data_19082 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Backbone and ILV methyl resonance assignments of E. coli thymidylate synthase bound to cofactor and a nucleotide analogue ; _BMRB_accession_number 19082 _BMRB_flat_file_name bmr19082.str _Entry_type original _Submission_date 2013-03-08 _Accession_date 2013-03-08 _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 Sapienza Paul J. . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 322 "13C chemical shifts" 774 "15N chemical shifts" 230 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2014-05-04 update BMRB 'update entry citation' 2013-06-04 original author 'original release' stop_ save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title 'Backbone and ILV methyl resonance assignments of E. coli thymidylate synthase bound to cofactor and a nucleotide analogue.' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 23653343 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Sapienza Paul J. . 2 Lee Andrew L. . stop_ _Journal_abbreviation 'Biomol. NMR Assignments' _Journal_name_full 'Biomolecular NMR assignments' _Journal_volume 8 _Journal_issue 1 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 195 _Page_last 199 _Year 2014 _Details . save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name thymidylate_synthase _Enzyme_commission_number 2.1.1.45 loop_ _Mol_system_component_name _Mol_label thymidylate_synthase $thymidylate_synthase '5-METHYL-5,6,7,8-TETRAHYDROFOLIC ACID' $entity_C2F 5-FLUORO-2'-DEOXYURIDINE-5'-MONOPHOSPHATE $entity_UFP stop_ _System_molecular_weight 62526 _System_physical_state native _System_oligomer_state ? _System_paramagnetic no _System_thiol_state . _Database_query_date . _Details 'Dimer covalently bound to inhibitor and cofactor' save_ ######################## # Monomeric polymers # ######################## save_thymidylate_synthase _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common thymidylate_synthase _Molecular_mass 30479.6 _Mol_thiol_state 'free and other bound' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 264 _Mol_residue_sequence ; MKQYLELMQKVLDEGTQKND RTGTGTLSIFGHQMRFNLQD GFPLVTTKRCHLRSIIHELL WFLQGDTNIAYLHENNVTIW DEWADENGDLGPVYGKQWRA WPTPDGRHIDQITTVLNQLK NDPDSRRIIVSAWNVGELDK MALAPCHAFFQFYVADGKLS CQLYQRSCDVFLGLPFNIAS YALLVHMMAQQCDLEVGDFV WTGGDTHLYSNHMDQTHLQL SREPRPLPKLIIKRKPESIF DYRFEDFEIEGYDPHPGIKA PVAI ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 1 MET 2 2 LYS 3 3 GLN 4 4 TYR 5 5 LEU 6 6 GLU 7 7 LEU 8 8 MET 9 9 GLN 10 10 LYS 11 11 VAL 12 12 LEU 13 13 ASP 14 14 GLU 15 15 GLY 16 16 THR 17 17 GLN 18 18 LYS 19 19 ASN 20 20 ASP 21 21 ARG 22 22 THR 23 23 GLY 24 24 THR 25 25 GLY 26 26 THR 27 27 LEU 28 28 SER 29 29 ILE 30 30 PHE 31 31 GLY 32 32 HIS 33 33 GLN 34 34 MET 35 35 ARG 36 36 PHE 37 37 ASN 38 38 LEU 39 39 GLN 40 40 ASP 41 41 GLY 42 42 PHE 43 43 PRO 44 44 LEU 45 45 VAL 46 46 THR 47 47 THR 48 48 LYS 49 49 ARG 50 50 CYS 51 51 HIS 52 52 LEU 53 53 ARG 54 54 SER 55 55 ILE 56 56 ILE 57 57 HIS 58 58 GLU 59 59 LEU 60 60 LEU 61 61 TRP 62 62 PHE 63 63 LEU 64 64 GLN 65 65 GLY 66 66 ASP 67 67 THR 68 68 ASN 69 69 ILE 70 70 ALA 71 71 TYR 72 72 LEU 73 73 HIS 74 74 GLU 75 75 ASN 76 76 ASN 77 77 VAL 78 78 THR 79 79 ILE 80 80 TRP 81 81 ASP 82 82 GLU 83 83 TRP 84 84 ALA 85 85 ASP 86 86 GLU 87 87 ASN 88 88 GLY 89 89 ASP 90 90 LEU 91 91 GLY 92 92 PRO 93 93 VAL 94 94 TYR 95 95 GLY 96 96 LYS 97 97 GLN 98 98 TRP 99 99 ARG 100 100 ALA 101 101 TRP 102 102 PRO 103 103 THR 104 104 PRO 105 105 ASP 106 106 GLY 107 107 ARG 108 108 HIS 109 109 ILE 110 110 ASP 111 111 GLN 112 112 ILE 113 113 THR 114 114 THR 115 115 VAL 116 116 LEU 117 117 ASN 118 118 GLN 119 119 LEU 120 120 LYS 121 121 ASN 122 122 ASP 123 123 PRO 124 124 ASP 125 125 SER 126 126 ARG 127 127 ARG 128 128 ILE 129 129 ILE 130 130 VAL 131 131 SER 132 132 ALA 133 133 TRP 134 134 ASN 135 135 VAL 136 136 GLY 137 137 GLU 138 138 LEU 139 139 ASP 140 140 LYS 141 141 MET 142 142 ALA 143 143 LEU 144 144 ALA 145 145 PRO 146 146 CYS 147 147 HIS 148 148 ALA 149 149 PHE 150 150 PHE 151 151 GLN 152 152 PHE 153 153 TYR 154 154 VAL 155 155 ALA 156 156 ASP 157 157 GLY 158 158 LYS 159 159 LEU 160 160 SER 161 161 CYS 162 162 GLN 163 163 LEU 164 164 TYR 165 165 GLN 166 166 ARG 167 167 SER 168 168 CYS 169 169 ASP 170 170 VAL 171 171 PHE 172 172 LEU 173 173 GLY 174 174 LEU 175 175 PRO 176 176 PHE 177 177 ASN 178 178 ILE 179 179 ALA 180 180 SER 181 181 TYR 182 182 ALA 183 183 LEU 184 184 LEU 185 185 VAL 186 186 HIS 187 187 MET 188 188 MET 189 189 ALA 190 190 GLN 191 191 GLN 192 192 CYS 193 193 ASP 194 194 LEU 195 195 GLU 196 196 VAL 197 197 GLY 198 198 ASP 199 199 PHE 200 200 VAL 201 201 TRP 202 202 THR 203 203 GLY 204 204 GLY 205 205 ASP 206 206 THR 207 207 HIS 208 208 LEU 209 209 TYR 210 210 SER 211 211 ASN 212 212 HIS 213 213 MET 214 214 ASP 215 215 GLN 216 216 THR 217 217 HIS 218 218 LEU 219 219 GLN 220 220 LEU 221 221 SER 222 222 ARG 223 223 GLU 224 224 PRO 225 225 ARG 226 226 PRO 227 227 LEU 228 228 PRO 229 229 LYS 230 230 LEU 231 231 ILE 232 232 ILE 233 233 LYS 234 234 ARG 235 235 LYS 236 236 PRO 237 237 GLU 238 238 SER 239 239 ILE 240 240 PHE 241 241 ASP 242 242 TYR 243 243 ARG 244 244 PHE 245 245 GLU 246 246 ASP 247 247 PHE 248 248 GLU 249 249 ILE 250 250 GLU 251 251 GLY 252 252 TYR 253 253 ASP 254 254 PRO 255 255 HIS 256 256 PRO 257 257 GLY 258 258 ILE 259 259 LYS 260 260 ALA 261 261 PRO 262 262 VAL 263 263 ALA 264 264 ILE stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-10-14 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 1AIQ "Crystal Structure Of Thymidylate Synthase R126e Mutant" 99.62 264 99.62 99.62 0.00e+00 PDB 1AJM "Crystal Structure Of Thymidylate Synthase R126e Mutant" 99.62 264 99.62 99.62 0.00e+00 PDB 1AN5 "E. Coli Thymidylate Synthase In Complex With Cb3717" 100.00 265 100.00 100.00 0.00e+00 PDB 1AOB "E. Coli Thymidylate Synthase Complexed With Ddurd" 100.00 264 100.00 100.00 0.00e+00 PDB 1AXW "E. Coli Thymidylate Synthase In Complex With Methotrexate (Mtx) And 2'-Deoxyuridine 5'-Monophosphate (Dump)" 100.00 265 100.00 100.00 0.00e+00 PDB 1BDU "E. Coli Thymidylate Synthase Complexed With Durd" 100.00 265 100.00 100.00 0.00e+00 PDB 1BID "E. Coli Thymidylate Synthase Complexed With Dump" 100.00 265 100.00 100.00 0.00e+00 PDB 1BJG "D221(169)n Mutant Does Not Promote Opening Of The Cofactor Imidazolidine Ring" 99.62 264 99.62 100.00 0.00e+00 PDB 1BQ1 "E. Coli Thymidylate Synthase Mutant N177a In Complex With Cb3717 And 2'-Deoxyuridine 5'-Monophosphate (Dump)" 99.62 264 99.62 99.62 0.00e+00 PDB 1BQ2 "E. Coli Thymidylate Synthase Mutant N177a" 99.62 264 99.62 99.62 0.00e+00 PDB 1DDU "E. Coli Thymidylate Synthase In Complex With Cb3717 And 2', 5'-Dideoxyuridine (Ddurd)" 100.00 265 100.00 100.00 0.00e+00 PDB 1DNA "D221(169)n Mutant Does Not Promote Opening Of The Cofactor Imidazolidine Ring" 99.62 264 99.62 100.00 0.00e+00 PDB 1EV5 "Crystal Structure Analysis Of Ala167 Mutant Of Escherichia Coli" 99.62 264 98.48 98.86 0.00e+00 PDB 1EV8 "Crystal Structure Analysis Of Cys167 Mutant Of Escherichia Coli" 99.62 264 98.10 98.10 0.00e+00 PDB 1EVF "Crystal Structure Analysis Of Cys167 Mutant Of Escherichia Coli" 99.62 264 98.10 98.48 0.00e+00 PDB 1EVG "Crystal Structure Analysis Of Cys167 Mutant Of Escherichia Coli With Unmodified Catalytic Cysteine" 99.62 264 98.86 99.24 0.00e+00 PDB 1F4B "Crystal Structure Of Escherichia Coli Thymidylate Synthase" 99.62 264 100.00 100.00 0.00e+00 PDB 1F4C "Crystal Structure Of E. Coli Thymidylate Synthase Covalently Modified At C146 With N-[tosyl-D-Prolinyl]amino-Ethanethiol" 99.62 264 100.00 100.00 0.00e+00 PDB 1F4D "Crystal Structure Of E. Coli Thymidylate Synthase C146s, L143c Covalently Modified At C143 With N-[tosyl-D-Prolinyl]amino- Etha" 99.62 264 99.24 99.24 0.00e+00 PDB 1F4E "Crystal Structure Of E. Coli Thymidylate Synthase Complexed With Tosyl-D-Proline" 99.62 264 100.00 100.00 0.00e+00 PDB 1F4F "Crystal Structure Of E. Coli Thymidylate Synthase Complexed With Sp- 722" 99.62 264 100.00 100.00 0.00e+00 PDB 1F4G "Crystal Structure Of E. Coli Thymidylate Synthase Complexed With Sp- 876" 99.62 264 99.62 99.62 0.00e+00 PDB 1FFL "Crystal Structure Of The Apo-Thymidylate Synthase R166q Mutant" 99.62 264 99.62 100.00 0.00e+00 PDB 1FWM "Crystal Structure Of The Thymidylate Synthase R166q Mutant" 99.62 264 99.62 100.00 0.00e+00 PDB 1JG0 "Crystal Structure Of Escherichia Coli Thymidylate Synthase Complexed With 2'-Deoxyuridine-5'-Monophosphate And N,O-Didansyl-L-T" 99.62 264 99.24 99.24 0.00e+00 PDB 1JTQ "E. Coli Ts Complex With Dump And The Pyrrolo(2,3-D)pyrimidine-Based Antifolate Ly341770" 99.62 264 100.00 100.00 0.00e+00 PDB 1JTU "E. Coli Thymidylate Synthase In A Complex With Dump And Ly338913, A Polyglutamylated Pyrrolo(2,3-d)pyrimidine-based Antifolate" 99.62 264 100.00 100.00 0.00e+00 PDB 1JUT "E. Coli Thymidylate Synthase Bound To Dump And Ly338529, A Pyrrolo(2, 3-d)pyrimidine-based Antifolate" 99.62 264 100.00 100.00 0.00e+00 PDB 1KCE "E. Coli Thymidylate Synthase Mutant E58q In Complex With Cb3717 And 2'-Deoxyuridine 5'-Monophosphate (Dump)" 99.62 264 100.00 100.00 0.00e+00 PDB 1KZI "Crystal Structure Of EctsDUMPTHF COMPLEX" 99.62 264 100.00 100.00 0.00e+00 PDB 1KZJ "Crystal Structure Of Ects W80g/dump/cb3717 Complex" 99.62 264 99.62 99.62 0.00e+00 PDB 1NCE "Crystal Structure Of A Ternary Complex Of E. Coli Thymidylate Synthase D169c With Dump And The Antifolate Cb3717" 99.62 264 99.62 99.62 0.00e+00 PDB 1QQQ "Crystal Structure Analysis Of Ser254 Mutant Of Escherichia Coli Thymidylate Synthase" 99.62 264 98.10 98.10 0.00e+00 PDB 1SYN "E. Coli Thymidylate Synthase In Complex With Bw1843u89 And 2'-Deoxyuridine 5'-Monophosphate (Dump)" 100.00 265 100.00 100.00 0.00e+00 PDB 1TDU "E. Coli Thymidylate Synthase In Complex With Cb3717 And 2'- Deoxyuridine (durd)" 100.00 265 100.00 100.00 0.00e+00 PDB 1TJS "E. Coli Thymidylate Synthase" 100.00 265 100.00 100.00 0.00e+00 PDB 1TLC "Thymidylate Synthase Complexed With Dgmp And Folate Analog 1843u89" 100.00 265 100.00 100.00 0.00e+00 PDB 1TLS "Thymidylate Synthase Ternary Complex With Fdump And Methylenetetrahydrofolate" 99.62 264 100.00 100.00 0.00e+00 PDB 1TRG "E. Coli Thymidylate Synthase In Symmetric Complex With Cb3717 And 2'- Deoxyuridine 5'-Monophosphate (Dump)" 100.00 265 100.00 100.00 0.00e+00 PDB 1TSD "Thymidylate Synthase Complex With 2'-deoxyuridine 5'- Monophosphate (dump) And Folate Analog 1843u89" 100.00 265 100.00 100.00 0.00e+00 PDB 1TSN "Thymidylate Synthase Ternary Complex With Fdump And Methylenetetrahydrofolate" 99.62 264 100.00 100.00 0.00e+00 PDB 1TYS "Water-Mediated Substrate(Slash)product Discrimination: The Product Complex Of Thymidylate Synthase At 1.83 Angstroms" 99.62 264 99.62 99.62 0.00e+00 PDB 1ZPR "E. Coli Thymidylate Synthase Mutant E58q In Complex With Cb3717 And 2'-Deoxyuridine 5'-Monophosphate (Dump)" 99.62 264 99.62 100.00 0.00e+00 PDB 2A9W "E. Coli Ts Complexed With Dump And Inhibitor Ga9" 99.62 264 100.00 100.00 0.00e+00 PDB 2BBQ "Structural Basis For Recognition Of Polyglutamyl Folates By Thymidylate Synthase" 100.00 264 100.00 100.00 0.00e+00 PDB 2FTN "E. Coli Thymidylate Synthase Y94f Mutant" 99.62 264 99.62 100.00 0.00e+00 PDB 2FTO "Y94f Mutant Of Thymidylate Synthase Bound To Thymidine-5'-Phosphate And 10-Propargyl-5,8-Dideazafolid Acid" 99.62 264 99.62 100.00 0.00e+00 PDB 2FTQ "E. Coli Thymidylate Synthase At 1.8 A Resolution" 99.62 264 100.00 100.00 0.00e+00 PDB 2G8M "Escherichia Coli Thymidylate Synthase Y209w In Complex With Substrate, Dump, And A Cofactor Analog, Cb3717" 99.62 264 99.62 100.00 0.00e+00 PDB 2G8X "Escherichia Coli Y209w Apoprotein" 99.62 264 99.62 100.00 0.00e+00 PDB 2KCE "Binding Of The Anticancer Drug Zd1694 To E. Coli Thymidylate Synthase: Assessing Specificity And Affinity" 100.00 264 100.00 100.00 0.00e+00 PDB 2TSC "Structure, Multiple Site Binding, And Segmental Accomodation In Thymidylate Synthase On Binding DUMP AND An Anti-Folate" 100.00 264 99.62 99.62 0.00e+00 PDB 2VET "Crystal Structure Of The Thymidylate Synthase K48q Complexed With Dump" 100.00 264 99.62 100.00 0.00e+00 PDB 2VF0 "Crystal Structure Of The Thymidylate Synthase K48q Complexed With 5no2dump And Bw1843u89" 99.62 264 99.62 100.00 0.00e+00 PDB 3B5B "Crystal Structure Of The Thymidylate Synthase K48q" 100.00 264 99.62 100.00 0.00e+00 PDB 3B9H "E. Coli Thymidylate Synthase Complexed With 5-Nitro-2'-Deoxy Uridine" 99.62 264 100.00 100.00 0.00e+00 PDB 3BFI "E. Coli Thymidylate Synthase Y209m Mutant Complexed With 5-nitro-dump" 99.62 264 99.62 99.62 0.00e+00 PDB 3BGX "E. Coli Thymidylate Synthase C146s Mutant Complexed With Dtmp And Mtf" 99.62 264 99.62 99.62 0.00e+00 PDB 3BHL "E.Coli Thymidylate Synthase Complexes With 5-No2dump And Tetrahydrofolate At 1.4 A Resolution" 99.62 264 100.00 100.00 0.00e+00 PDB 3BHR "E. Coli Ts Complexed With 5-No2dump And Tetrahydrofolate At 1.9 A Resolution (Space Group 152)" 99.62 264 100.00 100.00 0.00e+00 PDB 3TMS "Plastic Adaptation Toward Mutations In Proteins: Structural Comparison Of Thymidylate Synthases" 100.00 264 100.00 100.00 0.00e+00 PDB 4GEV "E. Coli Thymidylate Synthase Y209w Variant In Complex With Substrate And A Cofactor Analog" 99.62 264 99.62 100.00 0.00e+00 PDB 4ISK "Crystal Structure Of E.coli Thymidylate Synthase With Dump And The Bgc 945 Inhibitor" 99.62 264 100.00 100.00 0.00e+00 PDB 4KNZ "Thymidylate Synthase Ternary Complex With Dump And Cb3717" 99.62 264 100.00 100.00 0.00e+00 PDB 4LRR "Ternary Complex Between E. Coli Thymidylate Synthase, Dump, And F9" 100.00 265 99.62 99.62 0.00e+00 DBJ BAB37107 "thymidylate synthetase [Escherichia coli O157:H7 str. Sakai]" 100.00 264 100.00 100.00 0.00e+00 DBJ BAE76896 "thymidylate synthetase [Escherichia coli str. K12 substr. W3110]" 100.00 264 100.00 100.00 0.00e+00 DBJ BAG78608 "thymidylate synthase [Escherichia coli SE11]" 100.00 264 100.00 100.00 0.00e+00 DBJ BAI27090 "thymidylate synthetase ThyA [Escherichia coli O26:H11 str. 11368]" 100.00 264 100.00 100.00 0.00e+00 DBJ BAI32133 "thymidylate synthetase ThyA [Escherichia coli O103:H2 str. 12009]" 100.00 264 100.00 100.00 0.00e+00 EMBL CAA27600 "thyA (C-terminal) [Escherichia coli]" 76.52 202 100.00 100.00 1.26e-148 EMBL CAP77283 "Thymidylate synthase [Escherichia coli LF82]" 100.00 264 100.00 100.00 0.00e+00 EMBL CAQ33153 "thymidylate synthase [Escherichia coli BL21(DE3)]" 100.00 264 99.62 99.62 0.00e+00 EMBL CAQ90255 "thymidylate synthetase [Escherichia fergusonii ATCC 35469]" 100.00 264 99.24 99.62 0.00e+00 EMBL CAQ99753 "thymidylate synthetase [Escherichia coli IAI1]" 100.00 264 100.00 100.00 0.00e+00 GB AAA24675 "thymidylate synthase [Escherichia coli]" 100.00 264 100.00 100.00 0.00e+00 GB AAB40474 "thymidylate synthetase [Escherichia coli str. K-12 substr. MG1655]" 100.00 264 99.62 99.62 0.00e+00 GB AAC75866 "thymidylate synthetase [Escherichia coli str. K-12 substr. MG1655]" 100.00 264 100.00 100.00 0.00e+00 GB AAG57938 "thymidylate synthetase [Escherichia coli O157:H7 str. EDL933]" 100.00 264 100.00 100.00 0.00e+00 GB AAN41256 "mutant thymidilate synthetase [Escherichia coli]" 100.00 264 99.62 99.62 0.00e+00 REF NP_311711 "thymidylate synthase [Escherichia coli O157:H7 str. Sakai]" 100.00 264 100.00 100.00 0.00e+00 REF NP_417304 "thymidylate synthetase [Escherichia coli str. K-12 substr. MG1655]" 100.00 264 100.00 100.00 0.00e+00 REF NP_708616 "thymidylate synthase [Shigella flexneri 2a str. 301]" 100.00 264 99.62 100.00 0.00e+00 REF WP_000607253 "thymidylate synthase, partial [Escherichia coli]" 93.56 247 100.00 100.00 0.00e+00 REF WP_000816225 "thymidylate synthase [Escherichia coli]" 100.00 264 99.62 99.62 0.00e+00 SP A1AF39 "RecName: Full=Thymidylate synthase; Short=TS; Short=TSase" 100.00 264 100.00 100.00 0.00e+00 SP A7ZQT3 "RecName: Full=Thymidylate synthase; Short=TS; Short=TSase" 100.00 264 100.00 100.00 0.00e+00 SP A8A3W0 "RecName: Full=Thymidylate synthase; Short=TS; Short=TSase" 100.00 264 99.62 100.00 0.00e+00 SP B1IU17 "RecName: Full=Thymidylate synthase; Short=TS; Short=TSase" 100.00 264 99.62 100.00 0.00e+00 SP B7LF04 "RecName: Full=Thymidylate synthase; Short=TS; Short=TSase" 100.00 264 100.00 100.00 0.00e+00 stop_ save_ ############# # Ligands # ############# save_C2F _Saveframe_category ligand _Mol_type "non-polymer (NON-POLYMER)" _Name_common '5-METHYL-5,6,7,8-TETRAHYDROFOLIC ACID' _BMRB_code C2F _PDB_code C2F _Molecular_mass 459.456 _Mol_charge 0 _Mol_paramagnetic no _Mol_aromatic yes _Details . loop_ _Atom_name _PDB_atom_name _Atom_type _Atom_chirality _Atom_charge _Atom_oxidation_number _Atom_unpaired_electrons N1 N1 N . 0 . ? C2 C2 C . 0 . ? NA2 NA2 N . 0 . ? N3 N3 N . 0 . ? C4 C4 C . 0 . ? O4 O4 O . 0 . ? C4A C4A C . 0 . ? N5 N5 N . 0 . ? C6 C6 C . 0 . ? C7 C7 C . 0 . ? N8 N8 N . 0 . ? C8A C8A C . 0 . ? C9 C9 C . 0 . ? N10 N10 N . 0 . ? C11 C11 C . 0 . ? C12 C12 C . 0 . ? C13 C13 C . 0 . ? C14 C14 C . 0 . ? C15 C15 C . 0 . ? C16 C16 C . 0 . ? C17 C17 C . 0 . ? C C C . 0 . ? O O O . 0 . ? N N N . 0 . ? CA CA C . 0 . ? CB CB C . 0 . ? CG CG C . 0 . ? CD CD C . 0 . ? OE1 OE1 O . 0 . ? OE2 OE2 O . 0 . ? CT CT C . 0 . ? O1 O1 O . 0 . ? O2 O2 O . 0 . ? HN21 HN21 H . 0 . ? HN22 HN22 H . 0 . ? HN3 HN3 H . 0 . ? H6 H6 H . 0 . ? H71 H71 H . 0 . ? H72 H72 H . 0 . ? HN8 HN8 H . 0 . ? H91 H91 H . 0 . ? H92 H92 H . 0 . ? HN1 HN1 H . 0 . ? H111 H111 H . 0 . ? H112 H112 H . 0 . ? H113 H113 H . 0 . ? H13 H13 H . 0 . ? H14 H14 H . 0 . ? H16 H16 H . 0 . ? H17 H17 H . 0 . ? HN HN H . 0 . ? HA HA H . 0 . ? HB1 HB1 H . 0 . ? HB2 HB2 H . 0 . ? HG1 HG1 H . 0 . ? HG2 HG2 H . 0 . ? HOE2 HOE2 H . 0 . ? HO2 HO2 H . 0 . ? stop_ loop_ _Bond_order _Bond_atom_one_atom_name _Bond_atom_two_atom_name _PDB_bond_atom_one_atom_name _PDB_bond_atom_two_atom_name DOUB N1 C2 ? ? SING N1 C8A ? ? SING C2 NA2 ? ? SING C2 N3 ? ? SING NA2 HN21 ? ? SING NA2 HN22 ? ? SING N3 C4 ? ? SING N3 HN3 ? ? DOUB C4 O4 ? ? SING C4 C4A ? ? SING C4A N5 ? ? DOUB C4A C8A ? ? SING N5 C6 ? ? SING N5 C11 ? ? SING C6 C7 ? ? SING C6 C9 ? ? SING C6 H6 ? ? SING C7 N8 ? ? SING C7 H71 ? ? SING C7 H72 ? ? SING N8 C8A ? ? SING N8 HN8 ? ? SING C9 N10 ? ? SING C9 H91 ? ? SING C9 H92 ? ? SING N10 C15 ? ? SING N10 HN1 ? ? SING C11 H111 ? ? SING C11 H112 ? ? SING C11 H113 ? ? DOUB C12 C13 ? ? SING C12 C17 ? ? SING C12 C ? ? SING C13 C14 ? ? SING C13 H13 ? ? DOUB C14 C15 ? ? SING C14 H14 ? ? SING C15 C16 ? ? DOUB C16 C17 ? ? SING C16 H16 ? ? SING C17 H17 ? ? DOUB C O ? ? SING C N ? ? SING N CA ? ? SING N HN ? ? SING CA CB ? ? SING CA CT ? ? SING CA HA ? ? SING CB CG ? ? SING CB HB1 ? ? SING CB HB2 ? ? SING CG CD ? ? SING CG HG1 ? ? SING CG HG2 ? ? DOUB CD OE1 ? ? SING CD OE2 ? ? SING OE2 HOE2 ? ? DOUB CT O1 ? ? SING CT O2 ? ? SING O2 HO2 ? ? stop_ _Mol_thiol_state 'not present' _Sequence_homology_query_date . save_ save_UFP _Saveframe_category ligand _Mol_type "non-polymer (DNA LINKING)" _Name_common 5-FLUORO-2'-DEOXYURIDINE-5'-MONOPHOSPHATE _BMRB_code UFP _PDB_code UFP _Molecular_mass 326.172 _Mol_charge 0 _Mol_paramagnetic no _Mol_aromatic no _Details . loop_ _Atom_name _PDB_atom_name _Atom_type _Atom_chirality _Atom_charge _Atom_oxidation_number _Atom_unpaired_electrons N1 N1 N . 0 . ? C2 C2 C . 0 . ? N3 N3 N . 0 . ? C4 C4 C . 0 . ? C5 C5 C . 0 . ? C6 C6 C . 0 . ? O2 O2 O . 0 . ? O4 O4 O . 0 . ? F5 F5 F . 0 . ? C1' C1' C . 0 . ? C2' C2' C . 0 . ? C3' C3' C . 0 . ? C4' C4' C . 0 . ? O3' O3' O . 0 . ? O4' O4' O . 0 . ? C5' C5' C . 0 . ? O5' O5' O . 0 . ? P P P . 0 . ? O1P O1P O . 0 . ? O2P O2P O . 0 . ? O3P O3P O . 0 . ? HN3 HN3 H . 0 . ? H6 H6 H . 0 . ? H1' H1' H . 0 . ? H2'1 H2'1 H . 0 . ? H2'2 H2'2 H . 0 . ? H3' H3' H . 0 . ? H4' H4' H . 0 . ? HO3' HO3' H . 0 . ? H5'1 H5'1 H . 0 . ? H5'2 H5'2 H . 0 . ? HOP2 HOP2 H . 0 . ? HOP3 HOP3 H . 0 . ? stop_ loop_ _Bond_order _Bond_atom_one_atom_name _Bond_atom_two_atom_name _PDB_bond_atom_one_atom_name _PDB_bond_atom_two_atom_name SING N1 C2 ? ? SING N1 C6 ? ? SING N1 C1' ? ? SING C2 N3 ? ? DOUB C2 O2 ? ? SING N3 C4 ? ? SING N3 HN3 ? ? SING C4 C5 ? ? DOUB C4 O4 ? ? DOUB C5 C6 ? ? SING C5 F5 ? ? SING C6 H6 ? ? SING C1' C2' ? ? SING C1' O4' ? ? SING C1' H1' ? ? SING C2' C3' ? ? SING C2' H2'1 ? ? SING C2' H2'2 ? ? SING C3' C4' ? ? SING C3' O3' ? ? SING C3' H3' ? ? SING C4' O4' ? ? SING C4' C5' ? ? SING C4' H4' ? ? SING O3' HO3' ? ? SING C5' O5' ? ? SING C5' H5'1 ? ? SING C5' H5'2 ? ? SING O5' P ? ? DOUB P O1P ? ? SING P O2P ? ? SING P O3P ? ? SING O2P HOP2 ? ? SING O3P HOP3 ? ? stop_ _Mol_thiol_state 'not present' _Sequence_homology_query_date . save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $thymidylate_synthase Enterobacteria 562 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 $thymidylate_synthase 'recombinant technology' . Escherichia coli . pET21a 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 $thymidylate_synthase 0.5 mM 'U-[2H, 13C, 15N]' H2O 95 % 'natural abundance' D2O 5 % 'natural abundance' stop_ save_ save_sample_2 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $thymidylate_synthase 0.5 mM 'U-[2H, 13C, 15N]' H2O 95 % 'natural abundance' D2O 5 % 'natural abundance' stop_ save_ save_sample_3 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $thymidylate_synthase 0.5 mM 'U-[2H, 15N]' D2O 99.8 % 'natural abundance' stop_ save_ save_sample_4 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $thymidylate_synthase . mM U-[13C] H2O 95 % 'natural abundance' D2O 5 % 'natural abundance' stop_ save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model INOVA _Field_strength 500 _Details . save_ save_spectrometer_2 _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model INOVA _Field_strength 700 _Details . save_ save_spectrometer_3 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model Avance _Field_strength 950 _Details . save_ ############################# # NMR applied experiments # ############################# save_2D_1H-15N_HSQC_1 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-15N HSQC' _Sample_label $sample_1 save_ save_3D_HNCO_2 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCO' _Sample_label $sample_1 save_ save_3D_HN(CA)CO_3 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HN(CA)CO' _Sample_label $sample_1 save_ save_3D_HNCA_4 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCA' _Sample_label $sample_1 save_ save_3D_HN(CO)CA_5 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HN(CO)CA' _Sample_label $sample_1 save_ save_3D_HN(CA)CB_6 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HN(CA)CB' _Sample_label $sample_1 save_ save_3D_HN(COCA)CB_7 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HN(COCA)CB' _Sample_label $sample_1 save_ save_2D_1H-13C_HSQC_aliphatic_8 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-13C HSQC aliphatic' _Sample_label $sample_4 save_ save_3D_HMCM[CG]CBCA_9 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HMCM[CG]CBCA' _Sample_label $sample_2 save_ save_HMCM(CGCBCA)CO_10 _Saveframe_category NMR_applied_experiment _Experiment_name HMCM(CGCBCA)CO _Sample_label $sample_2 save_ save_3D_[13C-F1,_13C-F2]-edited_NOESY_11 _Saveframe_category NMR_applied_experiment _Experiment_name '3D [13C-F1, 13C-F2]-edited NOESY' _Sample_label $sample_3 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' 0.175 . M pH 7.5 . pH pressure 1 . atm temperature 25 . K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference_1 _Saveframe_category chemical_shift_reference _Details . loop_ _Mol_common_name _Atom_type _Atom_isotope_number _Atom_group _Chem_shift_units _Chem_shift_value _Reference_method _Reference_type _External_reference_sample_geometry _External_reference_location _External_reference_axis _Indirect_shift_ratio DSS C 13 'methyl protons' ppm 0.00 na indirect . . . 0.251449530 DSS H 1 'methyl protons' ppm 0.00 internal direct . . . 1.000000000 DSS N 15 'methyl protons' ppm 0.00 na indirect . . . 0.101329118 stop_ save_ ################################### # Assigned chemical shift lists # ################################### ################################################################### # Chemical Shift Ambiguity Index Value Definitions # # # # The values other than 1 are used for those atoms with different # # chemical shifts that cannot be assigned to stereospecific atoms # # or to specific residues or chains. # # # # Index Value Definition # # # # 1 Unique (including isolated methyl protons, # # geminal atoms, and geminal methyl # # groups with identical chemical shifts) # # (e.g. ILE HD11, HD12, HD13 protons) # # 2 Ambiguity of geminal atoms or geminal methyl # # proton groups (e.g. ASP HB2 and HB3 # # protons, LEU CD1 and CD2 carbons, or # # LEU HD11, HD12, HD13 and HD21, HD22, # # HD23 methyl protons) # # 3 Aromatic atoms on opposite sides of # # symmetrical rings (e.g. TYR HE1 and HE2 # # protons) # # 4 Intraresidue ambiguities (e.g. LYS HG and # # HD protons or TRP HZ2 and HZ3 protons) # # 5 Interresidue ambiguities (LYS 12 vs. LYS 27) # # 6 Intermolecular ambiguities (e.g. ASP 31 CA # # in monomer 1 and ASP 31 CA in monomer 2 # # of an asymmetrical homodimer, duplex # # DNA assignments, or other assignments # # that may apply to atoms in one or more # # molecule in the molecular assembly) # # 9 Ambiguous, specific ambiguity not defined # # # ################################################################### save_assigned_chem_shift_list_1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Experiment_label '2D 1H-15N HSQC' '3D HNCO' '3D HN(CA)CO' '3D HNCA' '3D HN(CO)CA' '3D HN(CA)CB' '3D HN(COCA)CB' '2D 1H-13C HSQC aliphatic' '3D HMCM[CG]CBCA' HMCM(CGCBCA)CO '3D [13C-F1, 13C-F2]-edited NOESY' stop_ loop_ _Sample_label $sample_1 $sample_4 $sample_2 $sample_3 stop_ _Sample_conditions_label $sample_conditions_1 _Chem_shift_reference_set_label $chemical_shift_reference_1 _Mol_system_component_name thymidylate_synthase _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 2 2 LYS C C 178.4014 0.11 1 2 3 3 GLN H H 10.0171 0.01 1 3 3 3 GLN C C 178.5089 0.11 1 4 3 3 GLN CA C 59.2444 0.11 1 5 3 3 GLN N N 116.3613 0.07 1 6 4 4 TYR H H 6.8245 0.01 1 7 4 4 TYR C C 175.5143 0.11 1 8 4 4 TYR CA C 60.7566 0.11 1 9 4 4 TYR CB C 39.8983 0.11 1 10 4 4 TYR N N 118.0248 0.07 1 11 5 5 LEU H H 8.4870 0.01 1 12 5 5 LEU HD1 H 1.0360 0.01 2 13 5 5 LEU HD2 H 1.0026 0.01 2 14 5 5 LEU C C 179.8672 0.11 1 15 5 5 LEU CA C 57.4570 0.11 1 16 5 5 LEU CB C 39.7233 0.11 1 17 5 5 LEU CD1 C 25.9348 0.11 2 18 5 5 LEU CD2 C 21.6134 0.11 2 19 5 5 LEU N N 120.4470 0.07 1 20 6 6 GLU H H 8.1764 0.01 1 21 6 6 GLU C C 179.5479 0.11 1 22 6 6 GLU CA C 59.0433 0.11 1 23 6 6 GLU CB C 28.5682 0.11 1 24 6 6 GLU N N 118.9713 0.07 1 25 7 7 LEU H H 7.0880 0.01 1 26 7 7 LEU HD1 H -0.0280 0.01 2 27 7 7 LEU HD2 H 0.3413 0.01 2 28 7 7 LEU C C 176.9794 0.11 1 29 7 7 LEU CA C 57.0651 0.11 1 30 7 7 LEU CB C 38.7566 0.11 1 31 7 7 LEU CD1 C 20.3290 0.11 2 32 7 7 LEU CD2 C 26.2133 0.11 2 33 7 7 LEU N N 122.2916 0.07 1 34 8 8 MET H H 7.6970 0.01 1 35 8 8 MET C C 176.8254 0.11 1 36 8 8 MET CA C 60.7666 0.11 1 37 8 8 MET CB C 33.9567 0.11 1 38 8 8 MET N N 118.8879 0.07 1 39 9 9 GLN H H 7.7938 0.01 1 40 9 9 GLN C C 176.6110 0.11 1 41 9 9 GLN CA C 57.3512 0.11 1 42 9 9 GLN CB C 28.3189 0.11 1 43 9 9 GLN N N 115.9258 0.07 1 44 10 10 LYS H H 7.6975 0.01 1 45 10 10 LYS C C 178.4686 0.11 1 46 10 10 LYS CA C 59.3443 0.11 1 47 10 10 LYS CB C 31.9434 0.11 1 48 10 10 LYS N N 121.4571 0.07 1 49 11 11 VAL H H 8.1530 0.01 1 50 11 11 VAL HG1 H 0.7910 0.01 2 51 11 11 VAL HG2 H 0.6980 0.01 2 52 11 11 VAL C C 178.4838 0.11 1 53 11 11 VAL CA C 66.5325 0.11 1 54 11 11 VAL CB C 29.9258 0.11 1 55 11 11 VAL CG1 C 23.3260 0.11 2 56 11 11 VAL CG2 C 22.1140 0.11 2 57 11 11 VAL N N 119.8126 0.07 1 58 12 12 LEU H H 7.4072 0.01 1 59 12 12 LEU HD1 H 0.5445 0.01 2 60 12 12 LEU HD2 H 0.6334 0.01 2 61 12 12 LEU C C 179.9475 0.11 1 62 12 12 LEU CA C 57.6672 0.11 1 63 12 12 LEU CB C 40.6580 0.11 1 64 12 12 LEU CD1 C 25.6944 0.11 2 65 12 12 LEU CD2 C 23.6958 0.11 2 66 12 12 LEU N N 118.4070 0.07 1 67 13 13 ASP H H 8.4043 0.01 1 68 13 13 ASP C C 178.4500 0.11 1 69 13 13 ASP CA C 56.6320 0.11 1 70 13 13 ASP CB C 40.9426 0.11 1 71 13 13 ASP N N 118.4813 0.07 1 72 14 14 GLU H H 8.7391 0.01 1 73 14 14 GLU CA C 55.0852 0.11 1 74 14 14 GLU CB C 30.5957 0.11 1 75 14 14 GLU N N 116.4381 0.07 1 76 15 15 GLY H H 8.2150 0.01 1 77 15 15 GLY C C 173.2029 0.11 1 78 15 15 GLY CA C 45.7813 0.11 1 79 15 15 GLY N N 110.9534 0.07 1 80 16 16 THR H H 8.9900 0.01 1 81 16 16 THR C C 174.2754 0.11 1 82 16 16 THR CA C 60.3220 0.11 1 83 16 16 THR CB C 70.0928 0.11 1 84 16 16 THR N N 119.7316 0.07 1 85 17 17 GLN H H 8.5838 0.01 1 86 17 17 GLN C C 175.6700 0.11 1 87 17 17 GLN CA C 56.1101 0.11 1 88 17 17 GLN CB C 27.4555 0.11 1 89 17 17 GLN N N 127.5619 0.07 1 90 18 18 LYS H H 8.8317 0.01 1 91 18 18 LYS C C 176.4496 0.11 1 92 18 18 LYS CA C 55.0465 0.11 1 93 18 18 LYS CB C 35.4006 0.11 1 94 18 18 LYS N N 128.8647 0.07 1 95 19 19 ASN H H 8.4946 0.01 1 96 19 19 ASN C C 173.1677 0.11 1 97 19 19 ASN CA C 52.5609 0.11 1 98 19 19 ASN CB C 38.6192 0.11 1 99 19 19 ASN N N 123.1751 0.07 1 100 20 20 ASP H H 8.3903 0.01 1 101 20 20 ASP C C 175.5103 0.11 1 102 20 20 ASP CA C 52.7851 0.11 1 103 20 20 ASP CB C 45.9802 0.11 1 104 20 20 ASP N N 117.7085 0.07 1 105 21 21 ARG H H 8.7711 0.01 1 106 21 21 ARG C C 177.0363 0.11 1 107 21 21 ARG CA C 58.5569 0.11 1 108 21 21 ARG CB C 30.8679 0.11 1 109 21 21 ARG N N 123.8360 0.07 1 110 22 22 THR H H 8.2146 0.01 1 111 22 22 THR CA C 63.2532 0.11 1 112 22 22 THR CB C 70.5745 0.11 1 113 22 22 THR N N 108.2560 0.07 1 114 23 23 GLY H H 7.9963 0.01 1 115 23 23 GLY C C 174.3307 0.11 1 116 23 23 GLY CA C 45.2857 0.11 1 117 23 23 GLY N N 111.1249 0.07 1 118 24 24 THR H H 8.2641 0.01 1 119 24 24 THR CA C 65.5546 0.11 1 120 24 24 THR CB C 68.6249 0.11 1 121 24 24 THR N N 121.6001 0.07 1 122 25 25 GLY H H 9.1689 0.01 1 123 25 25 GLY C C 173.3056 0.11 1 124 25 25 GLY CA C 44.0700 0.11 1 125 25 25 GLY N N 115.0089 0.07 1 126 26 26 THR H H 8.5460 0.01 1 127 26 26 THR C C 174.6232 0.11 1 128 26 26 THR CA C 58.5062 0.11 1 129 26 26 THR CB C 72.4202 0.11 1 130 26 26 THR N N 111.8390 0.07 1 131 27 27 LEU H H 8.3829 0.01 1 132 27 27 LEU HD1 H 0.8468 0.01 2 133 27 27 LEU HD2 H 0.7757 0.01 2 134 27 27 LEU C C 176.7366 0.11 1 135 27 27 LEU CA C 54.0193 0.11 1 136 27 27 LEU CB C 43.8719 0.11 1 137 27 27 LEU CD1 C 24.9658 0.11 2 138 27 27 LEU CD2 C 24.0297 0.11 2 139 27 27 LEU N N 119.8396 0.07 1 140 28 28 SER H H 8.7224 0.01 1 141 28 28 SER C C 174.4795 0.11 1 142 28 28 SER CA C 56.8579 0.11 1 143 28 28 SER CB C 64.7448 0.11 1 144 28 28 SER N N 115.5310 0.07 1 145 29 29 ILE H H 8.8441 0.01 1 146 29 29 ILE HD1 H 0.4669 0.01 1 147 29 29 ILE C C 172.9501 0.11 1 148 29 29 ILE CA C 59.2378 0.11 1 149 29 29 ILE CB C 40.1152 0.11 1 150 29 29 ILE CD1 C 13.6016 0.11 1 151 29 29 ILE N N 121.2312 0.07 1 152 30 30 PHE H H 8.3057 0.01 1 153 30 30 PHE C C 175.3347 0.11 1 154 30 30 PHE CA C 54.8685 0.11 1 155 30 30 PHE CB C 39.2628 0.11 1 156 30 30 PHE N N 120.7416 0.07 1 157 31 31 GLY H H 7.2607 0.01 1 158 31 31 GLY C C 171.0837 0.11 1 159 31 31 GLY CA C 44.5900 0.11 1 160 31 31 GLY N N 114.8438 0.07 1 161 32 32 HIS H H 7.3311 0.01 1 162 32 32 HIS C C 172.4678 0.11 1 163 32 32 HIS CA C 55.8210 0.11 1 164 32 32 HIS CB C 33.8391 0.11 1 165 32 32 HIS N N 123.2518 0.07 1 166 33 33 GLN H H 6.9756 0.01 1 167 33 33 GLN C C 173.1246 0.11 1 168 33 33 GLN CA C 54.1322 0.11 1 169 33 33 GLN CB C 32.6085 0.11 1 170 33 33 GLN N N 127.5817 0.07 1 171 34 34 MET H H 9.2245 0.01 1 172 34 34 MET C C 172.5804 0.11 1 173 34 34 MET CA C 53.9992 0.11 1 174 34 34 MET CB C 36.1491 0.11 1 175 34 34 MET N N 122.8104 0.07 1 176 35 35 ARG H H 8.3282 0.01 1 177 35 35 ARG C C 174.0590 0.11 1 178 35 35 ARG CA C 54.6282 0.11 1 179 35 35 ARG CB C 33.4294 0.11 1 180 35 35 ARG N N 120.5658 0.07 1 181 36 36 PHE H H 9.2107 0.01 1 182 36 36 PHE C C 174.4195 0.11 1 183 36 36 PHE CA C 56.0674 0.11 1 184 36 36 PHE CB C 39.2369 0.11 1 185 36 36 PHE N N 124.6428 0.07 1 186 37 37 ASN H H 9.1632 0.01 1 187 37 37 ASN C C 179.1264 0.11 1 188 37 37 ASN CA C 52.5748 0.11 1 189 37 37 ASN CB C 36.6977 0.11 1 190 37 37 ASN N N 124.3569 0.07 1 191 38 38 LEU H H 9.3367 0.01 1 192 38 38 LEU C C 179.2667 0.11 1 193 38 38 LEU N N 131.1856 0.07 1 194 39 39 GLN C C 177.6604 0.11 1 195 39 39 GLN CA C 57.4787 0.11 1 196 39 39 GLN CB C 26.7464 0.11 1 197 40 40 ASP H H 7.7994 0.01 1 198 40 40 ASP C C 176.0832 0.11 1 199 40 40 ASP CA C 55.2804 0.11 1 200 40 40 ASP CB C 39.9216 0.11 1 201 40 40 ASP N N 119.2741 0.07 1 202 41 41 GLY H H 6.8564 0.01 1 203 41 41 GLY CA C 43.4991 0.11 1 204 41 41 GLY N N 107.0345 0.07 1 205 42 42 PHE H H 8.8755 0.01 1 206 42 42 PHE C C 174.8595 0.11 1 207 42 42 PHE CA C 55.1990 0.11 1 208 42 42 PHE CB C 39.0293 0.11 1 209 42 42 PHE N N 126.7359 0.07 1 210 44 44 LEU HD1 H 0.5185 0.01 2 211 44 44 LEU HD2 H -0.1529 0.01 2 212 44 44 LEU C C 173.1934 0.11 1 213 44 44 LEU CA C 51.0369 0.11 1 214 44 44 LEU CB C 43.6543 0.11 1 215 44 44 LEU CD1 C 23.5588 0.11 2 216 44 44 LEU CD2 C 25.8197 0.11 2 217 45 45 VAL H H 7.0805 0.01 1 218 45 45 VAL HG1 H 0.7270 0.01 2 219 45 45 VAL HG2 H 0.3680 0.01 2 220 45 45 VAL C C 173.9812 0.11 1 221 45 45 VAL CA C 65.0554 0.11 1 222 45 45 VAL CG1 C 21.2600 0.11 2 223 45 45 VAL CG2 C 22.3110 0.11 2 224 45 45 VAL N N 121.5952 0.07 1 225 46 46 THR H H 9.1795 0.01 1 226 46 46 THR CA C 62.7125 0.11 1 227 46 46 THR CB C 71.7560 0.11 1 228 46 46 THR N N 117.5938 0.07 1 229 47 47 THR C C 172.9967 0.11 1 230 47 47 THR CA C 64.0253 0.11 1 231 47 47 THR CB C 67.8770 0.11 1 232 48 48 LYS H H 7.2442 0.01 1 233 48 48 LYS C C 173.9407 0.11 1 234 48 48 LYS CA C 55.6258 0.11 1 235 48 48 LYS CB C 33.9075 0.11 1 236 48 48 LYS N N 117.0317 0.07 1 237 49 49 ARG H H 5.8212 0.01 1 238 49 49 ARG C C 175.8874 0.11 1 239 49 49 ARG CA C 57.5561 0.11 1 240 49 49 ARG CB C 28.4977 0.11 1 241 49 49 ARG N N 117.9160 0.07 1 242 50 50 CYS H H 8.3309 0.01 1 243 50 50 CYS C C 174.6990 0.11 1 244 50 50 CYS CA C 58.2314 0.11 1 245 50 50 CYS CB C 29.0358 0.11 1 246 50 50 CYS N N 129.3075 0.07 1 247 51 51 HIS H H 8.7207 0.01 1 248 51 51 HIS C C 174.8797 0.11 1 249 51 51 HIS CA C 55.6733 0.11 1 250 51 51 HIS CB C 29.2322 0.11 1 251 51 51 HIS N N 125.3928 0.07 1 252 52 52 LEU H H 7.8199 0.01 1 253 52 52 LEU HD1 H 0.6268 0.01 2 254 52 52 LEU HD2 H 0.5363 0.01 2 255 52 52 LEU C C 177.6012 0.11 1 256 52 52 LEU CA C 56.9534 0.11 1 257 52 52 LEU CD1 C 23.2077 0.11 2 258 52 52 LEU CD2 C 24.4703 0.11 2 259 52 52 LEU N N 127.7210 0.07 1 260 53 53 ARG H H 8.5981 0.01 1 261 53 53 ARG C C 177.5666 0.11 1 262 53 53 ARG CA C 59.7263 0.11 1 263 53 53 ARG N N 118.2745 0.07 1 264 54 54 SER C C 174.2440 0.11 1 265 54 54 SER CA C 61.9128 0.11 1 266 54 54 SER CB C 62.6809 0.11 1 267 55 55 ILE H H 6.7465 0.01 1 268 55 55 ILE HD1 H 0.2131 0.01 1 269 55 55 ILE C C 178.6041 0.11 1 270 55 55 ILE CA C 64.5876 0.11 1 271 55 55 ILE CB C 37.8686 0.11 1 272 55 55 ILE CD1 C 13.8116 0.11 1 273 55 55 ILE N N 120.7897 0.07 1 274 56 56 ILE H H 8.3130 0.01 1 275 56 56 ILE HD1 H 0.3842 0.01 1 276 56 56 ILE C C 177.4904 0.11 1 277 56 56 ILE CA C 65.7152 0.11 1 278 56 56 ILE CB C 36.7139 0.11 1 279 56 56 ILE CD1 C 13.2119 0.11 1 280 56 56 ILE N N 117.6657 0.07 1 281 57 57 HIS H H 7.6636 0.01 1 282 57 57 HIS C C 177.4378 0.11 1 283 57 57 HIS N N 114.7883 0.07 1 284 58 58 GLU H H 7.9344 0.01 1 285 58 58 GLU C C 175.8627 0.11 1 286 58 58 GLU CA C 59.8421 0.11 1 287 58 58 GLU CB C 28.5793 0.11 1 288 58 58 GLU N N 119.5050 0.07 1 289 59 59 LEU H H 7.1115 0.01 1 290 59 59 LEU HD1 H 0.9780 0.01 2 291 59 59 LEU HD2 H 0.6005 0.01 2 292 59 59 LEU C C 179.1115 0.11 1 293 59 59 LEU CA C 57.4717 0.11 1 294 59 59 LEU CB C 39.8487 0.11 1 295 59 59 LEU CD1 C 23.2560 0.11 2 296 59 59 LEU CD2 C 26.4269 0.11 2 297 59 59 LEU N N 120.3399 0.07 1 298 60 60 LEU H H 8.4130 0.01 1 299 60 60 LEU HD1 H 0.8306 0.01 2 300 60 60 LEU HD2 H 0.8120 0.01 2 301 60 60 LEU C C 180.4163 0.11 1 302 60 60 LEU CA C 57.7679 0.11 1 303 60 60 LEU CB C 38.9202 0.11 1 304 60 60 LEU CD1 C 25.3979 0.11 2 305 60 60 LEU CD2 C 21.4930 0.11 2 306 60 60 LEU N N 117.7831 0.07 1 307 61 61 TRP H H 8.2380 0.01 1 308 61 61 TRP C C 178.2721 0.11 1 309 61 61 TRP CA C 60.1650 0.11 1 310 61 61 TRP CB C 27.8347 0.11 1 311 61 61 TRP N N 123.9480 0.07 1 312 62 62 PHE H H 8.2780 0.01 1 313 62 62 PHE C C 180.6651 0.11 1 314 62 62 PHE CA C 56.8314 0.11 1 315 62 62 PHE N N 119.5131 0.07 1 316 63 63 LEU H H 8.3605 0.01 1 317 63 63 LEU HD1 H 1.0064 0.01 2 318 63 63 LEU HD2 H 1.1643 0.01 2 319 63 63 LEU C C 178.1286 0.11 1 320 63 63 LEU CA C 57.5240 0.11 1 321 63 63 LEU CB C 41.9778 0.11 1 322 63 63 LEU CD1 C 26.5014 0.11 2 323 63 63 LEU CD2 C 23.0372 0.11 2 324 63 63 LEU N N 116.0091 0.07 1 325 64 64 GLN H H 7.6325 0.01 1 326 64 64 GLN C C 177.6183 0.11 1 327 64 64 GLN CA C 55.8345 0.11 1 328 64 64 GLN CB C 28.7083 0.11 1 329 64 64 GLN N N 116.0440 0.07 1 330 65 65 GLY H H 8.0572 0.01 1 331 65 65 GLY C C 172.6957 0.11 1 332 65 65 GLY CA C 44.7197 0.11 1 333 65 65 GLY N N 109.5825 0.07 1 334 66 66 ASP H H 6.6969 0.01 1 335 66 66 ASP C C 175.1756 0.11 1 336 66 66 ASP CA C 53.1830 0.11 1 337 66 66 ASP CB C 42.5742 0.11 1 338 66 66 ASP N N 120.8391 0.07 1 339 67 67 THR H H 8.0477 0.01 1 340 67 67 THR C C 172.0265 0.11 1 341 67 67 THR CA C 60.9155 0.11 1 342 67 67 THR CB C 68.6657 0.11 1 343 67 67 THR N N 113.2304 0.07 1 344 68 68 ASN H H 8.4398 0.01 1 345 68 68 ASN C C 177.7724 0.11 1 346 68 68 ASN CA C 51.8575 0.11 1 347 68 68 ASN CB C 42.0290 0.11 1 348 68 68 ASN N N 123.1467 0.07 1 349 69 69 ILE H H 9.0777 0.01 1 350 69 69 ILE HD1 H 0.6486 0.01 1 351 69 69 ILE C C 175.9150 0.11 1 352 69 69 ILE CA C 63.3738 0.11 1 353 69 69 ILE CB C 36.5596 0.11 1 354 69 69 ILE CD1 C 13.9694 0.11 1 355 69 69 ILE N N 121.8109 0.07 1 356 70 70 ALA H H 9.0554 0.01 1 357 70 70 ALA C C 180.2427 0.11 1 358 70 70 ALA CA C 56.5786 0.11 1 359 70 70 ALA CB C 16.6223 0.11 1 360 70 70 ALA N N 129.1904 0.07 1 361 71 71 TYR H H 9.2845 0.01 1 362 71 71 TYR C C 177.9773 0.11 1 363 71 71 TYR CA C 60.9767 0.11 1 364 71 71 TYR CB C 39.0277 0.11 1 365 71 71 TYR N N 119.0070 0.07 1 366 72 72 LEU H H 6.5151 0.01 1 367 72 72 LEU HD1 H -0.2777 0.01 2 368 72 72 LEU HD2 H 0.2520 0.01 2 369 72 72 LEU C C 180.2955 0.11 1 370 72 72 LEU CA C 57.0607 0.11 1 371 72 72 LEU CB C 37.9896 0.11 1 372 72 72 LEU CD1 C 25.1995 0.11 2 373 72 72 LEU CD2 C 20.3220 0.11 2 374 72 72 LEU N N 118.0158 0.07 1 375 73 73 HIS H H 8.3405 0.01 1 376 73 73 HIS C C 179.6283 0.11 1 377 73 73 HIS CA C 57.8164 0.11 1 378 73 73 HIS CB C 28.3465 0.11 1 379 73 73 HIS N N 121.3803 0.07 1 380 74 74 GLU H H 8.4293 0.01 1 381 74 74 GLU C C 176.2483 0.11 1 382 74 74 GLU CA C 58.2908 0.11 1 383 74 74 GLU N N 122.8675 0.07 1 384 75 75 ASN H H 6.6932 0.01 1 385 75 75 ASN C C 172.9348 0.11 1 386 75 75 ASN CA C 52.4879 0.11 1 387 75 75 ASN CB C 38.1523 0.11 1 388 75 75 ASN N N 115.0967 0.07 1 389 76 76 ASN H H 7.7758 0.01 1 390 76 76 ASN C C 173.2247 0.11 1 391 76 76 ASN CA C 54.1783 0.11 1 392 76 76 ASN CB C 36.2652 0.11 1 393 76 76 ASN N N 115.3876 0.07 1 394 77 77 VAL H H 8.1436 0.01 1 395 77 77 VAL HG1 H 0.9910 0.01 2 396 77 77 VAL HG2 H 0.7570 0.01 2 397 77 77 VAL C C 176.7688 0.11 1 398 77 77 VAL CA C 61.7539 0.11 1 399 77 77 VAL CB C 31.2554 0.11 1 400 77 77 VAL CG1 C 22.3890 0.11 2 401 77 77 VAL CG2 C 20.6360 0.11 2 402 77 77 VAL N N 120.8769 0.07 1 403 78 78 THR H H 8.5242 0.01 1 404 78 78 THR C C 177.2901 0.11 1 405 78 78 THR CA C 61.3343 0.11 1 406 78 78 THR CB C 68.2301 0.11 1 407 78 78 THR N N 116.4085 0.07 1 408 79 79 ILE H H 6.2624 0.01 1 409 79 79 ILE HD1 H 0.7021 0.01 1 410 79 79 ILE C C 174.7448 0.11 1 411 79 79 ILE CA C 64.0962 0.11 1 412 79 79 ILE CB C 35.1794 0.11 1 413 79 79 ILE CD1 C 13.4833 0.11 1 414 79 79 ILE N N 113.7188 0.07 1 415 80 80 TRP H H 7.8335 0.01 1 416 80 80 TRP CA C 58.8246 0.11 1 417 80 80 TRP N N 118.7947 0.07 1 418 81 81 ASP H H 7.5023 0.01 1 419 81 81 ASP C C 179.7003 0.11 1 420 81 81 ASP CA C 57.9445 0.11 1 421 81 81 ASP CB C 39.1711 0.11 1 422 81 81 ASP N N 120.4085 0.07 1 423 82 82 GLU H H 8.2475 0.01 1 424 82 82 GLU C C 176.8977 0.11 1 425 82 82 GLU CA C 58.9636 0.11 1 426 82 82 GLU CB C 25.9630 0.11 1 427 82 82 GLU N N 115.8192 0.07 1 428 83 83 TRP H H 7.0614 0.01 1 429 83 83 TRP CA C 60.0291 0.11 1 430 83 83 TRP CB C 28.9407 0.11 1 431 83 83 TRP N N 116.0968 0.07 1 432 84 84 ALA H H 7.0474 0.01 1 433 84 84 ALA C C 177.2941 0.11 1 434 84 84 ALA CA C 51.1659 0.11 1 435 84 84 ALA CB C 19.8121 0.11 1 436 84 84 ALA N N 122.9054 0.07 1 437 85 85 ASP H H 8.2738 0.01 1 438 85 85 ASP C C 178.6490 0.11 1 439 85 85 ASP CA C 52.3456 0.11 1 440 85 85 ASP CB C 40.0307 0.11 1 441 85 85 ASP N N 121.1457 0.07 1 442 86 86 GLU H H 9.0259 0.01 1 443 86 86 GLU C C 177.0654 0.11 1 444 86 86 GLU CA C 58.4573 0.11 1 445 86 86 GLU CB C 28.0364 0.11 1 446 86 86 GLU N N 118.0723 0.07 1 447 87 87 ASN H H 8.2738 0.01 1 448 87 87 ASN C C 175.6106 0.11 1 449 87 87 ASN CA C 52.6040 0.11 1 450 87 87 ASN CB C 39.0966 0.11 1 451 87 87 ASN N N 117.6522 0.07 1 452 88 88 GLY H H 8.3331 0.01 1 453 88 88 GLY C C 173.2432 0.11 1 454 88 88 GLY CA C 45.0334 0.11 1 455 88 88 GLY N N 110.0374 0.07 1 456 89 89 ASP C C 177.6891 0.11 1 457 89 89 ASP CA C 55.8490 0.11 1 458 89 89 ASP CB C 42.3878 0.11 1 459 90 90 LEU H H 7.9544 0.01 1 460 90 90 LEU HD1 H 0.9210 0.01 2 461 90 90 LEU HD2 H 1.2820 0.01 2 462 90 90 LEU C C 176.8222 0.11 1 463 90 90 LEU CA C 54.2295 0.11 1 464 90 90 LEU CB C 44.0319 0.11 1 465 90 90 LEU CD1 C 27.5103 0.11 2 466 90 90 LEU CD2 C 23.7140 0.11 2 467 90 90 LEU N N 122.2581 0.07 1 468 91 91 GLY H H 8.0315 0.01 1 469 91 91 GLY C C 173.8005 0.11 1 470 91 91 GLY CA C 43.8080 0.11 1 471 91 91 GLY N N 108.1692 0.07 1 472 92 92 PRO C C 175.1898 0.11 1 473 92 92 PRO CA C 62.5720 0.11 1 474 92 92 PRO CB C 28.0222 0.11 1 475 93 93 VAL H H 8.5960 0.01 1 476 93 93 VAL HG1 H 0.8410 0.01 2 477 93 93 VAL HG2 H 0.7760 0.01 2 478 93 93 VAL C C 174.1199 0.11 1 479 93 93 VAL CA C 59.8285 0.11 1 480 93 93 VAL CB C 30.7441 0.11 1 481 93 93 VAL CG1 C 21.5410 0.11 2 482 93 93 VAL CG2 C 18.0670 0.11 2 483 93 93 VAL N N 115.1800 0.07 1 484 94 94 TYR H H 5.8270 0.01 1 485 94 94 TYR CA C 60.6469 0.11 1 486 94 94 TYR N N 111.5594 0.07 1 487 95 95 GLY H H 7.6923 0.01 1 488 95 95 GLY CA C 47.7429 0.11 1 489 95 95 GLY N N 102.98 0.07 1 490 96 96 LYS H H 6.6197 0.01 1 491 96 96 LYS C C 177.9822 0.11 1 492 96 96 LYS CA C 57.5928 0.11 1 493 96 96 LYS CB C 31.2222 0.11 1 494 96 96 LYS N N 119.5905 0.07 1 495 97 97 GLN H H 7.0259 0.01 1 496 97 97 GLN C C 179.2545 0.11 1 497 97 97 GLN CA C 56.2457 0.11 1 498 97 97 GLN CB C 26.5825 0.11 1 499 97 97 GLN N N 113.2414 0.07 1 500 98 98 TRP H H 9.1796 0.01 1 501 98 98 TRP C C 178.3755 0.11 1 502 98 98 TRP CA C 59.7734 0.11 1 503 98 98 TRP CB C 29.2430 0.11 1 504 98 98 TRP N N 116.9384 0.07 1 505 99 99 ARG H H 7.5734 0.01 1 506 99 99 ARG C C 176.8149 0.11 1 507 99 99 ARG CA C 53.4449 0.11 1 508 99 99 ARG CB C 28.6910 0.11 1 509 99 99 ARG N N 112.1063 0.07 1 510 100 100 ALA H H 8.5714 0.01 1 511 100 100 ALA C C 174.7622 0.11 1 512 100 100 ALA CA C 51.2115 0.11 1 513 100 100 ALA CB C 17.1141 0.11 1 514 100 100 ALA N N 127.4522 0.07 1 515 101 101 TRP H H 8.4083 0.01 1 516 101 101 TRP C C 176.5286 0.11 1 517 101 101 TRP CA C 55.8816 0.11 1 518 101 101 TRP CB C 26.5953 0.11 1 519 101 101 TRP N N 126.4372 0.07 1 520 104 104 PRO C C 176.0647 0.11 1 521 104 104 PRO CA C 64.5290 0.11 1 522 104 104 PRO CB C 30.5723 0.11 1 523 105 105 ASP H H 7.9405 0.01 1 524 105 105 ASP C C 176.3184 0.11 1 525 105 105 ASP CA C 52.5018 0.11 1 526 105 105 ASP CB C 39.1695 0.11 1 527 105 105 ASP N N 112.7706 0.07 1 528 106 106 GLY H H 7.5820 0.01 1 529 106 106 GLY C C 174.7723 0.11 1 530 106 106 GLY CA C 45.8328 0.11 1 531 106 106 GLY N N 107.4949 0.07 1 532 107 107 ARG H H 7.2858 0.01 1 533 107 107 ARG C C 175.4624 0.11 1 534 107 107 ARG CA C 54.4256 0.11 1 535 107 107 ARG CB C 30.6943 0.11 1 536 107 107 ARG N N 119.7730 0.07 1 537 108 108 HIS H H 8.1083 0.01 1 538 108 108 HIS C C 175.1059 0.11 1 539 108 108 HIS CA C 55.6597 0.11 1 540 108 108 HIS CB C 32.0696 0.11 1 541 108 108 HIS N N 118.8275 0.07 1 542 109 109 ILE H H 9.5629 0.01 1 543 109 109 ILE HD1 H 0.6434 0.01 1 544 109 109 ILE C C 174.1988 0.11 1 545 109 109 ILE CA C 60.2446 0.11 1 546 109 109 ILE CB C 38.9209 0.11 1 547 109 109 ILE CD1 C 13.3126 0.11 1 548 109 109 ILE N N 125.4393 0.07 1 549 110 110 ASP H H 8.6060 0.01 1 550 110 110 ASP C C 178.1117 0.11 1 551 110 110 ASP CA C 51.5687 0.11 1 552 110 110 ASP CB C 39.1954 0.11 1 553 110 110 ASP N N 126.4670 0.07 1 554 111 111 GLN H H 8.4368 0.01 1 555 111 111 GLN C C 177.5768 0.11 1 556 111 111 GLN CA C 59.2095 0.11 1 557 111 111 GLN CB C 31.5184 0.11 1 558 111 111 GLN N N 127.0561 0.07 1 559 112 112 ILE H H 7.9295 0.01 1 560 112 112 ILE HD1 H 0.4401 0.01 1 561 112 112 ILE C C 177.1483 0.11 1 562 112 112 ILE CA C 61.1410 0.11 1 563 112 112 ILE CB C 33.8170 0.11 1 564 112 112 ILE CD1 C 6.39 0.11 1 565 112 112 ILE N N 119.0074 0.07 1 566 113 113 THR H H 7.6423 0.01 1 567 113 113 THR C C 177.1506 0.11 1 568 113 113 THR CA C 67.3250 0.11 1 569 113 113 THR N N 118.3131 0.07 1 570 114 114 THR C C 176.1827 0.11 1 571 115 115 VAL H H 7.9671 0.01 1 572 115 115 VAL HG1 H 0.6100 0.01 2 573 115 115 VAL HG2 H 0.9360 0.01 2 574 115 115 VAL C C 177.5907 0.11 1 575 115 115 VAL CA C 65.0710 0.11 1 576 115 115 VAL CB C 30.2434 0.11 1 577 115 115 VAL CG1 C 22.5130 0.11 2 578 115 115 VAL CG2 C 21.9310 0.11 2 579 115 115 VAL N N 120.3580 0.07 1 580 116 116 LEU H H 7.7017 0.01 1 581 116 116 LEU HD1 H 0.7580 0.01 2 582 116 116 LEU HD2 H 0.7309 0.01 2 583 116 116 LEU C C 178.5666 0.11 1 584 116 116 LEU CA C 57.9971 0.11 1 585 116 116 LEU CB C 40.8017 0.11 1 586 116 116 LEU CD1 C 25.5920 0.11 2 587 116 116 LEU CD2 C 24.7974 0.11 2 588 116 116 LEU N N 122.0747 0.07 1 589 117 117 ASN H H 7.6856 0.01 1 590 117 117 ASN C C 178.5091 0.11 1 591 117 117 ASN CA C 56.0550 0.11 1 592 117 117 ASN CB C 37.6641 0.11 1 593 117 117 ASN N N 116.2597 0.07 1 594 118 118 GLN H H 8.4095 0.01 1 595 118 118 GLN C C 178.2358 0.11 1 596 118 118 GLN CA C 59.1951 0.11 1 597 118 118 GLN CB C 29.6324 0.11 1 598 118 118 GLN N N 121.9390 0.07 1 599 119 119 LEU H H 8.6480 0.01 1 600 119 119 LEU C C 178.0603 0.11 1 601 119 119 LEU CA C 57.6553 0.11 1 602 119 119 LEU CB C 41.6547 0.11 1 603 119 119 LEU N N 119.3462 0.07 1 604 120 120 LYS H H 7.2465 0.01 1 605 120 120 LYS C C 178.4373 0.11 1 606 120 120 LYS CA C 58.2460 0.11 1 607 120 120 LYS CB C 32.8617 0.11 1 608 120 120 LYS N N 113.1790 0.07 1 609 121 121 ASN H H 8.0046 0.01 1 610 121 121 ASN C C 174.7738 0.11 1 611 121 121 ASN CA C 54.0489 0.11 1 612 121 121 ASN CB C 40.3511 0.11 1 613 121 121 ASN N N 114.5642 0.07 1 614 122 122 ASP H H 9.1926 0.01 1 615 122 122 ASP C C 172.4997 0.11 1 616 122 122 ASP CA C 52.1567 0.11 1 617 122 122 ASP CB C 40.5552 0.11 1 618 122 122 ASP N N 123.6323 0.07 1 619 123 123 PRO C C 175.9450 0.11 1 620 123 123 PRO CA C 64.5393 0.11 1 621 123 123 PRO CB C 30.0620 0.11 1 622 124 124 ASP H H 7.9215 0.01 1 623 124 124 ASP C C 176.9305 0.11 1 624 124 124 ASP CA C 54.6981 0.11 1 625 124 124 ASP CB C 40.4357 0.11 1 626 124 124 ASP N N 114.9814 0.07 1 627 125 125 SER H H 7.9530 0.01 1 628 125 125 SER C C 176.2946 0.11 1 629 125 125 SER CA C 59.0317 0.11 1 630 125 125 SER CB C 62.2638 0.11 1 631 125 125 SER N N 116.1566 0.07 1 632 126 126 ARG H H 8.5132 0.01 1 633 126 126 ARG CA C 56.2651 0.11 1 634 126 126 ARG N N 127.6533 0.07 1 635 127 127 ARG H H 8.6908 0.01 1 636 127 127 ARG C C 174.9683 0.11 1 637 127 127 ARG CA C 54.2375 0.11 1 638 127 127 ARG CB C 29.6302 0.11 1 639 127 127 ARG N N 121.5945 0.07 1 640 128 128 ILE H H 8.5001 0.01 1 641 128 128 ILE HD1 H 0.7198 0.01 1 642 128 128 ILE C C 174.4192 0.11 1 643 128 128 ILE CA C 61.5319 0.11 1 644 128 128 ILE CB C 33.7809 0.11 1 645 128 128 ILE CD1 C 12.9399 0.11 1 646 128 128 ILE N N 124.7292 0.07 1 647 129 129 ILE H H 7.5630 0.01 1 648 129 129 ILE HD1 H -0.0343 0.01 1 649 129 129 ILE C C 175.2602 0.11 1 650 129 129 ILE CA C 58.3437 0.11 1 651 129 129 ILE CB C 43.2616 0.11 1 652 129 129 ILE CD1 C 13.2336 0.11 1 653 129 129 ILE N N 128.8847 0.07 1 654 130 130 VAL H H 7.8363 0.01 1 655 130 130 VAL HG1 H -0.1630 0.01 2 656 130 130 VAL HG2 H 0.1800 0.01 2 657 130 130 VAL C C 173.5958 0.11 1 658 130 130 VAL CA C 59.9454 0.11 1 659 130 130 VAL CB C 31.4120 0.11 1 660 130 130 VAL CG1 C 20.7290 0.11 2 661 130 130 VAL CG2 C 21.9440 0.11 2 662 130 130 VAL N N 127.2524 0.07 1 663 131 131 SER H H 8.9123 0.01 1 664 131 131 SER C C 175.1941 0.11 1 665 131 131 SER CA C 54.2016 0.11 1 666 131 131 SER CB C 65.8082 0.11 1 667 131 131 SER N N 116.6409 0.07 1 668 132 132 ALA H H 8.9649 0.01 1 669 132 132 ALA C C 176.1580 0.11 1 670 132 132 ALA CA C 50.7229 0.11 1 671 132 132 ALA CB C 18.7010 0.11 1 672 132 132 ALA N N 127.2803 0.07 1 673 133 133 TRP H H 9.0613 0.01 1 674 133 133 TRP CA C 56.1189 0.11 1 675 133 133 TRP CB C 27.2946 0.11 1 676 133 133 TRP N N 123.8107 0.07 1 677 134 134 ASN H H 6.7736 0.01 1 678 134 134 ASN C C 174.7950 0.11 1 679 134 134 ASN CA C 51.2680 0.11 1 680 134 134 ASN CB C 33.7827 0.11 1 681 134 134 ASN N N 125.2710 0.07 1 682 135 135 VAL H H 5.8578 0.01 1 683 135 135 VAL HG1 H 0.2900 0.01 2 684 135 135 VAL HG2 H 0.1710 0.01 2 685 135 135 VAL C C 175.6519 0.11 1 686 135 135 VAL CA C 64.6369 0.11 1 687 135 135 VAL CB C 30.3897 0.11 1 688 135 135 VAL CG1 C 20.6030 0.11 2 689 135 135 VAL CG2 C 21.8800 0.11 2 690 135 135 VAL N N 123.6520 0.07 1 691 136 136 GLY C C 173.1957 0.11 1 692 136 136 GLY CA C 45.6537 0.11 1 693 137 137 GLU H H 7.0229 0.01 1 694 137 137 GLU C C 176.1458 0.11 1 695 137 137 GLU CA C 55.3040 0.11 1 696 137 137 GLU CB C 30.6973 0.11 1 697 137 137 GLU N N 116.2356 0.07 1 698 138 138 LEU H H 6.6459 0.01 1 699 138 138 LEU HD1 H 0.3284 0.01 2 700 138 138 LEU HD2 H -0.4700 0.01 2 701 138 138 LEU C C 179.2423 0.11 1 702 138 138 LEU CA C 57.6320 0.11 1 703 138 138 LEU CB C 41.4805 0.11 1 704 138 138 LEU CD1 C 24.8598 0.11 2 705 138 138 LEU CD2 C 20.3590 0.11 2 706 138 138 LEU N N 121.5399 0.07 1 707 139 139 ASP H H 8.1990 0.01 1 708 139 139 ASP C C 176.7261 0.11 1 709 139 139 ASP CA C 55.3282 0.11 1 710 139 139 ASP CB C 38.9137 0.11 1 711 139 139 ASP N N 115.1477 0.07 1 712 140 140 LYS H H 7.1754 0.01 1 713 140 140 LYS C C 177.1318 0.11 1 714 140 140 LYS CA C 55.0254 0.11 1 715 140 140 LYS CB C 32.6058 0.11 1 716 140 140 LYS N N 117.4903 0.07 1 717 141 141 MET H H 7.1902 0.01 1 718 141 141 MET C C 176.9401 0.11 1 719 141 141 MET CA C 56.0578 0.11 1 720 141 141 MET CB C 32.4114 0.11 1 721 141 141 MET N N 120.2188 0.07 1 722 142 142 ALA H H 8.7533 0.01 1 723 142 142 ALA C C 178.0103 0.11 1 724 142 142 ALA CA C 54.9736 0.11 1 725 142 142 ALA CB C 19.4503 0.11 1 726 142 142 ALA N N 126.1676 0.07 1 727 143 143 LEU H H 6.5799 0.01 1 728 143 143 LEU HD1 H 0.3820 0.01 2 729 143 143 LEU HD2 H 0.8810 0.01 2 730 143 143 LEU C C 175.5130 0.11 1 731 143 143 LEU CA C 53.4775 0.11 1 732 143 143 LEU CB C 46.3966 0.11 1 733 143 143 LEU CD1 C 25.5050 0.11 2 734 143 143 LEU CD2 C 24.3540 0.11 2 735 143 143 LEU N N 111.3447 0.07 1 736 144 144 ALA H H 6.6892 0.01 1 737 144 144 ALA C C 176.6539 0.11 1 738 144 144 ALA CA C 50.0036 0.11 1 739 144 144 ALA CB C 15.4545 0.11 1 740 144 144 ALA N N 125.0657 0.07 1 741 145 145 PRO C C 179.0786 0.11 1 742 145 145 PRO CA C 63.4647 0.11 1 743 145 145 PRO CB C 32.4817 0.11 1 744 146 146 CYS H H 9.4864 0.01 1 745 146 146 CYS C C 174.2555 0.11 1 746 146 146 CYS CA C 58.6140 0.11 1 747 146 146 CYS CB C 29.5508 0.11 1 748 146 146 CYS N N 127.2333 0.07 1 749 147 147 HIS H H 6.9542 0.01 1 750 147 147 HIS C C 173.9167 0.11 1 751 147 147 HIS CA C 52.7304 0.11 1 752 147 147 HIS CB C 31.2891 0.11 1 753 147 147 HIS N N 116.6257 0.07 1 754 148 148 ALA H H 7.8598 0.01 1 755 148 148 ALA C C 175.2015 0.11 1 756 148 148 ALA CA C 54.3685 0.11 1 757 148 148 ALA CB C 21.7033 0.11 1 758 148 148 ALA N N 126.8985 0.07 1 759 149 149 PHE H H 7.2290 0.01 1 760 149 149 PHE C C 172.0164 0.11 1 761 149 149 PHE CA C 57.0378 0.11 1 762 149 149 PHE CB C 41.9449 0.11 1 763 149 149 PHE N N 119.2102 0.07 1 764 150 150 PHE H H 8.8750 0.01 1 765 150 150 PHE C C 171.5953 0.11 1 766 150 150 PHE CA C 54.8887 0.11 1 767 150 150 PHE CB C 40.6140 0.11 1 768 150 150 PHE N N 123.3002 0.07 1 769 151 151 GLN H H 8.7816 0.01 1 770 151 151 GLN C C 174.3800 0.11 1 771 151 151 GLN CA C 52.2226 0.11 1 772 151 151 GLN CB C 32.2366 0.11 1 773 151 151 GLN N N 120.4809 0.07 1 774 152 152 PHE H H 9.0038 0.01 1 775 152 152 PHE C C 173.0666 0.11 1 776 152 152 PHE CA C 56.8541 0.11 1 777 152 152 PHE CB C 41.7526 0.11 1 778 152 152 PHE N N 124.1159 0.07 1 779 153 153 TYR H H 7.9912 0.01 1 780 153 153 TYR C C 172.4757 0.11 1 781 153 153 TYR CA C 56.1127 0.11 1 782 153 153 TYR CB C 40.1945 0.11 1 783 153 153 TYR N N 122.0773 0.07 1 784 154 154 VAL H H 7.8918 0.01 1 785 154 154 VAL HG1 H 0.6160 0.01 2 786 154 154 VAL HG2 H 0.6990 0.01 2 787 154 154 VAL C C 174.8685 0.11 1 788 154 154 VAL CA C 59.8062 0.11 1 789 154 154 VAL CB C 32.7607 0.11 1 790 154 154 VAL CG1 C 21.1460 0.11 2 791 154 154 VAL CG2 C 22.7280 0.11 2 792 154 154 VAL N N 127.6698 0.07 1 793 155 155 ALA H H 7.8990 0.01 1 794 155 155 ALA C C 177.3130 0.11 1 795 155 155 ALA CA C 51.5498 0.11 1 796 155 155 ALA CB C 21.4440 0.11 1 797 155 155 ALA N N 125.9643 0.07 1 798 156 156 ASP H H 9.3834 0.01 1 799 156 156 ASP CA C 54.7551 0.11 1 800 156 156 ASP N N 124.3048 0.07 1 801 157 157 GLY H H 8.4477 0.01 1 802 157 157 GLY C C 173.5486 0.11 1 803 157 157 GLY CA C 45.4645 0.11 1 804 157 157 GLY N N 103.53 0.07 1 805 158 158 LYS H H 7.8632 0.01 1 806 158 158 LYS C C 175.6846 0.11 1 807 158 158 LYS CA C 53.9637 0.11 1 808 158 158 LYS CB C 34.0574 0.11 1 809 158 158 LYS N N 120.1560 0.07 1 810 159 159 LEU H H 9.0047 0.01 1 811 159 159 LEU HD1 H 0.2673 0.01 2 812 159 159 LEU HD2 H 0.7390 0.01 2 813 159 159 LEU C C 175.0806 0.11 1 814 159 159 LEU CA C 53.4202 0.11 1 815 159 159 LEU CB C 43.3982 0.11 1 816 159 159 LEU CD1 C 26.0134 0.11 2 817 159 159 LEU CD2 C 27.0164 0.11 2 818 159 159 LEU N N 126.3823 0.07 1 819 160 160 SER H H 9.7164 0.01 1 820 160 160 SER C C 172.9976 0.11 1 821 160 160 SER CA C 57.1392 0.11 1 822 160 160 SER CB C 66.2003 0.11 1 823 160 160 SER N N 122.3413 0.07 1 824 161 161 CYS H H 8.9762 0.01 1 825 161 161 CYS C C 172.5032 0.11 1 826 161 161 CYS CA C 56.0053 0.11 1 827 161 161 CYS CB C 31.9750 0.11 1 828 161 161 CYS N N 121.2300 0.07 1 829 162 162 GLN H H 9.6657 0.01 1 830 162 162 GLN C C 172.7041 0.11 1 831 162 162 GLN CA C 52.3512 0.11 1 832 162 162 GLN CB C 31.7000 0.11 1 833 162 162 GLN N N 129.4698 0.07 1 834 163 163 LEU H H 8.1178 0.01 1 835 163 163 LEU HD1 H 0.6600 0.01 2 836 163 163 LEU HD2 H 0.6570 0.01 2 837 163 163 LEU C C 173.3163 0.11 1 838 163 163 LEU CB C 45.2983 0.11 1 839 163 163 LEU CD1 C 22.3750 0.11 2 840 163 163 LEU CD2 C 25.4130 0.11 2 841 163 163 LEU N N 127.8029 0.07 1 842 164 164 TYR H H 8.9600 0.01 1 843 164 164 TYR C C 173.4364 0.11 1 844 164 164 TYR CA C 57.5615 0.11 1 845 164 164 TYR CB C 38.3792 0.11 1 846 164 164 TYR N N 123.8823 0.07 1 847 165 165 GLN H H 8.4463 0.01 1 848 165 165 GLN C C 173.5518 0.11 1 849 165 165 GLN CA C 53.6311 0.11 1 850 165 165 GLN CB C 26.3175 0.11 1 851 165 165 GLN N N 132.7481 0.07 1 852 166 166 ARG H H 6.9880 0.01 1 853 166 166 ARG CA C 57.0703 0.11 1 854 166 166 ARG CB C 28.6190 0.11 1 855 166 166 ARG N N 123.1375 0.07 1 856 167 167 SER H H 6.9405 0.01 1 857 167 167 SER C C 173.9056 0.11 1 858 167 167 SER CA C 55.6666 0.11 1 859 167 167 SER CB C 64.8660 0.11 1 860 167 167 SER N N 116.3079 0.07 1 861 168 168 CYS H H 9.1675 0.01 1 862 168 168 CYS C C 169.3922 0.11 1 863 168 168 CYS CA C 56.5742 0.11 1 864 168 168 CYS CB C 30.1056 0.11 1 865 168 168 CYS N N 130.8974 0.07 1 866 169 169 ASP H H 8.1438 0.01 1 867 169 169 ASP C C 176.4403 0.11 1 868 169 169 ASP CA C 52.4620 0.11 1 869 169 169 ASP CB C 40.1684 0.11 1 870 169 169 ASP N N 133.0570 0.07 1 871 170 170 VAL H H 9.3581 0.01 1 872 170 170 VAL HG1 H 0.4760 0.01 2 873 170 170 VAL HG2 H 0.7800 0.01 2 874 170 170 VAL C C 177.0540 0.11 1 875 170 170 VAL CA C 65.8004 0.11 1 876 170 170 VAL CB C 30.9633 0.11 1 877 170 170 VAL CG1 C 21.5190 0.11 2 878 170 170 VAL CG2 C 25.8120 0.11 2 879 170 170 VAL N N 126.3924 0.07 1 880 171 171 PHE H H 8.5539 0.01 1 881 171 171 PHE C C 173.4511 0.11 1 882 171 171 PHE CA C 62.7796 0.11 1 883 171 171 PHE CB C 40.2288 0.11 1 884 171 171 PHE N N 120.4518 0.07 1 885 172 172 LEU H H 7.5206 0.01 1 886 172 172 LEU HD1 H 0.6110 0.01 2 887 172 172 LEU HD2 H 0.5100 0.01 2 888 172 172 LEU C C 178.6357 0.11 1 889 172 172 LEU CA C 54.7570 0.11 1 890 172 172 LEU CB C 42.9207 0.11 1 891 172 172 LEU CD1 C 24.7940 0.11 2 892 172 172 LEU CD2 C 23.6360 0.11 2 893 172 172 LEU N N 115.4588 0.07 1 894 173 173 GLY H H 7.0851 0.01 1 895 173 173 GLY C C 177.3332 0.11 1 896 173 173 GLY CA C 47.0630 0.11 1 897 173 173 GLY N N 106.9279 0.07 1 898 174 174 LEU H H 8.0176 0.01 1 899 174 174 LEU HD1 H 0.0820 0.01 2 900 174 174 LEU HD2 H 0.3780 0.01 2 901 174 174 LEU C C 173.8140 0.11 1 902 174 174 LEU CA C 58.3423 0.11 1 903 174 174 LEU CB C 38.0273 0.11 1 904 174 174 LEU CD1 C 22.0160 0.11 2 905 174 174 LEU CD2 C 26.1553 0.11 2 906 174 174 LEU N N 121.7910 0.07 1 907 175 175 PRO C C 179.8256 0.11 1 908 175 175 PRO CA C 65.9451 0.11 1 909 175 175 PRO CB C 30.3337 0.11 1 910 176 176 PHE H H 6.7723 0.01 1 911 176 176 PHE C C 177.0230 0.11 1 912 176 176 PHE CA C 59.9908 0.11 1 913 176 176 PHE CB C 38.5893 0.11 1 914 176 176 PHE N N 115.5648 0.07 1 915 177 177 ASN H H 8.3345 0.01 1 916 177 177 ASN C C 177.0795 0.11 1 917 177 177 ASN CA C 58.0028 0.11 1 918 177 177 ASN CB C 40.4093 0.11 1 919 177 177 ASN N N 116.9557 0.07 1 920 178 178 ILE H H 8.2814 0.01 1 921 178 178 ILE HD1 H 0.3099 0.01 1 922 178 178 ILE C C 175.9598 0.11 1 923 178 178 ILE CA C 64.8640 0.11 1 924 178 178 ILE CB C 37.4406 0.11 1 925 178 178 ILE CD1 C 13.9586 0.11 1 926 178 178 ILE N N 115.9421 0.07 1 927 179 179 ALA H H 6.4741 0.01 1 928 179 179 ALA C C 177.9025 0.11 1 929 179 179 ALA CA C 54.0971 0.11 1 930 179 179 ALA CB C 18.8010 0.11 1 931 179 179 ALA N N 117.7913 0.07 1 932 180 180 SER H H 8.3005 0.01 1 933 180 180 SER C C 177.0611 0.11 1 934 180 180 SER CA C 61.3501 0.11 1 935 180 180 SER CB C 63.5932 0.11 1 936 180 180 SER N N 112.2599 0.07 1 937 181 181 TYR H H 7.3095 0.01 1 938 181 181 TYR C C 178.2672 0.11 1 939 181 181 TYR CA C 62.6082 0.11 1 940 181 181 TYR CB C 38.2695 0.11 1 941 181 181 TYR N N 114.1225 0.07 1 942 182 182 ALA H H 7.5900 0.01 1 943 182 182 ALA C C 179.5633 0.11 1 944 182 182 ALA CA C 55.2369 0.11 1 945 182 182 ALA CB C 18.3025 0.11 1 946 182 182 ALA N N 121.0149 0.07 1 947 183 183 LEU H H 8.0993 0.01 1 948 183 183 LEU HD1 H 0.1980 0.01 2 949 183 183 LEU HD2 H 0.0700 0.01 2 950 183 183 LEU C C 178.1535 0.11 1 951 183 183 LEU CA C 58.2886 0.11 1 952 183 183 LEU CB C 40.5356 0.11 1 953 183 183 LEU CD1 C 25.1890 0.11 2 954 183 183 LEU CD2 C 25.2540 0.11 2 955 183 183 LEU N N 120.1911 0.07 1 956 184 184 LEU H H 7.8940 0.01 1 957 184 184 LEU HD1 H 1.1472 0.01 2 958 184 184 LEU HD2 H 0.8724 0.01 2 959 184 184 LEU C C 179.2471 0.11 1 960 184 184 LEU CA C 57.5687 0.11 1 961 184 184 LEU CB C 40.0507 0.11 1 962 184 184 LEU CD1 C 22.5887 0.11 2 963 184 184 LEU CD2 C 27.2210 0.11 2 964 184 184 LEU N N 120.7033 0.07 1 965 185 185 VAL HG1 H 0.8285 0.01 2 966 185 185 VAL HG2 H 1.1697 0.01 2 967 185 185 VAL CG1 C 22.0671 0.11 2 968 185 185 VAL CG2 C 24.6480 0.11 2 969 188 188 MET C C 178.2954 0.11 1 970 188 188 MET CA C 57.6858 0.11 1 971 188 188 MET CB C 30.7759 0.11 1 972 189 189 ALA H H 8.8835 0.01 1 973 189 189 ALA C C 179.5846 0.11 1 974 189 189 ALA CA C 55.5761 0.11 1 975 189 189 ALA CB C 16.7742 0.11 1 976 189 189 ALA N N 121.4138 0.07 1 977 190 190 GLN H H 7.9276 0.01 1 978 190 190 GLN C C 180.2299 0.11 1 979 190 190 GLN CA C 58.7323 0.11 1 980 190 190 GLN N N 118.2666 0.07 1 981 191 191 GLN H H 8.1017 0.01 1 982 191 191 GLN C C 177.3420 0.11 1 983 191 191 GLN CA C 57.1662 0.11 1 984 191 191 GLN CB C 28.2395 0.11 1 985 191 191 GLN N N 115.7231 0.07 1 986 192 192 CYS H H 7.5012 0.01 1 987 192 192 CYS C C 172.3816 0.11 1 988 192 192 CYS CA C 58.2262 0.11 1 989 192 192 CYS CB C 27.7069 0.11 1 990 192 192 CYS N N 114.8265 0.07 1 991 193 193 ASP H H 7.4862 0.01 1 992 193 193 ASP C C 174.3846 0.11 1 993 193 193 ASP CA C 55.6596 0.11 1 994 193 193 ASP CB C 38.5421 0.11 1 995 193 193 ASP N N 118.3848 0.07 1 996 194 194 LEU H H 8.3435 0.01 1 997 194 194 LEU HD1 H 0.7150 0.01 2 998 194 194 LEU HD2 H 0.7120 0.01 2 999 194 194 LEU C C 176.7391 0.11 1 1000 194 194 LEU CA C 52.6716 0.11 1 1001 194 194 LEU CB C 45.3674 0.11 1 1002 194 194 LEU CD1 C 27.4210 0.11 2 1003 194 194 LEU CD2 C 22.3820 0.11 2 1004 194 194 LEU N N 118.2847 0.07 1 1005 195 195 GLU H H 7.8222 0.01 1 1006 195 195 GLU C C 177.0204 0.11 1 1007 195 195 GLU CA C 54.3169 0.11 1 1008 195 195 GLU CB C 30.8643 0.11 1 1009 195 195 GLU N N 118.8113 0.07 1 1010 196 196 VAL H H 8.4625 0.01 1 1011 196 196 VAL HG1 H 0.2260 0.01 2 1012 196 196 VAL HG2 H 0.7710 0.01 2 1013 196 196 VAL C C 175.5008 0.11 1 1014 196 196 VAL CA C 62.6535 0.11 1 1015 196 196 VAL CB C 31.8414 0.11 1 1016 196 196 VAL CG1 C 21.7530 0.11 2 1017 196 196 VAL CG2 C 17.9620 0.11 2 1018 196 196 VAL N N 114.9752 0.07 1 1019 197 197 GLY H H 8.3236 0.01 1 1020 197 197 GLY C C 172.0595 0.11 1 1021 197 197 GLY CA C 45.0715 0.11 1 1022 197 197 GLY N N 113.6985 0.07 1 1023 198 198 ASP H H 8.4835 0.01 1 1024 198 198 ASP C C 176.6349 0.11 1 1025 198 198 ASP CA C 52.7906 0.11 1 1026 198 198 ASP CB C 42.5893 0.11 1 1027 198 198 ASP N N 125.4745 0.07 1 1028 199 199 PHE H H 9.4210 0.01 1 1029 199 199 PHE C C 173.3684 0.11 1 1030 199 199 PHE CA C 55.1277 0.11 1 1031 199 199 PHE CB C 40.4910 0.11 1 1032 199 199 PHE N N 119.7318 0.07 1 1033 200 200 VAL H H 9.2507 0.01 1 1034 200 200 VAL HG1 H 0.3390 0.01 2 1035 200 200 VAL HG2 H 0.6480 0.01 2 1036 200 200 VAL C C 171.7795 0.11 1 1037 200 200 VAL CA C 60.3202 0.11 1 1038 200 200 VAL CB C 31.3325 0.11 1 1039 200 200 VAL CG1 C 20.8260 0.11 2 1040 200 200 VAL CG2 C 20.1390 0.11 2 1041 200 200 VAL N N 131.0171 0.07 1 1042 201 201 TRP H H 8.9264 0.01 1 1043 201 201 TRP C C 173.8762 0.11 1 1044 201 201 TRP CA C 58.3960 0.11 1 1045 201 201 TRP CB C 30.9158 0.11 1 1046 201 201 TRP N N 129.6998 0.07 1 1047 202 202 THR H H 7.5671 0.01 1 1048 202 202 THR C C 171.2465 0.11 1 1049 202 202 THR CA C 60.7806 0.11 1 1050 202 202 THR CB C 69.1079 0.11 1 1051 202 202 THR N N 125.0450 0.07 1 1052 203 203 GLY H H 7.6992 0.01 1 1053 203 203 GLY CA C 43.3119 0.11 1 1054 203 203 GLY N N 112.1830 0.07 1 1055 204 204 GLY H H 7.7191 0.01 1 1056 204 204 GLY C C 174.9364 0.11 1 1057 204 204 GLY CA C 44.8278 0.11 1 1058 204 204 GLY N N 107.6306 0.07 1 1059 205 205 ASP H H 7.6411 0.01 1 1060 205 205 ASP C C 174.3338 0.11 1 1061 205 205 ASP CA C 55.7384 0.11 1 1062 205 205 ASP CB C 40.9202 0.11 1 1063 205 205 ASP N N 129.1760 0.07 1 1064 206 206 THR H H 9.2752 0.01 1 1065 206 206 THR C C 172.2073 0.11 1 1066 206 206 THR CA C 63.5563 0.11 1 1067 206 206 THR CB C 68.3303 0.11 1 1068 206 206 THR N N 131.9570 0.07 1 1069 207 207 HIS H H 8.6313 0.01 1 1070 207 207 HIS C C 172.4288 0.11 1 1071 207 207 HIS CA C 52.9922 0.11 1 1072 207 207 HIS CB C 32.0951 0.11 1 1073 207 207 HIS N N 122.0647 0.07 1 1074 208 208 LEU H H 8.5298 0.01 1 1075 208 208 LEU HD1 H 0.9003 0.01 2 1076 208 208 LEU HD2 H 1.2210 0.01 2 1077 208 208 LEU CA C 51.1613 0.11 1 1078 208 208 LEU CD1 C 26.7289 0.11 2 1079 208 208 LEU CD2 C 24.2910 0.11 2 1080 208 208 LEU N N 119.6442 0.07 1 1081 209 209 TYR H H 8.7725 0.01 1 1082 209 209 TYR C C 178.9565 0.11 1 1083 209 209 TYR CA C 60.7961 0.11 1 1084 209 209 TYR CB C 37.7345 0.11 1 1085 209 209 TYR N N 122.9510 0.07 1 1086 210 210 SER H H 8.5807 0.01 1 1087 210 210 SER C C 174.6947 0.11 1 1088 210 210 SER CA C 60.8639 0.11 1 1089 210 210 SER CB C 62.4329 0.11 1 1090 210 210 SER N N 116.4866 0.07 1 1091 211 211 ASN H H 7.3655 0.01 1 1092 211 211 ASN C C 175.2205 0.11 1 1093 211 211 ASN CA C 51.5757 0.11 1 1094 211 211 ASN CB C 35.3299 0.11 1 1095 211 211 ASN N N 116.5393 0.07 1 1096 212 212 HIS H H 7.7674 0.01 1 1097 212 212 HIS C C 178.0556 0.11 1 1098 212 212 HIS CA C 52.9296 0.11 1 1099 212 212 HIS CB C 31.3703 0.11 1 1100 212 212 HIS N N 116.6658 0.07 1 1101 213 213 MET H H 7.4637 0.01 1 1102 213 213 MET C C 177.9938 0.11 1 1103 213 213 MET CA C 57.8167 0.11 1 1104 213 213 MET CB C 31.5452 0.11 1 1105 213 213 MET N N 123.5453 0.07 1 1106 214 214 ASP H H 9.2065 0.01 1 1107 214 214 ASP C C 179.6815 0.11 1 1108 214 214 ASP CA C 57.6002 0.11 1 1109 214 214 ASP CB C 38.8530 0.11 1 1110 214 214 ASP N N 123.1146 0.07 1 1111 215 215 GLN H H 9.4467 0.01 1 1112 215 215 GLN C C 177.1583 0.11 1 1113 215 215 GLN CA C 60.4421 0.11 1 1114 215 215 GLN CB C 25.3692 0.11 1 1115 215 215 GLN N N 123.1891 0.07 1 1116 216 216 THR H H 7.7301 0.01 1 1117 216 216 THR C C 175.7493 0.11 1 1118 216 216 THR CA C 67.5379 0.11 1 1119 216 216 THR N N 118.5545 0.07 1 1120 217 217 HIS H H 8.0212 0.01 1 1121 217 217 HIS C C 178.7481 0.11 1 1122 217 217 HIS CA C 60.1125 0.11 1 1123 217 217 HIS CB C 29.1050 0.11 1 1124 217 217 HIS N N 119.0415 0.07 1 1125 218 218 LEU H H 7.7088 0.01 1 1126 218 218 LEU HD1 H 0.8900 0.01 2 1127 218 218 LEU HD2 H 0.8998 0.01 2 1128 218 218 LEU C C 179.9178 0.11 1 1129 218 218 LEU CA C 57.4030 0.11 1 1130 218 218 LEU CB C 40.6966 0.11 1 1131 218 218 LEU CD1 C 22.6740 0.11 2 1132 218 218 LEU CD2 C 26.2047 0.11 2 1133 218 218 LEU N N 120.5273 0.07 1 1134 219 219 GLN H H 8.6056 0.01 1 1135 219 219 GLN C C 177.6780 0.11 1 1136 219 219 GLN CA C 61.0926 0.11 1 1137 219 219 GLN CB C 26.5228 0.11 1 1138 219 219 GLN N N 125.5622 0.07 1 1139 220 220 LEU H H 8.2491 0.01 1 1140 220 220 LEU HD1 H 0.5702 0.01 2 1141 220 220 LEU HD2 H 0.9030 0.01 2 1142 220 220 LEU C C 178.1717 0.11 1 1143 220 220 LEU CA C 56.2981 0.11 1 1144 220 220 LEU CB C 41.9042 0.11 1 1145 220 220 LEU CD1 C 26.7191 0.11 2 1146 220 220 LEU CD2 C 24.2810 0.11 2 1147 220 220 LEU N N 114.1813 0.07 1 1148 221 221 SER H H 7.5217 0.01 1 1149 221 221 SER C C 173.7672 0.11 1 1150 221 221 SER CB C 63.7150 0.11 1 1151 221 221 SER N N 114.8859 0.07 1 1152 222 222 ARG H H 7.5304 0.01 1 1153 222 222 ARG C C 174.6474 0.11 1 1154 222 222 ARG CA C 55.0766 0.11 1 1155 222 222 ARG CB C 30.5763 0.11 1 1156 222 222 ARG N N 124.5441 0.07 1 1157 223 223 GLU H H 8.4185 0.01 1 1158 223 223 GLU C C 174.9802 0.11 1 1159 223 223 GLU CB C 29.6039 0.11 1 1160 223 223 GLU N N 122.9162 0.07 1 1161 230 230 LEU HD1 H 0.1134 0.01 2 1162 230 230 LEU HD2 H 0.0076 0.01 2 1163 230 230 LEU C C 175.0810 0.11 1 1164 230 230 LEU CA C 53.6063 0.11 1 1165 230 230 LEU CB C 41.9222 0.11 1 1166 230 230 LEU CD1 C 21.9382 0.11 2 1167 230 230 LEU CD2 C 25.1251 0.11 2 1168 231 231 ILE H H 9.1060 0.01 1 1169 231 231 ILE HD1 H 0.6460 0.01 1 1170 231 231 ILE C C 174.5384 0.11 1 1171 231 231 ILE CA C 59.5096 0.11 1 1172 231 231 ILE CB C 38.8777 0.11 1 1173 231 231 ILE CD1 C 12.5502 0.11 1 1174 231 231 ILE N N 130.5504 0.07 1 1175 232 232 ILE H H 8.2495 0.01 1 1176 232 232 ILE HD1 H 0.8314 0.01 1 1177 232 232 ILE C C 178.4877 0.11 1 1178 232 232 ILE CA C 60.6192 0.11 1 1179 232 232 ILE CB C 36.6435 0.11 1 1180 232 232 ILE CD1 C 13.2642 0.11 1 1181 232 232 ILE N N 126.4637 0.07 1 1182 233 233 LYS H H 9.1152 0.01 1 1183 233 233 LYS C C 175.0829 0.11 1 1184 233 233 LYS CA C 57.8587 0.11 1 1185 233 233 LYS CB C 32.2165 0.11 1 1186 233 233 LYS N N 127.1503 0.07 1 1187 234 234 ARG H H 7.2309 0.01 1 1188 234 234 ARG C C 172.3286 0.11 1 1189 234 234 ARG CB C 32.5261 0.11 1 1190 234 234 ARG N N 116.8545 0.07 1 1191 235 235 LYS H H 8.2724 0.01 1 1192 235 235 LYS C C 173.8125 0.11 1 1193 235 235 LYS CA C 52.2233 0.11 1 1194 235 235 LYS CB C 32.3550 0.11 1 1195 235 235 LYS N N 123.0236 0.07 1 1196 236 236 PRO C C 176.0532 0.11 1 1197 236 236 PRO CA C 61.4391 0.11 1 1198 236 236 PRO CB C 32.1589 0.11 1 1199 237 237 GLU H H 8.9738 0.01 1 1200 237 237 GLU C C 175.3321 0.11 1 1201 237 237 GLU CA C 57.6462 0.11 1 1202 237 237 GLU CB C 29.0794 0.11 1 1203 237 237 GLU N N 118.9554 0.07 1 1204 238 238 SER H H 7.0136 0.01 1 1205 238 238 SER C C 174.8510 0.11 1 1206 238 238 SER CA C 56.0889 0.11 1 1207 238 238 SER CB C 66.0588 0.11 1 1208 238 238 SER N N 110.3235 0.07 1 1209 239 239 ILE H H 8.5348 0.01 1 1210 239 239 ILE HD1 H 0.7225 0.01 1 1211 239 239 ILE C C 172.9955 0.11 1 1212 239 239 ILE CA C 60.0806 0.11 1 1213 239 239 ILE CB C 38.2782 0.11 1 1214 239 239 ILE CD1 C 14.7015 0.11 1 1215 239 239 ILE N N 122.1890 0.07 1 1216 240 240 PHE H H 7.4047 0.01 1 1217 240 240 PHE C C 176.0602 0.11 1 1218 240 240 PHE CA C 57.0979 0.11 1 1219 240 240 PHE CB C 37.5240 0.11 1 1220 240 240 PHE N N 118.8113 0.07 1 1221 241 241 ASP H H 7.3025 0.01 1 1222 241 241 ASP C C 176.1413 0.11 1 1223 241 241 ASP CA C 53.5529 0.11 1 1224 241 241 ASP CB C 43.4097 0.11 1 1225 241 241 ASP N N 119.2861 0.07 1 1226 242 242 TYR H H 8.2619 0.01 1 1227 242 242 TYR C C 175.1860 0.11 1 1228 242 242 TYR CA C 59.9308 0.11 1 1229 242 242 TYR CB C 38.4081 0.11 1 1230 242 242 TYR N N 120.0863 0.07 1 1231 243 243 ARG H H 9.0409 0.01 1 1232 243 243 ARG C C 176.6895 0.11 1 1233 243 243 ARG CA C 53.0671 0.11 1 1234 243 243 ARG CB C 32.7748 0.11 1 1235 243 243 ARG N N 120.4314 0.07 1 1236 244 244 PHE H H 9.3976 0.01 1 1237 244 244 PHE C C 176.7697 0.11 1 1238 244 244 PHE CA C 61.8331 0.11 1 1239 244 244 PHE CB C 39.1143 0.11 1 1240 244 244 PHE N N 123.7040 0.07 1 1241 245 245 GLU H H 9.0404 0.01 1 1242 245 245 GLU C C 176.3245 0.11 1 1243 245 245 GLU CA C 57.7361 0.11 1 1244 245 245 GLU CB C 27.4220 0.11 1 1245 245 245 GLU N N 114.1544 0.07 1 1246 246 246 ASP H H 7.8286 0.01 1 1247 246 246 ASP C C 174.3799 0.11 1 1248 246 246 ASP CA C 55.8377 0.11 1 1249 246 246 ASP CB C 40.1906 0.11 1 1250 246 246 ASP N N 119.7304 0.07 1 1251 247 247 PHE H H 6.9154 0.01 1 1252 247 247 PHE C C 175.0153 0.11 1 1253 247 247 PHE CA C 56.0893 0.11 1 1254 247 247 PHE N N 116.2977 0.07 1 1255 248 248 GLU H H 8.9885 0.01 1 1256 248 248 GLU CA C 54.5215 0.11 1 1257 248 248 GLU CB C 32.5556 0.11 1 1258 248 248 GLU N N 124.3698 0.07 1 1259 249 249 ILE H H 8.5055 0.01 1 1260 249 249 ILE HD1 H 0.2061 0.01 1 1261 249 249 ILE C C 174.8607 0.11 1 1262 249 249 ILE CA C 57.5072 0.11 1 1263 249 249 ILE CB C 38.3041 0.11 1 1264 249 249 ILE CD1 C 13.0978 0.11 1 1265 249 249 ILE N N 124.1554 0.07 1 1266 250 250 GLU H H 9.1840 0.01 1 1267 250 250 GLU C C 176.7348 0.11 1 1268 250 250 GLU CA C 54.5782 0.11 1 1269 250 250 GLU CB C 31.9095 0.11 1 1270 250 250 GLU N N 129.9079 0.07 1 1271 251 251 GLY C C 175.1318 0.11 1 1272 251 251 GLY CA C 45.9795 0.11 1 1273 252 252 TYR H H 8.6634 0.01 1 1274 252 252 TYR C C 173.3032 0.11 1 1275 252 252 TYR CA C 55.4565 0.11 1 1276 252 252 TYR CB C 37.2564 0.11 1 1277 252 252 TYR N N 122.3354 0.07 1 1278 253 253 ASP H H 8.2810 0.01 1 1279 253 253 ASP C C 171.7562 0.11 1 1280 253 253 ASP CA C 50.5877 0.11 1 1281 253 253 ASP CB C 40.3285 0.11 1 1282 253 253 ASP N N 130.4880 0.07 1 1283 256 256 PRO C C 177.2772 0.11 1 1284 256 256 PRO CA C 63.2031 0.11 1 1285 256 256 PRO CB C 31.3495 0.11 1 1286 257 257 GLY H H 8.7918 0.01 1 1287 257 257 GLY C C 173.1273 0.11 1 1288 257 257 GLY CA C 45.4451 0.11 1 1289 257 257 GLY N N 108.5375 0.07 1 1290 258 258 ILE H H 8.2344 0.01 1 1291 258 258 ILE HD1 H 0.8810 0.01 1 1292 258 258 ILE C C 174.2732 0.11 1 1293 258 258 ILE CA C 60.4689 0.11 1 1294 258 258 ILE CB C 41.4142 0.11 1 1295 258 258 ILE CD1 C 13.8662 0.11 1 1296 258 258 ILE N N 123.5383 0.07 1 1297 259 259 LYS H H 8.5092 0.01 1 1298 259 259 LYS C C 176.4376 0.11 1 1299 259 259 LYS CA C 55.6143 0.11 1 1300 259 259 LYS CB C 32.1050 0.11 1 1301 259 259 LYS N N 128.4802 0.07 1 1302 260 260 ALA H H 8.6475 0.01 1 1303 260 260 ALA CA C 49.5240 0.11 1 1304 260 260 ALA N N 126.5272 0.07 1 1305 261 261 PRO C C 176.6484 0.11 1 1306 261 261 PRO CA C 61.2425 0.11 1 1307 261 261 PRO CB C 31.4503 0.11 1 1308 262 262 VAL H H 8.3425 0.01 1 1309 262 262 VAL HG1 H 0.9660 0.01 2 1310 262 262 VAL HG2 H 1.0440 0.01 2 1311 262 262 VAL C C 174.0914 0.11 1 1312 262 262 VAL CA C 60.2701 0.11 1 1313 262 262 VAL CB C 32.7039 0.11 1 1314 262 262 VAL CG1 C 19.2720 0.11 2 1315 262 262 VAL CG2 C 22.2080 0.11 2 1316 262 262 VAL N N 125.7096 0.07 1 1317 263 263 ALA H H 7.6458 0.01 1 1318 263 263 ALA C C 176.5260 0.11 1 1319 263 263 ALA CA C 51.0670 0.11 1 1320 263 263 ALA CB C 17.4175 0.11 1 1321 263 263 ALA N N 133.5817 0.07 1 1322 264 264 ILE H H 7.9118 0.01 1 1323 264 264 ILE HD1 H 0.5873 0.01 1 1324 264 264 ILE CB C 38.2453 0.11 1 1325 264 264 ILE CD1 C 13.3189 0.11 1 1326 264 264 ILE N N 129.8207 0.07 1 stop_ save_