data_4951 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Structure of the Anchor-Domain of Myristoylated and Non-myristoylated HIV-1 Nef Protein ; _BMRB_accession_number 4951 _BMRB_flat_file_name bmr4951.str _Entry_type original _Submission_date 2001-01-31 _Accession_date 2001-01-31 _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 Geyer Matthias . . 2 Munte Claudia E. . 3 Kalbitzer Hans R. . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 350 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2008-08-11 update BMRB 'Updating non-standard residue' 2008-07-17 update BMRB 'Updating non-standard residue' 2001-03-09 original author . stop_ _Original_release_date 2015-08-05 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; Structure of the Anchor-Domain of Myristoylated and Non-myristoylated HIV-1 Nef Protein ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code 99272560 _PubMed_ID ? loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Geyer Matthias . . 2 Munte Claudia E. . 3 Schorr Jacqueline . . 4 Kellner Roland . . 5 Kalbitzer Hans R. . stop_ _Journal_abbreviation 'J. Mol. Biol.' _Journal_volume 289 _Journal_issue 1 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 123 _Page_last 138 _Year 1999 _Details . loop_ _Keyword HIV 'NMR spectroscopy' Nef myristoylation myristylation 'structure determination' stop_ save_ ####################################### # Cited references within the entry # ####################################### save_ref_1 _Saveframe_category citation _Citation_full ; Neidig KP, Geyer M, Gorler A, Antz C, Saffrich R, Beneicke W, Kalbitzer HR. AURELIA, A program for computer-aided analysis of multidimensional NMR spectra. Journal of Biomolecular NMR, 6:255-270, 1995. ; _Citation_title . _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID ? loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 . . . . stop_ _Journal_abbreviation . _Journal_name_full . _Journal_volume . _Journal_issue . _Journal_CSD . _Book_title . _Book_chapter_title . _Book_volume . _Book_series . _Book_publisher . _Book_publisher_city . _Book_ISBN . _Conference_title . _Conference_site . _Conference_state_province . _Conference_country . _Conference_start_date . _Conference_end_date . _Conference_abstract_number . _Thesis_institution . _Thesis_institution_city . _Thesis_institution_country . _Page_first . _Page_last . _Year . _Details . save_ ################################## # Molecular system description # ################################## save_system_Nef _Saveframe_category molecular_system _Mol_system_name 'HIV-1 Nef' _Abbreviation_common Nef _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'myristoylated Nef anchor domain (Myr-2-57)' $myristoylated_Nef_anchor_domain stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state monomer _System_paramagnetic no _System_thiol_state 'all free' loop_ _Biological_function 'HIV accessory protein' 'membrane anchoring domain' stop_ _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_myristoylated_Nef_anchor_domain _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'HIV-1 Negative Factor' _Abbreviation_common Nef _Molecular_mass 6022 _Mol_thiol_state 'all free' _Details ; The molecule is myristoylated at Gly-2, which represents the natural co-translational modification of the HIV Nef protein ; ############################## # Polymer residue sequence # ############################## _Residue_count 58 _Mol_residue_sequence ; XGGKWSKSSVVGWPAVRERM RRAEPAADGVGAASRDLEKH GAITSSNTAANNAACAWX ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 1 MYR 2 2 GLY 3 3 GLY 4 4 LYS 5 5 TRP 6 6 SER 7 7 LYS 8 8 SER 9 9 SER 10 10 VAL 11 11 VAL 12 12 GLY 13 13 TRP 14 14 PRO 15 15 ALA 16 16 VAL 17 17 ARG 18 18 GLU 19 19 ARG 20 20 MET 21 21 ARG 22 22 ARG 23 23 ALA 24 24 GLU 25 25 PRO 26 26 ALA 27 27 ALA 28 28 ASP 29 29 GLY 30 30 VAL 31 31 GLY 32 32 ALA 33 33 ALA 34 34 SER 35 35 ARG 36 36 ASP 37 37 LEU 38 38 GLU 39 39 LYS 40 40 HIS 41 41 GLY 42 42 ALA 43 43 ILE 44 44 THR 45 45 SER 46 46 SER 47 47 ASN 48 48 THR 49 49 ALA 50 50 ALA 51 51 ASN 52 52 ASN 53 53 ALA 54 54 ALA 55 55 CYS 56 56 ALA 57 57 TRP 58 58 NH2 stop_ _Sequence_homology_query_date 2008-03-24 _Sequence_homology_query_revised_last_date 2008-01-16 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 4950 'HIV-1 Negative Factor' 101.79 56 100 100 2e-24 PDB 1QA4 'A Chain A, Hiv-1 Nef Anchor Domain, Nmr, 2Structures' 101.79 56 100 100 2e-24 PDB 1QA5 'A Chain A, Myristoylated Hiv-1 Nef AnchorDomain, Nmr, 2 Structures' 98.28 58 100 100 2e-24 DBJ BAC02670.1 'envelope glycoprotein [Humanimmunodeficiency virus 1]' 40.14 142 98 100 2e-24 DBJ BAC02671.1 'envelope glycoprotein [Humanimmunodeficiency virus 1]' 40.14 142 98 100 2e-24 EMBL CAA26947.1 'unnamed protein product [Aids-associatedretrovirus]' 27.67 206 100 100 2e-24 GenBank AAA44206.1 'nef protein [Human immunodeficiencyvirus 1]' 46.34 123 98 98 8e-24 GenBank AAA45001.1 'nef protein' 27.67 206 100 100 2e-24 GenBank AAB59874.1 'nef protein [Human immunodeficiencyvirus type 1]' 27.67 206 98 100 2e-24 GenBank AAD02461.1 'nef protein [Human immunodeficiencyvirus type 1]' 27.67 206 98 98 5e-24 PIR S03245 'nef protein (clone HXB3) - humanimmunodeficiency virus type 1' 27.67 206 100 100 2e-24 PRF 1103299A "E' gene" 27.67 206 98 100 2e-24 SWISS-PROT P04324 "NEF_HV112 Protein Nef (Negative factor)(F-protein) (3'ORF) [Contains: C-terminal core protein]" 27.67 206 100 100 2e-24 SWISS-PROT P05854 "NEF_HV1H3 Protein Nef (Negative factor)(F-protein) (3'ORF) [Contains: C-terminal core protein]" 27.67 206 100 100 2e-24 SWISS-PROT P03404 "NEF_HV1B1 Protein Nef (Negative factor)(F-protein) (3'ORF) [Contains: C-terminal core protein]" 27.67 206 98 100 2e-24 stop_ save_ ###################### # Polymer residues # ###################### save_chem_comp_MYR _Saveframe_category polymer_residue _Mol_type non-polymer _Name_common 'MYRISTIC ACID' _BMRB_code . _PDB_code MYR _Standard_residue_derivative . _Molecular_mass 228.371 _Mol_paramagnetic . _Details ; Information obtained from PDB's Chemical Component Dictionary at http://wwpdb-remediation.rutgers.edu/downloads.html Downloaded on Thu Jul 21 09:28:18 2011 ; loop_ _Atom_name _PDB_atom_name _Atom_type _Atom_chirality _Atom_charge _Atom_oxidation_number _Atom_unpaired_electrons C1 C1 C . 0 . ? O1 O1 O . 0 . ? O2 O2 O . 0 . ? C2 C2 C . 0 . ? C3 C3 C . 0 . ? C4 C4 C . 0 . ? C5 C5 C . 0 . ? C6 C6 C . 0 . ? C7 C7 C . 0 . ? C8 C8 C . 0 . ? C9 C9 C . 0 . ? C10 C10 C . 0 . ? C11 C11 C . 0 . ? C12 C12 C . 0 . ? C13 C13 C . 0 . ? C14 C14 C . 0 . ? HO2 HO2 H . 0 . ? H21 H21 H . 0 . ? H22 H22 H . 0 . ? H31 H31 H . 0 . ? H32 H32 H . 0 . ? H41 H41 H . 0 . ? H42 H42 H . 0 . ? H51 H51 H . 0 . ? H52 H52 H . 0 . ? H61 H61 H . 0 . ? H62 H62 H . 0 . ? H71 H71 H . 0 . ? H72 H72 H . 0 . ? H81 H81 H . 0 . ? H82 H82 H . 0 . ? H91 H91 H . 0 . ? H92 H92 H . 0 . ? H101 H101 H . 0 . ? H102 H102 H . 0 . ? H111 H111 H . 0 . ? H112 H112 H . 0 . ? H121 H121 H . 0 . ? H122 H122 H . 0 . ? H131 H131 H . 0 . ? H132 H132 H . 0 . ? H141 H141 H . 0 . ? H142 H142 H . 0 . ? H143 H143 H . 0 . ? stop_ loop_ _Bond_order _Bond_atom_one_atom_name _Bond_atom_two_atom_name _PDB_bond_atom_one_atom_name _PDB_bond_atom_two_atom_name DOUB C1 O1 ? ? SING C1 O2 ? ? SING C1 C2 ? ? SING O2 HO2 ? ? SING C2 C3 ? ? SING C2 H21 ? ? SING C2 H22 ? ? SING C3 C4 ? ? SING C3 H31 ? ? SING C3 H32 ? ? SING C4 C5 ? ? SING C4 H41 ? ? SING C4 H42 ? ? SING C5 C6 ? ? SING C5 H51 ? ? SING C5 H52 ? ? SING C6 C7 ? ? SING C6 H61 ? ? SING C6 H62 ? ? SING C7 C8 ? ? SING C7 H71 ? ? SING C7 H72 ? ? SING C8 C9 ? ? SING C8 H81 ? ? SING C8 H82 ? ? SING C9 C10 ? ? SING C9 H91 ? ? SING C9 H92 ? ? SING C10 C11 ? ? SING C10 H101 ? ? SING C10 H102 ? ? SING C11 C12 ? ? SING C11 H111 ? ? SING C11 H112 ? ? SING C12 C13 ? ? SING C12 H121 ? ? SING C12 H122 ? ? SING C13 C14 ? ? SING C13 H131 ? ? SING C13 H132 ? ? SING C14 H141 ? ? SING C14 H142 ? ? SING C14 H143 ? ? stop_ save_ save_chem_comp_NH2 _Saveframe_category polymer_residue _Mol_type non-polymer _Name_common 'AMINO GROUP' _BMRB_code . _PDB_code NH2 _Standard_residue_derivative . _Molecular_mass 16.023 _Mol_paramagnetic . _Details ; Information obtained from PDB's Chemical Component Dictionary at http://wwpdb-remediation.rutgers.edu/downloads.html Downloaded on Wed Jul 20 11:58:19 2011 ; loop_ _Atom_name _PDB_atom_name _Atom_type _Atom_chirality _Atom_charge _Atom_oxidation_number _Atom_unpaired_electrons N N N . 0 . ? HN1 HN1 H . 0 . ? HN2 HN2 H . 0 . ? stop_ loop_ _Bond_order _Bond_atom_one_atom_name _Bond_atom_two_atom_name _PDB_bond_atom_one_atom_name _PDB_bond_atom_two_atom_name SING N HN1 ? ? SING N HN2 ? ? stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $myristoylated_Nef_anchor_domain 'Human immunodeficiency virus type 1' 11676 viruses . HIV-1 'BEN allele (Nef_Hv112)' 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 $myristoylated_Nef_anchor_domain '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 $myristoylated_Nef_anchor_domain 0.37 mM 0.2 0.37 . stop_ save_ ############################ # Computer software used # ############################ save_AURELIA _Saveframe_category software _Name AURELIA _Version . loop_ _Task 'automated peak assignments' stop_ _Details . _Citation_label $ref_1 save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model 'DMX Avance' _Field_strength 800 _Details . save_ save_NMR_spectrometer_2 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model AMX _Field_strength 500 _Details . save_ ############################# # NMR applied experiments # ############################# save_1H-1H_NOESY_1 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-1H NOESY' _Sample_label $sample_1 save_ save_ROESY_2 _Saveframe_category NMR_applied_experiment _Experiment_name ROESY _Sample_label $sample_1 save_ save_TOCSY_3 _Saveframe_category NMR_applied_experiment _Experiment_name TOCSY _Sample_label $sample_1 save_ save_COSY_4 _Saveframe_category NMR_applied_experiment _Experiment_name COSY _Sample_label $sample_1 save_ save_NMR_applied_experiment _Saveframe_category NMR_applied_experiment _Experiment_name NMR_applied_experiment _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_1 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-1H NOESY' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_2 _Saveframe_category NMR_applied_experiment _Experiment_name ROESY _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_3 _Saveframe_category NMR_applied_experiment _Experiment_name TOCSY _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_4 _Saveframe_category NMR_applied_experiment _Experiment_name COSY _BMRB_pulse_sequence_accession_number . _Details . save_ ####################### # Sample conditions # ####################### save_Ex-cond_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 4.6 0.2 n/a temperature 285 1 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 DSS H 1 'methyl protons' ppm 0.0 internal direct . . . 1.0 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_shift_set_1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $Ex-cond_1 _Chem_shift_reference_set_label $chemical_shift_reference _Mol_system_component_name 'myristoylated Nef anchor domain (Myr-2-57)' _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 MYR H21 H 2.27 0.005 2 2 . 1 MYR H22 H 2.27 0.005 2 3 . 1 MYR H31 H 1.53 0.005 2 4 . 1 MYR H32 H 1.53 0.005 2 5 . 1 MYR H41 H 1.21 0.005 2 6 . 1 MYR H42 H 1.21 0.005 2 7 . 1 MYR H51 H 1.16 0.005 2 8 . 1 MYR H52 H 1.16 0.005 2 9 . 1 MYR H61 H 1.13 0.01 4 10 . 1 MYR H62 H 1.13 0.01 4 11 . 1 MYR H71 H 1.13 0.01 4 12 . 1 MYR H72 H 1.13 0.01 4 13 . 1 MYR H81 H 1.13 0.01 4 14 . 1 MYR H82 H 1.13 0.01 4 15 . 1 MYR H91 H 1.13 0.01 4 16 . 1 MYR H92 H 1.13 0.01 4 17 . 1 MYR H101 H 1.13 0.01 4 18 . 1 MYR H102 H 1.13 0.01 4 19 . 1 MYR H111 H 1.13 0.01 4 20 . 1 MYR H112 H 1.13 0.01 4 21 . 1 MYR H121 H 1.14 0.01 1 22 . 1 MYR H122 H 1.14 0.01 1 23 . 1 MYR H131 H 1.19 0.005 1 24 . 1 MYR H132 H 1.19 0.005 1 25 . 1 MYR H141 H 0.83 0.005 1 26 . 1 MYR H142 H 0.83 0.005 1 27 . 1 MYR H143 H 0.83 0.005 1 28 . 2 GLY H H 8.31 0.005 1 29 . 2 GLY HA2 H 3.91 0.01 1 30 . 2 GLY HA3 H 3.91 0.01 1 31 . 3 GLY H H 8.35 0.005 1 32 . 3 GLY HA2 H 3.86 0.01 1 33 . 3 GLY HA3 H 3.86 0.01 1 34 . 4 LYS H H 8.25 0.005 1 35 . 4 LYS HA H 4.16 0.005 1 36 . 4 LYS HB2 H 1.55 0.01 1 37 . 4 LYS HB3 H 1.55 0.01 1 38 . 4 LYS HG2 H 1.09 0.01 1 39 . 4 LYS HG3 H 1.09 0.01 1 40 . 4 LYS HD2 H 1.49 0.01 1 41 . 4 LYS HD3 H 1.49 0.01 1 42 . 4 LYS HE2 H 2.80 0.01 1 43 . 4 LYS HE3 H 2.80 0.01 1 44 . 4 LYS HZ H 7.50 0.005 1 45 . 5 TRP H H 8.10 0.005 1 46 . 5 TRP HA H 4.63 0.005 1 47 . 5 TRP HB2 H 3.29 0.005 1 48 . 5 TRP HB3 H 3.16 0.005 1 49 . 5 TRP HD1 H 7.20 0.005 1 50 . 5 TRP HE1 H 10.13 0.005 1 51 . 5 TRP HE3 H 7.56 0.005 1 52 . 5 TRP HZ2 H 7.42 0.005 1 53 . 5 TRP HZ3 H 7.07 0.005 1 54 . 5 TRP HH2 H 7.15 0.005 1 55 . 6 SER H H 7.96 0.005 1 56 . 6 SER HA H 4.31 0.005 1 57 . 6 SER HB2 H 3.78 0.005 1 58 . 6 SER HB3 H 3.71 0.005 1 59 . 7 LYS H H 8.30 0.005 1 60 . 7 LYS HA H 4.19 0.005 1 61 . 7 LYS HB2 H 1.80 0.005 1 62 . 7 LYS HB3 H 1.70 0.005 1 63 . 7 LYS HG2 H 1.38 0.01 1 64 . 7 LYS HG3 H 1.38 0.01 1 65 . 7 LYS HD2 H 1.63 0.01 1 66 . 7 LYS HD3 H 1.63 0.01 1 67 . 7 LYS HE2 H 2.93 0.01 1 68 . 7 LYS HE3 H 2.93 0.01 1 69 . 7 LYS HZ H 7.54 0.005 1 70 . 8 SER H H 8.22 0.005 1 71 . 8 SER HA H 4.39 0.005 1 72 . 8 SER HB2 H 3.83 0.005 1 73 . 8 SER HB3 H 3.77 0.005 1 74 . 9 SER H H 8.26 0.005 1 75 . 9 SER HA H 4.41 0.005 1 76 . 9 SER HB2 H 3.82 0.005 1 77 . 9 SER HB3 H 3.78 0.005 1 78 . 10 VAL H H 8.08 0.005 1 79 . 10 VAL HA H 4.03 0.005 1 80 . 10 VAL HB H 2.00 0.005 1 81 . 10 VAL HG1 H 0.84 0.005 1 82 . 10 VAL HG2 H 0.81 0.005 1 83 . 11 VAL H H 8.14 0.005 1 84 . 11 VAL HA H 3.99 0.005 1 85 . 11 VAL HB H 1.96 0.005 1 86 . 11 VAL HG1 H 0.87 0.005 1 87 . 11 VAL HG2 H 0.82 0.005 1 88 . 12 GLY H H 8.32 0.005 1 89 . 12 GLY HA2 H 3.83 0.005 1 90 . 12 GLY HA3 H 3.83 0.005 1 91 . 13 TRP H H 8.15 0.005 1 92 . 13 TRP HA H 4.85 0.005 1 93 . 13 TRP HB2 H 3.28 0.005 1 94 . 13 TRP HB3 H 3.12 0.005 1 95 . 13 TRP HD1 H 7.20 0.005 1 96 . 13 TRP HE1 H 10.12 0.005 1 97 . 13 TRP HE3 H 7.59 0.005 1 98 . 13 TRP HZ2 H 7.43 0.005 1 99 . 13 TRP HZ3 H 7.09 0.005 1 100 . 13 TRP HH2 H 7.17 0.005 1 101 . 14 PRO HA H 4.29 0.005 1 102 . 14 PRO HB2 H 2.23 0.005 1 103 . 14 PRO HB3 H 1.96 0.005 1 104 . 14 PRO HG2 H 1.86 0.005 1 105 . 14 PRO HG3 H 1.84 0.005 1 106 . 14 PRO HD2 H 3.74 0.005 1 107 . 14 PRO HD3 H 3.48 0.005 1 108 . 15 ALA H H 8.33 0.005 1 109 . 15 ALA HA H 4.25 0.005 1 110 . 15 ALA HB H 1.37 0.005 1 111 . 16 VAL H H 8.05 0.005 1 112 . 16 VAL HA H 3.90 0.005 1 113 . 16 VAL HB H 2.06 0.005 1 114 . 16 VAL HG1 H 0.93 0.005 1 115 . 16 VAL HG2 H 0.91 0.005 1 116 . 17 ARG H H 8.36 0.005 1 117 . 17 ARG HA H 4.22 0.005 1 118 . 17 ARG HB2 H 1.81 0.005 1 119 . 17 ARG HB3 H 1.73 0.005 1 120 . 17 ARG HG2 H 1.62 0.005 1 121 . 17 ARG HG3 H 1.58 0.005 1 122 . 17 ARG HD2 H 3.15 0.01 1 123 . 17 ARG HD3 H 3.15 0.01 1 124 . 17 ARG HE H 7.26 0.005 1 125 . 17 ARG HH11 H 6.32 0.05 5 126 . 17 ARG HH12 H 6.32 0.05 5 127 . 17 ARG HH21 H 6.53 0.05 5 128 . 17 ARG HH22 H 6.53 0.05 5 129 . 18 GLU H H 8.29 0.005 1 130 . 18 GLU HA H 4.21 0.005 1 131 . 18 GLU HB2 H 2.01 0.005 1 132 . 18 GLU HB3 H 1.96 0.005 1 133 . 18 GLU HG2 H 2.33 0.01 1 134 . 18 GLU HG3 H 2.33 0.01 1 135 . 19 ARG H H 8.36 0.005 1 136 . 19 ARG HA H 4.15 0.005 1 137 . 19 ARG HB2 H 1.74 0.005 1 138 . 19 ARG HB3 H 1.60 0.005 1 139 . 19 ARG HG2 H 1.57 0.005 1 140 . 19 ARG HG3 H 1.51 0.005 1 141 . 19 ARG HD2 H 3.08 0.01 1 142 . 19 ARG HD3 H 3.08 0.01 1 143 . 19 ARG HE H 7.20 0.005 1 144 . 19 ARG HH11 H 6.32 0.05 5 145 . 19 ARG HH12 H 6.32 0.05 5 146 . 19 ARG HH21 H 6.53 0.05 5 147 . 19 ARG HH22 H 6.53 0.05 5 148 . 20 MET H H 8.29 0.005 1 149 . 20 MET HA H 4.35 0.005 1 150 . 20 MET HB2 H 2.03 0.005 1 151 . 20 MET HB3 H 1.98 0.005 1 152 . 20 MET HG2 H 2.59 0.005 1 153 . 20 MET HG3 H 2.49 0.005 1 154 . 20 MET HE H 2.05 0.005 1 155 . 21 ARG H H 8.30 0.005 1 156 . 21 ARG HA H 4.25 0.005 1 157 . 21 ARG HB2 H 1.81 0.005 1 158 . 21 ARG HB3 H 1.73 0.005 1 159 . 21 ARG HG2 H 1.59 0.005 1 160 . 21 ARG HG3 H 1.56 0.005 1 161 . 21 ARG HD2 H 3.15 0.01 1 162 . 21 ARG HD3 H 3.15 0.01 1 163 . 21 ARG HE H 7.28 0.005 1 164 . 21 ARG HH11 H 6.32 0.05 5 165 . 21 ARG HH12 H 6.32 0.05 5 166 . 21 ARG HH21 H 6.58 0.05 5 167 . 21 ARG HH22 H 6.58 0.05 5 168 . 22 ARG H H 8.44 0.005 1 169 . 22 ARG HA H 4.21 0.005 1 170 . 22 ARG HB2 H 1.85 0.005 1 171 . 22 ARG HB3 H 1.73 0.005 1 172 . 22 ARG HG2 H 1.62 0.01 1 173 . 22 ARG HG3 H 1.62 0.01 1 174 . 22 ARG HD2 H 3.15 0.005 1 175 . 22 ARG HD3 H 3.15 0.005 1 176 . 22 ARG HE H 7.22 0.005 1 177 . 22 ARG HH11 H 6.32 0.05 5 178 . 22 ARG HH12 H 6.32 0.05 5 179 . 22 ARG HH21 H 6.53 0.05 5 180 . 22 ARG HH22 H 6.53 0.05 5 181 . 23 ALA H H 8.37 0.005 1 182 . 23 ALA HA H 4.26 0.005 1 183 . 23 ALA HB H 1.38 0.005 1 184 . 24 GLU H H 8.33 0.005 1 185 . 24 GLU HA H 4.59 0.005 1 186 . 24 GLU HB2 H 2.06 0.005 1 187 . 24 GLU HB3 H 1.84 0.005 1 188 . 24 GLU HG2 H 2.41 0.01 1 189 . 24 GLU HG3 H 2.41 0.01 1 190 . 25 PRO HA H 4.35 0.005 1 191 . 25 PRO HB2 H 2.26 0.005 1 192 . 25 PRO HB3 H 2.01 0.005 1 193 . 25 PRO HG2 H 1.96 0.005 1 194 . 25 PRO HG3 H 1.88 0.005 1 195 . 25 PRO HD2 H 3.75 0.005 1 196 . 25 PRO HD3 H 3.66 0.005 1 197 . 26 ALA H H 8.49 0.005 1 198 . 26 ALA HA H 4.23 0.005 1 199 . 26 ALA HB H 1.35 0.005 1 200 . 27 ALA H H 8.42 0.005 1 201 . 27 ALA HA H 4.26 0.005 1 202 . 27 ALA HB H 1.35 0.005 1 203 . 28 ASP H H 8.35 0.005 1 204 . 28 ASP HA H 4.59 0.005 1 205 . 28 ASP HB2 H 2.74 0.01 1 206 . 28 ASP HB3 H 2.74 0.01 1 207 . 29 GLY H H 8.32 0.005 1 208 . 29 GLY HA2 H 3.95 0.005 1 209 . 29 GLY HA3 H 3.93 0.005 1 210 . 30 VAL H H 8.07 0.005 1 211 . 30 VAL HA H 4.06 0.005 1 212 . 30 VAL HB H 2.08 0.005 1 213 . 30 VAL HG1 H 0.91 0.01 1 214 . 30 VAL HG2 H 0.91 0.01 1 215 . 31 GLY H H 8.63 0.005 1 216 . 31 GLY HA2 H 3.91 0.01 1 217 . 31 GLY HA3 H 3.91 0.01 1 218 . 32 ALA H H 8.22 0.005 1 219 . 32 ALA HA H 4.19 0.005 1 220 . 32 ALA HB H 1.36 0.005 1 221 . 33 ALA H H 8.37 0.005 1 222 . 33 ALA HA H 4.26 0.005 1 223 . 33 ALA HB H 1.38 0.005 1 224 . 34 SER H H 8.21 0.005 1 225 . 34 SER HA H 4.33 0.005 1 226 . 34 SER HB2 H 3.88 0.005 1 227 . 34 SER HB3 H 3.82 0.005 1 228 . 35 ARG H H 8.31 0.005 1 229 . 35 ARG HA H 4.27 0.005 1 230 . 35 ARG HB2 H 1.83 0.005 1 231 . 35 ARG HB3 H 1.74 0.005 1 232 . 35 ARG HG2 H 1.56 0.01 1 233 . 35 ARG HG3 H 1.56 0.01 1 234 . 35 ARG HD2 H 3.16 0.01 1 235 . 35 ARG HD3 H 3.16 0.01 1 236 . 35 ARG HE H 7.22 0.005 1 237 . 35 ARG HH11 H 6.32 0.05 5 238 . 35 ARG HH12 H 6.32 0.05 5 239 . 35 ARG HH21 H 6.53 0.05 5 240 . 35 ARG HH22 H 6.53 0.05 5 241 . 36 ASP H H 8.34 0.005 1 242 . 36 ASP HA H 4.57 0.005 1 243 . 36 ASP HB2 H 2.80 0.005 1 244 . 36 ASP HB3 H 2.65 0.005 1 245 . 37 LEU H H 8.21 0.005 1 246 . 37 LEU HA H 4.23 0.005 1 247 . 37 LEU HB2 H 1.64 0.005 1 248 . 37 LEU HB3 H 1.59 0.005 1 249 . 37 LEU HG H 1.60 0.005 1 250 . 37 LEU HD1 H 0.88 0.005 1 251 . 37 LEU HD2 H 0.82 0.005 1 252 . 38 GLU H H 8.19 0.005 1 253 . 38 GLU HA H 4.21 0.005 1 254 . 38 GLU HB2 H 2.00 0.005 1 255 . 38 GLU HB3 H 1.95 0.005 1 256 . 38 GLU HG2 H 2.36 0.005 1 257 . 38 GLU HG3 H 2.31 0.005 1 258 . 39 LYS H H 8.21 0.005 1 259 . 39 LYS HA H 4.21 0.005 1 260 . 39 LYS HB2 H 1.73 0.005 1 261 . 39 LYS HB3 H 1.68 0.005 1 262 . 39 LYS HG2 H 1.31 0.01 1 263 . 39 LYS HG3 H 1.31 0.01 1 264 . 39 LYS HD2 H 1.62 0.01 1 265 . 39 LYS HD3 H 1.62 0.01 1 266 . 39 LYS HE2 H 2.94 0.01 1 267 . 39 LYS HE3 H 2.94 0.01 1 268 . 39 LYS HZ H 7.55 0.005 1 269 . 40 HIS H H 8.56 0.005 1 270 . 40 HIS HA H 4.68 0.005 1 271 . 40 HIS HB2 H 3.27 0.005 1 272 . 40 HIS HB3 H 3.14 0.005 1 273 . 40 HIS HD2 H 7.27 0.005 1 274 . 40 HIS HE1 H 8.56 0.005 1 275 . 41 GLY H H 8.50 0.005 1 276 . 41 GLY HA2 H 3.94 0.005 1 277 . 41 GLY HA3 H 3.90 0.005 1 278 . 42 ALA H H 8.28 0.005 1 279 . 42 ALA HA H 4.31 0.005 1 280 . 42 ALA HB H 1.34 0.005 1 281 . 43 ILE H H 8.35 0.005 1 282 . 43 ILE HA H 4.21 0.005 1 283 . 43 ILE HB H 1.85 0.005 1 284 . 43 ILE HG12 H 1.48 0.005 1 285 . 43 ILE HG13 H 1.19 0.005 1 286 . 43 ILE HG2 H 0.88 0.005 1 287 . 43 ILE HD1 H 0.82 0.005 1 288 . 44 THR H H 8.35 0.005 1 289 . 44 THR HA H 4.39 0.005 1 290 . 44 THR HB H 4.21 0.005 1 291 . 44 THR HG2 H 1.16 0.005 1 292 . 45 SER H H 8.44 0.005 1 293 . 45 SER HA H 4.47 0.005 1 294 . 45 SER HB2 H 3.89 0.005 1 295 . 45 SER HB3 H 3.82 0.005 1 296 . 46 SER H H 8.46 0.005 1 297 . 46 SER HA H 4.44 0.005 1 298 . 46 SER HB2 H 3.87 0.005 1 299 . 46 SER HB3 H 3.81 0.005 1 300 . 47 ASN H H 8.51 0.005 1 301 . 47 ASN HA H 4.76 0.005 1 302 . 47 ASN HB2 H 2.83 0.005 1 303 . 47 ASN HB3 H 2.76 0.005 1 304 . 47 ASN HD21 H 7.64 0.005 1 305 . 47 ASN HD22 H 6.96 0.005 1 306 . 48 THR H H 8.17 0.005 1 307 . 48 THR HA H 4.25 0.005 1 308 . 48 THR HB H 4.25 0.005 1 309 . 48 THR HG2 H 1.17 0.005 1 310 . 49 ALA H H 8.34 0.005 1 311 . 49 ALA HA H 4.24 0.005 1 312 . 49 ALA HB H 1.37 0.005 1 313 . 50 ALA H H 8.25 0.005 1 314 . 50 ALA HA H 4.21 0.005 1 315 . 50 ALA HB H 1.34 0.005 1 316 . 51 ASN H H 8.31 0.005 1 317 . 51 ASN HA H 4.61 0.005 1 318 . 51 ASN HB2 H 2.80 0.005 1 319 . 51 ASN HB3 H 2.74 0.005 1 320 . 51 ASN HD21 H 7.64 0.005 1 321 . 51 ASN HD22 H 6.94 0.005 1 322 . 52 ASN H H 8.33 0.005 1 323 . 52 ASN HA H 4.63 0.005 1 324 . 52 ASN HB2 H 2.80 0.005 1 325 . 52 ASN HB3 H 2.74 0.005 1 326 . 52 ASN HD21 H 7.62 0.005 1 327 . 52 ASN HD22 H 6.94 0.005 1 328 . 53 ALA H H 8.22 0.005 1 329 . 53 ALA HA H 4.21 0.005 1 330 . 53 ALA HB H 1.36 0.005 1 331 . 54 ALA H H 8.18 0.005 1 332 . 54 ALA HA H 4.17 0.005 1 333 . 54 ALA HB H 1.33 0.005 1 334 . 55 CYS H H 8.11 0.005 1 335 . 55 CYS HA H 4.25 0.005 1 336 . 55 CYS HB2 H 2.68 0.005 1 337 . 55 CYS HB3 H 2.62 0.005 1 338 . 56 ALA H H 8.30 0.005 1 339 . 56 ALA HA H 4.19 0.005 1 340 . 56 ALA HB H 1.26 0.005 1 341 . 57 TRP H H 7.83 0.005 1 342 . 57 TRP HA H 4.63 0.005 1 343 . 57 TRP HB2 H 3.25 0.01 1 344 . 57 TRP HB3 H 3.25 0.01 1 345 . 57 TRP HD1 H 7.20 0.005 1 346 . 57 TRP HE1 H 10.16 0.005 1 347 . 57 TRP HE3 H 7.62 0.005 1 348 . 57 TRP HZ2 H 7.46 0.005 1 349 . 57 TRP HZ3 H 7.12 0.005 1 350 . 57 TRP HH2 H 7.19 0.005 1 stop_ save_