data_6628 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Specificity and Mechanism of the Histone Methyltransferase Pr-Set7 ; _BMRB_accession_number 6628 _BMRB_flat_file_name bmr6628.str _Entry_type original _Submission_date 2005-05-12 _Accession_date 2005-09-30 _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 Xiao Bing . . 2 Jing Chun . . 3 Kelly Geoff . . 4 Walker Philip . . 5 Muskett Frederick . . 6 Frenkiel Thomas . . 7 Martin Steve . . 8 Sarma Kavitha . . 9 Reinberg Danny . . 10 Gamblin Steven . . 11 Wilson Jonathan . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 179 "13C chemical shifts" 418 "15N chemical shifts" 179 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2005-11-22 original author . stop_ _Original_release_date 2005-11-22 save_ ############################# # Citation for this entry # ############################# save_citation_1 _Saveframe_category entry_citation _Citation_full . _Citation_title 'Specificity and mechanism of the histone methyltransferase Pr-Set7' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 15933069 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Xiao Bing . . 2 Jing Chun . . 3 Kelly Geoff . . 4 Walker Philip A. . 5 Muskett Frederick W. . 6 Frenkiel Thomas A. . 7 Martin Steve R. . 8 Sarma Kavitha . . 9 Reinberg Danny . . 10 Gamblin Steven J. . 11 Wilson Jonathan R. . stop_ _Journal_abbreviation 'Genes Dev.' _Journal_volume 19 _Journal_issue 12 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 1444 _Page_last 1454 _Year 2005 _Details . loop_ _Keyword nmr Pr-Set7 stop_ save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name Set7/9 _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label Set7/9 $Set7-9_polypeptide stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state protein _System_paramagnetic no _System_thiol_state 'all free' _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_Set7-9_polypeptide _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common set7/9 _Molecular_mass . _Mol_thiol_state 'all free' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 264 _Mol_residue_sequence ; GPLGSGQYKDNIRHGVCWIY YPDGGSLVGEVNEDGEMTGE KIAYVYPDERTALYGKFIDG EMIEGKLATLMSTEEGRPHF ELMPGNSVYHFDKSTSSCIS TNALLPDPYESERVYVAESL ISSAGEGLFSKVAVGPNTVM SFYNGVRITHQEVDSRDWAL NGNTLSLDEETVIDVPEPYN HVSKYCASLGHKANHSFTPN CIYDMFVHPRFGPIKCIRTL RAVEADEELTVAYGYDHSPP GKSGPEAPEWYQVELKAFQA TQQK ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 103 GLY 2 104 PRO 3 105 LEU 4 106 GLY 5 107 SER 6 108 GLY 7 109 GLN 8 110 TYR 9 111 LYS 10 112 ASP 11 113 ASN 12 114 ILE 13 115 ARG 14 116 HIS 15 117 GLY 16 118 VAL 17 119 CYS 18 120 TRP 19 121 ILE 20 122 TYR 21 123 TYR 22 124 PRO 23 125 ASP 24 126 GLY 25 127 GLY 26 128 SER 27 129 LEU 28 130 VAL 29 131 GLY 30 132 GLU 31 133 VAL 32 134 ASN 33 135 GLU 34 136 ASP 35 137 GLY 36 138 GLU 37 139 MET 38 140 THR 39 141 GLY 40 142 GLU 41 143 LYS 42 144 ILE 43 145 ALA 44 146 TYR 45 147 VAL 46 148 TYR 47 149 PRO 48 150 ASP 49 151 GLU 50 152 ARG 51 153 THR 52 154 ALA 53 155 LEU 54 156 TYR 55 157 GLY 56 158 LYS 57 159 PHE 58 160 ILE 59 161 ASP 60 162 GLY 61 163 GLU 62 164 MET 63 165 ILE 64 166 GLU 65 167 GLY 66 168 LYS 67 169 LEU 68 170 ALA 69 171 THR 70 172 LEU 71 173 MET 72 174 SER 73 175 THR 74 176 GLU 75 177 GLU 76 178 GLY 77 179 ARG 78 180 PRO 79 181 HIS 80 182 PHE 81 183 GLU 82 184 LEU 83 185 MET 84 186 PRO 85 187 GLY 86 188 ASN 87 189 SER 88 190 VAL 89 191 TYR 90 192 HIS 91 193 PHE 92 194 ASP 93 195 LYS 94 196 SER 95 197 THR 96 198 SER 97 199 SER 98 200 CYS 99 201 ILE 100 202 SER 101 203 THR 102 204 ASN 103 205 ALA 104 206 LEU 105 207 LEU 106 208 PRO 107 209 ASP 108 210 PRO 109 211 TYR 110 212 GLU 111 213 SER 112 214 GLU 113 215 ARG 114 216 VAL 115 217 TYR 116 218 VAL 117 219 ALA 118 220 GLU 119 221 SER 120 222 LEU 121 223 ILE 122 224 SER 123 225 SER 124 226 ALA 125 227 GLY 126 228 GLU 127 229 GLY 128 230 LEU 129 231 PHE 130 232 SER 131 233 LYS 132 234 VAL 133 235 ALA 134 236 VAL 135 237 GLY 136 238 PRO 137 239 ASN 138 240 THR 139 241 VAL 140 242 MET 141 243 SER 142 244 PHE 143 245 TYR 144 246 ASN 145 247 GLY 146 248 VAL 147 249 ARG 148 250 ILE 149 251 THR 150 252 HIS 151 253 GLN 152 254 GLU 153 255 VAL 154 256 ASP 155 257 SER 156 258 ARG 157 259 ASP 158 260 TRP 159 261 ALA 160 262 LEU 161 263 ASN 162 264 GLY 163 265 ASN 164 266 THR 165 267 LEU 166 268 SER 167 269 LEU 168 270 ASP 169 271 GLU 170 272 GLU 171 273 THR 172 274 VAL 173 275 ILE 174 276 ASP 175 277 VAL 176 278 PRO 177 279 GLU 178 280 PRO 179 281 TYR 180 282 ASN 181 283 HIS 182 284 VAL 183 285 SER 184 286 LYS 185 287 TYR 186 288 CYS 187 289 ALA 188 290 SER 189 291 LEU 190 292 GLY 191 293 HIS 192 294 LYS 193 295 ALA 194 296 ASN 195 297 HIS 196 298 SER 197 299 PHE 198 300 THR 199 301 PRO 200 302 ASN 201 303 CYS 202 304 ILE 203 305 TYR 204 306 ASP 205 307 MET 206 308 PHE 207 309 VAL 208 310 HIS 209 311 PRO 210 312 ARG 211 313 PHE 212 314 GLY 213 315 PRO 214 316 ILE 215 317 LYS 216 318 CYS 217 319 ILE 218 320 ARG 219 321 THR 220 322 LEU 221 323 ARG 222 324 ALA 223 325 VAL 224 326 GLU 225 327 ALA 226 328 ASP 227 329 GLU 228 330 GLU 229 331 LEU 230 332 THR 231 333 VAL 232 334 ALA 233 335 TYR 234 336 GLY 235 337 TYR 236 338 ASP 237 339 HIS 238 340 SER 239 341 PRO 240 342 PRO 241 343 GLY 242 344 LYS 243 345 SER 244 346 GLY 245 347 PRO 246 348 GLU 247 349 ALA 248 350 PRO 249 351 GLU 250 352 TRP 251 353 TYR 252 354 GLN 253 355 VAL 254 356 GLU 255 357 LEU 256 358 LYS 257 359 ALA 258 360 PHE 259 361 GLN 260 362 ALA 261 363 THR 262 364 GLN 263 365 GLN 264 366 LYS stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-01-28 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 1H3I "Crystal Structure Of The Histone Methyltransferase Set79" 89.77 293 100.00 100.00 2.46e-174 PDB 1MT6 "Structure Of Histone H3 K4-Specific Methyltransferase Set79 WITH ADOHCY" 87.12 280 100.00 100.00 1.07e-168 PDB 1MUF "Structure Of Histone H3 K4-Specific Methyltransferase Set79" 87.12 257 97.39 97.39 1.90e-162 PDB 1N6A "Structure Of Set7/9" 98.11 259 97.68 97.68 0.00e+00 PDB 1N6C "Structure Of Set7/9" 98.11 297 100.00 100.00 0.00e+00 PDB 1O9S "Crystal Structure Of A Ternary Complex Of The Human Histone Methyltransferase Set79" 98.11 259 100.00 100.00 0.00e+00 PDB 1XQH "Crystal Structure Of A Ternary Complex Of The Methyltransferase Set9 (Also Known As Set79) WITH A P53 Peptide And Sah" 100.00 264 100.00 100.00 0.00e+00 PDB 2F69 "Ternary Complex Of Set79 BOUND TO ADOHCY AND A TAF10 Peptide" 98.86 261 98.85 99.23 0.00e+00 PDB 3CBM "Set79-Er-Adomet Complex" 96.97 256 100.00 100.00 0.00e+00 PDB 3CBO "Set7/9-er-adohcy Complex" 96.97 256 100.00 100.00 0.00e+00 PDB 3CBP "Set7/9-er-sinefungin Complex" 96.97 256 100.00 100.00 0.00e+00 PDB 3M53 "Set79 IN COMPLEX WITH TAF10 PEPTIDE AND ADOHCY" 98.86 261 98.85 99.23 0.00e+00 PDB 3M54 "Set79 Y305F IN COMPLEX WITH TAF10 PEPTIDE AND ADOHCY" 98.86 261 98.47 99.23 0.00e+00 PDB 3M55 "Set79 Y305F IN COMPLEX WITH TAF10-K189me1 Peptide And Adohcy" 98.86 261 98.47 99.23 0.00e+00 PDB 3M56 "Set79 Y305F IN COMPLEX WITH TAF10-K189me2 Peptide And Adohcy" 98.86 261 98.47 99.23 0.00e+00 PDB 3M57 "Set79 Y245A IN COMPLEX WITH TAF10 PEPTIDE AND ADOHCY" 98.86 261 98.47 98.85 0.00e+00 PDB 3M58 "Set79 Y245A IN COMPLEX WITH TAF10-K189me1 Peptide And Adohcy" 98.86 261 98.47 98.85 0.00e+00 PDB 3M59 "Set79 Y245A IN COMPLEX WITH TAF10-K189me2 Peptide And Adohcy" 98.86 261 98.47 98.85 0.00e+00 PDB 3M5A "Set79 Y245A IN COMPLEX WITH TAF10-K189me3 Peptide And Adohcy" 98.86 261 98.47 98.85 0.00e+00 PDB 3OS5 "Set79-Dnmt1 K142me1 Complex" 96.97 256 100.00 100.00 0.00e+00 PDB 3VUZ "Crystal Structure Of Histone Methyltransferase Set7/9 In Comlex With Aam-1" 96.97 263 100.00 100.00 0.00e+00 PDB 3VV0 "Crystal Structure Of Histone Methyltransferase Set7/9 In Comlex With Daam-3" 96.97 263 100.00 100.00 0.00e+00 PDB 4E47 "Set79 IN COMPLEX WITH INHIBITOR (R)-(3-(3-Cyanophenyl)-1-Oxo-1- (Pyrrolidin-1-Yl)propan-2-Yl)-1,2,3,4-Tetrahydroisoquinoline-6-" 97.73 264 100.00 100.00 0.00e+00 PDB 4J7F "Set7/9y335paf In Complex With Taf10 Peptide And Adohcy" 98.86 261 98.47 98.85 0.00e+00 PDB 4J7I "Set7/9y335f In Complex With Taf10 Peptide And Adohcy" 98.86 261 98.47 99.23 0.00e+00 PDB 4J83 "Set7/9 In Complex With Taf10k189a Peptide And Adomet" 98.86 261 98.85 99.23 0.00e+00 PDB 4J8O "Set7/9 In Complex With Taf10k189a Peptide And Adohcy" 98.86 261 98.85 99.23 0.00e+00 PDB 4JDS "Setd7 In Complex With Inhibitor Pf-5426 And S-adenosyl-methionine" 97.73 264 100.00 100.00 0.00e+00 PDB 4JLG "Setd7 In Complex With Inhibitor (r)-pfi-2 And S-adenosyl-methionine" 97.73 264 100.00 100.00 0.00e+00 DBJ BAB21808 "KIAA1717 protein [Homo sapiens]" 98.11 420 100.00 100.00 0.00e+00 DBJ BAG11355 "SET domain-containing protein 7 [synthetic construct]" 98.11 366 100.00 100.00 0.00e+00 GB AAI21056 "SET domain containing (lysine methyltransferase) 7 [Homo sapiens]" 98.11 366 100.00 100.00 0.00e+00 GB AAI21057 "SET domain containing (lysine methyltransferase) 7 [Homo sapiens]" 98.11 366 100.00 100.00 0.00e+00 GB AAL56579 "histone H3-K4 methyltransferase [Homo sapiens]" 98.11 366 100.00 100.00 0.00e+00 GB AAL69901 "histone H3 lysine 4 specific methyltransferase [Homo sapiens]" 98.11 366 100.00 100.00 0.00e+00 GB AAY40937 "unknown [Homo sapiens]" 98.11 309 100.00 100.00 0.00e+00 REF NP_001244432 "histone-lysine N-methyltransferase SETD7 [Macaca mulatta]" 98.11 366 100.00 100.00 0.00e+00 REF NP_085151 "histone-lysine N-methyltransferase SETD7 [Homo sapiens]" 98.11 366 100.00 100.00 0.00e+00 REF XP_002745388 "PREDICTED: histone-lysine N-methyltransferase SETD7 [Callithrix jacchus]" 98.11 366 98.84 99.61 0.00e+00 REF XP_002815202 "PREDICTED: histone-lysine N-methyltransferase SETD7 [Pongo abelii]" 98.11 366 99.23 99.61 0.00e+00 REF XP_002916185 "PREDICTED: LOW QUALITY PROTEIN: histone-lysine N-methyltransferase SETD7-like [Ailuropoda melanoleuca]" 98.11 457 97.68 100.00 0.00e+00 SP Q8WTS6 "RecName: Full=Histone-lysine N-methyltransferase SETD7; AltName: Full=Histone H3-K4 methyltransferase SETD7; Short=H3-K4-HMTase" 98.11 366 100.00 100.00 0.00e+00 TPG DAA20878 "TPA: KIAA1717 protein-like [Bos taurus]" 98.11 456 97.68 99.61 0.00e+00 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $Set7-9_polypeptide Human 9606 Eukaryota Metazoa Homo sapiens stop_ save_ ######################### # Experimental source # ######################### save_experimental_source _Saveframe_category experimental_source loop_ _Mol_label _Production_method _Host_organism_name_common _Genus _Species _Strain _Vector_name $Set7-9_polypeptide 'recombinant technology' 'E. Coli' . . . . 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 $Set7-9_polypeptide 0.5 mM '[U-98% 13C; U-99% 15N; U-98% 2H]' Tris 20 mM . TCEP 0.5 mM . stop_ save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_800MHz_spectrometer _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model Inova _Field_strength 800 _Details . save_ ############################# # NMR applied experiments # ############################# save_1H{15N}-TROSY_1 _Saveframe_category NMR_applied_experiment _Experiment_name 1H{15N}-TROSY _Sample_label $sample_1 save_ save_TROSY-HNCA_2 _Saveframe_category NMR_applied_experiment _Experiment_name TROSY-HNCA _Sample_label . save_ save_TROSY-HN(CO)CA_3 _Saveframe_category NMR_applied_experiment _Experiment_name TROSY-HN(CO)CA _Sample_label . save_ save_TROSY-HN(CA)CO_4 _Saveframe_category NMR_applied_experiment _Experiment_name TROSY-HN(CA)CO _Sample_label . save_ save_TROSY-HNCO_5 _Saveframe_category NMR_applied_experiment _Experiment_name TROSY-HNCO _Sample_label . save_ save_TROSY-HN(CA)CB_6 _Saveframe_category NMR_applied_experiment _Experiment_name TROSY-HN(CA)CB _Sample_label . save_ save_TROSY-HN(COCA)CB_7 _Saveframe_category NMR_applied_experiment _Experiment_name TROSY-HN(COCA)CB _Sample_label . save_ save_1H{15N}-TROSY _Saveframe_category NMR_applied_experiment _Experiment_name 1H{15N}-TROSY _BMRB_pulse_sequence_accession_number . _Details . save_ ####################### # Sample conditions # ####################### save_conditions_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units 'ionic strength' 0.1 0.02 M pH 7.0 0.02 pH stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_referencing _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 0.0 . indirect . . . 0.251449530 DSS H 1 'methyl protons' ppm 0.0 internal direct . . . 1.0 DSS N 15 'methyl protons' ppm 0.0 . 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_chem_shift_list_1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $conditions_1 _Chem_shift_reference_set_label $chemical_shift_referencing _Mol_system_component_name Set7/9 _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 1 104 2 PRO CA C 62.49 0.2 1 2 104 2 PRO CB C 32.64 0.2 1 3 105 3 LEU H H 9.11 0.2 1 4 105 3 LEU CA C 52.13 0.2 1 5 105 3 LEU CB C 43.20 0.2 1 6 105 3 LEU N N 124.69 0.2 1 7 108 6 GLY CA C 45.15 0.2 1 8 109 7 GLN H H 8.203 0.01 1 9 109 7 GLN CA C 55.58 0.2 1 10 109 7 GLN CB C 29.06 0.2 1 11 109 7 GLN N N 119.130 0.2 1 12 110 8 TYR CA C 56.62 0.2 1 13 110 8 TYR CB C 39.55 0.2 1 14 111 9 LYS H H 8.704 0.01 1 15 111 9 LYS CA C 60.66 0.2 1 16 111 9 LYS CB C 31.34 0.2 1 17 111 9 LYS N N 129.919 0.2 1 18 112 10 ASP H H 8.828 0.01 1 19 112 10 ASP CA C 58.32 0.2 1 20 112 10 ASP CB C 37.75 0.2 1 21 112 10 ASP N N 123.142 0.2 1 22 113 11 ASN CA C 54.73 0.2 1 23 113 11 ASN CB C 40.79 0.2 1 24 114 12 ILE H H 8.295 0.2 1 25 114 12 ILE CA C 53.50 0.2 1 26 114 12 ILE CB C 38.77 0.2 1 27 114 12 ILE N N 117.647 0.2 1 28 115 13 ARG H H 7.929 0.01 1 29 115 13 ARG CA C 60.99 0.2 1 30 115 13 ARG CB C 37.79 0.2 1 31 115 13 ARG N N 126.682 0.2 1 32 116 14 HIS H H 8.465 0.01 1 33 116 14 HIS CA C 55.58 0.2 1 34 116 14 HIS CB C 30.49 0.2 1 35 116 14 HIS N N 126.143 0.2 1 36 117 15 GLY H H 8.428 0.01 1 37 117 15 GLY CA C 45.02 0.2 1 38 117 15 GLY N N 109.150 0.2 1 39 118 16 VAL H H 8.166 0.01 1 40 118 16 VAL CA C 62.29 0.2 1 41 118 16 VAL CB C 31.47 0.2 1 42 118 16 VAL N N 121.068 0.2 1 43 119 17 CYS H H 8.398 0.01 1 44 119 17 CYS CA C 57.67 0.2 1 45 119 17 CYS CB C 29.91 0.2 1 46 119 17 CYS N N 127.491 0.2 1 47 120 18 TRP H H 8.402 0.01 1 48 120 18 TRP CA C 55.91 0.2 1 49 120 18 TRP CB C 30.75 0.2 1 50 120 18 TRP N N 125.627 0.2 1 51 121 19 ILE H H 9.248 0.01 1 52 121 19 ILE CA C 60.01 0.2 1 53 121 19 ILE CB C 39.22 0.2 1 54 121 19 ILE N N 125.595 0.2 1 55 122 20 TYR H H 8.516 0.01 1 56 122 20 TYR CA C 57.34 0.2 1 57 122 20 TYR CB C 39.16 0.2 1 58 122 20 TYR N N 124.794 0.2 1 59 123 21 TYR H H 8.773 0.01 1 60 123 21 TYR CA C 55.78 0.2 1 61 123 21 TYR CB C 36.49 0.2 1 62 123 21 TYR N N 124.206 0.2 1 63 124 22 PRO CA C 64.96 0.2 1 64 124 22 PRO CB C 30.69 0.2 1 65 125 23 ASP H H 6.686 0.01 1 66 125 23 ASP CA C 54.28 0.2 1 67 125 23 ASP CB C 42.81 0.2 1 68 125 23 ASP N N 112.260 0.2 1 69 126 24 GLY H H 7.967 0.01 1 70 126 24 GLY CA C 44.76 0.2 1 71 126 24 GLY N N 108.819 0.2 1 72 127 25 GLY H H 9.239 0.01 1 73 127 25 GLY CA C 44.37 0.2 1 74 127 25 GLY N N 112.796 0.2 1 75 128 26 SER H H 8.415 0.01 1 76 128 26 SER CA C 57.67 0.2 1 77 128 26 SER CB C 66.20 0.2 1 78 128 26 SER N N 113.466 0.2 1 79 129 27 LEU H H 8.479 0.01 1 80 129 27 LEU CA C 53.04 0.2 1 81 129 27 LEU CB C 45.35 0.2 1 82 129 27 LEU N N 120.230 0.2 1 83 130 28 VAL H H 8.767 0.01 1 84 130 28 VAL CA C 57.80 0.2 1 85 130 28 VAL CB C 33.36 0.2 1 86 130 28 VAL N N 120.209 0.2 1 87 131 29 GLY H H 7.938 0.01 1 88 131 29 GLY CA C 44.50 0.2 1 89 131 29 GLY N N 112.311 0.2 1 90 132 30 GLU H H 8.281 0.01 1 91 132 30 GLU CA C 55.58 0.2 1 92 132 30 GLU CB C 29.58 0.2 1 93 132 30 GLU N N 122.097 0.2 1 94 133 31 VAL H H 7.601 0.01 1 95 133 31 VAL CA C 60.40 0.2 1 96 133 31 VAL CB C 32.38 0.2 1 97 133 31 VAL N N 118.860 0.2 1 98 134 32 ASN H H 8.433 0.01 1 99 134 32 ASN CA C 51.21 0.2 1 100 134 32 ASN CB C 38.11 0.2 1 101 134 32 ASN N N 120.237 0.2 1 102 135 33 GLU H H 9.043 0.01 1 103 135 33 GLU CA C 59.16 0.2 1 104 135 33 GLU CB C 28.41 0.2 1 105 135 33 GLU N N 118.573 0.2 1 106 136 34 ASP H H 7.269 0.01 1 107 136 34 ASP CA C 54.15 0.2 1 108 136 34 ASP CB C 41.44 0.2 1 109 136 34 ASP N N 117.228 0.2 1 110 137 35 GLY H H 8.270 0.01 1 111 137 35 GLY CA C 45.58 0.2 1 112 137 35 GLY N N 109.106 0.2 1 113 138 36 GLU H H 7.877 0.01 1 114 138 36 GLU CA C 54.47 0.2 1 115 138 36 GLU CB C 31.08 0.2 1 116 138 36 GLU N N 119.010 0.2 1 117 139 37 MET H H 9.249 0.01 1 118 139 37 MET CA C 53.10 0.2 1 119 139 37 MET CB C 28.60 0.2 1 120 139 37 MET N N 125.064 0.2 1 121 140 38 THR H H 7.586 0.01 1 122 140 38 THR CA C 59.56 0.2 1 123 140 38 THR CB C 72.13 0.2 1 124 140 38 THR N N 122.527 0.2 1 125 141 39 GLY H H 8.807 0.01 1 126 141 39 GLY CA C 44.70 0.2 1 127 141 39 GLY N N 115.354 0.2 1 128 143 41 LYS CA C 54.15 0.2 1 129 143 41 LYS CB C 31.54 0.2 1 130 144 42 ILE H H 7.929 0.01 1 131 144 42 ILE CA C 58.38 0.2 1 132 144 42 ILE CB C 37.46 0.2 1 133 144 42 ILE N N 126.682 0.2 1 134 145 43 ALA H H 8.002 0.01 1 135 145 43 ALA CA C 49.78 0.2 1 136 145 43 ALA CB C 23.32 0.2 1 137 145 43 ALA N N 124.524 0.2 1 138 146 44 TYR H H 8.003 0.01 1 139 146 44 TYR CA C 56.23 0.2 1 140 146 44 TYR CB C 37.07 0.2 1 141 146 44 TYR N N 120.479 0.2 1 142 147 45 VAL H H 8.291 0.01 1 143 147 45 VAL CA C 62.83 0.2 1 144 147 45 VAL CB C 31.75 0.2 1 145 147 45 VAL N N 122.097 0.2 1 146 148 46 TYR H H 7.456 0.01 1 147 148 46 TYR CA C 54.06 0.2 1 148 148 46 TYR CB C 37.51 0.2 1 149 148 46 TYR N N 117.217 0.2 1 150 149 47 PRO CA C 64.31 0.2 1 151 149 47 PRO CB C 31.93 0.2 1 152 150 48 ASP H H 7.254 0.01 1 153 150 48 ASP CA C 54.15 0.2 1 154 150 48 ASP CB C 39.41 0.2 1 155 150 48 ASP N N 114.749 0.2 1 156 151 49 GLU H H 8.837 0.01 1 157 151 49 GLU CA C 57.99 0.2 1 158 151 49 GLU CB C 27.10 0.2 1 159 151 49 GLU N N 114.594 0.2 1 160 152 50 ARG H H 7.939 0.2 1 161 152 50 ARG CA C 57.80 0.2 1 162 152 50 ARG CB C 33.95 0.2 1 163 152 50 ARG N N 116.034 0.2 1 164 153 51 THR H H 10.073 0.01 1 165 153 51 THR CA C 64.83 0.2 1 166 153 51 THR CB C 66.85 0.2 1 167 153 51 THR N N 122.549 0.2 1 168 154 52 ALA H H 8.972 0.01 1 169 154 52 ALA CA C 49.98 0.2 1 170 154 52 ALA CB C 24.56 0.2 1 171 154 52 ALA N N 130.145 0.2 1 172 155 53 LEU H H 9.412 0.01 1 173 155 53 LEU CA C 53.10 0.2 1 174 155 53 LEU CB C 42.94 0.2 1 175 155 53 LEU N N 119.939 0.2 1 176 156 54 TYR H H 9.452 0.01 1 177 156 54 TYR CA C 55.39 0.2 1 178 156 54 TYR CB C 42.87 0.2 1 179 156 54 TYR N N 124.995 0.2 1 180 157 55 GLY H H 9.657 0.01 1 181 157 55 GLY CA C 46.46 0.2 1 182 157 55 GLY N N 119.543 0.2 1 183 158 56 LYS H H 7.796 0.01 1 184 158 56 LYS CA C 55.71 0.2 1 185 158 56 LYS CB C 33.56 0.2 1 186 158 56 LYS N N 124.497 0.2 1 187 159 57 PHE H H 8.908 0.01 1 188 159 57 PHE CA C 55.78 0.2 1 189 159 57 PHE CB C 43.33 0.2 1 190 159 57 PHE N N 128.301 0.2 1 191 160 58 ILE H H 8.893 0.01 1 192 160 58 ILE CA C 60.99 0.2 1 193 160 58 ILE CB C 40.14 0.2 1 194 160 58 ILE N N 120.119 0.2 1 195 161 59 ASP H H 10.027 0.01 1 196 161 59 ASP CA C 54.54 0.2 1 197 161 59 ASP CB C 39.09 0.2 1 198 161 59 ASP N N 134.774 0.2 1 199 162 60 GLY H H 8.429 0.01 1 200 162 60 GLY CA C 45.68 0.2 1 201 162 60 GLY N N 101.867 0.2 1 202 163 61 GLU H H 8.204 0.01 1 203 163 61 GLU CA C 54.73 0.2 1 204 163 61 GLU CB C 30.62 0.2 1 205 163 61 GLU N N 124.255 0.2 1 206 164 62 MET H H 9.072 0.01 1 207 164 62 MET CA C 57.08 0.2 1 208 164 62 MET CB C 32.84 0.2 1 209 164 62 MET N N 128.250 0.2 1 210 165 63 ILE H H 8.598 0.01 1 211 165 63 ILE CA C 60.47 0.2 1 212 165 63 ILE N N 132.368 0.2 1 213 166 64 GLU H H 7.723 0.01 1 214 166 64 GLU CA C 56.30 0.2 1 215 166 64 GLU CB C 31.67 0.2 1 216 166 64 GLU N N 118.337 0.2 1 217 167 65 GLY H H 9.328 0.01 1 218 167 65 GLY CA C 43.59 0.2 1 219 167 65 GLY N N 115.623 0.2 1 220 168 66 LYS H H 8.934 0.01 1 221 168 66 LYS CA C 55.06 0.2 1 222 168 66 LYS CB C 34.73 0.2 1 223 168 66 LYS N N 123.989 0.2 1 224 169 67 LEU H H 8.697 0.01 1 225 169 67 LEU CA C 56.43 0.2 1 226 169 67 LEU CB C 42.09 0.2 1 227 169 67 LEU N N 123.985 0.2 1 228 170 68 ALA H H 9.637 0.01 1 229 170 68 ALA CA C 50.76 0.2 1 230 170 68 ALA CB C 23.52 0.2 1 231 170 68 ALA N N 130.458 0.2 1 232 171 69 THR H H 8.906 0.01 1 233 171 69 THR CA C 60.60 0.2 1 234 171 69 THR CB C 71.02 0.2 1 235 171 69 THR N N 116.155 0.2 1 236 172 70 LEU H H 9.413 0.01 1 237 172 70 LEU CA C 55.52 0.2 1 238 172 70 LEU CB C 40.72 0.2 1 239 172 70 LEU N N 130.334 0.2 1 240 173 71 MET H H 8.695 0.01 1 241 173 71 MET CA C 55.25 0.2 1 242 173 71 MET CB C 32.77 0.2 1 243 173 71 MET N N 128.024 0.2 1 244 174 72 SER H H 7.665 0.01 1 245 174 72 SER CA C 57.47 0.2 1 246 174 72 SER CB C 63.66 0.2 1 247 174 72 SER N N 112.350 0.2 1 248 175 73 THR H H 8.396 0.01 1 249 175 73 THR CA C 61.18 0.2 1 250 175 73 THR CB C 70.18 0.2 1 251 175 73 THR N N 114.140 0.2 1 252 176 74 GLU H H 8.460 0.01 1 253 176 74 GLU CA C 56.43 0.2 1 254 176 74 GLU CB C 30.30 0.2 1 255 176 74 GLU N N 124.210 0.2 1 256 177 75 GLU H H 7.863 0.01 1 257 177 75 GLU CA C 54.08 0.2 1 258 177 75 GLU CB C 31.54 0.2 1 259 177 75 GLU N N 120.888 0.2 1 260 178 76 GLY CA C 45.23 0.2 1 261 179 77 ARG H H 8.087 0.01 1 262 179 77 ARG CA C 55.58 0.2 1 263 179 77 ARG CB C 29.25 0.2 1 264 179 77 ARG N N 120.209 0.2 1 265 180 78 PRO CA C 62.36 0.2 1 266 181 79 HIS H H 7.383 0.01 1 267 181 79 HIS CA C 54.67 0.2 1 268 181 79 HIS CB C 31.34 0.2 1 269 181 79 HIS N N 120.692 0.2 1 270 182 80 PHE H H 8.233 0.01 1 271 182 80 PHE CA C 56.56 0.2 1 272 182 80 PHE CB C 40.92 0.2 1 273 182 80 PHE N N 123.669 0.2 1 274 183 81 GLU H H 8.454 0.01 1 275 183 81 GLU CA C 54.28 0.2 1 276 183 81 GLU CB C 31.60 0.2 1 277 183 81 GLU N N 121.288 0.2 1 278 184 82 LEU H H 8.903 0.01 1 279 184 82 LEU CA C 55.65 0.2 1 280 184 82 LEU CB C 40.85 0.2 1 281 184 82 LEU N N 127.761 0.2 1 282 185 83 MET H H 8.399 0.01 1 283 185 83 MET CA C 53.04 0.2 1 284 185 83 MET CB C 31.01 0.2 1 285 185 83 MET N N 123.176 0.2 1 286 186 84 PRO CA C 63.40 0.2 1 287 186 84 PRO CB C 31.54 0.2 1 288 187 85 GLY CA C 44.50 0.2 1 289 188 86 ASN CA C 52.78 0.2 1 290 188 86 ASN CB C 39.16 0.2 1 291 189 87 SER H H 8.178 0.01 1 292 189 87 SER CA C 60.01 0.2 1 293 189 87 SER CB C 63.01 0.2 1 294 189 87 SER N N 118.051 0.2 1 295 190 88 VAL H H 7.836 0.01 1 296 190 88 VAL CA C 60.21 0.2 1 297 190 88 VAL CB C 34.27 0.2 1 298 190 88 VAL N N 122.352 0.2 1 299 191 89 TYR H H 9.001 0.01 1 300 191 89 TYR CA C 56.23 0.2 1 301 191 89 TYR CB C 40.46 0.2 1 302 191 89 TYR N N 122.367 0.2 1 303 192 90 HIS H H 8.359 0.01 1 304 192 90 HIS CA C 53.82 0.2 1 305 192 90 HIS CB C 32.58 0.2 1 306 192 90 HIS N N 116.972 0.2 1 307 193 91 PHE H H 8.616 0.01 1 308 193 91 PHE CA C 59.88 0.2 1 309 193 91 PHE CB C 38.12 0.2 1 310 193 91 PHE N N 121.018 0.2 1 311 194 92 ASP H H 9.283 0.01 1 312 194 92 ASP CA C 52.84 0.2 1 313 194 92 ASP CB C 41.64 0.2 1 314 194 92 ASP N N 134.249 0.2 1 315 195 93 LYS H H 6.307 0.01 1 316 195 93 LYS CA C 57.21 0.2 1 317 195 93 LYS CB C 32.58 0.2 1 318 195 93 LYS N N 122.161 0.2 1 319 196 94 SER H H 9.940 0.01 1 320 196 94 SER CA C 57.80 0.2 1 321 196 94 SER CB C 64.96 0.2 1 322 196 94 SER N N 126.129 0.2 1 323 197 95 THR H H 8.234 0.01 1 324 197 95 THR CA C 59.16 0.2 1 325 197 95 THR CB C 71.02 0.2 1 326 197 95 THR N N 108.829 0.2 1 327 198 96 SER H H 8.478 0.01 1 328 198 96 SER CA C 60.60 0.2 1 329 198 96 SER CB C 63.01 0.2 1 330 198 96 SER N N 113.897 0.2 1 331 199 97 SER CA C 57.60 0.2 1 332 199 97 SER CB C 63.07 0.2 1 333 200 98 CYS H H 9.014 0.01 1 334 200 98 CYS CA C 55.52 0.2 1 335 200 98 CYS CB C 41.18 0.2 1 336 200 98 CYS N N 127.491 0.2 1 337 201 99 ILE H H 8.757 0.01 1 338 201 99 ILE CA C 60.99 0.2 1 339 201 99 ILE CB C 36.49 0.2 1 340 201 99 ILE N N 125.794 0.2 1 341 202 100 SER H H 8.487 0.01 1 342 202 100 SER CA C 60.27 0.2 1 343 202 100 SER CB C 62.68 0.2 1 344 202 100 SER N N 124.524 0.2 1 345 203 101 THR CA C 64.05 0.2 1 346 203 101 THR CB C 68.94 0.2 1 347 204 102 ASN H H 8.488 0.2 1 348 204 102 ASN CA C 52.52 0.2 1 349 204 102 ASN CB C 38.31 0.2 1 350 204 102 ASN N N 121.993 0.2 1 351 205 103 ALA H H 8.566 0.01 1 352 205 103 ALA CA C 54.86 0.2 1 353 205 103 ALA CB C 19.35 0.2 1 354 205 103 ALA N N 123.176 0.2 1 355 206 104 LEU H H 7.975 0.01 1 356 206 104 LEU CA C 53.30 0.2 1 357 206 104 LEU CB C 40.14 0.2 1 358 206 104 LEU N N 114.561 0.2 1 359 207 105 LEU H H 7.242 0.01 1 360 207 105 LEU CA C 51.54 0.2 1 361 207 105 LEU CB C 41.89 0.2 1 362 207 105 LEU N N 125.750 0.2 1 363 208 106 PRO CA C 63.07 0.2 1 364 208 106 PRO CB C 31.73 0.2 1 365 209 107 ASP CA C 55.25 0.2 1 366 209 107 ASP CB C 41.31 0.2 1 367 213 111 SER CA C 58.64 0.2 1 368 214 112 GLU H H 8.712 0.01 1 369 214 112 GLU CA C 54.33 0.2 1 370 214 112 GLU CB C 34.97 0.2 1 371 214 112 GLU N N 114.004 0.2 1 372 215 113 ARG H H 7.351 0.01 1 373 215 113 ARG CA C 54.33 0.2 1 374 215 113 ARG CB C 30.84 0.2 1 375 215 113 ARG N N 120.461 0.2 1 376 216 114 VAL H H 9.365 0.01 1 377 216 114 VAL CA C 64.14 0.2 1 378 216 114 VAL CB C 30.84 0.2 1 379 216 114 VAL N N 125.614 0.2 1 380 217 115 TYR CA C 55.58 0.2 1 381 217 115 TYR CB C 40.53 0.2 1 382 218 116 VAL H H 8.431 0.01 1 383 218 116 VAL CA C 60.79 0.2 1 384 218 116 VAL CB C 32.45 0.2 1 385 218 116 VAL N N 121.557 0.2 1 386 219 117 ALA H H 8.490 0.01 1 387 219 117 ALA CA C 50.95 0.2 1 388 219 117 ALA CB C 21.07 0.2 1 389 219 117 ALA N N 129.546 0.2 1 390 220 118 GLU H H 8.279 0.01 1 391 220 118 GLU CA C 58.12 0.2 1 392 220 118 GLU CB C 29.06 0.2 1 393 220 118 GLU N N 121.288 0.2 1 394 221 119 SER H H 8.612 0.01 1 395 221 119 SER CA C 58.64 0.2 1 396 221 119 SER CB C 62.36 0.2 1 397 221 119 SER N N 117.242 0.2 1 398 222 120 LEU H H 9.074 0.01 1 399 222 120 LEU CA C 55.65 0.2 1 400 222 120 LEU CB C 40.07 0.2 1 401 222 120 LEU N N 128.031 0.2 1 402 225 123 SER H H 8.387 0.01 1 403 225 123 SER CA C 59.62 0.2 1 404 225 123 SER CB C 62.49 0.2 1 405 225 123 SER N N 113.513 0.2 1 406 226 124 ALA H H 7.437 0.01 1 407 226 124 ALA CA C 52.26 0.2 1 408 226 124 ALA CB C 17.13 0.2 1 409 226 124 ALA N N 121.990 0.2 1 410 227 125 GLY H H 8.131 0.01 1 411 227 125 GLY CA C 45.87 0.2 1 412 227 125 GLY N N 107.207 0.2 1 413 228 126 GLU H H 8.371 0.01 1 414 228 126 GLU CA C 55.91 0.2 1 415 228 126 GLU CB C 31.40 0.2 1 416 228 126 GLU N N 124.147 0.2 1 417 229 127 GLY H H 9.331 0.01 1 418 229 127 GLY CA C 43.72 0.2 1 419 229 127 GLY N N 109.653 0.2 1 420 231 129 PHE CA C 63.54 0.2 1 421 232 130 SER CA C 58.24 0.2 1 422 232 130 SER CB C 64.40 0.2 1 423 234 132 VAL H H 7.680 0.01 1 424 234 132 VAL CA C 58.51 0.2 1 425 234 132 VAL CB C 35.71 0.2 1 426 234 132 VAL N N 109.346 0.2 1 427 235 133 ALA H H 8.234 0.01 1 428 235 133 ALA CA C 51.35 0.2 1 429 235 133 ALA CB C 18.05 0.2 1 430 235 133 ALA N N 124.524 0.2 1 431 236 134 VAL H H 8.371 0.01 1 432 236 134 VAL CA C 59.16 0.2 1 433 236 134 VAL CB C 35.90 0.2 1 434 236 134 VAL N N 115.921 0.2 1 435 237 135 GLY H H 8.248 0.01 1 436 237 135 GLY CA C 44.18 0.2 1 437 237 135 GLY N N 106.722 0.2 1 438 238 136 PRO CA C 62.22 0.2 1 439 238 136 PRO CB C 32.32 0.2 1 440 239 137 ASN H H 7.443 0.01 1 441 239 137 ASN CA C 51.99 0.2 1 442 239 137 ASN CB C 37.79 0.2 1 443 239 137 ASN N N 112.584 0.2 1 444 240 138 THR H H 8.560 0.01 1 445 240 138 THR CA C 63.07 0.2 1 446 240 138 THR CB C 69.40 0.2 1 447 240 138 THR N N 118.275 0.2 1 448 241 139 VAL H H 9.877 0.01 1 449 241 139 VAL CA C 64.83 0.2 1 450 241 139 VAL CB C 30.49 0.2 1 451 241 139 VAL N N 130.628 0.2 1 452 242 140 MET CA C 54.40 0.2 1 453 243 141 SER H H 6.767 0.01 1 454 243 141 SER CA C 56.36 0.2 1 455 243 141 SER CB C 65.55 0.2 1 456 243 141 SER N N 102.299 0.2 1 457 244 142 PHE H H 9.438 0.01 1 458 244 142 PHE CA C 54.34 0.2 1 459 244 142 PHE CB C 43.66 0.2 1 460 244 142 PHE N N 117.170 0.2 1 461 245 143 TYR CA C 54.93 0.2 1 462 246 144 ASN H H 6.516 0.01 1 463 246 144 ASN CA C 51.93 0.2 1 464 246 144 ASN CB C 40.20 0.2 1 465 246 144 ASN N N 117.604 0.2 1 466 247 145 GLY H H 6.739 0.01 1 467 247 145 GLY CA C 45.42 0.2 1 468 247 145 GLY N N 105.526 0.2 1 469 248 146 VAL CA C 61.79 0.2 1 470 248 146 VAL CB C 30.70 0.2 1 471 249 147 ARG H H 6.847 0.01 1 472 249 147 ARG CA C 54.79 0.2 1 473 249 147 ARG CB C 30.23 0.2 1 474 249 147 ARG N N 120.617 0.2 1 475 250 148 ILE H H 8.921 0.01 1 476 250 148 ILE CA C 59.03 0.2 1 477 250 148 ILE CB C 40.39 0.2 1 478 250 148 ILE N N 120.436 0.2 1 479 251 149 THR H H 8.052 0.01 1 480 251 149 THR CA C 60.73 0.2 1 481 251 149 THR CB C 71.81 0.2 1 482 251 149 THR N N 110.388 0.2 1 483 252 150 HIS H H 8.438 0.01 1 484 252 150 HIS CA C 59.56 0.2 1 485 252 150 HIS CB C 28.41 0.2 1 486 252 150 HIS N N 118.615 0.2 1 487 253 151 GLN H H 8.467 0.01 1 488 253 151 GLN CA C 59.36 0.2 1 489 253 151 GLN CB C 27.17 0.2 1 490 253 151 GLN N N 118.051 0.2 1 491 254 152 GLU H H 7.603 0.01 1 492 254 152 GLU CA C 58.77 0.2 1 493 254 152 GLU CB C 29.06 0.2 1 494 254 152 GLU N N 119.902 0.2 1 495 255 153 VAL H H 7.148 0.01 1 496 255 153 VAL CA C 66.20 0.2 1 497 255 153 VAL CB C 31.27 0.2 1 498 255 153 VAL N N 119.664 0.2 1 499 256 154 ASP H H 8.477 0.01 1 500 256 154 ASP CA C 56.30 0.2 1 501 256 154 ASP CB C 40.07 0.2 1 502 256 154 ASP N N 118.299 0.2 1 503 257 155 SER H H 7.313 0.01 1 504 257 155 SER CA C 58.38 0.2 1 505 257 155 SER CB C 63.92 0.2 1 506 257 155 SER N N 111.847 0.2 1 507 258 156 ARG H H 7.279 0.01 1 508 258 156 ARG CA C 53.76 0.2 1 509 258 156 ARG CB C 31.27 0.2 1 510 258 156 ARG N N 121.060 0.2 1 511 259 157 ASP H H 8.056 0.01 1 512 259 157 ASP CA C 54.34 0.2 1 513 259 157 ASP CB C 42.35 0.2 1 514 259 157 ASP N N 119.728 0.2 1 515 260 158 TRP H H 8.262 0.01 1 516 260 158 TRP CA C 60.01 0.2 1 517 260 158 TRP CB C 28.34 0.2 1 518 260 158 TRP N N 123.996 0.2 1 519 261 159 ALA H H 8.649 0.01 1 520 261 159 ALA CA C 54.47 0.2 1 521 261 159 ALA CB C 17.33 0.2 1 522 261 159 ALA N N 124.180 0.2 1 523 262 160 LEU H H 7.862 0.01 1 524 262 160 LEU CA C 54.60 0.2 1 525 262 160 LEU CB C 41.70 0.2 1 526 262 160 LEU N N 116.960 0.2 1 527 263 161 ASN CA C 54.41 0.2 1 528 263 161 ASN CB C 37.27 0.2 1 529 264 162 GLY H H 8.728 0.01 1 530 264 162 GLY CA C 47.76 0.2 1 531 264 162 GLY N N 109.169 0.2 1 532 265 163 ASN H H 9.398 0.01 1 533 265 163 ASN CA C 51.61 0.2 1 534 265 163 ASN CB C 39.03 0.2 1 535 265 163 ASN N N 116.702 0.2 1 536 266 164 THR H H 7.340 0.01 1 537 266 164 THR CA C 60.73 0.2 1 538 266 164 THR CB C 69.98 0.2 1 539 266 164 THR N N 113.696 0.2 1 540 267 165 LEU H H 8.784 0.01 1 541 267 165 LEU CA C 53.63 0.2 1 542 267 165 LEU CB C 44.31 0.2 1 543 267 165 LEU N N 125.291 0.2 1 544 268 166 SER H H 8.775 0.01 1 545 268 166 SER CA C 60.47 0.2 1 546 268 166 SER CB C 62.23 0.2 1 547 268 166 SER N N 123.445 0.2 1 548 269 167 LEU H H 8.718 0.01 1 549 269 167 LEU CA C 56.01 0.2 1 550 269 167 LEU CB C 43.13 0.2 1 551 269 167 LEU N N 129.110 0.2 1 552 270 168 ASP CA C 53.10 0.2 1 553 270 168 ASP CB C 40.07 0.2 1 554 271 169 GLU H H 8.797 0.01 1 555 271 169 GLU CA C 58.90 0.2 1 556 271 169 GLU CB C 28.67 0.2 1 557 271 169 GLU N N 116.140 0.2 1 558 272 170 GLU H H 8.583 0.01 1 559 272 170 GLU CA C 57.08 0.2 1 560 272 170 GLU CB C 31.93 0.2 1 561 272 170 GLU N N 117.774 0.2 1 562 273 171 THR H H 8.480 0.01 1 563 273 171 THR CA C 63.07 0.2 1 564 273 171 THR CB C 70.05 0.2 1 565 273 171 THR N N 119.036 0.2 1 566 274 172 VAL H H 8.799 0.01 1 567 274 172 VAL CA C 60.66 0.2 1 568 274 172 VAL CB C 33.29 0.2 1 569 274 172 VAL N N 128.840 0.2 1 570 275 173 ILE H H 8.607 0.01 1 571 275 173 ILE CA C 58.77 0.2 1 572 275 173 ILE CB C 38.38 0.2 1 573 275 173 ILE N N 125.571 0.2 1 574 281 179 TYR CA C 56.29 0.2 1 575 281 179 TYR CB C 40.07 0.2 1 576 282 180 ASN H H 8.116 0.01 1 577 282 180 ASN CA C 53.04 0.2 1 578 282 180 ASN CB C 40.00 0.2 1 579 282 180 ASN N N 117.286 0.2 1 580 283 181 HIS H H 9.836 0.01 1 581 283 181 HIS CA C 56.30 0.2 1 582 283 181 HIS CB C 31.27 0.2 1 583 283 181 HIS N N 119.400 0.2 1 584 284 182 VAL CA C 60.47 0.2 1 585 285 183 SER H H 7.772 0.01 1 586 285 183 SER CA C 57.67 0.2 1 587 285 183 SER CB C 65.03 0.2 1 588 285 183 SER N N 111.309 0.2 1 589 286 184 LYS H H 7.580 0.01 1 590 286 184 LYS CA C 56.88 0.2 1 591 286 184 LYS CB C 27.23 0.2 1 592 286 184 LYS N N 125.603 0.2 1 593 287 185 TYR H H 8.420 0.01 1 594 287 185 TYR CA C 63.79 0.2 1 595 287 185 TYR CB C 38.77 0.2 1 596 287 185 TYR N N 128.840 0.2 1 597 288 186 CYS CA C 58.45 0.2 1 598 288 186 CYS CB C 35.38 0.2 1 599 289 187 ALA H H 8.478 0.01 1 600 289 187 ALA CA C 50.69 0.2 1 601 289 187 ALA CB C 17.07 0.2 1 602 289 187 ALA N N 125.603 0.2 1 603 291 189 LEU CA C 52.80 0.2 1 604 292 190 GLY H H 8.987 0.01 1 605 292 190 GLY CA C 47.77 0.2 1 606 292 190 GLY N N 113.196 0.2 1 607 293 191 HIS H H 8.022 0.01 1 608 293 191 HIS CA C 57.21 0.2 1 609 293 191 HIS CB C 28.15 0.2 1 610 293 191 HIS N N 116.972 0.2 1 611 294 192 LYS H H 7.695 0.01 1 612 294 192 LYS CA C 53.95 0.2 1 613 294 192 LYS CB C 30.10 0.2 1 614 294 192 LYS N N 119.130 0.2 1 615 295 193 ALA H H 6.693 0.01 1 616 295 193 ALA CA C 52.06 0.2 1 617 295 193 ALA CB C 17.20 0.2 1 618 295 193 ALA N N 117.781 0.2 1 619 298 196 SER H H 6.687 0.01 1 620 298 196 SER CA C 55.58 0.2 1 621 298 196 SER CB C 65.03 0.2 1 622 298 196 SER N N 116.744 0.2 1 623 299 197 PHE H H 8.281 0.01 1 624 299 197 PHE CA C 60.21 0.2 1 625 299 197 PHE CB C 37.60 0.2 1 626 299 197 PHE N N 119.829 0.2 1 627 300 198 THR H H 8.489 0.01 1 628 300 198 THR CA C 57.34 0.2 1 629 300 198 THR CB C 68.48 0.2 1 630 300 198 THR N N 112.823 0.2 1 631 301 199 PRO CA C 63.20 0.2 1 632 301 199 PRO CB C 31.93 0.2 1 633 302 200 ASN H H 8.518 0.01 1 634 302 200 ASN CA C 55.32 0.2 1 635 302 200 ASN CB C 41.18 0.2 1 636 302 200 ASN N N 121.288 0.2 1 637 303 201 CYS H H 7.969 0.01 1 638 303 201 CYS CA C 53.21 0.2 1 639 303 201 CYS CB C 31.93 0.2 1 640 303 201 CYS N N 120.104 0.2 1 641 306 204 ASP CA C 51.80 0.2 1 642 306 204 ASP CB C 45.09 0.2 1 643 307 205 MET H H 8.749 0.01 1 644 307 205 MET CA C 56.10 0.2 1 645 307 205 MET CB C 32.19 0.2 1 646 307 205 MET N N 123.629 0.2 1 647 308 206 PHE H H 8.325 0.01 1 648 308 206 PHE CA C 58.51 0.2 1 649 308 206 PHE CB C 44.05 0.2 1 650 308 206 PHE N N 123.386 0.2 1 651 309 207 VAL H H 8.245 0.01 1 652 309 207 VAL CA C 61.77 0.2 1 653 309 207 VAL CB C 30.10 0.2 1 654 309 207 VAL N N 128.998 0.2 1 655 316 214 ILE CA C 61.50 0.2 1 656 317 215 LYS H H 6.689 0.01 1 657 317 215 LYS CA C 56.30 0.2 1 658 317 215 LYS CB C 29.71 0.2 1 659 317 215 LYS N N 115.918 0.2 1 660 318 216 CYS H H 7.662 0.01 1 661 318 216 CYS CA C 57.73 0.2 1 662 318 216 CYS CB C 33.36 0.2 1 663 318 216 CYS N N 117.781 0.2 1 664 319 217 ILE CA C 59.37 0.2 1 665 319 217 ILE CB C 45.23 0.2 1 666 320 218 ARG CA C 51.31 0.2 1 667 320 218 ARG CB C 30.84 0.2 1 668 323 221 ARG CA C 60.21 0.2 1 669 324 222 ALA H H 8.580 0.01 1 670 324 222 ALA CA C 50.95 0.2 1 671 324 222 ALA CB C 21.11 0.2 1 672 324 222 ALA N N 129.627 0.2 1 673 325 223 VAL H H 8.197 0.01 1 674 325 223 VAL CA C 57.54 0.2 1 675 325 223 VAL CB C 29.32 0.2 1 676 325 223 VAL N N 120.209 0.2 1 677 326 224 GLU CA C 54.67 0.2 1 678 326 224 GLU CB C 30.95 0.2 1 679 327 225 ALA H H 8.295 0.01 1 680 327 225 ALA CA C 53.76 0.2 1 681 327 225 ALA CB C 17.85 0.2 1 682 327 225 ALA N N 121.557 0.2 1 683 328 226 ASP H H 9.082 0.01 1 684 328 226 ASP CA C 56.82 0.2 1 685 328 226 ASP CB C 38.77 0.2 1 686 328 226 ASP N N 116.972 0.2 1 687 333 231 VAL CA C 58.51 0.2 1 688 333 231 VAL CB C 34.45 0.2 1 689 334 232 ALA H H 8.529 0.01 1 690 334 232 ALA CA C 52.06 0.2 1 691 334 232 ALA CB C 18.76 0.2 1 692 334 232 ALA N N 123.626 0.2 1 693 335 233 TYR CA C 56.17 0.2 1 694 335 233 TYR CB C 35.51 0.2 1 695 336 234 GLY H H 8.757 0.01 1 696 336 234 GLY CA C 46.72 0.2 1 697 336 234 GLY N N 108.611 0.2 1 698 337 235 TYR CA C 54.91 0.2 1 699 337 235 TYR CB C 39.99 0.2 1 700 338 236 ASP CA C 57.20 0.2 1 701 338 236 ASP CB C 39.27 0.2 1 702 343 241 GLY CA C 45.16 0.2 1 703 344 242 LYS CA C 53.01 0.2 1 704 344 242 LYS CB C 30.05 0.2 1 705 345 243 SER CA C 58.12 0.2 1 706 345 243 SER CB C 63.47 0.2 1 707 346 244 GLY H H 7.968 0.01 1 708 346 244 GLY CA C 44.37 0.2 1 709 346 244 GLY N N 111.219 0.2 1 710 348 246 GLU CA C 55.56 0.2 1 711 349 247 ALA H H 5.857 0.01 1 712 349 247 ALA CA C 54.71 0.2 1 713 349 247 ALA CB C 17.69 0.2 1 714 349 247 ALA N N 125.755 0.2 1 715 351 249 GLU CA C 60.27 0.2 1 716 351 249 GLU CB C 28.67 0.2 1 717 352 250 TRP H H 7.855 0.01 1 718 352 250 TRP CA C 58.64 0.2 1 719 352 250 TRP CB C 26.71 0.2 1 720 352 250 TRP N N 115.058 0.2 1 721 353 251 TYR H H 5.700 0.01 1 722 353 251 TYR CA C 60.92 0.2 1 723 353 251 TYR CB C 36.55 0.2 1 724 353 251 TYR N N 126.143 0.2 1 725 354 252 GLN H H 7.490 0.01 1 726 354 252 GLN CA C 59.16 0.2 1 727 354 252 GLN CB C 27.76 0.2 1 728 354 252 GLN N N 119.400 0.2 1 729 355 253 VAL H H 8.248 0.01 1 730 355 253 VAL CA C 66.40 0.2 1 731 355 253 VAL CB C 31.60 0.2 1 732 355 253 VAL N N 120.214 0.2 1 733 356 254 GLU H H 7.607 0.01 1 734 356 254 GLU CA C 59.43 0.2 1 735 356 254 GLU CB C 28.79 0.2 1 736 356 254 GLU N N 121.557 0.2 1 737 357 255 LEU H H 8.826 0.01 1 738 357 255 LEU CA C 57.79 0.2 1 739 357 255 LEU CB C 40.20 0.2 1 740 357 255 LEU N N 123.985 0.2 1 741 358 256 LYS H H 7.723 0.01 1 742 358 256 LYS CA C 59.16 0.2 1 743 358 256 LYS CB C 31.47 0.2 1 744 358 256 LYS N N 119.584 0.2 1 745 359 257 ALA H H 7.569 0.01 1 746 359 257 ALA CA C 54.67 0.2 1 747 359 257 ALA CB C 17.39 0.2 1 748 359 257 ALA N N 121.772 0.2 1 749 360 258 PHE H H 8.375 0.01 1 750 360 258 PHE CA C 60.27 0.2 1 751 360 258 PHE CB C 38.96 0.2 1 752 360 258 PHE N N 121.252 0.2 1 753 361 259 GLN H H 8.677 0.01 1 754 361 259 GLN CA C 58.06 0.2 1 755 361 259 GLN CB C 27.43 0.2 1 756 361 259 GLN N N 119.683 0.2 1 757 362 260 ALA H H 7.505 0.01 1 758 362 260 ALA CA C 53.89 0.2 1 759 362 260 ALA CB C 17.59 0.2 1 760 362 260 ALA N N 121.288 0.2 1 761 363 261 THR H H 7.511 0.01 1 762 363 261 THR CA C 62.75 0.2 1 763 363 261 THR CB C 69.79 0.2 1 764 363 261 THR N N 109.899 0.2 1 765 364 262 GLN H H 7.444 0.01 1 766 364 262 GLN CA C 55.32 0.2 1 767 364 262 GLN CB C 28.60 0.2 1 768 364 262 GLN N N 120.990 0.2 1 769 365 263 GLN H H 7.888 0.01 1 770 365 263 GLN CA C 55.58 0.2 1 771 365 263 GLN CB C 28.60 0.2 1 772 365 263 GLN N N 121.557 0.2 1 773 366 264 LYS H H 7.885 0.01 1 774 366 264 LYS CA C 57.40 0.2 1 775 366 264 LYS CB C 32.84 0.2 1 776 366 264 LYS N N 128.824 0.2 1 stop_ save_