data_18543 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Chemical shift assignments of DsbA(C33S) by solid-state NMR ; _BMRB_accession_number 18543 _BMRB_flat_file_name bmr18543.str _Entry_type original _Submission_date 2012-06-21 _Accession_date 2012-06-21 _Entry_origination author _NMR_STAR_version 2.1.1 _Experimental_method NMR _Details 'Solid-state NMR assignments of nanocrystalline DsbA(C33S) and membrane protein complex DsbA(C33S)/DsbB' loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Sperling Lindsay . . 2 Tang Ming . . 3 Berthold Deborah . . 4 Nesbitt Anna . . 5 Gennis Robert . . 6 Rienstra Chad . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "13C chemical shifts" 518 "15N chemical shifts" 128 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2013-06-05 update BMRB 'update entry citation' 2013-04-02 original author 'original release' stop_ loop_ _Related_BMRB_accession_number _Relationship 16327 'DsbA, wild type oxidized' 18544 'DsbA(C33S)/DsbB complex' stop_ save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title 'Solid-State NMR Study of a 41 kDa Membrane Protein Complex DsbA/DsbB.' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 23527473 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Sperling Lindsay J. . 2 Tang Ming . . 3 Berthold Deborah A. . 4 Nesbitt Anna E. . 5 Gennis Robert B. . 6 Rienstra Chad M. . stop_ _Journal_abbreviation 'J. Phys. Chem. B' _Journal_name_full 'The journal of physical chemistry. B' _Journal_volume 117 _Journal_issue 20 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 6052 _Page_last 6060 _Year 2013 _Details . loop_ _Keyword DsbA/DsbB 'Membrane Protein' 'Solid-state NMR' stop_ save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name 'DsbA(C33S) protein' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label DsbA(C33S) $DsbA(C33S) stop_ _System_molecular_weight 41000 _System_physical_state native _System_oligomer_state ? _System_paramagnetic no _System_thiol_state . _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_DsbA(C33S) _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common DsbA(C33S) _Molecular_mass . _Mol_thiol_state 'all free' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 189 _Mol_residue_sequence ; AQYEDGKQYTTLEKPVAGAP QVLEFFSFFCPHSYQFEEVL HISDNVKKKLPEGVKMTKYH VNFMGGDLGKDLTQAWAVAM ALGVEDKVTVPLFEGVQKTQ TIRSASDIRDVFINAGIKGE EYDAAWNSFVVKSLVAQQEK AAADVQLRGVPAMFVNGKYQ LNPQGMDTSNMDVFVQQYAD TVKYLSEKK ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 1 ALA 2 2 GLN 3 3 TYR 4 4 GLU 5 5 ASP 6 6 GLY 7 7 LYS 8 8 GLN 9 9 TYR 10 10 THR 11 11 THR 12 12 LEU 13 13 GLU 14 14 LYS 15 15 PRO 16 16 VAL 17 17 ALA 18 18 GLY 19 19 ALA 20 20 PRO 21 21 GLN 22 22 VAL 23 23 LEU 24 24 GLU 25 25 PHE 26 26 PHE 27 27 SER 28 28 PHE 29 29 PHE 30 30 CYS 31 31 PRO 32 32 HIS 33 33 SER 34 34 TYR 35 35 GLN 36 36 PHE 37 37 GLU 38 38 GLU 39 39 VAL 40 40 LEU 41 41 HIS 42 42 ILE 43 43 SER 44 44 ASP 45 45 ASN 46 46 VAL 47 47 LYS 48 48 LYS 49 49 LYS 50 50 LEU 51 51 PRO 52 52 GLU 53 53 GLY 54 54 VAL 55 55 LYS 56 56 MET 57 57 THR 58 58 LYS 59 59 TYR 60 60 HIS 61 61 VAL 62 62 ASN 63 63 PHE 64 64 MET 65 65 GLY 66 66 GLY 67 67 ASP 68 68 LEU 69 69 GLY 70 70 LYS 71 71 ASP 72 72 LEU 73 73 THR 74 74 GLN 75 75 ALA 76 76 TRP 77 77 ALA 78 78 VAL 79 79 ALA 80 80 MET 81 81 ALA 82 82 LEU 83 83 GLY 84 84 VAL 85 85 GLU 86 86 ASP 87 87 LYS 88 88 VAL 89 89 THR 90 90 VAL 91 91 PRO 92 92 LEU 93 93 PHE 94 94 GLU 95 95 GLY 96 96 VAL 97 97 GLN 98 98 LYS 99 99 THR 100 100 GLN 101 101 THR 102 102 ILE 103 103 ARG 104 104 SER 105 105 ALA 106 106 SER 107 107 ASP 108 108 ILE 109 109 ARG 110 110 ASP 111 111 VAL 112 112 PHE 113 113 ILE 114 114 ASN 115 115 ALA 116 116 GLY 117 117 ILE 118 118 LYS 119 119 GLY 120 120 GLU 121 121 GLU 122 122 TYR 123 123 ASP 124 124 ALA 125 125 ALA 126 126 TRP 127 127 ASN 128 128 SER 129 129 PHE 130 130 VAL 131 131 VAL 132 132 LYS 133 133 SER 134 134 LEU 135 135 VAL 136 136 ALA 137 137 GLN 138 138 GLN 139 139 GLU 140 140 LYS 141 141 ALA 142 142 ALA 143 143 ALA 144 144 ASP 145 145 VAL 146 146 GLN 147 147 LEU 148 148 ARG 149 149 GLY 150 150 VAL 151 151 PRO 152 152 ALA 153 153 MET 154 154 PHE 155 155 VAL 156 156 ASN 157 157 GLY 158 158 LYS 159 159 TYR 160 160 GLN 161 161 LEU 162 162 ASN 163 163 PRO 164 164 GLN 165 165 GLY 166 166 MET 167 167 ASP 168 168 THR 169 169 SER 170 170 ASN 171 171 MET 172 172 ASP 173 173 VAL 174 174 PHE 175 175 VAL 176 176 GLN 177 177 GLN 178 178 TYR 179 179 ALA 180 180 ASP 181 181 THR 182 182 VAL 183 183 LYS 184 184 TYR 185 185 LEU 186 186 SER 187 187 GLU 188 188 LYS 189 189 LYS stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-09-16 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 16327 DsbA 100.00 189 99.47 99.47 2.39e-135 BMRB 17710 DsbA 99.47 188 99.47 99.47 9.06e-135 BMRB 18396 oxidized_DsbA 100.00 189 98.94 99.47 9.91e-135 BMRB 18544 DsbA(C33S) 100.00 189 100.00 100.00 3.94e-136 PDB 1A23 "Solution Nmr Structure Of Reduced Dsba From Escherichia Coli, Minimized Average Structure" 100.00 189 99.47 99.47 2.39e-135 PDB 1A24 "Solution Nmr Structure Of Reduced Dsba From Escherichia Coli, Family Of 20 Structures" 100.00 189 99.47 99.47 2.39e-135 PDB 1A2J "Oxidized Dsba Crystal Form Ii" 100.00 189 99.47 99.47 2.39e-135 PDB 1A2L "Reduced Dsba At 2.7 Angstroms Resolution" 100.00 189 99.47 99.47 2.39e-135 PDB 1A2M "Oxidized Dsba At 2.7 Angstroms Resolution, Crystal Form Iii" 100.00 189 99.47 99.47 2.39e-135 PDB 1AC1 "Dsba Mutant H32l" 100.00 189 98.94 98.94 7.33e-134 PDB 1ACV "Dsba Mutant H32s" 100.00 189 98.94 98.94 4.63e-134 PDB 1BQ7 "Dsba Mutant P151a, Role Of The Cis-Proline In The Active Site Of Dsba" 100.00 189 98.94 98.94 2.65e-134 PDB 1DSB "Crystal Structure Of The Dsba Protein Required For Disulphide Bond Formation In Vivo" 100.00 189 99.47 99.47 2.39e-135 PDB 1FVJ "The 2.06 Angstrom Structure Of The H32y Mutant Of The Disulfide Bond Formation Protein (Dsba)" 100.00 189 98.94 99.47 2.20e-134 PDB 1FVK "The 1.7 Angstrom Structure Of Wild Type Disulfide Bond Formation Protein (Dsba)" 100.00 189 99.47 99.47 2.39e-135 PDB 1TI1 "Crystal Structure Of A Mutant Dsba" 100.00 189 99.47 100.00 1.27e-135 PDB 1U3A "Mutant Dsba" 100.00 189 99.47 100.00 1.27e-135 PDB 2B3S "Structure Of The Dsba Mutant (P31g-C33a)" 100.00 189 98.94 99.47 3.23e-134 PDB 2B6M "Structure Of The Dsba Mutant (P31a-C33a)" 100.00 189 98.94 99.47 1.41e-134 PDB 2HI7 "Crystal Structure Of Dsba-Dsbb-Ubiquinone Complex" 100.00 189 99.47 100.00 1.27e-135 PDB 2LEG "Membrane Protein Complex Dsbb-Dsba Structure By Joint Calculations With Solid-State Nmr And X-Ray Experimental Data" 100.00 189 99.47 100.00 1.27e-135 PDB 2ZUP "Updated Crystal Structure Of Dsbb-Dsba Complex From E. Coli" 100.00 189 99.47 100.00 1.27e-135 PDB 3DKS "Dsba Substrate Complex" 100.00 189 98.94 99.47 9.08e-135 PDB 3E9J "Structure Of The Charge-Transfer Intermediate Of The Transmembrane Redox Catalyst Dsbb" 100.00 189 99.47 100.00 1.27e-135 PDB 4TKY "The Complex Structure Of E. Coli Dsba Bound To A Peptide At The Dsba/dsbb Interface" 100.00 191 99.47 100.00 7.62e-136 PDB 4WET "Crystal Structure Of E.coli Dsba In Complex With Compound 16" 100.00 189 99.47 99.47 2.39e-135 PDB 4WEY "Crystal Structure Of E.coli Dsba In Complex With Compound 17" 100.00 189 99.47 99.47 2.39e-135 PDB 4WF4 "Crystal Structure Of E.coli Dsba Co-crystallised In Complex With Compound 4" 100.00 189 99.47 99.47 2.39e-135 PDB 4WF5 "Crystal Structure Of E.coli Dsba Soaked With Compound 4" 100.00 189 99.47 99.47 2.39e-135 DBJ BAB38206 "protein disulfide isomerase I [Escherichia coli O157:H7 str. Sakai]" 100.00 208 99.47 99.47 2.08e-135 DBJ BAE77448 "periplasmic protein disulfide isomerase I [Escherichia coli str. K12 substr. W3110]" 100.00 208 99.47 99.47 2.08e-135 DBJ BAG79665 "protein disulfide isomerase I [Escherichia coli SE11]" 100.00 208 99.47 99.47 2.08e-135 DBJ BAI27892 "periplasmic protein disulfide isomerase I [Escherichia coli O26:H11 str. 11368]" 100.00 208 99.47 99.47 2.08e-135 DBJ BAI33015 "periplasmic protein disulfide isomerase I [Escherichia coli O103:H2 str. 12009]" 100.00 208 99.47 99.47 2.08e-135 EMBL CAA44868 "PpfA protein [Escherichia coli K-12]" 100.00 208 99.47 99.47 2.08e-135 EMBL CAA56736 "dsbA [Escherichia coli K-12]" 100.00 208 99.47 99.47 2.08e-135 EMBL CAA90910 "DsbA protein [Escherichia coli]" 100.00 208 98.94 99.47 7.46e-135 EMBL CAP78318 "Thiol:disulfide interchange protein dsbA [Escherichia coli LF82]" 100.00 208 98.94 99.47 7.46e-135 EMBL CAQ34212 "protein disulfide oxidoreductase [Escherichia coli BL21(DE3)]" 100.00 208 99.47 99.47 2.08e-135 GB AAA23715 "putative [Escherichia coli]" 100.00 208 99.47 99.47 2.08e-135 GB AAB02995 "dsbA [Escherichia coli str. K-12 substr. MG1655]" 100.00 208 99.47 99.47 2.08e-135 GB AAC43519 "thiol:disulfide interchange protein DsbA mutant PH31/32PP [Escherichia coli]" 100.00 208 98.94 98.94 9.53e-134 GB AAC43520 "thiol:disulfide interchange protein DsbA mutant PH31/32TR [Escherichia coli]" 100.00 208 98.41 98.41 2.81e-133 GB AAC43521 "thiol:disulfide interchange protein DsbA mutant PH31/32LQ [Escherichia coli]" 100.00 208 98.41 98.41 5.36e-133 REF NP_312810 "protein disulfide isomerase I [Escherichia coli O157:H7 str. Sakai]" 100.00 208 99.47 99.47 2.08e-135 REF NP_418297 "periplasmic protein disulfide isomerase I [Escherichia coli str. K-12 substr. MG1655]" 100.00 208 99.47 99.47 2.08e-135 REF NP_709659 "periplasmic protein disulfide isomerase I [Shigella flexneri 2a str. 301]" 100.00 208 98.94 99.47 7.97e-135 REF WP_000725331 "thiol-disulfide isomerase [Shigella boydii]" 100.00 208 98.41 98.94 2.30e-134 REF WP_000725332 "thiol:disulfide interchange protein DsbA [Escherichia coli]" 100.00 208 98.94 99.47 2.55e-135 SP P0A4L5 "RecName: Full=Thiol:disulfide interchange protein DsbA; Flags: Precursor" 100.00 208 98.94 99.47 7.46e-135 SP P0A4L6 "RecName: Full=Thiol:disulfide interchange protein DsbA; Flags: Precursor" 100.00 208 98.94 99.47 7.46e-135 SP P0AEG4 "RecName: Full=Thiol:disulfide interchange protein DsbA; Flags: Precursor" 100.00 208 99.47 99.47 2.08e-135 SP P0AEG5 "RecName: Full=Thiol:disulfide interchange protein DsbA; Flags: Precursor" 100.00 208 99.47 99.47 2.08e-135 SP P52235 "RecName: Full=Thiol:disulfide interchange protein DsbA; Flags: Precursor" 100.00 208 98.94 99.47 7.97e-135 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $DsbA(C33S) Enterobacteria 562 Bacteria . Escherichia coli 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 $DsbA(C33S) 'recombinant technology' . Escherichia coli . pQE70 stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Saveframe_category sample _Sample_type solid _Details 'nanocrystalline DsbA(C33S)' loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $DsbA(C33S) 15 mg '[U-100% 13C; U-100% 15N]' H2O 90 % 'natural abundance' D2O 10 % [U-2H] stop_ save_ ############################ # Computer software used # ############################ save_VNMRJ _Saveframe_category software _Name VNMRJ _Version 3.1 loop_ _Vendor _Address _Electronic_address Varian . . stop_ loop_ _Task collection 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_SPARKY _Saveframe_category software _Name SPARKY _Version . loop_ _Vendor _Address _Electronic_address Goddard . . stop_ loop_ _Task 'chemical shift assignment' 'data analysis' 'peak picking' stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model VXRS _Field_strength 500 _Details . save_ ############################# # NMR applied experiments # ############################# save_3D_NCACX_1 _Saveframe_category NMR_applied_experiment _Experiment_name '3D NCACX' _Sample_label $sample_1 save_ save_3D_NCOCX_2 _Saveframe_category NMR_applied_experiment _Experiment_name '3D NCOCX' _Sample_label $sample_1 save_ save_2D_CC_3 _Saveframe_category NMR_applied_experiment _Experiment_name '2D CC' _Sample_label $sample_1 save_ save_2D_TEDOR_4 _Saveframe_category NMR_applied_experiment _Experiment_name '2D TEDOR' _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 pH 7.4 . pH pressure 1 . atm temperature 263 . K stop_ save_ save_sample_conditions_2 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 7.4 . pH pressure 1 . atm temperature 253 . 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 other other . 0.251449530 DSS N 15 'methyl protons' ppm 0.00 na indirect other other . 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_1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Experiment_label '3D NCACX' '3D NCOCX' stop_ loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $sample_conditions_1 _Chem_shift_reference_set_label $chemical_shift_reference_1 _Mol_system_component_name DsbA(C33S) _Text_data_format . _Text_data . loop_ _Atom_shift_assign_ID _Residue_author_seq_code _Residue_seq_code _Residue_label _Atom_name _Atom_type _Chem_shift_value _Chem_shift_value_error _Chem_shift_ambiguity_code 1 1 1 ALA CA C 51.458 0.30 1 2 1 1 ALA CB C 19.737 0.30 1 3 2 2 GLN C C 179.750 0.30 1 4 2 2 GLN CA C 59.815 0.30 1 5 2 2 GLN CB C 29.891 0.30 1 6 2 2 GLN CG C 32.485 0.30 1 7 2 2 GLN N N 121.171 0.30 1 8 3 3 TYR C C 176.938 0.30 1 9 3 3 TYR CA C 57.911 0.30 1 10 3 3 TYR CB C 40.489 0.30 1 11 3 3 TYR N N 121.707 0.30 1 12 4 4 GLU C C 174.586 0.30 1 13 4 4 GLU CA C 54.912 0.30 1 14 4 4 GLU CB C 33.806 0.30 1 15 4 4 GLU N N 122.755 0.30 1 16 5 5 ASP C C 177.361 0.30 1 17 5 5 ASP CA C 55.296 0.30 1 18 5 5 ASP CB C 41.388 0.30 1 19 5 5 ASP CG C 179.726 0.30 1 20 5 5 ASP N N 125.539 0.30 1 21 6 6 GLY C C 173.482 0.30 1 22 6 6 GLY CA C 44.911 0.30 1 23 6 6 GLY N N 116.854 0.30 1 24 7 7 LYS C C 175.438 0.30 1 25 7 7 LYS CA C 56.798 0.30 1 26 7 7 LYS CB C 32.206 0.30 1 27 7 7 LYS N N 122.043 0.30 1 28 8 8 GLN C C 174.182 0.30 1 29 8 8 GLN CA C 59.412 0.30 1 30 8 8 GLN CB C 27.100 0.30 1 31 8 8 GLN CG C 34.022 0.30 1 32 8 8 GLN N N 115.615 0.30 1 33 9 9 TYR C C 172.132 0.30 1 34 9 9 TYR CA C 55.102 0.30 1 35 9 9 TYR CB C 41.562 0.30 1 36 9 9 TYR CD1 C 132.294 0.30 3 37 9 9 TYR CE1 C 116.886 0.30 1 38 9 9 TYR CE2 C 116.886 0.30 1 39 9 9 TYR CZ C 158.147 0.30 1 40 9 9 TYR N N 111.606 0.30 1 41 10 10 THR C C 174.496 0.30 1 42 10 10 THR CA C 60.258 0.30 1 43 10 10 THR CB C 71.482 0.30 1 44 10 10 THR CG2 C 22.083 0.30 1 45 10 10 THR N N 111.517 0.30 1 46 11 11 THR C C 175.324 0.30 1 47 11 11 THR CA C 62.815 0.30 1 48 11 11 THR CB C 69.609 0.30 1 49 11 11 THR CG2 C 21.782 0.30 1 50 11 11 THR N N 120.997 0.30 1 51 12 12 LEU C C 177.401 0.30 1 52 12 12 LEU CA C 55.832 0.30 1 53 12 12 LEU CB C 41.606 0.30 1 54 12 12 LEU CG C 28.533 0.30 1 55 12 12 LEU CD1 C 24.601 0.30 1 56 12 12 LEU CD2 C 23.474 0.30 2 57 12 12 LEU N N 129.187 0.30 1 58 13 13 GLU C C 176.790 0.30 1 59 13 13 GLU CA C 58.721 0.30 1 60 13 13 GLU CB C 29.775 0.30 1 61 13 13 GLU N N 123.113 0.30 1 62 14 14 LYS C C 172.429 0.30 1 63 14 14 LYS CA C 52.304 0.30 1 64 14 14 LYS CB C 32.905 0.30 1 65 14 14 LYS CG C 24.440 0.30 1 66 14 14 LYS N N 117.657 0.30 1 67 15 15 PRO C C 176.412 0.30 1 68 15 15 PRO CA C 62.328 0.30 1 69 15 15 PRO CB C 32.653 0.30 1 70 15 15 PRO CG C 27.202 0.30 1 71 15 15 PRO CD C 50.734 0.30 1 72 15 15 PRO N N 135.650 0.30 1 73 16 16 VAL C C 176.008 0.30 1 74 16 16 VAL CA C 61.443 0.30 1 75 16 16 VAL CB C 32.778 0.30 1 76 16 16 VAL CG1 C 21.534 0.30 2 77 16 16 VAL CG2 C 21.555 0.30 2 78 16 16 VAL N N 123.263 0.30 1 79 17 17 ALA C C 178.952 0.30 1 80 17 17 ALA CA C 52.406 0.30 1 81 17 17 ALA CB C 18.886 0.30 1 82 17 17 ALA N N 132.328 0.30 1 83 18 18 GLY C C 174.000 0.30 1 84 18 18 GLY CA C 45.612 0.30 1 85 18 18 GLY N N 110.605 0.30 1 86 19 19 ALA C C 175.143 0.30 1 87 19 19 ALA CA C 50.243 0.30 1 88 19 19 ALA CB C 17.254 0.30 1 89 19 19 ALA N N 122.370 0.30 1 90 20 20 PRO CA C 62.310 0.30 1 91 20 20 PRO CB C 31.986 0.30 1 92 20 20 PRO CG C 27.823 0.30 1 93 20 20 PRO CD C 50.189 0.30 1 94 20 20 PRO N N 134.046 0.30 1 95 21 21 GLN C C 176.824 0.30 1 96 21 21 GLN CA C 60.088 0.30 1 97 21 21 GLN CB C 29.558 0.30 1 98 21 21 GLN CG C 31.832 0.30 1 99 21 21 GLN N N 121.846 0.30 1 100 22 22 VAL C C 172.959 0.30 1 101 22 22 VAL CA C 62.723 0.30 1 102 22 22 VAL CB C 33.562 0.30 1 103 22 22 VAL CG1 C 22.959 0.30 2 104 22 22 VAL CG2 C 21.328 0.30 2 105 22 22 VAL N N 116.011 0.30 1 106 23 23 LEU C C 173.441 0.30 1 107 23 23 LEU CA C 52.768 0.30 1 108 23 23 LEU CB C 46.120 0.30 1 109 23 23 LEU CG C 26.470 0.30 1 110 23 23 LEU CD1 C 22.358 0.30 1 111 23 23 LEU CD2 C 22.358 0.30 1 112 23 23 LEU N N 128.870 0.30 1 113 26 26 PHE C C 170.243 0.30 1 114 26 26 PHE CA C 54.800 0.30 1 115 27 27 SER C C 177.315 0.30 1 116 27 27 SER CA C 54.926 0.30 1 117 27 27 SER CB C 65.327 0.30 1 118 27 27 SER N N 108.245 0.30 1 119 28 28 PHE N N 131.123 0.30 1 120 31 31 PRO CA C 66.300 0.30 1 121 31 31 PRO CB C 32.265 0.30 1 122 31 31 PRO CG C 27.034 0.30 1 123 31 31 PRO CD C 51.602 0.30 1 124 31 31 PRO N N 146.652 0.30 1 125 32 32 HIS CA C 58.600 0.30 1 126 32 32 HIS CB C 29.688 0.30 1 127 32 32 HIS N N 120.465 0.30 1 128 33 33 SER CA C 63.509 0.30 1 129 33 33 SER CB C 65.105 0.30 1 130 39 39 VAL C C 176.841 0.30 1 131 39 39 VAL CA C 63.965 0.30 1 132 39 39 VAL CB C 32.407 0.30 1 133 39 39 VAL CG1 C 20.848 0.30 2 134 39 39 VAL N N 116.596 0.30 1 135 40 40 LEU C C 177.017 0.30 1 136 40 40 LEU CA C 55.158 0.30 1 137 40 40 LEU CB C 42.718 0.30 1 138 40 40 LEU CG C 27.163 0.30 1 139 40 40 LEU CD1 C 26.036 0.30 1 140 40 40 LEU CD2 C 26.036 0.30 1 141 40 40 LEU N N 114.924 0.30 1 142 44 44 ASP C C 178.435 0.30 1 143 44 44 ASP CA C 57.423 0.30 1 144 44 44 ASP CB C 40.196 0.30 1 145 44 44 ASP N N 120.797 0.30 1 146 46 46 VAL C C 177.949 0.30 1 147 46 46 VAL CA C 67.000 0.30 1 148 46 46 VAL CB C 31.500 0.30 1 149 46 46 VAL CG1 C 23.800 0.30 2 150 46 46 VAL CG2 C 22.500 0.30 2 151 46 46 VAL N N 120.200 0.30 1 152 47 47 LYS C C 179.295 0.30 1 153 47 47 LYS CA C 60.497 0.30 1 154 47 47 LYS CB C 32.153 0.30 1 155 47 47 LYS CG C 25.063 0.30 1 156 47 47 LYS N N 120.454 0.30 1 157 48 48 LYS C C 177.599 0.30 1 158 48 48 LYS CA C 58.474 0.30 1 159 48 48 LYS CB C 32.926 0.30 1 160 48 48 LYS CG C 25.527 0.30 1 161 48 48 LYS N N 115.412 0.30 1 162 49 49 LYS C C 176.229 0.30 1 163 49 49 LYS CA C 55.461 0.30 1 164 49 49 LYS CB C 34.277 0.30 1 165 49 49 LYS CG C 25.915 0.30 1 166 49 49 LYS N N 116.509 0.30 1 167 50 50 LEU CA C 53.330 0.30 1 168 50 50 LEU CB C 41.271 0.30 1 169 50 50 LEU CG C 25.864 0.30 1 170 50 50 LEU N N 120.267 0.30 1 171 51 51 PRO CA C 65.437 0.30 1 172 51 51 PRO CB C 32.376 0.30 1 173 51 51 PRO CG C 28.377 0.30 1 174 51 51 PRO CD C 52.693 0.30 1 175 51 51 PRO N N 152.954 0.30 1 176 52 52 GLU C C 179.651 0.30 1 177 52 52 GLU CA C 59.344 0.30 1 178 52 52 GLU CB C 28.114 0.30 1 179 52 52 GLU CG C 34.438 0.30 1 180 52 52 GLU N N 119.551 0.30 1 181 53 53 GLY C C 174.200 0.30 1 182 53 53 GLY CA C 45.678 0.30 1 183 53 53 GLY N N 110.735 0.30 1 184 54 54 VAL C C 174.617 0.30 1 185 54 54 VAL CA C 62.455 0.30 1 186 54 54 VAL CB C 32.060 0.30 1 187 54 54 VAL CG1 C 22.073 0.30 2 188 54 54 VAL N N 121.881 0.30 1 189 57 57 THR C C 171.806 0.30 1 190 57 57 THR CA C 62.875 0.30 1 191 57 57 THR CB C 70.478 0.30 1 192 57 57 THR CG2 C 22.783 0.30 1 193 57 57 THR N N 124.982 0.30 1 194 59 59 TYR CA C 52.104 0.30 1 195 61 61 VAL C C 176.453 0.30 1 196 61 61 VAL CA C 57.799 0.30 1 197 61 61 VAL CB C 33.749 0.30 1 198 61 61 VAL N N 110.625 0.30 1 199 65 65 GLY C C 176.579 0.30 1 200 65 65 GLY CA C 47.542 0.30 1 201 66 66 GLY CA C 45.600 0.30 1 202 67 67 ASP C C 178.257 0.30 1 203 67 67 ASP CA C 57.751 0.30 1 204 67 67 ASP CB C 39.841 0.30 1 205 67 67 ASP N N 128.168 0.30 1 206 68 68 LEU C C 179.000 0.30 1 207 68 68 LEU CA C 57.200 0.30 1 208 68 68 LEU CB C 42.377 0.30 1 209 68 68 LEU CG C 27.309 0.30 1 210 68 68 LEU N N 120.300 0.30 1 211 69 69 GLY C C 176.007 0.30 1 212 69 69 GLY CA C 48.134 0.30 1 213 69 69 GLY N N 106.875 0.30 1 214 70 70 LYS CA C 59.800 0.30 1 215 70 70 LYS CG C 25.300 0.30 1 216 70 70 LYS N N 121.113 0.30 1 217 72 72 LEU CB C 42.505 0.30 1 218 72 72 LEU CG C 28.272 0.30 1 219 73 73 THR C C 176.502 0.30 1 220 73 73 THR CA C 67.105 0.30 1 221 73 73 THR CB C 68.438 0.30 1 222 73 73 THR CG2 C 22.447 0.30 1 223 73 73 THR N N 119.711 0.30 1 224 74 74 GLN C C 177.512 0.30 1 225 74 74 GLN CA C 59.465 0.30 1 226 74 74 GLN CB C 25.947 0.30 1 227 74 74 GLN CG C 30.989 0.30 1 228 74 74 GLN CD C 177.356 0.30 1 229 74 74 GLN N N 125.222 0.30 1 230 74 74 GLN NE2 N 107.938 0.30 1 231 75 75 ALA C C 179.736 0.30 1 232 75 75 ALA CA C 54.856 0.30 1 233 75 75 ALA CB C 20.057 0.30 1 234 75 75 ALA N N 123.350 0.30 1 235 76 76 TRP C C 177.913 0.30 1 236 76 76 TRP CA C 59.249 0.30 1 237 76 76 TRP CB C 29.371 0.30 1 238 76 76 TRP N N 120.686 0.30 1 239 77 77 ALA C C 178.995 0.30 1 240 77 77 ALA CA C 55.110 0.30 1 241 77 77 ALA CB C 20.271 0.30 1 242 77 77 ALA N N 120.437 0.30 1 243 78 78 VAL C C 177.465 0.30 1 244 78 78 VAL CA C 67.215 0.30 1 245 78 78 VAL CB C 30.271 0.30 1 246 78 78 VAL CG1 C 23.754 0.30 2 247 78 78 VAL CG2 C 22.314 0.30 2 248 78 78 VAL N N 119.708 0.30 1 249 79 79 ALA C C 179.909 0.30 1 250 79 79 ALA CA C 54.954 0.30 1 251 79 79 ALA CB C 17.777 0.30 1 252 79 79 ALA N N 121.045 0.30 1 253 80 80 MET C C 179.384 0.30 1 254 80 80 MET CA C 58.561 0.30 1 255 80 80 MET CB C 34.424 0.30 1 256 80 80 MET CG C 31.166 0.30 1 257 80 80 MET N N 115.866 0.30 1 258 81 81 ALA C C 180.077 0.30 1 259 81 81 ALA CA C 54.659 0.30 1 260 81 81 ALA CB C 18.093 0.30 1 261 81 81 ALA N N 123.576 0.30 1 262 82 82 LEU C C 177.539 0.30 1 263 82 82 LEU CA C 54.567 0.30 1 264 82 82 LEU CB C 43.050 0.30 1 265 82 82 LEU CG C 26.746 0.30 1 266 82 82 LEU CD1 C 21.965 0.30 1 267 82 82 LEU CD2 C 21.965 0.30 1 268 82 82 LEU N N 113.424 0.30 1 269 83 83 GLY C C 176.806 0.30 1 270 83 83 GLY CA C 47.162 0.30 1 271 83 83 GLY N N 110.919 0.30 1 272 84 84 VAL C C 176.659 0.30 1 273 84 84 VAL CA C 59.287 0.30 1 274 84 84 VAL CB C 31.548 0.30 1 275 84 84 VAL CG1 C 20.423 0.30 2 276 84 84 VAL CG2 C 19.175 0.30 2 277 84 84 VAL N N 108.499 0.30 1 278 85 85 GLU C C 179.571 0.30 1 279 85 85 GLU CA C 61.714 0.30 1 280 85 85 GLU CB C 29.523 0.30 1 281 85 85 GLU CG C 36.201 0.30 1 282 85 85 GLU CD C 183.923 0.30 1 283 85 85 GLU N N 126.358 0.30 1 284 86 86 ASP C C 177.332 0.30 1 285 86 86 ASP CA C 56.098 0.30 1 286 86 86 ASP CB C 39.714 0.30 1 287 86 86 ASP CG C 180.132 0.30 1 288 86 86 ASP N N 116.172 0.30 1 289 87 87 LYS C C 177.969 0.30 1 290 87 87 LYS CA C 57.262 0.30 1 291 87 87 LYS CB C 34.053 0.30 1 292 87 87 LYS CG C 25.164 0.30 1 293 87 87 LYS CD C 29.327 0.30 1 294 87 87 LYS CE C 39.843 0.30 1 295 87 87 LYS N N 117.216 0.30 1 296 88 88 VAL C C 176.109 0.30 1 297 88 88 VAL CA C 60.914 0.30 1 298 88 88 VAL CB C 32.866 0.30 1 299 88 88 VAL CG1 C 19.422 0.30 2 300 88 88 VAL CG2 C 17.633 0.30 2 301 88 88 VAL N N 103.704 0.30 1 302 89 89 THR C C 175.041 0.30 1 303 89 89 THR CA C 69.428 0.30 1 304 89 89 THR CB C 69.707 0.30 1 305 89 89 THR CG2 C 21.382 0.30 1 306 89 89 THR N N 120.153 0.30 1 307 90 90 VAL C C 175.895 0.30 1 308 90 90 VAL CA C 69.172 0.30 1 309 90 90 VAL CB C 28.841 0.30 1 310 90 90 VAL CG1 C 24.254 0.30 2 311 90 90 VAL CG2 C 21.419 0.30 2 312 90 90 VAL N N 120.200 0.30 1 313 91 91 PRO CA C 65.686 0.30 1 314 91 91 PRO CB C 31.589 0.30 1 315 91 91 PRO CG C 27.811 0.30 1 316 91 91 PRO CD C 49.104 0.30 1 317 91 91 PRO N N 134.100 0.30 1 318 92 92 LEU C C 177.880 0.30 1 319 92 92 LEU CA C 57.941 0.30 1 320 92 92 LEU CB C 40.794 0.30 1 321 92 92 LEU CG C 27.025 0.30 1 322 92 92 LEU CD1 C 23.053 0.30 1 323 92 92 LEU CD2 C 23.053 0.30 1 324 92 92 LEU N N 120.185 0.30 1 325 94 94 GLU C C 180.303 0.30 1 326 94 94 GLU CA C 59.535 0.30 1 327 94 94 GLU CB C 29.558 0.30 1 328 94 94 GLU CD C 177.439 0.30 1 329 94 94 GLU N N 115.917 0.30 1 330 95 95 GLY C C 175.813 0.30 1 331 95 95 GLY CA C 46.435 0.30 1 332 95 95 GLY N N 107.985 0.30 1 333 96 96 VAL C C 177.899 0.30 1 334 96 96 VAL CA C 66.431 0.30 1 335 96 96 VAL CB C 32.022 0.30 1 336 96 96 VAL CG1 C 23.486 0.30 2 337 96 96 VAL CG2 C 21.612 0.30 2 338 96 96 VAL N N 119.865 0.30 1 339 97 97 GLN CA C 54.900 0.30 1 340 97 97 GLN CD C 172.000 0.30 1 341 97 97 GLN NE2 N 111.200 0.30 1 342 99 99 THR C C 175.705 0.30 1 343 99 99 THR CA C 62.151 0.30 1 344 99 99 THR CB C 68.734 0.30 1 345 99 99 THR CG2 C 22.288 0.30 1 346 99 99 THR N N 107.814 0.30 1 347 100 100 GLN C C 175.203 0.30 1 348 100 100 GLN CA C 57.492 0.30 1 349 100 100 GLN CB C 25.782 0.30 1 350 100 100 GLN CG C 34.391 0.30 1 351 100 100 GLN CD C 180.725 0.30 1 352 100 100 GLN N N 114.569 0.30 1 353 101 101 THR C C 175.507 0.30 1 354 101 101 THR CA C 60.965 0.30 1 355 101 101 THR CB C 68.644 0.30 1 356 101 101 THR CG2 C 22.759 0.30 1 357 101 101 THR N N 105.838 0.30 1 358 102 102 ILE C C 174.014 0.30 1 359 102 102 ILE CA C 60.761 0.30 1 360 102 102 ILE CB C 37.116 0.30 1 361 102 102 ILE CG1 C 27.128 0.30 1 362 102 102 ILE CG2 C 17.441 0.30 1 363 102 102 ILE CD1 C 14.586 0.30 1 364 102 102 ILE N N 121.067 0.30 1 365 103 103 ARG C C 175.372 0.30 1 366 103 103 ARG CA C 55.146 0.30 1 367 103 103 ARG CB C 32.428 0.30 1 368 103 103 ARG CG C 27.045 0.30 1 369 103 103 ARG N N 125.864 0.30 1 370 104 104 SER C C 174.454 0.30 1 371 104 104 SER CA C 56.762 0.30 1 372 104 104 SER CB C 67.126 0.30 1 373 104 104 SER N N 114.873 0.30 1 374 105 105 ALA C C 180.877 0.30 1 375 105 105 ALA CA C 55.250 0.30 1 376 105 105 ALA CB C 17.033 0.30 1 377 105 105 ALA N N 123.572 0.30 1 378 106 106 SER C C 176.280 0.30 1 379 106 106 SER CA C 61.351 0.30 1 380 106 106 SER CB C 62.196 0.30 1 381 106 106 SER N N 115.731 0.30 1 382 107 107 ASP C C 179.080 0.30 1 383 107 107 ASP CA C 57.070 0.30 1 384 107 107 ASP CB C 42.577 0.30 1 385 107 107 ASP N N 120.249 0.30 1 386 108 108 ILE C C 176.989 0.30 1 387 108 108 ILE CA C 65.825 0.30 1 388 108 108 ILE CB C 38.163 0.30 1 389 108 108 ILE CG1 C 28.922 0.30 1 390 108 108 ILE CG2 C 18.646 0.30 1 391 108 108 ILE CD1 C 15.220 0.30 1 392 108 108 ILE N N 119.990 0.30 1 393 109 109 ARG CA C 59.572 0.30 1 394 109 109 ARG CD C 43.310 0.30 1 395 110 110 ASP C C 179.249 0.30 1 396 110 110 ASP CA C 57.586 0.30 1 397 110 110 ASP CB C 40.187 0.30 1 398 110 110 ASP N N 117.237 0.30 1 399 111 111 VAL C C 179.159 0.30 1 400 111 111 VAL CA C 66.436 0.30 1 401 111 111 VAL CB C 30.900 0.30 1 402 111 111 VAL CG1 C 23.513 0.30 2 403 111 111 VAL CG2 C 21.665 0.30 2 404 111 111 VAL N N 120.156 0.30 1 405 113 113 ILE C C 182.271 0.30 1 406 113 113 ILE CA C 63.548 0.30 1 407 113 113 ILE CB C 37.765 0.30 1 408 113 113 ILE CG1 C 28.265 0.30 1 409 113 113 ILE CG2 C 17.400 0.30 1 410 113 113 ILE CD1 C 13.433 0.30 1 411 113 113 ILE N N 122.071 0.30 1 412 114 114 ASN CA C 55.576 0.30 1 413 114 114 ASN CB C 38.057 0.30 1 414 114 114 ASN N N 120.304 0.30 1 415 115 115 ALA C C 176.949 0.30 1 416 115 115 ALA CA C 51.865 0.30 1 417 115 115 ALA CB C 18.661 0.30 1 418 115 115 ALA N N 120.866 0.30 1 419 116 116 GLY C C 173.774 0.30 1 420 116 116 GLY CA C 45.142 0.30 1 421 116 116 GLY N N 105.391 0.30 1 422 117 117 ILE C C 175.152 0.30 1 423 117 117 ILE CA C 60.823 0.30 1 424 117 117 ILE CB C 37.462 0.30 1 425 117 117 ILE CG1 C 25.753 0.30 1 426 117 117 ILE CG2 C 20.574 0.30 1 427 117 117 ILE CD1 C 14.704 0.30 1 428 117 117 ILE N N 125.335 0.30 1 429 118 118 LYS C C 179.153 0.30 1 430 118 118 LYS CA C 56.654 0.30 1 431 118 118 LYS CB C 32.499 0.30 1 432 118 118 LYS CG C 25.457 0.30 1 433 118 118 LYS N N 126.118 0.30 1 434 119 119 GLY C C 175.015 0.30 1 435 119 119 GLY CA C 48.213 0.30 1 436 119 119 GLY N N 113.905 0.30 1 437 120 120 GLU CA C 59.581 0.30 1 438 120 120 GLU CB C 28.966 0.30 1 439 120 120 GLU N N 117.303 0.30 1 440 123 123 ASP C C 179.880 0.30 1 441 123 123 ASP CA C 57.366 0.30 1 442 123 123 ASP CB C 39.742 0.30 1 443 123 123 ASP N N 118.922 0.30 1 444 124 124 ALA C C 181.181 0.30 1 445 124 124 ALA CA C 54.643 0.30 1 446 124 124 ALA CB C 18.159 0.30 1 447 124 124 ALA N N 121.027 0.30 1 448 125 125 ALA C C 181.029 0.30 1 449 125 125 ALA CA C 54.921 0.30 1 450 125 125 ALA CB C 18.452 0.30 1 451 125 125 ALA N N 119.653 0.30 1 452 126 126 TRP C C 175.882 0.30 1 453 126 126 TRP CA C 61.166 0.30 1 454 127 127 ASN C C 174.615 0.30 1 455 127 127 ASN CA C 53.188 0.30 1 456 127 127 ASN CB C 40.156 0.30 1 457 127 127 ASN CG C 177.557 0.30 1 458 127 127 ASN N N 110.518 0.30 1 459 128 128 SER C C 175.614 0.30 1 460 128 128 SER CA C 59.100 0.30 1 461 128 128 SER CB C 65.612 0.30 1 462 128 128 SER N N 116.107 0.30 1 463 130 130 VAL CA C 67.100 0.30 1 464 131 131 VAL C C 177.700 0.30 1 465 131 131 VAL CA C 66.969 0.30 1 466 131 131 VAL CB C 31.529 0.30 1 467 131 131 VAL CG1 C 24.200 0.30 2 468 131 131 VAL CG2 C 22.900 0.30 2 469 131 131 VAL N N 120.594 0.30 1 470 133 133 SER CA C 61.228 0.30 1 471 133 133 SER CB C 62.422 0.30 1 472 134 134 LEU C C 181.386 0.30 1 473 134 134 LEU CA C 57.596 0.30 1 474 134 134 LEU CB C 43.960 0.30 1 475 134 134 LEU CG C 27.321 0.30 1 476 134 134 LEU CD1 C 22.897 0.30 1 477 134 134 LEU CD2 C 26.172 0.30 2 478 134 134 LEU N N 123.770 0.30 1 479 135 135 VAL C C 177.053 0.30 1 480 135 135 VAL CA C 68.960 0.30 1 481 135 135 VAL CB C 31.380 0.30 1 482 135 135 VAL CG1 C 23.797 0.30 2 483 135 135 VAL CG2 C 20.951 0.30 2 484 135 135 VAL N N 123.151 0.30 1 485 136 136 ALA C C 181.298 0.30 1 486 136 136 ALA CA C 54.941 0.30 1 487 136 136 ALA CB C 17.751 0.30 1 488 136 136 ALA N N 121.086 0.30 1 489 137 137 GLN C C 179.218 0.30 1 490 137 137 GLN CA C 59.150 0.30 1 491 137 137 GLN CB C 29.480 0.30 1 492 137 137 GLN N N 118.446 0.30 1 493 140 140 LYS CA C 58.811 0.30 1 494 140 140 LYS CB C 32.872 0.30 1 495 140 140 LYS CG C 24.819 0.30 1 496 140 140 LYS CD C 36.425 0.30 1 497 140 140 LYS CE C 42.366 0.30 1 498 140 140 LYS N N 122.187 0.30 1 499 141 141 ALA C C 179.440 0.30 1 500 141 141 ALA CA C 54.832 0.30 1 501 141 141 ALA CB C 18.298 0.30 1 502 142 142 ALA C C 178.825 0.30 1 503 142 142 ALA CA C 54.523 0.30 1 504 142 142 ALA CB C 17.889 0.30 1 505 142 142 ALA N N 116.973 0.30 1 506 143 143 ALA CA C 54.374 0.30 1 507 143 143 ALA CB C 17.953 0.30 1 508 143 143 ALA N N 120.256 0.30 1 509 144 144 ASP C C 178.286 0.30 1 510 144 144 ASP CA C 57.117 0.30 1 511 144 144 ASP CB C 40.034 0.30 1 512 145 145 VAL C C 174.268 0.30 1 513 145 145 VAL CA C 60.381 0.30 1 514 145 145 VAL CB C 30.887 0.30 1 515 145 145 VAL CG1 C 20.072 0.30 2 516 145 145 VAL CG2 C 19.130 0.30 2 517 145 145 VAL N N 108.467 0.30 1 518 146 146 GLN C C 175.328 0.30 1 519 146 146 GLN CA C 56.006 0.30 1 520 147 147 LEU CB C 43.032 0.30 1 521 147 147 LEU CG C 26.963 0.30 1 522 148 148 ARG C C 175.716 0.30 1 523 148 148 ARG CA C 54.630 0.30 1 524 148 148 ARG CB C 31.844 0.30 1 525 149 149 GLY C C 170.860 0.30 1 526 149 149 GLY CA C 45.168 0.30 1 527 149 149 GLY N N 105.616 0.30 1 528 150 150 VAL C C 173.007 0.30 1 529 150 150 VAL CA C 58.061 0.30 1 530 150 150 VAL CB C 35.028 0.30 1 531 150 150 VAL N N 110.477 0.30 1 532 152 152 ALA C C 174.774 0.30 1 533 152 152 ALA CA C 51.739 0.30 1 534 152 152 ALA CB C 25.293 0.30 1 535 153 153 MET C C 173.438 0.30 1 536 153 153 MET CB C 37.158 0.30 1 537 153 153 MET CG C 32.455 0.30 1 538 153 153 MET N N 121.304 0.30 1 539 155 155 VAL C C 176.081 0.30 1 540 155 155 VAL CA C 60.738 0.30 1 541 155 155 VAL CB C 34.794 0.30 1 542 155 155 VAL CG1 C 22.797 0.30 2 543 155 155 VAL CG2 C 20.495 0.30 2 544 155 155 VAL N N 123.034 0.30 1 545 156 156 ASN C C 174.193 0.30 1 546 156 156 ASN CA C 54.546 0.30 1 547 156 156 ASN CB C 37.337 0.30 1 548 156 156 ASN CG C 177.389 0.30 1 549 156 156 ASN N N 127.219 0.30 1 550 157 157 GLY C C 172.478 0.30 1 551 157 157 GLY CA C 46.392 0.30 1 552 157 157 GLY N N 105.259 0.30 1 553 158 158 LYS CA C 57.117 0.30 1 554 158 158 LYS CB C 37.324 0.30 1 555 158 158 LYS CG C 29.877 0.30 1 556 158 158 LYS N N 114.470 0.30 1 557 159 159 TYR C C 174.853 0.30 1 558 160 160 GLN C C 175.490 0.30 1 559 160 160 GLN CA C 53.406 0.30 1 560 160 160 GLN CB C 30.662 0.30 1 561 160 160 GLN CG C 32.483 0.30 1 562 160 160 GLN CD C 179.251 0.30 1 563 160 160 GLN N N 124.898 0.30 1 564 160 160 GLN NE2 N 108.307 0.30 1 565 161 161 LEU C C 177.480 0.30 1 566 161 161 LEU CA C 54.093 0.30 1 567 161 161 LEU CB C 40.838 0.30 1 568 161 161 LEU CG C 27.879 0.30 1 569 161 161 LEU CD1 C 24.185 0.30 1 570 161 161 LEU CD2 C 24.185 0.30 1 571 161 161 LEU N N 131.282 0.30 1 572 162 162 ASN C C 172.167 0.30 1 573 162 162 ASN CA C 49.993 0.30 1 574 162 162 ASN CB C 38.601 0.30 1 575 162 162 ASN N N 118.500 0.30 1 576 163 163 PRO CA C 64.800 0.30 1 577 163 163 PRO CB C 32.400 0.30 1 578 163 163 PRO CG C 27.892 0.30 1 579 163 163 PRO CD C 50.845 0.30 1 580 163 163 PRO N N 137.100 0.30 1 581 164 164 GLN C C 177.104 0.30 1 582 164 164 GLN CA C 57.638 0.30 1 583 164 164 GLN CB C 27.915 0.30 1 584 165 165 GLY C C 173.932 0.30 1 585 165 165 GLY CA C 44.720 0.30 1 586 165 165 GLY N N 106.700 0.30 1 587 166 166 MET N N 119.240 0.30 1 588 168 168 THR C C 175.645 0.30 1 589 168 168 THR CA C 60.794 0.30 1 590 168 168 THR CB C 68.554 0.30 1 591 168 168 THR N N 112.325 0.30 1 592 169 169 SER CA C 61.352 0.30 1 593 169 169 SER CB C 63.344 0.30 1 594 173 173 VAL CA C 65.729 0.30 1 595 173 173 VAL CB C 32.062 0.30 1 596 173 173 VAL CG1 C 22.379 0.30 2 597 173 173 VAL CG2 C 21.224 0.30 2 598 173 173 VAL N N 121.383 0.30 1 599 174 174 PHE CB C 27.900 0.30 1 600 175 175 VAL C C 177.693 0.30 1 601 175 175 VAL CA C 66.916 0.30 1 602 175 175 VAL CB C 31.784 0.30 1 603 175 175 VAL CG1 C 21.241 0.30 2 604 175 175 VAL CG2 C 24.102 0.30 2 605 175 175 VAL N N 117.001 0.30 1 606 176 176 GLN CA C 59.062 0.30 1 607 176 176 GLN CB C 27.711 0.30 1 608 176 176 GLN CG C 34.173 0.30 1 609 176 176 GLN CD C 180.000 0.30 1 610 176 176 GLN N N 116.511 0.30 1 611 176 176 GLN NE2 N 110.792 0.30 1 612 177 177 GLN C C 179.997 0.30 1 613 177 177 GLN CA C 59.039 0.30 1 614 177 177 GLN CB C 28.047 0.30 1 615 177 177 GLN CG C 34.200 0.30 1 616 178 178 TYR C C 178.114 0.30 1 617 178 178 TYR CA C 61.700 0.30 1 618 178 178 TYR N N 126.422 0.30 1 619 179 179 ALA C C 179.720 0.30 1 620 179 179 ALA CA C 55.266 0.30 1 621 179 179 ALA CB C 18.301 0.30 1 622 180 180 ASP N N 118.836 0.30 1 623 181 181 THR CB C 67.457 0.30 1 624 181 181 THR CG2 C 21.804 0.30 1 625 182 182 VAL CA C 67.772 0.30 1 626 182 182 VAL CB C 30.796 0.30 1 627 182 182 VAL CG1 C 24.154 0.30 2 628 182 182 VAL CG2 C 22.867 0.30 2 629 182 182 VAL N N 121.432 0.30 1 630 184 184 TYR C C 177.858 0.30 1 631 184 184 TYR CA C 59.909 0.30 1 632 185 185 LEU C C 178.477 0.30 1 633 185 185 LEU CA C 56.442 0.30 1 634 185 185 LEU CB C 42.463 0.30 1 635 185 185 LEU CG C 25.667 0.30 1 636 185 185 LEU CD1 C 23.503 0.30 1 637 185 185 LEU CD2 C 23.503 0.30 1 638 185 185 LEU N N 118.123 0.30 1 639 186 186 SER CA C 61.946 0.30 1 640 186 186 SER CB C 62.533 0.30 1 641 186 186 SER N N 114.977 0.30 1 642 187 187 GLU CA C 56.009 0.30 1 643 187 187 GLU CB C 30.411 0.30 1 644 187 187 GLU CG C 36.722 0.30 1 645 187 187 GLU N N 119.458 0.30 1 646 188 188 LYS CA C 57.552 0.30 1 stop_ save_