data_17003 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Vpr(1-20) Vpr(21-40) Vpr(25-40) ; _BMRB_accession_number 17003 _BMRB_flat_file_name bmr17003.str _Entry_type original _Submission_date 2010-06-16 _Accession_date 2010-06-16 _Entry_origination author _NMR_STAR_version 2.1.1 _Experimental_method NMR _Details 'N-terminal peptides of the HIV-1 Viral protein R Vpr' loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Fossen Torgils . . 2 Solbak Sara . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 2 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 284 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2010-10-14 original author . stop_ save_ ############################# # Citation for this entry # ############################# save_Citation1 _Saveframe_category entry_citation _Citation_full . _Citation_title 'The intriguing Cyclophilin A-HIV-1 Vpr interaction: prolyl cis/trans isomerisation catalysis and specific binding.' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 20920334 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Solbak Sara M. . 2 Reksten Tove R. . 3 Wray Victor . . 4 Bruns Karsten . . 5 Horvli Ole . . 6 Raae Arnt J. . 7 Henklein Petra . . 8 Henklein Peter . . 9 Roder Rene . . 10 Mitzner David . . 11 Schubert Ulrich . . 12 Fossen Torgils . . stop_ _Journal_abbreviation 'BMC Struct. Biol.' _Journal_name_full 'BMC structural biology' _Journal_volume 10 _Journal_issue 1 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 31 _Page_last 31 _Year 2010 _Details . save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name 'N-terminal Vpr peptides' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label Vpr(1-40) $N-terminal_Vpr_peptides Vpr(25-40) $N-terminal_Vpr_peptides 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_N-terminal_Vpr_peptides _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common N-terminal_Vpr_peptides _Molecular_mass . _Mol_thiol_state 'all free' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 40 _Mol_residue_sequence ; MEQAPEDQGPQREPYNEWTL ELLEELKSEAVRHFPRIWLH ; loop_ _Residue_seq_code _Residue_label 1 MET 2 GLU 3 GLN 4 ALA 5 PRO 6 GLU 7 ASP 8 GLN 9 GLY 10 PRO 11 GLN 12 ARG 13 GLU 14 PRO 15 TYR 16 ASN 17 GLU 18 TRP 19 THR 20 LEU 21 GLU 22 LEU 23 LEU 24 GLU 25 GLU 26 LEU 27 LYS 28 SER 29 GLU 30 ALA 31 VAL 32 ARG 33 HIS 34 PHE 35 PRO 36 ARG 37 ILE 38 TRP 39 LEU 40 HIS stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-10-07 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 DBJ BAA93966 "Vpr protein [Human immunodeficiency virus 1]" 100.00 96 97.50 100.00 1.61e-19 DBJ BAA93967 "Vpr protein [Human immunodeficiency virus 1]" 100.00 96 97.50 100.00 1.87e-19 DBJ BAA93972 "Vpr protein [Human immunodeficiency virus 1]" 100.00 96 97.50 100.00 2.64e-19 DBJ BAA93973 "Vpr protein [Human immunodeficiency virus 1]" 100.00 96 97.50 100.00 2.37e-19 DBJ BAA93975 "Vpr protein [Human immunodeficiency virus 1]" 100.00 96 97.50 100.00 2.85e-19 EMBL CAA06949 "vpr protein [Human immunodeficiency virus 1]" 100.00 96 97.50 100.00 4.42e-19 EMBL CAA92863 "vpr protein [Human immunodeficiency virus 1]" 100.00 96 97.50 97.50 1.38e-18 EMBL CAA92864 "vpr protein [Human immunodeficiency virus 1]" 100.00 96 100.00 100.00 1.14e-19 EMBL CAA92870 "vpr protein [Human immunodeficiency virus 1]" 100.00 96 97.50 100.00 3.93e-19 EMBL CAA92871 "vpr protein [Human immunodeficiency virus 1]" 100.00 96 97.50 97.50 1.42e-18 GB AAA21763 "vpr [Human immunodeficiency virus 1]" 100.00 96 100.00 100.00 1.19e-19 GB AAA44871 "vpR protein [Human immunodeficiency virus 1]" 100.00 96 100.00 100.00 1.03e-19 GB AAA44983 "vpr polyprotein [Human immunodeficiency virus 1]" 100.00 96 97.50 100.00 3.27e-19 GB AAA44990 "vpr protein [Human immunodeficiency virus 1]" 100.00 96 100.00 100.00 1.09e-19 GB AAA45055 "vpr protein [Human immunodeficiency virus 1]" 100.00 96 97.50 100.00 3.38e-19 SP P05954 "RecName: Full=Protein Vpr; AltName: Full=R ORF protein; AltName: Full=Viral protein R" 100.00 96 97.50 100.00 3.38e-19 SP P12519 "RecName: Full=Protein Vpr; AltName: Full=R ORF protein; AltName: Full=Viral protein R" 100.00 96 100.00 100.00 1.09e-19 SP P12520 "RecName: Full=Protein Vpr; AltName: Full=R ORF protein; AltName: Full=Viral protein R" 100.00 96 100.00 100.00 1.09e-19 SP P19555 "RecName: Full=Protein Vpr; AltName: Full=R ORF protein; AltName: Full=Viral protein R" 100.00 96 97.50 100.00 4.37e-19 SP P20883 "RecName: Full=Protein Vpr; AltName: Full=R ORF protein; AltName: Full=Viral protein R" 100.00 96 97.50 100.00 3.60e-19 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _ICTVdb_decimal_code _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species _Strain $N-terminal_Vpr_peptides HIV-1 00.061.1.06.009. 11676 virus . Lentivirus HIV NL4-3 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 $N-terminal_Vpr_peptides 'chemical synthesis' . . . . . stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Concentration_min_value _Concentration_max_value _Isotopic_labeling $N-terminal_Vpr_peptides . mM 1 2 'natural abundance' 'Aqueous Phosphate Buffer' 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 '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 . save_ ############################# # NMR applied experiments # ############################# save_2D_1H-1H_TOCSY_1 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-1H TOCSY' _Sample_label $sample_1 save_ save_2D_1H-1H_NOESY_2 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-1H NOESY' _Sample_label $sample_1 save_ save_2D_1H-1H_ROESY_3 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-1H ROESY' _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 300 . K pH 7 . pH pressure 1 . atm 'ionic strength' 0.050 . M 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 H 1 'methyl protons' ppm 0.00 internal direct . . . 1.000000000 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_1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Experiment_label '2D 1H-1H TOCSY' '2D 1H-1H NOESY' '2D 1H-1H ROESY' 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 Vpr(1-40) _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 1 MET HA H 4.43 . 1 2 2 2 GLU H H 8.56 . 1 3 2 2 GLU HA H 4.26 . 1 4 2 2 GLU HB2 H 2.05 . . 5 2 2 GLU HB3 H 1.96 . . 6 2 2 GLU HG2 H 2.27 . . 7 3 3 GLN H H 8.51 . 1 8 3 3 GLN HA H 4.34 . 1 9 3 3 GLN HB2 H 2.09 . . 10 3 3 GLN HB3 H 1.97 . . 11 3 3 GLN HE21 H 7.57 . . 12 3 3 GLN HE22 H 6.82 . . 13 3 3 GLN HG2 H 2.37 . . 14 4 4 ALA H H 8.52 . 1 15 4 4 ALA HA H 4.61 . 1 16 4 4 ALA HB H 1.39 . 1 17 5 5 PRO HA H 4.41 . 1 18 5 5 PRO HB2 H 2.33 . . 19 5 5 PRO HD2 H 3.82 . . 20 5 5 PRO HD3 H 3.68 . . 21 5 5 PRO HG2 H 2.05 . . 22 5 5 PRO HG3 H 1.91 . . 23 6 6 GLU H H 8.64 . 1 24 6 6 GLU HA H 4.24 . 1 25 6 6 GLU HB2 H 2.05 . . 26 6 6 GLU HB3 H 1.95 . . 27 6 6 GLU HG2 H 2.29 . . 28 7 7 ASP H H 8.29 . 1 29 7 7 ASP HA H 4.61 . 1 30 7 7 ASP HB2 H 2.73 . . 31 7 7 ASP HB3 H 2.68 . . 32 8 8 GLN H H 8.26 . 1 33 8 8 GLN HA H 4.37 . 1 34 8 8 GLN HB2 H 2.21 . . 35 8 8 GLN HB3 H 1.97 . . 36 8 8 GLN HE21 H 7.51 . . 37 8 8 GLN HE22 H 6.83 . . 38 8 8 GLN HG2 H 2.38 . . 39 9 9 GLY H H 8.30 . 1 40 9 9 GLY HA2 H 4.10 . . 41 10 10 PRO HA H 4.43 . 1 42 10 10 PRO HB2 H 2.29 . . 43 10 10 PRO HD2 H 3.63 . . 44 10 10 PRO HG2 H 2.02 . . 45 10 10 PRO HG3 H 1.91 . . 46 11 11 GLN H H 8.48 . 1 47 11 11 GLN HA H 4.31 . 1 48 11 11 GLN HB2 H 2.10 . . 49 11 11 GLN HB3 H 1.99 . . 50 11 11 GLN HE21 H 7.51 . . 51 11 11 GLN HE22 H 6.83 . . 52 11 11 GLN HG2 H 2.38 . . 53 11 11 GLN HG3 H 2.21 . . 54 12 12 ARG H H 8.34 . 1 55 12 12 ARG HA H 4.34 . 1 56 12 12 ARG HB2 H 1.84 . . 57 12 12 ARG HB3 H 1.75 . . 58 12 12 ARG HD2 H 3.18 . . 59 12 12 ARG HG2 H 1.62 . . 60 13 13 GLU H H 8.45 . 1 61 13 13 GLU HA H 4.56 . 1 62 13 13 GLU HB2 H 2.00 . . 63 13 13 GLU HB3 H 1.87 . . 64 13 13 GLU HG2 H 2.30 . . 65 14 14 PRO HA H 4.36 . 1 66 14 14 PRO HB2 H 2.22 . . 67 14 14 PRO HB3 H 1.98 . . 68 14 14 PRO HD2 H 3.78 . . 69 14 14 PRO HD3 H 3.66 . . 70 14 14 PRO HG2 H 1.83 . . 71 15 15 TYR H H 8.09 . 1 72 15 15 TYR HA H 4.50 . 1 73 15 15 TYR HB2 H 2.99 . . 74 15 15 TYR HD1 H 7.09 . . 75 15 15 TYR HD2 H 7.09 . . 76 15 15 TYR HE1 H 6.81 . . 77 15 15 TYR HE2 H 6.81 . . 78 16 16 ASN H H 8.12 . 1 79 16 16 ASN HA H 4.58 . 1 80 16 16 ASN HB2 H 2.60 . . 81 16 16 ASN HD21 H 7.50 . . 82 16 16 ASN HD22 H 6.84 . . 83 17 17 GLU H H 8.32 . 1 84 17 17 GLU HA H 4.11 . 1 85 17 17 GLU HB2 H 1.90 . . 86 17 17 GLU HB3 H 1.83 . . 87 17 17 GLU HG2 H 2.04 . . 88 18 18 TRP H H 8.07 . 1 89 18 18 TRP HA H 4.71 . 1 90 18 18 TRP HB2 H 3.28 . . 91 18 18 TRP HB3 H 3.36 . . 92 18 18 TRP HD1 H 7.26 . 1 93 18 18 TRP HE1 H 10.10 . 1 94 18 18 TRP HE3 H 7.63 . 1 95 18 18 TRP HH2 H 7.25 . 1 96 18 18 TRP HZ2 H 7.49 . 1 97 18 18 TRP HZ3 H 7.15 . 1 98 19 19 THR H H 7.81 . 1 99 19 19 THR HA H 4.21 . 1 100 19 19 THR HB H 4.13 . 1 101 19 19 THR HG2 H 1.08 . 1 102 20 20 LEU H H 7.89 . 1 103 20 20 LEU HA H 4.23 . 1 104 20 20 LEU HB2 H 1.60 . . 105 20 20 LEU HD1 H 0.92 . . 106 20 20 LEU HD2 H 0.87 . . 107 21 21 GLU HA H 4.38 . 1 108 21 21 GLU HB2 H 1.93 . . 109 21 21 GLU HB3 H 2.24 . . 110 22 22 LEU H H 8.43 . 1 111 22 22 LEU HA H 4.32 . 1 112 22 22 LEU HB2 H 1.62 . . 113 22 22 LEU HD1 H 0.88 . . 114 22 22 LEU HG H 1.62 . 1 115 23 23 LEU H H 8.19 . 1 116 23 23 LEU HA H 4.31 . 1 117 23 23 LEU HB2 H 1.69 . . 118 23 23 LEU HD1 H 0.88 . . 119 24 24 GLU H H 8.38 . 1 120 24 24 GLU HA H 4.20 . 1 121 24 24 GLU HB2 H 1.97 . . 122 24 24 GLU HG2 H 2.23 . . 123 25 25 GLU H H 8.41 . 1 124 25 25 GLU HA H 4.21 . 1 125 25 25 GLU HB2 H 1.98 . . 126 25 25 GLU HG2 H 2.23 . . 127 26 26 LEU H H 8.05 . 1 128 26 26 LEU HA H 4.12 . 1 129 26 26 LEU HB2 H 1.72 . . 130 26 26 LEU HD1 H 1.05 . . 131 26 26 LEU HD2 H 0.77 . . 132 27 27 LYS H H 8.23 . 1 133 27 27 LYS HA H 4.30 . 1 134 27 27 LYS HB2 H 1.80 . . 135 27 27 LYS HD2 H 1.68 . . 136 27 27 LYS HE2 H 2.96 . . 137 27 27 LYS HG2 H 1.43 . . 138 27 27 LYS HZ H 7.22 . 1 139 28 28 SER H H 8.21 . 1 140 28 28 SER HA H 4.40 . 1 141 28 28 SER HB2 H 3.87 . . 142 29 29 GLU H H 8.44 . 1 143 29 29 GLU HA H 4.23 . 1 144 29 29 GLU HB2 H 2.08 . . 145 29 29 GLU HB3 H 1.95 . . 146 29 29 GLU HG2 H 2.28 . . 147 30 30 ALA H H 8.15 . 1 148 30 30 ALA HA H 4.25 . 1 149 30 30 ALA HB H 1.38 . 1 150 31 31 VAL H H 7.85 . 1 151 31 31 VAL HA H 3.97 . 1 152 31 31 VAL HB H 2.02 . 1 153 31 31 VAL HG1 H 0.87 . . 154 32 32 ARG H H 8.11 . 1 155 32 32 ARG HA H 4.20 . 1 156 32 32 ARG HB2 H 1.64 . . 157 32 32 ARG HD2 H 3.11 . . 158 32 32 ARG HE H 6.98 . 1 159 32 32 ARG HG2 H 1.47 . . 160 33 33 HIS H H 8.15 . 1 161 33 33 HIS HA H 4.60 . 1 162 33 33 HIS HB2 H 3.11 . . 163 33 33 HIS HB3 H 3.00 . . 164 33 33 HIS HD2 H 7.03 . 1 165 33 33 HIS HE1 H 8.02 . 1 166 34 34 PHE H H 8.17 . 1 167 34 34 PHE HA H 4.81 . 1 168 34 34 PHE HB2 H 3.11 . . 169 34 34 PHE HB3 H 2.89 . . 170 34 34 PHE HD1 H 7.23 . . 171 34 34 PHE HD2 H 7.23 . . 172 34 34 PHE HE1 H 7.31 . . 173 34 34 PHE HE2 H 7.31 . . 174 34 34 PHE HZ H 7.27 . 1 175 35 35 PRO HA H 4.38 . 1 176 35 35 PRO HB2 H 2.24 . . 177 35 35 PRO HD2 H 3.66 . . 178 35 35 PRO HD3 H 3.46 . . 179 35 35 PRO HG2 H 1.92 . . 180 35 35 PRO HG3 H 1.83 . . 181 36 36 ARG H H 8.35 . 1 182 36 36 ARG HA H 4.18 . 1 183 36 36 ARG HB2 H 1.66 . . 184 36 36 ARG HD2 H 3.08 . . 185 36 36 ARG HE H 6.98 . 1 186 36 36 ARG HG2 H 1.52 . . 187 37 37 ILE H H 8.00 . 1 188 37 37 ILE HA H 4.12 . 1 189 37 37 ILE HB H 1.78 . 1 190 37 37 ILE HG12 H 1.36 . . 191 37 37 ILE HG13 H 1.13 . . 192 37 37 ILE HG2 H 0.80 . 1 193 38 38 TRP H H 8.23 . 1 194 38 38 TRP HA H 4.76 . 1 195 38 38 TRP HB2 H 3.23 . . 196 38 38 TRP HB3 H 3.13 . . 197 38 38 TRP HD1 H 7.15 . 1 198 38 38 TRP HE1 H 10.13 . 1 199 38 38 TRP HE3 H 7.60 . 1 200 38 38 TRP HH2 H 7.20 . 1 201 38 38 TRP HZ2 H 7.45 . 1 202 38 38 TRP HZ3 H 7.10 . 1 203 39 39 LEU H H 8.02 . 1 204 39 39 LEU HA H 4.24 . 1 205 39 39 LEU HB2 H 1.41 . . 206 39 39 LEU HD1 H 0.81 . . 207 40 40 HIS H H 7.93 . 1 208 40 40 HIS HA H 4.50 . 1 209 40 40 HIS HB2 H 2.94 . . 210 40 40 HIS HB3 H 3.10 . . 211 40 40 HIS HD2 H 6.98 . 1 212 40 40 HIS HE1 H 7.99 . 1 stop_ save_ save_assigned_chem_shift_list_1_2 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Experiment_label '2D 1H-1H TOCSY' '2D 1H-1H NOESY' '2D 1H-1H ROESY' 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 Vpr(25-40) _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 27 27 LYS H H 8.53 . 1 2 27 27 LYS HA H 4.33 . 1 3 27 27 LYS HB2 H 1.80 . . 4 27 27 LYS HD2 H 2.96 . . 5 27 27 LYS HG2 H 1.41 . . 6 27 27 LYS HG3 H 1.67 . . 7 28 28 SER H H 8.32 . 1 8 28 28 SER HA H 4.40 . 1 9 28 28 SER HB2 H 3.84 . . 10 29 29 GLU H H 8.45 . 1 11 29 29 GLU HA H 4.26 . 1 12 29 29 GLU HB2 H 2.05 . . 13 29 29 GLU HB3 H 1.91 . . 14 29 29 GLU HG2 H 2.25 . . 15 30 30 ALA H H 8.20 . 1 16 30 30 ALA HA H 4.27 . 1 17 30 30 ALA HB H 1.35 . 1 18 31 31 VAL H H 7.94 . 1 19 31 31 VAL HA H 3.97 . 1 20 31 31 VAL HB H 1.99 . 1 21 31 31 VAL HG1 H 0.90 . . 22 31 31 VAL HG2 H 0.81 . . 23 32 32 ARG H H 8.21 . 1 24 32 32 ARG HA H 4.23 . 1 25 32 32 ARG HB2 H 1.63 . . 26 32 32 ARG HD2 H 3.11 . . 27 32 32 ARG HG2 H 1.50 . . 28 33 33 HIS H H 8.29 . 1 29 33 33 HIS HA H 4.73 . 1 30 33 33 HIS HB2 H 3.19 . . 31 33 33 HIS HB3 H 3.15 . . 32 33 33 HIS HD2 H 7.14 . 1 33 33 33 HIS HE1 H 8.25 . 1 34 34 34 PHE H H 8.19 . 1 35 34 34 PHE HA H 4.75 . 1 36 34 34 PHE HB2 H 3.11 . . 37 34 34 PHE HB3 H 2.85 . . 38 34 34 PHE HD1 H 7.22 . . 39 34 34 PHE HD2 H 7.22 . . 40 34 34 PHE HE1 H 7.30 . . 41 34 34 PHE HE2 H 7.30 . . 42 35 35 PRO HA H 4.37 . 1 43 35 35 PRO HB2 H 2.24 . . 44 35 35 PRO HB3 H 1.93 . . 45 35 35 PRO HD2 H 3.65 . . 46 35 35 PRO HD3 H 3.47 . . 47 35 35 PRO HG2 H 1.85 . . 48 36 36 ARG H H 8.34 . 1 49 36 36 ARG HA H 4.18 . 1 50 36 36 ARG HB2 H 1.65 . . 51 36 36 ARG HD2 H 3.07 . . 52 36 36 ARG HG2 H 1.51 . . 53 37 37 ILE H H 8.00 . 1 54 37 37 ILE HA H 4.12 . 1 55 38 38 TRP H H 8.24 . 1 56 38 38 TRP HA H 4.70 . 1 57 38 38 TRP HB2 H 3.22 . . 58 38 38 TRP HB3 H 3.11 . . 59 38 38 TRP HD1 H 7.14 . 1 60 38 38 TRP HE1 H 10.13 . 1 61 38 38 TRP HE3 H 7.61 . 1 62 38 38 TRP HH2 H 7.21 . 1 63 38 38 TRP HZ2 H 7.45 . 1 64 38 38 TRP HZ3 H 7.12 . 1 65 39 39 LEU H H 8.00 . 1 66 39 39 LEU HA H 4.23 . 1 67 40 40 HIS H H 7.85 . 1 68 40 40 HIS HA H 4.47 . 1 69 40 40 HIS HB2 H 3.07 . . 70 40 40 HIS HB3 H 2.91 . . 71 40 40 HIS HD2 H 7.22 . 1 72 40 40 HIS HE1 H 8.16 . 1 stop_ save_