data_17507 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; DJ-1 backbone assignment ; _BMRB_accession_number 17507 _BMRB_flat_file_name bmr17507.str _Entry_type original _Submission_date 2011-03-04 _Accession_date 2011-03-04 _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 Eliezer David . . 2 Malgieri Gaetano . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 171 "13C chemical shifts" 533 "15N chemical shifts" 171 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2011-03-14 original author . stop_ _Original_release_date 2011-03-14 save_ ############################# # Citation for this entry # ############################# save_citation_1 _Saveframe_category entry_citation _Citation_full . _Citation_title 'Structural effects of Parkinson s disease linked DJ-1 mutations' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 18436956 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Malgieri Gaetano . . 2 Eliezer David . . stop_ _Journal_abbreviation 'Protein Sci.' _Journal_volume 17 _Journal_issue 5 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 855 _Page_last 868 _Year 2008 _Details . save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name 'DJ-1 protein' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label DJ-1 $DJ-1 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_DJ-1 _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common DJ-1 _Molecular_mass . _Mol_thiol_state 'all free' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 197 _Mol_residue_sequence ; MASKRALVILAKGAEEMETV IPVDVMRRAGIKVTVAGLAG KDPVQCSRDVVICPDASLED AKKEGPYDVVVLPGGNLGAQ NLSESAAVKEILKEQENRKG LIAAICAGPTALLAHEIGFG SKVTTHPLAKDKMMNGGHYT YSENRVEKDGLILTSRGPGT SFEFALAIVEALNGKEVAAQ VKAPLVLKDLEHHHHHH ; loop_ _Residue_seq_code _Residue_label 1 MET 2 ALA 3 SER 4 LYS 5 ARG 6 ALA 7 LEU 8 VAL 9 ILE 10 LEU 11 ALA 12 LYS 13 GLY 14 ALA 15 GLU 16 GLU 17 MET 18 GLU 19 THR 20 VAL 21 ILE 22 PRO 23 VAL 24 ASP 25 VAL 26 MET 27 ARG 28 ARG 29 ALA 30 GLY 31 ILE 32 LYS 33 VAL 34 THR 35 VAL 36 ALA 37 GLY 38 LEU 39 ALA 40 GLY 41 LYS 42 ASP 43 PRO 44 VAL 45 GLN 46 CYS 47 SER 48 ARG 49 ASP 50 VAL 51 VAL 52 ILE 53 CYS 54 PRO 55 ASP 56 ALA 57 SER 58 LEU 59 GLU 60 ASP 61 ALA 62 LYS 63 LYS 64 GLU 65 GLY 66 PRO 67 TYR 68 ASP 69 VAL 70 VAL 71 VAL 72 LEU 73 PRO 74 GLY 75 GLY 76 ASN 77 LEU 78 GLY 79 ALA 80 GLN 81 ASN 82 LEU 83 SER 84 GLU 85 SER 86 ALA 87 ALA 88 VAL 89 LYS 90 GLU 91 ILE 92 LEU 93 LYS 94 GLU 95 GLN 96 GLU 97 ASN 98 ARG 99 LYS 100 GLY 101 LEU 102 ILE 103 ALA 104 ALA 105 ILE 106 CYS 107 ALA 108 GLY 109 PRO 110 THR 111 ALA 112 LEU 113 LEU 114 ALA 115 HIS 116 GLU 117 ILE 118 GLY 119 PHE 120 GLY 121 SER 122 LYS 123 VAL 124 THR 125 THR 126 HIS 127 PRO 128 LEU 129 ALA 130 LYS 131 ASP 132 LYS 133 MET 134 MET 135 ASN 136 GLY 137 GLY 138 HIS 139 TYR 140 THR 141 TYR 142 SER 143 GLU 144 ASN 145 ARG 146 VAL 147 GLU 148 LYS 149 ASP 150 GLY 151 LEU 152 ILE 153 LEU 154 THR 155 SER 156 ARG 157 GLY 158 PRO 159 GLY 160 THR 161 SER 162 PHE 163 GLU 164 PHE 165 ALA 166 LEU 167 ALA 168 ILE 169 VAL 170 GLU 171 ALA 172 LEU 173 ASN 174 GLY 175 LYS 176 GLU 177 VAL 178 ALA 179 ALA 180 GLN 181 VAL 182 LYS 183 ALA 184 PRO 185 LEU 186 VAL 187 LEU 188 LYS 189 ASP 190 LEU 191 GLU 192 HIS 193 HIS 194 HIS 195 HIS 196 HIS 197 HIS 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 PDB 1J42 "Crystal Structure Of Human Dj-1" 95.94 189 99.47 99.47 3.54e-130 PDB 1P5F "Crystal Structure Of Human Dj-1" 95.94 189 100.00 100.00 7.97e-132 PDB 1PDV "Crystal Structure Of Human Dj-1, P 31 2 1 Space Group" 100.00 197 97.97 97.97 1.54e-134 PDB 1PDW "Crystal Structure Of Human Dj-1, P 1 21 1 Space Group" 100.00 197 97.97 97.97 1.54e-134 PDB 1PE0 "Crystal Structure Of The K130r Mutant Of Human Dj-1" 100.00 197 99.49 100.00 1.51e-138 PDB 1Q2U "Crystal Structure Of Dj-1RS AND IMPLICATION ON FAMILIAL PARKINSON'S Disease" 95.94 189 100.00 100.00 7.97e-132 PDB 1SOA "Human Dj-1 With Sulfinic Acid" 95.94 189 99.47 99.47 3.62e-130 PDB 1UCF "The Crystal Structure Of Dj-1, A Protein Related To Male Fertility And Parkinson's Disease" 95.94 189 100.00 100.00 7.97e-132 PDB 2OR3 "Pre-Oxidation Complex Of Human Dj-1" 95.94 189 100.00 100.00 7.97e-132 PDB 2R1T "Dopamine Quinone Conjugation To Dj-1" 94.92 187 99.47 99.47 1.19e-128 PDB 2R1U "Dj-1 Activation By Catechol Quinone Modification" 94.92 187 100.00 100.00 8.74e-130 PDB 2R1V "Norepinephrine Quinone Conjugation To Dj-1" 94.92 187 99.47 99.47 1.19e-128 PDB 2RK3 "Structure Of A104t Dj-1" 100.00 197 99.49 99.49 3.02e-138 PDB 2RK4 "Structure Of M26i Dj-1" 100.00 197 99.49 100.00 3.84e-138 PDB 2RK6 "Structure Of E163k Dj-1" 95.94 192 98.94 99.47 2.78e-129 PDB 3B36 "Structure Of M26l Dj-1" 95.94 192 99.47 100.00 8.42e-131 PDB 3B38 "Structure Of A104v Dj-1" 95.94 192 99.47 99.47 1.32e-130 PDB 3B3A "Structure Of E163kR145E DJ-1" 95.94 192 98.94 99.47 9.22e-130 PDB 3BWE "Crystal Structure Of Aggregated Form Of Dj1" 95.43 189 97.87 97.87 1.53e-126 PDB 3CY6 "Crystal Structure Of E18q Dj-1" 100.00 197 99.49 100.00 1.48e-138 PDB 3CYF "Crystal Structure Of E18n Dj-1" 100.00 197 98.98 98.98 1.18e-136 PDB 3CZ9 "Crystal Structure Of E18l Dj-1" 100.00 197 99.49 99.49 1.07e-137 PDB 3CZA "Crystal Structure Of E18d Dj-1" 100.00 197 99.49 100.00 2.65e-138 PDB 3EZG "Crystal Structure Of E18q Dj-1 With Oxidized C106" 99.49 196 98.98 99.49 4.71e-136 PDB 3F71 "Crystal Structure Of E18d Dj-1 With Oxidized C106" 99.49 196 98.98 99.49 6.46e-136 PDB 3SF8 "Structural Insights Into Thiol Stabilization Of Dj-1" 96.95 191 100.00 100.00 5.26e-133 PDB 4BTE "Dj-1 Cu(i) Complex" 95.94 189 100.00 100.00 7.97e-132 PDB 4MNT "Crystal Structure Of Human Dj-1 In Complex With Cu" 95.94 189 100.00 100.00 7.97e-132 PDB 4MTC "Crystal Structure Of Human C53a Dj-1" 95.94 189 99.47 99.47 1.94e-130 PDB 4N0M "Crystal Structure Of Human C53a Dj-1 In Complex With Cu" 95.94 189 99.47 99.47 1.94e-130 PDB 4N12 "Crystal Structure Of Human E18d Dj-1 In Complex With Cu" 95.94 189 98.94 99.47 1.22e-129 PDB 4OGF "Crystal Structure Of Human Dj-1 With Glyoxylate As Substrate Analog" 94.92 187 99.47 99.47 2.40e-128 PDB 4OQ4 "Crystal Structure Of E18a Human Dj-1" 95.94 192 98.94 98.94 4.36e-129 PDB 4P2G "Crystal Structure Of Dj-1 In Sulfinic Acid Form (aged Crystal)" 95.94 189 99.47 99.47 3.62e-130 PDB 4P34 "Crystal Structure Of Dj-1 In Sulfenic Acid Form (fresh Crystal)" 95.94 189 99.47 99.47 3.62e-130 PDB 4P35 "Crystal Structure Of Dj-1 With Zinc(ii) Bound (crystal I)" 95.94 189 100.00 100.00 7.97e-132 PDB 4P36 "Crystal Structure Of Dj-1 With Zn(ii) Bound (crystal 2)" 95.94 189 99.47 99.47 3.62e-130 PDB 4RKW "Crystal Structure Of Dj-1" 95.94 189 100.00 100.00 7.97e-132 PDB 4RKY "Crystal Structure Of Dj-1 Isoform X1" 95.94 189 99.47 99.47 3.62e-130 PDB 4S0Z "Crystal Structure Of M26v Human Dj-1" 95.94 192 99.47 100.00 1.47e-130 PDB 4ZGG "Crystal Structure Of A Dj-1 (park7) From Homo Sapiens At 1.23 A Resolution" 95.43 190 97.87 97.87 2.18e-126 DBJ BAA09603 "DJ-1 protein [Homo sapiens]" 95.94 189 100.00 100.00 7.97e-132 DBJ BAB71781 "DJ-1 [Chlorocebus aethiops]" 95.94 189 99.47 100.00 1.41e-131 DBJ BAB71782 "DJ-1 [Homo sapiens]" 95.94 189 99.47 99.47 3.54e-130 DBJ BAG34938 "unnamed protein product [Homo sapiens]" 95.94 189 100.00 100.00 7.97e-132 DBJ BAG73513 "Parkinson disease 7 [synthetic construct]" 95.94 189 100.00 100.00 7.97e-132 GB AAC12806 "RNA-binding protein regulatory subunit [Homo sapiens]" 95.94 189 100.00 100.00 7.97e-132 GB AAH08188 "Parkinson disease (autosomal recessive, early onset) 7 [Homo sapiens]" 95.94 189 100.00 100.00 7.97e-132 GB ACJ13695 "epididymis secretory sperm binding protein Li 67p [Homo sapiens]" 95.94 189 100.00 100.00 7.97e-132 GB ADQ32403 "Parkinson disease (autosomal recessive, early onset) 7 [synthetic construct]" 95.94 189 99.47 99.47 2.26e-130 GB EAW71591 "Parkinson disease (autosomal recessive, early onset) 7 [Homo sapiens]" 95.94 189 100.00 100.00 7.97e-132 REF NP_001116849 "protein DJ-1 [Homo sapiens]" 95.94 189 100.00 100.00 7.97e-132 REF NP_009193 "protein DJ-1 [Homo sapiens]" 95.94 189 100.00 100.00 7.97e-132 REF XP_001158093 "PREDICTED: protein DJ-1 isoform X1 [Pan troglodytes]" 95.94 189 99.47 100.00 1.41e-131 REF XP_001158489 "PREDICTED: protein DJ-1 isoform X1 [Pan troglodytes]" 95.94 189 99.47 100.00 1.41e-131 REF XP_002750288 "PREDICTED: protein DJ-1 isoform X1 [Callithrix jacchus]" 95.94 189 98.94 100.00 8.09e-131 SP Q95LI9 "RecName: Full=Protein deglycase DJ-1; AltName: Full=Parkinson disease protein 7 homolog; Flags: Precursor" 95.94 189 99.47 100.00 1.41e-131 SP Q99497 "RecName: Full=Protein deglycase DJ-1; Short=DJ-1; AltName: Full=Oncogene DJ1; AltName: Full=Parkinson disease protein 7; Flags:" 95.94 189 100.00 100.00 7.97e-132 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $DJ-1 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 $DJ-1 'recombinant technology' . Escherichia coli . pET24d 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 $DJ-1 0.3 mM '[U-13C; U-15N; U-2H]' DTT 2 mM 'natural abundance' 'sodium phosphate' 20 mM 'natural abundance' H2O 90 % 'natural abundance' D2O 10 % 'natural abundance' stop_ save_ save_sample_2 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $DJ-1 0.3 mM '[U-100% 15N]' DTT 2 mM 'natural abundance' 'sodium phosphate' 20 mM 'natural abundance' H2O 90 % 'natural abundance' D2O 10 % 'natural abundance' stop_ save_ save_sample_3 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $DJ-1 0.3 mM '[U-13C; U-15N]' DTT 2 mM 'natural abundance' 'sodium phosphate' 20 mM 'natural abundance' H2O 90 % 'natural abundance' D2O 10 % 'natural abundance' stop_ save_ ############################ # Computer software used # ############################ save_NMRView _Saveframe_category software _Name NMRView _Version . loop_ _Vendor _Address _Electronic_address 'Johnson, One Moon Scientific' . . stop_ loop_ _Task 'chemical shift assignment' 'data analysis' stop_ _Details . save_ save_NMRPipe _Saveframe_category software _Name NMRPipe _Version . loop_ _Vendor _Address _Electronic_address 'Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax' . . stop_ loop_ _Task 'chemical shift assignment' 'data analysis' processing stop_ _Details . save_ save_VNMR _Saveframe_category software _Name VNMR _Version . loop_ _Vendor _Address _Electronic_address Varian . . stop_ loop_ _Task collection stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model Avance _Field_strength 900 _Details . save_ save_spectrometer_2 _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model INOVA _Field_strength 600 _Details cold-probe save_ ############################# # NMR applied experiments # ############################# save_2D_1H-15N_HSQC_1 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-15N HSQC' _Sample_label $sample_2 save_ save_3D_HNCACB_2 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCACB' _Sample_label $sample_1 save_ save_3D_CBCA(CO)NH_3 _Saveframe_category NMR_applied_experiment _Experiment_name '3D CBCA(CO)NH' _Sample_label $sample_1 save_ save_3D_HNCO_4 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCO' _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_2D_1H-15N_HSQC_6 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-15N HSQC' _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' 20 . mM pH 6 . pH pressure 1 . atm temperature 300 . 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 . loop_ _Experiment_label '2D 1H-15N HSQC' '3D HNCACB' '3D CBCA(CO)NH' '3D HNCO' '3D HN(CA)CO' stop_ loop_ _Sample_label $sample_2 $sample_1 stop_ _Sample_conditions_label $sample_conditions_1 _Chem_shift_reference_set_label $chemical_shift_reference_1 _Mol_system_component_name DJ-1 _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 3 3 SER CA C 58.73 0.30 1 2 3 3 SER CB C 64.10 0.30 1 3 4 4 LYS H H 8.85 0.01 1 4 4 4 LYS C C 175.66 0.30 1 5 4 4 LYS CA C 54.69 0.30 1 6 4 4 LYS CB C 33.25 0.30 1 7 4 4 LYS N N 123.27 0.15 1 8 5 5 ARG H H 9.86 0.01 1 9 5 5 ARG C C 175.54 0.30 1 10 5 5 ARG CA C 54.76 0.30 1 11 5 5 ARG CB C 34.48 0.30 1 12 5 5 ARG N N 119.54 0.15 1 13 6 6 ALA H H 9.19 0.01 1 14 6 6 ALA C C 173.89 0.30 1 15 6 6 ALA CA C 49.52 0.30 1 16 6 6 ALA CB C 25.36 0.30 1 17 6 6 ALA N N 123.62 0.15 1 18 7 7 LEU H H 8.23 0.01 1 19 7 7 LEU C C 173.92 0.30 1 20 7 7 LEU CA C 52.87 0.30 1 21 7 7 LEU CB C 42.36 0.30 1 22 7 7 LEU N N 124.33 0.15 1 23 8 8 VAL H H 8.76 0.01 1 24 8 8 VAL C C 174.18 0.30 1 25 8 8 VAL CA C 60.50 0.30 1 26 8 8 VAL CB C 32.62 0.30 1 27 8 8 VAL N N 127.61 0.15 1 28 9 9 ILE H H 7.54 0.01 1 29 9 9 ILE C C 172.97 0.30 1 30 9 9 ILE CA C 62.32 0.30 1 31 9 9 ILE CB C 36.97 0.30 1 32 9 9 ILE N N 125.69 0.15 1 33 10 10 LEU H H 9.08 0.01 1 34 10 10 LEU C C 173.17 0.30 1 35 10 10 LEU CA C 53.66 0.30 1 36 10 10 LEU CB C 43.83 0.30 1 37 10 10 LEU N N 130.49 0.15 1 38 11 11 ALA H H 9.69 0.01 1 39 11 11 ALA C C 176.24 0.30 1 40 11 11 ALA CA C 49.01 0.30 1 41 11 11 ALA CB C 23.12 0.30 1 42 11 11 ALA N N 134.60 0.15 1 43 12 12 LYS H H 8.71 0.01 1 44 12 12 LYS C C 176.78 0.30 1 45 12 12 LYS CA C 58.14 0.30 1 46 12 12 LYS CB C 31.60 0.30 1 47 12 12 LYS N N 120.52 0.15 1 48 13 13 GLY H H 8.49 0.01 1 49 13 13 GLY C C 175.73 0.30 1 50 13 13 GLY CA C 44.72 0.30 1 51 13 13 GLY N N 108.35 0.15 1 52 14 14 ALA H H 8.22 0.01 1 53 14 14 ALA C C 176.51 0.30 1 54 14 14 ALA CA C 52.03 0.30 1 55 14 14 ALA CB C 19.64 0.30 1 56 14 14 ALA N N 124.13 0.15 1 57 15 15 GLU H H 7.65 0.01 1 58 15 15 GLU C C 179.10 0.30 1 59 15 15 GLU CA C 56.64 0.30 1 60 15 15 GLU CB C 29.56 0.30 1 61 15 15 GLU N N 126.27 0.15 1 62 16 16 GLU C C 180.46 0.30 1 63 17 17 MET H H 9.59 0.01 1 64 17 17 MET C C 177.45 0.30 1 65 17 17 MET CA C 60.91 0.30 1 66 17 17 MET CB C 32.94 0.30 1 67 17 17 MET N N 123.27 0.15 1 68 18 18 GLU H H 7.19 0.01 1 69 18 18 GLU C C 174.19 0.30 1 70 18 18 GLU CA C 56.12 0.30 1 71 18 18 GLU CB C 28.06 0.30 1 72 18 18 GLU N N 114.76 0.15 1 73 19 19 THR H H 7.26 0.01 1 74 19 19 THR C C 175.52 0.30 1 75 19 19 THR CA C 65.68 0.30 1 76 19 19 THR CB C 68.40 0.30 1 77 19 19 THR N N 110.94 0.15 1 78 20 20 VAL C C 176.41 0.30 1 79 20 20 VAL CA C 66.75 0.30 1 80 20 20 VAL CB C 31.39 0.30 1 81 21 21 ILE H H 8.11 0.01 1 82 21 21 ILE C C 174.30 0.30 1 83 21 21 ILE CA C 66.75 0.30 1 84 21 21 ILE CB C 35.11 0.30 1 85 21 21 ILE N N 116.85 0.15 1 86 22 22 PRO C C 177.59 0.30 1 87 22 22 PRO CA C 65.86 0.30 1 88 22 22 PRO CB C 29.63 0.30 1 89 23 23 VAL H H 7.05 0.01 1 90 23 23 VAL C C 175.75 0.30 1 91 23 23 VAL CA C 67.90 0.30 1 92 23 23 VAL CB C 31.48 0.30 1 93 23 23 VAL N N 115.40 0.15 1 94 24 24 ASP H H 8.29 0.01 1 95 24 24 ASP C C 176.35 0.30 1 96 24 24 ASP CA C 56.68 0.30 1 97 24 24 ASP CB C 38.43 0.30 1 98 24 24 ASP N N 117.07 0.15 1 99 25 25 VAL H H 8.55 0.01 1 100 25 25 VAL C C 177.13 0.30 1 101 25 25 VAL CA C 67.82 0.30 1 102 25 25 VAL CB C 30.75 0.30 1 103 25 25 VAL N N 115.58 0.15 1 104 26 26 MET H H 8.38 0.01 1 105 26 26 MET C C 178.32 0.30 1 106 26 26 MET CA C 60.85 0.30 1 107 26 26 MET CB C 33.34 0.30 1 108 26 26 MET N N 114.12 0.15 1 109 27 27 ARG H H 8.24 0.01 1 110 27 27 ARG C C 182.25 0.30 1 111 27 27 ARG CA C 60.84 0.30 1 112 27 27 ARG CB C 29.01 0.30 1 113 27 27 ARG N N 120.08 0.15 1 114 28 28 ARG H H 8.94 0.01 1 115 28 28 ARG C C 177.65 0.30 1 116 28 28 ARG CA C 59.30 0.30 1 117 28 28 ARG CB C 29.23 0.30 1 118 28 28 ARG N N 122.69 0.15 1 119 29 29 ALA H H 7.45 0.01 1 120 29 29 ALA C C 176.25 0.30 1 121 29 29 ALA CA C 51.58 0.30 1 122 29 29 ALA CB C 20.55 0.30 1 123 29 29 ALA N N 118.99 0.15 1 124 30 30 GLY H H 7.86 0.01 1 125 30 30 GLY C C 174.87 0.30 1 126 30 30 GLY CA C 45.13 0.30 1 127 30 30 GLY N N 105.74 0.15 1 128 31 31 ILE H H 7.68 0.01 1 129 31 31 ILE C C 175.73 0.30 1 130 31 31 ILE CA C 60.96 0.30 1 131 31 31 ILE CB C 37.67 0.30 1 132 31 31 ILE N N 123.10 0.15 1 133 32 32 LYS H H 8.65 0.01 1 134 32 32 LYS C C 175.70 0.30 1 135 32 32 LYS CA C 55.38 0.30 1 136 32 32 LYS CB C 31.09 0.30 1 137 32 32 LYS N N 128.79 0.15 1 138 33 33 VAL H H 9.50 0.01 1 139 33 33 VAL C C 175.50 0.30 1 140 33 33 VAL CA C 60.57 0.30 1 141 33 33 VAL CB C 32.69 0.30 1 142 33 33 VAL N N 131.42 0.15 1 143 34 34 THR H H 9.12 0.01 1 144 34 34 THR C C 172.67 0.30 1 145 34 34 THR CA C 61.76 0.30 1 146 34 34 THR CB C 70.08 0.30 1 147 34 34 THR N N 126.16 0.15 1 148 35 35 VAL H H 10.10 0.01 1 149 35 35 VAL C C 174.28 0.30 1 150 35 35 VAL CA C 61.84 0.30 1 151 35 35 VAL CB C 29.93 0.30 1 152 35 35 VAL N N 131.25 0.15 1 153 36 36 ALA H H 9.17 0.01 1 154 36 36 ALA C C 176.37 0.30 1 155 36 36 ALA CA C 48.67 0.30 1 156 36 36 ALA CB C 21.62 0.30 1 157 36 36 ALA N N 132.29 0.15 1 158 37 37 GLY H H 9.13 0.01 1 159 37 37 GLY C C 174.57 0.30 1 160 37 37 GLY CA C 44.21 0.30 1 161 37 37 GLY N N 110.19 0.15 1 162 38 38 LEU H H 8.42 0.01 1 163 38 38 LEU C C 177.20 0.30 1 164 38 38 LEU CA C 58.32 0.30 1 165 38 38 LEU CB C 42.34 0.30 1 166 38 38 LEU N N 130.38 0.15 1 167 39 39 ALA H H 8.74 0.01 1 168 39 39 ALA C C 176.51 0.30 1 169 39 39 ALA CA C 51.37 0.30 1 170 39 39 ALA CB C 18.59 0.30 1 171 39 39 ALA N N 118.23 0.15 1 172 40 40 GLY H H 7.37 0.01 1 173 40 40 GLY C C 173.03 0.30 1 174 40 40 GLY CA C 44.56 0.30 1 175 40 40 GLY N N 105.51 0.15 1 176 41 41 LYS H H 8.81 0.01 1 177 41 41 LYS C C 175.08 0.30 1 178 41 41 LYS CA C 55.66 0.30 1 179 41 41 LYS CB C 32.47 0.30 1 180 41 41 LYS N N 120.38 0.15 1 181 42 42 ASP H H 7.79 0.01 1 182 42 42 ASP C C 172.70 0.30 1 183 42 42 ASP CA C 53.45 0.30 1 184 42 42 ASP CB C 38.81 0.30 1 185 42 42 ASP N N 119.45 0.15 1 186 43 43 PRO C C 175.91 0.30 1 187 43 43 PRO CA C 63.51 0.30 1 188 43 43 PRO CB C 31.87 0.30 1 189 44 44 VAL H H 8.87 0.01 1 190 44 44 VAL C C 173.86 0.30 1 191 44 44 VAL CA C 61.89 0.30 1 192 44 44 VAL CB C 33.71 0.30 1 193 44 44 VAL N N 124.94 0.15 1 194 45 45 GLN C C 175.73 0.30 1 195 45 45 GLN CA C 56.32 0.30 1 196 45 45 GLN CB C 27.89 0.30 1 197 46 46 CYS H H 8.84 0.01 1 198 46 46 CYS C C 174.73 0.30 1 199 46 46 CYS CA C 61.63 0.30 1 200 46 46 CYS CB C 27.83 0.30 1 201 46 46 CYS N N 127.14 0.15 1 202 47 47 SER H H 9.12 0.01 1 203 47 47 SER C C 174.75 0.30 1 204 47 47 SER CA C 61.74 0.30 1 205 47 47 SER CB C 63.10 0.30 1 206 47 47 SER N N 118.74 0.15 1 207 48 48 ARG C C 174.08 0.30 1 208 48 48 ARG CA C 55.39 0.30 1 209 48 48 ARG CB C 26.84 0.30 1 210 49 49 ASP H H 7.70 0.01 1 211 49 49 ASP C C 176.29 0.30 1 212 49 49 ASP CA C 56.58 0.30 1 213 49 49 ASP CB C 38.15 0.30 1 214 49 49 ASP N N 108.75 0.15 1 215 50 50 VAL H H 7.88 0.01 1 216 50 50 VAL C C 174.18 0.30 1 217 50 50 VAL CA C 64.19 0.30 1 218 50 50 VAL CB C 30.11 0.30 1 219 50 50 VAL N N 122.51 0.15 1 220 51 51 VAL H H 9.23 0.01 1 221 51 51 VAL C C 175.30 0.30 1 222 51 51 VAL CA C 61.15 0.30 1 223 51 51 VAL CB C 32.39 0.30 1 224 51 51 VAL N N 131.47 0.15 1 225 52 52 ILE H H 8.29 0.01 1 226 52 52 ILE C C 176.12 0.30 1 227 52 52 ILE CA C 57.59 0.30 1 228 52 52 ILE CB C 41.18 0.30 1 229 52 52 ILE N N 126.62 0.15 1 230 53 53 CYS H H 8.56 0.01 1 231 53 53 CYS C C 172.78 0.30 1 232 53 53 CYS CA C 58.39 0.30 1 233 53 53 CYS CB C 27.39 0.30 1 234 53 53 CYS N N 126.33 0.15 1 235 54 54 PRO C C 174.81 0.30 1 236 54 54 PRO CA C 62.42 0.30 1 237 54 54 PRO CB C 32.15 0.30 1 238 55 55 ASP H H 8.96 0.01 1 239 55 55 ASP C C 176.19 0.30 1 240 55 55 ASP CA C 56.77 0.30 1 241 55 55 ASP CB C 42.45 0.30 1 242 55 55 ASP N N 119.39 0.15 1 243 56 56 ALA H H 7.74 0.01 1 244 56 56 ALA C C 176.42 0.30 1 245 56 56 ALA CA C 50.52 0.30 1 246 56 56 ALA CB C 22.81 0.30 1 247 56 56 ALA N N 116.44 0.15 1 248 57 57 SER H H 9.42 0.01 1 249 57 57 SER C C 174.68 0.30 1 250 57 57 SER CA C 56.98 0.30 1 251 57 57 SER CB C 64.27 0.30 1 252 57 57 SER N N 116.39 0.15 1 253 58 58 LEU H H 8.66 0.01 1 254 58 58 LEU C C 177.20 0.30 1 255 58 58 LEU CA C 58.01 0.30 1 256 58 58 LEU CB C 40.72 0.30 1 257 58 58 LEU N N 124.31 0.15 1 258 59 59 GLU H H 8.31 0.01 1 259 59 59 GLU C C 178.11 0.30 1 260 59 59 GLU CA C 59.29 0.30 1 261 59 59 GLU CB C 28.73 0.30 1 262 59 59 GLU N N 118.01 0.15 1 263 60 60 ASP H H 7.58 0.01 1 264 60 60 ASP C C 179.21 0.30 1 265 60 60 ASP CA C 56.75 0.30 1 266 60 60 ASP CB C 39.70 0.30 1 267 60 60 ASP N N 118.06 0.15 1 268 61 61 ALA H H 8.67 0.01 1 269 61 61 ALA C C 182.38 0.30 1 270 61 61 ALA CA C 54.35 0.30 1 271 61 61 ALA CB C 18.31 0.30 1 272 61 61 ALA N N 122.40 0.15 1 273 62 62 LYS H H 8.89 0.01 1 274 62 62 LYS C C 177.70 0.30 1 275 62 62 LYS CA C 59.26 0.30 1 276 62 62 LYS CB C 31.42 0.30 1 277 62 62 LYS N N 120.84 0.15 1 278 63 63 LYS H H 7.22 0.01 1 279 63 63 LYS C C 176.94 0.30 1 280 63 63 LYS CA C 57.48 0.30 1 281 63 63 LYS CB C 31.87 0.30 1 282 63 63 LYS N N 117.43 0.15 1 283 64 64 GLU H H 7.19 0.01 1 284 64 64 GLU C C 175.76 0.30 1 285 64 64 GLU CA C 54.80 0.30 1 286 64 64 GLU CB C 29.23 0.30 1 287 64 64 GLU N N 116.56 0.15 1 288 65 65 GLY H H 7.27 0.01 1 289 65 65 GLY C C 171.30 0.30 1 290 65 65 GLY CA C 44.17 0.30 1 291 65 65 GLY N N 106.44 0.15 1 292 66 66 PRO CA C 61.94 0.30 1 293 66 66 PRO CB C 34.41 0.30 1 294 67 67 TYR H H 9.45 0.01 1 295 67 67 TYR C C 175.24 0.30 1 296 67 67 TYR CA C 57.94 0.30 1 297 67 67 TYR CB C 39.93 0.30 1 298 67 67 TYR N N 118.55 0.15 1 299 68 68 ASP H H 8.70 0.01 1 300 68 68 ASP C C 175.58 0.30 1 301 68 68 ASP CA C 57.73 0.30 1 302 68 68 ASP CB C 42.46 0.30 1 303 68 68 ASP N N 122.39 0.15 1 304 69 69 VAL H H 7.66 0.01 1 305 69 69 VAL C C 171.36 0.30 1 306 69 69 VAL CA C 59.18 0.30 1 307 69 69 VAL CB C 33.50 0.30 1 308 69 69 VAL N N 111.70 0.15 1 309 70 70 VAL H H 7.51 0.01 1 310 70 70 VAL C C 173.41 0.30 1 311 70 70 VAL CA C 60.84 0.30 1 312 70 70 VAL CB C 33.43 0.30 1 313 70 70 VAL N N 128.01 0.15 1 314 71 71 VAL H H 9.42 0.01 1 315 71 71 VAL C C 174.14 0.30 1 316 71 71 VAL CA C 60.72 0.30 1 317 71 71 VAL CB C 33.22 0.30 1 318 71 71 VAL N N 126.62 0.15 1 319 72 72 LEU H H 9.32 0.01 1 320 72 72 LEU C C 173.78 0.30 1 321 72 72 LEU CA C 50.53 0.30 1 322 72 72 LEU CB C 40.45 0.30 1 323 72 72 LEU N N 126.50 0.15 1 324 73 73 PRO C C 174.38 0.30 1 325 73 73 PRO CA C 61.51 0.30 1 326 73 73 PRO CB C 32.31 0.30 1 327 74 74 GLY H H 6.87 0.01 1 328 74 74 GLY C C 175.43 0.30 1 329 74 74 GLY CA C 45.55 0.30 1 330 74 74 GLY N N 105.86 0.15 1 331 75 75 GLY H H 9.24 0.01 1 332 75 75 GLY C C 177.19 0.30 1 333 75 75 GLY CA C 44.18 0.30 1 334 75 75 GLY N N 116.85 0.15 1 335 77 77 LEU H H 9.05 0.01 1 336 77 77 LEU C C 178.45 0.30 1 337 77 77 LEU CA C 56.97 0.30 1 338 77 77 LEU CB C 40.12 0.30 1 339 77 77 LEU N N 121.42 0.15 1 340 78 78 GLY H H 6.47 0.01 1 341 78 78 GLY C C 176.36 0.30 1 342 78 78 GLY CA C 47.99 0.30 1 343 78 78 GLY N N 106.44 0.15 1 344 79 79 ALA H H 8.42 0.01 1 345 79 79 ALA C C 180.30 0.30 1 346 79 79 ALA CA C 55.10 0.30 1 347 79 79 ALA CB C 17.56 0.30 1 348 79 79 ALA N N 121.07 0.15 1 349 80 80 GLN H H 7.73 0.01 1 350 80 80 GLN C C 178.04 0.30 1 351 80 80 GLN CA C 59.27 0.30 1 352 80 80 GLN CB C 27.39 0.30 1 353 80 80 GLN N N 121.99 0.15 1 354 81 81 ASN H H 8.31 0.01 1 355 81 81 ASN C C 179.38 0.30 1 356 81 81 ASN CA C 56.23 0.30 1 357 81 81 ASN CB C 37.71 0.30 1 358 81 81 ASN N N 118.07 0.15 1 359 82 82 LEU H H 8.66 0.01 1 360 82 82 LEU C C 180.08 0.30 1 361 82 82 LEU CA C 58.09 0.30 1 362 82 82 LEU CB C 42.29 0.30 1 363 82 82 LEU N N 119.05 0.15 1 364 83 83 SER H H 8.23 0.01 1 365 83 83 SER C C 172.76 0.30 1 366 83 83 SER CA C 62.26 0.30 1 367 83 83 SER CB C 63.13 0.30 1 368 83 83 SER N N 116.37 0.15 1 369 84 84 GLU H H 7.32 0.01 1 370 84 84 GLU C C 176.43 0.30 1 371 84 84 GLU CA C 55.89 0.30 1 372 84 84 GLU CB C 29.99 0.30 1 373 84 84 GLU N N 117.37 0.15 1 374 85 85 SER H H 6.90 0.01 1 375 85 85 SER C C 175.44 0.30 1 376 85 85 SER CA C 56.97 0.30 1 377 85 85 SER CB C 62.95 0.30 1 378 85 85 SER N N 111.87 0.15 1 379 86 86 ALA H H 9.12 0.01 1 380 86 86 ALA C C 179.51 0.30 1 381 86 86 ALA CA C 54.33 0.30 1 382 86 86 ALA CB C 17.62 0.30 1 383 86 86 ALA N N 134.25 0.15 1 384 87 87 ALA H H 7.88 0.01 1 385 87 87 ALA C C 180.40 0.30 1 386 87 87 ALA CA C 54.36 0.30 1 387 87 87 ALA CB C 17.64 0.30 1 388 87 87 ALA N N 121.65 0.15 1 389 88 88 VAL H H 7.55 0.01 1 390 88 88 VAL C C 176.50 0.30 1 391 88 88 VAL CA C 66.00 0.30 1 392 88 88 VAL CB C 30.49 0.30 1 393 88 88 VAL N N 118.67 0.15 1 394 89 89 LYS H H 7.06 0.01 1 395 89 89 LYS C C 177.21 0.30 1 396 89 89 LYS CA C 60.62 0.30 1 397 89 89 LYS CB C 30.58 0.30 1 398 89 89 LYS N N 120.61 0.15 1 399 90 90 GLU H H 7.48 0.01 1 400 90 90 GLU C C 179.50 0.30 1 401 90 90 GLU CA C 59.17 0.30 1 402 90 90 GLU CB C 29.20 0.30 1 403 90 90 GLU N N 115.17 0.15 1 404 91 91 ILE H H 7.68 0.01 1 405 91 91 ILE C C 178.62 0.30 1 406 91 91 ILE CA C 63.77 0.30 1 407 91 91 ILE CB C 37.87 0.30 1 408 91 91 ILE N N 119.43 0.15 1 409 92 92 LEU H H 8.55 0.01 1 410 92 92 LEU C C 178.30 0.30 1 411 92 92 LEU CA C 57.56 0.30 1 412 92 92 LEU CB C 41.21 0.30 1 413 92 92 LEU N N 119.62 0.15 1 414 93 93 LYS H H 8.70 0.01 1 415 93 93 LYS C C 179.65 0.30 1 416 93 93 LYS CA C 58.03 0.30 1 417 93 93 LYS CB C 31.11 0.30 1 418 93 93 LYS N N 119.91 0.15 1 419 94 94 GLU H H 7.98 0.01 1 420 94 94 GLU C C 178.67 0.30 1 421 94 94 GLU CA C 59.26 0.30 1 422 94 94 GLU CB C 28.78 0.30 1 423 94 94 GLU N N 119.66 0.15 1 424 95 95 GLN H H 8.19 0.01 1 425 95 95 GLN C C 178.17 0.30 1 426 95 95 GLN CA C 58.10 0.30 1 427 95 95 GLN CB C 27.17 0.30 1 428 95 95 GLN N N 121.08 0.15 1 429 96 96 GLU H H 8.73 0.01 1 430 96 96 GLU C C 180.57 0.30 1 431 96 96 GLU CA C 59.40 0.30 1 432 96 96 GLU CB C 29.63 0.30 1 433 96 96 GLU N N 120.13 0.15 1 434 97 97 ASN H H 8.43 0.01 1 435 97 97 ASN C C 176.75 0.30 1 436 97 97 ASN CA C 56.08 0.30 1 437 97 97 ASN CB C 38.43 0.30 1 438 97 97 ASN N N 119.27 0.15 1 439 98 98 ARG H H 8.02 0.01 1 440 98 98 ARG C C 175.29 0.30 1 441 98 98 ARG CA C 55.51 0.30 1 442 98 98 ARG CB C 29.69 0.30 1 443 98 98 ARG N N 116.38 0.15 1 444 99 99 LYS H H 7.93 0.01 1 445 99 99 LYS C C 175.72 0.30 1 446 99 99 LYS CA C 57.14 0.30 1 447 99 99 LYS CB C 27.63 0.30 1 448 99 99 LYS N N 116.04 0.15 1 449 100 100 GLY H H 8.35 0.01 1 450 100 100 GLY C C 171.86 0.30 1 451 100 100 GLY CA C 43.36 0.30 1 452 100 100 GLY N N 105.69 0.15 1 453 101 101 LEU H H 7.20 0.01 1 454 101 101 LEU C C 177.35 0.30 1 455 101 101 LEU CA C 55.78 0.30 1 456 101 101 LEU CB C 42.45 0.30 1 457 101 101 LEU N N 119.10 0.15 1 458 102 102 ILE H H 9.02 0.01 1 459 102 102 ILE C C 172.34 0.30 1 460 102 102 ILE CA C 61.54 0.30 1 461 102 102 ILE CB C 40.32 0.30 1 462 102 102 ILE N N 128.01 0.15 1 463 103 103 ALA H H 9.16 0.01 1 464 103 103 ALA C C 175.64 0.30 1 465 103 103 ALA CA C 48.44 0.30 1 466 103 103 ALA CB C 22.36 0.30 1 467 103 103 ALA N N 129.26 0.15 1 468 104 104 ALA H H 9.44 0.01 1 469 104 104 ALA C C 173.52 0.30 1 470 104 104 ALA CA C 50.45 0.30 1 471 104 104 ALA CB C 22.47 0.30 1 472 104 104 ALA N N 124.48 0.15 1 473 105 105 ILE H H 7.66 0.01 1 474 105 105 ILE C C 173.44 0.30 1 475 105 105 ILE CA C 57.17 0.30 1 476 105 105 ILE CB C 40.24 0.30 1 477 105 105 ILE N N 117.42 0.15 1 478 106 106 CYS H H 8.34 0.01 1 479 106 106 CYS C C 177.38 0.30 1 480 106 106 CYS CA C 61.71 0.30 1 481 106 106 CYS CB C 27.40 0.30 1 482 106 106 CYS N N 130.56 0.15 1 483 107 107 ALA C C 179.20 0.30 1 484 107 107 ALA CA C 52.15 0.30 1 485 107 107 ALA CB C 18.35 0.30 1 486 108 108 GLY H H 9.19 0.01 1 487 108 108 GLY C C 172.32 0.30 1 488 108 108 GLY CA C 48.57 0.30 1 489 108 108 GLY N N 112.45 0.15 1 490 109 109 PRO CA C 65.34 0.30 1 491 109 109 PRO CB C 29.82 0.30 1 492 110 110 THR H H 8.02 0.01 1 493 110 110 THR C C 177.03 0.30 1 494 110 110 THR CA C 65.35 0.30 1 495 110 110 THR CB C 68.24 0.30 1 496 110 110 THR N N 106.90 0.15 1 497 111 111 ALA H H 7.95 0.01 1 498 111 111 ALA C C 178.84 0.30 1 499 111 111 ALA CA C 54.10 0.30 1 500 111 111 ALA CB C 17.43 0.30 1 501 111 111 ALA N N 125.41 0.15 1 502 112 112 LEU H H 7.50 0.01 1 503 112 112 LEU C C 178.17 0.30 1 504 112 112 LEU CA C 57.39 0.30 1 505 112 112 LEU CB C 38.18 0.30 1 506 112 112 LEU N N 115.18 0.15 1 507 113 113 LEU H H 6.50 0.01 1 508 113 113 LEU C C 180.33 0.30 1 509 113 113 LEU CA C 57.98 0.30 1 510 113 113 LEU CB C 40.44 0.30 1 511 113 113 LEU N N 119.22 0.15 1 512 114 114 ALA H H 7.44 0.01 1 513 114 114 ALA C C 178.45 0.30 1 514 114 114 ALA CA C 54.53 0.30 1 515 114 114 ALA CB C 18.06 0.30 1 516 114 114 ALA N N 121.24 0.15 1 517 115 115 HIS H H 7.15 0.01 1 518 115 115 HIS C C 173.05 0.30 1 519 115 115 HIS CA C 54.69 0.30 1 520 115 115 HIS CB C 30.58 0.30 1 521 115 115 HIS N N 111.99 0.15 1 522 116 116 GLU H H 7.87 0.01 1 523 116 116 GLU C C 175.08 0.30 1 524 116 116 GLU CA C 56.08 0.30 1 525 116 116 GLU CB C 25.61 0.30 1 526 116 116 GLU N N 116.19 0.15 1 527 117 117 ILE H H 8.72 0.01 1 528 117 117 ILE C C 177.42 0.30 1 529 117 117 ILE CA C 56.91 0.30 1 530 117 117 ILE CB C 36.32 0.30 1 531 117 117 ILE N N 120.55 0.15 1 532 118 118 GLY H H 9.15 0.01 1 533 118 118 GLY C C 175.40 0.30 1 534 118 118 GLY CA C 46.88 0.30 1 535 118 118 GLY N N 116.05 0.15 1 536 119 119 PHE H H 8.73 0.01 1 537 119 119 PHE C C 177.79 0.30 1 538 119 119 PHE CA C 56.51 0.30 1 539 119 119 PHE CB C 34.82 0.30 1 540 119 119 PHE N N 121.07 0.15 1 541 120 120 GLY H H 9.22 0.01 1 542 120 120 GLY C C 175.23 0.30 1 543 120 120 GLY CA C 43.98 0.30 1 544 120 120 GLY N N 111.01 0.15 1 545 121 121 SER H H 8.15 0.01 1 546 121 121 SER C C 172.26 0.30 1 547 121 121 SER CA C 59.61 0.30 1 548 121 121 SER CB C 64.29 0.30 1 549 121 121 SER N N 117.24 0.15 1 550 122 122 LYS H H 9.95 0.01 1 551 122 122 LYS C C 176.02 0.30 1 552 122 122 LYS CA C 55.36 0.30 1 553 122 122 LYS CB C 32.35 0.30 1 554 122 122 LYS N N 126.22 0.15 1 555 123 123 VAL H H 8.53 0.01 1 556 123 123 VAL C C 172.22 0.30 1 557 123 123 VAL CA C 57.91 0.30 1 558 123 123 VAL CB C 36.00 0.30 1 559 123 123 VAL N N 114.81 0.15 1 560 124 124 THR H H 8.56 0.01 1 561 124 124 THR C C 172.34 0.30 1 562 124 124 THR CA C 60.21 0.30 1 563 124 124 THR CB C 70.98 0.30 1 564 124 124 THR N N 114.75 0.15 1 565 125 125 THR H H 7.63 0.01 1 566 125 125 THR C C 174.24 0.30 1 567 125 125 THR CA C 59.37 0.30 1 568 125 125 THR CB C 75.99 0.30 1 569 125 125 THR N N 105.51 0.15 1 570 126 126 HIS H H 8.06 0.01 1 571 126 126 HIS C C 178.00 0.30 1 572 126 126 HIS CA C 59.03 0.30 1 573 126 126 HIS CB C 30.96 0.30 1 574 126 126 HIS N N 122.69 0.15 1 575 127 127 PRO C C 178.72 0.30 1 576 127 127 PRO CA C 66.53 0.30 1 577 127 127 PRO CB C 31.98 0.30 1 578 128 128 LEU H H 11.33 0.01 1 579 128 128 LEU C C 177.96 0.30 1 580 128 128 LEU CA C 56.78 0.30 1 581 128 128 LEU CB C 40.25 0.30 1 582 128 128 LEU N N 119.97 0.15 1 583 129 129 ALA H H 8.20 0.01 1 584 129 129 ALA C C 175.46 0.30 1 585 129 129 ALA CA C 50.97 0.30 1 586 129 129 ALA CB C 18.94 0.30 1 587 129 129 ALA N N 120.60 0.15 1 588 130 130 LYS H H 6.94 0.01 1 589 130 130 LYS C C 176.76 0.30 1 590 130 130 LYS CA C 60.32 0.30 1 591 130 130 LYS CB C 32.09 0.30 1 592 130 130 LYS N N 121.18 0.15 1 593 131 131 ASP H H 8.30 0.01 1 594 131 131 ASP C C 179.12 0.30 1 595 131 131 ASP CA C 57.25 0.30 1 596 131 131 ASP CB C 39.06 0.30 1 597 131 131 ASP N N 116.67 0.15 1 598 132 132 LYS H H 7.88 0.01 1 599 132 132 LYS C C 178.29 0.30 1 600 132 132 LYS CA C 58.80 0.30 1 601 132 132 LYS CB C 31.75 0.30 1 602 132 132 LYS N N 120.10 0.15 1 603 133 133 MET H H 7.76 0.01 1 604 133 133 MET C C 176.13 0.30 1 605 133 133 MET CA C 56.12 0.30 1 606 133 133 MET CB C 32.54 0.30 1 607 133 133 MET N N 117.03 0.15 1 608 134 134 MET H H 7.77 0.01 1 609 134 134 MET C C 178.22 0.30 1 610 134 134 MET CA C 53.17 0.30 1 611 134 134 MET CB C 29.99 0.30 1 612 134 134 MET N N 110.00 0.15 1 613 135 135 ASN H H 7.36 0.01 1 614 135 135 ASN C C 177.13 0.30 1 615 135 135 ASN CA C 55.42 0.30 1 616 135 135 ASN CB C 38.20 0.30 1 617 135 135 ASN N N 122.98 0.15 1 618 136 136 GLY H H 9.23 0.01 1 619 136 136 GLY C C 174.31 0.30 1 620 136 136 GLY CA C 44.65 0.30 1 621 136 136 GLY N N 120.38 0.15 1 622 137 137 GLY H H 8.30 0.01 1 623 137 137 GLY C C 175.50 0.30 1 624 137 137 GLY CA C 47.18 0.30 1 625 137 137 GLY N N 108.05 0.15 1 626 138 138 HIS H H 8.73 0.01 1 627 138 138 HIS C C 171.33 0.30 1 628 138 138 HIS CA C 55.78 0.30 1 629 138 138 HIS CB C 27.12 0.30 1 630 138 138 HIS N N 115.62 0.15 1 631 139 139 TYR H H 7.11 0.01 1 632 139 139 TYR C C 174.58 0.30 1 633 139 139 TYR CA C 56.15 0.30 1 634 139 139 TYR CB C 43.24 0.30 1 635 139 139 TYR N N 113.68 0.15 1 636 140 140 THR H H 8.53 0.01 1 637 140 140 THR C C 172.55 0.30 1 638 140 140 THR CA C 61.78 0.30 1 639 140 140 THR CB C 70.29 0.30 1 640 140 140 THR N N 116.55 0.15 1 641 141 141 TYR H H 8.94 0.01 1 642 141 141 TYR C C 174.90 0.30 1 643 141 141 TYR CA C 59.64 0.30 1 644 141 141 TYR CB C 39.36 0.30 1 645 141 141 TYR N N 126.74 0.15 1 646 142 142 SER H H 7.84 0.01 1 647 142 142 SER C C 172.51 0.30 1 648 142 142 SER CA C 54.57 0.30 1 649 142 142 SER CB C 65.22 0.30 1 650 142 142 SER N N 122.34 0.15 1 651 143 143 GLU H H 8.54 0.01 1 652 143 143 GLU C C 175.64 0.30 1 653 143 143 GLU CA C 54.68 0.30 1 654 143 143 GLU CB C 28.67 0.30 1 655 143 143 GLU N N 122.22 0.15 1 656 144 144 ASN H H 7.88 0.01 1 657 144 144 ASN C C 173.94 0.30 1 658 144 144 ASN CA C 53.34 0.30 1 659 144 144 ASN CB C 38.22 0.30 1 660 144 144 ASN N N 120.04 0.15 1 661 145 145 ARG H H 8.21 0.01 1 662 145 145 ARG C C 177.73 0.30 1 663 145 145 ARG CA C 60.47 0.30 1 664 145 145 ARG CB C 30.41 0.30 1 665 145 145 ARG N N 116.74 0.15 1 666 146 146 VAL H H 7.77 0.01 1 667 146 146 VAL C C 172.74 0.30 1 668 146 146 VAL CA C 61.45 0.30 1 669 146 146 VAL CB C 34.29 0.30 1 670 146 146 VAL N N 117.42 0.15 1 671 147 147 GLU H H 9.23 0.01 1 672 147 147 GLU C C 172.83 0.30 1 673 147 147 GLU CA C 53.42 0.30 1 674 147 147 GLU CB C 32.29 0.30 1 675 147 147 GLU N N 127.78 0.15 1 676 148 148 LYS H H 8.78 0.01 1 677 148 148 LYS C C 174.24 0.30 1 678 148 148 LYS CA C 55.71 0.30 1 679 148 148 LYS CB C 34.37 0.30 1 680 148 148 LYS N N 127.95 0.15 1 681 149 149 ASP H H 8.81 0.01 1 682 149 149 ASP C C 176.27 0.30 1 683 149 149 ASP CA C 52.86 0.30 1 684 149 149 ASP CB C 42.44 0.30 1 685 149 149 ASP N N 128.64 0.15 1 686 150 150 GLY H H 8.87 0.01 1 687 150 150 GLY C C 174.39 0.30 1 688 150 150 GLY CA C 47.26 0.30 1 689 150 150 GLY N N 115.46 0.15 1 690 151 151 LEU H H 8.91 0.01 1 691 151 151 LEU C C 174.41 0.30 1 692 151 151 LEU CA C 54.49 0.30 1 693 151 151 LEU CB C 40.16 0.30 1 694 151 151 LEU N N 128.65 0.15 1 695 152 152 ILE H H 7.79 0.01 1 696 152 152 ILE C C 174.52 0.30 1 697 152 152 ILE CA C 59.10 0.30 1 698 152 152 ILE CB C 36.27 0.30 1 699 152 152 ILE N N 118.87 0.15 1 700 153 153 LEU H H 9.33 0.01 1 701 153 153 LEU C C 175.98 0.30 1 702 153 153 LEU CA C 54.01 0.30 1 703 153 153 LEU CB C 45.50 0.30 1 704 153 153 LEU N N 135.12 0.15 1 705 154 154 THR H H 9.73 0.01 1 706 154 154 THR C C 174.23 0.30 1 707 154 154 THR CA C 58.58 0.30 1 708 154 154 THR CB C 72.92 0.30 1 709 154 154 THR N N 115.75 0.15 1 710 155 155 SER H H 7.29 0.01 1 711 155 155 SER C C 175.57 0.30 1 712 155 155 SER CA C 55.96 0.30 1 713 155 155 SER CB C 65.52 0.30 1 714 155 155 SER N N 108.52 0.15 1 715 156 156 ARG H H 6.82 0.01 1 716 156 156 ARG C C 174.97 0.30 1 717 156 156 ARG CA C 61.98 0.30 1 718 156 156 ARG CB C 32.89 0.30 1 719 156 156 ARG N N 122.28 0.15 1 720 157 157 GLY H H 8.65 0.01 1 721 157 157 GLY C C 171.25 0.30 1 722 157 157 GLY CA C 47.17 0.30 1 723 157 157 GLY N N 102.28 0.15 1 724 158 158 PRO C C 179.75 0.30 1 725 158 158 PRO CA C 66.30 0.30 1 726 158 158 PRO CB C 32.38 0.30 1 727 159 159 GLY H H 9.48 0.01 1 728 159 159 GLY C C 174.42 0.30 1 729 159 159 GLY CA C 45.66 0.30 1 730 159 159 GLY N N 102.61 0.15 1 731 160 160 THR H H 8.02 0.01 1 732 160 160 THR C C 176.10 0.30 1 733 160 160 THR CA C 61.73 0.30 1 734 160 160 THR CB C 68.15 0.30 1 735 160 160 THR N N 110.07 0.15 1 736 161 161 SER H H 7.83 0.01 1 737 161 161 SER C C 176.37 0.30 1 738 161 161 SER N N 117.68 0.15 1 739 162 162 PHE H H 8.58 0.01 1 740 162 162 PHE C C 177.51 0.30 1 741 162 162 PHE CA C 63.36 0.30 1 742 162 162 PHE CB C 38.05 0.30 1 743 162 162 PHE N N 119.79 0.15 1 744 163 163 GLU H H 8.44 0.01 1 745 163 163 GLU C C 179.35 0.30 1 746 163 163 GLU CA C 60.05 0.30 1 747 163 163 GLU CB C 29.05 0.30 1 748 163 163 GLU N N 120.61 0.15 1 749 164 164 PHE H H 8.79 0.01 1 750 164 164 PHE C C 175.02 0.30 1 751 164 164 PHE CA C 59.54 0.30 1 752 164 164 PHE CB C 39.64 0.30 1 753 164 164 PHE N N 120.94 0.15 1 754 165 165 ALA H H 8.41 0.01 1 755 165 165 ALA C C 179.14 0.30 1 756 165 165 ALA CA C 54.86 0.30 1 757 165 165 ALA CB C 18.88 0.30 1 758 165 165 ALA N N 119.85 0.15 1 759 166 166 LEU H H 8.72 0.01 1 760 166 166 LEU C C 178.54 0.30 1 761 166 166 LEU CA C 57.51 0.30 1 762 166 166 LEU CB C 40.03 0.30 1 763 166 166 LEU N N 116.79 0.15 1 764 167 167 ALA H H 8.04 0.01 1 765 167 167 ALA C C 180.92 0.30 1 766 167 167 ALA CA C 54.63 0.30 1 767 167 167 ALA CB C 17.80 0.30 1 768 167 167 ALA N N 123.61 0.15 1 769 168 168 ILE H H 7.58 0.01 1 770 168 168 ILE C C 177.12 0.30 1 771 168 168 ILE CA C 65.75 0.30 1 772 168 168 ILE CB C 37.23 0.30 1 773 168 168 ILE N N 120.77 0.15 1 774 169 169 VAL H H 7.83 0.01 1 775 169 169 VAL C C 177.58 0.30 1 776 169 169 VAL CA C 66.95 0.30 1 777 169 169 VAL CB C 30.49 0.30 1 778 169 169 VAL N N 117.82 0.15 1 779 170 170 GLU H H 8.76 0.01 1 780 170 170 GLU C C 178.61 0.30 1 781 170 170 GLU CA C 59.2 0.30 1 782 170 170 GLU CB C 38.75 0.30 1 783 170 170 GLU N N 120.20 0.15 1 784 171 171 ALA H H 7.84 0.01 1 785 171 171 ALA C C 178.75 0.30 1 786 171 171 ALA CA C 54.47 0.30 1 787 171 171 ALA CB C 28.8 0.30 1 788 171 171 ALA N N 121.13 0.15 1 789 172 172 LEU H H 7.85 0.01 1 790 172 172 LEU C C 177.40 0.30 1 791 172 172 LEU CA C 56.97 0.30 1 792 172 172 LEU CB C 41.67 0.30 1 793 172 172 LEU N N 115.75 0.15 1 794 173 173 ASN H H 8.96 0.01 1 795 173 173 ASN C C 176.17 0.30 1 796 173 173 ASN CA C 53.08 0.30 1 797 173 173 ASN CB C 41.01 0.30 1 798 173 173 ASN N N 114.98 0.15 1 799 174 174 GLY H H 7.93 0.01 1 800 174 174 GLY C C 174.06 0.30 1 801 174 174 GLY CA C 44.74 0.30 1 802 174 174 GLY N N 110.55 0.15 1 803 175 175 LYS H H 8.69 0.01 1 804 175 175 LYS C C 178.63 0.30 1 805 175 175 LYS CA C 59.62 0.30 1 806 175 175 LYS CB C 32.28 0.30 1 807 175 175 LYS N N 118.35 0.15 1 808 176 176 GLU H H 8.78 0.01 1 809 176 176 GLU C C 179.36 0.30 1 810 176 176 GLU CA C 59.67 0.30 1 811 176 176 GLU CB C 27.68 0.30 1 812 176 176 GLU N N 121.42 0.15 1 813 177 177 VAL H H 8.04 0.01 1 814 177 177 VAL C C 178.01 0.30 1 815 177 177 VAL CA C 65.68 0.30 1 816 177 177 VAL CB C 30.67 0.30 1 817 177 177 VAL N N 121.01 0.15 1 818 178 178 ALA H H 7.50 0.01 1 819 178 178 ALA C C 178.28 0.30 1 820 178 178 ALA CA C 55.72 0.30 1 821 178 178 ALA CB C 17.25 0.30 1 822 178 178 ALA N N 120.14 0.15 1 823 179 179 ALA H H 8.01 0.01 1 824 179 179 ALA C C 180.88 0.30 1 825 179 179 ALA CA C 55.10 0.30 1 826 179 179 ALA CB C 17.52 0.30 1 827 179 179 ALA N N 118.87 0.15 1 828 180 180 GLN H H 7.91 0.01 1 829 180 180 GLN C C 179.20 0.30 1 830 180 180 GLN CA C 58.24 0.30 1 831 180 180 GLN CB C 27.77 0.30 1 832 180 180 GLN N N 118.99 0.15 1 833 181 181 VAL H H 8.19 0.01 1 834 181 181 VAL C C 177.19 0.30 1 835 181 181 VAL CA C 64.23 0.30 1 836 181 181 VAL CB C 31.03 0.30 1 837 181 181 VAL N N 118.70 0.15 1 838 182 182 LYS H H 8.05 0.01 1 839 182 182 LYS C C 179.27 0.30 1 840 182 182 LYS CA C 59.17 0.30 1 841 182 182 LYS CB C 32.53 0.30 1 842 182 182 LYS N N 117.77 0.15 1 843 183 183 ALA H H 7.33 0.01 1 844 183 183 ALA C C 177.15 0.30 1 845 183 183 ALA CA C 57.08 0.30 1 846 183 183 ALA CB C 15.24 0.30 1 847 183 183 ALA N N 121.70 0.15 1 848 184 184 PRO C C 178.72 0.30 1 849 184 184 PRO CA C 64.37 0.30 1 850 184 184 PRO CB C 30.92 0.30 1 851 185 185 LEU H H 7.86 0.01 1 852 185 185 LEU C C 176.44 0.30 1 853 185 185 LEU CA C 56.09 0.30 1 854 185 185 LEU CB C 40.80 0.30 1 855 185 185 LEU N N 116.10 0.15 1 856 186 186 VAL H H 7.79 0.01 1 857 186 186 VAL C C 175.71 0.30 1 858 186 186 VAL CA C 63.14 0.30 1 859 186 186 VAL CB C 28.55 0.30 1 860 186 186 VAL N N 117.08 0.15 1 861 187 187 LEU H H 8.46 0.01 1 862 187 187 LEU C C 177.03 0.30 1 863 187 187 LEU CA C 54.42 0.30 1 864 187 187 LEU CB C 41.91 0.30 1 865 187 187 LEU N N 120.64 0.15 1 866 188 188 LYS H H 8.40 0.01 1 867 188 188 LYS C C 175.83 0.30 1 868 188 188 LYS CA C 56.49 0.30 1 869 188 188 LYS CB C 32.53 0.30 1 870 188 188 LYS N N 122.86 0.15 1 871 189 189 ASP H H 8.53 0.01 1 872 189 189 ASP C C 175.80 0.30 1 873 189 189 ASP CA C 54.28 0.30 1 874 189 189 ASP CB C 41.16 0.30 1 875 189 189 ASP N N 124.08 0.15 1 stop_ save_