data_19410 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Conformation and dynamics of the periplasmic membrane-protein chaperone complexes OmpX Skp and tOmpA Skp ; _BMRB_accession_number 19410 _BMRB_flat_file_name bmr19410.str _Entry_type original _Submission_date 2013-08-03 _Accession_date 2013-08-03 _Entry_origination author _NMR_STAR_version 2.1.1 _Experimental_method NMR _Details 'tOmpA (transmembrane domain of OmpA) backbone chemical shifts when bound to the Skp chaperone' loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Burmann Bjoern M. . 2 Wang Congwei . . 3 Hiller Sebastian . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 167 "13C chemical shifts" 424 "15N chemical shifts" 167 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2015-07-16 update author 'update entry citation' 2013-09-10 original author 'original release' stop_ loop_ _Related_BMRB_accession_number _Relationship 19407 'Corresponding chemical shifts of Skp when bound to its substrate OmpX' 19408 'Corresponding chemical shifts of apo-SKP' 19409 'Trimeric Skp bound with bound tOmpA' 19411 'OmpX within the trimeric chaperone Skp' stop_ _Original_release_date 2015-07-16 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; Conformation and dynamics of the periplasmic membrane-protein-chaperone complexes OmpX-Skp and tOmpA-Skp ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 24077225 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Burmann Bjoern M. . 2 Wang Congwei . . 3 Hiller Sebastian . . stop_ _Journal_abbreviation 'Nat. Struct. Mol. Biol.' _Journal_name_full 'Nature Structural and Molecular Biology' _Journal_volume 20 _Journal_issue 11 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 1265 _Page_last 1272 _Year 2013 _Details . save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name 'tOmpA within the tirmeric chaperone Skp' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label tOmpA $Escherichia_Coli_tOmpA 'Skp, chain 1' $Escherichia_Coli_Skp 'Skp, chain 2' $Escherichia_Coli_Skp 'Skp, chain 3' $Escherichia_Coli_Skp stop_ _System_molecular_weight 67100 _System_physical_state unfolded _System_oligomer_state ? _System_paramagnetic no _System_thiol_state . _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_Escherichia_Coli_tOmpA _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common Escherichia_Coli_tOmpA _Molecular_mass . _Mol_thiol_state 'not present' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 177 _Mol_residue_sequence ; MAPKDNTWYTGAKLGWSQYH DTGFINNNGPTHENQLGAGA FGGYQVNPYVGFEMGYDWLG RMPYKGSVENGAYKAQGVQL TAKLGYPITDDLDIYTRLGG MVWRADTKSNVYGKNHDTGV SPVFAGGVEYAITPEIATRL EYQWTNNIGDAHTIGTRPDN GMLSLGVSYRFGQGEAA ; loop_ _Residue_seq_code _Residue_label 1 MET 2 ALA 3 PRO 4 LYS 5 ASP 6 ASN 7 THR 8 TRP 9 TYR 10 THR 11 GLY 12 ALA 13 LYS 14 LEU 15 GLY 16 TRP 17 SER 18 GLN 19 TYR 20 HIS 21 ASP 22 THR 23 GLY 24 PHE 25 ILE 26 ASN 27 ASN 28 ASN 29 GLY 30 PRO 31 THR 32 HIS 33 GLU 34 ASN 35 GLN 36 LEU 37 GLY 38 ALA 39 GLY 40 ALA 41 PHE 42 GLY 43 GLY 44 TYR 45 GLN 46 VAL 47 ASN 48 PRO 49 TYR 50 VAL 51 GLY 52 PHE 53 GLU 54 MET 55 GLY 56 TYR 57 ASP 58 TRP 59 LEU 60 GLY 61 ARG 62 MET 63 PRO 64 TYR 65 LYS 66 GLY 67 SER 68 VAL 69 GLU 70 ASN 71 GLY 72 ALA 73 TYR 74 LYS 75 ALA 76 GLN 77 GLY 78 VAL 79 GLN 80 LEU 81 THR 82 ALA 83 LYS 84 LEU 85 GLY 86 TYR 87 PRO 88 ILE 89 THR 90 ASP 91 ASP 92 LEU 93 ASP 94 ILE 95 TYR 96 THR 97 ARG 98 LEU 99 GLY 100 GLY 101 MET 102 VAL 103 TRP 104 ARG 105 ALA 106 ASP 107 THR 108 LYS 109 SER 110 ASN 111 VAL 112 TYR 113 GLY 114 LYS 115 ASN 116 HIS 117 ASP 118 THR 119 GLY 120 VAL 121 SER 122 PRO 123 VAL 124 PHE 125 ALA 126 GLY 127 GLY 128 VAL 129 GLU 130 TYR 131 ALA 132 ILE 133 THR 134 PRO 135 GLU 136 ILE 137 ALA 138 THR 139 ARG 140 LEU 141 GLU 142 TYR 143 GLN 144 TRP 145 THR 146 ASN 147 ASN 148 ILE 149 GLY 150 ASP 151 ALA 152 HIS 153 THR 154 ILE 155 GLY 156 THR 157 ARG 158 PRO 159 ASP 160 ASN 161 GLY 162 MET 163 LEU 164 SER 165 LEU 166 GLY 167 VAL 168 SER 169 TYR 170 ARG 171 PHE 172 GLY 173 GLN 174 GLY 175 GLU 176 ALA 177 ALA stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-11-04 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 19940 OmpA 99.44 176 97.73 100.00 3.95e-122 PDB 1BXW "Outer Membrane Protein A (Ompa) Transmembrane Domain" 97.18 172 98.26 98.84 1.73e-119 PDB 1G90 "Nmr Solution Structure Of Outer Membrane Protein A Transmembrane Domain: 10 Conformers" 98.87 176 97.71 100.00 3.80e-121 PDB 1QJP "High Resolution Structure Of The Outer Membrane Protein A (ompa) Transmembrane Domain" 96.61 171 98.83 99.42 3.55e-119 PDB 2GE4 "High-Resolution Solution Structure Of Outer Membrane Protein A Transmembrane Domain" 100.00 177 97.74 100.00 5.97e-123 PDB 3NB3 "The Host Outer Membrane Proteins Ompa And Ompc Are Packed At Specific Sites In The Shigella Phage Sf6 Virion As Structural Comp" 99.44 346 98.86 99.43 1.39e-123 DBJ BAA35715 "outer membrane protein A (3a;II*;G;d) [Escherichia coli str. K12 substr. W3110]" 99.44 346 100.00 100.00 1.37e-125 DBJ BAB34464 "outer membrane protein 3a [Escherichia coli O157:H7 str. Sakai]" 99.44 346 100.00 100.00 1.37e-125 DBJ BAG76542 "outer membrane protein OmpA [Escherichia coli SE11]" 99.44 346 100.00 100.00 1.37e-125 DBJ BAI24400 "outer membrane protein A [Escherichia coli O26:H11 str. 11368]" 99.44 346 100.00 100.00 1.37e-125 DBJ BAI29850 "outer membrane protein A [Escherichia coli O103:H2 str. 12009]" 99.44 346 100.00 100.00 1.37e-125 EMBL CAA23588 "ompA protein [Escherichia coli]" 99.44 346 100.00 100.00 1.37e-125 EMBL CAP75420 "Outer membrane protein A [Escherichia coli LF82]" 99.44 346 98.30 98.86 3.05e-123 EMBL CAQ31485 "outer membrane protein 3a (II*;G;d) [Escherichia coli BL21(DE3)]" 99.44 346 100.00 100.00 1.37e-125 EMBL CAR02310 "outer membrane protein A (3a;II*;G;d) [Escherichia coli S88]" 99.44 346 99.43 100.00 2.01e-125 EMBL CAR07182 "outer membrane protein A (3a;II*;G;d) [Escherichia coli ED1a]" 99.44 346 98.30 99.43 3.73e-124 GB AAC74043 "outer membrane protein A (3a;II*;G;d) [Escherichia coli str. K-12 substr. MG1655]" 99.44 346 100.00 100.00 1.37e-125 GB AAF37887 "outer membrane protein A [Escherichia coli RS218]" 99.44 346 99.43 100.00 2.01e-125 GB AAG55443 "outer membrane protein 3a (II*;G;d) [Escherichia coli O157:H7 str. EDL933]" 99.44 346 100.00 100.00 1.37e-125 GB AAP74759 "outer membrane protein A precursor [Shigella sonnei]" 99.44 346 100.00 100.00 1.37e-125 GB AAT02227 "outer membrane protein A precursor [Shigella boydii]" 99.44 346 100.00 100.00 1.51e-125 REF NP_309068 "outer membrane protein A [Escherichia coli O157:H7 str. Sakai]" 99.44 346 100.00 100.00 1.37e-125 REF NP_415477 "outer membrane protein A (3a;II*;G;d) [Escherichia coli str. K-12 substr. MG1655]" 99.44 346 100.00 100.00 1.37e-125 REF WP_000315442 "membrane protein, partial [Escherichia coli]" 99.44 343 100.00 100.00 2.14e-125 REF WP_000630860 "membrane protein, partial [Escherichia coli]" 99.44 335 100.00 100.00 2.71e-125 REF WP_000750416 "MULTISPECIES: outer membrane protein A [Enterobacteriaceae]" 99.44 346 100.00 100.00 1.37e-125 SP P0A910 "RecName: Full=Outer membrane protein A; AltName: Full=Outer membrane protein II*; Flags: Precursor" 99.44 346 100.00 100.00 1.37e-125 SP P0A911 "RecName: Full=Outer membrane protein A; AltName: Full=Outer membrane protein II*; Flags: Precursor" 99.44 346 100.00 100.00 1.37e-125 stop_ save_ save_Escherichia_Coli_Skp _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common Escherichia_Coli_Skp _Molecular_mass . _Mol_thiol_state 'not present' _Details . _Residue_count 162 _Mol_residue_sequence ; MGSSHHHHHHSSGLVPRGSH MADKIAIVNMGSLFQQVAQK TGVSNTLENEFKGRASELQR METDLQAKMKKLQSMKAGSD RTKLEKDVMAQRQTFAQKAQ AFEQDRARRSNEERGKLVTR IQTAVKSVANSQDIDLVVDA NAVAYNSSDVKDITADVLKQ VK ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 0 MET 2 1 GLY 3 2 SER 4 3 SER 5 4 HIS 6 5 HIS 7 6 HIS 8 7 HIS 9 8 HIS 10 9 HIS 11 10 SER 12 11 SER 13 12 GLY 14 13 LEU 15 14 VAL 16 15 PRO 17 16 ARG 18 17 GLY 19 18 SER 20 19 HIS 21 20 MET 22 21 ALA 23 22 ASP 24 23 LYS 25 24 ILE 26 25 ALA 27 26 ILE 28 27 VAL 29 28 ASN 30 29 MET 31 30 GLY 32 31 SER 33 32 LEU 34 33 PHE 35 34 GLN 36 35 GLN 37 36 VAL 38 37 ALA 39 38 GLN 40 39 LYS 41 40 THR 42 41 GLY 43 42 VAL 44 43 SER 45 44 ASN 46 45 THR 47 46 LEU 48 47 GLU 49 48 ASN 50 49 GLU 51 50 PHE 52 51 LYS 53 52 GLY 54 53 ARG 55 54 ALA 56 55 SER 57 56 GLU 58 57 LEU 59 58 GLN 60 59 ARG 61 60 MET 62 61 GLU 63 62 THR 64 63 ASP 65 64 LEU 66 65 GLN 67 66 ALA 68 67 LYS 69 68 MET 70 69 LYS 71 70 LYS 72 71 LEU 73 72 GLN 74 73 SER 75 74 MET 76 75 LYS 77 76 ALA 78 77 GLY 79 78 SER 80 79 ASP 81 80 ARG 82 81 THR 83 82 LYS 84 83 LEU 85 84 GLU 86 85 LYS 87 86 ASP 88 87 VAL 89 88 MET 90 89 ALA 91 90 GLN 92 91 ARG 93 92 GLN 94 93 THR 95 94 PHE 96 95 ALA 97 96 GLN 98 97 LYS 99 98 ALA 100 99 GLN 101 100 ALA 102 101 PHE 103 102 GLU 104 103 GLN 105 104 ASP 106 105 ARG 107 106 ALA 108 107 ARG 109 108 ARG 110 109 SER 111 110 ASN 112 111 GLU 113 112 GLU 114 113 ARG 115 114 GLY 116 115 LYS 117 116 LEU 118 117 VAL 119 118 THR 120 119 ARG 121 120 ILE 122 121 GLN 123 122 THR 124 123 ALA 125 124 VAL 126 125 LYS 127 126 SER 128 127 VAL 129 128 ALA 130 129 ASN 131 130 SER 132 131 GLN 133 132 ASP 134 133 ILE 135 134 ASP 136 135 LEU 137 136 VAL 138 137 VAL 139 138 ASP 140 139 ALA 141 140 ASN 142 141 ALA 143 142 VAL 144 143 ALA 145 144 TYR 146 145 ASN 147 146 SER 148 147 SER 149 148 ASP 150 149 VAL 151 150 LYS 152 151 ASP 153 152 ILE 154 153 THR 155 154 ALA 156 155 ASP 157 156 VAL 158 157 LEU 159 158 LYS 160 159 GLN 161 160 VAL 162 161 LYS stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date . 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 UNP P0AEU7 . . . . . . stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species _Strain $Escherichia_Coli_tOmpA 'E. coli' 562 Bacteria . Escherichia coli K12 $Escherichia_Coli_Skp 'E. coli' 562 Bacteria . Escherichia coli K12 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 $Escherichia_Coli_tOmpA 'recombinant technology' . Escherichia coli 'BL21 (DE3)' pET28B-tOmpA $Escherichia_Coli_Skp 'recombinant technology' . Escherichia coli 'BL21 (DE3)' pET28B-Skp stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Saveframe_category sample _Sample_type solution _Details 'Protein samples were produced as a 3:1 ratio (Skp monomer per tOmpA)' loop_ _Mol_label _Concentration_value _Concentration_value_units _Concentration_min_value _Concentration_max_value _Isotopic_labeling $Escherichia_Coli_tOmpA . mM 0.6 1.05 '[U-13C; U-15N; U-2H]' $Escherichia_Coli_Skp . mM 0.6 1.05 '[U-99% 2H]' D2O 5 % . . 'natural abundance' MES 25 mM . . 'natural abundance' NaCl 150 mM . . 'natural abundance' stop_ save_ ############################ # Computer software used # ############################ save_TOPSPIN _Saveframe_category software _Name TOPSPIN _Version 3.2 loop_ _Vendor _Address _Electronic_address 'Bartels et al.' . . 'Bruker Biospin' . . Guntert . . 'Keller and Wuthrich' . . stop_ loop_ _Task 'chemical shift assignment' collection 'data analysis' processing stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model AscendII _Field_strength 700 _Details . save_ save_spectrometer_2 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model Avance _Field_strength 800 _Details . save_ ############################# # NMR applied experiments # ############################# save_2D_1H-15N_HSQC_1 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-15N HSQC' _Sample_label $sample_1 save_ save_3D_HNCA_2 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCA' _Sample_label $sample_1 save_ save_3D_HNCO_3 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCO' _Sample_label $sample_1 save_ save_3D_HNCACB_4 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCACB' _Sample_label $sample_1 save_ save_3D_HN(CA)CO_5 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HN(CA)CO' _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 'ionic strength' 0.150 . M pH 6.5 . pH pressure 1 . atm temperature 310 . 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_assigned_chem_shift_list_1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Experiment_label '2D 1H-15N HSQC' '3D HNCA' '3D HNCO' '3D HNCACB' '3D HN(CA)CO' 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 tOmpA _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 MET H H 8.45 0.02 1 2 1 1 MET C C 175.4 0.3 1 3 1 1 MET CA C 57.1 0.3 1 4 1 1 MET N N 119.9 0.3 1 5 2 2 ALA H H 8.05 0.02 1 6 2 2 ALA C C 177.6 0.3 1 7 2 2 ALA CA C 51.7 0.3 1 8 2 2 ALA CB C 18.4 0.3 1 9 2 2 ALA N N 125.4 0.3 1 10 4 4 LYS H H 8.30 0.02 1 11 4 4 LYS C C 175.2 0.3 1 12 4 4 LYS CA C 56.0 0.3 1 13 4 4 LYS CB C 29.7 0.3 1 14 4 4 LYS N N 124.0 0.3 1 15 5 5 ASP H H 8.24 0.02 1 16 5 5 ASP C C 176.2 0.3 1 17 5 5 ASP CA C 54.1 0.3 1 18 5 5 ASP CB C 40.6 0.3 1 19 5 5 ASP N N 120.9 0.3 1 20 6 6 ASN H H 8.14 0.02 1 21 6 6 ASN C C 175.4 0.3 1 22 6 6 ASN CA C 53.8 0.3 1 23 6 6 ASN CB C 38.0 0.3 1 24 6 6 ASN N N 121.0 0.3 1 25 7 7 THR H H 7.94 0.02 1 26 7 7 THR CA C 61.6 0.3 1 27 7 7 THR CB C 69.2 0.3 1 28 7 7 THR N N 115.1 0.3 1 29 8 8 TRP H H 8.44 0.02 1 30 8 8 TRP CA C 56.1 0.3 1 31 8 8 TRP CB C 29.3 0.3 1 32 8 8 TRP N N 123.8 0.3 1 33 9 9 TYR H H 7.93 0.02 1 34 9 9 TYR CA C 57.2 0.3 1 35 9 9 TYR CB C 37.9 0.3 1 36 9 9 TYR N N 120.8 0.3 1 37 10 10 THR H H 7.81 0.02 1 38 10 10 THR C C 174.9 0.3 1 39 10 10 THR CA C 61.5 0.3 1 40 10 10 THR CB C 69.6 0.3 1 41 10 10 THR N N 115.2 0.3 1 42 11 11 GLY H H 7.60 0.02 1 43 11 11 GLY C C 173.7 0.3 1 44 11 11 GLY CA C 44.9 0.3 1 45 11 11 GLY N N 110.3 0.3 1 46 12 12 ALA H H 7.92 0.02 1 47 12 12 ALA C C 177.6 0.3 1 48 12 12 ALA CA C 52.1 0.3 1 49 12 12 ALA CB C 18.5 0.3 1 50 12 12 ALA N N 123.6 0.3 1 51 13 13 LYS H H 8.08 0.02 1 52 13 13 LYS C C 176.2 0.3 1 53 13 13 LYS CA C 55.3 0.3 1 54 13 13 LYS CB C 31.5 0.3 1 55 13 13 LYS N N 120.3 0.3 1 56 14 14 LEU H H 8.15 0.02 1 57 14 14 LEU CA C 54.9 0.3 1 58 14 14 LEU CB C 40.9 0.3 1 59 14 14 LEU N N 122.1 0.3 1 60 15 15 GLY H H 8.20 0.02 1 61 15 15 GLY CA C 44.7 0.3 1 62 15 15 GLY N N 108.8 0.3 1 63 18 18 GLN H H 8.03 0.02 1 64 18 18 GLN C C 179.0 0.3 1 65 18 18 GLN CA C 55.6 0.3 1 66 18 18 GLN CB C 29.3 0.3 1 67 18 18 GLN N N 121.3 0.3 1 68 19 19 TYR H H 8.12 0.02 1 69 19 19 TYR CA C 56.7 0.3 1 70 19 19 TYR CB C 38.3 0.3 1 71 19 19 TYR N N 122.8 0.3 1 72 20 20 HIS H H 8.18 0.02 1 73 20 20 HIS C C 177.9 0.3 1 74 20 20 HIS CA C 55.6 0.3 1 75 20 20 HIS CB C 28.5 0.3 1 76 20 20 HIS N N 122.5 0.3 1 77 21 21 ASP H H 8.23 0.02 1 78 21 21 ASP C C 175.9 0.3 1 79 21 21 ASP CA C 54.1 0.3 1 80 21 21 ASP CB C 40.6 0.3 1 81 21 21 ASP N N 120.6 0.3 1 82 22 22 THR H H 8.07 0.02 1 83 22 22 THR C C 175.3 0.3 1 84 22 22 THR CA C 61.7 0.3 1 85 22 22 THR CB C 69.4 0.3 1 86 22 22 THR N N 114.0 0.3 1 87 23 23 GLY H H 8.38 0.02 1 88 23 23 GLY C C 173.9 0.3 1 89 23 23 GLY CA C 45.0 0.3 1 90 23 23 GLY N N 111.3 0.3 1 91 24 24 PHE H H 8.03 0.02 1 92 24 24 PHE CA C 57.6 0.3 1 93 24 24 PHE CB C 38.6 0.3 1 94 24 24 PHE N N 119.8 0.3 1 95 25 25 ILE H H 7.89 0.02 1 96 25 25 ILE C C 175.4 0.3 1 97 25 25 ILE CA C 60.6 0.3 1 98 25 25 ILE CB C 37.6 0.3 1 99 25 25 ILE N N 121.4 0.3 1 100 26 26 ASN H H 8.25 0.02 1 101 26 26 ASN C C 174.8 0.3 1 102 26 26 ASN CA C 52.8 0.3 1 103 26 26 ASN CB C 38.4 0.3 1 104 26 26 ASN N N 122.1 0.3 1 105 27 27 ASN H H 8.30 0.02 1 106 27 27 ASN C C 175.9 0.3 1 107 27 27 ASN CA C 53.1 0.3 1 108 27 27 ASN CB C 38.1 0.3 1 109 27 27 ASN N N 119.6 0.3 1 110 28 28 ASN H H 8.32 0.02 1 111 28 28 ASN C C 175.1 0.3 1 112 28 28 ASN CA C 52.9 0.3 1 113 28 28 ASN CB C 38.4 0.3 1 114 28 28 ASN N N 119.2 0.3 1 115 29 29 GLY H H 8.05 0.02 1 116 29 29 GLY C C 171.8 0.3 1 117 29 29 GLY CA C 44.2 0.3 1 118 29 29 GLY N N 109.1 0.3 1 119 31 31 THR H H 8.14 0.02 1 120 31 31 THR C C 174.6 0.3 1 121 31 31 THR CA C 61.5 0.3 1 122 31 31 THR CB C 69.2 0.3 1 123 31 31 THR N N 113.9 0.3 1 124 32 32 HIS H H 8.25 0.02 1 125 32 32 HIS C C 177.8 0.3 1 126 32 32 HIS CA C 55.7 0.3 1 127 32 32 HIS CB C 29.5 0.3 1 128 32 32 HIS N N 124.3 0.3 1 129 33 33 GLU H H 7.96 0.02 1 130 33 33 GLU C C 178.6 0.3 1 131 33 33 GLU CA C 56.9 0.3 1 132 33 33 GLU CB C 28.8 0.3 1 133 33 33 GLU N N 122.2 0.3 1 134 34 34 ASN H H 8.30 0.02 1 135 34 34 ASN C C 176.2 0.3 1 136 34 34 ASN CA C 53.0 0.3 1 137 34 34 ASN CB C 38.3 0.3 1 138 34 34 ASN N N 119.8 0.3 1 139 35 35 GLN H H 7.98 0.02 1 140 35 35 GLN C C 176.2 0.3 1 141 35 35 GLN CA C 55.3 0.3 1 142 35 35 GLN CB C 28.6 0.3 1 143 35 35 GLN N N 122.3 0.3 1 144 36 36 LEU H H 8.10 0.02 1 145 36 36 LEU C C 174.0 0.3 1 146 36 36 LEU CA C 54.9 0.3 1 147 36 36 LEU CB C 41.5 0.3 1 148 36 36 LEU N N 123.9 0.3 1 149 37 37 GLY H H 8.25 0.02 1 150 37 37 GLY C C 174.1 0.3 1 151 37 37 GLY CA C 45.0 0.3 1 152 37 37 GLY N N 109.0 0.3 1 153 38 38 ALA H H 8.08 0.02 1 154 38 38 ALA C C 178.3 0.3 1 155 38 38 ALA CA C 52.3 0.3 1 156 38 38 ALA CB C 18.5 0.3 1 157 38 38 ALA N N 123.8 0.3 1 158 39 39 GLY H H 8.28 0.02 1 159 39 39 GLY C C 174.1 0.3 1 160 39 39 GLY CA C 45.0 0.3 1 161 39 39 GLY N N 108.0 0.3 1 162 40 40 ALA H H 7.96 0.02 1 163 40 40 ALA C C 177.6 0.3 1 164 40 40 ALA CA C 52.2 0.3 1 165 40 40 ALA CB C 18.4 0.3 1 166 40 40 ALA N N 123.7 0.3 1 167 41 41 PHE H H 8.14 0.02 1 168 41 41 PHE C C 176.2 0.3 1 169 41 41 PHE CA C 57.4 0.3 1 170 41 41 PHE CB C 38.3 0.3 1 171 41 41 PHE N N 118.4 0.3 1 172 42 42 GLY H H 8.10 0.02 1 173 42 42 GLY C C 174.3 0.3 1 174 42 42 GLY CA C 45.0 0.3 1 175 42 42 GLY N N 110.1 0.3 1 176 43 43 GLY H H 7.81 0.02 1 177 43 43 GLY C C 173.7 0.3 1 178 43 43 GLY CA C 44.8 0.3 1 179 43 43 GLY N N 108.3 0.3 1 180 44 44 TYR H H 7.98 0.02 1 181 44 44 TYR C C 175.5 0.3 1 182 44 44 TYR CA C 57.4 0.3 1 183 44 44 TYR CB C 37.8 0.3 1 184 44 44 TYR N N 120.1 0.3 1 185 45 45 GLN H H 7.96 0.02 1 186 45 45 GLN C C 177.4 0.3 1 187 45 45 GLN CA C 55.5 0.3 1 188 45 45 GLN CB C 28.7 0.3 1 189 45 45 GLN N N 122.7 0.3 1 190 46 46 VAL H H 7.90 0.02 1 191 46 46 VAL CA C 61.7 0.3 1 192 46 46 VAL CB C 31.7 0.3 1 193 46 46 VAL N N 119.8 0.3 1 194 47 47 ASN H H 8.30 0.02 1 195 47 47 ASN CA C 51.0 0.3 1 196 47 47 ASN CB C 38.5 0.3 1 197 47 47 ASN N N 123.1 0.3 1 198 49 49 TYR H H 8.35 0.02 1 199 49 49 TYR CA C 61.4 0.3 1 200 49 49 TYR CB C 36.8 0.3 1 201 49 49 TYR N N 122.6 0.3 1 202 50 50 VAL H H 8.00 0.02 1 203 50 50 VAL CA C 61.1 0.3 1 204 50 50 VAL CB C 31.4 0.3 1 205 50 50 VAL N N 121.1 0.3 1 206 51 51 GLY H H 8.28 0.02 1 207 51 51 GLY C C 176.7 0.3 1 208 51 51 GLY CA C 44.8 0.3 1 209 51 51 GLY N N 112.2 0.3 1 210 52 52 PHE H H 7.90 0.02 1 211 52 52 PHE CA C 57.5 0.3 1 212 52 52 PHE CB C 38.3 0.3 1 213 52 52 PHE N N 120.0 0.3 1 214 53 53 GLU H H 7.96 0.02 1 215 53 53 GLU C C 175.8 0.3 1 216 53 53 GLU CA C 57.5 0.3 1 217 53 53 GLU CB C 28.5 0.3 1 218 53 53 GLU N N 122.5 0.3 1 219 54 54 MET H H 8.39 0.02 1 220 54 54 MET C C 175.9 0.3 1 221 54 54 MET CA C 56.3 0.3 1 222 54 54 MET CB C 32.6 0.3 1 223 54 54 MET N N 122.3 0.3 1 224 55 55 GLY H H 7.96 0.02 1 225 55 55 GLY C C 173.7 0.3 1 226 55 55 GLY CA C 44.9 0.3 1 227 55 55 GLY N N 111.0 0.3 1 228 56 56 TYR H H 7.80 0.02 1 229 56 56 TYR C C 173.9 0.3 1 230 56 56 TYR CA C 55.8 0.3 1 231 56 56 TYR CB C 37.5 0.3 1 232 56 56 TYR N N 120.9 0.3 1 233 57 57 ASP H H 8.21 0.02 1 234 57 57 ASP CA C 54.3 0.3 1 235 57 57 ASP CB C 40.5 0.3 1 236 57 57 ASP N N 120.3 0.3 1 237 58 58 TRP H H 8.32 0.02 1 238 58 58 TRP C C 174.4 0.3 1 239 58 58 TRP CA C 55.9 0.3 1 240 58 58 TRP CB C 29.5 0.3 1 241 58 58 TRP N N 124.8 0.3 1 242 59 59 LEU H H 8.28 0.02 1 243 59 59 LEU CA C 55.3 0.3 1 244 59 59 LEU CB C 41.0 0.3 1 245 59 59 LEU N N 123.7 0.3 1 246 60 60 GLY H H 8.13 0.02 1 247 60 60 GLY C C 174.6 0.3 1 248 60 60 GLY CA C 44.9 0.3 1 249 60 60 GLY N N 108.6 0.3 1 250 61 61 ARG H H 7.99 0.02 1 251 61 61 ARG C C 177.1 0.3 1 252 61 61 ARG CA C 55.9 0.3 1 253 61 61 ARG CB C 31.4 0.3 1 254 61 61 ARG N N 120.7 0.3 1 255 62 62 MET H H 8.33 0.02 1 256 62 62 MET C C 175.0 0.3 1 257 62 62 MET CA C 56.1 0.3 1 258 62 62 MET CB C 31.7 0.3 1 259 62 62 MET N N 120.7 0.3 1 260 64 64 TYR H H 7.58 0.02 1 261 64 64 TYR CA C 57.5 0.3 1 262 64 64 TYR CB C 37.6 0.3 1 263 64 64 TYR N N 120.1 0.3 1 264 65 65 LYS H H 8.27 0.02 1 265 65 65 LYS CA C 55.8 0.3 1 266 65 65 LYS CB C 32.6 0.3 1 267 65 65 LYS N N 117.5 0.3 1 268 66 66 GLY H H 7.80 0.02 1 269 66 66 GLY C C 173.8 0.3 1 270 66 66 GLY CA C 44.8 0.3 1 271 66 66 GLY N N 109.4 0.3 1 272 67 67 SER H H 8.09 0.02 1 273 67 67 SER CA C 57.9 0.3 1 274 67 67 SER CB C 63.4 0.3 1 275 67 67 SER N N 115.8 0.3 1 276 68 68 VAL H H 8.11 0.02 1 277 68 68 VAL C C 176.0 0.3 1 278 68 68 VAL CA C 62.0 0.3 1 279 68 68 VAL CB C 31.4 0.3 1 280 68 68 VAL N N 121.3 0.3 1 281 69 69 GLU H H 8.34 0.02 1 282 69 69 GLU CA C 55.6 0.3 1 283 69 69 GLU CB C 28.7 0.3 1 284 69 69 GLU N N 123.6 0.3 1 285 70 70 ASN H H 8.23 0.02 1 286 70 70 ASN CA C 52.8 0.3 1 287 70 70 ASN CB C 38.0 0.3 1 288 70 70 ASN N N 120.6 0.3 1 289 71 71 GLY H H 8.06 0.02 1 290 71 71 GLY C C 173.9 0.3 1 291 71 71 GLY CA C 45.1 0.3 1 292 71 71 GLY N N 108.4 0.3 1 293 72 72 ALA H H 7.99 0.02 1 294 72 72 ALA C C 177.5 0.3 1 295 72 72 ALA CA C 52.3 0.3 1 296 72 72 ALA CB C 18.5 0.3 1 297 72 72 ALA N N 123.6 0.3 1 298 73 73 TYR H H 7.98 0.02 1 299 73 73 TYR C C 175.6 0.3 1 300 73 73 TYR CA C 57.7 0.3 1 301 73 73 TYR CB C 37.5 0.3 1 302 73 73 TYR N N 118.8 0.3 1 303 74 74 LYS H H 7.85 0.02 1 304 74 74 LYS CA C 55.6 0.3 1 305 74 74 LYS CB C 32.0 0.3 1 306 74 74 LYS N N 123.2 0.3 1 307 75 75 ALA H H 8.06 0.02 1 308 75 75 ALA CA C 52.1 0.3 1 309 75 75 ALA CB C 18.3 0.3 1 310 75 75 ALA N N 125.0 0.3 1 311 76 76 GLN H H 8.21 0.02 1 312 76 76 GLN C C 176.3 0.3 1 313 76 76 GLN CA C 55.6 0.3 1 314 76 76 GLN CB C 28.5 0.3 1 315 76 76 GLN N N 119.3 0.3 1 316 77 77 GLY H H 8.28 0.02 1 317 77 77 GLY C C 174.0 0.3 1 318 77 77 GLY CA C 45.0 0.3 1 319 77 77 GLY N N 109.8 0.3 1 320 78 78 VAL H H 7.90 0.02 1 321 78 78 VAL C C 176.3 0.3 1 322 78 78 VAL CA C 62.0 0.3 1 323 78 78 VAL CB C 31.3 0.3 1 324 78 78 VAL N N 119.5 0.3 1 325 79 79 GLN H H 8.41 0.02 1 326 79 79 GLN C C 176.3 0.3 1 327 79 79 GLN CA C 56.1 0.3 1 328 79 79 GLN CB C 29.2 0.3 1 329 79 79 GLN N N 123.7 0.3 1 330 80 80 LEU H H 7.96 0.02 1 331 80 80 LEU CA C 57.4 0.3 1 332 80 80 LEU CB C 43.8 0.3 1 333 80 80 LEU N N 120.8 0.3 1 334 81 81 THR H H 7.79 0.02 1 335 81 81 THR C C 174.4 0.3 1 336 81 81 THR CA C 61.3 0.3 1 337 81 81 THR CB C 69.0 0.3 1 338 81 81 THR N N 115.2 0.3 1 339 82 82 ALA H H 8.09 0.02 1 340 82 82 ALA CA C 52.3 0.3 1 341 82 82 ALA CB C 18.4 0.3 1 342 82 82 ALA N N 125.7 0.3 1 343 83 83 LYS H H 8.07 0.02 1 344 83 83 LYS CA C 55.8 0.3 1 345 83 83 LYS CB C 31.7 0.3 1 346 83 83 LYS N N 120.2 0.3 1 347 84 84 LEU H H 7.99 0.02 1 348 84 84 LEU CA C 54.6 0.3 1 349 84 84 LEU CB C 41.6 0.3 1 350 84 84 LEU N N 122.6 0.3 1 351 85 85 GLY H H 8.02 0.02 1 352 85 85 GLY CA C 44.1 0.3 1 353 85 85 GLY N N 109.1 0.3 1 354 86 86 TYR H H 7.85 0.02 1 355 86 86 TYR CA C 56.7 0.3 1 356 86 86 TYR CB C 37.8 0.3 1 357 86 86 TYR N N 120.7 0.3 1 358 88 88 ILE H H 7.94 0.02 1 359 88 88 ILE C C 178.3 0.3 1 360 88 88 ILE CA C 62.1 0.3 1 361 88 88 ILE CB C 37.7 0.3 1 362 88 88 ILE N N 119.2 0.3 1 363 89 89 THR H H 7.90 0.02 1 364 89 89 THR CA C 62.8 0.3 1 365 89 89 THR CB C 69.0 0.3 1 366 89 89 THR N N 112.4 0.3 1 367 90 90 ASP H H 8.28 0.02 1 368 90 90 ASP C C 176.0 0.3 1 369 90 90 ASP CA C 53.7 0.3 1 370 90 90 ASP CB C 40.7 0.3 1 371 90 90 ASP N N 120.1 0.3 1 372 91 91 ASP H H 8.18 0.02 1 373 91 91 ASP C C 176.4 0.3 1 374 91 91 ASP CA C 54.9 0.3 1 375 91 91 ASP CB C 41.4 0.3 1 376 91 91 ASP N N 123.9 0.3 1 377 92 92 LEU H H 8.02 0.02 1 378 92 92 LEU C C 175.3 0.3 1 379 92 92 LEU CA C 56.6 0.3 1 380 92 92 LEU CB C 44.1 0.3 1 381 92 92 LEU N N 122.1 0.3 1 382 93 93 ASP H H 8.44 0.02 1 383 93 93 ASP C C 176.0 0.3 1 384 93 93 ASP CA C 53.0 0.3 1 385 93 93 ASP CB C 38.1 0.3 1 386 93 93 ASP N N 119.5 0.3 1 387 94 94 ILE H H 7.75 0.02 1 388 94 94 ILE CA C 61.5 0.3 1 389 94 94 ILE CB C 37.4 0.3 1 390 94 94 ILE N N 119.0 0.3 1 391 95 95 TYR H H 7.91 0.02 1 392 95 95 TYR CA C 57.0 0.3 1 393 95 95 TYR CB C 38.7 0.3 1 394 95 95 TYR N N 119.7 0.3 1 395 96 96 THR H H 7.93 0.02 1 396 96 96 THR C C 175.5 0.3 1 397 96 96 THR CA C 62.6 0.3 1 398 96 96 THR CB C 68.6 0.3 1 399 96 96 THR N N 115.1 0.3 1 400 97 97 ARG H H 7.60 0.02 1 401 97 97 ARG C C 175.4 0.3 1 402 97 97 ARG CA C 57.5 0.3 1 403 97 97 ARG CB C 30.8 0.3 1 404 97 97 ARG N N 120.4 0.3 1 405 98 98 LEU H H 8.07 0.02 1 406 98 98 LEU CA C 55.1 0.3 1 407 98 98 LEU CB C 41.1 0.3 1 408 98 98 LEU N N 122.3 0.3 1 409 99 99 GLY H H 8.28 0.02 1 410 99 99 GLY C C 174.5 0.3 1 411 99 99 GLY CA C 45.2 0.3 1 412 99 99 GLY N N 109.3 0.3 1 413 100 100 GLY H H 8.14 0.02 1 414 100 100 GLY C C 174.5 0.3 1 415 100 100 GLY CA C 44.8 0.3 1 416 100 100 GLY N N 109.0 0.3 1 417 101 101 MET H H 8.17 0.02 1 418 101 101 MET C C 176.5 0.3 1 419 101 101 MET CA C 55.3 0.3 1 420 101 101 MET CB C 31.7 0.3 1 421 101 101 MET N N 120.2 0.3 1 422 102 102 VAL H H 8.00 0.02 1 423 102 102 VAL C C 176.2 0.3 1 424 102 102 VAL CA C 61.2 0.3 1 425 102 102 VAL CB C 31.7 0.3 1 426 102 102 VAL N N 120.9 0.3 1 427 103 103 TRP H H 8.30 0.02 1 428 103 103 TRP C C 172.9 0.3 1 429 103 103 TRP CA C 55.8 0.3 1 430 103 103 TRP CB C 29.4 0.3 1 431 103 103 TRP N N 121.0 0.3 1 432 104 104 ARG H H 8.03 0.02 1 433 104 104 ARG CA C 55.5 0.3 1 434 104 104 ARG CB C 29.2 0.3 1 435 104 104 ARG N N 122.0 0.3 1 436 105 105 ALA H H 8.10 0.02 1 437 105 105 ALA CA C 52.1 0.3 1 438 105 105 ALA CB C 18.2 0.3 1 439 105 105 ALA N N 125.0 0.3 1 440 106 106 ASP H H 8.24 0.02 1 441 106 106 ASP C C 175.7 0.3 1 442 106 106 ASP CA C 53.8 0.3 1 443 106 106 ASP CB C 40.7 0.3 1 444 106 106 ASP N N 119.4 0.3 1 445 107 107 THR H H 7.97 0.02 1 446 107 107 THR C C 173.6 0.3 1 447 107 107 THR CA C 61.8 0.3 1 448 107 107 THR CB C 69.4 0.3 1 449 107 107 THR N N 114.5 0.3 1 450 108 108 LYS H H 7.91 0.02 1 451 108 108 LYS CA C 55.2 0.3 1 452 108 108 LYS CB C 31.3 0.3 1 453 108 108 LYS N N 119.8 0.3 1 454 109 109 SER H H 8.10 0.02 1 455 109 109 SER CA C 57.9 0.3 1 456 109 109 SER CB C 63.2 0.3 1 457 109 109 SER N N 116.1 0.3 1 458 110 110 ASN H H 8.36 0.02 1 459 110 110 ASN CA C 52.9 0.3 1 460 110 110 ASN CB C 37.8 0.3 1 461 110 110 ASN N N 119.5 0.3 1 462 111 111 VAL H H 7.88 0.02 1 463 111 111 VAL C C 175.9 0.3 1 464 111 111 VAL CA C 61.9 0.3 1 465 111 111 VAL CB C 31.7 0.3 1 466 111 111 VAL N N 119.6 0.3 1 467 112 112 TYR H H 8.08 0.02 1 468 112 112 TYR C C 175.3 0.3 1 469 112 112 TYR CA C 57.5 0.3 1 470 112 112 TYR CB C 37.9 0.3 1 471 112 112 TYR N N 123.0 0.3 1 472 113 113 GLY H H 8.30 0.02 1 473 113 113 GLY C C 173.9 0.3 1 474 113 113 GLY CA C 44.9 0.3 1 475 113 113 GLY N N 111.1 0.3 1 476 114 114 LYS H H 8.09 0.02 1 477 114 114 LYS C C 175.2 0.3 1 478 114 114 LYS CA C 55.4 0.3 1 479 114 114 LYS CB C 31.9 0.3 1 480 114 114 LYS N N 120.3 0.3 1 481 115 115 ASN H H 8.08 0.02 1 482 115 115 ASN C C 175.2 0.3 1 483 115 115 ASN CA C 53.9 0.3 1 484 115 115 ASN CB C 40.5 0.3 1 485 115 115 ASN N N 121.2 0.3 1 486 116 116 HIS H H 8.23 0.02 1 487 116 116 HIS C C 176.3 0.3 1 488 116 116 HIS CA C 56.2 0.3 1 489 116 116 HIS CB C 31.3 0.3 1 490 116 116 HIS N N 122.9 0.3 1 491 117 117 ASP H H 8.14 0.02 1 492 117 117 ASP CA C 54.0 0.3 1 493 117 117 ASP CB C 40.6 0.3 1 494 117 117 ASP N N 121.0 0.3 1 495 118 118 THR H H 8.02 0.02 1 496 118 118 THR C C 176.4 0.3 1 497 118 118 THR CA C 61.7 0.3 1 498 118 118 THR CB C 69.0 0.3 1 499 118 118 THR N N 113.9 0.3 1 500 119 119 GLY H H 8.32 0.02 1 501 119 119 GLY C C 173.9 0.3 1 502 119 119 GLY CA C 44.8 0.3 1 503 119 119 GLY N N 110.8 0.3 1 504 120 120 VAL H H 7.82 0.02 1 505 120 120 VAL C C 176.1 0.3 1 506 120 120 VAL CA C 61.7 0.3 1 507 120 120 VAL CB C 31.8 0.3 1 508 120 120 VAL N N 118.9 0.3 1 509 121 121 SER H H 8.21 0.02 1 510 121 121 SER C C 176.1 0.3 1 511 121 121 SER CA C 57.8 0.3 1 512 121 121 SER CB C 63.0 0.3 1 513 121 121 SER N N 118.7 0.3 1 514 123 123 VAL H H 8.08 0.02 1 515 123 123 VAL C C 176.2 0.3 1 516 123 123 VAL CA C 60.8 0.3 1 517 123 123 VAL CB C 30.8 0.3 1 518 123 123 VAL N N 120.7 0.3 1 519 124 124 PHE H H 7.98 0.02 1 520 124 124 PHE CA C 57.5 0.3 1 521 124 124 PHE CB C 38.8 0.3 1 522 124 124 PHE N N 119.6 0.3 1 523 125 125 ALA H H 8.03 0.02 1 524 125 125 ALA CA C 51.9 0.3 1 525 125 125 ALA CB C 18.5 0.3 1 526 125 125 ALA N N 124.9 0.3 1 527 126 126 GLY H H 7.87 0.02 1 528 126 126 GLY C C 176.4 0.3 1 529 126 126 GLY CA C 45.1 0.3 1 530 126 126 GLY N N 107.7 0.3 1 531 127 127 GLY H H 8.17 0.02 1 532 127 127 GLY CA C 44.8 0.3 1 533 127 127 GLY N N 109.1 0.3 1 534 128 128 VAL H H 7.86 0.02 1 535 128 128 VAL C C 176.0 0.3 1 536 128 128 VAL CA C 61.7 0.3 1 537 128 128 VAL CB C 31.7 0.3 1 538 128 128 VAL N N 119.1 0.3 1 539 129 129 GLU H H 8.42 0.02 1 540 129 129 GLU CA C 56.1 0.3 1 541 129 129 GLU CB C 29.3 0.3 1 542 129 129 GLU N N 124.1 0.3 1 543 130 130 TYR H H 7.94 0.02 1 544 130 130 TYR C C 175.1 0.3 1 545 130 130 TYR CA C 57.1 0.3 1 546 130 130 TYR CB C 38.3 0.3 1 547 130 130 TYR N N 121.1 0.3 1 548 131 131 ALA H H 8.14 0.02 1 549 131 131 ALA C C 177.1 0.3 1 550 131 131 ALA CA C 51.7 0.3 1 551 131 131 ALA CB C 18.5 0.3 1 552 131 131 ALA N N 125.8 0.3 1 553 132 132 ILE H H 7.99 0.02 1 554 132 132 ILE CA C 60.5 0.3 1 555 132 132 ILE CB C 37.9 0.3 1 556 132 132 ILE N N 120.2 0.3 1 557 133 133 THR H H 7.95 0.02 1 558 133 133 THR C C 175.8 0.3 1 559 133 133 THR CA C 61.0 0.3 1 560 133 133 THR CB C 69.2 0.3 1 561 133 133 THR N N 116.2 0.3 1 562 135 135 GLU H H 8.36 0.02 1 563 135 135 GLU C C 176.3 0.3 1 564 135 135 GLU CA C 56.2 0.3 1 565 135 135 GLU CB C 29.2 0.3 1 566 135 135 GLU N N 121.2 0.3 1 567 136 136 ILE H H 8.02 0.02 1 568 136 136 ILE CA C 60.6 0.3 1 569 136 136 ILE CB C 37.6 0.3 1 570 136 136 ILE N N 122.1 0.3 1 571 137 137 ALA H H 8.18 0.02 1 572 137 137 ALA CA C 52.2 0.3 1 573 137 137 ALA CB C 18.8 0.3 1 574 137 137 ALA N N 125.6 0.3 1 575 138 138 THR H H 7.98 0.02 1 576 138 138 THR CA C 61.1 0.3 1 577 138 138 THR CB C 69.6 0.3 1 578 138 138 THR N N 114.4 0.3 1 579 139 139 ARG H H 8.04 0.02 1 580 139 139 ARG C C 175.8 0.3 1 581 139 139 ARG CA C 55.7 0.3 1 582 139 139 ARG CB C 29.6 0.3 1 583 139 139 ARG N N 120.9 0.3 1 584 140 140 LEU H H 8.32 0.02 1 585 140 140 LEU C C 177.1 0.3 1 586 140 140 LEU CA C 54.9 0.3 1 587 140 140 LEU CB C 41.3 0.3 1 588 140 140 LEU N N 125.0 0.3 1 589 141 141 GLU H H 8.31 0.02 1 590 141 141 GLU C C 176.0 0.3 1 591 141 141 GLU CA C 56.2 0.3 1 592 141 141 GLU CB C 29.4 0.3 1 593 141 141 GLU N N 121.7 0.3 1 594 142 142 TYR H H 8.02 0.02 1 595 142 142 TYR C C 175.4 0.3 1 596 142 142 TYR CA C 57.4 0.3 1 597 142 142 TYR CB C 37.8 0.3 1 598 142 142 TYR N N 122.6 0.3 1 599 143 143 GLN H H 8.11 0.02 1 600 143 143 GLN C C 176.3 0.3 1 601 143 143 GLN CA C 55.0 0.3 1 602 143 143 GLN CB C 28.6 0.3 1 603 143 143 GLN N N 122.2 0.3 1 604 144 144 TRP H H 8.17 0.02 1 605 144 144 TRP C C 172.8 0.3 1 606 144 144 TRP CA C 54.0 0.3 1 607 144 144 TRP CB C 29.5 0.3 1 608 144 144 TRP N N 121.0 0.3 1 609 145 145 THR H H 8.08 0.02 1 610 145 145 THR C C 175.4 0.3 1 611 145 145 THR CA C 62.2 0.3 1 612 145 145 THR CB C 69.3 0.3 1 613 145 145 THR N N 114.2 0.3 1 614 146 146 ASN H H 8.19 0.02 1 615 146 146 ASN C C 177.4 0.3 1 616 146 146 ASN CA C 55.3 0.3 1 617 146 146 ASN CB C 40.5 0.3 1 618 146 146 ASN N N 120.3 0.3 1 619 147 147 ASN H H 8.16 0.02 1 620 147 147 ASN CA C 53.0 0.3 1 621 147 147 ASN CB C 37.4 0.3 1 622 147 147 ASN N N 121.8 0.3 1 623 148 148 ILE H H 7.99 0.02 1 624 148 148 ILE C C 176.7 0.3 1 625 148 148 ILE CA C 61.2 0.3 1 626 148 148 ILE CB C 37.8 0.3 1 627 148 148 ILE N N 121.0 0.3 1 628 149 149 GLY H H 8.28 0.02 1 629 149 149 GLY C C 173.9 0.3 1 630 149 149 GLY CA C 44.9 0.3 1 631 149 149 GLY N N 111.9 0.3 1 632 150 150 ASP H H 8.05 0.02 1 633 150 150 ASP C C 176.3 0.3 1 634 150 150 ASP CA C 53.9 0.3 1 635 150 150 ASP CB C 40.8 0.3 1 636 150 150 ASP N N 121.1 0.3 1 637 151 151 ALA H H 8.18 0.02 1 638 151 151 ALA C C 177.8 0.3 1 639 151 151 ALA CA C 52.3 0.3 1 640 151 151 ALA CB C 18.3 0.3 1 641 151 151 ALA N N 124.2 0.3 1 642 152 152 HIS H H 8.08 0.02 1 643 152 152 HIS CA C 55.3 0.3 1 644 152 152 HIS CB C 31.2 0.3 1 645 152 152 HIS N N 120.0 0.3 1 646 153 153 THR H H 7.93 0.02 1 647 153 153 THR C C 174.5 0.3 1 648 153 153 THR CA C 61.6 0.3 1 649 153 153 THR CB C 69.3 0.3 1 650 153 153 THR N N 113.3 0.3 1 651 154 154 ILE H H 8.08 0.02 1 652 154 154 ILE C C 176.6 0.3 1 653 154 154 ILE CA C 61.1 0.3 1 654 154 154 ILE CB C 37.8 0.3 1 655 154 154 ILE N N 123.4 0.3 1 656 155 155 GLY H H 8.34 0.02 1 657 155 155 GLY C C 174.1 0.3 1 658 155 155 GLY CA C 44.8 0.3 1 659 155 155 GLY N N 112.5 0.3 1 660 156 156 THR H H 7.92 0.02 1 661 156 156 THR C C 174.3 0.3 1 662 156 156 THR CA C 61.4 0.3 1 663 156 156 THR CB C 69.7 0.3 1 664 156 156 THR N N 113.8 0.3 1 665 157 157 ARG H H 8.29 0.02 1 666 157 157 ARG C C 175.2 0.3 1 667 157 157 ARG CA C 53.5 0.3 1 668 157 157 ARG CB C 29.3 0.3 1 669 157 157 ARG N N 124.6 0.3 1 670 159 159 ASP H H 8.30 0.02 1 671 159 159 ASP C C 176.2 0.3 1 672 159 159 ASP CA C 53.8 0.3 1 673 159 159 ASP CB C 40.6 0.3 1 674 159 159 ASP N N 120.4 0.3 1 675 160 160 ASN H H 8.29 0.02 1 676 160 160 ASN CA C 53.0 0.3 1 677 160 160 ASN CB C 38.4 0.3 1 678 160 160 ASN N N 119.5 0.3 1 679 161 161 GLY H H 8.43 0.02 1 680 161 161 GLY C C 174.3 0.3 1 681 161 161 GLY CA C 45.1 0.3 1 682 161 161 GLY N N 109.2 0.3 1 683 162 162 MET H H 8.06 0.02 1 684 162 162 MET C C 176.4 0.3 1 685 162 162 MET CA C 55.5 0.3 1 686 162 162 MET CB C 31.8 0.3 1 687 162 162 MET N N 120.0 0.3 1 688 163 163 LEU H H 8.13 0.02 1 689 163 163 LEU C C 177.4 0.3 1 690 163 163 LEU CA C 55.1 0.3 1 691 163 163 LEU CB C 41.1 0.3 1 692 163 163 LEU N N 122.6 0.3 1 693 164 164 SER H H 8.11 0.02 1 694 164 164 SER C C 176.4 0.3 1 695 164 164 SER CA C 57.8 0.3 1 696 164 164 SER CB C 63.0 0.3 1 697 164 164 SER N N 116.3 0.3 1 698 165 165 LEU H H 8.06 0.02 1 699 165 165 LEU CA C 55.2 0.3 1 700 165 165 LEU CB C 41.0 0.3 1 701 165 165 LEU N N 121.4 0.3 1 702 166 166 GLY H H 8.24 0.02 1 703 166 166 GLY C C 174.0 0.3 1 704 166 166 GLY CA C 45.0 0.3 1 705 166 166 GLY N N 109.5 0.3 1 706 167 167 VAL H H 7.81 0.02 1 707 167 167 VAL C C 176.0 0.3 1 708 167 167 VAL CA C 61.5 0.3 1 709 167 167 VAL CB C 31.5 0.3 1 710 167 167 VAL N N 118.8 0.3 1 711 168 168 SER H H 8.27 0.02 1 712 168 168 SER C C 173.1 0.3 1 713 168 168 SER CA C 55.7 0.3 1 714 168 168 SER CB C 63.1 0.3 1 715 168 168 SER N N 120.7 0.3 1 716 169 169 TYR H H 7.80 0.02 1 717 169 169 TYR C C 174.2 0.3 1 718 169 169 TYR CA C 55.2 0.3 1 719 169 169 TYR CB C 37.6 0.3 1 720 169 169 TYR N N 120.9 0.3 1 721 170 170 ARG H H 8.21 0.02 1 722 170 170 ARG C C 175.9 0.3 1 723 170 170 ARG CA C 55.2 0.3 1 724 170 170 ARG CB C 30.8 0.3 1 725 170 170 ARG N N 122.4 0.3 1 726 171 171 PHE H H 7.89 0.02 1 727 171 171 PHE C C 175.7 0.3 1 728 171 171 PHE CA C 57.6 0.3 1 729 171 171 PHE CB C 37.6 0.3 1 730 171 171 PHE N N 118.7 0.3 1 731 172 172 GLY H H 8.34 0.02 1 732 172 172 GLY C C 173.8 0.3 1 733 172 172 GLY CA C 45.0 0.3 1 734 172 172 GLY N N 111.0 0.3 1 735 173 173 GLN H H 8.17 0.02 1 736 173 173 GLN C C 176.5 0.3 1 737 173 173 GLN CA C 55.5 0.3 1 738 173 173 GLN CB C 28.5 0.3 1 739 173 173 GLN N N 120.3 0.3 1 740 174 174 GLY H H 8.38 0.02 1 741 174 174 GLY C C 173.9 0.3 1 742 174 174 GLY CA C 44.7 0.3 1 743 174 174 GLY N N 110.5 0.3 1 744 175 175 GLU H H 8.20 0.02 1 745 175 175 GLU C C 176.1 0.3 1 746 175 175 GLU CA C 55.9 0.3 1 747 175 175 GLU CB C 29.4 0.3 1 748 175 175 GLU N N 121.1 0.3 1 749 176 176 ALA H H 8.22 0.02 1 750 176 176 ALA C C 176.2 0.3 1 751 176 176 ALA CA C 51.8 0.3 1 752 176 176 ALA CB C 18.2 0.3 1 753 176 176 ALA N N 125.7 0.3 1 754 177 177 ALA H H 7.77 0.02 1 755 177 177 ALA C C 172.5 0.3 1 756 177 177 ALA CA C 53.3 0.3 1 757 177 177 ALA CB C 19.2 0.3 1 758 177 177 ALA N N 129.6 0.3 1 stop_ save_