data_19816 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; NMR structure of the C-domain of troponin C bound to the anchoring region of troponin I ; _BMRB_accession_number 19816 _BMRB_flat_file_name bmr19816.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 Robertson Ian M. . 2 Baryshnikova Olga K. . 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" 331 "13C chemical shifts" 216 "15N chemical shifts" 70 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2014-03-10 original author . stop_ loop_ _Related_BMRB_accession_number _Relationship 19817 'mutation G159D in 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 'C-domain of 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 8369.260 _Mol_thiol_state 'not present' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 72 _Mol_residue_sequence ; MGKSEEELSDLFRMFDKNAD GYIDLDELKIMLQATGETIT EDDIEELMKDGDKNNDGRID YDEFLEFMKGVE ; 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 GLY 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 98.59 100.00 1.41e-38 BMRB 15388 F153W 98.61 161 98.59 100.00 1.41e-38 BMRB 15400 F153(FTR) 98.61 161 98.59 98.59 6.07e-38 BMRB 15427 F104(FTR) 98.61 161 98.59 100.00 1.41e-38 BMRB 16752 TnC 98.61 161 97.18 100.00 5.16e-38 BMRB 17243 cCTnC 100.00 72 100.00 100.00 2.21e-40 BMRB 17440 CcTnC 100.00 72 100.00 100.00 2.21e-40 BMRB 19817 cCTnC 100.00 72 98.61 98.61 2.85e-39 BMRB 25120 cTnC 98.61 161 100.00 100.00 4.07e-39 PDB 1AJ4 "Structure Of Calcium-Saturated Cardiac Troponin C, Nmr, 1 Structure" 98.61 161 97.18 100.00 2.82e-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 98.59 100.00 1.70e-38 PDB 1FI5 "Nmr Structure Of The C Terminal Domain Of Cardiac Troponin C Bound To The N Terminal Domain Of Cardiac Troponin I." 98.61 81 97.18 100.00 1.23e-38 PDB 1IH0 "Structure Of The C-Domain Of Human Cardiac Troponin C In Complex With Ca2+ Sensitizer Emd 57033" 97.22 71 98.57 100.00 3.13e-38 PDB 1J1D "Crystal Structure Of The 46kda Domain Of Human Cardiac Troponin In The Ca2+ Saturated Form" 98.61 161 98.59 100.00 1.70e-38 PDB 1J1E "Crystal Structure Of The 52kda Domain Of Human Cardiac Troponin In The Ca2+ Saturated Form" 98.61 161 98.59 100.00 1.70e-38 PDB 1LA0 "Solution Structure Of Calcium Saturated Cardiac Troponin C In The Troponin C-Troponin I Complex" 98.61 161 97.18 100.00 5.16e-38 PDB 1OZS "C-Domain Of Human Cardiac Troponin C In Complex With The Inhibitory Region Of Human Cardiac Troponin I" 98.61 73 98.59 100.00 4.77e-39 PDB 1SBJ "Nmr Structure Of The Mg2+-Loaded C Terminal Domain Of Cardiac Troponin C Bound To The N Terminal Domain Of Cardiac Troponin I" 98.61 81 97.18 100.00 1.23e-38 PDB 1SCV "Nmr Structure Of The C Terminal Domain Of Cardiac Troponin C Bound To The N Terminal Domain Of Cardiac Troponin I" 98.61 81 97.18 100.00 1.23e-38 PDB 2JT0 "Solution Structure Of F104w Cardiac Troponin C" 98.61 161 98.59 100.00 1.41e-38 PDB 2JT3 "Solution Structure Of F153w Cardiac Troponin C" 98.61 161 98.59 100.00 1.41e-38 PDB 2JT8 "Solution Structure Of The F153-To-5-Flurotryptophan Mutant Of Human Cardiac Troponin C" 98.61 161 98.59 98.59 6.07e-38 PDB 2JTZ "Solution Structure And Chemical Shift Assignments Of The F104-To-5-Flurotryptophan Mutant Of Cardiac Troponin C" 98.61 161 98.59 98.59 6.07e-38 PDB 2KDH "The Solution Structure Of Human Cardiac Troponin C In Complex With The Green Tea Polyphenol; (-)- Epigallocatechin-3-Gallate" 100.00 72 100.00 100.00 2.21e-40 PDB 2L98 "Structure Of Trans-Resveratrol In Complex With The Cardiac Regulatory Protein Troponin C" 100.00 72 100.00 100.00 2.21e-40 PDB 2MLE "Nmr Structure Of The C-domain Of Troponin C Bound To The Anchoring Region Of Troponin I" 100.00 72 100.00 100.00 2.21e-40 PDB 2MLF "Nmr Structure Of The Dilated Cardiomyopathy Mutation G159d In Troponin C Bound To The Anchoring Region Of Troponin I" 100.00 72 98.61 98.61 2.85e-39 PDB 3CTN "Structure Of Calcium-Saturated Cardiac Troponin C, Nmr, 30 Structures" 98.61 76 97.18 100.00 1.45e-38 DBJ BAA02369 "cardiac troponin C [Gallus gallus]" 98.61 161 97.18 100.00 5.16e-38 DBJ BAG36483 "unnamed protein product [Homo sapiens]" 98.61 161 100.00 100.00 4.79e-39 EMBL CAA30736 "unnamed protein product [Homo sapiens]" 98.61 161 100.00 100.00 4.79e-39 EMBL CAG46663 "TNNC1 [Homo sapiens]" 98.61 161 100.00 100.00 4.79e-39 EMBL CAG46683 "TNNC1 [Homo sapiens]" 98.61 161 100.00 100.00 4.79e-39 GB AAA36772 "slow twitch skeletal/cardiac muscle troponin C [Homo sapiens]" 98.61 161 100.00 100.00 4.79e-39 GB AAA37492 "slow/cardiac troponin C, partial [Mus musculus]" 98.61 161 98.59 100.00 1.51e-38 GB AAA37493 "slow/cardiac troponin C [Mus musculus]" 98.61 161 98.59 100.00 1.51e-38 GB AAA48654 "slow muscle troponin C [Gallus gallus]" 98.61 161 97.18 100.00 5.16e-38 GB AAB91994 "cardiac ventricular troponin C [Homo sapiens]" 98.61 160 98.59 98.59 1.11e-36 PIR TPHUCC "troponin C, cardiac and slow skeletal muscle - human" 98.61 161 100.00 100.00 4.79e-39 PRF 1510257A "troponin C" 98.61 161 98.59 100.00 1.95e-38 PRF 750650A "troponin c,cardiac" 98.61 161 98.59 100.00 1.95e-38 REF NP_001029277 "troponin C, slow skeletal and cardiac muscles [Rattus norvegicus]" 98.61 161 98.59 100.00 1.51e-38 REF NP_001029523 "troponin C, slow skeletal and cardiac muscles [Bos taurus]" 98.61 161 98.59 100.00 1.95e-38 REF NP_001123715 "troponin C, slow skeletal and cardiac muscles [Sus scrofa]" 98.61 161 98.59 100.00 1.95e-38 REF NP_001272501 "troponin C, slow skeletal and cardiac muscles [Capra hircus]" 98.61 161 98.59 100.00 1.95e-38 REF NP_001291793 "troponin C type 1 (slow) [Ailuropoda melanoleuca]" 98.61 161 97.18 98.59 5.16e-38 SP P02591 "RecName: Full=Troponin C, slow skeletal and cardiac muscles; Short=TN-C" 98.61 161 100.00 100.00 4.79e-39 SP P09860 "RecName: Full=Troponin C, slow skeletal and cardiac muscles; Short=TN-C" 98.61 161 97.18 100.00 5.16e-38 SP P19123 "RecName: Full=Troponin C, slow skeletal and cardiac muscles; Short=TN-C" 98.61 161 98.59 100.00 1.51e-38 SP P63315 "RecName: Full=Troponin C, slow skeletal and cardiac muscles; Short=TN-C" 98.61 161 98.59 100.00 1.95e-38 SP P63316 "RecName: Full=Troponin C, slow skeletal and cardiac muscles; Short=TN-C" 98.61 161 100.00 100.00 4.79e-39 TPG DAA16908 "TPA: troponin C, slow skeletal and cardiac muscles [Bos taurus]" 98.61 161 98.59 100.00 1.95e-38 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 'data analysis' 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' 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 'geometry optimization' stop_ _Details . save_ save_VNMRJ _Saveframe_category software _Name VNMRJ _Version . loop_ _Vendor _Address _Electronic_address Varian . . stop_ loop_ _Task processing 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_2D_DQF-COSY_2 _Saveframe_category NMR_applied_experiment _Experiment_name '2D DQF-COSY' _Sample_label $sample_2 save_ save_2D_1H-1H_NOESY_3 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-1H NOESY' _Sample_label $sample_2 save_ save_3D_CBCA(CO)NH_4 _Saveframe_category NMR_applied_experiment _Experiment_name '3D CBCA(CO)NH' _Sample_label $sample_1 save_ save_3D_C(CO)NH_5 _Saveframe_category NMR_applied_experiment _Experiment_name '3D C(CO)NH' _Sample_label $sample_1 save_ save_3D_HNCACB_6 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCACB' _Sample_label $sample_1 save_ save_3D_H(CCO)NH_7 _Saveframe_category NMR_applied_experiment _Experiment_name '3D H(CCO)NH' _Sample_label $sample_1 save_ save_3D_HCCH-TOCSY_8 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HCCH-TOCSY' _Sample_label $sample_1 save_ save_3D_HNHA_9 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNHA' _Sample_label $sample_1 save_ save_3D_HNHB_10 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNHB' _Sample_label $sample_1 save_ save_3D_1H-15N_NOESY_11 _Saveframe_category NMR_applied_experiment _Experiment_name '3D 1H-15N NOESY' _Sample_label $sample_1 save_ save_3D_1H-15N_TOCSY_12 _Saveframe_category NMR_applied_experiment _Experiment_name '3D 1H-15N TOCSY' _Sample_label $sample_1 save_ save_3D_1H-13C_NOESY_13 _Saveframe_category NMR_applied_experiment _Experiment_name '3D 1H-13C NOESY' _Sample_label $sample_1 save_ save_2D_13C,15N_Filtered_NOESY_14 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 13C,15N Filtered NOESY' _Sample_label $sample_1 save_ save_2D_13C,15N_Filtered_TOCSY_15 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 13C,15N Filtered TOCSY' _Sample_label $sample_1 save_ save_3D_13C_Edited,_Filtered_NOESY_16 _Saveframe_category NMR_applied_experiment _Experiment_name '3D 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' '2D DQF-COSY' '3D CBCA(CO)NH' '3D C(CO)NH' '3D HNCACB' '3D H(CCO)NH' '3D HCCH-TOCSY' '3D HNHA' '3D HNHB' 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 HE H 2.1190 0.05 1 2 90 1 MET CE C 16.8520 0.30 1 3 91 2 GLY HA2 H 4.0230 0.05 2 4 91 2 GLY CA C 44.7760 0.30 1 5 92 3 LYS H H 8.5630 0.05 1 6 92 3 LYS HA H 4.4490 0.05 1 7 92 3 LYS HB3 H 1.7820 0.05 2 8 92 3 LYS HD3 H 1.5790 0.05 2 9 92 3 LYS HE3 H 2.9850 0.05 2 10 92 3 LYS CA C 56.0290 0.30 1 11 92 3 LYS CB C 33.6250 0.30 1 12 92 3 LYS CG C 25.0820 0.30 1 13 92 3 LYS CD C 28.9160 0.30 1 14 92 3 LYS CE C 42.5240 0.30 1 15 92 3 LYS N N 120.9540 0.50 1 16 93 4 SER H H 8.8000 0.05 1 17 93 4 SER HA H 4.4790 0.05 1 18 93 4 SER HB2 H 4.2740 0.05 2 19 93 4 SER HB3 H 4.0400 0.05 2 20 93 4 SER CA C 58.2200 0.30 1 21 93 4 SER CB C 64.7230 0.30 1 22 93 4 SER N N 117.4740 0.50 1 23 94 5 GLU H H 8.8650 0.05 1 24 94 5 GLU HA H 4.0540 0.05 1 25 94 5 GLU HB3 H 2.0810 0.05 2 26 94 5 GLU HG3 H 2.3800 0.05 2 27 94 5 GLU CA C 59.7200 0.30 1 28 94 5 GLU CB C 29.2500 0.30 1 29 94 5 GLU CG C 36.9660 0.30 1 30 94 5 GLU N N 122.0760 0.50 1 31 95 6 GLU H H 8.5720 0.05 1 32 95 6 GLU HA H 4.1260 0.05 1 33 95 6 GLU HB3 H 2.0790 0.05 2 34 95 6 GLU HG3 H 2.3460 0.05 2 35 95 6 GLU CA C 59.3930 0.30 1 36 95 6 GLU CB C 29.3750 0.30 1 37 95 6 GLU CG C 36.7240 0.30 1 38 95 6 GLU N N 119.4420 0.50 1 39 96 7 GLU H H 8.0400 0.05 1 40 96 7 GLU HA H 4.3080 0.05 1 41 96 7 GLU HG3 H 2.3270 0.05 2 42 96 7 GLU CA C 59.0090 0.30 1 43 96 7 GLU CB C 30.1420 0.30 1 44 96 7 GLU CG C 37.0880 0.30 1 45 96 7 GLU N N 120.5400 0.50 1 46 97 8 LEU H H 8.5350 0.05 1 47 97 8 LEU HA H 4.3040 0.05 1 48 97 8 LEU HB2 H 2.1100 0.05 2 49 97 8 LEU HB3 H 1.5730 0.05 2 50 97 8 LEU HG H 1.8360 0.05 1 51 97 8 LEU HD1 H 0.8680 0.05 2 52 97 8 LEU HD2 H 0.8410 0.05 2 53 97 8 LEU CA C 58.5870 0.30 1 54 97 8 LEU CB C 41.9920 0.30 1 55 97 8 LEU CG C 27.6230 0.30 1 56 97 8 LEU CD1 C 23.3840 0.30 2 57 97 8 LEU CD2 C 26.0930 0.30 2 58 97 8 LEU N N 119.5930 0.50 1 59 98 9 SER H H 8.6090 0.05 1 60 98 9 SER HA H 4.2980 0.05 1 61 98 9 SER HB3 H 4.0710 0.05 2 62 98 9 SER CA C 62.0490 0.30 1 63 98 9 SER CB C 62.3370 0.30 1 64 98 9 SER N N 115.7450 0.50 1 65 99 10 ASP H H 7.5700 0.05 1 66 99 10 ASP HA H 4.7110 0.05 1 67 99 10 ASP HB2 H 2.8390 0.05 2 68 99 10 ASP HB3 H 2.3960 0.05 2 69 99 10 ASP CA C 57.4020 0.30 1 70 99 10 ASP CB C 41.3130 0.30 1 71 99 10 ASP N N 121.7110 0.50 1 72 100 11 LEU H H 8.1630 0.05 1 73 100 11 LEU HA H 4.1580 0.05 1 74 100 11 LEU HB3 H 2.3060 0.05 2 75 100 11 LEU HG H 1.6230 0.05 1 76 100 11 LEU HD1 H 0.9740 0.05 2 77 100 11 LEU HD2 H 1.0910 0.05 2 78 100 11 LEU CA C 58.2550 0.30 1 79 100 11 LEU CB C 41.4450 0.30 1 80 100 11 LEU CG C 26.5520 0.30 1 81 100 11 LEU CD1 C 23.6160 0.30 2 82 100 11 LEU CD2 C 26.3970 0.30 2 83 100 11 LEU N N 118.0890 0.50 1 84 101 12 PHE H H 8.7570 0.05 1 85 101 12 PHE HA H 3.6770 0.05 1 86 101 12 PHE HB2 H 3.1710 0.05 2 87 101 12 PHE HB3 H 2.8930 0.05 2 88 101 12 PHE HD1 H 6.3930 0.05 3 89 101 12 PHE HD2 H 6.4050 0.05 3 90 101 12 PHE HE2 H 6.9620 0.05 3 91 101 12 PHE CA C 62.2340 0.30 1 92 101 12 PHE CB C 39.2500 0.30 1 93 101 12 PHE N N 120.4620 0.50 1 94 102 13 ARG H H 7.4840 0.05 1 95 102 13 ARG HA H 3.9970 0.05 1 96 102 13 ARG HB3 H 2.0500 0.05 2 97 102 13 ARG HG3 H 1.7050 0.05 2 98 102 13 ARG HD3 H 3.3300 0.05 2 99 102 13 ARG CA C 59.1400 0.30 1 100 102 13 ARG CB C 30.3820 0.30 1 101 102 13 ARG CG C 28.6950 0.30 1 102 102 13 ARG CD C 43.4360 0.30 1 103 102 13 ARG N N 115.5130 0.50 1 104 103 14 MET H H 7.6090 0.05 1 105 103 14 MET HA H 4.3740 0.05 1 106 103 14 MET HB2 H 2.6770 0.05 2 107 103 14 MET HB3 H 2.4140 0.05 2 108 103 14 MET HG3 H 3.2080 0.05 2 109 103 14 MET HE H 1.9060 0.05 1 110 103 14 MET CA C 55.9300 0.30 1 111 103 14 MET CB C 34.1250 0.30 1 112 103 14 MET CG C 32.5540 0.30 1 113 103 14 MET CE C 16.8090 0.30 1 114 103 14 MET N N 114.2240 0.50 1 115 104 15 PHE H H 7.3770 0.05 1 116 104 15 PHE HA H 4.2850 0.05 1 117 104 15 PHE HB2 H 2.8110 0.05 2 118 104 15 PHE HB3 H 2.5600 0.05 2 119 104 15 PHE CA C 59.4180 0.30 1 120 104 15 PHE CB C 41.6790 0.30 1 121 104 15 PHE N N 115.0690 0.50 1 122 105 16 ASP H H 7.2890 0.05 1 123 105 16 ASP HA H 4.4350 0.05 1 124 105 16 ASP HB3 H 1.4500 0.05 2 125 105 16 ASP CA C 52.2740 0.30 1 126 105 16 ASP CB C 38.8930 0.30 1 127 105 16 ASP N N 116.7340 0.50 1 128 106 17 LYS H H 7.5040 0.05 1 129 106 17 LYS HA H 4.0390 0.05 1 130 106 17 LYS HB3 H 1.8980 0.05 2 131 106 17 LYS HG2 H 1.5710 0.05 2 132 106 17 LYS HG3 H 1.4780 0.05 2 133 106 17 LYS HD3 H 1.6320 0.05 2 134 106 17 LYS HE3 H 3.0480 0.05 2 135 106 17 LYS CA C 58.2950 0.30 1 136 106 17 LYS CB C 32.9620 0.30 1 137 106 17 LYS CG C 25.0370 0.30 1 138 106 17 LYS CD C 28.3570 0.30 1 139 106 17 LYS CE C 42.7300 0.30 1 140 106 17 LYS N N 124.2540 0.50 1 141 107 18 ASN H H 8.0180 0.05 1 142 107 18 ASN HA H 4.7400 0.05 1 143 107 18 ASN HB2 H 3.3100 0.05 2 144 107 18 ASN HB3 H 2.8760 0.05 2 145 107 18 ASN CA C 51.7070 0.30 1 146 107 18 ASN CB C 36.9150 0.30 1 147 107 18 ASN N N 113.6290 0.50 1 148 108 19 ALA H H 7.8210 0.05 1 149 108 19 ALA HA H 4.1010 0.05 1 150 108 19 ALA HB H 1.3840 0.05 1 151 108 19 ALA CA C 54.1950 0.30 1 152 108 19 ALA CB C 17.0120 0.30 1 153 108 19 ALA N N 121.3550 0.50 1 154 109 20 ASP H H 8.5360 0.05 1 155 109 20 ASP HA H 4.7080 0.05 1 156 109 20 ASP HB2 H 3.1800 0.05 2 157 109 20 ASP HB3 H 2.4450 0.05 2 158 109 20 ASP CA C 53.2320 0.30 1 159 109 20 ASP CB C 40.9160 0.30 1 160 109 20 ASP N N 118.3730 0.50 1 161 110 21 GLY H H 10.4030 0.05 1 162 110 21 GLY HA2 H 4.0640 0.05 2 163 110 21 GLY HA3 H 3.4540 0.05 2 164 110 21 GLY CA C 44.9980 0.30 1 165 110 21 GLY N N 112.1850 0.50 1 166 111 22 TYR H H 8.0140 0.05 1 167 111 22 TYR HA H 5.1850 0.05 1 168 111 22 TYR HB2 H 2.7210 0.05 2 169 111 22 TYR HB3 H 2.5700 0.05 2 170 111 22 TYR HD2 H 6.7260 0.05 3 171 111 22 TYR CA C 56.1060 0.30 1 172 111 22 TYR CB C 43.0800 0.30 1 173 111 22 TYR N N 115.6300 0.50 1 174 112 23 ILE H H 9.8430 0.05 1 175 112 23 ILE HA H 4.7670 0.05 1 176 112 23 ILE HB H 1.8700 0.05 1 177 112 23 ILE HG13 H 0.2790 0.05 2 178 112 23 ILE HG2 H 0.9470 0.05 1 179 112 23 ILE HD1 H 0.2630 0.05 1 180 112 23 ILE CA C 60.5810 0.30 1 181 112 23 ILE CB C 38.8440 0.30 1 182 112 23 ILE CG1 C 26.9350 0.30 1 183 112 23 ILE CG2 C 17.2860 0.30 1 184 112 23 ILE CD1 C 15.4630 0.30 1 185 112 23 ILE N N 125.6310 0.50 1 186 113 24 ASP H H 9.0410 0.05 1 187 113 24 ASP HA H 4.9710 0.05 1 188 113 24 ASP HB2 H 3.3610 0.05 2 189 113 24 ASP HB3 H 2.4930 0.05 2 190 113 24 ASP CA C 51.9380 0.30 1 191 113 24 ASP CB C 42.1850 0.30 1 192 113 24 ASP N N 128.2850 0.50 1 193 114 25 LEU H H 8.5370 0.05 1 194 114 25 LEU HA H 3.9990 0.05 1 195 114 25 LEU HG H 1.6790 0.05 1 196 114 25 LEU HD1 H 0.9360 0.05 2 197 114 25 LEU HD2 H 0.9750 0.05 2 198 114 25 LEU CA C 58.8870 0.30 1 199 114 25 LEU CB C 42.6870 0.30 1 200 114 25 LEU CG C 27.2870 0.30 1 201 114 25 LEU CD1 C 25.3840 0.30 2 202 114 25 LEU CD2 C 24.5240 0.30 2 203 114 25 LEU N N 118.6960 0.50 1 204 115 26 ASP H H 7.9230 0.05 1 205 115 26 ASP HA H 4.3920 0.05 1 206 115 26 ASP HB2 H 2.8050 0.05 2 207 115 26 ASP HB3 H 2.6570 0.05 2 208 115 26 ASP CA C 57.9080 0.30 1 209 115 26 ASP CB C 40.6280 0.30 1 210 115 26 ASP N N 118.2680 0.50 1 211 116 27 GLU H H 8.6690 0.05 1 212 116 27 GLU HA H 4.0120 0.05 1 213 116 27 GLU HB3 H 2.2540 0.05 2 214 116 27 GLU HG3 H 2.8670 0.05 2 215 116 27 GLU CA C 59.1920 0.30 1 216 116 27 GLU CB C 29.4450 0.30 1 217 116 27 GLU CG C 37.8020 0.30 1 218 116 27 GLU N N 121.3430 0.50 1 219 117 28 LEU H H 8.6250 0.05 1 220 117 28 LEU HA H 4.1160 0.05 1 221 117 28 LEU HB2 H 2.0880 0.05 2 222 117 28 LEU HB3 H 1.7800 0.05 2 223 117 28 LEU HG H 1.4920 0.05 1 224 117 28 LEU HD1 H 0.9790 0.05 2 225 117 28 LEU HD2 H 1.0330 0.05 2 226 117 28 LEU CA C 58.5000 0.30 1 227 117 28 LEU CB C 42.0860 0.30 1 228 117 28 LEU CD1 C 26.3470 0.30 2 229 117 28 LEU CD2 C 23.2020 0.30 2 230 117 28 LEU N N 121.2330 0.50 1 231 118 29 LYS H H 8.6120 0.05 1 232 118 29 LYS HA H 3.8330 0.05 1 233 118 29 LYS HB3 H 2.0550 0.05 2 234 118 29 LYS HG3 H 1.3170 0.05 2 235 118 29 LYS HD3 H 1.7410 0.05 2 236 118 29 LYS HE3 H 2.9490 0.05 2 237 118 29 LYS CA C 61.2850 0.30 1 238 118 29 LYS CB C 32.5410 0.30 1 239 118 29 LYS CG C 25.9630 0.30 1 240 118 29 LYS CD C 29.8400 0.30 1 241 118 29 LYS CE C 42.0200 0.30 1 242 118 29 LYS N N 118.7730 0.50 1 243 119 30 ILE H H 8.1800 0.05 1 244 119 30 ILE HA H 3.8170 0.05 1 245 119 30 ILE HB H 1.9250 0.05 1 246 119 30 ILE HG12 H 1.6630 0.05 2 247 119 30 ILE HG13 H 1.2300 0.05 2 248 119 30 ILE HG2 H 0.9480 0.05 1 249 119 30 ILE HD1 H 0.8820 0.05 1 250 119 30 ILE CA C 64.9900 0.30 1 251 119 30 ILE CB C 38.3510 0.30 1 252 119 30 ILE CG1 C 29.4500 0.30 1 253 119 30 ILE CG2 C 17.3400 0.30 1 254 119 30 ILE CD1 C 13.4130 0.30 1 255 119 30 ILE N N 119.3630 0.50 1 256 120 31 MET H H 7.5160 0.05 1 257 120 31 MET HA H 4.2350 0.05 1 258 120 31 MET HB2 H 2.4580 0.05 2 259 120 31 MET HG2 H 2.1220 0.05 2 260 120 31 MET HE H 2.0120 0.05 1 261 120 31 MET CA C 57.1420 0.30 1 262 120 31 MET CB C 31.8090 0.30 1 263 120 31 MET CE C 19.9900 0.30 1 264 120 31 MET N N 119.3600 0.50 1 265 121 32 LEU H H 8.5120 0.05 1 266 121 32 LEU HA H 4.0400 0.05 1 267 121 32 LEU HB2 H 2.0860 0.05 2 268 121 32 LEU HB3 H 1.4370 0.05 2 269 121 32 LEU HG H 1.8590 0.05 1 270 121 32 LEU HD1 H 0.9040 0.05 2 271 121 32 LEU HD2 H 0.9010 0.05 2 272 121 32 LEU CA C 57.5230 0.30 1 273 121 32 LEU CB C 41.8380 0.30 1 274 121 32 LEU CG C 27.1100 0.30 1 275 121 32 LEU CD1 C 27.0360 0.30 2 276 121 32 LEU CD2 C 24.0040 0.30 2 277 121 32 LEU N N 117.9130 0.50 1 278 122 33 GLN H H 8.8440 0.05 1 279 122 33 GLN HA H 4.1210 0.05 1 280 122 33 GLN HB3 H 2.1440 0.05 2 281 122 33 GLN HG2 H 2.5910 0.05 2 282 122 33 GLN HG3 H 2.4580 0.05 2 283 122 33 GLN CA C 58.7580 0.30 1 284 122 33 GLN CB C 28.0980 0.30 1 285 122 33 GLN CG C 34.4300 0.30 1 286 122 33 GLN N N 120.7160 0.50 1 287 123 34 ALA H H 7.6030 0.05 1 288 123 34 ALA HA H 4.3290 0.05 1 289 123 34 ALA HB H 1.6130 0.05 1 290 123 34 ALA CA C 53.6290 0.30 1 291 123 34 ALA CB C 18.4500 0.30 1 292 123 34 ALA N N 121.2420 0.50 1 293 124 35 THR H H 7.5060 0.05 1 294 124 35 THR HA H 4.0590 0.05 1 295 124 35 THR HB H 4.3330 0.05 1 296 124 35 THR HG2 H 1.4480 0.05 1 297 124 35 THR CA C 64.0940 0.30 1 298 124 35 THR CB C 71.2880 0.30 1 299 124 35 THR CG2 C 21.5530 0.30 1 300 124 35 THR N N 106.7380 0.50 1 301 125 36 GLY H H 7.6940 0.05 1 302 125 36 GLY HA2 H 4.2820 0.05 2 303 125 36 GLY HA3 H 3.8180 0.05 2 304 125 36 GLY CA C 45.6170 0.30 1 305 125 36 GLY N N 108.3050 0.50 1 306 126 37 GLU H H 7.5180 0.05 1 307 126 37 GLU HA H 4.3160 0.05 1 308 126 37 GLU HB2 H 2.0720 0.05 2 309 126 37 GLU HB3 H 1.7210 0.05 2 310 126 37 GLU HG3 H 2.3820 0.05 2 311 126 37 GLU CA C 55.1050 0.30 1 312 126 37 GLU CB C 31.1380 0.30 1 313 126 37 GLU CG C 36.6840 0.30 1 314 126 37 GLU N N 120.0890 0.50 1 315 127 38 THR H H 8.6620 0.05 1 316 127 38 THR HA H 4.4450 0.05 1 317 127 38 THR HB H 4.1860 0.05 1 318 127 38 THR HG2 H 1.1690 0.05 1 319 127 38 THR CA C 63.5290 0.30 1 320 127 38 THR CB C 68.6730 0.30 1 321 127 38 THR CG2 C 21.7260 0.30 1 322 127 38 THR N N 119.9090 0.50 1 323 128 39 ILE H H 8.3890 0.05 1 324 128 39 ILE HA H 4.6590 0.05 1 325 128 39 ILE HB H 2.0640 0.05 1 326 128 39 ILE HG12 H 1.5600 0.05 2 327 128 39 ILE HG13 H 0.9350 0.05 2 328 128 39 ILE HG2 H 0.9460 0.05 1 329 128 39 ILE HD1 H 0.6060 0.05 1 330 128 39 ILE CA C 57.6810 0.30 1 331 128 39 ILE CB C 38.3750 0.30 1 332 128 39 ILE CG1 C 25.4550 0.30 1 333 128 39 ILE CG2 C 18.4230 0.30 1 334 128 39 ILE CD1 C 11.3900 0.30 1 335 128 39 ILE N N 128.7060 0.50 1 336 129 40 THR H H 9.7040 0.05 1 337 129 40 THR HB H 4.7390 0.05 1 338 129 40 THR HG2 H 1.2610 0.05 1 339 129 40 THR CA C 59.8580 0.30 1 340 129 40 THR CB C 72.3000 0.30 1 341 129 40 THR CG2 C 21.4560 0.30 1 342 129 40 THR N N 119.8430 0.50 1 343 130 41 GLU H H 8.9290 0.05 1 344 130 41 GLU HA H 4.0470 0.05 1 345 130 41 GLU HB3 H 2.1250 0.05 2 346 130 41 GLU HG3 H 2.3880 0.05 2 347 130 41 GLU CA C 59.8360 0.30 1 348 130 41 GLU CB C 29.1800 0.30 1 349 130 41 GLU CG C 36.6570 0.30 1 350 130 41 GLU N N 119.7390 0.50 1 351 131 42 ASP H H 7.8450 0.05 1 352 131 42 ASP HA H 4.3840 0.05 1 353 131 42 ASP HB3 H 2.4910 0.05 2 354 131 42 ASP CA C 57.4250 0.30 1 355 131 42 ASP CB C 40.8920 0.30 1 356 131 42 ASP N N 117.6730 0.50 1 357 132 43 ASP H H 7.5910 0.05 1 358 132 43 ASP HA H 4.2310 0.05 1 359 132 43 ASP HB2 H 3.2650 0.05 2 360 132 43 ASP HB3 H 2.3140 0.05 2 361 132 43 ASP CA C 58.2300 0.30 1 362 132 43 ASP CB C 42.1000 0.30 1 363 132 43 ASP N N 119.9020 0.50 1 364 133 44 ILE H H 7.1890 0.05 1 365 133 44 ILE HA H 3.3460 0.05 1 366 133 44 ILE HB H 1.8560 0.05 1 367 133 44 ILE HG2 H 0.9210 0.05 1 368 133 44 ILE HD1 H 0.8920 0.05 1 369 133 44 ILE CA C 65.4150 0.30 1 370 133 44 ILE CB C 38.7550 0.30 1 371 133 44 ILE CG1 C 29.7400 0.30 1 372 133 44 ILE CG2 C 18.3650 0.30 1 373 133 44 ILE CD1 C 14.1750 0.30 1 374 133 44 ILE N N 116.6270 0.50 1 375 134 45 GLU H H 8.1630 0.05 1 376 134 45 GLU HA H 3.9020 0.05 1 377 134 45 GLU HB3 H 2.1810 0.05 2 378 134 45 GLU HG3 H 2.4320 0.05 2 379 134 45 GLU CA C 59.6050 0.30 1 380 134 45 GLU CB C 30.1230 0.30 1 381 134 45 GLU CG C 36.4590 0.30 1 382 134 45 GLU N N 117.8670 0.50 1 383 135 46 GLU H H 8.4620 0.05 1 384 135 46 GLU HA H 4.2380 0.05 1 385 135 46 GLU HB3 H 2.0330 0.05 2 386 135 46 GLU HG2 H 2.4600 0.05 2 387 135 46 GLU HG3 H 2.3110 0.05 2 388 135 46 GLU CA C 58.8700 0.30 1 389 135 46 GLU CB C 29.3780 0.30 1 390 135 46 GLU CG C 37.2130 0.30 1 391 135 46 GLU N N 116.2980 0.50 1 392 136 47 LEU H H 8.1300 0.05 1 393 136 47 LEU HA H 4.2690 0.05 1 394 136 47 LEU HB2 H 2.1180 0.05 2 395 136 47 LEU HB3 H 1.5850 0.05 2 396 136 47 LEU HG H 2.3530 0.05 1 397 136 47 LEU HD1 H 0.9990 0.05 2 398 136 47 LEU HD2 H 1.0290 0.05 2 399 136 47 LEU CA C 58.5020 0.30 1 400 136 47 LEU CB C 41.8260 0.30 1 401 136 47 LEU CG C 26.9450 0.30 1 402 136 47 LEU CD1 C 24.4370 0.30 2 403 136 47 LEU CD2 C 26.8210 0.30 2 404 136 47 LEU N N 121.0220 0.50 1 405 137 48 MET H H 8.2000 0.05 1 406 137 48 MET HA H 4.3180 0.05 1 407 137 48 MET HB2 H 2.1770 0.05 2 408 137 48 MET HB3 H 1.9120 0.05 2 409 137 48 MET HG2 H 2.6140 0.05 2 410 137 48 MET HG3 H 2.4610 0.05 2 411 137 48 MET HE H 1.9190 0.05 1 412 137 48 MET CA C 57.7310 0.30 1 413 137 48 MET CB C 30.5590 0.30 1 414 137 48 MET CG C 32.1870 0.30 1 415 137 48 MET CE C 17.5810 0.30 1 416 137 48 MET N N 118.0270 0.50 1 417 138 49 LYS H H 8.0730 0.05 1 418 138 49 LYS HA H 4.0710 0.05 1 419 138 49 LYS HB3 H 1.9090 0.05 2 420 138 49 LYS HG3 H 1.4880 0.05 2 421 138 49 LYS HD3 H 1.6910 0.05 2 422 138 49 LYS HE3 H 2.9700 0.05 2 423 138 49 LYS CA C 59.0120 0.30 1 424 138 49 LYS CB C 32.5970 0.30 1 425 138 49 LYS CG C 25.4400 0.30 1 426 138 49 LYS CD C 29.4210 0.30 1 427 138 49 LYS CE C 42.2300 0.30 1 428 138 49 LYS N N 117.4270 0.50 1 429 139 50 ASP H H 7.6760 0.05 1 430 139 50 ASP HA H 4.3880 0.05 1 431 139 50 ASP HB2 H 3.1480 0.05 2 432 139 50 ASP HB3 H 2.7780 0.05 2 433 139 50 ASP CA C 56.7930 0.30 1 434 139 50 ASP CB C 43.4440 0.30 1 435 139 50 ASP N N 117.3800 0.50 1 436 140 51 GLY H H 7.8780 0.05 1 437 140 51 GLY HA2 H 4.0220 0.05 2 438 140 51 GLY HA3 H 2.7970 0.05 2 439 140 51 GLY CA C 46.3230 0.30 1 440 140 51 GLY N N 101.6920 0.50 1 441 141 52 ASP H H 8.5450 0.05 1 442 141 52 ASP HA H 4.5920 0.05 1 443 141 52 ASP HB2 H 2.9800 0.05 2 444 141 52 ASP HB3 H 2.2600 0.05 2 445 141 52 ASP CA C 53.3030 0.30 1 446 141 52 ASP CB C 39.5240 0.30 1 447 141 52 ASP N N 120.5400 0.50 1 448 142 53 LYS H H 7.7940 0.05 1 449 142 53 LYS HA H 4.1770 0.05 1 450 142 53 LYS HB3 H 1.9590 0.05 2 451 142 53 LYS HG2 H 1.6600 0.05 2 452 142 53 LYS HG3 H 1.4790 0.05 2 453 142 53 LYS HD3 H 1.7160 0.05 2 454 142 53 LYS HE3 H 3.1010 0.05 2 455 142 53 LYS CA C 57.7880 0.30 1 456 142 53 LYS CB C 33.0430 0.30 1 457 142 53 LYS CG C 24.7200 0.30 1 458 142 53 LYS CD C 28.5090 0.30 1 459 142 53 LYS CE C 42.2640 0.30 1 460 142 53 LYS N N 125.9060 0.50 1 461 143 54 ASN H H 8.1200 0.05 1 462 143 54 ASN HA H 4.8200 0.05 1 463 143 54 ASN HB2 H 3.2190 0.05 2 464 143 54 ASN HB3 H 2.8820 0.05 2 465 143 54 ASN CA C 51.6780 0.30 1 466 143 54 ASN CB C 37.1590 0.30 1 467 143 54 ASN N N 113.6880 0.50 1 468 144 55 ASN H H 7.7340 0.05 1 469 144 55 ASN HA H 4.5070 0.05 1 470 144 55 ASN HB2 H 3.0830 0.05 2 471 144 55 ASN HB3 H 2.6430 0.05 2 472 144 55 ASN CA C 55.0710 0.30 1 473 144 55 ASN CB C 38.0190 0.30 1 474 144 55 ASN N N 115.7560 0.50 1 475 145 56 ASP H H 8.6910 0.05 1 476 145 56 ASP HA H 4.7260 0.05 1 477 145 56 ASP HB2 H 3.0300 0.05 2 478 145 56 ASP HB3 H 2.3710 0.05 2 479 145 56 ASP CA C 52.9840 0.30 1 480 145 56 ASP CB C 40.9650 0.30 1 481 145 56 ASP N N 118.4200 0.50 1 482 146 57 GLY H H 10.3080 0.05 1 483 146 57 GLY HA2 H 4.0720 0.05 2 484 146 57 GLY HA3 H 3.4870 0.05 2 485 146 57 GLY CA C 45.7660 0.30 1 486 146 57 GLY N N 112.9330 0.50 1 487 147 58 ARG H H 7.6950 0.05 1 488 147 58 ARG HA H 4.9250 0.05 1 489 147 58 ARG HB3 H 1.5450 0.05 2 490 147 58 ARG HG3 H 1.2800 0.05 2 491 147 58 ARG HD2 H 2.5330 0.05 2 492 147 58 ARG HD3 H 2.2720 0.05 2 493 147 58 ARG CA C 53.9510 0.30 1 494 147 58 ARG CB C 34.3780 0.30 1 495 147 58 ARG CG C 25.8660 0.30 1 496 147 58 ARG CD C 43.1150 0.30 1 497 147 58 ARG N N 115.5730 0.50 1 498 148 59 ILE H H 9.4370 0.05 1 499 148 59 ILE HA H 5.0760 0.05 1 500 148 59 ILE HB H 1.7970 0.05 1 501 148 59 ILE HG2 H 0.9480 0.05 1 502 148 59 ILE HD1 H 0.3450 0.05 1 503 148 59 ILE CA C 60.5590 0.30 1 504 148 59 ILE CB C 39.9970 0.30 1 505 148 59 ILE CG1 C 28.2150 0.30 1 506 148 59 ILE CG2 C 17.2460 0.30 1 507 148 59 ILE CD1 C 13.3560 0.30 1 508 148 59 ILE N N 126.1150 0.50 1 509 149 60 ASP H H 9.3930 0.05 1 510 149 60 ASP HA H 5.1830 0.05 1 511 149 60 ASP HB2 H 3.2670 0.05 2 512 149 60 ASP HB3 H 2.7950 0.05 2 513 149 60 ASP CA C 52.5040 0.30 1 514 149 60 ASP CB C 41.9010 0.30 1 515 149 60 ASP N N 129.2750 0.50 1 516 150 61 TYR H H 8.4470 0.05 1 517 150 61 TYR HB2 H 2.4410 0.05 2 518 150 61 TYR HB3 H 2.1570 0.05 2 519 150 61 TYR HD1 H 6.3670 0.05 3 520 150 61 TYR HE1 H 6.5690 0.05 3 521 150 61 TYR CA C 62.1890 0.30 1 522 150 61 TYR CB C 38.0890 0.30 1 523 150 61 TYR N N 118.6910 0.50 1 524 151 62 ASP H H 7.7510 0.05 1 525 151 62 ASP HA H 4.0850 0.05 1 526 151 62 ASP HB3 H 2.6240 0.05 2 527 151 62 ASP CA C 57.9460 0.30 1 528 151 62 ASP CB C 40.6240 0.30 1 529 151 62 ASP N N 118.1100 0.50 1 530 152 63 GLU H H 8.8860 0.05 1 531 152 63 GLU HA H 4.0440 0.05 1 532 152 63 GLU HB2 H 2.4820 0.05 2 533 152 63 GLU HB3 H 2.2130 0.05 2 534 152 63 GLU HG3 H 3.0020 0.05 2 535 152 63 GLU CA C 58.6840 0.30 1 536 152 63 GLU CB C 29.7090 0.30 1 537 152 63 GLU CG C 37.5150 0.30 1 538 152 63 GLU N N 120.4420 0.50 1 539 153 64 PHE H H 9.3170 0.05 1 540 153 64 PHE HA H 4.0200 0.05 1 541 153 64 PHE HB2 H 3.4340 0.05 2 542 153 64 PHE HB3 H 3.1580 0.05 2 543 153 64 PHE HD1 H 6.8790 0.05 3 544 153 64 PHE HE1 H 7.1200 0.05 3 545 153 64 PHE HZ H 7.4650 0.05 1 546 153 64 PHE CA C 61.7060 0.30 1 547 153 64 PHE CB C 39.7780 0.30 1 548 153 64 PHE N N 125.2490 0.50 1 549 154 65 LEU H H 7.8650 0.05 1 550 154 65 LEU HA H 3.6720 0.05 1 551 154 65 LEU HB2 H 1.8120 0.05 2 552 154 65 LEU HG H 1.2820 0.05 1 553 154 65 LEU HD1 H 0.7380 0.05 2 554 154 65 LEU HD2 H 0.6980 0.05 2 555 154 65 LEU CA C 58.0930 0.30 1 556 154 65 LEU CB C 41.4880 0.30 1 557 154 65 LEU CD1 C 23.1870 0.30 2 558 154 65 LEU CD2 C 25.3130 0.30 2 559 154 65 LEU N N 117.5400 0.50 1 560 155 66 GLU H H 6.9180 0.05 1 561 155 66 GLU HA H 4.0740 0.05 1 562 155 66 GLU HB3 H 2.0730 0.05 2 563 155 66 GLU HG3 H 2.3290 0.05 2 564 155 66 GLU CA C 58.6220 0.30 1 565 155 66 GLU CB C 29.8200 0.30 1 566 155 66 GLU CG C 35.9760 0.30 1 567 155 66 GLU N N 116.2500 0.50 1 568 156 67 PHE H H 8.6130 0.05 1 569 156 67 PHE HA H 4.5990 0.05 1 570 156 67 PHE HB2 H 3.2990 0.05 2 571 156 67 PHE HB3 H 3.0640 0.05 2 572 156 67 PHE HD1 H 7.1180 0.05 3 573 156 67 PHE CA C 58.9370 0.30 1 574 156 67 PHE CB C 40.8040 0.30 1 575 156 67 PHE N N 122.2580 0.50 1 576 157 68 MET H H 7.4720 0.05 1 577 157 68 MET HA H 4.3500 0.05 1 578 157 68 MET HB3 H 1.6450 0.05 2 579 157 68 MET HG2 H 1.8660 0.05 2 580 157 68 MET HG3 H 1.3740 0.05 2 581 157 68 MET HE H 1.0580 0.05 1 582 157 68 MET CA C 52.9810 0.30 1 583 157 68 MET CB C 32.4140 0.30 1 584 157 68 MET CG C 31.9950 0.30 1 585 157 68 MET CE C 15.4770 0.30 1 586 157 68 MET N N 111.7260 0.50 1 587 158 69 LYS H H 7.1520 0.05 1 588 158 69 LYS HA H 4.0060 0.05 1 589 158 69 LYS HB3 H 1.9850 0.05 2 590 158 69 LYS HG3 H 1.4170 0.05 2 591 158 69 LYS HD3 H 1.7120 0.05 2 592 158 69 LYS HE3 H 2.9370 0.05 2 593 158 69 LYS CA C 58.6070 0.30 1 594 158 69 LYS CB C 32.1880 0.30 1 595 158 69 LYS CG C 24.4710 0.30 1 596 158 69 LYS CD C 29.4150 0.30 1 597 158 69 LYS CE C 42.0290 0.30 1 598 158 69 LYS N N 123.7540 0.50 1 599 159 70 GLY H H 8.8620 0.05 1 600 159 70 GLY HA2 H 3.9850 0.05 2 601 159 70 GLY HA3 H 3.7120 0.05 2 602 159 70 GLY CA C 45.4950 0.30 1 603 159 70 GLY N N 112.9750 0.50 1 604 160 71 VAL H H 7.4130 0.05 1 605 160 71 VAL HA H 3.7840 0.05 1 606 160 71 VAL HB H 1.9400 0.05 1 607 160 71 VAL HG1 H 0.6750 0.05 2 608 160 71 VAL HG2 H 0.8640 0.05 2 609 160 71 VAL CA C 63.2510 0.30 1 610 160 71 VAL CB C 31.9760 0.30 1 611 160 71 VAL CG1 C 21.9780 0.30 2 612 160 71 VAL CG2 C 22.0700 0.30 2 613 160 71 VAL N N 121.5100 0.50 1 614 161 72 GLU H H 7.9040 0.05 1 615 161 72 GLU CA C 57.8690 0.30 1 616 161 72 GLU CB C 31.9410 0.30 1 617 161 72 GLU N N 130.5080 0.50 1 stop_ save_