data_15712 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Backbone chemical shift assignements for monomeric apoSOD1 - variant A4V ; _BMRB_accession_number 15712 _BMRB_flat_file_name bmr15712.str _Entry_type original _Submission_date 2008-04-03 _Accession_date 2008-04-03 _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 Teilum Kaare . . 2 Akke Mikael . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 132 "13C chemical shifts" 401 "15N chemical shifts" 132 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2009-11-05 update BMRB 'complete entry citation' 2009-10-01 original author 'original release' stop_ loop_ _Related_BMRB_accession_number _Relationship 15711 'SOD1, wild type' 15713 'SOD1, mutant G85R' 15714 'SOD1, mutant D90A' stop_ save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title 'Transient structural distortion of metal-free Cu/Zn superoxide dismutase triggers aberrant oligomerization.' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 19828437 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Teilum Kaare . . 2 Smith Melanie H. . 3 Schulz Eike . . 4 Christensen Lea C. . 5 Solomentsev Gleb . . 6 Oliveberg Mikael . . 7 Akke Mikael . . stop_ _Journal_abbreviation 'Proc. Natl. Acad. Sci. U.S.A.' _Journal_name_full 'Proceedings of the National Academy of Sciences of the United States of America' _Journal_volume 106 _Journal_issue 43 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 18273 _Page_last 18278 _Year 2009 _Details . save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name SOD1 _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label chain $SOD1 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_SOD1 _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common SOD1 _Molecular_mass . _Mol_thiol_state 'all disulfide bound' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 153 _Mol_residue_sequence ; ATKVVAVLKGDGPVQGIINF EQKESNGPVKVWGSIKGLTE GLHGFHVHEEEDNTAGCTSA GPHFNPLSRKHGGPKDEERH VGDLGNVTADKDGVADVSIE DSVISLSGDHAIIGRTLVVH EKADDLGKGGNEESTKTGNA GSRLACGVIGIAQ ; loop_ _Residue_seq_code _Residue_label 1 ALA 2 THR 3 LYS 4 VAL 5 VAL 6 ALA 7 VAL 8 LEU 9 LYS 10 GLY 11 ASP 12 GLY 13 PRO 14 VAL 15 GLN 16 GLY 17 ILE 18 ILE 19 ASN 20 PHE 21 GLU 22 GLN 23 LYS 24 GLU 25 SER 26 ASN 27 GLY 28 PRO 29 VAL 30 LYS 31 VAL 32 TRP 33 GLY 34 SER 35 ILE 36 LYS 37 GLY 38 LEU 39 THR 40 GLU 41 GLY 42 LEU 43 HIS 44 GLY 45 PHE 46 HIS 47 VAL 48 HIS 49 GLU 50 GLU 51 GLU 52 ASP 53 ASN 54 THR 55 ALA 56 GLY 57 CYS 58 THR 59 SER 60 ALA 61 GLY 62 PRO 63 HIS 64 PHE 65 ASN 66 PRO 67 LEU 68 SER 69 ARG 70 LYS 71 HIS 72 GLY 73 GLY 74 PRO 75 LYS 76 ASP 77 GLU 78 GLU 79 ARG 80 HIS 81 VAL 82 GLY 83 ASP 84 LEU 85 GLY 86 ASN 87 VAL 88 THR 89 ALA 90 ASP 91 LYS 92 ASP 93 GLY 94 VAL 95 ALA 96 ASP 97 VAL 98 SER 99 ILE 100 GLU 101 ASP 102 SER 103 VAL 104 ILE 105 SER 106 LEU 107 SER 108 GLY 109 ASP 110 HIS 111 ALA 112 ILE 113 ILE 114 GLY 115 ARG 116 THR 117 LEU 118 VAL 119 VAL 120 HIS 121 GLU 122 LYS 123 ALA 124 ASP 125 ASP 126 LEU 127 GLY 128 LYS 129 GLY 130 GLY 131 ASN 132 GLU 133 GLU 134 SER 135 THR 136 LYS 137 THR 138 GLY 139 ASN 140 ALA 141 GLY 142 SER 143 ARG 144 LEU 145 ALA 146 CYS 147 GLY 148 VAL 149 ILE 150 GLY 151 ILE 152 ALA 153 GLN stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-08-05 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 99.35 99.35 1.88e-102 BMRB 15713 SOD1 100.00 153 98.69 98.69 1.95e-101 BMRB 15714 SOD1 100.00 153 98.69 98.69 1.85e-101 BMRB 18509 Superoxide_dismutase_C6A-C111S_thermostable_mutant 100.00 153 97.39 98.04 1.22e-99 BMRB 18708 SUPEROXIDE_DISMUTASE_CU-ZN 100.00 153 97.39 98.04 1.22e-99 BMRB 18968 SOD1 100.00 153 99.35 99.35 1.88e-102 BMRB 26570 SOD1 100.00 153 97.39 98.04 1.22e-99 BMRB 4202 "Superoxide Dismutase" 100.00 153 98.04 99.35 1.12e-101 PDB 1BA9 "The Solution Structure Of Reduced Monomeric Superoxide Dismutase, Nmr, 36 Structures" 99.35 153 98.03 99.34 5.44e-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 97.37 98.03 1.88e-99 PDB 1KMG "The Solution Structure Of Monomeric Copper-Free Superoxide Dismutase" 100.00 153 98.04 99.35 1.12e-101 PDB 1L3N "The Solution Structure Of Reduced Dimeric Copper Zinc Sod: The Structural Effects Of Dimerization" 100.00 153 97.39 98.04 1.22e-99 PDB 1MFM "Monomeric Human Sod Mutant F50eG51EE133Q AT ATOMIC Resolution" 100.00 153 98.04 99.35 1.12e-101 PDB 1N18 "Thermostable Mutant Of Human Superoxide Dismutase, C6a, C111s" 100.00 154 97.39 98.04 9.96e-100 PDB 1N19 "Structure Of The Hsod A4v Mutant" 100.00 154 98.04 98.69 2.96e-100 PDB 1RK7 "Solution Structure Of Apo Cu,Zn Superoxide Dismutase: Role Of Metal Ions In Protein Folding" 100.00 153 98.04 99.35 1.12e-101 PDB 1SOS "Atomic Structures Of Wild-type And Thermostable Mutant Recombinant Human Cu, Zn Superoxide Dismutase" 100.00 154 97.39 98.04 1.27e-99 PDB 1UXM "A4v Mutant Of Human Sod1" 100.00 153 97.39 97.39 2.52e-99 PDB 2AF2 "Solution Structure Of Disulfide Reduced And Copper Depleted Human Superoxide Dismutase" 100.00 153 97.39 98.04 1.22e-99 PDB 2GBT "C6aC111A CUZN SUPEROXIDE DISMUTASE" 100.00 153 98.04 98.04 3.76e-100 PDB 2LU5 "Structure And Chemical Shifts Of Cu(I),Zn(Ii) Superoxide Dismutase By Solid-State Nmr" 100.00 153 97.39 98.04 1.22e-99 PDB 2XJK "Monomeric Human Cu,Zn Superoxide Dismutase" 100.00 153 99.35 99.35 1.88e-102 PDB 2XJL "Monomeric Human Cu,Zn Superoxide Dismutase Without Cu Ligands" 100.00 153 97.39 97.39 1.25e-99 PDB 3GZQ "Human Sod1 A4v Metal-Free Variant" 100.00 154 97.39 97.39 2.60e-99 PDB 4BCY "Monomeric Human Cu,zn Superoxide Dismutase, Mutation H43f" 100.00 153 98.69 98.69 2.59e-101 GB AAA72747 "CuZn superoxide dismutase [synthetic construct]" 100.00 154 97.39 98.04 9.96e-100 GB AAA80237 "HSOD-GlyProGly-A+, partial [synthetic construct]" 100.00 171 97.39 98.04 3.84e-99 GB AAB27818 "Cu,Zn superoxide dismutase, SOD=SOD1 gene product {A to V single-site mutation} [human, Peptide Mutant, 153 aa]" 100.00 153 97.39 97.39 2.52e-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 . N/A 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 1 mM '[U-100% 13C; U-100% 15N]' MES 10 mM 'natural abundance' EDTA 1 mM 'natural abundance' D2O 10 % 'natural abundance' 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_SPARKY _Saveframe_category software _Name SPARKY _Version . loop_ _Vendor _Address _Electronic_address Goddard . . stop_ loop_ _Task 'chemical shift assignment' stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model INOVA _Field_strength 600 _Details . save_ ############################# # NMR applied experiments # ############################# save_2D_1H-15N_HSQC_1 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-15N HSQC' _Sample_label $sample_1 save_ save_3D_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_CBCA(CO)NH_5 _Saveframe_category NMR_applied_experiment _Experiment_name '3D CBCA(CO)NH' _Sample_label $sample_1 save_ save_3D_(HCA)CO(CA)NH_6 _Saveframe_category NMR_applied_experiment _Experiment_name '3D (HCA)CO(CA)NH' _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' 0.01 . M 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 DSS C 13 'methyl protons' ppm 0.00 na indirect . . . 0.251449530 water H 1 protons ppm 4.773 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 HNCACB' '3D CBCA(CO)NH' '3D (HCA)CO(CA)NH' 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 chain _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 173.017 0.030 1 2 2 2 THR CA C 62.569 0.033 1 3 3 3 LYS H H 8.605 0.030 1 4 3 3 LYS C C 175.165 0.007 1 5 3 3 LYS CA C 55.705 0.023 1 6 3 3 LYS CB C 35.011 0.007 1 7 3 3 LYS N N 126.661 0.019 1 8 4 4 VAL H H 8.753 0.001 1 9 4 4 VAL C C 174.292 0.015 1 10 4 4 VAL CA C 60.626 0.030 1 11 4 4 VAL N N 121.286 0.012 1 12 5 5 VAL H H 8.953 0.002 1 13 5 5 VAL C C 174.638 0.011 1 14 5 5 VAL CA C 59.754 0.014 1 15 5 5 VAL CB C 37.250 0.030 1 16 5 5 VAL N N 121.228 0.017 1 17 6 6 ALA H H 9.410 0.002 1 18 6 6 ALA C C 174.750 0.001 1 19 6 6 ALA CA C 51.063 0.031 1 20 6 6 ALA CB C 23.513 0.030 1 21 6 6 ALA N N 126.431 0.015 1 22 7 7 VAL H H 9.161 0.001 1 23 7 7 VAL C C 175.726 0.011 1 24 7 7 VAL CA C 62.010 0.094 1 25 7 7 VAL CB C 31.742 0.018 1 26 7 7 VAL N N 125.393 0.010 1 27 8 8 LEU H H 8.713 0.003 1 28 8 8 LEU C C 176.014 0.030 1 29 8 8 LEU CA C 54.161 0.015 1 30 8 8 LEU CB C 43.304 0.047 1 31 8 8 LEU N N 126.381 0.049 1 32 9 9 LYS H H 8.316 0.003 1 33 9 9 LYS C C 175.349 0.011 1 34 9 9 LYS CA C 55.331 0.011 1 35 9 9 LYS CB C 36.522 0.035 1 36 9 9 LYS N N 121.184 0.031 1 37 10 10 GLY H H 8.590 0.001 1 38 10 10 GLY C C 172.556 0.022 1 39 10 10 GLY CA C 45.484 0.126 1 40 10 10 GLY N N 111.990 0.009 1 41 11 11 ASP H H 8.746 0.001 1 42 11 11 ASP C C 176.879 0.018 1 43 11 11 ASP CA C 54.734 0.018 1 44 11 11 ASP CB C 41.079 0.004 1 45 11 11 ASP N N 121.224 0.025 1 46 12 12 GLY H H 8.208 0.001 1 47 12 12 GLY C C 173.503 0.030 1 48 12 12 GLY CA C 44.615 0.072 1 49 12 12 GLY N N 110.524 0.008 1 50 13 13 PRO C C 176.531 0.030 1 51 13 13 PRO CA C 63.470 0.030 1 52 13 13 PRO CB C 32.429 0.030 1 53 14 14 VAL H H 7.403 0.001 1 54 14 14 VAL C C 175.946 0.010 1 55 14 14 VAL CA C 62.986 0.042 1 56 14 14 VAL CB C 30.879 0.030 1 57 14 14 VAL N N 120.876 0.035 1 58 15 15 GLN H H 8.070 0.003 1 59 15 15 GLN C C 174.262 0.006 1 60 15 15 GLN CA C 54.255 0.037 1 61 15 15 GLN CB C 32.443 0.011 1 62 15 15 GLN N N 123.597 0.007 1 63 16 16 GLY H H 8.299 0.002 1 64 16 16 GLY C C 170.837 0.030 1 65 16 16 GLY CA C 46.837 0.087 1 66 16 16 GLY N N 107.976 0.017 1 67 17 17 ILE H H 8.021 0.001 1 68 17 17 ILE C C 174.044 0.006 1 69 17 17 ILE CA C 61.128 0.018 1 70 17 17 ILE CB C 40.683 0.018 1 71 17 17 ILE N N 120.799 0.015 1 72 18 18 ILE H H 8.788 0.003 1 73 18 18 ILE C C 172.695 0.012 1 74 18 18 ILE CA C 56.832 0.014 1 75 18 18 ILE CB C 37.635 0.030 1 76 18 18 ILE N N 126.703 0.013 1 77 19 19 ASN H H 8.759 0.001 1 78 19 19 ASN C C 172.589 0.002 1 79 19 19 ASN CA C 52.367 0.033 1 80 19 19 ASN CB C 40.578 0.057 1 81 19 19 ASN N N 124.622 0.020 1 82 20 20 PHE H H 8.478 0.002 1 83 20 20 PHE C C 175.605 0.002 1 84 20 20 PHE CA C 55.680 0.021 1 85 20 20 PHE CB C 42.209 0.040 1 86 20 20 PHE N N 115.907 0.009 1 87 21 21 GLU H H 9.531 0.001 1 88 21 21 GLU C C 173.782 0.008 1 89 21 21 GLU CA C 55.617 0.016 1 90 21 21 GLU CB C 34.969 0.036 1 91 21 21 GLU N N 121.689 0.015 1 92 22 22 GLN H H 9.172 0.002 1 93 22 22 GLN C C 174.421 0.022 1 94 22 22 GLN CA C 54.803 0.005 1 95 22 22 GLN CB C 32.276 0.019 1 96 22 22 GLN N N 128.986 0.024 1 97 23 23 LYS H H 9.126 0.002 1 98 23 23 LYS C C 176.359 0.012 1 99 23 23 LYS CA C 59.224 0.018 1 100 23 23 LYS CB C 33.230 0.062 1 101 23 23 LYS N N 129.020 0.014 1 102 24 24 GLU H H 8.115 0.002 1 103 24 24 GLU C C 177.190 0.010 1 104 24 24 GLU CA C 54.537 0.024 1 105 24 24 GLU CB C 32.210 0.009 1 106 24 24 GLU N N 116.050 0.017 1 107 25 25 SER H H 8.833 0.002 1 108 25 25 SER C C 174.653 0.005 1 109 25 25 SER CA C 61.100 0.056 1 110 25 25 SER CB C 62.744 0.032 1 111 25 25 SER N N 118.530 0.023 1 112 26 26 ASN H H 8.412 0.001 1 113 26 26 ASN C C 175.089 0.012 1 114 26 26 ASN CA C 53.131 0.028 1 115 26 26 ASN CB C 38.231 0.007 1 116 26 26 ASN N N 117.234 0.039 1 117 27 27 GLY H H 7.927 0.001 1 118 27 27 GLY C C 171.894 0.030 1 119 27 27 GLY CA C 44.668 0.063 1 120 27 27 GLY N N 108.072 0.010 1 121 28 28 PRO C C 176.224 0.030 1 122 28 28 PRO CA C 63.001 0.011 1 123 28 28 PRO CB C 32.863 0.030 1 124 29 29 VAL H H 8.910 0.002 1 125 29 29 VAL C C 175.139 0.012 1 126 29 29 VAL CA C 61.302 0.017 1 127 29 29 VAL CB C 33.472 0.034 1 128 29 29 VAL N N 121.721 0.017 1 129 30 30 LYS H H 9.243 0.002 1 130 30 30 LYS C C 175.094 0.006 1 131 30 30 LYS CA C 55.756 0.011 1 132 30 30 LYS CB C 34.479 0.047 1 133 30 30 LYS N N 128.634 0.014 1 134 31 31 VAL H H 9.186 0.003 1 135 31 31 VAL C C 175.471 0.002 1 136 31 31 VAL CA C 60.412 0.025 1 137 31 31 VAL CB C 33.512 0.022 1 138 31 31 VAL N N 126.802 0.022 1 139 32 32 TRP H H 8.949 0.001 1 140 32 32 TRP C C 173.561 0.013 1 141 32 32 TRP CA C 55.935 0.017 1 142 32 32 TRP CB C 32.517 0.020 1 143 32 32 TRP N N 124.993 0.025 1 144 33 33 GLY H H 8.544 0.001 1 145 33 33 GLY C C 171.302 0.030 1 146 33 33 GLY CA C 44.855 0.083 1 147 33 33 GLY N N 108.898 0.005 1 148 34 34 SER H H 7.879 0.001 1 149 34 34 SER C C 172.839 0.021 1 150 34 34 SER CA C 57.075 0.011 1 151 34 34 SER CB C 65.370 0.005 1 152 34 34 SER N N 114.308 0.007 1 153 35 35 ILE H H 8.663 0.001 1 154 35 35 ILE C C 173.174 0.011 1 155 35 35 ILE CA C 60.221 0.023 1 156 35 35 ILE CB C 41.365 0.083 1 157 35 35 ILE N N 123.897 0.019 1 158 36 36 LYS H H 9.029 0.001 1 159 36 36 LYS C C 175.555 0.018 1 160 36 36 LYS CA C 54.587 0.017 1 161 36 36 LYS CB C 35.323 0.019 1 162 36 36 LYS N N 124.269 0.038 1 163 37 37 GLY H H 8.304 0.004 1 164 37 37 GLY C C 174.695 0.015 1 165 37 37 GLY CA C 45.794 0.084 1 166 37 37 GLY N N 106.401 0.019 1 167 38 38 LEU H H 8.337 0.001 1 168 38 38 LEU C C 176.931 0.010 1 169 38 38 LEU CA C 53.584 0.024 1 170 38 38 LEU CB C 44.191 0.025 1 171 38 38 LEU N N 120.460 0.029 1 172 39 39 THR H H 7.936 0.002 1 173 39 39 THR C C 175.737 0.030 1 174 39 39 THR CA C 61.237 0.009 1 175 39 39 THR CB C 69.595 0.005 1 176 39 39 THR N N 110.557 0.027 1 177 40 40 GLU H H 8.711 0.002 1 178 40 40 GLU C C 175.986 0.030 1 179 40 40 GLU CA C 57.591 0.009 1 180 40 40 GLU CB C 30.560 0.065 1 181 40 40 GLU N N 126.298 0.030 1 182 41 41 GLY H H 8.668 0.002 1 183 41 41 GLY C C 172.904 0.030 1 184 41 41 GLY CA C 43.318 0.008 1 185 41 41 GLY N N 113.545 0.036 1 186 42 42 LEU H H 8.241 0.004 1 187 42 42 LEU C C 177.246 0.014 1 188 42 42 LEU CA C 55.169 0.030 1 189 42 42 LEU CB C 44.634 0.030 1 190 42 42 LEU N N 120.505 0.038 1 191 43 43 HIS H H 8.779 0.004 1 192 43 43 HIS C C 173.817 0.005 1 193 43 43 HIS CA C 54.667 0.017 1 194 43 43 HIS N N 116.518 0.021 1 195 44 44 GLY H H 8.649 0.001 1 196 44 44 GLY C C 172.222 0.030 1 197 44 44 GLY CA C 46.362 0.053 1 198 44 44 GLY N N 112.278 0.015 1 199 45 45 PHE H H 8.730 0.002 1 200 45 45 PHE C C 173.763 0.005 1 201 45 45 PHE CA C 55.120 0.045 1 202 45 45 PHE CB C 41.872 0.030 1 203 45 45 PHE N N 127.423 0.030 1 204 46 46 HIS H H 8.809 0.001 1 205 46 46 HIS C C 173.315 0.001 1 206 46 46 HIS CA C 53.547 0.015 1 207 46 46 HIS CB C 35.104 0.021 1 208 46 46 HIS N N 121.357 0.029 1 209 47 47 VAL H H 9.077 0.003 1 210 47 47 VAL C C 175.774 0.004 1 211 47 47 VAL CA C 61.423 0.023 1 212 47 47 VAL CB C 32.730 0.015 1 213 47 47 VAL N N 121.956 0.057 1 214 48 48 HIS H H 9.678 0.003 1 215 48 48 HIS C C 174.690 0.016 1 216 48 48 HIS CA C 55.650 0.060 1 217 48 48 HIS CB C 32.161 0.073 1 218 48 48 HIS N N 128.312 0.020 1 219 49 49 GLU H H 8.912 0.002 1 220 49 49 GLU C C 175.575 0.009 1 221 49 49 GLU CA C 56.514 0.047 1 222 49 49 GLU CB C 30.510 0.030 1 223 49 49 GLU N N 123.526 0.063 1 224 50 50 GLU H H 8.729 0.002 1 225 50 50 GLU C C 176.128 0.028 1 226 50 50 GLU CA C 56.495 0.030 1 227 50 50 GLU CB C 30.633 0.007 1 228 50 50 GLU N N 122.316 0.087 1 229 51 51 GLU H H 8.585 0.002 1 230 51 51 GLU C C 175.978 0.030 1 231 51 51 GLU CA C 56.716 0.012 1 232 51 51 GLU CB C 30.566 0.030 1 233 51 51 GLU N N 121.686 0.034 1 234 52 52 ASP C C 176.065 0.030 1 235 52 52 ASP CA C 54.139 0.030 1 236 52 52 ASP CB C 41.234 0.007 1 237 53 53 ASN H H 8.474 0.002 1 238 53 53 ASN C C 175.947 0.030 1 239 53 53 ASN CA C 53.764 0.017 1 240 53 53 ASN CB C 38.710 0.033 1 241 53 53 ASN N N 119.496 0.048 1 242 54 54 THR H H 8.244 0.001 1 243 54 54 THR C C 174.832 0.012 1 244 54 54 THR CA C 62.774 0.013 1 245 54 54 THR CB C 69.627 0.005 1 246 54 54 THR N N 113.462 0.030 1 247 55 55 ALA H H 8.182 0.001 1 248 55 55 ALA C C 177.964 0.010 1 249 55 55 ALA CA C 52.803 0.034 1 250 55 55 ALA CB C 19.135 0.012 1 251 55 55 ALA N N 125.271 0.007 1 252 56 56 GLY H H 8.169 0.003 1 253 56 56 GLY C C 174.335 0.008 1 254 56 56 GLY CA C 45.572 0.125 1 255 56 56 GLY N N 107.412 0.042 1 256 57 57 CYS H H 8.542 0.004 1 257 57 57 CYS C C 174.769 0.005 1 258 57 57 CYS CA C 55.925 0.021 1 259 57 57 CYS CB C 41.135 0.051 1 260 57 57 CYS N N 118.738 0.019 1 261 58 58 THR H H 8.150 0.005 1 262 58 58 THR C C 174.557 0.036 1 263 58 58 THR CA C 62.016 0.026 1 264 58 58 THR CB C 69.871 0.118 1 265 58 58 THR N N 113.985 0.035 1 266 59 59 SER H H 8.368 0.004 1 267 59 59 SER C C 174.059 0.037 1 268 59 59 SER CA C 58.441 0.046 1 269 59 59 SER CB C 63.840 0.043 1 270 59 59 SER N N 118.091 0.036 1 271 60 60 ALA H H 8.265 0.001 1 272 60 60 ALA C C 177.574 0.014 1 273 60 60 ALA CA C 52.475 0.029 1 274 60 60 ALA CB C 19.714 0.021 1 275 60 60 ALA N N 125.593 0.015 1 276 61 61 GLY H H 8.134 0.001 1 277 61 61 GLY C C 171.890 0.030 1 278 61 61 GLY CA C 44.747 0.079 1 279 61 61 GLY N N 107.880 0.014 1 280 62 62 PRO C C 176.588 0.030 1 281 62 62 PRO CA C 62.588 0.001 1 282 62 62 PRO CB C 34.814 0.030 1 283 63 63 HIS H H 8.635 0.001 1 284 63 63 HIS C C 176.277 0.129 1 285 63 63 HIS CA C 56.575 0.044 1 286 63 63 HIS CB C 33.186 0.028 1 287 63 63 HIS N N 122.203 0.031 1 288 64 64 PHE H H 8.510 0.004 1 289 64 64 PHE CA C 54.835 0.030 1 290 64 64 PHE CB C 41.103 0.030 1 291 64 64 PHE N N 121.911 0.067 1 292 66 66 PRO C C 177.083 0.003 1 293 66 66 PRO CA C 63.693 0.025 1 294 66 66 PRO CB C 32.215 0.009 1 295 67 67 LEU H H 8.090 0.001 1 296 67 67 LEU C C 177.628 0.005 1 297 67 67 LEU CA C 55.370 0.024 1 298 67 67 LEU CB C 41.776 0.020 1 299 67 67 LEU N N 119.673 0.016 1 300 68 68 SER H H 7.929 0.001 1 301 68 68 SER C C 174.608 0.030 1 302 68 68 SER CA C 58.549 0.018 1 303 68 68 SER CB C 63.721 0.030 1 304 68 68 SER N N 115.374 0.020 1 305 69 69 ARG C C 176.194 0.030 1 306 69 69 ARG CA C 56.042 0.012 1 307 69 69 ARG CB C 30.653 0.017 1 308 70 70 LYS H H 8.284 0.002 1 309 70 70 LYS C C 176.385 0.021 1 310 70 70 LYS CA C 56.487 0.032 1 311 70 70 LYS CB C 33.026 0.010 1 312 70 70 LYS N N 121.997 0.050 1 313 71 71 HIS H H 8.461 0.002 1 314 71 71 HIS C C 175.239 0.005 1 315 71 71 HIS CA C 55.761 0.021 1 316 71 71 HIS CB C 30.048 0.018 1 317 71 71 HIS N N 119.924 0.006 1 318 72 72 GLY H H 8.505 0.002 1 319 72 72 GLY C C 174.187 0.016 1 320 72 72 GLY CA C 45.317 0.114 1 321 72 72 GLY N N 110.568 0.011 1 322 73 73 GLY H H 8.295 0.002 1 323 73 73 GLY C C 171.972 0.030 1 324 73 73 GLY CA C 44.671 0.066 1 325 73 73 GLY N N 109.153 0.017 1 326 74 74 PRO C C 177.450 0.005 1 327 74 74 PRO CA C 63.481 0.025 1 328 74 74 PRO CB C 32.248 0.030 1 329 75 75 LYS H H 8.501 0.001 1 330 75 75 LYS C C 176.603 0.030 1 331 75 75 LYS CA C 56.486 0.016 1 332 75 75 LYS CB C 32.819 0.030 1 333 75 75 LYS N N 120.761 0.015 1 334 79 79 ARG H H 8.198 0.001 1 335 79 79 ARG C C 175.961 0.016 1 336 79 79 ARG CA C 56.046 0.013 1 337 79 79 ARG CB C 30.954 0.011 1 338 79 79 ARG N N 121.513 0.008 1 339 80 80 HIS H H 8.666 0.002 1 340 80 80 HIS C C 174.743 0.030 1 341 80 80 HIS CA C 55.653 0.020 1 342 80 80 HIS CB C 29.450 0.030 1 343 80 80 HIS N N 120.350 0.015 1 344 81 81 VAL C C 175.985 0.001 1 345 81 81 VAL CA C 62.495 0.002 1 346 82 82 GLY H H 8.755 0.004 1 347 82 82 GLY C C 171.377 0.030 1 348 82 82 GLY CA C 45.321 0.091 1 349 82 82 GLY N N 112.587 0.085 1 350 84 84 LEU C C 176.487 0.030 1 351 85 85 GLY H H 8.447 0.003 1 352 85 85 GLY C C 172.195 0.030 1 353 85 85 GLY CA C 44.730 0.103 1 354 85 85 GLY N N 108.941 0.030 1 355 86 86 ASN H H 8.290 0.002 1 356 86 86 ASN C C 177.041 0.014 1 357 86 86 ASN CA C 52.707 0.008 1 358 86 86 ASN CB C 41.791 0.047 1 359 86 86 ASN N N 116.773 0.009 1 360 87 87 VAL H H 9.032 0.002 1 361 87 87 VAL C C 174.588 0.009 1 362 87 87 VAL CA C 59.231 0.005 1 363 87 87 VAL CB C 32.960 0.013 1 364 87 87 VAL N N 114.934 0.023 1 365 88 88 THR H H 8.584 0.003 1 366 88 88 THR C C 173.578 0.004 1 367 88 88 THR CA C 61.722 0.016 1 368 88 88 THR CB C 70.017 0.083 1 369 88 88 THR N N 118.517 0.024 1 370 89 89 ALA H H 9.216 0.002 1 371 89 89 ALA C C 177.534 0.011 1 372 89 89 ALA CA C 49.611 0.027 1 373 89 89 ALA CB C 21.267 0.028 1 374 89 89 ALA N N 129.283 0.025 1 375 90 90 ASP H H 8.503 0.001 1 376 90 90 ASP C C 177.104 0.008 1 377 90 90 ASP CA C 52.663 0.017 1 378 90 90 ASP CB C 41.663 0.012 1 379 90 90 ASP N N 125.016 0.013 1 380 91 91 LYS H H 8.188 0.001 1 381 91 91 LYS C C 177.239 0.017 1 382 91 91 LYS CA C 58.567 0.017 1 383 91 91 LYS CB C 31.889 0.011 1 384 91 91 LYS N N 115.259 0.004 1 385 92 92 ASP H H 8.166 0.001 1 386 92 92 ASP C C 176.315 0.004 1 387 92 92 ASP CA C 54.413 0.022 1 388 92 92 ASP CB C 41.596 0.010 1 389 92 92 ASP N N 119.637 0.023 1 390 93 93 GLY H H 8.439 0.003 1 391 93 93 GLY C C 172.890 0.014 1 392 93 93 GLY CA C 47.020 0.070 1 393 93 93 GLY N N 111.518 0.008 1 394 94 94 VAL H H 7.955 0.003 1 395 94 94 VAL C C 176.550 0.011 1 396 94 94 VAL CA C 61.633 0.022 1 397 94 94 VAL CB C 33.023 0.041 1 398 94 94 VAL N N 119.454 0.058 1 399 95 95 ALA H H 9.577 0.003 1 400 95 95 ALA C C 174.877 0.001 1 401 95 95 ALA CA C 50.251 0.041 1 402 95 95 ALA CB C 21.184 0.042 1 403 95 95 ALA N N 131.307 0.032 1 404 96 96 ASP H H 8.616 0.002 1 405 96 96 ASP C C 175.567 0.011 1 406 96 96 ASP CA C 54.125 0.024 1 407 96 96 ASP CB C 41.873 0.018 1 408 96 96 ASP N N 125.273 0.015 1 409 97 97 VAL H H 8.650 0.003 1 410 97 97 VAL C C 176.622 0.006 1 411 97 97 VAL CA C 62.006 0.015 1 412 97 97 VAL CB C 33.714 0.022 1 413 97 97 VAL N N 125.075 0.072 1 414 98 98 SER H H 8.848 0.001 1 415 98 98 SER C C 173.034 0.030 1 416 98 98 SER CA C 58.359 0.017 1 417 98 98 SER CB C 62.630 0.017 1 418 98 98 SER N N 123.736 0.042 1 419 99 99 ILE H H 9.415 0.002 1 420 99 99 ILE C C 174.587 0.006 1 421 99 99 ILE CA C 60.327 0.018 1 422 99 99 ILE CB C 44.046 0.016 1 423 99 99 ILE N N 126.777 0.015 1 424 100 100 GLU H H 8.630 0.001 1 425 100 100 GLU C C 175.000 0.004 1 426 100 100 GLU CA C 55.646 0.029 1 427 100 100 GLU CB C 32.482 0.030 1 428 100 100 GLU N N 124.713 0.008 1 429 101 101 ASP H H 9.190 0.002 1 430 101 101 ASP C C 175.088 0.016 1 431 101 101 ASP CA C 54.106 0.022 1 432 101 101 ASP CB C 46.297 0.003 1 433 101 101 ASP N N 126.288 0.051 1 434 102 102 SER H H 8.892 0.001 1 435 102 102 SER C C 173.791 0.012 1 436 102 102 SER CA C 58.726 0.016 1 437 102 102 SER CB C 64.150 0.079 1 438 102 102 SER N N 119.376 0.015 1 439 103 103 VAL H H 8.833 0.003 1 440 103 103 VAL C C 177.768 0.009 1 441 103 103 VAL CA C 64.160 0.051 1 442 103 103 VAL CB C 32.708 0.030 1 443 103 103 VAL N N 122.962 0.043 1 444 104 104 ILE H H 7.831 0.002 1 445 104 104 ILE C C 173.067 0.021 1 446 104 104 ILE CA C 61.570 0.011 1 447 104 104 ILE CB C 39.827 0.030 1 448 104 104 ILE N N 113.960 0.025 1 449 105 105 SER H H 7.689 0.004 1 450 105 105 SER C C 173.788 0.018 1 451 105 105 SER CA C 56.660 0.014 1 452 105 105 SER CB C 65.403 0.034 1 453 105 105 SER N N 109.296 0.021 1 454 106 106 LEU H H 8.425 0.007 1 455 106 106 LEU C C 175.142 0.005 1 456 106 106 LEU CA C 55.031 0.007 1 457 106 106 LEU CB C 41.093 0.013 1 458 106 106 LEU N N 121.786 0.059 1 459 107 107 SER H H 8.251 0.002 1 460 107 107 SER C C 173.654 0.012 1 461 107 107 SER CA C 57.308 0.033 1 462 107 107 SER CB C 65.865 0.010 1 463 107 107 SER N N 112.872 0.032 1 464 108 108 GLY H H 8.604 0.001 1 465 108 108 GLY C C 175.293 0.030 1 466 108 108 GLY CA C 44.883 0.072 1 467 108 108 GLY N N 108.692 0.007 1 468 109 109 ASP H H 8.614 0.001 1 469 109 109 ASP C C 177.029 0.010 1 470 109 109 ASP CA C 56.469 0.030 1 471 109 109 ASP CB C 40.483 0.030 1 472 109 109 ASP N N 119.995 0.014 1 473 110 110 HIS H H 8.815 0.001 1 474 110 110 HIS C C 173.781 0.014 1 475 110 110 HIS CA C 53.921 0.031 1 476 110 110 HIS CB C 27.887 0.011 1 477 110 110 HIS N N 116.918 0.022 1 478 111 111 ALA H H 7.079 0.001 1 479 111 111 ALA C C 179.601 0.004 1 480 111 111 ALA CA C 52.363 0.023 1 481 111 111 ALA CB C 19.677 0.052 1 482 111 111 ALA N N 121.322 0.017 1 483 112 112 ILE H H 7.764 0.004 1 484 112 112 ILE C C 175.239 0.030 1 485 112 112 ILE CA C 62.066 0.008 1 486 112 112 ILE CB C 37.802 0.004 1 487 112 112 ILE N N 108.900 0.019 1 488 113 113 ILE H H 6.318 0.002 1 489 113 113 ILE C C 176.730 0.018 1 490 113 113 ILE CA C 63.216 0.024 1 491 113 113 ILE CB C 36.912 0.076 1 492 113 113 ILE N N 119.181 0.023 1 493 114 114 GLY H H 9.096 0.003 1 494 114 114 GLY C C 174.512 0.030 1 495 114 114 GLY CA C 45.269 0.122 1 496 114 114 GLY N N 116.705 0.025 1 497 115 115 ARG H H 7.781 0.002 1 498 115 115 ARG C C 174.117 0.030 1 499 115 115 ARG CA C 55.682 0.019 1 500 115 115 ARG CB C 30.432 0.002 1 501 115 115 ARG N N 119.162 0.024 1 502 116 116 THR H H 8.421 0.002 1 503 116 116 THR C C 173.079 0.004 1 504 116 116 THR CA C 62.263 0.024 1 505 116 116 THR CB C 70.361 0.007 1 506 116 116 THR N N 113.767 0.085 1 507 117 117 LEU H H 9.192 0.004 1 508 117 117 LEU C C 174.560 0.027 1 509 117 117 LEU CA C 53.707 0.013 1 510 117 117 LEU CB C 44.054 0.011 1 511 117 117 LEU N N 129.361 0.045 1 512 118 118 VAL H H 9.052 0.004 1 513 118 118 VAL C C 174.731 0.030 1 514 118 118 VAL CA C 60.540 0.013 1 515 118 118 VAL CB C 36.230 0.030 1 516 118 118 VAL N N 123.879 0.018 1 517 122 122 LYS C C 176.198 0.030 1 518 122 122 LYS CA C 55.122 0.030 1 519 122 122 LYS CB C 33.949 0.030 1 520 123 123 ALA H H 8.312 0.001 1 521 123 123 ALA C C 177.351 0.004 1 522 123 123 ALA CA C 51.938 0.038 1 523 123 123 ALA CB C 20.131 0.032 1 524 123 123 ALA N N 124.749 0.025 1 525 124 124 ASP H H 9.101 0.004 1 526 124 124 ASP C C 176.306 0.030 1 527 124 124 ASP CA C 54.495 0.030 1 528 124 124 ASP CB C 41.318 0.030 1 529 124 124 ASP N N 120.922 0.005 1 530 125 125 ASP C C 176.606 0.030 1 531 125 125 ASP CA C 54.480 0.041 1 532 125 125 ASP CB C 41.167 0.005 1 533 126 126 LEU H H 8.217 0.001 1 534 126 126 LEU C C 178.234 0.007 1 535 126 126 LEU CA C 55.689 0.029 1 536 126 126 LEU CB C 41.987 0.007 1 537 126 126 LEU N N 122.092 0.037 1 538 127 127 GLY H H 8.456 0.001 1 539 127 127 GLY C C 174.606 0.026 1 540 127 127 GLY CA C 45.675 0.089 1 541 127 127 GLY N N 108.967 0.021 1 542 128 128 LYS H H 8.126 0.002 1 543 128 128 LYS C C 177.289 0.006 1 544 128 128 LYS CA C 56.416 0.025 1 545 128 128 LYS CB C 32.911 0.017 1 546 128 128 LYS N N 120.489 0.017 1 547 129 129 GLY H H 8.521 0.001 1 548 129 129 GLY C C 174.708 0.009 1 549 129 129 GLY CA C 45.416 0.015 1 550 129 129 GLY N N 109.747 0.017 1 551 130 130 GLY H H 8.332 0.001 1 552 130 130 GLY C C 174.095 0.012 1 553 130 130 GLY CA C 45.437 0.110 1 554 130 130 GLY N N 108.764 0.005 1 555 131 131 ASN H H 8.396 0.001 1 556 131 131 ASN C C 175.501 0.016 1 557 131 131 ASN CA C 53.342 0.029 1 558 131 131 ASN CB C 39.059 0.008 1 559 131 131 ASN N N 118.557 0.010 1 560 132 132 GLU H H 8.581 0.002 1 561 132 132 GLU C C 176.825 0.016 1 562 132 132 GLU CA C 57.325 0.023 1 563 132 132 GLU CB C 29.968 0.018 1 564 132 132 GLU N N 121.025 0.044 1 565 133 133 GLU H H 8.449 0.001 1 566 133 133 GLU C C 177.057 0.020 1 567 133 133 GLU CA C 57.217 0.021 1 568 133 133 GLU CB C 30.053 0.014 1 569 133 133 GLU N N 120.997 0.004 1 570 134 134 SER H H 8.299 0.001 1 571 134 134 SER C C 175.172 0.009 1 572 134 134 SER CA C 59.020 0.018 1 573 134 134 SER CB C 63.679 0.022 1 574 134 134 SER N N 115.993 0.022 1 575 135 135 THR H H 8.081 0.001 1 576 135 135 THR C C 174.843 0.012 1 577 135 135 THR CA C 62.294 0.005 1 578 135 135 THR CB C 69.538 0.045 1 579 135 135 THR N N 114.961 0.010 1 580 136 136 LYS H H 8.252 0.002 1 581 136 136 LYS C C 176.890 0.011 1 582 136 136 LYS CA C 56.680 0.054 1 583 136 136 LYS CB C 32.964 0.011 1 584 136 136 LYS N N 123.272 0.038 1 585 137 137 THR H H 8.103 0.001 1 586 137 137 THR C C 175.212 0.019 1 587 137 137 THR CA C 62.024 0.024 1 588 137 137 THR CB C 69.858 0.064 1 589 137 137 THR N N 113.671 0.081 1 590 138 138 GLY H H 8.390 0.005 1 591 138 138 GLY C C 173.956 0.009 1 592 138 138 GLY CA C 45.610 0.120 1 593 138 138 GLY N N 110.983 0.050 1 594 139 139 ASN H H 8.330 0.001 1 595 139 139 ASN C C 174.985 0.010 1 596 139 139 ASN CA C 53.313 0.021 1 597 139 139 ASN CB C 39.198 0.022 1 598 139 139 ASN N N 118.625 0.023 1 599 140 140 ALA H H 8.372 0.002 1 600 140 140 ALA C C 177.656 0.002 1 601 140 140 ALA CA C 52.923 0.036 1 602 140 140 ALA CB C 18.699 0.002 1 603 140 140 ALA N N 124.051 0.009 1 604 141 141 GLY H H 8.256 0.002 1 605 141 141 GLY C C 174.642 0.012 1 606 141 141 GLY CA C 45.325 0.125 1 607 141 141 GLY N N 106.561 0.007 1 608 142 142 SER H H 8.663 0.001 1 609 142 142 SER C C 174.214 0.005 1 610 142 142 SER CA C 59.154 0.021 1 611 142 142 SER CB C 64.078 0.025 1 612 142 142 SER N N 117.050 0.018 1 613 143 143 ARG H H 8.682 0.002 1 614 143 143 ARG C C 175.251 0.030 1 615 143 143 ARG CA C 56.423 0.007 1 616 143 143 ARG CB C 30.711 0.030 1 617 143 143 ARG N N 121.975 0.019 1 618 144 144 LEU H H 8.186 0.030 1 619 144 144 LEU C C 176.991 0.030 1 620 144 144 LEU CA C 55.209 0.030 1 621 144 144 LEU CB C 42.554 0.030 1 622 144 144 LEU N N 122.835 0.030 1 623 145 145 ALA H H 8.259 0.030 1 624 145 145 ALA C C 175.157 0.030 1 625 145 145 ALA CA C 51.468 0.035 1 626 145 145 ALA CB C 22.041 0.030 1 627 145 145 ALA N N 124.345 0.030 1 628 146 146 CYS H H 8.718 0.002 1 629 146 146 CYS C C 173.802 0.012 1 630 146 146 CYS CA C 54.966 0.025 1 631 146 146 CYS CB C 45.517 0.049 1 632 146 146 CYS N N 116.090 0.013 1 633 147 147 GLY H H 8.685 0.003 1 634 147 147 GLY C C 171.305 0.030 1 635 147 147 GLY CA C 46.695 0.088 1 636 147 147 GLY N N 110.826 0.026 1 637 148 148 VAL H H 8.803 0.001 1 638 148 148 VAL C C 176.046 0.013 1 639 148 148 VAL CA C 62.683 0.025 1 640 148 148 VAL CB C 32.462 0.030 1 641 148 148 VAL N N 124.425 0.019 1 642 149 149 ILE H H 8.741 0.001 1 643 149 149 ILE C C 176.346 0.030 1 644 149 149 ILE CA C 62.330 0.015 1 645 149 149 ILE CB C 37.540 0.023 1 646 149 149 ILE N N 128.883 0.056 1 647 150 150 GLY H H 8.768 0.002 1 648 150 150 GLY C C 171.688 0.003 1 649 150 150 GLY CA C 45.346 0.110 1 650 150 150 GLY N N 117.365 0.018 1 651 151 151 ILE H H 8.158 0.001 1 652 151 151 ILE C C 176.125 0.008 1 653 151 151 ILE CA C 61.142 0.013 1 654 151 151 ILE CB C 38.857 0.020 1 655 151 151 ILE N N 118.881 0.020 1 656 152 152 ALA H H 8.624 0.001 1 657 152 152 ALA C C 176.233 0.014 1 658 152 152 ALA CA C 52.183 0.032 1 659 152 152 ALA CB C 19.913 0.004 1 660 152 152 ALA N N 130.375 0.021 1 661 153 153 GLN H H 8.043 0.001 1 662 153 153 GLN C C 180.609 0.030 1 663 153 153 GLN CA C 57.337 0.020 1 664 153 153 GLN CB C 30.714 0.030 1 665 153 153 GLN N N 125.349 0.005 1 stop_ save_