data_17570 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Solid-state NMR assignment of the C-terminal domain of the Ure2p prion in its fibrillar form ; _BMRB_accession_number 17570 _BMRB_flat_file_name bmr17570.str _Entry_type original _Submission_date 2011-04-01 _Accession_date 2011-04-01 _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 Habenstein Birgit . . 2 Wasmer Christian . . 3 Bousset Luc . . 4 Sourigues Yannick . . 5 Loquet Antoine . . 6 Meier Beat H. . 7 Melki Ronald . . 8 Bockmann Anja . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "13C chemical shifts" 527 "15N chemical shifts" 167 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2012-06-19 original author . stop_ loop_ _Related_BMRB_accession_number _Relationship 17499 'C-terminal domain of Ure2p in microcrystals' stop_ _Original_release_date 2012-06-19 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title 'Extensive de novo solid-state NMR assignments of the 33 kDa C-terminal domain of the Ure2 prion.' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 21805376 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Habenstein Birgit . . 2 Wasmer Christian . . 3 Bousset Luc . . 4 Sourigues Yannick . . 5 Schutz Anne . . 6 Loquet Antoine . . 7 Meier Beat H. . 8 Melki Ronald . . 9 Bockmann Anja . . stop_ _Journal_abbreviation 'J. Biomol. NMR' _Journal_name_full 'Journal of biomolecular NMR' _Journal_volume 51 _Journal_issue 3 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 235 _Page_last 243 _Year 2011 _Details . save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name 'Ure2p prion' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label Ure2p $Ure2p stop_ _System_molecular_weight 40270.77 _System_physical_state native _System_oligomer_state ? _System_paramagnetic no _System_thiol_state . loop_ _Biological_function prion stop_ _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_Ure2p _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'Ure2p prion' _Molecular_mass 40270.77 _Mol_thiol_state 'not present' loop_ _Biological_function 'nitrogen-dependent repression of the ureidosuccinate utilization pathway' stop_ _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 354 _Mol_residue_sequence ; MMNNNGNQVSNLSNALRQVN IGNRNSNTTTDQSNINFEFS TGVNNNNNNNSSSNNNNVQN NNSGRNGSQNNDNENNIKNT LEQHRQQQQAFSDMSHVEYS RITKFFQEQPLEGYTLFSHR SAPNGFKVAIVLSELGFHYN TIFLDFNLGEHRAPEFVSVN PNARVPALIDHGMDNLSIWE SGAILLHLVNKYYKETGNPL LWSDDLADQSQINAWLFFQT SGHAPMIGQALHFRYFHSQK IASAVERYTDEVRRVYGVVE MALAERREALVMELDTENAA AYSAGTTPMSQSRFFDYPVW LVGDKLTIADLAFVPWNNVV DRIGINIKIEFPEVYKWTKH MMRRPAVIKALRGE ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 -112 MET 2 -111 MET 3 -110 ASN 4 -109 ASN 5 -108 ASN 6 -107 GLY 7 -106 ASN 8 -105 GLN 9 -104 VAL 10 -103 SER 11 -102 ASN 12 -101 LEU 13 -100 SER 14 -99 ASN 15 -98 ALA 16 -97 LEU 17 -96 ARG 18 -95 GLN 19 -94 VAL 20 -93 ASN 21 -92 ILE 22 -91 GLY 23 -90 ASN 24 -89 ARG 25 -88 ASN 26 -87 SER 27 -86 ASN 28 -85 THR 29 -84 THR 30 -83 THR 31 -82 ASP 32 -81 GLN 33 -80 SER 34 -79 ASN 35 -78 ILE 36 -77 ASN 37 -76 PHE 38 -75 GLU 39 -74 PHE 40 -73 SER 41 -72 THR 42 -71 GLY 43 -70 VAL 44 -69 ASN 45 -68 ASN 46 -67 ASN 47 -66 ASN 48 -65 ASN 49 -64 ASN 50 -63 ASN 51 -62 SER 52 -61 SER 53 -60 SER 54 -59 ASN 55 -58 ASN 56 -57 ASN 57 -56 ASN 58 -55 VAL 59 -54 GLN 60 -53 ASN 61 -52 ASN 62 -51 ASN 63 -50 SER 64 -49 GLY 65 -48 ARG 66 -47 ASN 67 -46 GLY 68 -45 SER 69 -44 GLN 70 -43 ASN 71 -42 ASN 72 -41 ASP 73 -40 ASN 74 -39 GLU 75 -38 ASN 76 -37 ASN 77 -36 ILE 78 -35 LYS 79 -34 ASN 80 -33 THR 81 -32 LEU 82 -31 GLU 83 -30 GLN 84 -29 HIS 85 -28 ARG 86 -27 GLN 87 -26 GLN 88 -25 GLN 89 -24 GLN 90 -23 ALA 91 -22 PHE 92 -21 SER 93 -20 ASP 94 -19 MET 95 -18 SER 96 -17 HIS 97 -16 VAL 98 -15 GLU 99 -14 TYR 100 -13 SER 101 -12 ARG 102 -11 ILE 103 -10 THR 104 -9 LYS 105 -8 PHE 106 -7 PHE 107 -6 GLN 108 -5 GLU 109 -4 GLN 110 -3 PRO 111 -2 LEU 112 -1 GLU 113 0 GLY 114 1 TYR 115 2 THR 116 3 LEU 117 4 PHE 118 5 SER 119 6 HIS 120 7 ARG 121 8 SER 122 9 ALA 123 10 PRO 124 11 ASN 125 12 GLY 126 13 PHE 127 14 LYS 128 15 VAL 129 16 ALA 130 17 ILE 131 18 VAL 132 19 LEU 133 20 SER 134 21 GLU 135 22 LEU 136 23 GLY 137 24 PHE 138 25 HIS 139 26 TYR 140 27 ASN 141 28 THR 142 29 ILE 143 30 PHE 144 31 LEU 145 32 ASP 146 33 PHE 147 34 ASN 148 35 LEU 149 36 GLY 150 37 GLU 151 38 HIS 152 39 ARG 153 40 ALA 154 41 PRO 155 42 GLU 156 43 PHE 157 44 VAL 158 45 SER 159 46 VAL 160 47 ASN 161 48 PRO 162 49 ASN 163 50 ALA 164 51 ARG 165 52 VAL 166 53 PRO 167 54 ALA 168 55 LEU 169 56 ILE 170 57 ASP 171 58 HIS 172 59 GLY 173 60 MET 174 61 ASP 175 62 ASN 176 63 LEU 177 64 SER 178 65 ILE 179 66 TRP 180 67 GLU 181 68 SER 182 69 GLY 183 70 ALA 184 71 ILE 185 72 LEU 186 73 LEU 187 74 HIS 188 75 LEU 189 76 VAL 190 77 ASN 191 78 LYS 192 79 TYR 193 80 TYR 194 81 LYS 195 82 GLU 196 83 THR 197 84 GLY 198 85 ASN 199 86 PRO 200 87 LEU 201 88 LEU 202 89 TRP 203 90 SER 204 91 ASP 205 92 ASP 206 93 LEU 207 94 ALA 208 95 ASP 209 96 GLN 210 97 SER 211 98 GLN 212 99 ILE 213 100 ASN 214 101 ALA 215 102 TRP 216 103 LEU 217 104 PHE 218 105 PHE 219 106 GLN 220 107 THR 221 108 SER 222 109 GLY 223 110 HIS 224 111 ALA 225 112 PRO 226 113 MET 227 114 ILE 228 115 GLY 229 116 GLN 230 117 ALA 231 118 LEU 232 119 HIS 233 120 PHE 234 121 ARG 235 122 TYR 236 123 PHE 237 124 HIS 238 125 SER 239 126 GLN 240 127 LYS 241 128 ILE 242 129 ALA 243 130 SER 244 131 ALA 245 132 VAL 246 133 GLU 247 134 ARG 248 135 TYR 249 136 THR 250 137 ASP 251 138 GLU 252 139 VAL 253 140 ARG 254 141 ARG 255 142 VAL 256 143 TYR 257 144 GLY 258 145 VAL 259 146 VAL 260 147 GLU 261 148 MET 262 149 ALA 263 150 LEU 264 151 ALA 265 152 GLU 266 153 ARG 267 154 ARG 268 155 GLU 269 156 ALA 270 157 LEU 271 158 VAL 272 159 MET 273 160 GLU 274 161 LEU 275 162 ASP 276 163 THR 277 164 GLU 278 165 ASN 279 166 ALA 280 167 ALA 281 168 ALA 282 169 TYR 283 170 SER 284 171 ALA 285 172 GLY 286 173 THR 287 174 THR 288 175 PRO 289 176 MET 290 177 SER 291 178 GLN 292 179 SER 293 180 ARG 294 181 PHE 295 182 PHE 296 183 ASP 297 184 TYR 298 185 PRO 299 186 VAL 300 187 TRP 301 188 LEU 302 189 VAL 303 190 GLY 304 191 ASP 305 192 LYS 306 193 LEU 307 194 THR 308 195 ILE 309 196 ALA 310 197 ASP 311 198 LEU 312 199 ALA 313 200 PHE 314 201 VAL 315 202 PRO 316 203 TRP 317 204 ASN 318 205 ASN 319 206 VAL 320 207 VAL 321 208 ASP 322 209 ARG 323 210 ILE 324 211 GLY 325 212 ILE 326 213 ASN 327 214 ILE 328 215 LYS 329 216 ILE 330 217 GLU 331 218 PHE 332 219 PRO 333 220 GLU 334 221 VAL 335 222 TYR 336 223 LYS 337 224 TRP 338 225 THR 339 226 LYS 340 227 HIS 341 228 MET 342 229 MET 343 230 ARG 344 231 ARG 345 232 PRO 346 233 ALA 347 234 VAL 348 235 ILE 349 236 LYS 350 237 ALA 351 238 LEU 352 239 ARG 353 240 GLY 354 241 GLU stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-10-14 loop_ _Database_name _Database_accession_code _Database_entry_mol_name _Sequence_query_to_submitted_percentage _Sequence_subject_length _Sequence_identity _Sequence_positive _Sequence_homology_expectation_value BMRB 17499 Ure2p70-354 80.51 295 100.00 100.00 0.00e+00 PDB 1G6W "Crystal Structure Of The Globular Region Of The Prion Protein Ure2 From The Yeast Saccaromyces Cerevisiae" 73.73 261 100.00 100.00 0.00e+00 PDB 1G6Y "Crystal Structure Of The Globular Region Of The Prion Protien Ure2 From Yeast Saccharomyces Cerevisiae" 73.73 261 100.00 100.00 0.00e+00 PDB 1HQO "Crystal Structure Of The Nitrogen Regulation Fragment Of The Yeast Prion Protein Ure2p" 72.88 258 97.29 97.29 0.00e+00 PDB 1JZR "Ure2p In Complex With Glutathione" 73.45 260 100.00 100.00 0.00e+00 PDB 1K0A "Ure2p In Complex With S-Hexylglutathione" 73.45 260 100.00 100.00 0.00e+00 PDB 1K0B "Ure2p In Complex With Glutathione" 73.45 260 100.00 100.00 0.00e+00 PDB 1K0C "Ure2p In Complex With S-P-Nitrobenzylglutathione" 73.45 260 100.00 100.00 0.00e+00 PDB 1K0D "Ure2p In Complex With Glutathione" 73.45 260 100.00 100.00 0.00e+00 DBJ GAA25878 "K7_Ure2p [Saccharomyces cerevisiae Kyokai no. 7]" 100.00 354 100.00 100.00 0.00e+00 EMBL CAA93369 "N1165 [Saccharomyces cerevisiae]" 100.00 354 100.00 100.00 0.00e+00 EMBL CAA96134 "URE2 [Saccharomyces cerevisiae]" 100.00 354 100.00 100.00 0.00e+00 EMBL CAY82378 "Ure2p [Saccharomyces cerevisiae EC1118]" 100.00 354 100.00 100.00 0.00e+00 GB AAA35201 "glutathione transferase-like protein [Saccharomyces cerevisiae]" 100.00 354 100.00 100.00 0.00e+00 GB AAK51641 "Ure2p [Saccharomyces douglasii]" 101.41 359 96.94 97.77 0.00e+00 GB AAM91938 "Ure2p [Saccharomyces paradoxus]" 101.41 359 96.94 97.77 0.00e+00 GB AAM93167 "Ure2p [Saccharomyces cerevisiae]" 100.00 354 100.00 100.00 0.00e+00 GB AAM93168 "Ure2p [Saccharomyces cerevisiae]" 100.00 354 100.00 100.00 0.00e+00 REF NP_014170 "Ure2p [Saccharomyces cerevisiae S288c]" 100.00 354 100.00 100.00 0.00e+00 SP P23202 "RecName: Full=Transcriptional regulator URE2; AltName: Full=Disulfide reductase; AltName: Full=Glutathione peroxidase" 100.00 354 100.00 100.00 0.00e+00 SP Q7LLZ8 "RecName: Full=Protein URE2" 101.41 359 96.94 97.77 0.00e+00 TPG DAA10329 "TPA: Ure2p [Saccharomyces cerevisiae S288c]" 100.00 354 100.00 100.00 0.00e+00 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $Ure2p 'baker's yeast' 4932 Eukaryota Metazoa Saccharomyces cerevisiae stop_ save_ ######################### # Experimental source # ######################### save_experimental_source _Saveframe_category experimental_source loop_ _Mol_label _Production_method _Host_organism_name_common _Genus _Species _Strain _Variant _Vector_name $Ure2p 'recombinant technology' . Escherichia coli BL21 DE3 'pET 3A' stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Saveframe_category sample _Sample_type fiber _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $Ure2p 10-30 mg '[U-100% 13C; U-100% 15N]' KCl 75 mM 'natural abundance' TRIS 20 mM 'natural abundance' EGTA 1 mM 'natural abundance' dithiothreitol 1 mM 'natural abundance' DSS 0.5 mg 'natural abundance' H2O 100 % 'natural abundance' stop_ save_ ############################ # Computer software used # ############################ save_CCPNmr_Analysis _Saveframe_category software _Name ANALYSIS _Version 2.1.1 loop_ _Vendor _Address _Electronic_address CCPN . . stop_ loop_ _Task 'chemical shift assignment' stop_ _Details . save_ save_TOPSPIN _Saveframe_category software _Name TOPSPIN _Version . loop_ _Vendor _Address _Electronic_address 'Bruker Biospin' . . stop_ loop_ _Task processing stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model Avance _Field_strength 850 _Details . save_ ############################# # NMR applied experiments # ############################# save_3D_NCACB_(DREAM)_1 _Saveframe_category NMR_applied_experiment _Experiment_name '3D NCACB (DREAM)' _Sample_label $sample_1 save_ save_3D_CCC_2 _Saveframe_category NMR_applied_experiment _Experiment_name '3D CCC' _Sample_label $sample_1 save_ save_3D_CAN(CO)CA_3 _Saveframe_category NMR_applied_experiment _Experiment_name '3D CAN(CO)CA' _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 pH 7.5 . pH pressure 1 . atm temperature 273 . K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference_1 _Saveframe_category chemical_shift_reference _Details . loop_ _Mol_common_name _Atom_type _Atom_isotope_number _Atom_group _Chem_shift_units _Chem_shift_value _Reference_method _Reference_type _External_reference_sample_geometry _External_reference_location _External_reference_axis _Indirect_shift_ratio DSS C 13 'methyl protons' ppm 0.00 na indirect . . . 0.251449530 DSS N 15 'methyl protons' ppm 0.00 na indirect . . . 0.101329118 stop_ save_ ################################### # Assigned chemical shift lists # ################################### ################################################################### # Chemical Shift Ambiguity Index Value Definitions # # # # The values other than 1 are used for those atoms with different # # chemical shifts that cannot be assigned to stereospecific atoms # # or to specific residues or chains. # # # # Index Value Definition # # # # 1 Unique (including isolated methyl protons, # # geminal atoms, and geminal methyl # # groups with identical chemical shifts) # # (e.g. ILE HD11, HD12, HD13 protons) # # 2 Ambiguity of geminal atoms or geminal methyl # # proton groups (e.g. ASP HB2 and HB3 # # protons, LEU CD1 and CD2 carbons, or # # LEU HD11, HD12, HD13 and HD21, HD22, # # HD23 methyl protons) # # 3 Aromatic atoms on opposite sides of # # symmetrical rings (e.g. TYR HE1 and HE2 # # protons) # # 4 Intraresidue ambiguities (e.g. LYS HG and # # HD protons or TRP HZ2 and HZ3 protons) # # 5 Interresidue ambiguities (LYS 12 vs. LYS 27) # # 6 Intermolecular ambiguities (e.g. ASP 31 CA # # in monomer 1 and ASP 31 CA in monomer 2 # # of an asymmetrical homodimer, duplex # # DNA assignments, or other assignments # # that may apply to atoms in one or more # # molecule in the molecular assembly) # # 9 Ambiguous, specific ambiguity not defined # # # ################################################################### save_assigned_chem_shift_list_1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Experiment_label '3D NCACB (DREAM)' '3D CCC' '3D CAN(CO)CA' 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 Ure2p _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 1 114 TYR CA C 57.354 0.15 1 2 1 114 TYR CB C 42.587 0.15 1 3 1 114 TYR N N 118.412 0.15 1 4 2 115 THR CA C 63.488 0.15 1 5 2 115 THR CB C 69.397 0.15 1 6 2 115 THR N N 120.040 0.15 1 7 3 116 LEU CA C 52.836 0.107 1 8 3 116 LEU CB C 44.725 0.078 1 9 3 116 LEU CG C 27.638 0.067 1 10 3 116 LEU CD1 C 25.285 0.15 2 11 3 116 LEU CD2 C 23.080 0.15 2 12 3 116 LEU N N 129.320 0.15 1 13 4 117 PHE CA C 57.428 0.055 1 14 4 117 PHE CB C 40.057 0.163 1 15 4 117 PHE CD1 C 131.180 0.15 3 16 4 117 PHE CD2 C 131.180 0.15 3 17 4 117 PHE N N 125.318 0.15 1 18 5 118 SER CA C 53.952 0.15 1 19 5 118 SER CB C 64.582 0.028 1 20 10 123 PRO CA C 65.302 0.15 1 21 10 123 PRO CB C 31.651 0.15 1 22 10 123 PRO CG C 27.720 0.041 1 23 10 123 PRO CD C 50.521 0.15 1 24 12 125 GLY CA C 47.175 0.003 1 25 12 125 GLY N N 106.840 0.15 1 26 13 126 PHE CA C 56.853 0.15 1 27 13 126 PHE CB C 40.053 0.15 1 28 13 126 PHE N N 121.981 0.15 1 29 14 127 LYS CA C 59.746 0.007 1 30 14 127 LYS CB C 32.775 0.047 1 31 14 127 LYS CG C 24.604 0.15 1 32 14 127 LYS CD C 29.738 0.15 1 33 14 127 LYS N N 116.565 0.15 1 34 15 128 VAL CA C 66.101 0.103 1 35 15 128 VAL CB C 31.306 0.074 1 36 15 128 VAL CG1 C 22.509 0.15 2 37 15 128 VAL CG2 C 24.243 0.15 2 38 15 128 VAL N N 114.686 0.037 1 39 16 129 ALA CA C 55.673 0.15 1 40 16 129 ALA CB C 18.218 0.15 1 41 16 129 ALA N N 122.089 0.15 1 42 17 130 ILE CA C 65.783 0.15 1 43 17 130 ILE CB C 37.938 0.15 1 44 17 130 ILE N N 117.082 0.15 1 45 18 131 VAL CA C 67.746 0.024 1 46 18 131 VAL CB C 31.260 0.010 1 47 18 131 VAL CG1 C 21.393 0.074 2 48 18 131 VAL CG2 C 22.894 0.167 2 49 18 131 VAL N N 119.178 0.192 1 50 19 132 LEU CA C 59.064 0.042 1 51 19 132 LEU CB C 42.849 0.087 1 52 19 132 LEU CG C 25.579 0.060 1 53 19 132 LEU N N 119.346 0.15 1 54 21 134 GLU CA C 59.447 0.052 1 55 21 134 GLU CB C 31.048 0.002 1 56 21 134 GLU CG C 35.432 0.15 1 57 21 134 GLU N N 123.170 0.15 1 58 22 135 LEU CA C 54.911 0.086 1 59 22 135 LEU CB C 40.761 0.028 1 60 22 135 LEU CG C 27.727 0.15 1 61 22 135 LEU CD2 C 25.868 0.055 1 62 22 135 LEU N N 115.641 0.15 1 63 23 136 GLY CA C 45.798 0.009 1 64 23 136 GLY N N 106.093 0.15 1 65 24 137 PHE CA C 54.455 0.15 1 66 24 137 PHE CB C 39.204 0.15 1 67 24 137 PHE N N 119.063 0.15 1 68 26 139 TYR CA C 54.972 0.15 1 69 26 139 TYR CB C 41.875 0.15 1 70 26 139 TYR N N 120.184 0.15 1 71 27 140 ASN CA C 51.768 0.15 1 72 27 140 ASN CB C 42.109 0.15 1 73 27 140 ASN N N 117.306 0.15 1 74 28 141 THR CA C 61.663 0.15 1 75 28 141 THR CB C 69.347 0.15 1 76 28 141 THR N N 119.301 0.15 1 77 29 142 ILE CA C 60.092 0.104 1 78 29 142 ILE CB C 38.336 0.087 1 79 29 142 ILE CG1 C 26.929 0.15 1 80 29 142 ILE N N 128.104 0.15 1 81 30 143 PHE CA C 56.783 0.15 1 82 30 143 PHE CB C 37.768 0.15 1 83 30 143 PHE N N 127.766 0.15 1 84 32 145 ASP CA C 55.379 0.129 1 85 32 145 ASP CB C 36.811 0.092 1 86 32 145 ASP CG C 178.398 0.15 1 87 32 145 ASP N N 120.092 0.15 1 88 33 146 PHE CA C 54.493 0.15 1 89 33 146 PHE CB C 38.983 0.15 1 90 33 146 PHE N N 113.776 0.15 1 91 34 147 ASN CA C 54.712 0.15 1 92 34 147 ASN CB C 36.804 0.15 1 93 34 147 ASN N N 110.870 0.15 1 94 40 153 ALA CA C 50.280 0.038 1 95 40 153 ALA CB C 17.555 0.15 1 96 44 157 VAL CA C 64.711 0.15 1 97 44 157 VAL CB C 31.350 0.15 1 98 44 157 VAL CG2 C 21.473 0.15 1 99 45 158 SER CA C 61.460 0.15 1 100 45 158 SER CB C 63.171 0.15 1 101 45 158 SER N N 111.625 0.15 1 102 50 163 ALA CA C 53.341 0.042 1 103 50 163 ALA CB C 17.490 0.15 1 104 51 164 ARG CA C 53.794 0.15 1 105 51 164 ARG CB C 32.911 0.15 1 106 51 164 ARG N N 113.236 0.15 1 107 52 165 VAL CA C 65.060 0.15 1 108 52 165 VAL CB C 30.975 0.15 1 109 52 165 VAL N N 107.633 0.15 1 110 53 166 PRO CA C 61.575 0.15 1 111 53 166 PRO CG C 23.858 0.15 1 112 53 166 PRO CD C 50.203 0.15 1 113 54 167 ALA CA C 51.807 0.15 1 114 54 167 ALA CB C 22.266 0.15 1 115 54 167 ALA N N 116.182 0.15 1 116 55 168 LEU CA C 52.617 0.166 1 117 55 168 LEU CB C 47.768 0.093 1 118 55 168 LEU CG C 27.264 0.15 1 119 55 168 LEU CD2 C 26.638 0.042 1 120 55 168 LEU N N 124.184 0.15 1 121 56 169 ILE CA C 59.194 0.128 1 122 56 169 ILE CB C 42.326 0.001 1 123 56 169 ILE CG1 C 25.832 0.15 1 124 56 169 ILE N N 123.468 0.15 1 125 57 170 ASP C C 176.515 0.15 1 126 57 170 ASP CA C 51.761 0.196 1 127 57 170 ASP CB C 41.007 0.089 1 128 57 170 ASP CG C 179.243 0.099 1 129 57 170 ASP N N 126.009 0.15 1 130 58 171 HIS CA C 59.354 0.008 1 131 58 171 HIS CB C 27.833 0.110 1 132 58 171 HIS CG C 129.513 0.15 1 133 58 171 HIS CD2 C 127.986 0.15 1 134 58 171 HIS N N 122.522 0.15 1 135 59 172 GLY CA C 46.038 0.029 1 136 59 172 GLY N N 106.093 0.15 1 137 60 173 MET CA C 54.427 0.096 1 138 60 173 MET CB C 31.918 0.003 1 139 60 173 MET CG C 32.727 0.15 1 140 60 173 MET N N 122.104 0.15 1 141 61 174 ASP CA C 55.263 0.15 1 142 61 174 ASP CB C 39.095 0.15 1 143 61 174 ASP N N 117.576 0.15 1 144 62 175 ASN CA C 54.571 0.053 1 145 62 175 ASN CB C 36.290 0.077 1 146 62 175 ASN CG C 178.048 0.15 1 147 62 175 ASN N N 109.924 0.15 1 148 63 176 LEU CA C 55.732 0.067 1 149 63 176 LEU CB C 44.161 0.050 1 150 63 176 LEU CG C 26.940 0.032 1 151 63 176 LEU CD2 C 22.789 0.15 1 152 63 176 LEU N N 121.781 0.014 1 153 64 177 SER CA C 55.791 0.15 1 154 64 177 SER CB C 64.588 0.15 1 155 64 177 SER N N 121.074 0.15 1 156 65 178 ILE CA C 62.553 0.15 1 157 65 178 ILE CB C 40.490 0.15 1 158 65 178 ILE N N 124.374 0.15 1 159 69 182 GLY CA C 46.448 0.023 1 160 69 182 GLY N N 110.731 0.15 1 161 70 183 ALA CA C 53.947 0.15 1 162 70 183 ALA CB C 17.819 0.15 1 163 70 183 ALA N N 120.152 0.15 1 164 71 184 ILE CA C 66.012 0.080 1 165 71 184 ILE CB C 36.998 0.138 1 166 71 184 ILE CG1 C 28.698 0.107 1 167 71 184 ILE CG2 C 21.146 0.057 1 168 71 184 ILE CD1 C 14.359 0.153 1 169 71 184 ILE N N 120.101 0.15 1 170 72 185 LEU CA C 59.911 0.15 1 171 72 185 LEU CB C 40.556 0.15 1 172 72 185 LEU N N 119.088 0.15 1 173 73 186 LEU CA C 57.283 0.141 1 174 73 186 LEU CB C 41.843 0.133 1 175 73 186 LEU CG C 27.383 0.048 1 176 73 186 LEU CD2 C 25.552 0.15 1 177 73 186 LEU N N 114.427 0.15 1 178 74 187 HIS C C 176.422 0.15 1 179 74 187 HIS CA C 60.580 0.159 1 180 74 187 HIS CB C 31.598 0.188 1 181 74 187 HIS CG C 137.082 0.15 1 182 74 187 HIS CD2 C 115.129 0.15 1 183 74 187 HIS CE1 C 138.589 0.006 1 184 74 187 HIS N N 122.252 0.15 1 185 75 188 LEU CA C 57.936 0.082 1 186 75 188 LEU CB C 41.512 0.088 1 187 75 188 LEU CG C 25.799 0.090 1 188 75 188 LEU CD1 C 19.693 0.15 2 189 75 188 LEU CD2 C 21.811 0.15 2 190 75 188 LEU N N 115.549 0.15 1 191 76 189 VAL CA C 65.391 0.077 1 192 76 189 VAL CB C 30.707 0.086 1 193 76 189 VAL CG2 C 24.118 0.027 1 194 76 189 VAL N N 108.667 0.15 1 195 77 190 ASN CA C 56.993 0.009 1 196 77 190 ASN CB C 39.882 0.150 1 197 77 190 ASN CG C 178.346 0.15 1 198 77 190 ASN N N 121.035 0.15 1 199 78 191 LYS CA C 59.439 0.118 1 200 78 191 LYS CB C 32.277 0.052 1 201 78 191 LYS CG C 24.880 0.15 1 202 78 191 LYS CD C 29.288 0.15 1 203 78 191 LYS CE C 41.749 0.15 1 204 78 191 LYS N N 119.548 0.15 1 205 82 195 GLU CA C 58.970 0.040 1 206 82 195 GLU CB C 30.502 0.095 1 207 82 195 GLU CG C 36.397 0.15 1 208 82 195 GLU N N 119.593 0.15 1 209 83 196 THR CA C 62.602 0.131 1 210 83 196 THR CB C 72.467 0.013 1 211 83 196 THR CG2 C 19.613 0.15 1 212 83 196 THR N N 105.496 0.15 1 213 84 197 GLY CA C 45.631 0.005 1 214 84 197 GLY N N 112.446 0.15 1 215 85 198 ASN CA C 49.063 0.022 1 216 85 198 ASN CB C 40.638 0.043 1 217 85 198 ASN N N 119.739 0.15 1 218 86 199 PRO CA C 61.351 0.15 1 219 86 199 PRO CB C 31.981 0.15 1 220 86 199 PRO CG C 27.503 0.129 1 221 86 199 PRO CD C 50.401 0.15 1 222 87 200 LEU CA C 56.817 0.042 1 223 87 200 LEU CB C 43.200 0.121 1 224 87 200 LEU CG C 26.750 0.046 1 225 87 200 LEU CD1 C 23.082 0.043 2 226 87 200 LEU CD2 C 24.768 0.15 2 227 87 200 LEU N N 129.523 0.15 1 228 88 201 LEU CA C 56.301 0.039 1 229 88 201 LEU CB C 40.922 0.051 1 230 88 201 LEU CG C 26.867 0.180 1 231 88 201 LEU CD2 C 22.672 0.027 1 232 88 201 LEU N N 114.805 0.15 1 233 89 202 TRP CA C 53.573 0.15 1 234 89 202 TRP CB C 34.138 0.15 1 235 89 202 TRP N N 122.643 0.15 1 236 90 203 SER CA C 57.664 0.15 1 237 90 203 SER CB C 63.626 0.15 1 238 90 203 SER N N 113.394 0.15 1 239 91 204 ASP CA C 53.044 0.174 1 240 91 204 ASP CB C 40.294 0.163 1 241 91 204 ASP CG C 180.076 0.15 1 242 91 204 ASP N N 121.709 0.15 1 243 92 205 ASP CA C 52.981 0.15 1 244 92 205 ASP CB C 44.012 0.15 1 245 92 205 ASP N N 122.829 0.15 1 246 93 206 LEU CA C 58.506 0.026 1 247 93 206 LEU CB C 41.964 0.017 1 248 93 206 LEU CG C 27.131 0.133 1 249 93 206 LEU N N 128.137 0.304 1 250 94 207 ALA CA C 55.804 0.15 1 251 94 207 ALA CB C 18.597 0.15 1 252 94 207 ALA N N 119.966 0.15 1 253 95 208 ASP CA C 57.354 0.15 1 254 95 208 ASP CB C 39.726 0.15 1 255 95 208 ASP N N 118.614 0.15 1 256 96 209 GLN CA C 59.960 0.039 1 257 96 209 GLN CB C 27.295 0.128 1 258 96 209 GLN CG C 32.934 0.023 1 259 96 209 GLN N N 118.581 0.034 1 260 97 210 SER CA C 61.249 0.091 1 261 97 210 SER CB C 62.852 0.015 1 262 97 210 SER N N 116.864 0.15 1 263 98 211 GLN CA C 58.744 0.15 1 264 98 211 GLN CB C 29.760 0.15 1 265 98 211 GLN N N 121.808 0.15 1 266 99 212 ILE CA C 66.399 0.129 1 267 99 212 ILE CB C 38.676 0.098 1 268 99 212 ILE CG1 C 29.692 0.15 1 269 99 212 ILE CG2 C 17.531 0.100 1 270 99 212 ILE CD1 C 15.131 0.15 1 271 99 212 ILE N N 120.642 0.15 1 272 100 213 ASN C C 174.189 0.15 1 273 100 213 ASN CA C 55.435 0.106 1 274 100 213 ASN CB C 36.731 0.061 1 275 100 213 ASN CG C 178.134 0.15 1 276 100 213 ASN N N 117.060 0.15 1 277 101 214 ALA CA C 56.504 0.15 1 278 101 214 ALA CB C 15.838 0.15 1 279 101 214 ALA N N 126.237 0.15 1 280 102 215 TRP C C 177.883 0.15 1 281 102 215 TRP CA C 61.039 0.079 1 282 102 215 TRP CB C 31.495 0.003 1 283 102 215 TRP N N 116.169 0.15 1 284 103 216 LEU CA C 58.412 0.146 1 285 103 216 LEU CB C 43.485 0.116 1 286 103 216 LEU CG C 27.127 0.040 1 287 103 216 LEU CD1 C 24.065 0.15 2 288 103 216 LEU CD2 C 26.289 0.15 2 289 103 216 LEU N N 121.441 0.15 1 290 109 222 GLY CA C 44.785 0.005 1 291 109 222 GLY N N 110.135 0.15 1 292 110 223 HIS CA C 58.186 0.15 1 293 110 223 HIS CB C 29.744 0.15 1 294 110 223 HIS N N 120.157 0.15 1 295 111 224 ALA CA C 56.328 0.15 1 296 111 224 ALA CB C 15.932 0.15 1 297 111 224 ALA N N 121.183 0.15 1 298 112 225 PRO CA C 65.662 0.060 1 299 112 225 PRO CB C 30.922 0.046 1 300 112 225 PRO CG C 29.744 0.095 1 301 112 225 PRO CD C 51.123 0.027 1 302 113 226 MET CA C 56.951 0.185 1 303 113 226 MET CB C 33.218 0.004 1 304 113 226 MET CG C 34.479 0.15 1 305 113 226 MET N N 113.060 0.15 1 306 114 227 ILE CA C 66.316 0.170 1 307 114 227 ILE CB C 37.803 0.074 1 308 114 227 ILE CG1 C 30.880 0.15 1 309 114 227 ILE CG2 C 17.792 0.120 1 310 114 227 ILE CD1 C 14.263 0.15 1 311 114 227 ILE N N 121.441 0.15 1 312 115 228 GLY CA C 47.516 0.041 1 313 115 228 GLY N N 104.289 0.15 1 314 116 229 GLN CA C 56.860 0.059 1 315 116 229 GLN CB C 24.100 0.119 1 316 116 229 GLN CG C 32.068 0.15 1 317 116 229 GLN N N 119.819 0.15 1 318 117 230 ALA CA C 56.634 0.15 1 319 117 230 ALA CB C 19.004 0.15 1 320 117 230 ALA N N 122.156 0.15 1 321 118 231 LEU CA C 58.318 0.048 1 322 118 231 LEU CB C 42.973 0.007 1 323 118 231 LEU CG C 27.146 0.025 1 324 118 231 LEU N N 116.400 0.163 1 325 119 232 HIS CA C 61.571 0.15 1 326 119 232 HIS CB C 30.924 0.15 1 327 119 232 HIS N N 117.115 0.15 1 328 125 238 SER CA C 60.975 0.049 1 329 125 238 SER CB C 62.729 0.064 1 330 125 238 SER N N 118.784 0.15 1 331 126 239 GLN CA C 54.258 0.15 1 332 126 239 GLN CB C 32.478 0.15 1 333 126 239 GLN N N 116.968 0.15 1 334 127 240 LYS CA C 56.006 0.035 1 335 127 240 LYS CB C 31.557 0.047 1 336 127 240 LYS CG C 24.368 0.15 1 337 127 240 LYS CD C 28.904 0.15 1 338 127 240 LYS N N 125.118 0.15 1 339 128 241 ILE CA C 59.716 0.036 1 340 128 241 ILE CB C 38.099 0.101 1 341 128 241 ILE CG1 C 26.226 0.15 1 342 128 241 ILE CG2 C 19.268 0.040 1 343 128 241 ILE CD1 C 14.739 0.15 1 344 128 241 ILE N N 129.928 0.15 1 345 129 242 ALA CA C 56.356 0.15 1 346 129 242 ALA CB C 18.093 0.15 1 347 129 242 ALA N N 132.970 0.15 1 348 131 244 ALA CA C 54.923 0.15 1 349 131 244 ALA CB C 17.359 0.15 1 350 131 244 ALA N N 126.844 0.15 1 351 132 245 VAL CA C 68.251 0.126 1 352 132 245 VAL CB C 32.152 0.027 1 353 132 245 VAL CG1 C 22.808 0.15 2 354 132 245 VAL CG2 C 21.887 0.023 2 355 132 245 VAL N N 117.086 0.15 1 356 133 246 GLU CA C 58.976 0.025 1 357 133 246 GLU CB C 29.789 0.130 1 358 133 246 GLU CD C 183.781 0.15 1 359 133 246 GLU N N 118.670 0.15 1 360 134 247 ARG CA C 58.883 0.114 1 361 134 247 ARG CB C 28.957 0.023 1 362 134 247 ARG CG C 25.968 0.002 1 363 134 247 ARG N N 117.521 0.15 1 364 135 248 TYR C C 179.159 0.15 1 365 135 248 TYR CA C 63.441 0.142 1 366 135 248 TYR CB C 38.497 0.162 1 367 135 248 TYR CE2 C 119.954 0.15 3 368 135 248 TYR N N 114.719 0.15 1 369 137 250 ASP C C 177.902 0.15 1 370 137 250 ASP CA C 57.573 0.042 1 371 137 250 ASP CB C 39.679 0.028 1 372 137 250 ASP CG C 179.573 0.15 1 373 137 250 ASP N N 121.964 0.15 1 374 138 251 GLU CA C 57.950 0.097 1 375 138 251 GLU CB C 29.668 0.091 1 376 138 251 GLU CG C 34.661 0.15 1 377 138 251 GLU CD C 180.637 0.15 1 378 138 251 GLU N N 120.427 0.15 1 379 139 252 VAL CA C 67.734 0.037 1 380 139 252 VAL CB C 31.401 0.077 1 381 139 252 VAL CG1 C 21.485 0.047 2 382 139 252 VAL CG2 C 24.142 0.098 2 383 139 252 VAL N N 119.981 0.15 1 384 140 253 ARG CA C 62.183 0.15 1 385 140 253 ARG CB C 30.291 0.15 1 386 140 253 ARG N N 118.602 0.15 1 387 141 254 ARG CA C 60.456 0.15 1 388 141 254 ARG CB C 29.854 0.15 1 389 141 254 ARG N N 123.834 0.15 1 390 143 256 TYR CA C 63.761 0.15 1 391 143 256 TYR CB C 35.639 0.15 1 392 143 256 TYR N N 118.411 0.15 1 393 144 257 GLY CA C 47.504 0.003 1 394 144 257 GLY N N 107.400 0.15 1 395 145 258 VAL CA C 66.504 0.018 1 396 145 258 VAL CB C 31.759 0.148 1 397 145 258 VAL CG1 C 21.116 0.031 2 398 145 258 VAL CG2 C 22.380 0.113 2 399 145 258 VAL N N 123.333 0.15 1 400 146 259 VAL CA C 66.631 0.136 1 401 146 259 VAL CB C 31.842 0.034 1 402 146 259 VAL CG2 C 22.460 0.028 1 403 146 259 VAL N N 120.403 0.15 1 404 147 260 GLU CA C 59.675 0.15 1 405 147 260 GLU CB C 30.093 0.15 1 406 147 260 GLU N N 120.258 0.15 1 407 148 261 MET CA C 58.535 0.15 1 408 148 261 MET CB C 32.453 0.15 1 409 148 261 MET N N 116.304 0.15 1 410 149 262 ALA CA C 55.183 0.15 1 411 149 262 ALA CB C 18.466 0.15 1 412 149 262 ALA N N 123.373 0.15 1 413 150 263 LEU CA C 57.845 0.040 1 414 150 263 LEU CB C 41.851 0.107 1 415 150 263 LEU CG C 25.784 0.010 1 416 150 263 LEU N N 119.561 0.15 1 417 151 264 ALA CA C 55.476 0.15 1 418 151 264 ALA CB C 18.239 0.15 1 419 151 264 ALA N N 121.278 0.15 1 420 152 265 GLU CA C 59.365 0.062 1 421 152 265 GLU CB C 29.435 0.039 1 422 152 265 GLU CG C 36.438 0.15 1 423 152 265 GLU CD C 183.618 0.15 1 424 152 265 GLU N N 119.346 0.15 1 425 153 266 ARG CA C 58.365 0.100 1 426 153 266 ARG CB C 28.724 0.059 1 427 153 266 ARG CG C 26.796 0.15 1 428 153 266 ARG CD C 42.985 0.15 1 429 153 266 ARG N N 120.224 0.15 1 430 154 267 ARG CA C 58.219 0.063 1 431 154 267 ARG CB C 28.636 0.065 1 432 154 267 ARG CG C 26.038 0.145 1 433 154 267 ARG CD C 42.114 0.019 1 434 154 267 ARG N N 120.190 0.034 1 435 155 268 GLU CA C 59.698 0.060 1 436 155 268 GLU CB C 29.274 0.055 1 437 155 268 GLU CD C 183.395 0.15 1 438 155 268 GLU N N 118.872 0.15 1 439 156 269 ALA CA C 54.886 0.15 1 440 156 269 ALA CB C 18.269 0.15 1 441 156 269 ALA N N 117.939 0.15 1 442 157 270 LEU CA C 58.418 0.053 1 443 157 270 LEU CB C 42.229 0.050 1 444 157 270 LEU CG C 26.796 0.15 1 445 157 270 LEU CD2 C 25.608 0.062 1 446 157 270 LEU N N 120.233 0.035 1 447 158 271 VAL CA C 67.318 0.046 1 448 158 271 VAL CB C 31.719 0.077 1 449 158 271 VAL CG2 C 22.659 0.15 1 450 158 271 VAL N N 119.371 0.15 1 451 162 275 ASP CA C 50.811 0.15 1 452 162 275 ASP CB C 38.462 0.15 1 453 162 275 ASP N N 129.320 0.15 1 454 163 276 THR CA C 63.306 0.027 1 455 163 276 THR CB C 68.813 0.023 1 456 163 276 THR CG2 C 22.133 0.15 1 457 163 276 THR N N 112.064 0.15 1 458 164 277 GLU CA C 55.223 0.127 1 459 164 277 GLU CG C 39.107 0.012 1 460 164 277 GLU CD C 181.879 0.15 1 461 164 277 GLU N N 117.171 0.15 1 462 170 283 SER CA C 57.309 0.15 1 463 170 283 SER CB C 63.981 0.15 1 464 170 283 SER N N 111.477 0.15 1 465 171 284 ALA CA C 52.944 0.15 1 466 171 284 ALA CB C 19.532 0.15 1 467 171 284 ALA N N 120.940 0.15 1 468 172 285 GLY CA C 45.595 0.016 1 469 172 285 GLY N N 105.098 0.15 1 470 173 286 THR CA C 65.257 0.15 1 471 173 286 THR CB C 68.587 0.15 1 472 173 286 THR N N 112.729 0.15 1 473 174 287 THR CA C 59.688 0.15 1 474 174 287 THR CB C 72.927 0.013 1 475 174 287 THR CG2 C 21.975 0.15 1 476 174 287 THR N N 117.160 0.15 1 477 175 288 PRO CA C 62.462 0.044 1 478 175 288 PRO CB C 32.049 0.112 1 479 175 288 PRO CG C 27.158 0.026 1 480 175 288 PRO CD C 51.338 0.011 1 481 176 289 MET CA C 56.541 0.005 1 482 176 289 MET CB C 30.469 0.040 1 483 176 289 MET CG C 32.724 0.15 1 484 176 289 MET N N 113.533 0.15 1 485 177 290 SER CA C 61.410 0.15 1 486 177 290 SER CB C 62.968 0.15 1 487 177 290 SER N N 116.200 0.15 1 488 178 291 GLN CA C 59.709 0.039 1 489 178 291 GLN CB C 27.140 0.060 1 490 178 291 GLN CG C 32.864 0.15 1 491 178 291 GLN N N 117.871 0.15 1 492 179 292 SER C C 175.897 0.15 1 493 179 292 SER CA C 61.623 0.030 1 494 179 292 SER CB C 63.104 0.062 1 495 180 293 ARG CA C 57.814 0.15 1 496 180 293 ARG CB C 30.662 0.15 1 497 180 293 ARG N N 119.210 0.15 1 498 185 298 PRO CA C 65.273 0.15 1 499 185 298 PRO CB C 30.137 0.15 1 500 185 298 PRO CG C 26.961 0.089 1 501 185 298 PRO CD C 50.884 0.15 1 502 186 299 VAL CA C 59.706 0.193 1 503 186 299 VAL CB C 33.596 0.099 1 504 186 299 VAL CG2 C 24.417 0.15 1 505 186 299 VAL N N 117.156 0.15 1 506 187 300 TRP CA C 53.544 0.108 1 507 187 300 TRP CB C 35.071 0.090 1 508 187 300 TRP CG C 112.595 0.060 1 509 187 300 TRP N N 120.963 0.15 1 510 188 301 LEU CA C 59.308 0.100 1 511 188 301 LEU CB C 42.432 0.058 1 512 188 301 LEU CG C 26.016 0.060 1 513 188 301 LEU CD2 C 19.631 0.15 1 514 188 301 LEU N N 122.995 0.15 1 515 189 302 VAL CA C 61.814 0.032 1 516 189 302 VAL CB C 34.783 0.070 1 517 189 302 VAL CG2 C 21.174 0.006 1 518 189 302 VAL N N 119.493 0.15 1 519 190 303 GLY CA C 46.336 0.023 1 520 190 303 GLY N N 112.446 0.15 1 521 192 305 LYS CA C 54.603 0.15 1 522 192 305 LYS CB C 36.653 0.15 1 523 192 305 LYS N N 116.234 0.15 1 524 193 306 LEU CA C 55.170 0.15 1 525 193 306 LEU CB C 40.872 0.011 1 526 193 306 LEU CG C 25.840 0.15 1 527 193 306 LEU N N 115.398 0.15 1 528 194 307 THR CA C 60.411 0.078 1 529 194 307 THR CB C 76.363 0.051 1 530 194 307 THR CG2 C 21.412 0.038 1 531 194 307 THR N N 115.205 0.261 1 532 195 308 ILE CA C 65.980 0.042 1 533 195 308 ILE CB C 38.901 0.130 1 534 195 308 ILE CG1 C 25.161 0.15 1 535 195 308 ILE CG2 C 21.580 0.141 1 536 195 308 ILE CD1 C 15.454 0.060 1 537 195 308 ILE N N 110.477 0.037 1 538 196 309 ALA CA C 55.389 0.15 1 539 196 309 ALA CB C 19.361 0.15 1 540 196 309 ALA N N 119.994 0.15 1 541 197 310 ASP C C 178.434 0.15 1 542 197 310 ASP CA C 57.131 0.112 1 543 197 310 ASP CB C 43.884 0.002 1 544 197 310 ASP CG C 179.685 0.15 1 545 197 310 ASP N N 111.776 0.15 1 546 198 311 LEU CA C 56.904 0.048 1 547 198 311 LEU CB C 42.329 0.121 1 548 198 311 LEU CG C 26.179 0.067 1 549 198 311 LEU CD2 C 21.703 0.014 1 550 198 311 LEU N N 112.881 0.041 1 551 199 312 ALA CA C 54.646 0.15 1 552 199 312 ALA CB C 18.051 0.15 1 553 199 312 ALA N N 117.263 0.15 1 554 200 313 PHE CA C 60.762 0.15 1 555 200 313 PHE CB C 40.604 0.15 1 556 200 313 PHE N N 106.342 0.15 1 557 201 314 VAL CA C 69.243 0.127 1 558 201 314 VAL CB C 30.259 0.017 1 559 201 314 VAL CG2 C 26.298 0.15 1 560 201 314 VAL N N 117.894 0.15 1 561 203 316 TRP CA C 58.921 0.029 1 562 203 316 TRP CB C 30.668 0.115 1 563 203 316 TRP CG C 111.919 0.030 1 564 203 316 TRP N N 115.493 0.15 1 565 206 319 VAL CA C 61.320 0.085 1 566 206 319 VAL CB C 33.379 0.036 1 567 206 319 VAL CG1 C 20.039 0.15 2 568 206 319 VAL CG2 C 20.932 0.15 2 569 206 319 VAL N N 110.044 0.15 1 570 207 320 VAL CA C 65.678 0.037 1 571 207 320 VAL CB C 31.599 0.052 1 572 207 320 VAL CG1 C 22.976 0.15 2 573 207 320 VAL CG2 C 18.848 0.15 2 574 207 320 VAL N N 111.843 0.15 1 575 208 321 ASP CA C 56.569 0.098 1 576 208 321 ASP CB C 38.618 0.081 1 577 208 321 ASP CG C 179.950 0.15 1 578 208 321 ASP N N 123.631 0.15 1 579 209 322 ARG CA C 57.640 0.141 1 580 209 322 ARG CB C 30.598 0.075 1 581 209 322 ARG CG C 27.424 0.15 1 582 209 322 ARG CD C 43.574 0.15 1 583 209 322 ARG N N 119.814 0.15 1 584 210 323 ILE CA C 60.223 0.004 1 585 210 323 ILE CB C 37.150 0.117 1 586 210 323 ILE CG1 C 27.414 0.036 1 587 210 323 ILE CG2 C 18.243 0.060 1 588 210 323 ILE CD1 C 15.831 0.028 1 589 210 323 ILE N N 109.248 0.15 1 590 211 324 GLY CA C 46.189 0.003 1 591 211 324 GLY N N 108.146 0.15 1 592 212 325 ILE CA C 60.539 0.164 1 593 212 325 ILE CB C 38.567 0.057 1 594 212 325 ILE CG1 C 27.664 0.052 1 595 212 325 ILE CG2 C 15.117 0.15 1 596 212 325 ILE CD1 C 15.174 0.018 1 597 212 325 ILE N N 119.521 0.040 1 598 213 326 ASN CA C 50.606 0.151 1 599 213 326 ASN CB C 38.374 0.019 1 600 213 326 ASN CG C 176.754 0.15 1 601 213 326 ASN N N 128.374 0.15 1 602 214 327 ILE CA C 66.878 0.15 1 603 214 327 ILE CB C 37.935 0.15 1 604 214 327 ILE N N 122.657 0.15 1 605 215 328 LYS CA C 59.734 0.110 1 606 215 328 LYS CB C 32.792 0.083 1 607 215 328 LYS CG C 24.579 0.164 1 608 215 328 LYS CD C 29.581 0.160 1 609 215 328 LYS CE C 41.939 0.15 1 610 215 328 LYS N N 117.295 0.050 1 611 216 329 ILE CA C 60.893 0.123 1 612 216 329 ILE CB C 38.779 0.143 1 613 216 329 ILE CG1 C 27.733 0.029 1 614 216 329 ILE CG2 C 17.091 0.056 1 615 216 329 ILE CD1 C 15.135 0.15 1 616 216 329 ILE N N 111.163 0.064 1 617 217 330 GLU CA C 59.477 0.027 1 618 217 330 GLU CB C 33.652 0.041 1 619 217 330 GLU CG C 33.499 0.15 1 620 217 330 GLU N N 117.460 0.15 1 621 218 331 PHE CA C 55.267 0.155 1 622 218 331 PHE CB C 40.432 0.165 1 623 218 331 PHE CZ C 130.170 0.15 1 624 218 331 PHE N N 115.678 0.15 1 625 219 332 PRO CA C 65.934 0.057 1 626 219 332 PRO CB C 32.771 0.044 1 627 219 332 PRO CG C 27.649 0.036 1 628 219 332 PRO CD C 49.759 0.076 1 629 219 332 PRO N N 135.267 0.15 1 630 220 333 GLU CA C 59.599 0.069 1 631 220 333 GLU CB C 27.629 0.093 1 632 220 333 GLU CG C 35.952 0.15 1 633 220 333 GLU CD C 183.321 0.15 1 634 220 333 GLU N N 124.522 0.15 1 635 221 334 VAL CA C 65.981 0.075 1 636 221 334 VAL CB C 30.499 0.078 1 637 221 334 VAL CG1 C 21.774 0.102 2 638 221 334 VAL CG2 C 22.871 0.094 2 639 221 334 VAL N N 128.155 0.133 1 640 222 335 TYR CA C 62.447 0.144 1 641 222 335 TYR CB C 37.750 0.097 1 642 222 335 TYR CD1 C 132.539 0.15 3 643 222 335 TYR CD2 C 132.539 0.15 3 644 222 335 TYR CE1 C 118.263 0.114 3 645 222 335 TYR CE2 C 118.263 0.114 3 646 222 335 TYR N N 123.603 0.15 1 647 223 336 LYS CA C 60.589 0.044 1 648 223 336 LYS CB C 32.369 0.051 1 649 223 336 LYS CD C 29.566 0.115 1 650 223 336 LYS CE C 42.634 0.15 1 651 223 336 LYS N N 118.952 0.15 1 652 224 337 TRP CA C 59.171 0.15 1 653 224 337 TRP CB C 30.989 0.15 1 654 224 337 TRP N N 122.621 0.15 1 655 225 338 THR CA C 67.724 0.098 1 656 225 338 THR CB C 69.170 0.070 1 657 225 338 THR CG2 C 22.666 0.15 1 658 225 338 THR N N 114.058 0.15 1 659 226 339 LYS CA C 59.126 0.067 1 660 226 339 LYS CB C 30.655 0.082 1 661 226 339 LYS CG C 23.765 0.15 1 662 226 339 LYS CD C 27.633 0.15 1 663 226 339 LYS N N 121.735 0.15 1 664 231 344 ARG CA C 55.171 0.065 1 665 231 344 ARG CB C 29.475 0.081 1 666 231 344 ARG CD C 42.896 0.15 1 667 231 344 ARG N N 122.089 0.15 1 668 232 345 PRO CA C 65.601 0.040 1 669 232 345 PRO CB C 32.155 0.051 1 670 232 345 PRO CG C 27.701 0.027 1 671 232 345 PRO CD C 50.668 0.015 1 672 232 345 PRO N N 137.092 0.15 1 673 233 346 ALA CA C 55.061 0.15 1 674 233 346 ALA CB C 17.701 0.15 1 675 233 346 ALA N N 118.750 0.15 1 676 234 347 VAL CA C 66.191 0.056 1 677 234 347 VAL CB C 31.715 0.053 1 678 234 347 VAL CG1 C 22.508 0.042 2 679 234 347 VAL CG2 C 22.803 0.004 2 680 234 347 VAL N N 118.901 0.275 1 681 235 348 ILE CA C 65.110 0.016 1 682 235 348 ILE CB C 38.692 0.076 1 683 235 348 ILE CG1 C 29.532 0.156 1 684 235 348 ILE CG2 C 17.057 0.044 1 685 235 348 ILE CD1 C 14.102 0.071 1 686 235 348 ILE N N 118.344 0.15 1 687 236 349 LYS CA C 59.600 0.052 1 688 236 349 LYS CB C 32.959 0.007 1 689 236 349 LYS CG C 24.528 0.045 1 690 236 349 LYS CD C 29.875 0.016 1 691 236 349 LYS N N 117.304 0.15 1 692 237 350 ALA CA C 54.624 0.15 1 693 237 350 ALA CB C 19.397 0.15 1 694 237 350 ALA N N 121.210 0.15 1 stop_ save_