data_15998 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Chemical shifts of the b'-x region of human protein disulfide isomerase ; _BMRB_accession_number 15998 _BMRB_flat_file_name bmr15998.str _Entry_type original _Submission_date 2008-10-23 _Accession_date 2008-10-23 _Entry_origination author _NMR_STAR_version 2.1.1 _Experimental_method NMR _Details 'Chemical shifts of the b'-x region of human protein disulfide isomerase.' loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Byrne Lee J. . 2 Howard Mark J. . 3 Williamson Richard A. . 4 Sidhu Ateesh . . 5 Freedman Robert B. . 6 Wallis Katrine . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 131 "13C chemical shifts" 123 "15N chemical shifts" 129 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2009-11-12 update BMRB 'complete entry citation' 2009-07-17 original author 'original release' stop_ save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title "Mapping of the ligand-binding site on the b' domain of human PDI: interaction with peptide ligands and the x-linker region." _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 19604149 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Byrne Lee J. . 2 Sidhu Ateesh . . 3 Wallis 'A. Katrine' . . 4 Ruddock Lloyd W. . 5 Freedman Robert B. . 6 Howard Mark J. . 7 Williamson Richard A. . stop_ _Journal_abbreviation 'Biochem. J.' _Journal_name_full 'The Biochemical journal' _Journal_volume 423 _Journal_issue 2 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 209 _Page_last 217 _Year 2009 _Details . loop_ _Keyword Domain 'ligand binding' PDI thioredoxin stop_ save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name b'-x _Enzyme_commission_number 'EC 5.3.4.1' loop_ _Mol_system_component_name _Mol_label b'-x $b'-x stop_ _System_molecular_weight 16296.7 _System_physical_state native _System_oligomer_state ? _System_paramagnetic no _System_thiol_state . _Database_query_date . _Details 'single polypeptide chain' save_ ######################## # Monomeric polymers # ######################## save_b'-x _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common b'-x _Molecular_mass 16296.7 _Mol_thiol_state 'all free' loop_ _Biological_function 'disulfide bond formation' 'disulfide bond isomerisation' 'ligand binding' stop_ _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 140 _Mol_residue_sequence ; KHNQLPLVIEFTEQTAPKIF GGEIKTHILLFLPKSVSDYD GKLSNFKTAAESFKGKILFI FIDSDHTDNQRILEFFGLKK EECPAVRLITLEEEMTKYKP ESEELTAERITEFCHRFLEG KIKPHLMSQELPEDWDKQPV ; loop_ _Residue_seq_code _Residue_label 1 LYS 2 HIS 3 ASN 4 GLN 5 LEU 6 PRO 7 LEU 8 VAL 9 ILE 10 GLU 11 PHE 12 THR 13 GLU 14 GLN 15 THR 16 ALA 17 PRO 18 LYS 19 ILE 20 PHE 21 GLY 22 GLY 23 GLU 24 ILE 25 LYS 26 THR 27 HIS 28 ILE 29 LEU 30 LEU 31 PHE 32 LEU 33 PRO 34 LYS 35 SER 36 VAL 37 SER 38 ASP 39 TYR 40 ASP 41 GLY 42 LYS 43 LEU 44 SER 45 ASN 46 PHE 47 LYS 48 THR 49 ALA 50 ALA 51 GLU 52 SER 53 PHE 54 LYS 55 GLY 56 LYS 57 ILE 58 LEU 59 PHE 60 ILE 61 PHE 62 ILE 63 ASP 64 SER 65 ASP 66 HIS 67 THR 68 ASP 69 ASN 70 GLN 71 ARG 72 ILE 73 LEU 74 GLU 75 PHE 76 PHE 77 GLY 78 LEU 79 LYS 80 LYS 81 GLU 82 GLU 83 CYS 84 PRO 85 ALA 86 VAL 87 ARG 88 LEU 89 ILE 90 THR 91 LEU 92 GLU 93 GLU 94 GLU 95 MET 96 THR 97 LYS 98 TYR 99 LYS 100 PRO 101 GLU 102 SER 103 GLU 104 GLU 105 LEU 106 THR 107 ALA 108 GLU 109 ARG 110 ILE 111 THR 112 GLU 113 PHE 114 CYS 115 HIS 116 ARG 117 PHE 118 LEU 119 GLU 120 GLY 121 LYS 122 ILE 123 LYS 124 PRO 125 HIS 126 LEU 127 MET 128 SER 129 GLN 130 GLU 131 LEU 132 PRO 133 GLU 134 ASP 135 TRP 136 ASP 137 LYS 138 GLN 139 PRO 140 VAL stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-09-30 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 15303 bb-PDI 91.43 228 100.00 100.00 2.19e-85 BMRB 15974 "b-b'-x" 100.00 236 100.00 100.00 1.28e-95 PDB 2K18 "Solution Structure Of Bb' Domains Of Human Protein Disulfide Isomerase" 91.43 228 100.00 100.00 2.19e-85 PDB 3BJ5 "Alternative Conformations Of The X Region Of Human Protein Disulphide- Isomerase Modulate Exposure Of The Substrate Binding B' " 99.29 147 99.28 99.28 3.25e-94 PDB 3UEM "Crystal Structure Of Human Pdi Bb'a' Domains" 100.00 361 100.00 100.00 1.14e-93 PDB 4EKZ "Crystal Structure Of Reduced Hpdi (abb'xa')" 100.00 482 100.00 100.00 2.89e-92 PDB 4EL1 "Crystal Structure Of Oxidized Hpdi (abb'xa')" 100.00 482 100.00 100.00 2.89e-92 PDB 4JU5 "Crystal Structure Of The Dimeric Form Of The Bb' Domains Of Human Protein Disulfide Isomerase" 98.57 238 100.00 100.00 6.06e-94 DBJ BAE79726 "protein disulfide isomerase [Macaca fuscata]" 100.00 510 98.57 100.00 3.34e-91 DBJ BAG37999 "unnamed protein product [Homo sapiens]" 100.00 508 100.00 100.00 2.20e-92 DBJ BAG59598 "unnamed protein product [Homo sapiens]" 100.00 451 100.00 100.00 8.87e-93 DBJ BAG60277 "unnamed protein product [Homo sapiens]" 100.00 492 99.29 99.29 6.14e-92 DBJ BAG62267 "unnamed protein product [Homo sapiens]" 100.00 452 100.00 100.00 6.96e-93 EMBL CAA28775 "unnamed protein product [Homo sapiens]" 100.00 508 100.00 100.00 5.92e-92 EMBL CAA30112 "glutathione-insulin transhydrogenase (216 AA) [Homo sapiens]" 55.00 216 100.00 100.00 2.62e-46 EMBL CAH93050 "hypothetical protein [Pongo abelii]" 100.00 508 99.29 100.00 5.32e-92 GB AAA61169 "thyroid hormone binding protein precursor [Homo sapiens]" 100.00 508 97.86 97.86 1.28e-89 GB AAC13652 "prolyl 4-hydroxylase beta-subunit [Homo sapiens]" 100.00 508 100.00 100.00 2.20e-92 GB AAH10859 "Prolyl 4-hydroxylase, beta polypeptide [Homo sapiens]" 100.00 508 100.00 100.00 2.20e-92 GB AAH29617 "Prolyl 4-hydroxylase, beta polypeptide [Homo sapiens]" 100.00 508 100.00 100.00 2.20e-92 GB AAH71892 "Prolyl 4-hydroxylase, beta polypeptide [Homo sapiens]" 100.00 508 100.00 100.00 2.20e-92 REF NP_000909 "protein disulfide-isomerase precursor [Homo sapiens]" 100.00 508 100.00 100.00 2.20e-92 REF NP_001126805 "protein disulfide-isomerase precursor [Pongo abelii]" 100.00 508 99.29 100.00 5.32e-92 REF NP_001233358 "protein disulfide-isomerase precursor [Pan troglodytes]" 100.00 508 99.29 99.29 1.91e-91 REF XP_002764185 "PREDICTED: protein disulfide-isomerase isoform X2 [Callithrix jacchus]" 100.00 510 97.86 98.57 9.80e-91 REF XP_003282223 "PREDICTED: protein disulfide-isomerase isoform X1 [Nomascus leucogenys]" 100.00 505 98.57 99.29 4.86e-91 SP P07237 "RecName: Full=Protein disulfide-isomerase; Short=PDI; AltName: Full=Cellular thyroid hormone-binding protein; AltName: Full=Pro" 100.00 508 100.00 100.00 2.20e-92 SP Q2HWU2 "RecName: Full=Protein disulfide-isomerase; Short=PDI; AltName: Full=Prolyl 4-hydroxylase subunit beta; Flags: Precursor" 100.00 510 98.57 100.00 3.34e-91 SP Q5R5B6 "RecName: Full=Protein disulfide-isomerase; Short=PDI; AltName: Full=Cellular thyroid hormone-binding protein; AltName: Full=Pro" 100.00 508 99.29 100.00 5.32e-92 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $b'-x Human 9606 Eukaryota Metazoa Homo sapiens stop_ save_ ######################### # Experimental source # ######################### save_experimental_source _Saveframe_category experimental_source loop_ _Mol_label _Production_method _Host_organism_name_common _Genus _Species _Strain _Vector_name $b'-x 'recombinant technology' . Escherichia coli BL21(DE3) pET23b stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling D2O 10 % 'natural abundance' H2O 90 % 'natural abundance' 'sodium phosphate' 20 mM 'natural abundance' 'sodium chloride' 150 mM 'natural abundance' $b'-x 1.5 mM '[U-99% 13C; U-99% 15N]' stop_ save_ ############################ # Computer software used # ############################ save_CCPN_Analysis _Saveframe_category software _Name CCPN_Analysis _Version 1.15 loop_ _Vendor _Address _Electronic_address CCPN . www.ccpn.ac.uk/ccpn stop_ loop_ _Task 'chemical shift assignment' 'data analysis' 'peak picking' stop_ _Details . save_ save_NMRPipe _Saveframe_category software _Name NMRPipe _Version . loop_ _Vendor _Address _Electronic_address 'Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax' . www.spin.niddk.nih.gov stop_ loop_ _Task processing stop_ _Details . save_ save_VNMR _Saveframe_category software _Name VNMR _Version . loop_ _Vendor _Address _Electronic_address Varian . www.varianinc.com stop_ loop_ _Task collection 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_2D_1H-15N_HSQC_1 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-15N HSQC' _Sample_label $sample_1 save_ save_3D_CBCA(CO)NH_2 _Saveframe_category NMR_applied_experiment _Experiment_name '3D CBCA(CO)NH' _Sample_label $sample_1 save_ save_3D_HNCACB_3 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCACB' _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' 0.15 . M pH 6.5 . pH pressure 1 . atm temperature 298 . K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference_1 _Saveframe_category chemical_shift_reference _Details . loop_ _Mol_common_name _Atom_type _Atom_isotope_number _Atom_group _Chem_shift_units _Chem_shift_value _Reference_method _Reference_type _External_reference_sample_geometry _External_reference_location _External_reference_axis _Indirect_shift_ratio DSS C 13 'methyl protons' ppm 0.00 . indirect . . . 0.251449530 DSS H 1 'methyl protons' ppm 0.00 internal direct . . . 1.000000000 DSS N 15 'methyl protons' ppm 0.00 . 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 ; Extra peaks of x-linker found for a few C-terminal residues, probably the result of the x-linker binding within the b' domain peptide binding site. Additional 15N and 1H backbone amide chemical shifts corresponding to (in ppm): 338-Leu (123.40, 8.05), 339-Met (126.04, 7.82), 340-Ser (117.11, 8.54), 341-Gln (120.22, 7.78), 342-Glu (120.01, 8.13), 345-Glu (122.73, 8.44), 346-Asp (115.83, 8.27), 347-Trp (119.01, 7.72), 348-Asp (125.48, 8.34), 349-Lys (120.43, 7.95), 350-Gln (123.86, 8.39) ; loop_ _Software_label $CCPN_Analysis stop_ loop_ _Experiment_label '2D 1H-15N HSQC' '3D CBCA(CO)NH' '3D HNCACB' 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 b'-x _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 1 213 1 LYS CA C 53.108 0.345 1 2 213 1 LYS N N 112.247 0.064 1 3 214 2 HIS H H 8.279 0.003 1 4 214 2 HIS CA C 55.919 0.345 1 5 214 2 HIS N N 120.146 0.064 1 6 215 3 ASN H H 7.567 0.003 1 7 215 3 ASN CA C 53.243 0.345 1 8 215 3 ASN N N 116.943 0.064 1 9 216 4 GLN H H 7.855 0.003 1 10 216 4 GLN CA C 55.837 0.345 1 11 216 4 GLN N N 120.457 0.064 1 12 217 5 LEU H H 8.454 0.003 1 13 217 5 LEU CA C 53.093 0.345 1 14 217 5 LEU N N 123.981 0.064 1 15 219 7 LEU H H 8.242 0.003 1 16 219 7 LEU CA C 56.830 0.345 1 17 219 7 LEU N N 120.527 0.064 1 18 220 8 VAL H H 7.396 0.003 1 19 220 8 VAL CA C 59.868 0.345 1 20 220 8 VAL N N 111.563 0.064 1 21 221 9 ILE H H 8.740 0.003 1 22 221 9 ILE N N 125.409 0.064 1 23 222 10 GLU H H 8.351 0.003 1 24 222 10 GLU CA C 54.719 0.345 1 25 222 10 GLU N N 127.615 0.064 1 26 223 11 PHE H H 8.737 0.003 1 27 223 11 PHE CA C 59.301 0.345 1 28 223 11 PHE N N 129.439 0.064 1 29 224 12 THR H H 7.080 0.003 1 30 224 12 THR N N 118.224 0.064 1 31 225 13 GLU H H 9.068 0.003 1 32 225 13 GLU CA C 59.605 0.345 1 33 225 13 GLU N N 120.600 0.064 1 34 226 14 GLN H H 7.941 0.003 1 35 226 14 GLN CA C 58.347 0.345 1 36 226 14 GLN N N 114.532 0.064 1 37 227 15 THR H H 7.466 0.003 1 38 227 15 THR CA C 61.758 0.345 1 39 227 15 THR N N 108.962 0.064 1 40 228 16 ALA H H 7.597 0.003 1 41 228 16 ALA CA C 56.769 0.345 1 42 228 16 ALA N N 125.382 0.064 1 43 230 18 LYS H H 7.239 0.003 1 44 230 18 LYS CA C 57.578 0.345 1 45 230 18 LYS N N 115.497 0.064 1 46 231 19 ILE H H 7.605 0.003 1 47 231 19 ILE CA C 64.287 0.345 1 48 231 19 ILE N N 119.490 0.064 1 49 232 20 PHE H H 7.921 0.003 1 50 232 20 PHE CA C 59.714 0.345 1 51 232 20 PHE N N 115.238 0.064 1 52 233 21 GLY H H 7.654 0.003 1 53 233 21 GLY CA C 45.294 0.345 1 54 233 21 GLY N N 106.806 0.064 1 55 234 22 GLY H H 7.434 0.003 1 56 234 22 GLY CA C 44.758 0.345 1 57 234 22 GLY N N 107.760 0.064 1 58 235 23 GLU H H 8.482 0.003 1 59 235 23 GLU CA C 58.186 0.345 1 60 235 23 GLU N N 117.309 0.064 1 61 236 24 ILE H H 7.825 0.003 1 62 236 24 ILE CA C 61.839 0.345 1 63 236 24 ILE N N 119.610 0.064 1 64 237 25 LYS H H 8.573 0.003 1 65 237 25 LYS CA C 55.422 0.345 1 66 237 25 LYS N N 125.505 0.064 1 67 238 26 THR H H 6.789 0.003 1 68 238 26 THR CA C 62.106 0.345 1 69 238 26 THR N N 116.034 0.064 1 70 239 27 HIS H H 8.870 0.003 1 71 239 27 HIS CA C 54.084 0.345 1 72 239 27 HIS N N 125.874 0.064 1 73 240 28 ILE H H 9.274 0.003 1 74 240 28 ILE CA C 58.877 0.345 1 75 240 28 ILE N N 122.550 0.064 1 76 241 29 LEU H H 9.073 0.003 1 77 241 29 LEU CA C 53.616 0.345 1 78 241 29 LEU N N 129.024 0.064 1 79 242 30 LEU H H 8.732 0.003 1 80 242 30 LEU CA C 53.027 0.345 1 81 242 30 LEU N N 123.279 0.064 1 82 243 31 PHE H H 9.174 0.003 1 83 243 31 PHE CA C 57.042 0.345 1 84 243 31 PHE N N 128.070 0.064 1 85 244 32 LEU H H 9.092 0.003 1 86 244 32 LEU CA C 50.848 0.345 1 87 244 32 LEU N N 127.194 0.064 1 88 246 34 LYS H H 8.284 0.003 1 89 246 34 LYS CA C 58.921 0.345 1 90 246 34 LYS N N 124.128 0.064 1 91 247 35 SER H H 7.599 0.003 1 92 247 35 SER CA C 63.735 0.345 1 93 247 35 SER N N 108.152 0.064 1 94 248 36 VAL H H 7.548 0.003 1 95 248 36 VAL CA C 62.179 0.345 1 96 248 36 VAL N N 123.012 0.064 1 97 249 37 SER H H 8.453 0.003 1 98 249 37 SER CA C 59.535 0.345 1 99 249 37 SER N N 120.932 0.064 1 100 250 38 ASP H H 9.057 0.003 1 101 250 38 ASP CA C 54.178 0.345 1 102 250 38 ASP N N 122.866 0.064 1 103 251 39 TYR H H 7.643 0.003 1 104 251 39 TYR CA C 63.076 0.345 1 105 251 39 TYR N N 120.248 0.064 1 106 252 40 ASP H H 8.724 0.003 1 107 252 40 ASP CA C 57.418 0.345 1 108 252 40 ASP N N 114.979 0.064 1 109 253 41 GLY H H 7.770 0.003 1 110 253 41 GLY CA C 47.138 0.345 1 111 253 41 GLY N N 110.160 0.064 1 112 254 42 LYS H H 8.017 0.003 1 113 254 42 LYS CA C 60.026 0.345 1 114 254 42 LYS N N 123.280 0.064 1 115 255 43 LEU H H 8.185 0.003 1 116 255 43 LEU CA C 57.487 0.345 1 117 255 43 LEU N N 119.835 0.064 1 118 256 44 SER H H 8.364 0.003 1 119 256 44 SER CA C 62.648 0.345 1 120 256 44 SER N N 114.667 0.064 1 121 257 45 ASN H H 8.038 0.003 1 122 257 45 ASN CA C 56.344 0.345 1 123 257 45 ASN N N 121.918 0.064 1 124 258 46 PHE H H 7.712 0.003 1 125 258 46 PHE CA C 61.774 0.345 1 126 258 46 PHE N N 122.043 0.064 1 127 259 47 LYS H H 8.506 0.003 1 128 259 47 LYS CA C 59.813 0.345 1 129 259 47 LYS N N 117.163 0.064 1 130 260 48 THR H H 8.338 0.003 1 131 260 48 THR CA C 66.543 0.345 1 132 260 48 THR N N 116.642 0.064 1 133 261 49 ALA H H 7.672 0.003 1 134 261 49 ALA CA C 54.994 0.345 1 135 261 49 ALA N N 124.597 0.064 1 136 262 50 ALA H H 7.284 0.003 1 137 262 50 ALA CA C 53.943 0.345 1 138 262 50 ALA N N 119.111 0.064 1 139 263 51 GLU H H 6.998 0.003 1 140 263 51 GLU CA C 58.774 0.345 1 141 263 51 GLU N N 113.822 0.064 1 142 264 52 SER H H 7.507 0.003 1 143 264 52 SER CA C 60.789 0.345 1 144 264 52 SER N N 112.033 0.064 1 145 265 53 PHE H H 7.188 0.003 1 146 265 53 PHE CA C 57.066 0.345 1 147 265 53 PHE N N 115.949 0.064 1 148 266 54 LYS H H 7.356 0.003 1 149 266 54 LYS CA C 58.888 0.345 1 150 266 54 LYS N N 123.440 0.064 1 151 267 55 GLY H H 9.633 0.003 1 152 267 55 GLY CA C 45.590 0.345 1 153 267 55 GLY N N 115.080 0.064 1 154 268 56 LYS H H 8.353 0.003 1 155 268 56 LYS CA C 56.068 0.345 1 156 268 56 LYS N N 118.885 0.064 1 157 269 57 ILE H H 7.862 0.003 1 158 269 57 ILE CA C 60.430 0.345 1 159 269 57 ILE N N 116.447 0.064 1 160 270 58 LEU H H 8.423 0.003 1 161 270 58 LEU CA C 54.587 0.345 1 162 270 58 LEU N N 130.561 0.064 1 163 271 59 PHE H H 9.296 0.003 1 164 271 59 PHE CA C 56.504 0.345 1 165 271 59 PHE N N 130.419 0.064 1 166 272 60 ILE H H 9.137 0.003 1 167 272 60 ILE CA C 59.000 0.345 1 168 272 60 ILE N N 123.727 0.064 1 169 273 61 PHE H H 8.868 0.003 1 170 273 61 PHE CA C 54.653 0.345 1 171 273 61 PHE N N 122.206 0.064 1 172 274 62 ILE H H 8.789 0.003 1 173 274 62 ILE CA C 59.883 0.345 1 174 274 62 ILE N N 121.086 0.064 1 175 275 63 ASP H H 8.500 0.003 1 176 275 63 ASP CA C 52.551 0.345 1 177 275 63 ASP N N 123.507 0.064 1 178 276 64 SER H H 7.454 0.003 1 179 276 64 SER CA C 60.513 0.345 1 180 276 64 SER N N 123.930 0.064 1 181 277 65 ASP H H 8.315 0.003 1 182 277 65 ASP CA C 55.710 0.345 1 183 277 65 ASP N N 118.964 0.064 1 184 278 66 HIS H H 7.282 0.003 1 185 278 66 HIS CA C 58.410 0.345 1 186 278 66 HIS N N 121.464 0.064 1 187 279 67 THR H H 8.859 0.003 1 188 279 67 THR CA C 65.783 0.345 1 189 279 67 THR N N 127.641 0.064 1 190 280 68 ASP H H 11.157 0.003 1 191 280 68 ASP CA C 56.759 0.345 1 192 280 68 ASP N N 125.193 0.064 1 193 281 69 ASN H H 8.031 0.003 1 194 281 69 ASN CA C 52.721 0.345 1 195 281 69 ASN N N 115.320 0.064 1 196 282 70 GLN H H 7.620 0.003 1 197 282 70 GLN CA C 59.518 0.345 1 198 282 70 GLN N N 120.210 0.064 1 199 283 71 ARG H H 7.670 0.003 1 200 283 71 ARG CA C 55.891 0.345 1 201 283 71 ARG N N 118.233 0.064 1 202 284 72 ILE H H 8.102 0.003 1 203 284 72 ILE CA C 64.207 0.345 1 204 284 72 ILE N N 120.850 0.064 1 205 285 73 LEU H H 7.526 0.003 1 206 285 73 LEU CA C 60.587 0.345 1 207 285 73 LEU N N 122.376 0.064 1 208 286 74 GLU H H 8.040 0.003 1 209 286 74 GLU CA C 59.305 0.345 1 210 286 74 GLU N N 117.373 0.064 1 211 287 75 PHE H H 8.432 0.003 1 212 287 75 PHE CA C 58.312 0.345 1 213 287 75 PHE N N 122.409 0.064 1 214 288 76 PHE H H 7.572 0.003 1 215 288 76 PHE CA C 59.996 0.034 1 216 288 76 PHE N N 112.764 0.064 1 217 289 77 GLY H H 8.025 0.003 1 218 289 77 GLY CA C 46.721 0.345 1 219 289 77 GLY N N 110.914 0.064 1 220 290 78 LEU H H 7.815 0.003 1 221 290 78 LEU N N 121.223 0.064 1 222 291 79 LYS H H 8.207 0.003 1 223 291 79 LYS CA C 54.039 0.345 1 224 291 79 LYS N N 119.198 0.064 1 225 292 80 LYS H H 9.150 0.003 1 226 292 80 LYS CA C 61.143 0.345 1 227 292 80 LYS N N 124.515 0.064 1 228 293 81 GLU H H 9.465 0.003 1 229 293 81 GLU CA C 58.747 0.345 1 230 293 81 GLU N N 116.490 0.064 1 231 294 82 GLU H H 7.666 0.003 1 232 294 82 GLU CA C 53.213 0.345 1 233 294 82 GLU N N 117.826 0.064 1 234 295 83 CYS H H 7.112 0.003 1 235 295 83 CYS CA C 58.405 0.345 1 236 295 83 CYS N N 117.800 0.064 1 237 297 85 ALA H H 8.442 0.003 1 238 297 85 ALA CA C 51.660 0.345 1 239 297 85 ALA N N 123.199 0.064 1 240 298 86 VAL H H 8.676 0.003 1 241 298 86 VAL CA C 59.443 0.345 1 242 298 86 VAL N N 118.191 0.064 1 243 299 87 ARG H H 9.006 0.003 1 244 299 87 ARG CA C 53.148 0.345 1 245 299 87 ARG N N 123.276 0.064 1 246 300 88 LEU H H 8.804 0.003 1 247 300 88 LEU CA C 54.439 0.345 1 248 300 88 LEU N N 125.674 0.064 1 249 301 89 ILE H H 9.682 0.003 1 250 301 89 ILE CA C 58.265 0.345 1 251 301 89 ILE N N 122.053 0.064 1 252 302 90 THR H H 8.892 0.003 1 253 302 90 THR CA C 59.027 0.345 1 254 302 90 THR N N 113.685 0.064 1 255 303 91 LEU H H 8.661 0.003 1 256 303 91 LEU CA C 54.479 0.345 1 257 303 91 LEU N N 124.833 0.064 1 258 304 92 GLU H H 7.552 0.003 1 259 304 92 GLU CA C 56.477 0.345 1 260 304 92 GLU N N 123.524 0.064 1 261 305 93 GLU H H 8.571 0.003 1 262 305 93 GLU CA C 59.354 0.345 1 263 306 94 GLU H H 7.959 0.003 1 264 306 94 GLU CA C 54.688 0.345 1 265 306 94 GLU N N 116.072 0.064 1 266 307 95 MET H H 9.105 0.003 1 267 307 95 MET CA C 56.470 0.345 1 268 307 95 MET N N 125.240 0.064 1 269 308 96 THR H H 8.414 0.003 1 270 308 96 THR CA C 62.091 0.345 1 271 308 96 THR N N 121.297 0.064 1 272 309 97 LYS H H 8.787 0.003 1 273 309 97 LYS CA C 54.431 0.345 1 274 309 97 LYS N N 123.623 0.064 1 275 310 98 TYR H H 9.620 0.003 1 276 310 98 TYR CA C 57.575 0.345 1 277 310 98 TYR N N 120.029 0.064 1 278 311 99 LYS H H 9.303 0.003 1 279 311 99 LYS CA C 52.692 0.345 1 280 311 99 LYS N N 122.561 0.064 1 281 313 101 GLU H H 9.093 0.003 1 282 313 101 GLU CA C 57.594 0.345 1 283 313 101 GLU N N 119.485 0.064 1 284 314 102 SER H H 7.585 0.003 1 285 314 102 SER CA C 56.457 0.345 1 286 314 102 SER N N 112.072 0.064 1 287 315 103 GLU H H 8.805 0.003 1 288 315 103 GLU CA C 56.245 0.345 1 289 316 104 GLU H H 8.021 0.003 1 290 316 104 GLU CA C 57.754 0.345 1 291 316 104 GLU N N 120.801 0.064 1 292 317 105 LEU H H 8.701 0.003 1 293 317 105 LEU CA C 53.144 0.345 1 294 317 105 LEU N N 125.227 0.064 1 295 318 106 THR H H 6.794 0.003 1 296 318 106 THR CA C 59.511 0.345 1 297 318 106 THR N N 107.901 0.064 1 298 319 107 ALA H H 9.371 0.003 1 299 319 107 ALA CA C 55.944 0.345 1 300 319 107 ALA N N 125.644 0.064 1 301 320 108 GLU H H 9.417 0.003 1 302 320 108 GLU CA C 60.373 0.345 1 303 320 108 GLU N N 118.400 0.064 1 304 321 109 ARG H H 7.739 0.003 1 305 321 109 ARG CA C 57.860 0.345 1 306 321 109 ARG N N 119.891 0.064 1 307 322 110 ILE H H 8.566 0.003 1 308 322 110 ILE CA C 65.423 0.345 1 309 323 111 THR H H 8.589 0.003 1 310 323 111 THR CA C 67.726 0.345 1 311 323 111 THR N N 117.034 0.064 1 312 324 112 GLU H H 8.117 0.003 1 313 324 112 GLU CA C 59.986 0.345 1 314 324 112 GLU N N 121.738 0.064 1 315 325 113 PHE H H 7.969 0.003 1 316 325 113 PHE CA C 59.500 0.345 1 317 325 113 PHE N N 119.892 0.064 1 318 326 114 CYS H H 7.690 0.003 1 319 326 114 CYS CA C 64.318 0.345 1 320 326 114 CYS N N 115.992 0.064 1 321 327 115 HIS H H 8.621 0.003 1 322 327 115 HIS CA C 60.479 0.345 1 323 327 115 HIS N N 118.145 0.064 1 324 328 116 ARG H H 8.827 0.003 1 325 328 116 ARG N N 119.331 0.064 1 326 329 117 PHE H H 8.406 0.003 1 327 329 117 PHE CA C 59.547 0.345 1 328 329 117 PHE N N 121.087 0.064 1 329 330 118 LEU H H 8.195 0.003 1 330 330 118 LEU CA C 57.450 0.345 1 331 330 118 LEU N N 124.806 0.064 1 332 331 119 GLU H H 7.731 0.003 1 333 331 119 GLU CA C 56.056 0.345 1 334 331 119 GLU N N 116.511 0.064 1 335 332 120 GLY H H 7.778 0.003 1 336 332 120 GLY CA C 46.543 0.345 1 337 332 120 GLY N N 108.571 0.064 1 338 333 121 LYS H H 8.040 0.003 1 339 333 121 LYS CA C 56.291 0.345 1 340 333 121 LYS N N 116.586 0.064 1 341 334 122 ILE H H 8.028 0.003 1 342 334 122 ILE CA C 58.683 0.345 1 343 334 122 ILE N N 119.355 0.064 1 344 335 123 LYS H H 8.873 0.003 1 345 335 123 LYS CA C 54.683 0.345 1 346 335 123 LYS N N 129.335 0.064 1 347 337 125 HIS H H 8.468 0.003 1 348 337 125 HIS CA C 55.189 0.345 1 349 337 125 HIS N N 120.194 0.064 1 350 338 126 LEU H H 8.372 0.003 1 351 338 126 LEU N N 126.039 0.064 1 352 339 127 MET H H 8.340 0.003 1 353 339 127 MET N N 120.765 0.064 1 354 340 128 SER H H 8.254 0.003 1 355 340 128 SER N N 116.455 0.064 1 356 341 129 GLN H H 8.002 0.003 1 357 341 129 GLN CA C 57.722 0.345 1 358 341 129 GLN N N 120.298 0.064 1 359 342 130 GLU H H 8.314 0.003 1 360 342 130 GLU N N 120.874 0.064 1 361 343 131 LEU H H 8.259 0.003 1 362 343 131 LEU CA C 52.958 0.345 1 363 343 131 LEU N N 124.976 0.064 1 364 345 133 GLU H H 8.564 0.003 1 365 345 133 GLU CA C 57.153 0.345 1 366 345 133 GLU N N 120.705 0.064 1 367 346 134 ASP H H 8.338 0.003 1 368 346 134 ASP CA C 54.052 0.345 1 369 346 134 ASP N N 119.191 0.064 1 370 347 135 TRP H H 7.808 0.003 1 371 347 135 TRP CA C 58.015 0.345 1 372 347 135 TRP N N 120.812 0.064 1 373 348 136 ASP H H 8.053 0.003 1 374 348 136 ASP CA C 53.865 0.345 1 375 348 136 ASP N N 120.742 0.064 1 376 349 137 LYS H H 7.633 0.003 1 377 349 137 LYS CA C 56.065 0.345 1 378 349 137 LYS N N 120.630 0.064 1 379 350 138 GLN H H 8.233 0.003 1 380 350 138 GLN CA C 53.457 0.345 1 381 350 138 GLN N N 123.335 0.064 1 382 352 140 VAL H H 8.373 0.003 1 383 352 140 VAL N N 122.157 0.064 1 stop_ save_