data_6057 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Sequence-specific resonance assignments of the tandem SH3 domains in autoinhibitory form of p47phox ; _BMRB_accession_number 6057 _BMRB_flat_file_name bmr6057.str _Entry_type original _Submission_date 2003-12-27 _Accession_date 2004-01-02 _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 Yuzawa Satoru . . 2 Yokochi Masashi . . 3 Fujioka Yuko . . 4 Ogura Kenji . . 5 Sumimoto Hideki . . 6 Inagaki Fuyuhiko . . 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" 551 "15N chemical shifts" 179 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2004-06-28 update BMRB 'citation updated' stop_ save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; Solution structure of the tandem SH3 domains of p47phox in an autoinhibited form. ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 15123602 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Yuzawa Satoru . . 2 Ogura Kenji . . 3 Horiuchi M. . . 4 Suzuki N. N. . 5 Fujioka Yuko . . 6 Kataoka M. . . 7 Sumimoto Hideki . . 8 Inagaki Fuyuhiko . . stop_ _Journal_abbreviation 'J. Biol. Chem.' _Journal_volume 29 _Journal_issue 3 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 451 _Page_last 452 _Year 2004 _Details . loop_ _Keyword p47phox 'SH3 domain' autoinhibition multidomain 'NADPH oxidase' stop_ save_ ####################################### # Cited references within the entry # ####################################### save_ref-1 _Saveframe_category citation _Citation_full ; Delaglio F, Grzesiek S, Vuister GW, Zhu G, Pfeifer J, Bax A. NMRPipe: a multidimensional spectral processing system based on UNIX pipes. J Biomol NMR. 1995 Nov;6(3):277-93. ; _Citation_title 'NMRPipe: a multidimensional spectral processing system based on UNIX pipes.' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 8520220 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Delaglio F. . . 2 Grzesiek S. . . 3 Vuister 'G. W.' W. . 4 Zhu G. . . 5 Pfeifer J. . . 6 Bax A. . . stop_ _Journal_abbreviation 'J. Biomol. NMR' _Journal_name_full 'Journal of biomolecular NMR' _Journal_volume 6 _Journal_issue 3 _Journal_CSD . _Book_title . _Book_chapter_title . _Book_volume . _Book_series . _Book_publisher . _Book_publisher_city . _Book_ISBN . _Conference_title . _Conference_site . _Conference_state_province . _Conference_country . _Conference_start_date . _Conference_end_date . _Conference_abstract_number . _Thesis_institution . _Thesis_institution_city . _Thesis_institution_country . _Page_first 277 _Page_last 293 _Year 1995 _Details ; The NMRPipe system is a UNIX software environment of processing, graphics, and analysis tools designed to meet current routine and research-oriented multidimensional processing requirements, and to anticipate and accommodate future demands and developments. The system is based on UNIX pipes, which allow programs running simultaneously to exchange streams of data under user control. In an NMRPipe processing scheme, a stream of spectral data flows through a pipeline of processing programs, each of which performs one component of the overall scheme, such as Fourier transformation or linear prediction. Complete multidimensional processing schemes are constructed as simple UNIX shell scripts. The processing modules themselves maintain and exploit accurate records of data sizes, detection modes, and calibration information in all dimensions, so that schemes can be constructed without the need to explicitly define or anticipate data sizes or storage details of real and imaginary channels during processing. The asynchronous pipeline scheme provides other substantial advantages, including high flexibility, favorable processing speeds, choice of both all-in-memory and disk-bound processing, easy adaptation to different data formats, simpler software development and maintenance, and the ability to distribute processing tasks on multi-CPU computers and computer networks. ; save_ save_ref-2 _Saveframe_category citation _Citation_full ; Yokochi & Inagaki, unpublished http://fermi.pharm.hokudai.ac.jp ; _Citation_title . _Citation_status . _Citation_type . _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID ? _Journal_abbreviation . _Journal_name_full . _Journal_volume . _Journal_issue . _Journal_CSD . _Book_title . _Book_chapter_title . _Book_volume . _Book_series . _Book_publisher . _Book_publisher_city . _Book_ISBN . _Conference_title . _Conference_site . _Conference_state_province . _Conference_country . _Conference_start_date . _Conference_end_date . _Conference_abstract_number . _Thesis_institution . _Thesis_institution_city . _Thesis_institution_country . _Page_first . _Page_last . _Year . _Details . save_ ################################## # Molecular system description # ################################## save_system_p47phox _Saveframe_category molecular_system _Mol_system_name 'tandem SH3 domain in autoinhibited form of p47phox' _Abbreviation_common p47phox _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label p47phox $p47phox stop_ _System_molecular_weight 21988.85 _System_physical_state native _System_oligomer_state monomer _System_paramagnetic no _System_thiol_state 'all free' loop_ _Biological_function 'signal transduction' 'NADPH oxidase' stop_ _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_p47phox _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common p47phox _Abbreviation_common p47phox _Molecular_mass 21988.85 _Mol_thiol_state 'all free' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 193 _Mol_residue_sequence ; GAMDITGPIILQTYRAIADY EKTSGSEMALSTGDVVEVVE KSESGWWFCQMKAKRGWIPA SFLEPLDSPDETEDPEPNYA GEPYVAIKAYTAVEGDEVSL LEGEAVEVIHKLLDGWWVIR KDDVTGYFPSMYLQKSGQDV SQAQRQIKRGAPPRRSSIRN AHSIHQRSRKRLSQDAYRRN SVRFLQQRRRQAR ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 148 GLY 2 149 ALA 3 150 MET 4 151 ASP 5 152 ILE 6 153 THR 7 154 GLY 8 155 PRO 9 156 ILE 10 157 ILE 11 158 LEU 12 159 GLN 13 160 THR 14 161 TYR 15 162 ARG 16 163 ALA 17 164 ILE 18 165 ALA 19 166 ASP 20 167 TYR 21 168 GLU 22 169 LYS 23 170 THR 24 171 SER 25 172 GLY 26 173 SER 27 174 GLU 28 175 MET 29 176 ALA 30 177 LEU 31 178 SER 32 179 THR 33 180 GLY 34 181 ASP 35 182 VAL 36 183 VAL 37 184 GLU 38 185 VAL 39 186 VAL 40 187 GLU 41 188 LYS 42 189 SER 43 190 GLU 44 191 SER 45 192 GLY 46 193 TRP 47 194 TRP 48 195 PHE 49 196 CYS 50 197 GLN 51 198 MET 52 199 LYS 53 200 ALA 54 201 LYS 55 202 ARG 56 203 GLY 57 204 TRP 58 205 ILE 59 206 PRO 60 207 ALA 61 208 SER 62 209 PHE 63 210 LEU 64 211 GLU 65 212 PRO 66 213 LEU 67 214 ASP 68 215 SER 69 216 PRO 70 217 ASP 71 218 GLU 72 219 THR 73 220 GLU 74 221 ASP 75 222 PRO 76 223 GLU 77 224 PRO 78 225 ASN 79 226 TYR 80 227 ALA 81 228 GLY 82 229 GLU 83 230 PRO 84 231 TYR 85 232 VAL 86 233 ALA 87 234 ILE 88 235 LYS 89 236 ALA 90 237 TYR 91 238 THR 92 239 ALA 93 240 VAL 94 241 GLU 95 242 GLY 96 243 ASP 97 244 GLU 98 245 VAL 99 246 SER 100 247 LEU 101 248 LEU 102 249 GLU 103 250 GLY 104 251 GLU 105 252 ALA 106 253 VAL 107 254 GLU 108 255 VAL 109 256 ILE 110 257 HIS 111 258 LYS 112 259 LEU 113 260 LEU 114 261 ASP 115 262 GLY 116 263 TRP 117 264 TRP 118 265 VAL 119 266 ILE 120 267 ARG 121 268 LYS 122 269 ASP 123 270 ASP 124 271 VAL 125 272 THR 126 273 GLY 127 274 TYR 128 275 PHE 129 276 PRO 130 277 SER 131 278 MET 132 279 TYR 133 280 LEU 134 281 GLN 135 282 LYS 136 283 SER 137 284 GLY 138 285 GLN 139 286 ASP 140 287 VAL 141 288 SER 142 289 GLN 143 290 ALA 144 291 GLN 145 292 ARG 146 293 GLN 147 294 ILE 148 295 LYS 149 296 ARG 150 297 GLY 151 298 ALA 152 299 PRO 153 300 PRO 154 301 ARG 155 302 ARG 156 303 SER 157 304 SER 158 305 ILE 159 306 ARG 160 307 ASN 161 308 ALA 162 309 HIS 163 310 SER 164 311 ILE 165 312 HIS 166 313 GLN 167 314 ARG 168 315 SER 169 316 ARG 170 317 LYS 171 318 ARG 172 319 LEU 173 320 SER 174 321 GLN 175 322 ASP 176 323 ALA 177 324 TYR 178 325 ARG 179 326 ARG 180 327 ASN 181 328 SER 182 329 VAL 183 330 ARG 184 331 PHE 185 332 LEU 186 333 GLN 187 334 GLN 188 335 ARG 189 336 ARG 190 337 ARG 191 338 GLN 192 339 ALA 193 340 ARG 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 1NG2 "Structure Of Autoinhibited P47phox" 95.85 193 100.00 100.00 9.73e-132 PDB 1OV3 "Structure Of The P22phox-P47phox Complex" 67.36 138 100.00 100.00 4.98e-89 PDB 1UEC "Crystal Structure Of Autoinhibited Form Of Tandem Sh3 Domain Of P47phox" 100.00 193 100.00 100.00 8.25e-139 PDB 1WLP "Solution Structure Of The P22phox-P47phox Complex" 70.47 138 100.00 100.00 3.12e-94 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species _Fraction _Gene_mnemonic $p47phox Human 9606 Eukaryota Metazoa Homo sapiens cytoplasm NCF-1 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_type _Vector_name $p47phox 'recombinant technology' 'E. coli' Escherichia coli BL21 DE3 plasmid 'pPRO EX HTb' 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 $p47phox 1.0 mM '[U-90% 2H; U-98% 13C; U-98% 15N]' stop_ save_ ############################ # Computer software used # ############################ save_nmrPipe _Saveframe_category software _Name nmrPipe _Version . loop_ _Task 'raw spectral data processing' stop_ _Details . _Citation_label $ref-1 save_ save_Olivia _Saveframe_category software _Name Olivia _Version . loop_ _Task 'data processing' 'assignment analysis' stop_ _Details 'In-house developed software for automating the peak assignment process.' _Citation_label $ref-2 save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model INOVAplus _Field_strength 600 _Details . save_ ############################# # NMR applied experiments # ############################# save_1H-15N_HSQC_1 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-15N HSQC' _Sample_label $sample_1 save_ save_HNCO_2 _Saveframe_category NMR_applied_experiment _Experiment_name HNCO _Sample_label $sample_1 save_ save_HN(CA)CO_3 _Saveframe_category NMR_applied_experiment _Experiment_name HN(CA)CO _Sample_label $sample_1 save_ save_HNCA_4 _Saveframe_category NMR_applied_experiment _Experiment_name HNCA _Sample_label $sample_1 save_ save_HN(CO)CA_5 _Saveframe_category NMR_applied_experiment _Experiment_name HN(CO)CA _Sample_label $sample_1 save_ save_NH(CO)CACB_6 _Saveframe_category NMR_applied_experiment _Experiment_name NH(CO)CACB _Sample_label $sample_1 save_ save_HNCACB_7 _Saveframe_category NMR_applied_experiment _Experiment_name HNCACB _Sample_label $sample_1 save_ ####################### # Sample conditions # ####################### save_Ex-cond_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 6.5 0.05 n/a temperature 298 0.1 K 'ionic strength' 0.20 . M stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference _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 H 1 'methyl protons' ppm 0.0 internal direct . . . 1.000000000 DSS N 15 'methyl protons' ppm 0.0 . indirect . . . 0.101329118 DSS C 13 'methyl protons' ppm 0.0 . indirect . . . 0.251449530 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_shift_set_1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $Ex-cond_1 _Chem_shift_reference_set_label $chemical_shift_reference _Mol_system_component_name p47phox _Text_data_format . _Text_data . loop_ _Atom_shift_assign_ID _Residue_author_seq_code _Residue_seq_code _Residue_label _Atom_name _Atom_type _Chem_shift_value _Chem_shift_value_error _Chem_shift_ambiguity_code 1 . 2 ALA C C 178.0 0.14 1 2 . 2 ALA CA C 52.8 0.14 1 3 . 2 ALA CB C 18.4 0.14 1 4 . 3 MET H H 8.44 0.01 1 5 . 3 MET C C 175.9 0.14 1 6 . 3 MET CA C 54.9 0.14 1 7 . 3 MET CB C 31.8 0.14 1 8 . 3 MET N N 118.2 0.07 1 9 . 4 ASP H H 8.07 0.01 1 10 . 4 ASP C C 176.1 0.14 1 11 . 4 ASP CA C 54.1 0.14 1 12 . 4 ASP CB C 40.6 0.14 1 13 . 4 ASP N N 121.5 0.07 1 14 . 5 ILE H H 8.04 0.01 1 15 . 5 ILE C C 176.6 0.14 1 16 . 5 ILE CA C 60.8 0.14 1 17 . 5 ILE CB C 37.8 0.14 1 18 . 5 ILE N N 121.0 0.07 1 19 . 6 THR H H 8.20 0.01 1 20 . 6 THR C C 174.8 0.14 1 21 . 6 THR CA C 61.5 0.14 1 22 . 6 THR CB C 69.4 0.14 1 23 . 6 THR N N 117.9 0.07 1 24 . 7 GLY H H 8.08 0.01 1 25 . 7 GLY CA C 44.1 0.14 1 26 . 7 GLY N N 111.8 0.07 1 27 . 8 PRO C C 176.7 0.14 1 28 . 8 PRO CA C 62.5 0.14 1 29 . 8 PRO CB C 31.3 0.14 1 30 . 9 ILE H H 8.15 0.01 1 31 . 9 ILE C C 175.9 0.14 1 32 . 9 ILE CA C 60.6 0.14 1 33 . 9 ILE CB C 37.8 0.14 1 34 . 9 ILE N N 121.9 0.07 1 35 . 10 ILE H H 8.26 0.01 1 36 . 10 ILE C C 175.9 0.14 1 37 . 10 ILE CA C 60.0 0.14 1 38 . 10 ILE CB C 37.5 0.14 1 39 . 10 ILE N N 127.4 0.07 1 40 . 11 LEU H H 8.37 0.01 1 41 . 11 LEU C C 177.2 0.14 1 42 . 11 LEU CA C 53.9 0.14 1 43 . 11 LEU CB C 41.0 0.14 1 44 . 11 LEU N N 127.7 0.07 1 45 . 12 GLN H H 8.85 0.01 1 46 . 12 GLN C C 175.9 0.14 1 47 . 12 GLN CA C 55.9 0.14 1 48 . 12 GLN CB C 29.9 0.14 1 49 . 12 GLN N N 122.5 0.07 1 50 . 13 THR H H 8.29 0.01 1 51 . 13 THR C C 173.9 0.14 1 52 . 13 THR CA C 59.9 0.14 1 53 . 13 THR CB C 69.9 0.14 1 54 . 13 THR N N 114.1 0.07 1 55 . 14 TYR H H 9.21 0.01 1 56 . 14 TYR C C 173.4 0.14 1 57 . 14 TYR CA C 55.8 0.14 1 58 . 14 TYR CB C 43.4 0.14 1 59 . 14 TYR N N 127.1 0.07 1 60 . 15 ARG H H 9.54 0.01 1 61 . 15 ARG C C 175.4 0.14 1 62 . 15 ARG CA C 52.7 0.14 1 63 . 15 ARG CB C 33.4 0.14 1 64 . 15 ARG N N 118.6 0.07 1 65 . 16 ALA H H 9.09 0.01 1 66 . 16 ALA C C 179.4 0.14 1 67 . 16 ALA CA C 50.8 0.14 1 68 . 16 ALA CB C 19.5 0.14 1 69 . 16 ALA N N 126.7 0.07 1 70 . 17 ILE H H 8.67 0.01 1 71 . 17 ILE C C 174.4 0.14 1 72 . 17 ILE CA C 60.6 0.14 1 73 . 17 ILE CB C 37.5 0.14 1 74 . 17 ILE N N 117.1 0.07 1 75 . 18 ALA H H 7.71 0.01 1 76 . 18 ALA C C 174.5 0.14 1 77 . 18 ALA CA C 50.5 0.14 1 78 . 18 ALA CB C 21.4 0.14 1 79 . 18 ALA N N 121.1 0.07 1 80 . 19 ASP H H 7.87 0.01 1 81 . 19 ASP C C 174.8 0.14 1 82 . 19 ASP CA C 52.6 0.14 1 83 . 19 ASP CB C 38.0 0.14 1 84 . 19 ASP N N 114.0 0.07 1 85 . 20 TYR H H 8.93 0.01 1 86 . 20 TYR C C 174.3 0.14 1 87 . 20 TYR CA C 57.4 0.14 1 88 . 20 TYR CB C 40.8 0.14 1 89 . 20 TYR N N 124.5 0.07 1 90 . 21 GLU H H 7.54 0.01 1 91 . 21 GLU C C 174.7 0.14 1 92 . 21 GLU CA C 54.4 0.14 1 93 . 21 GLU CB C 29.4 0.14 1 94 . 21 GLU N N 127.3 0.07 1 95 . 22 LYS H H 7.79 0.01 1 96 . 22 LYS C C 177.3 0.14 1 97 . 22 LYS CA C 56.2 0.14 1 98 . 22 LYS CB C 32.4 0.14 1 99 . 22 LYS N N 121.4 0.07 1 100 . 23 THR H H 8.76 0.01 1 101 . 23 THR C C 174.4 0.14 1 102 . 23 THR CA C 61.1 0.14 1 103 . 23 THR CB C 69.9 0.14 1 104 . 23 THR N N 115.2 0.07 1 105 . 24 SER H H 7.75 0.01 1 106 . 24 SER CA C 57.9 0.14 1 107 . 24 SER CB C 64.6 0.14 1 108 . 24 SER N N 115.9 0.07 1 109 . 26 SER C C 174.8 0.14 1 110 . 26 SER CA C 58.0 0.14 1 111 . 26 SER CB C 63.6 0.14 1 112 . 27 GLU H H 7.66 0.01 1 113 . 27 GLU C C 175.2 0.14 1 114 . 27 GLU CA C 55.6 0.14 1 115 . 27 GLU CB C 31.8 0.14 1 116 . 27 GLU N N 122.0 0.07 1 117 . 28 MET H H 7.64 0.01 1 118 . 28 MET C C 172.6 0.14 1 119 . 28 MET CA C 54.4 0.14 1 120 . 28 MET CB C 35.0 0.14 1 121 . 28 MET N N 119.2 0.07 1 122 . 29 ALA H H 7.99 0.01 1 123 . 29 ALA C C 177.4 0.14 1 124 . 29 ALA CA C 50.9 0.14 1 125 . 29 ALA CB C 19.7 0.14 1 126 . 29 ALA N N 124.4 0.07 1 127 . 30 LEU H H 8.73 0.01 1 128 . 30 LEU C C 177.1 0.14 1 129 . 30 LEU CA C 53.4 0.14 1 130 . 30 LEU CB C 45.8 0.14 1 131 . 30 LEU N N 118.2 0.07 1 132 . 31 SER H H 9.09 0.01 1 133 . 31 SER C C 173.3 0.14 1 134 . 31 SER CA C 56.3 0.14 1 135 . 31 SER CB C 64.7 0.14 1 136 . 31 SER N N 120.8 0.07 1 137 . 32 THR H H 8.08 0.01 1 138 . 32 THR C C 175.7 0.14 1 139 . 32 THR CA C 64.9 0.14 1 140 . 32 THR CB C 67.9 0.14 1 141 . 32 THR N N 119.0 0.07 1 142 . 33 GLY H H 9.40 0.01 1 143 . 33 GLY C C 174.6 0.14 1 144 . 33 GLY CA C 44.6 0.14 1 145 . 33 GLY N N 117.0 0.07 1 146 . 34 ASP H H 8.50 0.01 1 147 . 34 ASP C C 175.1 0.14 1 148 . 34 ASP CA C 55.7 0.14 1 149 . 34 ASP CB C 41.3 0.14 1 150 . 34 ASP N N 123.8 0.07 1 151 . 35 VAL H H 8.03 0.01 1 152 . 35 VAL C C 176.3 0.14 1 153 . 35 VAL CA C 61.1 0.14 1 154 . 35 VAL CB C 32.1 0.14 1 155 . 35 VAL N N 120.4 0.07 1 156 . 36 VAL H H 9.14 0.01 1 157 . 36 VAL C C 174.6 0.14 1 158 . 36 VAL CA C 57.9 0.14 1 159 . 36 VAL CB C 33.9 0.14 1 160 . 36 VAL N N 119.8 0.07 1 161 . 37 GLU H H 8.81 0.01 1 162 . 37 GLU C C 176.8 0.14 1 163 . 37 GLU CA C 54.1 0.14 1 164 . 37 GLU CB C 31.0 0.14 1 165 . 37 GLU N N 120.0 0.07 1 166 . 38 VAL H H 8.85 0.01 1 167 . 38 VAL C C 174.4 0.14 1 168 . 38 VAL CA C 62.6 0.14 1 169 . 38 VAL CB C 31.0 0.14 1 170 . 38 VAL N N 125.2 0.07 1 171 . 39 VAL H H 8.69 0.01 1 172 . 39 VAL C C 176.7 0.14 1 173 . 39 VAL CA C 63.6 0.14 1 174 . 39 VAL CB C 31.5 0.14 1 175 . 39 VAL N N 129.6 0.07 1 176 . 40 GLU H H 7.91 0.01 1 177 . 40 GLU C C 175.0 0.14 1 178 . 40 GLU CA C 55.5 0.14 1 179 . 40 GLU CB C 32.8 0.14 1 180 . 40 GLU N N 118.1 0.07 1 181 . 41 LYS H H 8.48 0.01 1 182 . 41 LYS C C 175.2 0.14 1 183 . 41 LYS CA C 54.2 0.14 1 184 . 41 LYS CB C 32.2 0.14 1 185 . 41 LYS N N 127.6 0.07 1 186 . 42 SER H H 6.49 0.01 1 187 . 42 SER C C 176.3 0.14 1 188 . 42 SER CA C 57.1 0.14 1 189 . 42 SER CB C 64.0 0.14 1 190 . 42 SER N N 114.0 0.07 1 191 . 43 GLU H H 9.20 0.01 1 192 . 43 GLU C C 176.0 0.14 1 193 . 43 GLU CA C 57.5 0.14 1 194 . 43 GLU CB C 28.3 0.14 1 195 . 43 GLU N N 126.9 0.07 1 196 . 44 SER H H 8.25 0.01 1 197 . 44 SER C C 175.2 0.14 1 198 . 44 SER CA C 59.6 0.14 1 199 . 44 SER CB C 64.7 0.14 1 200 . 44 SER N N 116.5 0.07 1 201 . 45 GLY H H 8.22 0.01 1 202 . 45 GLY C C 172.4 0.14 1 203 . 45 GLY CA C 45.1 0.14 1 204 . 45 GLY N N 109.0 0.07 1 205 . 46 TRP H H 8.10 0.01 1 206 . 46 TRP C C 174.4 0.14 1 207 . 46 TRP CA C 55.9 0.14 1 208 . 46 TRP CB C 29.4 0.14 1 209 . 46 TRP N N 122.7 0.07 1 210 . 47 TRP H H 9.63 0.01 1 211 . 47 TRP C C 175.1 0.14 1 212 . 47 TRP CA C 53.3 0.14 1 213 . 47 TRP CB C 31.4 0.14 1 214 . 47 TRP N N 124.8 0.07 1 215 . 48 PHE H H 8.79 0.01 1 216 . 48 PHE C C 175.3 0.14 1 217 . 48 PHE CA C 56.9 0.14 1 218 . 48 PHE CB C 38.4 0.14 1 219 . 48 PHE N N 127.5 0.07 1 220 . 49 CYS H H 8.32 0.01 1 221 . 49 CYS C C 170.7 0.14 1 222 . 49 CYS CA C 57.3 0.14 1 223 . 49 CYS CB C 32.8 0.14 1 224 . 49 CYS N N 125.4 0.07 1 225 . 50 GLN H H 9.16 0.01 1 226 . 50 GLN C C 173.8 0.14 1 227 . 50 GLN CA C 53.3 0.14 1 228 . 50 GLN CB C 32.3 0.14 1 229 . 50 GLN N N 117.1 0.07 1 230 . 51 MET H H 8.83 0.01 1 231 . 51 MET C C 174.9 0.14 1 232 . 51 MET CA C 55.3 0.14 1 233 . 51 MET CB C 34.5 0.14 1 234 . 51 MET N N 123.9 0.07 1 235 . 52 LYS H H 9.33 0.01 1 236 . 52 LYS C C 175.8 0.14 1 237 . 52 LYS CA C 58.3 0.14 1 238 . 52 LYS CB C 29.1 0.14 1 239 . 52 LYS N N 125.6 0.07 1 240 . 53 ALA H H 8.24 0.01 1 241 . 53 ALA C C 177.1 0.14 1 242 . 53 ALA CA C 52.6 0.14 1 243 . 53 ALA CB C 18.0 0.14 1 244 . 53 ALA N N 121.8 0.07 1 245 . 54 LYS H H 7.88 0.01 1 246 . 54 LYS C C 174.7 0.14 1 247 . 54 LYS CA C 55.1 0.14 1 248 . 54 LYS CB C 33.9 0.14 1 249 . 54 LYS N N 120.2 0.07 1 250 . 55 ARG H H 8.14 0.01 1 251 . 55 ARG C C 175.9 0.14 1 252 . 55 ARG CA C 54.4 0.14 1 253 . 55 ARG CB C 32.9 0.14 1 254 . 55 ARG N N 119.0 0.07 1 255 . 56 GLY H H 7.89 0.01 1 256 . 56 GLY C C 170.5 0.14 1 257 . 56 GLY CA C 44.9 0.14 1 258 . 56 GLY N N 106.7 0.07 1 259 . 57 TRP H H 8.66 0.01 1 260 . 57 TRP C C 176.3 0.14 1 261 . 57 TRP CA C 57.2 0.14 1 262 . 57 TRP CB C 30.5 0.14 1 263 . 57 TRP N N 121.8 0.07 1 264 . 58 ILE H H 9.50 0.01 1 265 . 58 ILE CA C 56.5 0.14 1 266 . 58 ILE CB C 41.8 0.14 1 267 . 58 ILE N N 120.1 0.07 1 268 . 59 PRO C C 177.0 0.14 1 269 . 59 PRO CA C 61.2 0.14 1 270 . 59 PRO CB C 30.0 0.14 1 271 . 60 ALA H H 8.05 0.01 1 272 . 60 ALA C C 179.3 0.14 1 273 . 60 ALA CA C 54.0 0.14 1 274 . 60 ALA CB C 16.0 0.14 1 275 . 60 ALA N N 128.8 0.07 1 276 . 61 SER H H 8.23 0.01 1 277 . 61 SER C C 175.2 0.14 1 278 . 61 SER CA C 59.1 0.14 1 279 . 61 SER CB C 62.5 0.14 1 280 . 61 SER N N 111.1 0.07 1 281 . 62 PHE H H 7.46 0.01 1 282 . 62 PHE C C 174.1 0.14 1 283 . 62 PHE CA C 59.8 0.14 1 284 . 62 PHE CB C 38.5 0.14 1 285 . 62 PHE N N 119.7 0.07 1 286 . 63 LEU H H 7.64 0.01 1 287 . 63 LEU C C 176.9 0.14 1 288 . 63 LEU CA C 52.5 0.14 1 289 . 63 LEU CB C 45.6 0.14 1 290 . 63 LEU N N 119.1 0.07 1 291 . 64 GLU H H 9.49 0.01 1 292 . 64 GLU CA C 51.8 0.14 1 293 . 64 GLU CB C 30.6 0.14 1 294 . 64 GLU N N 119.1 0.07 1 295 . 65 PRO C C 176.5 0.14 1 296 . 65 PRO CA C 61.2 0.14 1 297 . 65 PRO CB C 30.4 0.14 1 298 . 66 LEU H H 7.96 0.01 1 299 . 66 LEU C C 178.6 0.14 1 300 . 66 LEU CA C 56.2 0.14 1 301 . 66 LEU CB C 41.0 0.14 1 302 . 66 LEU N N 118.6 0.07 1 303 . 67 ASP H H 8.47 0.01 1 304 . 67 ASP C C 175.9 0.14 1 305 . 67 ASP CA C 54.9 0.14 1 306 . 67 ASP CB C 40.5 0.14 1 307 . 67 ASP N N 115.7 0.07 1 308 . 68 SER H H 7.39 0.01 1 309 . 68 SER CA C 54.7 0.14 1 310 . 68 SER CB C 64.6 0.14 1 311 . 68 SER N N 116.8 0.07 1 312 . 69 PRO C C 176.4 0.14 1 313 . 69 PRO CA C 63.0 0.14 1 314 . 69 PRO CB C 31.2 0.14 1 315 . 70 ASP H H 7.59 0.01 1 316 . 70 ASP C C 174.4 0.14 1 317 . 70 ASP CA C 54.3 0.14 1 318 . 70 ASP CB C 41.5 0.14 1 319 . 70 ASP N N 119.4 0.07 1 320 . 71 GLU H H 8.19 0.01 1 321 . 71 GLU C C 177.5 0.14 1 322 . 71 GLU CA C 54.7 0.14 1 323 . 71 GLU CB C 28.6 0.14 1 324 . 71 GLU N N 122.7 0.07 1 325 . 72 THR H H 8.37 0.01 1 326 . 72 THR C C 176.7 0.14 1 327 . 72 THR CA C 63.6 0.14 1 328 . 72 THR CB C 69.3 0.14 1 329 . 72 THR N N 120.8 0.07 1 330 . 73 GLU H H 8.72 0.01 1 331 . 73 GLU C C 176.1 0.14 1 332 . 73 GLU CA C 56.2 0.14 1 333 . 73 GLU CB C 29.5 0.14 1 334 . 73 GLU N N 119.4 0.07 1 335 . 74 ASP H H 7.22 0.01 1 336 . 74 ASP C C 175.4 0.14 1 337 . 74 ASP CA C 53.7 0.14 1 338 . 74 ASP CB C 40.0 0.14 1 339 . 74 ASP N N 122.3 0.07 1 340 . 75 PRO C C 176.1 0.14 1 341 . 75 PRO CA C 61.6 0.14 1 342 . 75 PRO CB C 31.5 0.14 1 343 . 76 GLU H H 8.36 0.01 1 344 . 76 GLU C C 175.2 0.14 1 345 . 76 GLU CA C 54.2 0.14 1 346 . 76 GLU CB C 28.3 0.14 1 347 . 76 GLU N N 119.6 0.07 1 348 . 77 PRO C C 175.3 0.14 1 349 . 77 PRO CA C 62.5 0.14 1 350 . 77 PRO CB C 30.5 0.14 1 351 . 78 ASN H H 8.55 0.01 1 352 . 78 ASN C C 175.7 0.14 1 353 . 78 ASN CA C 50.2 0.14 1 354 . 78 ASN CB C 37.7 0.14 1 355 . 78 ASN N N 120.8 0.07 1 356 . 79 TYR H H 8.13 0.01 1 357 . 79 TYR C C 175.8 0.14 1 358 . 79 TYR CA C 61.1 0.14 1 359 . 79 TYR CB C 36.9 0.14 1 360 . 79 TYR N N 120.0 0.07 1 361 . 80 ALA H H 7.41 0.01 1 362 . 80 ALA C C 179.3 0.14 1 363 . 80 ALA CA C 54.0 0.14 1 364 . 80 ALA CB C 17.4 0.14 1 365 . 80 ALA N N 121.7 0.07 1 366 . 81 GLY H H 6.72 0.01 1 367 . 81 GLY C C 172.5 0.14 1 368 . 81 GLY CA C 43.4 0.14 1 369 . 81 GLY N N 102.4 0.07 1 370 . 82 GLU H H 7.85 0.01 1 371 . 82 GLU C C 175.6 0.14 1 372 . 82 GLU CA C 52.8 0.14 1 373 . 82 GLU CB C 33.1 0.14 1 374 . 82 GLU N N 119.7 0.07 1 375 . 83 PRO C C 176.5 0.14 1 376 . 83 PRO CA C 63.7 0.14 1 377 . 83 PRO CB C 31.1 0.14 1 378 . 84 TYR H H 8.91 0.01 1 379 . 84 TYR C C 174.3 0.14 1 380 . 84 TYR CA C 56.6 0.14 1 381 . 84 TYR CB C 44.6 0.14 1 382 . 84 TYR N N 127.8 0.07 1 383 . 85 VAL H H 9.34 0.01 1 384 . 85 VAL C C 175.3 0.14 1 385 . 85 VAL CA C 58.9 0.14 1 386 . 85 VAL CB C 34.9 0.14 1 387 . 85 VAL N N 117.3 0.07 1 388 . 86 ALA H H 8.47 0.01 1 389 . 86 ALA C C 179.5 0.14 1 390 . 86 ALA CA C 51.8 0.14 1 391 . 86 ALA CB C 17.2 0.14 1 392 . 86 ALA N N 126.5 0.07 1 393 . 87 ILE H H 8.97 0.01 1 394 . 87 ILE C C 174.5 0.14 1 395 . 87 ILE CA C 60.1 0.14 1 396 . 87 ILE CB C 37.8 0.14 1 397 . 87 ILE N N 119.5 0.07 1 398 . 88 LYS H H 7.48 0.01 1 399 . 88 LYS C C 172.8 0.14 1 400 . 88 LYS CA C 54.9 0.14 1 401 . 88 LYS CB C 34.7 0.14 1 402 . 88 LYS N N 122.3 0.07 1 403 . 89 ALA H H 8.22 0.01 1 404 . 89 ALA C C 177.5 0.14 1 405 . 89 ALA CA C 51.6 0.14 1 406 . 89 ALA CB C 18.9 0.14 1 407 . 89 ALA N N 124.1 0.07 1 408 . 90 TYR H H 8.55 0.01 1 409 . 90 TYR C C 173.6 0.14 1 410 . 90 TYR CA C 58.5 0.14 1 411 . 90 TYR CB C 41.1 0.14 1 412 . 90 TYR N N 121.0 0.07 1 413 . 91 THR H H 7.32 0.01 1 414 . 91 THR C C 171.3 0.14 1 415 . 91 THR CA C 60.4 0.14 1 416 . 91 THR CB C 69.4 0.14 1 417 . 91 THR N N 125.6 0.07 1 418 . 92 ALA H H 8.62 0.01 1 419 . 92 ALA C C 177.9 0.14 1 420 . 92 ALA CA C 52.7 0.14 1 421 . 92 ALA CB C 19.9 0.14 1 422 . 92 ALA N N 127.7 0.07 1 423 . 93 VAL H H 8.68 0.01 1 424 . 93 VAL C C 176.8 0.14 1 425 . 93 VAL CA C 62.7 0.14 1 426 . 93 VAL CB C 32.3 0.14 1 427 . 93 VAL N N 122.0 0.07 1 428 . 94 GLU H H 6.74 0.01 1 429 . 94 GLU C C 178.6 0.14 1 430 . 94 GLU CA C 54.4 0.14 1 431 . 94 GLU CB C 31.4 0.14 1 432 . 94 GLU N N 118.0 0.07 1 433 . 95 GLY H H 8.85 0.01 1 434 . 95 GLY C C 173.7 0.14 1 435 . 95 GLY CA C 46.3 0.14 1 436 . 95 GLY N N 107.4 0.07 1 437 . 96 ASP H H 8.21 0.01 1 438 . 96 ASP C C 175.6 0.14 1 439 . 96 ASP CA C 52.2 0.14 1 440 . 96 ASP CB C 39.0 0.14 1 441 . 96 ASP N N 117.3 0.07 1 442 . 97 GLU H H 7.39 0.01 1 443 . 97 GLU C C 176.2 0.14 1 444 . 97 GLU CA C 54.5 0.14 1 445 . 97 GLU CB C 32.0 0.14 1 446 . 97 GLU N N 119.1 0.07 1 447 . 98 VAL H H 8.33 0.01 1 448 . 98 VAL C C 174.0 0.14 1 449 . 98 VAL CA C 60.6 0.14 1 450 . 98 VAL CB C 34.1 0.14 1 451 . 98 VAL N N 121.6 0.07 1 452 . 99 SER H H 8.09 0.01 1 453 . 99 SER C C 174.5 0.14 1 454 . 99 SER CA C 57.4 0.14 1 455 . 99 SER CB C 63.6 0.14 1 456 . 99 SER N N 119.5 0.07 1 457 . 100 LEU H H 8.69 0.01 1 458 . 100 LEU C C 176.7 0.14 1 459 . 100 LEU CA C 53.3 0.14 1 460 . 100 LEU CB C 44.8 0.14 1 461 . 100 LEU N N 121.7 0.07 1 462 . 101 LEU H H 9.11 0.01 1 463 . 101 LEU C C 176.9 0.14 1 464 . 101 LEU CA C 52.5 0.14 1 465 . 101 LEU CB C 41.8 0.14 1 466 . 101 LEU N N 122.4 0.07 1 467 . 102 GLU H H 8.17 0.01 1 468 . 102 GLU C C 177.6 0.14 1 469 . 102 GLU CA C 58.4 0.14 1 470 . 102 GLU CB C 28.4 0.14 1 471 . 102 GLU N N 118.8 0.07 1 472 . 103 GLY H H 8.90 0.01 1 473 . 103 GLY C C 174.3 0.14 1 474 . 103 GLY CA C 44.4 0.14 1 475 . 103 GLY N N 114.0 0.07 1 476 . 104 GLU H H 7.60 0.01 1 477 . 104 GLU C C 174.7 0.14 1 478 . 104 GLU CA C 58.3 0.14 1 479 . 104 GLU CB C 30.4 0.14 1 480 . 104 GLU N N 120.8 0.07 1 481 . 105 ALA H H 8.31 0.01 1 482 . 105 ALA C C 177.7 0.14 1 483 . 105 ALA CA C 51.1 0.14 1 484 . 105 ALA CB C 19.2 0.14 1 485 . 105 ALA N N 126.4 0.07 1 486 . 106 VAL H H 8.85 0.01 1 487 . 106 VAL C C 174.6 0.14 1 488 . 106 VAL CA C 58.8 0.14 1 489 . 106 VAL CB C 35.6 0.14 1 490 . 106 VAL N N 114.2 0.07 1 491 . 107 GLU H H 8.26 0.01 1 492 . 107 GLU C C 176.1 0.14 1 493 . 107 GLU CA C 53.8 0.14 1 494 . 107 GLU CB C 31.8 0.14 1 495 . 107 GLU N N 118.3 0.07 1 496 . 108 VAL H H 9.62 0.01 1 497 . 108 VAL C C 176.6 0.14 1 498 . 108 VAL CA C 63.2 0.14 1 499 . 108 VAL CB C 31.7 0.14 1 500 . 108 VAL N N 124.6 0.07 1 501 . 109 ILE H H 8.67 0.01 1 502 . 109 ILE C C 175.2 0.14 1 503 . 109 ILE CA C 59.5 0.14 1 504 . 109 ILE CB C 39.0 0.14 1 505 . 109 ILE N N 122.7 0.07 1 506 . 110 HIS H H 7.68 0.01 1 507 . 110 HIS C C 174.7 0.14 1 508 . 110 HIS CA C 54.1 0.14 1 509 . 110 HIS CB C 34.2 0.14 1 510 . 110 HIS N N 121.4 0.07 1 511 . 111 LYS H H 8.29 0.01 1 512 . 111 LYS C C 173.5 0.14 1 513 . 111 LYS CA C 54.4 0.14 1 514 . 111 LYS CB C 30.9 0.14 1 515 . 111 LYS N N 131.7 0.07 1 516 . 112 LEU H H 6.00 0.01 1 517 . 112 LEU C C 178.9 0.14 1 518 . 112 LEU CA C 55.0 0.14 1 519 . 112 LEU CB C 42.5 0.14 1 520 . 112 LEU N N 122.2 0.07 1 521 . 113 LEU H H 8.81 0.01 1 522 . 113 LEU C C 175.9 0.14 1 523 . 113 LEU CA C 56.1 0.14 1 524 . 113 LEU CB C 41.8 0.14 1 525 . 113 LEU N N 119.5 0.07 1 526 . 114 ASP H H 7.56 0.01 1 527 . 114 ASP C C 178.2 0.14 1 528 . 114 ASP CA C 52.9 0.14 1 529 . 114 ASP CB C 38.5 0.14 1 530 . 114 ASP N N 115.0 0.07 1 531 . 115 GLY H H 7.85 0.01 1 532 . 115 GLY C C 173.6 0.14 1 533 . 115 GLY CA C 45.2 0.14 1 534 . 115 GLY N N 104.9 0.07 1 535 . 116 TRP H H 7.92 0.01 1 536 . 116 TRP C C 174.9 0.14 1 537 . 116 TRP CA C 57.1 0.14 1 538 . 116 TRP CB C 27.6 0.14 1 539 . 116 TRP N N 125.3 0.07 1 540 . 117 TRP H H 8.41 0.01 1 541 . 117 TRP C C 175.4 0.14 1 542 . 117 TRP CA C 53.7 0.14 1 543 . 117 TRP CB C 31.0 0.14 1 544 . 117 TRP N N 124.9 0.07 1 545 . 118 VAL H H 8.31 0.01 1 546 . 118 VAL C C 176.2 0.14 1 547 . 118 VAL CA C 61.8 0.14 1 548 . 118 VAL CB C 30.3 0.14 1 549 . 118 VAL N N 119.2 0.07 1 550 . 119 ILE H H 9.33 0.01 1 551 . 119 ILE C C 172.7 0.14 1 552 . 119 ILE CA C 57.8 0.14 1 553 . 119 ILE CB C 41.5 0.14 1 554 . 119 ILE N N 123.9 0.07 1 555 . 120 ARG H H 9.19 0.01 1 556 . 120 ARG C C 174.6 0.14 1 557 . 120 ARG CA C 53.7 0.14 1 558 . 120 ARG CB C 33.8 0.14 1 559 . 120 ARG N N 119.8 0.07 1 560 . 121 LYS H H 8.73 0.01 1 561 . 121 LYS C C 175.4 0.14 1 562 . 121 LYS CA C 54.7 0.14 1 563 . 121 LYS CB C 33.1 0.14 1 564 . 121 LYS N N 127.2 0.07 1 565 . 122 ASP H H 9.34 0.01 1 566 . 122 ASP C C 174.6 0.14 1 567 . 122 ASP CA C 56.8 0.14 1 568 . 122 ASP CB C 39.0 0.14 1 569 . 122 ASP N N 127.2 0.07 1 570 . 123 ASP H H 8.48 0.01 1 571 . 123 ASP C C 175.9 0.14 1 572 . 123 ASP CA C 54.6 0.14 1 573 . 123 ASP CB C 40.3 0.14 1 574 . 123 ASP N N 119.9 0.07 1 575 . 124 VAL H H 8.06 0.01 1 576 . 124 VAL C C 175.2 0.14 1 577 . 124 VAL CA C 62.1 0.14 1 578 . 124 VAL CB C 32.8 0.14 1 579 . 124 VAL N N 122.1 0.07 1 580 . 125 THR H H 7.69 0.01 1 581 . 125 THR C C 174.4 0.14 1 582 . 125 THR CA C 59.2 0.14 1 583 . 125 THR CB C 71.2 0.14 1 584 . 125 THR N N 116.3 0.07 1 585 . 126 GLY H H 8.28 0.01 1 586 . 126 GLY C C 170.7 0.14 1 587 . 126 GLY CA C 45.0 0.14 1 588 . 126 GLY N N 108.7 0.07 1 589 . 127 TYR H H 9.45 0.01 1 590 . 127 TYR C C 176.5 0.14 1 591 . 127 TYR CA C 58.8 0.14 1 592 . 127 TYR CB C 41.6 0.14 1 593 . 127 TYR N N 118.6 0.07 1 594 . 128 PHE H H 9.35 0.01 1 595 . 128 PHE CA C 56.4 0.14 1 596 . 128 PHE CB C 46.1 0.14 1 597 . 128 PHE N N 121.4 0.07 1 598 . 129 PRO C C 177.2 0.14 1 599 . 129 PRO CA C 60.8 0.14 1 600 . 129 PRO CB C 29.1 0.14 1 601 . 130 SER H H 7.93 0.01 1 602 . 130 SER C C 176.9 0.14 1 603 . 130 SER CA C 59.7 0.14 1 604 . 130 SER CB C 60.7 0.14 1 605 . 130 SER N N 124.5 0.07 1 606 . 131 MET H H 8.20 0.01 1 607 . 131 MET C C 176.3 0.14 1 608 . 131 MET CA C 56.0 0.14 1 609 . 131 MET CB C 32.2 0.14 1 610 . 131 MET N N 119.1 0.07 1 611 . 132 TYR H H 7.07 0.01 1 612 . 132 TYR C C 174.6 0.14 1 613 . 132 TYR CA C 52.9 0.14 1 614 . 132 TYR CB C 36.0 0.14 1 615 . 132 TYR N N 116.6 0.07 1 616 . 133 LEU H H 7.70 0.01 1 617 . 133 LEU C C 175.8 0.14 1 618 . 133 LEU CA C 53.0 0.14 1 619 . 133 LEU CB C 45.6 0.14 1 620 . 133 LEU N N 121.5 0.07 1 621 . 134 GLN H H 9.21 0.01 1 622 . 134 GLN C C 174.2 0.14 1 623 . 134 GLN CA C 53.7 0.14 1 624 . 134 GLN CB C 32.9 0.14 1 625 . 134 GLN N N 119.9 0.07 1 626 . 135 LYS H H 8.67 0.01 1 627 . 135 LYS C C 176.7 0.14 1 628 . 135 LYS CA C 57.2 0.14 1 629 . 135 LYS CB C 31.8 0.14 1 630 . 135 LYS N N 128.4 0.07 1 631 . 136 SER H H 7.77 0.01 1 632 . 136 SER C C 175.6 0.14 1 633 . 136 SER CA C 59.2 0.14 1 634 . 136 SER CB C 62.9 0.14 1 635 . 136 SER N N 118.8 0.07 1 636 . 137 GLY H H 8.66 0.01 1 637 . 137 GLY C C 174.1 0.14 1 638 . 137 GLY CA C 45.0 0.14 1 639 . 137 GLY N N 113.7 0.07 1 640 . 138 GLN H H 7.66 0.01 1 641 . 138 GLN C C 175.2 0.14 1 642 . 138 GLN CA C 54.5 0.14 1 643 . 138 GLN CB C 29.2 0.14 1 644 . 138 GLN N N 119.5 0.07 1 645 . 139 ASP H H 8.38 0.01 1 646 . 139 ASP C C 177.0 0.14 1 647 . 139 ASP CA C 54.0 0.14 1 648 . 139 ASP CB C 40.9 0.14 1 649 . 139 ASP N N 122.2 0.07 1 650 . 140 VAL H H 8.29 0.01 1 651 . 140 VAL C C 176.9 0.14 1 652 . 140 VAL CA C 62.9 0.14 1 653 . 140 VAL CB C 31.5 0.14 1 654 . 140 VAL N N 123.3 0.07 1 655 . 141 SER H H 8.42 0.01 1 656 . 141 SER C C 175.9 0.14 1 657 . 141 SER CA C 59.3 0.14 1 658 . 141 SER CB C 63.4 0.14 1 659 . 141 SER N N 119.5 0.07 1 660 . 142 GLN H H 8.26 0.01 1 661 . 142 GLN C C 177.3 0.14 1 662 . 142 GLN CA C 56.8 0.14 1 663 . 142 GLN CB C 27.8 0.14 1 664 . 142 GLN N N 122.0 0.07 1 665 . 143 ALA H H 7.89 0.01 1 666 . 143 ALA C C 179.3 0.14 1 667 . 143 ALA CA C 53.6 0.14 1 668 . 143 ALA CB C 18.0 0.14 1 669 . 143 ALA N N 122.9 0.07 1 670 . 144 GLN H H 8.11 0.01 1 671 . 144 GLN C C 177.5 0.14 1 672 . 144 GLN CA C 57.0 0.14 1 673 . 144 GLN CB C 27.9 0.14 1 674 . 144 GLN N N 117.8 0.07 1 675 . 145 ARG H H 7.87 0.01 1 676 . 145 ARG C C 176.9 0.14 1 677 . 145 ARG CA C 56.8 0.14 1 678 . 145 ARG CB C 29.6 0.14 1 679 . 145 ARG N N 119.8 0.07 1 680 . 146 GLN H H 7.78 0.01 1 681 . 146 GLN C C 176.1 0.14 1 682 . 146 GLN CA C 55.3 0.14 1 683 . 146 GLN CB C 28.1 0.14 1 684 . 146 GLN N N 118.5 0.07 1 685 . 147 ILE H H 7.59 0.01 1 686 . 147 ILE C C 176.6 0.14 1 687 . 147 ILE CA C 61.8 0.14 1 688 . 147 ILE CB C 37.2 0.14 1 689 . 147 ILE N N 120.9 0.07 1 690 . 148 LYS H H 8.15 0.01 1 691 . 148 LYS C C 176.4 0.14 1 692 . 148 LYS CA C 56.2 0.14 1 693 . 148 LYS CB C 31.6 0.14 1 694 . 148 LYS N N 124.9 0.07 1 695 . 149 ARG H H 7.41 0.01 1 696 . 149 ARG C C 175.8 0.14 1 697 . 149 ARG CA C 55.5 0.14 1 698 . 149 ARG CB C 30.3 0.14 1 699 . 149 ARG N N 118.9 0.07 1 700 . 150 GLY H H 7.86 0.01 1 701 . 150 GLY C C 172.2 0.14 1 702 . 150 GLY CA C 43.5 0.14 1 703 . 150 GLY N N 106.1 0.07 1 704 . 151 ALA H H 7.71 0.01 1 705 . 151 ALA CA C 50.1 0.14 1 706 . 151 ALA CB C 15.8 0.14 1 707 . 151 ALA N N 121.1 0.07 1 708 . 153 PRO C C 177.3 0.14 1 709 . 153 PRO CA C 61.8 0.14 1 710 . 153 PRO CB C 31.0 0.14 1 711 . 154 ARG H H 8.51 0.01 1 712 . 154 ARG C C 178.7 0.14 1 713 . 154 ARG CA C 55.2 0.14 1 714 . 154 ARG CB C 30.4 0.14 1 715 . 154 ARG N N 122.5 0.07 1 716 . 155 ARG H H 9.02 0.01 1 717 . 155 ARG C C 177.7 0.14 1 718 . 155 ARG CA C 57.9 0.14 1 719 . 155 ARG CB C 27.9 0.14 1 720 . 155 ARG N N 125.1 0.07 1 721 . 156 SER H H 7.61 0.01 1 722 . 156 SER C C 175.1 0.14 1 723 . 156 SER CA C 59.1 0.14 1 724 . 156 SER CB C 61.6 0.14 1 725 . 156 SER N N 111.2 0.07 1 726 . 157 SER H H 7.43 0.01 1 727 . 157 SER C C 173.8 0.14 1 728 . 157 SER CA C 58.8 0.14 1 729 . 157 SER CB C 64.3 0.14 1 730 . 157 SER N N 117.4 0.07 1 731 . 158 ILE H H 7.07 0.01 1 732 . 158 ILE C C 176.2 0.14 1 733 . 158 ILE CA C 61.5 0.14 1 734 . 158 ILE CB C 36.7 0.14 1 735 . 158 ILE N N 124.2 0.07 1 736 . 159 ARG H H 8.47 0.01 1 737 . 159 ARG C C 176.1 0.14 1 738 . 159 ARG CA C 55.7 0.14 1 739 . 159 ARG CB C 29.7 0.14 1 740 . 159 ARG N N 128.5 0.07 1 741 . 160 ASN H H 8.57 0.01 1 742 . 160 ASN C C 174.0 0.14 1 743 . 160 ASN CA C 52.8 0.14 1 744 . 160 ASN CB C 37.0 0.14 1 745 . 160 ASN N N 117.6 0.07 1 746 . 161 ALA H H 7.89 0.01 1 747 . 161 ALA C C 177.5 0.14 1 748 . 161 ALA CA C 51.8 0.14 1 749 . 161 ALA CB C 18.9 0.14 1 750 . 161 ALA N N 121.6 0.07 1 751 . 162 HIS H H 9.47 0.01 1 752 . 162 HIS C C 173.7 0.14 1 753 . 162 HIS CA C 55.2 0.14 1 754 . 162 HIS CB C 31.1 0.14 1 755 . 162 HIS N N 123.0 0.07 1 756 . 163 SER H H 8.27 0.01 1 757 . 163 SER C C 176.2 0.14 1 758 . 163 SER CA C 55.0 0.14 1 759 . 163 SER CB C 64.3 0.14 1 760 . 163 SER N N 119.8 0.07 1 761 . 164 ILE H H 8.98 0.01 1 762 . 164 ILE C C 175.7 0.14 1 763 . 164 ILE CA C 61.4 0.14 1 764 . 164 ILE CB C 37.1 0.14 1 765 . 164 ILE N N 123.9 0.07 1 766 . 165 HIS H H 8.52 0.01 1 767 . 165 HIS C C 175.9 0.14 1 768 . 165 HIS CA C 54.8 0.14 1 769 . 165 HIS CB C 32.2 0.14 1 770 . 165 HIS N N 123.3 0.07 1 771 . 166 GLN H H 8.80 0.01 1 772 . 166 GLN C C 175.8 0.14 1 773 . 166 GLN CA C 56.4 0.14 1 774 . 166 GLN CB C 28.2 0.14 1 775 . 166 GLN N N 121.6 0.07 1 776 . 167 ARG H H 7.64 0.01 1 777 . 167 ARG C C 175.3 0.14 1 778 . 167 ARG CA C 54.2 0.14 1 779 . 167 ARG CB C 30.7 0.14 1 780 . 167 ARG N N 117.2 0.07 1 781 . 168 SER H H 8.29 0.01 1 782 . 168 SER C C 174.7 0.14 1 783 . 168 SER CA C 57.4 0.14 1 784 . 168 SER CB C 64.3 0.14 1 785 . 168 SER N N 116.4 0.07 1 786 . 169 ARG H H 8.55 0.01 1 787 . 169 ARG C C 176.1 0.14 1 788 . 169 ARG CA C 55.5 0.14 1 789 . 169 ARG CB C 29.7 0.14 1 790 . 169 ARG N N 123.0 0.07 1 791 . 170 LYS H H 9.06 0.01 1 792 . 170 LYS C C 176.3 0.14 1 793 . 170 LYS CA C 56.5 0.14 1 794 . 170 LYS CB C 31.6 0.14 1 795 . 170 LYS N N 126.8 0.07 1 796 . 171 ARG H H 8.05 0.01 1 797 . 171 ARG C C 175.6 0.14 1 798 . 171 ARG CA C 54.2 0.14 1 799 . 171 ARG CB C 30.9 0.14 1 800 . 171 ARG N N 125.6 0.07 1 801 . 172 LEU H H 8.78 0.01 1 802 . 172 LEU C C 176.4 0.14 1 803 . 172 LEU CA C 54.9 0.14 1 804 . 172 LEU CB C 40.8 0.14 1 805 . 172 LEU N N 128.9 0.07 1 806 . 173 SER H H 8.18 0.01 1 807 . 173 SER C C 175.1 0.14 1 808 . 173 SER CA C 56.9 0.14 1 809 . 173 SER CB C 64.6 0.14 1 810 . 173 SER N N 116.5 0.07 1 811 . 174 GLN H H 9.19 0.01 1 812 . 174 GLN C C 178.3 0.14 1 813 . 174 GLN CA C 59.1 0.14 1 814 . 174 GLN CB C 27.3 0.14 1 815 . 174 GLN N N 120.6 0.07 1 816 . 175 ASP H H 8.40 0.01 1 817 . 175 ASP C C 177.6 0.14 1 818 . 175 ASP CA C 56.9 0.14 1 819 . 175 ASP CB C 40.6 0.14 1 820 . 175 ASP N N 117.6 0.07 1 821 . 176 ALA H H 7.77 0.01 1 822 . 176 ALA C C 180.3 0.14 1 823 . 176 ALA CA C 54.8 0.14 1 824 . 176 ALA CB C 17.9 0.14 1 825 . 176 ALA N N 124.0 0.07 1 826 . 177 TYR H H 8.17 0.01 1 827 . 177 TYR C C 179.0 0.14 1 828 . 177 TYR CA C 63.3 0.14 1 829 . 177 TYR CB C 38.0 0.14 1 830 . 177 TYR N N 117.7 0.07 1 831 . 178 ARG H H 8.24 0.01 1 832 . 178 ARG C C 178.4 0.14 1 833 . 178 ARG CA C 59.7 0.14 1 834 . 178 ARG CB C 29.1 0.14 1 835 . 178 ARG N N 119.6 0.07 1 836 . 179 ARG H H 8.42 0.01 1 837 . 179 ARG C C 179.7 0.14 1 838 . 179 ARG CA C 59.1 0.14 1 839 . 179 ARG CB C 29.1 0.14 1 840 . 179 ARG N N 119.4 0.07 1 841 . 180 ASN H H 8.19 0.01 1 842 . 180 ASN C C 177.4 0.14 1 843 . 180 ASN CA C 54.8 0.14 1 844 . 180 ASN CB C 37.0 0.14 1 845 . 180 ASN N N 118.2 0.07 1 846 . 181 SER H H 8.01 0.01 1 847 . 181 SER C C 175.5 0.14 1 848 . 181 SER CA C 61.8 0.14 1 849 . 181 SER CB C 63.0 0.14 1 850 . 181 SER N N 117.2 0.07 1 851 . 182 VAL H H 8.31 0.01 1 852 . 182 VAL C C 178.6 0.14 1 853 . 182 VAL CA C 66.1 0.14 1 854 . 182 VAL CB C 31.0 0.14 1 855 . 182 VAL N N 119.9 0.07 1 856 . 183 ARG H H 7.81 0.01 1 857 . 183 ARG C C 178.4 0.14 1 858 . 183 ARG CA C 58.6 0.14 1 859 . 183 ARG CB C 28.9 0.14 1 860 . 183 ARG N N 118.8 0.07 1 861 . 184 PHE H H 7.69 0.01 1 862 . 184 PHE C C 178.0 0.14 1 863 . 184 PHE CA C 61.0 0.14 1 864 . 184 PHE CB C 38.7 0.14 1 865 . 184 PHE N N 119.8 0.07 1 866 . 185 LEU H H 8.34 0.01 1 867 . 185 LEU C C 179.8 0.14 1 868 . 185 LEU CA C 57.0 0.14 1 869 . 185 LEU CB C 40.6 0.14 1 870 . 185 LEU N N 120.0 0.07 1 871 . 186 GLN H H 8.24 0.01 1 872 . 186 GLN C C 178.1 0.14 1 873 . 186 GLN CA C 57.8 0.14 1 874 . 186 GLN CB C 27.7 0.14 1 875 . 186 GLN N N 118.6 0.07 1 876 . 187 GLN H H 7.64 0.01 1 877 . 187 GLN C C 177.3 0.14 1 878 . 187 GLN CA C 56.9 0.14 1 879 . 187 GLN CB C 27.9 0.14 1 880 . 187 GLN N N 118.1 0.07 1 881 . 188 ARG H H 7.65 0.01 1 882 . 188 ARG C C 177.2 0.14 1 883 . 188 ARG CA C 56.8 0.14 1 884 . 188 ARG CB C 29.6 0.14 1 885 . 188 ARG N N 119.8 0.07 1 886 . 189 ARG H H 7.82 0.01 1 887 . 189 ARG C C 176.8 0.14 1 888 . 189 ARG CA C 56.5 0.14 1 889 . 189 ARG CB C 29.5 0.14 1 890 . 189 ARG N N 120.0 0.07 1 891 . 190 ARG H H 7.93 0.01 1 892 . 190 ARG C C 176.4 0.14 1 893 . 190 ARG CA C 56.2 0.14 1 894 . 190 ARG CB C 29.6 0.14 1 895 . 190 ARG N N 121.0 0.07 1 896 . 191 GLN H H 8.10 0.01 1 897 . 191 GLN C C 175.5 0.14 1 898 . 191 GLN CA C 55.4 0.14 1 899 . 191 GLN CB C 28.7 0.14 1 900 . 191 GLN N N 121.0 0.07 1 901 . 192 ALA H H 8.15 0.01 1 902 . 192 ALA C C 176.6 0.14 1 903 . 192 ALA CA C 52.2 0.14 1 904 . 192 ALA CB C 18.5 0.14 1 905 . 192 ALA N N 126.1 0.07 1 906 . 193 ARG H H 7.82 0.01 1 907 . 193 ARG CA C 57.0 0.14 1 908 . 193 ARG CB C 30.6 0.14 1 909 . 193 ARG N N 125.7 0.07 1 stop_ save_