data_5785 ####################### # Entry information # ####################### save_entry_information _Entry.Sf_category entry_information _Entry.Sf_framecode entry_information _Entry.ID 5785 _Entry.Title ; Global Orientation of Bound MMP-3 and N-TIMP-1 in Solution via Residual Dipolar Couplings ; _Entry.Type . _Entry.Version_type original _Entry.Submission_date 2003-04-25 _Entry.Accession_date 2003-04-25 _Entry.Last_release_date 2004-03-15 _Entry.Original_release_date 2004-03-15 _Entry.Origination author _Entry.NMR_STAR_version 3.1.1.61 _Entry.Original_NMR_STAR_version 2.1 _Entry.Experimental_method NMR _Entry.Experimental_method_subtype . _Entry.Details . _Entry.BMRB_internal_directory_name . loop_ _Entry_author.Ordinal _Entry_author.Given_name _Entry_author.Family_name _Entry_author.First_initial _Entry_author.Middle_initials _Entry_author.Family_title _Entry_author.Entry_ID 1 S. Arumugam . . . 5785 2 Steven 'Van Doren' . R. . 5785 stop_ loop_ _Data_set.Type _Data_set.Count _Data_set.Entry_ID assigned_chemical_shifts 1 5785 stop_ loop_ _Datum.Type _Datum.Count _Datum.Entry_ID '1H chemical shifts' 729 5785 '13C chemical shifts' 495 5785 '15N chemical shifts' 138 5785 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 . . 2004-03-15 2003-04-25 original author . 5785 stop_ loop_ _Related_entries.Database_name _Related_entries.Database_accession_code _Related_entries.Relationship _Related_entries.Entry_ID BMRB 5099 'backbone and sidechain resonance assignments for N-TIMP-1' 5785 BMRB 5153 'backbone dynamics data for N-TIMP-1' 5785 stop_ save_ ############### # Citations # ############### save_entry_citation _Citation.Sf_category citations _Citation.Sf_framecode entry_citation _Citation.Entry_ID 5785 _Citation.ID 1 _Citation.Class 'entry citation' _Citation.CAS_abstract_code . _Citation.MEDLINE_UI_code 22718511 _Citation.DOI . _Citation.PubMed_ID 12834347 _Citation.Full_citation . _Citation.Title ; Global Orientation of Bound MMP-3 and N-TIMP-1 in Solution via Residual Dipolar Couplings ; _Citation.Status published _Citation.Type journal _Citation.Journal_abbrev Biochemistry _Citation.Journal_name_full . _Citation.Journal_volume 42 _Citation.Journal_issue 26 _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 7950 _Citation.Page_last 7958 _Citation.Year 2003 _Citation.Details ; Most of the backbone assignments and nearly 80% of the side chain assignments of MMP-3 when in complex with N-TIMP-1. ; 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 S. Arumugam . . . 5785 1 2 Steven 'Van Doren' . R. . 5785 1 stop_ loop_ _Citation_keyword.Keyword _Citation_keyword.Entry_ID _Citation_keyword.Citation_ID 'MMP-3/N-TIMP-1 complex' 5785 1 stop_ save_ save_ref_1 _Citation.Sf_category citations _Citation.Sf_framecode ref_1 _Citation.Entry_ID 5785 _Citation.ID 2 _Citation.Class 'reference citation' _Citation.CAS_abstract_code . _Citation.MEDLINE_UI_code . _Citation.DOI . _Citation.PubMed_ID 9657677 _Citation.Full_citation ; Arumugam S, Hemme CL, Yoshida N, Suzuki K, Nagase H, Berjanskii M, Wu B, Van Doren SR. TIMP-1 contact sites and perturbations of stromelysin 1 mapped by NMR and a paramagnetic surface probe. Biochemistry. 1998 Jul 7;37(27):9650-7. ; _Citation.Title 'TIMP-1 contact sites and perturbations of stromelysin 1 mapped by NMR and a paramagnetic surface probe.' _Citation.Status published _Citation.Type journal _Citation.Journal_abbrev Biochemistry _Citation.Journal_name_full Biochemistry _Citation.Journal_volume 37 _Citation.Journal_issue 27 _Citation.Journal_ASTM . _Citation.Journal_ISSN 0006-2960 _Citation.Journal_CSD . _Citation.Book_title . _Citation.Book_chapter_title . _Citation.Book_volume . _Citation.Book_series . _Citation.Book_publisher . _Citation.Book_publisher_city . _Citation.Book_ISBN . _Citation.Conference_title . _Citation.Conference_site . _Citation.Conference_state_province . _Citation.Conference_country . _Citation.Conference_start_date . _Citation.Conference_end_date . _Citation.Conference_abstract_number . _Citation.Thesis_institution . _Citation.Thesis_institution_city . _Citation.Thesis_institution_country . _Citation.WWW_URL . _Citation.Page_first 9650 _Citation.Page_last 9657 _Citation.Year 1998 _Citation.Details ; Surfaces of the 173 residue catalytic domain of human matrix metalloproteinase 3 (MMP-3(DeltaC)) affected by binding of the N-terminal, 126 residue inhibitory domain of human TIMP-1 (N-TIMP-1) have been investigated using an amide-directed, NMR-based approach. The interface was mapped by a novel method that compares amide proton line broadening by paramagnetic Gd-EDTA in the presence and absence of the binding partner. The results are consistent with the X-ray model of the complex of MMP-3(DeltaC) with TIMP-1 (Gomis et al. (1997) Nature 389, 77-81). Residues Tyr155, Asn162, Val163, Leu164, His166, Ala167, Ala169, and Phe210 of MMP-3(DeltaC) are protected from broadening by the Gd-EDTA probe by binding to N-TIMP-1. N-TIMP-1-induced exposure of backbone amides of Asp238, Asn240, Gly241, and Ser244 of helix C of MMP-3(DeltaC) to Gd-EDTA confirms that the displacement of the N-terminus of MMP-3(DeltaC) occurs not only in the crystal but also in solution. These results validate comparative paramagnetic surface probing as a means of mapping protein-protein interfaces. Novel N-TIMP-1-dependent changes in hydrogen bonding near the active site of MMP-3(DeltaC) are reported. N-TIMP-1 binding causes the amide of Tyr223 of MMP-3(DeltaC) bound by N-TIMP-1 to exchange with water rapidly, implying a lack of the hydrogen bond observed in the crystal structure. The backbone amide proton of Asn162 becomes protected from rapid exchange upon forming a complex with N-TIMP-1 and could form a hydrogen bond to N-TIMP-1. N-TIMP-1 binding dramatically increases the rate of amide hydrogen exchange of Asp177 of the fifth beta strand of MMP-3(DeltaC), disrupting its otherwise stable hydrogen bond. ; 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 S. Arumugam S. . . 5785 2 2 'C. L.' Hemme C. L. . 5785 2 3 N. Yoshida N. . . 5785 2 4 K. Suzuki K. . . 5785 2 5 H. Nagase H. . . 5785 2 6 M. Berjanskii M. . . 5785 2 7 B. Wu B. . . 5785 2 8 'S. R.' 'Van Doren' S. R. . 5785 2 stop_ save_ ############################################# # Molecular system (assembly) description # ############################################# save_system_MMP-3_stromelysin-1 _Assembly.Sf_category assembly _Assembly.Sf_framecode system_MMP-3_stromelysin-1 _Assembly.Entry_ID 5785 _Assembly.ID 1 _Assembly.Name 'Matrix MetalloProteinase-3 in complex with N-TIMP-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 'all disulfide bound' _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 complex 5785 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 'Matrix MetalloProteinase-3 catalytic domain' 1 $MMP-3(DC) . . . native . . . . . 5785 1 2 'N-TIMP-1, inhibitor' 2 $N-TIMP-1 . . . native . . . . . 5785 1 3 'CALCIUM (II) ION, I' 3 $CA . . . native . . . . . 5785 1 4 'CALCIUM (II) ION, II' 3 $CA . . . native . . . . . 5785 1 5 'CALCIUM (II) ION, III' 3 $CA . . . native . . . . . 5785 1 6 'ZINC (II) ION, I' 4 $ZN . . . native . . . . . 5785 1 7 'ZINC (II) ION, II' 4 $ZN . . . native . . . . . 5785 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 . 2 . 2 CYS 1 1 SG . 2 . 2 CYS 70 70 SG . . . . . . . . . . 5785 1 2 disulfide single . 2 . 2 CYS 3 3 SG . 2 . 2 CYS 99 99 SG . . . . . . . . . . 5785 1 3 disulfide single . 2 . 2 CYS 13 13 SG . 2 . 2 CYS 124 124 SG . . . . . . . . . . 5785 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 1OO9 . . . . . 'Residue Glutamate-202 was not mutated to Glutamine in the complex studied here.' 5785 1 stop_ loop_ _Assembly_common_name.Name _Assembly_common_name.Type _Assembly_common_name.Entry_ID _Assembly_common_name.Assembly_ID 'Matrix MetalloProteinase-3 in complex with N-TIMP-1' system 5785 1 'MMP-3, stromelysin-1' abbreviation 5785 1 stop_ loop_ _Assembly_bio_function.Biological_function _Assembly_bio_function.Entry_ID _Assembly_bio_function.Assembly_ID 'MMP-3 - enzyme involved in wound healing, arthritis and some forms of cancer' 5785 1 'N-TIMP-1 inhibitor that binds to Matrix Metalloproteinases' 5785 1 stop_ save_ #################################### # Biological polymers and ligands # #################################### save_MMP-3(DC) _Entity.Sf_category entity _Entity.Sf_framecode MMP-3(DC) _Entity.Entry_ID 5785 _Entity.ID 1 _Entity.BMRB_code . _Entity.Name 'Matrix MetalloProteinases-3 or stromelysin 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 ; FRTFPGIPKWRKTHLTYRIV NYTPDLPKDAVDSAVEKALK VWEEVTPLTFSRLYEGEADI MISFAVREHGDFYPFDGPGN VLAHAYAPGPGINGDAHFDD DEQWTKDTTGTNLFLVAAHQ IGHSLGLFHSANTEALMYPL YHSLTDLTRFRLSQDDINGI QSLYGPPPDSPET ; _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 173 _Entity.Number_of_nonpolymer_components . _Entity.Paramagnetic . _Entity.Thiol_state 'not present' _Entity.Src_method . _Entity.Parent_entity_ID 1 _Entity.Fragment . _Entity.Mutation . _Entity.EC_number . _Entity.Calc_isoelectric_point . _Entity.Formula_weight 19492 _Entity.Formula_weight_exptl . _Entity.Formula_weight_exptl_meth . _Entity.Details . _Entity.DB_query_date . _Entity.DB_query_revised_last_date 2015-01-28 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 BMRB 4327 . N-TIMP-1 . . . . . 100.00 126 100.00 100.00 1.03e-89 . . . . 5785 1 2 no BMRB 5154 . N-TIMP-1 . . . . . 100.00 126 100.00 100.00 1.03e-89 . . . . 5785 1 3 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 1.03e-89 . . . . 5785 1 4 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 1.03e-89 . . . . 5785 1 5 no PDB 1UEA . "Mmp-3TIMP-1 Complex" . . . . . 100.00 184 98.41 98.41 2.54e-86 . . . . 5785 1 6 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 1.03e-89 . . . . 5785 1 7 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 3.02e-86 . . . . 5785 1 8 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 2.89e-87 . . . . 5785 1 9 no DBJ BAA01913 . "tissue inhibitor of metalloproteinases [Homo sapiens]" . . . . . 85.71 166 99.07 99.07 5.86e-72 . . . . 5785 1 10 no DBJ BAG34878 . "unnamed protein product [Homo sapiens]" . . . . . 100.00 207 100.00 100.00 2.01e-88 . . . . 5785 1 11 no DBJ BAG52016 . "unnamed protein product [Homo sapiens]" . . . . . 100.00 207 100.00 100.00 2.61e-88 . . . . 5785 1 12 no EMBL CAA26443 . "unnamed protein product [Homo sapiens]" . . . . . 100.00 207 100.00 100.00 2.53e-88 . . . . 5785 1 13 no EMBL CAA26902 . "unnamed protein product [Homo sapiens]" . . . . . 100.00 207 100.00 100.00 2.01e-88 . . . . 5785 1 14 no EMBL CAG28566 . "TIMP1 [Homo sapiens]" . . . . . 100.00 207 100.00 100.00 2.01e-88 . . . . 5785 1 15 no EMBL CAG46779 . "TIMP1 [Homo sapiens]" . . . . . 100.00 207 100.00 100.00 2.01e-88 . . . . 5785 1 16 no EMBL CAH90650 . "hypothetical protein [Pongo abelii]" . . . . . 100.00 207 100.00 100.00 2.01e-88 . . . . 5785 1 17 no GB AAA52436 . "prefibroblast collagenase inhibitor [Homo sapiens]" . . . . . 100.00 207 100.00 100.00 2.01e-88 . . . . 5785 1 18 no GB AAA63234 . "collagenase inhibitor [Homo sapiens]" . . . . . 100.00 207 100.00 100.00 2.01e-88 . . . . 5785 1 19 no GB AAA99943 . "metalloprotease-1 tissue inhibitor [Papio cynocephalus]" . . . . . 100.00 207 100.00 100.00 2.50e-88 . . . . 5785 1 20 no GB AAD14009 . "metalloproteinase inhibitor [Homo sapiens]" . . . . . 100.00 207 100.00 100.00 2.01e-88 . . . . 5785 1 21 no GB AAH00866 . "TIMP metallopeptidase inhibitor 1 [Homo sapiens]" . . . . . 100.00 207 100.00 100.00 2.01e-88 . . . . 5785 1 22 no PIR JC4303 . "matrix metalloproteinase-1 tissue inhibitor - baboon" . . . . . 100.00 207 100.00 100.00 2.50e-88 . . . . 5785 1 23 no PRF 1107278A . "erythroid potentiating activity" . . . . . 100.00 207 100.00 100.00 2.01e-88 . . . . 5785 1 24 no PRF 1308125A . "metalloproteinase inhibitor" . . . . . 100.00 207 100.00 100.00 2.01e-88 . . . . 5785 1 25 no REF NP_001028111 . "metalloproteinase inhibitor 1 precursor [Macaca mulatta]" . . . . . 100.00 207 99.21 99.21 7.27e-87 . . . . 5785 1 26 no REF NP_001125351 . "metalloproteinase inhibitor 1 precursor [Pongo abelii]" . . . . . 100.00 207 100.00 100.00 2.01e-88 . . . . 5785 1 27 no REF NP_003245 . "metalloproteinase inhibitor 1 precursor [Homo sapiens]" . . . . . 100.00 207 100.00 100.00 2.01e-88 . . . . 5785 1 28 no REF XP_003271098 . "PREDICTED: metalloproteinase inhibitor 1 [Nomascus leucogenys]" . . . . . 67.46 143 100.00 100.00 5.95e-55 . . . . 5785 1 29 no REF XP_003917687 . "PREDICTED: metalloproteinase inhibitor 1 [Papio anubis]" . . . . . 100.00 207 100.00 100.00 2.50e-88 . . . . 5785 1 30 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 2.01e-88 . . . . 5785 1 31 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 2.50e-88 . . . . 5785 1 32 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 2.01e-88 . . . . 5785 1 33 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 7.27e-87 . . . . 5785 1 stop_ loop_ _Entity_common_name.Name _Entity_common_name.Type _Entity_common_name.Entry_ID _Entity_common_name.Entity_ID 'Matrix MetalloProteinases-3 or stromelysin 1' common 5785 1 MMP-3 abbreviation 5785 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 83 PHE . 5785 1 2 84 ARG . 5785 1 3 85 THR . 5785 1 4 86 PHE . 5785 1 5 87 PRO . 5785 1 6 88 GLY . 5785 1 7 89 ILE . 5785 1 8 90 PRO . 5785 1 9 91 LYS . 5785 1 10 92 TRP . 5785 1 11 93 ARG . 5785 1 12 94 LYS . 5785 1 13 95 THR . 5785 1 14 96 HIS . 5785 1 15 97 LEU . 5785 1 16 98 THR . 5785 1 17 99 TYR . 5785 1 18 100 ARG . 5785 1 19 101 ILE . 5785 1 20 102 VAL . 5785 1 21 103 ASN . 5785 1 22 104 TYR . 5785 1 23 105 THR . 5785 1 24 106 PRO . 5785 1 25 107 ASP . 5785 1 26 108 LEU . 5785 1 27 109 PRO . 5785 1 28 110 LYS . 5785 1 29 111 ASP . 5785 1 30 112 ALA . 5785 1 31 113 VAL . 5785 1 32 114 ASP . 5785 1 33 115 SER . 5785 1 34 116 ALA . 5785 1 35 117 VAL . 5785 1 36 118 GLU . 5785 1 37 119 LYS . 5785 1 38 120 ALA . 5785 1 39 121 LEU . 5785 1 40 122 LYS . 5785 1 41 123 VAL . 5785 1 42 124 TRP . 5785 1 43 125 GLU . 5785 1 44 126 GLU . 5785 1 45 127 VAL . 5785 1 46 128 THR . 5785 1 47 129 PRO . 5785 1 48 130 LEU . 5785 1 49 131 THR . 5785 1 50 132 PHE . 5785 1 51 133 SER . 5785 1 52 134 ARG . 5785 1 53 135 LEU . 5785 1 54 136 TYR . 5785 1 55 137 GLU . 5785 1 56 138 GLY . 5785 1 57 139 GLU . 5785 1 58 140 ALA . 5785 1 59 141 ASP . 5785 1 60 142 ILE . 5785 1 61 143 MET . 5785 1 62 144 ILE . 5785 1 63 145 SER . 5785 1 64 146 PHE . 5785 1 65 147 ALA . 5785 1 66 148 VAL . 5785 1 67 149 ARG . 5785 1 68 150 GLU . 5785 1 69 151 HIS . 5785 1 70 152 GLY . 5785 1 71 153 ASP . 5785 1 72 154 PHE . 5785 1 73 155 TYR . 5785 1 74 156 PRO . 5785 1 75 157 PHE . 5785 1 76 158 ASP . 5785 1 77 159 GLY . 5785 1 78 160 PRO . 5785 1 79 161 GLY . 5785 1 80 162 ASN . 5785 1 81 163 VAL . 5785 1 82 164 LEU . 5785 1 83 165 ALA . 5785 1 84 166 HIS . 5785 1 85 167 ALA . 5785 1 86 168 TYR . 5785 1 87 169 ALA . 5785 1 88 170 PRO . 5785 1 89 171 GLY . 5785 1 90 172 PRO . 5785 1 91 173 GLY . 5785 1 92 174 ILE . 5785 1 93 175 ASN . 5785 1 94 176 GLY . 5785 1 95 177 ASP . 5785 1 96 178 ALA . 5785 1 97 179 HIS . 5785 1 98 180 PHE . 5785 1 99 181 ASP . 5785 1 100 182 ASP . 5785 1 101 183 ASP . 5785 1 102 184 GLU . 5785 1 103 185 GLN . 5785 1 104 186 TRP . 5785 1 105 187 THR . 5785 1 106 188 LYS . 5785 1 107 189 ASP . 5785 1 108 190 THR . 5785 1 109 191 THR . 5785 1 110 192 GLY . 5785 1 111 193 THR . 5785 1 112 194 ASN . 5785 1 113 195 LEU . 5785 1 114 196 PHE . 5785 1 115 197 LEU . 5785 1 116 198 VAL . 5785 1 117 199 ALA . 5785 1 118 200 ALA . 5785 1 119 201 HIS . 5785 1 120 202 GLN . 5785 1 121 203 ILE . 5785 1 122 204 GLY . 5785 1 123 205 HIS . 5785 1 124 206 SER . 5785 1 125 207 LEU . 5785 1 126 208 GLY . 5785 1 127 209 LEU . 5785 1 128 210 PHE . 5785 1 129 211 HIS . 5785 1 130 212 SER . 5785 1 131 213 ALA . 5785 1 132 214 ASN . 5785 1 133 215 THR . 5785 1 134 216 GLU . 5785 1 135 217 ALA . 5785 1 136 218 LEU . 5785 1 137 219 MET . 5785 1 138 220 TYR . 5785 1 139 221 PRO . 5785 1 140 222 LEU . 5785 1 141 223 TYR . 5785 1 142 224 HIS . 5785 1 143 225 SER . 5785 1 144 226 LEU . 5785 1 145 227 THR . 5785 1 146 228 ASP . 5785 1 147 229 LEU . 5785 1 148 230 THR . 5785 1 149 231 ARG . 5785 1 150 232 PHE . 5785 1 151 233 ARG . 5785 1 152 234 LEU . 5785 1 153 235 SER . 5785 1 154 236 GLN . 5785 1 155 237 ASP . 5785 1 156 238 ASP . 5785 1 157 239 ILE . 5785 1 158 240 ASN . 5785 1 159 241 GLY . 5785 1 160 242 ILE . 5785 1 161 243 GLN . 5785 1 162 244 SER . 5785 1 163 245 LEU . 5785 1 164 246 TYR . 5785 1 165 247 GLY . 5785 1 166 248 PRO . 5785 1 167 249 PRO . 5785 1 168 250 PRO . 5785 1 169 251 ASP . 5785 1 170 252 SER . 5785 1 171 253 PRO . 5785 1 172 254 GLU . 5785 1 173 255 THR . 5785 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 . PHE 1 1 5785 1 . ARG 2 2 5785 1 . THR 3 3 5785 1 . PHE 4 4 5785 1 . PRO 5 5 5785 1 . GLY 6 6 5785 1 . ILE 7 7 5785 1 . PRO 8 8 5785 1 . LYS 9 9 5785 1 . TRP 10 10 5785 1 . ARG 11 11 5785 1 . LYS 12 12 5785 1 . THR 13 13 5785 1 . HIS 14 14 5785 1 . LEU 15 15 5785 1 . THR 16 16 5785 1 . TYR 17 17 5785 1 . ARG 18 18 5785 1 . ILE 19 19 5785 1 . VAL 20 20 5785 1 . ASN 21 21 5785 1 . TYR 22 22 5785 1 . THR 23 23 5785 1 . PRO 24 24 5785 1 . ASP 25 25 5785 1 . LEU 26 26 5785 1 . PRO 27 27 5785 1 . LYS 28 28 5785 1 . ASP 29 29 5785 1 . ALA 30 30 5785 1 . VAL 31 31 5785 1 . ASP 32 32 5785 1 . SER 33 33 5785 1 . ALA 34 34 5785 1 . VAL 35 35 5785 1 . GLU 36 36 5785 1 . LYS 37 37 5785 1 . ALA 38 38 5785 1 . LEU 39 39 5785 1 . LYS 40 40 5785 1 . VAL 41 41 5785 1 . TRP 42 42 5785 1 . GLU 43 43 5785 1 . GLU 44 44 5785 1 . VAL 45 45 5785 1 . THR 46 46 5785 1 . PRO 47 47 5785 1 . LEU 48 48 5785 1 . THR 49 49 5785 1 . PHE 50 50 5785 1 . SER 51 51 5785 1 . ARG 52 52 5785 1 . LEU 53 53 5785 1 . TYR 54 54 5785 1 . GLU 55 55 5785 1 . GLY 56 56 5785 1 . GLU 57 57 5785 1 . ALA 58 58 5785 1 . ASP 59 59 5785 1 . ILE 60 60 5785 1 . MET 61 61 5785 1 . ILE 62 62 5785 1 . SER 63 63 5785 1 . PHE 64 64 5785 1 . ALA 65 65 5785 1 . VAL 66 66 5785 1 . ARG 67 67 5785 1 . GLU 68 68 5785 1 . HIS 69 69 5785 1 . GLY 70 70 5785 1 . ASP 71 71 5785 1 . PHE 72 72 5785 1 . TYR 73 73 5785 1 . PRO 74 74 5785 1 . PHE 75 75 5785 1 . ASP 76 76 5785 1 . GLY 77 77 5785 1 . PRO 78 78 5785 1 . GLY 79 79 5785 1 . ASN 80 80 5785 1 . VAL 81 81 5785 1 . LEU 82 82 5785 1 . ALA 83 83 5785 1 . HIS 84 84 5785 1 . ALA 85 85 5785 1 . TYR 86 86 5785 1 . ALA 87 87 5785 1 . PRO 88 88 5785 1 . GLY 89 89 5785 1 . PRO 90 90 5785 1 . GLY 91 91 5785 1 . ILE 92 92 5785 1 . ASN 93 93 5785 1 . GLY 94 94 5785 1 . ASP 95 95 5785 1 . ALA 96 96 5785 1 . HIS 97 97 5785 1 . PHE 98 98 5785 1 . ASP 99 99 5785 1 . ASP 100 100 5785 1 . ASP 101 101 5785 1 . GLU 102 102 5785 1 . GLN 103 103 5785 1 . TRP 104 104 5785 1 . THR 105 105 5785 1 . LYS 106 106 5785 1 . ASP 107 107 5785 1 . THR 108 108 5785 1 . THR 109 109 5785 1 . GLY 110 110 5785 1 . THR 111 111 5785 1 . ASN 112 112 5785 1 . LEU 113 113 5785 1 . PHE 114 114 5785 1 . LEU 115 115 5785 1 . VAL 116 116 5785 1 . ALA 117 117 5785 1 . ALA 118 118 5785 1 . HIS 119 119 5785 1 . GLN 120 120 5785 1 . ILE 121 121 5785 1 . GLY 122 122 5785 1 . HIS 123 123 5785 1 . SER 124 124 5785 1 . LEU 125 125 5785 1 . GLY 126 126 5785 1 . LEU 127 127 5785 1 . PHE 128 128 5785 1 . HIS 129 129 5785 1 . SER 130 130 5785 1 . ALA 131 131 5785 1 . ASN 132 132 5785 1 . THR 133 133 5785 1 . GLU 134 134 5785 1 . ALA 135 135 5785 1 . LEU 136 136 5785 1 . MET 137 137 5785 1 . TYR 138 138 5785 1 . PRO 139 139 5785 1 . LEU 140 140 5785 1 . TYR 141 141 5785 1 . HIS 142 142 5785 1 . SER 143 143 5785 1 . LEU 144 144 5785 1 . THR 145 145 5785 1 . ASP 146 146 5785 1 . LEU 147 147 5785 1 . THR 148 148 5785 1 . ARG 149 149 5785 1 . PHE 150 150 5785 1 . ARG 151 151 5785 1 . LEU 152 152 5785 1 . SER 153 153 5785 1 . GLN 154 154 5785 1 . ASP 155 155 5785 1 . ASP 156 156 5785 1 . ILE 157 157 5785 1 . ASN 158 158 5785 1 . GLY 159 159 5785 1 . ILE 160 160 5785 1 . GLN 161 161 5785 1 . SER 162 162 5785 1 . LEU 163 163 5785 1 . TYR 164 164 5785 1 . GLY 165 165 5785 1 . PRO 166 166 5785 1 . PRO 167 167 5785 1 . PRO 168 168 5785 1 . ASP 169 169 5785 1 . SER 170 170 5785 1 . PRO 171 171 5785 1 . GLU 172 172 5785 1 . THR 173 173 5785 1 stop_ save_ save_N-TIMP-1 _Entity.Sf_category entity _Entity.Sf_framecode N-TIMP-1 _Entity.Entry_ID 5785 _Entity.ID 2 _Entity.BMRB_code . _Entity.Name 'N-terminal domain of Tissue Inhibitor of MatrixmetalloProteinases-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 'all disulfide bound' _Entity.Src_method . _Entity.Parent_entity_ID 2 _Entity.Fragment . _Entity.Mutation . _Entity.EC_number . _Entity.Calc_isoelectric_point . _Entity.Formula_weight 14252 _Entity.Formula_weight_exptl . _Entity.Formula_weight_exptl_meth . _Entity.Details . _Entity.DB_query_date 2008-08-19 _Entity.DB_query_revised_last_date 2008-08-19 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 . . SWISS-PROT Q5RC60 . 'Metalloproteinase inhibitor 1 precursor (TIMP-1)' . . . . . 100.00 207 100.00 100.00 1.71e-70 . . . . 5785 2 . . SWISS-PROT Q95KL9 . 'Metalloproteinase inhibitor 1 precursor (TIMP-1)' . . . . . 100.00 207 99.21 99.21 2.67e-69 . . . . 5785 2 . . SWISS-PROT P01033 . 'Metalloproteinase inhibitor 1 precursor (Tissue inhibitor of metalloproteinases) (TIMP-1) (Erythroid-potentiating activity) (EPA) (Fibroblast collagenase inhibitor) (Collagenase inhibitor)' . . . . . 100.00 207 100.00 100.00 1.71e-70 . . . . 5785 2 . . SWISS-PROT P49061 . 'Metalloproteinase inhibitor 1 precursor (TIMP-1)' . . . . . 100.00 207 100.00 100.00 2.03e-70 . . . . 5785 2 . . REF NP_001028111 . 'tissue inhibitor of matrix metalloproteinase-1 [Macaca mulatta]' . . . . . 100.00 207 99.21 99.21 2.67e-69 . . . . 5785 2 . . REF NP_003245 . 'tissue inhibitor of metalloproteinase 1 precursor [Homo sapiens]' . . . . . 100.00 207 100.00 100.00 1.71e-70 . . . . 5785 2 . . PRF 1107278A . 'erythroid potentiating activity' . . . . . 100.00 207 100.00 100.00 1.71e-70 . . . . 5785 2 . . PRF 1308125A . 'metalloproteinase inhibitor' . . . . . 100.00 207 100.00 100.00 1.71e-70 . . . . 5785 2 . . GenBank AAH00866 . 'TIMP metallopeptidase inhibitor 1 [Homo sapiens]' . . . . . 100.00 207 100.00 100.00 1.71e-70 . . . . 5785 2 . . PIR JC4303 . 'matrix metalloproteinase-1 tissue inhibitor - baboon' . . . . . 100.00 207 100.00 100.00 2.03e-70 . . . . 5785 2 . . GenBank AAA99943 . 'metalloprotease-1 tissue inhibitor' . . . . . 100.00 207 100.00 100.00 2.03e-70 . . . . 5785 2 . . GenBank AAD14009 . 'metalloproteinase inhibitor [Homo sapiens]' . . . . . 100.00 207 100.00 100.00 1.71e-70 . . . . 5785 2 . . GenBank AAA52436 . 'prefibroblast collagenase inhibitor' . . . . . 100.00 207 100.00 100.00 1.71e-70 . . . . 5785 2 . . GenBank AAA63234 . 'collagenase inhibitor [Homo sapiens]' . . . . . 100.00 207 100.00 100.00 1.71e-70 . . . . 5785 2 . . EMBL CAG46779 . 'TIMP1 [Homo sapiens]' . . . . . 100.00 207 100.00 100.00 1.71e-70 . . . . 5785 2 . . EMBL CAH90650 . 'hypothetical protein [Pongo abelii]' . . . . . 100.00 207 100.00 100.00 1.71e-70 . . . . 5785 2 . . EMBL CAA26902 . 'unnamed protein product [Homo sapiens]' . . . . . 100.00 207 100.00 100.00 1.71e-70 . . . . 5785 2 . . EMBL CAG28566 . 'TIMP1 [Homo sapiens]' . . . . . 100.00 207 100.00 100.00 1.71e-70 . . . . 5785 2 . . DBJ BAG52016 . 'unnamed protein product [Homo sapiens]' . . . . . 100.00 207 100.00 100.00 2.09e-70 . . . . 5785 2 . . EMBL CAA26443 . 'unnamed protein product [Homo sapiens]' . . . . . 100.00 207 100.00 100.00 2.04e-70 . . . . 5785 2 . . DBJ BAA01913 . 'tissue inhibitor of metalloproteinases [Homo sapiens]' . . . . . 85.71 166 99.07 99.07 1.92e-57 . . . . 5785 2 . . DBJ BAG34878 . 'unnamed protein product [Homo sapiens]' . . . . . 100.00 207 100.00 100.00 1.71e-70 . . . . 5785 2 . . PDB 1UEA . 'Mmp-3TIMP-1 Complex' . . . . . 100.00 184 98.41 98.41 1.24e-68 . . . . 5785 2 . . 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 1.37e-70 . . . . 5785 2 . . 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 1.37e-70 . . . . 5785 2 . . 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 1.37e-70 . . . . 5785 2 . . BMRB 5153 . 'N-terminal domain of Tissue Inhibitor of Metalloproteinases-1' . . . . . 100.00 126 100.00 100.00 1.37e-70 . . . . 5785 2 . . BMRB 5154 . 'N-terminal domain of Tissue Inhibitor of Metalloproteinases-1' . . . . . 100.00 126 100.00 100.00 1.37e-70 . . . . 5785 2 . . BMRB 4327 . 'N-terminal inhibitory domain of human tissue inhibitor of metalloproteinases-1' . . . . . 100.00 126 100.00 100.00 1.37e-70 . . . . 5785 2 . . BMRB 5099 . 'N-terminus of Tissue Inhibitor of Metalloproteinases-1/Matrix MetalloProteinases-3(catalytic domain) complex' . . . . . 100.00 126 100.00 100.00 1.37e-70 . . . . 5785 2 stop_ loop_ _Entity_common_name.Name _Entity_common_name.Type _Entity_common_name.Entry_ID _Entity_common_name.Entity_ID 'N-terminal domain of Tissue Inhibitor of MatrixmetalloProteinases-1' common 5785 2 N-TIMP-1 abbreviation 5785 2 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 . 5785 2 2 . THR . 5785 2 3 . CYS . 5785 2 4 . VAL . 5785 2 5 . PRO . 5785 2 6 . PRO . 5785 2 7 . HIS . 5785 2 8 . PRO . 5785 2 9 . GLN . 5785 2 10 . THR . 5785 2 11 . ALA . 5785 2 12 . PHE . 5785 2 13 . CYS . 5785 2 14 . ASN . 5785 2 15 . SER . 5785 2 16 . ASP . 5785 2 17 . LEU . 5785 2 18 . VAL . 5785 2 19 . ILE . 5785 2 20 . ARG . 5785 2 21 . ALA . 5785 2 22 . LYS . 5785 2 23 . PHE . 5785 2 24 . VAL . 5785 2 25 . GLY . 5785 2 26 . THR . 5785 2 27 . PRO . 5785 2 28 . GLU . 5785 2 29 . VAL . 5785 2 30 . ASN . 5785 2 31 . GLN . 5785 2 32 . THR . 5785 2 33 . THR . 5785 2 34 . LEU . 5785 2 35 . TYR . 5785 2 36 . GLN . 5785 2 37 . ARG . 5785 2 38 . TYR . 5785 2 39 . GLU . 5785 2 40 . ILE . 5785 2 41 . LYS . 5785 2 42 . MET . 5785 2 43 . THR . 5785 2 44 . LYS . 5785 2 45 . MET . 5785 2 46 . TYR . 5785 2 47 . LYS . 5785 2 48 . GLY . 5785 2 49 . PHE . 5785 2 50 . GLN . 5785 2 51 . ALA . 5785 2 52 . LEU . 5785 2 53 . GLY . 5785 2 54 . ASP . 5785 2 55 . ALA . 5785 2 56 . ALA . 5785 2 57 . ASP . 5785 2 58 . ILE . 5785 2 59 . ARG . 5785 2 60 . PHE . 5785 2 61 . VAL . 5785 2 62 . TYR . 5785 2 63 . THR . 5785 2 64 . PRO . 5785 2 65 . ALA . 5785 2 66 . MET . 5785 2 67 . GLU . 5785 2 68 . SER . 5785 2 69 . VAL . 5785 2 70 . CYS . 5785 2 71 . GLY . 5785 2 72 . TYR . 5785 2 73 . PHE . 5785 2 74 . HIS . 5785 2 75 . ARG . 5785 2 76 . SER . 5785 2 77 . HIS . 5785 2 78 . ASN . 5785 2 79 . ARG . 5785 2 80 . SER . 5785 2 81 . GLU . 5785 2 82 . GLU . 5785 2 83 . PHE . 5785 2 84 . LEU . 5785 2 85 . ILE . 5785 2 86 . ALA . 5785 2 87 . GLY . 5785 2 88 . LYS . 5785 2 89 . LEU . 5785 2 90 . GLN . 5785 2 91 . ASP . 5785 2 92 . GLY . 5785 2 93 . LEU . 5785 2 94 . LEU . 5785 2 95 . HIS . 5785 2 96 . ILE . 5785 2 97 . THR . 5785 2 98 . THR . 5785 2 99 . CYS . 5785 2 100 . SER . 5785 2 101 . PHE . 5785 2 102 . VAL . 5785 2 103 . ALA . 5785 2 104 . PRO . 5785 2 105 . TRP . 5785 2 106 . ASN . 5785 2 107 . SER . 5785 2 108 . LEU . 5785 2 109 . SER . 5785 2 110 . LEU . 5785 2 111 . ALA . 5785 2 112 . GLN . 5785 2 113 . ARG . 5785 2 114 . ARG . 5785 2 115 . GLY . 5785 2 116 . PHE . 5785 2 117 . THR . 5785 2 118 . LYS . 5785 2 119 . THR . 5785 2 120 . TYR . 5785 2 121 . THR . 5785 2 122 . VAL . 5785 2 123 . GLY . 5785 2 124 . CYS . 5785 2 125 . GLU . 5785 2 126 . GLU . 5785 2 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 5785 2 . THR 2 2 5785 2 . CYS 3 3 5785 2 . VAL 4 4 5785 2 . PRO 5 5 5785 2 . PRO 6 6 5785 2 . HIS 7 7 5785 2 . PRO 8 8 5785 2 . GLN 9 9 5785 2 . THR 10 10 5785 2 . ALA 11 11 5785 2 . PHE 12 12 5785 2 . CYS 13 13 5785 2 . ASN 14 14 5785 2 . SER 15 15 5785 2 . ASP 16 16 5785 2 . LEU 17 17 5785 2 . VAL 18 18 5785 2 . ILE 19 19 5785 2 . ARG 20 20 5785 2 . ALA 21 21 5785 2 . LYS 22 22 5785 2 . PHE 23 23 5785 2 . VAL 24 24 5785 2 . GLY 25 25 5785 2 . THR 26 26 5785 2 . PRO 27 27 5785 2 . GLU 28 28 5785 2 . VAL 29 29 5785 2 . ASN 30 30 5785 2 . GLN 31 31 5785 2 . THR 32 32 5785 2 . THR 33 33 5785 2 . LEU 34 34 5785 2 . TYR 35 35 5785 2 . GLN 36 36 5785 2 . ARG 37 37 5785 2 . TYR 38 38 5785 2 . GLU 39 39 5785 2 . ILE 40 40 5785 2 . LYS 41 41 5785 2 . MET 42 42 5785 2 . THR 43 43 5785 2 . LYS 44 44 5785 2 . MET 45 45 5785 2 . TYR 46 46 5785 2 . LYS 47 47 5785 2 . GLY 48 48 5785 2 . PHE 49 49 5785 2 . GLN 50 50 5785 2 . ALA 51 51 5785 2 . LEU 52 52 5785 2 . GLY 53 53 5785 2 . ASP 54 54 5785 2 . ALA 55 55 5785 2 . ALA 56 56 5785 2 . ASP 57 57 5785 2 . ILE 58 58 5785 2 . ARG 59 59 5785 2 . PHE 60 60 5785 2 . VAL 61 61 5785 2 . TYR 62 62 5785 2 . THR 63 63 5785 2 . PRO 64 64 5785 2 . ALA 65 65 5785 2 . MET 66 66 5785 2 . GLU 67 67 5785 2 . SER 68 68 5785 2 . VAL 69 69 5785 2 . CYS 70 70 5785 2 . GLY 71 71 5785 2 . TYR 72 72 5785 2 . PHE 73 73 5785 2 . HIS 74 74 5785 2 . ARG 75 75 5785 2 . SER 76 76 5785 2 . HIS 77 77 5785 2 . ASN 78 78 5785 2 . ARG 79 79 5785 2 . SER 80 80 5785 2 . GLU 81 81 5785 2 . GLU 82 82 5785 2 . PHE 83 83 5785 2 . LEU 84 84 5785 2 . ILE 85 85 5785 2 . ALA 86 86 5785 2 . GLY 87 87 5785 2 . LYS 88 88 5785 2 . LEU 89 89 5785 2 . GLN 90 90 5785 2 . ASP 91 91 5785 2 . GLY 92 92 5785 2 . LEU 93 93 5785 2 . LEU 94 94 5785 2 . HIS 95 95 5785 2 . ILE 96 96 5785 2 . THR 97 97 5785 2 . THR 98 98 5785 2 . CYS 99 99 5785 2 . SER 100 100 5785 2 . PHE 101 101 5785 2 . VAL 102 102 5785 2 . ALA 103 103 5785 2 . PRO 104 104 5785 2 . TRP 105 105 5785 2 . ASN 106 106 5785 2 . SER 107 107 5785 2 . LEU 108 108 5785 2 . SER 109 109 5785 2 . LEU 110 110 5785 2 . ALA 111 111 5785 2 . GLN 112 112 5785 2 . ARG 113 113 5785 2 . ARG 114 114 5785 2 . GLY 115 115 5785 2 . PHE 116 116 5785 2 . THR 117 117 5785 2 . LYS 118 118 5785 2 . THR 119 119 5785 2 . TYR 120 120 5785 2 . THR 121 121 5785 2 . VAL 122 122 5785 2 . GLY 123 123 5785 2 . CYS 124 124 5785 2 . GLU 125 125 5785 2 . GLU 126 126 5785 2 stop_ save_ save_CA _Entity.Sf_category entity _Entity.Sf_framecode CA _Entity.Entry_ID 5785 _Entity.ID 3 _Entity.BMRB_code . _Entity.Name CA _Entity.Type non-polymer _Entity.Polymer_common_type . _Entity.Polymer_type . _Entity.Polymer_type_details . _Entity.Polymer_strand_ID . _Entity.Polymer_seq_one_letter_code_can . _Entity.Polymer_seq_one_letter_code . _Entity.Target_identifier . _Entity.Polymer_author_defined_seq . _Entity.Polymer_author_seq_details . _Entity.Ambiguous_conformational_states no _Entity.Ambiguous_chem_comp_sites no _Entity.Nstd_monomer . _Entity.Nstd_chirality no _Entity.Nstd_linkage no _Entity.Nonpolymer_comp_ID CA _Entity.Nonpolymer_comp_label $chem_comp_CA _Entity.Number_of_monomers . _Entity.Number_of_nonpolymer_components . _Entity.Paramagnetic . _Entity.Thiol_state . _Entity.Src_method . _Entity.Parent_entity_ID 3 _Entity.Fragment . _Entity.Mutation . _Entity.EC_number . _Entity.Calc_isoelectric_point . _Entity.Formula_weight . _Entity.Formula_weight_exptl . _Entity.Formula_weight_exptl_meth . _Entity.Details . _Entity.DB_query_date . _Entity.DB_query_revised_last_date . 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 . CA . 5785 3 stop_ save_ save_ZN _Entity.Sf_category entity _Entity.Sf_framecode ZN _Entity.Entry_ID 5785 _Entity.ID 4 _Entity.BMRB_code . _Entity.Name ZN _Entity.Type non-polymer _Entity.Polymer_common_type . _Entity.Polymer_type . _Entity.Polymer_type_details . _Entity.Polymer_strand_ID . _Entity.Polymer_seq_one_letter_code_can . _Entity.Polymer_seq_one_letter_code . _Entity.Target_identifier . _Entity.Polymer_author_defined_seq . _Entity.Polymer_author_seq_details . _Entity.Ambiguous_conformational_states no _Entity.Ambiguous_chem_comp_sites no _Entity.Nstd_monomer . _Entity.Nstd_chirality no _Entity.Nstd_linkage no _Entity.Nonpolymer_comp_ID ZN _Entity.Nonpolymer_comp_label $chem_comp_ZN _Entity.Number_of_monomers . _Entity.Number_of_nonpolymer_components . _Entity.Paramagnetic . _Entity.Thiol_state . _Entity.Src_method . _Entity.Parent_entity_ID 4 _Entity.Fragment . _Entity.Mutation . _Entity.EC_number . _Entity.Calc_isoelectric_point . _Entity.Formula_weight . _Entity.Formula_weight_exptl . _Entity.Formula_weight_exptl_meth . _Entity.Details . _Entity.DB_query_date . _Entity.DB_query_revised_last_date . 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 . ZN . 5785 4 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 5785 _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 2 $N-TIMP-1 . 9606 organism . 'Homo sapiens' Human . . Eukaryota Metazoa Homo sapiens . . . . . . . . . . . . . . . . . . . . . 5785 1 2 1 $MMP-3(DC) . 9606 organism . 'Homo sapiens' Human . . Eukaryota Metazoa Homo sapiens . . . . . . . . . . . . . . . . . . . . . 5785 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 5785 _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 $MMP-3(DC) . 'recombinant technology' 'Escherichia coli' 'E. coli' . . Escherichia coli BL21(DE3) . . . . . . . . . . . . . . . pGEMEX-MMP-3(DC) . . . . . . 5785 1 2 2 $N-TIMP-1 . 'recombinant technology' 'Escherichia coli' 'E. coli' . . Escherichia coli . . . . . . . . . . . . . . . . pET3A-N-TIMP-1 . . . . . . 5785 1 stop_ save_ ################################# # Polymer residues and ligands # ################################# save_chem_comp_CA _Chem_comp.Sf_category chem_comp _Chem_comp.Sf_framecode chem_comp_CA _Chem_comp.Entry_ID 5785 _Chem_comp.ID CA _Chem_comp.Provenance . _Chem_comp.Name 'CALCIUM ION' _Chem_comp.Type non-polymer _Chem_comp.BMRB_code . _Chem_comp.PDB_code CA _Chem_comp.Ambiguous_flag no _Chem_comp.Initial_date 1999-07-08 _Chem_comp.Modified_date 2011-06-04 _Chem_comp.Release_status REL _Chem_comp.Replaced_by . _Chem_comp.Replaces . _Chem_comp.One_letter_code . _Chem_comp.Three_letter_code CA _Chem_comp.Number_atoms_all . _Chem_comp.Number_atoms_nh . _Chem_comp.PubChem_code . _Chem_comp.Subcomponent_list . _Chem_comp.InChI_code . _Chem_comp.Mon_nstd_flag . _Chem_comp.Mon_nstd_class . _Chem_comp.Mon_nstd_details . _Chem_comp.Mon_nstd_parent . _Chem_comp.Mon_nstd_parent_comp_ID . _Chem_comp.Std_deriv_one_letter_code . _Chem_comp.Std_deriv_three_letter_code . _Chem_comp.Std_deriv_BMRB_code . _Chem_comp.Std_deriv_PDB_code . _Chem_comp.Std_deriv_chem_comp_name . _Chem_comp.Synonyms . _Chem_comp.Formal_charge 2 _Chem_comp.Paramagnetic . _Chem_comp.Aromatic no _Chem_comp.Formula Ca _Chem_comp.Formula_weight 40.078 _Chem_comp.Formula_mono_iso_wt_nat . _Chem_comp.Formula_mono_iso_wt_13C . _Chem_comp.Formula_mono_iso_wt_15N . _Chem_comp.Formula_mono_iso_wt_13C_15N . _Chem_comp.Image_file_name . _Chem_comp.Image_file_format . _Chem_comp.Topo_file_name . _Chem_comp.Topo_file_format . _Chem_comp.Struct_file_name . _Chem_comp.Struct_file_format . _Chem_comp.Stereochem_param_file_name . _Chem_comp.Stereochem_param_file_format . _Chem_comp.Model_details . _Chem_comp.Model_erf . _Chem_comp.Model_source . _Chem_comp.Model_coordinates_details . _Chem_comp.Model_coordinates_missing_flag no _Chem_comp.Ideal_coordinates_details . _Chem_comp.Ideal_coordinates_missing_flag no _Chem_comp.Model_coordinates_db_code . _Chem_comp.Processing_site RCSB _Chem_comp.Vendor . _Chem_comp.Vendor_product_code . _Chem_comp.Details ; Information obtained from PDB's Chemical Component Dictionary at http://wwpdb-remediation.rutgers.edu/downloads.html Downloaded on Wed Jul 13 17:18:35 2011 ; _Chem_comp.DB_query_date . _Chem_comp.DB_last_query_revised_last_date . loop_ _Chem_comp_descriptor.Descriptor _Chem_comp_descriptor.Type _Chem_comp_descriptor.Program _Chem_comp_descriptor.Program_version _Chem_comp_descriptor.Entry_ID _Chem_comp_descriptor.Comp_ID [Ca+2] SMILES ACDLabs 10.04 5785 CA [Ca++] SMILES_CANONICAL CACTVS 3.341 5785 CA [Ca++] SMILES CACTVS 3.341 5785 CA [Ca+2] SMILES_CANONICAL 'OpenEye OEToolkits' 1.5.0 5785 CA [Ca+2] SMILES 'OpenEye OEToolkits' 1.5.0 5785 CA InChI=1S/Ca/q+2 InChI InChI 1.03 5785 CA BHPQYMZQTOCNFJ-UHFFFAOYSA-N InChIKey InChI 1.03 5785 CA stop_ loop_ _Chem_comp_identifier.Identifier _Chem_comp_identifier.Type _Chem_comp_identifier.Program _Chem_comp_identifier.Program_version _Chem_comp_identifier.Entry_ID _Chem_comp_identifier.Comp_ID calcium 'SYSTEMATIC NAME' ACDLabs 10.04 5785 CA 'calcium(+2) cation' 'SYSTEMATIC NAME' 'OpenEye OEToolkits' 1.5.0 5785 CA stop_ loop_ _Chem_comp_atom.Atom_ID _Chem_comp_atom.BMRB_code _Chem_comp_atom.PDB_atom_ID _Chem_comp_atom.Alt_atom_ID _Chem_comp_atom.Auth_atom_ID _Chem_comp_atom.Type_symbol _Chem_comp_atom.Isotope_number _Chem_comp_atom.Chirality _Chem_comp_atom.Stereo_config _Chem_comp_atom.Charge _Chem_comp_atom.Partial_charge _Chem_comp_atom.Oxidation_number _Chem_comp_atom.Unpaired_electron_number _Chem_comp_atom.Align _Chem_comp_atom.Aromatic_flag _Chem_comp_atom.Leaving_atom_flag _Chem_comp_atom.Substruct_code _Chem_comp_atom.Ionizable _Chem_comp_atom.Drawing_2D_coord_x _Chem_comp_atom.Drawing_2D_coord_y _Chem_comp_atom.Model_Cartn_x _Chem_comp_atom.Model_Cartn_x_esd _Chem_comp_atom.Model_Cartn_y _Chem_comp_atom.Model_Cartn_y_esd _Chem_comp_atom.Model_Cartn_z _Chem_comp_atom.Model_Cartn_z_esd _Chem_comp_atom.Model_Cartn_x_ideal _Chem_comp_atom.Model_Cartn_y_ideal _Chem_comp_atom.Model_Cartn_z_ideal _Chem_comp_atom.PDBX_ordinal _Chem_comp_atom.Details _Chem_comp_atom.Entry_ID _Chem_comp_atom.Comp_ID CA . CA . . CA . . N 2 . . . . no no . . . . 0.000 . 0.000 . 0.000 . 0.000 0.000 0.000 1 . 5785 CA stop_ save_ save_chem_comp_ZN _Chem_comp.Sf_category chem_comp _Chem_comp.Sf_framecode chem_comp_ZN _Chem_comp.Entry_ID 5785 _Chem_comp.ID ZN _Chem_comp.Provenance . _Chem_comp.Name 'ZINC ION' _Chem_comp.Type non-polymer _Chem_comp.BMRB_code . _Chem_comp.PDB_code ZN _Chem_comp.Ambiguous_flag no _Chem_comp.Initial_date 1999-07-08 _Chem_comp.Modified_date 2011-06-04 _Chem_comp.Release_status REL _Chem_comp.Replaced_by . _Chem_comp.Replaces . _Chem_comp.One_letter_code . _Chem_comp.Three_letter_code ZN _Chem_comp.Number_atoms_all . _Chem_comp.Number_atoms_nh . _Chem_comp.PubChem_code . _Chem_comp.Subcomponent_list . _Chem_comp.InChI_code . _Chem_comp.Mon_nstd_flag . _Chem_comp.Mon_nstd_class . _Chem_comp.Mon_nstd_details . _Chem_comp.Mon_nstd_parent . _Chem_comp.Mon_nstd_parent_comp_ID . _Chem_comp.Std_deriv_one_letter_code . _Chem_comp.Std_deriv_three_letter_code . _Chem_comp.Std_deriv_BMRB_code . _Chem_comp.Std_deriv_PDB_code . _Chem_comp.Std_deriv_chem_comp_name . _Chem_comp.Synonyms . _Chem_comp.Formal_charge 2 _Chem_comp.Paramagnetic . _Chem_comp.Aromatic no _Chem_comp.Formula Zn _Chem_comp.Formula_weight 65.409 _Chem_comp.Formula_mono_iso_wt_nat . _Chem_comp.Formula_mono_iso_wt_13C . _Chem_comp.Formula_mono_iso_wt_15N . _Chem_comp.Formula_mono_iso_wt_13C_15N . _Chem_comp.Image_file_name . _Chem_comp.Image_file_format . _Chem_comp.Topo_file_name . _Chem_comp.Topo_file_format . _Chem_comp.Struct_file_name . _Chem_comp.Struct_file_format . _Chem_comp.Stereochem_param_file_name . _Chem_comp.Stereochem_param_file_format . _Chem_comp.Model_details . _Chem_comp.Model_erf . _Chem_comp.Model_source . _Chem_comp.Model_coordinates_details . _Chem_comp.Model_coordinates_missing_flag no _Chem_comp.Ideal_coordinates_details . _Chem_comp.Ideal_coordinates_missing_flag no _Chem_comp.Model_coordinates_db_code . _Chem_comp.Processing_site RCSB _Chem_comp.Vendor . _Chem_comp.Vendor_product_code . _Chem_comp.Details ; Information obtained from PDB's Chemical Component Dictionary at http://wwpdb-remediation.rutgers.edu/downloads.html Downloaded on Mon Jul 25 12:26:23 2011 ; _Chem_comp.DB_query_date . _Chem_comp.DB_last_query_revised_last_date . loop_ _Chem_comp_descriptor.Descriptor _Chem_comp_descriptor.Type _Chem_comp_descriptor.Program _Chem_comp_descriptor.Program_version _Chem_comp_descriptor.Entry_ID _Chem_comp_descriptor.Comp_ID [Zn+2] SMILES ACDLabs 10.04 5785 ZN [Zn++] SMILES_CANONICAL CACTVS 3.341 5785 ZN [Zn++] SMILES CACTVS 3.341 5785 ZN [Zn+2] SMILES_CANONICAL 'OpenEye OEToolkits' 1.5.0 5785 ZN [Zn+2] SMILES 'OpenEye OEToolkits' 1.5.0 5785 ZN InChI=1S/Zn/q+2 InChI InChI 1.03 5785 ZN PTFCDOFLOPIGGS-UHFFFAOYSA-N InChIKey InChI 1.03 5785 ZN stop_ loop_ _Chem_comp_identifier.Identifier _Chem_comp_identifier.Type _Chem_comp_identifier.Program _Chem_comp_identifier.Program_version _Chem_comp_identifier.Entry_ID _Chem_comp_identifier.Comp_ID zinc 'SYSTEMATIC NAME' ACDLabs 10.04 5785 ZN 'zinc(+2) cation' 'SYSTEMATIC NAME' 'OpenEye OEToolkits' 1.5.0 5785 ZN stop_ loop_ _Chem_comp_atom.Atom_ID _Chem_comp_atom.BMRB_code _Chem_comp_atom.PDB_atom_ID _Chem_comp_atom.Alt_atom_ID _Chem_comp_atom.Auth_atom_ID _Chem_comp_atom.Type_symbol _Chem_comp_atom.Isotope_number _Chem_comp_atom.Chirality _Chem_comp_atom.Stereo_config _Chem_comp_atom.Charge _Chem_comp_atom.Partial_charge _Chem_comp_atom.Oxidation_number _Chem_comp_atom.Unpaired_electron_number _Chem_comp_atom.Align _Chem_comp_atom.Aromatic_flag _Chem_comp_atom.Leaving_atom_flag _Chem_comp_atom.Substruct_code _Chem_comp_atom.Ionizable _Chem_comp_atom.Drawing_2D_coord_x _Chem_comp_atom.Drawing_2D_coord_y _Chem_comp_atom.Model_Cartn_x _Chem_comp_atom.Model_Cartn_x_esd _Chem_comp_atom.Model_Cartn_y _Chem_comp_atom.Model_Cartn_y_esd _Chem_comp_atom.Model_Cartn_z _Chem_comp_atom.Model_Cartn_z_esd _Chem_comp_atom.Model_Cartn_x_ideal _Chem_comp_atom.Model_Cartn_y_ideal _Chem_comp_atom.Model_Cartn_z_ideal _Chem_comp_atom.PDBX_ordinal _Chem_comp_atom.Details _Chem_comp_atom.Entry_ID _Chem_comp_atom.Comp_ID ZN . ZN . . ZN . . N 2 . . . . no no . . . . 0.000 . 0.000 . 0.000 . 0.000 0.000 0.000 1 . 5785 ZN stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Sample.Sf_category sample _Sample.Sf_framecode sample_1 _Sample.Entry_ID 5785 _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 'Matrix MetalloProteinases-3 or stromelysin 1' '[U-98% 15N]' . . 1 $MMP-3(DC) . . 0.8 . . mM . . . . 5785 1 2 'N-terminal domain of Tissue Inhibitor of MatrixmetalloProteinases-1' . . . 2 $N-TIMP-1 . . 0.8 . . mM . . . . 5785 1 stop_ save_ save_sample_2 _Sample.Sf_category sample _Sample.Sf_framecode sample_2 _Sample.Entry_ID 5785 _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 'Matrix MetalloProteinases-3 or stromelysin 1' '[U-98% 13C; U-98% 15N]' . . 1 $MMP-3(DC) . . 0.8 . . mM . . . . 5785 2 2 'N-terminal domain of Tissue Inhibitor of MatrixmetalloProteinases-1' . . . 2 $N-TIMP-1 . . 0.8 . . mM . . . . 5785 2 stop_ save_ save_sample_3 _Sample.Sf_category sample _Sample.Sf_framecode sample_3 _Sample.Entry_ID 5785 _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 'Matrix MetalloProteinases-3 or stromelysin 1' '[U-96% 2H]' . . 1 $MMP-3(DC) . . 0.6 . . mM . . . . 5785 3 2 'N-terminal domain of Tissue Inhibitor of MatrixmetalloProteinases-1' . . . 2 $N-TIMP-1 . . 0.6 . . mM . . . . 5785 3 stop_ save_ ####################### # Sample conditions # ####################### save_EXP-COND_1 _Sample_condition_list.Sf_category sample_conditions _Sample_condition_list.Sf_framecode EXP-COND_1 _Sample_condition_list.Entry_ID 5785 _Sample_condition_list.ID 1 _Sample_condition_list.Details . loop_ _Sample_condition_variable.Type _Sample_condition_variable.Val _Sample_condition_variable.Val_err _Sample_condition_variable.Val_units _Sample_condition_variable.Entry_ID _Sample_condition_variable.Sample_condition_list_ID pH 6.6 0.1 n/a 5785 1 temperature 310 1 K 5785 1 'ionic strength' 0.145 0.05 M 5785 1 stop_ save_ ############################ # Computer software used # ############################ save_SYBYL_TRIAD _Software.Sf_category software _Software.Sf_framecode SYBYL_TRIAD _Software.Entry_ID 5785 _Software.ID 1 _Software.Name 'SYBYL TRIAD' _Software.Version '6.2, 6.3, 6.6' _Software.Details . loop_ _Task.Task _Task.Entry_ID _Task.Software_ID 'data process' 5785 1 'data analysis' 5785 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 5785 _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 5785 _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 . . . 5785 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 5785 _Experiment_list.ID 1 _Experiment_list.Details ; 8 MM Nalorac probe was used for most of the experiments except the [u-2H]MMP-3/N-TIMP-1 complex where a 5 mm probe was used. ; 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 . . . . . . . . . . . . . . . . . 1 $EXP-COND_1 . . . 1 $spectrometer_1 . . . . . . . . . . . . . . . . 5785 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 5785 _Chem_shift_reference.ID 1 _Chem_shift_reference.Details . loop_ _Chem_shift_ref.Atom_type _Chem_shift_ref.Atom_isotope_number _Chem_shift_ref.Mol_common_name _Chem_shift_ref.Atom_group _Chem_shift_ref.Concentration_val _Chem_shift_ref.Concentration_units _Chem_shift_ref.Solvent _Chem_shift_ref.Rank _Chem_shift_ref.Chem_shift_units _Chem_shift_ref.Chem_shift_val _Chem_shift_ref.Ref_method _Chem_shift_ref.Ref_type _Chem_shift_ref.Indirect_shift_ratio _Chem_shift_ref.External_ref_loc _Chem_shift_ref.External_ref_sample_geometry _Chem_shift_ref.External_ref_axis _Chem_shift_ref.Indirect_shift_ratio_cit_ID _Chem_shift_ref.Indirect_shift_ratio_cit_label _Chem_shift_ref.Ref_correction_type _Chem_shift_ref.Correction_val _Chem_shift_ref.Correction_val_cit_ID _Chem_shift_ref.Correction_val_cit_label _Chem_shift_ref.Entry_ID _Chem_shift_ref.Chem_shift_reference_ID H 1 DSS 'methyl protons' . . . . ppm 0.0 internal direct 1.000000000 . . . . . . . . . 5785 1 N 15 DSS 'methyl protons' . . . . ppm 0.0 . indirect 0.101329118 . . . . . . . . . 5785 1 C 13 DSS 'methyl protons' . . . . ppm 0.0 . indirect 0.251449530 . . . . . . . . . 5785 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_MMP-3_CPX_SHIFTS _Assigned_chem_shift_list.Sf_category assigned_chemical_shifts _Assigned_chem_shift_list.Sf_framecode MMP-3_CPX_SHIFTS _Assigned_chem_shift_list.Entry_ID 5785 _Assigned_chem_shift_list.ID 1 _Assigned_chem_shift_list.Sample_condition_list_ID 1 _Assigned_chem_shift_list.Sample_condition_list_label $EXP-COND_1 _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 $sample_1 . 5785 1 . . 2 $sample_2 . 5785 1 . . 3 $sample_3 . 5785 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 2 2 ARG HG2 H 1 1.67 0.02 . 2 . . . . 84 . . . 5785 1 2 . 1 1 2 2 ARG HD2 H 1 3.26 0.02 . 2 . . . . 84 . . . 5785 1 3 . 1 1 2 2 ARG CG C 13 28.24 0.12 . 9 . . . . 84 . . . 5785 1 4 . 1 1 2 2 ARG CD C 13 43.36 0.12 . 1 . . . . 84 . . . 5785 1 5 . 1 1 3 3 THR HB H 1 4.89 0.02 . 1 . . . . 85 . . . 5785 1 6 . 1 1 3 3 THR HG21 H 1 1.19 0.02 . 1 . . . . 85 . . . 5785 1 7 . 1 1 3 3 THR HG22 H 1 1.19 0.02 . 1 . . . . 85 . . . 5785 1 8 . 1 1 3 3 THR HG23 H 1 1.19 0.02 . 1 . . . . 85 . . . 5785 1 9 . 1 1 3 3 THR CB C 13 69.94 0.12 . 1 . . . . 85 . . . 5785 1 10 . 1 1 3 3 THR CG2 C 13 21.47 0.12 . 1 . . . . 85 . . . 5785 1 11 . 1 1 7 7 ILE HG12 H 1 1.32 0.02 . 2 . . . . 89 . . . 5785 1 12 . 1 1 7 7 ILE HG13 H 1 1.06 0.02 . 2 . . . . 89 . . . 5785 1 13 . 1 1 7 7 ILE HD11 H 1 0.74 0.02 . 1 . . . . 89 . . . 5785 1 14 . 1 1 7 7 ILE HD12 H 1 0.74 0.02 . 1 . . . . 89 . . . 5785 1 15 . 1 1 7 7 ILE HD13 H 1 0.74 0.02 . 1 . . . . 89 . . . 5785 1 16 . 1 1 7 7 ILE CG1 C 13 26.88 0.12 . 2 . . . . 89 . . . 5785 1 17 . 1 1 7 7 ILE CD1 C 13 12.76 0.12 . 1 . . . . 89 . . . 5785 1 18 . 1 1 8 8 PRO CA C 13 63.81 0.12 . 1 . . . . 90 . . . 5785 1 19 . 1 1 9 9 LYS H H 1 6.90 0.02 . 1 . . . . 91 . . . 5785 1 20 . 1 1 9 9 LYS HA H 1 4.39 0.02 . 1 . . . . 91 . . . 5785 1 21 . 1 1 9 9 LYS HG2 H 1 0.99 0.02 . 2 . . . . 91 . . . 5785 1 22 . 1 1 9 9 LYS HD2 H 1 1.39 0.02 . 2 . . . . 91 . . . 5785 1 23 . 1 1 9 9 LYS HD3 H 1 1.29 0.02 . 2 . . . . 91 . . . 5785 1 24 . 1 1 9 9 LYS HE2 H 1 2.79 0.02 . 2 . . . . 91 . . . 5785 1 25 . 1 1 9 9 LYS C C 13 175.24 0.12 . 1 . . . . 91 . . . 5785 1 26 . 1 1 9 9 LYS CA C 13 54.23 0.12 . 1 . . . . 91 . . . 5785 1 27 . 1 1 9 9 LYS CG C 13 22.65 0.12 . 1 . . . . 91 . . . 5785 1 28 . 1 1 9 9 LYS CD C 13 29.94 0.12 . 1 . . . . 91 . . . 5785 1 29 . 1 1 9 9 LYS CE C 13 41.94 0.12 . 1 . . . . 91 . . . 5785 1 30 . 1 1 9 9 LYS N N 15 110.59 0.1 . 1 . . . . 91 . . . 5785 1 31 . 1 1 10 10 TRP H H 1 8.07 0.02 . 1 . . . . 92 . . . 5785 1 32 . 1 1 10 10 TRP HA H 1 4.49 0.02 . 1 . . . . 92 . . . 5785 1 33 . 1 1 10 10 TRP C C 13 176.5 0.12 . 1 . . . . 92 . . . 5785 1 34 . 1 1 10 10 TRP CA C 13 57.95 0.12 . 1 . . . . 92 . . . 5785 1 35 . 1 1 10 10 TRP N N 15 122.44 0.1 . 1 . . . . 92 . . . 5785 1 36 . 1 1 11 11 ARG H H 1 8.10 0.02 . 1 . . . . 93 . . . 5785 1 37 . 1 1 11 11 ARG HA H 1 4.46 0.02 . 1 . . . . 93 . . . 5785 1 38 . 1 1 11 11 ARG HB2 H 1 2.07 0.02 . 2 . . . . 93 . . . 5785 1 39 . 1 1 11 11 ARG HB3 H 1 1.77 0.02 . 2 . . . . 93 . . . 5785 1 40 . 1 1 11 11 ARG HG2 H 1 1.71 0.02 . 2 . . . . 93 . . . 5785 1 41 . 1 1 11 11 ARG HG3 H 1 1.58 0.02 . 2 . . . . 93 . . . 5785 1 42 . 1 1 11 11 ARG HD2 H 1 3.11 0.02 . 2 . . . . 93 . . . 5785 1 43 . 1 1 11 11 ARG C C 13 174.94 0.12 . 1 . . . . 93 . . . 5785 1 44 . 1 1 11 11 ARG CA C 13 55.74 0.12 . 1 . . . . 93 . . . 5785 1 45 . 1 1 11 11 ARG CB C 13 28.58 0.12 . 1 . . . . 93 . . . 5785 1 46 . 1 1 11 11 ARG CG C 13 27.35 0.12 . 1 . . . . 93 . . . 5785 1 47 . 1 1 11 11 ARG CD C 13 42.88 0.12 . 1 . . . . 93 . . . 5785 1 48 . 1 1 11 11 ARG N N 15 119.53 0.1 . 1 . . . . 93 . . . 5785 1 49 . 1 1 12 12 LYS H H 1 7.45 0.02 . 1 . . . . 94 . . . 5785 1 50 . 1 1 12 12 LYS HA H 1 4.63 0.02 . 1 . . . . 94 . . . 5785 1 51 . 1 1 12 12 LYS HB2 H 1 1.84 0.02 . 2 . . . . 94 . . . 5785 1 52 . 1 1 12 12 LYS HG2 H 1 1.05 0.02 . 2 . . . . 94 . . . 5785 1 53 . 1 1 12 12 LYS HG3 H 1 1.28 0.02 . 2 . . . . 94 . . . 5785 1 54 . 1 1 12 12 LYS HD2 H 1 1.60 0.02 . 2 . . . . 94 . . . 5785 1 55 . 1 1 12 12 LYS HE2 H 1 2.83 0.02 . 2 . . . . 94 . . . 5785 1 56 . 1 1 12 12 LYS C C 13 174.42 0.12 . 1 . . . . 94 . . . 5785 1 57 . 1 1 12 12 LYS CA C 13 54.19 0.02 . 1 . . . . 94 . . . 5785 1 58 . 1 1 12 12 LYS CB C 13 33.94 0.12 . 1 . . . . 94 . . . 5785 1 59 . 1 1 12 12 LYS CG C 13 22.88 0.12 . 1 . . . . 94 . . . 5785 1 60 . 1 1 12 12 LYS CE C 13 41.94 0.02 . 1 . . . . 94 . . . 5785 1 61 . 1 1 12 12 LYS N N 15 117.09 0.1 . 1 . . . . 94 . . . 5785 1 62 . 1 1 13 13 THR H H 1 7.95 0.02 . 1 . . . . 95 . . . 5785 1 63 . 1 1 13 13 THR HA H 1 4.19 0.02 . 1 . . . . 95 . . . 5785 1 64 . 1 1 13 13 THR C C 13 172.64 0.12 . 1 . . . . 95 . . . 5785 1 65 . 1 1 13 13 THR CA C 13 60.76 0.12 . 1 . . . . 95 . . . 5785 1 66 . 1 1 13 13 THR N N 15 105.46 0.1 . 1 . . . . 95 . . . 5785 1 67 . 1 1 14 14 HIS H H 1 6.91 0.02 . 1 . . . . 96 . . . 5785 1 68 . 1 1 14 14 HIS HA H 1 4.94 0.02 . 1 . . . . 96 . . . 5785 1 69 . 1 1 14 14 HIS HB2 H 1 2.89 0.02 . 1 . . . . 96 . . . 5785 1 70 . 1 1 14 14 HIS HB3 H 1 2.66 0.02 . 1 . . . . 96 . . . 5785 1 71 . 1 1 14 14 HIS C C 13 174.00 0.12 . 1 . . . . 96 . . . 5785 1 72 . 1 1 14 14 HIS CA C 13 53.93 0.12 . 1 . . . . 96 . . . 5785 1 73 . 1 1 14 14 HIS CB C 13 29.71 0.12 . 1 . . . . 96 . . . 5785 1 74 . 1 1 14 14 HIS N N 15 120.63 0.1 . 1 . . . . 96 . . . 5785 1 75 . 1 1 15 15 LEU H H 1 8.11 0.02 . 1 . . . . 97 . . . 5785 1 76 . 1 1 15 15 LEU HA H 1 4.39 0.02 . 1 . . . . 97 . . . 5785 1 77 . 1 1 15 15 LEU HB2 H 1 1.19 0.02 . 2 . . . . 97 . . . 5785 1 78 . 1 1 15 15 LEU HB3 H 1 0.77 0.02 . 2 . . . . 97 . . . 5785 1 79 . 1 1 15 15 LEU HG H 1 0.66 0.02 . 1 . . . . 97 . . . 5785 1 80 . 1 1 15 15 LEU HD11 H 1 -0.40 0.02 . 1 . . . . 97 . . . 5785 1 81 . 1 1 15 15 LEU HD12 H 1 -0.40 0.02 . 1 . . . . 97 . . . 5785 1 82 . 1 1 15 15 LEU HD13 H 1 -0.40 0.02 . 1 . . . . 97 . . . 5785 1 83 . 1 1 15 15 LEU HD21 H 1 -0.20 0.02 . 1 . . . . 97 . . . 5785 1 84 . 1 1 15 15 LEU HD22 H 1 -0.20 0.02 . 1 . . . . 97 . . . 5785 1 85 . 1 1 15 15 LEU HD23 H 1 -0.20 0.02 . 1 . . . . 97 . . . 5785 1 86 . 1 1 15 15 LEU C C 13 176.42 0.12 . 1 . . . . 97 . . . 5785 1 87 . 1 1 15 15 LEU CA C 13 52.57 0.12 . 1 . . . . 97 . . . 5785 1 88 . 1 1 15 15 LEU CG C 13 26.88 0.12 . 1 . . . . 97 . . . 5785 1 89 . 1 1 15 15 LEU CD1 C 13 22.65 0.12 . 1 . . . . 97 . . . 5785 1 90 . 1 1 15 15 LEU CD2 C 13 24.76 0.12 . 1 . . . . 97 . . . 5785 1 91 . 1 1 15 15 LEU N N 15 128.38 0.1 . 1 . . . . 97 . . . 5785 1 92 . 1 1 16 16 THR H H 1 9.10 0.02 . 1 . . . . 98 . . . 5785 1 93 . 1 1 16 16 THR HA H 1 5.63 0.02 . 1 . . . . 98 . . . 5785 1 94 . 1 1 16 16 THR HB H 1 3.96 0.02 . 1 . . . . 98 . . . 5785 1 95 . 1 1 16 16 THR HG21 H 1 1.02 0.02 . 1 . . . . 98 . . . 5785 1 96 . 1 1 16 16 THR HG22 H 1 1.02 0.02 . 1 . . . . 98 . . . 5785 1 97 . 1 1 16 16 THR HG23 H 1 1.02 0.02 . 1 . . . . 98 . . . 5785 1 98 . 1 1 16 16 THR C C 13 174.62 0.12 . 1 . . . . 98 . . . 5785 1 99 . 1 1 16 16 THR CA C 13 57.96 0.12 . 1 . . . . 98 . . . 5785 1 100 . 1 1 16 16 THR CB C 13 72.66 0.12 . 1 . . . . 98 . . . 5785 1 101 . 1 1 16 16 THR CG2 C 13 21.39 0.12 . 1 . . . . 98 . . . 5785 1 102 . 1 1 16 16 THR N N 15 110.83 0.1 . 1 . . . . 98 . . . 5785 1 103 . 1 1 17 17 TYR H H 1 8.53 0.02 . 1 . . . . 99 . . . 5785 1 104 . 1 1 17 17 TYR HA H 1 5.53 0.02 . 1 . . . . 99 . . . 5785 1 105 . 1 1 17 17 TYR HB2 H 1 2.65 0.02 . 9 . . . . 99 . . . 5785 1 106 . 1 1 17 17 TYR C C 13 171.89 0.12 . 1 . . . . 99 . . . 5785 1 107 . 1 1 17 17 TYR CA C 13 54.56 0.12 . 1 . . . . 99 . . . 5785 1 108 . 1 1 17 17 TYR N N 15 118.00 0.1 . 1 . . . . 99 . . . 5785 1 109 . 1 1 18 18 ARG H H 1 8.12 0.02 . 1 . . . . 100 . . . 5785 1 110 . 1 1 18 18 ARG HA H 1 4.19 0.02 . 1 . . . . 100 . . . 5785 1 111 . 1 1 18 18 ARG HB2 H 1 1.80 0.02 . 2 . . . . 100 . . . 5785 1 112 . 1 1 18 18 ARG HB3 H 1 1.95 0.02 . 9 . . . . 100 . . . 5785 1 113 . 1 1 18 18 ARG HG2 H 1 1.24 0.02 . 2 . . . . 100 . . . 5785 1 114 . 1 1 18 18 ARG C C 13 173.99 0.12 . 1 . . . . 100 . . . 5785 1 115 . 1 1 18 18 ARG CA C 13 54.87 0.12 . 1 . . . . 100 . . . 5785 1 116 . 1 1 18 18 ARG CB C 13 34.41 0.12 . 1 . . . . 100 . . . 5785 1 117 . 1 1 18 18 ARG N N 15 119.95 0.1 . 1 . . . . 100 . . . 5785 1 118 . 1 1 19 19 ILE H H 1 8.22 0.02 . 1 . . . . 101 . . . 5785 1 119 . 1 1 19 19 ILE HA H 1 4.24 0.02 . 1 . . . . 101 . . . 5785 1 120 . 1 1 19 19 ILE HB H 1 1.53 0.02 . 1 . . . . 101 . . . 5785 1 121 . 1 1 19 19 ILE HG12 H 1 0.67 0.02 . 2 . . . . 101 . . . 5785 1 122 . 1 1 19 19 ILE HG21 H 1 0.19 0.02 . 1 . . . . 101 . . . 5785 1 123 . 1 1 19 19 ILE HG22 H 1 0.19 0.02 . 1 . . . . 101 . . . 5785 1 124 . 1 1 19 19 ILE HG23 H 1 0.19 0.02 . 1 . . . . 101 . . . 5785 1 125 . 1 1 19 19 ILE HD11 H 1 0.86 0.02 . 1 . . . . 101 . . . 5785 1 126 . 1 1 19 19 ILE HD12 H 1 0.86 0.02 . 1 . . . . 101 . . . 5785 1 127 . 1 1 19 19 ILE HD13 H 1 0.86 0.02 . 1 . . . . 101 . . . 5785 1 128 . 1 1 19 19 ILE C C 13 175.56 0.12 . 1 . . . . 101 . . . 5785 1 129 . 1 1 19 19 ILE CA C 13 61.31 0.12 . 1 . . . . 101 . . . 5785 1 130 . 1 1 19 19 ILE CB C 13 36.76 0.12 . 1 . . . . 101 . . . 5785 1 131 . 1 1 19 19 ILE CG1 C 13 28.01 0.12 . 1 . . . . 101 . . . 5785 1 132 . 1 1 19 19 ILE CG2 C 13 17.00 0.12 . 1 . . . . 101 . . . 5785 1 133 . 1 1 19 19 ILE CD1 C 13 13.23 0.12 . 1 . . . . 101 . . . 5785 1 134 . 1 1 19 19 ILE N N 15 128.55 0.1 . 1 . . . . 101 . . . 5785 1 135 . 1 1 20 20 VAL H H 1 9.38 0.02 . 1 . . . . 102 . . . 5785 1 136 . 1 1 20 20 VAL HA H 1 3.30 0.02 . 1 . . . . 102 . . . 5785 1 137 . 1 1 20 20 VAL HB H 1 1.96 0.02 . 1 . . . . 102 . . . 5785 1 138 . 1 1 20 20 VAL HG11 H 1 0.91 0.02 . 1 . . . . 102 . . . 5785 1 139 . 1 1 20 20 VAL HG12 H 1 0.91 0.02 . 1 . . . . 102 . . . 5785 1 140 . 1 1 20 20 VAL HG13 H 1 0.91 0.02 . 1 . . . . 102 . . . 5785 1 141 . 1 1 20 20 VAL HG21 H 1 0.85 0.02 . 1 . . . . 102 . . . 5785 1 142 . 1 1 20 20 VAL HG22 H 1 0.85 0.02 . 1 . . . . 102 . . . 5785 1 143 . 1 1 20 20 VAL HG23 H 1 0.85 0.02 . 1 . . . . 102 . . . 5785 1 144 . 1 1 20 20 VAL C C 13 175.37 0.12 . 1 . . . . 102 . . . 5785 1 145 . 1 1 20 20 VAL CA C 13 65.76 0.12 . 1 . . . . 102 . . . 5785 1 146 . 1 1 20 20 VAL CB C 13 32.26 0.12 . 1 . . . . 102 . . . 5785 1 147 . 1 1 20 20 VAL CG1 C 13 23.05 0.12 . 1 . . . . 102 . . . 5785 1 148 . 1 1 20 20 VAL CG2 C 13 20.68 0.12 . 1 . . . . 102 . . . 5785 1 149 . 1 1 20 20 VAL N N 15 130.04 0.1 . 1 . . . . 102 . . . 5785 1 150 . 1 1 21 21 ASN H H 1 7.56 0.02 . 1 . . . . 103 . . . 5785 1 151 . 1 1 21 21 ASN HA H 1 4.59 0.02 . 1 . . . . 103 . . . 5785 1 152 . 1 1 21 21 ASN C C 13 170.11 0.12 . 1 . . . . 103 . . . 5785 1 153 . 1 1 21 21 ASN CA C 13 51.23 0.12 . 1 . . . . 103 . . . 5785 1 154 . 1 1 21 21 ASN N N 15 116.5 0.1 . 1 . . . . 103 . . . 5785 1 155 . 1 1 22 22 TYR H H 1 8.03 0.02 . 1 . . . . 104 . . . 5785 1 156 . 1 1 22 22 TYR CA C 13 58.64 0.12 . 1 . . . . 104 . . . 5785 1 157 . 1 1 22 22 TYR N N 15 112.78 0.1 . 1 . . . . 104 . . . 5785 1 158 . 1 1 23 23 THR H H 1 7.95 0.02 . 1 . . . . 105 . . . 5785 1 159 . 1 1 23 23 THR HB H 1 3.06 0.02 . 1 . . . . 105 . . . 5785 1 160 . 1 1 23 23 THR HG21 H 1 0.28 0.02 . 1 . . . . 105 . . . 5785 1 161 . 1 1 23 23 THR HG22 H 1 0.28 0.02 . 1 . . . . 105 . . . 5785 1 162 . 1 1 23 23 THR HG23 H 1 0.28 0.02 . 1 . . . . 105 . . . 5785 1 163 . 1 1 23 23 THR CB C 13 67.12 0.12 . 1 . . . . 105 . . . 5785 1 164 . 1 1 23 23 THR CG2 C 13 18.65 0.12 . 1 . . . . 105 . . . 5785 1 165 . 1 1 23 23 THR N N 15 117.95 0.1 . 1 . . . . 105 . . . 5785 1 166 . 1 1 24 24 PRO HA H 1 4.49 0.02 . 1 . . . . 106 . . . 5785 1 167 . 1 1 24 24 PRO C C 13 177.51 0.12 . 1 . . . . 106 . . . 5785 1 168 . 1 1 25 25 ASP H H 1 8.83 0.02 . 1 . . . . 107 . . . 5785 1 169 . 1 1 25 25 ASP HA H 1 3.98 0.02 . 1 . . . . 107 . . . 5785 1 170 . 1 1 25 25 ASP HB2 H 1 2.61 0.02 . 2 . . . . 107 . . . 5785 1 171 . 1 1 25 25 ASP HB3 H 1 3.15 0.02 . 2 . . . . 107 . . . 5785 1 172 . 1 1 25 25 ASP C C 13 175.56 0.12 . 1 . . . . 107 . . . 5785 1 173 . 1 1 25 25 ASP CA C 13 55.78 0.12 . 1 . . . . 107 . . . 5785 1 174 . 1 1 25 25 ASP CB C 13 41.24 0.12 . 1 . . . . 107 . . . 5785 1 175 . 1 1 25 25 ASP N N 15 122.15 0.1 . 1 . . . . 107 . . . 5785 1 176 . 1 1 26 26 LEU H H 1 6.92 0.02 . 1 . . . . 108 . . . 5785 1 177 . 1 1 26 26 LEU HA H 1 4.76 0.02 . 1 . . . . 108 . . . 5785 1 178 . 1 1 26 26 LEU HB2 H 1 1.32 0.02 . 2 . . . . 108 . . . 5785 1 179 . 1 1 26 26 LEU HB3 H 1 1.07 0.02 . 2 . . . . 108 . . . 5785 1 180 . 1 1 26 26 LEU HG H 1 1.42 0.02 . 1 . . . . 108 . . . 5785 1 181 . 1 1 26 26 LEU HD11 H 1 0.86 0.02 . 2 . . . . 108 . . . 5785 1 182 . 1 1 26 26 LEU HD12 H 1 0.86 0.02 . 2 . . . . 108 . . . 5785 1 183 . 1 1 26 26 LEU HD13 H 1 0.86 0.02 . 2 . . . . 108 . . . 5785 1 184 . 1 1 26 26 LEU HD21 H 1 0.44 0.02 . 2 . . . . 108 . . . 5785 1 185 . 1 1 26 26 LEU HD22 H 1 0.44 0.02 . 2 . . . . 108 . . . 5785 1 186 . 1 1 26 26 LEU HD23 H 1 0.44 0.02 . 2 . . . . 108 . . . 5785 1 187 . 1 1 26 26 LEU C C 13 173.12 0.12 . 1 . . . . 108 . . . 5785 1 188 . 1 1 26 26 LEU CA C 13 51.05 0.12 . 1 . . . . 108 . . . 5785 1 189 . 1 1 26 26 LEU CB C 13 47.12 0.12 . 1 . . . . 108 . . . 5785 1 190 . 1 1 26 26 LEU CG C 13 26.12 0.12 . 1 . . . . 108 . . . 5785 1 191 . 1 1 26 26 LEU CD1 C 13 24.46 0.12 . 2 . . . . 108 . . . 5785 1 192 . 1 1 26 26 LEU CD2 C 13 25.88 0.12 . 2 . . . . 108 . . . 5785 1 193 . 1 1 26 26 LEU N N 15 116.84 0.1 . 1 . . . . 108 . . . 5785 1 194 . 1 1 27 27 PRO HA H 1 4.38 0.02 . 1 . . . . 109 . . . 5785 1 195 . 1 1 27 27 PRO HB2 H 1 2.33 0.02 . 2 . . . . 109 . . . 5785 1 196 . 1 1 27 27 PRO HB3 H 1 1.92 0.02 . 2 . . . . 109 . . . 5785 1 197 . 1 1 27 27 PRO C C 13 177.82 0.12 . 1 . . . . 109 . . . 5785 1 198 . 1 1 27 27 PRO CB C 13 32.06 0.12 . 1 . . . . 109 . . . 5785 1 199 . 1 1 28 28 LYS H H 1 8.54 0.02 . 1 . . . . 110 . . . 5785 1 200 . 1 1 28 28 LYS HA H 1 3.60 0.02 . 1 . . . . 110 . . . 5785 1 201 . 1 1 28 28 LYS HB2 H 1 1.35 0.02 . 2 . . . . 110 . . . 5785 1 202 . 1 1 28 28 LYS HB3 H 1 1.24 0.02 . 2 . . . . 110 . . . 5785 1 203 . 1 1 28 28 LYS HG2 H 1 0.94 0.02 . 2 . . . . 110 . . . 5785 1 204 . 1 1 28 28 LYS HG3 H 1 0.52 0.02 . 2 . . . . 110 . . . 5785 1 205 . 1 1 28 28 LYS HD2 H 1 1.16 0.02 . 2 . . . . 110 . . . 5785 1 206 . 1 1 28 28 LYS HD3 H 1 1.06 0.02 . 2 . . . . 110 . . . 5785 1 207 . 1 1 28 28 LYS HE2 H 1 2.60 0.02 . 2 . . . . 110 . . . 5785 1 208 . 1 1 28 28 LYS HE3 H 1 2.54 0.02 . 2 . . . . 110 . . . 5785 1 209 . 1 1 28 28 LYS C C 13 178.3 0.12 . 1 . . . . 110 . . . 5785 1 210 . 1 1 28 28 LYS CA C 13 60.43 0.12 . 1 . . . . 110 . . . 5785 1 211 . 1 1 28 28 LYS CB C 13 32.06 0.12 . 1 . . . . 110 . . . 5785 1 212 . 1 1 28 28 LYS CG C 13 24.06 0.12 . 1 . . . . 110 . . . 5785 1 213 . 1 1 28 28 LYS CD C 13 28.94 0.12 . 1 . . . . 110 . . . 5785 1 214 . 1 1 28 28 LYS CE C 13 41.7 0.12 . 1 . . . . 110 . . . 5785 1 215 . 1 1 28 28 LYS N N 15 124.31 0.1 . 1 . . . . 110 . . . 5785 1 216 . 1 1 29 29 ASP H H 1 8.42 0.02 . 1 . . . . 111 . . . 5785 1 217 . 1 1 29 29 ASP HA H 1 4.22 0.02 . 1 . . . . 111 . . . 5785 1 218 . 1 1 29 29 ASP HB2 H 1 2.59 0.02 . 2 . . . . 111 . . . 5785 1 219 . 1 1 29 29 ASP HB3 H 1 2.53 0.02 . 2 . . . . 111 . . . 5785 1 220 . 1 1 29 29 ASP C C 13 178.55 0.12 . 1 . . . . 111 . . . 5785 1 221 . 1 1 29 29 ASP CA C 13 56.52 0.12 . 1 . . . . 111 . . . 5785 1 222 . 1 1 29 29 ASP CB C 13 39.58 0.12 . 1 . . . . 111 . . . 5785 1 223 . 1 1 29 29 ASP N N 15 114.04 0.1 . 1 . . . . 111 . . . 5785 1 224 . 1 1 30 30 ALA H H 1 7.24 0.02 . 1 . . . . 112 . . . 5785 1 225 . 1 1 30 30 ALA HA H 1 4.19 0.02 . 1 . . . . 112 . . . 5785 1 226 . 1 1 30 30 ALA HB1 H 1 1.46 0.02 . 1 . . . . 112 . . . 5785 1 227 . 1 1 30 30 ALA HB2 H 1 1.46 0.02 . 1 . . . . 112 . . . 5785 1 228 . 1 1 30 30 ALA HB3 H 1 1.46 0.02 . 1 . . . . 112 . . . 5785 1 229 . 1 1 30 30 ALA C C 13 180.55 0.12 . 1 . . . . 112 . . . 5785 1 230 . 1 1 30 30 ALA CA C 13 54.01 0.12 . 1 . . . . 112 . . . 5785 1 231 . 1 1 30 30 ALA CB C 13 18.65 0.12 . 1 . . . . 112 . . . 5785 1 232 . 1 1 30 30 ALA N N 15 122.79 0.1 . 1 . . . . 112 . . . 5785 1 233 . 1 1 31 31 VAL H H 1 7.46 0.02 . 1 . . . . 113 . . . 5785 1 234 . 1 1 31 31 VAL HA H 1 3.43 0.02 . 1 . . . . 113 . . . 5785 1 235 . 1 1 31 31 VAL HB H 1 2.46 0.02 . 1 . . . . 113 . . . 5785 1 236 . 1 1 31 31 VAL HG11 H 1 0.80 0.02 . 1 . . . . 113 . . . 5785 1 237 . 1 1 31 31 VAL HG12 H 1 0.80 0.02 . 1 . . . . 113 . . . 5785 1 238 . 1 1 31 31 VAL HG13 H 1 0.80 0.02 . 1 . . . . 113 . . . 5785 1 239 . 1 1 31 31 VAL HG21 H 1 0.83 0.02 . 1 . . . . 113 . . . 5785 1 240 . 1 1 31 31 VAL HG22 H 1 0.83 0.02 . 1 . . . . 113 . . . 5785 1 241 . 1 1 31 31 VAL HG23 H 1 0.83 0.02 . 1 . . . . 113 . . . 5785 1 242 . 1 1 31 31 VAL C C 13 177.07 0.12 . 1 . . . . 113 . . . 5785 1 243 . 1 1 31 31 VAL CA C 13 66.28 0.12 . 1 . . . . 113 . . . 5785 1 244 . 1 1 31 31 VAL CB C 13 31.31 0.12 . 1 . . . . 113 . . . 5785 1 245 . 1 1 31 31 VAL CG2 C 13 20.92 0.12 . 1 . . . . 113 . . . 5785 1 246 . 1 1 31 31 VAL N N 15 122.13 0.1 . 1 . . . . 113 . . . 5785 1 247 . 1 1 32 32 ASP H H 1 8.46 0.02 . 1 . . . . 114 . . . 5785 1 248 . 1 1 32 32 ASP HA H 1 4.06 0.02 . 1 . . . . 114 . . . 5785 1 249 . 1 1 32 32 ASP HB2 H 1 2.71 0.02 . 2 . . . . 114 . . . 5785 1 250 . 1 1 32 32 ASP HB3 H 1 2.56 0.02 . 2 . . . . 114 . . . 5785 1 251 . 1 1 32 32 ASP C C 13 178.79 0.12 . 1 . . . . 114 . . . 5785 1 252 . 1 1 32 32 ASP CA C 13 57.86 0.12 . 1 . . . . 114 . . . 5785 1 253 . 1 1 32 32 ASP CB C 13 39.58 0.12 . 1 . . . . 114 . . . 5785 1 254 . 1 1 32 32 ASP N N 15 119.77 0.1 . 1 . . . . 114 . . . 5785 1 255 . 1 1 33 33 SER H H 1 7.95 0.02 . 1 . . . . 115 . . . 5785 1 256 . 1 1 33 33 SER HA H 1 4.12 0.02 . 1 . . . . 115 . . . 5785 1 257 . 1 1 33 33 SER HB2 H 1 3.82 0.02 . 2 . . . . 115 . . . 5785 1 258 . 1 1 33 33 SER HB3 H 1 3.89 0.02 . 2 . . . . 115 . . . 5785 1 259 . 1 1 33 33 SER C C 13 176.58 0.12 . 1 . . . . 115 . . . 5785 1 260 . 1 1 33 33 SER CA C 13 61.3 0.12 . 1 . . . . 115 . . . 5785 1 261 . 1 1 33 33 SER CB C 13 62.97 0.12 . 1 . . . . 115 . . . 5785 1 262 . 1 1 33 33 SER N N 15 112.88 0.1 . 1 . . . . 115 . . . 5785 1 263 . 1 1 34 34 ALA H H 1 7.63 0.02 . 1 . . . . 116 . . . 5785 1 264 . 1 1 34 34 ALA HA H 1 4.08 0.02 . 1 . . . . 116 . . . 5785 1 265 . 1 1 34 34 ALA HB1 H 1 1.36 0.02 . 1 . . . . 116 . . . 5785 1 266 . 1 1 34 34 ALA HB2 H 1 1.36 0.02 . 1 . . . . 116 . . . 5785 1 267 . 1 1 34 34 ALA HB3 H 1 1.36 0.02 . 1 . . . . 116 . . . 5785 1 268 . 1 1 34 34 ALA C C 13 179.36 0.12 . 1 . . . . 116 . . . 5785 1 269 . 1 1 34 34 ALA CA C 13 55.5 0.12 . 1 . . . . 116 . . . 5785 1 270 . 1 1 34 34 ALA CB C 13 17.94 0.12 . 1 . . . . 116 . . . 5785 1 271 . 1 1 34 34 ALA N N 15 124.7 0.1 . 1 . . . . 116 . . . 5785 1 272 . 1 1 35 35 VAL H H 1 7.93 0.02 . 1 . . . . 117 . . . 5785 1 273 . 1 1 35 35 VAL HA H 1 3.12 0.02 . 1 . . . . 117 . . . 5785 1 274 . 1 1 35 35 VAL HB H 1 1.93 0.02 . 1 . . . . 117 . . . 5785 1 275 . 1 1 35 35 VAL HG11 H 1 0.64 0.02 . 1 . . . . 117 . . . 5785 1 276 . 1 1 35 35 VAL HG12 H 1 0.64 0.02 . 1 . . . . 117 . . . 5785 1 277 . 1 1 35 35 VAL HG13 H 1 0.64 0.02 . 1 . . . . 117 . . . 5785 1 278 . 1 1 35 35 VAL HG21 H 1 0.42 0.02 . 1 . . . . 117 . . . 5785 1 279 . 1 1 35 35 VAL HG22 H 1 0.42 0.02 . 1 . . . . 117 . . . 5785 1 280 . 1 1 35 35 VAL HG23 H 1 0.42 0.02 . 1 . . . . 117 . . . 5785 1 281 . 1 1 35 35 VAL C C 13 177.07 0.12 . 1 . . . . 117 . . . 5785 1 282 . 1 1 35 35 VAL CA C 13 66.8 0.12 . 1 . . . . 117 . . . 5785 1 283 . 1 1 35 35 VAL CB C 13 31.08 0.12 . 1 . . . . 117 . . . 5785 1 284 . 1 1 35 35 VAL CG1 C 13 21.95 0.12 . 1 . . . . 117 . . . 5785 1 285 . 1 1 35 35 VAL CG2 C 13 21.39 0.12 . 1 . . . . 117 . . . 5785 1 286 . 1 1 35 35 VAL N N 15 116.29 0.12 . 1 . . . . 117 . . . 5785 1 287 . 1 1 36 36 GLU H H 1 8.27 0.0 . 1 . . . . 118 . . . 5785 1 288 . 1 1 36 36 GLU HA H 1 3.56 0.02 . 1 . . . . 118 . . . 5785 1 289 . 1 1 36 36 GLU HB2 H 1 2.07 0.02 . 2 . . . . 118 . . . 5785 1 290 . 1 1 36 36 GLU HB3 H 1 1.94 0.02 . 2 . . . . 118 . . . 5785 1 291 . 1 1 36 36 GLU HG2 H 1 2.36 0.02 . 2 . . . . 118 . . . 5785 1 292 . 1 1 36 36 GLU HG3 H 1 2.08 0.02 . 2 . . . . 118 . . . 5785 1 293 . 1 1 36 36 GLU C C 13 179.47 0.12 . 1 . . . . 118 . . . 5785 1 294 . 1 1 36 36 GLU CA C 13 60.08 0.12 . 1 . . . . 118 . . . 5785 1 295 . 1 1 36 36 GLU CB C 13 28.95 0.12 . 1 . . . . 118 . . . 5785 1 296 . 1 1 36 36 GLU CG C 13 36.75 0.12 . 1 . . . . 118 . . . 5785 1 297 . 1 1 36 36 GLU N N 15 118.45 0.1 . 1 . . . . 118 . . . 5785 1 298 . 1 1 37 37 LYS H H 1 8.17 0.02 . 1 . . . . 119 . . . 5785 1 299 . 1 1 37 37 LYS HA H 1 3.79 0.02 . 1 . . . . 119 . . . 5785 1 300 . 1 1 37 37 LYS HB2 H 1 1.62 0.02 . 2 . . . . 119 . . . 5785 1 301 . 1 1 37 37 LYS HB3 H 1 1.76 0.02 . 2 . . . . 119 . . . 5785 1 302 . 1 1 37 37 LYS HG2 H 1 1.40 0.02 . 2 . . . . 119 . . . 5785 1 303 . 1 1 37 37 LYS HG3 H 1 1.11 0.02 . 2 . . . . 119 . . . 5785 1 304 . 1 1 37 37 LYS HD2 H 1 1.22 0.02 . 2 . . . . 119 . . . 5785 1 305 . 1 1 37 37 LYS HD3 H 1 0.96 0.02 . 2 . . . . 119 . . . 5785 1 306 . 1 1 37 37 LYS HE2 H 1 2.38 0.02 . 2 . . . . 119 . . . 5785 1 307 . 1 1 37 37 LYS C C 13 178.87 0.12 . 1 . . . . 119 . . . 5785 1 308 . 1 1 37 37 LYS CA C 13 59.65 0.12 . 1 . . . . 119 . . . 5785 1 309 . 1 1 37 37 LYS CB C 13 32.06 0.12 . 1 . . . . 119 . . . 5785 1 310 . 1 1 37 37 LYS CG C 13 25.47 0.12 . 1 . . . . 119 . . . 5785 1 311 . 1 1 37 37 LYS CD C 13 28.76 0.12 . 1 . . . . 119 . . . 5785 1 312 . 1 1 37 37 LYS CE C 13 41.47 0.12 . 1 . . . . 119 . . . 5785 1 313 . 1 1 37 37 LYS N N 15 119.5 0.1 . 1 . . . . 119 . . . 5785 1 314 . 1 1 38 38 ALA H H 1 7.95 0.02 . 1 . . . . 120 . . . 5785 1 315 . 1 1 38 38 ALA HA H 1 3.87 0.02 . 1 . . . . 120 . . . 5785 1 316 . 1 1 38 38 ALA HB1 H 1 1.26 0.02 . 1 . . . . 120 . . . 5785 1 317 . 1 1 38 38 ALA HB2 H 1 1.26 0.02 . 1 . . . . 120 . . . 5785 1 318 . 1 1 38 38 ALA HB3 H 1 1.26 0.02 . 1 . . . . 120 . . . 5785 1 319 . 1 1 38 38 ALA C C 13 178.22 0.12 . 1 . . . . 120 . . . 5785 1 320 . 1 1 38 38 ALA CA C 13 55.48 0.12 . 1 . . . . 120 . . . 5785 1 321 . 1 1 38 38 ALA CB C 13 18.18 0.12 . 1 . . . . 120 . . . 5785 1 322 . 1 1 38 38 ALA N N 15 123.73 0.1 . 1 . . . . 120 . . . 5785 1 323 . 1 1 39 39 LEU H H 1 7.55 0.02 . 1 . . . . 121 . . . 5785 1 324 . 1 1 39 39 LEU HA H 1 3.53 0.02 . 1 . . . . 121 . . . 5785 1 325 . 1 1 39 39 LEU HB2 H 1 1.32 0.02 . 2 . . . . 121 . . . 5785 1 326 . 1 1 39 39 LEU HG H 1 1.05 0.02 . 1 . . . . 121 . . . 5785 1 327 . 1 1 39 39 LEU HD11 H 1 -0.58 0.02 . 1 . . . . 121 . . . 5785 1 328 . 1 1 39 39 LEU HD12 H 1 -0.58 0.02 . 1 . . . . 121 . . . 5785 1 329 . 1 1 39 39 LEU HD13 H 1 -0.58 0.02 . 1 . . . . 121 . . . 5785 1 330 . 1 1 39 39 LEU HD21 H 1 -0.68 0.02 . 1 . . . . 121 . . . 5785 1 331 . 1 1 39 39 LEU HD22 H 1 -0.68 0.02 . 1 . . . . 121 . . . 5785 1 332 . 1 1 39 39 LEU HD23 H 1 -0.68 0.02 . 1 . . . . 121 . . . 5785 1 333 . 1 1 39 39 LEU C C 13 179.78 0.12 . 1 . . . . 121 . . . 5785 1 334 . 1 1 39 39 LEU CA C 13 57.44 0.12 . 1 . . . . 121 . . . 5785 1 335 . 1 1 39 39 LEU CB C 13 40.53 0.12 . 1 . . . . 121 . . . 5785 1 336 . 1 1 39 39 LEU CG C 13 24.95 0.12 . 1 . . . . 121 . . . 5785 1 337 . 1 1 39 39 LEU CD1 C 13 21.26 0.12 . 1 . . . . 121 . . . 5785 1 338 . 1 1 39 39 LEU CD2 C 13 24.7 0.12 . 1 . . . . 121 . . . 5785 1 339 . 1 1 39 39 LEU N N 15 115.42 0.1 . 1 . . . . 121 . . . 5785 1 340 . 1 1 40 40 LYS H H 1 7.79 0.02 . 1 . . . . 122 . . . 5785 1 341 . 1 1 40 40 LYS HA H 1 3.99 0.02 . 1 . . . . 122 . . . 5785 1 342 . 1 1 40 40 LYS HB2 H 1 1.87 0.02 . 2 . . . . 122 . . . 5785 1 343 . 1 1 40 40 LYS HB3 H 1 1.95 0.02 . 2 . . . . 122 . . . 5785 1 344 . 1 1 40 40 LYS HG2 H 1 1.48 0.02 . 2 . . . . 122 . . . 5785 1 345 . 1 1 40 40 LYS HD2 H 1 1.58 0.02 . 2 . . . . 122 . . . 5785 1 346 . 1 1 40 40 LYS HE2 H 1 2.89 0.02 . 2 . . . . 122 . . . 5785 1 347 . 1 1 40 40 LYS C C 13 178.54 0.12 . 1 . . . . 122 . . . 5785 1 348 . 1 1 40 40 LYS CA C 13 58.42 0.12 . 1 . . . . 122 . . . 5785 1 349 . 1 1 40 40 LYS CB C 13 31.82 0.12 . 1 . . . . 122 . . . 5785 1 350 . 1 1 40 40 LYS CG C 13 24.76 0.12 . 1 . . . . 122 . . . 5785 1 351 . 1 1 40 40 LYS CD C 13 28.53 0.12 . 1 . . . . 122 . . . 5785 1 352 . 1 1 40 40 LYS CE C 13 41.92 0.12 . 1 . . . . 122 . . . 5785 1 353 . 1 1 40 40 LYS N N 15 119.26 0.1 . 1 . . . . 122 . . . 5785 1 354 . 1 1 41 41 VAL H H 1 7.35 0.02 . 1 . . . . 123 . . . 5785 1 355 . 1 1 41 41 VAL HA H 1 3.58 0.02 . 1 . . . . 123 . . . 5785 1 356 . 1 1 41 41 VAL HB H 1 1.87 0.02 . 1 . . . . 123 . . . 5785 1 357 . 1 1 41 41 VAL HG11 H 1 0.76 0.02 . 1 . . . . 123 . . . 5785 1 358 . 1 1 41 41 VAL HG12 H 1 0.76 0.02 . 1 . . . . 123 . . . 5785 1 359 . 1 1 41 41 VAL HG13 H 1 0.76 0.02 . 1 . . . . 123 . . . 5785 1 360 . 1 1 41 41 VAL HG21 H 1 0.36 0.02 . 1 . . . . 123 . . . 5785 1 361 . 1 1 41 41 VAL HG22 H 1 0.36 0.02 . 1 . . . . 123 . . . 5785 1 362 . 1 1 41 41 VAL HG23 H 1 0.36 0.02 . 1 . . . . 123 . . . 5785 1 363 . 1 1 41 41 VAL C C 13 177.06 0.12 . 1 . . . . 123 . . . 5785 1 364 . 1 1 41 41 VAL CA C 13 65.23 0.12 . 1 . . . . 123 . . . 5785 1 365 . 1 1 41 41 VAL CB C 13 30.88 0.12 . 1 . . . . 123 . . . 5785 1 366 . 1 1 41 41 VAL CG1 C 13 21.38 0.12 . 1 . . . . 123 . . . 5785 1 367 . 1 1 41 41 VAL CG2 C 13 21.16 0.12 . 1 . . . . 123 . . . 5785 1 368 . 1 1 41 41 VAL N N 15 115.97 0.1 . 1 . . . . 123 . . . 5785 1 369 . 1 1 42 42 TRP H H 1 6.49 0.02 . 1 . . . . 124 . . . 5785 1 370 . 1 1 42 42 TRP HA H 1 4.54 0.02 . 1 . . . . 124 . . . 5785 1 371 . 1 1 42 42 TRP C C 13 179.93 0.12 . 1 . . . . 124 . . . 5785 1 372 . 1 1 42 42 TRP CA C 13 57.27 0.12 . 1 . . . . 124 . . . 5785 1 373 . 1 1 42 42 TRP N N 15 117.48 0.1 . 1 . . . . 124 . . . 5785 1 374 . 1 1 43 43 GLU H H 1 8.57 0.02 . 1 . . . . 125 . . . 5785 1 375 . 1 1 43 43 GLU HA H 1 3.79 0.02 . 1 . . . . 125 . . . 5785 1 376 . 1 1 43 43 GLU HB2 H 1 2.22 0.02 . 2 . . . . 125 . . . 5785 1 377 . 1 1 43 43 GLU HB3 H 1 2.15 0.02 . 2 . . . . 125 . . . 5785 1 378 . 1 1 43 43 GLU HG2 H 1 2.69 0.02 . 2 . . . . 125 . . . 5785 1 379 . 1 1 43 43 GLU HG3 H 1 2.31 0.02 . 2 . . . . 125 . . . 5785 1 380 . 1 1 43 43 GLU C C 13 178.59 0.12 . 1 . . . . 125 . . . 5785 1 381 . 1 1 43 43 GLU CA C 13 59.45 0.12 . 1 . . . . 125 . . . 5785 1 382 . 1 1 43 43 GLU CB C 13 30.84 0.12 . 1 . . . . 125 . . . 5785 1 383 . 1 1 43 43 GLU CG C 13 36.51 0.12 . 1 . . . . 125 . . . 5785 1 384 . 1 1 43 43 GLU N N 15 123.07 0.1 . 1 . . . . 125 . . . 5785 1 385 . 1 1 44 44 GLU H H 1 7.80 0.02 . 1 . . . . 126 . . . 5785 1 386 . 1 1 44 44 GLU HA H 1 4.04 0.02 . 1 . . . . 126 . . . 5785 1 387 . 1 1 44 44 GLU HB2 H 1 2.09 0.02 . 2 . . . . 126 . . . 5785 1 388 . 1 1 44 44 GLU HB3 H 1 1.95 0.02 . 2 . . . . 126 . . . 5785 1 389 . 1 1 44 44 GLU HG2 H 1 2.49 0.02 . 2 . . . . 126 . . . 5785 1 390 . 1 1 44 44 GLU HG3 H 1 2.28 0.02 . 2 . . . . 126 . . . 5785 1 391 . 1 1 44 44 GLU C C 13 178.00 0.12 . 1 . . . . 126 . . . 5785 1 392 . 1 1 44 44 GLU CA C 13 58.49 0.12 . 1 . . . . 126 . . . 5785 1 393 . 1 1 44 44 GLU CB C 13 30.37 0.12 . 1 . . . . 126 . . . 5785 1 394 . 1 1 44 44 GLU CG C 13 36.52 0.12 . 1 . . . . 126 . . . 5785 1 395 . 1 1 44 44 GLU N N 15 112.22 0.1 . 1 . . . . 126 . . . 5785 1 396 . 1 1 45 45 VAL H H 1 6.98 0.02 . 1 . . . . 127 . . . 5785 1 397 . 1 1 45 45 VAL HA H 1 4.59 0.02 . 1 . . . . 127 . . . 5785 1 398 . 1 1 45 45 VAL HB H 1 2.58 0.02 . 1 . . . . 127 . . . 5785 1 399 . 1 1 45 45 VAL HG11 H 1 1.11 0.02 . 1 . . . . 127 . . . 5785 1 400 . 1 1 45 45 VAL HG12 H 1 1.11 0.02 . 1 . . . . 127 . . . 5785 1 401 . 1 1 45 45 VAL HG13 H 1 1.11 0.02 . 1 . . . . 127 . . . 5785 1 402 . 1 1 45 45 VAL HG21 H 1 0.85 0.02 . 1 . . . . 127 . . . 5785 1 403 . 1 1 45 45 VAL HG22 H 1 0.85 0.02 . 1 . . . . 127 . . . 5785 1 404 . 1 1 45 45 VAL HG23 H 1 0.85 0.02 . 1 . . . . 127 . . . 5785 1 405 . 1 1 45 45 VAL C C 13 174.53 0.12 . 1 . . . . 127 . . . 5785 1 406 . 1 1 45 45 VAL CA C 13 60.11 0.12 . 1 . . . . 127 . . . 5785 1 407 . 1 1 45 45 VAL CB C 13 32.26 0.12 . 1 . . . . 127 . . . 5785 1 408 . 1 1 45 45 VAL CG1 C 13 18.56 0.12 . 1 . . . . 127 . . . 5785 1 409 . 1 1 45 45 VAL CG2 C 13 21.16 0.12 . 1 . . . . 127 . . . 5785 1 410 . 1 1 45 45 VAL N N 15 105.36 0.1 . 1 . . . . 127 . . . 5785 1 411 . 1 1 46 46 THR H H 1 7.52 0.02 . 1 . . . . 128 . . . 5785 1 412 . 1 1 46 46 THR HA H 1 5.32 0.02 . 1 . . . . 128 . . . 5785 1 413 . 1 1 46 46 THR HB H 1 4.08 0.02 . 1 . . . . 128 . . . 5785 1 414 . 1 1 46 46 THR HG21 H 1 1.41 0.02 . 1 . . . . 128 . . . 5785 1 415 . 1 1 46 46 THR HG22 H 1 1.41 0.02 . 1 . . . . 128 . . . 5785 1 416 . 1 1 46 46 THR HG23 H 1 1.41 0.02 . 1 . . . . 128 . . . 5785 1 417 . 1 1 46 46 THR C C 13 172.84 0.12 . 1 . . . . 128 . . . 5785 1 418 . 1 1 46 46 THR CA C 13 60.08 0.12 . 1 . . . . 128 . . . 5785 1 419 . 1 1 46 46 THR CB C 13 71.35 0.12 . 1 . . . . 128 . . . 5785 1 420 . 1 1 46 46 THR CG2 C 13 24.29 0.12 . 1 . . . . 128 . . . 5785 1 421 . 1 1 46 46 THR N N 15 111.33 0.1 . 1 . . . . 128 . . . 5785 1 422 . 1 1 47 47 PRO HA H 1 4.80 0.02 . 1 . . . . 129 . . . 5785 1 423 . 1 1 47 47 PRO HB2 H 1 2.06 0.02 . 2 . . . . 129 . . . 5785 1 424 . 1 1 47 47 PRO HB3 H 1 1.97 0.02 . 2 . . . . 129 . . . 5785 1 425 . 1 1 47 47 PRO HG2 H 1 1.74 0.02 . 9 . . . . 129 . . . 5785 1 426 . 1 1 47 47 PRO C C 13 176.63 0.12 . 1 . . . . 129 . . . 5785 1 427 . 1 1 47 47 PRO CB C 13 31.35 0.12 . 1 . . . . 129 . . . 5785 1 428 . 1 1 48 48 LEU H H 1 7.27 0.02 . 1 . . . . 130 . . . 5785 1 429 . 1 1 48 48 LEU HA H 1 4.30 0.02 . 1 . . . . 130 . . . 5785 1 430 . 1 1 48 48 LEU HB2 H 1 1.25 0.02 . 2 . . . . 130 . . . 5785 1 431 . 1 1 48 48 LEU HG H 1 1.00 0.02 . 1 . . . . 130 . . . 5785 1 432 . 1 1 48 48 LEU HD11 H 1 0.14 0.02 . 1 . . . . 130 . . . 5785 1 433 . 1 1 48 48 LEU HD12 H 1 0.14 0.02 . 1 . . . . 130 . . . 5785 1 434 . 1 1 48 48 LEU HD13 H 1 0.14 0.02 . 1 . . . . 130 . . . 5785 1 435 . 1 1 48 48 LEU HD21 H 1 0.21 0.02 . 1 . . . . 130 . . . 5785 1 436 . 1 1 48 48 LEU HD22 H 1 0.21 0.02 . 1 . . . . 130 . . . 5785 1 437 . 1 1 48 48 LEU HD23 H 1 0.21 0.02 . 1 . . . . 130 . . . 5785 1 438 . 1 1 48 48 LEU C C 13 176.84 0.12 . 1 . . . . 130 . . . 5785 1 439 . 1 1 48 48 LEU CA C 13 54.99 0.12 . 1 . . . . 130 . . . 5785 1 440 . 1 1 48 48 LEU CG C 13 27.06 0.12 . 1 . . . . 130 . . . 5785 1 441 . 1 1 48 48 LEU CD1 C 13 21.39 0.12 . 1 . . . . 130 . . . 5785 1 442 . 1 1 48 48 LEU CD2 C 13 25.88 0.12 . 1 . . . . 130 . . . 5785 1 443 . 1 1 48 48 LEU N N 15 118.08 0.1 . 1 . . . . 130 . . . 5785 1 444 . 1 1 49 49 THR H H 1 8.03 0.02 . 1 . . . . 131 . . . 5785 1 445 . 1 1 49 49 THR HA H 1 4.41 0.02 . 1 . . . . 131 . . . 5785 1 446 . 1 1 49 49 THR HB H 1 3.90 0.02 . 1 . . . . 131 . . . 5785 1 447 . 1 1 49 49 THR HG21 H 1 1.08 0.02 . 1 . . . . 131 . . . 5785 1 448 . 1 1 49 49 THR HG22 H 1 1.08 0.02 . 1 . . . . 131 . . . 5785 1 449 . 1 1 49 49 THR HG23 H 1 1.08 0.02 . 1 . . . . 131 . . . 5785 1 450 . 1 1 49 49 THR C C 13 172.45 0.12 . 1 . . . . 131 . . . 5785 1 451 . 1 1 49 49 THR CA C 13 59.77 0.12 . 1 . . . . 131 . . . 5785 1 452 . 1 1 49 49 THR CB C 13 70.18 0.12 . 1 . . . . 131 . . . 5785 1 453 . 1 1 49 49 THR CG2 C 13 21.00 0.12 . 1 . . . . 131 . . . 5785 1 454 . 1 1 49 49 THR N N 15 110.88 0.1 . 1 . . . . 131 . . . 5785 1 455 . 1 1 50 50 PHE H H 1 8.16 0.02 . 1 . . . . 132 . . . 5785 1 456 . 1 1 50 50 PHE HA H 1 5.57 0.02 . 1 . . . . 132 . . . 5785 1 457 . 1 1 50 50 PHE HB2 H 1 2.70 0.02 . 3 . . . . 132 . . . 5785 1 458 . 1 1 50 50 PHE C C 13 176.99 0.12 . 1 . . . . 132 . . . 5785 1 459 . 1 1 50 50 PHE CA C 13 55.94 0.12 . 1 . . . . 132 . . . 5785 1 460 . 1 1 50 50 PHE CB C 13 42.89 0.12 . 1 . . . . 132 . . . 5785 1 461 . 1 1 50 50 PHE N N 15 117.69 0.1 . 1 . . . . 132 . . . 5785 1 462 . 1 1 51 51 SER H H 1 8.62 0.02 . 1 . . . . 133 . . . 5785 1 463 . 1 1 51 51 SER HA H 1 4.78 0.02 . 1 . . . . 133 . . . 5785 1 464 . 1 1 51 51 SER HB2 H 1 3.77 0.02 . 2 . . . . 133 . . . 5785 1 465 . 1 1 51 51 SER HB3 H 1 3.60 0.02 . 2 . . . . 133 . . . 5785 1 466 . 1 1 51 51 SER C C 13 171.55 0.12 . 1 . . . . 133 . . . 5785 1 467 . 1 1 51 51 SER CA C 13 57.44 0.12 . 1 . . . . 133 . . . 5785 1 468 . 1 1 51 51 SER CB C 13 65.33 0.02 . 1 . . . . 133 . . . 5785 1 469 . 1 1 51 51 SER N N 15 116.98 0.1 . 1 . . . . 133 . . . 5785 1 470 . 1 1 52 52 ARG H H 1 8.39 0.02 . 1 . . . . 134 . . . 5785 1 471 . 1 1 52 52 ARG HA H 1 3.40 0.02 . 1 . . . . 134 . . . 5785 1 472 . 1 1 52 52 ARG HB2 H 1 1.38 0.02 . 2 . . . . 134 . . . 5785 1 473 . 1 1 52 52 ARG HB3 H 1 1.09 0.02 . 2 . . . . 134 . . . 5785 1 474 . 1 1 52 52 ARG C C 13 175.75 0.12 . 1 . . . . 134 . . . 5785 1 475 . 1 1 52 52 ARG CA C 13 55.35 0.12 . 1 . . . . 134 . . . 5785 1 476 . 1 1 52 52 ARG N N 15 125.52 0.1 . 1 . . . . 134 . . . 5785 1 477 . 1 1 53 53 LEU H H 1 8.50 0.02 . 1 . . . . 135 . . . 5785 1 478 . 1 1 53 53 LEU HA H 1 4.55 0.02 . 1 . . . . 135 . . . 5785 1 479 . 1 1 53 53 LEU HB2 H 1 1.52 0.02 . 2 . . . . 135 . . . 5785 1 480 . 1 1 53 53 LEU HB3 H 1 1.65 0.02 . 9 . . . . 135 . . . 5785 1 481 . 1 1 53 53 LEU HG H 1 1.40 0.02 . 1 . . . . 135 . . . 5785 1 482 . 1 1 53 53 LEU HD11 H 1 0.78 0.02 . 1 . . . . 135 . . . 5785 1 483 . 1 1 53 53 LEU HD12 H 1 0.78 0.02 . 1 . . . . 135 . . . 5785 1 484 . 1 1 53 53 LEU HD13 H 1 0.78 0.02 . 1 . . . . 135 . . . 5785 1 485 . 1 1 53 53 LEU HD21 H 1 0.69 0.02 . 1 . . . . 135 . . . 5785 1 486 . 1 1 53 53 LEU HD22 H 1 0.69 0.02 . 1 . . . . 135 . . . 5785 1 487 . 1 1 53 53 LEU HD23 H 1 0.69 0.02 . 1 . . . . 135 . . . 5785 1 488 . 1 1 53 53 LEU C C 13 177.04 0.12 . 1 . . . . 135 . . . 5785 1 489 . 1 1 53 53 LEU CA C 13 52.82 0.12 . 1 . . . . 135 . . . 5785 1 490 . 1 1 53 53 LEU CB C 13 45.02 0.12 . 1 . . . . 135 . . . 5785 1 491 . 1 1 53 53 LEU CG C 13 27.06 0.12 . 1 . . . . 135 . . . 5785 1 492 . 1 1 53 53 LEU CD1 C 13 22.57 0.12 . 1 . . . . 135 . . . 5785 1 493 . 1 1 53 53 LEU CD2 C 13 24.46 0.12 . 1 . . . . 135 . . . 5785 1 494 . 1 1 53 53 LEU N N 15 125.69 0.1 . 1 . . . . 135 . . . 5785 1 495 . 1 1 54 54 TYR H H 1 9.11 0.02 . 1 . . . . 136 . . . 5785 1 496 . 1 1 54 54 TYR HA H 1 4.34 0.02 . 1 . . . . 136 . . . 5785 1 497 . 1 1 54 54 TYR HB2 H 1 3.22 0.02 . 2 . . . . 136 . . . 5785 1 498 . 1 1 54 54 TYR HB3 H 1 2.58 0.02 . 2 . . . . 136 . . . 5785 1 499 . 1 1 54 54 TYR C C 13 174.19 0.12 . 1 . . . . 136 . . . 5785 1 500 . 1 1 54 54 TYR CA C 13 58.49 0.12 . 1 . . . . 136 . . . 5785 1 501 . 1 1 54 54 TYR CB C 13 39.11 0.12 . 1 . . . . 136 . . . 5785 1 502 . 1 1 54 54 TYR N N 15 119.42 0.1 . 1 . . . . 136 . . . 5785 1 503 . 1 1 55 55 GLU H H 1 7.43 0.02 . 1 . . . . 137 . . . 5785 1 504 . 1 1 55 55 GLU HA H 1 4.27 0.02 . 1 . . . . 137 . . . 5785 1 505 . 1 1 55 55 GLU HB2 H 1 1.82 0.02 . 2 . . . . 137 . . . 5785 1 506 . 1 1 55 55 GLU HG2 H 1 1.99 0.02 . 2 . . . . 137 . . . 5785 1 507 . 1 1 55 55 GLU HG3 H 1 2.07 0.02 . 2 . . . . 137 . . . 5785 1 508 . 1 1 55 55 GLU C C 13 174.78 0.12 . 1 . . . . 137 . . . 5785 1 509 . 1 1 55 55 GLU CA C 13 54.36 0.02 . 1 . . . . 137 . . . 5785 1 510 . 1 1 55 55 GLU CB C 13 32.73 0.12 . 1 . . . . 137 . . . 5785 1 511 . 1 1 55 55 GLU CG C 13 34.86 0.12 . 1 . . . . 137 . . . 5785 1 512 . 1 1 55 55 GLU N N 15 117.05 0.1 . 1 . . . . 137 . . . 5785 1 513 . 1 1 56 56 GLY H H 1 8.42 0.02 . 1 . . . . 138 . . . 5785 1 514 . 1 1 56 56 GLY HA2 H 1 3.95 0.02 . 2 . . . . 138 . . . 5785 1 515 . 1 1 56 56 GLY HA3 H 1 3.65 0.02 . 2 . . . . 138 . . . 5785 1 516 . 1 1 56 56 GLY C C 13 172.40 0.12 . 1 . . . . 138 . . . 5785 1 517 . 1 1 56 56 GLY CA C 13 44.25 0.12 . 1 . . . . 138 . . . 5785 1 518 . 1 1 56 56 GLY N N 15 108.68 0.1 . 1 . . . . 138 . . . 5785 1 519 . 1 1 57 57 GLU H H 1 8.10 0.02 . 1 . . . . 139 . . . 5785 1 520 . 1 1 57 57 GLU HA H 1 4.20 0.02 . 1 . . . . 139 . . . 5785 1 521 . 1 1 57 57 GLU HB2 H 1 1.82 0.02 . 2 . . . . 139 . . . 5785 1 522 . 1 1 57 57 GLU HB3 H 1 1.74 0.02 . 2 . . . . 139 . . . 5785 1 523 . 1 1 57 57 GLU HG2 H 1 2.05 0.02 . 2 . . . . 139 . . . 5785 1 524 . 1 1 57 57 GLU C C 13 175.48 0.12 . 1 . . . . 139 . . . 5785 1 525 . 1 1 57 57 GLU CA C 13 55.72 0.12 . 1 . . . . 139 . . . 5785 1 526 . 1 1 57 57 GLU CB C 13 29.60 0.12 . 9 . . . . 139 . . . 5785 1 527 . 1 1 57 57 GLU CG C 13 35.57 0.12 . 1 . . . . 139 . . . 5785 1 528 . 1 1 57 57 GLU N N 15 119.51 0.1 . 1 . . . . 139 . . . 5785 1 529 . 1 1 58 58 ALA H H 1 7.91 0.02 . 1 . . . . 140 . . . 5785 1 530 . 1 1 58 58 ALA HA H 1 4.35 0.02 . 1 . . . . 140 . . . 5785 1 531 . 1 1 58 58 ALA HB1 H 1 0.78 0.02 . 1 . . . . 140 . . . 5785 1 532 . 1 1 58 58 ALA HB2 H 1 0.78 0.02 . 1 . . . . 140 . . . 5785 1 533 . 1 1 58 58 ALA HB3 H 1 0.78 0.02 . 1 . . . . 140 . . . 5785 1 534 . 1 1 58 58 ALA C C 13 176.18 0.12 . 1 . . . . 140 . . . 5785 1 535 . 1 1 58 58 ALA CA C 13 49.42 0.12 . 1 . . . . 140 . . . 5785 1 536 . 1 1 58 58 ALA CB C 13 21.94 0.12 . 1 . . . . 140 . . . 5785 1 537 . 1 1 58 58 ALA N N 15 131.73 0.1 . 1 . . . . 140 . . . 5785 1 538 . 1 1 59 59 ASP H H 1 8.20 0.02 . 1 . . . . 141 . . . 5785 1 539 . 1 1 59 59 ASP HA H 1 4.39 0.02 . 1 . . . . 141 . . . 5785 1 540 . 1 1 59 59 ASP HB2 H 1 2.66 0.02 . 2 . . . . 141 . . . 5785 1 541 . 1 1 59 59 ASP HB3 H 1 2.15 0.02 . 2 . . . . 141 . . . 5785 1 542 . 1 1 59 59 ASP C C 13 177.49 0.12 . 1 . . . . 141 . . . 5785 1 543 . 1 1 59 59 ASP CA C 13 58.37 0.12 . 1 . . . . 141 . . . 5785 1 544 . 1 1 59 59 ASP CB C 13 41.00 0.12 . 1 . . . . 141 . . . 5785 1 545 . 1 1 59 59 ASP N N 15 122.36 0.1 . 1 . . . . 141 . . . 5785 1 546 . 1 1 60 60 ILE H H 1 8.55 0.02 . 1 . . . . 142 . . . 5785 1 547 . 1 1 60 60 ILE HA H 1 4.09 0.02 . 1 . . . . 142 . . . 5785 1 548 . 1 1 60 60 ILE HB H 1 1.78 0.02 . 1 . . . . 142 . . . 5785 1 549 . 1 1 60 60 ILE HG12 H 1 1.62 0.02 . 2 . . . . 142 . . . 5785 1 550 . 1 1 60 60 ILE HG13 H 1 0.88 0.02 . 2 . . . . 142 . . . 5785 1 551 . 1 1 60 60 ILE HG21 H 1 0.85 0.02 . 1 . . . . 142 . . . 5785 1 552 . 1 1 60 60 ILE HG22 H 1 0.85 0.02 . 1 . . . . 142 . . . 5785 1 553 . 1 1 60 60 ILE HG23 H 1 0.85 0.02 . 1 . . . . 142 . . . 5785 1 554 . 1 1 60 60 ILE HD11 H 1 0.65 0.02 . 1 . . . . 142 . . . 5785 1 555 . 1 1 60 60 ILE HD12 H 1 0.65 0.02 . 1 . . . . 142 . . . 5785 1 556 . 1 1 60 60 ILE HD13 H 1 0.65 0.02 . 1 . . . . 142 . . . 5785 1 557 . 1 1 60 60 ILE C C 13 174.62 0.12 . 1 . . . . 142 . . . 5785 1 558 . 1 1 60 60 ILE CA C 13 60.49 0.12 . 1 . . . . 142 . . . 5785 1 559 . 1 1 60 60 ILE CB C 13 39.12 0.12 . 1 . . . . 142 . . . 5785 1 560 . 1 1 60 60 ILE CG1 C 13 28.52 0.12 . 1 . . . . 142 . . . 5785 1 561 . 1 1 60 60 ILE CG2 C 13 14.31 0.12 . 1 . . . . 142 . . . 5785 1 562 . 1 1 60 60 ILE CD1 C 13 14.31 0.12 . 1 . . . . 142 . . . 5785 1 563 . 1 1 60 60 ILE N N 15 124.30 0.1 . 1 . . . . 142 . . . 5785 1 564 . 1 1 61 61 MET H H 1 7.21 0.02 . 1 . . . . 143 . . . 5785 1 565 . 1 1 61 61 MET HA H 1 4.79 0.02 . 1 . . . . 143 . . . 5785 1 566 . 1 1 61 61 MET HB2 H 1 1.68 0.02 . 2 . . . . 143 . . . 5785 1 567 . 1 1 61 61 MET HB3 H 1 2.10 0.02 . 2 . . . . 143 . . . 5785 1 568 . 1 1 61 61 MET HE1 H 1 2.09 0.02 . 1 . . . . 143 . . . 5785 1 569 . 1 1 61 61 MET HE2 H 1 2.09 0.02 . 1 . . . . 143 . . . 5785 1 570 . 1 1 61 61 MET HE3 H 1 2.09 0.02 . 1 . . . . 143 . . . 5785 1 571 . 1 1 61 61 MET C C 13 176.89 0.12 . 1 . . . . 143 . . . 5785 1 572 . 1 1 61 61 MET CA C 13 53.64 0.12 . 1 . . . . 143 . . . 5785 1 573 . 1 1 61 61 MET CE C 13 18.79 0.12 . 1 . . . . 143 . . . 5785 1 574 . 1 1 61 61 MET N N 15 126.90 0.1 . 1 . . . . 143 . . . 5785 1 575 . 1 1 62 62 ILE H H 1 9.05 0.02 . 1 . . . . 144 . . . 5785 1 576 . 1 1 62 62 ILE HA H 1 5.36 0.02 . 1 . . . . 144 . . . 5785 1 577 . 1 1 62 62 ILE HB H 1 1.83 0.02 . 1 . . . . 144 . . . 5785 1 578 . 1 1 62 62 ILE HG12 H 1 1.60 0.02 . 2 . . . . 144 . . . 5785 1 579 . 1 1 62 62 ILE HG13 H 1 0.91 0.02 . 2 . . . . 144 . . . 5785 1 580 . 1 1 62 62 ILE HG21 H 1 0.61 0.02 . 1 . . . . 144 . . . 5785 1 581 . 1 1 62 62 ILE HG22 H 1 0.61 0.02 . 1 . . . . 144 . . . 5785 1 582 . 1 1 62 62 ILE HG23 H 1 0.61 0.02 . 1 . . . . 144 . . . 5785 1 583 . 1 1 62 62 ILE HD11 H 1 0.65 0.02 . 1 . . . . 144 . . . 5785 1 584 . 1 1 62 62 ILE HD12 H 1 0.65 0.02 . 1 . . . . 144 . . . 5785 1 585 . 1 1 62 62 ILE HD13 H 1 0.65 0.02 . 1 . . . . 144 . . . 5785 1 586 . 1 1 62 62 ILE C C 13 174.35 0.12 . 1 . . . . 144 . . . 5785 1 587 . 1 1 62 62 ILE CA C 13 60.49 0.12 . 1 . . . . 144 . . . 5785 1 588 . 1 1 62 62 ILE CB C 13 39.82 0.12 . 1 . . . . 144 . . . 5785 1 589 . 1 1 62 62 ILE CG1 C 13 28.48 0.12 . 1 . . . . 144 . . . 5785 1 590 . 1 1 62 62 ILE CG2 C 13 16.43 0.12 . 1 . . . . 144 . . . 5785 1 591 . 1 1 62 62 ILE CD1 C 13 14.31 0.12 . 1 . . . . 144 . . . 5785 1 592 . 1 1 62 62 ILE N N 15 128.53 0.1 . 1 . . . . 144 . . . 5785 1 593 . 1 1 63 63 SER H H 1 8.34 0.02 . 1 . . . . 145 . . . 5785 1 594 . 1 1 63 63 SER HA H 1 4.92 0.02 . 1 . . . . 145 . . . 5785 1 595 . 1 1 63 63 SER HB2 H 1 3.64 0.02 . 2 . . . . 145 . . . 5785 1 596 . 1 1 63 63 SER HB3 H 1 3.58 0.02 . 9 . . . . 145 . . . 5785 1 597 . 1 1 63 63 SER C C 13 172.03 0.12 . 1 . . . . 145 . . . 5785 1 598 . 1 1 63 63 SER CA C 13 56.72 0.02 . 1 . . . . 145 . . . 5785 1 599 . 1 1 63 63 SER CB C 13 66.51 0.12 . 1 . . . . 145 . . . 5785 1 600 . 1 1 63 63 SER N N 15 118.52 0.1 . 1 . . . . 145 . . . 5785 1 601 . 1 1 64 64 PHE H H 1 9.29 0.02 . 1 . . . . 146 . . . 5785 1 602 . 1 1 64 64 PHE HA H 1 5.19 0.02 . 1 . . . . 146 . . . 5785 1 603 . 1 1 64 64 PHE HB2 H 1 2.50 0.02 . 2 . . . . 146 . . . 5785 1 604 . 1 1 64 64 PHE HB3 H 1 2.69 0.02 . 2 . . . . 146 . . . 5785 1 605 . 1 1 64 64 PHE C C 13 176.12 0.12 . 1 . . . . 146 . . . 5785 1 606 . 1 1 64 64 PHE CA C 13 56.52 0.12 . 1 . . . . 146 . . . 5785 1 607 . 1 1 64 64 PHE CB C 13 41.24 0.12 . 1 . . . . 146 . . . 5785 1 608 . 1 1 64 64 PHE N N 15 120.77 0.1 . 1 . . . . 146 . . . 5785 1 609 . 1 1 65 65 ALA H H 1 9.18 0.02 . 1 . . . . 147 . . . 5785 1 610 . 1 1 65 65 ALA HA H 1 4.75 0.02 . 1 . . . . 147 . . . 5785 1 611 . 1 1 65 65 ALA HB1 H 1 0.95 0.02 . 1 . . . . 147 . . . 5785 1 612 . 1 1 65 65 ALA HB2 H 1 0.95 0.02 . 1 . . . . 147 . . . 5785 1 613 . 1 1 65 65 ALA HB3 H 1 0.95 0.02 . 1 . . . . 147 . . . 5785 1 614 . 1 1 65 65 ALA C C 13 175.21 0.12 . 1 . . . . 147 . . . 5785 1 615 . 1 1 65 65 ALA CA C 13 50.88 0.12 . 1 . . . . 147 . . . 5785 1 616 . 1 1 65 65 ALA CB C 13 23.35 0.12 . 1 . . . . 147 . . . 5785 1 617 . 1 1 65 65 ALA N N 15 125.98 0.1 . 1 . . . . 147 . . . 5785 1 618 . 1 1 66 66 VAL H H 1 8.11 0.02 . 1 . . . . 148 . . . 5785 1 619 . 1 1 66 66 VAL HA H 1 4.83 0.02 . 1 . . . . 148 . . . 5785 1 620 . 1 1 66 66 VAL HB H 1 2.08 0.02 . 1 . . . . 148 . . . 5785 1 621 . 1 1 66 66 VAL HG11 H 1 0.75 0.02 . 2 . . . . 148 . . . 5785 1 622 . 1 1 66 66 VAL HG12 H 1 0.75 0.02 . 2 . . . . 148 . . . 5785 1 623 . 1 1 66 66 VAL HG13 H 1 0.75 0.02 . 2 . . . . 148 . . . 5785 1 624 . 1 1 66 66 VAL HG21 H 1 0.79 0.02 . 2 . . . . 148 . . . 5785 1 625 . 1 1 66 66 VAL HG22 H 1 0.79 0.02 . 2 . . . . 148 . . . 5785 1 626 . 1 1 66 66 VAL HG23 H 1 0.79 0.02 . 2 . . . . 148 . . . 5785 1 627 . 1 1 66 66 VAL C C 13 174.52 0.12 . 1 . . . . 148 . . . 5785 1 628 . 1 1 66 66 VAL CA C 13 59.26 0.12 . 1 . . . . 148 . . . 5785 1 629 . 1 1 66 66 VAL CB C 13 35.09 0.02 . 1 . . . . 148 . . . 5785 1 630 . 1 1 66 66 VAL CG1 C 13 18.32 0.02 . 1 . . . . 148 . . . 5785 1 631 . 1 1 66 66 VAL CG2 C 13 22.34 0.02 . 1 . . . . 148 . . . 5785 1 632 . 1 1 66 66 VAL N N 15 112.76 0.1 . 1 . . . . 148 . . . 5785 1 633 . 1 1 67 67 ARG H H 1 9.51 0.02 . 1 . . . . 149 . . . 5785 1 634 . 1 1 67 67 ARG HA H 1 3.65 0.02 . 1 . . . . 149 . . . 5785 1 635 . 1 1 67 67 ARG HD2 H 1 3.12 0.02 . 2 . . . . 149 . . . 5785 1 636 . 1 1 67 67 ARG C C 13 177.46 0.12 . 1 . . . . 149 . . . 5785 1 637 . 1 1 67 67 ARG CA C 13 56.63 0.12 . 1 . . . . 149 . . . 5785 1 638 . 1 1 67 67 ARG CD C 13 43.13 0.12 . 1 . . . . 149 . . . 5785 1 639 . 1 1 67 67 ARG N N 15 118.06 0.1 . 1 . . . . 149 . . . 5785 1 640 . 1 1 68 68 GLU H H 1 8.27 0.02 . 1 . . . . 150 . . . 5785 1 641 . 1 1 68 68 GLU HA H 1 4.13 0.02 . 1 . . . . 150 . . . 5785 1 642 . 1 1 68 68 GLU HB2 H 1 2.06 0.02 . 2 . . . . 150 . . . 5785 1 643 . 1 1 68 68 GLU HB3 H 1 1.94 0.02 . 9 . . . . 150 . . . 5785 1 644 . 1 1 68 68 GLU HG2 H 1 2.28 0.02 . 2 . . . . 150 . . . 5785 1 645 . 1 1 68 68 GLU C C 13 175.18 0.12 . 1 . . . . 150 . . . 5785 1 646 . 1 1 68 68 GLU CA C 13 58.02 0.12 . 1 . . . . 150 . . . 5785 1 647 . 1 1 68 68 GLU CB C 13 28.76 0.02 . 1 . . . . 150 . . . 5785 1 648 . 1 1 68 68 GLU CG C 13 36.06 0.02 . 1 . . . . 150 . . . 5785 1 649 . 1 1 68 68 GLU N N 15 128.71 0.1 . 1 . . . . 150 . . . 5785 1 650 . 1 1 69 69 HIS H H 1 9.17 0.02 . 1 . . . . 151 . . . 5785 1 651 . 1 1 69 69 HIS HA H 1 4.96 0.02 . 1 . . . . 151 . . . 5785 1 652 . 1 1 69 69 HIS HB2 H 1 3.27 0.02 . 2 . . . . 151 . . . 5785 1 653 . 1 1 69 69 HIS HB3 H 1 2.66 0.02 . 2 . . . . 151 . . . 5785 1 654 . 1 1 69 69 HIS C C 13 174.62 0.12 . 1 . . . . 151 . . . 5785 1 655 . 1 1 69 69 HIS CA C 13 54.29 0.12 . 1 . . . . 151 . . . 5785 1 656 . 1 1 69 69 HIS CB C 13 29.00 0.12 . 1 . . . . 151 . . . 5785 1 657 . 1 1 69 69 HIS N N 15 121.72 0.1 . 1 . . . . 151 . . . 5785 1 658 . 1 1 70 70 GLY C C 13 173.79 0.12 . 1 . . . . 152 . . . 5785 1 659 . 1 1 71 71 ASP H H 1 6.77 0.02 . 1 . . . . 153 . . . 5785 1 660 . 1 1 71 71 ASP HA H 1 4.28 0.02 . 1 . . . . 153 . . . 5785 1 661 . 1 1 71 71 ASP HB2 H 1 3.04 0.02 . 2 . . . . 153 . . . 5785 1 662 . 1 1 71 71 ASP HB3 H 1 2.87 0.02 . 2 . . . . 153 . . . 5785 1 663 . 1 1 71 71 ASP C C 13 175.32 0.12 . 1 . . . . 153 . . . 5785 1 664 . 1 1 71 71 ASP CA C 13 50.75 0.12 . 1 . . . . 153 . . . 5785 1 665 . 1 1 71 71 ASP N N 15 117.27 0.1 . 1 . . . . 153 . . . 5785 1 666 . 1 1 72 72 PHE H H 1 7.36 0.02 . 1 . . . . 154 . . . 5785 1 667 . 1 1 72 72 PHE HA H 1 4.13 0.02 . 1 . . . . 154 . . . 5785 1 668 . 1 1 72 72 PHE C C 13 174.06 0.12 . 1 . . . . 154 . . . 5785 1 669 . 1 1 72 72 PHE N N 15 112.52 0.1 . 1 . . . . 154 . . . 5785 1 670 . 1 1 73 73 TYR H H 1 6.65 0.02 . 1 . . . . 155 . . . 5785 1 671 . 1 1 73 73 TYR N N 15 118.97 0.1 . 1 . . . . 155 . . . 5785 1 672 . 1 1 74 74 PRO C C 13 171.89 0.12 . 1 . . . . 156 . . . 5785 1 673 . 1 1 75 75 PHE H H 1 8.12 0.02 . 1 . . . . 157 . . . 5785 1 674 . 1 1 75 75 PHE HA H 1 4.85 0.02 . 1 . . . . 157 . . . 5785 1 675 . 1 1 75 75 PHE HB2 H 1 3.80 0.02 . 2 . . . . 157 . . . 5785 1 676 . 1 1 75 75 PHE C C 13 176.05 0.12 . 1 . . . . 157 . . . 5785 1 677 . 1 1 75 75 PHE CA C 13 57.4 0.12 . 1 . . . . 157 . . . 5785 1 678 . 1 1 75 75 PHE N N 15 119.94 0.1 . 1 . . . . 157 . . . 5785 1 679 . 1 1 76 76 ASP H H 1 8.02 0.02 . 1 . . . . 158 . . . 5785 1 680 . 1 1 76 76 ASP HA H 1 4.55 0.02 . 1 . . . . 158 . . . 5785 1 681 . 1 1 76 76 ASP C C 13 177.94 0.12 . 1 . . . . 158 . . . 5785 1 682 . 1 1 76 76 ASP CA C 13 53.67 0.12 . 1 . . . . 158 . . . 5785 1 683 . 1 1 76 76 ASP N N 15 116.61 0.1 . 1 . . . . 158 . . . 5785 1 684 . 1 1 77 77 GLY H H 1 8.95 0.02 . 1 . . . . 159 . . . 5785 1 685 . 1 1 77 77 GLY CA C 13 43.78 0.12 . 1 . . . . 159 . . . 5785 1 686 . 1 1 77 77 GLY N N 15 111.07 0.1 . 1 . . . . 159 . . . 5785 1 687 . 1 1 78 78 PRO HA H 1 3.75 0.02 . 1 . . . . 160 . . . 5785 1 688 . 1 1 78 78 PRO HB2 H 1 2.11 0.02 . 2 . . . . 160 . . . 5785 1 689 . 1 1 78 78 PRO HB3 H 1 1.66 0.02 . 2 . . . . 160 . . . 5785 1 690 . 1 1 78 78 PRO HG2 H 1 1.85 0.02 . 2 . . . . 160 . . . 5785 1 691 . 1 1 78 78 PRO C C 13 178.03 0.12 . 1 . . . . 160 . . . 5785 1 692 . 1 1 78 78 PRO CB C 13 31.35 0.12 . 1 . . . . 160 . . . 5785 1 693 . 1 1 79 79 GLY C C 13 173.63 0.12 . 1 . . . . 161 . . . 5785 1 694 . 1 1 80 80 ASN H H 1 8.47 0.02 . 1 . . . . 162 . . . 5785 1 695 . 1 1 80 80 ASN HA H 1 4.17 0.02 . 1 . . . . 162 . . . 5785 1 696 . 1 1 80 80 ASN C C 13 173.49 0.12 . 1 . . . . 162 . . . 5785 1 697 . 1 1 80 80 ASN CA C 13 56.77 0.12 . 1 . . . . 162 . . . 5785 1 698 . 1 1 80 80 ASN N N 15 118.78 0.1 . 1 . . . . 162 . . . 5785 1 699 . 1 1 81 81 VAL H H 1 9.71 0.02 . 1 . . . . 163 . . . 5785 1 700 . 1 1 81 81 VAL HB H 1 2.42 0.02 . 1 . . . . 163 . . . 5785 1 701 . 1 1 81 81 VAL HG11 H 1 1.15 0.02 . 2 . . . . 163 . . . 5785 1 702 . 1 1 81 81 VAL HG12 H 1 1.15 0.02 . 2 . . . . 163 . . . 5785 1 703 . 1 1 81 81 VAL HG13 H 1 1.15 0.02 . 2 . . . . 163 . . . 5785 1 704 . 1 1 81 81 VAL HG21 H 1 1.24 0.02 . 2 . . . . 163 . . . 5785 1 705 . 1 1 81 81 VAL HG22 H 1 1.24 0.02 . 2 . . . . 163 . . . 5785 1 706 . 1 1 81 81 VAL HG23 H 1 1.24 0.02 . 2 . . . . 163 . . . 5785 1 707 . 1 1 81 81 VAL CA C 13 64.76 0.12 . 1 . . . . 163 . . . 5785 1 708 . 1 1 81 81 VAL CG2 C 13 22.34 0.12 . 1 . . . . 163 . . . 5785 1 709 . 1 1 81 81 VAL N N 15 127.55 0.1 . 1 . . . . 163 . . . 5785 1 710 . 1 1 82 82 LEU H H 1 9.52 0.02 . 1 . . . . 164 . . . 5785 1 711 . 1 1 82 82 LEU HA H 1 4.38 0.02 . 1 . . . . 164 . . . 5785 1 712 . 1 1 82 82 LEU HG H 1 1.62 0.02 . 1 . . . . 164 . . . 5785 1 713 . 1 1 82 82 LEU HD11 H 1 0.34 0.02 . 1 . . . . 164 . . . 5785 1 714 . 1 1 82 82 LEU HD12 H 1 0.34 0.02 . 1 . . . . 164 . . . 5785 1 715 . 1 1 82 82 LEU HD13 H 1 0.34 0.02 . 1 . . . . 164 . . . 5785 1 716 . 1 1 82 82 LEU HD21 H 1 0.39 0.02 . 1 . . . . 164 . . . 5785 1 717 . 1 1 82 82 LEU HD22 H 1 0.39 0.02 . 1 . . . . 164 . . . 5785 1 718 . 1 1 82 82 LEU HD23 H 1 0.39 0.02 . 1 . . . . 164 . . . 5785 1 719 . 1 1 82 82 LEU C C 13 175.71 0.12 . 1 . . . . 164 . . . 5785 1 720 . 1 1 82 82 LEU CA C 13 55.65 0.12 . 1 . . . . 164 . . . 5785 1 721 . 1 1 82 82 LEU CG C 13 26.12 0.12 . 1 . . . . 164 . . . 5785 1 722 . 1 1 82 82 LEU CD1 C 13 21.87 0.12 . 1 . . . . 164 . . . 5785 1 723 . 1 1 82 82 LEU CD2 C 13 25.41 0.12 . 1 . . . . 164 . . . 5785 1 724 . 1 1 82 82 LEU N N 15 129.32 0.1 . 1 . . . . 164 . . . 5785 1 725 . 1 1 83 83 ALA H H 1 7.52 0.02 . 1 . . . . 165 . . . 5785 1 726 . 1 1 83 83 ALA HB1 H 1 1.28 0.02 . 1 . . . . 165 . . . 5785 1 727 . 1 1 83 83 ALA HB2 H 1 1.28 0.02 . 1 . . . . 165 . . . 5785 1 728 . 1 1 83 83 ALA HB3 H 1 1.28 0.02 . 1 . . . . 165 . . . 5785 1 729 . 1 1 83 83 ALA C C 13 174.66 0.12 . 1 . . . . 165 . . . 5785 1 730 . 1 1 83 83 ALA CA C 13 51.46 0.12 . 1 . . . . 165 . . . 5785 1 731 . 1 1 83 83 ALA CB C 13 22.34 0.12 . 1 . . . . 165 . . . 5785 1 732 . 1 1 83 83 ALA N N 15 116.47 0.1 . 1 . . . . 165 . . . 5785 1 733 . 1 1 84 84 HIS H H 1 8.77 0.02 . 1 . . . . 166 . . . 5785 1 734 . 1 1 84 84 HIS HB2 H 1 3.07 0.02 . 2 . . . . 166 . . . 5785 1 735 . 1 1 84 84 HIS HB3 H 1 2.88 0.02 . 2 . . . . 166 . . . 5785 1 736 . 1 1 84 84 HIS C C 13 172.48 0.12 . 1 . . . . 166 . . . 5785 1 737 . 1 1 84 84 HIS CA C 13 54.31 0.12 . 1 . . . . 166 . . . 5785 1 738 . 1 1 84 84 HIS N N 15 108.45 0.1 . 1 . . . . 166 . . . 5785 1 739 . 1 1 85 85 ALA H H 1 6.95 0.02 . 1 . . . . 167 . . . 5785 1 740 . 1 1 85 85 ALA HB1 H 1 1.49 0.02 . 1 . . . . 167 . . . 5785 1 741 . 1 1 85 85 ALA HB2 H 1 1.49 0.02 . 1 . . . . 167 . . . 5785 1 742 . 1 1 85 85 ALA HB3 H 1 1.49 0.02 . 1 . . . . 167 . . . 5785 1 743 . 1 1 85 85 ALA C C 13 174.62 0.12 . 1 . . . . 167 . . . 5785 1 744 . 1 1 85 85 ALA CA C 13 51.78 0.12 . 1 . . . . 167 . . . 5785 1 745 . 1 1 85 85 ALA CB C 13 24.7 0.12 . 1 . . . . 167 . . . 5785 1 746 . 1 1 85 85 ALA N N 15 118.92 0.1 . 1 . . . . 167 . . . 5785 1 747 . 1 1 86 86 TYR H H 1 7.77 0.02 . 1 . . . . 168 . . . 5785 1 748 . 1 1 86 86 TYR HA H 1 4.17 0.02 . 1 . . . . 168 . . . 5785 1 749 . 1 1 86 86 TYR HB2 H 1 2.80 0.02 . 2 . . . . 168 . . . 5785 1 750 . 1 1 86 86 TYR C C 13 173.97 0.12 . 1 . . . . 168 . . . 5785 1 751 . 1 1 86 86 TYR CA C 13 57.05 0.12 . 1 . . . . 168 . . . 5785 1 752 . 1 1 86 86 TYR N N 15 116.35 0.1 . 1 . . . . 168 . . . 5785 1 753 . 1 1 87 87 ALA H H 1 7.78 0.02 . 1 . . . . 169 . . . 5785 1 754 . 1 1 87 87 ALA HB1 H 1 1.18 0.02 . 1 . . . . 169 . . . 5785 1 755 . 1 1 87 87 ALA HB2 H 1 1.18 0.02 . 1 . . . . 169 . . . 5785 1 756 . 1 1 87 87 ALA HB3 H 1 1.18 0.02 . 1 . . . . 169 . . . 5785 1 757 . 1 1 87 87 ALA CA C 13 50.54 0.12 . 1 . . . . 169 . . . 5785 1 758 . 1 1 87 87 ALA CB C 13 16.9 0.12 . 1 . . . . 169 . . . 5785 1 759 . 1 1 87 87 ALA N N 15 121.80 0.1 . 1 . . . . 169 . . . 5785 1 760 . 1 1 89 89 GLY HA2 H 1 3.49 0.02 . 2 . . . . 171 . . . 5785 1 761 . 1 1 90 90 PRO HA H 1 4.55 0.02 . 1 . . . . 172 . . . 5785 1 762 . 1 1 90 90 PRO HB2 H 1 1.91 0.02 . 2 . . . . 172 . . . 5785 1 763 . 1 1 90 90 PRO HB3 H 1 2.21 0.02 . 2 . . . . 172 . . . 5785 1 764 . 1 1 90 90 PRO C C 13 177.89 0.12 . 1 . . . . 172 . . . 5785 1 765 . 1 1 90 90 PRO CB C 13 33.00 0.12 . 1 . . . . 172 . . . 5785 1 766 . 1 1 91 91 GLY H H 1 8.62 0.02 . 1 . . . . 173 . . . 5785 1 767 . 1 1 91 91 GLY C C 13 175.29 0.12 . 1 . . . . 173 . . . 5785 1 768 . 1 1 91 91 GLY CA C 13 46.49 0.12 . 1 . . . . 173 . . . 5785 1 769 . 1 1 91 91 GLY N N 15 109.84 0.1 . 1 . . . . 173 . . . 5785 1 770 . 1 1 92 92 ILE H H 1 8.71 0.02 . 1 . . . . 174 . . . 5785 1 771 . 1 1 92 92 ILE HA H 1 4.01 0.02 . 1 . . . . 174 . . . 5785 1 772 . 1 1 92 92 ILE HB H 1 1.39 0.02 . 1 . . . . 174 . . . 5785 1 773 . 1 1 92 92 ILE HG12 H 1 0.84 0.02 . 9 . . . . 174 . . . 5785 1 774 . 1 1 92 92 ILE HG13 H 1 0.31 0.02 . 9 . . . . 174 . . . 5785 1 775 . 1 1 92 92 ILE HG21 H 1 0.26 0.02 . 1 . . . . 174 . . . 5785 1 776 . 1 1 92 92 ILE HG22 H 1 0.26 0.02 . 1 . . . . 174 . . . 5785 1 777 . 1 1 92 92 ILE HG23 H 1 0.26 0.02 . 1 . . . . 174 . . . 5785 1 778 . 1 1 92 92 ILE HD11 H 1 0.53 0.02 . 1 . . . . 174 . . . 5785 1 779 . 1 1 92 92 ILE HD12 H 1 0.53 0.02 . 1 . . . . 174 . . . 5785 1 780 . 1 1 92 92 ILE HD13 H 1 0.53 0.02 . 1 . . . . 174 . . . 5785 1 781 . 1 1 92 92 ILE C C 13 174.01 0.12 . 1 . . . . 174 . . . 5785 1 782 . 1 1 92 92 ILE CA C 13 61.48 0.12 . 1 . . . . 174 . . . 5785 1 783 . 1 1 92 92 ILE CB C 13 37.22 0.12 . 1 . . . . 174 . . . 5785 1 784 . 1 1 92 92 ILE CG1 C 13 28.01 0.12 . 1 . . . . 174 . . . 5785 1 785 . 1 1 92 92 ILE CG2 C 13 15.72 0.12 . 1 . . . . 174 . . . 5785 1 786 . 1 1 92 92 ILE CD1 C 13 15.01 0.12 . 1 . . . . 174 . . . 5785 1 787 . 1 1 92 92 ILE N N 15 132.24 0.1 . 1 . . . . 174 . . . 5785 1 788 . 1 1 93 93 ASN H H 1 7.07 0.02 . 1 . . . . 175 . . . 5785 1 789 . 1 1 93 93 ASN CA C 13 55.73 0.12 . 1 . . . . 175 . . . 5785 1 790 . 1 1 93 93 ASN N N 15 118.39 0.1 . 1 . . . . 175 . . . 5785 1 791 . 1 1 94 94 GLY C C 13 171.64 0.12 . 1 . . . . 176 . . . 5785 1 792 . 1 1 95 95 ASP H H 1 7.76 0.02 . 1 . . . . 177 . . . 5785 1 793 . 1 1 95 95 ASP HA H 1 4.54 0.02 . 1 . . . . 177 . . . 5785 1 794 . 1 1 95 95 ASP C C 13 173.85 0.12 . 1 . . . . 177 . . . 5785 1 795 . 1 1 95 95 ASP CA C 13 55.10 0.12 . 1 . . . . 177 . . . 5785 1 796 . 1 1 95 95 ASP N N 15 121.59 0.1 . 1 . . . . 177 . . . 5785 1 797 . 1 1 96 96 ALA H H 1 7.91 0.02 . 1 . . . . 178 . . . 5785 1 798 . 1 1 96 96 ALA HA H 1 4.75 0.02 . 1 . . . . 178 . . . 5785 1 799 . 1 1 96 96 ALA C C 13 175.05 0.12 . 1 . . . . 178 . . . 5785 1 800 . 1 1 96 96 ALA CA C 13 51.35 0.12 . 1 . . . . 178 . . . 5785 1 801 . 1 1 96 96 ALA N N 15 118.68 0.1 . 1 . . . . 178 . . . 5785 1 802 . 1 1 97 97 HIS H H 1 8.79 0.02 . 1 . . . . 179 . . . 5785 1 803 . 1 1 97 97 HIS HA H 1 5.65 0.02 . 1 . . . . 179 . . . 5785 1 804 . 1 1 97 97 HIS HB2 H 1 3.06 0.02 . 2 . . . . 179 . . . 5785 1 805 . 1 1 97 97 HIS C C 13 172.83 0.12 . 1 . . . . 179 . . . 5785 1 806 . 1 1 97 97 HIS CA C 13 50.59 0.12 . 1 . . . . 179 . . . 5785 1 807 . 1 1 97 97 HIS N N 15 119.99 0.1 . 1 . . . . 179 . . . 5785 1 808 . 1 1 98 98 PHE H H 1 8.44 0.02 . 1 . . . . 180 . . . 5785 1 809 . 1 1 98 98 PHE HA H 1 4.04 0.02 . 1 . . . . 180 . . . 5785 1 810 . 1 1 98 98 PHE C C 13 174.27 0.12 . 1 . . . . 180 . . . 5785 1 811 . 1 1 98 98 PHE CA C 13 56.64 0.12 . 1 . . . . 180 . . . 5785 1 812 . 1 1 98 98 PHE N N 15 121.73 0.1 . 1 . . . . 180 . . . 5785 1 813 . 1 1 99 99 ASP H H 1 7.98 0.02 . 1 . . . . 181 . . . 5785 1 814 . 1 1 99 99 ASP C C 13 179.38 0.12 . 1 . . . . 181 . . . 5785 1 815 . 1 1 99 99 ASP CA C 13 53.72 0.12 . 1 . . . . 181 . . . 5785 1 816 . 1 1 99 99 ASP N N 15 124.00 0.1 . 1 . . . . 181 . . . 5785 1 817 . 1 1 100 100 ASP H H 1 9.80 0.02 . 1 . . . . 182 . . . 5785 1 818 . 1 1 100 100 ASP HA H 1 5.40 0.02 . 1 . . . . 182 . . . 5785 1 819 . 1 1 100 100 ASP HB2 H 1 2.35 0.02 . 2 . . . . 182 . . . 5785 1 820 . 1 1 100 100 ASP HB3 H 1 2.77 0.02 . 2 . . . . 182 . . . 5785 1 821 . 1 1 100 100 ASP C C 13 179.33 0.12 . 1 . . . . 182 . . . 5785 1 822 . 1 1 100 100 ASP CA C 13 53.03 0.12 . 1 . . . . 182 . . . 5785 1 823 . 1 1 100 100 ASP CB C 13 40.53 0.12 . 1 . . . . 182 . . . 5785 1 824 . 1 1 100 100 ASP N N 15 128.89 0.1 . 1 . . . . 182 . . . 5785 1 825 . 1 1 101 101 ASP H H 1 9.26 0.02 . 1 . . . . 183 . . . 5785 1 826 . 1 1 101 101 ASP HA H 1 4.85 0.02 . 1 . . . . 183 . . . 5785 1 827 . 1 1 101 101 ASP C C 13 177.35 0.12 . 1 . . . . 183 . . . 5785 1 828 . 1 1 101 101 ASP CA C 13 56.31 0.12 . 1 . . . . 183 . . . 5785 1 829 . 1 1 101 101 ASP CB C 13 38.65 0.12 . 1 . . . . 183 . . . 5785 1 830 . 1 1 101 101 ASP N N 15 124.72 0.1 . 1 . . . . 183 . . . 5785 1 831 . 1 1 102 102 GLU H H 1 7.18 0.02 . 1 . . . . 184 . . . 5785 1 832 . 1 1 102 102 GLU HA H 1 4.26 0.02 . 1 . . . . 184 . . . 5785 1 833 . 1 1 102 102 GLU C C 13 175.74 0.12 . 1 . . . . 184 . . . 5785 1 834 . 1 1 102 102 GLU CA C 13 52.87 0.12 . 1 . . . . 184 . . . 5785 1 835 . 1 1 102 102 GLU N N 15 116.58 0.1 . 1 . . . . 184 . . . 5785 1 836 . 1 1 103 103 GLN H H 1 8.34 0.02 . 1 . . . . 185 . . . 5785 1 837 . 1 1 103 103 GLN HA H 1 4.27 0.02 . 1 . . . . 185 . . . 5785 1 838 . 1 1 103 103 GLN HB2 H 1 1.84 0.02 . 2 . . . . 185 . . . 5785 1 839 . 1 1 103 103 GLN HB3 H 1 1.62 0.02 . 2 . . . . 185 . . . 5785 1 840 . 1 1 103 103 GLN HG2 H 1 2.07 0.02 . 2 . . . . 185 . . . 5785 1 841 . 1 1 103 103 GLN HG3 H 1 1.84 0.02 . 2 . . . . 185 . . . 5785 1 842 . 1 1 103 103 GLN C C 13 173.50 0.12 . 1 . . . . 185 . . . 5785 1 843 . 1 1 103 103 GLN CA C 13 53.51 0.12 . 1 . . . . 185 . . . 5785 1 844 . 1 1 103 103 GLN CB C 13 27.12 0.12 . 1 . . . . 185 . . . 5785 1 845 . 1 1 103 103 GLN CG C 13 32.73 0.12 . 1 . . . . 185 . . . 5785 1 846 . 1 1 103 103 GLN N N 15 126.59 0.1 . 1 . . . . 185 . . . 5785 1 847 . 1 1 104 104 TRP H H 1 9.52 0.02 . 1 . . . . 186 . . . 5785 1 848 . 1 1 104 104 TRP HA H 1 4.96 0.02 . 1 . . . . 186 . . . 5785 1 849 . 1 1 104 104 TRP C C 13 177.55 0.12 . 1 . . . . 186 . . . 5785 1 850 . 1 1 104 104 TRP CA C 13 56.96 0.12 . 1 . . . . 186 . . . 5785 1 851 . 1 1 104 104 TRP N N 15 131.97 0.1 . 1 . . . . 186 . . . 5785 1 852 . 1 1 105 105 THR H H 1 8.79 0.02 . 1 . . . . 187 . . . 5785 1 853 . 1 1 105 105 THR HA H 1 4.80 0.02 . 1 . . . . 187 . . . 5785 1 854 . 1 1 105 105 THR HB H 1 4.35 0.02 . 1 . . . . 187 . . . 5785 1 855 . 1 1 105 105 THR HG21 H 1 0.97 0.02 . 1 . . . . 187 . . . 5785 1 856 . 1 1 105 105 THR HG22 H 1 0.97 0.02 . 1 . . . . 187 . . . 5785 1 857 . 1 1 105 105 THR HG23 H 1 0.97 0.02 . 1 . . . . 187 . . . 5785 1 858 . 1 1 105 105 THR C C 13 175.43 0.12 . 1 . . . . 187 . . . 5785 1 859 . 1 1 105 105 THR CA C 13 60.08 0.12 . 1 . . . . 187 . . . 5785 1 860 . 1 1 105 105 THR CB C 13 72.29 0.12 . 1 . . . . 187 . . . 5785 1 861 . 1 1 105 105 THR CG2 C 13 20.53 0.12 . 1 . . . . 187 . . . 5785 1 862 . 1 1 105 105 THR N N 15 111.35 0.1 . 1 . . . . 187 . . . 5785 1 863 . 1 1 106 106 LYS H H 1 8.91 0.02 . 1 . . . . 188 . . . 5785 1 864 . 1 1 106 106 LYS HA H 1 4.46 0.02 . 1 . . . . 188 . . . 5785 1 865 . 1 1 106 106 LYS HB2 H 1 1.88 0.02 . 2 . . . . 188 . . . 5785 1 866 . 1 1 106 106 LYS HB3 H 1 1.65 0.02 . 2 . . . . 188 . . . 5785 1 867 . 1 1 106 106 LYS HG2 H 1 1.40 0.02 . 1 . . . . 188 . . . 5785 1 868 . 1 1 106 106 LYS HD2 H 1 1.58 0.02 . 2 . . . . 188 . . . 5785 1 869 . 1 1 106 106 LYS HE3 H 1 2.89 0.02 . 2 . . . . 188 . . . 5785 1 870 . 1 1 106 106 LYS C C 13 176.27 0.12 . 1 . . . . 188 . . . 5785 1 871 . 1 1 106 106 LYS CA C 13 56.38 0.12 . 1 . . . . 188 . . . 5785 1 872 . 1 1 106 106 LYS CB C 13 32.97 0.12 . 1 . . . . 188 . . . 5785 1 873 . 1 1 106 106 LYS CG C 13 23.99 0.12 . 1 . . . . 188 . . . 5785 1 874 . 1 1 106 106 LYS CD C 13 29.19 0.12 . 1 . . . . 188 . . . 5785 1 875 . 1 1 106 106 LYS CE C 13 41.47 0.12 . 1 . . . . 188 . . . 5785 1 876 . 1 1 106 106 LYS N N 15 120.13 0.1 . 1 . . . . 188 . . . 5785 1 877 . 1 1 107 107 ASP H H 1 7.41 0.02 . 1 . . . . 189 . . . 5785 1 878 . 1 1 107 107 ASP HA H 1 4.80 0.02 . 1 . . . . 189 . . . 5785 1 879 . 1 1 107 107 ASP HB2 H 1 2.63 0.02 . 2 . . . . 189 . . . 5785 1 880 . 1 1 107 107 ASP HB3 H 1 3.24 0.02 . 2 . . . . 189 . . . 5785 1 881 . 1 1 107 107 ASP C C 13 177.81 0.12 . 1 . . . . 189 . . . 5785 1 882 . 1 1 107 107 ASP CA C 13 52.28 0.12 . 1 . . . . 189 . . . 5785 1 883 . 1 1 107 107 ASP CB C 13 41.47 0.12 . 1 . . . . 189 . . . 5785 1 884 . 1 1 107 107 ASP N N 15 121.14 0.1 . 1 . . . . 189 . . . 5785 1 885 . 1 1 108 108 THR HA H 1 4.58 0.02 . 1 . . . . 190 . . . 5785 1 886 . 1 1 108 108 THR HB H 1 4.80 0.02 . 1 . . . . 190 . . . 5785 1 887 . 1 1 108 108 THR HG21 H 1 1.15 0.02 . 1 . . . . 190 . . . 5785 1 888 . 1 1 108 108 THR HG22 H 1 1.15 0.02 . 1 . . . . 190 . . . 5785 1 889 . 1 1 108 108 THR HG23 H 1 1.15 0.02 . 1 . . . . 190 . . . 5785 1 890 . 1 1 108 108 THR C C 13 174.92 0.12 . 1 . . . . 190 . . . 5785 1 891 . 1 1 108 108 THR CB C 13 67.93 0.12 . 1 . . . . 190 . . . 5785 1 892 . 1 1 108 108 THR CG2 C 13 21.39 0.12 . 1 . . . . 190 . . . 5785 1 893 . 1 1 109 109 THR H H 1 8.17 0.02 . 1 . . . . 191 . . . 5785 1 894 . 1 1 109 109 THR HB H 1 3.95 0.02 . 1 . . . . 191 . . . 5785 1 895 . 1 1 109 109 THR HG21 H 1 1.00 0.02 . 1 . . . . 191 . . . 5785 1 896 . 1 1 109 109 THR HG22 H 1 1.00 0.02 . 1 . . . . 191 . . . 5785 1 897 . 1 1 109 109 THR HG23 H 1 1.00 0.02 . 1 . . . . 191 . . . 5785 1 898 . 1 1 109 109 THR C C 13 175.32 0.12 . 1 . . . . 191 . . . 5785 1 899 . 1 1 109 109 THR CA C 13 64.05 0.12 . 1 . . . . 191 . . . 5785 1 900 . 1 1 109 109 THR CB C 13 69.94 0.12 . 1 . . . . 191 . . . 5785 1 901 . 1 1 109 109 THR CG2 C 13 21.47 0.12 . 1 . . . . 191 . . . 5785 1 902 . 1 1 109 109 THR N N 15 115.33 0.1 . 1 . . . . 191 . . . 5785 1 903 . 1 1 110 110 GLY H H 1 7.22 0.02 . 1 . . . . 192 . . . 5785 1 904 . 1 1 110 110 GLY HA2 H 1 4.28 0.02 . 2 . . . . 192 . . . 5785 1 905 . 1 1 110 110 GLY C C 13 173.42 0.12 . 1 . . . . 192 . . . 5785 1 906 . 1 1 110 110 GLY CA C 13 45.11 0.02 . 1 . . . . 192 . . . 5785 1 907 . 1 1 110 110 GLY N N 15 112.39 0.1 . 1 . . . . 192 . . . 5785 1 908 . 1 1 111 111 THR H H 1 8.29 0.02 . 1 . . . . 193 . . . 5785 1 909 . 1 1 111 111 THR HB H 1 2.85 0.02 . 1 . . . . 193 . . . 5785 1 910 . 1 1 111 111 THR HG21 H 1 0.61 0.02 . 1 . . . . 193 . . . 5785 1 911 . 1 1 111 111 THR HG22 H 1 0.61 0.02 . 1 . . . . 193 . . . 5785 1 912 . 1 1 111 111 THR HG23 H 1 0.61 0.02 . 1 . . . . 193 . . . 5785 1 913 . 1 1 111 111 THR CA C 13 62.3 0.12 . 1 . . . . 193 . . . 5785 1 914 . 1 1 111 111 THR CB C 13 67.82 0.12 . 1 . . . . 193 . . . 5785 1 915 . 1 1 111 111 THR CG2 C 13 24.53 0.12 . 1 . . . . 193 . . . 5785 1 916 . 1 1 111 111 THR N N 15 123.56 0.1 . 1 . . . . 193 . . . 5785 1 917 . 1 1 112 112 ASN HA H 1 4.72 0.02 . 1 . . . . 194 . . . 5785 1 918 . 1 1 112 112 ASN HB2 H 1 3.01 0.02 . 2 . . . . 194 . . . 5785 1 919 . 1 1 112 112 ASN HB3 H 1 2.76 0.02 . 2 . . . . 194 . . . 5785 1 920 . 1 1 112 112 ASN C C 13 174.92 0.12 . 1 . . . . 194 . . . 5785 1 921 . 1 1 112 112 ASN CB C 13 39.35 0.12 . 1 . . . . 194 . . . 5785 1 922 . 1 1 113 113 LEU H H 1 7.86 0.02 . 1 . . . . 195 . . . 5785 1 923 . 1 1 113 113 LEU HG H 1 1.04 0.02 . 1 . . . . 195 . . . 5785 1 924 . 1 1 113 113 LEU HD11 H 1 0.59 0.02 . 2 . . . . 195 . . . 5785 1 925 . 1 1 113 113 LEU HD12 H 1 0.59 0.02 . 2 . . . . 195 . . . 5785 1 926 . 1 1 113 113 LEU HD13 H 1 0.59 0.02 . 2 . . . . 195 . . . 5785 1 927 . 1 1 113 113 LEU HD21 H 1 -0.32 0.02 . 1 . . . . 195 . . . 5785 1 928 . 1 1 113 113 LEU HD22 H 1 -0.32 0.02 . 1 . . . . 195 . . . 5785 1 929 . 1 1 113 113 LEU HD23 H 1 -0.32 0.02 . 1 . . . . 195 . . . 5785 1 930 . 1 1 113 113 LEU C C 13 176.51 0.12 . 1 . . . . 195 . . . 5785 1 931 . 1 1 113 113 LEU CA C 13 57.78 0.12 . 1 . . . . 195 . . . 5785 1 932 . 1 1 113 113 LEU CG C 13 27.06 0.12 . 1 . . . . 195 . . . 5785 1 933 . 1 1 113 113 LEU CD1 C 13 28.01 0.12 . 1 . . . . 195 . . . 5785 1 934 . 1 1 113 113 LEU CD2 C 13 21.39 0.12 . 1 . . . . 195 . . . 5785 1 935 . 1 1 113 113 LEU N N 15 128.21 0.1 . 1 . . . . 195 . . . 5785 1 936 . 1 1 114 114 PHE H H 1 8.11 0.02 . 1 . . . . 196 . . . 5785 1 937 . 1 1 114 114 PHE HA H 1 3.92 0.02 . 1 . . . . 196 . . . 5785 1 938 . 1 1 114 114 PHE HB2 H 1 3.25 0.02 . 2 . . . . 196 . . . 5785 1 939 . 1 1 114 114 PHE HB3 H 1 3.11 0.02 . 9 . . . . 196 . . . 5785 1 940 . 1 1 114 114 PHE C C 13 175.20 0.12 . 1 . . . . 196 . . . 5785 1 941 . 1 1 114 114 PHE CA C 13 60.92 0.12 . 1 . . . . 196 . . . 5785 1 942 . 1 1 114 114 PHE N N 15 119.32 0.1 . 1 . . . . 196 . . . 5785 1 943 . 1 1 115 115 LEU H H 1 8.45 0.02 . 1 . . . . 197 . . . 5785 1 944 . 1 1 115 115 LEU HB2 H 1 1.65 0.02 . 2 . . . . 197 . . . 5785 1 945 . 1 1 115 115 LEU HG H 1 1.52 0.02 . 1 . . . . 197 . . . 5785 1 946 . 1 1 115 115 LEU HD11 H 1 0.58 0.02 . 1 . . . . 197 . . . 5785 1 947 . 1 1 115 115 LEU HD12 H 1 0.58 0.02 . 1 . . . . 197 . . . 5785 1 948 . 1 1 115 115 LEU HD13 H 1 0.58 0.02 . 1 . . . . 197 . . . 5785 1 949 . 1 1 115 115 LEU HD21 H 1 0.75 0.02 . 1 . . . . 197 . . . 5785 1 950 . 1 1 115 115 LEU HD22 H 1 0.75 0.02 . 1 . . . . 197 . . . 5785 1 951 . 1 1 115 115 LEU HD23 H 1 0.75 0.02 . 1 . . . . 197 . . . 5785 1 952 . 1 1 115 115 LEU C C 13 179.79 0.12 . 1 . . . . 197 . . . 5785 1 953 . 1 1 115 115 LEU CA C 13 57.63 0.12 . 1 . . . . 197 . . . 5785 1 954 . 1 1 115 115 LEU CG C 13 26.35 0.12 . 1 . . . . 197 . . . 5785 1 955 . 1 1 115 115 LEU CD1 C 13 22.1 0.12 . 1 . . . . 197 . . . 5785 1 956 . 1 1 115 115 LEU CD2 C 13 25.17 0.12 . 1 . . . . 197 . . . 5785 1 957 . 1 1 115 115 LEU N N 15 119.04 0.1 . 1 . . . . 197 . . . 5785 1 958 . 1 1 116 116 VAL H H 1 7.35 0.02 . 1 . . . . 198 . . . 5785 1 959 . 1 1 116 116 VAL HB H 1 2.21 0.02 . 1 . . . . 198 . . . 5785 1 960 . 1 1 116 116 VAL HG11 H 1 1.23 0.02 . 2 . . . . 198 . . . 5785 1 961 . 1 1 116 116 VAL HG12 H 1 1.23 0.02 . 2 . . . . 198 . . . 5785 1 962 . 1 1 116 116 VAL HG13 H 1 1.23 0.02 . 2 . . . . 198 . . . 5785 1 963 . 1 1 116 116 VAL HG21 H 1 1.17 0.02 . 2 . . . . 198 . . . 5785 1 964 . 1 1 116 116 VAL HG22 H 1 1.17 0.02 . 2 . . . . 198 . . . 5785 1 965 . 1 1 116 116 VAL HG23 H 1 1.17 0.02 . 2 . . . . 198 . . . 5785 1 966 . 1 1 116 116 VAL C C 13 178.12 0.12 . 1 . . . . 198 . . . 5785 1 967 . 1 1 116 116 VAL CA C 13 66.53 0.12 . 1 . . . . 198 . . . 5785 1 968 . 1 1 116 116 VAL CB C 13 32.26 0.12 . 1 . . . . 198 . . . 5785 1 969 . 1 1 116 116 VAL CG1 C 13 22.81 0.12 . 1 . . . . 198 . . . 5785 1 970 . 1 1 116 116 VAL CG2 C 13 23.76 0.12 . 1 . . . . 198 . . . 5785 1 971 . 1 1 116 116 VAL N N 15 117.71 0.1 . 1 . . . . 198 . . . 5785 1 972 . 1 1 117 117 ALA H H 1 9.17 0.02 . 1 . . . . 199 . . . 5785 1 973 . 1 1 117 117 ALA HA H 1 3.93 0.02 . 1 . . . . 199 . . . 5785 1 974 . 1 1 117 117 ALA HB1 H 1 0.97 0.02 . 1 . . . . 199 . . . 5785 1 975 . 1 1 117 117 ALA HB2 H 1 0.97 0.02 . 1 . . . . 199 . . . 5785 1 976 . 1 1 117 117 ALA HB3 H 1 0.97 0.02 . 1 . . . . 199 . . . 5785 1 977 . 1 1 117 117 ALA C C 13 178.58 0.12 . 1 . . . . 199 . . . 5785 1 978 . 1 1 117 117 ALA CA C 13 55.57 0.12 . 1 . . . . 199 . . . 5785 1 979 . 1 1 117 117 ALA CB C 13 16.2 0.12 . 1 . . . . 199 . . . 5785 1 980 . 1 1 117 117 ALA N N 15 121.65 0.1 . 1 . . . . 199 . . . 5785 1 981 . 1 1 118 118 ALA H H 1 8.50 0.02 . 1 . . . . 200 . . . 5785 1 982 . 1 1 118 118 ALA HA H 1 3.74 0.02 . 1 . . . . 200 . . . 5785 1 983 . 1 1 118 118 ALA HB1 H 1 0.88 0.02 . 1 . . . . 200 . . . 5785 1 984 . 1 1 118 118 ALA HB2 H 1 0.88 0.02 . 1 . . . . 200 . . . 5785 1 985 . 1 1 118 118 ALA HB3 H 1 0.88 0.02 . 1 . . . . 200 . . . 5785 1 986 . 1 1 118 118 ALA C C 13 179.36 0.12 . 1 . . . . 200 . . . 5785 1 987 . 1 1 118 118 ALA CA C 13 56.52 0.12 . 1 . . . . 200 . . . 5785 1 988 . 1 1 118 118 ALA CB C 13 16.76 0.12 . 1 . . . . 200 . . . 5785 1 989 . 1 1 118 118 ALA N N 15 118.91 0.1 . 1 . . . . 200 . . . 5785 1 990 . 1 1 119 119 HIS H H 1 7.15 0.02 . 1 . . . . 201 . . . 5785 1 991 . 1 1 119 119 HIS HA H 1 3.78 0.02 . 1 . . . . 201 . . . 5785 1 992 . 1 1 119 119 HIS C C 13 176.14 0.12 . 1 . . . . 201 . . . 5785 1 993 . 1 1 119 119 HIS CA C 13 59.29 0.12 . 1 . . . . 201 . . . 5785 1 994 . 1 1 119 119 HIS N N 15 117.72 0.1 . 1 . . . . 201 . . . 5785 1 995 . 1 1 120 120 GLN C C 13 178.94 0.12 . 1 . . . . 202 . . . 5785 1 996 . 1 1 120 120 GLN CA C 13 58.53 0.12 . 1 . . . . 202 . . . 5785 1 997 . 1 1 121 121 ILE H H 1 8.86 0.02 . 1 . . . . 203 . . . 5785 1 998 . 1 1 121 121 ILE HB H 1 1.82 0.02 . 1 . . . . 203 . . . 5785 1 999 . 1 1 121 121 ILE HG12 H 1 1.32 0.02 . 2 . . . . 203 . . . 5785 1 1000 . 1 1 121 121 ILE HG13 H 1 1.07 0.02 . 2 . . . . 203 . . . 5785 1 1001 . 1 1 121 121 ILE HG21 H 1 0.51 0.02 . 1 . . . . 203 . . . 5785 1 1002 . 1 1 121 121 ILE HG22 H 1 0.51 0.02 . 1 . . . . 203 . . . 5785 1 1003 . 1 1 121 121 ILE HG23 H 1 0.51 0.02 . 1 . . . . 203 . . . 5785 1 1004 . 1 1 121 121 ILE HD11 H 1 0.44 0.02 . 1 . . . . 203 . . . 5785 1 1005 . 1 1 121 121 ILE HD12 H 1 0.44 0.02 . 1 . . . . 203 . . . 5785 1 1006 . 1 1 121 121 ILE HD13 H 1 0.44 0.02 . 1 . . . . 203 . . . 5785 1 1007 . 1 1 121 121 ILE C C 13 177.8 0.12 . 1 . . . . 203 . . . 5785 1 1008 . 1 1 121 121 ILE CA C 13 62.52 0.12 . 1 . . . . 203 . . . 5785 1 1009 . 1 1 121 121 ILE CB C 13 35.8 0.12 . 1 . . . . 203 . . . 5785 1 1010 . 1 1 121 121 ILE CG1 C 13 29.19 0.12 . 1 . . . . 203 . . . 5785 1 1011 . 1 1 121 121 ILE CG2 C 13 17.61 0.12 . 1 . . . . 203 . . . 5785 1 1012 . 1 1 121 121 ILE CD1 C 13 11.24 0.12 . 1 . . . . 203 . . . 5785 1 1013 . 1 1 121 121 ILE N N 15 118.17 0.1 . 1 . . . . 203 . . . 5785 1 1014 . 1 1 122 122 GLY H H 1 7.41 0.02 . 1 . . . . 204 . . . 5785 1 1015 . 1 1 122 122 GLY HA2 H 1 2.37 0.02 . 2 . . . . 204 . . . 5785 1 1016 . 1 1 122 122 GLY C C 13 178.12 0.12 . 1 . . . . 204 . . . 5785 1 1017 . 1 1 122 122 GLY CA C 13 48.01 0.12 . 1 . . . . 204 . . . 5785 1 1018 . 1 1 122 122 GLY N N 15 109.73 0.1 . 1 . . . . 204 . . . 5785 1 1019 . 1 1 123 123 HIS H H 1 7.18 0.02 . 1 . . . . 205 . . . 5785 1 1020 . 1 1 123 123 HIS HA H 1 5.42 0.02 . 1 . . . . 205 . . . 5785 1 1021 . 1 1 123 123 HIS C C 13 180.17 0.12 . 1 . . . . 205 . . . 5785 1 1022 . 1 1 123 123 HIS CA C 13 58.05 0.12 . 1 . . . . 205 . . . 5785 1 1023 . 1 1 123 123 HIS N N 15 119.42 0.1 . 1 . . . . 205 . . . 5785 1 1024 . 1 1 124 124 SER H H 1 8.32 0.02 . 1 . . . . 206 . . . 5785 1 1025 . 1 1 124 124 SER HA H 1 3.92 0.02 . 1 . . . . 206 . . . 5785 1 1026 . 1 1 124 124 SER C C 13 175.48 0.12 . 1 . . . . 206 . . . 5785 1 1027 . 1 1 124 124 SER CA C 13 62.49 0.12 . 1 . . . . 206 . . . 5785 1 1028 . 1 1 124 124 SER N N 15 122.06 0.1 . 1 . . . . 206 . . . 5785 1 1029 . 1 1 125 125 LEU H H 1 7.33 0.02 . 1 . . . . 207 . . . 5785 1 1030 . 1 1 125 125 LEU HG H 1 1.82 0.02 . 1 . . . . 207 . . . 5785 1 1031 . 1 1 125 125 LEU HD11 H 1 0.64 0.02 . 1 . . . . 207 . . . 5785 1 1032 . 1 1 125 125 LEU HD12 H 1 0.64 0.02 . 1 . . . . 207 . . . 5785 1 1033 . 1 1 125 125 LEU HD13 H 1 0.64 0.02 . 1 . . . . 207 . . . 5785 1 1034 . 1 1 125 125 LEU HD21 H 1 0.19 0.02 . 1 . . . . 207 . . . 5785 1 1035 . 1 1 125 125 LEU HD22 H 1 0.19 0.02 . 1 . . . . 207 . . . 5785 1 1036 . 1 1 125 125 LEU HD23 H 1 0.19 0.02 . 1 . . . . 207 . . . 5785 1 1037 . 1 1 125 125 LEU C C 13 178.14 0.12 . 1 . . . . 207 . . . 5785 1 1038 . 1 1 125 125 LEU CA C 13 54.86 0.02 . 1 . . . . 207 . . . 5785 1 1039 . 1 1 125 125 LEU CG C 13 25.17 0.12 . 1 . . . . 207 . . . 5785 1 1040 . 1 1 125 125 LEU CD1 C 13 21.87 0.12 . 1 . . . . 207 . . . 5785 1 1041 . 1 1 125 125 LEU CD2 C 13 24.94 0.12 . 1 . . . . 207 . . . 5785 1 1042 . 1 1 125 125 LEU N N 15 114.24 0.1 . 1 . . . . 207 . . . 5785 1 1043 . 1 1 126 126 GLY H H 1 8.09 0.02 . 1 . . . . 208 . . . 5785 1 1044 . 1 1 126 126 GLY C C 13 173.78 0.12 . 1 . . . . 208 . . . 5785 1 1045 . 1 1 126 126 GLY CA C 13 44.33 0.02 . 1 . . . . 208 . . . 5785 1 1046 . 1 1 126 126 GLY N N 15 108.27 0.1 . 1 . . . . 208 . . . 5785 1 1047 . 1 1 127 127 LEU H H 1 8.01 0.02 . 1 . . . . 209 . . . 5785 1 1048 . 1 1 127 127 LEU CA C 13 54.7 0.12 . 1 . . . . 209 . . . 5785 1 1049 . 1 1 127 127 LEU N N 15 118.72 0.1 . 1 . . . . 209 . . . 5785 1 1050 . 1 1 128 128 PHE H H 1 8.12 0.02 . 1 . . . . 210 . . . 5785 1 1051 . 1 1 128 128 PHE CA C 13 54.85 0.12 . 1 . . . . 210 . . . 5785 1 1052 . 1 1 128 128 PHE N N 15 119.93 0.1 . 1 . . . . 210 . . . 5785 1 1053 . 1 1 129 129 HIS C C 13 175.5 0.12 . 1 . . . . 211 . . . 5785 1 1054 . 1 1 129 129 HIS CA C 13 55.66 0.12 . 1 . . . . 211 . . . 5785 1 1055 . 1 1 130 130 SER H H 1 6.88 0.02 . 1 . . . . 212 . . . 5785 1 1056 . 1 1 130 130 SER HA H 1 4.08 0.02 . 1 . . . . 212 . . . 5785 1 1057 . 1 1 130 130 SER HB2 H 1 3.60 0.02 . 2 . . . . 212 . . . 5785 1 1058 . 1 1 130 130 SER C C 13 175.18 0.12 . 1 . . . . 212 . . . 5785 1 1059 . 1 1 130 130 SER CA C 13 55.31 0.12 . 1 . . . . 212 . . . 5785 1 1060 . 1 1 130 130 SER CB C 13 64.06 0.12 . 1 . . . . 212 . . . 5785 1 1061 . 1 1 130 130 SER N N 15 114.37 0.1 . 1 . . . . 212 . . . 5785 1 1062 . 1 1 131 131 ALA H H 1 8.76 0.02 . 1 . . . . 213 . . . 5785 1 1063 . 1 1 131 131 ALA HA H 1 4.58 0.02 . 1 . . . . 213 . . . 5785 1 1064 . 1 1 131 131 ALA HB1 H 1 1.36 0.02 . 1 . . . . 213 . . . 5785 1 1065 . 1 1 131 131 ALA HB2 H 1 1.36 0.02 . 1 . . . . 213 . . . 5785 1 1066 . 1 1 131 131 ALA HB3 H 1 1.36 0.02 . 1 . . . . 213 . . . 5785 1 1067 . 1 1 131 131 ALA C C 13 176.77 0.12 . 1 . . . . 213 . . . 5785 1 1068 . 1 1 131 131 ALA CA C 13 52.01 0.12 . 1 . . . . 213 . . . 5785 1 1069 . 1 1 131 131 ALA CB C 13 18.88 0.12 . 1 . . . . 213 . . . 5785 1 1070 . 1 1 131 131 ALA N N 15 128.5 0.1 . 1 . . . . 213 . . . 5785 1 1071 . 1 1 132 132 ASN H H 1 8.65 0.02 . 1 . . . . 214 . . . 5785 1 1072 . 1 1 132 132 ASN HA H 1 4.41 0.02 . 1 . . . . 214 . . . 5785 1 1073 . 1 1 132 132 ASN HB2 H 1 2.71 0.02 . 2 . . . . 214 . . . 5785 1 1074 . 1 1 132 132 ASN C C 13 176.16 0.12 . 1 . . . . 214 . . . 5785 1 1075 . 1 1 132 132 ASN CA C 13 52.40 0.12 . 1 . . . . 214 . . . 5785 1 1076 . 1 1 132 132 ASN CB C 13 37.24 0.12 . 1 . . . . 214 . . . 5785 1 1077 . 1 1 132 132 ASN N N 15 120.75 0.1 . 1 . . . . 214 . . . 5785 1 1078 . 1 1 133 133 THR H H 1 7.84 0.02 . 1 . . . . 215 . . . 5785 1 1079 . 1 1 133 133 THR HA H 1 1.88 0.02 . 1 . . . . 215 . . . 5785 1 1080 . 1 1 133 133 THR HB H 1 3.64 0.02 . 1 . . . . 215 . . . 5785 1 1081 . 1 1 133 133 THR HG21 H 1 0.80 0.02 . 1 . . . . 215 . . . 5785 1 1082 . 1 1 133 133 THR HG22 H 1 0.80 0.02 . 1 . . . . 215 . . . 5785 1 1083 . 1 1 133 133 THR HG23 H 1 0.80 0.02 . 1 . . . . 215 . . . 5785 1 1084 . 1 1 133 133 THR C C 13 175.29 0.12 . 1 . . . . 215 . . . 5785 1 1085 . 1 1 133 133 THR CA C 13 63.42 0.12 . 1 . . . . 215 . . . 5785 1 1086 . 1 1 133 133 THR CB C 13 68.06 0.12 . 1 . . . . 215 . . . 5785 1 1087 . 1 1 133 133 THR CG2 C 13 21.47 0.12 . 1 . . . . 215 . . . 5785 1 1088 . 1 1 133 133 THR N N 15 117.55 0.1 . 1 . . . . 215 . . . 5785 1 1089 . 1 1 134 134 GLU H H 1 7.95 0.02 . 1 . . . . 216 . . . 5785 1 1090 . 1 1 134 134 GLU HA H 1 4.26 0.02 . 1 . . . . 216 . . . 5785 1 1091 . 1 1 134 134 GLU C C 13 176.26 0.12 . 1 . . . . 216 . . . 5785 1 1092 . 1 1 134 134 GLU CA C 13 55.47 0.12 . 1 . . . . 216 . . . 5785 1 1093 . 1 1 134 134 GLU N N 15 118.52 0.1 . 1 . . . . 216 . . . 5785 1 1094 . 1 1 135 135 ALA H H 1 7.66 0.02 . 1 . . . . 217 . . . 5785 1 1095 . 1 1 135 135 ALA HB1 H 1 1.67 0.02 . 1 . . . . 217 . . . 5785 1 1096 . 1 1 135 135 ALA HB2 H 1 1.67 0.02 . 1 . . . . 217 . . . 5785 1 1097 . 1 1 135 135 ALA HB3 H 1 1.67 0.02 . 1 . . . . 217 . . . 5785 1 1098 . 1 1 135 135 ALA C C 13 179.28 0.12 . 1 . . . . 217 . . . 5785 1 1099 . 1 1 135 135 ALA CA C 13 51.49 0.12 . 1 . . . . 217 . . . 5785 1 1100 . 1 1 135 135 ALA CB C 13 19.03 0.12 . 1 . . . . 217 . . . 5785 1 1101 . 1 1 135 135 ALA N N 15 123.79 0.1 . 1 . . . . 217 . . . 5785 1 1102 . 1 1 136 136 LEU HD11 H 1 0.68 0.02 . 1 . . . . 218 . . . 5785 1 1103 . 1 1 136 136 LEU HD12 H 1 0.68 0.02 . 1 . . . . 218 . . . 5785 1 1104 . 1 1 136 136 LEU HD13 H 1 0.68 0.02 . 1 . . . . 218 . . . 5785 1 1105 . 1 1 136 136 LEU HD21 H 1 1.04 0.02 . 1 . . . . 218 . . . 5785 1 1106 . 1 1 136 136 LEU HD22 H 1 1.04 0.02 . 1 . . . . 218 . . . 5785 1 1107 . 1 1 136 136 LEU HD23 H 1 1.04 0.02 . 1 . . . . 218 . . . 5785 1 1108 . 1 1 136 136 LEU CD1 C 13 27.3 0.12 . 1 . . . . 218 . . . 5785 1 1109 . 1 1 136 136 LEU CD2 C 13 22.34 0.12 . 1 . . . . 218 . . . 5785 1 1110 . 1 1 137 137 MET HE1 H 1 0.51 0.02 . 1 . . . . 219 . . . 5785 1 1111 . 1 1 137 137 MET HE2 H 1 0.51 0.02 . 1 . . . . 219 . . . 5785 1 1112 . 1 1 137 137 MET HE3 H 1 0.51 0.02 . 1 . . . . 219 . . . 5785 1 1113 . 1 1 137 137 MET CA C 13 54.03 0.12 . 1 . . . . 219 . . . 5785 1 1114 . 1 1 137 137 MET CE C 13 11.94 0.12 . 1 . . . . 219 . . . 5785 1 1115 . 1 1 138 138 TYR H H 1 8.06 0.02 . 1 . . . . 220 . . . 5785 1 1116 . 1 1 138 138 TYR N N 15 128.62 0.1 . 1 . . . . 220 . . . 5785 1 1117 . 1 1 140 140 LEU H H 1 7.042 0.02 . 1 . . . . 222 . . . 5785 1 1118 . 1 1 140 140 LEU CA C 13 61.36 0.12 . 1 . . . . 222 . . . 5785 1 1119 . 1 1 140 140 LEU N N 15 116.8 0.1 . 1 . . . . 222 . . . 5785 1 1120 . 1 1 141 141 TYR H H 1 8.03 0.02 . 1 . . . . 223 . . . 5785 1 1121 . 1 1 141 141 TYR HB2 H 1 2.76 0.02 . 2 . . . . 223 . . . 5785 1 1122 . 1 1 141 141 TYR CA C 13 55.37 0.12 . 1 . . . . 223 . . . 5785 1 1123 . 1 1 141 141 TYR CB C 13 39.58 0.12 . 1 . . . . 223 . . . 5785 1 1124 . 1 1 141 141 TYR N N 15 122.81 0.1 . 1 . . . . 223 . . . 5785 1 1125 . 1 1 142 142 HIS C C 13 176.42 0.12 . 1 . . . . 224 . . . 5785 1 1126 . 1 1 143 143 SER H H 1 8.65 0.02 . 1 . . . . 225 . . . 5785 1 1127 . 1 1 143 143 SER HA H 1 4.11 0.02 . 1 . . . . 225 . . . 5785 1 1128 . 1 1 143 143 SER HB2 H 1 3.81 0.02 . 2 . . . . 225 . . . 5785 1 1129 . 1 1 143 143 SER C C 13 174.33 0.12 . 1 . . . . 225 . . . 5785 1 1130 . 1 1 143 143 SER CA C 13 58.53 0.02 . 1 . . . . 225 . . . 5785 1 1131 . 1 1 143 143 SER CB C 13 63.21 0.12 . 1 . . . . 225 . . . 5785 1 1132 . 1 1 143 143 SER N N 15 118.56 0.1 . 1 . . . . 225 . . . 5785 1 1133 . 1 1 144 144 LEU H H 1 7.53 0.02 . 1 . . . . 226 . . . 5785 1 1134 . 1 1 144 144 LEU HG H 1 1.50 0.02 . 1 . . . . 226 . . . 5785 1 1135 . 1 1 144 144 LEU HD11 H 1 0.82 0.02 . 1 . . . . 226 . . . 5785 1 1136 . 1 1 144 144 LEU HD12 H 1 0.82 0.02 . 1 . . . . 226 . . . 5785 1 1137 . 1 1 144 144 LEU HD13 H 1 0.82 0.02 . 1 . . . . 226 . . . 5785 1 1138 . 1 1 144 144 LEU HD21 H 1 0.89 0.02 . 1 . . . . 226 . . . 5785 1 1139 . 1 1 144 144 LEU HD22 H 1 0.89 0.02 . 1 . . . . 226 . . . 5785 1 1140 . 1 1 144 144 LEU HD23 H 1 0.89 0.02 . 1 . . . . 226 . . . 5785 1 1141 . 1 1 144 144 LEU CA C 13 54.3 0.12 . 1 . . . . 226 . . . 5785 1 1142 . 1 1 144 144 LEU CG C 13 26.83 0.12 . 1 . . . . 226 . . . 5785 1 1143 . 1 1 144 144 LEU CD1 C 13 23.52 0.12 . 1 . . . . 226 . . . 5785 1 1144 . 1 1 144 144 LEU CD2 C 13 25.02 0.12 . 1 . . . . 226 . . . 5785 1 1145 . 1 1 144 144 LEU N N 15 122.84 0.1 . 1 . . . . 226 . . . 5785 1 1146 . 1 1 145 145 THR HA H 1 4.09 0.02 . 1 . . . . 227 . . . 5785 1 1147 . 1 1 145 145 THR C C 13 173.66 0.12 . 1 . . . . 227 . . . 5785 1 1148 . 1 1 146 146 ASP HA H 1 4.69 0.02 . 1 . . . . 228 . . . 5785 1 1149 . 1 1 146 146 ASP HB2 H 1 2.75 0.02 . 2 . . . . 228 . . . 5785 1 1150 . 1 1 146 146 ASP HB3 H 1 2.63 0.02 . 2 . . . . 228 . . . 5785 1 1151 . 1 1 146 146 ASP C C 13 176.95 0.12 . 1 . . . . 228 . . . 5785 1 1152 . 1 1 146 146 ASP CA C 13 52.62 0.12 . 1 . . . . 228 . . . 5785 1 1153 . 1 1 146 146 ASP CB C 13 38.88 0.12 . 1 . . . . 228 . . . 5785 1 1154 . 1 1 147 147 LEU H H 1 8.82 0.02 . 1 . . . . 229 . . . 5785 1 1155 . 1 1 147 147 LEU HA H 1 3.99 0.02 . 1 . . . . 229 . . . 5785 1 1156 . 1 1 147 147 LEU HB2 H 1 1.64 0.02 . 2 . . . . 229 . . . 5785 1 1157 . 1 1 147 147 LEU HB3 H 1 1.53 0.02 . 2 . . . . 229 . . . 5785 1 1158 . 1 1 147 147 LEU HG H 1 1.65 0.02 . 1 . . . . 229 . . . 5785 1 1159 . 1 1 147 147 LEU HD11 H 1 0.83 0.02 . 1 . . . . 229 . . . 5785 1 1160 . 1 1 147 147 LEU HD12 H 1 0.83 0.02 . 1 . . . . 229 . . . 5785 1 1161 . 1 1 147 147 LEU HD13 H 1 0.83 0.02 . 1 . . . . 229 . . . 5785 1 1162 . 1 1 147 147 LEU HD21 H 1 0.90 0.02 . 1 . . . . 229 . . . 5785 1 1163 . 1 1 147 147 LEU HD22 H 1 0.90 0.02 . 1 . . . . 229 . . . 5785 1 1164 . 1 1 147 147 LEU HD23 H 1 0.90 0.02 . 1 . . . . 229 . . . 5785 1 1165 . 1 1 147 147 LEU C C 13 178.85 0.12 . 1 . . . . 229 . . . 5785 1 1166 . 1 1 147 147 LEU CB C 13 41.7 0.12 . 1 . . . . 229 . . . 5785 1 1167 . 1 1 147 147 LEU CG C 13 26.83 0.12 . 1 . . . . 229 . . . 5785 1 1168 . 1 1 147 147 LEU CD1 C 13 23.28 0.12 . 1 . . . . 229 . . . 5785 1 1169 . 1 1 147 147 LEU CD2 C 13 24.94 0.12 . 1 . . . . 229 . . . 5785 1 1170 . 1 1 147 147 LEU N N 15 126.16 0.1 . 1 . . . . 229 . . . 5785 1 1171 . 1 1 148 148 THR H H 1 8.40 0.02 . 1 . . . . 230 . . . 5785 1 1172 . 1 1 148 148 THR HA H 1 4.05 0.02 . 1 . . . . 230 . . . 5785 1 1173 . 1 1 148 148 THR HB H 1 4.18 0.02 . 1 . . . . 230 . . . 5785 1 1174 . 1 1 148 148 THR HG21 H 1 1.19 0.02 . 1 . . . . 230 . . . 5785 1 1175 . 1 1 148 148 THR HG22 H 1 1.19 0.02 . 1 . . . . 230 . . . 5785 1 1176 . 1 1 148 148 THR HG23 H 1 1.19 0.02 . 1 . . . . 230 . . . 5785 1 1177 . 1 1 148 148 THR C C 13 175.91 0.12 . 1 . . . . 230 . . . 5785 1 1178 . 1 1 148 148 THR CA C 13 64.36 0.12 . 1 . . . . 230 . . . 5785 1 1179 . 1 1 148 148 THR CB C 13 68.61 0.12 . 1 . . . . 230 . . . 5785 1 1180 . 1 1 148 148 THR CG2 C 13 21.7 0.12 . 1 . . . . 230 . . . 5785 1 1181 . 1 1 148 148 THR N N 15 111.76 0.1 . 1 . . . . 230 . . . 5785 1 1182 . 1 1 149 149 ARG H H 1 7.40 0.02 . 1 . . . . 231 . . . 5785 1 1183 . 1 1 149 149 ARG HA H 1 4.22 0.02 . 1 . . . . 231 . . . 5785 1 1184 . 1 1 149 149 ARG HB2 H 1 1.96 0.02 . 2 . . . . 231 . . . 5785 1 1185 . 1 1 149 149 ARG HB3 H 1 1.59 0.02 . 2 . . . . 231 . . . 5785 1 1186 . 1 1 149 149 ARG HG2 H 1 1.53 0.02 . 2 . . . . 231 . . . 5785 1 1187 . 1 1 149 149 ARG HD2 H 1 3.06 0.02 . 2 . . . . 231 . . . 5785 1 1188 . 1 1 149 149 ARG C C 13 175.89 0.12 . 1 . . . . 231 . . . 5785 1 1189 . 1 1 149 149 ARG CA C 13 54.78 0.12 . 1 . . . . 231 . . . 5785 1 1190 . 1 1 149 149 ARG CB C 13 30.13 0.12 . 1 . . . . 231 . . . 5785 1 1191 . 1 1 149 149 ARG CG C 13 27.06 0.12 . 1 . . . . 231 . . . 5785 1 1192 . 1 1 149 149 ARG CD C 13 42.89 0.12 . 1 . . . . 231 . . . 5785 1 1193 . 1 1 149 149 ARG N N 15 119.64 0.1 . 1 . . . . 231 . . . 5785 1 1194 . 1 1 150 150 PHE H H 1 7.26 0.02 . 1 . . . . 232 . . . 5785 1 1195 . 1 1 150 150 PHE HA H 1 4.19 0.02 . 1 . . . . 232 . . . 5785 1 1196 . 1 1 150 150 PHE HB2 H 1 3.03 0.02 . 2 . . . . 232 . . . 5785 1 1197 . 1 1 150 150 PHE HB3 H 1 2.79 0.02 . 9 . . . . 232 . . . 5785 1 1198 . 1 1 150 150 PHE C C 13 175.00 0.12 . 1 . . . . 232 . . . 5785 1 1199 . 1 1 150 150 PHE CA C 13 59.96 0.12 . 1 . . . . 232 . . . 5785 1 1200 . 1 1 150 150 PHE N N 15 121.28 0.1 . 1 . . . . 232 . . . 5785 1 1201 . 1 1 151 151 ARG H H 1 7.04 0.02 . 1 . . . . 233 . . . 5785 1 1202 . 1 1 151 151 ARG HB2 H 1 1.37 0.02 . 2 . . . . 233 . . . 5785 1 1203 . 1 1 151 151 ARG HB3 H 1 1.58 0.02 . 2 . . . . 233 . . . 5785 1 1204 . 1 1 151 151 ARG HG2 H 1 1.27 0.02 . 2 . . . . 233 . . . 5785 1 1205 . 1 1 151 151 ARG HD2 H 1 3.01 0.02 . 2 . . . . 233 . . . 5785 1 1206 . 1 1 151 151 ARG HD3 H 1 2.97 0.02 . 2 . . . . 233 . . . 5785 1 1207 . 1 1 151 151 ARG C C 13 174.56 0.12 . 1 . . . . 233 . . . 5785 1 1208 . 1 1 151 151 ARG CA C 13 54.3 0.12 . 1 . . . . 233 . . . 5785 1 1209 . 1 1 151 151 ARG CB C 13 32.5 0.12 . 1 . . . . 233 . . . 5785 1 1210 . 1 1 151 151 ARG CG C 13 25.41 0.12 . 1 . . . . 233 . . . 5785 1 1211 . 1 1 151 151 ARG CD C 13 43.13 0.12 . 1 . . . . 233 . . . 5785 1 1212 . 1 1 151 151 ARG N N 15 126.73 0.1 . 1 . . . . 233 . . . 5785 1 1213 . 1 1 152 152 LEU H H 1 8.18 0.02 . 1 . . . . 234 . . . 5785 1 1214 . 1 1 152 152 LEU CA C 13 54.86 0.12 . 1 . . . . 234 . . . 5785 1 1215 . 1 1 152 152 LEU N N 15 122.83 0.1 . 1 . . . . 234 . . . 5785 1 1216 . 1 1 153 153 SER HA H 1 4.34 0.02 . 1 . . . . 235 . . . 5785 1 1217 . 1 1 153 153 SER HB2 H 1 3.77 0.02 . 2 . . . . 235 . . . 5785 1 1218 . 1 1 153 153 SER C C 13 175.11 0.12 . 1 . . . . 235 . . . 5785 1 1219 . 1 1 153 153 SER CB C 13 63.91 0.12 . 1 . . . . 235 . . . 5785 1 1220 . 1 1 154 154 GLN HA H 1 3.76 0.02 . 1 . . . . 236 . . . 5785 1 1221 . 1 1 154 154 GLN HB2 H 1 1.97 0.02 . 2 . . . . 236 . . . 5785 1 1222 . 1 1 154 154 GLN HB3 H 1 2.07 0.02 . 2 . . . . 236 . . . 5785 1 1223 . 1 1 154 154 GLN HG2 H 1 2.35 0.02 . 2 . . . . 236 . . . 5785 1 1224 . 1 1 154 154 GLN C C 13 177.78 0.12 . 1 . . . . 236 . . . 5785 1 1225 . 1 1 154 154 GLN CB C 13 27.53 0.02 . 1 . . . . 236 . . . 5785 1 1226 . 1 1 154 154 GLN CG C 13 33.34 0.02 . 1 . . . . 236 . . . 5785 1 1227 . 1 1 155 155 ASP H H 1 8.03 0.02 . 1 . . . . 237 . . . 5785 1 1228 . 1 1 155 155 ASP HA H 1 4.39 0.02 . 1 . . . . 237 . . . 5785 1 1229 . 1 1 155 155 ASP HB2 H 1 2.69 0.02 . 2 . . . . 237 . . . 5785 1 1230 . 1 1 155 155 ASP HB3 H 1 2.41 0.02 . 2 . . . . 237 . . . 5785 1 1231 . 1 1 155 155 ASP CB C 13 40.53 0.12 . 1 . . . . 237 . . . 5785 1 1232 . 1 1 155 155 ASP N N 15 117.85 0.1 . 1 . . . . 237 . . . 5785 1 1233 . 1 1 156 156 ASP H H 1 7.46 0.02 . 1 . . . . 238 . . . 5785 1 1234 . 1 1 156 156 ASP HA H 1 4.53 0.02 . 1 . . . . 238 . . . 5785 1 1235 . 1 1 156 156 ASP C C 13 178.14 0.12 . 1 . . . . 238 . . . 5785 1 1236 . 1 1 156 156 ASP CA C 13 57.86 0.12 . 1 . . . . 238 . . . 5785 1 1237 . 1 1 156 156 ASP N N 15 120.55 0.1 . 1 . . . . 238 . . . 5785 1 1238 . 1 1 157 157 ILE H H 1 7.87 0.02 . 1 . . . . 239 . . . 5785 1 1239 . 1 1 157 157 ILE HB H 1 1.72 0.02 . 1 . . . . 239 . . . 5785 1 1240 . 1 1 157 157 ILE HG12 H 1 0.98 0.02 . 9 . . . . 239 . . . 5785 1 1241 . 1 1 157 157 ILE HG21 H 1 0.73 0.02 . 1 . . . . 239 . . . 5785 1 1242 . 1 1 157 157 ILE HG22 H 1 0.73 0.02 . 1 . . . . 239 . . . 5785 1 1243 . 1 1 157 157 ILE HG23 H 1 0.73 0.02 . 1 . . . . 239 . . . 5785 1 1244 . 1 1 157 157 ILE HD11 H 1 0.65 0.02 . 1 . . . . 239 . . . 5785 1 1245 . 1 1 157 157 ILE HD12 H 1 0.65 0.02 . 1 . . . . 239 . . . 5785 1 1246 . 1 1 157 157 ILE HD13 H 1 0.65 0.02 . 1 . . . . 239 . . . 5785 1 1247 . 1 1 157 157 ILE C C 13 177.62 0.12 . 1 . . . . 239 . . . 5785 1 1248 . 1 1 157 157 ILE CA C 13 65.8 0.12 . 1 . . . . 239 . . . 5785 1 1249 . 1 1 157 157 ILE CB C 13 38.17 0.12 . 1 . . . . 239 . . . 5785 1 1250 . 1 1 157 157 ILE CG1 C 13 25.88 0.12 . 1 . . . . 239 . . . 5785 1 1251 . 1 1 157 157 ILE CG2 C 13 17.38 0.12 . 1 . . . . 239 . . . 5785 1 1252 . 1 1 157 157 ILE CD1 C 13 13.12 0.12 . 1 . . . . 239 . . . 5785 1 1253 . 1 1 157 157 ILE N N 15 119.89 0.1 . 1 . . . . 239 . . . 5785 1 1254 . 1 1 158 158 ASN H H 1 9.01 0.02 . 1 . . . . 240 . . . 5785 1 1255 . 1 1 158 158 ASN HA H 1 4.15 0.02 . 1 . . . . 240 . . . 5785 1 1256 . 1 1 158 158 ASN HB2 H 1 2.73 0.02 . 2 . . . . 240 . . . 5785 1 1257 . 1 1 158 158 ASN HB3 H 1 2.96 0.02 . 2 . . . . 240 . . . 5785 1 1258 . 1 1 158 158 ASN C C 13 179.54 0.12 . 1 . . . . 240 . . . 5785 1 1259 . 1 1 158 158 ASN CA C 13 55.64 0.12 . 1 . . . . 240 . . . 5785 1 1260 . 1 1 158 158 ASN CB C 13 37.00 0.2 . 1 . . . . 240 . . . 5785 1 1261 . 1 1 158 158 ASN N N 15 118.7 0.1 . 1 . . . . 240 . . . 5785 1 1262 . 1 1 159 159 GLY H H 1 8.16 0.02 . 1 . . . . 241 . . . 5785 1 1263 . 1 1 159 159 GLY C C 13 176.82 0.12 . 1 . . . . 241 . . . 5785 1 1264 . 1 1 159 159 GLY CA C 13 47.29 0.12 . 1 . . . . 241 . . . 5785 1 1265 . 1 1 159 159 GLY N N 15 108.52 0.1 . 1 . . . . 241 . . . 5785 1 1266 . 1 1 160 160 ILE H H 1 8.42 0.02 . 1 . . . . 242 . . . 5785 1 1267 . 1 1 160 160 ILE HA H 1 4.16 0.02 . 1 . . . . 242 . . . 5785 1 1268 . 1 1 160 160 ILE HB H 1 2.04 0.02 . 1 . . . . 242 . . . 5785 1 1269 . 1 1 160 160 ILE HG12 H 1 1.75 0.02 . 2 . . . . 242 . . . 5785 1 1270 . 1 1 160 160 ILE HG21 H 1 1.49 0.02 . 1 . . . . 242 . . . 5785 1 1271 . 1 1 160 160 ILE HG22 H 1 1.49 0.02 . 1 . . . . 242 . . . 5785 1 1272 . 1 1 160 160 ILE HG23 H 1 1.49 0.02 . 1 . . . . 242 . . . 5785 1 1273 . 1 1 160 160 ILE HD11 H 1 0.76 0.02 . 1 . . . . 242 . . . 5785 1 1274 . 1 1 160 160 ILE HD12 H 1 0.76 0.02 . 1 . . . . 242 . . . 5785 1 1275 . 1 1 160 160 ILE HD13 H 1 0.76 0.02 . 1 . . . . 242 . . . 5785 1 1276 . 1 1 160 160 ILE C C 13 178.28 0.12 . 1 . . . . 242 . . . 5785 1 1277 . 1 1 160 160 ILE CA C 13 61.11 0.12 . 1 . . . . 242 . . . 5785 1 1278 . 1 1 160 160 ILE CB C 13 35.09 0.12 . 9 . . . . 242 . . . 5785 1 1279 . 1 1 160 160 ILE CG1 C 13 30.84 0.12 . 1 . . . . 242 . . . 5785 1 1280 . 1 1 160 160 ILE CG2 C 13 20.21 0.12 . 1 . . . . 242 . . . 5785 1 1281 . 1 1 160 160 ILE CD1 C 13 14.78 0.12 . 1 . . . . 242 . . . 5785 1 1282 . 1 1 160 160 ILE N N 15 123.7 0.1 . 1 . . . . 242 . . . 5785 1 1283 . 1 1 161 161 GLN H H 1 8.75 0.02 . 1 . . . . 243 . . . 5785 1 1284 . 1 1 161 161 GLN HA H 1 4.07 0.02 . 1 . . . . 243 . . . 5785 1 1285 . 1 1 161 161 GLN C C 13 180.15 0.12 . 1 . . . . 243 . . . 5785 1 1286 . 1 1 161 161 GLN CA C 13 58.43 0.12 . 1 . . . . 243 . . . 5785 1 1287 . 1 1 161 161 GLN N N 15 123.86 0.1 . 1 . . . . 243 . . . 5785 1 1288 . 1 1 162 162 SER H H 1 8.02 0.02 . 1 . . . . 244 . . . 5785 1 1289 . 1 1 162 162 SER HA H 1 4.08 0.02 . 1 . . . . 244 . . . 5785 1 1290 . 1 1 162 162 SER C C 13 175.08 0.12 . 1 . . . . 244 . . . 5785 1 1291 . 1 1 162 162 SER CA C 13 61.64 0.12 . 1 . . . . 244 . . . 5785 1 1292 . 1 1 162 162 SER N N 15 117.97 0.1 . 1 . . . . 244 . . . 5785 1 1293 . 1 1 163 163 LEU H H 1 6.66 0.02 . 1 . . . . 245 . . . 5785 1 1294 . 1 1 163 163 LEU HA H 1 3.94 0.02 . 1 . . . . 245 . . . 5785 1 1295 . 1 1 163 163 LEU C C 13 177.72 0.12 . 1 . . . . 245 . . . 5785 1 1296 . 1 1 163 163 LEU CA C 13 56.58 0.12 . 1 . . . . 245 . . . 5785 1 1297 . 1 1 163 163 LEU N N 15 118.45 0.1 . 1 . . . . 245 . . . 5785 1 1298 . 1 1 164 164 TYR H H 1 7.50 0.02 . 1 . . . . 246 . . . 5785 1 1299 . 1 1 164 164 TYR HA H 1 4.66 0.02 . 1 . . . . 246 . . . 5785 1 1300 . 1 1 164 164 TYR C C 13 175.65 0.12 . 1 . . . . 246 . . . 5785 1 1301 . 1 1 164 164 TYR CA C 13 58.95 0.12 . 1 . . . . 246 . . . 5785 1 1302 . 1 1 164 164 TYR N N 15 112.93 0.1 . 1 . . . . 246 . . . 5785 1 1303 . 1 1 165 165 GLY H H 1 8.29 0.02 . 1 . . . . 247 . . . 5785 1 1304 . 1 1 165 165 GLY CA C 13 43.93 0.12 . 1 . . . . 247 . . . 5785 1 1305 . 1 1 165 165 GLY N N 15 109.61 0.1 . 1 . . . . 247 . . . 5785 1 1306 . 1 1 166 166 PRO HB2 H 1 2.19 0.02 . 2 . . . . 248 . . . 5785 1 1307 . 1 1 166 166 PRO HB3 H 1 1.98 0.02 . 2 . . . . 248 . . . 5785 1 1308 . 1 1 166 166 PRO CB C 13 33.47 0.12 . 1 . . . . 248 . . . 5785 1 1309 . 1 1 168 168 PRO HA H 1 4.29 0.02 . 1 . . . . 250 . . . 5785 1 1310 . 1 1 168 168 PRO HB2 H 1 1.85 0.02 . 1 . . . . 250 . . . 5785 1 1311 . 1 1 168 168 PRO HB3 H 1 2.11 0.02 . 1 . . . . 250 . . . 5785 1 1312 . 1 1 168 168 PRO HG2 H 1 1.85 0.02 . 2 . . . . 250 . . . 5785 1 1313 . 1 1 168 168 PRO HD2 H 1 3.44 0.02 . 2 . . . . 250 . . . 5785 1 1314 . 1 1 168 168 PRO HD3 H 1 3.63 0.02 . 2 . . . . 250 . . . 5785 1 1315 . 1 1 168 168 PRO C C 13 176.6 0.12 . 1 . . . . 250 . . . 5785 1 1316 . 1 1 168 168 PRO CB C 13 31.59 0.12 . 1 . . . . 250 . . . 5785 1 1317 . 1 1 168 168 PRO CG C 13 26.83 0.12 . 1 . . . . 250 . . . 5785 1 1318 . 1 1 168 168 PRO CD C 13 50.21 0.12 . 1 . . . . 250 . . . 5785 1 1319 . 1 1 169 169 ASP H H 1 8.22 0.02 . 1 . . . . 251 . . . 5785 1 1320 . 1 1 169 169 ASP HA H 1 4.43 0.02 . 1 . . . . 251 . . . 5785 1 1321 . 1 1 169 169 ASP HB2 H 1 2.55 0.02 . 2 . . . . 251 . . . 5785 1 1322 . 1 1 169 169 ASP HB3 H 1 2.49 0.02 . 2 . . . . 251 . . . 5785 1 1323 . 1 1 169 169 ASP C C 13 176.05 0.12 . 1 . . . . 251 . . . 5785 1 1324 . 1 1 169 169 ASP CA C 13 54.07 0.12 . 1 . . . . 251 . . . 5785 1 1325 . 1 1 169 169 ASP CB C 13 41.00 0.12 . 1 . . . . 251 . . . 5785 1 1326 . 1 1 169 169 ASP N N 15 120.62 0.1 . 1 . . . . 251 . . . 5785 1 1327 . 1 1 170 170 SER H H 1 8.04 0.02 . 1 . . . . 252 . . . 5785 1 1328 . 1 1 170 170 SER HA H 1 4.64 0.02 . 1 . . . . 252 . . . 5785 1 1329 . 1 1 170 170 SER HB2 H 1 3.69 0.02 . 2 . . . . 252 . . . 5785 1 1330 . 1 1 170 170 SER HB3 H 1 3.74 0.02 . 2 . . . . 252 . . . 5785 1 1331 . 1 1 170 170 SER C C 13 172.79 0.12 . 1 . . . . 252 . . . 5785 1 1332 . 1 1 170 170 SER CA C 13 56.07 0.12 . 1 . . . . 252 . . . 5785 1 1333 . 1 1 170 170 SER CB C 13 63.35 0.12 . 1 . . . . 252 . . . 5785 1 1334 . 1 1 170 170 SER N N 15 117.28 0.1 . 1 . . . . 252 . . . 5785 1 1335 . 1 1 171 171 PRO HA H 1 4.34 0.02 . 1 . . . . 253 . . . 5785 1 1336 . 1 1 171 171 PRO HB2 H 1 2.15 0.02 . 2 . . . . 253 . . . 5785 1 1337 . 1 1 171 171 PRO HB3 H 1 1.82 0.02 . 2 . . . . 253 . . . 5785 1 1338 . 1 1 171 171 PRO HG2 H 1 1.89 0.02 . 2 . . . . 253 . . . 5785 1 1339 . 1 1 171 171 PRO HD2 H 1 3.67 0.02 . 2 . . . . 253 . . . 5785 1 1340 . 1 1 171 171 PRO C C 13 176.93 0.12 . 1 . . . . 253 . . . 5785 1 1341 . 1 1 171 171 PRO CB C 13 31.59 0.02 . 1 . . . . 253 . . . 5785 1 1342 . 1 1 171 171 PRO CG C 13 26.83 0.02 . 1 . . . . 253 . . . 5785 1 1343 . 1 1 171 171 PRO CD C 13 50.45 0.12 . 1 . . . . 253 . . . 5785 1 1344 . 1 1 172 172 GLU H H 1 8.34 0.02 . 1 . . . . 254 . . . 5785 1 1345 . 1 1 172 172 GLU HA H 1 4.20 0.02 . 1 . . . . 254 . . . 5785 1 1346 . 1 1 172 172 GLU HB2 H 1 1.97 0.02 . 2 . . . . 254 . . . 5785 1 1347 . 1 1 172 172 GLU HB3 H 1 1.82 0.02 . 2 . . . . 254 . . . 5785 1 1348 . 1 1 172 172 GLU HG2 H 1 2.18 0.02 . 2 . . . . 254 . . . 5785 1 1349 . 1 1 172 172 GLU C C 13 176.09 0.12 . 1 . . . . 254 . . . 5785 1 1350 . 1 1 172 172 GLU CA C 13 56.59 0.12 . 1 . . . . 254 . . . 5785 1 1351 . 1 1 172 172 GLU CB C 13 29.94 0.12 . 1 . . . . 254 . . . 5785 1 1352 . 1 1 172 172 GLU CG C 13 36.04 0.12 . 1 . . . . 254 . . . 5785 1 1353 . 1 1 172 172 GLU N N 15 121.71 0.1 . 1 . . . . 254 . . . 5785 1 1354 . 1 1 173 173 THR H H 1 7.63 0.02 . 1 . . . . 255 . . . 5785 1 1355 . 1 1 173 173 THR HB H 1 4.12 0.02 . 1 . . . . 255 . . . 5785 1 1356 . 1 1 173 173 THR HG21 H 1 1.04 0.02 . 1 . . . . 255 . . . 5785 1 1357 . 1 1 173 173 THR HG22 H 1 1.04 0.02 . 1 . . . . 255 . . . 5785 1 1358 . 1 1 173 173 THR HG23 H 1 1.04 0.02 . 1 . . . . 255 . . . 5785 1 1359 . 1 1 173 173 THR CA C 13 62.88 0.12 . 1 . . . . 255 . . . 5785 1 1360 . 1 1 173 173 THR CB C 13 70.53 0.12 . 1 . . . . 255 . . . 5785 1 1361 . 1 1 173 173 THR CG2 C 13 21.63 0.12 . 1 . . . . 255 . . . 5785 1 1362 . 1 1 173 173 THR N N 15 120.53 0.1 . 1 . . . . 255 . . . 5785 1 stop_ save_