data_4936 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; 1H, 13C and 15N chemical shift assignments of the outer membrane protein OmpX from E.coli in DHPC micelles ; _BMRB_accession_number 4936 _BMRB_flat_file_name bmr4936.str _Entry_type original _Submission_date 2001-01-09 _Accession_date 2001-01-09 _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 Fernandez Cesar . . 2 Adeishvili Koba . . 3 Wuthrich Kurt . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 140 "13C chemical shifts" 407 "15N chemical shifts" 140 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2005-09-22 update author 'update of chemical shift table' 2001-07-31 original author 'original release' stop_ save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; Transverse relaxation-optimized NMR spectroscopy with the outer membrane protein OmpX in dihexanoyl phosphatidylcholine micelles. ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 11226244 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Fernandez Cesar . . 2 Adeishvili Koba . . 3 Wuthrich Kurt . . stop_ _Journal_abbreviation 'Proc. Natl. Acad. Sci. U. S. A.' _Journal_name_full 'Proceedings of the National Academy of Science of the USA' _Journal_volume 98 _Journal_issue 5 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 2358 _Page_last 2363 _Year 2001 _Details ; The data reported here represent the 1H, 13C and 15N chemical shifts of 2H/13C/15N labeled OmpX in DHPC micelles obtained using TROSY-type triple resonance experiments. The size of the OmpX/DHPC particles is of about 60 kDa. ; loop_ _Keyword 'membrane proteins' OmpX TROSY 'NMR spectroscopy' 'sequential resonance assignment' 'isotope labeling' stop_ save_ ####################################### # Cited references within the entry # ####################################### save_ref_1 _Saveframe_category citation _Citation_full . _Citation_title ; The program XEASY for computer-supported NMR spectral analysis of biological macromolecules. ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID ? loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Bartels C. . . 2 Xia T.-H. . . 3 Billeter Martin . . 4 Guntert Peter . . 5 Wuthrich Kurt . . stop_ _Journal_abbreviation 'J. Biomol. NMR' _Journal_name_full . _Journal_volume 6 _Journal_issue . _Journal_CSD . _Book_title . _Book_chapter_title . _Book_volume . _Book_series . _Book_publisher . _Book_publisher_city . _Book_ISBN . _Conference_title . _Conference_site . _Conference_state_province . _Conference_country . _Conference_start_date . _Conference_end_date . _Conference_abstract_number . _Thesis_institution . _Thesis_institution_city . _Thesis_institution_country . _Page_first 1 _Page_last 10 _Year 1995 _Details . save_ ################################## # Molecular system description # ################################## save_system_OmpX _Saveframe_category molecular_system _Mol_system_name 'Outer membrane protein X in DHPC micelles' _Abbreviation_common OmpX _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label OmpX $OmpX stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state monomer _System_paramagnetic no _System_thiol_state 'not present' loop_ _Biological_function ; OmpX belongs to a family of highly conserved bacterial proteins that promote bacterial adhesion to mammalian cells and entry into them. Moreover, these proteins have a role in the resistance against attack by the human complement system. ; stop_ _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_OmpX _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'Outer membrane protein X' _Name_variant H100N _Abbreviation_common OmpX _Molecular_mass . _Mol_thiol_state 'not present' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 148 _Mol_residue_sequence ; ATSTVTGGYAQSDAQGQMNK MGGFNLKYRYEEDNSPLGVI GSFTYTEKSRTASSGDYNKN QYYGITAGPAYRINDWASIY GVVGVGYGKFQTTEYPTYKH DTTDYGFSYGAGLQFNPMEN VALDFSYEQSRIRSVDVGTW IAGVGYRF ; loop_ _Residue_seq_code _Residue_label 1 ALA 2 THR 3 SER 4 THR 5 VAL 6 THR 7 GLY 8 GLY 9 TYR 10 ALA 11 GLN 12 SER 13 ASP 14 ALA 15 GLN 16 GLY 17 GLN 18 MET 19 ASN 20 LYS 21 MET 22 GLY 23 GLY 24 PHE 25 ASN 26 LEU 27 LYS 28 TYR 29 ARG 30 TYR 31 GLU 32 GLU 33 ASP 34 ASN 35 SER 36 PRO 37 LEU 38 GLY 39 VAL 40 ILE 41 GLY 42 SER 43 PHE 44 THR 45 TYR 46 THR 47 GLU 48 LYS 49 SER 50 ARG 51 THR 52 ALA 53 SER 54 SER 55 GLY 56 ASP 57 TYR 58 ASN 59 LYS 60 ASN 61 GLN 62 TYR 63 TYR 64 GLY 65 ILE 66 THR 67 ALA 68 GLY 69 PRO 70 ALA 71 TYR 72 ARG 73 ILE 74 ASN 75 ASP 76 TRP 77 ALA 78 SER 79 ILE 80 TYR 81 GLY 82 VAL 83 VAL 84 GLY 85 VAL 86 GLY 87 TYR 88 GLY 89 LYS 90 PHE 91 GLN 92 THR 93 THR 94 GLU 95 TYR 96 PRO 97 THR 98 TYR 99 LYS 100 HIS 101 ASP 102 THR 103 THR 104 ASP 105 TYR 106 GLY 107 PHE 108 SER 109 TYR 110 GLY 111 ALA 112 GLY 113 LEU 114 GLN 115 PHE 116 ASN 117 PRO 118 MET 119 GLU 120 ASN 121 VAL 122 ALA 123 LEU 124 ASP 125 PHE 126 SER 127 TYR 128 GLU 129 GLN 130 SER 131 ARG 132 ILE 133 ARG 134 SER 135 VAL 136 ASP 137 VAL 138 GLY 139 THR 140 TRP 141 ILE 142 ALA 143 GLY 144 VAL 145 GLY 146 TYR 147 ARG 148 PHE stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-01-28 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 15201 Outer_membrane_protein_X 100.00 148 99.32 100.00 1.77e-101 BMRB 18796 OmpX 100.00 148 99.32 100.00 1.77e-101 BMRB 18797 OmpX 100.00 148 99.32 100.00 1.77e-101 PDB 1ORM "Nmr Fold Of The Outer Membrane Protein Ompx In Dhpc Micelles" 99.32 148 98.64 100.00 1.38e-99 PDB 1Q9F "Nmr Structure Of The Outer Membrane Protein Ompx In Dhpc Micelles" 100.00 148 98.65 100.00 2.71e-100 PDB 1Q9G "Nmr Structure Of The Outer Membrane Protein Ompx In Dhpc Micelles" 100.00 148 98.65 100.00 2.71e-100 PDB 1QJ8 "Crystal Structure Of The Outer Membrane Protein Ompx From Escherichia Coli" 100.00 148 98.65 100.00 2.71e-100 PDB 1QJ9 "Crystal Structure Of The Outer Membrane Protein Ompx From Escherichia Coli" 100.00 148 98.65 100.00 2.71e-100 PDB 2M06 "Nmr Structure Of Ompx In Phopspholipid Nanodiscs" 100.00 148 99.32 100.00 1.77e-101 PDB 2M07 "Nmr Structure Of Ompx In Dpc Micelles" 100.00 148 99.32 100.00 1.77e-101 DBJ BAA35486 "outer membrane protein [Escherichia coli str. K-12 substr. W3110]" 100.00 171 99.32 100.00 1.93e-102 DBJ BAB34315 "outer membrane protein X [Escherichia coli O157:H7 str. Sakai]" 100.00 171 99.32 100.00 1.93e-102 DBJ BAG76394 "conserved hypothetical protein [Escherichia coli SE11]" 100.00 171 99.32 100.00 1.93e-102 DBJ BAI24257 "outer membrane protein X [Escherichia coli O26:H11 str. 11368]" 100.00 171 99.32 100.00 1.93e-102 DBJ BAI29701 "outer membrane protein X [Escherichia coli O103:H2 str. 12009]" 100.00 171 99.32 100.00 1.93e-102 EMBL CAP75284 "Outer membrane protein X [Escherichia coli LF82]" 100.00 171 99.32 100.00 1.93e-102 EMBL CAQ31315 "outer membrane protein X [Escherichia coli BL21(DE3)]" 100.00 171 99.32 100.00 1.93e-102 EMBL CAQ97717 "outer membrane protein [Escherichia coli IAI1]" 100.00 171 99.32 100.00 1.93e-102 EMBL CAR02170 "outer membrane protein [Escherichia coli S88]" 100.00 171 99.32 100.00 1.93e-102 EMBL CAR06985 "outer membrane protein [Escherichia coli ED1a]" 100.00 171 99.32 100.00 1.93e-102 GB AAA21856 "similar to outer membrane protein X from Enterobacter cloacae, Swiss-Prot Accession Number P25253; ORF2, partial [Escherichia c" 77.03 137 99.12 100.00 5.72e-75 GB AAA66329 "outer membrane protein [Escherichia coli str. K-12 substr. MG1655]" 100.00 171 99.32 100.00 1.93e-102 GB AAC73901 "outer membrane protein X [Escherichia coli str. K-12 substr. MG1655]" 100.00 171 99.32 100.00 1.93e-102 GB AAG55186 "outer membrane protein X [Escherichia coli O157:H7 str. EDL933]" 100.00 171 99.32 100.00 1.93e-102 GB AAN42399 "outer membrane protein X [Shigella flexneri 2a str. 301]" 100.00 171 99.32 100.00 1.93e-102 REF NP_286578 "outer membrane protein X [Escherichia coli O157:H7 str. EDL933]" 100.00 171 99.32 100.00 1.93e-102 REF NP_308919 "outer membrane protein X [Escherichia coli O157:H7 str. Sakai]" 100.00 171 99.32 100.00 1.93e-102 REF NP_415335 "outer membrane protein X [Escherichia coli str. K-12 substr. MG1655]" 100.00 171 99.32 100.00 1.93e-102 REF NP_706692 "outer membrane protein X [Shigella flexneri 2a str. 301]" 100.00 171 99.32 100.00 1.93e-102 REF NP_752830 "outer membrane protein X [Escherichia coli CFT073]" 100.00 173 99.32 100.00 1.71e-102 SP P0A917 "RecName: Full=Outer membrane protein X; Flags: Precursor [Escherichia coli K-12]" 100.00 171 99.32 100.00 1.93e-102 SP P0A918 "RecName: Full=Outer membrane protein X; Flags: Precursor [Escherichia coli CFT073]" 100.00 171 99.32 100.00 1.93e-102 SP P0A919 "RecName: Full=Outer membrane protein X; Flags: Precursor [Escherichia coli O157:H7]" 100.00 171 99.32 100.00 1.93e-102 SP P0A920 "RecName: Full=Outer membrane protein X; Flags: Precursor [Shigella flexneri]" 100.00 171 99.32 100.00 1.93e-102 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $OmpX 'Escherichia coli' 562 Eubacteria . Escherichia coli stop_ save_ ######################### # Experimental source # ######################### save_experimental_source _Saveframe_category experimental_source loop_ _Mol_label _Production_method _Host_organism_name_common _Genus _Species _Strain _Vector_type _Vector_name _Details $OmpX 'recombinant technology' 'E. coli' Escherichia coli BL21(DE3)pLyS plasmid pET3b-OmpX 'Protein obtained in inclusion bodies' stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample _Saveframe_category sample _Sample_type micelles _Details 'the 2H labeling range is 85-100%' loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $OmpX 2.0 mM '[U-98% 13C; U-98% 15N; U-2H]' DHPC 300 mM . H2O 97 % . D2O 3 % . KPO4 20 mM . NaCl 100 mM . stop_ save_ ############################ # Computer software used # ############################ save_XEASY _Saveframe_category software _Name XEASY _Version . _Details . _Citation_label $ref_1 save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model DRX _Field_strength 750 _Details . save_ ############################# # NMR applied experiments # ############################# save_HNCA_1 _Saveframe_category NMR_applied_experiment _Experiment_name HNCA _Sample_label $sample save_ save_HN(CO)CA_2 _Saveframe_category NMR_applied_experiment _Experiment_name HN(CO)CA _Sample_label $sample save_ save_HNCACB_3 _Saveframe_category NMR_applied_experiment _Experiment_name HNCACB _Sample_label $sample save_ save_3D_[1H,1H]-NOESY-[15N,1H]-TROSY_4 _Saveframe_category NMR_applied_experiment _Experiment_name '3D [1H,1H]-NOESY-[15N,1H]-TROSY' _Sample_label $sample save_ save_NMR_spec_expt__0_1 _Saveframe_category NMR_applied_experiment _Experiment_name HNCA _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_2 _Saveframe_category NMR_applied_experiment _Experiment_name HN(CO)CA _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_3 _Saveframe_category NMR_applied_experiment _Experiment_name HNCACB _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_4 _Saveframe_category NMR_applied_experiment _Experiment_name '3D [1H,1H]-NOESY-[15N,1H]-TROSY' _BMRB_pulse_sequence_accession_number . _Details . save_ ####################### # Sample conditions # ####################### save_exp_conditions _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 6.8 0.2 pH temperature 303 1 K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference _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 H 1 'methyl protons' ppm 0.0 internal direct . . . 1.0 DSS N 15 'methyl protons' ppm 0.0 . indirect . . . 0.101329118 DSS C 13 'methyl protons' ppm 0.0 . indirect . . . 0.251449530 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_chemical_shifts _Saveframe_category assigned_chemical_shifts _Details . loop_ _Sample_label $sample stop_ _Sample_conditions_label $exp_conditions _Chem_shift_reference_set_label $chemical_shift_reference _Mol_system_component_name OmpX _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 ALA CA C 51.7 0.3 1 2 . 1 ALA CB C 19.6 0.3 1 3 . 1 ALA C C 174.0 0.3 1 4 . 2 THR N N 112.9 0.3 1 5 . 2 THR H H 8.28 0.03 1 6 . 2 THR CA C 60.6 0.3 1 7 . 2 THR CB C 71.6 0.3 1 8 . 2 THR C C 173.4 0.3 1 9 . 3 SER N N 120.9 0.3 1 10 . 3 SER H H 8.86 0.03 1 11 . 3 SER CA C 56.5 0.3 1 12 . 3 SER CB C 65.0 0.3 1 13 . 3 SER C C 175.5 0.3 1 14 . 4 THR N N 116.8 0.3 1 15 . 4 THR H H 8.55 0.03 1 16 . 4 THR CA C 60.9 0.3 1 17 . 4 THR CB C 70.2 0.3 1 18 . 4 THR C C 174.5 0.3 1 19 . 5 VAL N N 128.8 0.3 1 20 . 5 VAL H H 8.59 0.03 1 21 . 5 VAL CA C 59.3 0.3 1 22 . 5 VAL CB C 33.5 0.3 1 23 . 5 VAL C C 174.5 0.3 1 24 . 6 THR N N 115.3 0.3 1 25 . 6 THR H H 8.70 0.03 1 26 . 6 THR CA C 58.3 0.3 1 27 . 6 THR CB C 70.5 0.3 1 28 . 6 THR C C 172.8 0.3 1 29 . 7 GLY N N 105.8 0.3 1 30 . 7 GLY H H 8.61 0.03 1 31 . 7 GLY CA C 44.1 0.3 1 32 . 7 GLY C C 172.3 0.3 1 33 . 8 GLY N N 106.4 0.3 1 34 . 8 GLY H H 9.00 0.03 1 35 . 8 GLY CA C 45.5 0.3 1 36 . 8 GLY C C 172.9 0.3 1 37 . 9 TYR N N 121.0 0.3 1 38 . 9 TYR H H 8.19 0.03 1 39 . 9 TYR CA C 56.8 0.3 1 40 . 9 TYR CB C 40.5 0.3 1 41 . 9 TYR C C 172.5 0.3 1 42 . 10 ALA N N 126.6 0.3 1 43 . 10 ALA H H 6.97 0.03 1 44 . 10 ALA CA C 48.2 0.3 1 45 . 10 ALA CB C 22.2 0.3 1 46 . 10 ALA C C 174.2 0.3 1 47 . 11 GLN N N 119.3 0.3 1 48 . 11 GLN H H 8.29 0.03 1 49 . 11 GLN CA C 53.7 0.3 1 50 . 11 GLN CB C 32.5 0.3 1 51 . 11 GLN C C 175.3 0.3 1 52 . 12 SER N N 124.1 0.3 1 53 . 12 SER H H 9.22 0.03 1 54 . 12 SER CA C 56.9 0.3 1 55 . 12 SER CB C 63.6 0.3 1 56 . 12 SER C C 172.5 0.3 1 57 . 13 ASP N N 123.9 0.3 1 58 . 13 ASP H H 9.08 0.03 1 59 . 13 ASP CA C 52.5 0.3 1 60 . 13 ASP CB C 41.9 0.3 1 61 . 13 ASP C C 174.6 0.3 1 62 . 14 ALA N N 127.7 0.3 1 63 . 14 ALA H H 8.55 0.03 1 64 . 14 ALA CA C 49.8 0.3 1 65 . 14 ALA CB C 19.4 0.3 1 66 . 14 ALA C C 176.0 0.3 1 67 . 15 GLN N N 122.4 0.3 1 68 . 15 GLN H H 8.31 0.03 1 69 . 15 GLN CA C 56.8 0.3 1 70 . 15 GLN CB C 27.9 0.3 1 71 . 15 GLN C C 176.5 0.3 1 72 . 16 GLY N N 112.2 0.3 1 73 . 16 GLY H H 8.59 0.03 1 74 . 16 GLY CA C 44.9 0.3 1 75 . 16 GLY C C 174.4 0.3 1 76 . 17 GLN N N 119.3 0.3 1 77 . 17 GLN H H 8.08 0.03 1 78 . 17 GLN CA C 54.6 0.3 1 79 . 17 GLN CB C 28.4 0.3 1 80 . 17 GLN C C 176.1 0.3 1 81 . 18 MET N N 119.8 0.3 1 82 . 18 MET H H 8.37 0.03 1 83 . 18 MET CA C 55.7 0.3 1 84 . 18 MET CB C 31.8 0.3 1 85 . 18 MET C C 175.4 0.3 1 86 . 19 ASN N N 117.9 0.3 1 87 . 19 ASN H H 7.99 0.03 1 88 . 19 ASN CA C 52.3 0.3 1 89 . 19 ASN CB C 39.4 0.3 1 90 . 19 ASN C C 174.4 0.3 1 91 . 20 LYS N N 120.8 0.3 1 92 . 20 LYS H H 8.34 0.03 1 93 . 20 LYS CA C 55.7 0.3 1 94 . 20 LYS CB C 31.9 0.3 1 95 . 20 LYS C C 176.3 0.3 1 96 . 21 MET N N 120.0 0.3 1 97 . 21 MET H H 8.48 0.03 1 98 . 21 MET CA C 54.5 0.3 1 99 . 21 MET CB C 34.6 0.3 1 100 . 21 MET C C 175.0 0.3 1 101 . 22 GLY N N 110.9 0.3 1 102 . 22 GLY H H 8.37 0.03 1 103 . 22 GLY CA C 43.6 0.3 1 104 . 22 GLY C C 175.0 0.3 1 105 . 23 GLY N N 110.6 0.3 1 106 . 23 GLY H H 8.20 0.03 1 107 . 23 GLY CA C 45.9 0.3 1 108 . 23 GLY C C 172.4 0.3 1 109 . 24 PHE N N 121.9 0.3 1 110 . 24 PHE H H 9.31 0.03 1 111 . 24 PHE CA C 54.6 0.3 1 112 . 24 PHE CB C 43.0 0.3 1 113 . 24 PHE C C 169.6 0.3 1 114 . 25 ASN N N 117.9 0.3 1 115 . 25 ASN H H 8.39 0.03 1 116 . 25 ASN CA C 50.6 0.3 1 117 . 25 ASN CB C 42.1 0.3 1 118 . 25 ASN C C 172.1 0.3 1 119 . 26 LEU N N 125.5 0.3 1 120 . 26 LEU H H 9.26 0.03 1 121 . 26 LEU CA C 53.1 0.3 1 122 . 26 LEU CB C 46.2 0.3 1 123 . 26 LEU C C 175.4 0.3 1 124 . 27 LYS N N 117.6 0.3 1 125 . 27 LYS H H 8.77 0.03 1 126 . 27 LYS CA C 55.0 0.3 1 127 . 27 LYS CB C 36.3 0.3 1 128 . 27 LYS C C 174.7 0.3 1 129 . 28 TYR N N 120.7 0.3 1 130 . 28 TYR H H 8.33 0.03 1 131 . 28 TYR CA C 55.7 0.3 1 132 . 28 TYR CB C 41.6 0.3 1 133 . 28 TYR C C 172.3 0.3 1 134 . 29 ARG N N 129.6 0.3 1 135 . 29 ARG H H 8.70 0.03 1 136 . 29 ARG CA C 52.7 0.3 1 137 . 29 ARG CB C 33.9 0.3 1 138 . 29 ARG C C 172.5 0.3 1 139 . 30 TYR N N 126.3 0.3 1 140 . 30 TYR H H 8.82 0.03 1 141 . 30 TYR CA C 56.5 0.3 1 142 . 30 TYR CB C 42.0 0.3 1 143 . 30 TYR C C 174.8 0.3 1 144 . 31 GLU N N 128.0 0.3 1 145 . 31 GLU H H 8.19 0.03 1 146 . 31 GLU CA C 54.5 0.3 1 147 . 31 GLU CB C 31.9 0.3 1 148 . 31 GLU C C 174.2 0.3 1 149 . 32 GLU N N 121.2 0.3 1 150 . 32 GLU H H 8.99 0.03 1 151 . 32 GLU CA C 54.1 0.3 1 152 . 32 GLU CB C 29.9 0.3 1 153 . 32 GLU C C 176.6 0.3 1 154 . 33 ASP N N 120.9 0.3 1 155 . 33 ASP H H 8.51 0.03 1 156 . 33 ASP CA C 55.4 0.3 1 157 . 33 ASP CB C 39.8 0.3 1 158 . 33 ASP C C 176.7 0.3 1 159 . 34 ASN N N 114.6 0.3 1 160 . 34 ASN H H 8.37 0.03 1 161 . 34 ASN CA C 53.1 0.3 1 162 . 34 ASN CB C 37.4 0.3 1 163 . 34 ASN C C 174.1 0.3 1 164 . 35 SER N N 112.4 0.3 1 165 . 35 SER H H 7.14 0.03 1 166 . 35 SER CA C 54.0 0.3 1 167 . 35 SER CB C 64.4 0.3 1 168 . 36 PRO CA C 62.9 0.3 1 169 . 36 PRO CB C 31.2 0.3 1 170 . 36 PRO C C 175.4 0.3 1 171 . 37 LEU N N 122.8 0.3 1 172 . 37 LEU H H 7.84 0.03 1 173 . 37 LEU CA C 53.5 0.3 1 174 . 37 LEU CB C 43.1 0.3 1 175 . 37 LEU C C 176.2 0.3 1 176 . 38 GLY N N 116.5 0.3 1 177 . 38 GLY H H 8.97 0.03 1 178 . 38 GLY CA C 44.3 0.3 1 179 . 38 GLY C C 172.7 0.3 1 180 . 39 VAL N N 116.2 0.3 1 181 . 39 VAL H H 7.88 0.03 1 182 . 39 VAL CA C 58.7 0.3 1 183 . 39 VAL CB C 35.4 0.3 1 184 . 39 VAL C C 171.7 0.3 1 185 . 40 ILE N N 124.5 0.3 1 186 . 40 ILE H H 9.05 0.03 1 187 . 40 ILE CA C 58.2 0.3 1 188 . 40 ILE CB C 43.7 0.3 1 189 . 40 ILE C C 171.6 0.3 1 190 . 41 GLY N N 111.4 0.3 1 191 . 41 GLY H H 8.85 0.03 1 192 . 41 GLY CA C 42.8 0.3 1 193 . 41 GLY C C 171.9 0.3 1 194 . 42 SER N N 116.5 0.3 1 195 . 42 SER H H 9.08 0.03 1 196 . 42 SER CA C 55.9 0.3 1 197 . 42 SER CB C 62.3 0.3 1 198 . 42 SER C C 171.9 0.3 1 199 . 43 PHE N N 128.9 0.3 1 200 . 43 PHE H H 9.17 0.03 1 201 . 43 PHE CA C 55.8 0.3 1 202 . 43 PHE CB C 42.7 0.3 1 203 . 43 PHE C C 172.6 0.3 1 204 . 44 THR N N 126.3 0.3 1 205 . 44 THR H H 8.71 0.03 1 206 . 44 THR CA C 60.0 0.3 1 207 . 44 THR CB C 69.7 0.3 1 208 . 44 THR C C 171.1 0.3 1 209 . 45 TYR N N 125.4 0.3 1 210 . 45 TYR H H 8.08 0.03 1 211 . 45 TYR CA C 55.4 0.3 1 212 . 45 TYR CB C 40.7 0.3 1 213 . 45 TYR C C 173.8 0.3 1 214 . 46 THR N N 117.2 0.3 1 215 . 46 THR H H 8.50 0.03 1 216 . 46 THR CA C 58.5 0.3 1 217 . 46 THR CB C 71.1 0.3 1 218 . 46 THR C C 171.6 0.3 1 219 . 47 GLU N N 111.6 0.3 1 220 . 47 GLU H H 8.13 0.03 1 221 . 47 GLU CA C 54.1 0.3 1 222 . 47 GLU CB C 32.1 0.3 1 223 . 48 LYS CA C 55.9 0.3 1 224 . 48 LYS C C 175.2 0.3 1 225 . 49 SER N N 123.3 0.3 1 226 . 49 SER H H 8.88 0.03 1 227 . 49 SER CA C 58.0 0.3 1 228 . 49 SER CB C 63.7 0.3 1 229 . 49 SER C C 174.1 0.3 1 230 . 50 ARG N N 123.7 0.3 1 231 . 50 ARG H H 8.53 0.03 1 232 . 50 ARG CA C 55.9 0.3 1 233 . 50 ARG CB C 30.6 0.3 1 234 . 50 ARG C C 176.1 0.3 1 235 . 51 THR N N 115.1 0.3 1 236 . 51 THR H H 8.20 0.03 1 237 . 51 THR CA C 61.1 0.3 1 238 . 51 THR CB C 69.2 0.3 1 239 . 51 THR C C 174.4 0.3 1 240 . 52 ALA N N 126.3 0.3 1 241 . 52 ALA H H 8.40 0.03 1 242 . 52 ALA CA C 52.0 0.3 1 243 . 52 ALA CB C 18.8 0.3 1 244 . 52 ALA C C 178.1 0.3 1 245 . 53 SER N N 115.0 0.3 1 246 . 53 SER H H 8.26 0.03 1 247 . 53 SER CA C 58.5 0.3 1 248 . 53 SER CB C 62.5 0.3 1 249 . 53 SER C C 174.8 0.3 1 250 . 54 SER N N 116.7 0.3 1 251 . 54 SER H H 8.02 0.03 1 252 . 54 SER CA C 58.3 0.3 1 253 . 54 SER CB C 62.7 0.3 1 254 . 54 SER C C 175.0 0.3 1 255 . 55 GLY N N 110.7 0.3 1 256 . 55 GLY H H 8.18 0.03 1 257 . 55 GLY CA C 44.7 0.3 1 258 . 55 GLY C C 173.7 0.3 1 259 . 56 ASP N N 120.5 0.3 1 260 . 56 ASP H H 7.84 0.03 1 261 . 56 ASP CA C 53.7 0.3 1 262 . 56 ASP CB C 40.5 0.3 1 263 . 56 ASP C C 175.5 0.3 1 264 . 57 TYR N N 120.8 0.3 1 265 . 57 TYR H H 8.07 0.03 1 266 . 57 TYR CA C 57.1 0.3 1 267 . 57 TYR CB C 37.9 0.3 1 268 . 57 TYR C C 175.5 0.3 1 269 . 58 ASN N N 121.2 0.3 1 270 . 58 ASN H H 8.19 0.03 1 271 . 58 ASN CA C 52.5 0.3 1 272 . 58 ASN CB C 39.1 0.3 1 273 . 58 ASN C C 173.9 0.3 1 274 . 59 LYS N N 120.7 0.3 1 275 . 59 LYS H H 8.11 0.03 1 276 . 59 LYS CA C 55.2 0.3 1 277 . 59 LYS CB C 33.8 0.3 1 278 . 59 LYS C C 171.6 0.3 1 279 . 60 ASN N N 122.1 0.3 1 280 . 60 ASN H H 8.27 0.03 1 281 . 60 ASN CA C 51.8 0.3 1 282 . 60 ASN CB C 39.8 0.3 1 283 . 60 ASN C C 175.2 0.3 1 284 . 61 GLN N N 119.8 0.3 1 285 . 61 GLN H H 8.47 0.03 1 286 . 61 GLN CA C 54.4 0.3 1 287 . 61 GLN CB C 34.9 0.3 1 288 . 61 GLN C C 173.4 0.3 1 289 . 62 TYR N N 122.9 0.3 1 290 . 62 TYR H H 8.55 0.03 1 291 . 62 TYR CA C 56.4 0.3 1 292 . 62 TYR CB C 39.8 0.3 1 293 . 62 TYR C C 171.5 0.3 1 294 . 63 TYR N N 123.1 0.3 1 295 . 63 TYR H H 8.27 0.03 1 296 . 63 TYR CA C 54.3 0.3 1 297 . 63 TYR CB C 41.4 0.3 1 298 . 63 TYR C C 174.0 0.3 1 299 . 64 GLY N N 106.2 0.3 1 300 . 64 GLY H H 8.58 0.03 1 301 . 64 GLY CA C 44.2 0.3 1 302 . 64 GLY C C 174.2 0.3 1 303 . 65 ILE N N 127.9 0.3 1 304 . 65 ILE H H 8.94 0.03 1 305 . 65 ILE CA C 59.7 0.3 1 306 . 65 ILE CB C 39.3 0.3 1 307 . 65 ILE C C 174.4 0.3 1 308 . 66 THR N N 115.3 0.3 1 309 . 66 THR H H 8.75 0.03 1 310 . 66 THR CA C 58.4 0.3 1 311 . 66 THR CB C 72.9 0.3 1 312 . 66 THR C C 172.5 0.3 1 313 . 67 ALA N N 119.1 0.3 1 314 . 67 ALA H H 9.24 0.03 1 315 . 67 ALA CA C 51.4 0.3 1 316 . 67 ALA CB C 22.1 0.3 1 317 . 67 ALA C C 176.5 0.3 1 318 . 68 GLY N N 104.3 0.3 1 319 . 68 GLY H H 8.83 0.03 1 320 . 68 GLY CA C 45.6 0.3 1 321 . 69 PRO CA C 61.0 0.3 1 322 . 69 PRO CB C 32.6 0.3 1 323 . 69 PRO C C 173.6 0.3 1 324 . 70 ALA N N 120.0 0.3 1 325 . 70 ALA H H 7.76 0.03 1 326 . 70 ALA CA C 49.3 0.3 1 327 . 70 ALA CB C 20.8 0.3 1 328 . 70 ALA C C 175.2 0.3 1 329 . 71 TYR N N 125.4 0.3 1 330 . 71 TYR H H 9.64 0.03 1 331 . 71 TYR CA C 55.7 0.3 1 332 . 71 TYR CB C 41.5 0.3 1 333 . 71 TYR C C 173.9 0.3 1 334 . 72 ARG N N 131.0 0.3 1 335 . 72 ARG H H 8.78 0.03 1 336 . 72 ARG CA C 55.7 0.3 1 337 . 72 ARG CB C 29.3 0.3 1 338 . 72 ARG C C 173.9 0.3 1 339 . 73 ILE N N 129.2 0.3 1 340 . 73 ILE H H 8.38 0.03 1 341 . 73 ILE CA C 62.5 0.3 1 342 . 73 ILE C C 176.2 0.3 1 343 . 74 ASN N N 114.6 0.3 1 344 . 74 ASN H H 7.87 0.03 1 345 . 74 ASN CA C 51.6 0.3 1 346 . 74 ASN CB C 36.7 0.3 1 347 . 74 ASN C C 174.6 0.3 1 348 . 75 ASP N N 113.7 0.3 1 349 . 75 ASP H H 8.27 0.03 1 350 . 75 ASP CA C 56.4 0.3 1 351 . 75 ASP CB C 39.5 0.3 1 352 . 75 ASP C C 175.5 0.3 1 353 . 76 TRP N N 113.5 0.3 1 354 . 76 TRP H H 7.96 0.03 1 355 . 76 TRP CA C 55.5 0.3 1 356 . 76 TRP C C 176.1 0.3 1 357 . 77 ALA N N 124.4 0.3 1 358 . 77 ALA H H 7.67 0.03 1 359 . 77 ALA CA C 51.6 0.3 1 360 . 77 ALA CB C 21.2 0.3 1 361 . 77 ALA C C 175.3 0.3 1 362 . 78 SER N N 113.5 0.3 1 363 . 78 SER H H 8.01 0.03 1 364 . 78 SER CA C 57.0 0.3 1 365 . 78 SER CB C 64.9 0.3 1 366 . 78 SER C C 176.1 0.3 1 367 . 79 ILE N N 120.0 0.3 1 368 . 79 ILE H H 8.95 0.03 1 369 . 79 ILE CA C 58.0 0.3 1 370 . 79 ILE CB C 41.9 0.3 1 371 . 79 ILE C C 172.3 0.3 1 372 . 80 TYR N N 119.8 0.3 1 373 . 80 TYR H H 8.22 0.03 1 374 . 80 TYR CA C 55.5 0.3 1 375 . 80 TYR CB C 40.9 0.3 1 376 . 80 TYR C C 172.9 0.3 1 377 . 81 GLY N N 105.5 0.3 1 378 . 81 GLY H H 7.97 0.03 1 379 . 81 GLY CA C 43.8 0.3 1 380 . 81 GLY C C 170.7 0.3 1 381 . 82 VAL N N 110.8 0.3 1 382 . 82 VAL H H 8.43 0.03 1 383 . 82 VAL CA C 57.9 0.3 1 384 . 82 VAL CB C 35.1 0.3 1 385 . 82 VAL C C 174.2 0.3 1 386 . 83 VAL N N 112.8 0.3 1 387 . 83 VAL H H 8.82 0.03 1 388 . 83 VAL CA C 58.7 0.3 1 389 . 83 VAL C C 174.5 0.3 1 390 . 84 GLY N N 108.2 0.3 1 391 . 84 GLY H H 8.45 0.03 1 392 . 84 GLY CA C 46.4 0.3 1 393 . 84 GLY C C 171.2 0.3 1 394 . 85 VAL N N 121.7 0.3 1 395 . 85 VAL H H 8.73 0.03 1 396 . 85 VAL CA C 59.1 0.3 1 397 . 85 VAL CB C 35.6 0.3 1 398 . 85 VAL C C 172.4 0.3 1 399 . 86 GLY N N 113.2 0.3 1 400 . 86 GLY H H 8.85 0.03 1 401 . 86 GLY CA C 43.0 0.3 1 402 . 86 GLY C C 171.9 0.3 1 403 . 87 TYR N N 122.8 0.3 1 404 . 87 TYR H H 9.04 0.03 1 405 . 87 TYR CA C 55.4 0.3 1 406 . 87 TYR CB C 42.3 0.3 1 407 . 87 TYR C C 173.6 0.3 1 408 . 88 GLY N N 111.8 0.3 1 409 . 88 GLY H H 7.89 0.03 1 410 . 88 GLY CA C 44.1 0.3 1 411 . 88 GLY C C 174.1 0.3 1 412 . 89 LYS N N 106.4 0.3 1 413 . 89 LYS H H 8.61 0.03 1 414 . 89 LYS CA C 54.3 0.3 1 415 . 90 PHE CA C 54.9 0.3 1 416 . 90 PHE C C 174.9 0.3 1 417 . 91 GLN N N 121.6 0.3 1 418 . 91 GLN H H 8.27 0.03 1 419 . 91 GLN CA C 55.0 0.3 1 420 . 91 GLN CB C 29.5 0.3 1 421 . 91 GLN C C 175.9 0.3 1 422 . 92 THR N N 116.5 0.3 1 423 . 92 THR H H 8.40 0.03 1 424 . 92 THR CA C 60.6 0.3 1 425 . 92 THR CB C 69.1 0.3 1 426 . 92 THR C C 174.4 0.3 1 427 . 93 THR N N 115.6 0.3 1 428 . 93 THR H H 8.04 0.03 1 429 . 93 THR CA C 61.3 0.3 1 430 . 93 THR CB C 68.7 0.3 1 431 . 93 THR C C 174.4 0.3 1 432 . 94 GLU N N 122.8 0.3 1 433 . 94 GLU H H 8.29 0.03 1 434 . 94 GLU CA C 56.5 0.3 1 435 . 94 GLU CB C 29.1 0.3 1 436 . 94 GLU C C 175.5 0.3 1 437 . 95 TYR N N 119.7 0.3 1 438 . 95 TYR H H 7.85 0.03 1 439 . 95 TYR CA C 55.1 0.3 1 440 . 95 TYR CB C 37.6 0.3 1 441 . 96 PRO CA C 63.4 0.3 1 442 . 96 PRO CB C 30.9 0.3 1 443 . 96 PRO C C 176.9 0.3 1 444 . 97 THR N N 112.0 0.3 1 445 . 97 THR H H 7.88 0.03 1 446 . 97 THR CA C 61.6 0.3 1 447 . 97 THR CB C 68.8 0.3 1 448 . 97 THR C C 174.1 0.3 1 449 . 98 TYR N N 121.6 0.3 1 450 . 98 TYR H H 7.94 0.03 1 451 . 98 TYR CA C 57.2 0.3 1 452 . 98 TYR CB C 37.8 0.3 1 453 . 98 TYR C C 175.0 0.3 1 454 . 99 LYS N N 122.8 0.3 1 455 . 99 LYS H H 7.99 0.03 1 456 . 99 LYS CA C 55.6 0.3 1 457 . 99 LYS CB C 32.1 0.3 1 458 . 99 LYS C C 175.8 0.3 1 459 . 100 HIS N N 119.3 0.3 1 460 . 100 HIS H H 8.27 0.03 1 461 . 100 HIS CA C 54.6 0.3 1 462 . 100 HIS CB C 28.7 0.3 1 463 . 100 HIS C C 173.7 0.3 1 464 . 101 ASP N N 122.4 0.3 1 465 . 101 ASP H H 8.36 0.03 1 466 . 101 ASP CA C 53.7 0.3 1 467 . 101 ASP CB C 40.7 0.3 1 468 . 101 ASP C C 175.9 0.3 1 469 . 102 THR N N 115.3 0.3 1 470 . 102 THR H H 8.27 0.03 1 471 . 102 THR CA C 61.3 0.3 1 472 . 102 THR CB C 69.2 0.3 1 473 . 102 THR C C 173.6 0.3 1 474 . 103 THR N N 118.4 0.3 1 475 . 103 THR H H 8.19 0.03 1 476 . 103 THR CA C 57.2 0.3 1 477 . 103 THR CB C 64.1 0.3 1 478 . 103 THR C C 173.5 0.3 1 479 . 104 ASP N N 121.4 0.3 1 480 . 104 ASP H H 8.14 0.03 1 481 . 104 ASP CA C 53.4 0.3 1 482 . 104 ASP CB C 43.0 0.3 1 483 . 104 ASP C C 172.9 0.3 1 484 . 105 TYR N N 116.0 0.3 1 485 . 105 TYR H H 8.36 0.03 1 486 . 105 TYR CA C 55.8 0.3 1 487 . 105 TYR CB C 41.2 0.3 1 488 . 105 TYR C C 176.1 0.3 1 489 . 106 GLY N N 107.8 0.3 1 490 . 106 GLY H H 9.03 0.03 1 491 . 106 GLY CA C 44.2 0.3 1 492 . 106 GLY C C 172.1 0.3 1 493 . 107 PHE N N 120.5 0.3 1 494 . 107 PHE H H 8.72 0.03 1 495 . 107 PHE CA C 57.3 0.3 1 496 . 107 PHE CB C 40.0 0.3 1 497 . 107 PHE C C 175.3 0.3 1 498 . 108 SER N N 121.5 0.3 1 499 . 108 SER H H 7.88 0.03 1 500 . 108 SER CA C 55.9 0.3 1 501 . 108 SER CB C 65.5 0.3 1 502 . 108 SER C C 171.5 0.3 1 503 . 109 TYR N N 117.9 0.3 1 504 . 109 TYR H H 8.51 0.03 1 505 . 109 TYR CA C 55.1 0.3 1 506 . 109 TYR CB C 39.5 0.3 1 507 . 109 TYR C C 173.1 0.3 1 508 . 110 GLY N N 105.9 0.3 1 509 . 110 GLY H H 8.81 0.03 1 510 . 110 GLY CA C 45.8 0.3 1 511 . 110 GLY C C 171.4 0.3 1 512 . 111 ALA N N 118.9 0.3 1 513 . 111 ALA H H 8.14 0.03 1 514 . 111 ALA CA C 50.7 0.3 1 515 . 111 ALA CB C 21.8 0.3 1 516 . 111 ALA C C 174.4 0.3 1 517 . 112 GLY N N 105.5 0.3 1 518 . 112 GLY H H 7.64 0.03 1 519 . 112 GLY CA C 44.9 0.3 1 520 . 112 GLY C C 169.6 0.3 1 521 . 113 LEU N N 115.9 0.3 1 522 . 113 LEU H H 8.83 0.03 1 523 . 113 LEU CA C 52.3 0.3 1 524 . 113 LEU CB C 46.2 0.3 1 525 . 113 LEU C C 174.8 0.3 1 526 . 114 GLN N N 115.5 0.3 1 527 . 114 GLN H H 7.78 0.03 1 528 . 114 GLN CA C 53.4 0.3 1 529 . 114 GLN CB C 32.9 0.3 1 530 . 114 GLN C C 176.5 0.3 1 531 . 115 PHE N N 126.1 0.3 1 532 . 115 PHE H H 9.63 0.03 1 533 . 115 PHE CA C 54.8 0.3 1 534 . 115 PHE CB C 42.8 0.3 1 535 . 115 PHE C C 175.3 0.3 1 536 . 116 ASN N N 119.8 0.3 1 537 . 116 ASN H H 9.43 0.03 1 538 . 116 ASN CA C 50.9 0.3 1 539 . 116 ASN CB C 40.4 0.3 1 540 . 117 PRO CA C 63.7 0.3 1 541 . 117 PRO C C 175.1 0.3 1 542 . 118 MET N N 110.6 0.3 1 543 . 118 MET H H 7.24 0.03 1 544 . 118 MET CA C 53.8 0.3 1 545 . 118 MET CB C 35.6 0.3 1 546 . 118 MET C C 170.2 0.3 1 547 . 119 GLU N N 120.0 0.3 1 548 . 119 GLU H H 8.95 0.03 1 549 . 119 GLU CA C 58.9 0.3 1 550 . 119 GLU CB C 28.2 0.3 1 551 . 119 GLU C C 176.5 0.3 1 552 . 120 ASN N N 112.0 0.3 1 553 . 120 ASN H H 8.30 0.03 1 554 . 120 ASN CA C 53.0 0.3 1 555 . 120 ASN CB C 38.3 0.3 1 556 . 120 ASN C C 174.5 0.3 1 557 . 121 VAL N N 118.0 0.3 1 558 . 121 VAL H H 7.54 0.03 1 559 . 121 VAL CA C 60.3 0.3 1 560 . 121 VAL CB C 34.9 0.3 1 561 . 121 VAL C C 174.4 0.3 1 562 . 122 ALA N N 126.1 0.3 1 563 . 122 ALA H H 8.13 0.03 1 564 . 122 ALA CA C 49.3 0.3 1 565 . 122 ALA CB C 22.8 0.3 1 566 . 122 ALA C C 174.9 0.3 1 567 . 123 LEU N N 119.8 0.3 1 568 . 123 LEU H H 8.89 0.03 1 569 . 123 LEU CA C 53.2 0.3 1 570 . 123 LEU CB C 43.9 0.3 1 571 . 123 LEU C C 174.3 0.3 1 572 . 124 ASP N N 126.6 0.3 1 573 . 124 ASP H H 8.48 0.03 1 574 . 124 ASP CA C 53.5 0.3 1 575 . 124 ASP CB C 47.0 0.3 1 576 . 124 ASP C C 171.9 0.3 1 577 . 125 PHE N N 123.0 0.3 1 578 . 125 PHE H H 8.59 0.03 1 579 . 125 PHE CA C 55.3 0.3 1 580 . 125 PHE CB C 42.3 0.3 1 581 . 125 PHE C C 173.8 0.3 1 582 . 126 SER N N 118.7 0.3 1 583 . 126 SER H H 9.28 0.03 1 584 . 126 SER CA C 57.8 0.3 1 585 . 126 SER CB C 66.6 0.3 1 586 . 126 SER C C 171.3 0.3 1 587 . 127 TYR N N 117.9 0.3 1 588 . 127 TYR H H 8.39 0.03 1 589 . 127 TYR CA C 54.8 0.3 1 590 . 127 TYR CB C 42.2 0.3 1 591 . 127 TYR C C 174.1 0.3 1 592 . 128 GLU N N 129.9 0.3 1 593 . 128 GLU H H 8.43 0.03 1 594 . 128 GLU CA C 53.7 0.3 1 595 . 128 GLU CB C 33.4 0.3 1 596 . 128 GLU C C 172.2 0.3 1 597 . 129 GLN N N 127.3 0.3 1 598 . 129 GLN H H 9.16 0.03 1 599 . 129 GLN CA C 53.0 0.3 1 600 . 129 GLN CB C 31.0 0.3 1 601 . 129 GLN C C 173.6 0.3 1 602 . 130 SER N N 118.3 0.3 1 603 . 130 SER H H 8.41 0.03 1 604 . 130 SER CA C 56.1 0.3 1 605 . 130 SER CB C 65.8 0.3 1 606 . 130 SER C C 173.7 0.3 1 607 . 131 ARG N N 126.5 0.3 1 608 . 131 ARG H H 7.61 0.03 1 609 . 131 ARG CA C 54.9 0.3 1 610 . 131 ARG CB C 30.6 0.3 1 611 . 131 ARG C C 174.6 0.3 1 612 . 132 ILE N N 129.2 0.3 1 613 . 132 ILE H H 8.68 0.03 1 614 . 132 ILE CA C 58.6 0.3 1 615 . 132 ILE CB C 38.3 0.3 1 616 . 132 ILE C C 175.2 0.3 1 617 . 133 ARG N N 126.8 0.3 1 618 . 133 ARG H H 9.31 0.03 1 619 . 133 ARG CA C 57.7 0.3 1 620 . 133 ARG CB C 27.2 0.3 1 621 . 134 SER C C 173.0 0.3 1 622 . 135 VAL N N 124.0 0.3 1 623 . 135 VAL H H 8.13 0.03 1 624 . 135 VAL CA C 61.4 0.3 1 625 . 135 VAL CB C 32.2 0.3 1 626 . 135 VAL C C 174.5 0.3 1 627 . 136 ASP N N 127.2 0.3 1 628 . 136 ASP H H 8.07 0.03 1 629 . 136 ASP CA C 53.7 0.3 1 630 . 136 ASP CB C 40.8 0.3 1 631 . 136 ASP C C 175.0 0.3 1 632 . 137 VAL N N 124.4 0.3 1 633 . 137 VAL H H 8.68 0.03 1 634 . 137 VAL CA C 60.2 0.3 1 635 . 137 VAL CB C 32.4 0.3 1 636 . 137 VAL C C 174.8 0.3 1 637 . 138 GLY N N 117.6 0.3 1 638 . 138 GLY H H 8.27 0.03 1 639 . 138 GLY CA C 44.3 0.3 1 640 . 138 GLY C C 172.7 0.3 1 641 . 139 THR N N 123.8 0.3 1 642 . 139 THR H H 8.68 0.03 1 643 . 139 THR CA C 60.6 0.3 1 644 . 139 THR CB C 69.6 0.3 1 645 . 139 THR C C 172.0 0.3 1 646 . 140 TRP N N 126.3 0.3 1 647 . 140 TRP H H 8.37 0.03 1 648 . 140 TRP CA C 55.7 0.3 1 649 . 140 TRP CB C 32.2 0.3 1 650 . 140 TRP C C 175.3 0.3 1 651 . 141 ILE N N 122.7 0.3 1 652 . 141 ILE H H 8.87 0.03 1 653 . 141 ILE CA C 60.0 0.3 1 654 . 141 ILE CB C 40.3 0.3 1 655 . 141 ILE C C 174.7 0.3 1 656 . 142 ALA N N 127.3 0.3 1 657 . 142 ALA H H 8.16 0.03 1 658 . 142 ALA CA C 50.3 0.3 1 659 . 142 ALA CB C 21.7 0.3 1 660 . 142 ALA C C 175.6 0.3 1 661 . 143 GLY N N 108.5 0.3 1 662 . 143 GLY H H 9.47 0.03 1 663 . 143 GLY CA C 44.9 0.3 1 664 . 143 GLY C C 172.0 0.3 1 665 . 144 VAL N N 113.5 0.3 1 666 . 144 VAL H H 8.63 0.03 1 667 . 144 VAL CA C 57.9 0.3 1 668 . 144 VAL CB C 35.3 0.3 1 669 . 144 VAL C C 173.7 0.3 1 670 . 145 GLY N N 107.4 0.3 1 671 . 145 GLY H H 8.40 0.03 1 672 . 145 GLY CA C 46.0 0.3 1 673 . 145 GLY C C 171.3 0.3 1 674 . 146 TYR N N 119.2 0.3 1 675 . 146 TYR H H 8.04 0.03 1 676 . 146 TYR CA C 55.0 0.3 1 677 . 146 TYR CB C 42.9 0.3 1 678 . 146 TYR C C 172.4 0.3 1 679 . 147 ARG N N 125.8 0.3 1 680 . 147 ARG H H 7.72 0.03 1 681 . 147 ARG CA C 53.1 0.3 1 682 . 147 ARG CB C 32.4 0.3 1 683 . 147 ARG C C 174.2 0.3 1 684 . 148 PHE N N 128.4 0.3 1 685 . 148 PHE H H 8.79 0.03 1 686 . 148 PHE CA C 57.5 0.3 1 687 . 148 PHE CB C 39.9 0.3 1 stop_ save_