data_18695 ####################### # Entry information # ####################### save_entry_information _Entry.Sf_category entry_information _Entry.Sf_framecode entry_information _Entry.ID 18695 _Entry.Title ; Allosteric communication in the KIX domain proceeds through dynamic re-packing of the hydrophobic core ; _Entry.Type macromolecule _Entry.Version_type original _Entry.Submission_date 2012-08-31 _Entry.Accession_date 2012-08-31 _Entry.Last_release_date . _Entry.Original_release_date . _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 SOLUTION _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 Sven Bruschweiler . . . 18695 2 Paul Schanda . . . 18695 3 Robert Konrat . . . 18695 4 Martin Tollinger . . . 18695 stop_ loop_ _SG_project.SG_project_ID _SG_project.Project_name _SG_project.Full_name_of_center _SG_project.Initial_of_center _SG_project.Entry_ID 1 'not applicable' 'not applicable' . 18695 stop_ loop_ _Struct_keywords.Keywords _Struct_keywords.Text _Struct_keywords.Entry_ID 'CREB binding protein' . 18695 'mixed-lineage leukemia activation domain' . 18695 'phosphorylated kinase inducible domain of CREB' . 18695 'ternary complex' . 18695 stop_ loop_ _Data_set.Type _Data_set.Count _Data_set.Entry_ID assigned_chemical_shifts 1 18695 stop_ loop_ _Datum.Type _Datum.Count _Datum.Entry_ID '13C chemical shifts' 323 18695 '15N chemical shifts' 92 18695 '1H chemical shifts' 558 18695 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 2 . . 2014-02-19 2012-08-31 update BMRB 'update entry citation' 18695 1 . . 2013-06-04 2012-08-31 original author 'original release' 18695 stop_ loop_ _Related_entries.Database_name _Related_entries.Database_accession_code _Related_entries.Relationship _Related_entries.Entry_ID BMRB 18694 'KIX domain complex(2)' 18695 PDB 2LXT 'BMRB Entry Tracking System' 18695 stop_ save_ ############### # Citations # ############### save_entry_citation _Citation.Sf_category citations _Citation.Sf_framecode entry_citation _Citation.Entry_ID 18695 _Citation.ID 1 _Citation.Class 'entry citation' _Citation.CAS_abstract_code . _Citation.MEDLINE_UI_code . _Citation.DOI . _Citation.PubMed_ID 23651431 _Citation.Full_citation . _Citation.Title 'Allosteric Communication in the KIX Domain Proceeds through Dynamic Repacking of the Hydrophobic Core.' _Citation.Status published _Citation.Type journal _Citation.Journal_abbrev 'ACS Chem. Biol.' _Citation.Journal_name_full 'ACS chemical biology' _Citation.Journal_volume 8 _Citation.Journal_issue 7 _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 1600 _Citation.Page_last 1610 _Citation.Year 2013 _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 Sven Bruschweiler . . . 18695 1 2 Robert Konrat . . . 18695 1 3 Martin Tollinger . . . 18695 1 stop_ save_ ############################################# # Molecular system (assembly) description # ############################################# save_assembly _Assembly.Sf_category assembly _Assembly.Sf_framecode assembly _Assembly.Entry_ID 18695 _Assembly.ID 1 _Assembly.Name 'KIX domain complex (3)' _Assembly.BMRB_code . _Assembly.Number_of_components 3 _Assembly.Organic_ligands . _Assembly.Metal_ions . _Assembly.Non_standard_bonds . _Assembly.Ambiguous_conformational_states . _Assembly.Ambiguous_chem_comp_sites . _Assembly.Molecules_in_chemical_exchange . _Assembly.Paramagnetic no _Assembly.Thiol_state . _Assembly.Molecular_mass . _Assembly.Enzyme_commission_number . _Assembly.Details . _Assembly.DB_query_date . _Assembly.DB_query_revised_last_date . 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 'KIX domain complex (3), 1' 1 $KIX_1 A . yes native no no . . . 18695 1 2 'KIX domain complex (3), 2' 2 $KIX_2 B . no native no no . . . 18695 1 3 'KIX domain complex (3), 3' 3 $KIX_3 C . yes native no no . . . 18695 1 stop_ save_ #################################### # Biological polymers and ligands # #################################### save_KIX_1 _Entity.Sf_category entity _Entity.Sf_framecode KIX_1 _Entity.Entry_ID 18695 _Entity.ID 1 _Entity.BMRB_code . _Entity.Name KIX_1 _Entity.Type polymer _Entity.Polymer_common_type . _Entity.Polymer_type polypeptide(L) _Entity.Polymer_type_details . _Entity.Polymer_strand_ID A _Entity.Polymer_seq_one_letter_code_can . _Entity.Polymer_seq_one_letter_code ; GVRKGWHEHVTQDLRSHLVH KLVQAIFPTPDPAALKDRRM ENLVAYAKKVEGDMYESANS RDEYYHLLAEKIYKIQKELE EKRRSRL ; _Entity.Target_identifier . _Entity.Polymer_author_defined_seq . _Entity.Polymer_author_seq_details . _Entity.Ambiguous_conformational_states no _Entity.Ambiguous_chem_comp_sites no _Entity.Nstd_monomer no _Entity.Nstd_chirality no _Entity.Nstd_linkage no _Entity.Nonpolymer_comp_ID . _Entity.Nonpolymer_comp_label . _Entity.Number_of_monomers 87 _Entity.Number_of_nonpolymer_components . _Entity.Paramagnetic no _Entity.Thiol_state 'not present' _Entity.Src_method man _Entity.Parent_entity_ID . _Entity.Fragment . _Entity.Mutation . _Entity.EC_number . _Entity.Calc_isoelectric_point . _Entity.Formula_weight 10353.954 _Entity.Formula_weight_exptl . _Entity.Formula_weight_exptl_meth . _Entity.Details . _Entity.DB_query_date . _Entity.DB_query_revised_last_date 2015-11-25 loop_ _Entity_db_link.Ordinal _Entity_db_link.Author_supplied _Entity_db_link.Database_code _Entity_db_link.Accession_code _Entity_db_link.Entry_mol_code _Entity_db_link.Entry_mol_name _Entity_db_link.Entry_experimental_method _Entity_db_link.Entry_structure_resolution _Entity_db_link.Entry_relation_type _Entity_db_link.Entry_details _Entity_db_link.Chimera_segment_ID _Entity_db_link.Seq_query_to_submitted_percent _Entity_db_link.Seq_subject_length _Entity_db_link.Seq_identity _Entity_db_link.Seq_positive _Entity_db_link.Seq_homology_expectation_val _Entity_db_link.Seq_align_begin _Entity_db_link.Seq_align_end _Entity_db_link.Seq_difference_details _Entity_db_link.Seq_alignment_details _Entity_db_link.Entry_ID _Entity_db_link.Entity_ID 1 no BMRB 16851 . KIX . . . . . 100.00 87 100.00 100.00 8.64e-56 . . . . 18695 1 2 no BMRB 18314 . entity_1 . . . . . 100.00 87 100.00 100.00 8.64e-56 . . . . 18695 1 3 no BMRB 18315 . KIX . . . . . 100.00 87 100.00 100.00 8.64e-56 . . . . 18695 1 4 no BMRB 18694 . KIX_1 . . . . . 100.00 87 100.00 100.00 8.64e-56 . . . . 18695 1 5 no PDB 1KDX . "Kix Domain Of Mouse Cbp (Creb Binding Protein) In Complex With Phosphorylated Kinase Inducible Domain (Pkid) Of Rat Creb (Cycli" . . . . . 91.95 81 100.00 100.00 1.80e-50 . . . . 18695 1 6 no PDB 1SB0 . "Solution Structure Of The Kix Domain Of Cbp Bound To The Transactivation Domain Of C-Myb" . . . . . 100.00 87 100.00 100.00 8.64e-56 . . . . 18695 1 7 no PDB 2AGH . "Structural Basis For Cooperative Transcription Factor Binding To The Cbp Coactivator" . . . . . 100.00 87 100.00 100.00 8.64e-56 . . . . 18695 1 8 no PDB 2KWF . "The Structure Of E-Protein Activation Domain 1 Bound To The Kix Domain Of CbpP300 ELUCIDATES LEUKEMIA INDUCTION BY E2A-Pbx1" . . . . . 100.00 87 100.00 100.00 8.64e-56 . . . . 18695 1 9 no PDB 2LQH . "Nmr Structure Of Foxo3a Transactivation Domains (Cr2c-Cr3) In Complex With Cbp Kix Domain (2b3l Conformation)" . . . . . 100.00 87 100.00 100.00 8.64e-56 . . . . 18695 1 10 no PDB 2LQI . "Nmr Structure Of Foxo3a Transactivation Domains (Cr2c-Cr3) In Complex With Cbp Kix Domain (2l3b Conformation)" . . . . . 100.00 87 100.00 100.00 8.64e-56 . . . . 18695 1 11 no PDB 2LXS . "Allosteric Communication In The Kix Domain Proceeds Through Dynamic Re-packing Of The Hydrophobic Core" . . . . . 100.00 87 100.00 100.00 8.64e-56 . . . . 18695 1 12 no PDB 2LXT . "Allosteric Communication In The Kix Domain Proceeds Through Dynamic Re-packing Of The Hydrophobic Core" . . . . . 100.00 87 100.00 100.00 8.64e-56 . . . . 18695 1 13 no DBJ BAE06125 . "CREBBP variant protein [Homo sapiens]" . . . . . 100.00 2404 100.00 100.00 4.26e-51 . . . . 18695 1 14 no DBJ BAG65526 . "unnamed protein product [Homo sapiens]" . . . . . 100.00 1198 100.00 100.00 2.02e-50 . . . . 18695 1 15 no DBJ BAI45616 . "CREB binding protein [synthetic construct]" . . . . . 100.00 2442 100.00 100.00 4.30e-51 . . . . 18695 1 16 no GB AAB28651 . "CREB-binding protein [Mus sp.]" . . . . . 100.00 2441 98.85 100.00 9.48e-51 . . . . 18695 1 17 no GB AAC08447 . "CBP [Homo sapiens]" . . . . . 100.00 555 100.00 100.00 7.56e-55 . . . . 18695 1 18 no GB AAC51331 . "CREB-binding protein [Homo sapiens]" . . . . . 100.00 2442 100.00 100.00 4.30e-51 . . . . 18695 1 19 no GB AAC51770 . "CREB-binding protein [Homo sapiens]" . . . . . 100.00 2442 100.00 100.00 4.30e-51 . . . . 18695 1 20 no GB AAH72594 . "Crebbp protein, partial [Mus musculus]" . . . . . 100.00 1589 100.00 100.00 1.76e-51 . . . . 18695 1 21 no PRF 1923401A . "protein CBP" . . . . . 100.00 2441 97.70 98.85 1.20e-49 . . . . 18695 1 22 no REF NP_001020603 . "CREB-binding protein [Mus musculus]" . . . . . 100.00 2441 100.00 100.00 4.59e-51 . . . . 18695 1 23 no REF NP_001073315 . "CREB-binding protein isoform b [Homo sapiens]" . . . . . 100.00 2404 100.00 100.00 4.26e-51 . . . . 18695 1 24 no REF NP_001157494 . "CREB-binding protein [Bos taurus]" . . . . . 100.00 2435 98.85 98.85 2.85e-50 . . . . 18695 1 25 no REF NP_001247644 . "CREB-binding protein [Macaca mulatta]" . . . . . 100.00 2442 100.00 100.00 4.17e-51 . . . . 18695 1 26 no REF NP_004371 . "CREB-binding protein isoform a [Homo sapiens]" . . . . . 100.00 2442 100.00 100.00 4.30e-51 . . . . 18695 1 27 no SP P45481 . "RecName: Full=CREB-binding protein" . . . . . 100.00 2441 100.00 100.00 4.59e-51 . . . . 18695 1 28 no SP Q6JHU9 . "RecName: Full=CREB-binding protein" . . . . . 100.00 2442 100.00 100.00 4.17e-51 . . . . 18695 1 29 no SP Q92793 . "RecName: Full=CREB-binding protein" . . . . . 100.00 2442 100.00 100.00 4.30e-51 . . . . 18695 1 30 no TPG DAA15549 . "TPA: CREB binding protein [Bos taurus]" . . . . . 100.00 2435 98.85 98.85 2.85e-50 . . . . 18695 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 1 586 GLY . 18695 1 2 587 VAL . 18695 1 3 588 ARG . 18695 1 4 589 LYS . 18695 1 5 590 GLY . 18695 1 6 591 TRP . 18695 1 7 592 HIS . 18695 1 8 593 GLU . 18695 1 9 594 HIS . 18695 1 10 595 VAL . 18695 1 11 596 THR . 18695 1 12 597 GLN . 18695 1 13 598 ASP . 18695 1 14 599 LEU . 18695 1 15 600 ARG . 18695 1 16 601 SER . 18695 1 17 602 HIS . 18695 1 18 603 LEU . 18695 1 19 604 VAL . 18695 1 20 605 HIS . 18695 1 21 606 LYS . 18695 1 22 607 LEU . 18695 1 23 608 VAL . 18695 1 24 609 GLN . 18695 1 25 610 ALA . 18695 1 26 611 ILE . 18695 1 27 612 PHE . 18695 1 28 613 PRO . 18695 1 29 614 THR . 18695 1 30 615 PRO . 18695 1 31 616 ASP . 18695 1 32 617 PRO . 18695 1 33 618 ALA . 18695 1 34 619 ALA . 18695 1 35 620 LEU . 18695 1 36 621 LYS . 18695 1 37 622 ASP . 18695 1 38 623 ARG . 18695 1 39 624 ARG . 18695 1 40 625 MET . 18695 1 41 626 GLU . 18695 1 42 627 ASN . 18695 1 43 628 LEU . 18695 1 44 629 VAL . 18695 1 45 630 ALA . 18695 1 46 631 TYR . 18695 1 47 632 ALA . 18695 1 48 633 LYS . 18695 1 49 634 LYS . 18695 1 50 635 VAL . 18695 1 51 636 GLU . 18695 1 52 637 GLY . 18695 1 53 638 ASP . 18695 1 54 639 MET . 18695 1 55 640 TYR . 18695 1 56 641 GLU . 18695 1 57 642 SER . 18695 1 58 643 ALA . 18695 1 59 644 ASN . 18695 1 60 645 SER . 18695 1 61 646 ARG . 18695 1 62 647 ASP . 18695 1 63 648 GLU . 18695 1 64 649 TYR . 18695 1 65 650 TYR . 18695 1 66 651 HIS . 18695 1 67 652 LEU . 18695 1 68 653 LEU . 18695 1 69 654 ALA . 18695 1 70 655 GLU . 18695 1 71 656 LYS . 18695 1 72 657 ILE . 18695 1 73 658 TYR . 18695 1 74 659 LYS . 18695 1 75 660 ILE . 18695 1 76 661 GLN . 18695 1 77 662 LYS . 18695 1 78 663 GLU . 18695 1 79 664 LEU . 18695 1 80 665 GLU . 18695 1 81 666 GLU . 18695 1 82 667 LYS . 18695 1 83 668 ARG . 18695 1 84 669 ARG . 18695 1 85 670 SER . 18695 1 86 671 ARG . 18695 1 87 672 LEU . 18695 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 . GLY 1 1 18695 1 . VAL 2 2 18695 1 . ARG 3 3 18695 1 . LYS 4 4 18695 1 . GLY 5 5 18695 1 . TRP 6 6 18695 1 . HIS 7 7 18695 1 . GLU 8 8 18695 1 . HIS 9 9 18695 1 . VAL 10 10 18695 1 . THR 11 11 18695 1 . GLN 12 12 18695 1 . ASP 13 13 18695 1 . LEU 14 14 18695 1 . ARG 15 15 18695 1 . SER 16 16 18695 1 . HIS 17 17 18695 1 . LEU 18 18 18695 1 . VAL 19 19 18695 1 . HIS 20 20 18695 1 . LYS 21 21 18695 1 . LEU 22 22 18695 1 . VAL 23 23 18695 1 . GLN 24 24 18695 1 . ALA 25 25 18695 1 . ILE 26 26 18695 1 . PHE 27 27 18695 1 . PRO 28 28 18695 1 . THR 29 29 18695 1 . PRO 30 30 18695 1 . ASP 31 31 18695 1 . PRO 32 32 18695 1 . ALA 33 33 18695 1 . ALA 34 34 18695 1 . LEU 35 35 18695 1 . LYS 36 36 18695 1 . ASP 37 37 18695 1 . ARG 38 38 18695 1 . ARG 39 39 18695 1 . MET 40 40 18695 1 . GLU 41 41 18695 1 . ASN 42 42 18695 1 . LEU 43 43 18695 1 . VAL 44 44 18695 1 . ALA 45 45 18695 1 . TYR 46 46 18695 1 . ALA 47 47 18695 1 . LYS 48 48 18695 1 . LYS 49 49 18695 1 . VAL 50 50 18695 1 . GLU 51 51 18695 1 . GLY 52 52 18695 1 . ASP 53 53 18695 1 . MET 54 54 18695 1 . TYR 55 55 18695 1 . GLU 56 56 18695 1 . SER 57 57 18695 1 . ALA 58 58 18695 1 . ASN 59 59 18695 1 . SER 60 60 18695 1 . ARG 61 61 18695 1 . ASP 62 62 18695 1 . GLU 63 63 18695 1 . TYR 64 64 18695 1 . TYR 65 65 18695 1 . HIS 66 66 18695 1 . LEU 67 67 18695 1 . LEU 68 68 18695 1 . ALA 69 69 18695 1 . GLU 70 70 18695 1 . LYS 71 71 18695 1 . ILE 72 72 18695 1 . TYR 73 73 18695 1 . LYS 74 74 18695 1 . ILE 75 75 18695 1 . GLN 76 76 18695 1 . LYS 77 77 18695 1 . GLU 78 78 18695 1 . LEU 79 79 18695 1 . GLU 80 80 18695 1 . GLU 81 81 18695 1 . LYS 82 82 18695 1 . ARG 83 83 18695 1 . ARG 84 84 18695 1 . SER 85 85 18695 1 . ARG 86 86 18695 1 . LEU 87 87 18695 1 stop_ save_ save_KIX_2 _Entity.Sf_category entity _Entity.Sf_framecode KIX_2 _Entity.Entry_ID 18695 _Entity.ID 2 _Entity.BMRB_code . _Entity.Name KIX_2 _Entity.Type polymer _Entity.Polymer_common_type . _Entity.Polymer_type polypeptide(L) _Entity.Polymer_type_details . _Entity.Polymer_strand_ID B _Entity.Polymer_seq_one_letter_code_can . _Entity.Polymer_seq_one_letter_code DAGNILPSDIMDFVLKNTP _Entity.Target_identifier . _Entity.Polymer_author_defined_seq . _Entity.Polymer_author_seq_details . _Entity.Ambiguous_conformational_states no _Entity.Ambiguous_chem_comp_sites no _Entity.Nstd_monomer no _Entity.Nstd_chirality no _Entity.Nstd_linkage no _Entity.Nonpolymer_comp_ID . _Entity.Nonpolymer_comp_label . _Entity.Number_of_monomers 19 _Entity.Number_of_nonpolymer_components . _Entity.Paramagnetic no _Entity.Thiol_state 'not present' _Entity.Src_method man _Entity.Parent_entity_ID . _Entity.Fragment . _Entity.Mutation . _Entity.EC_number . _Entity.Calc_isoelectric_point . _Entity.Formula_weight 2061.352 _Entity.Formula_weight_exptl . _Entity.Formula_weight_exptl_meth . _Entity.Details . _Entity.DB_query_date . _Entity.DB_query_revised_last_date 2015-01-29 loop_ _Entity_db_link.Ordinal _Entity_db_link.Author_supplied _Entity_db_link.Database_code _Entity_db_link.Accession_code _Entity_db_link.Entry_mol_code _Entity_db_link.Entry_mol_name _Entity_db_link.Entry_experimental_method _Entity_db_link.Entry_structure_resolution _Entity_db_link.Entry_relation_type _Entity_db_link.Entry_details _Entity_db_link.Chimera_segment_ID _Entity_db_link.Seq_query_to_submitted_percent _Entity_db_link.Seq_subject_length _Entity_db_link.Seq_identity _Entity_db_link.Seq_positive _Entity_db_link.Seq_homology_expectation_val _Entity_db_link.Seq_align_begin _Entity_db_link.Seq_align_end _Entity_db_link.Seq_difference_details _Entity_db_link.Seq_alignment_details _Entity_db_link.Entry_ID _Entity_db_link.Entity_ID 1 no BMRB 18694 . KIX_2 . . . . . 100.00 19 100.00 100.00 1.97e-03 . . . . 18695 2 2 no PDB 2LXS . "Allosteric Communication In The Kix Domain Proceeds Through Dynamic Re-packing Of The Hydrophobic Core" . . . . . 100.00 19 100.00 100.00 1.97e-03 . . . . 18695 2 3 no PDB 2LXT . "Allosteric Communication In The Kix Domain Proceeds Through Dynamic Re-packing Of The Hydrophobic Core" . . . . . 100.00 19 100.00 100.00 1.97e-03 . . . . 18695 2 4 no DBJ BAD92745 . "myeloid/lymphoid or mixed-lineage leukemia (trithorax homolog, Drosophila) variant [Homo sapiens]" . . . . . 89.47 2880 100.00 100.00 1.40e-01 . . . . 18695 2 5 no EMBL CAA93625 . "ALL-1 protein [Homo sapiens]" . . . . . 89.47 4005 100.00 100.00 1.21e-01 . . . . 18695 2 6 no GB AAA58669 . "HRX [Homo sapiens]" . . . . . 89.47 3969 100.00 100.00 1.18e-01 . . . . 18695 2 7 no GB AAA62593 . "All-1 protein, partial [Mus musculus domesticus]" . . . . . 89.47 3866 100.00 100.00 1.21e-01 . . . . 18695 2 8 no GB AAQ63624 . "myeloid/lymphoid or mixed-lineage leukemia (trithorax homolog, Drosophila) [Homo sapiens]" . . . . . 89.47 3969 100.00 100.00 1.27e-01 . . . . 18695 2 9 no GB ABM46715 . "MLL [Gorilla gorilla]" . . . . . 89.47 1791 100.00 100.00 3.72e-01 . . . . 18695 2 10 no GB ABM54290 . "MLL [Pan paniscus]" . . . . . 89.47 1598 100.00 100.00 5.02e-01 . . . . 18695 2 11 no PIR A48205 . "All-1 protein +GTE form - mouse (fragment)" . . . . . 89.47 3869 100.00 100.00 1.20e-01 . . . . 18695 2 12 no REF NP_001074518 . "histone-lysine N-methyltransferase 2A [Mus musculus]" . . . . . 89.47 3963 100.00 100.00 1.16e-01 . . . . 18695 2 13 no REF NP_001184033 . "histone-lysine N-methyltransferase 2A isoform 1 precursor [Homo sapiens]" . . . . . 89.47 3972 100.00 100.00 1.27e-01 . . . . 18695 2 14 no REF NP_005924 . "histone-lysine N-methyltransferase 2A isoform 2 precursor [Homo sapiens]" . . . . . 89.47 3969 100.00 100.00 1.27e-01 . . . . 18695 2 15 no REF XP_001093874 . "PREDICTED: histone-lysine N-methyltransferase MLL [Macaca mulatta]" . . . . . 89.47 3986 100.00 100.00 1.17e-01 . . . . 18695 2 16 no REF XP_002188579 . "PREDICTED: histone-lysine N-methyltransferase MLL [Taeniopygia guttata]" . . . . . 89.47 3849 100.00 100.00 9.23e-02 . . . . 18695 2 17 no SP P55200 . "RecName: Full=Histone-lysine N-methyltransferase 2A; Short=Lysine N-methyltransferase 2A; AltName: Full=ALL-1; AltName: Full=My" . . . . . 89.47 3966 100.00 100.00 1.12e-01 . . . . 18695 2 18 no SP Q03164 . "RecName: Full=Histone-lysine N-methyltransferase 2A; Short=Lysine N-methyltransferase 2A; AltName: Full=ALL-1; AltName: Full=CX" . . . . . 89.47 3969 100.00 100.00 1.27e-01 . . . . 18695 2 19 no TPG DAA22311 . "TPA: myeloid/lymphoid or mixed-lineage leukemia-like [Bos taurus]" . . . . . 89.47 3821 100.00 100.00 1.58e-01 . . . . 18695 2 stop_ loop_ _Entity_comp_index.ID _Entity_comp_index.Auth_seq_ID _Entity_comp_index.Comp_ID _Entity_comp_index.Comp_label _Entity_comp_index.Entry_ID _Entity_comp_index.Entity_ID 1 . ASP . 18695 2 2 . ALA . 18695 2 3 . GLY . 18695 2 4 . ASN . 18695 2 5 . ILE . 18695 2 6 . LEU . 18695 2 7 . PRO . 18695 2 8 . SER . 18695 2 9 . ASP . 18695 2 10 . ILE . 18695 2 11 . MET . 18695 2 12 . ASP . 18695 2 13 . PHE . 18695 2 14 . VAL . 18695 2 15 . LEU . 18695 2 16 . LYS . 18695 2 17 . ASN . 18695 2 18 . THR . 18695 2 19 . PRO . 18695 2 stop_ loop_ _Entity_poly_seq.Hetero _Entity_poly_seq.Mon_ID _Entity_poly_seq.Num _Entity_poly_seq.Comp_index_ID _Entity_poly_seq.Entry_ID _Entity_poly_seq.Entity_ID . ASP 1 1 18695 2 . ALA 2 2 18695 2 . GLY 3 3 18695 2 . ASN 4 4 18695 2 . ILE 5 5 18695 2 . LEU 6 6 18695 2 . PRO 7 7 18695 2 . SER 8 8 18695 2 . ASP 9 9 18695 2 . ILE 10 10 18695 2 . MET 11 11 18695 2 . ASP 12 12 18695 2 . PHE 13 13 18695 2 . VAL 14 14 18695 2 . LEU 15 15 18695 2 . LYS 16 16 18695 2 . ASN 17 17 18695 2 . THR 18 18 18695 2 . PRO 19 19 18695 2 stop_ save_ save_KIX_3 _Entity.Sf_category entity _Entity.Sf_framecode KIX_3 _Entity.Entry_ID 18695 _Entity.ID 3 _Entity.BMRB_code . _Entity.Name KIX_3 _Entity.Type polymer _Entity.Polymer_common_type . _Entity.Polymer_type polypeptide(L) _Entity.Polymer_type_details . _Entity.Polymer_strand_ID C _Entity.Polymer_seq_one_letter_code_can . _Entity.Polymer_seq_one_letter_code ; DSVTDSQKRREILSRRPXYR KILNDLSSDAPGVP ; _Entity.Target_identifier . _Entity.Polymer_author_defined_seq . _Entity.Polymer_author_seq_details . _Entity.Ambiguous_conformational_states no _Entity.Ambiguous_chem_comp_sites no _Entity.Nstd_monomer yes _Entity.Nstd_chirality no _Entity.Nstd_linkage no _Entity.Nonpolymer_comp_ID . _Entity.Nonpolymer_comp_label . _Entity.Number_of_monomers 34 _Entity.Number_of_nonpolymer_components . _Entity.Paramagnetic no _Entity.Thiol_state 'not present' _Entity.Src_method man _Entity.Parent_entity_ID . _Entity.Fragment . _Entity.Mutation . _Entity.EC_number . _Entity.Calc_isoelectric_point . _Entity.Formula_weight 3944.323 _Entity.Formula_weight_exptl . _Entity.Formula_weight_exptl_meth . _Entity.Details . _Entity.DB_query_date . _Entity.DB_query_revised_last_date 2015-01-29 loop_ _Entity_db_link.Ordinal _Entity_db_link.Author_supplied _Entity_db_link.Database_code _Entity_db_link.Accession_code _Entity_db_link.Entry_mol_code _Entity_db_link.Entry_mol_name _Entity_db_link.Entry_experimental_method _Entity_db_link.Entry_structure_resolution _Entity_db_link.Entry_relation_type _Entity_db_link.Entry_details _Entity_db_link.Chimera_segment_ID _Entity_db_link.Seq_query_to_submitted_percent _Entity_db_link.Seq_subject_length _Entity_db_link.Seq_identity _Entity_db_link.Seq_positive _Entity_db_link.Seq_homology_expectation_val _Entity_db_link.Seq_align_begin _Entity_db_link.Seq_align_end _Entity_db_link.Seq_difference_details _Entity_db_link.Seq_alignment_details _Entity_db_link.Entry_ID _Entity_db_link.Entity_ID 1 no BMRB 6784 . kinase_inducible_domain_of_CREB . . . . . 100.00 60 97.06 97.06 9.99e-14 . . . . 18695 3 2 no BMRB 6788 . Ser133-phosphorylated_kinase_inducible_domain_of_CREB . . . . . 100.00 60 100.00 100.00 1.19e-13 . . . . 18695 3 3 no PDB 1KDX . "Kix Domain Of Mouse Cbp (Creb Binding Protein) In Complex With Phosphorylated Kinase Inducible Domain (Pkid) Of Rat Creb (Cycli" . . . . . 79.41 28 100.00 100.00 1.50e-07 . . . . 18695 3 4 no PDB 2LXT . "Allosteric Communication In The Kix Domain Proceeds Through Dynamic Re-packing Of The Hydrophobic Core" . . . . . 100.00 34 100.00 100.00 6.11e-13 . . . . 18695 3 5 no DBJ BAA36482 . "CREB [Taeniopygia guttata]" . . . . . 100.00 327 97.06 97.06 4.41e-13 . . . . 18695 3 6 no DBJ BAC32173 . "unnamed protein product [Mus musculus]" . . . . . 100.00 327 97.06 97.06 4.79e-13 . . . . 18695 3 7 no DBJ BAC32174 . "unnamed protein product [Mus musculus]" . . . . . 100.00 327 97.06 97.06 4.79e-13 . . . . 18695 3 8 no DBJ BAG11405 . "cAMP response element-binding protein [synthetic construct]" . . . . . 100.00 341 97.06 97.06 5.72e-13 . . . . 18695 3 9 no DBJ BAG35615 . "unnamed protein product [Homo sapiens]" . . . . . 100.00 341 97.06 97.06 5.72e-13 . . . . 18695 3 10 no EMBL CAA32890 . "unnamed protein product [Rattus norvegicus]" . . . . . 100.00 341 97.06 97.06 6.54e-13 . . . . 18695 3 11 no EMBL CAA39151 . "CREB protein [Homo sapiens]" . . . . . 100.00 341 97.06 97.06 5.72e-13 . . . . 18695 3 12 no EMBL CAA40347 . "CREB2 [Bos taurus]" . . . . . 100.00 325 97.06 97.06 4.53e-13 . . . . 18695 3 13 no EMBL CAA42620 . "delta CREB [Homo sapiens]" . . . . . 100.00 327 97.06 97.06 5.20e-13 . . . . 18695 3 14 no EMBL CAA47953 . "c-AMP-responsive-element binding protein delta [Mus musculus]" . . . . . 100.00 327 97.06 97.06 4.79e-13 . . . . 18695 3 15 no GB AAA35715 . "transactivator protein [Homo sapiens]" . . . . . 100.00 327 97.06 97.06 4.32e-13 . . . . 18695 3 16 no GB AAA35716 . "active transcription factor CREB-A [Homo sapiens]" . . . . . 100.00 327 97.06 97.06 4.32e-13 . . . . 18695 3 17 no GB AAA35717 . "active transcription factor CREB-B [Homo sapiens]" . . . . . 100.00 341 97.06 97.06 5.72e-13 . . . . 18695 3 18 no GB AAA37456 . "cAMP respone element binding protein [Mus musculus]" . . . . . 100.00 341 97.06 97.06 5.96e-13 . . . . 18695 3 19 no GB AAB20597 . "CREB327 [Homo sapiens]" . . . . . 100.00 327 97.06 97.06 4.32e-13 . . . . 18695 3 20 no PIR A40120 . "cAMP-responsive enhancer-binding protein CREB - human" . . . . . 100.00 326 97.06 97.06 4.93e-13 . . . . 18695 3 21 no PRF 1504306A . "cAMP regulated nuclear factor CREB" . . . . . 100.00 341 97.06 97.06 6.54e-13 . . . . 18695 3 22 no REF NP_001017818 . "cyclic AMP-responsive element-binding protein 1 [Danio rerio]" . . . . . 100.00 257 97.06 97.06 2.41e-12 . . . . 18695 3 23 no REF NP_001032815 . "cyclic AMP-responsive element-binding protein 1 isoform C [Mus musculus]" . . . . . 100.00 287 97.06 97.06 4.58e-13 . . . . 18695 3 24 no REF NP_001041721 . "cyclic AMP-responsive element-binding protein 1 [Taeniopygia guttata]" . . . . . 100.00 327 97.06 97.06 4.41e-13 . . . . 18695 3 25 no REF NP_001093399 . "cyclic AMP-responsive element-binding protein 1 [Sus scrofa]" . . . . . 100.00 327 97.06 97.06 4.64e-13 . . . . 18695 3 26 no REF NP_001153276 . "cyclic AMP-responsive element-binding protein 1 [Pongo abelii]" . . . . . 100.00 341 97.06 97.06 5.72e-13 . . . . 18695 3 27 no SP P15337 . "RecName: Full=Cyclic AMP-responsive element-binding protein 1; Short=CREB-1; Short=cAMP-responsive element-binding protein 1 [R" . . . . . 100.00 341 97.06 97.06 6.54e-13 . . . . 18695 3 28 no SP P16220 . "RecName: Full=Cyclic AMP-responsive element-binding protein 1; Short=CREB-1; Short=cAMP-responsive element-binding protein 1 [H" . . . . . 100.00 341 97.06 97.06 5.72e-13 . . . . 18695 3 29 no SP P27925 . "RecName: Full=Cyclic AMP-responsive element-binding protein 1; Short=CREB-1; Short=cAMP-responsive element-binding protein 1; A" . . . . . 100.00 325 97.06 97.06 4.58e-13 . . . . 18695 3 30 no SP Q01147 . "RecName: Full=Cyclic AMP-responsive element-binding protein 1; Short=CREB-1; Short=cAMP-responsive element-binding protein 1 [M" . . . . . 100.00 341 97.06 97.06 5.96e-13 . . . . 18695 3 31 no TPG DAA32469 . "TPA: cyclic AMP-responsive element-binding protein 1 [Bos taurus]" . . . . . 100.00 325 97.06 97.06 4.58e-13 . . . . 18695 3 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 1 116 ASP . 18695 3 2 117 SER . 18695 3 3 118 VAL . 18695 3 4 119 THR . 18695 3 5 120 ASP . 18695 3 6 121 SER . 18695 3 7 122 GLN . 18695 3 8 123 LYS . 18695 3 9 124 ARG . 18695 3 10 125 ARG . 18695 3 11 126 GLU . 18695 3 12 127 ILE . 18695 3 13 128 LEU . 18695 3 14 129 SER . 18695 3 15 130 ARG . 18695 3 16 131 ARG . 18695 3 17 132 PRO . 18695 3 18 133 SEP . 18695 3 19 134 TYR . 18695 3 20 135 ARG . 18695 3 21 136 LYS . 18695 3 22 137 ILE . 18695 3 23 138 LEU . 18695 3 24 139 ASN . 18695 3 25 140 ASP . 18695 3 26 141 LEU . 18695 3 27 142 SER . 18695 3 28 143 SER . 18695 3 29 144 ASP . 18695 3 30 145 ALA . 18695 3 31 146 PRO . 18695 3 32 147 GLY . 18695 3 33 148 VAL . 18695 3 34 149 PRO . 18695 3 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 . ASP 1 1 18695 3 . SER 2 2 18695 3 . VAL 3 3 18695 3 . THR 4 4 18695 3 . ASP 5 5 18695 3 . SER 6 6 18695 3 . GLN 7 7 18695 3 . LYS 8 8 18695 3 . ARG 9 9 18695 3 . ARG 10 10 18695 3 . GLU 11 11 18695 3 . ILE 12 12 18695 3 . LEU 13 13 18695 3 . SER 14 14 18695 3 . ARG 15 15 18695 3 . ARG 16 16 18695 3 . PRO 17 17 18695 3 . SEP 18 18 18695 3 . TYR 19 19 18695 3 . ARG 20 20 18695 3 . LYS 21 21 18695 3 . ILE 22 22 18695 3 . LEU 23 23 18695 3 . ASN 24 24 18695 3 . ASP 25 25 18695 3 . LEU 26 26 18695 3 . SER 27 27 18695 3 . SER 28 28 18695 3 . ASP 29 29 18695 3 . ALA 30 30 18695 3 . PRO 31 31 18695 3 . GLY 32 32 18695 3 . VAL 33 33 18695 3 . PRO 34 34 18695 3 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 18695 _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 $KIX_1 . 9606 organism . 'Homo sapiens' Human . . Eukaryota Metazoa Homo sapiens . . . . . . . . . . . . . . . . . . . . . 18695 1 2 2 $KIX_2 . 9606 organism . 'Homo sapiens' Human . . Eukaryota Metazoa Homo sapiens . . . . . . . . . . . . . . . . . . . . . 18695 1 3 3 $KIX_3 . 9606 organism . 'Homo sapiens' Human . . Eukaryota Metazoa Homo sapiens . . . . . . . . . . . . . . . . . . . . . 18695 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 18695 _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 $KIX_1 . 'recombinant technology' 'Escherichia coli' . . . Escherichia coli . . . . . . . . . . . . . . . . pET-15b . . . . . . 18695 1 2 2 $KIX_2 . 'recombinant technology' 'Escherichia coli' . . . Escherichia coli . . . . . . . . . . . . . . . . pETMBP . . . . . . 18695 1 3 3 $KIX_3 . 'recombinant technology' 'Escherichia coli' . . . Escherichia coli . . . . . . . . . . . . . . . . pETtrx . . . . . . 18695 1 stop_ save_ ################################# # Polymer residues and ligands # ################################# save_chem_comp_SEP _Chem_comp.Sf_category chem_comp _Chem_comp.Sf_framecode chem_comp_SEP _Chem_comp.Entry_ID 18695 _Chem_comp.ID SEP _Chem_comp.Provenance PDB _Chem_comp.Name PHOSPHOSERINE _Chem_comp.Type 'L-PEPTIDE LINKING' _Chem_comp.BMRB_code SEP _Chem_comp.PDB_code SEP _Chem_comp.Ambiguous_flag no _Chem_comp.Initial_date 2012-04-05 _Chem_comp.Modified_date 2012-04-05 _Chem_comp.Release_status REL _Chem_comp.Replaced_by . _Chem_comp.Replaces . _Chem_comp.One_letter_code S _Chem_comp.Three_letter_code SEP _Chem_comp.Number_atoms_all 19 _Chem_comp.Number_atoms_nh 11 _Chem_comp.PubChem_code . _Chem_comp.Subcomponent_list . _Chem_comp.InChI_code InChI=1S/C3H8NO6P/c4-2(3(5)6)1-10-11(7,8)9/h2H,1,4H2,(H,5,6)(H2,7,8,9)/t2-/m0/s1 _Chem_comp.Mon_nstd_flag . _Chem_comp.Mon_nstd_class . _Chem_comp.Mon_nstd_details . _Chem_comp.Mon_nstd_parent . _Chem_comp.Mon_nstd_parent_comp_ID SER _Chem_comp.Std_deriv_one_letter_code . _Chem_comp.Std_deriv_three_letter_code . _Chem_comp.Std_deriv_BMRB_code . _Chem_comp.Std_deriv_PDB_code . _Chem_comp.Std_deriv_chem_comp_name . _Chem_comp.Synonyms PHOSPHONOSERINE _Chem_comp.Formal_charge 0 _Chem_comp.Paramagnetic . _Chem_comp.Aromatic no _Chem_comp.Formula 'C3 H8 N O6 P' _Chem_comp.Formula_weight 185.072 _Chem_comp.Formula_mono_iso_wt_nat . _Chem_comp.Formula_mono_iso_wt_13C . _Chem_comp.Formula_mono_iso_wt_15N . _Chem_comp.Formula_mono_iso_wt_13C_15N . _Chem_comp.Image_file_name . _Chem_comp.Image_file_format . _Chem_comp.Topo_file_name . _Chem_comp.Topo_file_format . _Chem_comp.Struct_file_name . _Chem_comp.Struct_file_format . _Chem_comp.Stereochem_param_file_name . _Chem_comp.Stereochem_param_file_format . _Chem_comp.Model_details . _Chem_comp.Model_erf . _Chem_comp.Model_source . _Chem_comp.Model_coordinates_details . _Chem_comp.Model_coordinates_missing_flag no _Chem_comp.Ideal_coordinates_details . _Chem_comp.Ideal_coordinates_missing_flag no _Chem_comp.Model_coordinates_db_code 1BX6 _Chem_comp.Processing_site RCSB _Chem_comp.Vendor . _Chem_comp.Vendor_product_code . _Chem_comp.Details . _Chem_comp.DB_query_date . _Chem_comp.DB_last_query_revised_last_date . loop_ _Chem_comp_descriptor.Descriptor _Chem_comp_descriptor.Type _Chem_comp_descriptor.Program _Chem_comp_descriptor.Program_version _Chem_comp_descriptor.Entry_ID _Chem_comp_descriptor.Comp_ID BZQFBWGGLXLEPQ-REOHCLBHSA-N InChIKey InChI 1.03 18695 SEP C(C(C(=O)O)N)OP(=O)(O)O SMILES 'OpenEye OEToolkits' 1.5.0 18695 SEP C([C@@H](C(=O)O)N)OP(=O)(O)O SMILES_CANONICAL 'OpenEye OEToolkits' 1.5.0 18695 SEP InChI=1S/C3H8NO6P/c4-2(3(5)6)1-10-11(7,8)9/h2H,1,4H2,(H,5,6)(H2,7,8,9)/t2-/m0/s1 InChI InChI 1.03 18695 SEP N[C@@H](CO[P](O)(O)=O)C(O)=O SMILES_CANONICAL CACTVS 3.341 18695 SEP N[CH](CO[P](O)(O)=O)C(O)=O SMILES CACTVS 3.341 18695 SEP O=P(O)(O)OCC(C(=O)O)N SMILES ACDLabs 10.04 18695 SEP stop_ loop_ _Chem_comp_identifier.Identifier _Chem_comp_identifier.Type _Chem_comp_identifier.Program _Chem_comp_identifier.Program_version _Chem_comp_identifier.Entry_ID _Chem_comp_identifier.Comp_ID '(2S)-2-amino-3-phosphonooxy-propanoic acid' 'SYSTEMATIC NAME' 'OpenEye OEToolkits' 1.5.0 18695 SEP O-phosphono-L-serine 'SYSTEMATIC NAME' ACDLabs 10.04 18695 SEP stop_ loop_ _Chem_comp_atom.Atom_ID _Chem_comp_atom.BMRB_code _Chem_comp_atom.PDB_atom_ID _Chem_comp_atom.Alt_atom_ID _Chem_comp_atom.Auth_atom_ID _Chem_comp_atom.Type_symbol _Chem_comp_atom.Isotope_number _Chem_comp_atom.Chirality _Chem_comp_atom.Stereo_config _Chem_comp_atom.Charge _Chem_comp_atom.Partial_charge _Chem_comp_atom.Oxidation_number _Chem_comp_atom.Unpaired_electron_number _Chem_comp_atom.Align _Chem_comp_atom.Aromatic_flag _Chem_comp_atom.Leaving_atom_flag _Chem_comp_atom.Substruct_code _Chem_comp_atom.Ionizable _Chem_comp_atom.Drawing_2D_coord_x _Chem_comp_atom.Drawing_2D_coord_y _Chem_comp_atom.Model_Cartn_x _Chem_comp_atom.Model_Cartn_x_esd _Chem_comp_atom.Model_Cartn_y _Chem_comp_atom.Model_Cartn_y_esd _Chem_comp_atom.Model_Cartn_z _Chem_comp_atom.Model_Cartn_z_esd _Chem_comp_atom.Model_Cartn_x_ideal _Chem_comp_atom.Model_Cartn_y_ideal _Chem_comp_atom.Model_Cartn_z_ideal _Chem_comp_atom.PDBX_ordinal _Chem_comp_atom.Details _Chem_comp_atom.Entry_ID _Chem_comp_atom.Comp_ID N N N N . N . . N 0 . . . 1 no no . . . . 12.751 . 44.134 . -4.949 . 1.855 0.421 1.751 1 . 18695 SEP CA CA CA CA . C . . S 0 . . . 1 no no . . . . 12.373 . 44.600 . -6.265 . 0.401 0.620 1.687 2 . 18695 SEP CB CB CB CB . C . . N 0 . . . 1 no no . . . . 11.077 . 45.353 . -6.305 . -0.139 0.015 0.391 3 . 18695 SEP OG OG OG OG . O . . N 0 . . . 1 no no . . . . 10.895 . 45.809 . -7.608 . 0.477 0.655 -0.727 4 . 18695 SEP C C C C . C . . N 0 . . . 1 no no . . . . 13.435 . 45.364 . -6.941 . -0.249 -0.053 2.867 5 . 18695 SEP O O O O . O . . N 0 . . . 1 no no . . . . 14.373 . 45.871 . -6.303 . 0.254 -1.038 3.354 6 . 18695 SEP OXT OXT OXT OXT . O . . N 0 . . . 1 no yes . . . . 13.281 . 45.410 . -8.244 . -1.389 0.439 3.377 7 . 18695 SEP P P P P . P . . N 0 . . . 1 no no . . . . 9.607 . 45.328 . -8.384 . -0.135 -0.027 -2.050 8 . 18695 SEP O1P O1P O1P O1P . O . . N 0 . . . 1 no no . . . . 9.500 . 46.086 . -9.633 . -1.601 0.172 -2.074 9 . 18695 SEP O2P O2P O2P O2P . O . . N 0 . . . 1 no no . . . . 9.829 . 43.907 . -8.669 . 0.520 0.649 -3.356 10 . 18695 SEP O3P O3P O3P O3P . O . . N 0 . . . 1 no no . . . . 8.402 . 45.541 . -7.535 . 0.191 -1.603 -2.041 11 . 18695 SEP H H H H . H . . N 0 . . . 1 no no . . . . 13.632 . 43.621 . -4.921 . 2.237 0.796 0.895 12 . 18695 SEP H2 H2 H2 2HN . H . . N 0 . . . 1 no yes . . . . 12.001 . 43.575 . -4.540 . 2.013 -0.574 1.727 13 . 18695 SEP HA HA HA HA . H . . N 0 . . . 1 no no . . . . 12.213 . 43.656 . -6.837 . 0.179 1.687 1.711 14 . 18695 SEP HB2 HB2 HB2 1HB . H . . N 0 . . . 1 no no . . . . 10.214 . 44.753 . -5.930 . 0.082 -1.051 0.367 15 . 18695 SEP HB3 HB3 HB3 2HB . H . . N 0 . . . 1 no no . . . . 11.026 . 46.170 . -5.548 . -1.218 0.163 0.344 16 . 18695 SEP HXT HXT HXT HXT . H . . N 0 . . . 1 no yes . . . . 13.966 . 45.902 . -8.680 . -1.807 0.006 4.134 17 . 18695 SEP HOP2 HOP2 HOP2 2HOP . H . . N 0 . . . 0 no no . . . . 9.054 . 43.617 . -9.135 . 0.127 0.212 -4.124 18 . 18695 SEP HOP3 HOP3 HOP3 3HOP . H . . N 0 . . . 0 no no . . . . 7.627 . 45.251 . -8.001 . 1.154 -1.689 -2.025 19 . 18695 SEP stop_ loop_ _Chem_comp_bond.ID _Chem_comp_bond.Type _Chem_comp_bond.Value_order _Chem_comp_bond.Atom_ID_1 _Chem_comp_bond.Atom_ID_2 _Chem_comp_bond.Aromatic_flag _Chem_comp_bond.Stereo_config _Chem_comp_bond.Ordinal _Chem_comp_bond.Details _Chem_comp_bond.Entry_ID _Chem_comp_bond.Comp_ID 1 . SING N CA no N 1 . 18695 SEP 2 . SING N H no N 2 . 18695 SEP 3 . SING N H2 no N 3 . 18695 SEP 4 . SING CA CB no N 4 . 18695 SEP 5 . SING CA C no N 5 . 18695 SEP 6 . SING CA HA no N 6 . 18695 SEP 7 . SING CB OG no N 7 . 18695 SEP 8 . SING CB HB2 no N 8 . 18695 SEP 9 . SING CB HB3 no N 9 . 18695 SEP 10 . SING OG P no N 10 . 18695 SEP 11 . DOUB C O no N 11 . 18695 SEP 12 . SING C OXT no N 12 . 18695 SEP 13 . SING OXT HXT no N 13 . 18695 SEP 14 . DOUB P O1P no N 14 . 18695 SEP 15 . SING P O2P no N 15 . 18695 SEP 16 . SING P O3P no N 16 . 18695 SEP 17 . SING O2P HOP2 no N 17 . 18695 SEP 18 . SING O3P HOP3 no N 18 . 18695 SEP stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Sample.Sf_category sample _Sample.Sf_framecode sample_1 _Sample.Entry_ID 18695 _Sample.ID 1 _Sample.Type solution _Sample.Sub_type . _Sample.Details . _Sample.Aggregate_sample_number . _Sample.Solvent_system '90% H2O/10% D2O' _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 KIX_1 '[U-100% 13C; U-100% 15N]' . . 1 $KIX_1 . . 1 . . mM . . . . 18695 1 2 KIX_2 'natural abundance' . . 2 $KIX_2 . . 2 . . mM . . . . 18695 1 3 KIX_3 '[U-100% 13C; U-100% 15N]' . . 3 $KIX_3 . . 2 . . mM . . . . 18695 1 4 'sodium chloride' 'natural abundance' . . . . . . 25 . . mM . . . . 18695 1 5 'potassium phosphate' 'natural abundance' . . . . . . 50 . . mM . . . . 18695 1 6 'sodium azide' 'natural abundance' . . . . . . 1 . . mM . . . . 18695 1 7 H2O 'natural abundance' . . . . . . 90 . . % . . . . 18695 1 8 D2O 'natural abundance' . . . . . . 10 . . % . . . . 18695 1 stop_ save_ ####################### # Sample conditions # ####################### save_sample_conditions_1 _Sample_condition_list.Sf_category sample_conditions _Sample_condition_list.Sf_framecode sample_conditions_1 _Sample_condition_list.Entry_ID 18695 _Sample_condition_list.ID 1 _Sample_condition_list.Details . loop_ _Sample_condition_variable.Type _Sample_condition_variable.Val _Sample_condition_variable.Val_err _Sample_condition_variable.Val_units _Sample_condition_variable.Entry_ID _Sample_condition_variable.Sample_condition_list_ID pH 5.8 . pH 18695 1 pressure 1 . atm 18695 1 temperature 300 . K 18695 1 stop_ save_ ############################ # Computer software used # ############################ save_ARIA _Software.Sf_category software _Software.Sf_framecode ARIA _Software.Entry_ID 18695 _Software.ID 1 _Software.Name ARIA _Software.Version 2.3.1 _Software.Details . loop_ _Vendor.Name _Vendor.Address _Vendor.Electronic_address _Vendor.Entry_ID _Vendor.Software_ID 'Linge, O'Donoghue and Nilges' . . 18695 1 stop_ loop_ _Task.Task _Task.Entry_ID _Task.Software_ID 'structure solution' 18695 1 stop_ save_ save_CNS _Software.Sf_category software _Software.Sf_framecode CNS _Software.Entry_ID 18695 _Software.ID 2 _Software.Name CNS _Software.Version 1.2 _Software.Details . loop_ _Vendor.Name _Vendor.Address _Vendor.Electronic_address _Vendor.Entry_ID _Vendor.Software_ID 'Brunger, Adams, Clore, Gros, Nilges and Read' . . 18695 2 stop_ loop_ _Task.Task _Task.Entry_ID _Task.Software_ID 'structure solution' 18695 2 stop_ save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _NMR_spectrometer.Sf_category NMR_spectrometer _NMR_spectrometer.Sf_framecode spectrometer_1 _NMR_spectrometer.Entry_ID 18695 _NMR_spectrometer.ID 1 _NMR_spectrometer.Details . _NMR_spectrometer.Manufacturer Varian _NMR_spectrometer.Model INOVA _NMR_spectrometer.Serial_number . _NMR_spectrometer.Field_strength 800 save_ save_spectrometer_2 _NMR_spectrometer.Sf_category NMR_spectrometer _NMR_spectrometer.Sf_framecode spectrometer_2 _NMR_spectrometer.Entry_ID 18695 _NMR_spectrometer.ID 2 _NMR_spectrometer.Details . _NMR_spectrometer.Manufacturer Varian _NMR_spectrometer.Model INOVA _NMR_spectrometer.Serial_number . _NMR_spectrometer.Field_strength 500 save_ save_NMR_spectrometer_list _NMR_spectrometer_list.Sf_category NMR_spectrometer_list _NMR_spectrometer_list.Sf_framecode NMR_spectrometer_list _NMR_spectrometer_list.Entry_ID 18695 _NMR_spectrometer_list.ID 1 loop_ _NMR_spectrometer_view.ID _NMR_spectrometer_view.Name _NMR_spectrometer_view.Manufacturer _NMR_spectrometer_view.Model _NMR_spectrometer_view.Serial_number _NMR_spectrometer_view.Field_strength _NMR_spectrometer_view.Details _NMR_spectrometer_view.Citation_ID _NMR_spectrometer_view.Citation_label _NMR_spectrometer_view.Entry_ID _NMR_spectrometer_view.NMR_spectrometer_list_ID 1 spectrometer_1 Varian INOVA . 800 . . . 18695 1 2 spectrometer_2 Varian INOVA . 500 . . . 18695 1 stop_ save_ ############################# # NMR applied experiments # ############################# save_experiment_list _Experiment_list.Sf_category experiment_list _Experiment_list.Sf_framecode experiment_list _Experiment_list.Entry_ID 18695 _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 '2D 1H-15N HSQC' no . . . . . . . . . . 1 $sample_1 isotropic . . 1 $sample_conditions_1 . . . . . . . . . . . . . . . . . . . . . 18695 1 2 '3D CBCA(CO)NH' no . . . . . . . . . . 1 $sample_1 isotropic . . 1 $sample_conditions_1 . . . . . . . . . . . . . . . . . . . . . 18695 1 3 '3D HN(CO)CA' no . . . . . . . . . . 1 $sample_1 isotropic . . 1 $sample_conditions_1 . . . . . . . . . . . . . . . . . . . . . 18695 1 4 '3D HNCO' no . . . . . . . . . . 1 $sample_1 isotropic . . 1 $sample_conditions_1 . . . . . . . . . . . . . . . . . . . . . 18695 1 5 '3D HNCA' no . . . . . . . . . . 1 $sample_1 isotropic . . 1 $sample_conditions_1 . . . . . . . . . . . . . . . . . . . . . 18695 1 6 '3D HNCACB' no . . . . . . . . . . 1 $sample_1 isotropic . . 1 $sample_conditions_1 . . . . . . . . . . . . . . . . . . . . . 18695 1 7 '3D 1H-15N NOESY' no . . . . . . . . . . 1 $sample_1 isotropic . . 1 $sample_conditions_1 . . . . . . . . . . . . . . . . . . . . . 18695 1 8 '3D 1H-13C NOESY' no . . . . . . . . . . 1 $sample_1 isotropic . . 1 $sample_conditions_1 . . . . . . . . . . . . . . . . . . . . . 18695 1 stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference_1 _Chem_shift_reference.Sf_category chem_shift_reference _Chem_shift_reference.Sf_framecode chemical_shift_reference_1 _Chem_shift_reference.Entry_ID 18695 _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 0.00 na indirect 0.251449530 . . . . . . . . . 18695 1 H 1 DSS 'methyl protons' . . . . ppm 0.00 internal direct 1.000000000 . . . . . . . . . 18695 1 N 15 DSS 'methyl protons' . . . . ppm 0.00 na indirect 0.101329118 . . . . . . . . . 18695 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_assigned_chem_shift_list_1 _Assigned_chem_shift_list.Sf_category assigned_chemical_shifts _Assigned_chem_shift_list.Sf_framecode assigned_chem_shift_list_1 _Assigned_chem_shift_list.Entry_ID 18695 _Assigned_chem_shift_list.ID 1 _Assigned_chem_shift_list.Sample_condition_list_ID 1 _Assigned_chem_shift_list.Sample_condition_list_label $sample_conditions_1 _Assigned_chem_shift_list.Chem_shift_reference_ID 1 _Assigned_chem_shift_list.Chem_shift_reference_label $chemical_shift_reference_1 _Assigned_chem_shift_list.Chem_shift_1H_err . _Assigned_chem_shift_list.Chem_shift_13C_err . _Assigned_chem_shift_list.Chem_shift_15N_err . _Assigned_chem_shift_list.Chem_shift_31P_err . _Assigned_chem_shift_list.Chem_shift_2H_err . _Assigned_chem_shift_list.Chem_shift_19F_err . _Assigned_chem_shift_list.Error_derivation_method . _Assigned_chem_shift_list.Details . _Assigned_chem_shift_list.Text_data_format . _Assigned_chem_shift_list.Text_data . loop_ _Chem_shift_experiment.Experiment_ID _Chem_shift_experiment.Experiment_name _Chem_shift_experiment.Sample_ID _Chem_shift_experiment.Sample_label _Chem_shift_experiment.Sample_state _Chem_shift_experiment.Entry_ID _Chem_shift_experiment.Assigned_chem_shift_list_ID 1 '2D 1H-15N HSQC' . . . 18695 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 28 28 PRO HD2 H 1 3.664 0.007 . 2 . . . A 613 PRO HD2 . 18695 1 2 . 1 1 29 29 THR H H 1 7.951 0.006 . 1 . . . A 614 THR H . 18695 1 3 . 1 1 29 29 THR HA H 1 4.332 0.016 . 1 . . . A 614 THR HA . 18695 1 4 . 1 1 29 29 THR HB H 1 4.113 0.007 . 1 . . . A 614 THR HB . 18695 1 5 . 1 1 29 29 THR HG21 H 1 1.010 0.005 . 1 . . . A 614 THR HG21 . 18695 1 6 . 1 1 29 29 THR HG22 H 1 1.010 0.005 . 1 . . . A 614 THR HG22 . 18695 1 7 . 1 1 29 29 THR HG23 H 1 1.010 0.005 . 1 . . . A 614 THR HG23 . 18695 1 8 . 1 1 29 29 THR CA C 13 58.360 0.000 . 1 . . . A 614 THR CA . 18695 1 9 . 1 1 29 29 THR CB C 13 69.597 0.000 . 1 . . . A 614 THR CB . 18695 1 10 . 1 1 29 29 THR CG2 C 13 21.366 0.014 . 1 . . . A 614 THR CG2 . 18695 1 11 . 1 1 29 29 THR N N 15 109.455 0.058 . 1 . . . A 614 THR N . 18695 1 12 . 1 1 30 30 PRO HA H 1 4.002 0.011 . 1 . . . A 615 PRO HA . 18695 1 13 . 1 1 30 30 PRO HB2 H 1 0.896 0.000 . 1 . . . A 615 PRO HB2 . 18695 1 14 . 1 1 30 30 PRO HB3 H 1 0.896 0.000 . 1 . . . A 615 PRO HB3 . 18695 1 15 . 1 1 30 30 PRO HD2 H 1 3.235 0.012 . 1 . . . A 615 PRO HD2 . 18695 1 16 . 1 1 30 30 PRO HD3 H 1 3.235 0.012 . 1 . . . A 615 PRO HD3 . 18695 1 17 . 1 1 30 30 PRO C C 13 176.506 0.000 . 1 . . . A 615 PRO C . 18695 1 18 . 1 1 30 30 PRO CA C 13 62.702 0.030 . 1 . . . A 615 PRO CA . 18695 1 19 . 1 1 30 30 PRO CB C 13 31.231 0.000 . 1 . . . A 615 PRO CB . 18695 1 20 . 1 1 31 31 ASP H H 1 8.197 0.005 . 1 . . . A 616 ASP H . 18695 1 21 . 1 1 31 31 ASP HA H 1 4.718 0.009 . 1 . . . A 616 ASP HA . 18695 1 22 . 1 1 31 31 ASP HB2 H 1 2.967 0.000 . 2 . . . A 616 ASP HB2 . 18695 1 23 . 1 1 31 31 ASP HB3 H 1 2.787 0.008 . 2 . . . A 616 ASP HB3 . 18695 1 24 . 1 1 31 31 ASP CA C 13 52.041 0.000 . 1 . . . A 616 ASP CA . 18695 1 25 . 1 1 31 31 ASP CB C 13 39.743 0.000 . 1 . . . A 616 ASP CB . 18695 1 26 . 1 1 31 31 ASP N N 15 122.774 0.024 . 1 . . . A 616 ASP N . 18695 1 27 . 1 1 32 32 PRO HA H 1 4.067 0.011 . 1 . . . A 617 PRO HA . 18695 1 28 . 1 1 32 32 PRO HB2 H 1 2.293 0.000 . 1 . . . A 617 PRO HB2 . 18695 1 29 . 1 1 32 32 PRO HB3 H 1 2.293 0.000 . 1 . . . A 617 PRO HB3 . 18695 1 30 . 1 1 32 32 PRO C C 13 178.900 0.000 . 1 . . . A 617 PRO C . 18695 1 31 . 1 1 32 32 PRO CA C 13 66.019 0.013 . 1 . . . A 617 PRO CA . 18695 1 32 . 1 1 33 33 ALA H H 1 8.095 0.011 . 1 . . . A 618 ALA H . 18695 1 33 . 1 1 33 33 ALA HA H 1 4.060 0.009 . 1 . . . A 618 ALA HA . 18695 1 34 . 1 1 33 33 ALA HB1 H 1 1.420 0.008 . 1 . . . A 618 ALA HB1 . 18695 1 35 . 1 1 33 33 ALA HB2 H 1 1.420 0.008 . 1 . . . A 618 ALA HB2 . 18695 1 36 . 1 1 33 33 ALA HB3 H 1 1.420 0.008 . 1 . . . A 618 ALA HB3 . 18695 1 37 . 1 1 33 33 ALA C C 13 180.531 0.000 . 1 . . . A 618 ALA C . 18695 1 38 . 1 1 33 33 ALA CA C 13 54.762 0.016 . 1 . . . A 618 ALA CA . 18695 1 39 . 1 1 33 33 ALA CB C 13 18.183 0.038 . 1 . . . A 618 ALA CB . 18695 1 40 . 1 1 33 33 ALA N N 15 118.514 0.073 . 1 . . . A 618 ALA N . 18695 1 41 . 1 1 34 34 ALA H H 1 8.047 0.008 . 1 . . . A 619 ALA H . 18695 1 42 . 1 1 34 34 ALA HA H 1 4.311 0.015 . 1 . . . A 619 ALA HA . 18695 1 43 . 1 1 34 34 ALA HB1 H 1 1.518 0.011 . 1 . . . A 619 ALA HB1 . 18695 1 44 . 1 1 34 34 ALA HB2 H 1 1.518 0.011 . 1 . . . A 619 ALA HB2 . 18695 1 45 . 1 1 34 34 ALA HB3 H 1 1.518 0.011 . 1 . . . A 619 ALA HB3 . 18695 1 46 . 1 1 34 34 ALA C C 13 179.290 0.000 . 1 . . . A 619 ALA C . 18695 1 47 . 1 1 34 34 ALA CA C 13 54.943 0.084 . 1 . . . A 619 ALA CA . 18695 1 48 . 1 1 34 34 ALA CB C 13 18.528 0.097 . 1 . . . A 619 ALA CB . 18695 1 49 . 1 1 34 34 ALA N N 15 122.474 0.096 . 1 . . . A 619 ALA N . 18695 1 50 . 1 1 35 35 LEU H H 1 7.588 0.013 . 1 . . . A 620 LEU H . 18695 1 51 . 1 1 35 35 LEU HA H 1 4.028 0.025 . 1 . . . A 620 LEU HA . 18695 1 52 . 1 1 35 35 LEU HB2 H 1 1.767 0.000 . 1 . . . A 620 LEU HB2 . 18695 1 53 . 1 1 35 35 LEU HB3 H 1 1.767 0.000 . 1 . . . A 620 LEU HB3 . 18695 1 54 . 1 1 35 35 LEU HG H 1 1.510 0.017 . 1 . . . A 620 LEU HG . 18695 1 55 . 1 1 35 35 LEU HD11 H 1 0.823 0.022 . 2 . . . A 620 LEU HD11 . 18695 1 56 . 1 1 35 35 LEU HD12 H 1 0.823 0.022 . 2 . . . A 620 LEU HD12 . 18695 1 57 . 1 1 35 35 LEU HD13 H 1 0.823 0.022 . 2 . . . A 620 LEU HD13 . 18695 1 58 . 1 1 35 35 LEU HD21 H 1 0.829 0.016 . 2 . . . A 620 LEU HD21 . 18695 1 59 . 1 1 35 35 LEU HD22 H 1 0.829 0.016 . 2 . . . A 620 LEU HD22 . 18695 1 60 . 1 1 35 35 LEU HD23 H 1 0.829 0.016 . 2 . . . A 620 LEU HD23 . 18695 1 61 . 1 1 35 35 LEU C C 13 178.264 0.000 . 1 . . . A 620 LEU C . 18695 1 62 . 1 1 35 35 LEU CA C 13 57.111 0.022 . 1 . . . A 620 LEU CA . 18695 1 63 . 1 1 35 35 LEU CB C 13 42.081 0.000 . 1 . . . A 620 LEU CB . 18695 1 64 . 1 1 35 35 LEU CD1 C 13 25.290 0.041 . 2 . . . A 620 LEU CD1 . 18695 1 65 . 1 1 35 35 LEU CD2 C 13 23.221 0.045 . 2 . . . A 620 LEU CD2 . 18695 1 66 . 1 1 35 35 LEU N N 15 113.984 0.034 . 1 . . . A 620 LEU N . 18695 1 67 . 1 1 36 36 LYS H H 1 7.253 0.013 . 1 . . . A 621 LYS H . 18695 1 68 . 1 1 36 36 LYS HA H 1 4.315 0.004 . 1 . . . A 621 LYS HA . 18695 1 69 . 1 1 36 36 LYS HB2 H 1 1.939 0.005 . 2 . . . A 621 LYS HB2 . 18695 1 70 . 1 1 36 36 LYS HB3 H 1 1.761 0.003 . 2 . . . A 621 LYS HB3 . 18695 1 71 . 1 1 36 36 LYS HG2 H 1 1.498 0.005 . 1 . . . A 621 LYS HG2 . 18695 1 72 . 1 1 36 36 LYS HG3 H 1 1.498 0.005 . 1 . . . A 621 LYS HG3 . 18695 1 73 . 1 1 36 36 LYS C C 13 175.864 0.000 . 1 . . . A 621 LYS C . 18695 1 74 . 1 1 36 36 LYS CA C 13 55.624 0.007 . 1 . . . A 621 LYS CA . 18695 1 75 . 1 1 36 36 LYS CB C 13 32.846 0.000 . 1 . . . A 621 LYS CB . 18695 1 76 . 1 1 36 36 LYS N N 15 115.103 0.086 . 1 . . . A 621 LYS N . 18695 1 77 . 1 1 37 37 ASP H H 1 7.433 0.003 . 1 . . . A 622 ASP H . 18695 1 78 . 1 1 37 37 ASP HA H 1 4.477 0.016 . 1 . . . A 622 ASP HA . 18695 1 79 . 1 1 37 37 ASP HB2 H 1 3.043 0.012 . 2 . . . A 622 ASP HB2 . 18695 1 80 . 1 1 37 37 ASP HB3 H 1 2.835 0.006 . 2 . . . A 622 ASP HB3 . 18695 1 81 . 1 1 37 37 ASP C C 13 178.100 0.000 . 1 . . . A 622 ASP C . 18695 1 82 . 1 1 37 37 ASP CA C 13 54.094 0.007 . 1 . . . A 622 ASP CA . 18695 1 83 . 1 1 37 37 ASP CB C 13 44.198 0.030 . 1 . . . A 622 ASP CB . 18695 1 84 . 1 1 37 37 ASP N N 15 123.385 0.017 . 1 . . . A 622 ASP N . 18695 1 85 . 1 1 38 38 ARG H H 1 9.101 0.001 . 1 . . . A 623 ARG H . 18695 1 86 . 1 1 38 38 ARG HA H 1 4.081 0.010 . 1 . . . A 623 ARG HA . 18695 1 87 . 1 1 38 38 ARG HB2 H 1 1.832 0.011 . 1 . . . A 623 ARG HB2 . 18695 1 88 . 1 1 38 38 ARG HB3 H 1 1.832 0.011 . 1 . . . A 623 ARG HB3 . 18695 1 89 . 1 1 38 38 ARG C C 13 178.239 0.000 . 1 . . . A 623 ARG C . 18695 1 90 . 1 1 38 38 ARG CA C 13 58.889 0.064 . 1 . . . A 623 ARG CA . 18695 1 91 . 1 1 38 38 ARG CB C 13 29.365 0.000 . 1 . . . A 623 ARG CB . 18695 1 92 . 1 1 38 38 ARG CD C 13 43.166 0.000 . 1 . . . A 623 ARG CD . 18695 1 93 . 1 1 38 38 ARG N N 15 130.438 0.019 . 1 . . . A 623 ARG N . 18695 1 94 . 1 1 39 39 ARG H H 1 9.575 0.005 . 1 . . . A 624 ARG H . 18695 1 95 . 1 1 39 39 ARG HA H 1 3.807 0.011 . 1 . . . A 624 ARG HA . 18695 1 96 . 1 1 39 39 ARG HG2 H 1 1.503 0.011 . 1 . . . A 624 ARG HG2 . 18695 1 97 . 1 1 39 39 ARG HG3 H 1 1.503 0.011 . 1 . . . A 624 ARG HG3 . 18695 1 98 . 1 1 39 39 ARG HD2 H 1 3.168 0.000 . 2 . . . A 624 ARG HD2 . 18695 1 99 . 1 1 39 39 ARG HD3 H 1 2.820 0.000 . 2 . . . A 624 ARG HD3 . 18695 1 100 . 1 1 39 39 ARG C C 13 178.414 0.000 . 1 . . . A 624 ARG C . 18695 1 101 . 1 1 39 39 ARG CA C 13 58.648 0.055 . 1 . . . A 624 ARG CA . 18695 1 102 . 1 1 39 39 ARG CB C 13 28.348 0.000 . 1 . . . A 624 ARG CB . 18695 1 103 . 1 1 39 39 ARG N N 15 119.003 0.029 . 1 . . . A 624 ARG N . 18695 1 104 . 1 1 40 40 MET H H 1 7.895 0.003 . 1 . . . A 625 MET H . 18695 1 105 . 1 1 40 40 MET HA H 1 4.481 0.010 . 1 . . . A 625 MET HA . 18695 1 106 . 1 1 40 40 MET HB2 H 1 2.357 0.007 . 2 . . . A 625 MET HB2 . 18695 1 107 . 1 1 40 40 MET HB3 H 1 2.362 0.003 . 2 . . . A 625 MET HB3 . 18695 1 108 . 1 1 40 40 MET HE1 H 1 1.890 0.015 . 1 . . . A 625 MET HE1 . 18695 1 109 . 1 1 40 40 MET HE2 H 1 1.890 0.015 . 1 . . . A 625 MET HE2 . 18695 1 110 . 1 1 40 40 MET HE3 H 1 1.890 0.015 . 1 . . . A 625 MET HE3 . 18695 1 111 . 1 1 40 40 MET C C 13 178.803 0.000 . 1 . . . A 625 MET C . 18695 1 112 . 1 1 40 40 MET CA C 13 57.155 0.000 . 1 . . . A 625 MET CA . 18695 1 113 . 1 1 40 40 MET CB C 13 30.803 0.000 . 1 . . . A 625 MET CB . 18695 1 114 . 1 1 40 40 MET CE C 13 17.510 0.023 . 1 . . . A 625 MET CE . 18695 1 115 . 1 1 40 40 MET N N 15 120.211 0.017 . 1 . . . A 625 MET N . 18695 1 116 . 1 1 41 41 GLU H H 1 7.396 0.012 . 1 . . . A 626 GLU H . 18695 1 117 . 1 1 41 41 GLU HA H 1 4.039 0.015 . 1 . . . A 626 GLU HA . 18695 1 118 . 1 1 41 41 GLU HB2 H 1 2.115 0.001 . 1 . . . A 626 GLU HB2 . 18695 1 119 . 1 1 41 41 GLU HB3 H 1 2.115 0.001 . 1 . . . A 626 GLU HB3 . 18695 1 120 . 1 1 41 41 GLU C C 13 179.587 0.000 . 1 . . . A 626 GLU C . 18695 1 121 . 1 1 41 41 GLU CA C 13 59.063 0.011 . 1 . . . A 626 GLU CA . 18695 1 122 . 1 1 41 41 GLU CB C 13 28.369 0.000 . 1 . . . A 626 GLU CB . 18695 1 123 . 1 1 41 41 GLU N N 15 117.810 0.065 . 1 . . . A 626 GLU N . 18695 1 124 . 1 1 42 42 ASN H H 1 7.451 0.008 . 1 . . . A 627 ASN H . 18695 1 125 . 1 1 42 42 ASN HA H 1 4.474 0.011 . 1 . . . A 627 ASN HA . 18695 1 126 . 1 1 42 42 ASN HB2 H 1 2.800 0.003 . 1 . . . A 627 ASN HB2 . 18695 1 127 . 1 1 42 42 ASN HB3 H 1 2.800 0.003 . 1 . . . A 627 ASN HB3 . 18695 1 128 . 1 1 42 42 ASN HD21 H 1 7.768 0.001 . 1 . . . A 627 ASN HD21 . 18695 1 129 . 1 1 42 42 ASN HD22 H 1 6.809 0.001 . 1 . . . A 627 ASN HD22 . 18695 1 130 . 1 1 42 42 ASN C C 13 177.652 0.000 . 1 . . . A 627 ASN C . 18695 1 131 . 1 1 42 42 ASN CA C 13 55.903 0.009 . 1 . . . A 627 ASN CA . 18695 1 132 . 1 1 42 42 ASN CB C 13 37.288 0.000 . 1 . . . A 627 ASN CB . 18695 1 133 . 1 1 42 42 ASN N N 15 118.006 0.022 . 1 . . . A 627 ASN N . 18695 1 134 . 1 1 42 42 ASN ND2 N 15 111.634 0.042 . 1 . . . A 627 ASN ND2 . 18695 1 135 . 1 1 43 43 LEU H H 1 7.906 0.007 . 1 . . . A 628 LEU H . 18695 1 136 . 1 1 43 43 LEU HA H 1 4.208 0.012 . 1 . . . A 628 LEU HA . 18695 1 137 . 1 1 43 43 LEU HB2 H 1 1.679 0.026 . 2 . . . A 628 LEU HB2 . 18695 1 138 . 1 1 43 43 LEU HB3 H 1 2.496 0.000 . 2 . . . A 628 LEU HB3 . 18695 1 139 . 1 1 43 43 LEU HG H 1 1.767 0.012 . 1 . . . A 628 LEU HG . 18695 1 140 . 1 1 43 43 LEU HD11 H 1 1.133 0.013 . 2 . . . A 628 LEU HD11 . 18695 1 141 . 1 1 43 43 LEU HD12 H 1 1.133 0.013 . 2 . . . A 628 LEU HD12 . 18695 1 142 . 1 1 43 43 LEU HD13 H 1 1.133 0.013 . 2 . . . A 628 LEU HD13 . 18695 1 143 . 1 1 43 43 LEU HD21 H 1 1.179 0.015 . 2 . . . A 628 LEU HD21 . 18695 1 144 . 1 1 43 43 LEU HD22 H 1 1.179 0.015 . 2 . . . A 628 LEU HD22 . 18695 1 145 . 1 1 43 43 LEU HD23 H 1 1.179 0.015 . 2 . . . A 628 LEU HD23 . 18695 1 146 . 1 1 43 43 LEU C C 13 177.655 0.000 . 1 . . . A 628 LEU C . 18695 1 147 . 1 1 43 43 LEU CA C 13 59.212 0.008 . 1 . . . A 628 LEU CA . 18695 1 148 . 1 1 43 43 LEU CB C 13 41.350 0.033 . 1 . . . A 628 LEU CB . 18695 1 149 . 1 1 43 43 LEU CG C 13 28.517 0.078 . 1 . . . A 628 LEU CG . 18695 1 150 . 1 1 43 43 LEU CD1 C 13 24.959 0.048 . 2 . . . A 628 LEU CD1 . 18695 1 151 . 1 1 43 43 LEU CD2 C 13 27.024 0.046 . 2 . . . A 628 LEU CD2 . 18695 1 152 . 1 1 43 43 LEU N N 15 124.319 0.112 . 1 . . . A 628 LEU N . 18695 1 153 . 1 1 44 44 VAL H H 1 8.265 0.013 . 1 . . . A 629 VAL H . 18695 1 154 . 1 1 44 44 VAL HA H 1 3.468 0.008 . 1 . . . A 629 VAL HA . 18695 1 155 . 1 1 44 44 VAL HB H 1 2.095 0.013 . 1 . . . A 629 VAL HB . 18695 1 156 . 1 1 44 44 VAL HG11 H 1 0.886 0.006 . 2 . . . A 629 VAL HG11 . 18695 1 157 . 1 1 44 44 VAL HG12 H 1 0.886 0.006 . 2 . . . A 629 VAL HG12 . 18695 1 158 . 1 1 44 44 VAL HG13 H 1 0.886 0.006 . 2 . . . A 629 VAL HG13 . 18695 1 159 . 1 1 44 44 VAL HG21 H 1 1.093 0.010 . 2 . . . A 629 VAL HG21 . 18695 1 160 . 1 1 44 44 VAL HG22 H 1 1.093 0.010 . 2 . . . A 629 VAL HG22 . 18695 1 161 . 1 1 44 44 VAL HG23 H 1 1.093 0.010 . 2 . . . A 629 VAL HG23 . 18695 1 162 . 1 1 44 44 VAL C C 13 177.545 0.000 . 1 . . . A 629 VAL C . 18695 1 163 . 1 1 44 44 VAL CA C 13 67.237 0.043 . 1 . . . A 629 VAL CA . 18695 1 164 . 1 1 44 44 VAL CB C 13 31.652 0.068 . 1 . . . A 629 VAL CB . 18695 1 165 . 1 1 44 44 VAL CG1 C 13 21.257 0.044 . 2 . . . A 629 VAL CG1 . 18695 1 166 . 1 1 44 44 VAL CG2 C 13 22.695 0.027 . 2 . . . A 629 VAL CG2 . 18695 1 167 . 1 1 44 44 VAL N N 15 120.553 0.031 . 1 . . . A 629 VAL N . 18695 1 168 . 1 1 45 45 ALA H H 1 8.151 0.013 . 1 . . . A 630 ALA H . 18695 1 169 . 1 1 45 45 ALA HA H 1 4.004 0.013 . 1 . . . A 630 ALA HA . 18695 1 170 . 1 1 45 45 ALA HB1 H 1 1.520 0.017 . 1 . . . A 630 ALA HB1 . 18695 1 171 . 1 1 45 45 ALA HB2 H 1 1.520 0.017 . 1 . . . A 630 ALA HB2 . 18695 1 172 . 1 1 45 45 ALA HB3 H 1 1.520 0.017 . 1 . . . A 630 ALA HB3 . 18695 1 173 . 1 1 45 45 ALA C C 13 180.803 0.000 . 1 . . . A 630 ALA C . 18695 1 174 . 1 1 45 45 ALA CA C 13 55.422 0.050 . 1 . . . A 630 ALA CA . 18695 1 175 . 1 1 45 45 ALA CB C 13 18.118 0.044 . 1 . . . A 630 ALA CB . 18695 1 176 . 1 1 45 45 ALA N N 15 120.598 0.031 . 1 . . . A 630 ALA N . 18695 1 177 . 1 1 46 46 TYR H H 1 8.131 0.028 . 1 . . . A 631 TYR H . 18695 1 178 . 1 1 46 46 TYR HA H 1 4.218 0.016 . 1 . . . A 631 TYR HA . 18695 1 179 . 1 1 46 46 TYR HB2 H 1 3.227 0.005 . 1 . . . A 631 TYR HB2 . 18695 1 180 . 1 1 46 46 TYR HB3 H 1 3.227 0.005 . 1 . . . A 631 TYR HB3 . 18695 1 181 . 1 1 46 46 TYR HD1 H 1 6.949 0.006 . 3 . . . A 631 TYR HD1 . 18695 1 182 . 1 1 46 46 TYR HD2 H 1 6.949 0.006 . 3 . . . A 631 TYR HD2 . 18695 1 183 . 1 1 46 46 TYR HE1 H 1 6.593 0.006 . 3 . . . A 631 TYR HE1 . 18695 1 184 . 1 1 46 46 TYR HE2 H 1 6.593 0.006 . 3 . . . A 631 TYR HE2 . 18695 1 185 . 1 1 46 46 TYR C C 13 176.361 0.000 . 1 . . . A 631 TYR C . 18695 1 186 . 1 1 46 46 TYR CA C 13 61.585 0.009 . 1 . . . A 631 TYR CA . 18695 1 187 . 1 1 46 46 TYR CB C 13 38.274 0.000 . 1 . . . A 631 TYR CB . 18695 1 188 . 1 1 46 46 TYR CD1 C 13 132.406 0.048 . 3 . . . A 631 TYR CD1 . 18695 1 189 . 1 1 46 46 TYR CD2 C 13 132.406 0.048 . 3 . . . A 631 TYR CD2 . 18695 1 190 . 1 1 46 46 TYR CE1 C 13 118.411 0.034 . 3 . . . A 631 TYR CE1 . 18695 1 191 . 1 1 46 46 TYR CE2 C 13 118.411 0.034 . 3 . . . A 631 TYR CE2 . 18695 1 192 . 1 1 46 46 TYR N N 15 121.213 0.146 . 1 . . . A 631 TYR N . 18695 1 193 . 1 1 47 47 ALA H H 1 8.367 0.019 . 1 . . . A 632 ALA H . 18695 1 194 . 1 1 47 47 ALA HA H 1 3.668 0.020 . 1 . . . A 632 ALA HA . 18695 1 195 . 1 1 47 47 ALA HB1 H 1 1.521 0.014 . 1 . . . A 632 ALA HB1 . 18695 1 196 . 1 1 47 47 ALA HB2 H 1 1.521 0.014 . 1 . . . A 632 ALA HB2 . 18695 1 197 . 1 1 47 47 ALA HB3 H 1 1.521 0.014 . 1 . . . A 632 ALA HB3 . 18695 1 198 . 1 1 47 47 ALA C C 13 178.960 0.000 . 1 . . . A 632 ALA C . 18695 1 199 . 1 1 47 47 ALA CA C 13 55.307 0.065 . 1 . . . A 632 ALA CA . 18695 1 200 . 1 1 47 47 ALA CB C 13 19.885 0.043 . 1 . . . A 632 ALA CB . 18695 1 201 . 1 1 47 47 ALA N N 15 122.461 0.066 . 1 . . . A 632 ALA N . 18695 1 202 . 1 1 48 48 LYS H H 1 8.522 0.016 . 1 . . . A 633 LYS H . 18695 1 203 . 1 1 48 48 LYS HA H 1 3.977 0.008 . 1 . . . A 633 LYS HA . 18695 1 204 . 1 1 48 48 LYS HB2 H 1 1.853 0.003 . 1 . . . A 633 LYS HB2 . 18695 1 205 . 1 1 48 48 LYS HB3 H 1 1.853 0.003 . 1 . . . A 633 LYS HB3 . 18695 1 206 . 1 1 48 48 LYS HD2 H 1 1.598 0.021 . 1 . . . A 633 LYS HD2 . 18695 1 207 . 1 1 48 48 LYS HD3 H 1 1.598 0.021 . 1 . . . A 633 LYS HD3 . 18695 1 208 . 1 1 48 48 LYS C C 13 179.928 0.000 . 1 . . . A 633 LYS C . 18695 1 209 . 1 1 48 48 LYS CA C 13 59.727 0.005 . 1 . . . A 633 LYS CA . 18695 1 210 . 1 1 48 48 LYS CB C 13 32.865 0.000 . 1 . . . A 633 LYS CB . 18695 1 211 . 1 1 48 48 LYS N N 15 116.170 0.064 . 1 . . . A 633 LYS N . 18695 1 212 . 1 1 49 49 LYS H H 1 7.914 0.005 . 1 . . . A 634 LYS H . 18695 1 213 . 1 1 49 49 LYS HA H 1 4.014 0.023 . 1 . . . A 634 LYS HA . 18695 1 214 . 1 1 49 49 LYS HB2 H 1 2.049 0.008 . 1 . . . A 634 LYS HB2 . 18695 1 215 . 1 1 49 49 LYS HB3 H 1 2.049 0.008 . 1 . . . A 634 LYS HB3 . 18695 1 216 . 1 1 49 49 LYS C C 13 178.514 0.000 . 1 . . . A 634 LYS C . 18695 1 217 . 1 1 49 49 LYS CA C 13 59.230 0.093 . 1 . . . A 634 LYS CA . 18695 1 218 . 1 1 49 49 LYS CB C 13 31.916 0.000 . 1 . . . A 634 LYS CB . 18695 1 219 . 1 1 49 49 LYS N N 15 123.724 0.075 . 1 . . . A 634 LYS N . 18695 1 220 . 1 1 50 50 VAL H H 1 8.153 0.020 . 1 . . . A 635 VAL H . 18695 1 221 . 1 1 50 50 VAL HA H 1 3.643 0.012 . 1 . . . A 635 VAL HA . 18695 1 222 . 1 1 50 50 VAL HB H 1 1.837 0.007 . 1 . . . A 635 VAL HB . 18695 1 223 . 1 1 50 50 VAL HG11 H 1 0.741 0.011 . 2 . . . A 635 VAL HG11 . 18695 1 224 . 1 1 50 50 VAL HG12 H 1 0.741 0.011 . 2 . . . A 635 VAL HG12 . 18695 1 225 . 1 1 50 50 VAL HG13 H 1 0.741 0.011 . 2 . . . A 635 VAL HG13 . 18695 1 226 . 1 1 50 50 VAL HG21 H 1 0.504 0.007 . 2 . . . A 635 VAL HG21 . 18695 1 227 . 1 1 50 50 VAL HG22 H 1 0.504 0.007 . 2 . . . A 635 VAL HG22 . 18695 1 228 . 1 1 50 50 VAL HG23 H 1 0.504 0.007 . 2 . . . A 635 VAL HG23 . 18695 1 229 . 1 1 50 50 VAL C C 13 178.305 0.000 . 1 . . . A 635 VAL C . 18695 1 230 . 1 1 50 50 VAL CA C 13 66.133 0.045 . 1 . . . A 635 VAL CA . 18695 1 231 . 1 1 50 50 VAL CB C 13 31.641 0.052 . 1 . . . A 635 VAL CB . 18695 1 232 . 1 1 50 50 VAL CG1 C 13 21.957 0.024 . 2 . . . A 635 VAL CG1 . 18695 1 233 . 1 1 50 50 VAL CG2 C 13 22.122 0.056 . 2 . . . A 635 VAL CG2 . 18695 1 234 . 1 1 50 50 VAL N N 15 119.138 0.025 . 1 . . . A 635 VAL N . 18695 1 235 . 1 1 51 51 GLU H H 1 8.347 0.015 . 1 . . . A 636 GLU H . 18695 1 236 . 1 1 51 51 GLU HA H 1 3.763 0.010 . 1 . . . A 636 GLU HA . 18695 1 237 . 1 1 51 51 GLU HB2 H 1 1.554 0.022 . 2 . . . A 636 GLU HB2 . 18695 1 238 . 1 1 51 51 GLU HB3 H 1 1.564 0.022 . 2 . . . A 636 GLU HB3 . 18695 1 239 . 1 1 51 51 GLU HG2 H 1 2.292 0.006 . 1 . . . A 636 GLU HG2 . 18695 1 240 . 1 1 51 51 GLU HG3 H 1 2.292 0.006 . 1 . . . A 636 GLU HG3 . 18695 1 241 . 1 1 51 51 GLU C C 13 178.645 0.000 . 1 . . . A 636 GLU C . 18695 1 242 . 1 1 51 51 GLU CA C 13 61.868 0.039 . 1 . . . A 636 GLU CA . 18695 1 243 . 1 1 51 51 GLU CB C 13 28.816 0.018 . 1 . . . A 636 GLU CB . 18695 1 244 . 1 1 51 51 GLU N N 15 119.794 0.011 . 1 . . . A 636 GLU N . 18695 1 245 . 1 1 52 52 GLY H H 1 8.089 0.023 . 1 . . . A 637 GLY H . 18695 1 246 . 1 1 52 52 GLY HA2 H 1 3.860 0.013 . 2 . . . A 637 GLY HA2 . 18695 1 247 . 1 1 52 52 GLY HA3 H 1 3.595 0.025 . 2 . . . A 637 GLY HA3 . 18695 1 248 . 1 1 52 52 GLY C C 13 176.641 0.000 . 1 . . . A 637 GLY C . 18695 1 249 . 1 1 52 52 GLY CA C 13 47.502 0.002 . 1 . . . A 637 GLY CA . 18695 1 250 . 1 1 52 52 GLY N N 15 106.417 0.034 . 1 . . . A 637 GLY N . 18695 1 251 . 1 1 53 53 ASP H H 1 8.411 0.012 . 1 . . . A 638 ASP H . 18695 1 252 . 1 1 53 53 ASP HA H 1 4.514 0.000 . 1 . . . A 638 ASP HA . 18695 1 253 . 1 1 53 53 ASP HB2 H 1 2.950 0.017 . 2 . . . A 638 ASP HB2 . 18695 1 254 . 1 1 53 53 ASP HB3 H 1 2.693 0.004 . 2 . . . A 638 ASP HB3 . 18695 1 255 . 1 1 53 53 ASP C C 13 180.170 0.000 . 1 . . . A 638 ASP C . 18695 1 256 . 1 1 53 53 ASP CA C 13 57.006 0.011 . 1 . . . A 638 ASP CA . 18695 1 257 . 1 1 53 53 ASP CB C 13 39.862 0.000 . 1 . . . A 638 ASP CB . 18695 1 258 . 1 1 53 53 ASP N N 15 122.792 0.040 . 1 . . . A 638 ASP N . 18695 1 259 . 1 1 54 54 MET H H 1 8.326 0.005 . 1 . . . A 639 MET H . 18695 1 260 . 1 1 54 54 MET HA H 1 4.460 0.010 . 1 . . . A 639 MET HA . 18695 1 261 . 1 1 54 54 MET HG2 H 1 2.425 0.017 . 2 . . . A 639 MET HG2 . 18695 1 262 . 1 1 54 54 MET HG3 H 1 2.423 0.015 . 2 . . . A 639 MET HG3 . 18695 1 263 . 1 1 54 54 MET HE1 H 1 2.025 0.017 . 1 . . . A 639 MET HE1 . 18695 1 264 . 1 1 54 54 MET HE2 H 1 2.025 0.017 . 1 . . . A 639 MET HE2 . 18695 1 265 . 1 1 54 54 MET HE3 H 1 2.025 0.017 . 1 . . . A 639 MET HE3 . 18695 1 266 . 1 1 54 54 MET C C 13 177.917 0.000 . 1 . . . A 639 MET C . 18695 1 267 . 1 1 54 54 MET CA C 13 58.107 0.015 . 1 . . . A 639 MET CA . 18695 1 268 . 1 1 54 54 MET CE C 13 19.774 0.045 . 1 . . . A 639 MET CE . 18695 1 269 . 1 1 54 54 MET N N 15 120.533 0.056 . 1 . . . A 639 MET N . 18695 1 270 . 1 1 55 55 TYR H H 1 9.393 0.005 . 1 . . . A 640 TYR H . 18695 1 271 . 1 1 55 55 TYR HA H 1 4.276 0.018 . 1 . . . A 640 TYR HA . 18695 1 272 . 1 1 55 55 TYR HB2 H 1 3.573 0.001 . 2 . . . A 640 TYR HB2 . 18695 1 273 . 1 1 55 55 TYR HB3 H 1 3.052 0.003 . 2 . . . A 640 TYR HB3 . 18695 1 274 . 1 1 55 55 TYR HD1 H 1 6.535 0.017 . 3 . . . A 640 TYR HD1 . 18695 1 275 . 1 1 55 55 TYR HD2 H 1 6.535 0.017 . 3 . . . A 640 TYR HD2 . 18695 1 276 . 1 1 55 55 TYR HE1 H 1 5.936 0.005 . 3 . . . A 640 TYR HE1 . 18695 1 277 . 1 1 55 55 TYR HE2 H 1 5.936 0.005 . 3 . . . A 640 TYR HE2 . 18695 1 278 . 1 1 55 55 TYR C C 13 178.394 0.000 . 1 . . . A 640 TYR C . 18695 1 279 . 1 1 55 55 TYR CA C 13 62.253 0.017 . 1 . . . A 640 TYR CA . 18695 1 280 . 1 1 55 55 TYR CB C 13 38.802 0.000 . 1 . . . A 640 TYR CB . 18695 1 281 . 1 1 55 55 TYR CD1 C 13 132.613 0.050 . 3 . . . A 640 TYR CD1 . 18695 1 282 . 1 1 55 55 TYR CD2 C 13 132.613 0.050 . 3 . . . A 640 TYR CD2 . 18695 1 283 . 1 1 55 55 TYR CE1 C 13 117.079 0.032 . 3 . . . A 640 TYR CE1 . 18695 1 284 . 1 1 55 55 TYR CE2 C 13 117.079 0.032 . 3 . . . A 640 TYR CE2 . 18695 1 285 . 1 1 55 55 TYR N N 15 121.734 0.024 . 1 . . . A 640 TYR N . 18695 1 286 . 1 1 56 56 GLU H H 1 8.012 0.008 . 1 . . . A 641 GLU H . 18695 1 287 . 1 1 56 56 GLU HA H 1 4.327 0.018 . 1 . . . A 641 GLU HA . 18695 1 288 . 1 1 56 56 GLU HB2 H 1 2.163 0.005 . 1 . . . A 641 GLU HB2 . 18695 1 289 . 1 1 56 56 GLU HB3 H 1 2.163 0.005 . 1 . . . A 641 GLU HB3 . 18695 1 290 . 1 1 56 56 GLU HG2 H 1 2.577 0.014 . 2 . . . A 641 GLU HG2 . 18695 1 291 . 1 1 56 56 GLU HG3 H 1 2.508 0.006 . 2 . . . A 641 GLU HG3 . 18695 1 292 . 1 1 56 56 GLU C C 13 177.892 0.000 . 1 . . . A 641 GLU C . 18695 1 293 . 1 1 56 56 GLU CA C 13 57.559 0.009 . 1 . . . A 641 GLU CA . 18695 1 294 . 1 1 56 56 GLU CB C 13 29.575 0.000 . 1 . . . A 641 GLU CB . 18695 1 295 . 1 1 56 56 GLU CG C 13 35.164 0.105 . 1 . . . A 641 GLU CG . 18695 1 296 . 1 1 56 56 GLU N N 15 114.967 0.025 . 1 . . . A 641 GLU N . 18695 1 297 . 1 1 57 57 SER H H 1 7.900 0.005 . 1 . . . A 642 SER H . 18695 1 298 . 1 1 57 57 SER HA H 1 4.420 0.007 . 1 . . . A 642 SER HA . 18695 1 299 . 1 1 57 57 SER HB2 H 1 3.910 0.014 . 2 . . . A 642 SER HB2 . 18695 1 300 . 1 1 57 57 SER HB3 H 1 3.907 0.014 . 2 . . . A 642 SER HB3 . 18695 1 301 . 1 1 57 57 SER C C 13 175.199 0.000 . 1 . . . A 642 SER C . 18695 1 302 . 1 1 57 57 SER CA C 13 60.205 0.011 . 1 . . . A 642 SER CA . 18695 1 303 . 1 1 57 57 SER CB C 13 64.606 0.065 . 1 . . . A 642 SER CB . 18695 1 304 . 1 1 57 57 SER N N 15 112.599 0.022 . 1 . . . A 642 SER N . 18695 1 305 . 1 1 58 58 ALA H H 1 8.108 0.008 . 1 . . . A 643 ALA H . 18695 1 306 . 1 1 58 58 ALA HA H 1 4.176 0.016 . 1 . . . A 643 ALA HA . 18695 1 307 . 1 1 58 58 ALA HB1 H 1 1.566 0.008 . 1 . . . A 643 ALA HB1 . 18695 1 308 . 1 1 58 58 ALA HB2 H 1 1.566 0.008 . 1 . . . A 643 ALA HB2 . 18695 1 309 . 1 1 58 58 ALA HB3 H 1 1.566 0.008 . 1 . . . A 643 ALA HB3 . 18695 1 310 . 1 1 58 58 ALA C C 13 177.957 0.000 . 1 . . . A 643 ALA C . 18695 1 311 . 1 1 58 58 ALA CA C 13 52.674 0.014 . 1 . . . A 643 ALA CA . 18695 1 312 . 1 1 58 58 ALA CB C 13 19.857 0.028 . 1 . . . A 643 ALA CB . 18695 1 313 . 1 1 58 58 ALA N N 15 123.630 0.063 . 1 . . . A 643 ALA N . 18695 1 314 . 1 1 59 59 ASN H H 1 9.145 0.008 . 1 . . . A 644 ASN H . 18695 1 315 . 1 1 59 59 ASN HA H 1 5.072 0.013 . 1 . . . A 644 ASN HA . 18695 1 316 . 1 1 59 59 ASN HB2 H 1 2.911 0.018 . 2 . . . A 644 ASN HB2 . 18695 1 317 . 1 1 59 59 ASN HB3 H 1 2.725 0.007 . 2 . . . A 644 ASN HB3 . 18695 1 318 . 1 1 59 59 ASN HD21 H 1 7.981 0.015 . 1 . . . A 644 ASN HD21 . 18695 1 319 . 1 1 59 59 ASN HD22 H 1 6.995 0.002 . 1 . . . A 644 ASN HD22 . 18695 1 320 . 1 1 59 59 ASN C C 13 173.946 0.000 . 1 . . . A 644 ASN C . 18695 1 321 . 1 1 59 59 ASN CA C 13 53.486 0.002 . 1 . . . A 644 ASN CA . 18695 1 322 . 1 1 59 59 ASN CB C 13 40.107 0.087 . 1 . . . A 644 ASN CB . 18695 1 323 . 1 1 59 59 ASN N N 15 117.266 0.025 . 1 . . . A 644 ASN N . 18695 1 324 . 1 1 59 59 ASN ND2 N 15 115.679 0.070 . 1 . . . A 644 ASN ND2 . 18695 1 325 . 1 1 60 60 SER H H 1 6.869 0.008 . 1 . . . A 645 SER H . 18695 1 326 . 1 1 60 60 SER HA H 1 3.624 0.010 . 1 . . . A 645 SER HA . 18695 1 327 . 1 1 60 60 SER HB2 H 1 3.877 0.018 . 1 . . . A 645 SER HB2 . 18695 1 328 . 1 1 60 60 SER HB3 H 1 3.877 0.018 . 1 . . . A 645 SER HB3 . 18695 1 329 . 1 1 60 60 SER C C 13 171.968 0.000 . 1 . . . A 645 SER C . 18695 1 330 . 1 1 60 60 SER CA C 13 56.533 0.032 . 1 . . . A 645 SER CA . 18695 1 331 . 1 1 60 60 SER CB C 13 64.969 0.000 . 1 . . . A 645 SER CB . 18695 1 332 . 1 1 60 60 SER N N 15 111.279 0.016 . 1 . . . A 645 SER N . 18695 1 333 . 1 1 61 61 ARG H H 1 8.715 0.005 . 1 . . . A 646 ARG H . 18695 1 334 . 1 1 61 61 ARG HA H 1 3.165 0.011 . 1 . . . A 646 ARG HA . 18695 1 335 . 1 1 61 61 ARG HB2 H 1 1.877 0.005 . 2 . . . A 646 ARG HB2 . 18695 1 336 . 1 1 61 61 ARG HB3 H 1 1.876 0.004 . 2 . . . A 646 ARG HB3 . 18695 1 337 . 1 1 61 61 ARG HD2 H 1 3.356 0.001 . 2 . . . A 646 ARG HD2 . 18695 1 338 . 1 1 61 61 ARG HD3 H 1 3.266 0.013 . 2 . . . A 646 ARG HD3 . 18695 1 339 . 1 1 61 61 ARG C C 13 177.235 0.000 . 1 . . . A 646 ARG C . 18695 1 340 . 1 1 61 61 ARG CA C 13 59.049 0.046 . 1 . . . A 646 ARG CA . 18695 1 341 . 1 1 61 61 ARG CB C 13 30.334 0.041 . 1 . . . A 646 ARG CB . 18695 1 342 . 1 1 61 61 ARG N N 15 122.346 0.026 . 1 . . . A 646 ARG N . 18695 1 343 . 1 1 62 62 ASP H H 1 8.238 0.005 . 1 . . . A 647 ASP H . 18695 1 344 . 1 1 62 62 ASP HA H 1 4.447 0.011 . 1 . . . A 647 ASP HA . 18695 1 345 . 1 1 62 62 ASP HB2 H 1 2.557 0.002 . 2 . . . A 647 ASP HB2 . 18695 1 346 . 1 1 62 62 ASP HB3 H 1 2.407 0.014 . 2 . . . A 647 ASP HB3 . 18695 1 347 . 1 1 62 62 ASP C C 13 179.432 0.000 . 1 . . . A 647 ASP C . 18695 1 348 . 1 1 62 62 ASP CA C 13 57.504 0.000 . 1 . . . A 647 ASP CA . 18695 1 349 . 1 1 62 62 ASP CB C 13 41.032 0.049 . 1 . . . A 647 ASP CB . 18695 1 350 . 1 1 62 62 ASP N N 15 117.089 0.042 . 1 . . . A 647 ASP N . 18695 1 351 . 1 1 63 63 GLU H H 1 7.982 0.016 . 1 . . . A 648 GLU H . 18695 1 352 . 1 1 63 63 GLU HA H 1 3.923 0.019 . 1 . . . A 648 GLU HA . 18695 1 353 . 1 1 63 63 GLU HB2 H 1 1.877 0.007 . 1 . . . A 648 GLU HB2 . 18695 1 354 . 1 1 63 63 GLU HB3 H 1 1.877 0.007 . 1 . . . A 648 GLU HB3 . 18695 1 355 . 1 1 63 63 GLU HG2 H 1 2.468 0.000 . 1 . . . A 648 GLU HG2 . 18695 1 356 . 1 1 63 63 GLU HG3 H 1 2.468 0.000 . 1 . . . A 648 GLU HG3 . 18695 1 357 . 1 1 63 63 GLU C C 13 176.934 0.000 . 1 . . . A 648 GLU C . 18695 1 358 . 1 1 63 63 GLU CA C 13 59.736 0.019 . 1 . . . A 648 GLU CA . 18695 1 359 . 1 1 63 63 GLU CB C 13 29.711 0.000 . 1 . . . A 648 GLU CB . 18695 1 360 . 1 1 63 63 GLU N N 15 122.214 0.045 . 1 . . . A 648 GLU N . 18695 1 361 . 1 1 64 64 TYR H H 1 7.421 0.006 . 1 . . . A 649 TYR H . 18695 1 362 . 1 1 64 64 TYR HA H 1 3.963 0.019 . 1 . . . A 649 TYR HA . 18695 1 363 . 1 1 64 64 TYR HB2 H 1 2.970 0.006 . 2 . . . A 649 TYR HB2 . 18695 1 364 . 1 1 64 64 TYR HB3 H 1 2.568 0.017 . 2 . . . A 649 TYR HB3 . 18695 1 365 . 1 1 64 64 TYR HD1 H 1 6.744 0.010 . 3 . . . A 649 TYR HD1 . 18695 1 366 . 1 1 64 64 TYR HD2 H 1 6.744 0.010 . 3 . . . A 649 TYR HD2 . 18695 1 367 . 1 1 64 64 TYR HE1 H 1 6.752 0.019 . 3 . . . A 649 TYR HE1 . 18695 1 368 . 1 1 64 64 TYR HE2 H 1 6.752 0.019 . 3 . . . A 649 TYR HE2 . 18695 1 369 . 1 1 64 64 TYR C C 13 176.398 0.000 . 1 . . . A 649 TYR C . 18695 1 370 . 1 1 64 64 TYR CA C 13 60.797 0.007 . 1 . . . A 649 TYR CA . 18695 1 371 . 1 1 64 64 TYR CB C 13 38.706 0.000 . 1 . . . A 649 TYR CB . 18695 1 372 . 1 1 64 64 TYR CD1 C 13 133.172 0.041 . 3 . . . A 649 TYR CD1 . 18695 1 373 . 1 1 64 64 TYR CD2 C 13 133.172 0.041 . 3 . . . A 649 TYR CD2 . 18695 1 374 . 1 1 64 64 TYR CE1 C 13 118.264 0.033 . 3 . . . A 649 TYR CE1 . 18695 1 375 . 1 1 64 64 TYR CE2 C 13 118.264 0.033 . 3 . . . A 649 TYR CE2 . 18695 1 376 . 1 1 64 64 TYR N N 15 122.127 0.091 . 1 . . . A 649 TYR N . 18695 1 377 . 1 1 65 65 TYR H H 1 8.002 0.006 . 1 . . . A 650 TYR H . 18695 1 378 . 1 1 65 65 TYR HA H 1 3.878 0.019 . 1 . . . A 650 TYR HA . 18695 1 379 . 1 1 65 65 TYR HB2 H 1 3.037 0.017 . 2 . . . A 650 TYR HB2 . 18695 1 380 . 1 1 65 65 TYR HB3 H 1 2.746 0.016 . 2 . . . A 650 TYR HB3 . 18695 1 381 . 1 1 65 65 TYR HD1 H 1 7.096 0.018 . 3 . . . A 650 TYR HD1 . 18695 1 382 . 1 1 65 65 TYR HD2 H 1 7.096 0.018 . 3 . . . A 650 TYR HD2 . 18695 1 383 . 1 1 65 65 TYR HE1 H 1 6.786 0.027 . 3 . . . A 650 TYR HE1 . 18695 1 384 . 1 1 65 65 TYR HE2 H 1 6.786 0.027 . 3 . . . A 650 TYR HE2 . 18695 1 385 . 1 1 65 65 TYR C C 13 178.543 0.000 . 1 . . . A 650 TYR C . 18695 1 386 . 1 1 65 65 TYR CA C 13 61.904 0.008 . 1 . . . A 650 TYR CA . 18695 1 387 . 1 1 65 65 TYR CB C 13 38.116 0.000 . 1 . . . A 650 TYR CB . 18695 1 388 . 1 1 65 65 TYR CD1 C 13 132.054 0.053 . 3 . . . A 650 TYR CD1 . 18695 1 389 . 1 1 65 65 TYR CD2 C 13 132.054 0.053 . 3 . . . A 650 TYR CD2 . 18695 1 390 . 1 1 65 65 TYR CE1 C 13 118.244 0.041 . 3 . . . A 650 TYR CE1 . 18695 1 391 . 1 1 65 65 TYR CE2 C 13 118.244 0.041 . 3 . . . A 650 TYR CE2 . 18695 1 392 . 1 1 65 65 TYR N N 15 115.815 0.074 . 1 . . . A 650 TYR N . 18695 1 393 . 1 1 66 66 HIS H H 1 8.234 0.008 . 1 . . . A 651 HIS H . 18695 1 394 . 1 1 66 66 HIS HA H 1 4.233 0.011 . 1 . . . A 651 HIS HA . 18695 1 395 . 1 1 66 66 HIS HB2 H 1 3.297 0.019 . 1 . . . A 651 HIS HB2 . 18695 1 396 . 1 1 66 66 HIS HB3 H 1 3.297 0.019 . 1 . . . A 651 HIS HB3 . 18695 1 397 . 1 1 66 66 HIS CA C 13 59.833 0.017 . 1 . . . A 651 HIS CA . 18695 1 398 . 1 1 66 66 HIS CB C 13 28.239 0.000 . 1 . . . A 651 HIS CB . 18695 1 399 . 1 1 66 66 HIS N N 15 115.975 0.091 . 1 . . . A 651 HIS N . 18695 1 400 . 1 1 67 67 LEU H H 1 9.206 0.006 . 1 . . . A 652 LEU H . 18695 1 401 . 1 1 67 67 LEU HA H 1 4.096 0.023 . 1 . . . A 652 LEU HA . 18695 1 402 . 1 1 67 67 LEU HB2 H 1 1.835 0.068 . 1 . . . A 652 LEU HB2 . 18695 1 403 . 1 1 67 67 LEU HB3 H 1 1.835 0.068 . 1 . . . A 652 LEU HB3 . 18695 1 404 . 1 1 67 67 LEU HD11 H 1 0.954 0.008 . 2 . . . A 652 LEU HD11 . 18695 1 405 . 1 1 67 67 LEU HD12 H 1 0.954 0.008 . 2 . . . A 652 LEU HD12 . 18695 1 406 . 1 1 67 67 LEU HD13 H 1 0.954 0.008 . 2 . . . A 652 LEU HD13 . 18695 1 407 . 1 1 67 67 LEU HD21 H 1 0.907 0.023 . 2 . . . A 652 LEU HD21 . 18695 1 408 . 1 1 67 67 LEU HD22 H 1 0.907 0.023 . 2 . . . A 652 LEU HD22 . 18695 1 409 . 1 1 67 67 LEU HD23 H 1 0.907 0.023 . 2 . . . A 652 LEU HD23 . 18695 1 410 . 1 1 67 67 LEU C C 13 180.801 0.000 . 1 . . . A 652 LEU C . 18695 1 411 . 1 1 67 67 LEU CA C 13 58.096 0.003 . 1 . . . A 652 LEU CA . 18695 1 412 . 1 1 67 67 LEU CB C 13 42.224 0.069 . 1 . . . A 652 LEU CB . 18695 1 413 . 1 1 67 67 LEU CD1 C 13 25.904 0.069 . 2 . . . A 652 LEU CD1 . 18695 1 414 . 1 1 67 67 LEU CD2 C 13 22.153 0.042 . 2 . . . A 652 LEU CD2 . 18695 1 415 . 1 1 67 67 LEU N N 15 122.802 0.030 . 1 . . . A 652 LEU N . 18695 1 416 . 1 1 68 68 LEU H H 1 7.984 0.018 . 1 . . . A 653 LEU H . 18695 1 417 . 1 1 68 68 LEU HA H 1 3.791 0.018 . 1 . . . A 653 LEU HA . 18695 1 418 . 1 1 68 68 LEU HB2 H 1 1.747 0.013 . 1 . . . A 653 LEU HB2 . 18695 1 419 . 1 1 68 68 LEU HB3 H 1 1.747 0.013 . 1 . . . A 653 LEU HB3 . 18695 1 420 . 1 1 68 68 LEU HG H 1 1.481 0.013 . 1 . . . A 653 LEU HG . 18695 1 421 . 1 1 68 68 LEU HD11 H 1 0.275 0.009 . 2 . . . A 653 LEU HD11 . 18695 1 422 . 1 1 68 68 LEU HD12 H 1 0.275 0.009 . 2 . . . A 653 LEU HD12 . 18695 1 423 . 1 1 68 68 LEU HD13 H 1 0.275 0.009 . 2 . . . A 653 LEU HD13 . 18695 1 424 . 1 1 68 68 LEU HD21 H 1 0.666 0.009 . 2 . . . A 653 LEU HD21 . 18695 1 425 . 1 1 68 68 LEU HD22 H 1 0.666 0.009 . 2 . . . A 653 LEU HD22 . 18695 1 426 . 1 1 68 68 LEU HD23 H 1 0.666 0.009 . 2 . . . A 653 LEU HD23 . 18695 1 427 . 1 1 68 68 LEU C C 13 178.280 0.000 . 1 . . . A 653 LEU C . 18695 1 428 . 1 1 68 68 LEU CA C 13 58.269 0.021 . 1 . . . A 653 LEU CA . 18695 1 429 . 1 1 68 68 LEU CB C 13 42.750 0.082 . 1 . . . A 653 LEU CB . 18695 1 430 . 1 1 68 68 LEU CG C 13 26.629 0.048 . 1 . . . A 653 LEU CG . 18695 1 431 . 1 1 68 68 LEU CD1 C 13 25.940 0.034 . 2 . . . A 653 LEU CD1 . 18695 1 432 . 1 1 68 68 LEU CD2 C 13 24.206 0.029 . 2 . . . A 653 LEU CD2 . 18695 1 433 . 1 1 68 68 LEU N N 15 120.850 0.077 . 1 . . . A 653 LEU N . 18695 1 434 . 1 1 69 69 ALA H H 1 8.361 0.016 . 1 . . . A 654 ALA H . 18695 1 435 . 1 1 69 69 ALA HA H 1 3.808 0.017 . 1 . . . A 654 ALA HA . 18695 1 436 . 1 1 69 69 ALA HB1 H 1 1.079 0.020 . 1 . . . A 654 ALA HB1 . 18695 1 437 . 1 1 69 69 ALA HB2 H 1 1.079 0.020 . 1 . . . A 654 ALA HB2 . 18695 1 438 . 1 1 69 69 ALA HB3 H 1 1.079 0.020 . 1 . . . A 654 ALA HB3 . 18695 1 439 . 1 1 69 69 ALA C C 13 178.807 0.000 . 1 . . . A 654 ALA C . 18695 1 440 . 1 1 69 69 ALA CA C 13 55.018 0.055 . 1 . . . A 654 ALA CA . 18695 1 441 . 1 1 69 69 ALA CB C 13 17.852 0.040 . 1 . . . A 654 ALA CB . 18695 1 442 . 1 1 69 69 ALA N N 15 119.709 0.078 . 1 . . . A 654 ALA N . 18695 1 443 . 1 1 70 70 GLU H H 1 8.459 0.016 . 1 . . . A 655 GLU H . 18695 1 444 . 1 1 70 70 GLU HA H 1 3.991 0.025 . 1 . . . A 655 GLU HA . 18695 1 445 . 1 1 70 70 GLU HB2 H 1 1.993 0.013 . 2 . . . A 655 GLU HB2 . 18695 1 446 . 1 1 70 70 GLU HB3 H 1 1.821 0.029 . 2 . . . A 655 GLU HB3 . 18695 1 447 . 1 1 70 70 GLU HG2 H 1 2.267 0.027 . 2 . . . A 655 GLU HG2 . 18695 1 448 . 1 1 70 70 GLU HG3 H 1 2.264 0.027 . 2 . . . A 655 GLU HG3 . 18695 1 449 . 1 1 70 70 GLU C C 13 177.455 0.000 . 1 . . . A 655 GLU C . 18695 1 450 . 1 1 70 70 GLU CA C 13 60.010 0.004 . 1 . . . A 655 GLU CA . 18695 1 451 . 1 1 70 70 GLU CB C 13 29.662 0.000 . 1 . . . A 655 GLU CB . 18695 1 452 . 1 1 70 70 GLU N N 15 118.371 0.034 . 1 . . . A 655 GLU N . 18695 1 453 . 1 1 71 71 LYS H H 1 7.766 0.007 . 1 . . . A 656 LYS H . 18695 1 454 . 1 1 71 71 LYS HA H 1 4.120 0.010 . 1 . . . A 656 LYS HA . 18695 1 455 . 1 1 71 71 LYS HB2 H 1 1.974 0.018 . 1 . . . A 656 LYS HB2 . 18695 1 456 . 1 1 71 71 LYS HB3 H 1 1.974 0.018 . 1 . . . A 656 LYS HB3 . 18695 1 457 . 1 1 71 71 LYS C C 13 178.423 0.000 . 1 . . . A 656 LYS C . 18695 1 458 . 1 1 71 71 LYS CA C 13 58.376 0.049 . 1 . . . A 656 LYS CA . 18695 1 459 . 1 1 71 71 LYS CB C 13 31.274 0.032 . 1 . . . A 656 LYS CB . 18695 1 460 . 1 1 71 71 LYS N N 15 119.253 0.039 . 1 . . . A 656 LYS N . 18695 1 461 . 1 1 72 72 ILE H H 1 8.121 0.015 . 1 . . . A 657 ILE H . 18695 1 462 . 1 1 72 72 ILE HA H 1 3.442 0.017 . 1 . . . A 657 ILE HA . 18695 1 463 . 1 1 72 72 ILE HB H 1 1.916 0.021 . 1 . . . A 657 ILE HB . 18695 1 464 . 1 1 72 72 ILE HG12 H 1 1.707 0.016 . 1 . . . A 657 ILE HG12 . 18695 1 465 . 1 1 72 72 ILE HG13 H 1 1.707 0.016 . 1 . . . A 657 ILE HG13 . 18695 1 466 . 1 1 72 72 ILE HG21 H 1 0.837 0.006 . 1 . . . A 657 ILE HG21 . 18695 1 467 . 1 1 72 72 ILE HG22 H 1 0.837 0.006 . 1 . . . A 657 ILE HG22 . 18695 1 468 . 1 1 72 72 ILE HG23 H 1 0.837 0.006 . 1 . . . A 657 ILE HG23 . 18695 1 469 . 1 1 72 72 ILE HD11 H 1 0.712 0.007 . 1 . . . A 657 ILE HD11 . 18695 1 470 . 1 1 72 72 ILE HD12 H 1 0.712 0.007 . 1 . . . A 657 ILE HD12 . 18695 1 471 . 1 1 72 72 ILE HD13 H 1 0.712 0.007 . 1 . . . A 657 ILE HD13 . 18695 1 472 . 1 1 72 72 ILE C C 13 176.810 0.000 . 1 . . . A 657 ILE C . 18695 1 473 . 1 1 72 72 ILE CA C 13 65.546 0.033 . 1 . . . A 657 ILE CA . 18695 1 474 . 1 1 72 72 ILE CB C 13 37.439 0.094 . 1 . . . A 657 ILE CB . 18695 1 475 . 1 1 72 72 ILE CG2 C 13 18.501 0.163 . 1 . . . A 657 ILE CG2 . 18695 1 476 . 1 1 72 72 ILE CD1 C 13 13.035 0.163 . 1 . . . A 657 ILE CD1 . 18695 1 477 . 1 1 72 72 ILE N N 15 117.639 0.070 . 1 . . . A 657 ILE N . 18695 1 478 . 1 1 73 73 TYR H H 1 8.879 0.008 . 1 . . . A 658 TYR H . 18695 1 479 . 1 1 73 73 TYR HB2 H 1 3.127 0.060 . 2 . . . A 658 TYR HB2 . 18695 1 480 . 1 1 73 73 TYR HB3 H 1 3.125 0.058 . 2 . . . A 658 TYR HB3 . 18695 1 481 . 1 1 73 73 TYR HD1 H 1 6.931 0.010 . 3 . . . A 658 TYR HD1 . 18695 1 482 . 1 1 73 73 TYR HD2 H 1 6.931 0.010 . 3 . . . A 658 TYR HD2 . 18695 1 483 . 1 1 73 73 TYR HE1 H 1 7.137 0.028 . 3 . . . A 658 TYR HE1 . 18695 1 484 . 1 1 73 73 TYR HE2 H 1 7.137 0.028 . 3 . . . A 658 TYR HE2 . 18695 1 485 . 1 1 73 73 TYR C C 13 177.199 0.000 . 1 . . . A 658 TYR C . 18695 1 486 . 1 1 73 73 TYR CA C 13 62.395 0.001 . 1 . . . A 658 TYR CA . 18695 1 487 . 1 1 73 73 TYR CD1 C 13 132.402 0.035 . 3 . . . A 658 TYR CD1 . 18695 1 488 . 1 1 73 73 TYR CD2 C 13 132.402 0.035 . 3 . . . A 658 TYR CD2 . 18695 1 489 . 1 1 73 73 TYR CE1 C 13 118.937 0.016 . 3 . . . A 658 TYR CE1 . 18695 1 490 . 1 1 73 73 TYR CE2 C 13 118.937 0.016 . 3 . . . A 658 TYR CE2 . 18695 1 491 . 1 1 73 73 TYR N N 15 120.790 0.021 . 1 . . . A 658 TYR N . 18695 1 492 . 1 1 74 74 LYS H H 1 8.427 0.010 . 1 . . . A 659 LYS H . 18695 1 493 . 1 1 74 74 LYS HA H 1 3.918 0.000 . 1 . . . A 659 LYS HA . 18695 1 494 . 1 1 74 74 LYS HB2 H 1 1.977 0.000 . 1 . . . A 659 LYS HB2 . 18695 1 495 . 1 1 74 74 LYS HB3 H 1 1.977 0.000 . 1 . . . A 659 LYS HB3 . 18695 1 496 . 1 1 74 74 LYS C C 13 180.195 0.000 . 1 . . . A 659 LYS C . 18695 1 497 . 1 1 74 74 LYS CA C 13 59.890 0.022 . 1 . . . A 659 LYS CA . 18695 1 498 . 1 1 74 74 LYS CB C 13 32.780 0.000 . 1 . . . A 659 LYS CB . 18695 1 499 . 1 1 74 74 LYS N N 15 117.005 0.070 . 1 . . . A 659 LYS N . 18695 1 500 . 1 1 75 75 ILE H H 1 8.422 0.013 . 1 . . . A 660 ILE H . 18695 1 501 . 1 1 75 75 ILE HA H 1 3.591 0.013 . 1 . . . A 660 ILE HA . 18695 1 502 . 1 1 75 75 ILE HB H 1 1.969 0.011 . 1 . . . A 660 ILE HB . 18695 1 503 . 1 1 75 75 ILE HG21 H 1 0.907 0.007 . 1 . . . A 660 ILE HG21 . 18695 1 504 . 1 1 75 75 ILE HG22 H 1 0.907 0.007 . 1 . . . A 660 ILE HG22 . 18695 1 505 . 1 1 75 75 ILE HG23 H 1 0.907 0.007 . 1 . . . A 660 ILE HG23 . 18695 1 506 . 1 1 75 75 ILE HD11 H 1 0.934 0.022 . 1 . . . A 660 ILE HD11 . 18695 1 507 . 1 1 75 75 ILE HD12 H 1 0.934 0.022 . 1 . . . A 660 ILE HD12 . 18695 1 508 . 1 1 75 75 ILE HD13 H 1 0.934 0.022 . 1 . . . A 660 ILE HD13 . 18695 1 509 . 1 1 75 75 ILE C C 13 177.460 0.000 . 1 . . . A 660 ILE C . 18695 1 510 . 1 1 75 75 ILE CA C 13 66.128 0.094 . 1 . . . A 660 ILE CA . 18695 1 511 . 1 1 75 75 ILE CB C 13 38.408 0.055 . 1 . . . A 660 ILE CB . 18695 1 512 . 1 1 75 75 ILE CG2 C 13 18.030 0.050 . 1 . . . A 660 ILE CG2 . 18695 1 513 . 1 1 75 75 ILE CD1 C 13 14.364 0.077 . 1 . . . A 660 ILE CD1 . 18695 1 514 . 1 1 75 75 ILE N N 15 121.312 0.063 . 1 . . . A 660 ILE N . 18695 1 515 . 1 1 76 76 GLN H H 1 8.888 0.009 . 1 . . . A 661 GLN H . 18695 1 516 . 1 1 76 76 GLN HA H 1 3.896 0.014 . 1 . . . A 661 GLN HA . 18695 1 517 . 1 1 76 76 GLN HB2 H 1 2.207 0.024 . 1 . . . A 661 GLN HB2 . 18695 1 518 . 1 1 76 76 GLN HB3 H 1 2.207 0.024 . 1 . . . A 661 GLN HB3 . 18695 1 519 . 1 1 76 76 GLN HG2 H 1 2.644 0.000 . 1 . . . A 661 GLN HG2 . 18695 1 520 . 1 1 76 76 GLN HG3 H 1 2.644 0.000 . 1 . . . A 661 GLN HG3 . 18695 1 521 . 1 1 76 76 GLN C C 13 180.038 0.000 . 1 . . . A 661 GLN C . 18695 1 522 . 1 1 76 76 GLN CA C 13 60.106 0.049 . 1 . . . A 661 GLN CA . 18695 1 523 . 1 1 76 76 GLN CB C 13 27.762 0.000 . 1 . . . A 661 GLN CB . 18695 1 524 . 1 1 76 76 GLN N N 15 118.553 0.021 . 1 . . . A 661 GLN N . 18695 1 525 . 1 1 77 77 LYS H H 1 8.107 0.008 . 1 . . . A 662 LYS H . 18695 1 526 . 1 1 77 77 LYS C C 13 179.364 0.000 . 1 . . . A 662 LYS C . 18695 1 527 . 1 1 77 77 LYS CA C 13 57.991 0.010 . 1 . . . A 662 LYS CA . 18695 1 528 . 1 1 77 77 LYS CB C 13 31.310 0.000 . 1 . . . A 662 LYS CB . 18695 1 529 . 1 1 77 77 LYS N N 15 118.014 0.099 . 1 . . . A 662 LYS N . 18695 1 530 . 1 1 78 78 GLU H H 1 8.039 0.013 . 1 . . . A 663 GLU H . 18695 1 531 . 1 1 78 78 GLU HA H 1 4.096 0.018 . 1 . . . A 663 GLU HA . 18695 1 532 . 1 1 78 78 GLU HB2 H 1 2.168 0.005 . 1 . . . A 663 GLU HB2 . 18695 1 533 . 1 1 78 78 GLU HB3 H 1 2.168 0.005 . 1 . . . A 663 GLU HB3 . 18695 1 534 . 1 1 78 78 GLU HG2 H 1 2.409 0.025 . 2 . . . A 663 GLU HG2 . 18695 1 535 . 1 1 78 78 GLU HG3 H 1 2.425 0.013 . 2 . . . A 663 GLU HG3 . 18695 1 536 . 1 1 78 78 GLU C C 13 179.289 0.000 . 1 . . . A 663 GLU C . 18695 1 537 . 1 1 78 78 GLU CA C 13 59.553 0.013 . 1 . . . A 663 GLU CA . 18695 1 538 . 1 1 78 78 GLU CB C 13 28.784 0.000 . 1 . . . A 663 GLU CB . 18695 1 539 . 1 1 78 78 GLU N N 15 122.154 0.098 . 1 . . . A 663 GLU N . 18695 1 540 . 1 1 79 79 LEU H H 1 8.500 0.018 . 1 . . . A 664 LEU H . 18695 1 541 . 1 1 79 79 LEU HA H 1 3.869 0.020 . 1 . . . A 664 LEU HA . 18695 1 542 . 1 1 79 79 LEU HB2 H 1 1.964 0.016 . 2 . . . A 664 LEU HB2 . 18695 1 543 . 1 1 79 79 LEU HB3 H 1 1.377 0.010 . 2 . . . A 664 LEU HB3 . 18695 1 544 . 1 1 79 79 LEU HG H 1 1.753 0.019 . 1 . . . A 664 LEU HG . 18695 1 545 . 1 1 79 79 LEU HD11 H 1 0.900 0.008 . 2 . . . A 664 LEU HD11 . 18695 1 546 . 1 1 79 79 LEU HD12 H 1 0.900 0.008 . 2 . . . A 664 LEU HD12 . 18695 1 547 . 1 1 79 79 LEU HD13 H 1 0.900 0.008 . 2 . . . A 664 LEU HD13 . 18695 1 548 . 1 1 79 79 LEU HD21 H 1 0.726 0.004 . 2 . . . A 664 LEU HD21 . 18695 1 549 . 1 1 79 79 LEU HD22 H 1 0.726 0.004 . 2 . . . A 664 LEU HD22 . 18695 1 550 . 1 1 79 79 LEU HD23 H 1 0.726 0.004 . 2 . . . A 664 LEU HD23 . 18695 1 551 . 1 1 79 79 LEU C C 13 178.863 0.000 . 1 . . . A 664 LEU C . 18695 1 552 . 1 1 79 79 LEU CA C 13 58.401 0.034 . 1 . . . A 664 LEU CA . 18695 1 553 . 1 1 79 79 LEU CB C 13 41.721 0.061 . 1 . . . A 664 LEU CB . 18695 1 554 . 1 1 79 79 LEU CG C 13 27.284 0.000 . 1 . . . A 664 LEU CG . 18695 1 555 . 1 1 79 79 LEU CD1 C 13 26.702 0.047 . 2 . . . A 664 LEU CD1 . 18695 1 556 . 1 1 79 79 LEU CD2 C 13 23.776 0.034 . 2 . . . A 664 LEU CD2 . 18695 1 557 . 1 1 79 79 LEU N N 15 120.017 0.059 . 1 . . . A 664 LEU N . 18695 1 558 . 1 1 80 80 GLU H H 1 8.030 0.010 . 1 . . . A 665 GLU H . 18695 1 559 . 1 1 80 80 GLU HA H 1 3.934 0.016 . 1 . . . A 665 GLU HA . 18695 1 560 . 1 1 80 80 GLU HB2 H 1 2.118 0.000 . 2 . . . A 665 GLU HB2 . 18695 1 561 . 1 1 80 80 GLU HB3 H 1 2.103 0.015 . 2 . . . A 665 GLU HB3 . 18695 1 562 . 1 1 80 80 GLU HG2 H 1 2.345 0.000 . 1 . . . A 665 GLU HG2 . 18695 1 563 . 1 1 80 80 GLU HG3 H 1 2.345 0.000 . 1 . . . A 665 GLU HG3 . 18695 1 564 . 1 1 80 80 GLU C C 13 179.049 0.000 . 1 . . . A 665 GLU C . 18695 1 565 . 1 1 80 80 GLU CA C 13 59.335 0.014 . 1 . . . A 665 GLU CA . 18695 1 566 . 1 1 80 80 GLU CB C 13 29.108 0.022 . 1 . . . A 665 GLU CB . 18695 1 567 . 1 1 80 80 GLU N N 15 118.340 0.073 . 1 . . . A 665 GLU N . 18695 1 568 . 1 1 81 81 GLU H H 1 7.844 0.009 . 1 . . . A 666 GLU H . 18695 1 569 . 1 1 81 81 GLU HA H 1 4.002 0.012 . 1 . . . A 666 GLU HA . 18695 1 570 . 1 1 81 81 GLU HB2 H 1 2.115 0.014 . 2 . . . A 666 GLU HB2 . 18695 1 571 . 1 1 81 81 GLU HB3 H 1 2.124 0.019 . 2 . . . A 666 GLU HB3 . 18695 1 572 . 1 1 81 81 GLU HG2 H 1 2.387 0.012 . 2 . . . A 666 GLU HG2 . 18695 1 573 . 1 1 81 81 GLU HG3 H 1 2.302 0.007 . 2 . . . A 666 GLU HG3 . 18695 1 574 . 1 1 81 81 GLU C C 13 179.357 0.000 . 1 . . . A 666 GLU C . 18695 1 575 . 1 1 81 81 GLU CA C 13 59.063 0.055 . 1 . . . A 666 GLU CA . 18695 1 576 . 1 1 81 81 GLU CB C 13 28.942 0.028 . 1 . . . A 666 GLU CB . 18695 1 577 . 1 1 81 81 GLU CG C 13 35.411 0.092 . 1 . . . A 666 GLU CG . 18695 1 578 . 1 1 81 81 GLU N N 15 118.765 0.006 . 1 . . . A 666 GLU N . 18695 1 579 . 1 1 82 82 LYS H H 1 8.029 0.014 . 1 . . . A 667 LYS H . 18695 1 580 . 1 1 82 82 LYS HA H 1 4.074 0.003 . 1 . . . A 667 LYS HA . 18695 1 581 . 1 1 82 82 LYS HD2 H 1 1.591 0.000 . 1 . . . A 667 LYS HD2 . 18695 1 582 . 1 1 82 82 LYS HD3 H 1 1.591 0.000 . 1 . . . A 667 LYS HD3 . 18695 1 583 . 1 1 82 82 LYS C C 13 179.419 0.000 . 1 . . . A 667 LYS C . 18695 1 584 . 1 1 82 82 LYS CA C 13 57.599 0.015 . 1 . . . A 667 LYS CA . 18695 1 585 . 1 1 82 82 LYS CB C 13 32.172 0.000 . 1 . . . A 667 LYS CB . 18695 1 586 . 1 1 82 82 LYS N N 15 118.988 0.132 . 1 . . . A 667 LYS N . 18695 1 587 . 1 1 83 83 ARG H H 1 8.201 0.011 . 1 . . . A 668 ARG H . 18695 1 588 . 1 1 83 83 ARG HA H 1 3.950 0.011 . 1 . . . A 668 ARG HA . 18695 1 589 . 1 1 83 83 ARG HB2 H 1 1.845 0.019 . 1 . . . A 668 ARG HB2 . 18695 1 590 . 1 1 83 83 ARG HB3 H 1 1.845 0.019 . 1 . . . A 668 ARG HB3 . 18695 1 591 . 1 1 83 83 ARG HG2 H 1 1.567 0.000 . 1 . . . A 668 ARG HG2 . 18695 1 592 . 1 1 83 83 ARG HG3 H 1 1.567 0.000 . 1 . . . A 668 ARG HG3 . 18695 1 593 . 1 1 83 83 ARG HD2 H 1 3.121 0.000 . 2 . . . A 668 ARG HD2 . 18695 1 594 . 1 1 83 83 ARG HD3 H 1 3.120 0.001 . 2 . . . A 668 ARG HD3 . 18695 1 595 . 1 1 83 83 ARG C C 13 178.177 0.000 . 1 . . . A 668 ARG C . 18695 1 596 . 1 1 83 83 ARG CA C 13 59.150 0.089 . 1 . . . A 668 ARG CA . 18695 1 597 . 1 1 83 83 ARG CB C 13 30.301 0.000 . 1 . . . A 668 ARG CB . 18695 1 598 . 1 1 83 83 ARG CD C 13 43.624 0.000 . 1 . . . A 668 ARG CD . 18695 1 599 . 1 1 83 83 ARG N N 15 119.302 0.065 . 1 . . . A 668 ARG N . 18695 1 600 . 1 1 84 84 ARG H H 1 7.759 0.010 . 1 . . . A 669 ARG H . 18695 1 601 . 1 1 84 84 ARG HA H 1 4.160 0.007 . 1 . . . A 669 ARG HA . 18695 1 602 . 1 1 84 84 ARG HB2 H 1 1.878 0.008 . 2 . . . A 669 ARG HB2 . 18695 1 603 . 1 1 84 84 ARG HB3 H 1 1.877 0.008 . 2 . . . A 669 ARG HB3 . 18695 1 604 . 1 1 84 84 ARG HG2 H 1 1.685 0.000 . 1 . . . A 669 ARG HG2 . 18695 1 605 . 1 1 84 84 ARG HG3 H 1 1.685 0.000 . 1 . . . A 669 ARG HG3 . 18695 1 606 . 1 1 84 84 ARG HD2 H 1 3.159 0.000 . 1 . . . A 669 ARG HD2 . 18695 1 607 . 1 1 84 84 ARG HD3 H 1 3.159 0.000 . 1 . . . A 669 ARG HD3 . 18695 1 608 . 1 1 84 84 ARG C C 13 177.297 0.000 . 1 . . . A 669 ARG C . 18695 1 609 . 1 1 84 84 ARG CA C 13 57.802 0.003 . 1 . . . A 669 ARG CA . 18695 1 610 . 1 1 84 84 ARG CB C 13 30.322 0.055 . 1 . . . A 669 ARG CB . 18695 1 611 . 1 1 84 84 ARG N N 15 118.035 0.060 . 1 . . . A 669 ARG N . 18695 1 612 . 1 1 85 85 SER H H 1 7.785 0.006 . 1 . . . A 670 SER H . 18695 1 613 . 1 1 85 85 SER HA H 1 4.398 0.009 . 1 . . . A 670 SER HA . 18695 1 614 . 1 1 85 85 SER HB2 H 1 3.913 0.010 . 2 . . . A 670 SER HB2 . 18695 1 615 . 1 1 85 85 SER HB3 H 1 3.918 0.012 . 2 . . . A 670 SER HB3 . 18695 1 616 . 1 1 85 85 SER C C 13 174.236 0.000 . 1 . . . A 670 SER C . 18695 1 617 . 1 1 85 85 SER CA C 13 59.101 0.003 . 1 . . . A 670 SER CA . 18695 1 618 . 1 1 85 85 SER CB C 13 63.809 0.079 . 1 . . . A 670 SER CB . 18695 1 619 . 1 1 85 85 SER N N 15 114.264 0.038 . 1 . . . A 670 SER N . 18695 1 620 . 1 1 86 86 ARG H H 1 7.734 0.003 . 1 . . . A 671 ARG H . 18695 1 621 . 1 1 86 86 ARG HA H 1 4.329 0.015 . 1 . . . A 671 ARG HA . 18695 1 622 . 1 1 86 86 ARG HB2 H 1 1.739 0.000 . 2 . . . A 671 ARG HB2 . 18695 1 623 . 1 1 86 86 ARG HB3 H 1 1.915 0.007 . 2 . . . A 671 ARG HB3 . 18695 1 624 . 1 1 86 86 ARG HG2 H 1 1.663 0.000 . 2 . . . A 671 ARG HG2 . 18695 1 625 . 1 1 86 86 ARG HG3 H 1 1.734 0.005 . 2 . . . A 671 ARG HG3 . 18695 1 626 . 1 1 86 86 ARG HD2 H 1 3.146 0.000 . 2 . . . A 671 ARG HD2 . 18695 1 627 . 1 1 86 86 ARG HD3 H 1 3.147 0.000 . 2 . . . A 671 ARG HD3 . 18695 1 628 . 1 1 86 86 ARG C C 13 175.293 0.000 . 1 . . . A 671 ARG C . 18695 1 629 . 1 1 86 86 ARG CA C 13 56.326 0.000 . 1 . . . A 671 ARG CA . 18695 1 630 . 1 1 86 86 ARG CB C 13 30.677 0.045 . 1 . . . A 671 ARG CB . 18695 1 631 . 1 1 86 86 ARG CG C 13 26.913 0.000 . 1 . . . A 671 ARG CG . 18695 1 632 . 1 1 86 86 ARG CD C 13 43.792 0.000 . 1 . . . A 671 ARG CD . 18695 1 633 . 1 1 86 86 ARG N N 15 122.047 0.053 . 1 . . . A 671 ARG N . 18695 1 634 . 1 1 87 87 LEU H H 1 7.698 0.056 . 1 . . . A 672 LEU H . 18695 1 635 . 1 1 87 87 LEU HA H 1 4.143 0.014 . 1 . . . A 672 LEU HA . 18695 1 636 . 1 1 87 87 LEU HB2 H 1 1.543 0.016 . 2 . . . A 672 LEU HB2 . 18695 1 637 . 1 1 87 87 LEU HB3 H 1 1.581 0.009 . 2 . . . A 672 LEU HB3 . 18695 1 638 . 1 1 87 87 LEU HG H 1 1.590 0.008 . 1 . . . A 672 LEU HG . 18695 1 639 . 1 1 87 87 LEU HD11 H 1 0.862 0.008 . 2 . . . A 672 LEU HD11 . 18695 1 640 . 1 1 87 87 LEU HD12 H 1 0.862 0.008 . 2 . . . A 672 LEU HD12 . 18695 1 641 . 1 1 87 87 LEU HD13 H 1 0.862 0.008 . 2 . . . A 672 LEU HD13 . 18695 1 642 . 1 1 87 87 LEU HD21 H 1 0.834 0.017 . 2 . . . A 672 LEU HD21 . 18695 1 643 . 1 1 87 87 LEU HD22 H 1 0.834 0.017 . 2 . . . A 672 LEU HD22 . 18695 1 644 . 1 1 87 87 LEU HD23 H 1 0.834 0.017 . 2 . . . A 672 LEU HD23 . 18695 1 645 . 1 1 87 87 LEU CA C 13 56.591 0.037 . 1 . . . A 672 LEU CA . 18695 1 646 . 1 1 87 87 LEU CB C 13 43.172 0.073 . 1 . . . A 672 LEU CB . 18695 1 647 . 1 1 87 87 LEU CG C 13 27.181 0.000 . 1 . . . A 672 LEU CG . 18695 1 648 . 1 1 87 87 LEU CD1 C 13 25.291 0.027 . 2 . . . A 672 LEU CD1 . 18695 1 649 . 1 1 87 87 LEU CD2 C 13 23.358 0.069 . 2 . . . A 672 LEU CD2 . 18695 1 650 . 1 1 87 87 LEU N N 15 127.942 0.089 . 1 . . . A 672 LEU N . 18695 1 651 . 3 3 1 1 ASP H H 1 8.092 0.009 . 1 . . . C 116 ASP H1 . 18695 1 652 . 3 3 1 1 ASP HA H 1 4.521 0.019 . 1 . . . C 116 ASP HA . 18695 1 653 . 3 3 1 1 ASP HB2 H 1 2.694 0.006 . 2 . . . C 116 ASP HB2 . 18695 1 654 . 3 3 1 1 ASP HB3 H 1 2.695 0.007 . 2 . . . C 116 ASP HB3 . 18695 1 655 . 3 3 1 1 ASP C C 13 176.304 0.012 . 1 . . . C 116 ASP C . 18695 1 656 . 3 3 1 1 ASP CA C 13 54.783 0.002 . 1 . . . C 116 ASP CA . 18695 1 657 . 3 3 1 1 ASP CB C 13 41.092 0.066 . 1 . . . C 116 ASP CB . 18695 1 658 . 3 3 1 1 ASP N N 15 120.754 0.007 . 1 . . . C 116 ASP N . 18695 1 659 . 3 3 2 2 SER H H 1 8.266 0.007 . 1 . . . C 117 SER H . 18695 1 660 . 3 3 2 2 SER HA H 1 4.451 0.015 . 1 . . . C 117 SER HA . 18695 1 661 . 3 3 2 2 SER HB2 H 1 3.893 0.019 . 2 . . . C 117 SER HB2 . 18695 1 662 . 3 3 2 2 SER HB3 H 1 3.909 0.020 . 2 . . . C 117 SER HB3 . 18695 1 663 . 3 3 2 2 SER C C 13 174.893 0.000 . 1 . . . C 117 SER C . 18695 1 664 . 3 3 2 2 SER CA C 13 58.653 0.019 . 1 . . . C 117 SER CA . 18695 1 665 . 3 3 2 2 SER CB C 13 63.748 0.059 . 1 . . . C 117 SER CB . 18695 1 666 . 3 3 2 2 SER N N 15 115.611 0.021 . 1 . . . C 117 SER N . 18695 1 667 . 3 3 3 3 VAL H H 1 8.110 0.010 . 1 . . . C 118 VAL H . 18695 1 668 . 3 3 3 3 VAL HA H 1 4.148 0.014 . 1 . . . C 118 VAL HA . 18695 1 669 . 3 3 3 3 VAL HB H 1 2.122 0.012 . 1 . . . C 118 VAL HB . 18695 1 670 . 3 3 3 3 VAL HG11 H 1 0.950 0.005 . 2 . . . C 118 VAL HG11 . 18695 1 671 . 3 3 3 3 VAL HG12 H 1 0.950 0.005 . 2 . . . C 118 VAL HG12 . 18695 1 672 . 3 3 3 3 VAL HG13 H 1 0.950 0.005 . 2 . . . C 118 VAL HG13 . 18695 1 673 . 3 3 3 3 VAL HG21 H 1 0.956 0.004 . 2 . . . C 118 VAL HG21 . 18695 1 674 . 3 3 3 3 VAL HG22 H 1 0.956 0.004 . 2 . . . C 118 VAL HG22 . 18695 1 675 . 3 3 3 3 VAL HG23 H 1 0.956 0.004 . 2 . . . C 118 VAL HG23 . 18695 1 676 . 3 3 3 3 VAL C C 13 176.909 0.007 . 1 . . . C 118 VAL C . 18695 1 677 . 3 3 3 3 VAL CA C 13 63.122 0.012 . 1 . . . C 118 VAL CA . 18695 1 678 . 3 3 3 3 VAL CB C 13 32.396 0.090 . 1 . . . C 118 VAL CB . 18695 1 679 . 3 3 3 3 VAL CG1 C 13 20.960 0.090 . 2 . . . C 118 VAL CG1 . 18695 1 680 . 3 3 3 3 VAL CG2 C 13 21.215 0.063 . 2 . . . C 118 VAL CG2 . 18695 1 681 . 3 3 3 3 VAL N N 15 122.158 0.019 . 1 . . . C 118 VAL N . 18695 1 682 . 3 3 4 4 THR H H 1 8.175 0.005 . 1 . . . C 119 THR H . 18695 1 683 . 3 3 4 4 THR HA H 1 4.288 0.006 . 1 . . . C 119 THR HA . 18695 1 684 . 3 3 4 4 THR HB H 1 4.167 0.000 . 1 . . . C 119 THR HB . 18695 1 685 . 3 3 4 4 THR HG21 H 1 1.233 0.009 . 1 . . . C 119 THR HG1 . 18695 1 686 . 3 3 4 4 THR HG22 H 1 1.233 0.009 . 1 . . . C 119 THR HG1 . 18695 1 687 . 3 3 4 4 THR HG23 H 1 1.233 0.009 . 1 . . . C 119 THR HG1 . 18695 1 688 . 3 3 4 4 THR C C 13 175.180 0.006 . 1 . . . C 119 THR C . 18695 1 689 . 3 3 4 4 THR CA C 13 62.723 0.036 . 1 . . . C 119 THR CA . 18695 1 690 . 3 3 4 4 THR CB C 13 69.600 0.000 . 1 . . . C 119 THR CB . 18695 1 691 . 3 3 4 4 THR CG2 C 13 21.842 0.031 . 1 . . . C 119 THR CG2 . 18695 1 692 . 3 3 4 4 THR N N 15 116.781 0.073 . 1 . . . C 119 THR N . 18695 1 693 . 3 3 5 5 ASP H H 1 8.319 0.005 . 1 . . . C 120 ASP H . 18695 1 694 . 3 3 5 5 ASP HA H 1 4.545 0.021 . 1 . . . C 120 ASP HA . 18695 1 695 . 3 3 5 5 ASP HB2 H 1 2.702 0.006 . 2 . . . C 120 ASP HB2 . 18695 1 696 . 3 3 5 5 ASP HB3 H 1 2.700 0.005 . 2 . . . C 120 ASP HB3 . 18695 1 697 . 3 3 5 5 ASP C C 13 177.546 0.004 . 1 . . . C 120 ASP C . 18695 1 698 . 3 3 5 5 ASP CA C 13 55.831 0.016 . 1 . . . C 120 ASP CA . 18695 1 699 . 3 3 5 5 ASP CB C 13 41.141 0.073 . 1 . . . C 120 ASP CB . 18695 1 700 . 3 3 5 5 ASP N N 15 122.504 0.042 . 1 . . . C 120 ASP N . 18695 1 701 . 3 3 6 6 SER H H 1 8.400 0.007 . 1 . . . C 121 SER H . 18695 1 702 . 3 3 6 6 SER HA H 1 4.140 0.004 . 1 . . . C 121 SER HA . 18695 1 703 . 3 3 6 6 SER HB2 H 1 3.916 0.011 . 2 . . . C 121 SER HB2 . 18695 1 704 . 3 3 6 6 SER HB3 H 1 3.933 0.014 . 2 . . . C 121 SER HB3 . 18695 1 705 . 3 3 6 6 SER C C 13 176.400 0.001 . 1 . . . C 121 SER C . 18695 1 706 . 3 3 6 6 SER CA C 13 61.002 0.008 . 1 . . . C 121 SER CA . 18695 1 707 . 3 3 6 6 SER CB C 13 63.018 0.157 . 1 . . . C 121 SER CB . 18695 1 708 . 3 3 6 6 SER N N 15 116.525 0.029 . 1 . . . C 121 SER N . 18695 1 709 . 3 3 7 7 GLN H H 1 8.142 0.013 . 1 . . . C 122 GLN H . 18695 1 710 . 3 3 7 7 GLN HA H 1 4.030 0.009 . 1 . . . C 122 GLN HA . 18695 1 711 . 3 3 7 7 GLN HB2 H 1 2.111 0.018 . 2 . . . C 122 GLN HB2 . 18695 1 712 . 3 3 7 7 GLN HB3 H 1 2.128 0.014 . 2 . . . C 122 GLN HB3 . 18695 1 713 . 3 3 7 7 GLN HG2 H 1 2.382 0.014 . 2 . . . C 122 GLN HG2 . 18695 1 714 . 3 3 7 7 GLN HG3 H 1 2.361 0.009 . 2 . . . C 122 GLN HG3 . 18695 1 715 . 3 3 7 7 GLN HE21 H 1 7.590 0.002 . 1 . . . C 122 GLN HE21 . 18695 1 716 . 3 3 7 7 GLN HE22 H 1 6.804 0.002 . 1 . . . C 122 GLN HE22 . 18695 1 717 . 3 3 7 7 GLN C C 13 178.031 0.008 . 1 . . . C 122 GLN C . 18695 1 718 . 3 3 7 7 GLN CA C 13 58.429 0.032 . 1 . . . C 122 GLN CA . 18695 1 719 . 3 3 7 7 GLN CB C 13 28.223 0.066 . 1 . . . C 122 GLN CB . 18695 1 720 . 3 3 7 7 GLN CG C 13 33.841 0.022 . 1 . . . C 122 GLN CG . 18695 1 721 . 3 3 7 7 GLN N N 15 122.204 0.018 . 1 . . . C 122 GLN N . 18695 1 722 . 3 3 7 7 GLN NE2 N 15 112.089 0.034 . 1 . . . C 122 GLN NE2 . 18695 1 723 . 3 3 8 8 LYS H H 1 8.104 0.009 . 1 . . . C 123 LYS H . 18695 1 724 . 3 3 8 8 LYS HA H 1 4.045 0.019 . 1 . . . C 123 LYS HA . 18695 1 725 . 3 3 8 8 LYS HB2 H 1 1.846 0.009 . 1 . . . C 123 LYS HB2 . 18695 1 726 . 3 3 8 8 LYS HB3 H 1 1.846 0.009 . 1 . . . C 123 LYS HB3 . 18695 1 727 . 3 3 8 8 LYS HG2 H 1 1.471 0.000 . 1 . . . C 123 LYS HG2 . 18695 1 728 . 3 3 8 8 LYS HG3 H 1 1.471 0.000 . 1 . . . C 123 LYS HG3 . 18695 1 729 . 3 3 8 8 LYS C C 13 178.553 0.009 . 1 . . . C 123 LYS C . 18695 1 730 . 3 3 8 8 LYS CA C 13 58.438 0.045 . 1 . . . C 123 LYS CA . 18695 1 731 . 3 3 8 8 LYS CB C 13 30.059 0.161 . 1 . . . C 123 LYS CB . 18695 1 732 . 3 3 8 8 LYS N N 15 120.800 0.032 . 1 . . . C 123 LYS N . 18695 1 733 . 3 3 9 9 ARG H H 1 8.073 0.010 . 1 . . . C 124 ARG H . 18695 1 734 . 3 3 9 9 ARG HA H 1 3.970 0.012 . 1 . . . C 124 ARG HA . 18695 1 735 . 3 3 9 9 ARG HB2 H 1 1.835 0.005 . 2 . . . C 124 ARG HB2 . 18695 1 736 . 3 3 9 9 ARG HB3 H 1 1.835 0.006 . 2 . . . C 124 ARG HB3 . 18695 1 737 . 3 3 9 9 ARG HG2 H 1 1.541 0.004 . 2 . . . C 124 ARG HG2 . 18695 1 738 . 3 3 9 9 ARG HG3 H 1 1.735 0.014 . 2 . . . C 124 ARG HG3 . 18695 1 739 . 3 3 9 9 ARG HD2 H 1 3.198 0.005 . 1 . . . C 124 ARG HD2 . 18695 1 740 . 3 3 9 9 ARG HD3 H 1 3.198 0.005 . 1 . . . C 124 ARG HD3 . 18695 1 741 . 3 3 9 9 ARG C C 13 178.235 0.002 . 1 . . . C 124 ARG C . 18695 1 742 . 3 3 9 9 ARG CA C 13 58.944 0.035 . 1 . . . C 124 ARG CA . 18695 1 743 . 3 3 9 9 ARG CB C 13 30.180 0.073 . 1 . . . C 124 ARG CB . 18695 1 744 . 3 3 9 9 ARG CG C 13 27.838 0.064 . 1 . . . C 124 ARG CG . 18695 1 745 . 3 3 9 9 ARG N N 15 118.721 0.012 . 1 . . . C 124 ARG N . 18695 1 746 . 3 3 10 10 ARG H H 1 7.881 0.014 . 1 . . . C 125 ARG H . 18695 1 747 . 3 3 10 10 ARG HA H 1 3.950 0.018 . 1 . . . C 125 ARG HA . 18695 1 748 . 3 3 10 10 ARG HB2 H 1 1.781 0.011 . 1 . . . C 125 ARG HB2 . 18695 1 749 . 3 3 10 10 ARG HB3 H 1 1.781 0.011 . 1 . . . C 125 ARG HB3 . 18695 1 750 . 3 3 10 10 ARG HG2 H 1 1.528 0.014 . 1 . . . C 125 ARG HG2 . 18695 1 751 . 3 3 10 10 ARG HG3 H 1 1.528 0.014 . 1 . . . C 125 ARG HG3 . 18695 1 752 . 3 3 10 10 ARG HD2 H 1 2.955 0.013 . 1 . . . C 125 ARG HD2 . 18695 1 753 . 3 3 10 10 ARG HD3 H 1 2.955 0.013 . 1 . . . C 125 ARG HD3 . 18695 1 754 . 3 3 10 10 ARG C C 13 178.073 0.022 . 1 . . . C 125 ARG C . 18695 1 755 . 3 3 10 10 ARG CA C 13 58.887 0.030 . 1 . . . C 125 ARG CA . 18695 1 756 . 3 3 10 10 ARG CB C 13 29.990 0.021 . 1 . . . C 125 ARG CB . 18695 1 757 . 3 3 10 10 ARG N N 15 119.866 0.023 . 1 . . . C 125 ARG N . 18695 1 758 . 3 3 11 11 GLU H H 1 8.053 0.006 . 1 . . . C 126 GLU H . 18695 1 759 . 3 3 11 11 GLU HA H 1 3.973 0.009 . 1 . . . C 126 GLU HA . 18695 1 760 . 3 3 11 11 GLU HB2 H 1 2.062 0.006 . 2 . . . C 126 GLU HB2 . 18695 1 761 . 3 3 11 11 GLU HB3 H 1 2.068 0.011 . 2 . . . C 126 GLU HB3 . 18695 1 762 . 3 3 11 11 GLU HG2 H 1 2.325 0.011 . 2 . . . C 126 GLU HG2 . 18695 1 763 . 3 3 11 11 GLU HG3 H 1 2.170 0.002 . 2 . . . C 126 GLU HG3 . 18695 1 764 . 3 3 11 11 GLU C C 13 178.575 0.003 . 1 . . . C 126 GLU C . 18695 1 765 . 3 3 11 11 GLU CA C 13 58.839 0.082 . 1 . . . C 126 GLU CA . 18695 1 766 . 3 3 11 11 GLU CB C 13 29.455 0.031 . 1 . . . C 126 GLU CB . 18695 1 767 . 3 3 11 11 GLU CG C 13 36.145 0.021 . 1 . . . C 126 GLU CG . 18695 1 768 . 3 3 11 11 GLU N N 15 121.372 0.070 . 1 . . . C 126 GLU N . 18695 1 769 . 3 3 12 12 ILE H H 1 7.766 0.006 . 1 . . . C 127 ILE H . 18695 1 770 . 3 3 12 12 ILE HA H 1 3.681 0.007 . 1 . . . C 127 ILE HA . 18695 1 771 . 3 3 12 12 ILE HB H 1 1.817 0.004 . 1 . . . C 127 ILE HB . 18695 1 772 . 3 3 12 12 ILE HG12 H 1 1.121 0.015 . 2 . . . C 127 ILE HG12 . 18695 1 773 . 3 3 12 12 ILE HG13 H 1 1.620 0.007 . 2 . . . C 127 ILE HG13 . 18695 1 774 . 3 3 12 12 ILE HG21 H 1 0.858 0.014 . 1 . . . C 127 ILE HG21 . 18695 1 775 . 3 3 12 12 ILE HG22 H 1 0.858 0.014 . 1 . . . C 127 ILE HG21 . 18695 1 776 . 3 3 12 12 ILE HG23 H 1 0.858 0.014 . 1 . . . C 127 ILE HG23 . 18695 1 777 . 3 3 12 12 ILE HD11 H 1 0.825 0.021 . 1 . . . C 127 ILE HD11 . 18695 1 778 . 3 3 12 12 ILE HD12 H 1 0.825 0.021 . 1 . . . C 127 ILE HD12 . 18695 1 779 . 3 3 12 12 ILE HD13 H 1 0.825 0.021 . 1 . . . C 127 ILE HD13 . 18695 1 780 . 3 3 12 12 ILE C C 13 178.873 0.034 . 1 . . . C 127 ILE C . 18695 1 781 . 3 3 12 12 ILE CA C 13 64.189 0.031 . 1 . . . C 127 ILE CA . 18695 1 782 . 3 3 12 12 ILE CB C 13 38.408 0.075 . 1 . . . C 127 ILE CB . 18695 1 783 . 3 3 12 12 ILE CG1 C 13 28.563 0.082 . 1 . . . C 127 ILE CG1 . 18695 1 784 . 3 3 12 12 ILE CG2 C 13 17.408 0.087 . 1 . . . C 127 ILE CG2 . 18695 1 785 . 3 3 12 12 ILE CD1 C 13 13.244 0.038 . 1 . . . C 127 ILE CD1 . 18695 1 786 . 3 3 12 12 ILE N N 15 119.812 0.035 . 1 . . . C 127 ILE N . 18695 1 787 . 3 3 13 13 LEU H H 1 7.901 0.008 . 1 . . . C 128 LEU H . 18695 1 788 . 3 3 13 13 LEU HA H 1 3.895 0.007 . 1 . . . C 128 LEU HA . 18695 1 789 . 3 3 13 13 LEU HB2 H 1 1.802 0.016 . 1 . . . C 128 LEU HB2 . 18695 1 790 . 3 3 13 13 LEU HB3 H 1 1.802 0.016 . 1 . . . C 128 LEU HB3 . 18695 1 791 . 3 3 13 13 LEU HD11 H 1 0.409 0.018 . 2 . . . C 128 LEU HD11 . 18695 1 792 . 3 3 13 13 LEU HD12 H 1 0.409 0.018 . 2 . . . C 128 LEU HD12 . 18695 1 793 . 3 3 13 13 LEU HD13 H 1 0.409 0.018 . 2 . . . C 128 LEU HD13 . 18695 1 794 . 3 3 13 13 LEU HD21 H 1 0.380 0.011 . 2 . . . C 128 LEU HD21 . 18695 1 795 . 3 3 13 13 LEU HD22 H 1 0.380 0.011 . 2 . . . C 128 LEU HD23 . 18695 1 796 . 3 3 13 13 LEU HD23 H 1 0.380 0.011 . 2 . . . C 128 LEU HD23 . 18695 1 797 . 3 3 13 13 LEU C C 13 177.961 0.000 . 1 . . . C 128 LEU C . 18695 1 798 . 3 3 13 13 LEU CA C 13 57.881 0.023 . 1 . . . C 128 LEU CA . 18695 1 799 . 3 3 13 13 LEU CB C 13 40.412 0.000 . 1 . . . C 128 LEU CB . 18695 1 800 . 3 3 13 13 LEU CD2 C 13 24.277 0.100 . 2 . . . C 128 LEU CD2 . 18695 1 801 . 3 3 13 13 LEU N N 15 122.163 0.041 . 1 . . . C 128 LEU N . 18695 1 802 . 3 3 14 14 SER H H 1 7.666 0.009 . 1 . . . C 129 SER H . 18695 1 803 . 3 3 14 14 SER HA H 1 3.888 0.001 . 1 . . . C 129 SER HA . 18695 1 804 . 3 3 14 14 SER HB2 H 1 3.704 0.000 . 1 . . . C 129 SER HB2 . 18695 1 805 . 3 3 14 14 SER HB3 H 1 3.704 0.000 . 1 . . . C 129 SER HB3 . 18695 1 806 . 3 3 14 14 SER C C 13 174.397 0.000 . 1 . . . C 129 SER C . 18695 1 807 . 3 3 14 14 SER CA C 13 60.842 0.028 . 1 . . . C 129 SER CA . 18695 1 808 . 3 3 14 14 SER CB C 13 62.873 0.000 . 1 . . . C 129 SER CB . 18695 1 809 . 3 3 14 14 SER N N 15 109.832 0.038 . 1 . . . C 129 SER N . 18695 1 810 . 3 3 15 15 ARG H H 1 7.169 0.003 . 1 . . . C 130 ARG H . 18695 1 811 . 3 3 15 15 ARG HA H 1 4.318 0.004 . 1 . . . C 130 ARG HA . 18695 1 812 . 3 3 15 15 ARG HB2 H 1 1.771 0.011 . 2 . . . C 130 ARG HB2 . 18695 1 813 . 3 3 15 15 ARG HB3 H 1 1.756 0.000 . 2 . . . C 130 ARG HB3 . 18695 1 814 . 3 3 15 15 ARG HG2 H 1 2.073 0.000 . 1 . . . C 130 ARG HG2 . 18695 1 815 . 3 3 15 15 ARG HG3 H 1 2.073 0.000 . 1 . . . C 130 ARG HG3 . 18695 1 816 . 3 3 15 15 ARG HD2 H 1 3.212 0.025 . 2 . . . C 130 ARG HD2 . 18695 1 817 . 3 3 15 15 ARG HD3 H 1 3.203 0.026 . 2 . . . C 130 ARG HD3 . 18695 1 818 . 3 3 15 15 ARG C C 13 177.152 0.013 . 1 . . . C 130 ARG C . 18695 1 819 . 3 3 15 15 ARG CA C 13 56.106 0.003 . 1 . . . C 130 ARG CA . 18695 1 820 . 3 3 15 15 ARG CB C 13 27.714 0.017 . 1 . . . C 130 ARG CB . 18695 1 821 . 3 3 15 15 ARG N N 15 117.950 0.027 . 1 . . . C 130 ARG N . 18695 1 822 . 3 3 16 16 ARG H H 1 8.200 0.015 . 1 . . . C 131 ARG H . 18695 1 823 . 3 3 16 16 ARG HA H 1 4.288 0.005 . 1 . . . C 131 ARG HA . 18695 1 824 . 3 3 16 16 ARG HD2 H 1 3.228 0.002 . 1 . . . C 131 ARG HD2 . 18695 1 825 . 3 3 16 16 ARG HD3 H 1 3.228 0.002 . 1 . . . C 131 ARG HD3 . 18695 1 826 . 3 3 16 16 ARG CA C 13 52.594 0.000 . 1 . . . C 131 ARG CA . 18695 1 827 . 3 3 16 16 ARG CB C 13 28.102 0.000 . 1 . . . C 131 ARG CB . 18695 1 828 . 3 3 16 16 ARG N N 15 121.605 0.021 . 1 . . . C 131 ARG N . 18695 1 829 . 3 3 18 18 SEP N N 15 113.204 0.000 . 1 . . . C 133 SEP N . 18695 1 830 . 3 3 19 19 TYR H H 1 6.922 0.008 . 1 . . . C 134 TYR H . 18695 1 831 . 3 3 19 19 TYR HA H 1 4.263 0.016 . 1 . . . C 134 TYR HA . 18695 1 832 . 3 3 19 19 TYR HB2 H 1 3.709 0.006 . 1 . . . C 134 TYR HB2 . 18695 1 833 . 3 3 19 19 TYR HB3 H 1 3.709 0.006 . 1 . . . C 134 TYR HB3 . 18695 1 834 . 3 3 19 19 TYR HD1 H 1 6.449 0.022 . 3 . . . C 134 TYR HD1 . 18695 1 835 . 3 3 19 19 TYR HD2 H 1 6.449 0.022 . 3 . . . C 134 TYR HD2 . 18695 1 836 . 3 3 19 19 TYR HE1 H 1 6.578 0.000 . 3 . . . C 134 TYR HE1 . 18695 1 837 . 3 3 19 19 TYR HE2 H 1 6.578 0.000 . 3 . . . C 134 TYR HE2 . 18695 1 838 . 3 3 19 19 TYR C C 13 178.247 0.000 . 1 . . . C 134 TYR C . 18695 1 839 . 3 3 19 19 TYR CA C 13 64.466 0.000 . 1 . . . C 134 TYR CA . 18695 1 840 . 3 3 19 19 TYR CD1 C 13 132.198 0.000 . 3 . . . C 134 TYR CD1 . 18695 1 841 . 3 3 19 19 TYR CD2 C 13 132.198 0.000 . 3 . . . C 134 TYR CD2 . 18695 1 842 . 3 3 19 19 TYR CE1 C 13 116.864 0.000 . 3 . . . C 134 TYR CE1 . 18695 1 843 . 3 3 19 19 TYR CE2 C 13 116.864 0.000 . 3 . . . C 134 TYR CE2 . 18695 1 844 . 3 3 19 19 TYR N N 15 119.826 0.049 . 1 . . . C 134 TYR N . 18695 1 845 . 3 3 20 20 ARG H H 1 8.015 0.009 . 1 . . . C 135 ARG H . 18695 1 846 . 3 3 20 20 ARG HA H 1 4.001 0.000 . 1 . . . C 135 ARG HA . 18695 1 847 . 3 3 20 20 ARG HB2 H 1 1.897 0.000 . 1 . . . C 135 ARG HB2 . 18695 1 848 . 3 3 20 20 ARG HG2 H 1 1.480 0.023 . 2 . . . C 135 ARG HG2 . 18695 1 849 . 3 3 20 20 ARG HG3 H 1 1.466 0.021 . 2 . . . C 135 ARG HG3 . 18695 1 850 . 3 3 20 20 ARG C C 13 176.524 0.000 . 1 . . . C 135 ARG C . 18695 1 851 . 3 3 20 20 ARG CA C 13 59.727 0.000 . 1 . . . C 135 ARG CA . 18695 1 852 . 3 3 20 20 ARG N N 15 118.319 0.044 . 1 . . . C 135 ARG N . 18695 1 853 . 3 3 21 21 LYS H H 1 8.258 0.005 . 1 . . . C 136 LYS H . 18695 1 854 . 3 3 21 21 LYS HA H 1 4.240 0.000 . 1 . . . C 136 LYS HA . 18695 1 855 . 3 3 21 21 LYS HB2 H 1 1.910 0.019 . 1 . . . C 136 LYS HB2 . 18695 1 856 . 3 3 21 21 LYS HB3 H 1 1.910 0.019 . 1 . . . C 136 LYS HB3 . 18695 1 857 . 3 3 21 21 LYS CA C 13 59.884 0.000 . 1 . . . C 136 LYS CA . 18695 1 858 . 3 3 21 21 LYS N N 15 119.202 0.036 . 1 . . . C 136 LYS N . 18695 1 859 . 3 3 22 22 ILE H H 1 7.156 0.019 . 1 . . . C 137 ILE H . 18695 1 860 . 3 3 22 22 ILE HG21 H 1 0.887 0.022 . 1 . . . C 137 ILE HG21 . 18695 1 861 . 3 3 22 22 ILE HG22 H 1 0.887 0.022 . 1 . . . C 137 ILE HG22 . 18695 1 862 . 3 3 22 22 ILE HG23 H 1 0.887 0.022 . 1 . . . C 137 ILE HG23 . 18695 1 863 . 3 3 22 22 ILE HD11 H 1 1.106 0.013 . 1 . . . C 137 ILE HD11 . 18695 1 864 . 3 3 22 22 ILE HD12 H 1 1.106 0.013 . 1 . . . C 137 ILE HD12 . 18695 1 865 . 3 3 22 22 ILE HD13 H 1 1.106 0.013 . 1 . . . C 137 ILE HD13 . 18695 1 866 . 3 3 22 22 ILE CG2 C 13 18.190 0.065 . 1 . . . C 137 ILE CG2 . 18695 1 867 . 3 3 22 22 ILE CD1 C 13 15.066 0.028 . 1 . . . C 137 ILE CD1 . 18695 1 868 . 3 3 22 22 ILE N N 15 123.670 0.000 . 1 . . . C 137 ILE N . 18695 1 869 . 3 3 23 23 LEU H H 1 7.914 0.006 . 1 . . . C 138 LEU H . 18695 1 870 . 3 3 23 23 LEU HA H 1 3.656 0.022 . 1 . . . C 138 LEU HA . 18695 1 871 . 3 3 23 23 LEU HB2 H 1 1.900 0.025 . 1 . . . C 138 LEU HB2 . 18695 1 872 . 3 3 23 23 LEU HB3 H 1 1.900 0.025 . 1 . . . C 138 LEU HB3 . 18695 1 873 . 3 3 23 23 LEU HG H 1 1.544 0.000 . 1 . . . C 138 LEU HG . 18695 1 874 . 3 3 23 23 LEU HD11 H 1 0.642 0.007 . 2 . . . C 138 LEU HD11 . 18695 1 875 . 3 3 23 23 LEU HD12 H 1 0.642 0.007 . 2 . . . C 138 LEU HD12 . 18695 1 876 . 3 3 23 23 LEU HD13 H 1 0.642 0.007 . 2 . . . C 138 LEU HD13 . 18695 1 877 . 3 3 23 23 LEU HD21 H 1 0.529 0.002 . 2 . . . C 138 LEU HD21 . 18695 1 878 . 3 3 23 23 LEU HD22 H 1 0.529 0.002 . 2 . . . C 138 LEU HD22 . 18695 1 879 . 3 3 23 23 LEU HD23 H 1 0.529 0.002 . 2 . . . C 138 LEU HD23 . 18695 1 880 . 3 3 23 23 LEU C C 13 179.372 0.000 . 1 . . . C 138 LEU C . 18695 1 881 . 3 3 23 23 LEU CA C 13 58.167 0.009 . 1 . . . C 138 LEU CA . 18695 1 882 . 3 3 23 23 LEU CD1 C 13 25.576 0.033 . 2 . . . C 138 LEU CD1 . 18695 1 883 . 3 3 23 23 LEU CD2 C 13 23.372 0.029 . 2 . . . C 138 LEU CD2 . 18695 1 884 . 3 3 23 23 LEU N N 15 119.504 0.040 . 1 . . . C 138 LEU N . 18695 1 885 . 3 3 24 24 ASN H H 1 8.472 0.009 . 1 . . . C 139 ASN H . 18695 1 886 . 3 3 24 24 ASN HA H 1 4.296 0.021 . 1 . . . C 139 ASN HA . 18695 1 887 . 3 3 24 24 ASN HB2 H 1 2.785 0.025 . 1 . . . C 139 ASN HB2 . 18695 1 888 . 3 3 24 24 ASN HB3 H 1 2.785 0.025 . 1 . . . C 139 ASN HB3 . 18695 1 889 . 3 3 24 24 ASN HD21 H 1 7.592 0.010 . 1 . . . C 139 ASN HD21 . 18695 1 890 . 3 3 24 24 ASN HD22 H 1 6.883 0.024 . 1 . . . C 139 ASN HD22 . 18695 1 891 . 3 3 24 24 ASN C C 13 177.454 0.000 . 1 . . . C 139 ASN C . 18695 1 892 . 3 3 24 24 ASN CA C 13 56.102 0.000 . 1 . . . C 139 ASN CA . 18695 1 893 . 3 3 24 24 ASN N N 15 118.084 0.024 . 1 . . . C 139 ASN N . 18695 1 894 . 3 3 24 24 ASN ND2 N 15 112.088 0.032 . 1 . . . C 139 ASN ND2 . 18695 1 895 . 3 3 25 25 ASP H H 1 8.059 0.002 . 1 . . . C 140 ASP H . 18695 1 896 . 3 3 25 25 ASP HB2 H 1 2.819 0.000 . 1 . . . C 140 ASP HB2 . 18695 1 897 . 3 3 25 25 ASP HB3 H 1 2.819 0.000 . 1 . . . C 140 ASP HB3 . 18695 1 898 . 3 3 25 25 ASP C C 13 178.686 0.000 . 1 . . . C 140 ASP C . 18695 1 899 . 3 3 25 25 ASP CA C 13 57.094 0.000 . 1 . . . C 140 ASP CA . 18695 1 900 . 3 3 25 25 ASP N N 15 120.958 0.028 . 1 . . . C 140 ASP N . 18695 1 901 . 3 3 26 26 LEU H H 1 8.085 0.006 . 1 . . . C 141 LEU H . 18695 1 902 . 3 3 26 26 LEU HA H 1 3.945 0.010 . 1 . . . C 141 LEU HA . 18695 1 903 . 3 3 26 26 LEU HB2 H 1 1.952 0.032 . 2 . . . C 141 LEU HB2 . 18695 1 904 . 3 3 26 26 LEU HB3 H 1 1.954 0.031 . 2 . . . C 141 LEU HB3 . 18695 1 905 . 3 3 26 26 LEU HG H 1 1.399 0.007 . 1 . . . C 141 LEU HG . 18695 1 906 . 3 3 26 26 LEU HD11 H 1 0.738 0.016 . 2 . . . C 141 LEU HD11 . 18695 1 907 . 3 3 26 26 LEU HD12 H 1 0.738 0.016 . 2 . . . C 141 LEU HD12 . 18695 1 908 . 3 3 26 26 LEU HD13 H 1 0.738 0.016 . 2 . . . C 141 LEU HD13 . 18695 1 909 . 3 3 26 26 LEU HD21 H 1 0.681 0.014 . 2 . . . C 141 LEU HD21 . 18695 1 910 . 3 3 26 26 LEU HD22 H 1 0.681 0.014 . 2 . . . C 141 LEU HD22 . 18695 1 911 . 3 3 26 26 LEU HD23 H 1 0.681 0.014 . 2 . . . C 141 LEU HD23 . 18695 1 912 . 3 3 26 26 LEU C C 13 177.859 0.011 . 1 . . . C 141 LEU C . 18695 1 913 . 3 3 26 26 LEU CA C 13 57.677 0.026 . 1 . . . C 141 LEU CA . 18695 1 914 . 3 3 26 26 LEU CD1 C 13 26.407 0.032 . 2 . . . C 141 LEU CD1 . 18695 1 915 . 3 3 26 26 LEU CD2 C 13 22.860 0.020 . 2 . . . C 141 LEU CD2 . 18695 1 916 . 3 3 26 26 LEU N N 15 117.231 0.027 . 1 . . . C 141 LEU N . 18695 1 917 . 3 3 27 27 SER H H 1 7.597 0.004 . 1 . . . C 142 SER H . 18695 1 918 . 3 3 27 27 SER HA H 1 4.320 0.013 . 1 . . . C 142 SER HA . 18695 1 919 . 3 3 27 27 SER HB2 H 1 3.742 0.004 . 2 . . . C 142 SER HB2 . 18695 1 920 . 3 3 27 27 SER HB3 H 1 4.060 0.000 . 2 . . . C 142 SER HB3 . 18695 1 921 . 3 3 27 27 SER C C 13 174.685 0.000 . 1 . . . C 142 SER C . 18695 1 922 . 3 3 27 27 SER CA C 13 59.075 0.000 . 1 . . . C 142 SER CA . 18695 1 923 . 3 3 27 27 SER CB C 13 63.930 0.060 . 1 . . . C 142 SER CB . 18695 1 924 . 3 3 27 27 SER N N 15 109.816 0.031 . 1 . . . C 142 SER N . 18695 1 925 . 3 3 28 28 SER H H 1 7.613 0.007 . 1 . . . C 143 SER H . 18695 1 926 . 3 3 28 28 SER HA H 1 4.360 0.000 . 1 . . . C 143 SER HA . 18695 1 927 . 3 3 28 28 SER HB2 H 1 3.939 0.005 . 1 . . . C 143 SER HB2 . 18695 1 928 . 3 3 28 28 SER C C 13 174.283 0.016 . 1 . . . C 143 SER C . 18695 1 929 . 3 3 28 28 SER CA C 13 59.259 0.004 . 1 . . . C 143 SER CA . 18695 1 930 . 3 3 28 28 SER CB C 13 63.801 0.065 . 1 . . . C 143 SER CB . 18695 1 931 . 3 3 28 28 SER N N 15 117.276 0.018 . 1 . . . C 143 SER N . 18695 1 932 . 3 3 29 29 ASP H H 1 8.362 0.005 . 1 . . . C 144 ASP H . 18695 1 933 . 3 3 29 29 ASP HA H 1 4.651 0.019 . 1 . . . C 144 ASP HA . 18695 1 934 . 3 3 29 29 ASP HB2 H 1 2.692 0.003 . 1 . . . C 144 ASP HB2 . 18695 1 935 . 3 3 29 29 ASP HB3 H 1 2.692 0.003 . 1 . . . C 144 ASP HB3 . 18695 1 936 . 3 3 29 29 ASP C C 13 175.250 0.001 . 1 . . . C 144 ASP C . 18695 1 937 . 3 3 29 29 ASP CA C 13 54.119 0.012 . 1 . . . C 144 ASP CA . 18695 1 938 . 3 3 29 29 ASP CB C 13 41.092 0.065 . 1 . . . C 144 ASP CB . 18695 1 939 . 3 3 29 29 ASP N N 15 122.050 0.022 . 1 . . . C 144 ASP N . 18695 1 940 . 3 3 30 30 ALA H H 1 7.963 0.014 . 1 . . . C 145 ALA H . 18695 1 941 . 3 3 30 30 ALA HA H 1 4.380 0.016 . 1 . . . C 145 ALA HA . 18695 1 942 . 3 3 30 30 ALA HB1 H 1 1.309 0.013 . 1 . . . C 145 ALA HB1 . 18695 1 943 . 3 3 30 30 ALA HB2 H 1 1.309 0.013 . 1 . . . C 145 ALA HB2 . 18695 1 944 . 3 3 30 30 ALA HB3 H 1 1.309 0.013 . 1 . . . C 145 ALA HB3 . 18695 1 945 . 3 3 30 30 ALA C C 13 175.294 0.000 . 1 . . . C 145 ALA C . 18695 1 946 . 3 3 30 30 ALA CA C 13 50.559 0.000 . 1 . . . C 145 ALA CA . 18695 1 947 . 3 3 30 30 ALA CB C 13 18.385 0.024 . 1 . . . C 145 ALA CB . 18695 1 948 . 3 3 30 30 ALA N N 15 124.417 0.014 . 1 . . . C 145 ALA N . 18695 1 949 . 3 3 31 31 PRO HD2 H 1 3.602 0.014 . 1 . . . C 146 PRO HD2 . 18695 1 950 . 3 3 31 31 PRO HD3 H 1 3.602 0.014 . 1 . . . C 146 PRO HD3 . 18695 1 951 . 3 3 31 31 PRO C C 13 176.623 0.000 . 1 . . . C 146 PRO C . 18695 1 952 . 3 3 31 31 PRO CA C 13 63.334 0.000 . 1 . . . C 146 PRO CA . 18695 1 953 . 3 3 32 32 GLY H H 1 8.461 0.013 . 1 . . . C 147 GLY H . 18695 1 954 . 3 3 32 32 GLY HA2 H 1 3.967 0.004 . 2 . . . C 147 GLY HA2 . 18695 1 955 . 3 3 32 32 GLY HA3 H 1 3.831 0.020 . 2 . . . C 147 GLY HA3 . 18695 1 956 . 3 3 32 32 GLY C C 13 172.675 0.000 . 1 . . . C 147 GLY C . 18695 1 957 . 3 3 32 32 GLY CA C 13 45.269 0.076 . 1 . . . C 147 GLY CA . 18695 1 958 . 3 3 32 32 GLY N N 15 109.408 0.059 . 1 . . . C 147 GLY N . 18695 1 959 . 3 3 33 33 VAL H H 1 7.603 0.004 . 1 . . . C 148 VAL H . 18695 1 960 . 3 3 33 33 VAL HA H 1 4.396 0.010 . 1 . . . C 148 VAL HA . 18695 1 961 . 3 3 33 33 VAL HB H 1 1.969 0.006 . 1 . . . C 148 VAL HB . 18695 1 962 . 3 3 33 33 VAL HG11 H 1 0.855 0.019 . 2 . . . C 148 VAL HG11 . 18695 1 963 . 3 3 33 33 VAL HG12 H 1 0.855 0.019 . 2 . . . C 148 VAL HG12 . 18695 1 964 . 3 3 33 33 VAL HG13 H 1 0.855 0.019 . 2 . . . C 148 VAL HG13 . 18695 1 965 . 3 3 33 33 VAL HG21 H 1 0.840 0.008 . 2 . . . C 148 VAL HG21 . 18695 1 966 . 3 3 33 33 VAL HG22 H 1 0.840 0.008 . 2 . . . C 148 VAL HG22 . 18695 1 967 . 3 3 33 33 VAL HG23 H 1 0.840 0.008 . 2 . . . C 148 VAL HG23 . 18695 1 968 . 3 3 33 33 VAL C C 13 173.951 0.000 . 1 . . . C 148 VAL C . 18695 1 969 . 3 3 33 33 VAL CA C 13 58.898 0.000 . 1 . . . C 148 VAL CA . 18695 1 970 . 3 3 33 33 VAL CB C 13 34.446 0.051 . 1 . . . C 148 VAL CB . 18695 1 971 . 3 3 33 33 VAL CG1 C 13 21.226 0.111 . 2 . . . C 148 VAL CG1 . 18695 1 972 . 3 3 33 33 VAL CG2 C 13 20.045 0.078 . 2 . . . C 148 VAL CG2 . 18695 1 973 . 3 3 33 33 VAL N N 15 118.214 0.074 . 1 . . . C 148 VAL N . 18695 1 stop_ save_