data_4353 ####################### # Entry information # ####################### save_entry_information _Entry.Sf_category entry_information _Entry.Sf_framecode entry_information _Entry.ID 4353 _Entry.Title ; 1H, 13C, and 15N Resonance Assignments of C-terminal Domain of MutY ; _Entry.Type macromolecule _Entry.Version_type original _Entry.Submission_date 1999-06-04 _Entry.Accession_date 1999-06-04 _Entry.Last_release_date 1999-09-15 _Entry.Original_release_date 1999-09-15 _Entry.Origination author _Entry.NMR_STAR_version 3.1.1.61 _Entry.Original_NMR_STAR_version 2.1 _Entry.Experimental_method NMR _Entry.Experimental_method_subtype . _Entry.Details . _Entry.BMRB_internal_directory_name . loop_ _Entry_author.Ordinal _Entry_author.Given_name _Entry_author.Family_name _Entry_author.First_initial _Entry_author.Middle_initials _Entry_author.Family_title _Entry_author.Entry_ID 1 David Volk . E . 4353 2 Varatharasa Thiviyanathan . . . 4353 3 Paul House . G . 4353 4 Stephen Lloyd . . . 4353 5 David Gorenstein . G . 4353 stop_ loop_ _Data_set.Type _Data_set.Count _Data_set.Entry_ID assigned_chemical_shifts 1 4353 stop_ loop_ _Datum.Type _Datum.Count _Datum.Entry_ID '13C chemical shifts' 344 4353 '15N chemical shifts' 101 4353 '1H chemical shifts' 420 4353 stop_ loop_ _Release.Release_number _Release.Format_type _Release.Format_version _Release.Date _Release.Submission_date _Release.Type _Release.Author _Release.Detail _Release.Entry_ID 1 . . 1999-09-15 1999-06-04 original author . 4353 stop_ save_ ############### # Citations # ############### save_entry_citation _Citation.Sf_category citations _Citation.Sf_framecode entry_citation _Citation.Entry_ID 4353 _Citation.ID 1 _Citation.Class 'entry citation' _Citation.CAS_abstract_code . _Citation.MEDLINE_UI_code . _Citation.DOI . _Citation.PubMed_ID . _Citation.Full_citation ; Volk, D. E., Thiviyanathan, V., House, P. G., Lloyd, S., and Gorenstein, D. G., "1H, 13C, and 15N Resonance Assignments of C-terminal Domain of MutY," J. Biomol. NMR, submitted. ; _Citation.Title '1H, 13C, and 15N Resonance Assignments of C-terminal Domain of MutY' _Citation.Status submitted _Citation.Type journal _Citation.Journal_abbrev 'J. Biomol. NMR' _Citation.Journal_name_full 'Journal of Biomolecular NMR' _Citation.Journal_volume . _Citation.Journal_issue . _Citation.Journal_ASTM . _Citation.Journal_ISSN . _Citation.Journal_CSD . _Citation.Book_title . _Citation.Book_chapter_title . _Citation.Book_volume . _Citation.Book_series . _Citation.Book_publisher . _Citation.Book_publisher_city . _Citation.Book_ISBN . _Citation.Conference_title . _Citation.Conference_site . _Citation.Conference_state_province . _Citation.Conference_country . _Citation.Conference_start_date . _Citation.Conference_end_date . _Citation.Conference_abstract_number . _Citation.Thesis_institution . _Citation.Thesis_institution_city . _Citation.Thesis_institution_country . _Citation.WWW_URL . _Citation.Page_first . _Citation.Page_last . _Citation.Year . _Citation.Details . loop_ _Citation_author.Ordinal _Citation_author.Given_name _Citation_author.Family_name _Citation_author.First_initial _Citation_author.Middle_initials _Citation_author.Family_title _Citation_author.Entry_ID _Citation_author.Citation_ID 1 David Volk . E . 4353 1 2 Varatharasa Thiviyanathan . . . 4353 1 3 Paul House . G . 4353 1 4 Stephen Lloyd . . . 4353 1 5 David Gorenstein . G . 4353 1 stop_ loop_ _Citation_keyword.Keyword _Citation_keyword.Entry_ID _Citation_keyword.Citation_ID '8-oxo Guanosine' 4353 1 'Adenine Glycosylase' 4353 1 'G:A mismatch' 4353 1 stop_ save_ save_ref_1 _Citation.Sf_category citations _Citation.Sf_framecode ref_1 _Citation.Entry_ID 4353 _Citation.ID 2 _Citation.Class 'reference citation' _Citation.CAS_abstract_code . _Citation.MEDLINE_UI_code . _Citation.DOI . _Citation.PubMed_ID 9287157 _Citation.Full_citation ; Manuel, R.C., & Lloyd, R.S., (1997) Biochemistry, 36, 11140-11152 ; _Citation.Title 'Cloning, overexpression, and biochemical characterization of the catalytic domain of MutY.' _Citation.Status published _Citation.Type journal _Citation.Journal_abbrev Biochemistry _Citation.Journal_name_full Biochemistry _Citation.Journal_volume 36 _Citation.Journal_issue 37 _Citation.Journal_ASTM . _Citation.Journal_ISSN 0006-2960 _Citation.Journal_CSD . _Citation.Book_title . _Citation.Book_chapter_title . _Citation.Book_volume . _Citation.Book_series . _Citation.Book_publisher . _Citation.Book_publisher_city . _Citation.Book_ISBN . _Citation.Conference_title . _Citation.Conference_site . _Citation.Conference_state_province . _Citation.Conference_country . _Citation.Conference_start_date . _Citation.Conference_end_date . _Citation.Conference_abstract_number . _Citation.Thesis_institution . _Citation.Thesis_institution_city . _Citation.Thesis_institution_country . _Citation.WWW_URL . _Citation.Page_first 11140 _Citation.Page_last 11152 _Citation.Year 1997 _Citation.Details ; Proteolysis of MutY with trypsin indicated that this DNA mismatch repair enzyme could exist as two modules and that the N-terminal domain (Met1-Lys225), designated as p26, could serve as the catalytic domain [Manuel et al. (1996) J. Biol. Chem. 271, 16218-16226]. In this study, the p26 domain has been cloned, overproduced, and purified to homogeneity. Synthetic DNA duplexes containing mismatches, generated with regular bases and nucleotide analogs containing altered functional groups, have been used to characterize the substrate specificity and mismatch repair efficiency of p26. In general, p26 recognized and cleaved most of the substrates which were catalyzed by the intact protein. However, p26 displayed enhanced specificity for DNA containing an inosine. guanine mismatch, and the specificity constant (Kcat/Km) was 2-fold higher. The truncated MutY was able to cleave DNA containing an abasic site with equal efficiency. Dissociation constants (Kd) were obtained for p26 on noncleavable DNA substrates containing a tetrahydrofuran (abasic site analog) or a reduced abasic site. p26 bound these substrates with high specificity, and the Kd values were 3-fold higher when compared to the intact MutY. p26 contains both DNA glycosylase and AP lyase activities, and we provide evidence for a reaction mechanism that proceeds through an imino intermediate. Thus, we have shown for the first time that deletion of 125 amino acids at the C-terminus of MutY generates a stable catalytic domain which retains the functional identity of the intact protein. ; loop_ _Citation_author.Ordinal _Citation_author.Given_name _Citation_author.Family_name _Citation_author.First_initial _Citation_author.Middle_initials _Citation_author.Family_title _Citation_author.Entry_ID _Citation_author.Citation_ID 1 'R C' Manuel R. C. . 4353 2 2 'R S' Lloyd R. S. . 4353 2 stop_ save_ ############################################# # Molecular system (assembly) description # ############################################# save_system _Assembly.Sf_category assembly _Assembly.Sf_framecode system _Assembly.Entry_ID 4353 _Assembly.ID 1 _Assembly.Name 'p13 c-terminal domain' _Assembly.BMRB_code . _Assembly.Number_of_components . _Assembly.Organic_ligands . _Assembly.Metal_ions . _Assembly.Non_standard_bonds . _Assembly.Ambiguous_conformational_states . _Assembly.Ambiguous_chem_comp_sites . _Assembly.Molecules_in_chemical_exchange . _Assembly.Paramagnetic no _Assembly.Thiol_state . _Assembly.Molecular_mass . _Assembly.Enzyme_commission_number . _Assembly.Details ; * References for biological significance of the protein: -Noll, D.M., Gogos, A., Granek, J.A., & Clarke, N.D., (1999) Biochemistry, 38, 6374-6379. -Guan, Y., Manuel, R.C., Arvai, A.S., Parikh, S.S., Mol, C.D., Miller, J.H., & Lloyd, R.S., (1998) Nat. Struct. Biol, 5, 1058-1064 * References for the NMR experiment -Muhandiram, D.R., & Kay, L.E., (1994) J. Magn. Reson. B., 103, 203-216 ; _Assembly.DB_query_date . _Assembly.DB_query_revised_last_date . loop_ _Assembly_type.Type _Assembly_type.Entry_ID _Assembly_type.Assembly_ID monomer 4353 1 stop_ loop_ _Entity_assembly.ID _Entity_assembly.Entity_assembly_name _Entity_assembly.Entity_ID _Entity_assembly.Entity_label _Entity_assembly.Asym_ID _Entity_assembly.PDB_chain_ID _Entity_assembly.Experimental_data_reported _Entity_assembly.Physical_state _Entity_assembly.Conformational_isomer _Entity_assembly.Chemical_exchange_state _Entity_assembly.Magnetic_equivalence_group_code _Entity_assembly.Role _Entity_assembly.Details _Entity_assembly.Entry_ID _Entity_assembly.Assembly_ID 1 protein 1 $protein . . . native . . . . . 4353 1 stop_ loop_ _Assembly_common_name.Name _Assembly_common_name.Type _Assembly_common_name.Entry_ID _Assembly_common_name.Assembly_ID 'p13 c-terminal domain' system 4353 1 'p13 monomer' abbreviation 4353 1 stop_ loop_ _Assembly_bio_function.Biological_function _Assembly_bio_function.Entry_ID _Assembly_bio_function.Assembly_ID ; The MutY protein, of which the p13_c-terminal_domain is a fragment, functions as a DNA glycosylase (Adenine glycosylase) ; 4353 1 stop_ save_ #################################### # Biological polymers and ligands # #################################### save_protein _Entity.Sf_category entity _Entity.Sf_framecode protein _Entity.Entry_ID 4353 _Entity.ID 1 _Entity.BMRB_code . _Entity.Name 'p13 c-terminal domain' _Entity.Type polymer _Entity.Polymer_common_type . _Entity.Polymer_type polypeptide(L) _Entity.Polymer_type_details . _Entity.Polymer_strand_ID . _Entity.Polymer_seq_one_letter_code_can . _Entity.Polymer_seq_one_letter_code ; KQTLPERTGYFLLLQHEDEV LLAQRPPSGLWGGLYCFPQF ADEESLRQWLAQRQIAADML TQLTAFRHTFSHFHLDIVPM WLPVSSFTGCMDEGNALWYN LAQPPSVGLAAPVERLLQQL RTGAPV ; _Entity.Target_identifier . _Entity.Polymer_author_defined_seq . _Entity.Polymer_author_seq_details . _Entity.Ambiguous_conformational_states . _Entity.Ambiguous_chem_comp_sites . _Entity.Nstd_monomer . _Entity.Nstd_chirality . _Entity.Nstd_linkage . _Entity.Nonpolymer_comp_ID . _Entity.Nonpolymer_comp_label . _Entity.Number_of_monomers 126 _Entity.Number_of_nonpolymer_components . _Entity.Paramagnetic . _Entity.Thiol_state . _Entity.Src_method . _Entity.Parent_entity_ID . _Entity.Fragment . _Entity.Mutation . _Entity.EC_number . _Entity.Calc_isoelectric_point . _Entity.Formula_weight . _Entity.Formula_weight_exptl . _Entity.Formula_weight_exptl_meth . _Entity.Details . _Entity.DB_query_date . _Entity.DB_query_revised_last_date 2015-11-24 loop_ _Entity_db_link.Ordinal _Entity_db_link.Author_supplied _Entity_db_link.Database_code _Entity_db_link.Accession_code _Entity_db_link.Entry_mol_code _Entity_db_link.Entry_mol_name _Entity_db_link.Entry_experimental_method _Entity_db_link.Entry_structure_resolution _Entity_db_link.Entry_relation_type _Entity_db_link.Entry_details _Entity_db_link.Chimera_segment_ID _Entity_db_link.Seq_query_to_submitted_percent _Entity_db_link.Seq_subject_length _Entity_db_link.Seq_identity _Entity_db_link.Seq_positive _Entity_db_link.Seq_homology_expectation_val _Entity_db_link.Seq_align_begin _Entity_db_link.Seq_align_end _Entity_db_link.Seq_difference_details _Entity_db_link.Seq_alignment_details _Entity_db_link.Entry_ID _Entity_db_link.Entity_ID 1 no DBJ BAB37260 . "adenine glycosylase [Escherichia coli O157:H7 str. Sakai]" . . . . . 100.00 350 99.21 99.21 4.19e-83 . . . . 4353 1 2 no DBJ BAE77024 . "adenine DNA glycosylase [Escherichia coli str. K12 substr. W3110]" . . . . . 100.00 350 99.21 99.21 4.28e-83 . . . . 4353 1 3 no DBJ BAG66699 . "adenine DNA glycosylase [Escherichia coli O111:H-]" . . . . . 100.00 350 98.41 98.41 2.15e-82 . . . . 4353 1 4 no DBJ BAG78754 . "adenine glycosylase [Escherichia coli SE11]" . . . . . 100.00 350 99.21 99.21 4.37e-83 . . . . 4353 1 5 no DBJ BAI27248 . "adenine DNA glycosylase MutY [Escherichia coli O26:H11 str. 11368]" . . . . . 100.00 350 99.21 99.21 4.28e-83 . . . . 4353 1 6 no EMBL CAA36624 . "unnamed protein product [Escherichia coli K-12]" . . . . . 100.00 350 99.21 99.21 4.28e-83 . . . . 4353 1 7 no EMBL CAP77398 . "A/G-specific adenine glycosylase [Escherichia coli LF82]" . . . . . 100.00 350 97.62 98.41 1.27e-81 . . . . 4353 1 8 no EMBL CAQ33271 . "adenine glycosylase; G.C--> T.A transversions [Escherichia coli BL21(DE3)]" . . . . . 100.00 350 99.21 99.21 4.28e-83 . . . . 4353 1 9 no EMBL CAQ90396 . "adenine DNA glycosylase [Escherichia fergusonii ATCC 35469]" . . . . . 100.00 350 97.62 97.62 1.06e-81 . . . . 4353 1 10 no EMBL CAQ99909 . "adenine DNA glycosylase [Escherichia coli IAI1]" . . . . . 100.00 350 98.41 98.41 2.15e-82 . . . . 4353 1 11 no GB AAA69128 . "CG Site No. 18130; alternate name micA [Escherichia coli str. K-12 substr. MG1655]" . . . . . 100.00 350 99.21 99.21 4.28e-83 . . . . 4353 1 12 no GB AAA72957 . "A/G-specific adenine glycosylase [Escherichia coli]" . . . . . 100.00 350 99.21 99.21 4.28e-83 . . . . 4353 1 13 no GB AAC75998 . "adenine DNA glycosylase [Escherichia coli str. K-12 substr. MG1655]" . . . . . 100.00 350 99.21 99.21 4.28e-83 . . . . 4353 1 14 no GB AAG58092 . "adenine glycosylase; G.C --> T.A transversions [Escherichia coli O157:H7 str. EDL933]" . . . . . 100.00 350 99.21 99.21 4.19e-83 . . . . 4353 1 15 no GB AAN44439 . "adenine glycosylase [Shigella flexneri 2a str. 301]" . . . . . 100.00 350 98.41 98.41 2.22e-82 . . . . 4353 1 16 no REF NP_311864 . "adenine DNA glycosylase [Escherichia coli O157:H7 str. Sakai]" . . . . . 100.00 350 99.21 99.21 4.19e-83 . . . . 4353 1 17 no REF NP_417436 . "adenine DNA glycosylase [Escherichia coli str. K-12 substr. MG1655]" . . . . . 100.00 350 99.21 99.21 4.28e-83 . . . . 4353 1 18 no REF NP_708732 . "adenine DNA glycosylase [Shigella flexneri 2a str. 301]" . . . . . 100.00 350 98.41 98.41 2.22e-82 . . . . 4353 1 19 no REF WP_001295382 . "MULTISPECIES: A/G-specific adenine glycosylase [Enterobacteriaceae]" . . . . . 100.00 350 99.21 99.21 4.37e-83 . . . . 4353 1 20 no REF WP_001296362 . "MULTISPECIES: A/G-specific adenine glycosylase [Enterobacteriaceae]" . . . . . 100.00 350 98.41 98.41 4.89e-82 . . . . 4353 1 21 no SP P17802 . "RecName: Full=A/G-specific adenine glycosylase" . . . . . 100.00 350 99.21 99.21 4.28e-83 . . . . 4353 1 stop_ loop_ _Entity_common_name.Name _Entity_common_name.Type _Entity_common_name.Entry_ID _Entity_common_name.Entity_ID 'p13 c-terminal domain' common 4353 1 'p13 monomer' variant 4353 1 stop_ loop_ _Entity_comp_index.ID _Entity_comp_index.Auth_seq_ID _Entity_comp_index.Comp_ID _Entity_comp_index.Comp_label _Entity_comp_index.Entry_ID _Entity_comp_index.Entity_ID 1 225 LYS . 4353 1 2 226 GLN . 4353 1 3 227 THR . 4353 1 4 228 LEU . 4353 1 5 229 PRO . 4353 1 6 230 GLU . 4353 1 7 231 ARG . 4353 1 8 232 THR . 4353 1 9 233 GLY . 4353 1 10 234 TYR . 4353 1 11 235 PHE . 4353 1 12 236 LEU . 4353 1 13 237 LEU . 4353 1 14 248 LEU . 4353 1 15 239 GLN . 4353 1 16 240 HIS . 4353 1 17 241 GLU . 4353 1 18 242 ASP . 4353 1 19 243 GLU . 4353 1 20 244 VAL . 4353 1 21 245 LEU . 4353 1 22 246 LEU . 4353 1 23 247 ALA . 4353 1 24 248 GLN . 4353 1 25 249 ARG . 4353 1 26 250 PRO . 4353 1 27 251 PRO . 4353 1 28 252 SER . 4353 1 29 253 GLY . 4353 1 30 254 LEU . 4353 1 31 255 TRP . 4353 1 32 256 GLY . 4353 1 33 257 GLY . 4353 1 34 258 LEU . 4353 1 35 259 TYR . 4353 1 36 260 CYS . 4353 1 37 261 PHE . 4353 1 38 262 PRO . 4353 1 39 263 GLN . 4353 1 40 264 PHE . 4353 1 41 265 ALA . 4353 1 42 266 ASP . 4353 1 43 267 GLU . 4353 1 44 268 GLU . 4353 1 45 269 SER . 4353 1 46 270 LEU . 4353 1 47 271 ARG . 4353 1 48 272 GLN . 4353 1 49 273 TRP . 4353 1 50 274 LEU . 4353 1 51 275 ALA . 4353 1 52 276 GLN . 4353 1 53 277 ARG . 4353 1 54 278 GLN . 4353 1 55 279 ILE . 4353 1 56 280 ALA . 4353 1 57 281 ALA . 4353 1 58 282 ASP . 4353 1 59 283 MET . 4353 1 60 284 LEU . 4353 1 61 285 THR . 4353 1 62 286 GLN . 4353 1 63 287 LEU . 4353 1 64 288 THR . 4353 1 65 289 ALA . 4353 1 66 290 PHE . 4353 1 67 291 ARG . 4353 1 68 292 HIS . 4353 1 69 293 THR . 4353 1 70 294 PHE . 4353 1 71 295 SER . 4353 1 72 296 HIS . 4353 1 73 297 PHE . 4353 1 74 298 HIS . 4353 1 75 299 LEU . 4353 1 76 300 ASP . 4353 1 77 301 ILE . 4353 1 78 302 VAL . 4353 1 79 303 PRO . 4353 1 80 304 MET . 4353 1 81 305 TRP . 4353 1 82 306 LEU . 4353 1 83 307 PRO . 4353 1 84 308 VAL . 4353 1 85 309 SER . 4353 1 86 310 SER . 4353 1 87 311 PHE . 4353 1 88 312 THR . 4353 1 89 313 GLY . 4353 1 90 314 CYS . 4353 1 91 315 MET . 4353 1 92 316 ASP . 4353 1 93 317 GLU . 4353 1 94 318 GLY . 4353 1 95 319 ASN . 4353 1 96 320 ALA . 4353 1 97 321 LEU . 4353 1 98 322 TRP . 4353 1 99 323 TYR . 4353 1 100 324 ASN . 4353 1 101 325 LEU . 4353 1 102 326 ALA . 4353 1 103 327 GLN . 4353 1 104 328 PRO . 4353 1 105 329 PRO . 4353 1 106 330 SER . 4353 1 107 331 VAL . 4353 1 108 332 GLY . 4353 1 109 333 LEU . 4353 1 110 334 ALA . 4353 1 111 335 ALA . 4353 1 112 336 PRO . 4353 1 113 337 VAL . 4353 1 114 338 GLU . 4353 1 115 339 ARG . 4353 1 116 340 LEU . 4353 1 117 341 LEU . 4353 1 118 342 GLN . 4353 1 119 343 GLN . 4353 1 120 344 LEU . 4353 1 121 345 ARG . 4353 1 122 346 THR . 4353 1 123 347 GLY . 4353 1 124 348 ALA . 4353 1 125 349 PRO . 4353 1 126 350 VAL . 4353 1 stop_ loop_ _Entity_poly_seq.Hetero _Entity_poly_seq.Mon_ID _Entity_poly_seq.Num _Entity_poly_seq.Comp_index_ID _Entity_poly_seq.Entry_ID _Entity_poly_seq.Entity_ID . LYS 1 1 4353 1 . GLN 2 2 4353 1 . THR 3 3 4353 1 . LEU 4 4 4353 1 . PRO 5 5 4353 1 . GLU 6 6 4353 1 . ARG 7 7 4353 1 . THR 8 8 4353 1 . GLY 9 9 4353 1 . TYR 10 10 4353 1 . PHE 11 11 4353 1 . LEU 12 12 4353 1 . LEU 13 13 4353 1 . LEU 14 14 4353 1 . GLN 15 15 4353 1 . HIS 16 16 4353 1 . GLU 17 17 4353 1 . ASP 18 18 4353 1 . GLU 19 19 4353 1 . VAL 20 20 4353 1 . LEU 21 21 4353 1 . LEU 22 22 4353 1 . ALA 23 23 4353 1 . GLN 24 24 4353 1 . ARG 25 25 4353 1 . PRO 26 26 4353 1 . PRO 27 27 4353 1 . SER 28 28 4353 1 . GLY 29 29 4353 1 . LEU 30 30 4353 1 . TRP 31 31 4353 1 . GLY 32 32 4353 1 . GLY 33 33 4353 1 . LEU 34 34 4353 1 . TYR 35 35 4353 1 . CYS 36 36 4353 1 . PHE 37 37 4353 1 . PRO 38 38 4353 1 . GLN 39 39 4353 1 . PHE 40 40 4353 1 . ALA 41 41 4353 1 . ASP 42 42 4353 1 . GLU 43 43 4353 1 . GLU 44 44 4353 1 . SER 45 45 4353 1 . LEU 46 46 4353 1 . ARG 47 47 4353 1 . GLN 48 48 4353 1 . TRP 49 49 4353 1 . LEU 50 50 4353 1 . ALA 51 51 4353 1 . GLN 52 52 4353 1 . ARG 53 53 4353 1 . GLN 54 54 4353 1 . ILE 55 55 4353 1 . ALA 56 56 4353 1 . ALA 57 57 4353 1 . ASP 58 58 4353 1 . MET 59 59 4353 1 . LEU 60 60 4353 1 . THR 61 61 4353 1 . GLN 62 62 4353 1 . LEU 63 63 4353 1 . THR 64 64 4353 1 . ALA 65 65 4353 1 . PHE 66 66 4353 1 . ARG 67 67 4353 1 . HIS 68 68 4353 1 . THR 69 69 4353 1 . PHE 70 70 4353 1 . SER 71 71 4353 1 . HIS 72 72 4353 1 . PHE 73 73 4353 1 . HIS 74 74 4353 1 . LEU 75 75 4353 1 . ASP 76 76 4353 1 . ILE 77 77 4353 1 . VAL 78 78 4353 1 . PRO 79 79 4353 1 . MET 80 80 4353 1 . TRP 81 81 4353 1 . LEU 82 82 4353 1 . PRO 83 83 4353 1 . VAL 84 84 4353 1 . SER 85 85 4353 1 . SER 86 86 4353 1 . PHE 87 87 4353 1 . THR 88 88 4353 1 . GLY 89 89 4353 1 . CYS 90 90 4353 1 . MET 91 91 4353 1 . ASP 92 92 4353 1 . GLU 93 93 4353 1 . GLY 94 94 4353 1 . ASN 95 95 4353 1 . ALA 96 96 4353 1 . LEU 97 97 4353 1 . TRP 98 98 4353 1 . TYR 99 99 4353 1 . ASN 100 100 4353 1 . LEU 101 101 4353 1 . ALA 102 102 4353 1 . GLN 103 103 4353 1 . PRO 104 104 4353 1 . PRO 105 105 4353 1 . SER 106 106 4353 1 . VAL 107 107 4353 1 . GLY 108 108 4353 1 . LEU 109 109 4353 1 . ALA 110 110 4353 1 . ALA 111 111 4353 1 . PRO 112 112 4353 1 . VAL 113 113 4353 1 . GLU 114 114 4353 1 . ARG 115 115 4353 1 . LEU 116 116 4353 1 . LEU 117 117 4353 1 . GLN 118 118 4353 1 . GLN 119 119 4353 1 . LEU 120 120 4353 1 . ARG 121 121 4353 1 . THR 122 122 4353 1 . GLY 123 123 4353 1 . ALA 124 124 4353 1 . PRO 125 125 4353 1 . VAL 126 126 4353 1 stop_ save_ #################### # Natural source # #################### save_natural_source _Entity_natural_src_list.Sf_category natural_source _Entity_natural_src_list.Sf_framecode natural_source _Entity_natural_src_list.Entry_ID 4353 _Entity_natural_src_list.ID 1 loop_ _Entity_natural_src.ID _Entity_natural_src.Entity_ID _Entity_natural_src.Entity_label _Entity_natural_src.Entity_chimera_segment_ID _Entity_natural_src.NCBI_taxonomy_ID _Entity_natural_src.Type _Entity_natural_src.Common _Entity_natural_src.Organism_name_scientific _Entity_natural_src.Organism_name_common _Entity_natural_src.Organism_acronym _Entity_natural_src.ICTVdb_decimal_code _Entity_natural_src.Superkingdom _Entity_natural_src.Kingdom _Entity_natural_src.Genus _Entity_natural_src.Species _Entity_natural_src.Strain _Entity_natural_src.Variant _Entity_natural_src.Subvariant _Entity_natural_src.Organ _Entity_natural_src.Tissue _Entity_natural_src.Tissue_fraction _Entity_natural_src.Cell_line _Entity_natural_src.Cell_type _Entity_natural_src.ATCC_number _Entity_natural_src.Organelle _Entity_natural_src.Cellular_location _Entity_natural_src.Fragment _Entity_natural_src.Fraction _Entity_natural_src.Secretion _Entity_natural_src.Plasmid _Entity_natural_src.Plasmid_details _Entity_natural_src.Gene_mnemonic _Entity_natural_src.Dev_stage _Entity_natural_src.Details _Entity_natural_src.Citation_ID _Entity_natural_src.Citation_label _Entity_natural_src.Entry_ID _Entity_natural_src.Entity_natural_src_list_ID 1 1 $protein . 562 . . 'Escherichia coli' 'E. coli' . . Eubacteria . Escherichia coli . . . . . . BL21 DE3 . . . . . . . . . . . . . 4353 1 stop_ save_ ######################### # Experimental source # ######################### save_experimental_source _Entity_experimental_src_list.Sf_category experimental_source _Entity_experimental_src_list.Sf_framecode experimental_source _Entity_experimental_src_list.Entry_ID 4353 _Entity_experimental_src_list.ID 1 loop_ _Entity_experimental_src.ID _Entity_experimental_src.Entity_ID _Entity_experimental_src.Entity_label _Entity_experimental_src.Entity_chimera_segment_ID _Entity_experimental_src.Production_method _Entity_experimental_src.Host_org_scientific_name _Entity_experimental_src.Host_org_name_common _Entity_experimental_src.Host_org_details _Entity_experimental_src.Host_org_NCBI_taxonomy_ID _Entity_experimental_src.Host_org_genus _Entity_experimental_src.Host_org_species _Entity_experimental_src.Host_org_strain _Entity_experimental_src.Host_org_variant _Entity_experimental_src.Host_org_subvariant _Entity_experimental_src.Host_org_organ _Entity_experimental_src.Host_org_tissue _Entity_experimental_src.Host_org_tissue_fraction _Entity_experimental_src.Host_org_cell_line _Entity_experimental_src.Host_org_cell_type _Entity_experimental_src.Host_org_cellular_location _Entity_experimental_src.Host_org_organelle _Entity_experimental_src.Host_org_gene _Entity_experimental_src.Host_org_culture_collection _Entity_experimental_src.Host_org_ATCC_number _Entity_experimental_src.Vector_type _Entity_experimental_src.PDBview_host_org_vector_name _Entity_experimental_src.PDBview_plasmid_name _Entity_experimental_src.Vector_name _Entity_experimental_src.Vector_details _Entity_experimental_src.Vendor_name _Entity_experimental_src.Host_org_dev_stage _Entity_experimental_src.Details _Entity_experimental_src.Citation_ID _Entity_experimental_src.Citation_label _Entity_experimental_src.Entry_ID _Entity_experimental_src.Entity_experimental_src_list_ID 1 1 $protein . 'recombinant technology' . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 4353 1 stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Sample.Sf_category sample _Sample.Sf_framecode sample_1 _Sample.Entry_ID 4353 _Sample.ID 1 _Sample.Type solution _Sample.Sub_type . _Sample.Details . _Sample.Aggregate_sample_number . _Sample.Solvent_system . _Sample.Preparation_date . _Sample.Preparation_expiration_date . _Sample.Polycrystallization_protocol . _Sample.Single_crystal_protocol . _Sample.Crystal_grow_apparatus . _Sample.Crystal_grow_atmosphere . _Sample.Crystal_grow_details . _Sample.Crystal_grow_method . _Sample.Crystal_grow_method_cit_ID . _Sample.Crystal_grow_pH . _Sample.Crystal_grow_pH_range . _Sample.Crystal_grow_pressure . _Sample.Crystal_grow_pressure_esd . _Sample.Crystal_grow_seeding . _Sample.Crystal_grow_seeding_cit_ID . _Sample.Crystal_grow_temp . _Sample.Crystal_grow_temp_details . _Sample.Crystal_grow_temp_esd . _Sample.Crystal_grow_time . _Sample.Oriented_sample_prep_protocol . _Sample.Lyophilization_cryo_protectant . _Sample.Storage_protocol . loop_ _Sample_component.ID _Sample_component.Mol_common_name _Sample_component.Isotopic_labeling _Sample_component.Assembly_ID _Sample_component.Assembly_label _Sample_component.Entity_ID _Sample_component.Entity_label _Sample_component.Product_ID _Sample_component.Type _Sample_component.Concentration_val _Sample_component.Concentration_val_min _Sample_component.Concentration_val_max _Sample_component.Concentration_val_units _Sample_component.Concentration_val_err _Sample_component.Vendor _Sample_component.Vendor_product_name _Sample_component.Vendor_product_code _Sample_component.Entry_ID _Sample_component.Sample_ID 1 'p13 c-terminal domain' '[U-95% 13C; U-95% 15N]' . . 1 $protein . . . 0.7 1.3 mM . . . . 4353 1 stop_ save_ ####################### # Sample conditions # ####################### save_sample_conditions_1 _Sample_condition_list.Sf_category sample_conditions _Sample_condition_list.Sf_framecode sample_conditions_1 _Sample_condition_list.Entry_ID 4353 _Sample_condition_list.ID 1 _Sample_condition_list.Details . loop_ _Sample_condition_variable.Type _Sample_condition_variable.Val _Sample_condition_variable.Val_err _Sample_condition_variable.Val_units _Sample_condition_variable.Entry_ID _Sample_condition_variable.Sample_condition_list_ID pH 6.50 0.2 n/a 4353 1 temperature 298 0.5 K 4353 1 stop_ save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_list _NMR_spectrometer.Sf_category NMR_spectrometer _NMR_spectrometer.Sf_framecode spectrometer_list _NMR_spectrometer.Entry_ID 4353 _NMR_spectrometer.ID 1 _NMR_spectrometer.Details 'spectrometer information not available' _NMR_spectrometer.Manufacturer unknown _NMR_spectrometer.Model unknown _NMR_spectrometer.Serial_number . _NMR_spectrometer.Field_strength 0 save_ save_NMR_spectrometer_list _NMR_spectrometer_list.Sf_category NMR_spectrometer_list _NMR_spectrometer_list.Sf_framecode NMR_spectrometer_list _NMR_spectrometer_list.Entry_ID 4353 _NMR_spectrometer_list.ID 1 loop_ _NMR_spectrometer_view.ID _NMR_spectrometer_view.Name _NMR_spectrometer_view.Manufacturer _NMR_spectrometer_view.Model _NMR_spectrometer_view.Serial_number _NMR_spectrometer_view.Field_strength _NMR_spectrometer_view.Details _NMR_spectrometer_view.Citation_ID _NMR_spectrometer_view.Citation_label _NMR_spectrometer_view.Entry_ID _NMR_spectrometer_view.NMR_spectrometer_list_ID 1 spectrometer_1 unknown unknown . 0 'spectrometer information not available' . . 4353 1 stop_ save_ ############################# # NMR applied experiments # ############################# save_experiment_list _Experiment_list.Sf_category experiment_list _Experiment_list.Sf_framecode experiment_list _Experiment_list.Entry_ID 4353 _Experiment_list.ID 1 _Experiment_list.Details . save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference_1 _Chem_shift_reference.Sf_category chem_shift_reference _Chem_shift_reference.Sf_framecode chemical_shift_reference_1 _Chem_shift_reference.Entry_ID 4353 _Chem_shift_reference.ID 1 _Chem_shift_reference.Details . loop_ _Chem_shift_ref.Atom_type _Chem_shift_ref.Atom_isotope_number _Chem_shift_ref.Mol_common_name _Chem_shift_ref.Atom_group _Chem_shift_ref.Concentration_val _Chem_shift_ref.Concentration_units _Chem_shift_ref.Solvent _Chem_shift_ref.Rank _Chem_shift_ref.Chem_shift_units _Chem_shift_ref.Chem_shift_val _Chem_shift_ref.Ref_method _Chem_shift_ref.Ref_type _Chem_shift_ref.Indirect_shift_ratio _Chem_shift_ref.External_ref_loc _Chem_shift_ref.External_ref_sample_geometry _Chem_shift_ref.External_ref_axis _Chem_shift_ref.Indirect_shift_ratio_cit_ID _Chem_shift_ref.Indirect_shift_ratio_cit_label _Chem_shift_ref.Ref_correction_type _Chem_shift_ref.Correction_val _Chem_shift_ref.Correction_val_cit_ID _Chem_shift_ref.Correction_val_cit_label _Chem_shift_ref.Entry_ID _Chem_shift_ref.Chem_shift_reference_ID H 1 DSS 'methyl protons' . . . . ppm 0.0 . indirect 1 . . . . . . . . . 4353 1 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_chemical_shifts_set_1 _Assigned_chem_shift_list.Sf_category assigned_chemical_shifts _Assigned_chem_shift_list.Sf_framecode assigned_chemical_shifts_set_1 _Assigned_chem_shift_list.Entry_ID 4353 _Assigned_chem_shift_list.ID 1 _Assigned_chem_shift_list.Sample_condition_list_ID 1 _Assigned_chem_shift_list.Sample_condition_list_label $sample_conditions_1 _Assigned_chem_shift_list.Chem_shift_reference_ID 1 _Assigned_chem_shift_list.Chem_shift_reference_label $chemical_shift_reference_1 _Assigned_chem_shift_list.Chem_shift_1H_err . _Assigned_chem_shift_list.Chem_shift_13C_err . _Assigned_chem_shift_list.Chem_shift_15N_err . _Assigned_chem_shift_list.Chem_shift_31P_err . _Assigned_chem_shift_list.Chem_shift_2H_err . _Assigned_chem_shift_list.Chem_shift_19F_err . _Assigned_chem_shift_list.Error_derivation_method . _Assigned_chem_shift_list.Details . _Assigned_chem_shift_list.Text_data_format . _Assigned_chem_shift_list.Text_data . loop_ _Chem_shift_experiment.Experiment_ID _Chem_shift_experiment.Experiment_name _Chem_shift_experiment.Sample_ID _Chem_shift_experiment.Sample_label _Chem_shift_experiment.Sample_state _Chem_shift_experiment.Entry_ID _Chem_shift_experiment.Assigned_chem_shift_list_ID . . 1 $sample_1 . 4353 1 stop_ loop_ _Atom_chem_shift.ID _Atom_chem_shift.Assembly_atom_ID _Atom_chem_shift.Entity_assembly_ID _Atom_chem_shift.Entity_ID _Atom_chem_shift.Comp_index_ID _Atom_chem_shift.Seq_ID _Atom_chem_shift.Comp_ID _Atom_chem_shift.Atom_ID _Atom_chem_shift.Atom_type _Atom_chem_shift.Atom_isotope_number _Atom_chem_shift.Val _Atom_chem_shift.Val_err _Atom_chem_shift.Assign_fig_of_merit _Atom_chem_shift.Ambiguity_code _Atom_chem_shift.Occupancy _Atom_chem_shift.Resonance_ID _Atom_chem_shift.Auth_entity_assembly_ID _Atom_chem_shift.Auth_asym_ID _Atom_chem_shift.Auth_seq_ID _Atom_chem_shift.Auth_comp_ID _Atom_chem_shift.Auth_atom_ID _Atom_chem_shift.Details _Atom_chem_shift.Entry_ID _Atom_chem_shift.Assigned_chem_shift_list_ID 1 . 1 1 1 1 LYS HA H 1 4.3 0.01 . 1 . . . . . . . . 4353 1 2 . 1 1 1 1 LYS HB2 H 1 1.82 0.01 . 2 . . . . . . . . 4353 1 3 . 1 1 1 1 LYS HB3 H 1 1.77 0.01 . 2 . . . . . . . . 4353 1 4 . 1 1 1 1 LYS HG2 H 1 1.45 0.01 . 2 . . . . . . . . 4353 1 5 . 1 1 1 1 LYS HG3 H 1 1.43 0.01 . 2 . . . . . . . . 4353 1 6 . 1 1 1 1 LYS HD2 H 1 1.69 0.01 . 1 . . . . . . . . 4353 1 7 . 1 1 1 1 LYS HD3 H 1 1.69 0.01 . 1 . . . . . . . . 4353 1 8 . 1 1 1 1 LYS HE2 H 1 2.98 0.01 . 1 . . . . . . . . 4353 1 9 . 1 1 1 1 LYS HE3 H 1 2.98 0.01 . 1 . . . . . . . . 4353 1 10 . 1 1 1 1 LYS CA C 13 56.4 0.2 . 1 . . . . . . . . 4353 1 11 . 1 1 1 1 LYS CB C 13 33.1 0.2 . 1 . . . . . . . . 4353 1 12 . 1 1 1 1 LYS CG C 13 24.7 0.2 . 1 . . . . . . . . 4353 1 13 . 1 1 1 1 LYS CD C 13 29 0.2 . 1 . . . . . . . . 4353 1 14 . 1 1 1 1 LYS CE C 13 41.8 0.2 . 1 . . . . . . . . 4353 1 15 . 1 1 3 3 THR HA H 1 4.4 0.01 . 1 . . . . . . . . 4353 1 16 . 1 1 3 3 THR HB H 1 4.18 0.01 . 1 . . . . . . . . 4353 1 17 . 1 1 3 3 THR HG21 H 1 1.21 0.01 . 1 . . . . . . . . 4353 1 18 . 1 1 3 3 THR HG22 H 1 1.21 0.01 . 1 . . . . . . . . 4353 1 19 . 1 1 3 3 THR HG23 H 1 1.21 0.01 . 1 . . . . . . . . 4353 1 20 . 1 1 3 3 THR CA C 13 61.5 0.2 . 1 . . . . . . . . 4353 1 21 . 1 1 3 3 THR CB C 13 69.7 0.2 . 1 . . . . . . . . 4353 1 22 . 1 1 3 3 THR CG2 C 13 21.54 0.2 . 1 . . . . . . . . 4353 1 23 . 1 1 5 5 PRO HA H 1 4.56 0.01 . 1 . . . . . . . . 4353 1 24 . 1 1 5 5 PRO HB2 H 1 2.42 0.01 . 2 . . . . . . . . 4353 1 25 . 1 1 5 5 PRO HB3 H 1 1.94 0.01 . 2 . . . . . . . . 4353 1 26 . 1 1 5 5 PRO HG2 H 1 2.2 0.01 . 1 . . . . . . . . 4353 1 27 . 1 1 5 5 PRO HG3 H 1 2.2 0.01 . 1 . . . . . . . . 4353 1 28 . 1 1 5 5 PRO C C 13 175.1 0.1 . 1 . . . . . . . . 4353 1 29 . 1 1 5 5 PRO CA C 13 63.05 0.2 . 1 . . . . . . . . 4353 1 30 . 1 1 5 5 PRO CB C 13 32.75 0.2 . 1 . . . . . . . . 4353 1 31 . 1 1 6 6 GLU H H 1 8.44 0.01 . 1 . . . . . . . . 4353 1 32 . 1 1 6 6 GLU HA H 1 5.14 0.01 . 1 . . . . . . . . 4353 1 33 . 1 1 6 6 GLU HB2 H 1 2.08 0.01 . 1 . . . . . . . . 4353 1 34 . 1 1 6 6 GLU HB3 H 1 2.08 0.01 . 1 . . . . . . . . 4353 1 35 . 1 1 6 6 GLU HG2 H 1 2.45 0.01 . 2 . . . . . . . . 4353 1 36 . 1 1 6 6 GLU HG3 H 1 2.2 0.01 . 2 . . . . . . . . 4353 1 37 . 1 1 6 6 GLU C C 13 176.2 0.1 . 1 . . . . . . . . 4353 1 38 . 1 1 6 6 GLU CA C 13 55.15 0.2 . 1 . . . . . . . . 4353 1 39 . 1 1 6 6 GLU CB C 13 31.75 0.2 . 1 . . . . . . . . 4353 1 40 . 1 1 6 6 GLU CG C 13 36.5 0.2 . 1 . . . . . . . . 4353 1 41 . 1 1 6 6 GLU N N 15 176.2 0.1 . 1 . . . . . . . . 4353 1 42 . 1 1 7 7 ARG H H 1 9.03 0.01 . 1 . . . . . . . . 4353 1 43 . 1 1 7 7 ARG HA H 1 4.81 0.01 . 1 . . . . . . . . 4353 1 44 . 1 1 7 7 ARG HB2 H 1 1.9 0.01 . 2 . . . . . . . . 4353 1 45 . 1 1 7 7 ARG HB3 H 1 1.76 0.01 . 2 . . . . . . . . 4353 1 46 . 1 1 7 7 ARG HG2 H 1 1.54 0.01 . 2 . . . . . . . . 4353 1 47 . 1 1 7 7 ARG HG3 H 1 1.44 0.01 . 2 . . . . . . . . 4353 1 48 . 1 1 7 7 ARG HD2 H 1 2.9 0.01 . 2 . . . . . . . . 4353 1 49 . 1 1 7 7 ARG HD3 H 1 2.64 0.01 . 2 . . . . . . . . 4353 1 50 . 1 1 7 7 ARG C C 13 174.9 0.1 . 1 . . . . . . . . 4353 1 51 . 1 1 7 7 ARG CA C 13 55.15 0.2 . 1 . . . . . . . . 4353 1 52 . 1 1 7 7 ARG CB C 13 33.35 0.2 . 1 . . . . . . . . 4353 1 53 . 1 1 7 7 ARG CG C 13 27.2 0.2 . 1 . . . . . . . . 4353 1 54 . 1 1 7 7 ARG CD C 13 23.2 0.2 . 1 . . . . . . . . 4353 1 55 . 1 1 7 7 ARG N N 15 123.59 0.1 . 1 . . . . . . . . 4353 1 56 . 1 1 8 8 THR H H 1 8.65 0.01 . 1 . . . . . . . . 4353 1 57 . 1 1 8 8 THR HA H 1 5.28 0.01 . 1 . . . . . . . . 4353 1 58 . 1 1 8 8 THR C C 13 174.5 0.1 . 1 . . . . . . . . 4353 1 59 . 1 1 8 8 THR CA C 13 61.88 0.2 . 1 . . . . . . . . 4353 1 60 . 1 1 8 8 THR CB C 13 71.05 0.2 . 1 . . . . . . . . 4353 1 61 . 1 1 8 8 THR CG2 C 13 22.3 0.2 . 1 . . . . . . . . 4353 1 62 . 1 1 8 8 THR N N 15 118.11 0.1 . 1 . . . . . . . . 4353 1 63 . 1 1 9 9 GLY H H 1 9.09 0.01 . 1 . . . . . . . . 4353 1 64 . 1 1 9 9 GLY HA2 H 1 4.72 0.01 . 1 . . . . . . . . 4353 1 65 . 1 1 9 9 GLY HA3 H 1 4.72 0.01 . 1 . . . . . . . . 4353 1 66 . 1 1 9 9 GLY C C 13 170.2 0.1 . 1 . . . . . . . . 4353 1 67 . 1 1 9 9 GLY CA C 13 44.92 0.2 . 1 . . . . . . . . 4353 1 68 . 1 1 9 9 GLY N N 15 113.04 0.1 . 1 . . . . . . . . 4353 1 69 . 1 1 10 10 TYR H H 1 8.88 0.01 . 1 . . . . . . . . 4353 1 70 . 1 1 10 10 TYR HA H 1 5.19 0.01 . 1 . . . . . . . . 4353 1 71 . 1 1 10 10 TYR HB2 H 1 2.77 0.01 . 2 . . . . . . . . 4353 1 72 . 1 1 10 10 TYR HB3 H 1 2.54 0.01 . 2 . . . . . . . . 4353 1 73 . 1 1 10 10 TYR C C 13 176.2 0.1 . 1 . . . . . . . . 4353 1 74 . 1 1 10 10 TYR CA C 13 57.04 0.2 . 1 . . . . . . . . 4353 1 75 . 1 1 10 10 TYR CB C 13 40.35 0.2 . 1 . . . . . . . . 4353 1 76 . 1 1 10 10 TYR N N 15 122.8 0.1 . 1 . . . . . . . . 4353 1 77 . 1 1 11 11 PHE H H 1 8.59 0.01 . 1 . . . . . . . . 4353 1 78 . 1 1 11 11 PHE HA H 1 5.74 0.01 . 1 . . . . . . . . 4353 1 79 . 1 1 11 11 PHE HB2 H 1 2.65 0.01 . 1 . . . . . . . . 4353 1 80 . 1 1 11 11 PHE HB3 H 1 2.50 0.01 . 1 . . . . . . . . 4353 1 81 . 1 1 11 11 PHE C C 13 124.3 0.1 . 1 . . . . . . . . 4353 1 82 . 1 1 11 11 PHE CA C 13 53.83 0.2 . 1 . . . . . . . . 4353 1 83 . 1 1 11 11 PHE CB C 13 41.69 0.2 . 1 . . . . . . . . 4353 1 84 . 1 1 11 11 PHE N N 15 122.45 0.1 . 1 . . . . . . . . 4353 1 85 . 1 1 12 12 LEU H H 1 8.56 0.01 . 1 . . . . . . . . 4353 1 86 . 1 1 12 12 LEU HA H 1 4.96 0.01 . 1 . . . . . . . . 4353 1 87 . 1 1 12 12 LEU C C 13 174.4 0.1 . 1 . . . . . . . . 4353 1 88 . 1 1 12 12 LEU CA C 13 53.79 0.2 . 1 . . . . . . . . 4353 1 89 . 1 1 12 12 LEU CB C 13 45.18 0.2 . 1 . . . . . . . . 4353 1 90 . 1 1 12 12 LEU N N 15 123.72 0.1 . 1 . . . . . . . . 4353 1 91 . 1 1 13 13 LEU H H 1 9.59 0.01 . 1 . . . . . . . . 4353 1 92 . 1 1 13 13 LEU CA C 13 53.8 0.2 . 1 . . . . . . . . 4353 1 93 . 1 1 13 13 LEU CB C 13 41.46 0.2 . 1 . . . . . . . . 4353 1 94 . 1 1 13 13 LEU N N 15 133.56 0.1 . 1 . . . . . . . . 4353 1 95 . 1 1 15 15 GLN C C 13 174.5 0.1 . 1 . . . . . . . . 4353 1 96 . 1 1 15 15 GLN CA C 13 53.75 0.2 . 1 . . . . . . . . 4353 1 97 . 1 1 15 15 GLN CB C 13 32.04 0.2 . 1 . . . . . . . . 4353 1 98 . 1 1 16 16 HIS C C 13 173.8 0.1 . 1 . . . . . . . . 4353 1 99 . 1 1 16 16 HIS CA C 13 54.09 0.2 . 1 . . . . . . . . 4353 1 100 . 1 1 16 16 HIS CB C 13 30.41 0.2 . 1 . . . . . . . . 4353 1 101 . 1 1 17 17 GLU HA H 1 3.36 0.01 . 1 . . . . . . . . 4353 1 102 . 1 1 17 17 GLU HB2 H 1 1.9 0.01 . 1 . . . . . . . . 4353 1 103 . 1 1 17 17 GLU HB3 H 1 1.9 0.01 . 1 . . . . . . . . 4353 1 104 . 1 1 17 17 GLU HG2 H 1 1.81 0.01 . 1 . . . . . . . . 4353 1 105 . 1 1 17 17 GLU HG3 H 1 1.81 0.01 . 1 . . . . . . . . 4353 1 106 . 1 1 17 17 GLU CA C 13 58.92 0.2 . 1 . . . . . . . . 4353 1 107 . 1 1 17 17 GLU CB C 13 26.59 0.2 . 1 . . . . . . . . 4353 1 108 . 1 1 17 17 GLU CG C 13 35.88 0.2 . 1 . . . . . . . . 4353 1 109 . 1 1 18 18 ASP H H 1 8.52 0.01 . 1 . . . . . . . . 4353 1 110 . 1 1 18 18 ASP HA H 1 4.94 0.01 . 1 . . . . . . . . 4353 1 111 . 1 1 18 18 ASP HB2 H 1 2.9 0.01 . 2 . . . . . . . . 4353 1 112 . 1 1 18 18 ASP HB3 H 1 2.8 0.01 . 2 . . . . . . . . 4353 1 113 . 1 1 18 18 ASP C C 13 174 0.1 . 1 . . . . . . . . 4353 1 114 . 1 1 18 18 ASP CA C 13 54.21 0.2 . 1 . . . . . . . . 4353 1 115 . 1 1 18 18 ASP CB C 13 40.73 0.2 . 1 . . . . . . . . 4353 1 116 . 1 1 18 18 ASP N N 15 123.24 0.1 . 1 . . . . . . . . 4353 1 117 . 1 1 19 19 GLU H H 1 8.3 0.01 . 1 . . . . . . . . 4353 1 118 . 1 1 19 19 GLU HA H 1 5.67 0.01 . 1 . . . . . . . . 4353 1 119 . 1 1 19 19 GLU C C 13 175.9 0.1 . 1 . . . . . . . . 4353 1 120 . 1 1 19 19 GLU CA C 13 54.61 0.2 . 1 . . . . . . . . 4353 1 121 . 1 1 19 19 GLU CB C 13 33.85 0.2 . 1 . . . . . . . . 4353 1 122 . 1 1 19 19 GLU N N 15 117.68 0.1 . 1 . . . . . . . . 4353 1 123 . 1 1 20 20 VAL H H 1 9.01 0.01 . 1 . . . . . . . . 4353 1 124 . 1 1 20 20 VAL HA H 1 5.96 0.01 . 1 . . . . . . . . 4353 1 125 . 1 1 20 20 VAL HB H 1 2.1 0.01 . 1 . . . . . . . . 4353 1 126 . 1 1 20 20 VAL HG11 H 1 1.1 0.01 . 1 . . . . . . . . 4353 1 127 . 1 1 20 20 VAL HG12 H 1 1.1 0.01 . 1 . . . . . . . . 4353 1 128 . 1 1 20 20 VAL HG13 H 1 1.1 0.01 . 1 . . . . . . . . 4353 1 129 . 1 1 20 20 VAL HG21 H 1 1.1 0.01 . 1 . . . . . . . . 4353 1 130 . 1 1 20 20 VAL HG22 H 1 1.1 0.01 . 1 . . . . . . . . 4353 1 131 . 1 1 20 20 VAL HG23 H 1 1.1 0.01 . 1 . . . . . . . . 4353 1 132 . 1 1 20 20 VAL C C 13 174.8 0.1 . 1 . . . . . . . . 4353 1 133 . 1 1 20 20 VAL CA C 13 58.68 0.2 . 1 . . . . . . . . 4353 1 134 . 1 1 20 20 VAL CB C 13 36.06 0.2 . 1 . . . . . . . . 4353 1 135 . 1 1 20 20 VAL CG1 C 13 20.94 0.2 . 1 . . . . . . . . 4353 1 136 . 1 1 20 20 VAL CG2 C 13 21.43 0.2 . 1 . . . . . . . . 4353 1 137 . 1 1 20 20 VAL N N 15 117.27 0.1 . 1 . . . . . . . . 4353 1 138 . 1 1 21 21 LEU H H 1 7.7 0.01 . 1 . . . . . . . . 4353 1 139 . 1 1 21 21 LEU HA H 1 3.95 0.01 . 1 . . . . . . . . 4353 1 140 . 1 1 21 21 LEU C C 13 175.8 0.1 . 1 . . . . . . . . 4353 1 141 . 1 1 21 21 LEU CA C 13 55.96 0.2 . 1 . . . . . . . . 4353 1 142 . 1 1 21 21 LEU CB C 13 41.44 0.2 . 1 . . . . . . . . 4353 1 143 . 1 1 21 21 LEU N N 15 128.64 0.1 . 1 . . . . . . . . 4353 1 144 . 1 1 22 22 LEU H H 1 9.01 0.01 . 1 . . . . . . . . 4353 1 145 . 1 1 22 22 LEU HA H 1 4.68 0.01 . 1 . . . . . . . . 4353 1 146 . 1 1 22 22 LEU HB2 H 1 1.17 0.01 . 1 . . . . . . . . 4353 1 147 . 1 1 22 22 LEU HB3 H 1 1.17 0.01 . 1 . . . . . . . . 4353 1 148 . 1 1 22 22 LEU C C 13 174.8 0.1 . 1 . . . . . . . . 4353 1 149 . 1 1 22 22 LEU CA C 13 52.78 0.2 . 1 . . . . . . . . 4353 1 150 . 1 1 22 22 LEU CB C 13 46.29 0.2 . 1 . . . . . . . . 4353 1 151 . 1 1 22 22 LEU N N 15 125.68 0.1 . 1 . . . . . . . . 4353 1 152 . 1 1 23 23 ALA H H 1 8.75 0.01 . 1 . . . . . . . . 4353 1 153 . 1 1 23 23 ALA HA H 1 5.03 0.01 . 1 . . . . . . . . 4353 1 154 . 1 1 23 23 ALA HB1 H 1 1.25 0.01 . 1 . . . . . . . . 4353 1 155 . 1 1 23 23 ALA HB2 H 1 1.25 0.01 . 1 . . . . . . . . 4353 1 156 . 1 1 23 23 ALA HB3 H 1 1.25 0.01 . 1 . . . . . . . . 4353 1 157 . 1 1 23 23 ALA C C 13 177.2 0.1 . 1 . . . . . . . . 4353 1 158 . 1 1 23 23 ALA CA C 13 50.63 0.2 . 1 . . . . . . . . 4353 1 159 . 1 1 23 23 ALA CB C 13 22 0.2 . 1 . . . . . . . . 4353 1 160 . 1 1 23 23 ALA N N 15 120.5 0.1 . 1 . . . . . . . . 4353 1 161 . 1 1 24 24 GLN H H 1 8.72 0.01 . 1 . . . . . . . . 4353 1 162 . 1 1 24 24 GLN HA H 1 3.39 0.01 . 1 . . . . . . . . 4353 1 163 . 1 1 24 24 GLN C C 13 176.2 0.1 . 1 . . . . . . . . 4353 1 164 . 1 1 24 24 GLN CA C 13 56.25 0.2 . 1 . . . . . . . . 4353 1 165 . 1 1 24 24 GLN CB C 13 28.5 0.2 . 1 . . . . . . . . 4353 1 166 . 1 1 24 24 GLN N N 15 125.43 0.1 . 1 . . . . . . . . 4353 1 167 . 1 1 25 25 ARG H H 1 8.54 0.01 . 1 . . . . . . . . 4353 1 168 . 1 1 25 25 ARG CA C 13 54.9 0.2 . 1 . . . . . . . . 4353 1 169 . 1 1 25 25 ARG CB C 13 28.76 0.2 . 1 . . . . . . . . 4353 1 170 . 1 1 25 25 ARG N N 15 130.62 0.1 . 1 . . . . . . . . 4353 1 171 . 1 1 27 27 PRO HA H 1 4.08 0.01 . 1 . . . . . . . . 4353 1 172 . 1 1 27 27 PRO HB2 H 1 2.24 0.01 . 1 . . . . . . . . 4353 1 173 . 1 1 27 27 PRO HB3 H 1 2.24 0.01 . 1 . . . . . . . . 4353 1 174 . 1 1 27 27 PRO C C 13 177 0.1 . 1 . . . . . . . . 4353 1 175 . 1 1 27 27 PRO CA C 13 64.81 0.2 . 1 . . . . . . . . 4353 1 176 . 1 1 27 27 PRO CB C 13 35.51 0.2 . 1 . . . . . . . . 4353 1 177 . 1 1 28 28 SER H H 1 7.86 0.01 . 1 . . . . . . . . 4353 1 178 . 1 1 28 28 SER HA H 1 4.45 0.01 . 1 . . . . . . . . 4353 1 179 . 1 1 28 28 SER HB2 H 1 3.91 0.01 . 2 . . . . . . . . 4353 1 180 . 1 1 28 28 SER HB3 H 1 3.8 0.01 . 2 . . . . . . . . 4353 1 181 . 1 1 28 28 SER C C 13 174.5 0.1 . 1 . . . . . . . . 4353 1 182 . 1 1 28 28 SER CA C 13 58.14 0.2 . 1 . . . . . . . . 4353 1 183 . 1 1 28 28 SER CB C 13 63.56 0.2 . 1 . . . . . . . . 4353 1 184 . 1 1 28 28 SER N N 15 111.07 0.1 . 1 . . . . . . . . 4353 1 185 . 1 1 29 29 GLY H H 1 7.72 0.01 . 1 . . . . . . . . 4353 1 186 . 1 1 29 29 GLY HA2 H 1 4.08 0.01 . 2 . . . . . . . . 4353 1 187 . 1 1 29 29 GLY HA3 H 1 3.79 0.01 . 2 . . . . . . . . 4353 1 188 . 1 1 29 29 GLY CA C 13 44.15 0.2 . 1 . . . . . . . . 4353 1 189 . 1 1 29 29 GLY N N 15 108.97 0.1 . 1 . . . . . . . . 4353 1 190 . 1 1 30 30 LEU H H 1 8.22 0.01 . 1 . . . . . . . . 4353 1 191 . 1 1 30 30 LEU HA H 1 4.15 0.01 . 1 . . . . . . . . 4353 1 192 . 1 1 30 30 LEU HB2 H 1 3.59 0.01 . 1 . . . . . . . . 4353 1 193 . 1 1 30 30 LEU HB3 H 1 3.59 0.01 . 1 . . . . . . . . 4353 1 194 . 1 1 30 30 LEU C C 13 174.2 0.1 . 1 . . . . . . . . 4353 1 195 . 1 1 30 30 LEU CA C 13 55.52 0.2 . 1 . . . . . . . . 4353 1 196 . 1 1 30 30 LEU CB C 13 29.9 0.2 . 1 . . . . . . . . 4353 1 197 . 1 1 30 30 LEU N N 15 121.82 0.1 . 1 . . . . . . . . 4353 1 198 . 1 1 31 31 TRP H H 1 7.82 0.01 . 1 . . . . . . . . 4353 1 199 . 1 1 31 31 TRP C C 13 175.6 0.1 . 1 . . . . . . . . 4353 1 200 . 1 1 31 31 TRP CA C 13 56.83 0.2 . 1 . . . . . . . . 4353 1 201 . 1 1 31 31 TRP CB C 13 25.55 0.2 . 1 . . . . . . . . 4353 1 202 . 1 1 31 31 TRP N N 15 114.73 0.1 . 1 . . . . . . . . 4353 1 203 . 1 1 32 32 GLY H H 1 7.72 0.01 . 1 . . . . . . . . 4353 1 204 . 1 1 32 32 GLY HA2 H 1 3.68 0.01 . 2 . . . . . . . . 4353 1 205 . 1 1 32 32 GLY HA3 H 1 3.59 0.01 . 2 . . . . . . . . 4353 1 206 . 1 1 32 32 GLY C C 13 176.06 0.1 . 1 . . . . . . . . 4353 1 207 . 1 1 32 32 GLY CA C 13 47.83 0.2 . 1 . . . . . . . . 4353 1 208 . 1 1 32 32 GLY N N 15 104.48 0.1 . 1 . . . . . . . . 4353 1 209 . 1 1 33 33 GLY H H 1 7.65 0.01 . 1 . . . . . . . . 4353 1 210 . 1 1 33 33 GLY HA2 H 1 4.14 0.01 . 2 . . . . . . . . 4353 1 211 . 1 1 33 33 GLY HA3 H 1 3.59 0.01 . 2 . . . . . . . . 4353 1 212 . 1 1 33 33 GLY C C 13 173.49 0.1 . 1 . . . . . . . . 4353 1 213 . 1 1 33 33 GLY CA C 13 45.44 0.2 . 1 . . . . . . . . 4353 1 214 . 1 1 33 33 GLY N N 15 112.62 0.1 . 1 . . . . . . . . 4353 1 215 . 1 1 34 34 LEU H H 1 7.61 0.01 . 1 . . . . . . . . 4353 1 216 . 1 1 34 34 LEU HA H 1 4.58 0.01 . 1 . . . . . . . . 4353 1 217 . 1 1 34 34 LEU HB2 H 1 1.79 0.01 . 1 . . . . . . . . 4353 1 218 . 1 1 34 34 LEU HB3 H 1 1.14 0.01 . 1 . . . . . . . . 4353 1 219 . 1 1 34 34 LEU HD11 H 1 0.85 0.01 . 1 . . . . . . . . 4353 1 220 . 1 1 34 34 LEU HD12 H 1 0.85 0.01 . 1 . . . . . . . . 4353 1 221 . 1 1 34 34 LEU HD13 H 1 0.85 0.01 . 1 . . . . . . . . 4353 1 222 . 1 1 34 34 LEU HD21 H 1 0.72 0.01 . 1 . . . . . . . . 4353 1 223 . 1 1 34 34 LEU HD22 H 1 0.72 0.01 . 1 . . . . . . . . 4353 1 224 . 1 1 34 34 LEU HD23 H 1 0.72 0.01 . 1 . . . . . . . . 4353 1 225 . 1 1 34 34 LEU HG H 1 1.46 0.01 . 1 . . . . . . . . 4353 1 226 . 1 1 34 34 LEU C C 13 176.9 0.1 . 1 . . . . . . . . 4353 1 227 . 1 1 34 34 LEU CA C 13 53.05 0.2 . 1 . . . . . . . . 4353 1 228 . 1 1 34 34 LEU CB C 13 43.3 0.2 . 1 . . . . . . . . 4353 1 229 . 1 1 34 34 LEU CD2 C 13 21.7 0.2 . 1 . . . . . . . . 4353 1 230 . 1 1 34 34 LEU N N 15 120.35 0.1 . 1 . . . . . . . . 4353 1 231 . 1 1 35 35 TYR H H 1 8.83 0.01 . 1 . . . . . . . . 4353 1 232 . 1 1 35 35 TYR HA H 1 4.64 0.01 . 1 . . . . . . . . 4353 1 233 . 1 1 35 35 TYR C C 13 176.5 0.1 . 1 . . . . . . . . 4353 1 234 . 1 1 35 35 TYR CA C 13 59.49 0.2 . 1 . . . . . . . . 4353 1 235 . 1 1 35 35 TYR CB C 13 39.03 0.2 . 1 . . . . . . . . 4353 1 236 . 1 1 35 35 TYR N N 15 118.81 0.1 . 1 . . . . . . . . 4353 1 237 . 1 1 36 36 CYS H H 1 8.85 0.01 . 1 . . . . . . . . 4353 1 238 . 1 1 36 36 CYS C C 13 172 0.1 . 1 . . . . . . . . 4353 1 239 . 1 1 36 36 CYS CA C 13 57.08 0.2 . 1 . . . . . . . . 4353 1 240 . 1 1 36 36 CYS CB C 13 29.61 0.2 . 1 . . . . . . . . 4353 1 241 . 1 1 36 36 CYS N N 15 119.51 0.1 . 1 . . . . . . . . 4353 1 242 . 1 1 37 37 PHE H H 1 6.13 0.01 . 1 . . . . . . . . 4353 1 243 . 1 1 37 37 PHE CA C 13 57.33 0.2 . 1 . . . . . . . . 4353 1 244 . 1 1 37 37 PHE CB C 13 37.92 0.2 . 1 . . . . . . . . 4353 1 245 . 1 1 37 37 PHE N N 15 127.23 0.1 . 1 . . . . . . . . 4353 1 246 . 1 1 38 38 PRO HA H 1 3.99 0.01 . 1 . . . . . . . . 4353 1 247 . 1 1 38 38 PRO C C 13 173 0.1 . 1 . . . . . . . . 4353 1 248 . 1 1 38 38 PRO CA C 13 64.57 0.2 . 1 . . . . . . . . 4353 1 249 . 1 1 38 38 PRO CB C 13 32.23 0.2 . 1 . . . . . . . . 4353 1 250 . 1 1 39 39 GLN H H 1 7.57 0.01 . 1 . . . . . . . . 4353 1 251 . 1 1 39 39 GLN C C 13 174.36 0.1 . 1 . . . . . . . . 4353 1 252 . 1 1 39 39 GLN CA C 13 53.8 0.2 . 1 . . . . . . . . 4353 1 253 . 1 1 39 39 GLN CB C 13 31.19 0.2 . 1 . . . . . . . . 4353 1 254 . 1 1 39 39 GLN N N 15 124.15 0.1 . 1 . . . . . . . . 4353 1 255 . 1 1 40 40 PHE H H 1 9.3 0.01 . 1 . . . . . . . . 4353 1 256 . 1 1 40 40 PHE CA C 13 56.51 0.2 . 1 . . . . . . . . 4353 1 257 . 1 1 40 40 PHE CB C 13 43.85 0.2 . 1 . . . . . . . . 4353 1 258 . 1 1 40 40 PHE N N 15 123.3 0.1 . 1 . . . . . . . . 4353 1 259 . 1 1 41 41 ALA H H 1 9.4 0.01 . 1 . . . . . . . . 4353 1 260 . 1 1 41 41 ALA HA H 1 4.48 0.01 . 1 . . . . . . . . 4353 1 261 . 1 1 41 41 ALA HB1 H 1 1.52 0.01 . 1 . . . . . . . . 4353 1 262 . 1 1 41 41 ALA HB2 H 1 1.52 0.01 . 1 . . . . . . . . 4353 1 263 . 1 1 41 41 ALA HB3 H 1 1.52 0.01 . 1 . . . . . . . . 4353 1 264 . 1 1 41 41 ALA C C 13 176.6 0.1 . 1 . . . . . . . . 4353 1 265 . 1 1 41 41 ALA CA C 13 53.84 0.2 . 1 . . . . . . . . 4353 1 266 . 1 1 41 41 ALA CB C 13 19.55 0.2 . 1 . . . . . . . . 4353 1 267 . 1 1 41 41 ALA N N 15 124.29 0.1 . 1 . . . . . . . . 4353 1 268 . 1 1 42 42 ASP H H 1 7.41 0.01 . 1 . . . . . . . . 4353 1 269 . 1 1 42 42 ASP HA H 1 4.35 0.01 . 1 . . . . . . . . 4353 1 270 . 1 1 42 42 ASP HB2 H 1 2.89 0.01 . 1 . . . . . . . . 4353 1 271 . 1 1 42 42 ASP HB3 H 1 2.89 0.01 . 1 . . . . . . . . 4353 1 272 . 1 1 42 42 ASP C C 13 174 0.1 . 1 . . . . . . . . 4353 1 273 . 1 1 42 42 ASP CA C 13 52.27 0.2 . 1 . . . . . . . . 4353 1 274 . 1 1 42 42 ASP CB C 13 41.8 0.2 . 1 . . . . . . . . 4353 1 275 . 1 1 42 42 ASP N N 15 109.26 0.1 . 1 . . . . . . . . 4353 1 276 . 1 1 43 43 GLU H H 1 8.08 0.01 . 1 . . . . . . . . 4353 1 277 . 1 1 43 43 GLU C C 13 178.2 0.1 . 1 . . . . . . . . 4353 1 278 . 1 1 43 43 GLU CA C 13 59.19 0.2 . 1 . . . . . . . . 4353 1 279 . 1 1 43 43 GLU CB C 13 29.34 0.2 . 1 . . . . . . . . 4353 1 280 . 1 1 43 43 GLU N N 15 120.08 0.1 . 1 . . . . . . . . 4353 1 281 . 1 1 47 47 ARG C C 13 180.4 0.1 . 1 . . . . . . . . 4353 1 282 . 1 1 47 47 ARG CA C 13 60.55 0.2 . 1 . . . . . . . . 4353 1 283 . 1 1 47 47 ARG CB C 13 29.53 0.2 . 1 . . . . . . . . 4353 1 284 . 1 1 48 48 GLN H H 1 8.63 0.01 . 1 . . . . . . . . 4353 1 285 . 1 1 48 48 GLN HA H 1 4.16 0.01 . 1 . . . . . . . . 4353 1 286 . 1 1 48 48 GLN HB2 H 1 2.18 0.01 . 1 . . . . . . . . 4353 1 287 . 1 1 48 48 GLN HB3 H 1 2.18 0.01 . 1 . . . . . . . . 4353 1 288 . 1 1 48 48 GLN HG2 H 1 2.54 0.01 . 2 . . . . . . . . 4353 1 289 . 1 1 48 48 GLN HG3 H 1 2.45 0.01 . 2 . . . . . . . . 4353 1 290 . 1 1 48 48 GLN C C 13 177.7 0.1 . 1 . . . . . . . . 4353 1 291 . 1 1 48 48 GLN CA C 13 58.92 0.2 . 1 . . . . . . . . 4353 1 292 . 1 1 48 48 GLN CB C 13 27.99 0.2 . 1 . . . . . . . . 4353 1 293 . 1 1 48 48 GLN CG C 13 33.84 0.2 . 1 . . . . . . . . 4353 1 294 . 1 1 48 48 GLN N N 15 122.19 0.1 . 1 . . . . . . . . 4353 1 295 . 1 1 49 49 TRP H H 1 7.81 0.01 . 1 . . . . . . . . 4353 1 296 . 1 1 49 49 TRP HA H 1 4.11 0.01 . 1 . . . . . . . . 4353 1 297 . 1 1 49 49 TRP C C 13 180 0.1 . 1 . . . . . . . . 4353 1 298 . 1 1 49 49 TRP CA C 13 62.15 0.2 . 1 . . . . . . . . 4353 1 299 . 1 1 49 49 TRP CB C 13 30.36 0.2 . 1 . . . . . . . . 4353 1 300 . 1 1 49 49 TRP N N 15 123.86 0.1 . 1 . . . . . . . . 4353 1 301 . 1 1 50 50 LEU H H 1 7.68 0.01 . 1 . . . . . . . . 4353 1 302 . 1 1 50 50 LEU HA H 1 4 0.01 . 1 . . . . . . . . 4353 1 303 . 1 1 50 50 LEU HB2 H 1 2.05 0.01 . 1 . . . . . . . . 4353 1 304 . 1 1 50 50 LEU HB3 H 1 2.05 0.01 . 1 . . . . . . . . 4353 1 305 . 1 1 50 50 LEU HG H 1 1.93 0.01 . 1 . . . . . . . . 4353 1 306 . 1 1 50 50 LEU C C 13 179.2 0.1 . 1 . . . . . . . . 4353 1 307 . 1 1 50 50 LEU CA C 13 58.13 0.2 . 1 . . . . . . . . 4353 1 308 . 1 1 50 50 LEU CB C 13 41.17 0.2 . 1 . . . . . . . . 4353 1 309 . 1 1 50 50 LEU N N 15 117.4 0.1 . 1 . . . . . . . . 4353 1 310 . 1 1 51 51 ALA H H 1 8.08 0.01 . 1 . . . . . . . . 4353 1 311 . 1 1 51 51 ALA HA H 1 4.08 0.01 . 1 . . . . . . . . 4353 1 312 . 1 1 51 51 ALA C C 13 178.1 0.1 . 1 . . . . . . . . 4353 1 313 . 1 1 51 51 ALA CA C 13 55.2 0.2 . 1 . . . . . . . . 4353 1 314 . 1 1 51 51 ALA CB C 13 17.69 0.2 . 1 . . . . . . . . 4353 1 315 . 1 1 51 51 ALA N N 15 122.47 0.1 . 1 . . . . . . . . 4353 1 316 . 1 1 52 52 GLN H H 1 8.38 0.01 . 1 . . . . . . . . 4353 1 317 . 1 1 52 52 GLN C C 13 175 0.1 . 1 . . . . . . . . 4353 1 318 . 1 1 52 52 GLN CA C 13 58.41 0.2 . 1 . . . . . . . . 4353 1 319 . 1 1 52 52 GLN CB C 13 28.49 0.2 . 1 . . . . . . . . 4353 1 320 . 1 1 52 52 GLN N N 15 119.37 0.1 . 1 . . . . . . . . 4353 1 321 . 1 1 53 53 ARG H H 1 8.6 0.01 . 1 . . . . . . . . 4353 1 322 . 1 1 53 53 ARG CA C 13 55.41 0.2 . 1 . . . . . . . . 4353 1 323 . 1 1 53 53 ARG CB C 13 32.51 0.2 . 1 . . . . . . . . 4353 1 324 . 1 1 53 53 ARG N N 15 122.19 0.1 . 1 . . . . . . . . 4353 1 325 . 1 1 54 54 GLN HA H 1 3.79 0.01 . 1 . . . . . . . . 4353 1 326 . 1 1 54 54 GLN C C 13 174.9 0.1 . 1 . . . . . . . . 4353 1 327 . 1 1 54 54 GLN CA C 13 56.86 0.2 . 1 . . . . . . . . 4353 1 328 . 1 1 54 54 GLN CB C 13 25.66 0.2 . 1 . . . . . . . . 4353 1 329 . 1 1 55 55 ILE H H 1 7.87 0.01 . 1 . . . . . . . . 4353 1 330 . 1 1 55 55 ILE HA H 1 4.09 0.01 . 1 . . . . . . . . 4353 1 331 . 1 1 55 55 ILE HB H 1 1.61 0.01 . 1 . . . . . . . . 4353 1 332 . 1 1 55 55 ILE HG21 H 1 1.96 0.01 . 2 . . . . . . . . 4353 1 333 . 1 1 55 55 ILE HG22 H 1 1.96 0.01 . 2 . . . . . . . . 4353 1 334 . 1 1 55 55 ILE HG23 H 1 1.96 0.01 . 2 . . . . . . . . 4353 1 335 . 1 1 55 55 ILE HD11 H 1 0.93 0.01 . 2 . . . . . . . . 4353 1 336 . 1 1 55 55 ILE HD12 H 1 0.93 0.01 . 2 . . . . . . . . 4353 1 337 . 1 1 55 55 ILE HD13 H 1 0.93 0.01 . 2 . . . . . . . . 4353 1 338 . 1 1 55 55 ILE C C 13 175.5 0.1 . 1 . . . . . . . . 4353 1 339 . 1 1 55 55 ILE CA C 13 60.57 0.2 . 1 . . . . . . . . 4353 1 340 . 1 1 55 55 ILE CB C 13 38.71 0.2 . 1 . . . . . . . . 4353 1 341 . 1 1 55 55 ILE N N 15 120.79 0.1 . 1 . . . . . . . . 4353 1 342 . 1 1 56 56 ALA H H 1 8.46 0.01 . 1 . . . . . . . . 4353 1 343 . 1 1 56 56 ALA HA H 1 4.12 0.01 . 1 . . . . . . . . 4353 1 344 . 1 1 56 56 ALA HB1 H 1 1.46 0.01 . 1 . . . . . . . . 4353 1 345 . 1 1 56 56 ALA HB2 H 1 1.46 0.01 . 1 . . . . . . . . 4353 1 346 . 1 1 56 56 ALA HB3 H 1 1.46 0.01 . 1 . . . . . . . . 4353 1 347 . 1 1 56 56 ALA C C 13 178.7 0.1 . 1 . . . . . . . . 4353 1 348 . 1 1 56 56 ALA CA C 13 53.38 0.2 . 1 . . . . . . . . 4353 1 349 . 1 1 56 56 ALA CB C 13 18.61 0.2 . 1 . . . . . . . . 4353 1 350 . 1 1 56 56 ALA N N 15 131.17 0.1 . 1 . . . . . . . . 4353 1 351 . 1 1 57 57 ALA H H 1 8.5 0.01 . 1 . . . . . . . . 4353 1 352 . 1 1 57 57 ALA HA H 1 4.56 0.01 . 1 . . . . . . . . 4353 1 353 . 1 1 57 57 ALA HB1 H 1 1.4 0.01 . 1 . . . . . . . . 4353 1 354 . 1 1 57 57 ALA HB2 H 1 1.4 0.01 . 1 . . . . . . . . 4353 1 355 . 1 1 57 57 ALA HB3 H 1 1.4 0.01 . 1 . . . . . . . . 4353 1 356 . 1 1 57 57 ALA C C 13 177.9 0.1 . 1 . . . . . . . . 4353 1 357 . 1 1 57 57 ALA CA C 13 51.38 0.2 . 1 . . . . . . . . 4353 1 358 . 1 1 57 57 ALA CB C 13 19.45 0.2 . 1 . . . . . . . . 4353 1 359 . 1 1 57 57 ALA N N 15 124.29 0.1 . 1 . . . . . . . . 4353 1 360 . 1 1 58 58 ASP H H 1 8.15 0.01 . 1 . . . . . . . . 4353 1 361 . 1 1 58 58 ASP HA H 1 4.22 0.01 . 1 . . . . . . . . 4353 1 362 . 1 1 58 58 ASP HB2 H 1 2.62 0.01 . 2 . . . . . . . . 4353 1 363 . 1 1 58 58 ASP HB3 H 1 2.44 0.01 . 2 . . . . . . . . 4353 1 364 . 1 1 58 58 ASP C C 13 177.1 0.1 . 1 . . . . . . . . 4353 1 365 . 1 1 58 58 ASP CA C 13 57.32 0.2 . 1 . . . . . . . . 4353 1 366 . 1 1 58 58 ASP CB C 13 40.32 0.2 . 1 . . . . . . . . 4353 1 367 . 1 1 58 58 ASP N N 15 120.36 0.2 . 1 . . . . . . . . 4353 1 368 . 1 1 59 59 MET H H 1 8.53 0.01 . 1 . . . . . . . . 4353 1 369 . 1 1 59 59 MET HA H 1 4.85 0.01 . 1 . . . . . . . . 4353 1 370 . 1 1 59 59 MET C C 13 174.4 0.1 . 1 . . . . . . . . 4353 1 371 . 1 1 59 59 MET CA C 13 52.73 0.2 . 1 . . . . . . . . 4353 1 372 . 1 1 59 59 MET CB C 13 37.7 0.2 . 1 . . . . . . . . 4353 1 373 . 1 1 59 59 MET N N 15 113.75 0.1 . 1 . . . . . . . . 4353 1 374 . 1 1 60 60 LEU H H 1 7.36 0.01 . 1 . . . . . . . . 4353 1 375 . 1 1 60 60 LEU HA H 1 4.38 0.01 . 1 . . . . . . . . 4353 1 376 . 1 1 60 60 LEU HB2 H 1 1.88 0.01 . 1 . . . . . . . . 4353 1 377 . 1 1 60 60 LEU HB3 H 1 1.88 0.01 . 1 . . . . . . . . 4353 1 378 . 1 1 60 60 LEU C C 13 177.3 0.1 . 1 . . . . . . . . 4353 1 379 . 1 1 60 60 LEU CA C 13 56.61 0.2 . 1 . . . . . . . . 4353 1 380 . 1 1 60 60 LEU CB C 13 43.22 0.2 . 1 . . . . . . . . 4353 1 381 . 1 1 60 60 LEU N N 15 122.88 0.1 . 1 . . . . . . . . 4353 1 382 . 1 1 61 61 THR H H 1 9.66 0.01 . 1 . . . . . . . . 4353 1 383 . 1 1 61 61 THR HA H 1 4.72 0.01 . 1 . . . . . . . . 4353 1 384 . 1 1 61 61 THR HG21 H 1 1.37 0.01 . 1 . . . . . . . . 4353 1 385 . 1 1 61 61 THR HG22 H 1 1.37 0.01 . 1 . . . . . . . . 4353 1 386 . 1 1 61 61 THR HG23 H 1 1.37 0.01 . 1 . . . . . . . . 4353 1 387 . 1 1 61 61 THR C C 13 172.8 0.1 . 1 . . . . . . . . 4353 1 388 . 1 1 61 61 THR CA C 13 62.17 0.2 . 1 . . . . . . . . 4353 1 389 . 1 1 61 61 THR CB C 13 72.45 0.2 . 1 . . . . . . . . 4353 1 390 . 1 1 61 61 THR N N 15 125.7 0.1 . 1 . . . . . . . . 4353 1 391 . 1 1 62 62 GLN H H 1 9.12 0.01 . 1 . . . . . . . . 4353 1 392 . 1 1 62 62 GLN HA H 1 4.91 0.01 . 1 . . . . . . . . 4353 1 393 . 1 1 62 62 GLN C C 13 176.3 0.1 . 1 . . . . . . . . 4353 1 394 . 1 1 62 62 GLN CA C 13 56.8 0.2 . 1 . . . . . . . . 4353 1 395 . 1 1 62 62 GLN CB C 13 29.6 0.2 . 1 . . . . . . . . 4353 1 396 . 1 1 62 62 GLN N N 15 129.62 0.1 . 1 . . . . . . . . 4353 1 397 . 1 1 62 62 GLN NE2 N 15 111.94 0.1 . 1 . . . . . . . . 4353 1 398 . 1 1 62 62 GLN HE21 H 1 7.71 0.01 . 2 . . . . . . . . 4353 1 399 . 1 1 62 62 GLN HE22 H 1 6.89 0.01 . 2 . . . . . . . . 4353 1 400 . 1 1 63 63 LEU H H 1 8.71 0.01 . 1 . . . . . . . . 4353 1 401 . 1 1 63 63 LEU HA H 1 4.77 0.01 . 1 . . . . . . . . 4353 1 402 . 1 1 63 63 LEU C C 13 175.9 0.1 . 1 . . . . . . . . 4353 1 403 . 1 1 63 63 LEU CA C 13 53.3 0.2 . 1 . . . . . . . . 4353 1 404 . 1 1 63 63 LEU CB C 13 41.42 0.2 . 1 . . . . . . . . 4353 1 405 . 1 1 63 63 LEU N N 15 128.5 0.1 . 1 . . . . . . . . 4353 1 406 . 1 1 64 64 THR H H 1 8.34 0.01 . 1 . . . . . . . . 4353 1 407 . 1 1 64 64 THR HA H 1 4 0.01 . 1 . . . . . . . . 4353 1 408 . 1 1 64 64 THR C C 13 173.8 0.1 . 1 . . . . . . . . 4353 1 409 . 1 1 64 64 THR CA C 13 64.9 0.2 . 1 . . . . . . . . 4353 1 410 . 1 1 64 64 THR CB C 13 69.49 0.2 . 1 . . . . . . . . 4353 1 411 . 1 1 64 64 THR N N 15 116.7 0.1 . 1 . . . . . . . . 4353 1 412 . 1 1 65 65 ALA H H 1 8.31 0.01 . 1 . . . . . . . . 4353 1 413 . 1 1 65 65 ALA HA H 1 4.9 0.01 . 1 . . . . . . . . 4353 1 414 . 1 1 65 65 ALA HB1 H 1 1.37 0.01 . 1 . . . . . . . . 4353 1 415 . 1 1 65 65 ALA HB2 H 1 1.37 0.01 . 1 . . . . . . . . 4353 1 416 . 1 1 65 65 ALA HB3 H 1 1.37 0.01 . 1 . . . . . . . . 4353 1 417 . 1 1 65 65 ALA C C 13 177.7 0.1 . 1 . . . . . . . . 4353 1 418 . 1 1 65 65 ALA CA C 13 51.99 0.2 . 1 . . . . . . . . 4353 1 419 . 1 1 65 65 ALA CB C 13 20.23 0.2 . 1 . . . . . . . . 4353 1 420 . 1 1 65 65 ALA N N 15 129.21 0.1 . 1 . . . . . . . . 4353 1 421 . 1 1 66 66 PHE H H 1 8.23 0.01 . 1 . . . . . . . . 4353 1 422 . 1 1 66 66 PHE HA H 1 4.92 0.01 . 1 . . . . . . . . 4353 1 423 . 1 1 66 66 PHE HB2 H 1 3.06 0.01 . 1 . . . . . . . . 4353 1 424 . 1 1 66 66 PHE HB3 H 1 3.06 0.01 . 1 . . . . . . . . 4353 1 425 . 1 1 66 66 PHE C C 13 172 0.1 . 1 . . . . . . . . 4353 1 426 . 1 1 66 66 PHE CA C 13 56.22 0.2 . 1 . . . . . . . . 4353 1 427 . 1 1 66 66 PHE CB C 13 40.87 0.2 . 1 . . . . . . . . 4353 1 428 . 1 1 66 66 PHE N N 15 116.7 0.1 . 1 . . . . . . . . 4353 1 429 . 1 1 67 67 ARG H H 1 8.47 0.01 . 1 . . . . . . . . 4353 1 430 . 1 1 67 67 ARG HA H 1 5.35 0.01 . 1 . . . . . . . . 4353 1 431 . 1 1 67 67 ARG C C 13 176.1 0.1 . 1 . . . . . . . . 4353 1 432 . 1 1 67 67 ARG CA C 13 54.99 0.2 . 1 . . . . . . . . 4353 1 433 . 1 1 67 67 ARG CB C 13 33.86 0.2 . 1 . . . . . . . . 4353 1 434 . 1 1 67 67 ARG N N 15 122.04 0.1 . 1 . . . . . . . . 4353 1 435 . 1 1 68 68 HIS H H 1 9.62 0.01 . 1 . . . . . . . . 4353 1 436 . 1 1 68 68 HIS CA C 13 55.98 0.2 . 1 . . . . . . . . 4353 1 437 . 1 1 68 68 HIS CB C 13 34.17 0.2 . 1 . . . . . . . . 4353 1 438 . 1 1 68 68 HIS N N 15 128.93 0.1 . 1 . . . . . . . . 4353 1 439 . 1 1 69 69 THR H H 1 8.33 0.01 . 1 . . . . . . . . 4353 1 440 . 1 1 69 69 THR HA H 1 4.44 0.01 . 1 . . . . . . . . 4353 1 441 . 1 1 69 69 THR HB H 1 3.67 0.01 . 1 . . . . . . . . 4353 1 442 . 1 1 69 69 THR HG21 H 1 1.14 0.01 . 1 . . . . . . . . 4353 1 443 . 1 1 69 69 THR HG22 H 1 1.14 0.01 . 1 . . . . . . . . 4353 1 444 . 1 1 69 69 THR HG23 H 1 1.14 0.01 . 1 . . . . . . . . 4353 1 445 . 1 1 69 69 THR CA C 13 64.58 0.2 . 1 . . . . . . . . 4353 1 446 . 1 1 69 69 THR CB C 13 70.51 0.2 . 1 . . . . . . . . 4353 1 447 . 1 1 69 69 THR CG2 C 13 22.8 0.2 . 1 . . . . . . . . 4353 1 448 . 1 1 69 69 THR N N 15 125.27 0.1 . 1 . . . . . . . . 4353 1 449 . 1 1 70 70 PHE H H 1 8.33 0.01 . 1 . . . . . . . . 4353 1 450 . 1 1 70 70 PHE CA C 13 56.79 0.2 . 1 . . . . . . . . 4353 1 451 . 1 1 70 70 PHE CB C 13 40.36 0.2 . 1 . . . . . . . . 4353 1 452 . 1 1 70 70 PHE N N 15 127.65 0.1 . 1 . . . . . . . . 4353 1 453 . 1 1 72 72 HIS C C 13 175.2 0.1 . 1 . . . . . . . . 4353 1 454 . 1 1 73 73 PHE H H 1 7.04 0.01 . 1 . . . . . . . . 4353 1 455 . 1 1 73 73 PHE C C 13 172.3 0.1 . 1 . . . . . . . . 4353 1 456 . 1 1 73 73 PHE CA C 13 57.07 0.2 . 1 . . . . . . . . 4353 1 457 . 1 1 73 73 PHE CB C 13 39.35 0.2 . 1 . . . . . . . . 4353 1 458 . 1 1 73 73 PHE N N 15 115.02 0.1 . 1 . . . . . . . . 4353 1 459 . 1 1 74 74 HIS H H 1 8.84 0.01 . 1 . . . . . . . . 4353 1 460 . 1 1 74 74 HIS HA H 1 5.06 0.01 . 1 . . . . . . . . 4353 1 461 . 1 1 74 74 HIS HB2 H 1 2.97 0.01 . 2 . . . . . . . . 4353 1 462 . 1 1 74 74 HIS HB3 H 1 2.94 0.01 . 2 . . . . . . . . 4353 1 463 . 1 1 74 74 HIS C C 13 174 0.1 . 1 . . . . . . . . 4353 1 464 . 1 1 74 74 HIS CA C 13 55.44 0.2 . 1 . . . . . . . . 4353 1 465 . 1 1 74 74 HIS CB C 13 33.59 0.2 . 1 . . . . . . . . 4353 1 466 . 1 1 74 74 HIS N N 15 117.97 0.1 . 1 . . . . . . . . 4353 1 467 . 1 1 75 75 LEU H H 1 9.34 0.01 . 1 . . . . . . . . 4353 1 468 . 1 1 75 75 LEU HA H 1 5.25 0.01 . 1 . . . . . . . . 4353 1 469 . 1 1 75 75 LEU HB2 H 1 2.59 0.01 . 2 . . . . . . . . 4353 1 470 . 1 1 75 75 LEU HB3 H 1 2.37 0.01 . 2 . . . . . . . . 4353 1 471 . 1 1 75 75 LEU C C 13 174.7 0.1 . 1 . . . . . . . . 4353 1 472 . 1 1 75 75 LEU CA C 13 53.06 0.2 . 1 . . . . . . . . 4353 1 473 . 1 1 75 75 LEU CB C 13 46.04 0.2 . 1 . . . . . . . . 4353 1 474 . 1 1 75 75 LEU N N 15 125.2 0.1 . 1 . . . . . . . . 4353 1 475 . 1 1 76 76 ASP H H 1 9.29 0.01 . 1 . . . . . . . . 4353 1 476 . 1 1 76 76 ASP HA H 1 5.12 0.01 . 1 . . . . . . . . 4353 1 477 . 1 1 76 76 ASP HB2 H 1 2.54 0.01 . 1 . . . . . . . . 4353 1 478 . 1 1 76 76 ASP HB3 H 1 2.54 0.01 . 1 . . . . . . . . 4353 1 479 . 1 1 76 76 ASP C C 13 174.3 0.1 . 1 . . . . . . . . 4353 1 480 . 1 1 76 76 ASP CA C 13 54.69 0.2 . 1 . . . . . . . . 4353 1 481 . 1 1 76 76 ASP CB C 13 41.2 0.2 . 1 . . . . . . . . 4353 1 482 . 1 1 76 76 ASP N N 15 129.62 0.1 . 1 . . . . . . . . 4353 1 483 . 1 1 77 77 ILE H H 1 8.89 0.01 . 1 . . . . . . . . 4353 1 484 . 1 1 77 77 ILE HA H 1 4.1 0.01 . 1 . . . . . . . . 4353 1 485 . 1 1 77 77 ILE C C 13 174.6 0.1 . 1 . . . . . . . . 4353 1 486 . 1 1 77 77 ILE CA C 13 60.65 0.2 . 1 . . . . . . . . 4353 1 487 . 1 1 77 77 ILE CB C 13 37.64 0.2 . 1 . . . . . . . . 4353 1 488 . 1 1 77 77 ILE N N 15 126.12 0.1 . 1 . . . . . . . . 4353 1 489 . 1 1 78 78 VAL H H 1 8.48 0.01 . 1 . . . . . . . . 4353 1 490 . 1 1 78 78 VAL HA H 1 4.68 0.01 . 1 . . . . . . . . 4353 1 491 . 1 1 78 78 VAL HB H 1 2.3 0.01 . 1 . . . . . . . . 4353 1 492 . 1 1 78 78 VAL HG11 H 1 0.98 0.01 . 2 . . . . . . . . 4353 1 493 . 1 1 78 78 VAL HG12 H 1 0.98 0.01 . 2 . . . . . . . . 4353 1 494 . 1 1 78 78 VAL HG13 H 1 0.98 0.01 . 2 . . . . . . . . 4353 1 495 . 1 1 78 78 VAL HG21 H 1 0.96 0.01 . 2 . . . . . . . . 4353 1 496 . 1 1 78 78 VAL HG22 H 1 0.96 0.01 . 2 . . . . . . . . 4353 1 497 . 1 1 78 78 VAL HG23 H 1 0.96 0.01 . 2 . . . . . . . . 4353 1 498 . 1 1 78 78 VAL CA C 13 59.59 0.2 . 1 . . . . . . . . 4353 1 499 . 1 1 78 78 VAL CB C 13 31.74 0.2 . 1 . . . . . . . . 4353 1 500 . 1 1 78 78 VAL CG1 C 13 22.52 0.2 . 1 . . . . . . . . 4353 1 501 . 1 1 78 78 VAL CG2 C 13 22.52 0.2 . 1 . . . . . . . . 4353 1 502 . 1 1 78 78 VAL N N 15 127.71 0.1 . 1 . . . . . . . . 4353 1 503 . 1 1 79 79 PRO HA H 1 4.92 0.01 . 1 . . . . . . . . 4353 1 504 . 1 1 79 79 PRO C C 13 176 0.1 . 1 . . . . . . . . 4353 1 505 . 1 1 79 79 PRO CA C 13 60.57 0.2 . 1 . . . . . . . . 4353 1 506 . 1 1 79 79 PRO CB C 13 31.76 0.2 . 1 . . . . . . . . 4353 1 507 . 1 1 80 80 MET H H 1 9.19 0.01 . 1 . . . . . . . . 4353 1 508 . 1 1 80 80 MET HA H 1 5.27 0.01 . 1 . . . . . . . . 4353 1 509 . 1 1 80 80 MET HB2 H 1 2.61 0.01 . 1 . . . . . . . . 4353 1 510 . 1 1 80 80 MET HB3 H 1 2.61 0.01 . 1 . . . . . . . . 4353 1 511 . 1 1 80 80 MET HG2 H 1 1.96 0.01 . 1 . . . . . . . . 4353 1 512 . 1 1 80 80 MET HG3 H 1 1.96 0.01 . 1 . . . . . . . . 4353 1 513 . 1 1 80 80 MET C C 13 173.5 0.1 . 1 . . . . . . . . 4353 1 514 . 1 1 80 80 MET CA C 13 53.56 0.2 . 1 . . . . . . . . 4353 1 515 . 1 1 80 80 MET CB C 13 33.88 0.2 . 1 . . . . . . . . 4353 1 516 . 1 1 80 80 MET N N 15 123.32 0.1 . 1 . . . . . . . . 4353 1 517 . 1 1 81 81 TRP H H 1 9.6 0.01 . 1 . . . . . . . . 4353 1 518 . 1 1 81 81 TRP HA H 1 5.47 0.01 . 1 . . . . . . . . 4353 1 519 . 1 1 81 81 TRP HB2 H 1 3.39 0.01 . 2 . . . . . . . . 4353 1 520 . 1 1 81 81 TRP HB3 H 1 2.92 0.01 . 2 . . . . . . . . 4353 1 521 . 1 1 81 81 TRP C C 13 173.96 0.1 . 1 . . . . . . . . 4353 1 522 . 1 1 81 81 TRP CA C 13 55.96 0.2 . 1 . . . . . . . . 4353 1 523 . 1 1 81 81 TRP CB C 13 31.49 0.2 . 1 . . . . . . . . 4353 1 524 . 1 1 81 81 TRP N N 15 127.53 0.1 . 1 . . . . . . . . 4353 1 525 . 1 1 82 82 LEU H H 1 8.64 0.01 . 1 . . . . . . . . 4353 1 526 . 1 1 82 82 LEU CA C 13 51.11 0.2 . 1 . . . . . . . . 4353 1 527 . 1 1 82 82 LEU CB C 13 46.05 0.2 . 1 . . . . . . . . 4353 1 528 . 1 1 82 82 LEU N N 15 129.35 0.1 . 1 . . . . . . . . 4353 1 529 . 1 1 84 84 VAL HA H 1 4.70 0.01 . 1 . . . . . . . . 4353 1 530 . 1 1 84 84 VAL HB H 1 2.32 0.01 . 1 . . . . . . . . 4353 1 531 . 1 1 84 84 VAL HG11 H 1 0.99 0.01 . 1 . . . . . . . . 4353 1 532 . 1 1 84 84 VAL HG12 H 1 0.99 0.01 . 1 . . . . . . . . 4353 1 533 . 1 1 84 84 VAL HG13 H 1 0.99 0.01 . 1 . . . . . . . . 4353 1 534 . 1 1 84 84 VAL HG21 H 1 0.99 0.01 . 1 . . . . . . . . 4353 1 535 . 1 1 84 84 VAL HG22 H 1 0.99 0.01 . 1 . . . . . . . . 4353 1 536 . 1 1 84 84 VAL HG23 H 1 0.99 0.01 . 1 . . . . . . . . 4353 1 537 . 1 1 84 84 VAL CA C 13 59.5 0.2 . 1 . . . . . . . . 4353 1 538 . 1 1 84 84 VAL CB C 13 35.6 0.2 . 1 . . . . . . . . 4353 1 539 . 1 1 84 84 VAL CG1 C 13 22.83 0.2 . 1 . . . . . . . . 4353 1 540 . 1 1 84 84 VAL CG2 C 13 22.83 0.2 . 1 . . . . . . . . 4353 1 541 . 1 1 85 85 SER HA H 1 4.65 0.01 . 1 . . . . . . . . 4353 1 542 . 1 1 85 85 SER HB2 H 1 3.96 0.01 . 2 . . . . . . . . 4353 1 543 . 1 1 85 85 SER HB3 H 1 3.92 0.01 . 2 . . . . . . . . 4353 1 544 . 1 1 85 85 SER C C 13 174.5 0.1 . 1 . . . . . . . . 4353 1 545 . 1 1 85 85 SER CA C 13 59.16 0.2 . 1 . . . . . . . . 4353 1 546 . 1 1 85 85 SER CB C 13 63.55 0.2 . 1 . . . . . . . . 4353 1 547 . 1 1 86 86 SER H H 1 7.7 0.01 . 1 . . . . . . . . 4353 1 548 . 1 1 86 86 SER HA H 1 4.33 0.01 . 1 . . . . . . . . 4353 1 549 . 1 1 86 86 SER HB2 H 1 3.76 0.01 . 1 . . . . . . . . 4353 1 550 . 1 1 86 86 SER HB3 H 1 3.76 0.01 . 1 . . . . . . . . 4353 1 551 . 1 1 86 86 SER C C 13 172.8 0.1 . 1 . . . . . . . . 4353 1 552 . 1 1 86 86 SER CA C 13 57.36 0.2 . 1 . . . . . . . . 4353 1 553 . 1 1 86 86 SER CB C 13 64.34 0.2 . 1 . . . . . . . . 4353 1 554 . 1 1 86 86 SER N N 15 114.32 0.1 . 1 . . . . . . . . 4353 1 555 . 1 1 87 87 PHE H H 1 8.3 0.01 . 1 . . . . . . . . 4353 1 556 . 1 1 87 87 PHE HA H 1 4.67 0.01 . 1 . . . . . . . . 4353 1 557 . 1 1 87 87 PHE HB2 H 1 2.76 0.01 . 2 . . . . . . . . 4353 1 558 . 1 1 87 87 PHE HB3 H 1 2.68 0.01 . 2 . . . . . . . . 4353 1 559 . 1 1 87 87 PHE C C 13 175.3 0.1 . 1 . . . . . . . . 4353 1 560 . 1 1 87 87 PHE CA C 13 57.59 0.2 . 1 . . . . . . . . 4353 1 561 . 1 1 87 87 PHE CB C 13 40.08 0.2 . 1 . . . . . . . . 4353 1 562 . 1 1 87 87 PHE N N 15 121.35 0.1 . 1 . . . . . . . . 4353 1 563 . 1 1 88 88 THR H H 1 8.15 0.01 . 1 . . . . . . . . 4353 1 564 . 1 1 88 88 THR HA H 1 4.29 0.01 . 1 . . . . . . . . 4353 1 565 . 1 1 88 88 THR HB H 1 4.16 0.01 . 1 . . . . . . . . 4353 1 566 . 1 1 88 88 THR HG21 H 1 1.1 0.01 . 1 . . . . . . . . 4353 1 567 . 1 1 88 88 THR HG22 H 1 1.1 0.01 . 1 . . . . . . . . 4353 1 568 . 1 1 88 88 THR HG23 H 1 1.1 0.01 . 1 . . . . . . . . 4353 1 569 . 1 1 88 88 THR C C 13 174.76 0.1 . 1 . . . . . . . . 4353 1 570 . 1 1 88 88 THR CA C 13 61.96 0.2 . 1 . . . . . . . . 4353 1 571 . 1 1 88 88 THR CB C 13 69.72 0.2 . 1 . . . . . . . . 4353 1 572 . 1 1 88 88 THR CG2 C 13 21.31 0.2 . 1 . . . . . . . . 4353 1 573 . 1 1 88 88 THR N N 15 117.83 0.1 . 1 . . . . . . . . 4353 1 574 . 1 1 89 89 GLY H H 1 7.57 0.01 . 1 . . . . . . . . 4353 1 575 . 1 1 89 89 GLY HA2 H 1 3.97 0.01 . 1 . . . . . . . . 4353 1 576 . 1 1 89 89 GLY HA3 H 1 3.97 0.01 . 1 . . . . . . . . 4353 1 577 . 1 1 89 89 GLY CA C 13 45.24 0.2 . 1 . . . . . . . . 4353 1 578 . 1 1 89 89 GLY N N 15 110.53 0.1 . 1 . . . . . . . . 4353 1 579 . 1 1 90 90 CYS H H 1 8.33 0.01 . 1 . . . . . . . . 4353 1 580 . 1 1 90 90 CYS CA C 13 58.95 0.2 . 1 . . . . . . . . 4353 1 581 . 1 1 90 90 CYS CB C 13 27.99 0.2 . 1 . . . . . . . . 4353 1 582 . 1 1 90 90 CYS N N 15 117.98 0.1 . 1 . . . . . . . . 4353 1 583 . 1 1 91 91 MET HA H 1 4.67 0.01 . 1 . . . . . . . . 4353 1 584 . 1 1 91 91 MET C C 13 176 0.1 . 1 . . . . . . . . 4353 1 585 . 1 1 91 91 MET CA C 13 55.68 0.2 . 1 . . . . . . . . 4353 1 586 . 1 1 91 91 MET CB C 13 32.29 0.2 . 1 . . . . . . . . 4353 1 587 . 1 1 92 92 ASP H H 1 8.46 0.01 . 1 . . . . . . . . 4353 1 588 . 1 1 92 92 ASP HA H 1 4.66 0.01 . 1 . . . . . . . . 4353 1 589 . 1 1 92 92 ASP HB2 H 1 2.72 0.01 . 2 . . . . . . . . 4353 1 590 . 1 1 92 92 ASP HB3 H 1 2.67 0.01 . 2 . . . . . . . . 4353 1 591 . 1 1 92 92 ASP C C 13 176.3 0.1 . 1 . . . . . . . . 4353 1 592 . 1 1 92 92 ASP CA C 13 54.66 0.2 . 1 . . . . . . . . 4353 1 593 . 1 1 92 92 ASP CB C 13 40.9 0.2 . 1 . . . . . . . . 4353 1 594 . 1 1 92 92 ASP N N 15 121.34 0.1 . 1 . . . . . . . . 4353 1 595 . 1 1 93 93 GLU H H 1 8.23 0.01 . 1 . . . . . . . . 4353 1 596 . 1 1 93 93 GLU HA H 1 4.4 0.01 . 1 . . . . . . . . 4353 1 597 . 1 1 93 93 GLU HB2 H 1 2.13 0.01 . 2 . . . . . . . . 4353 1 598 . 1 1 93 93 GLU HB3 H 1 2.03 0.01 . 2 . . . . . . . . 4353 1 599 . 1 1 93 93 GLU HG2 H 1 2.31 0.01 . 1 . . . . . . . . 4353 1 600 . 1 1 93 93 GLU HG3 H 1 2.31 0.01 . 1 . . . . . . . . 4353 1 601 . 1 1 93 93 GLU C C 13 177.3 0.1 . 1 . . . . . . . . 4353 1 602 . 1 1 93 93 GLU CA C 13 56.61 0.2 . 1 . . . . . . . . 4353 1 603 . 1 1 93 93 GLU CB C 13 30.29 0.2 . 1 . . . . . . . . 4353 1 604 . 1 1 93 93 GLU CG C 13 36.45 0.2 . 1 . . . . . . . . 4353 1 605 . 1 1 93 93 GLU N N 15 120.78 0.1 . 1 . . . . . . . . 4353 1 606 . 1 1 94 94 GLY H H 1 8.6 0.01 . 1 . . . . . . . . 4353 1 607 . 1 1 94 94 GLY HA2 H 1 3.97 0.01 . 2 . . . . . . . . 4353 1 608 . 1 1 94 94 GLY HA3 H 1 3.92 0.01 . 2 . . . . . . . . 4353 1 609 . 1 1 94 94 GLY C C 13 174.9 0.1 . 1 . . . . . . . . 4353 1 610 . 1 1 94 94 GLY CA C 13 46.02 0.2 . 1 . . . . . . . . 4353 1 611 . 1 1 94 94 GLY N N 15 110.67 0.1 . 1 . . . . . . . . 4353 1 612 . 1 1 95 95 ASN H H 1 8.52 0.01 . 1 . . . . . . . . 4353 1 613 . 1 1 95 95 ASN HA H 1 4.81 0.01 . 1 . . . . . . . . 4353 1 614 . 1 1 95 95 ASN C C 13 174.3 0.1 . 1 . . . . . . . . 4353 1 615 . 1 1 95 95 ASN CA C 13 53.26 0.2 . 1 . . . . . . . . 4353 1 616 . 1 1 95 95 ASN CB C 13 38.21 0.2 . 1 . . . . . . . . 4353 1 617 . 1 1 95 95 ASN N N 15 118.81 0.1 . 1 . . . . . . . . 4353 1 618 . 1 1 95 95 ASN ND2 N 15 112.25 0.1 . 1 . . . . . . . . 4353 1 619 . 1 1 95 95 ASN HD21 H 1 7.49 0.01 . 2 . . . . . . . . 4353 1 620 . 1 1 95 95 ASN HD22 H 1 6.89 0.01 . 2 . . . . . . . . 4353 1 621 . 1 1 96 96 ALA H H 1 7.82 0.01 . 1 . . . . . . . . 4353 1 622 . 1 1 96 96 ALA HA H 1 4.99 0.01 . 1 . . . . . . . . 4353 1 623 . 1 1 96 96 ALA HB1 H 1 1.37 0.01 . 1 . . . . . . . . 4353 1 624 . 1 1 96 96 ALA HB2 H 1 1.37 0.01 . 1 . . . . . . . . 4353 1 625 . 1 1 96 96 ALA HB3 H 1 1.37 0.01 . 1 . . . . . . . . 4353 1 626 . 1 1 96 96 ALA C C 13 176.4 0.1 . 1 . . . . . . . . 4353 1 627 . 1 1 96 96 ALA CA C 13 51.95 0.2 . 1 . . . . . . . . 4353 1 628 . 1 1 96 96 ALA CB C 13 21.19 0.2 . 1 . . . . . . . . 4353 1 629 . 1 1 96 96 ALA N N 15 122.73 0.1 . 1 . . . . . . . . 4353 1 630 . 1 1 97 97 LEU H H 1 9.03 0.01 . 1 . . . . . . . . 4353 1 631 . 1 1 97 97 LEU HA H 1 4.61 0.01 . 1 . . . . . . . . 4353 1 632 . 1 1 97 97 LEU C C 13 174.8 0.1 . 1 . . . . . . . . 4353 1 633 . 1 1 97 97 LEU CA C 13 54.36 0.2 . 1 . . . . . . . . 4353 1 634 . 1 1 97 97 LEU CB C 13 46 0.2 . 1 . . . . . . . . 4353 1 635 . 1 1 97 97 LEU N N 15 122.18 0.1 . 1 . . . . . . . . 4353 1 636 . 1 1 98 98 TRP H H 1 8.78 0.01 . 1 . . . . . . . . 4353 1 637 . 1 1 98 98 TRP HA H 1 4.85 0.01 . 1 . . . . . . . . 4353 1 638 . 1 1 98 98 TRP HB2 H 1 3.16 0.01 . 2 . . . . . . . . 4353 1 639 . 1 1 98 98 TRP HB3 H 1 3.06 0.01 . 2 . . . . . . . . 4353 1 640 . 1 1 98 98 TRP C C 13 175.1 0.1 . 1 . . . . . . . . 4353 1 641 . 1 1 98 98 TRP CA C 13 56.55 0.2 . 1 . . . . . . . . 4353 1 642 . 1 1 98 98 TRP CB C 13 28.51 0.2 . 1 . . . . . . . . 4353 1 643 . 1 1 98 98 TRP N N 15 125.7 0.1 . 1 . . . . . . . . 4353 1 644 . 1 1 99 99 TYR H H 1 9.71 0.01 . 1 . . . . . . . . 4353 1 645 . 1 1 99 99 TYR HA H 1 4.19 0.01 . 1 . . . . . . . . 4353 1 646 . 1 1 99 99 TYR C C 13 174.5 0.1 . 1 . . . . . . . . 4353 1 647 . 1 1 99 99 TYR CA C 13 57.83 0.2 . 1 . . . . . . . . 4353 1 648 . 1 1 99 99 TYR CB C 13 40.39 0.2 . 1 . . . . . . . . 4353 1 649 . 1 1 99 99 TYR N N 15 131.03 0.1 . 1 . . . . . . . . 4353 1 650 . 1 1 100 100 ASN H H 1 8.32 0.01 . 1 . . . . . . . . 4353 1 651 . 1 1 100 100 ASN HA H 1 4.77 0.01 . 1 . . . . . . . . 4353 1 652 . 1 1 100 100 ASN C C 13 174.5 0.1 . 1 . . . . . . . . 4353 1 653 . 1 1 100 100 ASN CA C 13 54.36 0.2 . 1 . . . . . . . . 4353 1 654 . 1 1 100 100 ASN CB C 13 39.55 0.2 . 1 . . . . . . . . 4353 1 655 . 1 1 100 100 ASN N N 15 129.64 0.1 . 1 . . . . . . . . 4353 1 656 . 1 1 101 101 LEU H H 1 9.09 0.01 . 1 . . . . . . . . 4353 1 657 . 1 1 101 101 LEU HA H 1 4.01 0.01 . 1 . . . . . . . . 4353 1 658 . 1 1 101 101 LEU C C 13 178.8 0.1 . 1 . . . . . . . . 4353 1 659 . 1 1 101 101 LEU CA C 13 57.37 0.2 . 1 . . . . . . . . 4353 1 660 . 1 1 101 101 LEU CB C 13 42.78 0.2 . 1 . . . . . . . . 4353 1 661 . 1 1 101 101 LEU N N 15 124.01 0.1 . 1 . . . . . . . . 4353 1 662 . 1 1 102 102 ALA H H 1 8.08 0.01 . 1 . . . . . . . . 4353 1 663 . 1 1 102 102 ALA HA H 1 4.4 0.01 . 1 . . . . . . . . 4353 1 664 . 1 1 102 102 ALA HB1 H 1 1.46 0.01 . 1 . . . . . . . . 4353 1 665 . 1 1 102 102 ALA HB2 H 1 1.46 0.01 . 1 . . . . . . . . 4353 1 666 . 1 1 102 102 ALA HB3 H 1 1.46 0.01 . 1 . . . . . . . . 4353 1 667 . 1 1 102 102 ALA C C 13 178.1 0.1 . 1 . . . . . . . . 4353 1 668 . 1 1 102 102 ALA CA C 13 53.02 0.2 . 1 . . . . . . . . 4353 1 669 . 1 1 102 102 ALA CB C 13 19.31 0.2 . 1 . . . . . . . . 4353 1 670 . 1 1 102 102 ALA N N 15 120.07 0.1 . 1 . . . . . . . . 4353 1 671 . 1 1 103 103 GLN H H 1 7.64 0.01 . 1 . . . . . . . . 4353 1 672 . 1 1 103 103 GLN HA H 1 4.58 0.01 . 1 . . . . . . . . 4353 1 673 . 1 1 103 103 GLN HB2 H 1 1.94 0.01 . 2 . . . . . . . . 4353 1 674 . 1 1 103 103 GLN HB3 H 1 1.75 0.01 . 2 . . . . . . . . 4353 1 675 . 1 1 103 103 GLN HG2 H 1 2.18 0.01 . 1 . . . . . . . . 4353 1 676 . 1 1 103 103 GLN HG3 H 1 2.18 0.01 . 1 . . . . . . . . 4353 1 677 . 1 1 103 103 GLN CA C 13 53 0.2 . 1 . . . . . . . . 4353 1 678 . 1 1 103 103 GLN CB C 13 29.05 0.2 . 1 . . . . . . . . 4353 1 679 . 1 1 103 103 GLN CG C 13 33.6 0.2 . 1 . . . . . . . . 4353 1 680 . 1 1 103 103 GLN N N 15 118.39 0.1 . 1 . . . . . . . . 4353 1 681 . 1 1 103 103 GLN NE2 N 15 111.68 0.1 . 1 . . . . . . . . 4353 1 682 . 1 1 103 103 GLN HE21 H 1 7.43 0.01 . 2 . . . . . . . . 4353 1 683 . 1 1 103 103 GLN HE22 H 1 6.76 0.01 . 2 . . . . . . . . 4353 1 684 . 1 1 105 105 PRO CA C 13 61.7 0.2 . 1 . . . . . . . . 4353 1 685 . 1 1 105 105 PRO CB C 13 31.98 0.2 . 1 . . . . . . . . 4353 1 686 . 1 1 106 106 SER H H 1 8.66 0.01 . 1 . . . . . . . . 4353 1 687 . 1 1 106 106 SER HA H 1 4.57 0.01 . 1 . . . . . . . . 4353 1 688 . 1 1 106 106 SER HB3 H 1 3.84 0.01 . 1 . . . . . . . . 4353 1 689 . 1 1 106 106 SER HB2 H 1 3.84 0.01 . 1 . . . . . . . . 4353 1 690 . 1 1 106 106 SER C C 13 174.3 0.1 . 1 . . . . . . . . 4353 1 691 . 1 1 106 106 SER CA C 13 57.35 0.2 . 1 . . . . . . . . 4353 1 692 . 1 1 106 106 SER CB C 13 62.74 0.2 . 1 . . . . . . . . 4353 1 693 . 1 1 106 106 SER N N 15 116.85 0.1 . 1 . . . . . . . . 4353 1 694 . 1 1 107 107 VAL H H 1 7.19 0.01 . 1 . . . . . . . . 4353 1 695 . 1 1 107 107 VAL HA H 1 4.57 0.01 . 1 . . . . . . . . 4353 1 696 . 1 1 107 107 VAL HB H 1 2.08 0.01 . 1 . . . . . . . . 4353 1 697 . 1 1 107 107 VAL HG11 H 1 0.61 0.01 . 2 . . . . . . . . 4353 1 698 . 1 1 107 107 VAL HG12 H 1 0.61 0.01 . 2 . . . . . . . . 4353 1 699 . 1 1 107 107 VAL HG13 H 1 0.61 0.01 . 2 . . . . . . . . 4353 1 700 . 1 1 107 107 VAL HG21 H 1 0.4 0.01 . 2 . . . . . . . . 4353 1 701 . 1 1 107 107 VAL HG22 H 1 0.4 0.01 . 2 . . . . . . . . 4353 1 702 . 1 1 107 107 VAL HG23 H 1 0.4 0.01 . 2 . . . . . . . . 4353 1 703 . 1 1 107 107 VAL C C 13 175.2 0.1 . 1 . . . . . . . . 4353 1 704 . 1 1 107 107 VAL CA C 13 59.28 0.2 . 1 . . . . . . . . 4353 1 705 . 1 1 107 107 VAL CB C 13 34.7 0.2 . 1 . . . . . . . . 4353 1 706 . 1 1 107 107 VAL CG1 C 13 21.63 0.2 . 1 . . . . . . . . 4353 1 707 . 1 1 107 107 VAL CG2 C 13 17.92 0.2 . 1 . . . . . . . . 4353 1 708 . 1 1 107 107 VAL N N 15 117 0.1 . 1 . . . . . . . . 4353 1 709 . 1 1 108 108 GLY H H 1 8.76 0.01 . 1 . . . . . . . . 4353 1 710 . 1 1 108 108 GLY HA2 H 1 4.11 0.01 . 2 . . . . . . . . 4353 1 711 . 1 1 108 108 GLY HA3 H 1 3.37 0.01 . 2 . . . . . . . . 4353 1 712 . 1 1 108 108 GLY C C 13 173.9 0.1 . 1 . . . . . . . . 4353 1 713 . 1 1 108 108 GLY CA C 13 46.28 0.2 . 1 . . . . . . . . 4353 1 714 . 1 1 108 108 GLY N N 15 109.97 0.1 . 1 . . . . . . . . 4353 1 715 . 1 1 109 109 LEU H H 1 8.56 0.01 . 1 . . . . . . . . 4353 1 716 . 1 1 109 109 LEU HA H 1 4.89 0.01 . 1 . . . . . . . . 4353 1 717 . 1 1 109 109 LEU C C 13 177.1 0.1 . 1 . . . . . . . . 4353 1 718 . 1 1 109 109 LEU CA C 13 53.02 0.2 . 1 . . . . . . . . 4353 1 719 . 1 1 109 109 LEU CB C 13 45.1 0.2 . 1 . . . . . . . . 4353 1 720 . 1 1 109 109 LEU N N 15 125.84 0.1 . 1 . . . . . . . . 4353 1 721 . 1 1 110 110 ALA H H 1 8.01 0.01 . 1 . . . . . . . . 4353 1 722 . 1 1 110 110 ALA HA H 1 3.87 0.01 . 1 . . . . . . . . 4353 1 723 . 1 1 110 110 ALA HB1 H 1 0.66 0.01 . 1 . . . . . . . . 4353 1 724 . 1 1 110 110 ALA HB2 H 1 0.66 0.01 . 1 . . . . . . . . 4353 1 725 . 1 1 110 110 ALA HB3 H 1 0.66 0.01 . 1 . . . . . . . . 4353 1 726 . 1 1 110 110 ALA CA C 13 51.42 0.2 . 1 . . . . . . . . 4353 1 727 . 1 1 110 110 ALA CB C 13 18.78 0.2 . 1 . . . . . . . . 4353 1 728 . 1 1 110 110 ALA N N 15 123.3 0.1 . 1 . . . . . . . . 4353 1 729 . 1 1 111 111 ALA H H 1 8.19 0.01 . 1 . . . . . . . . 4353 1 730 . 1 1 111 111 ALA HA H 1 4.59 0.01 . 1 . . . . . . . . 4353 1 731 . 1 1 111 111 ALA HB1 H 1 1.35 0.01 . 1 . . . . . . . . 4353 1 732 . 1 1 111 111 ALA HB2 H 1 1.35 0.01 . 1 . . . . . . . . 4353 1 733 . 1 1 111 111 ALA HB3 H 1 1.35 0.01 . 1 . . . . . . . . 4353 1 734 . 1 1 111 111 ALA CA C 13 50.21 0.2 . 1 . . . . . . . . 4353 1 735 . 1 1 111 111 ALA CB C 13 17.98 0.2 . 1 . . . . . . . . 4353 1 736 . 1 1 111 111 ALA N N 15 125.69 0.1 . 1 . . . . . . . . 4353 1 737 . 1 1 112 112 PRO HA H 1 4.54 0.01 . 1 . . . . . . . . 4353 1 738 . 1 1 112 112 PRO HB2 H 1 2.19 0.01 . 2 . . . . . . . . 4353 1 739 . 1 1 112 112 PRO HB3 H 1 1.61 0.01 . 2 . . . . . . . . 4353 1 740 . 1 1 112 112 PRO C C 13 176.6 0.1 . 1 . . . . . . . . 4353 1 741 . 1 1 112 112 PRO CA C 13 65.16 0.2 . 1 . . . . . . . . 4353 1 742 . 1 1 112 112 PRO CB C 13 31.76 0.2 . 1 . . . . . . . . 4353 1 743 . 1 1 113 113 VAL H H 1 7.39 0.01 . 1 . . . . . . . . 4353 1 744 . 1 1 113 113 VAL HA H 1 3.59 0.01 . 1 . . . . . . . . 4353 1 745 . 1 1 113 113 VAL C C 13 177.5 0.1 . 1 . . . . . . . . 4353 1 746 . 1 1 113 113 VAL CA C 13 66.75 0.2 . 1 . . . . . . . . 4353 1 747 . 1 1 113 113 VAL CB C 13 30.79 0.2 . 1 . . . . . . . . 4353 1 748 . 1 1 113 113 VAL N N 15 115.58 0.1 . 1 . . . . . . . . 4353 1 749 . 1 1 114 114 GLU H H 1 8.42 0.01 . 1 . . . . . . . . 4353 1 750 . 1 1 114 114 GLU HA H 1 3.86 0.01 . 1 . . . . . . . . 4353 1 751 . 1 1 114 114 GLU HB2 H 1 2.03 0.01 . 2 . . . . . . . . 4353 1 752 . 1 1 114 114 GLU HB3 H 1 1.97 0.01 . 2 . . . . . . . . 4353 1 753 . 1 1 114 114 GLU HG2 H 1 2.18 0.01 . 2 . . . . . . . . 4353 1 754 . 1 1 114 114 GLU HG3 H 1 2.15 0.01 . 2 . . . . . . . . 4353 1 755 . 1 1 114 114 GLU C C 13 178.56 0.1 . 1 . . . . . . . . 4353 1 756 . 1 1 114 114 GLU CA C 13 60.58 0.2 . 1 . . . . . . . . 4353 1 757 . 1 1 114 114 GLU CB C 13 28.8 0.2 . 1 . . . . . . . . 4353 1 758 . 1 1 114 114 GLU N N 15 120.21 0.1 . 1 . . . . . . . . 4353 1 759 . 1 1 115 115 ARG H H 1 8.15 0.01 . 1 . . . . . . . . 4353 1 760 . 1 1 115 115 ARG HA H 1 4.03 0.01 . 1 . . . . . . . . 4353 1 761 . 1 1 115 115 ARG HB2 H 1 1.75 0.01 . 2 . . . . . . . . 4353 1 762 . 1 1 115 115 ARG HB3 H 1 1.57 0.01 . 2 . . . . . . . . 4353 1 763 . 1 1 115 115 ARG HG2 H 1 1.4 0.01 . 2 . . . . . . . . 4353 1 764 . 1 1 115 115 ARG HG3 H 1 1.37 0.01 . 2 . . . . . . . . 4353 1 765 . 1 1 115 115 ARG HE H 1 2.76 0.01 . 1 . . . . . . . . 4353 1 766 . 1 1 115 115 ARG C C 13 179.2 0.1 . 1 . . . . . . . . 4353 1 767 . 1 1 115 115 ARG CA C 13 58.93 0.2 . 1 . . . . . . . . 4353 1 768 . 1 1 115 115 ARG CB C 13 29.68 0.2 . 1 . . . . . . . . 4353 1 769 . 1 1 115 115 ARG N N 15 118.1 0.1 . 1 . . . . . . . . 4353 1 770 . 1 1 116 116 LEU H H 1 7.4 0.01 . 1 . . . . . . . . 4353 1 771 . 1 1 116 116 LEU HA H 1 4.16 0.01 . 1 . . . . . . . . 4353 1 772 . 1 1 116 116 LEU C C 13 179.1 0.1 . 1 . . . . . . . . 4353 1 773 . 1 1 116 116 LEU CA C 13 57.58 0.2 . 1 . . . . . . . . 4353 1 774 . 1 1 116 116 LEU CB C 13 42.54 0.2 . 1 . . . . . . . . 4353 1 775 . 1 1 116 116 LEU N N 15 120.07 0.1 . 1 . . . . . . . . 4353 1 776 . 1 1 117 117 LEU H H 1 8.72 0.01 . 1 . . . . . . . . 4353 1 777 . 1 1 117 117 LEU C C 13 179.6 0.1 . 1 . . . . . . . . 4353 1 778 . 1 1 117 117 LEU CA C 13 58.4 0.2 . 1 . . . . . . . . 4353 1 779 . 1 1 117 117 LEU CB C 13 40.65 0.2 . 1 . . . . . . . . 4353 1 780 . 1 1 117 117 LEU N N 15 119.65 0.1 . 1 . . . . . . . . 4353 1 781 . 1 1 118 118 GLN H H 1 7.98 0.01 . 1 . . . . . . . . 4353 1 782 . 1 1 118 118 GLN HA H 1 4.05 0.01 . 1 . . . . . . . . 4353 1 783 . 1 1 118 118 GLN HB2 H 1 2.11 0.01 . 1 . . . . . . . . 4353 1 784 . 1 1 118 118 GLN HB3 H 1 2.11 0.01 . 1 . . . . . . . . 4353 1 785 . 1 1 118 118 GLN HG2 H 1 2.48 0.01 . 2 . . . . . . . . 4353 1 786 . 1 1 118 118 GLN HG3 H 1 2.42 0.01 . 2 . . . . . . . . 4353 1 787 . 1 1 118 118 GLN C C 13 178.9 0.1 . 1 . . . . . . . . 4353 1 788 . 1 1 118 118 GLN CA C 13 58.69 0.2 . 1 . . . . . . . . 4353 1 789 . 1 1 118 118 GLN CB C 13 27.7 0.2 . 1 . . . . . . . . 4353 1 790 . 1 1 118 118 GLN N N 15 117 0.1 . 1 . . . . . . . . 4353 1 791 . 1 1 119 119 GLN H H 1 7.47 0.01 . 1 . . . . . . . . 4353 1 792 . 1 1 119 119 GLN HA H 1 4.07 0.01 . 1 . . . . . . . . 4353 1 793 . 1 1 119 119 GLN C C 13 178.5 0.1 . 1 . . . . . . . . 4353 1 794 . 1 1 119 119 GLN CA C 13 58.43 0.2 . 1 . . . . . . . . 4353 1 795 . 1 1 119 119 GLN CB C 13 27.98 0.2 . 1 . . . . . . . . 4353 1 796 . 1 1 119 119 GLN N N 15 118.25 0.1 . 1 . . . . . . . . 4353 1 797 . 1 1 120 120 LEU H H 1 7.87 0.01 . 1 . . . . . . . . 4353 1 798 . 1 1 120 120 LEU HA H 1 3.97 0.01 . 1 . . . . . . . . 4353 1 799 . 1 1 120 120 LEU HB2 H 1 1.89 0.01 . 2 . . . . . . . . 4353 1 800 . 1 1 120 120 LEU HB3 H 1 1.42 0.01 . 2 . . . . . . . . 4353 1 801 . 1 1 120 120 LEU HG H 1 1.73 0.01 . 2 . . . . . . . . 4353 1 802 . 1 1 120 120 LEU HD11 H 1 0.8 0.01 . 2 . . . . . . . . 4353 1 803 . 1 1 120 120 LEU HD12 H 1 0.8 0.01 . 2 . . . . . . . . 4353 1 804 . 1 1 120 120 LEU HD13 H 1 0.8 0.01 . 2 . . . . . . . . 4353 1 805 . 1 1 120 120 LEU HD21 H 1 0.45 0.01 . 2 . . . . . . . . 4353 1 806 . 1 1 120 120 LEU HD22 H 1 0.45 0.01 . 2 . . . . . . . . 4353 1 807 . 1 1 120 120 LEU HD23 H 1 0.45 0.01 . 2 . . . . . . . . 4353 1 808 . 1 1 120 120 LEU C C 13 179.2 0.1 . 1 . . . . . . . . 4353 1 809 . 1 1 120 120 LEU CA C 13 56.76 0.2 . 1 . . . . . . . . 4353 1 810 . 1 1 120 120 LEU CB C 13 41.7 0.2 . 1 . . . . . . . . 4353 1 811 . 1 1 120 120 LEU CG C 13 26.59 0.2 . 1 . . . . . . . . 4353 1 812 . 1 1 120 120 LEU CD1 C 13 25.76 0.2 . 1 . . . . . . . . 4353 1 813 . 1 1 120 120 LEU CD2 C 13 22.08 0.2 . 1 . . . . . . . . 4353 1 814 . 1 1 120 120 LEU N N 15 119.22 0.1 . 1 . . . . . . . . 4353 1 815 . 1 1 121 121 ARG H H 1 8.14 0.01 . 1 . . . . . . . . 4353 1 816 . 1 1 121 121 ARG HA H 1 4.15 0.01 . 1 . . . . . . . . 4353 1 817 . 1 1 121 121 ARG C C 13 177.5 0.1 . 1 . . . . . . . . 4353 1 818 . 1 1 121 121 ARG CA C 13 58.4 0.2 . 1 . . . . . . . . 4353 1 819 . 1 1 121 121 ARG CB C 13 30.78 0.2 . 1 . . . . . . . . 4353 1 820 . 1 1 121 121 ARG N N 15 119.09 0.1 . 1 . . . . . . . . 4353 1 821 . 1 1 122 122 THR H H 1 7.71 0.01 . 1 . . . . . . . . 4353 1 822 . 1 1 122 122 THR HA H 1 4.29 0.01 . 1 . . . . . . . . 4353 1 823 . 1 1 122 122 THR C C 13 175.7 0.1 . 1 . . . . . . . . 4353 1 824 . 1 1 122 122 THR CA C 13 63 0.2 . 1 . . . . . . . . 4353 1 825 . 1 1 122 122 THR CB C 13 70.29 0.2 . 1 . . . . . . . . 4353 1 826 . 1 1 122 122 THR N N 15 110.39 0.1 . 1 . . . . . . . . 4353 1 827 . 1 1 123 123 GLY H H 1 7.87 0.01 . 1 . . . . . . . . 4353 1 828 . 1 1 123 123 GLY HA2 H 1 4.09 0.01 . 2 . . . . . . . . 4353 1 829 . 1 1 123 123 GLY HA3 H 1 3.85 0.01 . 2 . . . . . . . . 4353 1 830 . 1 1 123 123 GLY C C 13 172.96 0.1 . 1 . . . . . . . . 4353 1 831 . 1 1 123 123 GLY CA C 13 45.18 0.2 . 1 . . . . . . . . 4353 1 832 . 1 1 123 123 GLY N N 15 110.24 0.1 . 1 . . . . . . . . 4353 1 833 . 1 1 124 124 ALA H H 1 8.06 0.01 . 1 . . . . . . . . 4353 1 834 . 1 1 124 124 ALA HA H 1 4.52 0.01 . 1 . . . . . . . . 4353 1 835 . 1 1 124 124 ALA HB1 H 1 1.23 0.01 . 1 . . . . . . . . 4353 1 836 . 1 1 124 124 ALA HB2 H 1 1.23 0.01 . 1 . . . . . . . . 4353 1 837 . 1 1 124 124 ALA HB3 H 1 1.23 0.01 . 1 . . . . . . . . 4353 1 838 . 1 1 124 124 ALA CA C 13 50.3 0.2 . 1 . . . . . . . . 4353 1 839 . 1 1 124 124 ALA CB C 13 18.25 0.2 . 1 . . . . . . . . 4353 1 840 . 1 1 124 124 ALA N N 15 124.29 0.1 . 1 . . . . . . . . 4353 1 841 . 1 1 125 125 PRO HA H 1 4.31 0.01 . 1 . . . . . . . . 4353 1 842 . 1 1 125 125 PRO HB2 H 1 1.71 0.01 . 1 . . . . . . . . 4353 1 843 . 1 1 125 125 PRO HB3 H 1 1.77 0.01 . 1 . . . . . . . . 4353 1 844 . 1 1 125 125 PRO HG2 H 1 1.40 0.01 . 1 . . . . . . . . 4353 1 845 . 1 1 125 125 PRO HG3 H 1 1.18 0.01 . 1 . . . . . . . . 4353 1 846 . 1 1 125 125 PRO HD2 H 1 3.24 0.01 . 1 . . . . . . . . 4353 1 847 . 1 1 125 125 PRO HD3 H 1 3.05 0.01 . 1 . . . . . . . . 4353 1 848 . 1 1 125 125 PRO CA C 13 63.09 0.2 . 1 . . . . . . . . 4353 1 849 . 1 1 125 125 PRO CB C 13 31.73 0.2 . 1 . . . . . . . . 4353 1 850 . 1 1 125 125 PRO CG C 13 26.6 0.2 . 1 . . . . . . . . 4353 1 851 . 1 1 125 125 PRO CD C 13 50.0 0.2 . 1 . . . . . . . . 4353 1 852 . 1 1 126 126 VAL H H 1 7.55 0.01 . 1 . . . . . . . . 4353 1 853 . 1 1 126 126 VAL HA H 1 4.02 0.01 . 1 . . . . . . . . 4353 1 854 . 1 1 126 126 VAL HB H 1 2.01 0.01 . 1 . . . . . . . . 4353 1 855 . 1 1 126 126 VAL HG11 H 1 0.88 0.01 . 2 . . . . . . . . 4353 1 856 . 1 1 126 126 VAL HG12 H 1 0.88 0.01 . 2 . . . . . . . . 4353 1 857 . 1 1 126 126 VAL HG13 H 1 0.88 0.01 . 2 . . . . . . . . 4353 1 858 . 1 1 126 126 VAL HG21 H 1 0.87 0.01 . 2 . . . . . . . . 4353 1 859 . 1 1 126 126 VAL HG22 H 1 0.87 0.01 . 2 . . . . . . . . 4353 1 860 . 1 1 126 126 VAL HG23 H 1 0.87 0.01 . 2 . . . . . . . . 4353 1 861 . 1 1 126 126 VAL CA C 13 63.39 0.2 . 1 . . . . . . . . 4353 1 862 . 1 1 126 126 VAL CB C 13 33.8 0.2 . 1 . . . . . . . . 4353 1 863 . 1 1 126 126 VAL CG1 C 13 20.21 0.2 . 1 . . . . . . . . 4353 1 864 . 1 1 126 126 VAL CG2 C 13 21.67 0.2 . 1 . . . . . . . . 4353 1 865 . 1 1 126 126 VAL N N 15 122.04 0.1 . 1 . . . . . . . . 4353 1 stop_ save_