data_4349 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Backbone Resonance Assignments for the Fv Fragment of the Catalytic Antibody NPN43C9 with Bound p-nitrophenol ; _BMRB_accession_number 4349 _BMRB_flat_file_name bmr4349.str _Entry_type original _Submission_date 1999-05-19 _Accession_date 1999-05-19 _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 Kroon Gerard 'J. A.' . 2 Martinez-Yamout Maria A. . 3 Krebs Joseph F. . 4 Chung John . . 5 Dyson H. Jane . 6 Wright Peter E. . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 2 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 385 "13C chemical shifts" 564 "15N chemical shifts" 195 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2007-07-13 original author . stop_ _Original_release_date 2007-07-13 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full ; Kroon, G. J. A., Martinez-Yamout, M. A., Krebs, J. F., Chung, J., Dyson, H. J., and Wright, P. E., "Backbone Resonance Assignments for the Fv Fragment of the Catalytic Antibody NPN43C9 with Bound p-nitrophenol," J. Biomol. NMR 15, 83-84 (1999). ; _Citation_title ; Backbone Resonance Assignments for the Fv Fragment of the Catalytic Antibody NPN43C9 with Bound p-nitrophenol ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code 20016852 _PubMed_ID ? loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Kroon Gerard 'J. A.' . 2 Martinez-Yamout Maria A. . 3 Krebs Joseph F. . 4 Chung John . . 5 Dyson H. Jane . 6 Wright Peter E. . stop_ _Journal_abbreviation 'J. Biomol. NMR' _Journal_name_full 'Journal of Biomolecular NMR' _Journal_volume 15 _Journal_issue . _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 83 _Page_last 84 _Year 1999 _Details . loop_ _Keyword 'Catalytic antibody' 'Fv fragment' stop_ save_ ####################################### # Cited references within the entry # ####################################### save_citation_1 _Saveframe_category citation _Citation_full 'Delaglio et al. J. Biomol. NMR, 6, 277 (1995)' _Citation_title 'NMRPipe: a multidimensional spectral processing system based on UNIX pipes.' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 8520220 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Delaglio F . . 2 Grzesiek S . . 3 Vuister 'G W' W. . 4 Zhu G . . 5 Pfeifer J . . 6 Bax A . . stop_ _Journal_abbreviation 'J. Biomol. NMR' _Journal_name_full 'Journal of biomolecular NMR' _Journal_volume 6 _Journal_issue 3 _Journal_CSD . _Book_title . _Book_chapter_title . _Book_volume . _Book_series . _Book_publisher . _Book_publisher_city . _Book_ISBN . _Conference_title . _Conference_site . _Conference_state_province . _Conference_country . _Conference_start_date . _Conference_end_date . _Conference_abstract_number . _Thesis_institution . _Thesis_institution_city . _Thesis_institution_country . _Page_first 277 _Page_last 293 _Year 1995 _Details ; The NMRPipe system is a UNIX software environment of processing, graphics, and analysis tools designed to meet current routine and research-oriented multidimensional processing requirements, and to anticipate and accommodate future demands and developments. The system is based on UNIX pipes, which allow programs running simultaneously to exchange streams of data under user control. In an NMRPipe processing scheme, a stream of spectral data flows through a pipeline of processing programs, each of which performs one component of the overall scheme, such as Fourier transformation or linear prediction. Complete multidimensional processing schemes are constructed as simple UNIX shell scripts. The processing modules themselves maintain and exploit accurate records of data sizes, detection modes, and calibration information in all dimensions, so that schemes can be constructed without the need to explicitly define or anticipate data sizes or storage details of real and imaginary channels during processing. The asynchronous pipeline scheme provides other substantial advantages, including high flexibility, favorable processing speeds, choice of both all-in-memory and disk-bound processing, easy adaptation to different data formats, simpler software development and maintenance, and the ability to distribute processing tasks on multi-CPU computers and computer networks. ; save_ save_citation_2 _Saveframe_category citation _Citation_full 'Johson et al. J. Biomol. NMR, 4, 603 (1994)' _Citation_title 'NMR View: A computer program for the visualization and analysis of NMR data' _Citation_status . _Citation_type . _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID ? loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Johson . . . stop_ _Journal_abbreviation 'J. Biomol. NMR' _Journal_name_full . _Journal_volume 4 _Journal_issue 5 _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 603 _Page_last 614 _Year 1994 _Details . save_ save_citation_3 _Saveframe_category citation _Citation_full 'Grezsiek et al. J. Biomol. NMR, 3, 185 (1993)' _Citation_title 'Amino acid type determination in the sequential assignment procedure of uniformly 13C/15N-enriched proteins' _Citation_status . _Citation_type . _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 8477186 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Grzesiek S. . . 2 Bax A. . . stop_ _Journal_abbreviation 'J. Biomol. NMR' _Journal_name_full . _Journal_volume 3 _Journal_issue 2 _Journal_CSD . _Book_title . _Book_chapter_title . _Book_volume . _Book_series . _Book_publisher . _Book_publisher_city . _Book_ISBN . _Conference_title . _Conference_site . _Conference_state_province . _Conference_country . _Conference_start_date . _Conference_end_date . _Conference_abstract_number . _Thesis_institution . _Thesis_institution_city . _Thesis_institution_country . _Page_first 185 _Page_last 204 _Year 1993 _Details . save_ ################################## # Molecular system description # ################################## save_FvNPN43C9 _Saveframe_category molecular_system _Mol_system_name 'Fv fragment of the catalytic antibody NPN43C9' _Abbreviation_common FvNPN43C9 _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label Vh $Vh Vl $Vl p-nitrophenol $NPO stop_ _System_molecular_weight 29309 _System_physical_state native _System_oligomer_state heterodimer _System_paramagnetic no _System_thiol_state 'fully oxidized' loop_ _Biological_function 'esterolytic antibody' stop_ _Database_query_date . _Details ; The transition state analog in the model structure has been replaced by the product p-nitrophenol in this study. The backbone assignments of the dimer are 90% complete. The 13CA and 13CB chemical shifts were obtained using deuterated protein and are NOT corrected for the deuterium effect. ; save_ ######################## # Monomeric polymers # ######################## save_Vl _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'Variable light chain' _Abbreviation_common vl _Molecular_mass . _Mol_thiol_state . _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 113 _Mol_residue_sequence ; DVVMTQTPSSLAMSVGQKVT MSCKSSQSLLNISNQKNYLA WYQQKPGQSPKLLVYFASTR ESGVPDRFIGSGSGTDFTLT ISSVQAEDQADYFCQQHYRA PRTFGGGTKLEIK ; loop_ _Residue_seq_code _Residue_label 1 ASP 2 VAL 3 VAL 4 MET 5 THR 6 GLN 7 THR 8 PRO 9 SER 10 SER 11 LEU 12 ALA 13 MET 14 SER 15 VAL 16 GLY 17 GLN 18 LYS 19 VAL 20 THR 21 MET 22 SER 23 CYS 24 LYS 25 SER 26 SER 27 GLN 28 SER 29 LEU 30 LEU 31 ASN 32 ILE 33 SER 34 ASN 35 GLN 36 LYS 37 ASN 38 TYR 39 LEU 40 ALA 41 TRP 42 TYR 43 GLN 44 GLN 45 LYS 46 PRO 47 GLY 48 GLN 49 SER 50 PRO 51 LYS 52 LEU 53 LEU 54 VAL 55 TYR 56 PHE 57 ALA 58 SER 59 THR 60 ARG 61 GLU 62 SER 63 GLY 64 VAL 65 PRO 66 ASP 67 ARG 68 PHE 69 ILE 70 GLY 71 SER 72 GLY 73 SER 74 GLY 75 THR 76 ASP 77 PHE 78 THR 79 LEU 80 THR 81 ILE 82 SER 83 SER 84 VAL 85 GLN 86 ALA 87 GLU 88 ASP 89 GLN 90 ALA 91 ASP 92 TYR 93 PHE 94 CYS 95 GLN 96 GLN 97 HIS 98 TYR 99 ARG 100 ALA 101 PRO 102 ARG 103 THR 104 PHE 105 GLY 106 GLY 107 GLY 108 THR 109 LYS 110 LEU 111 GLU 112 ILE 113 LYS stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-01-29 loop_ _Database_name _Database_accession_code _Database_entry_mol_name _Sequence_query_to_submitted_percentage _Sequence_subject_length _Sequence_identity _Sequence_positive _Sequence_homology_expectation_value PDB 43C9 "Crystallographic Structure Of The Esterolytic And Amidolytic 43c9 Antibody" 100.00 118 100.00 100.00 1.26e-77 PDB 43CA "Crystallographic Structure Of The Esterolytic And Amidolytic 43c9 Antibody With Bound P-Nitrophenol" 100.00 117 100.00 100.00 8.99e-78 GB AAA73053 "7A4-1/212 SCA fusion protein, partial [synthetic construct]" 100.00 244 100.00 100.00 2.76e-77 stop_ save_ save_Vh _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'Variable heavy chain' _Abbreviation_common vh _Molecular_mass . _Mol_thiol_state . _Details . _Residue_count 117 _Mol_residue_sequence ; QVQLVESGPGLVAPSQSLSI TCTVSGISLSRYNVHWVRQS PGKGLEWLGMIWGGGSIEYN PALKSRLSISKDNSKSQIFL KMNSLQTDDSAMYYCVSYGY GGDRFSYWGQGTLVTVS ; loop_ _Residue_seq_code _Residue_label 1 GLN 2 VAL 3 GLN 4 LEU 5 VAL 6 GLU 7 SER 8 GLY 9 PRO 10 GLY 11 LEU 12 VAL 13 ALA 14 PRO 15 SER 16 GLN 17 SER 18 LEU 19 SER 20 ILE 21 THR 22 CYS 23 THR 24 VAL 25 SER 26 GLY 27 ILE 28 SER 29 LEU 30 SER 31 ARG 32 TYR 33 ASN 34 VAL 35 HIS 36 TRP 37 VAL 38 ARG 39 GLN 40 SER 41 PRO 42 GLY 43 LYS 44 GLY 45 LEU 46 GLU 47 TRP 48 LEU 49 GLY 50 MET 51 ILE 52 TRP 53 GLY 54 GLY 55 GLY 56 SER 57 ILE 58 GLU 59 TYR 60 ASN 61 PRO 62 ALA 63 LEU 64 LYS 65 SER 66 ARG 67 LEU 68 SER 69 ILE 70 SER 71 LYS 72 ASP 73 ASN 74 SER 75 LYS 76 SER 77 GLN 78 ILE 79 PHE 80 LEU 81 LYS 82 MET 83 ASN 84 SER 85 LEU 86 GLN 87 THR 88 ASP 89 ASP 90 SER 91 ALA 92 MET 93 TYR 94 TYR 95 CYS 96 VAL 97 SER 98 TYR 99 GLY 100 TYR 101 GLY 102 GLY 103 ASP 104 ARG 105 PHE 106 SER 107 TYR 108 TRP 109 GLY 110 GLN 111 GLY 112 THR 113 LEU 114 VAL 115 THR 116 VAL 117 SER stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date . save_ ############# # Ligands # ############# save_NPO _Saveframe_category ligand _Mol_type non-polymer _Name_common "NPO (P-NITROPHENOL)" _BMRB_code . _PDB_code NPO _Molecular_mass 139.109 _Mol_charge 0 _Mol_paramagnetic . _Mol_aromatic yes _Details ; Information obtained from PDB's Chemical Component Dictionary at http://wwpdb-remediation.rutgers.edu/downloads.html Downloaded on Thu Jul 14 16:35:50 2011 ; loop_ _Atom_name _PDB_atom_name _Atom_type _Atom_chirality _Atom_charge _Atom_oxidation_number _Atom_unpaired_electrons C1 C1 C . 0 . ? C2 C2 C . 0 . ? C3 C3 C . 0 . ? C4 C4 C . 0 . ? C5 C5 C . 0 . ? C6 C6 C . 0 . ? OH OH O . 0 . ? N1 N1 N . 1 . ? O2 O2 O . -1 . ? O3 O3 O . 0 . ? H2 H2 H . 0 . ? H3 H3 H . 0 . ? H5 H5 H . 0 . ? H6 H6 H . 0 . ? HO HO H . 0 . ? stop_ loop_ _Bond_order _Bond_atom_one_atom_name _Bond_atom_two_atom_name _PDB_bond_atom_one_atom_name _PDB_bond_atom_two_atom_name DOUB C1 C2 ? ? SING C1 C6 ? ? SING C1 N1 ? ? SING C2 C3 ? ? SING C2 H2 ? ? DOUB C3 C4 ? ? SING C3 H3 ? ? SING C4 C5 ? ? SING C4 OH ? ? DOUB C5 C6 ? ? SING C5 H5 ? ? SING C6 H6 ? ? SING OH HO ? ? SING N1 O2 ? ? DOUB N1 O3 ? ? stop_ _Mol_thiol_state . _Sequence_homology_query_date . save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $Vh mouse 10090 Eukaryota Metazoa Mus musculus $Vl mouse 10090 Eukaryota Metazoa Mus musculus stop_ save_ ######################### # Experimental source # ######################### save_experimental_source _Saveframe_category experimental_source loop_ _Mol_label _Production_method _Host_organism_name_common _Genus _Species _Strain _Vector_type _Vector_name $Vh 'recombinant technology' 'E. coli' Escherichia coli BL21(DE3) plasmid pJK34 $Vl 'recombinant technology' 'E. coli' Escherichia coli BL21(DE3) plasmid pJK34 stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Saveframe_category sample _Sample_type solution _Details ; All samples contained the same concentration of protein and were made using the same buffer conditions. ; loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $Vh 0.5 mM '[U-90% 15N; U-90% 13C, U-70% 2H]' $Vl 0.5 mM '[U-90% 15N; U-90% 13C, U-70% 2H]' d11Tris 10 mM . NaCl 100 mM . p-nitrophenol 80 uM . stop_ save_ ############################ # Computer software used # ############################ save_NMRPipe _Saveframe_category software _Name NMRPipe _Version . loop_ _Task 'data processing' stop_ _Details . _Citation_label $citation_1 save_ save_NMRView _Saveframe_category software _Name NMRView _Version NMRView3.1.2. loop_ _Task 'data analysis' stop_ _Details . _Citation_label $citation_2 save_ save_seq_prob _Saveframe_category software _Name seq_prob _Version . loop_ _Task assignments stop_ _Details . _Citation_label $citation_3 save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model AMX _Field_strength 500 _Details . save_ save_spectrometer_2 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model DRX _Field_strength 600 _Details . save_ save_spectrometer_3 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model DRX _Field_strength 800 _Details . save_ ############################# # NMR applied experiments # ############################# save_2D_1H-15N_HSQC_1 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-15N HSQC' _Sample_label $sample_1 save_ save_3D_1H-1H-15N_NOESY_2 _Saveframe_category NMR_applied_experiment _Experiment_name '3D 1H-1H-15N NOESY' _Sample_label $sample_1 save_ save_3D_1H-1H-15N_TOCSY_3 _Saveframe_category NMR_applied_experiment _Experiment_name '3D 1H-1H-15N TOCSY' _Sample_label $sample_1 save_ save_3D_HNCA_4 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCA' _Sample_label $sample_1 save_ save_3D_HN(CO)CA_5 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HN(CO)CA' _Sample_label $sample_1 save_ save_3D_HNCACB_6 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCACB' _Sample_label $sample_1 save_ save_3D_HN(CO)CACB_7 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HN(CO)CACB' _Sample_label $sample_1 save_ save_3D_HNCO_8 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCO' _Sample_label $sample_1 save_ ####################### # Sample conditions # ####################### save_conditions_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 6.8 0.2 pH temperature 298 1 K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference_set_1 _Saveframe_category chemical_shift_reference _Details . loop_ _Mol_common_name _Atom_type _Atom_isotope_number _Atom_group _Chem_shift_units _Chem_shift_value _Reference_method _Reference_type _External_reference_sample_geometry _External_reference_location _External_reference_axis _Indirect_shift_ratio DSS C 13 'methyl protons' ppm 0.0 . indirect . . . 0.251449530 DSS H 1 'methyl protons' ppm 0.0 internal direct . . . 1.000000000 DSS N 15 'methyl protons' ppm 0.0 . indirect . . . 0.101329118 stop_ save_ ################################### # Assigned chemical shift lists # ################################### ################################################################### # Chemical Shift Ambiguity Index Value Definitions # # # # The values other than 1 are used for those atoms with different # # chemical shifts that cannot be assigned to stereospecific atoms # # or to specific residues or chains. # # # # Index Value Definition # # # # 1 Unique (including isolated methyl protons, # # geminal atoms, and geminal methyl # # groups with identical chemical shifts) # # (e.g. ILE HD11, HD12, HD13 protons) # # 2 Ambiguity of geminal atoms or geminal methyl # # proton groups (e.g. ASP HB2 and HB3 # # protons, LEU CD1 and CD2 carbons, or # # LEU HD11, HD12, HD13 and HD21, HD22, # # HD23 methyl protons) # # 3 Aromatic atoms on opposite sides of # # symmetrical rings (e.g. TYR HE1 and HE2 # # protons) # # 4 Intraresidue ambiguities (e.g. LYS HG and # # HD protons or TRP HZ2 and HZ3 protons) # # 5 Interresidue ambiguities (LYS 12 vs. LYS 27) # # 6 Intermolecular ambiguities (e.g. ASP 31 CA # # in monomer 1 and ASP 31 CA in monomer 2 # # of an asymmetrical homodimer, duplex # # DNA assignments, or other assignments # # that may apply to atoms in one or more # # molecule in the molecular assembly) # # 9 Ambiguous, specific ambiguity not defined # # # ################################################################### save_assigned_chemical_shifts_Vl _Saveframe_category assigned_chemical_shifts _Details ; The chemical shifts for 13CA and 13CB have NOT been corrected for the deuterium effect. Sample = "Vl bound" ; loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $conditions_1 _Chem_shift_reference_set_label $chemical_shift_reference_set_1 _Mol_system_component_name Vl _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 VAL C C 176.2 0.5 1 2 . 2 VAL CB C 40.4 0.3 1 3 . 3 VAL H H 8.51 0.04 1 4 . 3 VAL HA H 4.03 0.04 1 5 . 3 VAL C C 175.5 0.5 1 6 . 3 VAL CA C 62.0 0.3 1 7 . 3 VAL CB C 33.5 0.3 1 8 . 3 VAL N N 127.7 0.3 1 9 . 4 MET H H 8.86 0.04 1 10 . 4 MET HA H 5.44 0.04 1 11 . 4 MET C C 176.1 0.5 1 12 . 4 MET CA C 51.5 0.3 1 13 . 4 MET CB C 30.3 0.3 1 14 . 4 MET N N 127.6 0.3 1 15 . 5 THR H H 9.50 0.04 1 16 . 5 THR HA H 4.61 0.04 1 17 . 5 THR C C 171.9 0.5 1 18 . 5 THR CA C 61.9 0.3 1 19 . 5 THR CB C 70.0 0.3 1 20 . 5 THR N N 120.5 0.3 1 21 . 6 GLN H H 8.56 0.04 1 22 . 6 GLN HA H 4.86 0.04 1 23 . 6 GLN C C 175.7 0.5 1 24 . 6 GLN CA C 60.0 0.3 1 25 . 6 GLN CB C 31.0 0.3 1 26 . 6 GLN N N 129.6 0.3 1 27 . 7 THR H H 8.24 0.04 1 28 . 7 THR HA H 4.14 0.04 1 29 . 7 THR CA C 59.8 0.3 1 30 . 7 THR CB C 65.1 0.3 1 31 . 7 THR N N 127.8 0.3 1 32 . 8 PRO C C 177.6 0.5 1 33 . 8 PRO CB C 30.8 0.3 1 34 . 9 SER H H 9.28 0.04 1 35 . 9 SER C C 175.8 0.5 1 36 . 9 SER CA C 61.2 0.3 1 37 . 9 SER CB C 62.9 0.3 1 38 . 9 SER N N 115.6 0.3 1 39 . 10 SER H H 7.73 0.04 1 40 . 10 SER HA H 5.33 0.04 1 41 . 10 SER C C 172.0 0.5 1 42 . 10 SER CA C 57.2 0.3 1 43 . 10 SER CB C 64.9 0.3 1 44 . 10 SER N N 115.8 0.3 1 45 . 11 LEU H H 8.86 0.04 1 46 . 11 LEU HA H 4.59 0.04 1 47 . 11 LEU C C 173.8 0.5 1 48 . 11 LEU CA C 54.7 0.3 1 49 . 11 LEU CB C 46.2 0.3 1 50 . 11 LEU N N 124.6 0.3 1 51 . 12 ALA H H 8.42 0.04 1 52 . 12 ALA HA H 5.46 0.04 1 53 . 12 ALA C C 175.1 0.5 1 54 . 12 ALA CA C 50.3 0.3 1 55 . 12 ALA CB C 19.4 0.3 1 56 . 12 ALA N N 127.8 0.3 1 57 . 13 MET H H 8.53 0.04 1 58 . 13 MET HA H 4.99 0.04 1 59 . 13 MET C C 174.5 0.5 1 60 . 13 MET CA C 52.7 0.3 1 61 . 13 MET CB C 35.6 0.3 1 62 . 13 MET N N 121.4 0.3 1 63 . 14 SER H H 8.28 0.04 1 64 . 14 SER HA H 4.97 0.04 1 65 . 14 SER C C 173.3 0.5 1 66 . 14 SER CA C 57.1 0.3 1 67 . 14 SER CB C 64.7 0.3 1 68 . 14 SER N N 116.5 0.3 1 69 . 15 VAL H H 8.24 0.04 1 70 . 15 VAL HA H 3.36 0.04 1 71 . 15 VAL C C 177.8 0.5 1 72 . 15 VAL CA C 64.5 0.3 1 73 . 15 VAL CB C 31.1 0.3 1 74 . 15 VAL N N 120.9 0.3 1 75 . 16 GLY H H 9.50 0.04 1 76 . 16 GLY HA2 H 4.28 0.04 1 77 . 16 GLY HA3 H 4.28 0.04 1 78 . 16 GLY C C 175.2 0.5 1 79 . 16 GLY CA C 44.1 0.3 1 80 . 16 GLY N N 115.8 0.3 1 81 . 17 GLN H H 7.57 0.04 1 82 . 17 GLN HA H 4.30 0.04 1 83 . 17 GLN C C 174.4 0.5 1 84 . 17 GLN CA C 56.0 0.3 1 85 . 17 GLN CB C 30.2 0.3 1 86 . 17 GLN N N 120.2 0.3 1 87 . 18 LYS H H 8.17 0.04 1 88 . 18 LYS HA H 4.61 0.04 1 89 . 18 LYS C C 176.3 0.5 1 90 . 18 LYS CA C 55.4 0.3 1 91 . 18 LYS CB C 32.6 0.3 1 92 . 18 LYS N N 122.8 0.3 1 93 . 19 VAL H H 8.52 0.04 1 94 . 19 VAL HA H 4.29 0.04 1 95 . 19 VAL CA C 60.3 0.3 1 96 . 19 VAL CB C 34.5 0.3 1 97 . 19 VAL N N 127.0 0.3 1 98 . 20 THR H H 8.12 0.04 1 99 . 20 THR HA H 4.84 0.04 1 100 . 20 THR CA C 61.3 0.3 1 101 . 20 THR CB C 70.8 0.3 1 102 . 20 THR N N 120.4 0.3 1 103 . 21 MET H H 8.69 0.04 1 104 . 21 MET HA H 4.71 0.04 1 105 . 21 MET C C 174.0 0.5 1 106 . 21 MET CA C 54.9 0.3 1 107 . 21 MET CB C 34.7 0.3 1 108 . 21 MET N N 125.0 0.3 1 109 . 22 SER H H 8.83 0.04 1 110 . 22 SER HA H 5.56 0.04 1 111 . 22 SER C C 174.8 0.5 1 112 . 22 SER CA C 57.9 0.3 1 113 . 22 SER CB C 64.9 0.3 1 114 . 22 SER N N 115.6 0.3 1 115 . 23 CYS H H 9.35 0.04 1 116 . 23 CYS HA H 5.17 0.04 1 117 . 23 CYS C C 171.3 0.5 1 118 . 23 CYS CA C 56.0 0.3 1 119 . 23 CYS CB C 47.4 0.3 1 120 . 23 CYS N N 128.2 0.3 1 121 . 24 LYS H H 9.00 0.04 1 122 . 24 LYS HA H 5.76 0.04 1 123 . 24 LYS C C 175.7 0.5 1 124 . 24 LYS CA C 53.8 0.3 1 125 . 24 LYS CB C 35.4 0.3 1 126 . 24 LYS N N 128.6 0.3 1 127 . 25 SER H H 9.28 0.04 1 128 . 25 SER HA H 5.57 0.04 1 129 . 25 SER C C 176.2 0.5 1 130 . 25 SER CA C 55.6 0.3 1 131 . 25 SER CB C 66.6 0.3 1 132 . 25 SER N N 119.4 0.3 1 133 . 26 SER H H 8.17 0.04 1 134 . 26 SER HA H 4.90 0.04 1 135 . 26 SER C C 174.3 0.5 1 136 . 26 SER CA C 60.2 0.3 1 137 . 26 SER CB C 62.5 0.3 1 138 . 26 SER N N 116.8 0.3 1 139 . 27 GLN H H 7.30 0.04 1 140 . 27 GLN HA H 4.48 0.04 1 141 . 27 GLN C C 174.5 0.5 1 142 . 27 GLN CA C 53.8 0.3 1 143 . 27 GLN CB C 32.4 0.3 1 144 . 27 GLN N N 117.3 0.3 1 145 . 28 SER H H 8.58 0.04 1 146 . 28 SER C C 176.2 0.5 1 147 . 28 SER CA C 58.1 0.3 1 148 . 28 SER CB C 64.8 0.3 1 149 . 28 SER N N 117.1 0.3 1 150 . 29 LEU H H 8.54 0.04 1 151 . 29 LEU HA H 3.88 0.04 1 152 . 29 LEU C C 175.7 0.5 1 153 . 29 LEU CA C 52.7 0.3 1 154 . 29 LEU CB C 40.8 0.3 1 155 . 29 LEU N N 125.0 0.3 1 156 . 30 LEU H H 7.50 0.04 1 157 . 30 LEU HA H 4.27 0.04 1 158 . 30 LEU C C 175.5 0.5 1 159 . 30 LEU CA C 54.5 0.3 1 160 . 30 LEU CB C 42.1 0.3 1 161 . 30 LEU N N 122.5 0.3 1 162 . 31 ASN H H 9.01 0.04 1 163 . 31 ASN C C 174.8 0.5 1 164 . 31 ASN CA C 51.9 0.3 1 165 . 31 ASN CB C 39.5 0.3 1 166 . 31 ASN N N 129.0 0.3 1 167 . 32 ILE H H 8.56 0.04 1 168 . 32 ILE HA H 4.71 0.04 1 169 . 32 ILE C C 177.4 0.5 1 170 . 32 ILE CA C 63.3 0.3 1 171 . 32 ILE CB C 37.2 0.3 1 172 . 32 ILE N N 124.7 0.3 1 173 . 33 SER H H 8.40 0.04 1 174 . 33 SER HA H 4.71 0.04 1 175 . 33 SER C C 175.5 0.5 1 176 . 33 SER CA C 60.8 0.3 1 177 . 33 SER CB C 62.8 0.3 1 178 . 33 SER N N 116.8 0.3 1 179 . 34 ASN H H 7.32 0.04 1 180 . 34 ASN HA H 4.77 0.04 1 181 . 34 ASN C C 175.1 0.5 1 182 . 34 ASN CA C 51.5 0.3 1 183 . 34 ASN CB C 38.4 0.3 1 184 . 34 ASN N N 116.0 0.3 1 185 . 35 GLN H H 8.46 0.04 1 186 . 35 GLN HA H 3.62 0.04 1 187 . 35 GLN C C 174.5 0.5 1 188 . 35 GLN CA C 57.0 0.3 1 189 . 35 GLN CB C 25.0 0.3 1 190 . 35 GLN N N 114.2 0.3 1 191 . 36 LYS H H 7.96 0.04 1 192 . 36 LYS HA H 4.59 0.04 1 193 . 36 LYS C C 175.4 0.5 1 194 . 36 LYS CA C 54.9 0.3 1 195 . 36 LYS CB C 34.1 0.3 1 196 . 36 LYS N N 117.7 0.3 1 197 . 37 ASN H H 9.16 0.04 1 198 . 37 ASN HA H 5.47 0.04 1 199 . 37 ASN C C 176.1 0.5 1 200 . 37 ASN CA C 52.5 0.3 1 201 . 37 ASN CB C 42.5 0.3 1 202 . 37 ASN N N 121.0 0.3 1 203 . 38 TYR H H 8.63 0.04 1 204 . 38 TYR HA H 4.57 0.04 1 205 . 38 TYR C C 173.2 0.5 1 206 . 38 TYR CA C 57.9 0.3 1 207 . 38 TYR CB C 36.5 0.3 1 208 . 38 TYR N N 127.0 0.3 1 209 . 39 LEU H H 7.04 0.04 1 210 . 39 LEU HA H 4.65 0.04 1 211 . 39 LEU CA C 52.7 0.3 1 212 . 39 LEU CB C 44.3 0.3 1 213 . 39 LEU N N 127.7 0.3 1 214 . 40 ALA H H 8.81 0.04 1 215 . 40 ALA C C 175.8 0.5 1 216 . 40 ALA CA C 49.8 0.3 1 217 . 40 ALA CB C 23.1 0.3 1 218 . 40 ALA N N 128.7 0.3 1 219 . 41 TRP H H 8.70 0.04 1 220 . 41 TRP HA H 5.51 0.04 1 221 . 41 TRP C C 176.1 0.5 1 222 . 41 TRP CA C 56.0 0.3 1 223 . 41 TRP CB C 34.0 0.3 1 224 . 41 TRP N N 116.9 0.3 1 225 . 42 TYR H H 9.94 0.04 1 226 . 42 TYR HA H 5.38 0.04 1 227 . 42 TYR C C 174.1 0.5 1 228 . 42 TYR CA C 56.0 0.3 1 229 . 42 TYR CB C 42.8 0.3 1 230 . 42 TYR N N 118.6 0.3 1 231 . 43 GLN H H 9.03 0.04 1 232 . 43 GLN HA H 4.41 0.04 1 233 . 43 GLN CA C 53.2 0.3 1 234 . 43 GLN CB C 34.0 0.3 1 235 . 43 GLN N N 122.1 0.3 1 236 . 46 PRO C C 178.5 0.5 1 237 . 46 PRO CB C 30.9 0.3 1 238 . 47 GLY H H 8.70 0.04 1 239 . 47 GLY HA2 H 4.71 0.04 1 240 . 47 GLY HA3 H 4.71 0.04 1 241 . 47 GLY C C 174.0 0.5 1 242 . 47 GLY CA C 45.4 0.3 1 243 . 47 GLY N N 113.5 0.3 1 244 . 48 GLN H H 7.85 0.04 1 245 . 48 GLN HA H 4.79 0.04 1 246 . 48 GLN CA C 53.5 0.3 1 247 . 48 GLN CB C 31.2 0.3 1 248 . 48 GLN N N 119.0 0.3 1 249 . 49 SER H H 8.49 0.04 1 250 . 49 SER HA H 4.34 0.04 1 251 . 49 SER CA C 57.2 0.3 1 252 . 49 SER CB C 61.7 0.3 1 253 . 49 SER N N 117.1 0.3 1 254 . 52 LEU C C 175.5 0.5 1 255 . 53 LEU H H 9.25 0.04 1 256 . 53 LEU HA H 4.69 0.04 1 257 . 53 LEU C C 176.4 0.5 1 258 . 53 LEU CA C 54.6 0.3 1 259 . 53 LEU CB C 45.4 0.3 1 260 . 53 LEU N N 124.8 0.3 1 261 . 54 VAL H H 7.26 0.04 1 262 . 54 VAL HA H 5.03 0.04 1 263 . 54 VAL C C 173.2 0.5 1 264 . 54 VAL CA C 59.3 0.3 1 265 . 54 VAL CB C 37.2 0.3 1 266 . 54 VAL N N 117.0 0.3 1 267 . 55 TYR H H 9.53 0.04 1 268 . 55 TYR HA H 5.26 0.04 1 269 . 55 TYR C C 180.5 0.5 1 270 . 55 TYR CA C 54.9 0.3 1 271 . 55 TYR CB C 40.6 0.3 1 272 . 55 TYR N N 124.0 0.3 1 273 . 56 PHE H H 7.67 0.04 1 274 . 56 PHE HA H 5.15 0.04 1 275 . 56 PHE C C 178.8 0.5 1 276 . 56 PHE CA C 59.7 0.3 1 277 . 56 PHE CB C 36.6 0.3 1 278 . 56 PHE N N 116.5 0.3 1 279 . 57 ALA H H 8.75 0.04 1 280 . 57 ALA C C 178.8 0.5 1 281 . 57 ALA CA C 57.5 0.3 1 282 . 57 ALA CB C 20.0 0.3 1 283 . 57 ALA N N 112.6 0.3 1 284 . 58 SER H H 8.75 0.04 1 285 . 58 SER C C 175.3 0.5 1 286 . 58 SER CA C 57.6 0.3 1 287 . 58 SER CB C 65.7 0.3 1 288 . 58 SER N N 112.6 0.3 1 289 . 59 THR H H 8.73 0.04 1 290 . 59 THR HA H 4.21 0.04 1 291 . 59 THR CA C 62.9 0.3 1 292 . 59 THR CB C 68.5 0.3 1 293 . 59 THR N N 123.7 0.3 1 294 . 60 ARG H H 8.81 0.04 1 295 . 60 ARG HA H 4.48 0.04 1 296 . 60 ARG C C 176.8 0.5 1 297 . 60 ARG CA C 57.0 0.3 1 298 . 60 ARG CB C 30.8 0.3 1 299 . 60 ARG N N 128.7 0.3 1 300 . 61 GLU H H 8.05 0.04 1 301 . 61 GLU HA H 4.83 0.04 1 302 . 61 GLU C C 175.8 0.5 1 303 . 61 GLU CA C 55.4 0.3 1 304 . 61 GLU CB C 30.5 0.3 1 305 . 61 GLU N N 126.3 0.3 1 306 . 62 SER H H 9.99 0.04 1 307 . 62 SER C C 175.9 0.5 1 308 . 62 SER CA C 59.9 0.3 1 309 . 62 SER CB C 63.2 0.3 1 310 . 62 SER N N 124.4 0.3 1 311 . 63 GLY H H 8.84 0.04 1 312 . 63 GLY HA2 H 4.71 0.04 1 313 . 63 GLY HA3 H 4.71 0.04 1 314 . 63 GLY C C 174.4 0.5 1 315 . 63 GLY CA C 45.2 0.3 1 316 . 63 GLY N N 113.9 0.3 1 317 . 64 VAL H H 7.50 0.04 1 318 . 64 VAL HA H 4.28 0.04 1 319 . 64 VAL CA C 60.2 0.3 1 320 . 64 VAL CB C 32.4 0.3 1 321 . 64 VAL N N 125.2 0.3 1 322 . 65 PRO CB C 33.1 0.3 1 323 . 66 ASP H H 8.41 0.04 1 324 . 66 ASP HA H 4.08 0.04 1 325 . 66 ASP C C 176.2 0.5 1 326 . 66 ASP CA C 55.7 0.3 1 327 . 66 ASP CB C 39.5 0.3 1 328 . 66 ASP N N 119.5 0.3 1 329 . 67 ARG H H 7.04 0.04 1 330 . 67 ARG HA H 4.22 0.04 1 331 . 67 ARG C C 174.8 0.5 1 332 . 67 ARG CA C 56.0 0.3 1 333 . 67 ARG CB C 28.7 0.3 1 334 . 67 ARG N N 113.6 0.3 1 335 . 68 PHE H H 7.43 0.04 1 336 . 68 PHE HA H 4.66 0.04 1 337 . 68 PHE C C 175.0 0.5 1 338 . 68 PHE CA C 58.2 0.3 1 339 . 68 PHE CB C 38.9 0.3 1 340 . 68 PHE N N 118.4 0.3 1 341 . 69 ILE H H 9.06 0.04 1 342 . 69 ILE HA H 4.20 0.04 1 343 . 69 ILE C C 176.9 0.5 1 344 . 69 ILE CA C 60.4 0.3 1 345 . 69 ILE CB C 41.5 0.3 1 346 . 69 ILE N N 123.3 0.3 1 347 . 70 GLY H H 9.473 0.5 1 348 . 70 GLY HA2 H 5.05 0.04 2 349 . 70 GLY HA3 H 3.70 0.04 2 350 . 70 GLY CA C 44.1 0.3 1 351 . 70 GLY N N 120.0 0.3 1 352 . 71 SER H H 9.37 0.04 1 353 . 71 SER HA H 4.85 0.04 1 354 . 71 SER C C 174.2 0.5 1 355 . 71 SER CA C 57.1 0.3 1 356 . 71 SER CB C 65.7 0.3 1 357 . 71 SER N N 118.3 0.3 1 358 . 72 GLY H H 8.41 0.04 1 359 . 72 GLY HA2 H 5.10 0.04 2 360 . 72 GLY HA3 H 3.65 0.04 2 361 . 72 GLY C C 172.1 0.5 1 362 . 72 GLY CA C 44.3 0.3 1 363 . 72 GLY N N 111.5 0.3 1 364 . 73 SER H H 6.98 0.04 1 365 . 73 SER HA H 4.22 0.04 1 366 . 73 SER C C 174.4 0.5 1 367 . 73 SER CA C 57.1 0.3 1 368 . 73 SER CB C 64.1 0.3 1 369 . 73 SER N N 109.0 0.3 1 370 . 74 GLY H H 8.81 0.04 1 371 . 74 GLY HA2 H 4.14 0.04 1 372 . 74 GLY HA3 H 4.14 0.04 1 373 . 74 GLY C C 172.1 0.5 1 374 . 74 GLY CA C 48.0 0.3 1 375 . 74 GLY N N 113.2 0.3 1 376 . 75 THR H H 8.15 0.04 1 377 . 75 THR HA H 4.20 0.04 1 378 . 75 THR C C 173.9 0.5 1 379 . 75 THR CA C 60.8 0.3 1 380 . 75 THR CB C 70.8 0.3 1 381 . 75 THR N N 116.7 0.3 1 382 . 76 ASP H H 6.79 0.04 1 383 . 76 ASP HA H 5.04 0.04 1 384 . 76 ASP C C 173.4 0.5 1 385 . 76 ASP CA C 54.0 0.3 1 386 . 76 ASP CB C 42.5 0.3 1 387 . 76 ASP N N 122.0 0.3 1 388 . 77 PHE H H 8.52 0.04 1 389 . 77 PHE HA H 5.19 0.04 1 390 . 77 PHE C C 176.2 0.5 1 391 . 77 PHE CA C 57.3 0.3 1 392 . 77 PHE CB C 41.5 0.3 1 393 . 77 PHE N N 122.4 0.3 1 394 . 78 THR H H 8.92 0.04 1 395 . 78 THR HA H 5.50 0.04 1 396 . 78 THR C C 171.9 0.5 1 397 . 78 THR CA C 60.7 0.3 1 398 . 78 THR CB C 72.8 0.3 1 399 . 78 THR N N 117.2 0.3 1 400 . 79 LEU H H 8.27 0.04 1 401 . 79 LEU HA H 4.39 0.04 1 402 . 79 LEU CA C 53.2 0.3 1 403 . 79 LEU CB C 39.7 0.3 1 404 . 79 LEU N N 126.7 0.3 1 405 . 80 THR H H 8.72 0.04 1 406 . 80 THR HA H 5.13 0.04 1 407 . 80 THR CA C 60.2 0.3 1 408 . 80 THR CB C 70.5 0.3 1 409 . 80 THR N N 124.9 0.3 1 410 . 81 ILE H H 8.72 0.04 1 411 . 81 ILE HA H 4.54 0.04 1 412 . 81 ILE C C 177.1 0.5 1 413 . 81 ILE CA C 59.4 0.3 1 414 . 81 ILE CB C 37.4 0.3 1 415 . 81 ILE N N 124.9 0.3 1 416 . 82 SER H H 9.24 0.04 1 417 . 82 SER HA H 3.63 0.04 1 418 . 82 SER C C 174.0 0.5 1 419 . 82 SER CA C 61.1 0.3 1 420 . 82 SER CB C 62.2 0.3 1 421 . 82 SER N N 123.3 0.3 1 422 . 83 SER H H 6.00 0.04 1 423 . 83 SER HA H 3.81 0.04 1 424 . 83 SER C C 174.2 0.5 1 425 . 83 SER CA C 56.3 0.3 1 426 . 83 SER CB C 62.4 0.3 1 427 . 83 SER N N 113.6 0.3 1 428 . 84 VAL H H 8.70 0.04 1 429 . 84 VAL HA H 3.84 0.04 1 430 . 84 VAL C C 174.2 0.5 1 431 . 84 VAL CA C 62.6 0.3 1 432 . 84 VAL CB C 32.2 0.3 1 433 . 84 VAL N N 126.9 0.3 1 434 . 85 GLN H H 8.90 0.04 1 435 . 85 GLN HA H 4.65 0.04 1 436 . 85 GLN C C 176.7 0.5 1 437 . 85 GLN CA C 52.9 0.3 1 438 . 85 GLN CB C 30.9 0.3 1 439 . 85 GLN N N 125.6 0.3 1 440 . 86 ALA H H 9.18 0.04 1 441 . 86 ALA HA H 3.81 0.04 1 442 . 86 ALA C C 180.3 0.5 1 443 . 86 ALA CA C 55.8 0.3 1 444 . 86 ALA CB C 16.9 0.3 1 445 . 86 ALA N N 125.8 0.3 1 446 . 87 GLU H H 8.73 0.04 1 447 . 87 GLU HA H 4.72 0.04 1 448 . 87 GLU C C 175.6 0.5 1 449 . 87 GLU CA C 57.1 0.3 1 450 . 87 GLU CB C 28.1 0.3 1 451 . 87 GLU N N 114.0 0.3 1 452 . 88 ASP H H 8.03 0.04 1 453 . 88 ASP HA H 4.55 0.04 1 454 . 88 ASP C C 177.0 0.5 1 455 . 88 ASP CA C 54.2 0.3 1 456 . 88 ASP CB C 39.7 0.3 1 457 . 88 ASP N N 120.5 0.3 1 458 . 89 GLN H H 7.20 0.04 1 459 . 89 GLN HA H 4.07 0.04 1 460 . 89 GLN C C 174.0 0.5 1 461 . 89 GLN CA C 58.0 0.3 1 462 . 89 GLN CB C 28.1 0.3 1 463 . 89 GLN N N 122.9 0.3 1 464 . 90 ALA H H 8.24 0.04 1 465 . 90 ALA HA H 4.33 0.04 1 466 . 90 ALA C C 174.4 0.5 1 467 . 90 ALA CA C 51.8 0.3 1 468 . 90 ALA CB C 20.0 0.3 1 469 . 90 ALA N N 128.7 0.3 1 470 . 91 ASP H H 7.77 0.04 1 471 . 91 ASP HA H 5.43 0.04 1 472 . 91 ASP C C 175.1 0.5 1 473 . 91 ASP CA C 53.5 0.3 1 474 . 91 ASP CB C 43.2 0.3 1 475 . 91 ASP N N 118.0 0.3 1 476 . 92 TYR H H 8.82 0.04 1 477 . 92 TYR HA H 5.39 0.04 1 478 . 92 TYR C C 176.7 0.5 1 479 . 92 TYR CA C 56.4 0.3 1 480 . 92 TYR CB C 41.9 0.3 1 481 . 92 TYR N N 119.7 0.3 1 482 . 93 PHE H H 9.06 0.04 1 483 . 93 PHE HA H 5.70 0.04 1 484 . 93 PHE C C 175.0 0.5 1 485 . 93 PHE CA C 56.8 0.3 1 486 . 93 PHE CB C 44.0 0.3 1 487 . 93 PHE N N 119.7 0.3 1 488 . 94 CYS H H 7.49 0.04 1 489 . 94 CYS HA H 5.85 0.04 1 490 . 94 CYS C C 172.6 0.5 1 491 . 94 CYS CA C 52.5 0.3 1 492 . 94 CYS CB C 45.0 0.3 1 493 . 94 CYS N N 115.6 0.3 1 494 . 95 GLN H H 8.70 0.04 1 495 . 95 GLN HA H 4.67 0.04 1 496 . 95 GLN C C 173.7 0.5 1 497 . 95 GLN CA C 54.2 0.3 1 498 . 95 GLN CB C 33.6 0.3 1 499 . 95 GLN N N 121.8 0.3 1 500 . 96 GLN H H 8.12 0.04 1 501 . 96 GLN HA H 4.87 0.04 1 502 . 96 GLN C C 173.2 0.5 1 503 . 96 GLN CA C 52.4 0.3 1 504 . 96 GLN CB C 28.4 0.3 1 505 . 96 GLN N N 125.3 0.3 1 506 . 97 HIS H H 7.58 0.04 1 507 . 97 HIS HA H 3.57 0.04 1 508 . 97 HIS C C 173.1 0.5 1 509 . 97 HIS CA C 54.8 0.3 1 510 . 97 HIS CB C 32.6 0.3 1 511 . 97 HIS N N 118.1 0.3 1 512 . 98 TYR H H 8.96 0.04 1 513 . 98 TYR HA H 3.97 0.04 1 514 . 98 TYR C C 175.9 0.5 1 515 . 98 TYR CA C 59.7 0.3 1 516 . 98 TYR CB C 42.0 0.3 1 517 . 98 TYR N N 124.9 0.3 1 518 . 99 ARG H H 8.33 0.04 1 519 . 99 ARG HA H 4.25 0.04 1 520 . 99 ARG C C 173.5 0.5 1 521 . 99 ARG CA C 53.6 0.3 1 522 . 99 ARG CB C 33.5 0.3 1 523 . 99 ARG N N 117.4 0.3 1 524 . 100 ALA H H 8.52 0.04 1 525 . 100 ALA HA H 4.72 0.04 1 526 . 100 ALA CA C 50.1 0.3 1 527 . 100 ALA CB C 17.9 0.3 1 528 . 100 ALA N N 124.1 0.3 1 529 . 102 ARG C C 173.3 0.5 1 530 . 102 ARG CB C 25.6 0.3 1 531 . 103 THR H H 7.29 0.04 1 532 . 103 THR HA H 4.02 0.04 1 533 . 103 THR CA C 61.6 0.3 1 534 . 103 THR CB C 70.8 0.3 1 535 . 103 THR N N 112.5 0.3 1 536 . 104 PHE H H 8.68 0.04 1 537 . 104 PHE HA H 5.11 0.04 1 538 . 104 PHE C C 179.0 0.5 1 539 . 104 PHE CA C 56.6 0.3 1 540 . 104 PHE CB C 42.2 0.3 1 541 . 104 PHE N N 118.2 0.3 1 542 . 105 GLY H H 8.97 0.04 1 543 . 105 GLY HA2 H 4.17 0.04 1 544 . 105 GLY HA3 H 4.17 0.04 1 545 . 105 GLY C C 173.9 0.5 1 546 . 105 GLY CA C 44.4 0.3 1 547 . 105 GLY N N 107.7 0.3 1 548 . 106 GLY H H 8.35 0.04 1 549 . 106 GLY HA2 H 4.34 0.04 1 550 . 106 GLY HA3 H 4.34 0.04 1 551 . 106 GLY C C 175.7 0.5 1 552 . 106 GLY CA C 45.8 0.3 1 553 . 106 GLY N N 104.2 0.3 1 554 . 107 GLY H H 7.37 0.04 1 555 . 107 GLY HA2 H 4.07 0.04 2 556 . 107 GLY HA3 H 3.756 0.04 2 557 . 107 GLY C C 173.2 0.5 1 558 . 107 GLY CA C 45.1 0.3 1 559 . 107 GLY N N 108.5 0.3 1 560 . 108 THR H H 8.27 0.04 1 561 . 108 THR HA H 4.72 0.04 1 562 . 108 THR C C 173.7 0.5 1 563 . 108 THR CA C 62.1 0.3 1 564 . 108 THR CB C 72.7 0.3 1 565 . 108 THR N N 119.0 0.3 1 566 . 109 LYS H H 8.27 0.04 1 567 . 109 LYS HA H 4.74 0.04 1 568 . 109 LYS C C 174.0 0.5 1 569 . 109 LYS CA C 56.2 0.3 1 570 . 109 LYS CB C 32.0 0.3 1 571 . 109 LYS N N 129.8 0.3 1 572 . 110 LEU H H 8.85 0.04 1 573 . 110 LEU HA H 5.14 0.04 1 574 . 110 LEU C C 175.3 0.5 1 575 . 110 LEU CA C 53.8 0.3 1 576 . 110 LEU CB C 43.5 0.3 1 577 . 110 LEU N N 130.6 0.3 1 578 . 111 GLU H H 8.93 0.04 1 579 . 111 GLU HA H 4.57 0.04 1 580 . 111 GLU C C 174.1 0.5 1 581 . 111 GLU CA C 54.6 0.3 1 582 . 111 GLU CB C 32.4 0.3 1 583 . 111 GLU N N 128.1 0.3 1 584 . 112 ILE H H 8.35 0.04 1 585 . 112 ILE HA H 5.03 0.04 1 586 . 112 ILE C C 175.5 0.5 1 587 . 112 ILE CA C 57.6 0.3 1 588 . 112 ILE CB C 36.8 0.3 1 589 . 112 ILE N N 124.2 0.3 1 590 . 113 LYS H H 8.28 0.04 1 591 . 113 LYS HA H 4.20 0.04 1 592 . 113 LYS CA C 56.9 0.3 1 593 . 113 LYS CB C 33.6 0.3 1 594 . 113 LYS N N 133.3 0.3 1 stop_ save_ save_assigned_chemical_shifts_Vh _Saveframe_category assigned_chemical_shifts _Details ; The chemical shifts for 13CA and 13CB have NOT been corrected for the deuterium effect. Sample = "Vh bound" ; loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $conditions_1 _Chem_shift_reference_set_label $chemical_shift_reference_set_1 _Mol_system_component_name Vh _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 GLN C C 177.3 0.5 1 2 . 1 GLN CA C 59.2 0.3 1 3 . 1 GLN CB C 27.2 0.3 1 4 . 2 VAL H H 8.06 0.04 1 5 . 2 VAL HA H 4.13 0.04 1 6 . 2 VAL C C 175.7 0.5 1 7 . 2 VAL CA C 61.8 0.3 1 8 . 2 VAL CB C 32.1 0.3 1 9 . 2 VAL N N 123.9 0.3 1 10 . 3 GLN H H 8.13 0.04 1 11 . 3 GLN HA H 4.33 0.04 1 12 . 3 GLN CA C 55.5 0.3 1 13 . 3 GLN CB C 35.3 0.3 1 14 . 3 GLN N N 126.8 0.3 1 15 . 9 PRO C C 177.4 0.5 1 16 . 9 PRO CA C 63.4 0.3 1 17 . 9 PRO CB C 32.1 0.3 1 18 . 10 GLY H H 8.56 0.04 1 19 . 10 GLY HA2 H 4.1 0.04 1 20 . 10 GLY HA3 H 4.1 0.04 1 21 . 10 GLY C C 172.8 0.5 1 22 . 10 GLY CA C 46.3 0.3 1 23 . 10 GLY N N 112 0.3 1 24 . 11 LEU H H 7.7 0.04 1 25 . 11 LEU HA H 5.16 0.04 1 26 . 11 LEU C C 176.3 0.5 1 27 . 11 LEU CA C 54.3 0.3 1 28 . 11 LEU CB C 43.1 0.3 1 29 . 11 LEU N N 128.7 0.3 1 30 . 12 VAL H H 8.57 0.04 1 31 . 12 VAL HA H 4.24 0.04 1 32 . 12 VAL C C 172.7 0.5 1 33 . 12 VAL CA C 59.9 0.3 1 34 . 12 VAL CB C 34.8 0.3 1 35 . 12 VAL N N 123.9 0.3 1 36 . 13 ALA H H 7.96 0.04 1 37 . 13 ALA HA H 4.92 0.04 1 38 . 13 ALA C C 49.3 0.5 1 39 . 13 ALA CA C 59.9 0.3 1 40 . 13 ALA CB C 17.9 0.3 1 41 . 13 ALA N N 127 0.3 1 42 . 14 PRO C C 176.2 0.5 1 43 . 14 PRO CA C 62.5 0.3 1 44 . 14 PRO CB C 33.8 0.3 1 45 . 15 SER H H 9.18 0.04 1 46 . 15 SER C C 174.4 0.5 1 47 . 15 SER CA C 61 0.3 1 48 . 15 SER CB C 62.5 0.3 1 49 . 15 SER N N 117.2 0.3 1 50 . 16 GLN H H 7.71 0.04 1 51 . 16 GLN HA H 4.45 0.04 1 52 . 16 GLN C C 173.7 0.5 1 53 . 16 GLN CA C 54.9 0.3 1 54 . 16 GLN CB C 28.2 0.3 1 55 . 16 GLN N N 122.5 0.3 1 56 . 17 SER H H 7.96 0.04 1 57 . 17 SER HA H 4.98 0.04 1 58 . 17 SER C C 172.7 0.5 1 59 . 17 SER CA C 57.4 0.3 1 60 . 17 SER CB C 65.1 0.3 1 61 . 17 SER N N 112.7 0.3 1 62 . 18 LEU H H 8.91 0.04 1 63 . 18 LEU HA H 4.45 0.04 1 64 . 18 LEU C C 174.9 0.5 1 65 . 18 LEU CA C 53.1 0.3 1 66 . 18 LEU CB C 45.4 0.3 1 67 . 18 LEU N N 122.7 0.3 1 68 . 19 SER H H 8.02 0.04 1 69 . 19 SER HA H 5.25 0.04 1 70 . 19 SER C C 173.4 0.5 1 71 . 19 SER CA C 56.8 0.3 1 72 . 19 SER CB C 64.3 0.3 1 73 . 19 SER N N 121.4 0.3 1 74 . 20 ILE H H 8.98 0.04 1 75 . 20 ILE HA H 4.79 0.04 1 76 . 20 ILE C C 176.3 0.5 1 77 . 20 ILE CA C 59.2 0.3 1 78 . 20 ILE CB C 40.2 0.3 1 79 . 20 ILE N N 125.3 0.3 1 80 . 21 THR H H 8.54 0.04 1 81 . 21 THR HA H 4.98 0.04 1 82 . 21 THR C C 173 0.5 1 83 . 21 THR CA C 61.3 0.3 1 84 . 21 THR CB C 70.6 0.3 1 85 . 21 THR N N 121.7 0.3 1 86 . 22 CYS H H 9.83 0.04 1 87 . 22 CYS HA H 5 0.04 1 88 . 22 CYS C C 173.4 0.5 1 89 . 22 CYS CA C 54.6 0.3 1 90 . 22 CYS CB C 43.7 0.3 1 91 . 22 CYS N N 128.4 0.3 1 92 . 23 THR H H 9.03 0.04 1 93 . 23 THR HA H 4.65 0.04 1 94 . 23 THR C C 174.4 0.5 1 95 . 23 THR CA C 63 0.3 1 96 . 23 THR CB C 68.7 0.3 1 97 . 23 THR N N 126.9 0.3 1 98 . 24 VAL H H 8.61 0.04 1 99 . 24 VAL HA H 4.7 0.04 1 100 . 24 VAL C C 174.9 0.5 1 101 . 24 VAL CA C 60.4 0.3 1 102 . 24 VAL CB C 32.6 0.3 1 103 . 24 VAL N N 128.3 0.3 1 104 . 25 SER H H 8.79 0.04 1 105 . 25 SER HA H 4.75 0.04 1 106 . 25 SER C C 174.4 0.5 1 107 . 25 SER CA C 56.7 0.3 1 108 . 25 SER CB C 64.7 0.3 1 109 . 25 SER N N 121 0.3 1 110 . 26 GLY H H 8.63 0.04 1 111 . 26 GLY HA2 H 4.7 0.04 1 112 . 26 GLY HA3 H 4.7 0.04 1 113 . 26 GLY C C 173 0.5 1 114 . 26 GLY CA C 45.5 0.3 1 115 . 26 GLY N N 111.1 0.3 1 116 . 27 ILE H H 6.66 0.04 1 117 . 27 ILE HA H 4.25 0.04 1 118 . 27 ILE C C 174.3 0.5 1 119 . 27 ILE CA C 58.8 0.3 1 120 . 27 ILE CB C 41.1 0.3 1 121 . 27 ILE N N 111.2 0.3 1 122 . 28 SER H H 8.26 0.04 1 123 . 28 SER HA H 4.51 0.04 1 124 . 28 SER C C 176.8 0.5 1 125 . 28 SER CA C 56.3 0.3 1 126 . 28 SER CB C 63.4 0.3 1 127 . 28 SER N N 115.5 0.3 1 128 . 29 LEU H H 8.97 0.04 1 129 . 29 LEU HA H 4.7 0.04 1 130 . 29 LEU C C 176.2 0.5 1 131 . 29 LEU CA C 56 0.3 1 132 . 29 LEU CB C 40.5 0.3 1 133 . 29 LEU N N 129 0.3 1 134 . 30 SER H H 7.97 0.04 1 135 . 30 SER HA H 4.44 0.04 1 136 . 30 SER C C 175.2 0.5 1 137 . 30 SER CA C 59.7 0.3 1 138 . 30 SER CB C 62.9 0.3 1 139 . 30 SER N N 111.5 0.3 1 140 . 31 ARG H H 7.39 0.04 1 141 . 31 ARG HA H 4.69 0.04 1 142 . 31 ARG C C 175.5 0.5 1 143 . 31 ARG CA C 55.8 0.3 1 144 . 31 ARG CB C 31.5 0.3 1 145 . 31 ARG N N 119.1 0.3 1 146 . 32 TYR H H 7.63 0.04 1 147 . 32 TYR HA H 4.54 0.04 1 148 . 32 TYR C C 173.6 0.5 1 149 . 32 TYR CA C 57.8 0.3 1 150 . 32 TYR CB C 39.9 0.3 1 151 . 32 TYR N N 119.6 0.3 1 152 . 33 ASN H H 8.64 0.04 1 153 . 33 ASN HA H 4.84 0.04 1 154 . 33 ASN CA C 51.4 0.3 1 155 . 33 ASN CB C 39.7 0.3 1 156 . 33 ASN N N 118.6 0.3 1 157 . 34 VAL H H 8.3 0.04 1 158 . 34 VAL HA H 4.89 0.04 1 159 . 34 VAL CA C 61.6 0.3 1 160 . 34 VAL CB C 33 0.3 1 161 . 34 VAL N N 123 0.3 1 162 . 36 TRP C C 174.9 0.5 1 163 . 36 TRP CB C 32.9 0.3 1 164 . 37 VAL H H 9.31 0.04 1 165 . 37 VAL HA H 4.92 0.04 1 166 . 37 VAL C C 173.4 0.5 1 167 . 37 VAL CA C 59.6 0.3 1 168 . 37 VAL CB C 36.6 0.3 1 169 . 37 VAL N N 123.9 0.3 1 170 . 38 ARG H H 9.23 0.04 1 171 . 38 ARG HA H 5.81 0.04 1 172 . 38 ARG C C 173.3 0.5 1 173 . 38 ARG CA C 52.8 0.3 1 174 . 38 ARG CB C 32.2 0.3 1 175 . 38 ARG N N 120.8 0.3 1 176 . 39 GLN H H 9.14 0.04 1 177 . 39 GLN HA H 5.11 0.04 1 178 . 39 GLN C C 174.6 0.5 1 179 . 39 GLN CA C 54.1 0.3 1 180 . 39 GLN CB C 32.6 0.3 1 181 . 39 GLN N N 121.7 0.3 1 182 . 40 SER H H 8.45 0.04 1 183 . 40 SER HA H 4.98 0.04 1 184 . 40 SER CA C 55.7 0.3 1 185 . 40 SER CB C 64.6 0.3 1 186 . 40 SER N N 124 0.3 1 187 . 41 PRO C C 178.9 0.5 1 188 . 41 PRO CA C 64.5 0.3 1 189 . 41 PRO CB C 31.2 0.3 1 190 . 42 GLY H H 8.61 0.04 1 191 . 42 GLY HA2 H 4.7 0.04 1 192 . 42 GLY HA3 H 4.7 0.04 1 193 . 42 GLY C C 175.2 0.5 1 194 . 42 GLY CA C 45.7 0.3 1 195 . 42 GLY N N 107.3 0.3 1 196 . 43 LYS H H 7.42 0.04 1 197 . 43 LYS HA H 4.45 0.04 1 198 . 43 LYS C C 177 0.5 1 199 . 43 LYS CA C 55.5 0.3 1 200 . 43 LYS CB C 33.3 0.3 1 201 . 43 LYS N N 118.9 0.3 1 202 . 44 GLY H H 8.08 0.04 1 203 . 44 GLY HA2 H 4.04 0.04 2 204 . 44 GLY HA3 H 3.85 0.04 2 205 . 44 GLY C C 174.3 0.5 1 206 . 44 GLY CA C 45.3 0.3 1 207 . 44 GLY N N 109.8 0.3 1 208 . 45 LEU H H 7.92 0.04 1 209 . 45 LEU HA H 4.47 0.04 1 210 . 45 LEU C C 176.1 0.5 1 211 . 45 LEU CA C 54.8 0.3 1 212 . 45 LEU CB C 41 0.3 1 213 . 45 LEU N N 125.6 0.3 1 214 . 46 GLU H H 9.16 0.04 1 215 . 46 GLU HA H 4.7 0.04 1 216 . 46 GLU C C 173.9 0.5 1 217 . 46 GLU CA C 54.7 0.3 1 218 . 46 GLU CB C 34.3 0.3 1 219 . 46 GLU N N 123.4 0.3 1 220 . 47 TRP H H 10.09 0.04 1 221 . 47 TRP C C 175.6 0.5 1 222 . 47 TRP CA C 58.9 0.3 1 223 . 47 TRP CB C 30.3 0.3 1 224 . 47 TRP N N 129.4 0.3 1 225 . 48 LEU H H 8.93 0.04 1 226 . 48 LEU HA H 4.32 0.04 1 227 . 48 LEU C C 175.3 0.5 1 228 . 48 LEU CA C 56.3 0.3 1 229 . 48 LEU CB C 41.2 0.3 1 230 . 48 LEU N N 127.6 0.3 1 231 . 49 GLY H H 6.16 0.04 1 232 . 49 GLY HA2 H 3.68 0.04 1 233 . 49 GLY HA3 H 3.68 0.04 1 234 . 49 GLY C C 170 0.5 1 235 . 49 GLY CA C 44.6 0.3 1 236 . 49 GLY N N 102.7 0.3 1 237 . 50 MET H H 8.74 0.04 1 238 . 50 MET HA H 5.24 0.04 1 239 . 50 MET C C 171.7 0.5 1 240 . 50 MET CA C 54.1 0.3 1 241 . 50 MET CB C 35 0.3 1 242 . 50 MET N N 113.6 0.3 1 243 . 51 ILE H H 9.26 0.04 1 244 . 51 ILE HA H 5.17 0.04 1 245 . 51 ILE C C 175.5 0.5 1 246 . 51 ILE CA C 58.6 0.3 1 247 . 51 ILE CB C 41.2 0.3 1 248 . 51 ILE N N 118.6 0.3 1 249 . 52 TRP H H 9.55 0.04 1 250 . 52 TRP C C 179 0.5 1 251 . 52 TRP CA C 57.6 0.3 1 252 . 52 TRP CB C 30 0.3 1 253 . 52 TRP N N 131.5 0.3 1 254 . 53 GLY H H 9.06 0.04 1 255 . 53 GLY C C 177.4 0.5 1 256 . 53 GLY CA C 47.5 0.3 1 257 . 53 GLY N N 112.4 0.3 1 258 . 54 GLY H H 8.79 0.04 1 259 . 54 GLY C C 175.4 0.5 1 260 . 54 GLY CA C 45.9 0.3 1 261 . 54 GLY N N 108 0.3 1 262 . 55 GLY H H 8.14 0.04 1 263 . 55 GLY HA2 H 4.68 0.04 1 264 . 55 GLY HA3 H 4.68 0.04 1 265 . 55 GLY CA C 44.8 0.3 1 266 . 55 GLY N N 107.5 0.3 1 267 . 56 SER H H 7.96 0.04 1 268 . 56 SER C C 172.9 0.5 1 269 . 56 SER CA C 59.9 0.3 1 270 . 56 SER CB C 62.6 0.3 1 271 . 56 SER N N 117.7 0.3 1 272 . 57 ILE H H 8.46 0.04 1 273 . 57 ILE CA C 60.5 0.3 1 274 . 57 ILE CB C 41.5 0.3 1 275 . 57 ILE N N 124.7 0.3 1 276 . 58 GLU H H 8.46 0.04 1 277 . 58 GLU C C 174.1 0.5 1 278 . 58 GLU CA C 54.9 0.3 1 279 . 58 GLU CB C 34.3 0.3 1 280 . 58 GLU N N 124.7 0.3 1 281 . 59 TYR H H 8.69 0.04 1 282 . 59 TYR HA H 4.84 0.04 1 283 . 59 TYR C C 176.4 0.5 1 284 . 59 TYR CA C 56.5 0.3 1 285 . 59 TYR CB C 42.1 0.3 1 286 . 59 TYR N N 118.2 0.3 1 287 . 60 ASN H H 8.26 0.04 1 288 . 60 ASN HA H 4.69 0.04 1 289 . 60 ASN CA C 51.7 0.3 1 290 . 60 ASN CB C 38.3 0.3 1 291 . 60 ASN N N 121.9 0.3 1 292 . 61 PRO C C 178 0.5 1 293 . 61 PRO CB C 31.7 0.3 1 294 . 62 ALA H H 8.11 0.04 1 295 . 62 ALA HA H 4.26 0.04 1 296 . 62 ALA C C 178.6 0.5 1 297 . 62 ALA CA C 53.8 0.3 1 298 . 62 ALA CB C 18 0.3 1 299 . 62 ALA N N 118.9 0.3 1 300 . 63 LEU H H 7.45 0.04 1 301 . 63 LEU HA H 4.56 0.04 1 302 . 63 LEU C C 176.8 0.5 1 303 . 63 LEU CA C 53.8 0.3 1 304 . 63 LEU CB C 44 0.3 1 305 . 63 LEU N N 116.4 0.3 1 306 . 64 LYS H H 7.22 0.04 1 307 . 64 LYS HA H 3.47 0.04 1 308 . 64 LYS C C 176.4 0.5 1 309 . 64 LYS CA C 59.8 0.3 1 310 . 64 LYS CB C 32.2 0.3 1 311 . 64 LYS N N 120.7 0.3 1 312 . 65 SER H H 8.48 0.04 1 313 . 65 SER C C 175.1 0.5 1 314 . 65 SER CA C 60.3 0.3 1 315 . 65 SER CB C 62.6 0.3 1 316 . 65 SER N N 112.7 0.3 1 317 . 66 ARG H H 7.91 0.04 1 318 . 66 ARG HA H 4.6 0.04 1 319 . 66 ARG C C 174.4 0.5 1 320 . 66 ARG CA C 55.3 0.3 1 321 . 66 ARG CB C 31.1 0.3 1 322 . 66 ARG N N 118.5 0.3 1 323 . 67 LEU H H 7.02 0.04 1 324 . 67 LEU HA H 5.13 0.04 1 325 . 67 LEU C C 175.6 0.5 1 326 . 67 LEU CA C 53.7 0.3 1 327 . 67 LEU CB C 47.1 0.3 1 328 . 67 LEU N N 120.7 0.3 1 329 . 68 SER H H 8.48 0.04 1 330 . 68 SER HA H 4.92 0.04 1 331 . 68 SER C C 173.7 0.5 1 332 . 68 SER CA C 57.5 0.3 1 333 . 68 SER CB C 65.1 0.3 1 334 . 68 SER N N 114 0.3 1 335 . 69 ILE H H 8.43 0.04 1 336 . 69 ILE HA H 5.08 0.04 1 337 . 69 ILE C C 173.5 0.5 1 338 . 69 ILE CA C 59.7 0.3 1 339 . 69 ILE CB C 40.8 0.3 1 340 . 69 ILE N N 128.9 0.3 1 341 . 70 SER H H 8.44 0.04 1 342 . 70 SER HA H 4.67 0.04 1 343 . 70 SER C C 172.5 0.5 1 344 . 70 SER CA C 57.3 0.3 1 345 . 70 SER CB C 65.7 0.3 1 346 . 70 SER N N 117.6 0.3 1 347 . 71 LYS H H 9.1 0.04 1 348 . 71 LYS HA H 5.18 0.04 1 349 . 71 LYS C C 173.7 0.5 1 350 . 71 LYS CA C 55.3 0.3 1 351 . 71 LYS CB C 36.8 0.3 1 352 . 71 LYS N N 116.7 0.3 1 353 . 72 ASP H H 8.83 0.04 1 354 . 72 ASP HA H 4.97 0.04 1 355 . 72 ASP C C 176.4 0.5 1 356 . 72 ASP CA C 52.6 0.3 1 357 . 72 ASP CB C 42.5 0.3 1 358 . 72 ASP N N 120.8 0.3 1 359 . 73 ASN H H 9.35 0.04 1 360 . 73 ASN C C 178.3 0.5 1 361 . 73 ASN CA C 56.5 0.3 1 362 . 73 ASN CB C 38.1 0.3 1 363 . 73 ASN N N 124.9 0.3 1 364 . 74 SER H H 8.58 0.04 1 365 . 74 SER C C 175.9 0.5 1 366 . 74 SER CA C 61.2 0.3 1 367 . 74 SER CB C 65.4 0.3 1 368 . 74 SER N N 117.1 0.3 1 369 . 75 LYS H H 7.49 0.04 1 370 . 75 LYS HA H 4.35 0.04 1 371 . 75 LYS C C 175.5 0.5 1 372 . 75 LYS CA C 43.1 0.3 1 373 . 75 LYS CB C 33 0.3 1 374 . 75 LYS N N 120.9 0.3 1 375 . 76 SER H H 7.85 0.04 1 376 . 76 SER HA H 4.72 0.04 1 377 . 76 SER C C 172.5 0.5 1 378 . 76 SER CA C 58.9 0.3 1 379 . 76 SER CB C 62.1 0.3 1 380 . 76 SER N N 114.8 0.3 1 381 . 77 GLN H H 7.25 0.04 1 382 . 77 GLN HA H 5.28 0.04 1 383 . 77 GLN C C 173.7 0.5 1 384 . 77 GLN CA C 53 0.3 1 385 . 77 GLN CB C 34.1 0.3 1 386 . 77 GLN N N 114.6 0.3 1 387 . 78 ILE H H 8.6 0.04 1 388 . 78 ILE HA H 4.43 0.04 1 389 . 78 ILE C C 173.5 0.5 1 390 . 78 ILE CA C 59.3 0.3 1 391 . 78 ILE CB C 40 0.3 1 392 . 78 ILE N N 120.3 0.3 1 393 . 79 PHE H H 9.37 0.04 1 394 . 79 PHE HA H 5.51 0.04 1 395 . 79 PHE CA C 56.5 0.3 1 396 . 79 PHE CB C 40.6 0.3 1 397 . 79 PHE N N 126.4 0.3 1 398 . 80 LEU H H 8.46 0.04 1 399 . 80 LEU C C 174.4 0.5 1 400 . 80 LEU CA C 53.7 0.3 1 401 . 80 LEU CB C 41.5 0.3 1 402 . 80 LEU N N 124.6 0.3 1 403 . 81 LYS H H 8.8 0.04 1 404 . 81 LYS HA H 5.34 0.04 1 405 . 81 LYS C C 172.7 0.5 1 406 . 81 LYS CA C 54 0.3 1 407 . 81 LYS CB C 34.4 0.3 1 408 . 81 LYS N N 127.6 0.3 1 409 . 82 MET H H 8.76 0.04 1 410 . 82 MET HA H 5.32 0.04 1 411 . 82 MET C C 174.2 0.5 1 412 . 82 MET CA C 53.7 0.3 1 413 . 82 MET CB C 37.2 0.3 1 414 . 82 MET N N 124.7 0.3 1 415 . 83 ASN H H 8.58 0.04 1 416 . 83 ASN HA H 4.86 0.04 1 417 . 83 ASN C C 174 0.5 1 418 . 83 ASN CA C 51.6 0.3 1 419 . 83 ASN CB C 40.6 0.3 1 420 . 83 ASN N N 123.2 0.3 1 421 . 84 SER H H 8.57 0.04 1 422 . 84 SER HA H 3.6 0.04 1 423 . 84 SER C C 174.1 0.5 1 424 . 84 SER CA C 57.3 0.3 1 425 . 84 SER CB C 61.2 0.3 1 426 . 84 SER N N 113.5 0.3 1 427 . 85 LEU H H 8.13 0.04 1 428 . 85 LEU HA H 3.95 0.04 1 429 . 85 LEU C C 177.3 0.5 1 430 . 85 LEU CA C 55.8 0.3 1 431 . 85 LEU CB C 41.8 0.3 1 432 . 85 LEU N N 119.3 0.3 1 433 . 86 GLN H H 9.4 0.04 1 434 . 86 GLN HA H 4.75 0.04 1 435 . 86 GLN C C 177.6 0.5 1 436 . 86 GLN CA C 52.5 0.3 1 437 . 86 GLN CB C 31.3 0.3 1 438 . 86 GLN N N 119.9 0.3 1 439 . 87 THR H H 8.98 0.04 1 440 . 87 THR HA H 4.72 0.04 1 441 . 87 THR C C 176.9 0.5 1 442 . 87 THR CA C 66.3 0.3 1 443 . 87 THR CB C 68.1 0.3 1 444 . 87 THR N N 116.5 0.3 1 445 . 88 ASP H H 8.27 0.04 1 446 . 88 ASP HA H 4.68 0.04 1 447 . 88 ASP C C 175.9 0.5 1 448 . 88 ASP CA C 54.9 0.3 1 449 . 88 ASP CB C 39.2 0.3 1 450 . 88 ASP N N 118.5 0.3 1 451 . 89 ASP H H 8.25 0.04 1 452 . 89 ASP HA H 4.73 0.04 1 453 . 89 ASP C C 176.8 0.5 1 454 . 89 ASP CA C 55 0.3 1 455 . 89 ASP CB C 41.4 0.3 1 456 . 89 ASP N N 116.8 0.3 1 457 . 90 SER H H 7.75 0.04 1 458 . 90 SER HA H 4.56 0.04 1 459 . 90 SER C C 173.4 0.5 1 460 . 90 SER CA C 60.3 0.3 1 461 . 90 SER CB C 63.4 0.3 1 462 . 90 SER N N 119.6 0.3 1 463 . 91 ALA H H 8.99 0.04 1 464 . 91 ALA HA H 4.35 0.04 1 465 . 91 ALA C C 175 0.5 1 466 . 91 ALA CA C 51.9 0.3 1 467 . 91 ALA CB C 20.6 0.3 1 468 . 91 ALA N N 127.2 0.3 1 469 . 92 MET H H 8.26 0.04 1 470 . 92 MET HA H 4.94 0.04 1 471 . 92 MET CA C 54 0.3 1 472 . 92 MET CB C 32.6 0.3 1 473 . 92 MET N N 119.9 0.3 1 474 . 93 TYR H H 9.11 0.04 1 475 . 93 TYR CB C 41.7 0.3 1 476 . 93 TYR N N 127.3 0.3 1 477 . 96 VAL C C 174.2 0.5 1 478 . 96 VAL CB C 34.5 0.3 1 479 . 97 SER H H 8.93 0.04 1 480 . 97 SER HA H 5.63 0.04 1 481 . 97 SER C C 172.8 0.5 1 482 . 97 SER CA C 55.9 0.3 1 483 . 97 SER CB C 67.6 0.3 1 484 . 97 SER N N 121.4 0.3 1 485 . 98 TYR H H 8.27 0.04 1 486 . 98 TYR CA C 54.9 0.3 1 487 . 98 TYR CB C 39.1 0.3 1 488 . 98 TYR N N 118.4 0.3 1 489 . 100 TYR C C 176.1 0.5 1 490 . 100 TYR CB C 39.9 0.3 1 491 . 101 GLY H H 8.67 0.04 1 492 . 101 GLY HA2 H 4.72 0.04 1 493 . 101 GLY HA3 H 4.72 0.04 1 494 . 101 GLY C C 175.2 0.5 1 495 . 101 GLY CA C 45.4 0.3 1 496 . 101 GLY N N 109.7 0.3 1 497 . 102 GLY H H 8.52 0.04 1 498 . 102 GLY HA2 H 4.67 0.04 1 499 . 102 GLY HA3 H 4.67 0.04 1 500 . 102 GLY CA C 43.5 0.3 1 501 . 102 GLY N N 111.1 0.3 1 502 . 103 ASP H H 8.42 0.04 1 503 . 103 ASP HA H 4.72 0.04 1 504 . 103 ASP C C 175.8 0.5 1 505 . 103 ASP CA C 55.7 0.3 1 506 . 103 ASP CB C 40.5 0.3 1 507 . 103 ASP N N 119.3 0.3 1 508 . 104 ARG H H 7.66 0.04 1 509 . 104 ARG HA H 4.51 0.04 1 510 . 104 ARG CA C 53.6 0.3 1 511 . 104 ARG CB C 31.8 0.3 1 512 . 104 ARG N N 118.8 0.3 1 513 . 105 PHE H H 10.55 0.04 1 514 . 105 PHE CB C 39.5 0.3 1 515 . 105 PHE N N 127.5 0.3 1 516 . 112 THR H H 8.57 0.04 1 517 . 112 THR HA H 4.68 0.04 1 518 . 112 THR C C 171.6 0.5 1 519 . 112 THR CA C 59.9 0.3 1 520 . 112 THR CB C 20.6 0.3 1 521 . 112 THR N N 118.6 0.3 1 522 . 113 LEU H H 8.54 0.04 1 523 . 113 LEU HA H 4.66 0.04 1 524 . 113 LEU C C 177.3 0.5 1 525 . 113 LEU CA C 55.5 0.3 1 526 . 113 LEU CB C 41.7 0.3 1 527 . 113 LEU N N 134.1 0.3 1 528 . 114 VAL H H 9.15 0.04 1 529 . 114 VAL HA H 4.55 0.04 1 530 . 114 VAL C C 175.1 0.5 1 531 . 114 VAL CA C 61.4 0.3 1 532 . 114 VAL CB C 33.1 0.3 1 533 . 114 VAL N N 132.5 0.3 1 534 . 115 THR H H 8.35 0.04 1 535 . 115 THR HA H 4.3 0.04 1 536 . 115 THR C C 174.7 0.5 1 537 . 115 THR CA C 61.7 0.3 1 538 . 115 THR CB C 70 0.3 1 539 . 115 THR N N 125.8 0.3 1 540 . 116 VAL H H 9.7 0.04 1 541 . 116 VAL HA H 5.51 0.04 1 542 . 116 VAL C C 175.4 0.5 1 543 . 116 VAL CA C 55.1 0.3 1 544 . 116 VAL CB C 31.9 0.3 1 545 . 116 VAL N N 130.5 0.3 1 546 . 117 SER H H 8.46 0.04 1 547 . 117 SER HA H 4.47 0.04 1 548 . 117 SER CA C 58.5 0.3 1 549 . 117 SER CB C 71.5 0.3 1 550 . 117 SER N N 116.8 0.3 1 stop_ save_