data_4353 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; 1H, 13C, and 15N Resonance Assignments of C-terminal Domain of MutY ; _BMRB_accession_number 4353 _BMRB_flat_file_name bmr4353.str _Entry_type original _Submission_date 1999-06-04 _Accession_date 1999-06-04 _Entry_origination author _NMR_STAR_version 2.1.1 _Experimental_method NMR _Details . loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Volk David E . 2 Thiviyanathan Varatharasa . . 3 House Paul G . 4 Lloyd Stephen . . 5 Gorenstein David G . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 360 "13C chemical shifts" 344 "15N chemical shifts" 101 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 1999-09-15 original author . stop_ _Original_release_date 1999-09-15 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full ; 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 _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID ? loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Volk David E . 2 Thiviyanathan Varatharasa . . 3 House Paul G . 4 Lloyd Stephen . . 5 Gorenstein David G . stop_ _Journal_abbreviation 'J. Biomol. NMR' _Journal_name_full 'Journal of Biomolecular NMR' _Journal_volume . _Journal_issue . _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first . _Page_last . _Year . _Details . loop_ _Keyword '8-oxo Guanosine' 'Adenine Glycosylase' 'G:A mismatch' stop_ save_ ####################################### # Cited references within the entry # ####################################### save_ref_1 _Saveframe_category citation _Citation_full ; 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 _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 9287157 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Manuel 'R C' C. . 2 Lloyd 'R S' S. . stop_ _Journal_abbreviation Biochemistry _Journal_name_full Biochemistry _Journal_volume 36 _Journal_issue 37 _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 11140 _Page_last 11152 _Year 1997 _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. ; save_ ################################## # Molecular system description # ################################## save_system _Saveframe_category molecular_system _Mol_system_name 'p13 c-terminal domain' _Abbreviation_common 'p13 monomer' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label protein $protein stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state monomer _System_paramagnetic no _System_thiol_state . loop_ _Biological_function ; The MutY protein, of which the p13_c-terminal_domain is a fragment, functions as a DNA glycosylase (Adenine glycosylase) ; stop_ _Database_query_date . _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 ; save_ ######################## # Monomeric polymers # ######################## save_protein _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'p13 c-terminal domain' _Name_variant 'p13 monomer' _Molecular_mass . _Mol_thiol_state . _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 126 _Mol_residue_sequence ; KQTLPERTGYFLLLQHEDEV LLAQRPPSGLWGGLYCFPQF ADEESLRQWLAQRQIAADML TQLTAFRHTFSHFHLDIVPM WLPVSSFTGCMDEGNALWYN LAQPPSVGLAAPVERLLQQL RTGAPV ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 225 LYS 2 226 GLN 3 227 THR 4 228 LEU 5 229 PRO 6 230 GLU 7 231 ARG 8 232 THR 9 233 GLY 10 234 TYR 11 235 PHE 12 236 LEU 13 237 LEU 14 248 LEU 15 239 GLN 16 240 HIS 17 241 GLU 18 242 ASP 19 243 GLU 20 244 VAL 21 245 LEU 22 246 LEU 23 247 ALA 24 248 GLN 25 249 ARG 26 250 PRO 27 251 PRO 28 252 SER 29 253 GLY 30 254 LEU 31 255 TRP 32 256 GLY 33 257 GLY 34 258 LEU 35 259 TYR 36 260 CYS 37 261 PHE 38 262 PRO 39 263 GLN 40 264 PHE 41 265 ALA 42 266 ASP 43 267 GLU 44 268 GLU 45 269 SER 46 270 LEU 47 271 ARG 48 272 GLN 49 273 TRP 50 274 LEU 51 275 ALA 52 276 GLN 53 277 ARG 54 278 GLN 55 279 ILE 56 280 ALA 57 281 ALA 58 282 ASP 59 283 MET 60 284 LEU 61 285 THR 62 286 GLN 63 287 LEU 64 288 THR 65 289 ALA 66 290 PHE 67 291 ARG 68 292 HIS 69 293 THR 70 294 PHE 71 295 SER 72 296 HIS 73 297 PHE 74 298 HIS 75 299 LEU 76 300 ASP 77 301 ILE 78 302 VAL 79 303 PRO 80 304 MET 81 305 TRP 82 306 LEU 83 307 PRO 84 308 VAL 85 309 SER 86 310 SER 87 311 PHE 88 312 THR 89 313 GLY 90 314 CYS 91 315 MET 92 316 ASP 93 317 GLU 94 318 GLY 95 319 ASN 96 320 ALA 97 321 LEU 98 322 TRP 99 323 TYR 100 324 ASN 101 325 LEU 102 326 ALA 103 327 GLN 104 328 PRO 105 329 PRO 106 330 SER 107 331 VAL 108 332 GLY 109 333 LEU 110 334 ALA 111 335 ALA 112 336 PRO 113 337 VAL 114 338 GLU 115 339 ARG 116 340 LEU 117 341 LEU 118 342 GLN 119 343 GLN 120 344 LEU 121 345 ARG 122 346 THR 123 347 GLY 124 348 ALA 125 349 PRO 126 350 VAL stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-09-15 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 DBJ BAB37260 "adenine glycosylase [Escherichia coli O157:H7 str. Sakai]" 100.00 350 99.21 99.21 3.90e-83 DBJ BAE77024 "adenine DNA glycosylase [Escherichia coli str. K12 substr. W3110]" 100.00 350 99.21 99.21 3.98e-83 DBJ BAG66699 "adenine DNA glycosylase [Escherichia coli O111:H-]" 100.00 350 98.41 98.41 2.00e-82 DBJ BAG78754 "adenine glycosylase [Escherichia coli SE11]" 100.00 350 99.21 99.21 4.07e-83 DBJ BAI27248 "adenine DNA glycosylase MutY [Escherichia coli O26:H11 str. 11368]" 100.00 350 99.21 99.21 3.98e-83 EMBL CAA36624 "unnamed protein product [Escherichia coli K-12]" 100.00 350 99.21 99.21 3.98e-83 EMBL CAP77398 "A/G-specific adenine glycosylase [Escherichia coli LF82]" 100.00 350 97.62 98.41 1.18e-81 EMBL CAQ33271 "adenine glycosylase; G.C--> T.A transversions [Escherichia coli BL21(DE3)]" 100.00 350 99.21 99.21 3.98e-83 EMBL CAQ90396 "adenine DNA glycosylase [Escherichia fergusonii ATCC 35469]" 100.00 350 97.62 97.62 9.82e-82 EMBL CAQ99909 "adenine DNA glycosylase [Escherichia coli IAI1]" 100.00 350 98.41 98.41 2.00e-82 GB AAA69128 "CG Site No. 18130; alternate name micA [Escherichia coli str. K-12 substr. MG1655]" 100.00 350 99.21 99.21 3.98e-83 GB AAA72957 "A/G-specific adenine glycosylase [Escherichia coli]" 100.00 350 99.21 99.21 3.98e-83 GB AAC75998 "adenine DNA glycosylase [Escherichia coli str. K-12 substr. MG1655]" 100.00 350 99.21 99.21 3.98e-83 GB AAG58092 "adenine glycosylase; G.C --> T.A transversions [Escherichia coli O157:H7 str. EDL933]" 100.00 350 99.21 99.21 3.90e-83 GB AAN44439 "adenine glycosylase [Shigella flexneri 2a str. 301]" 100.00 350 98.41 98.41 2.06e-82 REF NP_311864 "adenine DNA glycosylase [Escherichia coli O157:H7 str. Sakai]" 100.00 350 99.21 99.21 3.90e-83 REF NP_417436 "adenine DNA glycosylase [Escherichia coli str. K-12 substr. MG1655]" 100.00 350 99.21 99.21 3.98e-83 REF NP_708732 "adenine DNA glycosylase [Shigella flexneri 2a str. 301]" 100.00 350 98.41 98.41 2.06e-82 REF WP_001295382 "MULTISPECIES: A/G-specific adenine glycosylase [Enterobacteriaceae]" 100.00 350 99.21 99.21 4.07e-83 REF WP_001296362 "MULTISPECIES: A/G-specific adenine glycosylase [Enterobacteriaceae]" 100.00 350 98.41 98.41 4.55e-82 SP P17802 "RecName: Full=A/G-specific adenine glycosylase" 100.00 350 99.21 99.21 3.98e-83 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species _Cell_line _Cell_type $protein 'E. coli' 562 Eubacteria . Escherichia coli BL21 DE3 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 $protein 'recombinant technology' . . . . . stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Concentration_min_value _Concentration_max_value _Isotopic_labeling $protein . mM 0.7 1.3 '[U-95% 13C; U-95% 15N]' stop_ save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_list _Saveframe_category NMR_spectrometer _Manufacturer unknown _Model unknown _Field_strength 0 _Details 'spectrometer information not available' save_ ####################### # Sample conditions # ####################### save_sample_conditions_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 6.50 0.2 n/a temperature 298 0.5 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 H 1 'methyl protons' ppm 0.0 . indirect . . . 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 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $sample_conditions_1 _Chem_shift_reference_set_label $chemical_shift_reference_1 _Mol_system_component_name protein _Text_data_format . _Text_data . loop_ _Atom_shift_assign_ID _Residue_author_seq_code _Residue_seq_code _Residue_label _Atom_name _Atom_type _Chem_shift_value _Chem_shift_value_error _Chem_shift_ambiguity_code 1 . 1 LYS HA H 4.3 0.01 1 2 . 1 LYS HB2 H 1.82 0.01 2 3 . 1 LYS HB3 H 1.77 0.01 2 4 . 1 LYS HG2 H 1.45 0.01 2 5 . 1 LYS HG3 H 1.43 0.01 2 6 . 1 LYS HD2 H 1.69 0.01 1 7 . 1 LYS HD3 H 1.69 0.01 1 8 . 1 LYS HE2 H 2.98 0.01 1 9 . 1 LYS HE3 H 2.98 0.01 1 10 . 1 LYS CA C 56.4 0.2 1 11 . 1 LYS CB C 33.1 0.2 1 12 . 1 LYS CG C 24.7 0.2 1 13 . 1 LYS CD C 29 0.2 1 14 . 1 LYS CE C 41.8 0.2 1 15 . 3 THR HA H 4.4 0.01 1 16 . 3 THR HB H 4.18 0.01 1 17 . 3 THR HG2 H 1.21 0.01 1 18 . 3 THR CA C 61.5 0.2 1 19 . 3 THR CB C 69.7 0.2 1 20 . 3 THR CG2 C 21.54 0.2 1 21 . 5 PRO HA H 4.56 0.01 1 22 . 5 PRO HB2 H 2.42 0.01 2 23 . 5 PRO HB3 H 1.94 0.01 2 24 . 5 PRO HG2 H 2.2 0.01 1 25 . 5 PRO HG3 H 2.2 0.01 1 26 . 5 PRO C C 175.1 0.1 1 27 . 5 PRO CA C 63.05 0.2 1 28 . 5 PRO CB C 32.75 0.2 1 29 . 6 GLU H H 8.44 0.01 1 30 . 6 GLU HA H 5.14 0.01 1 31 . 6 GLU HB2 H 2.08 0.01 1 32 . 6 GLU HB3 H 2.08 0.01 1 33 . 6 GLU HG2 H 2.45 0.01 2 34 . 6 GLU HG3 H 2.2 0.01 2 35 . 6 GLU C C 176.2 0.1 1 36 . 6 GLU CA C 55.15 0.2 1 37 . 6 GLU CB C 31.75 0.2 1 38 . 6 GLU CG C 36.5 0.2 1 39 . 6 GLU N N 176.2 0.1 1 40 . 7 ARG H H 9.03 0.01 1 41 . 7 ARG HA H 4.81 0.01 1 42 . 7 ARG HB2 H 1.9 0.01 2 43 . 7 ARG HB3 H 1.76 0.01 2 44 . 7 ARG HG2 H 1.54 0.01 2 45 . 7 ARG HG3 H 1.44 0.01 2 46 . 7 ARG HD2 H 2.9 0.01 2 47 . 7 ARG HD3 H 2.64 0.01 2 48 . 7 ARG C C 174.9 0.1 1 49 . 7 ARG CA C 55.15 0.2 1 50 . 7 ARG CB C 33.35 0.2 1 51 . 7 ARG CG C 27.2 0.2 1 52 . 7 ARG CD C 23.2 0.2 1 53 . 7 ARG N N 123.59 0.1 1 54 . 8 THR H H 8.65 0.01 1 55 . 8 THR HA H 5.28 0.01 1 56 . 8 THR C C 174.5 0.1 1 57 . 8 THR CA C 61.88 0.2 1 58 . 8 THR CB C 71.05 0.2 1 59 . 8 THR CG2 C 22.3 0.2 1 60 . 8 THR N N 118.11 0.1 1 61 . 9 GLY H H 9.09 0.01 1 62 . 9 GLY HA2 H 4.72 0.01 1 63 . 9 GLY HA3 H 4.72 0.01 1 64 . 9 GLY C C 170.2 0.1 1 65 . 9 GLY CA C 44.92 0.2 1 66 . 9 GLY N N 113.04 0.1 1 67 . 10 TYR H H 8.88 0.01 1 68 . 10 TYR HA H 5.19 0.01 1 69 . 10 TYR HB2 H 2.77 0.01 2 70 . 10 TYR HB3 H 2.54 0.01 2 71 . 10 TYR C C 176.2 0.1 1 72 . 10 TYR CA C 57.04 0.2 1 73 . 10 TYR CB C 40.35 0.2 1 74 . 10 TYR N N 122.8 0.1 1 75 . 11 PHE H H 8.59 0.01 1 76 . 11 PHE HA H 5.74 0.01 1 77 . 11 PHE HB2 H 2.65 0.01 1 78 . 11 PHE HB3 H 2.50 0.01 1 79 . 11 PHE C C 124.3 0.1 1 80 . 11 PHE CA C 53.83 0.2 1 81 . 11 PHE CB C 41.69 0.2 1 82 . 11 PHE N N 122.45 0.1 1 83 . 12 LEU H H 8.56 0.01 1 84 . 12 LEU HA H 4.96 0.01 1 85 . 12 LEU C C 174.4 0.1 1 86 . 12 LEU CA C 53.79 0.2 1 87 . 12 LEU CB C 45.18 0.2 1 88 . 12 LEU N N 123.72 0.1 1 89 . 13 LEU H H 9.59 0.01 1 90 . 13 LEU CA C 53.8 0.2 1 91 . 13 LEU CB C 41.46 0.2 1 92 . 13 LEU N N 133.56 0.1 1 93 . 15 GLN C C 174.5 0.1 1 94 . 15 GLN CA C 53.75 0.2 1 95 . 15 GLN CB C 32.04 0.2 1 96 . 16 HIS C C 173.8 0.1 1 97 . 16 HIS CA C 54.09 0.2 1 98 . 16 HIS CB C 30.41 0.2 1 99 . 17 GLU HA H 3.36 0.01 1 100 . 17 GLU HB2 H 1.9 0.01 1 101 . 17 GLU HB3 H 1.9 0.01 1 102 . 17 GLU HG2 H 1.81 0.01 1 103 . 17 GLU HG3 H 1.81 0.01 1 104 . 17 GLU CA C 58.92 0.2 1 105 . 17 GLU CB C 26.59 0.2 1 106 . 17 GLU CG C 35.88 0.2 1 107 . 18 ASP H H 8.52 0.01 1 108 . 18 ASP HA H 4.94 0.01 1 109 . 18 ASP HB2 H 2.9 0.01 2 110 . 18 ASP HB3 H 2.8 0.01 2 111 . 18 ASP C C 174 0.1 1 112 . 18 ASP CA C 54.21 0.2 1 113 . 18 ASP CB C 40.73 0.2 1 114 . 18 ASP N N 123.24 0.1 1 115 . 19 GLU H H 8.3 0.01 1 116 . 19 GLU HA H 5.67 0.01 1 117 . 19 GLU C C 175.9 0.1 1 118 . 19 GLU CA C 54.61 0.2 1 119 . 19 GLU CB C 33.85 0.2 1 120 . 19 GLU N N 117.68 0.1 1 121 . 20 VAL H H 9.01 0.01 1 122 . 20 VAL HA H 5.96 0.01 1 123 . 20 VAL HB H 2.1 0.01 1 124 . 20 VAL HG1 H 1.1 0.01 1 125 . 20 VAL HG2 H 1.1 0.01 1 126 . 20 VAL C C 174.8 0.1 1 127 . 20 VAL CA C 58.68 0.2 1 128 . 20 VAL CB C 36.06 0.2 1 129 . 20 VAL CG1 C 20.94 0.2 1 130 . 20 VAL CG2 C 21.43 0.2 1 131 . 20 VAL N N 117.27 0.1 1 132 . 21 LEU H H 7.7 0.01 1 133 . 21 LEU HA H 3.95 0.01 1 134 . 21 LEU C C 175.8 0.1 1 135 . 21 LEU CA C 55.96 0.2 1 136 . 21 LEU CB C 41.44 0.2 1 137 . 21 LEU N N 128.64 0.1 1 138 . 22 LEU H H 9.01 0.01 1 139 . 22 LEU HA H 4.68 0.01 1 140 . 22 LEU HB2 H 1.17 0.01 1 141 . 22 LEU HB3 H 1.17 0.01 1 142 . 22 LEU C C 174.8 0.1 1 143 . 22 LEU CA C 52.78 0.2 1 144 . 22 LEU CB C 46.29 0.2 1 145 . 22 LEU N N 125.68 0.1 1 146 . 23 ALA H H 8.75 0.01 1 147 . 23 ALA HA H 5.03 0.01 1 148 . 23 ALA HB H 1.25 0.01 1 149 . 23 ALA C C 177.2 0.1 1 150 . 23 ALA CA C 50.63 0.2 1 151 . 23 ALA CB C 22 0.2 1 152 . 23 ALA N N 120.5 0.1 1 153 . 24 GLN H H 8.72 0.01 1 154 . 24 GLN HA H 3.39 0.01 1 155 . 24 GLN C C 176.2 0.1 1 156 . 24 GLN CA C 56.25 0.2 1 157 . 24 GLN CB C 28.5 0.2 1 158 . 24 GLN N N 125.43 0.1 1 159 . 25 ARG H H 8.54 0.01 1 160 . 25 ARG CA C 54.9 0.2 1 161 . 25 ARG CB C 28.76 0.2 1 162 . 25 ARG N N 130.62 0.1 1 163 . 27 PRO HA H 4.08 0.01 1 164 . 27 PRO HB2 H 2.24 0.01 1 165 . 27 PRO HB3 H 2.24 0.01 1 166 . 27 PRO C C 177 0.1 1 167 . 27 PRO CA C 64.81 0.2 1 168 . 27 PRO CB C 35.51 0.2 1 169 . 28 SER H H 7.86 0.01 1 170 . 28 SER HA H 4.45 0.01 1 171 . 28 SER HB2 H 3.91 0.01 2 172 . 28 SER HB3 H 3.8 0.01 2 173 . 28 SER C C 174.5 0.1 1 174 . 28 SER CA C 58.14 0.2 1 175 . 28 SER CB C 63.56 0.2 1 176 . 28 SER N N 111.07 0.1 1 177 . 29 GLY H H 7.72 0.01 1 178 . 29 GLY HA2 H 4.08 0.01 2 179 . 29 GLY HA3 H 3.79 0.01 2 180 . 29 GLY CA C 44.15 0.2 1 181 . 29 GLY N N 108.97 0.1 1 182 . 30 LEU H H 8.22 0.01 1 183 . 30 LEU HA H 4.15 0.01 1 184 . 30 LEU HB2 H 3.59 0.01 1 185 . 30 LEU HB3 H 3.59 0.01 1 186 . 30 LEU C C 174.2 0.1 1 187 . 30 LEU CA C 55.52 0.2 1 188 . 30 LEU CB C 29.9 0.2 1 189 . 30 LEU N N 121.82 0.1 1 190 . 31 TRP H H 7.82 0.01 1 191 . 31 TRP C C 175.6 0.1 1 192 . 31 TRP CA C 56.83 0.2 1 193 . 31 TRP CB C 25.55 0.2 1 194 . 31 TRP N N 114.73 0.1 1 195 . 32 GLY H H 7.72 0.01 1 196 . 32 GLY HA2 H 3.68 0.01 2 197 . 32 GLY HA3 H 3.59 0.01 2 198 . 32 GLY C C 176.06 0.1 1 199 . 32 GLY CA C 47.83 0.2 1 200 . 32 GLY N N 104.48 0.1 1 201 . 33 GLY H H 7.65 0.01 1 202 . 33 GLY HA2 H 4.14 0.01 2 203 . 33 GLY HA3 H 3.59 0.01 2 204 . 33 GLY C C 173.49 0.1 1 205 . 33 GLY CA C 45.44 0.2 1 206 . 33 GLY N N 112.62 0.1 1 207 . 34 LEU H H 7.61 0.01 1 208 . 34 LEU HA H 4.58 0.01 1 209 . 34 LEU HB2 H 1.79 0.01 1 210 . 34 LEU HB3 H 1.14 0.01 1 211 . 34 LEU HD1 H 0.85 0.01 1 212 . 34 LEU HD2 H 0.72 0.01 1 213 . 34 LEU HG H 1.46 0.01 1 214 . 34 LEU C C 176.9 0.1 1 215 . 34 LEU CA C 53.05 0.2 1 216 . 34 LEU CB C 43.3 0.2 1 217 . 34 LEU CD2 C 21.7 0.2 1 218 . 34 LEU N N 120.35 0.1 1 219 . 35 TYR H H 8.83 0.01 1 220 . 35 TYR HA H 4.64 0.01 1 221 . 35 TYR C C 176.5 0.1 1 222 . 35 TYR CA C 59.49 0.2 1 223 . 35 TYR CB C 39.03 0.2 1 224 . 35 TYR N N 118.81 0.1 1 225 . 36 CYS H H 8.85 0.01 1 226 . 36 CYS C C 172 0.1 1 227 . 36 CYS CA C 57.08 0.2 1 228 . 36 CYS CB C 29.61 0.2 1 229 . 36 CYS N N 119.51 0.1 1 230 . 37 PHE H H 6.13 0.01 1 231 . 37 PHE CA C 57.33 0.2 1 232 . 37 PHE CB C 37.92 0.2 1 233 . 37 PHE N N 127.23 0.1 1 234 . 38 PRO HA H 3.99 0.01 1 235 . 38 PRO C C 173 0.1 1 236 . 38 PRO CA C 64.57 0.2 1 237 . 38 PRO CB C 32.23 0.2 1 238 . 39 GLN H H 7.57 0.01 1 239 . 39 GLN C C 174.36 0.1 1 240 . 39 GLN CA C 53.8 0.2 1 241 . 39 GLN CB C 31.19 0.2 1 242 . 39 GLN N N 124.15 0.1 1 243 . 40 PHE H H 9.3 0.01 1 244 . 40 PHE CA C 56.51 0.2 1 245 . 40 PHE CB C 43.85 0.2 1 246 . 40 PHE N N 123.3 0.1 1 247 . 41 ALA H H 9.4 0.01 1 248 . 41 ALA HA H 4.48 0.01 1 249 . 41 ALA HB H 1.52 0.01 1 250 . 41 ALA C C 176.6 0.1 1 251 . 41 ALA CA C 53.84 0.2 1 252 . 41 ALA CB C 19.55 0.2 1 253 . 41 ALA N N 124.29 0.1 1 254 . 42 ASP H H 7.41 0.01 1 255 . 42 ASP HA H 4.35 0.01 1 256 . 42 ASP HB2 H 2.89 0.01 1 257 . 42 ASP HB3 H 2.89 0.01 1 258 . 42 ASP C C 174 0.1 1 259 . 42 ASP CA C 52.27 0.2 1 260 . 42 ASP CB C 41.8 0.2 1 261 . 42 ASP N N 109.26 0.1 1 262 . 43 GLU H H 8.08 0.01 1 263 . 43 GLU C C 178.2 0.1 1 264 . 43 GLU CA C 59.19 0.2 1 265 . 43 GLU CB C 29.34 0.2 1 266 . 43 GLU N N 120.08 0.1 1 267 . 47 ARG C C 180.4 0.1 1 268 . 47 ARG CA C 60.55 0.2 1 269 . 47 ARG CB C 29.53 0.2 1 270 . 48 GLN H H 8.63 0.01 1 271 . 48 GLN HA H 4.16 0.01 1 272 . 48 GLN HB2 H 2.18 0.01 1 273 . 48 GLN HB3 H 2.18 0.01 1 274 . 48 GLN HG2 H 2.54 0.01 2 275 . 48 GLN HG3 H 2.45 0.01 2 276 . 48 GLN C C 177.7 0.1 1 277 . 48 GLN CA C 58.92 0.2 1 278 . 48 GLN CB C 27.99 0.2 1 279 . 48 GLN CG C 33.84 0.2 1 280 . 48 GLN N N 122.19 0.1 1 281 . 49 TRP H H 7.81 0.01 1 282 . 49 TRP HA H 4.11 0.01 1 283 . 49 TRP C C 180 0.1 1 284 . 49 TRP CA C 62.15 0.2 1 285 . 49 TRP CB C 30.36 0.2 1 286 . 49 TRP N N 123.86 0.1 1 287 . 50 LEU H H 7.68 0.01 1 288 . 50 LEU HA H 4 0.01 1 289 . 50 LEU HB2 H 2.05 0.01 1 290 . 50 LEU HB3 H 2.05 0.01 1 291 . 50 LEU HG H 1.93 0.01 1 292 . 50 LEU C C 179.2 0.1 1 293 . 50 LEU CA C 58.13 0.2 1 294 . 50 LEU CB C 41.17 0.2 1 295 . 50 LEU N N 117.4 0.1 1 296 . 51 ALA H H 8.08 0.01 1 297 . 51 ALA HA H 4.08 0.01 1 298 . 51 ALA C C 178.1 0.1 1 299 . 51 ALA CA C 55.2 0.2 1 300 . 51 ALA CB C 17.69 0.2 1 301 . 51 ALA N N 122.47 0.1 1 302 . 52 GLN H H 8.38 0.01 1 303 . 52 GLN C C 175 0.1 1 304 . 52 GLN CA C 58.41 0.2 1 305 . 52 GLN CB C 28.49 0.2 1 306 . 52 GLN N N 119.37 0.1 1 307 . 53 ARG H H 8.6 0.01 1 308 . 53 ARG CA C 55.41 0.2 1 309 . 53 ARG CB C 32.51 0.2 1 310 . 53 ARG N N 122.19 0.1 1 311 . 54 GLN HA H 3.79 0.01 1 312 . 54 GLN C C 174.9 0.1 1 313 . 54 GLN CA C 56.86 0.2 1 314 . 54 GLN CB C 25.66 0.2 1 315 . 55 ILE H H 7.87 0.01 1 316 . 55 ILE HA H 4.09 0.01 1 317 . 55 ILE HB H 1.61 0.01 1 318 . 55 ILE HG2 H 1.96 0.01 2 319 . 55 ILE HD1 H 0.93 0.01 2 320 . 55 ILE C C 175.5 0.1 1 321 . 55 ILE CA C 60.57 0.2 1 322 . 55 ILE CB C 38.71 0.2 1 323 . 55 ILE N N 120.79 0.1 1 324 . 56 ALA H H 8.46 0.01 1 325 . 56 ALA HA H 4.12 0.01 1 326 . 56 ALA HB H 1.46 0.01 1 327 . 56 ALA C C 178.7 0.1 1 328 . 56 ALA CA C 53.38 0.2 1 329 . 56 ALA CB C 18.61 0.2 1 330 . 56 ALA N N 131.17 0.1 1 331 . 57 ALA H H 8.5 0.01 1 332 . 57 ALA HA H 4.56 0.01 1 333 . 57 ALA HB H 1.4 0.01 1 334 . 57 ALA C C 177.9 0.1 1 335 . 57 ALA CA C 51.38 0.2 1 336 . 57 ALA CB C 19.45 0.2 1 337 . 57 ALA N N 124.29 0.1 1 338 . 58 ASP H H 8.15 0.01 1 339 . 58 ASP HA H 4.22 0.01 1 340 . 58 ASP HB2 H 2.62 0.01 2 341 . 58 ASP HB3 H 2.44 0.01 2 342 . 58 ASP C C 177.1 0.1 1 343 . 58 ASP CA C 57.32 0.2 1 344 . 58 ASP CB C 40.32 0.2 1 345 . 58 ASP N N 120.36 0.2 1 346 . 59 MET H H 8.53 0.01 1 347 . 59 MET HA H 4.85 0.01 1 348 . 59 MET C C 174.4 0.1 1 349 . 59 MET CA C 52.73 0.2 1 350 . 59 MET CB C 37.7 0.2 1 351 . 59 MET N N 113.75 0.1 1 352 . 60 LEU H H 7.36 0.01 1 353 . 60 LEU HA H 4.38 0.01 1 354 . 60 LEU HB2 H 1.88 0.01 1 355 . 60 LEU HB3 H 1.88 0.01 1 356 . 60 LEU C C 177.3 0.1 1 357 . 60 LEU CA C 56.61 0.2 1 358 . 60 LEU CB C 43.22 0.2 1 359 . 60 LEU N N 122.88 0.1 1 360 . 61 THR H H 9.66 0.01 1 361 . 61 THR HA H 4.72 0.01 1 362 . 61 THR HG2 H 1.37 0.01 1 363 . 61 THR C C 172.8 0.1 1 364 . 61 THR CA C 62.17 0.2 1 365 . 61 THR CB C 72.45 0.2 1 366 . 61 THR N N 125.7 0.1 1 367 . 62 GLN H H 9.12 0.01 1 368 . 62 GLN HA H 4.91 0.01 1 369 . 62 GLN C C 176.3 0.1 1 370 . 62 GLN CA C 56.8 0.2 1 371 . 62 GLN CB C 29.6 0.2 1 372 . 62 GLN N N 129.62 0.1 1 373 . 62 GLN NE2 N 111.94 0.1 1 374 . 62 GLN HE21 H 7.71 0.01 2 375 . 62 GLN HE22 H 6.89 0.01 2 376 . 63 LEU H H 8.71 0.01 1 377 . 63 LEU HA H 4.77 0.01 1 378 . 63 LEU C C 175.9 0.1 1 379 . 63 LEU CA C 53.3 0.2 1 380 . 63 LEU CB C 41.42 0.2 1 381 . 63 LEU N N 128.5 0.1 1 382 . 64 THR H H 8.34 0.01 1 383 . 64 THR HA H 4 0.01 1 384 . 64 THR C C 173.8 0.1 1 385 . 64 THR CA C 64.9 0.2 1 386 . 64 THR CB C 69.49 0.2 1 387 . 64 THR N N 116.7 0.1 1 388 . 65 ALA H H 8.31 0.01 1 389 . 65 ALA HA H 4.9 0.01 1 390 . 65 ALA HB H 1.37 0.01 1 391 . 65 ALA C C 177.7 0.1 1 392 . 65 ALA CA C 51.99 0.2 1 393 . 65 ALA CB C 20.23 0.2 1 394 . 65 ALA N N 129.21 0.1 1 395 . 66 PHE H H 8.23 0.01 1 396 . 66 PHE HA H 4.92 0.01 1 397 . 66 PHE HB2 H 3.06 0.01 1 398 . 66 PHE HB3 H 3.06 0.01 1 399 . 66 PHE C C 172 0.1 1 400 . 66 PHE CA C 56.22 0.2 1 401 . 66 PHE CB C 40.87 0.2 1 402 . 66 PHE N N 116.7 0.1 1 403 . 67 ARG H H 8.47 0.01 1 404 . 67 ARG HA H 5.35 0.01 1 405 . 67 ARG C C 176.1 0.1 1 406 . 67 ARG CA C 54.99 0.2 1 407 . 67 ARG CB C 33.86 0.2 1 408 . 67 ARG N N 122.04 0.1 1 409 . 68 HIS H H 9.62 0.01 1 410 . 68 HIS CA C 55.98 0.2 1 411 . 68 HIS CB C 34.17 0.2 1 412 . 68 HIS N N 128.93 0.1 1 413 . 69 THR H H 8.33 0.01 1 414 . 69 THR HA H 4.44 0.01 1 415 . 69 THR HB H 3.67 0.01 1 416 . 69 THR HG2 H 1.14 0.01 1 417 . 69 THR CA C 64.58 0.2 1 418 . 69 THR CB C 70.51 0.2 1 419 . 69 THR CG2 C 22.8 0.2 1 420 . 69 THR N N 125.27 0.1 1 421 . 70 PHE H H 8.33 0.01 1 422 . 70 PHE CA C 56.79 0.2 1 423 . 70 PHE CB C 40.36 0.2 1 424 . 70 PHE N N 127.65 0.1 1 425 . 72 HIS C C 175.2 0.1 1 426 . 73 PHE H H 7.04 0.01 1 427 . 73 PHE C C 172.3 0.1 1 428 . 73 PHE CA C 57.07 0.2 1 429 . 73 PHE CB C 39.35 0.2 1 430 . 73 PHE N N 115.02 0.1 1 431 . 74 HIS H H 8.84 0.01 1 432 . 74 HIS HA H 5.06 0.01 1 433 . 74 HIS HB2 H 2.97 0.01 2 434 . 74 HIS HB3 H 2.94 0.01 2 435 . 74 HIS C C 174 0.1 1 436 . 74 HIS CA C 55.44 0.2 1 437 . 74 HIS CB C 33.59 0.2 1 438 . 74 HIS N N 117.97 0.1 1 439 . 75 LEU H H 9.34 0.01 1 440 . 75 LEU HA H 5.25 0.01 1 441 . 75 LEU HB2 H 2.59 0.01 2 442 . 75 LEU HB3 H 2.37 0.01 2 443 . 75 LEU C C 174.7 0.1 1 444 . 75 LEU CA C 53.06 0.2 1 445 . 75 LEU CB C 46.04 0.2 1 446 . 75 LEU N N 125.2 0.1 1 447 . 76 ASP H H 9.29 0.01 1 448 . 76 ASP HA H 5.12 0.01 1 449 . 76 ASP HB2 H 2.54 0.01 1 450 . 76 ASP HB3 H 2.54 0.01 1 451 . 76 ASP C C 174.3 0.1 1 452 . 76 ASP CA C 54.69 0.2 1 453 . 76 ASP CB C 41.2 0.2 1 454 . 76 ASP N N 129.62 0.1 1 455 . 77 ILE H H 8.89 0.01 1 456 . 77 ILE HA H 4.1 0.01 1 457 . 77 ILE C C 174.6 0.1 1 458 . 77 ILE CA C 60.65 0.2 1 459 . 77 ILE CB C 37.64 0.2 1 460 . 77 ILE N N 126.12 0.1 1 461 . 78 VAL H H 8.48 0.01 1 462 . 78 VAL HA H 4.68 0.01 1 463 . 78 VAL HB H 2.3 0.01 1 464 . 78 VAL HG1 H 0.98 0.01 2 465 . 78 VAL HG2 H 0.96 0.01 2 466 . 78 VAL CA C 59.59 0.2 1 467 . 78 VAL CB C 31.74 0.2 1 468 . 78 VAL CG1 C 22.52 0.2 1 469 . 78 VAL CG2 C 22.52 0.2 1 470 . 78 VAL N N 127.71 0.1 1 471 . 79 PRO HA H 4.92 0.01 1 472 . 79 PRO C C 176 0.1 1 473 . 79 PRO CA C 60.57 0.2 1 474 . 79 PRO CB C 31.76 0.2 1 475 . 80 MET H H 9.19 0.01 1 476 . 80 MET HA H 5.27 0.01 1 477 . 80 MET HB2 H 2.61 0.01 1 478 . 80 MET HB3 H 2.61 0.01 1 479 . 80 MET HG2 H 1.96 0.01 1 480 . 80 MET HG3 H 1.96 0.01 1 481 . 80 MET C C 173.5 0.1 1 482 . 80 MET CA C 53.56 0.2 1 483 . 80 MET CB C 33.88 0.2 1 484 . 80 MET N N 123.32 0.1 1 485 . 81 TRP H H 9.6 0.01 1 486 . 81 TRP HA H 5.47 0.01 1 487 . 81 TRP HB2 H 3.39 0.01 2 488 . 81 TRP HB3 H 2.92 0.01 2 489 . 81 TRP C C 173.96 0.1 1 490 . 81 TRP CA C 55.96 0.2 1 491 . 81 TRP CB C 31.49 0.2 1 492 . 81 TRP N N 127.53 0.1 1 493 . 82 LEU H H 8.64 0.01 1 494 . 82 LEU CA C 51.11 0.2 1 495 . 82 LEU CB C 46.05 0.2 1 496 . 82 LEU N N 129.35 0.1 1 497 . 84 VAL HA H 4.70 0.01 1 498 . 84 VAL HB H 2.32 0.01 1 499 . 84 VAL HG1 H 0.99 0.01 1 500 . 84 VAL HG2 H 0.99 0.01 1 501 . 84 VAL CA C 59.5 0.2 1 502 . 84 VAL CB C 35.6 0.2 1 503 . 84 VAL CG1 C 22.83 0.2 1 504 . 84 VAL CG2 C 22.83 0.2 1 505 . 85 SER HA H 4.65 0.01 1 506 . 85 SER HB2 H 3.96 0.01 2 507 . 85 SER HB3 H 3.92 0.01 2 508 . 85 SER C C 174.5 0.1 1 509 . 85 SER CA C 59.16 0.2 1 510 . 85 SER CB C 63.55 0.2 1 511 . 86 SER H H 7.7 0.01 1 512 . 86 SER HA H 4.33 0.01 1 513 . 86 SER HB2 H 3.76 0.01 1 514 . 86 SER HB3 H 3.76 0.01 1 515 . 86 SER C C 172.8 0.1 1 516 . 86 SER CA C 57.36 0.2 1 517 . 86 SER CB C 64.34 0.2 1 518 . 86 SER N N 114.32 0.1 1 519 . 87 PHE H H 8.3 0.01 1 520 . 87 PHE HA H 4.67 0.01 1 521 . 87 PHE HB2 H 2.76 0.01 2 522 . 87 PHE HB3 H 2.68 0.01 2 523 . 87 PHE C C 175.3 0.1 1 524 . 87 PHE CA C 57.59 0.2 1 525 . 87 PHE CB C 40.08 0.2 1 526 . 87 PHE N N 121.35 0.1 1 527 . 88 THR H H 8.15 0.01 1 528 . 88 THR HA H 4.29 0.01 1 529 . 88 THR HB H 4.16 0.01 1 530 . 88 THR HG2 H 1.1 0.01 1 531 . 88 THR C C 174.76 0.1 1 532 . 88 THR CA C 61.96 0.2 1 533 . 88 THR CB C 69.72 0.2 1 534 . 88 THR CG2 C 21.31 0.2 1 535 . 88 THR N N 117.83 0.1 1 536 . 89 GLY H H 7.57 0.01 1 537 . 89 GLY HA2 H 3.97 0.01 1 538 . 89 GLY HA3 H 3.97 0.01 1 539 . 89 GLY CA C 45.24 0.2 1 540 . 89 GLY N N 110.53 0.1 1 541 . 90 CYS H H 8.33 0.01 1 542 . 90 CYS CA C 58.95 0.2 1 543 . 90 CYS CB C 27.99 0.2 1 544 . 90 CYS N N 117.98 0.1 1 545 . 91 MET HA H 4.67 0.01 1 546 . 91 MET C C 176 0.1 1 547 . 91 MET CA C 55.68 0.2 1 548 . 91 MET CB C 32.29 0.2 1 549 . 92 ASP H H 8.46 0.01 1 550 . 92 ASP HA H 4.66 0.01 1 551 . 92 ASP HB2 H 2.72 0.01 2 552 . 92 ASP HB3 H 2.67 0.01 2 553 . 92 ASP C C 176.3 0.1 1 554 . 92 ASP CA C 54.66 0.2 1 555 . 92 ASP CB C 40.9 0.2 1 556 . 92 ASP N N 121.34 0.1 1 557 . 93 GLU H H 8.23 0.01 1 558 . 93 GLU HA H 4.4 0.01 1 559 . 93 GLU HB2 H 2.13 0.01 2 560 . 93 GLU HB3 H 2.03 0.01 2 561 . 93 GLU HG2 H 2.31 0.01 1 562 . 93 GLU HG3 H 2.31 0.01 1 563 . 93 GLU C C 177.3 0.1 1 564 . 93 GLU CA C 56.61 0.2 1 565 . 93 GLU CB C 30.29 0.2 1 566 . 93 GLU CG C 36.45 0.2 1 567 . 93 GLU N N 120.78 0.1 1 568 . 94 GLY H H 8.6 0.01 1 569 . 94 GLY HA2 H 3.97 0.01 2 570 . 94 GLY HA3 H 3.92 0.01 2 571 . 94 GLY C C 174.9 0.1 1 572 . 94 GLY CA C 46.02 0.2 1 573 . 94 GLY N N 110.67 0.1 1 574 . 95 ASN H H 8.52 0.01 1 575 . 95 ASN HA H 4.81 0.01 1 576 . 95 ASN C C 174.3 0.1 1 577 . 95 ASN CA C 53.26 0.2 1 578 . 95 ASN CB C 38.21 0.2 1 579 . 95 ASN N N 118.81 0.1 1 580 . 95 ASN ND2 N 112.25 0.1 1 581 . 95 ASN HD21 H 7.49 0.01 2 582 . 95 ASN HD22 H 6.89 0.01 2 583 . 96 ALA H H 7.82 0.01 1 584 . 96 ALA HA H 4.99 0.01 1 585 . 96 ALA HB H 1.37 0.01 1 586 . 96 ALA C C 176.4 0.1 1 587 . 96 ALA CA C 51.95 0.2 1 588 . 96 ALA CB C 21.19 0.2 1 589 . 96 ALA N N 122.73 0.1 1 590 . 97 LEU H H 9.03 0.01 1 591 . 97 LEU HA H 4.61 0.01 1 592 . 97 LEU C C 174.8 0.1 1 593 . 97 LEU CA C 54.36 0.2 1 594 . 97 LEU CB C 46 0.2 1 595 . 97 LEU N N 122.18 0.1 1 596 . 98 TRP H H 8.78 0.01 1 597 . 98 TRP HA H 4.85 0.01 1 598 . 98 TRP HB2 H 3.16 0.01 2 599 . 98 TRP HB3 H 3.06 0.01 2 600 . 98 TRP C C 175.1 0.1 1 601 . 98 TRP CA C 56.55 0.2 1 602 . 98 TRP CB C 28.51 0.2 1 603 . 98 TRP N N 125.7 0.1 1 604 . 99 TYR H H 9.71 0.01 1 605 . 99 TYR HA H 4.19 0.01 1 606 . 99 TYR C C 174.5 0.1 1 607 . 99 TYR CA C 57.83 0.2 1 608 . 99 TYR CB C 40.39 0.2 1 609 . 99 TYR N N 131.03 0.1 1 610 . 100 ASN H H 8.32 0.01 1 611 . 100 ASN HA H 4.77 0.01 1 612 . 100 ASN C C 174.5 0.1 1 613 . 100 ASN CA C 54.36 0.2 1 614 . 100 ASN CB C 39.55 0.2 1 615 . 100 ASN N N 129.64 0.1 1 616 . 101 LEU H H 9.09 0.01 1 617 . 101 LEU HA H 4.01 0.01 1 618 . 101 LEU C C 178.8 0.1 1 619 . 101 LEU CA C 57.37 0.2 1 620 . 101 LEU CB C 42.78 0.2 1 621 . 101 LEU N N 124.01 0.1 1 622 . 102 ALA H H 8.08 0.01 1 623 . 102 ALA HA H 4.4 0.01 1 624 . 102 ALA HB H 1.46 0.01 1 625 . 102 ALA C C 178.1 0.1 1 626 . 102 ALA CA C 53.02 0.2 1 627 . 102 ALA CB C 19.31 0.2 1 628 . 102 ALA N N 120.07 0.1 1 629 . 103 GLN H H 7.64 0.01 1 630 . 103 GLN HA H 4.58 0.01 1 631 . 103 GLN HB2 H 1.94 0.01 2 632 . 103 GLN HB3 H 1.75 0.01 2 633 . 103 GLN HG2 H 2.18 0.01 1 634 . 103 GLN HG3 H 2.18 0.01 1 635 . 103 GLN CA C 53 0.2 1 636 . 103 GLN CB C 29.05 0.2 1 637 . 103 GLN CG C 33.6 0.2 1 638 . 103 GLN N N 118.39 0.1 1 639 . 103 GLN NE2 N 111.68 0.1 1 640 . 103 GLN HE21 H 7.43 0.01 2 641 . 103 GLN HE22 H 6.76 0.01 2 642 . 105 PRO CA C 61.7 0.2 1 643 . 105 PRO CB C 31.98 0.2 1 644 . 106 SER H H 8.66 0.01 1 645 . 106 SER HA H 4.57 0.01 1 646 . 106 SER HB3 H 3.84 0.01 1 647 . 106 SER HB2 H 3.84 0.01 1 648 . 106 SER C C 174.3 0.1 1 649 . 106 SER CA C 57.35 0.2 1 650 . 106 SER CB C 62.74 0.2 1 651 . 106 SER N N 116.85 0.1 1 652 . 107 VAL H H 7.19 0.01 1 653 . 107 VAL HA H 4.57 0.01 1 654 . 107 VAL HB H 2.08 0.01 1 655 . 107 VAL HG1 H 0.61 0.01 2 656 . 107 VAL HG2 H 0.4 0.01 2 657 . 107 VAL C C 175.2 0.1 1 658 . 107 VAL CA C 59.28 0.2 1 659 . 107 VAL CB C 34.7 0.2 1 660 . 107 VAL CG1 C 21.63 0.2 1 661 . 107 VAL CG2 C 17.92 0.2 1 662 . 107 VAL N N 117 0.1 1 663 . 108 GLY H H 8.76 0.01 1 664 . 108 GLY HA2 H 4.11 0.01 2 665 . 108 GLY HA3 H 3.37 0.01 2 666 . 108 GLY C C 173.9 0.1 1 667 . 108 GLY CA C 46.28 0.2 1 668 . 108 GLY N N 109.97 0.1 1 669 . 109 LEU H H 8.56 0.01 1 670 . 109 LEU HA H 4.89 0.01 1 671 . 109 LEU C C 177.1 0.1 1 672 . 109 LEU CA C 53.02 0.2 1 673 . 109 LEU CB C 45.1 0.2 1 674 . 109 LEU N N 125.84 0.1 1 675 . 110 ALA H H 8.01 0.01 1 676 . 110 ALA HA H 3.87 0.01 1 677 . 110 ALA HB H 0.66 0.01 1 678 . 110 ALA CA C 51.42 0.2 1 679 . 110 ALA CB C 18.78 0.2 1 680 . 110 ALA N N 123.3 0.1 1 681 . 111 ALA H H 8.19 0.01 1 682 . 111 ALA HA H 4.59 0.01 1 683 . 111 ALA HB H 1.35 0.01 1 684 . 111 ALA CA C 50.21 0.2 1 685 . 111 ALA CB C 17.98 0.2 1 686 . 111 ALA N N 125.69 0.1 1 687 . 112 PRO HA H 4.54 0.01 1 688 . 112 PRO HB2 H 2.19 0.01 2 689 . 112 PRO HB3 H 1.61 0.01 2 690 . 112 PRO C C 176.6 0.1 1 691 . 112 PRO CA C 65.16 0.2 1 692 . 112 PRO CB C 31.76 0.2 1 693 . 113 VAL H H 7.39 0.01 1 694 . 113 VAL HA H 3.59 0.01 1 695 . 113 VAL C C 177.5 0.1 1 696 . 113 VAL CA C 66.75 0.2 1 697 . 113 VAL CB C 30.79 0.2 1 698 . 113 VAL N N 115.58 0.1 1 699 . 114 GLU H H 8.42 0.01 1 700 . 114 GLU HA H 3.86 0.01 1 701 . 114 GLU HB2 H 2.03 0.01 2 702 . 114 GLU HB3 H 1.97 0.01 2 703 . 114 GLU HG2 H 2.18 0.01 2 704 . 114 GLU HG3 H 2.15 0.01 2 705 . 114 GLU C C 178.56 0.1 1 706 . 114 GLU CA C 60.58 0.2 1 707 . 114 GLU CB C 28.8 0.2 1 708 . 114 GLU N N 120.21 0.1 1 709 . 115 ARG H H 8.15 0.01 1 710 . 115 ARG HA H 4.03 0.01 1 711 . 115 ARG HB2 H 1.75 0.01 2 712 . 115 ARG HB3 H 1.57 0.01 2 713 . 115 ARG HG2 H 1.4 0.01 2 714 . 115 ARG HG3 H 1.37 0.01 2 715 . 115 ARG HE H 2.76 0.01 1 716 . 115 ARG C C 179.2 0.1 1 717 . 115 ARG CA C 58.93 0.2 1 718 . 115 ARG CB C 29.68 0.2 1 719 . 115 ARG N N 118.1 0.1 1 720 . 116 LEU H H 7.4 0.01 1 721 . 116 LEU HA H 4.16 0.01 1 722 . 116 LEU C C 179.1 0.1 1 723 . 116 LEU CA C 57.58 0.2 1 724 . 116 LEU CB C 42.54 0.2 1 725 . 116 LEU N N 120.07 0.1 1 726 . 117 LEU H H 8.72 0.01 1 727 . 117 LEU C C 179.6 0.1 1 728 . 117 LEU CA C 58.4 0.2 1 729 . 117 LEU CB C 40.65 0.2 1 730 . 117 LEU N N 119.65 0.1 1 731 . 118 GLN H H 7.98 0.01 1 732 . 118 GLN HA H 4.05 0.01 1 733 . 118 GLN HB2 H 2.11 0.01 1 734 . 118 GLN HB3 H 2.11 0.01 1 735 . 118 GLN HG2 H 2.48 0.01 2 736 . 118 GLN HG3 H 2.42 0.01 2 737 . 118 GLN C C 178.9 0.1 1 738 . 118 GLN CA C 58.69 0.2 1 739 . 118 GLN CB C 27.7 0.2 1 740 . 118 GLN N N 117 0.1 1 741 . 119 GLN H H 7.47 0.01 1 742 . 119 GLN HA H 4.07 0.01 1 743 . 119 GLN C C 178.5 0.1 1 744 . 119 GLN CA C 58.43 0.2 1 745 . 119 GLN CB C 27.98 0.2 1 746 . 119 GLN N N 118.25 0.1 1 747 . 120 LEU H H 7.87 0.01 1 748 . 120 LEU HA H 3.97 0.01 1 749 . 120 LEU HB2 H 1.89 0.01 2 750 . 120 LEU HB3 H 1.42 0.01 2 751 . 120 LEU HG H 1.73 0.01 2 752 . 120 LEU HD1 H 0.8 0.01 2 753 . 120 LEU HD2 H 0.45 0.01 2 754 . 120 LEU C C 179.2 0.1 1 755 . 120 LEU CA C 56.76 0.2 1 756 . 120 LEU CB C 41.7 0.2 1 757 . 120 LEU CG C 26.59 0.2 1 758 . 120 LEU CD1 C 25.76 0.2 1 759 . 120 LEU CD2 C 22.08 0.2 1 760 . 120 LEU N N 119.22 0.1 1 761 . 121 ARG H H 8.14 0.01 1 762 . 121 ARG HA H 4.15 0.01 1 763 . 121 ARG C C 177.5 0.1 1 764 . 121 ARG CA C 58.4 0.2 1 765 . 121 ARG CB C 30.78 0.2 1 766 . 121 ARG N N 119.09 0.1 1 767 . 122 THR H H 7.71 0.01 1 768 . 122 THR HA H 4.29 0.01 1 769 . 122 THR C C 175.7 0.1 1 770 . 122 THR CA C 63 0.2 1 771 . 122 THR CB C 70.29 0.2 1 772 . 122 THR N N 110.39 0.1 1 773 . 123 GLY H H 7.87 0.01 1 774 . 123 GLY HA2 H 4.09 0.01 2 775 . 123 GLY HA3 H 3.85 0.01 2 776 . 123 GLY C C 172.96 0.1 1 777 . 123 GLY CA C 45.18 0.2 1 778 . 123 GLY N N 110.24 0.1 1 779 . 124 ALA H H 8.06 0.01 1 780 . 124 ALA HA H 4.52 0.01 1 781 . 124 ALA HB H 1.23 0.01 1 782 . 124 ALA CA C 50.3 0.2 1 783 . 124 ALA CB C 18.25 0.2 1 784 . 124 ALA N N 124.29 0.1 1 785 . 125 PRO HA H 4.31 0.01 1 786 . 125 PRO HB2 H 1.71 0.01 1 787 . 125 PRO HB3 H 1.77 0.01 1 788 . 125 PRO HG2 H 1.40 0.01 1 789 . 125 PRO HG3 H 1.18 0.01 1 790 . 125 PRO HD2 H 3.24 0.01 1 791 . 125 PRO HD3 H 3.05 0.01 1 792 . 125 PRO CA C 63.09 0.2 1 793 . 125 PRO CB C 31.73 0.2 1 794 . 125 PRO CG C 26.6 0.2 1 795 . 125 PRO CD C 50.0 0.2 1 796 . 126 VAL H H 7.55 0.01 1 797 . 126 VAL HA H 4.02 0.01 1 798 . 126 VAL HB H 2.01 0.01 1 799 . 126 VAL HG1 H 0.88 0.01 2 800 . 126 VAL HG2 H 0.87 0.01 2 801 . 126 VAL CA C 63.39 0.2 1 802 . 126 VAL CB C 33.8 0.2 1 803 . 126 VAL CG1 C 20.21 0.2 1 804 . 126 VAL CG2 C 21.67 0.2 1 805 . 126 VAL N N 122.04 0.1 1 stop_ save_