data_18797 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; NMR structure of OmpX in DPC micelles ; _BMRB_accession_number 18797 _BMRB_flat_file_name bmr18797.str _Entry_type original _Submission_date 2012-10-21 _Accession_date 2012-10-21 _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 Hagn Franz X. . 2 Etzkorn Manuel . . 3 Raschle Thomas . . 4 Wagner Gerhard . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 128 "13C chemical shifts" 383 "15N chemical shifts" 128 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2013-02-18 update BMRB 'update entry citation' 2012-12-19 update BMRB ; update shifts: the following were changed to the corresponding carbonyl carbon: 49 SER H 174.13 52 ALA H 175.23 56 ASP H 175.60 94 GLU N 175.78 97 THR H 174.32 101 ASP H 176.04 ; 2012-12-10 original author 'original release' stop_ loop_ _Related_BMRB_accession_number _Relationship 18796 'NMR resonance assignment of OmpX in phospholipid nanodiscs' 4936 'NMR resonance assignment of OmpX in DHPC micelles' stop_ save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title 'Optimized phospholipid bilayer nanodiscs facilitate high-resolution structure determination of membrane proteins.' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 23294159 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Hagn Franz . . 2 Etzkorn Manuel . . 3 Raschle Thomas . . 4 Wagner Gerhard . . stop_ _Journal_abbreviation 'J. Am. Chem. Soc.' _Journal_name_full 'Journal of the American Chemical Society' _Journal_volume 135 _Journal_issue 5 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 1919 _Page_last 1925 _Year 2013 _Details . save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name 'OmpX in DPC micelles' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label OmpX $OmpX 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_OmpX _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common OmpX _Molecular_mass 16395.943 _Mol_thiol_state 'not present' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 148 _Mol_residue_sequence ; ATSTVTGGYAQSDAQGQMNK MGGFNLKYRYEEDNSPLGVI GSFTYTEKSRTASSGDYNKN QYYGITAGPAYRINDWASIY GVVGVGYGKFQTTEYPTYKH DTSDYGFSYGAGLQFNPMEN VALDFSYEQSRIRSVDVGTW IAGVGYRF ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 1 ALA 2 2 THR 3 3 SER 4 4 THR 5 5 VAL 6 6 THR 7 7 GLY 8 8 GLY 9 9 TYR 10 10 ALA 11 11 GLN 12 12 SER 13 13 ASP 14 14 ALA 15 15 GLN 16 16 GLY 17 17 GLN 18 18 MET 19 19 ASN 20 20 LYS 21 21 MET 22 22 GLY 23 23 GLY 24 24 PHE 25 25 ASN 26 26 LEU 27 27 LYS 28 28 TYR 29 29 ARG 30 30 TYR 31 31 GLU 32 32 GLU 33 33 ASP 34 34 ASN 35 35 SER 36 36 PRO 37 37 LEU 38 38 GLY 39 39 VAL 40 40 ILE 41 41 GLY 42 42 SER 43 43 PHE 44 44 THR 45 45 TYR 46 46 THR 47 47 GLU 48 48 LYS 49 49 SER 50 50 ARG 51 51 THR 52 52 ALA 53 53 SER 54 54 SER 55 55 GLY 56 56 ASP 57 57 TYR 58 58 ASN 59 59 LYS 60 60 ASN 61 61 GLN 62 62 TYR 63 63 TYR 64 64 GLY 65 65 ILE 66 66 THR 67 67 ALA 68 68 GLY 69 69 PRO 70 70 ALA 71 71 TYR 72 72 ARG 73 73 ILE 74 74 ASN 75 75 ASP 76 76 TRP 77 77 ALA 78 78 SER 79 79 ILE 80 80 TYR 81 81 GLY 82 82 VAL 83 83 VAL 84 84 GLY 85 85 VAL 86 86 GLY 87 87 TYR 88 88 GLY 89 89 LYS 90 90 PHE 91 91 GLN 92 92 THR 93 93 THR 94 94 GLU 95 95 TYR 96 96 PRO 97 97 THR 98 98 TYR 99 99 LYS 100 100 HIS 101 101 ASP 102 102 THR 103 103 SER 104 104 ASP 105 105 TYR 106 106 GLY 107 107 PHE 108 108 SER 109 109 TYR 110 110 GLY 111 111 ALA 112 112 GLY 113 113 LEU 114 114 GLN 115 115 PHE 116 116 ASN 117 117 PRO 118 118 MET 119 119 GLU 120 120 ASN 121 121 VAL 122 122 ALA 123 123 LEU 124 124 ASP 125 125 PHE 126 126 SER 127 127 TYR 128 128 GLU 129 129 GLN 130 130 SER 131 131 ARG 132 132 ILE 133 133 ARG 134 134 SER 135 135 VAL 136 136 ASP 137 137 VAL 138 138 GLY 139 139 THR 140 140 TRP 141 141 ILE 142 142 ALA 143 143 GLY 144 144 VAL 145 145 GLY 146 146 TYR 147 147 ARG 148 148 PHE stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-11-04 loop_ _Database_name _Database_accession_code _Database_entry_mol_name _Sequence_query_to_submitted_percentage _Sequence_subject_length _Sequence_identity _Sequence_positive _Sequence_homology_expectation_value BMRB 15201 Outer_membrane_protein_X 100.00 148 100.00 100.00 9.78e-102 BMRB 18796 OmpX 100.00 148 100.00 100.00 9.78e-102 BMRB 19892 OUTER_MEMBRANE_PROTEIN_X 100.00 148 99.32 100.00 1.18e-100 PDB 1ORM "Nmr Fold Of The Outer Membrane Protein Ompx In Dhpc Micelles" 99.32 148 99.32 100.00 7.08e-100 PDB 1Q9F "Nmr Structure Of The Outer Membrane Protein Ompx In Dhpc Micelles" 100.00 148 99.32 100.00 1.18e-100 PDB 1Q9G "Nmr Structure Of The Outer Membrane Protein Ompx In Dhpc Micelles" 100.00 148 99.32 100.00 1.18e-100 PDB 1QJ8 "Crystal Structure Of The Outer Membrane Protein Ompx From Escherichia Coli" 100.00 148 99.32 100.00 1.18e-100 PDB 1QJ9 "Crystal Structure Of The Outer Membrane Protein Ompx From Escherichia Coli" 100.00 148 99.32 100.00 1.18e-100 PDB 2M06 "Nmr Structure Of Ompx In Phopspholipid Nanodiscs" 100.00 148 100.00 100.00 9.78e-102 PDB 2M07 "Nmr Structure Of Ompx In Dpc Micelles" 100.00 148 100.00 100.00 9.78e-102 PDB 2MNH "Refined Structure Of Outer Membrane Protein X In Nanodisc By Measuring Residual Dipolar Couplings" 100.00 148 99.32 100.00 1.18e-100 DBJ BAA35486 "outer membrane protein [Escherichia coli str. K12 substr. W3110]" 100.00 171 100.00 100.00 1.11e-102 DBJ BAB34315 "outer membrane protein X [Escherichia coli O157:H7 str. Sakai]" 100.00 171 100.00 100.00 1.11e-102 DBJ BAG76394 "conserved hypothetical protein [Escherichia coli SE11]" 100.00 171 100.00 100.00 1.11e-102 DBJ BAI24257 "outer membrane protein X [Escherichia coli O26:H11 str. 11368]" 100.00 171 100.00 100.00 1.11e-102 DBJ BAI29701 "outer membrane protein X [Escherichia coli O103:H2 str. 12009]" 100.00 171 100.00 100.00 1.11e-102 EMBL CAP75284 "Outer membrane protein X [Escherichia coli LF82]" 100.00 171 100.00 100.00 1.11e-102 EMBL CAQ31315 "outer membrane protein X [Escherichia coli BL21(DE3)]" 100.00 171 100.00 100.00 1.11e-102 EMBL CAQ97717 "outer membrane protein [Escherichia coli IAI1]" 100.00 171 100.00 100.00 1.11e-102 EMBL CAR02170 "outer membrane protein [Escherichia coli S88]" 100.00 171 100.00 100.00 1.11e-102 EMBL CAR06985 "outer membrane protein [Escherichia coli ED1a]" 100.00 171 100.00 100.00 1.11e-102 GB AAA21856 "similar to outer membrane protein X from Enterobacter cloacae, Swiss-Prot Accession Number P25253; ORF2, partial [Escherichia c" 77.03 137 100.00 100.00 3.04e-75 GB AAA66329 "outer membrane protein [Escherichia coli str. K-12 substr. MG1655]" 100.00 171 100.00 100.00 1.11e-102 GB AAC73901 "outer membrane protein X [Escherichia coli str. K-12 substr. MG1655]" 100.00 171 100.00 100.00 1.11e-102 GB AAG55186 "outer membrane protein X [Escherichia coli O157:H7 str. EDL933]" 100.00 171 100.00 100.00 1.11e-102 GB AAN42399 "outer membrane protein X [Shigella flexneri 2a str. 301]" 100.00 171 100.00 100.00 1.11e-102 REF NP_308919 "outer membrane protein X [Escherichia coli O157:H7 str. Sakai]" 100.00 171 100.00 100.00 1.11e-102 REF NP_415335 "outer membrane protein X [Escherichia coli str. K-12 substr. MG1655]" 100.00 171 100.00 100.00 1.11e-102 REF NP_706692 "outer membrane protein X [Shigella flexneri 2a str. 301]" 100.00 171 100.00 100.00 1.11e-102 REF WP_001295296 "MULTISPECIES: outer membrane protein X [Proteobacteria]" 100.00 171 100.00 100.00 1.11e-102 REF WP_001340109 "outer membrane protein X [Escherichia coli]" 100.00 171 100.00 100.00 1.30e-102 SP P0A917 "RecName: Full=Outer membrane protein X; Flags: Precursor" 100.00 171 100.00 100.00 1.11e-102 SP P0A918 "RecName: Full=Outer membrane protein X; Flags: Precursor" 100.00 171 100.00 100.00 1.11e-102 SP P0A919 "RecName: Full=Outer membrane protein X; Flags: Precursor" 100.00 171 100.00 100.00 1.11e-102 SP P0A920 "RecName: Full=Outer membrane protein X; Flags: Precursor" 100.00 171 100.00 100.00 1.11e-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 _Strain _Variant $OmpX Enterobacteria 562 Bacteria . Escherichia coli BL21 DE3 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 _Details $OmpX 'recombinant technology' . Escherichia coli . pET11a 'cloned via NdeI/BamHI restriction sites' 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 'potassium phosphate' 20 mM 'natural abundance' 'sodium chloride' 50 mM 'natural abundance' EDTA 10 mM 'natural abundance' 'sodium azide' 0.05 % 'natural abundance' DPC 110 mM 'natural abundance' H2O 95 % 'natural abundance' D2O 5 % 'natural abundance' $OmpX 0.5 mM '[U-13C; U-15N; U-2H]' stop_ save_ ############################ # Computer software used # ############################ 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_TOPSPIN _Saveframe_category software _Name TOPSPIN _Version . loop_ _Vendor _Address _Electronic_address 'Bruker Biospin' . . stop_ loop_ _Task collection 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' 'peak picking' 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 refinement 'structure solution' stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model Avance _Field_strength 750 _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_HNCO_2 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCO' _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_HN(CA)CO_5 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HN(CA)CO' _Sample_label $sample_1 save_ save_3D_HNCACB_6 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCACB' _Sample_label $sample_1 save_ save_3D_1H-15N_NOESY_7 _Saveframe_category NMR_applied_experiment _Experiment_name '3D 1H-15N NOESY' _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' 0.1 . M pH 6.5 . pH pressure 1 . atm temperature 318 . K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference_1 _Saveframe_category chemical_shift_reference _Details . loop_ _Mol_common_name _Atom_type _Atom_isotope_number _Atom_group _Chem_shift_units _Chem_shift_value _Reference_method _Reference_type _External_reference_sample_geometry _External_reference_location _External_reference_axis _Indirect_shift_ratio DSS C 13 'methyl protons' ppm 0.00 na indirect . . . 0.251449530 DSS H 1 'methyl protons' ppm 0.00 internal direct . . . 1.000000000 DSS N 15 'methyl protons' ppm 0.00 na indirect . . . 0.101329118 stop_ save_ ################################### # Assigned chemical shift lists # ################################### ################################################################### # Chemical Shift Ambiguity Index Value Definitions # # # # The values other than 1 are used for those atoms with different # # chemical shifts that cannot be assigned to stereospecific atoms # # or to specific residues or chains. # # # # Index Value Definition # # # # 1 Unique (including isolated methyl protons, # # geminal atoms, and geminal methyl # # groups with identical chemical shifts) # # (e.g. ILE HD11, HD12, HD13 protons) # # 2 Ambiguity of geminal atoms or geminal methyl # # proton groups (e.g. ASP HB2 and HB3 # # protons, LEU CD1 and CD2 carbons, or # # LEU HD11, HD12, HD13 and HD21, HD22, # # HD23 methyl protons) # # 3 Aromatic atoms on opposite sides of # # symmetrical rings (e.g. TYR HE1 and HE2 # # protons) # # 4 Intraresidue ambiguities (e.g. LYS HG and # # HD protons or TRP HZ2 and HZ3 protons) # # 5 Interresidue ambiguities (LYS 12 vs. LYS 27) # # 6 Intermolecular ambiguities (e.g. ASP 31 CA # # in monomer 1 and ASP 31 CA in monomer 2 # # of an asymmetrical homodimer, duplex # # DNA assignments, or other assignments # # that may apply to atoms in one or more # # molecule in the molecular assembly) # # 9 Ambiguous, specific ambiguity not defined # # # ################################################################### save_assigned_chem_shift_list_1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Experiment_label '2D 1H-15N HSQC' '3D HNCO' '3D HNCA' '3D HN(CO)CA' '3D HN(CA)CO' '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 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 1 ALA C C 174.17 0.05 1 2 1 1 ALA CA C 51.56 0.05 1 3 1 1 ALA CB C 19.31 0.05 1 4 2 2 THR H H 8.49 0.02 1 5 2 2 THR C C 173.57 0.05 1 6 2 2 THR CA C 61.04 0.05 1 7 2 2 THR CB C 71.93 0.05 1 8 2 2 THR N N 114.28 0.05 1 9 3 3 SER H H 9.00 0.02 1 10 3 3 SER C C 172.59 0.05 1 11 3 3 SER CA C 56.76 0.05 1 12 3 3 SER CB C 65.48 0.05 1 13 3 3 SER N N 122.43 0.05 1 14 4 4 THR H H 8.61 0.02 1 15 4 4 THR C C 174.64 0.05 1 16 4 4 THR CA C 61.39 0.05 1 17 4 4 THR CB C 70.68 0.05 1 18 4 4 THR N N 117.24 0.05 1 19 5 5 VAL H H 8.75 0.02 1 20 5 5 VAL C C 174.77 0.05 1 21 5 5 VAL CA C 59.76 0.05 1 22 5 5 VAL CB C 33.49 0.05 1 23 5 5 VAL N N 129.44 0.05 1 24 6 6 THR H H 8.89 0.02 1 25 6 6 THR C C 172.93 0.05 1 26 6 6 THR CA C 58.59 0.05 1 27 6 6 THR CB C 70.93 0.05 1 28 6 6 THR N N 116.43 0.05 1 29 7 7 GLY H H 8.76 0.02 1 30 7 7 GLY C C 172.43 0.05 1 31 7 7 GLY CA C 44.32 0.05 1 32 7 7 GLY N N 105.59 0.05 1 33 8 8 GLY H H 9.10 0.02 1 34 8 8 GLY C C 173.03 0.05 1 35 8 8 GLY CA C 45.93 0.05 1 36 8 8 GLY N N 106.53 0.05 1 37 9 9 TYR H H 8.41 0.02 1 38 9 9 TYR C C 172.39 0.05 1 39 9 9 TYR CA C 56.84 0.05 1 40 9 9 TYR CB C 41.08 0.05 1 41 9 9 TYR N N 121.73 0.05 1 42 10 10 ALA H H 6.91 0.02 1 43 10 10 ALA C C 174.02 0.05 1 44 10 10 ALA CA C 48.21 0.05 1 45 10 10 ALA CB C 22.22 0.05 1 46 10 10 ALA N N 128.46 0.05 1 47 11 11 GLN H H 8.10 0.02 1 48 11 11 GLN C C 175.65 0.05 1 49 11 11 GLN CA C 53.83 0.05 1 50 11 11 GLN CB C 32.06 0.05 1 51 11 11 GLN N N 118.83 0.05 1 52 12 12 SER H H 9.16 0.02 1 53 12 12 SER C C 172.71 0.05 1 54 12 12 SER CA C 57.19 0.05 1 55 12 12 SER CB C 64.18 0.05 1 56 12 12 SER N N 124.20 0.05 1 57 13 13 ASP H H 9.07 0.02 1 58 13 13 ASP C C 174.86 0.05 1 59 13 13 ASP CA C 52.96 0.05 1 60 13 13 ASP CB C 42.92 0.05 1 61 13 13 ASP N N 124.95 0.05 1 62 14 14 ALA H H 8.56 0.02 1 63 14 14 ALA C C 176.23 0.05 1 64 14 14 ALA CA C 49.81 0.05 1 65 14 14 ALA CB C 19.50 0.05 1 66 14 14 ALA N N 128.73 0.05 1 67 15 15 GLN H H 8.34 0.02 1 68 15 15 GLN C C 176.66 0.05 1 69 15 15 GLN CA C 57.12 0.05 1 70 15 15 GLN CB C 28.16 0.05 1 71 15 15 GLN N N 122.75 0.05 1 72 16 16 GLY H H 8.65 0.02 1 73 16 16 GLY C C 174.40 0.05 1 74 16 16 GLY CA C 45.18 0.05 1 75 16 16 GLY N N 112.80 0.05 1 76 17 17 GLN H H 8.08 .02 1 77 17 17 GLN C C 175.72 0.05 1 78 17 17 GLN CA C 54.60 0.05 1 79 17 17 GLN CB C 32.80 0.05 1 80 17 17 GLN N N 119.30 0.05 1 81 18 18 MET H H 8.37 0.02 1 82 18 18 MET C C 175.40 0.05 1 83 18 18 MET CA C 55.98 0.05 1 84 18 18 MET CB C 35.59 0.05 1 85 18 18 MET N N 120.17 0.05 1 86 19 19 ASN H H 7.99 0.02 1 87 19 19 ASN C C 174.40 0.05 1 88 19 19 ASN CA C 52.30 0.05 1 89 19 19 ASN CB C 39.40 0.05 1 90 19 19 ASN N N 117.90 0.05 1 91 20 20 LYS H H 8.34 0.02 1 92 20 20 LYS C C 176.41 0.05 1 93 20 20 LYS CA C 55.70 0.05 1 94 20 20 LYS CB C 31.90 0.05 1 95 20 20 LYS N N 120.80 0.05 1 96 21 21 MET H H 8.58 0.02 1 97 21 21 MET C C 175.27 0.05 1 98 21 21 MET CA C 54.80 0.05 1 99 21 21 MET CB C 34.73 0.05 1 100 21 21 MET N N 120.50 0.05 1 101 22 22 GLY H H 8.43 0.02 1 102 22 22 GLY C C 174.03 0.05 1 103 22 22 GLY CA C 43.81 0.05 1 104 22 22 GLY N N 111.28 0.05 1 105 23 23 GLY H H 8.18 0.02 1 106 23 23 GLY C C 171.85 0.05 1 107 23 23 GLY CA C 46.15 0.05 1 108 23 23 GLY N N 120.17 0.05 1 109 24 24 PHE H H 9.23 0.02 1 110 24 24 PHE C C 171.57 0.05 1 111 24 24 PHE CA C 54.73 0.05 1 112 24 24 PHE CB C 43.51 0.05 1 113 24 24 PHE N N 121.37 0.05 1 114 25 25 ASN H H 8.52 0.02 1 115 25 25 ASN C C 172.08 0.05 1 116 25 25 ASN CA C 50.87 0.05 1 117 25 25 ASN CB C 46.45 0.05 1 118 25 25 ASN N N 118.95 0.05 1 119 26 26 LEU H H 9.34 0.02 1 120 26 26 LEU C C 175.62 0.05 1 121 26 26 LEU CA C 53.49 0.05 1 122 26 26 LEU CB C 46.63 0.05 1 123 26 26 LEU N N 126.15 0.05 1 124 27 27 LYS H H 8.85 0.02 1 125 27 27 LYS C C 175.12 0.05 1 126 27 27 LYS CA C 55.19 0.05 1 127 27 27 LYS CB C 36.57 0.05 1 128 27 27 LYS N N 117.98 0.05 1 129 28 28 TYR H H 8.43 0.02 1 130 28 28 TYR C C 172.48 0.05 1 131 28 28 TYR CA C 56.28 0.05 1 132 28 28 TYR CB C 41.90 0.05 1 133 28 28 TYR N N 120.82 0.05 1 134 29 29 ARG H H 8.67 0.02 1 135 29 29 ARG C C 172.78 0.05 1 136 29 29 ARG CA C 53.00 0.05 1 137 29 29 ARG CB C 34.01 0.05 1 138 29 29 ARG N N 129.66 0.05 1 139 30 30 TYR H H 8.93 0.02 1 140 30 30 TYR C C 175.00 0.05 1 141 30 30 TYR CA C 56.83 0.05 1 142 30 30 TYR CB C 42.14 0.05 1 143 30 30 TYR N N 127.21 0.05 1 144 31 31 GLU H H 8.17 0.02 1 145 31 31 GLU C C 174.25 0.05 1 146 31 31 GLU CA C 54.63 0.05 1 147 31 31 GLU CB C 32.49 0.05 1 148 31 31 GLU N N 128.09 0.05 1 149 32 32 GLU H H 9.12 0.02 1 150 32 32 GLU C C 176.92 0.05 1 151 32 32 GLU CA C 54.57 0.05 1 152 32 32 GLU CB C 30.77 0.05 1 153 32 32 GLU N N 122.61 0.05 1 154 33 33 ASP H H 8.60 0.02 1 155 33 33 ASP C C 176.99 0.05 1 156 33 33 ASP CA C 55.87 0.05 1 157 33 33 ASP CB C 40.27 0.05 1 158 33 33 ASP N N 121.92 0.05 1 159 34 34 ASN H H 8.42 0.02 1 160 34 34 ASN C C 174.28 0.05 1 161 34 34 ASN CA C 53.36 0.05 1 162 34 34 ASN CB C 37.95 0.05 1 163 34 34 ASN N N 115.30 0.05 1 164 35 35 SER H H 7.27 0.02 1 165 35 35 SER CA C 54.26 0.05 1 166 35 35 SER CB C 64.92 0.05 1 167 35 35 SER N N 112.97 0.05 1 168 36 36 PRO CA C 63.36 0.05 1 169 36 36 PRO CB C 31.47 0.05 1 170 37 37 LEU H H 7.91 0.02 1 171 37 37 LEU C C 176.30 0.05 1 172 37 37 LEU CA C 53.84 0.05 1 173 37 37 LEU CB C 43.69 0.05 1 174 37 37 LEU N N 123.00 0.05 1 175 38 38 GLY H H 9.11 0.02 1 176 38 38 GLY C C 172.34 0.05 1 177 38 38 GLY CA C 44.43 0.05 1 178 38 38 GLY N N 117.32 0.05 1 179 39 39 VAL H H 7.98 0.02 1 180 39 39 VAL C C 171.72 0.05 1 181 39 39 VAL CA C 59.00 0.05 1 182 39 39 VAL CB C 35.61 0.05 1 183 39 39 VAL N N 116.55 0.05 1 184 40 40 ILE H H 9.16 0.02 1 185 40 40 ILE C C 171.60 0.05 1 186 40 40 ILE CA C 58.54 0.05 1 187 40 40 ILE CB C 44.13 0.05 1 188 40 40 ILE N N 125.64 0.05 1 189 41 41 GLY H H 8.93 0.02 1 190 41 41 GLY C C 172.00 0.05 1 191 41 41 GLY CA C 43.15 0.05 1 192 41 41 GLY N N 111.83 0.05 1 193 42 42 SER H H 9.19 0.02 1 194 42 42 SER C C 172.10 0.05 1 195 42 42 SER CA C 56.22 0.05 1 196 42 42 SER CB C 62.92 0.05 1 197 42 42 SER N N 116.94 0.05 1 198 43 43 PHE H H 9.30 0.02 1 199 43 43 PHE C C 172.92 0.05 1 200 43 43 PHE CA C 55.96 0.05 1 201 43 43 PHE CB C 42.43 0.05 1 202 43 43 PHE N N 129.23 0.05 1 203 44 44 THR H H 8.82 0.02 1 204 44 44 THR C C 171.34 0.05 1 205 44 44 THR CA C 60.41 0.05 1 206 44 44 THR CB C 70.22 0.05 1 207 44 44 THR N N 126.53 0.05 1 208 45 45 TYR H H 8.21 0.02 1 209 45 45 TYR C C 174.00 0.05 1 210 45 45 TYR CA C 55.67 0.05 1 211 45 45 TYR CB C 41.00 0.05 1 212 45 45 TYR N N 125.84 0.05 1 213 46 46 THR H H 8.55 0.02 1 214 46 46 THR C C 171.91 0.05 1 215 46 46 THR CA C 58.72 0.05 1 216 46 46 THR CB C 71.71 0.05 1 217 46 46 THR N N 117.67 0.05 1 218 47 47 GLU H H 8.17 0.02 1 219 47 47 GLU CA C 54.58 0.05 1 220 47 47 GLU CB C 32.67 0.05 1 221 47 47 GLU N N 112.16 0.05 1 222 49 49 SER C C 174.13 0.05 1 223 49 49 SER CA C 58.21 0.05 1 224 49 49 SER CB C 64.07 0.05 1 225 50 50 ARG H H 8.60 0.02 1 226 50 50 ARG C C 176.27 0.05 1 227 50 50 ARG CA C 55.96 0.05 1 228 50 50 ARG CB C 30.98 0.05 1 229 50 50 ARG N N 124.00 0.05 1 230 51 51 THR H H 8.24 0.02 1 231 51 51 THR C C 174.40 0.05 1 232 51 51 THR CA C 61.82 0.05 1 233 51 51 THR N N 115.72 0.05 1 234 52 52 ALA C C 175.23 0.05 1 235 52 52 ALA CA C 52.00 0.05 1 236 52 52 ALA CB C 18.80 0.05 1 237 53 53 SER H H 8.00 0.02 1 238 53 53 SER C C 175.36 0.05 1 239 53 53 SER CA C 58.35 0.05 1 240 53 53 SER CB C 62.93 0.05 1 241 53 53 SER N N 113.99 0.05 1 242 54 54 SER H H 8.05 0.02 1 243 54 54 SER C C 173.88 0.05 1 244 54 54 SER CA C 58.50 0.05 1 245 54 54 SER CB C 62.96 0.05 1 246 54 54 SER N N 113.51 0.05 1 247 55 55 GLY H H 8.14 0.02 1 248 55 55 GLY CA C 44.20 0.05 1 249 55 55 GLY N N 112.64 0.05 1 250 56 56 ASP C C 175.60 0.05 1 251 56 56 ASP CA C 54.10 0.05 1 252 56 56 ASP CB C 41.00 0.05 1 253 57 57 TYR H H 8.15 0.02 1 254 57 57 TYR CA C 57.28 0.05 1 255 57 57 TYR CB C 38.40 0.05 1 256 57 57 TYR N N 121.14 0.05 1 257 59 59 LYS CA C 55.41 0.05 1 258 59 59 LYS CB C 34.22 0.05 1 259 60 60 ASN H H 8.36 0.02 1 260 60 60 ASN C C 175.26 0.05 1 261 60 60 ASN CA C 52.20 0.05 1 262 60 60 ASN CB C 40.23 0.05 1 263 60 60 ASN N N 122.74 0.05 1 264 61 61 GLN H H 8.53 0.02 1 265 61 61 GLN C C 172.50 0.05 1 266 61 61 GLN CA C 54.74 0.05 1 267 61 61 GLN CB C 34.84 0.05 1 268 61 61 GLN N N 120.45 0.05 1 269 62 62 TYR H H 8.61 0.02 1 270 62 62 TYR C C 171.43 0.05 1 271 62 62 TYR CA C 56.84 0.05 1 272 62 62 TYR CB C 39.93 0.05 1 273 62 62 TYR N N 123.62 0.05 1 274 63 63 TYR H H 8.40 0.02 1 275 63 63 TYR C C 174.28 0.05 1 276 63 63 TYR CA C 54.58 0.05 1 277 63 63 TYR CB C 41.32 0.05 1 278 63 63 TYR N N 123.92 0.05 1 279 64 64 GLY H H 8.76 0.02 1 280 64 64 GLY C C 174.09 0.05 1 281 64 64 GLY CA C 44.57 0.05 1 282 64 64 GLY N N 107.51 0.05 1 283 65 65 ILE H H 8.90 0.02 1 284 65 65 ILE C C 174.35 0.05 1 285 65 65 ILE CA C 59.96 0.05 1 286 65 65 ILE CB C 39.74 0.05 1 287 65 65 ILE N N 128.47 0.05 1 288 66 66 THR H H 8.90 0.02 1 289 66 66 THR C C 172.60 0.05 1 290 66 66 THR CA C 58.67 0.05 1 291 66 66 THR CB C 73.10 0.05 1 292 66 66 THR N N 115.89 0.05 1 293 67 67 ALA H H 9.37 0.02 1 294 67 67 ALA C C 176.67 0.05 1 295 67 67 ALA CA C 51.50 0.05 1 296 67 67 ALA CB C 22.06 0.05 1 297 67 67 ALA N N 119.73 0.05 1 298 68 68 GLY H H 8.90 0.02 1 299 68 68 GLY CA C 45.92 0.05 1 300 68 68 GLY N N 104.24 0.05 1 301 69 69 PRO CA C 61.04 0.05 1 302 69 69 PRO CB C 32.69 0.05 1 303 70 70 ALA H H 7.87 0.02 1 304 70 70 ALA C C 175.59 0.05 1 305 70 70 ALA CA C 49.49 0.05 1 306 70 70 ALA CB C 20.98 0.05 1 307 70 70 ALA N N 120.22 0.05 1 308 71 71 TYR H H 9.78 0.02 1 309 71 71 TYR C C 174.09 0.05 1 310 71 71 TYR CA C 56.12 0.05 1 311 71 71 TYR CB C 41.92 0.05 1 312 71 71 TYR N N 126.08 0.05 1 313 72 72 ARG H H 8.77 0.02 1 314 72 72 ARG C C 174.16 0.05 1 315 72 72 ARG CA C 56.02 0.05 1 316 72 72 ARG CB C 29.62 0.05 1 317 72 72 ARG N N 131.41 0.05 1 318 73 73 ILE H H 8.40 0.02 1 319 73 73 ILE C C 175.73 0.05 1 320 73 73 ILE CA C 62.95 0.05 1 321 73 73 ILE CB C 38.51 0.05 1 322 73 73 ILE N N 129.55 0.05 1 323 74 74 ASN H H 7.92 0.02 1 324 74 74 ASN C C 174.86 0.05 1 325 74 74 ASN CA C 51.83 0.05 1 326 74 74 ASN CB C 36.84 0.05 1 327 74 74 ASN N N 114.87 0.05 1 328 75 75 ASP H H 8.32 0.02 1 329 75 75 ASP C C 175.82 0.05 1 330 75 75 ASP CA C 56.92 0.05 1 331 75 75 ASP CB C 40.23 0.05 1 332 75 75 ASP N N 113.98 0.05 1 333 76 76 TRP H H 7.97 0.02 1 334 76 76 TRP C C 176.31 0.05 1 335 76 76 TRP CA C 55.41 0.05 1 336 76 76 TRP CB C 31.16 0.05 1 337 76 76 TRP N N 113.60 0.05 1 338 77 77 ALA H H 7.74 0.02 1 339 77 77 ALA C C 175.62 0.05 1 340 77 77 ALA CA C 52.07 0.05 1 341 77 77 ALA CB C 21.14 0.05 1 342 77 77 ALA N N 125.52 0.05 1 343 78 78 SER H H 8.10 0.02 1 344 78 78 SER C C 170.06 0.05 1 345 78 78 SER CA C 57.25 0.05 1 346 78 78 SER CB C 65.32 0.05 1 347 78 78 SER N N 114.14 0.05 1 348 79 79 ILE H H 8.96 0.02 1 349 79 79 ILE C C 172.47 0.05 1 350 79 79 ILE CA C 58.45 0.05 1 351 79 79 ILE CB C 42.10 0.05 1 352 79 79 ILE N N 120.65 0.05 1 353 80 80 TYR H H 8.36 0.02 1 354 80 80 TYR C C 173.00 0.05 1 355 80 80 TYR CA C 55.98 0.05 1 356 80 80 TYR CB C 41.03 0.05 1 357 80 80 TYR N N 120.58 0.05 1 358 81 81 GLY H H 8.05 0.02 1 359 81 81 GLY C C 170.92 0.05 1 360 81 81 GLY CA C 44.00 0.05 1 361 81 81 GLY N N 106.14 0.05 1 362 82 82 VAL H H 8.49 0.02 1 363 82 82 VAL C C 174.37 0.05 1 364 82 82 VAL CA C 58.18 0.05 1 365 82 82 VAL CB C 35.44 0.05 1 366 82 82 VAL N N 111.38 0.05 1 367 83 83 VAL H H 8.97 0.02 1 368 83 83 VAL C C 174.68 0.05 1 369 83 83 VAL CA C 59.09 0.05 1 370 83 83 VAL CB C 36.02 0.05 1 371 83 83 VAL N N 113.66 0.05 1 372 84 84 GLY H H 8.48 0.02 1 373 84 84 GLY C C 171.44 0.05 1 374 84 84 GLY CA C 46.77 0.05 1 375 84 84 GLY N N 108.31 0.05 1 376 85 85 VAL H H 8.92 0.02 1 377 85 85 VAL C C 172.56 0.05 1 378 85 85 VAL CA C 59.17 0.05 1 379 85 85 VAL CB C 35.81 0.05 1 380 85 85 VAL N N 122.52 0.05 1 381 86 86 GLY H H 8.88 0.02 1 382 86 86 GLY C C 172.21 0.05 1 383 86 86 GLY CA C 43.28 0.05 1 384 86 86 GLY N N 113.36 0.05 1 385 87 87 TYR H H 9.31 0.02 1 386 87 87 TYR C C 174.03 0.05 1 387 87 87 TYR CA C 55.93 0.05 1 388 87 87 TYR CB C 42.03 0.05 1 389 87 87 TYR N N 123.83 0.05 1 390 88 88 GLY H H 8.00 0.02 1 391 88 88 GLY C C 170.62 0.05 1 392 88 88 GLY CA C 44.40 0.05 1 393 88 88 GLY N N 112.30 0.05 1 394 89 89 LYS H H 8.23 0.02 1 395 89 89 LYS CA C 54.48 0.05 1 396 89 89 LYS N N 122.41 0.05 1 397 90 90 PHE C C 175.19 0.05 1 398 90 90 PHE CA C 55.03 0.05 1 399 90 90 PHE CB C 40.51 0.05 1 400 91 91 GLN H H 8.37 0.02 1 401 91 91 GLN CA C 55.33 0.05 1 402 91 91 GLN CB C 29.70 0.05 1 403 91 91 GLN N N 122.38 0.05 1 404 94 94 GLU C C 175.78 0.05 1 405 94 94 GLU CA C 57.03 0.05 1 406 94 94 GLU CB C 29.46 0.05 1 407 95 95 TYR H H 7.83 0.02 1 408 95 95 TYR CA C 55.29 0.05 1 409 95 95 TYR CB C 37.73 0.05 1 410 95 95 TYR N N 120.24 0.05 1 411 97 97 THR C C 174.32 0.05 1 412 97 97 THR CA C 62.21 0.05 1 413 98 98 TYR H H 8.04 0.02 1 414 98 98 TYR C C 175.00 0.05 1 415 98 98 TYR CA C 57.53 0.05 1 416 98 98 TYR CB C 38.35 0.05 1 417 98 98 TYR N N 122.54 0.05 1 418 101 101 ASP C C 176.04 0.05 1 419 101 101 ASP CA C 54.02 0.05 1 420 101 101 ASP CB C 39.70 0.05 1 421 102 102 THR H H 8.52 0.02 1 422 102 102 THR C C 173.84 0.05 1 423 102 102 THR CA C 61.59 0.05 1 424 102 102 THR CB C 69.97 0.05 1 425 102 102 THR N N 117.65 0.05 1 426 103 103 SER H H 8.24 0.02 1 427 103 103 SER C C 173.58 0.05 1 428 103 103 SER CA C 57.31 0.05 1 429 103 103 SER N N 119.47 0.05 1 430 104 104 ASP H H 8.27 0.02 1 431 104 104 ASP C C 173.10 0.05 1 432 104 104 ASP CA C 53.60 0.05 1 433 104 104 ASP CB C 44.06 0.05 1 434 104 104 ASP N N 122.25 0.05 1 435 105 105 TYR H H 8.56 0.02 1 436 105 105 TYR C C 175.86 0.05 1 437 105 105 TYR CA C 55.55 0.05 1 438 105 105 TYR CB C 41.63 0.05 1 439 105 105 TYR N N 116.04 0.05 1 440 106 106 GLY H H 9.19 0.02 1 441 106 106 GLY C C 172.03 0.05 1 442 106 106 GLY CA C 44.49 0.05 1 443 106 106 GLY N N 108.50 0.05 1 444 107 107 PHE H H 8.86 0.02 1 445 107 107 PHE C C 175.43 0.05 1 446 107 107 PHE CA C 57.54 0.05 1 447 107 107 PHE CB C 40.20 0.05 1 448 107 107 PHE N N 121.42 0.05 1 449 108 108 SER H H 8.11 0.02 1 450 108 108 SER C C 171.43 0.05 1 451 108 108 SER CA C 56.10 0.05 1 452 108 108 SER CB C 65.72 0.05 1 453 108 108 SER N N 123.25 0.05 1 454 109 109 TYR H H 8.48 0.02 1 455 109 109 TYR C C 173.56 0.05 1 456 109 109 TYR CA C 55.32 0.05 1 457 109 109 TYR CB C 39.56 0.05 1 458 109 109 TYR N N 117.84 0.05 1 459 110 110 GLY H H 8.98 0.02 1 460 110 110 GLY C C 171.35 0.05 1 461 110 110 GLY CA C 46.16 0.05 1 462 110 110 GLY N N 106.40 0.05 1 463 111 111 ALA H H 8.39 0.02 1 464 111 111 ALA C C 174.64 0.05 1 465 111 111 ALA CA C 50.97 0.05 1 466 111 111 ALA CB C 22.15 0.05 1 467 111 111 ALA N N 119.14 0.05 1 468 112 112 GLY H H 7.82 0.02 1 469 112 112 GLY C C 169.77 0.05 1 470 112 112 GLY CA C 45.27 0.05 1 471 112 112 GLY N N 106.07 0.05 1 472 113 113 LEU H H 8.93 0.02 1 473 113 113 LEU C C 175.09 0.05 1 474 113 113 LEU CA C 52.69 0.05 1 475 113 113 LEU CB C 46.56 0.05 1 476 113 113 LEU N N 116.37 0.05 1 477 114 114 GLN H H 7.86 0.02 1 478 114 114 GLN C C 176.91 0.05 1 479 114 114 GLN CA C 53.73 0.05 1 480 114 114 GLN CB C 33.29 0.05 1 481 114 114 GLN N N 115.86 0.05 1 482 115 115 PHE H H 9.75 0.02 1 483 115 115 PHE C C 175.74 0.05 1 484 115 115 PHE CA C 55.20 0.05 1 485 115 115 PHE CB C 43.37 0.05 1 486 115 115 PHE N N 126.58 0.05 1 487 116 116 ASN H H 9.45 0.02 1 488 116 116 ASN CA C 51.20 0.05 1 489 116 116 ASN CB C 40.65 0.05 1 490 116 116 ASN N N 119.92 0.05 1 491 117 117 PRO CA C 63.70 0.05 1 492 118 118 MET H H 7.31 0.02 1 493 118 118 MET C C 176.13 0.05 1 494 118 118 MET CA C 53.98 0.05 1 495 118 118 MET CB C 36.31 0.05 1 496 118 118 MET N N 110.53 0.05 1 497 119 119 GLU H H 9.12 0.02 1 498 119 119 GLU C C 176.81 0.05 1 499 119 119 GLU CA C 59.60 0.05 1 500 119 119 GLU CB C 29.15 0.05 1 501 119 119 GLU N N 120.32 0.05 1 502 120 120 ASN H H 8.43 0.02 1 503 120 120 ASN C C 174.08 0.05 1 504 120 120 ASN CA C 53.40 0.05 1 505 120 120 ASN CB C 38.83 0.05 1 506 120 120 ASN N N 112.49 0.05 1 507 121 121 VAL H H 7.50 0.02 1 508 121 121 VAL C C 174.75 0.05 1 509 121 121 VAL CA C 60.69 0.05 1 510 121 121 VAL CB C 34.90 0.05 1 511 121 121 VAL N N 117.76 0.05 1 512 122 122 ALA H H 8.23 0.02 1 513 122 122 ALA C C 175.14 0.05 1 514 122 122 ALA CA C 49.39 0.05 1 515 122 122 ALA CB C 22.82 0.05 1 516 122 122 ALA N N 127.19 0.05 1 517 123 123 LEU H H 8.91 0.02 1 518 123 123 LEU C C 174.31 0.05 1 519 123 123 LEU CA C 53.66 0.05 1 520 123 123 LEU CB C 44.51 0.05 1 521 123 123 LEU N N 120.27 0.05 1 522 124 124 ASP H H 8.58 0.02 1 523 124 124 ASP C C 171.83 0.05 1 524 124 124 ASP CA C 53.82 0.05 1 525 124 124 ASP CB C 47.49 0.05 1 526 124 124 ASP N N 127.35 0.05 1 527 125 125 PHE H H 8.67 0.02 1 528 125 125 PHE C C 174.13 0.05 1 529 125 125 PHE CA C 55.66 0.05 1 530 125 125 PHE CB C 42.70 0.05 1 531 125 125 PHE N N 123.39 0.05 1 532 126 126 SER H H 9.39 0.02 1 533 126 126 SER C C 169.98 0.05 1 534 126 126 SER CA C 58.12 0.05 1 535 126 126 SER CB C 66.95 0.05 1 536 126 126 SER N N 118.68 0.05 1 537 127 127 TYR H H 8.61 0.02 1 538 127 127 TYR C C 174.39 0.05 1 539 127 127 TYR CA C 55.44 0.05 1 540 127 127 TYR CB C 43.10 0.05 1 541 127 127 TYR N N 119.08 0.05 1 542 128 128 GLU H H 8.51 0.02 1 543 128 128 GLU C C 172.59 0.05 1 544 128 128 GLU CA C 54.13 0.05 1 545 128 128 GLU CB C 33.50 0.05 1 546 128 128 GLU N N 130.07 0.05 1 547 129 129 GLN H H 9.33 0.02 1 548 129 129 GLN C C 173.69 0.05 1 549 129 129 GLN CA C 53.21 0.05 1 550 129 129 GLN CB C 31.05 0.05 1 551 129 129 GLN N N 128.67 0.05 1 552 130 130 SER H H 8.58 0.02 1 553 130 130 SER C C 174.21 0.05 1 554 130 130 SER CA C 56.45 0.05 1 555 130 130 SER CB C 66.26 0.05 1 556 130 130 SER N N 118.63 0.05 1 557 131 131 ARG H H 7.69 0.02 1 558 131 131 ARG C C 174.74 0.05 1 559 131 131 ARG CA C 55.34 0.05 1 560 131 131 ARG CB C 30.91 0.05 1 561 131 131 ARG N N 126.85 0.05 1 562 132 132 ILE H H 8.73 0.02 1 563 132 132 ILE C C 175.50 0.05 1 564 132 132 ILE CA C 58.89 0.05 1 565 132 132 ILE CB C 38.32 0.05 1 566 132 132 ILE N N 129.47 0.05 1 567 133 133 ARG H H 9.40 0.02 1 568 133 133 ARG CA C 58.11 0.05 1 569 133 133 ARG CB C 27.32 0.05 1 570 133 133 ARG N N 127.22 0.05 1 571 134 134 SER C C 173.29 0.05 1 572 134 134 SER CA C 58.49 0.05 1 573 134 134 SER CB C 62.86 0.05 1 574 135 135 VAL H H 8.27 0.02 1 575 135 135 VAL C C 174.65 0.05 1 576 135 135 VAL CA C 61.87 0.05 1 577 135 135 VAL CB C 32.06 0.05 1 578 135 135 VAL N N 124.81 0.05 1 579 136 136 ASP H H 8.01 0.02 1 580 136 136 ASP C C 175.13 0.05 1 581 136 136 ASP CA C 54.22 0.05 1 582 136 136 ASP CB C 41.75 0.05 1 583 136 136 ASP N N 127.75 0.05 1 584 137 137 VAL H H 8.72 0.02 1 585 137 137 VAL C C 174.69 0.05 1 586 137 137 VAL CA C 60.45 0.05 1 587 137 137 VAL CB C 32.80 0.05 1 588 137 137 VAL N N 124.52 0.05 1 589 138 138 GLY H H 8.24 0.02 1 590 138 138 GLY C C 172.93 0.05 1 591 138 138 GLY CA C 44.48 0.05 1 592 138 138 GLY N N 116.92 0.05 1 593 139 139 THR H H 8.71 0.02 1 594 139 139 THR C C 171.92 0.05 1 595 139 139 THR CA C 60.89 0.05 1 596 139 139 THR CB C 70.29 0.05 1 597 139 139 THR N N 125.07 0.05 1 598 140 140 TRP H H 8.33 0.02 1 599 140 140 TRP C C 175.07 0.05 1 600 140 140 TRP CA C 55.13 0.05 1 601 140 140 TRP CB C 32.10 0.05 1 602 140 140 TRP N N 125.84 0.05 1 603 141 141 ILE H H 8.98 0.02 1 604 141 141 ILE C C 174.87 0.05 1 605 141 141 ILE CA C 60.39 0.05 1 606 141 141 ILE CB C 40.63 0.05 1 607 141 141 ILE N N 123.24 0.05 1 608 142 142 ALA H H 8.35 0.02 1 609 142 142 ALA C C 175.70 0.05 1 610 142 142 ALA CA C 50.53 0.05 1 611 142 142 ALA CB C 22.21 0.05 1 612 142 142 ALA N N 127.68 0.05 1 613 143 143 GLY H H 9.52 0.02 1 614 143 143 GLY C C 172.09 0.05 1 615 143 143 GLY CA C 45.43 0.05 1 616 143 143 GLY N N 109.03 0.05 1 617 144 144 VAL H H 8.75 0.02 1 618 144 144 VAL C C 174.01 0.05 1 619 144 144 VAL CA C 58.27 0.05 1 620 144 144 VAL CB C 35.49 0.05 1 621 144 144 VAL N N 114.11 0.05 1 622 145 145 GLY H H 8.59 0.02 1 623 145 145 GLY C C 171.21 0.05 1 624 145 145 GLY CA C 46.77 0.05 1 625 145 145 GLY N N 107.36 0.05 1 626 146 146 TYR H H 8.37 0.02 1 627 146 146 TYR C C 172.44 0.05 1 628 146 146 TYR CA C 55.25 0.05 1 629 146 146 TYR CB C 44.27 0.05 1 630 146 146 TYR N N 121.96 0.05 1 631 147 147 ARG H H 7.69 0.02 1 632 147 147 ARG C C 173.85 0.05 1 633 147 147 ARG CA C 53.36 0.05 1 634 147 147 ARG CB C 32.42 0.05 1 635 147 147 ARG N N 129.59 0.05 1 636 148 148 PHE H H 8.80 0.02 1 637 148 148 PHE CA C 57.68 0.05 1 638 148 148 PHE CB C 39.99 0.05 1 639 148 148 PHE N N 128.55 0.05 1 stop_ save_