data_16869 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Backbone assignment of the catalytic core of a Y-family DNA polymerase ; _BMRB_accession_number 16869 _BMRB_flat_file_name bmr16869.str _Entry_type original _Submission_date 2010-04-15 _Accession_date 2010-04-15 _Entry_origination author _NMR_STAR_version 2.1.1 _Experimental_method NMR _Details 'The first 20 residues in the sequence are an affinity tag (for the purpose of protein purification) and have sequential numbers -19 to 0.' loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Ma Dejian . . 2 Fowler Jason . . 3 Yuan Chunhua . . 4 Suo Zucai . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 185 "13C chemical shifts" 513 "15N chemical shifts" 185 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2010-10-05 update BMRB 'Update entry citation' 2010-07-27 original author 'original release' stop_ loop_ _Related_BMRB_accession_number _Relationship 17201 'little finger domain of Dpo4' stop_ save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title 'Backbone assignment of the catalytic core of a Y-family DNA polymerase.' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 20582735 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Ma Dejian . . 2 Fowler Jason D. . 3 Yuan Chunhua . . 4 Suo Zucai . . stop_ _Journal_abbreviation 'Biomol. NMR Assignments' _Journal_name_full 'Biomolecular NMR assignments' _Journal_volume 4 _Journal_issue 2 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 207 _Page_last 209 _Year 2010 _Details . save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name 'catalytic core of Dpo4' _Enzyme_commission_number 'EC 2.7.7.7' loop_ _Mol_system_component_name _Mol_label 'catalytic core of Dpo4' $Dpo4 stop_ _System_molecular_weight 27957.5 _System_physical_state native _System_oligomer_state ? _System_paramagnetic no _System_thiol_state . _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_Dpo4 _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common Dpo4 _Molecular_mass 27957.5 _Mol_thiol_state 'all free' loop_ _Biological_function 'DNA Repair Enzyme' stop_ _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 250 _Mol_residue_sequence ; MGSSHHHHHHSSGLVPRGSH MIVLFVDFDYFYAQVEEVLN PSLKGKPVVVCVFSGRFEDS GAVATANYEARKFGVKAGIP IVEAKKILPNAVYLPMRKEV YQQVSSRIMNLLREYSEKIE IASIDEAYLDISDKVRDYRE AYNLGLEIKNKILEKEKITV TVGISKNKVFAKIAADMAKP NGIKVIDDEEVKRLIRELDI ADVPGIGNITAEKLKKLGIN KLVDTLSIEFDKLKGMIGEA KAKYLISLAR ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 -19 MET 2 -18 GLY 3 -17 SER 4 -16 SER 5 -15 HIS 6 -14 HIS 7 -13 HIS 8 -12 HIS 9 -11 HIS 10 -10 HIS 11 -9 SER 12 -8 SER 13 -7 GLY 14 -6 LEU 15 -5 VAL 16 -4 PRO 17 -3 ARG 18 -2 GLY 19 -1 SER 20 0 HIS 21 1 MET 22 2 ILE 23 3 VAL 24 4 LEU 25 5 PHE 26 6 VAL 27 7 ASP 28 8 PHE 29 9 ASP 30 10 TYR 31 11 PHE 32 12 TYR 33 13 ALA 34 14 GLN 35 15 VAL 36 16 GLU 37 17 GLU 38 18 VAL 39 19 LEU 40 20 ASN 41 21 PRO 42 22 SER 43 23 LEU 44 24 LYS 45 25 GLY 46 26 LYS 47 27 PRO 48 28 VAL 49 29 VAL 50 30 VAL 51 31 CYS 52 32 VAL 53 33 PHE 54 34 SER 55 35 GLY 56 36 ARG 57 37 PHE 58 38 GLU 59 39 ASP 60 40 SER 61 41 GLY 62 42 ALA 63 43 VAL 64 44 ALA 65 45 THR 66 46 ALA 67 47 ASN 68 48 TYR 69 49 GLU 70 50 ALA 71 51 ARG 72 52 LYS 73 53 PHE 74 54 GLY 75 55 VAL 76 56 LYS 77 57 ALA 78 58 GLY 79 59 ILE 80 60 PRO 81 61 ILE 82 62 VAL 83 63 GLU 84 64 ALA 85 65 LYS 86 66 LYS 87 67 ILE 88 68 LEU 89 69 PRO 90 70 ASN 91 71 ALA 92 72 VAL 93 73 TYR 94 74 LEU 95 75 PRO 96 76 MET 97 77 ARG 98 78 LYS 99 79 GLU 100 80 VAL 101 81 TYR 102 82 GLN 103 83 GLN 104 84 VAL 105 85 SER 106 86 SER 107 87 ARG 108 88 ILE 109 89 MET 110 90 ASN 111 91 LEU 112 92 LEU 113 93 ARG 114 94 GLU 115 95 TYR 116 96 SER 117 97 GLU 118 98 LYS 119 99 ILE 120 100 GLU 121 101 ILE 122 102 ALA 123 103 SER 124 104 ILE 125 105 ASP 126 106 GLU 127 107 ALA 128 108 TYR 129 109 LEU 130 110 ASP 131 111 ILE 132 112 SER 133 113 ASP 134 114 LYS 135 115 VAL 136 116 ARG 137 117 ASP 138 118 TYR 139 119 ARG 140 120 GLU 141 121 ALA 142 122 TYR 143 123 ASN 144 124 LEU 145 125 GLY 146 126 LEU 147 127 GLU 148 128 ILE 149 129 LYS 150 130 ASN 151 131 LYS 152 132 ILE 153 133 LEU 154 134 GLU 155 135 LYS 156 136 GLU 157 137 LYS 158 138 ILE 159 139 THR 160 140 VAL 161 141 THR 162 142 VAL 163 143 GLY 164 144 ILE 165 145 SER 166 146 LYS 167 147 ASN 168 148 LYS 169 149 VAL 170 150 PHE 171 151 ALA 172 152 LYS 173 153 ILE 174 154 ALA 175 155 ALA 176 156 ASP 177 157 MET 178 158 ALA 179 159 LYS 180 160 PRO 181 161 ASN 182 162 GLY 183 163 ILE 184 164 LYS 185 165 VAL 186 166 ILE 187 167 ASP 188 168 ASP 189 169 GLU 190 170 GLU 191 171 VAL 192 172 LYS 193 173 ARG 194 174 LEU 195 175 ILE 196 176 ARG 197 177 GLU 198 178 LEU 199 179 ASP 200 180 ILE 201 181 ALA 202 182 ASP 203 183 VAL 204 184 PRO 205 185 GLY 206 186 ILE 207 187 GLY 208 188 ASN 209 189 ILE 210 190 THR 211 191 ALA 212 192 GLU 213 193 LYS 214 194 LEU 215 195 LYS 216 196 LYS 217 197 LEU 218 198 GLY 219 199 ILE 220 200 ASN 221 201 LYS 222 202 LEU 223 203 VAL 224 204 ASP 225 205 THR 226 206 LEU 227 207 SER 228 208 ILE 229 209 GLU 230 210 PHE 231 211 ASP 232 212 LYS 233 213 LEU 234 214 LYS 235 215 GLY 236 216 MET 237 217 ILE 238 218 GLY 239 219 GLU 240 220 ALA 241 221 LYS 242 222 ALA 243 223 LYS 244 224 TYR 245 225 LEU 246 226 ILE 247 227 SER 248 228 LEU 249 229 ALA 250 230 ARG stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-09-30 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 1JX4 "Crystal Structure Of A Y-Family Dna Polymerase In A Ternary Complex With Dna Substrates And An Incoming Nucleotide" 91.60 352 98.25 98.25 1.12e-152 PDB 1JXL "Crystal Structure Of A Y-Family Dna Polymerase In A Ternary Complex With Dna Substrates And An Incoming Nucleotide" 92.00 352 100.00 100.00 8.32e-158 PDB 1N48 "Y-Family Dna Polymerase Dpo4 In Complex With Dna Containing Abasic Lesion" 92.00 352 100.00 100.00 8.32e-158 PDB 1N56 "Y-Family Dna Polymerase Dpo4 In Complex With Dna Containing Abasic Lesion" 92.00 352 100.00 100.00 8.32e-158 PDB 1RYR "Replication Of A Cis-Syn Thymine Dimer At Atomic Resolution" 92.00 352 100.00 100.00 8.32e-158 PDB 1RYS "Replication Of A Cis-Syn Thymine Dimer At Atomic Resolution" 92.00 352 100.00 100.00 8.32e-158 PDB 1S0M "Crystal Structure Of A Benzo[a]pyrene Diol Epoxide Adduct In A Ternary Complex With A Dna Polymerase" 92.00 352 100.00 100.00 8.32e-158 PDB 1S0N "Snapshots Of Replication Through An Abasic Lesion: Structural Basis For Base Substitution And Frameshift" 92.00 352 100.00 100.00 8.32e-158 PDB 1S0O "Snapshots Of Replication Through An Abasic Lesion: Structural Basis For Base Substitution And Frameshift" 92.00 352 100.00 100.00 8.32e-158 PDB 1S10 "Snapshots Of Replication Through An Abasic Lesion: Structural Basis For Base Substitution And Frameshift" 92.00 352 100.00 100.00 8.32e-158 PDB 1S97 "Dpo4 With Gt Mismatch" 92.00 352 100.00 100.00 8.32e-158 PDB 1S9F "Dpo With At Matched" 92.00 352 100.00 100.00 8.32e-158 PDB 2AGO "Fidelity Of Dpo4: Effect Of Metal Ions, Nucleotide Selection And Pyrophosphorolysis" 92.00 341 100.00 100.00 3.28e-158 PDB 2AGP "Fidelity Of Dpo4: Effect Of Metal Ions, Nucleotide Selection And Pyrophosphorolysis" 92.00 341 100.00 100.00 3.28e-158 PDB 2AGQ "Fidelity Of Dpo4: Effect Of Metal Ions, Nucleotide Selection And Pyrophosphorolysis" 92.00 341 100.00 100.00 3.28e-158 PDB 2ASD "Oxog-Modified Insertion Ternary Complex" 95.20 360 97.90 97.90 6.37e-158 PDB 2ASJ "Oxog-Modified Preinsertion Binary Complex" 95.20 360 97.90 97.90 6.37e-158 PDB 2ASL "Oxog-Modified Postinsertion Binary Complex" 95.20 360 97.90 97.90 6.37e-158 PDB 2ATL "Unmodified Insertion Ternary Complex" 95.20 360 97.90 97.90 6.37e-158 PDB 2AU0 "Unmodified Preinsertion Binary Complex" 95.20 360 97.90 97.90 6.37e-158 PDB 2IA6 "Bypass Of Major Benzopyrene-Dg Adduct By Y-Family Dna Polymerase With Unique Structural Gap" 92.00 352 100.00 100.00 8.32e-158 PDB 2IBK "Bypass Of Major Benzopyrene-Dg Adduct By Y-Family Dna Polymerase With Unique Structural Gap" 92.00 352 100.00 100.00 8.32e-158 PDB 2IMW "Mechanism Of Template-Independent Nucleotide Incorporation Catalyzed By A Template-Dependent Dna Polymerase" 92.00 348 100.00 100.00 5.69e-158 PDB 2R8G "Selectivity Of Nucleoside Triphosphate Incorporation Opposite 1,N2-Propanodeoxyguanosine (Pdg) By The Sulfolobus Solfataricus D" 92.00 352 100.00 100.00 8.32e-158 PDB 2R8H "Selectivity Of Nucleoside Triphosphate Incorporation Opposite 1,N2- Propanodeoxyguanosine (Pdg) By The Sulfolobus Solfataricus " 92.00 352 100.00 100.00 8.32e-158 PDB 2R8I "Selectivity Of Nucleoside Triphosphate Incorporation Opposite 1,N2-Propanodeoxyguanosine (Pdg) By The Sulfolobus Solfataricus D" 92.00 352 100.00 100.00 8.32e-158 PDB 2RDI "Snapshots Of A Y-family Dna Polymerase In Replication: Dpo4 In Apo And Binary/ternary Complex Forms" 92.00 342 100.00 100.00 2.82e-158 PDB 2RDJ "Snapshots Of A Y-family Dna Polymerase In Replication: Dpo4 In Apo And Binary/ternary Complex Forms" 92.00 352 100.00 100.00 8.32e-158 PDB 3FDS "Structural Insight Into Recruitment Of Translesion Dna Polymerase Dpo4 To Sliding Clamp Pcna" 92.00 352 100.00 100.00 8.32e-158 PDB 3GII "Dpo4 Extension Ternary Complex With Disordered A Opposite An Oxog In Anti Conformation" 91.60 341 100.00 100.00 3.79e-157 PDB 3GIJ "Dpo4 Extension Ternary Complex With Oxog(Syn)-A(Anti) And Oxog(Anti)- A(Syn) Pairs" 91.60 341 100.00 100.00 3.79e-157 PDB 3GIK "Dpo4 Extension Ternary Complex With The Oxog(Anti)-C(Anti) Pair" 91.60 341 100.00 100.00 3.79e-157 PDB 3GIL "Dpo4 Extension Ternary Complex With Oxog(Anti)-T(Anti) Pair" 91.60 341 100.00 100.00 3.79e-157 PDB 3GIM "Dpo4 Extension Ternary Complex With Oxog(Anti)-G(Syn) Pair" 91.60 341 100.00 100.00 3.79e-157 PDB 3KHG "Dpo4 Extension Ternary Complex With Misinserted A Opposite The 2- Aminofluorene-Guanine [af]g Lesion" 91.60 341 100.00 100.00 3.79e-157 PDB 3KHH "Dpo4 Extension Ternary Complex With A C Base Opposite The 2- Aminofluorene-Guanine [af]g Lesion" 91.60 341 100.00 100.00 3.79e-157 PDB 3KHL "Dpo4 Post-Extension Ternary Complex With Misinserted A Opposite The 2- Aminofluorene-Guanine [af]g Lesion" 91.60 341 100.00 100.00 3.79e-157 PDB 3KHR "Dpo4 Post-Extension Ternary Complex With The Correct C Opposite The 2- Aminofluorene-Guanine [af]g Lesion" 91.60 341 100.00 100.00 3.79e-157 PDB 3M9M "Crystal Structure Of Dpo4 In Complex With Dna Containing The Major Cisplatin Lesion" 92.00 352 100.00 100.00 8.32e-158 PDB 3M9N "Crystal Structure Of Dpo4 In Complex With Dna Containing The Major Cisplatin Lesion" 92.00 352 100.00 100.00 8.32e-158 PDB 3M9O "Crystal Structure Of Dpo4 In Complex With Dna Containing The Major Cisplatin Lesion" 92.00 352 100.00 100.00 8.32e-158 PDB 3PR4 "Dpo4 Y12a Mutant Incorporating Dadp Opposite Template Dt" 92.00 341 99.57 99.57 6.33e-157 PDB 3PR5 "Dpo4 Y12a Mutant Incorporating Adp Opposite Template Dt" 92.00 341 99.57 99.57 6.33e-157 PDB 3QZ7 "T-3 Ternary Complex Of Dpo4" 92.00 360 100.00 100.00 5.01e-157 PDB 3QZ8 "Tt-4 Ternary Complex Of Dpo4" 92.00 360 100.00 100.00 5.01e-157 PDB 3RAQ "Dpo4 Extension Ternary Complex With 3'-terminal Primer C Base Opposite The 1-methylguanine (mg1) Lesion" 91.60 341 100.00 100.00 3.79e-157 PDB 3RAX "Dpo4 Extension Ternary Complex With 3'-terminal Primer T Base Opposite The 1-methylguanine (m1g) Lesion" 91.60 341 100.00 100.00 3.79e-157 PDB 3RB0 "Dpo4 Extension Ternary Complex With 3'-terminal Primer G Base Opposite The 1-methylguanine (m1g) Lesion" 91.60 341 100.00 100.00 3.79e-157 PDB 3RB3 "Dpo4 Extension Ternary Complex With 3'-terminal Primer A Base Opposite The 1-methylguanine (m1g) Lesion" 91.60 341 100.00 100.00 3.79e-157 PDB 3RB4 "Dpo4 Extension Ternary Complex With 3'-terminal Primer G Base Opposite The 3-methylcytosine (m3c) Lesion" 91.60 341 100.00 100.00 3.79e-157 PDB 3RB6 "Dpo4 Extension Ternary Complex With 3'-terminal Primer A Base Opposite The 3-methylcytosine (m3c) Lesion" 91.60 341 100.00 100.00 3.79e-157 PDB 3RBD "Dpo4 Extension Ternary Complex With 3'-terminal Primer C Base Opposite The 3-methylcytosine (m3c) Lesion" 91.60 341 100.00 100.00 3.79e-157 PDB 3RBE "Dpo4 Extension Ternary Complex With 3'-terminal Primer T Base Opposite The 3-methylcytosine (m3c) Lesion" 91.60 341 100.00 100.00 3.79e-157 PDB 3T5H "Ternary Complex Of Hne Adduct Modified Dna (5'-Cxg-3' Vs 13-Mer) With Dpo4 And Incoming Ddgt" 92.00 341 100.00 100.00 3.28e-158 PDB 3T5J "Ternary Complex Of Hne Adduct Modified Dna (5'-Txg-3' Vs 13-Mer) With Dpo4 And Incoming Ddtp" 92.00 341 100.00 100.00 3.28e-158 PDB 3T5K "Ternary Complex Of Hne Adduct Modified Dna (5'-Txg-3' Vs 14-Mer) With Dpo4 And Incoming Ddtp" 92.00 341 100.00 100.00 3.28e-158 PDB 3T5L "Ternary Complex Of Hne Adduct Modified Dna (5'-Cxg-3' Vs 14-Mer) With Dpo4 And Incoming Ddgt" 92.00 341 100.00 100.00 3.28e-158 PDB 4F4Z "Y-family Dna Polymerase Chimera Dpo4-dpo4-dbh" 92.00 361 100.00 100.00 6.11e-157 PDB 4FBT "Dpo4 Post-insertion Complex With The N-(deoxyguanosin-8-yl)-1- Aminopyrene Lesion" 92.00 341 100.00 100.00 3.28e-158 PDB 4FBU "Dpo4 Polymerase Pre-insertion Binary Complex With The N- (deoxyguanosin-8-yl)-1-aminopyrene Lesion" 92.00 341 100.00 100.00 3.28e-158 PDB 4G3I "Crystal Structure Of Dpo4 In Complex With Dna Duplex" 92.00 342 100.00 100.00 3.01e-158 PDB 4QW8 "Ternary Crystal Structures Of A Y-family Dna Polymerase Dpo4 From Sulfolobus Solfataricus In Complex With Dna And D-dctp" 92.00 349 100.00 100.00 1.04e-157 PDB 4QW9 "Ternary Crystal Structures Of A Y-family Dna Polymerase Dpo4 From Sulfolobus Solfataricus In Complex With Dna And (-)ftc-ppnp" 92.00 349 100.00 100.00 1.04e-157 PDB 4QWA "Ternary Crystal Structures Of A Y-family Dna Polymerase Dpo4 From Sulfolobus Solfataricus In Complex With Dna And (-)3tc-dp" 92.00 349 100.00 100.00 1.04e-157 PDB 4QWB "Crystal Structure Of Dpo4 Linker Region P236a Mutant With An Incoming D-dcdp" 92.00 343 100.00 100.00 3.02e-158 PDB 4QWC "Ternary Crystal Structures Of A Y-family Dna Polymerase Dpo4 From Sulfolobus Solfataricus In Complex With Dna And L-dcdp" 92.00 343 100.00 100.00 4.28e-158 PDB 4QWD "Ternary Crystal Structures Of A Y-family Dna Polymerase Dpo4 From Sulfolobus Solfataricus In Complex With Dna And (-)3tc-ppnp" 92.00 349 100.00 100.00 1.04e-157 PDB 4QWE "Ternary Crystal Structures Of A Y-family Dna Polymerase Dpo4 From Sulfolobus Solfataricus In Complex With Dna And (-)ftc-dp" 92.00 349 100.00 100.00 1.04e-157 PDB 4RUA "Crystal Structure Of Y-family Dna Polymerase Dpo4 Bypassing A Mefapy- Dg Adduct" 92.00 341 100.00 100.00 3.28e-158 PDB 4RUC "Crystal Structure Of Y-family Dna Polymerase Dpo4 Extending From A Mefapy-dg:dc Pair" 92.00 341 100.00 100.00 3.28e-158 PDB 4RZR "Bypass Of A Bulky Adduct Dg1,8 By Dpo4" 92.00 352 100.00 100.00 8.32e-158 PDB 4TQR "Ternary Complex Of Y-family Dna Polymerase Dpo4 With (5's)-8,5'-cyclo- 2'-deoxyguanosine And Dttp" 92.00 342 100.00 100.00 3.87e-158 GB AAK42588 "DNA polymerase IV (family Y) (dpo4) [Sulfolobus solfataricus P2]" 92.00 352 100.00 100.00 8.32e-158 GB ACX90547 "DNA-directed DNA polymerase [Sulfolobus solfataricus 98/2]" 92.00 352 100.00 100.00 8.32e-158 GB AKA72680 "DNA polymerase IV [Sulfolobus solfataricus]" 92.00 352 100.00 100.00 8.32e-158 GB AKA75380 "DNA polymerase IV [Sulfolobus solfataricus]" 92.00 352 100.00 100.00 8.32e-158 GB AKA78071 "DNA polymerase IV [Sulfolobus solfataricus]" 92.00 352 100.00 100.00 8.32e-158 REF WP_009993137 "DNA polymerase IV [Sulfolobus solfataricus]" 92.00 352 100.00 100.00 8.32e-158 SP Q97W02 "RecName: Full=DNA polymerase IV; Short=Pol IV" 92.00 352 100.00 100.00 8.32e-158 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species _Strain _Gene_mnemonic $Dpo4 'Sulfolobus solfataricus' 2287 Archaea . Sulfolobus solfataricus P2 dinP 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 _Details $Dpo4 'recombinant technology' . Escherichia coli BL21(DE3) pET22b 'Vector contains the gene for Dpo4.' 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 $Dpo4 0.2 mM '[U-100% 13C; U-100% 15N]' H2O 95 % 'natural abundance' D2O 5 % 'natural abundance' stop_ save_ ############################ # Computer software used # ############################ save_xwinnmr _Saveframe_category software _Name xwinnmr _Version . loop_ _Vendor _Address _Electronic_address 'Bruker Biospin' . . stop_ loop_ _Task collection stop_ _Details . save_ save_NMRPipe _Saveframe_category software _Name NMRPipe _Version . loop_ _Vendor _Address _Electronic_address 'Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax' . . stop_ loop_ _Task 'peak picking' processing stop_ _Details . save_ save_SPARKY _Saveframe_category software _Name SPARKY _Version . loop_ _Vendor _Address _Electronic_address Goddard . . stop_ loop_ _Task 'chemical shift assignment' 'data analysis' 'peak picking' stop_ _Details . save_ save_MARS _Saveframe_category software _Name MARS _Version . loop_ _Vendor _Address _Electronic_address 'Jung and Zweckstetter' . . stop_ loop_ _Task 'chemical shift assignment' 'data analysis' stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model DRX _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_CBCA(CO)NH_3 _Saveframe_category NMR_applied_experiment _Experiment_name '3D CBCA(CO)NH' _Sample_label $sample_1 save_ save_3D_HNCO_4 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCO' _Sample_label $sample_1 save_ save_3D_HNCA_5 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCA' _Sample_label $sample_1 save_ save_3D_HN(CO)CA_6 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HN(CO)CA' _Sample_label $sample_1 save_ save_3D_1H-15N_NOESY_7 _Saveframe_category NMR_applied_experiment _Experiment_name '3D 1H-15N NOESY' _Sample_label $sample_1 save_ ####################### # Sample conditions # ####################### save_sample_conditions_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units 'ionic strength' 170 . mM pH 7.0 . pH pressure 1 . atm temperature 323 . 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 water C 13 protons ppm 4.51 internal indirect . . . 0.251449530 water H 1 protons ppm 4.51 internal direct . . . 1.0 water N 15 protons ppm 4.51 internal 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 CBCA(CO)NH' '3D HNCO' '3D HNCA' 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 'catalytic core of Dpo4' _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 21 MET C C 175.339 0.200 1 2 1 21 MET CB C 34.863 0.200 1 3 2 22 ILE H H 8.281 0.020 1 4 2 22 ILE C C 173.333 0.200 1 5 2 22 ILE CA C 62.502 0.200 1 6 2 22 ILE CB C 40.878 0.200 1 7 2 22 ILE N N 122.408 0.200 1 8 3 23 VAL H H 8.818 0.020 1 9 3 23 VAL C C 172.476 0.200 1 10 3 23 VAL CA C 60.717 0.200 1 11 3 23 VAL CB C 34.451 0.200 1 12 3 23 VAL N N 125.746 0.200 1 13 4 24 LEU H H 9.098 0.020 1 14 4 24 LEU CA C 54.055 0.200 1 15 4 24 LEU N N 128.639 0.200 1 16 6 26 VAL C C 170.819 0.200 1 17 6 26 VAL CB C 32.985 0.200 1 18 7 27 ASP H H 8.146 0.020 1 19 7 27 ASP C C 177.004 0.200 1 20 7 27 ASP CA C 51.025 0.200 1 21 7 27 ASP CB C 43.804 0.200 1 22 7 27 ASP N N 125.142 0.200 1 23 8 28 PHE H H 8.306 0.020 1 24 8 28 PHE C C 175.108 0.200 1 25 8 28 PHE CA C 54.286 0.200 1 26 8 28 PHE N N 124.535 0.200 1 27 9 29 ASP H H 7.409 0.020 1 28 9 29 ASP CA C 55.924 0.200 1 29 9 29 ASP N N 122.885 0.200 1 30 11 31 PHE C C 176.815 0.200 1 31 12 32 TYR H H 8.378 0.020 1 32 12 32 TYR C C 177.377 0.200 1 33 12 32 TYR CA C 57.562 0.200 1 34 12 32 TYR CB C 36.991 0.200 1 35 12 32 TYR N N 113.745 0.200 1 36 13 33 ALA H H 6.694 0.020 1 37 13 33 ALA C C 178.134 0.200 1 38 13 33 ALA CA C 54.164 0.200 1 39 13 33 ALA CB C 18.528 0.200 1 40 13 33 ALA N N 113.256 0.200 1 41 14 34 GLN H H 8.337 0.020 1 42 14 34 GLN C C 178.605 0.200 1 43 14 34 GLN CA C 59.993 0.200 1 44 14 34 GLN CB C 28.099 0.200 1 45 14 34 GLN N N 119.618 0.200 1 46 15 35 VAL H H 8.200 0.020 1 47 15 35 VAL C C 177.824 0.200 1 48 15 35 VAL CA C 67.294 0.200 1 49 15 35 VAL N N 117.114 0.200 1 50 16 36 GLU H H 7.068 0.020 1 51 16 36 GLU C C 179.515 0.200 1 52 16 36 GLU CA C 58.903 0.200 1 53 16 36 GLU N N 115.414 0.200 1 54 17 37 GLU H H 7.738 0.020 1 55 17 37 GLU C C 177.947 0.200 1 56 17 37 GLU CA C 58.961 0.200 1 57 17 37 GLU CB C 30.261 0.200 1 58 17 37 GLU N N 119.135 0.200 1 59 18 38 VAL H H 7.959 0.020 1 60 18 38 VAL C C 177.562 0.200 1 61 18 38 VAL CA C 65.993 0.200 1 62 18 38 VAL N N 119.152 0.200 1 63 19 39 LEU H H 7.933 0.020 1 64 19 39 LEU C C 177.740 0.200 1 65 19 39 LEU CA C 56.467 0.200 1 66 19 39 LEU CB C 42.316 0.200 1 67 19 39 LEU N N 117.923 0.200 1 68 20 40 ASN H H 7.543 0.020 1 69 20 40 ASN CA C 49.994 0.200 1 70 20 40 ASN N N 114.281 0.200 1 71 22 42 SER C C 175.170 0.200 1 72 22 42 SER CB C 63.010 0.200 1 73 23 43 LEU H H 8.337 0.020 1 74 23 43 LEU C C 176.689 0.200 1 75 23 43 LEU CA C 55.447 0.200 1 76 23 43 LEU CB C 42.277 0.200 1 77 23 43 LEU N N 119.618 0.200 1 78 24 44 LYS H H 7.127 0.020 1 79 24 44 LYS CA C 58.533 0.200 1 80 24 44 LYS N N 116.659 0.200 1 81 25 45 GLY C C 174.138 0.200 1 82 26 46 LYS H H 7.478 0.020 1 83 26 46 LYS CA C 60.299 0.200 1 84 26 46 LYS N N 119.646 0.200 1 85 27 47 PRO C C 174.865 0.200 1 86 27 47 PRO CA C 62.561 0.200 1 87 27 47 PRO CB C 30.606 0.200 1 88 28 48 VAL H H 7.845 0.020 1 89 28 48 VAL C C 173.592 0.200 1 90 28 48 VAL CA C 61.808 0.200 1 91 28 48 VAL N N 125.373 0.200 1 92 29 49 VAL H H 8.717 0.020 1 93 29 49 VAL C C 174.283 0.200 1 94 29 49 VAL CA C 60.935 0.200 1 95 29 49 VAL N N 126.689 0.200 1 96 30 50 VAL H H 8.813 0.020 1 97 30 50 VAL C C 176.711 0.200 1 98 30 50 VAL CA C 61.928 0.200 1 99 30 50 VAL N N 127.067 0.200 1 100 31 51 CYS H H 9.387 0.020 1 101 31 51 CYS C C 172.443 0.200 1 102 31 51 CYS CA C 58.859 0.200 1 103 31 51 CYS CB C 31.405 0.200 1 104 31 51 CYS N N 126.817 0.200 1 105 32 52 VAL H H 8.777 0.020 1 106 32 52 VAL CA C 60.967 0.200 1 107 32 52 VAL N N 121.155 0.200 1 108 36 56 ARG C C 174.052 0.200 1 109 36 56 ARG CB C 30.804 0.200 1 110 37 57 PHE H H 7.622 0.020 1 111 37 57 PHE CA C 57.713 0.200 1 112 37 57 PHE N N 125.529 0.200 1 113 39 59 ASP C C 174.915 0.200 1 114 39 59 ASP CB C 40.730 0.200 1 115 40 60 SER H H 7.905 0.020 1 116 40 60 SER CA C 58.374 0.200 1 117 40 60 SER N N 115.062 0.200 1 118 41 61 GLY C C 173.294 0.200 1 119 42 62 ALA H H 8.353 0.020 1 120 42 62 ALA C C 176.183 0.200 1 121 42 62 ALA CA C 50.551 0.200 1 122 42 62 ALA CB C 22.508 0.200 1 123 42 62 ALA N N 122.698 0.200 1 124 43 63 VAL H H 8.562 0.020 1 125 43 63 VAL C C 176.414 0.200 1 126 43 63 VAL CA C 64.355 0.200 1 127 43 63 VAL CB C 31.592 0.200 1 128 43 63 VAL N N 120.226 0.200 1 129 44 64 ALA H H 9.897 0.020 1 130 44 64 ALA C C 177.497 0.200 1 131 44 64 ALA CA C 53.808 0.200 1 132 44 64 ALA CB C 19.659 0.200 1 133 44 64 ALA N N 133.521 0.200 1 134 45 65 THR H H 7.774 0.020 1 135 45 65 THR CA C 62.216 0.200 1 136 45 65 THR N N 109.072 0.200 1 137 46 66 ALA C C 181.609 0.200 1 138 46 66 ALA CB C 17.779 0.200 1 139 47 67 ASN H H 8.780 0.020 1 140 47 67 ASN CA C 58.963 0.200 1 141 47 67 ASN N N 117.975 0.200 1 142 48 68 TYR C C 177.123 0.200 1 143 48 68 TYR CB C 37.439 0.200 1 144 49 69 GLU H H 8.081 0.020 1 145 49 69 GLU CA C 59.824 0.200 1 146 49 69 GLU N N 118.538 0.200 1 147 50 70 ALA C C 178.148 0.200 1 148 50 70 ALA CB C 17.873 0.200 1 149 51 71 ARG H H 8.229 0.020 1 150 51 71 ARG C C 178.290 0.200 1 151 51 71 ARG CA C 59.242 0.200 1 152 51 71 ARG CB C 28.371 0.200 1 153 51 71 ARG N N 114.615 0.200 1 154 52 72 LYS H H 7.639 0.020 1 155 52 72 LYS C C 177.231 0.200 1 156 52 72 LYS CA C 58.978 0.200 1 157 52 72 LYS CB C 31.400 0.200 1 158 52 72 LYS N N 120.094 0.200 1 159 53 73 PHE H H 7.168 0.020 1 160 53 73 PHE C C 175.384 0.200 1 161 53 73 PHE CA C 58.623 0.200 1 162 53 73 PHE CB C 40.247 0.200 1 163 53 73 PHE N N 115.190 0.200 1 164 54 74 GLY H H 7.789 0.020 1 165 54 74 GLY C C 174.119 0.200 1 166 54 74 GLY CA C 44.804 0.200 1 167 54 74 GLY N N 104.367 0.200 1 168 55 75 VAL H H 6.996 0.020 1 169 55 75 VAL C C 172.561 0.200 1 170 55 75 VAL CA C 64.231 0.200 1 171 55 75 VAL CB C 30.596 0.200 1 172 55 75 VAL N N 119.418 0.200 1 173 56 76 LYS H H 6.357 0.020 1 174 56 76 LYS CA C 53.787 0.200 1 175 56 76 LYS N N 121.206 0.200 1 176 57 77 ALA C C 178.510 0.200 1 177 57 77 ALA CB C 18.773 0.200 1 178 58 78 GLY H H 8.740 0.020 1 179 58 78 GLY C C 174.609 0.200 1 180 58 78 GLY CA C 45.174 0.200 1 181 58 78 GLY N N 108.513 0.200 1 182 59 79 ILE H H 7.198 0.020 1 183 59 79 ILE CA C 59.649 0.200 1 184 59 79 ILE N N 116.273 0.200 1 185 60 80 PRO C C 178.477 0.200 1 186 60 80 PRO CA C 62.827 0.200 1 187 60 80 PRO CB C 32.957 0.200 1 188 61 81 ILE H H 8.250 0.020 1 189 61 81 ILE C C 177.435 0.200 1 190 61 81 ILE CA C 65.207 0.200 1 191 61 81 ILE N N 126.162 0.200 1 192 62 82 VAL H H 8.197 0.020 1 193 62 82 VAL C C 177.550 0.200 1 194 62 82 VAL CA C 65.566 0.200 1 195 62 82 VAL CB C 31.171 0.200 1 196 62 82 VAL N N 114.823 0.200 1 197 63 83 GLU H H 6.726 0.020 1 198 63 83 GLU C C 178.887 0.200 1 199 63 83 GLU CA C 58.234 0.200 1 200 63 83 GLU CB C 29.315 0.200 1 201 63 83 GLU N N 118.162 0.200 1 202 64 84 ALA H H 7.905 0.020 1 203 64 84 ALA CA C 55.616 0.200 1 204 64 84 ALA N N 123.004 0.200 1 205 65 85 LYS C C 177.804 0.200 1 206 65 85 LYS CB C 32.368 0.200 1 207 66 86 LYS H H 7.011 0.020 1 208 66 86 LYS C C 178.043 0.200 1 209 66 86 LYS CA C 58.640 0.200 1 210 66 86 LYS CB C 32.376 0.200 1 211 66 86 LYS N N 116.782 0.200 1 212 67 87 ILE H H 7.173 0.020 1 213 67 87 ILE C C 175.902 0.200 1 214 67 87 ILE CA C 63.377 0.200 1 215 67 87 ILE CB C 39.363 0.200 1 216 67 87 ILE N N 116.935 0.200 1 217 68 88 LEU H H 8.449 0.020 1 218 68 88 LEU CA C 51.323 0.200 1 219 68 88 LEU N N 118.758 0.200 1 220 70 90 ASN C C 175.896 0.200 1 221 70 90 ASN CB C 38.858 0.200 1 222 71 91 ALA H H 8.942 0.020 1 223 71 91 ALA C C 173.888 0.200 1 224 71 91 ALA CA C 51.425 0.200 1 225 71 91 ALA CB C 18.817 0.200 1 226 71 91 ALA N N 124.897 0.200 1 227 72 92 VAL H H 7.866 0.020 1 228 72 92 VAL C C 174.276 0.200 1 229 72 92 VAL CA C 62.718 0.200 1 230 72 92 VAL N N 119.374 0.200 1 231 73 93 TYR H H 8.306 0.020 1 232 73 93 TYR CA C 57.741 0.200 1 233 73 93 TYR N N 126.984 0.200 1 234 79 99 GLU C C 179.282 0.200 1 235 79 99 GLU CB C 28.263 0.200 1 236 80 100 VAL H H 6.857 0.020 1 237 80 100 VAL C C 178.135 0.200 1 238 80 100 VAL CA C 65.536 0.200 1 239 80 100 VAL CB C 30.855 0.200 1 240 80 100 VAL N N 119.678 0.200 1 241 81 101 TYR H H 6.890 0.020 1 242 81 101 TYR C C 179.053 0.200 1 243 81 101 TYR CA C 57.796 0.200 1 244 81 101 TYR CB C 36.102 0.200 1 245 81 101 TYR N N 119.697 0.200 1 246 82 102 GLN H H 8.798 0.020 1 247 82 102 GLN C C 180.643 0.200 1 248 82 102 GLN CA C 59.076 0.200 1 249 82 102 GLN CB C 28.371 0.200 1 250 82 102 GLN N N 117.703 0.200 1 251 83 103 GLN H H 7.650 0.020 1 252 83 103 GLN C C 178.800 0.200 1 253 83 103 GLN CA C 58.978 0.200 1 254 83 103 GLN CB C 27.926 0.200 1 255 83 103 GLN N N 120.091 0.200 1 256 84 104 VAL H H 7.729 0.020 1 257 84 104 VAL C C 177.751 0.200 1 258 84 104 VAL CA C 67.018 0.200 1 259 84 104 VAL CB C 31.750 0.200 1 260 84 104 VAL N N 118.682 0.200 1 261 85 105 SER H H 8.606 0.020 1 262 85 105 SER C C 176.921 0.200 1 263 85 105 SER CA C 61.877 0.200 1 264 85 105 SER CB C 63.401 0.200 1 265 85 105 SER N N 111.786 0.200 1 266 86 106 SER H H 8.622 0.020 1 267 86 106 SER C C 176.814 0.200 1 268 86 106 SER CA C 62.491 0.200 1 269 86 106 SER N N 112.824 0.200 1 270 87 107 ARG H H 7.508 0.020 1 271 87 107 ARG C C 180.317 0.200 1 272 87 107 ARG CA C 61.019 0.200 1 273 87 107 ARG CB C 30.521 0.200 1 274 87 107 ARG N N 119.546 0.200 1 275 88 108 ILE H H 8.095 0.020 1 276 88 108 ILE C C 178.011 0.200 1 277 88 108 ILE CA C 66.481 0.200 1 278 88 108 ILE N N 121.529 0.200 1 279 89 109 MET H H 9.320 0.020 1 280 89 109 MET C C 179.078 0.200 1 281 89 109 MET CA C 58.242 0.200 1 282 89 109 MET CB C 30.333 0.200 1 283 89 109 MET N N 118.223 0.200 1 284 90 110 ASN H H 7.794 0.020 1 285 90 110 ASN C C 177.855 0.200 1 286 90 110 ASN CA C 56.184 0.200 1 287 90 110 ASN CB C 37.983 0.200 1 288 90 110 ASN N N 115.757 0.200 1 289 91 111 LEU H H 7.553 0.020 1 290 91 111 LEU C C 178.882 0.200 1 291 91 111 LEU CA C 58.340 0.200 1 292 91 111 LEU CB C 41.220 0.200 1 293 91 111 LEU N N 122.871 0.200 1 294 92 112 LEU H H 7.727 0.020 1 295 92 112 LEU CA C 57.818 0.200 1 296 92 112 LEU N N 117.548 0.200 1 297 93 113 ARG C C 177.268 0.200 1 298 93 113 ARG CB C 30.088 0.200 1 299 94 114 GLU H H 7.396 0.020 1 300 94 114 GLU C C 178.994 0.200 1 301 94 114 GLU CA C 58.326 0.200 1 302 94 114 GLU CB C 29.081 0.200 1 303 94 114 GLU N N 116.225 0.200 1 304 95 115 TYR H H 7.757 0.020 1 305 95 115 TYR C C 176.384 0.200 1 306 95 115 TYR CA C 60.880 0.200 1 307 95 115 TYR CB C 39.465 0.200 1 308 95 115 TYR N N 116.412 0.200 1 309 96 116 SER H H 7.205 0.020 1 310 96 116 SER CA C 58.006 0.200 1 311 96 116 SER N N 108.963 0.200 1 312 97 117 GLU C C 177.367 0.200 1 313 97 117 GLU CB C 29.296 0.200 1 314 98 118 LYS H H 8.191 0.020 1 315 98 118 LYS C C 173.785 0.200 1 316 98 118 LYS CA C 55.399 0.200 1 317 98 118 LYS CB C 31.783 0.200 1 318 98 118 LYS N N 123.233 0.200 1 319 99 119 ILE H H 7.577 0.020 1 320 99 119 ILE C C 173.788 0.200 1 321 99 119 ILE CA C 58.564 0.200 1 322 99 119 ILE N N 121.312 0.200 1 323 100 120 GLU H H 9.267 0.020 1 324 100 120 GLU C C 175.146 0.200 1 325 100 120 GLU CA C 54.761 0.200 1 326 100 120 GLU CB C 32.180 0.200 1 327 100 120 GLU N N 128.802 0.200 1 328 101 121 ILE H H 8.813 0.020 1 329 101 121 ILE C C 174.736 0.200 1 330 101 121 ILE CA C 62.096 0.200 1 331 101 121 ILE N N 128.982 0.200 1 332 102 122 ALA H H 9.760 0.020 1 333 102 122 ALA CA C 52.550 0.200 1 334 102 122 ALA N N 118.763 0.200 1 335 103 123 SER C C 177.562 0.200 1 336 104 124 ILE H H 7.944 0.020 1 337 104 124 ILE C C 173.582 0.200 1 338 104 124 ILE CA C 62.497 0.200 1 339 104 124 ILE CB C 38.833 0.200 1 340 104 124 ILE N N 117.923 0.200 1 341 105 125 ASP H H 7.998 0.020 1 342 105 125 ASP C C 173.316 0.200 1 343 105 125 ASP CA C 50.709 0.200 1 344 105 125 ASP CB C 41.067 0.200 1 345 105 125 ASP N N 116.191 0.200 1 346 106 126 GLU H H 6.340 0.020 1 347 106 126 GLU C C 174.827 0.200 1 348 106 126 GLU CA C 55.027 0.200 1 349 106 126 GLU CB C 30.841 0.200 1 350 106 126 GLU N N 113.998 0.200 1 351 107 127 ALA H H 8.060 0.020 1 352 107 127 ALA C C 174.311 0.200 1 353 107 127 ALA CA C 51.064 0.200 1 354 107 127 ALA CB C 23.188 0.200 1 355 107 127 ALA N N 122.213 0.200 1 356 108 128 TYR H H 8.948 0.020 1 357 108 128 TYR C C 175.135 0.200 1 358 108 128 TYR CA C 57.278 0.200 1 359 108 128 TYR CB C 41.435 0.200 1 360 108 128 TYR N N 116.594 0.200 1 361 109 129 LEU H H 10.001 0.020 1 362 109 129 LEU C C 175.339 0.200 1 363 109 129 LEU CA C 54.940 0.200 1 364 109 129 LEU CB C 45.242 0.200 1 365 109 129 LEU N N 123.803 0.200 1 366 110 130 ASP H H 8.268 0.020 1 367 110 130 ASP C C 178.594 0.200 1 368 110 130 ASP CA C 53.883 0.200 1 369 110 130 ASP N N 122.390 0.200 1 370 111 131 ILE H H 8.235 0.020 1 371 111 131 ILE C C 176.249 0.200 1 372 111 131 ILE CA C 60.779 0.200 1 373 111 131 ILE CB C 40.128 0.200 1 374 111 131 ILE N N 120.197 0.200 1 375 112 132 SER H H 8.841 0.020 1 376 112 132 SER CA C 62.684 0.200 1 377 112 132 SER N N 119.608 0.200 1 378 113 133 ASP C C 176.385 0.200 1 379 113 133 ASP CB C 40.697 0.200 1 380 114 134 LYS H H 7.862 0.020 1 381 114 134 LYS C C 176.240 0.200 1 382 114 134 LYS CA C 55.520 0.200 1 383 114 134 LYS CB C 34.365 0.200 1 384 114 134 LYS N N 116.872 0.200 1 385 115 135 VAL H H 7.263 0.020 1 386 115 135 VAL C C 174.887 0.200 1 387 115 135 VAL CA C 58.293 0.200 1 388 115 135 VAL N N 108.792 0.200 1 389 116 136 ARG H H 8.899 0.020 1 390 116 136 ARG C C 176.240 0.200 1 391 116 136 ARG CA C 56.800 0.200 1 392 116 136 ARG CB C 31.674 0.200 1 393 116 136 ARG N N 118.166 0.200 1 394 117 137 ASP H H 7.247 0.020 1 395 117 137 ASP CA C 52.609 0.200 1 396 117 137 ASP N N 113.359 0.200 1 397 118 138 TYR C C 178.144 0.200 1 398 118 138 TYR CB C 38.433 0.200 1 399 119 139 ARG H H 8.191 0.020 1 400 119 139 ARG C C 179.210 0.200 1 401 119 139 ARG CA C 59.557 0.200 1 402 119 139 ARG CB C 28.898 0.200 1 403 119 139 ARG N N 123.575 0.200 1 404 120 140 GLU H H 8.699 0.020 1 405 120 140 GLU C C 180.507 0.200 1 406 120 140 GLU CA C 59.624 0.200 1 407 120 140 GLU CB C 30.258 0.200 1 408 120 140 GLU N N 120.173 0.200 1 409 121 141 ALA H H 8.110 0.020 1 410 121 141 ALA C C 177.470 0.200 1 411 121 141 ALA CA C 55.631 0.200 1 412 121 141 ALA CB C 19.654 0.200 1 413 121 141 ALA N N 120.597 0.200 1 414 122 142 TYR H H 8.284 0.020 1 415 122 142 TYR C C 176.249 0.200 1 416 122 142 TYR CA C 61.884 0.200 1 417 122 142 TYR CB C 38.154 0.200 1 418 122 142 TYR N N 119.691 0.200 1 419 123 143 ASN H H 7.732 0.020 1 420 123 143 ASN C C 178.258 0.200 1 421 123 143 ASN CA C 56.330 0.200 1 422 123 143 ASN CB C 37.848 0.200 1 423 123 143 ASN N N 116.731 0.200 1 424 124 144 LEU H H 8.049 0.020 1 425 124 144 LEU C C 178.485 0.200 1 426 124 144 LEU CA C 57.921 0.200 1 427 124 144 LEU CB C 42.022 0.200 1 428 124 144 LEU N N 123.438 0.200 1 429 125 145 GLY H H 8.614 0.020 1 430 125 145 GLY C C 174.739 0.200 1 431 125 145 GLY CA C 47.934 0.200 1 432 125 145 GLY N N 106.675 0.200 1 433 126 146 LEU H H 7.970 0.020 1 434 126 146 LEU C C 178.809 0.200 1 435 126 146 LEU CA C 57.870 0.200 1 436 126 146 LEU N N 121.116 0.200 1 437 127 147 GLU H H 7.652 0.020 1 438 127 147 GLU C C 178.879 0.200 1 439 127 147 GLU CA C 60.016 0.200 1 440 127 147 GLU N N 121.284 0.200 1 441 128 148 ILE H H 8.235 0.020 1 442 128 148 ILE C C 177.562 0.200 1 443 128 148 ILE CA C 66.283 0.200 1 444 128 148 ILE N N 120.197 0.200 1 445 129 149 LYS H H 7.933 0.020 1 446 129 149 LYS C C 175.668 0.200 1 447 129 149 LYS CA C 60.048 0.200 1 448 129 149 LYS CB C 31.167 0.200 1 449 129 149 LYS N N 117.923 0.200 1 450 130 150 ASN H H 8.357 0.020 1 451 130 150 ASN C C 177.375 0.200 1 452 130 150 ASN CA C 56.406 0.200 1 453 130 150 ASN CB C 37.992 0.200 1 454 130 150 ASN N N 118.573 0.200 1 455 131 151 LYS H H 8.631 0.020 1 456 131 151 LYS C C 179.782 0.200 1 457 131 151 LYS CA C 58.982 0.200 1 458 131 151 LYS CB C 31.742 0.200 1 459 131 151 LYS N N 122.565 0.200 1 460 132 152 ILE H H 8.234 0.020 1 461 132 152 ILE C C 178.376 0.200 1 462 132 152 ILE CA C 66.397 0.200 1 463 132 152 ILE CB C 41.967 0.200 1 464 132 152 ILE N N 118.702 0.200 1 465 133 153 LEU H H 7.652 0.020 1 466 133 153 LEU C C 179.977 0.200 1 467 133 153 LEU CA C 58.462 0.200 1 468 133 153 LEU N N 121.284 0.200 1 469 134 154 GLU H H 8.284 0.020 1 470 134 154 GLU C C 178.320 0.200 1 471 134 154 GLU CA C 59.558 0.200 1 472 134 154 GLU CB C 29.871 0.200 1 473 134 154 GLU N N 119.429 0.200 1 474 135 155 LYS H H 8.197 0.020 1 475 135 155 LYS C C 178.229 0.200 1 476 135 155 LYS CA C 58.096 0.200 1 477 135 155 LYS CB C 33.346 0.200 1 478 135 155 LYS N N 114.823 0.200 1 479 136 156 GLU H H 8.199 0.020 1 480 136 156 GLU C C 175.690 0.200 1 481 136 156 GLU CA C 54.482 0.200 1 482 136 156 GLU CB C 30.936 0.200 1 483 136 156 GLU N N 113.621 0.200 1 484 137 157 LYS H H 7.660 0.020 1 485 137 157 LYS C C 173.742 0.200 1 486 137 157 LYS CA C 57.790 0.200 1 487 137 157 LYS CB C 28.470 0.200 1 488 137 157 LYS N N 112.554 0.200 1 489 138 158 ILE H H 6.283 0.020 1 490 138 158 ILE C C 175.489 0.200 1 491 138 158 ILE CA C 57.141 0.200 1 492 138 158 ILE CB C 40.627 0.200 1 493 138 158 ILE N N 114.121 0.200 1 494 139 159 THR H H 10.105 0.020 1 495 139 159 THR C C 173.974 0.200 1 496 139 159 THR CA C 61.485 0.200 1 497 139 159 THR N N 118.032 0.200 1 498 140 160 VAL H H 7.430 0.020 1 499 140 160 VAL C C 173.630 0.200 1 500 140 160 VAL CA C 58.153 0.200 1 501 140 160 VAL N N 112.460 0.200 1 502 141 161 THR H H 8.919 0.020 1 503 141 161 THR C C 172.993 0.200 1 504 141 161 THR CA C 62.238 0.200 1 505 141 161 THR CB C 70.457 0.200 1 506 141 161 THR N N 118.246 0.200 1 507 142 162 VAL H H 7.728 0.020 1 508 142 162 VAL C C 174.537 0.200 1 509 142 162 VAL CA C 59.762 0.200 1 510 142 162 VAL N N 125.273 0.200 1 511 143 163 GLY H H 9.402 0.020 1 512 143 163 GLY C C 173.086 0.200 1 513 143 163 GLY CA C 44.115 0.200 1 514 143 163 GLY N N 114.250 0.200 1 515 144 164 ILE H H 8.560 0.020 1 516 144 164 ILE C C 175.709 0.200 1 517 144 164 ILE CA C 59.888 0.200 1 518 144 164 ILE N N 123.634 0.200 1 519 145 165 SER H H 8.688 0.020 1 520 145 165 SER C C 174.781 0.200 1 521 145 165 SER CA C 57.406 0.200 1 522 145 165 SER CB C 63.488 0.200 1 523 145 165 SER N N 117.145 0.200 1 524 146 166 LYS H H 8.812 0.020 1 525 146 166 LYS C C 174.729 0.200 1 526 146 166 LYS CA C 56.014 0.200 1 527 146 166 LYS CB C 32.187 0.200 1 528 146 166 LYS N N 116.190 0.200 1 529 147 167 ASN H H 7.567 0.020 1 530 147 167 ASN CA C 52.064 0.200 1 531 147 167 ASN N N 110.535 0.200 1 532 148 168 LYS C C 177.439 0.200 1 533 148 168 LYS CB C 32.370 0.200 1 534 149 169 VAL H H 7.171 0.020 1 535 149 169 VAL C C 177.742 0.200 1 536 149 169 VAL CA C 66.387 0.200 1 537 149 169 VAL N N 118.508 0.200 1 538 150 170 PHE H H 8.097 0.020 1 539 150 170 PHE C C 177.535 0.200 1 540 150 170 PHE CA C 61.450 0.200 1 541 150 170 PHE CB C 39.475 0.200 1 542 150 170 PHE N N 115.169 0.200 1 543 151 171 ALA H H 7.924 0.020 1 544 151 171 ALA C C 177.923 0.200 1 545 151 171 ALA CA C 55.798 0.200 1 546 151 171 ALA CB C 18.245 0.200 1 547 151 171 ALA N N 122.989 0.200 1 548 152 172 LYS H H 7.312 0.020 1 549 152 172 LYS C C 178.145 0.200 1 550 152 172 LYS CA C 59.143 0.200 1 551 152 172 LYS CB C 29.561 0.200 1 552 152 172 LYS N N 119.107 0.200 1 553 153 173 ILE H H 7.791 0.020 1 554 153 173 ILE C C 177.579 0.200 1 555 153 173 ILE CA C 65.607 0.200 1 556 153 173 ILE N N 119.479 0.200 1 557 154 174 ALA H H 8.057 0.020 1 558 154 174 ALA C C 178.435 0.200 1 559 154 174 ALA CA C 55.695 0.200 1 560 154 174 ALA CB C 17.392 0.200 1 561 154 174 ALA N N 120.188 0.200 1 562 155 175 ALA H H 7.484 0.020 1 563 155 175 ALA C C 179.698 0.200 1 564 155 175 ALA CA C 54.817 0.200 1 565 155 175 ALA CB C 18.518 0.200 1 566 155 175 ALA N N 118.230 0.200 1 567 156 176 ASP H H 8.558 0.020 1 568 156 176 ASP C C 179.350 0.200 1 569 156 176 ASP CA C 57.825 0.200 1 570 156 176 ASP CB C 40.175 0.200 1 571 156 176 ASP N N 119.153 0.200 1 572 157 177 MET H H 7.921 0.020 1 573 157 177 MET C C 176.798 0.200 1 574 157 177 MET CA C 57.983 0.200 1 575 157 177 MET CB C 33.560 0.200 1 576 157 177 MET N N 116.006 0.200 1 577 158 178 ALA H H 7.594 0.020 1 578 158 178 ALA C C 176.112 0.200 1 579 158 178 ALA CA C 51.717 0.200 1 580 158 178 ALA CB C 21.114 0.200 1 581 158 178 ALA N N 121.549 0.200 1 582 159 179 LYS H H 7.278 0.020 1 583 159 179 LYS CA C 54.851 0.200 1 584 159 179 LYS N N 118.152 0.200 1 585 161 181 ASN C C 176.533 0.200 1 586 161 181 ASN CB C 36.866 0.200 1 587 162 182 GLY H H 7.840 0.020 1 588 162 182 GLY C C 174.025 0.200 1 589 162 182 GLY CA C 44.320 0.200 1 590 162 182 GLY N N 105.527 0.200 1 591 163 183 ILE H H 8.240 0.020 1 592 163 183 ILE C C 172.854 0.200 1 593 163 183 ILE CA C 59.958 0.200 1 594 163 183 ILE CB C 39.760 0.200 1 595 163 183 ILE N N 117.370 0.200 1 596 164 184 LYS H H 8.186 0.020 1 597 164 184 LYS C C 173.143 0.200 1 598 164 184 LYS CA C 55.456 0.200 1 599 164 184 LYS CB C 36.541 0.200 1 600 164 184 LYS N N 127.270 0.200 1 601 165 185 VAL H H 8.611 0.020 1 602 165 185 VAL C C 175.972 0.200 1 603 165 185 VAL CA C 60.046 0.200 1 604 165 185 VAL CB C 27.551 0.200 1 605 165 185 VAL N N 126.362 0.200 1 606 166 186 ILE H H 8.595 0.020 1 607 166 186 ILE C C 174.618 0.200 1 608 166 186 ILE CA C 61.107 0.200 1 609 166 186 ILE N N 127.415 0.200 1 610 167 187 ASP H H 8.375 0.020 1 611 167 187 ASP C C 175.038 0.200 1 612 167 187 ASP CA C 52.500 0.200 1 613 167 187 ASP CB C 37.898 0.200 1 614 167 187 ASP N N 127.979 0.200 1 615 168 188 ASP H H 6.776 0.020 1 616 168 188 ASP C C 178.823 0.200 1 617 168 188 ASP CA C 51.440 0.200 1 618 168 188 ASP CB C 40.611 0.200 1 619 168 188 ASP N N 119.743 0.200 1 620 169 189 GLU H H 7.829 0.020 1 621 169 189 GLU C C 178.982 0.200 1 622 169 189 GLU CA C 58.970 0.200 1 623 169 189 GLU CB C 29.161 0.200 1 624 169 189 GLU N N 118.818 0.200 1 625 170 190 GLU H H 8.179 0.020 1 626 170 190 GLU C C 178.822 0.200 1 627 170 190 GLU CA C 59.012 0.200 1 628 170 190 GLU CB C 28.863 0.200 1 629 170 190 GLU N N 123.256 0.200 1 630 171 191 VAL H H 8.254 0.020 1 631 171 191 VAL C C 176.508 0.200 1 632 171 191 VAL CA C 67.256 0.200 1 633 171 191 VAL N N 120.758 0.200 1 634 172 192 LYS H H 6.812 0.020 1 635 172 192 LYS C C 179.110 0.200 1 636 172 192 LYS CA C 59.606 0.200 1 637 172 192 LYS CB C 32.126 0.200 1 638 172 192 LYS N N 114.543 0.200 1 639 173 193 ARG H H 7.174 0.020 1 640 173 193 ARG C C 178.674 0.200 1 641 173 193 ARG CA C 59.352 0.200 1 642 173 193 ARG CB C 30.101 0.200 1 643 173 193 ARG N N 117.577 0.200 1 644 174 194 LEU H H 8.571 0.020 1 645 174 194 LEU C C 179.502 0.200 1 646 174 194 LEU CA C 57.989 0.200 1 647 174 194 LEU CB C 42.113 0.200 1 648 174 194 LEU N N 120.659 0.200 1 649 175 195 ILE H H 8.255 0.020 1 650 175 195 ILE C C 176.120 0.200 1 651 175 195 ILE CA C 66.267 0.200 1 652 175 195 ILE CB C 38.575 0.200 1 653 175 195 ILE N N 117.988 0.200 1 654 176 196 ARG H H 6.897 0.020 1 655 176 196 ARG C C 176.590 0.200 1 656 176 196 ARG CA C 58.000 0.200 1 657 176 196 ARG CB C 30.714 0.200 1 658 176 196 ARG N N 113.626 0.200 1 659 177 197 GLU H H 7.648 0.020 1 660 177 197 GLU C C 177.457 0.200 1 661 177 197 GLU CA C 56.936 0.200 1 662 177 197 GLU CB C 32.179 0.200 1 663 177 197 GLU N N 114.995 0.200 1 664 178 198 LEU H H 8.382 0.020 1 665 178 198 LEU C C 176.296 0.200 1 666 178 198 LEU CA C 55.992 0.200 1 667 178 198 LEU CB C 43.582 0.200 1 668 178 198 LEU N N 124.077 0.200 1 669 179 199 ASP H H 8.928 0.020 1 670 179 199 ASP C C 178.113 0.200 1 671 179 199 ASP CA C 54.788 0.200 1 672 179 199 ASP CB C 41.860 0.200 1 673 179 199 ASP N N 127.919 0.200 1 674 180 200 ILE H H 8.135 0.020 1 675 180 200 ILE C C 175.668 0.200 1 676 180 200 ILE CA C 62.453 0.200 1 677 180 200 ILE CB C 38.020 0.200 1 678 180 200 ILE N N 124.936 0.200 1 679 181 201 ALA H H 8.384 0.020 1 680 181 201 ALA C C 178.071 0.200 1 681 181 201 ALA CA C 53.565 0.200 1 682 181 201 ALA CB C 18.408 0.200 1 683 181 201 ALA N N 118.551 0.200 1 684 182 202 ASP H H 7.739 0.020 1 685 182 202 ASP C C 175.818 0.200 1 686 182 202 ASP CA C 54.285 0.200 1 687 182 202 ASP CB C 41.653 0.200 1 688 182 202 ASP N N 116.125 0.200 1 689 183 203 VAL H H 7.285 0.020 1 690 183 203 VAL CA C 61.065 0.200 1 691 183 203 VAL N N 122.319 0.200 1 692 187 207 GLY C C 173.888 0.200 1 693 188 208 ASN H H 8.055 0.020 1 694 188 208 ASN C C 179.782 0.200 1 695 188 208 ASN CA C 53.544 0.200 1 696 188 208 ASN N N 120.551 0.200 1 697 189 209 ILE H H 8.252 0.020 1 698 189 209 ILE CA C 66.311 0.200 1 699 189 209 ILE N N 118.283 0.200 1 700 190 210 THR C C 175.717 0.200 1 701 190 210 THR CB C 68.094 0.200 1 702 191 211 ALA H H 8.206 0.020 1 703 191 211 ALA C C 179.247 0.200 1 704 191 211 ALA CA C 55.869 0.200 1 705 191 211 ALA CB C 17.588 0.200 1 706 191 211 ALA N N 121.989 0.200 1 707 192 212 GLU H H 8.012 0.020 1 708 192 212 GLU C C 179.159 0.200 1 709 192 212 GLU CA C 59.698 0.200 1 710 192 212 GLU CB C 29.210 0.200 1 711 192 212 GLU N N 117.495 0.200 1 712 193 213 LYS H H 7.640 0.020 1 713 193 213 LYS C C 178.882 0.200 1 714 193 213 LYS CA C 59.834 0.200 1 715 193 213 LYS CB C 32.339 0.200 1 716 193 213 LYS N N 119.144 0.200 1 717 194 214 LEU H H 7.735 0.020 1 718 194 214 LEU C C 179.301 0.200 1 719 194 214 LEU CA C 57.814 0.200 1 720 194 214 LEU CB C 40.403 0.200 1 721 194 214 LEU N N 117.192 0.200 1 722 195 215 LYS H H 8.289 0.020 1 723 195 215 LYS C C 181.282 0.200 1 724 195 215 LYS CA C 59.963 0.200 1 725 195 215 LYS CB C 31.975 0.200 1 726 195 215 LYS N N 121.473 0.200 1 727 196 216 LYS H H 7.640 0.020 1 728 196 216 LYS C C 177.919 0.200 1 729 196 216 LYS CA C 58.978 0.200 1 730 196 216 LYS CB C 31.885 0.200 1 731 196 216 LYS N N 119.908 0.200 1 732 197 217 LEU H H 7.287 0.020 1 733 197 217 LEU C C 176.602 0.200 1 734 197 217 LEU CA C 54.459 0.200 1 735 197 217 LEU CB C 42.587 0.200 1 736 197 217 LEU N N 117.778 0.200 1 737 198 218 GLY H H 7.737 0.020 1 738 198 218 GLY C C 173.583 0.200 1 739 198 218 GLY CA C 45.113 0.200 1 740 198 218 GLY N N 106.126 0.200 1 741 199 219 ILE H H 7.662 0.020 1 742 199 219 ILE C C 172.379 0.200 1 743 199 219 ILE CA C 60.016 0.200 1 744 199 219 ILE N N 121.874 0.200 1 745 200 220 ASN H H 8.521 0.020 1 746 200 220 ASN C C 175.172 0.200 1 747 200 220 ASN CA C 54.711 0.200 1 748 200 220 ASN CB C 42.327 0.200 1 749 200 220 ASN N N 122.618 0.200 1 750 201 221 LYS H H 8.551 0.020 1 751 201 221 LYS C C 178.457 0.200 1 752 201 221 LYS CA C 52.913 0.200 1 753 201 221 LYS CB C 35.402 0.200 1 754 201 221 LYS N N 119.914 0.200 1 755 202 222 LEU H H 8.936 0.020 1 756 202 222 LEU C C 179.375 0.200 1 757 202 222 LEU CA C 59.306 0.200 1 758 202 222 LEU N N 122.602 0.200 1 759 203 223 VAL H H 7.878 0.020 1 760 203 223 VAL C C 176.192 0.200 1 761 203 223 VAL CA C 64.410 0.200 1 762 203 223 VAL CB C 31.215 0.200 1 763 203 223 VAL N N 115.227 0.200 1 764 204 224 ASP H H 7.712 0.020 1 765 204 224 ASP C C 178.856 0.200 1 766 204 224 ASP CA C 57.017 0.200 1 767 204 224 ASP CB C 41.742 0.200 1 768 204 224 ASP N N 122.437 0.200 1 769 205 225 THR H H 7.826 0.020 1 770 205 225 THR C C 174.465 0.200 1 771 205 225 THR CA C 65.449 0.200 1 772 205 225 THR CB C 69.093 0.200 1 773 205 225 THR N N 110.629 0.200 1 774 206 226 LEU H H 7.143 0.020 1 775 206 226 LEU C C 178.129 0.200 1 776 206 226 LEU CA C 55.511 0.200 1 777 206 226 LEU CB C 41.157 0.200 1 778 206 226 LEU N N 115.741 0.200 1 779 207 227 SER H H 7.574 0.020 1 780 207 227 SER C C 172.914 0.200 1 781 207 227 SER CA C 58.798 0.200 1 782 207 227 SER CB C 64.539 0.200 1 783 207 227 SER N N 112.634 0.200 1 784 208 228 ILE H H 6.936 0.020 1 785 208 228 ILE C C 174.140 0.200 1 786 208 228 ILE CA C 58.409 0.200 1 787 208 228 ILE CB C 40.243 0.200 1 788 208 228 ILE N N 119.131 0.200 1 789 209 229 GLU H H 8.682 0.020 1 790 209 229 GLU CA C 57.714 0.200 1 791 209 229 GLU N N 126.137 0.200 1 792 210 230 PHE C C 177.093 0.200 1 793 210 230 PHE CB C 39.160 0.200 1 794 211 231 ASP H H 8.928 0.020 1 795 211 231 ASP C C 179.217 0.200 1 796 211 231 ASP CA C 57.777 0.200 1 797 211 231 ASP CB C 40.446 0.200 1 798 211 231 ASP N N 115.951 0.200 1 799 212 232 LYS H H 7.169 0.020 1 800 212 232 LYS C C 178.736 0.200 1 801 212 232 LYS CA C 58.578 0.200 1 802 212 232 LYS CB C 32.089 0.200 1 803 212 232 LYS N N 119.219 0.200 1 804 213 233 LEU H H 7.455 0.020 1 805 213 233 LEU C C 178.662 0.200 1 806 213 233 LEU CA C 58.117 0.200 1 807 213 233 LEU CB C 42.171 0.200 1 808 213 233 LEU N N 120.899 0.200 1 809 214 234 LYS H H 8.509 0.020 1 810 214 234 LYS C C 178.863 0.200 1 811 214 234 LYS CA C 58.885 0.200 1 812 214 234 LYS CB C 31.232 0.200 1 813 214 234 LYS N N 118.173 0.200 1 814 215 235 GLY H H 7.574 0.020 1 815 215 235 GLY C C 174.300 0.200 1 816 215 235 GLY CA C 46.416 0.200 1 817 215 235 GLY N N 106.531 0.200 1 818 216 236 MET H H 7.334 0.020 1 819 216 236 MET C C 177.632 0.200 1 820 216 236 MET CA C 57.429 0.200 1 821 216 236 MET CB C 34.425 0.200 1 822 216 236 MET N N 117.308 0.200 1 823 217 237 ILE H H 7.574 0.020 1 824 217 237 ILE C C 175.994 0.200 1 825 217 237 ILE CA C 60.581 0.200 1 826 217 237 ILE CB C 40.079 0.200 1 827 217 237 ILE N N 106.531 0.200 1 828 218 238 GLY H H 7.827 0.020 1 829 218 238 GLY CA C 44.646 0.200 1 830 218 238 GLY N N 113.095 0.200 1 831 219 239 GLU C C 177.533 0.200 1 832 219 239 GLU CB C 28.211 0.200 1 833 220 240 ALA H H 7.389 0.020 1 834 220 240 ALA C C 179.866 0.200 1 835 220 240 ALA CA C 54.250 0.200 1 836 220 240 ALA N N 117.301 0.200 1 837 221 241 LYS H H 8.339 0.020 1 838 221 241 LYS C C 178.129 0.200 1 839 221 241 LYS CA C 58.704 0.200 1 840 221 241 LYS CB C 31.591 0.200 1 841 221 241 LYS N N 119.158 0.200 1 842 222 242 ALA H H 7.893 0.020 1 843 222 242 ALA C C 178.488 0.200 1 844 222 242 ALA CA C 56.239 0.200 1 845 222 242 ALA CB C 18.326 0.200 1 846 222 242 ALA N N 120.564 0.200 1 847 223 243 LYS H H 8.592 0.020 1 848 223 243 LYS C C 179.199 0.200 1 849 223 243 LYS CA C 60.176 0.200 1 850 223 243 LYS CB C 32.221 0.200 1 851 223 243 LYS N N 116.235 0.200 1 852 224 244 TYR H H 7.756 0.020 1 853 224 244 TYR C C 176.498 0.200 1 854 224 244 TYR CA C 60.163 0.200 1 855 224 244 TYR CB C 38.307 0.200 1 856 224 244 TYR N N 120.895 0.200 1 857 225 245 LEU H H 8.012 0.020 1 858 225 245 LEU C C 178.354 0.200 1 859 225 245 LEU CA C 58.118 0.200 1 860 225 245 LEU CB C 42.408 0.200 1 861 225 245 LEU N N 117.495 0.200 1 862 226 246 ILE H H 8.104 0.020 1 863 226 246 ILE C C 177.834 0.200 1 864 226 246 ILE CA C 64.137 0.200 1 865 226 246 ILE CB C 37.479 0.200 1 866 226 246 ILE N N 116.279 0.200 1 867 227 247 SER H H 7.981 0.020 1 868 227 247 SER C C 176.403 0.200 1 869 227 247 SER CA C 62.339 0.200 1 870 227 247 SER N N 115.585 0.200 1 871 228 248 LEU H H 7.557 0.020 1 872 228 248 LEU C C 179.090 0.200 1 873 228 248 LEU CA C 57.674 0.200 1 874 228 248 LEU CB C 43.450 0.200 1 875 228 248 LEU N N 122.423 0.200 1 876 229 249 ALA H H 8.158 0.020 1 877 229 249 ALA C C 177.577 0.200 1 878 229 249 ALA CA C 54.377 0.200 1 879 229 249 ALA CB C 18.549 0.200 1 880 229 249 ALA N N 119.739 0.200 1 881 230 250 ARG H H 7.827 0.020 1 882 230 250 ARG CA C 56.496 0.200 1 883 230 250 ARG N N 113.095 0.200 1 stop_ save_