data_5930 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Backbone 1H, 15N, 13C Resonance Assignment of a-ADT ; _BMRB_accession_number 5930 _BMRB_flat_file_name bmr5930.str _Entry_type original _Submission_date 2003-09-02 _Accession_date 2003-09-02 _Entry_origination author _NMR_STAR_version 2.1.1 _Experimental_method NMR _Details . loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 John Michael . . 2 Heller Markus . . 3 Coles Murray . . 4 Bosch Gundula . . 5 Baumeister Wolfgang . . 6 Kessler Horst . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 299 "13C chemical shifts" 290 "15N chemical shifts" 145 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2004-04-07 original author . stop_ loop_ _Related_BMRB_accession_number _Relationship 5936 'chmeical shifts of b-ADT' stop_ _Original_release_date 2004-04-07 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; Letter to the Editor: Backbone 1H, 15N and 13C resonance assignments of [agr]-ADT and [bgr]-ADT ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 15014236 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 John Michael . . 2 Heller Markus . . 3 Coles Murray . . 4 Bosch Gundula . . 5 Baumeister Wolfgang . . 6 Kessler Horst . . stop_ _Journal_abbreviation 'J. Biomol. NMR' _Journal_volume 29 _Journal_issue 2 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 209 _Page_last 210 _Year 2004 _Details . save_ ####################################### # Cited references within the entry # ####################################### save_citation_Wishart(1995) _Saveframe_category citation _Citation_full 'J. Biomol. NMR, 6 (1995) 135-140.' _Citation_title '1H, 13C and 15N chemical shift referencing in biomolecular NMR.' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 8589602 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Wishart 'D S' S. . 2 Bigam 'C G' G. . 3 Yao J . . 4 Abildgaard F . . 5 Dyson 'H J' J. . 6 Oldfield E . . 7 Markley 'J L' L. . 8 Sykes 'B D' D. . stop_ _Journal_abbreviation 'J. Biomol. NMR' _Journal_name_full 'Journal of biomolecular NMR' _Journal_volume 6 _Journal_issue 2 _Journal_CSD . _Book_title . _Book_chapter_title . _Book_volume . _Book_series . _Book_publisher . _Book_publisher_city . _Book_ISBN . _Conference_title . _Conference_site . _Conference_state_province . _Conference_country . _Conference_start_date . _Conference_end_date . _Conference_abstract_number . _Thesis_institution . _Thesis_institution_city . _Thesis_institution_country . _Page_first 135 _Page_last 140 _Year 1995 _Details ; A considerable degree of variability exists in the way that 1H, 13C and 15N chemical shifts are reported and referenced for biomolecules. In this article we explore some of the reasons for this situation and propose guidelines for future chemical shift referencing and for conversion from many common 1H, 13C and 15N chemical shift standards, now used in biomolecular NMR, to those proposed here. ; save_ ################################## # Molecular system description # ################################## save_system_aADT _Saveframe_category molecular_system _Mol_system_name aADT _Abbreviation_common aADT _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label aADT $aADT stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state monomer _System_paramagnetic no _System_thiol_state 'all free' loop_ _Biological_function chaperonin stop_ _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_aADT _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'apical domain of the Thermosome' _Abbreviation_common aADT _Molecular_mass . _Mol_thiol_state 'all free' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 159 _Mol_residue_sequence ; MSGIVIDKEKVHSKMPDVVK NAKIALIDSALEIKKTEIEA KVQISDPSKIQDFLNQETNT FKQMVEKIKKSGANVVLCQK GIDDVAQHYLAKEGIYAVRR VKKSDMEKLAKATGAKIVTD LDDLTPSVLGEAETVEERKI GDDRMTFVMGCKNHHHHHH ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 213 MET 2 214 SER 3 215 GLY 4 216 ILE 5 217 VAL 6 218 ILE 7 219 ASP 8 220 LYS 9 221 GLU 10 222 LYS 11 223 VAL 12 224 HIS 13 225 SER 14 226 LYS 15 227 MET 16 228 PRO 17 229 ASP 18 230 VAL 19 231 VAL 20 232 LYS 21 233 ASN 22 234 ALA 23 235 LYS 24 236 ILE 25 237 ALA 26 238 LEU 27 239 ILE 28 240 ASP 29 241 SER 30 242 ALA 31 243 LEU 32 244 GLU 33 245 ILE 34 246 LYS 35 247 LYS 36 248 THR 37 249 GLU 38 250 ILE 39 251 GLU 40 252 ALA 41 253 LYS 42 254 VAL 43 255 GLN 44 256 ILE 45 257 SER 46 258 ASP 47 259 PRO 48 260 SER 49 261 LYS 50 262 ILE 51 263 GLN 52 264 ASP 53 265 PHE 54 266 LEU 55 267 ASN 56 268 GLN 57 269 GLU 58 270 THR 59 271 ASN 60 272 THR 61 273 PHE 62 274 LYS 63 275 GLN 64 276 MET 65 277 VAL 66 278 GLU 67 279 LYS 68 280 ILE 69 281 LYS 70 282 LYS 71 283 SER 72 284 GLY 73 285 ALA 74 286 ASN 75 287 VAL 76 288 VAL 77 289 LEU 78 290 CYS 79 291 GLN 80 292 LYS 81 293 GLY 82 294 ILE 83 295 ASP 84 296 ASP 85 297 VAL 86 298 ALA 87 299 GLN 88 300 HIS 89 301 TYR 90 302 LEU 91 303 ALA 92 304 LYS 93 305 GLU 94 306 GLY 95 307 ILE 96 308 TYR 97 309 ALA 98 310 VAL 99 311 ARG 100 312 ARG 101 313 VAL 102 314 LYS 103 315 LYS 104 316 SER 105 317 ASP 106 318 MET 107 319 GLU 108 320 LYS 109 321 LEU 110 322 ALA 111 323 LYS 112 324 ALA 113 325 THR 114 326 GLY 115 327 ALA 116 328 LYS 117 329 ILE 118 330 VAL 119 331 THR 120 332 ASP 121 333 LEU 122 334 ASP 123 335 ASP 124 336 LEU 125 337 THR 126 338 PRO 127 339 SER 128 340 VAL 129 341 LEU 130 342 GLY 131 343 GLU 132 344 ALA 133 345 GLU 134 346 THR 135 347 VAL 136 348 GLU 137 349 GLU 138 350 ARG 139 351 LYS 140 352 ILE 141 353 GLY 142 354 ASP 143 355 ASP 144 356 ARG 145 357 MET 146 358 THR 147 359 PHE 148 360 VAL 149 361 MET 150 362 GLY 151 363 CYS 152 364 LYS 153 365 ASN 154 1 HIS 155 2 HIS 156 3 HIS 157 4 HIS 158 5 HIS 159 6 HIS stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2014-10-26 loop_ _Database_name _Database_accession_code _Database_entry_mol_name _Sequence_query_to_submitted_percentage _Sequence_subject_length _Sequence_identity _Sequence_positive _Sequence_homology_expectation_value PDB 1A6D "Thermosome From T. Acidophilum" 96.23 545 99.35 100.00 2.07e-99 PDB 1A6E "Thermosome-Mg-Adp-Alf3 Complex" 96.23 545 99.35 100.00 2.07e-99 PDB 1ASS "Apical Domain Of The Chaperonin From Thermoplasma Acidophilum" 100.00 159 100.00 100.00 5.45e-110 PDB 1ASX "Apical Domain Of The Chaperonin From Thermoplasma Acidophilum" 100.00 159 100.00 100.00 5.45e-110 EMBL CAA86610 "thermosome alpha-subunit [Thermoplasma acidophilum]" 96.23 545 99.35 100.00 2.98e-99 EMBL CAC12109 "thermosome, alpha chain [Thermoplasma acidophilum]" 96.23 549 99.35 100.00 2.85e-99 REF NP_394440 "thermosome, alpha chain [Thermoplasma acidophilum DSM 1728]" 96.23 549 99.35 100.00 2.85e-99 REF WP_010901391 "thermosome subunit [Thermoplasma acidophilum]" 96.23 549 99.35 100.00 2.85e-99 SP P48424 "RecName: Full=Thermosome subunit alpha; AltName: Full=Chaperonin subunit alpha; AltName: Full=Thermosome subunit 1 [Thermoplasm" 96.23 545 99.35 100.00 2.98e-99 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $aADT 'Thermoplasma acidophilum' 2303 Archaea . Thermoplasma acidophilum 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 $aADT 'recombinant technology' . . . . . stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_15N _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Concentration_min_value _Concentration_max_value _Isotopic_labeling $aADT . mM 0.7 1.0 [U-15N] 'Na Phosphate' 25 mM . . . NaCl 100 mM . . . stop_ save_ save_sample_CN _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Concentration_min_value _Concentration_max_value _Isotopic_labeling $aADT . mM 0.7 1.0 '[U-13C; U-15N]' 'Na Phosphate' 25 mM . . . NaCl 100 mM . . . stop_ save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model DMX _Field_strength 750 _Details . save_ save_NMR_spectrometer_2 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model DMX _Field_strength 600 _Details . save_ ####################### # Sample conditions # ####################### save_general_condition _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 5.5 0.2 n/a temperature 315 0.2 K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference _Saveframe_category chemical_shift_reference _Details . loop_ _Mol_common_name _Atom_type _Atom_isotope_number _Atom_group _Chem_shift_units _Chem_shift_value _Reference_method _Reference_type _External_reference_sample_geometry _External_reference_location _External_reference_axis _Indirect_shift_ratio DSS H 1 'methyl protons' ppm 0.00 internal direct . . . 1.0 DSS N 15 'methyl protons' ppm 0.00 . indirect . . . 0.101329118 DSS C 13 'methyl protons' ppm 0.00 . indirect . . . 0.251449530 stop_ save_ ################################### # Assigned chemical shift lists # ################################### ################################################################### # Chemical Shift Ambiguity Index Value Definitions # # # # The values other than 1 are used for those atoms with different # # chemical shifts that cannot be assigned to stereospecific atoms # # or to specific residues or chains. # # # # Index Value Definition # # # # 1 Unique (including isolated methyl protons, # # geminal atoms, and geminal methyl # # groups with identical chemical shifts) # # (e.g. ILE HD11, HD12, HD13 protons) # # 2 Ambiguity of geminal atoms or geminal methyl # # proton groups (e.g. ASP HB2 and HB3 # # protons, LEU CD1 and CD2 carbons, or # # LEU HD11, HD12, HD13 and HD21, HD22, # # HD23 methyl protons) # # 3 Aromatic atoms on opposite sides of # # symmetrical rings (e.g. TYR HE1 and HE2 # # protons) # # 4 Intraresidue ambiguities (e.g. LYS HG and # # HD protons or TRP HZ2 and HZ3 protons) # # 5 Interresidue ambiguities (LYS 12 vs. LYS 27) # # 6 Intermolecular ambiguities (e.g. ASP 31 CA # # in monomer 1 and ASP 31 CA in monomer 2 # # of an asymmetrical homodimer, duplex # # DNA assignments, or other assignments # # that may apply to atoms in one or more # # molecule in the molecular assembly) # # 9 Ambiguous, specific ambiguity not defined # # # ################################################################### save_aADT_bb _Saveframe_category assigned_chemical_shifts _Details . loop_ _Sample_label $sample_15N $sample_CN stop_ _Sample_conditions_label $general_condition _Chem_shift_reference_set_label $chemical_shift_reference _Mol_system_component_name aADT _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 . 3 GLY C C 172.4 0.1 1 2 . 3 GLY CA C 45.5 0.1 1 3 . 4 ILE H H 8.77 0.01 1 4 . 4 ILE HA H 4.31 0.01 1 5 . 4 ILE C C 173.5 0.1 1 6 . 4 ILE CA C 60.2 0.1 1 7 . 4 ILE N N 121.8 0.1 1 8 . 5 VAL H H 8.18 0.01 1 9 . 5 VAL HA H 4.28 0.01 1 10 . 5 VAL C C 175.1 0.1 1 11 . 5 VAL CA C 61 0.1 1 12 . 5 VAL N N 126.7 0.1 1 13 . 6 ILE H H 9.22 0.01 1 14 . 6 ILE HA H 4.39 0.01 1 15 . 6 ILE C C 176 0.1 1 16 . 6 ILE CA C 58.6 0.1 1 17 . 6 ILE N N 127.8 0.1 1 18 . 7 ASP H H 8.94 0.01 1 19 . 7 ASP HA H 4.63 0.01 1 20 . 7 ASP CA C 54 0.1 1 21 . 7 ASP N N 131.4 0.1 1 22 . 8 LYS H H 8.19 0.01 1 23 . 8 LYS HA H 4.67 0.01 1 24 . 8 LYS C C 174.1 0.1 1 25 . 8 LYS CA C 54 0.1 1 26 . 8 LYS N N 120.8 0.1 1 27 . 9 GLU H H 8.94 0.01 1 28 . 9 GLU HA H 4.24 0.01 1 29 . 9 GLU C C 174.9 0.1 1 30 . 9 GLU CA C 54.2 0.1 1 31 . 9 GLU N N 123.1 0.1 1 32 . 10 LYS H H 8.57 0.01 1 33 . 10 LYS HA H 4 0.01 1 34 . 10 LYS C C 178.8 0.1 1 35 . 10 LYS CA C 56 0.1 1 36 . 10 LYS N N 122 0.1 1 37 . 11 VAL H H 8.25 0.01 1 38 . 11 VAL HA H 3.93 0.01 1 39 . 11 VAL C C 173.1 0.1 1 40 . 11 VAL CA C 64.2 0.1 1 41 . 11 VAL N N 119.4 0.1 1 42 . 12 HIS H H 7.46 0.01 1 43 . 12 HIS HA H 4.88 0.01 1 44 . 12 HIS C C 176.2 0.1 1 45 . 12 HIS CA C 55.9 0.1 1 46 . 12 HIS N N 120.9 0.1 1 47 . 13 SER H H 8.31 0.01 1 48 . 13 SER HA H 4.09 0.01 1 49 . 13 SER C C 175.7 0.1 1 50 . 13 SER CA C 61.4 0.1 1 51 . 13 SER N N 123.4 0.1 1 52 . 14 LYS H H 10.53 0.01 1 53 . 14 LYS HA H 4.52 0.01 1 54 . 14 LYS C C 178.2 0.1 1 55 . 14 LYS CA C 55.7 0.1 1 56 . 14 LYS N N 122.4 0.1 1 57 . 15 MET H H 7.74 0.01 1 58 . 15 MET HA H 4.22 0.01 1 59 . 15 MET CA C 56.1 0.1 1 60 . 15 MET N N 119.8 0.1 1 61 . 16 PRO HA H 4.47 0.01 1 62 . 16 PRO C C 174.4 0.1 1 63 . 16 PRO CA C 63 0.1 1 64 . 17 ASP H H 8.17 0.01 1 65 . 17 ASP HA H 4.69 0.01 1 66 . 17 ASP C C 175.5 0.1 1 67 . 17 ASP CA C 55.9 0.1 1 68 . 17 ASP N N 115.7 0.1 1 69 . 18 VAL H H 7.37 0.01 1 70 . 18 VAL HA H 4.78 0.01 1 71 . 18 VAL C C 174.3 0.1 1 72 . 18 VAL CA C 60.6 0.1 1 73 . 18 VAL N N 114.8 0.1 1 74 . 19 VAL H H 9.42 0.01 1 75 . 19 VAL HA H 4.13 0.01 1 76 . 19 VAL C C 174.8 0.1 1 77 . 19 VAL CA C 61.9 0.1 1 78 . 19 VAL N N 128.2 0.1 1 79 . 20 LYS H H 8.35 0.01 1 80 . 20 LYS HA H 4.88 0.01 1 81 . 20 LYS C C 176.9 0.1 1 82 . 20 LYS CA C 54.4 0.1 1 83 . 20 LYS N N 126.5 0.1 1 84 . 21 ASN H H 8.94 0.01 1 85 . 21 ASN HA H 4.27 0.01 1 86 . 21 ASN C C 174.6 0.1 1 87 . 21 ASN CA C 54.8 0.1 1 88 . 21 ASN N N 120.2 0.1 1 89 . 22 ALA H H 7.63 0.01 1 90 . 22 ALA HA H 4.38 0.01 1 91 . 22 ALA C C 177 0.1 1 92 . 22 ALA CA C 52.1 0.1 1 93 . 22 ALA N N 122.1 0.1 1 94 . 23 LYS H H 9.49 0.01 1 95 . 23 LYS HA H 5.08 0.01 1 96 . 23 LYS C C 175.8 0.1 1 97 . 23 LYS CA C 54.7 0.1 1 98 . 23 LYS N N 126.2 0.1 1 99 . 24 ILE H H 9.07 0.01 1 100 . 24 ILE HA H 4.42 0.01 1 101 . 24 ILE C C 174.2 0.1 1 102 . 24 ILE CA C 61.4 0.1 1 103 . 24 ILE N N 123.2 0.1 1 104 . 25 ALA H H 9.11 0.01 1 105 . 25 ALA HA H 4.8 0.01 1 106 . 25 ALA C C 174.9 0.1 1 107 . 25 ALA CA C 49.9 0.1 1 108 . 25 ALA N N 129.9 0.1 1 109 . 26 LEU H H 9.34 0.01 1 110 . 26 LEU HA H 4.98 0.01 1 111 . 26 LEU C C 174.3 0.1 1 112 . 26 LEU CA C 53.3 0.1 1 113 . 26 LEU N N 125 0.1 1 114 . 27 ILE H H 8.27 0.01 1 115 . 27 ILE HA H 4.98 0.01 1 116 . 27 ILE C C 175.3 0.1 1 117 . 27 ILE CA C 59.1 0.1 1 118 . 27 ILE N N 121.1 0.1 1 119 . 28 ASP H H 9.11 0.01 1 120 . 28 ASP HA H 4.82 0.01 1 121 . 28 ASP C C 174.7 0.1 1 122 . 28 ASP CA C 52.8 0.1 1 123 . 28 ASP N N 127.6 0.1 1 124 . 29 SER H H 6.94 0.01 1 125 . 29 SER HA H 4.42 0.01 1 126 . 29 SER C C 172 0.1 1 127 . 29 SER CA C 56.6 0.1 1 128 . 29 SER N N 111.8 0.1 1 129 . 30 ALA H H 8.26 0.01 1 130 . 30 ALA HA H 4.41 0.01 1 131 . 30 ALA C C 178.8 0.1 1 132 . 30 ALA CA C 52.1 0.1 1 133 . 30 ALA N N 121.7 0.1 1 134 . 31 LEU H H 8.47 0.01 1 135 . 31 LEU HA H 4.78 0.01 1 136 . 31 LEU C C 174.3 0.1 1 137 . 31 LEU CA C 53.2 0.1 1 138 . 31 LEU N N 127.1 0.1 1 139 . 32 GLU H H 7.25 0.01 1 140 . 32 GLU HA H 4.74 0.01 1 141 . 32 GLU C C 174.6 0.1 1 142 . 32 GLU CA C 54.3 0.1 1 143 . 32 GLU N N 117.6 0.1 1 144 . 33 ILE H H 8.77 0.01 1 145 . 33 ILE HA H 4.16 0.01 1 146 . 33 ILE C C 175.6 0.1 1 147 . 33 ILE CA C 60.6 0.1 1 148 . 33 ILE N N 121 0.1 1 149 . 34 LYS H H 8.38 0.01 1 150 . 34 LYS HA H 4.36 0.01 1 151 . 34 LYS C C 176.5 0.1 1 152 . 34 LYS CA C 56.1 0.1 1 153 . 34 LYS N N 126.3 0.1 1 154 . 35 LYS H H 8.41 0.01 1 155 . 35 LYS HA H 4.36 0.01 1 156 . 35 LYS C C 176.9 0.1 1 157 . 35 LYS CA C 56.8 0.1 1 158 . 35 LYS N N 124.4 0.1 1 159 . 36 THR H H 8.12 0.01 1 160 . 36 THR HA H 4.29 0.01 1 161 . 36 THR C C 175 0.1 1 162 . 36 THR CA C 62.3 0.1 1 163 . 36 THR N N 113.9 0.1 1 164 . 37 GLU H H 8.28 0.01 1 165 . 37 GLU HA H 4.31 0.01 1 166 . 37 GLU C C 176.9 0.1 1 167 . 37 GLU CA C 57.2 0.1 1 168 . 37 GLU N N 122.3 0.1 1 169 . 38 ILE H H 7.83 0.01 1 170 . 38 ILE HA H 4.05 0.01 1 171 . 38 ILE C C 176.6 0.1 1 172 . 38 ILE CA C 62 0.1 1 173 . 38 ILE N N 120.1 0.1 1 174 . 39 GLU H H 8.16 0.01 1 175 . 39 GLU HA H 4.21 0.01 1 176 . 39 GLU C C 176.6 0.1 1 177 . 39 GLU CA C 57.3 0.1 1 178 . 39 GLU N N 122.9 0.1 1 179 . 40 ALA H H 7.98 0.01 1 180 . 40 ALA HA H 4.25 0.01 1 181 . 40 ALA C C 178 0.1 1 182 . 40 ALA CA C 53.1 0.1 1 183 . 40 ALA N N 123.3 0.1 1 184 . 41 LYS H H 7.96 0.01 1 185 . 41 LYS HA H 4.25 0.01 1 186 . 41 LYS C C 176.9 0.1 1 187 . 41 LYS CA C 56.8 0.1 1 188 . 41 LYS N N 118.7 0.1 1 189 . 42 VAL H H 7.8 0.01 1 190 . 42 VAL HA H 4.05 0.01 1 191 . 42 VAL C C 176 0.1 1 192 . 42 VAL CA C 62.6 0.1 1 193 . 42 VAL N N 119.4 0.1 1 194 . 43 GLN H H 8.14 0.01 1 195 . 43 GLN HA H 4.34 0.01 1 196 . 43 GLN C C 175.8 0.1 1 197 . 43 GLN CA C 56 0.1 1 198 . 43 GLN N N 122.7 0.1 1 199 . 44 ILE H H 7.91 0.01 1 200 . 44 ILE HA H 4.18 0.01 1 201 . 44 ILE C C 175.9 0.1 1 202 . 44 ILE CA C 61.1 0.1 1 203 . 44 ILE N N 120.9 0.1 1 204 . 45 SER H H 8.19 0.01 1 205 . 45 SER HA H 4.42 0.01 1 206 . 45 SER C C 173.7 0.1 1 207 . 45 SER CA C 58.6 0.1 1 208 . 45 SER N N 118.8 0.1 1 209 . 46 ASP H H 7.82 0.01 1 210 . 46 ASP HA H 4.98 0.01 1 211 . 46 ASP CA C 51.6 0.1 1 212 . 46 ASP N N 122.3 0.1 1 213 . 47 PRO HA H 4.35 0.01 1 214 . 47 PRO C C 178 0.1 1 215 . 47 PRO CA C 64.4 0.1 1 216 . 48 SER H H 8.42 0.01 1 217 . 48 SER HA H 4.36 0.01 1 218 . 48 SER C C 175.6 0.1 1 219 . 48 SER CA C 60.4 0.1 1 220 . 48 SER N N 114.6 0.1 1 221 . 49 LYS H H 7.75 0.01 1 222 . 49 LYS HA H 4.4 0.01 1 223 . 49 LYS C C 177.4 0.1 1 224 . 49 LYS CA C 56.4 0.1 1 225 . 49 LYS N N 121.9 0.1 1 226 . 50 ILE H H 7.65 0.01 1 227 . 50 ILE HA H 4 0.01 1 228 . 50 ILE C C 176.9 0.1 1 229 . 50 ILE CA C 63 0.1 1 230 . 50 ILE N N 120.2 0.1 1 231 . 51 GLN H H 8.12 0.01 1 232 . 51 GLN HA H 4.13 0.01 1 233 . 51 GLN C C 176.8 0.1 1 234 . 51 GLN CA C 57.5 0.1 1 235 . 51 GLN N N 121.2 0.1 1 236 . 52 ASP H H 7.97 0.01 1 237 . 52 ASP HA H 4.5 0.01 1 238 . 52 ASP C C 177.6 0.1 1 239 . 52 ASP CA C 56 0.1 1 240 . 52 ASP N N 120 0.1 1 241 . 53 PHE H H 7.92 0.01 1 242 . 53 PHE HA H 4.37 0.01 1 243 . 53 PHE C C 177.2 0.1 1 244 . 53 PHE CA C 59.7 0.1 1 245 . 53 PHE N N 120.1 0.1 1 246 . 54 LEU H H 8.17 0.01 1 247 . 54 LEU HA H 4.18 0.01 1 248 . 54 LEU C C 178.8 0.1 1 249 . 54 LEU CA C 56.8 0.1 1 250 . 54 LEU N N 120.9 0.1 1 251 . 55 ASN H H 8.26 0.01 1 252 . 55 ASN HA H 4.62 0.01 1 253 . 55 ASN C C 176.5 0.1 1 254 . 55 ASN CA C 54.5 0.1 1 255 . 55 ASN N N 118.7 0.1 1 256 . 56 GLN H H 8.06 0.01 1 257 . 56 GLN HA H 4.25 0.01 1 258 . 56 GLN C C 177.8 0.1 1 259 . 56 GLN CA C 57.8 0.1 1 260 . 56 GLN N N 120.1 0.1 1 261 . 57 GLU H H 8.41 0.01 1 262 . 57 GLU HA H 4.04 0.01 1 263 . 57 GLU C C 177.6 0.1 1 264 . 57 GLU CA C 58.9 0.1 1 265 . 57 GLU N N 121.3 0.1 1 266 . 58 THR H H 8.18 0.01 1 267 . 58 THR HA H 4.21 0.01 1 268 . 58 THR C C 175.6 0.1 1 269 . 58 THR CA C 65.3 0.1 1 270 . 58 THR N N 114 0.1 1 271 . 59 ASN H H 8.14 0.01 1 272 . 59 ASN HA H 4.52 0.01 1 273 . 59 ASN C C 177 0.1 1 274 . 59 ASN CA C 55.6 0.1 1 275 . 59 ASN N N 119.8 0.1 1 276 . 60 THR H H 8.17 0.01 1 277 . 60 THR HA H 3.91 0.01 1 278 . 60 THR C C 176.6 0.1 1 279 . 60 THR CA C 66.3 0.1 1 280 . 60 THR N N 117.4 0.1 1 281 . 61 PHE H H 7.96 0.01 1 282 . 61 PHE HA H 4.45 0.01 1 283 . 61 PHE C C 177.7 0.1 1 284 . 61 PHE CA C 61.7 0.1 1 285 . 61 PHE N N 120.7 0.1 1 286 . 62 LYS H H 8.23 0.01 1 287 . 62 LYS HA H 3.41 0.01 1 288 . 62 LYS C C 179.2 0.1 1 289 . 62 LYS CA C 60.2 0.1 1 290 . 62 LYS N N 120.4 0.1 1 291 . 63 GLN H H 7.87 0.01 1 292 . 63 GLN HA H 4.03 0.01 1 293 . 63 GLN C C 178.5 0.1 1 294 . 63 GLN CA C 58.8 0.1 1 295 . 63 GLN N N 117.8 0.1 1 296 . 64 MET H H 7.85 0.01 1 297 . 64 MET HA H 3.94 0.01 1 298 . 64 MET C C 177.6 0.1 1 299 . 64 MET CA C 59.7 0.1 1 300 . 64 MET N N 119.7 0.1 1 301 . 65 VAL H H 7.78 0.01 1 302 . 65 VAL HA H 3.47 0.01 1 303 . 65 VAL C C 177.4 0.1 1 304 . 65 VAL CA C 67 0.1 1 305 . 65 VAL N N 117.2 0.1 1 306 . 66 GLU H H 8.31 0.01 1 307 . 66 GLU HA H 3.98 0.01 1 308 . 66 GLU C C 178.7 0.1 1 309 . 66 GLU CA C 59.6 0.1 1 310 . 66 GLU N N 121.6 0.1 1 311 . 67 LYS H H 7.74 0.01 1 312 . 67 LYS HA H 3.97 0.01 1 313 . 67 LYS C C 179.5 0.1 1 314 . 67 LYS CA C 59.9 0.1 1 315 . 67 LYS N N 118.9 0.1 1 316 . 68 ILE H H 7.49 0.01 1 317 . 68 ILE HA H 3.56 0.01 1 318 . 68 ILE C C 178.8 0.1 1 319 . 68 ILE CA C 65.3 0.1 1 320 . 68 ILE N N 119 0.1 1 321 . 69 LYS H H 8.89 0.01 1 322 . 69 LYS HA H 4.07 0.01 1 323 . 69 LYS C C 180.4 0.1 1 324 . 69 LYS CA C 59.3 0.1 1 325 . 69 LYS N N 122.2 0.1 1 326 . 70 LYS H H 8.6 0.01 1 327 . 70 LYS HA H 4.08 0.01 1 328 . 70 LYS C C 177.9 0.1 1 329 . 70 LYS CA C 58.8 0.1 1 330 . 70 LYS N N 119.7 0.1 1 331 . 71 SER H H 7.45 0.01 1 332 . 71 SER HA H 4.09 0.01 1 333 . 71 SER C C 173.3 0.1 1 334 . 71 SER CA C 61.1 0.1 1 335 . 71 SER N N 113.9 0.1 1 336 . 72 GLY H H 7.56 0.01 1 337 . 72 GLY HA2 H 4.29 0.01 2 338 . 72 GLY HA3 H 3.64 0.01 2 339 . 72 GLY C C 173.7 0.1 1 340 . 72 GLY CA C 44.2 0.1 1 341 . 72 GLY N N 106.7 0.1 1 342 . 73 ALA H H 7.39 0.01 1 343 . 73 ALA HA H 4.06 0.01 1 344 . 73 ALA C C 176.7 0.1 1 345 . 73 ALA CA C 52.9 0.1 1 346 . 73 ALA N N 122.2 0.1 1 347 . 74 ASN H H 8.88 0.01 1 348 . 74 ASN HA H 4.75 0.01 1 349 . 74 ASN C C 174.5 0.1 1 350 . 74 ASN CA C 52.2 0.1 1 351 . 74 ASN N N 116 0.1 1 352 . 75 VAL H H 7.95 0.01 1 353 . 75 VAL HA H 5.37 0.01 1 354 . 75 VAL C C 174.6 0.1 1 355 . 75 VAL CA C 60.9 0.1 1 356 . 75 VAL N N 120.5 0.1 1 357 . 76 VAL H H 9.41 0.01 1 358 . 76 VAL HA H 4.91 0.01 1 359 . 76 VAL C C 173.6 0.1 1 360 . 76 VAL CA C 60.3 0.1 1 361 . 76 VAL N N 126.7 0.1 1 362 . 77 LEU H H 8.92 0.01 1 363 . 77 LEU HA H 4.86 0.01 1 364 . 77 LEU C C 173.2 0.1 1 365 . 77 LEU CA C 53.9 0.1 1 366 . 77 LEU N N 127.7 0.1 1 367 . 78 CYS H H 8.49 0.01 1 368 . 78 CYS HA H 5.63 0.01 1 369 . 78 CYS C C 174.1 0.1 1 370 . 78 CYS CA C 55.9 0.1 1 371 . 78 CYS N N 123.6 0.1 1 372 . 79 GLN H H 8.49 0.01 1 373 . 79 GLN HA H 4.89 0.01 1 374 . 79 GLN C C 175.8 0.1 1 375 . 79 GLN CA C 56.9 0.1 1 376 . 79 GLN N N 127.9 0.1 1 377 . 80 LYS H H 7.89 0.01 1 378 . 80 LYS HA H 4.66 0.01 1 379 . 80 LYS C C 174.7 0.1 1 380 . 80 LYS CA C 53.5 0.1 1 381 . 80 LYS N N 118 0.1 1 382 . 81 GLY H H 8.07 0.01 1 383 . 81 GLY HA2 H 3.96 0.01 2 384 . 81 GLY HA3 H 3.85 0.01 2 385 . 81 GLY C C 171.9 0.1 1 386 . 81 GLY CA C 45.5 0.1 1 387 . 81 GLY N N 106.4 0.1 1 388 . 82 ILE H H 7.35 0.01 1 389 . 82 ILE HA H 4.4 0.01 1 390 . 82 ILE C C 175.2 0.1 1 391 . 82 ILE CA C 60.8 0.1 1 392 . 82 ILE N N 114.7 0.1 1 393 . 83 ASP H H 8.49 0.01 1 394 . 83 ASP HA H 4.63 0.01 1 395 . 83 ASP C C 176.7 0.1 1 396 . 83 ASP CA C 55.3 0.1 1 397 . 83 ASP N N 128.7 0.1 1 398 . 84 ASP H H 8.72 0.01 1 399 . 84 ASP HA H 4.06 0.01 1 400 . 84 ASP C C 178.3 0.1 1 401 . 84 ASP CA C 58.6 0.1 1 402 . 84 ASP N N 124.3 0.1 1 403 . 85 VAL H H 9.04 0.01 1 404 . 85 VAL HA H 3.53 0.01 1 405 . 85 VAL C C 178.3 0.1 1 406 . 85 VAL CA C 66.5 0.1 1 407 . 85 VAL N N 121.3 0.1 1 408 . 86 ALA H H 6.56 0.01 1 409 . 86 ALA HA H 3.91 0.01 1 410 . 86 ALA C C 179.3 0.1 1 411 . 86 ALA CA C 55.5 0.1 1 412 . 86 ALA N N 120.3 0.1 1 413 . 87 GLN H H 8.45 0.01 1 414 . 87 GLN HA H 3.49 0.01 1 415 . 87 GLN C C 177 0.1 1 416 . 87 GLN CA C 59.9 0.1 1 417 . 87 GLN N N 115.8 0.1 1 418 . 88 HIS H H 7.49 0.01 1 419 . 88 HIS HA H 3.74 0.01 1 420 . 88 HIS C C 177.5 0.1 1 421 . 88 HIS CA C 59.5 0.1 1 422 . 88 HIS N N 116.6 0.1 1 423 . 89 TYR H H 7.62 0.01 1 424 . 89 TYR HA H 4.07 0.01 1 425 . 89 TYR C C 178 0.1 1 426 . 89 TYR CA C 62.3 0.1 1 427 . 89 TYR N N 117.7 0.1 1 428 . 90 LEU H H 8.61 0.01 1 429 . 90 LEU HA H 3.91 0.01 1 430 . 90 LEU CA C 57.7 0.1 1 431 . 90 LEU N N 119.9 0.1 1 432 . 91 ALA H H 8.06 0.01 1 433 . 91 ALA HA H 3.77 0.01 1 434 . 91 ALA C C 172.2 0.1 1 435 . 91 ALA CA C 55.1 0.1 1 436 . 91 ALA N N 119.8 0.1 1 437 . 92 LYS H H 7.87 0.01 1 438 . 92 LYS HA H 3.9 0.01 1 439 . 92 LYS C C 178.1 0.1 1 440 . 92 LYS CA C 59 0.1 1 441 . 92 LYS N N 120.6 0.1 1 442 . 93 GLU H H 7.27 0.01 1 443 . 93 GLU HA H 4.53 0.01 1 444 . 93 GLU C C 176.4 0.1 1 445 . 93 GLU CA C 55 0.1 1 446 . 93 GLU N N 114.8 0.1 1 447 . 94 GLY H H 7.83 0.01 1 448 . 94 GLY HA2 H 4.05 0.01 2 449 . 94 GLY HA3 H 3.81 0.01 2 450 . 94 GLY C C 173.7 0.1 1 451 . 94 GLY CA C 46 0.1 1 452 . 94 GLY N N 108.4 0.1 1 453 . 95 ILE H H 7.79 0.01 1 454 . 95 ILE HA H 4.02 0.01 1 455 . 95 ILE C C 173.9 0.1 1 456 . 95 ILE CA C 60.6 0.1 1 457 . 95 ILE N N 121 0.1 1 458 . 96 TYR H H 7.67 0.01 1 459 . 96 TYR HA H 4.14 0.01 1 460 . 96 TYR C C 174.2 0.1 1 461 . 96 TYR CA C 58.3 0.1 1 462 . 96 TYR N N 128.2 0.1 1 463 . 97 ALA H H 7.98 0.01 1 464 . 97 ALA HA H 6.26 0.01 1 465 . 97 ALA C C 173.9 0.1 1 466 . 97 ALA CA C 49.5 0.1 1 467 . 97 ALA N N 131.2 0.1 1 468 . 98 VAL H H 8.01 0.01 1 469 . 98 VAL HA H 4.21 0.01 1 470 . 98 VAL C C 173.8 0.1 1 471 . 98 VAL CA C 60.8 0.1 1 472 . 98 VAL N N 118.9 0.1 1 473 . 99 ARG H H 8.7 0.01 1 474 . 99 ARG HA H 5.2 0.01 1 475 . 99 ARG C C 172.8 0.1 1 476 . 99 ARG CA C 53.1 0.1 1 477 . 99 ARG N N 122.6 0.1 1 478 . 100 ARG H H 8 0.01 1 479 . 100 ARG HA H 3.52 0.01 1 480 . 100 ARG C C 175.1 0.1 1 481 . 100 ARG CA C 56.3 0.1 1 482 . 100 ARG N N 114.5 0.1 1 483 . 101 VAL H H 8.42 0.01 1 484 . 101 VAL HA H 3.66 0.01 1 485 . 101 VAL C C 176.5 0.1 1 486 . 101 VAL CA C 63.5 0.1 1 487 . 101 VAL N N 121.4 0.1 1 488 . 102 LYS H H 9.02 0.01 1 489 . 102 LYS HA H 4.13 0.01 1 490 . 102 LYS C C 178.6 0.1 1 491 . 102 LYS CA C 57.4 0.1 1 492 . 102 LYS N N 126.4 0.1 1 493 . 103 LYS H H 8.86 0.01 1 494 . 103 LYS HA H 3.74 0.01 1 495 . 103 LYS C C 178.3 0.1 1 496 . 103 LYS CA C 60.5 0.1 1 497 . 103 LYS N N 125.5 0.1 1 498 . 104 SER H H 8.53 0.01 1 499 . 104 SER HA H 4.19 0.01 1 500 . 104 SER C C 177.8 0.1 1 501 . 104 SER CA C 61.1 0.1 1 502 . 104 SER N N 111.5 0.1 1 503 . 105 ASP H H 6.89 0.01 1 504 . 105 ASP HA H 4.57 0.01 1 505 . 105 ASP C C 178 0.1 1 506 . 105 ASP CA C 57.3 0.1 1 507 . 105 ASP N N 123.2 0.1 1 508 . 106 MET H H 8.07 0.01 1 509 . 106 MET HA H 4 0.01 1 510 . 106 MET C C 178.3 0.1 1 511 . 106 MET CA C 58.1 0.1 1 512 . 106 MET N N 120.3 0.1 1 513 . 107 GLU H H 8.15 0.01 1 514 . 107 GLU HA H 3.96 0.01 1 515 . 107 GLU C C 179.4 0.1 1 516 . 107 GLU CA C 59.5 0.1 1 517 . 107 GLU N N 117.7 0.1 1 518 . 108 LYS H H 7.69 0.01 1 519 . 108 LYS HA H 4.06 0.01 1 520 . 108 LYS C C 179.9 0.1 1 521 . 108 LYS CA C 59.6 0.1 1 522 . 108 LYS N N 120.5 0.1 1 523 . 109 LEU H H 8.48 0.01 1 524 . 109 LEU HA H 3.95 0.01 1 525 . 109 LEU C C 180 0.1 1 526 . 109 LEU CA C 57.5 0.1 1 527 . 109 LEU N N 120.5 0.1 1 528 . 110 ALA H H 8.69 0.01 1 529 . 110 ALA HA H 3.9 0.01 1 530 . 110 ALA C C 179.5 0.1 1 531 . 110 ALA CA C 56.1 0.1 1 532 . 110 ALA N N 127.6 0.1 1 533 . 111 LYS H H 7.58 0.01 1 534 . 111 LYS HA H 4.08 0.01 1 535 . 111 LYS C C 179 0.1 1 536 . 111 LYS CA C 59 0.1 1 537 . 111 LYS N N 117 0.1 1 538 . 112 ALA H H 7.91 0.01 1 539 . 112 ALA HA H 4.22 0.01 1 540 . 112 ALA C C 178.7 0.1 1 541 . 112 ALA CA C 54.5 0.1 1 542 . 112 ALA N N 118.6 0.1 1 543 . 113 THR H H 7.94 0.01 1 544 . 113 THR HA H 4.72 0.01 1 545 . 113 THR C C 175.8 0.1 1 546 . 113 THR CA C 61.7 0.1 1 547 . 113 THR N N 102.7 0.1 1 548 . 114 GLY H H 7.79 0.01 1 549 . 114 GLY HA2 H 4.18 0.01 2 550 . 114 GLY HA3 H 3.88 0.01 2 551 . 114 GLY C C 173.4 0.1 1 552 . 114 GLY CA C 46 0.1 1 553 . 114 GLY N N 111.1 0.1 1 554 . 115 ALA H H 7.46 0.01 1 555 . 115 ALA HA H 4.17 0.01 1 556 . 115 ALA C C 176 0.1 1 557 . 115 ALA CA C 51.3 0.1 1 558 . 115 ALA N N 122.7 0.1 1 559 . 116 LYS H H 8.03 0.01 1 560 . 116 LYS HA H 4.58 0.01 1 561 . 116 LYS C C 175.3 0.1 1 562 . 116 LYS CA C 54.4 0.1 1 563 . 116 LYS N N 118.8 0.1 1 564 . 117 ILE H H 8.37 0.01 1 565 . 117 ILE HA H 4.09 0.01 1 566 . 117 ILE C C 176.8 0.1 1 567 . 117 ILE CA C 62.4 0.1 1 568 . 117 ILE N N 124.1 0.1 1 569 . 118 VAL H H 8.54 0.01 1 570 . 118 VAL HA H 4.7 0.01 1 571 . 118 VAL C C 175 0.1 1 572 . 118 VAL CA C 60.3 0.1 1 573 . 118 VAL N N 124.6 0.1 1 574 . 119 THR H H 8.63 0.01 1 575 . 119 THR HA H 4.55 0.01 1 576 . 119 THR C C 173.9 0.1 1 577 . 119 THR CA C 62 0.1 1 578 . 119 THR N N 115.8 0.1 1 579 . 120 ASP H H 7.71 0.01 1 580 . 120 ASP HA H 4.76 0.01 1 581 . 120 ASP C C 177 0.1 1 582 . 120 ASP CA C 52.9 0.1 1 583 . 120 ASP N N 122 0.1 1 584 . 121 LEU H H 8.83 0.01 1 585 . 121 LEU HA H 3.88 0.01 1 586 . 121 LEU C C 178.6 0.1 1 587 . 121 LEU CA C 57.5 0.1 1 588 . 121 LEU N N 125.9 0.1 1 589 . 122 ASP H H 8.85 0.01 1 590 . 122 ASP HA H 4.49 0.01 1 591 . 122 ASP C C 176.7 0.1 1 592 . 122 ASP CA C 56.7 0.1 1 593 . 122 ASP N N 118.9 0.1 1 594 . 123 ASP H H 7.88 0.01 1 595 . 123 ASP HA H 4.76 0.01 1 596 . 123 ASP C C 176.1 0.1 1 597 . 123 ASP CA C 54.1 0.1 1 598 . 123 ASP N N 117.6 0.1 1 599 . 124 LEU H H 7.43 0.01 1 600 . 124 LEU HA H 4.18 0.01 1 601 . 124 LEU C C 174.3 0.1 1 602 . 124 LEU CA C 55.9 0.1 1 603 . 124 LEU N N 120.9 0.1 1 604 . 125 THR H H 7.21 0.01 1 605 . 125 THR HA H 4.88 0.01 1 606 . 125 THR CA C 58.9 0.1 1 607 . 125 THR N N 118.2 0.1 1 608 . 126 PRO HA H 4.47 0.01 1 609 . 126 PRO C C 178.8 0.1 1 610 . 126 PRO CA C 65.7 0.1 1 611 . 127 SER H H 7.73 0.01 1 612 . 127 SER HA H 4.37 0.01 1 613 . 127 SER C C 175.6 0.1 1 614 . 127 SER CA C 60.4 0.1 1 615 . 127 SER N N 108.3 0.1 1 616 . 128 VAL H H 7.46 0.01 1 617 . 128 VAL HA H 4.74 0.01 1 618 . 128 VAL C C 176 0.1 1 619 . 128 VAL CA C 61 0.1 1 620 . 128 VAL N N 111.5 0.1 1 621 . 129 LEU H H 7.09 0.01 1 622 . 129 LEU HA H 4.69 0.01 1 623 . 129 LEU C C 178 0.1 1 624 . 129 LEU CA C 54.3 0.1 1 625 . 129 LEU N N 120.2 0.1 1 626 . 130 GLY H H 9.44 0.01 1 627 . 130 GLY HA2 H 4.52 0.01 2 628 . 130 GLY HA3 H 3.36 0.01 2 629 . 130 GLY C C 173.3 0.1 1 630 . 130 GLY CA C 43.6 0.1 1 631 . 130 GLY N N 108.5 0.1 1 632 . 131 GLU H H 8.45 0.01 1 633 . 131 GLU HA H 5.42 0.01 1 634 . 131 GLU C C 174.9 0.1 1 635 . 131 GLU CA C 55.3 0.1 1 636 . 131 GLU N N 119.7 0.1 1 637 . 132 ALA H H 7.96 0.01 1 638 . 132 ALA HA H 4.71 0.01 1 639 . 132 ALA CA C 50.9 0.1 1 640 . 132 ALA N N 121.3 0.1 1 641 . 133 GLU H H 8.14 0.01 1 642 . 133 GLU HA H 4.23 0.01 1 643 . 133 GLU C C 178.6 0.1 1 644 . 133 GLU CA C 60.2 0.1 1 645 . 133 GLU N N 122.8 0.1 1 646 . 134 THR H H 8.03 0.01 1 647 . 134 THR HA H 5.23 0.01 1 648 . 134 THR C C 172.7 0.1 1 649 . 134 THR CA C 61.4 0.1 1 650 . 134 THR N N 110.7 0.1 1 651 . 135 VAL H H 8.57 0.01 1 652 . 135 VAL HA H 4.88 0.01 1 653 . 135 VAL C C 173.6 0.1 1 654 . 135 VAL CA C 61.4 0.1 1 655 . 135 VAL N N 125.4 0.1 1 656 . 136 GLU H H 8.96 0.01 1 657 . 136 GLU HA H 5.36 0.01 1 658 . 136 GLU C C 174 0.1 1 659 . 136 GLU CA C 53.6 0.1 1 660 . 136 GLU N N 123.6 0.1 1 661 . 137 GLU H H 8.7 0.01 1 662 . 137 GLU HA H 5.36 0.01 1 663 . 137 GLU C C 176.9 0.1 1 664 . 137 GLU CA C 55.6 0.1 1 665 . 137 GLU N N 124.6 0.1 1 666 . 138 ARG H H 9.08 0.01 1 667 . 138 ARG HA H 4.71 0.01 1 668 . 138 ARG C C 174.2 0.1 1 669 . 138 ARG CA C 54.6 0.1 1 670 . 138 ARG N N 126.4 0.1 1 671 . 139 LYS H H 8.41 0.01 1 672 . 139 LYS HA H 4.93 0.01 1 673 . 139 LYS C C 175.8 0.1 1 674 . 139 LYS CA C 55.5 0.1 1 675 . 139 LYS N N 123.1 0.1 1 676 . 140 ILE H H 8.62 0.01 1 677 . 140 ILE HA H 4.26 0.01 1 678 . 140 ILE C C 176.4 0.1 1 679 . 140 ILE CA C 59.7 0.1 1 680 . 140 ILE N N 128.7 0.1 1 681 . 141 GLY H H 8.77 0.01 1 682 . 141 GLY HA2 H 3.98 0.01 2 683 . 141 GLY HA3 H 3.61 0.01 2 684 . 141 GLY C C 174.5 0.1 1 685 . 141 GLY CA C 46.9 0.1 1 686 . 141 GLY N N 118.3 0.1 1 687 . 142 ASP H H 8.85 0.01 1 688 . 142 ASP HA H 4.68 0.01 1 689 . 142 ASP C C 175.6 0.1 1 690 . 142 ASP CA C 54.7 0.1 1 691 . 142 ASP N N 126.5 0.1 1 692 . 143 ASP H H 7.91 0.01 1 693 . 143 ASP HA H 4.88 0.01 1 694 . 143 ASP C C 174.6 0.1 1 695 . 143 ASP CA C 54.1 0.1 1 696 . 143 ASP N N 120 0.1 1 697 . 144 ARG H H 8.36 0.01 1 698 . 144 ARG HA H 4.87 0.01 1 699 . 144 ARG C C 174.6 0.1 1 700 . 144 ARG CA C 55.8 0.1 1 701 . 144 ARG N N 122.1 0.1 1 702 . 145 MET H H 8.7 0.01 1 703 . 145 MET HA H 4.8 0.01 1 704 . 145 MET C C 174 0.1 1 705 . 145 MET CA C 54.5 0.1 1 706 . 145 MET N N 119.2 0.1 1 707 . 146 THR H H 8.62 0.01 1 708 . 146 THR HA H 4.97 0.01 1 709 . 146 THR C C 172.3 0.1 1 710 . 146 THR CA C 63.6 0.1 1 711 . 146 THR N N 118 0.1 1 712 . 147 PHE H H 9.91 0.01 1 713 . 147 PHE HA H 4.86 0.01 1 714 . 147 PHE C C 174.3 0.1 1 715 . 147 PHE CA C 56.7 0.1 1 716 . 147 PHE N N 129.6 0.1 1 717 . 148 VAL H H 8.9 0.01 1 718 . 148 VAL HA H 4.47 0.01 1 719 . 148 VAL C C 174.5 0.1 1 720 . 148 VAL CA C 61.7 0.1 1 721 . 148 VAL N N 124.9 0.1 1 722 . 149 MET H H 9.03 0.01 1 723 . 149 MET HA H 4.95 0.01 1 724 . 149 MET C C 176.3 0.1 1 725 . 149 MET CA C 53.6 0.1 1 726 . 149 MET N N 124.4 0.1 1 727 . 150 GLY H H 8.62 0.01 1 728 . 150 GLY HA2 H 3.96 0.01 2 729 . 150 GLY HA3 H 3.81 0.01 2 730 . 150 GLY CA C 47.8 0.1 1 731 . 150 GLY N N 111.6 0.1 1 732 . 151 CYS H H 8.36 0.01 1 733 . 151 CYS CA C 60.7 0.1 1 734 . 151 CYS N N 119.4 0.1 1 stop_ save_