data_6407 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; 1H, 15N resonance assignment of the C-terminal domain of Human Papillomavirus Oncoprotein E6 ; _BMRB_accession_number 6407 _BMRB_flat_file_name bmr6407.str _Entry_type original _Submission_date 2004-12-02 _Accession_date 2004-12-02 _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 Nomine Yves . . 2 Trave Gilles . . 3 Kieffer Bruno . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 459 "15N chemical shifts" 78 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2005-03-18 original author . stop_ _Original_release_date 2005-03-18 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; 1H and 15N resonance assignment, secondary structure and dynamic behaviour of the C-terminal domain of human papillomavirus Oncoprotein E6 ; _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 Nomine Yves . . 2 Charbonnier Sebastian . . 3 Miguet Laurent . . 4 Potier Noelle . . 5 'Van Dorsselaer' Alain . . 6 Atkinson R. Andrew . 7 Trave Gilles . . 8 Kieffer Bruno . . stop_ _Journal_abbreviation 'J. Biomol. NMR' _Journal_volume 31 _Journal_issue 2 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 129 _Page_last 141 _Year 2005 _Details . loop_ _Keyword '3-D NMR' 'C-terminal domain' dynamics 'HPV oncoprotein E6' stop_ save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name 'HPV16 E6 C-terminal domain' _Abbreviation_common 'HPV16 E6 C-terminal domain' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'HPV16 E6 C-terminal domain' $E6-C_4C-4S 'ZINC (II) ION' $ZN stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state protein _System_paramagnetic no _System_thiol_state 'all other bound' loop_ _Biological_function 'induced the p53 ubiquitination' oncoprotein stop_ _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_E6-C_4C-4S _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'C terminal domain of E6' _Name_variant 'E6 C-terminal domain' _Abbreviation_common 'E6 C-terminal domain' _Molecular_mass . _Mol_thiol_state 'all other bound' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 75 _Mol_residue_sequence ; GAMSYSLYGTTLEQQYNKPL SDLLIRCINCQKPLSPEEKQ RHLDKKQRFHNIRGRWTGRC MSCSRSSRTRRETQL ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 77 GLY 2 78 ALA 3 79 MET 4 80 SER 5 81 TYR 6 82 SER 7 83 LEU 8 84 TYR 9 85 GLY 10 86 THR 11 87 THR 12 88 LEU 13 89 GLU 14 90 GLN 15 91 GLN 16 92 TYR 17 93 ASN 18 94 LYS 19 95 PRO 20 96 LEU 21 97 SER 22 98 ASP 23 99 LEU 24 100 LEU 25 101 ILE 26 102 ARG 27 103 CYS 28 104 ILE 29 105 ASN 30 106 CYS 31 107 GLN 32 108 LYS 33 109 PRO 34 110 LEU 35 111 SER 36 112 PRO 37 113 GLU 38 114 GLU 39 115 LYS 40 116 GLN 41 117 ARG 42 118 HIS 43 119 LEU 44 120 ASP 45 121 LYS 46 122 LYS 47 123 GLN 48 124 ARG 49 125 PHE 50 126 HIS 51 127 ASN 52 128 ILE 53 129 ARG 54 130 GLY 55 131 ARG 56 132 TRP 57 133 THR 58 134 GLY 59 135 ARG 60 136 CYS 61 137 MET 62 138 SER 63 139 CYS 64 140 SER 65 141 ARG 66 142 SER 67 143 SER 68 144 ARG 69 145 THR 70 146 ARG 71 147 ARG 72 148 GLU 73 149 THR 74 150 GLN 75 151 LEU stop_ _Sequence_homology_query_date 2010-09-19 _Sequence_homology_query_revised_last_date 2008-08-19 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 2FK4 'Solution Structure Of The C-Terminal Zinc Binding Domain Of The Hpv16 E6 Oncoprotein' 100.00 75 100.00 100.00 6.69e-37 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 Wed Jun 15 12:20:01 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 $E6-C_4C-4S Human 9606 Viruses 'dsDNA viruses' Papillomavirus 'Human Papillomavirus type E6' 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 _Details $E6-C_4C-4S 'recombinant technology' 'E. coli' . . . . ; This construct corresponds to residues 77-151 of HPV16 E6 with four non-conserved cystein residues (80,97, 111 and 140) mutated into serines. At the N-terminus of the construct there are three additional residues (GAM) due to TEV cleveage. ; stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Saveframe_category sample _Sample_type solution _Details ; The E6-C 4C/4S construct corresponds to residues 77-151 of HPV16 E6 with four non-conserved cystein residues (80,97,111 and 140) mutated into serines. At the N-terminus of the construct there are three additional residues (GAM) due to TEV cleavage. ; loop_ _Mol_label _Concentration_value _Concentration_value_units _Concentration_min_value _Concentration_max_value _Isotopic_labeling $E6-C_4C-4S . mM 0.3 1.2 [U-15N] 'Tris-HCl deuterated' 20 mM . . . NaCl 50 mM . . . dithiothreitol 1 mM . . . 'deuterium oxide' 10 % . . . stop_ save_ ############################ # Computer software used # ############################ save_NMRPipe _Saveframe_category software _Name NMRPipe _Version . _Details . save_ save_XEASY _Saveframe_category software _Name XEASY _Version . _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_500MHz_spectrometer _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model DMX _Field_strength 500 _Details . save_ ############################# # NMR applied experiments # ############################# save_1H-15N_HSQC_1 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-15N HSQC' _Sample_label $sample_1 save_ save_15N_NOESY-HSQC_2 _Saveframe_category NMR_applied_experiment _Experiment_name '15N NOESY-HSQC' _Sample_label $sample_1 save_ save_15N_TOCSY-HSQC_3 _Saveframe_category NMR_applied_experiment _Experiment_name '15N TOCSY-HSQC' _Sample_label $sample_1 save_ save_NMR_spec_expt__0_1 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-15N HSQC' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_2 _Saveframe_category NMR_applied_experiment _Experiment_name '15N NOESY-HSQC' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_3 _Saveframe_category NMR_applied_experiment _Experiment_name '15N TOCSY-HSQC' _BMRB_pulse_sequence_accession_number . _Details . save_ ####################### # Sample conditions # ####################### save_conditions_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 6.8 0.1 pH temperature 288 0.1 K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_referencing _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 DSS H 1 'methyl protons' ppm 0.0 external direct . 'outside sample' . 1.0 $entry_citation $entry_citation DSS N 15 'methyl protons' ppm 0.0 external indirect . 'outside sample' . 0.101329118 $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_list_1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $conditions_1 _Chem_shift_reference_set_label $chemical_shift_referencing _Mol_system_component_name 'HPV16 E6 C-terminal domain' _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 . 3 MET H H 8.54 0.01 1 2 . 3 MET HA H 4.49 0.01 1 3 . 3 MET HB2 H 2.04 0.01 1 4 . 3 MET HB3 H 2.04 0.01 1 5 . 3 MET HG2 H 2.55 0.01 1 6 . 3 MET HG3 H 2.55 0.01 1 7 . 3 MET N N 121.05 0.02 1 8 . 4 SER H H 8.28 0.01 1 9 . 4 SER HA H 4.67 0.01 1 10 . 4 SER HB2 H 3.83 0.01 1 11 . 4 SER HB3 H 3.83 0.01 1 12 . 4 SER N N 118.41 0.02 1 13 . 5 TYR H H 8.33 0.01 1 14 . 5 TYR HA H 4.88 0.01 1 15 . 5 TYR HB2 H 3.24 0.01 2 16 . 5 TYR HB3 H 3.01 0.01 2 17 . 5 TYR HD1 H 7.03 0.01 1 18 . 5 TYR HD2 H 7.03 0.01 1 19 . 5 TYR HE1 H 6.77 0.01 1 20 . 5 TYR HE2 H 6.77 0.01 1 21 . 5 TYR N N 122.10 0.02 1 22 . 6 SER H H 8.31 0.01 1 23 . 6 SER HA H 5.59 0.01 1 24 . 6 SER HB2 H 3.50 0.01 2 25 . 6 SER HB3 H 3.35 0.01 2 26 . 6 SER N N 117.89 0.02 1 27 . 7 LEU H H 8.47 0.01 1 28 . 7 LEU HA H 4.76 0.01 1 29 . 7 LEU HB2 H 1.60 0.01 2 30 . 7 LEU HB3 H 1.52 0.01 2 31 . 7 LEU HG H 1.21 0.01 1 32 . 7 LEU HD1 H 1.08 0.01 2 33 . 7 LEU HD2 H 0.73 0.01 2 34 . 7 LEU N N 122.10 0.02 1 35 . 8 TYR H H 8.80 0.01 1 36 . 8 TYR HA H 4.69 0.01 1 37 . 8 TYR HB2 H 3.31 0.01 2 38 . 8 TYR HB3 H 2.86 0.01 2 39 . 8 TYR HD1 H 7.20 0.01 1 40 . 8 TYR HD2 H 7.20 0.01 1 41 . 8 TYR HE1 H 6.80 0.01 1 42 . 8 TYR HE2 H 6.80 0.01 1 43 . 8 TYR N N 119.73 0.02 1 44 . 9 GLY H H 7.61 0.01 1 45 . 9 GLY HA2 H 4.20 0.01 1 46 . 9 GLY HA3 H 4.20 0.01 1 47 . 9 GLY N N 111.30 0.02 1 48 . 10 THR H H 7.52 0.01 1 49 . 10 THR HA H 4.35 0.01 1 50 . 11 THR H H 7.11 0.01 1 51 . 11 THR HA H 4.19 0.01 1 52 . 11 THR HB H 4.07 0.01 1 53 . 11 THR HG2 H 1.50 0.01 1 54 . 11 THR N N 119.20 0.02 1 55 . 12 LEU H H 7.57 0.01 1 56 . 12 LEU HA H 3.73 0.01 1 57 . 12 LEU HB2 H 1.30 0.01 1 58 . 12 LEU HB3 H 1.30 0.01 1 59 . 12 LEU HG H 1.21 0.01 1 60 . 12 LEU HD1 H 0.68 0.01 1 61 . 12 LEU HD2 H 0.68 0.01 1 62 . 12 LEU N N 123.42 0.02 1 63 . 13 GLU H H 7.79 0.01 1 64 . 13 GLU HA H 4.27 0.01 1 65 . 13 GLU HB2 H 2.25 0.01 1 66 . 13 GLU HB3 H 2.25 0.01 1 67 . 13 GLU HG2 H 2.50 0.01 1 68 . 13 GLU HG3 H 2.50 0.01 1 69 . 13 GLU N N 117.62 0.02 1 70 . 14 GLN H H 7.42 0.01 1 71 . 14 GLN HA H 4.05 0.01 1 72 . 14 GLN HB2 H 2.21 0.01 2 73 . 14 GLN HB3 H 2.11 0.01 2 74 . 14 GLN HG2 H 2.53 0.01 2 75 . 14 GLN HG3 H 2.36 0.01 2 76 . 14 GLN HE21 H 6.83 0.01 2 77 . 14 GLN HE22 H 7.52 0.01 2 78 . 14 GLN N N 118.15 0.02 1 79 . 14 GLN NE2 N 112.88 0.02 1 80 . 15 GLN H H 8.32 0.01 1 81 . 15 GLN HA H 3.88 0.01 1 82 . 15 GLN HB2 H 1.92 0.01 2 83 . 15 GLN HB3 H 1.37 0.01 2 84 . 15 GLN HG2 H 2.15 0.01 2 85 . 15 GLN HG3 H 1.75 0.01 2 86 . 15 GLN HE21 H 6.67 0.01 2 87 . 15 GLN HE22 H 7.27 0.01 2 88 . 15 GLN N N 119.73 0.02 1 89 . 15 GLN NE2 N 111.56 0.02 1 90 . 16 TYR H H 7.79 0.01 1 91 . 16 TYR HA H 4.37 0.01 1 92 . 16 TYR HB2 H 3.01 0.01 2 93 . 16 TYR HB3 H 2.59 0.01 2 94 . 16 TYR HD1 H 7.16 0.01 1 95 . 16 TYR HD2 H 7.16 0.01 1 96 . 16 TYR HE1 H 6.68 0.01 1 97 . 16 TYR HE2 H 6.68 0.01 1 98 . 16 TYR N N 114.72 0.02 1 99 . 17 ASN H H 7.98 0.01 1 100 . 17 ASN HA H 4.37 0.01 1 101 . 17 ASN HB2 H 3.12 0.01 2 102 . 17 ASN HB3 H 2.64 0.01 2 103 . 17 ASN HD21 H 7.53 0.01 2 104 . 17 ASN HD22 H 6.78 0.01 2 105 . 17 ASN N N 119.73 0.02 1 106 . 17 ASN ND2 N 113.04 0.12 1 107 . 18 LYS H H 7.64 0.01 1 108 . 18 LYS HA H 4.65 0.01 1 109 . 18 LYS HB2 H 1.70 0.01 2 110 . 18 LYS HB3 H 1.38 0.01 2 111 . 18 LYS HG2 H 1.32 0.01 1 112 . 18 LYS HG3 H 1.32 0.01 1 113 . 18 LYS HD2 H 1.58 0.01 2 114 . 18 LYS HD3 H 1.50 0.01 2 115 . 18 LYS HE2 H 2.92 0.01 2 116 . 18 LYS HE3 H 2.74 0.01 2 117 . 18 LYS N N 117.62 0.02 1 118 . 19 PRO HA H 4.40 0.01 1 119 . 19 PRO HB2 H 2.22 0.01 2 120 . 19 PRO HB3 H 1.91 0.01 2 121 . 19 PRO HG2 H 1.85 0.01 2 122 . 19 PRO HG3 H 1.67 0.01 2 123 . 19 PRO HD2 H 3.61 0.01 2 124 . 19 PRO HD3 H 3.57 0.01 2 125 . 20 LEU H H 8.63 0.01 1 126 . 20 LEU HA H 3.66 0.01 1 127 . 20 LEU HB2 H 1.61 0.01 2 128 . 20 LEU HB3 H 1.31 0.01 2 129 . 20 LEU HG H 1.66 0.01 1 130 . 20 LEU HD1 H 0.66 0.01 2 131 . 20 LEU HD2 H 0.59 0.01 2 132 . 20 LEU N N 113.14 0.02 1 133 . 21 SER H H 9.91 0.01 1 134 . 21 SER HA H 4.39 0.01 1 135 . 21 SER N N 123.42 0.02 1 136 . 22 ASP H H 7.81 0.01 1 137 . 22 ASP HA H 4.58 0.01 1 138 . 22 ASP HB2 H 2.71 0.01 2 139 . 22 ASP HB3 H 2.45 0.01 2 140 . 22 ASP N N 121.84 0.02 1 141 . 23 LEU H H 7.25 0.01 1 142 . 23 LEU HA H 4.15 0.01 1 143 . 23 LEU HB2 H 2.06 0.01 2 144 . 23 LEU HB3 H 0.90 0.01 2 145 . 23 LEU HG H 1.31 0.01 1 146 . 23 LEU HD1 H 0.28 0.01 2 147 . 23 LEU HD2 H 0.24 0.01 2 148 . 23 LEU N N 122.89 0.02 1 149 . 24 LEU H H 8.32 0.01 1 150 . 24 LEU HA H 4.22 0.01 1 151 . 24 LEU HB2 H 1.76 0.01 2 152 . 24 LEU HB3 H 1.40 0.01 2 153 . 24 LEU HG H 0.84 0.01 1 154 . 24 LEU HD1 H -0.45 0.01 2 155 . 24 LEU HD2 H -0.53 0.01 2 156 . 24 LEU N N 126.32 0.02 1 157 . 25 ILE H H 8.37 0.01 1 158 . 25 ILE HA H 4.18 0.01 1 159 . 25 ILE HB H 1.21 0.01 1 160 . 25 ILE HG12 H 1.09 0.01 1 161 . 25 ILE HG13 H 0.53 0.01 1 162 . 25 ILE HG2 H 0.61 0.01 1 163 . 25 ILE HD1 H -0.17 0.01 1 164 . 25 ILE N N 130.80 0.02 1 165 . 26 ARG H H 7.77 0.01 1 166 . 26 ARG HA H 4.84 0.01 1 167 . 26 ARG HB2 H 1.45 0.01 2 168 . 26 ARG HB3 H 1.26 0.01 2 169 . 26 ARG HG2 H 1.18 0.01 2 170 . 26 ARG HG3 H 0.83 0.01 2 171 . 26 ARG HD2 H 3.20 0.01 2 172 . 26 ARG HD3 H 2.96 0.01 2 173 . 26 ARG HE H 7.40 0.01 1 174 . 26 ARG N N 125.79 0.02 1 175 . 27 CYS H H 8.74 0.01 1 176 . 27 CYS HA H 4.24 0.01 1 177 . 27 CYS HB2 H 3.40 0.01 2 178 . 27 CYS HB3 H 2.70 0.01 2 179 . 27 CYS N N 123.68 0.02 1 180 . 28 ILE H H 9.52 0.01 1 181 . 28 ILE HA H 4.10 0.01 1 182 . 28 ILE HB H 2.06 0.01 1 183 . 28 ILE HG12 H 1.45 0.01 1 184 . 28 ILE HG13 H 1.30 0.01 1 185 . 28 ILE HG2 H 1.01 0.01 1 186 . 28 ILE HD1 H 0.89 0.01 1 187 . 28 ILE N N 132.38 0.02 1 188 . 29 ASN H H 8.89 0.01 1 189 . 29 ASN HA H 4.93 0.01 1 190 . 29 ASN HB2 H 3.42 0.01 2 191 . 29 ASN HB3 H 2.85 0.01 2 192 . 29 ASN HD21 H 8.32 0.01 2 193 . 29 ASN HD22 H 7.09 0.01 2 194 . 29 ASN N N 123.16 0.02 1 195 . 29 ASN ND2 N 115.51 0.02 1 196 . 30 CYS H H 8.01 0.01 1 197 . 30 CYS HA H 4.88 0.01 1 198 . 30 CYS HB2 H 3.23 0.01 2 199 . 30 CYS HB3 H 2.53 0.01 2 200 . 30 CYS N N 118.15 0.02 1 201 . 31 GLN H H 7.79 0.01 1 202 . 31 GLN HA H 4.09 0.01 1 203 . 31 GLN HB2 H 2.25 0.01 2 204 . 31 GLN HB3 H 2.16 0.01 2 205 . 31 GLN HG2 H 2.45 0.01 2 206 . 31 GLN HG3 H 2.36 0.01 2 207 . 31 GLN HE21 H 7.24 0.01 2 208 . 31 GLN HE22 H 6.55 0.01 2 209 . 31 GLN N N 116.04 0.02 1 210 . 31 GLN NE2 N 113.67 0.02 1 211 . 32 LYS H H 8.36 0.01 1 212 . 32 LYS HA H 4.55 0.01 1 213 . 32 LYS HB2 H 1.98 0.01 1 214 . 32 LYS HB3 H 1.98 0.01 1 215 . 32 LYS HG2 H 1.60 0.01 2 216 . 32 LYS HG3 H 1.53 0.01 2 217 . 32 LYS HD2 H 1.82 0.01 2 218 . 32 LYS HD3 H 1.75 0.01 2 219 . 32 LYS HE2 H 3.04 0.01 1 220 . 32 LYS HE3 H 3.04 0.01 1 221 . 32 LYS N N 123.91 0.02 1 222 . 33 PRO HA H 4.41 0.01 1 223 . 33 PRO HB2 H 2.12 0.01 2 224 . 33 PRO HB3 H 1.96 0.01 2 225 . 33 PRO HG2 H 2.19 0.01 2 226 . 33 PRO HG3 H 1.79 0.01 2 227 . 33 PRO HD2 H 3.97 0.01 2 228 . 33 PRO HD3 H 3.60 0.01 2 229 . 34 LEU H H 9.41 0.01 1 230 . 34 LEU HA H 4.54 0.01 1 231 . 34 LEU HB2 H 1.96 0.01 2 232 . 34 LEU HB3 H 1.42 0.01 2 233 . 34 LEU HG H 1.62 0.01 1 234 . 34 LEU HD1 H 0.68 0.01 2 235 . 34 LEU HD2 H 0.62 0.01 2 236 . 34 LEU N N 127.37 0.02 1 237 . 35 SER H H 9.75 0.01 1 238 . 35 SER HA H 4.77 0.01 1 239 . 35 SER HB2 H 3.98 0.01 1 240 . 35 SER HB3 H 3.98 0.01 1 241 . 35 SER HG H 6.00 0.01 1 242 . 35 SER N N 122.36 0.02 1 243 . 36 PRO HA H 4.14 0.01 1 244 . 36 PRO HB2 H 2.38 0.01 2 245 . 36 PRO HB3 H 1.93 0.01 2 246 . 36 PRO HG2 H 2.23 0.01 2 247 . 36 PRO HG3 H 2.04 0.01 2 248 . 36 PRO HD2 H 3.97 0.01 2 249 . 36 PRO HD3 H 3.84 0.01 2 250 . 37 GLU H H 8.89 0.01 1 251 . 37 GLU HA H 4.09 0.01 1 252 . 37 GLU HB2 H 2.16 0.01 2 253 . 37 GLU HB3 H 1.89 0.01 2 254 . 37 GLU HG2 H 2.38 0.01 2 255 . 37 GLU HG3 H 2.28 0.01 2 256 . 37 GLU N N 118.94 0.02 1 257 . 38 GLU H H 8.04 0.01 1 258 . 38 GLU HA H 4.00 0.01 1 259 . 38 GLU HB2 H 2.53 0.01 1 260 . 38 GLU HB3 H 2.53 0.01 1 261 . 38 GLU HG2 H 2.40 0.01 1 262 . 38 GLU HG3 H 2.40 0.01 1 263 . 38 GLU N N 122.63 0.02 1 264 . 39 LYS H H 8.36 0.01 1 265 . 39 LYS HA H 3.98 0.01 1 266 . 39 LYS HB2 H 1.98 0.01 2 267 . 39 LYS HB3 H 1.60 0.01 2 268 . 39 LYS HG2 H 1.01 0.01 1 269 . 39 LYS HG3 H 1.01 0.01 1 270 . 39 LYS HD2 H 1.75 0.01 1 271 . 39 LYS HD3 H 1.75 0.01 1 272 . 39 LYS HE2 H 2.74 0.01 2 273 . 39 LYS HE3 H 2.49 0.01 2 274 . 39 LYS N N 121.31 0.02 1 275 . 40 GLN H H 8.39 0.01 1 276 . 40 GLN HA H 3.86 0.01 1 277 . 40 GLN HB2 H 2.43 0.01 1 278 . 40 GLN HB3 H 2.43 0.01 1 279 . 40 GLN HG2 H 2.10 0.01 1 280 . 40 GLN HG3 H 2.10 0.01 1 281 . 40 GLN HE21 H 8.09 0.01 2 282 . 40 GLN HE22 H 6.96 0.01 2 283 . 40 GLN N N 119.73 0.02 1 284 . 40 GLN NE2 N 117.62 0.02 1 285 . 41 ARG H H 8.02 0.01 1 286 . 41 ARG HA H 4.19 0.01 1 287 . 41 ARG HB2 H 1.99 0.01 1 288 . 41 ARG HB3 H 1.99 0.01 1 289 . 41 ARG HG2 H 1.73 0.01 1 290 . 41 ARG HG3 H 1.73 0.01 1 291 . 41 ARG HD2 H 3.16 0.01 1 292 . 41 ARG HD3 H 3.16 0.01 1 293 . 41 ARG N N 121.05 0.02 1 294 . 42 HIS H H 7.60 0.01 1 295 . 42 HIS HA H 4.07 0.01 1 296 . 42 HIS HB2 H 3.52 0.01 2 297 . 42 HIS HB3 H 2.69 0.01 2 298 . 42 HIS HD2 H 6.54 0.01 1 299 . 42 HIS HE1 H 7.56 0.01 1 300 . 42 HIS N N 117.89 0.02 1 301 . 43 LEU H H 7.51 0.01 1 302 . 43 LEU HA H 4.32 0.01 1 303 . 43 LEU HB2 H 2.09 0.01 2 304 . 43 LEU HB3 H 1.79 0.01 2 305 . 43 LEU HG H 1.64 0.01 1 306 . 43 LEU HD1 H 0.94 0.01 1 307 . 43 LEU HD2 H 0.94 0.01 1 308 . 43 LEU N N 118.41 0.02 1 309 . 44 ASP H H 9.03 0.01 1 310 . 44 ASP HA H 4.29 0.01 1 311 . 44 ASP HB2 H 2.71 0.01 1 312 . 44 ASP HB3 H 2.71 0.01 1 313 . 44 ASP N N 122.36 0.02 1 314 . 45 LYS H H 8.25 0.01 1 315 . 45 LYS HA H 4.31 0.01 1 316 . 45 LYS HB2 H 2.00 0.01 1 317 . 45 LYS HB3 H 2.00 0.01 1 318 . 45 LYS HG2 H 1.65 0.01 1 319 . 45 LYS HG3 H 1.65 0.01 1 320 . 45 LYS HD2 H 1.51 0.01 1 321 . 45 LYS HD3 H 1.51 0.01 1 322 . 45 LYS N N 116.57 0.02 1 323 . 46 LYS H H 7.75 0.01 1 324 . 46 LYS HA H 4.20 0.01 1 325 . 46 LYS HB2 H 2.09 0.01 2 326 . 46 LYS HB3 H 1.82 0.01 2 327 . 46 LYS HG2 H 1.30 0.01 2 328 . 46 LYS HG3 H 1.22 0.01 2 329 . 46 LYS HD2 H 1.59 0.01 2 330 . 46 LYS HD3 H 1.52 0.01 2 331 . 46 LYS N N 118.94 0.02 1 332 . 47 GLN H H 7.92 0.01 1 333 . 47 GLN HA H 4.21 0.01 1 334 . 47 GLN HG2 H 2.13 0.01 2 335 . 47 GLN HG3 H 1.87 0.01 2 336 . 47 GLN HE21 H 6.98 0.01 2 337 . 47 GLN HE22 H 6.63 0.01 2 338 . 47 GLN N N 125.79 0.02 1 339 . 47 GLN NE2 N 110.51 0.02 1 340 . 48 ARG H H 8.80 0.01 1 341 . 48 ARG HA H 4.13 0.01 1 342 . 48 ARG HB2 H 2.41 0.01 2 343 . 48 ARG HB3 H 2.20 0.01 2 344 . 48 ARG HG2 H 1.50 0.01 1 345 . 48 ARG HG3 H 1.50 0.01 1 346 . 48 ARG HD2 H 2.19 0.01 2 347 . 48 ARG HD3 H 2.06 0.01 2 348 . 48 ARG HE H 3.79 0.01 1 349 . 48 ARG N N 125.53 0.02 1 350 . 49 PHE H H 8.55 0.01 1 351 . 49 PHE HA H 4.92 0.01 1 352 . 49 PHE HB2 H 3.28 0.01 2 353 . 49 PHE HB3 H 2.63 0.01 2 354 . 49 PHE HD1 H 6.95 0.01 1 355 . 49 PHE HD2 H 6.95 0.01 1 356 . 49 PHE HE1 H 6.56 0.01 1 357 . 49 PHE HE2 H 6.56 0.01 1 358 . 49 PHE HZ H 6.54 0.01 4 359 . 49 PHE N N 118.68 0.02 1 360 . 50 HIS H H 8.81 0.01 1 361 . 50 HIS HA H 5.29 0.01 1 362 . 50 HIS HB2 H 2.79 0.01 1 363 . 50 HIS HB3 H 2.79 0.01 1 364 . 50 HIS N N 119.20 0.02 1 365 . 51 ASN H H 9.18 0.01 1 366 . 51 ASN HA H 4.32 0.01 1 367 . 51 ASN HB2 H 1.80 0.01 2 368 . 51 ASN HB3 H -0.25 0.01 2 369 . 51 ASN HD21 H 5.75 0.01 2 370 . 51 ASN HD22 H 3.85 0.01 2 371 . 51 ASN N N 130.27 0.02 1 372 . 51 ASN ND2 N 107.35 0.02 1 373 . 52 ILE H H 8.53 0.01 1 374 . 52 ILE HA H 4.22 0.01 1 375 . 52 ILE HB H 1.69 0.01 1 376 . 52 ILE HG12 H 1.32 0.01 1 377 . 52 ILE HG13 H 1.09 0.01 1 378 . 52 ILE HG2 H 0.80 0.01 1 379 . 52 ILE HD1 H 0.74 0.01 1 380 . 52 ILE N N 128.42 0.02 1 381 . 53 ARG H H 9.45 0.01 1 382 . 53 ARG HA H 3.77 0.01 1 383 . 53 ARG HB2 H 1.73 0.01 2 384 . 53 ARG HB3 H 1.54 0.01 2 385 . 53 ARG HG2 H 1.96 0.01 1 386 . 53 ARG HG3 H 1.96 0.01 1 387 . 53 ARG HD2 H 3.21 0.01 2 388 . 53 ARG HD3 H 3.11 0.01 2 389 . 53 ARG N N 127.37 0.02 1 390 . 54 GLY H H 7.91 0.01 1 391 . 54 GLY HA2 H 4.08 0.01 2 392 . 54 GLY HA3 H 3.58 0.01 2 393 . 54 GLY N N 104.45 0.02 1 394 . 55 ARG H H 7.37 0.01 1 395 . 55 ARG HA H 4.55 0.01 1 396 . 55 ARG HB2 H 1.78 0.01 2 397 . 55 ARG HB3 H 1.66 0.01 2 398 . 55 ARG HG2 H 1.50 0.01 1 399 . 55 ARG HG3 H 1.50 0.01 1 400 . 55 ARG HD2 H 3.11 0.01 1 401 . 55 ARG HD3 H 3.11 0.01 1 402 . 55 ARG N N 120.52 0.02 1 403 . 56 TRP H H 8.82 0.01 1 404 . 56 TRP HA H 4.59 0.01 1 405 . 56 TRP HB2 H 3.01 0.01 2 406 . 56 TRP HB3 H 2.78 0.01 2 407 . 56 TRP HD1 H 7.27 0.01 1 408 . 56 TRP HE1 H 10.18 0.01 1 409 . 56 TRP HE3 H 7.17 0.01 1 410 . 56 TRP HZ2 H 7.54 0.01 1 411 . 56 TRP HZ3 H 6.90 0.01 1 412 . 56 TRP HH2 H 6.77 0.01 1 413 . 56 TRP N N 123.42 0.02 1 414 . 56 TRP NE1 N 123.26 0.02 1 415 . 57 THR H H 9.05 0.01 1 416 . 57 THR HA H 5.87 0.01 1 417 . 57 THR HB H 4.31 0.01 1 418 . 57 THR HG2 H 1.17 0.01 1 419 . 57 THR N N 115.78 0.02 1 420 . 58 GLY H H 7.96 0.01 1 421 . 58 GLY HA2 H 4.94 0.01 2 422 . 58 GLY HA3 H 3.62 0.01 2 423 . 58 GLY N N 109.72 0.02 1 424 . 59 ARG H H 10.55 0.01 1 425 . 59 ARG HA H 5.73 0.01 1 426 . 59 ARG HB2 H 1.68 0.01 1 427 . 59 ARG HB3 H 1.68 0.01 1 428 . 59 ARG HG2 H 1.72 0.01 1 429 . 59 ARG HG3 H 1.72 0.01 1 430 . 59 ARG HD2 H 3.09 0.01 1 431 . 59 ARG HD3 H 3.09 0.01 1 432 . 59 ARG HE H 7.55 0.01 1 433 . 59 ARG N N 129.22 0.02 1 434 . 60 CYS H H 9.54 0.01 1 435 . 60 CYS HA H 4.42 0.01 1 436 . 60 CYS HB2 H 3.89 0.01 2 437 . 60 CYS HB3 H 2.58 0.01 2 438 . 60 CYS N N 129.48 0.02 1 439 . 61 MET H H 9.78 0.01 1 440 . 61 MET HA H 4.09 0.01 1 441 . 61 MET HB2 H 2.26 0.01 2 442 . 61 MET HB3 H 2.16 0.01 2 443 . 61 MET HG2 H 2.79 0.01 2 444 . 61 MET HG3 H 2.71 0.01 2 445 . 61 MET HE H 2.40 0.01 1 446 . 61 MET N N 121.05 0.02 1 447 . 62 SER H H 8.63 0.01 1 448 . 62 SER HA H 4.22 0.01 1 449 . 62 SER HB2 H 4.02 0.01 1 450 . 62 SER HB3 H 4.02 0.01 1 451 . 62 SER N N 118.15 0.02 1 452 . 63 CYS H H 8.80 0.01 1 453 . 63 CYS HA H 4.13 0.01 1 454 . 63 CYS HB2 H 3.06 0.01 2 455 . 63 CYS HB3 H 2.83 0.01 2 456 . 63 CYS N N 124.47 0.02 1 457 . 64 SER H H 7.99 0.01 1 458 . 64 SER HA H 4.29 0.01 1 459 . 64 SER HB2 H 3.96 0.01 2 460 . 64 SER HB3 H 3.85 0.01 2 461 . 64 SER N N 116.57 0.02 1 462 . 65 ARG H H 7.64 0.01 1 463 . 65 ARG HA H 4.26 0.01 1 464 . 65 ARG HB2 H 1.84 0.01 2 465 . 65 ARG HB3 H 1.90 0.01 2 466 . 65 ARG HG2 H 1.74 0.01 2 467 . 65 ARG HG3 H 1.63 0.01 2 468 . 65 ARG N N 121.84 0.02 1 469 . 66 SER H H 7.94 0.01 1 470 . 66 SER HA H 4.31 0.01 1 471 . 66 SER HB2 H 3.95 0.01 2 472 . 66 SER HB3 H 3.84 0.01 2 473 . 66 SER N N 116.83 0.02 1 474 . 67 SER H H 7.93 0.01 1 475 . 67 SER HA H 4.56 0.01 1 476 . 67 SER HB2 H 4.02 0.01 1 477 . 67 SER HB3 H 4.02 0.01 1 478 . 67 SER N N 118.53 0.02 1 479 . 68 ARG H H 8.33 0.01 1 480 . 68 ARG HA H 4.37 0.01 1 481 . 68 ARG HB2 H 1.85 0.01 2 482 . 68 ARG HB3 H 1.74 0.01 2 483 . 68 ARG HG2 H 1.76 0.01 2 484 . 68 ARG HG3 H 1.60 0.01 2 485 . 68 ARG HD2 H 3.15 0.01 1 486 . 68 ARG HD3 H 3.15 0.01 1 487 . 68 ARG N N 124.47 0.02 1 488 . 69 THR H H 8.13 0.01 1 489 . 69 THR HA H 4.27 0.01 1 490 . 69 THR HB H 4.15 0.01 1 491 . 69 THR HG2 H 1.21 0.01 1 492 . 69 THR N N 115.78 0.02 1 493 . 70 ARG H H 8.33 0.01 1 494 . 70 ARG HA H 4.29 0.01 1 495 . 70 ARG HB2 H 2.10 0.01 2 496 . 70 ARG HB3 H 1.97 0.01 2 497 . 70 ARG HG2 H 2.42 0.01 2 498 . 70 ARG HG3 H 2.23 0.01 2 499 . 71 ARG H H 8.44 0.01 1 500 . 71 ARG HA H 4.26 0.01 1 501 . 71 ARG HB2 H 1.80 0.01 2 502 . 71 ARG HB3 H 1.72 0.01 2 503 . 71 ARG HG2 H 1.59 0.01 1 504 . 71 ARG HG3 H 1.59 0.01 1 505 . 71 ARG HD2 H 3.15 0.01 1 506 . 71 ARG HD3 H 3.15 0.01 1 507 . 71 ARG N N 123.42 0.02 1 508 . 72 GLU H H 8.59 0.01 1 509 . 72 GLU HA H 4.27 0.01 1 510 . 72 GLU HB2 H 2.03 0.01 2 511 . 72 GLU HB3 H 1.92 0.01 2 512 . 72 GLU HG2 H 2.28 0.01 1 513 . 72 GLU HG3 H 2.28 0.01 1 514 . 72 GLU N N 122.89 0.02 1 515 . 73 THR H H 8.14 0.01 1 516 . 73 THR HA H 4.29 0.01 1 517 . 73 THR HB H 4.16 0.01 1 518 . 73 THR HG2 H 1.15 0.01 1 519 . 73 THR N N 115.51 0.02 1 520 . 74 GLN H H 8.38 0.01 1 521 . 74 GLN HA H 4.30 0.01 1 522 . 74 GLN HB2 H 2.08 0.01 2 523 . 74 GLN HB3 H 1.95 0.01 2 524 . 74 GLN HG2 H 2.31 0.01 1 525 . 74 GLN HG3 H 2.31 0.01 1 526 . 74 GLN HE21 H 6.88 0.01 2 527 . 74 GLN HE22 H 7.66 0.01 2 528 . 74 GLN N N 124.47 0.02 1 529 . 74 GLN NE2 N 113.93 0.02 1 530 . 75 LEU H H 8.02 0.01 1 531 . 75 LEU HA H 4.12 0.01 1 532 . 75 LEU HB2 H 1.56 0.01 1 533 . 75 LEU HB3 H 1.56 0.01 1 534 . 75 LEU HG H 0.84 0.01 1 535 . 75 LEU HD1 H 0.79 0.01 1 536 . 75 LEU HD2 H 0.79 0.01 1 537 . 75 LEU N N 130.80 0.02 1 stop_ save_