data_17210 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Backbone 1H, 13C, and 15N Chemical Shift Backbone 1H, 13C, and 15N chemical shift assignments for the nucleotide-binding domain of E.coli DnaK in the ATP-bound state ; _BMRB_accession_number 17210 _BMRB_flat_file_name bmr17210.str _Entry_type original _Submission_date 2010-09-27 _Accession_date 2010-09-27 _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 Zhuravleva Anastasia . . 2 Gierasch Lila M. . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 331 "13C chemical shifts" 1026 "15N chemical shifts" 331 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2011-05-05 original author . stop_ loop_ _Related_BMRB_accession_number _Relationship 17208 'NBD(1-388) (ADP-bound state)' 17209 'NBD(1-388) (apo form)' 6229 'Entry containing backbone chemical shift assignments for the NBD of thermus thermophilus DnaK' stop_ _Original_release_date 2011-05-05 save_ ############################# # Citation for this entry # ############################# save_citation_1 _Saveframe_category entry_citation _Citation_full . _Citation_title 'Allosteric signal transmission in the nucleotide-binding domain of 70-kDa heat shock protein (Hsp70) molecular chaperones.' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 21482798 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Zhuravleva Anastasia . . 2 Gierasch Lila M. . stop_ _Journal_abbreviation 'Proc. Natl. Acad. Sci. U.S.A.' _Journal_name_full 'Proceedings of the National Academy of Sciences of the United States of America' _Journal_volume 108 _Journal_issue 17 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 6987 _Page_last 6992 _Year 2011 _Details . loop_ _Keyword allostery 'conformational ensemble' DnaK 'Hsp70 molecular chaperone' 'interdomain linker' 'nucleotide-binding domain' 'subdomain motions' stop_ save_ ####################################### # Cited references within the entry # ####################################### save_Ref_1 _Saveframe_category citation _Citation_full . _Citation_title 'Nmrpipe - a Multidimensional Spectral Processing System Based on Unix Pipes' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID ? loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Delaglio F. . . 2 Grzesiek S. . . 3 Vuister G. . . 4 Zhu G. . . 5 Pfeifer J. . . 6 Bax A. . . stop_ _Journal_abbreviation 'J. Biomol. NMR' _Journal_name_full . _Journal_volume 6 _Journal_issue . _Journal_CSD . _Book_title . _Book_chapter_title . _Book_volume . _Book_series . _Book_publisher . _Book_publisher_city . _Book_ISBN . _Conference_title . _Conference_site . _Conference_state_province . _Conference_country . _Conference_start_date . _Conference_end_date . _Conference_abstract_number . _Thesis_institution . _Thesis_institution_city . _Thesis_institution_country . _Page_first 277 _Page_last 293 _Year 1995 _Details . save_ save_Ref_2 _Saveframe_category citation _Citation_full . _Citation_title 'Automated analysis of protein NMR assignments using methods from artificial intelligence' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID ? loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Zimmerman D. . . 2 Kulikowski C. . . 3 Huang Y. . . 4 Feng W. . . 5 Tashiro M. . . 6 Shimotakahara S. . . 7 Chien C. . . 8 Powers R. . . 9 Montelione G. . . stop_ _Journal_abbreviation 'J. Mol. Biol.' _Journal_name_full . _Journal_volume 269 _Journal_issue . _Journal_CSD . _Book_title . _Book_chapter_title . _Book_volume . _Book_series . _Book_publisher . _Book_publisher_city . _Book_ISBN . _Conference_title . _Conference_site . _Conference_state_province . _Conference_country . _Conference_start_date . _Conference_end_date . _Conference_abstract_number . _Thesis_institution . _Thesis_institution_city . _Thesis_institution_country . _Page_first 592 _Page_last 610 _Year 1997 _Details . save_ save_Ref_3 _Saveframe_category citation _Citation_full . _Citation_title 'Optimizing the process of nuclear magnetic resonance spectrum analysis and computer aided resonance assignment' _Citation_status published _Citation_type thesis _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID ? loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Keller R. . . stop_ _Journal_abbreviation . _Journal_name_full . _Journal_volume . _Journal_issue . _Journal_CSD . _Book_title . _Book_chapter_title . _Book_volume . _Book_series . _Book_publisher . _Book_publisher_city . _Book_ISBN . _Conference_title . _Conference_site . _Conference_state_province . _Conference_country . _Conference_start_date . _Conference_end_date . _Conference_abstract_number . _Thesis_institution ETH _Thesis_institution_city Zurich _Thesis_institution_country Switzerland _Page_first . _Page_last . _Year . _Details . save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name NBD(1-392) _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label NBD $the_nucleotide-binding_domain_of_DnaK ATP $ATP ATPgS $AGS MG $MG stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state ? _System_paramagnetic no _System_thiol_state . _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_the_nucleotide-binding_domain_of_DnaK _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common the_nucleotide-binding_domain_of_DnaK _Molecular_mass . _Mol_thiol_state 'all free' loop_ _Biological_function 'molecular chaperon' stop_ _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 392 _Mol_residue_sequence ; MGKIIGIDLGTTNSCVAIMD GTTPRVLENAEGDRTTPSII AYTQDGETLVGQPAKRQAVT NPQNTLFAIKRLIGRRFQDE EVQRDVSIMPFKIIAADNGD AWVEVKGQKMAPPQISAEVL KKMKKTAEDYLGEPVTEAVI TVPAYFNDAQRQATKDAGRI AGLEVKRIINEPTAAALAYG LDKGTGNRTIAVYDLGGGAF DISIIEIDEVDGEKTFEVLA TNGDTHLGGEDFDSRLINYL VEEFKKDQGIDLRNDPLAMQ RLKEAAEKAKIELSSAQQTD VNLPYITADATGPKHMNIKV TRAKLESLVEDLVNRSIEPL KVALQDAGLSVSDIDDVILV GGQTRMPMVQKKVAEFFGKE PRKDVNPDEAVAIGAAVQGG VLTGDVKDVLLL ; loop_ _Residue_seq_code _Residue_label 1 MET 2 GLY 3 LYS 4 ILE 5 ILE 6 GLY 7 ILE 8 ASP 9 LEU 10 GLY 11 THR 12 THR 13 ASN 14 SER 15 CYS 16 VAL 17 ALA 18 ILE 19 MET 20 ASP 21 GLY 22 THR 23 THR 24 PRO 25 ARG 26 VAL 27 LEU 28 GLU 29 ASN 30 ALA 31 GLU 32 GLY 33 ASP 34 ARG 35 THR 36 THR 37 PRO 38 SER 39 ILE 40 ILE 41 ALA 42 TYR 43 THR 44 GLN 45 ASP 46 GLY 47 GLU 48 THR 49 LEU 50 VAL 51 GLY 52 GLN 53 PRO 54 ALA 55 LYS 56 ARG 57 GLN 58 ALA 59 VAL 60 THR 61 ASN 62 PRO 63 GLN 64 ASN 65 THR 66 LEU 67 PHE 68 ALA 69 ILE 70 LYS 71 ARG 72 LEU 73 ILE 74 GLY 75 ARG 76 ARG 77 PHE 78 GLN 79 ASP 80 GLU 81 GLU 82 VAL 83 GLN 84 ARG 85 ASP 86 VAL 87 SER 88 ILE 89 MET 90 PRO 91 PHE 92 LYS 93 ILE 94 ILE 95 ALA 96 ALA 97 ASP 98 ASN 99 GLY 100 ASP 101 ALA 102 TRP 103 VAL 104 GLU 105 VAL 106 LYS 107 GLY 108 GLN 109 LYS 110 MET 111 ALA 112 PRO 113 PRO 114 GLN 115 ILE 116 SER 117 ALA 118 GLU 119 VAL 120 LEU 121 LYS 122 LYS 123 MET 124 LYS 125 LYS 126 THR 127 ALA 128 GLU 129 ASP 130 TYR 131 LEU 132 GLY 133 GLU 134 PRO 135 VAL 136 THR 137 GLU 138 ALA 139 VAL 140 ILE 141 THR 142 VAL 143 PRO 144 ALA 145 TYR 146 PHE 147 ASN 148 ASP 149 ALA 150 GLN 151 ARG 152 GLN 153 ALA 154 THR 155 LYS 156 ASP 157 ALA 158 GLY 159 ARG 160 ILE 161 ALA 162 GLY 163 LEU 164 GLU 165 VAL 166 LYS 167 ARG 168 ILE 169 ILE 170 ASN 171 GLU 172 PRO 173 THR 174 ALA 175 ALA 176 ALA 177 LEU 178 ALA 179 TYR 180 GLY 181 LEU 182 ASP 183 LYS 184 GLY 185 THR 186 GLY 187 ASN 188 ARG 189 THR 190 ILE 191 ALA 192 VAL 193 TYR 194 ASP 195 LEU 196 GLY 197 GLY 198 GLY 199 ALA 200 PHE 201 ASP 202 ILE 203 SER 204 ILE 205 ILE 206 GLU 207 ILE 208 ASP 209 GLU 210 VAL 211 ASP 212 GLY 213 GLU 214 LYS 215 THR 216 PHE 217 GLU 218 VAL 219 LEU 220 ALA 221 THR 222 ASN 223 GLY 224 ASP 225 THR 226 HIS 227 LEU 228 GLY 229 GLY 230 GLU 231 ASP 232 PHE 233 ASP 234 SER 235 ARG 236 LEU 237 ILE 238 ASN 239 TYR 240 LEU 241 VAL 242 GLU 243 GLU 244 PHE 245 LYS 246 LYS 247 ASP 248 GLN 249 GLY 250 ILE 251 ASP 252 LEU 253 ARG 254 ASN 255 ASP 256 PRO 257 LEU 258 ALA 259 MET 260 GLN 261 ARG 262 LEU 263 LYS 264 GLU 265 ALA 266 ALA 267 GLU 268 LYS 269 ALA 270 LYS 271 ILE 272 GLU 273 LEU 274 SER 275 SER 276 ALA 277 GLN 278 GLN 279 THR 280 ASP 281 VAL 282 ASN 283 LEU 284 PRO 285 TYR 286 ILE 287 THR 288 ALA 289 ASP 290 ALA 291 THR 292 GLY 293 PRO 294 LYS 295 HIS 296 MET 297 ASN 298 ILE 299 LYS 300 VAL 301 THR 302 ARG 303 ALA 304 LYS 305 LEU 306 GLU 307 SER 308 LEU 309 VAL 310 GLU 311 ASP 312 LEU 313 VAL 314 ASN 315 ARG 316 SER 317 ILE 318 GLU 319 PRO 320 LEU 321 LYS 322 VAL 323 ALA 324 LEU 325 GLN 326 ASP 327 ALA 328 GLY 329 LEU 330 SER 331 VAL 332 SER 333 ASP 334 ILE 335 ASP 336 ASP 337 VAL 338 ILE 339 LEU 340 VAL 341 GLY 342 GLY 343 GLN 344 THR 345 ARG 346 MET 347 PRO 348 MET 349 VAL 350 GLN 351 LYS 352 LYS 353 VAL 354 ALA 355 GLU 356 PHE 357 PHE 358 GLY 359 LYS 360 GLU 361 PRO 362 ARG 363 LYS 364 ASP 365 VAL 366 ASN 367 PRO 368 ASP 369 GLU 370 ALA 371 VAL 372 ALA 373 ILE 374 GLY 375 ALA 376 ALA 377 VAL 378 GLN 379 GLY 380 GLY 381 VAL 382 LEU 383 THR 384 GLY 385 ASP 386 VAL 387 LYS 388 ASP 389 VAL 390 LEU 391 LEU 392 LEU stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-07-08 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 17208 the_nucleotide-binding_domain_of_DnaK 98.98 388 99.74 99.74 0.00e+00 BMRB 17209 the_nucleotide-binding_domain_of_DnaK 98.98 388 99.74 99.74 0.00e+00 PDB 1DKG "Crystal Structure Of The Nucleotide Exchange Factor Grpe Bound To The Atpase Domain Of The Molecular Chaperone Dnak" 97.70 383 99.48 99.48 0.00e+00 PDB 2KHO "Nmr-Rdc XRAY STRUCTURE OF E. COLI HSP70 (DNAK) CHAPERONE (1-605) Complexed With Adp And Substrate" 100.00 605 99.74 99.74 0.00e+00 PDB 4B9Q "Open Conformation Of Atp-Bound Hsp70 Homolog Dnak" 99.74 605 97.70 97.70 0.00e+00 PDB 4JN4 "Allosteric Opening Of The Polypeptide-binding Site When An Hsp70 Binds Atp" 99.74 608 100.00 100.00 0.00e+00 PDB 4JNE "Allosteric Opening Of The Polypeptide-binding Site When An Hsp70 Binds Atp" 99.74 608 100.00 100.00 0.00e+00 DBJ BAA01595 "DnaK protein homolog [Escherichia coli]" 100.00 638 99.74 99.74 0.00e+00 DBJ BAB33437 "heat shock protein DnaK [Escherichia coli O157:H7 str. Sakai]" 100.00 638 99.74 99.74 0.00e+00 DBJ BAB96589 "chaperone Hsp70, co-chaperone with DnaJ [Escherichia coli str. K12 substr. W3110]" 100.00 638 99.74 99.74 0.00e+00 DBJ BAG75537 "chaperone protein DnaK [Escherichia coli SE11]" 100.00 638 99.74 99.74 0.00e+00 DBJ BAI23377 "chaperone Hsp70 [Escherichia coli O26:H11 str. 11368]" 100.00 638 99.74 99.74 0.00e+00 EMBL CAD01165 "DnaK protein (heat shock protein 70) [Salmonella enterica subsp. enterica serovar Typhi str. CT18]" 100.00 638 96.94 98.47 0.00e+00 EMBL CAP74584 "chaperone protein dnaK [Escherichia coli LF82]" 100.00 638 99.74 99.74 0.00e+00 EMBL CAQ30531 "chaperone Hsp70; DNA biosynthesis; autoregulated heat shock proteins, subunit of DnaJ/DnaK/GrpE [Escherichia coli BL21(DE3)]" 100.00 638 99.74 99.74 0.00e+00 EMBL CAQ87598 "chaperone Hsp70, co-chaperone with DnaJ [Escherichia fergusonii ATCC 35469]" 100.00 638 99.74 99.74 0.00e+00 EMBL CAQ96905 "chaperone Hsp70, co-chaperone with DnaJ [Escherichia coli IAI1]" 100.00 638 99.74 99.74 0.00e+00 GB AAA23694 "heat shock protein 70 precursor [Escherichia coli]" 100.00 638 99.74 99.74 0.00e+00 GB AAB02910 "DnaK [Salmonella enterica subsp. enterica serovar Typhimurium]" 100.00 638 96.94 98.47 0.00e+00 GB AAC73125 "chaperone Hsp70, with co-chaperone DnaJ [Escherichia coli str. K-12 substr. MG1655]" 100.00 638 99.74 99.74 0.00e+00 GB AAG54314 "chaperone Hsp70; DNA biosynthesis; autoregulated heat shock proteins [Escherichia coli O157:H7 str. EDL933]" 100.00 638 99.74 99.74 0.00e+00 GB AAL18976 "chaperone Hsp70 [Salmonella enterica subsp. enterica serovar Typhimurium str. LT2]" 100.00 638 96.94 98.47 0.00e+00 PIR AE0503 "DnaK protein (heat shock protein 70) [imported] - Salmonella enterica subsp. enterica serovar Typhi (strain CT18)" 100.00 638 96.94 98.47 0.00e+00 REF NP_308041 "molecular chaperone DnaK [Escherichia coli O157:H7 str. Sakai]" 100.00 638 99.74 99.74 0.00e+00 REF NP_414555 "chaperone Hsp70, with co-chaperone DnaJ [Escherichia coli str. K-12 substr. MG1655]" 100.00 638 99.74 99.74 0.00e+00 REF NP_454622 "DnaK protein [Salmonella enterica subsp. enterica serovar Typhi str. CT18]" 100.00 638 96.94 98.47 0.00e+00 REF NP_459017 "chaperone protein DnaK [Salmonella enterica subsp. enterica serovar Typhimurium str. LT2]" 100.00 638 96.94 98.47 0.00e+00 REF NP_705973 "molecular chaperone DnaK [Shigella flexneri 2a str. 301]" 100.00 638 99.49 99.49 0.00e+00 SP A1A766 "RecName: Full=Chaperone protein DnaK; AltName: Full=HSP70; AltName: Full=Heat shock 70 kDa protein; AltName: Full=Heat shock pr" 100.00 638 99.74 99.74 0.00e+00 SP A7MIK5 "RecName: Full=Chaperone protein DnaK; AltName: Full=HSP70; AltName: Full=Heat shock 70 kDa protein; AltName: Full=Heat shock pr" 100.00 638 97.70 98.98 0.00e+00 SP A7ZHA4 "RecName: Full=Chaperone protein DnaK; AltName: Full=HSP70; AltName: Full=Heat shock 70 kDa protein; AltName: Full=Heat shock pr" 100.00 638 99.74 99.74 0.00e+00 SP A7ZVV7 "RecName: Full=Chaperone protein DnaK; AltName: Full=HSP70; AltName: Full=Heat shock 70 kDa protein; AltName: Full=Heat shock pr" 100.00 638 99.74 99.74 0.00e+00 SP A8ALU3 "RecName: Full=Chaperone protein DnaK; AltName: Full=HSP70; AltName: Full=Heat shock 70 kDa protein; AltName: Full=Heat shock pr" 100.00 638 97.45 98.72 0.00e+00 stop_ save_ ############# # Ligands # ############# save_ATP _Saveframe_category ligand _Mol_type non-polymer _Name_common "ATP (ADENOSINE-5'-TRIPHOSPHATE)" _BMRB_code . _PDB_code ATP _Molecular_mass 507.181 _Mol_charge 0 _Mol_paramagnetic . _Mol_aromatic yes _Details ; Information obtained from PDB's Chemical Component Dictionary at http://wwpdb-remediation.rutgers.edu/downloads.html Downloaded on Mon Dec 5 13:35:56 2011 ; loop_ _Atom_name _PDB_atom_name _Atom_type _Atom_chirality _Atom_charge _Atom_oxidation_number _Atom_unpaired_electrons PG PG P . 0 . ? O1G O1G O . 0 . ? O2G O2G O . 0 . ? O3G O3G O . 0 . ? PB PB P . 0 . ? O1B O1B O . 0 . ? O2B O2B O . 0 . ? O3B O3B O . 0 . ? PA PA P . 0 . ? O1A O1A O . 0 . ? O2A O2A O . 0 . ? O3A O3A O . 0 . ? O5' O5' O . 0 . ? C5' C5' C . 0 . ? C4' C4' C . 0 . ? O4' O4' O . 0 . ? C3' C3' C . 0 . ? O3' O3' O . 0 . ? C2' C2' C . 0 . ? O2' O2' O . 0 . ? C1' C1' C . 0 . ? N9 N9 N . 0 . ? C8 C8 C . 0 . ? N7 N7 N . 0 . ? C5 C5 C . 0 . ? C6 C6 C . 0 . ? N6 N6 N . 0 . ? N1 N1 N . 0 . ? C2 C2 C . 0 . ? N3 N3 N . 0 . ? C4 C4 C . 0 . ? HOG2 HOG2 H . 0 . ? HOG3 HOG3 H . 0 . ? HOB2 HOB2 H . 0 . ? HOA2 HOA2 H . 0 . ? H5'1 H5'1 H . 0 . ? H5'2 H5'2 H . 0 . ? H4' H4' H . 0 . ? H3' H3' H . 0 . ? HO3' HO3' H . 0 . ? H2' H2' H . 0 . ? HO2' HO2' H . 0 . ? H1' H1' H . 0 . ? H8 H8 H . 0 . ? HN61 HN61 H . 0 . ? HN62 HN62 H . 0 . ? H2 H2 H . 0 . ? stop_ loop_ _Bond_order _Bond_atom_one_atom_name _Bond_atom_two_atom_name _PDB_bond_atom_one_atom_name _PDB_bond_atom_two_atom_name DOUB PG O1G ? ? SING PG O2G ? ? SING PG O3G ? ? SING PG O3B ? ? SING O2G HOG2 ? ? SING O3G HOG3 ? ? DOUB PB O1B ? ? SING PB O2B ? ? SING PB O3B ? ? SING PB O3A ? ? SING O2B HOB2 ? ? DOUB PA O1A ? ? SING PA O2A ? ? SING PA O3A ? ? SING PA O5' ? ? SING O2A HOA2 ? ? SING O5' C5' ? ? SING C5' C4' ? ? SING C5' H5'1 ? ? SING C5' H5'2 ? ? SING C4' O4' ? ? SING C4' C3' ? ? SING C4' H4' ? ? SING O4' C1' ? ? SING C3' O3' ? ? SING C3' C2' ? ? SING C3' H3' ? ? SING O3' HO3' ? ? SING C2' O2' ? ? SING C2' C1' ? ? SING C2' H2' ? ? SING O2' HO2' ? ? SING C1' N9 ? ? SING C1' H1' ? ? SING N9 C8 ? ? SING N9 C4 ? ? DOUB C8 N7 ? ? SING C8 H8 ? ? SING N7 C5 ? ? SING C5 C6 ? ? DOUB C5 C4 ? ? SING C6 N6 ? ? DOUB C6 N1 ? ? SING N6 HN61 ? ? SING N6 HN62 ? ? SING N1 C2 ? ? DOUB C2 N3 ? ? SING C2 H2 ? ? SING N3 C4 ? ? stop_ _Mol_thiol_state . _Sequence_homology_query_date . save_ save_AGS _Saveframe_category ligand _Mol_type non-polymer _Name_common "AGS (PHOSPHOTHIOPHOSPHORIC ACID-ADENYLATE ESTER)" _BMRB_code . _PDB_code AGS _Molecular_mass 523.247 _Mol_charge 0 _Mol_paramagnetic . _Mol_aromatic yes _Details ; Information obtained from PDB's Chemical Component Dictionary at http://wwpdb-remediation.rutgers.edu/downloads.html Downloaded on Mon Dec 5 13:36:40 2011 ; loop_ _Atom_name _PDB_atom_name _Atom_type _Atom_chirality _Atom_charge _Atom_oxidation_number _Atom_unpaired_electrons PG PG P . 0 . ? S1G S1G S . 0 . ? O2G O2G O . 0 . ? O3G O3G O . 0 . ? PB PB P . 0 . ? O1B O1B O . 0 . ? O2B O2B O . 0 . ? O3B O3B O . 0 . ? PA PA P . 0 . ? O1A O1A O . 0 . ? O2A O2A O . 0 . ? O3A O3A O . 0 . ? O5' O5' O . 0 . ? C5' C5' C . 0 . ? C4' C4' C . 0 . ? O4' O4' O . 0 . ? C3' C3' C . 0 . ? O3' O3' O . 0 . ? C2' C2' C . 0 . ? O2' O2' O . 0 . ? C1' C1' C . 0 . ? N9 N9 N . 0 . ? C8 C8 C . 0 . ? N7 N7 N . 0 . ? C5 C5 C . 0 . ? C6 C6 C . 0 . ? N6 N6 N . 0 . ? N1 N1 N . 0 . ? C2 C2 C . 0 . ? N3 N3 N . 0 . ? C4 C4 C . 0 . ? HSG HSG H . 0 . ? HOG2 HOG2 H . 0 . ? HOB2 HOB2 H . 0 . ? HOA2 HOA2 H . 0 . ? H5'1 H5'1 H . 0 . ? H5'2 H5'2 H . 0 . ? H4' H4' H . 0 . ? H3' H3' H . 0 . ? HO3' HO3' H . 0 . ? H2' H2' H . 0 . ? HO2' HO2' H . 0 . ? H1' H1' H . 0 . ? H8 H8 H . 0 . ? HN61 HN61 H . 0 . ? HN62 HN62 H . 0 . ? H2 H2 H . 0 . ? stop_ loop_ _Bond_order _Bond_atom_one_atom_name _Bond_atom_two_atom_name _PDB_bond_atom_one_atom_name _PDB_bond_atom_two_atom_name SING PG S1G ? ? SING PG O2G ? ? DOUB PG O3G ? ? SING PG O3B ? ? SING S1G HSG ? ? SING O2G HOG2 ? ? DOUB PB O1B ? ? SING PB O2B ? ? SING PB O3B ? ? SING PB O3A ? ? SING O2B HOB2 ? ? DOUB PA O1A ? ? SING PA O2A ? ? SING PA O3A ? ? SING PA O5' ? ? SING O2A HOA2 ? ? SING O5' C5' ? ? SING C5' C4' ? ? SING C5' H5'1 ? ? SING C5' H5'2 ? ? SING C4' O4' ? ? SING C4' C3' ? ? SING C4' H4' ? ? SING O4' C1' ? ? SING C3' O3' ? ? SING C3' C2' ? ? SING C3' H3' ? ? SING O3' HO3' ? ? SING C2' O2' ? ? SING C2' C1' ? ? SING C2' H2' ? ? SING O2' HO2' ? ? SING C1' N9 ? ? SING C1' H1' ? ? SING N9 C8 ? ? SING N9 C4 ? ? DOUB C8 N7 ? ? SING C8 H8 ? ? SING N7 C5 ? ? SING C5 C6 ? ? DOUB C5 C4 ? ? SING C6 N6 ? ? DOUB C6 N1 ? ? SING N6 HN61 ? ? SING N6 HN62 ? ? SING N1 C2 ? ? DOUB C2 N3 ? ? SING C2 H2 ? ? SING N3 C4 ? ? stop_ _Mol_thiol_state . _Sequence_homology_query_date . save_ save_MG _Saveframe_category ligand _Mol_type non-polymer _Name_common "MG (MAGNESIUM ION)" _BMRB_code . _PDB_code MG _Molecular_mass 24.305 _Mol_charge 2 _Mol_paramagnetic . _Mol_aromatic no _Details ; Information obtained from PDB's Chemical Component Dictionary at http://wwpdb-remediation.rutgers.edu/downloads.html Downloaded on Mon Dec 5 12:39:07 2011 ; loop_ _Atom_name _PDB_atom_name _Atom_type _Atom_chirality _Atom_charge _Atom_oxidation_number _Atom_unpaired_electrons MG MG MG . 2 . ? stop_ _Mol_thiol_state . _Sequence_homology_query_date . save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $the_nucleotide-binding_domain_of_DnaK 'E. coli' 562 bacteria . Escherichia coli 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 $the_nucleotide-binding_domain_of_DnaK 'recombinant technology' . Escherichia coli BL21(DE3) pMS119-EH stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_DnaK392_ATP _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling 'potassium phosphate' 10 mM 'natural abundance' 'magnesium chloride' 10 mM 'natural abundance' 'AEBSF protease inhibitor' 1 uM 'natural abundance' DTT 5 mM 'natural abundance' DSS 0.5 mM 'natural abundance' ATP 10 mM 'natural abundance' 'potassium chloride' 10 mM 'natural abundance' $the_nucleotide-binding_domain_of_DnaK 0.5 mM '[U-97% 2H; U-95% 13C; U-95% 15N]' H2O 95 % 'natural abundance' D2O 5 % 'natural abundance' stop_ save_ save_DnaK392_ATPgS _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling 'potassium phosphate' 10 mM 'natural abundance' 'magnesium chloride' 10 mM 'natural abundance' 'AEBSF protease inhibitor' 1 uM 'natural abundance' DTT 5 mM 'natural abundance' DSS 0.5 mM 'natural abundance' ATPgS 10 mM 'natural abundance' 'potassium chloride' 10 mM 'natural abundance' $the_nucleotide-binding_domain_of_DnaK 0.5 mM '[U-97% 2H; U-95% 13C; U-95% 15N]' H2O 95 % 'natural abundance' D2O 5 % 'natural abundance' stop_ save_ ############################ # Computer software used # ############################ save_NMRPipe _Saveframe_category software _Name NMRPipe _Version . loop_ _Vendor _Address _Electronic_address 'Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax' . . stop_ loop_ _Task processing stop_ _Details . save_ save_NMRDraw _Saveframe_category software _Name NMRDraw _Version . loop_ _Vendor _Address _Electronic_address 'Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax' . . stop_ loop_ _Task 'peak picking' stop_ _Details . save_ save_CARA _Saveframe_category software _Name CARA _Version . loop_ _Vendor _Address _Electronic_address 'Keller, Wuthrich' . . stop_ loop_ _Task 'chemical shift assignment' stop_ _Details . save_ save_AutoAssign _Saveframe_category software _Name AutoAssign _Version . loop_ _Vendor _Address _Electronic_address 'Zimmerman, Moseley, Kulikowski and Montelione' . . stop_ loop_ _Task 'chemical shift assignment' stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model Avance _Field_strength 600 _Details 'TCI cryoprobe' save_ ############################# # NMR applied experiments # ############################# save_2D_1H-15N_TROSY_1 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-15N TROSY' _Sample_label $DnaK392_ATP save_ save_3D_TROSY-HNCO_2 _Saveframe_category NMR_applied_experiment _Experiment_name '3D TROSY-HNCO' _Sample_label $DnaK392_ATP save_ save_3D_TROSY-HNCACB_3 _Saveframe_category NMR_applied_experiment _Experiment_name '3D TROSY-HNCACB' _Sample_label $DnaK392_ATP save_ save_3D_TROSY-HN(CO)CACB_4 _Saveframe_category NMR_applied_experiment _Experiment_name '3D TROSY-HN(CO)CACB' _Sample_label $DnaK392_ATP save_ save_2D_1H-15N_TROSY_5 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-15N TROSY' _Sample_label $DnaK392_ATPgS save_ save_3D_TROSY-HNCO_6 _Saveframe_category NMR_applied_experiment _Experiment_name '3D TROSY-HNCO' _Sample_label $DnaK392_ATPgS save_ save_3D_TROSY-HN(CA)CO_7 _Saveframe_category NMR_applied_experiment _Experiment_name '3D TROSY-HN(CA)CO' _Sample_label $DnaK392_ATPgS save_ save_3D_TROSY-HNCACB_8 _Saveframe_category NMR_applied_experiment _Experiment_name '3D TROSY-HNCACB' _Sample_label $DnaK392_ATPgS save_ save_3D_TROSY-HNCA_9 _Saveframe_category NMR_applied_experiment _Experiment_name '3D TROSY-HNCA' _Sample_label $DnaK392_ATPgS save_ ####################### # Sample conditions # ####################### save_sample_conditions_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units 'ionic strength' 0.050 . M pH 7.0 0.1 pH pressure 1 . atm temperature 299 0.2 K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference_1 _Saveframe_category chemical_shift_reference _Details . loop_ _Mol_common_name _Atom_type _Atom_isotope_number _Atom_group _Chem_shift_units _Chem_shift_value _Reference_method _Reference_type _External_reference_sample_geometry _External_reference_location _External_reference_axis _Indirect_shift_ratio DSS C 13 'methyl protons' ppm 0.00 na indirect . . . 0.251449530 DSS H 1 'methyl protons' ppm 0.00 internal direct . . . 1.000000000 DSS N 15 'methyl protons' ppm 0.00 na indirect . . . 0.101329118 stop_ save_ ################################### # Assigned chemical shift lists # ################################### ################################################################### # Chemical Shift Ambiguity Index Value Definitions # # # # The values other than 1 are used for those atoms with different # # chemical shifts that cannot be assigned to stereospecific atoms # # or to specific residues or chains. # # # # Index Value Definition # # # # 1 Unique (including isolated methyl protons, # # geminal atoms, and geminal methyl # # groups with identical chemical shifts) # # (e.g. ILE HD11, HD12, HD13 protons) # # 2 Ambiguity of geminal atoms or geminal methyl # # proton groups (e.g. ASP HB2 and HB3 # # protons, LEU CD1 and CD2 carbons, or # # LEU HD11, HD12, HD13 and HD21, HD22, # # HD23 methyl protons) # # 3 Aromatic atoms on opposite sides of # # symmetrical rings (e.g. TYR HE1 and HE2 # # protons) # # 4 Intraresidue ambiguities (e.g. LYS HG and # # HD protons or TRP HZ2 and HZ3 protons) # # 5 Interresidue ambiguities (LYS 12 vs. LYS 27) # # 6 Intermolecular ambiguities (e.g. ASP 31 CA # # in monomer 1 and ASP 31 CA in monomer 2 # # of an asymmetrical homodimer, duplex # # DNA assignments, or other assignments # # that may apply to atoms in one or more # # molecule in the molecular assembly) # # 9 Ambiguous, specific ambiguity not defined # # # ################################################################### save_assigned_chem_shift_list_1 _Saveframe_category assigned_chemical_shifts _Details 'Chemical shifts for CA, CB and N atoms were corrected for H2-isotope effects' loop_ _Software_label $NMRPipe $NMRDraw $CARA $AutoAssign stop_ loop_ _Experiment_label '2D 1H-15N TROSY' '3D TROSY-HNCO' '3D TROSY-HNCACB' '3D TROSY-HN(CO)CACB' '3D TROSY-HN(CA)CO' '3D TROSY-HNCA' stop_ loop_ _Sample_label $DnaK392_ATP $DnaK392_ATPgS stop_ _Sample_conditions_label $sample_conditions_1 _Chem_shift_reference_set_label $chemical_shift_reference_1 _Mol_system_component_name NBD _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 2 GLY C C 170.522 0.3 1 2 2 2 GLY CA C 43.368 0.3 1 3 3 3 LYS H H 8.997 0.03 1 4 3 3 LYS C C 175.5 0.3 1 5 3 3 LYS CA C 55.375 0.3 1 6 3 3 LYS CB C 33.009 0.3 1 7 3 3 LYS N N 121.967 0.3 1 8 4 4 ILE H H 8.029 0.03 1 9 4 4 ILE C C 176.395 0.3 1 10 4 4 ILE CA C 61.032 0.3 1 11 4 4 ILE CB C 38.179 0.3 1 12 4 4 ILE N N 122.138 0.3 1 13 5 5 ILE H H 7.496 0.03 1 14 5 5 ILE C C 173.798 0.3 1 15 5 5 ILE CA C 61.169 0.3 1 16 5 5 ILE CB C 39.479 0.3 1 17 5 5 ILE N N 120.481 0.3 1 18 6 6 GLY H H 9.084 0.03 1 19 6 6 GLY C C 171.658 0.3 1 20 6 6 GLY CA C 44.589 0.3 1 21 6 6 GLY N N 109.888 0.3 1 22 7 7 ILE H H 8.541 0.03 1 23 7 7 ILE C C 174.193 0.3 1 24 7 7 ILE CA C 60.569 0.3 1 25 7 7 ILE CB C 42.779 0.3 1 26 7 7 ILE N N 123.693 0.3 1 27 8 8 ASP H H 8.186 0.03 1 28 8 8 ASP C C 175.781 0.3 1 29 8 8 ASP CA C 51.621 0.3 1 30 8 8 ASP CB C 42.284 0.3 1 31 8 8 ASP N N 124.111 0.3 1 32 9 9 LEU H H 6.623 0.03 1 33 9 9 LEU C C 175.009 0.3 1 34 9 9 LEU CA C 52.349 0.3 1 35 9 9 LEU CB C 42.359 0.3 1 36 9 9 LEU N N 128.619 0.3 1 37 10 10 GLY H H 7.398 0.03 1 38 10 10 GLY CA C 45.644 0.3 1 39 10 10 GLY N N 115.402 0.3 1 40 12 12 THR C C 175.122 0.3 1 41 13 13 ASN H H 9.326 0.03 1 42 13 13 ASN C C 174.711 0.3 1 43 13 13 ASN CA C 53.281 0.3 1 44 13 13 ASN CB C 43.87 0.3 1 45 13 13 ASN N N 122.271 0.3 1 46 14 14 SER H H 9.677 0.03 1 47 14 14 SER C C 172.105 0.3 1 48 14 14 SER CA C 58.444 0.3 1 49 14 14 SER CB C 65.859 0.3 1 50 14 14 SER N N 118.29 0.3 1 51 15 15 CYS H H 8.501 0.03 1 52 15 15 CYS C C 170.588 0.3 1 53 15 15 CYS CA C 58.08 0.3 1 54 15 15 CYS CB C 30.099 0.3 1 55 15 15 CYS N N 123.581 0.3 1 56 16 16 VAL H H 9.162 0.03 1 57 16 16 VAL C C 170.397 0.3 1 58 16 16 VAL CA C 58.639 0.3 1 59 16 16 VAL CB C 35.399 0.3 1 60 16 16 VAL N N 127.825 0.3 1 61 17 17 ALA H H 9.021 0.03 1 62 17 17 ALA C C 175.273 0.3 1 63 17 17 ALA CA C 49.779 0.3 1 64 17 17 ALA CB C 23.599 0.3 1 65 17 17 ALA N N 128.355 0.3 1 66 18 18 ILE H H 8.476 0.03 1 67 18 18 ILE C C 174.573 0.3 1 68 18 18 ILE CA C 58.969 0.3 1 69 18 18 ILE CB C 43.379 0.3 1 70 18 18 ILE N N 113.508 0.3 1 71 19 19 MET H H 8.293 0.03 1 72 19 19 MET C C 174.724 0.3 1 73 19 19 MET CA C 53.922 0.3 1 74 19 19 MET CB C 29.474 0.3 1 75 19 19 MET N N 120.804 0.3 1 76 20 20 ASP H H 8.349 0.03 1 77 20 20 ASP C C 176.001 0.3 1 78 20 20 ASP CA C 52.121 0.3 1 79 20 20 ASP CB C 40.549 0.3 1 80 20 20 ASP N N 127.728 0.3 1 81 21 21 GLY H H 8.191 0.03 1 82 21 21 GLY C C 174.499 0.3 1 83 21 21 GLY CA C 46.489 0.3 1 84 21 21 GLY N N 114.691 0.3 1 85 22 22 THR H H 8.3 0.03 1 86 22 22 THR C C 174.324 0.3 1 87 22 22 THR CA C 61.929 0.3 1 88 22 22 THR CB C 69.209 0.3 1 89 22 22 THR N N 116.479 0.3 1 90 23 23 THR H H 7.625 0.03 1 91 23 23 THR C C 171.699 0.3 1 92 23 23 THR CA C 59.192 0.3 1 93 23 23 THR CB C 71.272 0.3 1 94 23 23 THR N N 118.712 0.3 1 95 24 24 PRO C C 176.234 0.3 1 96 24 24 PRO CA C 62.409 0.3 1 97 24 24 PRO CB C 32.794 0.3 1 98 25 25 ARG H H 9.06 0.03 1 99 25 25 ARG C C 174.668 0.3 1 100 25 25 ARG CA C 55.259 0.3 1 101 25 25 ARG CB C 33.909 0.3 1 102 25 25 ARG N N 123.794 0.3 1 103 26 26 VAL H H 8.353 0.03 1 104 26 26 VAL C C 175.613 0.3 1 105 26 26 VAL CA C 63.039 0.3 1 106 26 26 VAL CB C 32.199 0.3 1 107 26 26 VAL N N 127.998 0.3 1 108 27 27 LEU H H 7.926 0.03 1 109 27 27 LEU C C 175.884 0.3 1 110 27 27 LEU CA C 53.919 0.3 1 111 27 27 LEU CB C 42.751 0.3 1 112 27 27 LEU N N 125.974 0.3 1 113 28 28 GLU H H 8.128 0.03 1 114 28 28 GLU C C 176.293 0.3 1 115 28 28 GLU CA C 55.901 0.3 1 116 28 28 GLU CB C 30.569 0.3 1 117 28 28 GLU N N 120.432 0.3 1 118 29 29 ASN H H 8.102 0.03 1 119 29 29 ASN C C 177.518 0.3 1 120 29 29 ASN CA C 51.449 0.3 1 121 29 29 ASN CB C 38.909 0.3 1 122 29 29 ASN N N 118.763 0.3 1 123 30 30 ALA H H 8.43 0.03 1 124 30 30 ALA C C 178.563 0.3 1 125 30 30 ALA CA C 54.879 0.3 1 126 30 30 ALA CB C 18.499 0.3 1 127 30 30 ALA N N 121.742 0.3 1 128 31 31 GLU H H 7.635 0.03 1 129 31 31 GLU C C 176.2 0.3 1 130 31 31 GLU CA C 58.589 0.3 1 131 31 31 GLU CB C 29.169 0.3 1 132 31 31 GLU N N 116.585 0.3 1 133 32 32 GLY H H 8.153 0.03 1 134 32 32 GLY C C 173.549 0.3 1 135 32 32 GLY CA C 44.989 0.3 1 136 32 32 GLY N N 108.459 0.3 1 137 33 33 ASP H H 7.806 0.03 1 138 33 33 ASP C C 177.592 0.3 1 139 33 33 ASP CA C 53.349 0.3 1 140 33 33 ASP CB C 43.709 0.3 1 141 33 33 ASP N N 119.714 0.3 1 142 34 34 ARG H H 9.157 0.03 1 143 34 34 ARG C C 175.258 0.3 1 144 34 34 ARG CA C 58.059 0.3 1 145 34 34 ARG CB C 31.409 0.3 1 146 34 34 ARG N N 123.514 0.3 1 147 35 35 THR H H 7.454 0.03 1 148 35 35 THR C C 173.024 0.3 1 149 35 35 THR CA C 60.466 0.3 1 150 35 35 THR CB C 71.997 0.3 1 151 35 35 THR N N 109.166 0.3 1 152 36 36 THR H H 9.251 0.03 1 153 36 36 THR C C 171.699 0.3 1 154 36 36 THR CA C 60.029 0.3 1 155 36 36 THR CB C 72.909 0.3 1 156 36 36 THR N N 117.557 0.3 1 157 38 38 SER C C 174.867 0.3 1 158 39 39 ILE H H 8.476 0.03 1 159 39 39 ILE C C 173.273 0.3 1 160 39 39 ILE CA C 60.498 0.3 1 161 39 39 ILE CB C 41.879 0.3 1 162 39 39 ILE N N 128.252 0.3 1 163 40 40 ILE H H 8.551 0.03 1 164 40 40 ILE C C 173.491 0.3 1 165 40 40 ILE CA C 61.069 0.3 1 166 40 40 ILE CB C 43.179 0.3 1 167 40 40 ILE N N 128.865 0.3 1 168 41 41 ALA H H 9.351 0.03 1 169 41 41 ALA C C 174.503 0.3 1 170 41 41 ALA CA C 49.742 0.3 1 171 41 41 ALA CB C 24.874 0.3 1 172 41 41 ALA N N 127.454 0.3 1 173 42 42 TYR H H 7.849 0.03 1 174 42 42 TYR C C 177.374 0.3 1 175 42 42 TYR CA C 56.882 0.3 1 176 42 42 TYR CB C 39.006 0.3 1 177 42 42 TYR N N 121.494 0.3 1 178 43 43 THR H H 8.626 0.03 1 179 43 43 THR CA C 61.253 0.3 1 180 43 43 THR CB C 71.256 0.3 1 181 43 43 THR N N 114.994 0.3 1 182 44 44 GLN C C 176.65 0.3 1 183 44 44 GLN CA C 58.459 0.3 1 184 45 45 ASP H H 7.884 0.03 1 185 45 45 ASP C C 176.247 0.3 1 186 45 45 ASP CA C 53.749 0.3 1 187 45 45 ASP CB C 40.509 0.3 1 188 45 45 ASP N N 116.454 0.3 1 189 46 46 GLY H H 7.67 0.03 1 190 46 46 GLY C C 174.717 0.3 1 191 46 46 GLY CA C 45.889 0.3 1 192 46 46 GLY N N 107.522 0.3 1 193 47 47 GLU H H 7.562 0.03 1 194 47 47 GLU C C 175.942 0.3 1 195 47 47 GLU CA C 55.889 0.3 1 196 47 47 GLU CB C 31.169 0.3 1 197 47 47 GLU N N 120.957 0.3 1 198 48 48 THR H H 8.538 0.03 1 199 48 48 THR C C 174.075 0.3 1 200 48 48 THR CA C 61.629 0.3 1 201 48 48 THR CB C 69.484 0.3 1 202 48 48 THR N N 120.67 0.3 1 203 49 49 LEU H H 9.136 0.03 1 204 49 49 LEU C C 175.72 0.3 1 205 49 49 LEU CA C 52.582 0.3 1 206 49 49 LEU CB C 45.059 0.3 1 207 49 49 LEU N N 127.416 0.3 1 208 50 50 VAL H H 8.532 0.03 1 209 50 50 VAL C C 175.949 0.3 1 210 50 50 VAL CA C 60.939 0.3 1 211 50 50 VAL CB C 35.599 0.3 1 212 50 50 VAL N N 120.764 0.3 1 213 51 51 GLY H H 8.718 0.03 1 214 51 51 GLY C C 176.001 0.3 1 215 51 51 GLY CA C 44.989 0.3 1 216 51 51 GLY N N 114.359 0.3 1 217 52 52 GLN H H 10.57 0.03 1 218 52 52 GLN CA C 60.789 0.3 1 219 52 52 GLN CB C 25.969 0.3 1 220 52 52 GLN N N 129.196 0.3 1 221 53 53 PRO C C 178.98 0.3 1 222 53 53 PRO CA C 65.817 0.3 1 223 53 53 PRO CB C 31.687 0.3 1 224 54 54 ALA H H 6.446 0.03 1 225 54 54 ALA C C 179.561 0.3 1 226 54 54 ALA CA C 53.725 0.3 1 227 54 54 ALA CB C 19.399 0.3 1 228 54 54 ALA N N 116.63 0.3 1 229 55 55 LYS H H 8.196 0.03 1 230 55 55 LYS C C 179.094 0.3 1 231 55 55 LYS CA C 60.172 0.3 1 232 55 55 LYS CB C 33.009 0.3 1 233 55 55 LYS N N 122.638 0.3 1 234 56 56 ARG H H 8.053 0.03 1 235 56 56 ARG C C 176.92 0.3 1 236 56 56 ARG CA C 58.996 0.3 1 237 56 56 ARG CB C 30.709 0.3 1 238 56 56 ARG N N 115.4 0.3 1 239 57 57 GLN H H 7.03 0.03 1 240 57 57 GLN C C 175.286 0.3 1 241 57 57 GLN CA C 53.889 0.3 1 242 57 57 GLN CB C 29.469 0.3 1 243 57 57 GLN N N 111.336 0.3 1 244 58 58 ALA H H 7.237 0.03 1 245 58 58 ALA C C 179.824 0.3 1 246 58 58 ALA CA C 55.779 0.3 1 247 58 58 ALA CB C 18.787 0.3 1 248 58 58 ALA N N 125.185 0.3 1 249 59 59 VAL H H 7.969 0.03 1 250 59 59 VAL C C 176.676 0.3 1 251 59 59 VAL CA C 64.875 0.3 1 252 59 59 VAL CB C 31.777 0.3 1 253 59 59 VAL N N 113.489 0.3 1 254 60 60 THR H H 7.021 0.03 1 255 60 60 THR C C 174.557 0.3 1 256 60 60 THR CA C 61.754 0.3 1 257 60 60 THR CB C 69.309 0.3 1 258 60 60 THR N N 107.899 0.3 1 259 61 61 ASN H H 7.512 0.03 1 260 61 61 ASN C C 173.699 0.3 1 261 61 61 ASN CA C 51.249 0.3 1 262 61 61 ASN CB C 38.709 0.3 1 263 61 61 ASN N N 120.401 0.3 1 264 62 62 PRO C C 179.064 0.3 1 265 62 62 PRO CA C 65.884 0.3 1 266 62 62 PRO CB C 31.787 0.3 1 267 63 63 GLN H H 8.577 0.03 1 268 63 63 GLN C C 176.001 0.3 1 269 63 63 GLN CA C 58.789 0.3 1 270 63 63 GLN CB C 28.88 0.3 1 271 63 63 GLN N N 114.909 0.3 1 272 64 64 ASN H H 6.595 0.03 1 273 64 64 ASN C C 173.448 0.3 1 274 64 64 ASN CA C 52.249 0.3 1 275 64 64 ASN CB C 40.509 0.3 1 276 64 64 ASN N N 112.699 0.3 1 277 65 65 THR H H 6.927 0.03 1 278 65 65 THR C C 172.207 0.3 1 279 65 65 THR CA C 63.829 0.3 1 280 65 65 THR CB C 68.584 0.3 1 281 65 65 THR N N 117.144 0.3 1 282 66 66 LEU H H 9.662 0.03 1 283 66 66 LEU C C 174.03 0.3 1 284 66 66 LEU CA C 53.819 0.3 1 285 66 66 LEU CB C 42.359 0.3 1 286 66 66 LEU N N 128.08 0.3 1 287 67 67 PHE H H 6.34 0.03 1 288 67 67 PHE C C 171.522 0.3 1 289 67 67 PHE CA C 54.549 0.3 1 290 67 67 PHE CB C 40.197 0.3 1 291 67 67 PHE N N 115.749 0.3 1 292 68 68 ALA H H 9.113 0.03 1 293 68 68 ALA C C 177.343 0.3 1 294 68 68 ALA CA C 54.079 0.3 1 295 68 68 ALA CB C 16.887 0.3 1 296 68 68 ALA N N 115.128 0.3 1 297 69 69 ILE H H 7.742 0.03 1 298 69 69 ILE C C 177.899 0.3 1 299 69 69 ILE CA C 60.869 0.3 1 300 69 69 ILE CB C 35.179 0.3 1 301 69 69 ILE N N 118.629 0.3 1 302 70 70 LYS H H 8.064 0.03 1 303 70 70 LYS C C 176.939 0.3 1 304 70 70 LYS CA C 59.203 0.3 1 305 70 70 LYS CB C 34.985 0.3 1 306 70 70 LYS N N 122.69 0.3 1 307 71 71 ARG H H 7.711 0.03 1 308 71 71 ARG C C 175.933 0.3 1 309 71 71 ARG CA C 58.107 0.3 1 310 71 71 ARG CB C 30.938 0.3 1 311 71 71 ARG N N 114.925 0.3 1 312 72 72 LEU H H 7.746 0.03 1 313 72 72 LEU C C 177.168 0.3 1 314 72 72 LEU CA C 54.619 0.3 1 315 72 72 LEU CB C 44.659 0.3 1 316 72 72 LEU N N 115.069 0.3 1 317 73 73 ILE H H 7.067 0.03 1 318 73 73 ILE C C 175.448 0.3 1 319 73 73 ILE CA C 63.144 0.3 1 320 73 73 ILE CB C 39.686 0.3 1 321 73 73 ILE N N 119.267 0.3 1 322 74 74 GLY H H 9.929 0.03 1 323 74 74 GLY C C 173.724 0.3 1 324 74 74 GLY CA C 46.189 0.3 1 325 74 74 GLY N N 115.053 0.3 1 326 75 75 ARG H H 7.988 0.03 1 327 75 75 ARG C C 176.978 0.3 1 328 75 75 ARG CA C 55.959 0.3 1 329 75 75 ARG CB C 32.609 0.3 1 330 75 75 ARG N N 118.153 0.3 1 331 76 76 ARG H H 8.766 0.03 1 332 76 76 ARG C C 176.76 0.3 1 333 76 76 ARG CA C 54.759 0.3 1 334 76 76 ARG CB C 30.209 0.3 1 335 76 76 ARG N N 121.432 0.3 1 336 77 77 PHE H H 8.765 0.03 1 337 77 77 PHE C C 175.437 0.3 1 338 77 77 PHE CA C 61.849 0.3 1 339 77 77 PHE CB C 39.209 0.3 1 340 77 77 PHE N N 123.047 0.3 1 341 78 78 GLN H H 8.197 0.03 1 342 78 78 GLN C C 175.563 0.3 1 343 78 78 GLN CA C 55.889 0.3 1 344 78 78 GLN CB C 28.269 0.3 1 345 78 78 GLN N N 111.787 0.3 1 346 79 79 ASP H H 7.305 0.03 1 347 79 79 ASP C C 177.55 0.3 1 348 79 79 ASP CA C 54.849 0.3 1 349 79 79 ASP CB C 41.909 0.3 1 350 79 79 ASP N N 123.451 0.3 1 351 80 80 GLU H H 9.097 0.03 1 352 80 80 GLU C C 178.978 0.3 1 353 80 80 GLU CA C 60.589 0.3 1 354 80 80 GLU CB C 29.669 0.3 1 355 80 80 GLU N N 127.634 0.3 1 356 81 81 GLU H H 9.266 0.03 1 357 81 81 GLU C C 178.587 0.3 1 358 81 81 GLU CA C 59.189 0.3 1 359 81 81 GLU CB C 29.053 0.3 1 360 81 81 GLU N N 118.827 0.3 1 361 82 82 VAL H H 6.822 0.03 1 362 82 82 VAL C C 178.147 0.3 1 363 82 82 VAL CA C 65.979 0.3 1 364 82 82 VAL CB C 31.862 0.3 1 365 82 82 VAL N N 119.481 0.3 1 366 83 83 GLN H H 8.068 0.03 1 367 83 83 GLN C C 178.628 0.3 1 368 83 83 GLN CA C 58.103 0.3 1 369 83 83 GLN CB C 28.469 0.3 1 370 83 83 GLN N N 116.574 0.3 1 371 84 84 ARG H H 7.504 0.03 1 372 84 84 ARG C C 178.225 0.3 1 373 84 84 ARG CA C 58.959 0.3 1 374 84 84 ARG CB C 30.009 0.3 1 375 84 84 ARG N N 119.882 0.3 1 376 85 85 ASP H H 7.371 0.03 1 377 85 85 ASP C C 178.561 0.3 1 378 85 85 ASP CA C 57.102 0.3 1 379 85 85 ASP CB C 39.885 0.3 1 380 85 85 ASP N N 121.555 0.3 1 381 86 86 VAL H H 8.314 0.03 1 382 86 86 VAL C C 178.038 0.3 1 383 86 86 VAL CA C 66.539 0.3 1 384 86 86 VAL CB C 32.199 0.3 1 385 86 86 VAL N N 121.897 0.3 1 386 87 87 SER H H 7.274 0.03 1 387 87 87 SER C C 174.751 0.3 1 388 87 87 SER CA C 60.449 0.3 1 389 87 87 SER CB C 64.111 0.3 1 390 87 87 SER N N 111.018 0.3 1 391 88 88 ILE H H 7.287 0.03 1 392 88 88 ILE C C 176.793 0.3 1 393 88 88 ILE CA C 62.069 0.3 1 394 88 88 ILE CB C 40.479 0.3 1 395 88 88 ILE N N 116.163 0.3 1 396 89 89 MET H H 7.775 0.03 1 397 89 89 MET CA C 53.018 0.3 1 398 89 89 MET CB C 30.713 0.3 1 399 89 89 MET N N 122.108 0.3 1 400 90 90 PRO C C 176.298 0.3 1 401 91 91 PHE H H 5.957 0.03 1 402 91 91 PHE C C 173.446 0.3 1 403 91 91 PHE CA C 53.149 0.3 1 404 91 91 PHE CB C 40.846 0.3 1 405 91 91 PHE N N 115.234 0.3 1 406 92 92 LYS H H 8.949 0.03 1 407 92 92 LYS C C 174.658 0.3 1 408 92 92 LYS CA C 56.934 0.3 1 409 92 92 LYS CB C 33.609 0.3 1 410 92 92 LYS N N 122.159 0.3 1 411 93 93 ILE H H 7.858 0.03 1 412 93 93 ILE C C 175.592 0.3 1 413 93 93 ILE CA C 61.669 0.3 1 414 93 93 ILE CB C 39.479 0.3 1 415 93 93 ILE N N 129.106 0.3 1 416 94 94 ILE H H 8.671 0.03 1 417 94 94 ILE C C 173.491 0.3 1 418 94 94 ILE CA C 59.369 0.3 1 419 94 94 ILE CB C 43.179 0.3 1 420 94 94 ILE N N 121.109 0.3 1 421 95 95 ALA H H 7.503 0.03 1 422 95 95 ALA C C 177.869 0.3 1 423 95 95 ALA CA C 50.679 0.3 1 424 95 95 ALA CB C 18.399 0.3 1 425 95 95 ALA N N 123.201 0.3 1 426 96 96 ALA H H 8.595 0.03 1 427 96 96 ALA CA C 50.679 0.3 1 428 96 96 ALA CB C 17.173 0.3 1 429 96 96 ALA N N 126.171 0.3 1 430 97 97 ASP C C 176.583 0.3 1 431 98 98 ASN H H 7.322 0.03 1 432 98 98 ASN C C 177.11 0.3 1 433 98 98 ASN CA C 52.449 0.3 1 434 98 98 ASN CB C 37.809 0.3 1 435 98 98 ASN N N 114.448 0.3 1 436 99 99 GLY H H 7.814 0.03 1 437 99 99 GLY C C 175.111 0.3 1 438 99 99 GLY CA C 44.789 0.3 1 439 99 99 GLY N N 108.402 0.3 1 440 100 100 ASP H H 7.99 0.03 1 441 100 100 ASP C C 174.25 0.3 1 442 100 100 ASP CA C 55.749 0.3 1 443 100 100 ASP CB C 40.509 0.3 1 444 100 100 ASP N N 124.434 0.3 1 445 101 101 ALA H H 8.363 0.03 1 446 101 101 ALA C C 174.717 0.3 1 447 101 101 ALA CA C 52.879 0.3 1 448 101 101 ALA CB C 19.799 0.3 1 449 101 101 ALA N N 121.94 0.3 1 450 102 102 TRP H H 9.597 0.03 1 451 102 102 TRP C C 174.585 0.3 1 452 102 102 TRP CA C 55.249 0.3 1 453 102 102 TRP CB C 33.709 0.3 1 454 102 102 TRP N N 129.817 0.3 1 455 103 103 VAL H H 8.854 0.03 1 456 103 103 VAL C C 174.367 0.3 1 457 103 103 VAL CA C 60.239 0.3 1 458 103 103 VAL CB C 35.699 0.3 1 459 103 103 VAL N N 115.244 0.3 1 460 104 104 GLU H H 8.494 0.03 1 461 104 104 GLU C C 174.856 0.3 1 462 104 104 GLU CA C 54.989 0.3 1 463 104 104 GLU CB C 33.369 0.3 1 464 104 104 GLU N N 125.677 0.3 1 465 105 105 VAL H H 8.621 0.03 1 466 105 105 VAL C C 175.528 0.3 1 467 105 105 VAL CA C 61.23 0.3 1 468 105 105 VAL CB C 35.299 0.3 1 469 105 105 VAL N N 126.482 0.3 1 470 106 106 LYS H H 9.296 0.03 1 471 106 106 LYS C C 176.643 0.3 1 472 106 106 LYS CA C 57.259 0.3 1 473 106 106 LYS CB C 30.049 0.3 1 474 106 106 LYS N N 128.042 0.3 1 475 107 107 GLY H H 8.613 0.03 1 476 107 107 GLY C C 173.491 0.3 1 477 107 107 GLY CA C 45.389 0.3 1 478 107 107 GLY N N 104.879 0.3 1 479 108 108 GLN H H 8.05 0.03 1 480 108 108 GLN C C 174.46 0.3 1 481 108 108 GLN CA C 53.964 0.3 1 482 108 108 GLN CB C 30.369 0.3 1 483 108 108 GLN N N 121.713 0.3 1 484 109 109 LYS H H 8.603 0.03 1 485 109 109 LYS C C 176.083 0.3 1 486 109 109 LYS CA C 56.759 0.3 1 487 109 109 LYS CB C 33.209 0.3 1 488 109 109 LYS N N 125.097 0.3 1 489 110 110 MET H H 9.381 0.03 1 490 110 110 MET C C 172.44 0.3 1 491 110 110 MET CA C 54.889 0.3 1 492 110 110 MET CB C 36.869 0.3 1 493 110 110 MET N N 123.789 0.3 1 494 111 111 ALA H H 7.549 0.03 1 495 111 111 ALA C C 177.299 0.3 1 496 111 111 ALA CA C 48.779 0.3 1 497 111 111 ALA CB C 19.399 0.3 1 498 111 111 ALA N N 126.114 0.3 1 499 113 113 PRO C C 177.725 0.3 1 500 113 113 PRO CA C 66.642 0.3 1 501 113 113 PRO CB C 31.163 0.3 1 502 114 114 GLN H H 7.359 0.03 1 503 114 114 GLN C C 176.893 0.3 1 504 114 114 GLN CA C 59.034 0.3 1 505 114 114 GLN CB C 29.299 0.3 1 506 114 114 GLN N N 113.894 0.3 1 507 115 115 ILE H H 7.272 0.03 1 508 115 115 ILE CA C 63.315 0.3 1 509 115 115 ILE CB C 38.003 0.3 1 510 115 115 ILE N N 119.41 0.3 1 511 116 116 SER C C 176.579 0.3 1 512 116 116 SER CA C 62.474 0.3 1 513 117 117 ALA H H 8.135 0.03 1 514 117 117 ALA C C 179.316 0.3 1 515 117 117 ALA CA C 55.304 0.3 1 516 117 117 ALA CB C 19.7 0.3 1 517 117 117 ALA N N 122.328 0.3 1 518 118 118 GLU H H 7.596 0.03 1 519 118 118 GLU C C 180.551 0.3 1 520 118 118 GLU CA C 58.81 0.3 1 521 118 118 GLU CB C 28.4 0.3 1 522 118 118 GLU N N 115.833 0.3 1 523 119 119 VAL H H 6.951 0.03 1 524 119 119 VAL C C 178.587 0.3 1 525 119 119 VAL CA C 66.191 0.3 1 526 119 119 VAL CB C 31.778 0.3 1 527 119 119 VAL N N 119.657 0.3 1 528 120 120 LEU H H 7.533 0.03 1 529 120 120 LEU C C 178.589 0.3 1 530 120 120 LEU CA C 58.233 0.3 1 531 120 120 LEU CB C 41.43 0.3 1 532 120 120 LEU N N 119.03 0.3 1 533 121 121 LYS H H 8.94 0.03 1 534 121 121 LYS C C 179.065 0.3 1 535 121 121 LYS CA C 60.706 0.3 1 536 121 121 LYS CB C 33.037 0.3 1 537 121 121 LYS N N 120.706 0.3 1 538 122 122 LYS H H 7.169 0.03 1 539 122 122 LYS C C 179.661 0.3 1 540 122 122 LYS CA C 58.958 0.3 1 541 122 122 LYS CB C 31.912 0.3 1 542 122 122 LYS N N 121.236 0.3 1 543 123 123 MET H H 8.101 0.03 1 544 123 123 MET C C 177.057 0.3 1 545 123 123 MET CA C 57.906 0.3 1 546 123 123 MET CB C 32.509 0.3 1 547 123 123 MET N N 122.246 0.3 1 548 124 124 LYS H H 8.363 0.03 1 549 124 124 LYS C C 177.227 0.3 1 550 124 124 LYS CA C 60.259 0.3 1 551 124 124 LYS CB C 34.909 0.3 1 552 124 124 LYS N N 121.328 0.3 1 553 125 125 LYS H H 8.157 0.03 1 554 125 125 LYS C C 177.768 0.3 1 555 125 125 LYS CA C 58.759 0.3 1 556 125 125 LYS CB C 32.62 0.3 1 557 125 125 LYS N N 120.063 0.3 1 558 126 126 THR H H 7.961 0.03 1 559 126 126 THR C C 176.701 0.3 1 560 126 126 THR CA C 67.129 0.3 1 561 126 126 THR CB C 69.284 0.3 1 562 126 126 THR N N 116.309 0.3 1 563 127 127 ALA H H 7.557 0.03 1 564 127 127 ALA C C 178.537 0.3 1 565 127 127 ALA CA C 55.479 0.3 1 566 127 127 ALA CB C 19.199 0.3 1 567 127 127 ALA N N 122.984 0.3 1 568 128 128 GLU H H 8.639 0.03 1 569 128 128 GLU C C 180.787 0.3 1 570 128 128 GLU CA C 60.089 0.3 1 571 128 128 GLU CB C 29.569 0.3 1 572 128 128 GLU N N 120.893 0.3 1 573 129 129 ASP H H 8.981 0.03 1 574 129 129 ASP C C 178.044 0.3 1 575 129 129 ASP CA C 57.149 0.3 1 576 129 129 ASP CB C 39.909 0.3 1 577 129 129 ASP N N 122.019 0.3 1 578 130 130 TYR H H 7.292 0.03 1 579 130 130 TYR C C 177.518 0.3 1 580 130 130 TYR CA C 61.349 0.3 1 581 130 130 TYR CB C 39.509 0.3 1 582 130 130 TYR N N 120.231 0.3 1 583 131 131 LEU H H 8.669 0.03 1 584 131 131 LEU C C 178.861 0.3 1 585 131 131 LEU CA C 56.219 0.3 1 586 131 131 LEU CB C 44.359 0.3 1 587 131 131 LEU N N 117.834 0.3 1 588 132 132 GLY H H 8.526 0.03 1 589 132 132 GLY C C 173.316 0.3 1 590 132 132 GLY CA C 45.889 0.3 1 591 132 132 GLY N N 107.969 0.3 1 592 133 133 GLU H H 7.259 0.03 1 593 133 133 GLU C C 171.499 0.3 1 594 133 133 GLU CA C 53.289 0.3 1 595 133 133 GLU CB C 31.269 0.3 1 596 133 133 GLU N N 116.681 0.3 1 597 134 134 PRO C C 176.876 0.3 1 598 134 134 PRO CA C 62.712 0.3 1 599 134 134 PRO CB C 32.538 0.3 1 600 135 135 VAL H H 9.908 0.03 1 601 135 135 VAL C C 175.277 0.3 1 602 135 135 VAL CA C 62.539 0.3 1 603 135 135 VAL CB C 34.499 0.3 1 604 135 135 VAL N N 125.773 0.3 1 605 136 136 THR H H 9.057 0.03 1 606 136 136 THR C C 174.518 0.3 1 607 136 136 THR CA C 61.009 0.3 1 608 136 136 THR CB C 71.009 0.3 1 609 136 136 THR N N 114.011 0.3 1 610 137 137 GLU H H 7.76 0.03 1 611 137 137 GLU C C 174.382 0.3 1 612 137 137 GLU CA C 55.889 0.3 1 613 137 137 GLU CB C 35.469 0.3 1 614 137 137 GLU N N 123.208 0.3 1 615 138 138 ALA H H 8.281 0.03 1 616 138 138 ALA C C 175.884 0.3 1 617 138 138 ALA CA C 50.779 0.3 1 618 138 138 ALA CB C 25.299 0.3 1 619 138 138 ALA N N 119.483 0.3 1 620 139 139 VAL H H 8.882 0.03 1 621 139 139 VAL C C 174.711 0.3 1 622 139 139 VAL CA C 62.339 0.3 1 623 139 139 VAL CB C 34.347 0.3 1 624 139 139 VAL N N 122.35 0.3 1 625 140 140 ILE H H 7.378 0.03 1 626 140 140 ILE C C 174.349 0.3 1 627 140 140 ILE CA C 59.432 0.3 1 628 140 140 ILE CB C 41.379 0.3 1 629 140 140 ILE N N 124.872 0.3 1 630 141 141 THR H H 7.872 0.03 1 631 141 141 THR C C 174.143 0.3 1 632 141 141 THR CA C 59.929 0.3 1 633 141 141 THR CB C 70.009 0.3 1 634 141 141 THR N N 116.949 0.3 1 635 142 142 VAL H H 7.925 0.03 1 636 142 142 VAL CA C 57.569 0.3 1 637 142 142 VAL CB C 33.799 0.3 1 638 142 142 VAL N N 109.209 0.3 1 639 145 145 TYR C C 176.468 0.3 1 640 146 146 PHE H H 7.231 0.03 1 641 146 146 PHE C C 177.799 0.3 1 642 146 146 PHE CA C 56.336 0.3 1 643 146 146 PHE CB C 37.009 0.3 1 644 146 146 PHE N N 124.086 0.3 1 645 147 147 ASN H H 9.197 0.03 1 646 147 147 ASN C C 176.345 0.3 1 647 147 147 ASN CA C 51.249 0.3 1 648 147 147 ASN CB C 39.109 0.3 1 649 147 147 ASN N N 124.912 0.3 1 650 148 148 ASP H H 8.372 0.03 1 651 148 148 ASP C C 178.219 0.3 1 652 148 148 ASP CA C 58.549 0.3 1 653 148 148 ASP CB C 40.792 0.3 1 654 148 148 ASP N N 117.886 0.3 1 655 149 149 ALA H H 8.126 0.03 1 656 149 149 ALA C C 181.896 0.3 1 657 149 149 ALA CA C 55.448 0.3 1 658 149 149 ALA CB C 18.199 0.3 1 659 149 149 ALA N N 125.19 0.3 1 660 150 150 GLN H H 8.672 0.03 1 661 150 150 GLN C C 179.445 0.3 1 662 150 150 GLN CA C 59.507 0.3 1 663 150 150 GLN CB C 29.652 0.3 1 664 150 150 GLN N N 120.41 0.3 1 665 151 151 ARG H H 8.463 0.03 1 666 151 151 ARG C C 178.102 0.3 1 667 151 151 ARG CA C 61.359 0.3 1 668 151 151 ARG CB C 30.009 0.3 1 669 151 151 ARG N N 122.105 0.3 1 670 152 152 GLN H H 8.77 0.03 1 671 152 152 GLN C C 178.044 0.3 1 672 152 152 GLN CA C 58.889 0.3 1 673 152 152 GLN CB C 28.069 0.3 1 674 152 152 GLN N N 120.712 0.3 1 675 153 153 ALA H H 8.122 0.03 1 676 153 153 ALA C C 179.399 0.3 1 677 153 153 ALA CA C 54.868 0.3 1 678 153 153 ALA CB C 19.799 0.3 1 679 153 153 ALA N N 121.198 0.3 1 680 154 154 THR C C 175.802 0.3 1 681 155 155 LYS H H 8.005 0.03 1 682 155 155 LYS C C 179.596 0.3 1 683 155 155 LYS CA C 61.359 0.3 1 684 155 155 LYS CB C 32.109 0.3 1 685 155 155 LYS N N 123.414 0.3 1 686 156 156 ASP H H 8.697 0.03 1 687 156 156 ASP C C 177.869 0.3 1 688 156 156 ASP CA C 57.649 0.3 1 689 156 156 ASP CB C 40.209 0.3 1 690 156 156 ASP N N 121.846 0.3 1 691 157 157 ALA H H 7.747 0.03 1 692 157 157 ALA C C 179.153 0.3 1 693 157 157 ALA CA C 55.079 0.3 1 694 157 157 ALA CB C 18.299 0.3 1 695 157 157 ALA N N 122.5 0.3 1 696 158 158 GLY H H 7.558 0.03 1 697 158 158 GLY C C 174.168 0.3 1 698 158 158 GLY CA C 47.589 0.3 1 699 158 158 GLY N N 103.953 0.3 1 700 159 159 ARG H H 8.057 0.03 1 701 159 159 ARG C C 181.546 0.3 1 702 159 159 ARG CA C 59.959 0.3 1 703 159 159 ARG CB C 29.709 0.3 1 704 159 159 ARG N N 124.625 0.3 1 705 160 160 ILE H H 8.441 0.03 1 706 160 160 ILE C C 177.285 0.3 1 707 160 160 ILE CA C 65.369 0.3 1 708 160 160 ILE CB C 38.48 0.3 1 709 160 160 ILE N N 124.085 0.3 1 710 161 161 ALA H H 7.421 0.03 1 711 161 161 ALA C C 175.666 0.3 1 712 161 161 ALA CA C 52.579 0.3 1 713 161 161 ALA CB C 20.299 0.3 1 714 161 161 ALA N N 120.846 0.3 1 715 162 162 GLY H H 7.828 0.03 1 716 162 162 GLY C C 174.191 0.3 1 717 162 162 GLY CA C 45.389 0.3 1 718 162 162 GLY N N 106.617 0.3 1 719 163 163 LEU H H 8.167 0.03 1 720 163 163 LEU C C 175.242 0.3 1 721 163 163 LEU CA C 52.294 0.3 1 722 163 163 LEU CB C 44.059 0.3 1 723 163 163 LEU N N 120.012 0.3 1 724 164 164 GLU H H 8.867 0.03 1 725 164 164 GLU C C 175.744 0.3 1 726 164 164 GLU CA C 55.789 0.3 1 727 164 164 GLU CB C 29.669 0.3 1 728 164 164 GLU N N 124.37 0.3 1 729 165 165 VAL H H 8.429 0.03 1 730 165 165 VAL C C 175.744 0.3 1 731 165 165 VAL CA C 62.639 0.3 1 732 165 165 VAL CB C 30.199 0.3 1 733 165 165 VAL N N 129.741 0.3 1 734 166 166 LYS H H 8.861 0.03 1 735 166 166 LYS C C 177.505 0.3 1 736 166 166 LYS CA C 56.348 0.3 1 737 166 166 LYS CB C 32.609 0.3 1 738 166 166 LYS N N 129.675 0.3 1 739 167 167 ARG H H 7.138 0.03 1 740 167 167 ARG C C 173.465 0.3 1 741 167 167 ARG CA C 54.947 0.3 1 742 167 167 ARG CB C 34.909 0.3 1 743 167 167 ARG N N 114.179 0.3 1 744 168 168 ILE H H 8.183 0.03 1 745 168 168 ILE C C 176.433 0.3 1 746 168 168 ILE CA C 58.969 0.3 1 747 168 168 ILE CB C 38.263 0.3 1 748 168 168 ILE N N 124.325 0.3 1 749 169 169 ILE H H 7.584 0.03 1 750 169 169 ILE C C 173.417 0.3 1 751 169 169 ILE CA C 57.69 0.3 1 752 169 169 ILE CB C 41.679 0.3 1 753 169 169 ILE N N 120.93 0.3 1 754 170 170 ASN H H 8.574 0.03 1 755 170 170 ASN C C 177.884 0.3 1 756 170 170 ASN CA C 51.856 0.3 1 757 170 170 ASN CB C 38.833 0.3 1 758 170 170 ASN N N 122.678 0.3 1 759 171 171 GLU H H 8.901 0.03 1 760 171 171 GLU CA C 60.964 0.3 1 761 171 171 GLU CB C 27.169 0.3 1 762 171 171 GLU N N 123.313 0.3 1 763 172 172 PRO C C 178.607 0.3 1 764 173 173 THR H H 6.515 0.03 1 765 173 173 THR C C 175.359 0.3 1 766 173 173 THR CA C 66.075 0.3 1 767 173 173 THR CB C 67.855 0.3 1 768 173 173 THR N N 113.252 0.3 1 769 174 174 ALA H H 7.898 0.03 1 770 174 174 ALA C C 178.864 0.3 1 771 174 174 ALA CA C 55.797 0.3 1 772 174 174 ALA CB C 18.168 0.3 1 773 174 174 ALA N N 123.973 0.3 1 774 175 175 ALA H H 7.942 0.03 1 775 175 175 ALA C C 178.861 0.3 1 776 175 175 ALA CA C 55.233 0.3 1 777 175 175 ALA CB C 18.168 0.3 1 778 175 175 ALA N N 119.594 0.3 1 779 176 176 ALA H H 7.769 0.03 1 780 176 176 ALA C C 179.386 0.3 1 781 176 176 ALA CA C 55.364 0.3 1 782 176 176 ALA CB C 18.969 0.3 1 783 176 176 ALA N N 118.952 0.3 1 784 177 177 LEU H H 7.966 0.03 1 785 177 177 LEU CA C 57.919 0.3 1 786 177 177 LEU CB C 42.113 0.3 1 787 177 177 LEU N N 120.292 0.3 1 788 182 182 ASP C C 176.019 0.3 1 789 182 182 ASP CA C 54.112 0.3 1 790 183 183 LYS H H 7.57 0.03 1 791 183 183 LYS C C 177.139 0.3 1 792 183 183 LYS CA C 56.114 0.3 1 793 183 183 LYS CB C 32.548 0.3 1 794 183 183 LYS N N 120.509 0.3 1 795 184 184 GLY H H 8.484 0.03 1 796 184 184 GLY C C 174.109 0.3 1 797 184 184 GLY CA C 45.142 0.3 1 798 184 184 GLY N N 110.448 0.3 1 799 185 185 THR H H 7.871 0.03 1 800 185 185 THR C C 175.255 0.3 1 801 185 185 THR CA C 62.504 0.3 1 802 185 185 THR CB C 70.134 0.3 1 803 185 185 THR N N 113.987 0.3 1 804 186 186 GLY H H 8.388 0.03 1 805 186 186 GLY C C 172.952 0.3 1 806 186 186 GLY CA C 44.689 0.3 1 807 186 186 GLY N N 111.937 0.3 1 808 187 187 ASN H H 8.284 0.03 1 809 187 187 ASN C C 175.826 0.3 1 810 187 187 ASN CA C 53.149 0.3 1 811 187 187 ASN CB C 38.682 0.3 1 812 187 187 ASN N N 121.29 0.3 1 813 188 188 ARG H H 8.843 0.03 1 814 188 188 ARG C C 174.109 0.3 1 815 188 188 ARG CA C 54.497 0.3 1 816 188 188 ARG CB C 34.709 0.3 1 817 188 188 ARG N N 123.567 0.3 1 818 189 189 THR H H 9.841 0.03 1 819 189 189 THR C C 174.635 0.3 1 820 189 189 THR CA C 62.329 0.3 1 821 189 189 THR CB C 69.409 0.3 1 822 189 189 THR N N 121.88 0.3 1 823 190 190 ILE H H 9.41 0.03 1 824 190 190 ILE C C 173.807 0.3 1 825 190 190 ILE CA C 58.769 0.3 1 826 190 190 ILE CB C 41.732 0.3 1 827 190 190 ILE N N 121.352 0.3 1 828 191 191 ALA H H 7.97 0.03 1 829 191 191 ALA C C 174.717 0.3 1 830 191 191 ALA CA C 49.564 0.3 1 831 191 191 ALA CB C 21.584 0.3 1 832 191 191 ALA N N 123.313 0.3 1 833 192 192 VAL H H 9.124 0.03 1 834 192 192 VAL C C 173.507 0.3 1 835 192 192 VAL CA C 61.939 0.3 1 836 192 192 VAL CB C 32.886 0.3 1 837 192 192 VAL N N 123.225 0.3 1 838 193 193 TYR H H 8.861 0.03 1 839 193 193 TYR C C 172.241 0.3 1 840 193 193 TYR CA C 57.149 0.3 1 841 193 193 TYR CB C 40.284 0.3 1 842 193 193 TYR N N 134.378 0.3 1 843 194 194 ASP H H 8.913 0.03 1 844 194 194 ASP C C 175.329 0.3 1 845 194 194 ASP CA C 51.549 0.3 1 846 194 194 ASP CB C 42.522 0.3 1 847 194 194 ASP N N 129.502 0.3 1 848 195 195 LEU H H 8.074 0.03 1 849 195 195 LEU CA C 53.704 0.3 1 850 195 195 LEU CB C 44.744 0.3 1 851 195 195 LEU N N 128.119 0.3 1 852 200 200 PHE C C 174.565 0.3 1 853 201 201 ASP H H 8.81 0.03 1 854 201 201 ASP C C 171.87 0.3 1 855 201 201 ASP CA C 52.926 0.3 1 856 201 201 ASP CB C 45.976 0.3 1 857 201 201 ASP N N 131.747 0.3 1 858 202 202 ILE H H 7.961 0.03 1 859 202 202 ILE C C 173.666 0.3 1 860 202 202 ILE CA C 55.733 0.3 1 861 202 202 ILE CB C 40.879 0.3 1 862 202 202 ILE N N 119.652 0.3 1 863 203 203 SER H H 8.326 0.03 1 864 203 203 SER C C 172.026 0.3 1 865 203 203 SER CA C 57.564 0.3 1 866 203 203 SER CB C 66.909 0.3 1 867 203 203 SER N N 120.823 0.3 1 868 204 204 ILE H H 8.831 0.03 1 869 204 204 ILE C C 175.258 0.3 1 870 204 204 ILE CA C 58.969 0.3 1 871 204 204 ILE CB C 37.379 0.3 1 872 204 204 ILE N N 126.274 0.3 1 873 205 205 ILE H H 9.107 0.03 1 874 205 205 ILE C C 172.785 0.3 1 875 205 205 ILE CA C 60.519 0.3 1 876 205 205 ILE CB C 42.778 0.3 1 877 205 205 ILE N N 129.564 0.3 1 878 206 206 GLU H H 9.361 0.03 1 879 206 206 GLU C C 175.307 0.3 1 880 206 206 GLU CA C 55.126 0.3 1 881 206 206 GLU CB C 31.682 0.3 1 882 206 206 GLU N N 129.678 0.3 1 883 207 207 ILE H H 9.366 0.03 1 884 207 207 ILE C C 174.775 0.3 1 885 207 207 ILE CA C 60.092 0.3 1 886 207 207 ILE CB C 39.404 0.3 1 887 207 207 ILE N N 131.408 0.3 1 888 208 208 ASP H H 8.248 0.03 1 889 208 208 ASP C C 174.81 0.3 1 890 208 208 ASP CA C 52.249 0.3 1 891 208 208 ASP CB C 43.047 0.3 1 892 208 208 ASP N N 127.966 0.3 1 893 209 209 GLU H H 8.508 0.03 1 894 209 209 GLU C C 175.184 0.3 1 895 209 209 GLU CA C 55.452 0.3 1 896 209 209 GLU CB C 32.069 0.3 1 897 209 209 GLU N N 122.576 0.3 1 898 210 210 VAL H H 8.623 0.03 1 899 210 210 VAL C C 176.001 0.3 1 900 210 210 VAL CA C 62.139 0.3 1 901 210 210 VAL CB C 34.399 0.3 1 902 210 210 VAL N N 127.082 0.3 1 903 211 211 ASP H H 9.263 0.03 1 904 211 211 ASP C C 175.738 0.3 1 905 211 211 ASP CA C 55.749 0.3 1 906 211 211 ASP CB C 39.809 0.3 1 907 211 211 ASP N N 129.73 0.3 1 908 212 212 GLY H H 8.493 0.03 1 909 212 212 GLY C C 173.71 0.3 1 910 212 212 GLY CA C 45.052 0.3 1 911 212 212 GLY N N 104.613 0.3 1 912 213 213 GLU H H 7.78 0.03 1 913 213 213 GLU C C 175.184 0.3 1 914 213 213 GLU CA C 55.023 0.3 1 915 213 213 GLU CB C 31.041 0.3 1 916 213 213 GLU N N 121.636 0.3 1 917 214 214 LYS H H 8.518 0.03 1 918 214 214 LYS C C 175.447 0.3 1 919 214 214 LYS CA C 55.471 0.3 1 920 214 214 LYS CB C 34.275 0.3 1 921 214 214 LYS N N 125.984 0.3 1 922 215 215 THR H H 8.755 0.03 1 923 215 215 THR C C 173.199 0.3 1 924 215 215 THR CA C 60.329 0.3 1 925 215 215 THR CB C 70.809 0.3 1 926 215 215 THR N N 116.68 0.3 1 927 216 216 PHE H H 8.349 0.03 1 928 216 216 PHE C C 174.775 0.3 1 929 216 216 PHE CA C 56.449 0.3 1 930 216 216 PHE CB C 41.484 0.3 1 931 216 216 PHE N N 120.413 0.3 1 932 217 217 GLU H H 8.87 0.03 1 933 217 217 GLU C C 174.711 0.3 1 934 217 217 GLU CA C 55.089 0.3 1 935 217 217 GLU CB C 33.184 0.3 1 936 217 217 GLU N N 125.049 0.3 1 937 218 218 VAL H H 9.111 0.03 1 938 218 218 VAL C C 176.176 0.3 1 939 218 218 VAL CA C 63.653 0.3 1 940 218 218 VAL CB C 31.713 0.3 1 941 218 218 VAL N N 128.547 0.3 1 942 219 219 LEU H H 9.301 0.03 1 943 219 219 LEU C C 177.869 0.3 1 944 219 219 LEU CA C 55.71 0.3 1 945 219 219 LEU CB C 42.959 0.3 1 946 219 219 LEU N N 129.896 0.3 1 947 220 220 ALA H H 7.511 0.03 1 948 220 220 ALA C C 175.393 0.3 1 949 220 220 ALA CA C 52.648 0.3 1 950 220 220 ALA CB C 23.999 0.3 1 951 220 220 ALA N N 117.234 0.3 1 952 221 221 THR H H 8.566 0.03 1 953 221 221 THR C C 172.366 0.3 1 954 221 221 THR CA C 60.832 0.3 1 955 221 221 THR CB C 71.506 0.3 1 956 221 221 THR N N 115.831 0.3 1 957 222 222 ASN H H 9.336 0.03 1 958 222 222 ASN C C 173.642 0.3 1 959 222 222 ASN CA C 53.049 0.3 1 960 222 222 ASN CB C 41.909 0.3 1 961 222 222 ASN N N 128.633 0.3 1 962 223 223 GLY H H 9.8 0.03 1 963 223 223 GLY C C 170.911 0.3 1 964 223 223 GLY CA C 46.014 0.3 1 965 223 223 GLY N N 110.058 0.3 1 966 224 224 ASP H H 8.777 0.03 1 967 224 224 ASP C C 176.536 0.3 1 968 224 224 ASP CA C 54.049 0.3 1 969 224 224 ASP CB C 44.109 0.3 1 970 224 224 ASP N N 119.738 0.3 1 971 225 225 THR H H 8.549 0.03 1 972 225 225 THR C C 173.765 0.3 1 973 225 225 THR CA C 63.129 0.3 1 974 225 225 THR CB C 68.679 0.3 1 975 225 225 THR N N 118.284 0.3 1 976 226 226 HIS H H 8.984 0.03 1 977 226 226 HIS C C 172.843 0.3 1 978 226 226 HIS CA C 54.069 0.3 1 979 226 226 HIS CB C 28.209 0.3 1 980 226 226 HIS N N 120.863 0.3 1 981 227 227 LEU H H 6.735 0.03 1 982 227 227 LEU C C 172.032 0.3 1 983 227 227 LEU CA C 54.389 0.3 1 984 227 227 LEU CB C 44.059 0.3 1 985 227 227 LEU N N 124.154 0.3 1 986 228 228 GLY H H 8.674 0.03 1 987 228 228 GLY C C 175.125 0.3 1 988 228 228 GLY CA C 44.189 0.3 1 989 228 228 GLY N N 108.114 0.3 1 990 229 229 GLY H H 9.687 0.03 1 991 229 229 GLY CA C 48.077 0.3 1 992 229 229 GLY N N 108.693 0.3 1 993 230 230 GLU C C 179.97 0.3 1 994 231 231 ASP H H 7.935 0.03 1 995 231 231 ASP C C 179.099 0.3 1 996 231 231 ASP CA C 56.049 0.3 1 997 231 231 ASP CB C 41.609 0.3 1 998 231 231 ASP N N 117.962 0.3 1 999 233 233 ASP C C 179.302 0.3 1 1000 233 233 ASP CA C 57.995 0.3 1 1001 233 233 ASP CB C 39.531 0.3 1 1002 234 234 SER H H 8.065 0.03 1 1003 234 234 SER C C 176.683 0.3 1 1004 234 234 SER CA C 61.928 0.3 1 1005 234 234 SER CB C 63.287 0.3 1 1006 234 234 SER N N 113.821 0.3 1 1007 235 235 ARG H H 7.327 0.03 1 1008 235 235 ARG C C 179.715 0.3 1 1009 235 235 ARG CA C 56.89 0.3 1 1010 235 235 ARG CB C 29.992 0.3 1 1011 235 235 ARG N N 118.607 0.3 1 1012 236 236 LEU H H 7.33 0.03 1 1013 236 236 LEU C C 177.885 0.3 1 1014 236 236 LEU CA C 57.504 0.3 1 1015 236 236 LEU CB C 41.763 0.3 1 1016 236 236 LEU N N 121.255 0.3 1 1017 237 237 ILE H H 9.049 0.03 1 1018 237 237 ILE C C 177.203 0.3 1 1019 237 237 ILE CA C 67.061 0.3 1 1020 237 237 ILE CB C 38.795 0.3 1 1021 237 237 ILE N N 121.651 0.3 1 1022 238 238 ASN H H 8.03 0.03 1 1023 238 238 ASN CA C 56.991 0.3 1 1024 238 238 ASN CB C 38.225 0.3 1 1025 238 238 ASN N N 116.379 0.3 1 1026 239 239 TYR C C 176.362 0.3 1 1027 239 239 TYR CA C 61.086 0.3 1 1028 239 239 TYR CB C 39.081 0.3 1 1029 240 240 LEU H H 8.246 0.03 1 1030 240 240 LEU C C 179.27 0.3 1 1031 240 240 LEU CA C 58.278 0.3 1 1032 240 240 LEU CB C 41.763 0.3 1 1033 240 240 LEU N N 119.989 0.3 1 1034 241 241 VAL H H 8.57 0.03 1 1035 241 241 VAL C C 179.928 0.3 1 1036 241 241 VAL CA C 66.846 0.3 1 1037 241 241 VAL CB C 32.399 0.3 1 1038 241 241 VAL N N 118.718 0.3 1 1039 242 242 GLU H H 8.224 0.03 1 1040 242 242 GLU C C 179.912 0.3 1 1041 242 242 GLU CA C 59.496 0.3 1 1042 242 242 GLU CB C 28.878 0.3 1 1043 242 242 GLU N N 122.332 0.3 1 1044 243 243 GLU H H 8.643 0.03 1 1045 243 243 GLU C C 178.899 0.3 1 1046 243 243 GLU CA C 59.389 0.3 1 1047 243 243 GLU CB C 29.469 0.3 1 1048 243 243 GLU N N 121.61 0.3 1 1049 244 244 PHE C C 177.826 0.3 1 1050 245 245 LYS H H 8.094 0.03 1 1051 245 245 LYS C C 179.694 0.3 1 1052 245 245 LYS CA C 59.959 0.3 1 1053 245 245 LYS CB C 33.009 0.3 1 1054 245 245 LYS N N 120.488 0.3 1 1055 246 246 LYS H H 7.822 0.03 1 1056 246 246 LYS C C 177.81 0.3 1 1057 246 246 LYS CA C 59.759 0.3 1 1058 246 246 LYS CB C 32.609 0.3 1 1059 246 246 LYS N N 120.84 0.3 1 1060 247 247 ASP H H 7.747 0.03 1 1061 247 247 ASP C C 177.343 0.3 1 1062 247 247 ASP CA C 56.849 0.3 1 1063 247 247 ASP CB C 43.009 0.3 1 1064 247 247 ASP N N 117.221 0.3 1 1065 248 248 GLN H H 8.174 0.03 1 1066 248 248 GLN C C 177.285 0.3 1 1067 248 248 GLN CA C 55.389 0.3 1 1068 248 248 GLN CB C 30.169 0.3 1 1069 248 248 GLN N N 113.494 0.3 1 1070 249 249 GLY H H 7.729 0.03 1 1071 249 249 GLY C C 173.491 0.3 1 1072 249 249 GLY CA C 46.289 0.3 1 1073 249 249 GLY N N 108.748 0.3 1 1074 250 250 ILE H H 6.193 0.03 1 1075 250 250 ILE C C 173.876 0.3 1 1076 250 250 ILE CA C 59.685 0.3 1 1077 250 250 ILE CB C 42.779 0.3 1 1078 250 250 ILE N N 118.751 0.3 1 1079 251 251 ASP H H 8.892 0.03 1 1080 251 251 ASP C C 176.876 0.3 1 1081 251 251 ASP CA C 52.249 0.3 1 1082 251 251 ASP CB C 41.209 0.3 1 1083 251 251 ASP N N 128.01 0.3 1 1084 252 252 LEU H H 9.053 0.03 1 1085 252 252 LEU C C 176.935 0.3 1 1086 252 252 LEU CA C 56.819 0.3 1 1087 252 252 LEU CB C 42.559 0.3 1 1088 252 252 LEU N N 128.15 0.3 1 1089 253 253 ARG H H 8.055 0.03 1 1090 253 253 ARG C C 177.903 0.3 1 1091 253 253 ARG CA C 58.959 0.3 1 1092 253 253 ARG CB C 29.809 0.3 1 1093 253 253 ARG N N 115.26 0.3 1 1094 254 254 ASN H H 7.164 0.03 1 1095 254 254 ASN C C 173.701 0.3 1 1096 254 254 ASN CA C 53.149 0.3 1 1097 254 254 ASN CB C 38.809 0.3 1 1098 254 254 ASN N N 114.25 0.3 1 1099 255 255 ASP H H 7.905 0.03 1 1100 255 255 ASP C C 173.599 0.3 1 1101 255 255 ASP CA C 50.449 0.3 1 1102 255 255 ASP CB C 42.209 0.3 1 1103 255 255 ASP N N 122.541 0.3 1 1104 256 256 PRO C C 179.984 0.3 1 1105 256 256 PRO CA C 64.859 0.3 1 1106 256 256 PRO CB C 32.206 0.3 1 1107 257 257 LEU H H 7.628 0.03 1 1108 257 257 LEU C C 179.328 0.3 1 1109 257 257 LEU CA C 57.854 0.3 1 1110 257 257 LEU CB C 41.018 0.3 1 1111 257 257 LEU N N 120.5 0.3 1 1112 258 258 ALA H H 7.564 0.03 1 1113 258 258 ALA C C 180.67 0.3 1 1114 258 258 ALA CA C 54.979 0.3 1 1115 258 258 ALA CB C 18.999 0.3 1 1116 258 258 ALA N N 124.419 0.3 1 1117 259 259 MET H H 8.123 0.03 1 1118 259 259 MET C C 180.254 0.3 1 1119 259 259 MET CA C 56.089 0.3 1 1120 259 259 MET CB C 29.169 0.3 1 1121 259 259 MET N N 114.063 0.3 1 1122 260 260 GLN H H 7.856 0.03 1 1123 260 260 GLN C C 179.262 0.3 1 1124 260 260 GLN CA C 59.241 0.3 1 1125 260 260 GLN CB C 28.625 0.3 1 1126 260 260 GLN N N 122.68 0.3 1 1127 261 261 ARG H H 7.953 0.03 1 1128 261 261 ARG C C 180.32 0.3 1 1129 261 261 ARG CA C 59.878 0.3 1 1130 261 261 ARG CB C 30.989 0.3 1 1131 261 261 ARG N N 120.478 0.3 1 1132 262 262 LEU H H 8.917 0.03 1 1133 262 262 LEU C C 177.749 0.3 1 1134 262 262 LEU CA C 57.722 0.3 1 1135 262 262 LEU CB C 42.807 0.3 1 1136 262 262 LEU N N 122.507 0.3 1 1137 263 263 LYS H H 8.043 0.03 1 1138 263 263 LYS C C 178.434 0.3 1 1139 263 263 LYS CA C 59.9 0.3 1 1140 263 263 LYS CB C 31.874 0.3 1 1141 263 263 LYS N N 121.548 0.3 1 1142 264 264 GLU H H 7.084 0.03 1 1143 264 264 GLU C C 179.085 0.3 1 1144 264 264 GLU CA C 58.934 0.3 1 1145 264 264 GLU CB C 30.124 0.3 1 1146 264 264 GLU N N 118.442 0.3 1 1147 265 265 ALA H H 8.014 0.03 1 1148 265 265 ALA C C 180.554 0.3 1 1149 265 265 ALA CA C 54.243 0.3 1 1150 265 265 ALA CB C 19.812 0.3 1 1151 265 265 ALA N N 121.671 0.3 1 1152 266 266 ALA H H 9.239 0.03 1 1153 266 266 ALA C C 178.394 0.3 1 1154 266 266 ALA CA C 55.379 0.3 1 1155 266 266 ALA CB C 19.029 0.3 1 1156 266 266 ALA N N 122.669 0.3 1 1157 267 267 GLU H H 7.466 0.03 1 1158 267 267 GLU C C 178.02 0.3 1 1159 267 267 GLU CA C 59.889 0.3 1 1160 267 267 GLU CB C 28.524 0.3 1 1161 267 267 GLU N N 118.966 0.3 1 1162 268 268 LYS H H 7.37 0.03 1 1163 268 268 LYS C C 178.598 0.3 1 1164 268 268 LYS CA C 59.759 0.3 1 1165 268 268 LYS CB C 32.709 0.3 1 1166 268 268 LYS N N 117.742 0.3 1 1167 269 269 ALA H H 8.009 0.03 1 1168 269 269 ALA C C 178.511 0.3 1 1169 269 269 ALA CA C 54.686 0.3 1 1170 269 269 ALA CB C 17.876 0.3 1 1171 269 269 ALA N N 122.037 0.3 1 1172 270 270 LYS H H 8.162 0.03 1 1173 270 270 LYS C C 178.889 0.3 1 1174 270 270 LYS CA C 60.359 0.3 1 1175 270 270 LYS CB C 31.109 0.3 1 1176 270 270 LYS N N 118.656 0.3 1 1177 271 271 ILE H H 7.817 0.03 1 1178 271 271 ILE CA C 66.113 0.3 1 1179 271 271 ILE CB C 37.778 0.3 1 1180 271 271 ILE N N 119.896 0.3 1 1181 274 274 SER C C 173.064 0.3 1 1182 274 274 SER CA C 60.643 0.3 1 1183 274 274 SER CB C 62.463 0.3 1 1184 275 275 SER H H 7.758 0.03 1 1185 275 275 SER C C 172.981 0.3 1 1186 275 275 SER CA C 58.983 0.3 1 1187 275 275 SER CB C 64.677 0.3 1 1188 275 275 SER N N 113.205 0.3 1 1189 276 276 ALA H H 8.233 0.03 1 1190 276 276 ALA CA C 51.279 0.3 1 1191 276 276 ALA CB C 21.899 0.3 1 1192 276 276 ALA N N 126.142 0.3 1 1193 277 277 GLN C C 176.409 0.3 1 1194 277 277 GLN CA C 56.577 0.3 1 1195 277 277 GLN CB C 30.074 0.3 1 1196 278 278 GLN H H 7.497 0.03 1 1197 278 278 GLN C C 172.499 0.3 1 1198 278 278 GLN CA C 55.389 0.3 1 1199 278 278 GLN CB C 30.869 0.3 1 1200 278 278 GLN N N 115.189 0.3 1 1201 279 279 THR H H 8.526 0.03 1 1202 279 279 THR C C 170.121 0.3 1 1203 279 279 THR CA C 60.729 0.3 1 1204 279 279 THR CB C 69.909 0.3 1 1205 279 279 THR N N 116.562 0.3 1 1206 280 280 ASP H H 7.926 0.03 1 1207 280 280 ASP C C 175.737 0.3 1 1208 280 280 ASP CA C 53.549 0.3 1 1209 280 280 ASP CB C 43.209 0.3 1 1210 280 280 ASP N N 123.505 0.3 1 1211 281 281 VAL H H 9.244 0.03 1 1212 281 281 VAL C C 173.485 0.3 1 1213 281 281 VAL CA C 63.139 0.3 1 1214 281 281 VAL CB C 31.099 0.3 1 1215 281 281 VAL N N 126.596 0.3 1 1216 282 282 ASN H H 8.406 0.03 1 1217 282 282 ASN C C 174.109 0.3 1 1218 282 282 ASN CA C 51.749 0.3 1 1219 282 282 ASN CB C 40.309 0.3 1 1220 282 282 ASN N N 127.965 0.3 1 1221 283 283 LEU H H 8.834 0.03 1 1222 283 283 LEU C C 172.699 0.3 1 1223 283 283 LEU CA C 50.828 0.3 1 1224 283 283 LEU CB C 44.559 0.3 1 1225 283 283 LEU N N 124.966 0.3 1 1226 284 284 PRO C C 177.518 0.3 1 1227 284 284 PRO CA C 62.313 0.3 1 1228 284 284 PRO CB C 32.759 0.3 1 1229 285 285 TYR H H 11.969 0.03 1 1230 285 285 TYR C C 176.853 0.3 1 1231 285 285 TYR CA C 59.149 0.3 1 1232 285 285 TYR CB C 34.909 0.3 1 1233 285 285 TYR N N 126.975 0.3 1 1234 286 286 ILE H H 7.969 0.03 1 1235 286 286 ILE C C 174.016 0.3 1 1236 286 286 ILE CA C 60.169 0.3 1 1237 286 286 ILE CB C 38.379 0.3 1 1238 286 286 ILE N N 121.033 0.3 1 1239 287 287 THR H H 7.351 0.03 1 1240 287 287 THR C C 171.681 0.3 1 1241 287 287 THR CA C 60.929 0.3 1 1242 287 287 THR CB C 67.509 0.3 1 1243 287 287 THR N N 112.709 0.3 1 1244 288 288 ALA H H 8.37 0.03 1 1245 288 288 ALA C C 175.606 0.3 1 1246 288 288 ALA CA C 52.379 0.3 1 1247 288 288 ALA CB C 22.199 0.3 1 1248 288 288 ALA N N 124.433 0.3 1 1249 289 289 ASP H H 8.019 0.03 1 1250 289 289 ASP C C 177.399 0.3 1 1251 289 289 ASP CA C 52.949 0.3 1 1252 289 289 ASP CB C 42.109 0.3 1 1253 289 289 ASP N N 122.7 0.3 1 1254 290 290 ALA C C 179.386 0.3 1 1255 290 290 ALA CA C 55.129 0.3 1 1256 290 290 ALA CB C 18.832 0.3 1 1257 291 291 THR H H 8.525 0.03 1 1258 291 291 THR C C 174.892 0.3 1 1259 291 291 THR CA C 62.929 0.3 1 1260 291 291 THR CB C 70.009 0.3 1 1261 291 291 THR N N 109.405 0.3 1 1262 292 292 GLY H H 7.765 0.03 1 1263 292 292 GLY C C 171.199 0.3 1 1264 292 292 GLY CA C 44.489 0.3 1 1265 292 292 GLY N N 111.772 0.3 1 1266 293 293 PRO C C 175.826 0.3 1 1267 293 293 PRO CA C 62.535 0.3 1 1268 293 293 PRO CB C 33.645 0.3 1 1269 294 294 LYS H H 8.123 0.03 1 1270 294 294 LYS C C 174.109 0.3 1 1271 294 294 LYS CA C 52.959 0.3 1 1272 294 294 LYS CB C 35.309 0.3 1 1273 294 294 LYS N N 119.015 0.3 1 1274 295 295 HIS H H 8.46 0.03 1 1275 295 295 HIS C C 174.892 0.3 1 1276 295 295 HIS CA C 54.349 0.3 1 1277 295 295 HIS CB C 33.709 0.3 1 1278 295 295 HIS N N 120.091 0.3 1 1279 296 296 MET H H 8.119 0.03 1 1280 296 296 MET C C 175.184 0.3 1 1281 296 296 MET CA C 54.789 0.3 1 1282 296 296 MET CB C 35.569 0.3 1 1283 296 296 MET N N 123.519 0.3 1 1284 297 297 ASN H H 9.289 0.03 1 1285 297 297 ASN C C 173.331 0.3 1 1286 297 297 ASN CA C 54.049 0.3 1 1287 297 297 ASN CB C 39.709 0.3 1 1288 297 297 ASN N N 129.791 0.3 1 1289 298 298 ILE H H 8.439 0.03 1 1290 298 298 ILE C C 173.798 0.3 1 1291 298 298 ILE CA C 60.869 0.3 1 1292 298 298 ILE CB C 42.879 0.3 1 1293 298 298 ILE N N 125.357 0.3 1 1294 299 299 LYS H H 8.53 0.03 1 1295 299 299 LYS C C 176.176 0.3 1 1296 299 299 LYS CA C 55.859 0.3 1 1297 299 299 LYS CB C 32.809 0.3 1 1298 299 299 LYS N N 130.141 0.3 1 1299 300 300 VAL H H 9.034 0.03 1 1300 300 300 VAL C C 175.242 0.3 1 1301 300 300 VAL CA C 61.739 0.3 1 1302 300 300 VAL CB C 34.299 0.3 1 1303 300 300 VAL N N 127.093 0.3 1 1304 301 301 THR H H 7.756 0.03 1 1305 301 301 THR C C 175.024 0.3 1 1306 301 301 THR CA C 60.029 0.3 1 1307 301 301 THR CB C 70.92 0.3 1 1308 301 301 THR N N 116.155 0.3 1 1309 302 302 ARG H H 8.75 0.03 1 1310 302 302 ARG C C 177.46 0.3 1 1311 302 302 ARG CA C 60.259 0.3 1 1312 302 302 ARG CB C 30.009 0.3 1 1313 302 302 ARG N N 123.873 0.3 1 1314 303 303 ALA H H 8.418 0.03 1 1315 303 303 ALA C C 180.612 0.3 1 1316 303 303 ALA CA C 55.379 0.3 1 1317 303 303 ALA CB C 18.199 0.3 1 1318 303 303 ALA N N 120.77 0.3 1 1319 304 304 LYS H H 7.971 0.03 1 1320 304 304 LYS C C 178.995 0.3 1 1321 304 304 LYS CA C 57.359 0.3 1 1322 304 304 LYS CB C 30.309 0.3 1 1323 304 304 LYS N N 120.914 0.3 1 1324 305 305 LEU H H 7.91 0.03 1 1325 305 305 LEU C C 178.132 0.3 1 1326 305 305 LEU CA C 58.859 0.3 1 1327 305 305 LEU CB C 41.73 0.3 1 1328 305 305 LEU N N 121.086 0.3 1 1329 306 306 GLU H H 8.79 0.03 1 1330 306 306 GLU C C 178.531 0.3 1 1331 306 306 GLU CA C 60.399 0.3 1 1332 306 306 GLU CB C 28.85 0.3 1 1333 306 306 GLU N N 117.053 0.3 1 1334 307 307 SER H H 7.646 0.03 1 1335 307 307 SER CA C 61.219 0.3 1 1336 307 307 SER CB C 63.287 0.3 1 1337 307 307 SER N N 113.443 0.3 1 1338 308 308 LEU C C 179.153 0.3 1 1339 308 308 LEU CA C 56.84 0.3 1 1340 308 308 LEU CB C 43.756 0.3 1 1341 309 309 VAL H H 7.383 0.03 1 1342 309 309 VAL C C 176.686 0.3 1 1343 309 309 VAL CA C 60.439 0.3 1 1344 309 309 VAL CB C 32.699 0.3 1 1345 309 309 VAL N N 106.505 0.3 1 1346 310 310 GLU H H 7.654 0.03 1 1347 310 310 GLU C C 177.067 0.3 1 1348 310 310 GLU CA C 61.189 0.3 1 1349 310 310 GLU CB C 28.816 0.3 1 1350 310 310 GLU N N 126.978 0.3 1 1351 311 311 ASP H H 8.689 0.03 1 1352 311 311 ASP C C 178.598 0.3 1 1353 311 311 ASP CA C 56.849 0.3 1 1354 311 311 ASP CB C 39.409 0.3 1 1355 311 311 ASP N N 115.029 0.3 1 1356 312 312 LEU H H 7.134 0.03 1 1357 312 312 LEU C C 178.044 0.3 1 1358 312 312 LEU CA C 57.419 0.3 1 1359 312 312 LEU CB C 41.659 0.3 1 1360 312 312 LEU N N 122.102 0.3 1 1361 313 313 VAL H H 7.236 0.03 1 1362 313 313 VAL C C 180.437 0.3 1 1363 313 313 VAL CA C 67.239 0.3 1 1364 313 313 VAL CB C 31.499 0.3 1 1365 313 313 VAL N N 117.536 0.3 1 1366 314 314 ASN H H 8.565 0.03 1 1367 314 314 ASN C C 178.686 0.3 1 1368 314 314 ASN CA C 56.149 0.3 1 1369 314 314 ASN CB C 37.309 0.3 1 1370 314 314 ASN N N 121.247 0.3 1 1371 315 315 ARG H H 7.882 0.03 1 1372 315 315 ARG C C 177.985 0.3 1 1373 315 315 ARG CA C 59.259 0.3 1 1374 315 315 ARG CB C 30.409 0.3 1 1375 315 315 ARG N N 122.892 0.3 1 1376 316 316 SER H H 7.322 0.03 1 1377 316 316 SER C C 172.207 0.3 1 1378 316 316 SER CA C 60.149 0.3 1 1379 316 316 SER CB C 62.909 0.3 1 1380 316 316 SER N N 115.379 0.3 1 1381 317 317 ILE H H 7.02 0.03 1 1382 317 317 ILE C C 178.176 0.3 1 1383 317 317 ILE CA C 61.069 0.3 1 1384 317 317 ILE CB C 36.079 0.3 1 1385 317 317 ILE N N 119.838 0.3 1 1386 318 318 GLU H H 7.298 0.03 1 1387 318 318 GLU CA C 61.289 0.3 1 1388 318 318 GLU CB C 26.669 0.3 1 1389 318 318 GLU N N 119.35 0.3 1 1390 319 319 PRO C C 180.073 0.3 1 1391 320 320 LEU H H 7.645 0.03 1 1392 320 320 LEU C C 177.885 0.3 1 1393 320 320 LEU CA C 58.571 0.3 1 1394 320 320 LEU N N 117.941 0.3 1 1395 321 321 LYS H H 7.528 0.03 1 1396 321 321 LYS C C 180.079 0.3 1 1397 321 321 LYS CA C 60.071 0.3 1 1398 321 321 LYS CB C 32.587 0.3 1 1399 321 321 LYS N N 117.841 0.3 1 1400 322 322 VAL H H 7.328 0.03 1 1401 322 322 VAL C C 177.089 0.3 1 1402 322 322 VAL CA C 66.512 0.3 1 1403 322 322 VAL CB C 32.002 0.3 1 1404 322 322 VAL N N 120.35 0.3 1 1405 323 323 ALA H H 8.152 0.03 1 1406 323 323 ALA C C 179.579 0.3 1 1407 323 323 ALA CA C 55.074 0.3 1 1408 323 323 ALA CB C 17.457 0.3 1 1409 323 323 ALA N N 122.791 0.3 1 1410 324 324 LEU H H 7.742 0.03 1 1411 324 324 LEU C C 178.783 0.3 1 1412 324 324 LEU CA C 58.819 0.3 1 1413 324 324 LEU CB C 40.975 0.3 1 1414 324 324 LEU N N 115.921 0.3 1 1415 325 325 GLN H H 7.635 0.03 1 1416 325 325 GLN CA C 59.128 0.3 1 1417 325 325 GLN CB C 28.475 0.3 1 1418 325 325 GLN N N 119.345 0.3 1 1419 326 326 ASP C C 178.336 0.3 1 1420 327 327 ALA H H 7.881 0.03 1 1421 327 327 ALA C C 176.794 0.3 1 1422 327 327 ALA CA C 52.089 0.3 1 1423 327 327 ALA CB C 19.194 0.3 1 1424 327 327 ALA N N 120.279 0.3 1 1425 328 328 GLY H H 7.892 0.03 1 1426 328 328 GLY C C 174.6 0.3 1 1427 328 328 GLY CA C 45.989 0.3 1 1428 328 328 GLY N N 109.299 0.3 1 1429 329 329 LEU H H 7.907 0.03 1 1430 329 329 LEU C C 175.684 0.3 1 1431 329 329 LEU CA C 53.419 0.3 1 1432 329 329 LEU CB C 46.359 0.3 1 1433 329 329 LEU N N 119.374 0.3 1 1434 330 330 SER H H 9.202 0.03 1 1435 330 330 SER C C 176.425 0.3 1 1436 330 330 SER CA C 56.749 0.3 1 1437 330 330 SER CB C 66.209 0.3 1 1438 330 330 SER N N 116.589 0.3 1 1439 331 331 VAL H H 8.672 0.03 1 1440 331 331 VAL C C 178.219 0.3 1 1441 331 331 VAL CA C 66.748 0.3 1 1442 331 331 VAL CB C 31.699 0.3 1 1443 331 331 VAL N N 119.215 0.3 1 1444 332 332 SER H H 7.653 0.03 1 1445 332 332 SER C C 174.966 0.3 1 1446 332 332 SER CA C 60.149 0.3 1 1447 332 332 SER CB C 62.909 0.3 1 1448 332 332 SER N N 113.97 0.3 1 1449 333 333 ASP H H 7.71 0.03 1 1450 333 333 ASP C C 174.82 0.3 1 1451 333 333 ASP CA C 55.749 0.3 1 1452 333 333 ASP CB C 43.407 0.3 1 1453 333 333 ASP N N 120.302 0.3 1 1454 334 334 ILE H H 7.089 0.03 1 1455 334 334 ILE C C 175.102 0.3 1 1456 334 334 ILE CA C 58.056 0.3 1 1457 334 334 ILE CB C 35.37 0.3 1 1458 334 334 ILE N N 119.187 0.3 1 1459 335 335 ASP H H 9.054 0.03 1 1460 335 335 ASP C C 175.627 0.3 1 1461 335 335 ASP CA C 57.549 0.3 1 1462 335 335 ASP CB C 43.122 0.3 1 1463 335 335 ASP N N 127.649 0.3 1 1464 336 336 ASP H H 7.095 0.03 1 1465 336 336 ASP C C 173.024 0.3 1 1466 336 336 ASP CA C 53.349 0.3 1 1467 336 336 ASP CB C 46.509 0.3 1 1468 336 336 ASP N N 115.12 0.3 1 1469 337 337 VAL H H 8.928 0.03 1 1470 337 337 VAL CA C 60.509 0.3 1 1471 337 337 VAL CB C 33.599 0.3 1 1472 337 337 VAL N N 121.875 0.3 1 1473 338 338 ILE C C 173.728 0.3 1 1474 338 338 ILE CA C 58.949 0.3 1 1475 338 338 ILE CB C 39.57 0.3 1 1476 339 339 LEU H H 8.765 0.03 1 1477 339 339 LEU C C 175.318 0.3 1 1478 339 339 LEU CA C 53.741 0.3 1 1479 339 339 LEU CB C 41.325 0.3 1 1480 339 339 LEU N N 126.747 0.3 1 1481 340 340 VAL H H 9.551 0.03 1 1482 340 340 VAL C C 172.382 0.3 1 1483 340 340 VAL CA C 61.14 0.3 1 1484 340 340 VAL CB C 35.337 0.3 1 1485 340 340 VAL N N 124.476 0.3 1 1486 341 341 GLY H H 7.733 0.03 1 1487 341 341 GLY C C 177.343 0.3 1 1488 341 341 GLY CA C 42.005 0.3 1 1489 341 341 GLY N N 109.979 0.3 1 1490 342 342 GLY H H 9.379 0.03 1 1491 342 342 GLY C C 174.081 0.3 1 1492 342 342 GLY CA C 47. 0.3 1 1493 342 342 GLY N N 116.438 0.3 1 1494 343 343 GLN H H 6.619 0.03 1 1495 343 343 GLN C C 178.336 0.3 1 1496 343 343 GLN CA C 55.273 0.3 1 1497 343 343 GLN CB C 29.869 0.3 1 1498 343 343 GLN N N 116.218 0.3 1 1499 344 344 THR H H 7.627 0.03 1 1500 344 344 THR C C 173.491 0.3 1 1501 344 344 THR CA C 63.785 0.3 1 1502 344 344 THR CB C 69.609 0.3 1 1503 344 344 THR N N 109.348 0.3 1 1504 345 345 ARG H H 6.814 0.03 1 1505 345 345 ARG C C 176.66 0.3 1 1506 345 345 ARG CA C 57.559 0.3 1 1507 345 345 ARG CB C 30.123 0.3 1 1508 345 345 ARG N N 117.543 0.3 1 1509 346 346 MET H H 6.808 0.03 1 1510 346 346 MET C C 174.999 0.3 1 1511 346 346 MET CA C 54.589 0.3 1 1512 346 346 MET CB C 33.369 0.3 1 1513 346 346 MET N N 119.379 0.3 1 1514 347 347 PRO C C 178.919 0.3 1 1515 347 347 PRO CA C 66.851 0.3 1 1516 347 347 PRO CB C 31.653 0.3 1 1517 348 348 MET H H 9.24 0.03 1 1518 348 348 MET C C 178.526 0.3 1 1519 348 348 MET CA C 60.089 0.3 1 1520 348 348 MET CB C 33.569 0.3 1 1521 348 348 MET N N 117.244 0.3 1 1522 349 349 VAL H H 7.103 0.03 1 1523 349 349 VAL C C 176.468 0.3 1 1524 349 349 VAL CA C 67.039 0.3 1 1525 349 349 VAL CB C 31.699 0.3 1 1526 349 349 VAL N N 117.99 0.3 1 1527 350 350 GLN H H 6.984 0.03 1 1528 350 350 GLN C C 178.511 0.3 1 1529 350 350 GLN CA C 60.289 0.3 1 1530 350 350 GLN CB C 27.269 0.3 1 1531 350 350 GLN N N 116.74 0.3 1 1532 351 351 LYS H H 8.35 0.03 1 1533 351 351 LYS C C 178.871 0.3 1 1534 351 351 LYS CA C 59.159 0.3 1 1535 351 351 LYS CB C 32.909 0.3 1 1536 351 351 LYS N N 118.825 0.3 1 1537 352 352 LYS H H 8.019 0.03 1 1538 352 352 LYS CA C 58.72 0.3 1 1539 352 352 LYS CB C 31.538 0.3 1 1540 352 352 LYS N N 119.793 0.3 1 1541 353 353 VAL C C 177.823 0.3 1 1542 353 353 VAL CA C 67.82 0.3 1 1543 353 353 VAL CB C 31.965 0.3 1 1544 354 354 ALA H H 8.083 0.03 1 1545 354 354 ALA C C 181.777 0.3 1 1546 354 354 ALA CA C 54.907 0.3 1 1547 354 354 ALA CB C 18.763 0.3 1 1548 354 354 ALA N N 123.02 0.3 1 1549 355 355 GLU H H 8.358 0.03 1 1550 355 355 GLU CA C 59.048 0.3 1 1551 355 355 GLU CB C 30.049 0.3 1 1552 355 355 GLU N N 119.084 0.3 1 1553 356 356 PHE C C 177.019 0.3 1 1554 356 356 PHE CA C 61.861 0.3 1 1555 356 356 PHE CB C 38.779 0.3 1 1556 357 357 PHE H H 8.093 0.03 1 1557 357 357 PHE C C 176.347 0.3 1 1558 357 357 PHE CA C 60.975 0.3 1 1559 357 357 PHE CB C 39.548 0.3 1 1560 357 357 PHE N N 112.465 0.3 1 1561 358 358 GLY H H 8.2 0.03 1 1562 358 358 GLY C C 173.558 0.3 1 1563 358 358 GLY CA C 45.973 0.3 1 1564 358 358 GLY N N 109.899 0.3 1 1565 359 359 LYS H H 7.453 0.03 1 1566 359 359 LYS CA C 54.421 0.3 1 1567 359 359 LYS CB C 34.678 0.3 1 1568 359 359 LYS N N 116.613 0.3 1 1569 363 363 LYS C C 176.719 0.3 1 1570 363 363 LYS CA C 56.337 0.3 1 1571 363 363 LYS CB C 32.649 0.3 1 1572 364 364 ASP H H 8.728 0.03 1 1573 364 364 ASP C C 175.339 0.3 1 1574 364 364 ASP CA C 53.892 0.3 1 1575 364 364 ASP CB C 39.332 0.3 1 1576 364 364 ASP N N 117.704 0.3 1 1577 365 365 VAL H H 6.828 0.03 1 1578 365 365 VAL CA C 61.597 0.3 1 1579 365 365 VAL CB C 33.403 0.3 1 1580 365 365 VAL N N 119.427 0.3 1 1581 367 367 PRO C C 178.136 0.3 1 1582 367 367 PRO CA C 64.616 0.3 1 1583 368 368 ASP H H 8.438 0.03 1 1584 368 368 ASP C C 177.221 0.3 1 1585 368 368 ASP CA C 55.938 0.3 1 1586 368 368 ASP CB C 42.154 0.3 1 1587 368 368 ASP N N 119.324 0.3 1 1588 369 369 GLU H H 7.145 0.03 1 1589 369 369 GLU C C 175.808 0.3 1 1590 369 369 GLU CA C 56.771 0.3 1 1591 369 369 GLU CB C 32.398 0.3 1 1592 369 369 GLU N N 118.128 0.3 1 1593 370 370 ALA H H 7.31 0.03 1 1594 370 370 ALA CA C 56.267 0.3 1 1595 370 370 ALA CB C 19.287 0.3 1 1596 370 370 ALA N N 119.768 0.3 1 1597 372 372 ALA C C 179.737 0.3 1 1598 372 372 ALA CA C 55.239 0.3 1 1599 372 372 ALA CB C 18.04 0.3 1 1600 373 373 ILE H H 7.97 0.03 1 1601 373 373 ILE C C 178.219 0.3 1 1602 373 373 ILE CA C 65.68 0.3 1 1603 373 373 ILE CB C 37.49 0.3 1 1604 373 373 ILE N N 116.73 0.3 1 1605 374 374 GLY H H 8.047 0.03 1 1606 374 374 GLY C C 175.884 0.3 1 1607 374 374 GLY CA C 47.289 0.3 1 1608 374 374 GLY N N 107.455 0.3 1 1609 375 375 ALA H H 7.917 0.03 1 1610 375 375 ALA C C 179.083 0.3 1 1611 375 375 ALA CA C 55.479 0.3 1 1612 375 375 ALA CB C 17.799 0.3 1 1613 375 375 ALA N N 124.103 0.3 1 1614 376 376 ALA H H 8.124 0.03 1 1615 376 376 ALA C C 180.601 0.3 1 1616 376 376 ALA CA C 55.079 0.3 1 1617 376 376 ALA CB C 17.235 0.3 1 1618 376 376 ALA N N 122.151 0.3 1 1619 377 377 VAL H H 8.493 0.03 1 1620 377 377 VAL C C 178.082 0.3 1 1621 377 377 VAL CA C 67.065 0.3 1 1622 377 377 VAL CB C 31.103 0.3 1 1623 377 377 VAL N N 123.021 0.3 1 1624 378 378 GLN H H 8.068 0.03 1 1625 378 378 GLN C C 179.628 0.3 1 1626 378 378 GLN CA C 58.536 0.3 1 1627 378 378 GLN CB C 27.651 0.3 1 1628 378 378 GLN N N 119.338 0.3 1 1629 379 379 GLY H H 8.287 0.03 1 1630 379 379 GLY C C 174.313 0.3 1 1631 379 379 GLY CA C 47.873 0.3 1 1632 379 379 GLY N N 109.975 0.3 1 1633 380 380 GLY H H 8.32 0.03 1 1634 380 380 GLY CA C 46.099 0.3 1 1635 380 380 GLY N N 109.787 0.3 1 1636 381 381 VAL C C 179.92 0.3 1 1637 381 381 VAL CA C 65.471 0.3 1 1638 381 381 VAL CB C 32.199 0.3 1 1639 382 382 LEU H H 7.526 0.03 1 1640 382 382 LEU C C 179.458 0.3 1 1641 382 382 LEU CA C 57.504 0.3 1 1642 382 382 LEU CB C 41.398 0.3 1 1643 382 382 LEU N N 120.348 0.3 1 1644 383 383 THR H H 7.898 0.03 1 1645 383 383 THR C C 175.783 0.3 1 1646 383 383 THR CA C 62.826 0.3 1 1647 383 383 THR CB C 69.536 0.3 1 1648 383 383 THR N N 108.852 0.3 1 1649 384 384 GLY H H 7.575 0.03 1 1650 384 384 GLY C C 173.539 0.3 1 1651 384 384 GLY CA C 45.25 0.3 1 1652 384 384 GLY N N 110.46 0.3 1 1653 385 385 ASP H H 8.048 0.03 1 1654 385 385 ASP C C 175.686 0.3 1 1655 385 385 ASP CA C 56.77 0.3 1 1656 385 385 ASP CB C 42.652 0.3 1 1657 385 385 ASP N N 120.9 0.3 1 1658 386 386 VAL H H 7.086 0.03 1 1659 386 386 VAL C C 175.249 0.3 1 1660 386 386 VAL CA C 61.487 0.3 1 1661 386 386 VAL CB C 33.735 0.3 1 1662 386 386 VAL N N 119.882 0.3 1 1663 387 387 LYS H H 8.539 0.03 1 1664 387 387 LYS C C 175.826 0.3 1 1665 387 387 LYS CA C 55.959 0.3 1 1666 387 387 LYS CB C 34.198 0.3 1 1667 387 387 LYS N N 126.276 0.3 1 1668 388 388 ASP H H 8.32 0.03 1 1669 388 388 ASP C C 174.836 0.3 1 1670 388 388 ASP CA C 54.942 0.3 1 1671 388 388 ASP CB C 40.28 0.3 1 1672 388 388 ASP N N 117.302 0.3 1 1673 389 389 VAL H H 7.56 0.03 1 1674 389 389 VAL CA C 62.073 0.3 1 1675 389 389 VAL CB C 35.506 0.3 1 1676 389 389 VAL N N 118.993 0.3 1 1677 390 390 LEU C C 174.984 0.3 1 1678 390 390 LEU CA C 54.482 0.3 1 1679 390 390 LEU CB C 44.04 0.3 1 1680 391 391 LEU H H 8.302 0.03 1 1681 391 391 LEU C C 175.763 0.3 1 1682 391 391 LEU CA C 54.89 0.3 1 1683 391 391 LEU CB C 41.733 0.3 1 1684 391 391 LEU N N 126.931 0.3 1 1685 392 392 LEU H H 8.143 0.03 1 1686 392 392 LEU CA C 56.667 0.3 1 1687 392 392 LEU CB C 43.327 0.3 1 1688 392 392 LEU N N 131.699 0.3 1 stop_ save_