data_15974 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Chemical shifts of the b-b'-x region of human protein disulfide isomerase ; _BMRB_accession_number 15974 _BMRB_flat_file_name bmr15974.str _Entry_type original _Submission_date 2008-10-06 _Accession_date 2008-10-06 _Entry_origination author _NMR_STAR_version 2.1.1 _Experimental_method NMR _Details 'Chemical shifts of the b-b'-x region of human protein disulfide isomerase.' loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Byrne Lee J. . 2 Howard Mark J. . 3 Williamson Richard A. . 4 Sidhu Ateesh . . 5 Freedman Robert B. . 6 Wallis Katrine . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 218 "13C chemical shifts" 190 "15N chemical shifts" 215 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2009-11-12 update BMRB 'complete entry citation' 2009-07-17 original author 'original release' stop_ save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title "Mapping of the ligand-binding site on the b' domain of human PDI: interaction with peptide ligands and the x-linker region." _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 19604149 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Byrne Lee J. . 2 Sidhu Ateesh . . 3 Wallis 'A. Katrine' . . 4 Ruddock Lloyd W. . 5 Freedman Robert B. . 6 Howard Mark J. . 7 Williamson Richard A. . stop_ _Journal_abbreviation 'Biochem. J.' _Journal_name_full 'The Biochemical journal' _Journal_volume 423 _Journal_issue 2 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 209 _Page_last 217 _Year 2009 _Details . loop_ _Keyword 'ligand binding' PDI 'protein folding' thioredoxin stop_ save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name b-b'-x _Enzyme_commission_number 'EC 5.3.4.1' loop_ _Mol_system_component_name _Mol_label b-b'-x $b-b'-x stop_ _System_molecular_weight 26645.1 _System_physical_state native _System_oligomer_state ? _System_paramagnetic no _System_thiol_state . loop_ _Biological_function 'Peptide binding domain' stop_ _Database_query_date . _Details 'single polypeptide chain' save_ ######################## # Monomeric polymers # ######################## save_b-b'-x _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common b-b'-x _Molecular_mass 26645.1 _Mol_thiol_state 'all free' loop_ _Biological_function 'disulfide bond formation; disulfide bond isomerisation; ligand binding' stop_ _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 236 _Mol_residue_sequence ; GPAATTLPDGAAAESLVESS EVAVIGFFKDVESDSAKQFL QAAEAIDDIPFGITSNSDVF SKYQLDKDGVVLFKKFDEGR NNFEGEVTKENLLDFIKHNQ LPLVIEFTEQTAPKIFGGEI KTHILLFLPKSVSDYDGKLS NFKTAAESFKGKILFIFIDS DHTDNQRILEFFGLKKEECP AVRLITLEEEMTKYKPESEE LTAERITEFCHRFLEGKIKP HLMSQELPEDWDKQPV ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 117 GLY 2 118 PRO 3 119 ALA 4 120 ALA 5 121 THR 6 122 THR 7 123 LEU 8 124 PRO 9 125 ASP 10 126 GLY 11 127 ALA 12 128 ALA 13 129 ALA 14 130 GLU 15 131 SER 16 132 LEU 17 133 VAL 18 134 GLU 19 135 SER 20 136 SER 21 137 GLU 22 138 VAL 23 139 ALA 24 140 VAL 25 141 ILE 26 142 GLY 27 143 PHE 28 144 PHE 29 145 LYS 30 146 ASP 31 147 VAL 32 148 GLU 33 149 SER 34 150 ASP 35 151 SER 36 152 ALA 37 153 LYS 38 154 GLN 39 155 PHE 40 156 LEU 41 157 GLN 42 158 ALA 43 159 ALA 44 160 GLU 45 161 ALA 46 162 ILE 47 163 ASP 48 164 ASP 49 165 ILE 50 166 PRO 51 167 PHE 52 168 GLY 53 169 ILE 54 170 THR 55 171 SER 56 172 ASN 57 173 SER 58 174 ASP 59 175 VAL 60 176 PHE 61 177 SER 62 178 LYS 63 179 TYR 64 180 GLN 65 181 LEU 66 182 ASP 67 183 LYS 68 184 ASP 69 185 GLY 70 186 VAL 71 187 VAL 72 188 LEU 73 189 PHE 74 190 LYS 75 191 LYS 76 192 PHE 77 193 ASP 78 194 GLU 79 195 GLY 80 196 ARG 81 197 ASN 82 198 ASN 83 199 PHE 84 200 GLU 85 201 GLY 86 202 GLU 87 203 VAL 88 204 THR 89 205 LYS 90 206 GLU 91 207 ASN 92 208 LEU 93 209 LEU 94 210 ASP 95 211 PHE 96 212 ILE 97 213 LYS 98 214 HIS 99 215 ASN 100 216 GLN 101 217 LEU 102 218 PRO 103 219 LEU 104 220 VAL 105 221 ILE 106 222 GLU 107 223 PHE 108 224 THR 109 225 GLU 110 226 GLN 111 227 THR 112 228 ALA 113 229 PRO 114 230 LYS 115 231 ILE 116 232 PHE 117 233 GLY 118 234 GLY 119 235 GLU 120 236 ILE 121 237 LYS 122 238 THR 123 239 HIS 124 240 ILE 125 241 LEU 126 242 LEU 127 243 PHE 128 244 LEU 129 245 PRO 130 246 LYS 131 247 SER 132 248 VAL 133 249 SER 134 250 ASP 135 251 TYR 136 252 ASP 137 253 GLY 138 254 LYS 139 255 LEU 140 256 SER 141 257 ASN 142 258 PHE 143 259 LYS 144 260 THR 145 261 ALA 146 262 ALA 147 263 GLU 148 264 SER 149 265 PHE 150 266 LYS 151 267 GLY 152 268 LYS 153 269 ILE 154 270 LEU 155 271 PHE 156 272 ILE 157 273 PHE 158 274 ILE 159 275 ASP 160 276 SER 161 277 ASP 162 278 HIS 163 279 THR 164 280 ASP 165 281 ASN 166 282 GLN 167 283 ARG 168 284 ILE 169 285 LEU 170 286 GLU 171 287 PHE 172 288 PHE 173 289 GLY 174 290 LEU 175 291 LYS 176 292 LYS 177 293 GLU 178 294 GLU 179 295 CYS 180 296 PRO 181 297 ALA 182 298 VAL 183 299 ARG 184 300 LEU 185 301 ILE 186 302 THR 187 303 LEU 188 304 GLU 189 305 GLU 190 306 GLU 191 307 MET 192 308 THR 193 309 LYS 194 310 TYR 195 311 LYS 196 312 PRO 197 313 GLU 198 314 SER 199 315 GLU 200 316 GLU 201 317 LEU 202 318 THR 203 319 ALA 204 320 GLU 205 321 ARG 206 322 ILE 207 323 THR 208 324 GLU 209 325 PHE 210 326 CYS 211 327 HIS 212 328 ARG 213 329 PHE 214 330 LEU 215 331 GLU 216 332 GLY 217 333 LYS 218 334 ILE 219 335 LYS 220 336 PRO 221 337 HIS 222 338 LEU 223 339 MET 224 340 SER 225 341 GLN 226 342 GLU 227 343 LEU 228 344 PRO 229 345 GLU 230 346 ASP 231 347 TRP 232 348 ASP 233 349 LYS 234 350 GLN 235 351 PRO 236 352 VAL 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 BMRB 15303 bb-PDI 94.49 228 100.00 100.00 3.60e-157 BMRB 15998 "b'-x" 59.32 140 100.00 100.00 2.15e-95 PDB 2K18 "Solution Structure Of Bb' Domains Of Human Protein Disulfide Isomerase" 94.49 228 100.00 100.00 3.60e-157 PDB 3BJ5 "Alternative Conformations Of The X Region Of Human Protein Disulphide- Isomerase Modulate Exposure Of The Substrate Binding B' " 59.32 147 98.57 99.29 3.60e-94 PDB 3UEM "Crystal Structure Of Human Pdi Bb'a' Domains" 101.27 361 98.33 98.33 2.85e-163 PDB 4EKZ "Crystal Structure Of Reduced Hpdi (abb'xa')" 100.00 482 100.00 100.00 7.82e-165 PDB 4EL1 "Crystal Structure Of Oxidized Hpdi (abb'xa')" 100.00 482 100.00 100.00 7.82e-165 PDB 4JU5 "Crystal Structure Of The Dimeric Form Of The Bb' Domains Of Human Protein Disulfide Isomerase" 98.73 238 100.00 100.00 1.22e-165 DBJ BAE79726 "protein disulfide isomerase [Macaca fuscata]" 100.00 510 99.15 100.00 1.87e-163 DBJ BAE87231 "unnamed protein product [Macaca fascicularis]" 100.00 510 97.88 99.58 2.30e-161 DBJ BAE88032 "unnamed protein product [Macaca fascicularis]" 81.78 336 97.41 98.96 4.11e-128 DBJ BAG37999 "unnamed protein product [Homo sapiens]" 100.00 508 100.00 100.00 7.68e-165 DBJ BAG60277 "unnamed protein product [Homo sapiens]" 100.00 492 99.58 99.58 3.99e-164 EMBL CAA28775 "unnamed protein product [Homo sapiens]" 100.00 508 100.00 100.00 1.72e-164 EMBL CAH93050 "hypothetical protein [Pongo abelii]" 100.00 508 98.73 99.58 3.67e-163 GB AAA61169 "thyroid hormone binding protein precursor [Homo sapiens]" 100.00 508 98.31 98.31 2.24e-160 GB AAC13652 "prolyl 4-hydroxylase beta-subunit [Homo sapiens]" 100.00 508 100.00 100.00 7.68e-165 GB AAH10859 "Prolyl 4-hydroxylase, beta polypeptide [Homo sapiens]" 100.00 508 100.00 100.00 7.68e-165 GB AAH29617 "Prolyl 4-hydroxylase, beta polypeptide [Homo sapiens]" 100.00 508 100.00 100.00 7.68e-165 GB AAH71892 "Prolyl 4-hydroxylase, beta polypeptide [Homo sapiens]" 100.00 508 100.00 100.00 7.68e-165 REF NP_000909 "protein disulfide-isomerase precursor [Homo sapiens]" 100.00 508 100.00 100.00 7.68e-165 REF NP_001126805 "protein disulfide-isomerase precursor [Pongo abelii]" 100.00 508 98.73 99.58 3.67e-163 REF NP_001233358 "protein disulfide-isomerase precursor [Pan troglodytes]" 100.00 508 99.58 99.58 6.22e-164 REF XP_002764185 "PREDICTED: protein disulfide-isomerase isoform X2 [Callithrix jacchus]" 100.00 510 97.46 99.15 1.87e-161 REF XP_003282223 "PREDICTED: protein disulfide-isomerase isoform X1 [Nomascus leucogenys]" 100.00 505 97.88 98.31 2.65e-159 SP P07237 "RecName: Full=Protein disulfide-isomerase; Short=PDI; AltName: Full=Cellular thyroid hormone-binding protein; AltName: Full=Pro" 100.00 508 100.00 100.00 7.68e-165 SP Q2HWU2 "RecName: Full=Protein disulfide-isomerase; Short=PDI; AltName: Full=Prolyl 4-hydroxylase subunit beta; Flags: Precursor" 100.00 510 99.15 100.00 1.87e-163 SP Q5R5B6 "RecName: Full=Protein disulfide-isomerase; Short=PDI; AltName: Full=Cellular thyroid hormone-binding protein; AltName: Full=Pro" 100.00 508 98.73 99.58 3.67e-163 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $b-b'-x 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 $b-b'-x 'recombinant technology' . Escherichia coli BL21(DE3) pET23 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 $b-b'-x 10 % '[U-99% 13C; U-99% 15N]' D2O 10 % 'natural abundance' 'sodium phosphate' 20 mM 'natural abundance' 'sodium chloride' 150 mM 'natural abundance' stop_ save_ ############################ # Computer software used # ############################ save_CCPN_Analysis _Saveframe_category software _Name CCPN_Analysis _Version 1.15 loop_ _Vendor _Address _Electronic_address CCPN . www.ccpn.ac.uk/ccpn stop_ loop_ _Task 'chemical shift assignment' 'data analysis' 'peak picking' stop_ _Details . save_ save_NMRPipe _Saveframe_category software _Name NMRPipe _Version . loop_ _Vendor _Address _Electronic_address 'Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax' . www.spin.niddk.nih.gov stop_ loop_ _Task processing stop_ _Details . save_ save_VNMR _Saveframe_category software _Name VNMR _Version . loop_ _Vendor _Address _Electronic_address Varian . www.varianinc.com stop_ loop_ _Task collection stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model INOVA _Field_strength 600 _Details . save_ ############################# # NMR applied experiments # ############################# save_2D_1H-15N_HSQC_1 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-15N HSQC' _Sample_label $sample_1 save_ save_3D_CBCA(CO)NH_2 _Saveframe_category NMR_applied_experiment _Experiment_name '3D CBCA(CO)NH' _Sample_label $sample_1 save_ save_3D_HNCACB_3 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCACB' _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' 0.15 . M pH 6.5 . pH pressure 1 . atm temperature 313 . 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 . indirect . . . 0.251449530 DSS H 1 'methyl protons' ppm 0.00 internal direct . . . 1.000000000 DSS N 15 'methyl protons' ppm 0.00 . 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_ _Software_label $CCPN_Analysis stop_ loop_ _Experiment_label '2D 1H-15N HSQC' '3D CBCA(CO)NH' '3D HNCACB' 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 b-b'-x _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 1 119 3 ALA H H 8.334 0.003 1 2 119 3 ALA CA C 53.021 0.345 1 3 119 3 ALA N N 123.884 0.064 1 4 120 4 ALA H H 7.422 0.003 1 5 120 4 ALA CA C 50.480 0.345 1 6 120 4 ALA N N 117.801 0.064 1 7 121 5 THR H H 8.589 0.003 1 8 121 5 THR CA C 62.493 0.345 1 9 121 5 THR N N 119.099 0.064 1 10 122 6 THR H H 8.739 0.003 1 11 122 6 THR CA C 63.360 0.345 1 12 122 6 THR N N 124.896 0.064 1 13 123 7 LEU H H 8.858 0.003 1 14 123 7 LEU CA C 50.291 0.345 1 15 123 7 LEU N N 126.386 0.064 1 16 125 9 ASP H H 7.065 0.003 1 17 125 9 ASP CA C 52.455 0.345 1 18 125 9 ASP N N 112.007 0.064 1 19 126 10 GLY H H 9.026 0.003 1 20 126 10 GLY CA C 47.345 0.345 1 21 126 10 GLY N N 106.501 0.064 1 22 127 11 ALA H H 7.962 0.003 1 23 127 11 ALA CA C 55.080 0.345 1 24 127 11 ALA N N 125.099 0.064 1 25 128 12 ALA H H 8.227 0.003 1 26 128 12 ALA CA C 51.446 0.345 1 27 128 12 ALA N N 121.622 0.064 1 28 129 13 ALA H H 7.548 0.003 1 29 129 13 ALA N N 120.392 0.064 1 30 130 14 GLU H H 8.359 0.003 1 31 130 14 GLU CA C 59.254 0.345 1 32 130 14 GLU N N 117.010 0.064 1 33 131 15 SER H H 7.866 0.003 1 34 131 15 SER N N 112.698 0.064 1 35 132 16 LEU H H 7.418 0.003 1 36 132 16 LEU CA C 58.399 0.345 1 37 132 16 LEU N N 122.760 0.064 1 38 133 17 VAL H H 7.898 0.003 1 39 133 17 VAL CA C 66.839 0.345 1 40 133 17 VAL N N 119.213 0.064 1 41 134 18 GLU H H 8.149 0.003 1 42 134 18 GLU CA C 58.004 0.345 1 43 134 18 GLU N N 115.008 0.064 1 44 135 19 SER H H 7.501 0.003 1 45 135 19 SER CA C 59.789 0.345 1 46 135 19 SER N N 112.465 0.064 1 47 136 20 SER H H 7.050 0.003 1 48 136 20 SER CA C 57.240 0.345 1 49 136 20 SER N N 115.384 0.064 1 50 137 21 GLU H H 8.624 0.003 1 51 137 21 GLU CA C 60.184 0.345 1 52 137 21 GLU N N 124.453 0.064 1 53 138 22 VAL H H 7.268 0.003 1 54 138 22 VAL CA C 60.608 0.345 1 55 138 22 VAL N N 113.488 0.064 1 56 139 23 ALA H H 9.055 0.003 1 57 139 23 ALA CA C 51.383 0.345 1 58 139 23 ALA N N 126.864 0.064 1 59 140 24 VAL H H 7.934 0.003 1 60 140 24 VAL CA C 60.799 0.345 1 61 140 24 VAL N N 120.100 0.064 1 62 141 25 ILE H H 9.025 0.003 1 63 141 25 ILE CA C 60.016 0.345 1 64 141 25 ILE N N 124.336 0.064 1 65 142 26 GLY H H 8.573 0.003 1 66 142 26 GLY CA C 44.442 0.345 1 67 142 26 GLY N N 115.676 0.064 1 68 143 27 PHE H H 8.401 0.003 1 69 143 27 PHE CA C 55.033 0.345 1 70 143 27 PHE N N 127.905 0.064 1 71 144 28 PHE H H 8.129 0.003 1 72 144 28 PHE N N 116.987 0.064 1 73 145 29 LYS H H 9.351 0.003 1 74 145 29 LYS CA C 59.022 0.345 1 75 145 29 LYS N N 124.714 0.064 1 76 146 30 ASP H H 8.787 0.003 1 77 146 30 ASP CA C 51.873 0.345 1 78 146 30 ASP N N 117.151 0.064 1 79 147 31 VAL H H 8.468 0.003 1 80 147 31 VAL CA C 63.843 0.345 1 81 147 31 VAL N N 121.000 0.064 1 82 148 32 GLU H H 8.193 0.003 1 83 148 32 GLU CA C 55.342 0.345 1 84 148 32 GLU N N 117.096 0.064 1 85 149 33 SER H H 7.468 0.003 1 86 149 33 SER CA C 58.099 0.345 1 87 149 33 SER N N 115.851 0.064 1 88 150 34 ASP H H 8.800 0.003 1 89 150 34 ASP N N 121.384 0.064 1 90 151 35 SER H H 8.381 0.003 1 91 151 35 SER CA C 61.557 0.345 1 92 151 35 SER N N 113.957 0.064 1 93 152 36 ALA H H 6.911 0.003 1 94 152 36 ALA CA C 54.552 0.345 1 95 152 36 ALA N N 125.334 0.064 1 96 153 37 LYS H H 7.983 0.003 1 97 153 37 LYS CA C 60.130 0.345 1 98 153 37 LYS N N 115.884 0.064 1 99 154 38 GLN H H 7.827 0.003 1 100 154 38 GLN N N 118.751 0.064 1 101 155 39 PHE H H 7.670 0.003 1 102 155 39 PHE CA C 57.470 0.345 1 103 155 39 PHE N N 119.718 0.064 1 104 157 41 GLN H H 7.648 0.003 1 105 157 41 GLN CA C 58.805 0.345 1 106 157 41 GLN N N 117.606 0.064 1 107 158 42 ALA H H 7.601 0.003 1 108 158 42 ALA CA C 55.266 0.345 1 109 158 42 ALA N N 123.575 0.064 1 110 159 43 ALA H H 7.250 0.003 1 111 159 43 ALA CA C 53.236 0.345 1 112 159 43 ALA N N 117.922 0.064 1 113 160 44 GLU H H 6.921 0.003 1 114 160 44 GLU CA C 57.291 0.345 1 115 160 44 GLU N N 112.737 0.064 1 116 161 45 ALA H H 7.205 0.003 1 117 161 45 ALA CA C 52.551 0.345 1 118 161 45 ALA N N 119.716 0.064 1 119 162 46 ILE H H 7.004 0.003 1 120 162 46 ILE CA C 59.684 0.345 1 121 162 46 ILE N N 118.915 0.064 1 122 163 47 ASP H H 8.272 0.003 1 123 163 47 ASP CA C 54.462 0.345 1 124 164 48 ASP H H 8.465 0.003 1 125 164 48 ASP N N 115.673 0.064 1 126 165 49 ILE H H 7.112 0.003 1 127 165 49 ILE CA C 57.635 0.345 1 128 165 49 ILE N N 118.816 0.064 1 129 167 51 PHE H H 8.638 0.003 1 130 167 51 PHE CA C 55.554 0.345 1 131 167 51 PHE N N 120.134 0.064 1 132 168 52 GLY H H 9.439 0.003 1 133 168 52 GLY CA C 43.569 0.345 1 134 168 52 GLY N N 108.761 0.064 1 135 169 53 ILE H H 8.874 0.003 1 136 169 53 ILE CA C 58.515 0.345 1 137 170 54 THR H H 8.590 0.003 1 138 170 54 THR CA C 60.203 0.345 1 139 170 54 THR N N 121.162 0.064 1 140 171 55 SER H H 8.617 0.003 1 141 171 55 SER N N 119.742 0.064 1 142 174 58 ASP H H 8.575 0.003 1 143 174 58 ASP CA C 57.458 0.345 1 144 174 58 ASP N N 122.135 0.064 1 145 175 59 VAL H H 7.969 0.003 1 146 175 59 VAL N N 122.183 0.064 1 147 177 61 SER H H 8.016 0.003 1 148 177 61 SER N N 111.922 0.064 1 149 178 62 LYS H H 7.597 0.003 1 150 178 62 LYS N N 123.889 0.064 1 151 179 63 TYR H H 6.992 0.003 1 152 179 63 TYR CA C 58.518 0.345 1 153 179 63 TYR N N 113.722 0.064 1 154 180 64 GLN H H 7.798 0.003 1 155 180 64 GLN CA C 57.097 0.345 1 156 180 64 GLN N N 113.618 0.064 1 157 181 65 LEU H H 8.008 0.003 1 158 181 65 LEU CA C 54.956 0.345 1 159 181 65 LEU N N 120.464 0.064 1 160 182 66 ASP H H 8.493 0.003 1 161 182 66 ASP CA C 53.247 0.345 1 162 182 66 ASP N N 120.368 0.064 1 163 183 67 LYS H H 7.653 0.003 1 164 183 67 LYS CA C 54.642 0.345 1 165 184 68 ASP H H 7.682 0.003 1 166 184 68 ASP N N 116.997 0.064 1 167 185 69 GLY H H 8.592 0.003 1 168 185 69 GLY CA C 45.512 0.345 1 169 185 69 GLY N N 107.227 0.064 1 170 186 70 VAL H H 8.401 0.003 1 171 186 70 VAL CA C 61.274 0.345 1 172 186 70 VAL N N 117.764 0.064 1 173 187 71 VAL H H 8.879 0.003 1 174 187 71 VAL N N 126.762 0.064 1 175 188 72 LEU H H 8.635 0.003 1 176 188 72 LEU CA C 54.303 0.345 1 177 188 72 LEU N N 128.005 0.064 1 178 189 73 PHE H H 9.517 0.003 1 179 189 73 PHE CA C 57.049 0.345 1 180 189 73 PHE N N 126.455 0.064 1 181 190 74 LYS H H 8.378 0.003 1 182 190 74 LYS CA C 53.577 0.345 1 183 190 74 LYS N N 115.942 0.064 1 184 191 75 LYS H H 7.931 0.003 1 185 191 75 LYS CA C 55.783 0.345 1 186 191 75 LYS N N 121.296 0.064 1 187 192 76 PHE H H 6.590 0.003 1 188 192 76 PHE CA C 54.462 0.345 1 189 192 76 PHE N N 113.434 0.064 1 190 193 77 ASP H H 8.850 0.003 1 191 193 77 ASP CA C 56.028 0.345 1 192 193 77 ASP N N 117.643 0.064 1 193 194 78 GLU H H 10.153 0.003 1 194 194 78 GLU CA C 58.247 0.345 1 195 194 78 GLU N N 123.557 0.064 1 196 195 79 GLY H H 7.735 0.003 1 197 195 79 GLY CA C 46.548 0.345 1 198 195 79 GLY N N 108.948 0.064 1 199 196 80 ARG H H 7.184 0.003 1 200 196 80 ARG CA C 58.215 0.345 1 201 196 80 ARG N N 121.147 0.064 1 202 197 81 ASN H H 9.182 0.003 1 203 197 81 ASN CA C 53.714 0.345 1 204 197 81 ASN N N 121.628 0.064 1 205 198 82 ASN H H 9.033 0.003 1 206 198 82 ASN CA C 52.479 0.345 1 207 198 82 ASN N N 123.273 0.064 1 208 199 83 PHE H H 8.323 0.003 1 209 199 83 PHE CA C 58.957 0.345 1 210 199 83 PHE N N 124.817 0.064 1 211 200 84 GLU H H 7.354 0.003 1 212 200 84 GLU CA C 54.908 0.345 1 213 200 84 GLU N N 128.486 0.064 1 214 201 85 GLY H H 6.932 0.003 1 215 201 85 GLY CA C 43.356 0.345 1 216 201 85 GLY N N 108.389 0.064 1 217 202 86 GLU H H 8.336 0.003 1 218 202 86 GLU CA C 56.160 0.345 1 219 202 86 GLU N N 120.356 0.064 1 220 203 87 VAL H H 9.029 0.003 1 221 203 87 VAL CA C 64.378 0.345 1 222 203 87 VAL N N 126.416 0.064 1 223 204 88 THR H H 7.168 0.003 1 224 204 88 THR CA C 58.017 0.345 1 225 204 88 THR N N 117.666 0.064 1 226 205 89 LYS H H 9.280 0.003 1 227 205 89 LYS CA C 60.760 0.345 1 228 205 89 LYS N N 124.035 0.064 1 229 206 90 GLU H H 9.048 0.003 1 230 206 90 GLU N N 116.601 0.064 1 231 207 91 ASN H H 7.946 0.003 1 232 207 91 ASN CA C 55.458 0.345 1 233 207 91 ASN N N 118.078 0.064 1 234 208 92 LEU H H 8.483 0.003 1 235 208 92 LEU CA C 57.627 0.345 1 236 208 92 LEU N N 121.473 0.064 1 237 209 93 LEU H H 8.424 0.003 1 238 209 93 LEU CA C 59.102 0.345 1 239 209 93 LEU N N 120.062 0.064 1 240 210 94 ASP H H 7.598 0.003 1 241 210 94 ASP CA C 57.739 0.345 1 242 210 94 ASP N N 118.751 0.064 1 243 211 95 PHE H H 7.853 0.003 1 244 211 95 PHE CA C 60.356 0.345 1 245 211 95 PHE N N 120.689 0.064 1 246 212 96 ILE H H 8.705 0.003 1 247 212 96 ILE CA C 65.478 0.345 1 248 212 96 ILE N N 121.200 0.064 1 249 213 97 LYS H H 8.167 0.003 1 250 213 97 LYS CA C 59.270 0.345 1 251 213 97 LYS N N 117.848 0.064 1 252 214 98 HIS H H 7.803 0.003 1 253 214 98 HIS CA C 58.277 0.345 1 254 214 98 HIS N N 113.703 0.064 1 255 215 99 ASN H H 7.252 0.003 1 256 215 99 ASN CA C 54.415 0.345 1 257 215 99 ASN N N 114.181 0.064 1 258 216 100 GLN H H 7.580 0.003 1 259 216 100 GLN CA C 57.319 0.345 1 260 216 100 GLN N N 115.084 0.064 1 261 217 101 LEU H H 7.396 0.003 1 262 217 101 LEU CA C 51.904 0.345 1 263 217 101 LEU N N 119.539 0.064 1 264 219 103 LEU H H 9.316 0.003 1 265 219 103 LEU CA C 57.844 0.345 1 266 219 103 LEU N N 123.036 0.064 1 267 220 104 VAL H H 7.638 0.003 1 268 220 104 VAL CA C 59.453 0.345 1 269 220 104 VAL N N 109.842 0.064 1 270 221 105 ILE H H 8.647 0.003 1 271 221 105 ILE CA C 60.084 0.345 1 272 221 105 ILE N N 124.595 0.064 1 273 222 106 GLU H H 8.306 0.003 1 274 222 106 GLU CA C 54.835 0.345 1 275 222 106 GLU N N 127.843 0.064 1 276 223 107 PHE H H 8.636 0.003 1 277 223 107 PHE CA C 59.241 0.345 1 278 223 107 PHE N N 128.976 0.064 1 279 225 109 GLU H H 8.896 0.003 1 280 225 109 GLU CA C 59.296 0.345 1 281 225 109 GLU N N 120.147 0.064 1 282 226 110 GLN H H 7.854 0.003 1 283 226 110 GLN CA C 58.152 0.345 1 284 226 110 GLN N N 114.547 0.064 1 285 227 111 THR H H 7.428 0.003 1 286 227 111 THR CA C 61.787 0.345 1 287 227 111 THR N N 108.817 0.064 1 288 228 112 ALA H H 7.616 0.003 1 289 228 112 ALA CA C 56.793 0.345 1 290 228 112 ALA N N 125.461 0.064 1 291 230 114 LYS H H 7.177 0.003 1 292 230 114 LYS CA C 57.069 0.345 1 293 230 114 LYS N N 115.633 0.064 1 294 231 115 ILE H H 7.563 0.003 1 295 231 115 ILE CA C 64.310 0.345 1 296 231 115 ILE N N 118.863 0.064 1 297 232 116 PHE H H 7.885 0.003 1 298 232 116 PHE CA C 59.024 0.345 1 299 232 116 PHE N N 115.406 0.064 1 300 233 117 GLY H H 7.565 0.003 1 301 233 117 GLY CA C 45.474 0.345 1 302 233 117 GLY N N 106.707 0.064 1 303 234 118 GLY H H 7.409 0.003 1 304 234 118 GLY CA C 44.819 0.345 1 305 234 118 GLY N N 107.890 0.064 1 306 235 119 GLU H H 8.376 0.003 1 307 235 119 GLU CA C 57.868 0.345 1 308 235 119 GLU N N 117.566 0.064 1 309 236 120 ILE H H 7.757 0.003 1 310 236 120 ILE CA C 61.874 0.345 1 311 236 120 ILE N N 119.550 0.064 1 312 237 121 LYS H H 8.475 0.003 1 313 237 121 LYS CA C 55.616 0.345 1 314 237 121 LYS N N 125.375 0.064 1 315 238 122 THR H H 6.766 0.003 1 316 238 122 THR CA C 62.016 0.345 1 317 238 122 THR N N 115.882 0.064 1 318 239 123 HIS H H 8.797 0.003 1 319 239 123 HIS CA C 53.584 0.345 1 320 239 123 HIS N N 125.682 0.064 1 321 240 124 ILE H H 9.191 0.003 1 322 240 124 ILE CA C 58.868 0.345 1 323 240 124 ILE N N 122.571 0.064 1 324 241 125 LEU H H 8.991 0.003 1 325 241 125 LEU CA C 53.694 0.345 1 326 241 125 LEU N N 128.576 0.064 1 327 242 126 LEU H H 8.652 0.003 1 328 242 126 LEU CA C 52.903 0.345 1 329 242 126 LEU N N 123.265 0.064 1 330 243 127 PHE H H 9.049 0.003 1 331 243 127 PHE CA C 56.649 0.345 1 332 243 127 PHE N N 127.243 0.064 1 333 244 128 LEU H H 8.946 0.003 1 334 244 128 LEU CA C 50.994 0.345 1 335 244 128 LEU N N 126.870 0.064 1 336 246 130 LYS H H 8.213 0.003 1 337 246 130 LYS CA C 58.693 0.345 1 338 246 130 LYS N N 123.812 0.064 1 339 247 131 SER H H 7.575 0.003 1 340 247 131 SER CA C 58.340 0.345 1 341 247 131 SER N N 108.212 0.064 1 342 248 132 VAL H H 7.434 0.003 1 343 248 132 VAL CA C 61.882 0.345 1 344 248 132 VAL N N 122.210 0.064 1 345 249 133 SER H H 8.341 0.003 1 346 249 133 SER CA C 59.770 0.345 1 347 249 133 SER N N 120.161 0.064 1 348 250 134 ASP H H 8.868 0.003 1 349 250 134 ASP CA C 54.120 0.345 1 350 250 134 ASP N N 122.175 0.064 1 351 251 135 TYR H H 7.566 0.003 1 352 251 135 TYR CA C 62.723 0.345 1 353 251 135 TYR N N 120.506 0.064 1 354 252 136 ASP H H 8.579 0.003 1 355 252 136 ASP CA C 57.481 0.345 1 356 252 136 ASP N N 115.273 0.064 1 357 253 137 GLY H H 7.762 0.003 1 358 253 137 GLY CA C 47.036 0.345 1 359 253 137 GLY N N 110.041 0.064 1 360 254 138 LYS H H 7.997 0.003 1 361 254 138 LYS CA C 59.742 0.345 1 362 254 138 LYS N N 123.122 0.064 1 363 255 139 LEU H H 8.049 0.003 1 364 255 139 LEU CA C 57.491 0.345 1 365 255 139 LEU N N 120.067 0.064 1 366 256 140 SER H H 8.277 0.003 1 367 256 140 SER CA C 62.165 0.345 1 368 256 140 SER N N 114.597 0.064 1 369 257 141 ASN H H 7.962 0.003 1 370 257 141 ASN N N 121.668 0.064 1 371 258 142 PHE H H 7.694 0.003 1 372 258 142 PHE CA C 61.403 0.345 1 373 258 142 PHE N N 121.741 0.064 1 374 259 143 LYS H H 8.451 0.003 1 375 259 143 LYS N N 117.577 0.064 1 376 260 144 THR H H 8.186 0.003 1 377 260 144 THR CA C 66.832 0.345 1 378 260 144 THR N N 116.007 0.064 1 379 261 145 ALA H H 7.515 0.003 1 380 261 145 ALA N N 123.834 0.064 1 381 262 146 ALA H H 7.305 0.003 1 382 262 146 ALA CA C 54.099 0.345 1 383 262 146 ALA N N 119.601 0.064 1 384 263 147 GLU H H 7.018 0.003 1 385 263 147 GLU N N 114.367 0.064 1 386 264 148 SER H H 7.431 0.003 1 387 264 148 SER CA C 60.691 0.345 1 388 264 148 SER N N 111.951 0.064 1 389 265 149 PHE H H 7.186 0.003 1 390 265 149 PHE CA C 57.792 0.345 1 391 265 149 PHE N N 115.757 0.064 1 392 266 150 LYS H H 7.200 0.003 1 393 266 150 LYS CA C 58.585 0.345 1 394 266 150 LYS N N 123.803 0.064 1 395 267 151 GLY H H 9.620 0.003 1 396 267 151 GLY CA C 45.508 0.345 1 397 267 151 GLY N N 115.315 0.064 1 398 268 152 LYS H H 8.340 0.003 1 399 268 152 LYS CA C 57.151 0.345 1 400 268 152 LYS N N 118.786 0.064 1 401 269 153 ILE H H 7.816 0.003 1 402 269 153 ILE CA C 60.316 0.345 1 403 269 153 ILE N N 116.451 0.064 1 404 270 154 LEU H H 8.269 0.003 1 405 270 154 LEU CA C 54.667 0.345 1 406 270 154 LEU N N 129.712 0.064 1 407 271 155 PHE H H 9.190 0.003 1 408 271 155 PHE CA C 56.602 0.345 1 409 271 155 PHE N N 129.783 0.064 1 410 272 156 ILE H H 9.058 0.003 1 411 272 156 ILE CA C 58.918 0.345 1 412 272 156 ILE N N 123.846 0.064 1 413 273 157 PHE H H 8.869 0.003 1 414 273 157 PHE CA C 54.617 0.345 1 415 273 157 PHE N N 122.984 0.064 1 416 274 158 ILE H H 8.723 0.003 1 417 274 158 ILE N N 122.057 0.064 1 418 275 159 ASP H H 8.351 0.003 1 419 275 159 ASP N N 123.660 0.064 1 420 276 160 SER H H 7.501 0.003 1 421 276 160 SER CA C 60.600 0.345 1 422 276 160 SER N N 123.917 0.064 1 423 277 161 ASP H H 8.359 0.003 1 424 277 161 ASP CA C 55.542 0.345 1 425 277 161 ASP N N 119.459 0.064 1 426 278 162 HIS H H 7.191 0.003 1 427 278 162 HIS CA C 54.658 0.345 1 428 278 162 HIS N N 121.127 0.064 1 429 279 163 THR H H 7.978 0.003 1 430 279 163 THR N N 121.813 0.064 1 431 280 164 ASP H H 10.688 0.003 1 432 280 164 ASP CA C 56.720 0.345 1 433 280 164 ASP N N 124.396 0.064 1 434 281 165 ASN H H 7.910 0.003 1 435 281 165 ASN CA C 52.694 0.345 1 436 281 165 ASN N N 114.954 0.064 1 437 282 166 GLN H H 7.605 0.003 1 438 282 166 GLN CA C 59.569 0.345 1 439 282 166 GLN N N 120.987 0.064 1 440 283 167 ARG H H 8.428 0.003 1 441 283 167 ARG N N 117.933 0.064 1 442 284 168 ILE H H 7.671 0.003 1 443 284 168 ILE CA C 61.043 0.345 1 444 284 168 ILE N N 119.611 0.064 1 445 285 169 LEU H H 8.329 0.003 1 446 285 169 LEU CA C 55.324 0.345 1 447 285 169 LEU N N 119.370 0.064 1 448 286 170 GLU H H 7.193 0.003 1 449 286 170 GLU N N 119.153 0.064 1 450 287 171 PHE H H 8.127 0.003 1 451 287 171 PHE CA C 60.744 0.345 1 452 287 171 PHE N N 121.800 0.064 1 453 288 172 PHE H H 7.517 0.003 1 454 288 172 PHE CA C 59.555 0.345 1 455 288 172 PHE N N 113.040 0.064 1 456 289 173 GLY H H 7.974 0.003 1 457 289 173 GLY CA C 46.787 0.345 1 458 289 173 GLY N N 110.739 0.064 1 459 290 174 LEU H H 7.720 0.003 1 460 290 174 LEU N N 120.817 0.064 1 461 291 175 LYS H H 8.101 0.003 1 462 291 175 LYS CA C 53.950 0.345 1 463 291 175 LYS N N 119.119 0.064 1 464 292 176 LYS H H 9.008 0.003 1 465 292 176 LYS N N 124.031 0.064 1 466 293 177 GLU H H 9.392 0.003 1 467 293 177 GLU CA C 58.812 0.345 1 468 293 177 GLU N N 116.569 0.064 1 469 294 178 GLU H H 7.608 0.003 1 470 294 178 GLU CA C 55.814 0.345 1 471 294 178 GLU N N 118.151 0.064 1 472 295 179 CYS H H 7.036 0.003 1 473 295 179 CYS CA C 58.361 0.345 1 474 295 179 CYS N N 117.667 0.064 1 475 297 181 ALA H H 8.382 0.003 1 476 297 181 ALA CA C 51.566 0.345 1 477 297 181 ALA N N 123.043 0.064 1 478 298 182 VAL H H 8.604 0.003 1 479 298 182 VAL CA C 59.382 0.345 1 480 298 182 VAL N N 118.135 0.064 1 481 299 183 ARG H H 8.916 0.003 1 482 299 183 ARG CA C 53.018 0.345 1 483 299 183 ARG N N 123.088 0.064 1 484 300 184 LEU H H 8.689 0.003 1 485 300 184 LEU CA C 54.187 0.345 1 486 300 184 LEU N N 125.144 0.064 1 487 301 185 ILE H H 9.564 0.003 1 488 301 185 ILE CA C 58.588 0.345 1 489 301 185 ILE N N 121.813 0.064 1 490 302 186 THR H H 8.726 0.003 1 491 302 186 THR CA C 59.152 0.345 1 492 302 186 THR N N 114.061 0.064 1 493 303 187 LEU H H 8.564 0.003 1 494 303 187 LEU CA C 54.365 0.345 1 495 303 187 LEU N N 125.042 0.064 1 496 304 188 GLU H H 7.514 0.003 1 497 304 188 GLU CA C 56.586 0.345 1 498 304 188 GLU N N 123.343 0.064 1 499 305 189 GLU H H 8.455 0.003 1 500 305 189 GLU CA C 59.251 0.345 1 501 305 189 GLU N N 122.165 0.064 1 502 306 190 GLU H H 7.898 0.003 1 503 306 190 GLU CA C 54.949 0.345 1 504 306 190 GLU N N 116.276 0.064 1 505 307 191 MET H H 8.830 0.003 1 506 307 191 MET CA C 56.144 0.345 1 507 307 191 MET N N 123.727 0.064 1 508 308 192 THR H H 8.379 0.003 1 509 308 192 THR CA C 62.318 0.345 1 510 308 192 THR N N 121.817 0.064 1 511 309 193 LYS H H 8.566 0.003 1 512 309 193 LYS CA C 55.026 0.345 1 513 309 193 LYS N N 123.438 0.064 1 514 310 194 TYR H H 9.548 0.003 1 515 310 194 TYR N N 119.468 0.064 1 516 311 195 LYS H H 9.161 0.003 1 517 311 195 LYS CA C 52.592 0.345 1 518 311 195 LYS N N 122.445 0.064 1 519 314 198 SER H H 7.482 0.003 1 520 314 198 SER CA C 56.482 0.345 1 521 314 198 SER N N 111.708 0.064 1 522 315 199 GLU H H 8.695 0.003 1 523 315 199 GLU CA C 55.881 0.345 1 524 315 199 GLU N N 122.859 0.064 1 525 316 200 GLU H H 8.226 0.003 1 526 316 200 GLU CA C 57.401 0.345 1 527 316 200 GLU N N 121.367 0.064 1 528 317 201 LEU H H 8.574 0.003 1 529 317 201 LEU CA C 53.056 0.345 1 530 317 201 LEU N N 125.387 0.064 1 531 318 202 THR H H 6.789 0.003 1 532 318 202 THR CA C 59.382 0.345 1 533 318 202 THR N N 108.240 0.064 1 534 319 203 ALA H H 9.234 0.003 1 535 319 203 ALA CA C 56.183 0.345 1 536 319 203 ALA N N 125.340 0.064 1 537 320 204 GLU H H 9.305 0.003 1 538 320 204 GLU CA C 60.364 0.345 1 539 320 204 GLU N N 118.241 0.064 1 540 321 205 ARG H H 7.635 0.003 1 541 321 205 ARG CA C 57.917 0.345 1 542 321 205 ARG N N 119.609 0.064 1 543 322 206 ILE H H 8.485 0.003 1 544 322 206 ILE CA C 65.413 0.345 1 545 322 206 ILE N N 121.726 0.064 1 546 323 207 THR H H 8.567 0.003 1 547 323 207 THR N N 116.897 0.064 1 548 324 208 GLU H H 8.016 0.003 1 549 324 208 GLU CA C 59.877 0.345 1 550 324 208 GLU N N 121.638 0.064 1 551 325 209 PHE H H 7.884 0.003 1 552 325 209 PHE CA C 55.511 0.345 1 553 325 209 PHE N N 119.832 0.064 1 554 326 210 CYS H H 7.697 0.003 1 555 326 210 CYS CA C 64.370 0.345 1 556 326 210 CYS N N 116.039 0.064 1 557 327 211 HIS H H 8.571 0.003 1 558 327 211 HIS CA C 60.323 0.345 1 559 327 211 HIS N N 118.010 0.064 1 560 328 212 ARG H H 8.707 0.003 1 561 328 212 ARG CA C 59.947 0.345 1 562 328 212 ARG N N 118.831 0.064 1 563 329 213 PHE H H 8.268 0.003 1 564 329 213 PHE CA C 56.323 0.345 1 565 329 213 PHE N N 120.405 0.064 1 566 330 214 LEU H H 8.167 0.003 1 567 330 214 LEU CA C 57.531 0.345 1 568 330 214 LEU N N 123.563 0.064 1 569 331 215 GLU H H 7.705 0.003 1 570 331 215 GLU CA C 56.206 0.345 1 571 331 215 GLU N N 116.305 0.064 1 572 332 216 GLY H H 7.686 0.003 1 573 332 216 GLY CA C 46.447 0.345 1 574 332 216 GLY N N 108.487 0.064 1 575 333 217 LYS H H 7.949 0.003 1 576 333 217 LYS CA C 56.128 0.345 1 577 333 217 LYS N N 116.568 0.064 1 578 334 218 ILE H H 7.831 0.003 1 579 334 218 ILE CA C 58.759 0.345 1 580 334 218 ILE N N 118.578 0.064 1 581 335 219 LYS H H 8.660 0.003 1 582 335 219 LYS CA C 54.382 0.345 1 583 335 219 LYS N N 128.120 0.064 1 584 337 221 HIS H H 8.423 0.003 1 585 337 221 HIS CA C 57.245 0.345 1 586 337 221 HIS N N 120.443 0.064 1 587 338 222 LEU H H 7.770 0.003 1 588 338 222 LEU CA C 53.557 0.345 1 589 338 222 LEU N N 118.691 0.064 1 590 339 223 MET H H 7.672 0.003 1 591 339 223 MET CA C 55.786 0.345 1 592 339 223 MET N N 120.342 0.064 1 593 340 224 SER H H 8.115 0.003 1 594 340 224 SER CA C 58.394 0.345 1 595 340 224 SER N N 116.249 0.064 1 596 341 225 GLN H H 8.229 0.003 1 597 341 225 GLN N N 121.190 0.064 1 598 342 226 GLU H H 7.910 0.003 1 599 342 226 GLU CA C 57.319 0.345 1 600 342 226 GLU N N 120.578 0.064 1 601 343 227 LEU H H 8.062 0.003 1 602 343 227 LEU CA C 55.122 0.345 1 603 343 227 LEU N N 125.128 0.064 1 604 345 229 GLU H H 8.327 0.003 1 605 345 229 GLU CA C 57.624 0.345 1 606 345 229 GLU N N 121.237 0.064 1 607 346 230 ASP H H 8.219 0.003 1 608 346 230 ASP CA C 54.056 0.345 1 609 346 230 ASP N N 119.152 0.064 1 610 347 231 TRP H H 7.739 0.003 1 611 347 231 TRP HE1 H 10.147 0.003 1 612 347 231 TRP CA C 57.900 0.345 1 613 347 231 TRP N N 120.667 0.064 1 614 347 231 TRP NE1 N 129.267 0.064 1 615 348 232 ASP H H 7.994 0.003 1 616 348 232 ASP CA C 53.986 0.345 1 617 348 232 ASP N N 120.564 0.064 1 618 349 233 LYS H H 7.551 0.003 1 619 349 233 LYS CA C 55.767 0.345 1 620 349 233 LYS N N 120.279 0.064 1 621 350 234 GLN H H 8.091 0.003 1 622 350 234 GLN CA C 53.526 0.345 1 623 350 234 GLN N N 122.932 0.064 1 stop_ save_