data_4619 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; N-terminal zinc-binding HHCC domain of HIV-2 integrase ; _BMRB_accession_number 4619 _BMRB_flat_file_name bmr4619.str _Entry_type original _Submission_date 2000-03-26 _Accession_date 2000-09-07 _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 Eijkelenboom A. P.A.M. . 2 'van den Ent' F. M.I. . 3 Plasterk R. H.A. . 4 Kaptein R. . . 5 Boelens R. . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 346 "13C chemical shifts" 184 "15N chemical shifts" 62 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2000-12-05 original author . stop_ _Original_release_date 2000-12-05 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; Solution structure of the N-terminal HHCC domain of HIV-2 integrase: a three-helix bundle stabilized by zinc ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code 98035191 _PubMed_ID ? loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Eijkelenboom A. P.A.M. . 2 'van den Ent' F. M.I. . 3 Vos A. . . 4 Doreleijers J. F. . 5 Hard K. . . 6 Tullius T. D. . 7 Plasterk R. H.A. . 8 Kaptein R. . . 9 Boelens R. . . stop_ _Journal_abbreviation 'Curr. Biol.' _Journal_volume 7 _Journal_issue . _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 739 _Page_last 746 _Year 1997 _Details . loop_ _Keyword integrase AIDS polyprotein dimer 'zinc-binding protein' helix-turn-helix stop_ save_ ################################## # Molecular system description # ################################## save_HHCC_domain_HIV-2 _Saveframe_category molecular_system _Mol_system_name 'Human immunodeficiency virus type 2 integrase' _Abbreviation_common 'HHCC domain HIV-2' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'HHCC domain of HIV-2 monomer 1' $HHCC_domain 'HHCC domain of HIV-2 monomer 2' $HHCC_domain Zn-1 $ZN Zn-2 $ZN stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state dimer _System_paramagnetic no _System_thiol_state 'all other bound' loop_ _Magnetic_equivalence_ID _Magnetically_equivalent_system_component 1 'HHCC domain of HIV-2 monomer 1' 1 'HHCC domain of HIV-2 monomer 2' 2 Zn-1 2 Zn-2 stop_ _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_HHCC_domain _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'Human immunodeficiency virus type 2 integrase' _Name_variant none _Molecular_mass . _Mol_thiol_state 'all other bound' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 55 _Mol_residue_sequence ; FLEKIEPAQEEHEKYHSNVK ELSHKFGIPNLVARQIVNSC AQCQQKGEAIHGQVN ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 1 PHE 2 2 LEU 3 3 GLU 4 4 LYS 5 5 ILE 6 6 GLU 7 7 PRO 8 8 ALA 9 9 GLN 10 10 GLU 11 11 GLU 12 12 HIS 13 13 GLU 14 14 LYS 15 15 TYR 16 16 HIS 17 17 SER 18 18 ASN 19 19 VAL 20 20 LYS 21 21 GLU 22 22 LEU 23 23 SER 24 24 HIS 25 25 LYS 26 26 PHE 27 27 GLY 28 28 ILE 29 29 PRO 30 30 ASN 31 31 LEU 32 32 VAL 33 33 ALA 34 34 ARG 35 35 GLN 36 36 ILE 37 37 VAL 38 38 ASN 39 39 SER 40 40 CYS 41 41 ALA 42 42 GLN 43 43 CYS 44 44 GLN 45 45 GLN 46 46 LYS 47 47 GLY 48 48 GLU 49 49 ALA 50 50 ILE 51 51 HIS 52 52 GLY 53 53 GLN 54 54 VAL 55 55 ASN stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-02-11 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 1E0E "N-Terminal Zinc-Binding Hhcc Domain Of Hiv-2 Integrase" 100.00 55 100.00 100.00 1.19e-30 PDB 3F9K "Two Domain Fragment Of Hiv-2 Integrase In Complex With Ledgf Ibd" 98.18 210 100.00 100.00 5.17e-29 EMBL CAA08005 "DNA polymerase [Human immunodeficiency virus 2]" 100.00 131 98.18 100.00 2.85e-30 EMBL CAA08033 "DNA polymerase [Human immunodeficiency virus 2]" 98.18 129 100.00 100.00 7.06e-30 EMBL CAA08041 "DNA polymerase [Human immunodeficiency virus 2]" 100.00 131 98.18 100.00 3.24e-30 GB AAB00764 "pol polyprotein [Human immunodeficiency virus 2]" 100.00 876 100.00 100.00 2.01e-28 GB ABU88863 "integrase [Human immunodeficiency virus 2]" 100.00 293 98.18 100.00 2.71e-29 GB ADQ26695 "integrase [Human immunodeficiency virus 2]" 100.00 293 100.00 100.00 1.27e-29 GB AEI83209 "integrase [Human immunodeficiency virus 2]" 100.00 293 98.18 100.00 3.01e-29 GB AHI42063 "integrase, partial [Human immunodeficiency virus 2]" 100.00 293 98.18 98.18 8.68e-29 PRF 1306388B "gene pol" 100.00 1036 100.00 100.00 7.32e-28 SP P04584 "RecName: Full=Gag-Pol polyprotein; AltName: Full=Pr160Gag-Pol; Contains: RecName: Full=Matrix protein p17; Short=MA; Contains: " 100.00 1464 100.00 100.00 4.10e-28 stop_ save_ ############# # Ligands # ############# save_ZN _Saveframe_category ligand _Mol_type non-polymer _Name_common "ZN (ZINC ION)" _BMRB_code . _PDB_code ZN _Molecular_mass 65.409 _Mol_charge 2 _Mol_paramagnetic . _Mol_aromatic no _Details ; Information obtained from PDB's Chemical Component Dictionary at http://wwpdb-remediation.rutgers.edu/downloads.html Downloaded on Thu Jun 2 09:48:05 2011 ; loop_ _Atom_name _PDB_atom_name _Atom_type _Atom_chirality _Atom_charge _Atom_oxidation_number _Atom_unpaired_electrons ZN ZN ZN . 2 . ? stop_ _Mol_thiol_state . _Sequence_homology_query_date . save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species _Details $HHCC_domain HIV-2 11720 . . . . 'isolate ROD' 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 $HHCC_domain 'recombinant technology' 'Escherichia coli' Escherichia coli . BL21(DE3) 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 $HHCC_domain 3.5 mM [U-15N] $ZN 1.1 eq . Tris 50 mM [U-2H] NaCl 150 mM . 2-mercaptoethanol 2 mM . D2O 99.99 % . stop_ save_ save_sample_2 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $HHCC_domain 3.5 mM [U-15N] $ZN 1.1 eq . Tris 50 mM [U-2H] NaCl 150 mM . 2-mercaptoethanol 2 mM . H2O 95 % . D2O 5 % . stop_ save_ save_sample_3 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $HHCC_domain 3.5 mM '[U-15N; U-13C]' $ZN 1.1 eq . Tris 50 mM [U-2H] NaCl 150 mM . 2-mercaptoethanol 2 mM . D2O 5 % . stop_ save_ save_sample_4 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $HHCC_domain 3.5 mM '[U-15N; U-13C]' $ZN 1.1 eq . Tris 50 mM [U-2H] NaCl 150 mM . 2-mercaptoethanol 2 mM . H2O 95 % . D2O 5 % . stop_ save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model 'Unity Plus' _Field_strength 500 _Details . save_ save_spectrometer_2 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model AMX _Field_strength 600 _Details . save_ save_spectrometer_3 _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model 'Unity Plus' _Field_strength 750 _Details . save_ ############################# # NMR applied experiments # ############################# save_2D_(1H,15N)-HSQC_1 _Saveframe_category NMR_applied_experiment _Experiment_name '2D (1H,15N)-HSQC' _Sample_label . save_ save_2D_(1H,15N)-HSMQC_2 _Saveframe_category NMR_applied_experiment _Experiment_name '2D (1H,15N)-HSMQC' _Sample_label . save_ save_2D_(1H,1H)_NOESY_3 _Saveframe_category NMR_applied_experiment _Experiment_name '2D (1H,1H) NOESY' _Sample_label . save_ save_2D_(1H,1H)_TOCSY_4 _Saveframe_category NMR_applied_experiment _Experiment_name '2D (1H,1H) TOCSY' _Sample_label . save_ save_3D_TOCSY_(15N,1H)_HSQC_5 _Saveframe_category NMR_applied_experiment _Experiment_name '3D TOCSY (15N,1H) HSQC' _Sample_label . save_ save_3D_TOCSY_(13C,1H)_HSQC_6 _Saveframe_category NMR_applied_experiment _Experiment_name '3D TOCSY (13C,1H) HSQC' _Sample_label . save_ save_3D_NOESY_(15N,1H)_HSQC_7 _Saveframe_category NMR_applied_experiment _Experiment_name '3D NOESY (15N,1H) HSQC' _Sample_label . save_ save_3D_NOESY_(13C,1H)_HSQC_8 _Saveframe_category NMR_applied_experiment _Experiment_name '3D NOESY (13C,1H) HSQC' _Sample_label . save_ save_3D_(13C)_HMQC_NOESY_(13C,1H)_HSQC_9 _Saveframe_category NMR_applied_experiment _Experiment_name '3D (13C) HMQC NOESY (13C,1H) HSQC' _Sample_label . save_ save_2D_13C-filtered_NOESY_10 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 13C-filtered NOESY' _Sample_label . save_ save_3D_13C-filtered_NOESY_(13C,1H)_HSQC_11 _Saveframe_category NMR_applied_experiment _Experiment_name '3D 13C-filtered NOESY (13C,1H) HSQC' _Sample_label . save_ save_3D_HNCO_12 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCO' _Sample_label . save_ save_3D_HNCA_13 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCA' _Sample_label . save_ save_3D_HN(CO)CA_14 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HN(CO)CA' _Sample_label . save_ save_3D_HNHA_15 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNHA' _Sample_label . save_ save_3D_HNHB_16 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNHB' _Sample_label . save_ save_3D_H(C)CH_DIPSI_17 _Saveframe_category NMR_applied_experiment _Experiment_name '3D H(C)CH DIPSI' _Sample_label . save_ save_3D_HCC(H)_DIPSI_18 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HCC(H) DIPSI' _Sample_label . save_ ####################### # Sample conditions # ####################### save_sample_cond_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 6.5 . pH temperature 300 . K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference _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 _Indirect_shift_ratio_citation_label _Correction_value_citation_label H2O H 1 protons ppm 4.75 internal direct internal . . . $entry_citation $entry_citation DDS C 13 'methyl protons' ppm 0.00 . indirect . . . 0.101329118 $entry_citation $entry_citation DDS N 15 'methyl protons' ppm 0.00 . indirect . . . 0.251449530 $entry_citation $entry_citation 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_chem_shift_set_1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $sample_cond_1 _Chem_shift_reference_set_label $chemical_shift_reference _Mol_system_component_name 'HHCC domain of HIV-2 monomer 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 PHE H H 8.300 . . 2 . 1 PHE HA H 4.577 . . 3 . 1 PHE HB3 H 3.154 . . 4 . 1 PHE HB2 H 3.154 . . 5 . 1 PHE HD1 H 7.235 . . 6 . 1 PHE HD2 H 7.235 . . 7 . 1 PHE HE1 H 7.363 . . 8 . 1 PHE HE2 H 7.363 . . 9 . 1 PHE N N 120.175 . . 10 . 1 PHE HZ H 7.319 . . 11 . 1 PHE CA C 56.716 . . 12 . 1 PHE CB C 37.027 . . 13 . 1 PHE CD1 C 129.310 . . 14 . 1 PHE CD2 C 129.310 . . 15 . 1 PHE CE1 C 129.397 . . 16 . 1 PHE CE2 C 129.397 . . 17 . 2 LEU H H 7.908 . . 18 . 2 LEU HA H 4.105 . . 19 . 2 LEU HB3 H 1.699 . . 20 . 2 LEU HB2 H 1.579 . . 21 . 2 LEU HG H 1.579 . . 22 . 2 LEU HD1 H 0.925 . . 23 . 2 LEU HD2 H 0.866 . . 24 . 2 LEU N N 122.850 . . 25 . 2 LEU CA C 54.714 . . 26 . 2 LEU CB C 39.955 . . 27 . 2 LEU CD1 C 23.160 . . 28 . 2 LEU CD2 C 21.713 . . 29 . 2 LEU CG C 25.001 . . 30 . 3 GLU H H 8.485 . . 31 . 3 GLU HA H 4.207 . . 32 . 3 GLU HB3 H 2.048 . . 33 . 3 GLU HB2 H 2.048 . . 34 . 3 GLU HG3 H 2.347 . . 35 . 3 GLU HG2 H 2.294 . . 36 . 3 GLU N N 119.00 . . 37 . 3 GLU CA C 55.682 . . 38 . 3 GLU CB C 27.760 . . 39 . 3 GLU CG C 34.446 . . 40 . 4 LYS N N 118.892 . . 41 . 4 LYS H H 8.061 . . 42 . 4 LYS HA H 4.429 . . 43 . 4 LYS HE3 H 3.088 . . 44 . 4 LYS HE2 H 3.088 . . 45 . 4 LYS HB3 H 2.025 . . 46 . 4 LYS HB2 H 1.932 . . 47 . 4 LYS HD3 H 1.840 . . 48 . 4 LYS HD2 H 1.800 . . 49 . 4 LYS HG3 H 1.630 . . 50 . 4 LYS HG2 H 1.504 . . 51 . 4 LYS CA C 54.307 . . 52 . 4 LYS CG C 23.223 . . 53 . 4 LYS CE C 40.380 . . 54 . 4 LYS CD C 26.966 . . 55 . 4 LYS CB C 31.352 . . 56 . 5 ILE H H 7.649 . . 57 . 5 ILE HA H 3.688 . . 58 . 5 ILE HB H 1.835 . . 59 . 5 ILE HG13 H 1.643 . . 60 . 5 ILE HG12 H 1.043 . . 61 . 5 ILE HG2 H 0.809 . . 62 . 5 ILE HD1 H 0.872 . . 63 . 5 ILE N N 120.007 . . 64 . 5 ILE CA C 62.204 . . 65 . 5 ILE CB C 35.970 . . 66 . 5 ILE CG1 C 26.716 . . 67 . 5 ILE CG2 C 15.560 . . 68 . 5 ILE CD1 C 11.580 . . 69 . 6 GLU H H 8.614 . . 70 . 6 GLU HA H 4.240 . . 71 . 6 GLU HB3 H 2.034 . . 72 . 6 GLU HB2 H 1.944 . . 73 . 6 GLU HG3 H 2.288 . . 74 . 6 GLU HG2 H 2.223 . . 75 . 6 GLU N N 122.120 . . 76 . 6 GLU CA C 58.448 . . 77 . 6 GLU CB C 24.840 . . 78 . 6 GLU CG C 34.300 . . 79 . 7 PRO HA H 4.238 . . 80 . 7 PRO HB3 H 2.322 . . 81 . 7 PRO HB2 H 1.698 . . 82 . 7 PRO HG3 H 2.078 . . 83 . 7 PRO HG2 H 2.024 . . 84 . 7 PRO HD3 H 3.612 . . 85 . 7 PRO HD2 H 3.494 . . 86 . 7 PRO CD C 47.860 . . 87 . 7 PRO CA C 63.604 . . 88 . 7 PRO CB C 28.826 . . 89 . 7 PRO CG C 25.900 . . 90 . 8 ALA H H 7.211 . . 91 . 8 ALA HA H 3.119 . . 92 . 8 ALA HB H 1.021 . . 93 . 8 ALA N N 122.501 . . 94 . 8 ALA CB C 16.842 . . 95 . 8 ALA CA C 52.213 . . 96 . 9 GLN H H 8.280 . . 97 . 9 GLN HA H 3.812 . . 98 . 9 GLN HB3 H 2.241 . . 99 . 9 GLN HB2 H 2.144 . . 100 . 9 GLN HG3 H 2.352 . . 101 . 9 GLN HG2 H 2.292 . . 102 . 9 GLN HE21 H 7.525 . . 103 . 9 GLN HE22 H 6.797 . . 104 . 9 GLN N N 120.362 . . 105 . 9 GLN CA C 57.260 . . 106 . 9 GLN CB C 26.216 . . 107 . 9 GLN CG C 32.020 . . 108 . 9 GLN NE2 N 112.222 . . 109 . 10 GLU H H 8.123 . . 110 . 10 GLU HA H 3.944 . . 111 . 10 GLU HB3 H 2.020 . . 112 . 10 GLU HB2 H 2.020 . . 113 . 10 GLU HG3 H 2.364 . . 114 . 10 GLU HG2 H 2.181 . . 115 . 10 GLU N N 120.966 . . 116 . 10 GLU CA C 57.120 . . 117 . 10 GLU CB C 27.239 . . 118 . 10 GLU CG C 34.226 . . 119 . 11 GLU H H 8.002 . . 120 . 11 GLU HA H 4.165 . . 121 . 11 GLU HB3 H 2.135 . . 122 . 11 GLU HB2 H 2.451 . . 123 . 11 GLU HG3 H 2.552 . . 124 . 11 GLU HG2 H 2.552 . . 125 . 11 GLU N N 121.066 . . 126 . 11 GLU CA C 57.253 . . 127 . 11 GLU CB C 26.875 . . 128 . 11 GLU CG C 32.618 . . 129 . 12 HIS H H 8.429 . . 130 . 12 HIS HA H 3.593 . . 131 . 12 HIS HB3 H 3.263 . . 132 . 12 HIS HB2 H 2.973 . . 133 . 12 HIS HD1 H 12.635 . . 134 . 12 HIS HE1 H 8.119 . . 135 . 12 HIS HD2 H 6.914 . . 136 . 12 HIS N N 118.812 . . 137 . 12 HIS CA C 58.958 . . 138 . 12 HIS CB C 26.513 . . 139 . 12 HIS CD2 C 138.851 . . 140 . 13 GLU H H 8.303 . . 141 . 13 GLU HA H 3.675 . . 142 . 13 GLU HB3 H 2.087 . . 143 . 13 GLU HB2 H 2.002 . . 144 . 13 GLU HG3 H 2.420 . . 145 . 13 GLU HG2 H 2.297 . . 146 . 13 GLU N N 119.305 . . 147 . 13 GLU CA C 56.963 . . 148 . 13 GLU CB C 27.099 . . 149 . 13 GLU CG C 34.285 . . 150 . 14 LYS H H 7.149 . . 151 . 14 LYS HA H 3.896 . . 152 . 14 LYS HB3 H 1.195 . . 153 . 14 LYS HG3 H 1.195 . . 154 . 14 LYS HB2 H 0.792 . . 155 . 14 LYS HG2 H 0.792 . . 156 . 14 LYS HD3 H 1.434 . . 157 . 14 LYS HD2 H 1.434 . . 158 . 14 LYS HE3 H 2.810 . . 159 . 14 LYS HE2 H 2.810 . . 160 . 14 LYS N N 115.008 . . 161 . 14 LYS CA C 56.390 . . 162 . 14 LYS CB C 31.360 . . 163 . 14 LYS CG C 23.257 . . 164 . 14 LYS CD C 27.172 . . 165 . 14 LYS CE C 39.771 . . 166 . 15 TYR H H 7.915 . . 167 . 15 TYR HA H 4.829 . . 168 . 15 TYR HB3 H 3.325 . . 169 . 15 TYR HB2 H 2.637 . . 170 . 15 TYR HD1 H 7.148 . . 171 . 15 TYR HD2 H 7.148 . . 172 . 15 TYR HE1 H 6.815 . . 173 . 15 TYR HE2 H 6.815 . . 174 . 15 TYR N N 115.369 . . 175 . 15 TYR CA C 55.160 . . 176 . 15 TYR CB C 38.303 . . 177 . 15 TYR CD1 C 131.029 . . 178 . 15 TYR CD2 C 131.029 . . 179 . 15 TYR CE1 C 115.494 . . 180 . 15 TYR CE2 C 115.494 . . 181 . 16 HIS H H 8.617 . . 182 . 16 HIS HB2 H 2.956 . . 183 . 16 HIS HB3 H 2.820 . . 184 . 16 HIS HA H 1.954 . . 185 . 16 HIS HD2 H 6.747 . . 186 . 16 HIS HE1 H 7.858 . . 187 . 16 HIS N N 117.959 . . 188 . 16 HIS CA C 54.592 . . 189 . 16 HIS CB C 24.964 . . 190 . 16 HIS CD2 C 136.861 . . 191 . 17 SER H H 6.661 . . 192 . 17 SER HA H 4.394 . . 193 . 17 SER HB3 H 4.058 . . 194 . 17 SER HB2 H 3.460 . . 195 . 17 SER N N 111.196 . . 196 . 17 SER CA C 56.586 . . 197 . 17 SER CB C 61.215 . . 198 . 18 ASN H H 8.918 . . 199 . 18 ASN HA H 4.668 . . 200 . 18 ASN HB3 H 3.607 . . 201 . 18 ASN HB2 H 3.125 . . 202 . 18 ASN HD21 H 7.595 . . 203 . 18 ASN HD22 H 6.860 . . 204 . 18 ASN N N 123.764 . . 205 . 18 ASN CA C 50.223 . . 206 . 18 ASN CB C 36.617 . . 207 . 18 ASN ND2 N 112.110 . . 208 . 19 VAL H H 8.237 . . 209 . 19 VAL HA H 3.372 . . 210 . 19 VAL HB H 2.068 . . 211 . 19 VAL HG1 H 0.935 . . 212 . 19 VAL HG2 H 1.025 . . 213 . 19 VAL N N 116.465 . . 214 . 19 VAL CB C 30.048 . . 215 . 19 VAL CG1 C 19.402 . . 216 . 19 VAL CG2 C 21.652 . . 217 . 19 VAL CA C 65.275 . . 218 . 20 LYS H H 8.036 . . 219 . 20 LYS HA H 3.971 . . 220 . 20 LYS HB3 H 1.892 . . 221 . 20 LYS HB2 H 1.828 . . 222 . 20 LYS HG3 H 1.494 . . 223 . 20 LYS HG2 H 1.362 . . 224 . 20 LYS HD3 H 1.690 . . 225 . 20 LYS HD2 H 1.690 . . 226 . 20 LYS HE3 H 2.970 . . 227 . 20 LYS HE2 H 2.970 . . 228 . 20 LYS N N 121.024 . . 229 . 20 LYS CA C 57.550 . . 230 . 20 LYS CB C 30.060 . . 231 . 20 LYS CG C 23.253 . . 232 . 20 LYS CD C 27.041 . . 233 . 20 LYS CE C 39.790 . . 234 . 21 GLU H H 8.471 . . 235 . 21 GLU HA H 4.134 . . 236 . 21 GLU HB3 H 2.222 . . 237 . 21 GLU HB2 H 2.015 . . 238 . 21 GLU HG3 H 2.480 . . 239 . 21 GLU HG2 H 2.314 . . 240 . 21 GLU N N 120.855 . . 241 . 21 GLU CA C 57.214 . . 242 . 21 GLU CB C 27.800 . . 243 . 21 GLU CG C 34.689 . . 244 . 22 LEU H H 8.810 . . 245 . 22 LEU HA H 4.345 . . 246 . 22 LEU HB3 H 1.307 . . 247 . 22 LEU HB2 H 2.105 . . 248 . 22 LEU HG H 2.002 . . 249 . 22 LEU HD1 H 1.100 . . 250 . 22 LEU HD2 H 0.860 . . 251 . 22 LEU N N 119.620 . . 252 . 22 LEU CA C 55.945 . . 253 . 22 LEU CB C 41.731 . . 254 . 22 LEU CG C 24.200 . . 255 . 22 LEU CD1 C 22.469 . . 256 . 22 LEU CD2 C 25.140 . . 257 . 23 SER H H 8.481 . . 258 . 23 SER HA H 4.286 . . 259 . 23 SER HB3 H 3.937 . . 260 . 23 SER HB2 H 3.937 . . 261 . 23 SER N N 115.093 . . 262 . 23 SER CA C 60.405 . . 263 . 23 SER CB C 61.100 . . 264 . 24 HIS H H 8.219 . . 265 . 24 HIS HA H 4.378 . . 266 . 24 HIS HB3 H 3.287 . . 267 . 24 HIS HB2 H 3.187 . . 268 . 24 HIS HD2 H 7.094 . . 269 . 24 HIS HE1 H 8.068 . . 270 . 24 HIS N N 120.324 . . 271 . 24 HIS CA C 56.762 . . 272 . 24 HIS CB C 27.709 . . 273 . 24 HIS CD2 C 134.531 . . 274 . 25 LYS H H 8.386 . . 275 . 25 LYS HA H 3.725 . . 276 . 25 LYS HB3 H 1.691 . . 277 . 25 LYS HB2 H 1.322 . . 278 . 25 LYS HG3 H 0.985 . . 279 . 25 LYS HG2 H 0.084 . . 280 . 25 LYS HD3 H 1.397 . . 281 . 25 LYS HD2 H 1.397 . . 282 . 25 LYS HE3 H 2.705 . . 283 . 25 LYS HE2 H 2.705 . . 284 . 25 LYS N N 119.025 . . 285 . 25 LYS CA C 57.305 . . 286 . 25 LYS CB C 31.066 . . 287 . 25 LYS CG C 23.283 . . 288 . 25 LYS CD C 27.485 . . 289 . 25 LYS CE C 39.588 . . 290 . 26 PHE H H 7.810 . . 291 . 26 PHE HA H 4.625 . . 292 . 26 PHE HB3 H 3.488 . . 293 . 26 PHE HB2 H 2.823 . . 294 . 26 PHE HD1 H 7.552 . . 295 . 26 PHE HD2 H 7.552 . . 296 . 26 PHE HE1 H 7.290 . . 297 . 26 PHE HE2 H 7.290 . . 298 . 26 PHE HZ H 7.220 . . 299 . 26 PHE N N 112.122 . . 300 . 26 PHE CA C 56.490 . . 301 . 26 PHE CB C 38.145 . . 302 . 26 PHE CD1 C 129.294 . . 303 . 26 PHE CD2 C 129.294 . . 304 . 27 GLY H H 7.708 . . 305 . 27 GLY HA3 H 4.005 . . 306 . 27 GLY HA2 H 3.919 . . 307 . 27 GLY N N 110.411 . . 308 . 27 GLY CA C 45.033 . . 309 . 28 ILE H H 6.805 . . 310 . 28 ILE HA H 4.682 . . 311 . 28 ILE HB H 1.640 . . 312 . 28 ILE HG13 H 1.425 . . 313 . 28 ILE HG12 H 0.957 . . 314 . 28 ILE HG2 H 0.883 . . 315 . 28 ILE HD1 H 0.624 . . 316 . 28 ILE N N 110.200 . . 317 . 28 ILE CB C 36.014 . . 318 . 28 ILE CG1 C 23.173 . . 319 . 28 ILE CG2 C 16.625 . . 320 . 28 ILE CD1 C 12.161 . . 321 . 28 ILE CA C 55.467 . . 322 . 29 PRO HA H 4.482 . . 323 . 29 PRO HB3 H 2.571 . . 324 . 29 PRO HB2 H 1.757 . . 325 . 29 PRO HG3 H 2.018 . . 326 . 29 PRO HG2 H 1.940 . . 327 . 29 PRO HD3 H 3.698 . . 328 . 29 PRO HD2 H 3.095 . . 329 . 29 PRO CA C 60.277 . . 330 . 29 PRO CB C 30.730 . . 331 . 29 PRO CG C 25.790 . . 332 . 29 PRO CD C 48.545 . . 333 . 30 ASN HA H 4.168 . . 334 . 30 ASN HB3 H 2.871 . . 335 . 30 ASN HB2 H 2.645 . . 336 . 30 ASN HD21 H 7.733 . . 337 . 30 ASN HD22 H 7.101 . . 338 . 30 ASN CA C 55.372 . . 339 . 30 ASN CB C 36.688 . . 340 . 30 ASN ND2 N 112.937 . . 341 . 31 LEU H H 8.759 . . 342 . 31 LEU HA H 3.976 . . 343 . 31 LEU HB3 H 1.735 . . 344 . 31 LEU HB2 H 1.507 . . 345 . 31 LEU HG H 1.652 . . 346 . 31 LEU HD1 H 0.924 . . 347 . 31 LEU HD2 H 0.879 . . 348 . 31 LEU N N 117.970 . . 349 . 31 LEU CB C 40.233 . . 350 . 31 LEU CA C 56.459 . . 351 . 31 LEU CD2 C 22.668 . . 352 . 31 LEU CD1 C 22.718 . . 353 . 31 LEU CG C 25.100 . . 354 . 32 VAL H H 6.787 . . 355 . 32 VAL HA H 3.709 . . 356 . 32 VAL HB H 1.937 . . 357 . 32 VAL HG1 H 0.911 . . 358 . 32 VAL HG2 H 0.973 . . 359 . 32 VAL N N 119.038 . . 360 . 32 VAL CA C 62.962 . . 361 . 32 VAL CB C 29.962 . . 362 . 32 VAL CG1 C 19.778 . . 363 . 32 VAL CG2 C 20.677 . . 364 . 33 ALA H H 7.815 . . 365 . 33 ALA HA H 3.811 . . 366 . 33 ALA HB H 1.519 . . 367 . 33 ALA N N 122.936 . . 368 . 33 ALA CB C 17.910 . . 369 . 33 ALA CA C 53.372 . . 370 . 34 ARG H H 8.799 . . 371 . 34 ARG HA H 3.774 . . 372 . 34 ARG HB3 H 1.886 . . 373 . 34 ARG HB2 H 1.853 . . 374 . 34 ARG HG3 H 1.715 . . 375 . 34 ARG HG2 H 1.678 . . 376 . 34 ARG HD3 H 3.196 . . 377 . 34 ARG HD2 H 3.162 . . 378 . 34 ARG N N 117.723 . . 379 . 34 ARG CA C 57.160 . . 380 . 34 ARG CB C 27.805 . . 381 . 34 ARG CG C 25.627 . . 382 . 34 ARG CD C 41.396 . . 383 . 35 GLN H H 7.451 . . 384 . 35 GLN HA H 3.995 . . 385 . 35 GLN HB3 H 2.266 . . 386 . 35 GLN HB2 H 2.155 . . 387 . 35 GLN HG3 H 2.480 . . 388 . 35 GLN HG2 H 2.403 . . 389 . 35 GLN HE21 H 7.326 . . 390 . 35 GLN HE22 H 6.775 . . 391 . 35 GLN N N 119.712 . . 392 . 35 GLN CA C 56.620 . . 393 . 35 GLN CB C 25.820 . . 394 . 35 GLN CG C 31.610 . . 395 . 35 GLN NE2 N 111.927 . . 396 . 36 ILE H H 7.550 . . 397 . 36 ILE HA H 3.528 . . 398 . 36 ILE HB H 1.847 . . 399 . 36 ILE HG13 H 1.831 . . 400 . 36 ILE HG12 H 0.919 . . 401 . 36 ILE HG2 H 0.593 . . 402 . 36 ILE HD1 H 0.627 . . 403 . 36 ILE N N 121.168 . . 404 . 36 ILE CA C 63.114 . . 405 . 36 ILE CB C 35.931 . . 406 . 36 ILE CG1 C 26.400 . . 407 . 36 ILE CG2 C 14.785 . . 408 . 36 ILE CD1 C 12.724 . . 409 . 37 VAL H H 7.598 . . 410 . 37 VAL HA H 2.731 . . 411 . 37 VAL HB H 1.827 . . 412 . 37 VAL HG1 H 0.967 . . 413 . 37 VAL HG2 H 0.931 . . 414 . 37 VAL N N 120.840 . . 415 . 37 VAL CA C 64.848 . . 416 . 37 VAL CB C 29.446 . . 417 . 37 VAL CG1 C 19.607 . . 418 . 37 VAL CG2 C 21.311 . . 419 . 38 ASN H H 8.630 . . 420 . 38 ASN HA H 4.444 . . 421 . 38 ASN HB3 H 2.822 . . 422 . 38 ASN HB2 H 2.761 . . 423 . 38 ASN HD21 H 7.468 . . 424 . 38 ASN HD22 H 6.793 . . 425 . 38 ASN N N 116.639 . . 426 . 38 ASN CA C 52.545 . . 427 . 38 ASN CB C 35.856 . . 428 . 38 ASN ND2 N 111.149 . . 429 . 39 SER H H 7.338 . . 430 . 39 SER HA H 4.368 . . 431 . 39 SER HB3 H 3.975 . . 432 . 39 SER HB2 H 3.975 . . 433 . 39 SER N N 113.951 . . 434 . 39 SER CA C 56.810 . . 435 . 39 SER CB C 61.597 . . 436 . 40 CYS H H 7.392 . . 437 . 40 CYS HA H 4.473 . . 438 . 40 CYS HB3 H 3.540 . . 439 . 40 CYS HB2 H 2.869 . . 440 . 40 CYS N N 125.928 . . 441 . 40 CYS CA C 56.210 . . 442 . 40 CYS CB C 26.889 . . 443 . 41 ALA H H 9.142 . . 444 . 41 ALA HA H 4.103 . . 445 . 41 ALA HB H 1.520 . . 446 . 41 ALA N N 134.186 . . 447 . 41 ALA CB C 16.553 . . 448 . 41 ALA CA C 53.141 . . 449 . 42 GLN H H 8.424 . . 450 . 42 GLN HA H 4.167 . . 451 . 42 GLN HB3 H 2.064 . . 452 . 42 GLN HB2 H 1.881 . . 453 . 42 GLN HG3 H 2.267 . . 454 . 42 GLN HG2 H 2.193 . . 455 . 42 GLN HE21 H 7.368 . . 456 . 42 GLN HE22 H 6.622 . . 457 . 42 GLN N N 119.388 . . 458 . 42 GLN CA C 56.919 . . 459 . 42 GLN CB C 27.810 . . 460 . 42 GLN CG C 32.230 . . 461 . 42 GLN NE2 N 112.824 . . 462 . 43 CYS H H 8.561 . . 463 . 43 CYS HA H 4.218 . . 464 . 43 CYS HB3 H 3.113 . . 465 . 43 CYS HB2 H 3.089 . . 466 . 43 CYS N N 122.149 . . 467 . 43 CYS CA C 62.058 . . 468 . 43 CYS CB C 27.287 . . 469 . 44 GLN H H 8.135 . . 470 . 44 GLN HA H 4.178 . . 471 . 44 GLN HB3 H 2.149 . . 472 . 44 GLN HB2 H 2.136 . . 473 . 44 GLN HG3 H 2.480 . . 474 . 44 GLN HG2 H 2.441 . . 475 . 44 GLN HE21 H 7.320 . . 476 . 44 GLN HE22 H 6.821 . . 477 . 44 GLN N N 119.848 . . 478 . 44 GLN CA C 55.044 . . 479 . 44 GLN CB C 26.607 . . 480 . 44 GLN CG C 31.644 . . 481 . 44 GLN NE2 N 113.234 . . 482 . 45 GLN H H 7.889 . . 483 . 45 GLN HA H 4.248 . . 484 . 45 GLN HB3 H 2.172 . . 485 . 45 GLN HB2 H 2.093 . . 486 . 45 GLN HG3 H 2.486 . . 487 . 45 GLN HG2 H 2.426 . . 488 . 45 GLN HE21 H 7.517 . . 489 . 45 GLN HE22 H 6.831 . . 490 . 45 GLN N N 119.655 . . 491 . 45 GLN CA C 54.489 . . 492 . 45 GLN CB C 26.800 . . 493 . 45 GLN CG C 31.850 . . 494 . 45 GLN NE2 N 113.052 . . 495 . 46 LYS H H 8.043 . . 496 . 46 LYS HA H 4.303 . . 497 . 46 LYS HB3 H 1.917 . . 498 . 46 LYS HB2 H 1.848 . . 499 . 46 LYS HG3 H 1.538 . . 500 . 46 LYS HG2 H 1.464 . . 501 . 46 LYS HD3 H 1.709 . . 502 . 46 LYS HD2 H 1.709 . . 503 . 46 LYS HE3 H 3.017 . . 504 . 46 LYS HE2 H 3.017 . . 505 . 46 LYS N N 121.592 . . 506 . 46 LYS CA C 54.700 . . 507 . 46 LYS CB C 30.910 . . 508 . 46 LYS CG C 23.023 . . 509 . 46 LYS CD C 27.000 . . 510 . 46 LYS CE C 39.906 . . 511 . 47 GLY H H 8.202 . . 512 . 47 GLY HA3 H 3.981 . . 513 . 47 GLY HA2 H 3.981 . . 514 . 47 GLY N N 109.793 . . 515 . 47 GLY CA C 43.306 . . 516 . 48 GLU H H 8.224 . . 517 . 48 GLU HA H 4.280 . . 518 . 48 GLU HB3 H 2.064 . . 519 . 48 GLU HB2 H 1.948 . . 520 . 48 GLU HG3 H 2.315 . . 521 . 48 GLU HG2 H 2.277 . . 522 . 48 GLU N N 121.446 . . 523 . 48 GLU CA C 54.387 . . 524 . 48 GLU CG C 34.136 . . 525 . 48 GLU CB C 28.310 . . 526 . 49 ALA H H 8.264 . . 527 . 49 ALA HA H 4.314 . . 528 . 49 ALA HB H 1.367 . . 529 . 49 ALA N N 125.657 . . 530 . 49 ALA CB C 17.156 . . 531 . 49 ALA CA C 50.412 . . 532 . 50 ILE H H 7.963 . . 533 . 50 ILE HA H 4.093 . . 534 . 50 ILE HB H 1.797 . . 535 . 50 ILE HG13 H 1.366 . . 536 . 50 ILE HG12 H 1.134 . . 537 . 50 ILE HG2 H 0.805 . . 538 . 50 ILE HD1 H 0.805 . . 539 . 50 ILE N N 120.168 . . 540 . 50 ILE CB C 36.520 . . 541 . 50 ILE CA C 59.071 . . 542 . 50 ILE CG1 C 25.196 . . 543 . 50 ILE CG2 C 15.545 . . 544 . 50 ILE CD1 C 10.990 . . 545 . 51 HIS H H 8.354 . . 546 . 51 HIS HA H 4.710 . . 547 . 51 HIS HB3 H 3.234 . . 548 . 51 HIS HB2 H 3.137 . . 549 . 51 HIS HD2 H 7.172 . . 550 . 51 HIS HE1 H 8.190 . . 551 . 51 HIS N N 123.390 . . 552 . 51 HIS CA C 53.470 . . 553 . 51 HIS CB C 27.625 . . 554 . 51 HIS CD2 C 134.871 . . 555 . 52 GLY HA3 H 3.957 . . 556 . 52 GLY HA2 H 3.957 . . 557 . 52 GLY CA C 43.095 . . 558 . 52 GLY H H 8.340 . . 559 . 52 GLY N N 110.960 . . 560 . 53 GLN H H 8.248 . . 561 . 53 GLN HA H 4.394 . . 562 . 53 GLN HB3 H 2.108 . . 563 . 53 GLN HB2 H 1.995 . . 564 . 53 GLN HG3 H 2.360 . . 565 . 53 GLN HG2 H 2.335 . . 566 . 53 GLN HE21 H 7.584 . . 567 . 53 GLN HE22 H 6.851 . . 568 . 53 GLN N N 121.184 . . 569 . 53 GLN CA C 53.660 . . 570 . 53 GLN CB C 27.567 . . 571 . 53 GLN CG C 31.700 . . 572 . 53 GLN NE2 N 113.586 . . 573 . 54 VAL H H 8.248 . . 574 . 54 VAL HA H 4.165 . . 575 . 54 VAL HB H 2.096 . . 576 . 54 VAL HG1 H 0.931 . . 577 . 54 VAL HG2 H 0.911 . . 578 . 54 VAL N N 122.516 . . 579 . 54 VAL CA C 60.109 . . 580 . 54 VAL CB C 30.810 . . 581 . 54 VAL CG1 C 19.385 . . 582 . 54 VAL CG2 C 18.363 . . 583 . 55 ASN H H 8.073 . . 584 . 55 ASN HA H 4.488 . . 585 . 55 ASN HB3 H 2.774 . . 586 . 55 ASN HB2 H 2.669 . . 587 . 55 ASN HD21 H 7.500 . . 588 . 55 ASN HD22 H 6.802 . . 589 . 55 ASN N N 128.509 . . 590 . 55 ASN CA C 52.658 . . 591 . 55 ASN CB C 38.427 . . 592 . 55 ASN ND2 N 113.752 . . stop_ save_