data_19750 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Solution NMR structure of gp41 ectodomain monomer on a DPC micelle ; _BMRB_accession_number 19750 _BMRB_flat_file_name bmr19750.str _Entry_type original _Submission_date 2014-01-23 _Accession_date 2014-01-23 _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 Roche Julien . . 2 Louis John M. . 3 Grishaev Alexander . . 4 Ying Jinfa . . 5 Bax Adriaan . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 125 "13C chemical shifts" 195 "15N chemical shifts" 68 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2014-04-15 update BMRB 'update entry citation' 2014-02-17 original author 'original release' stop_ save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title 'Dissociation of the trimeric gp41 ectodomain at the lipid-water interface suggests an active role in HIV-1 Env-mediated membrane fusion.' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 24550514 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Roche Julien . . 2 Louis John M. . 3 Grishaev Alexander . . 4 Ying Jinfa . . 5 Bax Adriaan . . stop_ _Journal_abbreviation 'Proc. Natl. Acad. Sci. U.S.A.' _Journal_name_full 'Proceedings of the National Academy of Sciences of the United States of America' _Journal_volume 111 _Journal_issue 9 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 3425 _Page_last 3430 _Year 2014 _Details . save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name 'gp41 ectodomain monomer on a DPC micelle' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'gp41 ectodomain monomer' $entity stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state ? _System_paramagnetic no _System_thiol_state . _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_entity _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common entity _Molecular_mass 7879.830 _Mol_thiol_state 'not present' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 72 _Mol_residue_sequence ; GSHMSGIVQQQNNLLRAIEA QQHLLQLTVWGIKQLQARSG GRGGWMEWDREINNYTSLIH SLIEESQNQQEK ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 -3 GLY 2 -2 SER 3 -1 HIS 4 0 MET 5 1 SER 6 2 GLY 7 3 ILE 8 4 VAL 9 5 GLN 10 6 GLN 11 7 GLN 12 8 ASN 13 9 ASN 14 10 LEU 15 11 LEU 16 12 ARG 17 13 ALA 18 14 ILE 19 15 GLU 20 16 ALA 21 17 GLN 22 18 GLN 23 19 HIS 24 20 LEU 25 21 LEU 26 22 GLN 27 23 LEU 28 24 THR 29 25 VAL 30 26 TRP 31 27 GLY 32 28 ILE 33 29 LYS 34 30 GLN 35 31 LEU 36 32 GLN 37 33 ALA 38 34 ARG 39 35 SER 40 36 GLY 41 37 GLY 42 38 ARG 43 39 GLY 44 40 GLY 45 41 TRP 46 42 MET 47 43 GLU 48 44 TRP 49 45 ASP 50 46 ARG 51 47 GLU 52 48 ILE 53 49 ASN 54 50 ASN 55 51 TYR 56 52 THR 57 53 SER 58 54 LEU 59 55 ILE 60 56 HIS 61 57 SER 62 58 LEU 63 59 ILE 64 60 GLU 65 61 GLU 66 62 SER 67 63 GLN 68 64 ASN 69 65 GLN 70 66 GLN 71 67 GLU 72 68 LYS 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 PDB 1DF4 "Interactions Between Hiv-1 Gp41 Core And Detergents And Their Implications For Membrane Fusion" 94.44 68 100.00 100.00 1.11e-38 PDB 1DF5 "Interactions Between Hiv-1 Gp41 Core And Detergents And Their Implications For Membrane Fusion" 94.44 68 100.00 100.00 1.11e-38 PDB 1DLB "Helical Interactions In The Hiv-1 Gp41 Core Reveals Structural Basis For The Inhibitory Activity Of Gp41 Peptides" 94.44 68 98.53 98.53 1.35e-37 PDB 1I5X "Hiv-1 Gp41 Core" 94.44 68 98.53 98.53 9.43e-38 PDB 1I5Y "Hiv-1 Gp41 Core" 94.44 68 98.53 98.53 4.81e-38 PDB 1K33 "Crystal Structure Analysis Of The Gp41 Core Mutant" 94.44 68 98.53 98.53 5.66e-38 PDB 1K34 "Crystal Structure Analysis Of Gp41 Core Mutant" 94.44 68 98.53 98.53 5.66e-38 PDB 1QR8 "Inhibition Of Hiv-1 Infectivity By The Gp41 Core: Role Of A Conserved Hydrophobic Cavity In Membrane Fusion" 94.44 68 98.53 98.53 3.18e-37 PDB 1QR9 "Inhibition Of Hiv-1 Infectivity By The Gp41 Core: Role Of A Conserved Hydrophobic Cavity In Membrane Fusion" 94.44 68 98.53 98.53 6.24e-38 PDB 1SZT "Atomic Structure Of A Thermostable Subdomain Of Hiv-1 Gp41" 94.44 68 100.00 100.00 1.11e-38 PDB 2MK3 "Solution Nmr Structure Of Gp41 Ectodomain Monomer On A Dpc Micelle" 100.00 72 100.00 100.00 5.34e-42 PDB 2OT5 "Crystal Structure Of The Hiv Gp41 Core With The Enfuvirtide Resistance Mutation N43d" 94.44 68 98.53 100.00 3.66e-38 PDB 3CP1 "Structure Of A Longer Thermalstable Core Domain Of Hiv-1 Gp41 Containing The Enfuvirtide Resistance Mutation N43d" 95.83 86 97.10 100.00 1.01e-38 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $entity HIV-1 11676 Viruses . Lentivirus . 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 $entity 'recombinant technology' . Escherichia coli . pET15b stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_Isotropic_sample _Saveframe_category sample _Sample_type solution _Details 'triple labelled (2H/15N/13C) CoreS sample (gp41 ectodomain construct:S546-R579-SGGRG-W628-K655) in solution containing 100 mM DPC' loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling DPC 100 mM '[U-99% 2H]' 'sodium phosphate' 50 mM 'natural abundance' H2O 93 % 'natural abundance' D2O 7 % 'natural abundance' $entity . mM '[U-2H; U-15N; U-13C]' stop_ save_ save_Aligned_sample _Saveframe_category sample _Sample_type 'gel solution' _Details 'triple labelled (2H/15/13C) CoreS sample in 5.5% acrylamide gel containing 30% cationic DADMAC-acrylamide copolymer. Compressed from 6 mm to 4.1 mm.' loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling DPC 100 mM '[U-99% 2H]' 'potassium phosphate' 50 mM 'natural abundance' H2O 93 % 'natural abundance' D2O 7 % 'natural abundance' $entity . mM '[U-2H; U-15N; U-13C]' 'acrylamide gel' 5.5 % 'natural abundance' 'cationic DADMAC-acrylamide copolymer' 30 % 'natural abundance' stop_ save_ ############################ # Computer software used # ############################ save_X-PLOR_NIH _Saveframe_category software _Name X-PLOR_NIH _Version 2.34 loop_ _Vendor _Address _Electronic_address 'Schwieters, Kuszewski, Tjandra and Clore' . . stop_ loop_ _Task 'structure solution' stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model Avance _Field_strength 600 _Details . save_ save_spectrometer_2 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model Avance _Field_strength 800 _Details . save_ save_spectrometer_3 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model Avance _Field_strength 900 _Details . save_ save_spectrometer_4 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model Avance _Field_strength 500 _Details . save_ ############################# # NMR applied experiments # ############################# save_3D_HNCACB_1 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCACB' _Sample_label $Isotropic_sample save_ save_3D_HNCO_2 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCO' _Sample_label $Isotropic_sample save_ save_3D_1H-15N_NOESY_3 _Saveframe_category NMR_applied_experiment _Experiment_name '3D 1H-15N NOESY' _Sample_label $Isotropic_sample save_ save_3D_HCCH-TOCSY_4 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HCCH-TOCSY' _Sample_label $Isotropic_sample save_ save_2D_1H-1H_NOESY_5 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-1H NOESY' _Sample_label $Isotropic_sample save_ save_2D_1H-15N_Artsy_6 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-15N Artsy' _Sample_label $Aligned_sample save_ save_2D_1H-15N_Trosy-HSQC_7 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-15N Trosy-HSQC' _Sample_label $Aligned_sample save_ save_3D_HNCO_8 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCO' _Sample_label $Aligned_sample save_ ####################### # Sample conditions # ####################### save_sample_conditions_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units 'ionic strength' 0.05 . M pH 4.0 . pH pressure 1 . atm temperature 310 . 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 0.00 na indirect . . . 0.251449530 DSS H 1 'methyl protons' ppm 0.00 internal direct . . . 1.000000000 DSS N 15 'methyl protons' ppm 0.00 na 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 '3D HNCACB' '3D HNCO' '3D HCCH-TOCSY' stop_ loop_ _Sample_label $Isotropic_sample stop_ _Sample_conditions_label $sample_conditions_1 _Chem_shift_reference_set_label $chemical_shift_reference_1 _Mol_system_component_name 'gp41 ectodomain monomer' _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 5 SER HA H 4.321 . . 2 1 5 SER H H 8.171 . . 3 1 5 SER C C 175.43 . . 4 1 5 SER CA C 59.11 . . 5 1 5 SER CB C 62.91 . . 6 1 5 SER N N 116.54 . . 7 2 6 GLY H H 8.294 . . 8 2 6 GLY C C 174.89 . . 9 2 6 GLY CA C 45.55 . . 10 2 6 GLY N N 110.89 . . 11 3 7 ILE H H 7.861 . . 12 3 7 ILE HA H 4.032 . . 13 3 7 ILE C C 176.74 . . 14 3 7 ILE CA C 62.24 . . 15 3 7 ILE CB C 37.46 . . 16 3 7 ILE N N 120.80 . . 17 4 8 VAL H H 7.857 . . 18 4 8 VAL HA H 3.883 . . 19 4 8 VAL C C 176.99 . . 20 4 8 VAL CA C 63.62 . . 21 4 8 VAL CB C 31.17 . . 22 4 8 VAL N N 121.09 . . 23 5 9 GLN H H 8.051 . . 24 5 9 GLN HA H 4.235 . . 25 5 9 GLN C C 176.96 . . 26 5 9 GLN CA C 56.75 . . 27 5 9 GLN CB C 28.25 . . 28 5 9 GLN N N 121.38 . . 29 6 10 GLN H H 8.018 . . 30 6 10 GLN HA H 4.368 . . 31 6 10 GLN C C 176.72 . . 32 6 10 GLN CA C 56.12 . . 33 6 10 GLN CB C 28.22 . . 34 6 10 GLN N N 119.48 . . 35 7 11 GLN H H 8.151 . . 36 7 11 GLN HA H 4.189 . . 37 7 11 GLN C C 176.18 . . 38 7 11 GLN CA C 56.85 . . 39 7 11 GLN CB C 28.08 . . 40 7 11 GLN N N 120.36 . . 41 8 12 ASN H H 8.256 . . 42 8 12 ASN HA H 4.452 . . 43 8 12 ASN C C 176.30 . . 44 8 12 ASN CA C 54.80 . . 45 8 12 ASN CB C 38.20 . . 46 8 12 ASN N N 119.23 . . 47 9 13 ASN H H 8.319 . . 48 9 13 ASN C C 177.15 . . 49 9 13 ASN CA C 54.94 . . 50 9 13 ASN CB C 37.68 . . 51 9 13 ASN N N 119.84 . . 52 10 14 LEU H H 8.194 . . 53 10 14 LEU HA H 4.134 . . 54 10 14 LEU C C 178.05 . . 55 10 14 LEU CA C 57.69 . . 56 10 14 LEU CB C 40.76 . . 57 10 14 LEU N N 122.90 . . 58 11 15 LEU H H 8.030 . . 59 11 15 LEU HA H 4.008 . . 60 11 15 LEU C C 178.83 . . 61 11 15 LEU CA C 57.67 . . 62 11 15 LEU CB C 40.23 . . 63 11 15 LEU N N 118.80 . . 64 12 16 ARG H H 7.845 . . 65 12 16 ARG HA H 4.013 . . 66 12 16 ARG C C 178.84 . . 67 12 16 ARG CA C 58.62 . . 68 12 16 ARG CB C 29.05 . . 69 12 16 ARG N N 117.71 . . 70 13 17 ALA H H 7.681 . . 71 13 17 ALA HA H 4.194 . . 72 13 17 ALA C C 180.04 . . 73 13 17 ALA CA C 54.48 . . 74 13 17 ALA CB C 17.50 . . 75 13 17 ALA N N 121.87 . . 76 14 18 ILE H H 7.975 . . 77 14 18 ILE HA H 3.733 . . 78 14 18 ILE C C 177.76 . . 79 14 18 ILE CA C 64.34 . . 80 14 18 ILE CB C 37.20 . . 81 14 18 ILE N N 118.01 . . 82 15 19 GLU H H 8.110 . . 83 15 19 GLU HA H 3.952 . . 84 15 19 GLU C C 177.03 . . 85 15 19 GLU CA C 57.92 . . 86 15 19 GLU CB C 27.42 . . 87 15 19 GLU N N 117.43 . . 88 16 20 ALA H H 7.457 . . 89 16 20 ALA HA H 4.343 . . 90 16 20 ALA C C 178.57 . . 91 16 20 ALA CA C 52.65 . . 92 16 20 ALA CB C 18.08 . . 93 16 20 ALA N N 119.58 . . 94 17 21 GLN H H 7.642 . . 95 17 21 GLN HA H 4.431 . . 96 17 21 GLN C C 176.16 . . 97 17 21 GLN CA C 54.63 . . 98 17 21 GLN CB C 26.38 . . 99 17 21 GLN N N 118.84 . . 100 18 22 GLN H H 7.975 . . 101 18 22 GLN HA H 4.017 . . 102 18 22 GLN C C 177.48 . . 103 18 22 GLN CA C 58.29 . . 104 18 22 GLN CB C 28.12 . . 105 18 22 GLN N N 120.73 . . 106 19 23 HIS H H 8.697 . . 107 19 23 HIS HA H 4.674 . . 108 19 23 HIS C C 176.33 . . 109 19 23 HIS CA C 56.96 . . 110 19 23 HIS CB C 27.42 . . 111 19 23 HIS N N 117.47 . . 112 20 24 LEU H H 8.026 . . 113 20 24 LEU HA H 4.050 . . 114 20 24 LEU C C 179.68 . . 115 20 24 LEU CA C 57.74 . . 116 20 24 LEU CB C 40.83 . . 117 20 24 LEU N N 120.41 . . 118 21 25 LEU H H 8.433 . . 119 21 25 LEU HA H 4.059 . . 120 21 25 LEU C C 178.54 . . 121 21 25 LEU CA C 58.13 . . 122 21 25 LEU CB C 40.13 . . 123 21 25 LEU N N 121.93 . . 124 22 26 GLN H H 8.087 . . 125 22 26 GLN HA H 4.013 . . 126 22 26 GLN C C 179.43 . . 127 22 26 GLN CA C 58.90 . . 128 22 26 GLN CB C 27.47 . . 129 22 26 GLN N N 118.54 . . 130 23 27 LEU H H 8.013 . . 131 23 27 LEU HA H 4.231 . . 132 23 27 LEU C C 178.42 . . 133 23 27 LEU CA C 57.63 . . 134 23 27 LEU CB C 41.29 . . 135 23 27 LEU N N 120.75 . . 136 24 28 THR H H 8.024 . . 137 24 28 THR C C 176.18 . . 138 24 28 THR N N 116.79 . . 139 25 29 VAL H H 8.068 . . 140 25 29 VAL HA H 3.575 . . 141 25 29 VAL C C 177.60 . . 142 25 29 VAL CA C 66.82 . . 143 25 29 VAL CB C 30.83 . . 144 25 29 VAL N N 121.13 . . 145 26 30 TRP H H 7.983 . . 146 26 30 TRP HA H 4.180 . . 147 26 30 TRP C C 178.70 . . 148 26 30 TRP CA C 61.43 . . 149 26 30 TRP CB C 27.74 . . 150 26 30 TRP N N 120.52 . . 151 27 31 GLY H H 8.846 . . 152 27 31 GLY C C 174.99 . . 153 27 31 GLY CA C 47.24 . . 154 27 31 GLY N N 107.88 . . 155 28 32 ILE H H 8.427 . . 156 28 32 ILE HA H 3.612 . . 157 28 32 ILE C C 178.03 . . 158 28 32 ILE CA C 64.86 . . 159 28 32 ILE CB C 36.51 . . 160 28 32 ILE N N 122.33 . . 161 29 33 LYS H H 7.993 . . 162 29 33 LYS HA H 4.022 . . 163 29 33 LYS C C 180.05 . . 164 29 33 LYS CA C 59.27 . . 165 29 33 LYS CB C 30.68 . . 166 29 33 LYS N N 119.85 . . 167 30 34 GLN H H 7.800 . . 168 30 34 GLN HA H 3.840 . . 169 30 34 GLN C C 178.75 . . 170 30 34 GLN CA C 57.16 . . 171 30 34 GLN CB C 26.86 . . 172 30 34 GLN N N 118.87 . . 173 31 35 LEU H H 7.873 . . 174 31 35 LEU HA H 3.966 . . 175 31 35 LEU C C 179.30 . . 176 31 35 LEU CA C 57.21 . . 177 31 35 LEU CB C 40.66 . . 178 31 35 LEU N N 120.22 . . 179 32 36 GLN H H 8.216 . . 180 32 36 GLN HA H 3.943 . . 181 32 36 GLN C C 177.91 . . 182 32 36 GLN CA C 58.22 . . 183 32 36 GLN CB C 28.02 . . 184 32 36 GLN N N 118.83 . . 185 33 37 ALA H H 7.647 . . 186 33 37 ALA HA H 4.185 . . 187 33 37 ALA C C 179.05 . . 188 33 37 ALA CA C 53.46 . . 189 33 37 ALA CB C 17.72 . . 190 33 37 ALA N N 121.34 . . 191 34 38 ARG H H 7.612 . . 192 34 38 ARG HA H 4.306 . . 193 34 38 ARG C C 176.80 . . 194 34 38 ARG CA C 56.23 . . 195 34 38 ARG CB C 29.65 . . 196 34 38 ARG N N 117.58 . . 197 35 39 SER H H 7.827 . . 198 35 39 SER HA H 4.343 . . 199 35 39 SER C C 175.29 . . 200 35 39 SER CA C 58.93 . . 201 35 39 SER CB C 63.37 . . 202 35 39 SER N N 114.96 . . 203 36 40 GLY H H 8.132 . . 204 36 40 GLY C C 174.84 . . 205 36 40 GLY CA C 45.34 . . 206 36 40 GLY N N 110.34 . . 207 37 41 GLY H H 8.190 . . 208 37 41 GLY C C 174.40 . . 209 37 41 GLY CA C 44.97 . . 210 37 41 GLY N N 108.88 . . 211 38 42 ARG H H 8.118 . . 212 38 42 ARG HA H 4.315 . . 213 38 42 ARG C C 176.90 . . 214 38 42 ARG CA C 56.05 . . 215 38 42 ARG CB C 29.75 . . 216 38 42 ARG N N 120.63 . . 217 39 43 GLY H H 8.374 . . 218 39 43 GLY C C 174.69 . . 219 39 43 GLY CA C 45.12 . . 220 39 43 GLY N N 109.36 . . 221 40 44 GLY H H 7.995 . . 222 40 44 GLY C C 174.68 . . 223 40 44 GLY CA C 45.08 . . 224 40 44 GLY N N 109.06 . . 225 41 45 TRP H H 8.176 . . 226 41 45 TRP HA H 4.399 . . 227 41 45 TRP C C 177.30 . . 228 41 45 TRP CA C 58.58 . . 229 41 45 TRP CB C 28.69 . . 230 41 45 TRP N N 121.26 . . 231 42 46 MET H H 8.120 . . 232 42 46 MET HA H 4.185 . . 233 42 46 MET C C 177.93 . . 234 42 46 MET CA C 57.46 . . 235 42 46 MET CB C 30.92 . . 236 42 46 MET N N 118.57 . . 237 43 47 GLU H H 7.834 . . 238 43 47 GLU HA H 4.199 . . 239 43 47 GLU C C 177.98 . . 240 43 47 GLU CA C 57.52 . . 241 43 47 GLU CB C 27.56 . . 242 43 47 GLU N N 119.60 . . 243 44 48 TRP H H 7.824 . . 244 44 48 TRP HA H 4.492 . . 245 44 48 TRP C C 177.48 . . 246 44 48 TRP CA C 58.96 . . 247 44 48 TRP CB C 28.42 . . 248 44 48 TRP N N 120.89 . . 249 45 49 ASP H H 8.325 . . 250 45 49 ASP HA H 4.352 . . 251 45 49 ASP C C 177.07 . . 252 45 49 ASP CA C 55.95 . . 253 45 49 ASP CB C 38.26 . . 254 45 49 ASP N N 118.21 . . 255 46 50 ARG H H 7.860 . . 256 46 50 ARG HA H 4.101 . . 257 46 50 ARG C C 178.41 . . 258 46 50 ARG CA C 58.44 . . 259 46 50 ARG CB C 29.19 . . 260 46 50 ARG N N 119.51 . . 261 47 51 GLU H H 7.874 . . 262 47 51 GLU HA H 4.287 . . 263 47 51 GLU C C 178.17 . . 264 47 51 GLU CA C 57.81 . . 265 47 51 GLU CB C 27.72 . . 266 47 51 GLU N N 118.47 . . 267 48 52 ILE H H 8.199 . . 268 48 52 ILE HA H 3.929 . . 269 48 52 ILE C C 178.06 . . 270 48 52 ILE CA C 64.03 . . 271 48 52 ILE CB C 36.99 . . 272 48 52 ILE N N 118.80 . . 273 49 53 ASN H H 8.085 . . 274 49 53 ASN HA H 4.599 . . 275 49 53 ASN C C 177.11 . . 276 49 53 ASN CA C 55.70 . . 277 49 53 ASN CB C 38.08 . . 278 49 53 ASN N N 119.58 . . 279 50 54 ASN H H 8.020 . . 280 50 54 ASN HA H 4.534 . . 281 50 54 ASN C C 177.12 . . 282 50 54 ASN CA C 55.06 . . 283 50 54 ASN CB C 37.68 . . 284 50 54 ASN N N 118.69 . . 285 51 55 TYR H H 8.106 . . 286 51 55 TYR HA H 4.534 . . 287 51 55 TYR C C 177.48 . . 288 51 55 TYR CA C 60.43 . . 289 51 55 TYR CB C 37.71 . . 290 51 55 TYR N N 118.43 . . 291 52 56 THR H H 8.247 . . 292 52 56 THR HA H 3.943 . . 293 52 56 THR C C 176.97 . . 294 52 56 THR CA C 66.22 . . 295 52 56 THR CB C 67.58 . . 296 52 56 THR N N 114.47 . . 297 53 57 SER H H 8.064 . . 298 53 57 SER HA H 4.338 . . 299 53 57 SER C C 176.99 . . 300 53 57 SER CA C 61.30 . . 301 53 57 SER CB C 62.02 . . 302 53 57 SER N N 118.26 . . 303 54 58 LEU H H 7.631 . . 304 54 58 LEU HA H 4.250 . . 305 54 58 LEU C C 179.06 . . 306 54 58 LEU CA C 57.69 . . 307 54 58 LEU CB C 40.99 . . 308 54 58 LEU N N 123.95 . . 309 55 59 ILE H H 8.051 . . 310 55 59 ILE HA H 3.719 . . 311 55 59 ILE C C 177.57 . . 312 55 59 ILE CA C 64.52 . . 313 55 59 ILE CB C 36.46 . . 314 55 59 ILE N N 118.77 . . 315 56 60 HIS H H 8.339 . . 316 56 60 HIS HA H 4.255 . . 317 56 60 HIS C C 176.79 . . 318 56 60 HIS CA C 59.09 . . 319 56 60 HIS CB C 27.60 . . 320 56 60 HIS N N 117.77 . . 321 57 61 SER H H 8.137 . . 322 57 61 SER HA H 4.245 . . 323 57 61 SER C C 175.99 . . 324 57 61 SER CA C 61.58 . . 325 57 61 SER CB C 62.28 . . 326 57 61 SER N N 115.35 . . 327 58 62 LEU H H 7.914 . . 328 58 62 LEU HA H 4.162 . . 329 58 62 LEU C C 178.93 . . 330 58 62 LEU CA C 57.29 . . 331 58 62 LEU CB C 41.19 . . 332 58 62 LEU N N 122.54 . . 333 59 63 ILE H H 7.921 . . 334 59 63 ILE HA H 3.789 . . 335 59 63 ILE C C 178.12 . . 336 59 63 ILE CA C 63.83 . . 337 59 63 ILE CB C 37.15 . . 338 59 63 ILE N N 118.01 . . 339 60 64 GLU H H 7.925 . . 340 60 64 GLU HA H 4.134 . . 341 60 64 GLU C C 177.95 . . 342 60 64 GLU CA C 57.56 . . 343 60 64 GLU CB C 27.71 . . 344 60 64 GLU N N 119.64 . . 345 61 65 GLU H H 8.048 . . 346 61 65 GLU HA H 4.245 . . 347 61 65 GLU C C 177.45 . . 348 61 65 GLU CA C 57.10 . . 349 61 65 GLU CB C 27.62 . . 350 61 65 GLU N N 118.99 . . 351 62 66 SER H H 7.893 . . 352 62 66 SER HA H 4.324 . . 353 62 66 SER C C 174.94 . . 354 62 66 SER CA C 59.62 . . 355 62 66 SER CB C 63.13 . . 356 62 66 SER N N 115.26 . . 357 63 67 GLN H H 7.824 . . 358 63 67 GLN C C 176.07 . . 359 63 67 GLN CA C 55.79 . . 360 63 67 GLN CB C 28.70 . . 361 63 67 GLN N N 120.40 . . 362 64 68 ASN H H 8.059 . . 363 64 68 ASN HA H 4.695 . . 364 64 68 ASN C C 175.30 . . 365 64 68 ASN CA C 53.28 . . 366 64 68 ASN CB C 38.34 . . 367 64 68 ASN N N 119.18 . . 368 65 69 GLN H H 8.144 . . 369 65 69 GLN HA H 4.320 . . 370 65 69 GLN C C 175.89 . . 371 65 69 GLN CA C 55.70 . . 372 65 69 GLN CB C 28.53 . . 373 65 69 GLN N N 120.74 . . 374 66 70 GLN H H 8.199 . . 375 66 70 GLN HA H 4.320 . . 376 66 70 GLN C C 175.84 . . 377 66 70 GLN CA C 55.61 . . 378 66 70 GLN CB C 28.67 . . 379 66 70 GLN N N 121.07 . . 380 67 71 GLU H H 8.194 . . 381 67 71 GLU C C 175.20 . . 382 67 71 GLU CA C 55.65 . . 383 67 71 GLU CB C 28.41 . . 384 67 71 GLU N N 122.32 . . 385 68 72 LYS H H 8.194 . . 386 68 72 LYS CA C 56.76 . . 387 68 72 LYS CB C 32.56 . . 388 68 72 LYS N N 127.05 . . stop_ save_