data_19817 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; NMR structure of the dilated cardiomyopathy mutation G159D in troponin C bound to the anchoring region of troponin I ; _BMRB_accession_number 19817 _BMRB_flat_file_name bmr19817.str _Entry_type original _Submission_date 2014-02-26 _Accession_date 2014-02-26 _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 Baryshnikova Olga K. . 2 Robertson Ian M. . 3 Mercier Pascal . . 4 Sykes Brian D. . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 370 "13C chemical shifts" 219 "15N chemical shifts" 75 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2014-03-10 original author . stop_ loop_ _Related_BMRB_accession_number _Relationship 19816 'C-domain of troponin C bound to the anchoring region of troponin I' stop_ _Original_release_date 2014-03-10 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title 'The dilated cardiomyopathy G159D mutation in cardiac troponin C weakens the anchoring interaction with troponin I.' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 18803402 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Baryshnikova Olga K. . 2 Robertson Ian M. . 3 Mercier Pascal . . 4 Sykes Brian D. . stop_ _Journal_abbreviation Biochemistry _Journal_volume 47 _Journal_issue 41 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 10950 _Page_last 10960 _Year 2008 _Details . save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name 'mutation G159D in troponin C bound to the anchoring region of troponin I' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label cCTnC $cCTnC Calcium_1 $entity_CA Calcium_2 $entity_CA stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state ? _System_paramagnetic no _System_thiol_state . _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_cCTnC _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common cCTnC _Molecular_mass 8427.296 _Mol_thiol_state 'not present' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 72 _Mol_residue_sequence ; MGKSEEELSDLFRMFDKNAD GYIDLDELKIMLQATGETIT EDDIEELMKDGDKNNDGRID YDEFLEFMKDVE ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 90 MET 2 91 GLY 3 92 LYS 4 93 SER 5 94 GLU 6 95 GLU 7 96 GLU 8 97 LEU 9 98 SER 10 99 ASP 11 100 LEU 12 101 PHE 13 102 ARG 14 103 MET 15 104 PHE 16 105 ASP 17 106 LYS 18 107 ASN 19 108 ALA 20 109 ASP 21 110 GLY 22 111 TYR 23 112 ILE 24 113 ASP 25 114 LEU 26 115 ASP 27 116 GLU 28 117 LEU 29 118 LYS 30 119 ILE 31 120 MET 32 121 LEU 33 122 GLN 34 123 ALA 35 124 THR 36 125 GLY 37 126 GLU 38 127 THR 39 128 ILE 40 129 THR 41 130 GLU 42 131 ASP 43 132 ASP 44 133 ILE 45 134 GLU 46 135 GLU 47 136 LEU 48 137 MET 49 138 LYS 50 139 ASP 51 140 GLY 52 141 ASP 53 142 LYS 54 143 ASN 55 144 ASN 56 145 ASP 57 146 GLY 58 147 ARG 59 148 ILE 60 149 ASP 61 150 TYR 62 151 ASP 63 152 GLU 64 153 PHE 65 154 LEU 66 155 GLU 67 156 PHE 68 157 MET 69 158 LYS 70 159 ASP 71 160 VAL 72 161 GLU stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-11-25 loop_ _Database_name _Database_accession_code _Database_entry_mol_name _Sequence_query_to_submitted_percentage _Sequence_subject_length _Sequence_identity _Sequence_positive _Sequence_homology_expectation_value BMRB 15385 F104W 98.61 161 97.18 98.59 2.34e-37 BMRB 15388 F153W 98.61 161 97.18 98.59 2.34e-37 BMRB 15400 F153(FTR) 98.61 161 97.18 97.18 9.64e-37 BMRB 15427 F104(FTR) 98.61 161 97.18 98.59 2.34e-37 BMRB 17243 cCTnC 100.00 72 98.61 98.61 2.85e-39 BMRB 17440 CcTnC 100.00 72 98.61 98.61 2.85e-39 BMRB 19816 cCTnC 100.00 72 98.61 98.61 2.85e-39 BMRB 25120 cTnC 98.61 161 98.59 98.59 6.41e-38 PDB 1DTL "Crystal Structure Of Calcium-Saturated (3ca2+) Cardiac Troponin C Complexed With The Calcium Sensitizer Bepridil At 2.15 A Reso" 98.61 161 97.18 98.59 2.13e-37 PDB 1IH0 "Structure Of The C-Domain Of Human Cardiac Troponin C In Complex With Ca2+ Sensitizer Emd 57033" 97.22 71 97.14 98.57 5.34e-37 PDB 1J1D "Crystal Structure Of The 46kda Domain Of Human Cardiac Troponin In The Ca2+ Saturated Form" 98.61 161 97.18 98.59 2.13e-37 PDB 1J1E "Crystal Structure Of The 52kda Domain Of Human Cardiac Troponin In The Ca2+ Saturated Form" 98.61 161 97.18 98.59 2.13e-37 PDB 1OZS "C-Domain Of Human Cardiac Troponin C In Complex With The Inhibitory Region Of Human Cardiac Troponin I" 98.61 73 97.18 98.59 6.41e-38 PDB 2JT0 "Solution Structure Of F104w Cardiac Troponin C" 98.61 161 97.18 98.59 2.34e-37 PDB 2JT3 "Solution Structure Of F153w Cardiac Troponin C" 98.61 161 97.18 98.59 2.34e-37 PDB 2JT8 "Solution Structure Of The F153-To-5-Flurotryptophan Mutant Of Human Cardiac Troponin C" 98.61 161 97.18 97.18 9.64e-37 PDB 2JTZ "Solution Structure And Chemical Shift Assignments Of The F104-To-5-Flurotryptophan Mutant Of Cardiac Troponin C" 98.61 161 97.18 97.18 9.64e-37 PDB 2KDH "The Solution Structure Of Human Cardiac Troponin C In Complex With The Green Tea Polyphenol; (-)- Epigallocatechin-3-Gallate" 100.00 72 98.61 98.61 2.85e-39 PDB 2L98 "Structure Of Trans-Resveratrol In Complex With The Cardiac Regulatory Protein Troponin C" 100.00 72 98.61 98.61 2.85e-39 PDB 2MLE "Nmr Structure Of The C-domain Of Troponin C Bound To The Anchoring Region Of Troponin I" 100.00 72 98.61 98.61 2.85e-39 PDB 2MLF "Nmr Structure Of The Dilated Cardiomyopathy Mutation G159d In Troponin C Bound To The Anchoring Region Of Troponin I" 100.00 72 100.00 100.00 3.65e-40 DBJ BAG36483 "unnamed protein product [Homo sapiens]" 98.61 161 98.59 98.59 7.06e-38 EMBL CAA30736 "unnamed protein product [Homo sapiens]" 98.61 161 98.59 98.59 7.06e-38 EMBL CAG46663 "TNNC1 [Homo sapiens]" 98.61 161 98.59 98.59 7.06e-38 EMBL CAG46683 "TNNC1 [Homo sapiens]" 98.61 161 98.59 98.59 7.06e-38 GB AAA36772 "slow twitch skeletal/cardiac muscle troponin C [Homo sapiens]" 98.61 161 98.59 98.59 7.06e-38 GB AAA37492 "slow/cardiac troponin C, partial [Mus musculus]" 98.61 161 97.18 98.59 2.34e-37 GB AAA37493 "slow/cardiac troponin C [Mus musculus]" 98.61 161 97.18 98.59 2.34e-37 GB AAB91994 "cardiac ventricular troponin C [Homo sapiens]" 98.61 160 97.18 97.18 1.84e-35 GB AAH30244 "Troponin C type 1 (slow) [Homo sapiens]" 98.61 161 98.59 98.59 7.06e-38 PIR TPHUCC "troponin C, cardiac and slow skeletal muscle - human" 98.61 161 98.59 98.59 7.06e-38 PRF 1510257A "troponin C" 98.61 161 97.18 98.59 2.64e-37 PRF 750650A "troponin c,cardiac" 98.61 161 97.18 98.59 2.64e-37 REF NP_001029277 "troponin C, slow skeletal and cardiac muscles [Rattus norvegicus]" 98.61 161 97.18 98.59 2.34e-37 REF NP_001029523 "troponin C, slow skeletal and cardiac muscles [Bos taurus]" 98.61 161 97.18 98.59 2.64e-37 REF NP_001123715 "troponin C, slow skeletal and cardiac muscles [Sus scrofa]" 98.61 161 97.18 98.59 2.64e-37 REF NP_001272501 "troponin C, slow skeletal and cardiac muscles [Capra hircus]" 98.61 161 97.18 98.59 2.64e-37 REF NP_003271 "troponin C, slow skeletal and cardiac muscles [Homo sapiens]" 98.61 161 98.59 98.59 7.06e-38 SP P02591 "RecName: Full=Troponin C, slow skeletal and cardiac muscles; Short=TN-C" 98.61 161 98.59 98.59 7.06e-38 SP P19123 "RecName: Full=Troponin C, slow skeletal and cardiac muscles; Short=TN-C" 98.61 161 97.18 98.59 2.34e-37 SP P63315 "RecName: Full=Troponin C, slow skeletal and cardiac muscles; Short=TN-C" 98.61 161 97.18 98.59 2.64e-37 SP P63316 "RecName: Full=Troponin C, slow skeletal and cardiac muscles; Short=TN-C" 98.61 161 98.59 98.59 7.06e-38 SP P63317 "RecName: Full=Troponin C, slow skeletal and cardiac muscles; Short=TN-C" 98.61 161 97.18 98.59 2.64e-37 TPG DAA16908 "TPA: troponin C, slow skeletal and cardiac muscles [Bos taurus]" 98.61 161 97.18 98.59 2.64e-37 stop_ save_ ############# # Ligands # ############# save_CA _Saveframe_category ligand _Mol_type "non-polymer (NON-POLYMER)" _Name_common 'CALCIUM ION' _BMRB_code CA _PDB_code CA _Molecular_mass 40.078 _Mol_charge 2 _Mol_paramagnetic . _Mol_aromatic no _Details . loop_ _Atom_name _PDB_atom_name _Atom_type _Atom_chirality _Atom_charge _Atom_oxidation_number _Atom_unpaired_electrons CA CA CA . 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 $cCTnC Human 9606 Eukaryota Metazoa Homo sapiens 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 $cCTnC 'recombinant technology' . Escherichia coli . BL21(DE3)pLysS 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 $cCTnC 0.5 mM '[U-95% 13C; U-95% 15N]' $entity_CA 2 mM 'natural abundance' DSS 0.2 mM 'natural abundance' 'potassium chloride' 100 mM 'natural abundance' 'sodium azide' 5 mM 'natural abundance' imidazole 10 mM 'natural abundance' 'troponin I(34-71)' 1.2 mM 'natural abundance' H2O 90 % 'natural abundance' D2O 10 % 'natural abundance' stop_ save_ save_sample_2 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $cCTnC 0.5 mM '[U-95% 13C; U-95% 15N]' $entity_CA 2 mM 'natural abundance' DSS 0.2 mM 'natural abundance' 'potassium chloride' 100 mM 'natural abundance' 'sodium azide' 5 mM 'natural abundance' imidazole 0.5 mM 'natural abundance' 'troponin I(34-71)' 1.2 mM 'natural abundance' imidazole 9.5 mM [U-2H] D2O 100 % 'natural abundance' stop_ save_ ############################ # Computer software used # ############################ save_CYANA _Saveframe_category software _Name CYANA _Version . loop_ _Vendor _Address _Electronic_address 'Guntert, Mumenthaler and Wuthrich' . . stop_ loop_ _Task 'structure solution' 'geometry optimization' stop_ _Details . save_ save_NMRDraw _Saveframe_category software _Name NMRDraw _Version . loop_ _Vendor _Address _Electronic_address 'Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax' . . stop_ loop_ _Task processing stop_ _Details . save_ save_NMRPipe _Saveframe_category software _Name NMRPipe _Version . loop_ _Vendor _Address _Electronic_address 'Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax' . . stop_ loop_ _Task processing stop_ _Details . save_ save_NMRView _Saveframe_category software _Name NMRView _Version . loop_ _Vendor _Address _Electronic_address 'Johnson, One Moon Scientific' . . stop_ loop_ _Task 'peak picking' 'chemical shift assignment' stop_ _Details . save_ save_ProcheckNMR _Saveframe_category software _Name ProcheckNMR _Version . loop_ _Vendor _Address _Electronic_address 'Laskowski and MacArthur' . . stop_ loop_ _Task refinement stop_ _Details . save_ save_TALOS _Saveframe_category software _Name TALOS _Version . loop_ _Vendor _Address _Electronic_address 'Cornilescu, Delaglio and Bax' . . stop_ loop_ _Task 'data analysis' refinement stop_ _Details . save_ save_X-PLOR_NIH _Saveframe_category software _Name X-PLOR_NIH _Version . loop_ _Vendor _Address _Electronic_address 'Schwieters, Kuszewski, Tjandra and Clore' . . stop_ loop_ _Task refinement stop_ _Details . save_ save_VNMRJ _Saveframe_category software _Name VNMRJ _Version . loop_ _Vendor _Address _Electronic_address Varian . . stop_ loop_ _Task 'data analysis' stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model INOVA _Field_strength 500 _Details . save_ save_spectrometer_2 _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model Unity _Field_strength 600 _Details . save_ save_spectrometer_3 _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model INOVA _Field_strength 800 _Details . save_ ############################# # NMR applied experiments # ############################# save_2D_1H-15N_HSQC_1 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-15N HSQC' _Sample_label $sample_1 save_ save_3D_HCCH-TOCSY_2 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HCCH-TOCSY' _Sample_label $sample_1 save_ save_3D_CBCA(CO)NH_3 _Saveframe_category NMR_applied_experiment _Experiment_name '3D CBCA(CO)NH' _Sample_label $sample_1 save_ save_3D_HNCACB_4 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCACB' _Sample_label $sample_1 save_ save_3D_H(CCO)NH_5 _Saveframe_category NMR_applied_experiment _Experiment_name '3D H(CCO)NH' _Sample_label $sample_1 save_ save_3D_C(CO)NH_6 _Saveframe_category NMR_applied_experiment _Experiment_name '3D C(CO)NH' _Sample_label $sample_1 save_ save_3D_1H-13C_NOESY_7 _Saveframe_category NMR_applied_experiment _Experiment_name '3D 1H-13C NOESY' _Sample_label $sample_1 save_ save_3D_1H-15N_NOESY_8 _Saveframe_category NMR_applied_experiment _Experiment_name '3D 1H-15N NOESY' _Sample_label $sample_1 save_ save_3D_1H-15N_TOCSY_9 _Saveframe_category NMR_applied_experiment _Experiment_name '3D 1H-15N TOCSY' _Sample_label $sample_1 save_ save_3D_HNHA_10 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNHA' _Sample_label $sample_1 save_ save_3D_HNHB_11 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNHB' _Sample_label $sample_1 save_ save_2D_DQF-COSY_12 _Saveframe_category NMR_applied_experiment _Experiment_name '2D DQF-COSY' _Sample_label $sample_2 save_ save_2D_1H-1H_NOESY_13 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-1H NOESY' _Sample_label $sample_2 save_ save_2D_13C-15N_Filtered_1H-1H_TOCSY_14 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 13C-15N Filtered 1H-1H TOCSY' _Sample_label $sample_1 save_ save_2D_13C-15N_Filtered_1H-1H_NOESY_15 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 13C-15N Filtered 1H-1H NOESY' _Sample_label $sample_1 save_ save_2D_13C_Edited,Filtered_NOESY_16 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 13C Edited,Filtered NOESY' _Sample_label $sample_1 save_ ####################### # Sample conditions # ####################### save_sample_conditions_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units temperature 273 . K pH 6.7 . pH pressure 1 . atm 'ionic strength' 0.12 . M stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference_1 _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 internal direct . . . 1 DSS C 13 'methyl protons' ppm 0 internal indirect . . . 0.25144953 DSS N 15 'methyl protons' ppm 0 internal 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_assigned_chem_shift_list_1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Experiment_label '2D 1H-15N HSQC' '3D HCCH-TOCSY' '3D CBCA(CO)NH' '3D HNCACB' '3D H(CCO)NH' '3D C(CO)NH' '3D 1H-15N TOCSY' '3D HNHA' '3D HNHB' '2D DQF-COSY' '2D 1H-1H NOESY' stop_ loop_ _Sample_label $sample_1 $sample_2 stop_ _Sample_conditions_label $sample_conditions_1 _Chem_shift_reference_set_label $chemical_shift_reference_1 _Mol_system_component_name cCTnC _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 90 1 MET HA H 3.3200 0.05 1 2 90 1 MET HB2 H 2.0200 0.05 1 3 90 1 MET HB3 H 1.6900 0.05 1 4 90 1 MET HG2 H 2.3300 0.05 1 5 90 1 MET CB C 25.9200 0.30 1 6 90 1 MET N N 122.8500 0.50 1 7 91 2 GLY CA C 45.0000 0.30 1 8 92 3 LYS H H 8.6100 0.05 1 9 92 3 LYS HA H 4.4300 0.05 1 10 92 3 LYS HB2 H 1.4800 0.05 1 11 92 3 LYS HB3 H 1.7800 0.05 1 12 92 3 LYS HG3 H 2.1000 0.05 2 13 92 3 LYS HD2 H 1.5900 0.05 2 14 92 3 LYS HE2 H 3.0100 0.05 2 15 92 3 LYS CA C 56.0000 0.30 1 16 92 3 LYS CB C 33.8000 0.30 1 17 92 3 LYS CG C 25.0000 0.30 1 18 92 3 LYS CD C 28.8000 0.30 1 19 92 3 LYS CE C 42.5000 0.30 1 20 92 3 LYS N N 121.1000 0.50 1 21 93 4 SER H H 8.7600 0.05 1 22 93 4 SER HA H 4.4700 0.05 1 23 93 4 SER HB2 H 4.2800 0.05 1 24 93 4 SER HB3 H 4.0600 0.05 2 25 93 4 SER CA C 58.1000 0.30 1 26 93 4 SER CB C 65.0000 0.30 1 27 93 4 SER N N 117.1900 0.50 1 28 94 5 GLU H H 8.8900 0.05 1 29 94 5 GLU HA H 4.0000 0.05 1 30 94 5 GLU HB2 H 2.0900 0.05 2 31 94 5 GLU HG2 H 2.4000 0.05 2 32 94 5 GLU CA C 60.0000 0.30 1 33 94 5 GLU CB C 29.1000 0.30 1 34 94 5 GLU CG C 36.8000 0.30 1 35 94 5 GLU N N 122.3500 0.50 1 36 95 6 GLU H H 8.6100 0.05 1 37 95 6 GLU HA H 4.0900 0.05 1 38 95 6 GLU HB2 H 2.0400 0.05 2 39 95 6 GLU HG2 H 2.3500 0.05 2 40 95 6 GLU CA C 59.7000 0.30 1 41 95 6 GLU CB C 29.2000 0.30 1 42 95 6 GLU CG C 36.8000 0.30 1 43 95 6 GLU N N 119.1600 0.50 1 44 96 7 GLU H H 7.9300 0.05 1 45 96 7 GLU HA H 4.2900 0.05 1 46 96 7 GLU HB2 H 2.2600 0.05 2 47 96 7 GLU HB3 H 2.1000 0.05 2 48 96 7 GLU HG2 H 2.2900 0.05 1 49 96 7 GLU HG3 H 2.4100 0.05 1 50 96 7 GLU CA C 59.0000 0.30 1 51 96 7 GLU CB C 30.2000 0.30 1 52 96 7 GLU CG C 37.1000 0.30 1 53 96 7 GLU N N 120.3000 0.50 1 54 97 8 LEU H H 8.5200 0.05 1 55 97 8 LEU HA H 4.2700 0.05 1 56 97 8 LEU HB2 H 2.1100 0.05 2 57 97 8 LEU HB3 H 1.5600 0.05 2 58 97 8 LEU HG H 1.7800 0.05 1 59 97 8 LEU HD1 H 0.8500 0.05 2 60 97 8 LEU HD2 H 0.8200 0.05 2 61 97 8 LEU CA C 58.5000 0.30 1 62 97 8 LEU CB C 41.9000 0.30 1 63 97 8 LEU CG C 27.0050 0.30 1 64 97 8 LEU CD1 C 23.2000 0.30 2 65 97 8 LEU CD2 C 26.1000 0.30 2 66 97 8 LEU N N 119.3400 0.50 1 67 98 9 SER H H 8.7000 0.05 1 68 98 9 SER HA H 4.2800 0.05 1 69 98 9 SER HB2 H 4.0900 0.05 2 70 98 9 SER CA C 62.3000 0.30 1 71 98 9 SER CB C 62.5000 0.30 1 72 98 9 SER N N 115.8000 0.50 1 73 99 10 ASP H H 7.5100 0.05 1 74 99 10 ASP HA H 4.7000 0.05 1 75 99 10 ASP HB2 H 2.8400 0.05 2 76 99 10 ASP CA C 58.5000 0.30 1 77 99 10 ASP CB C 41.4000 0.30 1 78 99 10 ASP N N 121.6000 0.50 1 79 100 11 LEU H H 8.1700 0.05 1 80 100 11 LEU HA H 4.1500 0.05 1 81 100 11 LEU HB2 H 1.6300 0.05 1 82 100 11 LEU HB3 H 2.3200 0.05 1 83 100 11 LEU HD1 H 0.9800 0.05 2 84 100 11 LEU HD2 H 1.0900 0.05 2 85 100 11 LEU CA C 58.3000 0.30 1 86 100 11 LEU CB C 41.6000 0.30 1 87 100 11 LEU CG C 26.5000 0.30 1 88 100 11 LEU CD1 C 23.4000 0.30 1 89 100 11 LEU CD2 C 26.5000 0.30 1 90 100 11 LEU N N 117.9000 0.50 1 91 101 12 PHE H H 8.7600 0.05 1 92 101 12 PHE HA H 4.2700 0.05 1 93 101 12 PHE HB2 H 3.1700 0.05 2 94 101 12 PHE HB3 H 2.8600 0.05 2 95 101 12 PHE HD1 H 6.3800 0.05 3 96 101 12 PHE HE1 H 6.8800 0.05 3 97 101 12 PHE CA C 62.2000 0.30 1 98 101 12 PHE CB C 39.2000 0.30 1 99 101 12 PHE N N 120.4900 0.50 1 100 102 13 ARG H H 7.4700 0.05 1 101 102 13 ARG HA H 3.9700 0.05 1 102 102 13 ARG HB2 H 2.0400 0.05 2 103 102 13 ARG HB3 H 2.1200 0.05 2 104 102 13 ARG HG2 H 2.0300 0.05 2 105 102 13 ARG HG3 H 1.6900 0.05 2 106 102 13 ARG HD2 H 3.3200 0.05 2 107 102 13 ARG CA C 59.2000 0.30 1 108 102 13 ARG CB C 30.4000 0.30 1 109 102 13 ARG CG C 28.6000 0.30 1 110 102 13 ARG CD C 43.4000 0.30 1 111 102 13 ARG N N 115.5200 0.50 1 112 103 14 MET H H 7.5900 0.05 1 113 103 14 MET HA H 4.3700 0.05 1 114 103 14 MET HB2 H 2.4000 0.05 1 115 103 14 MET HB3 H 1.8400 0.05 1 116 103 14 MET HG2 H 3.2200 0.05 1 117 103 14 MET HG3 H 2.6600 0.05 1 118 103 14 MET HE H 2.0100 0.05 1 119 103 14 MET CA C 55.9000 0.30 1 120 103 14 MET CB C 34.3000 0.30 1 121 103 14 MET CG C 32.5000 0.30 1 122 103 14 MET CE C 20.1000 0.30 1 123 103 14 MET N N 114.1500 0.50 1 124 104 15 PHE H H 7.3800 0.05 1 125 104 15 PHE HA H 4.2900 0.05 1 126 104 15 PHE HB2 H 2.8100 0.05 1 127 104 15 PHE HB3 H 2.5600 0.05 1 128 104 15 PHE HD2 H 7.4700 0.05 3 129 104 15 PHE HE2 H 7.2400 0.05 3 130 104 15 PHE HZ H 7.1700 0.05 1 131 104 15 PHE CA C 59.4000 0.30 1 132 104 15 PHE CB C 41.7000 0.30 1 133 104 15 PHE N N 115.0600 0.50 1 134 105 16 ASP H H 7.2700 0.05 1 135 105 16 ASP HA H 4.4200 0.05 1 136 105 16 ASP HB2 H 2.3500 0.05 1 137 105 16 ASP HB3 H 1.4700 0.05 1 138 105 16 ASP CA C 52.4000 0.30 1 139 105 16 ASP CB C 39.0000 0.30 1 140 105 16 ASP N N 116.7100 0.50 1 141 106 17 LYS H H 7.5100 0.05 1 142 106 17 LYS HA H 4.0300 0.05 1 143 106 17 LYS HB2 H 1.8900 0.05 2 144 106 17 LYS HG2 H 1.6400 0.05 2 145 106 17 LYS HD2 H 1.6700 0.05 2 146 106 17 LYS HE2 H 3.0400 0.05 2 147 106 17 LYS CA C 58.2000 0.30 1 148 106 17 LYS CB C 32.9000 0.30 1 149 106 17 LYS CG C 24.9000 0.30 1 150 106 17 LYS CD C 28.2000 0.30 1 151 106 17 LYS CE C 42.7000 0.30 1 152 106 17 LYS N N 124.2700 0.50 1 153 107 18 ASN H H 8.0000 0.05 1 154 107 18 ASN HA H 4.7300 0.05 1 155 107 18 ASN HB2 H 3.2900 0.05 1 156 107 18 ASN HB3 H 2.8600 0.05 1 157 107 18 ASN HD21 H 7.8580 0.05 2 158 107 18 ASN HD22 H 6.6910 0.05 2 159 107 18 ASN CA C 51.7000 0.30 1 160 107 18 ASN CB C 36.9000 0.30 1 161 107 18 ASN N N 113.6000 0.50 1 162 107 18 ASN ND2 N 112.4800 0.50 1 163 108 19 ALA H H 7.8100 0.05 1 164 108 19 ALA HA H 4.0700 0.05 1 165 108 19 ALA HB H 1.3800 0.05 1 166 108 19 ALA CA C 53.3000 0.30 1 167 108 19 ALA CB C 17.1000 0.30 1 168 108 19 ALA N N 121.6000 0.50 1 169 109 20 ASP H H 8.5200 0.05 1 170 109 20 ASP HA H 4.7000 0.05 1 171 109 20 ASP HB2 H 3.2000 0.05 1 172 109 20 ASP HB3 H 2.4500 0.05 1 173 109 20 ASP CA C 53.2000 0.30 1 174 109 20 ASP CB C 41.0000 0.30 1 175 109 20 ASP N N 118.4800 0.50 1 176 110 21 GLY H H 10.4000 0.05 1 177 110 21 GLY HA2 H 4.0600 0.05 1 178 110 21 GLY HA3 H 3.4400 0.05 1 179 110 21 GLY CA C 45.0000 0.30 1 180 110 21 GLY N N 112.2500 0.50 1 181 111 22 TYR H H 8.0000 0.05 1 182 111 22 TYR HA H 5.1700 0.05 1 183 111 22 TYR HB2 H 2.7300 0.05 2 184 111 22 TYR HB3 H 2.5700 0.05 2 185 111 22 TYR HD1 H 6.7000 0.05 3 186 111 22 TYR HE1 H 6.8200 0.05 3 187 111 22 TYR CA C 56.1000 0.30 1 188 111 22 TYR CB C 43.1000 0.30 1 189 111 22 TYR N N 115.5900 0.50 1 190 112 23 ILE H H 9.8300 0.05 1 191 112 23 ILE HA H 4.7600 0.05 1 192 112 23 ILE HB H 1.9000 0.05 1 193 112 23 ILE HG12 H 1.3200 0.05 1 194 112 23 ILE HG13 H 0.1800 0.05 1 195 112 23 ILE HG2 H 0.9500 0.05 1 196 112 23 ILE HD1 H 0.2500 0.05 1 197 112 23 ILE CA C 60.6000 0.30 1 198 112 23 ILE CB C 39.0000 0.30 1 199 112 23 ILE CG1 C 26.8000 0.30 1 200 112 23 ILE CG2 C 17.3000 0.30 1 201 112 23 ILE CD1 C 15.3000 0.30 1 202 112 23 ILE N N 125.5600 0.50 1 203 113 24 ASP H H 9.0300 0.05 1 204 113 24 ASP HA H 4.9600 0.05 1 205 113 24 ASP HB2 H 3.3600 0.05 2 206 113 24 ASP HB3 H 2.4600 0.05 2 207 113 24 ASP CA C 52.0000 0.30 1 208 113 24 ASP CB C 42.2000 0.30 1 209 113 24 ASP N N 128.3500 0.50 1 210 114 25 LEU H H 8.5300 0.05 1 211 114 25 LEU HA H 3.9800 0.05 1 212 114 25 LEU HB2 H 1.7200 0.05 2 213 114 25 LEU HG H 1.6700 0.05 1 214 114 25 LEU HD2 H 0.9500 0.05 2 215 114 25 LEU CA C 58.8000 0.30 1 216 114 25 LEU CB C 42.6000 0.30 1 217 114 25 LEU CG C 27.4000 0.30 1 218 114 25 LEU CD2 C 25.4000 0.30 1 219 114 25 LEU N N 118.3000 0.50 1 220 115 26 ASP H H 7.9200 0.05 1 221 115 26 ASP HA H 4.3700 0.05 1 222 115 26 ASP HB2 H 2.8100 0.05 1 223 115 26 ASP HB3 H 2.6400 0.05 1 224 115 26 ASP CA C 58.0000 0.30 1 225 115 26 ASP CB C 40.6400 0.30 1 226 115 26 ASP N N 118.3000 0.50 1 227 116 27 GLU H H 8.6700 0.05 1 228 116 27 GLU HA H 4.6300 0.05 1 229 116 27 GLU HB3 H 2.3800 0.05 2 230 116 27 GLU HG2 H 2.1800 0.05 2 231 116 27 GLU HG3 H 2.1800 0.05 2 232 116 27 GLU CA C 58.5000 0.30 1 233 116 27 GLU CB C 29.4000 0.30 1 234 116 27 GLU CG C 37.7960 0.30 1 235 116 27 GLU N N 121.4000 0.50 1 236 117 28 LEU H H 8.6700 0.05 1 237 117 28 LEU HA H 3.9900 0.05 1 238 117 28 LEU HB2 H 1.6900 0.05 2 239 117 28 LEU HG H 1.5100 0.05 1 240 117 28 LEU HD1 H 0.7680 0.05 2 241 117 28 LEU HD2 H 0.7300 0.05 2 242 117 28 LEU CA C 58.4600 0.30 1 243 117 28 LEU CB C 42.0500 0.30 1 244 117 28 LEU CG C 26.2500 0.30 1 245 117 28 LEU CD1 C 26.4380 0.30 1 246 117 28 LEU CD2 C 23.1500 0.30 2 247 117 28 LEU N N 121.2000 0.50 1 248 118 29 LYS H H 8.6100 0.05 1 249 118 29 LYS HA H 3.8200 0.05 1 250 118 29 LYS HB2 H 1.7400 0.05 2 251 118 29 LYS HG2 H 1.3200 0.05 2 252 118 29 LYS HB3 H 2.0500 0.05 2 253 118 29 LYS HD2 H 1.6200 0.05 2 254 118 29 LYS HE2 H 2.8900 0.05 2 255 118 29 LYS CA C 61.3000 0.30 1 256 118 29 LYS CB C 32.5000 0.30 1 257 118 29 LYS CG C 25.9000 0.30 1 258 118 29 LYS CD C 29.8000 0.30 1 259 118 29 LYS CE C 41.4000 0.30 1 260 118 29 LYS N N 118.8000 0.50 1 261 119 30 ILE H H 8.1800 0.05 1 262 119 30 ILE HA H 3.8100 0.05 1 263 119 30 ILE HB H 1.9500 0.05 1 264 119 30 ILE HG12 H 1.7500 0.05 1 265 119 30 ILE HG13 H 1.2400 0.05 1 266 119 30 ILE HG2 H 0.9400 0.05 1 267 119 30 ILE HD1 H 0.9200 0.05 1 268 119 30 ILE CA C 65.1000 0.30 1 269 119 30 ILE CB C 38.2000 0.30 1 270 119 30 ILE CG1 C 29.4000 0.30 1 271 119 30 ILE CG2 C 17.4000 0.30 1 272 119 30 ILE CD1 C 13.3000 0.30 1 273 119 30 ILE N N 119.4000 0.50 1 274 120 31 MET H H 7.5000 0.05 1 275 120 31 MET HA H 3.3600 0.05 1 276 120 31 MET HB2 H 2.0400 0.05 1 277 120 31 MET HB3 H 1.7100 0.05 1 278 120 31 MET HG2 H 2.4800 0.05 1 279 120 31 MET HG3 H 2.4800 0.05 1 280 120 31 MET HE H 1.0600 0.05 1 281 120 31 MET CA C 57.1000 0.30 1 282 120 31 MET CB C 31.6000 0.30 1 283 120 31 MET CG C 32.3000 0.30 1 284 120 31 MET CE C 15.5000 0.30 1 285 120 31 MET N N 119.3400 0.50 1 286 121 32 LEU H H 8.5200 0.05 1 287 121 32 LEU HA H 4.0300 0.05 1 288 121 32 LEU HB2 H 2.0800 0.05 1 289 121 32 LEU HB3 H 1.4400 0.05 1 290 121 32 LEU HG H 1.8800 0.05 1 291 121 32 LEU HD1 H 0.9000 0.05 2 292 121 32 LEU HD2 H 0.9000 0.05 2 293 121 32 LEU CA C 57.6000 0.30 1 294 121 32 LEU CB C 41.7000 0.30 1 295 121 32 LEU CG C 27.3000 0.30 1 296 121 32 LEU CD1 C 26.8000 0.30 1 297 121 32 LEU CD2 C 23.8000 0.30 1 298 121 32 LEU N N 117.9200 0.50 1 299 122 33 GLN H H 8.8100 0.05 1 300 122 33 GLN HA H 4.1100 0.05 1 301 122 33 GLN HB2 H 2.1900 0.05 2 302 122 33 GLN HB3 H 2.2600 0.05 2 303 122 33 GLN HG2 H 2.5800 0.05 2 304 122 33 GLN HG3 H 2.4400 0.05 2 305 122 33 GLN CA C 58.8000 0.30 1 306 122 33 GLN CB C 28.0000 0.30 1 307 122 33 GLN CG C 34.4000 0.30 1 308 122 33 GLN N N 120.7800 0.50 1 309 122 33 GLN NE2 N 110.4940 0.50 1 310 123 34 ALA H H 7.5800 0.05 1 311 123 34 ALA HA H 4.3000 0.05 1 312 123 34 ALA HB H 1.6000 0.05 1 313 123 34 ALA CA C 53.6000 0.30 1 314 123 34 ALA CB C 18.5000 0.30 1 315 123 34 ALA N N 121.2200 0.50 1 316 124 35 THR H H 7.4900 0.05 1 317 124 35 THR HA H 4.0500 0.05 1 318 124 35 THR HB H 4.3300 0.05 1 319 124 35 THR HG2 H 1.4400 0.05 1 320 124 35 THR CA C 64.2000 0.30 1 321 124 35 THR CB C 71.3000 0.30 1 322 124 35 THR CG2 C 21.5000 0.30 1 323 124 35 THR N N 106.7200 0.50 1 324 125 36 GLY H H 7.6800 0.05 1 325 125 36 GLY HA2 H 4.2600 0.05 1 326 125 36 GLY HA3 H 3.8000 0.05 1 327 125 36 GLY CA C 45.6000 0.30 1 328 125 36 GLY N N 108.3500 0.50 1 329 126 37 GLU H H 7.5000 0.05 1 330 126 37 GLU HA H 4.2800 0.05 1 331 126 37 GLU HB2 H 1.8800 0.05 1 332 126 37 GLU HB3 H 1.6900 0.05 1 333 126 37 GLU HG2 H 2.0400 0.05 1 334 126 37 GLU HG3 H 2.1200 0.05 1 335 126 37 GLU CA C 55.2000 0.30 1 336 126 37 GLU CB C 31.0000 0.30 1 337 126 37 GLU CG C 36.6000 0.30 1 338 126 37 GLU N N 120.1000 0.50 1 339 127 38 THR H H 8.6500 0.05 1 340 127 38 THR HA H 4.1700 0.05 1 341 127 38 THR HB H 4.0800 0.05 1 342 127 38 THR HG2 H 1.1600 0.05 1 343 127 38 THR CA C 63.7000 0.30 1 344 127 38 THR CB C 68.8000 0.30 1 345 127 38 THR CG2 C 21.7000 0.30 1 346 127 38 THR N N 119.8300 0.50 1 347 128 39 ILE H H 8.3700 0.05 1 348 128 39 ILE HA H 4.6400 0.05 1 349 128 39 ILE HB H 2.0600 0.05 1 350 128 39 ILE HG13 H 1.5900 0.05 1 351 128 39 ILE HG2 H 0.9500 0.05 1 352 128 39 ILE HD1 H 0.6100 0.05 1 353 128 39 ILE CA C 57.7000 0.30 1 354 128 39 ILE CB C 38.2000 0.30 1 355 128 39 ILE CG1 C 25.5000 0.30 1 356 128 39 ILE CG2 C 18.5000 0.30 1 357 128 39 ILE CD1 C 11.3000 0.30 1 358 128 39 ILE N N 128.6300 0.50 1 359 129 40 THR H H 9.6800 0.05 1 360 129 40 THR HA H 4.7500 0.05 1 361 129 40 THR HB H 4.7000 0.05 1 362 129 40 THR HG2 H 1.2500 0.05 1 363 129 40 THR CA C 59.7000 0.30 1 364 129 40 THR CB C 72.3000 0.30 1 365 129 40 THR CG2 C 21.5000 0.30 1 366 129 40 THR N N 119.8300 0.50 1 367 130 41 GLU H H 8.9200 0.05 1 368 130 41 GLU HA H 4.0300 0.05 1 369 130 41 GLU HB2 H 2.5400 0.05 2 370 130 41 GLU HG2 H 2.3500 0.05 2 371 130 41 GLU CA C 59.8000 0.30 1 372 130 41 GLU CB C 29.1000 0.30 1 373 130 41 GLU CG C 36.5000 0.30 1 374 130 41 GLU N N 119.7600 0.50 1 375 131 42 ASP H H 7.8300 0.05 1 376 131 42 ASP HA H 4.3800 0.05 1 377 131 42 ASP HB3 H 2.4800 0.05 2 378 131 42 ASP CA C 57.3000 0.30 1 379 131 42 ASP CB C 40.8000 0.30 1 380 131 42 ASP N N 117.7500 0.50 1 381 132 43 ASP H H 7.5700 0.05 1 382 132 43 ASP HA H 4.2200 0.05 1 383 132 43 ASP HB2 H 3.2400 0.05 1 384 132 43 ASP HB3 H 2.3100 0.05 1 385 132 43 ASP CA C 58.2000 0.30 1 386 132 43 ASP CB C 42.1000 0.30 1 387 132 43 ASP N N 119.8800 0.50 1 388 133 44 ILE H H 7.1800 0.05 1 389 133 44 ILE HA H 3.3400 0.05 1 390 133 44 ILE HB H 1.8600 0.05 1 391 133 44 ILE HG12 H 1.7900 0.05 1 392 133 44 ILE HG13 H 0.8100 0.05 1 393 133 44 ILE HG2 H 0.9500 0.05 1 394 133 44 ILE HD1 H 0.9000 0.05 1 395 133 44 ILE CA C 65.5000 0.30 1 396 133 44 ILE CB C 38.7000 0.30 1 397 133 44 ILE CG1 C 29.6000 0.30 1 398 133 44 ILE CG2 C 18.4000 0.30 1 399 133 44 ILE CD1 C 14.1000 0.30 1 400 133 44 ILE N N 116.5800 0.50 1 401 134 45 GLU H H 8.1500 0.05 1 402 134 45 GLU HA H 3.8900 0.05 1 403 134 45 GLU HB2 H 2.1800 0.05 2 404 134 45 GLU HG2 H 2.4300 0.05 2 405 134 45 GLU HG3 H 2.1800 0.05 2 406 134 45 GLU CA C 59.6000 0.30 1 407 134 45 GLU CB C 30.1000 0.30 1 408 134 45 GLU CG C 36.4000 0.30 1 409 134 45 GLU N N 117.7400 0.50 1 410 135 46 GLU H H 8.4300 0.05 1 411 135 46 GLU HA H 4.2200 0.05 1 412 135 46 GLU HB2 H 2.1500 0.05 1 413 135 46 GLU HB3 H 1.9900 0.05 1 414 135 46 GLU HG2 H 2.4700 0.05 1 415 135 46 GLU HG3 H 2.3100 0.05 1 416 135 46 GLU CA C 58.9000 0.30 1 417 135 46 GLU CB C 29.3000 0.30 1 418 135 46 GLU CG C 37.2000 0.30 1 419 135 46 GLU N N 116.3000 0.50 1 420 136 47 LEU H H 8.1000 0.05 1 421 136 47 LEU HA H 4.2600 0.05 1 422 136 47 LEU HB2 H 1.5700 0.05 2 423 136 47 LEU HB3 H 2.1500 0.05 2 424 136 47 LEU HG H 2.1600 0.05 1 425 136 47 LEU HD1 H 1.0000 0.05 2 426 136 47 LEU HD2 H 1.0200 0.05 2 427 136 47 LEU CA C 57.4000 0.30 1 428 136 47 LEU CB C 41.7000 0.30 1 429 136 47 LEU CG C 26.8000 0.30 1 430 136 47 LEU CD1 C 24.3000 0.30 1 431 136 47 LEU CD2 C 26.8000 0.30 1 432 136 47 LEU N N 120.7000 0.50 1 433 137 48 MET H H 8.1800 0.05 1 434 137 48 MET HA H 4.2900 0.05 1 435 137 48 MET HB3 H 1.8700 0.05 2 436 137 48 MET HG2 H 2.6100 0.05 1 437 137 48 MET HG3 H 2.4700 0.05 1 438 137 48 MET HE H 1.9000 0.05 1 439 137 48 MET CA C 57.7000 0.30 1 440 137 48 MET CB C 30.6000 0.30 1 441 137 48 MET CG C 32.2000 0.30 1 442 137 48 MET CE C 16.8000 0.30 1 443 137 48 MET N N 117.9300 0.50 1 444 138 49 LYS H H 8.0600 0.05 1 445 138 49 LYS HA H 4.0700 0.05 1 446 138 49 LYS HB2 H 1.8800 0.05 1 447 138 49 LYS HB3 H 1.8800 0.05 1 448 138 49 LYS HG3 H 1.5100 0.05 2 449 138 49 LYS HD2 H 1.6900 0.05 2 450 138 49 LYS HE2 H 2.9700 0.05 2 451 138 49 LYS CA C 59.0000 0.30 1 452 138 49 LYS CB C 32.6000 0.30 1 453 138 49 LYS CG C 25.4000 0.30 1 454 138 49 LYS CD C 29.3000 0.30 1 455 138 49 LYS CE C 42.2000 0.30 1 456 138 49 LYS N N 117.3700 0.50 1 457 139 50 ASP H H 7.6500 0.05 1 458 139 50 ASP HA H 4.3800 0.05 1 459 139 50 ASP HB2 H 3.1200 0.05 2 460 139 50 ASP HB3 H 2.8000 0.05 2 461 139 50 ASP CA C 56.7000 0.30 1 462 139 50 ASP CB C 43.2000 0.30 1 463 139 50 ASP N N 117.3300 0.50 1 464 140 51 GLY H H 7.8500 0.05 1 465 140 51 GLY HA2 H 3.9100 0.05 2 466 140 51 GLY HA3 H 2.7200 0.05 2 467 140 51 GLY CA C 46.2000 0.30 1 468 140 51 GLY N N 101.8500 0.50 1 469 141 52 ASP H H 8.5000 0.05 1 470 141 52 ASP HA H 4.5700 0.05 1 471 141 52 ASP HB2 H 2.9200 0.05 1 472 141 52 ASP HB3 H 2.2900 0.05 1 473 141 52 ASP CA C 53.2000 0.30 1 474 141 52 ASP CB C 39.5000 0.30 1 475 141 52 ASP N N 120.4200 0.50 1 476 142 53 LYS H H 7.7400 0.05 1 477 142 53 LYS HA H 4.1500 0.05 1 478 142 53 LYS HB2 H 1.9200 0.05 2 479 142 53 LYS HG3 H 1.5100 0.05 2 480 142 53 LYS HD2 H 1.7100 0.05 2 481 142 53 LYS HE2 H 3.1100 0.05 2 482 142 53 LYS CA C 57.9000 0.30 1 483 142 53 LYS CB C 33.0000 0.30 1 484 142 53 LYS CG C 24.7000 0.30 1 485 142 53 LYS CD C 28.4000 0.30 1 486 142 53 LYS CE C 42.3000 0.30 1 487 142 53 LYS N N 125.8900 0.50 1 488 143 54 ASN H H 8.1200 0.05 1 489 143 54 ASN HA H 4.8000 0.05 1 490 143 54 ASN HB2 H 3.3100 0.05 1 491 143 54 ASN HB3 H 2.8500 0.05 1 492 143 54 ASN HD21 H 7.8600 0.05 2 493 143 54 ASN HD22 H 6.6300 0.05 2 494 143 54 ASN CA C 51.7000 0.30 1 495 143 54 ASN CB C 37.2000 0.30 1 496 143 54 ASN N N 113.6100 0.50 1 497 143 54 ASN ND2 N 112.6040 0.50 1 498 144 55 ASN H H 7.7200 0.05 1 499 144 55 ASN HA H 4.5000 0.05 1 500 144 55 ASN HB2 H 3.0800 0.05 1 501 144 55 ASN HB3 H 2.6400 0.05 1 502 144 55 ASN CA C 55.1000 0.30 1 503 144 55 ASN CB C 37.8000 0.30 1 504 144 55 ASN N N 115.9000 0.50 1 505 144 55 ASN ND2 N 111.9510 0.50 1 506 145 56 ASP H H 8.6800 0.05 1 507 145 56 ASP HA H 4.7100 0.05 1 508 145 56 ASP HB2 H 3.0000 0.05 2 509 145 56 ASP HB3 H 2.3800 0.05 2 510 145 56 ASP CA C 53.0000 0.30 1 511 145 56 ASP CB C 41.0000 0.30 1 512 145 56 ASP N N 118.5700 0.50 1 513 146 57 GLY H H 10.3200 0.05 1 514 146 57 GLY HA2 H 4.0700 0.05 2 515 146 57 GLY HA3 H 3.4700 0.05 2 516 146 57 GLY CA C 45.7000 0.30 1 517 146 57 GLY N N 112.9400 0.50 1 518 147 58 ARG H H 7.6900 0.05 1 519 147 58 ARG HA H 4.9100 0.05 1 520 147 58 ARG HB2 H 1.5400 0.05 2 521 147 58 ARG HG3 H 1.2900 0.05 2 522 147 58 ARG HD2 H 2.5300 0.05 1 523 147 58 ARG HD3 H 2.2700 0.05 1 524 147 58 ARG CA C 54.0000 0.30 1 525 147 58 ARG CB C 34.4000 0.30 1 526 147 58 ARG CG C 25.8000 0.30 1 527 147 58 ARG CD C 43.1000 0.30 1 528 147 58 ARG N N 115.4400 0.50 1 529 148 59 ILE H H 9.4300 0.05 1 530 148 59 ILE HA H 5.0500 0.05 1 531 148 59 ILE HB H 1.8100 0.05 1 532 148 59 ILE HG12 H 0.3600 0.05 1 533 148 59 ILE HG13 H 1.6100 0.05 1 534 148 59 ILE HG2 H 0.9500 0.05 1 535 148 59 ILE HD1 H 0.3700 0.05 1 536 148 59 ILE CA C 60.6000 0.30 1 537 148 59 ILE CB C 40.0000 0.30 1 538 148 59 ILE CG1 C 28.1000 0.30 1 539 148 59 ILE CG2 C 17.3000 0.30 1 540 148 59 ILE CD1 C 13.3000 0.30 1 541 148 59 ILE N N 126.0900 0.50 1 542 149 60 ASP H H 9.3900 0.05 1 543 149 60 ASP HA H 5.1600 0.05 1 544 149 60 ASP HB2 H 3.2200 0.05 1 545 149 60 ASP HB3 H 2.8000 0.05 1 546 149 60 ASP CA C 52.5000 0.30 1 547 149 60 ASP CB C 41.9000 0.30 1 548 149 60 ASP N N 129.1700 0.50 1 549 150 61 TYR H H 8.4200 0.05 1 550 150 61 TYR HA H 3.3800 0.05 1 551 150 61 TYR HB2 H 2.4600 0.05 2 552 150 61 TYR HB3 H 2.1500 0.05 2 553 150 61 TYR HD1 H 6.3600 0.05 3 554 150 61 TYR HE1 H 6.5700 0.05 3 555 150 61 TYR CA C 62.2000 0.30 1 556 150 61 TYR CB C 38.2000 0.30 1 557 150 61 TYR N N 118.6000 0.50 1 558 151 62 ASP H H 7.7400 0.05 1 559 151 62 ASP HA H 4.0800 0.05 1 560 151 62 ASP HB2 H 2.6900 0.05 1 561 151 62 ASP HB3 H 2.5900 0.05 1 562 151 62 ASP CA C 57.9000 0.30 1 563 151 62 ASP CB C 40.6000 0.30 1 564 151 62 ASP N N 118.0600 0.50 1 565 152 63 GLU H H 8.8800 0.05 1 566 152 63 GLU HA H 4.0300 0.05 1 567 152 63 GLU HB2 H 2.4900 0.05 1 568 152 63 GLU HB3 H 2.3800 0.05 1 569 152 63 GLU HG2 H 2.9900 0.05 2 570 152 63 GLU CA C 58.7000 0.30 1 571 152 63 GLU CB C 29.7000 0.30 1 572 152 63 GLU CG C 37.5000 0.30 1 573 152 63 GLU N N 120.4800 0.50 1 574 153 64 PHE H H 9.2800 0.05 1 575 153 64 PHE HA H 4.0000 0.05 1 576 153 64 PHE HB2 H 3.4000 0.05 1 577 153 64 PHE HB3 H 3.1500 0.05 1 578 153 64 PHE HD1 H 6.8800 0.05 3 579 153 64 PHE HE1 H 6.3800 0.05 3 580 153 64 PHE HZ H 7.0700 0.05 1 581 153 64 PHE CA C 61.8000 0.30 1 582 153 64 PHE CB C 39.8000 0.30 1 583 153 64 PHE N N 124.9900 0.50 1 584 154 65 LEU H H 7.8800 0.05 1 585 154 65 LEU HA H 3.6500 0.05 1 586 154 65 LEU HB2 H 1.8100 0.05 1 587 154 65 LEU HB3 H 1.2800 0.05 1 588 154 65 LEU HG H 1.3800 0.05 1 589 154 65 LEU HD1 H 0.7300 0.05 2 590 154 65 LEU HD2 H 0.6800 0.05 2 591 154 65 LEU CA C 58.2000 0.30 1 592 154 65 LEU CB C 41.4000 0.30 1 593 154 65 LEU CG C 26.0000 0.30 1 594 154 65 LEU CD1 C 23.2000 0.30 1 595 154 65 LEU CD2 C 25.4000 0.30 1 596 154 65 LEU N N 117.7800 0.50 1 597 155 66 GLU H H 6.9100 0.05 1 598 155 66 GLU HA H 4.0500 0.05 1 599 155 66 GLU HB2 H 2.0700 0.05 2 600 155 66 GLU HG2 H 2.3200 0.05 2 601 155 66 GLU CA C 58.9000 0.30 1 602 155 66 GLU CB C 29.5000 0.30 1 603 155 66 GLU CG C 36.0000 0.30 1 604 155 66 GLU N N 116.5560 0.50 1 605 156 67 PHE H H 8.6100 0.05 1 606 156 67 PHE HA H 4.1200 0.05 1 607 156 67 PHE HB2 H 3.2500 0.05 1 608 156 67 PHE HB3 H 3.3400 0.05 1 609 156 67 PHE HD2 H 6.9600 0.05 3 610 156 67 PHE HE2 H 7.1400 0.05 3 611 156 67 PHE HZ H 7.3200 0.05 1 612 156 67 PHE CA C 58.6000 0.30 1 613 156 67 PHE CB C 40.9000 0.30 1 614 156 67 PHE N N 121.8000 0.50 1 615 157 68 MET H H 7.4900 0.05 1 616 157 68 MET HA H 4.3600 0.05 1 617 157 68 MET HB2 H 1.4000 0.05 1 618 157 68 MET HB3 H 1.9500 0.05 1 619 157 68 MET HG3 H 1.5600 0.05 1 620 157 68 MET HE H 1.8900 0.05 1 621 157 68 MET CA C 53.3000 0.30 1 622 157 68 MET CB C 32.5000 0.30 1 623 157 68 MET CE C 17.6000 0.30 1 624 157 68 MET N N 111.8000 0.50 1 625 158 69 LYS H H 7.1100 0.05 1 626 158 69 LYS HA H 3.9500 0.05 1 627 158 69 LYS HB2 H 1.9700 0.05 1 628 158 69 LYS HB3 H 1.8200 0.05 1 629 158 69 LYS HG2 H 1.4500 0.05 1 630 158 69 LYS HG3 H 1.3600 0.05 1 631 158 69 LYS HD2 H 1.6600 0.05 2 632 158 69 LYS HE2 H 2.9200 0.05 2 633 158 69 LYS CA C 59.3000 0.30 1 634 158 69 LYS CB C 32.4000 0.30 1 635 158 69 LYS CG C 24.0000 0.30 1 636 158 69 LYS CD C 29.4000 0.30 1 637 158 69 LYS CE C 42.2000 0.30 1 638 158 69 LYS N N 121.9700 0.50 1 639 159 70 ASP H H 8.4700 0.05 1 640 159 70 ASP HA H 4.4400 0.05 1 641 159 70 ASP HB2 H 2.7400 0.05 1 642 159 70 ASP HB3 H 2.5700 0.05 1 643 159 70 ASP CA C 54.9000 0.30 1 644 159 70 ASP CB C 40.4000 0.30 1 645 159 70 ASP N N 116.8000 0.50 1 646 160 71 VAL H H 7.2700 0.05 1 647 160 71 VAL HA H 3.7900 0.05 1 648 160 71 VAL HB H 1.9500 0.05 1 649 160 71 VAL HG1 H 0.7300 0.05 2 650 160 71 VAL HG2 H 0.8800 0.05 2 651 160 71 VAL CA C 63.3000 0.30 1 652 160 71 VAL CB C 32.1000 0.30 1 653 160 71 VAL CG1 C 22.1000 0.30 1 654 160 71 VAL CG2 C 22.2000 0.30 1 655 160 71 VAL N N 119.8000 0.50 1 656 161 72 GLU H H 7.8300 0.05 1 657 161 72 GLU HA H 4.0900 0.05 1 658 161 72 GLU HB2 H 1.9900 0.05 1 659 161 72 GLU HB3 H 1.8500 0.05 1 660 161 72 GLU HG2 H 2.1500 0.05 2 661 161 72 GLU CA C 58.3800 0.30 1 662 161 72 GLU CB C 31.2200 0.30 1 663 161 72 GLU CG C 36.7130 0.30 1 664 161 72 GLU N N 130.4000 0.50 1 stop_ save_