data_18340 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Structural Mechanism for Bax Inhibition by Cytomegalovirus Protein vMIA ; _BMRB_accession_number 18340 _BMRB_flat_file_name bmr18340.str _Entry_type original _Submission_date 2012-03-20 _Accession_date 2012-03-20 _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 Ma Junhe . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 106 "13C chemical shifts" 38 "15N chemical shifts" 11 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2013-02-11 update BMRB 'update entry citation' 2012-12-04 original author 'original release' stop_ save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title 'Structural mechanism of Bax inhibition by cytomegalovirus protein vMIA.' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 23213219 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Ma Junhe . . 2 Edlich Frank . . 3 Bermejo Guillermo A. . 4 Norris Kristi L. . 5 Youle Richard J. . 6 Tjandra Nico . . 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 109 _Journal_issue 51 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 20901 _Page_last 20906 _Year 2012 _Details . save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name Bax+vMIA _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label Bax $entity_1 vMIA $entity_2 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_1 _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common entity_1 _Molecular_mass 21204.494 _Mol_thiol_state . _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 192 _Mol_residue_sequence ; MDGSGEQPRGGGPTSSEQIM KTGALLLQGFIQDRAGRMGG EAPELALDPVPQDASTKKLS ECLKRIGDELDSNMELQRMI AAVDTDSPREVFFRVAADMF SDGNFNWGRVVALFYFASKL VLKALCTKVPELIRTIMGWT LDFLRERLLGWIQDQGGWDG LLSYFGTPTWQTVTIFVAGV LTASLTIWKKMG ; loop_ _Residue_seq_code _Residue_label 1 MET 2 ASP 3 GLY 4 SER 5 GLY 6 GLU 7 GLN 8 PRO 9 ARG 10 GLY 11 GLY 12 GLY 13 PRO 14 THR 15 SER 16 SER 17 GLU 18 GLN 19 ILE 20 MET 21 LYS 22 THR 23 GLY 24 ALA 25 LEU 26 LEU 27 LEU 28 GLN 29 GLY 30 PHE 31 ILE 32 GLN 33 ASP 34 ARG 35 ALA 36 GLY 37 ARG 38 MET 39 GLY 40 GLY 41 GLU 42 ALA 43 PRO 44 GLU 45 LEU 46 ALA 47 LEU 48 ASP 49 PRO 50 VAL 51 PRO 52 GLN 53 ASP 54 ALA 55 SER 56 THR 57 LYS 58 LYS 59 LEU 60 SER 61 GLU 62 CYS 63 LEU 64 LYS 65 ARG 66 ILE 67 GLY 68 ASP 69 GLU 70 LEU 71 ASP 72 SER 73 ASN 74 MET 75 GLU 76 LEU 77 GLN 78 ARG 79 MET 80 ILE 81 ALA 82 ALA 83 VAL 84 ASP 85 THR 86 ASP 87 SER 88 PRO 89 ARG 90 GLU 91 VAL 92 PHE 93 PHE 94 ARG 95 VAL 96 ALA 97 ALA 98 ASP 99 MET 100 PHE 101 SER 102 ASP 103 GLY 104 ASN 105 PHE 106 ASN 107 TRP 108 GLY 109 ARG 110 VAL 111 VAL 112 ALA 113 LEU 114 PHE 115 TYR 116 PHE 117 ALA 118 SER 119 LYS 120 LEU 121 VAL 122 LEU 123 LYS 124 ALA 125 LEU 126 CYS 127 THR 128 LYS 129 VAL 130 PRO 131 GLU 132 LEU 133 ILE 134 ARG 135 THR 136 ILE 137 MET 138 GLY 139 TRP 140 THR 141 LEU 142 ASP 143 PHE 144 LEU 145 ARG 146 GLU 147 ARG 148 LEU 149 LEU 150 GLY 151 TRP 152 ILE 153 GLN 154 ASP 155 GLN 156 GLY 157 GLY 158 TRP 159 ASP 160 GLY 161 LEU 162 LEU 163 SER 164 TYR 165 PHE 166 GLY 167 THR 168 PRO 169 THR 170 TRP 171 GLN 172 THR 173 VAL 174 THR 175 ILE 176 PHE 177 VAL 178 ALA 179 GLY 180 VAL 181 LEU 182 THR 183 ALA 184 SER 185 LEU 186 THR 187 ILE 188 TRP 189 LYS 190 LYS 191 MET 192 GLY stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-08-12 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 4632 "PROTEIN (APOPTOSIS REGULATOR BAX, MEMBRANE ISOFORM ALPHA)" 100.00 192 100.00 100.00 3.06e-135 PDB 1F16 "Solution Structure Of A Pro-Apoptotic Protein Bax" 100.00 192 100.00 100.00 3.06e-135 PDB 2K7W "Bax Activation Is Initiated At A Novel Interaction Site" 100.00 192 100.00 100.00 3.06e-135 PDB 2LR1 "Structural Mechanism For Bax Inhibition By Cytomegalovirus Protein Vmia" 100.00 192 100.00 100.00 3.06e-135 PDB 4BD2 "Bax Domain Swapped Dimer In Complex With Bidbh3" 89.06 174 98.83 98.83 1.46e-117 PDB 4BD6 "Bax Domain Swapped Dimer In Complex With Baxbh3" 89.06 174 98.83 98.83 1.46e-117 PDB 4BD7 "Bax Domain Swapped Dimer Induced By Octylmaltoside" 89.06 174 98.83 98.83 1.46e-117 PDB 4BD8 "Bax Domain Swapped Dimer Induced By Bimbh3 With Chaps" 89.06 174 98.83 98.83 1.46e-117 PDB 4ZIE "Crystal Structure Of Core/latch Dimer Of Bax In Complex With Bimbh3" 86.98 168 98.20 98.80 1.86e-113 PDB 4ZIF "Crystal Structure Of Core/latch Dimer Of Bax In Complex With Bimbh3mini" 86.98 168 98.20 98.80 1.86e-113 PDB 4ZIG "Crystal Structure Of Core/latch Dimer Of Bax In Complex With Bidbh3mini" 86.98 168 98.20 98.80 1.86e-113 PDB 4ZIH "Crystal Structure Of Core/latch Dimer Of Bax In Complex With Bimbh3mini" 85.42 167 98.78 98.78 1.84e-111 PDB 4ZII "Crystal Structure Of Core/latch Dimer Of Baxi66a In Complex With Bidbh3" 88.54 170 98.82 98.82 1.15e-116 DBJ BAC53619 "Bax [Canis lupus familiaris]" 100.00 192 97.40 98.44 1.99e-131 DBJ BAF83765 "unnamed protein product [Homo sapiens]" 100.00 192 100.00 100.00 3.06e-135 DBJ BAI46883 "BCL2-associated X protein [synthetic construct]" 84.38 218 98.77 98.77 5.43e-109 EMBL CAD10744 "bax isoform psi [Homo sapiens]" 90.10 173 100.00 100.00 1.38e-120 EMBL CCF78739 "Bcl associated protein x, partial [Bubalus bubalis]" 74.48 150 98.60 99.30 6.97e-96 GB AAA03619 "Bax alpha [Homo sapiens]" 100.00 192 100.00 100.00 3.06e-135 GB AAA03620 "Bax beta [Homo sapiens]" 84.38 218 98.77 98.77 5.43e-109 GB AAC48806 "bax-alpha [Bos taurus]" 100.00 192 97.40 98.44 1.07e-131 GB AAD22706 "bax epsilon [Homo sapiens]" 64.58 164 100.00 100.00 1.22e-80 GB AAF82094 "Bax zeta [Homo sapiens]" 59.38 114 100.00 100.00 4.86e-75 REF NP_001003011 "apoptosis regulator BAX [Canis lupus familiaris]" 100.00 192 97.40 98.44 1.99e-131 REF NP_001247945 "apoptosis regulator BAX [Macaca mulatta]" 100.00 192 98.44 98.96 1.85e-133 REF NP_001278357 "apoptosis regulator BAX isoform 1 [Homo sapiens]" 82.29 221 100.00 100.00 1.59e-108 REF NP_001278358 "apoptosis regulator BAX gamma [Homo sapiens]" 65.10 181 98.40 98.40 3.98e-81 REF NP_001278360 "apoptosis regulator BAX isoform zeta [Homo sapiens]" 59.38 114 100.00 100.00 4.86e-75 SP O02703 "RecName: Full=Apoptosis regulator BAX" 100.00 192 97.40 98.44 1.07e-131 SP Q07812 "RecName: Full=Apoptosis regulator BAX; AltName: Full=Bcl-2-like protein 4; Short=Bcl2-L-4" 100.00 192 100.00 100.00 3.06e-135 TPG DAA19512 "TPA: apoptosis regulator BAX [Bos taurus]" 100.00 192 97.40 98.44 1.07e-131 stop_ save_ save_entity_2 _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common entity_2 _Molecular_mass 2732.313 _Mol_thiol_state . _Details . _Residue_count 21 _Mol_residue_sequence ; CEALKKALRRHRFLWQRRQR A ; loop_ _Residue_seq_code _Residue_label 1 CYS 2 GLU 3 ALA 4 LEU 5 LYS 6 LYS 7 ALA 8 LEU 9 ARG 10 ARG 11 HIS 12 ARG 13 PHE 14 LEU 15 TRP 16 GLN 17 ARG 18 ARG 19 GLN 20 ARG 21 ALA stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-01-30 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 2LR1 "Structural Mechanism For Bax Inhibition By Cytomegalovirus Protein Vmia" 100.00 21 100.00 100.00 4.32e-04 EMBL CAA35396 "HCMVUL37 [Human herpesvirus 5]" 100.00 487 100.00 100.00 6.91e-04 GB AAK01675 "immediate early protein UL37 [Human herpesvirus 5]" 100.00 162 100.00 100.00 1.89e-04 GB AAK01676 "immediate early protein UL37 [Human herpesvirus 5]" 76.19 162 100.00 100.00 1.86e-01 GB AAK01677 "immediate early protein UL37 [Human herpesvirus 5]" 100.00 161 100.00 100.00 1.65e-04 GB AAK01678 "immediate early protein UL37 [Human herpesvirus 5]" 76.19 162 100.00 100.00 1.86e-01 GB AAK01679 "immediate early protein UL37 [Human herpesvirus 5]" 76.19 162 100.00 100.00 1.86e-01 REF YP_081496 "envelope glycoprotein UL37 [Human herpesvirus 5]" 76.19 488 100.00 100.00 4.44e-01 SP P16778 "RecName: Full=UL37 immediate early glycoprotein; Flags: Precursor [Human herpesvirus 5 strain AD169]" 100.00 487 100.00 100.00 6.91e-04 SP Q6SW94 "RecName: Full=UL37 immediate early glycoprotein; Flags: Precursor [Human herpesvirus 5 strain Merlin]" 76.19 488 100.00 100.00 4.44e-01 TPG DAA00142 "TPA: envelope glycoprotein UL37 [Human herpesvirus 5]" 100.00 487 100.00 100.00 6.91e-04 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_1 human 9606 Eukaryota Metazoa Homo sapiens $entity_2 human 9606 Eukaryota Metazoa Homo sapiens 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_1 'recombinant technology' . . . . pET28 $entity_2 'chemical synthesis' . . . . . stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_2 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $entity_1 0.1 mM 'natural abundance' $entity_2 0.1 mM '[U-100% 13C; U-100% 15N]' 'potassium phosphate' 20 mM 'natural abundance' D2O 10 % '[U-100% 2H]' H2O 90 % 'natural abundance' DTT 0 mM 'natural abundance' stop_ save_ save_sample_1 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $entity_1 0.1 mM '[U-100% 15N]' $entity_2 0.1 mM 'natural abundance' 'potassium phosphate' 20 mM 'natural abundance' D2O 10 % '[U-100% 2H]' H2O 90 % 'natural abundance' DTT 0 mM 'natural abundance' stop_ save_ ############################ # Computer software used # ############################ save_xplor _Saveframe_category software _Name xplor _Version . 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 800 _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_2D_1H-1H_TOCSY_2 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-1H TOCSY' _Sample_label $sample_2 save_ save_2D_1H-1H_NOESY_3 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-1H NOESY' _Sample_label $sample_2 save_ save_3D_HNCO_4 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCO' _Sample_label $sample_2 save_ save_3D_HNCACB_5 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCACB' _Sample_label $sample_2 save_ save_2D_1H-15N_HSQC_6 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-15N HSQC' _Sample_label $sample_2 save_ save_3D_1H-15N_NOESY_7 _Saveframe_category NMR_applied_experiment _Experiment_name '3D 1H-15N NOESY' _Sample_label $sample_2 save_ save_2D_1H-13C_HSQC_8 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-13C HSQC' _Sample_label $sample_2 save_ save_3D_1H-13C_NOESY_9 _Saveframe_category NMR_applied_experiment _Experiment_name '3D 1H-13C NOESY' _Sample_label $sample_2 save_ save_2D_DQF-COSY_10 _Saveframe_category NMR_applied_experiment _Experiment_name '2D DQF-COSY' _Sample_label $sample_2 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 6.2 . pH pressure 1 . atm 'ionic strength' 20 . mM 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 DSS C 13 'methyl protons' ppm 0.00 na indirect . . . 0.251449530 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 '2D 1H-15N HSQC' 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 vMIA _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 1 131 2 GLU H H 8.5528 0.02 1 2 131 2 GLU HA H 4.0841 0.02 1 3 131 2 GLU HB2 H 1.9934 0.02 2 4 131 2 GLU HB3 H 1.9934 0.02 2 5 131 2 GLU HG2 H 2.3759 0.02 2 6 131 2 GLU HG3 H 2.3759 0.02 2 7 132 3 ALA H H 8.6009 0.02 1 8 132 3 ALA HA H 4.1599 0.02 1 9 132 3 ALA HB H 1.3759 0.02 1 10 132 3 ALA CA C 53.6900 0.30 1 11 132 3 ALA CB C 18.5000 0.30 1 12 132 3 ALA N N 123.3000 0.30 1 13 133 4 LEU H H 7.9840 0.02 1 14 133 4 LEU HA H 4.2134 0.02 1 15 133 4 LEU HB2 H 1.6497 0.02 2 16 133 4 LEU HB3 H 1.6497 0.02 2 17 133 4 LEU HG H 1.5138 0.02 1 18 133 4 LEU HD1 H 0.9290 0.02 2 19 133 4 LEU HD2 H 0.9290 0.02 2 20 133 4 LEU CA C 55.9500 0.30 1 21 133 4 LEU CB C 42.0200 0.30 1 22 133 4 LEU CG C 26.7965 0.30 1 23 133 4 LEU CD1 C 24.5637 0.30 1 24 133 4 LEU CD2 C 24.5637 0.30 1 25 133 4 LEU N N 120.4000 0.30 1 26 134 5 LYS H H 7.9880 0.02 1 27 134 5 LYS HA H 4.1397 0.02 1 28 134 5 LYS HB2 H 2.2331 0.02 2 29 134 5 LYS HB3 H 2.2331 0.02 2 30 134 5 LYS HG2 H 1.4954 0.02 2 31 134 5 LYS HG3 H 1.4954 0.02 2 32 134 5 LYS HD2 H 1.8090 0.02 2 33 134 5 LYS HD3 H 1.8090 0.02 2 34 134 5 LYS HE2 H 2.9300 0.02 2 35 134 5 LYS HE3 H 2.9300 0.02 2 36 134 5 LYS CA C 57.7900 0.30 1 37 134 5 LYS CB C 32.6900 0.30 1 38 134 5 LYS CG C 55.2481 0.30 1 39 134 5 LYS N N 120.7000 0.30 1 40 135 6 LYS H H 8.4054 0.02 1 41 135 6 LYS HA H 4.1220 0.02 1 42 135 6 LYS HB2 H 1.8148 0.02 2 43 135 6 LYS HB3 H 1.8148 0.02 2 44 135 6 LYS HG2 H 1.3858 0.02 2 45 135 6 LYS HG3 H 1.3858 0.02 2 46 135 6 LYS HD2 H 1.6706 0.02 2 47 135 6 LYS HD3 H 1.6706 0.02 2 48 135 6 LYS CA C 57.6381 0.30 1 49 135 6 LYS CB C 32.8600 0.30 1 50 135 6 LYS CG C 55.2434 0.30 1 51 135 6 LYS CD C 59.4294 0.30 1 52 135 6 LYS N N 120.9000 0.30 1 53 136 7 ALA H H 8.0854 0.02 1 54 136 7 ALA HA H 4.1839 0.02 1 55 136 7 ALA HB H 1.4085 0.02 1 56 136 7 ALA CA C 53.2100 0.30 1 57 136 7 ALA CB C 18.7700 0.30 1 58 136 7 ALA N N 123.9000 0.30 1 59 137 8 LEU H H 8.1910 0.02 1 60 137 8 LEU HA H 4.2441 0.02 1 61 137 8 LEU HB2 H 1.6840 0.02 2 62 137 8 LEU HB3 H 1.6840 0.02 2 63 137 8 LEU HG H 1.6762 0.02 1 64 137 8 LEU HD1 H 0.9025 0.02 2 65 137 8 LEU HD2 H 0.9025 0.02 2 66 137 8 LEU CA C 55.9469 0.30 1 67 137 8 LEU CB C 42.2381 0.30 1 68 137 8 LEU CG C 57.0813 0.30 1 69 137 8 LEU CD1 C 55.1355 0.30 1 70 137 8 LEU CD2 C 55.1355 0.30 1 71 137 8 LEU N N 120.6000 0.30 1 72 138 9 ARG H H 8.0990 0.02 1 73 138 9 ARG HA H 4.1657 0.02 1 74 138 9 ARG HB2 H 1.7946 0.02 2 75 138 9 ARG HB3 H 1.7946 0.02 2 76 138 9 ARG HG2 H 1.5715 0.02 2 77 138 9 ARG HG3 H 1.5715 0.02 2 78 139 10 ARG H H 8.1630 0.02 1 79 139 10 ARG HA H 4.2030 0.02 1 80 139 10 ARG HB2 H 1.7630 0.02 2 81 139 10 ARG HB3 H 1.7630 0.02 2 82 140 11 HIS H H 8.4475 0.02 1 83 140 11 HIS HA H 4.5035 0.02 1 84 140 11 HIS HB2 H 3.1460 0.02 2 85 140 11 HIS HB3 H 3.1460 0.02 2 86 141 12 ARG H H 8.3205 0.02 1 87 141 12 ARG HA H 4.1669 0.02 1 88 141 12 ARG HB2 H 1.7080 0.02 2 89 141 12 ARG HB3 H 1.7080 0.02 2 90 142 13 PHE H H 8.3012 0.02 1 91 142 13 PHE HA H 4.5173 0.02 1 92 142 13 PHE HB2 H 2.8042 0.02 2 93 142 13 PHE HB3 H 2.8042 0.02 2 94 142 13 PHE CA C 58.1313 0.30 1 95 142 13 PHE CB C 39.3500 0.30 1 96 142 13 PHE CD1 C 132.0182 0.30 1 97 142 13 PHE CD2 C 132.0182 0.30 1 98 142 13 PHE N N 120.3000 0.30 1 99 143 14 LEU H H 8.2699 0.02 1 100 143 14 LEU HA H 4.2415 0.02 1 101 143 14 LEU HB2 H 1.4567 0.02 2 102 143 14 LEU HB3 H 1.4567 0.02 2 103 143 14 LEU HG H 1.6179 0.02 1 104 143 14 LEU HD1 H 0.8781 0.02 2 105 143 14 LEU HD2 H 0.8781 0.02 2 106 143 14 LEU CA C 56.0933 0.30 1 107 143 14 LEU CB C 42.0236 0.30 1 108 143 14 LEU CG C 57.2051 0.30 1 109 143 14 LEU CD1 C 55.0153 0.30 1 110 143 14 LEU CD2 C 55.0153 0.30 1 111 143 14 LEU N N 122.8000 0.30 1 112 144 15 TRP H H 8.0430 0.02 1 113 144 15 TRP HA H 4.4390 0.02 1 114 144 15 TRP HB2 H 3.2180 0.02 2 115 144 15 TRP HB3 H 3.2180 0.02 2 116 144 15 TRP HD1 H 7.2300 0.02 1 117 144 15 TRP HE1 H 10.160 0.02 1 118 145 16 GLN H H 8.0367 0.02 1 119 145 16 GLN HA H 4.0901 0.02 1 120 145 16 GLN HB2 H 1.8666 0.02 2 121 145 16 GLN HB3 H 1.8666 0.02 2 122 145 16 GLN HG2 H 2.1259 0.02 2 123 145 16 GLN HG3 H 2.1259 0.02 2 124 145 16 GLN CA C 56.4910 0.30 1 125 145 16 GLN CB C 29.2600 0.30 1 126 145 16 GLN CG C 24.7900 0.30 1 127 145 16 GLN N N 120.9000 0.30 1 128 146 17 ARG H H 8.0691 0.02 1 129 146 17 ARG HA H 4.0803 0.02 1 130 146 17 ARG HB2 H 1.5349 0.02 2 131 146 17 ARG HB3 H 1.5349 0.02 2 132 147 18 ARG H H 8.0691 0.02 1 133 147 18 ARG HA H 4.0803 0.02 1 134 147 18 ARG HB2 H 1.5349 0.02 2 135 147 18 ARG HB3 H 1.5349 0.02 2 136 148 19 GLN H H 8.3700 0.02 1 137 148 19 GLN HA H 4.0752 0.02 1 138 148 19 GLN HB2 H 2.0468 0.02 2 139 148 19 GLN HB3 H 2.0468 0.02 2 140 148 19 GLN HG2 H 2.2845 0.02 2 141 148 19 GLN HG3 H 2.2845 0.02 2 142 148 19 GLN CA C 55.9610 0.30 1 143 148 19 GLN CB C 29.3100 0.30 1 144 148 19 GLN CG C 24.7900 0.30 1 145 148 19 GLN N N 121.6000 0.30 1 146 149 20 ARG H H 8.1950 0.02 1 147 149 20 ARG HA H 4.0614 0.02 1 148 149 20 ARG HB2 H 1.6978 0.02 2 149 149 20 ARG HB3 H 1.6978 0.02 2 150 150 21 ALA H H 8.3802 0.02 1 151 150 21 ALA HA H 4.25572 0.02 1 152 150 21 ALA HB H 1.3795 0.02 1 153 150 21 ALA CA C 52.3100 0.30 1 154 150 21 ALA CB C 19.5100 0.30 1 155 150 21 ALA N N 126.0000 0.30 1 stop_ save_