data_6209 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Solution Structure of a Calmodulin-Like Calcium-Binding Domain from Arabidopsis thaliana ; _BMRB_accession_number 6209 _BMRB_flat_file_name bmr6209.str _Entry_type original _Submission_date 2004-05-19 _Accession_date 2004-05-20 _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 Song Jikui . . 2 Zhao Qin . . 3 Thao Sandy . . 4 Frederick Ronnie O. . 5 Markley John L. . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 residual_dipolar_couplings 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 341 "13C chemical shifts" 261 "15N chemical shifts" 69 "residual dipolar couplings" 55 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2005-01-07 update BMRB 'citation updated' 2004-06-30 original author 'original release' stop_ save_ ############################# # Citation for this entry # ############################# save_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; Letter to the Editor: Solution Structure of a Calmodulin-Like Calcium-Binding Domain from Arabidopsis thaliana ; _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 Song Jikui . . 2 Zhao Qin . . 3 Thao Sandy . . 4 Frederick Ronnie O. . 5 Markley John L. . stop_ _Journal_abbreviation 'J. Biomol. NMR' _Journal_volume 30 _Journal_issue 4 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 451 _Page_last 456 _Year 2004 _Details . save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name 'N-domain of At3g03410.1' _Abbreviation_common 'N-domain of At3g03410.1' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'Calmodulin like protein' $Calmodulin_like_protein stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state monomer _System_paramagnetic no _System_thiol_state 'all free' _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_Calmodulin_like_protein _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'N-terminal domain of At3g03410.1' _Name_variant 'N-terminal domain of At3g03410.1' _Abbreviation_common 'N-terminal domain of At3g03410.1' _Molecular_mass . _Mol_thiol_state 'all free' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 67 _Mol_residue_sequence ; SSAKRVFEKFDKNKDGKLSL DEFREVALAFSPYFTQEDIV KFFEEIDVDGNGELNADEFT SCIEKML ; loop_ _Residue_seq_code _Residue_label 1 SER 2 SER 3 ALA 4 LYS 5 ARG 6 VAL 7 PHE 8 GLU 9 LYS 10 PHE 11 ASP 12 LYS 13 ASN 14 LYS 15 ASP 16 GLY 17 LYS 18 LEU 19 SER 20 LEU 21 ASP 22 GLU 23 PHE 24 ARG 25 GLU 26 VAL 27 ALA 28 LEU 29 ALA 30 PHE 31 SER 32 PRO 33 TYR 34 PHE 35 THR 36 GLN 37 GLU 38 ASP 39 ILE 40 VAL 41 LYS 42 PHE 43 PHE 44 GLU 45 GLU 46 ILE 47 ASP 48 VAL 49 ASP 50 GLY 51 ASN 52 GLY 53 GLU 54 LEU 55 ASN 56 ALA 57 ASP 58 GLU 59 PHE 60 THR 61 SER 62 CYS 63 ILE 64 GLU 65 LYS 66 MET 67 LEU stop_ _Sequence_homology_query_date 2010-09-18 _Sequence_homology_query_revised_last_date 2010-09-18 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 SP Q9SRP5 'RecName: Full=Probable calcium-binding protein CML34; AltName: Full=Calmodulin-like protein 2; AltName: Full=Calmodulin-like protein 34' 98.51 131 100.00 100.00 1.89e-29 REF NP_186991 'calmodulin-related protein, putative [Arabidopsis thaliana]' 98.51 131 100.00 100.00 1.89e-29 GB ABK32174 'At3g03410 [Arabidopsis thaliana]' 98.51 131 100.00 100.00 1.89e-29 GB AAF01604 'calmodulin-like protein [Arabidopsis thaliana]' 98.51 131 100.00 100.00 1.89e-29 PDB 1TIZ 'Solution Structure Of A Calmodulin-Like Calcium-Binding Domain From Arabidopsis Thaliana' 100.00 67 100.00 100.00 8.28e-30 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $Calmodulin_like_protein 'thale cress' 3702 Eukaryota Viridiplantae Arabidopsis thaliana 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 $Calmodulin_like_protein 'recombinant technology' 'E. coli' Escherichia coli . plasmid pDEST17 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 $Calmodulin_like_protein 1 mM [U-15N] DTT 5 mM . Bis-Tris 20 mM . CaCl2 5 mM . DSS 1 mM . stop_ save_ save_2 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $Calmodulin_like_protein 1 mM '[U-15N; U-13C]' DTT 5 mM . Bis-Tris 20 mM . CaCl2 5 mM . DSS 1 mM . stop_ save_ save_3 _Saveframe_category sample _Sample_type solution _Details 'Dissolved in 5% Pentaethylene Glycol Monododecyl Ether (weakly aligned medium)' loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $Calmodulin_like_protein 1 mM '[U-15N; U-13C]' DTT 5 mM . Bis-Tris 20 mM . CaCl2 5 mM . DSS 1 mM . PEG 5 % . stop_ save_ ############################ # Computer software used # ############################ save_XWINNMR _Saveframe_category software _Name XWINNMR _Version 3.2 loop_ _Vendor _Address _Electronic_address Bruker . . stop_ loop_ _Task 'Data collection' stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model DMX _Field_strength 600 _Details . save_ ############################# # NMR applied experiments # ############################# save_HNCACB_1 _Saveframe_category NMR_applied_experiment _Experiment_name HNCACB _Sample_label . save_ save_HN(CO)CACB_2 _Saveframe_category NMR_applied_experiment _Experiment_name HN(CO)CACB _Sample_label . save_ save_N15_edited_NOESY_3 _Saveframe_category NMR_applied_experiment _Experiment_name 'N15 edited NOESY' _Sample_label . save_ save_N15_edited_TOCSY_4 _Saveframe_category NMR_applied_experiment _Experiment_name 'N15 edited TOCSY' _Sample_label . save_ save_IPAP-HSQC_5 _Saveframe_category NMR_applied_experiment _Experiment_name IPAP-HSQC _Sample_label . save_ save_NMR_spec_expt__0_1 _Saveframe_category NMR_applied_experiment _Experiment_name HNCACB _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_2 _Saveframe_category NMR_applied_experiment _Experiment_name HN(CO)CACB _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_3 _Saveframe_category NMR_applied_experiment _Experiment_name 'N15 edited NOESY' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_4 _Saveframe_category NMR_applied_experiment _Experiment_name 'N15 edited TOCSY' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_5 _Saveframe_category NMR_applied_experiment _Experiment_name IPAP-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 6.4 0.2 pH temperature 298 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 _Indirect_shift_ratio_citation_label _Correction_value_citation_label DSS H 1 'methyl protons' ppm 0.00 internal indirect . . . 1.0 $citation $citation DSS N 15 'methyl protons' ppm 0.00 . indirect . . . 0.101329118 $citation $citation DSS C 13 'methyl protons' ppm 0.00 . indirect . . . 0.251449530 $citation $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_shift_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_reference _Mol_system_component_name 'Calmodulin like protein' _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 . 2 SER C C 175.508 0.10 1 2 . 2 SER CA C 59.472 0.10 1 3 . 2 SER CB C 63.633 0.10 1 4 . 2 SER HA H 4.596 0.05 1 5 . 2 SER HB2 H 4.040 0.05 2 6 . 2 SER HB3 H 4.101 0.05 2 7 . 3 ALA C C 179.029 0.10 1 8 . 3 ALA CA C 55.439 0.10 1 9 . 3 ALA CB C 19.431 0.10 1 10 . 3 ALA HA H 4.215 0.05 1 11 . 3 ALA H H 8.997 0.05 1 12 . 3 ALA N N 126.234 0.10 1 13 . 3 ALA HB H 1.570 0.05 1 14 . 4 LYS C C 178.197 0.05 1 15 . 4 LYS CA C 59.215 0.10 1 16 . 4 LYS CB C 32.518 0.10 1 17 . 4 LYS CD C 29.307 0.10 1 18 . 4 LYS CE C 42.150 0.10 1 19 . 4 LYS CG C 25.313 0.10 1 20 . 4 LYS HA H 4.126 0.05 1 21 . 4 LYS HB2 H 1.948 0.05 2 22 . 4 LYS HD2 H 1.726 0.05 2 23 . 4 LYS HE2 H 3.027 0.05 2 24 . 4 LYS HG2 H 1.540 0.05 2 25 . 4 LYS H H 8.236 0.05 1 26 . 4 LYS N N 119.550 0.10 1 27 . 5 ARG C C 179.538 0.10 1 28 . 5 ARG CA C 58.836 0.10 1 29 . 5 ARG CB C 30.164 0.10 1 30 . 5 ARG CD C 43.433 0.10 1 31 . 5 ARG CG C 27.627 0.10 1 32 . 5 ARG HA H 4.308 0.05 1 33 . 5 ARG HB2 H 2.105 0.05 2 34 . 5 ARG HD2 H 3.344 0.05 2 35 . 5 ARG HG2 H 1.858 0.05 2 36 . 5 ARG HG3 H 1.806 0.05 2 37 . 5 ARG H H 7.900 0.05 2 38 . 5 ARG N N 119.852 0.10 1 39 . 6 VAL C C 176.961 0.10 1 40 . 6 VAL CA C 66.918 0.10 1 41 . 6 VAL CB C 32.371 0.10 1 42 . 6 VAL CG1 C 23.139 0.20 1 43 . 6 VAL HA H 3.871 0.05 1 44 . 6 VAL HB H 2.527 0.05 1 45 . 6 VAL H H 8.100 0.05 1 46 . 6 VAL N N 122.024 0.05 1 47 . 6 VAL HG1 H 1.308 0.10 2 48 . 7 PHE C C 176.425 0.10 1 49 . 7 PHE CA C 62.189 0.10 1 50 . 7 PHE CB C 39.222 0.10 1 51 . 7 PHE HA H 3.464 0.05 1 52 . 7 PHE HB2 H 3.081 0.05 2 53 . 7 PHE HB3 H 3.438 0.05 2 54 . 7 PHE H H 8.359 0.05 1 55 . 7 PHE N N 121.905 0.05 1 56 . 7 PHE HD1 H 6.834 0.05 4 57 . 7 PHE HE1 H 6.967 0.05 4 58 . 8 GLU C C 179.048 0.10 1 59 . 8 GLU CA C 59.150 0.10 1 60 . 8 GLU CB C 29.955 0.10 1 61 . 8 GLU CG C 37.012 0.10 1 62 . 8 GLU HA H 4.059 0.05 1 63 . 8 GLU HB2 H 2.229 0.05 2 64 . 8 GLU HB3 H 2.124 0.05 2 65 . 8 GLU HG2 H 2.729 0.05 2 66 . 8 GLU HG3 H 2.471 0.05 2 67 . 8 GLU H H 8.211 0.05 1 68 . 8 GLU N N 115.687 0.10 1 69 . 9 LYS C C 178.025 0.10 1 70 . 9 LYS CA C 58.741 0.10 1 71 . 9 LYS CB C 32.460 0.10 1 72 . 9 LYS CD C 29.474 0.10 1 73 . 9 LYS CE C 42.160 0.10 1 74 . 9 LYS CG C 24.576 0.20 1 75 . 9 LYS HA H 3.902 0.05 1 76 . 9 LYS HB2 H 1.816 0.05 2 77 . 9 LYS HD2 H 1.509 0.05 2 78 . 9 LYS HD3 H 1.442 0.05 2 79 . 9 LYS HE2 H 2.722 0.05 2 80 . 9 LYS HG2 H 1.063 0.05 2 81 . 9 LYS HG3 H 0.557 0.05 2 82 . 9 LYS H H 7.814 0.05 1 83 . 9 LYS N N 119.885 0.10 1 84 . 10 PHE C C 175.164 0.10 1 85 . 10 PHE CA C 59.402 0.10 1 86 . 10 PHE CB C 39.474 0.10 1 87 . 10 PHE HA H 4.385 0.05 1 88 . 10 PHE HB2 H 3.168 0.05 2 89 . 10 PHE HB3 H 2.370 0.05 2 90 . 10 PHE H H 7.519 0.05 1 91 . 10 PHE N N 114.808 0.10 1 92 . 11 ASP C C 177.621 0.10 1 93 . 11 ASP CA C 52.638 0.10 1 94 . 11 ASP CB C 38.058 0.10 1 95 . 11 ASP HA H 4.572 0.05 1 96 . 11 ASP HB2 H 2.836 0.05 2 97 . 11 ASP HB3 H 2.027 0.05 2 98 . 11 ASP H H 7.489 0.05 1 99 . 11 ASP N N 122.545 0.05 1 100 . 12 LYS C C 177.745 0.10 1 101 . 12 LYS CA C 59.173 0.10 1 102 . 12 LYS CB C 33.086 0.10 1 103 . 12 LYS CD C 29.017 0.10 1 104 . 12 LYS CE C 42.105 0.10 1 105 . 12 LYS CG C 25.067 0.10 1 106 . 12 LYS HA H 4.007 0.05 1 107 . 12 LYS HB2 H 1.989 0.05 2 108 . 12 LYS HD2 H 1.808 0.05 2 109 . 12 LYS HE2 H 3.105 0.05 2 110 . 12 LYS HG2 H 1.556 0.05 2 111 . 12 LYS HG3 H 1.670 0.05 2 112 . 12 LYS H H 7.682 0.05 1 113 . 12 LYS N N 128.363 0.10 1 114 . 13 ASN C C 174.506 0.10 1 115 . 13 ASN CA C 51.740 0.10 1 116 . 13 ASN CB C 36.747 0.10 1 117 . 13 ASN HA H 4.833 0.05 1 118 . 13 ASN HB2 H 3.344 0.05 2 119 . 13 ASN HB3 H 2.854 0.05 2 120 . 13 ASN HD21 H 8.057 0.05 2 121 . 13 ASN HD22 H 6.712 0.05 2 122 . 13 ASN H H 7.946 0.05 1 123 . 13 ASN N N 113.684 0.10 1 124 . 13 ASN ND2 N 114.876 0.10 1 125 . 14 LYS C C 175.752 0.10 1 126 . 14 LYS CA C 57.023 0.20 1 127 . 14 LYS CB C 29.305 0.10 1 128 . 14 LYS CD C 28.917 0.10 1 129 . 14 LYS CE C 42.554 0.10 1 130 . 14 LYS CG C 24.837 0.20 1 131 . 14 LYS HA H 3.970 0.05 1 132 . 14 LYS HB2 H 1.999 0.05 2 133 . 14 LYS HD2 H 1.825 0.05 2 134 . 14 LYS HD3 H 1.729 0.05 2 135 . 14 LYS HE2 H 3.088 0.05 2 136 . 14 LYS HE3 H 3.060 0.05 2 137 . 14 LYS HG2 H 1.426 0.05 2 138 . 14 LYS H H 7.746 0.05 1 139 . 14 LYS N N 116.760 0.10 1 140 . 15 ASP C C 178.137 0.10 1 141 . 15 ASP CA C 52.873 0.10 1 142 . 15 ASP CB C 40.852 0.10 1 143 . 15 ASP HA H 4.779 0.05 1 144 . 15 ASP HB2 H 3.131 0.05 2 145 . 15 ASP HB3 H 2.482 0.05 2 146 . 15 ASP H H 8.311 0.05 1 147 . 15 ASP N N 118.730 0.10 1 148 . 16 GLY C C 173.227 0.10 1 149 . 16 GLY CA C 46.050 0.10 1 150 . 16 GLY HA2 H 3.753 0.05 2 151 . 16 GLY HA3 H 4.266 0.05 2 152 . 16 GLY H H 10.545 0.05 1 153 . 16 GLY N N 114.350 0.10 1 154 . 17 LYS C C 175.723 0.10 1 155 . 17 LYS CA C 53.939 0.10 1 156 . 17 LYS CB C 36.070 0.10 1 157 . 17 LYS CD C 29.255 0.10 1 158 . 17 LYS CE C 42.464 0.10 1 159 . 17 LYS CG C 24.005 0.10 1 160 . 17 LYS HA H 5.341 0.05 1 161 . 17 LYS HB2 H 1.618 0.05 2 162 . 17 LYS HD2 H 1.456 0.05 2 163 . 17 LYS HD3 H 1.646 0.05 2 164 . 17 LYS HE2 H 2.965 0.05 2 165 . 17 LYS HG2 H 1.314 0.05 2 166 . 17 LYS H H 7.979 0.05 1 167 . 17 LYS N N 119.026 0.10 1 168 . 18 LEU C C 177.150 0.10 1 169 . 18 LEU CA C 53.173 0.10 1 170 . 18 LEU CB C 43.433 0.10 1 171 . 18 LEU CD1 C 22.941 0.10 1 172 . 18 LEU CD2 C 26.893 0.10 1 173 . 18 LEU CG C 26.606 0.10 1 174 . 18 LEU HA H 5.745 0.05 1 175 . 18 LEU HB2 H 1.863 0.05 2 176 . 18 LEU HB3 H 1.516 0.05 2 177 . 18 LEU HG H 1.171 0.05 1 178 . 18 LEU H H 9.731 0.05 1 179 . 18 LEU N N 124.947 0.10 1 180 . 18 LEU HD1 H 0.353 0.05 2 181 . 18 LEU HD2 H 0.342 0.05 2 182 . 19 SER C C 175.336 0.10 1 183 . 19 SER CA C 56.191 0.10 1 184 . 19 SER CB C 65.840 0.10 1 185 . 19 SER HA H 4.936 0.05 1 186 . 19 SER HB2 H 4.509 0.05 2 187 . 19 SER HB3 H 4.086 0.05 2 188 . 19 SER H H 9.006 0.05 1 189 . 19 SER N N 121.155 0.10 1 190 . 20 LEU C C 178.403 0.10 1 191 . 20 LEU CA C 59.179 0.10 1 192 . 20 LEU CB C 40.624 0.10 1 193 . 20 LEU CD1 C 25.737 0.10 1 194 . 20 LEU CD2 C 23.213 0.10 1 195 . 20 LEU CG C 27.217 0.20 1 196 . 20 LEU HA H 3.631 0.05 1 197 . 20 LEU HB2 H 1.542 0.05 2 198 . 20 LEU HB3 H 0.712 0.05 2 199 . 20 LEU HG H 1.277 0.05 1 200 . 20 LEU H H 9.070 0.05 1 201 . 20 LEU N N 124.998 0.10 1 202 . 20 LEU HD1 H 0.745 0.05 2 203 . 20 LEU HD2 H 0.562 0.05 2 204 . 21 ASP C C 179.341 0.10 1 205 . 21 ASP CA C 57.531 0.10 1 206 . 21 ASP CB C 40.600 0.10 1 207 . 21 ASP HA H 4.384 0.05 1 208 . 21 ASP HB2 H 2.695 0.05 2 209 . 21 ASP HB3 H 2.623 0.05 2 210 . 21 ASP H H 8.283 0.05 1 211 . 21 ASP N N 117.675 0.10 1 212 . 22 GLU C C 179.693 0.10 1 213 . 22 GLU CA C 58.431 0.10 1 214 . 22 GLU CB C 30.637 0.10 1 215 . 22 GLU CG C 37.177 0.20 1 216 . 22 GLU HA H 4.447 0.05 1 217 . 22 GLU HB2 H 2.490 0.05 2 218 . 22 GLU HB3 H 2.389 0.05 2 219 . 22 GLU HG2 H 2.637 0.05 2 220 . 22 GLU HG3 H 2.452 0.05 2 221 . 22 GLU H H 7.695 0.05 1 222 . 22 GLU N N 120.933 0.10 1 223 . 23 PHE C C 176.259 0.10 1 224 . 23 PHE CA C 61.285 0.10 1 225 . 23 PHE CB C 40.173 0.10 1 226 . 23 PHE HA H 4.130 0.05 1 227 . 23 PHE HB2 H 3.324 0.05 2 228 . 23 PHE HB3 H 3.379 0.05 2 229 . 23 PHE H H 9.264 0.05 1 230 . 23 PHE N N 121.354 0.10 1 231 . 23 PHE HD1 H 7.120 0.10 4 232 . 23 PHE HE1 H 7.256 0.10 4 233 . 24 ARG C C 176.966 0.10 1 234 . 24 ARG CA C 60.160 0.10 1 235 . 24 ARG CB C 29.848 0.10 1 236 . 24 ARG CD C 43.445 0.10 1 237 . 24 ARG CG C 27.879 0.10 1 238 . 24 ARG HA H 3.794 0.05 1 239 . 24 ARG HB2 H 2.042 0.05 2 240 . 24 ARG HD2 H 3.378 0.05 2 241 . 24 ARG HE H 7.450 0.05 1 242 . 24 ARG HG2 H 1.614 0.05 2 243 . 24 ARG HG3 H 1.835 0.05 2 244 . 24 ARG H H 8.794 0.05 1 245 . 24 ARG N N 121.286 0.10 1 246 . 24 ARG NE N 85.774 0.10 1 247 . 25 GLU C C 178.796 0.10 1 248 . 25 GLU CA C 59.037 0.10 1 249 . 25 GLU CB C 29.421 0.10 1 250 . 25 GLU CG C 36.544 0.10 1 251 . 25 GLU HA H 4.034 0.05 1 252 . 25 GLU HB2 H 2.374 0.05 2 253 . 25 GLU HG2 H 2.650 0.05 2 254 . 25 GLU HG3 H 2.420 0.05 2 255 . 25 GLU H H 6.959 0.05 1 256 . 25 GLU N N 114.590 0.10 1 257 . 26 VAL C C 177.161 0.10 1 258 . 26 VAL CA C 64.947 0.10 1 259 . 26 VAL CB C 30.652 0.10 1 260 . 26 VAL CG1 C 21.327 0.20 1 261 . 26 VAL CG2 C 22.445 0.10 1 262 . 26 VAL HA H 2.546 0.05 1 263 . 26 VAL HB H 1.725 0.05 1 264 . 26 VAL H H 6.921 0.05 1 265 . 26 VAL N N 121.223 0.10 1 266 . 26 VAL HG1 H 0.685 0.05 2 267 . 26 VAL HG2 H 0.476 0.05 2 268 . 27 ALA C C 179.512 0.10 1 269 . 27 ALA CA C 55.443 0.10 1 270 . 27 ALA CB C 17.938 0.10 1 271 . 27 ALA HA H 3.764 0.05 1 272 . 27 ALA H H 7.739 0.05 1 273 . 27 ALA N N 121.408 0.10 1 274 . 27 ALA HB H 1.093 0.05 1 275 . 28 LEU C C 178.908 0.10 1 276 . 28 LEU CA C 56.400 0.10 1 277 . 28 LEU CB C 41.710 0.10 1 278 . 28 LEU CD1 C 23.155 0.10 1 279 . 28 LEU CD2 C 25.752 0.10 1 280 . 28 LEU CG C 27.239 0.10 1 281 . 28 LEU HA H 4.504 0.05 1 282 . 28 LEU HB2 H 1.750 0.05 2 283 . 28 LEU HB3 H 1.470 0.05 2 284 . 28 LEU HG H 1.899 0.05 1 285 . 28 LEU H H 7.969 0.05 1 286 . 28 LEU N N 116.595 0.05 1 287 . 28 LEU HD1 H 1.064 0.05 2 288 . 28 LEU HD2 H 0.893 0.05 2 289 . 29 ALA C C 179.310 0.10 1 290 . 29 ALA CA C 54.075 0.10 1 291 . 29 ALA CB C 18.240 0.10 1 292 . 29 ALA HA H 4.170 0.05 1 293 . 29 ALA H H 7.408 0.05 1 294 . 29 ALA N N 122.153 0.05 1 295 . 29 ALA HB H 1.475 0.05 1 296 . 30 PHE C C 178.397 0.10 1 297 . 30 PHE CA C 60.178 0.10 1 298 . 30 PHE CB C 39.847 0.10 1 299 . 30 PHE HA H 4.530 0.05 1 300 . 30 PHE HB2 H 3.369 0.05 2 301 . 30 PHE HB3 H 3.171 0.05 2 302 . 30 PHE H H 7.687 0.05 1 303 . 30 PHE N N 118.401 0.30 1 304 . 31 SER CA C 59.230 0.10 1 305 . 31 SER CB C 64.944 0.10 1 306 . 31 SER HA H 4.683 0.05 1 307 . 31 SER H H 8.303 0.05 1 308 . 31 SER N N 114.908 0.20 1 309 . 32 PRO C C 176.673 0.10 1 310 . 32 PRO CA C 63.523 0.10 1 311 . 32 PRO CB C 31.780 0.10 1 312 . 32 PRO CD C 50.609 0.10 1 313 . 32 PRO CG C 26.283 0.10 1 314 . 32 PRO HA H 4.565 0.05 1 315 . 32 PRO HB2 H 2.189 0.05 2 316 . 32 PRO HB3 H 1.521 0.05 2 317 . 32 PRO HD2 H 3.558 0.05 2 318 . 32 PRO HD3 H 3.503 0.05 2 319 . 32 PRO HG2 H 1.829 0.05 2 320 . 32 PRO HG3 H 1.205 0.05 2 321 . 33 TYR C C 176.386 0.10 1 322 . 33 TYR CA C 57.221 0.10 1 323 . 33 TYR CB C 38.236 0.10 1 324 . 33 TYR HA H 4.595 0.05 1 325 . 33 TYR HB2 H 3.292 0.05 2 326 . 33 TYR HB3 H 2.634 0.05 2 327 . 33 TYR H H 7.310 0.05 1 328 . 33 TYR N N 117.121 0.10 1 329 . 33 TYR HD1 H 7.040 0.05 4 330 . 33 TYR HE1 H 6.959 0.05 4 331 . 34 PHE C C 176.786 0.10 1 332 . 34 PHE CA C 57.270 0.10 1 333 . 34 PHE CB C 39.890 0.10 1 334 . 34 PHE HA H 5.071 0.05 1 335 . 34 PHE HB2 H 3.359 0.05 2 336 . 34 PHE HB3 H 3.006 0.05 2 337 . 34 PHE H H 7.246 0.05 1 338 . 34 PHE N N 121.144 0.10 1 339 . 34 PHE HD1 H 7.287 0.05 4 340 . 34 PHE HE1 H 7.445 0.05 4 341 . 35 THR C C 175.702 0.10 1 342 . 35 THR CA C 60.359 0.10 1 343 . 35 THR CB C 71.586 0.10 1 344 . 35 THR CG2 C 22.143 0.10 1 345 . 35 THR HA H 4.628 0.05 1 346 . 35 THR HB H 4.812 0.05 1 347 . 35 THR H H 9.221 0.05 1 348 . 35 THR N N 115.550 0.05 1 349 . 35 THR HG2 H 1.492 0.05 1 350 . 36 GLN C C 177.935 0.10 1 351 . 36 GLN CA C 59.095 0.10 1 352 . 36 GLN CB C 27.668 0.10 1 353 . 36 GLN CG C 32.750 0.10 1 354 . 36 GLN HA H 4.138 0.05 1 355 . 36 GLN HB2 H 2.077 0.05 2 356 . 36 GLN HB3 H 2.232 0.05 2 357 . 36 GLN HE21 H 7.448 0.05 2 358 . 36 GLN HE22 H 6.563 0.05 2 359 . 36 GLN HG2 H 2.524 0.05 2 360 . 36 GLN HG3 H 2.489 0.05 2 361 . 36 GLN H H 9.028 0.05 1 362 . 36 GLN N N 122.343 0.10 1 363 . 36 GLN NE2 N 111.235 0.10 1 364 . 37 GLU C C 179.087 0.10 1 365 . 37 GLU CA C 60.074 0.10 1 366 . 37 GLU CB C 29.241 0.10 1 367 . 37 GLU CG C 37.130 0.10 1 368 . 37 GLU HA H 4.026 0.05 1 369 . 37 GLU HB2 H 2.066 0.05 2 370 . 37 GLU HB3 H 1.983 0.05 2 371 . 37 GLU HG2 H 2.436 0.05 2 372 . 37 GLU HG3 H 2.332 0.05 2 373 . 37 GLU H H 8.591 0.05 1 374 . 37 GLU N N 118.877 0.10 1 375 . 38 ASP C C 177.928 0.10 1 376 . 38 ASP CA C 57.066 0.10 1 377 . 38 ASP CB C 40.852 0.10 1 378 . 38 ASP HA H 4.257 0.05 1 379 . 38 ASP HB2 H 3.000 0.05 2 380 . 38 ASP HB3 H 2.304 0.05 2 381 . 38 ASP H H 7.770 0.05 1 382 . 38 ASP N N 121.627 0.10 1 383 . 39 ILE C C 177.537 0.10 1 384 . 39 ILE CA C 66.460 0.20 1 385 . 39 ILE CB C 37.997 0.10 1 386 . 39 ILE CD1 C 13.786 0.10 1 387 . 39 ILE CG1 C 30.230 0.10 1 388 . 39 ILE CG2 C 17.613 0.10 1 389 . 39 ILE HA H 3.576 0.05 1 390 . 39 ILE HB H 2.097 0.05 1 391 . 39 ILE HG12 H 0.804 0.05 2 392 . 39 ILE HG13 H 1.982 0.05 2 393 . 39 ILE H H 8.067 0.05 1 394 . 39 ILE N N 122.000 0.10 1 395 . 39 ILE HD1 H 0.909 0.05 1 396 . 39 ILE HG2 H 1.029 0.05 1 397 . 40 VAL C C 177.545 0.10 1 398 . 40 VAL CA C 67.046 0.10 1 399 . 40 VAL CB C 31.875 0.20 1 400 . 40 VAL CG1 C 23.446 0.10 1 401 . 40 VAL CG2 C 21.450 0.10 1 402 . 40 VAL HA H 3.667 0.05 1 403 . 40 VAL HB H 2.140 0.05 1 404 . 40 VAL H H 8.212 0.05 1 405 . 40 VAL N N 121.201 0.10 1 406 . 40 VAL HG1 H 1.151 0.05 2 407 . 40 VAL HG2 H 1.024 0.05 2 408 . 41 LYS C C 179.606 0.10 1 409 . 41 LYS CA C 59.490 0.20 1 410 . 41 LYS CB C 32.181 0.10 1 411 . 41 LYS CD C 28.223 0.10 1 412 . 41 LYS CE C 42.168 0.10 1 413 . 41 LYS CG C 25.054 0.10 1 414 . 41 LYS HA H 4.147 0.05 1 415 . 41 LYS HB2 H 1.909 0.05 2 416 . 41 LYS HD2 H 1.721 0.05 2 417 . 41 LYS HE2 H 2.992 0.05 2 418 . 41 LYS HG2 H 1.456 0.05 2 419 . 41 LYS HG3 H 1.598 0.05 2 420 . 41 LYS H H 7.651 0.05 1 421 . 41 LYS N N 120.489 0.10 1 422 . 42 PHE C C 177.406 0.10 1 423 . 42 PHE CA C 58.770 0.10 1 424 . 42 PHE CB C 39.048 0.10 1 425 . 42 PHE HA H 4.684 0.05 1 426 . 42 PHE HB2 H 3.419 0.05 2 427 . 42 PHE H H 8.219 0.05 1 428 . 42 PHE N N 120.716 0.20 1 429 . 43 PHE C C 176.836 0.10 1 430 . 43 PHE CA C 62.221 0.10 1 431 . 43 PHE CB C 39.707 0.10 1 432 . 43 PHE HA H 3.144 0.05 1 433 . 43 PHE HB2 H 3.364 0.05 2 434 . 43 PHE HB3 H 2.974 0.05 2 435 . 43 PHE H H 8.756 0.05 1 436 . 43 PHE N N 121.387 0.10 1 437 . 43 PHE HD1 H 6.841 0.05 4 438 . 43 PHE HE1 H 6.972 0.05 4 439 . 44 GLU C C 178.965 0.10 1 440 . 44 GLU CA C 59.134 0.10 1 441 . 44 GLU CB C 29.666 0.10 1 442 . 44 GLU CG C 37.045 0.10 1 443 . 44 GLU HA H 4.040 0.05 1 444 . 44 GLU HB2 H 2.286 0.05 2 445 . 44 GLU HB3 H 2.131 0.05 2 446 . 44 GLU HG2 H 2.854 0.05 2 447 . 44 GLU HG3 H 2.460 0.05 2 448 . 44 GLU H H 8.533 0.05 1 449 . 44 GLU N N 116.746 0.10 1 450 . 45 GLU C C 178.466 0.10 1 451 . 45 GLU CA C 58.696 0.10 1 452 . 45 GLU CB C 29.699 0.10 1 453 . 45 GLU CG C 36.313 0.10 1 454 . 45 GLU HA H 4.028 0.05 1 455 . 45 GLU HB2 H 2.327 0.05 2 456 . 45 GLU HB3 H 2.154 0.05 2 457 . 45 GLU HG2 H 2.475 0.05 2 458 . 45 GLU HG3 H 2.286 0.05 2 459 . 45 GLU H H 7.746 0.05 1 460 . 45 GLU N N 119.517 0.10 1 461 . 46 ILE C C 176.862 0.10 1 462 . 46 ILE CA C 62.585 0.10 1 463 . 46 ILE CB C 37.916 0.10 1 464 . 46 ILE CD1 C 15.019 0.10 1 465 . 46 ILE CG1 C 27.713 0.20 1 466 . 46 ILE CG2 C 19.773 0.10 1 467 . 46 ILE HA H 3.903 0.05 1 468 . 46 ILE HB H 1.538 0.05 1 469 . 46 ILE HG12 H 1.029 0.05 2 470 . 46 ILE HG13 H 1.539 0.05 2 471 . 46 ILE H H 7.607 0.05 1 472 . 46 ILE N N 118.394 0.20 1 473 . 46 ILE HD1 H 0.476 0.05 1 474 . 46 ILE HG2 H 0.836 0.05 1 475 . 47 ASP C C 177.553 0.10 1 476 . 47 ASP CA C 52.685 0.10 1 477 . 47 ASP CB C 38.618 0.10 1 478 . 47 ASP HA H 4.391 0.05 1 479 . 47 ASP HB2 H 2.649 0.05 2 480 . 47 ASP HB3 H 1.741 0.05 2 481 . 47 ASP H H 7.659 0.05 1 482 . 47 ASP N N 121.794 0.10 1 483 . 48 VAL C C 178.015 0.10 1 484 . 48 VAL CA C 65.800 0.10 1 485 . 48 VAL CB C 32.182 0.10 1 486 . 48 VAL CG1 C 21.525 0.10 1 487 . 48 VAL CG2 C 21.772 0.10 1 488 . 48 VAL HA H 3.806 0.05 1 489 . 48 VAL HB H 2.172 0.05 1 490 . 48 VAL H H 8.039 0.05 1 491 . 48 VAL N N 126.600 0.20 1 492 . 48 VAL HG1 H 1.145 0.05 2 493 . 48 VAL HG2 H 1.044 0.05 2 494 . 49 ASP C C 177.926 0.05 1 495 . 49 ASP CA C 53.245 0.05 1 496 . 49 ASP CB C 39.622 0.05 1 497 . 49 ASP HA H 4.656 0.05 1 498 . 49 ASP HB2 H 3.123 0.05 2 499 . 49 ASP HB3 H 2.685 0.05 2 500 . 49 ASP H H 8.005 0.05 1 501 . 49 ASP N N 117.223 0.10 1 502 . 50 GLY C C 175.086 0.10 1 503 . 50 GLY CA C 47.259 0.10 1 504 . 50 GLY HA2 H 3.899 0.05 2 505 . 50 GLY H H 7.858 0.05 1 506 . 50 GLY N N 110.188 0.10 1 507 . 51 ASN C C 176.980 0.10 1 508 . 51 ASN CA C 52.503 0.10 1 509 . 51 ASN CB C 38.124 0.10 1 510 . 51 ASN HA H 4.716 0.05 1 511 . 51 ASN HB2 H 3.368 0.05 2 512 . 51 ASN HB3 H 2.628 0.05 2 513 . 51 ASN HD21 H 6.894 0.05 2 514 . 51 ASN HD22 H 7.904 0.05 2 515 . 51 ASN H H 8.128 0.05 1 516 . 51 ASN N N 119.915 0.10 1 517 . 51 ASN ND2 N 116.020 0.10 1 518 . 52 GLY C C 172.855 0.10 1 519 . 52 GLY CA C 46.056 0.10 1 520 . 52 GLY HA2 H 3.741 0.05 2 521 . 52 GLY HA3 H 4.282 0.05 2 522 . 52 GLY H H 10.961 0.05 1 523 . 52 GLY N N 115.144 0.10 1 524 . 53 GLU C C 174.357 0.10 1 525 . 53 GLU CA C 53.836 0.10 1 526 . 53 GLU CB C 33.310 0.10 1 527 . 53 GLU CG C 34.998 0.10 1 528 . 53 GLU HA H 5.064 0.05 1 529 . 53 GLU HB2 H 1.975 0.05 2 530 . 53 GLU HB3 H 1.773 0.05 2 531 . 53 GLU HG2 H 2.179 0.05 2 532 . 53 GLU HG3 H 2.022 0.05 2 533 . 53 GLU H H 7.686 0.05 1 534 . 53 GLU N N 116.758 0.10 1 535 . 54 LEU C C 177.451 0.10 1 536 . 54 LEU CA C 52.732 0.10 1 537 . 54 LEU CB C 42.116 0.10 1 538 . 54 LEU CD1 C 21.436 0.10 1 539 . 54 LEU CD2 C 26.517 0.10 1 540 . 54 LEU CG C 26.270 0.10 1 541 . 54 LEU HA H 5.622 0.05 1 542 . 54 LEU HB2 H 2.158 0.05 2 543 . 54 LEU HB3 H 1.425 0.05 2 544 . 54 LEU HG H 1.547 0.05 1 545 . 54 LEU H H 9.642 0.05 1 546 . 54 LEU N N 125.227 0.10 1 547 . 54 LEU HD1 H -0.036 0.05 2 548 . 54 LEU HD2 H 0.574 0.05 2 549 . 55 ASN C C 175.125 0.10 1 550 . 55 ASN CA C 51.000 0.10 1 551 . 55 ASN CB C 38.928 0.10 1 552 . 55 ASN HA H 5.226 0.05 1 553 . 55 ASN HB2 H 3.515 0.05 2 554 . 55 ASN HB3 H 2.962 0.05 2 555 . 55 ASN HD21 H 7.122 0.05 2 556 . 55 ASN HD22 H 7.440 0.05 2 557 . 55 ASN H H 8.632 0.05 1 558 . 55 ASN N N 123.279 0.10 1 559 . 55 ASN ND2 N 112.614 0.10 1 560 . 56 ALA C C 180.149 0.10 1 561 . 56 ALA CA C 56.021 0.10 1 562 . 56 ALA CB C 17.672 0.10 1 563 . 56 ALA HA H 3.240 0.05 1 564 . 56 ALA H H 8.657 0.05 1 565 . 56 ALA N N 122.129 0.10 1 566 . 56 ALA HB H 0.936 0.05 1 567 . 57 ASP C C 179.089 0.10 1 568 . 57 ASP CA C 57.622 0.10 1 569 . 57 ASP CB C 40.387 0.10 1 570 . 57 ASP HA H 4.383 0.05 1 571 . 57 ASP HB2 H 2.740 0.05 2 572 . 57 ASP H H 8.113 0.05 1 573 . 57 ASP N N 121.289 0.10 1 574 . 58 GLU C C 179.679 0.10 1 575 . 58 GLU CA C 58.930 0.10 1 576 . 58 GLU CB C 29.886 0.10 1 577 . 58 GLU CG C 37.069 0.10 1 578 . 58 GLU HA H 4.115 0.05 1 579 . 58 GLU HB2 H 2.351 0.05 2 580 . 58 GLU HB3 H 2.425 0.05 2 581 . 58 GLU HG2 H 2.865 0.05 2 582 . 58 GLU HG3 H 2.361 0.05 2 583 . 58 GLU H H 8.711 0.05 1 584 . 58 GLU N N 122.726 0.10 1 585 . 59 PHE C C 176.869 0.10 1 586 . 59 PHE CA C 61.948 0.10 1 587 . 59 PHE CB C 40.987 0.10 1 588 . 59 PHE HA H 4.196 0.05 1 589 . 59 PHE HB2 H 3.249 0.05 2 590 . 59 PHE HB3 H 3.258 0.05 2 591 . 59 PHE H H 8.496 0.05 1 592 . 59 PHE N N 118.797 0.10 1 593 . 59 PHE HE1 H 7.178 0.05 4 594 . 60 THR C C 176.173 0.10 1 595 . 60 THR CA C 66.898 0.10 1 596 . 60 THR CB C 68.630 0.10 1 597 . 60 THR CG2 C 21.740 0.10 1 598 . 60 THR HA H 3.749 0.05 1 599 . 60 THR HB H 4.388 0.05 1 600 . 60 THR H H 8.826 0.05 1 601 . 60 THR N N 115.281 0.10 1 602 . 60 THR HG2 H 1.351 0.05 1 603 . 61 SER C C 175.790 0.10 1 604 . 61 SER CA C 61.384 0.10 1 605 . 61 SER CB C 63.083 0.10 1 606 . 61 SER HA H 4.301 0.05 1 607 . 61 SER HB2 H 4.019 0.05 2 608 . 61 SER H H 7.839 0.05 1 609 . 61 SER N N 116.463 0.10 1 610 . 62 CYS C C 176.042 0.10 1 611 . 62 CYS CA C 61.035 0.10 1 612 . 62 CYS CB C 27.810 0.10 1 613 . 62 CYS HA H 4.379 0.05 1 614 . 62 CYS HB2 H 2.880 0.05 2 615 . 62 CYS HB3 H 2.839 0.05 2 616 . 62 CYS H H 7.294 0.05 1 617 . 62 CYS N N 119.214 0.10 1 618 . 63 ILE C C 177.807 0.10 1 619 . 63 ILE CA C 62.391 0.10 1 620 . 63 ILE CB C 37.244 0.10 1 621 . 63 ILE CD1 C 12.297 0.10 1 622 . 63 ILE CG1 C 28.220 0.10 1 623 . 63 ILE CG2 C 18.376 0.10 1 624 . 63 ILE HA H 3.837 0.05 1 625 . 63 ILE HB H 1.643 0.05 1 626 . 63 ILE HG12 H 1.068 0.05 2 627 . 63 ILE H H 7.671 0.05 1 628 . 63 ILE N N 119.675 0.10 1 629 . 63 ILE HD1 H 0.657 0.05 1 630 . 63 ILE HG2 H 0.832 0.05 1 631 . 64 GLU C C 178.134 0.10 1 632 . 64 GLU CA C 59.133 0.10 1 633 . 64 GLU CB C 29.380 0.20 1 634 . 64 GLU CG C 36.765 0.10 1 635 . 64 GLU HA H 4.096 0.05 1 636 . 64 GLU HB2 H 2.147 0.05 2 637 . 64 GLU HG2 H 2.390 0.05 2 638 . 64 GLU H H 8.206 0.05 1 639 . 64 GLU N N 120.206 0.10 1 640 . 65 LYS C C 177.219 0.10 1 641 . 65 LYS CA C 57.467 0.10 1 642 . 65 LYS CB C 32.864 0.20 1 643 . 65 LYS CD C 29.359 0.10 1 644 . 65 LYS CE C 42.231 0.10 1 645 . 65 LYS CG C 25.314 0.10 1 646 . 65 LYS HA H 4.360 0.05 1 647 . 65 LYS HB2 H 1.992 0.05 2 648 . 65 LYS HD2 H 1.739 0.05 2 649 . 65 LYS HE2 H 3.067 0.05 2 650 . 65 LYS HG2 H 1.570 0.05 2 651 . 65 LYS H H 7.577 0.05 1 652 . 65 LYS N N 117.359 0.10 1 653 . 66 MET C C 175.099 0.10 1 654 . 66 MET CA C 56.222 0.10 1 655 . 66 MET CB C 34.043 0.10 1 656 . 66 MET CG C 32.352 0.20 1 657 . 66 MET HA H 4.444 0.05 1 658 . 66 MET HB2 H 2.098 0.05 2 659 . 66 MET HB3 H 2.022 0.05 2 660 . 66 MET HG2 H 2.505 0.05 2 661 . 66 MET HG3 H 2.413 0.05 2 662 . 66 MET H H 7.869 0.05 1 663 . 66 MET N N 119.284 0.10 1 664 . 67 LEU CA C 56.427 0.10 1 665 . 67 LEU CB C 43.465 0.10 1 666 . 67 LEU HA H 4.293 0.05 1 667 . 67 LEU HB2 H 1.722 0.05 2 668 . 67 LEU HB3 H 1.674 0.05 2 669 . 67 LEU HG H 0.880 0.05 1 670 . 67 LEU H H 7.276 0.05 1 671 . 67 LEU N N 126.258 0.20 1 stop_ loop_ _Atom_shift_assign_ID_ambiguity 57,56 232,231 330,329 340,339 438,437 593 stop_ save_ save_residual_dipolar_couplings _Saveframe_category residual_dipolar_couplings loop_ _Sample_label $sample_1 stop_ _Details . _Sample_conditions_label $Conditions_1 _Spectrometer_frequency_1H . _Text_data_format . _Text_data . loop_ _Residual_dipolar_coupling_ID _Atom_one_residue_seq_code _Atom_one_residue_label _Atom_one_atom_name _Atom_two_residue_seq_code _Atom_two_residue_label _Atom_two_atom_name _Residual_dipolar_coupling_value _Atom_one_mol_system_component_name _Atom_two_mol_system_component_name _Residual_dipolar_coupling_min_value _Residual_dipolar_coupling_max_value _Residual_dipolar_coupling_value_error 1DHN 3 ALA H 3 ALA N 4.47 ? ? . . . 1DHN 4 LYS H 4 LYS N 14.86 ? ? . . . 1DHN 5 ARG H 5 ARG N 10.19 ? ? . . . 1DHN 6 VAL H 6 VAL N 9.47 ? ? . . . 1DHN 7 PHE H 7 PHE N 11.36 ? ? . . . 1DHN 8 GLU H 8 GLU N 12.76 ? ? . . . 1DHN 9 LYS H 9 LYS N 12.14 ? ? . . . 1DHN 10 PHE H 10 PHE N 7.29 ? ? . . . 1DHN 11 ASP H 11 ASP N 17.93 ? ? . . . 1DHN 12 LYS H 12 LYS N 9.37 ? ? . . . 1DHN 13 ASN H 13 ASN N 15.48 ? ? . . . 1DHN 14 LYS H 14 LYS N -26 ? ? . . . 1DHN 15 ASP H 15 ASP N -18.3 ? ? . . . 1DHN 16 GLY H 16 GLY N -23.66 ? ? . . . 1DHN 17 LYS H 17 LYS N 4.26 ? ? . . . 1DHN 18 LEU H 18 LEU N 3.46 ? ? . . . 1DHN 20 LEU H 20 LEU N -6.82 ? ? . . . 1DHN 21 ASP H 21 ASP N -18.59 ? ? . . . 1DHN 22 GLU H 22 GLU N -21.11 ? ? . . . 1DHN 23 PHE H 23 PHE N -8.15 ? ? . . . 1DHN 24 ARG H 24 ARG N -4.63 ? ? . . . 1DHN 25 GLU H 25 GLU N -29.38 ? ? . . . 1DHN 26 VAL H 26 VAL N -12.97 ? ? . . . 1DHN 28 LEU H 28 LEU N -12.66 ? ? . . . 1DHN 29 ALA H 29 ALA N -33.44 ? ? . . . 1DHN 31 SER H 31 SER N -10.95 ? ? . . . 1DHN 33 TYR H 33 TYR N 17.51 ? ? . . . 1DHN 35 THR H 35 THR N 10.27 ? ? . . . 1DHN 36 GLN H 36 GLN N -10.6 ? ? . . . 1DHN 37 GLU H 37 GLU N -25.98 ? ? . . . 1DHN 39 ILE H 39 ILE N -8.64 ? ? . . . 1DHN 40 VAL H 40 VAL N -14.82 ? ? . . . 1DHN 41 LYS H 41 LYS N -27.9 ? ? . . . 1DHN 42 PHE H 42 PHE N -23.8 ? ? . . . 1DHN 43 PHE H 43 PHE N -14 ? ? . . . 1DHN 44 GLU H 44 GLU N -21.12 ? ? . . . 1DHN 46 ILE H 46 ILE N -10.43 ? ? . . . 1DHN 47 ASP H 47 ASP N -9.36 ? ? . . . 1DHN 48 VAL H 48 VAL N 20.44 ? ? . . . 1DHN 50 GLY H 50 GLY N -7.02 ? ? . . . 1DHN 51 ASN H 51 ASN N 17.7 ? ? . . . 1DHN 52 GLY H 52 GLY N 5.32 ? ? . . . 1DHN 53 GLU H 53 GLU N -10.95 ? ? . . . 1DHN 54 LEU H 54 LEU N -5.93 ? ? . . . 1DHN 55 ASN H 55 ASN N 11.96 ? ? . . . 1DHN 56 ALA H 56 ALA N -13.89 ? ? . . . 1DHN 57 ASP H 57 ASP N -14.82 ? ? . . . 1DHN 58 GLU H 58 GLU N -4.66 ? ? . . . 1DHN 59 PHE H 59 PHE N -13.98 ? ? . . . 1DHN 60 THR H 60 THR N -25.14 ? ? . . . 1DHN 62 CYS H 62 CYS N -1.05 ? ? . . . 1DHN 64 GLU H 64 GLU N -22.7 ? ? . . . 1DHN 65 LYS H 65 LYS N 0.8 ? ? . . . 1DHN 66 MET H 66 MET N -11.47 ? ? . . . 1DHN 67 LEU H 67 LEU N -21.21 ? ? . . . stop_ save_