data_4559 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; The NMR structure of the nucleocapsid protein from the mouse mammary tumor virus reveals unusual folding of the C-terminal zinc knuckle ; _BMRB_accession_number 4559 _BMRB_flat_file_name bmr4559.str _Entry_type original _Submission_date 1999-12-13 _Accession_date 1999-12-14 _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 Klein Daniel J . 2 Johnson Philip E . 3 Zollars Eric S . 4 'De Guzman' Roberto N . 5 Summers Michael F . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 230 "15N chemical shifts" 42 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2000-10-06 original author . stop_ _Original_release_date 2000-10-06 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; The NMR structure of the nucleocapsid protein from the mouse mammary tumor virus reveals unusual folding of the C-terminal zinc knuckle ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code 20143476 _PubMed_ID 10677209 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Klein Daniel J . 2 Johnson Philip E . 3 Zollars Eric S . 4 'De Guzman' Roberto N . 5 Summers Michael F . stop_ _Journal_abbreviation Biochemistry _Journal_volume 39 _Journal_issue . _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 1604 _Page_last 1612 _Year 2000 _Details . save_ ################################## # Molecular system description # ################################## save_system_MMTV_NC _Saveframe_category molecular_system _Mol_system_name 'mouse mammary tumor virus nucleocapsid protein' _Abbreviation_common 'MMTV NC' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'mmtv nc' $mmtv_nc 'zinc ion 1' $ZN 'zinc ion 2' $ZN stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state monomer _System_paramagnetic no _System_thiol_state 'all other bound' _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_mmtv_nc _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'mouse mammary tumor virus nucleocapsid protein' _Abbreviation_common 'mmtv nc' _Molecular_mass . _Mol_thiol_state 'all other bound' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 60 _Mol_residue_sequence ; PVCFSCGKTGHIKRDCKEEK GSKRAPPGLCPRCKKGYHWK SECKSKFDKDGNPLPPLETN ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 29 PRO 2 30 VAL 3 31 CYS 4 32 PHE 5 33 SER 6 34 CYS 7 35 GLY 8 36 LYS 9 37 THR 10 38 GLY 11 39 HIS 12 40 ILE 13 41 LYS 14 42 ARG 15 43 ASP 16 44 CYS 17 45 LYS 18 46 GLU 19 47 GLU 20 48 LYS 21 49 GLY 22 50 SER 23 51 LYS 24 52 ARG 25 53 ALA 26 54 PRO 27 55 PRO 28 56 GLY 29 57 LEU 30 58 CYS 31 59 PRO 32 60 ARG 33 61 CYS 34 62 LYS 35 63 LYS 36 64 GLY 37 65 TYR 38 66 HIS 39 67 TRP 40 68 LYS 41 69 SER 42 70 GLU 43 71 CYS 44 72 LYS 45 73 SER 46 74 LYS 47 75 PHE 48 76 ASP 49 77 LYS 50 78 ASP 51 79 GLY 52 80 ASN 53 81 PRO 54 82 LEU 55 83 PRO 56 84 PRO 57 85 LEU 58 86 GLU 59 87 THR 60 88 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 1DSV "Structure Of The Mmtv Nucleocapsid Protein (C-Terminal Zinc Finger)" 51.67 31 100.00 100.00 1.40e-12 DBJ BAA03765 "gag pro pol polyprotein [Mouse mammary tumor virus]" 100.00 591 98.33 100.00 8.96e-34 GB AAA66623 "gag protein, partial [Mouse mammary tumor virus]" 100.00 233 100.00 100.00 1.98e-35 GB AAF31472 "Gag [Exogenous mouse mammary tumor virus]" 100.00 591 100.00 100.00 2.22e-34 GB AAF31473 "Gag-Pro [Exogenous mouse mammary tumor virus]" 100.00 860 100.00 100.00 1.54e-33 GB AAF31474 "Gag-Pro-Pol [Exogenous mouse mammary tumor virus]" 100.00 1755 100.00 100.00 8.28e-36 SP P11283 "RecName: Full=Gag-Pro-Pol polyprotein; Contains: RecName: Full=Matrix protein p10; Contains: RecName: Full=Phosphorylated prote" 100.00 1755 100.00 100.00 8.28e-36 SP P11284 "RecName: Full=Gag polyprotein; Contains: RecName: Full=Matrix protein p10; Contains: RecName: Full=Phosphorylated protein pp21;" 100.00 591 100.00 100.00 2.27e-34 SP Q9IZT2 "RecName: Full=Gag-Pro polyprotein; Contains: RecName: Full=Matrix protein p10; Contains: RecName: Full=Phosphorylated protein p" 100.00 860 100.00 100.00 1.54e-33 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 9 15:19:31 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 $mmtv_nc 'Mammalian type B retroviruses' 11633 . . 'Mammalian type B retroviruses' . 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 $mmtv_nc 'recombinant technology' . . . . . 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 $mmtv_nc . mM [U-15N] acetate 25 mM [U-2H] NaCl 25 mM . ZnCl2 0.1 M . BME 0.1 mM . stop_ save_ save_sample_2 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $mmtv_nc . mM . acetate 25 mM [U-2H] NaCl 25 mM . ZnCl2 0.1 M . BME 0.1 mM . stop_ save_ ############################ # Computer software used # ############################ save_DYANA _Saveframe_category software _Name DYANA _Version . loop_ _Task 'structure calculation' stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer1 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model DMX _Field_strength 600 _Details . save_ save_NMR_spectrometer2 _Saveframe_category NMR_spectrometer _Manufacturer GE _Model 'Omega PSG' _Field_strength 600 _Details . save_ ############################# # NMR applied experiments # ############################# save_2D_NOESY_(50_and_200_ms)_1 _Saveframe_category NMR_applied_experiment _Experiment_name '2D NOESY (50 and 200 ms)' _Sample_label . save_ save_15N-edited_NOESY-HSQC_(m_=_200_ms)_2 _Saveframe_category NMR_applied_experiment _Experiment_name '15N-edited NOESY-HSQC (m = 200 ms)' _Sample_label . save_ save_15N,15N-edited_HMQC-NOESY-HSQC_(m_=_120_ms)_3 _Saveframe_category NMR_applied_experiment _Experiment_name '15N,15N-edited HMQC-NOESY-HSQC (m = 120 ms)' _Sample_label . save_ save_15N-edited_TOCSY_70_ms_clean-MLEV-17_mixing_period_4 _Saveframe_category NMR_applied_experiment _Experiment_name '15N-edited TOCSY 70 ms clean-MLEV-17 mixing period' _Sample_label . save_ save_HNHA_5 _Saveframe_category NMR_applied_experiment _Experiment_name HNHA _Sample_label . save_ save_HNHB_6 _Saveframe_category NMR_applied_experiment _Experiment_name HNHB _Sample_label . save_ save_15N_T1_7 _Saveframe_category NMR_applied_experiment _Experiment_name '15N T1' _Sample_label . save_ save_15N_T2_8 _Saveframe_category NMR_applied_experiment _Experiment_name '15N T2' _Sample_label . save_ save_15N-{1H}_NOE_9 _Saveframe_category NMR_applied_experiment _Experiment_name '15N-{1H} NOE' _Sample_label . save_ save_NMR_spec_expt__0_1 _Saveframe_category NMR_applied_experiment _Experiment_name '2D NOESY (50 and 200 ms)' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_2 _Saveframe_category NMR_applied_experiment _Experiment_name '15N-edited NOESY-HSQC (m = 200 ms)' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_3 _Saveframe_category NMR_applied_experiment _Experiment_name '15N,15N-edited HMQC-NOESY-HSQC (m = 120 ms)' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_4 _Saveframe_category NMR_applied_experiment _Experiment_name '15N-edited TOCSY 70 ms clean-MLEV-17 mixing period' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_5 _Saveframe_category NMR_applied_experiment _Experiment_name HNHA _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_6 _Saveframe_category NMR_applied_experiment _Experiment_name HNHB _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_7 _Saveframe_category NMR_applied_experiment _Experiment_name '15N T1' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_8 _Saveframe_category NMR_applied_experiment _Experiment_name '15N T2' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_9 _Saveframe_category NMR_applied_experiment _Experiment_name '15N-{1H} NOE' _BMRB_pulse_sequence_accession_number . _Details . save_ ####################### # Sample conditions # ####################### save_sample_cond_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 7.0 . n/a temperature 298 . 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 DSS H 1 'methyl protons' ppm 0.0 internal direct . . . . $entry_citation $entry_citation DSS N 15 'methyl protons' ppm 0.0 . indirect . . . 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_chemical_shift_set _Saveframe_category assigned_chemical_shifts _Details . loop_ _Sample_label $sample_1 $sample_2 stop_ _Sample_conditions_label $sample_cond_1 _Chem_shift_reference_set_label $chemical_shift_reference _Mol_system_component_name 'mmtv nc' _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 PRO HA H 4.35 . . 2 . 1 PRO HB2 H 2.11 . . 3 . 1 PRO HB3 H 2.11 . . 4 . 1 PRO HG2 H 1.56 . . 5 . 1 PRO HG3 H 1.56 . . 6 . 1 PRO HD2 H 3.47 . . 7 . 1 PRO HD3 H 3.47 . . 8 . 2 VAL N N 119.7 . . 9 . 2 VAL H H 7.93 . . 10 . 2 VAL HA H 4.12 . . 11 . 2 VAL HB H 1.67 . . 12 . 2 VAL HG1 H 0.75 . . 13 . 2 VAL HG2 H 0.62 . . 14 . 3 CYS N N 129.4 . . 15 . 3 CYS H H 8.29 . . 16 . 3 CYS HA H 4.09 . . 17 . 3 CYS HB2 H 1.77 . . 18 . 3 CYS HB3 H 2.82 . . 19 . 4 PHE N N 128.7 . . 20 . 4 PHE H H 8.51 . . 21 . 4 PHE HA H 4.58 . . 22 . 4 PHE HB2 H 3.34 . . 23 . 4 PHE HB3 H 3.05 . . 24 . 4 PHE HD1 H 7.31 . . 25 . 4 PHE HD2 H 7.31 . . 26 . 4 PHE HE1 H 7.03 . . 27 . 4 PHE HE2 H 7.03 . . 28 . 5 SER N N 117.5 . . 29 . 5 SER H H 9.49 . . 30 . 5 SER HA H 4.58 . . 31 . 5 SER HB2 H 4.15 . . 32 . 5 SER HB3 H 3.86 . . 33 . 6 CYS N N 119.0 . . 34 . 6 CYS H H 8.81 . . 35 . 6 CYS HA H 4.95 . . 36 . 6 CYS HB2 H 3.24 . . 37 . 6 CYS HB3 H 2.60 . . 38 . 7 GLY N N 113.2 . . 39 . 7 GLY H H 7.98 . . 40 . 7 GLY HA2 H 3.78 . . 41 . 7 GLY HA3 H 4.09 . . 42 . 8 LYS N N 121.4 . . 43 . 8 LYS H H 8.31 . . 44 . 8 LYS HA H 4.47 . . 45 . 8 LYS HB2 H 1.95 . . 46 . 8 LYS HB3 H 1.85 . . 47 . 8 LYS HG2 H 1.63 . . 48 . 8 LYS HG3 H 1.63 . . 49 . 8 LYS HD2 H 1.45 . . 50 . 8 LYS HD3 H 1.45 . . 51 . 8 LYS HE2 H 3.01 . . 52 . 8 LYS HE3 H 3.01 . . 53 . 9 THR N N 110.9 . . 54 . 9 THR H H 8.09 . . 55 . 9 THR HA H 4.59 . . 56 . 9 THR HB H 4.09 . . 57 . 9 THR HG2 H 1.113 . . 58 . 10 GLY N N 108.5 . . 59 . 10 GLY H H 8.79 . . 60 . 10 GLY HA2 H 4.57 . . 61 . 10 GLY HA3 H 3.64 . . 62 . 11 HIS N N 114.1 . . 63 . 11 HIS H H 7.23 . . 64 . 11 HIS HA H 4.74 . . 65 . 11 HIS HB2 H 3.21 . . 66 . 11 HIS HB3 H 3.21 . . 67 . 12 ILE N N 109.3 . . 68 . 12 ILE H H 8.07 . . 69 . 12 ILE HA H 4.78 . . 70 . 12 ILE HB H 2.12 . . 71 . 12 ILE HG2 H 0.89 . . 72 . 12 ILE HD1 H 1.25 . . 73 . 13 LYS N N 122.8 . . 74 . 13 LYS H H 8.72 . . 75 . 13 LYS HA H 4.75 . . 76 . 13 LYS HB2 H 1.97 . . 77 . 13 LYS HB3 H 1.54 . . 78 . 14 ARG N N 118.6 . . 79 . 14 ARG H H 8.20 . . 80 . 14 ARG HA H 4.09 . . 81 . 14 ARG HB2 H 1.61 . . 82 . 14 ARG HB3 H 1.95 . . 83 . 14 ARG HG2 H 1.26 . . 84 . 14 ARG HG3 H 1.26 . . 85 . 15 ASP N N 116.1 . . 86 . 15 ASP H H 7.89 . . 87 . 15 ASP HA H 4.85 . . 88 . 15 ASP HB2 H 2.98 . . 89 . 15 ASP HB3 H 2.57 . . 90 . 16 CYS N N 124.3 . . 91 . 16 CYS H H 7.74 . . 92 . 16 CYS HA H 3.65 . . 93 . 16 CYS HB2 H 3.35 . . 94 . 16 CYS HB3 H 2.99 . . 95 . 17 LYS N N 128.7 . . 96 . 17 LYS H H 8.65 . . 97 . 17 LYS HA H 4.46 . . 98 . 17 LYS HB2 H 1.96 . . 99 . 17 LYS HB3 H 1.96 . . 100 . 17 LYS HG2 H 1.63 . . 101 . 17 LYS HG3 H 1.63 . . 102 . 17 LYS HD2 H 1.39 . . 103 . 17 LYS HD3 H 1.39 . . 104 . 17 LYS HE2 H 3.02 . . 105 . 17 LYS HE3 H 3.02 . . 106 . 18 GLU N N 122.9 . . 107 . 18 GLU H H 8.57 . . 108 . 18 GLU HA H 4.20 . . 109 . 18 GLU HB2 H 2.07 . . 110 . 18 GLU HB3 H 1.92 . . 111 . 18 GLU HG2 H 2.39 . . 112 . 18 GLU HG3 H 2.25 . . 113 . 19 GLU N N 122.5 . . 114 . 19 GLU H H 8.30 . . 115 . 19 GLU HA H 4.19 . . 116 . 19 GLU HB2 H 2.05 . . 117 . 19 GLU HB3 H 1.94 . . 118 . 19 GLU HG2 H 2.40 . . 119 . 19 GLU HG3 H 2.40 . . 120 . 28 GLY N N 106.9 . . 121 . 28 GLY H H 7.35 . . 122 . 28 GLY HA2 H 4.10 . . 123 . 28 GLY HA3 H 3.63 . . 124 . 29 LEU N N 120.2 . . 125 . 29 LEU H H 7.96 . . 126 . 29 LEU HA H 3.10 . . 127 . 29 LEU HB2 H 1.20 . . 128 . 29 LEU HB3 H 1.02 . . 129 . 29 LEU HG H 0.45 . . 130 . 29 LEU HD1 H 0.23 . . 131 . 29 LEU HD2 H 0.23 . . 132 . 30 CYS N N 106.6 . . 133 . 30 CYS H H 8.21 . . 134 . 30 CYS HA H 4.54 . . 135 . 30 CYS HB2 H 2.62 . . 136 . 30 CYS HB3 H 1.90 . . 137 . 31 PRO HA H 4.58 . . 138 . 32 ARG N N 124.0 . . 139 . 32 ARG H H 9.25 . . 140 . 32 ARG HA H 4.36 . . 141 . 32 ARG HB2 H 2.17 . . 142 . 32 ARG HB3 H 1.64 . . 143 . 32 ARG HG2 H 1.47 . . 144 . 32 ARG HG3 H 1.47 . . 145 . 32 ARG HD2 H 3.19 . . 146 . 32 ARG HD3 H 3.19 . . 147 . 33 CYS N N 116.6 . . 148 . 33 CYS H H 8.85 . . 149 . 33 CYS HA H 4.83 . . 150 . 33 CYS HB2 H 3.20 . . 151 . 33 CYS HB3 H 2.64 . . 152 . 34 LYS N N 119.0 . . 153 . 34 LYS H H 7.98 . . 154 . 34 LYS HA H 4.03 . . 155 . 34 LYS HB2 H 2.02 . . 156 . 34 LYS HB3 H 1.89 . . 157 . 34 LYS HG2 H 1.37 . . 158 . 34 LYS HG3 H 1.37 . . 159 . 34 LYS HD2 H 1.24 . . 160 . 34 LYS HD3 H 1.24 . . 161 . 35 LYS N N 116.6 . . 162 . 35 LYS H H 8.68 . . 163 . 35 LYS HA H 4.50 . . 164 . 35 LYS HB2 H 2.01 . . 165 . 35 LYS HB3 H 1.90 . . 166 . 36 GLY N N 128.3 . . 167 . 36 GLY H H 6.81 . . 168 . 36 GLY HA2 H 4.03 . . 169 . 36 GLY HA3 H 3.83 . . 170 . 37 TYR N N 122.5 . . 171 . 37 TYR H H 8.78 . . 172 . 37 TYR HA H 4.29 . . 173 . 37 TYR HB2 H 2.76 . . 174 . 37 TYR HB3 H 2.54 . . 175 . 37 TYR HD1 H 6.91 . . 176 . 37 TYR HD2 H 6.91 . . 177 . 37 TYR HE1 H 6.68 . . 178 . 37 TYR HE2 H 6.68 . . 179 . 38 HIS N N 116.8 . . 180 . 38 HIS H H 6.85 . . 181 . 38 HIS HA H 4.51 . . 182 . 38 HIS HB2 H 3.36 . . 183 . 38 HIS HB3 H 3.36 . . 184 . 39 TRP N N 121.1 . . 185 . 39 TRP H H 8.74 . . 186 . 39 TRP HA H 4.78 . . 187 . 39 TRP HB2 H 3.69 . . 188 . 39 TRP HB3 H 2.95 . . 189 . 39 TRP HD1 H 7.47 . . 190 . 39 TRP HE1 H 10.22 . . 191 . 40 LYS N N 124.8 . . 192 . 40 LYS H H 9.66 . . 193 . 40 LYS HA H 4.63 . . 194 . 40 LYS HB2 H 2.03 . . 195 . 40 LYS HB3 H 1.74 . . 196 . 40 LYS HG2 H 1.60 . . 197 . 40 LYS HG3 H 1.60 . . 198 . 40 LYS HD2 H 1.50 . . 199 . 40 LYS HD3 H 1.50 . . 200 . 41 SER N N 110.2 . . 201 . 41 SER H H 8.17 . . 202 . 41 SER HA H 4.19 . . 203 . 41 SER HB2 H 4.02 . . 204 . 41 SER HB3 H 3.90 . . 205 . 42 GLU N N 120.4 . . 206 . 42 GLU H H 7.94 . . 207 . 42 GLU HA H 4.41 . . 208 . 42 GLU HB2 H 2.22 . . 209 . 42 GLU HB3 H 2.22 . . 210 . 42 GLU HG2 H 2.38 . . 211 . 42 GLU HG3 H 2.38 . . 212 . 43 CYS N N 123.7 . . 213 . 43 CYS H H 7.55 . . 214 . 43 CYS HA H 3.58 . . 215 . 43 CYS HB2 H 3.38 . . 216 . 43 CYS HB3 H 3.04 . . 217 . 44 LYS N N 128.7 . . 218 . 44 LYS H H 8.62 . . 219 . 44 LYS HA H 4.56 . . 220 . 44 LYS HB2 H 2.03 . . 221 . 44 LYS HB3 H 1.54 . . 222 . 45 SER N N 119.3 . . 223 . 45 SER H H 8.36 . . 224 . 45 SER HA H 4.27 . . 225 . 45 SER HB2 H 3.90 . . 226 . 45 SER HB3 H 3.80 . . 227 . 47 PHE N N 116.5 . . 228 . 47 PHE H H 7.69 . . 229 . 47 PHE HA H 5.26 . . 230 . 47 PHE HB2 H 2.84 . . 231 . 47 PHE HB3 H 2.69 . . 232 . 47 PHE HD1 H 7.02 . . 233 . 47 PHE HD2 H 7.02 . . 234 . 47 PHE HE1 H 7.31 . . 235 . 47 PHE HE2 H 7.31 . . 236 . 48 ASP N N 119.3 . . 237 . 48 ASP H H 8.83 . . 238 . 48 ASP HA H 4.88 . . 239 . 48 ASP HB2 H 3.30 . . 240 . 48 ASP HB3 H 2.82 . . 241 . 49 LYS N N 117.4 . . 242 . 49 LYS H H 7.95 . . 243 . 49 LYS HA H 3.97 . . 244 . 49 LYS HB2 H 1.91 . . 245 . 49 LYS HB3 H 1.74 . . 246 . 49 LYS HG2 H 1.37 . . 247 . 49 LYS HG3 H 1.37 . . 248 . 49 LYS HD2 H 2.81 . . 249 . 49 LYS HD3 H 2.81 . . 250 . 50 ASP N N 118.7 . . 251 . 50 ASP H H 7.86 . . 252 . 50 ASP HA H 4.78 . . 253 . 50 ASP HB2 H 2.92 . . 254 . 50 ASP HB3 H 2.53 . . 255 . 51 GLY N N 107.7 . . 256 . 51 GLY H H 8.18 . . 257 . 51 GLY HA2 H 4.21 . . 258 . 51 GLY HA3 H 3.50 . . 259 . 52 ASN N N 121.4 . . 260 . 52 ASN H H 8.78 . . 261 . 52 ASN HA H 5.06 . . 262 . 52 ASN HB2 H 2.63 . . 263 . 52 ASN HB3 H 2.85 . . 264 . 53 PRO HA H 4.37 . . 265 . 54 LEU N N 123.8 . . 266 . 54 LEU H H 7.62 . . 267 . 54 LEU HA H 4.68 . . 268 . 54 LEU HB2 H 1.36 . . 269 . 54 LEU HB3 H 1.23 . . 270 . 54 LEU HG H 1.07 . . 271 . 54 LEU HD1 H 0.86 . . 272 . 54 LEU HD2 H 0.41 . . stop_ save_