data_15969 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Heteronuclear NMR assignments for the dimeric human hepatitis B virus core protein under capsid dissociating conditions ; _BMRB_accession_number 15969 _BMRB_flat_file_name bmr15969.str _Entry_type original _Submission_date 2008-10-01 _Accession_date 2008-10-01 _Entry_origination author _NMR_STAR_version 2.1.1 _Experimental_method NMR _Details ; 13C, 15N, 1H chemical shifts of the dimeric human hepatitis B virus core protein (residues 1 - 149) acquired at 298 K and pH 9.5 ; loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Freund Stefan M.V. . 2 Johnson Christopher M. . 3 Jaulent Agnes . . 4 Ferguson Neil . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 100 "13C chemical shifts" 327 "15N chemical shifts" 97 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2009-03-20 update BMRB 'update entry citation' 2009-02-16 original author 'original release' stop_ save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title 'Moving towards high resolution descriptions of the molecular interactions and structural rearrangements of the human hepatitis B core protein' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 18952101 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Freund Stefan M.V. . 2 Johnson Christopher M. . 3 Jaulent Agnes . . 4 Ferguson Neil . . stop_ _Journal_abbreviation 'J. Mol. Biol.' _Journal_name_full 'Journal of molecular biology' _Journal_volume 384 _Journal_issue 5 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 1301 _Page_last 1303 _Year 2008 _Details . loop_ _Keyword allostery anti-viral 'hepatitis B virus' 'shift mapping' TROSY stop_ save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name 'Hepatitis B core protein homodimer' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'Hepatitis B virus coat protein monomer, chain 1' $Hepatitis_B_virus_coat_protein 'Hepatitis B virus coat protein monomer, chain 2' $Hepatitis_B_virus_coat_protein stop_ _System_molecular_weight 33540 _System_physical_state native _System_oligomer_state ? _System_paramagnetic no _System_thiol_state . loop_ _Magnetic_equivalence_ID _Magnetically_equivalent_system_component 1 'Hepatitis B virus coat protein monomer, chain 1' 1 'Hepatitis B virus coat protein monomer, chain 2' stop_ loop_ _Biological_function 'Homodimer formed by coat protein monomers are basic building block of hepatitis B nucleocapsid cores' stop_ _Database_query_date . _Details ; Homodimer formed by the human hepatitis B core protein (residues 1-149). The deposited assignments correspond to a homodimer where each monomer is magnetically equivalent. In nature, this homodimer self-associates into a complex of 120 homodimers to give a virus capsid complex. In the capsid form, for which a crystal structure exists, each homodimer contains a disulphide linkage connecting Cys61 of each monomer. However, under the conditions of our study, we deliberately used thiol reductants to reduce thiol linkages. Thus, it is not clear whether the disulphide linkage is present under the conditions of our study, nor is there NMR evidence to support/refute this. ; save_ ######################## # Monomeric polymers # ######################## save_Hepatitis_B_virus_coat_protein _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common Hepatitis_B_virus_coat_protein _Molecular_mass 33540 _Mol_thiol_state unknown loop_ _Biological_function 'Viral capsid core protein' stop_ _Details ; The dimeric coat protein corresponds to residues 1-149 fragment originating from the full length human hepatitis B core protein (183 residues in untruncated form) ; ############################## # Polymer residue sequence # ############################## _Residue_count 149 _Mol_residue_sequence ; MDIDPYKEFGATVELLSFLP SDFFPSVRDLLDTAAALYRD ALESPEHCSPHHTALRQAIL CWGDLMTLATWVGTNLEDPA SRDLVVSYVNTNVGLKFRQL LWFHISCLTFGRETVLEYLV SFGVWIRTPPAYRPPNAPIL STLPETTVV ; loop_ _Residue_seq_code _Residue_label 1 MET 2 ASP 3 ILE 4 ASP 5 PRO 6 TYR 7 LYS 8 GLU 9 PHE 10 GLY 11 ALA 12 THR 13 VAL 14 GLU 15 LEU 16 LEU 17 SER 18 PHE 19 LEU 20 PRO 21 SER 22 ASP 23 PHE 24 PHE 25 PRO 26 SER 27 VAL 28 ARG 29 ASP 30 LEU 31 LEU 32 ASP 33 THR 34 ALA 35 ALA 36 ALA 37 LEU 38 TYR 39 ARG 40 ASP 41 ALA 42 LEU 43 GLU 44 SER 45 PRO 46 GLU 47 HIS 48 CYS 49 SER 50 PRO 51 HIS 52 HIS 53 THR 54 ALA 55 LEU 56 ARG 57 GLN 58 ALA 59 ILE 60 LEU 61 CYS 62 TRP 63 GLY 64 ASP 65 LEU 66 MET 67 THR 68 LEU 69 ALA 70 THR 71 TRP 72 VAL 73 GLY 74 THR 75 ASN 76 LEU 77 GLU 78 ASP 79 PRO 80 ALA 81 SER 82 ARG 83 ASP 84 LEU 85 VAL 86 VAL 87 SER 88 TYR 89 VAL 90 ASN 91 THR 92 ASN 93 VAL 94 GLY 95 LEU 96 LYS 97 PHE 98 ARG 99 GLN 100 LEU 101 LEU 102 TRP 103 PHE 104 HIS 105 ILE 106 SER 107 CYS 108 LEU 109 THR 110 PHE 111 GLY 112 ARG 113 GLU 114 THR 115 VAL 116 LEU 117 GLU 118 TYR 119 LEU 120 VAL 121 SER 122 PHE 123 GLY 124 VAL 125 TRP 126 ILE 127 ARG 128 THR 129 PRO 130 PRO 131 ALA 132 TYR 133 ARG 134 PRO 135 PRO 136 ASN 137 ALA 138 PRO 139 ILE 140 LEU 141 SER 142 THR 143 LEU 144 PRO 145 GLU 146 THR 147 THR 148 VAL 149 VAL 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 PDB 2G33 "Human Hepatitis B Virus T4 Capsid, Strain Adyw" 100.00 150 97.99 97.99 2.67e-100 PDB 2G34 "Human Hepatitis B Virus T4 Capsid Strain Adyw Complexed With Assembly Effector Hap1" 100.00 150 97.99 97.99 2.67e-100 PDB 2QIJ "Hepatitis B Capsid Protein With An N-Terminal Extension Modelled Into 8.9 A Data" 97.99 157 100.00 100.00 2.04e-101 PDB 3KXS "Crystal Structure Of Hbv Capsid Mutant Dimer (Oxy Form), Strain Adyw" 95.97 143 99.30 99.30 3.08e-98 PDB 3V6Z "Crystal Structure Of Hepatitis B Virus E-antigen" 100.00 159 97.99 97.99 5.01e-100 PDB 4BMG "Crystal Structure Of Hexameric Hbc149 Y132a" 100.00 154 99.33 99.33 2.44e-102 PDB 4G93 "Crystal Structure Of The Human Hepatitis B Virus T = 4 Capsid, Adyw Strain, In Complex With The Phenylpropenamide Assembly Acce" 100.00 150 97.99 97.99 2.67e-100 DBJ BAA85372 "core [Hepatitis B virus]" 100.00 183 97.32 100.00 5.29e-102 DBJ BAA85376 "precore/core [Hepatitis B virus]" 100.00 212 98.66 100.00 3.49e-102 EMBL CAA59662 "core [Hepatitis B virus]" 100.00 183 97.32 99.33 3.81e-102 EMBL CAM58608 "precore protein [Hepatitis B virus]" 100.00 212 97.32 99.33 6.02e-101 EMBL CAM58609 "core protein [Hepatitis B virus]" 100.00 183 97.32 99.33 6.03e-102 EMBL CAM58712 "core protein [Hepatitis B virus]" 100.00 183 97.32 99.33 6.03e-102 EMBL CAM58713 "core protein [Hepatitis B virus]" 100.00 183 97.32 99.33 6.03e-102 GB AAA02846 "precore protein, partial [Hepatitis B virus]" 55.03 111 98.78 100.00 1.99e-50 GB AAA02847 "core protein, partial [Hepatitis B virus]" 55.03 82 98.78 100.00 9.75e-51 GB AAA45486 "core antigen [Hepatitis B virus]" 100.00 183 100.00 100.00 4.48e-104 GB AAL31811 "core protein [Hepatitis B virus]" 100.00 183 98.66 100.00 4.74e-103 GB AAL31812 "core protein [Hepatitis B virus]" 100.00 183 98.66 100.00 4.74e-103 SP P03147 "RecName: Full=Capsid protein; AltName: Full=Core antigen; AltName: Full=Core protein; AltName: Full=HBcAg; AltName: Full=p21.5" 100.00 183 100.00 100.00 4.48e-104 SP Q9QMI2 "RecName: Full=Capsid protein; AltName: Full=Core antigen; AltName: Full=Core protein; AltName: Full=HBcAg; AltName: Full=p21.5" 100.00 183 97.32 100.00 5.29e-102 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species _Strain $Hepatitis_B_virus_coat_protein 'Hepatitis B virus' 10407 Viruses . Orthohepadnavirus 'Hepatitis B virus' 'sub type adyw' 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 $Hepatitis_B_virus_coat_protein 'recombinant technology' . Escherichia coli 'BL21 (de3)' pT7-SC 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 _Isotopic_labeling $Hepatitis_B_virus_coat_protein 150 uM '[U-13C; U-15N; U-2H]' stop_ save_ ############################ # Computer software used # ############################ save_Felix _Saveframe_category software _Name FELIX _Version 2004 loop_ _Vendor _Address _Electronic_address Accelrys . . stop_ loop_ _Task 'chemical shift assignment' stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_AV700 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model Avance _Field_strength 700 _Details . save_ save_AV900 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model Avance _Field_strength 900 _Details . save_ ############################# # NMR applied experiments # ############################# save_2D_1H-15N_TROSY_1 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-15N TROSY' _Sample_label $sample_1 save_ save_3D_TROSY_HNCO_2 _Saveframe_category NMR_applied_experiment _Experiment_name '3D TROSY_HNCO' _Sample_label $sample_1 save_ save_3D_TROSY-HNCA_3 _Saveframe_category NMR_applied_experiment _Experiment_name '3D TROSY-HNCA' _Sample_label $sample_1 save_ save_3D_TROSY-HN(CA)CB_4 _Saveframe_category NMR_applied_experiment _Experiment_name '3D TROSY-HN(CA)CB' _Sample_label $sample_1 save_ save_3D_TROSY-HN(CO)CA_5 _Saveframe_category NMR_applied_experiment _Experiment_name '3D TROSY-HN(CO)CA' _Sample_label $sample_1 save_ save_3D_1H-15N_NOESY_6 _Saveframe_category NMR_applied_experiment _Experiment_name '3D 1H-15N NOESY' _Sample_label $sample_1 save_ save_3D_TROSY-HN(COCA)CB_7 _Saveframe_category NMR_applied_experiment _Experiment_name '3D TROSY-HN(COCA)CB' _Sample_label $sample_1 save_ save_3D_TROSY-HN(CA)CO_8 _Saveframe_category NMR_applied_experiment _Experiment_name '3D TROSY-HN(CA)CO' _Sample_label $sample_1 save_ save_2D_1H-15N_TROSY_9 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-15N TROSY' _Sample_label $sample_1 save_ save_3D_HN(CACO)NH_10 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HN(CACO)NH' _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 'ionic strength' '< 30' . mM pH 9.5 . 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 water C 13 protons ppm 4.75 internal indirect . . . 0.25144953 water H 1 protons ppm 4.75 internal direct . . . 1.0 water N 15 protons ppm 4.75 internal 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_ _Software_label $Felix stop_ loop_ _Experiment_label '2D 1H-15N TROSY' 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 'Hepatitis B virus coat protein monomer, chain 1' _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 C C 179.04 0.3 1 2 1 1 MET CA C 56.31 0.3 1 3 1 1 MET CB C 37.31 0.3 1 4 2 2 ASP H H 9.461 0.05 1 5 2 2 ASP CA C 52.69 0.3 1 6 2 2 ASP CB C 40.67 0.3 1 7 2 2 ASP N N 128.274 0.3 1 8 3 3 ILE H H 7.886 0.05 1 9 3 3 ILE C C 174.53 0.3 1 10 3 3 ILE CA C 59.36 0.3 1 11 3 3 ILE CB C 39.07 0.3 1 12 3 3 ILE N N 123.332 0.3 1 13 4 4 ASP H H 9.436 0.05 1 14 4 4 ASP CA C 49.73 0.3 1 15 4 4 ASP CB C 42.4 0.3 1 16 4 4 ASP N N 131.086 0.3 1 17 5 5 PRO C C 177.19 0.3 1 18 5 5 PRO CA C 63.19 0.3 1 19 5 5 PRO CB C 30.72 0.3 1 20 6 6 TYR H H 9.162 0.05 1 21 6 6 TYR C C 178.19 0.3 1 22 6 6 TYR CA C 59.12 0.3 1 23 6 6 TYR CB C 37.7 0.3 1 24 6 6 TYR N N 117.926 0.3 1 25 7 7 LYS H H 7.484 0.05 1 26 7 7 LYS C C 180.88 0.3 1 27 7 7 LYS CA C 60.07 0.3 1 28 7 7 LYS CB C 32.14 0.3 1 29 7 7 LYS N N 125.693 0.3 1 30 9 9 PHE C C 174.45 0.3 1 31 9 9 PHE CA C 57.39 0.3 1 32 9 9 PHE CB C 40.55 0.3 1 33 10 10 GLY H H 7.560 0.05 1 34 10 10 GLY C C 173.65 0.3 1 35 10 10 GLY CA C 45.34 0.3 1 36 10 10 GLY N N 103.764 0.3 1 37 11 11 ALA H H 7.641 0.05 1 38 11 11 ALA C C 173.46 0.3 1 39 11 11 ALA CA C 48.38 0.3 1 40 11 11 ALA CB C 21.23 0.3 1 41 11 11 ALA N N 121.378 0.3 1 42 12 12 THR H H 6.419 0.05 1 43 12 12 THR C C 175 0.3 1 44 12 12 THR CA C 58.85 0.3 1 45 12 12 THR CB C 73.9 0.3 1 46 12 12 THR N N 105.252 0.3 1 47 13 13 VAL H H 10.407 0.05 1 48 13 13 VAL C C 178.93 0.3 1 49 13 13 VAL CA C 65.76 0.3 1 50 13 13 VAL CB C 31.3 0.3 1 51 13 13 VAL N N 123.148 0.3 1 52 14 14 GLU C C 178.81 0.3 1 53 14 14 GLU CA C 58.98 0.3 1 54 14 14 GLU CB C 28.67 0.3 1 55 15 15 LEU H H 7.736 0.05 1 56 15 15 LEU C C 178.7 0.3 1 57 15 15 LEU CA C 57.22 0.3 1 58 15 15 LEU CB C 41.5 0.3 1 59 15 15 LEU N N 120.375 0.3 1 60 16 16 LEU H H 6.816 0.05 1 61 16 16 LEU C C 179.16 0.3 1 62 16 16 LEU CA C 55.1 0.3 1 63 16 16 LEU CB C 39.88 0.3 1 64 16 16 LEU N N 119.000 0.3 1 65 17 17 SER H H 7.668 0.05 1 66 17 17 SER C C 174.38 0.3 1 67 17 17 SER CA C 60.39 0.3 1 68 17 17 SER CB C 62.72 0.3 1 69 17 17 SER N N 114.259 0.3 1 70 18 18 PHE H H 6.815 0.05 1 71 18 18 PHE C C 176.38 0.3 1 72 18 18 PHE CA C 58.88 0.3 1 73 18 18 PHE CB C 38.39 0.3 1 74 18 18 PHE N N 118.085 0.3 1 75 19 19 LEU H H 6.986 0.05 1 76 19 19 LEU C C 174.5 0.3 1 77 19 19 LEU CA C 52.91 0.3 1 78 19 19 LEU CB C 39.3 0.3 1 79 19 19 LEU N N 120.312 0.3 1 80 21 21 SER C C 175.22 0.3 1 81 21 21 SER CA C 62.9 0.3 1 82 21 21 SER CB C 69.68 0.3 1 83 22 22 ASP H H 7.490 0.05 1 84 22 22 ASP C C 174.3 0.3 1 85 22 22 ASP CA C 54.68 0.3 1 86 22 22 ASP CB C 39.08 0.3 1 87 22 22 ASP N N 117.192 0.3 1 88 23 23 PHE H H 7.527 0.05 1 89 23 23 PHE C C 176.64 0.3 1 90 23 23 PHE CA C 54.64 0.3 1 91 23 23 PHE CB C 40.46 0.3 1 92 23 23 PHE N N 119.546 0.3 1 93 25 25 PRO C C 174.78 0.3 1 94 25 25 PRO CA C 61.7 0.3 1 95 25 25 PRO CB C 31.76 0.3 1 96 26 26 SER H H 8.745 0.05 1 97 26 26 SER C C 174.18 0.3 1 98 26 26 SER CA C 57.2 0.3 1 99 26 26 SER CB C 64.05 0.3 1 100 26 26 SER N N 115.59 0.3 1 101 27 27 VAL H H 8.695 0.05 1 102 27 27 VAL C C 177.41 0.3 1 103 27 27 VAL CA C 67.02 0.3 1 104 27 27 VAL CB C 30.43 0.3 1 105 27 27 VAL N N 120.748 0.3 1 106 28 28 ARG H H 8.078 0.05 1 107 28 28 ARG C C 178.01 0.3 1 108 28 28 ARG CA C 58.42 0.3 1 109 28 28 ARG CB C 29.62 0.3 1 110 28 28 ARG N N 118.378 0.3 1 111 29 29 ASP H H 7.743 0.05 1 112 29 29 ASP C C 179.72 0.3 1 113 29 29 ASP CA C 57.23 0.3 1 114 29 29 ASP CB C 39.54 0.3 1 115 29 29 ASP N N 119.647 0.3 1 116 30 30 LEU H H 8.126 0.05 1 117 30 30 LEU C C 178.9 0.3 1 118 30 30 LEU CA C 58.05 0.3 1 119 30 30 LEU CB C 41.69 0.3 1 120 30 30 LEU N N 123.049 0.3 1 121 31 31 LEU H H 8.803 0.05 1 122 31 31 LEU C C 180.47 0.3 1 123 31 31 LEU CA C 56.88 0.3 1 124 31 31 LEU CB C 40.33 0.3 1 125 31 31 LEU N N 120.445 0.3 1 126 32 32 ASP H H 8.436 0.05 1 127 32 32 ASP C C 179.76 0.3 1 128 32 32 ASP CA C 56.33 0.3 1 129 32 32 ASP CB C 39.29 0.3 1 130 32 32 ASP N N 121.567 0.3 1 131 33 33 THR H H 8.274 0.05 1 132 33 33 THR C C 175.57 0.3 1 133 33 33 THR CA C 66.73 0.3 1 134 33 33 THR CB C 67.99 0.3 1 135 33 33 THR N N 120.882 0.3 1 136 34 34 ALA H H 8.667 0.05 1 137 34 34 ALA C C 178.93 0.3 1 138 34 34 ALA CA C 55.2 0.3 1 139 34 34 ALA CB C 16.05 0.3 1 140 34 34 ALA N N 123.066 0.3 1 141 35 35 ALA H H 8.028 0.05 1 142 35 35 ALA C C 179.32 0.3 1 143 35 35 ALA CA C 54.14 0.3 1 144 35 35 ALA CB C 17.87 0.3 1 145 35 35 ALA N N 117.980 0.3 1 146 36 36 ALA H H 8.102 0.05 1 147 36 36 ALA C C 179.99 0.3 1 148 36 36 ALA CA C 54.31 0.3 1 149 36 36 ALA CB C 17.87 0.3 1 150 36 36 ALA N N 120.619 0.3 1 151 37 37 LEU H H 7.861 0.05 1 152 37 37 LEU C C 179.36 0.3 1 153 37 37 LEU CA C 55.64 0.3 1 154 37 37 LEU CB C 42.01 0.3 1 155 37 37 LEU N N 113.596 0.3 1 156 38 38 TYR H H 7.735 0.05 1 157 38 38 TYR C C 176.23 0.3 1 158 38 38 TYR CA C 56.67 0.3 1 159 38 38 TYR CB C 38.96 0.3 1 160 38 38 TYR N N 113.763 0.3 1 161 39 39 ARG H H 7.535 0.05 1 162 39 39 ARG C C 177.02 0.3 1 163 39 39 ARG CA C 61.44 0.3 1 164 39 39 ARG CB C 29.7 0.3 1 165 39 39 ARG N N 121.806 0.3 1 166 41 41 ALA C C 181.84 0.3 1 167 41 41 ALA CA C 54.21 0.3 1 168 41 41 ALA CB C 18.81 0.3 1 169 42 42 LEU H H 9.145 0.05 1 170 42 42 LEU C C 179.81 0.3 1 171 42 42 LEU CA C 57.81 0.3 1 172 42 42 LEU CB C 39.14 0.3 1 173 42 42 LEU N N 119.081 0.3 1 174 43 43 GLU H H 8.455 0.05 1 175 43 43 GLU C C 175.11 0.3 1 176 43 43 GLU CA C 57.22 0.3 1 177 43 43 GLU CB C 29.69 0.3 1 178 43 43 GLU N N 118.648 0.3 1 179 44 44 SER H H 7.082 0.05 1 180 44 44 SER C C 173.3 0.3 1 181 44 44 SER CA C 57.42 0.3 1 182 44 44 SER CB C 63.44 0.3 1 183 44 44 SER N N 115.838 0.3 1 184 50 50 PRO C C 179.25 0.3 1 185 50 50 PRO CA C 64.89 0.3 1 186 51 51 HIS H H 7.312 0.05 1 187 51 51 HIS C C 177.41 0.3 1 188 51 51 HIS CA C 59.5 0.3 1 189 51 51 HIS CB C 28.76 0.3 1 190 51 51 HIS N N 112.910 0.3 1 191 52 52 HIS H H 7.919 0.05 1 192 52 52 HIS C C 177.88 0.3 1 193 52 52 HIS CA C 61.91 0.3 1 194 52 52 HIS CB C 29.27 0.3 1 195 52 52 HIS N N 119.591 0.3 1 196 53 53 THR H H 8.238 0.05 1 197 53 53 THR CA C 66.69 0.3 1 198 53 53 THR CB C 68.3 0.3 1 199 53 53 THR N N 117.424 0.3 1 200 54 54 ALA H H 8.187 0.05 1 201 54 54 ALA C C 179.07 0.3 1 202 54 54 ALA CA C 55.86 0.3 1 203 54 54 ALA CB C 17.23 0.3 1 204 54 54 ALA N N 122.235 0.3 1 205 55 55 LEU H H 8.203 0.05 1 206 55 55 LEU C C 178.44 0.3 1 207 55 55 LEU CA C 57.56 0.3 1 208 55 55 LEU CB C 41.43 0.3 1 209 55 55 LEU N N 119.627 0.3 1 210 56 56 ARG H H 8.558 0.05 1 211 56 56 ARG C C 177.54 0.3 1 212 56 56 ARG CA C 60.32 0.3 1 213 56 56 ARG CB C 30.32 0.3 1 214 56 56 ARG N N 117.051 0.3 1 215 57 57 GLN H H 7.196 0.05 1 216 57 57 GLN C C 179.28 0.3 1 217 57 57 GLN CA C 56.79 0.3 1 218 58 58 ALA H H 8.449 0.05 1 219 58 58 ALA C C 179.51 0.3 1 220 58 58 ALA CA C 55.15 0.3 1 221 58 58 ALA CB C 17.46 0.3 1 222 58 58 ALA N N 123.232 0.3 1 223 59 59 ILE H H 8.523 0.05 1 224 59 59 ILE C C 179.37 0.3 1 225 59 59 ILE CA C 65.91 0.3 1 226 59 59 ILE CB C 37.78 0.3 1 227 59 59 ILE N N 118.539 0.3 1 228 60 60 LEU H H 7.688 0.05 1 229 60 60 LEU CA C 57.37 0.3 1 230 60 60 LEU CB C 40.39 0.3 1 231 60 60 LEU N N 121.030 0.3 1 232 61 61 CYS H H 8.755 0.05 1 233 61 61 CYS C C 176.58 0.3 1 234 61 61 CYS CA C 59.8 0.3 1 235 61 61 CYS CB C 42.18 0.3 1 236 61 61 CYS N N 121.982 0.3 1 237 62 62 TRP H H 8.415 0.05 1 238 62 62 TRP C C 177.72 0.3 1 239 62 62 TRP CA C 59.59 0.3 1 240 62 62 TRP CB C 28.04 0.3 1 241 62 62 TRP N N 119.193 0.3 1 242 63 63 GLY H H 8.051 0.05 1 243 63 63 GLY C C 177.06 0.3 1 244 63 63 GLY CA C 47.05 0.3 1 245 63 63 GLY N N 104.569 0.3 1 246 64 64 ASP H H 8.171 0.05 1 247 64 64 ASP C C 179.83 0.3 1 248 64 64 ASP CA C 58.02 0.3 1 249 64 64 ASP CB C 40.13 0.3 1 250 64 64 ASP N N 125.074 0.3 1 251 65 65 LEU H H 8.136 0.05 1 252 65 65 LEU C C 178.52 0.3 1 253 65 65 LEU CA C 57.89 0.3 1 254 65 65 LEU CB C 39.97 0.3 1 255 65 65 LEU N N 124.609 0.3 1 256 66 66 MET H H 8.457 0.05 1 257 66 66 MET C C 180.29 0.3 1 258 66 66 MET CA C 56.32 0.3 1 259 66 66 MET N N 118.791 0.3 1 260 67 67 THR H H 8.680 0.05 1 261 67 67 THR CA C 66.73 0.3 1 262 67 67 THR CB C 67.85 0.3 1 263 67 67 THR N N 121.332 0.3 1 264 68 68 LEU H H 7.907 0.05 1 265 68 68 LEU C C 178.03 0.3 1 266 68 68 LEU CA C 58.66 0.3 1 267 68 68 LEU CB C 40.41 0.3 1 268 68 68 LEU N N 124.876 0.3 1 269 69 69 ALA H H 8.464 0.05 1 270 69 69 ALA C C 180.2 0.3 1 271 69 69 ALA CA C 55.31 0.3 1 272 69 69 ALA CB C 17.06 0.3 1 273 69 69 ALA N N 122.041 0.3 1 274 70 70 THR H H 8.497 0.05 1 275 70 70 THR C C 176.5 0.3 1 276 70 70 THR CA C 65.99 0.3 1 277 70 70 THR CB C 68.47 0.3 1 278 70 70 THR N N 116.854 0.3 1 279 71 71 TRP H H 8.748 0.05 1 280 71 71 TRP C C 180.27 0.3 1 281 71 71 TRP CA C 62.27 0.3 1 282 71 71 TRP CB C 28 0.3 1 283 71 71 TRP N N 126.853 0.3 1 284 72 72 VAL H H 8.956 0.05 1 285 72 72 VAL C C 177.42 0.3 1 286 72 72 VAL CA C 65.75 0.3 1 287 72 72 VAL CB C 30.76 0.3 1 288 72 72 VAL N N 119.100 0.3 1 289 73 73 GLY H H 7.707 0.05 1 290 73 73 GLY C C 174.81 0.3 1 291 73 73 GLY CA C 46.45 0.3 1 292 73 73 GLY N N 104.816 0.3 1 293 75 75 ASN H H 7.828 0.05 1 294 75 75 ASN C C 175.97 0.3 1 295 75 75 ASN CA C 58.94 0.3 1 296 75 75 ASN CB C 38.63 0.3 1 297 76 76 LEU H H 6.676 0.05 1 298 76 76 LEU C C 174.51 0.3 1 299 76 76 LEU CA C 55.91 0.3 1 300 76 76 LEU CB C 38.48 0.3 1 301 76 76 LEU N N 115.387 0.3 1 302 80 80 ALA C C 181.07 0.3 1 303 80 80 ALA CA C 54.61 0.3 1 304 80 80 ALA CB C 17.52 0.3 1 305 81 81 SER H H 7.758 0.05 1 306 81 81 SER C C 180 0.3 1 307 81 81 SER CA C 62.06 0.3 1 308 81 81 SER CB C 62.74 0.3 1 309 81 81 SER N N 115.109 0.3 1 310 83 83 ASP C C 179.38 0.3 1 311 83 83 ASP CA C 56.76 0.3 1 312 83 83 ASP CB C 39.7 0.3 1 313 84 84 LEU H H 8.021 0.05 1 314 84 84 LEU C C 179.85 0.3 1 315 84 84 LEU CA C 58.01 0.3 1 316 84 84 LEU CB C 42 0.3 1 317 84 84 LEU N N 121.615 0.3 1 318 85 85 VAL H H 7.879 0.05 1 319 85 85 VAL C C 177.35 0.3 1 320 85 85 VAL CA C 66.41 0.3 1 321 85 85 VAL CB C 30.99 0.3 1 322 85 85 VAL N N 118.404 0.3 1 323 86 86 VAL H H 8.176 0.05 1 324 86 86 VAL C C 178.61 0.3 1 325 86 86 VAL CA C 67.27 0.3 1 326 86 86 VAL N N 119.846 0.3 1 327 87 87 SER H H 8.320 0.05 1 328 87 87 SER CA C 61.37 0.3 1 329 87 87 SER CB C 62.38 0.3 1 330 87 87 SER N N 114.606 0.3 1 331 88 88 TYR H H 7.972 0.05 1 332 88 88 TYR C C 178.39 0.3 1 333 88 88 TYR CA C 61.32 0.3 1 334 88 88 TYR CB C 37.17 0.3 1 335 88 88 TYR N N 124.866 0.3 1 336 89 89 VAL H H 8.141 0.05 1 337 89 89 VAL C C 177.29 0.3 1 338 89 89 VAL CA C 66.38 0.3 1 339 89 89 VAL CB C 30.92 0.3 1 340 89 89 VAL N N 119.224 0.3 1 341 93 93 VAL H H 7.579 0.05 1 342 93 93 VAL C C 175.77 0.3 1 343 93 93 VAL CA C 64.32 0.3 1 344 93 93 VAL CB C 30.65 0.3 1 345 93 93 VAL N N 119.019 0.3 1 346 94 94 GLY H H 7.976 0.05 1 347 94 94 GLY C C 175.59 0.3 1 348 94 94 GLY CA C 47.76 0.3 1 349 94 94 GLY N N 106.594 0.3 1 350 95 95 LEU C C 177.97 0.3 1 351 95 95 LEU CA C 58.24 0.3 1 352 95 95 LEU CB C 39.8 0.3 1 353 96 96 LYS H H 7.299 0.05 1 354 96 96 LYS C C 179.86 0.3 1 355 96 96 LYS CA C 58.7 0.3 1 356 96 96 LYS CB C 30.21 0.3 1 357 96 96 LYS N N 117.492 0.3 1 358 97 97 PHE H H 7.668 0.05 1 359 97 97 PHE C C 177.39 0.3 1 360 97 97 PHE CA C 62.57 0.3 1 361 97 97 PHE CB C 38.93 0.3 1 362 97 97 PHE N N 117.825 0.3 1 363 98 98 ARG C C 177.66 0.3 1 364 98 98 ARG CA C 59.43 0.3 1 365 98 98 ARG CB C 29.59 0.3 1 366 99 99 GLN H H 7.358 0.05 1 367 99 99 GLN C C 177.08 0.3 1 368 99 99 GLN CA C 58.47 0.3 1 369 99 99 GLN CB C 27.62 0.3 1 370 100 100 LEU H H 7.326 0.05 1 371 100 100 LEU C C 179.61 0.3 1 372 100 100 LEU CA C 58.22 0.3 1 373 100 100 LEU CB C 43.52 0.3 1 374 100 100 LEU N N 119.998 0.3 1 375 101 101 LEU H H 8.838 0.05 1 376 101 101 LEU C C 178.88 0.3 1 377 101 101 LEU CA C 58.06 0.3 1 378 101 101 LEU CB C 41.62 0.3 1 379 101 101 LEU N N 117.329 0.3 1 380 102 102 TRP H H 8.402 0.05 1 381 102 102 TRP C C 179.08 0.3 1 382 102 102 TRP CA C 62.84 0.3 1 383 102 102 TRP CB C 28.71 0.3 1 384 102 102 TRP N N 118.549 0.3 1 385 103 103 PHE H H 9.196 0.05 1 386 103 103 PHE C C 177.18 0.3 1 387 103 103 PHE CA C 62.16 0.3 1 388 103 103 PHE CB C 39.15 0.3 1 389 103 103 PHE N N 122.655 0.3 1 390 104 104 HIS H H 8.064 0.05 1 391 104 104 HIS C C 178 0.3 1 392 104 104 HIS CA C 61.1 0.3 1 393 104 104 HIS CB C 31.83 0.3 1 394 104 104 HIS N N 118.280 0.3 1 395 105 105 ILE H H 8.596 0.05 1 396 105 105 ILE C C 178.87 0.3 1 397 105 105 ILE CA C 65.47 0.3 1 398 105 105 ILE CB C 37.15 0.3 1 399 105 105 ILE N N 118.720 0.3 1 400 106 106 SER H H 8.290 0.05 1 401 106 106 SER CA C 61.81 0.3 1 402 106 106 SER CB C 61.14 0.3 1 403 106 106 SER N N 117.520 0.3 1 404 107 107 CYS H H 7.915 0.05 1 405 107 107 CYS C C 177.83 0.3 1 406 107 107 CYS CA C 63.98 0.3 1 407 107 107 CYS CB C 25.44 0.3 1 408 107 107 CYS N N 121.918 0.3 1 409 108 108 LEU H H 7.378 0.05 1 410 108 108 LEU C C 178.23 0.3 1 411 108 108 LEU CA C 57.18 0.3 1 412 108 108 LEU CB C 41 0.3 1 413 108 108 LEU N N 119.581 0.3 1 414 109 109 THR H H 7.627 0.05 1 415 109 109 THR C C 175.22 0.3 1 416 109 109 THR CA C 64.99 0.3 1 417 109 109 THR CB C 69.22 0.3 1 418 109 109 THR N N 115.552 0.3 1 419 110 110 PHE H H 8.469 0.05 1 420 110 110 PHE C C 176.31 0.3 1 421 110 110 PHE CA C 58.26 0.3 1 422 110 110 PHE CB C 40.06 0.3 1 423 110 110 PHE N N 116.690 0.3 1 424 111 111 GLY H H 7.201 0.05 1 425 111 111 GLY C C 174.28 0.3 1 426 111 111 GLY CA C 44.04 0.3 1 427 111 111 GLY N N 110.391 0.3 1 428 114 114 THR C C 177.07 0.3 1 429 114 114 THR CA C 65.57 0.3 1 430 114 114 THR CB C 68.15 0.3 1 431 115 115 VAL H H 7.574 0.05 1 432 115 115 VAL C C 177.78 0.3 1 433 115 115 VAL CA C 66.65 0.3 1 434 115 115 VAL CB C 30.57 0.3 1 435 115 115 VAL N N 123.776 0.3 1 436 116 116 LEU H H 8.786 0.05 1 437 116 116 LEU C C 179.14 0.3 1 438 116 116 LEU CA C 57.72 0.3 1 439 116 116 LEU CB C 40.22 0.3 1 440 116 116 LEU N N 119.832 0.3 1 441 117 117 GLU H H 8.137 0.05 1 442 117 117 GLU C C 179.5 0.3 1 443 117 117 GLU CA C 59.09 0.3 1 444 117 117 GLU CB C 28.72 0.3 1 445 117 117 GLU N N 118.256 0.3 1 446 118 118 TYR H H 7.873 0.05 1 447 118 118 TYR C C 176.68 0.3 1 448 118 118 TYR CA C 60.61 0.3 1 449 118 118 TYR CB C 37.82 0.3 1 450 118 118 TYR N N 121.829 0.3 1 451 119 119 LEU H H 8.801 0.05 1 452 119 119 LEU C C 180.59 0.3 1 453 119 119 LEU CA C 58.27 0.3 1 454 119 119 LEU CB C 40.82 0.3 1 455 119 119 LEU N N 119.859 0.3 1 456 120 120 VAL H H 8.417 0.05 1 457 120 120 VAL C C 179.56 0.3 1 458 120 120 VAL CA C 66.08 0.3 1 459 120 120 VAL CB C 31.2 0.3 1 460 120 120 VAL N N 120.120 0.3 1 461 121 121 SER H H 8.453 0.05 1 462 121 121 SER C C 181.62 0.3 1 463 121 121 SER CA C 61.47 0.3 1 464 121 121 SER CB C 62.12 0.3 1 465 121 121 SER N N 117.387 0.3 1 466 122 122 PHE H H 9.478 0.05 1 467 122 122 PHE C C 177.17 0.3 1 468 122 122 PHE CA C 61.87 0.3 1 469 122 122 PHE CB C 37.94 0.3 1 470 122 122 PHE N N 127.077 0.3 1 471 123 123 GLY H H 7.915 0.05 1 472 123 123 GLY C C 175.16 0.3 1 473 123 123 GLY CA C 46.8 0.3 1 474 123 123 GLY N N 106.058 0.3 1 475 124 124 VAL H H 7.602 0.05 1 476 124 124 VAL C C 178.88 0.3 1 477 124 124 VAL CA C 65.77 0.3 1 478 124 124 VAL CB C 31.09 0.3 1 479 124 124 VAL N N 120.580 0.3 1 480 125 125 TRP H H 7.894 0.05 1 481 125 125 TRP C C 178.28 0.3 1 482 125 125 TRP CA C 62.86 0.3 1 483 125 125 TRP CB C 28.18 0.3 1 484 125 125 TRP N N 123.340 0.3 1 485 126 126 ILE H H 8.638 0.05 1 486 126 126 ILE C C 177.15 0.3 1 487 126 126 ILE CA C 61.49 0.3 1 488 126 126 ILE CB C 37.1 0.3 1 489 126 126 ILE N N 117.741 0.3 1 490 127 127 ARG H H 7.205 0.05 1 491 127 127 ARG C C 177.01 0.3 1 492 127 127 ARG CA C 56.48 0.3 1 493 127 127 ARG CB C 30.18 0.3 1 494 127 127 ARG N N 118.334 0.3 1 495 128 128 THR H H 7.476 0.05 1 496 128 128 THR C C 181.53 0.3 1 497 128 128 THR CA C 61.34 0.3 1 498 128 128 THR CB C 69.34 0.3 1 499 128 128 THR N N 121.718 0.3 1 500 131 131 ALA C C 178.17 0.3 1 501 131 131 ALA CA C 53.65 0.3 1 502 131 131 ALA CB C 17.42 0.3 1 503 132 132 TYR H H 7.654 0.05 1 504 132 132 TYR C C 174.76 0.3 1 505 132 132 TYR CA C 55.45 0.3 1 506 132 132 TYR CB C 38.58 0.3 1 507 132 132 TYR N N 113.663 0.3 1 508 133 133 ARG H H 7.141 0.05 1 509 133 133 ARG C C 173.63 0.3 1 510 133 133 ARG CA C 53.75 0.3 1 511 133 133 ARG CB C 30.37 0.3 1 512 133 133 ARG N N 122.695 0.3 1 513 138 138 PRO C C 174.89 0.3 1 514 138 138 PRO CA C 62.47 0.3 1 515 138 138 PRO CB C 31.44 0.3 1 516 139 139 ILE H H 8.242 0.05 1 517 139 139 ILE C C 175.08 0.3 1 518 139 139 ILE CA C 59.35 0.3 1 519 139 139 ILE CB C 41.04 0.3 1 520 139 139 ILE N N 118.923 0.3 1 521 140 140 LEU H H 7.986 0.05 1 522 140 140 LEU CA C 54.08 0.3 1 523 140 140 LEU CB C 39.75 0.3 1 524 140 140 LEU N N 128.177 0.3 1 stop_ save_