data_4344 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; 1H and 15N Chemical Shift Assignments for Apo-CopZ ; _BMRB_accession_number 4344 _BMRB_flat_file_name bmr4344.str _Entry_type original _Submission_date 1999-05-06 _Accession_date 1999-05-06 _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 Wimmer Reinhard . . 2 Herrmann Torsten . . 3 Solioz Marc . . 4 Wuethrich Kurt . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 359 "15N chemical shifts" 74 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 1999-05-25 original author . stop_ _Original_release_date 1999-05-25 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full ; Wimmer, R., Herrmann, T., Solioz, M., and Wuethrich, K., "NMR Structure and Metal Interactions of the CopZ Copper Chaperone," J. Biol. Chem., In press. ; _Citation_title 'NMR Structure and Metal Interactions of the CopZ Copper Chaperone' _Citation_status 'in press' _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 Wimmer Reinhard . . 2 Herrmann Torsten . . 3 Solioz Marc . . 4 Wuethrich Kurt . . stop_ _Journal_abbreviation 'J. Biol. Chem.' _Journal_name_full 'Journal of Biological Chemistry' _Journal_volume . _Journal_issue . _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first . _Page_last . _Year . _Details . loop_ _Keyword 'Copper Chaperone' 'metal binding protein' stop_ save_ ################################## # Molecular system description # ################################## save_apo_CopZ _Saveframe_category molecular_system _Mol_system_name CopZ _Abbreviation_common CopZ _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'apo CopZ monomer' $CopZ_peptide stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state monomer _System_paramagnetic no _System_thiol_state . loop_ _Biological_function 'copper chaperone' stop_ _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_CopZ_peptide _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common CopZ _Abbreviation_common CopZ _Molecular_mass . _Mol_thiol_state . _Details ; expression in E.coli yielded an N-terminus changed from MKQ to AQ No disulfides exist in the molecule. ; ############################## # Polymer residue sequence # ############################## _Residue_count 68 _Mol_residue_sequence ; AQEFSVKGMSCNHCVARIEE AVGRISGVKKVKVQLKKEKA VVKFDEANVQATEICQAINE LGYQAEVI ; loop_ _Residue_seq_code _Residue_label 1 ALA 2 GLN 3 GLU 4 PHE 5 SER 6 VAL 7 LYS 8 GLY 9 MET 10 SER 11 CYS 12 ASN 13 HIS 14 CYS 15 VAL 16 ALA 17 ARG 18 ILE 19 GLU 20 GLU 21 ALA 22 VAL 23 GLY 24 ARG 25 ILE 26 SER 27 GLY 28 VAL 29 LYS 30 LYS 31 VAL 32 LYS 33 VAL 34 GLN 35 LEU 36 LYS 37 LYS 38 GLU 39 LYS 40 ALA 41 VAL 42 VAL 43 LYS 44 PHE 45 ASP 46 GLU 47 ALA 48 ASN 49 VAL 50 GLN 51 ALA 52 THR 53 GLU 54 ILE 55 CYS 56 GLN 57 ALA 58 ILE 59 ASN 60 GLU 61 LEU 62 GLY 63 TYR 64 GLN 65 ALA 66 GLU 67 VAL 68 ILE stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-08-18 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 1CPZ "Copper Chaperone Of Enterococcus Hirae (Apo-Form)" 100.00 68 100.00 100.00 1.78e-38 EMBL CAA86836 "activator of copYZAB [Enterococcus hirae ATCC 9790]" 98.53 69 100.00 100.00 6.66e-38 GB AFM70728 "copper chaperone [Enterococcus hirae ATCC 9790]" 98.53 69 100.00 100.00 6.66e-38 GB EOF61613 "copper chaperone CopZ [Enterococcus hirae EnGen0127]" 98.53 69 100.00 100.00 6.66e-38 GB EOH69882 "copper chaperone CopZ [Enterococcus hirae ATCC 9790]" 98.53 69 100.00 100.00 6.66e-38 GB EOU07149 "copper chaperone CopZ [Enterococcus hirae ATCC 9790]" 98.53 69 100.00 100.00 6.66e-38 GB KDR91397 "copper-binding protein [Enterococcus hirae]" 98.53 69 100.00 100.00 6.66e-38 REF WP_010718490 "MULTISPECIES: copper chaperone CopZ [Enterococcus]" 98.53 69 100.00 100.00 6.66e-38 SP Q47840 "RecName: Full=Copper chaperone CopZ; AltName: Full=Activator of copYZAB" 98.53 69 100.00 100.00 6.66e-38 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species _Strain _ATCC_number _Fraction _Gene_mnemonic $CopZ_peptide 'Enterococcus hirae' 1354 Eubacteria . Enterococcus hirae wild-type 9790 cytoplasm copZ stop_ save_ ######################### # Experimental source # ######################### save_experimental_source _Saveframe_category experimental_source loop_ _Mol_label _Production_method _Host_organism_name_common _Genus _Species _Strain _Vector_type _Vector_name _Details $CopZ_peptide 'recombinant technology' 'E. coli' Escherichia coli BL21 plasmid 'pQE6 plus helper plasmid pREP4' ; overexpression in E. coli resulted in a modification of the N-terminus from MKQ to AQ ; stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Saveframe_category sample _Sample_type solution _Details 'the sample was prepared and sealed under oxygen-free conditions' loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $CopZ_peptide 1.3 mM [U-15N] 'sodium phosphate' 50 mM . Na2S2O4 10 uM . stop_ save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer1 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model DRX _Field_strength 500 _Details . save_ save_NMR_spectrometer2 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model DRX _Field_strength 600 _Details . save_ save_NMR_spectrometer3 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model DRX _Field_strength 750 _Details . save_ ############################# # NMR applied experiments # ############################# save_2D_2QF-COSY_1 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 2QF-COSY' _Sample_label . save_ save_2D_3QF-COSY_2 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 3QF-COSY' _Sample_label . save_ save_2D_1H-1H_TOCSY_3 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-1H TOCSY' _Sample_label . save_ save_2D_1H-1H_NOESY_4 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-1H NOESY' _Sample_label . save_ save_2D_1H-15N_HSQC_5 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-15N HSQC' _Sample_label . save_ save_3D_1H-1H-15N_NOESY_6 _Saveframe_category NMR_applied_experiment _Experiment_name '3D 1H-1H-15N NOESY' _Sample_label . save_ save_3D_1H-1H-15N_TOCSY_7 _Saveframe_category NMR_applied_experiment _Experiment_name '3D 1H-1H-15N TOCSY' _Sample_label . save_ save_3D_ct-HNHB_8 _Saveframe_category NMR_applied_experiment _Experiment_name '3D ct-HNHB' _Sample_label . save_ save_mixing_time_of_NOESY_spectra:_50_ms_9 _Saveframe_category NMR_applied_experiment _Experiment_name 'mixing time of NOESY spectra: 50 ms' _Sample_label . save_ save_mixing_time_of_TOCSY_spectra:_50_and_90_ms_10 _Saveframe_category NMR_applied_experiment _Experiment_name 'mixing time of TOCSY spectra: 50 and 90 ms' _Sample_label . save_ save_NMR_spec_expt__0_1 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 2QF-COSY' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_2 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 3QF-COSY' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_3 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-1H TOCSY' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_4 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-1H NOESY' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_5 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-15N HSQC' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_6 _Saveframe_category NMR_applied_experiment _Experiment_name '3D 1H-1H-15N NOESY' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_7 _Saveframe_category NMR_applied_experiment _Experiment_name '3D 1H-1H-15N TOCSY' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_8 _Saveframe_category NMR_applied_experiment _Experiment_name '3D ct-HNHB' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_9 _Saveframe_category NMR_applied_experiment _Experiment_name 'mixing time of NOESY spectra: 50 ms' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_10 _Saveframe_category NMR_applied_experiment _Experiment_name 'mixing time of TOCSY spectra: 50 and 90 ms' _BMRB_pulse_sequence_accession_number . _Details . save_ ####################### # Sample conditions # ####################### save_conditions_1 _Saveframe_category sample_conditions _Details 'The sample contained 50mM NaPi and 10uM Na2S2O4' loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 7.0 0.1 na temperature 288.2 0.2 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 DSS N 15 'methyl protons' ppm 0.0 . indirect . . . 0.101329118 stop_ save_ ################################### # Assigned chemical shift lists # ################################### ################################################################### # Chemical Shift Ambiguity Index Value Definitions # # # # The values other than 1 are used for those atoms with different # # chemical shifts that cannot be assigned to stereospecific atoms # # or to specific residues or chains. # # # # Index Value Definition # # # # 1 Unique (including isolated methyl protons, # # geminal atoms, and geminal methyl # # groups with identical chemical shifts) # # (e.g. ILE HD11, HD12, HD13 protons) # # 2 Ambiguity of geminal atoms or geminal methyl # # proton groups (e.g. ASP HB2 and HB3 # # protons, LEU CD1 and CD2 carbons, or # # LEU HD11, HD12, HD13 and HD21, HD22, # # HD23 methyl protons) # # 3 Aromatic atoms on opposite sides of # # symmetrical rings (e.g. TYR HE1 and HE2 # # protons) # # 4 Intraresidue ambiguities (e.g. LYS HG and # # HD protons or TRP HZ2 and HZ3 protons) # # 5 Interresidue ambiguities (LYS 12 vs. LYS 27) # # 6 Intermolecular ambiguities (e.g. ASP 31 CA # # in monomer 1 and ASP 31 CA in monomer 2 # # of an asymmetrical homodimer, duplex # # DNA assignments, or other assignments # # that may apply to atoms in one or more # # molecule in the molecular assembly) # # 9 Ambiguous, specific ambiguity not defined # # # ################################################################### save_shift_set_1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Experiment_label '2D 2QF-COSY' '2D 3QF-COSY' '2D 1H-1H TOCSY' '2D 1H-1H NOESY' '2D 1H-15N HSQC' '3D 1H-1H-15N NOESY' '3D 1H-1H-15N TOCSY' '3D ct-HNHB' 'mixing time of NOESY spectra: 50 ms' 'mixing time of TOCSY spectra: 50 and 90 ms' stop_ loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $conditions_1 _Chem_shift_reference_set_label $chemical_shift_reference _Mol_system_component_name 'apo CopZ monomer' _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 ALA HA H 4.16 0.02 1 2 . 1 ALA HB H 1.33 0.02 1 3 . 2 GLN N N 119.6 0.05 1 4 . 2 GLN H H 8.57 0.02 1 5 . 2 GLN HA H 4.52 0.02 1 6 . 2 GLN HB2 H 2.21 0.02 2 7 . 2 GLN NE2 N 117.2 0.05 1 8 . 2 GLN HE21 H 7.95 0.02 2 9 . 2 GLN HE22 H 6.84 0.02 2 10 . 3 GLU N N 124.1 0.05 1 11 . 3 GLU H H 8.72 0.02 1 12 . 3 GLU HA H 5.35 0.02 1 13 . 3 GLU HB2 H 1.96 0.02 2 14 . 3 GLU HB3 H 1.88 0.02 2 15 . 3 GLU HG2 H 2.10 0.02 2 16 . 3 GLU HG3 H 2.25 0.02 2 17 . 4 PHE N N 118.3 0.05 1 18 . 4 PHE H H 9.15 0.02 1 19 . 4 PHE HA H 5.16 0.02 1 20 . 4 PHE HB2 H 2.55 0.02 2 21 . 4 PHE HB3 H 2.77 0.02 2 22 . 4 PHE HD1 H 7.07 0.02 1 23 . 4 PHE HD2 H 7.07 0.02 1 24 . 4 PHE HE1 H 7.25 0.02 1 25 . 4 PHE HE2 H 7.25 0.02 1 26 . 4 PHE HZ H 6.95 0.02 1 27 . 5 SER N N 118.9 0.05 1 28 . 5 SER H H 9.35 0.02 1 29 . 5 SER HA H 4.85 0.02 1 30 . 5 SER HB2 H 3.86 0.02 2 31 . 5 SER HB3 H 3.99 0.02 2 32 . 6 VAL N N 124.5 0.05 1 33 . 6 VAL H H 8.08 0.02 1 34 . 6 VAL HA H 4.60 0.02 1 35 . 6 VAL HB H 1.62 0.02 1 36 . 6 VAL HG1 H 0.72 0.02 2 37 . 6 VAL HG2 H 0.60 0.02 2 38 . 7 LYS N N 126.2 0.05 1 39 . 7 LYS H H 8.97 0.02 1 40 . 7 LYS HA H 4.72 0.02 1 41 . 7 LYS HB2 H 1.89 0.02 2 42 . 7 LYS HE2 H 2.96 0.02 2 43 . 8 GLY N N 107.6 0.05 1 44 . 8 GLY H H 8.72 0.02 1 45 . 8 GLY HA2 H 4.70 0.02 2 46 . 8 GLY HA3 H 3.74 0.02 2 47 . 9 MET N N 121.6 0.05 1 48 . 9 MET H H 9.29 0.02 1 49 . 9 MET HA H 4.96 0.02 1 50 . 9 MET HB2 H 2.45 0.02 2 51 . 9 MET HB3 H 1.57 0.02 2 52 . 9 MET HG2 H 1.35 0.02 2 53 . 9 MET HG3 H 1.91 0.02 2 54 . 10 SER N N 121.0 0.05 1 55 . 10 SER H H 11.08 0.02 1 56 . 10 SER HA H 4.80 0.02 1 57 . 10 SER HB2 H 3.80 0.02 2 58 . 10 SER HB3 H 3.96 0.02 2 59 . 11 CYS N N 119.3 0.05 1 60 . 11 CYS H H 8.67 0.02 1 61 . 11 CYS HA H 5.14 0.02 1 62 . 11 CYS HB2 H 3.16 0.02 2 63 . 11 CYS HB3 H 3.42 0.02 2 64 . 12 ASN N N 117.6 0.05 1 65 . 12 ASN H H 8.25 0.02 1 66 . 12 ASN HA H 4.68 0.02 1 67 . 12 ASN HB2 H 2.69 0.02 2 68 . 12 ASN HB3 H 2.81 0.02 2 69 . 12 ASN ND2 N 112.1 0.05 1 70 . 12 ASN HD21 H 7.69 0.02 2 71 . 12 ASN HD22 H 6.90 0.02 2 72 . 13 HIS HA H 4.56 0.02 1 73 . 13 HIS HB2 H 3.29 0.02 2 74 . 13 HIS HD2 H 7.15 0.02 1 75 . 13 HIS HE1 H 7.90 0.02 1 76 . 14 CYS N N 122.7 0.05 1 77 . 14 CYS H H 7.70 0.02 1 78 . 14 CYS HA H 3.91 0.02 1 79 . 14 CYS HB2 H 3.32 0.02 2 80 . 14 CYS HB3 H 2.57 0.02 2 81 . 15 VAL N N 116.2 0.05 1 82 . 15 VAL H H 6.67 0.02 1 83 . 15 VAL HA H 3.11 0.02 1 84 . 15 VAL HB H 2.37 0.02 1 85 . 15 VAL HG1 H 1.03 0.02 2 86 . 15 VAL HG2 H 0.90 0.02 2 87 . 16 ALA N N 119.6 0.05 1 88 . 16 ALA H H 7.43 0.02 1 89 . 16 ALA HA H 4.13 0.02 1 90 . 16 ALA HB H 1.48 0.02 1 91 . 17 ARG N N 117.9 0.05 1 92 . 17 ARG H H 8.33 0.02 1 93 . 17 ARG HA H 4.05 0.02 1 94 . 17 ARG HB2 H 1.92 0.02 2 95 . 17 ARG HB3 H 2.03 0.02 2 96 . 17 ARG HG2 H 1.66 0.02 2 97 . 17 ARG HG3 H 1.73 0.02 2 98 . 17 ARG HD2 H 3.25 0.02 2 99 . 17 ARG HD3 H 3.33 0.02 2 100 . 18 ILE N N 120.4 0.05 1 101 . 18 ILE H H 8.14 0.02 1 102 . 18 ILE HA H 3.45 0.02 1 103 . 18 ILE HB H 1.60 0.02 1 104 . 18 ILE HG2 H 0.49 0.02 1 105 . 18 ILE HG12 H 0.45 0.02 2 106 . 18 ILE HG13 H 1.73 0.02 2 107 . 18 ILE HD1 H 0.05 0.02 1 108 . 19 GLU N N 118.3 0.05 1 109 . 19 GLU H H 8.64 0.02 1 110 . 19 GLU HA H 3.61 0.02 1 111 . 19 GLU HB2 H 1.91 0.02 2 112 . 19 GLU HB3 H 2.06 0.02 2 113 . 19 GLU HG2 H 2.67 0.02 2 114 . 20 GLU N N 119.3 0.05 1 115 . 20 GLU H H 8.23 0.02 1 116 . 20 GLU HA H 3.96 0.02 1 117 . 20 GLU HB2 H 2.04 0.02 2 118 . 20 GLU HB3 H 2.12 0.02 2 119 . 20 GLU HG2 H 2.30 0.02 1 120 . 20 GLU HG3 H 2.30 0.02 1 121 . 21 ALA N N 119.7 0.05 1 122 . 21 ALA H H 7.67 0.02 1 123 . 21 ALA HA H 4.01 0.02 1 124 . 21 ALA HB H 1.48 0.02 1 125 . 22 VAL N N 116.9 0.05 1 126 . 22 VAL H H 8.65 0.02 1 127 . 22 VAL HA H 3.53 0.02 1 128 . 22 VAL HB H 1.91 0.02 1 129 . 22 VAL HG2 H 0.72 0.02 2 130 . 23 GLY N N 126.2 0.05 1 131 . 23 GLY H H 7.71 0.02 1 132 . 23 GLY HA2 H 3.78 0.02 2 133 . 23 GLY HA3 H 3.66 0.02 2 134 . 24 ARG N N 115.5 0.05 1 135 . 24 ARG H H 6.88 0.02 1 136 . 24 ARG HA H 4.28 0.02 1 137 . 24 ARG HB2 H 1.86 0.02 2 138 . 24 ARG HB3 H 1.91 0.02 2 139 . 24 ARG HG2 H 1.75 0.02 2 140 . 24 ARG HD2 H 3.17 0.02 2 141 . 24 ARG HE H 7.34 0.02 1 142 . 25 ILE N N 123.8 0.05 1 143 . 25 ILE H H 7.44 0.02 1 144 . 25 ILE HA H 3.74 0.02 1 145 . 25 ILE HB H 1.94 0.02 1 146 . 25 ILE HG2 H 0.77 0.02 1 147 . 25 ILE HG12 H 0.70 0.02 2 148 . 25 ILE HG13 H 0.95 0.02 2 149 . 25 ILE HD1 H 1.79 0.02 1 150 . 26 SER N N 124.8 0.05 1 151 . 26 SER H H 8.76 0.02 1 152 . 26 SER HA H 4.14 0.02 1 153 . 26 SER HB2 H 3.85 0.02 2 154 . 26 SER HB3 H 3.87 0.02 2 155 . 27 GLY N N 113.5 0.05 1 156 . 27 GLY H H 8.68 0.02 1 157 . 27 GLY HA2 H 4.48 0.02 2 158 . 27 GLY HA3 H 3.77 0.02 2 159 . 28 VAL N N 121.7 0.05 1 160 . 28 VAL H H 8.11 0.02 1 161 . 28 VAL HA H 3.91 0.02 1 162 . 28 VAL HB H 2.38 0.02 1 163 . 28 VAL HG1 H 0.76 0.02 2 164 . 28 VAL HG2 H 0.73 0.02 2 165 . 29 LYS N N 127.9 0.05 1 166 . 29 LYS H H 9.20 0.02 1 167 . 29 LYS HA H 4.52 0.02 1 168 . 29 LYS HB2 H 1.49 0.02 2 169 . 29 LYS HB3 H 1.88 0.02 2 170 . 29 LYS HE2 H 2.93 0.02 2 171 . 30 LYS N N 117.6 0.05 1 172 . 30 LYS H H 7.75 0.02 1 173 . 30 LYS HA H 4.60 0.02 1 174 . 30 LYS HB2 H 1.69 0.02 2 175 . 30 LYS HB3 H 1.79 0.02 2 176 . 30 LYS HE2 H 2.91 0.02 2 177 . 31 VAL N N 122.8 0.05 1 178 . 31 VAL H H 8.76 0.02 1 179 . 31 VAL HA H 4.97 0.02 1 180 . 31 VAL HB H 1.96 0.02 1 181 . 31 VAL HG1 H 0.92 0.02 2 182 . 31 VAL HG2 H 0.72 0.02 2 183 . 32 LYS N N 126.8 0.05 1 184 . 32 LYS H H 8.57 0.02 1 185 . 32 LYS HA H 4.87 0.02 1 186 . 32 LYS HB2 H 1.62 0.02 2 187 . 32 LYS HB3 H 1.76 0.02 2 188 . 32 LYS HG2 H 1.29 0.02 2 189 . 32 LYS HD2 H 1.72 0.02 2 190 . 32 LYS HE2 H 2.93 0.02 2 191 . 33 VAL N N 129.3 0.05 1 192 . 33 VAL H H 10.02 0.02 1 193 . 33 VAL HA H 4.39 0.02 1 194 . 33 VAL HB H 2.13 0.02 1 195 . 33 VAL HG1 H 0.82 0.02 2 196 . 33 VAL HG2 H 0.78 0.02 2 197 . 34 GLN N N 127.2 0.05 1 198 . 34 GLN H H 8.96 0.02 1 199 . 34 GLN HA H 4.60 0.02 1 200 . 34 GLN HB2 H 2.03 0.02 2 201 . 34 GLN HB3 H 1.94 0.02 2 202 . 34 GLN HG2 H 2.15 0.02 2 203 . 34 GLN HG3 H 2.23 0.02 2 204 . 34 GLN NE2 N 109.7 0.05 1 205 . 34 GLN HE21 H 7.30 0.02 2 206 . 34 GLN HE22 H 6.82 0.02 2 207 . 35 LEU N N 126.5 0.05 1 208 . 35 LEU H H 8.81 0.02 1 209 . 35 LEU HA H 3.84 0.02 1 210 . 35 LEU HB2 H 1.43 0.02 2 211 . 35 LEU HB3 H 1.75 0.02 2 212 . 35 LEU HG H 1.36 0.02 1 213 . 35 LEU HD1 H 0.72 0.02 1 214 . 35 LEU HD2 H 0.72 0.02 1 215 . 36 LYS N N 116.2 0.05 1 216 . 36 LYS H H 8.76 0.02 1 217 . 36 LYS HA H 4.06 0.02 1 218 . 36 LYS HB2 H 1.86 0.02 2 219 . 37 LYS N N 114.1 0.05 1 220 . 37 LYS H H 6.98 0.02 1 221 . 37 LYS HA H 4.35 0.02 1 222 . 37 LYS HB2 H 1.49 0.02 2 223 . 37 LYS HB3 H 1.92 0.02 2 224 . 37 LYS HG2 H 1.32 0.02 2 225 . 37 LYS HG3 H 1.45 0.02 2 226 . 37 LYS HD2 H 1.59 0.02 2 227 . 37 LYS HE2 H 2.92 0.02 2 228 . 38 GLU N N 115.2 0.05 1 229 . 38 GLU H H 7.75 0.02 1 230 . 38 GLU HA H 3.54 0.02 1 231 . 38 GLU HB2 H 2.31 0.02 2 232 . 38 GLU HB3 H 2.28 0.02 2 233 . 38 GLU HG2 H 2.17 0.02 2 234 . 38 GLU HG3 H 2.21 0.02 2 235 . 39 LYS N N 115.2 0.05 1 236 . 39 LYS H H 7.56 0.02 1 237 . 39 LYS HA H 5.62 0.02 1 238 . 39 LYS HB2 H 1.63 0.02 2 239 . 39 LYS HB3 H 1.70 0.02 2 240 . 39 LYS HG2 H 1.27 0.02 2 241 . 39 LYS HG3 H 1.37 0.02 2 242 . 39 LYS HD2 H 1.49 0.02 2 243 . 39 LYS HD3 H 1.57 0.02 2 244 . 39 LYS HE2 H 2.78 0.02 2 245 . 39 LYS HE3 H 2.72 0.02 2 246 . 40 ALA N N 121.3 0.05 1 247 . 40 ALA H H 9.28 0.02 1 248 . 40 ALA HA H 5.23 0.02 1 249 . 40 ALA HB H 1.05 0.02 1 250 . 41 VAL N N 122.0 0.05 1 251 . 41 VAL H H 8.99 0.02 1 252 . 41 VAL HA H 4.89 0.02 1 253 . 41 VAL HB H 2.00 0.02 1 254 . 41 VAL HG1 H 0.92 0.02 2 255 . 41 VAL HG2 H 0.85 0.02 2 256 . 42 VAL N N 127.5 0.05 1 257 . 42 VAL H H 9.23 0.02 1 258 . 42 VAL HA H 5.04 0.02 1 259 . 42 VAL HB H 2.29 0.02 1 260 . 42 VAL HG1 H 1.02 0.02 2 261 . 42 VAL HG2 H 0.74 0.02 2 262 . 43 LYS N N 128.1 0.05 1 263 . 43 LYS H H 9.11 0.02 1 264 . 43 LYS HA H 4.88 0.02 1 265 . 43 LYS HB2 H 1.75 0.02 2 266 . 43 LYS HB3 H 1.87 0.02 2 267 . 43 LYS HG2 H 1.28 0.02 2 268 . 43 LYS HG3 H 1.47 0.02 2 269 . 43 LYS HD2 H 1.59 0.02 2 270 . 43 LYS HD3 H 1.70 0.02 2 271 . 43 LYS HE2 H 2.90 0.02 2 272 . 44 PHE N N 123.7 0.05 1 273 . 44 PHE H H 8.78 0.02 1 274 . 44 PHE HA H 5.32 0.02 1 275 . 44 PHE HB2 H 2.73 0.02 2 276 . 44 PHE HB3 H 2.91 0.02 2 277 . 44 PHE HD1 H 6.95 0.02 1 278 . 44 PHE HD2 H 6.95 0.02 1 279 . 44 PHE HE1 H 7.41 0.02 1 280 . 44 PHE HE2 H 7.41 0.02 1 281 . 45 ASP N N 120.0 0.05 1 282 . 45 ASP H H 8.66 0.02 1 283 . 45 ASP HA H 4.71 0.02 1 284 . 45 ASP HB2 H 2.66 0.02 2 285 . 45 ASP HB3 H 3.02 0.02 2 286 . 46 GLU N N 127.9 0.05 1 287 . 46 GLU H H 9.02 0.02 1 288 . 46 GLU HA H 4.83 0.02 1 289 . 46 GLU HB2 H 2.07 0.02 2 290 . 46 GLU HB3 H 2.28 0.02 2 291 . 46 GLU HG2 H 2.17 0.02 2 292 . 47 ALA N N 120.3 0.05 1 293 . 47 ALA H H 8.43 0.02 1 294 . 47 ALA HA H 4.27 0.02 1 295 . 47 ALA HB H 1.42 0.02 1 296 . 48 ASN N N 113.8 0.05 1 297 . 48 ASN H H 7.87 0.02 1 298 . 48 ASN HA H 4.90 0.02 1 299 . 48 ASN HB2 H 2.49 0.02 2 300 . 48 ASN HB3 H 2.84 0.02 2 301 . 48 ASN ND2 N 113.1 0.05 1 302 . 48 ASN HD21 H 6.94 0.02 2 303 . 48 ASN HD22 H 7.72 0.02 2 304 . 49 VAL N N 121.7 0.05 1 305 . 49 VAL H H 8.12 0.02 1 306 . 49 VAL HA H 4.33 0.02 1 307 . 49 VAL HB H 2.07 0.02 1 308 . 49 VAL HG1 H 0.91 0.02 2 309 . 49 VAL HG2 H 0.56 0.02 2 310 . 50 GLN N N 120.7 0.05 1 311 . 50 GLN H H 8.30 0.02 1 312 . 50 GLN HA H 4.81 0.02 1 313 . 50 GLN HB2 H 1.92 0.02 2 314 . 50 GLN HB3 H 2.42 0.02 2 315 . 50 GLN HG2 H 2.46 0.02 2 316 . 50 GLN NE2 N 114.1 0.05 1 317 . 50 GLN HE21 H 7.65 0.02 2 318 . 50 GLN HE22 H 6.99 0.02 2 319 . 51 ALA N N 125.5 0.05 1 320 . 51 ALA H H 9.48 0.02 1 321 . 51 ALA HA H 3.82 0.02 1 322 . 51 ALA HB H 1.67 0.02 1 323 . 52 THR N N 108.3 0.05 1 324 . 52 THR H H 8.23 0.02 1 325 . 52 THR HA H 3.96 0.02 1 326 . 52 THR HB H 4.21 0.02 1 327 . 52 THR HG2 H 1.34 0.02 1 328 . 53 GLU N N 122.4 0.05 1 329 . 53 GLU H H 7.40 0.02 1 330 . 53 GLU HA H 4.07 0.02 1 331 . 53 GLU HB2 H 2.30 0.02 2 332 . 53 GLU HB3 H 1.98 0.02 2 333 . 53 GLU HG2 H 2.23 0.02 2 334 . 54 ILE N N 121.1 0.05 1 335 . 54 ILE H H 7.06 0.02 1 336 . 54 ILE HA H 3.28 0.02 1 337 . 54 ILE HB H 1.69 0.02 1 338 . 54 ILE HG2 H -0.04 0.02 1 339 . 54 ILE HG12 H 0.58 0.02 2 340 . 54 ILE HG13 H 1.08 0.02 2 341 . 54 ILE HD1 H 0.01 0.02 1 342 . 55 CYS N N 115.9 0.05 1 343 . 55 CYS H H 7.91 0.02 1 344 . 55 CYS HA H 3.57 0.02 1 345 . 55 CYS HB2 H 2.91 0.02 2 346 . 55 CYS HB3 H 3.08 0.02 2 347 . 55 CYS HG H 2.22 0.02 1 348 . 56 GLN N N 117.6 0.05 1 349 . 56 GLN H H 8.02 0.02 1 350 . 56 GLN HA H 4.00 0.02 1 351 . 56 GLN HB2 H 2.04 0.02 2 352 . 56 GLN HB3 H 2.19 0.02 2 353 . 56 GLN HG2 H 2.44 0.02 2 354 . 56 GLN NE2 N 112.4 0.05 1 355 . 56 GLN HE21 H 7.75 0.02 2 356 . 56 GLN HE22 H 6.91 0.02 2 357 . 57 ALA N N 120.7 0.05 1 358 . 57 ALA H H 7.43 0.02 1 359 . 57 ALA HA H 4.06 0.02 1 360 . 57 ALA HB H 1.35 0.02 1 361 . 58 ILE N N 116.9 0.05 1 362 . 58 ILE H H 7.38 0.02 1 363 . 58 ILE HA H 3.50 0.02 1 364 . 58 ILE HB H 1.64 0.02 1 365 . 58 ILE HG2 H 0.82 0.02 1 366 . 58 ILE HG12 H 0.16 0.02 2 367 . 58 ILE HG13 H 0.37 0.02 2 368 . 58 ILE HD1 H 1.70 0.02 1 369 . 59 ASN N N 121.3 0.05 1 370 . 59 ASN H H 8.62 0.02 1 371 . 59 ASN HA H 5.04 0.02 1 372 . 59 ASN HB2 H 2.83 0.02 2 373 . 59 ASN HB3 H 2.90 0.02 2 374 . 59 ASN ND2 N 107.9 0.05 1 375 . 59 ASN HD21 H 7.27 0.02 2 376 . 59 ASN HD22 H 6.66 0.02 2 377 . 60 GLU N N 120.7 0.05 1 378 . 60 GLU H H 8.30 0.02 1 379 . 60 GLU HA H 4.03 0.02 1 380 . 60 GLU HB2 H 2.07 0.02 2 381 . 61 LEU N N 116.9 0.05 1 382 . 61 LEU H H 7.37 0.02 1 383 . 61 LEU HA H 4.25 0.02 1 384 . 61 LEU HB2 H 2.31 0.02 2 385 . 61 LEU HB3 H 1.63 0.02 2 386 . 61 LEU HG H 2.07 0.02 1 387 . 61 LEU HD1 H 0.83 0.02 2 388 . 61 LEU HD2 H 0.91 0.02 2 389 . 62 GLY N N 126.2 0.05 1 390 . 62 GLY H H 7.90 0.02 1 391 . 62 GLY HA2 H 4.07 0.02 2 392 . 62 GLY HA3 H 3.55 0.02 2 393 . 63 TYR N N 119.3 0.05 1 394 . 63 TYR H H 6.50 0.02 1 395 . 63 TYR HA H 4.73 0.02 1 396 . 63 TYR HB2 H 2.29 0.02 2 397 . 63 TYR HB3 H 3.27 0.02 2 398 . 63 TYR HD1 H 6.80 0.02 1 399 . 63 TYR HD2 H 6.80 0.02 1 400 . 63 TYR HE1 H 6.87 0.02 1 401 . 63 TYR HE2 H 6.87 0.02 1 402 . 64 GLN N N 116.5 0.05 1 403 . 64 GLN H H 8.08 0.02 1 404 . 64 GLN HA H 4.86 0.02 1 405 . 64 GLN HB2 H 1.93 0.02 2 406 . 64 GLN HG2 H 2.22 0.02 2 407 . 64 GLN NE2 N 112.1 0.05 1 408 . 64 GLN HE21 H 7.50 0.02 2 409 . 64 GLN HE22 H 6.75 0.02 2 410 . 65 ALA N N 109.3 0.05 1 411 . 65 ALA H H 9.73 0.02 1 412 . 65 ALA HA H 6.02 0.02 1 413 . 65 ALA HB H 1.35 0.02 1 414 . 66 GLU N N 119.0 0.05 1 415 . 66 GLU H H 8.66 0.02 1 416 . 66 GLU HA H 4.84 0.02 1 417 . 66 GLU HB2 H 2.08 0.02 2 418 . 66 GLU HB3 H 1.90 0.02 2 419 . 66 GLU HG2 H 2.25 0.02 2 420 . 66 GLU HG3 H 2.31 0.02 2 421 . 67 VAL N N 123.4 0.05 1 422 . 67 VAL H H 8.83 0.02 1 423 . 67 VAL HA H 3.68 0.02 1 424 . 67 VAL HB H 1.91 0.02 1 425 . 67 VAL HG1 H 0.87 0.02 2 426 . 67 VAL HG2 H 0.78 0.02 2 427 . 68 ILE N N 107.9 0.05 1 428 . 68 ILE H H 7.47 0.02 1 429 . 68 ILE HA H 4.10 0.02 1 430 . 68 ILE HB H 1.69 0.02 1 431 . 68 ILE HG2 H 0.86 0.02 1 432 . 68 ILE HG12 H 1.35 0.02 2 433 . 68 ILE HD1 H 0.78 0.02 1 stop_ save_