data_4264 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Complex of the amino terminal domain of enzyme I and the histidine-containing phosphocarrier protein HPr from Escherichia coli nmr, restrained regularized mean structure ; _BMRB_accession_number 4264 _BMRB_flat_file_name bmr4264.str _Entry_type original _Submission_date 1998-11-04 _Accession_date 1998-11-04 _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 Clore G. M. . 2 Garrett D. S. . 3 Gronenborn A. M. . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 4 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 1799 "13C chemical shifts" 2194 "15N chemical shifts" 696 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2000-05-02 original author . stop_ _Original_release_date 2000-05-02 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; Solution structure of the 40,000 Mr phosphoryl transfer complex between the N-terminal domain of enzyme I and HPr. ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code 99140298 _PubMed_ID ? loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 GARRETT D. S. . 2 SEOK Y. J. . 3 PETERKOFSKY A. . . 4 GRONENBORN A. M. . 5 CLORE G. M. . stop_ _Journal_abbreviation 'Nat. Struct. Biol.' _Journal_name_full 'Nature Structural Biology' _Journal_volume 6 _Journal_issue . _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 166 _Page_last 173 _Year 1999 _Details . loop_ _Keyword PHOSPHOTRANSFERASE TRANSFERASE KINASE 'SUGAR TRANSPORT' stop_ save_ ################################## # Molecular system description # ################################## save_system_HPR _Saveframe_category molecular_system _Mol_system_name 'Phosphotransferase system, enzyme I' _Abbreviation_common HPR _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'Enzyme I, N-terminal' $EIN 'Histidine Phosphocarrier' $HPr stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state monomer _System_paramagnetic no _System_thiol_state 'not present' _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_EIN _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'Enzyme I, N-terminal' _Molecular_mass . _Mol_thiol_state 'not present' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 259 _Mol_residue_sequence ; MISGILASPGIAFGKALLLK EDEIVIDRKKISADQVDQEV ERFLSGRAKASAQLETIKTK AGETFGEEKEAIFEGHIMLL EDEELEQEIIALIKDKHMTA DAAAHEVIEGQASALEELDD EYLKERAADVRDIGKRLLRN ILGLKIIDLSAIQDEVILVA ADLTPSETAQLNLKKVLGFI TDAGGRTSHTSIMARSLELP AIVGTGSVTSQVKNDDYLIL DAVNNQVYVNPTNEVIDKMR AVQEQVASEKAELAKLKDR ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 1 MET 2 2 ILE 3 3 SER 4 4 GLY 5 5 ILE 6 6 LEU 7 7 ALA 8 8 SER 9 9 PRO 10 10 GLY 11 11 ILE 12 12 ALA 13 13 PHE 14 14 GLY 15 15 LYS 16 16 ALA 17 17 LEU 18 18 LEU 19 19 LEU 20 20 LYS 21 21 GLU 22 22 ASP 23 23 GLU 24 24 ILE 25 25 VAL 26 26 ILE 27 27 ASP 28 28 ARG 29 29 LYS 30 30 LYS 31 31 ILE 32 32 SER 33 33 ALA 34 34 ASP 35 35 GLN 36 36 VAL 37 37 ASP 38 38 GLN 39 39 GLU 40 40 VAL 41 41 GLU 42 42 ARG 43 43 PHE 44 44 LEU 45 45 SER 46 46 GLY 47 47 ARG 48 48 ALA 49 49 LYS 50 50 ALA 51 51 SER 52 52 ALA 53 53 GLN 54 54 LEU 55 55 GLU 56 56 THR 57 57 ILE 58 58 LYS 59 59 THR 60 60 LYS 61 61 ALA 62 62 GLY 63 63 GLU 64 64 THR 65 65 PHE 66 66 GLY 67 67 GLU 68 68 GLU 69 69 LYS 70 70 GLU 71 71 ALA 72 72 ILE 73 73 PHE 74 74 GLU 75 75 GLY 76 76 HIS 77 77 ILE 78 78 MET 79 79 LEU 80 80 LEU 81 81 GLU 82 82 ASP 83 83 GLU 84 84 GLU 85 85 LEU 86 86 GLU 87 87 GLN 88 88 GLU 89 89 ILE 90 90 ILE 91 91 ALA 92 92 LEU 93 93 ILE 94 94 LYS 95 95 ASP 96 96 LYS 97 97 HIS 98 98 MET 99 99 THR 100 100 ALA 101 101 ASP 102 102 ALA 103 103 ALA 104 104 ALA 105 105 HIS 106 106 GLU 107 107 VAL 108 108 ILE 109 109 GLU 110 110 GLY 111 111 GLN 112 112 ALA 113 113 SER 114 114 ALA 115 115 LEU 116 116 GLU 117 117 GLU 118 118 LEU 119 119 ASP 120 120 ASP 121 121 GLU 122 122 TYR 123 123 LEU 124 124 LYS 125 125 GLU 126 126 ARG 127 127 ALA 128 128 ALA 129 129 ASP 130 130 VAL 131 131 ARG 132 132 ASP 133 133 ILE 134 134 GLY 135 135 LYS 136 136 ARG 137 137 LEU 138 138 LEU 139 139 ARG 140 140 ASN 141 141 ILE 142 142 LEU 143 143 GLY 144 144 LEU 145 145 LYS 146 146 ILE 147 147 ILE 148 148 ASP 149 149 LEU 150 150 SER 151 151 ALA 152 152 ILE 153 153 GLN 154 154 ASP 155 155 GLU 156 156 VAL 157 157 ILE 158 158 LEU 159 159 VAL 160 160 ALA 161 161 ALA 162 162 ASP 163 163 LEU 164 164 THR 165 165 PRO 166 166 SER 167 167 GLU 168 168 THR 169 169 ALA 170 170 GLN 171 171 LEU 172 172 ASN 173 173 LEU 174 174 LYS 175 175 LYS 176 176 VAL 177 177 LEU 178 178 GLY 179 179 PHE 180 180 ILE 181 181 THR 182 182 ASP 183 183 ALA 184 184 GLY 185 185 GLY 186 186 ARG 187 187 THR 188 188 SER 189 189 HIS 190 190 THR 191 191 SER 192 192 ILE 193 193 MET 194 194 ALA 195 195 ARG 196 196 SER 197 197 LEU 198 198 GLU 199 199 LEU 200 200 PRO 201 201 ALA 202 202 ILE 203 203 VAL 204 204 GLY 205 205 THR 206 206 GLY 207 207 SER 208 208 VAL 209 209 THR 210 210 SER 211 211 GLN 212 212 VAL 213 213 LYS 214 214 ASN 215 215 ASP 216 216 ASP 217 217 TYR 218 218 LEU 219 219 ILE 220 220 LEU 221 221 ASP 222 222 ALA 223 223 VAL 224 224 ASN 225 225 ASN 226 226 GLN 227 227 VAL 228 228 TYR 229 229 VAL 230 230 ASN 231 231 PRO 232 232 THR 233 233 ASN 234 234 GLU 235 235 VAL 236 236 ILE 237 237 ASP 238 238 LYS 239 239 MET 240 240 ARG 241 241 ALA 242 242 VAL 243 243 GLN 244 244 GLU 245 245 GLN 246 246 VAL 247 247 ALA 248 248 SER 249 249 GLU 250 250 LYS 251 251 ALA 252 252 GLU 253 253 LEU 254 254 ALA 255 255 LYS 256 256 LEU 257 257 LYS 258 258 ASP 259 259 ARG stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-11-24 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 17095 EIN 100.00 259 100.00 100.00 0.00e+00 BMRB 19958 N-terminal_Domain_of_Enzyme_I 100.00 259 100.00 100.00 0.00e+00 BMRB 25731 entity 99.61 573 100.00 100.00 6.45e-175 BMRB 4106 "N-terminal Domain of Enzyme I" 100.00 259 100.00 100.00 0.00e+00 PDB 1EZA "Amino Terminal Domain Of Enzyme I From Escherichia Coli Nmr, Restrained Regularized Mean Structure" 100.00 259 100.00 100.00 0.00e+00 PDB 1EZB "Amino Terminal Domain Of Enzyme I From Escherichia Coli, Nmr, 17 Structures" 100.00 259 100.00 100.00 0.00e+00 PDB 1EZC "Amino Terminal Domain Of Enzyme I From Escherichia Coli, Nmr, 17 Structures" 100.00 259 100.00 100.00 0.00e+00 PDB 1EZD "Amino Terminal Domain Of Enzyme I From Escherichia Coli Nmr, 16 Structures" 100.00 259 100.00 100.00 0.00e+00 PDB 1ZYM "Amino Terminal Domain Of Enzyme I From Escherichia Coli" 99.61 258 100.00 100.00 4.13e-180 PDB 2EZA "Amino Terminal Domain Of Enzyme I From Escherichia Coli, Nmr, Restrained Regularized Mean Structure" 100.00 259 100.00 100.00 0.00e+00 PDB 2EZB "Amino Terminal Domain Of Enzyme I From Escherichia Coli, Nmr, 14 Structures" 100.00 259 100.00 100.00 0.00e+00 PDB 2EZC "Amino Terminal Domain Of Enzyme I From Escherichia Coli, Nmr, 14 Structures" 100.00 259 100.00 100.00 0.00e+00 PDB 2HWG "Structure Of Phosphorylated Enzyme I Of The Phosphoenolpyruvate:sugar Phosphotransferase System" 99.23 575 98.05 98.05 9.40e-168 PDB 2KX9 "Solution Structure Of The Enzyme I Dimer Using Residual Dipolar Couplings And Small Angle X-Ray Scattering" 99.61 573 100.00 100.00 6.45e-175 PDB 2L5H "Solution Structure Of The H189q Mutant Of The Enzyme I Dimer Using Residual Dipolar Couplings And Small Angle X-Ray Scattering" 99.61 573 99.61 99.61 1.08e-173 PDB 2MP0 "Protein Phosphorylation Upon A Fleeting Encounter" 99.61 258 100.00 100.00 4.13e-180 PDB 2N5T "Ensemble Solution Structure Of The Phosphoenolpyruvate-enzyme I Complex From The Bacterial Hosphotransferase System" 99.61 575 100.00 100.00 7.04e-175 PDB 2XDF "Solution Structure Of The Enzyme I Dimer Complexed With Hpr Using Residual Dipolar Couplings And Small Angle X-Ray Scattering" 99.61 573 100.00 100.00 6.45e-175 PDB 3EZA "Complex Of The Amino Terminal Domain Of Enzyme I And The Histidine-Containing Phosphocarrier Protein Hpr From Escherichia Coli " 96.14 249 100.00 100.00 2.96e-174 PDB 3EZB "Complex Of The Amino Terminal Domain Of Enzyme I And The Histidine-Containing Phosphocarrier Protein Hpr From Escherichia Coli" 100.00 259 100.00 100.00 0.00e+00 PDB 3EZE "Complex Of The Amino Terminal Domain Of Enzyme I And The Histidine-Containing Phosphocarrier Protein Hpr From Escherichia Coli " 100.00 259 100.00 100.00 0.00e+00 DBJ BAA16290 "PEP-protein phosphotransferase of PTS system [Escherichia coli str. K12 substr. W3110]" 99.61 575 100.00 100.00 7.04e-175 DBJ BAB36711 "PEP-protein phosphotransferase system enzyme I [Escherichia coli O157:H7 str. Sakai]" 99.61 575 100.00 100.00 5.72e-175 DBJ BAG78231 "PTS system enzyme I [Escherichia coli SE11]" 99.61 575 100.00 100.00 5.72e-175 DBJ BAI26669 "PEP-protein phosphotransferase PtsI [Escherichia coli O26:H11 str. 11368]" 99.61 575 100.00 100.00 5.72e-175 DBJ BAI31701 "PEP-protein phosphotransferase PtsI [Escherichia coli O103:H2 str. 12009]" 99.61 575 100.00 100.00 5.72e-175 EMBL CAP76888 "Phosphoenolpyruvate-protein phosphotransferase [Escherichia coli LF82]" 99.61 575 100.00 100.00 5.72e-175 EMBL CAQ32794 "PTS enzyme I, subunit of EIIAsc, EIIBgl, EIIChb, CmtAB mannitol PTS permease, enzyme II [glc], fructose PTS transporter, EIIABC" 99.61 575 100.00 100.00 5.72e-175 EMBL CAQ88296 "PEP-protein phosphotransferase of PTS system (enzyme I) [Escherichia fergusonii ATCC 35469]" 99.61 575 98.06 99.22 1.65e-171 EMBL CAQ99314 "PEP-protein phosphotransferase of PTS system (enzyme I) [Escherichia coli IAI1]" 99.61 575 100.00 100.00 5.72e-175 EMBL CAR03878 "PEP-protein phosphotransferase of PTS system (enzyme I) [Escherichia coli S88]" 99.61 575 100.00 100.00 5.25e-175 GB AAA24385 "enzyme I [Escherichia coli]" 99.61 575 100.00 100.00 7.04e-175 GB AAA24441 "enzyme I [Escherichia coli]" 99.61 575 100.00 100.00 7.04e-175 GB AAC75469 "PEP-protein phosphotransferase of PTS system (enzyme I) [Escherichia coli str. K-12 substr. MG1655]" 99.61 575 100.00 100.00 7.04e-175 GB AAG57535 "PEP-protein phosphotransferase system enzyme I [Escherichia coli O157:H7 str. EDL933]" 99.61 575 100.00 100.00 5.72e-175 GB AAN43978 "PEP-protein phosphotransferase system enzyme I [Shigella flexneri 2a str. 301]" 99.61 575 100.00 100.00 5.72e-175 REF NP_311315 "phosphoenolpyruvate-protein phosphotransferase [Escherichia coli O157:H7 str. Sakai]" 99.61 575 100.00 100.00 5.72e-175 REF NP_416911 "PEP-protein phosphotransferase of PTS system (enzyme I) [Escherichia coli str. K-12 substr. MG1655]" 99.61 575 100.00 100.00 7.04e-175 REF NP_708271 "phosphoenolpyruvate-protein phosphotransferase [Shigella flexneri 2a str. 301]" 99.61 575 100.00 100.00 5.72e-175 REF WP_000112669 "phosphoenolpyruvate--protein phosphotransferase, partial [Escherichia coli]" 85.71 539 100.00 100.00 2.00e-148 REF WP_000328837 "phosphoenolpyruvate--protein phosphotransferase, partial [Escherichia coli]" 52.90 454 100.00 100.00 2.57e-85 SP P08839 "RecName: Full=Phosphoenolpyruvate-protein phosphotransferase; AltName: Full=Phosphotransferase system, enzyme I" 99.61 575 100.00 100.00 7.04e-175 stop_ save_ save_HPr _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'Histidine Phosphocarrier' _Molecular_mass . _Mol_thiol_state 'not present' _Details . _Residue_count 85 _Mol_residue_sequence ; MFQQEVTITAPNGLHTRPAA QFVKEAKGFTSEITVTSNGK SASAKSLFKLQTLGLTQGTV VTISAEGEDEQKAVEHLVKL MAELE ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 301 MET 2 302 PHE 3 303 GLN 4 304 GLN 5 305 GLU 6 306 VAL 7 307 THR 8 308 ILE 9 309 THR 10 310 ALA 11 311 PRO 12 312 ASN 13 313 GLY 14 314 LEU 15 315 HIS 16 316 THR 17 317 ARG 18 318 PRO 19 319 ALA 20 320 ALA 21 321 GLN 22 322 PHE 23 323 VAL 24 324 LYS 25 325 GLU 26 326 ALA 27 327 LYS 28 328 GLY 29 329 PHE 30 330 THR 31 331 SER 32 332 GLU 33 333 ILE 34 334 THR 35 335 VAL 36 336 THR 37 337 SER 38 338 ASN 39 339 GLY 40 340 LYS 41 341 SER 42 342 ALA 43 343 SER 44 344 ALA 45 345 LYS 46 346 SER 47 347 LEU 48 348 PHE 49 349 LYS 50 350 LEU 51 351 GLN 52 352 THR 53 353 LEU 54 354 GLY 55 355 LEU 56 356 THR 57 357 GLN 58 358 GLY 59 359 THR 60 360 VAL 61 361 VAL 62 362 THR 63 363 ILE 64 364 SER 65 365 ALA 66 366 GLU 67 367 GLY 68 368 GLU 69 369 ASP 70 370 GLU 71 371 GLN 72 372 LYS 73 373 ALA 74 374 VAL 75 375 GLU 76 376 HIS 77 377 LEU 78 378 VAL 79 379 LYS 80 380 LEU 81 381 MET 82 382 ALA 83 383 GLU 84 384 LEU 85 385 GLU stop_ _Sequence_homology_query_date 2008-08-19 _Sequence_homology_query_revised_last_date 2008-08-19 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 SWISS-PROT P0AA07 'Phosphocarrier protein HPr (Histidine-containing protein)' 100.00 85 100.00 100.00 8.74e-41 SWISS-PROT P0AA08 'Phosphocarrier protein HPr (Histidine-containing protein)' 100.00 85 100.00 100.00 8.74e-41 SWISS-PROT P0AA05 'Phosphocarrier protein HPr (Histidine-containing protein)' 100.00 85 100.00 100.00 8.74e-41 SWISS-PROT P0AA06 'Phosphocarrier protein HPr (Histidine-containing protein)' 100.00 85 100.00 100.00 8.74e-41 REF NP_456968 'phosphohistidinoprotein-hexose phosphotransferase component of PTS system (Hpr) [Salmonella enterica subsp. enterica serovar Typhi str. CT18]' 100.00 85 100.00 100.00 8.74e-41 SWISS-PROT P0AA04 'Phosphocarrier protein HPr (Histidine-containing protein)' 100.00 85 100.00 100.00 8.74e-41 REF NP_311314 'phosphohistidinoprotein-hexose phosphotransferase component of PTS system (Hpr) [Escherichia coli O157:H7 str. Sakai]' 100.00 85 100.00 100.00 8.74e-41 REF NP_416910 'phosphohistidinoprotein-hexose phosphotransferase component of PTS system (Hpr) [Escherichia coli str. K-12 substr. MG1655]' 100.00 85 100.00 100.00 8.74e-41 REF AP_003009 'phosphohistidinoprotein-hexose phosphotransferase component of PTS system (Hpr) [Escherichia coli W3110]' 100.00 85 100.00 100.00 8.74e-41 REF NP_288977 'phosphohistidinoprotein-hexose phosphotransferase component of PTS system (Hpr) [Escherichia coli O157:H7 EDL933]' 100.00 85 100.00 100.00 8.74e-41 PIR AE0810 'phosphocarrier protein HPr [imported] - Salmonella enterica subsp. enterica serovar Typhi (strain CT18)' 100.00 85 100.00 100.00 8.74e-41 PRF 1107231B 'protein,His containing' 100.00 85 100.00 100.00 8.74e-41 GenBank AAA24440 HPr 100.00 85 100.00 100.00 8.74e-41 GenBank AAA27052 'ptsH protein' 100.00 85 100.00 100.00 8.74e-41 GenBank AAA24384 'HPr protein (EC 2.7.1.68)' 100.00 85 100.00 100.00 8.74e-41 GenBank AAA24438 'histidine-containing protein' 100.00 85 100.00 100.00 8.74e-41 EMBL CAD07663 'phosphocarrier protein HPr [Salmonella enterica subsp. enterica serovar Typhi]' 100.00 85 100.00 100.00 8.74e-41 GenBank AAA23655 'ptsH protein' 100.00 85 100.00 100.00 8.74e-41 EMBL CAA32865 'unnamed protein product [Salmonella typhimurium]' 100.00 85 100.00 100.00 8.74e-41 EMBL CAA35818 'unnamed protein product [Klebsiella pneumoniae]' 100.00 85 98.82 100.00 1.98e-40 DBJ BAB36710 'PTS system protein HPr [Escherichia coli O157:H7 str. Sakai]' 100.00 85 100.00 100.00 8.74e-41 DBJ BAB92987 'HPr of PTS system [Serratia marcescens]' 100.00 85 98.82 100.00 1.79e-40 PDB 3EZE 'Complex Of The Amino Terminal Domain Of Enzyme I And The Histidine-Containing Phosphocarrier Protein Hpr From Escherichia Coli Nmr, Restrained Regularized Mean Structure' 100.00 85 100.00 100.00 8.74e-41 DBJ BAA16289 'phosphohistidinoprotein-hexose phosphotransferase component of PTS system (Hpr) [Escherichia coli W3110]' 100.00 85 100.00 100.00 8.74e-41 PDB 3EZA 'Complex Of The Amino Terminal Domain Of Enzyme I And The Histidine-Containing Phosphocarrier Protein Hpr From Escherichia Coli Nmr, Restrained Regularized Mean Structure' 100.00 85 100.00 100.00 8.74e-41 PDB 3EZB 'Complex Of The Amino Terminal Domain Of Enzyme I And The Histidine-Containing Phosphocarrier Protein Hpr From Escherichia Coli' 100.00 85 100.00 100.00 8.74e-41 PDB 1VRC 'Complex Of Enzyme Iiamannose And The Histidine-Containing Phosphocarrier Protein Hpr From Escherichia Coli Nmr, Restrained Regularized Mean Structure' 100.00 85 100.00 100.00 8.74e-41 PDB 2JEL 'Jel42 FabHPR COMPLEX' 100.00 85 100.00 100.00 8.74e-41 PDB 1PFH 'The Phosphorylated Form Of The Histidine-Containing Phosphocarrier Protein Hpr' 100.00 85 100.00 100.00 8.74e-41 PDB 1POH 'The 2.0 Angstroms Resolution Structure Of Escherichia Coli Histidine-Containing Phosphocarrier Protein Hpr: A Redetermination' 100.00 85 100.00 100.00 8.74e-41 PDB 1HDN 'The High-Resolution Structure Of The Histidine-Containing Phosphocarrier Protein Hpr From Escherichia Coli Determined By Restrained Molecular Dynamics From Nmr Nuclear Overhauser Effect Data' 100.00 85 100.00 100.00 8.74e-41 PDB 1J6T 'Complex Of Enzyme Iiamtl And The Histidine-Containing Phosphocarrier Protein Hpr From Escherichia Coli Nmr, Restrained Regularized Mean Structure' 100.00 85 100.00 100.00 8.74e-41 PDB 1CM3 'His15asp Hpr From E. Coli' 100.00 85 98.82 98.82 8.11e-40 PDB 1GGR 'Complex Of Enzyme Iiaglc And The Histidine-Containing Phosphocarrier Protein Hpr From Escherichia Coli Nmr, Restrained Regularized Mean Structure' 100.00 85 100.00 100.00 8.74e-41 BMRB 29 'phosphocarrier protein HPr' 100.00 85 100.00 100.00 8.74e-41 PDB 1CM2 'Structure Of His15asp Hpr After Hydrolysis Of Ringed Species.' 100.00 85 98.82 98.82 8.11e-40 BMRB 2060 'phosphocarrier protein HPr' 100.00 85 100.00 100.00 8.74e-41 BMRB 2371 'phosphocarrier protein HPr' 100.00 85 100.00 100.00 8.74e-41 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species _Strain _Plasmid $EIN 'E. coli' 562 Eubacteria . Escherichia coli GI698 PLP2 $HPr 'E. coli' 562 Euacteria . Escherichia coli GI698 PSP100 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 $EIN 'recombinant technology' 'E. Coli' Escherichia coli . . $HPr 'recombinant technology' 'E. Coli' Escherichia coli . . stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_one _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $EIN . mM . $HPr . mM . D2O . % . H2O . % . stop_ save_ save_sample_two _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $EIN . mM [U-2H] $HPr . mM [U-2H] D2O . % . H2O . % . stop_ save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer-1 _Saveframe_category NMR_spectrometer _Manufacturer BRUKER _Model DMX _Field_strength 500 _Details . save_ save_NMR_spectrometer-2 _Saveframe_category NMR_spectrometer _Manufacturer BRUKER _Model DMX _Field_strength 600 _Details . save_ save_NMR_spectrometer-3 _Saveframe_category NMR_spectrometer _Manufacturer BRUKER _Model DMX _Field_strength 750 _Details . save_ ############################# # NMR applied experiments # ############################# save_(1)_TRIPLE_RESONANCE_FOR_ASSIGNMENT_OF_PROTEIN._1 _Saveframe_category NMR_applied_experiment _Experiment_name '(1) TRIPLE RESONANCE FOR ASSIGNMENT OF PROTEIN.' _Sample_label . save_ save_(2)_QUANTITATIVE_J_CORRELATION_FOR_COUPLING_CONSTANTS._2 _Saveframe_category NMR_applied_experiment _Experiment_name '(2) QUANTITATIVE J CORRELATION FOR COUPLING CONSTANTS.' _Sample_label . save_ save_(3)_3D_AND_4D_HETERONUCLEAR_SEPARATED_AND_FILTERED_NOE_E_3 _Saveframe_category NMR_applied_experiment _Experiment_name '(3) 3D AND 4D HETERONUCLEAR SEPARATED AND FILTERED NOE E' _Sample_label . save_ save_(4)_IPAP_EXPTS_FOR_DIPOLAR_COUPLINGS_DIPOLAR_COUPLINGS_WERE_MEASURED_IN_A_4 _Saveframe_category NMR_applied_experiment _Experiment_name '(4) IPAP EXPTS FOR DIPOLAR COUPLINGS DIPOLAR COUPLINGS WERE MEASURED IN A' _Sample_label . save_ save_NEMATIC_PHASE_OF_A_CO_SUSPENSION_OF_PHAGE_FD_(CLORE_ET_AL._1998_J._AM._CHEM._5 _Saveframe_category NMR_applied_experiment _Experiment_name 'NEMATIC PHASE OF A CO SUSPENSION OF PHAGE FD (CLORE ET AL. 1998 J. AM. CHEM.' _Sample_label . save_ save_SOC"_6 _Saveframe_category NMR_applied_experiment _Experiment_name SOC" _Sample_label . save_ save_NMR_spec_expt__0_1 _Saveframe_category NMR_applied_experiment _Experiment_name '(1) TRIPLE RESONANCE FOR ASSIGNMENT OF PROTEIN.' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_2 _Saveframe_category NMR_applied_experiment _Experiment_name '(2) QUANTITATIVE J CORRELATION FOR COUPLING CONSTANTS.' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_3 _Saveframe_category NMR_applied_experiment _Experiment_name '(3) 3D AND 4D HETERONUCLEAR SEPARATED AND FILTERED NOE E' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_4 _Saveframe_category NMR_applied_experiment _Experiment_name '(4) IPAP EXPTS FOR DIPOLAR COUPLINGS DIPOLAR COUPLINGS WERE MEASURED IN A' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_5 _Saveframe_category NMR_applied_experiment _Experiment_name 'NEMATIC PHASE OF A CO SUSPENSION OF PHAGE FD (CLORE ET AL. 1998 J. AM. CHEM.' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_6 _Saveframe_category NMR_applied_experiment _Experiment_name SOC" _BMRB_pulse_sequence_accession_number . _Details . save_ ####################### # Sample conditions # ####################### save_sample_cond_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 7.0 . n/a temperature 313 . K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference_one _Saveframe_category chemical_shift_reference _Details . 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_chemical_shift_assignment_1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Sample_label $sample_one stop_ _Sample_conditions_label $sample_cond_1 _Chem_shift_reference_set_label $chemical_shift_reference_one _Mol_system_component_name 'Enzyme I, N-terminal' _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 MET HA H 4.11 0.03 1 2 . 1 MET HB3 H 2.05 0.03 2 3 . 1 MET CA C 55.99 0.50 1 4 . 1 MET CB C 33.15 0.50 1 5 . 2 ILE HA H 4.24 0.03 1 6 . 2 ILE HB H 1.63 0.03 1 7 . 2 ILE HD1 H 0.44 0.03 1 8 . 2 ILE HG13 H 1.07 0.03 2 9 . 2 ILE HG12 H 0.81 0.03 2 10 . 2 ILE HG2 H 0.65 0.03 1 11 . 2 ILE CA C 61.60 0.50 1 12 . 2 ILE CB C 40.09 0.50 1 13 . 2 ILE CD1 C 11.78 0.50 1 14 . 2 ILE CG1 C 27.15 0.50 1 15 . 2 ILE CG2 C 17.60 0.50 1 16 . 3 SER HA H 4.23 0.03 1 17 . 3 SER HB3 H 3.67 0.03 2 18 . 3 SER HB2 H 3.63 0.03 2 19 . 3 SER H H 8.14 0.03 1 20 . 3 SER C C 173.12 0.50 1 21 . 3 SER CA C 57.14 0.50 1 22 . 3 SER CB C 66.46 0.50 1 23 . 3 SER N N 119.60 0.25 1 24 . 4 GLY HA3 H 3.31 0.03 2 25 . 4 GLY HA2 H 4.21 0.03 2 26 . 4 GLY H H 8.61 0.03 1 27 . 4 GLY CA C 46.92 0.50 1 28 . 4 GLY N N 108.17 0.25 1 29 . 5 ILE HA H 4.11 0.03 1 30 . 5 ILE HB H 1.52 0.03 1 31 . 5 ILE HD1 H 0.90 0.03 1 32 . 5 ILE HG13 H 1.11 0.03 2 33 . 5 ILE HG2 H 0.62 0.03 1 34 . 5 ILE H H 9.50 0.03 1 35 . 5 ILE C C 175.42 0.50 1 36 . 5 ILE CA C 60.01 0.50 1 37 . 5 ILE CB C 39.29 0.50 1 38 . 5 ILE CD1 C 13.74 0.50 1 39 . 5 ILE CG2 C 16.83 0.50 1 40 . 5 ILE N N 130.61 0.25 1 41 . 6 LEU HA H 4.04 0.03 1 42 . 6 LEU HB3 H 1.72 0.03 2 43 . 6 LEU HB2 H 1.41 0.03 2 44 . 6 LEU HD1 H 0.67 0.03 2 45 . 6 LEU HD2 H 0.80 0.03 2 46 . 6 LEU HG H 1.56 0.03 1 47 . 6 LEU H H 8.71 0.03 1 48 . 6 LEU C C 175.20 0.50 1 49 . 6 LEU CA C 55.85 0.50 1 50 . 6 LEU CB C 40.95 0.50 1 51 . 6 LEU CD1 C 23.55 0.50 2 52 . 6 LEU CD2 C 25.92 0.50 2 53 . 6 LEU CG C 25.95 0.50 1 54 . 6 LEU N N 127.83 0.25 1 55 . 7 ALA HA H 4.25 0.03 1 56 . 7 ALA HB H 1.25 0.03 1 57 . 7 ALA H H 7.94 0.03 1 58 . 7 ALA C C 176.88 0.50 1 59 . 7 ALA CA C 53.50 0.50 1 60 . 7 ALA CB C 21.57 0.50 1 61 . 7 ALA N N 130.30 0.25 1 62 . 8 SER HA H 4.84 0.03 1 63 . 8 SER HB2 H 3.58 0.03 2 64 . 8 SER H H 7.57 0.03 1 65 . 8 SER CB C 64.69 0.50 1 66 . 8 SER N N 110.95 0.25 1 67 . 9 PRO HA H 4.96 0.03 1 68 . 9 PRO HB3 H 1.93 0.03 2 69 . 9 PRO HB2 H 2.37 0.03 2 70 . 9 PRO C C 176.17 0.50 1 71 . 9 PRO CA C 63.24 0.50 1 72 . 9 PRO CB C 33.76 0.50 1 73 . 10 GLY H H 6.33 0.03 1 74 . 10 GLY CA C 44.08 0.50 1 75 . 10 GLY N N 104.09 0.25 1 76 . 11 ILE HA H 5.38 0.03 1 77 . 11 ILE HB H 1.67 0.03 1 78 . 11 ILE HD1 H 0.77 0.03 1 79 . 11 ILE HG13 H 1.03 0.03 2 80 . 11 ILE HG2 H 0.66 0.03 1 81 . 11 ILE H H 8.52 0.03 1 82 . 11 ILE C C 174.24 0.50 1 83 . 11 ILE CA C 59.85 0.50 1 84 . 11 ILE CB C 41.56 0.50 1 85 . 11 ILE CD1 C 14.62 0.50 1 86 . 11 ILE CG1 C 28.87 0.50 1 87 . 11 ILE CG2 C 17.68 0.50 1 88 . 11 ILE N N 117.64 0.25 1 89 . 12 ALA HA H 4.96 0.03 1 90 . 12 ALA HB H 1.17 0.03 1 91 . 12 ALA H H 8.49 0.03 1 92 . 12 ALA CA C 50.52 0.50 1 93 . 12 ALA CB C 23.98 0.50 1 94 . 12 ALA N N 127.20 0.25 1 95 . 13 PHE HA H 5.04 0.03 1 96 . 13 PHE HB3 H 3.19 0.03 2 97 . 13 PHE HD1 H 7.24 0.03 2 98 . 13 PHE HE1 H 7.08 0.03 2 99 . 13 PHE H H 8.53 0.03 1 100 . 13 PHE HZ H 6.81 0.03 1 101 . 13 PHE C C 175.29 0.50 1 102 . 13 PHE CA C 55.44 0.50 1 103 . 13 PHE CB C 41.29 0.50 1 104 . 13 PHE CD1 C 132.56 0.50 2 105 . 13 PHE CE1 C 131.20 0.50 2 106 . 13 PHE CZ C 128.56 0.50 1 107 . 13 PHE N N 120.61 0.25 1 108 . 14 GLY HA3 H 3.73 0.03 2 109 . 14 GLY HA2 H 3.92 0.03 2 110 . 14 GLY H H 8.18 0.03 1 111 . 14 GLY C C 180.44 0.50 1 112 . 14 GLY CA C 45.79 0.50 1 113 . 14 GLY N N 107.60 0.25 1 114 . 15 LYS HA H 4.72 0.03 1 115 . 15 LYS HB3 H 1.70 0.03 2 116 . 15 LYS HB2 H 1.77 0.03 2 117 . 15 LYS HD3 H 1.74 0.03 2 118 . 15 LYS HE3 H 2.98 0.03 2 119 . 15 LYS HG3 H 1.53 0.03 2 120 . 15 LYS H H 8.41 0.03 1 121 . 15 LYS C C 175.78 0.50 1 122 . 15 LYS CA C 55.70 0.50 1 123 . 15 LYS CB C 34.73 0.50 1 124 . 15 LYS CD C 30.02 0.50 1 125 . 15 LYS CG C 25.58 0.50 1 126 . 15 LYS N N 118.50 0.25 1 127 . 16 ALA HA H 4.59 0.03 1 128 . 16 ALA HB H 1.20 0.03 1 129 . 16 ALA H H 8.89 0.03 1 130 . 16 ALA C C 178.35 0.50 1 131 . 16 ALA CA C 51.78 0.50 1 132 . 16 ALA CB C 20.84 0.50 1 133 . 16 ALA N N 121.79 0.25 1 134 . 17 LEU HA H 4.79 0.03 1 135 . 17 LEU HB3 H 1.21 0.03 2 136 . 17 LEU HB2 H 1.73 0.03 2 137 . 17 LEU HD1 H 0.81 0.03 2 138 . 17 LEU HD2 H 0.94 0.03 2 139 . 17 LEU HG H 1.39 0.03 1 140 . 17 LEU H H 8.57 0.03 1 141 . 17 LEU C C 173.75 0.50 1 142 . 17 LEU CA C 54.81 0.50 1 143 . 17 LEU CB C 43.97 0.50 1 144 . 17 LEU CD1 C 26.27 0.50 2 145 . 17 LEU CD2 C 24.24 0.50 2 146 . 17 LEU N N 126.67 0.25 1 147 . 18 LEU HA H 4.90 0.03 1 148 . 18 LEU HB3 H 1.70 0.03 2 149 . 18 LEU HB2 H 1.03 0.03 2 150 . 18 LEU HD1 H 0.89 0.03 2 151 . 18 LEU HD2 H 0.72 0.03 2 152 . 18 LEU HG H 1.37 0.03 1 153 . 18 LEU H H 8.81 0.03 1 154 . 18 LEU C C 176.09 0.50 1 155 . 18 LEU CA C 53.76 0.50 1 156 . 18 LEU CB C 43.70 0.50 1 157 . 18 LEU CD1 C 25.91 0.50 2 158 . 18 LEU CD2 C 23.95 0.50 2 159 . 18 LEU CG C 28.46 0.50 1 160 . 18 LEU N N 127.89 0.25 1 161 . 19 LEU HA H 4.48 0.03 1 162 . 19 LEU HB2 H 1.62 0.03 2 163 . 19 LEU HD1 H 0.87 0.03 2 164 . 19 LEU HD2 H 0.80 0.03 2 165 . 19 LEU HG H 1.59 0.03 1 166 . 19 LEU H H 8.96 0.03 1 167 . 19 LEU C C 175.41 0.50 1 168 . 19 LEU CA C 53.97 0.50 1 169 . 19 LEU CB C 41.67 0.50 1 170 . 19 LEU CD1 C 25.90 0.50 2 171 . 19 LEU CD2 C 24.34 0.50 2 172 . 19 LEU CG C 27.45 0.50 1 173 . 19 LEU N N 129.10 0.25 1 174 . 20 LYS HA H 4.48 0.03 1 175 . 20 LYS HB3 H 1.77 0.03 2 176 . 20 LYS HB2 H 1.53 0.03 2 177 . 20 LYS HD3 H 1.64 0.03 2 178 . 20 LYS HD2 H 1.70 0.03 2 179 . 20 LYS HE3 H 2.96 0.03 2 180 . 20 LYS HG3 H 1.35 0.03 2 181 . 20 LYS H H 7.93 0.03 1 182 . 20 LYS CA C 55.71 0.50 1 183 . 20 LYS CB C 34.57 0.50 1 184 . 20 LYS CD C 29.39 0.50 1 185 . 20 LYS CE C 42.26 0.50 1 186 . 20 LYS CG C 24.95 0.50 1 187 . 20 LYS N N 125.06 0.25 1 188 . 21 GLU HA H 4.45 0.03 1 189 . 21 GLU HB3 H 1.84 0.03 2 190 . 21 GLU HB2 H 1.97 0.03 2 191 . 21 GLU HG3 H 2.13 0.03 2 192 . 21 GLU H H 8.67 0.03 1 193 . 21 GLU CA C 55.67 0.50 1 194 . 21 GLU CB C 32.19 0.50 1 195 . 21 GLU CG C 36.77 0.50 1 196 . 21 GLU N N 124.89 0.25 1 197 . 22 ASP HA H 4.55 0.03 1 198 . 22 ASP HB3 H 2.53 0.03 2 199 . 22 ASP HB2 H 2.68 0.03 2 200 . 22 ASP H H 8.68 0.03 1 201 . 22 ASP C C 176.25 0.50 1 202 . 22 ASP CA C 54.36 0.50 1 203 . 22 ASP CB C 41.70 0.50 1 204 . 22 ASP N N 122.63 0.25 1 205 . 23 GLU HA H 4.07 0.03 1 206 . 23 GLU HB2 H 1.87 0.03 2 207 . 23 GLU HG3 H 2.23 0.03 2 208 . 23 GLU HG2 H 2.16 0.03 2 209 . 23 GLU H H 8.50 0.03 1 210 . 23 GLU C C 176.05 0.50 1 211 . 23 GLU CA C 56.89 0.50 1 212 . 23 GLU CB C 30.64 0.50 1 213 . 23 GLU CG C 36.36 0.50 1 214 . 23 GLU N N 122.21 0.25 1 215 . 24 ILE HA H 3.68 0.03 1 216 . 24 ILE HB H 1.64 0.03 1 217 . 24 ILE HD1 H 0.89 0.03 1 218 . 24 ILE HG13 H 1.61 0.03 2 219 . 24 ILE HG2 H 0.65 0.03 1 220 . 24 ILE H H 8.33 0.03 1 221 . 24 ILE C C 175.17 0.50 1 222 . 24 ILE CA C 62.31 0.50 1 223 . 24 ILE CB C 38.96 0.50 1 224 . 24 ILE CD1 C 11.57 0.50 1 225 . 24 ILE CG1 C 28.77 0.50 1 226 . 24 ILE CG2 C 18.00 0.50 1 227 . 24 ILE N N 123.76 0.25 1 228 . 25 VAL HA H 4.00 0.03 1 229 . 25 VAL HB H 1.91 0.03 1 230 . 25 VAL HG1 H 0.79 0.03 2 231 . 25 VAL H H 8.05 0.03 1 232 . 25 VAL C C 174.72 0.50 1 233 . 25 VAL CA C 62.17 0.50 1 234 . 25 VAL CB C 32.78 0.50 1 235 . 25 VAL CG1 C 21.14 0.50 2 236 . 25 VAL N N 130.56 0.25 1 237 . 26 ILE HA H 4.31 0.03 1 238 . 26 ILE HB H 1.56 0.03 1 239 . 26 ILE HD1 H 0.44 0.03 1 240 . 26 ILE HG13 H 1.07 0.03 2 241 . 26 ILE HG2 H 0.58 0.03 1 242 . 26 ILE H H 7.89 0.03 1 243 . 26 ILE C C 176.00 0.50 1 244 . 26 ILE CA C 58.62 0.50 1 245 . 26 ILE CB C 38.06 0.50 1 246 . 26 ILE CD1 C 11.76 0.50 1 247 . 26 ILE CG2 C 17.66 0.50 1 248 . 26 ILE N N 126.35 0.25 1 249 . 27 ASP HA H 4.56 0.03 1 250 . 27 ASP HB3 H 3.21 0.03 2 251 . 27 ASP HB2 H 2.70 0.03 2 252 . 27 ASP H H 9.42 0.03 1 253 . 27 ASP C C 176.30 0.50 1 254 . 27 ASP CA C 53.95 0.50 1 255 . 27 ASP CB C 41.82 0.50 1 256 . 27 ASP N N 128.22 0.25 1 257 . 28 ARG HA H 4.30 0.03 1 258 . 28 ARG HB3 H 2.11 0.03 2 259 . 28 ARG HD3 H 3.10 0.03 2 260 . 28 ARG HD2 H 3.00 0.03 2 261 . 28 ARG HG3 H 1.46 0.03 2 262 . 28 ARG HG2 H 1.65 0.03 2 263 . 28 ARG H H 8.21 0.03 1 264 . 28 ARG CA C 55.69 0.50 1 265 . 28 ARG CB C 29.49 0.50 1 266 . 28 ARG CD C 43.41 0.50 1 267 . 28 ARG CG C 28.19 0.50 1 268 . 28 ARG N N 123.89 0.25 1 269 . 29 LYS HA H 4.20 0.03 1 270 . 29 LYS HB2 H 1.86 0.03 2 271 . 29 LYS HE3 H 2.95 0.03 2 272 . 29 LYS HG3 H 1.59 0.03 2 273 . 29 LYS HG2 H 1.45 0.03 2 274 . 29 LYS H H 8.09 0.03 1 275 . 29 LYS C C 176.33 0.50 1 276 . 29 LYS CA C 57.23 0.50 1 277 . 29 LYS CB C 32.40 0.50 1 278 . 29 LYS CD C 29.45 0.50 1 279 . 29 LYS CE C 41.89 0.50 1 280 . 29 LYS CG C 24.45 0.50 1 281 . 29 LYS N N 122.18 0.25 1 282 . 30 LYS HA H 4.83 0.03 1 283 . 30 LYS HB3 H 1.78 0.03 2 284 . 30 LYS HB2 H 1.91 0.03 2 285 . 30 LYS HD3 H 1.74 0.03 2 286 . 30 LYS HE3 H 3.04 0.03 2 287 . 30 LYS HG3 H 1.62 0.03 2 288 . 30 LYS HG2 H 1.58 0.03 2 289 . 30 LYS H H 8.24 0.03 1 290 . 30 LYS CA C 55.49 0.50 1 291 . 30 LYS CB C 33.21 0.50 1 292 . 30 LYS CD C 29.03 0.50 1 293 . 30 LYS CE C 42.63 0.50 1 294 . 30 LYS CG C 25.17 0.50 1 295 . 30 LYS N N 122.75 0.25 1 296 . 31 ILE HA H 4.36 0.03 1 297 . 31 ILE HB H 1.93 0.03 1 298 . 31 ILE HD1 H 0.62 0.03 1 299 . 31 ILE HG13 H 1.22 0.03 2 300 . 31 ILE HG12 H 1.44 0.03 2 301 . 31 ILE HG2 H 0.74 0.03 1 302 . 31 ILE H H 8.27 0.03 1 303 . 31 ILE CA C 60.68 0.50 1 304 . 31 ILE CB C 38.89 0.50 1 305 . 31 ILE CD1 C 15.40 0.50 1 306 . 31 ILE CG2 C 19.18 0.50 1 307 . 31 ILE N N 118.08 0.25 1 308 . 32 SER HA H 4.45 0.03 1 309 . 32 SER HB3 H 4.03 0.03 2 310 . 32 SER HB2 H 3.80 0.03 2 311 . 32 SER H H 8.07 0.03 1 312 . 32 SER CA C 57.06 0.50 1 313 . 32 SER CB C 65.02 0.50 1 314 . 32 SER N N 113.77 0.25 1 315 . 33 ALA HA H 3.77 0.03 1 316 . 33 ALA HB H 1.48 0.03 1 317 . 33 ALA H H 8.69 0.03 1 318 . 33 ALA CA C 55.46 0.50 1 319 . 33 ALA CB C 18.62 0.50 1 320 . 33 ALA N N 123.70 0.25 1 321 . 34 ASP HA H 4.49 0.03 1 322 . 34 ASP HB2 H 2.69 0.03 2 323 . 34 ASP H H 8.22 0.03 1 324 . 34 ASP C C 176.72 0.50 1 325 . 34 ASP CA C 55.34 0.50 1 326 . 34 ASP CB C 40.27 0.50 1 327 . 34 ASP N N 113.39 0.25 1 328 . 35 GLN HA H 4.51 0.03 1 329 . 35 GLN HB3 H 2.39 0.03 2 330 . 35 GLN HB2 H 2.17 0.03 2 331 . 35 GLN HE21 H 6.71 0.03 2 332 . 35 GLN HE22 H 7.67 0.03 2 333 . 35 GLN HG3 H 2.38 0.03 2 334 . 35 GLN H H 7.78 0.03 1 335 . 35 GLN C C 176.11 0.50 1 336 . 35 GLN CA C 55.84 0.50 1 337 . 35 GLN CB C 30.89 0.50 1 338 . 35 GLN CG C 34.94 0.50 1 339 . 35 GLN N N 118.07 0.25 1 340 . 35 GLN NE2 N 111.48 0.25 1 341 . 36 VAL HA H 3.35 0.03 1 342 . 36 VAL HB H 2.11 0.03 1 343 . 36 VAL HG1 H 1.16 0.03 2 344 . 36 VAL HG2 H 0.99 0.03 2 345 . 36 VAL H H 7.12 0.03 1 346 . 36 VAL CA C 67.21 0.50 1 347 . 36 VAL CB C 32.68 0.50 1 348 . 36 VAL CG1 C 23.88 0.50 2 349 . 36 VAL CG2 C 22.20 0.50 2 350 . 36 VAL N N 120.52 0.25 1 351 . 37 ASP HA H 4.33 0.03 1 352 . 37 ASP HB2 H 2.63 0.03 2 353 . 37 ASP H H 8.51 0.03 1 354 . 37 ASP C C 179.47 0.50 1 355 . 37 ASP CA C 58.34 0.50 1 356 . 37 ASP CB C 39.76 0.50 1 357 . 37 ASP N N 118.32 0.25 1 358 . 38 GLN HA H 4.14 0.03 1 359 . 38 GLN HB3 H 2.21 0.03 2 360 . 38 GLN HE21 H 6.81 0.03 2 361 . 38 GLN HE22 H 7.66 0.03 2 362 . 38 GLN HG3 H 2.42 0.03 2 363 . 38 GLN H H 8.07 0.03 1 364 . 38 GLN C C 179.00 0.50 1 365 . 38 GLN CA C 58.89 0.50 1 366 . 38 GLN CB C 28.79 0.50 1 367 . 38 GLN CG C 34.70 0.50 1 368 . 38 GLN N N 119.71 0.25 1 369 . 38 GLN NE2 N 111.19 0.25 1 370 . 39 GLU HA H 4.17 0.03 1 371 . 39 GLU H H 8.15 0.03 1 372 . 39 GLU C C 179.18 0.50 1 373 . 39 GLU CA C 59.40 0.50 1 374 . 39 GLU CB C 29.87 0.50 1 375 . 39 GLU N N 121.68 0.25 1 376 . 40 VAL HA H 3.63 0.03 1 377 . 40 VAL HB H 2.37 0.03 1 378 . 40 VAL HG1 H 1.20 0.03 2 379 . 40 VAL HG2 H 1.07 0.03 2 380 . 40 VAL H H 8.72 0.03 1 381 . 40 VAL C C 178.40 0.50 1 382 . 40 VAL CA C 68.54 0.50 1 383 . 40 VAL CB C 31.98 0.50 1 384 . 40 VAL CG1 C 24.12 0.50 2 385 . 40 VAL CG2 C 21.92 0.50 2 386 . 40 VAL N N 121.69 0.25 1 387 . 41 GLU HA H 4.03 0.03 1 388 . 41 GLU HB3 H 2.14 0.03 2 389 . 41 GLU H H 7.88 0.03 1 390 . 41 GLU C C 178.94 0.50 1 391 . 41 GLU CA C 59.90 0.50 1 392 . 41 GLU CB C 29.09 0.50 1 393 . 41 GLU CG C 36.34 0.50 1 394 . 41 GLU N N 118.50 0.25 1 395 . 42 ARG HA H 4.07 0.03 1 396 . 42 ARG HB3 H 2.09 0.03 2 397 . 42 ARG H H 8.19 0.03 1 398 . 42 ARG C C 180.22 0.50 1 399 . 42 ARG CA C 60.21 0.50 1 400 . 42 ARG CB C 31.15 0.50 1 401 . 42 ARG N N 121.40 0.25 1 402 . 43 PHE H H 8.02 0.03 1 403 . 43 PHE CA C 60.22 0.50 1 404 . 43 PHE CB C 38.23 0.50 1 405 . 43 PHE N N 119.31 0.25 1 406 . 44 LEU HA H 3.24 0.03 1 407 . 44 LEU HB3 H 1.80 0.03 2 408 . 44 LEU H H 8.51 0.03 1 409 . 44 LEU C C 180.78 0.50 1 410 . 44 LEU CA C 58.29 0.50 1 411 . 44 LEU CB C 41.34 0.50 1 412 . 44 LEU N N 120.49 0.25 1 413 . 45 SER HA H 4.23 0.03 1 414 . 45 SER HB3 H 3.97 0.03 2 415 . 45 SER HB2 H 3.92 0.03 2 416 . 45 SER H H 9.01 0.03 1 417 . 45 SER C C 177.58 0.50 1 418 . 45 SER CA C 61.58 0.50 1 419 . 45 SER CB C 63.10 0.50 1 420 . 45 SER N N 116.16 0.25 1 421 . 46 GLY H H 7.93 0.03 1 422 . 46 GLY C C 175.04 0.50 1 423 . 46 GLY CA C 47.29 0.50 1 424 . 46 GLY N N 110.22 0.25 1 425 . 47 ARG HA H 3.64 0.03 1 426 . 47 ARG HB3 H 2.12 0.03 2 427 . 47 ARG H H 8.74 0.03 1 428 . 47 ARG CA C 60.41 0.50 1 429 . 47 ARG CB C 29.88 0.50 1 430 . 47 ARG N N 122.56 0.25 1 431 . 48 ALA HA H 4.17 0.03 1 432 . 48 ALA HB H 1.48 0.03 1 433 . 48 ALA H H 7.87 0.03 1 434 . 48 ALA CA C 55.28 0.50 1 435 . 48 ALA CB C 18.02 0.50 1 436 . 48 ALA N N 121.11 0.25 1 437 . 49 LYS HA H 4.02 0.03 1 438 . 49 LYS HB3 H 1.78 0.03 2 439 . 49 LYS HE3 H 2.96 0.03 2 440 . 49 LYS HG3 H 1.33 0.03 2 441 . 49 LYS H H 7.64 0.03 1 442 . 49 LYS CA C 60.16 0.50 1 443 . 49 LYS CB C 33.10 0.50 1 444 . 49 LYS CE C 42.26 0.50 1 445 . 49 LYS N N 119.03 0.25 1 446 . 50 ALA HA H 4.18 0.03 1 447 . 50 ALA HB H 1.51 0.03 1 448 . 50 ALA H H 8.00 0.03 1 449 . 50 ALA CA C 55.00 0.50 1 450 . 50 ALA CB C 18.29 0.50 1 451 . 50 ALA N N 121.31 0.25 1 452 . 51 SER HA H 3.92 0.03 1 453 . 51 SER H H 8.14 0.03 1 454 . 51 SER C C 175.68 0.50 1 455 . 51 SER CB C 63.06 0.50 1 456 . 51 SER N N 114.64 0.25 1 457 . 52 ALA HA H 4.17 0.03 1 458 . 52 ALA HB H 1.51 0.03 1 459 . 52 ALA H H 7.73 0.03 1 460 . 52 ALA C C 181.64 0.50 1 461 . 52 ALA CA C 55.35 0.50 1 462 . 52 ALA CB C 18.08 0.50 1 463 . 52 ALA N N 122.31 0.25 1 464 . 53 GLN HA H 4.03 0.03 1 465 . 53 GLN H H 7.89 0.03 1 466 . 53 GLN HE21 H 7.55 0.03 2 467 . 53 GLN C C 179.89 0.50 1 468 . 53 GLN CA C 58.83 0.50 1 469 . 53 GLN CB C 27.79 0.50 1 470 . 53 GLN CG C 33.72 0.50 1 471 . 53 GLN N N 117.41 0.25 1 472 . 53 GLN NE2 N 111.22 0.25 1 473 . 54 LEU HA H 3.98 0.03 1 474 . 54 LEU HB3 H 2.08 0.03 2 475 . 54 LEU H H 8.20 0.03 1 476 . 54 LEU C C 178.53 0.50 1 477 . 54 LEU CA C 58.26 0.50 1 478 . 54 LEU CB C 43.12 0.50 1 479 . 54 LEU N N 119.69 0.25 1 480 . 55 GLU HA H 3.96 0.03 1 481 . 55 GLU HB3 H 2.12 0.03 2 482 . 55 GLU H H 8.52 0.03 1 483 . 55 GLU C C 179.25 0.50 1 484 . 55 GLU CA C 60.33 0.50 1 485 . 55 GLU CB C 29.16 0.50 1 486 . 55 GLU CG C 35.86 0.50 1 487 . 55 GLU N N 121.46 0.25 1 488 . 56 THR HA H 3.98 0.03 1 489 . 56 THR HB H 4.26 0.03 1 490 . 56 THR HG2 H 1.22 0.03 1 491 . 56 THR H H 7.58 0.03 1 492 . 56 THR C C 176.53 0.50 1 493 . 56 THR CA C 66.68 0.50 1 494 . 56 THR CB C 69.08 0.50 1 495 . 56 THR CG2 C 22.27 0.50 1 496 . 56 THR N N 116.22 0.25 1 497 . 57 ILE HA H 3.29 0.03 1 498 . 57 ILE HB H 1.51 0.03 1 499 . 57 ILE HD1 H 0.81 0.03 1 500 . 57 ILE HG13 H 0.66 0.03 2 501 . 57 ILE HG2 H 0.04 0.03 1 502 . 57 ILE H H 7.88 0.03 1 503 . 57 ILE C C 176.74 0.50 1 504 . 57 ILE CA C 66.01 0.50 1 505 . 57 ILE CB C 38.57 0.50 1 506 . 57 ILE CG1 C 34.75 0.50 1 507 . 57 ILE CG2 C 16.93 0.50 1 508 . 57 ILE N N 123.45 0.25 1 509 . 58 LYS HA H 3.66 0.03 1 510 . 58 LYS HB3 H 1.80 0.03 2 511 . 58 LYS HD3 H 1.64 0.03 2 512 . 58 LYS HE3 H 2.90 0.03 2 513 . 58 LYS H H 8.71 0.03 1 514 . 58 LYS C C 177.74 0.50 1 515 . 58 LYS CA C 60.46 0.50 1 516 . 58 LYS CB C 32.68 0.50 1 517 . 58 LYS CE C 40.94 0.50 1 518 . 58 LYS CG C 24.91 0.50 1 519 . 58 LYS N N 120.48 0.25 1 520 . 59 THR HA H 3.97 0.03 1 521 . 59 THR HB H 4.25 0.03 1 522 . 59 THR HG2 H 1.23 0.03 1 523 . 59 THR H H 7.70 0.03 1 524 . 59 THR C C 177.39 0.50 1 525 . 59 THR CA C 66.37 0.50 1 526 . 59 THR CB C 69.21 0.50 1 527 . 59 THR CG2 C 22.05 0.50 1 528 . 59 THR N N 114.17 0.25 1 529 . 60 LYS HA H 4.11 0.03 1 530 . 60 LYS HB3 H 1.90 0.03 2 531 . 60 LYS HB2 H 1.84 0.03 2 532 . 60 LYS HD3 H 1.63 0.03 2 533 . 60 LYS HE3 H 2.95 0.03 2 534 . 60 LYS HG3 H 1.52 0.03 2 535 . 60 LYS H H 7.91 0.03 1 536 . 60 LYS C C 178.98 0.50 1 537 . 60 LYS CA C 58.89 0.50 1 538 . 60 LYS CB C 31.86 0.50 1 539 . 60 LYS CD C 28.73 0.50 1 540 . 60 LYS CE C 42.48 0.50 1 541 . 60 LYS CG C 25.08 0.50 1 542 . 60 LYS N N 122.84 0.25 1 543 . 61 ALA HA H 4.33 0.03 1 544 . 61 ALA HB H 1.50 0.03 1 545 . 61 ALA H H 9.00 0.03 1 546 . 61 ALA C C 180.73 0.50 1 547 . 61 ALA CA C 55.25 0.50 1 548 . 61 ALA CB C 18.74 0.50 1 549 . 61 ALA N N 122.39 0.25 1 550 . 62 GLY HA3 H 4.02 0.03 2 551 . 62 GLY HA2 H 4.12 0.03 2 552 . 62 GLY H H 8.30 0.03 1 553 . 62 GLY C C 176.74 0.50 1 554 . 62 GLY CA C 47.03 0.50 1 555 . 62 GLY N N 105.30 0.25 1 556 . 63 GLU HA H 4.10 0.03 1 557 . 63 GLU HB3 H 2.19 0.03 2 558 . 63 GLU HB2 H 2.05 0.03 2 559 . 63 GLU HG3 H 2.40 0.03 2 560 . 63 GLU H H 7.73 0.03 1 561 . 63 GLU C C 178.19 0.50 1 562 . 63 GLU CA C 58.93 0.50 1 563 . 63 GLU CB C 30.38 0.50 1 564 . 63 GLU CG C 36.62 0.50 1 565 . 63 GLU N N 120.67 0.25 1 566 . 64 THR HA H 3.91 0.03 1 567 . 64 THR HB H 3.69 0.03 1 568 . 64 THR HG2 H 0.47 0.03 1 569 . 64 THR H H 8.05 0.03 1 570 . 64 THR C C 175.09 0.50 1 571 . 64 THR CA C 65.19 0.50 1 572 . 64 THR CB C 69.88 0.50 1 573 . 64 THR CG2 C 22.18 0.50 1 574 . 64 THR N N 113.43 0.25 1 575 . 65 PHE HA H 4.80 0.03 1 576 . 65 PHE HB3 H 3.37 0.03 2 577 . 65 PHE HD1 H 7.45 0.03 2 578 . 65 PHE H H 8.64 0.03 1 579 . 65 PHE C C 176.59 0.50 1 580 . 65 PHE CA C 58.57 0.50 1 581 . 65 PHE CB C 41.49 0.50 1 582 . 65 PHE CD1 C 132.27 0.50 2 583 . 65 PHE N N 116.96 0.25 1 584 . 66 GLY HA3 H 4.08 0.03 2 585 . 66 GLY HA2 H 4.66 0.03 2 586 . 66 GLY H H 7.88 0.03 1 587 . 66 GLY C C 175.06 0.50 1 588 . 66 GLY CA C 44.96 0.50 1 589 . 66 GLY N N 109.19 0.25 1 590 . 67 GLU HA H 4.12 0.03 1 591 . 67 GLU HB3 H 2.08 0.03 2 592 . 67 GLU HG3 H 2.32 0.03 2 593 . 67 GLU H H 8.63 0.03 1 594 . 67 GLU C C 178.71 0.50 1 595 . 67 GLU CA C 59.79 0.50 1 596 . 67 GLU CB C 30.10 0.50 1 597 . 67 GLU CG C 36.44 0.50 1 598 . 67 GLU N N 119.29 0.25 1 599 . 68 GLU HA H 4.06 0.03 1 600 . 68 GLU HB3 H 2.05 0.03 2 601 . 68 GLU HG3 H 2.32 0.03 2 602 . 68 GLU H H 8.89 0.03 1 603 . 68 GLU CA C 59.74 0.50 1 604 . 68 GLU CB C 29.18 0.50 1 605 . 68 GLU CG C 36.62 0.50 1 606 . 68 GLU N N 119.76 0.25 1 607 . 69 LYS HA H 4.09 0.03 1 608 . 69 LYS HB2 H 1.85 0.03 2 609 . 69 LYS H H 7.59 0.03 1 610 . 69 LYS CA C 57.47 0.50 1 611 . 69 LYS CB C 32.30 0.50 1 612 . 69 LYS CD C 28.44 0.50 1 613 . 69 LYS CE C 40.53 0.50 1 614 . 69 LYS CG C 25.88 0.50 1 615 . 69 LYS N N 116.98 0.25 1 616 . 70 GLU HA H 3.96 0.03 1 617 . 70 GLU HB3 H 2.07 0.03 2 618 . 70 GLU HG3 H 2.36 0.03 2 619 . 70 GLU H H 7.77 0.03 1 620 . 70 GLU CA C 60.69 0.50 1 621 . 70 GLU CB C 30.08 0.50 1 622 . 70 GLU CG C 36.56 0.50 1 623 . 70 GLU N N 119.23 0.25 1 624 . 71 ALA HA H 4.14 0.03 1 625 . 71 ALA HB H 1.47 0.03 1 626 . 71 ALA H H 7.74 0.03 1 627 . 71 ALA C C 180.81 0.50 1 628 . 71 ALA CA C 54.92 0.50 1 629 . 71 ALA CB C 18.50 0.50 1 630 . 71 ALA N N 118.03 0.25 1 631 . 72 ILE HA H 3.42 0.03 1 632 . 72 ILE HB H 1.44 0.03 1 633 . 72 ILE HD1 H 0.67 0.03 1 634 . 72 ILE HG13 H 0.91 0.03 2 635 . 72 ILE HG12 H 0.95 0.03 2 636 . 72 ILE HG2 H -0.03 0.03 1 637 . 72 ILE H H 7.37 0.03 1 638 . 72 ILE C C 178.04 0.50 1 639 . 72 ILE CA C 64.56 0.50 1 640 . 72 ILE CB C 37.68 0.50 1 641 . 72 ILE CD1 C 13.46 0.50 1 642 . 72 ILE CG2 C 16.16 0.50 1 643 . 72 ILE N N 118.34 0.25 1 644 . 73 PHE HA H 3.93 0.03 1 645 . 73 PHE HD1 H 7.07 0.03 2 646 . 73 PHE HE1 H 6.94 0.03 2 647 . 73 PHE H H 7.00 0.03 1 648 . 73 PHE C C 177.81 0.50 1 649 . 73 PHE CA C 62.26 0.50 1 650 . 73 PHE CB C 38.87 0.50 1 651 . 73 PHE CD1 C 131.49 0.50 2 652 . 73 PHE CE1 C 131.01 0.50 2 653 . 73 PHE N N 116.70 0.25 1 654 . 74 GLU HA H 4.09 0.03 1 655 . 74 GLU HB3 H 2.08 0.03 2 656 . 74 GLU H H 8.24 0.03 1 657 . 74 GLU C C 179.28 0.50 1 658 . 74 GLU CA C 60.09 0.50 1 659 . 74 GLU CB C 29.59 0.50 1 660 . 74 GLU CG C 36.32 0.50 1 661 . 74 GLU N N 120.98 0.25 1 662 . 75 GLY HA3 H 3.74 0.03 2 663 . 75 GLY H H 7.73 0.03 1 664 . 75 GLY C C 175.73 0.50 1 665 . 75 GLY CA C 47.26 0.50 1 666 . 75 GLY N N 105.99 0.25 1 667 . 76 HIS HD2 H 6.64 0.03 1 668 . 76 HIS H H 7.75 0.03 1 669 . 76 HIS C C 177.72 0.50 1 670 . 76 HIS CA C 59.51 0.50 1 671 . 76 HIS CB C 32.30 0.50 1 672 . 76 HIS CD2 C 115.42 0.50 1 673 . 76 HIS N N 121.63 0.25 1 674 . 77 ILE HA H 3.51 0.03 1 675 . 77 ILE HB H 1.93 0.03 1 676 . 77 ILE HD1 H 0.81 0.03 1 677 . 77 ILE HG13 H 1.94 0.03 2 678 . 77 ILE HG2 H 0.92 0.03 1 679 . 77 ILE H H 8.00 0.03 1 680 . 77 ILE C C 177.23 0.50 1 681 . 77 ILE CA C 66.77 0.50 1 682 . 77 ILE CB C 38.82 0.50 1 683 . 77 ILE CD1 C 14.00 0.50 1 684 . 77 ILE CG1 C 32.08 0.50 1 685 . 77 ILE CG2 C 17.71 0.50 1 686 . 77 ILE N N 119.78 0.25 1 687 . 78 MET HE H 2.19 0.03 1 688 . 78 MET H H 7.87 0.03 1 689 . 78 MET CA C 59.30 0.50 1 690 . 78 MET CB C 33.73 0.50 1 691 . 78 MET CE C 17.19 0.50 1 692 . 78 MET CG C 32.75 0.50 1 693 . 78 MET N N 117.04 0.25 1 694 . 79 LEU HA H 4.03 0.03 1 695 . 79 LEU HB3 H 1.99 0.03 2 696 . 79 LEU HB2 H 1.60 0.03 2 697 . 79 LEU HD1 H 0.83 0.03 2 698 . 79 LEU HD2 H 0.94 0.03 2 699 . 79 LEU HG H 1.83 0.03 1 700 . 79 LEU H H 8.05 0.03 1 701 . 79 LEU C C 177.32 0.50 1 702 . 79 LEU CA C 58.89 0.50 1 703 . 79 LEU CB C 42.83 0.50 1 704 . 79 LEU CD1 C 23.91 0.50 2 705 . 79 LEU CD2 C 25.52 0.50 2 706 . 79 LEU CG C 27.36 0.50 1 707 . 79 LEU N N 119.23 0.25 1 708 . 80 LEU HA H 3.79 0.03 1 709 . 80 LEU HD2 H 0.92 0.03 2 710 . 80 LEU HG H 1.69 0.03 1 711 . 80 LEU H H 8.00 0.03 1 712 . 80 LEU C C 177.58 0.50 1 713 . 80 LEU CA C 57.88 0.50 1 714 . 80 LEU CB C 42.51 0.50 1 715 . 80 LEU CD2 C 26.29 0.50 2 716 . 80 LEU N N 116.83 0.25 1 717 . 81 GLU HA H 4.01 0.03 1 718 . 81 GLU H H 7.98 0.03 1 719 . 81 GLU C C 175.38 0.50 1 720 . 81 GLU CA C 56.36 0.50 1 721 . 81 GLU CB C 29.06 0.50 1 722 . 81 GLU CG C 37.16 0.50 1 723 . 81 GLU N N 112.73 0.25 1 724 . 82 ASP HA H 4.44 0.03 1 725 . 82 ASP H H 7.25 0.03 1 726 . 82 ASP C C 177.96 0.50 1 727 . 82 ASP CA C 56.37 0.50 1 728 . 82 ASP CB C 45.04 0.50 1 729 . 82 ASP N N 121.72 0.25 1 730 . 83 GLU HA H 4.14 0.03 1 731 . 83 GLU HB3 H 2.14 0.03 2 732 . 83 GLU HG3 H 2.41 0.03 2 733 . 83 GLU H H 9.24 0.03 1 734 . 83 GLU C C 178.63 0.50 1 735 . 83 GLU CA C 60.12 0.50 1 736 . 83 GLU CB C 30.22 0.50 1 737 . 83 GLU CG C 37.14 0.50 1 738 . 83 GLU N N 128.15 0.25 1 739 . 84 GLU H H 8.66 0.03 1 740 . 84 GLU CA C 59.68 0.50 1 741 . 84 GLU CB C 28.93 0.50 1 742 . 84 GLU CG C 36.94 0.50 1 743 . 84 GLU N N 121.27 0.25 1 744 . 85 LEU HB3 H 1.89 0.03 2 745 . 85 LEU HD1 H 0.92 0.03 2 746 . 85 LEU HG H 1.68 0.03 1 747 . 85 LEU H H 8.00 0.03 1 748 . 85 LEU CA C 58.83 0.50 1 749 . 85 LEU CB C 41.83 0.50 1 750 . 85 LEU CD1 C 24.98 0.50 2 751 . 85 LEU CD2 C 26.78 0.50 2 752 . 85 LEU CG C 27.17 0.50 1 753 . 85 LEU N N 122.39 0.25 1 754 . 86 GLU HA H 3.86 0.03 1 755 . 86 GLU HB3 H 1.87 0.03 2 756 . 86 GLU HG3 H 2.24 0.03 2 757 . 86 GLU HG2 H 2.16 0.03 2 758 . 86 GLU H H 7.61 0.03 1 759 . 86 GLU C C 177.54 0.50 1 760 . 86 GLU CA C 60.14 0.50 1 761 . 86 GLU CB C 30.55 0.50 1 762 . 86 GLU CG C 36.47 0.50 1 763 . 86 GLU N N 116.97 0.25 1 764 . 87 GLN HA H 3.93 0.03 1 765 . 87 GLN HB2 H 2.22 0.03 2 766 . 87 GLN HE21 H 6.77 0.03 2 767 . 87 GLN HE22 H 7.51 0.03 2 768 . 87 GLN HG3 H 2.61 0.03 2 769 . 87 GLN HG2 H 2.53 0.03 2 770 . 87 GLN H H 7.98 0.03 1 771 . 87 GLN C C 179.10 0.50 1 772 . 87 GLN CA C 59.09 0.50 1 773 . 87 GLN CB C 28.69 0.50 1 774 . 87 GLN CG C 34.49 0.50 1 775 . 87 GLN N N 115.51 0.25 1 776 . 87 GLN NE2 N 111.33 0.25 1 777 . 88 GLU HA H 4.01 0.03 1 778 . 88 GLU HB3 H 2.04 0.03 2 779 . 88 GLU HG3 H 2.48 0.03 2 780 . 88 GLU H H 8.26 0.03 1 781 . 88 GLU C C 179.16 0.50 1 782 . 88 GLU CA C 59.98 0.50 1 783 . 88 GLU CB C 29.96 0.50 1 784 . 88 GLU CG C 36.70 0.50 1 785 . 88 GLU N N 120.25 0.25 1 786 . 89 ILE HA H 3.32 0.03 1 787 . 89 ILE HB H 1.25 0.03 1 788 . 89 ILE HD1 H 0.48 0.03 1 789 . 89 ILE HG2 H -0.09 0.03 1 790 . 89 ILE H H 7.81 0.03 1 791 . 89 ILE CA C 66.61 0.50 1 792 . 89 ILE CB C 37.83 0.50 1 793 . 89 ILE CD1 C 14.87 0.50 1 794 . 89 ILE CG2 C 15.63 0.50 1 795 . 89 ILE N N 119.33 0.25 1 796 . 90 ILE HA H 3.47 0.03 1 797 . 90 ILE HB H 1.87 0.03 1 798 . 90 ILE H H 8.22 0.03 1 799 . 90 ILE C C 177.34 0.50 1 800 . 90 ILE CA C 66.55 0.50 1 801 . 90 ILE CB C 37.68 0.50 1 802 . 90 ILE N N 117.93 0.25 1 803 . 91 ALA HA H 4.07 0.03 1 804 . 91 ALA HB H 1.46 0.03 1 805 . 91 ALA H H 8.06 0.03 1 806 . 91 ALA C C 180.04 0.50 1 807 . 91 ALA CA C 55.65 0.50 1 808 . 91 ALA CB C 18.22 0.50 1 809 . 91 ALA N N 120.65 0.25 1 810 . 92 LEU HA H 3.96 0.03 1 811 . 92 LEU HB3 H 1.98 0.03 2 812 . 92 LEU HD1 H 0.94 0.03 2 813 . 92 LEU HD2 H 0.83 0.03 2 814 . 92 LEU H H 7.27 0.03 1 815 . 92 LEU C C 179.93 0.50 1 816 . 92 LEU CA C 58.35 0.50 1 817 . 92 LEU CB C 41.65 0.50 1 818 . 92 LEU CD1 C 27.07 0.50 2 819 . 92 LEU N N 117.46 0.25 1 820 . 93 ILE HA H 4.14 0.03 1 821 . 93 ILE HB H 1.89 0.03 1 822 . 93 ILE HD1 H 0.70 0.03 1 823 . 93 ILE HG2 H 1.05 0.03 1 824 . 93 ILE H H 7.50 0.03 1 825 . 93 ILE CA C 65.52 0.50 1 826 . 93 ILE CB C 39.62 0.50 1 827 . 93 ILE CD1 C 15.24 0.50 1 828 . 93 ILE CG2 C 18.21 0.50 1 829 . 93 ILE N N 119.99 0.25 1 830 . 94 LYS HA H 3.99 0.03 1 831 . 94 LYS HB3 H 1.75 0.03 2 832 . 94 LYS HB2 H 1.87 0.03 2 833 . 94 LYS HG3 H 1.59 0.03 2 834 . 94 LYS H H 8.54 0.03 1 835 . 94 LYS C C 178.05 0.50 1 836 . 94 LYS CA C 60.40 0.50 1 837 . 94 LYS CB C 33.56 0.50 1 838 . 94 LYS CG C 25.72 0.50 1 839 . 94 LYS N N 114.98 0.25 1 840 . 95 ASP HA H 4.63 0.03 1 841 . 95 ASP HB3 H 2.85 0.03 2 842 . 95 ASP HB2 H 2.53 0.03 2 843 . 95 ASP H H 8.88 0.03 1 844 . 95 ASP C C 178.38 0.50 1 845 . 95 ASP CA C 56.03 0.50 1 846 . 95 ASP CB C 41.38 0.50 1 847 . 95 ASP N N 114.92 0.25 1 848 . 96 LYS HA H 4.43 0.03 1 849 . 96 LYS HB2 H 2.16 0.03 2 850 . 96 LYS HD3 H 1.61 0.03 2 851 . 96 LYS HG3 H 1.47 0.03 2 852 . 96 LYS HG2 H 1.31 0.03 2 853 . 96 LYS H H 7.19 0.03 1 854 . 96 LYS C C 175.68 0.50 1 855 . 96 LYS CA C 55.46 0.50 1 856 . 96 LYS CB C 32.90 0.50 1 857 . 96 LYS CD C 29.21 0.50 1 858 . 96 LYS CE C 42.24 0.50 1 859 . 96 LYS CG C 25.99 0.50 1 860 . 96 LYS N N 114.91 0.25 1 861 . 97 HIS HA H 4.48 0.03 1 862 . 97 HIS H H 7.31 0.03 1 863 . 97 HIS C C 174.45 0.50 1 864 . 97 HIS CA C 56.25 0.50 1 865 . 97 HIS CB C 26.62 0.50 1 866 . 97 HIS N N 115.65 0.25 1 867 . 98 MET HA H 4.55 0.03 1 868 . 98 MET H H 7.27 0.03 1 869 . 98 MET C C 174.55 0.50 1 870 . 98 MET CA C 55.69 0.50 1 871 . 98 MET CB C 36.20 0.50 1 872 . 98 MET CG C 33.13 0.50 1 873 . 98 MET N N 116.72 0.25 1 874 . 99 THR HA H 3.98 0.03 1 875 . 99 THR HB H 4.52 0.03 1 876 . 99 THR HG2 H 1.24 0.03 1 877 . 99 THR H H 8.35 0.03 1 878 . 99 THR C C 175.99 0.50 1 879 . 99 THR CA C 61.16 0.50 1 880 . 99 THR CB C 71.98 0.50 1 881 . 99 THR CG2 C 23.91 0.50 1 882 . 99 THR N N 105.92 0.25 1 883 . 100 ALA HA H 3.88 0.03 1 884 . 100 ALA HB H 1.67 0.03 1 885 . 100 ALA H H 10.46 0.03 1 886 . 100 ALA C C 179.08 0.50 1 887 . 100 ALA CA C 55.93 0.50 1 888 . 100 ALA CB C 20.06 0.50 1 889 . 100 ALA N N 121.28 0.25 1 890 . 101 ASP HA H 4.15 0.03 1 891 . 101 ASP HB2 H 2.41 0.03 2 892 . 101 ASP H H 9.38 0.03 1 893 . 101 ASP C C 176.86 0.50 1 894 . 101 ASP CA C 55.83 0.50 1 895 . 101 ASP CB C 40.25 0.50 1 896 . 101 ASP N N 108.75 0.25 1 897 . 102 ALA HA H 3.95 0.03 1 898 . 102 ALA HB H 1.41 0.03 1 899 . 102 ALA H H 7.53 0.03 1 900 . 102 ALA C C 180.13 0.50 1 901 . 102 ALA CA C 56.05 0.50 1 902 . 102 ALA CB C 18.54 0.50 1 903 . 102 ALA N N 122.52 0.25 1 904 . 103 ALA HA H 4.06 0.03 1 905 . 103 ALA HB H 1.38 0.03 1 906 . 103 ALA H H 8.87 0.03 1 907 . 103 ALA C C 178.46 0.50 1 908 . 103 ALA CA C 54.97 0.50 1 909 . 103 ALA CB C 21.20 0.50 1 910 . 103 ALA N N 120.96 0.25 1 911 . 104 ALA HA H 3.76 0.03 1 912 . 104 ALA HB H 1.33 0.03 1 913 . 104 ALA H H 8.25 0.03 1 914 . 104 ALA C C 178.79 0.50 1 915 . 104 ALA CA C 55.32 0.50 1 916 . 104 ALA CB C 18.07 0.50 1 917 . 104 ALA N N 117.46 0.25 1 918 . 105 HIS HA H 4.05 0.03 1 919 . 105 HIS HD2 H 6.89 0.03 1 920 . 105 HIS H H 8.21 0.03 1 921 . 105 HIS C C 176.54 0.50 1 922 . 105 HIS CA C 61.07 0.50 1 923 . 105 HIS CB C 31.32 0.50 1 924 . 105 HIS CD2 C 120.41 0.50 1 925 . 105 HIS N N 115.56 0.25 1 926 . 106 GLU HA H 3.77 0.03 1 927 . 106 GLU HB3 H 2.19 0.03 2 928 . 106 GLU HB2 H 1.99 0.03 2 929 . 106 GLU HG3 H 2.25 0.03 2 930 . 106 GLU HG2 H 2.15 0.03 2 931 . 106 GLU H H 8.16 0.03 1 932 . 106 GLU C C 180.54 0.50 1 933 . 106 GLU CA C 59.88 0.50 1 934 . 106 GLU CB C 29.49 0.50 1 935 . 106 GLU CG C 36.09 0.50 1 936 . 106 GLU N N 117.29 0.25 1 937 . 107 VAL HA H 3.67 0.03 1 938 . 107 VAL HB H 1.77 0.03 1 939 . 107 VAL HG1 H 0.98 0.03 2 940 . 107 VAL HG2 H 0.88 0.03 2 941 . 107 VAL H H 7.83 0.03 1 942 . 107 VAL C C 178.88 0.50 1 943 . 107 VAL CA C 66.59 0.50 1 944 . 107 VAL CB C 32.43 0.50 1 945 . 107 VAL N N 118.47 0.25 1 946 . 108 ILE HA H 3.57 0.03 1 947 . 108 ILE HB H 2.05 0.03 1 948 . 108 ILE HD1 H 0.73 0.03 1 949 . 108 ILE HG13 H 1.46 0.03 2 950 . 108 ILE HG2 H 0.83 0.03 1 951 . 108 ILE H H 8.28 0.03 1 952 . 108 ILE C C 177.58 0.50 1 953 . 108 ILE CA C 64.51 0.50 1 954 . 108 ILE CB C 36.83 0.50 1 955 . 108 ILE CD1 C 11.49 0.50 1 956 . 108 ILE CG1 C 27.45 0.50 1 957 . 108 ILE CG2 C 18.14 0.50 1 958 . 108 ILE N N 120.21 0.25 1 959 . 109 GLU HA H 3.98 0.03 1 960 . 109 GLU HB2 H 1.61 0.03 2 961 . 109 GLU HG3 H 2.02 0.03 2 962 . 109 GLU H H 8.61 0.03 1 963 . 109 GLU C C 180.12 0.50 1 964 . 109 GLU CA C 58.84 0.50 1 965 . 109 GLU CB C 28.18 0.50 1 966 . 109 GLU CG C 35.66 0.50 1 967 . 109 GLU N N 118.93 0.25 1 968 . 110 GLY H H 7.77 0.03 1 969 . 110 GLY CA C 47.37 0.50 1 970 . 110 GLY N N 107.12 0.25 1 971 . 111 GLN HA H 4.21 0.03 1 972 . 111 GLN HB3 H 2.08 0.03 1 973 . 111 GLN HB2 H 2.08 0.03 1 974 . 111 GLN HE21 H 6.84 0.03 2 975 . 111 GLN HE22 H 6.19 0.03 2 976 . 111 GLN H H 7.74 0.03 1 977 . 111 GLN C C 178.18 0.50 1 978 . 111 GLN CA C 58.44 0.50 1 979 . 111 GLN CB C 28.36 0.50 1 980 . 111 GLN CG C 32.96 0.50 1 981 . 111 GLN N N 121.62 0.25 1 982 . 111 GLN NE2 N 109.31 0.25 1 983 . 112 ALA HA H 3.84 0.03 1 984 . 112 ALA HB H 1.34 0.03 1 985 . 112 ALA H H 8.54 0.03 1 986 . 112 ALA C C 179.12 0.50 1 987 . 112 ALA CA C 56.28 0.50 1 988 . 112 ALA CB C 18.54 0.50 1 989 . 112 ALA N N 121.37 0.25 1 990 . 113 SER HA H 4.19 0.03 1 991 . 113 SER HB3 H 3.90 0.03 2 992 . 113 SER H H 8.45 0.03 1 993 . 113 SER C C 176.76 0.50 1 994 . 113 SER CA C 62.25 0.50 1 995 . 113 SER CB C 63.05 0.50 1 996 . 113 SER N N 111.43 0.25 1 997 . 114 ALA HA H 4.11 0.03 1 998 . 114 ALA HB H 1.46 0.03 1 999 . 114 ALA H H 7.42 0.03 1 1000 . 114 ALA CA C 54.95 0.50 1 1001 . 114 ALA CB C 17.92 0.50 1 1002 . 114 ALA N N 123.59 0.25 1 1003 . 115 LEU HA H 4.01 0.03 1 1004 . 115 LEU HB3 H 1.94 0.03 2 1005 . 115 LEU HD1 H 0.84 0.03 2 1006 . 115 LEU HD2 H 0.80 0.03 2 1007 . 115 LEU H H 7.60 0.03 1 1008 . 115 LEU C C 178.76 0.50 1 1009 . 115 LEU CA C 57.59 0.50 1 1010 . 115 LEU CB C 42.46 0.50 1 1011 . 115 LEU CD1 C 25.32 0.50 2 1012 . 115 LEU CD2 C 23.59 0.50 2 1013 . 115 LEU N N 117.41 0.25 1 1014 . 116 GLU HA H 3.92 0.03 1 1015 . 116 GLU HB3 H 2.14 0.03 2 1016 . 116 GLU HG3 H 2.23 0.03 2 1017 . 116 GLU H H 7.76 0.03 1 1018 . 116 GLU C C 177.71 0.50 1 1019 . 116 GLU CA C 58.61 0.50 1 1020 . 116 GLU CB C 29.85 0.50 1 1021 . 116 GLU CG C 37.48 0.50 1 1022 . 116 GLU N N 115.96 0.25 1 1023 . 117 GLU HA H 4.14 0.03 1 1024 . 117 GLU HB3 H 2.04 0.03 2 1025 . 117 GLU HB2 H 2.11 0.03 2 1026 . 117 GLU HG3 H 2.40 0.03 2 1027 . 117 GLU H H 7.44 0.03 1 1028 . 117 GLU C C 177.03 0.50 1 1029 . 117 GLU CA C 57.76 0.50 1 1030 . 117 GLU CB C 30.21 0.50 1 1031 . 117 GLU CG C 36.48 0.50 1 1032 . 117 GLU N N 117.33 0.25 1 1033 . 118 LEU HA H 4.23 0.03 1 1034 . 118 LEU HB2 H 1.86 0.03 2 1035 . 118 LEU HD1 H 0.85 0.03 2 1036 . 118 LEU HD2 H 0.94 0.03 2 1037 . 118 LEU HG H 1.88 0.03 1 1038 . 118 LEU H H 7.15 0.03 1 1039 . 118 LEU C C 176.75 0.50 1 1040 . 118 LEU CA C 55.41 0.50 1 1041 . 118 LEU CB C 42.14 0.50 1 1042 . 118 LEU CD1 C 22.96 0.50 2 1043 . 118 LEU CD2 C 26.64 0.50 2 1044 . 118 LEU N N 118.51 0.25 1 1045 . 119 ASP HA H 4.37 0.03 1 1046 . 119 ASP HB3 H 2.45 0.03 2 1047 . 119 ASP HB2 H 2.86 0.03 2 1048 . 119 ASP H H 8.01 0.03 1 1049 . 119 ASP C C 174.98 0.50 1 1050 . 119 ASP CA C 55.18 0.50 1 1051 . 119 ASP CB C 40.45 0.50 1 1052 . 119 ASP N N 118.03 0.25 1 1053 . 120 ASP HA H 4.70 0.03 1 1054 . 120 ASP HB3 H 2.56 0.03 2 1055 . 120 ASP HB2 H 2.51 0.03 2 1056 . 120 ASP H H 7.69 0.03 1 1057 . 120 ASP CA C 54.04 0.50 1 1058 . 120 ASP CB C 44.66 0.50 1 1059 . 120 ASP N N 119.18 0.25 1 1060 . 121 GLU HA H 3.87 0.03 1 1061 . 121 GLU HB3 H 2.00 0.03 1 1062 . 121 GLU HB2 H 2.00 0.03 1 1063 . 121 GLU HG3 H 2.25 0.03 2 1064 . 121 GLU H H 8.99 0.03 1 1065 . 121 GLU C C 178.18 0.50 1 1066 . 121 GLU CA C 60.22 0.50 1 1067 . 121 GLU CB C 30.09 0.50 1 1068 . 121 GLU CG C 36.37 0.50 1 1069 . 121 GLU N N 126.81 0.25 1 1070 . 122 TYR HA H 4.30 0.03 1 1071 . 122 TYR HB2 H 3.10 0.03 2 1072 . 122 TYR HD1 H 7.06 0.03 2 1073 . 122 TYR HE1 H 6.73 0.03 2 1074 . 122 TYR H H 8.25 0.03 1 1075 . 122 TYR C C 178.51 0.50 1 1076 . 122 TYR CA C 61.21 0.50 1 1077 . 122 TYR CB C 37.77 0.50 1 1078 . 122 TYR CD1 C 133.53 0.50 2 1079 . 122 TYR CE1 C 118.23 0.50 2 1080 . 122 TYR N N 119.60 0.25 1 1081 . 123 LEU HA H 4.04 0.03 1 1082 . 123 LEU HD1 H 1.31 0.03 2 1083 . 123 LEU HD2 H 1.42 0.03 2 1084 . 123 LEU HG H 1.68 0.03 1 1085 . 123 LEU H H 8.07 0.03 1 1086 . 123 LEU C C 179.23 0.50 1 1087 . 123 LEU CA C 57.50 0.50 1 1088 . 123 LEU CB C 41.15 0.50 1 1089 . 123 LEU CD1 C 25.15 0.50 2 1090 . 123 LEU CD2 C 25.20 0.50 2 1091 . 123 LEU CG C 26.87 0.50 1 1092 . 123 LEU N N 120.00 0.25 1 1093 . 124 LYS HA H 3.89 0.03 1 1094 . 124 LYS HB3 H 1.55 0.03 2 1095 . 124 LYS HB2 H 1.91 0.03 2 1096 . 124 LYS H H 8.06 0.03 1 1097 . 124 LYS C C 180.94 0.50 1 1098 . 124 LYS CA C 60.31 0.50 1 1099 . 124 LYS CB C 32.48 0.50 1 1100 . 124 LYS CD C 30.03 0.50 1 1101 . 124 LYS CG C 26.15 0.50 1 1102 . 124 LYS N N 119.01 0.25 1 1103 . 125 GLU HA H 4.06 0.03 1 1104 . 125 GLU HB3 H 2.10 0.03 2 1105 . 125 GLU HG3 H 2.41 0.03 2 1106 . 125 GLU H H 7.63 0.03 1 1107 . 125 GLU C C 178.98 0.50 1 1108 . 125 GLU CA C 59.36 0.50 1 1109 . 125 GLU CB C 29.23 0.50 1 1110 . 125 GLU CG C 36.68 0.50 1 1111 . 125 GLU N N 120.03 0.25 1 1112 . 126 ARG H H 7.67 0.03 1 1113 . 126 ARG C C 178.75 0.50 1 1114 . 126 ARG CA C 58.43 0.50 1 1115 . 126 ARG CB C 30.13 0.50 1 1116 . 126 ARG N N 118.82 0.25 1 1117 . 127 ALA HA H 3.80 0.03 1 1118 . 127 ALA HB H 1.58 0.03 1 1119 . 127 ALA H H 8.10 0.03 1 1120 . 127 ALA C C 178.78 0.50 1 1121 . 127 ALA CA C 55.65 0.50 1 1122 . 127 ALA CB C 19.26 0.50 1 1123 . 127 ALA N N 121.63 0.25 1 1124 . 128 ALA HA H 4.11 0.03 1 1125 . 128 ALA HB H 1.54 0.03 1 1126 . 128 ALA H H 7.46 0.03 1 1127 . 128 ALA CA C 55.33 0.50 1 1128 . 128 ALA CB C 18.17 0.50 1 1129 . 128 ALA N N 119.18 0.25 1 1130 . 130 VAL HA H 3.74 0.03 1 1131 . 130 VAL HB H 2.32 0.03 1 1132 . 130 VAL HG1 H 1.11 0.03 2 1133 . 130 VAL HG2 H 0.89 0.03 2 1134 . 130 VAL CA C 66.46 0.50 1 1135 . 130 VAL CB C 31.87 0.50 1 1136 . 130 VAL CG1 C 22.82 0.50 2 1137 . 130 VAL CG2 C 21.48 0.50 2 1138 . 131 ARG HA H 3.90 0.03 1 1139 . 131 ARG HD3 H 2.97 0.03 2 1140 . 131 ARG H H 8.24 0.03 1 1141 . 131 ARG CA C 61.09 0.50 1 1142 . 131 ARG CB C 30.27 0.50 1 1143 . 131 ARG CD C 42.45 0.50 1 1144 . 131 ARG N N 117.86 0.25 1 1145 . 132 ASP HA H 4.44 0.03 1 1146 . 132 ASP HB3 H 3.04 0.03 2 1147 . 132 ASP H H 7.99 0.03 1 1148 . 132 ASP CA C 57.83 0.50 1 1149 . 132 ASP CB C 41.80 0.50 1 1150 . 132 ASP N N 121.51 0.25 1 1151 . 133 ILE HA H 3.92 0.03 1 1152 . 133 ILE HB H 1.88 0.03 1 1153 . 133 ILE HD1 H 0.70 0.03 1 1154 . 133 ILE HG13 H 1.77 0.03 2 1155 . 133 ILE HG12 H 1.04 0.03 2 1156 . 133 ILE HG2 H 0.90 0.03 1 1157 . 133 ILE H H 8.11 0.03 1 1158 . 133 ILE C C 178.68 0.50 1 1159 . 133 ILE CA C 65.05 0.50 1 1160 . 133 ILE CB C 38.83 0.50 1 1161 . 133 ILE CD1 C 15.33 0.50 1 1162 . 133 ILE CG1 C 28.80 0.50 1 1163 . 133 ILE CG2 C 19.45 0.50 1 1164 . 133 ILE N N 119.48 0.25 1 1165 . 134 GLY HA3 H 3.70 0.03 2 1166 . 134 GLY H H 8.75 0.03 1 1167 . 134 GLY C C 175.03 0.50 1 1168 . 134 GLY CA C 48.39 0.50 1 1169 . 134 GLY N N 107.59 0.25 1 1170 . 135 LYS HA H 3.99 0.03 1 1171 . 135 LYS HB2 H 1.95 0.03 2 1172 . 135 LYS H H 8.53 0.03 1 1173 . 135 LYS C C 178.21 0.50 1 1174 . 135 LYS CA C 60.55 0.50 1 1175 . 135 LYS CB C 32.54 0.50 1 1176 . 135 LYS N N 122.41 0.25 1 1177 . 136 ARG H H 7.63 0.03 1 1178 . 136 ARG C C 180.27 0.50 1 1179 . 136 ARG CA C 60.27 0.50 1 1180 . 136 ARG N N 119.31 0.25 1 1181 . 137 LEU HA H 3.95 0.03 1 1182 . 137 LEU H H 8.87 0.03 1 1183 . 137 LEU C C 177.90 0.50 1 1184 . 137 LEU CA C 59.15 0.50 1 1185 . 137 LEU CB C 41.84 0.50 1 1186 . 137 LEU N N 121.99 0.25 1 1187 . 138 LEU HA H 3.88 0.03 1 1188 . 138 LEU HB3 H 1.33 0.03 2 1189 . 138 LEU HD1 H 1.01 0.03 2 1190 . 138 LEU HG H 1.85 0.03 1 1191 . 138 LEU H H 8.91 0.03 1 1192 . 138 LEU C C 179.22 0.50 1 1193 . 138 LEU CA C 58.73 0.50 1 1194 . 138 LEU CB C 42.28 0.50 1 1195 . 138 LEU CD1 C 25.11 0.50 2 1196 . 138 LEU N N 118.91 0.25 1 1197 . 139 ARG H H 8.69 0.03 1 1198 . 139 ARG C C 178.24 0.50 1 1199 . 139 ARG CA C 61.76 0.50 1 1200 . 139 ARG CB C 30.12 0.50 1 1201 . 139 ARG N N 115.93 0.25 1 1202 . 140 ASN HA H 4.64 0.03 1 1203 . 140 ASN H H 7.64 0.03 1 1204 . 140 ASN C C 178.35 0.50 1 1205 . 140 ASN CA C 57.43 0.50 1 1206 . 140 ASN CB C 41.34 0.50 1 1207 . 140 ASN N N 114.65 0.25 1 1208 . 141 ILE HA H 3.69 0.03 1 1209 . 141 ILE HB H 1.88 0.03 1 1210 . 141 ILE HG2 H 0.89 0.03 1 1211 . 141 ILE H H 8.74 0.03 1 1212 . 141 ILE C C 177.23 0.50 1 1213 . 141 ILE CA C 66.46 0.50 1 1214 . 141 ILE CB C 39.02 0.50 1 1215 . 141 ILE CG2 C 17.23 0.50 1 1216 . 141 ILE N N 122.10 0.25 1 1217 . 142 LEU HA H 4.14 0.03 1 1218 . 142 LEU HB3 H 1.65 0.03 2 1219 . 142 LEU HD1 H 0.98 0.03 2 1220 . 142 LEU H H 8.05 0.03 1 1221 . 142 LEU C C 177.18 0.50 1 1222 . 142 LEU CA C 55.91 0.50 1 1223 . 142 LEU CB C 43.70 0.50 1 1224 . 142 LEU CG C 28.44 0.50 1 1225 . 142 LEU CD2 C 26.55 0.50 2 1226 . 142 LEU N N 115.53 0.25 1 1227 . 143 GLY H H 7.62 0.03 1 1228 . 143 GLY CA C 46.86 0.50 1 1229 . 143 GLY N N 108.73 0.25 1 1230 . 144 LEU HA H 4.39 0.03 1 1231 . 144 LEU H H 8.15 0.03 1 1232 . 144 LEU CA C 53.77 0.50 1 1233 . 144 LEU CB C 43.08 0.50 1 1234 . 144 LEU CD1 C 26.72 0.50 2 1235 . 144 LEU CD2 C 21.87 0.50 2 1236 . 144 LEU N N 119.41 0.25 1 1237 . 145 LYS HA H 4.04 0.03 1 1238 . 145 LYS HB3 H 1.75 0.03 2 1239 . 145 LYS HB2 H 1.69 0.03 2 1240 . 145 LYS HD3 H 1.66 0.03 2 1241 . 145 LYS HE3 H 2.97 0.03 2 1242 . 145 LYS HG3 H 1.31 0.03 2 1243 . 145 LYS HG2 H 1.43 0.03 2 1244 . 145 LYS H H 8.40 0.03 1 1245 . 145 LYS CA C 57.35 0.50 1 1246 . 145 LYS CB C 33.07 0.50 1 1247 . 145 LYS CD C 29.32 0.50 1 1248 . 145 LYS CG C 25.02 0.50 1 1249 . 145 LYS N N 120.02 0.25 1 1250 . 146 ILE HA H 4.33 0.03 1 1251 . 146 ILE HB H 1.74 0.03 1 1252 . 146 ILE HD1 H 0.77 0.03 1 1253 . 146 ILE HG13 H 1.11 0.03 2 1254 . 146 ILE HG2 H 0.81 0.03 1 1255 . 146 ILE H H 8.26 0.03 1 1256 . 146 ILE C C 176.44 0.50 1 1257 . 146 ILE CA C 59.34 0.50 1 1258 . 146 ILE CB C 39.39 0.50 1 1259 . 146 ILE CD1 C 13.65 0.50 1 1260 . 146 ILE CG1 C 27.73 0.50 1 1261 . 146 ILE CG2 C 17.62 0.50 1 1262 . 146 ILE N N 126.16 0.25 1 1263 . 147 ILE HA H 3.84 0.03 1 1264 . 147 ILE HB H 1.75 0.03 1 1265 . 147 ILE HD1 H 0.79 0.03 1 1266 . 147 ILE HG13 H 1.11 0.03 2 1267 . 147 ILE HG12 H 1.53 0.03 2 1268 . 147 ILE HG2 H 0.79 0.03 1 1269 . 147 ILE H H 8.83 0.03 1 1270 . 147 ILE C C 174.81 0.50 1 1271 . 147 ILE CA C 62.35 0.50 1 1272 . 147 ILE CB C 38.48 0.50 1 1273 . 147 ILE CD1 C 13.59 0.50 1 1274 . 147 ILE CG1 C 28.51 0.50 1 1275 . 147 ILE CG2 C 17.50 0.50 1 1276 . 147 ILE N N 129.02 0.25 1 1277 . 148 ASP HA H 4.85 0.03 1 1278 . 148 ASP HB3 H 2.52 0.03 2 1279 . 148 ASP HB2 H 2.85 0.03 2 1280 . 148 ASP H H 8.31 0.03 1 1281 . 148 ASP C C 177.30 0.50 1 1282 . 148 ASP CA C 52.63 0.50 1 1283 . 148 ASP CB C 41.25 0.50 1 1284 . 148 ASP N N 126.06 0.25 1 1285 . 149 LEU HA H 4.16 0.03 1 1286 . 149 LEU HB3 H 0.92 0.03 2 1287 . 149 LEU HB2 H 1.59 0.03 2 1288 . 149 LEU HD1 H 0.76 0.03 2 1289 . 149 LEU HD2 H 0.84 0.03 2 1290 . 149 LEU HG H 1.82 0.03 1 1291 . 149 LEU H H 8.50 0.03 1 1292 . 149 LEU C C 177.11 0.50 1 1293 . 149 LEU CA C 56.11 0.50 1 1294 . 149 LEU CB C 41.27 0.50 1 1295 . 149 LEU CD1 C 23.73 0.50 2 1296 . 149 LEU CD2 C 25.82 0.50 2 1297 . 149 LEU N N 125.84 0.25 1 1298 . 150 SER HA H 4.40 0.03 1 1299 . 150 SER HB3 H 3.96 0.03 2 1300 . 150 SER H H 8.54 0.03 1 1301 . 150 SER C C 175.47 0.50 1 1302 . 150 SER CA C 60.81 0.50 1 1303 . 150 SER CB C 64.01 0.50 1 1304 . 150 SER N N 115.67 0.25 1 1305 . 151 ALA HA H 4.44 0.03 1 1306 . 151 ALA HB H 1.33 0.03 1 1307 . 151 ALA H H 7.41 0.03 1 1308 . 151 ALA C C 177.01 0.50 1 1309 . 151 ALA CA C 51.80 0.50 1 1310 . 151 ALA CB C 19.22 0.50 1 1311 . 151 ALA N N 124.54 0.25 1 1312 . 152 ILE HA H 3.85 0.03 1 1313 . 152 ILE HB H 1.74 0.03 1 1314 . 152 ILE HD1 H 0.80 0.03 1 1315 . 152 ILE HG13 H 1.08 0.03 2 1316 . 152 ILE HG12 H 1.54 0.03 2 1317 . 152 ILE HG2 H 0.99 0.03 1 1318 . 152 ILE H H 6.88 0.03 1 1319 . 152 ILE CA C 63.02 0.50 1 1320 . 152 ILE CB C 38.64 0.50 1 1321 . 152 ILE CD1 C 14.31 0.50 1 1322 . 152 ILE CG2 C 18.56 0.50 1 1323 . 152 ILE N N 118.96 0.25 1 1324 . 153 GLN HA H 4.34 0.03 1 1325 . 153 GLN HB3 H 1.87 0.03 2 1326 . 153 GLN HB2 H 2.17 0.03 2 1327 . 153 GLN HE21 H 6.73 0.03 2 1328 . 153 GLN HE22 H 7.33 0.03 2 1329 . 153 GLN HG3 H 2.36 0.03 2 1330 . 153 GLN H H 8.66 0.03 1 1331 . 153 GLN C C 175.17 0.50 1 1332 . 153 GLN CA C 56.47 0.50 1 1333 . 153 GLN CB C 30.79 0.50 1 1334 . 153 GLN CG C 33.74 0.50 1 1335 . 153 GLN N N 124.88 0.25 1 1336 . 153 GLN NE2 N 111.57 0.25 1 1337 . 154 ASP HA H 4.85 0.03 1 1338 . 154 ASP HB3 H 2.68 0.03 2 1339 . 154 ASP HB2 H 2.35 0.03 2 1340 . 154 ASP H H 7.45 0.03 1 1341 . 154 ASP C C 173.55 0.50 1 1342 . 154 ASP CA C 53.07 0.50 1 1343 . 154 ASP CB C 43.90 0.50 1 1344 . 154 ASP N N 119.86 0.25 1 1345 . 155 GLU HA H 4.92 0.03 1 1346 . 155 GLU HB3 H 2.00 0.03 2 1347 . 155 GLU HB2 H 1.84 0.03 2 1348 . 155 GLU HG3 H 2.34 0.03 2 1349 . 155 GLU H H 8.10 0.03 1 1350 . 155 GLU C C 177.72 0.50 1 1351 . 155 GLU CA C 56.73 0.50 1 1352 . 155 GLU CB C 29.78 0.50 1 1353 . 155 GLU CG C 37.36 0.50 1 1354 . 155 GLU N N 117.39 0.25 1 1355 . 156 VAL HA H 5.18 0.03 1 1356 . 156 VAL HB H 2.00 0.03 1 1357 . 156 VAL HG1 H 0.75 0.03 2 1358 . 156 VAL H H 8.31 0.03 1 1359 . 156 VAL C C 175.38 0.50 1 1360 . 156 VAL CA C 59.12 0.50 1 1361 . 156 VAL CB C 37.38 0.50 1 1362 . 156 VAL CG1 C 22.54 0.50 2 1363 . 156 VAL N N 115.39 0.25 1 1364 . 157 ILE HA H 3.87 0.03 1 1365 . 157 ILE HB H 1.14 0.03 1 1366 . 157 ILE HG2 H 0.37 0.03 1 1367 . 157 ILE H H 8.58 0.03 1 1368 . 157 ILE C C 174.65 0.50 1 1369 . 157 ILE CA C 60.92 0.50 1 1370 . 157 ILE CB C 39.53 0.50 1 1371 . 157 ILE CG2 C 18.12 0.50 1 1372 . 157 ILE N N 121.02 0.25 1 1373 . 158 LEU HA H 4.64 0.03 1 1374 . 158 LEU HB3 H 1.48 0.03 2 1375 . 158 LEU HB2 H 1.58 0.03 2 1376 . 158 LEU HD1 H 0.88 0.03 2 1377 . 158 LEU HG H 1.61 0.03 1 1378 . 158 LEU H H 7.80 0.03 1 1379 . 158 LEU C C 174.78 0.50 1 1380 . 158 LEU CA C 55.25 0.50 1 1381 . 158 LEU CB C 44.48 0.50 1 1382 . 158 LEU CD1 C 26.21 0.50 2 1383 . 158 LEU CG C 27.75 0.50 1 1384 . 158 LEU N N 128.19 0.25 1 1385 . 159 VAL HA H 5.08 0.03 1 1386 . 159 VAL HB H 1.76 0.03 1 1387 . 159 VAL HG1 H 0.63 0.03 2 1388 . 159 VAL HG2 H 0.68 0.03 2 1389 . 159 VAL H H 8.69 0.03 1 1390 . 159 VAL C C 173.98 0.50 1 1391 . 159 VAL CA C 60.95 0.50 1 1392 . 159 VAL CB C 33.46 0.50 1 1393 . 159 VAL N N 125.12 0.25 1 1394 . 160 ALA HA H 4.88 0.03 1 1395 . 160 ALA HB H 1.29 0.03 1 1396 . 160 ALA H H 8.27 0.03 1 1397 . 160 ALA C C 175.93 0.50 1 1398 . 160 ALA CA C 50.19 0.50 1 1399 . 160 ALA CB C 24.65 0.50 1 1400 . 160 ALA N N 125.78 0.25 1 1401 . 161 ALA HA H 4.24 0.03 1 1402 . 161 ALA HB H 1.52 0.03 1 1403 . 161 ALA H H 9.35 0.03 1 1404 . 161 ALA C C 177.24 0.50 1 1405 . 161 ALA CA C 56.08 0.50 1 1406 . 161 ALA CB C 18.36 0.50 1 1407 . 161 ALA N N 125.02 0.25 1 1408 . 162 ASP HA H 4.47 0.03 1 1409 . 162 ASP HB2 H 2.88 0.03 2 1410 . 162 ASP H H 7.50 0.03 1 1411 . 162 ASP C C 174.14 0.50 1 1412 . 162 ASP CA C 52.92 0.50 1 1413 . 162 ASP CB C 42.72 0.50 1 1414 . 162 ASP N N 109.63 0.25 1 1415 . 163 LEU HB2 H 1.38 0.03 2 1416 . 163 LEU HD1 H 0.66 0.03 2 1417 . 163 LEU HD2 H 0.54 0.03 2 1418 . 163 LEU HG H 1.25 0.03 1 1419 . 163 LEU H H 7.98 0.03 1 1420 . 163 LEU C C 178.84 0.50 1 1421 . 163 LEU CA C 55.00 0.50 1 1422 . 163 LEU CB C 45.87 0.50 1 1423 . 163 LEU CD1 C 24.66 0.50 2 1424 . 163 LEU CD2 C 25.96 0.50 2 1425 . 163 LEU CG C 27.57 0.50 1 1426 . 163 LEU N N 119.11 0.25 1 1427 . 164 THR HA H 4.74 0.03 1 1428 . 164 THR HB H 4.40 0.03 1 1429 . 164 THR HG2 H 1.18 0.03 1 1430 . 164 THR H H 8.92 0.03 1 1431 . 164 THR CA C 59.67 0.50 1 1432 . 164 THR CB C 68.70 0.50 1 1433 . 164 THR CG2 C 22.02 0.50 1 1434 . 164 THR N N 115.15 0.25 1 1435 . 165 PRO HB2 H 1.84 0.03 2 1436 . 165 PRO HD3 H 3.17 0.03 2 1437 . 165 PRO HG3 H 1.59 0.03 2 1438 . 165 PRO CA C 65.28 0.50 1 1439 . 165 PRO CD C 43.71 0.50 1 1440 . 166 SER HA H 4.01 0.03 1 1441 . 166 SER HB2 H 3.75 0.03 2 1442 . 166 SER H H 8.68 0.03 1 1443 . 166 SER CA C 61.79 0.50 1 1444 . 166 SER CB C 61.94 0.50 1 1445 . 166 SER N N 112.05 0.25 1 1446 . 167 GLU H H 7.43 0.03 1 1447 . 167 GLU C C 179.06 0.50 1 1448 . 167 GLU CA C 59.31 0.50 1 1449 . 167 GLU CB C 30.22 0.50 1 1450 . 167 GLU CG C 37.43 0.50 1 1451 . 167 GLU N N 121.22 0.25 1 1452 . 168 THR HA H 3.77 0.03 1 1453 . 168 THR HB H 4.25 0.03 1 1454 . 168 THR HG2 H 1.17 0.03 1 1455 . 168 THR H H 8.36 0.03 1 1456 . 168 THR CA C 65.66 0.50 1 1457 . 168 THR CB C 68.25 0.50 1 1458 . 168 THR CG2 C 22.82 0.50 1 1459 . 168 THR N N 110.19 0.25 1 1460 . 169 ALA HA H 4.13 0.03 1 1461 . 169 ALA HB H 1.32 0.03 1 1462 . 169 ALA H H 7.62 0.03 1 1463 . 169 ALA C C 177.44 0.50 1 1464 . 169 ALA CA C 54.17 0.50 1 1465 . 169 ALA CB C 19.67 0.50 1 1466 . 169 ALA N N 119.89 0.25 1 1467 . 170 GLN HA H 4.12 0.03 1 1468 . 170 GLN HB2 H 2.15 0.03 2 1469 . 170 GLN HE21 H 7.00 0.03 2 1470 . 170 GLN HE22 H 7.68 0.03 2 1471 . 170 GLN H H 7.08 0.03 1 1472 . 170 GLN C C 175.65 0.50 1 1473 . 170 GLN CA C 55.97 0.50 1 1474 . 170 GLN CB C 31.80 0.50 1 1475 . 170 GLN CG C 35.19 0.50 1 1476 . 170 GLN N N 111.44 0.25 1 1477 . 170 GLN NE2 N 112.24 0.25 1 1478 . 171 LEU HA H 3.78 0.03 1 1479 . 171 LEU HB2 H 1.15 0.03 2 1480 . 171 LEU HD1 H 0.89 0.03 2 1481 . 171 LEU HD2 H 0.83 0.03 2 1482 . 171 LEU HG H 1.95 0.03 1 1483 . 171 LEU H H 7.10 0.03 1 1484 . 171 LEU CA C 55.75 0.50 1 1485 . 171 LEU CB C 43.93 0.50 1 1486 . 171 LEU CD1 C 26.08 0.50 2 1487 . 171 LEU CD2 C 24.95 0.50 2 1488 . 171 LEU CG C 26.64 0.50 1 1489 . 171 LEU N N 116.67 0.25 1 1490 . 172 ASN HA H 4.79 0.03 1 1491 . 172 ASN HB3 H 2.93 0.03 2 1492 . 172 ASN HB2 H 2.84 0.03 2 1493 . 172 ASN HD21 H 6.95 0.03 2 1494 . 172 ASN HD22 H 7.58 0.03 2 1495 . 172 ASN H H 7.77 0.03 1 1496 . 172 ASN C C 176.19 0.50 1 1497 . 172 ASN CA C 51.89 0.50 1 1498 . 172 ASN CB C 37.16 0.50 1 1499 . 172 ASN N N 118.05 0.25 1 1500 . 172 ASN ND2 N 110.07 0.25 1 1501 . 173 LEU HA H 3.96 0.03 1 1502 . 173 LEU HB3 H 1.71 0.03 2 1503 . 173 LEU HB2 H 1.60 0.03 2 1504 . 173 LEU HD1 H 0.94 0.03 2 1505 . 173 LEU HD2 H 0.87 0.03 2 1506 . 173 LEU HG H 1.38 0.03 1 1507 . 173 LEU H H 8.30 0.03 1 1508 . 173 LEU C C 178.03 0.50 1 1509 . 173 LEU CA C 57.44 0.50 1 1510 . 173 LEU CB C 41.38 0.50 1 1511 . 173 LEU CD1 C 25.81 0.50 2 1512 . 173 LEU CD2 C 23.53 0.50 2 1513 . 173 LEU CG C 29.34 0.50 1 1514 . 173 LEU N N 125.32 0.25 1 1515 . 174 LYS HA H 4.22 0.03 1 1516 . 174 LYS HB2 H 1.82 0.03 2 1517 . 174 LYS HG3 H 1.50 0.03 2 1518 . 174 LYS H H 7.88 0.03 1 1519 . 174 LYS C C 177.70 0.50 1 1520 . 174 LYS CA C 57.53 0.50 1 1521 . 174 LYS CB C 32.16 0.50 1 1522 . 174 LYS CD C 28.68 0.50 1 1523 . 174 LYS CE C 42.37 0.50 1 1524 . 174 LYS CG C 25.32 0.50 1 1525 . 174 LYS N N 115.21 0.25 1 1526 . 175 LYS HA H 4.36 0.03 1 1527 . 175 LYS H H 7.50 0.03 1 1528 . 175 LYS CA C 54.63 0.50 1 1529 . 175 LYS CB C 33.30 0.50 1 1530 . 175 LYS N N 115.57 0.25 1 1531 . 176 VAL HA H 4.33 0.03 1 1532 . 176 VAL HB H 1.84 0.03 1 1533 . 176 VAL HG1 H 0.85 0.03 2 1534 . 176 VAL HG2 H 0.58 0.03 2 1535 . 176 VAL H H 7.15 0.03 1 1536 . 176 VAL C C 175.16 0.50 1 1537 . 176 VAL CA C 62.25 0.50 1 1538 . 176 VAL CB C 32.55 0.50 1 1539 . 176 VAL CG1 C 22.57 0.50 2 1540 . 176 VAL CG2 C 22.50 0.50 2 1541 . 176 VAL N N 116.98 0.25 1 1542 . 177 LEU HA H 4.24 0.03 1 1543 . 177 LEU H H 8.79 0.03 1 1544 . 177 LEU C C 176.80 0.50 1 1545 . 177 LEU CA C 54.73 0.50 1 1546 . 177 LEU CB C 44.02 0.50 1 1547 . 177 LEU N N 123.07 0.25 1 1548 . 178 GLY HA3 H 3.74 0.03 2 1549 . 178 GLY HA2 H 3.90 0.03 2 1550 . 178 GLY H H 6.97 0.03 1 1551 . 178 GLY C C 180.11 0.50 1 1552 . 178 GLY CA C 45.40 0.50 1 1553 . 178 GLY N N 100.77 0.25 1 1554 . 179 PHE HA H 5.60 0.03 1 1555 . 179 PHE HD1 H 6.85 0.03 2 1556 . 179 PHE HE1 H 6.85 0.03 2 1557 . 179 PHE H H 7.80 0.03 1 1558 . 179 PHE C C 174.20 0.50 1 1559 . 179 PHE CA C 56.43 0.50 1 1560 . 179 PHE CB C 44.15 0.50 1 1561 . 179 PHE CD1 C 132.58 0.50 2 1562 . 179 PHE CE1 C 130.29 0.50 2 1563 . 179 PHE N N 114.83 0.25 1 1564 . 180 ILE HA H 5.48 0.03 1 1565 . 180 ILE HB H 1.55 0.03 1 1566 . 180 ILE HD1 H 0.66 0.03 1 1567 . 180 ILE HG2 H 0.90 0.03 1 1568 . 180 ILE H H 8.80 0.03 1 1569 . 180 ILE C C 176.08 0.50 1 1570 . 180 ILE CA C 60.04 0.50 1 1571 . 180 ILE CB C 41.13 0.50 1 1572 . 180 ILE CD1 C 16.61 0.50 1 1573 . 180 ILE CG2 C 20.77 0.50 1 1574 . 180 ILE N N 119.43 0.25 1 1575 . 181 THR HA H 6.35 0.03 1 1576 . 181 THR HB H 4.43 0.03 1 1577 . 181 THR HG2 H 1.02 0.03 1 1578 . 181 THR H H 8.24 0.03 1 1579 . 181 THR C C 177.94 0.50 1 1580 . 181 THR CA C 58.64 0.50 1 1581 . 181 THR CB C 72.10 0.50 1 1582 . 181 THR N N 111.42 0.25 1 1583 . 182 ASP H H 8.10 0.03 1 1584 . 182 ASP C C 178.15 0.50 1 1585 . 182 ASP CA C 56.71 0.50 1 1586 . 182 ASP CB C 41.50 0.50 1 1587 . 182 ASP N N 124.07 0.25 1 1588 . 183 ALA HA H 4.84 0.03 1 1589 . 183 ALA HB H 1.51 0.03 1 1590 . 183 ALA H H 8.57 0.03 1 1591 . 183 ALA CA C 50.91 0.50 1 1592 . 183 ALA CB C 20.89 0.50 1 1593 . 183 ALA N N 121.95 0.25 1 1594 . 184 GLY HA2 H 4.59 0.03 2 1595 . 184 GLY H H 8.44 0.03 1 1596 . 184 GLY C C 172.93 0.50 1 1597 . 184 GLY CA C 45.23 0.50 1 1598 . 184 GLY N N 109.75 0.25 1 1599 . 185 GLY H H 7.79 0.03 1 1600 . 185 GLY N N 104.06 0.25 1 1601 . 187 THR HA H 4.40 0.03 1 1602 . 187 THR HB H 4.58 0.03 1 1603 . 187 THR HG2 H 1.09 0.03 1 1604 . 187 THR C C 173.67 0.50 1 1605 . 187 THR CA C 60.74 0.50 1 1606 . 187 THR CB C 68.44 0.50 1 1607 . 187 THR CG2 C 21.99 0.50 1 1608 . 188 SER HA H 4.42 0.03 1 1609 . 188 SER HB3 H 3.83 0.03 2 1610 . 188 SER H H 7.44 0.03 1 1611 . 188 SER CA C 58.51 0.50 1 1612 . 188 SER CB C 64.83 0.50 1 1613 . 188 SER N N 117.09 0.25 1 1614 . 189 HIS HA H 4.18 0.03 1 1615 . 189 HIS HB3 H 3.23 0.03 2 1616 . 189 HIS HB2 H 3.06 0.03 2 1617 . 189 HIS HD2 H 6.35 0.03 1 1618 . 189 HIS H H 9.17 0.03 1 1619 . 189 HIS C C 176.94 0.50 1 1620 . 189 HIS CA C 60.68 0.50 1 1621 . 189 HIS CB C 28.94 0.50 1 1622 . 189 HIS CD2 C 124.14 0.50 1 1623 . 189 HIS N N 121.87 0.25 1 1624 . 190 THR H H 8.45 0.03 1 1625 . 190 THR N N 114.30 0.25 1 1626 . 191 SER CA C 62.98 0.50 1 1627 . 191 SER CB C 63.01 0.50 1 1628 . 192 ILE HA H 3.47 0.03 1 1629 . 192 ILE HB H 1.77 0.03 1 1630 . 192 ILE HD1 H 0.74 0.03 1 1631 . 192 ILE HG2 H 0.85 0.03 1 1632 . 192 ILE H H 7.97 0.03 1 1633 . 192 ILE C C 179.74 0.50 1 1634 . 192 ILE CA C 64.94 0.50 1 1635 . 192 ILE CB C 38.44 0.50 1 1636 . 192 ILE CD1 C 13.27 0.50 1 1637 . 192 ILE CG2 C 17.63 0.50 1 1638 . 192 ILE N N 120.97 0.25 1 1639 . 193 MET HA H 4.00 0.03 1 1640 . 193 MET HB3 H 1.58 0.03 2 1641 . 193 MET HG3 H 1.94 0.03 2 1642 . 193 MET H H 8.34 0.03 1 1643 . 193 MET C C 178.53 0.50 1 1644 . 193 MET CA C 58.27 0.50 1 1645 . 193 MET CB C 31.44 0.50 1 1646 . 193 MET CG C 32.37 0.50 1 1647 . 193 MET N N 120.55 0.25 1 1648 . 194 ALA HA H 3.81 0.03 1 1649 . 194 ALA HB H 1.40 0.03 1 1650 . 194 ALA H H 8.50 0.03 1 1651 . 194 ALA C C 179.85 0.50 1 1652 . 194 ALA CA C 56.68 0.50 1 1653 . 194 ALA CB C 18.59 0.50 1 1654 . 194 ALA N N 121.80 0.25 1 1655 . 195 ARG HA H 4.25 0.03 1 1656 . 195 ARG HB3 H 2.05 0.03 2 1657 . 195 ARG HD3 H 3.84 0.03 2 1658 . 195 ARG H H 8.14 0.03 1 1659 . 195 ARG C C 180.76 0.50 1 1660 . 195 ARG CA C 60.32 0.50 1 1661 . 195 ARG CB C 30.96 0.50 1 1662 . 195 ARG CD C 44.59 0.50 1 1663 . 195 ARG N N 115.85 0.25 1 1664 . 196 SER HA H 4.29 0.03 1 1665 . 196 SER HB3 H 4.06 0.03 2 1666 . 196 SER HB2 H 4.11 0.03 2 1667 . 196 SER H H 8.01 0.03 1 1668 . 196 SER C C 175.42 0.50 1 1669 . 196 SER CA C 61.94 0.50 1 1670 . 196 SER CB C 63.33 0.50 1 1671 . 196 SER N N 116.20 0.25 1 1672 . 197 LEU HA H 4.38 0.03 1 1673 . 197 LEU HB3 H 1.68 0.03 2 1674 . 197 LEU H H 7.55 0.03 1 1675 . 197 LEU C C 175.39 0.50 1 1676 . 197 LEU CA C 54.69 0.50 1 1677 . 197 LEU CB C 43.37 0.50 1 1678 . 197 LEU CD2 C 22.39 0.50 2 1679 . 197 LEU CG C 26.92 0.50 1 1680 . 197 LEU N N 120.25 0.25 1 1681 . 198 GLU HA H 3.79 0.03 1 1682 . 198 GLU HB2 H 2.24 0.03 2 1683 . 198 GLU HG3 H 2.20 0.03 2 1684 . 198 GLU H H 7.81 0.03 1 1685 . 198 GLU CA C 57.72 0.50 1 1686 . 198 GLU CB C 27.31 0.50 1 1687 . 198 GLU N N 116.07 0.25 1 1688 . 199 LEU HA H 4.86 0.03 1 1689 . 199 LEU HD1 H 0.82 0.03 2 1690 . 199 LEU H H 8.13 0.03 1 1691 . 199 LEU CA C 51.27 0.50 1 1692 . 199 LEU N N 119.48 0.25 1 1693 . 200 PRO HA H 4.20 0.03 1 1694 . 200 PRO HB2 H 1.65 0.03 2 1695 . 200 PRO C C 175.90 0.50 1 1696 . 200 PRO CA C 62.23 0.50 1 1697 . 200 PRO CB C 32.79 0.50 1 1698 . 201 ALA HA H 5.48 0.03 1 1699 . 201 ALA HB H 0.87 0.03 1 1700 . 201 ALA H H 8.67 0.03 1 1701 . 201 ALA C C 176.09 0.50 1 1702 . 201 ALA CA C 51.98 0.50 1 1703 . 201 ALA CB C 22.33 0.50 1 1704 . 201 ALA N N 118.76 0.25 1 1705 . 202 ILE HA H 4.61 0.03 1 1706 . 202 ILE HB H 1.25 0.03 1 1707 . 202 ILE HG2 H 0.63 0.03 1 1708 . 202 ILE H H 7.76 0.03 1 1709 . 202 ILE C C 174.30 0.50 1 1710 . 202 ILE CA C 61.24 0.50 1 1711 . 202 ILE CB C 42.04 0.50 1 1712 . 202 ILE N N 122.10 0.25 1 1713 . 203 VAL HA H 5.28 0.03 1 1714 . 203 VAL HB H 2.26 0.03 1 1715 . 203 VAL HG1 H 0.66 0.03 2 1716 . 203 VAL HG2 H 0.41 0.03 2 1717 . 203 VAL H H 8.33 0.03 1 1718 . 203 VAL C C 176.80 0.50 1 1719 . 203 VAL CA C 57.89 0.50 1 1720 . 203 VAL CB C 34.21 0.50 1 1721 . 203 VAL CG1 C 20.13 0.50 2 1722 . 203 VAL CG2 C 17.75 0.50 2 1723 . 203 VAL N N 116.02 0.25 1 1724 . 204 GLY HA2 H 3.63 0.03 2 1725 . 204 GLY H H 7.37 0.03 1 1726 . 204 GLY C C 176.32 0.50 1 1727 . 204 GLY CA C 48.83 0.50 1 1728 . 204 GLY N N 106.14 0.25 1 1729 . 205 THR HA H 4.53 0.03 1 1730 . 205 THR HB H 4.15 0.03 1 1731 . 205 THR HG2 H 0.85 0.03 1 1732 . 205 THR H H 7.80 0.03 1 1733 . 205 THR C C 177.69 0.50 1 1734 . 205 THR CA C 63.44 0.50 1 1735 . 205 THR CB C 71.22 0.50 1 1736 . 205 THR CG2 C 22.90 0.50 1 1737 . 205 THR N N 106.12 0.25 1 1738 . 206 GLY HA3 H 3.51 0.03 2 1739 . 206 GLY HA2 H 4.53 0.03 2 1740 . 206 GLY H H 9.97 0.03 1 1741 . 206 GLY C C 176.24 0.50 1 1742 . 206 GLY CA C 47.56 0.50 1 1743 . 206 GLY N N 115.28 0.25 1 1744 . 207 SER HA H 4.73 0.03 1 1745 . 207 SER HB3 H 4.05 0.03 2 1746 . 207 SER HB2 H 3.65 0.03 2 1747 . 207 SER H H 7.77 0.03 1 1748 . 207 SER CA C 58.11 0.50 1 1749 . 207 SER CB C 64.17 0.50 1 1750 . 207 SER N N 112.50 0.25 1 1751 . 208 VAL HA H 3.79 0.03 1 1752 . 208 VAL HB H 2.18 0.03 1 1753 . 208 VAL HG1 H 0.84 0.03 2 1754 . 208 VAL HG2 H 0.75 0.03 2 1755 . 208 VAL H H 7.85 0.03 1 1756 . 208 VAL C C 177.50 0.50 1 1757 . 208 VAL CA C 67.25 0.50 1 1758 . 208 VAL CB C 30.55 0.50 1 1759 . 208 VAL CG1 C 23.33 0.50 2 1760 . 208 VAL CG2 C 20.11 0.50 2 1761 . 208 VAL N N 127.36 0.25 1 1762 . 209 THR HA H 3.73 0.03 1 1763 . 209 THR HG2 H 1.04 0.03 1 1764 . 209 THR H H 9.74 0.03 1 1765 . 209 THR C C 176.00 0.50 1 1766 . 209 THR CA C 64.97 0.50 1 1767 . 209 THR CB C 69.51 0.50 1 1768 . 209 THR N N 112.88 0.25 1 1769 . 210 SER HA H 4.63 0.03 1 1770 . 210 SER HB3 H 3.94 0.03 2 1771 . 210 SER HB2 H 3.92 0.03 2 1772 . 210 SER H H 7.63 0.03 1 1773 . 210 SER CA C 59.38 0.50 1 1774 . 210 SER CB C 64.53 0.50 1 1775 . 210 SER N N 114.17 0.25 1 1776 . 211 GLN HA H 4.43 0.03 1 1777 . 211 GLN HB2 H 2.29 0.03 2 1778 . 211 GLN HG2 H 2.15 0.03 2 1779 . 211 GLN H H 7.65 0.03 1 1780 . 211 GLN C C 174.48 0.50 1 1781 . 211 GLN CA C 56.86 0.50 1 1782 . 211 GLN CB C 32.62 0.50 1 1783 . 211 GLN CG C 34.99 0.50 1 1784 . 211 GLN N N 119.06 0.25 1 1785 . 212 VAL HA H 4.17 0.03 1 1786 . 212 VAL HB H 1.81 0.03 1 1787 . 212 VAL HG1 H 0.75 0.03 2 1788 . 212 VAL HG2 H 0.84 0.03 2 1789 . 212 VAL H H 7.30 0.03 1 1790 . 212 VAL C C 172.99 0.50 1 1791 . 212 VAL CA C 61.21 0.50 1 1792 . 212 VAL CB C 34.88 0.50 1 1793 . 212 VAL CG1 C 23.32 0.50 2 1794 . 212 VAL N N 118.57 0.25 1 1795 . 213 LYS HA H 4.50 0.03 1 1796 . 213 LYS HB3 H 1.70 0.03 2 1797 . 213 LYS HE3 H 2.99 0.03 2 1798 . 213 LYS H H 8.86 0.03 1 1799 . 213 LYS C C 175.95 0.50 1 1800 . 213 LYS CA C 53.91 0.50 1 1801 . 213 LYS CB C 35.15 0.50 1 1802 . 213 LYS CD C 29.08 0.50 1 1803 . 213 LYS CE C 42.47 0.50 1 1804 . 213 LYS CG C 24.37 0.50 1 1805 . 213 LYS N N 124.05 0.25 1 1806 . 214 ASN HA H 4.16 0.03 1 1807 . 214 ASN HB2 H 2.63 0.03 2 1808 . 214 ASN HD21 H 6.94 0.03 2 1809 . 214 ASN HD22 H 7.45 0.03 2 1810 . 214 ASN H H 8.46 0.03 1 1811 . 214 ASN C C 176.84 0.50 1 1812 . 214 ASN CA C 55.78 0.50 1 1813 . 214 ASN CB C 39.09 0.50 1 1814 . 214 ASN N N 118.16 0.25 1 1815 . 214 ASN ND2 N 111.78 0.25 1 1816 . 215 ASP HA H 4.22 0.03 1 1817 . 215 ASP HB3 H 2.95 0.03 2 1818 . 215 ASP HB2 H 3.16 0.03 2 1819 . 215 ASP H H 8.84 0.03 1 1820 . 215 ASP CA C 57.68 0.50 1 1821 . 215 ASP CB C 39.80 0.50 1 1822 . 215 ASP N N 116.34 0.25 1 1823 . 216 ASP HA H 4.75 0.03 1 1824 . 216 ASP HB2 H 2.72 0.03 2 1825 . 216 ASP H H 7.89 0.03 1 1826 . 216 ASP CA C 56.32 0.50 1 1827 . 216 ASP CB C 42.23 0.50 1 1828 . 216 ASP N N 120.84 0.25 1 1829 . 217 TYR HA H 4.42 0.03 1 1830 . 217 TYR HB3 H 3.14 0.03 2 1831 . 217 TYR H H 8.54 0.03 1 1832 . 217 TYR C C 174.13 0.50 1 1833 . 217 TYR CA C 59.23 0.50 1 1834 . 217 TYR CB C 39.83 0.50 1 1835 . 217 TYR N N 122.76 0.25 1 1836 . 218 LEU HA H 5.44 0.03 1 1837 . 218 LEU HB2 H 1.65 0.03 2 1838 . 218 LEU HD1 H 0.72 0.03 2 1839 . 218 LEU HD2 H 0.53 0.03 2 1840 . 218 LEU HG H 1.56 0.03 1 1841 . 218 LEU H H 8.58 0.03 1 1842 . 218 LEU C C 176.40 0.50 1 1843 . 218 LEU CA C 52.83 0.50 1 1844 . 218 LEU CB C 45.74 0.50 1 1845 . 218 LEU CD1 C 25.36 0.50 2 1846 . 218 LEU CG C 27.02 0.50 1 1847 . 218 LEU N N 126.80 0.25 1 1848 . 219 ILE HA H 4.21 0.03 1 1849 . 219 ILE HB H 1.66 0.03 1 1850 . 219 ILE HD1 H 0.48 0.03 1 1851 . 219 ILE HG2 H 0.09 0.03 1 1852 . 219 ILE H H 7.95 0.03 1 1853 . 219 ILE C C 174.80 0.50 1 1854 . 219 ILE CA C 61.25 0.50 1 1855 . 219 ILE CB C 39.83 0.50 1 1856 . 219 ILE CD1 C 15.49 0.50 1 1857 . 219 ILE CG2 C 16.62 0.50 1 1858 . 219 ILE N N 114.56 0.25 1 1859 . 220 LEU HA H 4.29 0.03 1 1860 . 220 LEU HD1 H 0.68 0.03 2 1861 . 220 LEU HD2 H 0.64 0.03 2 1862 . 220 LEU HG H 1.54 0.03 1 1863 . 220 LEU H H 9.07 0.03 1 1864 . 220 LEU C C 172.68 0.50 1 1865 . 220 LEU CA C 53.66 0.50 1 1866 . 220 LEU CB C 44.18 0.50 1 1867 . 220 LEU CD1 C 25.20 0.50 2 1868 . 220 LEU CD2 C 26.55 0.50 2 1869 . 220 LEU N N 130.27 0.25 1 1870 . 221 ASP HA H 5.00 0.03 1 1871 . 221 ASP HB3 H 2.22 0.03 2 1872 . 221 ASP H H 8.59 0.03 1 1873 . 221 ASP C C 175.57 0.50 1 1874 . 221 ASP CA C 52.98 0.50 1 1875 . 221 ASP CB C 40.56 0.50 1 1876 . 221 ASP N N 124.41 0.25 1 1877 . 222 ALA HA H 4.49 0.03 1 1878 . 222 ALA HB H 1.46 0.03 1 1879 . 222 ALA H H 8.38 0.03 1 1880 . 222 ALA C C 175.47 0.50 1 1881 . 222 ALA CA C 51.88 0.50 1 1882 . 222 ALA CB C 18.35 0.50 1 1883 . 222 ALA N N 127.87 0.25 1 1884 . 223 VAL HA H 4.07 0.03 1 1885 . 223 VAL HB H 2.19 0.03 1 1886 . 223 VAL HG1 H 0.83 0.03 2 1887 . 223 VAL HG2 H 0.94 0.03 2 1888 . 223 VAL H H 8.69 0.03 1 1889 . 223 VAL C C 177.47 0.50 1 1890 . 223 VAL CA C 65.51 0.50 1 1891 . 223 VAL CB C 32.82 0.50 1 1892 . 223 VAL CG1 C 21.59 0.50 2 1893 . 223 VAL N N 117.70 0.25 1 1894 . 224 ASN HA H 4.61 0.03 1 1895 . 224 ASN HB3 H 2.62 0.03 2 1896 . 224 ASN HB2 H 2.71 0.03 2 1897 . 224 ASN H H 9.51 0.03 1 1898 . 224 ASN C C 175.40 0.50 1 1899 . 224 ASN CA C 53.37 0.50 1 1900 . 224 ASN CB C 39.36 0.50 1 1901 . 224 ASN N N 116.95 0.25 1 1902 . 225 ASN HA H 4.18 0.03 1 1903 . 225 ASN HB2 H 2.24 0.03 2 1904 . 225 ASN H H 7.58 0.03 1 1905 . 225 ASN C C 172.48 0.50 1 1906 . 225 ASN CA C 53.15 0.50 1 1907 . 225 ASN CB C 36.38 0.50 1 1908 . 225 ASN N N 116.95 0.25 1 1909 . 226 GLN HA H 4.73 0.03 1 1910 . 226 GLN HB3 H 1.57 0.03 2 1911 . 226 GLN HB2 H 1.75 0.03 2 1912 . 226 GLN HE21 H 6.54 0.03 2 1913 . 226 GLN HE22 H 7.17 0.03 2 1914 . 226 GLN HG3 H 1.98 0.03 2 1915 . 226 GLN HG2 H 1.83 0.03 2 1916 . 226 GLN H H 8.70 0.03 1 1917 . 226 GLN CA C 55.69 0.50 1 1918 . 226 GLN CB C 33.72 0.50 1 1919 . 226 GLN CG C 34.01 0.50 1 1920 . 226 GLN N N 118.30 0.25 1 1921 . 226 GLN NE2 N 109.55 0.25 1 1922 . 227 VAL HA H 4.76 0.03 1 1923 . 227 VAL HB H 1.79 0.03 1 1924 . 227 VAL HG1 H 0.73 0.03 2 1925 . 227 VAL HG2 H 0.62 0.03 2 1926 . 227 VAL H H 7.85 0.03 1 1927 . 227 VAL C C 174.96 0.50 1 1928 . 227 VAL CA C 60.80 0.50 1 1929 . 227 VAL CB C 33.86 0.50 1 1930 . 227 VAL CG1 C 22.51 0.50 2 1931 . 227 VAL N N 120.97 0.25 1 1932 . 228 TYR HA H 4.60 0.03 1 1933 . 228 TYR HB2 H 2.87 0.03 2 1934 . 228 TYR HE1 H 6.73 0.03 2 1935 . 228 TYR H H 9.00 0.03 1 1936 . 228 TYR C C 174.84 0.50 1 1937 . 228 TYR CA C 57.28 0.50 1 1938 . 228 TYR CB C 39.44 0.50 1 1939 . 228 TYR CE1 C 118.23 0.50 2 1940 . 228 TYR N N 126.40 0.25 1 1941 . 229 VAL HA H 4.26 0.03 1 1942 . 229 VAL HB H 1.95 0.03 1 1943 . 229 VAL HG1 H 0.91 0.03 2 1944 . 229 VAL HG2 H 0.70 0.03 2 1945 . 229 VAL H H 8.46 0.03 1 1946 . 229 VAL C C 175.62 0.50 1 1947 . 229 VAL CA C 61.98 0.50 1 1948 . 229 VAL CB C 32.85 0.50 1 1949 . 229 VAL CG1 C 21.99 0.50 2 1950 . 229 VAL CG2 C 21.54 0.50 2 1951 . 229 VAL N N 122.91 0.25 1 1952 . 230 ASN HA H 4.85 0.03 1 1953 . 230 ASN HB3 H 2.85 0.03 2 1954 . 230 ASN HB2 H 2.94 0.03 2 1955 . 230 ASN H H 10.03 0.03 1 1956 . 230 ASN CA C 55.02 0.50 1 1957 . 230 ASN CB C 38.18 0.50 1 1958 . 230 ASN N N 124.15 0.25 1 1959 . 231 PRO HA H 4.70 0.03 1 1960 . 231 PRO C C 176.92 0.50 1 1961 . 231 PRO CA C 62.15 0.50 1 1962 . 231 PRO CB C 33.26 0.50 1 1963 . 232 THR HA H 4.31 0.03 1 1964 . 232 THR HB H 4.72 0.03 1 1965 . 232 THR HG2 H 1.42 0.03 1 1966 . 232 THR H H 7.74 0.03 1 1967 . 232 THR CA C 60.97 0.50 1 1968 . 232 THR CB C 70.92 0.50 1 1969 . 232 THR CG2 C 22.46 0.50 1 1970 . 232 THR N N 108.65 0.25 1 1971 . 233 ASN HA H 4.24 0.03 1 1972 . 233 ASN HB3 H 2.70 0.03 2 1973 . 233 ASN HB2 H 2.81 0.03 2 1974 . 233 ASN HD21 H 6.84 0.03 2 1975 . 233 ASN HD22 H 7.58 0.03 2 1976 . 233 ASN H H 8.83 0.03 1 1977 . 233 ASN CA C 56.87 0.50 1 1978 . 233 ASN CB C 37.93 0.50 1 1979 . 233 ASN N N 118.91 0.25 1 1980 . 233 ASN ND2 N 111.82 0.25 1 1981 . 234 GLU HA H 4.08 0.03 1 1982 . 234 GLU HB3 H 2.04 0.03 2 1983 . 234 GLU HB2 H 1.93 0.03 2 1984 . 234 GLU HG3 H 2.28 0.03 2 1985 . 234 GLU H H 8.53 0.03 1 1986 . 234 GLU C C 179.07 0.50 1 1987 . 234 GLU CA C 59.97 0.50 1 1988 . 234 GLU CB C 29.40 0.50 1 1989 . 234 GLU CG C 36.81 0.50 1 1990 . 234 GLU N N 118.34 0.25 1 1991 . 235 VAL HA H 3.48 0.03 1 1992 . 235 VAL HB H 2.00 0.03 1 1993 . 235 VAL HG1 H 0.95 0.03 2 1994 . 235 VAL HG2 H 0.41 0.03 2 1995 . 235 VAL H H 7.18 0.03 1 1996 . 235 VAL C C 177.76 0.50 1 1997 . 235 VAL CA C 66.71 0.50 1 1998 . 235 VAL CB C 31.91 0.50 1 1999 . 235 VAL CG1 C 23.62 0.50 2 2000 . 235 VAL CG2 C 21.66 0.50 2 2001 . 235 VAL N N 121.55 0.25 1 2002 . 236 ILE HA H 3.47 0.03 1 2003 . 236 ILE HB H 1.88 0.03 1 2004 . 236 ILE HD1 H 0.69 0.03 1 2005 . 236 ILE HG2 H 0.91 0.03 1 2006 . 236 ILE H H 8.01 0.03 1 2007 . 236 ILE CA C 67.14 0.50 1 2008 . 236 ILE CB C 38.09 0.50 1 2009 . 236 ILE CD1 C 13.93 0.50 1 2010 . 236 ILE CG2 C 17.72 0.50 1 2011 . 236 ILE N N 120.65 0.25 1 2012 . 237 ASP HA H 4.28 0.03 1 2013 . 237 ASP HB3 H 2.56 0.03 2 2014 . 237 ASP HB2 H 2.67 0.03 2 2015 . 237 ASP H H 8.25 0.03 1 2016 . 237 ASP C C 179.79 0.50 1 2017 . 237 ASP CA C 58.04 0.50 1 2018 . 237 ASP CB C 40.54 0.50 1 2019 . 237 ASP N N 117.87 0.25 1 2020 . 238 LYS HA H 4.07 0.03 1 2021 . 238 LYS HB3 H 1.90 0.03 2 2022 . 238 LYS HB2 H 1.96 0.03 2 2023 . 238 LYS H H 7.68 0.03 1 2024 . 238 LYS C C 180.80 0.50 1 2025 . 238 LYS CA C 59.67 0.50 1 2026 . 238 LYS CB C 32.60 0.50 1 2027 . 238 LYS CD C 29.61 0.50 1 2028 . 238 LYS CG C 25.21 0.50 1 2029 . 238 LYS N N 120.61 0.25 1 2030 . 239 MET HA H 4.76 0.03 1 2031 . 239 MET HE H 1.94 0.03 1 2032 . 239 MET H H 8.46 0.03 1 2033 . 239 MET CA C 55.56 0.50 1 2034 . 239 MET CB C 29.82 0.50 1 2035 . 239 MET CE C 16.15 0.50 1 2036 . 239 MET N N 117.31 0.25 1 2037 . 240 ARG HA H 4.08 0.03 1 2038 . 240 ARG HB3 H 2.04 0.03 2 2039 . 240 ARG HB2 H 1.80 0.03 2 2040 . 240 ARG HD3 H 2.86 0.03 2 2041 . 240 ARG HD2 H 2.76 0.03 2 2042 . 240 ARG HG3 H 1.67 0.03 2 2043 . 240 ARG HG2 H 1.48 0.03 2 2044 . 240 ARG H H 9.03 0.03 1 2045 . 240 ARG C C 178.81 0.50 1 2046 . 240 ARG CA C 59.27 0.50 1 2047 . 240 ARG CB C 29.66 0.50 1 2048 . 240 ARG CD C 43.19 0.50 1 2049 . 240 ARG CG C 27.41 0.50 1 2050 . 240 ARG N N 123.79 0.25 1 2051 . 241 ALA HA H 4.28 0.03 1 2052 . 241 ALA HB H 1.55 0.03 1 2053 . 241 ALA H H 7.43 0.03 1 2054 . 241 ALA CA C 55.36 0.50 1 2055 . 241 ALA CB C 17.89 0.50 1 2056 . 241 ALA N N 121.65 0.25 1 2057 . 242 VAL HA H 3.76 0.03 1 2058 . 242 VAL H H 7.66 0.03 1 2059 . 242 VAL CA C 66.58 0.50 1 2060 . 242 VAL CB C 31.86 0.50 1 2061 . 242 VAL N N 120.28 0.25 1 2062 . 243 GLN HA H 3.90 0.03 1 2063 . 243 GLN HE21 H 6.78 0.03 2 2064 . 243 GLN HE22 H 7.50 0.03 2 2065 . 243 GLN H H 8.40 0.03 1 2066 . 243 GLN CA C 59.80 0.50 1 2067 . 243 GLN CB C 29.13 0.50 1 2068 . 243 GLN CG C 34.23 0.50 1 2069 . 243 GLN N N 119.82 0.25 1 2070 . 243 GLN NE2 N 111.01 0.25 1 2071 . 244 GLU HA H 4.09 0.03 1 2072 . 244 GLU HB3 H 2.03 0.03 2 2073 . 244 GLU H H 8.06 0.03 1 2074 . 244 GLU C C 175.26 0.50 1 2075 . 244 GLU CA C 59.30 0.50 1 2076 . 244 GLU CB C 29.77 0.50 1 2077 . 244 GLU CG C 36.56 0.50 1 2078 . 244 GLU N N 118.70 0.25 1 2079 . 245 GLN HA H 4.13 0.03 1 2080 . 245 GLN HB3 H 2.27 0.03 2 2081 . 245 GLN HE21 H 6.69 0.03 2 2082 . 245 GLN HE22 H 7.54 0.03 2 2083 . 245 GLN HG3 H 2.48 0.03 2 2084 . 245 GLN HG2 H 2.39 0.03 2 2085 . 245 GLN H H 7.92 0.03 1 2086 . 245 GLN CA C 59.02 0.50 1 2087 . 245 GLN CB C 28.49 0.50 1 2088 . 245 GLN CG C 33.83 0.50 1 2089 . 245 GLN N N 120.79 0.25 1 2090 . 245 GLN NE2 N 110.94 0.25 1 2091 . 246 VAL HA H 3.82 0.03 1 2092 . 246 VAL HB H 2.20 0.03 1 2093 . 246 VAL HG1 H 1.05 0.03 2 2094 . 246 VAL HG2 H 0.97 0.03 2 2095 . 246 VAL H H 8.41 0.03 1 2096 . 246 VAL C C 176.08 0.50 1 2097 . 246 VAL CA C 65.68 0.50 1 2098 . 246 VAL CB C 32.26 0.50 1 2099 . 246 VAL CG1 C 22.83 0.50 2 2100 . 246 VAL CG2 C 21.62 0.50 2 2101 . 246 VAL N N 119.64 0.25 1 2102 . 247 ALA HA H 4.25 0.03 1 2103 . 247 ALA HB H 1.54 0.03 1 2104 . 247 ALA H H 8.12 0.03 1 2105 . 247 ALA CA C 54.99 0.50 1 2106 . 247 ALA CB C 18.45 0.50 1 2107 . 247 ALA N N 122.50 0.25 1 2108 . 248 SER HA H 4.32 0.03 1 2109 . 248 SER HB3 H 4.02 0.03 2 2110 . 248 SER H H 8.15 0.03 1 2111 . 248 SER CA C 61.10 0.50 1 2112 . 248 SER CB C 63.42 0.50 1 2113 . 248 SER N N 114.71 0.25 1 2114 . 249 GLU HA H 4.17 0.03 1 2115 . 249 GLU HB3 H 2.10 0.03 2 2116 . 249 GLU H H 8.08 0.03 1 2117 . 249 GLU CA C 58.82 0.50 1 2118 . 249 GLU CB C 29.89 0.50 1 2119 . 249 GLU CG C 36.73 0.50 1 2120 . 249 GLU N N 122.34 0.25 1 2121 . 250 LYS HA H 4.11 0.03 1 2122 . 250 LYS HB3 H 1.90 0.03 2 2123 . 250 LYS HD3 H 1.68 0.03 2 2124 . 250 LYS HE3 H 2.99 0.03 2 2125 . 250 LYS HG3 H 1.58 0.03 2 2126 . 250 LYS HG2 H 1.47 0.03 2 2127 . 250 LYS H H 8.00 0.03 1 2128 . 250 LYS CA C 58.74 0.50 1 2129 . 250 LYS CB C 32.68 0.50 1 2130 . 250 LYS CD C 29.39 0.50 1 2131 . 250 LYS CE C 42.37 0.50 1 2132 . 250 LYS CG C 25.30 0.50 1 2133 . 250 LYS N N 119.59 0.25 1 2134 . 251 ALA HA H 4.21 0.03 1 2135 . 251 ALA HB H 1.49 0.03 1 2136 . 251 ALA H H 7.97 0.03 1 2137 . 251 ALA C C 177.59 0.50 1 2138 . 251 ALA CA C 54.40 0.50 1 2139 . 251 ALA CB C 18.66 0.50 1 2140 . 251 ALA N N 122.40 0.25 1 2141 . 252 GLU HA H 4.13 0.03 1 2142 . 252 GLU HB3 H 2.07 0.03 2 2143 . 252 GLU HG3 H 2.31 0.03 2 2144 . 252 GLU H H 8.04 0.03 1 2145 . 252 GLU CA C 58.27 0.50 1 2146 . 252 GLU CB C 29.82 0.50 1 2147 . 252 GLU CG C 36.26 0.50 1 2148 . 252 GLU N N 118.31 0.25 1 2149 . 253 LEU HA H 4.18 0.03 1 2150 . 253 LEU HB3 H 1.76 0.03 2 2151 . 253 LEU HB2 H 1.59 0.03 2 2152 . 253 LEU HD1 H 0.92 0.03 2 2153 . 253 LEU HD2 H 0.87 0.03 2 2154 . 253 LEU HG H 1.74 0.03 1 2155 . 253 LEU H H 7.91 0.03 1 2156 . 253 LEU C C 176.46 0.50 1 2157 . 253 LEU CA C 56.91 0.50 1 2158 . 253 LEU CB C 42.21 0.50 1 2159 . 253 LEU CD1 C 25.18 0.50 2 2160 . 253 LEU CD2 C 23.65 0.50 2 2161 . 253 LEU CG C 27.30 0.50 1 2162 . 253 LEU N N 120.31 0.25 1 2163 . 254 ALA HA H 4.19 0.03 1 2164 . 254 ALA HB H 1.45 0.03 1 2165 . 254 ALA H H 7.82 0.03 1 2166 . 254 ALA CA C 53.85 0.50 1 2167 . 254 ALA CB C 18.75 0.50 1 2168 . 254 ALA N N 121.45 0.25 1 2169 . 255 LYS HA H 4.21 0.03 1 2170 . 255 LYS HB3 H 1.87 0.03 2 2171 . 255 LYS HD3 H 1.69 0.03 2 2172 . 255 LYS HE3 H 2.97 0.03 2 2173 . 255 LYS HG3 H 1.55 0.03 2 2174 . 255 LYS HG2 H 1.44 0.03 2 2175 . 255 LYS H H 7.61 0.03 1 2176 . 255 LYS C C 176.07 0.50 1 2177 . 255 LYS CA C 57.37 0.50 1 2178 . 255 LYS CB C 33.01 0.50 1 2179 . 255 LYS CD C 29.51 0.50 1 2180 . 255 LYS CE C 42.33 0.50 1 2181 . 255 LYS CG C 25.30 0.50 1 2182 . 255 LYS N N 117.40 0.25 1 2183 . 256 LEU HA H 4.27 0.03 1 2184 . 256 LEU HB3 H 1.73 0.03 2 2185 . 256 LEU HB2 H 1.60 0.03 2 2186 . 256 LEU HD1 H 0.93 0.03 2 2187 . 256 LEU HD2 H 0.86 0.03 2 2188 . 256 LEU HG H 1.71 0.03 1 2189 . 256 LEU H H 7.76 0.03 1 2190 . 256 LEU CA C 55.73 0.50 1 2191 . 256 LEU CB C 42.44 0.50 1 2192 . 256 LEU CD1 C 25.28 0.50 2 2193 . 256 LEU CD2 C 23.50 0.50 2 2194 . 256 LEU CG C 27.14 0.50 1 2195 . 256 LEU N N 120.45 0.25 1 2196 . 257 LYS HA H 4.29 0.03 1 2197 . 257 LYS HB3 H 1.79 0.03 2 2198 . 257 LYS HB2 H 1.86 0.03 2 2199 . 257 LYS HD3 H 1.68 0.03 2 2200 . 257 LYS HE3 H 2.98 0.03 2 2201 . 257 LYS HG3 H 1.44 0.03 2 2202 . 257 LYS H H 7.87 0.03 1 2203 . 257 LYS C C 176.40 0.50 1 2204 . 257 LYS CA C 56.75 0.50 1 2205 . 257 LYS CB C 33.32 0.50 1 2206 . 257 LYS CD C 29.32 0.50 1 2207 . 257 LYS CE C 42.25 0.50 1 2208 . 257 LYS CG C 24.93 0.50 1 2209 . 257 LYS N N 120.13 0.25 1 2210 . 258 ASP HA H 4.59 0.03 1 2211 . 258 ASP HB3 H 2.61 0.03 2 2212 . 258 ASP HB2 H 2.71 0.03 2 2213 . 258 ASP H H 8.13 0.03 1 2214 . 258 ASP C C 175.15 0.50 1 2215 . 258 ASP CA C 54.81 0.50 1 2216 . 258 ASP CB C 41.37 0.50 1 2217 . 258 ASP N N 120.78 0.25 1 2218 . 259 ARG HA H 4.14 0.03 1 2219 . 259 ARG HB3 H 1.83 0.03 2 2220 . 259 ARG HB2 H 1.71 0.03 2 2221 . 259 ARG HD3 H 3.17 0.03 2 2222 . 259 ARG HG3 H 1.58 0.03 2 2223 . 259 ARG H H 7.65 0.03 1 2224 . 259 ARG CA C 57.66 0.50 1 2225 . 259 ARG CB C 31.82 0.50 1 2226 . 259 ARG CD C 43.78 0.50 1 2227 . 259 ARG CG C 27.29 0.50 1 2228 . 259 ARG N N 124.88 0.25 1 stop_ save_ save_chemical_shift_assignment_2 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Sample_label $sample_one stop_ _Sample_conditions_label $sample_cond_1 _Chem_shift_reference_set_label $chemical_shift_reference_one _Mol_system_component_name 'Histidine Phosphocarrier' _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 MET HA H 4.59 0.03 1 2 . 1 MET HB3 H 2.24 0.03 2 3 . 1 MET HB2 H 2.04 0.03 2 4 . 1 MET HG3 H 2.43 0.03 2 5 . 1 MET C C 174.55 0.50 1 6 . 1 MET CA C 55.13 0.50 1 7 . 1 MET CB C 32.94 0.50 1 8 . 1 MET CG C 31.62 0.50 1 9 . 2 PHE HA H 4.75 0.03 1 10 . 2 PHE HB3 H 3.10 0.03 2 11 . 2 PHE HD1 H 7.22 0.03 2 12 . 2 PHE HE1 H 7.32 0.03 2 13 . 2 PHE H H 8.97 0.03 1 14 . 2 PHE HZ H 7.23 0.03 1 15 . 2 PHE C C 172.81 0.50 1 16 . 2 PHE CA C 57.76 0.50 1 17 . 2 PHE CB C 43.16 0.50 1 18 . 2 PHE CD1 C 132.47 0.50 2 19 . 2 PHE CE1 C 131.72 0.50 2 20 . 2 PHE N N 129.22 0.25 1 21 . 3 GLN HA H 5.69 0.03 1 22 . 3 GLN HB3 H 2.04 0.03 2 23 . 3 GLN HB2 H 1.95 0.03 2 24 . 3 GLN H H 7.62 0.03 1 25 . 3 GLN C C 173.67 0.50 1 26 . 3 GLN CA C 54.10 0.50 1 27 . 3 GLN CB C 33.08 0.50 1 28 . 3 GLN N N 123.14 0.25 1 29 . 4 GLN HA H 4.36 0.03 1 30 . 4 GLN HB3 H 1.81 0.03 2 31 . 4 GLN HG3 H 2.35 0.03 2 32 . 4 GLN H H 8.52 0.03 1 33 . 4 GLN C C 173.45 0.50 1 34 . 4 GLN CA C 55.92 0.50 1 35 . 4 GLN CB C 34.57 0.50 1 36 . 4 GLN CG C 35.03 0.50 1 37 . 4 GLN N N 119.68 0.25 1 38 . 5 GLU HA H 5.40 0.03 1 39 . 5 GLU HB3 H 1.80 0.03 2 40 . 5 GLU HG3 H 2.10 0.03 2 41 . 5 GLU H H 8.23 0.03 1 42 . 5 GLU C C 176.02 0.50 1 43 . 5 GLU CA C 55.18 0.50 1 44 . 5 GLU CB C 32.72 0.50 1 45 . 5 GLU CG C 37.24 0.50 1 46 . 5 GLU N N 122.44 0.25 1 47 . 6 VAL HA H 4.49 0.03 1 48 . 6 VAL HB H 2.09 0.03 1 49 . 6 VAL HG1 H 1.02 0.03 2 50 . 6 VAL HG2 H 0.84 0.03 2 51 . 6 VAL H H 9.19 0.03 1 52 . 6 VAL CA C 60.67 0.50 1 53 . 6 VAL CB C 35.44 0.50 1 54 . 6 VAL CG1 C 21.84 0.50 2 55 . 6 VAL CG2 C 20.71 0.50 2 56 . 6 VAL N N 121.05 0.25 1 57 . 7 THR HA H 4.84 0.03 1 58 . 7 THR HB H 3.83 0.03 1 59 . 7 THR HG2 H 0.89 0.03 1 60 . 7 THR H H 8.09 0.03 1 61 . 7 THR C C 174.32 0.50 1 62 . 7 THR CA C 62.09 0.50 1 63 . 7 THR CB C 69.68 0.50 1 64 . 7 THR CG2 C 21.28 0.50 1 65 . 7 THR N N 122.09 0.25 1 66 . 8 ILE HA H 3.91 0.03 1 67 . 8 ILE HB H 2.05 0.03 1 68 . 8 ILE HD1 H 0.67 0.03 1 69 . 8 ILE HG13 H 1.14 0.03 2 70 . 8 ILE HG12 H 1.55 0.03 2 71 . 8 ILE HG2 H 0.80 0.03 1 72 . 8 ILE H H 8.64 0.03 1 73 . 8 ILE C C 176.33 0.50 1 74 . 8 ILE CA C 62.00 0.50 1 75 . 8 ILE CB C 37.38 0.50 1 76 . 8 ILE CD1 C 13.85 0.50 1 77 . 8 ILE CG1 C 28.00 0.50 1 78 . 8 ILE CG2 C 17.84 0.50 1 79 . 8 ILE N N 126.35 0.25 1 80 . 9 THR HA H 4.47 0.03 1 81 . 9 THR HB H 4.36 0.03 1 82 . 9 THR HG2 H 1.13 0.03 1 83 . 9 THR H H 8.63 0.03 1 84 . 9 THR C C 175.18 0.50 1 85 . 9 THR CA C 61.78 0.50 1 86 . 9 THR CB C 69.78 0.50 1 87 . 9 THR CG2 C 21.77 0.50 1 88 . 9 THR N N 120.17 0.25 1 89 . 10 ALA HA H 4.48 0.03 1 90 . 10 ALA HB H 1.27 0.03 1 91 . 10 ALA H H 7.33 0.03 1 92 . 10 ALA CA C 51.17 0.50 1 93 . 10 ALA CB C 18.78 0.50 1 94 . 10 ALA N N 129.53 0.25 1 95 . 11 PRO HA H 4.10 0.03 1 96 . 11 PRO HB3 H 1.86 0.03 2 97 . 11 PRO HB2 H 2.28 0.03 2 98 . 11 PRO C C 177.93 0.50 1 99 . 11 PRO CA C 65.46 0.50 1 100 . 11 PRO CB C 32.30 0.50 1 101 . 11 PRO CG C 27.62 0.50 1 102 . 12 ASN HA H 4.74 0.03 1 103 . 12 ASN HB3 H 2.61 0.03 2 104 . 12 ASN HB2 H 2.67 0.03 2 105 . 12 ASN H H 8.60 0.03 1 106 . 12 ASN C C 175.42 0.50 1 107 . 12 ASN CA C 52.95 0.50 1 108 . 12 ASN CB C 38.74 0.50 1 109 . 12 ASN N N 114.27 0.25 1 110 . 13 GLY H H 7.89 0.03 1 111 . 13 GLY CA C 45.59 0.50 1 112 . 13 GLY N N 106.32 0.25 1 113 . 14 LEU HA H 4.40 0.03 1 114 . 14 LEU HB3 H 0.98 0.03 2 115 . 14 LEU HB2 H 1.92 0.03 2 116 . 14 LEU HD1 H 0.61 0.03 2 117 . 14 LEU HD2 H 0.47 0.03 2 118 . 14 LEU HG H 1.21 0.03 1 119 . 14 LEU H H 7.95 0.03 1 120 . 14 LEU C C 174.77 0.50 1 121 . 14 LEU CA C 53.78 0.50 1 122 . 14 LEU CB C 41.17 0.50 1 123 . 14 LEU CD1 C 24.66 0.50 2 124 . 14 LEU CD2 C 25.48 0.50 2 125 . 14 LEU CG C 28.25 0.50 1 126 . 14 LEU N N 122.61 0.25 1 127 . 15 HIS HA H 4.61 0.03 1 128 . 15 HIS HB3 H 3.08 0.03 2 129 . 15 HIS HB2 H 3.33 0.03 2 130 . 15 HIS HD2 H 7.15 0.03 1 131 . 15 HIS H H 7.03 0.03 1 132 . 15 HIS C C 174.20 0.50 1 133 . 15 HIS CA C 55.25 0.50 1 134 . 15 HIS CB C 30.54 0.50 1 135 . 15 HIS CD2 C 119.70 0.50 1 136 . 15 HIS N N 120.90 0.25 1 137 . 16 THR HA H 3.72 0.03 1 138 . 16 THR HB H 4.13 0.03 1 139 . 16 THR HG2 H 1.21 0.03 1 140 . 16 THR H H 7.81 0.03 1 141 . 16 THR C C 174.97 0.50 1 142 . 16 THR CA C 68.19 0.50 1 143 . 16 THR CB C 68.99 0.50 1 144 . 16 THR CG2 C 22.70 0.50 1 145 . 16 THR N N 113.21 0.25 1 146 . 17 ARG HA H 4.25 0.03 1 147 . 17 ARG HB3 H 1.96 0.03 2 148 . 17 ARG HD3 H 3.24 0.03 2 149 . 17 ARG HG3 H 1.56 0.03 2 150 . 17 ARG HG2 H 1.71 0.03 2 151 . 17 ARG CA C 61.56 0.50 1 152 . 17 ARG CB C 27.41 0.50 1 153 . 17 ARG CD C 43.50 0.50 1 154 . 17 ARG CG C 27.63 0.50 1 155 . 18 PRO HA H 4.46 0.03 1 156 . 18 PRO HB3 H 2.16 0.03 2 157 . 18 PRO HB2 H 1.68 0.03 2 158 . 18 PRO CA C 65.49 0.50 1 159 . 18 PRO CB C 31.42 0.50 1 160 . 19 ALA HA H 3.81 0.03 1 161 . 19 ALA HB H 1.19 0.03 1 162 . 19 ALA H H 8.24 0.03 1 163 . 19 ALA C C 178.48 0.50 1 164 . 19 ALA CA C 55.91 0.50 1 165 . 19 ALA CB C 18.07 0.50 1 166 . 19 ALA N N 121.15 0.25 1 167 . 20 ALA HA H 4.01 0.03 1 168 . 20 ALA HB H 1.54 0.03 1 169 . 20 ALA H H 8.23 0.03 1 170 . 20 ALA C C 180.02 0.50 1 171 . 20 ALA CA C 55.59 0.50 1 172 . 20 ALA CB C 18.22 0.50 1 173 . 20 ALA N N 119.25 0.25 1 174 . 21 GLN HA H 3.96 0.03 1 175 . 21 GLN HB3 H 2.20 0.03 2 176 . 21 GLN HB2 H 2.17 0.03 2 177 . 21 GLN HG3 H 2.48 0.03 2 178 . 21 GLN HG2 H 2.38 0.03 2 179 . 21 GLN H H 7.59 0.03 1 180 . 21 GLN C C 177.48 0.50 1 181 . 21 GLN CA C 59.09 0.50 1 182 . 21 GLN CB C 28.36 0.50 1 183 . 21 GLN CG C 33.69 0.50 1 184 . 21 GLN N N 117.50 0.25 1 185 . 22 PHE HA H 3.86 0.03 1 186 . 22 PHE HB3 H 3.50 0.03 2 187 . 22 PHE HB2 H 2.97 0.03 2 188 . 22 PHE HD1 H 7.10 0.03 2 189 . 22 PHE HE1 H 7.24 0.03 2 190 . 22 PHE H H 8.42 0.03 1 191 . 22 PHE HZ H 6.88 0.03 1 192 . 22 PHE CA C 62.43 0.50 1 193 . 22 PHE CB C 39.72 0.50 1 194 . 22 PHE CD1 C 132.51 0.50 2 195 . 22 PHE CE1 C 131.53 0.50 2 196 . 22 PHE N N 121.10 0.25 1 197 . 23 VAL HA H 4.12 0.03 1 198 . 23 VAL HB H 2.09 0.03 1 199 . 23 VAL HG1 H 0.89 0.03 2 200 . 23 VAL HG2 H 1.12 0.03 2 201 . 23 VAL H H 8.31 0.03 1 202 . 23 VAL C C 178.23 0.50 1 203 . 23 VAL CA C 65.48 0.50 1 204 . 23 VAL CB C 32.26 0.50 1 205 . 23 VAL CG1 C 22.03 0.50 2 206 . 23 VAL CG2 C 23.39 0.50 2 207 . 23 VAL N N 119.08 0.25 1 208 . 24 LYS HA H 3.78 0.03 1 209 . 24 LYS HB3 H 1.92 0.03 2 210 . 24 LYS HD3 H 1.64 0.03 2 211 . 24 LYS HE3 H 2.93 0.03 2 212 . 24 LYS HG3 H 1.59 0.03 2 213 . 24 LYS HG2 H 1.36 0.03 2 214 . 24 LYS H H 8.02 0.03 1 215 . 24 LYS C C 180.06 0.50 1 216 . 24 LYS CA C 60.62 0.50 1 217 . 24 LYS CB C 32.69 0.50 1 218 . 24 LYS CD C 29.96 0.50 1 219 . 24 LYS CE C 42.17 0.50 1 220 . 24 LYS CG C 25.76 0.50 1 221 . 24 LYS N N 118.39 0.25 1 222 . 25 GLU HA H 3.93 0.03 1 223 . 25 GLU HB3 H 1.95 0.03 2 224 . 25 GLU HB2 H 2.00 0.03 2 225 . 25 GLU HG3 H 2.48 0.03 2 226 . 25 GLU HG2 H 2.31 0.03 2 227 . 25 GLU H H 8.07 0.03 1 228 . 25 GLU C C 180.12 0.50 1 229 . 25 GLU CA C 59.17 0.50 1 230 . 25 GLU CB C 29.30 0.50 1 231 . 25 GLU CG C 37.18 0.50 1 232 . 25 GLU N N 117.39 0.25 1 233 . 26 ALA HA H 3.92 0.03 1 234 . 26 ALA HB H 1.18 0.03 1 235 . 26 ALA H H 8.74 0.03 1 236 . 26 ALA C C 178.83 0.50 1 237 . 26 ALA CA C 55.87 0.50 1 238 . 26 ALA CB C 18.92 0.50 1 239 . 26 ALA N N 124.40 0.25 1 240 . 27 LYS HA H 3.88 0.03 1 241 . 27 LYS HE3 H 3.06 0.03 2 242 . 27 LYS H H 7.98 0.03 1 243 . 27 LYS C C 177.50 0.50 1 244 . 27 LYS CA C 59.16 0.50 1 245 . 27 LYS CB C 32.98 0.50 1 246 . 27 LYS N N 112.44 0.25 1 247 . 28 GLY HA3 H 3.86 0.03 2 248 . 28 GLY HA2 H 3.33 0.03 2 249 . 28 GLY H H 7.51 0.03 1 250 . 28 GLY C C 172.95 0.50 1 251 . 28 GLY CA C 45.39 0.50 1 252 . 28 GLY N N 105.51 0.25 1 253 . 29 PHE HA H 4.70 0.03 1 254 . 29 PHE HB3 H 2.72 0.03 2 255 . 29 PHE HD1 H 7.26 0.03 2 256 . 29 PHE HE1 H 6.86 0.03 2 257 . 29 PHE H H 7.33 0.03 1 258 . 29 PHE HZ H 6.59 0.03 1 259 . 29 PHE CA C 57.73 0.50 1 260 . 29 PHE CB C 40.51 0.50 1 261 . 29 PHE CD1 C 132.62 0.50 2 262 . 29 PHE CE1 C 130.95 0.50 2 263 . 29 PHE N N 119.28 0.25 1 264 . 30 THR HA H 4.15 0.03 1 265 . 30 THR HB H 4.20 0.03 1 266 . 30 THR HG2 H 1.25 0.03 1 267 . 30 THR H H 10.90 0.03 1 268 . 30 THR C C 177.34 0.50 1 269 . 30 THR CA C 64.19 0.50 1 270 . 30 THR CB C 69.56 0.50 1 271 . 30 THR CG2 C 22.19 0.50 1 272 . 30 THR N N 118.65 0.25 1 273 . 31 SER HA H 4.38 0.03 1 274 . 31 SER HB3 H 3.48 0.03 2 275 . 31 SER HB2 H 3.15 0.03 2 276 . 31 SER H H 9.04 0.03 1 277 . 31 SER C C 173.06 0.50 1 278 . 31 SER CA C 61.59 0.50 1 279 . 31 SER CB C 65.88 0.50 1 280 . 31 SER N N 119.81 0.25 1 281 . 32 GLU HA H 4.38 0.03 1 282 . 32 GLU HB3 H 2.04 0.03 2 283 . 32 GLU HG3 H 2.30 0.03 2 284 . 32 GLU H H 7.83 0.03 1 285 . 32 GLU C C 177.45 0.50 1 286 . 32 GLU CA C 56.44 0.50 1 287 . 32 GLU CB C 30.60 0.50 1 288 . 32 GLU CG C 36.29 0.50 1 289 . 32 GLU N N 121.37 0.25 1 290 . 33 ILE HA H 5.09 0.03 1 291 . 33 ILE HB H 1.36 0.03 1 292 . 33 ILE HD1 H 0.77 0.03 1 293 . 33 ILE HG2 H 0.68 0.03 1 294 . 33 ILE H H 9.12 0.03 1 295 . 33 ILE C C 175.53 0.50 1 296 . 33 ILE CA C 60.81 0.50 1 297 . 33 ILE CB C 41.97 0.50 1 298 . 33 ILE CD1 C 16.65 0.50 1 299 . 33 ILE CG2 C 18.76 0.50 1 300 . 33 ILE N N 128.13 0.25 1 301 . 34 THR HA H 4.92 0.03 1 302 . 34 THR HB H 3.84 0.03 1 303 . 34 THR HG2 H 1.06 0.03 1 304 . 34 THR H H 9.64 0.03 1 305 . 34 THR C C 172.97 0.50 1 306 . 34 THR CA C 61.68 0.50 1 307 . 34 THR CB C 71.84 0.50 1 308 . 34 THR CG2 C 22.05 0.50 1 309 . 34 THR N N 124.67 0.25 1 310 . 35 VAL HA H 4.80 0.03 1 311 . 35 VAL HB H 1.82 0.03 1 312 . 35 VAL HG1 H 0.96 0.03 2 313 . 35 VAL HG2 H 0.67 0.03 2 314 . 35 VAL H H 9.29 0.03 1 315 . 35 VAL C C 174.52 0.50 1 316 . 35 VAL CA C 61.17 0.50 1 317 . 35 VAL CB C 33.70 0.50 1 318 . 35 VAL CG1 C 22.06 0.50 2 319 . 35 VAL CG2 C 22.09 0.50 2 320 . 35 VAL N N 125.86 0.25 1 321 . 36 THR HA H 5.43 0.03 1 322 . 36 THR HB H 3.72 0.03 1 323 . 36 THR HG2 H 1.01 0.03 1 324 . 36 THR H H 8.88 0.03 1 325 . 36 THR C C 174.19 0.50 1 326 . 36 THR CA C 61.26 0.50 1 327 . 36 THR CB C 71.44 0.50 1 328 . 36 THR CG2 C 21.07 0.50 1 329 . 36 THR N N 121.96 0.25 1 330 . 37 SER HA H 4.72 0.03 1 331 . 37 SER HB3 H 3.58 0.03 2 332 . 37 SER H H 9.02 0.03 1 333 . 37 SER CA C 57.17 0.50 1 334 . 37 SER CB C 65.48 0.50 1 335 . 37 SER N N 118.99 0.25 1 336 . 38 ASN HA H 4.36 0.03 1 337 . 38 ASN HB3 H 2.78 0.03 2 338 . 38 ASN HB2 H 3.06 0.03 2 339 . 38 ASN H H 9.64 0.03 1 340 . 38 ASN C C 175.36 0.50 1 341 . 38 ASN CA C 54.59 0.50 1 342 . 38 ASN CB C 38.04 0.50 1 343 . 38 ASN N N 126.93 0.25 1 344 . 39 GLY HA3 H 3.55 0.03 2 345 . 39 GLY HA2 H 4.09 0.03 2 346 . 39 GLY H H 8.53 0.03 1 347 . 39 GLY C C 173.59 0.50 1 348 . 39 GLY CA C 45.75 0.50 1 349 . 39 GLY N N 102.96 0.25 1 350 . 40 LYS HA H 4.62 0.03 1 351 . 40 LYS HB3 H 1.80 0.03 2 352 . 40 LYS HD3 H 1.71 0.03 2 353 . 40 LYS HE3 H 2.99 0.03 2 354 . 40 LYS HG3 H 1.46 0.03 2 355 . 40 LYS HG2 H 1.38 0.03 2 356 . 40 LYS H H 7.89 0.03 1 357 . 40 LYS C C 174.48 0.50 1 358 . 40 LYS CA C 55.38 0.50 1 359 . 40 LYS CB C 35.35 0.50 1 360 . 40 LYS CD C 29.45 0.50 1 361 . 40 LYS CE C 42.36 0.50 1 362 . 40 LYS CG C 25.13 0.50 1 363 . 40 LYS N N 122.44 0.25 1 364 . 41 SER HA H 5.78 0.03 1 365 . 41 SER HB3 H 3.58 0.03 2 366 . 41 SER HB2 H 3.48 0.03 2 367 . 41 SER H H 8.30 0.03 1 368 . 41 SER C C 173.57 0.50 1 369 . 41 SER CA C 57.29 0.50 1 370 . 41 SER CB C 66.99 0.50 1 371 . 41 SER N N 115.80 0.25 1 372 . 42 ALA HA H 4.51 0.03 1 373 . 42 ALA HB H 1.15 0.03 1 374 . 42 ALA H H 9.06 0.03 1 375 . 42 ALA C C 175.70 0.50 1 376 . 42 ALA CA C 51.17 0.50 1 377 . 42 ALA CB C 23.92 0.50 1 378 . 42 ALA N N 123.44 0.25 1 379 . 43 SER HA H 4.80 0.03 1 380 . 43 SER HB3 H 4.10 0.03 2 381 . 43 SER HB2 H 3.75 0.03 2 382 . 43 SER H H 8.36 0.03 1 383 . 43 SER C C 175.87 0.50 1 384 . 43 SER CA C 57.32 0.50 1 385 . 43 SER CB C 64.46 0.50 1 386 . 43 SER N N 114.15 0.25 1 387 . 44 ALA HA H 4.14 0.03 1 388 . 44 ALA HB H 1.25 0.03 1 389 . 44 ALA H H 8.40 0.03 1 390 . 44 ALA C C 173.76 0.50 1 391 . 44 ALA CA C 53.17 0.50 1 392 . 44 ALA CB C 20.42 0.50 1 393 . 44 ALA N N 127.00 0.25 1 394 . 45 LYS HA H 4.26 0.03 1 395 . 45 LYS HB3 H 1.46 0.03 2 396 . 45 LYS H H 7.60 0.03 1 397 . 45 LYS C C 175.23 0.50 1 398 . 45 LYS CA C 56.10 0.50 1 399 . 45 LYS CB C 33.32 0.50 1 400 . 45 LYS N N 107.64 0.25 1 401 . 46 SER HA H 5.11 0.03 1 402 . 46 SER HB3 H 3.87 0.03 2 403 . 46 SER H H 7.22 0.03 1 404 . 46 SER C C 174.32 0.50 1 405 . 46 SER CA C 55.05 0.50 1 406 . 46 SER CB C 64.79 0.50 1 407 . 46 SER N N 113.29 0.25 1 408 . 47 LEU HA H 4.08 0.03 1 409 . 47 LEU HB3 H 1.55 0.03 2 410 . 47 LEU HD1 H 0.94 0.03 2 411 . 47 LEU HD2 H 0.87 0.03 2 412 . 47 LEU H H 8.83 0.03 1 413 . 47 LEU C C 177.99 0.50 1 414 . 47 LEU CA C 58.23 0.50 1 415 . 47 LEU CB C 42.90 0.50 1 416 . 47 LEU CD1 C 27.24 0.50 2 417 . 47 LEU CD2 C 23.84 0.50 2 418 . 47 LEU N N 130.73 0.25 1 419 . 48 PHE HA H 4.10 0.03 1 420 . 48 PHE HB3 H 2.90 0.03 2 421 . 48 PHE HB2 H 2.98 0.03 2 422 . 48 PHE HD1 H 7.04 0.03 2 423 . 48 PHE H H 8.17 0.03 1 424 . 48 PHE C C 177.39 0.50 1 425 . 48 PHE CA C 60.98 0.50 1 426 . 48 PHE CB C 40.18 0.50 1 427 . 48 PHE CD1 C 131.96 0.50 2 428 . 48 PHE N N 115.87 0.25 1 429 . 49 LYS HA H 4.06 0.03 1 430 . 49 LYS HB3 H 1.96 0.03 2 431 . 49 LYS HE3 H 2.99 0.03 2 432 . 49 LYS HG3 H 1.76 0.03 2 433 . 49 LYS H H 8.15 0.03 1 434 . 49 LYS C C 179.97 0.50 1 435 . 49 LYS CA C 56.93 0.50 1 436 . 49 LYS CB C 31.97 0.50 1 437 . 49 LYS CE C 42.32 0.50 1 438 . 49 LYS CG C 25.02 0.50 1 439 . 49 LYS N N 115.20 0.25 1 440 . 50 LEU HA H 3.71 0.03 1 441 . 50 LEU HB3 H 1.86 0.03 2 442 . 50 LEU HB2 H 1.56 0.03 2 443 . 50 LEU HD1 H 0.74 0.03 2 444 . 50 LEU HG H 1.67 0.03 1 445 . 50 LEU H H 8.70 0.03 1 446 . 50 LEU C C 179.06 0.50 1 447 . 50 LEU CA C 58.67 0.50 1 448 . 50 LEU CB C 42.63 0.50 1 449 . 50 LEU CD1 C 26.44 0.50 2 450 . 50 LEU CD2 C 25.15 0.50 2 451 . 50 LEU CG C 26.90 0.50 1 452 . 50 LEU N N 122.57 0.25 1 453 . 51 GLN HA H 4.10 0.03 1 454 . 51 GLN HB3 H 2.08 0.03 2 455 . 51 GLN HG3 H 2.35 0.03 2 456 . 51 GLN H H 7.63 0.03 1 457 . 51 GLN C C 176.70 0.50 1 458 . 51 GLN CA C 58.24 0.50 1 459 . 51 GLN CB C 28.98 0.50 1 460 . 51 GLN CG C 34.51 0.50 1 461 . 51 GLN N N 112.12 0.25 1 462 . 52 THR HA H 4.05 0.03 1 463 . 52 THR HB H 4.24 0.03 1 464 . 52 THR HG2 H 1.15 0.03 1 465 . 52 THR H H 7.25 0.03 1 466 . 52 THR C C 174.69 0.50 1 467 . 52 THR CA C 63.08 0.50 1 468 . 52 THR CB C 69.69 0.50 1 469 . 52 THR CG2 C 22.11 0.50 1 470 . 52 THR N N 106.52 0.25 1 471 . 53 LEU HA H 4.19 0.03 1 472 . 53 LEU HB3 H 1.31 0.03 2 473 . 53 LEU HD1 H 0.74 0.03 2 474 . 53 LEU HD2 H 0.64 0.03 2 475 . 53 LEU HG H 1.68 0.03 1 476 . 53 LEU H H 7.33 0.03 1 477 . 53 LEU C C 177.63 0.50 1 478 . 53 LEU CA C 55.37 0.50 1 479 . 53 LEU CB C 42.55 0.50 1 480 . 53 LEU CD1 C 26.34 0.50 2 481 . 53 LEU CD2 C 23.62 0.50 2 482 . 53 LEU CG C 27.70 0.50 1 483 . 53 LEU N N 119.62 0.25 1 484 . 54 GLY HA3 H 3.65 0.03 2 485 . 54 GLY HA2 H 3.80 0.03 2 486 . 54 GLY H H 8.12 0.03 1 487 . 54 GLY CA C 47.26 0.50 1 488 . 54 GLY N N 107.45 0.25 1 489 . 55 LEU HA H 4.19 0.03 1 490 . 55 LEU HB3 H 1.20 0.03 2 491 . 55 LEU HD1 H 0.72 0.03 2 492 . 55 LEU HD2 H 0.61 0.03 2 493 . 55 LEU HG H 1.44 0.03 1 494 . 55 LEU H H 8.12 0.03 1 495 . 55 LEU C C 175.65 0.50 1 496 . 55 LEU CA C 54.03 0.50 1 497 . 55 LEU CB C 40.87 0.50 1 498 . 55 LEU CD1 C 26.19 0.50 2 499 . 55 LEU CD2 C 23.88 0.50 2 500 . 55 LEU CG C 26.25 0.50 1 501 . 55 LEU N N 124.24 0.25 1 502 . 56 THR HA H 4.14 0.03 1 503 . 56 THR HB H 4.26 0.03 1 504 . 56 THR HG2 H 1.01 0.03 1 505 . 56 THR H H 7.25 0.03 1 506 . 56 THR C C 175.54 0.50 1 507 . 56 THR CA C 60.63 0.50 1 508 . 56 THR CB C 71.01 0.50 1 509 . 56 THR CG2 C 22.31 0.50 1 510 . 56 THR N N 110.89 0.25 1 511 . 57 GLN HA H 3.58 0.03 1 512 . 57 GLN HB3 H 1.93 0.03 2 513 . 57 GLN HB2 H 2.12 0.03 2 514 . 57 GLN HG3 H 2.06 0.03 2 515 . 57 GLN H H 8.73 0.03 1 516 . 57 GLN C C 176.72 0.50 1 517 . 57 GLN CA C 58.88 0.50 1 518 . 57 GLN CB C 28.36 0.50 1 519 . 57 GLN CG C 34.24 0.50 1 520 . 57 GLN N N 121.95 0.25 1 521 . 58 GLY HA3 H 3.42 0.03 2 522 . 58 GLY HA2 H 4.25 0.03 2 523 . 58 GLY H H 9.17 0.03 1 524 . 58 GLY C C 174.33 0.50 1 525 . 58 GLY CA C 44.98 0.50 1 526 . 58 GLY N N 115.43 0.25 1 527 . 59 THR HA H 4.02 0.03 1 528 . 59 THR HB H 4.02 0.03 1 529 . 59 THR HG2 H 1.20 0.03 1 530 . 59 THR H H 7.81 0.03 1 531 . 59 THR C C 172.89 0.50 1 532 . 59 THR CA C 64.54 0.50 1 533 . 59 THR CB C 69.79 0.50 1 534 . 59 THR CG2 C 22.53 0.50 1 535 . 59 THR N N 117.92 0.25 1 536 . 60 VAL HA H 4.43 0.03 1 537 . 60 VAL HB H 1.90 0.03 1 538 . 60 VAL HG1 H 0.96 0.03 2 539 . 60 VAL HG2 H 0.75 0.03 2 540 . 60 VAL H H 8.48 0.03 1 541 . 60 VAL C C 176.10 0.50 1 542 . 60 VAL CA C 62.62 0.50 1 543 . 60 VAL CB C 32.30 0.50 1 544 . 60 VAL CG1 C 21.37 0.50 2 545 . 60 VAL CG2 C 21.45 0.50 2 546 . 60 VAL N N 127.43 0.25 1 547 . 61 VAL HA H 4.90 0.03 1 548 . 61 VAL HB H 1.98 0.03 1 549 . 61 VAL HG1 H 0.74 0.03 1 550 . 61 VAL HG2 H 0.74 0.03 1 551 . 61 VAL H H 9.23 0.03 1 552 . 61 VAL C C 174.87 0.50 1 553 . 61 VAL CA C 59.49 0.50 1 554 . 61 VAL CB C 34.59 0.50 1 555 . 61 VAL CG1 C 23.11 0.50 2 556 . 61 VAL CG2 C 21.32 0.50 2 557 . 61 VAL N N 125.89 0.25 1 558 . 62 THR HA H 4.82 0.03 1 559 . 62 THR HB H 3.80 0.03 1 560 . 62 THR HG2 H 0.96 0.03 1 561 . 62 THR H H 8.80 0.03 1 562 . 62 THR C C 171.82 0.50 1 563 . 62 THR CA C 62.51 0.50 1 564 . 62 THR CB C 70.39 0.50 1 565 . 62 THR CG2 C 21.79 0.50 1 566 . 62 THR N N 118.34 0.25 1 567 . 63 ILE HA H 4.82 0.03 1 568 . 63 ILE HB H 1.82 0.03 1 569 . 63 ILE HG13 H 1.67 0.03 2 570 . 63 ILE HG2 H 0.87 0.03 1 571 . 63 ILE H H 8.96 0.03 1 572 . 63 ILE C C 173.88 0.50 1 573 . 63 ILE CA C 60.94 0.50 1 574 . 63 ILE CB C 38.66 0.50 1 575 . 63 ILE CG1 C 31.14 0.50 1 576 . 63 ILE CG2 C 18.29 0.50 1 577 . 63 ILE N N 129.02 0.25 1 578 . 64 SER HA H 5.55 0.03 1 579 . 64 SER HB3 H 3.65 0.03 2 580 . 64 SER H H 9.00 0.03 1 581 . 64 SER C C 172.49 0.50 1 582 . 64 SER CA C 56.08 0.50 1 583 . 64 SER CB C 66.24 0.50 1 584 . 64 SER N N 121.06 0.25 1 585 . 65 ALA HA H 5.64 0.03 1 586 . 65 ALA HB H 1.30 0.03 1 587 . 65 ALA H H 9.11 0.03 1 588 . 65 ALA CA C 50.53 0.50 1 589 . 65 ALA CB C 25.53 0.50 1 590 . 65 ALA N N 123.99 0.25 1 591 . 66 GLU HA H 5.32 0.03 1 592 . 66 GLU HB3 H 1.91 0.03 2 593 . 66 GLU HB2 H 1.96 0.03 2 594 . 66 GLU HG3 H 2.18 0.03 2 595 . 66 GLU HG2 H 2.08 0.03 2 596 . 66 GLU H H 8.33 0.03 1 597 . 66 GLU C C 175.50 0.50 1 598 . 66 GLU CA C 54.59 0.50 1 599 . 66 GLU CB C 33.69 0.50 1 600 . 66 GLU CG C 37.03 0.50 1 601 . 66 GLU N N 119.02 0.25 1 602 . 67 GLY HA3 H 3.92 0.03 2 603 . 67 GLY HA2 H 3.75 0.03 2 604 . 67 GLY H H 10.06 0.03 1 605 . 67 GLY C C 175.33 0.50 1 606 . 67 GLY CA C 45.61 0.50 1 607 . 67 GLY N N 118.36 0.25 1 608 . 68 GLU HA H 3.99 0.03 1 609 . 68 GLU HB3 H 1.96 0.03 2 610 . 68 GLU HG3 H 2.26 0.03 2 611 . 68 GLU H H 8.93 0.03 1 612 . 68 GLU C C 177.18 0.50 1 613 . 68 GLU CA C 59.64 0.50 1 614 . 68 GLU CB C 30.19 0.50 1 615 . 68 GLU CG C 36.33 0.50 1 616 . 68 GLU N N 118.51 0.25 1 617 . 69 ASP HA H 4.87 0.03 1 618 . 69 ASP HB3 H 2.62 0.03 2 619 . 69 ASP HB2 H 3.27 0.03 2 620 . 69 ASP H H 7.22 0.03 1 621 . 69 ASP C C 176.44 0.50 1 622 . 69 ASP CA C 51.32 0.50 1 623 . 69 ASP CB C 40.06 0.50 1 624 . 69 ASP N N 113.88 0.25 1 625 . 70 GLU HA H 3.75 0.03 1 626 . 70 GLU H H 6.86 0.03 1 627 . 70 GLU C C 176.43 0.50 1 628 . 70 GLU CA C 59.79 0.50 1 629 . 70 GLU CB C 28.04 0.50 1 630 . 70 GLU N N 116.29 0.25 1 631 . 71 GLN HA H 3.23 0.03 1 632 . 71 GLN HB3 H 1.39 0.03 2 633 . 71 GLN HB2 H 1.48 0.03 2 634 . 71 GLN HG3 H 1.08 0.03 2 635 . 71 GLN H H 7.68 0.03 1 636 . 71 GLN C C 177.17 0.50 1 637 . 71 GLN CA C 59.12 0.50 1 638 . 71 GLN CB C 27.26 0.50 1 639 . 71 GLN CG C 32.71 0.50 1 640 . 71 GLN N N 119.26 0.25 1 641 . 72 LYS HA H 3.84 0.03 1 642 . 72 LYS HB3 H 1.75 0.03 2 643 . 72 LYS HD3 H 1.73 0.03 2 644 . 72 LYS HE3 H 2.99 0.03 2 645 . 72 LYS HG3 H 1.43 0.03 2 646 . 72 LYS HG2 H 1.49 0.03 2 647 . 72 LYS H H 7.38 0.03 1 648 . 72 LYS C C 178.63 0.50 1 649 . 72 LYS CA C 58.83 0.50 1 650 . 72 LYS CB C 32.55 0.50 1 651 . 72 LYS CD C 29.48 0.50 1 652 . 72 LYS CE C 42.26 0.50 1 653 . 72 LYS CG C 25.33 0.50 1 654 . 72 LYS N N 118.62 0.25 1 655 . 73 ALA HA H 1.92 0.03 1 656 . 73 ALA HB H 0.58 0.03 1 657 . 73 ALA H H 8.25 0.03 1 658 . 73 ALA C C 178.72 0.50 1 659 . 73 ALA CA C 54.21 0.50 1 660 . 73 ALA CB C 18.64 0.50 1 661 . 73 ALA N N 120.54 0.25 1 662 . 74 VAL HA H 3.22 0.03 1 663 . 74 VAL HB H 2.13 0.03 1 664 . 74 VAL HG1 H 0.90 0.03 2 665 . 74 VAL HG2 H 1.10 0.03 2 666 . 74 VAL H H 7.21 0.03 1 667 . 74 VAL C C 177.65 0.50 1 668 . 74 VAL CA C 67.64 0.50 1 669 . 74 VAL CB C 32.18 0.50 1 670 . 74 VAL CG1 C 23.19 0.50 2 671 . 74 VAL CG2 C 24.78 0.50 2 672 . 74 VAL N N 115.39 0.25 1 673 . 75 GLU HA H 3.80 0.03 1 674 . 75 GLU HB3 H 2.04 0.03 2 675 . 75 GLU HB2 H 1.92 0.03 2 676 . 75 GLU HG3 H 2.50 0.03 2 677 . 75 GLU HG2 H 2.20 0.03 2 678 . 75 GLU H H 8.18 0.03 1 679 . 75 GLU C C 179.74 0.50 1 680 . 75 GLU CA C 60.46 0.50 1 681 . 75 GLU CB C 29.73 0.50 1 682 . 75 GLU CG C 37.53 0.50 1 683 . 75 GLU N N 116.34 0.25 1 684 . 76 HIS HA H 4.19 0.03 1 685 . 76 HIS HB3 H 3.07 0.03 2 686 . 76 HIS HB2 H 3.22 0.03 2 687 . 76 HIS HD2 H 6.67 0.03 1 688 . 76 HIS HE1 H 6.89 0.03 1 689 . 76 HIS H H 8.19 0.03 1 690 . 76 HIS C C 177.64 0.50 1 691 . 76 HIS CA C 60.26 0.50 1 692 . 76 HIS CB C 32.32 0.50 1 693 . 76 HIS CD2 C 116.88 0.50 1 694 . 76 HIS N N 117.61 0.25 1 695 . 77 LEU HA H 4.01 0.03 1 696 . 77 LEU HD1 H 0.24 0.03 2 697 . 77 LEU HD2 H 0.57 0.03 2 698 . 77 LEU HG H 1.89 0.03 1 699 . 77 LEU H H 7.95 0.03 1 700 . 77 LEU C C 179.19 0.50 1 701 . 77 LEU CA C 57.84 0.50 1 702 . 77 LEU CB C 40.97 0.50 1 703 . 77 LEU CD1 C 21.11 0.50 2 704 . 77 LEU CD2 C 26.79 0.50 2 705 . 77 LEU CG C 27.13 0.50 1 706 . 77 LEU N N 118.64 0.25 1 707 . 78 VAL HA H 3.55 0.03 1 708 . 78 VAL HB H 2.10 0.03 1 709 . 78 VAL HG1 H 0.95 0.03 2 710 . 78 VAL HG2 H 0.89 0.03 2 711 . 78 VAL H H 8.90 0.03 1 712 . 78 VAL C C 178.20 0.50 1 713 . 78 VAL CA C 67.16 0.50 1 714 . 78 VAL CB C 31.80 0.50 1 715 . 78 VAL CG1 C 23.90 0.50 2 716 . 78 VAL CG2 C 21.41 0.50 2 717 . 78 VAL N N 119.33 0.25 1 718 . 79 LYS HA H 3.97 0.03 1 719 . 79 LYS HB3 H 1.81 0.03 2 720 . 79 LYS HB2 H 1.90 0.03 2 721 . 79 LYS HD3 H 1.63 0.03 2 722 . 79 LYS HE3 H 2.94 0.03 2 723 . 79 LYS HG3 H 1.47 0.03 2 724 . 79 LYS HG2 H 1.30 0.03 2 725 . 79 LYS H H 7.19 0.03 1 726 . 79 LYS C C 178.73 0.50 1 727 . 79 LYS CA C 59.76 0.50 1 728 . 79 LYS CB C 32.31 0.50 1 729 . 79 LYS CD C 29.63 0.50 1 730 . 79 LYS CE C 42.30 0.50 1 731 . 79 LYS CG C 25.18 0.50 1 732 . 79 LYS N N 120.06 0.25 1 733 . 80 LEU HA H 4.01 0.03 1 734 . 80 LEU HB3 H 1.68 0.03 2 735 . 80 LEU HB2 H 1.80 0.03 2 736 . 80 LEU HD1 H 0.85 0.03 2 737 . 80 LEU HG H 1.64 0.03 1 738 . 80 LEU H H 7.62 0.03 1 739 . 80 LEU C C 179.75 0.50 1 740 . 80 LEU CA C 57.99 0.50 1 741 . 80 LEU CB C 42.51 0.50 1 742 . 80 LEU CD1 C 25.38 0.50 2 743 . 80 LEU CG C 27.39 0.50 1 744 . 80 LEU N N 117.83 0.25 1 745 . 81 MET HA H 4.00 0.03 1 746 . 81 MET HB3 H 2.02 0.03 2 747 . 81 MET HB2 H 2.26 0.03 2 748 . 81 MET HG3 H 2.53 0.03 2 749 . 81 MET HG2 H 2.46 0.03 2 750 . 81 MET H H 8.01 0.03 1 751 . 81 MET C C 177.39 0.50 1 752 . 81 MET CA C 58.77 0.50 1 753 . 81 MET CB C 33.46 0.50 1 754 . 81 MET CG C 34.26 0.50 1 755 . 81 MET N N 115.97 0.25 1 756 . 82 ALA HA H 4.26 0.03 1 757 . 82 ALA HB H 1.51 0.03 1 758 . 82 ALA H H 7.88 0.03 1 759 . 82 ALA C C 179.30 0.50 1 760 . 82 ALA CA C 54.04 0.50 1 761 . 82 ALA CB C 19.18 0.50 1 762 . 82 ALA N N 118.71 0.25 1 763 . 83 GLU HA H 4.37 0.03 1 764 . 83 GLU HB3 H 1.99 0.03 2 765 . 83 GLU HB2 H 2.12 0.03 2 766 . 83 GLU HG3 H 2.39 0.03 2 767 . 83 GLU H H 7.71 0.03 1 768 . 83 GLU C C 176.66 0.50 1 769 . 83 GLU CA C 56.22 0.50 1 770 . 83 GLU CB C 30.63 0.50 1 771 . 83 GLU CG C 36.49 0.50 1 772 . 83 GLU N N 115.95 0.25 1 773 . 84 LEU HA H 4.21 0.03 1 774 . 84 LEU HB3 H 1.42 0.03 2 775 . 84 LEU HB2 H 1.76 0.03 2 776 . 84 LEU HD1 H 0.85 0.03 2 777 . 84 LEU HD2 H 0.90 0.03 2 778 . 84 LEU HG H 2.01 0.03 1 779 . 84 LEU H H 7.20 0.03 1 780 . 84 LEU C C 175.94 0.50 1 781 . 84 LEU CA C 56.19 0.50 1 782 . 84 LEU CB C 43.27 0.50 1 783 . 84 LEU CD1 C 23.77 0.50 2 784 . 84 LEU CD2 C 26.46 0.50 2 785 . 84 LEU CG C 26.47 0.50 1 786 . 84 LEU N N 121.36 0.25 1 787 . 85 GLU HA H 4.21 0.03 1 788 . 85 GLU HB3 H 2.06 0.03 2 789 . 85 GLU HB2 H 1.92 0.03 2 790 . 85 GLU HG3 H 2.20 0.03 2 791 . 85 GLU H H 7.75 0.03 1 792 . 85 GLU CA C 57.98 0.50 1 793 . 85 GLU CB C 32.82 0.50 1 794 . 85 GLU CG C 36.84 0.50 1 795 . 85 GLU N N 125.33 0.25 1 stop_ save_ save_chemical_shift_assignment_3 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Sample_label $sample_two stop_ _Sample_conditions_label $sample_cond_1 _Chem_shift_reference_set_label $chemical_shift_reference_one _Mol_system_component_name 'Enzyme I, N-terminal' _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 ILE CA C 61.08 0.50 1 2 . 2 ILE CB C 39.04 0.50 1 3 . 2 ILE CG1 C 26.16 0.50 1 4 . 2 ILE CG2 C 16.35 0.50 1 5 . 3 SER H H 8.14 0.03 1 6 . 3 SER CA C 56.70 0.50 1 7 . 3 SER CB C 65.77 0.50 1 8 . 3 SER N N 119.31 0.25 1 9 . 4 GLY H H 8.61 0.03 1 10 . 4 GLY CA C 46.39 0.50 1 11 . 4 GLY N N 107.94 0.25 1 12 . 5 ILE H H 9.51 0.03 1 13 . 5 ILE CA C 59.46 0.50 1 14 . 5 ILE CB C 38.25 0.50 1 15 . 5 ILE CG1 C 26.18 0.50 1 16 . 5 ILE CG2 C 15.90 0.50 1 17 . 5 ILE N N 130.57 0.25 1 18 . 6 LEU H H 8.70 0.03 1 19 . 6 LEU CA C 55.19 0.50 1 20 . 6 LEU CB C 39.74 0.50 1 21 . 6 LEU CD2 C 24.90 0.50 2 22 . 6 LEU CG C 26.04 0.50 1 23 . 6 LEU N N 127.38 0.25 1 24 . 7 ALA H H 7.94 0.03 1 25 . 7 ALA CA C 52.92 0.50 1 26 . 7 ALA CB C 20.63 0.50 1 27 . 7 ALA N N 129.97 0.25 1 28 . 8 SER H H 7.57 0.03 1 29 . 8 SER CA C 53.89 0.50 1 30 . 8 SER CB C 64.22 0.50 1 31 . 8 SER N N 110.72 0.25 1 32 . 9 PRO CA C 62.68 0.50 1 33 . 9 PRO CB C 32.73 0.50 1 34 . 9 PRO CG C 26.30 0.50 1 35 . 10 GLY H H 6.30 0.03 1 36 . 10 GLY CA C 43.57 0.50 1 37 . 10 GLY N N 103.71 0.25 1 38 . 11 ILE H H 8.51 0.03 1 39 . 11 ILE CA C 59.34 0.50 1 40 . 11 ILE CB C 40.38 0.50 1 41 . 11 ILE CD1 C 13.37 0.50 1 42 . 11 ILE CG1 C 27.62 0.50 1 43 . 11 ILE CG2 C 16.61 0.50 1 44 . 11 ILE N N 117.55 0.25 1 45 . 12 ALA H H 8.48 0.03 1 46 . 12 ALA CA C 50.02 0.50 1 47 . 12 ALA CB C 23.05 0.50 1 48 . 12 ALA N N 126.85 0.25 1 49 . 13 PHE H H 8.53 0.03 1 50 . 13 PHE CA C 55.10 0.50 1 51 . 13 PHE CB C 40.50 0.50 1 52 . 13 PHE N N 120.33 0.25 1 53 . 14 GLY H H 8.17 0.03 1 54 . 14 GLY CA C 45.28 0.50 1 55 . 14 GLY N N 107.24 0.25 1 56 . 15 LYS H H 8.40 0.03 1 57 . 15 LYS CA C 55.23 0.50 1 58 . 15 LYS CB C 33.69 0.50 1 59 . 15 LYS CD C 29.02 0.50 1 60 . 15 LYS CG C 24.41 0.50 1 61 . 15 LYS N N 118.38 0.25 1 62 . 16 ALA H H 8.89 0.03 1 63 . 16 ALA CA C 51.27 0.50 1 64 . 16 ALA CB C 19.93 0.50 1 65 . 16 ALA N N 121.56 0.25 1 66 . 17 LEU H H 8.57 0.03 1 67 . 17 LEU CA C 54.32 0.50 1 68 . 17 LEU CB C 42.85 0.50 1 69 . 17 LEU CD1 C 25.16 0.50 2 70 . 17 LEU CG C 27.07 0.50 1 71 . 17 LEU N N 126.53 0.25 1 72 . 18 LEU H H 8.80 0.03 1 73 . 18 LEU CA C 53.26 0.50 1 74 . 18 LEU CB C 42.59 0.50 1 75 . 18 LEU CD1 C 24.89 0.50 2 76 . 18 LEU CD2 C 22.77 0.50 2 77 . 18 LEU CG C 27.17 0.50 1 78 . 18 LEU N N 127.61 0.25 1 79 . 19 LEU H H 8.95 0.03 1 80 . 19 LEU CA C 53.40 0.50 1 81 . 19 LEU CB C 40.54 0.50 1 82 . 19 LEU CD1 C 24.84 0.50 2 83 . 19 LEU CD2 C 23.84 0.50 2 84 . 19 LEU CG C 26.24 0.50 1 85 . 19 LEU N N 128.73 0.25 1 86 . 20 LYS H H 7.92 0.03 1 87 . 20 LYS CA C 55.22 0.50 1 88 . 20 LYS CB C 33.52 0.50 1 89 . 20 LYS CD C 28.27 0.50 1 90 . 20 LYS CE C 41.66 0.50 1 91 . 20 LYS CG C 23.78 0.50 1 92 . 20 LYS N N 124.83 0.25 1 93 . 21 GLU H H 8.66 0.03 1 94 . 21 GLU CA C 55.18 0.50 1 95 . 21 GLU CB C 31.24 0.50 1 96 . 21 GLU CG C 35.91 0.50 1 97 . 21 GLU N N 124.59 0.25 1 98 . 22 ASP H H 8.66 0.03 1 99 . 22 ASP CA C 53.93 0.50 1 100 . 22 ASP CB C 40.97 0.50 1 101 . 22 ASP N N 122.35 0.25 1 102 . 23 GLU H H 8.49 0.03 1 103 . 23 GLU CA C 56.33 0.50 1 104 . 23 GLU CB C 29.75 0.50 1 105 . 23 GLU CG C 35.52 0.50 1 106 . 23 GLU N N 121.97 0.25 1 107 . 24 ILE H H 8.32 0.03 1 108 . 24 ILE CA C 61.74 0.50 1 109 . 24 ILE CB C 37.89 0.50 1 110 . 24 ILE CG1 C 26.97 0.50 1 111 . 24 ILE CG2 C 17.02 0.50 1 112 . 24 ILE N N 123.59 0.25 1 113 . 25 VAL H H 8.07 0.03 1 114 . 25 VAL CA C 61.66 0.50 1 115 . 25 VAL CB C 31.79 0.50 1 116 . 25 VAL CG1 C 20.06 0.50 2 117 . 25 VAL N N 130.34 0.25 1 118 . 26 ILE H H 7.88 0.03 1 119 . 26 ILE CA C 58.13 0.50 1 120 . 26 ILE CB C 37.05 0.50 1 121 . 26 ILE CG1 C 25.76 0.50 1 122 . 26 ILE CG2 C 16.72 0.50 1 123 . 26 ILE N N 126.02 0.25 1 124 . 27 ASP H H 9.41 0.03 1 125 . 27 ASP CA C 53.52 0.50 1 126 . 27 ASP CB C 41.06 0.50 1 127 . 27 ASP N N 127.97 0.25 1 128 . 28 ARG H H 8.21 0.03 1 129 . 28 ARG CA C 55.14 0.50 1 130 . 28 ARG CB C 28.58 0.50 1 131 . 28 ARG CD C 42.65 0.50 1 132 . 28 ARG CG C 27.01 0.50 1 133 . 28 ARG N N 123.66 0.25 1 134 . 29 LYS H H 8.08 0.03 1 135 . 29 LYS CA C 56.73 0.50 1 136 . 29 LYS CB C 31.46 0.50 1 137 . 29 LYS CD C 28.27 0.50 1 138 . 29 LYS CE C 41.18 0.50 1 139 . 29 LYS CG C 23.29 0.50 1 140 . 29 LYS N N 121.99 0.25 1 141 . 30 LYS H H 8.24 0.03 1 142 . 30 LYS CA C 54.85 0.50 1 143 . 30 LYS CB C 32.04 0.50 1 144 . 30 LYS CD C 27.81 0.50 1 145 . 30 LYS CE C 41.99 0.50 1 146 . 30 LYS CG C 23.95 0.50 1 147 . 30 LYS N N 122.34 0.25 1 148 . 31 ILE H H 8.28 0.03 1 149 . 31 ILE CA C 60.23 0.50 1 150 . 31 ILE CB C 38.10 0.50 1 151 . 31 ILE CG1 C 23.85 0.50 1 152 . 31 ILE CG2 C 18.16 0.50 1 153 . 31 ILE N N 117.95 0.25 1 154 . 32 SER H H 8.10 0.03 1 155 . 32 SER CA C 56.63 0.50 1 156 . 32 SER CB C 64.39 0.50 1 157 . 32 SER N N 113.71 0.25 1 158 . 33 ALA H H 8.70 0.03 1 159 . 33 ALA CA C 54.94 0.50 1 160 . 33 ALA CB C 17.82 0.50 1 161 . 33 ALA N N 123.23 0.25 1 162 . 34 ASP H H 8.23 0.03 1 163 . 34 ASP CA C 54.86 0.50 1 164 . 34 ASP CB C 39.60 0.50 1 165 . 34 ASP N N 113.18 0.25 1 166 . 35 GLN HE21 H 6.71 0.03 2 167 . 35 GLN HE22 H 7.68 0.03 2 168 . 35 GLN H H 7.74 0.03 1 169 . 35 GLN CA C 55.35 0.50 1 170 . 35 GLN CB C 30.08 0.50 1 171 . 35 GLN CG C 34.25 0.50 1 172 . 35 GLN N N 117.83 0.25 1 173 . 35 GLN NE2 N 111.59 0.25 1 174 . 36 VAL H H 7.11 0.03 1 175 . 36 VAL CA C 66.55 0.50 1 176 . 36 VAL CB C 31.66 0.50 1 177 . 36 VAL CG2 C 21.14 0.50 2 178 . 36 VAL N N 120.28 0.25 1 179 . 37 ASP H H 8.50 0.03 1 180 . 37 ASP CA C 57.84 0.50 1 181 . 37 ASP CB C 39.13 0.50 1 182 . 37 ASP N N 118.04 0.25 1 183 . 38 GLN HE21 H 6.82 0.03 2 184 . 38 GLN HE22 H 7.66 0.03 2 185 . 38 GLN H H 8.08 0.03 1 186 . 38 GLN CA C 58.32 0.50 1 187 . 38 GLN CB C 27.99 0.50 1 188 . 38 GLN CG C 33.97 0.50 1 189 . 38 GLN N N 119.44 0.25 1 190 . 38 GLN NE2 N 111.21 0.25 1 191 . 39 GLU H H 8.13 0.03 1 192 . 39 GLU CA C 58.68 0.50 1 193 . 39 GLU CB C 29.19 0.50 1 194 . 39 GLU CG C 36.59 0.50 1 195 . 39 GLU N N 121.36 0.25 1 196 . 40 VAL H H 8.72 0.03 1 197 . 40 VAL CA C 67.87 0.50 1 198 . 40 VAL CB C 30.96 0.50 1 199 . 40 VAL N N 121.48 0.25 1 200 . 41 GLU H H 7.88 0.03 1 201 . 41 GLU CA C 59.32 0.50 1 202 . 41 GLU CB C 28.35 0.50 1 203 . 41 GLU CG C 35.55 0.50 1 204 . 41 GLU N N 118.20 0.25 1 205 . 42 ARG H H 8.18 0.03 1 206 . 42 ARG CA C 59.62 0.50 1 207 . 42 ARG CB C 30.20 0.50 1 208 . 42 ARG CD C 43.46 0.50 1 209 . 42 ARG N N 121.18 0.25 1 210 . 43 PHE H H 8.02 0.03 1 211 . 43 PHE CA C 59.65 0.50 1 212 . 43 PHE CB C 37.50 0.50 1 213 . 43 PHE N N 119.05 0.25 1 214 . 44 LEU H H 8.52 0.03 1 215 . 44 LEU CA C 57.83 0.50 1 216 . 44 LEU CB C 40.30 0.50 1 217 . 44 LEU CG C 25.07 0.50 2 218 . 44 LEU N N 120.24 0.25 1 219 . 45 SER H H 9.00 0.03 1 220 . 45 SER CA C 60.97 0.50 1 221 . 45 SER CB C 62.39 0.50 1 222 . 45 SER N N 115.93 0.25 1 223 . 46 GLY H H 7.92 0.03 1 224 . 46 GLY CA C 46.73 0.50 1 225 . 46 GLY N N 109.97 0.25 1 226 . 47 ARG H H 8.72 0.03 1 227 . 47 ARG CA C 59.71 0.50 1 228 . 47 ARG CB C 28.90 0.50 1 229 . 47 ARG CD C 42.64 0.50 1 230 . 47 ARG CG C 25.07 0.50 1 231 . 47 ARG N N 122.41 0.25 1 232 . 48 ALA H H 7.86 0.03 1 233 . 48 ALA CA C 54.76 0.50 1 234 . 48 ALA CB C 17.27 0.50 1 235 . 48 ALA N N 120.88 0.25 1 236 . 49 LYS H H 7.64 0.03 1 237 . 49 LYS CA C 59.32 0.50 1 238 . 49 LYS CB C 32.11 0.50 1 239 . 49 LYS CG C 24.99 0.50 1 240 . 49 LYS N N 118.86 0.25 1 241 . 50 ALA H H 8.00 0.03 1 242 . 50 ALA CA C 54.48 0.50 1 243 . 50 ALA CB C 17.84 0.50 1 244 . 50 ALA N N 120.98 0.25 1 245 . 51 SER H H 8.15 0.03 1 246 . 51 SER CA C 60.70 0.50 1 247 . 51 SER CB C 62.64 0.50 1 248 . 51 SER N N 114.64 0.25 1 249 . 52 ALA H H 7.73 0.03 1 250 . 52 ALA CA C 54.86 0.50 1 251 . 52 ALA CB C 17.36 0.50 1 252 . 52 ALA N N 122.08 0.25 1 253 . 53 GLN H H 7.88 0.03 1 254 . 53 GLN CA C 58.20 0.50 1 255 . 53 GLN CB C 27.25 0.50 1 256 . 53 GLN CG C 32.87 0.50 1 257 . 53 GLN N N 117.17 0.25 1 258 . 54 LEU H H 8.18 0.03 1 259 . 54 LEU CA C 57.76 0.50 1 260 . 54 LEU CB C 42.06 0.50 1 261 . 54 LEU CG C 25.52 0.50 2 262 . 54 LEU N N 119.37 0.25 1 263 . 55 GLU H H 8.51 0.03 1 264 . 55 GLU CA C 59.57 0.50 1 265 . 55 GLU CB C 28.30 0.50 1 266 . 55 GLU CG C 34.98 0.50 1 267 . 55 GLU N N 121.06 0.25 1 268 . 56 THR H H 7.57 0.03 1 269 . 56 THR CA C 66.13 0.50 1 270 . 56 THR CB C 68.33 0.50 1 271 . 56 THR CG2 C 21.35 0.50 1 272 . 56 THR N N 115.90 0.25 1 273 . 57 ILE H H 7.86 0.03 1 274 . 57 ILE CA C 65.36 0.50 1 275 . 57 ILE CB C 37.55 0.50 1 276 . 57 ILE N N 123.22 0.25 1 277 . 58 LYS H H 8.67 0.03 1 278 . 58 LYS CA C 59.85 0.50 1 279 . 58 LYS CB C 31.82 0.50 1 280 . 58 LYS CG C 23.85 0.50 1 281 . 58 LYS N N 120.25 0.25 1 282 . 59 THR H H 7.70 0.03 1 283 . 59 THR CA C 65.66 0.50 1 284 . 59 THR CB C 68.43 0.50 1 285 . 59 THR CG2 C 21.13 0.50 1 286 . 59 THR N N 113.94 0.25 1 287 . 60 LYS H H 7.89 0.03 1 288 . 60 LYS CA C 58.30 0.50 1 289 . 60 LYS CB C 30.91 0.50 1 290 . 60 LYS CD C 27.32 0.50 1 291 . 60 LYS CE C 41.68 0.50 1 292 . 60 LYS CG C 23.84 0.50 1 293 . 60 LYS N N 122.56 0.25 1 294 . 61 ALA H H 8.96 0.03 1 295 . 61 ALA CA C 54.68 0.50 1 296 . 61 ALA CB C 17.88 0.50 1 297 . 61 ALA N N 122.12 0.25 1 298 . 62 GLY H H 8.29 0.03 1 299 . 62 GLY CA C 46.67 0.50 1 300 . 62 GLY N N 105.12 0.25 1 301 . 63 GLU H H 7.74 0.03 1 302 . 63 GLU CA C 58.37 0.50 1 303 . 63 GLU CB C 29.59 0.50 1 304 . 63 GLU CG C 35.73 0.50 1 305 . 63 GLU N N 120.50 0.25 1 306 . 64 THR H H 8.04 0.03 1 307 . 64 THR CA C 64.55 0.50 1 308 . 64 THR CB C 69.12 0.50 1 309 . 64 THR CG2 C 21.25 0.50 1 310 . 64 THR N N 113.16 0.25 1 311 . 65 PHE H H 8.63 0.03 1 312 . 65 PHE CA C 58.15 0.50 1 313 . 65 PHE CB C 40.71 0.50 1 314 . 65 PHE N N 116.84 0.25 1 315 . 66 GLY H H 7.89 0.03 1 316 . 66 GLY CA C 44.51 0.50 1 317 . 66 GLY N N 109.05 0.25 1 318 . 67 GLU H H 8.61 0.03 1 319 . 67 GLU CA C 59.22 0.50 1 320 . 67 GLU CB C 29.35 0.50 1 321 . 67 GLU CG C 35.60 0.50 1 322 . 67 GLU N N 119.09 0.25 1 323 . 68 GLU H H 8.86 0.03 1 324 . 68 GLU CA C 59.16 0.50 1 325 . 68 GLU CB C 28.33 0.50 1 326 . 68 GLU N N 119.52 0.25 1 327 . 69 LYS H H 7.58 0.03 1 328 . 69 LYS CA C 57.01 0.50 1 329 . 69 LYS CB C 31.32 0.50 1 330 . 69 LYS CD C 27.26 0.50 1 331 . 69 LYS CE C 39.88 0.50 1 332 . 69 LYS CG C 24.77 0.50 1 333 . 69 LYS N N 116.76 0.25 1 334 . 70 GLU H H 7.77 0.03 1 335 . 70 GLU CA C 60.11 0.50 1 336 . 70 GLU CB C 29.11 0.50 1 337 . 70 GLU CG C 35.64 0.50 1 338 . 70 GLU N N 118.83 0.25 1 339 . 71 ALA H H 7.74 0.03 1 340 . 71 ALA CA C 54.37 0.50 1 341 . 71 ALA CB C 17.76 0.50 1 342 . 71 ALA N N 117.84 0.25 1 343 . 72 ILE H H 7.37 0.03 1 344 . 72 ILE CA C 64.03 0.50 1 345 . 72 ILE CB C 36.68 0.50 1 346 . 72 ILE N N 118.17 0.25 1 347 . 73 PHE H H 7.01 0.03 1 348 . 73 PHE CA C 61.65 0.50 1 349 . 73 PHE CB C 38.04 0.50 1 350 . 73 PHE N N 116.48 0.25 1 351 . 74 GLU H H 8.23 0.03 1 352 . 74 GLU CA C 59.51 0.50 1 353 . 74 GLU CB C 28.91 0.50 1 354 . 74 GLU CG C 35.51 0.50 1 355 . 74 GLU N N 120.73 0.25 1 356 . 75 GLY H H 7.74 0.03 1 357 . 75 GLY CA C 46.69 0.50 1 358 . 75 GLY N N 105.73 0.25 1 359 . 76 HIS CB C 31.55 0.50 1 360 . 77 ILE H H 7.99 0.03 1 361 . 77 ILE CA C 66.03 0.50 1 362 . 77 ILE CB C 37.86 0.50 1 363 . 77 ILE N N 119.62 0.25 1 364 . 78 MET H H 7.86 0.03 1 365 . 78 MET CA C 58.77 0.50 1 366 . 78 MET CB C 32.77 0.50 1 367 . 78 MET CG C 31.85 0.50 1 368 . 78 MET N N 116.74 0.25 1 369 . 79 LEU H H 8.03 0.03 1 370 . 79 LEU CA C 58.37 0.50 1 371 . 79 LEU CB C 41.77 0.50 1 372 . 79 LEU CD1 C 22.88 0.50 2 373 . 79 LEU CD2 C 24.98 0.50 2 374 . 79 LEU N N 119.03 0.25 1 375 . 80 LEU H H 7.98 0.03 1 376 . 80 LEU CA C 57.30 0.50 1 377 . 80 LEU CB C 41.52 0.50 1 378 . 80 LEU CD1 C 23.60 0.50 2 379 . 80 LEU CD2 C 26.00 0.50 2 380 . 80 LEU N N 116.52 0.25 1 381 . 81 GLU H H 7.97 0.03 1 382 . 81 GLU CA C 55.85 0.50 1 383 . 81 GLU CB C 28.24 0.50 1 384 . 81 GLU CG C 36.24 0.50 1 385 . 81 GLU N N 112.53 0.25 1 386 . 82 ASP H H 7.23 0.03 1 387 . 82 ASP CA C 55.88 0.50 1 388 . 82 ASP CB C 44.37 0.50 1 389 . 82 ASP N N 121.50 0.25 1 390 . 83 GLU H H 9.21 0.03 1 391 . 83 GLU CA C 59.53 0.50 1 392 . 83 GLU CB C 29.42 0.50 1 393 . 83 GLU CG C 36.43 0.50 1 394 . 83 GLU N N 127.86 0.25 1 395 . 84 GLU H H 8.64 0.03 1 396 . 84 GLU CA C 59.22 0.50 1 397 . 84 GLU CB C 28.15 0.50 1 398 . 84 GLU CG C 36.01 0.50 1 399 . 84 GLU N N 121.16 0.25 1 400 . 85 LEU H H 8.00 0.03 1 401 . 85 LEU CA C 58.30 0.50 1 402 . 85 LEU CB C 40.79 0.50 1 403 . 85 LEU CD2 C 26.11 0.50 2 404 . 85 LEU N N 122.17 0.25 1 405 . 86 GLU H H 7.59 0.03 1 406 . 86 GLU CA C 59.38 0.50 1 407 . 86 GLU CB C 29.76 0.50 1 408 . 86 GLU CG C 36.32 0.50 1 409 . 86 GLU N N 116.69 0.25 1 410 . 87 GLN HE21 H 6.77 0.03 2 411 . 87 GLN HE22 H 7.51 0.03 2 412 . 87 GLN H H 7.99 0.03 1 413 . 87 GLN CA C 58.48 0.50 1 414 . 87 GLN CB C 27.86 0.50 1 415 . 87 GLN CG C 33.73 0.50 1 416 . 87 GLN N N 115.26 0.25 1 417 . 87 GLN NE2 N 111.33 0.25 1 418 . 88 GLU H H 8.26 0.03 1 419 . 88 GLU CA C 59.38 0.50 1 420 . 88 GLU CB C 29.00 0.50 1 421 . 88 GLU CG C 35.86 0.50 1 422 . 88 GLU N N 119.91 0.25 1 423 . 89 ILE H H 7.81 0.03 1 424 . 89 ILE CA C 65.87 0.50 1 425 . 89 ILE CB C 36.80 0.50 1 426 . 89 ILE N N 119.21 0.25 1 427 . 90 ILE H H 8.22 0.03 1 428 . 90 ILE CA C 65.95 0.50 1 429 . 90 ILE CB C 36.77 0.50 1 430 . 90 ILE CG2 C 16.71 0.50 1 431 . 90 ILE N N 117.64 0.25 1 432 . 91 ALA H H 8.06 0.03 1 433 . 91 ALA CA C 55.10 0.50 1 434 . 91 ALA CB C 17.53 0.50 1 435 . 91 ALA N N 120.43 0.25 1 436 . 92 LEU H H 7.28 0.03 1 437 . 92 LEU CA C 57.83 0.50 1 438 . 92 LEU CB C 40.60 0.50 1 439 . 92 LEU CD1 C 26.19 0.50 2 440 . 92 LEU CD2 C 22.08 0.50 2 441 . 92 LEU N N 117.29 0.25 1 442 . 93 ILE H H 7.50 0.03 1 443 . 93 ILE CA C 64.77 0.50 1 444 . 93 ILE CB C 38.70 0.50 1 445 . 93 ILE CG2 C 17.11 0.50 1 446 . 93 ILE N N 119.83 0.25 1 447 . 94 LYS H H 8.56 0.03 1 448 . 94 LYS CA C 59.76 0.50 1 449 . 94 LYS CB C 32.65 0.50 1 450 . 94 LYS CD C 28.82 0.50 1 451 . 94 LYS N N 114.84 0.25 1 452 . 95 ASP H H 8.78 0.03 1 453 . 95 ASP CA C 55.58 0.50 1 454 . 95 ASP CB C 40.66 0.50 1 455 . 95 ASP N N 114.80 0.25 1 456 . 96 LYS H H 7.16 0.03 1 457 . 96 LYS CA C 55.00 0.50 1 458 . 96 LYS CB C 31.88 0.50 1 459 . 96 LYS CE C 42.21 0.50 1 460 . 96 LYS CG C 24.89 0.50 1 461 . 96 LYS N N 114.65 0.25 1 462 . 97 HIS H H 7.29 0.03 1 463 . 97 HIS CA C 55.60 0.50 1 464 . 97 HIS CB C 25.68 0.50 1 465 . 97 HIS N N 115.13 0.25 1 466 . 98 MET H H 7.32 0.03 1 467 . 98 MET CA C 55.22 0.50 1 468 . 98 MET CB C 35.28 0.50 1 469 . 98 MET CG C 32.25 0.50 1 470 . 98 MET N N 116.58 0.25 1 471 . 99 THR H H 8.35 0.03 1 472 . 99 THR CA C 60.66 0.50 1 473 . 99 THR CB C 71.29 0.50 1 474 . 99 THR N N 105.73 0.25 1 475 . 100 ALA H H 10.46 0.03 1 476 . 100 ALA CA C 55.29 0.50 1 477 . 100 ALA CB C 19.19 0.50 1 478 . 100 ALA N N 121.00 0.25 1 479 . 101 ASP H H 9.36 0.03 1 480 . 101 ASP CA C 55.34 0.50 1 481 . 101 ASP CB C 39.51 0.50 1 482 . 101 ASP N N 108.53 0.25 1 483 . 102 ALA H H 7.53 0.03 1 484 . 102 ALA CA C 55.39 0.50 1 485 . 102 ALA CB C 17.68 0.50 1 486 . 102 ALA N N 122.36 0.25 1 487 . 103 ALA H H 8.88 0.03 1 488 . 103 ALA CA C 54.32 0.50 1 489 . 103 ALA CB C 20.32 0.50 1 490 . 103 ALA N N 120.77 0.25 1 491 . 104 ALA H H 8.24 0.03 1 492 . 104 ALA CA C 54.60 0.50 1 493 . 104 ALA CB C 17.21 0.50 1 494 . 104 ALA N N 117.23 0.25 1 495 . 105 HIS H H 8.21 0.03 1 496 . 105 HIS CA C 60.41 0.50 1 497 . 105 HIS CB C 30.40 0.50 1 498 . 105 HIS N N 115.19 0.25 1 499 . 106 GLU H H 8.16 0.03 1 500 . 106 GLU CA C 59.28 0.50 1 501 . 106 GLU CB C 28.59 0.50 1 502 . 106 GLU CG C 35.25 0.50 1 503 . 106 GLU N N 117.21 0.25 1 504 . 107 VAL H H 7.82 0.03 1 505 . 107 VAL CA C 65.99 0.50 1 506 . 107 VAL CB C 31.53 0.50 1 507 . 107 VAL CG1 C 23.04 0.50 2 508 . 107 VAL N N 118.24 0.25 1 509 . 108 ILE H H 8.25 0.03 1 510 . 108 ILE CA C 63.90 0.50 1 511 . 108 ILE CB C 35.72 0.50 1 512 . 108 ILE CG1 C 27.60 0.50 1 513 . 108 ILE CG2 C 17.17 0.50 1 514 . 108 ILE N N 119.98 0.25 1 515 . 109 GLU H H 8.55 0.03 1 516 . 109 GLU CA C 58.27 0.50 1 517 . 109 GLU CB C 27.42 0.50 1 518 . 109 GLU CG C 34.91 0.50 1 519 . 109 GLU N N 118.52 0.25 1 520 . 110 GLY H H 7.76 0.03 1 521 . 110 GLY CA C 46.84 0.50 1 522 . 110 GLY N N 106.89 0.25 1 523 . 111 GLN HE22 H 6.18 0.03 2 524 . 111 GLN HE21 H 6.84 0.03 2 525 . 111 GLN H H 7.74 0.03 1 526 . 111 GLN CA C 57.87 0.50 1 527 . 111 GLN CB C 27.52 0.50 1 528 . 111 GLN CG C 32.36 0.50 1 529 . 111 GLN N N 121.41 0.25 1 530 . 111 GLN NE2 N 109.39 0.25 1 531 . 112 ALA H H 8.53 0.03 1 532 . 112 ALA CA C 55.63 0.50 1 533 . 112 ALA CB C 17.74 0.50 1 534 . 112 ALA N N 121.08 0.25 1 535 . 113 SER H H 8.43 0.03 1 536 . 113 SER CA C 61.51 0.50 1 537 . 113 SER CB C 62.47 0.50 1 538 . 113 SER N N 111.24 0.25 1 539 . 114 ALA H H 7.41 0.03 1 540 . 114 ALA CA C 54.52 0.50 1 541 . 114 ALA CB C 17.40 0.50 1 542 . 114 ALA N N 123.30 0.25 1 543 . 115 LEU H H 7.59 0.03 1 544 . 115 LEU CA C 56.93 0.50 1 545 . 115 LEU CB C 41.40 0.50 1 546 . 115 LEU CD1 C 24.50 0.50 2 547 . 115 LEU CG C 25.88 0.50 1 548 . 115 LEU N N 117.23 0.25 1 549 . 116 GLU H H 7.75 0.03 1 550 . 116 GLU CA C 57.93 0.50 1 551 . 116 GLU CB C 28.96 0.50 1 552 . 116 GLU CG C 36.58 0.50 1 553 . 116 GLU N N 115.67 0.25 1 554 . 117 GLU H H 7.43 0.03 1 555 . 117 GLU CA C 57.17 0.50 1 556 . 117 GLU CB C 29.29 0.50 1 557 . 117 GLU CG C 35.70 0.50 1 558 . 117 GLU N N 117.05 0.25 1 559 . 118 LEU H H 7.15 0.03 1 560 . 118 LEU CA C 54.90 0.50 1 561 . 118 LEU CB C 41.00 0.50 1 562 . 118 LEU CD1 C 22.02 0.50 2 563 . 118 LEU CD2 C 25.75 0.50 2 564 . 118 LEU N N 118.34 0.25 1 565 . 119 ASP H H 8.00 0.03 1 566 . 119 ASP CA C 54.70 0.50 1 567 . 119 ASP CB C 39.72 0.50 1 568 . 119 ASP N N 117.81 0.25 1 569 . 120 ASP H H 7.68 0.03 1 570 . 120 ASP CA C 53.56 0.50 1 571 . 120 ASP CB C 43.89 0.50 1 572 . 120 ASP N N 119.01 0.25 1 573 . 121 GLU H H 8.97 0.03 1 574 . 121 GLU CA C 59.68 0.50 1 575 . 121 GLU CB C 29.17 0.50 1 576 . 121 GLU CG C 35.55 0.50 1 577 . 121 GLU N N 126.52 0.25 1 578 . 122 TYR H H 8.24 0.03 1 579 . 122 TYR CA C 60.72 0.50 1 580 . 122 TYR CB C 37.06 0.50 1 581 . 122 TYR N N 119.42 0.25 1 582 . 123 LEU H H 8.07 0.03 1 583 . 123 LEU CA C 57.08 0.50 1 584 . 123 LEU CB C 40.12 0.50 1 585 . 123 LEU CG C 25.74 0.50 1 586 . 123 LEU N N 119.82 0.25 1 587 . 124 LYS H H 8.05 0.03 1 588 . 124 LYS CA C 59.73 0.50 1 589 . 124 LYS CB C 31.54 0.50 1 590 . 124 LYS CG C 24.88 0.50 1 591 . 124 LYS N N 118.75 0.25 1 592 . 125 GLU H H 7.61 0.03 1 593 . 125 GLU CA C 58.69 0.50 1 594 . 125 GLU CB C 28.34 0.50 1 595 . 125 GLU N N 119.79 0.25 1 596 . 126 ARG HE H 7.32 0.03 0 597 . 126 ARG CA C 58.06 0.50 1 598 . 126 ARG CD C 42.97 0.50 1 599 . 126 ARG CG C 25.11 0.50 1 600 . 126 ARG NE N 83.63 0.25 1 601 . 127 ALA H H 8.10 0.03 1 602 . 127 ALA CA C 55.02 0.50 1 603 . 127 ALA CB C 18.42 0.50 1 604 . 127 ALA N N 121.34 0.25 1 605 . 128 ALA H H 7.46 0.03 1 606 . 128 ALA CA C 54.75 0.50 1 607 . 128 ALA CB C 17.30 0.50 1 608 . 128 ALA N N 118.91 0.25 1 609 . 129 ASP H H 7.67 0.03 1 610 . 129 ASP CA C 57.51 0.50 1 611 . 129 ASP CB C 39.91 0.50 1 612 . 129 ASP N N 120.41 0.25 1 613 . 130 VAL H H 7.66 0.03 1 614 . 130 VAL CA C 65.92 0.50 1 615 . 130 VAL CB C 31.11 0.50 1 616 . 130 VAL CG1 C 21.63 0.50 2 617 . 130 VAL N N 120.23 0.25 1 618 . 131 ARG HE H 8.67 0.03 0 619 . 131 ARG H H 8.25 0.03 1 620 . 131 ARG CA C 60.50 0.50 1 621 . 131 ARG CB C 28.77 0.50 1 622 . 131 ARG CD C 42.58 0.50 1 623 . 131 ARG CG C 29.19 0.50 1 624 . 131 ARG N N 117.50 0.25 1 625 . 131 ARG NE N 86.33 0.25 1 626 . 132 ASP H H 7.97 0.03 1 627 . 132 ASP CA C 57.29 0.50 1 628 . 132 ASP CB C 41.19 0.50 1 629 . 132 ASP N N 121.30 0.25 1 630 . 133 ILE H H 8.11 0.03 1 631 . 133 ILE CA C 64.48 0.50 1 632 . 133 ILE CB C 37.84 0.50 1 633 . 133 ILE CG1 C 27.45 0.50 1 634 . 133 ILE CG2 C 18.42 0.50 1 635 . 133 ILE N N 119.13 0.25 1 636 . 134 GLY H H 8.73 0.03 1 637 . 134 GLY CA C 47.83 0.50 1 638 . 134 GLY N N 107.41 0.25 1 639 . 135 LYS H H 8.50 0.03 1 640 . 135 LYS CA C 59.96 0.50 1 641 . 135 LYS CB C 31.57 0.50 1 642 . 135 LYS CD C 28.93 0.50 1 643 . 135 LYS CG C 25.01 0.50 1 644 . 135 LYS N N 122.26 0.25 1 645 . 136 ARG HE H 8.12 0.03 0 646 . 136 ARG H H 7.61 0.03 1 647 . 136 ARG CA C 59.70 0.50 1 648 . 136 ARG CB C 29.46 0.50 1 649 . 136 ARG CD C 42.01 0.50 1 650 . 136 ARG N N 119.09 0.25 1 651 . 136 ARG NE N 80.09 0.25 1 652 . 137 LEU H H 8.87 0.03 1 653 . 137 LEU CA C 58.60 0.50 1 654 . 137 LEU CB C 40.85 0.50 1 655 . 137 LEU CD1 C 24.99 0.50 2 656 . 137 LEU CD2 C 21.30 0.50 2 657 . 137 LEU CG C 26.10 0.50 1 658 . 137 LEU N N 121.77 0.25 1 659 . 138 LEU H H 8.89 0.03 1 660 . 138 LEU CA C 58.09 0.50 1 661 . 138 LEU CB C 41.08 0.50 1 662 . 138 LEU CD2 C 24.90 0.50 2 663 . 138 LEU CG C 27.14 0.50 1 664 . 138 LEU N N 118.59 0.25 1 665 . 139 ARG H H 8.68 0.03 1 666 . 139 ARG CA C 61.13 0.50 1 667 . 139 ARG CB C 29.31 0.50 1 668 . 139 ARG CD C 42.75 0.50 1 669 . 139 ARG N N 115.61 0.25 1 670 . 140 ASN H H 7.63 0.03 1 671 . 140 ASN CA C 56.88 0.50 1 672 . 140 ASN CB C 40.73 0.50 1 673 . 140 ASN N N 114.39 0.25 1 674 . 141 ILE H H 8.73 0.03 1 675 . 141 ILE CA C 65.81 0.50 1 676 . 141 ILE CB C 38.18 0.50 1 677 . 141 ILE CG2 C 16.45 0.50 1 678 . 141 ILE N N 121.89 0.25 1 679 . 142 LEU H H 8.03 0.03 1 680 . 142 LEU CA C 55.45 0.50 1 681 . 142 LEU CB C 42.66 0.50 1 682 . 142 LEU CD1 C 22.39 0.50 2 683 . 142 LEU CD2 C 25.59 0.50 2 684 . 142 LEU N N 115.25 0.25 1 685 . 143 GLY H H 7.60 0.03 1 686 . 143 GLY CA C 46.38 0.50 1 687 . 143 GLY N N 108.50 0.25 1 688 . 144 LEU H H 8.16 0.03 1 689 . 144 LEU CA C 53.22 0.50 1 690 . 144 LEU CB C 42.02 0.50 1 691 . 144 LEU CD1 C 25.91 0.50 2 692 . 144 LEU N N 119.26 0.25 1 693 . 145 LYS H H 8.38 0.03 1 694 . 145 LYS CA C 56.82 0.50 1 695 . 145 LYS CB C 32.08 0.50 1 696 . 145 LYS CD C 27.96 0.50 1 697 . 145 LYS CE C 41.61 0.50 1 698 . 145 LYS CG C 23.93 0.50 1 699 . 145 LYS N N 119.73 0.25 1 700 . 146 ILE H H 8.26 0.03 1 701 . 146 ILE CA C 58.84 0.50 1 702 . 146 ILE CB C 38.40 0.50 1 703 . 146 ILE CG1 C 26.65 0.50 1 704 . 146 ILE CG2 C 16.79 0.50 1 705 . 146 ILE N N 125.93 0.25 1 706 . 147 ILE H H 8.80 0.03 1 707 . 147 ILE CA C 61.79 0.50 1 708 . 147 ILE CB C 37.49 0.50 1 709 . 147 ILE CG1 C 27.32 0.50 1 710 . 147 ILE CG2 C 16.53 0.50 1 711 . 147 ILE N N 128.67 0.25 1 712 . 148 ASP H H 8.31 0.03 1 713 . 148 ASP CA C 52.21 0.50 1 714 . 148 ASP CB C 40.53 0.50 1 715 . 148 ASP N N 125.78 0.25 1 716 . 149 LEU H H 8.50 0.03 1 717 . 149 LEU CA C 55.57 0.50 1 718 . 149 LEU CB C 40.40 0.50 1 719 . 149 LEU CD1 C 22.67 0.50 2 720 . 149 LEU CD2 C 24.96 0.50 2 721 . 149 LEU CG C 26.53 0.50 1 722 . 149 LEU N N 125.53 0.25 1 723 . 150 SER H H 8.53 0.03 1 724 . 150 SER CA C 60.28 0.50 1 725 . 150 SER CB C 63.36 0.50 1 726 . 150 SER N N 115.48 0.25 1 727 . 151 ALA H H 7.41 0.03 1 728 . 151 ALA CA C 51.30 0.50 1 729 . 151 ALA CB C 18.42 0.50 1 730 . 151 ALA N N 124.28 0.25 1 731 . 152 ILE H H 6.88 0.03 1 732 . 152 ILE CA C 62.45 0.50 1 733 . 152 ILE CB C 37.74 0.50 1 734 . 152 ILE CG1 C 26.50 0.50 1 735 . 152 ILE CG2 C 17.50 0.50 1 736 . 152 ILE N N 118.81 0.25 1 737 . 153 GLN HE21 H 6.73 0.03 2 738 . 153 GLN HE22 H 7.33 0.03 2 739 . 153 GLN H H 8.64 0.03 1 740 . 153 GLN CA C 55.93 0.50 1 741 . 153 GLN CB C 30.00 0.50 1 742 . 153 GLN CG C 33.00 0.50 1 743 . 153 GLN N N 124.56 0.25 1 744 . 153 GLN NE2 N 111.58 0.25 1 745 . 154 ASP H H 7.44 0.03 1 746 . 154 ASP CA C 52.64 0.50 1 747 . 154 ASP CB C 43.14 0.50 1 748 . 154 ASP N N 119.57 0.25 1 749 . 155 GLU H H 8.09 0.03 1 750 . 155 GLU CA C 56.25 0.50 1 751 . 155 GLU CB C 28.94 0.50 1 752 . 155 GLU CG C 36.42 0.50 1 753 . 155 GLU N N 117.06 0.25 1 754 . 156 VAL H H 8.31 0.03 1 755 . 156 VAL CA C 58.63 0.50 1 756 . 156 VAL CB C 36.45 0.50 1 757 . 156 VAL CG1 C 21.54 0.50 2 758 . 156 VAL CG2 C 16.79 0.50 2 759 . 156 VAL N N 115.25 0.25 1 760 . 157 ILE H H 8.56 0.03 1 761 . 157 ILE CA C 60.37 0.50 1 762 . 157 ILE CB C 38.51 0.50 1 763 . 157 ILE CG1 C 28.68 0.50 1 764 . 157 ILE CG2 C 17.01 0.50 1 765 . 157 ILE N N 120.81 0.25 1 766 . 158 LEU H H 7.81 0.03 1 767 . 158 LEU CA C 54.75 0.50 1 768 . 158 LEU CB C 43.24 0.50 1 769 . 158 LEU CD1 C 25.16 0.50 2 770 . 158 LEU CG C 26.62 0.50 1 771 . 158 LEU N N 127.85 0.25 1 772 . 159 VAL H H 8.68 0.03 1 773 . 159 VAL CA C 60.41 0.50 1 774 . 159 VAL CB C 32.52 0.50 1 775 . 159 VAL CG1 C 22.92 0.50 2 776 . 159 VAL CG2 C 20.37 0.50 2 777 . 159 VAL N N 124.91 0.25 1 778 . 160 ALA H H 8.26 0.03 1 779 . 160 ALA CA C 49.76 0.50 1 780 . 160 ALA CB C 23.70 0.50 1 781 . 160 ALA N N 125.39 0.25 1 782 . 161 ALA H H 9.33 0.03 1 783 . 161 ALA CA C 55.54 0.50 1 784 . 161 ALA CB C 17.61 0.50 1 785 . 161 ALA N N 124.68 0.25 1 786 . 162 ASP H H 7.48 0.03 1 787 . 162 ASP CA C 52.51 0.50 1 788 . 162 ASP CB C 42.06 0.50 1 789 . 162 ASP N N 109.44 0.25 1 790 . 163 LEU H H 7.95 0.03 1 791 . 163 LEU CA C 54.01 0.50 1 792 . 163 LEU CB C 44.72 0.50 1 793 . 163 LEU CD2 C 24.70 0.50 2 794 . 163 LEU CG C 26.38 0.50 1 795 . 163 LEU N N 118.95 0.25 1 796 . 164 THR H H 8.91 0.03 1 797 . 164 THR CA C 59.10 0.50 1 798 . 164 THR CB C 68.09 0.50 1 799 . 164 THR N N 114.99 0.25 1 800 . 165 PRO CA C 64.62 0.50 1 801 . 166 SER H H 8.69 0.03 1 802 . 166 SER CA C 61.25 0.50 1 803 . 166 SER CB C 61.25 0.50 1 804 . 166 SER N N 111.81 0.25 1 805 . 167 GLU H H 7.42 0.03 1 806 . 167 GLU CA C 58.73 0.50 1 807 . 167 GLU CB C 29.35 0.50 1 808 . 167 GLU CG C 36.59 0.50 1 809 . 167 GLU N N 121.06 0.25 1 810 . 168 THR H H 8.35 0.03 1 811 . 168 THR CA C 65.10 0.50 1 812 . 168 THR CB C 67.57 0.50 1 813 . 168 THR CG2 C 22.07 0.50 1 814 . 168 THR N N 109.99 0.25 1 815 . 169 ALA H H 7.61 0.03 1 816 . 169 ALA CA C 53.70 0.50 1 817 . 169 ALA CB C 18.75 0.50 1 818 . 169 ALA N N 119.68 0.25 1 819 . 170 GLN HE21 H 7.00 0.03 2 820 . 170 GLN HE22 H 7.55 0.03 2 821 . 170 GLN H H 7.09 0.03 1 822 . 170 GLN CA C 55.45 0.50 1 823 . 170 GLN CB C 30.95 0.50 1 824 . 170 GLN CG C 34.49 0.50 1 825 . 170 GLN N N 111.36 0.25 1 826 . 170 GLN NE2 N 112.28 0.25 1 827 . 171 LEU H H 7.09 0.03 1 828 . 171 LEU CA C 55.23 0.50 1 829 . 171 LEU CB C 42.77 0.50 1 830 . 171 LEU CD1 C 25.24 0.50 2 831 . 171 LEU CD2 C 23.89 0.50 2 832 . 171 LEU N N 116.48 0.25 1 833 . 172 ASN H H 7.79 0.03 1 834 . 172 ASN CA C 51.51 0.50 1 835 . 172 ASN CB C 36.53 0.50 1 836 . 172 ASN N N 117.88 0.25 1 837 . 173 LEU H H 8.30 0.03 1 838 . 173 LEU CA C 56.90 0.50 1 839 . 173 LEU CB C 40.25 0.50 1 840 . 173 LEU CD1 C 24.86 0.50 2 841 . 173 LEU CD2 C 22.40 0.50 2 842 . 173 LEU N N 125.06 0.25 1 843 . 174 LYS H H 7.88 0.03 1 844 . 174 LYS CA C 57.02 0.50 1 845 . 174 LYS CB C 31.29 0.50 1 846 . 174 LYS CG C 24.24 0.50 1 847 . 174 LYS N N 115.02 0.25 1 848 . 175 LYS H H 7.49 0.03 1 849 . 175 LYS CA C 54.22 0.50 1 850 . 175 LYS CB C 32.43 0.50 1 851 . 175 LYS CG C 23.71 0.50 1 852 . 175 LYS N N 115.43 0.25 1 853 . 176 VAL H H 7.14 0.03 1 854 . 176 VAL CA C 61.66 0.50 1 855 . 176 VAL CB C 31.55 0.50 1 856 . 176 VAL CG2 C 21.51 0.50 2 857 . 176 VAL N N 116.84 0.25 1 858 . 177 LEU H H 8.78 0.03 1 859 . 177 LEU CA C 54.23 0.50 1 860 . 177 LEU CB C 42.91 0.50 1 861 . 177 LEU CD1 C 21.21 0.50 2 862 . 177 LEU CD2 C 25.69 0.50 2 863 . 177 LEU N N 122.75 0.25 1 864 . 178 GLY H H 6.95 0.03 1 865 . 178 GLY CA C 44.67 0.50 1 866 . 178 GLY N N 100.39 0.25 1 867 . 179 PHE H H 7.83 0.03 1 868 . 179 PHE CA C 56.03 0.50 1 869 . 179 PHE CB C 43.38 0.50 1 870 . 179 PHE N N 114.72 0.25 1 871 . 180 ILE H H 8.81 0.03 1 872 . 180 ILE CA C 59.56 0.50 1 873 . 180 ILE CB C 40.17 0.50 1 874 . 180 ILE CG1 C 26.43 0.50 1 875 . 180 ILE CG2 C 19.51 0.50 1 876 . 180 ILE N N 119.22 0.25 1 877 . 181 THR H H 8.26 0.03 1 878 . 181 THR CA C 58.25 0.50 1 879 . 181 THR CB C 71.38 0.50 1 880 . 181 THR CG2 C 20.12 0.50 1 881 . 181 THR N N 111.20 0.25 1 882 . 182 ASP H H 8.11 0.03 1 883 . 182 ASP CA C 56.23 0.50 1 884 . 182 ASP CB C 40.87 0.50 1 885 . 182 ASP N N 123.82 0.25 1 886 . 183 ALA H H 8.59 0.03 1 887 . 183 ALA CA C 50.40 0.50 1 888 . 183 ALA CB C 20.12 0.50 1 889 . 183 ALA N N 121.68 0.25 1 890 . 184 GLY H H 8.42 0.03 1 891 . 184 GLY CA C 44.78 0.50 1 892 . 184 GLY N N 109.57 0.25 1 893 . 185 GLY H H 7.77 0.03 1 894 . 185 GLY CA C 43.84 0.50 1 895 . 185 GLY N N 103.89 0.25 1 896 . 187 THR CA C 60.24 0.50 1 897 . 187 THR CB C 67.81 0.50 1 898 . 188 SER H H 7.43 0.03 1 899 . 188 SER CA C 57.99 0.50 1 900 . 188 SER CB C 64.18 0.50 1 901 . 188 SER N N 116.96 0.25 1 902 . 189 HIS H H 9.15 0.03 1 903 . 189 HIS CA C 60.11 0.50 1 904 . 189 HIS CB C 28.27 0.50 1 905 . 189 HIS N N 121.54 0.25 1 906 . 190 THR H H 8.45 0.03 1 907 . 190 THR CA C 67.07 0.50 1 908 . 190 THR CB C 67.88 0.50 1 909 . 190 THR N N 114.19 0.25 1 910 . 191 SER CA C 61.91 0.50 2 911 . 192 ILE H H 7.96 0.03 1 912 . 192 ILE CA C 64.41 0.50 1 913 . 192 ILE CB C 37.41 0.50 1 914 . 192 ILE N N 120.71 0.25 1 915 . 193 MET H H 8.33 0.03 1 916 . 193 MET CA C 57.66 0.50 1 917 . 193 MET CB C 30.54 0.50 1 918 . 193 MET N N 120.33 0.25 1 919 . 194 ALA H H 8.47 0.03 1 920 . 194 ALA CA C 56.06 0.50 1 921 . 194 ALA CB C 17.75 0.50 1 922 . 194 ALA N N 121.48 0.25 1 923 . 195 ARG H H 8.16 0.03 1 924 . 195 ARG CA C 59.76 0.50 1 925 . 195 ARG CB C 30.12 0.50 1 926 . 195 ARG CD C 43.70 0.50 1 927 . 195 ARG CG C 28.96 0.50 1 928 . 195 ARG N N 115.69 0.25 1 929 . 196 SER H H 8.00 0.03 1 930 . 196 SER CA C 61.36 0.50 1 931 . 196 SER CB C 62.61 0.50 1 932 . 196 SER N N 116.00 0.25 1 933 . 197 LEU H H 7.54 0.03 1 934 . 197 LEU CA C 54.25 0.50 1 935 . 197 LEU CB C 42.30 0.50 1 936 . 197 LEU CD2 C 21.61 0.50 2 937 . 197 LEU CG C 25.76 0.50 2 938 . 197 LEU N N 120.02 0.25 1 939 . 198 GLU H H 7.80 0.03 1 940 . 198 GLU CA C 57.13 0.50 1 941 . 198 GLU CB C 26.50 0.50 1 942 . 198 GLU N N 115.94 0.25 1 943 . 199 LEU H H 8.13 0.03 1 944 . 199 LEU CA C 50.88 0.50 1 945 . 199 LEU CB C 44.00 0.50 1 946 . 199 LEU N N 119.36 0.25 1 947 . 200 PRO CA C 61.65 0.50 1 948 . 200 PRO CB C 31.85 0.50 1 949 . 200 PRO CD C 49.63 0.50 1 950 . 200 PRO CG C 27.62 0.50 1 951 . 201 ALA H H 8.66 0.03 1 952 . 201 ALA CA C 51.49 0.50 1 953 . 201 ALA CB C 21.36 0.50 1 954 . 201 ALA N N 118.51 0.25 1 955 . 202 ILE H H 7.77 0.03 1 956 . 202 ILE CA C 60.76 0.50 1 957 . 202 ILE CB C 40.89 0.50 1 958 . 202 ILE CG2 C 16.85 0.50 1 959 . 202 ILE N N 121.92 0.25 1 960 . 203 VAL H H 8.32 0.03 1 961 . 203 VAL CA C 57.36 0.50 1 962 . 203 VAL CB C 33.29 0.50 1 963 . 203 VAL CG2 C 19.03 0.50 1 964 . 203 VAL N N 115.83 0.25 1 965 . 204 GLY H H 7.36 0.03 1 966 . 204 GLY CA C 48.27 0.50 1 967 . 204 GLY N N 105.96 0.25 1 968 . 205 THR H H 7.81 0.03 1 969 . 205 THR CA C 62.92 0.50 1 970 . 205 THR CB C 70.55 0.50 1 971 . 205 THR CG2 C 21.89 0.50 1 972 . 205 THR N N 106.05 0.25 1 973 . 206 GLY H H 9.96 0.03 1 974 . 206 GLY CA C 47.06 0.50 1 975 . 206 GLY N N 115.11 0.25 1 976 . 207 SER H H 7.77 0.03 1 977 . 207 SER CA C 57.63 0.50 1 978 . 207 SER CB C 63.44 0.50 1 979 . 207 SER N N 112.36 0.25 1 980 . 208 VAL H H 7.85 0.03 1 981 . 208 VAL CA C 66.59 0.50 1 982 . 208 VAL CB C 29.62 0.50 1 983 . 208 VAL N N 127.23 0.25 1 984 . 209 THR H H 9.75 0.03 1 985 . 209 THR CA C 64.44 0.50 1 986 . 209 THR CB C 68.77 0.50 1 987 . 209 THR N N 112.67 0.25 1 988 . 210 SER H H 7.62 0.03 1 989 . 210 SER CA C 58.94 0.50 1 990 . 210 SER CB C 63.84 0.50 1 991 . 210 SER N N 113.93 0.25 1 992 . 211 GLN HE21 H 6.94 0.03 2 993 . 211 GLN HE22 H 6.76 0.03 2 994 . 211 GLN H H 7.64 0.03 1 995 . 211 GLN CA C 56.34 0.50 1 996 . 211 GLN CB C 31.96 0.50 1 997 . 211 GLN CG C 34.15 0.50 1 998 . 211 GLN N N 118.82 0.25 1 999 . 211 GLN NE2 N 111.27 0.25 1 1000 . 212 VAL H H 7.29 0.03 1 1001 . 212 VAL CA C 60.70 0.50 1 1002 . 212 VAL CB C 33.89 0.50 1 1003 . 212 VAL CG1 C 22.20 0.50 2 1004 . 212 VAL N N 118.45 0.25 1 1005 . 213 LYS H H 8.86 0.03 1 1006 . 213 LYS CA C 53.41 0.50 1 1007 . 213 LYS CB C 34.11 0.50 1 1008 . 213 LYS CD C 27.94 0.50 1 1009 . 213 LYS CE C 41.66 0.50 1 1010 . 213 LYS CG C 23.22 0.50 1 1011 . 213 LYS N N 123.73 0.25 1 1012 . 214 ASN HD21 H 6.95 0.03 2 1013 . 214 ASN HD22 H 7.45 0.03 2 1014 . 214 ASN H H 8.46 0.03 1 1015 . 214 ASN CA C 55.34 0.50 1 1016 . 214 ASN CB C 38.53 0.50 1 1017 . 214 ASN N N 117.84 0.25 1 1018 . 214 ASN ND2 N 111.84 0.25 1 1019 . 215 ASP H H 8.86 0.03 1 1020 . 215 ASP CA C 57.24 0.50 1 1021 . 215 ASP CB C 38.92 0.50 1 1022 . 215 ASP N N 116.14 0.25 1 1023 . 216 ASP H H 7.89 0.03 1 1024 . 216 ASP CA C 55.88 0.50 1 1025 . 216 ASP CB C 41.22 0.50 1 1026 . 216 ASP N N 120.54 0.25 1 1027 . 217 TYR H H 8.53 0.03 1 1028 . 217 TYR CA C 58.80 0.50 1 1029 . 217 TYR CB C 39.10 0.50 1 1030 . 217 TYR N N 122.51 0.25 1 1031 . 218 LEU H H 8.57 0.03 1 1032 . 218 LEU CA C 52.38 0.50 1 1033 . 218 LEU CB C 44.66 0.50 1 1034 . 218 LEU CD2 C 25.46 0.50 2 1035 . 218 LEU N N 126.59 0.25 1 1036 . 219 ILE H H 7.96 0.03 1 1037 . 219 ILE CA C 60.71 0.50 1 1038 . 219 ILE CB C 38.80 0.50 1 1039 . 219 ILE N N 114.32 0.25 1 1040 . 220 LEU H H 9.07 0.03 1 1041 . 220 LEU CA C 53.15 0.50 1 1042 . 220 LEU CB C 43.07 0.50 1 1043 . 220 LEU CD1 C 24.33 0.50 2 1044 . 220 LEU CD2 C 25.63 0.50 2 1045 . 220 LEU CG C 26.89 0.50 1 1046 . 220 LEU N N 130.01 0.25 1 1047 . 221 ASP H H 8.58 0.03 1 1048 . 221 ASP CA C 52.56 0.50 1 1049 . 221 ASP CB C 39.74 0.50 1 1050 . 221 ASP N N 124.17 0.25 1 1051 . 222 ALA H H 8.38 0.03 1 1052 . 222 ALA CA C 51.36 0.50 1 1053 . 222 ALA CB C 17.45 0.50 1 1054 . 222 ALA N N 127.64 0.25 1 1055 . 223 VAL H H 8.71 0.03 1 1056 . 223 VAL CA C 64.90 0.50 1 1057 . 223 VAL CB C 32.00 0.50 1 1058 . 223 VAL N N 117.66 0.25 1 1059 . 224 ASN H H 9.53 0.03 1 1060 . 224 ASN CA C 52.96 0.50 1 1061 . 224 ASN CB C 38.74 0.50 1 1062 . 224 ASN N N 116.66 0.25 1 1063 . 225 ASN H H 7.57 0.03 1 1064 . 225 ASN CA C 52.78 0.50 1 1065 . 225 ASN CB C 35.78 0.50 1 1066 . 225 ASN N N 116.87 0.25 1 1067 . 226 GLN HE21 H 6.54 0.03 2 1068 . 226 GLN HE22 H 7.17 0.03 2 1069 . 226 GLN H H 8.69 0.03 1 1070 . 226 GLN CA C 55.21 0.50 1 1071 . 226 GLN CB C 32.76 0.50 1 1072 . 226 GLN CG C 33.27 0.50 1 1073 . 226 GLN N N 118.04 0.25 1 1074 . 226 GLN NE2 N 109.76 0.25 1 1075 . 227 VAL H H 7.82 0.03 1 1076 . 227 VAL CA C 60.23 0.50 1 1077 . 227 VAL CB C 32.88 0.50 1 1078 . 227 VAL CG1 C 21.13 0.50 2 1079 . 227 VAL CG2 C 20.39 0.50 2 1080 . 227 VAL N N 120.64 0.25 1 1081 . 228 TYR H H 9.01 0.03 1 1082 . 228 TYR CA C 56.76 0.50 1 1083 . 228 TYR CB C 38.66 0.50 1 1084 . 228 TYR N N 126.17 0.25 1 1085 . 229 VAL H H 8.45 0.03 1 1086 . 229 VAL CA C 61.41 0.50 1 1087 . 229 VAL CB C 31.85 0.50 1 1088 . 229 VAL CG2 C 20.62 0.50 2 1089 . 229 VAL N N 122.70 0.25 1 1090 . 230 ASN H H 10.03 0.03 1 1091 . 230 ASN CA C 54.56 0.50 1 1092 . 230 ASN CB C 37.47 0.50 1 1093 . 230 ASN N N 123.91 0.25 1 1094 . 231 PRO CA C 61.65 0.50 1 1095 . 231 PRO CB C 32.15 0.50 1 1096 . 231 PRO CD C 50.76 0.50 1 1097 . 231 PRO CG C 26.09 0.50 1 1098 . 232 THR H H 7.74 0.03 1 1099 . 232 THR CA C 60.45 0.50 1 1100 . 232 THR CB C 70.33 0.50 1 1101 . 232 THR N N 108.48 0.25 1 1102 . 233 ASN HD21 H 6.84 0.03 2 1103 . 233 ASN HD22 H 7.59 0.03 2 1104 . 233 ASN H H 8.83 0.03 1 1105 . 233 ASN CA C 56.53 0.50 1 1106 . 233 ASN CB C 37.39 0.50 1 1107 . 233 ASN N N 118.59 0.25 1 1108 . 233 ASN ND2 N 111.94 0.25 1 1109 . 234 GLU H H 8.51 0.03 1 1110 . 234 GLU CA C 59.34 0.50 1 1111 . 234 GLU CB C 28.43 0.50 1 1112 . 234 GLU CG C 35.97 0.50 1 1113 . 234 GLU N N 118.11 0.25 1 1114 . 235 VAL H H 7.17 0.03 1 1115 . 235 VAL CA C 66.06 0.50 1 1116 . 235 VAL CB C 30.86 0.50 1 1117 . 235 VAL CG1 C 22.65 0.50 2 1118 . 235 VAL N N 121.35 0.25 1 1119 . 236 ILE H H 8.00 0.03 1 1120 . 236 ILE CA C 66.30 0.50 1 1121 . 236 ILE CB C 37.30 0.50 1 1122 . 236 ILE CG2 C 16.76 0.50 1 1123 . 236 ILE N N 120.42 0.25 1 1124 . 237 ASP H H 8.23 0.03 1 1125 . 237 ASP CA C 57.51 0.50 1 1126 . 237 ASP CB C 39.86 0.50 1 1127 . 237 ASP N N 117.64 0.25 1 1128 . 238 LYS H H 7.67 0.03 1 1129 . 238 LYS CA C 59.02 0.50 1 1130 . 238 LYS CB C 31.62 0.50 1 1131 . 238 LYS CD C 28.48 0.50 1 1132 . 238 LYS CG C 24.10 0.50 1 1133 . 238 LYS N N 120.45 0.25 1 1134 . 239 MET H H 8.46 0.03 1 1135 . 239 MET CA C 55.13 0.50 1 1136 . 239 MET CB C 29.16 0.50 1 1137 . 239 MET CG C 30.87 0.50 1 1138 . 239 MET N N 117.16 0.25 1 1139 . 240 ARG HE H 6.48 0.03 2 1140 . 240 ARG H H 9.02 0.03 1 1141 . 240 ARG CA C 58.77 0.50 1 1142 . 240 ARG CB C 28.89 0.50 1 1143 . 240 ARG CD C 42.41 0.50 1 1144 . 240 ARG CG C 26.23 0.50 1 1145 . 240 ARG N N 123.50 0.25 1 1146 . 240 ARG NE N 83.39 0.25 1 1147 . 241 ALA H H 7.42 0.03 1 1148 . 241 ALA CA C 54.74 0.50 1 1149 . 241 ALA CB C 17.09 0.50 1 1150 . 241 ALA N N 121.44 0.25 1 1151 . 242 VAL H H 7.65 0.03 1 1152 . 242 VAL CA C 65.92 0.50 1 1153 . 242 VAL N N 120.23 0.25 1 1154 . 243 GLN HE21 H 6.78 0.03 2 1155 . 243 GLN HE22 H 7.50 0.03 2 1156 . 243 GLN H H 8.37 0.03 1 1157 . 243 GLN CA C 59.26 0.50 1 1158 . 243 GLN CB C 28.31 0.50 1 1159 . 243 GLN CG C 33.41 0.50 1 1160 . 243 GLN N N 119.53 0.25 1 1161 . 243 GLN NE2 N 110.89 0.25 1 1162 . 244 GLU H H 8.07 0.03 1 1163 . 244 GLU CA C 58.91 0.50 1 1164 . 244 GLU CB C 29.01 0.50 1 1165 . 244 GLU CG C 35.75 0.50 1 1166 . 244 GLU N N 118.55 0.25 1 1167 . 245 GLN HE21 H 6.68 0.03 2 1168 . 245 GLN HE22 H 7.54 0.03 2 1169 . 245 GLN H H 7.92 0.03 1 1170 . 245 GLN CA C 58.56 0.50 1 1171 . 245 GLN CB C 27.64 0.50 1 1172 . 245 GLN CG C 33.06 0.50 1 1173 . 245 GLN N N 120.71 0.25 1 1174 . 245 GLN NE2 N 110.89 0.25 1 1175 . 246 VAL H H 8.41 0.03 1 1176 . 246 VAL CA C 65.20 0.50 1 1177 . 246 VAL CB C 31.31 0.50 1 1178 . 246 VAL CG1 C 21.77 0.50 2 1179 . 246 VAL N N 119.56 0.25 1 1180 . 247 ALA H H 8.11 0.03 1 1181 . 247 ALA CA C 54.44 0.50 1 1182 . 247 ALA CB C 17.65 0.50 1 1183 . 247 ALA N N 122.17 0.25 1 1184 . 248 SER H H 8.15 0.03 1 1185 . 248 SER CA C 60.70 0.50 1 1186 . 248 SER CB C 62.64 0.50 1 1187 . 248 SER N N 114.65 0.25 1 1188 . 249 GLU H H 8.08 0.03 1 1189 . 249 GLU CA C 58.33 0.50 1 1190 . 249 GLU CB C 29.02 0.50 1 1191 . 249 GLU CG C 35.93 0.50 1 1192 . 249 GLU N N 122.19 0.25 1 1193 . 250 LYS H H 8.00 0.03 1 1194 . 250 LYS CA C 58.33 0.50 1 1195 . 250 LYS CB C 31.73 0.50 1 1196 . 250 LYS CD C 28.10 0.50 1 1197 . 250 LYS CE C 41.60 0.50 1 1198 . 250 LYS CG C 24.22 0.50 1 1199 . 250 LYS N N 119.36 0.25 1 1200 . 251 ALA H H 7.95 0.03 1 1201 . 251 ALA CA C 53.89 0.50 1 1202 . 251 ALA CB C 17.88 0.50 1 1203 . 251 ALA N N 122.06 0.25 1 1204 . 252 GLU H H 8.03 0.03 1 1205 . 252 GLU CA C 57.80 0.50 1 1206 . 252 GLU CB C 28.99 0.50 1 1207 . 252 GLU CG C 35.46 0.50 1 1208 . 252 GLU N N 118.17 0.25 1 1209 . 253 LEU H H 7.91 0.03 1 1210 . 253 LEU CA C 56.48 0.50 1 1211 . 253 LEU CB C 41.06 0.50 1 1212 . 253 LEU CD1 C 24.36 0.50 2 1213 . 253 LEU CD2 C 22.64 0.50 2 1214 . 253 LEU CG C 26.17 0.50 1 1215 . 253 LEU N N 120.00 0.25 1 1216 . 254 ALA H H 7.81 0.03 1 1217 . 254 ALA CA C 53.34 0.50 1 1218 . 254 ALA CB C 18.00 0.50 1 1219 . 254 ALA N N 121.06 0.25 1 1220 . 255 LYS H H 7.60 0.03 1 1221 . 255 LYS CA C 56.92 0.50 1 1222 . 255 LYS CB C 32.03 0.50 1 1223 . 255 LYS CD C 28.45 0.50 1 1224 . 255 LYS CE C 41.63 0.50 1 1225 . 255 LYS CG C 24.13 0.50 1 1226 . 255 LYS N N 117.29 0.25 1 1227 . 256 LEU H H 7.75 0.03 1 1228 . 256 LEU CA C 55.29 0.50 1 1229 . 256 LEU CB C 41.27 0.50 1 1230 . 256 LEU CD1 C 24.42 0.50 2 1231 . 256 LEU CD2 C 22.47 0.50 2 1232 . 256 LEU CG C 26.03 0.50 1 1233 . 256 LEU N N 120.25 0.25 1 1234 . 257 LYS H H 7.86 0.03 1 1235 . 257 LYS CA C 56.33 0.50 1 1236 . 257 LYS CB C 32.35 0.50 1 1237 . 257 LYS CD C 28.30 0.50 1 1238 . 257 LYS CE C 41.65 0.50 1 1239 . 257 LYS CG C 23.75 0.50 1 1240 . 257 LYS N N 119.95 0.25 1 1241 . 258 ASP H H 8.12 0.03 1 1242 . 258 ASP CA C 54.37 0.50 1 1243 . 258 ASP CB C 40.64 0.50 1 1244 . 258 ASP N N 120.53 0.25 1 1245 . 259 ARG HE H 7.12 0.03 2 1246 . 259 ARG H H 7.65 0.03 1 1247 . 259 ARG CA C 57.08 0.50 1 1248 . 259 ARG CB C 30.79 0.50 1 1249 . 259 ARG CD C 43.49 0.50 1 1250 . 259 ARG CG C 27.44 0.50 1 1251 . 259 ARG N N 124.69 0.25 1 1252 . 259 ARG NE N 85.34 0.25 1 stop_ save_ save_chemical_shift_assignment_4 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Sample_label $sample_two stop_ _Sample_conditions_label $sample_cond_1 _Chem_shift_reference_set_label $chemical_shift_reference_one _Mol_system_component_name 'Histidine Phosphocarrier' _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 MET CA C 54.74 0.50 1 2 . 1 MET CB C 32.10 0.50 1 3 . 1 MET CG C 30.80 0.50 1 4 . 2 PHE H H 8.98 0.03 1 5 . 2 PHE CA C 57.22 0.50 1 6 . 2 PHE CB C 42.27 0.50 1 7 . 2 PHE N N 129.03 0.25 1 8 . 3 GLN HE21 H 7.35 0.03 2 9 . 3 GLN HE22 H 6.61 0.03 2 10 . 3 GLN H H 7.62 0.03 1 11 . 3 GLN CA C 53.68 0.50 1 12 . 3 GLN CB C 32.55 0.50 1 13 . 3 GLN N N 122.91 0.25 1 14 . 3 GLN NE2 N 110.63 0.25 1 15 . 4 GLN HE21 H 7.37 0.03 2 16 . 4 GLN HE22 H 6.79 0.03 2 17 . 4 GLN H H 8.52 0.03 1 18 . 4 GLN CA C 55.42 0.50 1 19 . 4 GLN CB C 33.61 0.50 1 20 . 4 GLN CG C 34.25 0.50 1 21 . 4 GLN N N 119.46 0.25 1 22 . 4 GLN NE2 N 109.79 0.25 1 23 . 5 GLU H H 8.22 0.03 1 24 . 5 GLU CA C 54.71 0.50 1 25 . 5 GLU CB C 31.84 0.50 1 26 . 5 GLU CG C 36.40 0.50 1 27 . 5 GLU N N 122.16 0.25 1 28 . 6 VAL H H 9.20 0.03 1 29 . 6 VAL CA C 60.15 0.50 1 30 . 6 VAL CB C 34.44 0.50 1 31 . 6 VAL CG1 C 20.87 0.50 2 32 . 6 VAL CG2 C 19.60 0.50 2 33 . 6 VAL N N 120.92 0.25 1 34 . 7 THR H H 8.09 0.03 1 35 . 7 THR CA C 61.57 0.50 1 36 . 7 THR CB C 69.02 0.50 1 37 . 7 THR CG2 C 20.61 0.50 1 38 . 7 THR N N 121.84 0.25 1 39 . 8 ILE H H 8.63 0.03 1 40 . 8 ILE CA C 61.50 0.50 1 41 . 8 ILE CB C 36.41 0.50 1 42 . 8 ILE CG1 C 26.78 0.50 1 43 . 8 ILE CG2 C 16.63 0.50 1 44 . 8 ILE N N 126.07 0.25 1 45 . 9 THR H H 8.64 0.03 1 46 . 9 THR CA C 61.37 0.50 1 47 . 9 THR CB C 69.22 0.50 1 48 . 9 THR CG2 C 21.02 0.50 1 49 . 9 THR N N 119.93 0.25 1 50 . 10 ALA H H 7.32 0.03 1 51 . 10 ALA CA C 50.65 0.50 1 52 . 10 ALA CB C 17.92 0.50 1 53 . 10 ALA N N 129.32 0.25 1 54 . 11 PRO CA C 64.87 0.50 1 55 . 11 PRO CB C 31.41 0.50 1 56 . 11 PRO CD C 50.35 0.50 1 57 . 11 PRO CG C 27.14 0.50 1 58 . 12 ASN HD21 H 7.30 0.03 2 59 . 12 ASN HD22 H 6.75 0.03 2 60 . 12 ASN H H 8.60 0.03 1 61 . 12 ASN CA C 52.54 0.50 1 62 . 12 ASN CB C 38.19 0.50 1 63 . 12 ASN N N 113.98 0.25 1 64 . 12 ASN ND2 N 112.17 0.25 1 65 . 13 GLY H H 7.88 0.03 1 66 . 13 GLY CA C 45.08 0.50 1 67 . 13 GLY N N 106.13 0.25 1 68 . 14 LEU H H 7.95 0.03 1 69 . 14 LEU CA C 53.31 0.50 1 70 . 14 LEU CB C 40.07 0.50 1 71 . 14 LEU N N 122.44 0.25 1 72 . 15 HIS H H 7.02 0.03 1 73 . 15 HIS CA C 54.76 0.50 1 74 . 15 HIS CB C 29.84 0.50 1 75 . 15 HIS N N 120.70 0.25 1 76 . 16 THR H H 7.80 0.03 1 77 . 16 THR CA C 67.71 0.50 1 78 . 16 THR CB C 68.45 0.50 1 79 . 16 THR CG2 C 21.98 0.50 1 80 . 16 THR N N 112.94 0.25 1 81 . 17 ARG H H 8.67 0.03 1 82 . 17 ARG CA C 61.02 0.50 1 83 . 17 ARG N N 118.78 0.25 1 84 . 18 PRO CA C 64.91 0.50 1 85 . 18 PRO CB C 30.32 0.50 1 86 . 19 ALA H H 8.24 0.03 1 87 . 19 ALA CA C 55.37 0.50 1 88 . 19 ALA CB C 17.34 0.50 1 89 . 19 ALA N N 120.93 0.25 1 90 . 20 ALA H H 8.20 0.03 1 91 . 20 ALA CA C 55.08 0.50 1 92 . 20 ALA CB C 17.44 0.50 1 93 . 20 ALA N N 118.98 0.25 1 94 . 21 GLN HE21 H 7.70 0.03 2 95 . 21 GLN HE22 H 6.78 0.03 2 96 . 21 GLN H H 7.58 0.03 1 97 . 21 GLN CA C 58.50 0.50 1 98 . 21 GLN CB C 27.59 0.50 1 99 . 21 GLN CG C 32.90 0.50 1 100 . 21 GLN N N 117.21 0.25 1 101 . 21 GLN NE2 N 111.00 0.25 1 102 . 22 PHE H H 8.42 0.03 1 103 . 22 PHE CA C 61.75 0.50 1 104 . 22 PHE CB C 38.98 0.50 1 105 . 22 PHE N N 120.88 0.25 1 106 . 23 VAL H H 8.30 0.03 1 107 . 23 VAL CA C 64.92 0.50 1 108 . 23 VAL CB C 31.34 0.50 1 109 . 23 VAL N N 118.82 0.25 1 110 . 24 LYS H H 8.00 0.03 1 111 . 24 LYS CA C 60.06 0.50 1 112 . 24 LYS CB C 31.73 0.50 1 113 . 24 LYS CE C 41.72 0.50 1 114 . 24 LYS CG C 24.65 0.50 1 115 . 24 LYS N N 118.11 0.25 1 116 . 25 GLU H H 8.06 0.03 1 117 . 25 GLU CA C 58.62 0.50 1 118 . 25 GLU CB C 28.35 0.50 1 119 . 25 GLU CG C 36.26 0.50 1 120 . 25 GLU N N 117.15 0.25 1 121 . 26 ALA H H 8.74 0.03 1 122 . 26 ALA CA C 55.26 0.50 1 123 . 26 ALA CB C 18.14 0.50 1 124 . 26 ALA N N 124.16 0.25 1 125 . 27 LYS H H 7.97 0.03 1 126 . 27 LYS CA C 58.55 0.50 1 127 . 27 LYS CB C 32.17 0.50 1 128 . 27 LYS CD C 29.23 0.50 1 129 . 27 LYS CE C 41.42 0.50 1 130 . 27 LYS CG C 25.83 0.50 1 131 . 27 LYS N N 112.22 0.25 1 132 . 28 GLY H H 7.50 0.03 1 133 . 28 GLY CA C 45.00 0.50 1 134 . 28 GLY N N 105.31 0.25 1 135 . 29 PHE H H 7.34 0.03 1 136 . 29 PHE CA C 57.22 0.50 1 137 . 29 PHE CB C 39.75 0.50 1 138 . 29 PHE N N 119.16 0.25 1 139 . 30 THR H H 10.90 0.03 1 140 . 30 THR CA C 63.74 0.50 1 141 . 30 THR CB C 68.95 0.50 1 142 . 30 THR CG2 C 21.50 0.50 1 143 . 30 THR N N 118.41 0.25 1 144 . 31 SER H H 9.04 0.03 1 145 . 31 SER CA C 61.12 0.50 1 146 . 31 SER CB C 65.61 0.50 1 147 . 31 SER N N 119.60 0.25 1 148 . 32 GLU H H 7.83 0.03 1 149 . 32 GLU CA C 55.93 0.50 1 150 . 32 GLU CB C 29.70 0.50 1 151 . 32 GLU CG C 35.51 0.50 1 152 . 32 GLU N N 121.05 0.25 1 153 . 33 ILE H H 9.12 0.03 1 154 . 33 ILE CA C 60.34 0.50 1 155 . 33 ILE CB C 40.88 0.50 1 156 . 33 ILE CG1 C 25.91 0.50 1 157 . 33 ILE CG2 C 17.90 0.50 1 158 . 33 ILE N N 127.92 0.25 1 159 . 34 THR H H 9.64 0.03 1 160 . 34 THR CA C 61.21 0.50 1 161 . 34 THR CB C 71.23 0.50 1 162 . 34 THR CG2 C 21.24 0.50 1 163 . 34 THR N N 124.32 0.25 1 164 . 35 VAL H H 9.29 0.03 1 165 . 35 VAL CA C 60.79 0.50 1 166 . 35 VAL CB C 32.72 0.50 1 167 . 35 VAL CG1 C 20.98 0.50 2 168 . 35 VAL N N 125.60 0.25 1 169 . 36 THR H H 8.89 0.03 1 170 . 36 THR CA C 60.76 0.50 1 171 . 36 THR CB C 70.72 0.50 1 172 . 36 THR CG2 C 20.21 0.50 1 173 . 36 THR N N 121.61 0.25 1 174 . 37 SER H H 9.02 0.03 1 175 . 37 SER CA C 56.80 0.50 1 176 . 37 SER CB C 65.18 0.50 1 177 . 37 SER N N 118.72 0.25 1 178 . 38 ASN HD21 H 7.50 0.03 2 179 . 38 ASN HD22 H 6.91 0.03 2 180 . 38 ASN H H 9.64 0.03 1 181 . 38 ASN CA C 54.16 0.50 1 182 . 38 ASN CB C 37.48 0.50 1 183 . 38 ASN N N 126.67 0.25 1 184 . 38 ASN ND2 N 112.90 0.25 1 185 . 39 GLY H H 8.52 0.03 1 186 . 39 GLY CA C 45.31 0.50 1 187 . 39 GLY N N 102.81 0.25 1 188 . 40 LYS H H 7.89 0.03 1 189 . 40 LYS CA C 54.90 0.50 1 190 . 40 LYS CB C 34.38 0.50 1 191 . 40 LYS CD C 28.59 0.50 1 192 . 40 LYS CE C 41.89 0.50 1 193 . 40 LYS CG C 23.99 0.50 1 194 . 40 LYS N N 122.33 0.25 1 195 . 41 SER H H 8.29 0.03 1 196 . 41 SER CA C 56.94 0.50 1 197 . 41 SER CB C 66.67 0.50 1 198 . 41 SER N N 115.58 0.25 1 199 . 42 ALA H H 9.07 0.03 1 200 . 42 ALA CA C 50.68 0.50 1 201 . 42 ALA CB C 23.03 0.50 1 202 . 42 ALA N N 123.23 0.25 1 203 . 43 SER H H 8.37 0.03 1 204 . 43 SER CA C 56.88 0.50 1 205 . 43 SER CB C 63.86 0.50 1 206 . 43 SER N N 113.97 0.25 1 207 . 44 ALA H H 8.39 0.03 1 208 . 44 ALA CA C 52.67 0.50 1 209 . 44 ALA CB C 19.59 0.50 1 210 . 44 ALA N N 126.64 0.25 1 211 . 45 LYS H H 7.59 0.03 1 212 . 45 LYS CA C 55.60 0.50 1 213 . 45 LYS CB C 32.49 0.50 1 214 . 45 LYS CG C 26.12 0.50 1 215 . 45 LYS N N 107.43 0.25 1 216 . 46 SER H H 7.23 0.03 1 217 . 46 SER CA C 54.62 0.50 1 218 . 46 SER CB C 64.33 0.50 1 219 . 46 SER N N 113.17 0.25 1 220 . 47 LEU H H 8.83 0.03 1 221 . 47 LEU CA C 57.65 0.50 1 222 . 47 LEU CB C 41.85 0.50 1 223 . 47 LEU CD1 C 26.14 0.50 2 224 . 47 LEU N N 130.44 0.25 1 225 . 48 PHE H H 8.15 0.03 1 226 . 48 PHE CA C 60.50 0.50 1 227 . 48 PHE CB C 39.46 0.50 1 228 . 48 PHE N N 115.65 0.25 1 229 . 49 LYS H H 8.17 0.03 1 230 . 49 LYS CA C 56.34 0.50 1 231 . 49 LYS CB C 31.13 0.50 1 232 . 49 LYS CG C 23.72 0.50 1 233 . 49 LYS N N 114.95 0.25 1 234 . 50 LEU H H 8.70 0.03 1 235 . 50 LEU CA C 58.05 0.50 1 236 . 50 LEU CB C 41.53 0.50 1 237 . 50 LEU CD1 C 25.36 0.50 2 238 . 50 LEU CD2 C 23.93 0.50 2 239 . 50 LEU N N 122.30 0.25 1 240 . 51 GLN H H 7.63 0.03 1 241 . 51 GLN CA C 57.78 0.50 1 242 . 51 GLN CB C 28.10 0.50 1 243 . 51 GLN CG C 33.65 0.50 1 244 . 51 GLN N N 112.00 0.25 1 245 . 52 THR H H 7.24 0.03 1 246 . 52 THR CA C 62.61 0.50 1 247 . 52 THR CB C 69.12 0.50 1 248 . 52 THR CG2 C 21.40 0.50 1 249 . 52 THR N N 106.29 0.25 1 250 . 53 LEU H H 7.33 0.03 1 251 . 53 LEU CA C 54.93 0.50 1 252 . 53 LEU CB C 41.61 0.50 1 253 . 53 LEU CD2 C 22.56 0.50 2 254 . 53 LEU CG C 26.34 0.50 1 255 . 53 LEU N N 119.31 0.25 1 256 . 54 GLY H H 8.10 0.03 1 257 . 54 GLY CA C 46.81 0.50 1 258 . 54 GLY N N 107.17 0.25 1 259 . 55 LEU H H 8.11 0.03 1 260 . 55 LEU CA C 53.61 0.50 1 261 . 55 LEU CB C 39.75 0.50 1 262 . 55 LEU CG C 25.12 0.50 2 263 . 55 LEU CD2 C 22.86 0.50 2 264 . 55 LEU N N 123.97 0.25 1 265 . 56 THR H H 7.24 0.03 1 266 . 56 THR CA C 60.14 0.50 1 267 . 56 THR CB C 70.46 0.50 1 268 . 56 THR CG2 C 21.43 0.50 1 269 . 56 THR N N 110.81 0.25 1 270 . 57 GLN HE21 H 7.20 0.03 2 271 . 57 GLN HE22 H 6.85 0.03 2 272 . 57 GLN H H 8.72 0.03 1 273 . 57 GLN CA C 58.30 0.50 1 274 . 57 GLN CB C 27.48 0.50 1 275 . 57 GLN CG C 33.39 0.50 1 276 . 57 GLN N N 121.57 0.25 1 277 . 57 GLN NE2 N 110.64 0.25 1 278 . 58 GLY H H 9.17 0.03 1 279 . 58 GLY CA C 44.50 0.50 1 280 . 58 GLY N N 115.20 0.25 1 281 . 59 THR H H 7.82 0.03 1 282 . 59 THR CA C 63.99 0.50 1 283 . 59 THR CB C 69.15 0.50 1 284 . 59 THR CG2 C 21.75 0.50 1 285 . 59 THR N N 117.77 0.25 1 286 . 60 VAL H H 8.47 0.03 1 287 . 60 VAL CA C 62.05 0.50 1 288 . 60 VAL CB C 31.32 0.50 1 289 . 60 VAL CG1 C 20.53 0.50 2 290 . 60 VAL N N 127.07 0.25 1 291 . 61 VAL H H 9.24 0.03 1 292 . 61 VAL CA C 58.99 0.50 1 293 . 61 VAL CB C 33.64 0.50 1 294 . 61 VAL CG1 C 22.13 0.50 2 295 . 61 VAL CG2 C 20.40 0.50 2 296 . 61 VAL N N 125.84 0.25 1 297 . 62 THR H H 8.80 0.03 1 298 . 62 THR CA C 61.99 0.50 1 299 . 62 THR CB C 69.66 0.50 1 300 . 62 THR CG2 C 21.15 0.50 1 301 . 62 THR N N 118.12 0.25 1 302 . 63 ILE H H 8.96 0.03 1 303 . 63 ILE CA C 60.38 0.50 1 304 . 63 ILE CB C 37.66 0.50 1 305 . 63 ILE N N 128.81 0.25 1 306 . 64 SER H H 9.00 0.03 1 307 . 64 SER CA C 55.76 0.50 1 308 . 64 SER CB C 66.02 0.50 1 309 . 64 SER N N 120.74 0.25 1 310 . 65 ALA H H 9.11 0.03 1 311 . 65 ALA CA C 50.10 0.50 1 312 . 65 ALA CB C 24.59 0.50 1 313 . 65 ALA N N 123.70 0.25 1 314 . 66 GLU H H 8.33 0.03 1 315 . 66 GLU CA C 54.13 0.50 1 316 . 66 GLU CB C 32.77 0.50 1 317 . 66 GLU CG C 36.19 0.50 1 318 . 66 GLU N N 118.78 0.25 1 319 . 67 GLY H H 10.06 0.03 1 320 . 67 GLY CA C 44.99 0.50 1 321 . 67 GLY N N 117.98 0.25 1 322 . 68 GLU H H 8.92 0.03 1 323 . 68 GLU CA C 59.10 0.50 1 324 . 68 GLU CB C 29.34 0.50 1 325 . 68 GLU CG C 35.54 0.50 1 326 . 68 GLU N N 118.33 0.25 1 327 . 69 ASP H H 7.21 0.03 1 328 . 69 ASP CA C 50.95 0.50 1 329 . 69 ASP CB C 39.48 0.50 1 330 . 69 ASP N N 113.71 0.25 1 331 . 70 GLU H H 6.85 0.03 1 332 . 70 GLU CA C 59.22 0.50 1 333 . 70 GLU CB C 27.21 0.50 1 334 . 70 GLU CG C 33.94 0.50 1 335 . 70 GLU N N 116.05 0.25 1 336 . 71 GLN HE21 H 7.38 0.03 2 337 . 71 GLN HE22 H 6.47 0.03 2 338 . 71 GLN H H 7.67 0.03 1 339 . 71 GLN CA C 58.52 0.50 1 340 . 71 GLN CB C 26.34 0.50 1 341 . 71 GLN CG C 31.91 0.50 1 342 . 71 GLN N N 118.97 0.25 1 343 . 71 GLN NE2 N 110.31 0.25 1 344 . 72 LYS H H 7.37 0.03 1 345 . 72 LYS CA C 58.31 0.50 1 346 . 72 LYS CB C 31.69 0.50 1 347 . 72 LYS CD C 28.68 0.50 1 348 . 72 LYS CE C 41.63 0.50 1 349 . 72 LYS CG C 24.27 0.50 1 350 . 72 LYS N N 118.40 0.25 1 351 . 73 ALA H H 8.24 0.03 1 352 . 73 ALA CA C 53.64 0.50 1 353 . 73 ALA CB C 17.80 0.50 1 354 . 73 ALA N N 120.23 0.25 1 355 . 74 VAL H H 7.19 0.03 1 356 . 74 VAL CA C 66.95 0.50 1 357 . 74 VAL CB C 31.32 0.50 1 358 . 74 VAL CG1 C 22.12 0.50 2 359 . 74 VAL N N 115.12 0.25 1 360 . 75 GLU H H 8.17 0.03 1 361 . 75 GLU CA C 59.88 0.50 1 362 . 75 GLU CB C 28.88 0.50 1 363 . 75 GLU CG C 36.65 0.50 1 364 . 75 GLU N N 116.02 0.25 1 365 . 76 HIS H H 8.18 0.03 1 366 . 76 HIS CA C 59.71 0.50 1 367 . 76 HIS CB C 31.54 0.50 1 368 . 76 HIS N N 117.54 0.25 1 369 . 77 LEU H H 7.94 0.03 1 370 . 77 LEU CA C 57.39 0.50 1 371 . 77 LEU CB C 39.97 0.50 1 372 . 77 LEU CD1 C 19.79 0.50 2 373 . 77 LEU CD2 C 25.78 0.50 2 374 . 77 LEU N N 118.30 0.25 1 375 . 78 VAL H H 8.90 0.03 1 376 . 78 VAL CA C 66.53 0.50 1 377 . 78 VAL CB C 30.85 0.50 1 378 . 78 VAL CG1 C 22.66 0.50 2 379 . 78 VAL N N 119.00 0.25 1 380 . 79 LYS H H 7.18 0.03 1 381 . 79 LYS CA C 59.22 0.50 1 382 . 79 LYS CB C 31.29 0.50 1 383 . 79 LYS CD C 28.64 0.50 1 384 . 79 LYS CE C 41.58 0.50 1 385 . 79 LYS CG C 24.09 0.50 1 386 . 79 LYS N N 119.93 0.25 1 387 . 80 LEU H H 7.62 0.03 1 388 . 80 LEU CA C 57.49 0.50 1 389 . 80 LEU CB C 41.37 0.50 1 390 . 80 LEU CG C 26.16 0.50 1 391 . 80 LEU N N 117.63 0.25 1 392 . 81 MET H H 8.00 0.03 1 393 . 81 MET CA C 58.19 0.50 1 394 . 81 MET CB C 32.53 0.50 1 395 . 81 MET CG C 33.19 0.50 1 396 . 81 MET N N 115.69 0.25 1 397 . 82 ALA H H 7.90 0.03 1 398 . 82 ALA CA C 53.53 0.50 1 399 . 82 ALA N N 118.54 0.25 1 400 . 83 GLU H H 7.71 0.03 1 401 . 83 GLU CA C 55.76 0.50 1 402 . 83 GLU CB C 29.77 0.50 1 403 . 83 GLU CG C 35.81 0.50 1 404 . 83 GLU N N 115.80 0.25 1 405 . 84 LEU H H 7.19 0.03 1 406 . 84 LEU CA C 55.74 0.50 1 407 . 84 LEU CB C 42.13 0.50 1 408 . 84 LEU CD1 C 22.79 0.50 2 409 . 84 LEU CG C 25.21 0.50 1 410 . 84 LEU N N 121.15 0.25 1 411 . 85 GLU H H 7.76 0.03 1 412 . 85 GLU CA C 57.41 0.50 1 413 . 85 GLU CB C 31.83 0.50 1 414 . 85 GLU N N 125.25 0.25 1 stop_ save_