data_5186 ####################### # Entry information # ####################### save_entry_information _Entry.Sf_category entry_information _Entry.Sf_framecode entry_information _Entry.ID 5186 _Entry.Title ; 1H, 13C, and 15N backbone assignment of the vascular endothelial growth factor receptor-binding domain ; _Entry.Type . _Entry.Version_type original _Entry.Submission_date 2001-10-19 _Entry.Accession_date 2001-10-22 _Entry.Last_release_date 2002-05-07 _Entry.Original_release_date 2002-05-07 _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 Borlan Pan . . . 5186 2 Wayne Fairbrother . J. . 5186 stop_ loop_ _Data_set.Type _Data_set.Count _Data_set.Entry_ID assigned_chemical_shifts 1 5186 stop_ loop_ _Datum.Type _Datum.Count _Datum.Entry_ID '1H chemical shifts' 184 5186 '13C chemical shifts' 260 5186 '15N chemical shifts' 85 5186 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 . . 2002-05-07 2001-10-19 original author . 5186 stop_ loop_ _Related_entries.Database_name _Related_entries.Database_accession_code _Related_entries.Relationship _Related_entries.Entry_ID BMRB 5185 'Assignments for vascular endothelial growth factor in complex with v107' 5186 BMRB 5198 'Assignments for v107 in complex with vascular endothelial growth factor' 5186 stop_ save_ ############### # Citations # ############### save_entry_citation _Citation.Sf_category citations _Citation.Sf_framecode entry_citation _Citation.Entry_ID 5186 _Citation.ID 1 _Citation.Class 'entry citation' _Citation.CAS_abstract_code . _Citation.MEDLINE_UI_code 21880667 _Citation.DOI . _Citation.PubMed_ID 11883783 _Citation.Full_citation . _Citation.Title ; 1H, 13C, and 15N Resonance Assignment of the Vascular Endothelial Growth Factor Receptor-binding Domain in Complex with a Receptor-blocking Peptide ; _Citation.Status published _Citation.Type journal _Citation.Journal_abbrev 'J. Biomol. NMR' _Citation.Journal_name_full . _Citation.Journal_volume 22 _Citation.Journal_issue 2 _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 189 _Citation.Page_last 190 _Citation.Year 2002 _Citation.Details . loop_ _Citation_author.Ordinal _Citation_author.Given_name _Citation_author.Family_name _Citation_author.First_initial _Citation_author.Middle_initials _Citation_author.Family_title _Citation_author.Entry_ID _Citation_author.Citation_ID 1 Borlan Pan . . . 5186 1 2 Wayne Fairbrother . J. . 5186 1 stop_ loop_ _Citation_keyword.Keyword _Citation_keyword.Entry_ID _Citation_keyword.Citation_ID 'vascular endothelial growth factor' 5186 1 stop_ save_ save_ref_1 _Citation.Sf_category citations _Citation.Sf_framecode ref_1 _Citation.Entry_ID 5186 _Citation.ID 2 _Citation.Class 'reference citation' _Citation.CAS_abstract_code . _Citation.MEDLINE_UI_code . _Citation.DOI . _Citation.PubMed_ID 9336848 _Citation.Full_citation ; Fairbrother WJ, Champe MA, Christinger HW, Keyt BA, Starovasnik MA. 1H, 13C, and 15N backbone assignment and secondary structure of the receptor-binding domain of vascular endothelial growth factor. Protein Sci. 1997 Oct;6(10):2250-60. ; _Citation.Title '1H, 13C, and 15N backbone assignment and secondary structure of the receptor-binding domain of vascular endothelial growth factor.' _Citation.Status published _Citation.Type journal _Citation.Journal_abbrev 'Protein Sci.' _Citation.Journal_name_full 'Protein science : a publication of the Protein Society' _Citation.Journal_volume 6 _Citation.Journal_issue 10 _Citation.Journal_ASTM . _Citation.Journal_ISSN 0961-8368 _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 2250 _Citation.Page_last 2260 _Citation.Year 1997 _Citation.Details ; Nearly complete sequence-specific 1H, 13C, and 15N resonance assignments are reported for the backbone atoms of the receptor-binding domain of vascular endothelial growth factor (VEGF), a 23-kDa homodimeric protein that is a major regulator of both normal and pathological angiogenesis. The assignment strategy relied on the use of seven 3D triple-resonance experiments [HN(CO)CA, HNCA, HNCO, (HCA)CONH, HN(COCA)HA, HN(CA)HA, and CBCA-(CO)NH] and a 3D 15N-TOCSY-HSQC experiment recorded on a 0.5 mM (12 mg/mL) sample at 500 MHz, pH 7.0, 45 degrees C. Under these conditions, 15N relaxation data show that the protein has a rotational correlation time of 15.0 ns. Despite this unusually long correlation time, assignments were obtained for 94 of the 99 residues; 8 residues lack amide 1H and 15N assignments, presumably due to rapid exchange of the amide 1H with solvent under the experimental conditions used. The secondary structure of the protein was deduced from the chemical shift indices of the 1H alpha, 13C alpha, 13C beta, and 13CO nuclei, and from analysis of backbone NOEs observed in a 3D 15N-NOESY-HSQC spectrum. Two helices and a significant amount of beta-sheet structure were identified, in general agreement with the secondary structure found in a recently determined crystal structure of a similar VEGF construct [Muller YA et al., 1997, Proc Natl Acad Sci USA 94:7192-7197]. ; 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 'W J' Fairbrother W. J. . 5186 2 2 'M A' Champe M. A. . 5186 2 3 'H W' Christinger H. W. . 5186 2 4 'B A' Keyt B. A. . 5186 2 5 'M A' Starovasnik M. A. . 5186 2 stop_ save_ ############################################# # Molecular system (assembly) description # ############################################# save_system_VEGF _Assembly.Sf_category assembly _Assembly.Sf_framecode system_VEGF _Assembly.Entry_ID 5186 _Assembly.ID 1 _Assembly.Name 'vascular endothelial growth factor receptor-binding domain dimer' _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 23250.8 _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 dimer 5186 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 'VEGF subunit 1' 1 $VEGF . . . native . . 1 . . 5186 1 2 'VEGF subunit 2' 1 $VEGF . . . native . . 1 . . 5186 1 stop_ loop_ _Bond.ID _Bond.Type _Bond.Value_order _Bond.Assembly_atom_ID_1 _Bond.Entity_assembly_ID_1 _Bond.Entity_assembly_name_1 _Bond.Entity_ID_1 _Bond.Comp_ID_1 _Bond.Comp_index_ID_1 _Bond.Seq_ID_1 _Bond.Atom_ID_1 _Bond.Assembly_atom_ID_2 _Bond.Entity_assembly_ID_2 _Bond.Entity_assembly_name_2 _Bond.Entity_ID_2 _Bond.Comp_ID_2 _Bond.Comp_index_ID_2 _Bond.Seq_ID_2 _Bond.Atom_ID_2 _Bond.Auth_entity_assembly_ID_1 _Bond.Auth_entity_assembly_name_1 _Bond.Auth_seq_ID_1 _Bond.Auth_comp_ID_1 _Bond.Auth_atom_ID_1 _Bond.Auth_entity_assembly_ID_2 _Bond.Auth_entity_assembly_name_2 _Bond.Auth_seq_ID_2 _Bond.Auth_comp_ID_2 _Bond.Auth_atom_ID_2 _Bond.Entry_ID _Bond.Assembly_ID 1 disulfide single . 1 . . CYS 16 16 SG . 1 . 1 CYS 58 58 SG . . . . . . . . . . 5186 1 2 disulfide single . 1 . . CYS 47 47 SG . 1 . 1 CYS 92 92 SG . . . . . . . . . . 5186 1 3 disulfide single . 1 . . CYS 51 51 SG . 1 . 1 CYS 94 94 SG . . . . . . . . . . 5186 1 4 disulfide single . 1 . . CYS 41 41 SG . 2 . 1 CYS 50 50 SG . . . . . . . . . . 5186 1 5 disulfide single . 2 . . CYS 16 16 SG . 2 . 1 CYS 58 58 SG . . . . . . . . . . 5186 1 6 disulfide single . 2 . . CYS 47 47 SG . 2 . 1 CYS 92 92 SG . . . . . . . . . . 5186 1 7 disulfide single . 2 . . CYS 51 51 SG . 2 . 1 CYS 94 94 SG . . . . . . . . . . 5186 1 8 disulfide single . 2 . . CYS 41 41 SG . 1 . 1 CYS 50 50 SG . . . . . . . . . . 5186 1 stop_ loop_ _Assembly_common_name.Name _Assembly_common_name.Type _Assembly_common_name.Entry_ID _Assembly_common_name.Assembly_ID 'vascular endothelial growth factor receptor-binding domain dimer' system 5186 1 VEGF abbreviation 5186 1 stop_ save_ #################################### # Biological polymers and ligands # #################################### save_VEGF _Entity.Sf_category entity _Entity.Sf_framecode VEGF _Entity.Entry_ID 5186 _Entity.ID 1 _Entity.BMRB_code . _Entity.Name 'vascular endothelial growth factor' _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 ; HHEVVKFMDVYQRSYCHPIE TLVDIFQEYPDEIEYIFKPS CVPLMRCGGCCNDEGLECVP TEESNITMQIMRIKPHQGQH IGEMSFLQHNKCECRPKKD ; _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 99 _Entity.Number_of_nonpolymer_components . _Entity.Paramagnetic . _Entity.Thiol_state 'all disulfide bound' _Entity.Src_method . _Entity.Parent_entity_ID . _Entity.Fragment . _Entity.Mutation . _Entity.EC_number . _Entity.Calc_isoelectric_point . _Entity.Formula_weight 11625.4 _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 5198 . VEGF . . . . . 100.00 99 100.00 100.00 5.41e-66 . . . . 5186 1 2 no PDB 1BJ1 . "Vascular Endothelial Growth Factor In Complex With A Neutralizing Antibody" . . . . . 100.00 102 100.00 100.00 5.80e-66 . . . . 5186 1 3 no PDB 1CZ8 . "Vascular Endothelial Growth Factor In Complex With An Affinity Matured Antibody" . . . . . 94.95 94 100.00 100.00 5.27e-62 . . . . 5186 1 4 no PDB 1FLT . "Vegf In Complex With Domain 2 Of The Flt-1 Receptor" . . . . . 98.99 98 100.00 100.00 4.65e-65 . . . . 5186 1 5 no PDB 1KAT . "Solution Structure Of A Phage-Derived Peptide Antagonist In Complex With Vascular Endothelial Growth Factor" . . . . . 100.00 99 100.00 100.00 5.41e-66 . . . . 5186 1 6 no PDB 1MJV . "Disulfide Deficient Mutant Of Vascular Endothelial Growth Factor A (C51a And C60a)" . . . . . 95.96 96 97.89 97.89 2.26e-61 . . . . 5186 1 7 no PDB 1MKG . "Disulfide Deficient Mutant Of Vascular Endothelial Growth Factor A (C57a And C102a)" . . . . . 95.96 96 97.89 97.89 2.26e-61 . . . . 5186 1 8 no PDB 1MKK . "Disulfide Deficient Mutant Of Vascular Endothelial Growth Factor A (C61a And C104a)" . . . . . 95.96 96 97.89 97.89 2.26e-61 . . . . 5186 1 9 no PDB 1QTY . "Vascular Endothelial Growth Factor In Complex With Domain 2 Of The Flt-1 Receptor" . . . . . 100.00 102 100.00 100.00 5.80e-66 . . . . 5186 1 10 no PDB 1TZH . "Crystal Structure Of The Fab Yads1 Complexed With H-Vegf" . . . . . 100.00 102 100.00 100.00 5.80e-66 . . . . 5186 1 11 no PDB 1TZI . "Crystal Structure Of The Fab Yads2 Complexed With H-Vegf" . . . . . 100.00 102 100.00 100.00 5.80e-66 . . . . 5186 1 12 no PDB 1VPF . "Structure Of Human Vascular Endothelial Growth Factor" . . . . . 100.00 102 100.00 100.00 5.80e-66 . . . . 5186 1 13 no PDB 1VPP . "Complex Between Vegf And A Receptor Blocking Peptide" . . . . . 100.00 102 100.00 100.00 5.80e-66 . . . . 5186 1 14 no PDB 2FJG . "Structure Of The G6 Fab, A Phage Derived Fab Fragment, In Complex With Vegf" . . . . . 100.00 102 100.00 100.00 5.80e-66 . . . . 5186 1 15 no PDB 2FJH . "Structure Of The B20-4 Fab, A Phage Derived Fab Fragment, In Complex With Vegf" . . . . . 100.00 102 100.00 100.00 5.80e-66 . . . . 5186 1 16 no PDB 2QR0 . "Structure Of Vegf Complexed To A Fab Containing Tyr And Ser In The Cdrs" . . . . . 97.98 97 100.00 100.00 3.66e-64 . . . . 5186 1 17 no PDB 2VPF . "Vascular Endothelial Growth Factor Refined To 1.93 Angstroms Resolution" . . . . . 100.00 102 100.00 100.00 5.80e-66 . . . . 5186 1 18 no PDB 3BDY . "Dual Specific Bh1 Fab In Complex With Vegf" . . . . . 100.00 102 100.00 100.00 5.80e-66 . . . . 5186 1 19 no PDB 3P9W . "Crystal Structure Of An Engineered Human Autonomous Vh Domain In Complex With Vegf" . . . . . 100.00 106 100.00 100.00 3.06e-66 . . . . 5186 1 20 no PDB 3QTK . "The Crystal Structure Of Chemically Synthesized Vegf-A" . . . . . 100.00 102 100.00 100.00 5.80e-66 . . . . 5186 1 21 no PDB 3S1B . "The Development Of Peptide-Based Tools For The Analysis Of Angiogenesis" . . . . . 96.97 96 100.00 100.00 1.71e-63 . . . . 5186 1 22 no PDB 3S1K . "The Development Of Peptide-Based Tools For The Analysis Of Angiogenesis" . . . . . 100.00 102 100.00 100.00 5.80e-66 . . . . 5186 1 23 no PDB 3V2A . "Vegfr-2VEGF-A Complex Structure" . . . . . 100.00 134 100.00 100.00 5.35e-66 . . . . 5186 1 24 no PDB 4GLN . "Crystal Structure Of Chemically Synthesized Heterochiral {d-protein Antagonist Plus Vegf-a} Protein Complex In Space Group P21/" . . . . . 100.00 102 100.00 100.00 5.80e-66 . . . . 5186 1 25 no PDB 4GLS . "Crystal Structure Of Chemically Synthesized Heterochiral {d-protein Antagonist Plus Vegf-a} Protein Complex In Space Group P21" . . . . . 100.00 102 100.00 100.00 5.80e-66 . . . . 5186 1 26 no PDB 4KZN . "Crystal Structure Of Human Vegf-a Receptor Binding Domain" . . . . . 100.00 104 100.00 100.00 7.51e-66 . . . . 5186 1 27 no DBJ BAA78418 . "vascular endothelial growth factor isoform VEGF165 [Homo sapiens]" . . . . . 100.00 191 100.00 100.00 6.51e-66 . . . . 5186 1 28 no DBJ BAB68520 . "vascular endothelial growth factor [Felis catus]" . . . . . 98.99 189 96.94 97.96 2.79e-62 . . . . 5186 1 29 no DBJ BAD92722 . "vascular endothelial growth factor variant [Homo sapiens]" . . . . . 98.99 148 98.98 98.98 5.85e-65 . . . . 5186 1 30 no DBJ BAG70136 . "vascular endothelial growth factor isoform VEGF165 [Homo sapiens]" . . . . . 100.00 191 100.00 100.00 6.51e-66 . . . . 5186 1 31 no DBJ BAG70265 . "vascular endothelial growth factor isoform VEGF165 [Homo sapiens]" . . . . . 100.00 191 100.00 100.00 6.51e-66 . . . . 5186 1 32 no EMBL CAA09179 . "VEGF183 protein [Homo sapiens]" . . . . . 100.00 209 100.00 100.00 3.19e-66 . . . . 5186 1 33 no EMBL CAA44447 . "vascular endothelial growth factor [Homo sapiens]" . . . . . 100.00 191 100.00 100.00 6.51e-66 . . . . 5186 1 34 no EMBL CAA57143 . "unnamed protein product [Sus scrofa]" . . . . . 98.99 190 97.96 97.96 5.28e-63 . . . . 5186 1 35 no EMBL CAB82426 . "vascular endothelial growth factor 188 [Canis lupus familiaris]" . . . . . 98.99 214 96.94 97.96 2.18e-62 . . . . 5186 1 36 no EMBL CAC19923 . "vascular endothelial growth factor [Callithrix jacchus]" . . . . . 95.96 124 98.95 98.95 2.11e-61 . . . . 5186 1 37 no GB AAA35789 . "vascular endothelial growth factor [Homo sapiens]" . . . . . 100.00 191 100.00 100.00 6.51e-66 . . . . 5186 1 38 no GB AAA36804 . "vascular endothelial growth factor [Homo sapiens]" . . . . . 100.00 215 100.00 100.00 2.28e-66 . . . . 5186 1 39 no GB AAA36807 . "vascular permeability factor precursor [Homo sapiens]" . . . . . 100.00 215 100.00 100.00 2.28e-66 . . . . 5186 1 40 no GB AAB47118 . "simVEGF165 [Macaca fascicularis]" . . . . . 100.00 191 100.00 100.00 6.51e-66 . . . . 5186 1 41 no GB AAC63102 . "vascular endothelial growth factor [Homo sapiens]" . . . . . 100.00 254 100.00 100.00 9.73e-66 . . . . 5186 1 42 no PRF 2105202A . "vascular endothelial growth factor" . . . . . 98.99 190 97.96 97.96 5.28e-63 . . . . 5186 1 43 no REF NP_001003175 . "vascular endothelial growth factor A isoform 1 precursor [Canis lupus familiaris]" . . . . . 98.99 214 96.94 97.96 2.18e-62 . . . . 5186 1 44 no REF NP_001009854 . "vascular endothelial growth factor A precursor [Felis catus]" . . . . . 98.99 189 96.94 97.96 2.79e-62 . . . . 5186 1 45 no REF NP_001020537 . "vascular endothelial growth factor A isoform a [Homo sapiens]" . . . . . 100.00 412 100.00 100.00 9.44e-66 . . . . 5186 1 46 no REF NP_001020538 . "vascular endothelial growth factor A isoform c [Homo sapiens]" . . . . . 100.00 389 100.00 100.00 5.62e-66 . . . . 5186 1 47 no REF NP_001020539 . "vascular endothelial growth factor A isoform d [Homo sapiens]" . . . . . 100.00 371 100.00 100.00 8.37e-66 . . . . 5186 1 48 no SP P15692 . "RecName: Full=Vascular endothelial growth factor A; Short=VEGF-A; AltName: Full=Vascular permeability factor; Short=VPF; Flags:" . . . . . 100.00 232 100.00 100.00 8.37e-66 . . . . 5186 1 49 no SP P49151 . "RecName: Full=Vascular endothelial growth factor A; Short=VEGF-A; AltName: Full=Vascular permeability factor; Short=VPF; Flags:" . . . . . 98.99 190 97.96 97.96 5.28e-63 . . . . 5186 1 50 no SP Q9MYV3 . "RecName: Full=Vascular endothelial growth factor A; Short=VEGF-A; AltName: Full=Vascular permeability factor; Short=VPF; Flags:" . . . . . 98.99 214 96.94 97.96 2.18e-62 . . . . 5186 1 stop_ loop_ _Entity_common_name.Name _Entity_common_name.Type _Entity_common_name.Entry_ID _Entity_common_name.Entity_ID 'vascular endothelial growth factor' common 5186 1 VEGF(11-109) variant 5186 1 VEGF abbreviation 5186 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 11 HIS . 5186 1 2 12 HIS . 5186 1 3 13 GLU . 5186 1 4 14 VAL . 5186 1 5 15 VAL . 5186 1 6 16 LYS . 5186 1 7 17 PHE . 5186 1 8 18 MET . 5186 1 9 19 ASP . 5186 1 10 20 VAL . 5186 1 11 21 TYR . 5186 1 12 22 GLN . 5186 1 13 23 ARG . 5186 1 14 24 SER . 5186 1 15 25 TYR . 5186 1 16 26 CYS . 5186 1 17 27 HIS . 5186 1 18 28 PRO . 5186 1 19 29 ILE . 5186 1 20 30 GLU . 5186 1 21 31 THR . 5186 1 22 32 LEU . 5186 1 23 33 VAL . 5186 1 24 34 ASP . 5186 1 25 35 ILE . 5186 1 26 36 PHE . 5186 1 27 37 GLN . 5186 1 28 38 GLU . 5186 1 29 39 TYR . 5186 1 30 40 PRO . 5186 1 31 41 ASP . 5186 1 32 42 GLU . 5186 1 33 43 ILE . 5186 1 34 44 GLU . 5186 1 35 45 TYR . 5186 1 36 46 ILE . 5186 1 37 47 PHE . 5186 1 38 48 LYS . 5186 1 39 49 PRO . 5186 1 40 50 SER . 5186 1 41 51 CYS . 5186 1 42 52 VAL . 5186 1 43 53 PRO . 5186 1 44 54 LEU . 5186 1 45 55 MET . 5186 1 46 56 ARG . 5186 1 47 57 CYS . 5186 1 48 58 GLY . 5186 1 49 59 GLY . 5186 1 50 60 CYS . 5186 1 51 61 CYS . 5186 1 52 62 ASN . 5186 1 53 63 ASP . 5186 1 54 64 GLU . 5186 1 55 65 GLY . 5186 1 56 66 LEU . 5186 1 57 67 GLU . 5186 1 58 68 CYS . 5186 1 59 69 VAL . 5186 1 60 70 PRO . 5186 1 61 71 THR . 5186 1 62 72 GLU . 5186 1 63 73 GLU . 5186 1 64 74 SER . 5186 1 65 75 ASN . 5186 1 66 76 ILE . 5186 1 67 77 THR . 5186 1 68 78 MET . 5186 1 69 79 GLN . 5186 1 70 80 ILE . 5186 1 71 81 MET . 5186 1 72 82 ARG . 5186 1 73 83 ILE . 5186 1 74 84 LYS . 5186 1 75 85 PRO . 5186 1 76 86 HIS . 5186 1 77 87 GLN . 5186 1 78 88 GLY . 5186 1 79 89 GLN . 5186 1 80 90 HIS . 5186 1 81 91 ILE . 5186 1 82 92 GLY . 5186 1 83 93 GLU . 5186 1 84 94 MET . 5186 1 85 95 SER . 5186 1 86 96 PHE . 5186 1 87 97 LEU . 5186 1 88 98 GLN . 5186 1 89 99 HIS . 5186 1 90 100 ASN . 5186 1 91 101 LYS . 5186 1 92 102 CYS . 5186 1 93 103 GLU . 5186 1 94 104 CYS . 5186 1 95 105 ARG . 5186 1 96 106 PRO . 5186 1 97 107 LYS . 5186 1 98 108 LYS . 5186 1 99 109 ASP . 5186 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 . HIS 1 1 5186 1 . HIS 2 2 5186 1 . GLU 3 3 5186 1 . VAL 4 4 5186 1 . VAL 5 5 5186 1 . LYS 6 6 5186 1 . PHE 7 7 5186 1 . MET 8 8 5186 1 . ASP 9 9 5186 1 . VAL 10 10 5186 1 . TYR 11 11 5186 1 . GLN 12 12 5186 1 . ARG 13 13 5186 1 . SER 14 14 5186 1 . TYR 15 15 5186 1 . CYS 16 16 5186 1 . HIS 17 17 5186 1 . PRO 18 18 5186 1 . ILE 19 19 5186 1 . GLU 20 20 5186 1 . THR 21 21 5186 1 . LEU 22 22 5186 1 . VAL 23 23 5186 1 . ASP 24 24 5186 1 . ILE 25 25 5186 1 . PHE 26 26 5186 1 . GLN 27 27 5186 1 . GLU 28 28 5186 1 . TYR 29 29 5186 1 . PRO 30 30 5186 1 . ASP 31 31 5186 1 . GLU 32 32 5186 1 . ILE 33 33 5186 1 . GLU 34 34 5186 1 . TYR 35 35 5186 1 . ILE 36 36 5186 1 . PHE 37 37 5186 1 . LYS 38 38 5186 1 . PRO 39 39 5186 1 . SER 40 40 5186 1 . CYS 41 41 5186 1 . VAL 42 42 5186 1 . PRO 43 43 5186 1 . LEU 44 44 5186 1 . MET 45 45 5186 1 . ARG 46 46 5186 1 . CYS 47 47 5186 1 . GLY 48 48 5186 1 . GLY 49 49 5186 1 . CYS 50 50 5186 1 . CYS 51 51 5186 1 . ASN 52 52 5186 1 . ASP 53 53 5186 1 . GLU 54 54 5186 1 . GLY 55 55 5186 1 . LEU 56 56 5186 1 . GLU 57 57 5186 1 . CYS 58 58 5186 1 . VAL 59 59 5186 1 . PRO 60 60 5186 1 . THR 61 61 5186 1 . GLU 62 62 5186 1 . GLU 63 63 5186 1 . SER 64 64 5186 1 . ASN 65 65 5186 1 . ILE 66 66 5186 1 . THR 67 67 5186 1 . MET 68 68 5186 1 . GLN 69 69 5186 1 . ILE 70 70 5186 1 . MET 71 71 5186 1 . ARG 72 72 5186 1 . ILE 73 73 5186 1 . LYS 74 74 5186 1 . PRO 75 75 5186 1 . HIS 76 76 5186 1 . GLN 77 77 5186 1 . GLY 78 78 5186 1 . GLN 79 79 5186 1 . HIS 80 80 5186 1 . ILE 81 81 5186 1 . GLY 82 82 5186 1 . GLU 83 83 5186 1 . MET 84 84 5186 1 . SER 85 85 5186 1 . PHE 86 86 5186 1 . LEU 87 87 5186 1 . GLN 88 88 5186 1 . HIS 89 89 5186 1 . ASN 90 90 5186 1 . LYS 91 91 5186 1 . CYS 92 92 5186 1 . GLU 93 93 5186 1 . CYS 94 94 5186 1 . ARG 95 95 5186 1 . PRO 96 96 5186 1 . LYS 97 97 5186 1 . LYS 98 98 5186 1 . ASP 99 99 5186 1 stop_ save_ #################### # Natural source # #################### save_natural_source _Entity_natural_src_list.Sf_category natural_source _Entity_natural_src_list.Sf_framecode natural_source _Entity_natural_src_list.Entry_ID 5186 _Entity_natural_src_list.ID 1 loop_ _Entity_natural_src.ID _Entity_natural_src.Entity_ID _Entity_natural_src.Entity_label _Entity_natural_src.Entity_chimera_segment_ID _Entity_natural_src.NCBI_taxonomy_ID _Entity_natural_src.Type _Entity_natural_src.Common _Entity_natural_src.Organism_name_scientific _Entity_natural_src.Organism_name_common _Entity_natural_src.Organism_acronym _Entity_natural_src.ICTVdb_decimal_code _Entity_natural_src.Superkingdom _Entity_natural_src.Kingdom _Entity_natural_src.Genus _Entity_natural_src.Species _Entity_natural_src.Strain _Entity_natural_src.Variant _Entity_natural_src.Subvariant _Entity_natural_src.Organ _Entity_natural_src.Tissue _Entity_natural_src.Tissue_fraction _Entity_natural_src.Cell_line _Entity_natural_src.Cell_type _Entity_natural_src.ATCC_number _Entity_natural_src.Organelle _Entity_natural_src.Cellular_location _Entity_natural_src.Fragment _Entity_natural_src.Fraction _Entity_natural_src.Secretion _Entity_natural_src.Plasmid _Entity_natural_src.Plasmid_details _Entity_natural_src.Gene_mnemonic _Entity_natural_src.Dev_stage _Entity_natural_src.Details _Entity_natural_src.Citation_ID _Entity_natural_src.Citation_label _Entity_natural_src.Entry_ID _Entity_natural_src.Entity_natural_src_list_ID 1 1 $VEGF . 9606 . . 'Homo sapiens' Human . . Eukaryota Metazoa Homo sapiens . . . . . . . . . . . . . . . . . . . . . 5186 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 5186 _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 $VEGF . 'recombinant technology' . 'E. coli' . . . . . . . . . . . . . . . . . . . . . . . . . . . 5186 1 stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_Sample_1 _Sample.Sf_category sample _Sample.Sf_framecode Sample_1 _Sample.Entry_ID 5186 _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 'vascular endothelial growth factor' '[U-98% 13C; U-98% 15N]' . . 1 $VEGF . . 1.0 . . mM . . . . 5186 1 stop_ save_ save_Sample_2 _Sample.Sf_category sample _Sample.Sf_framecode Sample_2 _Sample.Entry_ID 5186 _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 'vascular endothelial growth factor' '[U-98% 13C; U-98% 15N]' . . 1 $VEGF . . 2.0 . . mM . . . . 5186 2 stop_ save_ ####################### # Sample conditions # ####################### save_Cond_1 _Sample_condition_list.Sf_category sample_conditions _Sample_condition_list.Sf_framecode Cond_1 _Sample_condition_list.Entry_ID 5186 _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 7.0 0.1 n/a 5186 1 temperature 318 0.2 K 5186 1 stop_ save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer_1 _NMR_spectrometer.Sf_category NMR_spectrometer _NMR_spectrometer.Sf_framecode NMR_spectrometer_1 _NMR_spectrometer.Entry_ID 5186 _NMR_spectrometer.ID 1 _NMR_spectrometer.Details . _NMR_spectrometer.Manufacturer Bruker _NMR_spectrometer.Model AMX _NMR_spectrometer.Serial_number . _NMR_spectrometer.Field_strength 500 save_ save_NMR_spectrometer_2 _NMR_spectrometer.Sf_category NMR_spectrometer _NMR_spectrometer.Sf_framecode NMR_spectrometer_2 _NMR_spectrometer.Entry_ID 5186 _NMR_spectrometer.ID 2 _NMR_spectrometer.Details . _NMR_spectrometer.Manufacturer Bruker _NMR_spectrometer.Model DRX _NMR_spectrometer.Serial_number . _NMR_spectrometer.Field_strength 800 save_ save_spectrometer_list _NMR_spectrometer_list.Sf_category NMR_spectrometer_list _NMR_spectrometer_list.Sf_framecode spectrometer_list _NMR_spectrometer_list.Entry_ID 5186 _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 NMR_spectrometer_1 Bruker AMX . 500 . . . 5186 1 2 NMR_spectrometer_2 Bruker DRX . 800 . . . 5186 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 5186 _Experiment_list.ID 1 _Experiment_list.Details . 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 5186 _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 1.0 . . . . . . . . . 5186 1 N 15 DSS 'methyl protons' . . . . ppm 0.0 . indirect 0.101329118 . . . . . . . . . 5186 1 C 13 DSS 'methyl protons' . . . . ppm 0.0 . indirect 0.251449530 . . . . . . . . . 5186 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_shift_set_1 _Assigned_chem_shift_list.Sf_category assigned_chemical_shifts _Assigned_chem_shift_list.Sf_framecode shift_set_1 _Assigned_chem_shift_list.Entry_ID 5186 _Assigned_chem_shift_list.ID 1 _Assigned_chem_shift_list.Sample_condition_list_ID 1 _Assigned_chem_shift_list.Sample_condition_list_label $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 . 5186 1 . . 2 $Sample_2 . 5186 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 3 3 GLU HA H 1 4.30 0.02 . 1 . . . . . . . . 5186 1 2 . 1 1 3 3 GLU C C 13 175.90 0.20 . 1 . . . . . . . . 5186 1 3 . 1 1 3 3 GLU CA C 13 56.60 0.20 . 1 . . . . . . . . 5186 1 4 . 1 1 3 3 GLU CB C 13 31.30 0.20 . 1 . . . . . . . . 5186 1 5 . 1 1 4 4 VAL H H 1 8.05 0.02 . 1 . . . . . . . . 5186 1 6 . 1 1 4 4 VAL HA H 1 4.27 0.02 . 1 . . . . . . . . 5186 1 7 . 1 1 4 4 VAL C C 13 175.83 0.20 . 1 . . . . . . . . 5186 1 8 . 1 1 4 4 VAL CA C 13 61.66 0.20 . 1 . . . . . . . . 5186 1 9 . 1 1 4 4 VAL CB C 13 33.90 0.20 . 1 . . . . . . . . 5186 1 10 . 1 1 4 4 VAL N N 15 123.12 0.10 . 1 . . . . . . . . 5186 1 11 . 1 1 5 5 VAL H H 1 8.58 0.02 . 1 . . . . . . . . 5186 1 12 . 1 1 5 5 VAL HA H 1 4.07 0.02 . 1 . . . . . . . . 5186 1 13 . 1 1 5 5 VAL C C 13 175.89 0.20 . 1 . . . . . . . . 5186 1 14 . 1 1 5 5 VAL CA C 13 63.22 0.20 . 1 . . . . . . . . 5186 1 15 . 1 1 5 5 VAL CB C 13 32.30 0.20 . 1 . . . . . . . . 5186 1 16 . 1 1 5 5 VAL N N 15 128.73 0.10 . 1 . . . . . . . . 5186 1 17 . 1 1 6 6 LYS H H 1 8.90 0.02 . 1 . . . . . . . . 5186 1 18 . 1 1 6 6 LYS HA H 1 4.09 0.02 . 1 . . . . . . . . 5186 1 19 . 1 1 6 6 LYS C C 13 178.17 0.20 . 1 . . . . . . . . 5186 1 20 . 1 1 6 6 LYS CA C 13 56.85 0.20 . 1 . . . . . . . . 5186 1 21 . 1 1 6 6 LYS CB C 13 33.30 0.20 . 1 . . . . . . . . 5186 1 22 . 1 1 6 6 LYS N N 15 127.56 0.10 . 1 . . . . . . . . 5186 1 23 . 1 1 7 7 PHE H H 1 8.83 0.02 . 1 . . . . . . . . 5186 1 24 . 1 1 7 7 PHE HA H 1 4.62 0.02 . 1 . . . . . . . . 5186 1 25 . 1 1 7 7 PHE C C 13 176.31 0.20 . 1 . . . . . . . . 5186 1 26 . 1 1 7 7 PHE CA C 13 61.22 0.20 . 1 . . . . . . . . 5186 1 27 . 1 1 7 7 PHE CB C 13 40.10 0.20 . 1 . . . . . . . . 5186 1 28 . 1 1 7 7 PHE N N 15 122.81 0.10 . 1 . . . . . . . . 5186 1 29 . 1 1 8 8 MET H H 1 8.91 0.02 . 1 . . . . . . . . 5186 1 30 . 1 1 8 8 MET HA H 1 3.96 0.02 . 1 . . . . . . . . 5186 1 31 . 1 1 8 8 MET C C 13 178.39 0.20 . 1 . . . . . . . . 5186 1 32 . 1 1 8 8 MET CA C 13 57.87 0.20 . 1 . . . . . . . . 5186 1 33 . 1 1 8 8 MET CB C 13 31.60 0.20 . 1 . . . . . . . . 5186 1 34 . 1 1 8 8 MET N N 15 115.31 0.10 . 1 . . . . . . . . 5186 1 35 . 1 1 9 9 ASP H H 1 7.16 0.02 . 1 . . . . . . . . 5186 1 36 . 1 1 9 9 ASP HA H 1 4.49 0.02 . 1 . . . . . . . . 5186 1 37 . 1 1 9 9 ASP C C 13 178.04 0.20 . 1 . . . . . . . . 5186 1 38 . 1 1 9 9 ASP CA C 13 57.42 0.20 . 1 . . . . . . . . 5186 1 39 . 1 1 9 9 ASP CB C 13 41.30 0.20 . 1 . . . . . . . . 5186 1 40 . 1 1 9 9 ASP N N 15 118.56 0.10 . 1 . . . . . . . . 5186 1 41 . 1 1 10 10 VAL H H 1 7.95 0.02 . 1 . . . . . . . . 5186 1 42 . 1 1 10 10 VAL HA H 1 3.43 0.02 . 1 . . . . . . . . 5186 1 43 . 1 1 10 10 VAL C C 13 177.99 0.20 . 1 . . . . . . . . 5186 1 44 . 1 1 10 10 VAL CA C 13 66.73 0.20 . 1 . . . . . . . . 5186 1 45 . 1 1 10 10 VAL N N 15 119.59 0.10 . 1 . . . . . . . . 5186 1 46 . 1 1 11 11 TYR H H 1 8.65 0.02 . 1 . . . . . . . . 5186 1 47 . 1 1 11 11 TYR HA H 1 3.65 0.02 . 1 . . . . . . . . 5186 1 48 . 1 1 11 11 TYR C C 13 177.99 0.20 . 1 . . . . . . . . 5186 1 49 . 1 1 11 11 TYR CA C 13 62.19 0.20 . 1 . . . . . . . . 5186 1 50 . 1 1 11 11 TYR CB C 13 39.00 0.20 . 1 . . . . . . . . 5186 1 51 . 1 1 11 11 TYR N N 15 120.46 0.10 . 1 . . . . . . . . 5186 1 52 . 1 1 12 12 GLN H H 1 7.84 0.02 . 1 . . . . . . . . 5186 1 53 . 1 1 12 12 GLN HA H 1 3.94 0.02 . 1 . . . . . . . . 5186 1 54 . 1 1 12 12 GLN C C 13 178.57 0.20 . 1 . . . . . . . . 5186 1 55 . 1 1 12 12 GLN CA C 13 59.03 0.20 . 1 . . . . . . . . 5186 1 56 . 1 1 12 12 GLN CB C 13 29.30 0.20 . 1 . . . . . . . . 5186 1 57 . 1 1 12 12 GLN N N 15 115.56 0.10 . 1 . . . . . . . . 5186 1 58 . 1 1 13 13 ARG H H 1 7.87 0.02 . 1 . . . . . . . . 5186 1 59 . 1 1 13 13 ARG HA H 1 3.97 0.02 . 1 . . . . . . . . 5186 1 60 . 1 1 13 13 ARG C C 13 177.18 0.20 . 1 . . . . . . . . 5186 1 61 . 1 1 13 13 ARG CA C 13 58.54 0.20 . 1 . . . . . . . . 5186 1 62 . 1 1 13 13 ARG CB C 13 32.00 0.20 . 1 . . . . . . . . 5186 1 63 . 1 1 13 13 ARG N N 15 116.68 0.10 . 1 . . . . . . . . 5186 1 64 . 1 1 14 14 SER H H 1 7.78 0.02 . 1 . . . . . . . . 5186 1 65 . 1 1 14 14 SER HA H 1 4.28 0.02 . 1 . . . . . . . . 5186 1 66 . 1 1 14 14 SER C C 13 172.62 0.20 . 1 . . . . . . . . 5186 1 67 . 1 1 14 14 SER CA C 13 58.97 0.20 . 1 . . . . . . . . 5186 1 68 . 1 1 14 14 SER CB C 13 65.30 0.20 . 1 . . . . . . . . 5186 1 69 . 1 1 14 14 SER N N 15 112.37 0.10 . 1 . . . . . . . . 5186 1 70 . 1 1 15 15 TYR H H 1 6.79 0.02 . 1 . . . . . . . . 5186 1 71 . 1 1 15 15 TYR HA H 1 4.36 0.02 . 1 . . . . . . . . 5186 1 72 . 1 1 15 15 TYR C C 13 175.29 0.20 . 1 . . . . . . . . 5186 1 73 . 1 1 15 15 TYR CA C 13 59.66 0.20 . 1 . . . . . . . . 5186 1 74 . 1 1 15 15 TYR CB C 13 38.80 0.20 . 1 . . . . . . . . 5186 1 75 . 1 1 15 15 TYR N N 15 122.46 0.10 . 1 . . . . . . . . 5186 1 76 . 1 1 16 16 CYS H H 1 6.87 0.02 . 1 . . . . . . . . 5186 1 77 . 1 1 16 16 CYS HA H 1 4.65 0.02 . 1 . . . . . . . . 5186 1 78 . 1 1 16 16 CYS C C 13 171.64 0.20 . 1 . . . . . . . . 5186 1 79 . 1 1 16 16 CYS CA C 13 55.85 0.20 . 1 . . . . . . . . 5186 1 80 . 1 1 16 16 CYS CB C 13 39.00 0.20 . 1 . . . . . . . . 5186 1 81 . 1 1 16 16 CYS N N 15 126.65 0.10 . 1 . . . . . . . . 5186 1 82 . 1 1 17 17 HIS H H 1 9.20 0.02 . 1 . . . . . . . . 5186 1 83 . 1 1 17 17 HIS HA H 1 4.76 0.02 . 1 . . . . . . . . 5186 1 84 . 1 1 17 17 HIS C C 13 170.49 0.20 . 1 . . . . . . . . 5186 1 85 . 1 1 17 17 HIS CA C 13 55.54 0.20 . 1 . . . . . . . . 5186 1 86 . 1 1 17 17 HIS N N 15 124.53 0.10 . 1 . . . . . . . . 5186 1 87 . 1 1 18 18 PRO HA H 1 4.21 0.02 . 1 . . . . . . . . 5186 1 88 . 1 1 18 18 PRO C C 13 175.49 0.20 . 1 . . . . . . . . 5186 1 89 . 1 1 18 18 PRO CA C 13 63.30 0.20 . 1 . . . . . . . . 5186 1 90 . 1 1 19 19 ILE H H 1 9.00 0.02 . 1 . . . . . . . . 5186 1 91 . 1 1 19 19 ILE HA H 1 4.47 0.02 . 1 . . . . . . . . 5186 1 92 . 1 1 19 19 ILE C C 13 175.25 0.20 . 1 . . . . . . . . 5186 1 93 . 1 1 19 19 ILE CA C 13 59.45 0.20 . 1 . . . . . . . . 5186 1 94 . 1 1 19 19 ILE CB C 13 42.80 0.20 . 1 . . . . . . . . 5186 1 95 . 1 1 19 19 ILE N N 15 124.18 0.10 . 1 . . . . . . . . 5186 1 96 . 1 1 20 20 GLU H H 1 8.60 0.02 . 1 . . . . . . . . 5186 1 97 . 1 1 20 20 GLU HA H 1 4.15 0.02 . 1 . . . . . . . . 5186 1 98 . 1 1 20 20 GLU C C 13 175.33 0.20 . 1 . . . . . . . . 5186 1 99 . 1 1 20 20 GLU CA C 13 59.32 0.20 . 1 . . . . . . . . 5186 1 100 . 1 1 20 20 GLU N N 15 129.56 0.10 . 1 . . . . . . . . 5186 1 101 . 1 1 21 21 THR H H 1 9.36 0.02 . 1 . . . . . . . . 5186 1 102 . 1 1 21 21 THR HA H 1 4.25 0.02 . 1 . . . . . . . . 5186 1 103 . 1 1 21 21 THR C C 13 171.76 0.20 . 1 . . . . . . . . 5186 1 104 . 1 1 21 21 THR CA C 13 61.85 0.20 . 1 . . . . . . . . 5186 1 105 . 1 1 21 21 THR CB C 13 71.70 0.20 . 1 . . . . . . . . 5186 1 106 . 1 1 21 21 THR N N 15 127.06 0.10 . 1 . . . . . . . . 5186 1 107 . 1 1 22 22 LEU H H 1 8.58 0.02 . 1 . . . . . . . . 5186 1 108 . 1 1 22 22 LEU HA H 1 4.82 0.02 . 1 . . . . . . . . 5186 1 109 . 1 1 22 22 LEU C C 13 176.25 0.20 . 1 . . . . . . . . 5186 1 110 . 1 1 22 22 LEU CA C 13 53.39 0.20 . 1 . . . . . . . . 5186 1 111 . 1 1 22 22 LEU CB C 13 40.10 0.20 . 1 . . . . . . . . 5186 1 112 . 1 1 22 22 LEU N N 15 128.81 0.10 . 1 . . . . . . . . 5186 1 113 . 1 1 23 23 VAL H H 1 8.65 0.02 . 1 . . . . . . . . 5186 1 114 . 1 1 23 23 VAL HA H 1 4.07 0.02 . 1 . . . . . . . . 5186 1 115 . 1 1 23 23 VAL C C 13 175.51 0.20 . 1 . . . . . . . . 5186 1 116 . 1 1 23 23 VAL CA C 13 61.28 0.20 . 1 . . . . . . . . 5186 1 117 . 1 1 23 23 VAL CB C 13 35.10 0.20 . 1 . . . . . . . . 5186 1 118 . 1 1 23 23 VAL N N 15 125.43 0.10 . 1 . . . . . . . . 5186 1 119 . 1 1 24 24 ASP H H 1 8.55 0.02 . 1 . . . . . . . . 5186 1 120 . 1 1 24 24 ASP HA H 1 4.63 0.02 . 1 . . . . . . . . 5186 1 121 . 1 1 24 24 ASP C C 13 177.67 0.20 . 1 . . . . . . . . 5186 1 122 . 1 1 24 24 ASP CA C 13 55.02 0.20 . 1 . . . . . . . . 5186 1 123 . 1 1 24 24 ASP CB C 13 42.60 0.20 . 1 . . . . . . . . 5186 1 124 . 1 1 24 24 ASP N N 15 127.09 0.10 . 1 . . . . . . . . 5186 1 125 . 1 1 25 25 ILE H H 1 8.64 0.02 . 1 . . . . . . . . 5186 1 126 . 1 1 25 25 ILE HA H 1 3.41 0.02 . 1 . . . . . . . . 5186 1 127 . 1 1 25 25 ILE C C 13 178.14 0.20 . 1 . . . . . . . . 5186 1 128 . 1 1 25 25 ILE CA C 13 67.08 0.20 . 1 . . . . . . . . 5186 1 129 . 1 1 25 25 ILE CB C 13 37.90 0.20 . 1 . . . . . . . . 5186 1 130 . 1 1 25 25 ILE N N 15 127.68 0.10 . 1 . . . . . . . . 5186 1 131 . 1 1 26 26 PHE H H 1 8.53 0.02 . 1 . . . . . . . . 5186 1 132 . 1 1 26 26 PHE HA H 1 4.45 0.02 . 1 . . . . . . . . 5186 1 133 . 1 1 26 26 PHE C C 13 177.30 0.20 . 1 . . . . . . . . 5186 1 134 . 1 1 26 26 PHE CA C 13 59.86 0.20 . 1 . . . . . . . . 5186 1 135 . 1 1 26 26 PHE CB C 13 38.50 0.20 . 1 . . . . . . . . 5186 1 136 . 1 1 26 26 PHE N N 15 117.25 0.10 . 1 . . . . . . . . 5186 1 137 . 1 1 27 27 GLN H H 1 7.60 0.02 . 1 . . . . . . . . 5186 1 138 . 1 1 27 27 GLN HA H 1 4.10 0.02 . 1 . . . . . . . . 5186 1 139 . 1 1 27 27 GLN C C 13 177.43 0.20 . 1 . . . . . . . . 5186 1 140 . 1 1 27 27 GLN CA C 13 58.29 0.20 . 1 . . . . . . . . 5186 1 141 . 1 1 27 27 GLN CB C 13 29.20 0.20 . 1 . . . . . . . . 5186 1 142 . 1 1 27 27 GLN N N 15 116.25 0.10 . 1 . . . . . . . . 5186 1 143 . 1 1 28 28 GLU H H 1 7.24 0.02 . 1 . . . . . . . . 5186 1 144 . 1 1 28 28 GLU HA H 1 4.10 0.02 . 1 . . . . . . . . 5186 1 145 . 1 1 28 28 GLU C C 13 176.22 0.20 . 1 . . . . . . . . 5186 1 146 . 1 1 28 28 GLU CA C 13 57.07 0.20 . 1 . . . . . . . . 5186 1 147 . 1 1 28 28 GLU CB C 13 31.70 0.20 . 1 . . . . . . . . 5186 1 148 . 1 1 28 28 GLU N N 15 117.81 0.10 . 1 . . . . . . . . 5186 1 149 . 1 1 29 29 TYR H H 1 8.23 0.02 . 1 . . . . . . . . 5186 1 150 . 1 1 29 29 TYR HA H 1 4.87 0.02 . 1 . . . . . . . . 5186 1 151 . 1 1 29 29 TYR C C 13 173.48 0.20 . 1 . . . . . . . . 5186 1 152 . 1 1 29 29 TYR CA C 13 56.93 0.20 . 1 . . . . . . . . 5186 1 153 . 1 1 29 29 TYR N N 15 118.03 0.10 . 1 . . . . . . . . 5186 1 154 . 1 1 30 30 PRO HA H 1 4.59 0.02 . 1 . . . . . . . . 5186 1 155 . 1 1 30 30 PRO C C 13 177.94 0.20 . 1 . . . . . . . . 5186 1 156 . 1 1 30 30 PRO CA C 13 64.90 0.20 . 1 . . . . . . . . 5186 1 157 . 1 1 30 30 PRO CB C 13 32.50 0.20 . 1 . . . . . . . . 5186 1 158 . 1 1 31 31 ASP H H 1 8.51 0.02 . 1 . . . . . . . . 5186 1 159 . 1 1 31 31 ASP HA H 1 4.77 0.02 . 1 . . . . . . . . 5186 1 160 . 1 1 31 31 ASP C C 13 177.80 0.20 . 1 . . . . . . . . 5186 1 161 . 1 1 31 31 ASP CA C 13 54.92 0.20 . 1 . . . . . . . . 5186 1 162 . 1 1 31 31 ASP CB C 13 41.20 0.20 . 1 . . . . . . . . 5186 1 163 . 1 1 31 31 ASP N N 15 115.81 0.10 . 1 . . . . . . . . 5186 1 164 . 1 1 32 32 GLU H H 1 7.83 0.02 . 1 . . . . . . . . 5186 1 165 . 1 1 32 32 GLU HA H 1 4.84 0.02 . 1 . . . . . . . . 5186 1 166 . 1 1 32 32 GLU C C 13 176.70 0.20 . 1 . . . . . . . . 5186 1 167 . 1 1 32 32 GLU CA C 13 56.68 0.20 . 1 . . . . . . . . 5186 1 168 . 1 1 32 32 GLU CB C 13 29.10 0.20 . 1 . . . . . . . . 5186 1 169 . 1 1 32 32 GLU N N 15 121.99 0.10 . 1 . . . . . . . . 5186 1 170 . 1 1 33 33 ILE H H 1 7.37 0.02 . 1 . . . . . . . . 5186 1 171 . 1 1 33 33 ILE HA H 1 4.26 0.02 . 1 . . . . . . . . 5186 1 172 . 1 1 33 33 ILE C C 13 176.67 0.20 . 1 . . . . . . . . 5186 1 173 . 1 1 33 33 ILE CA C 13 62.60 0.20 . 1 . . . . . . . . 5186 1 174 . 1 1 33 33 ILE CB C 13 39.40 0.20 . 1 . . . . . . . . 5186 1 175 . 1 1 33 33 ILE N N 15 114.75 0.10 . 1 . . . . . . . . 5186 1 176 . 1 1 34 34 GLU H H 1 8.48 0.02 . 1 . . . . . . . . 5186 1 177 . 1 1 34 34 GLU HA H 1 4.11 0.02 . 1 . . . . . . . . 5186 1 178 . 1 1 34 34 GLU C C 13 175.79 0.20 . 1 . . . . . . . . 5186 1 179 . 1 1 34 34 GLU CA C 13 57.81 0.20 . 1 . . . . . . . . 5186 1 180 . 1 1 34 34 GLU CB C 13 30.50 0.20 . 1 . . . . . . . . 5186 1 181 . 1 1 34 34 GLU N N 15 120.68 0.10 . 1 . . . . . . . . 5186 1 182 . 1 1 35 35 TYR H H 1 7.66 0.02 . 1 . . . . . . . . 5186 1 183 . 1 1 35 35 TYR HA H 1 4.70 0.02 . 1 . . . . . . . . 5186 1 184 . 1 1 35 35 TYR C C 13 175.21 0.20 . 1 . . . . . . . . 5186 1 185 . 1 1 35 35 TYR CA C 13 57.74 0.20 . 1 . . . . . . . . 5186 1 186 . 1 1 35 35 TYR CB C 13 41.30 0.20 . 1 . . . . . . . . 5186 1 187 . 1 1 35 35 TYR N N 15 116.37 0.10 . 1 . . . . . . . . 5186 1 188 . 1 1 36 36 ILE H H 1 8.48 0.02 . 1 . . . . . . . . 5186 1 189 . 1 1 36 36 ILE HA H 1 4.19 0.02 . 1 . . . . . . . . 5186 1 190 . 1 1 36 36 ILE C C 13 174.58 0.20 . 1 . . . . . . . . 5186 1 191 . 1 1 36 36 ILE CA C 13 60.89 0.20 . 1 . . . . . . . . 5186 1 192 . 1 1 36 36 ILE CB C 13 40.40 0.20 . 1 . . . . . . . . 5186 1 193 . 1 1 36 36 ILE N N 15 118.12 0.10 . 1 . . . . . . . . 5186 1 194 . 1 1 37 37 PHE H H 1 8.16 0.02 . 1 . . . . . . . . 5186 1 195 . 1 1 37 37 PHE HA H 1 5.51 0.02 . 1 . . . . . . . . 5186 1 196 . 1 1 37 37 PHE C C 13 175.90 0.20 . 1 . . . . . . . . 5186 1 197 . 1 1 37 37 PHE CA C 13 56.96 0.20 . 1 . . . . . . . . 5186 1 198 . 1 1 37 37 PHE CB C 13 43.10 0.20 . 1 . . . . . . . . 5186 1 199 . 1 1 37 37 PHE N N 15 123.33 0.10 . 1 . . . . . . . . 5186 1 200 . 1 1 38 38 LYS H H 1 8.99 0.02 . 1 . . . . . . . . 5186 1 201 . 1 1 38 38 LYS HA H 1 4.60 0.02 . 1 . . . . . . . . 5186 1 202 . 1 1 38 38 LYS C C 13 174.84 0.20 . 1 . . . . . . . . 5186 1 203 . 1 1 38 38 LYS CA C 13 53.79 0.20 . 1 . . . . . . . . 5186 1 204 . 1 1 38 38 LYS N N 15 121.65 0.10 . 1 . . . . . . . . 5186 1 205 . 1 1 39 39 PRO HA H 1 4.77 0.02 . 1 . . . . . . . . 5186 1 206 . 1 1 39 39 PRO C C 13 173.90 0.20 . 1 . . . . . . . . 5186 1 207 . 1 1 39 39 PRO CA C 13 63.90 0.20 . 1 . . . . . . . . 5186 1 208 . 1 1 40 40 SER H H 1 8.48 0.02 . 1 . . . . . . . . 5186 1 209 . 1 1 40 40 SER HA H 1 4.27 0.02 . 1 . . . . . . . . 5186 1 210 . 1 1 40 40 SER C C 13 173.05 0.20 . 1 . . . . . . . . 5186 1 211 . 1 1 40 40 SER CA C 13 59.64 0.20 . 1 . . . . . . . . 5186 1 212 . 1 1 40 40 SER CB C 13 64.50 0.20 . 1 . . . . . . . . 5186 1 213 . 1 1 40 40 SER N N 15 109.06 0.10 . 1 . . . . . . . . 5186 1 214 . 1 1 41 41 CYS H H 1 8.13 0.02 . 1 . . . . . . . . 5186 1 215 . 1 1 41 41 CYS HA H 1 5.62 0.02 . 1 . . . . . . . . 5186 1 216 . 1 1 41 41 CYS C C 13 170.91 0.20 . 1 . . . . . . . . 5186 1 217 . 1 1 41 41 CYS CA C 13 56.03 0.20 . 1 . . . . . . . . 5186 1 218 . 1 1 41 41 CYS CB C 13 39.90 0.20 . 1 . . . . . . . . 5186 1 219 . 1 1 41 41 CYS N N 15 123.24 0.10 . 1 . . . . . . . . 5186 1 220 . 1 1 42 42 VAL H H 1 8.41 0.02 . 1 . . . . . . . . 5186 1 221 . 1 1 42 42 VAL HA H 1 4.74 0.02 . 1 . . . . . . . . 5186 1 222 . 1 1 42 42 VAL C C 13 172.82 0.20 . 1 . . . . . . . . 5186 1 223 . 1 1 42 42 VAL CA C 13 57.05 0.20 . 1 . . . . . . . . 5186 1 224 . 1 1 42 42 VAL N N 15 109.69 0.10 . 1 . . . . . . . . 5186 1 225 . 1 1 43 43 PRO HA H 1 4.91 0.02 . 1 . . . . . . . . 5186 1 226 . 1 1 43 43 PRO C C 13 175.34 0.20 . 1 . . . . . . . . 5186 1 227 . 1 1 43 43 PRO CA C 13 61.00 0.20 . 1 . . . . . . . . 5186 1 228 . 1 1 43 43 PRO CB C 13 30.80 0.20 . 1 . . . . . . . . 5186 1 229 . 1 1 44 44 LEU H H 1 9.01 0.02 . 1 . . . . . . . . 5186 1 230 . 1 1 44 44 LEU HA H 1 4.68 0.02 . 1 . . . . . . . . 5186 1 231 . 1 1 44 44 LEU C C 13 176.46 0.20 . 1 . . . . . . . . 5186 1 232 . 1 1 44 44 LEU CA C 13 52.83 0.20 . 1 . . . . . . . . 5186 1 233 . 1 1 44 44 LEU CB C 13 47.40 0.20 . 1 . . . . . . . . 5186 1 234 . 1 1 44 44 LEU N N 15 124.31 0.10 . 1 . . . . . . . . 5186 1 235 . 1 1 45 45 MET H H 1 8.62 0.02 . 1 . . . . . . . . 5186 1 236 . 1 1 45 45 MET HA H 1 4.77 0.02 . 1 . . . . . . . . 5186 1 237 . 1 1 45 45 MET C C 13 176.77 0.20 . 1 . . . . . . . . 5186 1 238 . 1 1 45 45 MET CA C 13 54.05 0.20 . 1 . . . . . . . . 5186 1 239 . 1 1 45 45 MET CB C 13 31.60 0.20 . 1 . . . . . . . . 5186 1 240 . 1 1 45 45 MET N N 15 121.25 0.10 . 1 . . . . . . . . 5186 1 241 . 1 1 46 46 ARG H H 1 8.65 0.02 . 1 . . . . . . . . 5186 1 242 . 1 1 46 46 ARG HA H 1 4.54 0.02 . 1 . . . . . . . . 5186 1 243 . 1 1 46 46 ARG C C 13 176.29 0.20 . 1 . . . . . . . . 5186 1 244 . 1 1 46 46 ARG CA C 13 52.32 0.20 . 1 . . . . . . . . 5186 1 245 . 1 1 46 46 ARG CB C 13 34.70 0.20 . 1 . . . . . . . . 5186 1 246 . 1 1 46 46 ARG N N 15 125.54 0.10 . 1 . . . . . . . . 5186 1 247 . 1 1 47 47 CYS H H 1 12.11 0.02 . 1 . . . . . . . . 5186 1 248 . 1 1 47 47 CYS HA H 1 4.29 0.02 . 1 . . . . . . . . 5186 1 249 . 1 1 47 47 CYS C C 13 175.18 0.20 . 1 . . . . . . . . 5186 1 250 . 1 1 47 47 CYS CA C 13 57.15 0.20 . 1 . . . . . . . . 5186 1 251 . 1 1 47 47 CYS CB C 13 39.80 0.20 . 1 . . . . . . . . 5186 1 252 . 1 1 47 47 CYS N N 15 125.81 0.10 . 1 . . . . . . . . 5186 1 253 . 1 1 48 48 GLY H H 1 8.40 0.02 . 1 . . . . . . . . 5186 1 254 . 1 1 48 48 GLY HA2 H 1 4.28 0.02 . 2 . . . . . . . . 5186 1 255 . 1 1 48 48 GLY HA3 H 1 3.61 0.02 . 2 . . . . . . . . 5186 1 256 . 1 1 48 48 GLY C C 13 170.56 0.20 . 1 . . . . . . . . 5186 1 257 . 1 1 48 48 GLY CA C 13 44.55 0.20 . 1 . . . . . . . . 5186 1 258 . 1 1 48 48 GLY N N 15 111.97 0.10 . 1 . . . . . . . . 5186 1 259 . 1 1 49 49 GLY H H 1 8.27 0.02 . 1 . . . . . . . . 5186 1 260 . 1 1 49 49 GLY HA2 H 1 4.53 0.02 . 2 . . . . . . . . 5186 1 261 . 1 1 49 49 GLY HA3 H 1 3.41 0.02 . 2 . . . . . . . . 5186 1 262 . 1 1 49 49 GLY C C 13 173.95 0.20 . 1 . . . . . . . . 5186 1 263 . 1 1 49 49 GLY CA C 13 44.98 0.20 . 1 . . . . . . . . 5186 1 264 . 1 1 49 49 GLY N N 15 103.94 0.10 . 1 . . . . . . . . 5186 1 265 . 1 1 50 50 CYS H H 1 8.09 0.02 . 1 . . . . . . . . 5186 1 266 . 1 1 50 50 CYS HA H 1 5.22 0.02 . 1 . . . . . . . . 5186 1 267 . 1 1 50 50 CYS C C 13 175.09 0.20 . 1 . . . . . . . . 5186 1 268 . 1 1 50 50 CYS CA C 13 53.17 0.20 . 1 . . . . . . . . 5186 1 269 . 1 1 50 50 CYS N N 15 111.56 0.10 . 1 . . . . . . . . 5186 1 270 . 1 1 52 52 ASN HA H 1 4.59 0.02 . 1 . . . . . . . . 5186 1 271 . 1 1 52 52 ASN C C 13 173.60 0.20 . 1 . . . . . . . . 5186 1 272 . 1 1 52 52 ASN CA C 13 55.60 0.20 . 1 . . . . . . . . 5186 1 273 . 1 1 52 52 ASN CB C 13 38.50 0.20 . 1 . . . . . . . . 5186 1 274 . 1 1 53 53 ASP H H 1 7.17 0.02 . 1 . . . . . . . . 5186 1 275 . 1 1 53 53 ASP HA H 1 4.71 0.02 . 1 . . . . . . . . 5186 1 276 . 1 1 53 53 ASP C C 13 176.40 0.20 . 1 . . . . . . . . 5186 1 277 . 1 1 53 53 ASP CA C 13 54.40 0.20 . 1 . . . . . . . . 5186 1 278 . 1 1 53 53 ASP N N 15 115.96 0.10 . 1 . . . . . . . . 5186 1 279 . 1 1 55 55 GLY H H 1 9.08 0.02 . 1 . . . . . . . . 5186 1 280 . 1 1 55 55 GLY HA2 H 1 4.14 0.02 . 2 . . . . . . . . 5186 1 281 . 1 1 55 55 GLY HA3 H 1 3.80 0.02 . 2 . . . . . . . . 5186 1 282 . 1 1 55 55 GLY C C 13 174.00 0.20 . 1 . . . . . . . . 5186 1 283 . 1 1 55 55 GLY N N 15 108.28 0.10 . 1 . . . . . . . . 5186 1 284 . 1 1 56 56 LEU H H 1 7.49 0.02 . 1 . . . . . . . . 5186 1 285 . 1 1 56 56 LEU HA H 1 4.96 0.02 . 1 . . . . . . . . 5186 1 286 . 1 1 56 56 LEU C C 13 175.16 0.20 . 1 . . . . . . . . 5186 1 287 . 1 1 56 56 LEU CA C 13 53.50 0.20 . 1 . . . . . . . . 5186 1 288 . 1 1 56 56 LEU CB C 13 45.80 0.20 . 1 . . . . . . . . 5186 1 289 . 1 1 56 56 LEU N N 15 119.62 0.10 . 1 . . . . . . . . 5186 1 290 . 1 1 57 57 GLU H H 1 9.16 0.02 . 1 . . . . . . . . 5186 1 291 . 1 1 57 57 GLU HA H 1 4.62 0.02 . 1 . . . . . . . . 5186 1 292 . 1 1 57 57 GLU C C 13 173.84 0.20 . 1 . . . . . . . . 5186 1 293 . 1 1 57 57 GLU CA C 13 53.91 0.20 . 1 . . . . . . . . 5186 1 294 . 1 1 57 57 GLU CB C 13 33.40 0.20 . 1 . . . . . . . . 5186 1 295 . 1 1 57 57 GLU N N 15 118.71 0.10 . 1 . . . . . . . . 5186 1 296 . 1 1 58 58 CYS H H 1 8.65 0.02 . 1 . . . . . . . . 5186 1 297 . 1 1 58 58 CYS HA H 1 4.76 0.02 . 1 . . . . . . . . 5186 1 298 . 1 1 58 58 CYS C C 13 173.89 0.20 . 1 . . . . . . . . 5186 1 299 . 1 1 58 58 CYS CA C 13 54.72 0.20 . 1 . . . . . . . . 5186 1 300 . 1 1 58 58 CYS CB C 13 36.30 0.20 . 1 . . . . . . . . 5186 1 301 . 1 1 58 58 CYS N N 15 123.06 0.10 . 1 . . . . . . . . 5186 1 302 . 1 1 59 59 VAL H H 1 8.93 0.02 . 1 . . . . . . . . 5186 1 303 . 1 1 59 59 VAL HA H 1 4.82 0.02 . 1 . . . . . . . . 5186 1 304 . 1 1 59 59 VAL C C 13 172.72 0.20 . 1 . . . . . . . . 5186 1 305 . 1 1 59 59 VAL CA C 13 57.97 0.20 . 1 . . . . . . . . 5186 1 306 . 1 1 59 59 VAL N N 15 124.18 0.10 . 1 . . . . . . . . 5186 1 307 . 1 1 60 60 PRO HA H 1 5.01 0.02 . 1 . . . . . . . . 5186 1 308 . 1 1 60 60 PRO C C 13 178.48 0.20 . 1 . . . . . . . . 5186 1 309 . 1 1 60 60 PRO CA C 13 62.50 0.20 . 1 . . . . . . . . 5186 1 310 . 1 1 61 61 THR H H 1 8.45 0.02 . 1 . . . . . . . . 5186 1 311 . 1 1 61 61 THR HA H 1 4.36 0.02 . 1 . . . . . . . . 5186 1 312 . 1 1 61 61 THR C C 13 175.17 0.20 . 1 . . . . . . . . 5186 1 313 . 1 1 61 61 THR CA C 13 61.24 0.20 . 1 . . . . . . . . 5186 1 314 . 1 1 61 61 THR CB C 13 69.10 0.20 . 1 . . . . . . . . 5186 1 315 . 1 1 61 61 THR N N 15 111.06 0.10 . 1 . . . . . . . . 5186 1 316 . 1 1 62 62 GLU H H 1 7.20 0.02 . 1 . . . . . . . . 5186 1 317 . 1 1 62 62 GLU HA H 1 4.54 0.02 . 1 . . . . . . . . 5186 1 318 . 1 1 62 62 GLU C C 13 175.06 0.20 . 1 . . . . . . . . 5186 1 319 . 1 1 62 62 GLU CA C 13 57.16 0.20 . 1 . . . . . . . . 5186 1 320 . 1 1 62 62 GLU CB C 13 34.40 0.20 . 1 . . . . . . . . 5186 1 321 . 1 1 62 62 GLU N N 15 120.90 0.10 . 1 . . . . . . . . 5186 1 322 . 1 1 63 63 GLU H H 1 8.82 0.02 . 1 . . . . . . . . 5186 1 323 . 1 1 63 63 GLU HA H 1 5.43 0.02 . 1 . . . . . . . . 5186 1 324 . 1 1 63 63 GLU C C 13 175.01 0.20 . 1 . . . . . . . . 5186 1 325 . 1 1 63 63 GLU CA C 13 55.24 0.20 . 1 . . . . . . . . 5186 1 326 . 1 1 63 63 GLU CB C 13 34.30 0.20 . 1 . . . . . . . . 5186 1 327 . 1 1 63 63 GLU N N 15 125.81 0.10 . 1 . . . . . . . . 5186 1 328 . 1 1 64 64 SER H H 1 8.82 0.02 . 1 . . . . . . . . 5186 1 329 . 1 1 64 64 SER HA H 1 4.69 0.02 . 1 . . . . . . . . 5186 1 330 . 1 1 64 64 SER C C 13 172.55 0.20 . 1 . . . . . . . . 5186 1 331 . 1 1 64 64 SER CA C 13 57.96 0.20 . 1 . . . . . . . . 5186 1 332 . 1 1 64 64 SER CB C 13 65.40 0.20 . 1 . . . . . . . . 5186 1 333 . 1 1 64 64 SER N N 15 113.59 0.10 . 1 . . . . . . . . 5186 1 334 . 1 1 65 65 ASN H H 1 8.52 0.02 . 1 . . . . . . . . 5186 1 335 . 1 1 65 65 ASN HA H 1 5.75 0.02 . 1 . . . . . . . . 5186 1 336 . 1 1 65 65 ASN C C 13 174.97 0.20 . 1 . . . . . . . . 5186 1 337 . 1 1 65 65 ASN CA C 13 53.07 0.20 . 1 . . . . . . . . 5186 1 338 . 1 1 65 65 ASN CB C 13 41.90 0.20 . 1 . . . . . . . . 5186 1 339 . 1 1 65 65 ASN N N 15 117.96 0.10 . 1 . . . . . . . . 5186 1 340 . 1 1 66 66 ILE H H 1 9.35 0.02 . 1 . . . . . . . . 5186 1 341 . 1 1 66 66 ILE HA H 1 4.68 0.02 . 1 . . . . . . . . 5186 1 342 . 1 1 66 66 ILE C C 13 172.86 0.20 . 1 . . . . . . . . 5186 1 343 . 1 1 66 66 ILE CA C 13 59.74 0.20 . 1 . . . . . . . . 5186 1 344 . 1 1 66 66 ILE CB C 13 42.60 0.20 . 1 . . . . . . . . 5186 1 345 . 1 1 66 66 ILE N N 15 122.65 0.10 . 1 . . . . . . . . 5186 1 346 . 1 1 67 67 THR H H 1 8.49 0.02 . 1 . . . . . . . . 5186 1 347 . 1 1 67 67 THR HA H 1 5.18 0.02 . 1 . . . . . . . . 5186 1 348 . 1 1 67 67 THR C C 13 173.48 0.20 . 1 . . . . . . . . 5186 1 349 . 1 1 67 67 THR CA C 13 62.18 0.20 . 1 . . . . . . . . 5186 1 350 . 1 1 67 67 THR CB C 13 69.80 0.20 . 1 . . . . . . . . 5186 1 351 . 1 1 67 67 THR N N 15 123.15 0.10 . 1 . . . . . . . . 5186 1 352 . 1 1 68 68 MET H H 1 9.21 0.02 . 1 . . . . . . . . 5186 1 353 . 1 1 68 68 MET HA H 1 5.09 0.02 . 1 . . . . . . . . 5186 1 354 . 1 1 68 68 MET C C 13 174.63 0.20 . 1 . . . . . . . . 5186 1 355 . 1 1 68 68 MET CA C 13 54.61 0.20 . 1 . . . . . . . . 5186 1 356 . 1 1 68 68 MET CB C 13 37.70 0.20 . 1 . . . . . . . . 5186 1 357 . 1 1 68 68 MET N N 15 123.68 0.10 . 1 . . . . . . . . 5186 1 358 . 1 1 69 69 GLN H H 1 8.15 0.02 . 1 . . . . . . . . 5186 1 359 . 1 1 69 69 GLN HA H 1 4.79 0.02 . 1 . . . . . . . . 5186 1 360 . 1 1 69 69 GLN C C 13 173.16 0.20 . 1 . . . . . . . . 5186 1 361 . 1 1 69 69 GLN CA C 13 55.86 0.20 . 1 . . . . . . . . 5186 1 362 . 1 1 69 69 GLN CB C 13 30.10 0.20 . 1 . . . . . . . . 5186 1 363 . 1 1 69 69 GLN N N 15 121.21 0.10 . 1 . . . . . . . . 5186 1 364 . 1 1 70 70 ILE H H 1 8.26 0.02 . 1 . . . . . . . . 5186 1 365 . 1 1 70 70 ILE HA H 1 4.67 0.02 . 1 . . . . . . . . 5186 1 366 . 1 1 70 70 ILE C C 13 176.46 0.20 . 1 . . . . . . . . 5186 1 367 . 1 1 70 70 ILE CA C 13 57.73 0.20 . 1 . . . . . . . . 5186 1 368 . 1 1 70 70 ILE CB C 13 41.80 0.20 . 1 . . . . . . . . 5186 1 369 . 1 1 70 70 ILE N N 15 119.97 0.10 . 1 . . . . . . . . 5186 1 370 . 1 1 71 71 MET H H 1 8.91 0.02 . 1 . . . . . . . . 5186 1 371 . 1 1 71 71 MET HA H 1 4.59 0.02 . 1 . . . . . . . . 5186 1 372 . 1 1 71 71 MET C C 13 174.08 0.20 . 1 . . . . . . . . 5186 1 373 . 1 1 71 71 MET CA C 13 55.98 0.20 . 1 . . . . . . . . 5186 1 374 . 1 1 71 71 MET CB C 13 34.10 0.20 . 1 . . . . . . . . 5186 1 375 . 1 1 71 71 MET N N 15 126.62 0.10 . 1 . . . . . . . . 5186 1 376 . 1 1 72 72 ARG H H 1 8.80 0.02 . 1 . . . . . . . . 5186 1 377 . 1 1 72 72 ARG HA H 1 4.67 0.02 . 1 . . . . . . . . 5186 1 378 . 1 1 72 72 ARG C C 13 175.44 0.20 . 1 . . . . . . . . 5186 1 379 . 1 1 72 72 ARG CA C 13 55.43 0.20 . 1 . . . . . . . . 5186 1 380 . 1 1 72 72 ARG CB C 13 32.50 0.20 . 1 . . . . . . . . 5186 1 381 . 1 1 72 72 ARG N N 15 127.62 0.10 . 1 . . . . . . . . 5186 1 382 . 1 1 73 73 ILE H H 1 9.20 0.02 . 1 . . . . . . . . 5186 1 383 . 1 1 73 73 ILE HA H 1 4.37 0.02 . 1 . . . . . . . . 5186 1 384 . 1 1 73 73 ILE C C 13 175.21 0.20 . 1 . . . . . . . . 5186 1 385 . 1 1 73 73 ILE CA C 13 61.39 0.20 . 1 . . . . . . . . 5186 1 386 . 1 1 73 73 ILE CB C 13 40.70 0.20 . 1 . . . . . . . . 5186 1 387 . 1 1 73 73 ILE N N 15 126.23 0.10 . 1 . . . . . . . . 5186 1 388 . 1 1 74 74 LYS H H 1 8.40 0.02 . 1 . . . . . . . . 5186 1 389 . 1 1 74 74 LYS HA H 1 4.96 0.02 . 1 . . . . . . . . 5186 1 390 . 1 1 74 74 LYS C C 13 174.55 0.20 . 1 . . . . . . . . 5186 1 391 . 1 1 74 74 LYS CA C 13 52.95 0.20 . 1 . . . . . . . . 5186 1 392 . 1 1 74 74 LYS N N 15 128.56 0.10 . 1 . . . . . . . . 5186 1 393 . 1 1 76 76 HIS HA H 1 4.25 0.02 . 1 . . . . . . . . 5186 1 394 . 1 1 76 76 HIS C C 13 175.20 0.20 . 1 . . . . . . . . 5186 1 395 . 1 1 76 76 HIS CA C 13 58.30 0.20 . 1 . . . . . . . . 5186 1 396 . 1 1 76 76 HIS CB C 13 29.30 0.20 . 1 . . . . . . . . 5186 1 397 . 1 1 77 77 GLN H H 1 8.26 0.02 . 1 . . . . . . . . 5186 1 398 . 1 1 77 77 GLN HA H 1 4.61 0.02 . 1 . . . . . . . . 5186 1 399 . 1 1 77 77 GLN C C 13 175.80 0.20 . 1 . . . . . . . . 5186 1 400 . 1 1 77 77 GLN CA C 13 56.60 0.20 . 1 . . . . . . . . 5186 1 401 . 1 1 77 77 GLN CB C 13 31.50 0.20 . 1 . . . . . . . . 5186 1 402 . 1 1 77 77 GLN N N 15 118.77 0.10 . 1 . . . . . . . . 5186 1 403 . 1 1 78 78 GLY H H 1 8.16 0.02 . 1 . . . . . . . . 5186 1 404 . 1 1 78 78 GLY HA2 H 1 4.22 0.02 . 2 . . . . . . . . 5186 1 405 . 1 1 78 78 GLY HA3 H 1 3.94 0.02 . 2 . . . . . . . . 5186 1 406 . 1 1 78 78 GLY C C 13 172.06 0.20 . 1 . . . . . . . . 5186 1 407 . 1 1 78 78 GLY CA C 13 45.71 0.20 . 1 . . . . . . . . 5186 1 408 . 1 1 78 78 GLY N N 15 107.78 0.10 . 1 . . . . . . . . 5186 1 409 . 1 1 79 79 GLN H H 1 8.14 0.02 . 1 . . . . . . . . 5186 1 410 . 1 1 79 79 GLN HA H 1 5.24 0.02 . 1 . . . . . . . . 5186 1 411 . 1 1 79 79 GLN C C 13 174.60 0.20 . 1 . . . . . . . . 5186 1 412 . 1 1 79 79 GLN CA C 13 54.30 0.20 . 1 . . . . . . . . 5186 1 413 . 1 1 79 79 GLN CB C 13 32.60 0.20 . 1 . . . . . . . . 5186 1 414 . 1 1 79 79 GLN N N 15 116.81 0.10 . 1 . . . . . . . . 5186 1 415 . 1 1 80 80 HIS H H 1 8.38 0.02 . 1 . . . . . . . . 5186 1 416 . 1 1 80 80 HIS HA H 1 4.74 0.02 . 1 . . . . . . . . 5186 1 417 . 1 1 80 80 HIS C C 13 173.60 0.20 . 1 . . . . . . . . 5186 1 418 . 1 1 80 80 HIS CA C 13 56.00 0.20 . 1 . . . . . . . . 5186 1 419 . 1 1 80 80 HIS N N 15 118.96 0.10 . 1 . . . . . . . . 5186 1 420 . 1 1 81 81 ILE H H 1 8.49 0.02 . 1 . . . . . . . . 5186 1 421 . 1 1 81 81 ILE HA H 1 4.30 0.02 . 1 . . . . . . . . 5186 1 422 . 1 1 81 81 ILE C C 13 175.70 0.20 . 1 . . . . . . . . 5186 1 423 . 1 1 81 81 ILE CA C 13 61.20 0.20 . 1 . . . . . . . . 5186 1 424 . 1 1 81 81 ILE CB C 13 37.80 0.20 . 1 . . . . . . . . 5186 1 425 . 1 1 81 81 ILE N N 15 124.33 0.10 . 1 . . . . . . . . 5186 1 426 . 1 1 82 82 GLY H H 1 8.61 0.02 . 1 . . . . . . . . 5186 1 427 . 1 1 82 82 GLY HA2 H 1 4.56 0.02 . 2 . . . . . . . . 5186 1 428 . 1 1 82 82 GLY HA3 H 1 3.60 0.02 . 2 . . . . . . . . 5186 1 429 . 1 1 82 82 GLY C C 13 171.76 0.20 . 1 . . . . . . . . 5186 1 430 . 1 1 82 82 GLY CA C 13 44.16 0.20 . 1 . . . . . . . . 5186 1 431 . 1 1 82 82 GLY N N 15 115.93 0.10 . 1 . . . . . . . . 5186 1 432 . 1 1 83 83 GLU H H 1 8.23 0.02 . 1 . . . . . . . . 5186 1 433 . 1 1 83 83 GLU HA H 1 4.75 0.02 . 1 . . . . . . . . 5186 1 434 . 1 1 83 83 GLU C C 13 176.75 0.20 . 1 . . . . . . . . 5186 1 435 . 1 1 83 83 GLU CA C 13 56.30 0.20 . 1 . . . . . . . . 5186 1 436 . 1 1 83 83 GLU CB C 13 31.50 0.20 . 1 . . . . . . . . 5186 1 437 . 1 1 83 83 GLU N N 15 119.14 0.10 . 1 . . . . . . . . 5186 1 438 . 1 1 84 84 MET H H 1 9.03 0.02 . 1 . . . . . . . . 5186 1 439 . 1 1 84 84 MET HA H 1 4.46 0.02 . 1 . . . . . . . . 5186 1 440 . 1 1 84 84 MET C C 13 173.73 0.20 . 1 . . . . . . . . 5186 1 441 . 1 1 84 84 MET CA C 13 55.47 0.20 . 1 . . . . . . . . 5186 1 442 . 1 1 84 84 MET CB C 13 38.10 0.20 . 1 . . . . . . . . 5186 1 443 . 1 1 84 84 MET N N 15 123.24 0.10 . 1 . . . . . . . . 5186 1 444 . 1 1 85 85 SER H H 1 7.90 0.02 . 1 . . . . . . . . 5186 1 445 . 1 1 85 85 SER HA H 1 5.40 0.02 . 1 . . . . . . . . 5186 1 446 . 1 1 85 85 SER C C 13 173.83 0.20 . 1 . . . . . . . . 5186 1 447 . 1 1 85 85 SER CA C 13 57.20 0.20 . 1 . . . . . . . . 5186 1 448 . 1 1 85 85 SER CB C 13 62.20 0.20 . 1 . . . . . . . . 5186 1 449 . 1 1 85 85 SER N N 15 116.50 0.10 . 1 . . . . . . . . 5186 1 450 . 1 1 86 86 PHE H H 1 9.27 0.02 . 1 . . . . . . . . 5186 1 451 . 1 1 86 86 PHE HA H 1 4.91 0.02 . 1 . . . . . . . . 5186 1 452 . 1 1 86 86 PHE C C 13 174.34 0.20 . 1 . . . . . . . . 5186 1 453 . 1 1 86 86 PHE CA C 13 57.00 0.20 . 1 . . . . . . . . 5186 1 454 . 1 1 86 86 PHE CB C 13 45.90 0.20 . 1 . . . . . . . . 5186 1 455 . 1 1 86 86 PHE N N 15 122.71 0.10 . 1 . . . . . . . . 5186 1 456 . 1 1 87 87 LEU H H 1 8.96 0.02 . 1 . . . . . . . . 5186 1 457 . 1 1 87 87 LEU HA H 1 4.82 0.02 . 1 . . . . . . . . 5186 1 458 . 1 1 87 87 LEU C C 13 176.96 0.20 . 1 . . . . . . . . 5186 1 459 . 1 1 87 87 LEU CA C 13 55.39 0.20 . 1 . . . . . . . . 5186 1 460 . 1 1 87 87 LEU CB C 13 44.40 0.20 . 1 . . . . . . . . 5186 1 461 . 1 1 87 87 LEU N N 15 123.15 0.10 . 1 . . . . . . . . 5186 1 462 . 1 1 88 88 GLN H H 1 9.41 0.02 . 1 . . . . . . . . 5186 1 463 . 1 1 88 88 GLN HA H 1 4.70 0.02 . 1 . . . . . . . . 5186 1 464 . 1 1 88 88 GLN C C 13 174.06 0.20 . 1 . . . . . . . . 5186 1 465 . 1 1 88 88 GLN CA C 13 54.66 0.20 . 1 . . . . . . . . 5186 1 466 . 1 1 88 88 GLN CB C 13 33.10 0.20 . 1 . . . . . . . . 5186 1 467 . 1 1 88 88 GLN N N 15 122.71 0.10 . 1 . . . . . . . . 5186 1 468 . 1 1 89 89 HIS H H 1 8.48 0.02 . 1 . . . . . . . . 5186 1 469 . 1 1 89 89 HIS HA H 1 5.16 0.02 . 1 . . . . . . . . 5186 1 470 . 1 1 89 89 HIS C C 13 174.34 0.20 . 1 . . . . . . . . 5186 1 471 . 1 1 89 89 HIS CA C 13 52.86 0.20 . 1 . . . . . . . . 5186 1 472 . 1 1 89 89 HIS CB C 13 34.00 0.20 . 1 . . . . . . . . 5186 1 473 . 1 1 89 89 HIS N N 15 120.80 0.10 . 1 . . . . . . . . 5186 1 474 . 1 1 90 90 ASN H H 1 8.60 0.02 . 1 . . . . . . . . 5186 1 475 . 1 1 90 90 ASN HA H 1 4.69 0.02 . 1 . . . . . . . . 5186 1 476 . 1 1 90 90 ASN C C 13 175.01 0.20 . 1 . . . . . . . . 5186 1 477 . 1 1 90 90 ASN CA C 13 54.23 0.20 . 1 . . . . . . . . 5186 1 478 . 1 1 90 90 ASN CB C 13 40.70 0.20 . 1 . . . . . . . . 5186 1 479 . 1 1 90 90 ASN N N 15 119.37 0.10 . 1 . . . . . . . . 5186 1 480 . 1 1 91 91 LYS H H 1 7.59 0.02 . 1 . . . . . . . . 5186 1 481 . 1 1 91 91 LYS HA H 1 4.39 0.02 . 1 . . . . . . . . 5186 1 482 . 1 1 91 91 LYS C C 13 175.29 0.20 . 1 . . . . . . . . 5186 1 483 . 1 1 91 91 LYS CA C 13 56.50 0.20 . 1 . . . . . . . . 5186 1 484 . 1 1 91 91 LYS CB C 13 37.60 0.20 . 1 . . . . . . . . 5186 1 485 . 1 1 91 91 LYS N N 15 117.65 0.10 . 1 . . . . . . . . 5186 1 486 . 1 1 92 92 CYS H H 1 8.80 0.02 . 1 . . . . . . . . 5186 1 487 . 1 1 92 92 CYS HA H 1 5.46 0.02 . 1 . . . . . . . . 5186 1 488 . 1 1 92 92 CYS C C 13 173.21 0.20 . 1 . . . . . . . . 5186 1 489 . 1 1 92 92 CYS CA C 13 54.47 0.20 . 1 . . . . . . . . 5186 1 490 . 1 1 92 92 CYS CB C 13 48.50 0.20 . 1 . . . . . . . . 5186 1 491 . 1 1 92 92 CYS N N 15 121.90 0.10 . 1 . . . . . . . . 5186 1 492 . 1 1 93 93 GLU H H 1 9.31 0.02 . 1 . . . . . . . . 5186 1 493 . 1 1 93 93 GLU HA H 1 4.57 0.02 . 1 . . . . . . . . 5186 1 494 . 1 1 93 93 GLU C C 13 174.24 0.20 . 1 . . . . . . . . 5186 1 495 . 1 1 93 93 GLU CA C 13 55.17 0.20 . 1 . . . . . . . . 5186 1 496 . 1 1 93 93 GLU CB C 13 35.50 0.20 . 1 . . . . . . . . 5186 1 497 . 1 1 93 93 GLU N N 15 121.12 0.10 . 1 . . . . . . . . 5186 1 498 . 1 1 94 94 CYS H H 1 8.44 0.02 . 1 . . . . . . . . 5186 1 499 . 1 1 94 94 CYS HA H 1 5.23 0.02 . 1 . . . . . . . . 5186 1 500 . 1 1 94 94 CYS C C 13 174.65 0.20 . 1 . . . . . . . . 5186 1 501 . 1 1 94 94 CYS CA C 13 56.96 0.20 . 1 . . . . . . . . 5186 1 502 . 1 1 94 94 CYS CB C 13 44.80 0.20 . 1 . . . . . . . . 5186 1 503 . 1 1 94 94 CYS N N 15 120.12 0.10 . 1 . . . . . . . . 5186 1 504 . 1 1 95 95 ARG H H 1 9.23 0.02 . 1 . . . . . . . . 5186 1 505 . 1 1 95 95 ARG HA H 1 4.92 0.02 . 1 . . . . . . . . 5186 1 506 . 1 1 95 95 ARG C C 13 173.43 0.20 . 1 . . . . . . . . 5186 1 507 . 1 1 95 95 ARG CA C 13 53.20 0.20 . 1 . . . . . . . . 5186 1 508 . 1 1 95 95 ARG N N 15 126.12 0.10 . 1 . . . . . . . . 5186 1 509 . 1 1 96 96 PRO HA H 1 4.66 0.02 . 1 . . . . . . . . 5186 1 510 . 1 1 96 96 PRO C C 13 177.24 0.20 . 1 . . . . . . . . 5186 1 511 . 1 1 96 96 PRO CA C 13 63.60 0.20 . 1 . . . . . . . . 5186 1 512 . 1 1 96 96 PRO CB C 13 32.40 0.20 . 1 . . . . . . . . 5186 1 513 . 1 1 97 97 LYS H H 1 8.11 0.02 . 1 . . . . . . . . 5186 1 514 . 1 1 97 97 LYS HA H 1 4.07 0.02 . 1 . . . . . . . . 5186 1 515 . 1 1 97 97 LYS C C 13 176.43 0.20 . 1 . . . . . . . . 5186 1 516 . 1 1 97 97 LYS CA C 13 57.25 0.20 . 1 . . . . . . . . 5186 1 517 . 1 1 97 97 LYS CB C 13 34.00 0.20 . 1 . . . . . . . . 5186 1 518 . 1 1 97 97 LYS N N 15 124.06 0.10 . 1 . . . . . . . . 5186 1 519 . 1 1 98 98 LYS H H 1 8.38 0.02 . 1 . . . . . . . . 5186 1 520 . 1 1 98 98 LYS HA H 1 4.31 0.02 . 1 . . . . . . . . 5186 1 521 . 1 1 98 98 LYS C C 13 175.33 0.20 . 1 . . . . . . . . 5186 1 522 . 1 1 98 98 LYS CA C 13 56.59 0.20 . 1 . . . . . . . . 5186 1 523 . 1 1 98 98 LYS CB C 13 33.70 0.20 . 1 . . . . . . . . 5186 1 524 . 1 1 98 98 LYS N N 15 123.59 0.10 . 1 . . . . . . . . 5186 1 525 . 1 1 99 99 ASP H H 1 7.84 0.02 . 1 . . . . . . . . 5186 1 526 . 1 1 99 99 ASP HA H 1 4.36 0.02 . 1 . . . . . . . . 5186 1 527 . 1 1 99 99 ASP C C 13 180.79 0.20 . 1 . . . . . . . . 5186 1 528 . 1 1 99 99 ASP CA C 13 56.20 0.20 . 1 . . . . . . . . 5186 1 529 . 1 1 99 99 ASP N N 15 127.24 0.10 . 1 . . . . . . . . 5186 1 stop_ save_