data_16327 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; DsbA wild type oxidized ; _BMRB_accession_number 16327 _BMRB_flat_file_name bmr16327.str _Entry_type original _Submission_date 2009-05-29 _Accession_date 2009-05-29 _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 Sperling Lindsay J. . 2 Berthold Deborah A. . 3 Sasser Terry L. . 4 Jeisy-Scott Vistoria . . 5 Rienstra Chad M. . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "13C chemical shifts" 694 "15N chemical shifts" 172 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2010-10-24 update author 'update the entry citation' 2010-02-11 update author 'update the chemical shifts' 2010-02-03 update BMRB 'complete entry citation' 2009-12-18 original author 'original release' stop_ save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title 'Assignment Strategies for Large Proteins by Magic-Angle Spinning NMR: The 21-kDa Disulfide-Bond-Forming Enzyme DsbA' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 20394752 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Sperling Lindsay J. . 2 Berthold Deborah A. . 3 Sasser Terry L. . 4 Jeisy-Scott Victoria J. . 5 Rienstra Chad M. . stop_ _Journal_abbreviation 'J. Mol. Biol.' _Journal_volume 399 _Journal_issue 2 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 268 _Page_last 282 _Year 2010 _Details . save_ ####################################### # Cited references within the entry # ####################################### save_reference_citation _Saveframe_category citation _Citation_full . _Citation_title 'High resolution NMR spectroscopy of nanocrystalline proteins at ultra-high magnetic field.' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 19953303 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Sperling Lindsay J. . 2 Nieuwkoop Andrew J. . 3 Lipton Andrew S. . 4 Berthold Deborah A. . 5 Rienstra Chad M. . stop_ _Journal_abbreviation 'J. Biomol. NMR' _Journal_name_full 'Journal of biomolecular NMR' _Journal_volume 46 _Journal_issue 2 _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 149 _Page_last 155 _Year 2010 _Details . save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name DsbA _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label DsbA $DsbA stop_ _System_molecular_weight 21000 _System_physical_state native _System_oligomer_state ? _System_paramagnetic no _System_thiol_state . _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_DsbA _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common DsbA _Molecular_mass 21000 _Mol_thiol_state 'all disulfide bound' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 189 _Mol_residue_sequence ; AQYEDGKQYTTLEKPVAGAP QVLEFFSFFCPHCYQFEEVL HISDNVKKKLPEGVKMTKYH VNFMGGDLGKDLTQAWAVAM ALGVEDKVTVPLFEGVQKTQ TIRSASDIRDVFINAGIKGE EYDAAWNSFVVKSLVAQQEK AAADVQLRGVPAMFVNGKYQ LNPQGMDTSNMDVFVQQYAD TVKYLSEKK ; loop_ _Residue_seq_code _Residue_label 1 ALA 2 GLN 3 TYR 4 GLU 5 ASP 6 GLY 7 LYS 8 GLN 9 TYR 10 THR 11 THR 12 LEU 13 GLU 14 LYS 15 PRO 16 VAL 17 ALA 18 GLY 19 ALA 20 PRO 21 GLN 22 VAL 23 LEU 24 GLU 25 PHE 26 PHE 27 SER 28 PHE 29 PHE 30 CYS 31 PRO 32 HIS 33 CYS 34 TYR 35 GLN 36 PHE 37 GLU 38 GLU 39 VAL 40 LEU 41 HIS 42 ILE 43 SER 44 ASP 45 ASN 46 VAL 47 LYS 48 LYS 49 LYS 50 LEU 51 PRO 52 GLU 53 GLY 54 VAL 55 LYS 56 MET 57 THR 58 LYS 59 TYR 60 HIS 61 VAL 62 ASN 63 PHE 64 MET 65 GLY 66 GLY 67 ASP 68 LEU 69 GLY 70 LYS 71 ASP 72 LEU 73 THR 74 GLN 75 ALA 76 TRP 77 ALA 78 VAL 79 ALA 80 MET 81 ALA 82 LEU 83 GLY 84 VAL 85 GLU 86 ASP 87 LYS 88 VAL 89 THR 90 VAL 91 PRO 92 LEU 93 PHE 94 GLU 95 GLY 96 VAL 97 GLN 98 LYS 99 THR 100 GLN 101 THR 102 ILE 103 ARG 104 SER 105 ALA 106 SER 107 ASP 108 ILE 109 ARG 110 ASP 111 VAL 112 PHE 113 ILE 114 ASN 115 ALA 116 GLY 117 ILE 118 LYS 119 GLY 120 GLU 121 GLU 122 TYR 123 ASP 124 ALA 125 ALA 126 TRP 127 ASN 128 SER 129 PHE 130 VAL 131 VAL 132 LYS 133 SER 134 LEU 135 VAL 136 ALA 137 GLN 138 GLN 139 GLU 140 LYS 141 ALA 142 ALA 143 ALA 144 ASP 145 VAL 146 GLN 147 LEU 148 ARG 149 GLY 150 VAL 151 PRO 152 ALA 153 MET 154 PHE 155 VAL 156 ASN 157 GLY 158 LYS 159 TYR 160 GLN 161 LEU 162 ASN 163 PRO 164 GLN 165 GLY 166 MET 167 ASP 168 THR 169 SER 170 ASN 171 MET 172 ASP 173 VAL 174 PHE 175 VAL 176 GLN 177 GLN 178 TYR 179 ALA 180 ASP 181 THR 182 VAL 183 LYS 184 TYR 185 LEU 186 SER 187 GLU 188 LYS 189 LYS stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-09-09 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 17710 DsbA 99.47 188 100.00 100.00 9.85e-136 BMRB 18396 oxidized_DsbA 100.00 189 99.47 100.00 4.85e-136 BMRB 18543 DsbA(C33S) 100.00 189 99.47 99.47 2.37e-135 BMRB 18544 DsbA(C33S) 100.00 189 99.47 99.47 2.37e-135 PDB 1A23 "Solution Nmr Structure Of Reduced Dsba From Escherichia Coli, Minimized Average Structure" 100.00 189 100.00 100.00 1.28e-136 PDB 1A24 "Solution Nmr Structure Of Reduced Dsba From Escherichia Coli, Family Of 20 Structures" 100.00 189 100.00 100.00 1.28e-136 PDB 1A2J "Oxidized Dsba Crystal Form Ii" 100.00 189 100.00 100.00 1.28e-136 PDB 1A2L "Reduced Dsba At 2.7 Angstroms Resolution" 100.00 189 100.00 100.00 1.28e-136 PDB 1A2M "Oxidized Dsba At 2.7 Angstroms Resolution, Crystal Form Iii" 100.00 189 100.00 100.00 1.28e-136 PDB 1AC1 "Dsba Mutant H32l" 100.00 189 99.47 99.47 6.40e-135 PDB 1ACV "Dsba Mutant H32s" 100.00 189 99.47 99.47 2.39e-135 PDB 1BQ7 "Dsba Mutant P151a, Role Of The Cis-Proline In The Active Site Of Dsba" 100.00 189 99.47 99.47 1.31e-135 PDB 1DSB "Crystal Structure Of The Dsba Protein Required For Disulphide Bond Formation In Vivo" 100.00 189 100.00 100.00 1.28e-136 PDB 1FVJ "The 2.06 Angstrom Structure Of The H32y Mutant Of The Disulfide Bond Formation Protein (Dsba)" 100.00 189 99.47 100.00 1.42e-135 PDB 1FVK "The 1.7 Angstrom Structure Of Wild Type Disulfide Bond Formation Protein (Dsba)" 100.00 189 100.00 100.00 1.28e-136 PDB 1TI1 "Crystal Structure Of A Mutant Dsba" 100.00 189 99.47 99.47 1.94e-135 PDB 1U3A "Mutant Dsba" 100.00 189 99.47 99.47 1.94e-135 PDB 2B3S "Structure Of The Dsba Mutant (P31g-C33a)" 100.00 189 98.94 98.94 6.23e-134 PDB 2B6M "Structure Of The Dsba Mutant (P31a-C33a)" 100.00 189 98.94 98.94 2.74e-134 PDB 2HI7 "Crystal Structure Of Dsba-Dsbb-Ubiquinone Complex" 100.00 189 99.47 99.47 1.94e-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 99.47 1.94e-135 PDB 2ZUP "Updated Crystal Structure Of Dsbb-Dsba Complex From E. Coli" 100.00 189 99.47 99.47 1.94e-135 PDB 3DKS "Dsba Substrate Complex" 100.00 189 99.47 100.00 5.41e-136 PDB 3E9J "Structure Of The Charge-Transfer Intermediate Of The Transmembrane Redox Catalyst Dsbb" 100.00 189 99.47 99.47 1.94e-135 PDB 4TKY "The Complex Structure Of E. Coli Dsba Bound To A Peptide At The Dsba/dsbb Interface" 100.00 191 99.47 99.47 1.36e-135 PDB 4WET "Crystal Structure Of E.coli Dsba In Complex With Compound 16" 100.00 189 100.00 100.00 1.28e-136 PDB 4WEY "Crystal Structure Of E.coli Dsba In Complex With Compound 17" 100.00 189 100.00 100.00 1.28e-136 PDB 4WF4 "Crystal Structure Of E.coli Dsba Co-crystallised In Complex With Compound 4" 100.00 189 100.00 100.00 1.28e-136 PDB 4WF5 "Crystal Structure Of E.coli Dsba Soaked With Compound 4" 100.00 189 100.00 100.00 1.28e-136 DBJ BAB38206 "protein disulfide isomerase I [Escherichia coli O157:H7 str. Sakai]" 100.00 208 100.00 100.00 8.34e-137 DBJ BAE77448 "periplasmic protein disulfide isomerase I [Escherichia coli str. K12 substr. W3110]" 100.00 208 100.00 100.00 8.34e-137 DBJ BAG79665 "protein disulfide isomerase I [Escherichia coli SE11]" 100.00 208 100.00 100.00 8.34e-137 DBJ BAI27892 "periplasmic protein disulfide isomerase I [Escherichia coli O26:H11 str. 11368]" 100.00 208 100.00 100.00 8.34e-137 DBJ BAI33015 "periplasmic protein disulfide isomerase I [Escherichia coli O103:H2 str. 12009]" 100.00 208 100.00 100.00 8.34e-137 EMBL CAA44868 "PpfA protein [Escherichia coli K-12]" 100.00 208 100.00 100.00 8.34e-137 EMBL CAA56736 "dsbA [Escherichia coli K-12]" 100.00 208 100.00 100.00 8.34e-137 EMBL CAA90910 "DsbA protein [Escherichia coli]" 100.00 208 99.47 100.00 2.97e-136 EMBL CAP78318 "Thiol:disulfide interchange protein dsbA [Escherichia coli LF82]" 100.00 208 99.47 100.00 2.97e-136 EMBL CAQ34212 "protein disulfide oxidoreductase [Escherichia coli BL21(DE3)]" 100.00 208 100.00 100.00 8.34e-137 GB AAA23715 "putative [Escherichia coli]" 100.00 208 100.00 100.00 8.34e-137 GB AAB02995 "dsbA [Escherichia coli str. K-12 substr. MG1655]" 100.00 208 100.00 100.00 8.34e-137 GB AAC43519 "thiol:disulfide interchange protein DsbA mutant PH31/32PP [Escherichia coli]" 100.00 208 99.47 99.47 3.22e-135 GB AAC43520 "thiol:disulfide interchange protein DsbA mutant PH31/32TR [Escherichia coli]" 100.00 208 98.94 98.94 1.16e-134 GB AAC43521 "thiol:disulfide interchange protein DsbA mutant PH31/32LQ [Escherichia coli]" 100.00 208 98.94 98.94 2.99e-134 REF NP_312810 "protein disulfide isomerase I [Escherichia coli O157:H7 str. Sakai]" 100.00 208 100.00 100.00 8.34e-137 REF NP_418297 "periplasmic protein disulfide isomerase I [Escherichia coli str. K-12 substr. MG1655]" 100.00 208 100.00 100.00 8.34e-137 REF NP_709659 "periplasmic protein disulfide isomerase I [Shigella flexneri 2a str. 301]" 100.00 208 99.47 100.00 3.65e-136 REF WP_000725331 "thiol-disulfide isomerase [Shigella boydii]" 100.00 208 98.94 99.47 2.17e-135 REF WP_000725332 "thiol:disulfide interchange protein DsbA [Escherichia coli]" 100.00 208 99.47 100.00 1.24e-136 SP P0A4L5 "RecName: Full=Thiol:disulfide interchange protein DsbA; Flags: Precursor" 100.00 208 99.47 100.00 2.97e-136 SP P0A4L6 "RecName: Full=Thiol:disulfide interchange protein DsbA; Flags: Precursor" 100.00 208 99.47 100.00 2.97e-136 SP P0AEG4 "RecName: Full=Thiol:disulfide interchange protein DsbA; Flags: Precursor" 100.00 208 100.00 100.00 8.34e-137 SP P0AEG5 "RecName: Full=Thiol:disulfide interchange protein DsbA; Flags: Precursor" 100.00 208 100.00 100.00 8.34e-137 SP P52235 "RecName: Full=Thiol:disulfide interchange protein DsbA; Flags: Precursor" 100.00 208 99.47 100.00 3.65e-136 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 'E. coli' 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 'purified from the natural source' . Escherichia coli . . stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Saveframe_category sample _Sample_type solid _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $DsbA 15 mg '[U-13C; U-15N]' stop_ save_ save_sample_2 _Saveframe_category sample _Sample_type solid _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $DsbA 15 mg '[2-13C-glycerol; U-15N]' stop_ save_ save_sample_3 _Saveframe_category sample _Sample_type solid _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $DsbA 15 mg '[1,3-13C-glycerol; U-15N]' stop_ save_ ############################ # Computer software used # ############################ save_SPARKY _Saveframe_category software _Name SPARKY _Version . loop_ _Vendor _Address _Electronic_address Goddard . . stop_ loop_ _Task 'chemical shift assignment' 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_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model INOVA _Field_strength 750 _Details . save_ save_spectrometer_2 _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model 'Infinity Plus' _Field_strength 500 _Details . save_ ############################# # NMR applied experiments # ############################# save_2D_13C-13C_1 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 13C-13C' _Sample_label $sample_1 save_ save_2D_13C-13C_2 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 13C-13C' _Sample_label $sample_2 save_ save_2D_13C-13C_3 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 13C-13C' _Sample_label $sample_3 save_ save_2D_15N-(13CA)-13CX_4 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 15N-(13CA)-13CX' _Sample_label $sample_1 save_ save_2D_15N-(13CO)-13CX_5 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 15N-(13CO)-13CX' _Sample_label $sample_1 save_ save_3D_15N-13CA-13CX_6 _Saveframe_category NMR_applied_experiment _Experiment_name '3D 15N-13CA-13CX' _Sample_label $sample_1 save_ save_3D_15N-13CO-13CX_7 _Saveframe_category NMR_applied_experiment _Experiment_name '3D 15N-13CO-13CX' _Sample_label $sample_1 save_ save_3D_13CA-15N-(13CO)-13CX_8 _Saveframe_category NMR_applied_experiment _Experiment_name '3D 13CA-15N-(13CO)-13CX' _Sample_label $sample_1 save_ save_4D_13CA-15N-13CO-13CX_9 _Saveframe_category NMR_applied_experiment _Experiment_name '4D 13CA-15N-13CO-13CX' _Sample_label $sample_1 save_ save_2D_15N-13CX_(TEDOR)_10 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 15N-13CX (TEDOR)' _Sample_label $sample_2 save_ save_3D_15N-13CA-13CX_11 _Saveframe_category NMR_applied_experiment _Experiment_name '3D 15N-13CA-13CX' _Sample_label $sample_2 save_ save_3D_15N-13CO-13CX_12 _Saveframe_category NMR_applied_experiment _Experiment_name '3D 15N-13CO-13CX' _Sample_label $sample_3 save_ save_2D_13CA-13CO_(IPAP)_13 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 13CA-13CO (IPAP)' _Sample_label $sample_1 save_ save_2D_13C-13C_(COSY)_14 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 13C-13C (COSY)' _Sample_label $sample_1 save_ save_2D_15N-13CX_(TEDOR)_15 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 15N-13CX (TEDOR)' _Sample_label $sample_3 save_ ####################### # Sample conditions # ####################### save_sample_conditions_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 7.0 . pH pressure 1 . atm temperature 273 . K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_13C-adamantane _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 adamantane C 13 'alkane carbons' ppm 40.48 external direct . 'separate tube (no insert) similar to the experimental sample tube' 'magic angle' 1.0 adamantane N 15 'alkane carbons' ppm 40.48 external direct . 'separate tube (no insert) similar to the experimental sample tube' 'magic angle' 1.0 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_ _Software_label $SPARKY $NMRPipe stop_ loop_ _Experiment_label '2D 13C-13C' '2D 15N-(13CA)-13CX' '2D 15N-(13CO)-13CX' '3D 15N-13CA-13CX' '3D 15N-13CO-13CX' '3D 13CA-15N-(13CO)-13CX' '4D 13CA-15N-13CO-13CX' '2D 15N-13CX (TEDOR)' '2D 13CA-13CO (IPAP)' '2D 13C-13C (COSY)' stop_ loop_ _Sample_label $sample_1 $sample_2 $sample_3 stop_ _Sample_conditions_label $sample_conditions_1 _Chem_shift_reference_set_label $13C-adamantane _Mol_system_component_name DsbA _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 C C 176.30 0.00 . 2 1 1 ALA CA C 51.14 0.00 . 3 1 1 ALA CB C 19.58 0.04 . 4 1 1 ALA N N 39.50 0.00 . 5 2 2 GLN C C 179.91 0.13 . 6 2 2 GLN CA C 59.82 0.12 . 7 2 2 GLN CB C 29.94 0.12 . 8 2 2 GLN CD C 177.13 0.25 . 9 2 2 GLN CG C 31.47 0.26 . 10 2 2 GLN N N 121.57 0.04 . 11 3 3 TYR C C 175.68 0.12 . 12 3 3 TYR CA C 58.36 0.33 . 13 3 3 TYR CB C 40.88 0.01 . 14 3 3 TYR N N 122.01 0.20 . 15 4 4 GLU C C 174.46 0.16 . 16 4 4 GLU CA C 55.05 0.17 . 17 4 4 GLU CB C 33.78 0.23 . 18 4 4 GLU CG C 36.94 0.00 . 19 4 4 GLU N N 122.78 0.19 . 20 5 5 ASP C C 177.33 0.04 . 21 5 5 ASP CA C 55.27 0.15 . 22 5 5 ASP CB C 41.15 0.20 . 23 5 5 ASP CG C 179.82 0.10 . 24 5 5 ASP N N 125.90 0.20 . 25 6 6 GLY C C 173.43 0.12 . 26 6 6 GLY CA C 45.03 0.08 . 27 6 6 GLY N N 117.03 0.10 . 28 7 7 LYS C C 175.55 0.09 . 29 7 7 LYS CA C 57.14 0.21 . 30 7 7 LYS CB C 32.15 0.11 . 31 7 7 LYS CG C 25.39 0.00 . 32 7 7 LYS N N 122.19 0.26 . 33 8 8 GLN C C 174.20 0.14 . 34 8 8 GLN CA C 59.45 0.16 . 35 8 8 GLN CB C 27.21 0.09 . 36 8 8 GLN CD C 179.66 0.00 . 37 8 8 GLN CG C 34.25 0.11 . 38 8 8 GLN N N 115.42 0.23 . 39 9 9 TYR C C 172.25 0.12 . 40 9 9 TYR CA C 55.17 0.18 . 41 9 9 TYR CB C 41.29 0.02 . 42 9 9 TYR CD1 C 132.72 0.00 . 43 9 9 TYR CD2 C 132.40 0.00 . 44 9 9 TYR CE1 C 117.09 0.24 . 45 9 9 TYR CG C 128.34 0.06 . 46 9 9 TYR CZ C 158.05 0.05 . 47 9 9 TYR N N 111.81 0.15 . 48 10 10 THR C C 174.52 0.11 . 49 10 10 THR CA C 60.38 0.12 . 50 10 10 THR CB C 71.62 0.06 . 51 10 10 THR CG2 C 22.20 0.06 . 52 10 10 THR N N 111.79 0.13 . 53 11 11 THR C C 175.43 0.10 . 54 11 11 THR CA C 62.87 0.16 . 55 11 11 THR CB C 69.72 0.12 . 56 11 11 THR CG2 C 21.70 0.12 . 57 11 11 THR N N 120.97 0.15 . 58 12 12 LEU C C 177.51 0.12 . 59 12 12 LEU CA C 55.93 0.17 . 60 12 12 LEU CB C 41.64 0.13 . 61 12 12 LEU CD1 C 24.70 0.15 . 62 12 12 LEU CG C 28.71 0.12 . 63 12 12 LEU N N 129.27 0.13 . 64 13 13 GLU C C 176.79 0.12 . 65 13 13 GLU CA C 58.58 0.20 . 66 13 13 GLU CB C 29.93 0.08 . 67 13 13 GLU CG C 32.48 0.00 . 68 13 13 GLU N N 123.38 0.13 . 69 14 14 LYS C C 172.52 0.14 . 70 14 14 LYS CA C 52.36 0.12 . 71 14 14 LYS CB C 32.81 0.09 . 72 14 14 LYS CG C 24.52 0.08 . 73 14 14 LYS N N 117.78 0.15 . 74 15 15 PRO C C 176.49 0.09 . 75 15 15 PRO CA C 62.58 0.12 . 76 15 15 PRO CB C 32.73 0.10 . 77 15 15 PRO CD C 50.87 0.14 . 78 15 15 PRO CG C 27.27 0.07 . 79 15 15 PRO N N 135.71 0.15 . 80 16 16 VAL C C 176.10 0.08 . 81 16 16 VAL CA C 61.52 0.12 . 82 16 16 VAL CB C 32.79 0.08 . 83 16 16 VAL CG1 C 21.64 0.13 . 84 16 16 VAL CG2 C 21.61 0.09 . 85 16 16 VAL N N 123.52 0.18 . 86 17 17 ALA C C 179.03 0.09 . 87 17 17 ALA CA C 52.60 0.17 . 88 17 17 ALA CB C 18.85 0.05 . 89 17 17 ALA N N 132.39 0.16 . 90 18 18 GLY C C 174.12 0.15 . 91 18 18 GLY CA C 45.84 0.10 . 92 18 18 GLY N N 110.95 0.19 . 93 19 19 ALA C C 175.22 0.13 . 94 19 19 ALA CA C 50.53 0.15 . 95 19 19 ALA CB C 17.29 0.13 . 96 19 19 ALA N N 122.32 0.12 . 97 20 20 PRO C C 175.84 0.21 . 98 20 20 PRO CA C 62.55 0.15 . 99 20 20 PRO CB C 31.69 0.21 . 100 20 20 PRO CD C 50.25 0.18 . 101 20 20 PRO CG C 27.79 0.08 . 102 20 20 PRO N N 134.28 0.16 . 103 21 21 GLN C C 176.89 0.10 . 104 21 21 GLN CA C 60.14 0.18 . 105 21 21 GLN CB C 29.81 0.10 . 106 21 21 GLN CG C 32.32 0.09 . 107 21 21 GLN N N 121.73 0.29 . 108 22 22 VAL C C 172.99 0.13 . 109 22 22 VAL CA C 62.79 0.17 . 110 22 22 VAL CB C 33.97 0.10 . 111 22 22 VAL CG1 C 22.87 0.10 . 112 22 22 VAL CG2 C 21.37 0.14 . 113 22 22 VAL N N 116.08 0.15 . 114 23 23 LEU C C 173.43 0.15 . 115 23 23 LEU CA C 52.81 0.12 . 116 23 23 LEU CB C 46.12 0.10 . 117 23 23 LEU CG C 26.70 0.15 . 118 23 23 LEU N N 128.94 0.14 . 119 24 24 GLU CA C 53.83 0.15 . 120 24 24 GLU N N 127.93 0.31 . 121 25 25 PHE C C 175.70 0.00 . 122 25 25 PHE CA C 56.30 0.05 . 123 25 25 PHE CG C 139.84 0.03 . 124 25 25 PHE CZ C 129.95 0.00 . 125 25 25 PHE N N 121.22 0.00 . 126 26 26 PHE C C 170.73 0.15 . 127 26 26 PHE CA C 55.00 0.09 . 128 26 26 PHE CB C 43.73 0.38 . 129 26 26 PHE CD1 C 131.35 0.02 . 130 26 26 PHE CD2 C 131.35 0.02 . 131 26 26 PHE CE1 C 130.80 0.00 . 132 26 26 PHE CE2 C 130.80 0.00 . 133 26 26 PHE CG C 136.39 0.05 . 134 26 26 PHE CZ C 129.39 0.06 . 135 26 26 PHE N N 119.85 0.07 . 136 27 27 SER C C 177.36 0.09 . 137 27 27 SER CA C 54.82 0.12 . 138 27 27 SER CB C 64.57 0.14 . 139 27 27 SER N N 108.93 0.13 . 140 28 28 PHE C C 176.49 0.17 . 141 28 28 PHE CA C 63.05 0.21 . 142 28 28 PHE CB C 38.51 0.08 . 143 28 28 PHE CD1 C 132.22 0.00 . 144 28 28 PHE CD2 C 132.22 0.00 . 145 28 28 PHE CG C 139.34 0.14 . 146 28 28 PHE N N 131.75 0.15 . 147 29 29 PHE C C 175.66 0.21 . 148 29 29 PHE CA C 59.52 0.17 . 149 29 29 PHE CB C 39.76 0.00 . 150 29 29 PHE CD1 C 131.15 0.00 . 151 29 29 PHE CD2 C 131.15 0.00 . 152 29 29 PHE CG C 139.91 0.09 . 153 29 29 PHE N N 115.95 0.21 . 154 30 30 CYS C C 174.29 0.09 . 155 30 30 CYS CA C 52.71 0.15 . 156 30 30 CYS CB C 46.32 0.38 . 157 30 30 CYS N N 120.39 0.30 . 158 31 31 PRO CA C 66.31 0.05 . 159 31 31 PRO CB C 32.72 0.05 . 160 31 31 PRO CD C 52.48 0.12 . 161 31 31 PRO CG C 27.92 0.00 . 162 31 31 PRO N N 153.66 0.28 . 163 32 32 HIS C C 177.84 0.03 . 164 32 32 HIS CA C 58.81 0.00 . 165 32 32 HIS CB C 29.57 0.17 . 166 32 32 HIS N N 120.10 0.10 . 167 33 33 CYS C C 175.58 0.04 . 168 33 33 CYS CA C 63.28 0.24 . 169 33 33 CYS CB C 33.68 0.11 . 170 33 33 CYS N N 116.97 0.27 . 171 34 34 TYR C C 177.59 0.00 . 172 34 34 TYR CA C 58.67 0.04 . 173 34 34 TYR CD1 C 133.75 0.00 . 174 34 34 TYR CG C 127.65 0.00 . 175 34 34 TYR N N 123.71 0.12 . 176 35 35 GLN C C 179.01 0.00 . 177 35 35 GLN CA C 58.90 0.00 . 178 35 35 GLN N N 118.10 0.00 . 179 36 36 PHE C C 176.45 0.51 . 180 36 36 PHE CA C 60.16 0.24 . 181 36 36 PHE CB C 38.59 0.00 . 182 36 36 PHE N N 121.17 0.22 . 183 37 37 GLU C C 177.81 0.07 . 184 37 37 GLU CA C 58.55 0.17 . 185 37 37 GLU CB C 30.92 0.00 . 186 37 37 GLU CG C 34.75 0.05 . 187 37 37 GLU N N 116.08 0.06 . 188 38 38 GLU C C 176.72 0.00 . 189 38 38 GLU CA C 58.79 0.07 . 190 38 38 GLU CB C 30.82 0.00 . 191 38 38 GLU CG C 34.93 0.00 . 192 38 38 GLU N N 112.80 0.11 . 193 39 39 VAL C C 176.85 0.08 . 194 39 39 VAL CA C 63.96 0.28 . 195 39 39 VAL CB C 32.68 0.04 . 196 39 39 VAL CG1 C 22.70 0.00 . 197 39 39 VAL CG2 C 20.93 0.11 . 198 39 39 VAL N N 116.56 0.16 . 199 40 40 LEU C C 176.29 0.00 . 200 40 40 LEU CA C 55.24 0.10 . 201 40 40 LEU CB C 42.05 0.06 . 202 40 40 LEU CD1 C 26.02 0.10 . 203 40 40 LEU CD2 C 26.02 0.10 . 204 40 40 LEU CG C 27.19 0.11 . 205 40 40 LEU N N 115.01 0.21 . 206 41 41 HIS C C 176.71 0.07 . 207 41 41 HIS CA C 55.78 0.09 . 208 41 41 HIS CB C 25.58 0.00 . 209 41 41 HIS CG C 131.22 0.09 . 210 41 41 HIS N N 112.04 0.26 . 211 42 42 ILE CA C 65.13 0.09 . 212 42 42 ILE CB C 35.67 0.08 . 213 42 42 ILE CD1 C 9.90 0.01 . 214 42 42 ILE CG1 C 27.12 0.02 . 215 42 42 ILE CG2 C 16.80 0.02 . 216 42 42 ILE N N 120.46 0.00 . 217 43 43 SER C C 176.46 0.01 . 218 43 43 SER CA C 57.54 0.02 . 219 43 43 SER CB C 61.41 0.04 . 220 44 44 ASP C C 177.94 0.00 . 221 44 44 ASP CA C 57.49 0.01 . 222 44 44 ASP CB C 40.31 0.00 . 223 44 44 ASP N N 120.79 0.11 . 224 45 45 ASN C C 178.35 0.02 . 225 45 45 ASN CA C 56.93 0.00 . 226 45 45 ASN CB C 40.08 0.02 . 227 46 46 VAL C C 178.09 0.12 . 228 46 46 VAL CA C 66.78 0.07 . 229 46 46 VAL CB C 31.94 0.16 . 230 46 46 VAL CG1 C 24.29 0.19 . 231 46 46 VAL CG2 C 22.49 0.00 . 232 46 46 VAL N N 120.29 0.06 . 233 47 47 LYS C C 179.25 0.09 . 234 47 47 LYS CA C 60.22 0.14 . 235 47 47 LYS CB C 32.61 0.10 . 236 47 47 LYS CG C 25.33 0.19 . 237 47 47 LYS N N 119.81 0.29 . 238 48 48 LYS C C 177.60 0.09 . 239 48 48 LYS CA C 58.63 0.23 . 240 48 48 LYS CB C 33.05 0.04 . 241 48 48 LYS N N 115.09 0.19 . 242 49 49 LYS CA C 55.74 0.08 . 243 49 49 LYS N N 116.81 0.21 . 244 50 50 LEU C C 174.40 0.00 . 245 50 50 LEU CA C 53.03 0.26 . 246 50 50 LEU CB C 41.37 0.04 . 247 50 50 LEU CG C 25.85 0.06 . 248 50 50 LEU N N 120.56 0.03 . 249 53 53 GLY C C 174.13 0.29 . 250 53 53 GLY CA C 45.55 0.25 . 251 53 53 GLY N N 110.92 0.08 . 252 54 54 VAL C C 174.41 0.00 . 253 54 54 VAL CA C 62.55 0.13 . 254 54 54 VAL CB C 31.84 0.06 . 255 54 54 VAL CG1 C 22.27 0.00 . 256 54 54 VAL CG2 C 21.72 0.00 . 257 54 54 VAL N N 121.69 0.04 . 258 56 56 MET C C 175.49 0.14 . 259 56 56 MET CA C 55.01 0.00 . 260 56 56 MET CB C 34.36 0.00 . 261 57 57 THR C C 171.90 0.11 . 262 57 57 THR CA C 62.90 0.16 . 263 57 57 THR CB C 70.31 0.14 . 264 57 57 THR CG2 C 22.60 0.07 . 265 57 57 THR N N 123.01 0.12 . 266 58 58 LYS CA C 55.06 0.00 . 267 59 59 TYR C C 173.17 0.13 . 268 59 59 TYR CA C 52.08 0.13 . 269 59 59 TYR CB C 40.96 0.03 . 270 59 59 TYR CD1 C 130.84 0.00 . 271 59 59 TYR CD2 C 131.73 0.01 . 272 59 59 TYR CG C 129.88 0.03 . 273 59 59 TYR N N 124.54 0.00 . 274 60 60 HIS C C 174.88 0.13 . 275 60 60 HIS CA C 56.20 0.14 . 276 60 60 HIS CB C 30.65 0.25 . 277 60 60 HIS CE1 C 139.01 0.07 . 278 60 60 HIS CG C 128.14 0.16 . 279 60 60 HIS N N 123.50 0.16 . 280 61 61 VAL C C 175.59 0.26 . 281 61 61 VAL CA C 57.86 0.12 . 282 61 61 VAL CB C 34.33 0.17 . 283 61 61 VAL CG1 C 21.71 0.10 . 284 61 61 VAL CG2 C 17.42 0.11 . 285 61 61 VAL N N 111.47 0.20 . 286 63 63 PHE CA C 58.02 0.03 . 287 63 63 PHE N N 111.08 0.00 . 288 64 64 MET C C 177.46 0.00 . 289 64 64 MET CA C 54.35 0.00 . 290 65 65 GLY C C 175.50 0.00 . 291 65 65 GLY CA C 47.46 0.06 . 292 65 65 GLY N N 111.30 0.00 . 293 66 66 GLY C C 176.93 0.10 . 294 66 66 GLY CA C 45.58 0.06 . 295 66 66 GLY N N 109.22 0.00 . 296 67 67 ASP C C 177.91 0.25 . 297 67 67 ASP CA C 57.67 0.14 . 298 67 67 ASP CB C 39.86 0.05 . 299 67 67 ASP CG C 176.74 0.00 . 300 67 67 ASP N N 128.19 0.08 . 301 68 68 LEU C C 179.24 0.12 . 302 68 68 LEU CA C 57.00 0.21 . 303 68 68 LEU CB C 42.19 0.18 . 304 68 68 LEU CG C 27.27 0.07 . 305 68 68 LEU N N 120.45 0.12 . 306 69 69 GLY C C 176.41 0.19 . 307 69 69 GLY CA C 48.25 0.12 . 308 69 69 GLY N N 107.15 0.13 . 309 70 70 LYS CA C 59.83 0.07 . 310 70 70 LYS CB C 31.84 0.00 . 311 70 70 LYS N N 121.49 0.34 . 312 72 72 LEU C C 178.05 0.00 . 313 72 72 LEU CA C 57.67 0.17 . 314 72 72 LEU CB C 42.68 0.04 . 315 72 72 LEU CG C 28.31 0.01 . 316 73 73 THR C C 176.63 0.12 . 317 73 73 THR CA C 66.96 0.21 . 318 73 73 THR CB C 68.59 0.13 . 319 73 73 THR CG2 C 22.11 0.15 . 320 73 73 THR N N 119.73 0.18 . 321 74 74 GLN C C 177.54 0.10 . 322 74 74 GLN CA C 59.58 0.15 . 323 74 74 GLN CB C 25.99 0.09 . 324 74 74 GLN CD C 177.45 0.02 . 325 74 74 GLN CG C 31.03 0.16 . 326 74 74 GLN N N 125.36 0.15 . 327 74 74 GLN NE2 N 108.38 0.07 . 328 75 75 ALA C C 179.81 0.08 . 329 75 75 ALA CA C 54.91 0.13 . 330 75 75 ALA CB C 20.12 0.10 . 331 75 75 ALA N N 123.41 0.14 . 332 76 76 TRP C C 177.76 0.14 . 333 76 76 TRP CA C 59.12 0.08 . 334 76 76 TRP CB C 29.71 0.06 . 335 76 76 TRP CD1 C 127.99 0.13 . 336 76 76 TRP CD2 C 129.38 0.03 . 337 76 76 TRP CE2 C 139.98 0.12 . 338 76 76 TRP CE3 C 121.71 0.04 . 339 76 76 TRP CG C 111.25 0.04 . 340 76 76 TRP N N 120.62 0.13 . 341 76 76 TRP NE1 N 128.84 0.09 . 342 77 77 ALA C C 179.01 0.17 . 343 77 77 ALA CA C 55.29 0.14 . 344 77 77 ALA CB C 20.28 0.04 . 345 77 77 ALA N N 120.17 0.23 . 346 78 78 VAL C C 177.27 0.13 . 347 78 78 VAL CA C 67.30 0.18 . 348 78 78 VAL CB C 30.31 0.04 . 349 78 78 VAL CG1 C 23.66 0.07 . 350 78 78 VAL CG2 C 22.35 0.05 . 351 78 78 VAL N N 119.79 0.16 . 352 79 79 ALA C C 179.84 0.08 . 353 79 79 ALA CA C 55.09 0.13 . 354 79 79 ALA CB C 17.77 0.09 . 355 79 79 ALA N N 121.08 0.21 . 356 80 80 MET C C 179.41 0.14 . 357 80 80 MET CA C 58.61 0.14 . 358 80 80 MET CB C 34.53 0.06 . 359 80 80 MET CG C 30.95 0.25 . 360 80 80 MET N N 115.95 0.20 . 361 81 81 ALA C C 180.15 0.04 . 362 81 81 ALA CA C 54.80 0.13 . 363 81 81 ALA CB C 18.12 0.14 . 364 81 81 ALA N N 123.80 0.21 . 365 82 82 LEU C C 177.50 0.11 . 366 82 82 LEU CA C 54.63 0.13 . 367 82 82 LEU CB C 43.19 0.17 . 368 82 82 LEU CD1 C 21.96 0.05 . 369 82 82 LEU CD2 C 21.96 0.05 . 370 82 82 LEU CG C 26.97 0.08 . 371 82 82 LEU N N 113.52 0.20 . 372 83 83 GLY C C 176.89 0.09 . 373 83 83 GLY CA C 47.39 0.20 . 374 83 83 GLY N N 111.39 0.15 . 375 84 84 VAL C C 176.82 0.07 . 376 84 84 VAL CA C 59.42 0.12 . 377 84 84 VAL CB C 31.65 0.09 . 378 84 84 VAL CG1 C 20.46 0.07 . 379 84 84 VAL CG2 C 19.22 0.09 . 380 84 84 VAL N N 108.82 0.15 . 381 85 85 GLU C C 179.65 0.12 . 382 85 85 GLU CA C 61.96 0.12 . 383 85 85 GLU CB C 29.43 0.10 . 384 85 85 GLU CD C 184.07 0.00 . 385 85 85 GLU CG C 36.47 0.05 . 386 85 85 GLU N N 126.74 0.19 . 387 86 86 ASP C C 177.32 0.12 . 388 86 86 ASP CA C 55.95 0.18 . 389 86 86 ASP CB C 39.83 0.10 . 390 86 86 ASP CG C 179.93 0.21 . 391 86 86 ASP N N 116.35 0.14 . 392 87 87 LYS C C 178.02 0.07 . 393 87 87 LYS CA C 57.30 0.17 . 394 87 87 LYS CB C 34.27 0.13 . 395 87 87 LYS CD C 29.44 0.09 . 396 87 87 LYS CE C 39.81 0.04 . 397 87 87 LYS CG C 25.32 0.10 . 398 87 87 LYS N N 117.20 0.15 . 399 88 88 VAL C C 176.12 0.07 . 400 88 88 VAL CA C 60.93 0.17 . 401 88 88 VAL CB C 32.93 0.14 . 402 88 88 VAL CG1 C 19.48 0.14 . 403 88 88 VAL CG2 C 17.61 0.08 . 404 88 88 VAL N N 104.04 0.14 . 405 89 89 THR C C 175.17 0.11 . 406 89 89 THR CA C 69.28 0.22 . 407 89 89 THR CB C 69.76 0.15 . 408 89 89 THR CG2 C 21.27 0.12 . 409 89 89 THR N N 120.85 0.21 . 410 90 90 VAL C C 175.97 0.12 . 411 90 90 VAL CA C 69.41 0.20 . 412 90 90 VAL CB C 28.88 0.21 . 413 90 90 VAL CG1 C 24.36 0.02 . 414 90 90 VAL CG2 C 21.46 0.14 . 415 90 90 VAL N N 120.28 0.10 . 416 91 91 PRO C C 181.10 0.15 . 417 91 91 PRO CA C 65.92 0.17 . 418 91 91 PRO CB C 31.63 0.25 . 419 91 91 PRO CD C 49.09 0.10 . 420 91 91 PRO CG C 27.82 0.17 . 421 91 91 PRO N N 133.86 0.20 . 422 92 92 LEU C C 177.88 0.18 . 423 92 92 LEU CA C 58.08 0.11 . 424 92 92 LEU CB C 40.10 0.07 . 425 92 92 LEU CD1 C 22.93 0.07 . 426 92 92 LEU CD2 C 22.93 0.07 . 427 92 92 LEU CG C 27.00 0.04 . 428 92 92 LEU N N 120.18 0.15 . 429 93 93 PHE C C 180.06 0.17 . 430 93 93 PHE CA C 63.99 0.16 . 431 93 93 PHE CB C 39.52 0.18 . 432 93 93 PHE CD1 C 132.13 0.01 . 433 93 93 PHE CD2 C 132.13 0.01 . 434 93 93 PHE CG C 141.57 0.11 . 435 93 93 PHE N N 120.05 0.23 . 436 94 94 GLU C C 180.40 0.12 . 437 94 94 GLU CA C 59.42 0.31 . 438 94 94 GLU CB C 29.63 0.06 . 439 94 94 GLU CG C 40.00 0.00 . 440 94 94 GLU N N 116.17 0.11 . 441 95 95 GLY C C 175.82 0.17 . 442 95 95 GLY CA C 46.68 0.17 . 443 95 95 GLY N N 108.30 0.07 . 444 96 96 VAL C C 178.19 0.05 . 445 96 96 VAL CA C 66.46 0.23 . 446 96 96 VAL CB C 32.19 0.07 . 447 96 96 VAL CG1 C 23.61 0.06 . 448 96 96 VAL CG2 C 21.84 0.13 . 449 96 96 VAL N N 119.71 0.26 . 450 98 98 LYS C C 177.28 0.05 . 451 98 98 LYS CA C 57.81 0.00 . 452 98 98 LYS CB C 34.43 0.19 . 453 99 99 THR C C 175.60 0.07 . 454 99 99 THR CA C 62.21 0.14 . 455 99 99 THR CB C 68.62 0.21 . 456 99 99 THR CG2 C 22.23 0.09 . 457 99 99 THR N N 107.44 0.20 . 458 100 100 GLN C C 175.36 0.16 . 459 100 100 GLN CA C 57.33 0.21 . 460 100 100 GLN CB C 25.56 0.18 . 461 100 100 GLN CG C 34.39 0.09 . 462 100 100 GLN N N 114.75 0.20 . 463 101 101 THR C C 175.33 0.10 . 464 101 101 THR CA C 60.88 0.14 . 465 101 101 THR CB C 68.78 0.17 . 466 101 101 THR CG2 C 22.89 0.07 . 467 101 101 THR N N 106.06 0.27 . 468 102 102 ILE C C 174.01 0.18 . 469 102 102 ILE CA C 60.84 0.14 . 470 102 102 ILE CB C 37.01 0.11 . 471 102 102 ILE CD1 C 14.81 0.12 . 472 102 102 ILE CG1 C 27.19 0.04 . 473 102 102 ILE CG2 C 17.46 0.06 . 474 102 102 ILE N N 121.05 0.14 . 475 103 103 ARG C C 175.36 0.19 . 476 103 103 ARG CA C 55.28 0.17 . 477 103 103 ARG CB C 32.71 0.00 . 478 103 103 ARG CD C 40.93 0.00 . 479 103 103 ARG CG C 27.18 0.00 . 480 103 103 ARG N N 126.00 0.14 . 481 104 104 SER C C 174.53 0.10 . 482 104 104 SER CA C 56.80 0.22 . 483 104 104 SER CB C 67.28 0.12 . 484 104 104 SER N N 115.11 0.27 . 485 105 105 ALA C C 180.84 0.08 . 486 105 105 ALA CA C 55.30 0.14 . 487 105 105 ALA CB C 16.94 0.06 . 488 105 105 ALA N N 123.73 0.11 . 489 106 106 SER C C 176.34 0.07 . 490 106 106 SER CA C 61.55 0.14 . 491 106 106 SER CB C 62.26 0.08 . 492 106 106 SER N N 116.14 0.14 . 493 107 107 ASP C C 179.12 0.19 . 494 107 107 ASP CA C 57.01 0.12 . 495 107 107 ASP CB C 42.51 0.26 . 496 107 107 ASP N N 120.34 0.16 . 497 108 108 ILE C C 176.99 0.19 . 498 108 108 ILE CA C 65.77 0.15 . 499 108 108 ILE CB C 38.28 0.08 . 500 108 108 ILE CD1 C 15.30 0.06 . 501 108 108 ILE CG1 C 28.97 0.13 . 502 108 108 ILE CG2 C 18.42 0.06 . 503 108 108 ILE N N 120.13 0.10 . 504 109 109 ARG C C 177.64 0.15 . 505 109 109 ARG CA C 59.19 0.27 . 506 109 109 ARG CB C 29.97 0.18 . 507 109 109 ARG CD C 43.27 0.06 . 508 109 109 ARG CZ C 159.73 0.03 . 509 109 109 ARG N N 121.05 0.19 . 510 110 110 ASP C C 179.32 0.32 . 511 110 110 ASP CA C 57.59 0.21 . 512 110 110 ASP CB C 40.17 0.09 . 513 110 110 ASP CG C 180.00 0.00 . 514 110 110 ASP N N 116.51 0.15 . 515 111 111 VAL C C 179.27 0.11 . 516 111 111 VAL CA C 66.43 0.13 . 517 111 111 VAL CB C 30.89 0.10 . 518 111 111 VAL CG1 C 23.60 0.07 . 519 111 111 VAL CG2 C 21.71 0.06 . 520 111 111 VAL N N 120.27 0.17 . 521 112 112 PHE C C 177.81 0.09 . 522 112 112 PHE CA C 62.05 0.16 . 523 112 112 PHE CB C 38.10 0.18 . 524 112 112 PHE CG C 142.33 0.04 . 525 112 112 PHE N N 120.54 0.13 . 526 113 113 ILE C C 182.26 0.13 . 527 113 113 ILE CA C 63.66 0.14 . 528 113 113 ILE CB C 37.94 0.06 . 529 113 113 ILE CD1 C 13.74 0.19 . 530 113 113 ILE CG1 C 28.30 0.09 . 531 113 113 ILE CG2 C 17.12 0.09 . 532 113 113 ILE N N 122.05 0.14 . 533 114 114 ASN C C 176.24 0.14 . 534 114 114 ASN CA C 55.61 0.18 . 535 114 114 ASN CB C 38.17 0.16 . 536 114 114 ASN CG C 176.66 0.10 . 537 114 114 ASN N N 120.41 0.12 . 538 115 115 ALA C C 177.04 0.08 . 539 115 115 ALA CA C 51.92 0.18 . 540 115 115 ALA CB C 18.90 0.06 . 541 115 115 ALA N N 120.93 0.17 . 542 116 116 GLY C C 173.90 0.11 . 543 116 116 GLY CA C 45.26 0.16 . 544 116 116 GLY N N 105.75 0.21 . 545 117 117 ILE C C 175.25 0.18 . 546 117 117 ILE CA C 61.03 0.17 . 547 117 117 ILE CB C 37.63 0.09 . 548 117 117 ILE CD1 C 14.67 0.09 . 549 117 117 ILE CG1 C 25.83 0.00 . 550 117 117 ILE CG2 C 20.60 0.09 . 551 117 117 ILE N N 125.36 0.16 . 552 118 118 LYS C C 179.24 0.10 . 553 118 118 LYS CA C 56.86 0.17 . 554 118 118 LYS CB C 32.64 0.10 . 555 118 118 LYS CG C 25.60 0.09 . 556 118 118 LYS N N 125.85 0.19 . 557 119 119 GLY C C 175.09 0.13 . 558 119 119 GLY CA C 48.32 0.16 . 559 119 119 GLY N N 113.61 0.28 . 560 120 120 GLU C C 180.12 0.07 . 561 120 120 GLU CA C 59.54 0.09 . 562 120 120 GLU CB C 28.63 0.00 . 563 120 120 GLU N N 117.26 0.26 . 564 121 121 GLU C C 179.38 0.22 . 565 121 121 GLU CA C 58.30 0.03 . 566 121 121 GLU CB C 29.67 0.09 . 567 121 121 GLU N N 120.94 0.07 . 568 122 122 TYR C C 177.01 0.00 . 569 122 122 TYR CA C 62.87 0.20 . 570 122 122 TYR CB C 38.02 0.08 . 571 122 122 TYR CE2 C 115.79 0.00 . 572 122 122 TYR CE1 C 117.64 0.02 . 573 122 122 TYR CG C 127.05 0.01 . 574 122 122 TYR N N 122.68 0.33 . 575 123 123 ASP C C 178.70 0.19 . 576 123 123 ASP CA C 57.40 0.14 . 577 123 123 ASP CB C 39.79 0.12 . 578 123 123 ASP CG C 180.06 0.00 . 579 123 123 ASP N N 119.04 0.19 . 580 124 124 ALA CA C 54.64 0.19 . 581 124 124 ALA CB C 18.14 0.08 . 582 124 124 ALA N N 121.03 0.10 . 583 125 125 ALA C C 181.09 0.17 . 584 125 125 ALA CA C 55.06 0.24 . 585 125 125 ALA CB C 18.47 0.07 . 586 125 125 ALA N N 119.62 0.01 . 587 126 126 TRP C C 176.01 0.11 . 588 126 126 TRP CA C 61.52 0.12 . 589 126 126 TRP CB C 29.12 0.35 . 590 126 126 TRP CD1 C 127.66 0.17 . 591 126 126 TRP CD2 C 128.62 0.08 . 592 126 126 TRP CE2 C 138.76 0.14 . 593 126 126 TRP CE3 C 122.73 0.06 . 594 126 126 TRP CG C 109.51 0.07 . 595 126 126 TRP N N 121.89 0.20 . 596 126 126 TRP NE1 N 130.95 0.08 . 597 127 127 ASN C C 174.72 0.22 . 598 127 127 ASN CA C 53.44 0.17 . 599 127 127 ASN CB C 40.31 0.13 . 600 127 127 ASN CG C 177.46 0.09 . 601 127 127 ASN N N 110.72 0.16 . 602 128 128 SER C C 175.51 0.00 . 603 128 128 SER CA C 59.33 0.23 . 604 128 128 SER CB C 65.68 0.05 . 605 128 128 SER N N 116.52 0.30 . 606 129 129 PHE C C 178.81 0.25 . 607 129 129 PHE CA C 61.70 0.06 . 608 129 129 PHE CB C 38.13 0.00 . 609 129 129 PHE CG C 137.40 0.02 . 610 129 129 PHE N N 123.91 0.00 . 611 130 130 VAL C C 177.18 0.04 . 612 130 130 VAL CA C 67.13 0.09 . 613 130 130 VAL CB C 31.55 0.00 . 614 130 130 VAL N N 119.92 0.28 . 615 131 131 VAL C C 177.46 0.01 . 616 131 131 VAL CA C 67.20 0.17 . 617 131 131 VAL CB C 31.53 0.04 . 618 131 131 VAL CG1 C 23.80 0.04 . 619 131 131 VAL CG2 C 22.39 0.02 . 620 131 131 VAL N N 121.15 0.08 . 621 132 132 LYS C C 180.34 0.07 . 622 132 132 LYS CA C 59.89 0.19 . 623 132 132 LYS CB C 31.95 0.03 . 624 132 132 LYS N N 120.32 0.06 . 625 133 133 SER C C 176.69 0.25 . 626 133 133 SER CA C 61.21 0.18 . 627 133 133 SER CB C 62.14 0.11 . 628 133 133 SER N N 115.23 0.33 . 629 134 134 LEU C C 181.36 0.11 . 630 134 134 LEU CA C 57.64 0.12 . 631 134 134 LEU CB C 44.21 0.17 . 632 134 134 LEU CD1 C 22.73 0.00 . 633 134 134 LEU CD2 C 22.73 0.00 . 634 134 134 LEU CG C 27.41 0.08 . 635 134 134 LEU N N 124.00 0.16 . 636 135 135 VAL C C 177.13 0.10 . 637 135 135 VAL CA C 69.06 0.12 . 638 135 135 VAL CB C 31.46 0.27 . 639 135 135 VAL CG1 C 23.77 0.10 . 640 135 135 VAL CG2 C 21.12 0.13 . 641 135 135 VAL N N 123.27 0.16 . 642 136 136 ALA C C 180.91 0.07 . 643 136 136 ALA CA C 55.09 0.22 . 644 136 136 ALA CB C 17.83 0.20 . 645 136 136 ALA N N 121.22 0.10 . 646 137 137 GLN C C 179.31 0.04 . 647 137 137 GLN CA C 59.30 0.12 . 648 137 137 GLN CB C 29.65 0.13 . 649 137 137 GLN CG C 33.81 0.00 . 650 137 137 GLN N N 118.70 0.12 . 651 138 138 GLN CA C 59.86 0.08 . 652 138 138 GLN N N 119.35 0.08 . 653 139 139 GLU CA C 59.83 0.14 . 654 139 139 GLU N N 121.28 0.00 . 655 140 140 LYS C C 177.73 0.01 . 656 140 140 LYS CA C 58.96 0.06 . 657 140 140 LYS CB C 32.68 0.00 . 658 140 140 LYS CG C 24.79 0.11 . 659 140 140 LYS N N 122.25 0.08 . 660 141 141 ALA C C 179.56 0.07 . 661 141 141 ALA CA C 55.01 0.14 . 662 141 141 ALA CB C 18.43 0.11 . 663 141 141 ALA N N 119.73 0.04 . 664 142 142 ALA C C 178.95 0.23 . 665 142 142 ALA CA C 54.43 0.12 . 666 142 142 ALA CB C 18.04 0.20 . 667 142 142 ALA N N 117.20 0.11 . 668 143 143 ALA C C 182.47 0.05 . 669 143 143 ALA CA C 54.55 0.11 . 670 143 143 ALA CB C 18.06 0.03 . 671 143 143 ALA N N 121.02 0.07 . 672 144 144 ASP C C 178.29 0.14 . 673 144 144 ASP CA C 57.38 0.13 . 674 144 144 ASP CB C 40.27 0.20 . 675 144 144 ASP CG C 180.04 0.03 . 676 144 144 ASP N N 120.87 0.11 . 677 145 145 VAL C C 174.01 0.17 . 678 145 145 VAL CA C 60.30 0.15 . 679 145 145 VAL CB C 30.89 0.09 . 680 145 145 VAL CG1 C 20.28 0.17 . 681 145 145 VAL CG2 C 19.09 0.05 . 682 145 145 VAL N N 108.52 0.21 . 683 146 146 GLN C C 175.46 0.10 . 684 146 146 GLN CA C 55.95 0.12 . 685 146 146 GLN CB C 26.17 0.08 . 686 146 146 GLN N N 118.23 0.19 . 687 147 147 LEU CA C 56.35 0.18 . 688 147 147 LEU CB C 43.07 0.08 . 689 147 147 LEU CG C 26.90 0.03 . 690 147 147 LEU N N 117.96 0.21 . 691 148 148 ARG C C 175.84 0.14 . 692 148 148 ARG CA C 55.04 0.10 . 693 148 148 ARG CB C 31.98 0.15 . 694 148 148 ARG CG C 26.98 0.26 . 695 148 148 ARG N N 123.37 0.09 . 696 149 149 GLY C C 171.08 0.21 . 697 149 149 GLY CA C 45.37 0.12 . 698 149 149 GLY N N 106.00 0.20 . 699 150 150 VAL C C 173.04 0.11 . 700 150 150 VAL CA C 57.95 0.12 . 701 150 150 VAL CB C 34.94 0.10 . 702 150 150 VAL CG1 C 25.88 0.11 . 703 150 150 VAL CG2 C 19.03 0.07 . 704 150 150 VAL N N 110.55 0.32 . 705 151 151 PRO C C 175.92 0.10 . 706 151 151 PRO CA C 62.45 0.15 . 707 151 151 PRO CB C 35.79 0.21 . 708 151 151 PRO CD C 51.56 0.12 . 709 151 151 PRO N N 133.84 0.20 . 710 152 152 ALA C C 174.79 0.13 . 711 152 152 ALA CA C 51.90 0.18 . 712 152 152 ALA CB C 25.57 0.06 . 713 152 152 ALA N N 122.80 0.18 . 714 153 153 MET C C 173.26 0.11 . 715 153 153 MET CA C 55.05 0.11 . 716 153 153 MET CB C 36.93 0.11 . 717 153 153 MET CG C 32.20 0.18 . 718 153 153 MET N N 121.33 0.13 . 719 154 154 PHE C C 176.36 0.15 . 720 154 154 PHE CA C 55.96 0.17 . 721 154 154 PHE CB C 43.91 0.00 . 722 154 154 PHE CD1 C 131.58 0.24 . 723 154 154 PHE CD2 C 130.15 0.02 . 724 154 154 PHE CG C 139.72 0.07 . 725 154 154 PHE N N 124.56 0.15 . 726 155 155 VAL C C 176.01 0.07 . 727 155 155 VAL CA C 60.84 0.16 . 728 155 155 VAL CB C 34.91 0.12 . 729 155 155 VAL CG1 C 22.80 0.10 . 730 155 155 VAL CG2 C 20.44 0.07 . 731 155 155 VAL N N 123.00 0.13 . 732 156 156 ASN C C 174.21 0.17 . 733 156 156 ASN CA C 54.70 0.13 . 734 156 156 ASN CB C 37.50 0.10 . 735 156 156 ASN CG C 177.27 0.02 . 736 156 156 ASN N N 127.12 0.10 . 737 157 157 GLY C C 172.66 0.11 . 738 157 157 GLY CA C 46.53 0.19 . 739 157 157 GLY N N 105.70 0.13 . 740 158 158 LYS C C 174.98 0.15 . 741 158 158 LYS CA C 57.24 0.16 . 742 158 158 LYS CB C 37.59 0.07 . 743 158 158 LYS N N 114.75 0.14 . 744 159 159 TYR C C 174.74 0.24 . 745 159 159 TYR CA C 55.45 0.09 . 746 159 159 TYR CB C 42.81 0.12 . 747 159 159 TYR CE1 C 118.05 0.03 . 748 159 159 TYR CG C 128.78 0.05 . 749 159 159 TYR N N 117.65 0.11 . 750 160 160 GLN C C 175.74 0.00 . 751 160 160 GLN CA C 53.42 0.07 . 752 160 160 GLN CB C 30.72 0.06 . 753 160 160 GLN CD C 179.25 0.04 . 754 160 160 GLN CG C 32.47 0.00 . 755 160 160 GLN NE2 N 108.80 0.06 . 756 161 161 LEU C C 177.70 0.02 . 757 161 161 LEU CB C 40.54 0.05 . 758 161 161 LEU CG C 28.26 0.06 . 759 162 162 ASN C C 172.31 0.14 . 760 162 162 ASN CA C 49.85 0.17 . 761 162 162 ASN CB C 38.56 0.12 . 762 162 162 ASN CG C 177.49 0.14 . 763 163 163 PRO C C 177.40 0.17 . 764 163 163 PRO CA C 64.79 0.20 . 765 163 163 PRO CB C 32.46 0.22 . 766 163 163 PRO CD C 50.79 0.09 . 767 163 163 PRO CG C 27.85 0.20 . 768 163 163 PRO N N 137.15 0.41 . 769 164 164 GLN C C 177.24 0.19 . 770 164 164 GLN CA C 58.10 0.18 . 771 164 164 GLN CB C 28.02 0.04 . 772 164 164 GLN CD C 173.86 0.00 . 773 164 164 GLN N N 114.89 0.27 . 774 165 165 GLY C C 173.66 0.26 . 775 165 165 GLY CA C 44.70 0.21 . 776 165 165 GLY N N 107.20 0.22 . 777 166 166 MET C C 174.11 0.35 . 778 166 166 MET CA C 54.54 0.21 . 779 166 166 MET CB C 34.51 0.18 . 780 166 166 MET N N 119.54 0.35 . 781 167 167 ASP CA C 54.39 0.18 . 782 167 167 ASP CB C 40.48 0.04 . 783 167 167 ASP CG C 178.72 0.09 . 784 167 167 ASP N N 121.08 0.31 . 785 168 168 THR C C 175.47 0.00 . 786 168 168 THR CA C 60.57 0.15 . 787 168 168 THR CB C 68.83 0.08 . 788 168 168 THR CG2 C 22.47 0.06 . 789 168 168 THR N N 112.41 0.17 . 790 169 169 SER C C 174.43 0.07 . 791 169 169 SER CA C 61.08 0.07 . 792 169 169 SER CB C 63.32 0.18 . 793 170 170 ASN CA C 52.13 0.01 . 794 171 171 MET C C 177.70 0.01 . 795 171 171 MET CB C 32.83 0.01 . 796 173 173 VAL CA C 65.75 0.05 . 797 173 173 VAL CB C 32.19 0.03 . 798 173 173 VAL N N 121.57 0.04 . 799 174 174 PHE C C 176.24 0.00 . 800 174 174 PHE CA C 61.82 0.15 . 801 174 174 PHE CG C 138.90 0.06 . 802 174 174 PHE N N 121.58 0.00 . 803 175 175 VAL C C 177.62 0.14 . 804 175 175 VAL CA C 66.96 0.11 . 805 175 175 VAL CB C 31.90 0.14 . 806 175 175 VAL CG1 C 21.27 0.04 . 807 175 175 VAL CG2 C 24.42 0.01 . 808 175 175 VAL N N 116.91 0.09 . 809 176 176 GLN C C 178.43 0.30 . 810 176 176 GLN CA C 58.84 0.26 . 811 176 176 GLN CB C 28.20 0.09 . 812 176 176 GLN CD C 180.16 0.02 . 813 176 176 GLN CG C 34.39 0.00 . 814 176 176 GLN N N 116.68 0.33 . 815 176 176 GLN NE2 N 110.96 0.17 . 816 177 177 GLN C C 179.97 0.13 . 817 177 177 GLN CA C 59.26 0.15 . 818 177 177 GLN CB C 28.17 0.04 . 819 177 177 GLN CG C 34.43 0.00 . 820 177 177 GLN N N 119.10 0.09 . 821 178 178 TYR C C 177.90 0.12 . 822 178 178 TYR CA C 61.91 0.08 . 823 178 178 TYR CB C 38.34 0.04 . 824 178 178 TYR CE1 C 117.36 0.03 . 825 178 178 TYR CG C 129.83 0.09 . 826 178 178 TYR N N 126.49 0.17 . 827 179 179 ALA C C 179.68 0.07 . 828 179 179 ALA CA C 55.47 0.20 . 829 179 179 ALA CB C 18.38 0.09 . 830 179 179 ALA N N 120.20 0.13 . 831 180 180 ASP C C 179.74 0.03 . 832 180 180 ASP CA C 57.43 0.12 . 833 180 180 ASP CB C 40.02 0.18 . 834 180 180 ASP CG C 179.49 0.00 . 835 180 180 ASP N N 118.72 0.20 . 836 181 181 THR C C 176.38 0.13 . 837 181 181 THR CA C 67.55 0.13 . 838 181 181 THR CB C 67.57 0.06 . 839 181 181 THR CG2 C 21.75 0.00 . 840 181 181 THR N N 120.15 0.07 . 841 182 182 VAL C C 177.57 0.15 . 842 182 182 VAL CA C 67.67 0.19 . 843 182 182 VAL CB C 30.70 0.26 . 844 182 182 VAL CG1 C 24.07 0.29 . 845 182 182 VAL CG2 C 22.48 0.19 . 846 182 182 VAL N N 121.52 0.14 . 847 183 183 LYS CA C 60.54 0.00 . 848 183 183 LYS N N 120.92 0.09 . 849 184 184 TYR C C 177.79 0.08 . 850 184 184 TYR CA C 60.56 0.17 . 851 184 184 TYR CG C 129.96 0.09 . 852 184 184 TYR N N 120.10 0.00 . 853 185 185 LEU C C 179.30 0.08 . 854 185 185 LEU CA C 56.59 0.10 . 855 185 185 LEU CB C 42.20 0.09 . 856 185 185 LEU CG C 25.72 0.04 . 857 185 185 LEU N N 118.05 0.17 . 858 186 186 SER C C 175.70 0.14 . 859 186 186 SER CA C 61.85 0.10 . 860 186 186 SER CB C 62.61 0.05 . 861 186 186 SER N N 114.96 0.18 . 862 187 187 GLU C C 175.92 0.00 . 863 187 187 GLU CA C 56.11 0.11 . 864 187 187 GLU CB C 30.14 0.00 . 865 187 187 GLU CG C 36.82 0.00 . 866 187 187 GLU N N 119.36 0.16 . stop_ save_