data_15966 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Solution NMR structure of integral membrane protein DsbB ; _BMRB_accession_number 15966 _BMRB_flat_file_name bmr15966.str _Entry_type original _Submission_date 2008-09-25 _Accession_date 2008-09-25 _Entry_origination author _NMR_STAR_version 2.1.1 _Experimental_method NMR _Details . loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Zhou Yunpeng . . 2 Cierpicki Tomasz . . 3 'Flores Jimenez' Ricardo H. . 4 Lukasik Stephen M. . 5 Ellena Jeffrey F. . 6 Cafiso David S. . 7 Kadukura Hiroshi . . 8 Beckwith Jon . . 9 Bushweller John H. . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 170 "13C chemical shifts" 499 "15N chemical shifts" 170 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2010-06-02 update BMRB 'edit assembly name' 2008-12-12 original author 'original release' stop_ save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title 'NMR solution structure of the integral membrane enzyme DsbB: functional insights into DsbB-catalyzed disulfide bond formation.' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 18922471 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Zhou Yunpeng . . 2 Cierpicki Tomasz . . 3 'Flores Jimenez' Ricardo H. . 4 Lukasik Stephen M. . 5 Ellena Jeffrey F. . 6 Cafiso David S. . 7 Kadukura Hiroshi . . 8 Beckwith Jon . . 9 Bushweller John H. . stop_ _Journal_abbreviation 'Mol. Cell' _Journal_volume 31 _Journal_issue 6 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 896 _Page_last 908 _Year 2008 _Details . save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name DsbB _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label DsbB $Disulfide_bond_formation_protein_B stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state ? _System_paramagnetic no _System_thiol_state . _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_Disulfide_bond_formation_protein_B _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common Disulfide_bond_formation_protein_B _Molecular_mass 20948.965 _Mol_thiol_state 'all disulfide bound' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 183 _Mol_residue_sequence ; MLRFLNQASQGRGAWLLMAF TALALELTALWFQHVMLLKP CVLSIYERAALFGVLGAALI GAIAPKTPLRYVAMVIWLYS AFRGVQLTYEHTMLQLYPSP FATSDFMVRFPEWLPLDKWV PQVFVASGDCAERQWDFLGL EMPQWLLGIFIAYLIVAVLV VISQPFKAKKRDLFGRGHHH HHH ; loop_ _Residue_seq_code _Residue_label 1 MET 2 LEU 3 ARG 4 PHE 5 LEU 6 ASN 7 GLN 8 ALA 9 SER 10 GLN 11 GLY 12 ARG 13 GLY 14 ALA 15 TRP 16 LEU 17 LEU 18 MET 19 ALA 20 PHE 21 THR 22 ALA 23 LEU 24 ALA 25 LEU 26 GLU 27 LEU 28 THR 29 ALA 30 LEU 31 TRP 32 PHE 33 GLN 34 HIS 35 VAL 36 MET 37 LEU 38 LEU 39 LYS 40 PRO 41 CYS 42 VAL 43 LEU 44 SER 45 ILE 46 TYR 47 GLU 48 ARG 49 ALA 50 ALA 51 LEU 52 PHE 53 GLY 54 VAL 55 LEU 56 GLY 57 ALA 58 ALA 59 LEU 60 ILE 61 GLY 62 ALA 63 ILE 64 ALA 65 PRO 66 LYS 67 THR 68 PRO 69 LEU 70 ARG 71 TYR 72 VAL 73 ALA 74 MET 75 VAL 76 ILE 77 TRP 78 LEU 79 TYR 80 SER 81 ALA 82 PHE 83 ARG 84 GLY 85 VAL 86 GLN 87 LEU 88 THR 89 TYR 90 GLU 91 HIS 92 THR 93 MET 94 LEU 95 GLN 96 LEU 97 TYR 98 PRO 99 SER 100 PRO 101 PHE 102 ALA 103 THR 104 SER 105 ASP 106 PHE 107 MET 108 VAL 109 ARG 110 PHE 111 PRO 112 GLU 113 TRP 114 LEU 115 PRO 116 LEU 117 ASP 118 LYS 119 TRP 120 VAL 121 PRO 122 GLN 123 VAL 124 PHE 125 VAL 126 ALA 127 SER 128 GLY 129 ASP 130 CYS 131 ALA 132 GLU 133 ARG 134 GLN 135 TRP 136 ASP 137 PHE 138 LEU 139 GLY 140 LEU 141 GLU 142 MET 143 PRO 144 GLN 145 TRP 146 LEU 147 LEU 148 GLY 149 ILE 150 PHE 151 ILE 152 ALA 153 TYR 154 LEU 155 ILE 156 VAL 157 ALA 158 VAL 159 LEU 160 VAL 161 VAL 162 ILE 163 SER 164 GLN 165 PRO 166 PHE 167 LYS 168 ALA 169 LYS 170 LYS 171 ARG 172 ASP 173 LEU 174 PHE 175 GLY 176 ARG 177 GLY 178 HIS 179 HIS 180 HIS 181 HIS 182 HIS 183 HIS stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-07-08 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 18395 DsbB 96.17 176 98.30 98.30 5.16e-120 BMRB 18493 DsbB 96.17 176 97.73 97.73 1.31e-118 PDB 2HI7 "Crystal Structure Of Dsba-Dsbb-Ubiquinone Complex" 96.17 176 97.73 97.73 1.31e-118 PDB 2K73 "Solution Nmr Structure Of Integral Membrane Protein Dsbb" 100.00 183 100.00 100.00 4.67e-129 PDB 2K74 "Solution Nmr Structure Of Dsbb-Ubiquinone Complex" 100.00 183 100.00 100.00 4.67e-129 PDB 2LEG "Membrane Protein Complex Dsbb-Dsba Structure By Joint Calculations With Solid-State Nmr And X-Ray Experimental Data" 96.17 176 97.73 97.73 1.31e-118 PDB 2LTQ "High Resolution Structure Of Dsbb C41s By Joint Calculation With Solid-state Nmr And X-ray Data" 96.17 176 97.73 97.73 1.31e-118 PDB 2ZUP "Updated Crystal Structure Of Dsbb-Dsba Complex From E. Coli" 96.17 176 97.73 97.73 1.31e-118 PDB 2ZUQ "Crystal Structure Of Dsbb-Fab Complex" 96.17 176 97.73 97.73 1.31e-118 PDB 3E9J "Structure Of The Charge-Transfer Intermediate Of The Transmembrane Redox Catalyst Dsbb" 99.45 182 97.80 97.80 1.76e-124 DBJ BAA36032 "oxidoreductase that catalyzes reoxidation of DsbA protein disulfide isomerase I [Escherichia coli str. K12 substr. W3110]" 96.17 176 97.73 97.73 1.72e-119 DBJ BAB35103 "protein-disulfide oxidoreductase [Escherichia coli O157:H7 str. Sakai]" 96.17 176 97.73 97.73 1.72e-119 DBJ BAI24997 "oxidoreductase DsbB [Escherichia coli O26:H11 str. 11368]" 96.17 176 97.16 97.73 3.10e-119 DBJ BAI30121 "oxidoreductase DsbB [Escherichia coli O103:H2 str. 12009]" 96.17 176 97.73 97.73 1.72e-119 DBJ BAI35441 "oxidoreductase DsbB [Escherichia coli O111:H- str. 11128]" 96.17 176 97.16 97.73 3.10e-119 EMBL CAQ31687 "DsbB[reduced] [Escherichia coli BL21(DE3)]" 96.17 176 97.73 97.73 1.72e-119 EMBL CAQ98064 "oxidoreductase that catalyzes reoxidation of DsbA protein disulfide isomerase I [Escherichia coli IAI1]" 96.17 176 97.73 97.73 1.72e-119 EMBL CAR12682 "oxidoreductase that catalyzes reoxidation of DsbA protein disulfide isomerase I [Escherichia coli UMN026]" 96.17 176 97.73 97.73 1.72e-119 EMBL CAR18016 "oxidoreductase that catalyzes reoxidation of DsbA protein disulfide isomerase I [Escherichia coli IAI39]" 96.17 176 97.16 97.16 5.53e-119 EMBL CAU97139 "oxidoreductase that catalyzes reoxidation of DsbA protein disulfide isomerase I [Escherichia coli 55989]" 96.17 176 97.73 97.73 1.72e-119 GB AAA23711 "oxido-reductase [Escherichia coli]" 96.17 178 97.73 97.73 8.47e-120 GB AAB25233 "DsbB=disulfide bond formation protein [Escherichia coli, Peptide, 176 aa]" 96.17 176 97.73 97.73 1.72e-119 GB AAC74269 "oxidoreductase that catalyzes reoxidation of DsbA protein disulfide isomerase I [Escherichia coli str. K-12 substr. MG1655]" 96.17 176 97.73 97.73 1.72e-119 GB AAG56036 "reoxidizes DsbA protein following formation of disulfide bond in P-ring of flagella [Escherichia coli O157:H7 str. EDL933]" 96.17 176 97.16 97.16 8.94e-119 GB AAN42789 "disulfide bond formation protein dsbB [Shigella flexneri 2a str. 301]" 96.17 176 97.16 97.73 3.10e-119 PIR H85696 "hypothetical protein dsbB [imported] - Escherichia coli (strain O157:H7, substrain EDL933)" 96.17 176 97.16 97.16 8.94e-119 REF NP_309707 "disulfide bond formation protein B [Escherichia coli O157:H7 str. Sakai]" 96.17 176 97.73 97.73 1.72e-119 REF NP_415703 "oxidoreductase that catalyzes reoxidation of DsbA protein disulfide isomerase I [Escherichia coli str. K-12 substr. MG1655]" 96.17 176 97.73 97.73 1.72e-119 REF NP_707082 "disulfide bond formation protein B [Shigella flexneri 2a str. 301]" 96.17 176 97.16 97.73 3.10e-119 REF WP_000652474 "disulfide bond formation protein B, partial [Escherichia coli]" 66.67 122 99.18 99.18 1.30e-80 REF WP_000943442 "disulfide bond formation protein B [Escherichia coli]" 96.17 176 97.16 97.73 4.64e-119 SP P0A6M2 "RecName: Full=Disulfide bond formation protein B; AltName: Full=Disulfide oxidoreductase" 96.17 176 97.73 97.73 1.72e-119 SP P0A6M3 "RecName: Full=Disulfide bond formation protein B; AltName: Full=Disulfide oxidoreductase" 96.17 176 97.73 97.73 1.72e-119 SP Q0T5L6 "RecName: Full=Disulfide bond formation protein B; AltName: Full=Disulfide oxidoreductase" 96.17 176 97.16 97.73 3.10e-119 SP Q31ZM6 "RecName: Full=Disulfide bond formation protein B; AltName: Full=Disulfide oxidoreductase" 96.17 176 97.16 97.73 4.64e-119 SP Q32H31 "RecName: Full=Disulfide bond formation protein B; AltName: Full=Disulfide oxidoreductase" 96.17 176 97.73 97.73 1.72e-119 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species _Gene_mnemonic $Disulfide_bond_formation_protein_B 'E. coli' 562 Bacteria . Escherichia coli dsbB 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 $Disulfide_bond_formation_protein_B 'recombinant technology' . Escherichia coli Rosetta(DE3) pET22b stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Saveframe_category sample _Sample_type 'DPC micelle' _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $Disulfide_bond_formation_protein_B 1.2 mM '[U-13C; U-15N; U-2H]' DPC 100 mM [U-2H] 'sodium phosphate' 25 mM 'natural abundance' 'potassium chloride' 50 mM 'natural abundance' stop_ save_ save_sample_2 _Saveframe_category sample _Sample_type 'DPC micelle' _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $Disulfide_bond_formation_protein_B 1.5 mM 'I,L,V methyl protonated, [U-13C; U-15N; U-2H]' DPC 100 mM [U-2H] 'sodium phosphate' 25 mM 'natural abundance' 'potassium chloride' 50 mM 'natural abundance' stop_ save_ save_sample_3 _Saveframe_category sample _Sample_type 'DPC micelle' _Details 'single Cys mutants to incorporate MTSL/dMTSL for PRE measurements' loop_ _Mol_label _Concentration_value _Concentration_value_units _Concentration_min_value _Concentration_max_value _Isotopic_labeling $Disulfide_bond_formation_protein_B . mM 0.5 1.0 '[U-15N; U-2H]' DPC 100 mM . . 'natural abundance' 'sodium phosphate' 25 mM . . 'natural abundance' 'potassium chloride' 50 mM . . 'natural abundance' stop_ save_ ############################ # Computer software used # ############################ save_VNMR _Saveframe_category software _Name VNMR _Version . loop_ _Vendor _Address _Electronic_address Varian . . stop_ loop_ _Task collection stop_ _Details . save_ save_X-PLOR_NIH _Saveframe_category software _Name 'X-PLOR NIH' _Version . loop_ _Vendor _Address _Electronic_address 'Schwieters, Kuszewski, Tjandra and Clore' . . stop_ loop_ _Task 'structure calculation' 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' stop_ _Details . save_ save_Molmol _Saveframe_category software _Name Molmol _Version . loop_ _Vendor _Address _Electronic_address 'Koradi, Billeter and Wuthrich' . . stop_ loop_ _Task 'data analysis' stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model INOVA _Field_strength 600 _Details . save_ ############################# # NMR applied experiments # ############################# save_3D_HNCO_1 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCO' _Sample_label $sample_1 save_ save_3D_HN(CA)CO_2 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HN(CA)CO' _Sample_label $sample_1 save_ save_3D_HNCA_3 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCA' _Sample_label $sample_1 save_ save_3D_HN(CO)CA_4 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HN(CO)CA' _Sample_label $sample_1 save_ save_3D_HNCACB_5 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCACB' _Sample_label $sample_1 save_ save_2D_1H-15N_HSQC_6 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-15N HSQC' _Sample_label $sample_1 save_ save_3D_HNCO_based_RDC_experiments_7 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCO based RDC experiments' _Sample_label $sample_1 save_ save_3D_1H-15N_NOESY_8 _Saveframe_category NMR_applied_experiment _Experiment_name '3D 1H-15N NOESY' _Sample_label $sample_2 save_ save_3D_1H-13C_NOESY_9 _Saveframe_category NMR_applied_experiment _Experiment_name '3D 1H-13C NOESY' _Sample_label $sample_2 save_ save_2D_1H-13C_HSQC_10 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-13C HSQC' _Sample_label $sample_2 save_ save_3D_13C-13C_NOESY_11 _Saveframe_category NMR_applied_experiment _Experiment_name '3D 13C-13C NOESY' _Sample_label $sample_2 save_ save_3D_HMCM[CG]CBCA_12 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HMCM[CG]CBCA' _Sample_label $sample_2 save_ save_2D_1H-15N_HSQC_13 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-15N HSQC' _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 'ionic strength' 0.1 . M pH 6.2 . pH pressure 1 . atm temperature 313 . 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 external indirect cylindrical 'separate tube (no insert) similar to the experimental sample tube' parallel 0.25144953 DSS H 1 'methyl protons' ppm 0 external direct cylindrical 'separate tube (no insert) similar to the experimental sample tube' parallel 1 DSS N 15 'methyl protons' ppm 0 external indirect cylindrical 'separate tube (no insert) similar to the experimental sample tube' parallel 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 '3D HNCO' '3D HN(CA)CO' '3D HNCA' '3D HN(CO)CA' '3D HNCACB' '2D 1H-15N HSQC' 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 DsbB _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 9.347 . 1 2 1 1 MET C C 177.405 . . 3 1 1 MET CA C 57.998 . 1 4 1 1 MET CB C 32.522 . 1 5 1 1 MET N N 131.202 . 1 6 2 2 LEU H H 8.742 . 1 7 2 2 LEU C C 179.420 . . 8 2 2 LEU CA C 57.698 . 1 9 2 2 LEU CB C 39.091 . 1 10 2 2 LEU N N 118.666 . 1 11 3 3 ARG H H 8.155 . 1 12 3 3 ARG C C 178.934 . . 13 3 3 ARG CA C 59.137 . 1 14 3 3 ARG CB C 28.508 . 1 15 3 3 ARG N N 121.295 . 1 16 4 4 PHE H H 7.963 . 1 17 4 4 PHE C C 177.721 . . 18 4 4 PHE CA C 60.975 . 1 19 4 4 PHE CB C 38.517 . 1 20 4 4 PHE N N 120.003 . 1 21 5 5 LEU H H 8.347 . 1 22 5 5 LEU C C 178.725 . . 23 5 5 LEU CA C 57.291 . 1 24 5 5 LEU CB C 40.732 . 1 25 5 5 LEU N N 120.413 . 1 26 6 6 ASN H H 8.374 . 1 27 6 6 ASN C C 179.602 . . 28 6 6 ASN CA C 57.310 . 1 29 6 6 ASN CB C 38.819 . 1 30 6 6 ASN N N 120.086 . 1 31 7 7 GLN H H 7.995 . 1 32 7 7 GLN C C 179.644 . . 33 7 7 GLN CA C 58.783 . 1 34 7 7 GLN CB C 27.716 . 1 35 7 7 GLN N N 120.249 . 1 36 8 8 ALA H H 8.708 . 1 37 8 8 ALA C C 180.078 . . 38 8 8 ALA CA C 54.174 . 1 39 8 8 ALA CB C 16.450 . 1 40 8 8 ALA N N 123.599 . 1 41 9 9 SER H H 8.102 . 1 42 9 9 SER C C 173.712 . . 43 9 9 SER CA C 60.367 . 1 44 9 9 SER CB C 63.168 . 1 45 9 9 SER N N 111.152 . 1 46 10 10 GLN H H 7.148 . 1 47 10 10 GLN C C 174.553 . . 48 10 10 GLN CA C 55.666 . 1 49 10 10 GLN CB C 29.189 . 1 50 10 10 GLN N N 119.388 . 1 51 11 11 GLY H H 7.699 . 1 52 11 11 GLY C C 172.277 . . 53 11 11 GLY CA C 43.522 . 1 54 11 11 GLY N N 108.553 . 1 55 12 12 ARG H H 8.659 . 1 56 12 12 ARG C C 178.556 . . 57 12 12 ARG CA C 59.956 . 1 58 12 12 ARG CB C 30.383 . 1 59 12 12 ARG N N 116.389 . 1 60 13 13 GLY H H 9.047 . 1 61 13 13 GLY C C 175.133 . . 62 13 13 GLY CA C 48.198 . 1 63 13 13 GLY N N 108.068 . 1 64 14 14 ALA H H 9.396 . 1 65 14 14 ALA C C 178.518 . . 66 14 14 ALA CA C 55.398 . 1 67 14 14 ALA CB C 16.947 . 1 68 14 14 ALA N N 123.163 . 1 69 15 15 TRP H H 6.450 . 1 70 15 15 TRP HE1 H 10.560 . 1 71 15 15 TRP C C 178.863 . . 72 15 15 TRP CA C 59.162 . 1 73 15 15 TRP CB C 28.570 . 1 74 15 15 TRP N N 116.771 . 1 75 15 15 TRP NE1 N 130.426 . 1 76 16 16 LEU H H 8.281 . 1 77 16 16 LEU C C 178.869 . . 78 16 16 LEU CA C 57.299 . 1 79 16 16 LEU CB C 40.511 . 1 80 16 16 LEU N N 118.728 . 1 81 17 17 LEU H H 8.538 . 1 82 17 17 LEU C C 178.876 . . 83 17 17 LEU CA C 57.667 . 1 84 17 17 LEU CB C 40.316 . 1 85 17 17 LEU N N 121.020 . 1 86 18 18 MET H H 8.235 . 1 87 18 18 MET C C 180.144 . . 88 18 18 MET CA C 60.059 . 1 89 18 18 MET CB C 31.468 . 1 90 18 18 MET N N 120.407 . 1 91 19 19 ALA H H 8.725 . 1 92 19 19 ALA C C 178.226 . . 93 19 19 ALA CA C 55.321 . 1 94 19 19 ALA CB C 16.931 . 1 95 19 19 ALA N N 124.297 . 1 96 20 20 PHE H H 8.516 . 1 97 20 20 PHE C C 177.106 . . 98 20 20 PHE CA C 61.560 . 1 99 20 20 PHE CB C 37.905 . 1 100 20 20 PHE N N 117.881 . 1 101 21 21 THR H H 8.225 . 1 102 21 21 THR C C 174.385 . . 103 21 21 THR CA C 65.672 . 1 104 21 21 THR CB C 68.535 . 1 105 21 21 THR N N 109.821 . 1 106 22 22 ALA H H 7.237 . 1 107 22 22 ALA C C 179.551 . . 108 22 22 ALA CA C 54.646 . 1 109 22 22 ALA CB C 16.991 . 1 110 22 22 ALA N N 124.170 . 1 111 23 23 LEU H H 8.414 . 1 112 23 23 LEU C C 178.052 . . 113 23 23 LEU CA C 57.651 . 1 114 23 23 LEU CB C 40.867 . 1 115 23 23 LEU N N 119.432 . 1 116 24 24 ALA H H 8.589 . 1 117 24 24 ALA C C 180.721 . . 118 24 24 ALA CA C 54.964 . 1 119 24 24 ALA CB C 16.311 . 1 120 24 24 ALA N N 120.552 . 1 121 25 25 LEU H H 7.628 . 1 122 25 25 LEU C C 178.811 . . 123 25 25 LEU CA C 57.932 . 1 124 25 25 LEU CB C 42.463 . 1 125 25 25 LEU N N 119.985 . 1 126 26 26 GLU H H 7.900 . 1 127 26 26 GLU C C 179.558 . . 128 26 26 GLU CA C 58.085 . 1 129 26 26 GLU CB C 26.206 . 1 130 26 26 GLU N N 118.529 . 1 131 27 27 LEU H H 8.470 . 1 132 27 27 LEU C C 178.412 . . 133 27 27 LEU CA C 57.606 . 1 134 27 27 LEU CB C 40.231 . 1 135 27 27 LEU N N 118.029 . 1 136 28 28 THR H H 7.934 . 1 137 28 28 THR C C 176.088 . . 138 28 28 THR CB C 67.595 . 1 139 28 28 THR N N 118.447 . 1 140 29 29 ALA H H 7.711 . 1 141 29 29 ALA C C 179.509 . . 142 29 29 ALA CA C 55.625 . 1 143 29 29 ALA CB C 16.291 . 1 144 29 29 ALA N N 123.275 . 1 145 30 30 LEU H H 7.586 . 1 146 30 30 LEU C C 178.762 . . 147 30 30 LEU CA C 57.170 . 1 148 30 30 LEU CB C 40.645 . 1 149 30 30 LEU N N 116.357 . 1 150 31 31 TRP H H 8.722 . 1 151 31 31 TRP HE1 H 10.286 . 1 152 31 31 TRP C C 179.130 . . 153 31 31 TRP CA C 61.864 . 1 154 31 31 TRP CB C 27.761 . 1 155 31 31 TRP N N 125.512 . 1 156 31 31 TRP NE1 N 130.244 . 1 157 32 32 PHE H H 8.614 . 1 158 32 32 PHE C C 177.155 . . 159 32 32 PHE CA C 61.007 . 1 160 32 32 PHE CB C 37.711 . 1 161 32 32 PHE N N 119.130 . 1 162 33 33 GLN H H 7.573 . 1 163 33 33 GLN C C 177.157 . . 164 33 33 GLN CA C 56.574 . 1 165 33 33 GLN CB C 29.413 . 1 166 33 33 GLN N N 117.222 . 1 167 34 34 HIS H H 8.825 . 1 168 34 34 HIS C C 175.555 . . 169 34 34 HIS CA C 58.449 . 1 170 34 34 HIS CB C 31.535 . 1 171 34 34 HIS N N 116.257 . 1 172 35 35 VAL H H 8.052 . 1 173 35 35 VAL C C 176.637 . . 174 35 35 VAL CA C 63.913 . 1 175 35 35 VAL CB C 29.681 . 1 176 35 35 VAL N N 117.626 . 1 177 36 36 MET H H 6.522 . 1 178 36 36 MET C C 175.210 . . 179 36 36 MET CA C 55.105 . 1 180 36 36 MET CB C 31.257 . 1 181 36 36 MET N N 114.512 . 1 182 37 37 LEU H H 6.415 . 1 183 37 37 LEU C C 176.927 . . 184 37 37 LEU CA C 55.560 . 1 185 37 37 LEU CB C 36.245 . 1 186 37 37 LEU N N 111.792 . 1 187 38 38 LEU H H 8.147 . 1 188 38 38 LEU C C 176.760 . . 189 38 38 LEU CA C 54.005 . 1 190 38 38 LEU CB C 40.407 . 1 191 38 38 LEU N N 119.145 . 1 192 39 39 LYS H H 8.851 . 1 193 39 39 LYS C C 175.322 . . 194 39 39 LYS CA C 53.945 . 1 195 39 39 LYS CB C 32.466 . 1 196 39 39 LYS N N 121.573 . 1 197 40 40 PRO C C 173.496 . . 198 40 40 PRO CA C 60.356 . 1 199 40 40 PRO CB C 29.145 . 1 200 41 41 CYS H H 8.346 . 1 201 41 41 CYS C C 174.256 . . 202 41 41 CYS CA C 56.180 . 1 203 41 41 CYS CB C 50.684 . 1 204 41 41 CYS N N 123.838 . 1 205 42 42 VAL H H 8.607 . 1 206 42 42 VAL C C 175.918 . . 207 42 42 VAL CA C 66.779 . 1 208 42 42 VAL CB C 30.522 . 1 209 42 42 VAL N N 119.305 . 1 210 43 43 LEU H H 6.177 . 1 211 43 43 LEU C C 178.121 . . 212 43 43 LEU CA C 58.176 . 1 213 43 43 LEU CB C 39.072 . 1 214 43 43 LEU N N 114.614 . 1 215 44 44 SER H H 6.736 . 1 216 44 44 SER C C 176.171 . . 217 44 44 SER CA C 60.790 . 1 218 44 44 SER CB C 61.787 . 1 219 44 44 SER N N 117.941 . 1 220 45 45 ILE H H 7.604 . 1 221 45 45 ILE C C 179.191 . . 222 45 45 ILE CA C 61.948 . 1 223 45 45 ILE CB C 32.764 . 1 224 45 45 ILE N N 121.404 . 1 225 46 46 TYR H H 7.872 . 1 226 46 46 TYR C C 178.831 . . 227 46 46 TYR CA C 58.937 . 1 228 46 46 TYR CB C 36.550 . 1 229 46 46 TYR N N 120.789 . 1 230 47 47 GLU H H 9.121 . 1 231 47 47 GLU C C 179.558 . . 232 47 47 GLU CA C 59.369 . 1 233 47 47 GLU CB C 26.740 . 1 234 47 47 GLU N N 121.627 . 1 235 48 48 ARG H H 8.410 . 1 236 48 48 ARG C C 181.217 . . 237 48 48 ARG CA C 59.649 . 1 238 48 48 ARG CB C 29.213 . 1 239 48 48 ARG N N 118.830 . 1 240 49 49 ALA H H 8.542 . 1 241 49 49 ALA C C 177.629 . . 242 49 49 ALA CA C 55.934 . 1 243 49 49 ALA CB C 16.267 . 1 244 49 49 ALA N N 123.800 . 1 245 50 50 ALA H H 8.796 . 1 246 50 50 ALA C C 179.948 . . 247 50 50 ALA CA C 55.508 . 1 248 50 50 ALA CB C 16.063 . 1 249 50 50 ALA N N 122.131 . 1 250 51 51 LEU H H 8.399 . 1 251 51 51 LEU C C 178.125 . . 252 51 51 LEU CA C 57.017 . 1 253 51 51 LEU CB C 40.998 . 1 254 51 51 LEU N N 118.238 . 1 255 52 52 PHE H H 8.079 . 1 256 52 52 PHE C C 178.555 . . 257 52 52 PHE CA C 61.700 . 1 258 52 52 PHE CB C 37.879 . 1 259 52 52 PHE N N 122.429 . 1 260 53 53 GLY H H 8.188 . 1 261 53 53 GLY C C 175.291 . . 262 53 53 GLY CA C 47.488 . 1 263 53 53 GLY N N 110.335 . 1 264 54 54 VAL H H 7.276 . 1 265 54 54 VAL C C 176.962 . . 266 54 54 VAL CA C 66.997 . 1 267 54 54 VAL CB C 30.108 . 1 268 54 54 VAL N N 121.839 . 1 269 55 55 LEU H H 7.915 . 1 270 55 55 LEU C C 178.207 . . 271 55 55 LEU CA C 58.710 . 1 272 55 55 LEU CB C 40.984 . 1 273 55 55 LEU N N 120.192 . 1 274 56 56 GLY H H 9.206 . 1 275 56 56 GLY C C 174.502 . . 276 56 56 GLY CA C 47.002 . 1 277 56 56 GLY N N 106.235 . 1 278 57 57 ALA H H 8.520 . 1 279 57 57 ALA C C 178.697 . . 280 57 57 ALA CA C 55.176 . 1 281 57 57 ALA CB C 17.376 . 1 282 57 57 ALA N N 123.124 . 1 283 58 58 ALA H H 8.013 . 1 284 58 58 ALA C C 179.124 . . 285 58 58 ALA CA C 54.449 . 1 286 58 58 ALA CB C 17.319 . 1 287 58 58 ALA N N 119.093 . 1 288 59 59 LEU H H 7.855 . 1 289 59 59 LEU C C 177.966 . . 290 59 59 LEU CA C 57.295 . 1 291 59 59 LEU CB C 40.230 . 1 292 59 59 LEU N N 115.699 . 1 293 60 60 ILE H H 7.978 . 1 294 60 60 ILE C C 179.391 . . 295 60 60 ILE CA C 64.206 . 1 296 60 60 ILE CB C 36.389 . 1 297 60 60 ILE N N 116.616 . 1 298 61 61 GLY H H 8.258 . 1 299 61 61 GLY C C 173.564 . . 300 61 61 GLY CA C 45.367 . 1 301 61 61 GLY N N 109.247 . 1 302 62 62 ALA H H 7.338 . 1 303 62 62 ALA C C 177.489 . . 304 62 62 ALA CA C 53.032 . 1 305 62 62 ALA CB C 18.268 . 1 306 62 62 ALA N N 118.569 . 1 307 63 63 ILE H H 7.137 . 1 308 63 63 ILE C C 176.654 . . 309 63 63 ILE CA C 65.924 . 1 310 63 63 ILE CB C 37.031 . 1 311 63 63 ILE N N 117.587 . 1 312 64 64 ALA H H 8.204 . 1 313 64 64 ALA CA C 50.926 . 1 314 64 64 ALA CB C 18.174 . 1 315 64 64 ALA N N 118.914 . 1 316 65 65 PRO C C 176.392 . . 317 65 65 PRO CA C 65.341 . 1 318 65 65 PRO CB C 30.080 . 1 319 66 66 LYS H H 8.360 . 1 320 66 66 LYS C C 177.036 . . 321 66 66 LYS CA C 57.161 . 1 322 66 66 LYS CB C 31.257 . 1 323 66 66 LYS N N 118.143 . 1 324 67 67 THR H H 8.106 . 1 325 67 67 THR C C 174.010 . . 326 67 67 THR CA C 60.181 . 1 327 67 67 THR CB C 69.743 . 1 328 67 67 THR N N 112.375 . 1 329 68 68 PRO C C 176.719 . . 330 68 68 PRO CA C 63.215 . 1 331 68 68 PRO CB C 31.602 . 1 332 69 69 LEU H H 8.066 . 1 333 69 69 LEU C C 179.115 . . 334 69 69 LEU CA C 57.202 . 1 335 69 69 LEU CB C 40.020 . 1 336 69 69 LEU N N 121.266 . 1 337 70 70 ARG H H 7.481 . 1 338 70 70 ARG C C 177.316 . . 339 70 70 ARG CA C 58.547 . 1 340 70 70 ARG CB C 27.609 . 1 341 70 70 ARG N N 114.705 . 1 342 71 71 TYR H H 7.502 . 1 343 71 71 TYR C C 178.651 . . 344 71 71 TYR CA C 58.589 . 1 345 71 71 TYR CB C 36.797 . 1 346 71 71 TYR N N 121.634 . 1 347 72 72 VAL H H 7.048 . 1 348 72 72 VAL C C 177.688 . . 349 72 72 VAL CA C 65.787 . 1 350 72 72 VAL CB C 30.505 . 1 351 72 72 VAL N N 118.946 . 1 352 73 73 ALA H H 7.282 . 1 353 73 73 ALA C C 179.780 . . 354 73 73 ALA CA C 55.416 . 1 355 73 73 ALA CB C 18.524 . 1 356 73 73 ALA N N 120.504 . 1 357 74 74 MET H H 7.973 . 1 358 74 74 MET C C 177.288 . . 359 74 74 MET CA C 60.534 . 1 360 74 74 MET CB C 32.554 . 1 361 74 74 MET N N 115.728 . 1 362 75 75 VAL H H 7.797 . 1 363 75 75 VAL C C 176.962 . . 364 75 75 VAL CA C 66.853 . 1 365 75 75 VAL CB C 30.549 . 1 366 75 75 VAL N N 118.522 . 1 367 76 76 ILE H H 7.851 . 1 368 76 76 ILE C C 178.711 . . 369 76 76 ILE CA C 65.349 . 1 370 76 76 ILE CB C 37.290 . 1 371 76 76 ILE N N 119.180 . 1 372 77 77 TRP H H 8.795 . 1 373 77 77 TRP HE1 H 9.157 . 1 374 77 77 TRP C C 177.189 . . 375 77 77 TRP CA C 58.458 . 1 376 77 77 TRP CB C 29.883 . 1 377 77 77 TRP N N 125.458 . 1 378 77 77 TRP NE1 N 124.408 . 1 379 78 78 LEU H H 8.471 . 1 380 78 78 LEU C C 177.916 . . 381 78 78 LEU CA C 58.533 . 1 382 78 78 LEU CB C 42.207 . 1 383 78 78 LEU N N 119.620 . 1 384 79 79 TYR H H 8.302 . 1 385 79 79 TYR C C 177.124 . . 386 79 79 TYR CA C 62.521 . 1 387 79 79 TYR CB C 38.930 . 1 388 79 79 TYR N N 117.135 . 1 389 80 80 SER H H 8.637 . 1 390 80 80 SER C C 176.104 . . 391 80 80 SER CA C 63.318 . 1 392 80 80 SER CB C 62.579 . 1 393 80 80 SER N N 114.893 . 1 394 81 81 ALA H H 8.702 . 1 395 81 81 ALA C C 178.459 . . 396 81 81 ALA CA C 54.788 . 1 397 81 81 ALA CB C 17.030 . 1 398 81 81 ALA N N 121.857 . 1 399 82 82 PHE H H 8.302 . 1 400 82 82 PHE C C 177.165 . . 401 82 82 PHE CA C 61.529 . 1 402 82 82 PHE CB C 38.216 . 1 403 82 82 PHE N N 119.237 . 1 404 83 83 ARG H H 8.266 . 1 405 83 83 ARG C C 179.021 . . 406 83 83 ARG CA C 56.442 . 1 407 83 83 ARG CB C 26.681 . 1 408 83 83 ARG N N 117.959 . 1 409 84 84 GLY H H 7.919 . 1 410 84 84 GLY C C 176.795 . . 411 84 84 GLY CA C 46.122 . 1 412 84 84 GLY N N 106.672 . 1 413 85 85 VAL H H 8.135 . 1 414 85 85 VAL C C 176.388 . . 415 85 85 VAL CA C 66.556 . 1 416 85 85 VAL CB C 30.130 . 1 417 85 85 VAL N N 125.389 . 1 418 86 86 GLN H H 7.707 . 1 419 86 86 GLN C C 179.932 . . 420 86 86 GLN CA C 60.154 . 1 421 86 86 GLN CB C 28.750 . 1 422 86 86 GLN N N 117.933 . 1 423 87 87 LEU H H 8.476 . 1 424 87 87 LEU C C 178.664 . . 425 87 87 LEU CA C 57.782 . 1 426 87 87 LEU N N 119.953 . 1 427 88 88 THR H H 8.136 . 1 428 88 88 THR C C 179.361 . . 429 88 88 THR CA C 64.905 . 1 430 88 88 THR CB C 68.190 . 1 431 88 88 THR N N 108.847 . 1 432 89 89 TYR H H 9.021 . 1 433 89 89 TYR C C 176.647 . . 434 89 89 TYR CA C 62.298 . 1 435 89 89 TYR CB C 37.434 . 1 436 89 89 TYR N N 128.296 . 1 437 90 90 GLU H H 7.785 . 1 438 90 90 GLU C C 178.787 . . 439 90 90 GLU CA C 59.393 . 1 440 90 90 GLU CB C 28.206 . 1 441 90 90 GLU N N 121.368 . 1 442 91 91 HIS H H 8.566 . 1 443 91 91 HIS C C 177.617 . . 444 91 91 HIS CA C 57.233 . 1 445 91 91 HIS CB C 33.188 . 1 446 91 91 HIS N N 120.006 . 1 447 92 92 THR H H 8.250 . 1 448 92 92 THR C C 176.711 . . 449 92 92 THR CA C 67.190 . 1 450 92 92 THR CB C 68.253 . 1 451 92 92 THR N N 115.439 . 1 452 93 93 MET H H 8.144 . 1 453 93 93 MET C C 178.899 . . 454 93 93 MET CA C 57.347 . 1 455 93 93 MET CB C 30.423 . 1 456 93 93 MET N N 120.675 . 1 457 94 94 LEU H H 7.848 . 1 458 94 94 LEU C C 177.956 . . 459 94 94 LEU CA C 57.048 . 1 460 94 94 LEU CB C 40.916 . 1 461 94 94 LEU N N 119.522 . 1 462 95 95 GLN H H 7.140 . 1 463 95 95 GLN C C 178.282 . . 464 95 95 GLN CA C 57.511 . 1 465 95 95 GLN CB C 28.199 . 1 466 95 95 GLN N N 113.631 . 1 467 96 96 LEU H H 7.881 . 1 468 96 96 LEU C C 176.681 . . 469 96 96 LEU CA C 56.301 . 1 470 96 96 LEU CB C 42.587 . 1 471 96 96 LEU N N 118.547 . 1 472 97 97 TYR H H 7.805 . 1 473 97 97 TYR C C 172.475 . . 474 97 97 TYR CA C 54.706 . 1 475 97 97 TYR CB C 37.674 . 1 476 97 97 TYR N N 117.316 . 1 477 98 98 PRO C C 177.531 . . 478 98 98 PRO CA C 63.113 . 1 479 99 99 SER H H 8.141 . 1 480 99 99 SER C C 173.792 . . 481 99 99 SER CA C 55.247 . 1 482 99 99 SER CB C 63.741 . 1 483 99 99 SER N N 117.855 . 1 484 100 100 PRO C C 176.479 . . 485 101 101 PHE H H 7.679 . 1 486 101 101 PHE C C 175.285 . . 487 101 101 PHE CA C 56.463 . 1 488 101 101 PHE CB C 38.594 . 1 489 101 101 PHE N N 117.813 . 1 490 102 102 ALA H H 7.818 . 1 491 102 102 ALA C C 177.704 . . 492 102 102 ALA CA C 52.237 . 1 493 102 102 ALA CB C 18.838 . 1 494 102 102 ALA N N 125.041 . 1 495 103 103 THR H H 8.066 . 1 496 103 103 THR C C 174.580 . . 497 103 103 THR CA C 61.318 . 1 498 103 103 THR CB C 69.216 . 1 499 103 103 THR N N 114.393 . 1 500 104 104 SER H H 8.122 . 1 501 104 104 SER C C 173.705 . . 502 104 104 SER CA C 57.912 . 1 503 104 104 SER CB C 63.389 . 1 504 104 104 SER N N 118.174 . 1 505 105 105 ASP H H 7.982 . 1 506 105 105 ASP C C 175.530 . . 507 105 105 ASP CA C 53.731 . 1 508 105 105 ASP CB C 40.778 . 1 509 105 105 ASP N N 122.499 . 1 510 106 106 PHE H H 7.936 . 1 511 106 106 PHE C C 174.891 . . 512 106 106 PHE CA C 56.492 . 1 513 106 106 PHE CB C 38.704 . 1 514 106 106 PHE N N 120.330 . 1 515 107 107 MET H H 7.764 . 1 516 107 107 MET C C 175.157 . . 517 107 107 MET CA C 54.216 . 1 518 107 107 MET CB C 33.840 . 1 519 107 107 MET N N 120.297 . 1 520 108 108 VAL H H 8.091 . 1 521 108 108 VAL C C 175.148 . . 522 108 108 VAL CA C 61.754 . 1 523 108 108 VAL CB C 31.622 . 1 524 108 108 VAL N N 120.245 . 1 525 109 109 ARG H H 7.770 . 1 526 109 109 ARG C C 174.696 . . 527 109 109 ARG CA C 54.231 . 1 528 109 109 ARG CB C 30.314 . 1 529 109 109 ARG N N 125.729 . 1 530 110 110 PHE H H 8.159 . 1 531 110 110 PHE C C 173.279 . . 532 110 110 PHE CA C 56.850 . 1 533 110 110 PHE CB C 38.145 . 1 534 110 110 PHE N N 121.869 . 1 535 111 111 PRO C C 177.750 . . 536 111 111 PRO CA C 61.799 . 1 537 111 111 PRO CB C 30.076 . 1 538 112 112 GLU H H 8.949 . 1 539 112 112 GLU C C 176.426 . . 540 112 112 GLU CA C 58.726 . 1 541 112 112 GLU CB C 28.737 . 1 542 112 112 GLU N N 122.431 . 1 543 113 113 TRP H H 6.490 . 1 544 113 113 TRP HE1 H 10.956 . 1 545 113 113 TRP C C 174.206 . . 546 113 113 TRP CA C 53.597 . 1 547 113 113 TRP CB C 27.953 . 1 548 113 113 TRP N N 111.276 . 1 549 113 113 TRP NE1 N 133.863 . 1 550 114 114 LEU H H 6.721 . 1 551 114 114 LEU C C 171.823 . . 552 114 114 LEU CA C 52.037 . 1 553 114 114 LEU CB C 41.237 . 1 554 114 114 LEU N N 121.088 . 1 555 115 115 PRO C C 176.764 . . 556 115 115 PRO CA C 61.062 . 1 557 115 115 PRO CB C 27.569 . 1 558 116 116 LEU H H 7.722 . 1 559 116 116 LEU C C 176.688 . . 560 116 116 LEU CA C 58.019 . 1 561 116 116 LEU CB C 38.948 . 1 562 116 116 LEU N N 124.442 . 1 563 117 117 ASP H H 8.900 . 1 564 117 117 ASP C C 176.557 . . 565 117 117 ASP CA C 55.623 . 1 566 117 117 ASP CB C 37.986 . 1 567 117 117 ASP N N 112.719 . 1 568 118 118 LYS H H 6.872 . 1 569 118 118 LYS C C 178.857 . . 570 118 118 LYS CA C 56.843 . 1 571 118 118 LYS CB C 31.243 . 1 572 118 118 LYS N N 118.748 . 1 573 119 119 TRP H H 7.710 . 1 574 119 119 TRP HE1 H 10.400 . 1 575 119 119 TRP C C 176.731 . . 576 119 119 TRP CA C 57.221 . 1 577 119 119 TRP CB C 30.198 . 1 578 119 119 TRP N N 118.474 . 1 579 119 119 TRP NE1 N 130.091 . 1 580 120 120 VAL H H 8.159 . 1 581 120 120 VAL C C 173.668 . . 582 120 120 VAL CA C 58.446 . 1 583 120 120 VAL CB C 31.030 . 1 584 120 120 VAL N N 113.487 . 1 585 121 121 PRO C C 178.248 . . 586 121 121 PRO CA C 64.902 . 1 587 121 121 PRO CB C 31.278 . 1 588 122 122 GLN H H 9.178 . 1 589 122 122 GLN C C 174.323 . . 590 122 122 GLN CA C 58.189 . 1 591 122 122 GLN CB C 27.102 . 1 592 122 122 GLN N N 116.281 . 1 593 123 123 VAL H H 7.485 . 1 594 123 123 VAL C C 175.758 . . 595 123 123 VAL CA C 61.517 . 1 596 123 123 VAL CB C 34.106 . 1 597 123 123 VAL N N 113.069 . 1 598 124 124 PHE H H 7.485 . 1 599 124 124 PHE C C 172.717 . . 600 124 124 PHE CA C 58.275 . 1 601 124 124 PHE CB C 38.553 . 1 602 124 124 PHE N N 113.292 . 1 603 125 125 VAL H H 7.085 . 1 604 125 125 VAL C C 176.125 . . 605 125 125 VAL CA C 62.551 . 1 606 125 125 VAL CB C 32.062 . 1 607 125 125 VAL N N 116.751 . 1 608 126 126 ALA H H 8.107 . 1 609 126 126 ALA C C 177.147 . . 610 126 126 ALA CA C 50.504 . 1 611 126 126 ALA CB C 21.074 . 1 612 126 126 ALA N N 130.959 . 1 613 127 127 SER H H 8.311 . 1 614 127 127 SER C C 173.401 . . 615 127 127 SER CA C 57.919 . 1 616 127 127 SER CB C 64.902 . 1 617 127 127 SER N N 113.784 . 1 618 128 128 GLY H H 7.812 . 1 619 128 128 GLY C C 172.224 . . 620 128 128 GLY CA C 44.182 . 1 621 128 128 GLY N N 106.584 . 1 622 129 129 ASP H H 8.315 . 1 623 129 129 ASP C C 178.751 . . 624 129 129 ASP CA C 52.647 . 1 625 129 129 ASP CB C 43.582 . 1 626 129 129 ASP N N 119.381 . 1 627 130 130 CYS H H 9.279 . 1 628 130 130 CYS C C 173.799 . . 629 130 130 CYS CA C 54.992 . 1 630 130 130 CYS CB C 38.294 . 1 631 130 130 CYS N N 123.031 . 1 632 131 131 ALA H H 8.741 . 1 633 131 131 ALA C C 177.755 . . 634 131 131 ALA CA C 53.491 . 1 635 131 131 ALA CB C 18.731 . 1 636 131 131 ALA N N 121.344 . 1 637 132 132 GLU H H 7.102 . 1 638 132 132 GLU C C 177.574 . . 639 132 132 GLU CA C 56.452 . 1 640 132 132 GLU CB C 29.694 . 1 641 132 132 GLU N N 116.699 . 1 642 133 133 ARG H H 8.810 . 1 643 133 133 ARG C C 176.148 . . 644 133 133 ARG CA C 56.597 . 1 645 133 133 ARG CB C 28.584 . 1 646 133 133 ARG N N 127.506 . 1 647 134 134 GLN H H 9.796 . 1 648 134 134 GLN C C 175.225 . . 649 134 134 GLN CA C 57.748 . 1 650 134 134 GLN CB C 35.351 . 1 651 134 134 GLN N N 122.401 . 1 652 135 135 TRP H H 8.901 . 1 653 135 135 TRP HE1 H 10.510 . 1 654 135 135 TRP C C 172.162 . . 655 135 135 TRP CA C 60.084 . 1 656 135 135 TRP CB C 31.102 . 1 657 135 135 TRP N N 122.875 . 1 658 135 135 TRP NE1 N 131.560 . 1 659 136 136 ASP H H 7.166 . 1 660 136 136 ASP C C 172.348 . . 661 136 136 ASP CA C 51.750 . 1 662 136 136 ASP CB C 43.938 . 1 663 136 136 ASP N N 124.973 . 1 664 137 137 PHE H H 7.987 . 1 665 137 137 PHE C C 176.161 . . 666 137 137 PHE CA C 56.742 . 1 667 137 137 PHE CB C 41.447 . 1 668 137 137 PHE N N 118.180 . 1 669 138 138 LEU H H 9.009 . 1 670 138 138 LEU C C 175.329 . . 671 138 138 LEU CA C 55.287 . 1 672 138 138 LEU CB C 38.356 . 1 673 138 138 LEU N N 126.743 . 1 674 139 139 GLY H H 8.194 . 1 675 139 139 GLY C C 174.034 . . 676 139 139 GLY CA C 44.734 . 1 677 139 139 GLY N N 102.807 . 1 678 140 140 LEU H H 7.516 . 1 679 140 140 LEU C C 176.447 . . 680 140 140 LEU CA C 53.728 . 1 681 140 140 LEU CB C 41.377 . 1 682 140 140 LEU N N 121.711 . 1 683 141 141 GLU H H 7.818 . 1 684 141 141 GLU C C 179.030 . . 685 141 141 GLU CA C 55.180 . 1 686 141 141 GLU CB C 30.661 . 1 687 141 141 GLU N N 123.429 . 1 688 142 142 MET H H 9.041 . 1 689 142 142 MET C C 173.942 . . 690 142 142 MET CA C 62.196 . 1 691 142 142 MET CB C 30.899 . 1 692 142 142 MET N N 123.227 . 1 693 143 143 PRO C C 176.957 . . 694 143 143 PRO CA C 65.553 . 1 695 143 143 PRO CB C 29.359 . 1 696 144 144 GLN H H 7.217 . 1 697 144 144 GLN C C 177.844 . . 698 144 144 GLN CA C 59.571 . 1 699 144 144 GLN CB C 28.097 . 1 700 144 144 GLN N N 114.960 . 1 701 145 145 TRP H H 7.260 . 1 702 145 145 TRP HE1 H 10.259 . 1 703 145 145 TRP C C 178.711 . . 704 145 145 TRP CA C 60.675 . 1 705 145 145 TRP CB C 29.604 . 1 706 145 145 TRP N N 118.012 . 1 707 145 145 TRP NE1 N 131.158 . 1 708 146 146 LEU H H 8.080 . 1 709 146 146 LEU C C 176.974 . . 710 146 146 LEU CA C 56.300 . 1 711 146 146 LEU CB C 40.604 . 1 712 146 146 LEU N N 117.572 . 1 713 147 147 LEU H H 8.077 . 1 714 147 147 LEU C C 178.637 . . 715 147 147 LEU CA C 58.345 . 1 716 147 147 LEU CB C 40.130 . 1 717 147 147 LEU N N 124.235 . 1 718 148 148 GLY H H 7.579 . 1 719 148 148 GLY C C 174.373 . . 720 148 148 GLY CA C 47.589 . 1 721 148 148 GLY N N 104.688 . 1 722 149 149 ILE H H 8.205 . 1 723 149 149 ILE C C 177.739 . . 724 149 149 ILE CA C 65.427 . 1 725 149 149 ILE CB C 37.279 . 1 726 149 149 ILE N N 122.006 . 1 727 150 150 PHE H H 9.369 . 1 728 150 150 PHE C C 178.878 . . 729 150 150 PHE CA C 63.086 . 1 730 150 150 PHE CB C 37.657 . 1 731 150 150 PHE N N 119.123 . 1 732 151 151 ILE H H 8.665 . 1 733 151 151 ILE C C 177.271 . . 734 151 151 ILE CA C 65.677 . 1 735 151 151 ILE CB C 36.086 . 1 736 151 151 ILE N N 120.869 . 1 737 152 152 ALA H H 8.286 . 1 738 152 152 ALA C C 179.308 . . 739 152 152 ALA CA C 55.877 . 1 740 152 152 ALA CB C 16.510 . 1 741 152 152 ALA N N 123.630 . 1 742 153 153 TYR H H 8.935 . 1 743 153 153 TYR C C 179.559 . . 744 153 153 TYR CA C 63.350 . 1 745 153 153 TYR CB C 38.866 . 1 746 153 153 TYR N N 115.956 . 1 747 154 154 LEU H H 8.727 . 1 748 154 154 LEU C C 177.312 . . 749 154 154 LEU CA C 57.977 . 1 750 154 154 LEU CB C 41.279 . 1 751 154 154 LEU N N 122.384 . 1 752 155 155 ILE H H 8.967 . 1 753 155 155 ILE C C 177.707 . . 754 155 155 ILE CA C 64.879 . 1 755 155 155 ILE CB C 36.695 . 1 756 155 155 ILE N N 119.157 . 1 757 156 156 VAL H H 8.324 . 1 758 156 156 VAL C C 176.402 . . 759 156 156 VAL CA C 67.196 . 1 760 156 156 VAL CB C 30.652 . 1 761 156 156 VAL N N 118.102 . 1 762 157 157 ALA H H 7.537 . 1 763 157 157 ALA C C 179.299 . . 764 157 157 ALA CA C 54.678 . 1 765 157 157 ALA CB C 15.044 . 1 766 157 157 ALA N N 122.495 . 1 767 158 158 VAL H H 7.828 . 1 768 158 158 VAL C C 177.556 . . 769 158 158 VAL CA C 66.637 . 1 770 158 158 VAL CB C 30.215 . 1 771 158 158 VAL N N 116.557 . 1 772 159 159 LEU H H 8.086 . 1 773 159 159 LEU C C 178.692 . . 774 159 159 LEU CA C 57.458 . 1 775 159 159 LEU CB C 40.767 . 1 776 159 159 LEU N N 118.831 . 1 777 160 160 VAL H H 8.537 . 1 778 160 160 VAL C C 180.205 . . 779 160 160 VAL CA C 66.928 . 1 780 160 160 VAL CB C 30.172 . 1 781 160 160 VAL N N 119.628 . 1 782 161 161 VAL H H 8.452 . 1 783 161 161 VAL C C 178.329 . . 784 161 161 VAL CA C 67.228 . 1 785 161 161 VAL CB C 30.416 . 1 786 161 161 VAL N N 124.125 . 1 787 162 162 ILE H H 8.500 . 1 788 162 162 ILE C C 175.786 . . 789 162 162 ILE CA C 63.857 . 1 790 162 162 ILE CB C 36.706 . 1 791 162 162 ILE N N 115.500 . 1 792 163 163 SER H H 7.685 . 1 793 163 163 SER C C 175.880 . . 794 163 163 SER CA C 60.135 . 1 795 163 163 SER CB C 63.261 . 1 796 163 163 SER N N 113.991 . 1 797 164 164 GLN H H 7.770 . 1 798 164 164 GLN C C 178.699 . . 799 164 164 GLN CA C 55.641 . 1 800 164 164 GLN N N 121.357 . 1 801 165 165 PRO C C 176.166 . . 802 165 165 PRO CA C 63.121 . 1 803 165 165 PRO CB C 29.640 . 1 804 166 166 PHE H H 7.618 . 1 805 166 166 PHE C C 175.045 . . 806 166 166 PHE CA C 57.917 . 1 807 166 166 PHE CB C 38.392 . 1 808 166 166 PHE N N 120.245 . 1 809 167 167 LYS H H 8.003 . 1 810 167 167 LYS C C 176.252 . . 811 167 167 LYS CA C 55.839 . 1 812 167 167 LYS CB C 32.368 . 1 813 167 167 LYS N N 121.820 . 1 814 168 168 ALA H H 8.093 . 1 815 168 168 ALA C C 177.305 . . 816 168 168 ALA CA C 52.183 . 1 817 168 168 ALA CB C 18.801 . 1 818 168 168 ALA N N 124.760 . 1 819 169 169 LYS H H 8.180 . 1 820 169 169 LYS N N 120.508 . 1 821 172 172 ASP C C 176.440 . . 822 172 172 ASP CA C 54.218 . 1 823 172 172 ASP CB C 40.642 . 1 824 173 173 LEU H H 7.906 . 1 825 173 173 LEU C C 176.846 . . 826 173 173 LEU CA C 55.788 . 1 827 173 173 LEU CB C 41.462 . 1 828 173 173 LEU N N 122.173 . 1 829 174 174 PHE H H 7.929 . 1 830 174 174 PHE C C 176.264 . . 831 174 174 PHE CA C 57.225 . 1 832 174 174 PHE CB C 38.627 . 1 833 174 174 PHE N N 117.074 . 1 834 175 175 GLY H H 8.041 . 1 835 175 175 GLY C C 174.274 . . 836 175 175 GLY CA C 45.288 . 1 837 175 175 GLY N N 109.436 . 1 838 176 176 ARG H H 8.162 . 1 839 176 176 ARG N N 120.588 . 1 stop_ save_