data_10010 save_study_list _Study_list.Sf_category study_list _Study_list.Sf_framecode study_list _Study_list.Entry_ID 10010 _Study_list.ID 1 loop_ _Study.ID _Study.Name _Study.Type _Study.Details _Study.Entry_ID _Study.Study_list_ID 1 'NMR measurement of bovine beta-lactoglobulin at neutral pH' 'Structure analysis' . 10010 1 stop_ loop_ _Study_keyword.Study_ID _Study_keyword.Keyword _Study_keyword.Entry_ID _Study_keyword.Study_list_ID 1 beta-lactoglobulin 10010 1 stop_ save_ ####################### # Entry information # ####################### save_entry_information _Entry.Sf_category entry_information _Entry.Sf_framecode entry_information _Entry.ID 10010 _Entry.Title ; bovine beta-lactoglobulin A34C mutant ; _Entry.Type macromolecule _Entry.Version_type original _Entry.Submission_date 2005-10-31 _Entry.Accession_date 2005-11-01 _Entry.Last_release_date 2007-06-13 _Entry.Original_release_date 2007-06-13 _Entry.Origination author _Entry.NMR_STAR_version 3.1.1.61 _Entry.Original_NMR_STAR_version 3.1 _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 Kazumasa Sakurai . . . 10010 2 Yuji Goto . . . 10010 stop_ loop_ _Entry_src.ID _Entry_src.Project_name _Entry_src.Organization_full_name _Entry_src.Organization_initials _Entry_src.Entry_ID 1 . ; Laboratory of Protein Folding, Inst. Protein Res., Osaka-Univ. ; . 10010 stop_ loop_ _Data_set.Type _Data_set.Count _Data_set.Entry_ID assigned_chemical_shifts 1 10010 stop_ loop_ _Datum.Type _Datum.Count _Datum.Entry_ID '13C chemical shifts' 463 10010 '15N chemical shifts' 147 10010 '1H chemical shifts' 147 10010 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 . . 2007-06-13 2005-10-31 original author . 10010 stop_ save_ ############### # Citations # ############### save_citation_1 _Citation.Sf_category citations _Citation.Sf_framecode citation_1 _Citation.Entry_ID 10010 _Citation.ID 1 _Citation.Class 'entry citation' _Citation.CAS_abstract_code . _Citation.MEDLINE_UI_code . _Citation.DOI . _Citation.PubMed_ID 16368109 _Citation.Full_citation . _Citation.Title ; Dynamics and Mechanism of the Tanford Transition of Bovine beta-Lactoglobulin Studied using Heteronuclear NMR Spectroscopy ; _Citation.Status published _Citation.Type journal _Citation.Journal_abbrev 'J. Mol. Biol.' _Citation.Journal_name_full . _Citation.Journal_volume 356 _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 483 _Citation.Page_last 496 _Citation.Year 2006 _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 Kazumasa Sakurai . . . 10010 1 2 Yuji Goto . . . 10010 1 stop_ save_ save_citation_2 _Citation.Sf_category citations _Citation.Sf_framecode citation_2 _Citation.Entry_ID 10010 _Citation.ID 2 _Citation.Class 'reference citation' _Citation.CAS_abstract_code . _Citation.MEDLINE_UI_code . _Citation.DOI . _Citation.PubMed_ID 9514124 _Citation.Full_citation ; Kim, T.-R., Goto, Y., Hirota, N., Kuwata, K., Denton, H., Wu, S.-Y., Sawyer, L., and Batt, C.A. (1997) High-level expression of bovine beta-lactoglobulin in Pichia pastoris and characterization of its physical properties. Protein Eng. 10:1339-1345. ; _Citation.Title ; High-level expression of bovine beta-lactoglobulin in Pichia pastoris and characterization of its physical properties. ; _Citation.Status published _Citation.Type journal _Citation.Journal_abbrev 'Protein Eng.' _Citation.Journal_name_full . _Citation.Journal_volume 10 _Citation.Journal_issue 11 _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 1339 _Citation.Page_last 1345 _Citation.Year 1997 _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 Tae-Rak Kim . . . 10010 2 2 Yuji Goto . . . 10010 2 3 Nami Hirota . . . 10010 2 4 Kazuo Kuwata . . . 10010 2 5 Helen Denton . . . 10010 2 6 Su-Ying Wu . . . 10010 2 7 Lindsay Sawyer . . . 10010 2 8 Carl Batt . A. . 10010 2 stop_ save_ save_citation_3 _Citation.Sf_category citations _Citation.Sf_framecode citation_3 _Citation.Entry_ID 10010 _Citation.ID 3 _Citation.Class 'reference citation' _Citation.CAS_abstract_code . _Citation.MEDLINE_UI_code . _Citation.DOI . _Citation.PubMed_ID 9790836 _Citation.Full_citation ; Kuwata, K., Hoshino, M., Era, S., Batt, C.A., and Goto, Y. (1998) alpha to beta Transition of beta-lactoglobulin as evidenced by heteronuclear NMR. J. Mol. Biol. 283: 731-739. ; _Citation.Title 'alpha to beta Transition of beta-lactoglobulin as evidenced by heteronuclear NMR.' _Citation.Status published _Citation.Type journal _Citation.Journal_abbrev 'J. Mol. Biol.' _Citation.Journal_name_full . _Citation.Journal_volume 283 _Citation.Journal_issue 4 _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 731 _Citation.Page_last 739 _Citation.Year 1998 _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 Kazuo Kuwata . . . 10010 3 2 Masaru Hoshino . . . 10010 3 3 Seiichi Era . . . 10010 3 4 Carl Batt . A. . 10010 3 5 Yuji Goto . . . 10010 3 stop_ save_ save_citation_4 _Citation.Sf_category citations _Citation.Sf_framecode citation_4 _Citation.Entry_ID 10010 _Citation.ID 4 _Citation.Class 'reference citation' _Citation.CAS_abstract_code . _Citation.MEDLINE_UI_code . _Citation.DOI . _Citation.PubMed_ID 9729790 _Citation.Full_citation ; Uhrinova, S., Uhrin, D., Denton, H., Smith, M., Sawyer, L., and Barlow, P.N. (1998) Complete assignment of 1H, 13C and 15N chemical shifts for bovine beta-lactoglobulin: Secondary structure and topology of the native state is retained in a partially unfolded form. J. Biomol. NMR 12: 89-107. ; _Citation.Title ; Complete assignment of 1H, 13C and 15N chemical shifts for bovine beta-lactoglobulin: Secondary structure and topology of the native state is retained in a partially unfolded form. ; _Citation.Status published _Citation.Type journal _Citation.Journal_abbrev 'J. Biomol. NMR' _Citation.Journal_name_full . _Citation.Journal_volume 12 _Citation.Journal_issue 1 _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 89 _Citation.Page_last 107 _Citation.Year 1998 _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 Stanislava Uhrinova . . . 10010 4 2 Dusan Uhrin . . . 10010 4 3 Helen Denton . . . 10010 4 4 Mark Smith . . . 10010 4 5 Lindsay Sawyer . . . 10010 4 6 Paul Barlow . N. . 10010 4 stop_ save_ ############################################# # Molecular system (assembly) description # ############################################# save_assembly _Assembly.Sf_category assembly _Assembly.Sf_framecode assembly _Assembly.Entry_ID 10010 _Assembly.ID 1 _Assembly.Name 'bovine beta-lactoglobulin A34C; disulfide linked dimer' _Assembly.BMRB_code . _Assembly.Number_of_components 2 _Assembly.Organic_ligands 0 _Assembly.Metal_ions 0 _Assembly.Non_standard_bonds . _Assembly.Ambiguous_conformational_states no _Assembly.Ambiguous_chem_comp_sites no _Assembly.Molecules_in_chemical_exchange no _Assembly.Paramagnetic no _Assembly.Thiol_state 'all disulfide bound' _Assembly.Molecular_mass 37000 _Assembly.Enzyme_commission_number . _Assembly.Details ; This sample is a symmetric homodimer, in which the same residues in each monomer generate the same signals, thus the spectrum seems of the monomer. ; _Assembly.DB_query_date . _Assembly.DB_query_revised_last_date . loop_ _Assembly_type.Type _Assembly_type.Entry_ID _Assembly_type.Assembly_ID 'protein-protein complex' 10010 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 'BLG A34C, 1' 1 $BLG_A34C . . yes native no no 1 . . 10010 1 2 'BLG A34C, 2' 1 $BLG_A34C . . yes native no no 1 . . 10010 1 stop_ loop_ _Bond.ID _Bond.Type _Bond.Value_order _Bond.Assembly_atom_ID_1 _Bond.Entity_assembly_ID_1 _Bond.Entity_assembly_name_1 _Bond.Entity_ID_1 _Bond.Comp_ID_1 _Bond.Comp_index_ID_1 _Bond.Seq_ID_1 _Bond.Atom_ID_1 _Bond.Assembly_atom_ID_2 _Bond.Entity_assembly_ID_2 _Bond.Entity_assembly_name_2 _Bond.Entity_ID_2 _Bond.Comp_ID_2 _Bond.Comp_index_ID_2 _Bond.Seq_ID_2 _Bond.Atom_ID_2 _Bond.Auth_entity_assembly_ID_1 _Bond.Auth_entity_assembly_name_1 _Bond.Auth_seq_ID_1 _Bond.Auth_comp_ID_1 _Bond.Auth_atom_ID_1 _Bond.Auth_entity_assembly_ID_2 _Bond.Auth_entity_assembly_name_2 _Bond.Auth_seq_ID_2 _Bond.Auth_comp_ID_2 _Bond.Auth_atom_ID_2 _Bond.Entry_ID _Bond.Assembly_ID 1 disulfide single . 1 . 1 CYS 69 69 SG . 1 . 1 CYS 163 163 SG . . . . . . . . . . 10010 1 2 disulfide single . 1 . 1 CYS 109 109 SG . 1 . 1 CYS 122 122 SG . . . . . . . . . . 10010 1 3 disulfide single . 1 . 1 CYS 37 37 SG . 2 . 1 CYS 37 37 SG . . . . . . . . . . 10010 1 4 disulfide single . 2 . 1 CYS 69 69 SG . 2 . 1 CYS 163 163 SG . . . . . . . . . . 10010 1 5 disulfide single . 2 . 1 CYS 109 109 SG . 2 . 1 CYS 122 122 SG . . . . . . . . . . 10010 1 stop_ loop_ _Entity_deleted_atom.ID _Entity_deleted_atom.Entity_atom_list_ID _Entity_deleted_atom.Entity_assembly_ID _Entity_deleted_atom.Entity_ID _Entity_deleted_atom.Comp_ID _Entity_deleted_atom.Comp_index_ID _Entity_deleted_atom.Seq_ID _Entity_deleted_atom.Atom_ID _Entity_deleted_atom.Auth_entity_assembly_ID _Entity_deleted_atom.Auth_seq_ID _Entity_deleted_atom.Auth_comp_ID _Entity_deleted_atom.Auth_atom_ID _Entity_deleted_atom.Entry_ID _Entity_deleted_atom.Assembly_ID 1 . 1 1 CYS 37 37 HG . . . . 10010 1 2 . 1 1 CYS 69 69 HG . . . . 10010 1 3 . 1 1 CYS 109 109 HG . . . . 10010 1 4 . 1 1 CYS 122 122 HG . . . . 10010 1 5 . 1 1 CYS 163 163 HG . . . . 10010 1 6 . 2 1 CYS 37 37 HG . . . . 10010 1 7 . 2 1 CYS 69 69 HG . . . . 10010 1 8 . 2 1 CYS 109 109 HG . . . . 10010 1 9 . 2 1 CYS 122 122 HG . . . . 10010 1 10 . 2 1 CYS 163 163 HG . . . . 10010 1 stop_ save_ #################################### # Biological polymers and ligands # #################################### save_BLG_A34C _Entity.Sf_category entity _Entity.Sf_framecode BLG_A34C _Entity.Entry_ID 10010 _Entity.ID 1 _Entity.BMRB_code . _Entity.Name BLG_A34C _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 ; EAEAYVTQTMKGLDIQKVAG TWYSLAMAASDISLLDCQSA PLRVYVEELKPTPEGDLEIL LQKWENDECAQKKIIAEKTK IPAVFKIDALNENKVLVLDT DYKKYLLFCMENSAEPEQSL VCQCLVRTPEVDDEALEKFD KALKALPMHIRLSFNPTQLE EQCHI ; _Entity.Polymer_seq_one_letter_code ; EAEAYVTQTMKGLDIQKVAG TWYSLAMAASDISLLDCQSA PLRVYVEELKPTPEGDLEIL LQKWENDECAQKKIIAEKTK IPAVFKIDALNENKVLVLDT DYKKYLLFCMENSAEPEQSL VCQCLVRTPEVDDEALEKFD KALKALPMHIRLSFNPTQLE EQCHI ; _Entity.Target_identifier . _Entity.Polymer_author_defined_seq . _Entity.Polymer_author_seq_details ; The first three residues are signal sequence necessary for the expression. The native sequence numbering starts at the forth residue. -3 EAE -1 1 AYVTQ TMKGL DIQKV AGTWY 20 21 SLAMA ASDIS LLDAQ SAPLR 40 41 VYVEE LKPTP EGDLE ILLQK 60 61 WENDE CAQKK IIAEK TKIPA 80 81 VFKID ALNEN KVLVL DTDYK 100 101 KYLLF CMENS AEPEQ SLVCQ 120 121 CLVRT PEVDD EALEK FDKAL 140 141 KALPM HIRLS FNPTQ LEEQC 160 161 HI 162 ; _Entity.Ambiguous_conformational_states no _Entity.Ambiguous_chem_comp_sites no _Entity.Nstd_monomer no _Entity.Nstd_chirality no _Entity.Nstd_linkage no _Entity.Nonpolymer_comp_ID . _Entity.Nonpolymer_comp_label . _Entity.Number_of_monomers 165 _Entity.Number_of_nonpolymer_components . _Entity.Paramagnetic no _Entity.Thiol_state 'free and bound' _Entity.Src_method . _Entity.Parent_entity_ID 1 _Entity.Fragment . _Entity.Mutation . _Entity.EC_number . _Entity.Calc_isoelectric_point . _Entity.Formula_weight 18400 _Entity.Formula_weight_exptl . _Entity.Formula_weight_exptl_meth . _Entity.Details . _Entity.DB_query_date . _Entity.DB_query_revised_last_date 2015-11-26 loop_ _Entity_db_link.Ordinal _Entity_db_link.Author_supplied _Entity_db_link.Database_code _Entity_db_link.Accession_code _Entity_db_link.Entry_mol_code _Entity_db_link.Entry_mol_name _Entity_db_link.Entry_experimental_method _Entity_db_link.Entry_structure_resolution _Entity_db_link.Entry_relation_type _Entity_db_link.Entry_details _Entity_db_link.Chimera_segment_ID _Entity_db_link.Seq_query_to_submitted_percent _Entity_db_link.Seq_subject_length _Entity_db_link.Seq_identity _Entity_db_link.Seq_positive _Entity_db_link.Seq_homology_expectation_val _Entity_db_link.Seq_align_begin _Entity_db_link.Seq_align_end _Entity_db_link.Seq_difference_details _Entity_db_link.Seq_alignment_details _Entity_db_link.Entry_ID _Entity_db_link.Entity_ID 1 no PDB 1B0O . "Bovine Beta-Lactoglobulin Complexed With Palmitate, Lattice Z" . . . . . 96.97 162 98.13 98.13 5.00e-109 . . . . 10010 1 2 no PDB 1B8E . "High Resolution Crystal Structure Of The Bovine Beta- Lactoglobulin (Isoforms A And B) In Orthorombic Space Group" . . . . . 96.97 162 98.13 98.13 5.00e-109 . . . . 10010 1 3 no PDB 1BEB . "Bovine Beta-Lactoglobulin, Lattice X" . . . . . 96.97 162 98.75 98.75 1.04e-109 . . . . 10010 1 4 no PDB 1BSO . "12-Bromododecanoic Acid Binds Inside The Calyx Of Bovine Beta-Lactoglobulin" . . . . . 96.97 162 99.38 99.38 1.39e-110 . . . . 10010 1 5 no PDB 1BSQ . "Structural And Functional Consequences Of Point Mutations Of Variants A And B Of Bovine Beta-Lactoglobulin" . . . . . 96.97 162 98.13 98.13 5.00e-109 . . . . 10010 1 6 no PDB 1BSY . "Structural Basis Of The Tanford Transition Of Bovine Beta- Lactoglobulin From Crystal Structures At Three Ph Values; Ph 7.1" . . . . . 96.97 162 99.38 99.38 1.39e-110 . . . . 10010 1 7 no PDB 1CJ5 . "Bovine Beta-Lactoglobulin A" . . . . . 98.18 162 99.38 99.38 1.89e-112 . . . . 10010 1 8 no PDB 1DV9 . "Structural Changes Accompanying Ph-Induced Dissociation Of The B-Lactoglobulin Dimer" . . . . . 98.18 162 99.38 99.38 1.89e-112 . . . . 10010 1 9 no PDB 1GX8 . "Bovine Beta-Lactoglobulin Complexed With Retinol, Trigonal Lattice Z" . . . . . 96.97 162 98.13 98.13 5.00e-109 . . . . 10010 1 10 no PDB 1GX9 . "Bovine Beta-Lactoglobulin Complexed With Retinoic Acid, Trigonal Lattice Z" . . . . . 96.97 162 98.13 98.13 5.00e-109 . . . . 10010 1 11 no PDB 1GXA . "Bovine Beta-Lactoglobulin Complexed With Retinol And Palmitic Acid, Trigonal Lattice Z" . . . . . 96.97 162 98.13 98.13 5.00e-109 . . . . 10010 1 12 no PDB 1QG5 . "High Resolution Crystal Structure Of The Bovine Beta- Lactoglobulin (Isoform A)" . . . . . 96.97 162 99.38 99.38 1.39e-110 . . . . 10010 1 13 no PDB 1UZ2 . "The Cys121ser Mutant Of Beta-lactoglobulin" . . . . . 96.97 162 98.75 98.75 7.71e-110 . . . . 10010 1 14 no PDB 2AKQ . "The Structure Of Bovine B-Lactoglobulin A In Crystals Grown At Very Low Ionic Strength" . . . . . 96.97 162 99.38 99.38 1.39e-110 . . . . 10010 1 15 no PDB 2BLG . "Structural Basis Of The Tanford Transition Of Bovine Beta- Lactoglobulin From Crystal Structures At Three Ph Values; Ph 8.2" . . . . . 96.97 162 99.38 99.38 1.39e-110 . . . . 10010 1 16 no PDB 2GJ5 . "Crystal Structure Of A Secondary Vitamin D3 Binding Site Of Milk Beta-Lactoglobulin" . . . . . 96.97 162 98.13 98.13 5.00e-109 . . . . 10010 1 17 no PDB 2Q2M . "Beta-Lactoglobulin (Native)" . . . . . 96.97 162 99.38 99.38 1.39e-110 . . . . 10010 1 18 no PDB 2Q2P . "Beta-Lactoglobulin (Reverse Native)" . . . . . 96.97 162 99.38 99.38 1.39e-110 . . . . 10010 1 19 no PDB 2Q39 . "Beta-Lactoglobulin (Low Humidity)" . . . . . 96.97 162 99.38 99.38 1.39e-110 . . . . 10010 1 20 no PDB 2R56 . "Crystal Structure Of A Recombinant Ige Fab Fragment In Complex With Bovine Beta-Lactoglobulin Allergen" . . . . . 96.97 162 98.13 98.13 5.00e-109 . . . . 10010 1 21 no PDB 3BLG . "Structural Basis Of The Tanford Transition Of Bovine Beta- Lactoglobulin From Crystal Structures At Three Ph Values; Ph 6.2" . . . . . 96.97 162 99.38 99.38 1.39e-110 . . . . 10010 1 22 no PDB 3NPO . "Bovine Beta Lactoglobulin Unliganded Form" . . . . . 96.97 162 98.13 98.13 5.00e-109 . . . . 10010 1 23 no PDB 3NQ3 . "Bovine Beta-Lactoglobulin Complex With Capric Acid" . . . . . 96.97 162 98.13 98.13 5.00e-109 . . . . 10010 1 24 no PDB 3NQ9 . "Bovine Beta-Lactoglobulin Complex With Caprylic Acid" . . . . . 96.97 162 98.13 98.13 5.00e-109 . . . . 10010 1 25 no PDB 3PH5 . "Bovine Beta Lactoglobulin Crystallized Through Ligandation Of Yttrium Cations" . . . . . 96.97 161 98.13 98.13 3.71e-109 . . . . 10010 1 26 no PDB 3PH6 . "Bovine Beta Lactoglobulin Crytsallized Through Ligandation Of Yttrium" . . . . . 96.97 161 98.13 98.13 3.71e-109 . . . . 10010 1 27 no PDB 3UEU . "Bovine Beta-Lactoglobulin Complex With Lauric Acid" . . . . . 96.97 162 98.13 98.13 5.00e-109 . . . . 10010 1 28 no PDB 3UEV . "Bovine Beta-Lactoglobulin Complex With Myristic Acid" . . . . . 96.97 162 98.13 98.13 5.00e-109 . . . . 10010 1 29 no PDB 3UEW . "Bovine Beta-Lactoglobulin Complex With Palmitic Acid" . . . . . 96.97 162 98.13 98.13 5.00e-109 . . . . 10010 1 30 no PDB 3UEX . "Bovine Beta-Lactoglobulin Complex With Stearic Acid" . . . . . 96.97 162 98.13 98.13 5.00e-109 . . . . 10010 1 31 no PDB 4DQ3 . "Bovine Beta-lactoglobulin Complex With Oleic Acid" . . . . . 96.97 162 98.13 98.13 5.00e-109 . . . . 10010 1 32 no PDB 4DQ4 . "Bovine Beta-lactoglobulin Complex With Linoleic Acid" . . . . . 96.97 162 98.13 98.13 5.00e-109 . . . . 10010 1 33 no PDB 4GNY . "Bovine Beta-lactoglobulin Complex With Dodecyl Sulfate" . . . . . 96.97 162 98.13 98.13 5.00e-109 . . . . 10010 1 34 no PDB 4IB6 . "Bovine Beta-lactoglobulin (isoform A) In Complex With Lauric Acid (c12)" . . . . . 96.97 162 99.38 99.38 1.39e-110 . . . . 10010 1 35 no PDB 4IB7 . "Bovine Beta-lactoglobulin (isoform A) In Complex With Dodecyltrimethylammonium (dtac)" . . . . . 96.97 162 99.38 99.38 1.39e-110 . . . . 10010 1 36 no PDB 4IB8 . "Bovine Beta-lactoglobulin (isoform A) In Complex With Dodecyl Sulphate (sds)" . . . . . 96.97 162 99.38 99.38 1.39e-110 . . . . 10010 1 37 no PDB 4IB9 . "Bovine Beta-lactoglobulin (isoform B) In Complex With Dodecyltrimethylammonium (dtac)" . . . . . 96.97 162 98.13 98.13 5.00e-109 . . . . 10010 1 38 no PDB 4IBA . "Bovine Beta-lactoglobulin (isoform B) In Complex With Dodecyl Sulphate (sds)" . . . . . 96.97 162 98.13 98.13 5.00e-109 . . . . 10010 1 39 no PDB 4KII . "Beta-lactoglobulin In Complex With Cp*rh(iii)cl N,n-di(pyridin-2-yl) Dodecanamide" . . . . . 96.97 162 99.38 99.38 1.39e-110 . . . . 10010 1 40 no PDB 4LZU . "Bovine Beta-lactoglobulin Crystallized In The Presence Of 2 Mm Zinc Chloride" . . . . . 96.97 162 98.13 98.13 5.00e-109 . . . . 10010 1 41 no PDB 4LZV . "Bovine Beta-lactoglobulin Crystallized In The Presence Of 20 Mm Zinc Chloride" . . . . . 96.97 162 98.13 98.13 5.00e-109 . . . . 10010 1 42 no PDB 4Y0P . "Bovine Beta-lactoglobulin Complex With Tetracaine (blg-tet)" . . . . . 96.97 162 98.13 98.13 5.00e-109 . . . . 10010 1 43 no PDB 4Y0Q . "Bovine Beta-lactoglobulin Complex With Pramocaine Crystallized From Sodium Citrate (blg-prm1)" . . . . . 96.97 162 98.13 98.13 5.00e-109 . . . . 10010 1 44 no PDB 4Y0R . "Bovine Beta-lactoglobulin Complex With Pramocaine Crystallized From Ammonium Sulphate (blg-prm2)" . . . . . 96.97 162 98.13 98.13 5.00e-109 . . . . 10010 1 45 no EMBL CAA06532 . "beta-lactoglobulin [Bubalus bubalis]" . . . . . 96.97 180 97.50 98.13 8.37e-109 . . . . 10010 1 46 no EMBL CAA32835 . "beta-lactoglobulin [Bos taurus]" . . . . . 96.97 178 98.75 98.75 2.38e-109 . . . . 10010 1 47 no EMBL CAA88303 . "beta-lactoglobulin variant B precursor [Bos taurus]" . . . . . 96.97 178 98.13 98.13 5.00e-109 . . . . 10010 1 48 no EMBL CAY39357 . "beta-lactoglobulin [Bubalus bubalis]" . . . . . 96.97 180 97.50 98.13 9.65e-109 . . . . 10010 1 49 no GB AAA30411 . "beta-lactoglobulin, partial [Bos taurus]" . . . . . 91.52 151 99.34 99.34 2.14e-103 . . . . 10010 1 50 no GB AAI08214 . "Lactoglobulin, beta [Bos taurus]" . . . . . 96.97 178 98.13 98.13 5.00e-109 . . . . 10010 1 51 no GB ABF48380 . "beta-lactoglobulin variant B precursor [Bos taurus]" . . . . . 96.97 178 98.13 98.13 5.00e-109 . . . . 10010 1 52 no GB ACG59280 . "major allergen beta-lactoglobulin [Bos taurus]" . . . . . 96.97 178 99.38 99.38 2.22e-110 . . . . 10010 1 53 no GB AFB74990 . "beta-lactoglobulin, partial [Bos grunniens]" . . . . . 65.45 108 97.22 97.22 1.04e-67 . . . . 10010 1 54 no PRF 0601265A . "lactoglobulin beta" . . . . . 96.97 162 97.50 98.13 8.17e-109 . . . . 10010 1 55 no REF NP_001277893 . "beta-lactoglobulin precursor [Bubalus bubalis]" . . . . . 96.97 180 97.50 98.13 9.65e-109 . . . . 10010 1 56 no REF NP_776354 . "beta-lactoglobulin precursor [Bos taurus]" . . . . . 96.97 178 98.13 98.13 5.00e-109 . . . . 10010 1 57 no REF XP_005888577 . "PREDICTED: beta-lactoglobulin isoform X1 [Bos mutus]" . . . . . 96.97 178 97.50 97.50 2.93e-108 . . . . 10010 1 58 no REF XP_006062245 . "PREDICTED: beta-lactoglobulin-like isoform X2 [Bubalus bubalis]" . . . . . 96.97 180 97.50 98.13 9.65e-109 . . . . 10010 1 59 no SP P02754 . "RecName: Full=Beta-lactoglobulin; Short=Beta-LG; AltName: Allergen=Bos d 5; Flags: Precursor" . . . . . 96.97 178 98.13 98.13 5.00e-109 . . . . 10010 1 60 no SP P02755 . "RecName: Full=Beta-lactoglobulin; Short=Beta-LG; Flags: Precursor" . . . . . 96.97 180 97.50 98.13 8.37e-109 . . . . 10010 1 61 no TPG DAA24277 . "TPA: beta-lactoglobulin precursor [Bos taurus]" . . . . . 96.97 178 98.75 98.75 1.44e-109 . . . . 10010 1 stop_ loop_ _Entity_common_name.Name _Entity_common_name.Type _Entity_common_name.Entry_ID _Entity_common_name.Entity_ID beta-lactoglobulin common 10010 1 stop_ loop_ _Entity_keyword.Keyword _Entity_keyword.Entry_ID _Entity_keyword.Entity_ID beta-barrel 10010 1 lipocalin 10010 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 -3 GLU . 10010 1 2 -2 ALA . 10010 1 3 -1 GLU . 10010 1 4 1 ALA . 10010 1 5 2 TYR . 10010 1 6 3 VAL . 10010 1 7 4 THR . 10010 1 8 5 GLN . 10010 1 9 6 THR . 10010 1 10 7 MET . 10010 1 11 8 LYS . 10010 1 12 9 GLY . 10010 1 13 10 LEU . 10010 1 14 11 ASP . 10010 1 15 12 ILE . 10010 1 16 13 GLN . 10010 1 17 14 LYS . 10010 1 18 15 VAL . 10010 1 19 16 ALA . 10010 1 20 17 GLY . 10010 1 21 18 THR . 10010 1 22 19 TRP . 10010 1 23 20 TYR . 10010 1 24 21 SER . 10010 1 25 22 LEU . 10010 1 26 23 ALA . 10010 1 27 24 MET . 10010 1 28 25 ALA . 10010 1 29 26 ALA . 10010 1 30 27 SER . 10010 1 31 28 ASP . 10010 1 32 29 ILE . 10010 1 33 30 SER . 10010 1 34 31 LEU . 10010 1 35 32 LEU . 10010 1 36 33 ASP . 10010 1 37 34 CYS . 10010 1 38 35 GLN . 10010 1 39 36 SER . 10010 1 40 37 ALA . 10010 1 41 38 PRO . 10010 1 42 39 LEU . 10010 1 43 40 ARG . 10010 1 44 41 VAL . 10010 1 45 42 TYR . 10010 1 46 43 VAL . 10010 1 47 44 GLU . 10010 1 48 45 GLU . 10010 1 49 46 LEU . 10010 1 50 47 LYS . 10010 1 51 48 PRO . 10010 1 52 49 THR . 10010 1 53 50 PRO . 10010 1 54 51 GLU . 10010 1 55 52 GLY . 10010 1 56 53 ASP . 10010 1 57 54 LEU . 10010 1 58 55 GLU . 10010 1 59 56 ILE . 10010 1 60 57 LEU . 10010 1 61 58 LEU . 10010 1 62 59 GLN . 10010 1 63 60 LYS . 10010 1 64 61 TRP . 10010 1 65 62 GLU . 10010 1 66 63 ASN . 10010 1 67 64 ASP . 10010 1 68 65 GLU . 10010 1 69 66 CYS . 10010 1 70 67 ALA . 10010 1 71 68 GLN . 10010 1 72 69 LYS . 10010 1 73 70 LYS . 10010 1 74 71 ILE . 10010 1 75 72 ILE . 10010 1 76 73 ALA . 10010 1 77 74 GLU . 10010 1 78 75 LYS . 10010 1 79 76 THR . 10010 1 80 77 LYS . 10010 1 81 78 ILE . 10010 1 82 79 PRO . 10010 1 83 80 ALA . 10010 1 84 81 VAL . 10010 1 85 82 PHE . 10010 1 86 83 LYS . 10010 1 87 84 ILE . 10010 1 88 85 ASP . 10010 1 89 86 ALA . 10010 1 90 87 LEU . 10010 1 91 88 ASN . 10010 1 92 89 GLU . 10010 1 93 90 ASN . 10010 1 94 91 LYS . 10010 1 95 92 VAL . 10010 1 96 93 LEU . 10010 1 97 94 VAL . 10010 1 98 95 LEU . 10010 1 99 96 ASP . 10010 1 100 97 THR . 10010 1 101 98 ASP . 10010 1 102 99 TYR . 10010 1 103 100 LYS . 10010 1 104 101 LYS . 10010 1 105 102 TYR . 10010 1 106 103 LEU . 10010 1 107 104 LEU . 10010 1 108 105 PHE . 10010 1 109 106 CYS . 10010 1 110 107 MET . 10010 1 111 108 GLU . 10010 1 112 109 ASN . 10010 1 113 110 SER . 10010 1 114 111 ALA . 10010 1 115 112 GLU . 10010 1 116 113 PRO . 10010 1 117 114 GLU . 10010 1 118 115 GLN . 10010 1 119 116 SER . 10010 1 120 117 LEU . 10010 1 121 118 VAL . 10010 1 122 119 CYS . 10010 1 123 120 GLN . 10010 1 124 121 CYS . 10010 1 125 122 LEU . 10010 1 126 123 VAL . 10010 1 127 124 ARG . 10010 1 128 125 THR . 10010 1 129 126 PRO . 10010 1 130 127 GLU . 10010 1 131 128 VAL . 10010 1 132 129 ASP . 10010 1 133 130 ASP . 10010 1 134 131 GLU . 10010 1 135 132 ALA . 10010 1 136 133 LEU . 10010 1 137 134 GLU . 10010 1 138 135 LYS . 10010 1 139 136 PHE . 10010 1 140 137 ASP . 10010 1 141 138 LYS . 10010 1 142 139 ALA . 10010 1 143 140 LEU . 10010 1 144 141 LYS . 10010 1 145 142 ALA . 10010 1 146 143 LEU . 10010 1 147 144 PRO . 10010 1 148 145 MET . 10010 1 149 146 HIS . 10010 1 150 147 ILE . 10010 1 151 148 ARG . 10010 1 152 149 LEU . 10010 1 153 150 SER . 10010 1 154 151 PHE . 10010 1 155 152 ASN . 10010 1 156 153 PRO . 10010 1 157 154 THR . 10010 1 158 155 GLN . 10010 1 159 156 LEU . 10010 1 160 157 GLU . 10010 1 161 158 GLU . 10010 1 162 159 GLN . 10010 1 163 160 CYS . 10010 1 164 161 HIS . 10010 1 165 162 ILE . 10010 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 . GLU 1 1 10010 1 . ALA 2 2 10010 1 . GLU 3 3 10010 1 . ALA 4 4 10010 1 . TYR 5 5 10010 1 . VAL 6 6 10010 1 . THR 7 7 10010 1 . GLN 8 8 10010 1 . THR 9 9 10010 1 . MET 10 10 10010 1 . LYS 11 11 10010 1 . GLY 12 12 10010 1 . LEU 13 13 10010 1 . ASP 14 14 10010 1 . ILE 15 15 10010 1 . GLN 16 16 10010 1 . LYS 17 17 10010 1 . VAL 18 18 10010 1 . ALA 19 19 10010 1 . GLY 20 20 10010 1 . THR 21 21 10010 1 . TRP 22 22 10010 1 . TYR 23 23 10010 1 . SER 24 24 10010 1 . LEU 25 25 10010 1 . ALA 26 26 10010 1 . MET 27 27 10010 1 . ALA 28 28 10010 1 . ALA 29 29 10010 1 . SER 30 30 10010 1 . ASP 31 31 10010 1 . ILE 32 32 10010 1 . SER 33 33 10010 1 . LEU 34 34 10010 1 . LEU 35 35 10010 1 . ASP 36 36 10010 1 . CYS 37 37 10010 1 . GLN 38 38 10010 1 . SER 39 39 10010 1 . ALA 40 40 10010 1 . PRO 41 41 10010 1 . LEU 42 42 10010 1 . ARG 43 43 10010 1 . VAL 44 44 10010 1 . TYR 45 45 10010 1 . VAL 46 46 10010 1 . GLU 47 47 10010 1 . GLU 48 48 10010 1 . LEU 49 49 10010 1 . LYS 50 50 10010 1 . PRO 51 51 10010 1 . THR 52 52 10010 1 . PRO 53 53 10010 1 . GLU 54 54 10010 1 . GLY 55 55 10010 1 . ASP 56 56 10010 1 . LEU 57 57 10010 1 . GLU 58 58 10010 1 . ILE 59 59 10010 1 . LEU 60 60 10010 1 . LEU 61 61 10010 1 . GLN 62 62 10010 1 . LYS 63 63 10010 1 . TRP 64 64 10010 1 . GLU 65 65 10010 1 . ASN 66 66 10010 1 . ASP 67 67 10010 1 . GLU 68 68 10010 1 . CYS 69 69 10010 1 . ALA 70 70 10010 1 . GLN 71 71 10010 1 . LYS 72 72 10010 1 . LYS 73 73 10010 1 . ILE 74 74 10010 1 . ILE 75 75 10010 1 . ALA 76 76 10010 1 . GLU 77 77 10010 1 . LYS 78 78 10010 1 . THR 79 79 10010 1 . LYS 80 80 10010 1 . ILE 81 81 10010 1 . PRO 82 82 10010 1 . ALA 83 83 10010 1 . VAL 84 84 10010 1 . PHE 85 85 10010 1 . LYS 86 86 10010 1 . ILE 87 87 10010 1 . ASP 88 88 10010 1 . ALA 89 89 10010 1 . LEU 90 90 10010 1 . ASN 91 91 10010 1 . GLU 92 92 10010 1 . ASN 93 93 10010 1 . LYS 94 94 10010 1 . VAL 95 95 10010 1 . LEU 96 96 10010 1 . VAL 97 97 10010 1 . LEU 98 98 10010 1 . ASP 99 99 10010 1 . THR 100 100 10010 1 . ASP 101 101 10010 1 . TYR 102 102 10010 1 . LYS 103 103 10010 1 . LYS 104 104 10010 1 . TYR 105 105 10010 1 . LEU 106 106 10010 1 . LEU 107 107 10010 1 . PHE 108 108 10010 1 . CYS 109 109 10010 1 . MET 110 110 10010 1 . GLU 111 111 10010 1 . ASN 112 112 10010 1 . SER 113 113 10010 1 . ALA 114 114 10010 1 . GLU 115 115 10010 1 . PRO 116 116 10010 1 . GLU 117 117 10010 1 . GLN 118 118 10010 1 . SER 119 119 10010 1 . LEU 120 120 10010 1 . VAL 121 121 10010 1 . CYS 122 122 10010 1 . GLN 123 123 10010 1 . CYS 124 124 10010 1 . LEU 125 125 10010 1 . VAL 126 126 10010 1 . ARG 127 127 10010 1 . THR 128 128 10010 1 . PRO 129 129 10010 1 . GLU 130 130 10010 1 . VAL 131 131 10010 1 . ASP 132 132 10010 1 . ASP 133 133 10010 1 . GLU 134 134 10010 1 . ALA 135 135 10010 1 . LEU 136 136 10010 1 . GLU 137 137 10010 1 . LYS 138 138 10010 1 . PHE 139 139 10010 1 . ASP 140 140 10010 1 . LYS 141 141 10010 1 . ALA 142 142 10010 1 . LEU 143 143 10010 1 . LYS 144 144 10010 1 . ALA 145 145 10010 1 . LEU 146 146 10010 1 . PRO 147 147 10010 1 . MET 148 148 10010 1 . HIS 149 149 10010 1 . ILE 150 150 10010 1 . ARG 151 151 10010 1 . LEU 152 152 10010 1 . SER 153 153 10010 1 . PHE 154 154 10010 1 . ASN 155 155 10010 1 . PRO 156 156 10010 1 . THR 157 157 10010 1 . GLN 158 158 10010 1 . LEU 159 159 10010 1 . GLU 160 160 10010 1 . GLU 161 161 10010 1 . GLN 162 162 10010 1 . CYS 163 163 10010 1 . HIS 164 164 10010 1 . ILE 165 165 10010 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 10010 _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 $BLG_A34C . 9913 . . . Cow . . Eukaryota Metazoa Bos taurus . . . . . . . . . . . . . milk . . . . . . . 10010 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 10010 _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 $BLG_A34C . 'recombinant technology' . 'Methylotrophic yeast' . . Pichia pastoris GS115 . . . . . . . . . . . . plasmid . . pPIC9 Invitrogen . . . 2 $citation_2 10010 1 stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Sample.Sf_category sample _Sample.Sf_framecode sample_1 _Sample.Entry_ID 10010 _Sample.ID 1 _Sample.Type solution _Sample.Sub_type . _Sample.Details ; Protein dissolved into water. (No buffer is added.) pH is adjusted by adding HCl. ; _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 'beta-lactoglobulin A34C polypeptide' '[U-99% 13C; U-99.3% 15N]' 1 $assembly . . . protein 2 . . mM 0.2 . . . 10010 1 2 'Hydrochloric acid' . . . . . . acid . 7 9 mM . . . . 10010 1 stop_ save_ ####################### # Sample conditions # ####################### save_conditions_for_BLG_A34C_at_pH_6.5 _Sample_condition_list.Sf_category sample_conditions _Sample_condition_list.Sf_framecode conditions_for_BLG_A34C_at_pH_6.5 _Sample_condition_list.Entry_ID 10010 _Sample_condition_list.ID 1 _Sample_condition_list.Details . loop_ _Sample_condition_variable.Type _Sample_condition_variable.Val _Sample_condition_variable.Val_err _Sample_condition_variable.Val_units _Sample_condition_variable.Entry_ID _Sample_condition_variable.Sample_condition_list_ID 'ionic strength' 0.000 0.000 M 10010 1 pH 6.5 0.1 pH 10010 1 temperature 313 0.1 K 10010 1 stop_ save_ ############################ # Computer software used # ############################ save_pipp.com _Software.Sf_category software _Software.Sf_framecode pipp.com _Software.Entry_ID 10010 _Software.ID 1 _Software.Name pipp.com _Software.Version . _Software.Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_Bruker_DRX800 _NMR_spectrometer.Sf_category NMR_spectrometer _NMR_spectrometer.Sf_framecode Bruker_DRX800 _NMR_spectrometer.Entry_ID 10010 _NMR_spectrometer.ID 1 _NMR_spectrometer.Details . _NMR_spectrometer.Manufacturer Bruker _NMR_spectrometer.Model DRX _NMR_spectrometer.Serial_number . _NMR_spectrometer.Field_strength 800 save_ ############################# # NMR applied experiments # ############################# save_NMR_experiment_list _Experiment_list.Sf_category experiment_list _Experiment_list.Sf_framecode NMR_experiment_list _Experiment_list.Entry_ID 10010 _Experiment_list.ID 1 _Experiment_list.Details . loop_ _Experiment.ID _Experiment.Name _Experiment.Raw_data_flag _Experiment.NMR_spec_expt_ID _Experiment.NMR_spec_expt_label _Experiment.MS_expt_ID _Experiment.MS_expt_label _Experiment.SAXS_expt_ID _Experiment.SAXS_expt_label _Experiment.FRET_expt_ID _Experiment.FRET_expt_label _Experiment.EMR_expt_ID _Experiment.EMR_expt_label _Experiment.Sample_ID _Experiment.Sample_label _Experiment.Sample_state _Experiment.Sample_volume _Experiment.Sample_volume_units _Experiment.Sample_condition_list_ID _Experiment.Sample_condition_list_label _Experiment.Sample_spinning_rate _Experiment.Sample_angle _Experiment.NMR_tube_type _Experiment.NMR_spectrometer_ID _Experiment.NMR_spectrometer_label _Experiment.NMR_spectrometer_probe_ID _Experiment.NMR_spectrometer_probe_label _Experiment.NMR_spectral_processing_ID _Experiment.NMR_spectral_processing_label _Experiment.Mass_spectrometer_ID _Experiment.Mass_spectrometer_label _Experiment.Xray_instrument_ID _Experiment.Xray_instrument_label _Experiment.Fluorescence_instrument_ID _Experiment.Fluorescence_instrument_label _Experiment.EMR_instrument_ID _Experiment.EMR_instrument_label _Experiment.Chromatographic_system_ID _Experiment.Chromatographic_system_label _Experiment.Chromatographic_column_ID _Experiment.Chromatographic_column_label _Experiment.Entry_ID _Experiment.Experiment_list_ID 1 '1H15N HSQC' no . . . . . . . . . . 1 $sample_1 . . . 1 $conditions_for_BLG_A34C_at_pH_6.5 . . . 1 $Bruker_DRX800 . . . . . . . . . . . . . . . . 10010 1 2 CBCA(CO)NH no . . . . . . . . . . 1 $sample_1 . . . 1 $conditions_for_BLG_A34C_at_pH_6.5 . . . 1 $Bruker_DRX800 . . . . . . . . . . . . . . . . 10010 1 3 HNCACB no . . . . . . . . . . 1 $sample_1 . . . 1 $conditions_for_BLG_A34C_at_pH_6.5 . . . 1 $Bruker_DRX800 . . . . . . . . . . . . . . . . 10010 1 4 HNCO no . . . . . . . . . . 1 $sample_1 . . . 1 $conditions_for_BLG_A34C_at_pH_6.5 . . . 1 $Bruker_DRX800 . . . . . . . . . . . . . . . . 10010 1 5 HNCACO no . . . . . . . . . . 1 $sample_1 . . . 1 $conditions_for_BLG_A34C_at_pH_6.5 . . . 1 $Bruker_DRX800 . . . . . . . . . . . . . . . . 10010 1 stop_ save_ save_1H15N_HSQC _NMR_spec_expt.Sf_category NMR_spectrometer_expt _NMR_spec_expt.Sf_framecode 1H15N_HSQC _NMR_spec_expt.Entry_ID 10010 _NMR_spec_expt.ID 1 _NMR_spec_expt.Name '1H15N HSQC' _NMR_spec_expt.Type . _NMR_spec_expt.Sample_volume . _NMR_spec_expt.Sample_volume_units . _NMR_spec_expt.NMR_tube_type . _NMR_spec_expt.Sample_spinning_rate . _NMR_spec_expt.Sample_angle . _NMR_spec_expt.NMR_spectrometer_ID 1 _NMR_spec_expt.NMR_spectrometer_label $Bruker_DRX800 _NMR_spec_expt.NMR_spectrometer_probe_ID . _NMR_spec_expt.NMR_spectrometer_probe_label . _NMR_spec_expt.Carrier_freq_switch_time . _NMR_spec_expt.Software_ID 1 _NMR_spec_expt.Software_label $pipp.com _NMR_spec_expt.Method_ID . _NMR_spec_expt.Method_label . _NMR_spec_expt.Pulse_seq_accession_BMRB_code . _NMR_spec_expt.Details . save_ save_CBCA(CO)NH _NMR_spec_expt.Sf_category NMR_spectrometer_expt _NMR_spec_expt.Sf_framecode CBCA(CO)NH _NMR_spec_expt.Entry_ID 10010 _NMR_spec_expt.ID 2 _NMR_spec_expt.Name CBCA(CO)NH _NMR_spec_expt.Type . _NMR_spec_expt.Sample_volume . _NMR_spec_expt.Sample_volume_units . _NMR_spec_expt.NMR_tube_type . _NMR_spec_expt.Sample_spinning_rate . _NMR_spec_expt.Sample_angle . _NMR_spec_expt.NMR_spectrometer_ID 1 _NMR_spec_expt.NMR_spectrometer_label $Bruker_DRX800 _NMR_spec_expt.NMR_spectrometer_probe_ID . _NMR_spec_expt.NMR_spectrometer_probe_label . _NMR_spec_expt.Carrier_freq_switch_time . _NMR_spec_expt.Software_ID 1 _NMR_spec_expt.Software_label $pipp.com _NMR_spec_expt.Method_ID . _NMR_spec_expt.Method_label . _NMR_spec_expt.Pulse_seq_accession_BMRB_code . _NMR_spec_expt.Details . save_ save_HNCACB _NMR_spec_expt.Sf_category NMR_spectrometer_expt _NMR_spec_expt.Sf_framecode HNCACB _NMR_spec_expt.Entry_ID 10010 _NMR_spec_expt.ID 3 _NMR_spec_expt.Name HNCACB _NMR_spec_expt.Type . _NMR_spec_expt.Sample_volume . _NMR_spec_expt.Sample_volume_units . _NMR_spec_expt.NMR_tube_type . _NMR_spec_expt.Sample_spinning_rate . _NMR_spec_expt.Sample_angle . _NMR_spec_expt.NMR_spectrometer_ID 1 _NMR_spec_expt.NMR_spectrometer_label $Bruker_DRX800 _NMR_spec_expt.NMR_spectrometer_probe_ID . _NMR_spec_expt.NMR_spectrometer_probe_label . _NMR_spec_expt.Carrier_freq_switch_time . _NMR_spec_expt.Software_ID 1 _NMR_spec_expt.Software_label $pipp.com _NMR_spec_expt.Method_ID . _NMR_spec_expt.Method_label . _NMR_spec_expt.Pulse_seq_accession_BMRB_code . _NMR_spec_expt.Details . save_ save_HNCO _NMR_spec_expt.Sf_category NMR_spectrometer_expt _NMR_spec_expt.Sf_framecode HNCO _NMR_spec_expt.Entry_ID 10010 _NMR_spec_expt.ID 4 _NMR_spec_expt.Name HNCO _NMR_spec_expt.Type . _NMR_spec_expt.Sample_volume . _NMR_spec_expt.Sample_volume_units . _NMR_spec_expt.NMR_tube_type . _NMR_spec_expt.Sample_spinning_rate . _NMR_spec_expt.Sample_angle . _NMR_spec_expt.NMR_spectrometer_ID 1 _NMR_spec_expt.NMR_spectrometer_label $Bruker_DRX800 _NMR_spec_expt.NMR_spectrometer_probe_ID . _NMR_spec_expt.NMR_spectrometer_probe_label . _NMR_spec_expt.Carrier_freq_switch_time . _NMR_spec_expt.Software_ID 1 _NMR_spec_expt.Software_label $pipp.com _NMR_spec_expt.Method_ID . _NMR_spec_expt.Method_label . _NMR_spec_expt.Pulse_seq_accession_BMRB_code . _NMR_spec_expt.Details . save_ save_HNCACO _NMR_spec_expt.Sf_category NMR_spectrometer_expt _NMR_spec_expt.Sf_framecode HNCACO _NMR_spec_expt.Entry_ID 10010 _NMR_spec_expt.ID 5 _NMR_spec_expt.Name HNCACO _NMR_spec_expt.Type . _NMR_spec_expt.Sample_volume . _NMR_spec_expt.Sample_volume_units . _NMR_spec_expt.NMR_tube_type . _NMR_spec_expt.Sample_spinning_rate . _NMR_spec_expt.Sample_angle . _NMR_spec_expt.NMR_spectrometer_ID 1 _NMR_spec_expt.NMR_spectrometer_label $Bruker_DRX800 _NMR_spec_expt.NMR_spectrometer_probe_ID . _NMR_spec_expt.NMR_spectrometer_probe_label . _NMR_spec_expt.Carrier_freq_switch_time . _NMR_spec_expt.Software_ID 1 _NMR_spec_expt.Software_label $pipp.com _NMR_spec_expt.Method_ID . _NMR_spec_expt.Method_label . _NMR_spec_expt.Pulse_seq_accession_BMRB_code . _NMR_spec_expt.Details . save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_default_reference _Chem_shift_reference.Sf_category chem_shift_reference _Chem_shift_reference.Sf_framecode default_reference _Chem_shift_reference.Entry_ID 10010 _Chem_shift_reference.ID 1 _Chem_shift_reference.Details . loop_ _Chem_shift_ref.Atom_type _Chem_shift_ref.Atom_isotope_number _Chem_shift_ref.Mol_common_name _Chem_shift_ref.Atom_group _Chem_shift_ref.Concentration_val _Chem_shift_ref.Concentration_units _Chem_shift_ref.Solvent _Chem_shift_ref.Rank _Chem_shift_ref.Chem_shift_units _Chem_shift_ref.Chem_shift_val _Chem_shift_ref.Ref_method _Chem_shift_ref.Ref_type _Chem_shift_ref.Indirect_shift_ratio _Chem_shift_ref.External_ref_loc _Chem_shift_ref.External_ref_sample_geometry _Chem_shift_ref.External_ref_axis _Chem_shift_ref.Indirect_shift_ratio_cit_ID _Chem_shift_ref.Indirect_shift_ratio_cit_label _Chem_shift_ref.Ref_correction_type _Chem_shift_ref.Correction_val _Chem_shift_ref.Correction_val_cit_ID _Chem_shift_ref.Correction_val_cit_label _Chem_shift_ref.Entry_ID _Chem_shift_ref.Chem_shift_reference_ID C 13 DSS 'methyl protons' . . . . ppm 0.0 . indirect 0.251449530 . . . . . . . . . 10010 1 H 1 DSS 'methyl protons' . . . . ppm 0.0 internal direct 1.0 . . . . . . . . . 10010 1 N 15 DSS 'methyl protons' . . . . ppm 0.0 . indirect 0.101329118 . . . . . . . . . 10010 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_assignment_for_bLG_A34C_at_pH_6.5 _Assigned_chem_shift_list.Sf_category assigned_chemical_shifts _Assigned_chem_shift_list.Sf_framecode assignment_for_bLG_A34C_at_pH_6.5 _Assigned_chem_shift_list.Entry_ID 10010 _Assigned_chem_shift_list.ID 1 _Assigned_chem_shift_list.Sample_condition_list_ID 1 _Assigned_chem_shift_list.Sample_condition_list_label $conditions_for_BLG_A34C_at_pH_6.5 _Assigned_chem_shift_list.Chem_shift_reference_ID 1 _Assigned_chem_shift_list.Chem_shift_reference_label $default_reference _Assigned_chem_shift_list.Chem_shift_1H_err 0.02 _Assigned_chem_shift_list.Chem_shift_13C_err 0.2 _Assigned_chem_shift_list.Chem_shift_15N_err 0.1 _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 '1H15N HSQC' 1 $sample_1 isotropic 10010 1 2 CBCA(CO)NH 1 $sample_1 isotropic 10010 1 3 HNCACB 1 $sample_1 isotropic 10010 1 4 HNCO 1 $sample_1 isotropic 10010 1 5 HNCACO 1 $sample_1 isotropic 10010 1 stop_ loop_ _Chem_shift_software.Software_ID _Chem_shift_software.Software_label _Chem_shift_software.Method_ID _Chem_shift_software.Method_label _Chem_shift_software.Entry_ID _Chem_shift_software.Assigned_chem_shift_list_ID 1 $pipp.com . . 10010 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 ALA CA C 13 52.68 0.2 . 1 . . . . -2 ALA CA . 10010 1 2 . 1 1 2 2 ALA CB C 13 19.32 0.2 . 1 . . . . -2 ALA CB . 10010 1 3 . 1 1 3 3 GLU H H 1 8.51 0.02 . 1 . . . . -1 GLU H . 10010 1 4 . 1 1 3 3 GLU C C 13 176.02 0.2 . 1 . . . . -1 GLU C . 10010 1 5 . 1 1 3 3 GLU CA C 13 56.71 0.2 . 1 . . . . -1 GLU CA . 10010 1 6 . 1 1 3 3 GLU CB C 13 30.26 0.2 . 1 . . . . -1 GLU CB . 10010 1 7 . 1 1 3 3 GLU N N 15 120.73 0.1 . 1 . . . . -1 GLU N . 10010 1 8 . 1 1 4 4 ALA H H 1 8.22 0.02 . 1 . . . . 1 ALA H . 10010 1 9 . 1 1 4 4 ALA C C 13 177.22 0.2 . 1 . . . . 1 ALA C . 10010 1 10 . 1 1 4 4 ALA CA C 13 52.56 0.2 . 1 . . . . 1 ALA CA . 10010 1 11 . 1 1 4 4 ALA CB C 13 19.49 0.2 . 1 . . . . 1 ALA CB . 10010 1 12 . 1 1 4 4 ALA N N 15 124.3 0.1 . 1 . . . . 1 ALA N . 10010 1 13 . 1 1 5 5 TYR H H 1 8.58 0.02 . 1 . . . . 2 TYR H . 10010 1 14 . 1 1 5 5 TYR C C 13 176.14 0.2 . 1 . . . . 2 TYR C . 10010 1 15 . 1 1 5 5 TYR CA C 13 58.91 0.2 . 1 . . . . 2 TYR CA . 10010 1 16 . 1 1 5 5 TYR CB C 13 38.88 0.2 . 1 . . . . 2 TYR CB . 10010 1 17 . 1 1 5 5 TYR N N 15 118.51 0.1 . 1 . . . . 2 TYR N . 10010 1 18 . 1 1 6 6 VAL H H 1 8.2 0.02 . 1 . . . . 3 VAL H . 10010 1 19 . 1 1 6 6 VAL C C 13 175.86 0.2 . 1 . . . . 3 VAL C . 10010 1 20 . 1 1 6 6 VAL CA C 13 63.2 0.2 . 1 . . . . 3 VAL CA . 10010 1 21 . 1 1 6 6 VAL CB C 13 32.01 0.2 . 1 . . . . 3 VAL CB . 10010 1 22 . 1 1 6 6 VAL N N 15 120.44 0.1 . 1 . . . . 3 VAL N . 10010 1 23 . 1 1 7 7 THR H H 1 7.91 0.02 . 1 . . . . 4 THR H . 10010 1 24 . 1 1 7 7 THR C C 13 174.91 0.2 . 1 . . . . 4 THR C . 10010 1 25 . 1 1 7 7 THR CA C 13 62.03 0.2 . 1 . . . . 4 THR CA . 10010 1 26 . 1 1 7 7 THR CB C 13 69.59 0.2 . 1 . . . . 4 THR CB . 10010 1 27 . 1 1 7 7 THR N N 15 115.29 0.1 . 1 . . . . 4 THR N . 10010 1 28 . 1 1 8 8 GLN H H 1 8.11 0.02 . 1 . . . . 5 GLN H . 10010 1 29 . 1 1 8 8 GLN C C 13 175.03 0.2 . 1 . . . . 5 GLN C . 10010 1 30 . 1 1 8 8 GLN CA C 13 55.67 0.2 . 1 . . . . 5 GLN CA . 10010 1 31 . 1 1 8 8 GLN CB C 13 29.14 0.2 . 1 . . . . 5 GLN CB . 10010 1 32 . 1 1 8 8 GLN N N 15 123.1 0.1 . 1 . . . . 5 GLN N . 10010 1 33 . 1 1 9 9 THR H H 1 7.65 0.02 . 1 . . . . 6 THR H . 10010 1 34 . 1 1 9 9 THR C C 13 174.89 0.2 . 1 . . . . 6 THR C . 10010 1 35 . 1 1 9 9 THR CA C 13 60.59 0.2 . 1 . . . . 6 THR CA . 10010 1 36 . 1 1 9 9 THR CB C 13 70.7 0.2 . 1 . . . . 6 THR CB . 10010 1 37 . 1 1 9 9 THR N N 15 110.49 0.1 . 1 . . . . 6 THR N . 10010 1 38 . 1 1 10 10 MET H H 1 7.87 0.02 . 1 . . . . 7 MET H . 10010 1 39 . 1 1 10 10 MET C C 13 175.8 0.2 . 1 . . . . 7 MET C . 10010 1 40 . 1 1 10 10 MET CA C 13 56.87 0.2 . 1 . . . . 7 MET CA . 10010 1 41 . 1 1 10 10 MET CB C 13 33.18 0.2 . 1 . . . . 7 MET CB . 10010 1 42 . 1 1 10 10 MET N N 15 120.44 0.1 . 1 . . . . 7 MET N . 10010 1 43 . 1 1 11 11 LYS H H 1 8.61 0.02 . 1 . . . . 8 LYS H . 10010 1 44 . 1 1 11 11 LYS C C 13 177.45 0.2 . 1 . . . . 8 LYS C . 10010 1 45 . 1 1 11 11 LYS CA C 13 56.94 0.2 . 1 . . . . 8 LYS CA . 10010 1 46 . 1 1 11 11 LYS CB C 13 32.71 0.2 . 1 . . . . 8 LYS CB . 10010 1 47 . 1 1 11 11 LYS N N 15 127.15 0.1 . 1 . . . . 8 LYS N . 10010 1 48 . 1 1 12 12 GLY H H 1 8.53 0.02 . 1 . . . . 9 GLY H . 10010 1 49 . 1 1 12 12 GLY C C 13 174.26 0.2 . 1 . . . . 9 GLY C . 10010 1 50 . 1 1 12 12 GLY CA C 13 45.84 0.2 . 1 . . . . 9 GLY CA . 10010 1 51 . 1 1 12 12 GLY N N 15 109.16 0.1 . 1 . . . . 9 GLY N . 10010 1 52 . 1 1 13 13 LEU H H 1 7.51 0.02 . 1 . . . . 10 LEU H . 10010 1 53 . 1 1 13 13 LEU C C 13 175.42 0.2 . 1 . . . . 10 LEU C . 10010 1 54 . 1 1 13 13 LEU CA C 13 56.29 0.2 . 1 . . . . 10 LEU CA . 10010 1 55 . 1 1 13 13 LEU CB C 13 43.02 0.2 . 1 . . . . 10 LEU CB . 10010 1 56 . 1 1 13 13 LEU N N 15 120.55 0.1 . 1 . . . . 10 LEU N . 10010 1 57 . 1 1 14 14 ASP H H 1 8.59 0.02 . 1 . . . . 11 ASP H . 10010 1 58 . 1 1 14 14 ASP C C 13 177.07 0.2 . 1 . . . . 11 ASP C . 10010 1 59 . 1 1 14 14 ASP CA C 13 52.06 0.2 . 1 . . . . 11 ASP CA . 10010 1 60 . 1 1 14 14 ASP CB C 13 40.53 0.2 . 1 . . . . 11 ASP CB . 10010 1 61 . 1 1 14 14 ASP N N 15 127.98 0.1 . 1 . . . . 11 ASP N . 10010 1 62 . 1 1 15 15 ILE H H 1 8.74 0.02 . 1 . . . . 12 ILE H . 10010 1 63 . 1 1 15 15 ILE C C 13 176.57 0.2 . 1 . . . . 12 ILE C . 10010 1 64 . 1 1 15 15 ILE CA C 13 61.77 0.2 . 1 . . . . 12 ILE CA . 10010 1 65 . 1 1 15 15 ILE CB C 13 39.14 0.2 . 1 . . . . 12 ILE CB . 10010 1 66 . 1 1 15 15 ILE N N 15 122.66 0.1 . 1 . . . . 12 ILE N . 10010 1 67 . 1 1 16 16 GLN H H 1 8.11 0.02 . 1 . . . . 13 GLN H . 10010 1 68 . 1 1 16 16 GLN C C 13 179.55 0.2 . 1 . . . . 13 GLN C . 10010 1 69 . 1 1 16 16 GLN CA C 13 57.9 0.2 . 1 . . . . 13 GLN CA . 10010 1 70 . 1 1 16 16 GLN CB C 13 27.35 0.2 . 1 . . . . 13 GLN CB . 10010 1 71 . 1 1 16 16 GLN N N 15 116.85 0.1 . 1 . . . . 13 GLN N . 10010 1 72 . 1 1 17 17 LYS H H 1 7.34 0.02 . 1 . . . . 14 LYS H . 10010 1 73 . 1 1 17 17 LYS C C 13 177.76 0.2 . 1 . . . . 14 LYS C . 10010 1 74 . 1 1 17 17 LYS CA C 13 57.56 0.2 . 1 . . . . 14 LYS CA . 10010 1 75 . 1 1 17 17 LYS CB C 13 33.39 0.2 . 1 . . . . 14 LYS CB . 10010 1 76 . 1 1 17 17 LYS N N 15 114.22 0.1 . 1 . . . . 14 LYS N . 10010 1 77 . 1 1 18 18 VAL H H 1 7.39 0.02 . 1 . . . . 15 VAL H . 10010 1 78 . 1 1 18 18 VAL C C 13 173.95 0.2 . 1 . . . . 15 VAL C . 10010 1 79 . 1 1 18 18 VAL CA C 13 60.99 0.2 . 1 . . . . 15 VAL CA . 10010 1 80 . 1 1 18 18 VAL CB C 13 31.25 0.2 . 1 . . . . 15 VAL CB . 10010 1 81 . 1 1 18 18 VAL N N 15 110.18 0.1 . 1 . . . . 15 VAL N . 10010 1 82 . 1 1 19 19 ALA H H 1 6.81 0.02 . 1 . . . . 16 ALA H . 10010 1 83 . 1 1 19 19 ALA C C 13 178.56 0.2 . 1 . . . . 16 ALA C . 10010 1 84 . 1 1 19 19 ALA CA C 13 52.77 0.2 . 1 . . . . 16 ALA CA . 10010 1 85 . 1 1 19 19 ALA CB C 13 20.28 0.2 . 1 . . . . 16 ALA CB . 10010 1 86 . 1 1 19 19 ALA N N 15 120.67 0.1 . 1 . . . . 16 ALA N . 10010 1 87 . 1 1 20 20 GLY H H 1 9.18 0.02 . 1 . . . . 17 GLY H . 10010 1 88 . 1 1 20 20 GLY C C 13 172.72 0.2 . 1 . . . . 17 GLY C . 10010 1 89 . 1 1 20 20 GLY CA C 13 44.42 0.2 . 1 . . . . 17 GLY CA . 10010 1 90 . 1 1 20 20 GLY N N 15 110.78 0.1 . 1 . . . . 17 GLY N . 10010 1 91 . 1 1 21 21 THR H H 1 8.28 0.02 . 1 . . . . 18 THR H . 10010 1 92 . 1 1 21 21 THR C C 13 173.9 0.2 . 1 . . . . 18 THR C . 10010 1 93 . 1 1 21 21 THR CA C 13 64 0.2 . 1 . . . . 18 THR CA . 10010 1 94 . 1 1 21 21 THR CB C 13 70.07 0.2 . 1 . . . . 18 THR CB . 10010 1 95 . 1 1 21 21 THR N N 15 117.41 0.1 . 1 . . . . 18 THR N . 10010 1 96 . 1 1 22 22 TRP H H 1 7.49 0.02 . 1 . . . . 19 TRP H . 10010 1 97 . 1 1 22 22 TRP C C 13 172.12 0.2 . 1 . . . . 19 TRP C . 10010 1 98 . 1 1 22 22 TRP CA C 13 55.73 0.2 . 1 . . . . 19 TRP CA . 10010 1 99 . 1 1 22 22 TRP CB C 13 36.97 0.2 . 1 . . . . 19 TRP CB . 10010 1 100 . 1 1 22 22 TRP N N 15 123.57 0.1 . 1 . . . . 19 TRP N . 10010 1 101 . 1 1 23 23 TYR H H 1 9.22 0.02 . 1 . . . . 20 TYR H . 10010 1 102 . 1 1 23 23 TYR C C 13 177.52 0.2 . 1 . . . . 20 TYR C . 10010 1 103 . 1 1 23 23 TYR CA C 13 56.86 0.2 . 1 . . . . 20 TYR CA . 10010 1 104 . 1 1 23 23 TYR CB C 13 42.01 0.2 . 1 . . . . 20 TYR CB . 10010 1 105 . 1 1 23 23 TYR N N 15 112.6 0.1 . 1 . . . . 20 TYR N . 10010 1 106 . 1 1 24 24 SER H H 1 9.93 0.02 . 1 . . . . 21 SER H . 10010 1 107 . 1 1 24 24 SER C C 13 172.82 0.2 . 1 . . . . 21 SER C . 10010 1 108 . 1 1 24 24 SER CA C 13 60.06 0.2 . 1 . . . . 21 SER CA . 10010 1 109 . 1 1 24 24 SER CB C 13 62.97 0.2 . 1 . . . . 21 SER CB . 10010 1 110 . 1 1 24 24 SER N N 15 119.91 0.1 . 1 . . . . 21 SER N . 10010 1 111 . 1 1 25 25 LEU C C 13 174.61 0.2 . 1 . . . . 22 LEU C . 10010 1 112 . 1 1 25 25 LEU CA C 13 56.71 0.2 . 1 . . . . 22 LEU CA . 10010 1 113 . 1 1 25 25 LEU CB C 13 44.02 0.2 . 1 . . . . 22 LEU CB . 10010 1 114 . 1 1 26 26 ALA H H 1 7.81 0.02 . 1 . . . . 23 ALA H . 10010 1 115 . 1 1 26 26 ALA C C 13 175.58 0.2 . 1 . . . . 23 ALA C . 10010 1 116 . 1 1 26 26 ALA CA C 13 50.86 0.2 . 1 . . . . 23 ALA CA . 10010 1 117 . 1 1 26 26 ALA CB C 13 23.34 0.2 . 1 . . . . 23 ALA CB . 10010 1 118 . 1 1 26 26 ALA N N 15 115.14 0.1 . 1 . . . . 23 ALA N . 10010 1 119 . 1 1 27 27 MET H H 1 9.24 0.02 . 1 . . . . 24 MET H . 10010 1 120 . 1 1 27 27 MET C C 13 173 0.2 . 1 . . . . 24 MET C . 10010 1 121 . 1 1 27 27 MET CA C 13 54.32 0.2 . 1 . . . . 24 MET CA . 10010 1 122 . 1 1 27 27 MET CB C 13 37 0.2 . 1 . . . . 24 MET CB . 10010 1 123 . 1 1 27 27 MET N N 15 114.58 0.1 . 1 . . . . 24 MET N . 10010 1 124 . 1 1 28 28 ALA H H 1 9.39 0.02 . 1 . . . . 25 ALA H . 10010 1 125 . 1 1 28 28 ALA C C 13 174.49 0.2 . 1 . . . . 25 ALA C . 10010 1 126 . 1 1 28 28 ALA CA C 13 51.26 0.2 . 1 . . . . 25 ALA CA . 10010 1 127 . 1 1 28 28 ALA CB C 13 24.85 0.2 . 1 . . . . 25 ALA CB . 10010 1 128 . 1 1 28 28 ALA N N 15 123.72 0.1 . 1 . . . . 25 ALA N . 10010 1 129 . 1 1 29 29 ALA H H 1 8.64 0.02 . 1 . . . . 26 ALA H . 10010 1 130 . 1 1 29 29 ALA C C 13 178.13 0.2 . 1 . . . . 26 ALA C . 10010 1 131 . 1 1 29 29 ALA CA C 13 51.07 0.2 . 1 . . . . 26 ALA CA . 10010 1 132 . 1 1 29 29 ALA CB C 13 25.27 0.2 . 1 . . . . 26 ALA CB . 10010 1 133 . 1 1 29 29 ALA N N 15 119.86 0.1 . 1 . . . . 26 ALA N . 10010 1 134 . 1 1 30 30 SER H H 1 8.96 0.02 . 1 . . . . 27 SER H . 10010 1 135 . 1 1 30 30 SER C C 13 173.65 0.2 . 1 . . . . 27 SER C . 10010 1 136 . 1 1 30 30 SER CA C 13 60.24 0.2 . 1 . . . . 27 SER CA . 10010 1 137 . 1 1 30 30 SER CB C 13 63.8 0.2 . 1 . . . . 27 SER CB . 10010 1 138 . 1 1 30 30 SER N N 15 116.44 0.1 . 1 . . . . 27 SER N . 10010 1 139 . 1 1 31 31 ASP H H 1 7.2 0.02 . 1 . . . . 28 ASP H . 10010 1 140 . 1 1 31 31 ASP C C 13 176.66 0.2 . 1 . . . . 28 ASP C . 10010 1 141 . 1 1 31 31 ASP CA C 13 52.68 0.2 . 1 . . . . 28 ASP CA . 10010 1 142 . 1 1 31 31 ASP CB C 13 44.4 0.2 . 1 . . . . 28 ASP CB . 10010 1 143 . 1 1 31 31 ASP N N 15 121.59 0.1 . 1 . . . . 28 ASP N . 10010 1 144 . 1 1 32 32 ILE H H 1 9.14 0.02 . 1 . . . . 29 ILE H . 10010 1 145 . 1 1 32 32 ILE C C 13 177.46 0.2 . 1 . . . . 29 ILE C . 10010 1 146 . 1 1 32 32 ILE CA C 13 65.78 0.2 . 1 . . . . 29 ILE CA . 10010 1 147 . 1 1 32 32 ILE CB C 13 39.42 0.2 . 1 . . . . 29 ILE CB . 10010 1 148 . 1 1 32 32 ILE N N 15 126.43 0.1 . 1 . . . . 29 ILE N . 10010 1 149 . 1 1 33 33 SER H H 1 8.55 0.02 . 1 . . . . 30 SER H . 10010 1 150 . 1 1 33 33 SER C C 13 175.79 0.2 . 1 . . . . 30 SER C . 10010 1 151 . 1 1 33 33 SER CA C 13 61.02 0.2 . 1 . . . . 30 SER CA . 10010 1 152 . 1 1 33 33 SER CB C 13 63.42 0.2 . 1 . . . . 30 SER CB . 10010 1 153 . 1 1 33 33 SER N N 15 113.18 0.1 . 1 . . . . 30 SER N . 10010 1 154 . 1 1 34 34 LEU H H 1 7.72 0.02 . 1 . . . . 31 LEU H . 10010 1 155 . 1 1 34 34 LEU C C 13 176.88 0.2 . 1 . . . . 31 LEU C . 10010 1 156 . 1 1 34 34 LEU CA C 13 57.56 0.2 . 1 . . . . 31 LEU CA . 10010 1 157 . 1 1 34 34 LEU CB C 13 41.76 0.2 . 1 . . . . 31 LEU CB . 10010 1 158 . 1 1 34 34 LEU N N 15 119.57 0.1 . 1 . . . . 31 LEU N . 10010 1 159 . 1 1 35 35 LEU H H 1 6.91 0.02 . 1 . . . . 32 LEU H . 10010 1 160 . 1 1 35 35 LEU C C 13 173.87 0.2 . 1 . . . . 32 LEU C . 10010 1 161 . 1 1 35 35 LEU CA C 13 53.98 0.2 . 1 . . . . 32 LEU CA . 10010 1 162 . 1 1 35 35 LEU CB C 13 46.89 0.2 . 1 . . . . 32 LEU CB . 10010 1 163 . 1 1 35 35 LEU N N 15 110.64 0.1 . 1 . . . . 32 LEU N . 10010 1 164 . 1 1 36 36 ASP H H 1 7.55 0.02 . 1 . . . . 33 ASP H . 10010 1 165 . 1 1 36 36 ASP C C 13 175.81 0.2 . 1 . . . . 33 ASP C . 10010 1 166 . 1 1 36 36 ASP CA C 13 56.24 0.2 . 1 . . . . 33 ASP CA . 10010 1 167 . 1 1 36 36 ASP CB C 13 42.14 0.2 . 1 . . . . 33 ASP CB . 10010 1 168 . 1 1 36 36 ASP N N 15 119.58 0.1 . 1 . . . . 33 ASP N . 10010 1 169 . 1 1 37 37 CYS H H 1 8.56 0.02 . 1 . . . . 34 CYS H . 10010 1 170 . 1 1 37 37 CYS C C 13 175.07 0.2 . 1 . . . . 34 CYS C . 10010 1 171 . 1 1 37 37 CYS CA C 13 58.16 0.2 . 1 . . . . 34 CYS CA . 10010 1 172 . 1 1 37 37 CYS CB C 13 45.24 0.2 . 1 . . . . 34 CYS CB . 10010 1 173 . 1 1 37 37 CYS N N 15 121.41 0.1 . 1 . . . . 34 CYS N . 10010 1 174 . 1 1 38 38 GLN H H 1 8.29 0.02 . 1 . . . . 35 GLN H . 10010 1 175 . 1 1 38 38 GLN C C 13 175.82 0.2 . 1 . . . . 35 GLN C . 10010 1 176 . 1 1 38 38 GLN CA C 13 59.25 0.2 . 1 . . . . 35 GLN CA . 10010 1 177 . 1 1 38 38 GLN CB C 13 28.86 0.2 . 1 . . . . 35 GLN CB . 10010 1 178 . 1 1 38 38 GLN N N 15 121.17 0.1 . 1 . . . . 35 GLN N . 10010 1 179 . 1 1 39 39 SER H H 1 7.34 0.02 . 1 . . . . 36 SER H . 10010 1 180 . 1 1 39 39 SER C C 13 174.24 0.2 . 1 . . . . 36 SER C . 10010 1 181 . 1 1 39 39 SER CA C 13 57.25 0.2 . 1 . . . . 36 SER CA . 10010 1 182 . 1 1 39 39 SER CB C 13 63.64 0.2 . 1 . . . . 36 SER CB . 10010 1 183 . 1 1 39 39 SER N N 15 106.73 0.1 . 1 . . . . 36 SER N . 10010 1 184 . 1 1 40 40 ALA H H 1 7.74 0.02 . 1 . . . . 37 ALA H . 10010 1 185 . 1 1 40 40 ALA C C 13 178.03 0.2 . 1 . . . . 37 ALA C . 10010 1 186 . 1 1 40 40 ALA CA C 13 51.69 0.2 . 1 . . . . 37 ALA CA . 10010 1 187 . 1 1 40 40 ALA CB C 13 17.98 0.2 . 1 . . . . 37 ALA CB . 10010 1 188 . 1 1 40 40 ALA N N 15 127.73 0.1 . 1 . . . . 37 ALA N . 10010 1 189 . 1 1 41 41 PRO C C 13 176.69 0.2 . 1 . . . . 38 PRO C . 10010 1 190 . 1 1 41 41 PRO CA C 13 65.15 0.2 . 1 . . . . 38 PRO CA . 10010 1 191 . 1 1 41 41 PRO CB C 13 32.01 0.2 . 1 . . . . 38 PRO CB . 10010 1 192 . 1 1 42 42 LEU H H 1 7.56 0.02 . 1 . . . . 39 LEU H . 10010 1 193 . 1 1 42 42 LEU C C 13 175.72 0.2 . 1 . . . . 39 LEU C . 10010 1 194 . 1 1 42 42 LEU CA C 13 52.08 0.2 . 1 . . . . 39 LEU CA . 10010 1 195 . 1 1 42 42 LEU CB C 13 41.02 0.2 . 1 . . . . 39 LEU CB . 10010 1 196 . 1 1 42 42 LEU N N 15 114.38 0.1 . 1 . . . . 39 LEU N . 10010 1 197 . 1 1 43 43 ARG H H 1 7.08 0.02 . 1 . . . . 40 ARG H . 10010 1 198 . 1 1 43 43 ARG C C 13 172.43 0.2 . 1 . . . . 40 ARG C . 10010 1 199 . 1 1 43 43 ARG CA C 13 55.29 0.2 . 1 . . . . 40 ARG CA . 10010 1 200 . 1 1 43 43 ARG CB C 13 29.62 0.2 . 1 . . . . 40 ARG CB . 10010 1 201 . 1 1 43 43 ARG N N 15 122.41 0.1 . 1 . . . . 40 ARG N . 10010 1 202 . 1 1 44 44 VAL H H 1 7.03 0.02 . 1 . . . . 41 VAL H . 10010 1 203 . 1 1 44 44 VAL C C 13 172.89 0.2 . 1 . . . . 41 VAL C . 10010 1 204 . 1 1 44 44 VAL CA C 13 57.36 0.2 . 1 . . . . 41 VAL CA . 10010 1 205 . 1 1 44 44 VAL CB C 13 34.62 0.2 . 1 . . . . 41 VAL CB . 10010 1 206 . 1 1 44 44 VAL N N 15 115.77 0.1 . 1 . . . . 41 VAL N . 10010 1 207 . 1 1 45 45 TYR H H 1 8.66 0.02 . 1 . . . . 42 TYR H . 10010 1 208 . 1 1 45 45 TYR C C 13 176.17 0.2 . 1 . . . . 42 TYR C . 10010 1 209 . 1 1 45 45 TYR CA C 13 55.33 0.2 . 1 . . . . 42 TYR CA . 10010 1 210 . 1 1 45 45 TYR CB C 13 38.85 0.2 . 1 . . . . 42 TYR CB . 10010 1 211 . 1 1 45 45 TYR N N 15 120.63 0.1 . 1 . . . . 42 TYR N . 10010 1 212 . 1 1 46 46 VAL H H 1 8.65 0.02 . 1 . . . . 43 VAL H . 10010 1 213 . 1 1 46 46 VAL C C 13 174.11 0.2 . 1 . . . . 43 VAL C . 10010 1 214 . 1 1 46 46 VAL CA C 13 64.51 0.2 . 1 . . . . 43 VAL CA . 10010 1 215 . 1 1 46 46 VAL CB C 13 31.92 0.2 . 1 . . . . 43 VAL CB . 10010 1 216 . 1 1 46 46 VAL N N 15 125.34 0.1 . 1 . . . . 43 VAL N . 10010 1 217 . 1 1 47 47 GLU H H 1 8.97 0.02 . 1 . . . . 44 GLU H . 10010 1 218 . 1 1 47 47 GLU C C 13 176.58 0.2 . 1 . . . . 44 GLU C . 10010 1 219 . 1 1 47 47 GLU CA C 13 55.83 0.2 . 1 . . . . 44 GLU CA . 10010 1 220 . 1 1 47 47 GLU CB C 13 32.86 0.2 . 1 . . . . 44 GLU CB . 10010 1 221 . 1 1 47 47 GLU N N 15 122.9 0.1 . 1 . . . . 44 GLU N . 10010 1 222 . 1 1 48 48 GLU H H 1 7.66 0.02 . 1 . . . . 45 GLU H . 10010 1 223 . 1 1 48 48 GLU C C 13 174.01 0.2 . 1 . . . . 45 GLU C . 10010 1 224 . 1 1 48 48 GLU CA C 13 55.48 0.2 . 1 . . . . 45 GLU CA . 10010 1 225 . 1 1 48 48 GLU CB C 13 34.68 0.2 . 1 . . . . 45 GLU CB . 10010 1 226 . 1 1 48 48 GLU N N 15 117.2 0.1 . 1 . . . . 45 GLU N . 10010 1 227 . 1 1 49 49 LEU H H 1 8.66 0.02 . 1 . . . . 46 LEU H . 10010 1 228 . 1 1 49 49 LEU C C 13 176.5 0.2 . 1 . . . . 46 LEU C . 10010 1 229 . 1 1 49 49 LEU CA C 13 53.71 0.2 . 1 . . . . 46 LEU CA . 10010 1 230 . 1 1 49 49 LEU CB C 13 43.8 0.2 . 1 . . . . 46 LEU CB . 10010 1 231 . 1 1 49 49 LEU N N 15 121.98 0.1 . 1 . . . . 46 LEU N . 10010 1 232 . 1 1 50 50 LYS H H 1 9.26 0.02 . 1 . . . . 47 LYS H . 10010 1 233 . 1 1 50 50 LYS C C 13 173.27 0.2 . 1 . . . . 47 LYS C . 10010 1 234 . 1 1 50 50 LYS CA C 13 53.01 0.2 . 1 . . . . 47 LYS CA . 10010 1 235 . 1 1 50 50 LYS CB C 13 34.64 0.2 . 1 . . . . 47 LYS CB . 10010 1 236 . 1 1 50 50 LYS N N 15 123.12 0.1 . 1 . . . . 47 LYS N . 10010 1 237 . 1 1 51 51 PRO C C 13 176.86 0.2 . 1 . . . . 48 PRO C . 10010 1 238 . 1 1 51 51 PRO CA C 13 62.25 0.2 . 1 . . . . 48 PRO CA . 10010 1 239 . 1 1 51 51 PRO CB C 13 32.44 0.2 . 1 . . . . 48 PRO CB . 10010 1 240 . 1 1 52 52 THR H H 1 8.8 0.02 . 1 . . . . 49 THR H . 10010 1 241 . 1 1 52 52 THR C C 13 175.83 0.2 . 1 . . . . 49 THR C . 10010 1 242 . 1 1 52 52 THR CA C 13 59.25 0.2 . 1 . . . . 49 THR CA . 10010 1 243 . 1 1 52 52 THR CB C 13 68.64 0.2 . 1 . . . . 49 THR CB . 10010 1 244 . 1 1 52 52 THR N N 15 115.66 0.1 . 1 . . . . 49 THR N . 10010 1 245 . 1 1 53 53 PRO C C 13 177.79 0.2 . 1 . . . . 50 PRO C . 10010 1 246 . 1 1 53 53 PRO CA C 13 65.36 0.2 . 1 . . . . 50 PRO CA . 10010 1 247 . 1 1 53 53 PRO CB C 13 31.74 0.2 . 1 . . . . 50 PRO CB . 10010 1 248 . 1 1 54 54 GLU H H 1 7.71 0.02 . 1 . . . . 51 GLU H . 10010 1 249 . 1 1 54 54 GLU C C 13 176.86 0.2 . 1 . . . . 51 GLU C . 10010 1 250 . 1 1 54 54 GLU CA C 13 56.83 0.2 . 1 . . . . 51 GLU CA . 10010 1 251 . 1 1 54 54 GLU CB C 13 29.44 0.2 . 1 . . . . 51 GLU CB . 10010 1 252 . 1 1 54 54 GLU N N 15 112.72 0.1 . 1 . . . . 51 GLU N . 10010 1 253 . 1 1 55 55 GLY H H 1 8.3 0.02 . 1 . . . . 52 GLY H . 10010 1 254 . 1 1 55 55 GLY C C 13 174.31 0.2 . 1 . . . . 52 GLY C . 10010 1 255 . 1 1 55 55 GLY CA C 13 45.76 0.2 . 1 . . . . 52 GLY CA . 10010 1 256 . 1 1 55 55 GLY N N 15 108.08 0.1 . 1 . . . . 52 GLY N . 10010 1 257 . 1 1 56 56 ASP H H 1 7.22 0.02 . 1 . . . . 53 ASP H . 10010 1 258 . 1 1 56 56 ASP C C 13 174.17 0.2 . 1 . . . . 53 ASP C . 10010 1 259 . 1 1 56 56 ASP CA C 13 54.09 0.2 . 1 . . . . 53 ASP CA . 10010 1 260 . 1 1 56 56 ASP CB C 13 41.63 0.2 . 1 . . . . 53 ASP CB . 10010 1 261 . 1 1 56 56 ASP N N 15 117.23 0.1 . 1 . . . . 53 ASP N . 10010 1 262 . 1 1 57 57 LEU H H 1 8.94 0.02 . 1 . . . . 54 LEU H . 10010 1 263 . 1 1 57 57 LEU C C 13 174.09 0.2 . 1 . . . . 54 LEU C . 10010 1 264 . 1 1 57 57 LEU CA C 13 54.19 0.2 . 1 . . . . 54 LEU CA . 10010 1 265 . 1 1 57 57 LEU CB C 13 46.38 0.2 . 1 . . . . 54 LEU CB . 10010 1 266 . 1 1 57 57 LEU N N 15 119.44 0.1 . 1 . . . . 54 LEU N . 10010 1 267 . 1 1 58 58 GLU H H 1 8.38 0.02 . 1 . . . . 55 GLU H . 10010 1 268 . 1 1 58 58 GLU C C 13 175.39 0.2 . 1 . . . . 55 GLU C . 10010 1 269 . 1 1 58 58 GLU CA C 13 55.42 0.2 . 1 . . . . 55 GLU CA . 10010 1 270 . 1 1 58 58 GLU CB C 13 30.8 0.2 . 1 . . . . 55 GLU CB . 10010 1 271 . 1 1 58 58 GLU N N 15 126 0.1 . 1 . . . . 55 GLU N . 10010 1 272 . 1 1 59 59 ILE H H 1 9.19 0.02 . 1 . . . . 56 ILE H . 10010 1 273 . 1 1 59 59 ILE C C 13 173.99 0.2 . 1 . . . . 56 ILE C . 10010 1 274 . 1 1 59 59 ILE CA C 13 60.96 0.2 . 1 . . . . 56 ILE CA . 10010 1 275 . 1 1 59 59 ILE CB C 13 39.95 0.2 . 1 . . . . 56 ILE CB . 10010 1 276 . 1 1 59 59 ILE N N 15 125.31 0.1 . 1 . . . . 56 ILE N . 10010 1 277 . 1 1 60 60 LEU H H 1 8.58 0.02 . 1 . . . . 57 LEU H . 10010 1 278 . 1 1 60 60 LEU C C 13 175.71 0.2 . 1 . . . . 57 LEU C . 10010 1 279 . 1 1 60 60 LEU CA C 13 54.78 0.2 . 1 . . . . 57 LEU CA . 10010 1 280 . 1 1 60 60 LEU CB C 13 42.46 0.2 . 1 . . . . 57 LEU CB . 10010 1 281 . 1 1 60 60 LEU N N 15 128.99 0.1 . 1 . . . . 57 LEU N . 10010 1 282 . 1 1 61 61 LEU H H 1 9.09 0.02 . 1 . . . . 58 LEU H . 10010 1 283 . 1 1 61 61 LEU C C 13 175.11 0.2 . 1 . . . . 58 LEU C . 10010 1 284 . 1 1 61 61 LEU CA C 13 53.2 0.2 . 1 . . . . 58 LEU CA . 10010 1 285 . 1 1 61 61 LEU CB C 13 46.25 0.2 . 1 . . . . 58 LEU CB . 10010 1 286 . 1 1 61 61 LEU N N 15 122.94 0.1 . 1 . . . . 58 LEU N . 10010 1 287 . 1 1 62 62 GLN H H 1 9.31 0.02 . 1 . . . . 59 GLN H . 10010 1 288 . 1 1 62 62 GLN C C 13 175.4 0.2 . 1 . . . . 59 GLN C . 10010 1 289 . 1 1 62 62 GLN CA C 13 53.84 0.2 . 1 . . . . 59 GLN CA . 10010 1 290 . 1 1 62 62 GLN CB C 13 31.93 0.2 . 1 . . . . 59 GLN CB . 10010 1 291 . 1 1 62 62 GLN N N 15 118.48 0.1 . 1 . . . . 59 GLN N . 10010 1 292 . 1 1 63 63 LYS H H 1 8.95 0.02 . 1 . . . . 60 LYS H . 10010 1 293 . 1 1 63 63 LYS C C 13 173.72 0.2 . 1 . . . . 60 LYS C . 10010 1 294 . 1 1 63 63 LYS CA C 13 55.34 0.2 . 1 . . . . 60 LYS CA . 10010 1 295 . 1 1 63 63 LYS CB C 13 37.54 0.2 . 1 . . . . 60 LYS CB . 10010 1 296 . 1 1 63 63 LYS N N 15 121.55 0.1 . 1 . . . . 60 LYS N . 10010 1 297 . 1 1 64 64 TRP H H 1 9.67 0.02 . 1 . . . . 61 TRP H . 10010 1 298 . 1 1 64 64 TRP C C 13 175.85 0.2 . 1 . . . . 61 TRP C . 10010 1 299 . 1 1 64 64 TRP CA C 13 57.97 0.2 . 1 . . . . 61 TRP CA . 10010 1 300 . 1 1 64 64 TRP CB C 13 29.84 0.2 . 1 . . . . 61 TRP CB . 10010 1 301 . 1 1 64 64 TRP N N 15 129.37 0.1 . 1 . . . . 61 TRP N . 10010 1 302 . 1 1 65 65 GLU H H 1 8.78 0.02 . 1 . . . . 62 GLU H . 10010 1 303 . 1 1 65 65 GLU C C 13 175.23 0.2 . 1 . . . . 62 GLU C . 10010 1 304 . 1 1 65 65 GLU CA C 13 55.71 0.2 . 1 . . . . 62 GLU CA . 10010 1 305 . 1 1 65 65 GLU CB C 13 32.66 0.2 . 1 . . . . 62 GLU CB . 10010 1 306 . 1 1 65 65 GLU N N 15 128.12 0.1 . 1 . . . . 62 GLU N . 10010 1 307 . 1 1 66 66 ASN H H 1 8.95 0.02 . 1 . . . . 63 ASN H . 10010 1 308 . 1 1 66 66 ASN C C 13 173.89 0.2 . 1 . . . . 63 ASN C . 10010 1 309 . 1 1 66 66 ASN CA C 13 54.92 0.2 . 1 . . . . 63 ASN CA . 10010 1 310 . 1 1 66 66 ASN CB C 13 37.23 0.2 . 1 . . . . 63 ASN CB . 10010 1 311 . 1 1 66 66 ASN N N 15 122.08 0.1 . 1 . . . . 63 ASN N . 10010 1 312 . 1 1 67 67 ASP H H 1 7.9 0.02 . 1 . . . . 64 ASP H . 10010 1 313 . 1 1 67 67 ASP C C 13 173.38 0.2 . 1 . . . . 64 ASP C . 10010 1 314 . 1 1 67 67 ASP CA C 13 55.38 0.2 . 1 . . . . 64 ASP CA . 10010 1 315 . 1 1 67 67 ASP CB C 13 39.8 0.2 . 1 . . . . 64 ASP CB . 10010 1 316 . 1 1 67 67 ASP N N 15 110.86 0.1 . 1 . . . . 64 ASP N . 10010 1 317 . 1 1 68 68 GLU H H 1 6.84 0.02 . 1 . . . . 65 GLU H . 10010 1 318 . 1 1 68 68 GLU C C 13 172.5 0.2 . 1 . . . . 65 GLU C . 10010 1 319 . 1 1 68 68 GLU CA C 13 54.27 0.2 . 1 . . . . 65 GLU CA . 10010 1 320 . 1 1 68 68 GLU CB C 13 32.8 0.2 . 1 . . . . 65 GLU CB . 10010 1 321 . 1 1 68 68 GLU N N 15 115.52 0.1 . 1 . . . . 65 GLU N . 10010 1 322 . 1 1 69 69 CYS H H 1 8.53 0.02 . 1 . . . . 66 CYS H . 10010 1 323 . 1 1 69 69 CYS C C 13 173.54 0.2 . 1 . . . . 66 CYS C . 10010 1 324 . 1 1 69 69 CYS CA C 13 55.23 0.2 . 1 . . . . 66 CYS CA . 10010 1 325 . 1 1 69 69 CYS CB C 13 39.75 0.2 . 1 . . . . 66 CYS CB . 10010 1 326 . 1 1 69 69 CYS N N 15 119.67 0.1 . 1 . . . . 66 CYS N . 10010 1 327 . 1 1 70 70 ALA H H 1 9.05 0.02 . 1 . . . . 67 ALA H . 10010 1 328 . 1 1 70 70 ALA C C 13 176.14 0.2 . 1 . . . . 67 ALA C . 10010 1 329 . 1 1 70 70 ALA CA C 13 51.33 0.2 . 1 . . . . 67 ALA CA . 10010 1 330 . 1 1 70 70 ALA CB C 13 21.5 0.2 . 1 . . . . 67 ALA CB . 10010 1 331 . 1 1 70 70 ALA N N 15 132.85 0.1 . 1 . . . . 67 ALA N . 10010 1 332 . 1 1 71 71 GLN H H 1 8.38 0.02 . 1 . . . . 68 GLN H . 10010 1 333 . 1 1 71 71 GLN C C 13 176.38 0.2 . 1 . . . . 68 GLN C . 10010 1 334 . 1 1 71 71 GLN CA C 13 55.05 0.2 . 1 . . . . 68 GLN CA . 10010 1 335 . 1 1 71 71 GLN CB C 13 31.14 0.2 . 1 . . . . 68 GLN CB . 10010 1 336 . 1 1 71 71 GLN N N 15 119.55 0.1 . 1 . . . . 68 GLN N . 10010 1 337 . 1 1 72 72 LYS H H 1 9.2 0.02 . 1 . . . . 69 LYS H . 10010 1 338 . 1 1 72 72 LYS C C 13 173.91 0.2 . 1 . . . . 69 LYS C . 10010 1 339 . 1 1 72 72 LYS CA C 13 54.08 0.2 . 1 . . . . 69 LYS CA . 10010 1 340 . 1 1 72 72 LYS CB C 13 35.61 0.2 . 1 . . . . 69 LYS CB . 10010 1 341 . 1 1 72 72 LYS N N 15 124.04 0.1 . 1 . . . . 69 LYS N . 10010 1 342 . 1 1 73 73 LYS H H 1 8.41 0.02 . 1 . . . . 70 LYS H . 10010 1 343 . 1 1 73 73 LYS C C 13 175.82 0.2 . 1 . . . . 70 LYS C . 10010 1 344 . 1 1 73 73 LYS CA C 13 55.19 0.2 . 1 . . . . 70 LYS CA . 10010 1 345 . 1 1 73 73 LYS CB C 13 34.67 0.2 . 1 . . . . 70 LYS CB . 10010 1 346 . 1 1 73 73 LYS N N 15 122.76 0.1 . 1 . . . . 70 LYS N . 10010 1 347 . 1 1 74 74 ILE H H 1 9.07 0.02 . 1 . . . . 71 ILE H . 10010 1 348 . 1 1 74 74 ILE C C 13 174.13 0.2 . 1 . . . . 71 ILE C . 10010 1 349 . 1 1 74 74 ILE CA C 13 59.6 0.2 . 1 . . . . 71 ILE CA . 10010 1 350 . 1 1 74 74 ILE CB C 13 41.51 0.2 . 1 . . . . 71 ILE CB . 10010 1 351 . 1 1 74 74 ILE N N 15 125 0.1 . 1 . . . . 71 ILE N . 10010 1 352 . 1 1 75 75 ILE H H 1 8.42 0.02 . 1 . . . . 72 ILE H . 10010 1 353 . 1 1 75 75 ILE C C 13 173.74 0.2 . 1 . . . . 72 ILE C . 10010 1 354 . 1 1 75 75 ILE CA C 13 60.24 0.2 . 1 . . . . 72 ILE CA . 10010 1 355 . 1 1 75 75 ILE CB C 13 37.96 0.2 . 1 . . . . 72 ILE CB . 10010 1 356 . 1 1 75 75 ILE N N 15 125.28 0.1 . 1 . . . . 72 ILE N . 10010 1 357 . 1 1 76 76 ALA H H 1 9.36 0.02 . 1 . . . . 73 ALA H . 10010 1 358 . 1 1 76 76 ALA C C 13 175.52 0.2 . 1 . . . . 73 ALA C . 10010 1 359 . 1 1 76 76 ALA CA C 13 49.65 0.2 . 1 . . . . 73 ALA CA . 10010 1 360 . 1 1 76 76 ALA CB C 13 19.61 0.2 . 1 . . . . 73 ALA CB . 10010 1 361 . 1 1 76 76 ALA N N 15 134 0.1 . 1 . . . . 73 ALA N . 10010 1 362 . 1 1 77 77 GLU H H 1 9.37 0.02 . 1 . . . . 74 GLU H . 10010 1 363 . 1 1 77 77 GLU C C 13 176.82 0.2 . 1 . . . . 74 GLU C . 10010 1 364 . 1 1 77 77 GLU CA C 13 55.36 0.2 . 1 . . . . 74 GLU CA . 10010 1 365 . 1 1 77 77 GLU CB C 13 32.45 0.2 . 1 . . . . 74 GLU CB . 10010 1 366 . 1 1 77 77 GLU N N 15 125.29 0.1 . 1 . . . . 74 GLU N . 10010 1 367 . 1 1 78 78 LYS H H 1 9.23 0.02 . 1 . . . . 75 LYS H . 10010 1 368 . 1 1 78 78 LYS C C 13 175.91 0.2 . 1 . . . . 75 LYS C . 10010 1 369 . 1 1 78 78 LYS CA C 13 57.32 0.2 . 1 . . . . 75 LYS CA . 10010 1 370 . 1 1 78 78 LYS CB C 13 32.17 0.2 . 1 . . . . 75 LYS CB . 10010 1 371 . 1 1 78 78 LYS N N 15 124.05 0.1 . 1 . . . . 75 LYS N . 10010 1 372 . 1 1 79 79 THR H H 1 8.36 0.02 . 1 . . . . 76 THR H . 10010 1 373 . 1 1 79 79 THR C C 13 174.56 0.2 . 1 . . . . 76 THR C . 10010 1 374 . 1 1 79 79 THR CA C 13 60.15 0.2 . 1 . . . . 76 THR CA . 10010 1 375 . 1 1 79 79 THR CB C 13 72.2 0.2 . 1 . . . . 76 THR CB . 10010 1 376 . 1 1 79 79 THR N N 15 112.06 0.1 . 1 . . . . 76 THR N . 10010 1 377 . 1 1 80 80 LYS H H 1 8.24 0.02 . 1 . . . . 77 LYS H . 10010 1 378 . 1 1 80 80 LYS C C 13 176.17 0.2 . 1 . . . . 77 LYS C . 10010 1 379 . 1 1 80 80 LYS CA C 13 57.54 0.2 . 1 . . . . 77 LYS CA . 10010 1 380 . 1 1 80 80 LYS CB C 13 32.18 0.2 . 1 . . . . 77 LYS CB . 10010 1 381 . 1 1 80 80 LYS N N 15 116.17 0.1 . 1 . . . . 77 LYS N . 10010 1 382 . 1 1 81 81 ILE H H 1 8.05 0.02 . 1 . . . . 78 ILE H . 10010 1 383 . 1 1 81 81 ILE C C 13 174.81 0.2 . 1 . . . . 78 ILE C . 10010 1 384 . 1 1 81 81 ILE CB C 13 39.1 0.2 . 1 . . . . 78 ILE CB . 10010 1 385 . 1 1 81 81 ILE N N 15 122.55 0.1 . 1 . . . . 78 ILE N . 10010 1 386 . 1 1 82 82 PRO C C 13 175.86 0.2 . 1 . . . . 79 PRO C . 10010 1 387 . 1 1 82 82 PRO CA C 13 64.74 0.2 . 1 . . . . 79 PRO CA . 10010 1 388 . 1 1 83 83 ALA H H 1 7.9 0.02 . 1 . . . . 80 ALA H . 10010 1 389 . 1 1 83 83 ALA C C 13 174.31 0.2 . 1 . . . . 80 ALA C . 10010 1 390 . 1 1 83 83 ALA CA C 13 52.82 0.2 . 1 . . . . 80 ALA CA . 10010 1 391 . 1 1 83 83 ALA CB C 13 19.82 0.2 . 1 . . . . 80 ALA CB . 10010 1 392 . 1 1 83 83 ALA N N 15 115.43 0.1 . 1 . . . . 80 ALA N . 10010 1 393 . 1 1 84 84 VAL H H 1 7.29 0.02 . 1 . . . . 81 VAL H . 10010 1 394 . 1 1 84 84 VAL C C 13 175.08 0.2 . 1 . . . . 81 VAL C . 10010 1 395 . 1 1 84 84 VAL CA C 13 61.99 0.2 . 1 . . . . 81 VAL CA . 10010 1 396 . 1 1 84 84 VAL CB C 13 33.58 0.2 . 1 . . . . 81 VAL CB . 10010 1 397 . 1 1 84 84 VAL N N 15 117.26 0.1 . 1 . . . . 81 VAL N . 10010 1 398 . 1 1 85 85 PHE H H 1 9.61 0.02 . 1 . . . . 82 PHE H . 10010 1 399 . 1 1 85 85 PHE C C 13 174.77 0.2 . 1 . . . . 82 PHE C . 10010 1 400 . 1 1 85 85 PHE CA C 13 55.94 0.2 . 1 . . . . 82 PHE CA . 10010 1 401 . 1 1 85 85 PHE CB C 13 43.66 0.2 . 1 . . . . 82 PHE CB . 10010 1 402 . 1 1 85 85 PHE N N 15 126.89 0.1 . 1 . . . . 82 PHE N . 10010 1 403 . 1 1 86 86 LYS H H 1 9.64 0.02 . 1 . . . . 83 LYS H . 10010 1 404 . 1 1 86 86 LYS C C 13 176.36 0.2 . 1 . . . . 83 LYS C . 10010 1 405 . 1 1 86 86 LYS CA C 13 55.67 0.2 . 1 . . . . 83 LYS CA . 10010 1 406 . 1 1 86 86 LYS CB C 13 34.81 0.2 . 1 . . . . 83 LYS CB . 10010 1 407 . 1 1 86 86 LYS N N 15 124.08 0.1 . 1 . . . . 83 LYS N . 10010 1 408 . 1 1 87 87 ILE H H 1 7.72 0.02 . 1 . . . . 84 ILE H . 10010 1 409 . 1 1 87 87 ILE C C 13 174.6 0.2 . 1 . . . . 84 ILE C . 10010 1 410 . 1 1 87 87 ILE CA C 13 59.43 0.2 . 1 . . . . 84 ILE CA . 10010 1 411 . 1 1 87 87 ILE CB C 13 43.88 0.2 . 1 . . . . 84 ILE CB . 10010 1 412 . 1 1 87 87 ILE N N 15 116.93 0.1 . 1 . . . . 84 ILE N . 10010 1 413 . 1 1 88 88 ASP H H 1 8.75 0.02 . 1 . . . . 85 ASP H . 10010 1 414 . 1 1 88 88 ASP C C 13 174.04 0.2 . 1 . . . . 85 ASP C . 10010 1 415 . 1 1 88 88 ASP CA C 13 53.6 0.2 . 1 . . . . 85 ASP CA . 10010 1 416 . 1 1 88 88 ASP CB C 13 40.87 0.2 . 1 . . . . 85 ASP CB . 10010 1 417 . 1 1 88 88 ASP N N 15 120.56 0.1 . 1 . . . . 85 ASP N . 10010 1 418 . 1 1 89 89 ALA H H 1 7.2 0.02 . 1 . . . . 86 ALA H . 10010 1 419 . 1 1 89 89 ALA C C 13 175.91 0.2 . 1 . . . . 86 ALA C . 10010 1 420 . 1 1 89 89 ALA CA C 13 51.88 0.2 . 1 . . . . 86 ALA CA . 10010 1 421 . 1 1 89 89 ALA CB C 13 22.72 0.2 . 1 . . . . 86 ALA CB . 10010 1 422 . 1 1 89 89 ALA N N 15 121.96 0.1 . 1 . . . . 86 ALA N . 10010 1 423 . 1 1 90 90 LEU H H 1 8.99 0.02 . 1 . . . . 87 LEU H . 10010 1 424 . 1 1 90 90 LEU C C 13 175.89 0.2 . 1 . . . . 87 LEU C . 10010 1 425 . 1 1 90 90 LEU CA C 13 55.66 0.2 . 1 . . . . 87 LEU CA . 10010 1 426 . 1 1 90 90 LEU CB C 13 38.52 0.2 . 1 . . . . 87 LEU CB . 10010 1 427 . 1 1 90 90 LEU N N 15 114.61 0.1 . 1 . . . . 87 LEU N . 10010 1 428 . 1 1 91 91 ASN H H 1 8.71 0.02 . 1 . . . . 88 ASN H . 10010 1 429 . 1 1 91 91 ASN C C 13 174.45 0.2 . 1 . . . . 88 ASN C . 10010 1 430 . 1 1 91 91 ASN CA C 13 55.2 0.2 . 1 . . . . 88 ASN CA . 10010 1 431 . 1 1 91 91 ASN CB C 13 38.23 0.2 . 1 . . . . 88 ASN CB . 10010 1 432 . 1 1 91 91 ASN N N 15 111.07 0.1 . 1 . . . . 88 ASN N . 10010 1 433 . 1 1 92 92 GLU H H 1 8.28 0.02 . 1 . . . . 89 GLU H . 10010 1 434 . 1 1 92 92 GLU C C 13 176.3 0.2 . 1 . . . . 89 GLU C . 10010 1 435 . 1 1 92 92 GLU CA C 13 53.97 0.2 . 1 . . . . 89 GLU CA . 10010 1 436 . 1 1 92 92 GLU CB C 13 32.43 0.2 . 1 . . . . 89 GLU CB . 10010 1 437 . 1 1 92 92 GLU N N 15 117.17 0.1 . 1 . . . . 89 GLU N . 10010 1 438 . 1 1 93 93 ASN H H 1 9.16 0.02 . 1 . . . . 90 ASN H . 10010 1 439 . 1 1 93 93 ASN C C 13 176.71 0.2 . 1 . . . . 90 ASN C . 10010 1 440 . 1 1 93 93 ASN CA C 13 52.99 0.2 . 1 . . . . 90 ASN CA . 10010 1 441 . 1 1 93 93 ASN CB C 13 40.25 0.2 . 1 . . . . 90 ASN CB . 10010 1 442 . 1 1 93 93 ASN N N 15 115.34 0.1 . 1 . . . . 90 ASN N . 10010 1 443 . 1 1 94 94 LYS H H 1 8.51 0.02 . 1 . . . . 91 LYS H . 10010 1 444 . 1 1 94 94 LYS C C 13 175.32 0.2 . 1 . . . . 91 LYS C . 10010 1 445 . 1 1 94 94 LYS CA C 13 55.52 0.2 . 1 . . . . 91 LYS CA . 10010 1 446 . 1 1 94 94 LYS CB C 13 37.95 0.2 . 1 . . . . 91 LYS CB . 10010 1 447 . 1 1 94 94 LYS N N 15 121.56 0.1 . 1 . . . . 91 LYS N . 10010 1 448 . 1 1 95 95 VAL H H 1 9.02 0.02 . 1 . . . . 92 VAL H . 10010 1 449 . 1 1 95 95 VAL C C 13 173.95 0.2 . 1 . . . . 92 VAL C . 10010 1 450 . 1 1 95 95 VAL CA C 13 61.31 0.2 . 1 . . . . 92 VAL CA . 10010 1 451 . 1 1 95 95 VAL CB C 13 35.09 0.2 . 1 . . . . 92 VAL CB . 10010 1 452 . 1 1 95 95 VAL N N 15 121.25 0.1 . 1 . . . . 92 VAL N . 10010 1 453 . 1 1 96 96 LEU H H 1 9.51 0.02 . 1 . . . . 93 LEU H . 10010 1 454 . 1 1 96 96 LEU C C 13 176.22 0.2 . 1 . . . . 93 LEU C . 10010 1 455 . 1 1 96 96 LEU CA C 13 53.88 0.2 . 1 . . . . 93 LEU CA . 10010 1 456 . 1 1 96 96 LEU CB C 13 44.51 0.2 . 1 . . . . 93 LEU CB . 10010 1 457 . 1 1 96 96 LEU N N 15 126.01 0.1 . 1 . . . . 93 LEU N . 10010 1 458 . 1 1 97 97 VAL H H 1 9.3 0.02 . 1 . . . . 94 VAL H . 10010 1 459 . 1 1 97 97 VAL C C 13 175.04 0.2 . 1 . . . . 94 VAL C . 10010 1 460 . 1 1 97 97 VAL CA C 13 63.57 0.2 . 1 . . . . 94 VAL CA . 10010 1 461 . 1 1 97 97 VAL CB C 13 31.66 0.2 . 1 . . . . 94 VAL CB . 10010 1 462 . 1 1 97 97 VAL N N 15 123.74 0.1 . 1 . . . . 94 VAL N . 10010 1 463 . 1 1 98 98 LEU H H 1 8.55 0.02 . 1 . . . . 95 LEU H . 10010 1 464 . 1 1 98 98 LEU C C 13 176.75 0.2 . 1 . . . . 95 LEU C . 10010 1 465 . 1 1 98 98 LEU CA C 13 57.82 0.2 . 1 . . . . 95 LEU CA . 10010 1 466 . 1 1 98 98 LEU CB C 13 42.73 0.2 . 1 . . . . 95 LEU CB . 10010 1 467 . 1 1 98 98 LEU N N 15 128.08 0.1 . 1 . . . . 95 LEU N . 10010 1 468 . 1 1 99 99 ASP H H 1 7.25 0.02 . 1 . . . . 96 ASP H . 10010 1 469 . 1 1 99 99 ASP C C 13 174.18 0.2 . 1 . . . . 96 ASP C . 10010 1 470 . 1 1 99 99 ASP CA C 13 54.85 0.2 . 1 . . . . 96 ASP CA . 10010 1 471 . 1 1 99 99 ASP CB C 13 44.33 0.2 . 1 . . . . 96 ASP CB . 10010 1 472 . 1 1 99 99 ASP N N 15 110.55 0.1 . 1 . . . . 96 ASP N . 10010 1 473 . 1 1 100 100 THR H H 1 7.76 0.02 . 1 . . . . 97 THR H . 10010 1 474 . 1 1 100 100 THR C C 13 169.55 0.2 . 1 . . . . 97 THR C . 10010 1 475 . 1 1 100 100 THR CA C 13 60.38 0.2 . 1 . . . . 97 THR CA . 10010 1 476 . 1 1 100 100 THR CB C 13 69.22 0.2 . 1 . . . . 97 THR CB . 10010 1 477 . 1 1 100 100 THR N N 15 119.07 0.1 . 1 . . . . 97 THR N . 10010 1 478 . 1 1 101 101 ASP H H 1 6.87 0.02 . 1 . . . . 98 ASP H . 10010 1 479 . 1 1 101 101 ASP C C 13 179.46 0.2 . 1 . . . . 98 ASP C . 10010 1 480 . 1 1 101 101 ASP CA C 13 52.66 0.2 . 1 . . . . 98 ASP CA . 10010 1 481 . 1 1 101 101 ASP CB C 13 42.29 0.2 . 1 . . . . 98 ASP CB . 10010 1 482 . 1 1 101 101 ASP N N 15 123.8 0.1 . 1 . . . . 98 ASP N . 10010 1 483 . 1 1 102 102 TYR H H 1 9.03 0.02 . 1 . . . . 99 TYR H . 10010 1 484 . 1 1 102 102 TYR C C 13 176.59 0.2 . 1 . . . . 99 TYR C . 10010 1 485 . 1 1 102 102 TYR CA C 13 65.05 0.2 . 1 . . . . 99 TYR CA . 10010 1 486 . 1 1 102 102 TYR CB C 13 36.77 0.2 . 1 . . . . 99 TYR CB . 10010 1 487 . 1 1 102 102 TYR N N 15 117.51 0.1 . 1 . . . . 99 TYR N . 10010 1 488 . 1 1 103 103 LYS H H 1 9.05 0.02 . 1 . . . . 100 LYS H . 10010 1 489 . 1 1 103 103 LYS C C 13 176.25 0.2 . 1 . . . . 100 LYS C . 10010 1 490 . 1 1 103 103 LYS CA C 13 56.84 0.2 . 1 . . . . 100 LYS CA . 10010 1 491 . 1 1 103 103 LYS CB C 13 34.53 0.2 . 1 . . . . 100 LYS CB . 10010 1 492 . 1 1 103 103 LYS N N 15 119.95 0.1 . 1 . . . . 100 LYS N . 10010 1 493 . 1 1 104 104 LYS H H 1 9.75 0.02 . 1 . . . . 101 LYS H . 10010 1 494 . 1 1 104 104 LYS C C 13 175.88 0.2 . 1 . . . . 101 LYS C . 10010 1 495 . 1 1 104 104 LYS CA C 13 59.47 0.2 . 1 . . . . 101 LYS CA . 10010 1 496 . 1 1 104 104 LYS CB C 13 35.59 0.2 . 1 . . . . 101 LYS CB . 10010 1 497 . 1 1 104 104 LYS N N 15 121.68 0.1 . 1 . . . . 101 LYS N . 10010 1 498 . 1 1 105 105 TYR H H 1 9.19 0.02 . 1 . . . . 102 TYR H . 10010 1 499 . 1 1 105 105 TYR C C 13 174.38 0.2 . 1 . . . . 102 TYR C . 10010 1 500 . 1 1 105 105 TYR CA C 13 56.72 0.2 . 1 . . . . 102 TYR CA . 10010 1 501 . 1 1 105 105 TYR CB C 13 44.16 0.2 . 1 . . . . 102 TYR CB . 10010 1 502 . 1 1 105 105 TYR N N 15 116.6 0.1 . 1 . . . . 102 TYR N . 10010 1 503 . 1 1 106 106 LEU H H 1 9.21 0.02 . 1 . . . . 103 LEU H . 10010 1 504 . 1 1 106 106 LEU C C 13 173.66 0.2 . 1 . . . . 103 LEU C . 10010 1 505 . 1 1 106 106 LEU CA C 13 56.82 0.2 . 1 . . . . 103 LEU CA . 10010 1 506 . 1 1 106 106 LEU CB C 13 44.31 0.2 . 1 . . . . 103 LEU CB . 10010 1 507 . 1 1 106 106 LEU N N 15 124.97 0.1 . 1 . . . . 103 LEU N . 10010 1 508 . 1 1 107 107 LEU H H 1 9.41 0.02 . 1 . . . . 104 LEU H . 10010 1 509 . 1 1 107 107 LEU C C 13 176.35 0.2 . 1 . . . . 104 LEU C . 10010 1 510 . 1 1 107 107 LEU CA C 13 52.65 0.2 . 1 . . . . 104 LEU CA . 10010 1 511 . 1 1 107 107 LEU CB C 13 44.04 0.2 . 1 . . . . 104 LEU CB . 10010 1 512 . 1 1 107 107 LEU N N 15 124.82 0.1 . 1 . . . . 104 LEU N . 10010 1 513 . 1 1 108 108 PHE H H 1 8.92 0.02 . 1 . . . . 105 PHE H . 10010 1 514 . 1 1 108 108 PHE C C 13 172.27 0.2 . 1 . . . . 105 PHE C . 10010 1 515 . 1 1 108 108 PHE CA C 13 55.95 0.2 . 1 . . . . 105 PHE CA . 10010 1 516 . 1 1 108 108 PHE CB C 13 42.33 0.2 . 1 . . . . 105 PHE CB . 10010 1 517 . 1 1 108 108 PHE N N 15 121.51 0.1 . 1 . . . . 105 PHE N . 10010 1 518 . 1 1 109 109 CYS H H 1 9.63 0.02 . 1 . . . . 106 CYS H . 10010 1 519 . 1 1 109 109 CYS C C 13 172.8 0.2 . 1 . . . . 106 CYS C . 10010 1 520 . 1 1 109 109 CYS CA C 13 55.74 0.2 . 1 . . . . 106 CYS CA . 10010 1 521 . 1 1 109 109 CYS CB C 13 49.56 0.2 . 1 . . . . 106 CYS CB . 10010 1 522 . 1 1 109 109 CYS N N 15 117.1 0.1 . 1 . . . . 106 CYS N . 10010 1 523 . 1 1 110 110 MET H H 1 9.97 0.02 . 1 . . . . 107 MET H . 10010 1 524 . 1 1 110 110 MET C C 13 173.22 0.2 . 1 . . . . 107 MET C . 10010 1 525 . 1 1 110 110 MET CA C 13 54.58 0.2 . 1 . . . . 107 MET CA . 10010 1 526 . 1 1 110 110 MET CB C 13 37.54 0.2 . 1 . . . . 107 MET CB . 10010 1 527 . 1 1 110 110 MET N N 15 120.86 0.1 . 1 . . . . 107 MET N . 10010 1 528 . 1 1 111 111 GLU H H 1 8.29 0.02 . 1 . . . . 108 GLU H . 10010 1 529 . 1 1 111 111 GLU C C 13 174.61 0.2 . 1 . . . . 108 GLU C . 10010 1 530 . 1 1 111 111 GLU CA C 13 55.21 0.2 . 1 . . . . 108 GLU CA . 10010 1 531 . 1 1 111 111 GLU CB C 13 33.62 0.2 . 1 . . . . 108 GLU CB . 10010 1 532 . 1 1 111 111 GLU N N 15 113.83 0.1 . 1 . . . . 108 GLU N . 10010 1 533 . 1 1 112 112 ASN H H 1 9.13 0.02 . 1 . . . . 109 ASN H . 10010 1 534 . 1 1 112 112 ASN C C 13 177.29 0.2 . 1 . . . . 109 ASN C . 10010 1 535 . 1 1 112 112 ASN CA C 13 52.08 0.2 . 1 . . . . 109 ASN CA . 10010 1 536 . 1 1 112 112 ASN CB C 13 38.89 0.2 . 1 . . . . 109 ASN CB . 10010 1 537 . 1 1 112 112 ASN N N 15 119.8 0.1 . 1 . . . . 109 ASN N . 10010 1 538 . 1 1 113 113 SER H H 1 9.67 0.02 . 1 . . . . 110 SER H . 10010 1 539 . 1 1 113 113 SER C C 13 174.66 0.2 . 1 . . . . 110 SER C . 10010 1 540 . 1 1 113 113 SER CA C 13 61 0.2 . 1 . . . . 110 SER CA . 10010 1 541 . 1 1 113 113 SER CB C 13 63.18 0.2 . 1 . . . . 110 SER CB . 10010 1 542 . 1 1 113 113 SER N N 15 121.2 0.1 . 1 . . . . 110 SER N . 10010 1 543 . 1 1 114 114 ALA H H 1 8.24 0.02 . 1 . . . . 111 ALA H . 10010 1 544 . 1 1 114 114 ALA C C 13 178.43 0.2 . 1 . . . . 111 ALA C . 10010 1 545 . 1 1 114 114 ALA CA C 13 53.82 0.2 . 1 . . . . 111 ALA CA . 10010 1 546 . 1 1 114 114 ALA CB C 13 19.44 0.2 . 1 . . . . 111 ALA CB . 10010 1 547 . 1 1 114 114 ALA N N 15 122.92 0.1 . 1 . . . . 111 ALA N . 10010 1 548 . 1 1 115 115 GLU H H 1 7.66 0.02 . 1 . . . . 112 GLU H . 10010 1 549 . 1 1 115 115 GLU C C 13 175.11 0.2 . 1 . . . . 112 GLU C . 10010 1 550 . 1 1 115 115 GLU CB C 13 29.89 0.2 . 1 . . . . 112 GLU CB . 10010 1 551 . 1 1 115 115 GLU N N 15 114.44 0.1 . 1 . . . . 112 GLU N . 10010 1 552 . 1 1 116 116 PRO C C 13 178.43 0.2 . 1 . . . . 113 PRO C . 10010 1 553 . 1 1 116 116 PRO CA C 13 66.36 0.2 . 1 . . . . 113 PRO CA . 10010 1 554 . 1 1 116 116 PRO CB C 13 31.9 0.2 . 1 . . . . 113 PRO CB . 10010 1 555 . 1 1 117 117 GLU H H 1 8.69 0.02 . 1 . . . . 114 GLU H . 10010 1 556 . 1 1 117 117 GLU C C 13 178.68 0.2 . 1 . . . . 114 GLU C . 10010 1 557 . 1 1 117 117 GLU CA C 13 59.62 0.2 . 1 . . . . 114 GLU CA . 10010 1 558 . 1 1 117 117 GLU CB C 13 29 0.2 . 1 . . . . 114 GLU CB . 10010 1 559 . 1 1 117 117 GLU N N 15 114.5 0.1 . 1 . . . . 114 GLU N . 10010 1 560 . 1 1 118 118 GLN H H 1 7.63 0.02 . 1 . . . . 115 GLN H . 10010 1 561 . 1 1 118 118 GLN C C 13 175.84 0.2 . 1 . . . . 115 GLN C . 10010 1 562 . 1 1 118 118 GLN CA C 13 56.42 0.2 . 1 . . . . 115 GLN CA . 10010 1 563 . 1 1 118 118 GLN CB C 13 29.42 0.2 . 1 . . . . 115 GLN CB . 10010 1 564 . 1 1 118 118 GLN N N 15 116.61 0.1 . 1 . . . . 115 GLN N . 10010 1 565 . 1 1 119 119 SER H H 1 7.68 0.02 . 1 . . . . 116 SER H . 10010 1 566 . 1 1 119 119 SER C C 13 173.2 0.2 . 1 . . . . 116 SER C . 10010 1 567 . 1 1 119 119 SER CA C 13 58.69 0.2 . 1 . . . . 116 SER CA . 10010 1 568 . 1 1 119 119 SER CB C 13 65.73 0.2 . 1 . . . . 116 SER CB . 10010 1 569 . 1 1 119 119 SER N N 15 110.49 0.1 . 1 . . . . 116 SER N . 10010 1 570 . 1 1 120 120 LEU H H 1 7.36 0.02 . 1 . . . . 117 LEU H . 10010 1 571 . 1 1 120 120 LEU C C 13 175.75 0.2 . 1 . . . . 117 LEU C . 10010 1 572 . 1 1 120 120 LEU CA C 13 56.66 0.2 . 1 . . . . 117 LEU CA . 10010 1 573 . 1 1 120 120 LEU CB C 13 42.99 0.2 . 1 . . . . 117 LEU CB . 10010 1 574 . 1 1 120 120 LEU N N 15 127.26 0.1 . 1 . . . . 117 LEU N . 10010 1 575 . 1 1 121 121 VAL H H 1 8.8 0.02 . 1 . . . . 118 VAL H . 10010 1 576 . 1 1 121 121 VAL C C 13 174.68 0.2 . 1 . . . . 118 VAL C . 10010 1 577 . 1 1 121 121 VAL CA C 13 60.05 0.2 . 1 . . . . 118 VAL CA . 10010 1 578 . 1 1 121 121 VAL CB C 13 35.74 0.2 . 1 . . . . 118 VAL CB . 10010 1 579 . 1 1 121 121 VAL N N 15 125.66 0.1 . 1 . . . . 118 VAL N . 10010 1 580 . 1 1 122 122 CYS H H 1 9.53 0.02 . 1 . . . . 119 CYS H . 10010 1 581 . 1 1 122 122 CYS C C 13 173.26 0.2 . 1 . . . . 119 CYS C . 10010 1 582 . 1 1 122 122 CYS CA C 13 55.35 0.2 . 1 . . . . 119 CYS CA . 10010 1 583 . 1 1 122 122 CYS CB C 13 50.23 0.2 . 1 . . . . 119 CYS CB . 10010 1 584 . 1 1 122 122 CYS N N 15 122 0.1 . 1 . . . . 119 CYS N . 10010 1 585 . 1 1 123 123 GLN H H 1 9.31 0.02 . 1 . . . . 120 GLN H . 10010 1 586 . 1 1 123 123 GLN C C 13 173.63 0.2 . 1 . . . . 120 GLN C . 10010 1 587 . 1 1 123 123 GLN CA C 13 55.57 0.2 . 1 . . . . 120 GLN CA . 10010 1 588 . 1 1 123 123 GLN CB C 13 32.77 0.2 . 1 . . . . 120 GLN CB . 10010 1 589 . 1 1 123 123 GLN N N 15 118.48 0.1 . 1 . . . . 120 GLN N . 10010 1 590 . 1 1 124 124 CYS H H 1 7.84 0.02 . 1 . . . . 121 CYS H . 10010 1 591 . 1 1 124 124 CYS C C 13 173 0.2 . 1 . . . . 121 CYS C . 10010 1 592 . 1 1 124 124 CYS CA C 13 56.76 0.2 . 1 . . . . 121 CYS CA . 10010 1 593 . 1 1 124 124 CYS CB C 13 27.62 0.2 . 1 . . . . 121 CYS CB . 10010 1 594 . 1 1 124 124 CYS N N 15 120.03 0.1 . 1 . . . . 121 CYS N . 10010 1 595 . 1 1 125 125 LEU H H 1 9.78 0.02 . 1 . . . . 122 LEU H . 10010 1 596 . 1 1 125 125 LEU C C 13 177.26 0.2 . 1 . . . . 122 LEU C . 10010 1 597 . 1 1 125 125 LEU CA C 13 52.64 0.2 . 1 . . . . 122 LEU CA . 10010 1 598 . 1 1 125 125 LEU CB C 13 44.96 0.2 . 1 . . . . 122 LEU CB . 10010 1 599 . 1 1 125 125 LEU N N 15 128.55 0.1 . 1 . . . . 122 LEU N . 10010 1 600 . 1 1 126 126 VAL H H 1 9.47 0.02 . 1 . . . . 123 VAL H . 10010 1 601 . 1 1 126 126 VAL C C 13 178.2 0.2 . 1 . . . . 123 VAL C . 10010 1 602 . 1 1 126 126 VAL CA C 13 59.26 0.2 . 1 . . . . 123 VAL CA . 10010 1 603 . 1 1 126 126 VAL CB C 13 37.29 0.2 . 1 . . . . 123 VAL CB . 10010 1 604 . 1 1 126 126 VAL N N 15 111.65 0.1 . 1 . . . . 123 VAL N . 10010 1 605 . 1 1 127 127 ARG H H 1 8.05 0.02 . 1 . . . . 124 ARG H . 10010 1 606 . 1 1 127 127 ARG C C 13 176.06 0.2 . 1 . . . . 124 ARG C . 10010 1 607 . 1 1 127 127 ARG CA C 13 57.03 0.2 . 1 . . . . 124 ARG CA . 10010 1 608 . 1 1 127 127 ARG CB C 13 33.72 0.2 . 1 . . . . 124 ARG CB . 10010 1 609 . 1 1 127 127 ARG N N 15 119.59 0.1 . 1 . . . . 124 ARG N . 10010 1 610 . 1 1 128 128 THR H H 1 7.59 0.02 . 1 . . . . 125 THR H . 10010 1 611 . 1 1 128 128 THR C C 13 172.88 0.2 . 1 . . . . 125 THR C . 10010 1 612 . 1 1 128 128 THR CA C 13 57.56 0.2 . 1 . . . . 125 THR CA . 10010 1 613 . 1 1 128 128 THR CB C 13 69.8 0.2 . 1 . . . . 125 THR CB . 10010 1 614 . 1 1 128 128 THR N N 15 108.1 0.1 . 1 . . . . 125 THR N . 10010 1 615 . 1 1 129 129 PRO C C 13 173.45 0.2 . 1 . . . . 126 PRO C . 10010 1 616 . 1 1 129 129 PRO CA C 13 62.21 0.2 . 1 . . . . 126 PRO CA . 10010 1 617 . 1 1 129 129 PRO CB C 13 26.72 0.2 . 1 . . . . 126 PRO CB . 10010 1 618 . 1 1 130 130 GLU H H 1 8.45 0.02 . 1 . . . . 127 GLU H . 10010 1 619 . 1 1 130 130 GLU C C 13 175.23 0.2 . 1 . . . . 127 GLU C . 10010 1 620 . 1 1 130 130 GLU CA C 13 54.34 0.2 . 1 . . . . 127 GLU CA . 10010 1 621 . 1 1 130 130 GLU CB C 13 33.49 0.2 . 1 . . . . 127 GLU CB . 10010 1 622 . 1 1 130 130 GLU N N 15 121.73 0.1 . 1 . . . . 127 GLU N . 10010 1 623 . 1 1 131 131 VAL H H 1 8.64 0.02 . 1 . . . . 128 VAL H . 10010 1 624 . 1 1 131 131 VAL C C 13 174.95 0.2 . 1 . . . . 128 VAL C . 10010 1 625 . 1 1 131 131 VAL CA C 13 64.01 0.2 . 1 . . . . 128 VAL CA . 10010 1 626 . 1 1 131 131 VAL CB C 13 31.44 0.2 . 1 . . . . 128 VAL CB . 10010 1 627 . 1 1 131 131 VAL N N 15 121.26 0.1 . 1 . . . . 128 VAL N . 10010 1 628 . 1 1 132 132 ASP H H 1 6.14 0.02 . 1 . . . . 129 ASP H . 10010 1 629 . 1 1 132 132 ASP C C 13 175.31 0.2 . 1 . . . . 129 ASP C . 10010 1 630 . 1 1 132 132 ASP CA C 13 52.93 0.2 . 1 . . . . 129 ASP CA . 10010 1 631 . 1 1 132 132 ASP CB C 13 43.11 0.2 . 1 . . . . 129 ASP CB . 10010 1 632 . 1 1 132 132 ASP N N 15 126.93 0.1 . 1 . . . . 129 ASP N . 10010 1 633 . 1 1 133 133 ASP H H 1 8.8 0.02 . 1 . . . . 130 ASP H . 10010 1 634 . 1 1 133 133 ASP C C 13 178.65 0.2 . 1 . . . . 130 ASP C . 10010 1 635 . 1 1 133 133 ASP CA C 13 57.77 0.2 . 1 . . . . 130 ASP CA . 10010 1 636 . 1 1 133 133 ASP CB C 13 40.88 0.2 . 1 . . . . 130 ASP CB . 10010 1 637 . 1 1 133 133 ASP N N 15 125.66 0.1 . 1 . . . . 130 ASP N . 10010 1 638 . 1 1 134 134 GLU H H 1 8.19 0.02 . 1 . . . . 131 GLU H . 10010 1 639 . 1 1 134 134 GLU C C 13 178.72 0.2 . 1 . . . . 131 GLU C . 10010 1 640 . 1 1 134 134 GLU CA C 13 59.45 0.2 . 1 . . . . 131 GLU CA . 10010 1 641 . 1 1 134 134 GLU CB C 13 29.12 0.2 . 1 . . . . 131 GLU CB . 10010 1 642 . 1 1 134 134 GLU N N 15 121.84 0.1 . 1 . . . . 131 GLU N . 10010 1 643 . 1 1 135 135 ALA H H 1 8.27 0.02 . 1 . . . . 132 ALA H . 10010 1 644 . 1 1 135 135 ALA C C 13 179.3 0.2 . 1 . . . . 132 ALA C . 10010 1 645 . 1 1 135 135 ALA CA C 13 55.2 0.2 . 1 . . . . 132 ALA CA . 10010 1 646 . 1 1 135 135 ALA CB C 13 18.67 0.2 . 1 . . . . 132 ALA CB . 10010 1 647 . 1 1 135 135 ALA N N 15 123.3 0.1 . 1 . . . . 132 ALA N . 10010 1 648 . 1 1 136 136 LEU H H 1 7.71 0.02 . 1 . . . . 133 LEU H . 10010 1 649 . 1 1 136 136 LEU C C 13 179.27 0.2 . 1 . . . . 133 LEU C . 10010 1 650 . 1 1 136 136 LEU CA C 13 57.93 0.2 . 1 . . . . 133 LEU CA . 10010 1 651 . 1 1 136 136 LEU CB C 13 41.51 0.2 . 1 . . . . 133 LEU CB . 10010 1 652 . 1 1 136 136 LEU N N 15 115.54 0.1 . 1 . . . . 133 LEU N . 10010 1 653 . 1 1 137 137 GLU H H 1 8.03 0.02 . 1 . . . . 134 GLU H . 10010 1 654 . 1 1 137 137 GLU C C 13 179.48 0.2 . 1 . . . . 134 GLU C . 10010 1 655 . 1 1 137 137 GLU CA C 13 59.56 0.2 . 1 . . . . 134 GLU CA . 10010 1 656 . 1 1 137 137 GLU CB C 13 29.14 0.2 . 1 . . . . 134 GLU CB . 10010 1 657 . 1 1 137 137 GLU N N 15 121.78 0.1 . 1 . . . . 134 GLU N . 10010 1 658 . 1 1 138 138 LYS H H 1 8.07 0.02 . 1 . . . . 135 LYS H . 10010 1 659 . 1 1 138 138 LYS C C 13 179.72 0.2 . 1 . . . . 135 LYS C . 10010 1 660 . 1 1 138 138 LYS CA C 13 59.6 0.2 . 1 . . . . 135 LYS CA . 10010 1 661 . 1 1 138 138 LYS CB C 13 32.27 0.2 . 1 . . . . 135 LYS CB . 10010 1 662 . 1 1 138 138 LYS N N 15 119.51 0.1 . 1 . . . . 135 LYS N . 10010 1 663 . 1 1 139 139 PHE H H 1 8.49 0.02 . 1 . . . . 136 PHE H . 10010 1 664 . 1 1 139 139 PHE C C 13 175.56 0.2 . 1 . . . . 136 PHE C . 10010 1 665 . 1 1 139 139 PHE CA C 13 60.47 0.2 . 1 . . . . 136 PHE CA . 10010 1 666 . 1 1 139 139 PHE CB C 13 39.11 0.2 . 1 . . . . 136 PHE CB . 10010 1 667 . 1 1 139 139 PHE N N 15 121.48 0.1 . 1 . . . . 136 PHE N . 10010 1 668 . 1 1 140 140 ASP H H 1 8.44 0.02 . 1 . . . . 137 ASP H . 10010 1 669 . 1 1 140 140 ASP C C 13 179.61 0.2 . 1 . . . . 137 ASP C . 10010 1 670 . 1 1 140 140 ASP CA C 13 57.8 0.2 . 1 . . . . 137 ASP CA . 10010 1 671 . 1 1 140 140 ASP CB C 13 40.91 0.2 . 1 . . . . 137 ASP CB . 10010 1 672 . 1 1 140 140 ASP N N 15 118.42 0.1 . 1 . . . . 137 ASP N . 10010 1 673 . 1 1 141 141 LYS H H 1 8.11 0.02 . 1 . . . . 138 LYS H . 10010 1 674 . 1 1 141 141 LYS C C 13 179.3 0.2 . 1 . . . . 138 LYS C . 10010 1 675 . 1 1 141 141 LYS CA C 13 59.59 0.2 . 1 . . . . 138 LYS CA . 10010 1 676 . 1 1 141 141 LYS CB C 13 32.42 0.2 . 1 . . . . 138 LYS CB . 10010 1 677 . 1 1 141 141 LYS N N 15 118.5 0.1 . 1 . . . . 138 LYS N . 10010 1 678 . 1 1 142 142 ALA H H 1 7.88 0.02 . 1 . . . . 139 ALA H . 10010 1 679 . 1 1 142 142 ALA C C 13 179.25 0.2 . 1 . . . . 139 ALA C . 10010 1 680 . 1 1 142 142 ALA CA C 13 54.26 0.2 . 1 . . . . 139 ALA CA . 10010 1 681 . 1 1 142 142 ALA CB C 13 17.79 0.2 . 1 . . . . 139 ALA CB . 10010 1 682 . 1 1 142 142 ALA N N 15 121.74 0.1 . 1 . . . . 139 ALA N . 10010 1 683 . 1 1 143 143 LEU H H 1 7.46 0.02 . 1 . . . . 140 LEU H . 10010 1 684 . 1 1 143 143 LEU C C 13 178.73 0.2 . 1 . . . . 140 LEU C . 10010 1 685 . 1 1 143 143 LEU CA C 13 55.34 0.2 . 1 . . . . 140 LEU CA . 10010 1 686 . 1 1 143 143 LEU CB C 13 41.44 0.2 . 1 . . . . 140 LEU CB . 10010 1 687 . 1 1 143 143 LEU N N 15 114.71 0.1 . 1 . . . . 140 LEU N . 10010 1 688 . 1 1 144 144 LYS H H 1 7.17 0.02 . 1 . . . . 141 LYS H . 10010 1 689 . 1 1 144 144 LYS C C 13 177 0.2 . 1 . . . . 141 LYS C . 10010 1 690 . 1 1 144 144 LYS CA C 13 59.23 0.2 . 1 . . . . 141 LYS CA . 10010 1 691 . 1 1 144 144 LYS CB C 13 32.46 0.2 . 1 . . . . 141 LYS CB . 10010 1 692 . 1 1 144 144 LYS N N 15 120.19 0.1 . 1 . . . . 141 LYS N . 10010 1 693 . 1 1 145 145 ALA H H 1 7.82 0.02 . 1 . . . . 142 ALA H . 10010 1 694 . 1 1 145 145 ALA C C 13 176.7 0.2 . 1 . . . . 142 ALA C . 10010 1 695 . 1 1 145 145 ALA CA C 13 51.72 0.2 . 1 . . . . 142 ALA CA . 10010 1 696 . 1 1 145 145 ALA CB C 13 19.32 0.2 . 1 . . . . 142 ALA CB . 10010 1 697 . 1 1 145 145 ALA N N 15 117.97 0.1 . 1 . . . . 142 ALA N . 10010 1 698 . 1 1 146 146 LEU H H 1 7.78 0.02 . 1 . . . . 143 LEU H . 10010 1 699 . 1 1 146 146 LEU C C 13 175.92 0.2 . 1 . . . . 143 LEU C . 10010 1 700 . 1 1 146 146 LEU CB C 13 42.71 0.2 . 1 . . . . 143 LEU CB . 10010 1 701 . 1 1 146 146 LEU N N 15 120.02 0.1 . 1 . . . . 143 LEU N . 10010 1 702 . 1 1 147 147 PRO C C 13 174.89 0.2 . 1 . . . . 144 PRO C . 10010 1 703 . 1 1 147 147 PRO CA C 13 62.3 0.2 . 1 . . . . 144 PRO CA . 10010 1 704 . 1 1 147 147 PRO CB C 13 28.25 0.2 . 1 . . . . 144 PRO CB . 10010 1 705 . 1 1 148 148 MET H H 1 7.66 0.02 . 1 . . . . 145 MET H . 10010 1 706 . 1 1 148 148 MET C C 13 177.41 0.2 . 1 . . . . 145 MET C . 10010 1 707 . 1 1 148 148 MET CA C 13 54.3 0.2 . 1 . . . . 145 MET CA . 10010 1 708 . 1 1 148 148 MET CB C 13 32.77 0.2 . 1 . . . . 145 MET CB . 10010 1 709 . 1 1 148 148 MET N N 15 117.94 0.1 . 1 . . . . 145 MET N . 10010 1 710 . 1 1 149 149 HIS H H 1 8.87 0.02 . 1 . . . . 146 HIS H . 10010 1 711 . 1 1 149 149 HIS C C 13 171.66 0.2 . 1 . . . . 146 HIS C . 10010 1 712 . 1 1 149 149 HIS CA C 13 57.19 0.2 . 1 . . . . 146 HIS CA . 10010 1 713 . 1 1 149 149 HIS CB C 13 31.38 0.2 . 1 . . . . 146 HIS CB . 10010 1 714 . 1 1 149 149 HIS N N 15 118.8 0.1 . 1 . . . . 146 HIS N . 10010 1 715 . 1 1 150 150 ILE H H 1 7.68 0.02 . 1 . . . . 147 ILE H . 10010 1 716 . 1 1 150 150 ILE C C 13 172.73 0.2 . 1 . . . . 147 ILE C . 10010 1 717 . 1 1 150 150 ILE CA C 13 59.44 0.2 . 1 . . . . 147 ILE CA . 10010 1 718 . 1 1 150 150 ILE CB C 13 40.58 0.2 . 1 . . . . 147 ILE CB . 10010 1 719 . 1 1 150 150 ILE N N 15 116.3 0.1 . 1 . . . . 147 ILE N . 10010 1 720 . 1 1 151 151 ARG H H 1 8.55 0.02 . 1 . . . . 148 ARG H . 10010 1 721 . 1 1 151 151 ARG C C 13 174.09 0.2 . 1 . . . . 148 ARG C . 10010 1 722 . 1 1 151 151 ARG CA C 13 55.14 0.2 . 1 . . . . 148 ARG CA . 10010 1 723 . 1 1 151 151 ARG CB C 13 34.33 0.2 . 1 . . . . 148 ARG CB . 10010 1 724 . 1 1 151 151 ARG N N 15 125.75 0.1 . 1 . . . . 148 ARG N . 10010 1 725 . 1 1 152 152 LEU H H 1 9.21 0.02 . 1 . . . . 149 LEU H . 10010 1 726 . 1 1 152 152 LEU C C 13 175.67 0.2 . 1 . . . . 149 LEU C . 10010 1 727 . 1 1 152 152 LEU CA C 13 54.42 0.2 . 1 . . . . 149 LEU CA . 10010 1 728 . 1 1 152 152 LEU CB C 13 46.72 0.2 . 1 . . . . 149 LEU CB . 10010 1 729 . 1 1 152 152 LEU N N 15 124.39 0.1 . 1 . . . . 149 LEU N . 10010 1 730 . 1 1 153 153 SER H H 1 8.84 0.02 . 1 . . . . 150 SER H . 10010 1 731 . 1 1 153 153 SER C C 13 173.35 0.2 . 1 . . . . 150 SER C . 10010 1 732 . 1 1 153 153 SER CA C 13 57.21 0.2 . 1 . . . . 150 SER CA . 10010 1 733 . 1 1 153 153 SER CB C 13 65.65 0.2 . 1 . . . . 150 SER CB . 10010 1 734 . 1 1 153 153 SER N N 15 116.5 0.1 . 1 . . . . 150 SER N . 10010 1 735 . 1 1 154 154 PHE H H 1 8.46 0.02 . 1 . . . . 151 PHE H . 10010 1 736 . 1 1 154 154 PHE C C 13 174.13 0.2 . 1 . . . . 151 PHE C . 10010 1 737 . 1 1 154 154 PHE CA C 13 58.41 0.2 . 1 . . . . 151 PHE CA . 10010 1 738 . 1 1 154 154 PHE CB C 13 41.49 0.2 . 1 . . . . 151 PHE CB . 10010 1 739 . 1 1 154 154 PHE N N 15 121.29 0.1 . 1 . . . . 151 PHE N . 10010 1 740 . 1 1 155 155 ASN H H 1 8.66 0.02 . 1 . . . . 152 ASN H . 10010 1 741 . 1 1 155 155 ASN C C 13 174.34 0.2 . 1 . . . . 152 ASN C . 10010 1 742 . 1 1 155 155 ASN CA C 13 50.9 0.2 . 1 . . . . 152 ASN CA . 10010 1 743 . 1 1 155 155 ASN CB C 13 38.11 0.2 . 1 . . . . 152 ASN CB . 10010 1 744 . 1 1 155 155 ASN N N 15 118.63 0.1 . 1 . . . . 152 ASN N . 10010 1 745 . 1 1 156 156 PRO C C 13 177.96 0.2 . 1 . . . . 153 PRO C . 10010 1 746 . 1 1 156 156 PRO CA C 13 66.45 0.2 . 1 . . . . 153 PRO CA . 10010 1 747 . 1 1 156 156 PRO CB C 13 32.18 0.2 . 1 . . . . 153 PRO CB . 10010 1 748 . 1 1 157 157 THR H H 1 7.7 0.02 . 1 . . . . 154 THR H . 10010 1 749 . 1 1 157 157 THR C C 13 176.71 0.2 . 1 . . . . 154 THR C . 10010 1 750 . 1 1 157 157 THR CA C 13 65.43 0.2 . 1 . . . . 154 THR CA . 10010 1 751 . 1 1 157 157 THR CB C 13 68.72 0.2 . 1 . . . . 154 THR CB . 10010 1 752 . 1 1 157 157 THR N N 15 110.84 0.1 . 1 . . . . 154 THR N . 10010 1 753 . 1 1 158 158 GLN H H 1 7.85 0.02 . 1 . . . . 155 GLN H . 10010 1 754 . 1 1 158 158 GLN C C 13 177.74 0.2 . 1 . . . . 155 GLN C . 10010 1 755 . 1 1 158 158 GLN CA C 13 57.87 0.2 . 1 . . . . 155 GLN CA . 10010 1 756 . 1 1 158 158 GLN CB C 13 28.67 0.2 . 1 . . . . 155 GLN CB . 10010 1 757 . 1 1 158 158 GLN N N 15 119.91 0.1 . 1 . . . . 155 GLN N . 10010 1 stop_ save_