data_4281 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Backbone and Side Chain 1H, 13C, and 15N Chemical Shift Assignments for AbrBN ; _BMRB_accession_number 4281 _BMRB_flat_file_name bmr4281.str _Entry_type original _Submission_date 1998-12-10 _Accession_date 1998-12-10 _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 Bobay Benjamin G. . 2 Andreeva Antonina . . 3 Mueller Geoffrey A. . 4 Cavanagh John . . 5 Murzin Alexey G. . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 325 "13C chemical shifts" 238 "15N chemical shifts" 54 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2005-08-05 update author 'update of PDB ID and remove the coupling constants' 2001-01-11 original author 'original release' stop_ save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; Revised structure of the AbrB N-terminal domain unifies a diverse superfamily of putative DNA-binding proteins ; _Citation_status 'in preparation' _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 Bobay Benjamin G. . 2 Andreeva Antonina . . 3 Mueller Geoffrey A. . 4 Cavanagh John . . 5 Murzin Alexey G. . stop_ _Journal_abbreviation . _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 . save_ ####################################### # Cited references within the entry # ####################################### save_ref_1 _Saveframe_category citation _Citation_full ; Hartel et al, Eur. J. Biochem v. 129, 343-357 (1982) and Orbons, et al, IBID, v 170, 225-239 (1987). ; _Citation_title . _Citation_status . _Citation_type . _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID ? _Journal_abbreviation . _Journal_name_full . _Journal_volume . _Journal_issue . _Journal_CSD . _Book_title . _Book_chapter_title . _Book_volume . _Book_series . _Book_publisher . _Book_publisher_city . _Book_ISBN . _Conference_title . _Conference_site . _Conference_state_province . _Conference_country . _Conference_start_date . _Conference_end_date . _Conference_abstract_number . _Thesis_institution . _Thesis_institution_city . _Thesis_institution_country . _Page_first . _Page_last . _Year . _Details . save_ save_ref_2 _Saveframe_category citation _Citation_full ; Live, D.H. et al, JACS, v. 106, 1939-1941 (1984) and Bax and Subramanian, J. Mag. Res., v. 67, 565-569 (1986) ; _Citation_title . _Citation_status . _Citation_type . _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID ? _Journal_abbreviation . _Journal_name_full . _Journal_volume . _Journal_issue . _Journal_CSD . _Book_title . _Book_chapter_title . _Book_volume . _Book_series . _Book_publisher . _Book_publisher_city . _Book_ISBN . _Conference_title . _Conference_site . _Conference_state_province . _Conference_country . _Conference_start_date . _Conference_end_date . _Conference_abstract_number . _Thesis_institution . _Thesis_institution_city . _Thesis_institution_country . _Page_first . _Page_last . _Year . _Details . save_ ################################## # Molecular system description # ################################## save_system_AbrB _Saveframe_category molecular_system _Mol_system_name AbrBN _Abbreviation_common AbrB _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'AbrBN subunit 1' $AbrBN 'AbrBN subunit 2' $AbrBN stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state dimer _System_paramagnetic no _System_thiol_state 'not present' loop_ _Magnetic_equivalence_ID _Magnetically_equivalent_system_component 1 'AbrBN subunit 1' 1 'AbrBN subunit 2' stop_ loop_ _Biological_function 'DNA-binding protein' 'gene regulator' 'expression inhibitor' stop_ _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_AbrBN _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common AbrB _Name_variant AbrBN _Molecular_mass 6100 _Mol_thiol_state . _Details ; N-terminal DNA binding domain, residues 1-53. Full protein is a hexamer of 94 residue components. ; ############################## # Polymer residue sequence # ############################## _Residue_count 53 _Mol_residue_sequence ; MKSTGIVRKVDELGRVVIPI ELRRTLGIAEKDALEIYVDD EKIILKKYKPNMT ; loop_ _Residue_seq_code _Residue_label 1 MET 2 LYS 3 SER 4 THR 5 GLY 6 ILE 7 VAL 8 ARG 9 LYS 10 VAL 11 ASP 12 GLU 13 LEU 14 GLY 15 ARG 16 VAL 17 VAL 18 ILE 19 PRO 20 ILE 21 GLU 22 LEU 23 ARG 24 ARG 25 THR 26 LEU 27 GLY 28 ILE 29 ALA 30 GLU 31 LYS 32 ASP 33 ALA 34 LEU 35 GLU 36 ILE 37 TYR 38 VAL 39 ASP 40 ASP 41 GLU 42 LYS 43 ILE 44 ILE 45 LEU 46 LYS 47 LYS 48 TYR 49 LYS 50 PRO 51 ASN 52 MET 53 THR stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-09-22 loop_ _Database_name _Database_accession_code _Database_entry_mol_name _Sequence_query_to_submitted_percentage _Sequence_subject_length _Sequence_identity _Sequence_positive _Sequence_homology_expectation_value BMRB 17650 ba 100.00 94 100.00 100.00 3.80e-27 PDB 1YFB "The Solution Structure Of The N-Domain Of The Transcription Factor Abrb" 96.23 59 100.00 100.00 4.83e-26 PDB 1YSF "The Solution Structure Of The N-Domain Of The Transcription Factor Abrb" 96.23 59 100.00 100.00 4.83e-26 PDB 1Z0R "Solution Structure Of The N-Terminal Dna Recognition Domain Of The Bacillus Subtilis Transcription-State Regulator Abrb" 100.00 53 100.00 100.00 5.56e-27 PDB 2K1N "Dna Bound Structure Of The N-Terminal Domain Of Abrb" 100.00 55 100.00 100.00 3.89e-27 PDB 2RO4 "Rdc-Refined Solution Structure Of The N-Terminal Dna Recognition Domain Of The Bacillus Subtilis Transition-State Regulator Abr" 100.00 53 100.00 100.00 5.56e-27 DBJ BAA05272 "transition state regulatory protein [Bacillus subtilis]" 100.00 96 100.00 100.00 2.41e-27 DBJ BAI83483 "transcriptional regulator [Bacillus subtilis subsp. natto BEST195]" 100.00 96 100.00 100.00 2.41e-27 DBJ BAL15827 "transition state transcriptional regulatory protein AbrB [Bacillus cereus NC7401]" 100.00 94 100.00 100.00 3.41e-27 DBJ BAM48968 "transcriptional regulator [Bacillus subtilis BEST7613]" 100.00 94 100.00 100.00 1.84e-27 DBJ BAM56238 "transcriptional regulator [Bacillus subtilis BEST7003]" 100.00 94 100.00 100.00 1.84e-27 EMBL CAA31307 "unnamed protein product [Bacillus subtilis subsp. subtilis str. 168]" 100.00 96 100.00 100.00 2.41e-27 EMBL CAA43955 "abrB [Bacillus subtilis]" 100.00 94 100.00 100.00 1.84e-27 EMBL CAB11813 "transcriptional regulator for transition state genes [Bacillus subtilis subsp. subtilis str. 168]" 100.00 96 100.00 100.00 2.41e-27 EMBL CBI41163 "transcriptional regulator for transition state genes [Bacillus amyloliquefaciens DSM 7]" 100.00 94 100.00 100.00 1.84e-27 EMBL CCF03572 "Transition state regulatory protein abrB [Bacillus methylotrophicus CAU B946]" 100.00 94 100.00 100.00 1.84e-27 GB AAA22195 "abrB protein [Bacillus subtilis]" 100.00 94 100.00 100.00 1.84e-27 GB AAP07140 "Transcription state regulatory protein abrB [Bacillus cereus ATCC 14579]" 100.00 94 100.00 100.00 3.41e-27 GB AAP24090 "transition state transcriptional regulatory protein AbrB [Bacillus anthracis str. Ames]" 100.00 94 100.00 100.00 3.80e-27 GB AAS38971 "transition state transcriptional regulatory protein AbrB [Bacillus cereus ATCC 10987]" 100.00 94 100.00 100.00 3.41e-27 GB AAT29114 "transition state transcriptional regulatory protein AbrB [Bacillus anthracis str. 'Ames Ancestor']" 100.00 94 100.00 100.00 3.80e-27 PRF 1715209A "transcription regulator AbrB" 100.00 94 100.00 100.00 1.84e-27 REF NP_387918 "transition state regulatory protein AbrB [Bacillus subtilis subsp. subtilis str. 168]" 100.00 96 100.00 100.00 2.41e-27 REF NP_829939 "transcription state transcriptional regulator AbrB [Bacillus cereus ATCC 14579]" 100.00 94 100.00 100.00 3.41e-27 REF NP_842604 "transition state transcriptional regulator AbrB [Bacillus anthracis str. Ames]" 100.00 94 100.00 100.00 3.80e-27 REF WP_000843034 "transition state regulator Abh [Bacillus anthracis]" 100.00 94 100.00 100.00 3.88e-27 REF WP_000843035 "transition state regulator Abh [Bacillus anthracis]" 100.00 94 100.00 100.00 3.80e-27 SP P08874 "RecName: Full=Transition state regulatory protein AbrB" 100.00 96 100.00 100.00 2.41e-27 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $AbrBN 'B. subtilis' 1423 Eubacteria . Bacillus subtilis stop_ save_ ######################### # Experimental source # ######################### save_experimental_source _Saveframe_category experimental_source loop_ _Mol_label _Production_method _Host_organism_name_common _Genus _Species _Strain _Variant _Vector_type _Vector_name $AbrBN 'recombinant technology' 'E. coli' Escherichia coli BL21 DE3 plasmid pET24 stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_one _Saveframe_category sample _Sample_type solution _Details ; pH 5.8, 15 mM KCl, 20 mM K-PO, 1mM DTT, .02% NaN3 All experiments run at 305 K. Samples were in 95%H2O/5%D2O. ; loop_ _Mol_label _Concentration_value _Concentration_value_units _Concentration_min_value _Concentration_max_value _Isotopic_labeling $AbrBN . mM 1.5 2.5 '[U-99% 13C; U-99% 15N]' KCl 15 mM . . . K-PO 10 mM . . . DTT 1 mM . . . NaN3 0.02 % . . . D20 5 % . . . H2O 95 % . . . stop_ save_ save_sample_two _Saveframe_category sample _Sample_type solution _Details ; pH 5.8, 15 mM KCl, 20 mM K-PO, 1mM DTT, .02% NaN3 All experiments run at 305 K. Samples were in 99% d2o buffers. ; loop_ _Mol_label _Concentration_value _Concentration_value_units _Concentration_min_value _Concentration_max_value _Isotopic_labeling $AbrBN . mM 1.5 2.5 '[U-99% 13C; U-99% 15N]' KCl 15 mM . . . K-PO 10 mM . . . DTT 1 mM . . . NaN3 0.02 % . . . D20 5 % . . . H2O 95 % . . . stop_ save_ ############################ # Computer software used # ############################ save_software_one _Saveframe_category software _Name ARIA _Version 1.2 _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer_one _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model INOVA _Field_strength 600 _Details . save_ ############################# # NMR applied experiments # ############################# save_1H-15N_NOESY_(120mS_and_150mS_mixing_time)_1 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-15N NOESY (120mS and 150mS mixing time)' _Sample_label . save_ save_1H-13C_COESY_(120mS_and_120mS_folded_mixing_time)_2 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-13C COESY (120mS and 120mS folded mixing time)' _Sample_label . save_ save_3-D_HNCA_3 _Saveframe_category NMR_applied_experiment _Experiment_name '3-D HNCA' _Sample_label . save_ save_3-D_HN(CO)CA_4 _Saveframe_category NMR_applied_experiment _Experiment_name '3-D HN(CO)CA' _Sample_label . save_ save_3-D_HNCO_5 _Saveframe_category NMR_applied_experiment _Experiment_name '3-D HNCO' _Sample_label . save_ save_3-D_HN(CA)CO_6 _Saveframe_category NMR_applied_experiment _Experiment_name '3-D HN(CA)CO' _Sample_label . save_ save_3-D_CBCA(CO)NH_7 _Saveframe_category NMR_applied_experiment _Experiment_name '3-D CBCA(CO)NH' _Sample_label . save_ save_3-D_HNCACB_8 _Saveframe_category NMR_applied_experiment _Experiment_name '3-D HNCACB' _Sample_label . save_ save_D2O_exchange_via_2-D_1H-15N_HSQC_9 _Saveframe_category NMR_applied_experiment _Experiment_name 'D2O exchange via 2-D 1H-15N HSQC' _Sample_label . save_ save_CC-TOCSY-(CO)NH_10 _Saveframe_category NMR_applied_experiment _Experiment_name CC-TOCSY-(CO)NH _Sample_label . save_ save_H(CC-TOCSY-CO)NH_11 _Saveframe_category NMR_applied_experiment _Experiment_name H(CC-TOCSY-CO)NH _Sample_label . save_ save_HCCH-TOCSY_12 _Saveframe_category NMR_applied_experiment _Experiment_name HCCH-TOCSY _Sample_label . save_ save_NMR_spec_expt__0_1 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-15N NOESY (120mS and 150mS mixing time)' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_2 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-13C COESY (120mS and 120mS folded mixing time)' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_3 _Saveframe_category NMR_applied_experiment _Experiment_name '3-D HNCA' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_4 _Saveframe_category NMR_applied_experiment _Experiment_name '3-D HN(CO)CA' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_5 _Saveframe_category NMR_applied_experiment _Experiment_name '3-D HNCO' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_6 _Saveframe_category NMR_applied_experiment _Experiment_name '3-D HN(CA)CO' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_7 _Saveframe_category NMR_applied_experiment _Experiment_name '3-D CBCA(CO)NH' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_8 _Saveframe_category NMR_applied_experiment _Experiment_name '3-D HNCACB' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_9 _Saveframe_category NMR_applied_experiment _Experiment_name 'D2O exchange via 2-D 1H-15N HSQC' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_10 _Saveframe_category NMR_applied_experiment _Experiment_name CC-TOCSY-(CO)NH _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_11 _Saveframe_category NMR_applied_experiment _Experiment_name H(CC-TOCSY-CO)NH _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_12 _Saveframe_category NMR_applied_experiment _Experiment_name HCCH-TOCSY _BMRB_pulse_sequence_accession_number . _Details . save_ ####################### # Sample conditions # ####################### save_standard_h2o_conditions _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 5.8 0.1 pH temperature 305 1 K stop_ save_ save_standard_d2o_conditions _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH* 5.8 0.1 pH temperature 305 1 K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference _Saveframe_category chemical_shift_reference _Details . loop_ _Mol_common_name _Atom_type _Atom_isotope_number _Atom_group _Chem_shift_units _Chem_shift_value _Reference_method _Reference_type _External_reference_sample_geometry _External_reference_location _External_reference_axis _Indirect_shift_ratio _Correction_value_citation_label H2O H 1 protons ppm . internal direct . . . 1.0 $ref_1 TMS C 13 'methyl protons' ppm 0.00 . indirect . . . 0.25144954 $ref_2 TMS N 15 'methyl protons' ppm 0.00 . indirect . . . 0.1013291444 $ref_2 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 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Sample_label $sample_one $sample_two stop_ _Sample_conditions_label $standard_h2o_conditions _Chem_shift_reference_set_label $chemical_shift_reference _Mol_system_component_name 'AbrBN subunit 1' _Text_data_format . _Text_data . loop_ _Atom_shift_assign_ID _Residue_author_seq_code _Residue_seq_code _Residue_label _Atom_name _Atom_type _Chem_shift_value _Chem_shift_value_error _Chem_shift_ambiguity_code 1 . 2 LYS HA H 4.804 . 1 2 . 2 LYS HB2 H 1.601 . 2 3 . 2 LYS HB3 H 1.686 . 2 4 . 2 LYS HG2 H 1.238 . 2 5 . 2 LYS HG3 H 1.599 . 2 6 . 2 LYS HD2 H 1.388 . 1 7 . 2 LYS HD3 H 1.388 . 1 8 . 2 LYS HE2 H 2.882 . 1 9 . 2 LYS HE3 H 2.882 . 1 10 . 2 LYS C C 177.469 . 1 11 . 2 LYS CA C 53.131 . 1 12 . 2 LYS CB C 31.740 . 1 13 . 2 LYS CG C 26.745 . 1 14 . 2 LYS CD C 21.752 . 1 15 . 2 LYS CE C 39.322 . 1 16 . 3 SER H H 8.760 . 1 17 . 3 SER HA H 4.188 . 1 18 . 3 SER HB2 H 3.684 . 2 19 . 3 SER HB3 H 3.709 . 2 20 . 3 SER C C 176.954 . 1 21 . 3 SER CA C 55.762 . 1 22 . 3 SER CB C 61.034 . 1 23 . 3 SER N N 118.691 . 1 24 . 4 THR H H 8.263 . 1 25 . 4 THR HA H 4.209 . 1 26 . 4 THR HB H 4.191 . 1 27 . 4 THR HG2 H 1.184 . 1 28 . 4 THR C C 177.495 . 1 29 . 4 THR CA C 59.898 . 1 30 . 4 THR CB C 67.745 . 1 31 . 4 THR CG2 C 19.169 . 1 32 . 4 THR N N 114.931 . 1 33 . 5 GLY H H 8.788 . 1 34 . 5 GLY HA2 H 3.883 . 1 35 . 5 GLY HA3 H 3.883 . 1 36 . 5 GLY C C 174.899 . 1 37 . 5 GLY CA C 42.625 . 1 38 . 5 GLY N N 111.273 . 1 39 . 6 ILE H H 8.380 . 1 40 . 6 ILE HA H 4.087 . 1 41 . 6 ILE HB H 1.748 . 1 42 . 6 ILE HG12 H 1.161 . 1 43 . 6 ILE HG13 H 1.460 . 1 44 . 6 ILE HG2 H 0.716 . 1 45 . 6 ILE HD1 H 0.772 . 1 46 . 6 ILE C C 176.156 . 1 47 . 6 ILE CA C 58.435 . 1 48 . 6 ILE CB C 36.458 . 1 49 . 6 ILE CG1 C 24.465 . 2 50 . 6 ILE CG2 C 15.409 . 1 51 . 6 ILE CD1 C 10.633 . 1 52 . 6 ILE N N 122.181 . 1 53 . 7 VAL H H 8.139 . 1 54 . 7 VAL HA H 4.906 . 1 55 . 7 VAL HB H 1.549 . 1 56 . 7 VAL HG1 H 0.239 . 2 57 . 7 VAL HG2 H 0.361 . 2 58 . 7 VAL C C 179.027 . 1 59 . 7 VAL CA C 58.123 . 1 60 . 7 VAL CB C 30.686 . 1 61 . 7 VAL CG1 C 17.932 . 1 62 . 7 VAL CG2 C 18.964 . 1 63 . 7 VAL N N 126.219 . 1 64 . 8 ARG H H 9.116 . 1 65 . 8 ARG HA H 4.735 . 1 66 . 8 ARG HB2 H 1.508 . 2 67 . 8 ARG HB3 H 1.971 . 2 68 . 8 ARG HG2 H 1.338 . 2 69 . 8 ARG HG3 H 1.739 . 2 70 . 8 ARG HD2 H 3.184 . 2 71 . 8 ARG HD3 H 3.470 . 2 72 . 8 ARG HE H 7.120 . 1 73 . 8 ARG C C 176.215 . 1 74 . 8 ARG CA C 50.296 . 1 75 . 8 ARG CB C 32.551 . 1 76 . 8 ARG CG C 24.043 . 1 77 . 8 ARG CD C 40.464 . 1 78 . 8 ARG N N 126.942 . 1 79 . 8 ARG NE N 84.500 . 1 80 . 9 LYS H H 8.490 . 1 81 . 9 LYS HA H 4.876 . 1 82 . 9 LYS HB2 H 1.593 . 1 83 . 9 LYS HB3 H 1.593 . 1 84 . 9 LYS HG2 H 1.370 . 1 85 . 9 LYS HG3 H 1.370 . 1 86 . 9 LYS HD2 H 1.230 . 1 87 . 9 LYS HD3 H 1.230 . 1 88 . 9 LYS HE2 H 2.930 . 1 89 . 9 LYS HE3 H 2.930 . 1 90 . 9 LYS C C 178.309 . 1 91 . 9 LYS CA C 52.603 . 1 92 . 9 LYS CB C 31.725 . 1 93 . 9 LYS CG C 26.530 . 1 94 . 9 LYS CD C 22.744 . 1 95 . 9 LYS CE C 39.299 . 1 96 . 9 LYS N N 119.452 . 1 97 . 10 VAL H H 8.304 . 1 98 . 10 VAL HA H 4.225 . 1 99 . 10 VAL HB H 1.857 . 1 100 . 10 VAL HG1 H 0.858 . 2 101 . 10 VAL HG2 H 0.750 . 2 102 . 10 VAL C C 176.695 . 1 103 . 10 VAL CA C 58.787 . 1 104 . 10 VAL CB C 31.761 . 1 105 . 10 VAL CG1 C 18.709 . 1 106 . 10 VAL CG2 C 18.709 . 1 107 . 10 VAL N N 121.420 . 1 108 . 11 ASP H H 8.511 . 1 109 . 11 ASP HA H 4.737 . 1 110 . 11 ASP HB2 H 2.714 . 2 111 . 11 ASP HB3 H 3.296 . 2 112 . 11 ASP C C 179.483 . 1 113 . 11 ASP CA C 50.205 . 1 114 . 11 ASP CB C 38.405 . 1 115 . 11 ASP N N 127.070 . 1 116 . 12 GLU H H 9.425 . 1 117 . 12 GLU HA H 4.014 . 1 118 . 12 GLU HB2 H 1.990 . 2 119 . 12 GLU HB3 H 2.037 . 2 120 . 12 GLU HG2 H 2.350 . 2 121 . 12 GLU HG3 H 2.293 . 2 122 . 12 GLU C C 178.796 . 1 123 . 12 GLU CA C 56.485 . 1 124 . 12 GLU CB C 25.885 . 1 125 . 12 GLU CG C 33.208 . 1 126 . 12 GLU N N 116.139 . 1 127 . 13 LEU H H 8.225 . 1 128 . 13 LEU HA H 4.423 . 1 129 . 13 LEU HB2 H 1.450 . 2 130 . 13 LEU HB3 H 1.523 . 2 131 . 13 LEU HG H 1.496 . 1 132 . 13 LEU HD1 H 0.773 . 2 133 . 13 LEU HD2 H 0.762 . 2 134 . 13 LEU C C 178.513 . 1 135 . 13 LEU CA C 51.578 . 1 136 . 13 LEU CB C 39.750 . 1 137 . 13 LEU CG C 24.973 . 1 138 . 13 LEU CD1 C 21.992 . 1 139 . 13 LEU CD2 C 20.445 . 1 140 . 13 LEU N N 121.643 . 1 141 . 14 GLY H H 8.108 . 1 142 . 14 GLY HA2 H 3.200 . 2 143 . 14 GLY HA3 H 4.080 . 2 144 . 14 GLY C C 178.153 . 1 145 . 14 GLY CA C 43.195 . 1 146 . 14 GLY N N 107.637 . 1 147 . 15 ARG H H 8.398 . 1 148 . 15 ARG HA H 5.139 . 1 149 . 15 ARG HB2 H 1.170 . 2 150 . 15 ARG HB3 H 2.124 . 2 151 . 15 ARG HG2 H 1.341 . 2 152 . 15 ARG HG3 H 1.510 . 2 153 . 15 ARG HD2 H 2.630 . 2 154 . 15 ARG HD3 H 3.188 . 2 155 . 15 ARG HE H 8.900 . 1 156 . 15 ARG C C 178.550 . 1 157 . 15 ARG CA C 52.530 . 1 158 . 15 ARG CB C 29.354 . 1 159 . 15 ARG CG C 24.432 . 1 160 . 15 ARG CD C 40.255 . 1 161 . 15 ARG N N 117.447 . 1 162 . 15 ARG NE N 84.400 . 1 163 . 16 VAL H H 8.307 . 1 164 . 16 VAL HA H 4.501 . 1 165 . 16 VAL HB H 1.602 . 1 166 . 16 VAL HG1 H 0.656 . 2 167 . 16 VAL HG2 H 0.702 . 2 168 . 16 VAL C C 176.831 . 1 169 . 16 VAL CA C 56.432 . 1 170 . 16 VAL CB C 33.298 . 1 171 . 16 VAL CG1 C 17.156 . 1 172 . 16 VAL CG2 C 18.466 . 1 173 . 16 VAL N N 117.958 . 1 174 . 17 VAL H H 8.079 . 1 175 . 17 VAL HA H 3.718 . 1 176 . 17 VAL HB H 1.792 . 1 177 . 17 VAL HG1 H 0.744 . 2 178 . 17 VAL HG2 H 0.856 . 2 179 . 17 VAL C C 178.585 . 1 180 . 17 VAL CA C 59.516 . 1 181 . 17 VAL CB C 30.068 . 1 182 . 17 VAL CG1 C 18.800 . 1 183 . 17 VAL CG2 C 19.600 . 1 184 . 17 VAL N N 125.478 . 1 185 . 18 ILE H H 8.480 . 1 186 . 18 ILE HA H 4.236 . 1 187 . 18 ILE HB H 1.847 . 1 188 . 18 ILE HG12 H 1.175 . 1 189 . 18 ILE HG13 H 1.375 . 1 190 . 18 ILE HG2 H 0.762 . 1 191 . 18 ILE HD1 H 0.539 . 1 192 . 18 ILE CA C 54.641 . 1 193 . 18 ILE CB C 34.382 . 1 194 . 18 ILE CG1 C 24.100 . 2 195 . 18 ILE CG2 C 15.787 . 1 196 . 18 ILE CD1 C 9.155 . 1 197 . 18 ILE N N 127.200 . 1 198 . 19 PRO HA H 4.372 . 1 199 . 19 PRO HB2 H 1.837 . 2 200 . 19 PRO HB3 H 2.623 . 2 201 . 19 PRO HG2 H 1.900 . 2 202 . 19 PRO HG3 H 1.947 . 2 203 . 19 PRO HD2 H 3.374 . 1 204 . 19 PRO HD3 H 3.374 . 1 205 . 19 PRO C C 179.797 . 1 206 . 19 PRO CA C 60.893 . 1 207 . 19 PRO CB C 30.282 . 1 208 . 19 PRO CG C 25.287 . 1 209 . 19 PRO CD C 48.160 . 1 210 . 20 ILE H H 8.941 . 1 211 . 20 ILE HA H 3.822 . 1 212 . 20 ILE HB H 1.825 . 1 213 . 20 ILE HG12 H 1.270 . 1 214 . 20 ILE HG13 H 1.270 . 1 215 . 20 ILE HG2 H 0.913 . 1 216 . 20 ILE HD1 H 0.883 . 1 217 . 20 ILE C C 177.531 . 1 218 . 20 ILE CA C 61.126 . 1 219 . 20 ILE CB C 35.742 . 1 220 . 20 ILE CG1 C 26.839 . 2 221 . 20 ILE CG2 C 14.553 . 1 222 . 20 ILE CD1 C 11.213 . 1 223 . 20 ILE N N 126.938 . 1 224 . 21 GLU H H 9.816 . 1 225 . 21 GLU HA H 3.964 . 1 226 . 21 GLU HB2 H 1.932 . 1 227 . 21 GLU HB3 H 1.932 . 1 228 . 21 GLU HG2 H 2.221 . 2 229 . 21 GLU HG3 H 2.351 . 2 230 . 21 GLU C C 180.909 . 1 231 . 21 GLU CA C 57.755 . 1 232 . 21 GLU CB C 25.764 . 1 233 . 21 GLU CG C 33.792 . 1 234 . 21 GLU N N 121.405 . 1 235 . 22 LEU H H 7.118 . 1 236 . 22 LEU HA H 4.216 . 1 237 . 22 LEU HB2 H 1.338 . 2 238 . 22 LEU HB3 H 1.641 . 2 239 . 22 LEU HG H 1.590 . 1 240 . 22 LEU HD1 H 0.794 . 2 241 . 22 LEU HD2 H 0.798 . 2 242 . 22 LEU C C 180.359 . 1 243 . 22 LEU CA C 54.327 . 1 244 . 22 LEU CB C 38.701 . 1 245 . 22 LEU CG C 25.271 . 1 246 . 22 LEU CD1 C 22.772 . 1 247 . 22 LEU CD2 C 20.793 . 1 248 . 22 LEU N N 117.115 . 1 249 . 23 ARG H H 7.568 . 1 250 . 23 ARG HA H 3.688 . 1 251 . 23 ARG HB2 H 1.970 . 2 252 . 23 ARG HB3 H 2.156 . 2 253 . 23 ARG HG2 H 1.137 . 2 254 . 23 ARG HG3 H 1.564 . 2 255 . 23 ARG HD2 H 3.071 . 2 256 . 23 ARG HD3 H 3.182 . 2 257 . 23 ARG HE H 6.900 . 1 258 . 23 ARG C C 180.412 . 1 259 . 23 ARG CA C 58.534 . 1 260 . 23 ARG CB C 27.100 . 1 261 . 23 ARG CG C 26.754 . 1 262 . 23 ARG CD C 40.998 . 1 263 . 23 ARG N N 117.465 . 1 264 . 23 ARG NE N 81.900 . 1 265 . 24 ARG H H 8.690 . 1 266 . 24 ARG HA H 4.074 . 1 267 . 24 ARG HB2 H 1.808 . 1 268 . 24 ARG HB3 H 1.808 . 1 269 . 24 ARG HG2 H 1.600 . 2 270 . 24 ARG HG3 H 1.701 . 2 271 . 24 ARG HD2 H 3.107 . 1 272 . 24 ARG HD3 H 3.107 . 1 273 . 24 ARG HE H 7.200 . 1 274 . 24 ARG C C 181.607 . 1 275 . 24 ARG CA C 56.713 . 1 276 . 24 ARG CB C 27.364 . 1 277 . 24 ARG CG C 24.836 . 1 278 . 24 ARG CD C 40.780 . 1 279 . 24 ARG N N 117.593 . 1 280 . 24 ARG NE N 84.400 . 1 281 . 25 THR H H 7.588 . 1 282 . 25 THR HA H 3.964 . 1 283 . 25 THR HB H 4.201 . 1 284 . 25 THR HG2 H 1.256 . 1 285 . 25 THR C C 177.169 . 1 286 . 25 THR CA C 63.621 . 1 287 . 25 THR CB C 66.370 . 1 288 . 25 THR CG2 C 19.024 . 1 289 . 25 THR N N 115.278 . 1 290 . 26 LEU H H 7.387 . 1 291 . 26 LEU HA H 4.369 . 1 292 . 26 LEU HB2 H 1.531 . 2 293 . 26 LEU HB3 H 1.626 . 2 294 . 26 LEU HG H 1.650 . 1 295 . 26 LEU HD1 H 0.751 . 2 296 . 26 LEU HD2 H 0.761 . 2 297 . 26 LEU C C 178.712 . 1 298 . 26 LEU CA C 52.271 . 1 299 . 26 LEU CB C 40.387 . 1 300 . 26 LEU CG C 25.213 . 1 301 . 26 LEU CD1 C 22.840 . 1 302 . 26 LEU CD2 C 20.496 . 1 303 . 26 LEU N N 118.354 . 1 304 . 27 GLY H H 7.695 . 1 305 . 27 GLY HA2 H 3.826 . 2 306 . 27 GLY HA3 H 3.870 . 2 307 . 27 GLY C C 176.181 . 1 308 . 27 GLY CA C 44.512 . 1 309 . 27 GLY N N 109.556 . 1 310 . 28 ILE H H 8.174 . 1 311 . 28 ILE HA H 4.179 . 1 312 . 28 ILE HB H 1.499 . 1 313 . 28 ILE HG12 H 1.504 . 1 314 . 28 ILE HG13 H 1.504 . 1 315 . 28 ILE HG2 H 0.790 . 1 316 . 28 ILE HD1 H 0.741 . 1 317 . 28 ILE C C 176.039 . 1 318 . 28 ILE CA C 58.022 . 1 319 . 28 ILE CB C 36.346 . 1 320 . 28 ILE CG1 C 24.808 . 2 321 . 28 ILE CG2 C 15.553 . 1 322 . 28 ILE CD1 C 11.199 . 1 323 . 28 ILE N N 119.528 . 1 324 . 29 ALA H H 9.472 . 1 325 . 29 ALA HA H 4.431 . 1 326 . 29 ALA HB H 1.349 . 1 327 . 29 ALA C C 178.860 . 1 328 . 29 ALA CA C 47.833 . 1 329 . 29 ALA CB C 18.659 . 1 330 . 29 ALA N N 110.840 . 1 331 . 30 GLU H H 8.584 . 1 332 . 30 GLU HA H 3.698 . 1 333 . 30 GLU HB2 H 1.861 . 2 334 . 30 GLU HB3 H 1.942 . 2 335 . 30 GLU HG2 H 2.097 . 2 336 . 30 GLU HG3 H 2.294 . 2 337 . 30 GLU C C 178.852 . 1 338 . 30 GLU CA C 56.753 . 1 339 . 30 GLU CB C 26.634 . 1 340 . 30 GLU CG C 33.700 . 1 341 . 30 GLU N N 119.415 . 1 342 . 31 LYS H H 8.222 . 1 343 . 31 LYS HA H 4.107 . 1 344 . 31 LYS HB2 H 1.980 . 2 345 . 31 LYS HB3 H 2.104 . 2 346 . 31 LYS HG2 H 1.607 . 2 347 . 31 LYS HG3 H 1.690 . 2 348 . 31 LYS HD2 H 1.351 . 1 349 . 31 LYS HD3 H 1.351 . 1 350 . 31 LYS HE2 H 2.923 . 1 351 . 31 LYS HE3 H 2.923 . 1 352 . 31 LYS C C 177.609 . 1 353 . 31 LYS CA C 55.551 . 1 354 . 31 LYS CB C 28.132 . 1 355 . 31 LYS CG C 26.520 . 1 356 . 31 LYS CD C 22.985 . 1 357 . 31 LYS CE C 30.477 . 1 358 . 31 LYS N N 115.560 . 1 359 . 32 ASP H H 7.781 . 1 360 . 32 ASP HA H 4.623 . 1 361 . 32 ASP HB2 H 2.483 . 2 362 . 32 ASP HB3 H 2.950 . 2 363 . 32 ASP C C 176.706 . 1 364 . 32 ASP CA C 52.790 . 1 365 . 32 ASP CB C 39.124 . 1 366 . 32 ASP N N 119.951 . 1 367 . 33 ALA H H 8.548 . 1 368 . 33 ALA HA H 4.621 . 1 369 . 33 ALA HB H 1.299 . 1 370 . 33 ALA C C 177.831 . 1 371 . 33 ALA CA C 48.426 . 1 372 . 33 ALA CB C 18.138 . 1 373 . 33 ALA N N 121.496 . 1 374 . 34 LEU H H 9.016 . 1 375 . 34 LEU HA H 5.015 . 1 376 . 34 LEU HB2 H 1.170 . 2 377 . 34 LEU HB3 H 1.570 . 2 378 . 34 LEU HG H 1.600 . 1 379 . 34 LEU HD1 H 0.636 . 2 380 . 34 LEU HD2 H 0.640 . 2 381 . 34 LEU C C 176.432 . 1 382 . 34 LEU CA C 50.509 . 1 383 . 34 LEU CB C 41.318 . 1 384 . 34 LEU CG C 24.093 . 1 385 . 34 LEU CD1 C 24.100 . 1 386 . 34 LEU CD2 C 20.607 . 1 387 . 34 LEU N N 121.358 . 1 388 . 35 GLU H H 9.428 . 1 389 . 35 GLU HA H 4.743 . 1 390 . 35 GLU HB2 H 1.841 . 2 391 . 35 GLU HB3 H 2.060 . 2 392 . 35 GLU HG2 H 1.972 . 1 393 . 35 GLU HG3 H 1.972 . 1 394 . 35 GLU C C 177.033 . 1 395 . 35 GLU CA C 52.469 . 1 396 . 35 GLU CB C 29.790 . 1 397 . 35 GLU CG C 33.631 . 1 398 . 35 GLU N N 123.379 . 1 399 . 36 ILE H H 8.373 . 1 400 . 36 ILE HA H 5.107 . 1 401 . 36 ILE HB H 1.601 . 1 402 . 36 ILE HG12 H 1.606 . 1 403 . 36 ILE HG13 H 1.606 . 1 404 . 36 ILE HG2 H 0.638 . 1 405 . 36 ILE HD1 H 0.689 . 1 406 . 36 ILE C C 177.525 . 1 407 . 36 ILE CA C 58.390 . 1 408 . 36 ILE CB C 36.419 . 1 409 . 36 ILE CG1 C 36.100 . 2 410 . 36 ILE CG2 C 11.349 . 1 411 . 36 ILE CD1 C 15.041 . 1 412 . 36 ILE N N 122.969 . 1 413 . 37 TYR H H 9.590 . 1 414 . 37 TYR HA H 5.045 . 1 415 . 37 TYR HB2 H 2.858 . 2 416 . 37 TYR HB3 H 2.963 . 2 417 . 37 TYR C C 175.168 . 1 418 . 37 TYR CA C 53.646 . 1 419 . 37 TYR CB C 38.447 . 1 420 . 37 TYR N N 127.104 . 1 421 . 38 VAL H H 8.680 . 1 422 . 38 VAL HA H 5.053 . 1 423 . 38 VAL HB H 1.949 . 1 424 . 38 VAL HG1 H 0.904 . 2 425 . 38 VAL HG2 H 0.900 . 2 426 . 38 VAL C C 176.831 . 1 427 . 38 VAL CA C 57.599 . 1 428 . 38 VAL CB C 32.467 . 1 429 . 38 VAL CG1 C 19.038 . 1 430 . 38 VAL CG2 C 19.038 . 1 431 . 38 VAL N N 116.566 . 1 432 . 39 ASP H H 8.535 . 1 433 . 39 ASP HA H 4.759 . 1 434 . 39 ASP HB2 H 2.551 . 1 435 . 39 ASP HB3 H 2.551 . 1 436 . 39 ASP C C 176.951 . 1 437 . 39 ASP CA C 51.041 . 1 438 . 39 ASP CB C 41.147 . 1 439 . 39 ASP N N 125.422 . 1 440 . 40 ASP H H 8.822 . 1 441 . 40 ASP HA H 4.141 . 1 442 . 40 ASP HB2 H 2.618 . 2 443 . 40 ASP HB3 H 2.816 . 2 444 . 40 ASP C C 177.469 . 1 445 . 40 ASP CA C 54.063 . 1 446 . 40 ASP CB C 36.974 . 1 447 . 40 ASP N N 123.683 . 1 448 . 41 GLU H H 8.831 . 1 449 . 41 GLU HA H 4.205 . 1 450 . 41 GLU HB2 H 2.134 . 2 451 . 41 GLU HB3 H 2.194 . 2 452 . 41 GLU HG2 H 2.138 . 1 453 . 41 GLU HG3 H 2.138 . 1 454 . 41 GLU C C 176.031 . 1 455 . 41 GLU CA C 54.221 . 1 456 . 41 GLU CB C 26.629 . 1 457 . 41 GLU CG C 33.943 . 1 458 . 41 GLU N N 118.692 . 1 459 . 42 LYS H H 8.004 . 1 460 . 42 LYS HA H 4.739 . 1 461 . 42 LYS HB2 H 1.508 . 2 462 . 42 LYS HB3 H 1.975 . 2 463 . 42 LYS HG2 H 1.600 . 1 464 . 42 LYS HG3 H 1.600 . 1 465 . 42 LYS HD2 H 1.333 . 1 466 . 42 LYS HD3 H 1.333 . 1 467 . 42 LYS HE2 H 2.901 . 1 468 . 42 LYS HE3 H 2.901 . 1 469 . 42 LYS C C 176.537 . 1 470 . 42 LYS CA C 52.523 . 1 471 . 42 LYS CB C 32.017 . 1 472 . 42 LYS CG C 26.544 . 1 473 . 42 LYS CD C 21.199 . 1 474 . 42 LYS CE C 38.659 . 1 475 . 42 LYS N N 118.263 . 1 476 . 43 ILE H H 8.616 . 1 477 . 43 ILE HA H 4.383 . 1 478 . 43 ILE HB H 1.607 . 1 479 . 43 ILE HG12 H 1.600 . 1 480 . 43 ILE HG13 H 1.600 . 1 481 . 43 ILE HG2 H 0.711 . 1 482 . 43 ILE HD1 H 0.577 . 1 483 . 43 ILE C C 175.446 . 1 484 . 43 ILE CA C 58.085 . 1 485 . 43 ILE CB C 36.755 . 1 486 . 43 ILE CG1 C 25.526 . 2 487 . 43 ILE CG2 C 15.358 . 1 488 . 43 ILE CD1 C 11.171 . 1 489 . 43 ILE N N 120.141 . 1 490 . 44 ILE H H 8.988 . 1 491 . 44 ILE HA H 4.795 . 1 492 . 44 ILE HB H 1.040 . 1 493 . 44 ILE HG12 H 0.985 . 1 494 . 44 ILE HG13 H 1.182 . 1 495 . 44 ILE HG2 H 0.624 . 1 496 . 44 ILE HD1 H 0.663 . 1 497 . 44 ILE C C 175.966 . 1 498 . 44 ILE CA C 57.042 . 1 499 . 44 ILE CB C 37.072 . 1 500 . 44 ILE CG1 C 26.337 . 2 501 . 44 ILE CG2 C 16.300 . 1 502 . 44 ILE CD1 C 12.076 . 1 503 . 44 ILE N N 127.837 . 1 504 . 45 LEU H H 9.420 . 1 505 . 45 LEU HA H 5.401 . 1 506 . 45 LEU HB2 H 1.166 . 2 507 . 45 LEU HB3 H 1.680 . 2 508 . 45 LEU HG H 1.554 . 1 509 . 45 LEU HD1 H 0.630 . 2 510 . 45 LEU HD2 H 0.610 . 2 511 . 45 LEU C C 177.356 . 1 512 . 45 LEU CA C 50.779 . 1 513 . 45 LEU CB C 41.538 . 1 514 . 45 LEU CG C 25.300 . 1 515 . 45 LEU CD1 C 23.400 . 1 516 . 45 LEU CD2 C 23.400 . 1 517 . 45 LEU N N 124.494 . 1 518 . 46 LYS H H 8.613 . 1 519 . 46 LYS HA H 4.776 . 1 520 . 46 LYS HB2 H 1.725 . 2 521 . 46 LYS HB3 H 1.895 . 2 522 . 46 LYS HG2 H 1.360 . 1 523 . 46 LYS HG3 H 1.360 . 1 524 . 46 LYS HD2 H 1.501 . 1 525 . 46 LYS HD3 H 1.501 . 1 526 . 46 LYS HE2 H 2.853 . 1 527 . 46 LYS HE3 H 2.853 . 1 528 . 46 LYS C C 176.922 . 1 529 . 46 LYS CA C 51.500 . 1 530 . 46 LYS CB C 34.200 . 1 531 . 46 LYS CG C 26.950 . 1 532 . 46 LYS CD C 21.596 . 1 533 . 46 LYS CE C 38.959 . 1 534 . 46 LYS N N 118.620 . 1 535 . 47 LYS H H 9.253 . 1 536 . 47 LYS HA H 4.182 . 1 537 . 47 LYS HB2 H 1.600 . 2 538 . 47 LYS HB3 H 1.821 . 2 539 . 47 LYS HG2 H 1.617 . 2 540 . 47 LYS HG3 H 1.452 . 2 541 . 47 LYS HD2 H 1.313 . 1 542 . 47 LYS HD3 H 1.313 . 1 543 . 47 LYS HE2 H 2.926 . 1 544 . 47 LYS HE3 H 2.926 . 1 545 . 47 LYS C C 178.026 . 1 546 . 47 LYS CA C 56.400 . 1 547 . 47 LYS CB C 29.700 . 1 548 . 47 LYS CG C 26.968 . 1 549 . 47 LYS CD C 23.294 . 1 550 . 47 LYS CE C 39.493 . 1 551 . 47 LYS N N 123.651 . 1 552 . 48 TYR H H 8.584 . 1 553 . 48 TYR HA H 4.566 . 1 554 . 48 TYR HB2 H 2.740 . 2 555 . 48 TYR HB3 H 2.697 . 2 556 . 48 TYR C C 175.903 . 1 557 . 48 TYR CA C 55.200 . 1 558 . 48 TYR CB C 36.800 . 1 559 . 48 TYR N N 126.965 . 1 560 . 49 LYS H H 8.096 . 1 561 . 49 LYS HA H 4.429 . 1 562 . 49 LYS HB2 H 1.492 . 2 563 . 49 LYS HB3 H 1.616 . 2 564 . 49 LYS HG2 H 1.601 . 1 565 . 49 LYS HG3 H 1.601 . 1 566 . 49 LYS HD2 H 1.230 . 1 567 . 49 LYS HD3 H 1.230 . 1 568 . 49 LYS HE2 H 2.910 . 1 569 . 49 LYS HE3 H 2.910 . 1 570 . 49 LYS CA C 50.700 . 1 571 . 49 LYS CB C 30.600 . 1 572 . 49 LYS CG C 26.600 . 1 573 . 49 LYS CD C 21.500 . 1 574 . 49 LYS CE C 39.900 . 1 575 . 49 LYS N N 129.273 . 1 576 . 50 PRO HA H 4.149 . 1 577 . 50 PRO HB2 H 1.826 . 2 578 . 50 PRO HB3 H 2.113 . 2 579 . 50 PRO HG2 H 1.823 . 1 580 . 50 PRO HG3 H 1.823 . 1 581 . 50 PRO HD2 H 2.978 . 2 582 . 50 PRO HD3 H 3.408 . 2 583 . 50 PRO C C 178.153 . 1 584 . 50 PRO CA C 60.300 . 1 585 . 50 PRO CB C 29.200 . 1 586 . 50 PRO CG C 24.240 . 1 587 . 50 PRO CD C 47.577 . 1 588 . 51 ASN H H 8.372 . 1 589 . 51 ASN HA H 4.569 . 1 590 . 51 ASN HB2 H 2.742 . 2 591 . 51 ASN HB3 H 2.780 . 2 592 . 51 ASN HD21 H 7.567 . 2 593 . 51 ASN HD22 H 6.887 . 2 594 . 51 ASN C C 176.655 . 1 595 . 51 ASN CA C 50.900 . 1 596 . 51 ASN CB C 36.100 . 1 597 . 51 ASN N N 117.769 . 1 598 . 51 ASN ND2 N 112.886 . 1 599 . 52 MET H H 8.249 . 1 600 . 52 MET HA H 4.496 . 1 601 . 52 MET HB2 H 1.950 . 2 602 . 52 MET HB3 H 2.130 . 2 603 . 52 MET HG2 H 2.470 . 2 604 . 52 MET HG3 H 2.516 . 2 605 . 52 MET C C 177.143 . 1 606 . 52 MET CA C 51.700 . 1 607 . 52 MET CB C 37.300 . 1 608 . 52 MET CG C 24.810 . 1 609 . 52 MET N N 120.664 . 1 610 . 53 THR H H 7.707 . 1 611 . 53 THR HA H 4.089 . 1 612 . 53 THR HB H 4.167 . 1 613 . 53 THR HG2 H 1.108 . 1 614 . 53 THR CA C 60.700 . 1 615 . 53 THR CB C 68.100 . 1 616 . 53 THR CG2 C 19.400 . 1 617 . 53 THR N N 119.751 . 1 stop_ save_