=PPIase [Escherichia coli SMS-3-5]" 97.52 432 100.00 100.00 0.00e+00 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $entity_1 'E. coli' 469008 Bacteria . Escherichia coli $entity_2 'E. coli' 469008 Bacteria . Escherichia coli 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 $entity_1 'recombinant technology' . Escherichia coli BL21(DE3) pET16b $entity_2 'recombinant technology' . Escherichia coli BL21(DE3) pCold 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 $entity_1 0.5 mM '[U-100% 13C; U-100% 15N]' $entity_2 0.5 mM '[U-100% 13C; U-100% 15N]' 'potassium chloride' 100 mM 'natural abundance' BME 3 mM 'natural abundance' 'potassium phosphate' 20 mM 'natural abundance' H2O 90 % 'natural abundance' D2O 10 % 'natural abundance' stop_ save_ ############################ # Computer software used # ############################ save_NMRPipe _Saveframe_category software _Name NMRPipe _Version . loop_ _Vendor _Address _Electronic_address 'Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax' . . stop_ loop_ _Task processing stop_ _Details . save_ save_SPARKY _Saveframe_category software _Name SPARKY _Version 3.113 loop_ _Vendor _Address _Electronic_address Goddard . . stop_ loop_ _Task 'chemical shift assignment' stop_ _Details . save_ save_CNS _Saveframe_category software _Name CNS _Version . loop_ _Vendor _Address _Electronic_address 'Brunger, Adams, Clore, Gros, Nilges and Read' . . stop_ loop_ _Task refinement stop_ _Details . save_ save_OLIVIA _Saveframe_category software _Name OLIVIA _Version 1.16 loop_ _Vendor _Address _Electronic_address 'Olivia, Yokochi Masashi' . . stop_ loop_ _Task 'chemical shift assignment' stop_ _Details . save_ save_CYANA _Saveframe_category software _Name CYANA _Version 3.0 loop_ _Vendor _Address _Electronic_address 'Guntert, Mumenthaler and Wuthrich' . . stop_ loop_ _Task 'structure solution' stop_ _Details . save_ save_TOPSPIN _Saveframe_category software _Name TOPSPIN _Version 3.1 loop_ _Vendor _Address _Electronic_address 'Bruker Biospin' . . stop_ loop_ _Task collection stop_ _Details . save_ save_VNMRJ _Saveframe_category software _Name VNMRJ _Version . loop_ _Vendor _Address _Electronic_address Varian . . stop_ loop_ _Task collection stop_ _Details . save_ save_X-PLOR_NIH _Saveframe_category software _Name X-PLOR_NIH _Version . loop_ _Vendor _Address _Electronic_address 'Schwieters, Kuszewski, Tjandra and Clore' . . stop_ loop_ _Task 'structure solution' stop_ _Details . save_ save_TALOSN _Saveframe_category software _Name TALOSN _Version . loop_ _Vendor _Address _Electronic_address 'Shen and Bax' . . stop_ loop_ _Task 'geometry optimization' stop_ _Details . save_ save_PSVS _Saveframe_category software _Name PSVS _Version 1.5 loop_ _Vendor _Address _Electronic_address 'Bhattacharya and Montelione' . . stop_ loop_ _Task validation stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model Avance _Field_strength 700 _Details . save_ save_spectrometer_2 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model Avance _Field_strength 600 _Details . save_ save_spectrometer_3 _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model INOVA _Field_strength 600 _Details . save_ save_spectrometer_4 _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model INOVA _Field_strength 800 _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_2D_1H-13C_HSQC_2 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-13C HSQC' _Sample_label $sample_1 save_ save_3D_1H-13C_NOESY_3 _Saveframe_category NMR_applied_experiment _Experiment_name '3D 1H-13C NOESY' _Sample_label $sample_1 save_ save_3D_1H-15N_NOESY_4 _Saveframe_category NMR_applied_experiment _Experiment_name '3D 1H-15N NOESY' _Sample_label $sample_1 save_ save_3D_HNCACB_5 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCACB' _Sample_label $sample_1 save_ save_3D_1H-13C_HMQC-NOESY_HMQC_6 _Saveframe_category NMR_applied_experiment _Experiment_name '3D 1H-13C HMQC-NOESY_HMQC' _Sample_label $sample_1 save_ save_2D_1H-13C_HMQC_7 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-13C HMQC' _Sample_label $sample_1 save_ save_3D_HCCH-TOCSY_8 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HCCH-TOCSY' _Sample_label $sample_1 save_ save_3D_H(CCO)NH_9 _Saveframe_category NMR_applied_experiment _Experiment_name '3D H(CCO)NH' _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' 100 . mM pH 7 . pH pressure 1 . atm temperature 273 . 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' '2D 1H-13C HSQC' 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 entity_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 12 MET HE H 2.108 0.02 1 2 1 12 MET CE C 17.403 0.20 1 3 3 14 VAL H H 8.321 0.02 1 4 3 14 VAL HG1 H 0.840 0.02 2 5 3 14 VAL HG2 H 0.858 0.02 2 6 3 14 VAL CG1 C 21.584 0.20 2 7 3 14 VAL CG2 C 17.303 0.20 2 8 3 14 VAL N N 122.686 0.20 1 9 4 15 SER H H 8.689 0.02 1 10 4 15 SER N N 121.236 0.20 1 11 5 16 VAL H H 8.806 0.02 1 12 5 16 VAL HG1 H 0.765 0.02 2 13 5 16 VAL HG2 H 1.056 0.02 2 14 5 16 VAL CG1 C 20.086 0.20 2 15 5 16 VAL CG2 C 21.484 0.20 2 16 5 16 VAL N N 125.511 0.20 1 17 6 17 GLU H H 8.922 0.02 1 18 6 17 GLU N N 126.142 0.20 1 19 7 18 THR H H 8.711 0.02 1 20 7 18 THR N N 118.421 0.20 1 21 8 19 THR H H 7.708 0.02 1 22 8 19 THR N N 117.503 0.20 1 23 9 20 GLN H H 8.239 0.02 1 24 9 20 GLN N N 119.524 0.20 1 25 11 22 LEU H H 8.990 0.02 1 26 11 22 LEU HD1 H 0.733 0.02 2 27 11 22 LEU HD2 H 0.934 0.02 2 28 11 22 LEU CD1 C 22.234 0.20 2 29 11 22 LEU CD2 C 25.718 0.20 2 30 11 22 LEU N N 129.153 0.20 1 31 12 23 GLY H H 8.537 0.02 1 32 12 23 GLY N N 106.953 0.20 1 33 13 24 ARG H H 8.919 0.02 1 34 13 24 ARG N N 124.485 0.20 1 35 14 25 ARG H H 8.684 0.02 1 36 14 25 ARG N N 120.539 0.20 1 37 15 26 VAL H H 9.312 0.02 1 38 15 26 VAL HG1 H 1.158 0.02 2 39 15 26 VAL HG2 H 1.054 0.02 2 40 15 26 VAL CG1 C 22.607 0.20 2 41 15 26 VAL CG2 C 21.443 0.20 2 42 15 26 VAL N N 126.770 0.20 1 43 16 27 THR H H 8.945 0.02 1 44 16 27 THR N N 125.094 0.20 1 45 17 28 ILE H H 8.563 0.02 1 46 17 28 ILE HD1 H 0.827 0.02 1 47 17 28 ILE CD1 C 13.908 0.20 1 48 17 28 ILE N N 129.070 0.20 1 49 18 29 THR H H 8.357 0.02 1 50 18 29 THR N N 121.479 0.20 1 51 19 30 ILE H H 9.912 0.02 1 52 19 30 ILE HD1 H 0.930 0.02 1 53 19 30 ILE CD1 C 14.412 0.20 1 54 19 30 ILE N N 127.534 0.20 1 55 20 31 ALA H H 8.690 0.02 1 56 20 31 ALA HB H 1.553 0.02 1 57 20 31 ALA CB C 19.542 0.20 1 58 20 31 ALA N N 129.247 0.20 1 59 21 32 ALA H H 9.376 0.02 1 60 21 32 ALA HB H 1.334 0.02 1 61 21 32 ALA CB C 18.742 0.20 1 62 21 32 ALA N N 126.228 0.20 1 63 22 33 ASP H H 8.927 0.02 1 64 22 33 ASP N N 115.111 0.20 1 65 23 34 SER H H 7.597 0.02 1 66 23 34 SER N N 116.495 0.20 1 67 24 35 ILE H H 7.390 0.02 1 68 24 35 ILE HD1 H 0.890 0.02 1 69 24 35 ILE CD1 C 14.923 0.20 1 70 24 35 ILE N N 122.361 0.20 1 71 25 36 GLU H H 8.233 0.02 1 72 25 36 GLU N N 117.692 0.20 1 73 26 37 THR H H 8.264 0.02 1 74 26 37 THR N N 115.095 0.20 1 75 27 38 ALA H H 7.328 0.02 1 76 27 38 ALA HB H 1.523 0.02 1 77 27 38 ALA CB C 18.985 0.20 1 78 27 38 ALA N N 125.189 0.20 1 79 28 39 VAL H H 8.607 0.02 1 80 28 39 VAL HG1 H 0.907 0.02 2 81 28 39 VAL HG2 H 0.823 0.02 2 82 28 39 VAL CG1 C 23.815 0.20 2 83 28 39 VAL CG2 C 20.965 0.20 2 84 28 39 VAL N N 119.922 0.20 1 85 29 40 LYS H H 8.102 0.02 1 86 29 40 LYS N N 118.843 0.20 1 87 30 41 SER H H 7.896 0.02 1 88 30 41 SER N N 112.454 0.20 1 89 31 42 GLU H H 7.871 0.02 1 90 31 42 GLU N N 121.930 0.20 1 91 32 43 LEU H H 8.664 0.02 1 92 32 43 LEU HD1 H 0.793 0.02 2 93 32 43 LEU HD2 H 0.679 0.02 2 94 32 43 LEU CD1 C 26.207 0.20 2 95 32 43 LEU CD2 C 23.471 0.20 2 96 32 43 LEU N N 121.004 0.20 1 97 33 44 VAL H H 7.683 0.02 1 98 33 44 VAL HG1 H 1.056 0.02 2 99 33 44 VAL HG2 H 0.655 0.02 2 100 33 44 VAL CG1 C 22.846 0.20 2 101 33 44 VAL CG2 C 21.438 0.20 2 102 33 44 VAL N N 118.838 0.20 1 103 34 45 ASN H H 7.241 0.02 1 104 34 45 ASN N N 118.030 0.20 1 105 35 46 VAL H H 8.445 0.02 1 106 35 46 VAL HG1 H 0.873 0.02 2 107 35 46 VAL HG2 H 0.872 0.02 2 108 35 46 VAL CG1 C 23.633 0.20 2 109 35 46 VAL CG2 C 22.866 0.20 2 110 35 46 VAL N N 121.777 0.20 1 111 36 47 ALA H H 8.311 0.02 1 112 36 47 ALA HB H 1.491 0.02 1 113 36 47 ALA CB C 18.907 0.20 1 114 36 47 ALA N N 120.267 0.20 1 115 37 48 LYS H H 7.351 0.02 1 116 37 48 LYS N N 114.141 0.20 1 117 38 49 LYS H H 7.606 0.02 1 118 38 49 LYS N N 115.473 0.20 1 119 39 50 VAL H H 7.419 0.02 1 120 39 50 VAL HG1 H 0.903 0.02 2 121 39 50 VAL HG2 H 0.718 0.02 2 122 39 50 VAL CG1 C 20.483 0.20 2 123 39 50 VAL CG2 C 21.327 0.20 2 124 39 50 VAL N N 116.433 0.20 1 125 40 51 ARG H H 8.368 0.02 1 126 40 51 ARG N N 124.277 0.20 1 127 41 52 ILE H H 8.073 0.02 1 128 41 52 ILE HD1 H 0.796 0.02 1 129 41 52 ILE CD1 C 13.971 0.20 1 130 41 52 ILE N N 124.148 0.20 1 131 42 53 ASP H H 8.573 0.02 1 132 42 53 ASP N N 124.954 0.20 1 133 43 54 GLY H H 8.475 0.02 1 134 43 54 GLY N N 110.101 0.20 1 135 44 55 PHE H H 8.085 0.02 1 136 44 55 PHE N N 118.593 0.20 1 137 45 56 ARG H H 8.721 0.02 1 138 45 56 ARG N N 122.232 0.20 1 139 46 57 LYS H H 8.634 0.02 1 140 46 57 LYS N N 122.694 0.20 1 141 47 58 GLY H H 8.924 0.02 1 142 47 58 GLY N N 113.989 0.20 1 143 48 59 LYS H H 8.093 0.02 1 144 48 59 LYS N N 119.432 0.20 1 145 49 60 VAL H H 8.061 0.02 1 146 49 60 VAL HG1 H 0.819 0.02 2 147 49 60 VAL HG2 H 0.654 0.02 2 148 49 60 VAL CG1 C 22.264 0.20 2 149 49 60 VAL CG2 C 21.368 0.20 2 150 49 60 VAL N N 123.619 0.20 1 151 51 62 MET HE H 1.939 0.02 1 152 51 62 MET CE C 16.268 0.20 1 153 52 63 ASN H H 8.833 0.02 1 154 52 63 ASN N N 123.474 0.20 1 155 53 64 ILE H H 7.208 0.02 1 156 53 64 ILE HD1 H 0.791 0.02 1 157 53 64 ILE CD1 C 11.563 0.20 1 158 53 64 ILE N N 121.514 0.20 1 159 54 65 VAL H H 7.494 0.02 1 160 54 65 VAL HG1 H 0.894 0.02 2 161 54 65 VAL HG2 H 0.893 0.02 2 162 54 65 VAL CG1 C 21.755 0.20 2 163 54 65 VAL CG2 C 21.202 0.20 2 164 54 65 VAL N N 120.799 0.20 1 165 55 66 ALA H H 8.869 0.02 1 166 55 66 ALA HB H 1.425 0.02 1 167 55 66 ALA CB C 17.841 0.20 1 168 55 66 ALA N N 120.856 0.20 1 169 56 67 GLN H H 7.666 0.02 1 170 56 67 GLN N N 118.538 0.20 1 171 57 68 ARG H H 8.020 0.02 1 172 57 68 ARG N N 116.667 0.20 1 173 58 69 TYR H H 8.619 0.02 1 174 58 69 TYR N N 114.284 0.20 1 175 59 70 GLY H H 8.158 0.02 1 176 59 70 GLY N N 109.105 0.20 1 177 60 71 ALA H H 8.507 0.02 1 178 60 71 ALA HB H 1.418 0.02 1 179 60 71 ALA CB C 17.878 0.20 1 180 60 71 ALA N N 122.730 0.20 1 181 61 72 SER H H 8.059 0.02 1 182 61 72 SER N N 115.187 0.20 1 183 62 73 VAL H H 8.399 0.02 1 184 62 73 VAL HG1 H 1.052 0.02 2 185 62 73 VAL HG2 H 0.902 0.02 2 186 62 73 VAL CG1 C 23.761 0.20 2 187 62 73 VAL CG2 C 22.741 0.20 2 188 62 73 VAL N N 122.495 0.20 1 189 63 74 ARG H H 8.300 0.02 1 190 63 74 ARG N N 118.635 0.20 1 191 64 75 GLN H H 7.481 0.02 1 192 64 75 GLN N N 116.268 0.20 1 193 65 76 ASP H H 7.847 0.02 1 194 65 76 ASP N N 121.702 0.20 1 195 66 77 VAL H H 8.728 0.02 1 196 66 77 VAL HG1 H 0.903 0.02 2 197 66 77 VAL CG1 C 23.133 0.20 2 198 66 77 VAL N N 121.548 0.20 1 199 67 78 LEU H H 8.284 0.02 1 200 67 78 LEU HD1 H 0.027 0.02 2 201 67 78 LEU HD2 H -0.120 0.02 2 202 67 78 LEU CD1 C 24.067 0.20 2 203 67 78 LEU CD2 C 22.218 0.20 2 204 67 78 LEU N N 119.779 0.20 1 205 68 79 GLY H H 7.660 0.02 1 206 68 79 GLY N N 104.928 0.20 1 207 69 80 ASP H H 7.723 0.02 1 208 69 80 ASP N N 123.146 0.20 1 209 70 81 LEU H H 8.948 0.02 1 210 70 81 LEU HD1 H 0.681 0.02 2 211 70 81 LEU HD2 H 0.738 0.02 2 212 70 81 LEU CD1 C 26.787 0.20 2 213 70 81 LEU CD2 C 22.399 0.20 2 214 70 81 LEU N N 118.632 0.20 1 215 71 82 MET H H 8.725 0.02 1 216 71 82 MET HE H 1.803 0.02 1 217 71 82 MET CE C 16.413 0.20 1 218 71 82 MET N N 120.051 0.20 1 219 72 83 SER H H 7.451 0.02 1 220 72 83 SER N N 115.745 0.20 1 221 73 84 ARG H H 8.634 0.02 1 222 73 84 ARG N N 121.209 0.20 1 223 74 85 ASN H H 8.347 0.02 1 224 74 85 ASN N N 114.087 0.20 1 225 75 86 PHE H H 7.738 0.02 1 226 75 86 PHE N N 121.314 0.20 1 227 76 87 ILE H H 8.218 0.02 1 228 76 87 ILE N N 119.891 0.20 1 229 77 88 ASP H H 7.666 0.02 1 230 77 88 ASP N N 116.921 0.20 1 231 78 89 ALA H H 7.513 0.02 1 232 78 89 ALA HB H 1.457 0.02 1 233 78 89 ALA CB C 18.752 0.20 1 234 78 89 ALA N N 120.884 0.20 1 235 79 90 ILE H H 8.030 0.02 1 236 79 90 ILE HD1 H 0.325 0.02 1 237 79 90 ILE CD1 C 13.436 0.20 1 238 79 90 ILE N N 113.413 0.20 1 239 80 91 ILE H H 7.892 0.02 1 240 80 91 ILE HD1 H 0.777 0.02 1 241 80 91 ILE CD1 C 13.166 0.20 1 242 80 91 ILE N N 122.547 0.20 1 243 81 92 LYS H H 7.821 0.02 1 244 81 92 LYS N N 121.440 0.20 1 245 82 93 GLU H H 8.011 0.02 1 246 82 93 GLU N N 114.760 0.20 1 247 83 94 LYS H H 7.737 0.02 1 248 83 94 LYS N N 117.012 0.20 1 249 84 95 ILE H H 7.948 0.02 1 250 84 95 ILE HD1 H 0.808 0.02 1 251 84 95 ILE CD1 C 13.491 0.20 1 252 84 95 ILE N N 119.229 0.20 1 253 85 96 ASN H H 8.653 0.02 1 254 85 96 ASN N N 124.286 0.20 1 255 87 98 ALA H H 9.209 0.02 1 256 87 98 ALA HB H 0.502 0.02 1 257 87 98 ALA CB C 18.741 0.20 1 258 87 98 ALA N N 125.524 0.20 1 259 88 99 GLY H H 7.554 0.02 1 260 88 99 GLY N N 107.014 0.20 1 261 89 100 ALA H H 8.411 0.02 1 262 89 100 ALA HB H 1.367 0.02 1 263 89 100 ALA CB C 18.461 0.20 1 264 89 100 ALA N N 124.058 0.20 1 265 91 102 THR H H 8.853 0.02 1 266 91 102 THR N N 117.682 0.20 1 267 92 103 TYR H H 9.054 0.02 1 268 92 103 TYR N N 126.639 0.20 1 269 93 104 VAL H H 9.523 0.02 1 270 93 104 VAL HG1 H 0.832 0.02 2 271 93 104 VAL HG2 H 0.729 0.02 2 272 93 104 VAL CG1 C 21.971 0.20 2 273 93 104 VAL CG2 C 19.213 0.20 2 274 93 104 VAL N N 124.611 0.20 1 275 95 106 GLY H H 6.857 0.02 1 276 95 106 GLY N N 109.037 0.20 1 277 96 107 GLU H H 8.389 0.02 1 278 96 107 GLU N N 119.656 0.20 1 279 97 108 TYR H H 8.911 0.02 1 280 97 108 TYR N N 126.986 0.20 1 281 98 109 LYS H H 8.380 0.02 1 282 98 109 LYS N N 131.055 0.20 1 283 99 110 LEU H H 7.947 0.02 1 284 99 110 LEU HD1 H 0.923 0.02 2 285 99 110 LEU HD2 H 0.849 0.02 2 286 99 110 LEU CD1 C 24.344 0.20 2 287 99 110 LEU CD2 C 24.891 0.20 2 288 99 110 LEU N N 124.566 0.20 1 289 100 111 GLY H H 8.274 0.02 1 290 100 111 GLY N N 113.138 0.20 1 291 101 112 GLU H H 7.884 0.02 1 292 101 112 GLU N N 119.234 0.20 1 293 102 113 ASP H H 8.627 0.02 1 294 102 113 ASP N N 121.919 0.20 1 295 103 114 PHE H H 8.923 0.02 1 296 103 114 PHE N N 123.333 0.20 1 297 104 115 THR H H 8.414 0.02 1 298 104 115 THR N N 126.257 0.20 1 299 105 116 TYR H H 8.945 0.02 1 300 105 116 TYR N N 122.193 0.20 1 301 106 117 SER H H 8.175 0.02 1 302 106 117 SER N N 112.325 0.20 1 303 107 118 VAL H H 9.037 0.02 1 304 107 118 VAL HG1 H 0.625 0.02 2 305 107 118 VAL HG2 H -0.553 0.02 2 306 107 118 VAL CG1 C 22.513 0.20 2 307 107 118 VAL CG2 C 21.989 0.20 2 308 107 118 VAL N N 121.772 0.20 1 309 108 119 GLU H H 8.971 0.02 1 310 108 119 GLU N N 125.633 0.20 1 311 109 120 PHE H H 7.865 0.02 1 312 109 120 PHE N N 117.269 0.20 1 313 110 121 GLU H H 8.612 0.02 1 314 110 121 GLU N N 118.490 0.20 1 315 111 122 VAL H H 8.113 0.02 1 316 111 122 VAL HG1 H 0.962 0.02 2 317 111 122 VAL HG2 H 0.866 0.02 2 318 111 122 VAL CG1 C 23.529 0.20 2 319 111 122 VAL CG2 C 17.936 0.20 2 320 111 122 VAL N N 113.925 0.20 1 321 112 123 TYR H H 8.124 0.02 1 322 112 123 TYR N N 118.544 0.20 1 323 114 125 GLU H H 8.361 0.02 1 324 114 125 GLU N N 121.276 0.20 1 325 115 126 VAL H H 8.116 0.02 1 326 115 126 VAL HG1 H 0.970 0.02 2 327 115 126 VAL HG2 H 0.832 0.02 2 328 115 126 VAL CG1 C 20.570 0.20 2 329 115 126 VAL CG2 C 20.669 0.20 2 330 115 126 VAL N N 120.757 0.20 1 331 116 127 GLU H H 8.387 0.02 1 332 116 127 GLU N N 125.503 0.20 1 333 117 128 LEU H H 7.909 0.02 1 334 117 128 LEU HD1 H 0.868 0.02 2 335 117 128 LEU HD2 H 0.823 0.02 2 336 117 128 LEU CD1 C 25.251 0.20 2 337 117 128 LEU CD2 C 23.554 0.20 2 338 117 128 LEU N N 130.026 0.20 1 339 118 129 GLN H H 9.439 0.02 1 340 118 129 GLN N N 122.222 0.20 1 341 119 130 GLY H H 8.515 0.02 1 342 119 130 GLY N N 104.672 0.20 1 343 120 131 LEU H H 8.169 0.02 1 344 120 131 LEU HD1 H 0.864 0.02 2 345 120 131 LEU HD2 H 0.775 0.02 2 346 120 131 LEU CD1 C 25.112 0.20 2 347 120 131 LEU CD2 C 23.634 0.20 2 348 120 131 LEU N N 120.851 0.20 1 349 121 132 GLU H H 8.675 0.02 1 350 121 132 GLU N N 112.795 0.20 1 351 122 133 ALA H H 7.322 0.02 1 352 122 133 ALA HB H 1.336 0.02 1 353 122 133 ALA CB C 18.937 0.20 1 354 122 133 ALA N N 119.680 0.20 1 355 123 134 ILE H H 7.113 0.02 1 356 123 134 ILE HD1 H 0.823 0.02 1 357 123 134 ILE CD1 C 13.841 0.20 1 358 123 134 ILE N N 122.198 0.20 1 359 124 135 GLU H H 8.320 0.02 1 360 124 135 GLU N N 126.781 0.20 1 361 125 136 VAL H H 8.437 0.02 1 362 125 136 VAL HG1 H 0.874 0.02 2 363 125 136 VAL HG2 H 0.917 0.02 2 364 125 136 VAL CG1 C 20.936 0.20 2 365 125 136 VAL CG2 C 20.062 0.20 2 366 125 136 VAL N N 122.729 0.20 1 367 126 137 GLU H H 9.158 0.02 1 368 126 137 GLU N N 127.493 0.20 1 369 127 138 LYS H H 9.275 0.02 1 370 127 138 LYS N N 130.787 0.20 1 371 129 140 ILE H H 8.119 0.02 1 372 129 140 ILE HD1 H 0.655 0.02 1 373 129 140 ILE CD1 C 10.630 0.20 1 374 129 140 ILE N N 124.502 0.20 1 375 130 141 VAL H H 8.073 0.02 1 376 130 141 VAL HG1 H 0.800 0.02 2 377 130 141 VAL HG2 H 0.808 0.02 2 378 130 141 VAL CG1 C 20.083 0.20 2 379 130 141 VAL CG2 C 21.442 0.20 2 380 130 141 VAL N N 125.533 0.20 1 381 131 142 GLU H H 8.568 0.02 1 382 131 142 GLU N N 124.955 0.20 1 383 132 143 VAL H H 8.673 0.02 1 384 132 143 VAL HG1 H 0.887 0.02 2 385 132 143 VAL HG2 H 0.830 0.02 2 386 132 143 VAL CG1 C 24.615 0.20 2 387 132 143 VAL CG2 C 23.148 0.20 2 388 132 143 VAL N N 121.174 0.20 1 389 133 144 THR H H 9.708 0.02 1 390 133 144 THR N N 122.775 0.20 1 391 134 145 ASP H H 8.847 0.02 1 392 134 145 ASP N N 120.437 0.20 1 393 135 146 ALA H H 8.114 0.02 1 394 135 146 ALA HB H 1.381 0.02 1 395 135 146 ALA CB C 17.626 0.20 1 396 135 146 ALA N N 121.403 0.20 1 397 136 147 ASP H H 7.909 0.02 1 398 136 147 ASP N N 121.077 0.20 1 399 137 148 VAL H H 7.633 0.02 1 400 137 148 VAL HG2 H 0.758 0.02 2 401 137 148 VAL CG2 C 22.361 0.20 2 402 137 148 VAL N N 122.378 0.20 1 403 138 149 ASP H H 8.702 0.02 1 404 138 149 ASP N N 119.985 0.20 1 405 139 150 GLY H H 8.183 0.02 1 406 139 150 GLY N N 107.217 0.20 1 407 140 151 MET H H 7.783 0.02 1 408 140 151 MET N N 123.628 0.20 1 409 141 152 LEU H H 8.573 0.02 1 410 141 152 LEU HD1 H 0.848 0.02 2 411 141 152 LEU HD2 H 0.783 0.02 2 412 141 152 LEU CD1 C 25.152 0.20 2 413 141 152 LEU CD2 C 23.810 0.20 2 414 141 152 LEU N N 120.944 0.20 1 415 142 153 ASP H H 8.017 0.02 1 416 142 153 ASP N N 118.780 0.20 1 417 143 154 THR H H 7.997 0.02 1 418 143 154 THR N N 117.532 0.20 1 419 144 155 LEU H H 8.341 0.02 1 420 144 155 LEU HD1 H 1.012 0.02 2 421 144 155 LEU HD2 H 0.758 0.02 2 422 144 155 LEU CD1 C 26.385 0.20 2 423 144 155 LEU CD2 C 22.361 0.20 2 424 144 155 LEU N N 121.797 0.20 1 425 145 156 ARG H H 8.276 0.02 1 426 145 156 ARG N N 118.718 0.20 1 427 146 157 LYS H H 7.907 0.02 1 428 146 157 LYS N N 118.663 0.20 1 429 147 158 GLN H H 7.872 0.02 1 430 147 158 GLN N N 117.919 0.20 1 431 148 159 GLN H H 7.754 0.02 1 432 148 159 GLN N N 117.785 0.20 1 433 149 160 ALA H H 8.038 0.02 1 434 149 160 ALA HB H 1.404 0.02 1 435 149 160 ALA CB C 18.591 0.20 1 436 149 160 ALA N N 123.339 0.20 1 437 150 161 THR H H 8.165 0.02 1 438 150 161 THR HA H 4.479 0.02 1 439 150 161 THR HB H 4.168 0.02 1 440 150 161 THR HG2 H 1.173 0.02 1 441 150 161 THR CA C 61.484 0.20 1 442 150 161 THR CB C 70.366 0.20 1 443 150 161 THR CG2 C 21.997 0.20 1 444 150 161 THR N N 115.053 0.20 1 445 151 162 TRP H H 8.458 0.02 1 446 151 162 TRP HA H 5.075 0.02 1 447 151 162 TRP HB2 H 2.912 0.02 2 448 151 162 TRP HB3 H 2.745 0.02 2 449 151 162 TRP HD1 H 7.031 0.02 1 450 151 162 TRP HE1 H 9.889 0.02 1 451 151 162 TRP HE3 H 7.174 0.02 1 452 151 162 TRP HZ2 H 7.346 0.02 1 453 151 162 TRP HH2 H 7.162 0.02 1 454 151 162 TRP CA C 56.283 0.20 1 455 151 162 TRP CB C 32.734 0.20 1 456 151 162 TRP CD1 C 127.457 0.20 1 457 151 162 TRP CE3 C 123.715 0.20 1 458 151 162 TRP CZ2 C 113.810 0.20 1 459 151 162 TRP CH2 C 123.293 0.20 1 460 151 162 TRP N N 123.202 0.20 1 461 151 162 TRP NE1 N 129.008 0.20 1 462 152 163 LYS HD2 H 1.701 0.02 1 463 152 163 LYS HD3 H 1.701 0.02 1 464 152 163 LYS H H 9.563 0.02 1 465 152 163 LYS HA H 4.975 0.02 1 466 152 163 LYS HB2 H 1.875 0.02 2 467 152 163 LYS HG2 H 1.430 0.02 1 468 152 163 LYS HG3 H 1.430 0.02 1 469 152 163 LYS HE2 H 3.003 0.02 1 470 152 163 LYS HE3 H 3.003 0.02 1 471 152 163 LYS CA C 54.320 0.20 1 472 152 163 LYS CB C 35.909 0.20 1 473 152 163 LYS CG C 23.829 0.20 1 474 152 163 LYS CD C 29.168 0.20 1 475 152 163 LYS CE C 42.067 0.20 1 476 152 163 LYS N N 121.595 0.20 1 477 153 164 GLU H H 8.909 0.02 1 478 153 164 GLU HA H 4.447 0.02 1 479 153 164 GLU HB2 H 1.849 0.02 1 480 153 164 GLU HB3 H 1.849 0.02 1 481 153 164 GLU HG2 H 2.462 0.02 2 482 153 164 GLU HG3 H 2.275 0.02 2 483 153 164 GLU CA C 58.257 0.20 1 484 153 164 GLU CB C 30.033 0.20 1 485 153 164 GLU CG C 37.295 0.20 1 486 153 164 GLU N N 124.093 0.20 1 487 154 165 LYS H H 8.844 0.02 1 488 154 165 LYS HA H 4.799 0.02 1 489 154 165 LYS HB2 H 1.708 0.02 1 490 154 165 LYS HB3 H 1.708 0.02 1 491 154 165 LYS HG2 H 1.153 0.02 1 492 154 165 LYS HG3 H 1.153 0.02 1 493 154 165 LYS HD3 H 1.492 0.02 2 494 154 165 LYS HE2 H 2.829 0.02 2 495 154 165 LYS HE3 H 2.579 0.02 2 496 154 165 LYS CA C 54.617 0.20 1 497 154 165 LYS CB C 36.240 0.20 1 498 154 165 LYS CG C 24.242 0.20 1 499 154 165 LYS CD C 29.876 0.20 1 500 154 165 LYS CE C 42.237 0.20 1 501 154 165 LYS N N 123.832 0.20 1 502 155 166 ASP H H 8.731 0.02 1 503 155 166 ASP HA H 4.905 0.02 1 504 155 166 ASP HB2 H 2.749 0.02 2 505 155 166 ASP HB3 H 2.703 0.02 2 506 155 166 ASP CA C 53.343 0.20 1 507 155 166 ASP CB C 40.693 0.20 1 508 155 166 ASP N N 123.644 0.20 1 509 156 167 GLY H H 7.292 0.02 1 510 156 167 GLY HA2 H 4.201 0.02 2 511 156 167 GLY HA3 H 3.933 0.02 2 512 156 167 GLY CA C 44.129 0.20 1 513 156 167 GLY N N 106.422 0.20 1 514 157 168 ALA H H 8.274 0.02 1 515 157 168 ALA HA H 4.235 0.02 1 516 157 168 ALA HB H 1.129 0.02 1 517 157 168 ALA CA C 51.251 0.20 1 518 157 168 ALA CB C 20.243 0.20 1 519 157 168 ALA N N 119.237 0.20 1 520 158 169 VAL H H 8.769 0.02 1 521 158 169 VAL HA H 3.889 0.02 1 522 158 169 VAL HB H 2.127 0.02 1 523 158 169 VAL HG1 H 1.046 0.02 2 524 158 169 VAL HG2 H 1.232 0.02 2 525 158 169 VAL CA C 64.399 0.20 1 526 158 169 VAL CB C 32.756 0.20 1 527 158 169 VAL CG1 C 23.846 0.20 2 528 158 169 VAL CG2 C 25.794 0.20 2 529 158 169 VAL N N 119.220 0.20 1 530 159 170 GLU H H 9.662 0.02 1 531 159 170 GLU N N 132.175 0.20 1 532 160 171 ALA HA H 3.879 0.02 1 533 160 171 ALA HB H 1.513 0.02 1 534 160 171 ALA CA C 55.489 0.20 1 535 160 171 ALA CB C 20.021 0.20 1 536 161 172 GLU H H 8.103 0.02 1 537 161 172 GLU HA H 4.708 0.02 1 538 161 172 GLU HB2 H 1.991 0.02 1 539 161 172 GLU HB3 H 1.991 0.02 1 540 161 172 GLU HG2 H 2.217 0.02 1 541 161 172 GLU HG3 H 2.217 0.02 1 542 161 172 GLU CA C 55.165 0.20 1 543 161 172 GLU CB C 29.623 0.20 1 544 161 172 GLU CG C 37.317 0.20 1 545 161 172 GLU N N 111.801 0.20 1 546 162 173 ASP H H 7.271 0.02 1 547 162 173 ASP HA H 5.253 0.02 1 548 162 173 ASP HB2 H 3.099 0.02 2 549 162 173 ASP HB3 H 2.777 0.02 2 550 162 173 ASP CA C 55.298 0.20 1 551 162 173 ASP CB C 42.216 0.20 1 552 162 173 ASP N N 122.930 0.20 1 553 163 174 ARG HD2 H 2.368 0.02 1 554 163 174 ARG HD3 H 2.368 0.02 1 555 163 174 ARG H H 8.907 0.02 1 556 163 174 ARG HA H 5.235 0.02 1 557 163 174 ARG HB2 H 1.059 0.02 2 558 163 174 ARG HB3 H 0.206 0.02 2 559 163 174 ARG HG2 H 0.778 0.02 1 560 163 174 ARG HG3 H 0.778 0.02 1 561 163 174 ARG C C 178.083 0.20 1 562 163 174 ARG CA C 54.650 0.20 1 563 163 174 ARG CB C 34.078 0.20 1 564 163 174 ARG CG C 26.068 0.20 1 565 163 174 ARG CD C 43.724 0.20 1 566 163 174 ARG N N 118.485 0.20 1 567 164 175 VAL H H 9.032 0.02 1 568 164 175 VAL HA H 5.380 0.02 1 569 164 175 VAL HB H 2.178 0.02 1 570 164 175 VAL HG1 H 1.119 0.02 2 571 164 175 VAL HG2 H 1.141 0.02 2 572 164 175 VAL CA C 58.289 0.20 1 573 164 175 VAL CB C 34.468 0.20 1 574 164 175 VAL CG1 C 19.565 0.20 2 575 164 175 VAL CG2 C 24.236 0.20 2 576 164 175 VAL N N 119.495 0.20 1 577 165 176 THR H H 8.435 0.02 1 578 165 176 THR HA H 5.221 0.02 1 579 165 176 THR HB H 3.899 0.02 1 580 165 176 THR HG2 H 0.941 0.02 1 581 165 176 THR CA C 62.053 0.20 1 582 165 176 THR CB C 69.362 0.20 1 583 165 176 THR CG2 C 19.888 0.20 1 584 165 176 THR N N 119.046 0.20 1 585 166 177 ILE H H 9.601 0.02 1 586 166 177 ILE HA H 5.737 0.02 1 587 166 177 ILE HB H 2.105 0.02 1 588 166 177 ILE HG12 H 1.579 0.02 2 589 166 177 ILE HG13 H 1.382 0.02 2 590 166 177 ILE HG2 H 1.023 0.02 1 591 166 177 ILE HD1 H 1.028 0.02 1 592 166 177 ILE CA C 58.583 0.20 1 593 166 177 ILE CB C 42.787 0.20 1 594 166 177 ILE CG1 C 24.919 0.20 1 595 166 177 ILE CG2 C 19.199 0.20 1 596 166 177 ILE CD1 C 14.460 0.20 1 597 166 177 ILE N N 119.692 0.20 1 598 167 178 ASP H H 8.550 0.02 1 599 167 178 ASP HA H 5.390 0.02 1 600 167 178 ASP HB2 H 2.639 0.02 1 601 167 178 ASP HB3 H 2.639 0.02 1 602 167 178 ASP CA C 52.627 0.20 1 603 167 178 ASP CB C 42.619 0.20 1 604 167 178 ASP N N 119.199 0.20 1 605 168 179 PHE HD1 H 6.967 0.02 1 606 168 179 PHE HD2 H 6.967 0.02 1 607 168 179 PHE H H 8.571 0.02 1 608 168 179 PHE HA H 6.119 0.02 1 609 168 179 PHE HB2 H 3.042 0.02 2 610 168 179 PHE HB3 H 3.004 0.02 2 611 168 179 PHE HE1 H 6.396 0.02 1 612 168 179 PHE HE2 H 6.396 0.02 1 613 168 179 PHE HZ H 6.498 0.02 1 614 168 179 PHE CA C 55.889 0.20 1 615 168 179 PHE CB C 43.768 0.20 1 616 168 179 PHE CD1 C 132.462 0.20 1 617 168 179 PHE CD2 C 132.462 0.20 1 618 168 179 PHE CE1 C 130.193 0.20 1 619 168 179 PHE CE2 C 130.193 0.20 1 620 168 179 PHE CZ C 130.112 0.20 1 621 168 179 PHE N N 114.527 0.20 1 622 169 180 THR H H 8.475 0.02 1 623 169 180 THR HA H 4.861 0.02 1 624 169 180 THR HB H 4.062 0.02 1 625 169 180 THR HG2 H 1.110 0.02 1 626 169 180 THR CA C 62.316 0.20 1 627 169 180 THR CB C 71.665 0.20 1 628 169 180 THR CG2 C 21.554 0.20 1 629 169 180 THR N N 114.593 0.20 1 630 170 181 GLY H H 9.228 0.02 1 631 170 181 GLY HA2 H 4.599 0.02 2 632 170 181 GLY HA3 H 2.643 0.02 2 633 170 181 GLY CA C 45.187 0.20 1 634 170 181 GLY N N 118.780 0.20 1 635 171 182 SER H H 8.992 0.02 1 636 171 182 SER HA H 5.037 0.02 1 637 171 182 SER HB2 H 3.560 0.02 2 638 171 182 SER HB3 H 3.328 0.02 2 639 171 182 SER CA C 57.422 0.20 1 640 171 182 SER CB C 66.244 0.20 1 641 171 182 SER N N 115.748 0.20 1 642 172 183 VAL H H 8.801 0.02 1 643 172 183 VAL HA H 4.499 0.02 1 644 172 183 VAL HB H 1.920 0.02 1 645 172 183 VAL HG1 H 0.921 0.02 2 646 172 183 VAL HG2 H 0.831 0.02 2 647 172 183 VAL CA C 61.491 0.20 1 648 172 183 VAL CB C 34.844 0.20 1 649 172 183 VAL CG1 C 21.491 0.20 2 650 172 183 VAL CG2 C 21.500 0.20 2 651 172 183 VAL N N 120.254 0.20 1 652 173 184 ASP H H 9.594 0.02 1 653 173 184 ASP HA H 4.331 0.02 1 654 173 184 ASP HB2 H 3.019 0.02 2 655 173 184 ASP HB3 H 2.731 0.02 2 656 173 184 ASP CA C 55.595 0.20 1 657 173 184 ASP CB C 39.751 0.20 1 658 173 184 ASP N N 128.874 0.20 1 659 174 185 GLY H H 8.678 0.02 1 660 174 185 GLY HA2 H 4.228 0.02 2 661 174 185 GLY HA3 H 3.611 0.02 2 662 174 185 GLY CA C 45.340 0.20 1 663 174 185 GLY N N 102.670 0.20 1 664 175 186 GLU H H 7.901 0.02 1 665 175 186 GLU HA H 4.691 0.02 1 666 175 186 GLU HB2 H 2.046 0.02 1 667 175 186 GLU HB3 H 2.046 0.02 1 668 175 186 GLU HG2 H 2.319 0.02 2 669 175 186 GLU HG3 H 2.218 0.02 2 670 175 186 GLU CA C 54.732 0.20 1 671 175 186 GLU CB C 32.406 0.20 1 672 175 186 GLU CG C 35.905 0.20 1 673 175 186 GLU N N 120.423 0.20 1 674 176 187 GLU H H 8.862 0.02 1 675 176 187 GLU HA H 4.484 0.02 1 676 176 187 GLU HB2 H 2.072 0.02 1 677 176 187 GLU HB3 H 2.072 0.02 1 678 176 187 GLU HG2 H 2.295 0.02 1 679 176 187 GLU HG3 H 2.295 0.02 1 680 176 187 GLU CA C 56.814 0.20 1 681 176 187 GLU CB C 30.310 0.20 1 682 176 187 GLU CG C 36.481 0.20 1 683 176 187 GLU N N 125.894 0.20 1 684 177 188 PHE HD1 H 7.093 0.02 1 685 177 188 PHE HD2 H 7.093 0.02 1 686 177 188 PHE H H 7.070 0.02 1 687 177 188 PHE HA H 5.070 0.02 1 688 177 188 PHE HB2 H 3.120 0.02 2 689 177 188 PHE HB3 H 3.046 0.02 2 690 177 188 PHE HE1 H 6.957 0.02 1 691 177 188 PHE HE2 H 6.957 0.02 1 692 177 188 PHE HZ H 7.120 0.02 1 693 177 188 PHE CA C 54.495 0.20 1 694 177 188 PHE CB C 41.107 0.20 1 695 177 188 PHE CD1 C 133.521 0.20 1 696 177 188 PHE CD2 C 133.521 0.20 1 697 177 188 PHE CE1 C 130.228 0.20 1 698 177 188 PHE CE2 C 130.228 0.20 1 699 177 188 PHE CZ C 128.358 0.20 1 700 177 188 PHE N N 117.486 0.20 1 701 178 189 GLU H H 9.035 0.02 1 702 178 189 GLU HA H 4.184 0.02 1 703 178 189 GLU HG2 H 2.367 0.02 1 704 178 189 GLU HG3 H 2.367 0.02 1 705 178 189 GLU CA C 57.985 0.20 1 706 178 189 GLU CG C 36.199 0.20 1 707 178 189 GLU N N 124.931 0.20 1 708 179 190 GLY H H 8.969 0.02 1 709 179 190 GLY HA2 H 4.433 0.02 2 710 179 190 GLY HA3 H 3.997 0.02 2 711 179 190 GLY CA C 45.685 0.20 1 712 179 190 GLY N N 113.354 0.20 1 713 180 191 GLY H H 7.781 0.02 1 714 180 191 GLY HA2 H 4.239 0.02 2 715 180 191 GLY HA3 H 2.966 0.02 2 716 180 191 GLY CA C 46.453 0.20 1 717 180 191 GLY N N 105.848 0.20 1 718 181 192 LYS HD2 H 1.622 0.02 1 719 181 192 LYS HD3 H 1.622 0.02 1 720 181 192 LYS H H 7.559 0.02 1 721 181 192 LYS HA H 5.256 0.02 1 722 181 192 LYS HB2 H 1.740 0.02 1 723 181 192 LYS HB3 H 1.740 0.02 1 724 181 192 LYS HG2 H 1.528 0.02 2 725 181 192 LYS HG3 H 1.245 0.02 2 726 181 192 LYS HE2 H 2.896 0.02 1 727 181 192 LYS HE3 H 2.896 0.02 1 728 181 192 LYS CA C 54.490 0.20 1 729 181 192 LYS CB C 35.963 0.20 1 730 181 192 LYS CG C 24.632 0.20 1 731 181 192 LYS CD C 29.577 0.20 1 732 181 192 LYS CE C 42.209 0.20 1 733 181 192 LYS N N 119.260 0.20 1 734 182 193 ALA H H 8.137 0.02 1 735 182 193 ALA HA H 4.380 0.02 1 736 182 193 ALA HB H 0.638 0.02 1 737 182 193 ALA CA C 51.619 0.20 1 738 182 193 ALA CB C 22.903 0.20 1 739 182 193 ALA N N 125.588 0.20 1 740 183 194 SER H H 8.407 0.02 1 741 183 194 SER HA H 5.116 0.02 1 742 183 194 SER HB2 H 3.679 0.02 2 743 183 194 SER HB3 H 3.565 0.02 2 744 183 194 SER CA C 56.391 0.20 1 745 183 194 SER CB C 65.460 0.20 1 746 183 194 SER N N 115.573 0.20 1 747 184 195 ASP H H 9.598 0.02 1 748 184 195 ASP HA H 3.811 0.02 1 749 184 195 ASP HB2 H 2.639 0.02 2 750 184 195 ASP HB3 H 2.581 0.02 2 751 184 195 ASP CA C 56.137 0.20 1 752 184 195 ASP CB C 39.589 0.20 1 753 184 195 ASP N N 123.160 0.20 1 754 185 196 PHE H H 9.181 0.02 1 755 185 196 PHE HA H 4.418 0.02 1 756 185 196 PHE HB2 H 3.287 0.02 2 757 185 196 PHE HB3 H 2.673 0.02 2 758 185 196 PHE HE1 H 7.269 0.02 3 759 185 196 PHE HE2 H 7.155 0.02 3 760 185 196 PHE HZ H 7.168 0.02 1 761 185 196 PHE CA C 58.099 0.20 1 762 185 196 PHE CB C 40.260 0.20 1 763 185 196 PHE CE1 C 131.266 0.20 3 764 185 196 PHE CE2 C 131.278 0.20 3 765 185 196 PHE CZ C 129.578 0.20 1 766 185 196 PHE N N 121.498 0.20 1 767 186 197 VAL H H 7.850 0.02 1 768 186 197 VAL HA H 4.564 0.02 1 769 186 197 VAL HB H 1.647 0.02 1 770 186 197 VAL HG1 H 0.445 0.02 2 771 186 197 VAL HG2 H 0.821 0.02 2 772 186 197 VAL CA C 61.926 0.20 1 773 186 197 VAL CB C 31.660 0.20 1 774 186 197 VAL CG1 C 20.703 0.20 2 775 186 197 VAL CG2 C 21.015 0.20 2 776 186 197 VAL N N 129.422 0.20 1 777 187 198 LEU H H 9.283 0.02 1 778 187 198 LEU HA H 4.430 0.02 1 779 187 198 LEU HB2 H 1.892 0.02 2 780 187 198 LEU HB3 H 1.230 0.02 2 781 187 198 LEU HG H 1.356 0.02 1 782 187 198 LEU HD1 H 0.956 0.02 2 783 187 198 LEU HD2 H 0.996 0.02 2 784 187 198 LEU CA C 53.073 0.20 1 785 187 198 LEU CB C 44.984 0.20 1 786 187 198 LEU CG C 27.614 0.20 1 787 187 198 LEU CD1 C 26.066 0.20 2 788 187 198 LEU CD2 C 23.268 0.20 2 789 187 198 LEU N N 130.824 0.20 1 790 188 199 ALA H H 8.641 0.02 1 791 188 199 ALA HA H 4.312 0.02 1 792 188 199 ALA HB H 1.278 0.02 1 793 188 199 ALA CA C 51.796 0.20 1 794 188 199 ALA CB C 17.044 0.20 1 795 188 199 ALA N N 132.350 0.20 1 796 189 200 MET H H 8.653 0.02 1 797 189 200 MET HA H 4.230 0.02 1 798 189 200 MET HB2 H 2.120 0.02 1 799 189 200 MET HB3 H 2.120 0.02 1 800 189 200 MET HG2 H 2.659 0.02 2 801 189 200 MET HG3 H 2.295 0.02 2 802 189 200 MET HE H 2.020 0.02 1 803 189 200 MET CA C 56.851 0.20 1 804 189 200 MET CB C 33.730 0.20 1 805 189 200 MET CG C 32.356 0.20 1 806 189 200 MET CE C 17.076 0.20 1 807 189 200 MET N N 125.268 0.20 1 808 190 201 GLY H H 10.188 0.02 1 809 190 201 GLY HA2 H 4.281 0.02 2 810 190 201 GLY HA3 H 3.953 0.02 2 811 190 201 GLY CA C 46.488 0.20 1 812 190 201 GLY N N 109.628 0.20 1 813 191 202 GLN H H 9.038 0.02 1 814 191 202 GLN HA H 4.611 0.02 1 815 191 202 GLN HB2 H 1.874 0.02 1 816 191 202 GLN HB3 H 1.874 0.02 1 817 191 202 GLN HG2 H 2.323 0.02 2 818 191 202 GLN HG3 H 2.262 0.02 2 819 191 202 GLN CA C 54.501 0.20 1 820 191 202 GLN CB C 29.226 0.20 1 821 191 202 GLN CG C 33.547 0.20 1 822 191 202 GLN N N 118.594 0.20 1 823 192 203 GLY H H 9.146 0.02 1 824 192 203 GLY HA2 H 3.997 0.02 1 825 192 203 GLY HA3 H 3.997 0.02 1 826 192 203 GLY CA C 46.442 0.20 1 827 192 203 GLY N N 110.857 0.20 1 828 193 204 ARG H H 8.314 0.02 1 829 193 204 ARG N N 117.275 0.20 1 830 194 205 MET H H 8.134 0.02 1 831 194 205 MET HA H 4.786 0.02 1 832 194 205 MET HB2 H 2.281 0.02 1 833 194 205 MET HB3 H 2.281 0.02 1 834 194 205 MET HE H 0.832 0.02 1 835 194 205 MET CA C 51.791 0.20 1 836 194 205 MET CB C 36.792 0.20 1 837 194 205 MET CE C 16.335 0.20 1 838 194 205 MET N N 114.902 0.20 1 839 195 206 ILE H H 7.539 0.02 1 840 195 206 ILE HA H 4.324 0.02 1 841 195 206 ILE HB H 1.923 0.02 1 842 195 206 ILE HG12 H 1.339 0.02 1 843 195 206 ILE HG13 H 1.339 0.02 1 844 195 206 ILE HG2 H 0.929 0.02 1 845 195 206 ILE HD1 H 0.358 0.02 1 846 195 206 ILE CA C 60.108 0.20 1 847 195 206 ILE CB C 37.344 0.20 1 848 195 206 ILE CG1 C 25.208 0.20 1 849 195 206 ILE CG2 C 18.583 0.20 1 850 195 206 ILE CD1 C 13.888 0.20 1 851 195 206 ILE N N 115.297 0.20 1 852 197 208 GLY H H 8.487 0.02 1 853 197 208 GLY HA2 H 4.396 0.02 2 854 197 208 GLY HA3 H 3.768 0.02 2 855 197 208 GLY CA C 45.758 0.20 1 856 197 208 GLY N N 111.674 0.20 1 857 198 209 PHE HD1 H 6.260 0.02 1 858 198 209 PHE HD2 H 6.260 0.02 1 859 198 209 PHE H H 7.726 0.02 1 860 198 209 PHE HB2 H 3.102 0.02 2 861 198 209 PHE HB3 H 2.536 0.02 2 862 198 209 PHE HE1 H 5.816 0.02 1 863 198 209 PHE HE2 H 5.816 0.02 1 864 198 209 PHE HZ H 5.767 0.02 1 865 198 209 PHE CB C 40.887 0.20 1 866 198 209 PHE CD1 C 130.484 0.20 1 867 198 209 PHE CD2 C 130.484 0.20 1 868 198 209 PHE CE1 C 130.263 0.20 1 869 198 209 PHE CE2 C 130.263 0.20 1 870 198 209 PHE CZ C 128.365 0.20 1 871 198 209 PHE N N 122.675 0.20 1 872 200 211 ASP HA H 4.225 0.02 1 873 200 211 ASP HB2 H 2.666 0.02 2 874 200 211 ASP HB3 H 2.523 0.02 2 875 200 211 ASP CA C 57.169 0.20 1 876 200 211 ASP CB C 40.401 0.20 1 877 201 212 GLY H H 7.407 0.02 1 878 201 212 GLY HA2 H 4.143 0.02 2 879 201 212 GLY HA3 H 3.618 0.02 2 880 201 212 GLY CA C 46.166 0.20 1 881 201 212 GLY N N 103.081 0.20 1 882 202 213 ILE H H 7.347 0.02 1 883 202 213 ILE HA H 3.880 0.02 1 884 202 213 ILE HB H 1.949 0.02 1 885 202 213 ILE HG12 H 0.939 0.02 1 886 202 213 ILE HG13 H 0.939 0.02 1 887 202 213 ILE HG2 H 1.177 0.02 1 888 202 213 ILE HD1 H 0.760 0.02 1 889 202 213 ILE CA C 63.220 0.20 1 890 202 213 ILE CB C 38.870 0.20 1 891 202 213 ILE CG1 C 29.197 0.20 1 892 202 213 ILE CG2 C 18.901 0.20 1 893 202 213 ILE CD1 C 14.012 0.20 1 894 202 213 ILE N N 119.155 0.20 1 895 203 214 LYS H H 7.042 0.02 1 896 203 214 LYS HA H 3.587 0.02 1 897 203 214 LYS HB2 H 1.741 0.02 1 898 203 214 LYS HB3 H 1.741 0.02 1 899 203 214 LYS HG2 H 1.151 0.02 1 900 203 214 LYS HG3 H 1.151 0.02 1 901 203 214 LYS HD2 H 1.764 0.02 2 902 203 214 LYS HD3 H 1.630 0.02 2 903 203 214 LYS HE2 H 2.952 0.02 1 904 203 214 LYS HE3 H 2.952 0.02 1 905 203 214 LYS CA C 58.657 0.20 1 906 203 214 LYS CB C 32.529 0.20 1 907 203 214 LYS CG C 26.029 0.20 1 908 203 214 LYS CD C 29.623 0.20 1 909 203 214 LYS CE C 42.230 0.20 1 910 203 214 LYS N N 117.433 0.20 1 911 204 215 GLY H H 8.921 0.02 1 912 204 215 GLY HA2 H 4.197 0.02 2 913 204 215 GLY HA3 H 3.511 0.02 2 914 204 215 GLY CA C 45.196 0.20 1 915 204 215 GLY N N 109.297 0.20 1 916 205 216 HIS H H 7.495 0.02 1 917 205 216 HIS HA H 4.663 0.02 1 918 205 216 HIS HB2 H 2.853 0.02 1 919 205 216 HIS HB3 H 2.853 0.02 1 920 205 216 HIS HD2 H 6.581 0.02 1 921 205 216 HIS CA C 55.763 0.20 1 922 205 216 HIS CB C 30.530 0.20 1 923 205 216 HIS CD2 C 120.764 0.20 1 924 205 216 HIS N N 117.777 0.20 1 925 206 217 LYS HD2 H 1.722 0.02 1 926 206 217 LYS HD3 H 1.722 0.02 1 927 206 217 LYS H H 8.617 0.02 1 928 206 217 LYS HA H 4.692 0.02 1 929 206 217 LYS HB2 H 1.793 0.02 2 930 206 217 LYS HB3 H 1.658 0.02 2 931 206 217 LYS HG2 H 1.356 0.02 2 932 206 217 LYS HG3 H 1.170 0.02 2 933 206 217 LYS HE2 H 2.984 0.02 1 934 206 217 LYS HE3 H 2.984 0.02 1 935 206 217 LYS CA C 54.689 0.20 1 936 206 217 LYS CB C 36.297 0.20 1 937 206 217 LYS CG C 24.814 0.20 1 938 206 217 LYS CD C 29.384 0.20 1 939 206 217 LYS CE C 42.225 0.20 1 940 206 217 LYS N N 117.895 0.20 1 941 207 218 ALA H H 8.782 0.02 1 942 207 218 ALA HA H 3.898 0.02 1 943 207 218 ALA HB H 1.411 0.02 1 944 207 218 ALA CA C 53.782 0.20 1 945 207 218 ALA CB C 18.048 0.20 1 946 207 218 ALA N N 121.134 0.20 1 947 208 219 GLY H H 9.209 0.02 1 948 208 219 GLY HA2 H 4.489 0.02 2 949 208 219 GLY HA3 H 3.837 0.02 2 950 208 219 GLY CA C 44.785 0.20 1 951 208 219 GLY N N 110.723 0.20 1 952 209 220 GLU H H 7.945 0.02 1 953 209 220 GLU HA H 4.635 0.02 1 954 209 220 GLU HG2 H 2.622 0.02 2 955 209 220 GLU HG3 H 2.388 0.02 2 956 209 220 GLU CA C 57.281 0.20 1 957 209 220 GLU CG C 38.328 0.20 1 958 209 220 GLU N N 119.791 0.20 1 959 210 221 GLU H H 8.298 0.02 1 960 210 221 GLU HA H 5.405 0.02 1 961 210 221 GLU HG2 H 2.212 0.02 2 962 210 221 GLU HG3 H 2.136 0.02 2 963 210 221 GLU CA C 54.691 0.20 1 964 210 221 GLU CG C 36.829 0.20 1 965 210 221 GLU N N 119.606 0.20 1 966 211 222 PHE HD1 H 6.509 0.02 1 967 211 222 PHE HD2 H 6.509 0.02 1 968 211 222 PHE H H 8.259 0.02 1 969 211 222 PHE HA H 5.018 0.02 1 970 211 222 PHE HB2 H 3.200 0.02 2 971 211 222 PHE HB3 H 2.969 0.02 2 972 211 222 PHE HE1 H 6.798 0.02 1 973 211 222 PHE HE2 H 6.798 0.02 1 974 211 222 PHE HZ H 6.745 0.02 1 975 211 222 PHE CA C 55.692 0.20 1 976 211 222 PHE CB C 39.015 0.20 1 977 211 222 PHE CD1 C 132.435 0.20 1 978 211 222 PHE CD2 C 132.435 0.20 1 979 211 222 PHE CE1 C 129.989 0.20 1 980 211 222 PHE CE2 C 129.989 0.20 1 981 211 222 PHE CZ C 127.415 0.20 1 982 211 222 PHE N N 120.111 0.20 1 983 212 223 THR H H 8.763 0.02 1 984 212 223 THR HA H 5.545 0.02 1 985 212 223 THR HB H 3.968 0.02 1 986 212 223 THR HG2 H 1.127 0.02 1 987 212 223 THR CA C 60.765 0.20 1 988 212 223 THR CB C 71.182 0.20 1 989 212 223 THR CG2 C 21.980 0.20 1 990 212 223 THR N N 115.346 0.20 1 991 213 224 ILE H H 8.962 0.02 1 992 213 224 ILE HA H 4.836 0.02 1 993 213 224 ILE HB H 1.884 0.02 1 994 213 224 ILE HG12 H 1.379 0.02 1 995 213 224 ILE HG13 H 1.379 0.02 1 996 213 224 ILE HG2 H 0.898 0.02 1 997 213 224 ILE HD1 H 0.271 0.02 1 998 213 224 ILE CA C 59.519 0.20 1 999 213 224 ILE CB C 41.492 0.20 1 1000 213 224 ILE CG1 C 26.404 0.20 1 1001 213 224 ILE CG2 C 18.331 0.20 1 1002 213 224 ILE CD1 C 14.543 0.20 1 1003 213 224 ILE N N 119.819 0.20 1 1004 214 225 ASP H H 8.515 0.02 1 1005 214 225 ASP HA H 5.469 0.02 1 1006 214 225 ASP HB3 H 2.523 0.02 2 1007 214 225 ASP CA C 53.881 0.20 1 1008 214 225 ASP CB C 43.054 0.20 1 1009 214 225 ASP N N 123.260 0.20 1 1010 215 226 VAL H H 8.628 0.02 1 1011 215 226 VAL HA H 4.538 0.02 1 1012 215 226 VAL HB H 1.921 0.02 1 1013 215 226 VAL HG1 H 0.623 0.02 2 1014 215 226 VAL HG2 H 0.677 0.02 2 1015 215 226 VAL CA C 59.971 0.20 1 1016 215 226 VAL CB C 36.323 0.20 1 1017 215 226 VAL CG1 C 21.702 0.20 2 1018 215 226 VAL CG2 C 20.958 0.20 2 1019 215 226 VAL N N 118.767 0.20 1 1020 216 227 THR H H 8.614 0.02 1 1021 216 227 THR HA H 4.955 0.02 1 1022 216 227 THR HB H 3.838 0.02 1 1023 216 227 THR HG2 H 1.046 0.02 1 1024 216 227 THR CA C 61.244 0.20 1 1025 216 227 THR CB C 70.208 0.20 1 1026 216 227 THR CG2 C 21.436 0.20 1 1027 216 227 THR N N 120.186 0.20 1 1028 217 228 PHE HD1 H 6.543 0.02 1 1029 217 228 PHE HD2 H 6.543 0.02 1 1030 217 228 PHE H H 8.916 0.02 1 1031 217 228 PHE HB2 H 3.289 0.02 2 1032 217 228 PHE HB3 H 2.274 0.02 2 1033 217 228 PHE HE1 H 6.827 0.02 1 1034 217 228 PHE HE2 H 6.827 0.02 1 1035 217 228 PHE HZ H 6.970 0.02 1 1036 217 228 PHE CB C 39.286 0.20 1 1037 217 228 PHE CD1 C 131.562 0.20 1 1038 217 228 PHE CD2 C 131.562 0.20 1 1039 217 228 PHE CE1 C 130.449 0.20 1 1040 217 228 PHE CE2 C 130.449 0.20 1 1041 217 228 PHE CZ C 128.204 0.20 1 1042 217 228 PHE N N 127.136 0.20 1 1043 218 229 PRO HA H 4.543 0.02 1 1044 218 229 PRO HB2 H 2.608 0.02 2 1045 218 229 PRO HB3 H 2.169 0.02 2 1046 218 229 PRO HG2 H 2.242 0.02 2 1047 218 229 PRO HG3 H 2.222 0.02 2 1048 218 229 PRO HD2 H 3.921 0.02 2 1049 218 229 PRO HD3 H 3.363 0.02 2 1050 218 229 PRO CA C 62.641 0.20 1 1051 218 229 PRO CB C 32.675 0.20 1 1052 218 229 PRO CG C 27.749 0.20 1 1053 218 229 PRO CD C 50.601 0.20 1 1054 219 230 GLU H H 8.900 0.02 1 1055 219 230 GLU HA H 3.909 0.02 1 1056 219 230 GLU HB2 H 2.037 0.02 1 1057 219 230 GLU HB3 H 2.037 0.02 1 1058 219 230 GLU HG2 H 2.414 0.02 2 1059 219 230 GLU HG3 H 2.358 0.02 2 1060 219 230 GLU CA C 59.384 0.20 1 1061 219 230 GLU CB C 29.121 0.20 1 1062 219 230 GLU CG C 36.632 0.20 1 1063 219 230 GLU N N 122.848 0.20 1 1064 220 231 GLU H H 8.206 0.02 1 1065 220 231 GLU HA H 4.519 0.02 1 1066 220 231 GLU HB2 H 2.170 0.02 2 1067 220 231 GLU HB3 H 1.962 0.02 2 1068 220 231 GLU HG2 H 2.263 0.02 1 1069 220 231 GLU HG3 H 2.263 0.02 1 1070 220 231 GLU CA C 55.592 0.20 1 1071 220 231 GLU CB C 28.823 0.20 1 1072 220 231 GLU CG C 36.325 0.20 1 1073 220 231 GLU N N 115.150 0.20 1 1074 221 232 TYR HD1 H 7.091 0.02 1 1075 221 232 TYR HD2 H 7.091 0.02 1 1076 221 232 TYR H H 7.493 0.02 1 1077 221 232 TYR HA H 4.495 0.02 1 1078 221 232 TYR HB2 H 3.388 0.02 2 1079 221 232 TYR HB3 H 2.456 0.02 2 1080 221 232 TYR HE1 H 6.764 0.02 1 1081 221 232 TYR HE2 H 6.764 0.02 1 1082 221 232 TYR CA C 59.117 0.20 1 1083 221 232 TYR CB C 40.489 0.20 1 1084 221 232 TYR CD1 C 132.059 0.20 1 1085 221 232 TYR CD2 C 132.059 0.20 1 1086 221 232 TYR CE1 C 119.738 0.20 1 1087 221 232 TYR CE2 C 119.738 0.20 1 1088 221 232 TYR N N 121.966 0.20 1 1089 222 233 HIS H H 6.861 0.02 1 1090 222 233 HIS HA H 4.119 0.02 1 1091 222 233 HIS HD2 H 6.694 0.02 1 1092 222 233 HIS CA C 58.261 0.20 1 1093 222 233 HIS CD2 C 118.781 0.20 1 1094 222 233 HIS N N 120.512 0.20 1 1095 223 234 ALA H H 5.663 0.02 1 1096 223 234 ALA HA H 4.548 0.02 1 1097 223 234 ALA HB H 1.170 0.02 1 1098 223 234 ALA CA C 50.958 0.20 1 1099 223 234 ALA CB C 18.617 0.20 1 1100 223 234 ALA N N 122.746 0.20 1 1101 224 235 GLU H H 8.924 0.02 1 1102 224 235 GLU HA H 3.813 0.02 1 1103 224 235 GLU HB2 H 2.083 0.02 1 1104 224 235 GLU HB3 H 2.083 0.02 1 1105 224 235 GLU HG2 H 2.336 0.02 1 1106 224 235 GLU HG3 H 2.336 0.02 1 1107 224 235 GLU CA C 59.725 0.20 1 1108 224 235 GLU CB C 29.672 0.20 1 1109 224 235 GLU CG C 35.949 0.20 1 1110 224 235 GLU N N 126.545 0.20 1 1111 225 236 ASN H H 8.749 0.02 1 1112 225 236 ASN HA H 4.471 0.02 1 1113 225 236 ASN HB2 H 2.770 0.02 2 1114 225 236 ASN HB3 H 2.744 0.02 2 1115 225 236 ASN CA C 54.484 0.20 1 1116 225 236 ASN CB C 36.925 0.20 1 1117 225 236 ASN N N 112.970 0.20 1 1118 226 237 LEU H H 7.118 0.02 1 1119 226 237 LEU HA H 4.098 0.02 1 1120 226 237 LEU HB2 H 0.909 0.02 2 1121 226 237 LEU HD1 H 0.105 0.02 2 1122 226 237 LEU HD2 H -0.153 0.02 2 1123 226 237 LEU CA C 54.102 0.20 1 1124 226 237 LEU CB C 43.468 0.20 1 1125 226 237 LEU CD1 C 25.267 0.20 2 1126 226 237 LEU CD2 C 21.566 0.20 2 1127 226 237 LEU N N 117.322 0.20 1 1128 227 238 LYS HD2 H 1.796 0.02 1 1129 227 238 LYS HD3 H 1.796 0.02 1 1130 227 238 LYS H H 7.025 0.02 1 1131 227 238 LYS HA H 3.856 0.02 1 1132 227 238 LYS HB2 H 1.944 0.02 2 1133 227 238 LYS HB3 H 1.833 0.02 2 1134 227 238 LYS HG2 H 1.573 0.02 2 1135 227 238 LYS HG3 H 1.513 0.02 2 1136 227 238 LYS HE2 H 3.022 0.02 2 1137 227 238 LYS HE3 H 3.084 0.02 2 1138 227 238 LYS CA C 58.207 0.20 1 1139 227 238 LYS CB C 32.513 0.20 1 1140 227 238 LYS CG C 24.051 0.20 1 1141 227 238 LYS CD C 30.044 0.20 1 1142 227 238 LYS CE C 42.363 0.20 1 1143 227 238 LYS N N 117.267 0.20 1 1144 228 239 GLY H H 7.257 0.02 1 1145 228 239 GLY HA2 H 4.023 0.02 2 1146 228 239 GLY HA3 H 3.723 0.02 2 1147 228 239 GLY CA C 46.160 0.20 1 1148 228 239 GLY N N 111.367 0.20 1 1149 229 240 LYS H H 7.873 0.02 1 1150 229 240 LYS HA H 4.418 0.02 1 1151 229 240 LYS HB2 H 1.898 0.02 1 1152 229 240 LYS HB3 H 1.898 0.02 1 1153 229 240 LYS HG2 H 1.360 0.02 2 1154 229 240 LYS HG3 H 1.206 0.02 2 1155 229 240 LYS HD2 H 1.649 0.02 2 1156 229 240 LYS HD3 H 1.588 0.02 2 1157 229 240 LYS HE2 H 2.968 0.02 1 1158 229 240 LYS HE3 H 2.968 0.02 1 1159 229 240 LYS CA C 55.724 0.20 1 1160 229 240 LYS CB C 33.287 0.20 1 1161 229 240 LYS CG C 25.207 0.20 1 1162 229 240 LYS CD C 28.733 0.20 1 1163 229 240 LYS CE C 42.496 0.20 1 1164 229 240 LYS N N 119.190 0.20 1 1165 230 241 ALA H H 8.334 0.02 1 1166 230 241 ALA HA H 4.895 0.02 1 1167 230 241 ALA HB H 1.416 0.02 1 1168 230 241 ALA CA C 51.813 0.20 1 1169 230 241 ALA CB C 19.164 0.20 1 1170 230 241 ALA N N 124.306 0.20 1 1171 231 242 ALA H H 9.282 0.02 1 1172 231 242 ALA HA H 5.210 0.02 1 1173 231 242 ALA HB H 1.290 0.02 1 1174 231 242 ALA CA C 50.416 0.20 1 1175 231 242 ALA CB C 24.200 0.20 1 1176 231 242 ALA N N 126.412 0.20 1 1177 232 243 LYS HD2 H 1.588 0.02 1 1178 232 243 LYS HD3 H 1.588 0.02 1 1179 232 243 LYS H H 8.665 0.02 1 1180 232 243 LYS HA H 5.426 0.02 1 1181 232 243 LYS HB2 H 1.579 0.02 2 1182 232 243 LYS HB3 H 1.545 0.02 2 1183 232 243 LYS HG2 H 1.456 0.02 2 1184 232 243 LYS HG3 H 1.407 0.02 2 1185 232 243 LYS HE2 H 2.940 0.02 1 1186 232 243 LYS HE3 H 2.940 0.02 1 1187 232 243 LYS CA C 54.633 0.20 1 1188 232 243 LYS CB C 36.032 0.20 1 1189 232 243 LYS CG C 24.949 0.20 1 1190 232 243 LYS CD C 29.296 0.20 1 1191 232 243 LYS CE C 42.050 0.20 1 1192 232 243 LYS N N 120.485 0.20 1 1193 233 244 PHE HD1 H 6.977 0.02 1 1194 233 244 PHE HD2 H 6.977 0.02 1 1195 233 244 PHE H H 9.121 0.02 1 1196 233 244 PHE HA H 5.254 0.02 1 1197 233 244 PHE HB2 H 2.658 0.02 2 1198 233 244 PHE HB3 H 2.500 0.02 2 1199 233 244 PHE HE1 H 7.146 0.02 1 1200 233 244 PHE HE2 H 7.146 0.02 1 1201 233 244 PHE HZ H 7.326 0.02 1 1202 233 244 PHE CA C 56.854 0.20 1 1203 233 244 PHE CB C 42.251 0.20 1 1204 233 244 PHE CD1 C 131.618 0.20 1 1205 233 244 PHE CD2 C 131.618 0.20 1 1206 233 244 PHE CE1 C 131.707 0.20 1 1207 233 244 PHE CE2 C 131.707 0.20 1 1208 233 244 PHE CZ C 128.858 0.20 1 1209 233 244 PHE N N 118.822 0.20 1 1210 234 245 ALA H H 8.567 0.02 1 1211 234 245 ALA HA H 4.667 0.02 1 1212 234 245 ALA HB H 1.360 0.02 1 1213 234 245 ALA CA C 51.795 0.20 1 1214 234 245 ALA CB C 18.824 0.20 1 1215 234 245 ALA N N 128.072 0.20 1 1216 235 246 ILE H H 9.154 0.02 1 1217 235 246 ILE HA H 4.755 0.02 1 1218 235 246 ILE HB H 0.584 0.02 1 1219 235 246 ILE HG12 H 1.075 0.02 2 1220 235 246 ILE HG13 H 0.928 0.02 2 1221 235 246 ILE HG2 H 0.513 0.02 1 1222 235 246 ILE HD1 H 0.341 0.02 1 1223 235 246 ILE CA C 58.479 0.20 1 1224 235 246 ILE CB C 38.426 0.20 1 1225 235 246 ILE CG1 C 27.364 0.20 1 1226 235 246 ILE CG2 C 18.035 0.20 1 1227 235 246 ILE CD1 C 12.315 0.20 1 1228 235 246 ILE N N 126.297 0.20 1 1229 236 247 ASN H H 8.564 0.02 1 1230 236 247 ASN HA H 5.027 0.02 1 1231 236 247 ASN HB2 H 2.865 0.02 2 1232 236 247 ASN HB3 H 2.702 0.02 2 1233 236 247 ASN CA C 52.135 0.20 1 1234 236 247 ASN CB C 40.272 0.20 1 1235 236 247 ASN N N 124.139 0.20 1 1236 237 248 LEU H H 8.596 0.02 1 1237 237 248 LEU HA H 4.734 0.02 1 1238 237 248 LEU HB2 H 1.322 0.02 1 1239 237 248 LEU HB3 H 1.322 0.02 1 1240 237 248 LEU HG H 1.386 0.02 1 1241 237 248 LEU HD1 H 0.859 0.02 2 1242 237 248 LEU HD2 H 0.901 0.02 2 1243 237 248 LEU CA C 54.643 0.20 1 1244 237 248 LEU CB C 42.878 0.20 1 1245 237 248 LEU CG C 28.139 0.20 1 1246 237 248 LEU CD1 C 27.140 0.20 2 1247 237 248 LEU CD2 C 25.210 0.20 2 1248 237 248 LEU N N 127.386 0.20 1 1249 238 249 LYS HD2 H 1.624 0.02 1 1250 238 249 LYS HD3 H 1.624 0.02 1 1251 238 249 LYS H H 8.685 0.02 1 1252 238 249 LYS HA H 4.391 0.02 1 1253 238 249 LYS HB3 H 1.466 0.02 2 1254 238 249 LYS HG2 H 1.238 0.02 1 1255 238 249 LYS HG3 H 1.238 0.02 1 1256 238 249 LYS HE2 H 2.822 0.02 1 1257 238 249 LYS HE3 H 2.822 0.02 1 1258 238 249 LYS CA C 58.269 0.20 1 1259 238 249 LYS CB C 33.506 0.20 1 1260 238 249 LYS CG C 25.247 0.20 1 1261 238 249 LYS CD C 28.876 0.20 1 1262 238 249 LYS CE C 41.617 0.20 1 1263 238 249 LYS N N 127.435 0.20 1 1264 239 250 LYS HD2 H 1.562 0.02 1 1265 239 250 LYS HD3 H 1.562 0.02 1 1266 239 250 LYS H H 7.615 0.02 1 1267 239 250 LYS HA H 4.476 0.02 1 1268 239 250 LYS HE2 H 2.812 0.02 1 1269 239 250 LYS HE3 H 2.812 0.02 1 1270 239 250 LYS CA C 56.878 0.20 1 1271 239 250 LYS CD C 29.328 0.20 1 1272 239 250 LYS CE C 41.675 0.20 1 1273 239 250 LYS N N 117.744 0.20 1 1274 240 251 VAL H H 9.168 0.02 1 1275 240 251 VAL HA H 4.639 0.02 1 1276 240 251 VAL HB H 2.301 0.02 1 1277 240 251 VAL HG1 H 1.076 0.02 2 1278 240 251 VAL HG2 H 1.044 0.02 2 1279 240 251 VAL CA C 62.171 0.20 1 1280 240 251 VAL CB C 34.556 0.20 1 1281 240 251 VAL CG1 C 22.922 0.20 2 1282 240 251 VAL CG2 C 23.005 0.20 2 1283 240 251 VAL N N 126.334 0.20 1 1284 241 252 GLU H H 9.362 0.02 1 1285 241 252 GLU HA H 5.348 0.02 1 1286 241 252 GLU HB2 H 1.903 0.02 1 1287 241 252 GLU HB3 H 1.903 0.02 1 1288 241 252 GLU HG2 H 2.017 0.02 1 1289 241 252 GLU HG3 H 2.017 0.02 1 1290 241 252 GLU CA C 54.221 0.20 1 1291 241 252 GLU CB C 29.566 0.20 1 1292 241 252 GLU CG C 37.622 0.20 1 1293 241 252 GLU N N 124.926 0.20 1 1294 242 253 GLU H H 9.527 0.02 1 1295 242 253 GLU HA H 5.523 0.02 1 1296 242 253 GLU HG2 H 2.109 0.02 1 1297 242 253 GLU HG3 H 2.109 0.02 1 1298 242 253 GLU CA C 52.932 0.20 1 1299 242 253 GLU CG C 34.897 0.20 1 1300 242 253 GLU N N 117.546 0.20 1 1301 243 254 ARG HD2 H 2.664 0.02 1 1302 243 254 ARG HD3 H 2.664 0.02 1 1303 243 254 ARG H H 8.482 0.02 1 1304 243 254 ARG HA H 3.779 0.02 1 1305 243 254 ARG HB2 H 1.182 0.02 2 1306 243 254 ARG HB3 H 1.070 0.02 2 1307 243 254 ARG HG2 H 0.794 0.02 2 1308 243 254 ARG HG3 H 0.628 0.02 2 1309 243 254 ARG CA C 56.033 0.20 1 1310 243 254 ARG CB C 30.420 0.20 1 1311 243 254 ARG CG C 26.918 0.20 1 1312 243 254 ARG CD C 43.143 0.20 1 1313 243 254 ARG N N 123.565 0.20 1 1314 244 255 GLU H H 8.282 0.02 1 1315 244 255 GLU HA H 4.256 0.02 1 1316 244 255 GLU HB2 H 1.835 0.02 2 1317 244 255 GLU HB3 H 1.661 0.02 2 1318 244 255 GLU HG2 H 2.086 0.02 2 1319 244 255 GLU HG3 H 1.985 0.02 2 1320 244 255 GLU CA C 56.281 0.20 1 1321 244 255 GLU CB C 30.974 0.20 1 1322 244 255 GLU CG C 36.714 0.20 1 1323 244 255 GLU N N 124.321 0.20 1 1324 245 256 LEU H H 8.511 0.02 1 1325 245 256 LEU N N 126.925 0.20 1 1326 246 257 PRO HA H 4.393 0.02 1 1327 246 257 PRO HB2 H 2.254 0.02 2 1328 246 257 PRO HB3 H 1.890 0.02 2 1329 246 257 PRO HG2 H 1.983 0.02 1 1330 246 257 PRO HG3 H 1.983 0.02 1 1331 246 257 PRO HD2 H 3.741 0.02 2 1332 246 257 PRO HD3 H 3.651 0.02 2 1333 246 257 PRO CA C 62.947 0.20 1 1334 246 257 PRO CB C 32.107 0.20 1 1335 246 257 PRO CG C 27.298 0.20 1 1336 246 257 PRO CD C 50.542 0.20 1 1337 247 258 GLU H H 8.521 0.02 1 1338 247 258 GLU HA H 4.349 0.02 1 1339 247 258 GLU HG2 H 2.410 0.02 1 1340 247 258 GLU HG3 H 2.410 0.02 1 1341 247 258 GLU CA C 55.571 0.20 1 1342 247 258 GLU CG C 33.920 0.20 1 1343 247 258 GLU N N 120.655 0.20 1 1344 248 259 LEU HD1 H 0.780 0.02 2 1345 248 259 LEU HD2 H 0.477 0.02 2 1346 248 259 LEU CD1 C 25.408 0.20 2 1347 248 259 LEU CD2 C 22.722 0.20 2 1348 249 260 THR H H 7.951 0.02 1 1349 249 260 THR N N 113.690 0.20 1 1350 250 261 ALA H H 8.700 0.02 1 1351 250 261 ALA HB H 1.486 0.02 1 1352 250 261 ALA CB C 18.160 0.20 1 1353 250 261 ALA N N 123.325 0.20 1 1354 251 262 GLU H H 8.344 0.02 1 1355 251 262 GLU N N 116.142 0.20 1 1356 252 263 PHE HD1 H 12.154 0.02 1 1357 252 263 PHE HD2 H 12.154 0.02 1 1358 252 263 PHE H H 7.920 0.02 1 1359 252 263 PHE HE1 H 7.159 0.02 1 1360 252 263 PHE HE2 H 7.159 0.02 1 1361 252 263 PHE CD1 C 132.047 0.20 1 1362 252 263 PHE CD2 C 132.047 0.20 1 1363 252 263 PHE CE1 C 131.296 0.20 1 1364 252 263 PHE CE2 C 131.296 0.20 1 1365 252 263 PHE N N 121.129 0.20 1 1366 253 264 ILE H H 8.248 0.02 1 1367 253 264 ILE HD1 H 0.657 0.02 1 1368 253 264 ILE CD1 C 13.046 0.20 1 1369 253 264 ILE N N 120.193 0.20 1 1370 256 267 PHE HD1 H 7.145 0.02 1 1371 256 267 PHE HD2 H 7.145 0.02 1 1372 256 267 PHE HE1 H 7.320 0.02 1 1373 256 267 PHE HE2 H 7.320 0.02 1 1374 256 267 PHE CD1 C 131.951 0.20 1 1375 256 267 PHE CD2 C 131.951 0.20 1 1376 256 267 PHE CE1 C 131.422 0.20 1 1377 256 267 PHE CE2 C 131.422 0.20 1 1378 257 268 GLY H H 7.723 0.02 1 1379 257 268 GLY N N 104.896 0.20 1 1380 258 269 VAL HG1 H 0.910 0.02 2 1381 258 269 VAL HG2 H 0.779 0.02 2 1382 258 269 VAL CG1 C 20.908 0.20 2 1383 258 269 VAL CG2 C 20.098 0.20 2 1384 259 270 GLU H H 8.587 0.02 1 1385 259 270 GLU N N 126.746 0.20 1 1386 260 271 ASP H H 8.255 0.02 1 1387 260 271 ASP N N 115.839 0.20 1 1388 261 272 GLY H H 8.119 0.02 1 1389 261 272 GLY N N 107.486 0.20 1 1390 262 273 SER H H 8.164 0.02 1 1391 262 273 SER N N 115.026 0.20 1 1392 263 274 VAL H H 8.670 0.02 1 1393 263 274 VAL HG2 H 1.018 0.02 2 1394 263 274 VAL CG2 C 22.102 0.20 2 1395 263 274 VAL N N 123.268 0.20 1 1396 264 275 GLU H H 8.811 0.02 1 1397 264 275 GLU N N 120.534 0.20 1 1398 265 276 GLY H H 8.376 0.02 1 1399 265 276 GLY N N 109.793 0.20 1 1400 266 277 LEU H H 8.087 0.02 1 1401 266 277 LEU HD1 H 0.491 0.02 2 1402 266 277 LEU HD2 H 0.803 0.02 2 1403 266 277 LEU CD1 C 23.090 0.20 2 1404 266 277 LEU CD2 C 26.005 0.20 2 1405 266 277 LEU N N 124.325 0.20 1 1406 267 278 ARG H H 8.581 0.02 1 1407 267 278 ARG N N 118.347 0.20 1 1408 268 279 ALA H H 7.727 0.02 1 1409 268 279 ALA HB H 1.518 0.02 1 1410 268 279 ALA CB C 17.875 0.20 1 1411 268 279 ALA N N 119.306 0.20 1 1412 269 280 GLU H H 7.895 0.02 1 1413 269 280 GLU N N 120.479 0.20 1 1414 270 281 VAL H H 8.356 0.02 1 1415 270 281 VAL HG1 H 0.875 0.02 2 1416 270 281 VAL HG2 H 1.021 0.02 2 1417 270 281 VAL CG1 C 22.753 0.20 2 1418 270 281 VAL CG2 C 22.283 0.20 2 1419 270 281 VAL N N 119.285 0.20 1 1420 271 282 ARG H H 7.645 0.02 1 1421 271 282 ARG N N 122.839 0.20 1 1422 274 285 MET HE H 2.072 0.02 1 1423 274 285 MET CE C 17.326 0.20 1 1424 277 288 GLU H H 8.193 0.02 1 1425 277 288 GLU N N 119.706 0.20 1 1426 278 289 LEU H H 8.892 0.02 1 1427 278 289 LEU HD1 H 0.711 0.02 2 1428 278 289 LEU HD2 H 0.783 0.02 2 1429 278 289 LEU CD1 C 26.733 0.20 2 1430 278 289 LEU CD2 C 23.810 0.20 2 1431 278 289 LEU N N 121.857 0.20 1 1432 279 290 LYS H H 8.005 0.02 1 1433 279 290 LYS N N 118.363 0.20 1 1434 280 291 SER H H 7.602 0.02 1 1435 280 291 SER N N 113.733 0.20 1 1436 281 292 ALA H H 8.207 0.02 1 1437 281 292 ALA HB H 1.450 0.02 1 1438 281 292 ALA CB C 18.749 0.20 1 1439 281 292 ALA N N 124.775 0.20 1 1440 282 293 ILE H H 8.782 0.02 1 1441 282 293 ILE HD1 H 0.847 0.02 1 1442 282 293 ILE CD1 C 14.138 0.20 1 1443 282 293 ILE N N 120.110 0.20 1 1444 283 294 ARG H H 7.661 0.02 1 1445 283 294 ARG N N 118.471 0.20 1 1446 284 295 ASN H H 8.387 0.02 1 1447 284 295 ASN N N 116.886 0.20 1 1448 285 296 ARG H H 8.257 0.02 1 1449 285 296 ARG N N 122.771 0.20 1 1450 286 297 VAL H H 8.358 0.02 1 1451 286 297 VAL HG1 H 1.116 0.02 2 1452 286 297 VAL CG1 C 22.147 0.20 2 1453 286 297 VAL N N 119.547 0.20 1 1454 287 298 LYS H H 8.326 0.02 1 1455 287 298 LYS N N 120.000 0.20 1 1456 288 299 SER H H 8.360 0.02 1 1457 288 299 SER N N 111.950 0.20 1 1458 289 300 GLN H H 7.394 0.02 1 1459 289 300 GLN N N 118.781 0.20 1 1460 290 301 ALA H H 8.242 0.02 1 1461 290 301 ALA HB H 1.405 0.02 1 1462 290 301 ALA CB C 17.592 0.20 1 1463 290 301 ALA N N 123.913 0.20 1 1464 291 302 ILE H H 8.409 0.02 1 1465 291 302 ILE HD1 H 0.786 0.02 1 1466 291 302 ILE CD1 C 12.212 0.20 1 1467 291 302 ILE N N 115.799 0.20 1 1468 292 303 GLU H H 8.269 0.02 1 1469 292 303 GLU N N 118.928 0.20 1 1470 293 304 GLY H H 8.063 0.02 1 1471 293 304 GLY N N 104.455 0.20 1 1472 294 305 LEU HD1 H 0.775 0.02 2 1473 294 305 LEU HD2 H 0.759 0.02 2 1474 294 305 LEU CD1 C 23.634 0.20 2 1475 294 305 LEU CD2 C 23.970 0.20 2 1476 295 306 VAL H H 8.391 0.02 1 1477 295 306 VAL N N 118.721 0.20 1 1478 296 307 LYS H H 8.216 0.02 1 1479 296 307 LYS N N 118.356 0.20 1 1480 297 308 ALA H H 7.187 0.02 1 1481 297 308 ALA HB H 1.446 0.02 1 1482 297 308 ALA CB C 20.335 0.20 1 1483 297 308 ALA N N 116.317 0.20 1 1484 298 309 ASN H H 7.322 0.02 1 1485 298 309 ASN N N 117.826 0.20 1 1486 299 310 ASP H H 8.358 0.02 1 1487 299 310 ASP N N 122.284 0.20 1 1488 300 311 ILE H H 7.726 0.02 1 1489 300 311 ILE HD1 H 0.845 0.02 1 1490 300 311 ILE CD1 C 14.325 0.20 1 1491 300 311 ILE N N 119.572 0.20 1 1492 301 312 ASP H H 8.436 0.02 1 1493 301 312 ASP N N 123.363 0.20 1 1494 302 313 VAL H H 8.151 0.02 1 1495 302 313 VAL HG1 H 1.110 0.02 2 1496 302 313 VAL HG2 H 0.868 0.02 2 1497 302 313 VAL CG1 C 23.893 0.20 2 1498 302 313 VAL CG2 C 20.781 0.20 2 1499 302 313 VAL N N 121.316 0.20 1 1500 304 315 ALA H H 8.724 0.02 1 1501 304 315 ALA HB H 1.459 0.02 1 1502 304 315 ALA CB C 18.042 0.20 1 1503 304 315 ALA N N 128.128 0.20 1 1504 305 316 ALA H H 8.807 0.02 1 1505 305 316 ALA HB H 1.402 0.02 1 1506 305 316 ALA CB C 18.290 0.20 1 1507 305 316 ALA N N 116.918 0.20 1 1508 306 317 LEU H H 7.200 0.02 1 1509 306 317 LEU HD1 H 0.866 0.02 2 1510 306 317 LEU HD2 H 0.877 0.02 2 1511 306 317 LEU CD1 C 24.942 0.20 2 1512 306 317 LEU CD2 C 22.097 0.20 2 1513 306 317 LEU N N 114.797 0.20 1 1514 307 318 ILE H H 7.162 0.02 1 1515 307 318 ILE HD1 H 0.842 0.02 1 1516 307 318 ILE CD1 C 13.006 0.20 1 1517 307 318 ILE N N 120.409 0.20 1 1518 308 319 ASP H H 8.500 0.02 1 1519 308 319 ASP N N 119.578 0.20 1 1520 309 320 SER H H 7.665 0.02 1 1521 309 320 SER N N 113.928 0.20 1 1522 310 321 GLU H H 7.577 0.02 1 1523 310 321 GLU N N 123.422 0.20 1 1524 311 322 ILE H H 8.722 0.02 1 1525 311 322 ILE HD1 H 0.906 0.02 1 1526 311 322 ILE CD1 C 14.193 0.20 1 1527 311 322 ILE N N 120.918 0.20 1 1528 312 323 ASP H H 7.339 0.02 1 1529 312 323 ASP N N 118.634 0.20 1 1530 313 324 VAL H H 7.379 0.02 1 1531 313 324 VAL N N 120.710 0.20 1 1532 314 325 LEU H H 8.068 0.02 1 1533 314 325 LEU HD1 H 0.810 0.02 2 1534 314 325 LEU HD2 H 0.971 0.02 2 1535 314 325 LEU CD1 C 21.616 0.20 2 1536 314 325 LEU CD2 C 26.456 0.20 2 1537 314 325 LEU N N 124.449 0.20 1 1538 315 326 ARG H H 8.694 0.02 1 1539 315 326 ARG N N 121.339 0.20 1 1540 318 329 ALA H H 8.025 0.02 1 1541 318 329 ALA HB H 1.651 0.02 1 1542 318 329 ALA CB C 17.959 0.20 1 1543 318 329 ALA N N 122.488 0.20 1 1544 319 330 ALA H H 8.051 0.02 1 1545 319 330 ALA HB H 1.233 0.02 1 1546 319 330 ALA CB C 17.769 0.20 1 1547 319 330 ALA N N 119.376 0.20 1 1548 320 331 GLN H H 7.724 0.02 1 1549 320 331 GLN N N 116.844 0.20 1 1550 321 332 ARG H H 7.570 0.02 1 1551 321 332 ARG N N 118.232 0.20 1 1552 322 333 PHE HD1 H 7.252 0.02 1 1553 322 333 PHE HD2 H 7.252 0.02 1 1554 322 333 PHE H H 7.605 0.02 1 1555 322 333 PHE HE1 H 7.266 0.02 1 1556 322 333 PHE HE2 H 7.266 0.02 1 1557 322 333 PHE HZ H 7.207 0.02 1 1558 322 333 PHE CD1 C 132.792 0.20 1 1559 322 333 PHE CD2 C 132.792 0.20 1 1560 322 333 PHE CE1 C 131.093 0.20 1 1561 322 333 PHE CE2 C 131.093 0.20 1 1562 322 333 PHE CZ C 129.156 0.20 1 1563 322 333 PHE N N 115.830 0.20 1 1564 323 334 GLY H H 7.891 0.02 1 1565 323 334 GLY N N 109.847 0.20 1 1566 324 335 GLY H H 8.143 0.02 1 1567 324 335 GLY N N 107.960 0.20 1 1568 325 336 ASN H H 8.197 0.02 1 1569 325 336 ASN N N 118.780 0.20 1 1570 326 337 GLU H H 8.573 0.02 1 1571 326 337 GLU N N 120.944 0.20 1 1572 327 338 LYS H H 8.065 0.02 1 1573 327 338 LYS N N 119.436 0.20 1 1574 328 339 GLN H H 7.930 0.02 1 1575 328 339 GLN N N 117.642 0.20 1 1576 329 340 ALA H H 8.010 0.02 1 1577 329 340 ALA HB H 1.327 0.02 1 1578 329 340 ALA CB C 18.289 0.20 1 1579 329 340 ALA N N 122.197 0.20 1 1580 330 341 LEU H H 7.727 0.02 1 1581 330 341 LEU HD1 H 0.848 0.02 2 1582 330 341 LEU HD2 H 0.758 0.02 2 1583 330 341 LEU CD1 C 24.741 0.20 2 1584 330 341 LEU CD2 C 22.361 0.20 2 1585 330 341 LEU N N 115.859 0.20 1 1586 332 343 LEU HD1 H 1.139 0.02 2 1587 332 343 LEU HD2 H 0.962 0.02 2 1588 332 343 LEU CD1 C 26.423 0.20 2 1589 332 343 LEU CD2 C 22.578 0.20 2 1590 334 345 ARG H H 8.747 0.02 1 1591 334 345 ARG N N 122.570 0.20 1 1592 335 346 GLU H H 9.552 0.02 1 1593 335 346 GLU N N 117.314 0.20 1 1594 336 347 LEU H H 7.468 0.02 1 1595 336 347 LEU HD1 H 0.693 0.02 2 1596 336 347 LEU HD2 H 0.804 0.02 2 1597 336 347 LEU CD1 C 22.379 0.20 2 1598 336 347 LEU CD2 C 25.003 0.20 2 1599 336 347 LEU N N 118.542 0.20 1 1600 337 348 PHE HD1 H 6.915 0.02 1 1601 337 348 PHE HD2 H 6.915 0.02 1 1602 337 348 PHE H H 7.652 0.02 1 1603 337 348 PHE HE1 H 7.058 0.02 1 1604 337 348 PHE HE2 H 7.058 0.02 1 1605 337 348 PHE HZ H 7.174 0.02 1 1606 337 348 PHE CD1 C 132.215 0.20 1 1607 337 348 PHE CD2 C 132.215 0.20 1 1608 337 348 PHE CE1 C 130.876 0.20 1 1609 337 348 PHE CE2 C 130.876 0.20 1 1610 337 348 PHE CZ C 129.147 0.20 1 1611 337 348 PHE N N 113.608 0.20 1 1612 338 349 GLU H H 7.360 0.02 1 1613 338 349 GLU N N 119.332 0.20 1 1614 339 350 GLU H H 8.687 0.02 1 1615 339 350 GLU N N 119.520 0.20 1 1616 340 351 GLN H H 8.641 0.02 1 1617 340 351 GLN N N 120.577 0.20 1 1618 341 352 ALA H H 8.722 0.02 1 1619 341 352 ALA HB H 1.497 0.02 1 1620 341 352 ALA CB C 20.356 0.20 1 1621 341 352 ALA N N 121.615 0.20 1 1622 342 353 LYS H H 8.272 0.02 1 1623 342 353 LYS N N 116.824 0.20 1 1624 343 354 ARG H H 7.677 0.02 1 1625 343 354 ARG N N 117.337 0.20 1 1626 344 355 ARG H H 7.996 0.02 1 1627 344 355 ARG N N 116.939 0.20 1 1628 345 356 VAL H H 8.132 0.02 1 1629 345 356 VAL HG1 H 0.960 0.02 2 1630 345 356 VAL HG2 H 0.897 0.02 2 1631 345 356 VAL CG1 C 22.815 0.20 2 1632 345 356 VAL CG2 C 23.018 0.20 2 1633 345 356 VAL N N 119.122 0.20 1 1634 346 357 VAL H H 8.585 0.02 1 1635 346 357 VAL N N 120.448 0.20 1 1636 347 358 VAL H H 8.497 0.02 1 1637 347 358 VAL HG1 H 0.818 0.02 2 1638 347 358 VAL HG2 H 0.874 0.02 2 1639 347 358 VAL CG1 C 25.857 0.20 2 1640 347 358 VAL CG2 C 20.936 0.20 2 1641 347 358 VAL N N 119.412 0.20 1 1642 348 359 GLY H H 7.919 0.02 1 1643 348 359 GLY N N 104.934 0.20 1 1644 349 360 LEU H H 8.244 0.02 1 1645 349 360 LEU HD1 H 0.819 0.02 2 1646 349 360 LEU HD2 H 0.875 0.02 2 1647 349 360 LEU CD1 C 26.434 0.20 2 1648 349 360 LEU CD2 C 22.753 0.20 2 1649 349 360 LEU N N 122.747 0.20 1 1650 350 361 LEU H H 8.626 0.02 1 1651 350 361 LEU N N 119.683 0.20 1 1652 351 362 LEU H H 9.121 0.02 1 1653 351 362 LEU HD1 H 1.084 0.02 2 1654 351 362 LEU HD2 H 0.622 0.02 2 1655 351 362 LEU CD1 C 23.697 0.20 2 1656 351 362 LEU CD2 C 21.124 0.20 2 1657 351 362 LEU N N 117.476 0.20 1 1658 352 363 GLY H H 8.174 0.02 1 1659 352 363 GLY N N 106.559 0.20 1 1660 353 364 GLU H H 7.695 0.02 1 1661 353 364 GLU N N 123.148 0.20 1 1662 354 365 VAL H H 8.118 0.02 1 1663 354 365 VAL HG1 H 0.947 0.02 2 1664 354 365 VAL CG1 C 22.027 0.20 2 1665 354 365 VAL N N 124.567 0.20 1 1666 355 366 ILE H H 8.464 0.02 1 1667 355 366 ILE HD1 H 0.847 0.02 1 1668 355 366 ILE CD1 C 14.138 0.20 1 1669 355 366 ILE N N 120.971 0.20 1 1670 356 367 ARG H H 8.131 0.02 1 1671 356 367 ARG N N 118.729 0.20 1 1672 357 368 THR H H 8.668 0.02 1 1673 357 368 THR N N 111.757 0.20 1 1674 358 369 ASN H H 7.415 0.02 1 1675 358 369 ASN N N 115.915 0.20 1 1676 359 370 GLU H H 7.702 0.02 1 1677 359 370 GLU N N 118.262 0.20 1 1678 360 371 LEU H H 8.013 0.02 1 1679 360 371 LEU HD1 H 0.673 0.02 2 1680 360 371 LEU HD2 H 0.807 0.02 2 1681 360 371 LEU CD1 C 25.044 0.20 2 1682 360 371 LEU CD2 C 22.174 0.20 2 1683 360 371 LEU N N 115.602 0.20 1 1684 361 372 LYS H H 8.313 0.02 1 1685 361 372 LYS N N 120.293 0.20 1 1686 362 373 ALA H H 8.957 0.02 1 1687 362 373 ALA HB H 1.286 0.02 1 1688 362 373 ALA CB C 18.214 0.20 1 1689 362 373 ALA N N 126.120 0.20 1 1690 363 374 ASP H H 8.956 0.02 1 1691 363 374 ASP N N 124.600 0.20 1 1692 364 375 GLU H H 9.040 0.02 1 1693 364 375 GLU N N 127.220 0.20 1 1694 367 378 VAL H H 8.008 0.02 1 1695 367 378 VAL HG1 H 0.921 0.02 2 1696 367 378 VAL HG2 H 0.838 0.02 2 1697 367 378 VAL CG1 C 23.971 0.20 2 1698 367 378 VAL CG2 C 21.554 0.20 2 1699 367 378 VAL N N 120.091 0.20 1 1700 368 379 LYS H H 7.731 0.02 1 1701 368 379 LYS N N 118.033 0.20 1 1702 369 380 GLY H H 7.892 0.02 1 1703 369 380 GLY N N 106.211 0.20 1 1704 370 381 LEU H H 8.275 0.02 1 1705 370 381 LEU HD1 H 0.818 0.02 2 1706 370 381 LEU HD2 H 0.875 0.02 2 1707 370 381 LEU CD1 C 25.857 0.20 2 1708 370 381 LEU CD2 C 22.753 0.20 2 1709 370 381 LEU N N 123.897 0.20 1 1710 371 382 ILE H H 7.998 0.02 1 1711 371 382 ILE HD1 H 0.803 0.02 1 1712 371 382 ILE CD1 C 14.401 0.20 1 1713 371 382 ILE N N 120.719 0.20 1 1714 372 383 GLU H H 8.261 0.02 1 1715 372 383 GLU N N 119.893 0.20 1 1716 373 384 GLU H H 8.096 0.02 1 1717 373 384 GLU N N 118.988 0.20 1 1718 374 385 MET H H 7.897 0.02 1 1719 374 385 MET HE H 1.703 0.02 1 1720 374 385 MET CE C 16.619 0.20 1 1721 374 385 MET N N 121.026 0.20 1 1722 375 386 ALA H H 8.462 0.02 1 1723 375 386 ALA HB H 1.543 0.02 1 1724 375 386 ALA CB C 19.068 0.20 1 1725 375 386 ALA N N 120.516 0.20 1 1726 377 388 ALA H H 7.414 0.02 1 1727 377 388 ALA HB H 1.199 0.02 1 1728 377 388 ALA CB C 18.819 0.20 1 1729 377 388 ALA N N 122.271 0.20 1 1730 378 389 TYR H H 7.862 0.02 1 1731 378 389 TYR HD1 H 7.260 0.02 3 1732 378 389 TYR HE1 H 6.828 0.02 3 1733 378 389 TYR CD1 C 133.672 0.20 1 1734 378 389 TYR CD2 C 133.672 0.20 1 1735 378 389 TYR CE1 C 118.147 0.20 1 1736 378 389 TYR CE2 C 118.147 0.20 1 1737 378 389 TYR N N 117.760 0.20 1 1738 379 390 GLU H H 8.545 0.02 1 1739 379 390 GLU N N 119.660 0.20 1 1740 380 391 ASP H H 8.214 0.02 1 1741 380 391 ASP N N 116.112 0.20 1 1742 382 393 LYS H H 7.862 0.02 1 1743 382 393 LYS N N 114.882 0.20 1 1744 383 394 GLU H H 7.462 0.02 1 1745 383 394 GLU N N 118.911 0.20 1 1746 384 395 VAL H H 7.190 0.02 1 1747 384 395 VAL HG1 H 0.580 0.02 2 1748 384 395 VAL HG2 H 0.420 0.02 2 1749 384 395 VAL CG1 C 20.931 0.20 2 1750 384 395 VAL CG2 C 21.528 0.20 2 1751 384 395 VAL N N 120.470 0.20 1 1752 385 396 ILE H H 8.202 0.02 1 1753 385 396 ILE HD1 H 0.800 0.02 1 1754 385 396 ILE CD1 C 13.634 0.20 1 1755 385 396 ILE N N 120.222 0.20 1 1756 386 397 GLU H H 7.991 0.02 1 1757 386 397 GLU N N 120.075 0.20 1 1758 387 398 PHE H H 8.067 0.02 1 1759 387 398 PHE HE1 H 7.212 0.02 1 1760 387 398 PHE HE2 H 7.212 0.02 1 1761 387 398 PHE HZ H 7.212 0.02 1 1762 387 398 PHE CD1 C 131.951 0.20 1 1763 387 398 PHE CD2 C 131.951 0.20 1 1764 387 398 PHE CE1 C 131.429 0.20 1 1765 387 398 PHE CE2 C 131.429 0.20 1 1766 387 398 PHE CZ C 129.835 0.20 1 1767 387 398 PHE N N 120.181 0.20 1 1768 388 399 TYR H H 8.565 0.02 1 1769 388 399 TYR HD1 H 7.105 0.02 3 1770 388 399 TYR HE1 H 6.801 0.02 3 1771 388 399 TYR CD1 C 133.255 0.20 1 1772 388 399 TYR CD2 C 133.255 0.20 1 1773 388 399 TYR CE1 C 118.192 0.20 1 1774 388 399 TYR CE2 C 118.192 0.20 1 1775 388 399 TYR N N 118.574 0.20 1 1776 389 400 SER H H 7.891 0.02 1 1777 389 400 SER N N 109.847 0.20 1 1778 390 401 LYS H H 7.198 0.02 1 1779 390 401 LYS N N 117.760 0.20 1 1780 391 402 ASN H H 7.453 0.02 1 1781 391 402 ASN N N 120.998 0.20 1 1782 392 403 LYS H H 8.563 0.02 1 1783 392 403 LYS N N 126.720 0.20 1 1784 393 404 GLU H H 8.329 0.02 1 1785 393 404 GLU N N 117.853 0.20 1 1786 394 405 LEU H H 7.674 0.02 1 1787 394 405 LEU HD1 H 0.345 0.02 2 1788 394 405 LEU HD2 H 0.594 0.02 2 1789 394 405 LEU CD1 C 25.070 0.20 2 1790 394 405 LEU CD2 C 22.449 0.20 2 1791 394 405 LEU N N 119.862 0.20 1 1792 395 406 MET H H 8.126 0.02 1 1793 395 406 MET HE H 1.917 0.02 1 1794 395 406 MET CE C 15.650 0.20 1 1795 395 406 MET N N 118.731 0.20 1 1796 396 407 ASP H H 8.725 0.02 1 1797 396 407 ASP N N 120.228 0.20 1 1798 397 408 ASN H H 7.907 0.02 1 1799 397 408 ASN N N 118.663 0.20 1 1800 398 409 MET H H 8.203 0.02 1 1801 398 409 MET HE H 1.906 0.02 1 1802 398 409 MET CE C 17.189 0.20 1 1803 398 409 MET N N 118.795 0.20 1 1804 399 410 ARG H H 8.587 0.02 1 1805 399 410 ARG N N 120.384 0.20 1 1806 400 411 ASN H H 7.677 0.02 1 1807 400 411 ASN N N 117.337 0.20 1 1808 401 412 VAL H H 7.969 0.02 1 1809 401 412 VAL HG1 H 1.083 0.02 2 1810 401 412 VAL HG2 H 0.959 0.02 2 1811 401 412 VAL CG1 C 22.352 0.20 2 1812 401 412 VAL CG2 C 21.735 0.20 2 1813 401 412 VAL N N 123.012 0.20 1 1814 402 413 ALA H H 8.239 0.02 1 1815 402 413 ALA HB H 1.454 0.02 1 1816 402 413 ALA CB C 18.037 0.20 1 1817 402 413 ALA N N 122.737 0.20 1 1818 403 414 LEU H H 8.362 0.02 1 1819 403 414 LEU HD1 H 0.786 0.02 2 1820 403 414 LEU HD2 H 0.749 0.02 2 1821 403 414 LEU CD1 C 24.197 0.20 2 1822 403 414 LEU CD2 C 24.518 0.20 2 1823 403 414 LEU N N 118.229 0.20 1 1824 404 415 GLU H H 8.034 0.02 1 1825 404 415 GLU N N 119.385 0.20 1 1826 406 417 GLN H H 8.645 0.02 1 1827 406 417 GLN N N 119.090 0.20 1 1828 407 418 ALA H H 8.853 0.02 1 1829 407 418 ALA HB H 1.465 0.02 1 1830 407 418 ALA CB C 18.378 0.20 1 1831 407 418 ALA N N 124.991 0.20 1 1832 408 419 VAL H H 8.189 0.02 1 1833 408 419 VAL HG1 H 0.950 0.02 2 1834 408 419 VAL HG2 H 0.862 0.02 2 1835 408 419 VAL CG1 C 23.145 0.20 2 1836 408 419 VAL CG2 C 21.043 0.20 2 1837 408 419 VAL N N 118.726 0.20 1 1838 409 420 GLU H H 8.121 0.02 1 1839 409 420 GLU N N 118.697 0.20 1 1840 410 421 ALA H H 7.890 0.02 1 1841 410 421 ALA HB H 1.400 0.02 1 1842 410 421 ALA CB C 17.121 0.20 1 1843 410 421 ALA N N 122.789 0.20 1 1844 411 422 VAL H H 7.723 0.02 1 1845 411 422 VAL HG1 H 0.760 0.02 2 1846 411 422 VAL HG2 H 1.014 0.02 2 1847 411 422 VAL CG1 C 25.865 0.20 2 1848 411 422 VAL CG2 C 23.201 0.20 2 1849 411 422 VAL N N 119.894 0.20 1 1850 412 423 LEU H H 8.487 0.02 1 1851 412 423 LEU HD1 H 0.772 0.02 2 1852 412 423 LEU HD2 H 0.724 0.02 2 1853 412 423 LEU CD1 C 25.595 0.20 2 1854 412 423 LEU CD2 C 23.981 0.20 2 1855 412 423 LEU N N 119.469 0.20 1 1856 413 424 ALA H H 7.632 0.02 1 1857 413 424 ALA HB H 1.467 0.02 1 1858 413 424 ALA CB C 18.180 0.20 1 1859 413 424 ALA N N 117.817 0.20 1 1860 414 425 LYS H H 7.130 0.02 1 1861 414 425 LYS N N 114.675 0.20 1 1862 415 426 ALA H H 7.157 0.02 1 1863 415 426 ALA HB H 1.253 0.02 1 1864 415 426 ALA CB C 19.600 0.20 1 1865 415 426 ALA N N 121.064 0.20 1 1866 416 427 LYS H H 8.689 0.02 1 1867 416 427 LYS N N 120.724 0.20 1 1868 417 428 VAL H H 8.428 0.02 1 1869 417 428 VAL HG1 H 0.785 0.02 2 1870 417 428 VAL HG2 H 0.808 0.02 2 1871 417 428 VAL CG1 C 20.929 0.20 2 1872 417 428 VAL CG2 C 21.442 0.20 2 1873 417 428 VAL N N 128.909 0.20 1 1874 418 429 THR H H 8.940 0.02 1 1875 418 429 THR N N 123.460 0.20 1 1876 419 430 GLU H H 8.773 0.02 1 1877 419 430 GLU N N 123.718 0.20 1 1878 420 431 LYS H H 8.275 0.02 1 1879 420 431 LYS N N 123.897 0.20 1 1880 421 432 GLU H H 9.158 0.02 1 1881 421 432 GLU N N 130.232 0.20 1 1882 422 433 THR H H 8.414 0.02 1 1883 422 433 THR N N 119.935 0.20 1 1884 423 434 THR H H 8.494 0.02 1 1885 423 434 THR N N 111.995 0.20 1 1886 424 435 PHE HD1 H 7.234 0.02 1 1887 424 435 PHE HD2 H 7.234 0.02 1 1888 424 435 PHE H H 9.852 0.02 1 1889 424 435 PHE HE1 H 7.094 0.02 1 1890 424 435 PHE HE2 H 7.094 0.02 1 1891 424 435 PHE HZ H 7.272 0.02 1 1892 424 435 PHE CD1 C 131.955 0.20 1 1893 424 435 PHE CD2 C 131.955 0.20 1 1894 424 435 PHE CE1 C 131.951 0.20 1 1895 424 435 PHE CE2 C 131.951 0.20 1 1896 424 435 PHE CZ C 129.814 0.20 1 1897 424 435 PHE N N 124.137 0.20 1 1898 425 436 ASN H H 9.407 0.02 1 1899 425 436 ASN N N 115.449 0.20 1 1900 426 437 GLU H H 7.666 0.02 1 1901 426 437 GLU N N 118.220 0.20 1 1902 427 438 LEU H H 7.928 0.02 1 1903 427 438 LEU HD1 H 1.012 0.02 2 1904 427 438 LEU HD2 H 0.921 0.02 2 1905 427 438 LEU CD1 C 26.385 0.20 2 1906 427 438 LEU CD2 C 23.971 0.20 2 1907 427 438 LEU N N 119.426 0.20 1 1908 428 439 MET H H 8.006 0.02 1 1909 428 439 MET HE H 1.703 0.02 1 1910 428 439 MET CE C 16.619 0.20 1 1911 428 439 MET N N 113.980 0.20 1 1912 429 440 ASN H H 7.558 0.02 1 1913 429 440 ASN N N 116.972 0.20 1 1914 430 441 GLN H H 7.787 0.02 1 1915 430 441 GLN N N 119.108 0.20 1 1916 431 442 GLN H H 8.129 0.02 1 1917 431 442 GLN N N 120.745 0.20 1 1918 432 443 ALA H H 7.919 0.02 1 1919 432 443 ALA HB H 1.311 0.02 1 1920 432 443 ALA CB C 19.768 0.20 1 1921 432 443 ALA N N 130.896 0.20 1 stop_ save_ save_assigned_chem_shift_list_1_dup _Saveframe_category assigned_chemical_shifts _Details . loop_ _Software_label $OLIVIA stop_ loop_ _Experiment_label '2D 1H-15N HSQC' '2D 1H-13C HSQC' 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 entity_1 _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 1005 6 THR HA H 4.386 0.02 1 2 1005 6 THR HB H 4.216 0.02 1 3 1005 6 THR HG2 H 1.265 0.02 1 4 1005 6 THR CA C 62.332 0.20 1 5 1005 6 THR CB C 69.920 0.20 1 6 1005 6 THR CG2 C 21.742 0.20 1 7 1006 7 ILE HA H 4.173 0.02 1 8 1006 7 ILE HB H 1.874 0.02 1 9 1006 7 ILE HG12 H 1.495 0.02 2 10 1006 7 ILE HG13 H 1.204 0.02 2 11 1006 7 ILE HG2 H 0.920 0.02 1 12 1006 7 ILE HD1 H 0.839 0.02 1 13 1006 7 ILE CA C 61.448 0.20 1 14 1006 7 ILE CB C 38.841 0.20 1 15 1006 7 ILE CG1 C 27.490 0.20 1 16 1006 7 ILE CG2 C 17.610 0.20 1 17 1006 7 ILE CD1 C 12.918 0.20 1 18 1007 8 ALA HA H 4.326 0.02 1 19 1007 8 ALA HB H 1.395 0.02 1 20 1007 8 ALA CA C 52.657 0.20 1 21 1007 8 ALA CB C 19.287 0.20 1 22 1008 9 LEU HA H 4.406 0.02 1 23 1008 9 LEU HB2 H 1.655 0.02 1 24 1008 9 LEU HB3 H 1.655 0.02 1 25 1008 9 LEU HG H 1.647 0.02 1 26 1008 9 LEU HD1 H 0.936 0.02 2 27 1008 9 LEU HD2 H 0.883 0.02 2 28 1008 9 LEU CA C 55.143 0.20 1 29 1008 9 LEU CB C 42.407 0.20 1 30 1008 9 LEU CG C 27.017 0.20 1 31 1008 9 LEU CD1 C 25.526 0.20 2 32 1008 9 LEU CD2 C 23.524 0.20 2 33 1013 14 LEU HD1 H 0.893 0.02 2 34 1013 14 LEU HD2 H 0.853 0.02 2 35 1013 14 LEU CD1 C 25.126 0.20 2 36 1013 14 LEU CD2 C 23.795 0.20 2 37 1014 15 LEU HG H 1.518 0.02 1 38 1014 15 LEU HD1 H 0.865 0.02 2 39 1014 15 LEU HD2 H 0.862 0.02 2 40 1014 15 LEU CG C 27.053 0.20 1 41 1014 15 LEU CD1 C 25.252 0.20 2 42 1014 15 LEU CD2 C 23.865 0.20 2 43 1015 16 PHE HD1 H 7.226 0.02 1 44 1015 16 PHE HD2 H 7.226 0.02 1 45 1015 16 PHE CD1 C 131.785 0.20 1 46 1015 16 PHE CD2 C 131.785 0.20 1 47 1016 17 THR HG2 H 1.217 0.02 1 48 1016 17 THR CG2 C 21.503 0.20 1 49 1019 20 THR H H 8.319 0.02 1 50 1019 20 THR N N 119.375 0.20 1 51 1020 21 LYS H H 8.427 0.02 1 52 1020 21 LYS N N 124.950 0.20 1 53 1021 22 ALA H H 8.433 0.02 1 54 1021 22 ALA N N 126.333 0.20 1 55 1022 23 ARG H H 8.498 0.02 1 56 1022 23 ARG N N 121.479 0.20 1 57 1023 24 THR H H 8.320 0.02 1 58 1023 24 THR N N 118.673 0.20 1 59 1025 26 GLU H H 8.564 0.02 1 60 1025 26 GLU N N 121.089 0.20 1 61 1026 27 MET H H 8.406 0.02 1 62 1026 27 MET N N 123.057 0.20 1 63 1028 29 VAL H H 8.393 0.02 1 64 1028 29 VAL N N 121.589 0.20 1 65 1029 30 LEU H H 8.450 0.02 1 66 1029 30 LEU N N 127.039 0.20 1 67 1030 31 GLU H H 8.508 0.02 1 68 1030 31 GLU N N 122.499 0.20 1 69 1031 32 ASN H H 8.581 0.02 1 70 1031 32 ASN N N 120.507 0.20 1 71 1032 33 ARG H H 8.455 0.02 1 72 1032 33 ARG N N 122.393 0.20 1 73 1033 34 ALA H H 8.361 0.02 1 74 1033 34 ALA N N 124.978 0.20 1 75 1034 35 ALA H H 8.312 0.02 1 76 1034 35 ALA N N 123.379 0.20 1 77 1035 36 GLN H H 8.375 0.02 1 78 1035 36 GLN N N 119.717 0.20 1 79 1036 37 GLY H H 8.413 0.02 1 80 1036 37 GLY N N 109.975 0.20 1 81 1037 38 ASP H H 8.283 0.02 1 82 1037 38 ASP N N 120.636 0.20 1 83 1038 39 ILE H H 8.248 0.02 1 84 1038 39 ILE N N 121.247 0.20 1 85 1039 40 THR H H 8.333 0.02 1 86 1039 40 THR N N 118.020 0.20 1 87 1040 41 ALA H H 8.267 0.02 1 88 1040 41 ALA N N 128.190 0.20 1 89 1042 43 GLY H H 8.655 0.02 1 90 1042 43 GLY N N 110.082 0.20 1 91 1043 44 GLY H H 8.363 0.02 1 92 1043 44 GLY N N 108.933 0.20 1 93 1044 45 ALA H H 8.252 0.02 1 94 1044 45 ALA N N 123.798 0.20 1 95 1045 46 ARG H H 8.361 0.02 1 96 1045 46 ARG N N 120.625 0.20 1 97 1046 47 ARG H H 8.450 0.02 1 98 1046 47 ARG N N 123.130 0.20 1 99 1048 49 THR H H 8.236 0.02 1 100 1048 49 THR N N 114.050 0.20 1 101 1049 50 GLY H H 8.573 0.02 1 102 1049 50 GLY N N 110.835 0.20 1 103 1050 51 ASP H H 8.385 0.02 1 104 1050 51 ASP N N 120.701 0.20 1 105 1051 52 GLN H H 8.522 0.02 1 106 1051 52 GLN N N 121.566 0.20 1 107 1052 53 THR H H 8.295 0.02 1 108 1052 53 THR N N 115.354 0.20 1 109 1053 54 ALA H H 8.252 0.02 1 110 1053 54 ALA N N 126.109 0.20 1 111 1054 55 ALA H H 8.137 0.02 1 112 1054 55 ALA N N 122.159 0.20 1 113 1055 56 LEU H H 8.084 0.02 1 114 1055 56 LEU N N 120.759 0.20 1 115 1057 58 ASP H H 8.415 0.02 1 116 1057 58 ASP N N 121.179 0.20 1 117 1058 59 SER H H 8.262 0.02 1 118 1058 59 SER N N 116.298 0.20 1 119 1059 60 LEU H H 8.259 0.02 1 120 1059 60 LEU N N 123.176 0.20 1 121 1060 61 SER H H 8.129 0.02 1 122 1060 61 SER N N 115.608 0.20 1 123 1061 62 ASP H H 8.294 0.02 1 124 1061 62 ASP N N 122.288 0.20 1 125 1062 63 LYS H H 8.182 0.02 1 126 1062 63 LYS N N 122.252 0.20 1 127 1064 65 ALA H H 8.498 0.02 1 128 1064 65 ALA N N 124.836 0.20 1 129 1065 66 LYS H H 8.357 0.02 1 130 1065 66 LYS N N 120.517 0.20 1 131 1066 67 ASN H H 8.484 0.02 1 132 1066 67 ASN N N 120.010 0.20 1 133 1067 68 ILE H H 8.161 0.02 1 134 1067 68 ILE N N 121.927 0.20 1 135 1068 69 ILE H H 8.270 0.02 1 136 1068 69 ILE N N 126.015 0.20 1 137 1069 70 LEU H H 8.348 0.02 1 138 1069 70 LEU N N 127.306 0.20 1 139 1070 71 LEU H H 8.334 0.02 1 140 1070 71 LEU N N 124.247 0.20 1 141 1071 72 ILE H H 8.211 0.02 1 142 1071 72 ILE N N 122.309 0.20 1 143 1072 73 GLY H H 8.496 0.02 1 144 1072 73 GLY N N 113.345 0.20 1 145 1073 74 ASP H H 8.350 0.02 1 146 1073 74 ASP N N 120.764 0.20 1 147 1074 75 GLY H H 8.564 0.02 1 148 1074 75 GLY N N 109.452 0.20 1 149 1075 76 MET H H 8.425 0.02 1 150 1075 76 MET N N 123.062 0.20 1 151 1076 77 GLY H H 8.572 0.02 1 152 1076 77 GLY N N 110.169 0.20 1 153 1077 78 ASP H H 8.368 0.02 1 154 1077 78 ASP N N 120.743 0.20 1 155 1078 79 SER H H 8.434 0.02 1 156 1078 79 SER N N 116.369 0.20 1 157 1079 80 GLU H H 8.505 0.02 1 158 1079 80 GLU N N 122.753 0.20 1 159 1080 81 ILE H H 8.184 0.02 1 160 1080 81 ILE N N 121.870 0.20 1 161 1081 82 THR H H 8.135 0.02 1 162 1081 82 THR N N 117.807 0.20 1 163 1082 83 ALA H H 8.200 0.02 1 164 1082 83 ALA N N 125.821 0.20 1 165 1083 84 ALA H H 8.179 0.02 1 166 1083 84 ALA N N 122.820 0.20 1 167 1084 85 ARG H H 8.218 0.02 1 168 1084 85 ARG N N 119.973 0.20 1 169 1085 86 ASN H H 8.350 0.02 1 170 1085 86 ASN N N 119.289 0.20 1 171 1086 87 TYR H H 8.194 0.02 1 172 1086 87 TYR N N 121.255 0.20 1 173 1087 88 ALA H H 8.193 0.02 1 174 1087 88 ALA N N 124.626 0.20 1 175 1088 89 GLU H H 8.293 0.02 1 176 1088 89 GLU N N 119.455 0.20 1 177 1089 90 GLY H H 8.310 0.02 1 178 1089 90 GLY N N 109.954 0.20 1 179 1090 91 ALA H H 8.217 0.02 1 180 1090 91 ALA N N 123.873 0.20 1 181 1091 92 GLY H H 8.457 0.02 1 182 1091 92 GLY N N 108.009 0.20 1 183 1094 95 PHE HD1 H 7.200 0.02 1 184 1094 95 PHE HD2 H 7.200 0.02 1 185 1094 95 PHE HE1 H 7.293 0.02 1 186 1094 95 PHE HE2 H 7.293 0.02 1 187 1094 95 PHE HZ H 7.248 0.02 1 188 1094 95 PHE CD1 C 132.007 0.20 1 189 1094 95 PHE CD2 C 132.007 0.20 1 190 1094 95 PHE CE1 C 131.369 0.20 1 191 1094 95 PHE CE2 C 131.369 0.20 1 192 1094 95 PHE CZ C 129.788 0.20 1 193 1097 98 ILE HG2 H 0.853 0.02 1 194 1097 98 ILE HD1 H 0.799 0.02 1 195 1097 98 ILE HG12 H 1.118 0.02 1 196 1097 98 ILE HG13 H 1.118 0.02 1 197 1097 98 ILE CG1 C 27.159 0.20 1 198 1097 98 ILE CG2 C 17.431 0.20 1 199 1097 98 ILE CD1 C 13.205 0.20 1 200 1099 100 ALA HB H 1.272 0.02 1 201 1099 100 ALA CB C 19.508 0.20 1 202 1100 101 LEU HD1 H 0.824 0.02 2 203 1100 101 LEU HD2 H 0.776 0.02 2 204 1100 101 LEU CD1 C 25.302 0.20 2 205 1100 101 LEU CD2 C 23.554 0.20 2 206 1102 103 LEU HD1 H 0.826 0.02 2 207 1102 103 LEU HD2 H 0.775 0.02 2 208 1102 103 LEU CD1 C 25.300 0.20 2 209 1102 103 LEU CD2 C 23.551 0.20 2 210 1106 107 TYR HD1 H 7.013 0.02 3 211 1106 107 TYR HE1 H 6.740 0.02 3 212 1106 107 TYR CD1 C 133.175 0.20 3 213 1106 107 TYR CE1 C 118.153 0.20 3 214 1108 109 HIS HD2 H 6.901 0.02 1 215 1108 109 HIS HE1 H 7.839 0.02 1 216 1108 109 HIS CD2 C 119.586 0.20 1 217 1108 109 HIS CE1 C 138.032 0.20 1 218 1110 111 ALA HB H 1.320 0.02 1 219 1110 111 ALA CB C 19.195 0.20 1 220 1111 112 LEU HD1 H 0.820 0.02 1 221 1111 112 LEU HD2 H 0.754 0.02 1 222 1111 112 LEU CD1 C 24.692 0.20 2 223 1111 112 LEU CD2 C 23.419 0.20 2 224 1125 126 ALA HB H 1.342 0.02 1 225 1125 126 ALA CB C 18.924 0.20 1 226 1126 127 ALA HB H 1.351 0.02 1 227 1126 127 ALA CB C 18.923 0.20 1 228 1128 129 ALA HB H 1.247 0.02 1 229 1128 129 ALA CB C 18.879 0.20 1 230 1129 130 THR HG2 H 1.080 0.02 1 231 1129 130 THR CG2 C 21.541 0.20 1 232 1130 131 ALA HB H 1.352 0.02 1 233 1130 131 ALA CB C 18.973 0.20 1 234 1131 132 TRP HD1 H 7.559 0.02 1 235 1131 132 TRP HE3 H 7.218 0.02 1 236 1131 132 TRP HZ2 H 7.440 0.02 1 237 1131 132 TRP HZ3 H 7.097 0.02 1 238 1131 132 TRP HH2 H 7.182 0.02 1 239 1131 132 TRP CD1 C 120.829 0.20 1 240 1131 132 TRP CE3 C 127.245 0.20 1 241 1131 132 TRP CZ2 C 114.600 0.20 1 242 1131 132 TRP CZ3 C 122.006 0.20 1 243 1131 132 TRP CH2 C 124.616 0.20 1 244 1134 135 GLY H H 8.324 0.02 1 245 1134 135 GLY N N 111.044 0.20 1 246 1135 136 VAL H H 7.986 0.02 1 247 1135 136 VAL N N 119.880 0.20 1 248 1136 137 LYS H H 8.485 0.02 1 249 1136 137 LYS N N 125.787 0.20 1 250 1137 138 THR H H 8.139 0.02 1 251 1137 138 THR N N 115.698 0.20 1 252 1138 139 TYR H H 8.431 0.02 1 253 1138 139 TYR N N 122.732 0.20 1 254 1139 140 ASN H H 8.487 0.02 1 255 1139 140 ASN N N 122.249 0.20 1 256 1140 141 GLY H H 7.820 0.02 1 257 1140 141 GLY N N 109.196 0.20 1 258 1141 142 ALA H H 8.139 0.02 1 259 1141 142 ALA N N 123.501 0.20 1 260 1142 143 LEU H H 8.258 0.02 1 261 1142 143 LEU N N 120.988 0.20 1 262 1143 144 GLY H H 8.396 0.02 1 263 1143 144 GLY N N 109.797 0.20 1 264 1144 145 VAL H H 7.918 0.02 1 265 1144 145 VAL N N 118.717 0.20 1 266 1145 146 ASP H H 8.531 0.02 1 267 1145 146 ASP N N 124.252 0.20 1 268 1146 147 ILE H H 8.108 0.02 1 269 1146 147 ILE N N 121.333 0.20 1 270 1147 148 HIS H H 8.523 0.02 1 271 1147 148 HIS N N 122.572 0.20 1 272 1148 149 GLU H H 8.093 0.02 1 273 1148 149 GLU N N 121.436 0.20 1 274 1149 150 LYS H H 8.480 0.02 1 275 1149 150 LYS N N 121.716 0.20 1 276 1150 151 ASP H H 8.282 0.02 1 277 1150 151 ASP N N 120.334 0.20 1 stop_ save_