data_4327 ####################### # Entry information # ####################### save_entry_information _Entry.Sf_category entry_information _Entry.Sf_framecode entry_information _Entry.ID 4327 _Entry.Title ; 1H, 13C, and 15N Resonance Assignment and Secondary Structure of the N-terminal Inhibitory Domain of Human Tissue Inhibitor of Metalloproteinases-1 ; _Entry.Type . _Entry.Version_type original _Entry.Submission_date 1999-03-25 _Entry.Accession_date 1999-03-29 _Entry.Last_release_date 1999-10-26 _Entry.Original_release_date 1999-10-26 _Entry.Origination author _Entry.NMR_STAR_version 3.1.1.61 _Entry.Original_NMR_STAR_version 2.1 _Entry.Experimental_method NMR _Entry.Experimental_method_subtype . _Entry.Details . _Entry.BMRB_internal_directory_name . loop_ _Entry_author.Ordinal _Entry_author.Given_name _Entry_author.Family_name _Entry_author.First_initial _Entry_author.Middle_initials _Entry_author.Family_title _Entry_author.Entry_ID 1 Bin Wu . . . 4327 2 S. Arumugam . . . 4327 3 Wen Huang . . . 4327 4 Keith Brew . . . 4327 5 Steven 'Van Doren' . R . 4327 stop_ loop_ _Data_set.Type _Data_set.Count _Data_set.Entry_ID assigned_chemical_shifts 1 4327 stop_ loop_ _Datum.Type _Datum.Count _Datum.Entry_ID '13C chemical shifts' 539 4327 '15N chemical shifts' 122 4327 '1H chemical shifts' 845 4327 stop_ loop_ _Release.Release_number _Release.Format_type _Release.Format_version _Release.Date _Release.Submission_date _Release.Type _Release.Author _Release.Detail _Release.Entry_ID 1 . . 1999-10-26 1999-03-25 original author . 4327 stop_ save_ ############### # Citations # ############### save_entry_citation _Citation.Sf_category citations _Citation.Sf_framecode entry_citation _Citation.Entry_ID 4327 _Citation.ID 1 _Citation.Class 'entry citation' _Citation.CAS_abstract_code . _Citation.MEDLINE_UI_code 99410895 _Citation.DOI . _Citation.PubMed_ID . _Citation.Full_citation ; Wu, B., Arumugam, S., Huang, W., Brew, K., and Van Doren, S.R., "1H, 13C and 15N Resonance Assignment and Secondary Structure of the N-terminal Inhibitory Domain of Human Tissue Inhibitor of Metalloproteinases-1," J. Biomol. NMR 14, 289-290 (1999). ; _Citation.Title ; 1H, 13C and 15N Resonance Assignment and Secondary Structure of the N-terminal Inhibitory Domain of Human Tissue Inhibitor of Metalloproteinases-1 ; _Citation.Status published _Citation.Type journal _Citation.Journal_abbrev 'J. Biomol. NMR' _Citation.Journal_name_full 'Journal of Biomolecular NMR' _Citation.Journal_volume 14 _Citation.Journal_issue . _Citation.Journal_ASTM . _Citation.Journal_ISSN . _Citation.Journal_CSD . _Citation.Book_title . _Citation.Book_chapter_title . _Citation.Book_volume . _Citation.Book_series . _Citation.Book_publisher . _Citation.Book_publisher_city . _Citation.Book_ISBN . _Citation.Conference_title . _Citation.Conference_site . _Citation.Conference_state_province . _Citation.Conference_country . _Citation.Conference_start_date . _Citation.Conference_end_date . _Citation.Conference_abstract_number . _Citation.Thesis_institution . _Citation.Thesis_institution_city . _Citation.Thesis_institution_country . _Citation.WWW_URL . _Citation.Page_first 289 _Citation.Page_last 290 _Citation.Year 1999 _Citation.Details . loop_ _Citation_author.Ordinal _Citation_author.Given_name _Citation_author.Family_name _Citation_author.First_initial _Citation_author.Middle_initials _Citation_author.Family_title _Citation_author.Entry_ID _Citation_author.Citation_ID 1 Bin Wu . . . 4327 1 2 S. Arumugam . . . 4327 1 3 Wen Huang . . . 4327 1 4 Keith Brew . . . 4327 1 5 Steven 'Van Doren' . R . 4327 1 stop_ loop_ _Citation_keyword.Keyword _Citation_keyword.Entry_ID _Citation_keyword.Citation_ID 'NMR assignments' 4327 1 'secondary structure' 4327 1 TIMP-1 4327 1 'tissue inhibitor of matrix metalloproteinases' 4327 1 stop_ save_ ############################################# # Molecular system (assembly) description # ############################################# save_system_N-TIMP-1 _Assembly.Sf_category assembly _Assembly.Sf_framecode system_N-TIMP-1 _Assembly.Entry_ID 4327 _Assembly.ID 1 _Assembly.Name 'N-terminal inhibitory domain of human tissue inhibitor of metalloproteinases-1' _Assembly.BMRB_code . _Assembly.Number_of_components . _Assembly.Organic_ligands . _Assembly.Metal_ions . _Assembly.Non_standard_bonds . _Assembly.Ambiguous_conformational_states . _Assembly.Ambiguous_chem_comp_sites . _Assembly.Molecules_in_chemical_exchange . _Assembly.Paramagnetic no _Assembly.Thiol_state 'fully oxidized' _Assembly.Molecular_mass . _Assembly.Enzyme_commission_number . _Assembly.Details . _Assembly.DB_query_date . _Assembly.DB_query_revised_last_date . loop_ _Assembly_type.Type _Assembly_type.Entry_ID _Assembly_type.Assembly_ID monomer 4327 1 stop_ loop_ _Entity_assembly.ID _Entity_assembly.Entity_assembly_name _Entity_assembly.Entity_ID _Entity_assembly.Entity_label _Entity_assembly.Asym_ID _Entity_assembly.PDB_chain_ID _Entity_assembly.Experimental_data_reported _Entity_assembly.Physical_state _Entity_assembly.Conformational_isomer _Entity_assembly.Chemical_exchange_state _Entity_assembly.Magnetic_equivalence_group_code _Entity_assembly.Role _Entity_assembly.Details _Entity_assembly.Entry_ID _Entity_assembly.Assembly_ID 1 N-TIMP-1 1 $N-TIMP-1 . . . native . . . . . 4327 1 stop_ loop_ _Bond.ID _Bond.Type _Bond.Value_order _Bond.Assembly_atom_ID_1 _Bond.Entity_assembly_ID_1 _Bond.Entity_assembly_name_1 _Bond.Entity_ID_1 _Bond.Comp_ID_1 _Bond.Comp_index_ID_1 _Bond.Seq_ID_1 _Bond.Atom_ID_1 _Bond.Assembly_atom_ID_2 _Bond.Entity_assembly_ID_2 _Bond.Entity_assembly_name_2 _Bond.Entity_ID_2 _Bond.Comp_ID_2 _Bond.Comp_index_ID_2 _Bond.Seq_ID_2 _Bond.Atom_ID_2 _Bond.Auth_entity_assembly_ID_1 _Bond.Auth_entity_assembly_name_1 _Bond.Auth_seq_ID_1 _Bond.Auth_comp_ID_1 _Bond.Auth_atom_ID_1 _Bond.Auth_entity_assembly_ID_2 _Bond.Auth_entity_assembly_name_2 _Bond.Auth_seq_ID_2 _Bond.Auth_comp_ID_2 _Bond.Auth_atom_ID_2 _Bond.Entry_ID _Bond.Assembly_ID 1 disulfide single . 1 . 1 CYS 1 1 SG . 1 . 1 CYS 70 70 SG . . . . . . . . . . 4327 1 2 disulfide single . 1 . 1 CYS 3 3 SG . 1 . 1 CYS 99 99 SG . . . . . . . . . . 4327 1 3 disulfide single . 1 . 1 CYS 13 13 SG . 1 . 1 CYS 124 124 SG . . . . . . . . . . 4327 1 stop_ loop_ _Assembly_db_link.Author_supplied _Assembly_db_link.Database_code _Assembly_db_link.Accession_code _Assembly_db_link.Entry_mol_code _Assembly_db_link.Entry_mol_name _Assembly_db_link.Entry_experimental_method _Assembly_db_link.Entry_structure_resolution _Assembly_db_link.Entry_relation_type _Assembly_db_link.Entry_details _Assembly_db_link.Entry_ID _Assembly_db_link.Assembly_ID yes PDB 1D2B . 'Chain A, The Mmp-Inhibitory, N-Terminal Domain Of Human Tissue Inhibitor Of Metalloproteinases-1 (N-Timp-1), Solution Nmr, 29 Structures' . . . . 4327 1 yes PDB 1UEA . 'Chain B, Mmp-3TIMP-1 Complex' . . . . 4327 1 stop_ loop_ _Assembly_common_name.Name _Assembly_common_name.Type _Assembly_common_name.Entry_ID _Assembly_common_name.Assembly_ID 'N-terminal inhibitory domain of human tissue inhibitor of metalloproteinases-1' system 4327 1 N-TIMP-1 abbreviation 4327 1 stop_ loop_ _Assembly_bio_function.Biological_function _Assembly_bio_function.Entry_ID _Assembly_bio_function.Assembly_ID ; N-TIMP-1 inhibits matrix metalloproteinases-1,-2, & -3 with Ki values less than 2.0 nM. ; 4327 1 stop_ save_ #################################### # Biological polymers and ligands # #################################### save_N-TIMP-1 _Entity.Sf_category entity _Entity.Sf_framecode N-TIMP-1 _Entity.Entry_ID 4327 _Entity.ID 1 _Entity.BMRB_code . _Entity.Name 'N-terminal inhibitory domain of human tissue inhibitor of metalloproteinases-1' _Entity.Type polymer _Entity.Polymer_common_type . _Entity.Polymer_type polypeptide(L) _Entity.Polymer_type_details . _Entity.Polymer_strand_ID . _Entity.Polymer_seq_one_letter_code_can . _Entity.Polymer_seq_one_letter_code ; CTCVPPHPQTAFCNSDLVIR AKFVGTPEVNQTTLYQRYEI KMTKMYKGFQALGDAADIRF VYTPAMESVCGYFHRSHNRS EEFLIAGKLQDGLLHITTCS FVAPWNSLSLAQRRGFTKTY TVGCEE ; _Entity.Target_identifier . _Entity.Polymer_author_defined_seq . _Entity.Polymer_author_seq_details . _Entity.Ambiguous_conformational_states . _Entity.Ambiguous_chem_comp_sites . _Entity.Nstd_monomer . _Entity.Nstd_chirality . _Entity.Nstd_linkage . _Entity.Nonpolymer_comp_ID . _Entity.Nonpolymer_comp_label . _Entity.Number_of_monomers 126 _Entity.Number_of_nonpolymer_components . _Entity.Paramagnetic . _Entity.Thiol_state . _Entity.Src_method . _Entity.Parent_entity_ID 1 _Entity.Fragment . _Entity.Mutation . _Entity.EC_number . _Entity.Calc_isoelectric_point . _Entity.Formula_weight 14236 _Entity.Formula_weight_exptl . _Entity.Formula_weight_exptl_meth . _Entity.Details ; The full human TIMP-1 sequence was reported by Docherty, A.J.P., Lyons, A., Smith, B.J., Wright, E.M., Stephens, P.E., Harris, T.J.R., Murphy, G. and Reynolds, J.J. (1985) "Sequence of human tissue inhibitor of metalloproteinases and its identity to erythroid protentiating activity" Nature, 318, 65-69 ; _Entity.DB_query_date . _Entity.DB_query_revised_last_date 2015-11-24 loop_ _Entity_db_link.Ordinal _Entity_db_link.Author_supplied _Entity_db_link.Database_code _Entity_db_link.Accession_code _Entity_db_link.Entry_mol_code _Entity_db_link.Entry_mol_name _Entity_db_link.Entry_experimental_method _Entity_db_link.Entry_structure_resolution _Entity_db_link.Entry_relation_type _Entity_db_link.Entry_details _Entity_db_link.Chimera_segment_ID _Entity_db_link.Seq_query_to_submitted_percent _Entity_db_link.Seq_subject_length _Entity_db_link.Seq_identity _Entity_db_link.Seq_positive _Entity_db_link.Seq_homology_expectation_val _Entity_db_link.Seq_align_begin _Entity_db_link.Seq_align_end _Entity_db_link.Seq_difference_details _Entity_db_link.Seq_alignment_details _Entity_db_link.Entry_ID _Entity_db_link.Entity_ID 1 no PDB 1D2B . "The Mmp-Inhibitory, N-Terminal Domain Of Human Tissue Inhibitor Of Metalloproteinases-1 (N-Timp-1), Solution Nmr, 29 Structures" . . . . . 100.00 126 100.00 100.00 1.51e-89 . . . . 4327 1 2 no PDB 1OO9 . "Orientation In Solution Of Mmp-3 Catalytic Domain And N- Timp-1 From Residual Dipolar Couplings" . . . . . 100.00 126 100.00 100.00 1.51e-89 . . . . 4327 1 3 no PDB 1UEA . "Mmp-3TIMP-1 Complex" . . . . . 100.00 184 98.41 98.41 3.72e-86 . . . . 4327 1 4 no PDB 2J0T . "Crystal Structure Of The Catalytic Domain Of Mmp-1 In Complex With The Inhibitory Domain Of Timp-1" . . . . . 100.00 126 100.00 100.00 1.51e-89 . . . . 4327 1 5 no PDB 3MA2 . "Complex Membrane Type-1 Matrix Metalloproteinase (mt1-mmp) With Tissue Inhibitor Of Metalloproteinase-1 (timp-1)" . . . . . 99.21 125 97.60 97.60 4.44e-86 . . . . 4327 1 6 no PDB 3V96 . "Complex Of Matrix Metalloproteinase-10 Catalytic Domain (Mmp-10cd) With Tissue Inhibitor Of Metalloproteinases-1 (Timp-1)" . . . . . 100.00 184 99.21 99.21 4.25e-87 . . . . 4327 1 7 no DBJ BAA01913 . "tissue inhibitor of metalloproteinases [Homo sapiens]" . . . . . 85.71 166 99.07 99.07 8.60e-72 . . . . 4327 1 8 no DBJ BAG34878 . "unnamed protein product [Homo sapiens]" . . . . . 100.00 207 100.00 100.00 2.96e-88 . . . . 4327 1 9 no DBJ BAG52016 . "unnamed protein product [Homo sapiens]" . . . . . 100.00 207 100.00 100.00 3.84e-88 . . . . 4327 1 10 no EMBL CAA26443 . "unnamed protein product [Homo sapiens]" . . . . . 100.00 207 100.00 100.00 3.72e-88 . . . . 4327 1 11 no EMBL CAA26902 . "unnamed protein product [Homo sapiens]" . . . . . 100.00 207 100.00 100.00 2.96e-88 . . . . 4327 1 12 no EMBL CAG28566 . "TIMP1 [Homo sapiens]" . . . . . 100.00 207 100.00 100.00 2.96e-88 . . . . 4327 1 13 no EMBL CAG46779 . "TIMP1 [Homo sapiens]" . . . . . 100.00 207 100.00 100.00 2.96e-88 . . . . 4327 1 14 no EMBL CAH90650 . "hypothetical protein [Pongo abelii]" . . . . . 100.00 207 100.00 100.00 2.96e-88 . . . . 4327 1 15 no GB AAA52436 . "prefibroblast collagenase inhibitor [Homo sapiens]" . . . . . 100.00 207 100.00 100.00 2.96e-88 . . . . 4327 1 16 no GB AAA63234 . "collagenase inhibitor [Homo sapiens]" . . . . . 100.00 207 100.00 100.00 2.96e-88 . . . . 4327 1 17 no GB AAA99943 . "metalloprotease-1 tissue inhibitor [Papio cynocephalus]" . . . . . 100.00 207 100.00 100.00 3.68e-88 . . . . 4327 1 18 no GB AAD14009 . "metalloproteinase inhibitor [Homo sapiens]" . . . . . 100.00 207 100.00 100.00 2.96e-88 . . . . 4327 1 19 no GB AAH00866 . "TIMP metallopeptidase inhibitor 1 [Homo sapiens]" . . . . . 100.00 207 100.00 100.00 2.96e-88 . . . . 4327 1 20 no PIR JC4303 . "matrix metalloproteinase-1 tissue inhibitor - baboon" . . . . . 100.00 207 100.00 100.00 3.68e-88 . . . . 4327 1 21 no PRF 1107278A . "erythroid potentiating activity" . . . . . 100.00 207 100.00 100.00 2.96e-88 . . . . 4327 1 22 no PRF 1308125A . "metalloproteinase inhibitor" . . . . . 100.00 207 100.00 100.00 2.96e-88 . . . . 4327 1 23 no REF NP_001028111 . "metalloproteinase inhibitor 1 precursor [Macaca mulatta]" . . . . . 100.00 207 99.21 99.21 1.07e-86 . . . . 4327 1 24 no REF NP_001125351 . "metalloproteinase inhibitor 1 precursor [Pongo abelii]" . . . . . 100.00 207 100.00 100.00 2.96e-88 . . . . 4327 1 25 no REF NP_003245 . "metalloproteinase inhibitor 1 precursor [Homo sapiens]" . . . . . 100.00 207 100.00 100.00 2.96e-88 . . . . 4327 1 26 no REF XP_003917687 . "PREDICTED: metalloproteinase inhibitor 1 [Papio anubis]" . . . . . 100.00 207 100.00 100.00 3.68e-88 . . . . 4327 1 27 no REF XP_005593482 . "PREDICTED: metalloproteinase inhibitor 1 [Macaca fascicularis]" . . . . . 100.00 207 99.21 99.21 1.07e-86 . . . . 4327 1 28 no SP P01033 . "RecName: Full=Metalloproteinase inhibitor 1; AltName: Full=Erythroid-potentiating activity; Short=EPA; AltName: Full=Fibroblast" . . . . . 100.00 207 100.00 100.00 2.96e-88 . . . . 4327 1 29 no SP P49061 . "RecName: Full=Metalloproteinase inhibitor 1; AltName: Full=Tissue inhibitor of metalloproteinases 1; Short=TIMP-1; Flags: Precu" . . . . . 100.00 207 100.00 100.00 3.68e-88 . . . . 4327 1 30 no SP Q5RC60 . "RecName: Full=Metalloproteinase inhibitor 1; AltName: Full=Tissue inhibitor of metalloproteinases 1; Short=TIMP-1; Flags: Precu" . . . . . 100.00 207 100.00 100.00 2.96e-88 . . . . 4327 1 31 no SP Q95KL9 . "RecName: Full=Metalloproteinase inhibitor 1; AltName: Full=Tissue inhibitor of metalloproteinases 1; Short=TIMP-1; Flags: Precu" . . . . . 100.00 207 99.21 99.21 1.07e-86 . . . . 4327 1 stop_ loop_ _Entity_common_name.Name _Entity_common_name.Type _Entity_common_name.Entry_ID _Entity_common_name.Entity_ID 'N-terminal inhibitory domain of human tissue inhibitor of metalloproteinases-1' common 4327 1 N-TIMP-1 abbreviation 4327 1 stop_ loop_ _Entity_comp_index.ID _Entity_comp_index.Auth_seq_ID _Entity_comp_index.Comp_ID _Entity_comp_index.Comp_label _Entity_comp_index.Entry_ID _Entity_comp_index.Entity_ID 1 . CYS . 4327 1 2 . THR . 4327 1 3 . CYS . 4327 1 4 . VAL . 4327 1 5 . PRO . 4327 1 6 . PRO . 4327 1 7 . HIS . 4327 1 8 . PRO . 4327 1 9 . GLN . 4327 1 10 . THR . 4327 1 11 . ALA . 4327 1 12 . PHE . 4327 1 13 . CYS . 4327 1 14 . ASN . 4327 1 15 . SER . 4327 1 16 . ASP . 4327 1 17 . LEU . 4327 1 18 . VAL . 4327 1 19 . ILE . 4327 1 20 . ARG . 4327 1 21 . ALA . 4327 1 22 . LYS . 4327 1 23 . PHE . 4327 1 24 . VAL . 4327 1 25 . GLY . 4327 1 26 . THR . 4327 1 27 . PRO . 4327 1 28 . GLU . 4327 1 29 . VAL . 4327 1 30 . ASN . 4327 1 31 . GLN . 4327 1 32 . THR . 4327 1 33 . THR . 4327 1 34 . LEU . 4327 1 35 . TYR . 4327 1 36 . GLN . 4327 1 37 . ARG . 4327 1 38 . TYR . 4327 1 39 . GLU . 4327 1 40 . ILE . 4327 1 41 . LYS . 4327 1 42 . MET . 4327 1 43 . THR . 4327 1 44 . LYS . 4327 1 45 . MET . 4327 1 46 . TYR . 4327 1 47 . LYS . 4327 1 48 . GLY . 4327 1 49 . PHE . 4327 1 50 . GLN . 4327 1 51 . ALA . 4327 1 52 . LEU . 4327 1 53 . GLY . 4327 1 54 . ASP . 4327 1 55 . ALA . 4327 1 56 . ALA . 4327 1 57 . ASP . 4327 1 58 . ILE . 4327 1 59 . ARG . 4327 1 60 . PHE . 4327 1 61 . VAL . 4327 1 62 . TYR . 4327 1 63 . THR . 4327 1 64 . PRO . 4327 1 65 . ALA . 4327 1 66 . MET . 4327 1 67 . GLU . 4327 1 68 . SER . 4327 1 69 . VAL . 4327 1 70 . CYS . 4327 1 71 . GLY . 4327 1 72 . TYR . 4327 1 73 . PHE . 4327 1 74 . HIS . 4327 1 75 . ARG . 4327 1 76 . SER . 4327 1 77 . HIS . 4327 1 78 . ASN . 4327 1 79 . ARG . 4327 1 80 . SER . 4327 1 81 . GLU . 4327 1 82 . GLU . 4327 1 83 . PHE . 4327 1 84 . LEU . 4327 1 85 . ILE . 4327 1 86 . ALA . 4327 1 87 . GLY . 4327 1 88 . LYS . 4327 1 89 . LEU . 4327 1 90 . GLN . 4327 1 91 . ASP . 4327 1 92 . GLY . 4327 1 93 . LEU . 4327 1 94 . LEU . 4327 1 95 . HIS . 4327 1 96 . ILE . 4327 1 97 . THR . 4327 1 98 . THR . 4327 1 99 . CYS . 4327 1 100 . SER . 4327 1 101 . PHE . 4327 1 102 . VAL . 4327 1 103 . ALA . 4327 1 104 . PRO . 4327 1 105 . TRP . 4327 1 106 . ASN . 4327 1 107 . SER . 4327 1 108 . LEU . 4327 1 109 . SER . 4327 1 110 . LEU . 4327 1 111 . ALA . 4327 1 112 . GLN . 4327 1 113 . ARG . 4327 1 114 . ARG . 4327 1 115 . GLY . 4327 1 116 . PHE . 4327 1 117 . THR . 4327 1 118 . LYS . 4327 1 119 . THR . 4327 1 120 . TYR . 4327 1 121 . THR . 4327 1 122 . VAL . 4327 1 123 . GLY . 4327 1 124 . CYS . 4327 1 125 . GLU . 4327 1 126 . GLU . 4327 1 stop_ loop_ _Entity_poly_seq.Hetero _Entity_poly_seq.Mon_ID _Entity_poly_seq.Num _Entity_poly_seq.Comp_index_ID _Entity_poly_seq.Entry_ID _Entity_poly_seq.Entity_ID . CYS 1 1 4327 1 . THR 2 2 4327 1 . CYS 3 3 4327 1 . VAL 4 4 4327 1 . PRO 5 5 4327 1 . PRO 6 6 4327 1 . HIS 7 7 4327 1 . PRO 8 8 4327 1 . GLN 9 9 4327 1 . THR 10 10 4327 1 . ALA 11 11 4327 1 . PHE 12 12 4327 1 . CYS 13 13 4327 1 . ASN 14 14 4327 1 . SER 15 15 4327 1 . ASP 16 16 4327 1 . LEU 17 17 4327 1 . VAL 18 18 4327 1 . ILE 19 19 4327 1 . ARG 20 20 4327 1 . ALA 21 21 4327 1 . LYS 22 22 4327 1 . PHE 23 23 4327 1 . VAL 24 24 4327 1 . GLY 25 25 4327 1 . THR 26 26 4327 1 . PRO 27 27 4327 1 . GLU 28 28 4327 1 . VAL 29 29 4327 1 . ASN 30 30 4327 1 . GLN 31 31 4327 1 . THR 32 32 4327 1 . THR 33 33 4327 1 . LEU 34 34 4327 1 . TYR 35 35 4327 1 . GLN 36 36 4327 1 . ARG 37 37 4327 1 . TYR 38 38 4327 1 . GLU 39 39 4327 1 . ILE 40 40 4327 1 . LYS 41 41 4327 1 . MET 42 42 4327 1 . THR 43 43 4327 1 . LYS 44 44 4327 1 . MET 45 45 4327 1 . TYR 46 46 4327 1 . LYS 47 47 4327 1 . GLY 48 48 4327 1 . PHE 49 49 4327 1 . GLN 50 50 4327 1 . ALA 51 51 4327 1 . LEU 52 52 4327 1 . GLY 53 53 4327 1 . ASP 54 54 4327 1 . ALA 55 55 4327 1 . ALA 56 56 4327 1 . ASP 57 57 4327 1 . ILE 58 58 4327 1 . ARG 59 59 4327 1 . PHE 60 60 4327 1 . VAL 61 61 4327 1 . TYR 62 62 4327 1 . THR 63 63 4327 1 . PRO 64 64 4327 1 . ALA 65 65 4327 1 . MET 66 66 4327 1 . GLU 67 67 4327 1 . SER 68 68 4327 1 . VAL 69 69 4327 1 . CYS 70 70 4327 1 . GLY 71 71 4327 1 . TYR 72 72 4327 1 . PHE 73 73 4327 1 . HIS 74 74 4327 1 . ARG 75 75 4327 1 . SER 76 76 4327 1 . HIS 77 77 4327 1 . ASN 78 78 4327 1 . ARG 79 79 4327 1 . SER 80 80 4327 1 . GLU 81 81 4327 1 . GLU 82 82 4327 1 . PHE 83 83 4327 1 . LEU 84 84 4327 1 . ILE 85 85 4327 1 . ALA 86 86 4327 1 . GLY 87 87 4327 1 . LYS 88 88 4327 1 . LEU 89 89 4327 1 . GLN 90 90 4327 1 . ASP 91 91 4327 1 . GLY 92 92 4327 1 . LEU 93 93 4327 1 . LEU 94 94 4327 1 . HIS 95 95 4327 1 . ILE 96 96 4327 1 . THR 97 97 4327 1 . THR 98 98 4327 1 . CYS 99 99 4327 1 . SER 100 100 4327 1 . PHE 101 101 4327 1 . VAL 102 102 4327 1 . ALA 103 103 4327 1 . PRO 104 104 4327 1 . TRP 105 105 4327 1 . ASN 106 106 4327 1 . SER 107 107 4327 1 . LEU 108 108 4327 1 . SER 109 109 4327 1 . LEU 110 110 4327 1 . ALA 111 111 4327 1 . GLN 112 112 4327 1 . ARG 113 113 4327 1 . ARG 114 114 4327 1 . GLY 115 115 4327 1 . PHE 116 116 4327 1 . THR 117 117 4327 1 . LYS 118 118 4327 1 . THR 119 119 4327 1 . TYR 120 120 4327 1 . THR 121 121 4327 1 . VAL 122 122 4327 1 . GLY 123 123 4327 1 . CYS 124 124 4327 1 . GLU 125 125 4327 1 . GLU 126 126 4327 1 stop_ save_ #################### # Natural source # #################### save_natural_source _Entity_natural_src_list.Sf_category natural_source _Entity_natural_src_list.Sf_framecode natural_source _Entity_natural_src_list.Entry_ID 4327 _Entity_natural_src_list.ID 1 loop_ _Entity_natural_src.ID _Entity_natural_src.Entity_ID _Entity_natural_src.Entity_label _Entity_natural_src.Entity_chimera_segment_ID _Entity_natural_src.NCBI_taxonomy_ID _Entity_natural_src.Type _Entity_natural_src.Common _Entity_natural_src.Organism_name_scientific _Entity_natural_src.Organism_name_common _Entity_natural_src.Organism_acronym _Entity_natural_src.ICTVdb_decimal_code _Entity_natural_src.Superkingdom _Entity_natural_src.Kingdom _Entity_natural_src.Genus _Entity_natural_src.Species _Entity_natural_src.Strain _Entity_natural_src.Variant _Entity_natural_src.Subvariant _Entity_natural_src.Organ _Entity_natural_src.Tissue _Entity_natural_src.Tissue_fraction _Entity_natural_src.Cell_line _Entity_natural_src.Cell_type _Entity_natural_src.ATCC_number _Entity_natural_src.Organelle _Entity_natural_src.Cellular_location _Entity_natural_src.Fragment _Entity_natural_src.Fraction _Entity_natural_src.Secretion _Entity_natural_src.Plasmid _Entity_natural_src.Plasmid_details _Entity_natural_src.Gene_mnemonic _Entity_natural_src.Dev_stage _Entity_natural_src.Details _Entity_natural_src.Citation_ID _Entity_natural_src.Citation_label _Entity_natural_src.Entry_ID _Entity_natural_src.Entity_natural_src_list_ID 1 1 $N-TIMP-1 . 9606 organism . 'Homo sapiens' human . . Eukaryota Metazoa Homo sapiens . . . . . . . . . . . . . . . . . . ; Full length TIMP-1 is found in the extracellular matrix of many human tissues and in body fluids. ; . . 4327 1 stop_ save_ ######################### # Experimental source # ######################### save_experimental_source _Entity_experimental_src_list.Sf_category experimental_source _Entity_experimental_src_list.Sf_framecode experimental_source _Entity_experimental_src_list.Entry_ID 4327 _Entity_experimental_src_list.ID 1 loop_ _Entity_experimental_src.ID _Entity_experimental_src.Entity_ID _Entity_experimental_src.Entity_label _Entity_experimental_src.Entity_chimera_segment_ID _Entity_experimental_src.Production_method _Entity_experimental_src.Host_org_scientific_name _Entity_experimental_src.Host_org_name_common _Entity_experimental_src.Host_org_details _Entity_experimental_src.Host_org_NCBI_taxonomy_ID _Entity_experimental_src.Host_org_genus _Entity_experimental_src.Host_org_species _Entity_experimental_src.Host_org_strain _Entity_experimental_src.Host_org_variant _Entity_experimental_src.Host_org_subvariant _Entity_experimental_src.Host_org_organ _Entity_experimental_src.Host_org_tissue _Entity_experimental_src.Host_org_tissue_fraction _Entity_experimental_src.Host_org_cell_line _Entity_experimental_src.Host_org_cell_type _Entity_experimental_src.Host_org_cellular_location _Entity_experimental_src.Host_org_organelle _Entity_experimental_src.Host_org_gene _Entity_experimental_src.Host_org_culture_collection _Entity_experimental_src.Host_org_ATCC_number _Entity_experimental_src.Vector_type _Entity_experimental_src.PDBview_host_org_vector_name _Entity_experimental_src.PDBview_plasmid_name _Entity_experimental_src.Vector_name _Entity_experimental_src.Vector_details _Entity_experimental_src.Vendor_name _Entity_experimental_src.Host_org_dev_stage _Entity_experimental_src.Details _Entity_experimental_src.Citation_ID _Entity_experimental_src.Citation_label _Entity_experimental_src.Entry_ID _Entity_experimental_src.Entity_experimental_src_list_ID 1 1 $N-TIMP-1 . 'recombinant technology' 'Escherichia coli' 'E. coli' . . Escherichia coli . . . . . . . . . . . . . . . . pET3a . . . . . . 4327 1 stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_15N-labeled_N-TIMP-1 _Sample.Sf_category sample _Sample.Sf_framecode 15N-labeled_N-TIMP-1 _Sample.Entry_ID 4327 _Sample.ID 1 _Sample.Type solution _Sample.Sub_type . _Sample.Details . _Sample.Aggregate_sample_number . _Sample.Solvent_system . _Sample.Preparation_date . _Sample.Preparation_expiration_date . _Sample.Polycrystallization_protocol . _Sample.Single_crystal_protocol . _Sample.Crystal_grow_apparatus . _Sample.Crystal_grow_atmosphere . _Sample.Crystal_grow_details . _Sample.Crystal_grow_method . _Sample.Crystal_grow_method_cit_ID . _Sample.Crystal_grow_pH . _Sample.Crystal_grow_pH_range . _Sample.Crystal_grow_pressure . _Sample.Crystal_grow_pressure_esd . _Sample.Crystal_grow_seeding . _Sample.Crystal_grow_seeding_cit_ID . _Sample.Crystal_grow_temp . _Sample.Crystal_grow_temp_details . _Sample.Crystal_grow_temp_esd . _Sample.Crystal_grow_time . _Sample.Oriented_sample_prep_protocol . _Sample.Lyophilization_cryo_protectant . _Sample.Storage_protocol . loop_ _Sample_component.ID _Sample_component.Mol_common_name _Sample_component.Isotopic_labeling _Sample_component.Assembly_ID _Sample_component.Assembly_label _Sample_component.Entity_ID _Sample_component.Entity_label _Sample_component.Product_ID _Sample_component.Type _Sample_component.Concentration_val _Sample_component.Concentration_val_min _Sample_component.Concentration_val_max _Sample_component.Concentration_val_units _Sample_component.Concentration_val_err _Sample_component.Vendor _Sample_component.Vendor_product_name _Sample_component.Vendor_product_code _Sample_component.Entry_ID _Sample_component.Sample_ID 1 'N-terminal inhibitory domain of human tissue inhibitor of metalloproteinases-1' [U-15N] . . 1 $N-TIMP-1 . . . 0.5 0.6 mM . . . . 4327 1 2 'sodium acetate d3' . . . . . . . 20 . . mM . . . . 4327 1 3 NaCl . . . . . . . 150 . . mM . . . . 4327 1 4 NaN3 . . . . . . . 1 . . mM . . . . 4327 1 5 D2O . . . . . . . 7 . . % . . . . 4327 1 6 H2O . . . . . . . 93 . . % . . . . 4327 1 stop_ save_ save_13C_15N-labeled_N-TIMP-1 _Sample.Sf_category sample _Sample.Sf_framecode 13C_15N-labeled_N-TIMP-1 _Sample.Entry_ID 4327 _Sample.ID 2 _Sample.Type solution _Sample.Sub_type . _Sample.Details . _Sample.Aggregate_sample_number . _Sample.Solvent_system . _Sample.Preparation_date . _Sample.Preparation_expiration_date . _Sample.Polycrystallization_protocol . _Sample.Single_crystal_protocol . _Sample.Crystal_grow_apparatus . _Sample.Crystal_grow_atmosphere . _Sample.Crystal_grow_details . _Sample.Crystal_grow_method . _Sample.Crystal_grow_method_cit_ID . _Sample.Crystal_grow_pH . _Sample.Crystal_grow_pH_range . _Sample.Crystal_grow_pressure . _Sample.Crystal_grow_pressure_esd . _Sample.Crystal_grow_seeding . _Sample.Crystal_grow_seeding_cit_ID . _Sample.Crystal_grow_temp . _Sample.Crystal_grow_temp_details . _Sample.Crystal_grow_temp_esd . _Sample.Crystal_grow_time . _Sample.Oriented_sample_prep_protocol . _Sample.Lyophilization_cryo_protectant . _Sample.Storage_protocol . loop_ _Sample_component.ID _Sample_component.Mol_common_name _Sample_component.Isotopic_labeling _Sample_component.Assembly_ID _Sample_component.Assembly_label _Sample_component.Entity_ID _Sample_component.Entity_label _Sample_component.Product_ID _Sample_component.Type _Sample_component.Concentration_val _Sample_component.Concentration_val_min _Sample_component.Concentration_val_max _Sample_component.Concentration_val_units _Sample_component.Concentration_val_err _Sample_component.Vendor _Sample_component.Vendor_product_name _Sample_component.Vendor_product_code _Sample_component.Entry_ID _Sample_component.Sample_ID 1 'N-terminal inhibitory domain of human tissue inhibitor of metalloproteinases-1' '[U-13C; U-15N]' . . 1 $N-TIMP-1 . . . 0.9 1.0 mM . . . . 4327 2 2 'sodium acetate d3' . . . . . . . 20 . . mM . . . . 4327 2 3 NaCl . . . . . . . 150 . . mM . . . . 4327 2 4 NaN3 . . . . . . . 1 . . mM . . . . 4327 2 5 D2O . . . . . . . 7 . . % . . . . 4327 2 6 H2O . . . . . . . 93 . . % . . . . 4327 2 stop_ save_ save_16%_13C-labeled_N-TIMP-1 _Sample.Sf_category sample _Sample.Sf_framecode 16%_13C-labeled_N-TIMP-1 _Sample.Entry_ID 4327 _Sample.ID 3 _Sample.Type solution _Sample.Sub_type . _Sample.Details . _Sample.Aggregate_sample_number . _Sample.Solvent_system . _Sample.Preparation_date . _Sample.Preparation_expiration_date . _Sample.Polycrystallization_protocol . _Sample.Single_crystal_protocol . _Sample.Crystal_grow_apparatus . _Sample.Crystal_grow_atmosphere . _Sample.Crystal_grow_details . _Sample.Crystal_grow_method . _Sample.Crystal_grow_method_cit_ID . _Sample.Crystal_grow_pH . _Sample.Crystal_grow_pH_range . _Sample.Crystal_grow_pressure . _Sample.Crystal_grow_pressure_esd . _Sample.Crystal_grow_seeding . _Sample.Crystal_grow_seeding_cit_ID . _Sample.Crystal_grow_temp . _Sample.Crystal_grow_temp_details . _Sample.Crystal_grow_temp_esd . _Sample.Crystal_grow_time . _Sample.Oriented_sample_prep_protocol . _Sample.Lyophilization_cryo_protectant . _Sample.Storage_protocol . loop_ _Sample_component.ID _Sample_component.Mol_common_name _Sample_component.Isotopic_labeling _Sample_component.Assembly_ID _Sample_component.Assembly_label _Sample_component.Entity_ID _Sample_component.Entity_label _Sample_component.Product_ID _Sample_component.Type _Sample_component.Concentration_val _Sample_component.Concentration_val_min _Sample_component.Concentration_val_max _Sample_component.Concentration_val_units _Sample_component.Concentration_val_err _Sample_component.Vendor _Sample_component.Vendor_product_name _Sample_component.Vendor_product_code _Sample_component.Entry_ID _Sample_component.Sample_ID 1 'N-terminal inhibitory domain of human tissue inhibitor of metalloproteinases-1' '[U-16% 13C]' . . 1 $N-TIMP-1 . . . 0.4 0.5 mM . . . . 4327 3 2 'sodium acetate d3' . . . . . . . 20 . . mM . . . . 4327 3 3 NaCl . . . . . . . 150 . . mM . . . . 4327 3 4 NaN3 . . . . . . . 1 . . mM . . . . 4327 3 5 D2O . . . . . . . 7 . . % . . . . 4327 3 6 H2O . . . . . . . 93 . . % . . . . 4327 3 stop_ save_ ####################### # Sample conditions # ####################### save_standard_conditions _Sample_condition_list.Sf_category sample_conditions _Sample_condition_list.Sf_framecode standard_conditions _Sample_condition_list.Entry_ID 4327 _Sample_condition_list.ID 1 _Sample_condition_list.Details . loop_ _Sample_condition_variable.Type _Sample_condition_variable.Val _Sample_condition_variable.Val_err _Sample_condition_variable.Val_units _Sample_condition_variable.Entry_ID _Sample_condition_variable.Sample_condition_list_ID 'ionic strength' 0.171 0.02 . 4327 1 pH 6.0 0.1 na 4327 1 temperature 293 1 K 4327 1 stop_ save_ ############################ # Computer software used # ############################ save_SYBYL_TRIAD _Software.Sf_category software _Software.Sf_framecode SYBYL_TRIAD _Software.Entry_ID 4327 _Software.ID 1 _Software.Name 'SYBYL TRIAD' _Software.Version '6.2 or 6.3' _Software.Details . loop_ _Task.Task _Task.Entry_ID _Task.Software_ID 'process and interpret NMR spectra' 4327 1 stop_ save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _NMR_spectrometer.Sf_category NMR_spectrometer _NMR_spectrometer.Sf_framecode spectrometer_1 _NMR_spectrometer.Entry_ID 4327 _NMR_spectrometer.ID 1 _NMR_spectrometer.Details . _NMR_spectrometer.Manufacturer Bruker _NMR_spectrometer.Model DRX _NMR_spectrometer.Serial_number . _NMR_spectrometer.Field_strength 500 save_ save_spectrometer_list _NMR_spectrometer_list.Sf_category NMR_spectrometer_list _NMR_spectrometer_list.Sf_framecode spectrometer_list _NMR_spectrometer_list.Entry_ID 4327 _NMR_spectrometer_list.ID 1 loop_ _NMR_spectrometer_view.ID _NMR_spectrometer_view.Name _NMR_spectrometer_view.Manufacturer _NMR_spectrometer_view.Model _NMR_spectrometer_view.Serial_number _NMR_spectrometer_view.Field_strength _NMR_spectrometer_view.Details _NMR_spectrometer_view.Citation_ID _NMR_spectrometer_view.Citation_label _NMR_spectrometer_view.Entry_ID _NMR_spectrometer_view.NMR_spectrometer_list_ID 1 spectrometer_1 Bruker DRX . 500 . . . 4327 1 stop_ save_ ############################# # NMR applied experiments # ############################# save_experiment_list _Experiment_list.Sf_category experiment_list _Experiment_list.Sf_framecode experiment_list _Experiment_list.Entry_ID 4327 _Experiment_list.ID 1 _Experiment_list.Details . loop_ _Experiment.ID _Experiment.Name _Experiment.Raw_data_flag _Experiment.NMR_spec_expt_ID _Experiment.NMR_spec_expt_label _Experiment.MS_expt_ID _Experiment.MS_expt_label _Experiment.SAXS_expt_ID _Experiment.SAXS_expt_label _Experiment.FRET_expt_ID _Experiment.FRET_expt_label _Experiment.EMR_expt_ID _Experiment.EMR_expt_label _Experiment.Sample_ID _Experiment.Sample_label _Experiment.Sample_state _Experiment.Sample_volume _Experiment.Sample_volume_units _Experiment.Sample_condition_list_ID _Experiment.Sample_condition_list_label _Experiment.Sample_spinning_rate _Experiment.Sample_angle _Experiment.NMR_tube_type _Experiment.NMR_spectrometer_ID _Experiment.NMR_spectrometer_label _Experiment.NMR_spectrometer_probe_ID _Experiment.NMR_spectrometer_probe_label _Experiment.NMR_spectral_processing_ID _Experiment.NMR_spectral_processing_label _Experiment.Mass_spectrometer_ID _Experiment.Mass_spectrometer_label _Experiment.Xray_instrument_ID _Experiment.Xray_instrument_label _Experiment.Fluorescence_instrument_ID _Experiment.Fluorescence_instrument_label _Experiment.EMR_instrument_ID _Experiment.EMR_instrument_label _Experiment.Chromatographic_system_ID _Experiment.Chromatographic_system_label _Experiment.Chromatographic_column_ID _Experiment.Chromatographic_column_label _Experiment.Entry_ID _Experiment.Experiment_list_ID 1 '15N HSQC' . . . . . . . . . . . . . . . . 1 $standard_conditions . . . 1 $spectrometer_1 . . . . . . . . . . . . . . . . 4327 1 2 HNCA . . . . . . . . . . . . . . . . 1 $standard_conditions . . . 1 $spectrometer_1 . . . . . . . . . . . . . . . . 4327 1 3 (HA)CA(CO)NH . . . . . . . . . . . . . . . . 1 $standard_conditions . . . 1 $spectrometer_1 . . . . . . . . . . . . . . . . 4327 1 4 HN(CA)HA . . . . . . . . . . . . . . . . 1 $standard_conditions . . . 1 $spectrometer_1 . . . . . . . . . . . . . . . . 4327 1 5 HN(CACO)NH . . . . . . . . . . . . . . . . 1 $standard_conditions . . . 1 $spectrometer_1 . . . . . . . . . . . . . . . . 4327 1 6 HNCO . . . . . . . . . . . . . . . . 1 $standard_conditions . . . 1 $spectrometer_1 . . . . . . . . . . . . . . . . 4327 1 7 CBCA(CO)NH . . . . . . . . . . . . . . . . 1 $standard_conditions . . . 1 $spectrometer_1 . . . . . . . . . . . . . . . . 4327 1 8 CCA(CO)NH . . . . . . . . . . . . . . . . 1 $standard_conditions . . . 1 $spectrometer_1 . . . . . . . . . . . . . . . . 4327 1 9 HCCH-TOCSY . . . . . . . . . . . . . . . . 1 $standard_conditions . . . 1 $spectrometer_1 . . . . . . . . . . . . . . . . 4327 1 10 '15N NOESY-HSQC' . . . . . . . . . . . . . . . . 1 $standard_conditions . . . 1 $spectrometer_1 . . . . . . . . . . . . . . . . 4327 1 11 'time-shared NOESY-(13C,15N)-HSQC' . . . . . . . . . . . . . . . . 1 $standard_conditions . . . 1 $spectrometer_1 . . . . . . . . . . . . . . . . 4327 1 12 '13C HSMQC-NOESY' . . . . . . . . . . . . . . . . 1 $standard_conditions . . . 1 $spectrometer_1 . . . . . . . . . . . . . . . . 4327 1 13 '13C HSQC' . . . . . . . . . . . . . . . . 1 $standard_conditions . . . 1 $spectrometer_1 . . . . . . . . . . . . . . . . 4327 1 14 'Nalorac 8 mm triple resonance probe with shieded' . . . . . . . . . . . . . . . . 1 $standard_conditions . . . 1 $spectrometer_1 . . . . . . . . . . . . . . . . 4327 1 15 'z-gradient coil' . . . . . . . . . . . . . . . . 1 $standard_conditions . . . 1 $spectrometer_1 . . . . . . . . . . . . . . . . 4327 1 stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference _Chem_shift_reference.Sf_category chem_shift_reference _Chem_shift_reference.Sf_framecode chemical_shift_reference _Chem_shift_reference.Entry_ID 4327 _Chem_shift_reference.ID 1 _Chem_shift_reference.Details . loop_ _Chem_shift_ref.Atom_type _Chem_shift_ref.Atom_isotope_number _Chem_shift_ref.Mol_common_name _Chem_shift_ref.Atom_group _Chem_shift_ref.Concentration_val _Chem_shift_ref.Concentration_units _Chem_shift_ref.Solvent _Chem_shift_ref.Rank _Chem_shift_ref.Chem_shift_units _Chem_shift_ref.Chem_shift_val _Chem_shift_ref.Ref_method _Chem_shift_ref.Ref_type _Chem_shift_ref.Indirect_shift_ratio _Chem_shift_ref.External_ref_loc _Chem_shift_ref.External_ref_sample_geometry _Chem_shift_ref.External_ref_axis _Chem_shift_ref.Indirect_shift_ratio_cit_ID _Chem_shift_ref.Indirect_shift_ratio_cit_label _Chem_shift_ref.Ref_correction_type _Chem_shift_ref.Correction_val _Chem_shift_ref.Correction_val_cit_ID _Chem_shift_ref.Correction_val_cit_label _Chem_shift_ref.Entry_ID _Chem_shift_ref.Chem_shift_reference_ID C 13 DSS 'methyl protons' . . . . ppm 0.0 . indirect 0.251449530 . . . . . . . 1 $entry_citation 4327 1 H 1 DSS 'methyl protons' . . . . ppm 0.0 internal direct 1.000000000 . . . . . . . 1 $entry_citation 4327 1 N 15 DSS 'methyl protons' . . . . ppm 0.0 . indirect 0.101329118 . . . . . . . 1 $entry_citation 4327 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_human_N-TIMP-1_free _Assigned_chem_shift_list.Sf_category assigned_chemical_shifts _Assigned_chem_shift_list.Sf_framecode human_N-TIMP-1_free _Assigned_chem_shift_list.Entry_ID 4327 _Assigned_chem_shift_list.ID 1 _Assigned_chem_shift_list.Sample_condition_list_ID 1 _Assigned_chem_shift_list.Sample_condition_list_label $standard_conditions _Assigned_chem_shift_list.Chem_shift_reference_ID 1 _Assigned_chem_shift_list.Chem_shift_reference_label $chemical_shift_reference _Assigned_chem_shift_list.Chem_shift_1H_err . _Assigned_chem_shift_list.Chem_shift_13C_err . _Assigned_chem_shift_list.Chem_shift_15N_err . _Assigned_chem_shift_list.Chem_shift_31P_err . _Assigned_chem_shift_list.Chem_shift_2H_err . _Assigned_chem_shift_list.Chem_shift_19F_err . _Assigned_chem_shift_list.Error_derivation_method . _Assigned_chem_shift_list.Details . _Assigned_chem_shift_list.Text_data_format . _Assigned_chem_shift_list.Text_data . loop_ _Chem_shift_experiment.Experiment_ID _Chem_shift_experiment.Experiment_name _Chem_shift_experiment.Sample_ID _Chem_shift_experiment.Sample_label _Chem_shift_experiment.Sample_state _Chem_shift_experiment.Entry_ID _Chem_shift_experiment.Assigned_chem_shift_list_ID . . 1 $15N-labeled_N-TIMP-1 . 4327 1 . . 2 $13C_15N-labeled_N-TIMP-1 . 4327 1 . . 3 $16%_13C-labeled_N-TIMP-1 . 4327 1 stop_ loop_ _Atom_chem_shift.ID _Atom_chem_shift.Assembly_atom_ID _Atom_chem_shift.Entity_assembly_ID _Atom_chem_shift.Entity_ID _Atom_chem_shift.Comp_index_ID _Atom_chem_shift.Seq_ID _Atom_chem_shift.Comp_ID _Atom_chem_shift.Atom_ID _Atom_chem_shift.Atom_type _Atom_chem_shift.Atom_isotope_number _Atom_chem_shift.Val _Atom_chem_shift.Val_err _Atom_chem_shift.Assign_fig_of_merit _Atom_chem_shift.Ambiguity_code _Atom_chem_shift.Occupancy _Atom_chem_shift.Resonance_ID _Atom_chem_shift.Auth_entity_assembly_ID _Atom_chem_shift.Auth_asym_ID _Atom_chem_shift.Auth_seq_ID _Atom_chem_shift.Auth_comp_ID _Atom_chem_shift.Auth_atom_ID _Atom_chem_shift.Details _Atom_chem_shift.Entry_ID _Atom_chem_shift.Assigned_chem_shift_list_ID 1 . 1 1 1 1 CYS HB2 H 1 3.02 0.03 . 2 . . . . . . . . 4327 1 2 . 1 1 1 1 CYS HB3 H 1 3.34 0.03 . 2 . . . . . . . . 4327 1 3 . 1 1 2 2 THR H H 1 6.97 0.03 . 1 . . . . . . . . 4327 1 4 . 1 1 2 2 THR HA H 1 4.61 0.03 . 1 . . . . . . . . 4327 1 5 . 1 1 2 2 THR HB H 1 4.45 0.03 . 1 . . . . . . . . 4327 1 6 . 1 1 2 2 THR HG21 H 1 1.19 0.03 . 1 . . . . . . . . 4327 1 7 . 1 1 2 2 THR HG22 H 1 1.19 0.03 . 1 . . . . . . . . 4327 1 8 . 1 1 2 2 THR HG23 H 1 1.19 0.03 . 1 . . . . . . . . 4327 1 9 . 1 1 2 2 THR C C 13 173.84 0.1 . 1 . . . . . . . . 4327 1 10 . 1 1 2 2 THR CA C 13 61.23 0.1 . 1 . . . . . . . . 4327 1 11 . 1 1 2 2 THR CB C 13 69.47 0.1 . 1 . . . . . . . . 4327 1 12 . 1 1 2 2 THR CG2 C 13 21.36 0.1 . 1 . . . . . . . . 4327 1 13 . 1 1 3 3 CYS H H 1 7.82 0.03 . 1 . . . . . . . . 4327 1 14 . 1 1 3 3 CYS HA H 1 4.89 0.03 . 1 . . . . . . . . 4327 1 15 . 1 1 3 3 CYS HB2 H 1 3.07 0.03 . 2 . . . . . . . . 4327 1 16 . 1 1 3 3 CYS HB3 H 1 3.44 0.03 . 2 . . . . . . . . 4327 1 17 . 1 1 3 3 CYS CA C 13 54.58 0.1 . 1 . . . . . . . . 4327 1 18 . 1 1 3 3 CYS CB C 13 41.47 0.1 . 1 . . . . . . . . 4327 1 19 . 1 1 3 3 CYS N N 15 120.25 0.01 . 1 . . . . . . . . 4327 1 20 . 1 1 4 4 VAL H H 1 8.36 0.03 . 1 . . . . . . . . 4327 1 21 . 1 1 4 4 VAL HA H 1 4.21 0.03 . 1 . . . . . . . . 4327 1 22 . 1 1 4 4 VAL HG11 H 1 1.05 0.03 . 1 . . . . . . . . 4327 1 23 . 1 1 4 4 VAL HG12 H 1 1.05 0.03 . 1 . . . . . . . . 4327 1 24 . 1 1 4 4 VAL HG13 H 1 1.05 0.03 . 1 . . . . . . . . 4327 1 25 . 1 1 4 4 VAL HG21 H 1 1.04 0.03 . 1 . . . . . . . . 4327 1 26 . 1 1 4 4 VAL HG22 H 1 1.04 0.03 . 1 . . . . . . . . 4327 1 27 . 1 1 4 4 VAL HG23 H 1 1.04 0.03 . 1 . . . . . . . . 4327 1 28 . 1 1 4 4 VAL CA C 13 64.77 0.1 . 1 . . . . . . . . 4327 1 29 . 1 1 4 4 VAL CG1 C 13 21.47 0.1 . 1 . . . . . . . . 4327 1 30 . 1 1 4 4 VAL CG2 C 13 22.04 0.1 . 1 . . . . . . . . 4327 1 31 . 1 1 6 6 PRO HA H 1 4.71 0.03 . 1 . . . . . . . . 4327 1 32 . 1 1 6 6 PRO HB2 H 1 2.02 0.03 . 2 . . . . . . . . 4327 1 33 . 1 1 6 6 PRO HB3 H 1 2.35 0.03 . 2 . . . . . . . . 4327 1 34 . 1 1 6 6 PRO HG2 H 1 1.94 0.03 . 2 . . . . . . . . 4327 1 35 . 1 1 6 6 PRO HG3 H 1 2.17 0.03 . 2 . . . . . . . . 4327 1 36 . 1 1 6 6 PRO HD2 H 1 3.51 0.03 . 2 . . . . . . . . 4327 1 37 . 1 1 6 6 PRO HD3 H 1 4.05 0.03 . 2 . . . . . . . . 4327 1 38 . 1 1 6 6 PRO C C 13 175.87 0.1 . 1 . . . . . . . . 4327 1 39 . 1 1 6 6 PRO CA C 13 61.2 0.1 . 1 . . . . . . . . 4327 1 40 . 1 1 6 6 PRO CB C 13 31.82 0.1 . 1 . . . . . . . . 4327 1 41 . 1 1 6 6 PRO CG C 13 26.65 0.1 . 1 . . . . . . . . 4327 1 42 . 1 1 6 6 PRO CD C 13 49.94 0.1 . 1 . . . . . . . . 4327 1 43 . 1 1 7 7 HIS H H 1 8.46 0.03 . 1 . . . . . . . . 4327 1 44 . 1 1 7 7 HIS HA H 1 4.68 0.03 . 1 . . . . . . . . 4327 1 45 . 1 1 7 7 HIS HB2 H 1 3.13 0.03 . 1 . . . . . . . . 4327 1 46 . 1 1 7 7 HIS HB3 H 1 3.13 0.03 . 1 . . . . . . . . 4327 1 47 . 1 1 7 7 HIS HD2 H 1 7.22 0.03 . 1 . . . . . . . . 4327 1 48 . 1 1 7 7 HIS HE1 H 1 6.83 0.03 . 1 . . . . . . . . 4327 1 49 . 1 1 7 7 HIS CA C 13 54.92 0.1 . 1 . . . . . . . . 4327 1 50 . 1 1 7 7 HIS CB C 13 29.94 0.1 . 1 . . . . . . . . 4327 1 51 . 1 1 7 7 HIS CD2 C 13 118.62 0.1 . 1 . . . . . . . . 4327 1 52 . 1 1 7 7 HIS CE1 C 13 136.53 0.1 . 1 . . . . . . . . 4327 1 53 . 1 1 7 7 HIS N N 15 120.31 0.01 . 1 . . . . . . . . 4327 1 54 . 1 1 8 8 PRO HA H 1 3.38 0.03 . 1 . . . . . . . . 4327 1 55 . 1 1 8 8 PRO HB2 H 1 1.48 0.03 . 2 . . . . . . . . 4327 1 56 . 1 1 8 8 PRO HB3 H 1 1.75 0.03 . 2 . . . . . . . . 4327 1 57 . 1 1 8 8 PRO HG2 H 1 1.68 0.03 . 2 . . . . . . . . 4327 1 58 . 1 1 8 8 PRO HG3 H 1 1.84 0.03 . 2 . . . . . . . . 4327 1 59 . 1 1 8 8 PRO HD2 H 1 3.05 0.03 . 2 . . . . . . . . 4327 1 60 . 1 1 8 8 PRO HD3 H 1 3.56 0.03 . 2 . . . . . . . . 4327 1 61 . 1 1 8 8 PRO C C 13 176.24 0.1 . 1 . . . . . . . . 4327 1 62 . 1 1 8 8 PRO CA C 13 65.7 0.1 . 1 . . . . . . . . 4327 1 63 . 1 1 8 8 PRO CB C 13 30.93 0.1 . 1 . . . . . . . . 4327 1 64 . 1 1 8 8 PRO CG C 13 26.88 0.1 . 1 . . . . . . . . 4327 1 65 . 1 1 8 8 PRO CD C 13 49.47 0.1 . 1 . . . . . . . . 4327 1 66 . 1 1 9 9 GLN H H 1 9.08 0.03 . 1 . . . . . . . . 4327 1 67 . 1 1 9 9 GLN HB2 H 1 1.47 0.03 . 2 . . . . . . . . 4327 1 68 . 1 1 9 9 GLN HB3 H 1 1.79 0.03 . 2 . . . . . . . . 4327 1 69 . 1 1 9 9 GLN HG2 H 1 2.07 0.03 . 1 . . . . . . . . 4327 1 70 . 1 1 9 9 GLN HG3 H 1 2.07 0.03 . 1 . . . . . . . . 4327 1 71 . 1 1 9 9 GLN C C 13 177.83 0.1 . 1 . . . . . . . . 4327 1 72 . 1 1 9 9 GLN CA C 13 58.62 0.1 . 1 . . . . . . . . 4327 1 73 . 1 1 9 9 GLN CB C 13 28.05 0.1 . 1 . . . . . . . . 4327 1 74 . 1 1 9 9 GLN CG C 13 33.93 0.1 . 1 . . . . . . . . 4327 1 75 . 1 1 9 9 GLN N N 15 118.76 0.01 . 1 . . . . . . . . 4327 1 76 . 1 1 10 10 THR H H 1 6.86 0.03 . 1 . . . . . . . . 4327 1 77 . 1 1 10 10 THR HA H 1 3.87 0.03 . 1 . . . . . . . . 4327 1 78 . 1 1 10 10 THR HB H 1 4.23 0.03 . 1 . . . . . . . . 4327 1 79 . 1 1 10 10 THR HG21 H 1 1.23 0.03 . 1 . . . . . . . . 4327 1 80 . 1 1 10 10 THR HG22 H 1 1.23 0.03 . 1 . . . . . . . . 4327 1 81 . 1 1 10 10 THR HG23 H 1 1.23 0.03 . 1 . . . . . . . . 4327 1 82 . 1 1 10 10 THR C C 13 175.98 0.1 . 1 . . . . . . . . 4327 1 83 . 1 1 10 10 THR CA C 13 65.39 0.1 . 1 . . . . . . . . 4327 1 84 . 1 1 10 10 THR CB C 13 68.29 0.1 . 1 . . . . . . . . 4327 1 85 . 1 1 10 10 THR CG2 C 13 22.21 0.1 . 1 . . . . . . . . 4327 1 86 . 1 1 10 10 THR N N 15 117.03 0.01 . 1 . . . . . . . . 4327 1 87 . 1 1 11 11 ALA H H 1 8.53 0.03 . 1 . . . . . . . . 4327 1 88 . 1 1 11 11 ALA HA H 1 4.11 0.03 . 1 . . . . . . . . 4327 1 89 . 1 1 11 11 ALA HB1 H 1 1.5 0.03 . 1 . . . . . . . . 4327 1 90 . 1 1 11 11 ALA HB2 H 1 1.5 0.03 . 1 . . . . . . . . 4327 1 91 . 1 1 11 11 ALA HB3 H 1 1.5 0.03 . 1 . . . . . . . . 4327 1 92 . 1 1 11 11 ALA C C 13 180.17 0.1 . 1 . . . . . . . . 4327 1 93 . 1 1 11 11 ALA CA C 13 54.31 0.1 . 1 . . . . . . . . 4327 1 94 . 1 1 11 11 ALA CB C 13 18.45 0.1 . 1 . . . . . . . . 4327 1 95 . 1 1 11 11 ALA N N 15 123.69 0.01 . 1 . . . . . . . . 4327 1 96 . 1 1 12 12 PHE H H 1 8.39 0.03 . 1 . . . . . . . . 4327 1 97 . 1 1 12 12 PHE HA H 1 3.86 0.03 . 1 . . . . . . . . 4327 1 98 . 1 1 12 12 PHE HB2 H 1 3 0.03 . 2 . . . . . . . . 4327 1 99 . 1 1 12 12 PHE HB3 H 1 3.2 0.03 . 2 . . . . . . . . 4327 1 100 . 1 1 12 12 PHE HD1 H 1 7.27 0.03 . 1 . . . . . . . . 4327 1 101 . 1 1 12 12 PHE HD2 H 1 7.27 0.03 . 1 . . . . . . . . 4327 1 102 . 1 1 12 12 PHE HE1 H 1 7.44 0.03 . 1 . . . . . . . . 4327 1 103 . 1 1 12 12 PHE HE2 H 1 7.44 0.03 . 1 . . . . . . . . 4327 1 104 . 1 1 12 12 PHE C C 13 176.54 0.1 . 1 . . . . . . . . 4327 1 105 . 1 1 12 12 PHE CA C 13 61.99 0.1 . 1 . . . . . . . . 4327 1 106 . 1 1 12 12 PHE CB C 13 39.4 0.1 . 1 . . . . . . . . 4327 1 107 . 1 1 12 12 PHE CD1 C 13 131.29 0.1 . 1 . . . . . . . . 4327 1 108 . 1 1 12 12 PHE CD2 C 13 131.29 0.1 . 1 . . . . . . . . 4327 1 109 . 1 1 12 12 PHE CE1 C 13 131.25 0.1 . 1 . . . . . . . . 4327 1 110 . 1 1 12 12 PHE CE2 C 13 131.25 0.1 . 1 . . . . . . . . 4327 1 111 . 1 1 12 12 PHE N N 15 119.32 0.01 . 1 . . . . . . . . 4327 1 112 . 1 1 13 13 CYS H H 1 7.89 0.03 . 1 . . . . . . . . 4327 1 113 . 1 1 13 13 CYS HA H 1 4.46 0.03 . 1 . . . . . . . . 4327 1 114 . 1 1 13 13 CYS HB2 H 1 2.9 0.03 . 2 . . . . . . . . 4327 1 115 . 1 1 13 13 CYS HB3 H 1 3.39 0.03 . 2 . . . . . . . . 4327 1 116 . 1 1 13 13 CYS C C 13 176.02 0.1 . 1 . . . . . . . . 4327 1 117 . 1 1 13 13 CYS CA C 13 56.33 0.1 . 1 . . . . . . . . 4327 1 118 . 1 1 13 13 CYS CB C 13 36.54 0.1 . 1 . . . . . . . . 4327 1 119 . 1 1 13 13 CYS N N 15 114.84 0.01 . 1 . . . . . . . . 4327 1 120 . 1 1 14 14 ASN H H 1 8.26 0.03 . 1 . . . . . . . . 4327 1 121 . 1 1 14 14 ASN HA H 1 4.69 0.03 . 1 . . . . . . . . 4327 1 122 . 1 1 14 14 ASN HB2 H 1 2.78 0.03 . 2 . . . . . . . . 4327 1 123 . 1 1 14 14 ASN HB3 H 1 2.88 0.03 . 2 . . . . . . . . 4327 1 124 . 1 1 14 14 ASN C C 13 175.51 0.1 . 1 . . . . . . . . 4327 1 125 . 1 1 14 14 ASN CA C 13 53.42 0.1 . 1 . . . . . . . . 4327 1 126 . 1 1 14 14 ASN CB C 13 38.69 0.1 . 1 . . . . . . . . 4327 1 127 . 1 1 14 14 ASN N N 15 115.91 0.01 . 1 . . . . . . . . 4327 1 128 . 1 1 15 15 SER H H 1 7.18 0.03 . 1 . . . . . . . . 4327 1 129 . 1 1 15 15 SER HA H 1 4.35 0.03 . 1 . . . . . . . . 4327 1 130 . 1 1 15 15 SER HB2 H 1 3.47 0.03 . 2 . . . . . . . . 4327 1 131 . 1 1 15 15 SER HB3 H 1 4.22 0.03 . 2 . . . . . . . . 4327 1 132 . 1 1 15 15 SER C C 13 171.89 0.1 . 1 . . . . . . . . 4327 1 133 . 1 1 15 15 SER CA C 13 59.33 0.1 . 1 . . . . . . . . 4327 1 134 . 1 1 15 15 SER CB C 13 63.65 0.1 . 1 . . . . . . . . 4327 1 135 . 1 1 15 15 SER N N 15 116.54 0.01 . 1 . . . . . . . . 4327 1 136 . 1 1 16 16 ASP H H 1 7.92 0.03 . 1 . . . . . . . . 4327 1 137 . 1 1 16 16 ASP HA H 1 4.62 0.03 . 1 . . . . . . . . 4327 1 138 . 1 1 16 16 ASP HB2 H 1 2.45 0.03 . 2 . . . . . . . . 4327 1 139 . 1 1 16 16 ASP HB3 H 1 2.67 0.03 . 2 . . . . . . . . 4327 1 140 . 1 1 16 16 ASP C C 13 175.07 0.1 . 1 . . . . . . . . 4327 1 141 . 1 1 16 16 ASP CA C 13 55.87 0.1 . 1 . . . . . . . . 4327 1 142 . 1 1 16 16 ASP CB C 13 43.15 0.1 . 1 . . . . . . . . 4327 1 143 . 1 1 16 16 ASP N N 15 119.65 0.01 . 1 . . . . . . . . 4327 1 144 . 1 1 17 17 LEU H H 1 7.4 0.03 . 1 . . . . . . . . 4327 1 145 . 1 1 17 17 LEU HA H 1 4.74 0.03 . 1 . . . . . . . . 4327 1 146 . 1 1 17 17 LEU HB2 H 1 1.36 0.03 . 1 . . . . . . . . 4327 1 147 . 1 1 17 17 LEU HB3 H 1 1.36 0.03 . 1 . . . . . . . . 4327 1 148 . 1 1 17 17 LEU HG H 1 1.6 0.03 . 1 . . . . . . . . 4327 1 149 . 1 1 17 17 LEU HD11 H 1 0.89 0.03 . 1 . . . . . . . . 4327 1 150 . 1 1 17 17 LEU HD12 H 1 0.89 0.03 . 1 . . . . . . . . 4327 1 151 . 1 1 17 17 LEU HD13 H 1 0.89 0.03 . 1 . . . . . . . . 4327 1 152 . 1 1 17 17 LEU HD21 H 1 0.91 0.03 . 1 . . . . . . . . 4327 1 153 . 1 1 17 17 LEU HD22 H 1 0.91 0.03 . 1 . . . . . . . . 4327 1 154 . 1 1 17 17 LEU HD23 H 1 0.91 0.03 . 1 . . . . . . . . 4327 1 155 . 1 1 17 17 LEU C C 13 174.92 0.1 . 1 . . . . . . . . 4327 1 156 . 1 1 17 17 LEU CA C 13 52.78 0.1 . 1 . . . . . . . . 4327 1 157 . 1 1 17 17 LEU CB C 13 46.08 0.1 . 1 . . . . . . . . 4327 1 158 . 1 1 17 17 LEU CG C 13 28.12 0.1 . 1 . . . . . . . . 4327 1 159 . 1 1 17 17 LEU CD1 C 13 25.76 0.1 . 1 . . . . . . . . 4327 1 160 . 1 1 17 17 LEU CD2 C 13 25.86 0.1 . 1 . . . . . . . . 4327 1 161 . 1 1 17 17 LEU N N 15 116.19 0.01 . 1 . . . . . . . . 4327 1 162 . 1 1 18 18 VAL H H 1 8.24 0.03 . 1 . . . . . . . . 4327 1 163 . 1 1 18 18 VAL HA H 1 5.21 0.03 . 1 . . . . . . . . 4327 1 164 . 1 1 18 18 VAL HB H 1 2.04 0.03 . 1 . . . . . . . . 4327 1 165 . 1 1 18 18 VAL HG11 H 1 1.19 0.03 . 1 . . . . . . . . 4327 1 166 . 1 1 18 18 VAL HG12 H 1 1.19 0.03 . 1 . . . . . . . . 4327 1 167 . 1 1 18 18 VAL HG13 H 1 1.19 0.03 . 1 . . . . . . . . 4327 1 168 . 1 1 18 18 VAL HG21 H 1 0.8 0.03 . 1 . . . . . . . . 4327 1 169 . 1 1 18 18 VAL HG22 H 1 0.8 0.03 . 1 . . . . . . . . 4327 1 170 . 1 1 18 18 VAL HG23 H 1 0.8 0.03 . 1 . . . . . . . . 4327 1 171 . 1 1 18 18 VAL C C 13 175.53 0.1 . 1 . . . . . . . . 4327 1 172 . 1 1 18 18 VAL CA C 13 61.2 0.1 . 1 . . . . . . . . 4327 1 173 . 1 1 18 18 VAL CB C 13 32.97 0.1 . 1 . . . . . . . . 4327 1 174 . 1 1 18 18 VAL CG1 C 13 22.8 0.1 . 1 . . . . . . . . 4327 1 175 . 1 1 18 18 VAL CG2 C 13 20.85 0.1 . 1 . . . . . . . . 4327 1 176 . 1 1 18 18 VAL N N 15 121.93 0.01 . 1 . . . . . . . . 4327 1 177 . 1 1 19 19 ILE H H 1 9.3 0.03 . 1 . . . . . . . . 4327 1 178 . 1 1 19 19 ILE HA H 1 5.18 0.03 . 1 . . . . . . . . 4327 1 179 . 1 1 19 19 ILE HB H 1 2.03 0.03 . 1 . . . . . . . . 4327 1 180 . 1 1 19 19 ILE HG12 H 1 0.65 0.03 . 2 . . . . . . . . 4327 1 181 . 1 1 19 19 ILE HG13 H 1 1.17 0.03 . 2 . . . . . . . . 4327 1 182 . 1 1 19 19 ILE HG21 H 1 0.91 0.03 . 1 . . . . . . . . 4327 1 183 . 1 1 19 19 ILE HG22 H 1 0.91 0.03 . 1 . . . . . . . . 4327 1 184 . 1 1 19 19 ILE HG23 H 1 0.91 0.03 . 1 . . . . . . . . 4327 1 185 . 1 1 19 19 ILE HD11 H 1 0.43 0.03 . 1 . . . . . . . . 4327 1 186 . 1 1 19 19 ILE HD12 H 1 0.43 0.03 . 1 . . . . . . . . 4327 1 187 . 1 1 19 19 ILE HD13 H 1 0.43 0.03 . 1 . . . . . . . . 4327 1 188 . 1 1 19 19 ILE C C 13 173.02 0.1 . 1 . . . . . . . . 4327 1 189 . 1 1 19 19 ILE CA C 13 58.5 0.1 . 1 . . . . . . . . 4327 1 190 . 1 1 19 19 ILE CB C 13 42.25 0.1 . 1 . . . . . . . . 4327 1 191 . 1 1 19 19 ILE CG1 C 13 24.76 0.1 . 1 . . . . . . . . 4327 1 192 . 1 1 19 19 ILE CG2 C 13 18.65 0.1 . 1 . . . . . . . . 4327 1 193 . 1 1 19 19 ILE CD1 C 13 13.95 0.1 . 1 . . . . . . . . 4327 1 194 . 1 1 19 19 ILE N N 15 121.67 0.01 . 1 . . . . . . . . 4327 1 195 . 1 1 20 20 ARG H H 1 8.87 0.03 . 1 . . . . . . . . 4327 1 196 . 1 1 20 20 ARG HA H 1 5.6 0.03 . 1 . . . . . . . . 4327 1 197 . 1 1 20 20 ARG HB2 H 1 1.18 0.03 . 2 . . . . . . . . 4327 1 198 . 1 1 20 20 ARG HB3 H 1 1.71 0.03 . 2 . . . . . . . . 4327 1 199 . 1 1 20 20 ARG HG2 H 1 1.18 0.03 . 1 . . . . . . . . 4327 1 200 . 1 1 20 20 ARG HG3 H 1 1.18 0.03 . 1 . . . . . . . . 4327 1 201 . 1 1 20 20 ARG HD2 H 1 1.55 0.03 . 2 . . . . . . . . 4327 1 202 . 1 1 20 20 ARG HD3 H 1 1.84 0.03 . 2 . . . . . . . . 4327 1 203 . 1 1 20 20 ARG C C 13 175.98 0.1 . 1 . . . . . . . . 4327 1 204 . 1 1 20 20 ARG CA C 13 53.88 0.1 . 1 . . . . . . . . 4327 1 205 . 1 1 20 20 ARG CB C 13 33.75 0.1 . 1 . . . . . . . . 4327 1 206 . 1 1 20 20 ARG CG C 13 26.51 0.1 . 1 . . . . . . . . 4327 1 207 . 1 1 20 20 ARG CD C 13 43.76 0.1 . 1 . . . . . . . . 4327 1 208 . 1 1 20 20 ARG N N 15 121.31 0.01 . 1 . . . . . . . . 4327 1 209 . 1 1 21 21 ALA H H 1 9.48 0.03 . 1 . . . . . . . . 4327 1 210 . 1 1 21 21 ALA HA H 1 5.17 0.03 . 1 . . . . . . . . 4327 1 211 . 1 1 21 21 ALA HB1 H 1 0.92 0.03 . 1 . . . . . . . . 4327 1 212 . 1 1 21 21 ALA HB2 H 1 0.92 0.03 . 1 . . . . . . . . 4327 1 213 . 1 1 21 21 ALA HB3 H 1 0.92 0.03 . 1 . . . . . . . . 4327 1 214 . 1 1 21 21 ALA C C 13 175.27 0.1 . 1 . . . . . . . . 4327 1 215 . 1 1 21 21 ALA CA C 13 50.88 0.1 . 1 . . . . . . . . 4327 1 216 . 1 1 21 21 ALA CB C 13 24.29 0.1 . 1 . . . . . . . . 4327 1 217 . 1 1 21 21 ALA N N 15 124.61 0.01 . 1 . . . . . . . . 4327 1 218 . 1 1 22 22 LYS H H 1 8.37 0.03 . 1 . . . . . . . . 4327 1 219 . 1 1 22 22 LYS HA H 1 4.98 0.03 . 1 . . . . . . . . 4327 1 220 . 1 1 22 22 LYS HB2 H 1 1.39 0.03 . 2 . . . . . . . . 4327 1 221 . 1 1 22 22 LYS HB3 H 1 1.97 0.03 . 2 . . . . . . . . 4327 1 222 . 1 1 22 22 LYS HG2 H 1 1.28 0.03 . 1 . . . . . . . . 4327 1 223 . 1 1 22 22 LYS HG3 H 1 1.28 0.03 . 1 . . . . . . . . 4327 1 224 . 1 1 22 22 LYS HD2 H 1 1.54 0.03 . 2 . . . . . . . . 4327 1 225 . 1 1 22 22 LYS HD3 H 1 1.71 0.03 . 2 . . . . . . . . 4327 1 226 . 1 1 22 22 LYS HE2 H 1 2.77 0.03 . 2 . . . . . . . . 4327 1 227 . 1 1 22 22 LYS HE3 H 1 2.87 0.03 . 2 . . . . . . . . 4327 1 228 . 1 1 22 22 LYS C C 13 175.83 0.1 . 1 . . . . . . . . 4327 1 229 . 1 1 22 22 LYS CA C 13 54.55 0.1 . 1 . . . . . . . . 4327 1 230 . 1 1 22 22 LYS CB C 13 34.29 0.1 . 1 . . . . . . . . 4327 1 231 . 1 1 22 22 LYS CG C 13 25.78 0.1 . 1 . . . . . . . . 4327 1 232 . 1 1 22 22 LYS CD C 13 29.36 0.1 . 1 . . . . . . . . 4327 1 233 . 1 1 22 22 LYS CE C 13 41.75 0.1 . 1 . . . . . . . . 4327 1 234 . 1 1 22 22 LYS N N 15 119.31 0.01 . 1 . . . . . . . . 4327 1 235 . 1 1 23 23 PHE H H 1 9.63 0.03 . 1 . . . . . . . . 4327 1 236 . 1 1 23 23 PHE HA H 1 4.38 0.03 . 1 . . . . . . . . 4327 1 237 . 1 1 23 23 PHE HB2 H 1 2.58 0.03 . 2 . . . . . . . . 4327 1 238 . 1 1 23 23 PHE HB3 H 1 2.67 0.03 . 2 . . . . . . . . 4327 1 239 . 1 1 23 23 PHE HD1 H 1 6.52 0.03 . 1 . . . . . . . . 4327 1 240 . 1 1 23 23 PHE HD2 H 1 6.52 0.03 . 1 . . . . . . . . 4327 1 241 . 1 1 23 23 PHE HE1 H 1 5.92 0.03 . 1 . . . . . . . . 4327 1 242 . 1 1 23 23 PHE HE2 H 1 5.92 0.03 . 1 . . . . . . . . 4327 1 243 . 1 1 23 23 PHE HZ H 1 6.08 0.03 . 1 . . . . . . . . 4327 1 244 . 1 1 23 23 PHE C C 13 176.24 0.1 . 1 . . . . . . . . 4327 1 245 . 1 1 23 23 PHE CA C 13 58.1 0.1 . 1 . . . . . . . . 4327 1 246 . 1 1 23 23 PHE CB C 13 38.84 0.1 . 1 . . . . . . . . 4327 1 247 . 1 1 23 23 PHE CD1 C 13 130.87 0.1 . 1 . . . . . . . . 4327 1 248 . 1 1 23 23 PHE CD2 C 13 130.87 0.1 . 1 . . . . . . . . 4327 1 249 . 1 1 23 23 PHE CE1 C 13 128.55 0.1 . 1 . . . . . . . . 4327 1 250 . 1 1 23 23 PHE CE2 C 13 128.55 0.1 . 1 . . . . . . . . 4327 1 251 . 1 1 23 23 PHE CZ C 13 127.34 0.1 . 1 . . . . . . . . 4327 1 252 . 1 1 23 23 PHE N N 15 124.94 0.01 . 1 . . . . . . . . 4327 1 253 . 1 1 24 24 VAL H H 1 7.92 0.03 . 1 . . . . . . . . 4327 1 254 . 1 1 24 24 VAL HA H 1 4.27 0.03 . 1 . . . . . . . . 4327 1 255 . 1 1 24 24 VAL HB H 1 2.04 0.03 . 1 . . . . . . . . 4327 1 256 . 1 1 24 24 VAL HG11 H 1 0.76 0.03 . 1 . . . . . . . . 4327 1 257 . 1 1 24 24 VAL HG12 H 1 0.76 0.03 . 1 . . . . . . . . 4327 1 258 . 1 1 24 24 VAL HG13 H 1 0.76 0.03 . 1 . . . . . . . . 4327 1 259 . 1 1 24 24 VAL HG21 H 1 0.52 0.03 . 1 . . . . . . . . 4327 1 260 . 1 1 24 24 VAL HG22 H 1 0.52 0.03 . 1 . . . . . . . . 4327 1 261 . 1 1 24 24 VAL HG23 H 1 0.52 0.03 . 1 . . . . . . . . 4327 1 262 . 1 1 24 24 VAL C C 13 175.68 0.1 . 1 . . . . . . . . 4327 1 263 . 1 1 24 24 VAL CA C 13 61.75 0.1 . 1 . . . . . . . . 4327 1 264 . 1 1 24 24 VAL CB C 13 32.34 0.1 . 1 . . . . . . . . 4327 1 265 . 1 1 24 24 VAL CG1 C 13 21.29 0.1 . 1 . . . . . . . . 4327 1 266 . 1 1 24 24 VAL CG2 C 13 19.06 0.1 . 1 . . . . . . . . 4327 1 267 . 1 1 24 24 VAL N N 15 118.32 0.01 . 1 . . . . . . . . 4327 1 268 . 1 1 25 25 GLY H H 1 8.26 0.03 . 1 . . . . . . . . 4327 1 269 . 1 1 25 25 GLY HA2 H 1 4.16 0.03 . 2 . . . . . . . . 4327 1 270 . 1 1 25 25 GLY HA3 H 1 4.38 0.03 . 2 . . . . . . . . 4327 1 271 . 1 1 25 25 GLY C C 13 173.12 0.1 . 1 . . . . . . . . 4327 1 272 . 1 1 25 25 GLY CA C 13 45.12 0.1 . 1 . . . . . . . . 4327 1 273 . 1 1 25 25 GLY N N 15 109.83 0.01 . 1 . . . . . . . . 4327 1 274 . 1 1 26 26 THR H H 1 8.39 0.03 . 1 . . . . . . . . 4327 1 275 . 1 1 26 26 THR HA H 1 4.67 0.03 . 1 . . . . . . . . 4327 1 276 . 1 1 26 26 THR HB H 1 4.31 0.03 . 1 . . . . . . . . 4327 1 277 . 1 1 26 26 THR HG21 H 1 1.35 0.03 . 1 . . . . . . . . 4327 1 278 . 1 1 26 26 THR HG22 H 1 1.35 0.03 . 1 . . . . . . . . 4327 1 279 . 1 1 26 26 THR HG23 H 1 1.35 0.03 . 1 . . . . . . . . 4327 1 280 . 1 1 26 26 THR CA C 13 59.57 0.1 . 1 . . . . . . . . 4327 1 281 . 1 1 26 26 THR CB C 13 68.77 0.1 . 1 . . . . . . . . 4327 1 282 . 1 1 26 26 THR CG2 C 13 21.53 0.1 . 1 . . . . . . . . 4327 1 283 . 1 1 26 26 THR N N 15 116.24 0.01 . 1 . . . . . . . . 4327 1 284 . 1 1 27 27 PRO HA H 1 4.35 0.03 . 1 . . . . . . . . 4327 1 285 . 1 1 27 27 PRO HB2 H 1 0.59 0.03 . 2 . . . . . . . . 4327 1 286 . 1 1 27 27 PRO HB3 H 1 1.19 0.03 . 2 . . . . . . . . 4327 1 287 . 1 1 27 27 PRO HG2 H 1 1.77 0.03 . 2 . . . . . . . . 4327 1 288 . 1 1 27 27 PRO HG3 H 1 1.86 0.03 . 2 . . . . . . . . 4327 1 289 . 1 1 27 27 PRO HD2 H 1 3.65 0.03 . 2 . . . . . . . . 4327 1 290 . 1 1 27 27 PRO HD3 H 1 3.88 0.03 . 2 . . . . . . . . 4327 1 291 . 1 1 27 27 PRO C C 13 176.48 0.1 . 1 . . . . . . . . 4327 1 292 . 1 1 27 27 PRO CA C 13 62.5 0.1 . 1 . . . . . . . . 4327 1 293 . 1 1 27 27 PRO CB C 13 30.41 0.1 . 1 . . . . . . . . 4327 1 294 . 1 1 27 27 PRO CG C 13 26.88 0.1 . 1 . . . . . . . . 4327 1 295 . 1 1 27 27 PRO CD C 13 49.71 0.1 . 1 . . . . . . . . 4327 1 296 . 1 1 28 28 GLU H H 1 8.45 0.03 . 1 . . . . . . . . 4327 1 297 . 1 1 28 28 GLU HA H 1 4.56 0.03 . 1 . . . . . . . . 4327 1 298 . 1 1 28 28 GLU HB2 H 1 1.87 0.03 . 2 . . . . . . . . 4327 1 299 . 1 1 28 28 GLU HB3 H 1 1.92 0.03 . 2 . . . . . . . . 4327 1 300 . 1 1 28 28 GLU HG2 H 1 2.08 0.03 . 1 . . . . . . . . 4327 1 301 . 1 1 28 28 GLU HG3 H 1 2.28 0.03 . 1 . . . . . . . . 4327 1 302 . 1 1 28 28 GLU C C 13 176.04 0.1 . 1 . . . . . . . . 4327 1 303 . 1 1 28 28 GLU CA C 13 54.22 0.1 . 1 . . . . . . . . 4327 1 304 . 1 1 28 28 GLU CB C 13 31.64 0.1 . 1 . . . . . . . . 4327 1 305 . 1 1 28 28 GLU CG C 13 35.73 0.1 . 1 . . . . . . . . 4327 1 306 . 1 1 28 28 GLU N N 15 121.68 0.01 . 1 . . . . . . . . 4327 1 307 . 1 1 29 29 VAL H H 1 9 0.03 . 1 . . . . . . . . 4327 1 308 . 1 1 29 29 VAL HA H 1 3.97 0.03 . 1 . . . . . . . . 4327 1 309 . 1 1 29 29 VAL HB H 1 1.98 0.03 . 1 . . . . . . . . 4327 1 310 . 1 1 29 29 VAL HG11 H 1 0.69 0.03 . 1 . . . . . . . . 4327 1 311 . 1 1 29 29 VAL HG12 H 1 0.69 0.03 . 1 . . . . . . . . 4327 1 312 . 1 1 29 29 VAL HG13 H 1 0.69 0.03 . 1 . . . . . . . . 4327 1 313 . 1 1 29 29 VAL HG21 H 1 0.88 0.03 . 1 . . . . . . . . 4327 1 314 . 1 1 29 29 VAL HG22 H 1 0.88 0.03 . 1 . . . . . . . . 4327 1 315 . 1 1 29 29 VAL HG23 H 1 0.88 0.03 . 1 . . . . . . . . 4327 1 316 . 1 1 29 29 VAL C C 13 174.72 0.1 . 1 . . . . . . . . 4327 1 317 . 1 1 29 29 VAL CA C 13 62.61 0.1 . 1 . . . . . . . . 4327 1 318 . 1 1 29 29 VAL CB C 13 32.77 0.1 . 1 . . . . . . . . 4327 1 319 . 1 1 29 29 VAL CG1 C 13 20.53 0.1 . 1 . . . . . . . . 4327 1 320 . 1 1 29 29 VAL CG2 C 13 21.22 0.1 . 1 . . . . . . . . 4327 1 321 . 1 1 29 29 VAL N N 15 127.86 0.01 . 1 . . . . . . . . 4327 1 322 . 1 1 30 30 ASN H H 1 8.57 0.03 . 1 . . . . . . . . 4327 1 323 . 1 1 30 30 ASN HA H 1 4.86 0.03 . 1 . . . . . . . . 4327 1 324 . 1 1 30 30 ASN HB2 H 1 2.71 0.03 . 2 . . . . . . . . 4327 1 325 . 1 1 30 30 ASN HB3 H 1 3.39 0.03 . 2 . . . . . . . . 4327 1 326 . 1 1 30 30 ASN HD21 H 1 7.61 0.03 . 2 . . . . . . . . 4327 1 327 . 1 1 30 30 ASN HD22 H 1 7.15 0.03 . 2 . . . . . . . . 4327 1 328 . 1 1 30 30 ASN C C 13 175.61 0.1 . 1 . . . . . . . . 4327 1 329 . 1 1 30 30 ASN CA C 13 52.1 0.1 . 1 . . . . . . . . 4327 1 330 . 1 1 30 30 ASN CB C 13 39 0.1 . 1 . . . . . . . . 4327 1 331 . 1 1 30 30 ASN N N 15 127.66 0.01 . 1 . . . . . . . . 4327 1 332 . 1 1 30 30 ASN ND2 N 15 114.99 0.01 . 1 . . . . . . . . 4327 1 333 . 1 1 31 31 GLN H H 1 9.02 0.03 . 1 . . . . . . . . 4327 1 334 . 1 1 31 31 GLN HA H 1 4.07 0.03 . 1 . . . . . . . . 4327 1 335 . 1 1 31 31 GLN HB2 H 1 1.98 0.03 . 2 . . . . . . . . 4327 1 336 . 1 1 31 31 GLN HB3 H 1 2.22 0.03 . 2 . . . . . . . . 4327 1 337 . 1 1 31 31 GLN HG2 H 1 2.37 0.03 . 2 . . . . . . . . 4327 1 338 . 1 1 31 31 GLN HG3 H 1 2.44 0.03 . 2 . . . . . . . . 4327 1 339 . 1 1 31 31 GLN HE21 H 1 7.49 0.03 . 2 . . . . . . . . 4327 1 340 . 1 1 31 31 GLN HE22 H 1 6.81 0.03 . 2 . . . . . . . . 4327 1 341 . 1 1 31 31 GLN C C 13 176.1 0.1 . 1 . . . . . . . . 4327 1 342 . 1 1 31 31 GLN CA C 13 57.3 0.1 . 1 . . . . . . . . 4327 1 343 . 1 1 31 31 GLN CB C 13 28.14 0.1 . 1 . . . . . . . . 4327 1 344 . 1 1 31 31 GLN CG C 13 33.53 0.1 . 1 . . . . . . . . 4327 1 345 . 1 1 31 31 GLN N N 15 124.34 0.01 . 1 . . . . . . . . 4327 1 346 . 1 1 31 31 GLN NE2 N 15 112.4 0.01 . 1 . . . . . . . . 4327 1 347 . 1 1 32 32 THR H H 1 8.53 0.03 . 1 . . . . . . . . 4327 1 348 . 1 1 32 32 THR HA H 1 4.26 0.03 . 1 . . . . . . . . 4327 1 349 . 1 1 32 32 THR HB H 1 4.39 0.03 . 1 . . . . . . . . 4327 1 350 . 1 1 32 32 THR HG21 H 1 1.22 0.03 . 1 . . . . . . . . 4327 1 351 . 1 1 32 32 THR HG22 H 1 1.22 0.03 . 1 . . . . . . . . 4327 1 352 . 1 1 32 32 THR HG23 H 1 1.22 0.03 . 1 . . . . . . . . 4327 1 353 . 1 1 32 32 THR C C 13 175.46 0.1 . 1 . . . . . . . . 4327 1 354 . 1 1 32 32 THR CA C 13 64.44 0.1 . 1 . . . . . . . . 4327 1 355 . 1 1 32 32 THR CB C 13 68.47 0.1 . 1 . . . . . . . . 4327 1 356 . 1 1 32 32 THR CG2 C 13 21.72 0.1 . 1 . . . . . . . . 4327 1 357 . 1 1 32 32 THR N N 15 114.16 0.01 . 1 . . . . . . . . 4327 1 358 . 1 1 33 33 THR H H 1 7.72 0.03 . 1 . . . . . . . . 4327 1 359 . 1 1 33 33 THR HA H 1 4.24 0.03 . 1 . . . . . . . . 4327 1 360 . 1 1 33 33 THR HB H 1 4.37 0.03 . 1 . . . . . . . . 4327 1 361 . 1 1 33 33 THR HG21 H 1 1.15 0.03 . 1 . . . . . . . . 4327 1 362 . 1 1 33 33 THR HG22 H 1 1.15 0.03 . 1 . . . . . . . . 4327 1 363 . 1 1 33 33 THR HG23 H 1 1.15 0.03 . 1 . . . . . . . . 4327 1 364 . 1 1 33 33 THR C C 13 174.83 0.1 . 1 . . . . . . . . 4327 1 365 . 1 1 33 33 THR CA C 13 61.54 0.1 . 1 . . . . . . . . 4327 1 366 . 1 1 33 33 THR CB C 13 69.41 0.1 . 1 . . . . . . . . 4327 1 367 . 1 1 33 33 THR CG2 C 13 21.43 0.1 . 1 . . . . . . . . 4327 1 368 . 1 1 33 33 THR N N 15 111.62 0.01 . 1 . . . . . . . . 4327 1 369 . 1 1 34 34 LEU H H 1 8.24 0.03 . 1 . . . . . . . . 4327 1 370 . 1 1 34 34 LEU HA H 1 3.8 0.03 . 1 . . . . . . . . 4327 1 371 . 1 1 34 34 LEU HB2 H 1 1.55 0.03 . 2 . . . . . . . . 4327 1 372 . 1 1 34 34 LEU HB3 H 1 1.95 0.03 . 2 . . . . . . . . 4327 1 373 . 1 1 34 34 LEU HG H 1 1.46 0.03 . 1 . . . . . . . . 4327 1 374 . 1 1 34 34 LEU HD11 H 1 0.88 0.03 . 1 . . . . . . . . 4327 1 375 . 1 1 34 34 LEU HD12 H 1 0.88 0.03 . 1 . . . . . . . . 4327 1 376 . 1 1 34 34 LEU HD13 H 1 0.88 0.03 . 1 . . . . . . . . 4327 1 377 . 1 1 34 34 LEU HD21 H 1 0.78 0.03 . 1 . . . . . . . . 4327 1 378 . 1 1 34 34 LEU HD22 H 1 0.78 0.03 . 1 . . . . . . . . 4327 1 379 . 1 1 34 34 LEU HD23 H 1 0.78 0.03 . 1 . . . . . . . . 4327 1 380 . 1 1 34 34 LEU C C 13 176.19 0.1 . 1 . . . . . . . . 4327 1 381 . 1 1 34 34 LEU CA C 13 56.03 0.1 . 1 . . . . . . . . 4327 1 382 . 1 1 34 34 LEU CB C 13 38.64 0.1 . 1 . . . . . . . . 4327 1 383 . 1 1 34 34 LEU CG C 13 26.41 0.1 . 1 . . . . . . . . 4327 1 384 . 1 1 34 34 LEU CD1 C 13 25.05 0.1 . 1 . . . . . . . . 4327 1 385 . 1 1 34 34 LEU CD2 C 13 22.99 0.1 . 1 . . . . . . . . 4327 1 386 . 1 1 34 34 LEU N N 15 116.95 0.01 . 1 . . . . . . . . 4327 1 387 . 1 1 35 35 TYR H H 1 7.83 0.03 . 1 . . . . . . . . 4327 1 388 . 1 1 35 35 TYR HA H 1 4.99 0.03 . 1 . . . . . . . . 4327 1 389 . 1 1 35 35 TYR HB2 H 1 2.94 0.03 . 2 . . . . . . . . 4327 1 390 . 1 1 35 35 TYR HB3 H 1 3.02 0.03 . 2 . . . . . . . . 4327 1 391 . 1 1 35 35 TYR HD1 H 1 7.07 0.03 . 1 . . . . . . . . 4327 1 392 . 1 1 35 35 TYR HD2 H 1 7.07 0.03 . 1 . . . . . . . . 4327 1 393 . 1 1 35 35 TYR HE1 H 1 6.95 0.03 . 1 . . . . . . . . 4327 1 394 . 1 1 35 35 TYR HE2 H 1 6.95 0.03 . 1 . . . . . . . . 4327 1 395 . 1 1 35 35 TYR C C 13 175.1 0.1 . 1 . . . . . . . . 4327 1 396 . 1 1 35 35 TYR CA C 13 57.48 0.1 . 1 . . . . . . . . 4327 1 397 . 1 1 35 35 TYR CB C 13 40.87 0.1 . 1 . . . . . . . . 4327 1 398 . 1 1 35 35 TYR CD1 C 13 132.4 0.1 . 1 . . . . . . . . 4327 1 399 . 1 1 35 35 TYR CD2 C 13 132.4 0.1 . 1 . . . . . . . . 4327 1 400 . 1 1 35 35 TYR CE1 C 13 117.91 0.1 . 1 . . . . . . . . 4327 1 401 . 1 1 35 35 TYR CE2 C 13 117.91 0.1 . 1 . . . . . . . . 4327 1 402 . 1 1 35 35 TYR N N 15 117.65 0.01 . 1 . . . . . . . . 4327 1 403 . 1 1 36 36 GLN H H 1 9.82 0.03 . 1 . . . . . . . . 4327 1 404 . 1 1 36 36 GLN HA H 1 5.36 0.03 . 1 . . . . . . . . 4327 1 405 . 1 1 36 36 GLN HB2 H 1 1.68 0.03 . 2 . . . . . . . . 4327 1 406 . 1 1 36 36 GLN HB3 H 1 2.05 0.03 . 2 . . . . . . . . 4327 1 407 . 1 1 36 36 GLN HG2 H 1 1.58 0.03 . 1 . . . . . . . . 4327 1 408 . 1 1 36 36 GLN HG3 H 1 1.58 0.03 . 1 . . . . . . . . 4327 1 409 . 1 1 36 36 GLN C C 13 172.53 0.1 . 1 . . . . . . . . 4327 1 410 . 1 1 36 36 GLN CA C 13 52.29 0.1 . 1 . . . . . . . . 4327 1 411 . 1 1 36 36 GLN CB C 13 31.82 0.1 . 1 . . . . . . . . 4327 1 412 . 1 1 36 36 GLN CG C 13 32.57 0.1 . 1 . . . . . . . . 4327 1 413 . 1 1 36 36 GLN N N 15 119.74 0.01 . 1 . . . . . . . . 4327 1 414 . 1 1 37 37 ARG H H 1 8.33 0.03 . 1 . . . . . . . . 4327 1 415 . 1 1 37 37 ARG HA H 1 5.29 0.03 . 1 . . . . . . . . 4327 1 416 . 1 1 37 37 ARG HB2 H 1 0.92 0.03 . 2 . . . . . . . . 4327 1 417 . 1 1 37 37 ARG HB3 H 1 1.1 0.03 . 2 . . . . . . . . 4327 1 418 . 1 1 37 37 ARG HG2 H 1 0.78 0.03 . 2 . . . . . . . . 4327 1 419 . 1 1 37 37 ARG HG3 H 1 1.28 0.03 . 2 . . . . . . . . 4327 1 420 . 1 1 37 37 ARG HD2 H 1 1.67 0.03 . 2 . . . . . . . . 4327 1 421 . 1 1 37 37 ARG HD3 H 1 2.53 0.03 . 2 . . . . . . . . 4327 1 422 . 1 1 37 37 ARG C C 13 174.17 0.1 . 1 . . . . . . . . 4327 1 423 . 1 1 37 37 ARG CA C 13 52.69 0.1 . 1 . . . . . . . . 4327 1 424 . 1 1 37 37 ARG CB C 13 33.22 0.1 . 1 . . . . . . . . 4327 1 425 . 1 1 37 37 ARG CG C 13 25.23 0.1 . 1 . . . . . . . . 4327 1 426 . 1 1 37 37 ARG CD C 13 43.64 0.1 . 1 . . . . . . . . 4327 1 427 . 1 1 37 37 ARG N N 15 118.79 0.01 . 1 . . . . . . . . 4327 1 428 . 1 1 38 38 TYR H H 1 9.12 0.03 . 1 . . . . . . . . 4327 1 429 . 1 1 38 38 TYR N N 15 122.68 0.01 . 1 . . . . . . . . 4327 1 430 . 1 1 38 38 TYR CE2 C 13 117.57 0.1 . 1 . . . . . . . . 4327 1 431 . 1 1 38 38 TYR CE1 C 13 117.57 0.1 . 1 . . . . . . . . 4327 1 432 . 1 1 38 38 TYR CD2 C 13 132.91 0.1 . 1 . . . . . . . . 4327 1 433 . 1 1 38 38 TYR CD1 C 13 132.91 0.1 . 1 . . . . . . . . 4327 1 434 . 1 1 38 38 TYR CB C 13 39.91 0.1 . 1 . . . . . . . . 4327 1 435 . 1 1 38 38 TYR CA C 13 56.32 0.1 . 1 . . . . . . . . 4327 1 436 . 1 1 38 38 TYR C C 13 174.75 0.1 . 1 . . . . . . . . 4327 1 437 . 1 1 38 38 TYR HE2 H 1 6.8 0.03 . 1 . . . . . . . . 4327 1 438 . 1 1 38 38 TYR HE1 H 1 6.8 0.03 . 1 . . . . . . . . 4327 1 439 . 1 1 38 38 TYR HD2 H 1 7.12 0.03 . 1 . . . . . . . . 4327 1 440 . 1 1 38 38 TYR HD1 H 1 7.12 0.03 . 1 . . . . . . . . 4327 1 441 . 1 1 38 38 TYR HB3 H 1 3.01 0.03 . 2 . . . . . . . . 4327 1 442 . 1 1 38 38 TYR HB2 H 1 2.65 0.03 . 2 . . . . . . . . 4327 1 443 . 1 1 38 38 TYR HA H 1 4.51 0.03 . 1 . . . . . . . . 4327 1 444 . 1 1 39 39 GLU H H 1 9 0.03 . 1 . . . . . . . . 4327 1 445 . 1 1 39 39 GLU HA H 1 4.55 0.03 . 1 . . . . . . . . 4327 1 446 . 1 1 39 39 GLU HB2 H 1 1.79 0.03 . 2 . . . . . . . . 4327 1 447 . 1 1 39 39 GLU HB3 H 1 1.83 0.03 . 2 . . . . . . . . 4327 1 448 . 1 1 39 39 GLU HG2 H 1 2.07 0.03 . 1 . . . . . . . . 4327 1 449 . 1 1 39 39 GLU HG3 H 1 2.07 0.03 . 1 . . . . . . . . 4327 1 450 . 1 1 39 39 GLU C C 13 175.49 0.1 . 1 . . . . . . . . 4327 1 451 . 1 1 39 39 GLU CA C 13 55.46 0.1 . 1 . . . . . . . . 4327 1 452 . 1 1 39 39 GLU CB C 13 28.8 0.1 . 1 . . . . . . . . 4327 1 453 . 1 1 39 39 GLU CG C 13 35.5 0.1 . 1 . . . . . . . . 4327 1 454 . 1 1 39 39 GLU N N 15 126.1 0.01 . 1 . . . . . . . . 4327 1 455 . 1 1 40 40 ILE H H 1 8.31 0.03 . 1 . . . . . . . . 4327 1 456 . 1 1 40 40 ILE HA H 1 5.09 0.03 . 1 . . . . . . . . 4327 1 457 . 1 1 40 40 ILE HB H 1 1.09 0.03 . 1 . . . . . . . . 4327 1 458 . 1 1 40 40 ILE HG12 H 1 0.93 0.03 . 1 . . . . . . . . 4327 1 459 . 1 1 40 40 ILE HG13 H 1 0.93 0.03 . 1 . . . . . . . . 4327 1 460 . 1 1 40 40 ILE HG21 H 1 -0.21 0.03 . 1 . . . . . . . . 4327 1 461 . 1 1 40 40 ILE HG22 H 1 -0.21 0.03 . 1 . . . . . . . . 4327 1 462 . 1 1 40 40 ILE HG23 H 1 -0.21 0.03 . 1 . . . . . . . . 4327 1 463 . 1 1 40 40 ILE HD11 H 1 0.12 0.03 . 1 . . . . . . . . 4327 1 464 . 1 1 40 40 ILE HD12 H 1 0.12 0.03 . 1 . . . . . . . . 4327 1 465 . 1 1 40 40 ILE HD13 H 1 0.12 0.03 . 1 . . . . . . . . 4327 1 466 . 1 1 40 40 ILE C C 13 174.46 0.1 . 1 . . . . . . . . 4327 1 467 . 1 1 40 40 ILE CA C 13 58.04 0.1 . 1 . . . . . . . . 4327 1 468 . 1 1 40 40 ILE CB C 13 43.05 0.1 . 1 . . . . . . . . 4327 1 469 . 1 1 40 40 ILE CG1 C 13 24.48 0.1 . 1 . . . . . . . . 4327 1 470 . 1 1 40 40 ILE CG2 C 13 16.8 0.1 . 1 . . . . . . . . 4327 1 471 . 1 1 40 40 ILE CD1 C 13 14.61 0.1 . 1 . . . . . . . . 4327 1 472 . 1 1 40 40 ILE N N 15 121.35 0.01 . 1 . . . . . . . . 4327 1 473 . 1 1 41 41 LYS H H 1 8.55 0.03 . 1 . . . . . . . . 4327 1 474 . 1 1 41 41 LYS HA H 1 4.65 0.03 . 1 . . . . . . . . 4327 1 475 . 1 1 41 41 LYS HB2 H 1 1.42 0.03 . 2 . . . . . . . . 4327 1 476 . 1 1 41 41 LYS HB3 H 1 1.63 0.03 . 2 . . . . . . . . 4327 1 477 . 1 1 41 41 LYS HG2 H 1 1.12 0.03 . 2 . . . . . . . . 4327 1 478 . 1 1 41 41 LYS HG3 H 1 1.26 0.03 . 2 . . . . . . . . 4327 1 479 . 1 1 41 41 LYS HD2 H 1 1.56 0.03 . 2 . . . . . . . . 4327 1 480 . 1 1 41 41 LYS HD3 H 1 1.65 0.03 . 2 . . . . . . . . 4327 1 481 . 1 1 41 41 LYS HE2 H 1 2.88 0.03 . 1 . . . . . . . . 4327 1 482 . 1 1 41 41 LYS HE3 H 1 2.88 0.03 . 1 . . . . . . . . 4327 1 483 . 1 1 41 41 LYS C C 13 175.34 0.1 . 1 . . . . . . . . 4327 1 484 . 1 1 41 41 LYS CA C 13 53.29 0.1 . 1 . . . . . . . . 4327 1 485 . 1 1 41 41 LYS CB C 13 33.93 0.1 . 1 . . . . . . . . 4327 1 486 . 1 1 41 41 LYS CG C 13 24.28 0.1 . 1 . . . . . . . . 4327 1 487 . 1 1 41 41 LYS CD C 13 28.53 0.1 . 1 . . . . . . . . 4327 1 488 . 1 1 41 41 LYS CE C 13 42 0.1 . 1 . . . . . . . . 4327 1 489 . 1 1 41 41 LYS N N 15 120.82 0.01 . 1 . . . . . . . . 4327 1 490 . 1 1 42 42 MET H H 1 9.57 0.03 . 1 . . . . . . . . 4327 1 491 . 1 1 42 42 MET HA H 1 4.31 0.03 . 1 . . . . . . . . 4327 1 492 . 1 1 42 42 MET HB2 H 1 1.88 0.03 . 2 . . . . . . . . 4327 1 493 . 1 1 42 42 MET HB3 H 1 2.24 0.03 . 2 . . . . . . . . 4327 1 494 . 1 1 42 42 MET HG2 H 1 2.46 0.03 . 1 . . . . . . . . 4327 1 495 . 1 1 42 42 MET HG3 H 1 2.46 0.03 . 1 . . . . . . . . 4327 1 496 . 1 1 42 42 MET C C 13 175.92 0.1 . 1 . . . . . . . . 4327 1 497 . 1 1 42 42 MET CA C 13 56.18 0.1 . 1 . . . . . . . . 4327 1 498 . 1 1 42 42 MET CB C 13 33.71 0.1 . 1 . . . . . . . . 4327 1 499 . 1 1 42 42 MET CG C 13 32.05 0.1 . 1 . . . . . . . . 4327 1 500 . 1 1 42 42 MET N N 15 129.25 0.01 . 1 . . . . . . . . 4327 1 501 . 1 1 43 43 THR H H 1 9.2 0.03 . 1 . . . . . . . . 4327 1 502 . 1 1 43 43 THR HA H 1 4.33 0.03 . 1 . . . . . . . . 4327 1 503 . 1 1 43 43 THR HB H 1 4.02 0.03 . 1 . . . . . . . . 4327 1 504 . 1 1 43 43 THR HG21 H 1 0.98 0.03 . 1 . . . . . . . . 4327 1 505 . 1 1 43 43 THR HG22 H 1 0.98 0.03 . 1 . . . . . . . . 4327 1 506 . 1 1 43 43 THR HG23 H 1 0.98 0.03 . 1 . . . . . . . . 4327 1 507 . 1 1 43 43 THR C C 13 175.32 0.1 . 1 . . . . . . . . 4327 1 508 . 1 1 43 43 THR CA C 13 61.61 0.1 . 1 . . . . . . . . 4327 1 509 . 1 1 43 43 THR CB C 13 68.24 0.1 . 1 . . . . . . . . 4327 1 510 . 1 1 43 43 THR CG2 C 13 22.45 0.1 . 1 . . . . . . . . 4327 1 511 . 1 1 43 43 THR N N 15 120.6 0.01 . 1 . . . . . . . . 4327 1 512 . 1 1 44 44 LYS H H 1 7.3 0.03 . 1 . . . . . . . . 4327 1 513 . 1 1 44 44 LYS HA H 1 4.24 0.03 . 1 . . . . . . . . 4327 1 514 . 1 1 44 44 LYS HB2 H 1 0.94 0.03 . 2 . . . . . . . . 4327 1 515 . 1 1 44 44 LYS HB3 H 1 1.39 0.03 . 2 . . . . . . . . 4327 1 516 . 1 1 44 44 LYS HG2 H 1 0.73 0.03 . 2 . . . . . . . . 4327 1 517 . 1 1 44 44 LYS HG3 H 1 0.87 0.03 . 2 . . . . . . . . 4327 1 518 . 1 1 44 44 LYS HD2 H 1 1.57 0.03 . 1 . . . . . . . . 4327 1 519 . 1 1 44 44 LYS HD3 H 1 1.57 0.03 . 1 . . . . . . . . 4327 1 520 . 1 1 44 44 LYS HE2 H 1 2.83 0.03 . 2 . . . . . . . . 4327 1 521 . 1 1 44 44 LYS HE3 H 1 2.9 0.03 . 2 . . . . . . . . 4327 1 522 . 1 1 44 44 LYS C C 13 172.82 0.1 . 1 . . . . . . . . 4327 1 523 . 1 1 44 44 LYS CA C 13 55.15 0.1 . 1 . . . . . . . . 4327 1 524 . 1 1 44 44 LYS CB C 13 35.84 0.1 . 1 . . . . . . . . 4327 1 525 . 1 1 44 44 LYS CG C 13 24.08 0.1 . 1 . . . . . . . . 4327 1 526 . 1 1 44 44 LYS CD C 13 27.98 0.1 . 1 . . . . . . . . 4327 1 527 . 1 1 44 44 LYS CE C 13 41.97 0.1 . 1 . . . . . . . . 4327 1 528 . 1 1 44 44 LYS N N 15 121.35 0.01 . 1 . . . . . . . . 4327 1 529 . 1 1 45 45 MET H H 1 8.72 0.03 . 1 . . . . . . . . 4327 1 530 . 1 1 45 45 MET HA H 1 4.58 0.03 . 1 . . . . . . . . 4327 1 531 . 1 1 45 45 MET HB2 H 1 1.47 0.03 . 2 . . . . . . . . 4327 1 532 . 1 1 45 45 MET HB3 H 1 1.88 0.03 . 2 . . . . . . . . 4327 1 533 . 1 1 45 45 MET HG2 H 1 1.98 0.03 . 1 . . . . . . . . 4327 1 534 . 1 1 45 45 MET HG3 H 1 1.98 0.03 . 1 . . . . . . . . 4327 1 535 . 1 1 45 45 MET C C 13 173.28 0.1 . 1 . . . . . . . . 4327 1 536 . 1 1 45 45 MET CA C 13 54.92 0.1 . 1 . . . . . . . . 4327 1 537 . 1 1 45 45 MET CB C 13 34.65 0.1 . 1 . . . . . . . . 4327 1 538 . 1 1 45 45 MET CG C 13 31.82 0.1 . 1 . . . . . . . . 4327 1 539 . 1 1 45 45 MET N N 15 125.27 0.01 . 1 . . . . . . . . 4327 1 540 . 1 1 46 46 TYR H H 1 8.67 0.03 . 1 . . . . . . . . 4327 1 541 . 1 1 46 46 TYR HA H 1 5.09 0.03 . 1 . . . . . . . . 4327 1 542 . 1 1 46 46 TYR HB2 H 1 2.49 0.03 . 2 . . . . . . . . 4327 1 543 . 1 1 46 46 TYR HB3 H 1 3.84 0.03 . 2 . . . . . . . . 4327 1 544 . 1 1 46 46 TYR HD1 H 1 6.98 0.03 . 1 . . . . . . . . 4327 1 545 . 1 1 46 46 TYR HD2 H 1 6.98 0.03 . 1 . . . . . . . . 4327 1 546 . 1 1 46 46 TYR HE1 H 1 6.39 0.03 . 1 . . . . . . . . 4327 1 547 . 1 1 46 46 TYR HE2 H 1 6.39 0.03 . 1 . . . . . . . . 4327 1 548 . 1 1 46 46 TYR C C 13 175.31 0.1 . 1 . . . . . . . . 4327 1 549 . 1 1 46 46 TYR CA C 13 57.89 0.1 . 1 . . . . . . . . 4327 1 550 . 1 1 46 46 TYR CB C 13 40.11 0.1 . 1 . . . . . . . . 4327 1 551 . 1 1 46 46 TYR CD1 C 13 131.64 0.1 . 1 . . . . . . . . 4327 1 552 . 1 1 46 46 TYR CD2 C 13 131.64 0.1 . 1 . . . . . . . . 4327 1 553 . 1 1 46 46 TYR CE1 C 13 117.52 0.1 . 1 . . . . . . . . 4327 1 554 . 1 1 46 46 TYR CE2 C 13 117.52 0.1 . 1 . . . . . . . . 4327 1 555 . 1 1 46 46 TYR N N 15 123.59 0.01 . 1 . . . . . . . . 4327 1 556 . 1 1 47 47 LYS H H 1 7.96 0.03 . 1 . . . . . . . . 4327 1 557 . 1 1 47 47 LYS HA H 1 4.42 0.03 . 1 . . . . . . . . 4327 1 558 . 1 1 47 47 LYS HB2 H 1 0.93 0.03 . 2 . . . . . . . . 4327 1 559 . 1 1 47 47 LYS HB3 H 1 1.71 0.03 . 2 . . . . . . . . 4327 1 560 . 1 1 47 47 LYS HG2 H 1 0.81 0.03 . 2 . . . . . . . . 4327 1 561 . 1 1 47 47 LYS HG3 H 1 1.16 0.03 . 2 . . . . . . . . 4327 1 562 . 1 1 47 47 LYS HD2 H 1 1.44 0.03 . 1 . . . . . . . . 4327 1 563 . 1 1 47 47 LYS HD3 H 1 1.44 0.03 . 1 . . . . . . . . 4327 1 564 . 1 1 47 47 LYS HE2 H 1 2.88 0.03 . 2 . . . . . . . . 4327 1 565 . 1 1 47 47 LYS HE3 H 1 2.94 0.03 . 2 . . . . . . . . 4327 1 566 . 1 1 47 47 LYS C C 13 174.46 0.1 . 1 . . . . . . . . 4327 1 567 . 1 1 47 47 LYS CA C 13 56.61 0.1 . 1 . . . . . . . . 4327 1 568 . 1 1 47 47 LYS CB C 13 36.61 0.1 . 1 . . . . . . . . 4327 1 569 . 1 1 47 47 LYS CG C 13 24.76 0.1 . 1 . . . . . . . . 4327 1 570 . 1 1 47 47 LYS CE C 13 42.18 0.1 . 1 . . . . . . . . 4327 1 571 . 1 1 47 47 LYS N N 15 121.55 0.01 . 1 . . . . . . . . 4327 1 572 . 1 1 48 48 GLY H H 1 9.09 0.03 . 1 . . . . . . . . 4327 1 573 . 1 1 48 48 GLY HA2 H 1 3.81 0.03 . 2 . . . . . . . . 4327 1 574 . 1 1 48 48 GLY HA3 H 1 4.69 0.03 . 2 . . . . . . . . 4327 1 575 . 1 1 48 48 GLY C C 13 174.17 0.1 . 1 . . . . . . . . 4327 1 576 . 1 1 48 48 GLY CA C 13 45.77 0.1 . 1 . . . . . . . . 4327 1 577 . 1 1 48 48 GLY N N 15 114.7 0.01 . 1 . . . . . . . . 4327 1 578 . 1 1 49 49 PHE H H 1 7.16 0.03 . 1 . . . . . . . . 4327 1 579 . 1 1 49 49 PHE HA H 1 4.13 0.03 . 1 . . . . . . . . 4327 1 580 . 1 1 49 49 PHE HB2 H 1 2.97 0.03 . 2 . . . . . . . . 4327 1 581 . 1 1 49 49 PHE HB3 H 1 3.29 0.03 . 2 . . . . . . . . 4327 1 582 . 1 1 49 49 PHE HD1 H 1 7.37 0.03 . 1 . . . . . . . . 4327 1 583 . 1 1 49 49 PHE HD2 H 1 7.37 0.03 . 1 . . . . . . . . 4327 1 584 . 1 1 49 49 PHE HE1 H 1 7.46 0.03 . 1 . . . . . . . . 4327 1 585 . 1 1 49 49 PHE HE2 H 1 7.46 0.03 . 1 . . . . . . . . 4327 1 586 . 1 1 49 49 PHE C C 13 177.71 0.1 . 1 . . . . . . . . 4327 1 587 . 1 1 49 49 PHE CA C 13 59.41 0.1 . 1 . . . . . . . . 4327 1 588 . 1 1 49 49 PHE CB C 13 38.68 0.1 . 1 . . . . . . . . 4327 1 589 . 1 1 49 49 PHE CD1 C 13 130.39 0.1 . 1 . . . . . . . . 4327 1 590 . 1 1 49 49 PHE CD2 C 13 130.39 0.1 . 1 . . . . . . . . 4327 1 591 . 1 1 49 49 PHE N N 15 119.66 0.01 . 1 . . . . . . . . 4327 1 592 . 1 1 50 50 GLN H H 1 8.78 0.03 . 1 . . . . . . . . 4327 1 593 . 1 1 50 50 GLN HA H 1 4.24 0.03 . 1 . . . . . . . . 4327 1 594 . 1 1 50 50 GLN HB2 H 1 2.12 0.03 . 2 . . . . . . . . 4327 1 595 . 1 1 50 50 GLN HB3 H 1 2.16 0.03 . 2 . . . . . . . . 4327 1 596 . 1 1 50 50 GLN HG2 H 1 2.45 0.03 . 1 . . . . . . . . 4327 1 597 . 1 1 50 50 GLN HG3 H 1 2.45 0.03 . 1 . . . . . . . . 4327 1 598 . 1 1 50 50 GLN HE21 H 1 7.69 0.03 . 2 . . . . . . . . 4327 1 599 . 1 1 50 50 GLN HE22 H 1 7.04 0.03 . 2 . . . . . . . . 4327 1 600 . 1 1 50 50 GLN C C 13 176.59 0.1 . 1 . . . . . . . . 4327 1 601 . 1 1 50 50 GLN CA C 13 57.4 0.1 . 1 . . . . . . . . 4327 1 602 . 1 1 50 50 GLN CB C 13 27.49 0.1 . 1 . . . . . . . . 4327 1 603 . 1 1 50 50 GLN CG C 13 33.97 0.1 . 1 . . . . . . . . 4327 1 604 . 1 1 50 50 GLN N N 15 118.23 0.01 . 1 . . . . . . . . 4327 1 605 . 1 1 50 50 GLN NE2 N 15 113.28 0.01 . 1 . . . . . . . . 4327 1 606 . 1 1 51 51 ALA H H 1 7.71 0.03 . 1 . . . . . . . . 4327 1 607 . 1 1 51 51 ALA HA H 1 4.24 0.03 . 1 . . . . . . . . 4327 1 608 . 1 1 51 51 ALA HB1 H 1 1.36 0.03 . 1 . . . . . . . . 4327 1 609 . 1 1 51 51 ALA HB2 H 1 1.36 0.03 . 1 . . . . . . . . 4327 1 610 . 1 1 51 51 ALA HB3 H 1 1.36 0.03 . 1 . . . . . . . . 4327 1 611 . 1 1 51 51 ALA C C 13 178.19 0.1 . 1 . . . . . . . . 4327 1 612 . 1 1 51 51 ALA CA C 13 53.28 0.1 . 1 . . . . . . . . 4327 1 613 . 1 1 51 51 ALA CB C 13 18.89 0.1 . 1 . . . . . . . . 4327 1 614 . 1 1 51 51 ALA N N 15 122.5 0.01 . 1 . . . . . . . . 4327 1 615 . 1 1 52 52 LEU H H 1 7.71 0.03 . 1 . . . . . . . . 4327 1 616 . 1 1 52 52 LEU HA H 1 4.35 0.03 . 1 . . . . . . . . 4327 1 617 . 1 1 52 52 LEU HB2 H 1 1.57 0.03 . 2 . . . . . . . . 4327 1 618 . 1 1 52 52 LEU HB3 H 1 2.33 0.03 . 2 . . . . . . . . 4327 1 619 . 1 1 52 52 LEU HG H 1 1.57 0.03 . 1 . . . . . . . . 4327 1 620 . 1 1 52 52 LEU HD11 H 1 0.8 0.03 . 1 . . . . . . . . 4327 1 621 . 1 1 52 52 LEU HD12 H 1 0.8 0.03 . 1 . . . . . . . . 4327 1 622 . 1 1 52 52 LEU HD13 H 1 0.8 0.03 . 1 . . . . . . . . 4327 1 623 . 1 1 52 52 LEU HD21 H 1 0.8 0.03 . 1 . . . . . . . . 4327 1 624 . 1 1 52 52 LEU HD22 H 1 0.8 0.03 . 1 . . . . . . . . 4327 1 625 . 1 1 52 52 LEU HD23 H 1 0.8 0.03 . 1 . . . . . . . . 4327 1 626 . 1 1 52 52 LEU C C 13 177.64 0.1 . 1 . . . . . . . . 4327 1 627 . 1 1 52 52 LEU CA C 13 54.66 0.1 . 1 . . . . . . . . 4327 1 628 . 1 1 52 52 LEU CB C 13 43.02 0.1 . 1 . . . . . . . . 4327 1 629 . 1 1 52 52 LEU CG C 13 26.45 0.1 . 1 . . . . . . . . 4327 1 630 . 1 1 52 52 LEU CD1 C 13 25.83 0.1 . 1 . . . . . . . . 4327 1 631 . 1 1 52 52 LEU CD2 C 13 22.94 0.1 . 1 . . . . . . . . 4327 1 632 . 1 1 52 52 LEU N N 15 116.36 0.01 . 1 . . . . . . . . 4327 1 633 . 1 1 53 53 GLY H H 1 7.93 0.03 . 1 . . . . . . . . 4327 1 634 . 1 1 53 53 GLY HA2 H 1 3.85 0.03 . 2 . . . . . . . . 4327 1 635 . 1 1 53 53 GLY HA3 H 1 4.08 0.03 . 2 . . . . . . . . 4327 1 636 . 1 1 53 53 GLY C C 13 173.84 0.1 . 1 . . . . . . . . 4327 1 637 . 1 1 53 53 GLY CA C 13 45.32 0.1 . 1 . . . . . . . . 4327 1 638 . 1 1 53 53 GLY N N 15 109.12 0.01 . 1 . . . . . . . . 4327 1 639 . 1 1 54 54 ASP H H 1 8.34 0.03 . 1 . . . . . . . . 4327 1 640 . 1 1 54 54 ASP HA H 1 4.52 0.03 . 1 . . . . . . . . 4327 1 641 . 1 1 54 54 ASP HB2 H 1 2.65 0.03 . 1 . . . . . . . . 4327 1 642 . 1 1 54 54 ASP HB3 H 1 2.65 0.03 . 1 . . . . . . . . 4327 1 643 . 1 1 54 54 ASP C C 13 176.15 0.1 . 1 . . . . . . . . 4327 1 644 . 1 1 54 54 ASP CA C 13 54.79 0.1 . 1 . . . . . . . . 4327 1 645 . 1 1 54 54 ASP CB C 13 40.62 0.1 . 1 . . . . . . . . 4327 1 646 . 1 1 54 54 ASP N N 15 120.82 0.01 . 1 . . . . . . . . 4327 1 647 . 1 1 55 55 ALA H H 1 8.14 0.03 . 1 . . . . . . . . 4327 1 648 . 1 1 55 55 ALA HA H 1 4.37 0.03 . 1 . . . . . . . . 4327 1 649 . 1 1 55 55 ALA HB1 H 1 1.37 0.03 . 1 . . . . . . . . 4327 1 650 . 1 1 55 55 ALA HB2 H 1 1.37 0.03 . 1 . . . . . . . . 4327 1 651 . 1 1 55 55 ALA HB3 H 1 1.37 0.03 . 1 . . . . . . . . 4327 1 652 . 1 1 55 55 ALA C C 13 176.58 0.1 . 1 . . . . . . . . 4327 1 653 . 1 1 55 55 ALA CA C 13 51.73 0.1 . 1 . . . . . . . . 4327 1 654 . 1 1 55 55 ALA CB C 13 18.38 0.1 . 1 . . . . . . . . 4327 1 655 . 1 1 55 55 ALA N N 15 123.83 0.01 . 1 . . . . . . . . 4327 1 656 . 1 1 56 56 ALA H H 1 7.69 0.03 . 1 . . . . . . . . 4327 1 657 . 1 1 56 56 ALA HA H 1 4.12 0.03 . 1 . . . . . . . . 4327 1 658 . 1 1 56 56 ALA HB1 H 1 1.3 0.03 . 1 . . . . . . . . 4327 1 659 . 1 1 56 56 ALA HB2 H 1 1.3 0.03 . 1 . . . . . . . . 4327 1 660 . 1 1 56 56 ALA HB3 H 1 1.3 0.03 . 1 . . . . . . . . 4327 1 661 . 1 1 56 56 ALA C C 13 176.17 0.1 . 1 . . . . . . . . 4327 1 662 . 1 1 56 56 ALA CA C 13 52.56 0.1 . 1 . . . . . . . . 4327 1 663 . 1 1 56 56 ALA CB C 13 19.47 0.1 . 1 . . . . . . . . 4327 1 664 . 1 1 56 56 ALA N N 15 121.83 0.01 . 1 . . . . . . . . 4327 1 665 . 1 1 57 57 ASP H H 1 8.08 0.03 . 1 . . . . . . . . 4327 1 666 . 1 1 57 57 ASP HA H 1 4.63 0.03 . 1 . . . . . . . . 4327 1 667 . 1 1 57 57 ASP HB2 H 1 2.54 0.03 . 2 . . . . . . . . 4327 1 668 . 1 1 57 57 ASP HB3 H 1 2.63 0.03 . 2 . . . . . . . . 4327 1 669 . 1 1 57 57 ASP C C 13 174.77 0.1 . 1 . . . . . . . . 4327 1 670 . 1 1 57 57 ASP CA C 13 53.06 0.1 . 1 . . . . . . . . 4327 1 671 . 1 1 57 57 ASP CB C 13 41.59 0.1 . 1 . . . . . . . . 4327 1 672 . 1 1 57 57 ASP N N 15 119.08 0.01 . 1 . . . . . . . . 4327 1 673 . 1 1 58 58 ILE H H 1 7.55 0.03 . 1 . . . . . . . . 4327 1 674 . 1 1 58 58 ILE HA H 1 4.15 0.03 . 1 . . . . . . . . 4327 1 675 . 1 1 58 58 ILE HB H 1 1.72 0.03 . 1 . . . . . . . . 4327 1 676 . 1 1 58 58 ILE HG12 H 1 1.21 0.03 . 2 . . . . . . . . 4327 1 677 . 1 1 58 58 ILE HG13 H 1 1.37 0.03 . 2 . . . . . . . . 4327 1 678 . 1 1 58 58 ILE HG21 H 1 0.85 0.03 . 1 . . . . . . . . 4327 1 679 . 1 1 58 58 ILE HG22 H 1 0.85 0.03 . 1 . . . . . . . . 4327 1 680 . 1 1 58 58 ILE HG23 H 1 0.85 0.03 . 1 . . . . . . . . 4327 1 681 . 1 1 58 58 ILE HD11 H 1 0.8 0.03 . 1 . . . . . . . . 4327 1 682 . 1 1 58 58 ILE HD12 H 1 0.8 0.03 . 1 . . . . . . . . 4327 1 683 . 1 1 58 58 ILE HD13 H 1 0.8 0.03 . 1 . . . . . . . . 4327 1 684 . 1 1 58 58 ILE C C 13 174.43 0.1 . 1 . . . . . . . . 4327 1 685 . 1 1 58 58 ILE CA C 13 60.33 0.1 . 1 . . . . . . . . 4327 1 686 . 1 1 58 58 ILE CB C 13 37.97 0.1 . 1 . . . . . . . . 4327 1 687 . 1 1 58 58 ILE CG1 C 13 27.12 0.1 . 1 . . . . . . . . 4327 1 688 . 1 1 58 58 ILE CG2 C 13 17.96 0.1 . 1 . . . . . . . . 4327 1 689 . 1 1 58 58 ILE CD1 C 13 13.08 0.1 . 1 . . . . . . . . 4327 1 690 . 1 1 58 58 ILE N N 15 123.72 0.01 . 1 . . . . . . . . 4327 1 691 . 1 1 59 59 ARG H H 1 8.61 0.03 . 1 . . . . . . . . 4327 1 692 . 1 1 59 59 ARG HA H 1 4.4 0.03 . 1 . . . . . . . . 4327 1 693 . 1 1 59 59 ARG HB2 H 1 1.49 0.03 . 1 . . . . . . . . 4327 1 694 . 1 1 59 59 ARG HB3 H 1 1.49 0.03 . 1 . . . . . . . . 4327 1 695 . 1 1 59 59 ARG HG2 H 1 1.21 0.03 . 2 . . . . . . . . 4327 1 696 . 1 1 59 59 ARG HG3 H 1 1.41 0.03 . 2 . . . . . . . . 4327 1 697 . 1 1 59 59 ARG HD2 H 1 3.09 0.03 . 1 . . . . . . . . 4327 1 698 . 1 1 59 59 ARG HD3 H 1 3.09 0.03 . 1 . . . . . . . . 4327 1 699 . 1 1 59 59 ARG C C 13 174.04 0.1 . 1 . . . . . . . . 4327 1 700 . 1 1 59 59 ARG CA C 13 55.39 0.1 . 1 . . . . . . . . 4327 1 701 . 1 1 59 59 ARG CB C 13 32.41 0.1 . 1 . . . . . . . . 4327 1 702 . 1 1 59 59 ARG CG C 13 27.35 0.1 . 1 . . . . . . . . 4327 1 703 . 1 1 59 59 ARG CD C 13 43.26 0.1 . 1 . . . . . . . . 4327 1 704 . 1 1 59 59 ARG N N 15 125.25 0.01 . 1 . . . . . . . . 4327 1 705 . 1 1 60 60 PHE H H 1 7.12 0.03 . 1 . . . . . . . . 4327 1 706 . 1 1 60 60 PHE HA H 1 5.66 0.03 . 1 . . . . . . . . 4327 1 707 . 1 1 60 60 PHE HB2 H 1 2.48 0.03 . 2 . . . . . . . . 4327 1 708 . 1 1 60 60 PHE HB3 H 1 2.66 0.03 . 2 . . . . . . . . 4327 1 709 . 1 1 60 60 PHE HD1 H 1 6.96 0.03 . 1 . . . . . . . . 4327 1 710 . 1 1 60 60 PHE HD2 H 1 6.96 0.03 . 1 . . . . . . . . 4327 1 711 . 1 1 60 60 PHE HE1 H 1 7.19 0.03 . 1 . . . . . . . . 4327 1 712 . 1 1 60 60 PHE HE2 H 1 7.19 0.03 . 1 . . . . . . . . 4327 1 713 . 1 1 60 60 PHE C C 13 174.38 0.1 . 1 . . . . . . . . 4327 1 714 . 1 1 60 60 PHE CA C 13 55.6 0.1 . 1 . . . . . . . . 4327 1 715 . 1 1 60 60 PHE CB C 13 45.09 0.1 . 1 . . . . . . . . 4327 1 716 . 1 1 60 60 PHE CD1 C 13 131.54 0.1 . 1 . . . . . . . . 4327 1 717 . 1 1 60 60 PHE CD2 C 13 131.54 0.1 . 1 . . . . . . . . 4327 1 718 . 1 1 60 60 PHE CE1 C 13 130.54 0.1 . 1 . . . . . . . . 4327 1 719 . 1 1 60 60 PHE CE2 C 13 130.54 0.1 . 1 . . . . . . . . 4327 1 720 . 1 1 60 60 PHE N N 15 113.8 0.01 . 1 . . . . . . . . 4327 1 721 . 1 1 61 61 VAL H H 1 8.62 0.03 . 1 . . . . . . . . 4327 1 722 . 1 1 61 61 VAL HA H 1 4.79 0.03 . 1 . . . . . . . . 4327 1 723 . 1 1 61 61 VAL HB H 1 1.69 0.03 . 1 . . . . . . . . 4327 1 724 . 1 1 61 61 VAL HG11 H 1 0.74 0.03 . 1 . . . . . . . . 4327 1 725 . 1 1 61 61 VAL HG12 H 1 0.74 0.03 . 1 . . . . . . . . 4327 1 726 . 1 1 61 61 VAL HG13 H 1 0.74 0.03 . 1 . . . . . . . . 4327 1 727 . 1 1 61 61 VAL HG21 H 1 0.74 0.03 . 1 . . . . . . . . 4327 1 728 . 1 1 61 61 VAL HG22 H 1 0.74 0.03 . 1 . . . . . . . . 4327 1 729 . 1 1 61 61 VAL HG23 H 1 0.74 0.03 . 1 . . . . . . . . 4327 1 730 . 1 1 61 61 VAL C C 13 172.87 0.1 . 1 . . . . . . . . 4327 1 731 . 1 1 61 61 VAL CA C 13 59.6 0.1 . 1 . . . . . . . . 4327 1 732 . 1 1 61 61 VAL CB C 13 34.67 0.1 . 1 . . . . . . . . 4327 1 733 . 1 1 61 61 VAL CG1 C 13 21.42 0.1 . 1 . . . . . . . . 4327 1 734 . 1 1 61 61 VAL CG2 C 13 22.39 0.1 . 1 . . . . . . . . 4327 1 735 . 1 1 61 61 VAL N N 15 117.22 0.01 . 1 . . . . . . . . 4327 1 736 . 1 1 62 62 TYR H H 1 9.15 0.03 . 1 . . . . . . . . 4327 1 737 . 1 1 62 62 TYR HA H 1 5.23 0.03 . 1 . . . . . . . . 4327 1 738 . 1 1 62 62 TYR HB2 H 1 1.78 0.03 . 2 . . . . . . . . 4327 1 739 . 1 1 62 62 TYR HB3 H 1 2.22 0.03 . 2 . . . . . . . . 4327 1 740 . 1 1 62 62 TYR HD1 H 1 6.92 0.03 . 1 . . . . . . . . 4327 1 741 . 1 1 62 62 TYR HD2 H 1 6.92 0.03 . 1 . . . . . . . . 4327 1 742 . 1 1 62 62 TYR HE1 H 1 6.68 0.03 . 1 . . . . . . . . 4327 1 743 . 1 1 62 62 TYR HE2 H 1 6.68 0.03 . 1 . . . . . . . . 4327 1 744 . 1 1 62 62 TYR C C 13 174.55 0.1 . 1 . . . . . . . . 4327 1 745 . 1 1 62 62 TYR CA C 13 57.15 0.1 . 1 . . . . . . . . 4327 1 746 . 1 1 62 62 TYR CB C 13 40.3 0.1 . 1 . . . . . . . . 4327 1 747 . 1 1 62 62 TYR CD1 C 13 132.32 0.1 . 1 . . . . . . . . 4327 1 748 . 1 1 62 62 TYR CD2 C 13 132.32 0.1 . 1 . . . . . . . . 4327 1 749 . 1 1 62 62 TYR CE1 C 13 118.53 0.1 . 1 . . . . . . . . 4327 1 750 . 1 1 62 62 TYR CE2 C 13 118.53 0.1 . 1 . . . . . . . . 4327 1 751 . 1 1 62 62 TYR N N 15 125.97 0.01 . 1 . . . . . . . . 4327 1 752 . 1 1 63 63 THR H H 1 8.98 0.03 . 1 . . . . . . . . 4327 1 753 . 1 1 63 63 THR HA H 1 5.71 0.03 . 1 . . . . . . . . 4327 1 754 . 1 1 63 63 THR HB H 1 4.33 0.03 . 1 . . . . . . . . 4327 1 755 . 1 1 63 63 THR HG21 H 1 1.64 0.03 . 1 . . . . . . . . 4327 1 756 . 1 1 63 63 THR HG22 H 1 1.64 0.03 . 1 . . . . . . . . 4327 1 757 . 1 1 63 63 THR HG23 H 1 1.64 0.03 . 1 . . . . . . . . 4327 1 758 . 1 1 63 63 THR CA C 13 58.96 0.1 . 1 . . . . . . . . 4327 1 759 . 1 1 63 63 THR CB C 13 72.53 0.1 . 1 . . . . . . . . 4327 1 760 . 1 1 63 63 THR CG2 C 13 19.35 0.1 . 1 . . . . . . . . 4327 1 761 . 1 1 63 63 THR N N 15 115.41 0.01 . 1 . . . . . . . . 4327 1 762 . 1 1 64 64 PRO HA H 1 4.1 0.03 . 1 . . . . . . . . 4327 1 763 . 1 1 64 64 PRO HB2 H 1 2.23 0.03 . 2 . . . . . . . . 4327 1 764 . 1 1 64 64 PRO HB3 H 1 2.52 0.03 . 2 . . . . . . . . 4327 1 765 . 1 1 64 64 PRO HG2 H 1 1.58 0.03 . 2 . . . . . . . . 4327 1 766 . 1 1 64 64 PRO HG3 H 1 1.92 0.03 . 2 . . . . . . . . 4327 1 767 . 1 1 64 64 PRO HD2 H 1 3.94 0.03 . 1 . . . . . . . . 4327 1 768 . 1 1 64 64 PRO HD3 H 1 3.94 0.03 . 1 . . . . . . . . 4327 1 769 . 1 1 64 64 PRO C C 13 174.6 0.1 . 1 . . . . . . . . 4327 1 770 . 1 1 64 64 PRO CA C 13 64.06 0.1 . 1 . . . . . . . . 4327 1 771 . 1 1 64 64 PRO CB C 13 32.29 0.1 . 1 . . . . . . . . 4327 1 772 . 1 1 64 64 PRO CD C 13 51.85 0.1 . 1 . . . . . . . . 4327 1 773 . 1 1 65 65 ALA H H 1 8.1 0.03 . 1 . . . . . . . . 4327 1 774 . 1 1 65 65 ALA HA H 1 4.07 0.03 . 1 . . . . . . . . 4327 1 775 . 1 1 65 65 ALA HB1 H 1 1.11 0.03 . 1 . . . . . . . . 4327 1 776 . 1 1 65 65 ALA HB2 H 1 1.11 0.03 . 1 . . . . . . . . 4327 1 777 . 1 1 65 65 ALA HB3 H 1 1.11 0.03 . 1 . . . . . . . . 4327 1 778 . 1 1 65 65 ALA C C 13 175.61 0.1 . 1 . . . . . . . . 4327 1 779 . 1 1 65 65 ALA CA C 13 52.1 0.1 . 1 . . . . . . . . 4327 1 780 . 1 1 65 65 ALA CB C 13 18.7 0.1 . 1 . . . . . . . . 4327 1 781 . 1 1 65 65 ALA N N 15 120.15 0.01 . 1 . . . . . . . . 4327 1 782 . 1 1 66 66 MET H H 1 6.95 0.03 . 1 . . . . . . . . 4327 1 783 . 1 1 66 66 MET HA H 1 5.01 0.03 . 1 . . . . . . . . 4327 1 784 . 1 1 66 66 MET HB2 H 1 1.99 0.03 . 2 . . . . . . . . 4327 1 785 . 1 1 66 66 MET HB3 H 1 2.31 0.03 . 2 . . . . . . . . 4327 1 786 . 1 1 66 66 MET HG2 H 1 2.59 0.03 . 1 . . . . . . . . 4327 1 787 . 1 1 66 66 MET HG3 H 1 2.59 0.03 . 1 . . . . . . . . 4327 1 788 . 1 1 66 66 MET CA C 13 54 0.1 . 1 . . . . . . . . 4327 1 789 . 1 1 66 66 MET CB C 13 34.75 0.1 . 1 . . . . . . . . 4327 1 790 . 1 1 66 66 MET CG C 13 31.82 0.1 . 1 . . . . . . . . 4327 1 791 . 1 1 66 66 MET N N 15 112.61 0.01 . 1 . . . . . . . . 4327 1 792 . 1 1 67 67 GLU HG2 H 1 2.05 0.03 . 1 . . . . . . . . 4327 1 793 . 1 1 67 67 GLU HG3 H 1 2.05 0.03 . 1 . . . . . . . . 4327 1 794 . 1 1 67 67 GLU CG C 13 36.33 0.1 . 1 . . . . . . . . 4327 1 795 . 1 1 69 69 VAL HA H 1 4.78 0.03 . 1 . . . . . . . . 4327 1 796 . 1 1 69 69 VAL HB H 1 2.52 0.03 . 1 . . . . . . . . 4327 1 797 . 1 1 69 69 VAL HG11 H 1 0.98 0.03 . 1 . . . . . . . . 4327 1 798 . 1 1 69 69 VAL HG12 H 1 0.98 0.03 . 1 . . . . . . . . 4327 1 799 . 1 1 69 69 VAL HG13 H 1 0.98 0.03 . 1 . . . . . . . . 4327 1 800 . 1 1 69 69 VAL HG21 H 1 0.96 0.03 . 1 . . . . . . . . 4327 1 801 . 1 1 69 69 VAL HG22 H 1 0.96 0.03 . 1 . . . . . . . . 4327 1 802 . 1 1 69 69 VAL HG23 H 1 0.96 0.03 . 1 . . . . . . . . 4327 1 803 . 1 1 69 69 VAL C C 13 174.75 0.1 . 1 . . . . . . . . 4327 1 804 . 1 1 69 69 VAL CA C 13 60.12 0.1 . 1 . . . . . . . . 4327 1 805 . 1 1 69 69 VAL CB C 13 29.37 0.1 . 1 . . . . . . . . 4327 1 806 . 1 1 69 69 VAL CG1 C 13 21.56 0.1 . 1 . . . . . . . . 4327 1 807 . 1 1 69 69 VAL CG2 C 13 20.27 0.1 . 1 . . . . . . . . 4327 1 808 . 1 1 70 70 CYS H H 1 8.05 0.03 . 1 . . . . . . . . 4327 1 809 . 1 1 70 70 CYS HA H 1 4.53 0.03 . 1 . . . . . . . . 4327 1 810 . 1 1 70 70 CYS HB2 H 1 3.66 0.03 . 1 . . . . . . . . 4327 1 811 . 1 1 70 70 CYS HB3 H 1 3.66 0.03 . 1 . . . . . . . . 4327 1 812 . 1 1 70 70 CYS C C 13 175.63 0.1 . 1 . . . . . . . . 4327 1 813 . 1 1 70 70 CYS CA C 13 55.01 0.1 . 1 . . . . . . . . 4327 1 814 . 1 1 70 70 CYS CB C 13 38.43 0.1 . 1 . . . . . . . . 4327 1 815 . 1 1 70 70 CYS N N 15 111.23 0.01 . 1 . . . . . . . . 4327 1 816 . 1 1 71 71 GLY H H 1 8.16 0.03 . 1 . . . . . . . . 4327 1 817 . 1 1 71 71 GLY HA2 H 1 3.34 0.03 . 2 . . . . . . . . 4327 1 818 . 1 1 71 71 GLY HA3 H 1 3.95 0.03 . 2 . . . . . . . . 4327 1 819 . 1 1 71 71 GLY C C 13 171.99 0.1 . 1 . . . . . . . . 4327 1 820 . 1 1 71 71 GLY CA C 13 47.35 0.1 . 1 . . . . . . . . 4327 1 821 . 1 1 71 71 GLY N N 15 107.98 0.01 . 1 . . . . . . . . 4327 1 822 . 1 1 72 72 TYR H H 1 8.45 0.03 . 1 . . . . . . . . 4327 1 823 . 1 1 72 72 TYR HA H 1 4.37 0.03 . 1 . . . . . . . . 4327 1 824 . 1 1 72 72 TYR HB2 H 1 2.35 0.03 . 2 . . . . . . . . 4327 1 825 . 1 1 72 72 TYR HB3 H 1 2.72 0.03 . 2 . . . . . . . . 4327 1 826 . 1 1 72 72 TYR HD1 H 1 6.59 0.03 . 1 . . . . . . . . 4327 1 827 . 1 1 72 72 TYR HD2 H 1 6.59 0.03 . 1 . . . . . . . . 4327 1 828 . 1 1 72 72 TYR HE1 H 1 6.19 0.03 . 1 . . . . . . . . 4327 1 829 . 1 1 72 72 TYR HE2 H 1 6.19 0.03 . 1 . . . . . . . . 4327 1 830 . 1 1 72 72 TYR C C 13 173.75 0.1 . 1 . . . . . . . . 4327 1 831 . 1 1 72 72 TYR CA C 13 58.07 0.1 . 1 . . . . . . . . 4327 1 832 . 1 1 72 72 TYR CB C 13 39.65 0.1 . 1 . . . . . . . . 4327 1 833 . 1 1 72 72 TYR CD1 C 13 132.47 0.1 . 1 . . . . . . . . 4327 1 834 . 1 1 72 72 TYR CD2 C 13 132.47 0.1 . 1 . . . . . . . . 4327 1 835 . 1 1 72 72 TYR CE1 C 13 117.38 0.1 . 1 . . . . . . . . 4327 1 836 . 1 1 72 72 TYR CE2 C 13 117.38 0.1 . 1 . . . . . . . . 4327 1 837 . 1 1 72 72 TYR N N 15 125.64 0.01 . 1 . . . . . . . . 4327 1 838 . 1 1 73 73 PHE H H 1 8.41 0.03 . 1 . . . . . . . . 4327 1 839 . 1 1 73 73 PHE HA H 1 4.07 0.03 . 1 . . . . . . . . 4327 1 840 . 1 1 73 73 PHE HB2 H 1 2.67 0.03 . 1 . . . . . . . . 4327 1 841 . 1 1 73 73 PHE HB3 H 1 2.67 0.03 . 1 . . . . . . . . 4327 1 842 . 1 1 73 73 PHE HD1 H 1 7.16 0.03 . 1 . . . . . . . . 4327 1 843 . 1 1 73 73 PHE HD2 H 1 7.16 0.03 . 1 . . . . . . . . 4327 1 844 . 1 1 73 73 PHE HE1 H 1 7.02 0.03 . 1 . . . . . . . . 4327 1 845 . 1 1 73 73 PHE HE2 H 1 7.02 0.03 . 1 . . . . . . . . 4327 1 846 . 1 1 73 73 PHE C C 13 172.99 0.1 . 1 . . . . . . . . 4327 1 847 . 1 1 73 73 PHE CA C 13 56.11 0.1 . 1 . . . . . . . . 4327 1 848 . 1 1 73 73 PHE CB C 13 38.43 0.1 . 1 . . . . . . . . 4327 1 849 . 1 1 73 73 PHE CD1 C 13 131.68 0.1 . 1 . . . . . . . . 4327 1 850 . 1 1 73 73 PHE CD2 C 13 131.68 0.1 . 1 . . . . . . . . 4327 1 851 . 1 1 73 73 PHE CE1 C 13 130.61 0.1 . 1 . . . . . . . . 4327 1 852 . 1 1 73 73 PHE CE2 C 13 130.61 0.1 . 1 . . . . . . . . 4327 1 853 . 1 1 73 73 PHE N N 15 131.54 0.01 . 1 . . . . . . . . 4327 1 854 . 1 1 74 74 HIS H H 1 7.33 0.03 . 1 . . . . . . . . 4327 1 855 . 1 1 74 74 HIS HA H 1 3.49 0.03 . 1 . . . . . . . . 4327 1 856 . 1 1 74 74 HIS HB2 H 1 1.83 0.03 . 2 . . . . . . . . 4327 1 857 . 1 1 74 74 HIS HB3 H 1 2.69 0.03 . 2 . . . . . . . . 4327 1 858 . 1 1 74 74 HIS HD2 H 1 6.54 0.03 . 1 . . . . . . . . 4327 1 859 . 1 1 74 74 HIS HE1 H 1 7.9 0.03 . 1 . . . . . . . . 4327 1 860 . 1 1 74 74 HIS C C 13 175.88 0.1 . 1 . . . . . . . . 4327 1 861 . 1 1 74 74 HIS CA C 13 56.39 0.1 . 1 . . . . . . . . 4327 1 862 . 1 1 74 74 HIS CB C 13 32.02 0.1 . 1 . . . . . . . . 4327 1 863 . 1 1 74 74 HIS CD2 C 13 116.65 0.1 . 1 . . . . . . . . 4327 1 864 . 1 1 74 74 HIS CE1 C 13 138.11 0.1 . 1 . . . . . . . . 4327 1 865 . 1 1 74 74 HIS N N 15 125.34 0.01 . 1 . . . . . . . . 4327 1 866 . 1 1 75 75 ARG H H 1 7.92 0.03 . 1 . . . . . . . . 4327 1 867 . 1 1 75 75 ARG HA H 1 4.17 0.03 . 1 . . . . . . . . 4327 1 868 . 1 1 75 75 ARG HB2 H 1 1.47 0.03 . 2 . . . . . . . . 4327 1 869 . 1 1 75 75 ARG HB3 H 1 1.72 0.03 . 2 . . . . . . . . 4327 1 870 . 1 1 75 75 ARG HG2 H 1 1.43 0.03 . 2 . . . . . . . . 4327 1 871 . 1 1 75 75 ARG HG3 H 1 1.48 0.03 . 2 . . . . . . . . 4327 1 872 . 1 1 75 75 ARG HD2 H 1 3.05 0.03 . 1 . . . . . . . . 4327 1 873 . 1 1 75 75 ARG HD3 H 1 3.05 0.03 . 1 . . . . . . . . 4327 1 874 . 1 1 75 75 ARG C C 13 174.95 0.1 . 1 . . . . . . . . 4327 1 875 . 1 1 75 75 ARG CA C 13 55.4 0.1 . 1 . . . . . . . . 4327 1 876 . 1 1 75 75 ARG CB C 13 30.47 0.1 . 1 . . . . . . . . 4327 1 877 . 1 1 75 75 ARG CG C 13 26.55 0.1 . 1 . . . . . . . . 4327 1 878 . 1 1 75 75 ARG CD C 13 42.88 0.1 . 1 . . . . . . . . 4327 1 879 . 1 1 75 75 ARG N N 15 126.98 0.01 . 1 . . . . . . . . 4327 1 880 . 1 1 76 76 SER H H 1 6.46 0.03 . 1 . . . . . . . . 4327 1 881 . 1 1 76 76 SER HA H 1 4.3 0.03 . 1 . . . . . . . . 4327 1 882 . 1 1 76 76 SER HB2 H 1 3.28 0.03 . 2 . . . . . . . . 4327 1 883 . 1 1 76 76 SER HB3 H 1 3.84 0.03 . 2 . . . . . . . . 4327 1 884 . 1 1 76 76 SER CA C 13 56.53 0.1 . 1 . . . . . . . . 4327 1 885 . 1 1 76 76 SER CB C 13 63.33 0.1 . 1 . . . . . . . . 4327 1 886 . 1 1 76 76 SER N N 15 113.15 0.01 . 1 . . . . . . . . 4327 1 887 . 1 1 77 77 HIS H H 1 8.92 0.03 . 1 . . . . . . . . 4327 1 888 . 1 1 77 77 HIS HA H 1 4.85 0.03 . 1 . . . . . . . . 4327 1 889 . 1 1 77 77 HIS HB2 H 1 3.06 0.03 . 2 . . . . . . . . 4327 1 890 . 1 1 77 77 HIS HB3 H 1 3.38 0.03 . 2 . . . . . . . . 4327 1 891 . 1 1 77 77 HIS HD2 H 1 7.15 0.03 . 1 . . . . . . . . 4327 1 892 . 1 1 77 77 HIS HE1 H 1 8.29 0.03 . 1 . . . . . . . . 4327 1 893 . 1 1 77 77 HIS C C 13 173.75 0.1 . 1 . . . . . . . . 4327 1 894 . 1 1 77 77 HIS CA C 13 54.87 0.1 . 1 . . . . . . . . 4327 1 895 . 1 1 77 77 HIS CB C 13 29.11 0.1 . 1 . . . . . . . . 4327 1 896 . 1 1 77 77 HIS CD2 C 13 119.59 0.1 . 1 . . . . . . . . 4327 1 897 . 1 1 77 77 HIS CE1 C 13 136.78 0.1 . 1 . . . . . . . . 4327 1 898 . 1 1 77 77 HIS N N 15 123.78 0.01 . 1 . . . . . . . . 4327 1 899 . 1 1 78 78 ASN H H 1 8.18 0.03 . 1 . . . . . . . . 4327 1 900 . 1 1 78 78 ASN HA H 1 4.91 0.03 . 1 . . . . . . . . 4327 1 901 . 1 1 78 78 ASN HB2 H 1 2.8 0.03 . 2 . . . . . . . . 4327 1 902 . 1 1 78 78 ASN HB3 H 1 3.08 0.03 . 2 . . . . . . . . 4327 1 903 . 1 1 78 78 ASN HD21 H 1 7.72 0.03 . 2 . . . . . . . . 4327 1 904 . 1 1 78 78 ASN HD22 H 1 7.01 0.03 . 2 . . . . . . . . 4327 1 905 . 1 1 78 78 ASN C C 13 175.82 0.1 . 1 . . . . . . . . 4327 1 906 . 1 1 78 78 ASN CA C 13 51.88 0.1 . 1 . . . . . . . . 4327 1 907 . 1 1 78 78 ASN CB C 13 38.17 0.1 . 1 . . . . . . . . 4327 1 908 . 1 1 78 78 ASN N N 15 119.59 0.01 . 1 . . . . . . . . 4327 1 909 . 1 1 78 78 ASN ND2 N 15 112.71 0.01 . 1 . . . . . . . . 4327 1 910 . 1 1 79 79 ARG H H 1 8.98 0.03 . 1 . . . . . . . . 4327 1 911 . 1 1 79 79 ARG HA H 1 4.33 0.03 . 1 . . . . . . . . 4327 1 912 . 1 1 79 79 ARG HB2 H 1 1.96 0.03 . 2 . . . . . . . . 4327 1 913 . 1 1 79 79 ARG HB3 H 1 2.02 0.03 . 2 . . . . . . . . 4327 1 914 . 1 1 79 79 ARG HG2 H 1 1.84 0.03 . 1 . . . . . . . . 4327 1 915 . 1 1 79 79 ARG HG3 H 1 1.84 0.03 . 1 . . . . . . . . 4327 1 916 . 1 1 79 79 ARG HD2 H 1 3.25 0.03 . 1 . . . . . . . . 4327 1 917 . 1 1 79 79 ARG HD3 H 1 3.25 0.03 . 1 . . . . . . . . 4327 1 918 . 1 1 79 79 ARG C C 13 177.71 0.1 . 1 . . . . . . . . 4327 1 919 . 1 1 79 79 ARG CA C 13 58.15 0.1 . 1 . . . . . . . . 4327 1 920 . 1 1 79 79 ARG CB C 13 29.69 0.1 . 1 . . . . . . . . 4327 1 921 . 1 1 79 79 ARG CG C 13 27.12 0.1 . 1 . . . . . . . . 4327 1 922 . 1 1 79 79 ARG CD C 13 43.3 0.1 . 1 . . . . . . . . 4327 1 923 . 1 1 79 79 ARG N N 15 125.28 0.01 . 1 . . . . . . . . 4327 1 924 . 1 1 80 80 SER H H 1 8.28 0.03 . 1 . . . . . . . . 4327 1 925 . 1 1 80 80 SER HA H 1 4.42 0.03 . 1 . . . . . . . . 4327 1 926 . 1 1 80 80 SER HB2 H 1 3.94 0.03 . 1 . . . . . . . . 4327 1 927 . 1 1 80 80 SER HB3 H 1 3.94 0.03 . 1 . . . . . . . . 4327 1 928 . 1 1 80 80 SER C C 13 173.6 0.1 . 1 . . . . . . . . 4327 1 929 . 1 1 80 80 SER CA C 13 58.69 0.1 . 1 . . . . . . . . 4327 1 930 . 1 1 80 80 SER CB C 13 63.46 0.1 . 1 . . . . . . . . 4327 1 931 . 1 1 80 80 SER N N 15 114.19 0.01 . 1 . . . . . . . . 4327 1 932 . 1 1 81 81 GLU H H 1 7.5 0.03 . 1 . . . . . . . . 4327 1 933 . 1 1 81 81 GLU HA H 1 4.18 0.03 . 1 . . . . . . . . 4327 1 934 . 1 1 81 81 GLU HB2 H 1 2.09 0.03 . 2 . . . . . . . . 4327 1 935 . 1 1 81 81 GLU HB3 H 1 2.29 0.03 . 2 . . . . . . . . 4327 1 936 . 1 1 81 81 GLU HG2 H 1 2.1 0.03 . 1 . . . . . . . . 4327 1 937 . 1 1 81 81 GLU HG3 H 1 2.1 0.03 . 1 . . . . . . . . 4327 1 938 . 1 1 81 81 GLU C C 13 175.88 0.1 . 1 . . . . . . . . 4327 1 939 . 1 1 81 81 GLU CA C 13 58.65 0.1 . 1 . . . . . . . . 4327 1 940 . 1 1 81 81 GLU CB C 13 30.86 0.1 . 1 . . . . . . . . 4327 1 941 . 1 1 81 81 GLU CG C 13 35.82 0.1 . 1 . . . . . . . . 4327 1 942 . 1 1 81 81 GLU N N 15 123.59 0.01 . 1 . . . . . . . . 4327 1 943 . 1 1 82 82 GLU H H 1 9.03 0.03 . 1 . . . . . . . . 4327 1 944 . 1 1 82 82 GLU HA H 1 4.67 0.03 . 1 . . . . . . . . 4327 1 945 . 1 1 82 82 GLU HB2 H 1 1.84 0.03 . 2 . . . . . . . . 4327 1 946 . 1 1 82 82 GLU HB3 H 1 1.94 0.03 . 2 . . . . . . . . 4327 1 947 . 1 1 82 82 GLU HG2 H 1 1.87 0.03 . 2 . . . . . . . . 4327 1 948 . 1 1 82 82 GLU HG3 H 1 2.32 0.03 . 2 . . . . . . . . 4327 1 949 . 1 1 82 82 GLU C C 13 176.9 0.1 . 1 . . . . . . . . 4327 1 950 . 1 1 82 82 GLU CA C 13 56.34 0.1 . 1 . . . . . . . . 4327 1 951 . 1 1 82 82 GLU CB C 13 31.7 0.1 . 1 . . . . . . . . 4327 1 952 . 1 1 82 82 GLU CG C 13 37.71 0.1 . 1 . . . . . . . . 4327 1 953 . 1 1 82 82 GLU N N 15 125.19 0.01 . 1 . . . . . . . . 4327 1 954 . 1 1 83 83 PHE H H 1 9.97 0.03 . 1 . . . . . . . . 4327 1 955 . 1 1 83 83 PHE HA H 1 4.87 0.03 . 1 . . . . . . . . 4327 1 956 . 1 1 83 83 PHE HB2 H 1 2.69 0.03 . 2 . . . . . . . . 4327 1 957 . 1 1 83 83 PHE HB3 H 1 3.02 0.03 . 2 . . . . . . . . 4327 1 958 . 1 1 83 83 PHE HD1 H 1 7.23 0.03 . 1 . . . . . . . . 4327 1 959 . 1 1 83 83 PHE HD2 H 1 7.23 0.03 . 1 . . . . . . . . 4327 1 960 . 1 1 83 83 PHE C C 13 173.24 0.1 . 1 . . . . . . . . 4327 1 961 . 1 1 83 83 PHE CA C 13 57.49 0.1 . 1 . . . . . . . . 4327 1 962 . 1 1 83 83 PHE CB C 13 41.79 0.1 . 1 . . . . . . . . 4327 1 963 . 1 1 83 83 PHE CD1 C 13 131.33 0.1 . 1 . . . . . . . . 4327 1 964 . 1 1 83 83 PHE CD2 C 13 131.33 0.1 . 1 . . . . . . . . 4327 1 965 . 1 1 83 83 PHE N N 15 125.36 0.01 . 1 . . . . . . . . 4327 1 966 . 1 1 84 84 LEU H H 1 9.62 0.03 . 1 . . . . . . . . 4327 1 967 . 1 1 84 84 LEU HA H 1 5.13 0.03 . 1 . . . . . . . . 4327 1 968 . 1 1 84 84 LEU HB2 H 1 1.7 0.03 . 2 . . . . . . . . 4327 1 969 . 1 1 84 84 LEU HB3 H 1 2.27 0.03 . 2 . . . . . . . . 4327 1 970 . 1 1 84 84 LEU HG H 1 1.31 0.03 . 1 . . . . . . . . 4327 1 971 . 1 1 84 84 LEU HD11 H 1 0.58 0.03 . 1 . . . . . . . . 4327 1 972 . 1 1 84 84 LEU HD12 H 1 0.58 0.03 . 1 . . . . . . . . 4327 1 973 . 1 1 84 84 LEU HD13 H 1 0.58 0.03 . 1 . . . . . . . . 4327 1 974 . 1 1 84 84 LEU HD21 H 1 0.64 0.03 . 1 . . . . . . . . 4327 1 975 . 1 1 84 84 LEU HD22 H 1 0.64 0.03 . 1 . . . . . . . . 4327 1 976 . 1 1 84 84 LEU HD23 H 1 0.64 0.03 . 1 . . . . . . . . 4327 1 977 . 1 1 84 84 LEU C C 13 175.19 0.1 . 1 . . . . . . . . 4327 1 978 . 1 1 84 84 LEU CA C 13 51.84 0.1 . 1 . . . . . . . . 4327 1 979 . 1 1 84 84 LEU CB C 13 43.08 0.1 . 1 . . . . . . . . 4327 1 980 . 1 1 84 84 LEU CG C 13 27.6 0.1 . 1 . . . . . . . . 4327 1 981 . 1 1 84 84 LEU CD1 C 13 23.35 0.1 . 1 . . . . . . . . 4327 1 982 . 1 1 84 84 LEU CD2 C 13 23.12 0.1 . 1 . . . . . . . . 4327 1 983 . 1 1 84 84 LEU N N 15 126.52 0.01 . 1 . . . . . . . . 4327 1 984 . 1 1 85 85 ILE H H 1 9.3 0.03 . 1 . . . . . . . . 4327 1 985 . 1 1 85 85 ILE HA H 1 4.46 0.03 . 1 . . . . . . . . 4327 1 986 . 1 1 85 85 ILE HB H 1 1.5 0.03 . 1 . . . . . . . . 4327 1 987 . 1 1 85 85 ILE HG12 H 1 0.81 0.03 . 2 . . . . . . . . 4327 1 988 . 1 1 85 85 ILE HG13 H 1 1.56 0.03 . 2 . . . . . . . . 4327 1 989 . 1 1 85 85 ILE HG21 H 1 0.65 0.03 . 1 . . . . . . . . 4327 1 990 . 1 1 85 85 ILE HG22 H 1 0.65 0.03 . 1 . . . . . . . . 4327 1 991 . 1 1 85 85 ILE HG23 H 1 0.65 0.03 . 1 . . . . . . . . 4327 1 992 . 1 1 85 85 ILE HD11 H 1 0.42 0.03 . 1 . . . . . . . . 4327 1 993 . 1 1 85 85 ILE HD12 H 1 0.42 0.03 . 1 . . . . . . . . 4327 1 994 . 1 1 85 85 ILE HD13 H 1 0.42 0.03 . 1 . . . . . . . . 4327 1 995 . 1 1 85 85 ILE C C 13 172.82 0.1 . 1 . . . . . . . . 4327 1 996 . 1 1 85 85 ILE CA C 13 60.97 0.1 . 1 . . . . . . . . 4327 1 997 . 1 1 85 85 ILE CB C 13 41.53 0.1 . 1 . . . . . . . . 4327 1 998 . 1 1 85 85 ILE CG1 C 13 26.18 0.1 . 1 . . . . . . . . 4327 1 999 . 1 1 85 85 ILE CG2 C 13 17.7 0.1 . 1 . . . . . . . . 4327 1 1000 . 1 1 85 85 ILE CD1 C 13 14.8 0.1 . 1 . . . . . . . . 4327 1 1001 . 1 1 85 85 ILE N N 15 125.04 0.01 . 1 . . . . . . . . 4327 1 1002 . 1 1 86 86 ALA H H 1 8.16 0.03 . 1 . . . . . . . . 4327 1 1003 . 1 1 86 86 ALA HA H 1 5.53 0.03 . 1 . . . . . . . . 4327 1 1004 . 1 1 86 86 ALA HB1 H 1 1.57 0.03 . 1 . . . . . . . . 4327 1 1005 . 1 1 86 86 ALA HB2 H 1 1.57 0.03 . 1 . . . . . . . . 4327 1 1006 . 1 1 86 86 ALA HB3 H 1 1.57 0.03 . 1 . . . . . . . . 4327 1 1007 . 1 1 86 86 ALA C C 13 175.92 0.1 . 1 . . . . . . . . 4327 1 1008 . 1 1 86 86 ALA CA C 13 50.08 0.1 . 1 . . . . . . . . 4327 1 1009 . 1 1 86 86 ALA CB C 13 19.8 0.1 . 1 . . . . . . . . 4327 1 1010 . 1 1 86 86 ALA N N 15 133.12 0.01 . 1 . . . . . . . . 4327 1 1011 . 1 1 87 87 GLY H H 1 8.49 0.03 . 1 . . . . . . . . 4327 1 1012 . 1 1 87 87 GLY HA2 H 1 3.61 0.03 . 2 . . . . . . . . 4327 1 1013 . 1 1 87 87 GLY HA3 H 1 5.2 0.03 . 2 . . . . . . . . 4327 1 1014 . 1 1 87 87 GLY C C 13 172.5 0.1 . 1 . . . . . . . . 4327 1 1015 . 1 1 87 87 GLY CA C 13 44.56 0.1 . 1 . . . . . . . . 4327 1 1016 . 1 1 87 87 GLY N N 15 106.61 0.01 . 1 . . . . . . . . 4327 1 1017 . 1 1 88 88 LYS H H 1 8.37 0.03 . 1 . . . . . . . . 4327 1 1018 . 1 1 88 88 LYS HA H 1 4.86 0.03 . 1 . . . . . . . . 4327 1 1019 . 1 1 88 88 LYS HB2 H 1 1.77 0.03 . 2 . . . . . . . . 4327 1 1020 . 1 1 88 88 LYS HB3 H 1 1.83 0.03 . 2 . . . . . . . . 4327 1 1021 . 1 1 88 88 LYS HG2 H 1 1.5 0.03 . 2 . . . . . . . . 4327 1 1022 . 1 1 88 88 LYS HG3 H 1 1.56 0.03 . 2 . . . . . . . . 4327 1 1023 . 1 1 88 88 LYS HD2 H 1 1.71 0.03 . 1 . . . . . . . . 4327 1 1024 . 1 1 88 88 LYS HD3 H 1 1.71 0.03 . 1 . . . . . . . . 4327 1 1025 . 1 1 88 88 LYS HE2 H 1 3.01 0.03 . 1 . . . . . . . . 4327 1 1026 . 1 1 88 88 LYS HE3 H 1 3.01 0.03 . 1 . . . . . . . . 4327 1 1027 . 1 1 88 88 LYS C C 13 174.87 0.1 . 1 . . . . . . . . 4327 1 1028 . 1 1 88 88 LYS CA C 13 53.96 0.1 . 1 . . . . . . . . 4327 1 1029 . 1 1 88 88 LYS CB C 13 35.45 0.1 . 1 . . . . . . . . 4327 1 1030 . 1 1 88 88 LYS CG C 13 24.56 0.1 . 1 . . . . . . . . 4327 1 1031 . 1 1 88 88 LYS CD C 13 28.53 0.1 . 1 . . . . . . . . 4327 1 1032 . 1 1 88 88 LYS CE C 13 41.77 0.1 . 1 . . . . . . . . 4327 1 1033 . 1 1 88 88 LYS N N 15 120.28 0.01 . 1 . . . . . . . . 4327 1 1034 . 1 1 89 89 LEU H H 1 9.8 0.03 . 1 . . . . . . . . 4327 1 1035 . 1 1 89 89 LEU HA H 1 5.07 0.03 . 1 . . . . . . . . 4327 1 1036 . 1 1 89 89 LEU HB2 H 1 1.38 0.03 . 2 . . . . . . . . 4327 1 1037 . 1 1 89 89 LEU HB3 H 1 1.43 0.03 . 2 . . . . . . . . 4327 1 1038 . 1 1 89 89 LEU HG H 1 1.37 0.03 . 1 . . . . . . . . 4327 1 1039 . 1 1 89 89 LEU HD11 H 1 0.73 0.03 . 1 . . . . . . . . 4327 1 1040 . 1 1 89 89 LEU HD12 H 1 0.73 0.03 . 1 . . . . . . . . 4327 1 1041 . 1 1 89 89 LEU HD13 H 1 0.73 0.03 . 1 . . . . . . . . 4327 1 1042 . 1 1 89 89 LEU HD21 H 1 0.68 0.03 . 1 . . . . . . . . 4327 1 1043 . 1 1 89 89 LEU HD22 H 1 0.68 0.03 . 1 . . . . . . . . 4327 1 1044 . 1 1 89 89 LEU HD23 H 1 0.68 0.03 . 1 . . . . . . . . 4327 1 1045 . 1 1 89 89 LEU C C 13 176.61 0.1 . 1 . . . . . . . . 4327 1 1046 . 1 1 89 89 LEU CA C 13 53.39 0.1 . 1 . . . . . . . . 4327 1 1047 . 1 1 89 89 LEU CB C 13 43.21 0.1 . 1 . . . . . . . . 4327 1 1048 . 1 1 89 89 LEU CG C 13 26.72 0.1 . 1 . . . . . . . . 4327 1 1049 . 1 1 89 89 LEU CD1 C 13 24.38 0.1 . 1 . . . . . . . . 4327 1 1050 . 1 1 89 89 LEU CD2 C 13 24.23 0.1 . 1 . . . . . . . . 4327 1 1051 . 1 1 89 89 LEU N N 15 125.33 0.01 . 1 . . . . . . . . 4327 1 1052 . 1 1 90 90 GLN H H 1 9.21 0.03 . 1 . . . . . . . . 4327 1 1053 . 1 1 90 90 GLN HA H 1 4.49 0.03 . 1 . . . . . . . . 4327 1 1054 . 1 1 90 90 GLN HB2 H 1 1.53 0.03 . 1 . . . . . . . . 4327 1 1055 . 1 1 90 90 GLN HB3 H 1 1.53 0.03 . 1 . . . . . . . . 4327 1 1056 . 1 1 90 90 GLN HG2 H 1 1.94 0.03 . 1 . . . . . . . . 4327 1 1057 . 1 1 90 90 GLN HG3 H 1 1.94 0.03 . 1 . . . . . . . . 4327 1 1058 . 1 1 90 90 GLN HE21 H 1 7.02 0.03 . 2 . . . . . . . . 4327 1 1059 . 1 1 90 90 GLN HE22 H 1 6.44 0.03 . 2 . . . . . . . . 4327 1 1060 . 1 1 90 90 GLN C C 13 175.09 0.1 . 1 . . . . . . . . 4327 1 1061 . 1 1 90 90 GLN CA C 13 54.6 0.1 . 1 . . . . . . . . 4327 1 1062 . 1 1 90 90 GLN CB C 13 30.47 0.1 . 1 . . . . . . . . 4327 1 1063 . 1 1 90 90 GLN CG C 13 33.22 0.1 . 1 . . . . . . . . 4327 1 1064 . 1 1 90 90 GLN N N 15 125.51 0.01 . 1 . . . . . . . . 4327 1 1065 . 1 1 90 90 GLN NE2 N 15 111.16 0.01 . 1 . . . . . . . . 4327 1 1066 . 1 1 91 91 ASP H H 1 9.45 0.03 . 1 . . . . . . . . 4327 1 1067 . 1 1 91 91 ASP HA H 1 4.23 0.03 . 1 . . . . . . . . 4327 1 1068 . 1 1 91 91 ASP HB2 H 1 2.58 0.03 . 2 . . . . . . . . 4327 1 1069 . 1 1 91 91 ASP HB3 H 1 2.83 0.03 . 2 . . . . . . . . 4327 1 1070 . 1 1 91 91 ASP C C 13 175.27 0.1 . 1 . . . . . . . . 4327 1 1071 . 1 1 91 91 ASP CA C 13 55.23 0.1 . 1 . . . . . . . . 4327 1 1072 . 1 1 91 91 ASP CB C 13 39.46 0.1 . 1 . . . . . . . . 4327 1 1073 . 1 1 91 91 ASP N N 15 128.56 0.01 . 1 . . . . . . . . 4327 1 1074 . 1 1 92 92 GLY H H 1 8.45 0.03 . 1 . . . . . . . . 4327 1 1075 . 1 1 92 92 GLY HA2 H 1 3.47 0.03 . 2 . . . . . . . . 4327 1 1076 . 1 1 92 92 GLY HA3 H 1 4.1 0.03 . 2 . . . . . . . . 4327 1 1077 . 1 1 92 92 GLY C C 13 172.62 0.1 . 1 . . . . . . . . 4327 1 1078 . 1 1 92 92 GLY CA C 13 45.17 0.1 . 1 . . . . . . . . 4327 1 1079 . 1 1 92 92 GLY N N 15 102.62 0.01 . 1 . . . . . . . . 4327 1 1080 . 1 1 93 93 LEU H H 1 7.67 0.03 . 1 . . . . . . . . 4327 1 1081 . 1 1 93 93 LEU HA H 1 4.65 0.03 . 1 . . . . . . . . 4327 1 1082 . 1 1 93 93 LEU HB2 H 1 1.06 0.03 . 2 . . . . . . . . 4327 1 1083 . 1 1 93 93 LEU HB3 H 1 1.54 0.03 . 2 . . . . . . . . 4327 1 1084 . 1 1 93 93 LEU HG H 1 1.45 0.03 . 1 . . . . . . . . 4327 1 1085 . 1 1 93 93 LEU HD11 H 1 0.16 0.03 . 1 . . . . . . . . 4327 1 1086 . 1 1 93 93 LEU HD12 H 1 0.16 0.03 . 1 . . . . . . . . 4327 1 1087 . 1 1 93 93 LEU HD13 H 1 0.16 0.03 . 1 . . . . . . . . 4327 1 1088 . 1 1 93 93 LEU HD21 H 1 0.67 0.03 . 1 . . . . . . . . 4327 1 1089 . 1 1 93 93 LEU HD22 H 1 0.67 0.03 . 1 . . . . . . . . 4327 1 1090 . 1 1 93 93 LEU HD23 H 1 0.67 0.03 . 1 . . . . . . . . 4327 1 1091 . 1 1 93 93 LEU C C 13 175.66 0.1 . 1 . . . . . . . . 4327 1 1092 . 1 1 93 93 LEU CA C 13 52.65 0.1 . 1 . . . . . . . . 4327 1 1093 . 1 1 93 93 LEU CB C 13 42.21 0.1 . 1 . . . . . . . . 4327 1 1094 . 1 1 93 93 LEU CG C 13 25.94 0.1 . 1 . . . . . . . . 4327 1 1095 . 1 1 93 93 LEU CD1 C 13 23.35 0.1 . 1 . . . . . . . . 4327 1 1096 . 1 1 93 93 LEU CD2 C 13 21.52 0.1 . 1 . . . . . . . . 4327 1 1097 . 1 1 93 93 LEU N N 15 121.2 0.01 . 1 . . . . . . . . 4327 1 1098 . 1 1 94 94 LEU H H 1 9.43 0.03 . 1 . . . . . . . . 4327 1 1099 . 1 1 94 94 LEU HA H 1 4.7 0.03 . 1 . . . . . . . . 4327 1 1100 . 1 1 94 94 LEU HB2 H 1 1.22 0.03 . 2 . . . . . . . . 4327 1 1101 . 1 1 94 94 LEU HB3 H 1 2.32 0.03 . 2 . . . . . . . . 4327 1 1102 . 1 1 94 94 LEU HG H 1 1.47 0.03 . 1 . . . . . . . . 4327 1 1103 . 1 1 94 94 LEU HD11 H 1 0.82 0.03 . 1 . . . . . . . . 4327 1 1104 . 1 1 94 94 LEU HD12 H 1 0.82 0.03 . 1 . . . . . . . . 4327 1 1105 . 1 1 94 94 LEU HD13 H 1 0.82 0.03 . 1 . . . . . . . . 4327 1 1106 . 1 1 94 94 LEU HD21 H 1 0.7 0.03 . 1 . . . . . . . . 4327 1 1107 . 1 1 94 94 LEU HD22 H 1 0.7 0.03 . 1 . . . . . . . . 4327 1 1108 . 1 1 94 94 LEU HD23 H 1 0.7 0.03 . 1 . . . . . . . . 4327 1 1109 . 1 1 94 94 LEU C C 13 173.95 0.1 . 1 . . . . . . . . 4327 1 1110 . 1 1 94 94 LEU CA C 13 54.99 0.1 . 1 . . . . . . . . 4327 1 1111 . 1 1 94 94 LEU CB C 13 41.4 0.1 . 1 . . . . . . . . 4327 1 1112 . 1 1 94 94 LEU CG C 13 27.35 0.1 . 1 . . . . . . . . 4327 1 1113 . 1 1 94 94 LEU CD1 C 13 23.41 0.1 . 1 . . . . . . . . 4327 1 1114 . 1 1 94 94 LEU CD2 C 13 25.94 0.1 . 1 . . . . . . . . 4327 1 1115 . 1 1 94 94 LEU N N 15 126.48 0.01 . 1 . . . . . . . . 4327 1 1116 . 1 1 95 95 HIS H H 1 9.71 0.03 . 1 . . . . . . . . 4327 1 1117 . 1 1 95 95 HIS HA H 1 5.65 0.03 . 1 . . . . . . . . 4327 1 1118 . 1 1 95 95 HIS HB2 H 1 2.93 0.03 . 2 . . . . . . . . 4327 1 1119 . 1 1 95 95 HIS HB3 H 1 3.13 0.03 . 2 . . . . . . . . 4327 1 1120 . 1 1 95 95 HIS HD2 H 1 6.99 0.03 . 1 . . . . . . . . 4327 1 1121 . 1 1 95 95 HIS HE1 H 1 7.74 0.03 . 1 . . . . . . . . 4327 1 1122 . 1 1 95 95 HIS C C 13 176.14 0.1 . 1 . . . . . . . . 4327 1 1123 . 1 1 95 95 HIS CA C 13 55.31 0.1 . 1 . . . . . . . . 4327 1 1124 . 1 1 95 95 HIS CB C 13 33.45 0.1 . 1 . . . . . . . . 4327 1 1125 . 1 1 95 95 HIS CD2 C 13 118.86 0.1 . 1 . . . . . . . . 4327 1 1126 . 1 1 95 95 HIS CE1 C 13 136.53 0.1 . 1 . . . . . . . . 4327 1 1127 . 1 1 95 95 HIS N N 15 129.15 0.01 . 1 . . . . . . . . 4327 1 1128 . 1 1 96 96 ILE H H 1 8.92 0.03 . 1 . . . . . . . . 4327 1 1129 . 1 1 96 96 ILE HA H 1 5.17 0.03 . 1 . . . . . . . . 4327 1 1130 . 1 1 96 96 ILE HB H 1 1.89 0.03 . 1 . . . . . . . . 4327 1 1131 . 1 1 96 96 ILE HG12 H 1 0.96 0.03 . 2 . . . . . . . . 4327 1 1132 . 1 1 96 96 ILE HG13 H 1 1.13 0.03 . 2 . . . . . . . . 4327 1 1133 . 1 1 96 96 ILE HG21 H 1 0.72 0.03 . 1 . . . . . . . . 4327 1 1134 . 1 1 96 96 ILE HG22 H 1 0.72 0.03 . 1 . . . . . . . . 4327 1 1135 . 1 1 96 96 ILE HG23 H 1 0.72 0.03 . 1 . . . . . . . . 4327 1 1136 . 1 1 96 96 ILE HD11 H 1 0.22 0.03 . 1 . . . . . . . . 4327 1 1137 . 1 1 96 96 ILE HD12 H 1 0.22 0.03 . 1 . . . . . . . . 4327 1 1138 . 1 1 96 96 ILE HD13 H 1 0.22 0.03 . 1 . . . . . . . . 4327 1 1139 . 1 1 96 96 ILE C C 13 176.34 0.1 . 1 . . . . . . . . 4327 1 1140 . 1 1 96 96 ILE CA C 13 59.24 0.1 . 1 . . . . . . . . 4327 1 1141 . 1 1 96 96 ILE CB C 13 42.88 0.1 . 1 . . . . . . . . 4327 1 1142 . 1 1 96 96 ILE CG1 C 13 23.82 0.1 . 1 . . . . . . . . 4327 1 1143 . 1 1 96 96 ILE CG2 C 13 17.23 0.1 . 1 . . . . . . . . 4327 1 1144 . 1 1 96 96 ILE CD1 C 13 13.34 0.1 . 1 . . . . . . . . 4327 1 1145 . 1 1 96 96 ILE N N 15 113.87 0.01 . 1 . . . . . . . . 4327 1 1146 . 1 1 97 97 THR H H 1 9.27 0.03 . 1 . . . . . . . . 4327 1 1147 . 1 1 97 97 THR HA H 1 4.77 0.03 . 1 . . . . . . . . 4327 1 1148 . 1 1 97 97 THR HB H 1 5.06 0.03 . 1 . . . . . . . . 4327 1 1149 . 1 1 97 97 THR HG21 H 1 1.3 0.03 . 1 . . . . . . . . 4327 1 1150 . 1 1 97 97 THR HG22 H 1 1.3 0.03 . 1 . . . . . . . . 4327 1 1151 . 1 1 97 97 THR HG23 H 1 1.3 0.03 . 1 . . . . . . . . 4327 1 1152 . 1 1 97 97 THR C C 13 175.95 0.1 . 1 . . . . . . . . 4327 1 1153 . 1 1 97 97 THR CA C 13 60.74 0.1 . 1 . . . . . . . . 4327 1 1154 . 1 1 97 97 THR CB C 13 73 0.1 . 1 . . . . . . . . 4327 1 1155 . 1 1 97 97 THR CG2 C 13 21.08 0.1 . 1 . . . . . . . . 4327 1 1156 . 1 1 97 97 THR N N 15 114.53 0.01 . 1 . . . . . . . . 4327 1 1157 . 1 1 98 98 THR H H 1 9.32 0.03 . 1 . . . . . . . . 4327 1 1158 . 1 1 98 98 THR HA H 1 4.48 0.03 . 1 . . . . . . . . 4327 1 1159 . 1 1 98 98 THR HB H 1 4.5 0.03 . 1 . . . . . . . . 4327 1 1160 . 1 1 98 98 THR HG21 H 1 1.36 0.03 . 1 . . . . . . . . 4327 1 1161 . 1 1 98 98 THR HG22 H 1 1.36 0.03 . 1 . . . . . . . . 4327 1 1162 . 1 1 98 98 THR HG23 H 1 1.36 0.03 . 1 . . . . . . . . 4327 1 1163 . 1 1 98 98 THR C C 13 174.11 0.1 . 1 . . . . . . . . 4327 1 1164 . 1 1 98 98 THR CA C 13 64.62 0.1 . 1 . . . . . . . . 4327 1 1165 . 1 1 98 98 THR CB C 13 67.66 0.1 . 1 . . . . . . . . 4327 1 1166 . 1 1 98 98 THR CG2 C 13 23.68 0.1 . 1 . . . . . . . . 4327 1 1167 . 1 1 98 98 THR N N 15 113.02 0.01 . 1 . . . . . . . . 4327 1 1168 . 1 1 99 99 CYS H H 1 8.4 0.03 . 1 . . . . . . . . 4327 1 1169 . 1 1 99 99 CYS HA H 1 4.48 0.03 . 1 . . . . . . . . 4327 1 1170 . 1 1 99 99 CYS HB2 H 1 2.73 0.03 . 2 . . . . . . . . 4327 1 1171 . 1 1 99 99 CYS HB3 H 1 3.5 0.03 . 2 . . . . . . . . 4327 1 1172 . 1 1 99 99 CYS C C 13 175.49 0.1 . 1 . . . . . . . . 4327 1 1173 . 1 1 99 99 CYS CA C 13 54 0.1 . 1 . . . . . . . . 4327 1 1174 . 1 1 99 99 CYS CB C 13 37.84 0.1 . 1 . . . . . . . . 4327 1 1175 . 1 1 99 99 CYS N N 15 117.12 0.01 . 1 . . . . . . . . 4327 1 1176 . 1 1 100 100 SER H H 1 7.81 0.03 . 1 . . . . . . . . 4327 1 1177 . 1 1 100 100 SER HA H 1 4.81 0.03 . 1 . . . . . . . . 4327 1 1178 . 1 1 100 100 SER HB2 H 1 3.85 0.03 . 1 . . . . . . . . 4327 1 1179 . 1 1 100 100 SER HB3 H 1 3.85 0.03 . 1 . . . . . . . . 4327 1 1180 . 1 1 100 100 SER C C 13 172.31 0.1 . 1 . . . . . . . . 4327 1 1181 . 1 1 100 100 SER CA C 13 58.07 0.1 . 1 . . . . . . . . 4327 1 1182 . 1 1 100 100 SER CB C 13 62.55 0.1 . 1 . . . . . . . . 4327 1 1183 . 1 1 100 100 SER N N 15 119.17 0.01 . 1 . . . . . . . . 4327 1 1184 . 1 1 101 101 PHE H H 1 9.71 0.03 . 1 . . . . . . . . 4327 1 1185 . 1 1 101 101 PHE HA H 1 4.3 0.03 . 1 . . . . . . . . 4327 1 1186 . 1 1 101 101 PHE HB2 H 1 2.63 0.03 . 2 . . . . . . . . 4327 1 1187 . 1 1 101 101 PHE HB3 H 1 3.31 0.03 . 2 . . . . . . . . 4327 1 1188 . 1 1 101 101 PHE HD1 H 1 7.22 0.03 . 1 . . . . . . . . 4327 1 1189 . 1 1 101 101 PHE HD2 H 1 7.22 0.03 . 1 . . . . . . . . 4327 1 1190 . 1 1 101 101 PHE HE1 H 1 7.06 0.03 . 1 . . . . . . . . 4327 1 1191 . 1 1 101 101 PHE HE2 H 1 7.06 0.03 . 1 . . . . . . . . 4327 1 1192 . 1 1 101 101 PHE C C 13 172.06 0.1 . 1 . . . . . . . . 4327 1 1193 . 1 1 101 101 PHE CA C 13 59.63 0.1 . 1 . . . . . . . . 4327 1 1194 . 1 1 101 101 PHE CB C 13 39.72 0.1 . 1 . . . . . . . . 4327 1 1195 . 1 1 101 101 PHE CD1 C 13 131.15 0.1 . 1 . . . . . . . . 4327 1 1196 . 1 1 101 101 PHE CD2 C 13 131.15 0.1 . 1 . . . . . . . . 4327 1 1197 . 1 1 101 101 PHE N N 15 127.41 0.01 . 1 . . . . . . . . 4327 1 1198 . 1 1 102 102 VAL H H 1 7.16 0.03 . 1 . . . . . . . . 4327 1 1199 . 1 1 102 102 VAL HA H 1 5.13 0.03 . 1 . . . . . . . . 4327 1 1200 . 1 1 102 102 VAL HB H 1 1.79 0.03 . 1 . . . . . . . . 4327 1 1201 . 1 1 102 102 VAL HG11 H 1 0.67 0.03 . 1 . . . . . . . . 4327 1 1202 . 1 1 102 102 VAL HG12 H 1 0.67 0.03 . 1 . . . . . . . . 4327 1 1203 . 1 1 102 102 VAL HG13 H 1 0.67 0.03 . 1 . . . . . . . . 4327 1 1204 . 1 1 102 102 VAL HG21 H 1 0.57 0.03 . 1 . . . . . . . . 4327 1 1205 . 1 1 102 102 VAL HG22 H 1 0.57 0.03 . 1 . . . . . . . . 4327 1 1206 . 1 1 102 102 VAL HG23 H 1 0.57 0.03 . 1 . . . . . . . . 4327 1 1207 . 1 1 102 102 VAL C C 13 175.6 0.1 . 1 . . . . . . . . 4327 1 1208 . 1 1 102 102 VAL CA C 13 60.31 0.1 . 1 . . . . . . . . 4327 1 1209 . 1 1 102 102 VAL CB C 13 34.87 0.1 . 1 . . . . . . . . 4327 1 1210 . 1 1 102 102 VAL CG1 C 13 20.52 0.1 . 1 . . . . . . . . 4327 1 1211 . 1 1 102 102 VAL CG2 C 13 21.53 0.1 . 1 . . . . . . . . 4327 1 1212 . 1 1 102 102 VAL N N 15 129.24 0.01 . 1 . . . . . . . . 4327 1 1213 . 1 1 103 103 ALA H H 1 8.78 0.03 . 1 . . . . . . . . 4327 1 1214 . 1 1 103 103 ALA HA H 1 4.98 0.03 . 1 . . . . . . . . 4327 1 1215 . 1 1 103 103 ALA HB1 H 1 1.05 0.03 . 1 . . . . . . . . 4327 1 1216 . 1 1 103 103 ALA HB2 H 1 1.05 0.03 . 1 . . . . . . . . 4327 1 1217 . 1 1 103 103 ALA HB3 H 1 1.05 0.03 . 1 . . . . . . . . 4327 1 1218 . 1 1 103 103 ALA CA C 13 49.78 0.1 . 1 . . . . . . . . 4327 1 1219 . 1 1 103 103 ALA CB C 13 21.23 0.1 . 1 . . . . . . . . 4327 1 1220 . 1 1 103 103 ALA N N 15 128.33 0.01 . 1 . . . . . . . . 4327 1 1221 . 1 1 104 104 PRO HA H 1 3.81 0.03 . 1 . . . . . . . . 4327 1 1222 . 1 1 104 104 PRO HB2 H 1 1.72 0.03 . 2 . . . . . . . . 4327 1 1223 . 1 1 104 104 PRO HB3 H 1 2.01 0.03 . 2 . . . . . . . . 4327 1 1224 . 1 1 104 104 PRO HG2 H 1 2.12 0.03 . 1 . . . . . . . . 4327 1 1225 . 1 1 104 104 PRO HG3 H 1 2.12 0.03 . 1 . . . . . . . . 4327 1 1226 . 1 1 104 104 PRO HD2 H 1 3.58 0.03 . 2 . . . . . . . . 4327 1 1227 . 1 1 104 104 PRO HD3 H 1 3.96 0.03 . 2 . . . . . . . . 4327 1 1228 . 1 1 104 104 PRO C C 13 178.52 0.1 . 1 . . . . . . . . 4327 1 1229 . 1 1 104 104 PRO CA C 13 62.22 0.1 . 1 . . . . . . . . 4327 1 1230 . 1 1 104 104 PRO CB C 13 30.73 0.1 . 1 . . . . . . . . 4327 1 1231 . 1 1 104 104 PRO CG C 13 27.12 0.1 . 1 . . . . . . . . 4327 1 1232 . 1 1 104 104 PRO CD C 13 50.18 0.1 . 1 . . . . . . . . 4327 1 1233 . 1 1 105 105 TRP H H 1 9.02 0.03 . 1 . . . . . . . . 4327 1 1234 . 1 1 105 105 TRP HA H 1 4.24 0.03 . 1 . . . . . . . . 4327 1 1235 . 1 1 105 105 TRP HB2 H 1 2.81 0.03 . 2 . . . . . . . . 4327 1 1236 . 1 1 105 105 TRP HB3 H 1 2.94 0.03 . 2 . . . . . . . . 4327 1 1237 . 1 1 105 105 TRP HD1 H 1 7.14 0.03 . 1 . . . . . . . . 4327 1 1238 . 1 1 105 105 TRP HE1 H 1 10.17 0.03 . 1 . . . . . . . . 4327 1 1239 . 1 1 105 105 TRP HE3 H 1 6.71 0.03 . 4 . . . . . . . . 4327 1 1240 . 1 1 105 105 TRP HZ2 H 1 7.51 0.03 . 1 . . . . . . . . 4327 1 1241 . 1 1 105 105 TRP HZ3 H 1 7.27 0.03 . 4 . . . . . . . . 4327 1 1242 . 1 1 105 105 TRP HH2 H 1 7.09 0.03 . 1 . . . . . . . . 4327 1 1243 . 1 1 105 105 TRP C C 13 176.7 0.1 . 1 . . . . . . . . 4327 1 1244 . 1 1 105 105 TRP CA C 13 59.95 0.1 . 1 . . . . . . . . 4327 1 1245 . 1 1 105 105 TRP CB C 13 30.15 0.1 . 1 . . . . . . . . 4327 1 1246 . 1 1 105 105 TRP CD1 C 13 128.08 0.1 . 1 . . . . . . . . 4327 1 1247 . 1 1 105 105 TRP CE3 C 13 120.59 0.1 . 4 . . . . . . . . 4327 1 1248 . 1 1 105 105 TRP CZ2 C 13 114.44 0.1 . 1 . . . . . . . . 4327 1 1249 . 1 1 105 105 TRP CZ3 C 13 119.97 0.1 . 4 . . . . . . . . 4327 1 1250 . 1 1 105 105 TRP CH2 C 13 124.67 0.1 . 1 . . . . . . . . 4327 1 1251 . 1 1 105 105 TRP N N 15 131.39 0.01 . 1 . . . . . . . . 4327 1 1252 . 1 1 105 105 TRP NE1 N 15 130.52 0.01 . 1 . . . . . . . . 4327 1 1253 . 1 1 106 106 ASN H H 1 9.09 0.03 . 1 . . . . . . . . 4327 1 1254 . 1 1 106 106 ASN HA H 1 4.35 0.03 . 1 . . . . . . . . 4327 1 1255 . 1 1 106 106 ASN HB2 H 1 2.71 0.03 . 2 . . . . . . . . 4327 1 1256 . 1 1 106 106 ASN HB3 H 1 2.89 0.03 . 2 . . . . . . . . 4327 1 1257 . 1 1 106 106 ASN HD21 H 1 7.69 0.03 . 2 . . . . . . . . 4327 1 1258 . 1 1 106 106 ASN HD22 H 1 6.95 0.03 . 2 . . . . . . . . 4327 1 1259 . 1 1 106 106 ASN C C 13 175.61 0.1 . 1 . . . . . . . . 4327 1 1260 . 1 1 106 106 ASN CA C 13 54.03 0.1 . 1 . . . . . . . . 4327 1 1261 . 1 1 106 106 ASN CB C 13 37.13 0.1 . 1 . . . . . . . . 4327 1 1262 . 1 1 106 106 ASN N N 15 112.64 0.01 . 1 . . . . . . . . 4327 1 1263 . 1 1 106 106 ASN ND2 N 15 112.09 0.01 . 1 . . . . . . . . 4327 1 1264 . 1 1 107 107 SER H H 1 7.56 0.03 . 1 . . . . . . . . 4327 1 1265 . 1 1 107 107 SER HA H 1 4.42 0.03 . 1 . . . . . . . . 4327 1 1266 . 1 1 107 107 SER HB2 H 1 3.89 0.03 . 2 . . . . . . . . 4327 1 1267 . 1 1 107 107 SER HB3 H 1 3.98 0.03 . 2 . . . . . . . . 4327 1 1268 . 1 1 107 107 SER C C 13 174.04 0.1 . 1 . . . . . . . . 4327 1 1269 . 1 1 107 107 SER CA C 13 58.75 0.1 . 1 . . . . . . . . 4327 1 1270 . 1 1 107 107 SER CB C 13 63.91 0.1 . 1 . . . . . . . . 4327 1 1271 . 1 1 107 107 SER N N 15 113.99 0.01 . 1 . . . . . . . . 4327 1 1272 . 1 1 108 108 LEU H H 1 7.12 0.03 . 1 . . . . . . . . 4327 1 1273 . 1 1 108 108 LEU HA H 1 4.44 0.03 . 1 . . . . . . . . 4327 1 1274 . 1 1 108 108 LEU HB2 H 1 1.36 0.03 . 2 . . . . . . . . 4327 1 1275 . 1 1 108 108 LEU HB3 H 1 1.52 0.03 . 2 . . . . . . . . 4327 1 1276 . 1 1 108 108 LEU HG H 1 1.93 0.03 . 1 . . . . . . . . 4327 1 1277 . 1 1 108 108 LEU HD11 H 1 0.8 0.03 . 1 . . . . . . . . 4327 1 1278 . 1 1 108 108 LEU HD12 H 1 0.8 0.03 . 1 . . . . . . . . 4327 1 1279 . 1 1 108 108 LEU HD13 H 1 0.8 0.03 . 1 . . . . . . . . 4327 1 1280 . 1 1 108 108 LEU HD21 H 1 0.97 0.03 . 1 . . . . . . . . 4327 1 1281 . 1 1 108 108 LEU HD22 H 1 0.97 0.03 . 1 . . . . . . . . 4327 1 1282 . 1 1 108 108 LEU HD23 H 1 0.97 0.03 . 1 . . . . . . . . 4327 1 1283 . 1 1 108 108 LEU C C 13 177.53 0.1 . 1 . . . . . . . . 4327 1 1284 . 1 1 108 108 LEU CA C 13 53.88 0.1 . 1 . . . . . . . . 4327 1 1285 . 1 1 108 108 LEU CB C 13 41.72 0.1 . 1 . . . . . . . . 4327 1 1286 . 1 1 108 108 LEU CG C 13 25.94 0.1 . 1 . . . . . . . . 4327 1 1287 . 1 1 108 108 LEU CD1 C 13 27.12 0.1 . 1 . . . . . . . . 4327 1 1288 . 1 1 108 108 LEU CD2 C 13 22.65 0.1 . 1 . . . . . . . . 4327 1 1289 . 1 1 108 108 LEU N N 15 123.5 0.01 . 1 . . . . . . . . 4327 1 1290 . 1 1 109 109 SER H H 1 8.63 0.03 . 1 . . . . . . . . 4327 1 1291 . 1 1 109 109 SER HA H 1 4.4 0.03 . 1 . . . . . . . . 4327 1 1292 . 1 1 109 109 SER HB2 H 1 3.95 0.03 . 2 . . . . . . . . 4327 1 1293 . 1 1 109 109 SER HB3 H 1 4.33 0.03 . 2 . . . . . . . . 4327 1 1294 . 1 1 109 109 SER C C 13 174.65 0.1 . 1 . . . . . . . . 4327 1 1295 . 1 1 109 109 SER CA C 13 56.57 0.1 . 1 . . . . . . . . 4327 1 1296 . 1 1 109 109 SER CB C 13 64.75 0.1 . 1 . . . . . . . . 4327 1 1297 . 1 1 109 109 SER N N 15 119.97 0.01 . 1 . . . . . . . . 4327 1 1298 . 1 1 110 110 LEU H H 1 8.82 0.03 . 1 . . . . . . . . 4327 1 1299 . 1 1 110 110 LEU HA H 1 3.81 0.03 . 1 . . . . . . . . 4327 1 1300 . 1 1 110 110 LEU HB2 H 1 1.58 0.03 . 2 . . . . . . . . 4327 1 1301 . 1 1 110 110 LEU HB3 H 1 1.64 0.03 . 2 . . . . . . . . 4327 1 1302 . 1 1 110 110 LEU HG H 1 1.58 0.03 . 1 . . . . . . . . 4327 1 1303 . 1 1 110 110 LEU HD11 H 1 0.91 0.03 . 1 . . . . . . . . 4327 1 1304 . 1 1 110 110 LEU HD12 H 1 0.91 0.03 . 1 . . . . . . . . 4327 1 1305 . 1 1 110 110 LEU HD13 H 1 0.91 0.03 . 1 . . . . . . . . 4327 1 1306 . 1 1 110 110 LEU HD21 H 1 0.83 0.03 . 1 . . . . . . . . 4327 1 1307 . 1 1 110 110 LEU HD22 H 1 0.83 0.03 . 1 . . . . . . . . 4327 1 1308 . 1 1 110 110 LEU HD23 H 1 0.83 0.03 . 1 . . . . . . . . 4327 1 1309 . 1 1 110 110 LEU C C 13 179.01 0.1 . 1 . . . . . . . . 4327 1 1310 . 1 1 110 110 LEU CA C 13 58.56 0.1 . 1 . . . . . . . . 4327 1 1311 . 1 1 110 110 LEU CB C 13 40.53 0.1 . 1 . . . . . . . . 4327 1 1312 . 1 1 110 110 LEU CG C 13 26.98 0.1 . 1 . . . . . . . . 4327 1 1313 . 1 1 110 110 LEU CD1 C 13 23.99 0.1 . 1 . . . . . . . . 4327 1 1314 . 1 1 110 110 LEU CD2 C 13 23.71 0.1 . 1 . . . . . . . . 4327 1 1315 . 1 1 110 110 LEU N N 15 123.13 0.01 . 1 . . . . . . . . 4327 1 1316 . 1 1 111 111 ALA H H 1 8.37 0.03 . 1 . . . . . . . . 4327 1 1317 . 1 1 111 111 ALA HA H 1 3.88 0.03 . 1 . . . . . . . . 4327 1 1318 . 1 1 111 111 ALA HB1 H 1 1.31 0.03 . 1 . . . . . . . . 4327 1 1319 . 1 1 111 111 ALA HB2 H 1 1.31 0.03 . 1 . . . . . . . . 4327 1 1320 . 1 1 111 111 ALA HB3 H 1 1.31 0.03 . 1 . . . . . . . . 4327 1 1321 . 1 1 111 111 ALA C C 13 180.88 0.1 . 1 . . . . . . . . 4327 1 1322 . 1 1 111 111 ALA CA C 13 54.8 0.1 . 1 . . . . . . . . 4327 1 1323 . 1 1 111 111 ALA CB C 13 17.99 0.1 . 1 . . . . . . . . 4327 1 1324 . 1 1 111 111 ALA N N 15 120.56 0.01 . 1 . . . . . . . . 4327 1 1325 . 1 1 112 112 GLN H H 1 7.61 0.03 . 1 . . . . . . . . 4327 1 1326 . 1 1 112 112 GLN HA H 1 4.11 0.03 . 1 . . . . . . . . 4327 1 1327 . 1 1 112 112 GLN HB2 H 1 1.7 0.03 . 1 . . . . . . . . 4327 1 1328 . 1 1 112 112 GLN HB3 H 1 1.7 0.03 . 1 . . . . . . . . 4327 1 1329 . 1 1 112 112 GLN HG2 H 1 2.37 0.03 . 1 . . . . . . . . 4327 1 1330 . 1 1 112 112 GLN HG3 H 1 2.37 0.03 . 1 . . . . . . . . 4327 1 1331 . 1 1 112 112 GLN HE21 H 1 7.3 0.03 . 2 . . . . . . . . 4327 1 1332 . 1 1 112 112 GLN HE22 H 1 6.86 0.03 . 2 . . . . . . . . 4327 1 1333 . 1 1 112 112 GLN C C 13 177.91 0.1 . 1 . . . . . . . . 4327 1 1334 . 1 1 112 112 GLN CA C 13 57.58 0.1 . 1 . . . . . . . . 4327 1 1335 . 1 1 112 112 GLN CB C 13 28.21 0.1 . 1 . . . . . . . . 4327 1 1336 . 1 1 112 112 GLN CG C 13 33.47 0.1 . 1 . . . . . . . . 4327 1 1337 . 1 1 112 112 GLN N N 15 119.53 0.01 . 1 . . . . . . . . 4327 1 1338 . 1 1 112 112 GLN NE2 N 15 110.19 0.01 . 1 . . . . . . . . 4327 1 1339 . 1 1 113 113 ARG H H 1 8.39 0.03 . 1 . . . . . . . . 4327 1 1340 . 1 1 113 113 ARG HA H 1 3.68 0.03 . 1 . . . . . . . . 4327 1 1341 . 1 1 113 113 ARG HB2 H 1 1.68 0.03 . 2 . . . . . . . . 4327 1 1342 . 1 1 113 113 ARG HB3 H 1 1.73 0.03 . 2 . . . . . . . . 4327 1 1343 . 1 1 113 113 ARG HG2 H 1 1.21 0.03 . 1 . . . . . . . . 4327 1 1344 . 1 1 113 113 ARG HG3 H 1 1.21 0.03 . 1 . . . . . . . . 4327 1 1345 . 1 1 113 113 ARG HD2 H 1 2.53 0.03 . 1 . . . . . . . . 4327 1 1346 . 1 1 113 113 ARG HD3 H 1 2.53 0.03 . 1 . . . . . . . . 4327 1 1347 . 1 1 113 113 ARG C C 13 179.45 0.1 . 1 . . . . . . . . 4327 1 1348 . 1 1 113 113 ARG CA C 13 60.4 0.1 . 1 . . . . . . . . 4327 1 1349 . 1 1 113 113 ARG CB C 13 30.08 0.1 . 1 . . . . . . . . 4327 1 1350 . 1 1 113 113 ARG CG C 13 28.3 0.1 . 1 . . . . . . . . 4327 1 1351 . 1 1 113 113 ARG CD C 13 43.31 0.1 . 1 . . . . . . . . 4327 1 1352 . 1 1 113 113 ARG N N 15 119.7 0.01 . 1 . . . . . . . . 4327 1 1353 . 1 1 114 114 ARG H H 1 8.34 0.03 . 1 . . . . . . . . 4327 1 1354 . 1 1 114 114 ARG HA H 1 3.93 0.03 . 1 . . . . . . . . 4327 1 1355 . 1 1 114 114 ARG HB2 H 1 1.73 0.03 . 1 . . . . . . . . 4327 1 1356 . 1 1 114 114 ARG HB3 H 1 1.73 0.03 . 1 . . . . . . . . 4327 1 1357 . 1 1 114 114 ARG HG2 H 1 1.59 0.03 . 2 . . . . . . . . 4327 1 1358 . 1 1 114 114 ARG HG3 H 1 1.71 0.03 . 2 . . . . . . . . 4327 1 1359 . 1 1 114 114 ARG HD2 H 1 3.08 0.03 . 1 . . . . . . . . 4327 1 1360 . 1 1 114 114 ARG HD3 H 1 3.08 0.03 . 1 . . . . . . . . 4327 1 1361 . 1 1 114 114 ARG C C 13 178.22 0.1 . 1 . . . . . . . . 4327 1 1362 . 1 1 114 114 ARG CA C 13 58.47 0.1 . 1 . . . . . . . . 4327 1 1363 . 1 1 114 114 ARG CB C 13 29.56 0.1 . 1 . . . . . . . . 4327 1 1364 . 1 1 114 114 ARG CG C 13 27.2 0.1 . 1 . . . . . . . . 4327 1 1365 . 1 1 114 114 ARG CD C 13 43.31 0.1 . 1 . . . . . . . . 4327 1 1366 . 1 1 114 114 ARG N N 15 120.94 0.01 . 1 . . . . . . . . 4327 1 1367 . 1 1 115 115 GLY H H 1 7.53 0.03 . 1 . . . . . . . . 4327 1 1368 . 1 1 115 115 GLY HA2 H 1 3.38 0.03 . 2 . . . . . . . . 4327 1 1369 . 1 1 115 115 GLY HA3 H 1 4.09 0.03 . 2 . . . . . . . . 4327 1 1370 . 1 1 115 115 GLY C C 13 175.85 0.1 . 1 . . . . . . . . 4327 1 1371 . 1 1 115 115 GLY CA C 13 44.2 0.1 . 1 . . . . . . . . 4327 1 1372 . 1 1 115 115 GLY N N 15 112.09 0.01 . 1 . . . . . . . . 4327 1 1373 . 1 1 116 116 PHE H H 1 7.78 0.03 . 1 . . . . . . . . 4327 1 1374 . 1 1 116 116 PHE HA H 1 3.84 0.03 . 1 . . . . . . . . 4327 1 1375 . 1 1 116 116 PHE HB2 H 1 2.65 0.03 . 1 . . . . . . . . 4327 1 1376 . 1 1 116 116 PHE HB3 H 1 2.65 0.03 . 1 . . . . . . . . 4327 1 1377 . 1 1 116 116 PHE HD1 H 1 7.37 0.03 . 1 . . . . . . . . 4327 1 1378 . 1 1 116 116 PHE HD2 H 1 7.37 0.03 . 1 . . . . . . . . 4327 1 1379 . 1 1 116 116 PHE HE1 H 1 7.14 0.03 . 1 . . . . . . . . 4327 1 1380 . 1 1 116 116 PHE HE2 H 1 7.14 0.03 . 1 . . . . . . . . 4327 1 1381 . 1 1 116 116 PHE HZ H 1 6.6 0.03 . 1 . . . . . . . . 4327 1 1382 . 1 1 116 116 PHE C C 13 175.01 0.1 . 1 . . . . . . . . 4327 1 1383 . 1 1 116 116 PHE CA C 13 62.88 0.1 . 1 . . . . . . . . 4327 1 1384 . 1 1 116 116 PHE CB C 13 38.3 0.1 . 1 . . . . . . . . 4327 1 1385 . 1 1 116 116 PHE CD1 C 13 131.67 0.1 . 1 . . . . . . . . 4327 1 1386 . 1 1 116 116 PHE CD2 C 13 131.67 0.1 . 1 . . . . . . . . 4327 1 1387 . 1 1 116 116 PHE CE1 C 13 130.23 0.1 . 1 . . . . . . . . 4327 1 1388 . 1 1 116 116 PHE CE2 C 13 130.23 0.1 . 1 . . . . . . . . 4327 1 1389 . 1 1 116 116 PHE CZ C 13 130.27 0.1 . 1 . . . . . . . . 4327 1 1390 . 1 1 116 116 PHE N N 15 120.27 0.01 . 1 . . . . . . . . 4327 1 1391 . 1 1 117 117 THR H H 1 7.6 0.03 . 1 . . . . . . . . 4327 1 1392 . 1 1 117 117 THR HA H 1 3.89 0.03 . 1 . . . . . . . . 4327 1 1393 . 1 1 117 117 THR HB H 1 4.2 0.03 . 1 . . . . . . . . 4327 1 1394 . 1 1 117 117 THR HG21 H 1 1.37 0.03 . 1 . . . . . . . . 4327 1 1395 . 1 1 117 117 THR HG22 H 1 1.37 0.03 . 1 . . . . . . . . 4327 1 1396 . 1 1 117 117 THR HG23 H 1 1.37 0.03 . 1 . . . . . . . . 4327 1 1397 . 1 1 117 117 THR C C 13 175.19 0.1 . 1 . . . . . . . . 4327 1 1398 . 1 1 117 117 THR CA C 13 64.29 0.1 . 1 . . . . . . . . 4327 1 1399 . 1 1 117 117 THR CB C 13 69.41 0.1 . 1 . . . . . . . . 4327 1 1400 . 1 1 117 117 THR CG2 C 13 21.8 0.1 . 1 . . . . . . . . 4327 1 1401 . 1 1 117 117 THR N N 15 107.11 0.01 . 1 . . . . . . . . 4327 1 1402 . 1 1 118 118 LYS H H 1 7.96 0.03 . 1 . . . . . . . . 4327 1 1403 . 1 1 118 118 LYS HA H 1 4.6 0.03 . 1 . . . . . . . . 4327 1 1404 . 1 1 118 118 LYS HB2 H 1 1.75 0.03 . 2 . . . . . . . . 4327 1 1405 . 1 1 118 118 LYS HB3 H 1 1.81 0.03 . 2 . . . . . . . . 4327 1 1406 . 1 1 118 118 LYS HG2 H 1 1.26 0.03 . 2 . . . . . . . . 4327 1 1407 . 1 1 118 118 LYS HG3 H 1 1.34 0.03 . 2 . . . . . . . . 4327 1 1408 . 1 1 118 118 LYS HD2 H 1 1.65 0.03 . 1 . . . . . . . . 4327 1 1409 . 1 1 118 118 LYS HD3 H 1 1.65 0.03 . 1 . . . . . . . . 4327 1 1410 . 1 1 118 118 LYS HE2 H 1 2.94 0.03 . 1 . . . . . . . . 4327 1 1411 . 1 1 118 118 LYS HE3 H 1 2.94 0.03 . 1 . . . . . . . . 4327 1 1412 . 1 1 118 118 LYS C C 13 176.63 0.1 . 1 . . . . . . . . 4327 1 1413 . 1 1 118 118 LYS CA C 13 58.81 0.1 . 1 . . . . . . . . 4327 1 1414 . 1 1 118 118 LYS CB C 13 36.23 0.1 . 1 . . . . . . . . 4327 1 1415 . 1 1 118 118 LYS CG C 13 24.51 0.1 . 1 . . . . . . . . 4327 1 1416 . 1 1 118 118 LYS CD C 13 28.79 0.1 . 1 . . . . . . . . 4327 1 1417 . 1 1 118 118 LYS CE C 13 41.91 0.1 . 1 . . . . . . . . 4327 1 1418 . 1 1 118 118 LYS N N 15 120.03 0.01 . 1 . . . . . . . . 4327 1 1419 . 1 1 119 119 THR H H 1 8.14 0.03 . 1 . . . . . . . . 4327 1 1420 . 1 1 119 119 THR HA H 1 4.2 0.03 . 1 . . . . . . . . 4327 1 1421 . 1 1 119 119 THR HB H 1 4.22 0.03 . 1 . . . . . . . . 4327 1 1422 . 1 1 119 119 THR HG21 H 1 1.05 0.03 . 1 . . . . . . . . 4327 1 1423 . 1 1 119 119 THR HG22 H 1 1.05 0.03 . 1 . . . . . . . . 4327 1 1424 . 1 1 119 119 THR HG23 H 1 1.05 0.03 . 1 . . . . . . . . 4327 1 1425 . 1 1 119 119 THR C C 13 177.44 0.1 . 1 . . . . . . . . 4327 1 1426 . 1 1 119 119 THR CA C 13 64.84 0.1 . 1 . . . . . . . . 4327 1 1427 . 1 1 119 119 THR CB C 13 68.5 0.1 . 1 . . . . . . . . 4327 1 1428 . 1 1 119 119 THR CG2 C 13 22.2 0.1 . 1 . . . . . . . . 4327 1 1429 . 1 1 119 119 THR N N 15 111.04 0.01 . 1 . . . . . . . . 4327 1 1430 . 1 1 120 120 TYR H H 1 9.43 0.03 . 1 . . . . . . . . 4327 1 1431 . 1 1 120 120 TYR HA H 1 4.63 0.03 . 1 . . . . . . . . 4327 1 1432 . 1 1 120 120 TYR HB2 H 1 1.52 0.03 . 2 . . . . . . . . 4327 1 1433 . 1 1 120 120 TYR HB3 H 1 2.31 0.03 . 2 . . . . . . . . 4327 1 1434 . 1 1 120 120 TYR HD1 H 1 6.1 0.03 . 1 . . . . . . . . 4327 1 1435 . 1 1 120 120 TYR HD2 H 1 6.1 0.03 . 1 . . . . . . . . 4327 1 1436 . 1 1 120 120 TYR HE1 H 1 5.73 0.03 . 1 . . . . . . . . 4327 1 1437 . 1 1 120 120 TYR HE2 H 1 5.73 0.03 . 1 . . . . . . . . 4327 1 1438 . 1 1 120 120 TYR C C 13 178.66 0.1 . 1 . . . . . . . . 4327 1 1439 . 1 1 120 120 TYR CA C 13 56.05 0.1 . 1 . . . . . . . . 4327 1 1440 . 1 1 120 120 TYR CB C 13 34.87 0.1 . 1 . . . . . . . . 4327 1 1441 . 1 1 120 120 TYR CD1 C 13 130.22 0.1 . 1 . . . . . . . . 4327 1 1442 . 1 1 120 120 TYR CD2 C 13 130.22 0.1 . 1 . . . . . . . . 4327 1 1443 . 1 1 120 120 TYR CE1 C 13 117.53 0.1 . 1 . . . . . . . . 4327 1 1444 . 1 1 120 120 TYR CE2 C 13 117.53 0.1 . 1 . . . . . . . . 4327 1 1445 . 1 1 120 120 TYR N N 15 124.79 0.01 . 1 . . . . . . . . 4327 1 1446 . 1 1 121 121 THR H H 1 8.04 0.03 . 1 . . . . . . . . 4327 1 1447 . 1 1 121 121 THR HA H 1 4.16 0.03 . 1 . . . . . . . . 4327 1 1448 . 1 1 121 121 THR HB H 1 4.25 0.03 . 1 . . . . . . . . 4327 1 1449 . 1 1 121 121 THR HG21 H 1 1.35 0.03 . 1 . . . . . . . . 4327 1 1450 . 1 1 121 121 THR HG22 H 1 1.35 0.03 . 1 . . . . . . . . 4327 1 1451 . 1 1 121 121 THR HG23 H 1 1.35 0.03 . 1 . . . . . . . . 4327 1 1452 . 1 1 121 121 THR C C 13 175.6 0.1 . 1 . . . . . . . . 4327 1 1453 . 1 1 121 121 THR CA C 13 64.72 0.1 . 1 . . . . . . . . 4327 1 1454 . 1 1 121 121 THR CB C 13 68.3 0.1 . 1 . . . . . . . . 4327 1 1455 . 1 1 121 121 THR CG2 C 13 21.1 0.1 . 1 . . . . . . . . 4327 1 1456 . 1 1 121 121 THR N N 15 113.18 0.01 . 1 . . . . . . . . 4327 1 1457 . 1 1 122 122 VAL H H 1 6.95 0.03 . 1 . . . . . . . . 4327 1 1458 . 1 1 122 122 VAL HA H 1 4.14 0.03 . 1 . . . . . . . . 4327 1 1459 . 1 1 122 122 VAL HB H 1 2.26 0.03 . 1 . . . . . . . . 4327 1 1460 . 1 1 122 122 VAL HG11 H 1 0.97 0.03 . 1 . . . . . . . . 4327 1 1461 . 1 1 122 122 VAL HG12 H 1 0.97 0.03 . 1 . . . . . . . . 4327 1 1462 . 1 1 122 122 VAL HG13 H 1 0.97 0.03 . 1 . . . . . . . . 4327 1 1463 . 1 1 122 122 VAL HG21 H 1 0.99 0.03 . 1 . . . . . . . . 4327 1 1464 . 1 1 122 122 VAL HG22 H 1 0.99 0.03 . 1 . . . . . . . . 4327 1 1465 . 1 1 122 122 VAL HG23 H 1 0.99 0.03 . 1 . . . . . . . . 4327 1 1466 . 1 1 122 122 VAL C C 13 177.16 0.1 . 1 . . . . . . . . 4327 1 1467 . 1 1 122 122 VAL CA C 13 63.25 0.1 . 1 . . . . . . . . 4327 1 1468 . 1 1 122 122 VAL CB C 13 31.25 0.1 . 1 . . . . . . . . 4327 1 1469 . 1 1 122 122 VAL CG1 C 13 21.12 0.1 . 1 . . . . . . . . 4327 1 1470 . 1 1 122 122 VAL CG2 C 13 20.67 0.1 . 1 . . . . . . . . 4327 1 1471 . 1 1 122 122 VAL N N 15 118.01 0.01 . 1 . . . . . . . . 4327 1 1472 . 1 1 123 123 GLY H H 1 7.89 0.03 . 1 . . . . . . . . 4327 1 1473 . 1 1 123 123 GLY HA2 H 1 3.81 0.03 . 2 . . . . . . . . 4327 1 1474 . 1 1 123 123 GLY HA3 H 1 4.21 0.03 . 2 . . . . . . . . 4327 1 1475 . 1 1 123 123 GLY C C 13 174.68 0.1 . 1 . . . . . . . . 4327 1 1476 . 1 1 123 123 GLY CA C 13 45.06 0.1 . 1 . . . . . . . . 4327 1 1477 . 1 1 123 123 GLY N N 15 108.72 0.01 . 1 . . . . . . . . 4327 1 1478 . 1 1 124 124 CYS H H 1 7.75 0.03 . 1 . . . . . . . . 4327 1 1479 . 1 1 124 124 CYS HA H 1 4.85 0.03 . 1 . . . . . . . . 4327 1 1480 . 1 1 124 124 CYS HB2 H 1 3.02 0.03 . 2 . . . . . . . . 4327 1 1481 . 1 1 124 124 CYS HB3 H 1 3.5 0.03 . 2 . . . . . . . . 4327 1 1482 . 1 1 124 124 CYS C C 13 174.9 0.1 . 1 . . . . . . . . 4327 1 1483 . 1 1 124 124 CYS CA C 13 53.57 0.1 . 1 . . . . . . . . 4327 1 1484 . 1 1 124 124 CYS CB C 13 37.46 0.1 . 1 . . . . . . . . 4327 1 1485 . 1 1 124 124 CYS N N 15 118.03 0.01 . 1 . . . . . . . . 4327 1 1486 . 1 1 125 125 GLU H H 1 8.37 0.03 . 1 . . . . . . . . 4327 1 1487 . 1 1 125 125 GLU HA H 1 4.35 0.03 . 1 . . . . . . . . 4327 1 1488 . 1 1 125 125 GLU HB2 H 1 1.97 0.03 . 2 . . . . . . . . 4327 1 1489 . 1 1 125 125 GLU HB3 H 1 2.11 0.03 . 2 . . . . . . . . 4327 1 1490 . 1 1 125 125 GLU HG2 H 1 2.31 0.03 . 2 . . . . . . . . 4327 1 1491 . 1 1 125 125 GLU HG3 H 1 2.36 0.03 . 2 . . . . . . . . 4327 1 1492 . 1 1 125 125 GLU C C 13 175.34 0.1 . 1 . . . . . . . . 4327 1 1493 . 1 1 125 125 GLU CA C 13 56.39 0.1 . 1 . . . . . . . . 4327 1 1494 . 1 1 125 125 GLU CB C 13 30.08 0.1 . 1 . . . . . . . . 4327 1 1495 . 1 1 125 125 GLU CG C 13 36.12 0.1 . 1 . . . . . . . . 4327 1 1496 . 1 1 125 125 GLU N N 15 122.44 0.01 . 1 . . . . . . . . 4327 1 1497 . 1 1 126 126 GLU H H 1 8.01 0.03 . 1 . . . . . . . . 4327 1 1498 . 1 1 126 126 GLU HA H 1 4.12 0.03 . 1 . . . . . . . . 4327 1 1499 . 1 1 126 126 GLU HB2 H 1 1.9 0.03 . 2 . . . . . . . . 4327 1 1500 . 1 1 126 126 GLU HB3 H 1 2.05 0.03 . 2 . . . . . . . . 4327 1 1501 . 1 1 126 126 GLU HG2 H 1 2.22 0.03 . 1 . . . . . . . . 4327 1 1502 . 1 1 126 126 GLU HG3 H 1 2.22 0.03 . 1 . . . . . . . . 4327 1 1503 . 1 1 126 126 GLU CA C 13 57.8 0.1 . 1 . . . . . . . . 4327 1 1504 . 1 1 126 126 GLU CB C 13 30.65 0.1 . 1 . . . . . . . . 4327 1 1505 . 1 1 126 126 GLU CG C 13 36.53 0.1 . 1 . . . . . . . . 4327 1 1506 . 1 1 126 126 GLU N N 15 127.46 0.01 . 1 . . . . . . . . 4327 1 stop_ save_