data_18585 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Griffithsin assignment ; _BMRB_accession_number 18585 _BMRB_flat_file_name bmr18585.str _Entry_type original _Submission_date 2012-07-09 _Accession_date 2012-07-09 _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 Xue Jie . . 2 Gao Yongguang . . 3 LiWang Patricia . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 107 "13C chemical shifts" 244 "15N chemical shifts" 107 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2013-02-19 update BMRB 'update entry citation' 2012-08-21 original author 'original release' stop_ save_ ############################# # Citation for this entry # ############################# save_GRFT_assignment _Saveframe_category entry_citation _Citation_full . _Citation_title 'The role of individual carbohydrate-binding sites in the function of the potent anti-HIV lectin griffithsin.' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 22827601 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Xue Jie . . 2 Gao Yongguang . . 3 Hoorelbeke Bart . . 4 Kagiampakis Ioannis . . 5 Zhao Bo . . 6 Demeler Borries . . 7 Balzarini Jan . . 8 Liwang Patricia J. . stop_ _Journal_abbreviation 'Mol. Pharm.' _Journal_name_full 'Molecular pharmaceutics' _Journal_volume 9 _Journal_issue 9 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 2613 _Page_last 2625 _Year 2012 _Details . loop_ _Keyword 'GRFT assignment' NMR stop_ save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name 'Griffithsin (GRFT)' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label GRFT $Griffithsin_(GRFT) stop_ _System_molecular_weight 14687 _System_physical_state recombinant _System_oligomer_state ? _System_paramagnetic no _System_thiol_state . _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_Griffithsin_(GRFT) _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common Griffithsin_(GRFT) _Molecular_mass . _Mol_thiol_state 'not present' loop_ _Biological_function 'Griffithsin is a lectin that binds carbohydrate, in particular mannose. It could bind high mannose structure on HIV gp120, thus interfere HIV entry.' stop_ _Details 'Amino acid analysis of GRFT failed to identify amino acid 31, the recombinant production of biologically active GRFT use alanine at 31 position.' ############################## # Polymer residue sequence # ############################## _Residue_count 140 _Mol_residue_sequence ; MGGSSHHHHHHSSGLVPRGS LTHRKFGGSGGSPFSGLSSI AVRSGSYLDAIIIDGVHHGG SGGNLSPTFTFGSGEYISNM TIRSGDYIDNISFETNMGRR FGPYGGSGGSANTLSNVKVI QINGSAGDYLDSLDIYYEQY ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 . MET 2 . GLY 3 . GLY 4 . SER 5 . SER 6 . HIS 7 . HIS 8 . HIS 9 . HIS 10 . HIS 11 . HIS 12 . SER 13 . SER 14 . GLY 15 . LEU 16 . VAL 17 . PRO 18 . ARG 19 . GLY 20 1 SER 21 2 LEU 22 3 THR 23 4 HIS 24 5 ARG 25 6 LYS 26 7 PHE 27 8 GLY 28 9 GLY 29 10 SER 30 11 GLY 31 12 GLY 32 13 SER 33 14 PRO 34 15 PHE 35 16 SER 36 17 GLY 37 18 LEU 38 19 SER 39 20 SER 40 21 ILE 41 22 ALA 42 23 VAL 43 24 ARG 44 25 SER 45 26 GLY 46 27 SER 47 28 TYR 48 29 LEU 49 30 ASP 50 31 ALA 51 32 ILE 52 33 ILE 53 34 ILE 54 35 ASP 55 36 GLY 56 37 VAL 57 38 HIS 58 39 HIS 59 40 GLY 60 41 GLY 61 42 SER 62 43 GLY 63 44 GLY 64 45 ASN 65 46 LEU 66 47 SER 67 48 PRO 68 49 THR 69 50 PHE 70 51 THR 71 52 PHE 72 53 GLY 73 54 SER 74 55 GLY 75 56 GLU 76 57 TYR 77 58 ILE 78 59 SER 79 60 ASN 80 61 MET 81 62 THR 82 63 ILE 83 64 ARG 84 65 SER 85 66 GLY 86 67 ASP 87 68 TYR 88 69 ILE 89 70 ASP 90 71 ASN 91 72 ILE 92 73 SER 93 74 PHE 94 75 GLU 95 76 THR 96 77 ASN 97 78 MET 98 79 GLY 99 80 ARG 100 81 ARG 101 82 PHE 102 83 GLY 103 84 PRO 104 85 TYR 105 86 GLY 106 87 GLY 107 88 SER 108 89 GLY 109 90 GLY 110 91 SER 111 92 ALA 112 93 ASN 113 94 THR 114 95 LEU 115 96 SER 116 97 ASN 117 98 VAL 118 99 LYS 119 100 VAL 120 101 ILE 121 102 GLN 122 103 ILE 123 104 ASN 124 105 GLY 125 106 SER 126 107 ALA 127 108 GLY 128 109 ASP 129 110 TYR 130 111 LEU 131 112 ASP 132 113 SER 133 114 LEU 134 115 ASP 135 116 ILE 136 117 TYR 137 118 TYR 138 119 GLU 139 120 GLN 140 121 TYR stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-01-29 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 18576 GRFT 100.00 140 100.00 100.00 3.80e-91 PDB 2GTY "Crystal Structure Of Unliganded Griffithsin" 86.43 122 100.00 100.00 5.87e-77 PDB 2GUC "Crystal Structure Of A Complex Of Griffithsin With Mannose At 1.78 A Resolution." 86.43 122 100.00 100.00 5.87e-77 PDB 2GUD "Crystal Structure Of A Complex Of Griffithsin With Mannose At 0.94 A Resolution" 86.43 122 100.00 100.00 5.87e-77 PDB 2GUE "Crystal Structure Of A Complex Of Griffithsin With N-Acetylglucosamine" 86.43 122 100.00 100.00 5.87e-77 PDB 2GUX "Selenomethionine Derivative Of Griffithsin" 98.57 138 98.55 98.55 2.66e-87 PDB 2HYQ "Crystal Structure Of A Complex Of Griffithsin With 6alpha-Mannobiose" 86.43 122 100.00 100.00 5.87e-77 PDB 2HYR "Crystal Structure Of A Complex Of Griffithsin With Maltose" 86.43 122 100.00 100.00 5.87e-77 PDB 2NU5 "Crystal Structure Of A Complex Of Griffithsin Cocrystallized With N- Acetylglucosamine" 86.43 122 100.00 100.00 5.87e-77 PDB 2NUO "Crystal Structure Of A Complex Of Griffithsin With Glucose" 86.43 122 100.00 100.00 5.87e-77 PDB 3LKY "Monomeric Griffithsin With A Single Gly-Ser Insertion" 87.86 123 98.37 98.37 4.21e-75 PDB 3LL2 "Monomeric Griffithsin In Complex With A High-Mannose Branched Carbohydrate" 87.86 123 97.56 97.56 6.44e-74 GB AAW66484 "griffithsin [synthetic construct]" 86.43 121 100.00 100.00 5.68e-77 GB AAW66485 "His-tagged griffithsin [synthetic construct]" 98.57 139 100.00 100.00 1.09e-89 GB ACM42413 "griffithsin [synthetic construct]" 86.43 122 100.00 100.00 4.61e-77 SP P84801 "RecName: Full=Griffithsin; Short=GRFT [Griffithsia sp. Q66D336]" 86.43 121 99.17 99.17 3.67e-76 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $Griffithsin_(GRFT) 'Red Algae' 9606 Eukaryota Protozoa Griffithsia . 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 _Details $Griffithsin_(GRFT) 'recombinant technology' . Escherichia coli BL21(DE3) 'pET 15b' 'pET15b is a bacteria expresson plasmid using T7 expression system' stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_GRFT_in_20_mM_sodium_phosphate_pH_7 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $Griffithsin_(GRFT) 500 uM '[U-100% 13C; U-100% 15N]' H2O 90 % 'natural abundance' D2O 10 % 'natural abundance' stop_ save_ ############################ # Computer software used # ############################ save_SPARKY_NMR_view_PIPP_NMRPIPE _Saveframe_category software _Name SPARKY_NMR_view_PIPP_NMRPIPE _Version . loop_ _Vendor _Address _Electronic_address 'Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax' . . Garrett . . Goddard . . 'Johnson, One Moon Scientific' . . stop_ loop_ _Task 'chemical shift assignment' stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model Avance _Field_strength 600 _Details 'cryoprobe, four channel 600-MHz Bruker Avance III' save_ ############################# # NMR applied experiments # ############################# save_2D_1H-15N_HSQC_1 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-15N HSQC' _Sample_label $GRFT_in_20_mM_sodium_phosphate_pH_7 save_ save_3D_HNCO_2 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCO' _Sample_label $GRFT_in_20_mM_sodium_phosphate_pH_7 save_ save_3D_HN(CA)CO_3 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HN(CA)CO' _Sample_label $GRFT_in_20_mM_sodium_phosphate_pH_7 save_ save_3D_HNCACB_4 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCACB' _Sample_label $GRFT_in_20_mM_sodium_phosphate_pH_7 save_ save_3D_CBCA(CO)NH_5 _Saveframe_category NMR_applied_experiment _Experiment_name '3D CBCA(CO)NH' _Sample_label $GRFT_in_20_mM_sodium_phosphate_pH_7 save_ save_3D_HNCA_6 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCA' _Sample_label $GRFT_in_20_mM_sodium_phosphate_pH_7 save_ save_3D_HN(CO)CA_7 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HN(CO)CA' _Sample_label $GRFT_in_20_mM_sodium_phosphate_pH_7 save_ ####################### # Sample conditions # ####################### save_GRFT_in_20_mM_sodium_phosphate_pH_7_conditions _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units 'ionic strength' 104 . mM pH 7 . pH pressure 1 . atm temperature 298 . K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference_1 _Saveframe_category chemical_shift_reference _Details . 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 C 13 'methyl protons' ppm 0 internal indirect . . . 0.25 DSS H 1 'methyl protons' ppm 0 internal direct . . . 1 DSS N 15 'methyl protons' ppm 0 internal indirect . . . 0.10 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' stop_ loop_ _Sample_label $GRFT_in_20_mM_sodium_phosphate_pH_7 stop_ _Sample_conditions_label $GRFT_in_20_mM_sodium_phosphate_pH_7_conditions _Chem_shift_reference_set_label $chemical_shift_reference_1 _Mol_system_component_name GRFT _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 1 20 SER H H 7.904 . 1 2 1 20 SER C C 174.2 . 1 3 1 20 SER CA C 57.73 . 1 4 1 20 SER N N 116.1 . 1 5 2 21 LEU H H 8.599 . 1 6 2 21 LEU C C 175.4 . 1 7 2 21 LEU CA C 55.36 . 1 8 2 21 LEU CB C 42.4 . 1 9 2 21 LEU N N 128.8 . 1 10 3 22 THR H H 8.792 . 1 11 3 22 THR C C 170.9 . 1 12 3 22 THR CA C 60.27 . 1 13 3 22 THR CB C 69.91 . 1 14 3 22 THR N N 122.5 . 1 15 4 23 HIS H H 8.166 . 1 16 4 23 HIS C C 173.2 . 1 17 4 23 HIS CA C 53.49 . 1 18 4 23 HIS CB C 31.91 . 1 19 4 23 HIS N N 118.7 . 1 20 5 24 ARG H H 8.307 . 1 21 5 24 ARG C C 171.7 . 1 22 5 24 ARG CA C 55.52 . 1 23 5 24 ARG N N 123.1 . 1 24 6 25 LYS H H 7.895 . 1 25 6 25 LYS C C 175.2 . 1 26 6 25 LYS CA C 54.27 . 1 27 6 25 LYS N N 125.4 . 1 28 7 26 PHE H H 9.216 . 1 29 7 26 PHE C C 175 . 1 30 7 26 PHE CA C 56.46 . 1 31 7 26 PHE CB C 42.59 . 1 32 7 26 PHE N N 125.7 . 1 33 8 27 GLY H H 8.198 . 1 34 8 27 GLY C C 174.5 . 1 35 8 27 GLY CA C 43.85 . 1 36 8 27 GLY N N 109.7 . 1 37 9 28 GLY H H 7.556 . 1 38 9 28 GLY C C 175.5 . 1 39 9 28 GLY CA C 44.75 . 1 40 9 28 GLY N N 109.2 . 1 41 10 29 SER H H 8.495 . 1 42 10 29 SER C C 175.9 . 1 43 10 29 SER CA C 58.66 . 1 44 10 29 SER CB C 64.51 . 1 45 10 29 SER N N 113.7 . 1 46 11 30 GLY H H 8.495 . 1 47 11 30 GLY C C 173.7 . 1 48 11 30 GLY CA C 44.41 . 1 49 11 30 GLY N N 111.8 . 1 50 12 31 GLY H H 7.997 . 1 51 12 31 GLY C C 174.2 . 1 52 12 31 GLY CA C 44.8 . 1 53 12 31 GLY N N 105.4 . 1 54 13 32 SER H H 8.313 . 1 55 13 32 SER CA C 55.73 . 1 56 13 32 SER CB C 63.89 . 1 57 13 32 SER N N 115.9 . 1 58 15 34 PHE H H 8.69 . 1 59 15 34 PHE C C 173.3 . 1 60 15 34 PHE CA C 56.31 . 1 61 15 34 PHE CB C 42.93 . 1 62 15 34 PHE N N 119.1 . 1 63 16 35 SER H H 8.535 . 1 64 16 35 SER C C 175.1 . 1 65 16 35 SER CA C 54.37 . 1 66 16 35 SER CB C 65.07 . 1 67 16 35 SER N N 116.1 . 1 68 17 36 GLY H H 8.995 . 1 69 17 36 GLY C C 175.5 . 1 70 17 36 GLY CA C 47.48 . 1 71 17 36 GLY N N 115.9 . 1 72 21 40 ILE H H 9.128 . 1 73 21 40 ILE C C 172.9 . 1 74 21 40 ILE CA C 59.83 . 1 75 21 40 ILE N N 121 . 1 76 22 41 ALA H H 8.87 . 1 77 22 41 ALA C C 175.1 . 1 78 22 41 ALA CA C 51.08 . 1 79 22 41 ALA CB C 23.97 . 1 80 22 41 ALA N N 128.2 . 1 81 23 42 VAL H H 8.979 . 1 82 23 42 VAL C C 175 . 1 83 23 42 VAL CA C 59.16 . 1 84 23 42 VAL N N 111.4 . 1 85 24 43 ARG H H 7.934 . 1 86 24 43 ARG C C 176.3 . 1 87 24 43 ARG CA C 55.5 . 1 88 24 43 ARG N N 116.6 . 1 89 25 44 SER H H 8.849 . 1 90 25 44 SER C C 173.6 . 1 91 25 44 SER CA C 58.37 . 1 92 25 44 SER CB C 68.64 . 1 93 25 44 SER N N 115.5 . 1 94 26 45 GLY H H 8.405 . 1 95 26 45 GLY C C 174.8 . 1 96 26 45 GLY CA C 46.94 . 1 97 26 45 GLY N N 114.3 . 1 98 28 47 TYR H H 7.848 . 1 99 28 47 TYR C C 174.2 . 1 100 28 47 TYR CA C 55.39 . 1 101 28 47 TYR CB C 39.38 . 1 102 28 47 TYR N N 117.4 . 1 103 29 48 LEU H H 8.714 . 1 104 29 48 LEU C C 174.2 . 1 105 29 48 LEU CA C 54.51 . 1 106 29 48 LEU N N 121.6 . 1 107 30 49 ASP H H 8.368 . 1 108 30 49 ASP CA C 57.16 . 1 109 30 49 ASP CB C 42.83 . 1 110 30 49 ASP N N 128.2 . 1 111 31 50 ALA H H 7.941 . 1 112 31 50 ALA C C 175.8 . 1 113 31 50 ALA CA C 51.6 . 1 114 31 50 ALA CB C 23.41 . 1 115 31 50 ALA N N 113.9 . 1 116 32 51 ILE H H 8.633 . 1 117 32 51 ILE C C 171 . 1 118 32 51 ILE CA C 60.06 . 1 119 32 51 ILE N N 118.5 . 1 120 33 52 ILE H H 9.024 . 1 121 33 52 ILE C C 177.1 . 1 122 33 52 ILE CA C 60.1 . 1 123 33 52 ILE N N 129.9 . 1 124 34 53 ILE H H 8.436 . 1 125 34 53 ILE C C 176.7 . 1 126 34 53 ILE CA C 60.07 . 1 127 34 53 ILE CB C 40.22 . 1 128 34 53 ILE N N 128.9 . 1 129 36 55 GLY H H 8.165 . 1 130 36 55 GLY C C 173.9 . 1 131 36 55 GLY CA C 45.13 . 1 132 36 55 GLY N N 134.3 . 1 133 37 56 VAL H H 7.834 . 1 134 37 56 VAL C C 173.9 . 1 135 37 56 VAL CA C 62.62 . 1 136 37 56 VAL N N 124.4 . 1 137 39 58 HIS H H 8.136 . 1 138 39 58 HIS C C 173.2 . 1 139 39 58 HIS CA C 58.08 . 1 140 39 58 HIS CB C 42.6 . 1 141 39 58 HIS N N 121.7 . 1 142 40 59 GLY H H 8.083 . 1 143 40 59 GLY CA C 43.03 . 1 144 40 59 GLY N N 107.4 . 1 145 41 60 GLY H H 7.869 . 1 146 41 60 GLY CA C 44.21 . 1 147 41 60 GLY N N 110.8 . 1 148 42 61 SER H H 8.459 . 1 149 42 61 SER C C 175.2 . 1 150 42 61 SER CA C 57.7 . 1 151 42 61 SER CB C 64.34 . 1 152 42 61 SER N N 112.9 . 1 153 43 62 GLY H H 8.524 . 1 154 43 62 GLY C C 174.1 . 1 155 43 62 GLY CA C 44.18 . 1 156 43 62 GLY N N 111.8 . 1 157 45 64 ASN H H 8.578 . 1 158 45 64 ASN C C 175.7 . 1 159 45 64 ASN CA C 52.03 . 1 160 45 64 ASN CB C 41.16 . 1 161 45 64 ASN N N 117.6 . 1 162 46 65 LEU H H 8.983 . 1 163 46 65 LEU C C 176 . 1 164 46 65 LEU CA C 55.36 . 1 165 46 65 LEU CB C 43.35 . 1 166 46 65 LEU N N 129.2 . 1 167 47 66 SER H H 9.37 . 1 168 47 66 SER C C 170.9 . 1 169 47 66 SER CA C 58.01 . 1 170 47 66 SER CB C 62.65 . 1 171 47 66 SER N N 128.6 . 1 172 49 68 THR H H 9.012 . 1 173 49 68 THR C C 173.3 . 1 174 49 68 THR CA C 63.6 . 1 175 49 68 THR N N 120.8 . 1 176 50 69 PHE H H 9.739 . 1 177 50 69 PHE C C 174.2 . 1 178 50 69 PHE CA C 57.73 . 1 179 50 69 PHE N N 135.3 . 1 180 51 70 THR H H 8.266 . 1 181 51 70 THR C C 174.6 . 1 182 51 70 THR CA C 61.43 . 1 183 51 70 THR CB C 69.58 . 1 184 51 70 THR N N 126.9 . 1 185 52 71 PHE H H 8.416 . 1 186 52 71 PHE C C 177.1 . 1 187 52 71 PHE CA C 59.94 . 1 188 52 71 PHE N N 127.2 . 1 189 53 72 GLY H H 9.591 . 1 190 53 72 GLY CA C 43.59 . 1 191 53 72 GLY N N 112.4 . 1 192 54 73 SER H H 8.652 . 1 193 54 73 SER CA C 60.06 . 1 194 54 73 SER CB C 62.72 . 1 195 54 73 SER N N 116.7 . 1 196 55 74 GLY H H 9.144 . 1 197 55 74 GLY C C 172.8 . 1 198 55 74 GLY CA C 45.72 . 1 199 55 74 GLY N N 117.3 . 1 200 56 75 GLU H H 7.939 . 1 201 56 75 GLU C C 175 . 1 202 56 75 GLU CA C 54.26 . 1 203 56 75 GLU N N 123.2 . 1 204 57 76 TYR H H 8.376 . 1 205 57 76 TYR C C 174.4 . 1 206 57 76 TYR CA C 54.91 . 1 207 57 76 TYR N N 123.2 . 1 208 59 78 SER H H 8.934 . 1 209 59 78 SER CA C 57.73 . 1 210 59 78 SER N N 124.3 . 1 211 60 79 ASN H H 7.727 . 1 212 60 79 ASN C C 173.7 . 1 213 60 79 ASN CA C 53.11 . 1 214 60 79 ASN CB C 43.51 . 1 215 60 79 ASN N N 121.3 . 1 216 61 80 MET H H 9.171 . 1 217 61 80 MET C C 173.7 . 1 218 61 80 MET CA C 55.95 . 1 219 61 80 MET CB C 38.35 . 1 220 61 80 MET N N 122.9 . 1 221 62 81 THR H H 8.715 . 1 222 62 81 THR C C 173.2 . 1 223 62 81 THR CA C 62.58 . 1 224 62 81 THR CB C 70.93 . 1 225 62 81 THR N N 122.6 . 1 226 63 82 ILE H H 8.796 . 1 227 63 82 ILE C C 176.6 . 1 228 63 82 ILE CA C 58.87 . 1 229 63 82 ILE N N 129.5 . 1 230 64 83 ARG H H 8.881 . 1 231 64 83 ARG C C 176.4 . 1 232 64 83 ARG CA C 54.76 . 1 233 64 83 ARG N N 127.2 . 1 234 65 84 SER H H 8.969 . 1 235 65 84 SER C C 174.2 . 1 236 65 84 SER CA C 58.95 . 1 237 65 84 SER CB C 67.91 . 1 238 65 84 SER N N 116.9 . 1 239 66 85 GLY H H 8.577 . 1 240 66 85 GLY C C 174.3 . 1 241 66 85 GLY CA C 47.13 . 1 242 66 85 GLY N N 114.6 . 1 243 67 86 ASP H H 8.567 . 1 244 67 86 ASP C C 173.2 . 1 245 67 86 ASP CA C 56.37 . 1 246 67 86 ASP N N 132.1 . 1 247 68 87 TYR H H 8.04 . 1 248 68 87 TYR C C 175 . 1 249 68 87 TYR CA C 54.79 . 1 250 68 87 TYR N N 116.1 . 1 251 69 88 ILE H H 8.449 . 1 252 69 88 ILE C C 174.4 . 1 253 69 88 ILE CA C 59.19 . 1 254 69 88 ILE N N 117.5 . 1 255 71 90 ASN H H 7.952 . 1 256 71 90 ASN C C 174.1 . 1 257 71 90 ASN CA C 53.23 . 1 258 71 90 ASN N N 117.2 . 1 259 72 91 ILE H H 8.621 . 1 260 72 91 ILE C C 172 . 1 261 72 91 ILE CA C 60.65 . 1 262 72 91 ILE CB C 43.86 . 1 263 72 91 ILE N N 124.2 . 1 264 73 92 SER H H 8.384 . 1 265 73 92 SER C C 173.2 . 1 266 73 92 SER CA C 56.99 . 1 267 73 92 SER CB C 66.41 . 1 268 73 92 SER N N 119.4 . 1 269 74 93 PHE H H 8.903 . 1 270 74 93 PHE C C 173 . 1 271 74 93 PHE CA C 57.4 . 1 272 74 93 PHE CB C 42.4 . 1 273 74 93 PHE N N 117.3 . 1 274 75 94 GLU H H 9.231 . 1 275 75 94 GLU C C 176.3 . 1 276 75 94 GLU CA C 53.95 . 1 277 75 94 GLU CB C 34.8 . 1 278 75 94 GLU N N 120.6 . 1 279 76 95 THR H H 8.975 . 1 280 76 95 THR C C 176.7 . 1 281 76 95 THR CA C 59.21 . 1 282 76 95 THR N N 112.7 . 1 283 77 96 ASN H H 9.405 . 1 284 77 96 ASN C C 175.6 . 1 285 77 96 ASN CA C 55.58 . 1 286 77 96 ASN CB C 35.64 . 1 287 77 96 ASN N N 120.6 . 1 288 78 97 MET H H 7.446 . 1 289 78 97 MET C C 176.1 . 1 290 78 97 MET CA C 54.63 . 1 291 78 97 MET N N 118.1 . 1 292 79 98 GLY H H 8.191 . 1 293 79 98 GLY C C 174.5 . 1 294 79 98 GLY CA C 45.6 . 1 295 79 98 GLY N N 109.3 . 1 296 80 99 ARG H H 7.098 . 1 297 80 99 ARG C C 175.2 . 1 298 80 99 ARG CA C 56.91 . 1 299 80 99 ARG N N 118.4 . 1 300 81 100 ARG H H 8.556 . 1 301 81 100 ARG C C 174.3 . 1 302 81 100 ARG CA C 55.13 . 1 303 81 100 ARG CB C 34.15 . 1 304 81 100 ARG N N 120 . 1 305 82 101 PHE H H 8.331 . 1 306 82 101 PHE C C 174.8 . 1 307 82 101 PHE CA C 56.15 . 1 308 82 101 PHE CB C 41.66 . 1 309 82 101 PHE N N 124.4 . 1 310 83 102 GLY H H 7.822 . 1 311 83 102 GLY C C 174.2 . 1 312 83 102 GLY CA C 43.59 . 1 313 83 102 GLY N N 115.4 . 1 314 85 104 TYR H H 7.923 . 1 315 85 104 TYR C C 172.1 . 1 316 85 104 TYR CA C 54.27 . 1 317 85 104 TYR N N 125 . 1 318 86 105 GLY H H 8.544 . 1 319 86 105 GLY C C 173.1 . 1 320 86 105 GLY CA C 43.77 . 1 321 86 105 GLY N N 111.8 . 1 322 87 106 GLY H H 7.943 . 1 323 87 106 GLY C C 174.5 . 1 324 87 106 GLY CA C 44.7 . 1 325 87 106 GLY N N 110.2 . 1 326 88 107 SER H H 8.336 . 1 327 88 107 SER C C 175.5 . 1 328 88 107 SER CA C 57.57 . 1 329 88 107 SER N N 111.3 . 1 330 89 108 GLY H H 8.262 . 1 331 89 108 GLY C C 173.3 . 1 332 89 108 GLY CA C 44.13 . 1 333 89 108 GLY N N 110.9 . 1 334 90 109 GLY H H 7.839 . 1 335 90 109 GLY C C 174.2 . 1 336 90 109 GLY CA C 45.2 . 1 337 90 109 GLY N N 104.5 . 1 338 91 110 SER H H 8.305 . 1 339 91 110 SER C C 173.9 . 1 340 91 110 SER CA C 57.12 . 1 341 91 110 SER CB C 65.04 . 1 342 91 110 SER N N 114.9 . 1 343 92 111 ALA H H 8.863 . 1 344 92 111 ALA C C 176.9 . 1 345 92 111 ALA CA C 52.53 . 1 346 92 111 ALA CB C 20.14 . 1 347 92 111 ALA N N 127.2 . 1 348 93 112 ASN H H 8.618 . 1 349 93 112 ASN C C 173.4 . 1 350 93 112 ASN CA C 53.64 . 1 351 93 112 ASN CB C 44.08 . 1 352 93 112 ASN N N 121.4 . 1 353 94 113 THR H H 8.731 . 1 354 94 113 THR C C 174 . 1 355 94 113 THR CA C 61.46 . 1 356 94 113 THR CB C 72.2 . 1 357 94 113 THR N N 118.1 . 1 358 95 114 LEU H H 9.137 . 1 359 95 114 LEU C C 175.2 . 1 360 95 114 LEU CA C 53.39 . 1 361 95 114 LEU N N 128.2 . 1 362 96 115 SER H H 9.11 . 1 363 96 115 SER C C 173.5 . 1 364 96 115 SER CA C 56.51 . 1 365 96 115 SER CB C 65.55 . 1 366 96 115 SER N N 119.8 . 1 367 97 116 ASN H H 8.616 . 1 368 97 116 ASN C C 172.4 . 1 369 97 116 ASN CA C 53.94 . 1 370 97 116 ASN N N 125.2 . 1 371 98 117 VAL H H 8.305 . 1 372 98 117 VAL C C 176.4 . 1 373 98 117 VAL CA C 58.46 . 1 374 98 117 VAL N N 109.5 . 1 375 99 118 LYS H H 8.232 . 1 376 99 118 LYS C C 177.2 . 1 377 99 118 LYS CA C 55.73 . 1 378 99 118 LYS N N 118.4 . 1 379 100 119 VAL H H 7.939 . 1 380 100 119 VAL C C 175.2 . 1 381 100 119 VAL CA C 65.24 . 1 382 100 119 VAL N N 127.1 . 1 383 101 120 ILE H H 9.209 . 1 384 101 120 ILE N N 129.4 . 1 385 104 123 ASN H H 8.286 . 1 386 104 123 ASN CA C 50.33 . 1 387 104 123 ASN N N 123.1 . 1 388 105 124 GLY H H 6.604 . 1 389 105 124 GLY C C 171.6 . 1 390 105 124 GLY CA C 47.87 . 1 391 105 124 GLY N N 106.1 . 1 392 106 125 SER H H 8.349 . 1 393 106 125 SER C C 172.9 . 1 394 106 125 SER CA C 57.79 . 1 395 106 125 SER CB C 65.86 . 1 396 106 125 SER N N 118.7 . 1 397 107 126 ALA H H 8.778 . 1 398 107 126 ALA C C 177.3 . 1 399 107 126 ALA CA C 52.45 . 1 400 107 126 ALA CB C 23.6 . 1 401 107 126 ALA N N 123.9 . 1 402 108 127 GLY H H 8.676 . 1 403 108 127 GLY C C 173.8 . 1 404 108 127 GLY CA C 46.87 . 1 405 108 127 GLY N N 116.2 . 1 406 109 128 ASP H H 8.436 . 1 407 109 128 ASP C C 173.7 . 1 408 109 128 ASP CA C 56.27 . 1 409 109 128 ASP CB C 41.28 . 1 410 109 128 ASP N N 131.2 . 1 411 110 129 TYR H H 8.367 . 1 412 110 129 TYR C C 174.2 . 1 413 110 129 TYR CA C 54.69 . 1 414 110 129 TYR N N 116.1 . 1 415 111 130 LEU H H 8.226 . 1 416 111 130 LEU C C 173.7 . 1 417 111 130 LEU CA C 53.83 . 1 418 111 130 LEU N N 120.8 . 1 419 112 131 ASP H H 8.219 . 1 420 112 131 ASP C C 176.1 . 1 421 112 131 ASP CA C 58.76 . 1 422 112 131 ASP N N 129.6 . 1 423 113 132 SER H H 8.344 . 1 424 113 132 SER C C 173.3 . 1 425 113 132 SER CA C 57.23 . 1 426 113 132 SER CB C 66.37 . 1 427 113 132 SER N N 106.5 . 1 428 114 133 LEU H H 8.562 . 1 429 114 133 LEU CA C 53.18 . 1 430 114 133 LEU N N 117.2 . 1 431 115 134 ASP H H 8.699 . 1 432 115 134 ASP CA C 53.12 . 1 433 115 134 ASP N N 125.9 . 1 434 116 135 ILE H H 8.73 . 1 435 116 135 ILE C C 175.3 . 1 436 116 135 ILE CA C 59.78 . 1 437 116 135 ILE N N 123.4 . 1 438 117 136 TYR H H 8.804 . 1 439 117 136 TYR C C 176.2 . 1 440 117 136 TYR CA C 56.66 . 1 441 117 136 TYR N N 127.1 . 1 442 118 137 TYR H H 9.04 . 1 443 118 137 TYR C C 171.2 . 1 444 118 137 TYR CA C 55.68 . 1 445 118 137 TYR CB C 41.14 . 1 446 118 137 TYR N N 122.1 . 1 447 119 138 GLU H H 8.396 . 1 448 119 138 GLU C C 175 . 1 449 119 138 GLU CA C 54.12 . 1 450 119 138 GLU N N 120 . 1 451 120 139 GLN H H 8.512 . 1 452 120 139 GLN C C 174.5 . 1 453 120 139 GLN CA C 54.29 . 1 454 120 139 GLN N N 125 . 1 455 121 140 TYR H H 8.445 . 1 456 121 140 TYR C C 180.7 . 1 457 121 140 TYR CA C 59.37 . 1 458 121 140 TYR N N 103.2 . 1 stop_ save_