data_5064 ####################### # Entry information # ####################### save_entry_information _Entry.Sf_category entry_information _Entry.Sf_framecode entry_information _Entry.ID 5064 _Entry.Title ; Backbone 1H, 13C, and 15N resonance assignments for a 14 kD protein, GABAA receptor associated protein (GABARAP) ; _Entry.Type macromolecule _Entry.Version_type original _Entry.Submission_date 2001-06-29 _Entry.Accession_date 2001-06-29 _Entry.Last_release_date 2001-11-06 _Entry.Original_release_date 2001-11-06 _Entry.Origination author _Entry.NMR_STAR_version 3.1.1.61 _Entry.Original_NMR_STAR_version 2.1 _Entry.Experimental_method NMR _Entry.Experimental_method_subtype . _Entry.Details . _Entry.BMRB_internal_directory_name . loop_ _Entry_author.Ordinal _Entry_author.Given_name _Entry_author.Family_name _Entry_author.First_initial _Entry_author.Middle_initials _Entry_author.Family_title _Entry_author.Entry_ID 1 Richard Harris . . . 5064 2 Mark McAlister . S.B. . 5064 3 Andrew Sankar . . . 5064 4 Stephen Moss . J. . 5064 5 Nicholas Keep . H. . 5064 6 Paul Driscoll . C. . 5064 stop_ loop_ _Data_set.Type _Data_set.Count _Data_set.Entry_ID assigned_chemical_shifts 1 5064 stop_ loop_ _Datum.Type _Datum.Count _Datum.Entry_ID '1H chemical shifts' 441 5064 '13C chemical shifts' 343 5064 '15N chemical shifts' 91 5064 stop_ loop_ _Release.Release_number _Release.Format_type _Release.Format_version _Release.Date _Release.Submission_date _Release.Type _Release.Author _Release.Detail _Release.Entry_ID 1 . . 2001-11-06 2001-06-28 original author . 5064 stop_ save_ ############### # Citations # ############### save_entry_citation _Citation.Sf_category citations _Citation.Sf_framecode entry_citation _Citation.Entry_ID 5064 _Citation.ID 1 _Citation.Class 'entry citation' _Citation.CAS_abstract_code . _Citation.MEDLINE_UI_code . _Citation.DOI . _Citation.PubMed_ID . _Citation.Full_citation . _Citation.Title ; Letter to the Editor: Backbone 1H, 13C, and 15N resonance assignments for a 14 kD protein, GABAA receptor associated protein (GABARAP) ; _Citation.Status published _Citation.Type journal _Citation.Journal_abbrev 'J. Biomol. NMR' _Citation.Journal_name_full . _Citation.Journal_volume 21 _Citation.Journal_issue 2 _Citation.Journal_ASTM . _Citation.Journal_ISSN . _Citation.Journal_CSD . _Citation.Book_title . _Citation.Book_chapter_title . _Citation.Book_volume . _Citation.Book_series . _Citation.Book_publisher . _Citation.Book_publisher_city . _Citation.Book_ISBN . _Citation.Conference_title . _Citation.Conference_site . _Citation.Conference_state_province . _Citation.Conference_country . _Citation.Conference_start_date . _Citation.Conference_end_date . _Citation.Conference_abstract_number . _Citation.Thesis_institution . _Citation.Thesis_institution_city . _Citation.Thesis_institution_country . _Citation.WWW_URL . _Citation.Page_first 185 _Citation.Page_last 186 _Citation.Year 2001 _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 Richard Harris . . . 5064 1 2 Mark McAlister . S.B. . 5064 1 3 Andrew Sankar . . . 5064 1 4 John Phelan . P. . 5064 1 5 Stephen Moss . J. . 5064 1 6 Nicholas Keep . H. . 5064 1 7 Paul Driscoll . C. . 5064 1 stop_ save_ ############################################# # Molecular system (assembly) description # ############################################# save_system_GABARAP _Assembly.Sf_category assembly _Assembly.Sf_framecode system_GABARAP _Assembly.Entry_ID 5064 _Assembly.ID 1 _Assembly.Name 'GABAA receptor associated protein' _Assembly.BMRB_code . _Assembly.Number_of_components . _Assembly.Organic_ligands . _Assembly.Metal_ions . _Assembly.Non_standard_bonds . _Assembly.Ambiguous_conformational_states . _Assembly.Ambiguous_chem_comp_sites . _Assembly.Molecules_in_chemical_exchange . _Assembly.Paramagnetic no _Assembly.Thiol_state 'not present' _Assembly.Molecular_mass . _Assembly.Enzyme_commission_number . _Assembly.Details ; Expressed construct contains an N-terminal hexahistidine purification tag: MGSSHHHHHHSSGLVPRGS before the initiating Met of GABARAP. ; _Assembly.DB_query_date . _Assembly.DB_query_revised_last_date . loop_ _Assembly_type.Type _Assembly_type.Entry_ID _Assembly_type.Assembly_ID monomer 5064 1 stop_ loop_ _Entity_assembly.ID _Entity_assembly.Entity_assembly_name _Entity_assembly.Entity_ID _Entity_assembly.Entity_label _Entity_assembly.Asym_ID _Entity_assembly.PDB_chain_ID _Entity_assembly.Experimental_data_reported _Entity_assembly.Physical_state _Entity_assembly.Conformational_isomer _Entity_assembly.Chemical_exchange_state _Entity_assembly.Magnetic_equivalence_group_code _Entity_assembly.Role _Entity_assembly.Details _Entity_assembly.Entry_ID _Entity_assembly.Assembly_ID 1 GABARAP 1 $GABARAP . . . native . . . . . 5064 1 stop_ loop_ _Assembly_db_link.Author_supplied _Assembly_db_link.Database_code _Assembly_db_link.Accession_code _Assembly_db_link.Entry_mol_code _Assembly_db_link.Entry_mol_name _Assembly_db_link.Entry_experimental_method _Assembly_db_link.Entry_structure_resolution _Assembly_db_link.Entry_relation_type _Assembly_db_link.Entry_details _Assembly_db_link.Entry_ID _Assembly_db_link.Assembly_ID . SWISS-PROT O95166 . . . . . . 5064 1 stop_ loop_ _Assembly_common_name.Name _Assembly_common_name.Type _Assembly_common_name.Entry_ID _Assembly_common_name.Assembly_ID 'GABAA receptor associated protein' system 5064 1 GABARAP abbreviation 5064 1 stop_ save_ #################################### # Biological polymers and ligands # #################################### save_GABARAP _Entity.Sf_category entity _Entity.Sf_framecode GABARAP _Entity.Entry_ID 5064 _Entity.ID 1 _Entity.BMRB_code . _Entity.Name 'GABA(A) receptor associated protein' _Entity.Type polymer _Entity.Polymer_common_type . _Entity.Polymer_type polypeptide(L) _Entity.Polymer_type_details . _Entity.Polymer_strand_ID . _Entity.Polymer_seq_one_letter_code_can . _Entity.Polymer_seq_one_letter_code ; MGSSHHHHHHSSGLVPRGSM KFVYKEEHPFEKRRSEGEKI RKKYPDRVPVIVEKAPKARI GDLDKKKYLVPSDLTVGQFY FLIRKRIHLRAEDALFFFVN NVIPPTSATMGQLYQEHHEE DFFLYIAYSDESVYGL ; _Entity.Target_identifier . _Entity.Polymer_author_defined_seq . _Entity.Polymer_author_seq_details . _Entity.Ambiguous_conformational_states . _Entity.Ambiguous_chem_comp_sites . _Entity.Nstd_monomer . _Entity.Nstd_chirality . _Entity.Nstd_linkage . _Entity.Nonpolymer_comp_ID . _Entity.Nonpolymer_comp_label . _Entity.Number_of_monomers 136 _Entity.Number_of_nonpolymer_components . _Entity.Paramagnetic . _Entity.Thiol_state 'not present' _Entity.Src_method . _Entity.Parent_entity_ID . _Entity.Fragment . _Entity.Mutation . _Entity.EC_number . _Entity.Calc_isoelectric_point . _Entity.Formula_weight 15998 _Entity.Formula_weight_exptl . _Entity.Formula_weight_exptl_meth . _Entity.Details . _Entity.DB_query_date . _Entity.DB_query_revised_last_date 2015-01-28 loop_ _Entity_db_link.Ordinal _Entity_db_link.Author_supplied _Entity_db_link.Database_code _Entity_db_link.Accession_code _Entity_db_link.Entry_mol_code _Entity_db_link.Entry_mol_name _Entity_db_link.Entry_experimental_method _Entity_db_link.Entry_structure_resolution _Entity_db_link.Entry_relation_type _Entity_db_link.Entry_details _Entity_db_link.Chimera_segment_ID _Entity_db_link.Seq_query_to_submitted_percent _Entity_db_link.Seq_subject_length _Entity_db_link.Seq_identity _Entity_db_link.Seq_positive _Entity_db_link.Seq_homology_expectation_val _Entity_db_link.Seq_align_begin _Entity_db_link.Seq_align_end _Entity_db_link.Seq_difference_details _Entity_db_link.Seq_alignment_details _Entity_db_link.Entry_ID _Entity_db_link.Entity_ID 1 no BMRB 5058 . GABARAP . . . . . 87.50 119 100.00 100.00 7.20e-80 . . . . 5064 1 2 no BMRB 5128 . GABARAP . . . . . 86.03 117 100.00 100.00 3.66e-78 . . . . 5064 1 3 no PDB 1GNU . "Gaba(a) Receptor Associated Protein Gabarap" . . . . . 86.03 117 100.00 100.00 3.66e-78 . . . . 5064 1 4 no PDB 1KJT . "Crystal Structure Of The Gaba(A) Receptor Associated Protein, Gabarap" . . . . . 87.50 119 99.16 99.16 4.08e-79 . . . . 5064 1 5 no PDB 1KLV . "Solution Structure And Backbone Dynamics Of Gabarap, Gabaa Receptor Associated Protein" . . . . . 86.03 117 100.00 100.00 3.66e-78 . . . . 5064 1 6 no PDB 1KM7 . "Solution Structure And Backbone Dynamics Of Gabarap, Gabaa Receptor Associated Protein" . . . . . 86.03 117 100.00 100.00 3.66e-78 . . . . 5064 1 7 no PDB 1KOT . "Solution Structure Of Human Gaba Receptor Associated Protein Gabarap" . . . . . 87.50 119 100.00 100.00 7.20e-80 . . . . 5064 1 8 no PDB 3D32 . "Complex Of Gaba(a) Receptor-associated Protein (gabarap) With A Synthetic Peptide" . . . . . 87.50 119 100.00 100.00 7.20e-80 . . . . 5064 1 9 no PDB 3DOW . "Complex Structure Of Gaba Type A Receptor Associated Protein And Its Binding Epitope On Calreticulin" . . . . . 87.50 119 100.00 100.00 7.20e-80 . . . . 5064 1 10 no PDB 3WIM . "Gabarap-lir Peptide Complex" . . . . . 86.03 117 100.00 100.00 3.66e-78 . . . . 5064 1 11 no DBJ BAB21549 . "MAP1 light chain 3 related protein [Homo sapiens]" . . . . . 86.03 117 100.00 100.00 3.66e-78 . . . . 5064 1 12 no DBJ BAB22426 . "unnamed protein product [Mus musculus]" . . . . . 86.03 117 99.15 100.00 1.46e-77 . . . . 5064 1 13 no DBJ BAB27806 . "unnamed protein product [Mus musculus]" . . . . . 86.03 117 100.00 100.00 3.66e-78 . . . . 5064 1 14 no DBJ BAG35138 . "unnamed protein product [Homo sapiens]" . . . . . 86.03 117 99.15 100.00 9.16e-78 . . . . 5064 1 15 no EMBL CAG00707 . "unnamed protein product, partial [Tetraodon nigroviridis]" . . . . . 85.29 116 98.28 98.28 2.64e-75 . . . . 5064 1 16 no EMBL CAG33324 . "GABARAP [Homo sapiens]" . . . . . 86.03 117 100.00 100.00 3.66e-78 . . . . 5064 1 17 no EMBL CAG47031 . "GABARAP [Homo sapiens]" . . . . . 86.03 117 100.00 100.00 3.66e-78 . . . . 5064 1 18 no EMBL CAP17839 . "GABAA receptor-associated protein 1 [Carassius carassius]" . . . . . 69.85 95 100.00 100.00 2.44e-61 . . . . 5064 1 19 no EMBL CDQ58630 . "unnamed protein product [Oncorhynchus mykiss]" . . . . . 85.29 122 98.28 99.14 3.53e-76 . . . . 5064 1 20 no GB AAD02337 . "MM46 [Homo sapiens]" . . . . . 86.03 117 100.00 100.00 3.66e-78 . . . . 5064 1 21 no GB AAD32455 . "ganglioside expression factor 2 homolog [Homo sapiens]" . . . . . 86.03 117 100.00 100.00 3.66e-78 . . . . 5064 1 22 no GB AAD47641 . "GABA-A receptor-associated protein [Homo sapiens]" . . . . . 86.03 117 100.00 100.00 3.66e-78 . . . . 5064 1 23 no GB AAD47642 . "GABA-A receptor-associated protein [Mus musculus]" . . . . . 86.03 117 100.00 100.00 3.66e-78 . . . . 5064 1 24 no GB AAD47643 . "GABA-A receptor-associated protein [Rattus norvegicus]" . . . . . 86.03 117 100.00 100.00 3.66e-78 . . . . 5064 1 25 no REF NP_001011192 . "GABA(A) receptor-associated protein like 1 [Xenopus (Silurana) tropicalis]" . . . . . 86.03 117 100.00 100.00 3.66e-78 . . . . 5064 1 26 no REF NP_001013278 . "GABA(A) receptor-associated protein [Danio rerio]" . . . . . 85.29 122 98.28 99.14 6.94e-76 . . . . 5064 1 27 no REF NP_001029220 . "gamma-aminobutyric acid receptor-associated protein [Bos taurus]" . . . . . 86.03 117 100.00 100.00 3.66e-78 . . . . 5064 1 28 no REF NP_001075611 . "gamma-aminobutyric acid receptor-associated protein [Oryctolagus cuniculus]" . . . . . 86.03 117 100.00 100.00 3.66e-78 . . . . 5064 1 29 no REF NP_001084530 . "uncharacterized protein LOC414477 [Xenopus laevis]" . . . . . 86.03 117 98.29 99.15 4.76e-77 . . . . 5064 1 30 no SP O95166 . "RecName: Full=Gamma-aminobutyric acid receptor-associated protein; AltName: Full=GABA(A) receptor-associated protein; AltName: " . . . . . 86.03 117 100.00 100.00 3.66e-78 . . . . 5064 1 31 no SP P60517 . "RecName: Full=Gamma-aminobutyric acid receptor-associated protein; AltName: Full=GABA(A) receptor-associated protein; Flags: Pr" . . . . . 86.03 117 100.00 100.00 3.66e-78 . . . . 5064 1 32 no SP Q8MK68 . "RecName: Full=Gamma-aminobutyric acid receptor-associated protein; AltName: Full=GABA(A) receptor-associated protein; Flags: Pr" . . . . . 86.03 117 100.00 100.00 3.66e-78 . . . . 5064 1 33 no SP Q9DCD6 . "RecName: Full=Gamma-aminobutyric acid receptor-associated protein; AltName: Full=GABA(A) receptor-associated protein; Flags: Pr" . . . . . 86.03 117 100.00 100.00 3.66e-78 . . . . 5064 1 34 no SP Q9GJW7 . "RecName: Full=Gamma-aminobutyric acid receptor-associated protein; AltName: Full=GABA(A) receptor-associated protein; Flags: Pr" . . . . . 86.03 117 100.00 100.00 3.66e-78 . . . . 5064 1 35 no TPG DAA18837 . "TPA: gamma-aminobutyric acid receptor-associated protein [Bos taurus]" . . . . . 86.03 117 100.00 100.00 3.66e-78 . . . . 5064 1 stop_ loop_ _Entity_common_name.Name _Entity_common_name.Type _Entity_common_name.Entry_ID _Entity_common_name.Entity_ID 'GABA(A) receptor associated protein' common 5064 1 GABARAP abbreviation 5064 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 -18 MET . 5064 1 2 -17 GLY . 5064 1 3 -16 SER . 5064 1 4 -15 SER . 5064 1 5 -14 HIS . 5064 1 6 -13 HIS . 5064 1 7 -12 HIS . 5064 1 8 -11 HIS . 5064 1 9 -10 HIS . 5064 1 10 -9 HIS . 5064 1 11 -8 SER . 5064 1 12 -7 SER . 5064 1 13 -6 GLY . 5064 1 14 -5 LEU . 5064 1 15 -4 VAL . 5064 1 16 -3 PRO . 5064 1 17 -2 ARG . 5064 1 18 -1 GLY . 5064 1 19 0 SER . 5064 1 20 1 MET . 5064 1 21 2 LYS . 5064 1 22 3 PHE . 5064 1 23 4 VAL . 5064 1 24 5 TYR . 5064 1 25 6 LYS . 5064 1 26 7 GLU . 5064 1 27 8 GLU . 5064 1 28 9 HIS . 5064 1 29 10 PRO . 5064 1 30 11 PHE . 5064 1 31 12 GLU . 5064 1 32 13 LYS . 5064 1 33 14 ARG . 5064 1 34 15 ARG . 5064 1 35 16 SER . 5064 1 36 17 GLU . 5064 1 37 18 GLY . 5064 1 38 19 GLU . 5064 1 39 20 LYS . 5064 1 40 21 ILE . 5064 1 41 22 ARG . 5064 1 42 23 LYS . 5064 1 43 24 LYS . 5064 1 44 25 TYR . 5064 1 45 26 PRO . 5064 1 46 27 ASP . 5064 1 47 28 ARG . 5064 1 48 29 VAL . 5064 1 49 30 PRO . 5064 1 50 31 VAL . 5064 1 51 32 ILE . 5064 1 52 33 VAL . 5064 1 53 34 GLU . 5064 1 54 35 LYS . 5064 1 55 36 ALA . 5064 1 56 37 PRO . 5064 1 57 38 LYS . 5064 1 58 39 ALA . 5064 1 59 40 ARG . 5064 1 60 41 ILE . 5064 1 61 42 GLY . 5064 1 62 43 ASP . 5064 1 63 44 LEU . 5064 1 64 45 ASP . 5064 1 65 46 LYS . 5064 1 66 47 LYS . 5064 1 67 48 LYS . 5064 1 68 49 TYR . 5064 1 69 50 LEU . 5064 1 70 51 VAL . 5064 1 71 52 PRO . 5064 1 72 53 SER . 5064 1 73 54 ASP . 5064 1 74 55 LEU . 5064 1 75 56 THR . 5064 1 76 57 VAL . 5064 1 77 58 GLY . 5064 1 78 59 GLN . 5064 1 79 60 PHE . 5064 1 80 61 TYR . 5064 1 81 62 PHE . 5064 1 82 63 LEU . 5064 1 83 64 ILE . 5064 1 84 65 ARG . 5064 1 85 66 LYS . 5064 1 86 67 ARG . 5064 1 87 68 ILE . 5064 1 88 69 HIS . 5064 1 89 70 LEU . 5064 1 90 71 ARG . 5064 1 91 72 ALA . 5064 1 92 73 GLU . 5064 1 93 74 ASP . 5064 1 94 75 ALA . 5064 1 95 76 LEU . 5064 1 96 77 PHE . 5064 1 97 78 PHE . 5064 1 98 79 PHE . 5064 1 99 80 VAL . 5064 1 100 81 ASN . 5064 1 101 82 ASN . 5064 1 102 83 VAL . 5064 1 103 84 ILE . 5064 1 104 85 PRO . 5064 1 105 86 PRO . 5064 1 106 87 THR . 5064 1 107 88 SER . 5064 1 108 89 ALA . 5064 1 109 90 THR . 5064 1 110 91 MET . 5064 1 111 92 GLY . 5064 1 112 93 GLN . 5064 1 113 94 LEU . 5064 1 114 95 TYR . 5064 1 115 96 GLN . 5064 1 116 97 GLU . 5064 1 117 98 HIS . 5064 1 118 99 HIS . 5064 1 119 100 GLU . 5064 1 120 101 GLU . 5064 1 121 102 ASP . 5064 1 122 103 PHE . 5064 1 123 104 PHE . 5064 1 124 105 LEU . 5064 1 125 106 TYR . 5064 1 126 107 ILE . 5064 1 127 108 ALA . 5064 1 128 109 TYR . 5064 1 129 110 SER . 5064 1 130 111 ASP . 5064 1 131 112 GLU . 5064 1 132 113 SER . 5064 1 133 114 VAL . 5064 1 134 115 TYR . 5064 1 135 116 GLY . 5064 1 136 117 LEU . 5064 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 . MET 1 1 5064 1 . GLY 2 2 5064 1 . SER 3 3 5064 1 . SER 4 4 5064 1 . HIS 5 5 5064 1 . HIS 6 6 5064 1 . HIS 7 7 5064 1 . HIS 8 8 5064 1 . HIS 9 9 5064 1 . HIS 10 10 5064 1 . SER 11 11 5064 1 . SER 12 12 5064 1 . GLY 13 13 5064 1 . LEU 14 14 5064 1 . VAL 15 15 5064 1 . PRO 16 16 5064 1 . ARG 17 17 5064 1 . GLY 18 18 5064 1 . SER 19 19 5064 1 . MET 20 20 5064 1 . LYS 21 21 5064 1 . PHE 22 22 5064 1 . VAL 23 23 5064 1 . TYR 24 24 5064 1 . LYS 25 25 5064 1 . GLU 26 26 5064 1 . GLU 27 27 5064 1 . HIS 28 28 5064 1 . PRO 29 29 5064 1 . PHE 30 30 5064 1 . GLU 31 31 5064 1 . LYS 32 32 5064 1 . ARG 33 33 5064 1 . ARG 34 34 5064 1 . SER 35 35 5064 1 . GLU 36 36 5064 1 . GLY 37 37 5064 1 . GLU 38 38 5064 1 . LYS 39 39 5064 1 . ILE 40 40 5064 1 . ARG 41 41 5064 1 . LYS 42 42 5064 1 . LYS 43 43 5064 1 . TYR 44 44 5064 1 . PRO 45 45 5064 1 . ASP 46 46 5064 1 . ARG 47 47 5064 1 . VAL 48 48 5064 1 . PRO 49 49 5064 1 . VAL 50 50 5064 1 . ILE 51 51 5064 1 . VAL 52 52 5064 1 . GLU 53 53 5064 1 . LYS 54 54 5064 1 . ALA 55 55 5064 1 . PRO 56 56 5064 1 . LYS 57 57 5064 1 . ALA 58 58 5064 1 . ARG 59 59 5064 1 . ILE 60 60 5064 1 . GLY 61 61 5064 1 . ASP 62 62 5064 1 . LEU 63 63 5064 1 . ASP 64 64 5064 1 . LYS 65 65 5064 1 . LYS 66 66 5064 1 . LYS 67 67 5064 1 . TYR 68 68 5064 1 . LEU 69 69 5064 1 . VAL 70 70 5064 1 . PRO 71 71 5064 1 . SER 72 72 5064 1 . ASP 73 73 5064 1 . LEU 74 74 5064 1 . THR 75 75 5064 1 . VAL 76 76 5064 1 . GLY 77 77 5064 1 . GLN 78 78 5064 1 . PHE 79 79 5064 1 . TYR 80 80 5064 1 . PHE 81 81 5064 1 . LEU 82 82 5064 1 . ILE 83 83 5064 1 . ARG 84 84 5064 1 . LYS 85 85 5064 1 . ARG 86 86 5064 1 . ILE 87 87 5064 1 . HIS 88 88 5064 1 . LEU 89 89 5064 1 . ARG 90 90 5064 1 . ALA 91 91 5064 1 . GLU 92 92 5064 1 . ASP 93 93 5064 1 . ALA 94 94 5064 1 . LEU 95 95 5064 1 . PHE 96 96 5064 1 . PHE 97 97 5064 1 . PHE 98 98 5064 1 . VAL 99 99 5064 1 . ASN 100 100 5064 1 . ASN 101 101 5064 1 . VAL 102 102 5064 1 . ILE 103 103 5064 1 . PRO 104 104 5064 1 . PRO 105 105 5064 1 . THR 106 106 5064 1 . SER 107 107 5064 1 . ALA 108 108 5064 1 . THR 109 109 5064 1 . MET 110 110 5064 1 . GLY 111 111 5064 1 . GLN 112 112 5064 1 . LEU 113 113 5064 1 . TYR 114 114 5064 1 . GLN 115 115 5064 1 . GLU 116 116 5064 1 . HIS 117 117 5064 1 . HIS 118 118 5064 1 . GLU 119 119 5064 1 . GLU 120 120 5064 1 . ASP 121 121 5064 1 . PHE 122 122 5064 1 . PHE 123 123 5064 1 . LEU 124 124 5064 1 . TYR 125 125 5064 1 . ILE 126 126 5064 1 . ALA 127 127 5064 1 . TYR 128 128 5064 1 . SER 129 129 5064 1 . ASP 130 130 5064 1 . GLU 131 131 5064 1 . SER 132 132 5064 1 . VAL 133 133 5064 1 . TYR 134 134 5064 1 . GLY 135 135 5064 1 . LEU 136 136 5064 1 stop_ save_ #################### # Natural source # #################### save_natural_source _Entity_natural_src_list.Sf_category natural_source _Entity_natural_src_list.Sf_framecode natural_source _Entity_natural_src_list.Entry_ID 5064 _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 $GABARAP . 9606 . . 'Homo sapiens' Human . . Eukaryota Metazoa Homo sapiens . . . . . . . . . . . . . . . . . . . . . 5064 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 5064 _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 $GABARAP . 'recombinant technology' 'Escherichia coli' 'E. coli' . . Escherichia coli BL21 DE3 . . . . . . . . . . . plasmid . . pET . . . . . . 5064 1 stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_Sample_1 _Sample.Sf_category sample _Sample.Sf_framecode Sample_1 _Sample.Entry_ID 5064 _Sample.ID 1 _Sample.Type solution _Sample.Sub_type . _Sample.Details . _Sample.Aggregate_sample_number . _Sample.Solvent_system . _Sample.Preparation_date . _Sample.Preparation_expiration_date . _Sample.Polycrystallization_protocol . _Sample.Single_crystal_protocol . _Sample.Crystal_grow_apparatus . _Sample.Crystal_grow_atmosphere . _Sample.Crystal_grow_details . _Sample.Crystal_grow_method . _Sample.Crystal_grow_method_cit_ID . _Sample.Crystal_grow_pH . _Sample.Crystal_grow_pH_range . _Sample.Crystal_grow_pressure . _Sample.Crystal_grow_pressure_esd . _Sample.Crystal_grow_seeding . _Sample.Crystal_grow_seeding_cit_ID . _Sample.Crystal_grow_temp . _Sample.Crystal_grow_temp_details . _Sample.Crystal_grow_temp_esd . _Sample.Crystal_grow_time . _Sample.Oriented_sample_prep_protocol . _Sample.Lyophilization_cryo_protectant . _Sample.Storage_protocol . loop_ _Sample_component.ID _Sample_component.Mol_common_name _Sample_component.Isotopic_labeling _Sample_component.Assembly_ID _Sample_component.Assembly_label _Sample_component.Entity_ID _Sample_component.Entity_label _Sample_component.Product_ID _Sample_component.Type _Sample_component.Concentration_val _Sample_component.Concentration_val_min _Sample_component.Concentration_val_max _Sample_component.Concentration_val_units _Sample_component.Concentration_val_err _Sample_component.Vendor _Sample_component.Vendor_product_name _Sample_component.Vendor_product_code _Sample_component.Entry_ID _Sample_component.Sample_ID 1 'GABA(A) receptor associated protein' '[U-13C; U-15N]' . . 1 $GABARAP . . . 0.5 1.0 mM . . . . 5064 1 stop_ save_ ####################### # Sample conditions # ####################### save_sample_conditions _Sample_condition_list.Sf_category sample_conditions _Sample_condition_list.Sf_framecode sample_conditions _Sample_condition_list.Entry_ID 5064 _Sample_condition_list.ID 1 _Sample_condition_list.Details . loop_ _Sample_condition_variable.Type _Sample_condition_variable.Val _Sample_condition_variable.Val_err _Sample_condition_variable.Val_units _Sample_condition_variable.Entry_ID _Sample_condition_variable.Sample_condition_list_ID pH 7.0 0.2 n/a 5064 1 temperature 293 0.2 K 5064 1 stop_ save_ ############################ # Computer software used # ############################ save_nmrPIPE _Software.Sf_category software _Software.Sf_framecode nmrPIPE _Software.Entry_ID 5064 _Software.ID 1 _Software.Name nmrPIPE _Software.Version . _Software.Details ; Delaglio et al. Journal of Biomolecular NMR (1995) 6, 277-293. ; loop_ _Task.Task _Task.Entry_ID _Task.Software_ID 'data processing' 5064 1 stop_ save_ save_ANSIG _Software.Sf_category software _Software.Sf_framecode ANSIG _Software.Entry_ID 5064 _Software.ID 2 _Software.Name ANSIG _Software.Version v3.3 _Software.Details ; Kraulis et al. Biochemistry (1994) 33, 3315-3531. ; loop_ _Task.Task _Task.Entry_ID _Task.Software_ID 'spectral analysis' 5064 2 stop_ save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer_1 _NMR_spectrometer.Sf_category NMR_spectrometer _NMR_spectrometer.Sf_framecode NMR_spectrometer_1 _NMR_spectrometer.Entry_ID 5064 _NMR_spectrometer.ID 1 _NMR_spectrometer.Details . _NMR_spectrometer.Manufacturer Varian _NMR_spectrometer.Model UNITYplus _NMR_spectrometer.Serial_number . _NMR_spectrometer.Field_strength 500 save_ save_NMR_spectrometer_2 _NMR_spectrometer.Sf_category NMR_spectrometer _NMR_spectrometer.Sf_framecode NMR_spectrometer_2 _NMR_spectrometer.Entry_ID 5064 _NMR_spectrometer.ID 2 _NMR_spectrometer.Details . _NMR_spectrometer.Manufacturer Varian _NMR_spectrometer.Model UNITYplus _NMR_spectrometer.Serial_number . _NMR_spectrometer.Field_strength 600 save_ save_spectrometer_list _NMR_spectrometer_list.Sf_category NMR_spectrometer_list _NMR_spectrometer_list.Sf_framecode spectrometer_list _NMR_spectrometer_list.Entry_ID 5064 _NMR_spectrometer_list.ID 1 loop_ _NMR_spectrometer_view.ID _NMR_spectrometer_view.Name _NMR_spectrometer_view.Manufacturer _NMR_spectrometer_view.Model _NMR_spectrometer_view.Serial_number _NMR_spectrometer_view.Field_strength _NMR_spectrometer_view.Details _NMR_spectrometer_view.Citation_ID _NMR_spectrometer_view.Citation_label _NMR_spectrometer_view.Entry_ID _NMR_spectrometer_view.NMR_spectrometer_list_ID 1 NMR_spectrometer_1 Varian UNITYplus . 500 . . . 5064 1 2 NMR_spectrometer_2 Varian UNITYplus . 600 . . . 5064 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 5064 _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 '1H-15N HSQC' . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 5064 1 2 '1H-15N NOESY' . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 5064 1 3 '1H-15N TOCSY' . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 5064 1 4 '1H-13C HCCH-TOCSY' . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 5064 1 5 HNCO . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 5064 1 6 HNCA . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 5064 1 7 HN(CO)CA . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 5064 1 8 HNCACB . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 5064 1 9 CBCA(CO)NH . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 5064 1 stop_ save_ save_NMR_spec_expt__0_1 _NMR_spec_expt.Sf_category NMR_spectrometer_expt _NMR_spec_expt.Sf_framecode NMR_spec_expt__0_1 _NMR_spec_expt.Entry_ID 5064 _NMR_spec_expt.ID 1 _NMR_spec_expt.Name '1H-15N HSQC' _NMR_spec_expt.Type . _NMR_spec_expt.Sample_volume . _NMR_spec_expt.Sample_volume_units . _NMR_spec_expt.NMR_tube_type . _NMR_spec_expt.Sample_spinning_rate . _NMR_spec_expt.Sample_angle . _NMR_spec_expt.NMR_spectrometer_ID . _NMR_spec_expt.NMR_spectrometer_label . _NMR_spec_expt.NMR_spectrometer_probe_ID . _NMR_spec_expt.NMR_spectrometer_probe_label . _NMR_spec_expt.Carrier_freq_switch_time . _NMR_spec_expt.Software_ID . _NMR_spec_expt.Software_label . _NMR_spec_expt.Method_ID . _NMR_spec_expt.Method_label . _NMR_spec_expt.Pulse_seq_accession_BMRB_code . _NMR_spec_expt.Details . save_ save_NMR_spec_expt__0_2 _NMR_spec_expt.Sf_category NMR_spectrometer_expt _NMR_spec_expt.Sf_framecode NMR_spec_expt__0_2 _NMR_spec_expt.Entry_ID 5064 _NMR_spec_expt.ID 2 _NMR_spec_expt.Name '1H-15N NOESY' _NMR_spec_expt.Type . _NMR_spec_expt.Sample_volume . _NMR_spec_expt.Sample_volume_units . _NMR_spec_expt.NMR_tube_type . _NMR_spec_expt.Sample_spinning_rate . _NMR_spec_expt.Sample_angle . _NMR_spec_expt.NMR_spectrometer_ID . _NMR_spec_expt.NMR_spectrometer_label . _NMR_spec_expt.NMR_spectrometer_probe_ID . _NMR_spec_expt.NMR_spectrometer_probe_label . _NMR_spec_expt.Carrier_freq_switch_time . _NMR_spec_expt.Software_ID . _NMR_spec_expt.Software_label . _NMR_spec_expt.Method_ID . _NMR_spec_expt.Method_label . _NMR_spec_expt.Pulse_seq_accession_BMRB_code . _NMR_spec_expt.Details . save_ save_NMR_spec_expt__0_3 _NMR_spec_expt.Sf_category NMR_spectrometer_expt _NMR_spec_expt.Sf_framecode NMR_spec_expt__0_3 _NMR_spec_expt.Entry_ID 5064 _NMR_spec_expt.ID 3 _NMR_spec_expt.Name '1H-15N TOCSY' _NMR_spec_expt.Type . _NMR_spec_expt.Sample_volume . _NMR_spec_expt.Sample_volume_units . _NMR_spec_expt.NMR_tube_type . _NMR_spec_expt.Sample_spinning_rate . _NMR_spec_expt.Sample_angle . _NMR_spec_expt.NMR_spectrometer_ID . _NMR_spec_expt.NMR_spectrometer_label . _NMR_spec_expt.NMR_spectrometer_probe_ID . _NMR_spec_expt.NMR_spectrometer_probe_label . _NMR_spec_expt.Carrier_freq_switch_time . _NMR_spec_expt.Software_ID . _NMR_spec_expt.Software_label . _NMR_spec_expt.Method_ID . _NMR_spec_expt.Method_label . _NMR_spec_expt.Pulse_seq_accession_BMRB_code . _NMR_spec_expt.Details . save_ save_NMR_spec_expt__0_4 _NMR_spec_expt.Sf_category NMR_spectrometer_expt _NMR_spec_expt.Sf_framecode NMR_spec_expt__0_4 _NMR_spec_expt.Entry_ID 5064 _NMR_spec_expt.ID 4 _NMR_spec_expt.Name '1H-13C HCCH-TOCSY' _NMR_spec_expt.Type . _NMR_spec_expt.Sample_volume . _NMR_spec_expt.Sample_volume_units . _NMR_spec_expt.NMR_tube_type . _NMR_spec_expt.Sample_spinning_rate . _NMR_spec_expt.Sample_angle . _NMR_spec_expt.NMR_spectrometer_ID . _NMR_spec_expt.NMR_spectrometer_label . _NMR_spec_expt.NMR_spectrometer_probe_ID . _NMR_spec_expt.NMR_spectrometer_probe_label . _NMR_spec_expt.Carrier_freq_switch_time . _NMR_spec_expt.Software_ID . _NMR_spec_expt.Software_label . _NMR_spec_expt.Method_ID . _NMR_spec_expt.Method_label . _NMR_spec_expt.Pulse_seq_accession_BMRB_code . _NMR_spec_expt.Details . save_ save_NMR_spec_expt__0_5 _NMR_spec_expt.Sf_category NMR_spectrometer_expt _NMR_spec_expt.Sf_framecode NMR_spec_expt__0_5 _NMR_spec_expt.Entry_ID 5064 _NMR_spec_expt.ID 5 _NMR_spec_expt.Name HNCO _NMR_spec_expt.Type . _NMR_spec_expt.Sample_volume . _NMR_spec_expt.Sample_volume_units . _NMR_spec_expt.NMR_tube_type . _NMR_spec_expt.Sample_spinning_rate . _NMR_spec_expt.Sample_angle . _NMR_spec_expt.NMR_spectrometer_ID . _NMR_spec_expt.NMR_spectrometer_label . _NMR_spec_expt.NMR_spectrometer_probe_ID . _NMR_spec_expt.NMR_spectrometer_probe_label . _NMR_spec_expt.Carrier_freq_switch_time . _NMR_spec_expt.Software_ID . _NMR_spec_expt.Software_label . _NMR_spec_expt.Method_ID . _NMR_spec_expt.Method_label . _NMR_spec_expt.Pulse_seq_accession_BMRB_code . _NMR_spec_expt.Details . save_ save_NMR_spec_expt__0_6 _NMR_spec_expt.Sf_category NMR_spectrometer_expt _NMR_spec_expt.Sf_framecode NMR_spec_expt__0_6 _NMR_spec_expt.Entry_ID 5064 _NMR_spec_expt.ID 6 _NMR_spec_expt.Name HNCA _NMR_spec_expt.Type . _NMR_spec_expt.Sample_volume . _NMR_spec_expt.Sample_volume_units . _NMR_spec_expt.NMR_tube_type . _NMR_spec_expt.Sample_spinning_rate . _NMR_spec_expt.Sample_angle . _NMR_spec_expt.NMR_spectrometer_ID . _NMR_spec_expt.NMR_spectrometer_label . _NMR_spec_expt.NMR_spectrometer_probe_ID . _NMR_spec_expt.NMR_spectrometer_probe_label . _NMR_spec_expt.Carrier_freq_switch_time . _NMR_spec_expt.Software_ID . _NMR_spec_expt.Software_label . _NMR_spec_expt.Method_ID . _NMR_spec_expt.Method_label . _NMR_spec_expt.Pulse_seq_accession_BMRB_code . _NMR_spec_expt.Details . save_ save_NMR_spec_expt__0_7 _NMR_spec_expt.Sf_category NMR_spectrometer_expt _NMR_spec_expt.Sf_framecode NMR_spec_expt__0_7 _NMR_spec_expt.Entry_ID 5064 _NMR_spec_expt.ID 7 _NMR_spec_expt.Name HN(CO)CA _NMR_spec_expt.Type . _NMR_spec_expt.Sample_volume . _NMR_spec_expt.Sample_volume_units . _NMR_spec_expt.NMR_tube_type . _NMR_spec_expt.Sample_spinning_rate . _NMR_spec_expt.Sample_angle . _NMR_spec_expt.NMR_spectrometer_ID . _NMR_spec_expt.NMR_spectrometer_label . _NMR_spec_expt.NMR_spectrometer_probe_ID . _NMR_spec_expt.NMR_spectrometer_probe_label . _NMR_spec_expt.Carrier_freq_switch_time . _NMR_spec_expt.Software_ID . _NMR_spec_expt.Software_label . _NMR_spec_expt.Method_ID . _NMR_spec_expt.Method_label . _NMR_spec_expt.Pulse_seq_accession_BMRB_code . _NMR_spec_expt.Details . save_ save_NMR_spec_expt__0_8 _NMR_spec_expt.Sf_category NMR_spectrometer_expt _NMR_spec_expt.Sf_framecode NMR_spec_expt__0_8 _NMR_spec_expt.Entry_ID 5064 _NMR_spec_expt.ID 8 _NMR_spec_expt.Name HNCACB _NMR_spec_expt.Type . _NMR_spec_expt.Sample_volume . _NMR_spec_expt.Sample_volume_units . _NMR_spec_expt.NMR_tube_type . _NMR_spec_expt.Sample_spinning_rate . _NMR_spec_expt.Sample_angle . _NMR_spec_expt.NMR_spectrometer_ID . _NMR_spec_expt.NMR_spectrometer_label . _NMR_spec_expt.NMR_spectrometer_probe_ID . _NMR_spec_expt.NMR_spectrometer_probe_label . _NMR_spec_expt.Carrier_freq_switch_time . _NMR_spec_expt.Software_ID . _NMR_spec_expt.Software_label . _NMR_spec_expt.Method_ID . _NMR_spec_expt.Method_label . _NMR_spec_expt.Pulse_seq_accession_BMRB_code . _NMR_spec_expt.Details . save_ save_NMR_spec_expt__0_9 _NMR_spec_expt.Sf_category NMR_spectrometer_expt _NMR_spec_expt.Sf_framecode NMR_spec_expt__0_9 _NMR_spec_expt.Entry_ID 5064 _NMR_spec_expt.ID 9 _NMR_spec_expt.Name CBCA(CO)NH _NMR_spec_expt.Type . _NMR_spec_expt.Sample_volume . _NMR_spec_expt.Sample_volume_units . _NMR_spec_expt.NMR_tube_type . _NMR_spec_expt.Sample_spinning_rate . _NMR_spec_expt.Sample_angle . _NMR_spec_expt.NMR_spectrometer_ID . _NMR_spec_expt.NMR_spectrometer_label . _NMR_spec_expt.NMR_spectrometer_probe_ID . _NMR_spec_expt.NMR_spectrometer_probe_label . _NMR_spec_expt.Carrier_freq_switch_time . _NMR_spec_expt.Software_ID . _NMR_spec_expt.Software_label . _NMR_spec_expt.Method_ID . _NMR_spec_expt.Method_label . _NMR_spec_expt.Pulse_seq_accession_BMRB_code . _NMR_spec_expt.Details . save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference _Chem_shift_reference.Sf_category chem_shift_reference _Chem_shift_reference.Sf_framecode chemical_shift_reference _Chem_shift_reference.Entry_ID 5064 _Chem_shift_reference.ID 1 _Chem_shift_reference.Details . loop_ _Chem_shift_ref.Atom_type _Chem_shift_ref.Atom_isotope_number _Chem_shift_ref.Mol_common_name _Chem_shift_ref.Atom_group _Chem_shift_ref.Concentration_val _Chem_shift_ref.Concentration_units _Chem_shift_ref.Solvent _Chem_shift_ref.Rank _Chem_shift_ref.Chem_shift_units _Chem_shift_ref.Chem_shift_val _Chem_shift_ref.Ref_method _Chem_shift_ref.Ref_type _Chem_shift_ref.Indirect_shift_ratio _Chem_shift_ref.External_ref_loc _Chem_shift_ref.External_ref_sample_geometry _Chem_shift_ref.External_ref_axis _Chem_shift_ref.Indirect_shift_ratio_cit_ID _Chem_shift_ref.Indirect_shift_ratio_cit_label _Chem_shift_ref.Ref_correction_type _Chem_shift_ref.Correction_val _Chem_shift_ref.Correction_val_cit_ID _Chem_shift_ref.Correction_val_cit_label _Chem_shift_ref.Entry_ID _Chem_shift_ref.Chem_shift_reference_ID H 1 DSS 'methyl protons' . . . . ppm 0.0 internal direct 1.0 . . . . . . . . . 5064 1 N 15 DSS 'methyl protons' . . . . ppm 0.0 . indirect 0.101329118 . . . . . . . . . 5064 1 C 13 DSS 'methyl protons' . . . . ppm 0.0 . indirect 0.251449530 . . . . . . . . . 5064 1 stop_ save_ ################################### # Assigned chemical shift lists # ################################### ################################################################### # Chemical Shift Ambiguity Index Value Definitions # # # # The values other than 1 are used for those atoms with different # # chemical shifts that cannot be assigned to stereospecific atoms # # or to specific residues or chains. # # # # Index Value Definition # # # # 1 Unique (including isolated methyl protons, # # geminal atoms, and geminal methyl # # groups with identical chemical shifts) # # (e.g. ILE HD11, HD12, HD13 protons) # # 2 Ambiguity of geminal atoms or geminal methyl # # proton groups (e.g. ASP HB2 and HB3 # # protons, LEU CD1 and CD2 carbons, or # # LEU HD11, HD12, HD13 and HD21, HD22, # # HD23 methyl protons) # # 3 Aromatic atoms on opposite sides of # # symmetrical rings (e.g. TYR HE1 and HE2 # # protons) # # 4 Intraresidue ambiguities (e.g. LYS HG and # # HD protons or TRP HZ2 and HZ3 protons) # # 5 Interresidue ambiguities (LYS 12 vs. LYS 27) # # 6 Intermolecular ambiguities (e.g. ASP 31 CA # # in monomer 1 and ASP 31 CA in monomer 2 # # of an asymmetrical homodimer, duplex # # DNA assignments, or other assignments # # that may apply to atoms in one or more # # molecule in the molecular assembly) # # 9 Ambiguous, specific ambiguity not defined # # # ################################################################### save_shift_set_1 _Assigned_chem_shift_list.Sf_category assigned_chemical_shifts _Assigned_chem_shift_list.Sf_framecode shift_set_1 _Assigned_chem_shift_list.Entry_ID 5064 _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 _Assigned_chem_shift_list.Chem_shift_reference_ID 1 _Assigned_chem_shift_list.Chem_shift_reference_label $chemical_shift_reference _Assigned_chem_shift_list.Chem_shift_1H_err . _Assigned_chem_shift_list.Chem_shift_13C_err . _Assigned_chem_shift_list.Chem_shift_15N_err . _Assigned_chem_shift_list.Chem_shift_31P_err . _Assigned_chem_shift_list.Chem_shift_2H_err . _Assigned_chem_shift_list.Chem_shift_19F_err . _Assigned_chem_shift_list.Error_derivation_method . _Assigned_chem_shift_list.Details ; Analysis of the triple resonance experiments allowed identification and sequential assignments for 91 out of the 110 GABARAP (117 less 7 prolines) backbone 15N and amide proton resonances (i.e. not including the hexahistidine tag). Definitive assignments have not been obtained for residues Met1-His9, Phe11-Arg15, Arg22, Lys47, Glu100, Phe103, and Phe104). Conformational slow exchange is observed as NH cross peak doubling for residues Glu17, Glu19, Lys20 and Leu105. Nine backbone NH cross-peaks in the HSQC spectrum, including two that display evidence of slow conformational exchange, remain unassigned to specific residues. The absence of an unambiguously identifiable NH crosspeak for 10 residues is tentatively attributed to exchange broadening. Examination of the spectrum under a variety of sample conditions (temperature, pH, peptide ligands, co-solvents) has failed to reveal these ?missing peaks?. Similar characteristics are obtained for a de-tagged variant of GABARAP and GABARAP expressed in the absence of a hexahistidine tag." ; _Assigned_chem_shift_list.Text_data_format . _Assigned_chem_shift_list.Text_data . loop_ _Chem_shift_experiment.Experiment_ID _Chem_shift_experiment.Experiment_name _Chem_shift_experiment.Sample_ID _Chem_shift_experiment.Sample_label _Chem_shift_experiment.Sample_state _Chem_shift_experiment.Entry_ID _Chem_shift_experiment.Assigned_chem_shift_list_ID . . 1 $Sample_1 . 5064 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 34 34 ARG CA C 13 58.265 0.05 . 1 . . . . . . . . 5064 1 2 . 1 1 34 34 ARG C C 13 178.7 0.05 . 1 . . . . . . . . 5064 1 3 . 1 1 34 34 ARG CB C 13 29.482 0.05 . 1 . . . . . . . . 5064 1 4 . 1 1 35 35 SER N N 15 112.389 0.05 . 1 . . . . . . . . 5064 1 5 . 1 1 35 35 SER H H 1 7.628 0.005 . 1 . . . . . . . . 5064 1 6 . 1 1 35 35 SER CA C 13 61.423 0.05 . 1 . . . . . . . . 5064 1 7 . 1 1 35 35 SER HA H 1 4.267 0.005 . 1 . . . . . . . . 5064 1 8 . 1 1 35 35 SER C C 13 177.758 0.05 . 1 . . . . . . . . 5064 1 9 . 1 1 35 35 SER CB C 13 62.864 0.05 . 1 . . . . . . . . 5064 1 10 . 1 1 35 35 SER HB2 H 1 4.017 0.005 . 2 . . . . . . . . 5064 1 11 . 1 1 36 36 GLU N N 15 121.794 0.05 . 1 . . . . . . . . 5064 1 12 . 1 1 36 36 GLU H H 1 7.77 0.005 . 1 . . . . . . . . 5064 1 13 . 1 1 36 36 GLU CA C 13 59.453 0.05 . 1 . . . . . . . . 5064 1 14 . 1 1 36 36 GLU HA H 1 4.108 0.005 . 1 . . . . . . . . 5064 1 15 . 1 1 36 36 GLU C C 13 179.514 0.05 . 1 . . . . . . . . 5064 1 16 . 1 1 36 36 GLU CB C 13 29.457 0.05 . 1 . . . . . . . . 5064 1 17 . 1 1 37 37 GLY N N 15 109.928 0.05 . 1 . . . . . . . . 5064 1 18 . 1 1 37 37 GLY H H 1 9.551 0.005 . 1 . . . . . . . . 5064 1 19 . 1 1 37 37 GLY CA C 13 47.365 0.05 . 1 . . . . . . . . 5064 1 20 . 1 1 37 37 GLY HA2 H 1 3.082 0.005 . 2 . . . . . . . . 5064 1 21 . 1 1 37 37 GLY HA3 H 1 4.087 0.005 . 2 . . . . . . . . 5064 1 22 . 1 1 37 37 GLY C C 13 176.044 0.05 . 1 . . . . . . . . 5064 1 23 . 1 1 38 38 GLU N N 15 120.555 0.05 . 1 . . . . . . . . 5064 1 24 . 1 1 38 38 GLU H H 1 8.722 0.005 . 1 . . . . . . . . 5064 1 25 . 1 1 38 38 GLU CA C 13 59.345 0.05 . 1 . . . . . . . . 5064 1 26 . 1 1 38 38 GLU HA H 1 3.16 0.005 . 1 . . . . . . . . 5064 1 27 . 1 1 38 38 GLU C C 13 179.74 0.05 . 1 . . . . . . . . 5064 1 28 . 1 1 38 38 GLU CB C 13 29.878 0.05 . 1 . . . . . . . . 5064 1 29 . 1 1 38 38 GLU CG C 13 36.805 0.05 . 1 . . . . . . . . 5064 1 30 . 1 1 38 38 GLU HG2 H 1 1.925 0.005 . 2 . . . . . . . . 5064 1 31 . 1 1 38 38 GLU HG3 H 1 2.033 0.005 . 2 . . . . . . . . 5064 1 32 . 1 1 38 38 GLU HB2 H 1 1.911 0.005 . 2 . . . . . . . . 5064 1 33 . 1 1 39 39 LYS N N 15 118.549 0.05 . 1 . . . . . . . . 5064 1 34 . 1 1 39 39 LYS H H 1 7.485 0.005 . 1 . . . . . . . . 5064 1 35 . 1 1 39 39 LYS CA C 13 59.546 0.05 . 1 . . . . . . . . 5064 1 36 . 1 1 39 39 LYS HA H 1 3.891 0.005 . 1 . . . . . . . . 5064 1 37 . 1 1 39 39 LYS C C 13 180.365 0.05 . 1 . . . . . . . . 5064 1 38 . 1 1 39 39 LYS CB C 13 32.576 0.05 . 1 . . . . . . . . 5064 1 39 . 1 1 39 39 LYS CG C 13 25.545 0.05 . 1 . . . . . . . . 5064 1 40 . 1 1 39 39 LYS HG2 H 1 1.377 0.005 . 2 . . . . . . . . 5064 1 41 . 1 1 39 39 LYS HG3 H 1 1.669 0.005 . 2 . . . . . . . . 5064 1 42 . 1 1 39 39 LYS CE C 13 41.768 0.05 . 1 . . . . . . . . 5064 1 43 . 1 1 39 39 LYS HB2 H 1 1.977 0.005 . 2 . . . . . . . . 5064 1 44 . 1 1 39 39 LYS HE2 H 1 2.965 0.005 . 2 . . . . . . . . 5064 1 45 . 1 1 40 40 ILE N N 15 121.326 0.05 . 1 . . . . . . . . 5064 1 46 . 1 1 40 40 ILE H H 1 8.327 0.005 . 1 . . . . . . . . 5064 1 47 . 1 1 40 40 ILE CA C 13 64.604 0.05 . 1 . . . . . . . . 5064 1 48 . 1 1 40 40 ILE HA H 1 3.8 0.005 . 1 . . . . . . . . 5064 1 49 . 1 1 40 40 ILE CB C 13 38.429 0.05 . 1 . . . . . . . . 5064 1 50 . 1 1 40 40 ILE HB H 1 1.824 0.005 . 1 . . . . . . . . 5064 1 51 . 1 1 40 40 ILE CG2 C 13 18.569 0.05 . 1 . . . . . . . . 5064 1 52 . 1 1 40 40 ILE HG21 H 1 0.86 0.005 . 1 . . . . . . . . 5064 1 53 . 1 1 40 40 ILE HG22 H 1 0.86 0.005 . 1 . . . . . . . . 5064 1 54 . 1 1 40 40 ILE HG23 H 1 0.86 0.005 . 1 . . . . . . . . 5064 1 55 . 1 1 40 40 ILE CD1 C 13 14.239 0.05 . 1 . . . . . . . . 5064 1 56 . 1 1 40 40 ILE HD11 H 1 0.869 0.005 . 1 . . . . . . . . 5064 1 57 . 1 1 40 40 ILE HD12 H 1 0.869 0.005 . 1 . . . . . . . . 5064 1 58 . 1 1 40 40 ILE HD13 H 1 0.869 0.005 . 1 . . . . . . . . 5064 1 59 . 1 1 40 40 ILE HG12 H 1 1.159 0.005 . 2 . . . . . . . . 5064 1 60 . 1 1 41 41 ARG CA C 13 56.303 0.05 . 1 . . . . . . . . 5064 1 61 . 1 1 41 41 ARG C C 13 178.995 0.05 . 1 . . . . . . . . 5064 1 62 . 1 1 41 41 ARG CB C 13 27.809 0.05 . 1 . . . . . . . . 5064 1 63 . 1 1 42 42 LYS N N 15 116.946 0.05 . 1 . . . . . . . . 5064 1 64 . 1 1 42 42 LYS H H 1 7.396 0.005 . 1 . . . . . . . . 5064 1 65 . 1 1 42 42 LYS CA C 13 57.935 0.05 . 1 . . . . . . . . 5064 1 66 . 1 1 42 42 LYS HA H 1 3.995 0.005 . 1 . . . . . . . . 5064 1 67 . 1 1 42 42 LYS C C 13 178.593 0.05 . 1 . . . . . . . . 5064 1 68 . 1 1 42 42 LYS CB C 13 32.896 0.05 . 1 . . . . . . . . 5064 1 69 . 1 1 42 42 LYS CG C 13 24.519 0.05 . 1 . . . . . . . . 5064 1 70 . 1 1 42 42 LYS HG2 H 1 1.353 0.005 . 2 . . . . . . . . 5064 1 71 . 1 1 42 42 LYS HG3 H 1 1.425 0.005 . 2 . . . . . . . . 5064 1 72 . 1 1 42 42 LYS CD C 13 29.684 0.05 . 1 . . . . . . . . 5064 1 73 . 1 1 42 42 LYS CE C 13 41.757 0.05 . 1 . . . . . . . . 5064 1 74 . 1 1 42 42 LYS HB2 H 1 1.763 0.005 . 2 . . . . . . . . 5064 1 75 . 1 1 42 42 LYS HD2 H 1 1.588 0.005 . 2 . . . . . . . . 5064 1 76 . 1 1 42 42 LYS HE2 H 1 2.878 0.005 . 2 . . . . . . . . 5064 1 77 . 1 1 43 43 LYS N N 15 118.977 0.05 . 1 . . . . . . . . 5064 1 78 . 1 1 43 43 LYS H H 1 7.735 0.005 . 1 . . . . . . . . 5064 1 79 . 1 1 43 43 LYS CA C 13 58.14 0.05 . 1 . . . . . . . . 5064 1 80 . 1 1 43 43 LYS HA H 1 3.802 0.005 . 1 . . . . . . . . 5064 1 81 . 1 1 43 43 LYS C C 13 176.959 0.05 . 1 . . . . . . . . 5064 1 82 . 1 1 43 43 LYS CB C 13 33.602 0.05 . 1 . . . . . . . . 5064 1 83 . 1 1 43 43 LYS HB2 H 1 1.499 0.005 . 2 . . . . . . . . 5064 1 84 . 1 1 43 43 LYS HB3 H 1 1.255 0.005 . 2 . . . . . . . . 5064 1 85 . 1 1 43 43 LYS CG C 13 24.962 0.05 . 1 . . . . . . . . 5064 1 86 . 1 1 43 43 LYS HG2 H 1 0.498 0.005 . 2 . . . . . . . . 5064 1 87 . 1 1 43 43 LYS HG3 H 1 0.934 0.005 . 2 . . . . . . . . 5064 1 88 . 1 1 43 43 LYS CD C 13 29.188 0.05 . 1 . . . . . . . . 5064 1 89 . 1 1 43 43 LYS CE C 13 41.758 0.05 . 1 . . . . . . . . 5064 1 90 . 1 1 43 43 LYS HD2 H 1 1.445 0.005 . 2 . . . . . . . . 5064 1 91 . 1 1 43 43 LYS HE2 H 1 2.791 0.005 . 2 . . . . . . . . 5064 1 92 . 1 1 44 44 TYR N N 15 115.229 0.05 . 1 . . . . . . . . 5064 1 93 . 1 1 44 44 TYR H H 1 8.07 0.005 . 1 . . . . . . . . 5064 1 94 . 1 1 44 44 TYR CA C 13 53.555 0.05 . 1 . . . . . . . . 5064 1 95 . 1 1 44 44 TYR HA H 1 5.091 0.005 . 1 . . . . . . . . 5064 1 96 . 1 1 44 44 TYR CB C 13 38.522 0.05 . 1 . . . . . . . . 5064 1 97 . 1 1 44 44 TYR HB2 H 1 2.679 0.005 . 2 . . . . . . . . 5064 1 98 . 1 1 44 44 TYR HB3 H 1 2.885 0.005 . 2 . . . . . . . . 5064 1 99 . 1 1 45 45 PRO CA C 13 64.515 0.05 . 1 . . . . . . . . 5064 1 100 . 1 1 45 45 PRO C C 13 177.614 0.05 . 1 . . . . . . . . 5064 1 101 . 1 1 45 45 PRO CB C 13 31.952 0.05 . 1 . . . . . . . . 5064 1 102 . 1 1 46 46 ASP N N 15 115.291 0.05 . 1 . . . . . . . . 5064 1 103 . 1 1 46 46 ASP H H 1 8.588 0.005 . 1 . . . . . . . . 5064 1 104 . 1 1 46 46 ASP CA C 13 53.038 0.05 . 1 . . . . . . . . 5064 1 105 . 1 1 46 46 ASP HA H 1 4.708 0.005 . 1 . . . . . . . . 5064 1 106 . 1 1 46 46 ASP C C 13 176.18 0.05 . 1 . . . . . . . . 5064 1 107 . 1 1 46 46 ASP CB C 13 40.533 0.05 . 1 . . . . . . . . 5064 1 108 . 1 1 46 46 ASP HB2 H 1 2.709 0.005 . 2 . . . . . . . . 5064 1 109 . 1 1 46 46 ASP HB3 H 1 2.831 0.005 . 2 . . . . . . . . 5064 1 110 . 1 1 47 47 ARG N N 15 119.391 0.05 . 1 . . . . . . . . 5064 1 111 . 1 1 47 47 ARG H H 1 7.842 0.005 . 1 . . . . . . . . 5064 1 112 . 1 1 47 47 ARG CA C 13 53.706 0.05 . 1 . . . . . . . . 5064 1 113 . 1 1 47 47 ARG HA H 1 4.913 0.005 . 1 . . . . . . . . 5064 1 114 . 1 1 47 47 ARG C C 13 175.023 0.05 . 1 . . . . . . . . 5064 1 115 . 1 1 47 47 ARG CB C 13 34.251 0.05 . 1 . . . . . . . . 5064 1 116 . 1 1 48 48 VAL N N 15 116.427 0.05 . 1 . . . . . . . . 5064 1 117 . 1 1 48 48 VAL H H 1 9.156 0.005 . 1 . . . . . . . . 5064 1 118 . 1 1 48 48 VAL CA C 13 57.168 0.05 . 1 . . . . . . . . 5064 1 119 . 1 1 48 48 VAL HA H 1 4.174 0.005 . 1 . . . . . . . . 5064 1 120 . 1 1 48 48 VAL CB C 13 34.057 0.05 . 1 . . . . . . . . 5064 1 121 . 1 1 48 48 VAL HB H 1 1.394 0.005 . 1 . . . . . . . . 5064 1 122 . 1 1 48 48 VAL CG1 C 13 18.792 0.05 . 2 . . . . . . . . 5064 1 123 . 1 1 48 48 VAL HG11 H 1 0.421 0.005 . 2 . . . . . . . . 5064 1 124 . 1 1 48 48 VAL HG12 H 1 0.421 0.005 . 2 . . . . . . . . 5064 1 125 . 1 1 48 48 VAL HG13 H 1 0.421 0.005 . 2 . . . . . . . . 5064 1 126 . 1 1 48 48 VAL CG2 C 13 21.866 0.05 . 2 . . . . . . . . 5064 1 127 . 1 1 48 48 VAL HG21 H 1 0.381 0.005 . 2 . . . . . . . . 5064 1 128 . 1 1 48 48 VAL HG22 H 1 0.381 0.005 . 2 . . . . . . . . 5064 1 129 . 1 1 48 48 VAL HG23 H 1 0.381 0.005 . 2 . . . . . . . . 5064 1 130 . 1 1 49 49 PRO CA C 13 60.963 0.05 . 1 . . . . . . . . 5064 1 131 . 1 1 49 49 PRO C C 13 175.561 0.05 . 1 . . . . . . . . 5064 1 132 . 1 1 49 49 PRO CB C 13 31.586 0.05 . 1 . . . . . . . . 5064 1 133 . 1 1 50 50 VAL N N 15 123.626 0.05 . 1 . . . . . . . . 5064 1 134 . 1 1 50 50 VAL H H 1 8.897 0.005 . 1 . . . . . . . . 5064 1 135 . 1 1 50 50 VAL CA C 13 59.297 0.05 . 1 . . . . . . . . 5064 1 136 . 1 1 50 50 VAL HA H 1 5.123 0.005 . 1 . . . . . . . . 5064 1 137 . 1 1 50 50 VAL C C 13 174.629 0.05 . 1 . . . . . . . . 5064 1 138 . 1 1 50 50 VAL CB C 13 36.274 0.05 . 1 . . . . . . . . 5064 1 139 . 1 1 50 50 VAL HB H 1 1.758 0.005 . 1 . . . . . . . . 5064 1 140 . 1 1 50 50 VAL CG1 C 13 22.485 0.05 . 2 . . . . . . . . 5064 1 141 . 1 1 50 50 VAL HG11 H 1 0.62 0.005 . 1 . . . . . . . . 5064 1 142 . 1 1 50 50 VAL HG12 H 1 0.62 0.005 . 1 . . . . . . . . 5064 1 143 . 1 1 50 50 VAL HG13 H 1 0.62 0.005 . 1 . . . . . . . . 5064 1 144 . 1 1 51 51 ILE N N 15 128.315 0.05 . 1 . . . . . . . . 5064 1 145 . 1 1 51 51 ILE H H 1 8.819 0.005 . 1 . . . . . . . . 5064 1 146 . 1 1 51 51 ILE CA C 13 56.83 0.05 . 1 . . . . . . . . 5064 1 147 . 1 1 51 51 ILE HA H 1 4.957 0.005 . 1 . . . . . . . . 5064 1 148 . 1 1 51 51 ILE C C 13 175.439 0.05 . 1 . . . . . . . . 5064 1 149 . 1 1 51 51 ILE CB C 13 36.478 0.05 . 1 . . . . . . . . 5064 1 150 . 1 1 51 51 ILE HB H 1 1.293 0.005 . 1 . . . . . . . . 5064 1 151 . 1 1 51 51 ILE CG2 C 13 17.428 0.05 . 1 . . . . . . . . 5064 1 152 . 1 1 51 51 ILE HG21 H 1 0.662 0.005 . 1 . . . . . . . . 5064 1 153 . 1 1 51 51 ILE HG22 H 1 0.662 0.005 . 1 . . . . . . . . 5064 1 154 . 1 1 51 51 ILE HG23 H 1 0.662 0.005 . 1 . . . . . . . . 5064 1 155 . 1 1 51 51 ILE CD1 C 13 8.659 0.05 . 1 . . . . . . . . 5064 1 156 . 1 1 51 51 ILE HD11 H 1 -0.556 0.005 . 1 . . . . . . . . 5064 1 157 . 1 1 51 51 ILE HD12 H 1 -0.556 0.005 . 1 . . . . . . . . 5064 1 158 . 1 1 51 51 ILE HD13 H 1 -0.556 0.005 . 1 . . . . . . . . 5064 1 159 . 1 1 52 52 VAL N N 15 126.726 0.05 . 1 . . . . . . . . 5064 1 160 . 1 1 52 52 VAL H H 1 9.13 0.005 . 1 . . . . . . . . 5064 1 161 . 1 1 52 52 VAL CA C 13 59.847 0.05 . 1 . . . . . . . . 5064 1 162 . 1 1 52 52 VAL HA H 1 5.746 0.005 . 1 . . . . . . . . 5064 1 163 . 1 1 52 52 VAL C C 13 176.383 0.05 . 1 . . . . . . . . 5064 1 164 . 1 1 52 52 VAL CB C 13 34.028 0.05 . 1 . . . . . . . . 5064 1 165 . 1 1 52 52 VAL HB H 1 2.064 0.005 . 1 . . . . . . . . 5064 1 166 . 1 1 52 52 VAL HG21 H 1 0.865 0.005 . 2 . . . . . . . . 5064 1 167 . 1 1 52 52 VAL HG22 H 1 0.865 0.005 . 2 . . . . . . . . 5064 1 168 . 1 1 52 52 VAL HG23 H 1 0.865 0.005 . 2 . . . . . . . . 5064 1 169 . 1 1 52 52 VAL CG1 C 13 22.388 0.05 . 2 . . . . . . . . 5064 1 170 . 1 1 52 52 VAL HG11 H 1 0.857 0.005 . 1 . . . . . . . . 5064 1 171 . 1 1 52 52 VAL HG12 H 1 0.857 0.005 . 1 . . . . . . . . 5064 1 172 . 1 1 52 52 VAL HG13 H 1 0.857 0.005 . 1 . . . . . . . . 5064 1 173 . 1 1 53 53 GLU N N 15 121.509 0.05 . 1 . . . . . . . . 5064 1 174 . 1 1 53 53 GLU H H 1 8.717 0.005 . 1 . . . . . . . . 5064 1 175 . 1 1 53 53 GLU CA C 13 54.567 0.05 . 1 . . . . . . . . 5064 1 176 . 1 1 53 53 GLU HA H 1 4.977 0.005 . 1 . . . . . . . . 5064 1 177 . 1 1 53 53 GLU C C 13 175.042 0.05 . 1 . . . . . . . . 5064 1 178 . 1 1 53 53 GLU CB C 13 36.4 0.05 . 1 . . . . . . . . 5064 1 179 . 1 1 53 53 GLU HB2 H 1 1.911 0.005 . 2 . . . . . . . . 5064 1 180 . 1 1 53 53 GLU HB3 H 1 2.304 0.005 . 2 . . . . . . . . 5064 1 181 . 1 1 53 53 GLU HG2 H 1 2.61 0.005 . 2 . . . . . . . . 5064 1 182 . 1 1 54 54 LYS N N 15 123.43 0.05 . 1 . . . . . . . . 5064 1 183 . 1 1 54 54 LYS H H 1 8.9 0.005 . 1 . . . . . . . . 5064 1 184 . 1 1 54 54 LYS CA C 13 56.056 0.05 . 1 . . . . . . . . 5064 1 185 . 1 1 54 54 LYS HA H 1 3.07 0.005 . 1 . . . . . . . . 5064 1 186 . 1 1 54 54 LYS C C 13 177.675 0.05 . 1 . . . . . . . . 5064 1 187 . 1 1 54 54 LYS CB C 13 32.867 0.05 . 1 . . . . . . . . 5064 1 188 . 1 1 55 55 ALA N N 15 130.41 0.05 . 1 . . . . . . . . 5064 1 189 . 1 1 55 55 ALA H H 1 8.943 0.005 . 1 . . . . . . . . 5064 1 190 . 1 1 55 55 ALA CA C 13 50.612 0.05 . 1 . . . . . . . . 5064 1 191 . 1 1 55 55 ALA HA H 1 4.424 0.005 . 1 . . . . . . . . 5064 1 192 . 1 1 55 55 ALA CB C 13 18.01 0.05 . 1 . . . . . . . . 5064 1 193 . 1 1 55 55 ALA HB1 H 1 1.205 0.005 . 1 . . . . . . . . 5064 1 194 . 1 1 55 55 ALA HB2 H 1 1.205 0.005 . 1 . . . . . . . . 5064 1 195 . 1 1 55 55 ALA HB3 H 1 1.205 0.005 . 1 . . . . . . . . 5064 1 196 . 1 1 56 56 PRO CA C 13 64.861 0.05 . 1 . . . . . . . . 5064 1 197 . 1 1 56 56 PRO C C 13 178.293 0.05 . 1 . . . . . . . . 5064 1 198 . 1 1 56 56 PRO CB C 13 32.099 0.05 . 1 . . . . . . . . 5064 1 199 . 1 1 57 57 LYS N N 15 114.561 0.05 . 1 . . . . . . . . 5064 1 200 . 1 1 57 57 LYS H H 1 8.465 0.005 . 1 . . . . . . . . 5064 1 201 . 1 1 57 57 LYS CA C 13 56.562 0.05 . 1 . . . . . . . . 5064 1 202 . 1 1 57 57 LYS HA H 1 4.057 0.005 . 1 . . . . . . . . 5064 1 203 . 1 1 57 57 LYS C C 13 176.985 0.05 . 1 . . . . . . . . 5064 1 204 . 1 1 57 57 LYS CB C 13 31.184 0.05 . 1 . . . . . . . . 5064 1 205 . 1 1 58 58 ALA N N 15 122.159 0.05 . 1 . . . . . . . . 5064 1 206 . 1 1 58 58 ALA H H 1 7.478 0.005 . 1 . . . . . . . . 5064 1 207 . 1 1 58 58 ALA CA C 13 52.816 0.05 . 1 . . . . . . . . 5064 1 208 . 1 1 58 58 ALA HA H 1 4.475 0.005 . 1 . . . . . . . . 5064 1 209 . 1 1 58 58 ALA C C 13 179.134 0.05 . 1 . . . . . . . . 5064 1 210 . 1 1 58 58 ALA CB C 13 20.932 0.05 . 1 . . . . . . . . 5064 1 211 . 1 1 58 58 ALA HB1 H 1 1.61 0.005 . 1 . . . . . . . . 5064 1 212 . 1 1 58 58 ALA HB2 H 1 1.61 0.005 . 1 . . . . . . . . 5064 1 213 . 1 1 58 58 ALA HB3 H 1 1.61 0.005 . 1 . . . . . . . . 5064 1 214 . 1 1 59 59 ARG N N 15 125.002 0.05 . 1 . . . . . . . . 5064 1 215 . 1 1 59 59 ARG H H 1 9.172 0.005 . 1 . . . . . . . . 5064 1 216 . 1 1 59 59 ARG CA C 13 55.748 0.05 . 1 . . . . . . . . 5064 1 217 . 1 1 59 59 ARG HA H 1 4.478 0.005 . 1 . . . . . . . . 5064 1 218 . 1 1 59 59 ARG C C 13 176.313 0.05 . 1 . . . . . . . . 5064 1 219 . 1 1 59 59 ARG CB C 13 29.431 0.05 . 1 . . . . . . . . 5064 1 220 . 1 1 60 60 ILE N N 15 115.5 0.05 . 1 . . . . . . . . 5064 1 221 . 1 1 60 60 ILE H H 1 6.961 0.005 . 1 . . . . . . . . 5064 1 222 . 1 1 60 60 ILE CA C 13 60.13 0.05 . 1 . . . . . . . . 5064 1 223 . 1 1 60 60 ILE HA H 1 4.488 0.005 . 1 . . . . . . . . 5064 1 224 . 1 1 60 60 ILE C C 13 174.415 0.05 . 1 . . . . . . . . 5064 1 225 . 1 1 60 60 ILE CB C 13 40.621 0.05 . 1 . . . . . . . . 5064 1 226 . 1 1 60 60 ILE HB H 1 2.076 0.005 . 1 . . . . . . . . 5064 1 227 . 1 1 60 60 ILE HG12 H 1 1.466 0.005 . 2 . . . . . . . . 5064 1 228 . 1 1 60 60 ILE HG13 H 1 1.785 0.005 . 2 . . . . . . . . 5064 1 229 . 1 1 60 60 ILE CG2 C 13 18.34 0.05 . 1 . . . . . . . . 5064 1 230 . 1 1 60 60 ILE HG21 H 1 1.107 0.005 . 1 . . . . . . . . 5064 1 231 . 1 1 60 60 ILE HG22 H 1 1.107 0.005 . 1 . . . . . . . . 5064 1 232 . 1 1 60 60 ILE HG23 H 1 1.107 0.005 . 1 . . . . . . . . 5064 1 233 . 1 1 60 60 ILE CD1 C 13 15.697 0.05 . 1 . . . . . . . . 5064 1 234 . 1 1 60 60 ILE HD11 H 1 1.142 0.005 . 1 . . . . . . . . 5064 1 235 . 1 1 60 60 ILE HD12 H 1 1.142 0.005 . 1 . . . . . . . . 5064 1 236 . 1 1 60 60 ILE HD13 H 1 1.142 0.005 . 1 . . . . . . . . 5064 1 237 . 1 1 61 61 GLY N N 15 108.02 0.05 . 1 . . . . . . . . 5064 1 238 . 1 1 61 61 GLY H H 1 8.337 0.005 . 1 . . . . . . . . 5064 1 239 . 1 1 61 61 GLY CA C 13 45.352 0.05 . 1 . . . . . . . . 5064 1 240 . 1 1 61 61 GLY HA2 H 1 3.895 0.005 . 2 . . . . . . . . 5064 1 241 . 1 1 61 61 GLY HA3 H 1 4.098 0.005 . 2 . . . . . . . . 5064 1 242 . 1 1 61 61 GLY C C 13 173.392 0.05 . 1 . . . . . . . . 5064 1 243 . 1 1 62 62 ASP N N 15 118.877 0.05 . 1 . . . . . . . . 5064 1 244 . 1 1 62 62 ASP H H 1 8.366 0.005 . 1 . . . . . . . . 5064 1 245 . 1 1 62 62 ASP CA C 13 54.044 0.05 . 1 . . . . . . . . 5064 1 246 . 1 1 62 62 ASP HA H 1 4.773 0.005 . 1 . . . . . . . . 5064 1 247 . 1 1 62 62 ASP C C 13 176.308 0.05 . 1 . . . . . . . . 5064 1 248 . 1 1 62 62 ASP CB C 13 43.06 0.05 . 1 . . . . . . . . 5064 1 249 . 1 1 62 62 ASP HB2 H 1 2.535 0.005 . 2 . . . . . . . . 5064 1 250 . 1 1 62 62 ASP HB3 H 1 2.733 0.005 . 2 . . . . . . . . 5064 1 251 . 1 1 63 63 LEU N N 15 123.497 0.05 . 1 . . . . . . . . 5064 1 252 . 1 1 63 63 LEU H H 1 8.151 0.005 . 1 . . . . . . . . 5064 1 253 . 1 1 63 63 LEU CA C 13 54.044 0.05 . 1 . . . . . . . . 5064 1 254 . 1 1 63 63 LEU HA H 1 4.423 0.005 . 1 . . . . . . . . 5064 1 255 . 1 1 63 63 LEU C C 13 177.406 0.05 . 1 . . . . . . . . 5064 1 256 . 1 1 63 63 LEU CB C 13 44.74 0.05 . 1 . . . . . . . . 5064 1 257 . 1 1 63 63 LEU HB3 H 1 1.84 0.005 . 2 . . . . . . . . 5064 1 258 . 1 1 63 63 LEU CD1 C 13 26.212 0.05 . 2 . . . . . . . . 5064 1 259 . 1 1 63 63 LEU HD11 H 1 0.957 0.005 . 2 . . . . . . . . 5064 1 260 . 1 1 63 63 LEU HD12 H 1 0.957 0.005 . 2 . . . . . . . . 5064 1 261 . 1 1 63 63 LEU HD13 H 1 0.957 0.005 . 2 . . . . . . . . 5064 1 262 . 1 1 64 64 ASP N N 15 122.569 0.05 . 1 . . . . . . . . 5064 1 263 . 1 1 64 64 ASP H H 1 8.726 0.005 . 1 . . . . . . . . 5064 1 264 . 1 1 64 64 ASP CA C 13 55.329 0.05 . 1 . . . . . . . . 5064 1 265 . 1 1 64 64 ASP HA H 1 4.41 0.005 . 1 . . . . . . . . 5064 1 266 . 1 1 64 64 ASP C C 13 176.14 0.05 . 1 . . . . . . . . 5064 1 267 . 1 1 64 64 ASP CB C 13 40.107 0.05 . 1 . . . . . . . . 5064 1 268 . 1 1 64 64 ASP HB2 H 1 2.791 0.005 . 2 . . . . . . . . 5064 1 269 . 1 1 65 65 LYS N N 15 120.57 0.05 . 1 . . . . . . . . 5064 1 270 . 1 1 65 65 LYS H H 1 7.455 0.005 . 1 . . . . . . . . 5064 1 271 . 1 1 65 65 LYS CA C 13 55.324 0.05 . 1 . . . . . . . . 5064 1 272 . 1 1 65 65 LYS HA H 1 4.502 0.005 . 1 . . . . . . . . 5064 1 273 . 1 1 65 65 LYS CB C 13 34.611 0.05 . 1 . . . . . . . . 5064 1 274 . 1 1 66 66 LYS CA C 13 56.634 0.05 . 1 . . . . . . . . 5064 1 275 . 1 1 66 66 LYS C C 13 174.707 0.05 . 1 . . . . . . . . 5064 1 276 . 1 1 67 67 LYS N N 15 119.361 0.05 . 1 . . . . . . . . 5064 1 277 . 1 1 67 67 LYS H H 1 6.968 0.005 . 1 . . . . . . . . 5064 1 278 . 1 1 67 67 LYS CA C 13 54.995 0.05 . 1 . . . . . . . . 5064 1 279 . 1 1 67 67 LYS HA H 1 5.088 0.005 . 1 . . . . . . . . 5064 1 280 . 1 1 67 67 LYS C C 13 175.466 0.05 . 1 . . . . . . . . 5064 1 281 . 1 1 67 67 LYS CB C 13 34.502 0.05 . 1 . . . . . . . . 5064 1 282 . 1 1 67 67 LYS HB2 H 1 1.577 0.005 . 2 . . . . . . . . 5064 1 283 . 1 1 67 67 LYS HG2 H 1 1.214 0.005 . 2 . . . . . . . . 5064 1 284 . 1 1 68 68 TYR N N 15 125.283 0.05 . 1 . . . . . . . . 5064 1 285 . 1 1 68 68 TYR H H 1 9.541 0.005 . 1 . . . . . . . . 5064 1 286 . 1 1 68 68 TYR CA C 13 57.059 0.05 . 1 . . . . . . . . 5064 1 287 . 1 1 68 68 TYR C C 13 174.539 0.05 . 1 . . . . . . . . 5064 1 288 . 1 1 68 68 TYR CB C 13 42.585 0.05 . 1 . . . . . . . . 5064 1 289 . 1 1 69 69 LEU N N 15 125.016 0.05 . 1 . . . . . . . . 5064 1 290 . 1 1 69 69 LEU H H 1 8.659 0.005 . 1 . . . . . . . . 5064 1 291 . 1 1 69 69 LEU CA C 13 53.689 0.05 . 1 . . . . . . . . 5064 1 292 . 1 1 69 69 LEU HA H 1 4.911 0.005 . 1 . . . . . . . . 5064 1 293 . 1 1 69 69 LEU C C 13 177.156 0.05 . 1 . . . . . . . . 5064 1 294 . 1 1 69 69 LEU CB C 13 42.592 0.05 . 1 . . . . . . . . 5064 1 295 . 1 1 69 69 LEU CG C 13 27.384 0.05 . 1 . . . . . . . . 5064 1 296 . 1 1 69 69 LEU HG H 1 1.059 0.005 . 1 . . . . . . . . 5064 1 297 . 1 1 69 69 LEU CD1 C 13 25.003 0.05 . 2 . . . . . . . . 5064 1 298 . 1 1 69 69 LEU HD11 H 1 0.406 0.005 . 2 . . . . . . . . 5064 1 299 . 1 1 69 69 LEU HD12 H 1 0.406 0.005 . 2 . . . . . . . . 5064 1 300 . 1 1 69 69 LEU HD13 H 1 0.406 0.005 . 2 . . . . . . . . 5064 1 301 . 1 1 69 69 LEU CD2 C 13 24.12 0.05 . 2 . . . . . . . . 5064 1 302 . 1 1 69 69 LEU HD21 H 1 0.458 0.005 . 2 . . . . . . . . 5064 1 303 . 1 1 69 69 LEU HD22 H 1 0.458 0.005 . 2 . . . . . . . . 5064 1 304 . 1 1 69 69 LEU HD23 H 1 0.458 0.005 . 2 . . . . . . . . 5064 1 305 . 1 1 69 69 LEU HB3 H 1 1.307 0.005 . 2 . . . . . . . . 5064 1 306 . 1 1 70 70 VAL N N 15 121.702 0.05 . 1 . . . . . . . . 5064 1 307 . 1 1 70 70 VAL H H 1 8.455 0.005 . 1 . . . . . . . . 5064 1 308 . 1 1 70 70 VAL CA C 13 58.314 0.05 . 1 . . . . . . . . 5064 1 309 . 1 1 70 70 VAL HA H 1 4.832 0.005 . 1 . . . . . . . . 5064 1 310 . 1 1 70 70 VAL CB C 13 33.35 0.05 . 1 . . . . . . . . 5064 1 311 . 1 1 70 70 VAL HB H 1 1.982 0.005 . 1 . . . . . . . . 5064 1 312 . 1 1 70 70 VAL CG1 C 13 20.479 0.05 . 2 . . . . . . . . 5064 1 313 . 1 1 70 70 VAL HG11 H 1 0.567 0.005 . 2 . . . . . . . . 5064 1 314 . 1 1 70 70 VAL HG12 H 1 0.567 0.005 . 2 . . . . . . . . 5064 1 315 . 1 1 70 70 VAL HG13 H 1 0.567 0.005 . 2 . . . . . . . . 5064 1 316 . 1 1 70 70 VAL CG2 C 13 22.345 0.05 . 2 . . . . . . . . 5064 1 317 . 1 1 70 70 VAL HG21 H 1 0.877 0.005 . 2 . . . . . . . . 5064 1 318 . 1 1 70 70 VAL HG22 H 1 0.877 0.005 . 2 . . . . . . . . 5064 1 319 . 1 1 70 70 VAL HG23 H 1 0.877 0.005 . 2 . . . . . . . . 5064 1 320 . 1 1 71 71 PRO CA C 13 63.561 0.05 . 1 . . . . . . . . 5064 1 321 . 1 1 71 71 PRO HA H 1 4.125 0.005 . 1 . . . . . . . . 5064 1 322 . 1 1 71 71 PRO C C 13 178.048 0.05 . 1 . . . . . . . . 5064 1 323 . 1 1 71 71 PRO CB C 13 32.601 0.05 . 1 . . . . . . . . 5064 1 324 . 1 1 71 71 PRO CG C 13 31.683 0.05 . 1 . . . . . . . . 5064 1 325 . 1 1 71 71 PRO CD C 13 48.684 0.05 . 1 . . . . . . . . 5064 1 326 . 1 1 71 71 PRO HD2 H 1 3.338 0.005 . 2 . . . . . . . . 5064 1 327 . 1 1 71 71 PRO HD3 H 1 3.412 0.005 . 2 . . . . . . . . 5064 1 328 . 1 1 71 71 PRO HB2 H 1 2.353 0.005 . 2 . . . . . . . . 5064 1 329 . 1 1 71 71 PRO HG2 H 1 2.064 0.005 . 2 . . . . . . . . 5064 1 330 . 1 1 72 72 SER N N 15 118.386 0.05 . 1 . . . . . . . . 5064 1 331 . 1 1 72 72 SER H H 1 8.38 0.005 . 1 . . . . . . . . 5064 1 332 . 1 1 72 72 SER CA C 13 60.895 0.05 . 1 . . . . . . . . 5064 1 333 . 1 1 72 72 SER C C 13 175.295 0.05 . 1 . . . . . . . . 5064 1 334 . 1 1 72 72 SER CB C 13 62.682 0.05 . 1 . . . . . . . . 5064 1 335 . 1 1 73 73 ASP N N 15 115.373 0.05 . 1 . . . . . . . . 5064 1 336 . 1 1 73 73 ASP H H 1 8.284 0.005 . 1 . . . . . . . . 5064 1 337 . 1 1 73 73 ASP CA C 13 53.355 0.05 . 1 . . . . . . . . 5064 1 338 . 1 1 73 73 ASP HA H 1 4.545 0.005 . 1 . . . . . . . . 5064 1 339 . 1 1 73 73 ASP C C 13 176.879 0.05 . 1 . . . . . . . . 5064 1 340 . 1 1 73 73 ASP CB C 13 40.32 0.05 . 1 . . . . . . . . 5064 1 341 . 1 1 73 73 ASP HB2 H 1 2.709 0.005 . 2 . . . . . . . . 5064 1 342 . 1 1 73 73 ASP HB3 H 1 2.791 0.005 . 2 . . . . . . . . 5064 1 343 . 1 1 74 74 LEU N N 15 123.864 0.05 . 1 . . . . . . . . 5064 1 344 . 1 1 74 74 LEU H H 1 7.405 0.005 . 1 . . . . . . . . 5064 1 345 . 1 1 74 74 LEU CA C 13 55.562 0.05 . 1 . . . . . . . . 5064 1 346 . 1 1 74 74 LEU HA H 1 4.276 0.005 . 1 . . . . . . . . 5064 1 347 . 1 1 74 74 LEU C C 13 177.715 0.05 . 1 . . . . . . . . 5064 1 348 . 1 1 74 74 LEU CB C 13 43.752 0.05 . 1 . . . . . . . . 5064 1 349 . 1 1 74 74 LEU HB2 H 1 1.474 0.005 . 2 . . . . . . . . 5064 1 350 . 1 1 74 74 LEU HB3 H 1 1.724 0.005 . 2 . . . . . . . . 5064 1 351 . 1 1 74 74 LEU HD11 H 1 0.878 0.005 . 2 . . . . . . . . 5064 1 352 . 1 1 74 74 LEU HD12 H 1 0.878 0.005 . 2 . . . . . . . . 5064 1 353 . 1 1 74 74 LEU HD13 H 1 0.878 0.005 . 2 . . . . . . . . 5064 1 354 . 1 1 74 74 LEU CD2 C 13 25.364 0.05 . 2 . . . . . . . . 5064 1 355 . 1 1 74 74 LEU HD21 H 1 1.001 0.005 . 2 . . . . . . . . 5064 1 356 . 1 1 74 74 LEU HD22 H 1 1.001 0.005 . 2 . . . . . . . . 5064 1 357 . 1 1 74 74 LEU HD23 H 1 1.001 0.005 . 2 . . . . . . . . 5064 1 358 . 1 1 75 75 THR N N 15 116.727 0.05 . 1 . . . . . . . . 5064 1 359 . 1 1 75 75 THR H H 1 8.775 0.005 . 1 . . . . . . . . 5064 1 360 . 1 1 75 75 THR CA C 13 60.918 0.05 . 1 . . . . . . . . 5064 1 361 . 1 1 75 75 THR HA H 1 4.997 0.005 . 1 . . . . . . . . 5064 1 362 . 1 1 75 75 THR C C 13 176.967 0.05 . 1 . . . . . . . . 5064 1 363 . 1 1 75 75 THR CB C 13 71.342 0.05 . 1 . . . . . . . . 5064 1 364 . 1 1 75 75 THR HB H 1 4.829 0.005 . 1 . . . . . . . . 5064 1 365 . 1 1 75 75 THR CG2 C 13 22.207 0.05 . 1 . . . . . . . . 5064 1 366 . 1 1 75 75 THR HG21 H 1 1.269 0.005 . 1 . . . . . . . . 5064 1 367 . 1 1 75 75 THR HG22 H 1 1.269 0.005 . 1 . . . . . . . . 5064 1 368 . 1 1 75 75 THR HG23 H 1 1.269 0.005 . 1 . . . . . . . . 5064 1 369 . 1 1 76 76 VAL N N 15 123.12 0.05 . 1 . . . . . . . . 5064 1 370 . 1 1 76 76 VAL H H 1 9.145 0.005 . 1 . . . . . . . . 5064 1 371 . 1 1 76 76 VAL CA C 13 66.546 0.05 . 1 . . . . . . . . 5064 1 372 . 1 1 76 76 VAL HA H 1 3.694 0.005 . 1 . . . . . . . . 5064 1 373 . 1 1 76 76 VAL C C 13 179.462 0.05 . 1 . . . . . . . . 5064 1 374 . 1 1 76 76 VAL CB C 13 31.801 0.05 . 1 . . . . . . . . 5064 1 375 . 1 1 76 76 VAL HB H 1 2.401 0.005 . 1 . . . . . . . . 5064 1 376 . 1 1 76 76 VAL HG11 H 1 0.872 0.005 . 2 . . . . . . . . 5064 1 377 . 1 1 76 76 VAL HG12 H 1 0.872 0.005 . 2 . . . . . . . . 5064 1 378 . 1 1 76 76 VAL HG13 H 1 0.872 0.005 . 2 . . . . . . . . 5064 1 379 . 1 1 76 76 VAL HG21 H 1 0.973 0.005 . 2 . . . . . . . . 5064 1 380 . 1 1 76 76 VAL HG22 H 1 0.973 0.005 . 2 . . . . . . . . 5064 1 381 . 1 1 76 76 VAL HG23 H 1 0.973 0.005 . 2 . . . . . . . . 5064 1 382 . 1 1 76 76 VAL CG1 C 13 22.699 0.05 . 2 . . . . . . . . 5064 1 383 . 1 1 77 77 GLY N N 15 105.524 0.05 . 1 . . . . . . . . 5064 1 384 . 1 1 77 77 GLY H H 1 8.943 0.005 . 1 . . . . . . . . 5064 1 385 . 1 1 77 77 GLY CA C 13 47.64 0.05 . 1 . . . . . . . . 5064 1 386 . 1 1 77 77 GLY HA2 H 1 3.933 0.005 . 2 . . . . . . . . 5064 1 387 . 1 1 77 77 GLY HA3 H 1 4.106 0.005 . 2 . . . . . . . . 5064 1 388 . 1 1 77 77 GLY C C 13 177.056 0.05 . 1 . . . . . . . . 5064 1 389 . 1 1 78 78 GLN N N 15 121.739 0.05 . 1 . . . . . . . . 5064 1 390 . 1 1 78 78 GLN H H 1 8.148 0.005 . 1 . . . . . . . . 5064 1 391 . 1 1 78 78 GLN CA C 13 58.726 0.05 . 1 . . . . . . . . 5064 1 392 . 1 1 78 78 GLN HA H 1 4.268 0.005 . 1 . . . . . . . . 5064 1 393 . 1 1 78 78 GLN C C 13 180.023 0.05 . 1 . . . . . . . . 5064 1 394 . 1 1 78 78 GLN CB C 13 28.963 0.05 . 1 . . . . . . . . 5064 1 395 . 1 1 78 78 GLN CG C 13 35.217 0.05 . 1 . . . . . . . . 5064 1 396 . 1 1 78 78 GLN HB2 H 1 2.101 0.005 . 2 . . . . . . . . 5064 1 397 . 1 1 78 78 GLN HG2 H 1 2.491 0.005 . 2 . . . . . . . . 5064 1 398 . 1 1 79 79 PHE N N 15 125.694 0.05 . 1 . . . . . . . . 5064 1 399 . 1 1 79 79 PHE H H 1 8.885 0.005 . 1 . . . . . . . . 5064 1 400 . 1 1 79 79 PHE CA C 13 61.266 0.05 . 1 . . . . . . . . 5064 1 401 . 1 1 79 79 PHE HA H 1 4.471 0.005 . 1 . . . . . . . . 5064 1 402 . 1 1 79 79 PHE C C 13 178.173 0.05 . 1 . . . . . . . . 5064 1 403 . 1 1 79 79 PHE CB C 13 39.559 0.05 . 1 . . . . . . . . 5064 1 404 . 1 1 79 79 PHE HB2 H 1 3.157 0.005 . 2 . . . . . . . . 5064 1 405 . 1 1 79 79 PHE HB3 H 1 3.282 0.005 . 2 . . . . . . . . 5064 1 406 . 1 1 80 80 TYR N N 15 118.811 0.05 . 1 . . . . . . . . 5064 1 407 . 1 1 80 80 TYR H H 1 9.156 0.005 . 1 . . . . . . . . 5064 1 408 . 1 1 80 80 TYR CA C 13 61.388 0.05 . 1 . . . . . . . . 5064 1 409 . 1 1 80 80 TYR HA H 1 3.954 0.005 . 1 . . . . . . . . 5064 1 410 . 1 1 80 80 TYR C C 13 178.751 0.05 . 1 . . . . . . . . 5064 1 411 . 1 1 80 80 TYR CB C 13 38.216 0.05 . 1 . . . . . . . . 5064 1 412 . 1 1 80 80 TYR HB2 H 1 2.771 0.005 . 2 . . . . . . . . 5064 1 413 . 1 1 80 80 TYR HB3 H 1 3.021 0.005 . 2 . . . . . . . . 5064 1 414 . 1 1 81 81 PHE N N 15 117.084 0.05 . 1 . . . . . . . . 5064 1 415 . 1 1 81 81 PHE H H 1 7.402 0.005 . 1 . . . . . . . . 5064 1 416 . 1 1 81 81 PHE CA C 13 61.652 0.05 . 1 . . . . . . . . 5064 1 417 . 1 1 81 81 PHE HA H 1 4.048 0.005 . 1 . . . . . . . . 5064 1 418 . 1 1 81 81 PHE C C 13 178.121 0.05 . 1 . . . . . . . . 5064 1 419 . 1 1 81 81 PHE CB C 13 38.623 0.05 . 1 . . . . . . . . 5064 1 420 . 1 1 81 81 PHE HB2 H 1 3.184 0.005 . 2 . . . . . . . . 5064 1 421 . 1 1 81 81 PHE HB3 H 1 3.288 0.005 . 2 . . . . . . . . 5064 1 422 . 1 1 82 82 LEU N N 15 120.433 0.05 . 1 . . . . . . . . 5064 1 423 . 1 1 82 82 LEU H H 1 7.602 0.005 . 1 . . . . . . . . 5064 1 424 . 1 1 82 82 LEU CA C 13 58.356 0.05 . 1 . . . . . . . . 5064 1 425 . 1 1 82 82 LEU HA H 1 3.949 0.005 . 1 . . . . . . . . 5064 1 426 . 1 1 82 82 LEU C C 13 180.138 0.05 . 1 . . . . . . . . 5064 1 427 . 1 1 82 82 LEU CB C 13 42.188 0.05 . 1 . . . . . . . . 5064 1 428 . 1 1 83 83 ILE N N 15 119.929 0.05 . 1 . . . . . . . . 5064 1 429 . 1 1 83 83 ILE H H 1 7.852 0.005 . 1 . . . . . . . . 5064 1 430 . 1 1 83 83 ILE CA C 13 61.337 0.05 . 1 . . . . . . . . 5064 1 431 . 1 1 83 83 ILE HA H 1 3.441 0.005 . 1 . . . . . . . . 5064 1 432 . 1 1 83 83 ILE C C 13 178.371 0.05 . 1 . . . . . . . . 5064 1 433 . 1 1 83 83 ILE CB C 13 34.781 0.05 . 1 . . . . . . . . 5064 1 434 . 1 1 83 83 ILE HB H 1 1.811 0.005 . 1 . . . . . . . . 5064 1 435 . 1 1 83 83 ILE CG1 C 13 26.686 0.05 . 1 . . . . . . . . 5064 1 436 . 1 1 83 83 ILE HG12 H 1 0.459 0.005 . 2 . . . . . . . . 5064 1 437 . 1 1 83 83 ILE HG13 H 1 0.694 0.005 . 2 . . . . . . . . 5064 1 438 . 1 1 83 83 ILE CG2 C 13 17.552 0.05 . 1 . . . . . . . . 5064 1 439 . 1 1 83 83 ILE HG21 H 1 0.373 0.005 . 1 . . . . . . . . 5064 1 440 . 1 1 83 83 ILE HG22 H 1 0.373 0.005 . 1 . . . . . . . . 5064 1 441 . 1 1 83 83 ILE HG23 H 1 0.373 0.005 . 1 . . . . . . . . 5064 1 442 . 1 1 83 83 ILE CD1 C 13 7.815 0.05 . 1 . . . . . . . . 5064 1 443 . 1 1 83 83 ILE HD11 H 1 -0.115 0.005 . 1 . . . . . . . . 5064 1 444 . 1 1 83 83 ILE HD12 H 1 -0.115 0.005 . 1 . . . . . . . . 5064 1 445 . 1 1 83 83 ILE HD13 H 1 -0.115 0.005 . 1 . . . . . . . . 5064 1 446 . 1 1 84 84 ARG N N 15 118.83 0.05 . 1 . . . . . . . . 5064 1 447 . 1 1 84 84 ARG H H 1 8.546 0.005 . 1 . . . . . . . . 5064 1 448 . 1 1 84 84 ARG CA C 13 60.473 0.05 . 1 . . . . . . . . 5064 1 449 . 1 1 84 84 ARG HA H 1 3.397 0.005 . 1 . . . . . . . . 5064 1 450 . 1 1 84 84 ARG C C 13 179.143 0.05 . 1 . . . . . . . . 5064 1 451 . 1 1 84 84 ARG CB C 13 30.497 0.05 . 1 . . . . . . . . 5064 1 452 . 1 1 84 84 ARG CG C 13 29.683 0.05 . 1 . . . . . . . . 5064 1 453 . 1 1 84 84 ARG CD C 13 43.128 0.05 . 1 . . . . . . . . 5064 1 454 . 1 1 84 84 ARG HB2 H 1 1.639 0.005 . 2 . . . . . . . . 5064 1 455 . 1 1 84 84 ARG HG2 H 1 1.177 0.005 . 2 . . . . . . . . 5064 1 456 . 1 1 84 84 ARG HD2 H 1 2.827 0.005 . 2 . . . . . . . . 5064 1 457 . 1 1 85 85 LYS N N 15 115.547 0.05 . 1 . . . . . . . . 5064 1 458 . 1 1 85 85 LYS H H 1 7.353 0.005 . 1 . . . . . . . . 5064 1 459 . 1 1 85 85 LYS CA C 13 58.374 0.05 . 1 . . . . . . . . 5064 1 460 . 1 1 85 85 LYS HA H 1 4 0.005 . 1 . . . . . . . . 5064 1 461 . 1 1 85 85 LYS C C 13 180.062 0.05 . 1 . . . . . . . . 5064 1 462 . 1 1 85 85 LYS CB C 13 32.257 0.05 . 1 . . . . . . . . 5064 1 463 . 1 1 86 86 ARG N N 15 118.98 0.05 . 1 . . . . . . . . 5064 1 464 . 1 1 86 86 ARG H H 1 7.552 0.005 . 1 . . . . . . . . 5064 1 465 . 1 1 86 86 ARG CA C 13 58.336 0.05 . 1 . . . . . . . . 5064 1 466 . 1 1 86 86 ARG HA H 1 4.019 0.005 . 1 . . . . . . . . 5064 1 467 . 1 1 86 86 ARG C C 13 176.003 0.05 . 1 . . . . . . . . 5064 1 468 . 1 1 86 86 ARG CB C 13 30.664 0.05 . 1 . . . . . . . . 5064 1 469 . 1 1 87 87 ILE N N 15 112.804 0.05 . 1 . . . . . . . . 5064 1 470 . 1 1 87 87 ILE H H 1 7.501 0.005 . 1 . . . . . . . . 5064 1 471 . 1 1 87 87 ILE CA C 13 61.264 0.05 . 1 . . . . . . . . 5064 1 472 . 1 1 87 87 ILE HA H 1 4.157 0.005 . 1 . . . . . . . . 5064 1 473 . 1 1 87 87 ILE C C 13 175.605 0.05 . 1 . . . . . . . . 5064 1 474 . 1 1 87 87 ILE CB C 13 38.478 0.05 . 1 . . . . . . . . 5064 1 475 . 1 1 87 87 ILE HB H 1 1.734 0.005 . 1 . . . . . . . . 5064 1 476 . 1 1 87 87 ILE CG1 C 13 27.681 0.05 . 1 . . . . . . . . 5064 1 477 . 1 1 87 87 ILE HG12 H 1 0.939 0.005 . 2 . . . . . . . . 5064 1 478 . 1 1 87 87 ILE HG13 H 1 1.346 0.005 . 2 . . . . . . . . 5064 1 479 . 1 1 87 87 ILE CG2 C 13 18.261 0.05 . 1 . . . . . . . . 5064 1 480 . 1 1 87 87 ILE HG21 H 1 0.744 0.005 . 1 . . . . . . . . 5064 1 481 . 1 1 87 87 ILE HG22 H 1 0.744 0.005 . 1 . . . . . . . . 5064 1 482 . 1 1 87 87 ILE HG23 H 1 0.744 0.005 . 1 . . . . . . . . 5064 1 483 . 1 1 87 87 ILE CD1 C 13 15.217 0.05 . 1 . . . . . . . . 5064 1 484 . 1 1 87 87 ILE HD11 H 1 0.445 0.005 . 1 . . . . . . . . 5064 1 485 . 1 1 87 87 ILE HD12 H 1 0.445 0.005 . 1 . . . . . . . . 5064 1 486 . 1 1 87 87 ILE HD13 H 1 0.445 0.005 . 1 . . . . . . . . 5064 1 487 . 1 1 88 88 HIS N N 15 116.043 0.05 . 1 . . . . . . . . 5064 1 488 . 1 1 88 88 HIS H H 1 7.514 0.005 . 1 . . . . . . . . 5064 1 489 . 1 1 88 88 HIS CA C 13 56.34 0.05 . 1 . . . . . . . . 5064 1 490 . 1 1 88 88 HIS HA H 1 4.225 0.005 . 1 . . . . . . . . 5064 1 491 . 1 1 88 88 HIS C C 13 175.4 0.05 . 1 . . . . . . . . 5064 1 492 . 1 1 88 88 HIS CB C 13 26.322 0.05 . 1 . . . . . . . . 5064 1 493 . 1 1 88 88 HIS HB2 H 1 3.299 0.005 . 2 . . . . . . . . 5064 1 494 . 1 1 88 88 HIS HB3 H 1 3.513 0.005 . 2 . . . . . . . . 5064 1 495 . 1 1 89 89 LEU N N 15 119.524 0.05 . 1 . . . . . . . . 5064 1 496 . 1 1 89 89 LEU H H 1 7.803 0.005 . 1 . . . . . . . . 5064 1 497 . 1 1 89 89 LEU CA C 13 54.575 0.05 . 1 . . . . . . . . 5064 1 498 . 1 1 89 89 LEU HA H 1 4.479 0.005 . 1 . . . . . . . . 5064 1 499 . 1 1 89 89 LEU C C 13 178.786 0.05 . 1 . . . . . . . . 5064 1 500 . 1 1 89 89 LEU CB C 13 43.279 0.05 . 1 . . . . . . . . 5064 1 501 . 1 1 89 89 LEU HB2 H 1 1.394 0.005 . 2 . . . . . . . . 5064 1 502 . 1 1 89 89 LEU HB3 H 1 1.71 0.005 . 2 . . . . . . . . 5064 1 503 . 1 1 89 89 LEU CD1 C 13 26.635 0.05 . 2 . . . . . . . . 5064 1 504 . 1 1 89 89 LEU HD11 H 1 0.85 0.005 . 2 . . . . . . . . 5064 1 505 . 1 1 89 89 LEU HD12 H 1 0.85 0.005 . 2 . . . . . . . . 5064 1 506 . 1 1 89 89 LEU HD13 H 1 0.85 0.005 . 2 . . . . . . . . 5064 1 507 . 1 1 90 90 ARG N N 15 123.67 0.05 . 1 . . . . . . . . 5064 1 508 . 1 1 90 90 ARG H H 1 9.144 0.005 . 1 . . . . . . . . 5064 1 509 . 1 1 90 90 ARG CA C 13 55.288 0.05 . 1 . . . . . . . . 5064 1 510 . 1 1 90 90 ARG HA H 1 4.357 0.005 . 1 . . . . . . . . 5064 1 511 . 1 1 90 90 ARG C C 13 178.759 0.05 . 1 . . . . . . . . 5064 1 512 . 1 1 90 90 ARG CB C 13 30.964 0.05 . 1 . . . . . . . . 5064 1 513 . 1 1 91 91 ALA N N 15 125.002 0.05 . 1 . . . . . . . . 5064 1 514 . 1 1 91 91 ALA H H 1 8.816 0.005 . 1 . . . . . . . . 5064 1 515 . 1 1 91 91 ALA CA C 13 55.374 0.05 . 1 . . . . . . . . 5064 1 516 . 1 1 91 91 ALA HA H 1 4.709 0.005 . 1 . . . . . . . . 5064 1 517 . 1 1 91 91 ALA C C 13 179.598 0.05 . 1 . . . . . . . . 5064 1 518 . 1 1 91 91 ALA CB C 13 18.191 0.05 . 1 . . . . . . . . 5064 1 519 . 1 1 92 92 GLU N N 15 112.177 0.05 . 1 . . . . . . . . 5064 1 520 . 1 1 92 92 GLU H H 1 8.888 0.005 . 1 . . . . . . . . 5064 1 521 . 1 1 92 92 GLU CA C 13 57.224 0.05 . 1 . . . . . . . . 5064 1 522 . 1 1 92 92 GLU HA H 1 4.094 0.005 . 1 . . . . . . . . 5064 1 523 . 1 1 92 92 GLU C C 13 177.281 0.05 . 1 . . . . . . . . 5064 1 524 . 1 1 92 92 GLU CB C 13 29.093 0.05 . 1 . . . . . . . . 5064 1 525 . 1 1 93 93 ASP N N 15 121.613 0.05 . 1 . . . . . . . . 5064 1 526 . 1 1 93 93 ASP H H 1 7.493 0.005 . 1 . . . . . . . . 5064 1 527 . 1 1 93 93 ASP CA C 13 54.634 0.05 . 1 . . . . . . . . 5064 1 528 . 1 1 93 93 ASP HA H 1 4.631 0.005 . 1 . . . . . . . . 5064 1 529 . 1 1 93 93 ASP CB C 13 42.358 0.05 . 1 . . . . . . . . 5064 1 530 . 1 1 94 94 ALA N N 15 127.085 0.05 . 1 . . . . . . . . 5064 1 531 . 1 1 94 94 ALA H H 1 8.53 0.005 . 1 . . . . . . . . 5064 1 532 . 1 1 94 94 ALA CA C 13 52.065 0.05 . 1 . . . . . . . . 5064 1 533 . 1 1 94 94 ALA HA H 1 4.048 0.005 . 1 . . . . . . . . 5064 1 534 . 1 1 94 94 ALA C C 13 175.834 0.05 . 1 . . . . . . . . 5064 1 535 . 1 1 94 94 ALA CB C 13 20.944 0.05 . 1 . . . . . . . . 5064 1 536 . 1 1 94 94 ALA HB1 H 1 1.435 0.005 . 1 . . . . . . . . 5064 1 537 . 1 1 94 94 ALA HB2 H 1 1.435 0.005 . 1 . . . . . . . . 5064 1 538 . 1 1 94 94 ALA HB3 H 1 1.435 0.005 . 1 . . . . . . . . 5064 1 539 . 1 1 95 95 LEU N N 15 117.128 0.05 . 1 . . . . . . . . 5064 1 540 . 1 1 95 95 LEU H H 1 7.046 0.005 . 1 . . . . . . . . 5064 1 541 . 1 1 95 95 LEU CA C 13 54.843 0.05 . 1 . . . . . . . . 5064 1 542 . 1 1 95 95 LEU HA H 1 4.574 0.005 . 1 . . . . . . . . 5064 1 543 . 1 1 95 95 LEU C C 13 174.001 0.05 . 1 . . . . . . . . 5064 1 544 . 1 1 95 95 LEU CB C 13 44.792 0.05 . 1 . . . . . . . . 5064 1 545 . 1 1 95 95 LEU CD1 C 13 27.477 0.05 . 2 . . . . . . . . 5064 1 546 . 1 1 95 95 LEU HD11 H 1 0.458 0.005 . 2 . . . . . . . . 5064 1 547 . 1 1 95 95 LEU HD12 H 1 0.458 0.005 . 2 . . . . . . . . 5064 1 548 . 1 1 95 95 LEU HD13 H 1 0.458 0.005 . 2 . . . . . . . . 5064 1 549 . 1 1 95 95 LEU CD2 C 13 24.818 0.05 . 2 . . . . . . . . 5064 1 550 . 1 1 95 95 LEU HD21 H 1 0.831 0.005 . 2 . . . . . . . . 5064 1 551 . 1 1 95 95 LEU HD22 H 1 0.831 0.005 . 2 . . . . . . . . 5064 1 552 . 1 1 95 95 LEU HD23 H 1 0.831 0.005 . 2 . . . . . . . . 5064 1 553 . 1 1 95 95 LEU HB3 H 1 1.123 0.005 . 2 . . . . . . . . 5064 1 554 . 1 1 96 96 PHE N N 15 124.206 0.05 . 1 . . . . . . . . 5064 1 555 . 1 1 96 96 PHE H H 1 9.212 0.005 . 1 . . . . . . . . 5064 1 556 . 1 1 96 96 PHE CA C 13 57.067 0.05 . 1 . . . . . . . . 5064 1 557 . 1 1 96 96 PHE C C 13 174.869 0.05 . 1 . . . . . . . . 5064 1 558 . 1 1 96 96 PHE CB C 13 43.12 0.05 . 1 . . . . . . . . 5064 1 559 . 1 1 97 97 PHE N N 15 119.924 0.05 . 1 . . . . . . . . 5064 1 560 . 1 1 97 97 PHE CA C 13 52.108 0.05 . 1 . . . . . . . . 5064 1 561 . 1 1 97 97 PHE HA H 1 6.037 0.005 . 1 . . . . . . . . 5064 1 562 . 1 1 97 97 PHE C C 13 174.394 0.05 . 1 . . . . . . . . 5064 1 563 . 1 1 97 97 PHE CB C 13 41.853 0.05 . 1 . . . . . . . . 5064 1 564 . 1 1 97 97 PHE HB2 H 1 2.837 0.005 . 2 . . . . . . . . 5064 1 565 . 1 1 97 97 PHE HB3 H 1 2.912 0.005 . 2 . . . . . . . . 5064 1 566 . 1 1 98 98 PHE N N 15 112.38 0.05 . 1 . . . . . . . . 5064 1 567 . 1 1 98 98 PHE H H 1 9.107 0.005 . 1 . . . . . . . . 5064 1 568 . 1 1 98 98 PHE CA C 13 56.204 0.05 . 1 . . . . . . . . 5064 1 569 . 1 1 98 98 PHE HA H 1 5.104 0.005 . 1 . . . . . . . . 5064 1 570 . 1 1 98 98 PHE C C 13 176.226 0.05 . 1 . . . . . . . . 5064 1 571 . 1 1 98 98 PHE CB C 13 43.759 0.05 . 1 . . . . . . . . 5064 1 572 . 1 1 98 98 PHE HB2 H 1 2.662 0.005 . 2 . . . . . . . . 5064 1 573 . 1 1 98 98 PHE HB3 H 1 2.808 0.005 . 2 . . . . . . . . 5064 1 574 . 1 1 99 99 VAL N N 15 121.911 0.05 . 1 . . . . . . . . 5064 1 575 . 1 1 99 99 VAL H H 1 9.358 0.005 . 1 . . . . . . . . 5064 1 576 . 1 1 99 99 VAL CA C 13 59.714 0.05 . 1 . . . . . . . . 5064 1 577 . 1 1 99 99 VAL HA H 1 4.565 0.005 . 1 . . . . . . . . 5064 1 578 . 1 1 99 99 VAL C C 13 175.905 0.05 . 1 . . . . . . . . 5064 1 579 . 1 1 99 99 VAL CB C 13 34.156 0.05 . 1 . . . . . . . . 5064 1 580 . 1 1 99 99 VAL HB H 1 1.71 0.005 . 1 . . . . . . . . 5064 1 581 . 1 1 99 99 VAL CG1 C 13 20.838 0.05 . 2 . . . . . . . . 5064 1 582 . 1 1 99 99 VAL HG11 H 1 0.635 0.005 . 2 . . . . . . . . 5064 1 583 . 1 1 99 99 VAL HG12 H 1 0.635 0.005 . 2 . . . . . . . . 5064 1 584 . 1 1 99 99 VAL HG13 H 1 0.635 0.005 . 2 . . . . . . . . 5064 1 585 . 1 1 99 99 VAL CG2 C 13 21.767 0.05 . 2 . . . . . . . . 5064 1 586 . 1 1 99 99 VAL HG21 H 1 0.831 0.005 . 2 . . . . . . . . 5064 1 587 . 1 1 99 99 VAL HG22 H 1 0.831 0.005 . 2 . . . . . . . . 5064 1 588 . 1 1 99 99 VAL HG23 H 1 0.831 0.005 . 2 . . . . . . . . 5064 1 589 . 1 1 100 100 ASN N N 15 126.129 0.05 . 1 . . . . . . . . 5064 1 590 . 1 1 100 100 ASN H H 1 9.964 0.005 . 1 . . . . . . . . 5064 1 591 . 1 1 100 100 ASN CA C 13 55.297 0.05 . 1 . . . . . . . . 5064 1 592 . 1 1 100 100 ASN HA H 1 4.317 0.005 . 1 . . . . . . . . 5064 1 593 . 1 1 100 100 ASN C C 13 175.331 0.05 . 1 . . . . . . . . 5064 1 594 . 1 1 100 100 ASN CB C 13 37.54 0.05 . 1 . . . . . . . . 5064 1 595 . 1 1 100 100 ASN HB2 H 1 2.724 0.005 . 2 . . . . . . . . 5064 1 596 . 1 1 100 100 ASN HB3 H 1 2.979 0.005 . 2 . . . . . . . . 5064 1 597 . 1 1 101 101 ASN N N 15 106.947 0.05 . 1 . . . . . . . . 5064 1 598 . 1 1 101 101 ASN H H 1 8.139 0.005 . 1 . . . . . . . . 5064 1 599 . 1 1 101 101 ASN CA C 13 55.532 0.05 . 1 . . . . . . . . 5064 1 600 . 1 1 101 101 ASN HA H 1 4.068 0.005 . 1 . . . . . . . . 5064 1 601 . 1 1 101 101 ASN C C 13 174.44 0.05 . 1 . . . . . . . . 5064 1 602 . 1 1 101 101 ASN CB C 13 38.284 0.05 . 1 . . . . . . . . 5064 1 603 . 1 1 102 102 VAL N N 15 118.743 0.05 . 1 . . . . . . . . 5064 1 604 . 1 1 102 102 VAL H H 1 8.237 0.005 . 1 . . . . . . . . 5064 1 605 . 1 1 102 102 VAL CA C 13 60.57 0.05 . 1 . . . . . . . . 5064 1 606 . 1 1 102 102 VAL HA H 1 4.703 0.005 . 1 . . . . . . . . 5064 1 607 . 1 1 102 102 VAL CB C 13 35.185 0.05 . 1 . . . . . . . . 5064 1 608 . 1 1 102 102 VAL HB H 1 2.217 0.005 . 1 . . . . . . . . 5064 1 609 . 1 1 102 102 VAL CG2 C 13 20.088 0.05 . 2 . . . . . . . . 5064 1 610 . 1 1 102 102 VAL HG21 H 1 0.98 0.005 . 2 . . . . . . . . 5064 1 611 . 1 1 102 102 VAL HG22 H 1 0.98 0.005 . 2 . . . . . . . . 5064 1 612 . 1 1 102 102 VAL HG23 H 1 0.98 0.005 . 2 . . . . . . . . 5064 1 613 . 1 1 103 103 ILE N N 15 126.972 0.05 . 1 . . . . . . . . 5064 1 614 . 1 1 103 103 ILE H H 1 8.53 0.005 . 1 . . . . . . . . 5064 1 615 . 1 1 103 103 ILE CA C 13 58.31 0.05 . 1 . . . . . . . . 5064 1 616 . 1 1 103 103 ILE HA H 1 5.209 0.005 . 1 . . . . . . . . 5064 1 617 . 1 1 103 103 ILE CB C 13 39.008 0.05 . 1 . . . . . . . . 5064 1 618 . 1 1 103 103 ILE HB H 1 1.765 0.005 . 1 . . . . . . . . 5064 1 619 . 1 1 103 103 ILE CG2 C 13 16.833 0.05 . 1 . . . . . . . . 5064 1 620 . 1 1 103 103 ILE HG21 H 1 1.166 0.005 . 1 . . . . . . . . 5064 1 621 . 1 1 103 103 ILE HG22 H 1 1.166 0.005 . 1 . . . . . . . . 5064 1 622 . 1 1 103 103 ILE HG23 H 1 1.166 0.005 . 1 . . . . . . . . 5064 1 623 . 1 1 103 103 ILE CD1 C 13 13.776 0.05 . 1 . . . . . . . . 5064 1 624 . 1 1 103 103 ILE HD11 H 1 0.832 0.005 . 1 . . . . . . . . 5064 1 625 . 1 1 103 103 ILE HD12 H 1 0.832 0.005 . 1 . . . . . . . . 5064 1 626 . 1 1 103 103 ILE HD13 H 1 0.832 0.005 . 1 . . . . . . . . 5064 1 627 . 1 1 103 103 ILE HG12 H 1 1.543 0.005 . 2 . . . . . . . . 5064 1 628 . 1 1 105 105 PRO CA C 13 62.067 0.05 . 1 . . . . . . . . 5064 1 629 . 1 1 105 105 PRO C C 13 178.979 0.05 . 1 . . . . . . . . 5064 1 630 . 1 1 105 105 PRO CB C 13 32.091 0.05 . 1 . . . . . . . . 5064 1 631 . 1 1 106 106 THR N N 15 113.672 0.05 . 1 . . . . . . . . 5064 1 632 . 1 1 106 106 THR H H 1 8.629 0.005 . 1 . . . . . . . . 5064 1 633 . 1 1 106 106 THR CA C 13 64.781 0.05 . 1 . . . . . . . . 5064 1 634 . 1 1 106 106 THR HA H 1 3.862 0.005 . 1 . . . . . . . . 5064 1 635 . 1 1 106 106 THR C C 13 176.17 0.05 . 1 . . . . . . . . 5064 1 636 . 1 1 106 106 THR CB C 13 68.718 0.05 . 1 . . . . . . . . 5064 1 637 . 1 1 106 106 THR HB H 1 4.241 0.005 . 1 . . . . . . . . 5064 1 638 . 1 1 106 106 THR CG2 C 13 23.003 0.05 . 1 . . . . . . . . 5064 1 639 . 1 1 106 106 THR HG21 H 1 1.368 0.005 . 1 . . . . . . . . 5064 1 640 . 1 1 106 106 THR HG22 H 1 1.368 0.005 . 1 . . . . . . . . 5064 1 641 . 1 1 106 106 THR HG23 H 1 1.368 0.005 . 1 . . . . . . . . 5064 1 642 . 1 1 107 107 SER N N 15 111.165 0.05 . 1 . . . . . . . . 5064 1 643 . 1 1 107 107 SER H H 1 7.816 0.005 . 1 . . . . . . . . 5064 1 644 . 1 1 107 107 SER CA C 13 57.876 0.05 . 1 . . . . . . . . 5064 1 645 . 1 1 107 107 SER HA H 1 4.444 0.005 . 1 . . . . . . . . 5064 1 646 . 1 1 107 107 SER C C 13 175.904 0.05 . 1 . . . . . . . . 5064 1 647 . 1 1 107 107 SER CB C 13 63.655 0.05 . 1 . . . . . . . . 5064 1 648 . 1 1 107 107 SER HB2 H 1 3.912 0.005 . 2 . . . . . . . . 5064 1 649 . 1 1 107 107 SER HB3 H 1 4.113 0.005 . 2 . . . . . . . . 5064 1 650 . 1 1 108 108 ALA N N 15 124.985 0.05 . 1 . . . . . . . . 5064 1 651 . 1 1 108 108 ALA H H 1 7.285 0.005 . 1 . . . . . . . . 5064 1 652 . 1 1 108 108 ALA CA C 13 52.264 0.05 . 1 . . . . . . . . 5064 1 653 . 1 1 108 108 ALA HA H 1 4.511 0.005 . 1 . . . . . . . . 5064 1 654 . 1 1 108 108 ALA C C 13 177.592 0.05 . 1 . . . . . . . . 5064 1 655 . 1 1 108 108 ALA CB C 13 19.146 0.05 . 1 . . . . . . . . 5064 1 656 . 1 1 108 108 ALA HB1 H 1 1.523 0.005 . 1 . . . . . . . . 5064 1 657 . 1 1 108 108 ALA HB2 H 1 1.523 0.005 . 1 . . . . . . . . 5064 1 658 . 1 1 108 108 ALA HB3 H 1 1.523 0.005 . 1 . . . . . . . . 5064 1 659 . 1 1 109 109 THR N N 15 108.767 0.05 . 1 . . . . . . . . 5064 1 660 . 1 1 109 109 THR H H 1 8.231 0.005 . 1 . . . . . . . . 5064 1 661 . 1 1 109 109 THR CA C 13 59.904 0.05 . 1 . . . . . . . . 5064 1 662 . 1 1 109 109 THR HA H 1 4.928 0.005 . 1 . . . . . . . . 5064 1 663 . 1 1 109 109 THR C C 13 176.906 0.05 . 1 . . . . . . . . 5064 1 664 . 1 1 109 109 THR CB C 13 70.714 0.05 . 1 . . . . . . . . 5064 1 665 . 1 1 109 109 THR HB H 1 4.903 0.005 . 1 . . . . . . . . 5064 1 666 . 1 1 109 109 THR CG2 C 13 21.993 0.05 . 1 . . . . . . . . 5064 1 667 . 1 1 109 109 THR HG21 H 1 1.223 0.005 . 1 . . . . . . . . 5064 1 668 . 1 1 109 109 THR HG22 H 1 1.223 0.005 . 1 . . . . . . . . 5064 1 669 . 1 1 109 109 THR HG23 H 1 1.223 0.005 . 1 . . . . . . . . 5064 1 670 . 1 1 110 110 MET N N 15 120.021 0.05 . 1 . . . . . . . . 5064 1 671 . 1 1 110 110 MET H H 1 9.391 0.005 . 1 . . . . . . . . 5064 1 672 . 1 1 110 110 MET CA C 13 55.815 0.05 . 1 . . . . . . . . 5064 1 673 . 1 1 110 110 MET HA H 1 4.883 0.005 . 1 . . . . . . . . 5064 1 674 . 1 1 110 110 MET C C 13 180.245 0.05 . 1 . . . . . . . . 5064 1 675 . 1 1 110 110 MET CB C 13 28.557 0.05 . 1 . . . . . . . . 5064 1 676 . 1 1 111 111 GLY N N 15 108.097 0.05 . 1 . . . . . . . . 5064 1 677 . 1 1 111 111 GLY H H 1 9.506 0.005 . 1 . . . . . . . . 5064 1 678 . 1 1 111 111 GLY CA C 13 47.065 0.05 . 1 . . . . . . . . 5064 1 679 . 1 1 111 111 GLY HA2 H 1 3.72 0.005 . 2 . . . . . . . . 5064 1 680 . 1 1 111 111 GLY HA3 H 1 4.04 0.005 . 2 . . . . . . . . 5064 1 681 . 1 1 111 111 GLY C C 13 177.116 0.05 . 1 . . . . . . . . 5064 1 682 . 1 1 112 112 GLN N N 15 124.43 0.05 . 1 . . . . . . . . 5064 1 683 . 1 1 112 112 GLN H H 1 8.024 0.005 . 1 . . . . . . . . 5064 1 684 . 1 1 112 112 GLN CA C 13 58.815 0.05 . 1 . . . . . . . . 5064 1 685 . 1 1 112 112 GLN HA H 1 4.137 0.005 . 1 . . . . . . . . 5064 1 686 . 1 1 112 112 GLN C C 13 180.108 0.05 . 1 . . . . . . . . 5064 1 687 . 1 1 112 112 GLN CB C 13 28.173 0.05 . 1 . . . . . . . . 5064 1 688 . 1 1 112 112 GLN HB2 H 1 2.131 0.005 . 2 . . . . . . . . 5064 1 689 . 1 1 112 112 GLN HB3 H 1 2.398 0.005 . 2 . . . . . . . . 5064 1 690 . 1 1 112 112 GLN HG2 H 1 2.453 0.005 . 2 . . . . . . . . 5064 1 691 . 1 1 113 113 LEU N N 15 120.805 0.05 . 1 . . . . . . . . 5064 1 692 . 1 1 113 113 LEU H H 1 8.478 0.005 . 1 . . . . . . . . 5064 1 693 . 1 1 113 113 LEU CA C 13 57.754 0.05 . 1 . . . . . . . . 5064 1 694 . 1 1 113 113 LEU HA H 1 4.269 0.005 . 1 . . . . . . . . 5064 1 695 . 1 1 113 113 LEU C C 13 179.574 0.05 . 1 . . . . . . . . 5064 1 696 . 1 1 113 113 LEU CB C 13 42.723 0.05 . 1 . . . . . . . . 5064 1 697 . 1 1 113 113 LEU HB2 H 1 1.644 0.005 . 2 . . . . . . . . 5064 1 698 . 1 1 113 113 LEU HB3 H 1 1.815 0.005 . 2 . . . . . . . . 5064 1 699 . 1 1 113 113 LEU CD1 C 13 24.322 0.05 . 2 . . . . . . . . 5064 1 700 . 1 1 113 113 LEU HD11 H 1 0.9 0.005 . 2 . . . . . . . . 5064 1 701 . 1 1 113 113 LEU HD12 H 1 0.9 0.005 . 2 . . . . . . . . 5064 1 702 . 1 1 113 113 LEU HD13 H 1 0.9 0.005 . 2 . . . . . . . . 5064 1 703 . 1 1 114 114 TYR N N 15 118.67 0.05 . 1 . . . . . . . . 5064 1 704 . 1 1 114 114 TYR H H 1 9.04 0.005 . 1 . . . . . . . . 5064 1 705 . 1 1 114 114 TYR CA C 13 63.094 0.05 . 1 . . . . . . . . 5064 1 706 . 1 1 114 114 TYR HA H 1 3.862 0.005 . 1 . . . . . . . . 5064 1 707 . 1 1 114 114 TYR C C 13 178.63 0.05 . 1 . . . . . . . . 5064 1 708 . 1 1 114 114 TYR CB C 13 39.622 0.05 . 1 . . . . . . . . 5064 1 709 . 1 1 114 114 TYR HB2 H 1 3.066 0.005 . 2 . . . . . . . . 5064 1 710 . 1 1 114 114 TYR HB3 H 1 3.327 0.005 . 2 . . . . . . . . 5064 1 711 . 1 1 115 115 GLN N N 15 119.182 0.05 . 1 . . . . . . . . 5064 1 712 . 1 1 115 115 GLN H H 1 8.387 0.005 . 1 . . . . . . . . 5064 1 713 . 1 1 115 115 GLN CA C 13 59.172 0.05 . 1 . . . . . . . . 5064 1 714 . 1 1 115 115 GLN C C 13 177.846 0.05 . 1 . . . . . . . . 5064 1 715 . 1 1 115 115 GLN CB C 13 28.506 0.05 . 1 . . . . . . . . 5064 1 716 . 1 1 116 116 GLU N N 15 114.95 0.05 . 1 . . . . . . . . 5064 1 717 . 1 1 116 116 GLU H H 1 7.419 0.005 . 1 . . . . . . . . 5064 1 718 . 1 1 116 116 GLU CA C 13 58.069 0.05 . 1 . . . . . . . . 5064 1 719 . 1 1 116 116 GLU HA H 1 3.98 0.005 . 1 . . . . . . . . 5064 1 720 . 1 1 116 116 GLU C C 13 178.737 0.05 . 1 . . . . . . . . 5064 1 721 . 1 1 116 116 GLU CB C 13 31.384 0.05 . 1 . . . . . . . . 5064 1 722 . 1 1 116 116 GLU HB2 H 1 1.518 0.005 . 2 . . . . . . . . 5064 1 723 . 1 1 116 116 GLU HB3 H 1 1.836 0.005 . 2 . . . . . . . . 5064 1 724 . 1 1 116 116 GLU HG3 H 1 2.055 0.005 . 2 . . . . . . . . 5064 1 725 . 1 1 117 117 HIS N N 15 112.267 0.05 . 1 . . . . . . . . 5064 1 726 . 1 1 117 117 HIS H H 1 8.136 0.005 . 1 . . . . . . . . 5064 1 727 . 1 1 117 117 HIS CA C 13 56.696 0.05 . 1 . . . . . . . . 5064 1 728 . 1 1 117 117 HIS HA H 1 4.735 0.005 . 1 . . . . . . . . 5064 1 729 . 1 1 117 117 HIS C C 13 177.859 0.05 . 1 . . . . . . . . 5064 1 730 . 1 1 117 117 HIS CB C 13 33.831 0.05 . 1 . . . . . . . . 5064 1 731 . 1 1 117 117 HIS HB2 H 1 2.811 0.005 . 2 . . . . . . . . 5064 1 732 . 1 1 117 117 HIS HB3 H 1 3.073 0.005 . 2 . . . . . . . . 5064 1 733 . 1 1 118 118 HIS N N 15 119.606 0.05 . 1 . . . . . . . . 5064 1 734 . 1 1 118 118 HIS H H 1 8.485 0.005 . 1 . . . . . . . . 5064 1 735 . 1 1 118 118 HIS CA C 13 57.255 0.05 . 1 . . . . . . . . 5064 1 736 . 1 1 118 118 HIS CB C 13 26.812 0.05 . 1 . . . . . . . . 5064 1 737 . 1 1 119 119 GLU CA C 13 55.903 0.05 . 1 . . . . . . . . 5064 1 738 . 1 1 119 119 GLU C C 13 175.572 0.05 . 1 . . . . . . . . 5064 1 739 . 1 1 120 120 GLU N N 15 120.776 0.05 . 1 . . . . . . . . 5064 1 740 . 1 1 120 120 GLU H H 1 8.212 0.005 . 1 . . . . . . . . 5064 1 741 . 1 1 120 120 GLU CA C 13 55.225 0.05 . 1 . . . . . . . . 5064 1 742 . 1 1 120 120 GLU HA H 1 4.227 0.005 . 1 . . . . . . . . 5064 1 743 . 1 1 120 120 GLU C C 13 175.611 0.05 . 1 . . . . . . . . 5064 1 744 . 1 1 120 120 GLU CB C 13 33.861 0.05 . 1 . . . . . . . . 5064 1 745 . 1 1 121 121 ASP N N 15 123.955 0.05 . 1 . . . . . . . . 5064 1 746 . 1 1 121 121 ASP H H 1 8.641 0.005 . 1 . . . . . . . . 5064 1 747 . 1 1 121 121 ASP CA C 13 57.381 0.05 . 1 . . . . . . . . 5064 1 748 . 1 1 121 121 ASP HA H 1 4.755 0.005 . 1 . . . . . . . . 5064 1 749 . 1 1 121 121 ASP C C 13 177.662 0.05 . 1 . . . . . . . . 5064 1 750 . 1 1 121 121 ASP CB C 13 40.71 0.05 . 1 . . . . . . . . 5064 1 751 . 1 1 123 123 PHE CA C 13 59.333 0.05 . 1 . . . . . . . . 5064 1 752 . 1 1 123 123 PHE C C 13 175.172 0.05 . 1 . . . . . . . . 5064 1 753 . 1 1 124 124 LEU N N 15 121.769 0.05 . 1 . . . . . . . . 5064 1 754 . 1 1 124 124 LEU H H 1 7.858 0.005 . 1 . . . . . . . . 5064 1 755 . 1 1 124 124 LEU CA C 13 53.155 0.05 . 1 . . . . . . . . 5064 1 756 . 1 1 124 124 LEU HA H 1 4.733 0.005 . 1 . . . . . . . . 5064 1 757 . 1 1 124 124 LEU C C 13 173.47 0.05 . 1 . . . . . . . . 5064 1 758 . 1 1 124 124 LEU CB C 13 46.053 0.05 . 1 . . . . . . . . 5064 1 759 . 1 1 124 124 LEU HB2 H 1 1.38 0.005 . 2 . . . . . . . . 5064 1 760 . 1 1 124 124 LEU HB3 H 1 2.065 0.005 . 2 . . . . . . . . 5064 1 761 . 1 1 124 124 LEU HG H 1 1.695 0.005 . 1 . . . . . . . . 5064 1 762 . 1 1 124 124 LEU CD1 C 13 26.83 0.05 . 2 . . . . . . . . 5064 1 763 . 1 1 124 124 LEU HD11 H 1 0.771 0.005 . 2 . . . . . . . . 5064 1 764 . 1 1 124 124 LEU HD12 H 1 0.771 0.005 . 2 . . . . . . . . 5064 1 765 . 1 1 124 124 LEU HD13 H 1 0.771 0.005 . 2 . . . . . . . . 5064 1 766 . 1 1 124 124 LEU CD2 C 13 24.79 0.05 . 2 . . . . . . . . 5064 1 767 . 1 1 124 124 LEU HD21 H 1 0.9 0.005 . 2 . . . . . . . . 5064 1 768 . 1 1 124 124 LEU HD22 H 1 0.9 0.005 . 2 . . . . . . . . 5064 1 769 . 1 1 124 124 LEU HD23 H 1 0.9 0.005 . 2 . . . . . . . . 5064 1 770 . 1 1 125 125 TYR N N 15 127.017 0.05 . 1 . . . . . . . . 5064 1 771 . 1 1 125 125 TYR H H 1 8.931 0.005 . 1 . . . . . . . . 5064 1 772 . 1 1 125 125 TYR CA C 13 57.781 0.05 . 1 . . . . . . . . 5064 1 773 . 1 1 125 125 TYR HA H 1 4.668 0.005 . 1 . . . . . . . . 5064 1 774 . 1 1 125 125 TYR C C 13 175.65 0.05 . 1 . . . . . . . . 5064 1 775 . 1 1 125 125 TYR CB C 13 38.751 0.05 . 1 . . . . . . . . 5064 1 776 . 1 1 126 126 ILE N N 15 123.577 0.05 . 1 . . . . . . . . 5064 1 777 . 1 1 126 126 ILE H H 1 9.381 0.005 . 1 . . . . . . . . 5064 1 778 . 1 1 126 126 ILE CA C 13 59.76 0.05 . 1 . . . . . . . . 5064 1 779 . 1 1 126 126 ILE HA H 1 4.858 0.005 . 1 . . . . . . . . 5064 1 780 . 1 1 126 126 ILE C C 13 175.188 0.05 . 1 . . . . . . . . 5064 1 781 . 1 1 126 126 ILE CB C 13 41.547 0.05 . 1 . . . . . . . . 5064 1 782 . 1 1 126 126 ILE HB H 1 1.539 0.005 . 1 . . . . . . . . 5064 1 783 . 1 1 126 126 ILE CG1 C 13 27.96 0.05 . 1 . . . . . . . . 5064 1 784 . 1 1 126 126 ILE HG12 H 1 0.832 0.005 . 2 . . . . . . . . 5064 1 785 . 1 1 126 126 ILE HG13 H 1 1.315 0.005 . 2 . . . . . . . . 5064 1 786 . 1 1 126 126 ILE CG2 C 13 16.909 0.05 . 1 . . . . . . . . 5064 1 787 . 1 1 126 126 ILE HG21 H 1 0.461 0.005 . 1 . . . . . . . . 5064 1 788 . 1 1 126 126 ILE HG22 H 1 0.461 0.005 . 1 . . . . . . . . 5064 1 789 . 1 1 126 126 ILE HG23 H 1 0.461 0.005 . 1 . . . . . . . . 5064 1 790 . 1 1 126 126 ILE CD1 C 13 13.296 0.05 . 1 . . . . . . . . 5064 1 791 . 1 1 126 126 ILE HD11 H 1 0.31 0.005 . 1 . . . . . . . . 5064 1 792 . 1 1 126 126 ILE HD12 H 1 0.31 0.005 . 1 . . . . . . . . 5064 1 793 . 1 1 126 126 ILE HD13 H 1 0.31 0.005 . 1 . . . . . . . . 5064 1 794 . 1 1 127 127 ALA N N 15 127.935 0.05 . 1 . . . . . . . . 5064 1 795 . 1 1 127 127 ALA H H 1 9.076 0.005 . 1 . . . . . . . . 5064 1 796 . 1 1 127 127 ALA CA C 13 48.861 0.05 . 1 . . . . . . . . 5064 1 797 . 1 1 127 127 ALA HA H 1 6.514 0.005 . 1 . . . . . . . . 5064 1 798 . 1 1 127 127 ALA C C 13 178.287 0.05 . 1 . . . . . . . . 5064 1 799 . 1 1 127 127 ALA CB C 13 23.381 0.05 . 1 . . . . . . . . 5064 1 800 . 1 1 127 127 ALA HB1 H 1 1.564 0.005 . 1 . . . . . . . . 5064 1 801 . 1 1 127 127 ALA HB2 H 1 1.564 0.005 . 1 . . . . . . . . 5064 1 802 . 1 1 127 127 ALA HB3 H 1 1.564 0.005 . 1 . . . . . . . . 5064 1 803 . 1 1 128 128 TYR N N 15 115.771 0.05 . 1 . . . . . . . . 5064 1 804 . 1 1 128 128 TYR H H 1 8.528 0.005 . 1 . . . . . . . . 5064 1 805 . 1 1 128 128 TYR CA C 13 55.027 0.05 . 1 . . . . . . . . 5064 1 806 . 1 1 128 128 TYR HA H 1 6.73 0.005 . 1 . . . . . . . . 5064 1 807 . 1 1 128 128 TYR C C 13 174.387 0.05 . 1 . . . . . . . . 5064 1 808 . 1 1 128 128 TYR CB C 13 42.918 0.05 . 1 . . . . . . . . 5064 1 809 . 1 1 128 128 TYR HB2 H 1 2.853 0.005 . 2 . . . . . . . . 5064 1 810 . 1 1 128 128 TYR HB3 H 1 3.274 0.005 . 2 . . . . . . . . 5064 1 811 . 1 1 129 129 SER N N 15 112.368 0.05 . 1 . . . . . . . . 5064 1 812 . 1 1 129 129 SER CA C 13 55.966 0.05 . 1 . . . . . . . . 5064 1 813 . 1 1 129 129 SER C C 13 173.059 0.05 . 1 . . . . . . . . 5064 1 814 . 1 1 129 129 SER HA H 1 4.652 0.005 . 1 . . . . . . . . 5064 1 815 . 1 1 129 129 SER CB C 13 65.162 0.05 . 1 . . . . . . . . 5064 1 816 . 1 1 129 129 SER HB2 H 1 4.268 0.005 . 2 . . . . . . . . 5064 1 817 . 1 1 130 130 ASP N N 15 120.193 0.05 . 1 . . . . . . . . 5064 1 818 . 1 1 130 130 ASP H H 1 9.466 0.005 . 1 . . . . . . . . 5064 1 819 . 1 1 130 130 ASP CA C 13 53.994 0.05 . 1 . . . . . . . . 5064 1 820 . 1 1 130 130 ASP HA H 1 4.835 0.005 . 1 . . . . . . . . 5064 1 821 . 1 1 130 130 ASP C C 13 175.635 0.05 . 1 . . . . . . . . 5064 1 822 . 1 1 130 130 ASP CB C 13 40.891 0.05 . 1 . . . . . . . . 5064 1 823 . 1 1 130 130 ASP HB2 H 1 3.074 0.005 . 2 . . . . . . . . 5064 1 824 . 1 1 131 131 GLU N N 15 119.224 0.05 . 1 . . . . . . . . 5064 1 825 . 1 1 131 131 GLU H H 1 8.569 0.005 . 1 . . . . . . . . 5064 1 826 . 1 1 131 131 GLU CA C 13 55.035 0.05 . 1 . . . . . . . . 5064 1 827 . 1 1 131 131 GLU HA H 1 4.629 0.005 . 1 . . . . . . . . 5064 1 828 . 1 1 131 131 GLU C C 13 175.698 0.05 . 1 . . . . . . . . 5064 1 829 . 1 1 131 131 GLU CB C 13 33.322 0.05 . 1 . . . . . . . . 5064 1 830 . 1 1 132 132 SER N N 15 112.192 0.05 . 1 . . . . . . . . 5064 1 831 . 1 1 132 132 SER H H 1 7.995 0.005 . 1 . . . . . . . . 5064 1 832 . 1 1 132 132 SER CA C 13 58.31 0.05 . 1 . . . . . . . . 5064 1 833 . 1 1 132 132 SER HA H 1 3.376 0.005 . 1 . . . . . . . . 5064 1 834 . 1 1 132 132 SER C C 13 174.04 0.05 . 1 . . . . . . . . 5064 1 835 . 1 1 132 132 SER CB C 13 62.729 0.05 . 1 . . . . . . . . 5064 1 836 . 1 1 132 132 SER HB2 H 1 2.461 0.005 . 2 . . . . . . . . 5064 1 837 . 1 1 132 132 SER HB3 H 1 3.494 0.005 . 2 . . . . . . . . 5064 1 838 . 1 1 133 133 VAL N N 15 118.985 0.05 . 1 . . . . . . . . 5064 1 839 . 1 1 133 133 VAL H H 1 6.988 0.005 . 1 . . . . . . . . 5064 1 840 . 1 1 133 133 VAL CA C 13 61.069 0.05 . 1 . . . . . . . . 5064 1 841 . 1 1 133 133 VAL HA H 1 4.16 0.005 . 1 . . . . . . . . 5064 1 842 . 1 1 133 133 VAL C C 13 175.297 0.05 . 1 . . . . . . . . 5064 1 843 . 1 1 133 133 VAL CB C 13 34.24 0.05 . 1 . . . . . . . . 5064 1 844 . 1 1 133 133 VAL HB H 1 1.818 0.005 . 1 . . . . . . . . 5064 1 845 . 1 1 133 133 VAL CG1 C 13 20.484 0.05 . 2 . . . . . . . . 5064 1 846 . 1 1 133 133 VAL HG11 H 1 0.753 0.005 . 2 . . . . . . . . 5064 1 847 . 1 1 133 133 VAL HG12 H 1 0.753 0.005 . 2 . . . . . . . . 5064 1 848 . 1 1 133 133 VAL HG13 H 1 0.753 0.005 . 2 . . . . . . . . 5064 1 849 . 1 1 133 133 VAL CG2 C 13 21 0.05 . 2 . . . . . . . . 5064 1 850 . 1 1 133 133 VAL HG21 H 1 0.756 0.005 . 2 . . . . . . . . 5064 1 851 . 1 1 133 133 VAL HG22 H 1 0.756 0.005 . 2 . . . . . . . . 5064 1 852 . 1 1 133 133 VAL HG23 H 1 0.756 0.005 . 2 . . . . . . . . 5064 1 853 . 1 1 134 134 TYR N N 15 127.374 0.05 . 1 . . . . . . . . 5064 1 854 . 1 1 134 134 TYR H H 1 8.279 0.005 . 1 . . . . . . . . 5064 1 855 . 1 1 134 134 TYR CA C 13 58.798 0.05 . 1 . . . . . . . . 5064 1 856 . 1 1 134 134 TYR HA H 1 3.684 0.005 . 1 . . . . . . . . 5064 1 857 . 1 1 134 134 TYR C C 13 178.544 0.05 . 1 . . . . . . . . 5064 1 858 . 1 1 134 134 TYR CB C 13 38.042 0.05 . 1 . . . . . . . . 5064 1 859 . 1 1 135 135 GLY N N 15 112.645 0.05 . 1 . . . . . . . . 5064 1 860 . 1 1 135 135 GLY H H 1 7.492 0.005 . 1 . . . . . . . . 5064 1 861 . 1 1 135 135 GLY CA C 13 45.127 0.05 . 1 . . . . . . . . 5064 1 862 . 1 1 135 135 GLY HA2 H 1 3.589 0.005 . 2 . . . . . . . . 5064 1 863 . 1 1 135 135 GLY HA3 H 1 3.688 0.005 . 2 . . . . . . . . 5064 1 864 . 1 1 135 135 GLY C C 13 172.661 0.05 . 1 . . . . . . . . 5064 1 865 . 1 1 136 136 LEU N N 15 126.912 0.05 . 1 . . . . . . . . 5064 1 866 . 1 1 136 136 LEU H H 1 7.467 0.005 . 1 . . . . . . . . 5064 1 867 . 1 1 136 136 LEU CA C 13 56.24 0.05 . 1 . . . . . . . . 5064 1 868 . 1 1 136 136 LEU HA H 1 4.078 0.005 . 1 . . . . . . . . 5064 1 869 . 1 1 136 136 LEU C C 13 174.286 0.05 . 1 . . . . . . . . 5064 1 870 . 1 1 136 136 LEU CB C 13 43.56 0.05 . 1 . . . . . . . . 5064 1 871 . 1 1 136 136 LEU HB3 H 1 1.492 0.005 . 2 . . . . . . . . 5064 1 872 . 1 1 136 136 LEU CD1 C 13 25.189 0.05 . 2 . . . . . . . . 5064 1 873 . 1 1 136 136 LEU HD11 H 1 0.823 0.005 . 2 . . . . . . . . 5064 1 874 . 1 1 136 136 LEU HD12 H 1 0.823 0.005 . 2 . . . . . . . . 5064 1 875 . 1 1 136 136 LEU HD13 H 1 0.823 0.005 . 2 . . . . . . . . 5064 1 stop_ save_