data_25046 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Backbone 1H, 15N Chemical Shift Assignments of the DC-SIGNR carbohydrate recognition domain in the Apo state. ; _BMRB_accession_number 25046 _BMRB_flat_file_name bmr25046.str _Entry_type original _Submission_date 2014-06-25 _Accession_date 2014-06-25 _Entry_origination author _NMR_STAR_version 2.1.1 _Experimental_method NMR _Details . loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Probert Fay . . 2 Dixon Ann . . 3 Mitchell Dan . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 84 "15N chemical shifts" 84 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2014-07-25 original author . stop_ loop_ _Related_BMRB_accession_number _Relationship 19297 'Assignment of DC-SIGNR carbohydrate recognition domain in holo (calcium bound) state.' stop_ _Original_release_date 2014-07-25 save_ ############################# # Citation for this entry # ############################# save_DC-SIGNR_apo_assignment_citation _Saveframe_category entry_citation _Citation_full . _Citation_title 'NMR evidence for oligosaccharide release from the DC-SIGNR (CLEC4M) carbohydrate recognition domain at low pH' _Citation_status 'in press' _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID ? loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Probert Fay . . 2 Dixon Ann . . 3 Mitchell Dan . . stop_ _Journal_abbreviation 'FEBS J.' _Journal_volume . _Journal_issue . _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first . _Page_last . _Year . _Details . save_ ####################################### # Cited references within the entry # ####################################### save_DC-SIGNR_holo_assignment_and_ligand_binding_citation _Saveframe_category citation _Citation_full . _Citation_title 'Solution NMR analyses of the C-type carbohydrate recognition domain of DC-SIGNR protein reveal different binding modes for HIV-derived oligosaccharides and smaller glycan fragments.' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 23788638 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Probert Fay . . 2 Dixon Ann M. . 3 Mitchell Dan A. . 4 Whittaker Sara B-M . 5 Crispin Max . . stop_ _Journal_abbreviation 'Biochem. J.' _Journal_name_full . _Journal_volume . _Journal_issue . _Journal_CSD . _Book_title . _Book_chapter_title . _Book_volume . _Book_series . _Book_publisher . _Book_publisher_city . _Book_ISBN . _Conference_title . _Conference_site . _Conference_state_province . _Conference_country . _Conference_start_date . _Conference_end_date . _Conference_abstract_number . _Thesis_institution . _Thesis_institution_city . _Thesis_institution_country . _Page_first . _Page_last . _Year . _Details . save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name 'DC-SIGNR CRD apo' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'DC-SIGNR CRD' $DC-SIGNR stop_ _System_molecular_weight 16194.7 _System_physical_state native _System_oligomer_state ? _System_paramagnetic no _System_thiol_state . _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_DC-SIGNR _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common DC-SIGNR _Molecular_mass 16194.7 _Mol_thiol_state 'not available' loop_ _Biological_function ; Probable pathogen-recognition receptor involved in peripheral immune surveillance in liver. May mediate the endocytosis of pathogens which are subsequently degraded in lysosomal compartments. Probably recognizes in a calcium-dependent manner high mannose N-linked oligosaccharides in a variety of pathogen antigens, including HIV-1 gp120, HIV-2 gp120, SIV gp120, ebolavirus glycoproteins, HCV E2, and human SARS coronavirus protein S. Is a receptor for ICAM3, probably by binding to mannose-like carbohydrates. Is presumably a coreceptor for the SARS coronavirus. ; stop_ _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 139 _Mol_residue_sequence ; AERLCRHCPKDWTFFQGNCY FMSNSQRNWHDSVTACQEVR AQLVVIKTAEEQNFLQLQTS RSNRFSWMGLSDLNQEGTWQ WVDGSPLSPSFQRYWNSGEP NNSGNEDCAEFSGSGWNDNR CDVDNYWICKKPAACFRDE ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 1 ALA 2 2 GLU 3 3 ARG 4 4 LEU 5 5 CYS 6 6 ARG 7 7 HIS 8 8 CYS 9 9 PRO 10 10 LYS 11 11 ASP 12 12 TRP 13 13 THR 14 14 PHE 15 15 PHE 16 16 GLN 17 17 GLY 18 18 ASN 19 19 CYS 20 20 TYR 21 21 PHE 22 22 MET 23 23 SER 24 24 ASN 25 25 SER 26 26 GLN 27 27 ARG 28 28 ASN 29 29 TRP 30 30 HIS 31 31 ASP 32 32 SER 33 33 VAL 34 34 THR 35 35 ALA 36 36 CYS 37 37 GLN 38 38 GLU 39 39 VAL 40 40 ARG 41 41 ALA 42 42 GLN 43 43 LEU 44 44 VAL 45 45 VAL 46 46 ILE 47 47 LYS 48 48 THR 49 49 ALA 50 50 GLU 51 51 GLU 52 52 GLN 53 53 ASN 54 54 PHE 55 55 LEU 56 56 GLN 57 57 LEU 58 58 GLN 59 59 THR 60 60 SER 61 61 ARG 62 62 SER 63 63 ASN 64 64 ARG 65 65 PHE 66 66 SER 67 67 TRP 68 68 MET 69 69 GLY 70 70 LEU 71 71 SER 72 72 ASP 73 73 LEU 74 74 ASN 75 75 GLN 76 76 GLU 77 77 GLY 78 78 THR 79 79 TRP 80 80 GLN 81 81 TRP 82 82 VAL 83 83 ASP 84 84 GLY 85 85 SER 86 86 PRO 87 87 LEU 88 88 SER 89 89 PRO 90 90 SER 91 91 PHE 92 92 GLN 93 93 ARG 94 94 TYR 95 95 TRP 96 96 ASN 97 97 SER 98 98 GLY 99 99 GLU 100 100 PRO 101 101 ASN 102 102 ASN 103 103 SER 104 104 GLY 105 105 ASN 106 106 GLU 107 107 ASP 108 108 CYS 109 109 ALA 110 110 GLU 111 111 PHE 112 112 SER 113 113 GLY 114 114 SER 115 115 GLY 116 116 TRP 117 117 ASN 118 118 ASP 119 119 ASN 120 120 ARG 121 121 CYS 122 122 ASP 123 123 VAL 124 124 ASP 125 125 ASN 126 126 TYR 127 127 TRP 128 128 ILE 129 129 CYS 130 130 LYS 131 131 LYS 132 132 PRO 133 133 ALA 134 134 ALA 135 135 CYS 136 136 PHE 137 137 ARG 138 138 ASP 139 139 GLU stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-08-05 loop_ _Database_name _Database_accession_code _Database_entry_mol_name _Sequence_query_to_submitted_percentage _Sequence_subject_length _Sequence_identity _Sequence_positive _Sequence_homology_expectation_value BMRB 19297 DC-SIGNR_carbohydrate_recognition_domain 100.00 139 100.00 100.00 1.22e-97 PDB 1K9J "Complex Of Dc-signr And Glcnac2man3" 100.00 139 100.00 100.00 1.22e-97 PDB 1SL6 "Crystal Structure Of A Fragment Of Dc-signr (containg The Carbohydrate Recognition Domain And Two Repeats Of The Neck) Complexe" 99.28 184 100.00 100.00 2.60e-98 PDB 1XAR "Crystal Structure Of A Fragment Of Dc-Signr (Containing The Carbohydrate Recognition Domain And Two Repeats Of The Neck)" 99.28 184 100.00 100.00 2.60e-98 PDB 1XPH "Structure Of Dc-Signr And A Portion Of Repeat Domain 8" 99.28 150 100.00 100.00 2.39e-97 DBJ BAF84967 "unnamed protein product [Homo sapiens]" 99.28 376 100.00 100.00 1.32e-100 DBJ BAG65307 "unnamed protein product [Homo sapiens]" 99.28 348 100.00 100.00 3.58e-101 GB AAG13815 "probable mannose binding C-type lectin DC-SIGNR [Homo sapiens]" 99.28 399 100.00 100.00 9.31e-101 GB AAG13848 "probable mannose binding C-type lectin DC-SIGNR [Homo sapiens]" 99.28 399 99.28 99.28 1.19e-99 GB AAH38851 "C-type lectin domain family 4, member M [Homo sapiens]" 99.28 399 100.00 100.00 9.31e-101 GB AAI10615 "CLEC4M protein [Homo sapiens]" 99.28 387 100.00 100.00 1.20e-100 GB AAK20998 "L-SIGN [Homo sapiens]" 99.28 376 100.00 100.00 1.32e-100 REF NP_001138376 "C-type lectin domain family 4 member M isoform 2 [Homo sapiens]" 99.28 348 100.00 100.00 4.22e-101 REF NP_001138377 "C-type lectin domain family 4 member M isoform 12 [Homo sapiens]" 99.28 375 100.00 100.00 1.34e-100 REF NP_001138378 "C-type lectin domain family 4 member M isoform 7 [Homo sapiens]" 100.00 263 99.28 99.28 1.70e-99 REF NP_001138379 "C-type lectin domain family 4 member M isoform 11 [Homo sapiens]" 100.00 332 99.28 99.28 1.50e-100 REF NP_001138381 "C-type lectin domain family 4 member M isoform 9 [Homo sapiens]" 99.28 353 100.00 100.00 1.98e-100 SP Q8HY06 "RecName: Full=C-type lectin domain family 4 member M; AltName: Full=CD209 antigen-like protein 1; AltName: CD_antigen=CD299" 99.28 376 97.10 98.55 4.45e-98 SP Q9H2X3 "RecName: Full=C-type lectin domain family 4 member M; AltName: Full=CD209 antigen-like protein 1; AltName: Full=DC-SIGN-related" 99.28 399 100.00 100.00 9.31e-101 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species _Gene_mnemonic _Details $DC-SIGNR Human 9606 Eukaryota Metazoa Homo sapiens CLEC4M 'Synonyms: CD209L, CD209L1, CD299' stop_ save_ ######################### # Experimental source # ######################### save_experimental_source _Saveframe_category experimental_source loop_ _Mol_label _Production_method _Host_organism_name_common _Genus _Species _Strain _Vector_name $DC-SIGNR 'recombinant technology' . Escherichia coli BL21(DE3) pT5T stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Saveframe_category sample _Sample_type solution _Details '20 mM d-HEPES, 20 mM NaCl pH 6.8 in 10% D2O / 90% H2O to a final concentration of 0.7 mM DC-SIGNR CRD' loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $DC-SIGNR 0.7 mM '[U-100% 15N]' HEPES 20 mM '[U-100% 2H]' NaCl 20 mM 'natural abundance' H2O 90 % 'natural abundance' D2O 10 % 'natural abundance' stop_ save_ ############################ # Computer software used # ############################ save_TOPSPIN _Saveframe_category software _Name TOPSPIN _Version . loop_ _Vendor _Address _Electronic_address 'Bruker Biospin' . . stop_ loop_ _Task collection processing stop_ _Details . save_ save_SPARKY _Saveframe_category software _Name SPARKY _Version . loop_ _Vendor _Address _Electronic_address Goddard . . stop_ loop_ _Task 'chemical shift assignment' 'peak picking' stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model Avance _Field_strength 700 _Details . save_ ############################# # NMR applied experiments # ############################# save_2D_1H-15N_HSQC_1 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-15N HSQC' _Sample_label $sample_1 save_ save_3D_CBCA(CO)NH_2 _Saveframe_category NMR_applied_experiment _Experiment_name '3D CBCA(CO)NH' _Sample_label $sample_1 save_ save_3D_C(CO)NH_3 _Saveframe_category NMR_applied_experiment _Experiment_name '3D C(CO)NH' _Sample_label $sample_1 save_ save_3D_HNCO_4 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCO' _Sample_label $sample_1 save_ save_3D_HNCA_5 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCA' _Sample_label $sample_1 save_ save_3D_HN(CO)CA_6 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HN(CO)CA' _Sample_label $sample_1 save_ save_3D_HNCACB_7 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCACB' _Sample_label $sample_1 save_ ####################### # Sample conditions # ####################### save_sample_conditions_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units temperature 310 . K pH 6.8 . pH pressure 1 . atm stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference_1 _Saveframe_category chemical_shift_reference _Details 'Proton chemical shifts were referenced against external DSS and nitrogen chemical shifts references indirectly to DSS using the absolute frequency ratio.' loop_ _Mol_common_name _Atom_type _Atom_isotope_number _Atom_group _Chem_shift_units _Chem_shift_value _Reference_method _Reference_type _External_reference_sample_geometry _External_reference_location _External_reference_axis _Indirect_shift_ratio DSS H 1 'methyl protons' ppm 0 external direct . . . 1.0 DSS N 15 'methyl protons' ppm 0 external indirect . . . 0.101329118 stop_ save_ ################################### # Assigned chemical shift lists # ################################### ################################################################### # Chemical Shift Ambiguity Index Value Definitions # # # # The values other than 1 are used for those atoms with different # # chemical shifts that cannot be assigned to stereospecific atoms # # or to specific residues or chains. # # # # Index Value Definition # # # # 1 Unique (including isolated methyl protons, # # geminal atoms, and geminal methyl # # groups with identical chemical shifts) # # (e.g. ILE HD11, HD12, HD13 protons) # # 2 Ambiguity of geminal atoms or geminal methyl # # proton groups (e.g. ASP HB2 and HB3 # # protons, LEU CD1 and CD2 carbons, or # # LEU HD11, HD12, HD13 and HD21, HD22, # # HD23 methyl protons) # # 3 Aromatic atoms on opposite sides of # # symmetrical rings (e.g. TYR HE1 and HE2 # # protons) # # 4 Intraresidue ambiguities (e.g. LYS HG and # # HD protons or TRP HZ2 and HZ3 protons) # # 5 Interresidue ambiguities (LYS 12 vs. LYS 27) # # 6 Intermolecular ambiguities (e.g. ASP 31 CA # # in monomer 1 and ASP 31 CA in monomer 2 # # of an asymmetrical homodimer, duplex # # DNA assignments, or other assignments # # that may apply to atoms in one or more # # molecule in the molecular assembly) # # 9 Ambiguous, specific ambiguity not defined # # # ################################################################### save_assigned_chem_shift_list_1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Experiment_label '2D 1H-15N HSQC' '3D CBCA(CO)NH' '3D C(CO)NH' '3D HNCO' '3D HNCA' '3D HN(CO)CA' '3D HNCACB' stop_ loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $sample_conditions_1 _Chem_shift_reference_set_label $chemical_shift_reference_1 _Mol_system_component_name 'DC-SIGNR CRD' _Text_data_format . _Text_data . loop_ _Atom_shift_assign_ID _Residue_author_seq_code _Residue_seq_code _Residue_label _Atom_name _Atom_type _Chem_shift_value _Chem_shift_value_error _Chem_shift_ambiguity_code 1 3 3 ARG H H 8.414 . . 2 3 3 ARG N N 122.66 . . 3 4 4 LEU H H 6.542 . . 4 4 4 LEU N N 117.813 . . 5 5 5 CYS H H 9.038 . . 6 5 5 CYS N N 121.254 . . 7 6 6 ARG H H 9.195 . . 8 6 6 ARG N N 123.273 . . 9 7 7 HIS H H 9.059 . . 10 7 7 HIS N N 125.858 . . 11 10 10 LYS H H 9.436 . . 12 10 10 LYS N N 124.869 . . 13 13 13 THR H H 9.714 . . 14 13 13 THR N N 119.04 . . 15 14 14 PHE H H 9.028 . . 16 14 14 PHE N N 128.789 . . 17 15 15 PHE H H 8.641 . . 18 15 15 PHE N N 126.505 . . 19 16 16 GLN H H 8.636 . . 20 16 16 GLN N N 127.179 . . 21 18 18 ASN H H 7.503 . . 22 18 18 ASN N N 118.147 . . 23 19 19 CYS H H 9.372 . . 24 19 19 CYS N N 117.021 . . 25 20 20 TYR H H 9.867 . . 26 20 20 TYR N N 121.178 . . 27 21 21 PHE H H 8.526 . . 28 21 21 PHE N N 125.247 . . 29 22 22 MET H H 7.662 . . 30 22 22 MET N N 127.166 . . 31 23 23 SER H H 7.66 . . 32 23 23 SER N N 118.893 . . 33 25 25 SER H H 7.123 . . 34 25 25 SER N N 113.436 . . 35 26 26 GLN H H 8.319 . . 36 26 26 GLN N N 116.662 . . 37 31 31 ASP H H 8.927 . . 38 31 31 ASP N N 118.345 . . 39 32 32 SER H H 7.8 . . 40 32 32 SER N N 123.288 . . 41 33 33 VAL H H 7.302 . . 42 33 33 VAL N N 122.902 . . 43 34 34 THR H H 7.438 . . 44 34 34 THR N N 114.731 . . 45 35 35 ALA H H 7.72 . . 46 35 35 ALA N N 124.562 . . 47 36 36 CYS H H 7.645 . . 48 36 36 CYS N N 112.524 . . 49 38 38 GLU H H 8.196 . . 50 38 38 GLU N N 119.465 . . 51 39 39 VAL H H 7.066 . . 52 39 39 VAL N N 109.769 . . 53 40 40 ARG H H 7.871 . . 54 40 40 ARG N N 115.656 . . 55 41 41 ALA H H 8.069 . . 56 41 41 ALA N N 120.291 . . 57 42 42 GLN H H 8.037 . . 58 42 42 GLN N N 116.856 . . 59 43 43 LEU H H 9.07 . . 60 43 43 LEU N N 133.098 . . 61 45 45 VAL H H 7.044 . . 62 45 45 VAL N N 127.82 . . 63 47 47 LYS H H 9.097 . . 64 47 47 LYS N N 123.146 . . 65 48 48 THR H H 7.458 . . 66 48 48 THR N N 107.032 . . 67 49 49 ALA H H 9.18 . . 68 49 49 ALA N N 125.065 . . 69 50 50 GLU H H 8.849 . . 70 50 50 GLU N N 117.334 . . 71 51 51 GLU H H 8.098 . . 72 51 51 GLU N N 123.556 . . 73 52 52 GLN H H 7.668 . . 74 52 52 GLN N N 121.349 . . 75 53 53 ASN H H 8.124 . . 76 53 53 ASN N N 116.964 . . 77 54 54 PHE H H 7.577 . . 78 54 54 PHE N N 120.404 . . 79 55 55 LEU H H 7.899 . . 80 55 55 LEU N N 120.063 . . 81 56 56 GLN H H 8.802 . . 82 56 56 GLN N N 122.304 . . 83 57 57 LEU H H 7.503 . . 84 57 57 LEU N N 119.593 . . 85 58 58 GLN H H 7.415 . . 86 58 58 GLN N N 116.309 . . 87 59 59 THR H H 7.671 . . 88 59 59 THR N N 111.756 . . 89 60 60 SER H H 8.094 . . 90 60 60 SER N N 118.719 . . 91 61 61 ARG H H 7.921 . . 92 61 61 ARG N N 121.494 . . 93 62 62 SER H H 7.182 . . 94 62 62 SER N N 111.486 . . 95 63 63 ASN H H 7.756 . . 96 63 63 ASN N N 118.41 . . 97 64 64 ARG H H 7.353 . . 98 64 64 ARG N N 116.397 . . 99 65 65 PHE H H 8.783 . . 100 65 65 PHE N N 125.362 . . 101 67 67 TRP H H 9.856 . . 102 67 67 TRP N N 124.869 . . 103 69 69 GLY H H 9.82 . . 104 69 69 GLY N N 112.058 . . 105 70 70 LEU H H 8.373 . . 106 70 70 LEU N N 127.786 . . 107 72 72 ASP H H 7.85 . . 108 72 72 ASP N N 123.573 . . 109 74 74 ASN H H 7.778 . . 110 74 74 ASN N N 115.662 . . 111 76 76 GLU H H 8.071 . . 112 76 76 GLU N N 127.907 . . 113 78 78 THR H H 8.268 . . 114 78 78 THR N N 121.58 . . 115 80 80 GLN H H 9.013 . . 116 80 80 GLN N N 123.431 . . 117 81 81 TRP H H 9.499 . . 118 81 81 TRP N N 126.962 . . 119 82 82 VAL H H 8.929 . . 120 82 82 VAL N N 115.286 . . 121 83 83 ASP H H 7.256 . . 122 83 83 ASP N N 117.882 . . 123 84 84 GLY H H 8.462 . . 124 84 84 GLY N N 109.033 . . 125 85 85 SER H H 8.245 . . 126 85 85 SER N N 119.122 . . 127 87 87 LEU H H 7.852 . . 128 87 87 LEU N N 121.448 . . 129 88 88 SER H H 8.942 . . 130 88 88 SER N N 127.337 . . 131 91 91 PHE H H 8.173 . . 132 91 91 PHE N N 120.462 . . 133 92 92 GLN H H 7.362 . . 134 92 92 GLN N N 117.665 . . 135 93 93 ARG H H 6.953 . . 136 93 93 ARG N N 113.603 . . 137 94 94 TYR H H 6.644 . . 138 94 94 TYR N N 118.51 . . 139 95 95 TRP H H 6.365 . . 140 95 95 TRP N N 117.872 . . 141 96 96 ASN H H 9.773 . . 142 96 96 ASN N N 122.655 . . 143 97 97 SER H H 8.488 . . 144 97 97 SER N N 114.049 . . 145 106 106 GLU H H 7.667 . . 146 106 106 GLU N N 123.009 . . 147 109 109 ALA H H 7.958 . . 148 109 109 ALA N N 126.411 . . 149 111 111 PHE H H 9.372 . . 150 111 111 PHE N N 120.799 . . 151 113 113 GLY H H 8.723 . . 152 113 113 GLY N N 115.666 . . 153 116 116 TRP H H 8.351 . . 154 116 116 TRP N N 122.348 . . 155 119 119 ASN H H 9.934 . . 156 119 119 ASN N N 124.91 . . 157 120 120 ARG H H 9.475 . . 158 120 120 ARG N N 122.429 . . 159 123 123 VAL H H 7.603 . . 160 123 123 VAL N N 121.405 . . 161 126 126 TYR H H 7.104 . . 162 126 126 TYR N N 116.631 . . 163 133 133 ALA H H 7.792 . . 164 133 133 ALA N N 122.859 . . 165 134 134 ALA H H 8.54 . . 166 134 134 ALA N N 123.55 . . 167 138 138 ASP H H 8.295 . . 168 138 138 ASP N N 122.505 . . stop_ save_