data_7430 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Solution structure of Reduced ERp18 ; _BMRB_accession_number 7430 _BMRB_flat_file_name bmr7430.str _Entry_type original _Submission_date 2008-09-25 _Accession_date 2008-09-25 _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 Rowe Michelle L. . 2 Alanen Heli I. . 3 Ruddock Lloyd W. . 4 Kelly Geoff . . 5 Schmidt Jurgen M. . 6 Williamson Richard A. . 7 Howard Mark J. . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 161 "13C chemical shifts" 287 "15N chemical shifts" 153 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2009-05-25 update author 'complete entry citation' 2009-04-22 original author 'original release' stop_ loop_ _Related_BMRB_accession_number _Relationship 15964 'Oxidised ERp18' stop_ save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title 'Solution Structure and Dynamics of ERp18: a Small ER Resident Oxidoreductase' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 19361226 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Rowe Michelle L. . 2 Ruddock Lloyd W. . 3 Kelly Geoff . . 4 Schmidt Jurgen M. . 5 Williamson Richard A. . 6 Howard Mark J. . stop_ _Journal_abbreviation Biochemistry _Journal_volume 48 _Journal_issue 21 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 4596 _Page_last 4606 _Year 2009 _Details . save_ ####################################### # Cited references within the entry # ####################################### save_reference_citation _Saveframe_category citation _Citation_full . _Citation_title 'Functional Characterization of ERp18, a New Endoplasmic Reticulum-located Thioredoxin Superfamily Member' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 12761212 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Alanen Heli I. . 2 Williamson Richard A. . 3 Howard Mark J. . 4 Lappi Anna-Kaisa . . 5 Jantti Heli P. . 6 Rautio Sini M. . 7 Kellokupu Sakari . . 8 Ruddock Lloyd W. . stop_ _Journal_abbreviation 'J. Biol. Chem.' _Journal_name_full . _Journal_volume 278 _Journal_issue 31 _Journal_CSD . _Book_title . _Book_chapter_title . _Book_volume . _Book_series . _Book_publisher . _Book_publisher_city . _Book_ISBN . _Conference_title . _Conference_site . _Conference_state_province . _Conference_country . _Conference_start_date . _Conference_end_date . _Conference_abstract_number . _Thesis_institution . _Thesis_institution_city . _Thesis_institution_country . _Page_first 28912 _Page_last 28920 _Year 2003 _Details . save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name ERp18 _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label ERp18 $ERp18 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_ERp18 _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common ERp18 _Molecular_mass 17771 _Mol_thiol_state 'all free' _Details 'The molecule contains an N-terminal His-tag (MHHHHHHM) followed by the ERp18 sequence with the first S being residue 24 in full length ERp18 numbering' ############################## # Polymer residue sequence # ############################## _Residue_count 157 _Mol_residue_sequence ; MHHHHHHMSDGHNGLGKGFG DHIHWRTLEDGKKEAAASGL PLMVIIHKSWCGACKALKPK FAESTEISELSHNFVMVNLE DEEEPKDEDFSPDGGYIPRI LFLDPSGKVHPEIINENGNP SYKYFYVSAEQVVQGMKEAQ ERLTGDAFRKKHLEDEL ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 16 MET 2 17 HIS 3 18 HIS 4 19 HIS 5 20 HIS 6 21 HIS 7 22 HIS 8 23 MET 9 24 SER 10 25 ASP 11 26 GLY 12 27 HIS 13 28 ASN 14 29 GLY 15 30 LEU 16 31 GLY 17 32 LYS 18 33 GLY 19 34 PHE 20 35 GLY 21 36 ASP 22 37 HIS 23 38 ILE 24 39 HIS 25 40 TRP 26 41 ARG 27 42 THR 28 43 LEU 29 44 GLU 30 45 ASP 31 46 GLY 32 47 LYS 33 48 LYS 34 49 GLU 35 50 ALA 36 51 ALA 37 52 ALA 38 53 SER 39 54 GLY 40 55 LEU 41 56 PRO 42 57 LEU 43 58 MET 44 59 VAL 45 60 ILE 46 61 ILE 47 62 HIS 48 63 LYS 49 64 SER 50 65 TRP 51 66 CYS 52 67 GLY 53 68 ALA 54 69 CYS 55 70 LYS 56 71 ALA 57 72 LEU 58 73 LYS 59 74 PRO 60 75 LYS 61 76 PHE 62 77 ALA 63 78 GLU 64 79 SER 65 80 THR 66 81 GLU 67 82 ILE 68 83 SER 69 84 GLU 70 85 LEU 71 86 SER 72 87 HIS 73 88 ASN 74 89 PHE 75 90 VAL 76 91 MET 77 92 VAL 78 93 ASN 79 94 LEU 80 95 GLU 81 96 ASP 82 97 GLU 83 98 GLU 84 99 GLU 85 100 PRO 86 101 LYS 87 102 ASP 88 103 GLU 89 104 ASP 90 105 PHE 91 106 SER 92 107 PRO 93 108 ASP 94 109 GLY 95 110 GLY 96 111 TYR 97 112 ILE 98 113 PRO 99 114 ARG 100 115 ILE 101 116 LEU 102 117 PHE 103 118 LEU 104 119 ASP 105 120 PRO 106 121 SER 107 122 GLY 108 123 LYS 109 124 VAL 110 125 HIS 111 126 PRO 112 127 GLU 113 128 ILE 114 129 ILE 115 130 ASN 116 131 GLU 117 132 ASN 118 133 GLY 119 134 ASN 120 135 PRO 121 136 SER 122 137 TYR 123 138 LYS 124 139 TYR 125 140 PHE 126 141 TYR 127 142 VAL 128 143 SER 129 144 ALA 130 145 GLU 131 146 GLN 132 147 VAL 133 148 VAL 134 149 GLN 135 150 GLY 136 151 MET 137 152 LYS 138 153 GLU 139 154 ALA 140 155 GLN 141 156 GLU 142 157 ARG 143 158 LEU 144 159 THR 145 160 GLY 146 161 ASP 147 162 ALA 148 163 PHE 149 164 ARG 150 165 LYS 151 166 LYS 152 167 HIS 153 168 LEU 154 169 GLU 155 170 ASP 156 171 GLU 157 172 LEU stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-01-28 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 15964 ERp18 100.00 157 100.00 100.00 1.85e-111 BMRB 16962 ERp18 100.00 157 100.00 100.00 1.85e-111 PDB 2K8V "Solution Structure Of Oxidised Erp18" 100.00 157 100.00 100.00 1.85e-111 DBJ BAG52132 "unnamed protein product [Homo sapiens]" 94.90 172 100.00 100.00 9.06e-105 GB AAD20035 "Unknown [Homo sapiens]" 94.90 172 100.00 100.00 9.06e-105 GB AAH01493 "Thioredoxin domain containing 12 (endoplasmic reticulum) [Homo sapiens]" 94.90 172 100.00 100.00 9.06e-105 GB AAH08913 "Thioredoxin domain containing 12 (endoplasmic reticulum) [Homo sapiens]" 94.90 172 99.33 99.33 2.15e-103 GB AAH08953 "Thioredoxin domain containing 12 (endoplasmic reticulum) [Homo sapiens]" 94.90 172 100.00 100.00 9.06e-105 GB AAN34781 "thioredoxin-like protein p19 [Homo sapiens]" 94.90 172 100.00 100.00 9.06e-105 REF NP_001253090 "thioredoxin domain containing 12 (endoplasmic reticulum) precursor [Macaca mulatta]" 94.90 172 99.33 100.00 1.46e-104 REF NP_056997 "thioredoxin domain-containing protein 12 precursor [Homo sapiens]" 94.90 172 100.00 100.00 9.06e-105 REF XP_001110583 "PREDICTED: thioredoxin domain-containing protein 12 [Macaca mulatta]" 94.90 208 98.66 100.00 1.31e-103 REF XP_002915769 "PREDICTED: thioredoxin domain-containing protein 12-like isoform 1 [Ailuropoda melanoleuca]" 94.90 172 97.32 99.33 2.60e-102 REF XP_003364421 "PREDICTED: thioredoxin domain-containing protein 12-like isoform X1 [Equus caballus]" 94.90 172 97.99 99.33 8.90e-103 SP O95881 "RecName: Full=Thioredoxin domain-containing protein 12; AltName: Full=Endoplasmic reticulum resident protein 18; Short=ER prote" 94.90 172 100.00 100.00 9.06e-105 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $ERp18 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 $ERp18 'recombinant technology' . Escherichia coli . pHIA128 stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_Reduced_15N_ERp18 _Saveframe_category sample _Sample_type solution _Details 'Sample Reduced prior to concentration using 5 mM DTT' loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $ERp18 0.7-1.5 mM '[U-99% 15N]' 'sodium phosphate' 20 mM 'natural abundance' 'sodium chloride' 100 % 'natural abundance' D2O 10 % 'natural abundance' stop_ save_ save_Reduced_13C_15N_ERp18 _Saveframe_category sample _Sample_type solution _Details 'Sample Reduced prior to concentration using 5 mM DTT' loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $ERp18 0.7-1.5 mM '[U-99% 13C; U-99% 15N]' 'sodium phosphate' 20 mM 'natural abundance' 'sodium chloride' 100 % 'natural abundance' D2O 10 % 'natural abundance' stop_ save_ ############################ # Computer software used # ############################ 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 'chemical shift assignment' 'peak picking' stop_ _Details . save_ save_CCPN_Analysis _Saveframe_category software _Name CCPN_Analysis _Version . loop_ _Vendor _Address _Electronic_address CCPN . . stop_ loop_ _Task 'chemical shift assignment' 'data analysis' 'peak picking' stop_ _Details . save_ save_CNS _Saveframe_category software _Name CNS _Version . loop_ _Vendor _Address _Electronic_address 'Brunger, Adams, Clore, Gros, Nilges and Read' . . stop_ loop_ _Task 'structure solution' stop_ _Details . save_ save_TALOS _Saveframe_category software _Name TALOS _Version . loop_ _Vendor _Address _Electronic_address 'Cornilescu, Delaglio and Bax' . . stop_ loop_ _Task 'geometry optimization' refinement stop_ _Details . save_ save_ProcheckNMR _Saveframe_category software _Name ProcheckNMR _Version . loop_ _Vendor _Address _Electronic_address 'Laskowski and MacArthur' . . stop_ loop_ _Task 'data analysis' validation stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model INOVA _Field_strength 600 _Details 'University of Kent; 5mm HCN z-pulse field gradient probe' save_ save_spectrometer_2 _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model INOVA _Field_strength 800 _Details 'NIMR, Mill Hill' save_ ############################# # NMR applied experiments # ############################# save_2D_1H-15N_HSQC_1 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-15N HSQC' _Sample_label $Reduced_15N_ERp18 save_ save_3D_CBCA(CO)NH_2 _Saveframe_category NMR_applied_experiment _Experiment_name '3D CBCA(CO)NH' _Sample_label $Reduced_13C_15N_ERp18 save_ save_3D_HNCACB_3 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCACB' _Sample_label $Reduced_13C_15N_ERp18 save_ ####################### # Sample conditions # ####################### save_sample_conditions_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units 'ionic strength' 100 . mM pH 6.5 . pH pressure 1 . atm temperature 298 . K 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 C 13 'methyl protons' ppm 0.00 na indirect . . . 0.251449530 DSS H 1 'methyl protons' ppm 0.00 internal direct . . . 1.000000000 DSS N 15 'methyl protons' ppm 0.00 na 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_Reduced_ERp18 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Software_label $NMRPipe $NMRView stop_ loop_ _Experiment_label '2D 1H-15N HSQC' '3D CBCA(CO)NH' '3D HNCACB' stop_ loop_ _Sample_label $Reduced_15N_ERp18 $Reduced_13C_15N_ERp18 stop_ _Sample_conditions_label $sample_conditions_1 _Chem_shift_reference_set_label $chemical_shift_reference_1 _Mol_system_component_name ERp18 _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 22 7 HIS CA C 56.307 0.5 1 2 22 7 HIS CB C 30.341 0.5 1 3 23 8 MET H H 8.449 0.02 1 4 23 8 MET CA C 55.742 0.5 1 5 23 8 MET CB C 32.842 0.5 1 6 23 8 MET N N 122.176 0.5 1 7 24 9 SER H H 8.428 0.02 1 8 24 9 SER CA C 58.412 0.5 1 9 24 9 SER CB C 63.9 0.5 1 10 24 9 SER N N 116.789 0.5 1 11 25 10 ASP H H 8.382 0.02 1 12 25 10 ASP CA C 54.487 0.5 1 13 25 10 ASP CB C 41.285 0.5 1 14 25 10 ASP N N 122.384 0.5 1 15 26 11 GLY H H 8.363 0.02 1 16 26 11 GLY CA C 45.546 0.5 1 17 26 11 GLY N N 108.671 0.5 1 18 27 12 HIS H H 8.35 0.02 1 19 27 12 HIS CA C 56.103 0.5 1 20 27 12 HIS CB C 29.813 0.5 1 21 27 12 HIS N N 118.814 0.5 1 22 28 13 ASN H H 8.505 0.02 1 23 28 13 ASN HD21 H 7.689 0.02 2 24 28 13 ASN HD22 H 7.041 0.02 2 25 28 13 ASN CA C 53.482 0.5 1 26 28 13 ASN CB C 39.386 0.5 1 27 28 13 ASN N N 119.523 0.5 1 28 28 13 ASN ND2 N 113.142 0.5 1 29 29 14 GLY H H 8.743 0.02 1 30 29 14 GLY CA C 45.534 0.5 1 31 29 14 GLY N N 110.136 0.5 1 32 30 15 LEU H H 8.466 0.02 1 33 30 15 LEU CA C 56.146 0.5 5 34 30 15 LEU CB C 42.864 0.5 5 35 30 15 LEU N N 120.511 0.5 1 36 31 16 GLY H H 8.886 0.02 1 37 31 16 GLY CA C 47.064 0.5 1 38 31 16 GLY N N 108.073 0.5 1 39 32 17 LYS H H 7.854 0.02 1 40 32 17 LYS CA C 55.661 0.5 1 41 32 17 LYS CB C 29.379 0.5 1 42 32 17 LYS N N 110.952 0.5 1 43 33 18 GLY H H 8.095 0.02 1 44 33 18 GLY CA C 44.893 0.5 1 45 33 18 GLY N N 103.957 0.5 1 46 34 19 PHE H H 7.887 0.02 1 47 34 19 PHE CA C 61.146 0.5 1 48 34 19 PHE CB C 38.963 0.5 1 49 34 19 PHE N N 117.883 0.5 1 50 35 20 GLY H H 7.696 0.02 1 51 35 20 GLY CA C 45.189 0.5 1 52 35 20 GLY N N 102.668 0.5 1 53 36 21 ASP H H 9.284 0.02 1 54 36 21 ASP CA C 56.026 0.5 1 55 36 21 ASP CB C 40.543 0.5 1 56 36 21 ASP N N 129.289 0.5 1 57 37 22 HIS H H 9.058 0.02 1 58 37 22 HIS CA C 56.628 0.5 1 59 37 22 HIS CB C 29.941 0.5 1 60 37 22 HIS N N 116.742 0.5 1 61 38 23 ILE H H 6.449 0.02 1 62 38 23 ILE CA C 59.183 0.5 1 63 38 23 ILE CB C 39.408 0.5 1 64 38 23 ILE N N 124.704 0.5 1 65 39 24 HIS H H 7.857 0.02 1 66 39 24 HIS CA C 52.931 0.5 1 67 39 24 HIS CB C 28.626 0.5 1 68 39 24 HIS N N 124.6 0.5 1 69 40 25 TRP H H 8.032 0.02 1 70 40 25 TRP HE1 H 10.645 0.02 1 71 40 25 TRP CA C 57.058 0.5 1 72 40 25 TRP CB C 30.411 0.5 1 73 40 25 TRP N N 130.002 0.5 1 74 40 25 TRP NE1 N 132.121 0.5 1 75 41 26 ARG H H 9.131 0.02 1 76 41 26 ARG CA C 54.5 0.5 1 77 41 26 ARG CB C 35.055 0.5 1 78 41 26 ARG N N 122.005 0.5 1 79 42 27 THR H H 8.562 0.02 1 80 42 27 THR CA C 61.294 0.5 1 81 42 27 THR CB C 70.325 0.5 1 82 42 27 THR N N 111.261 0.5 1 83 43 28 LEU H H 8.994 0.02 1 84 43 28 LEU CA C 59.121 0.5 1 85 43 28 LEU CB C 41.515 0.5 1 86 43 28 LEU N N 121.976 0.5 1 87 44 29 GLU H H 8.759 0.02 1 88 44 29 GLU CA C 59.928 0.5 1 89 44 29 GLU CB C 29.342 0.5 1 90 44 29 GLU N N 116.492 0.5 1 91 45 30 ASP H H 7.692 0.02 1 92 45 30 ASP CA C 57.131 0.5 1 93 45 30 ASP CB C 40.093 0.5 1 94 45 30 ASP N N 119.105 0.5 1 95 46 31 GLY H H 9.224 0.02 1 96 46 31 GLY CA C 47.426 0.5 1 97 46 31 GLY N N 111.508 0.5 1 98 47 32 LYS H H 8.691 0.02 1 99 47 32 LYS CA C 60.968 0.5 5 100 47 32 LYS CB C 32.534 0.5 5 101 47 32 LYS N N 121.519 0.5 1 102 48 33 LYS H H 7.234 0.02 1 103 48 33 LYS CA C 59.734 0.5 1 104 48 33 LYS CB C 32.349 0.5 1 105 48 33 LYS N N 119.937 0.5 1 106 49 34 GLU H H 8.179 0.02 1 107 49 34 GLU CA C 58.911 0.5 1 108 49 34 GLU CB C 29.393 0.5 1 109 49 34 GLU N N 121.748 0.5 1 110 50 35 ALA H H 9.142 0.02 1 111 50 35 ALA CA C 56.068 0.5 1 112 50 35 ALA CB C 19.504 0.5 1 113 50 35 ALA N N 125.093 0.5 1 114 51 36 ALA H H 7.548 0.02 1 115 51 36 ALA CA C 54.765 0.5 1 116 51 36 ALA CB C 18.095 0.5 1 117 51 36 ALA N N 118.057 0.5 1 118 52 37 ALA H H 7.517 0.02 1 119 52 37 ALA CA C 54.2 0.5 1 120 52 37 ALA CB C 19.225 0.5 1 121 52 37 ALA N N 118.541 0.5 1 122 53 38 SER H H 8.33 0.02 1 123 53 38 SER CA C 59.095 0.5 1 124 53 38 SER CB C 65.54 0.5 1 125 53 38 SER N N 110.905 0.5 1 126 54 39 GLY H H 8.454 0.02 1 127 54 39 GLY CA C 46.559 0.5 1 128 54 39 GLY N N 112.427 0.5 1 129 55 40 LEU H H 7.58 0.02 1 130 55 40 LEU CA C 51.891 0.5 1 131 55 40 LEU CB C 43.061 0.5 1 132 55 40 LEU N N 121.312 0.5 1 133 56 41 PRO CA C 61.426 0.5 1 134 56 41 PRO CB C 32.878 0.5 1 135 57 42 LEU H H 8.447 0.02 1 136 57 42 LEU CA C 55.025 0.5 1 137 57 42 LEU CB C 44.36 0.5 1 138 57 42 LEU N N 116.186 0.5 1 139 58 43 MET H H 8.61 0.02 1 140 58 43 MET CA C 54.951 0.5 1 141 58 43 MET CB C 34.319 0.5 1 142 58 43 MET N N 124.827 0.5 1 143 59 44 VAL H H 8.766 0.02 1 144 59 44 VAL CA C 60.237 0.5 1 145 59 44 VAL CB C 34.052 0.5 1 146 59 44 VAL N N 125.176 0.5 1 147 60 45 ILE H H 8.512 0.02 1 148 60 45 ILE CA C 60.138 0.5 1 149 60 45 ILE CB C 40.622 0.5 1 150 60 45 ILE N N 125.614 0.5 1 151 61 46 ILE H H 9.528 0.02 1 152 61 46 ILE CA C 61.356 0.5 1 153 61 46 ILE CB C 39.017 0.5 1 154 61 46 ILE N N 130.237 0.5 1 155 62 47 HIS H H 8.926 0.02 1 156 62 47 HIS CA C 54.153 0.5 1 157 62 47 HIS CB C 35.638 0.5 1 158 62 47 HIS N N 121.634 0.5 1 159 63 48 LYS H H 7.798 0.02 1 160 63 48 LYS CA C 52.412 0.5 1 161 63 48 LYS CB C 33.666 0.5 1 162 63 48 LYS N N 116.188 0.5 1 163 64 49 SER H H 10.807 0.02 1 164 64 49 SER CA C 60.779 0.5 1 165 64 49 SER CB C 62.612 0.5 1 166 64 49 SER N N 121.963 0.5 1 167 65 50 TRP H H 6.564 0.02 1 168 65 50 TRP HE1 H 10.456 0.02 1 169 65 50 TRP CA C 54.246 0.5 1 170 65 50 TRP CB C 29.5 0.5 1 171 65 50 TRP N N 115.717 0.5 1 172 65 50 TRP NE1 N 131.544 0.5 1 173 66 51 CYS H H 6.689 0.02 1 174 66 51 CYS CA C 60.195 0.5 1 175 66 51 CYS CB C 30.909 0.5 1 176 66 51 CYS N N 125.894 0.5 1 177 67 52 GLY H H 9.301 0.02 1 178 67 52 GLY CA C 47.51 0.5 1 179 67 52 GLY N N 119.542 0.5 1 180 68 53 ALA H H 9.861 0.02 1 181 68 53 ALA CA C 55.404 0.5 1 182 68 53 ALA CB C 18.521 0.5 1 183 68 53 ALA N N 133.08 0.5 1 184 69 54 CYS H H 9.891 0.02 1 185 69 54 CYS CA C 64.497 0.5 1 186 69 54 CYS CB C 29.057 0.5 1 187 69 54 CYS N N 127.404 0.5 1 188 70 55 LYS H H 8.059 0.02 1 189 70 55 LYS CA C 59.84 0.5 1 190 70 55 LYS CB C 32.942 0.5 1 191 70 55 LYS N N 118.141 0.5 1 192 71 56 ALA H H 7.517 0.02 1 193 71 56 ALA CA C 53.989 0.5 1 194 71 56 ALA CB C 18.501 0.5 1 195 71 56 ALA N N 118.54 0.5 1 196 72 57 LEU H H 7.351 0.02 1 197 72 57 LEU CA C 56.998 0.5 5 198 72 57 LEU CB C 42.256 0.5 5 199 72 57 LEU N N 117.293 0.5 1 200 73 58 LYS H H 7.101 0.02 1 201 73 58 LYS CA C 62.302 0.5 1 202 73 58 LYS CB C 30.098 0.5 1 203 73 58 LYS N N 115.956 0.5 1 204 74 59 PRO CA C 65.581 0.5 1 205 74 59 PRO CB C 30.726 0.5 1 206 75 60 LYS H H 6.694 0.02 1 207 75 60 LYS CA C 58.353 0.5 1 208 75 60 LYS CB C 32.606 0.5 1 209 75 60 LYS N N 115.897 0.5 1 210 76 61 PHE H H 8.285 0.02 1 211 76 61 PHE CA C 60.241 0.5 1 212 76 61 PHE CB C 41.785 0.5 1 213 76 61 PHE N N 120.489 0.5 1 214 77 62 ALA H H 9.036 0.02 1 215 77 62 ALA CA C 55.215 0.5 1 216 77 62 ALA CB C 19.141 0.5 1 217 77 62 ALA N N 119.89 0.5 1 218 78 63 GLU H H 7.541 0.02 1 219 78 63 GLU CA C 55.965 0.5 1 220 78 63 GLU CB C 29.63 0.5 1 221 78 63 GLU N N 111.511 0.5 1 222 79 64 SER H H 6.861 0.02 1 223 79 64 SER CA C 57.323 0.5 1 224 79 64 SER CB C 63.306 0.5 1 225 79 64 SER N N 111.856 0.5 1 226 80 65 THR H H 9.169 0.02 1 227 80 65 THR CA C 65.335 0.5 1 228 80 65 THR CB C 68.216 0.5 1 229 80 65 THR N N 129.658 0.5 1 230 81 66 GLU H H 8.354 0.02 1 231 81 66 GLU CA C 60.236 0.5 1 232 81 66 GLU CB C 30.136 0.5 1 233 81 66 GLU N N 123.573 0.5 1 234 82 67 ILE H H 7.922 0.02 1 235 82 67 ILE CA C 66.084 0.5 1 236 82 67 ILE CB C 37.806 0.5 1 237 82 67 ILE N N 119.503 0.5 1 238 83 68 SER H H 7.214 0.02 1 239 83 68 SER CA C 63.512 0.5 1 240 83 68 SER CB C 62.33 0.5 1 241 83 68 SER N N 112.464 0.5 1 242 84 69 GLU H H 8.224 0.02 1 243 84 69 GLU CA C 59.597 0.5 1 244 84 69 GLU CB C 29.64 0.5 1 245 84 69 GLU N N 120.267 0.5 1 246 85 70 LEU H H 8.455 0.02 1 247 85 70 LEU CA C 57.423 0.5 1 248 85 70 LEU CB C 42.942 0.5 1 249 85 70 LEU N N 119.797 0.5 1 250 86 71 SER H H 8.58 0.02 1 251 86 71 SER CA C 62.31 0.5 1 252 86 71 SER CB C 62.306 0.5 1 253 86 71 SER N N 114.965 0.5 1 254 87 72 HIS H H 7.189 0.02 1 255 87 72 HIS CA C 57.593 0.5 1 256 87 72 HIS CB C 28.816 0.5 1 257 87 72 HIS N N 119.159 0.5 1 258 88 73 ASN H H 8.148 0.02 1 259 88 73 ASN HD21 H 7.33 0.02 2 260 88 73 ASN HD22 H 7.166 0.02 2 261 88 73 ASN CA C 52.994 0.5 1 262 88 73 ASN CB C 38.894 0.5 1 263 88 73 ASN N N 116.602 0.5 1 264 88 73 ASN ND2 N 113.641 0.5 1 265 89 74 PHE H H 7.623 0.02 1 266 89 74 PHE CA C 56.882 0.5 1 267 89 74 PHE CB C 44.873 0.5 1 268 89 74 PHE N N 114.645 0.5 1 269 90 75 VAL H H 8.952 0.02 1 270 90 75 VAL CA C 63.301 0.5 1 271 90 75 VAL CB C 31.213 0.5 1 272 90 75 VAL N N 120.004 0.5 1 273 91 76 MET H H 7.486 0.02 1 274 91 76 MET CA C 53.528 0.5 1 275 91 76 MET CB C 30.717 0.5 1 276 91 76 MET N N 129.189 0.5 1 277 92 77 VAL H H 9.03 0.02 1 278 92 77 VAL CA C 60.953 0.5 1 279 92 77 VAL CB C 37.09 0.5 1 280 92 77 VAL N N 122.955 0.5 1 281 93 78 ASN H H 10.248 0.02 1 282 93 78 ASN HD22 H 6.557 0.02 2 283 93 78 ASN CA C 52.125 0.5 1 284 93 78 ASN CB C 41.857 0.5 1 285 93 78 ASN N N 126.507 0.5 1 286 93 78 ASN ND2 N 112.834 0.5 1 287 94 79 LEU H H 9.104 0.02 1 288 94 79 LEU CA C 52.41 0.5 1 289 94 79 LEU CB C 42.602 0.5 1 290 94 79 LEU N N 123.073 0.5 1 291 95 80 GLU H H 9.161 0.02 1 292 95 80 GLU CA C 53.391 0.5 1 293 95 80 GLU CB C 33.864 0.5 1 294 95 80 GLU N N 125.765 0.5 1 295 96 81 ASP H H 8.107 0.02 1 296 96 81 ASP CA C 57.563 0.5 1 297 96 81 ASP CB C 38.605 0.5 1 298 96 81 ASP N N 126.38 0.5 1 299 97 82 GLU H H 8.836 0.02 1 300 97 82 GLU CA C 58.555 0.5 1 301 97 82 GLU CB C 28.422 0.5 1 302 97 82 GLU N N 123.966 0.5 1 303 98 83 GLU H H 8.215 0.02 1 304 98 83 GLU CA C 56.619 0.5 1 305 98 83 GLU CB C 30.722 0.5 1 306 98 83 GLU N N 118.069 0.5 1 307 99 84 GLU H H 7.298 0.02 1 308 99 84 GLU CA C 54.482 0.5 1 309 99 84 GLU CB C 29.535 0.5 1 310 99 84 GLU N N 119.571 0.5 1 311 100 85 PRO CA C 62.512 0.5 1 312 100 85 PRO CB C 32.805 0.5 1 313 101 86 LYS H H 8.64 0.02 1 314 101 86 LYS CA C 55.615 0.5 1 315 101 86 LYS CB C 31.117 0.5 1 316 101 86 LYS N N 122.999 0.5 1 317 102 87 ASP H H 7.395 0.02 1 318 102 87 ASP CA C 54.233 0.5 1 319 102 87 ASP CB C 42.084 0.5 1 320 102 87 ASP N N 119.006 0.5 1 321 103 88 GLU H H 9.217 0.02 1 322 103 88 GLU CA C 58.996 0.5 1 323 103 88 GLU CB C 29.226 0.5 1 324 103 88 GLU N N 127.412 0.5 1 325 104 89 ASP H H 9.043 0.02 1 326 104 89 ASP CA C 56.138 0.5 1 327 104 89 ASP CB C 39.487 0.5 1 328 104 89 ASP N N 121.056 0.5 1 329 105 90 PHE H H 7.614 0.02 1 330 105 90 PHE CA C 58.124 0.5 1 331 105 90 PHE CB C 38.909 0.5 1 332 105 90 PHE N N 111.473 0.5 1 333 106 91 SER H H 7.907 0.02 1 334 106 91 SER CA C 55.565 0.5 1 335 106 91 SER CB C 63.139 0.5 1 336 106 91 SER N N 115.544 0.5 1 337 107 92 PRO CA C 65.329 0.5 1 338 107 92 PRO CB C 31.501 0.5 1 339 108 93 ASP H H 9.095 0.02 1 340 108 93 ASP CA C 52.726 0.5 1 341 108 93 ASP CB C 40.551 0.5 1 342 108 93 ASP N N 115.482 0.5 1 343 109 94 GLY H H 6.947 0.02 1 344 109 94 GLY CA C 44.385 0.5 1 345 109 94 GLY N N 106.691 0.5 1 346 110 95 GLY H H 8.423 0.02 1 347 110 95 GLY CA C 45.873 0.5 1 348 110 95 GLY N N 107.178 0.5 1 349 111 96 TYR H H 6.407 0.02 1 350 111 96 TYR CA C 55.619 0.5 1 351 111 96 TYR CB C 38.312 0.5 1 352 111 96 TYR N N 116.246 0.5 1 353 112 97 ILE H H 7.878 0.02 1 354 112 97 ILE CA C 58.65 0.5 1 355 112 97 ILE N N 113.713 0.5 1 356 113 98 PRO CA C 62.337 0.5 1 357 113 98 PRO CB C 34.315 0.5 1 358 114 99 ARG H H 8.514 0.02 1 359 114 99 ARG CA C 54.46 0.5 1 360 114 99 ARG CB C 34.399 0.5 1 361 114 99 ARG N N 117.55 0.5 1 362 115 100 ILE H H 8.819 0.02 1 363 115 100 ILE CA C 60.937 0.5 1 364 115 100 ILE CB C 39.021 0.5 1 365 115 100 ILE N N 122.056 0.5 1 366 116 101 LEU H H 8.692 0.02 1 367 116 101 LEU CA C 52.377 0.5 1 368 116 101 LEU CB C 46.493 0.5 1 369 116 101 LEU N N 127.243 0.5 1 370 117 102 PHE H H 9.004 0.02 1 371 117 102 PHE CA C 57.076 0.5 1 372 117 102 PHE CB C 42.048 0.5 1 373 117 102 PHE N N 116.784 0.5 1 374 118 103 LEU H H 9.303 0.02 1 375 118 103 LEU CA C 53.487 0.2 1 376 118 103 LEU CB C 45.454 0.2 1 377 118 103 LEU N N 124.741 0.2 1 378 119 104 ASP H H 8.351 0.02 1 379 119 104 ASP CA C 52.555 0.5 1 380 119 104 ASP CB C 39.406 0.5 1 381 119 104 ASP N N 117.539 0.5 1 382 120 105 PRO CA C 65.106 0.5 1 383 120 105 PRO CB C 31.459 0.5 1 384 121 106 SER H H 8.229 0.02 1 385 121 106 SER CA C 58.891 0.5 1 386 121 106 SER CB C 64.061 0.5 1 387 121 106 SER N N 111.546 0.5 1 388 122 107 GLY H H 8.97 0.02 1 389 122 107 GLY CA C 45.417 0.5 1 390 122 107 GLY N N 111.616 0.5 1 391 123 108 LYS H H 7.405 0.02 1 392 123 108 LYS CA C 54.729 0.5 1 393 123 108 LYS CB C 32.929 0.5 1 394 123 108 LYS N N 120.93 0.5 1 395 124 109 VAL H H 8.875 0.02 1 396 124 109 VAL CA C 64.103 0.5 1 397 124 109 VAL CB C 32.249 0.5 1 398 124 109 VAL N N 126.925 0.5 1 399 125 110 HIS H H 8.911 0.02 1 400 125 110 HIS CA C 54.469 0.5 1 401 125 110 HIS CB C 28.893 0.5 1 402 125 110 HIS N N 127.112 0.5 1 403 126 111 PRO CA C 63.311 0.5 1 404 126 111 PRO CB C 32.232 0.5 1 405 127 112 GLU H H 10.959 0.02 1 406 127 112 GLU CA C 57.439 0.5 1 407 127 112 GLU CB C 27.174 0.5 1 408 127 112 GLU N N 123.144 0.5 1 409 128 113 ILE H H 7.493 0.02 1 410 128 113 ILE CA C 61.518 0.5 1 411 128 113 ILE CB C 35.365 0.5 1 412 128 113 ILE N N 123.479 0.5 1 413 129 114 ILE H H 8.3 0.02 1 414 129 114 ILE CA C 59.109 0.5 1 415 129 114 ILE CB C 42.309 0.5 1 416 129 114 ILE N N 123.439 0.5 1 417 130 115 ASN H H 8.622 0.02 1 418 130 115 ASN HD21 H 7.76 0.02 2 419 130 115 ASN HD22 H 6.108 0.02 2 420 130 115 ASN CA C 51.381 0.5 1 421 130 115 ASN CB C 35.215 0.5 1 422 130 115 ASN N N 114.712 0.5 1 423 130 115 ASN ND2 N 110.191 0.5 1 424 131 116 GLU H H 8.463 0.02 1 425 131 116 GLU CA C 58.882 0.5 1 426 131 116 GLU CB C 29.606 0.5 1 427 131 116 GLU N N 127.9 0.5 1 428 132 117 ASN H H 7.545 0.02 1 429 132 117 ASN HD21 H 7.745 0.02 2 430 132 117 ASN HD22 H 7.146 0.02 2 431 132 117 ASN CA C 52.96 0.5 1 432 132 117 ASN CB C 39.777 0.5 1 433 132 117 ASN N N 113.958 0.5 1 434 132 117 ASN ND2 N 114.32 0.5 1 435 133 118 GLY H H 7.109 0.02 1 436 133 118 GLY CA C 44.662 0.5 1 437 133 118 GLY N N 107.288 0.5 1 438 134 119 ASN H H 8.795 0.02 1 439 134 119 ASN HD21 H 7.839 0.02 2 440 134 119 ASN HD22 H 7.175 0.02 2 441 134 119 ASN CA C 50.277 0.5 1 442 134 119 ASN CB C 40.102 0.5 1 443 134 119 ASN N N 122.889 0.5 1 444 134 119 ASN ND2 N 113.473 0.5 1 445 135 120 PRO CA C 64.32 0.5 1 446 135 120 PRO CB C 31.987 0.5 1 447 136 121 SER H H 8.26 0.02 1 448 136 121 SER CA C 60.199 0.5 1 449 136 121 SER CB C 63.228 0.5 1 450 136 121 SER N N 113.554 0.5 1 451 137 122 TYR H H 7.58 0.02 1 452 137 122 TYR CA C 54.584 0.5 1 453 137 122 TYR CB C 38.872 0.5 1 454 137 122 TYR N N 119.864 0.5 1 455 138 123 LYS H H 9.556 0.02 1 456 138 123 LYS CA C 60.415 0.5 1 457 138 123 LYS CB C 31.945 0.5 1 458 138 123 LYS N N 123.955 0.5 1 459 139 124 TYR H H 8.486 0.02 1 460 139 124 TYR CA C 56.009 0.5 1 461 139 124 TYR CB C 37.666 0.5 1 462 139 124 TYR N N 113.738 0.5 1 463 140 125 PHE H H 7.562 0.02 1 464 140 125 PHE CA C 56.561 0.5 1 465 140 125 PHE CB C 40.897 0.5 1 466 140 125 PHE N N 122.592 0.5 1 467 141 126 TYR H H 8.133 0.02 1 468 141 126 TYR CA C 57.326 0.5 1 469 141 126 TYR CB C 41.768 0.5 1 470 141 126 TYR N N 129.225 0.5 1 471 142 127 VAL H H 8.081 0.02 1 472 142 127 VAL CA C 61.414 0.5 1 473 142 127 VAL CB C 34.245 0.5 1 474 142 127 VAL N N 112.892 0.5 1 475 143 128 SER H H 7.362 0.02 1 476 143 128 SER CA C 55.028 0.5 1 477 143 128 SER CB C 67.261 0.5 1 478 143 128 SER N N 112.848 0.5 1 479 144 129 ALA H H 9.331 0.02 1 480 144 129 ALA CA C 55.568 0.5 1 481 144 129 ALA CB C 18.005 0.5 1 482 144 129 ALA N N 124.25 0.5 1 483 145 130 GLU H H 9.152 0.02 1 484 145 130 GLU CA C 60.626 0.5 1 485 145 130 GLU CB C 28.823 0.5 1 486 145 130 GLU N N 116.98 0.5 1 487 146 131 GLN H H 7.621 0.02 1 488 146 131 GLN HE21 H 7.603 0.02 2 489 146 131 GLN HE22 H 6.948 0.02 2 490 146 131 GLN CA C 58.552 0.5 1 491 146 131 GLN CB C 29.038 0.5 1 492 146 131 GLN N N 117.565 0.5 1 493 146 131 GLN NE2 N 112.41 0.5 1 494 147 132 VAL H H 7.78 0.02 1 495 147 132 VAL CA C 66.928 0.5 1 496 147 132 VAL CB C 31.324 0.5 1 497 147 132 VAL N N 121.486 0.5 1 498 148 133 VAL H H 8.609 0.02 1 499 148 133 VAL CA C 67.053 0.5 1 500 148 133 VAL CB C 31.927 0.5 1 501 148 133 VAL N N 119.56 0.5 1 502 149 134 GLN H H 7.365 0.02 1 503 149 134 GLN HE21 H 6.819 0.02 2 504 149 134 GLN HE22 H 6.271 0.02 2 505 149 134 GLN CA C 59.382 0.5 1 506 149 134 GLN CB C 27.86 0.5 1 507 149 134 GLN N N 117.08 0.5 1 508 149 134 GLN NE2 N 108.294 0.5 1 509 150 135 GLY H H 8.085 0.02 1 510 150 135 GLY CA C 47.499 0.5 1 511 150 135 GLY N N 107.849 0.5 1 512 151 136 MET H H 8.593 0.02 1 513 151 136 MET CA C 59.73 0.5 1 514 151 136 MET CB C 35.435 0.5 1 515 151 136 MET N N 119.39 0.5 1 516 152 137 LYS H H 8.591 0.02 1 517 152 137 LYS CA C 60.659 0.5 5 518 152 137 LYS CB C 32.617 0.5 5 519 152 137 LYS N N 119.226 0.5 1 520 153 138 GLU H H 7.87 0.02 1 521 153 138 GLU CA C 59.134 0.5 1 522 153 138 GLU CB C 28.879 0.5 1 523 153 138 GLU N N 120.709 0.5 1 524 154 139 ALA H H 8.493 0.02 1 525 154 139 ALA CA C 55.45 0.5 1 526 154 139 ALA CB C 18.695 0.5 1 527 154 139 ALA N N 120.598 0.5 1 528 155 140 GLN H H 8.582 0.02 1 529 155 140 GLN HE21 H 7.566 0.02 2 530 155 140 GLN HE22 H 6.983 0.02 2 531 155 140 GLN CA C 59.239 0.5 1 532 155 140 GLN CB C 28.027 0.5 1 533 155 140 GLN N N 116.438 0.5 1 534 155 140 GLN NE2 N 111.746 0.5 1 535 156 141 GLU H H 7.563 0.02 1 536 156 141 GLU CA C 58.896 0.5 1 537 156 141 GLU CB C 29.885 0.5 1 538 156 141 GLU N N 118.759 0.5 1 539 157 142 ARG H H 8.152 0.02 1 540 157 142 ARG CA C 58.08 0.5 1 541 157 142 ARG CB C 31.789 0.5 1 542 157 142 ARG N N 114.735 0.5 1 543 158 143 LEU H H 8.249 0.02 1 544 158 143 LEU CA C 54.749 0.5 1 545 158 143 LEU CB C 42.541 0.5 1 546 158 143 LEU N N 113.493 0.5 1 547 159 144 THR H H 7.007 0.02 1 548 159 144 THR CA C 63.038 0.5 1 549 159 144 THR CB C 69.731 0.5 1 550 159 144 THR N N 111.144 0.5 1 551 160 145 GLY H H 8.683 0.02 1 552 160 145 GLY CA C 45.832 0.5 1 553 160 145 GLY N N 112.264 0.5 1 554 161 146 ASP H H 8.499 0.02 1 555 161 146 ASP CA C 55.669 0.5 1 556 161 146 ASP CB C 41.225 0.5 1 557 161 146 ASP N N 121.131 0.5 1 558 162 147 ALA H H 8.293 0.02 1 559 162 147 ALA CA C 54.292 0.5 1 560 162 147 ALA CB C 18.617 0.5 1 561 162 147 ALA N N 122.285 0.5 1 562 163 148 PHE H H 7.895 0.02 1 563 163 148 PHE CA C 58.513 0.5 1 564 163 148 PHE CB C 39.235 0.5 1 565 163 148 PHE N N 116.233 0.5 1 566 164 149 ARG H H 7.71 0.02 1 567 164 149 ARG CA C 56.771 0.5 1 568 164 149 ARG CB C 30.809 0.5 1 569 164 149 ARG N N 120.439 0.5 1 570 165 150 LYS H H 8.107 0.02 1 571 165 150 LYS CA C 56.765 0.5 5 572 165 150 LYS CB C 32.894 0.5 5 573 165 150 LYS N N 121.264 0.5 1 574 166 151 LYS H H 8.159 0.02 1 575 166 151 LYS CA C 56.657 0.5 5 576 166 151 LYS CB C 33.053 0.5 5 577 166 151 LYS N N 121.969 0.5 1 578 167 152 HIS H H 8.424 0.02 1 579 167 152 HIS CA C 55.868 0.5 1 580 167 152 HIS CB C 29.574 0.5 1 581 167 152 HIS N N 119.99 0.5 1 582 168 153 LEU H H 8.265 0.02 1 583 168 153 LEU CA C 55.699 0.5 1 584 168 153 LEU CB C 42.336 0.5 1 585 168 153 LEU N N 123.679 0.5 1 586 169 154 GLU H H 8.529 0.02 1 587 169 154 GLU CA C 57.112 0.5 1 588 169 154 GLU CB C 29.964 0.5 1 589 169 154 GLU N N 120.238 0.5 1 590 170 155 ASP H H 8.182 0.02 1 591 170 155 ASP CA C 54.682 0.5 1 592 170 155 ASP CB C 41.229 0.5 1 593 170 155 ASP N N 119.994 0.5 1 594 171 156 GLU H H 8.146 0.02 1 595 171 156 GLU CA C 56.436 0.5 1 596 171 156 GLU CB C 30.488 0.5 1 597 171 156 GLU N N 120.779 0.5 1 598 172 157 LEU H H 7.844 0.02 1 599 172 157 LEU CA C 56.587 0.5 1 600 172 157 LEU CB C 43.187 0.5 1 601 172 157 LEU N N 128.867 0.5 1 stop_ loop_ _Atom_shift_assign_ID_ambiguity 33 197 '34,198' '99,517,571,575' '100,518,572,576' stop_ save_