data_18968 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Diffuse binding of Zn2+ to the denatured ensemble of Cu/Zn superoxide dismutase 1 ; _BMRB_accession_number 18968 _BMRB_flat_file_name bmr18968.str _Entry_type original _Submission_date 2013-01-22 _Accession_date 2013-01-22 _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 Szpryngiel Scarlett . . 2 Oliveberg Mikael . . 3 Maler Lena . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 146 "13C chemical shifts" 299 "15N chemical shifts" 148 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2015-07-29 original BMRB . stop_ _Original_release_date 2015-07-29 save_ ############################# # Citation for this entry # ############################# save_citation1 _Saveframe_category entry_citation _Citation_full . _Citation_title ; Diffuse binding of Zn2+ to the denatured ensemble of Cu/Zn superoxide dismutase 1 ; _Citation_status 'in preparation' _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 Szpryngiel Scarlett . . 2 Oliveberg Mikael . . 3 Maler Lena . . stop_ _Journal_abbreviation 'Not known' _Journal_volume . _Journal_issue . _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first . _Page_last . _Year . _Details . save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name 'Denatured SOD1' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label SOD1 $SOD1 stop_ _System_molecular_weight . _System_physical_state denatured _System_oligomer_state ? _System_paramagnetic no _System_thiol_state . _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_SOD1 _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common SOD1 _Molecular_mass . _Mol_thiol_state 'all free' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 153 _Mol_residue_sequence ; ATKAVAVLKGDGPVQGIINF EQKESNGPVKVWGSIKGLTE GLHGFHVHEEEDNTAGCTSA GPHFNPLSRKHGGPKDEERH VGDLGNVTADKDGVADVSIE DSVISLSGDHAIIGRTLVVH EKADDLGKGGNEESTKTGNA GSRLACGVIGIAQ ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 1 ALA 2 2 THR 3 3 LYS 4 4 ALA 5 5 VAL 6 6 ALA 7 7 VAL 8 8 LEU 9 9 LYS 10 10 GLY 11 11 ASP 12 12 GLY 13 13 PRO 14 14 VAL 15 15 GLN 16 16 GLY 17 17 ILE 18 18 ILE 19 19 ASN 20 20 PHE 21 21 GLU 22 22 GLN 23 23 LYS 24 24 GLU 25 25 SER 26 26 ASN 27 27 GLY 28 28 PRO 29 29 VAL 30 30 LYS 31 31 VAL 32 32 TRP 33 33 GLY 34 34 SER 35 35 ILE 36 36 LYS 37 37 GLY 38 38 LEU 39 39 THR 40 40 GLU 41 41 GLY 42 42 LEU 43 43 HIS 44 44 GLY 45 45 PHE 46 46 HIS 47 47 VAL 48 48 HIS 49 49 GLU 50 50 GLU 51 51 GLU 52 52 ASP 53 53 ASN 54 54 THR 55 55 ALA 56 56 GLY 57 57 CYS 58 58 THR 59 59 SER 60 60 ALA 61 61 GLY 62 62 PRO 63 63 HIS 64 64 PHE 65 65 ASN 66 66 PRO 67 67 LEU 68 68 SER 69 69 ARG 70 70 LYS 71 71 HIS 72 72 GLY 73 73 GLY 74 74 PRO 75 75 LYS 76 76 ASP 77 77 GLU 78 78 GLU 79 79 ARG 80 80 HIS 81 81 VAL 82 82 GLY 83 83 ASP 84 84 LEU 85 85 GLY 86 86 ASN 87 87 VAL 88 88 THR 89 89 ALA 90 90 ASP 91 91 LYS 92 92 ASP 93 93 GLY 94 94 VAL 95 95 ALA 96 96 ASP 97 97 VAL 98 98 SER 99 99 ILE 100 100 GLU 101 101 ASP 102 102 SER 103 103 VAL 104 104 ILE 105 105 SER 106 106 LEU 107 107 SER 108 108 GLY 109 109 ASP 110 110 HIS 111 111 ALA 112 112 ILE 113 113 ILE 114 114 GLY 115 115 ARG 116 116 THR 117 117 LEU 118 118 VAL 119 119 VAL 120 120 HIS 121 121 GLU 122 122 LYS 123 123 ALA 124 124 ASP 125 125 ASP 126 126 LEU 127 127 GLY 128 128 LYS 129 129 GLY 130 130 GLY 131 131 ASN 132 132 GLU 133 133 GLU 134 134 SER 135 135 THR 136 136 LYS 137 137 THR 138 138 GLY 139 139 ASN 140 140 ALA 141 141 GLY 142 142 SER 143 143 ARG 144 144 LEU 145 145 ALA 146 146 CYS 147 147 GLY 148 148 VAL 149 149 ILE 150 150 GLY 151 151 ILE 152 152 ALA 153 153 GLN stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-08-19 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 15711 SOD1 100.00 153 100.00 100.00 3.68e-103 BMRB 15712 SOD1 100.00 153 99.35 99.35 1.92e-102 BMRB 15713 SOD1 100.00 153 99.35 99.35 3.49e-102 BMRB 15714 SOD1 100.00 153 99.35 99.35 3.77e-102 BMRB 18509 Superoxide_dismutase_C6A-C111S_thermostable_mutant 100.00 153 98.04 98.69 1.90e-100 BMRB 18708 SUPEROXIDE_DISMUTASE_CU-ZN 100.00 153 98.04 98.69 1.90e-100 BMRB 26570 SOD1 100.00 153 98.04 98.69 1.90e-100 BMRB 4202 "Superoxide Dismutase" 100.00 153 98.69 100.00 2.33e-102 PDB 1BA9 "The Solution Structure Of Reduced Monomeric Superoxide Dismutase, Nmr, 36 Structures" 99.35 153 98.68 100.00 1.11e-101 PDB 1DSW "The Solution Structure Of A Monomeric, Reduced Form Of Human Copper, Zinc Superoxide Dismutase Bearing The Same Charge As The N" 99.35 153 98.03 98.68 4.72e-100 PDB 1FUN "Superoxide Dismutase Mutant With Lys 136 Replaced By Glu, Cys 6 Replaced By Ala And Cys 111 Replaced By Ser (K136e, C6a, C111s)" 100.00 153 97.39 98.69 1.06e-99 PDB 1HL4 "The Structure Of Apo Type Human Cu, Zn Superoxide Dismutase" 100.00 154 97.39 97.39 2.54e-99 PDB 1HL5 "The Structure Of Holo Type Human Cu, Zn Superoxide Dismutase" 100.00 153 97.39 97.39 2.45e-99 PDB 1KMG "The Solution Structure Of Monomeric Copper-Free Superoxide Dismutase" 100.00 153 98.69 100.00 2.33e-102 PDB 1L3N "The Solution Structure Of Reduced Dimeric Copper Zinc Sod: The Structural Effects Of Dimerization" 100.00 153 98.04 98.69 1.90e-100 PDB 1MFM "Monomeric Human Sod Mutant F50eG51EE133Q AT ATOMIC Resolution" 100.00 153 98.69 100.00 2.33e-102 PDB 1N18 "Thermostable Mutant Of Human Superoxide Dismutase, C6a, C111s" 100.00 154 98.04 98.69 1.69e-100 PDB 1N19 "Structure Of The Hsod A4v Mutant" 100.00 154 97.39 98.04 9.19e-100 PDB 1PTZ "Crystal Structure Of The Human Cu, Zn Superoxide Dismutase, Familial Amyotrophic Lateral Sclerosis (Fals) Mutant H43r" 100.00 153 97.39 98.04 1.75e-99 PDB 1PU0 "Structure Of Human Cu,Zn Superoxide Dismutase" 100.00 153 97.39 97.39 2.45e-99 PDB 1RK7 "Solution Structure Of Apo Cu,Zn Superoxide Dismutase: Role Of Metal Ions In Protein Folding" 100.00 153 98.69 100.00 2.33e-102 PDB 1SOS "Atomic Structures Of Wild-type And Thermostable Mutant Recombinant Human Cu, Zn Superoxide Dismutase" 100.00 154 98.04 98.69 1.97e-100 PDB 1SPD "Amyotrophic Lateral Sclerosis And Structural Defects In Cu,Zn Superoxide Dismutase" 100.00 154 97.39 97.39 2.54e-99 PDB 2AF2 "Solution Structure Of Disulfide Reduced And Copper Depleted Human Superoxide Dismutase" 100.00 153 98.04 98.69 1.90e-100 PDB 2C9S "1.24 Angstroms Resolution Structure Of Zn-Zn Human Superoxide Dismutase" 100.00 153 97.39 97.39 3.26e-99 PDB 2C9U "1.24 Angstroms Resolution Structure Of As-Isolated Cu-Zn Human Superoxide Dismutase" 100.00 153 97.39 97.39 2.45e-99 PDB 2C9V "Atomic Resolution Structure Of Cu-Zn Human Superoxide Dismutase" 100.00 153 97.39 97.39 2.45e-99 PDB 2GBT "C6aC111A CUZN SUPEROXIDE DISMUTASE" 100.00 153 98.69 98.69 8.86e-101 PDB 2GBU "C6a/c111a/c57a/c146a Apo Cuzn Superoxide Dismutase" 100.00 153 97.39 97.39 1.46e-98 PDB 2GBV "C6aC111AC57AC146A HOLO CUZN SUPEROXIDE DISMUTASE" 100.00 153 97.39 97.39 1.46e-98 PDB 2LU5 "Structure And Chemical Shifts Of Cu(I),Zn(Ii) Superoxide Dismutase By Solid-State Nmr" 100.00 153 98.04 98.69 1.90e-100 PDB 2V0A "Atomic Resolution Crystal Structure Of Human Superoxide Dismutase" 100.00 153 97.39 97.39 2.45e-99 PDB 2XJK "Monomeric Human Cu,Zn Superoxide Dismutase" 100.00 153 100.00 100.00 3.68e-103 PDB 2XJL "Monomeric Human Cu,Zn Superoxide Dismutase Without Cu Ligands" 100.00 153 98.04 98.04 2.59e-100 PDB 3ECU "Crystal Structure Of Human Apo Cu,Zn Superoxide Dismutase (Sod1)" 100.00 153 97.39 97.39 2.45e-99 PDB 3HFF "Monomeric Human Cu,Zn Superoxide Dismutase Without Zn Ligands" 100.00 153 97.39 97.39 1.48e-99 PDB 3KH3 "Crystal Structure Of Human CuZN SUPEROXIDE DISMUTASE RECOMBINANTLY Produced In Leishmania Tarantolae; P212121 Crystal Form Cont" 100.00 153 97.39 97.39 2.45e-99 PDB 3KH4 "Crystal Structure Of Human CuZN SUPEROXIDE DISMUTASE RECOMBINANTLY Produced In Leishmania Tarantolae; P6522 Crystal Form Contai" 100.00 153 97.39 97.39 2.45e-99 PDB 3RE0 "Crystal Structure Of Human Apo Cu,zn Superoxide Dismutase (sod1) Complexed With Cisplatin" 100.00 153 97.39 97.39 2.45e-99 PDB 3T5W "2me Modified Human Sod1" 100.00 153 97.39 97.39 3.26e-99 PDB 4B3E "Structure Of Copper-Zinc Superoxide Dismutase Complexed With Bicarbonate." 100.00 154 97.39 97.39 1.89e-99 PDB 4BCY "Monomeric Human Cu,zn Superoxide Dismutase, Mutation H43f" 100.00 153 99.35 99.35 4.59e-102 PDB 4FF9 "Crystal Structure Of Cysteinylated Wt Sod1" 100.00 153 97.39 97.39 2.45e-99 PDB 4OH2 "Crystal Structure Of Cu/zn Superoxide Dismutase I149t" 100.00 153 97.39 98.04 1.13e-99 DBJ BAA14373 "unnamed protein product [Schizosaccharomyces pombe]" 98.69 179 97.35 97.35 1.46e-97 DBJ BAC20345 "Cu,Zn-superoxide dismutase [Pan troglodytes]" 100.00 154 97.39 97.39 1.89e-99 DBJ BAG35052 "unnamed protein product [Homo sapiens]" 100.00 154 97.39 97.39 1.89e-99 DBJ BAG73767 "superoxide dismutase 1, soluble [synthetic construct]" 100.00 154 97.39 97.39 1.89e-99 EMBL CAA26182 "unnamed protein product [Homo sapiens]" 100.00 154 97.39 97.39 1.89e-99 EMBL CAG29351 "SOD1 [Homo sapiens]" 100.00 154 97.39 97.39 1.89e-99 EMBL CAG46542 "SOD1 [Homo sapiens]" 100.00 154 97.39 97.39 1.89e-99 GB AAA72747 "CuZn superoxide dismutase [synthetic construct]" 100.00 154 98.04 98.69 1.69e-100 GB AAA80237 "HSOD-GlyProGly-A+, partial [synthetic construct]" 100.00 171 98.04 98.69 7.34e-100 GB AAB05661 "Cu/Zn-superoxide dismutase [Homo sapiens]" 100.00 154 97.39 97.39 1.89e-99 GB AAD42179 "superoxide dismutase/HCV major epitope fusion protein [synthetic construct]" 100.00 839 97.39 97.39 1.11e-93 GB AAH01034 "Superoxide dismutase 1, soluble [Homo sapiens]" 100.00 154 97.39 97.39 1.89e-99 REF NP_000445 "superoxide dismutase [Cu-Zn] [Homo sapiens]" 100.00 154 97.39 97.39 1.89e-99 REF NP_001009025 "superoxide dismutase [Cu-Zn] [Pan troglodytes]" 100.00 154 97.39 97.39 1.89e-99 REF XP_003813274 "PREDICTED: superoxide dismutase [Cu-Zn] [Pan paniscus]" 100.00 154 97.39 97.39 1.89e-99 REF XP_008976454 "PREDICTED: superoxide dismutase [Cu-Zn] [Pan paniscus]" 100.00 154 97.39 97.39 1.89e-99 SP P00441 "RecName: Full=Superoxide dismutase [Cu-Zn]; AltName: Full=Superoxide dismutase 1; Short=hSod1" 100.00 154 97.39 97.39 1.89e-99 SP P60052 "RecName: Full=Superoxide dismutase [Cu-Zn]" 100.00 154 97.39 97.39 1.89e-99 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $SOD1 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 $SOD1 'recombinant technology' . Escherichia coli . pSOD1 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 $SOD1 0.2-0.5 mM '[U-100% 13C; U-100% 15N]' D2O 10 % '[U-99% 2H]' urea 9 M 'natural abundance' bis-Tris 10 mM 'natural abundance' H2O 90 % 'natural abundance' stop_ save_ ############################ # Computer software used # ############################ 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_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model Avance _Field_strength 700 _Details . save_ save_spectrometer_2 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model Avance _Field_strength 600 _Details . save_ ############################# # NMR applied experiments # ############################# save_2D_1H-15N_HSQC_1 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-15N HSQC' _Sample_label $sample_1 save_ save_3D_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_HNCACB_4 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCACB' _Sample_label $sample_1 save_ save_3D_HN(CO)CA_5 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HN(CO)CA' _Sample_label $sample_1 save_ save_3D_HCACO_6 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HCACO' _Sample_label $sample_1 save_ save_3D_CANCO_7 _Saveframe_category NMR_applied_experiment _Experiment_name '3D CANCO' _Sample_label $sample_1 save_ save_3D_1H-15N_NOESY_8 _Saveframe_category NMR_applied_experiment _Experiment_name '3D 1H-15N NOESY' _Sample_label $sample_1 save_ save_3D_1H-15N_TOCSY_9 _Saveframe_category NMR_applied_experiment _Experiment_name '3D 1H-15N TOCSY' _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' 10 . mM pH 6.3 . pH pressure 1 . atm temperature 298 . K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference_1 _Saveframe_category chemical_shift_reference _Details . loop_ _Mol_common_name _Atom_type _Atom_isotope_number _Atom_group _Chem_shift_units _Chem_shift_value _Reference_method _Reference_type _External_reference_sample_geometry _External_reference_location _External_reference_axis _Indirect_shift_ratio water C 13 protons ppm 4.70 external indirect . . . 0.251449530 water H 1 protons ppm 4.70 external indirect . . . 1 water N 15 protons ppm 4.70 external 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 HNCACB' '3D HN(CO)CA' '3D HCACO' '3D CANCO' '3D 1H-15N NOESY' '3D 1H-15N TOCSY' 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 SOD1 _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 2 2 THR C C 174.256 0 1 2 3 3 LYS H H 8.569 0.004 1 3 3 3 LYS C C 176.042 0.004 1 4 3 3 LYS CA C 55.919 0 1 5 3 3 LYS N N 124.352 0.087 1 6 4 4 ALA H H 8.496 0.003 1 7 4 4 ALA C C 177.532 0.026 1 8 4 4 ALA CA C 52.461 0.022 1 9 4 4 ALA N N 126.191 0.088 1 10 5 5 VAL H H 8.215 0.014 1 11 5 5 VAL C C 175.769 0.005 1 12 5 5 VAL CA C 62.162 0.025 1 13 5 5 VAL N N 119.765 0.07 1 14 6 6 ALA H H 8.429 0.007 1 15 6 6 ALA C C 177.249 0.017 1 16 6 6 ALA CA C 52.385 0.014 1 17 6 6 ALA N N 127.865 0.016 1 18 7 7 VAL H H 8.234 0.012 1 19 7 7 VAL C C 175.986 0.007 1 20 7 7 VAL CA C 62.332 0.029 1 21 7 7 VAL N N 120.415 0.024 1 22 8 8 LEU H H 8.492 0.011 1 23 8 8 LEU C C 177.082 0.006 1 24 8 8 LEU CA C 54.87 0.031 1 25 8 8 LEU N N 126.879 0.035 1 26 9 9 LYS H H 8.594 0.009 1 27 9 9 LYS C C 176.944 0.003 1 28 9 9 LYS CA C 56.686 0.026 1 29 9 9 LYS N N 123.072 0.044 1 30 10 10 GLY H H 8.501 0.006 1 31 10 10 GLY C C 173.593 0.016 1 32 10 10 GLY CA C 45.257 0.027 1 33 10 10 GLY N N 110.319 0.022 1 34 11 11 ASP H H 8.379 0.003 1 35 11 11 ASP C C 176.463 0.006 1 36 11 11 ASP CA C 54.357 0.007 1 37 11 11 ASP N N 120.311 0.065 1 38 12 12 GLY H H 8.287 0.002 1 39 12 12 GLY C C 171.517 0 1 40 12 12 GLY CA C 44.724 0 1 41 12 12 GLY N N 108.632 0.022 1 42 13 13 PRO C C 177.175 0 1 43 13 13 PRO CA C 63.138 0.014 1 44 14 14 VAL H H 8.398 0.007 1 45 14 14 VAL C C 176.278 0.001 1 46 14 14 VAL CA C 62.672 0.026 1 47 14 14 VAL N N 120.763 0.019 1 48 15 15 GLN H H 8.59 0.006 1 49 15 15 GLN C C 176.233 0.009 1 50 15 15 GLN CA C 55.904 0.008 1 51 15 15 GLN N N 124.343 0.032 1 52 16 16 GLY H H 8.476 0.004 1 53 16 16 GLY C C 173.542 0.009 1 54 16 16 GLY CA C 45.232 0.019 1 55 16 16 GLY N N 110.312 0.03 1 56 17 17 ILE H H 8.121 0.003 1 57 17 17 ILE C C 176.109 0.009 1 58 17 17 ILE CA C 61.084 0.044 1 59 17 17 ILE N N 120.379 0.031 1 60 18 18 ILE H H 8.389 0.005 1 61 18 18 ILE C C 175.457 0.012 1 62 18 18 ILE CA C 60.926 0.035 1 63 18 18 ILE N N 125.469 0.03 1 64 19 19 ASN H H 8.551 0.006 1 65 19 19 ASN C C 174.815 0.017 1 66 19 19 ASN CA C 52.922 0.019 1 67 19 19 ASN N N 123.41 0.032 1 68 20 20 PHE H H 8.406 0.005 1 69 20 20 PHE C C 175.597 0.001 1 70 20 20 PHE CA C 58.173 0.034 1 71 20 20 PHE N N 121.861 0.033 1 72 21 21 GLU H H 8.502 0.003 1 73 21 21 GLU C C 176.136 0 1 74 21 21 GLU CA C 56.649 0.019 1 75 21 21 GLU N N 122.256 0.037 1 76 22 22 GLN H H 8.452 0.006 1 77 22 22 GLN C C 175.882 0.007 1 78 22 22 GLN CA C 55.857 0.023 1 79 22 22 GLN N N 122.097 0.048 1 80 23 23 LYS H H 8.527 0.006 1 81 23 23 LYS C C 176.583 0 1 82 23 23 LYS CA C 56.533 0.035 1 83 23 23 LYS N N 123.392 0.043 1 84 24 24 GLU H H 8.676 0.003 1 85 24 24 GLU C C 176.577 0.013 1 86 24 24 GLU CA C 56.662 0.03 1 87 24 24 GLU N N 122.147 0.033 1 88 25 25 SER H H 8.508 0.007 1 89 25 25 SER C C 174.37 0.002 1 90 25 25 SER CA C 58.398 0.014 1 91 25 25 SER N N 116.879 0.015 1 92 26 26 ASN H H 8.605 0.008 1 93 26 26 ASN C C 175.29 0 1 94 26 26 ASN CA C 53.227 0.053 1 95 26 26 ASN N N 120.979 0.06 1 96 27 27 GLY H H 8.268 0.003 1 97 27 27 GLY C C 171.384 0 1 98 27 27 GLY CA C 44.698 0.036 1 99 27 27 GLY N N 108.755 0.04 1 100 28 28 PRO C C 177 0 1 101 28 28 PRO CA C 63.103 0.01 1 102 29 29 VAL H H 8.341 0.004 1 103 29 29 VAL C C 176.123 0 1 104 29 29 VAL CA C 62.562 0.027 1 105 29 29 VAL N N 120.858 0.045 1 106 30 30 LYS H H 8.504 0.007 1 107 30 30 LYS C C 175.963 0 1 108 30 30 LYS CA C 56.209 0.045 1 109 30 30 LYS N N 126.189 0.062 1 110 31 31 VAL H H 8.251 0.004 1 111 31 31 VAL C C 175.824 0.014 1 112 31 31 VAL CA C 62.029 0.032 1 113 31 31 VAL N N 122.117 0.012 1 114 32 32 TRP H H 8.51 0.007 1 115 32 32 TRP C C 176.575 0.006 1 116 32 32 TRP CA C 57.309 0.036 1 117 32 32 TRP N N 125.83 0.041 1 118 33 33 GLY H H 8.423 0.004 1 119 33 33 GLY C C 173.774 0.006 1 120 33 33 GLY CA C 45.271 0.05 1 121 33 33 GLY N N 110.59 0.028 1 122 34 34 SER H H 8.29 0.005 1 123 34 34 SER C C 174.695 0.006 1 124 34 34 SER CA C 58.261 0.019 1 125 34 34 SER N N 115.565 0.03 1 126 35 35 ILE H H 8.384 0.007 1 127 35 35 ILE C C 176.231 0 1 128 35 35 ILE CA C 61.308 0.012 1 129 35 35 ILE N N 122.892 0.03 1 130 36 36 LYS H H 8.528 0.005 1 131 36 36 LYS C C 176.966 0 1 132 36 36 LYS CA C 56.571 0.021 1 133 36 36 LYS N N 125.889 0.021 1 134 37 37 GLY H H 8.499 0.011 1 135 37 37 GLY C C 173.94 0.003 1 136 37 37 GLY CA C 45.267 0.049 1 137 37 37 GLY N N 110.336 0.024 1 138 38 38 LEU H H 8.225 0.003 1 139 38 38 LEU C C 177.748 0.016 1 140 38 38 LEU CA C 55.483 0.015 1 141 38 38 LEU N N 121.694 0.023 1 142 39 39 THR H H 8.351 0.003 1 143 39 39 THR C C 174.606 0 1 144 39 39 THR CA C 61.961 0.02 1 145 39 39 THR N N 114.374 0.036 1 146 40 40 GLU H H 8.508 0.005 1 147 40 40 GLU C C 176.764 0.018 1 148 40 40 GLU CA C 56.893 0.018 1 149 40 40 GLU N N 123.371 0.023 1 150 41 41 GLY H H 8.466 0.003 1 151 41 41 GLY C C 173.902 0.003 1 152 41 41 GLY CA C 45.273 0.034 1 153 41 41 GLY N N 109.759 0.033 1 154 42 42 LEU H H 8.163 0.003 1 155 42 42 LEU C C 177.315 0.019 1 156 42 42 LEU CA C 55.259 0.029 1 157 42 42 LEU N N 121.385 0.02 1 158 43 43 HIS H H 8.585 0.012 1 159 43 43 HIS C C 175.478 0.037 1 160 43 43 HIS CA C 55.914 0.038 1 161 43 43 HIS N N 119.738 0.025 1 162 44 44 GLY H H 8.415 0.007 1 163 44 44 GLY C C 173.468 0.001 1 164 44 44 GLY CA C 45.236 0.025 1 165 44 44 GLY N N 109.69 0.038 1 166 45 45 PHE H H 8.285 0.003 1 167 45 45 PHE C C 175.37 0.002 1 168 45 45 PHE CA C 57.79 0.026 1 169 45 45 PHE N N 120.18 0.041 1 170 46 46 HIS H H 8.562 0.007 1 171 46 46 HIS C C 174.458 0 1 172 46 46 HIS CA C 55.698 0.035 1 173 46 46 HIS N N 121.797 0.046 1 174 47 47 VAL H H 8.279 0.005 1 175 47 47 VAL C C 175.724 0.008 1 176 47 47 VAL CA C 62.366 0.016 1 177 47 47 VAL N N 122.318 0.016 1 178 48 48 HIS H H 8.701 0.008 1 179 48 48 HIS C C 174.755 0.028 1 180 48 48 HIS CA C 55.992 0.025 1 181 48 48 HIS N N 123.251 0.049 1 182 49 49 GLU H H 8.667 0.006 1 183 49 49 GLU C C 176.252 0.012 1 184 49 49 GLU CA C 56.775 0.026 1 185 49 49 GLU N N 123.634 0.04 1 186 50 50 GLU H H 8.677 0.003 1 187 50 50 GLU C C 176.507 0.009 1 188 50 50 GLU CA C 56.702 0.04 1 189 50 50 GLU N N 121.928 0.082 1 190 51 51 GLU H H 8.527 0.003 1 191 51 51 GLU C C 176.092 0.004 1 192 51 51 GLU CA C 56.716 0.019 1 193 51 51 GLU N N 121.776 0.023 1 194 52 52 ASP H H 8.501 0.006 1 195 52 52 ASP C C 176.301 0.017 1 196 52 52 ASP CA C 54.345 0.031 1 197 52 52 ASP N N 121.452 0.025 1 198 53 53 ASN H H 8.624 0.004 1 199 53 53 ASN C C 175.903 0.01 1 200 53 53 ASN CA C 53.525 0.051 1 201 53 53 ASN N N 120.678 0.026 1 202 54 54 THR H H 8.375 0.003 1 203 54 54 THR C C 174.85 0.014 1 204 54 54 THR CA C 62.561 0.026 1 205 54 54 THR N N 113.598 0.034 1 206 55 55 ALA H H 8.274 0.004 1 207 55 55 ALA C C 178.011 0.001 1 208 55 55 ALA CA C 53.022 0.017 1 209 55 55 ALA N N 125.75 0.028 1 210 56 56 GLY H H 8.343 0.002 1 211 56 56 GLY C C 174.203 0.006 1 212 56 56 GLY CA C 45.406 0.028 1 213 56 56 GLY N N 107.307 0.051 1 214 57 57 CYS H H 8.44 0.003 1 215 57 57 CYS C C 174.944 0 1 216 57 57 CYS CA C 55.657 0.019 1 217 57 57 CYS N N 118.506 0.059 1 218 58 58 THR H H 8.485 0.007 1 219 58 58 THR C C 174.515 0 1 220 58 58 THR CA C 61.907 0.002 1 221 58 58 THR N N 115.567 0.042 1 222 59 59 SER H H 8.491 0.007 1 223 59 59 SER C C 174.168 0.001 1 224 59 59 SER CA C 58.405 0.007 1 225 59 59 SER N N 118.145 0.029 1 226 60 60 ALA H H 8.409 0.006 1 227 60 60 ALA C C 177.594 0.024 1 228 60 60 ALA CA C 52.592 0.039 1 229 60 60 ALA N N 125.814 0.035 1 230 61 61 GLY H H 8.223 0.002 1 231 61 61 GLY C C 171.686 0 1 232 61 61 GLY CA C 44.633 0.001 1 233 61 61 GLY N N 107.749 0.027 1 234 62 62 PRO CA C 63.263 0.015 1 235 62 62 PRO N N 133.473 0 1 236 63 63 HIS H H 8.54 0.009 1 237 63 63 HIS CA C 55.956 0.044 1 238 63 63 HIS N N 119.44 0.049 1 239 64 64 PHE H H 8.312 0.003 1 240 64 64 PHE CA C 57.578 0.004 1 241 64 64 PHE N N 122.254 0.061 1 242 65 65 ASN H H 8.643 0.006 1 243 65 65 ASN CA C 50.737 0.015 1 244 65 65 ASN N N 123.001 0.03 1 245 66 66 PRO C C 173.132 0.001 1 246 66 66 PRO CA C 63.487 0.032 1 247 66 66 PRO N N 135.986 0.008 1 248 67 67 LEU H H 8.283 0.003 1 249 67 67 LEU C C 177.257 0.373 1 250 67 67 LEU CA C 55.227 0.038 1 251 67 67 LEU N N 120.848 0.036 1 252 68 68 SER H H 8.208 0.004 1 253 68 68 SER C C 174.609 0.017 1 254 68 68 SER CA C 58.415 0.006 1 255 68 68 SER N N 116.279 0.036 1 256 69 69 ARG H H 8.47 0.007 1 257 69 69 ARG C C 176.204 0 1 258 69 69 ARG CA C 56.169 0.031 1 259 69 69 ARG N N 123.341 0.05 1 260 70 70 LYS H H 8.516 0.005 1 261 70 70 LYS C C 176.389 0 1 262 70 70 LYS CA C 56.43 0 1 263 70 70 LYS N N 122.916 0.049 1 264 71 71 HIS H H 8.603 0.011 1 265 71 71 HIS C C 175.582 0.005 1 266 71 71 HIS CA C 56.2 0.04 1 267 71 71 HIS N N 121.122 0.095 1 268 72 72 GLY H H 8.559 0.007 1 269 72 72 GLY C C 174.112 0.003 1 270 72 72 GLY CA C 45.241 0.027 1 271 72 72 GLY N N 110.627 0.049 1 272 73 73 GLY H H 8.395 0.004 1 273 73 73 GLY C C 171.783 0 1 274 73 73 GLY CA C 44.607 0 1 275 73 73 GLY N N 108.949 0.02 1 276 74 74 PRO C C 177.242 0 1 277 74 74 PRO CA C 63.43 0.037 1 278 75 75 LYS H H 8.596 0.004 1 279 75 75 LYS C C 176.497 0.009 1 280 75 75 LYS CA C 56.633 0.01 1 281 75 75 LYS N N 121.19 0.051 1 282 76 76 ASP H H 8.452 0.007 1 283 76 76 ASP C C 176.316 0 1 284 76 76 ASP CA C 54.768 0.015 1 285 76 76 ASP N N 121.507 0.061 1 286 77 77 GLU H H 8.47 0.004 1 287 77 77 GLU C C 176.373 0 1 288 77 77 GLU CA C 56.679 0.035 1 289 77 77 GLU N N 120.824 0.034 1 290 78 78 GLU H H 8.444 0.003 1 291 78 78 GLU C C 176.285 0 1 292 78 78 GLU CA C 56.683 0.005 1 293 78 78 GLU N N 121.989 0.036 1 294 79 79 ARG H H 8.409 0.008 1 295 79 79 ARG C C 176.01 0.012 1 296 79 79 ARG CA C 56.039 0.049 1 297 79 79 ARG N N 122.129 0.015 1 298 80 80 HIS H H 8.77 0.018 1 299 80 80 HIS C C 174.89 0 1 300 80 80 HIS CA C 55.712 0.04 1 301 80 80 HIS N N 121.697 0.068 1 302 81 81 VAL H H 8.373 0.008 1 303 81 81 VAL C C 176.378 0.011 1 304 81 81 VAL CA C 62.659 0.009 1 305 81 81 VAL N N 121.978 0.031 1 306 82 82 GLY H H 8.534 0.007 1 307 82 82 GLY C C 173.696 0.023 1 308 82 82 GLY CA C 45.219 0.028 1 309 82 82 GLY N N 112.172 0.032 1 310 83 83 ASP H H 8.313 0.005 1 311 83 83 ASP C C 176.585 0.009 1 312 83 83 ASP CA C 54.455 0.006 1 313 83 83 ASP N N 120.564 0.028 1 314 84 84 LEU H H 8.428 0.006 1 315 84 84 LEU C C 177.925 0.005 1 316 84 84 LEU CA C 55.589 0.016 1 317 84 84 LEU N N 122.687 0.046 1 318 85 85 GLY H H 8.515 0.004 1 319 85 85 GLY C C 173.856 0.001 1 320 85 85 GLY CA C 45.385 0.012 1 321 85 85 GLY N N 108.647 0.034 1 322 86 86 ASN H H 8.392 0.004 1 323 86 86 ASN C C 175.338 0.003 1 324 86 86 ASN CA C 53.253 0.026 1 325 86 86 ASN N N 118.877 0.02 1 326 87 87 VAL H H 8.253 0.003 1 327 87 87 VAL C C 176.319 0.002 1 328 87 87 VAL CA C 62.581 0.014 1 329 87 87 VAL N N 120.293 0.039 1 330 88 88 THR H H 8.32 0.002 1 331 88 88 THR C C 174.244 0.005 1 332 88 88 THR CA C 61.78 0.015 1 333 88 88 THR N N 117.495 0.046 1 334 89 89 ALA H H 8.361 0.002 1 335 89 89 ALA C C 177.274 0.011 1 336 89 89 ALA CA C 52.537 0.014 1 337 89 89 ALA N N 126.201 0.036 1 338 90 90 ASP H H 8.416 0.004 1 339 90 90 ASP C C 176.51 0 1 340 90 90 ASP CA C 54.526 0.021 1 341 90 90 ASP N N 119.96 0.041 1 342 91 91 LYS H H 8.379 0.005 1 343 91 91 LYS C C 176.32 0 1 344 91 91 LYS CA C 56.76 0.041 1 345 91 91 LYS N N 121.423 0.035 1 346 92 92 ASP H H 8.45 0.003 1 347 92 92 ASP C C 176.684 0 1 348 92 92 ASP CA C 54.725 0.041 1 349 92 92 ASP N N 120.756 0.05 1 350 93 93 GLY H H 8.333 0.006 1 351 93 93 GLY C C 173.955 0.002 1 352 93 93 GLY CA C 45.499 0.012 1 353 93 93 GLY N N 108.878 0.038 1 354 94 94 VAL H H 8.085 0.005 1 355 94 94 VAL C C 175.844 0.002 1 356 94 94 VAL CA C 62.213 0.015 1 357 94 94 VAL N N 119.17 0.046 1 358 95 95 ALA H H 8.475 0.004 1 359 95 95 ALA C C 177.207 0.001 1 360 95 95 ALA CA C 52.398 0.027 1 361 95 95 ALA N N 127.62 0.044 1 362 96 96 ASP H H 8.414 0.003 1 363 96 96 ASP C C 176.222 0 1 364 96 96 ASP CA C 54.322 0.018 1 365 96 96 ASP N N 120.447 0.028 1 366 97 97 VAL H H 8.135 0.003 1 367 97 97 VAL C C 176.048 0.002 1 368 97 97 VAL CA C 62.022 0.041 1 369 97 97 VAL N N 119.46 0.021 1 370 98 98 SER H H 8.579 0.004 1 371 98 98 SER C C 174.797 0.003 1 372 98 98 SER CA C 58.363 0.015 1 373 98 98 SER N N 119.609 0.055 1 374 99 99 ILE H H 8.308 0.003 1 375 99 99 ILE C C 176.32 0 1 376 99 99 ILE CA C 61.565 0.02 1 377 99 99 ILE N N 123.038 0.054 1 378 100 100 GLU H H 8.553 0.003 1 379 100 100 GLU C C 176.272 0 1 380 100 100 GLU CA C 56.906 0.012 1 381 100 100 GLU N N 124.153 0.028 1 382 101 101 ASP H H 8.371 0.003 1 383 101 101 ASP C C 176.336 0 1 384 101 101 ASP CA C 54.667 0.019 1 385 101 101 ASP N N 121.458 0.032 1 386 102 102 SER H H 8.298 0.003 1 387 102 102 SER C C 174.612 0 1 388 102 102 SER CA C 58.715 0.023 1 389 102 102 SER N N 115.818 0.06 1 390 103 103 VAL H H 8.212 0.002 1 391 103 103 VAL C C 176.176 0 1 392 103 103 VAL CA C 62.721 0.03 1 393 103 103 VAL N N 121.748 0.042 1 394 104 104 ILE H H 8.253 0.003 1 395 104 104 ILE C C 176.202 0.01 1 396 104 104 ILE CA C 61.178 0.029 1 397 104 104 ILE N N 123.972 0.046 1 398 105 105 SER H H 8.461 0.006 1 399 105 105 SER C C 175.621 1.288 1 400 105 105 SER CA C 58.132 0.018 1 401 105 105 SER N N 119.786 0.05 1 402 106 106 LEU H H 8.513 0.007 1 403 106 106 LEU C C 177.463 0 1 404 106 106 LEU CA C 55.276 0.048 1 405 106 106 LEU N N 125.172 0.056 1 406 107 107 SER H H 8.398 0.003 1 407 107 107 SER C C 175.077 0.013 1 408 107 107 SER CA C 58.56 0.028 1 409 107 107 SER N N 115.765 0.052 1 410 108 108 GLY H H 8.435 0.003 1 411 108 108 GLY C C 173.819 0.003 1 412 108 108 GLY CA C 45.441 0.006 1 413 108 108 GLY N N 110.58 0.038 1 414 109 109 ASP H H 8.32 0.005 1 415 109 109 ASP C C 176.405 0 1 416 109 109 ASP CA C 54.557 0.052 1 417 109 109 ASP N N 120.314 0.048 1 418 110 110 HIS H H 8.417 0.018 1 419 110 110 HIS C C 174.558 0.007 1 420 110 110 HIS CA C 55.942 0.039 1 421 110 110 HIS N N 119.136 0.055 1 422 111 111 ALA H H 8.323 0.011 1 423 111 111 ALA C C 177.471 0.017 1 424 111 111 ALA CA C 52.705 0.048 1 425 111 111 ALA N N 124.434 0.037 1 426 112 112 ILE H H 8.283 0.005 1 427 112 112 ILE C C 176.238 0.008 1 428 112 112 ILE CA C 61.195 0.014 1 429 112 112 ILE N N 120.609 0.023 1 430 113 113 ILE H H 8.366 0.006 1 431 113 113 ILE C C 176.639 0.003 1 432 113 113 ILE CA C 61.216 0.012 1 433 113 113 ILE N N 125.565 0.022 1 434 114 114 GLY H H 8.536 0.005 1 435 114 114 GLY C C 173.745 0.023 1 436 114 114 GLY CA C 45.273 0.04 1 437 114 114 GLY N N 113.137 0.069 1 438 115 115 ARG H H 8.309 0.004 1 439 115 115 ARG C C 176.427 0.019 1 440 115 115 ARG CA C 56.135 0.009 1 441 115 115 ARG N N 120.657 0.042 1 442 116 116 THR H H 8.428 0.005 1 443 116 116 THR C C 174.226 0.002 1 444 116 116 THR CA C 62.111 0.052 1 445 116 116 THR N N 116.47 0.031 1 446 117 117 LEU H H 8.473 0.006 1 447 117 117 LEU C C 176.699 0.001 1 448 117 117 LEU CA C 55.171 0.016 1 449 117 117 LEU N N 125.721 0.047 1 450 118 118 VAL H H 8.374 0.004 1 451 118 118 VAL C C 175.801 0.025 1 452 118 118 VAL CA C 62.351 0.017 1 453 118 118 VAL N N 123.07 0.033 1 454 119 119 VAL H H 8.374 0.004 1 455 119 119 VAL C C 175.782 0.013 1 456 119 119 VAL CA C 62.136 0.026 1 457 119 119 VAL N N 125.109 0.06 1 458 120 120 HIS H H 8.646 0.016 1 459 120 120 HIS C C 174.819 0.001 1 460 120 120 HIS CA C 55.75 0.049 1 461 120 120 HIS N N 124.01 0.061 1 462 121 121 GLU H H 8.671 0.012 1 463 121 121 GLU C C 176.198 0.021 1 464 121 121 GLU CA C 56.694 0.013 1 465 121 121 GLU N N 123.321 0.113 1 466 122 122 LYS H H 8.596 0.005 1 467 122 122 LYS C C 176.233 0.013 1 468 122 122 LYS CA C 56.37 0.014 1 469 122 122 LYS N N 122.878 0.046 1 470 123 123 ALA H H 8.516 0.005 1 471 123 123 ALA C C 177.393 0.015 1 472 123 123 ALA CA C 52.552 0.038 1 473 123 123 ALA N N 125.871 0.017 1 474 124 124 ASP H H 8.425 0.004 1 475 124 124 ASP C C 176.051 0.005 1 476 124 124 ASP CA C 54.462 0.04 1 477 124 124 ASP N N 119.811 0.038 1 478 125 125 ASP H H 8.381 0.004 1 479 125 125 ASP C C 176.502 0.014 1 480 125 125 ASP CA C 54.362 0.02 1 481 125 125 ASP N N 120.476 0.052 1 482 126 126 LEU H H 8.323 0.003 1 483 126 126 LEU C C 178.105 0.002 1 484 126 126 LEU CA C 55.667 0.013 1 485 126 126 LEU N N 122.375 0.045 1 486 127 127 GLY H H 8.541 0.003 1 487 127 127 GLY C C 174.374 0.003 1 488 127 127 GLY CA C 45.553 0.026 1 489 127 127 GLY N N 109.004 0.058 1 490 128 128 LYS H H 8.224 0.003 1 491 128 128 LYS C C 177.202 0.023 1 492 128 128 LYS CA C 56.586 0.016 1 493 128 128 LYS N N 120.516 0.043 1 494 129 129 GLY H H 8.563 0.004 1 495 129 129 GLY C C 174.523 0.005 1 496 129 129 GLY CA C 45.354 0.026 1 497 129 129 GLY N N 109.723 0.038 1 498 130 130 GLY H H 8.408 0.004 1 499 130 130 GLY C C 174.021 0.004 1 500 130 130 GLY CA C 45.369 0.011 1 501 130 130 GLY N N 108.671 0.04 1 502 131 131 ASN H H 8.52 0.004 1 503 131 131 ASN C C 175.472 0.007 1 504 131 131 ASN CA C 53.358 0.016 1 505 131 131 ASN N N 118.643 0.043 1 506 132 132 GLU H H 8.71 0.004 1 507 132 132 GLU C C 176.688 0.001 1 508 132 132 GLU CA C 57.218 0.014 1 509 132 132 GLU N N 121.434 0.038 1 510 133 133 GLU H H 8.573 0.003 1 511 133 133 GLU C C 176.859 0.015 1 512 133 133 GLU CA C 56.985 0.013 1 513 133 133 GLU N N 121.667 0.049 1 514 134 134 SER H H 8.442 0.005 1 515 134 134 SER C C 175.122 0.008 1 516 134 134 SER CA C 58.803 0.014 1 517 134 134 SER N N 116.561 0.042 1 518 135 135 THR H H 8.274 0.003 1 519 135 135 THR C C 174.783 0 1 520 135 135 THR CA C 62.24 0.022 1 521 135 135 THR N N 115.535 0.044 1 522 136 136 LYS H H 8.395 0.005 1 523 136 136 LYS C C 176.796 0.006 1 524 136 136 LYS CA C 56.607 0.032 1 525 136 136 LYS N N 123.519 0.036 1 526 137 137 THR H H 8.254 0.003 1 527 137 137 THR C C 175.163 0.002 1 528 137 137 THR CA C 61.958 0.133 1 529 137 137 THR N N 114.341 0.041 1 530 138 138 GLY H H 8.464 0.004 1 531 138 138 GLY C C 173.856 0.004 1 532 138 138 GLY CA C 45.414 0.021 1 533 138 138 GLY N N 110.628 0.019 1 534 139 139 ASN H H 8.466 0.004 1 535 139 139 ASN C C 175.279 0.011 1 536 139 139 ASN CA C 53.237 0.011 1 537 139 139 ASN N N 118.884 0.032 1 538 140 140 ALA H H 8.514 0.007 1 539 140 140 ALA C C 178.112 0.002 1 540 140 140 ALA CA C 53.046 0.047 1 541 140 140 ALA N N 124.867 0.382 1 542 141 141 GLY H H 8.422 0.004 1 543 141 141 GLY C C 174.195 0.006 1 544 141 141 GLY CA C 45.359 0.01 1 545 141 141 GLY N N 107.648 0.04 1 546 142 142 SER H H 8.265 0.003 1 547 142 142 SER C C 174.65 0.016 1 548 142 142 SER CA C 58.475 0.021 1 549 142 142 SER N N 115.566 0.034 1 550 143 143 ARG H H 8.529 0.004 1 551 143 143 ARG C C 176.175 0.036 1 552 143 143 ARG CA C 56.316 0.022 1 553 143 143 ARG N N 123.222 0.076 1 554 144 144 LEU H H 8.413 0.004 1 555 144 144 LEU C C 176.921 0.006 1 556 144 144 LEU CA C 55.079 0.017 1 557 144 144 LEU N N 123.66 0.05 1 558 145 145 ALA H H 8.485 0.003 1 559 145 145 ALA C C 177.462 0.013 1 560 145 145 ALA CA C 52.45 0.037 1 561 145 145 ALA N N 125.227 0.024 1 562 146 146 CYS H H 8.494 0.005 1 563 146 146 CYS C C 175.116 0.006 1 564 146 146 CYS CA C 55.391 0.016 1 565 146 146 CYS N N 118.095 0.028 1 566 147 147 GLY H H 8.617 0.004 1 567 147 147 GLY C C 173.579 0.007 1 568 147 147 GLY CA C 45.451 0.015 1 569 147 147 GLY N N 110.845 0.045 1 570 148 148 VAL H H 8.095 0.004 1 571 148 148 VAL C C 176.101 0.017 1 572 148 148 VAL CA C 62.283 0.042 1 573 148 148 VAL N N 119.432 0.052 1 574 149 149 ILE H H 8.386 0.003 1 575 149 149 ILE C C 176.558 0.015 1 576 149 149 ILE CA C 61.204 0.027 1 577 149 149 ILE N N 125.069 0.066 1 578 150 150 GLY H H 8.518 0.006 1 579 150 150 GLY C C 173.62 0.003 1 580 150 150 GLY CA C 45.234 0.016 1 581 150 150 GLY N N 113.106 0.025 1 582 151 151 ILE H H 8.082 0.004 1 583 151 151 ILE C C 175.79 0.005 1 584 151 151 ILE CA C 61.026 0.02 1 585 151 151 ILE N N 119.944 0.2 1 586 152 152 ALA H H 8.474 0.005 1 587 152 152 ALA C C 176.56 0.001 1 588 152 152 ALA CA C 52.577 0.021 1 589 152 152 ALA N N 128.747 0.059 1 590 153 153 GLN H H 8.09 0.006 1 591 153 153 GLN C C 180.606 0 1 592 153 153 GLN CA C 57.541 0.009 1 593 153 153 GLN N N 125.438 0.038 1 stop_ save_