data_15713 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Backbone chemical shift assignements for monomeric apoSOD1 - variant G85R ; _BMRB_accession_number 15713 _BMRB_flat_file_name bmr15713.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" 127 "13C chemical shifts" 392 "15N chemical shifts" 127 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' 15712 'SOD1, mutant A4V' 15713 '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 ; ATKAVAVLKGDGPVQGIINF EQKESNGPVKVWGSIKGLTE GLHGFHVHEEEDNTAGCTSA GPHFNPLSRKHGGPKDEERH VGDLRNVTADKDGVADVSIE DSVISLSGDHAIIGRTLVVH EKADDLGKGGNEESTKTGNA GSRLACGVIGIAQ ; loop_ _Residue_seq_code _Residue_label 1 ALA 2 THR 3 LYS 4 ALA 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 ARG 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 3.43e-102 BMRB 15712 SOD1 100.00 153 98.69 98.69 1.95e-101 BMRB 15714 SOD1 100.00 153 98.69 98.69 3.19e-101 BMRB 18509 Superoxide_dismutase_C6A-C111S_thermostable_mutant 100.00 153 97.39 98.04 2.16e-99 BMRB 18708 SUPEROXIDE_DISMUTASE_CU-ZN 100.00 153 97.39 98.04 2.16e-99 BMRB 18968 SOD1 100.00 153 99.35 99.35 3.43e-102 BMRB 26570 SOD1 100.00 153 97.39 98.04 2.16e-99 BMRB 4202 "Superoxide Dismutase" 100.00 153 98.04 99.35 2.15e-101 PDB 1BA9 "The Solution Structure Of Reduced Monomeric Superoxide Dismutase, Nmr, 36 Structures" 99.35 153 98.03 99.34 1.07e-100 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 5.07e-99 PDB 1KMG "The Solution Structure Of Monomeric Copper-Free Superoxide Dismutase" 100.00 153 98.04 99.35 2.15e-101 PDB 1L3N "The Solution Structure Of Reduced Dimeric Copper Zinc Sod: The Structural Effects Of Dimerization" 100.00 153 97.39 98.04 2.16e-99 PDB 1MFM "Monomeric Human Sod Mutant F50eG51EE133Q AT ATOMIC Resolution" 100.00 153 98.04 99.35 2.15e-101 PDB 1N18 "Thermostable Mutant Of Human Superoxide Dismutase, C6a, C111s" 100.00 154 97.39 98.04 1.63e-99 PDB 1RK7 "Solution Structure Of Apo Cu,Zn Superoxide Dismutase: Role Of Metal Ions In Protein Folding" 100.00 153 98.04 99.35 2.15e-101 PDB 1SOS "Atomic Structures Of Wild-type And Thermostable Mutant Recombinant Human Cu, Zn Superoxide Dismutase" 100.00 154 97.39 98.04 2.24e-99 PDB 2AF2 "Solution Structure Of Disulfide Reduced And Copper Depleted Human Superoxide Dismutase" 100.00 153 97.39 98.04 2.16e-99 PDB 2GBT "C6aC111A CUZN SUPEROXIDE DISMUTASE" 100.00 153 98.04 98.04 1.01e-99 PDB 2LU5 "Structure And Chemical Shifts Of Cu(I),Zn(Ii) Superoxide Dismutase By Solid-State Nmr" 100.00 153 97.39 98.04 2.16e-99 PDB 2VR6 "Crystal Structure Of G85r Als Mutant Of Human Cu,Zn Superoxide Dismutase (Cuznsod) At 1.3 A Resolution" 100.00 153 97.39 97.39 1.10e-99 PDB 2VR7 "Crystal Structure Of G85r Als Mutant Of Human Cu,Zn Superoxide Dismutase (Cuznsod) At 1.58 A Resolution" 100.00 154 97.39 97.39 1.14e-99 PDB 2VR8 "Crystal Structure Of G85r Als Mutant Of Human Cu,Zn Superoxide Dismutase (Cuznsod) At 1.36 A Resolution" 100.00 154 97.39 97.39 1.34e-99 PDB 2XJK "Monomeric Human Cu,Zn Superoxide Dismutase" 100.00 153 99.35 99.35 3.43e-102 PDB 2XJL "Monomeric Human Cu,Zn Superoxide Dismutase Without Cu Ligands" 100.00 153 97.39 97.39 3.35e-99 PDB 2ZKW "Crystal Structure Of Human Cu-Zn Superoxide Dismutase Mutant G85r In Space Group P21" 100.00 159 97.39 97.39 9.79e-100 PDB 2ZKX "Crystal Structure Of Human Cu-Zn Superoxide Dismutase Mutant G85r In Space Group I212121" 100.00 159 97.39 97.39 9.79e-100 PDB 3CQP "Human Sod1 G85r Variant, Structure I" 100.00 153 97.39 97.39 1.10e-99 PDB 3CQQ "Human Sod1 G85r Variant, Structure Ii" 100.00 153 97.39 97.39 1.29e-99 PDB 4BCY "Monomeric Human Cu,zn Superoxide Dismutase, Mutation H43f" 100.00 153 98.69 98.69 3.60e-101 GB AAA72747 "CuZn superoxide dismutase [synthetic construct]" 100.00 154 97.39 98.04 1.63e-99 GB AAA80237 "HSOD-GlyProGly-A+, partial [synthetic construct]" 100.00 171 97.39 98.04 1.00e-98 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 1 1 ALA C C 173.728 0.016 1 2 1 1 ALA CA C 52.035 0.014 1 3 1 1 ALA CB C 20.306 0.013 1 4 2 2 THR H H 8.540 0.005 1 5 2 2 THR C C 172.387 0.008 1 6 2 2 THR CA C 62.640 0.040 1 7 2 2 THR CB C 70.490 0.127 1 8 2 2 THR N N 115.848 0.049 1 9 3 3 LYS H H 8.717 0.003 1 10 3 3 LYS C C 174.400 0.005 1 11 3 3 LYS CA C 55.036 0.031 1 12 3 3 LYS CB C 36.600 0.012 1 13 3 3 LYS N N 125.869 0.057 1 14 4 4 ALA H H 9.195 0.003 1 15 4 4 ALA C C 175.208 0.004 1 16 4 4 ALA CA C 50.642 0.030 1 17 4 4 ALA CB C 23.706 0.039 1 18 4 4 ALA N N 123.122 0.037 1 19 5 5 VAL H H 9.462 0.002 1 20 5 5 VAL C C 173.061 0.012 1 21 5 5 VAL CA C 60.433 0.034 1 22 5 5 VAL CB C 36.458 0.007 1 23 5 5 VAL N N 120.706 0.043 1 24 6 6 ALA H H 9.385 0.002 1 25 6 6 ALA C C 174.483 0.004 1 26 6 6 ALA CA C 50.939 0.013 1 27 6 6 ALA CB C 23.372 0.034 1 28 6 6 ALA N N 128.911 0.047 1 29 7 7 VAL H H 9.211 0.001 1 30 7 7 VAL C C 175.577 0.013 1 31 7 7 VAL CA C 62.097 0.018 1 32 7 7 VAL CB C 31.747 0.032 1 33 7 7 VAL N N 125.453 0.041 1 34 8 8 LEU H H 8.747 0.003 1 35 8 8 LEU C C 175.834 0.063 1 36 8 8 LEU CA C 54.247 0.044 1 37 8 8 LEU CB C 42.941 0.032 1 38 8 8 LEU N N 126.580 0.054 1 39 9 9 LYS H H 8.244 0.004 1 40 9 9 LYS C C 175.444 0.021 1 41 9 9 LYS CA C 55.245 0.087 1 42 9 9 LYS CB C 36.487 0.026 1 43 9 9 LYS N N 121.447 0.037 1 44 10 10 GLY H H 8.727 0.003 1 45 10 10 GLY C C 172.750 0.024 1 46 10 10 GLY CA C 45.496 0.024 1 47 10 10 GLY N N 112.380 0.066 1 48 11 11 ASP H H 8.732 0.002 1 49 11 11 ASP C C 176.647 0.017 1 50 11 11 ASP CA C 54.671 0.023 1 51 11 11 ASP CB C 41.046 0.007 1 52 11 11 ASP N N 121.133 0.046 1 53 12 12 GLY H H 8.125 0.003 1 54 12 12 GLY C C 173.552 0.030 1 55 12 12 GLY CA C 44.439 0.015 1 56 12 12 GLY N N 110.419 0.054 1 57 13 13 PRO C C 176.596 0.019 1 58 13 13 PRO CA C 63.475 0.019 1 59 13 13 PRO CB C 32.686 0.030 1 60 14 14 VAL H H 7.428 0.003 1 61 14 14 VAL C C 175.931 0.005 1 62 14 14 VAL CA C 63.119 0.088 1 63 14 14 VAL CB C 30.691 0.085 1 64 14 14 VAL N N 120.668 0.055 1 65 15 15 GLN H H 8.035 0.006 1 66 15 15 GLN C C 174.249 0.003 1 67 15 15 GLN CA C 53.992 0.053 1 68 15 15 GLN CB C 32.646 0.030 1 69 15 15 GLN N N 123.317 0.078 1 70 16 16 GLY H H 8.311 0.004 1 71 16 16 GLY C C 170.875 0.030 1 72 16 16 GLY CA C 46.722 0.023 1 73 16 16 GLY N N 107.575 0.050 1 74 17 17 ILE H H 8.022 0.003 1 75 17 17 ILE C C 174.021 0.015 1 76 17 17 ILE CA C 61.229 0.055 1 77 17 17 ILE CB C 41.103 0.048 1 78 17 17 ILE N N 120.654 0.040 1 79 18 18 ILE H H 8.780 0.005 1 80 18 18 ILE C C 172.526 0.001 1 81 18 18 ILE CA C 57.023 0.023 1 82 18 18 ILE CB C 37.651 0.052 1 83 18 18 ILE N N 126.344 0.038 1 84 19 19 ASN H H 8.773 0.003 1 85 19 19 ASN C C 172.192 0.005 1 86 19 19 ASN CA C 52.377 0.017 1 87 19 19 ASN CB C 40.389 0.027 1 88 19 19 ASN N N 124.408 0.067 1 89 20 20 PHE H H 8.506 0.004 1 90 20 20 PHE C C 176.243 0.009 1 91 20 20 PHE CA C 55.288 0.024 1 92 20 20 PHE CB C 43.211 0.009 1 93 20 20 PHE N N 115.094 0.055 1 94 21 21 GLU H H 9.622 0.003 1 95 21 21 GLU C C 173.695 0.003 1 96 21 21 GLU CA C 56.154 0.039 1 97 21 21 GLU CB C 34.531 0.015 1 98 21 21 GLU N N 122.316 0.042 1 99 22 22 GLN H H 9.193 0.004 1 100 22 22 GLN C C 174.613 0.040 1 101 22 22 GLN CA C 54.576 0.011 1 102 22 22 GLN CB C 32.487 0.030 1 103 22 22 GLN N N 129.807 0.063 1 104 23 23 LYS H H 9.212 0.006 1 105 23 23 LYS C C 176.193 0.016 1 106 23 23 LYS CA C 59.731 0.024 1 107 23 23 LYS CB C 33.232 0.030 1 108 23 23 LYS N N 129.949 0.064 1 109 24 24 GLU H H 8.140 0.002 1 110 24 24 GLU C C 177.291 0.001 1 111 24 24 GLU CA C 54.416 0.025 1 112 24 24 GLU CB C 32.451 0.030 1 113 24 24 GLU N N 115.670 0.028 1 114 25 25 SER H H 8.848 0.003 1 115 25 25 SER C C 174.517 0.015 1 116 25 25 SER CA C 61.189 0.036 1 117 25 25 SER CB C 62.816 0.011 1 118 25 25 SER N N 118.323 0.029 1 119 26 26 ASN H H 8.339 0.004 1 120 26 26 ASN C C 175.104 0.005 1 121 26 26 ASN CA C 53.006 0.011 1 122 26 26 ASN CB C 38.138 0.063 1 123 26 26 ASN N N 117.047 0.024 1 124 27 27 GLY H H 7.932 0.002 1 125 27 27 GLY CA C 44.629 0.014 1 126 27 27 GLY N N 108.074 0.029 1 127 28 28 PRO C C 176.215 0.030 1 128 28 28 PRO CA C 63.011 0.027 1 129 28 28 PRO CB C 33.033 0.013 1 130 29 29 VAL H H 8.911 0.004 1 131 29 29 VAL C C 175.209 0.004 1 132 29 29 VAL CA C 61.216 0.059 1 133 29 29 VAL CB C 33.600 0.033 1 134 29 29 VAL N N 121.498 0.050 1 135 30 30 LYS H H 9.202 0.005 1 136 30 30 LYS C C 175.233 0.002 1 137 30 30 LYS CA C 56.024 0.011 1 138 30 30 LYS CB C 34.283 0.047 1 139 30 30 LYS N N 128.692 0.039 1 140 31 31 VAL H H 9.219 0.004 1 141 31 31 VAL C C 175.382 0.019 1 142 31 31 VAL CA C 60.598 0.027 1 143 31 31 VAL CB C 33.468 0.056 1 144 31 31 VAL N N 127.046 0.048 1 145 32 32 TRP H H 8.984 0.003 1 146 32 32 TRP C C 173.449 0.004 1 147 32 32 TRP CA C 56.065 0.012 1 148 32 32 TRP CB C 32.302 0.005 1 149 32 32 TRP N N 125.479 0.061 1 150 33 33 GLY H H 8.557 0.006 1 151 33 33 GLY C C 171.372 0.030 1 152 33 33 GLY CA C 44.786 0.032 1 153 33 33 GLY N N 108.625 0.069 1 154 34 34 SER H H 7.842 0.003 1 155 34 34 SER C C 172.859 0.009 1 156 34 34 SER CA C 57.103 0.052 1 157 34 34 SER CB C 65.494 0.019 1 158 34 34 SER N N 113.746 0.034 1 159 35 35 ILE H H 8.644 0.004 1 160 35 35 ILE C C 173.099 0.015 1 161 35 35 ILE CA C 60.210 0.027 1 162 35 35 ILE CB C 41.236 0.041 1 163 35 35 ILE N N 124.123 0.051 1 164 36 36 LYS H H 9.031 0.003 1 165 36 36 LYS C C 175.494 0.010 1 166 36 36 LYS CA C 54.522 0.028 1 167 36 36 LYS CB C 35.282 0.044 1 168 36 36 LYS N N 124.254 0.055 1 169 37 37 GLY H H 8.270 0.003 1 170 37 37 GLY C C 174.769 0.030 1 171 37 37 GLY CA C 45.684 0.031 1 172 37 37 GLY N N 106.126 0.055 1 173 38 38 LEU H H 8.237 0.003 1 174 38 38 LEU C C 177.031 0.005 1 175 38 38 LEU CA C 53.553 0.020 1 176 38 38 LEU CB C 44.346 0.025 1 177 38 38 LEU N N 120.764 0.049 1 178 39 39 THR H H 8.219 0.003 1 179 39 39 THR C C 176.045 0.008 1 180 39 39 THR CA C 61.275 0.030 1 181 39 39 THR CB C 69.879 0.063 1 182 39 39 THR N N 110.589 0.047 1 183 40 40 GLU H H 8.742 0.002 1 184 40 40 GLU C C 176.040 0.030 1 185 40 40 GLU CA C 57.742 0.071 1 186 40 40 GLU CB C 30.459 0.019 1 187 40 40 GLU N N 126.079 0.053 1 188 41 41 GLY H H 8.696 0.004 1 189 41 41 GLY C C 178.360 0.030 1 190 41 41 GLY CA C 43.280 0.006 1 191 41 41 GLY N N 113.636 0.074 1 192 42 42 LEU H H 7.587 0.030 1 193 42 42 LEU N N 112.407 0.030 1 194 46 46 HIS C C 173.227 0.030 1 195 47 47 VAL H H 8.836 0.008 1 196 47 47 VAL C C 175.679 0.026 1 197 47 47 VAL CA C 61.651 0.006 1 198 47 47 VAL CB C 32.248 0.008 1 199 47 47 VAL N N 122.183 0.052 1 200 48 48 HIS H H 9.518 0.004 1 201 48 48 HIS C C 174.653 0.022 1 202 48 48 HIS CA C 55.795 0.067 1 203 48 48 HIS CB C 31.861 0.112 1 204 48 48 HIS N N 128.166 0.028 1 205 49 49 GLU H H 8.715 0.004 1 206 49 49 GLU C C 175.430 0.030 1 207 49 49 GLU CA C 56.428 0.045 1 208 49 49 GLU CB C 30.656 0.030 1 209 49 49 GLU N N 123.868 0.077 1 210 50 50 GLU H H 8.648 0.006 1 211 50 50 GLU C C 176.074 0.008 1 212 50 50 GLU CA C 56.369 0.033 1 213 50 50 GLU CB C 30.667 0.048 1 214 50 50 GLU N N 122.131 0.051 1 215 51 51 GLU H H 8.597 0.002 1 216 51 51 GLU C C 176.035 0.010 1 217 51 51 GLU CA C 56.906 0.002 1 218 51 51 GLU CB C 30.635 0.029 1 219 51 51 GLU N N 121.804 0.029 1 220 52 52 ASP H H 8.300 0.009 1 221 52 52 ASP C C 176.065 0.008 1 222 52 52 ASP CA C 54.169 0.054 1 223 52 52 ASP CB C 41.265 0.032 1 224 52 52 ASP N N 120.099 0.108 1 225 53 53 ASN H H 8.489 0.001 1 226 53 53 ASN C C 176.000 0.032 1 227 53 53 ASN CA C 53.812 0.047 1 228 53 53 ASN CB C 38.737 0.015 1 229 53 53 ASN N N 119.391 0.027 1 230 54 54 THR H H 8.248 0.003 1 231 54 54 THR C C 174.843 0.011 1 232 54 54 THR CA C 62.864 0.063 1 233 54 54 THR CB C 69.771 0.038 1 234 54 54 THR N N 113.372 0.040 1 235 55 55 ALA H H 8.169 0.002 1 236 55 55 ALA C C 178.085 0.040 1 237 55 55 ALA CA C 52.820 0.024 1 238 55 55 ALA CB C 19.048 0.049 1 239 55 55 ALA N N 125.260 0.042 1 240 56 56 GLY H H 8.186 0.005 1 241 56 56 GLY C C 174.401 0.030 1 242 56 56 GLY CA C 45.607 0.039 1 243 56 56 GLY N N 107.438 0.054 1 244 57 57 CYS H H 8.590 0.004 1 245 57 57 CYS C C 174.774 0.036 1 246 57 57 CYS CA C 55.949 0.031 1 247 57 57 CYS CB C 41.040 0.008 1 248 57 57 CYS N N 119.056 0.047 1 249 58 58 THR H H 8.138 0.003 1 250 58 58 THR C C 174.479 0.035 1 251 58 58 THR CA C 62.093 0.032 1 252 58 58 THR CB C 69.958 0.022 1 253 58 58 THR N N 114.215 0.092 1 254 59 59 SER H H 8.378 0.003 1 255 59 59 SER C C 174.103 0.022 1 256 59 59 SER CA C 58.509 0.034 1 257 59 59 SER CB C 63.883 0.029 1 258 59 59 SER N N 118.209 0.041 1 259 60 60 ALA H H 8.233 0.003 1 260 60 60 ALA C C 177.569 0.001 1 261 60 60 ALA CA C 52.464 0.018 1 262 60 60 ALA CB C 19.633 0.026 1 263 60 60 ALA N N 125.434 0.036 1 264 61 61 GLY H H 8.139 0.003 1 265 61 61 GLY C C 171.912 0.030 1 266 61 61 GLY CA C 44.682 0.005 1 267 61 61 GLY N N 107.843 0.032 1 268 62 62 PRO C C 176.876 0.003 1 269 62 62 PRO CA C 63.344 0.023 1 270 62 62 PRO CB C 32.139 0.011 1 271 63 63 HIS H H 8.462 0.002 1 272 63 63 HIS C C 174.343 0.015 1 273 63 63 HIS CA C 55.560 0.015 1 274 63 63 HIS CB C 29.755 0.069 1 275 63 63 HIS N N 118.571 0.038 1 276 64 64 PHE H H 8.141 0.004 1 277 64 64 PHE C C 174.448 0.022 1 278 64 64 PHE CA C 57.680 0.033 1 279 64 64 PHE CB C 39.886 0.029 1 280 64 64 PHE N N 121.786 0.034 1 281 65 65 ASN H H 8.422 0.002 1 282 65 65 ASN C C 173.360 0.030 1 283 65 65 ASN CA C 50.468 0.005 1 284 65 65 ASN CB C 39.215 0.030 1 285 65 65 ASN N N 123.168 0.029 1 286 66 66 PRO C C 177.116 0.005 1 287 66 66 PRO CA C 63.757 0.024 1 288 66 66 PRO CB C 32.195 0.011 1 289 67 67 LEU H H 8.072 0.002 1 290 67 67 LEU C C 177.657 0.004 1 291 67 67 LEU CA C 55.390 0.019 1 292 67 67 LEU CB C 41.736 0.017 1 293 67 67 LEU N N 119.476 0.021 1 294 68 68 SER H H 7.901 0.001 1 295 68 68 SER C C 174.590 0.015 1 296 68 68 SER CA C 58.581 0.023 1 297 68 68 SER CB C 63.798 0.011 1 298 68 68 SER N N 115.238 0.026 1 299 69 69 ARG H H 8.173 0.004 1 300 69 69 ARG C C 176.131 0.021 1 301 69 69 ARG CA C 56.059 0.002 1 302 69 69 ARG CB C 30.725 0.038 1 303 69 69 ARG N N 122.710 0.028 1 304 70 70 LYS H H 8.299 0.004 1 305 70 70 LYS C C 176.368 0.008 1 306 70 70 LYS CA C 56.451 0.008 1 307 70 70 LYS CB C 33.004 0.031 1 308 70 70 LYS N N 122.203 0.056 1 309 71 71 HIS H H 8.448 0.005 1 310 71 71 HIS C C 175.293 0.009 1 311 71 71 HIS CA C 55.844 0.035 1 312 71 71 HIS CB C 30.119 0.101 1 313 71 71 HIS N N 120.102 0.066 1 314 72 72 GLY H H 8.504 0.005 1 315 72 72 GLY C C 174.206 0.005 1 316 72 72 GLY CA C 45.224 0.003 1 317 72 72 GLY N N 110.598 0.051 1 318 73 73 GLY H H 8.295 0.003 1 319 73 73 GLY C C 171.987 0.030 1 320 73 73 GLY CA C 44.596 0.010 1 321 73 73 GLY N N 109.148 0.047 1 322 74 74 PRO C C 177.377 0.030 1 323 74 74 PRO CA C 63.553 0.036 1 324 74 74 PRO CB C 32.267 0.010 1 325 75 75 LYS H H 8.474 0.004 1 326 75 75 LYS C C 176.528 0.003 1 327 75 75 LYS CA C 56.482 0.037 1 328 75 75 LYS CB C 32.805 0.019 1 329 75 75 LYS N N 120.610 0.054 1 330 76 76 ASP H H 8.272 0.003 1 331 76 76 ASP C C 176.252 0.030 1 332 76 76 ASP CA C 54.837 0.023 1 333 76 76 ASP CB C 41.162 0.007 1 334 76 76 ASP N N 121.275 0.099 1 335 77 77 GLU H H 8.309 0.003 1 336 77 77 GLU C C 176.230 0.017 1 337 77 77 GLU CA C 56.670 0.018 1 338 77 77 GLU CB C 30.439 0.029 1 339 77 77 GLU N N 120.502 0.025 1 340 78 78 GLU H H 8.277 0.002 1 341 78 78 GLU C C 175.577 0.030 1 342 78 78 GLU CA C 56.461 0.030 1 343 78 78 GLU CB C 30.224 0.013 1 344 78 78 GLU N N 121.496 0.073 1 345 79 79 ARG H H 8.257 0.002 1 346 79 79 ARG C C 175.597 0.020 1 347 79 79 ARG CA C 55.705 0.017 1 348 79 79 ARG CB C 31.329 0.016 1 349 79 79 ARG N N 121.774 0.050 1 350 80 80 HIS H H 8.504 0.006 1 351 80 80 HIS C C 174.522 0.030 1 352 80 80 HIS CA C 55.001 0.035 1 353 80 80 HIS CB C 29.993 0.030 1 354 80 80 HIS N N 120.177 0.027 1 355 85 85 ARG C C 175.210 0.030 1 356 85 85 ARG CA C 57.328 0.030 1 357 86 86 ASN H H 8.045 0.007 1 358 86 86 ASN C C 175.802 0.011 1 359 86 86 ASN CA C 53.299 0.034 1 360 86 86 ASN CB C 43.545 0.001 1 361 86 86 ASN N N 115.267 0.057 1 362 87 87 VAL H H 8.845 0.006 1 363 87 87 VAL C C 174.323 0.020 1 364 87 87 VAL CA C 59.476 0.070 1 365 87 87 VAL CB C 33.442 0.052 1 366 87 87 VAL N N 112.350 0.077 1 367 88 88 THR H H 8.484 0.004 1 368 88 88 THR C C 173.563 0.021 1 369 88 88 THR CA C 61.812 0.126 1 370 88 88 THR CB C 70.137 0.078 1 371 88 88 THR N N 117.672 0.039 1 372 89 89 ALA H H 9.226 0.004 1 373 89 89 ALA C C 177.575 0.022 1 374 89 89 ALA CA C 49.634 0.038 1 375 89 89 ALA CB C 21.269 0.050 1 376 89 89 ALA N N 129.263 0.050 1 377 90 90 ASP H H 8.527 0.003 1 378 90 90 ASP C C 177.139 0.030 1 379 90 90 ASP CA C 52.635 0.036 1 380 90 90 ASP CB C 41.667 0.035 1 381 90 90 ASP N N 124.973 0.035 1 382 91 91 LYS H H 8.179 0.003 1 383 91 91 LYS C C 177.233 0.029 1 384 91 91 LYS CA C 58.568 0.029 1 385 91 91 LYS CB C 31.831 0.002 1 386 91 91 LYS N N 115.163 0.046 1 387 92 92 ASP H H 8.186 0.004 1 388 92 92 ASP C C 176.262 0.011 1 389 92 92 ASP CA C 54.377 0.048 1 390 92 92 ASP CB C 41.568 0.008 1 391 92 92 ASP N N 119.828 0.076 1 392 93 93 GLY H H 8.431 0.003 1 393 93 93 GLY C C 172.899 0.030 1 394 93 93 GLY CA C 47.047 0.016 1 395 93 93 GLY N N 111.424 0.049 1 396 94 94 VAL H H 7.948 0.002 1 397 94 94 VAL C C 176.496 0.044 1 398 94 94 VAL CA C 61.618 0.029 1 399 94 94 VAL CB C 33.052 0.018 1 400 94 94 VAL N N 119.309 0.040 1 401 95 95 ALA H H 9.624 0.005 1 402 95 95 ALA C C 174.746 0.030 1 403 95 95 ALA CA C 50.115 0.019 1 404 95 95 ALA CB C 20.968 0.040 1 405 95 95 ALA N N 131.587 0.039 1 406 96 96 ASP H H 8.582 0.004 1 407 96 96 ASP C C 175.673 0.016 1 408 96 96 ASP CA C 54.159 0.020 1 409 96 96 ASP CB C 42.093 0.009 1 410 96 96 ASP N N 125.031 0.036 1 411 97 97 VAL H H 8.623 0.005 1 412 97 97 VAL C C 176.488 0.005 1 413 97 97 VAL CA C 61.844 0.047 1 414 97 97 VAL CB C 33.918 0.006 1 415 97 97 VAL N N 124.547 0.043 1 416 98 98 SER H H 8.757 0.001 1 417 98 98 SER C C 173.079 0.010 1 418 98 98 SER CA C 58.274 0.035 1 419 98 98 SER CB C 62.610 0.049 1 420 98 98 SER N N 123.304 0.071 1 421 99 99 ILE H H 9.390 0.002 1 422 99 99 ILE C C 174.142 0.015 1 423 99 99 ILE CA C 60.206 0.037 1 424 99 99 ILE CB C 43.852 0.087 1 425 99 99 ILE N N 126.107 0.062 1 426 100 100 GLU H H 8.506 0.007 1 427 100 100 GLU C C 174.929 0.030 1 428 100 100 GLU CA C 55.685 0.057 1 429 100 100 GLU CB C 32.266 0.030 1 430 100 100 GLU N N 124.122 0.057 1 431 101 101 ASP C C 175.330 0.007 1 432 101 101 ASP CA C 53.940 0.025 1 433 102 102 SER H H 8.955 0.006 1 434 102 102 SER CA C 58.794 0.009 1 435 102 102 SER CB C 64.204 0.030 1 436 102 102 SER N N 119.803 0.064 1 437 103 103 VAL C C 177.577 0.030 1 438 104 104 ILE H H 7.796 0.005 1 439 104 104 ILE C C 172.958 0.038 1 440 104 104 ILE CA C 61.522 0.028 1 441 104 104 ILE CB C 39.647 0.080 1 442 104 104 ILE N N 114.023 0.046 1 443 105 105 SER H H 7.732 0.006 1 444 105 105 SER C C 173.872 0.044 1 445 105 105 SER CA C 56.252 0.081 1 446 105 105 SER CB C 65.557 0.029 1 447 105 105 SER N N 109.156 0.048 1 448 106 106 LEU H H 8.462 0.002 1 449 106 106 LEU C C 174.572 0.018 1 450 106 106 LEU CA C 54.602 0.017 1 451 106 106 LEU CB C 41.242 0.035 1 452 106 106 LEU N N 121.973 0.050 1 453 107 107 SER H H 8.218 0.004 1 454 107 107 SER C C 173.608 0.022 1 455 107 107 SER CA C 57.336 0.015 1 456 107 107 SER CB C 65.982 0.063 1 457 107 107 SER N N 112.345 0.043 1 458 108 108 GLY H H 8.604 0.002 1 459 108 108 GLY C C 175.308 0.030 1 460 108 108 GLY CA C 44.813 0.012 1 461 108 108 GLY N N 108.591 0.039 1 462 109 109 ASP H H 8.606 0.002 1 463 109 109 ASP C C 176.956 0.006 1 464 109 109 ASP CA C 56.468 0.014 1 465 109 109 ASP CB C 40.528 0.002 1 466 109 109 ASP N N 119.569 0.026 1 467 110 110 HIS H H 8.831 0.003 1 468 110 110 HIS C C 173.965 0.030 1 469 110 110 HIS CA C 53.886 0.012 1 470 110 110 HIS CB C 27.867 0.042 1 471 110 110 HIS N N 116.930 0.047 1 472 111 111 ALA H H 7.113 0.002 1 473 111 111 ALA C C 179.364 0.013 1 474 111 111 ALA CA C 52.307 0.020 1 475 111 111 ALA CB C 19.642 0.051 1 476 111 111 ALA N N 121.473 0.036 1 477 112 112 ILE H H 7.823 0.002 1 478 112 112 ILE C C 175.112 0.010 1 479 112 112 ILE CA C 61.873 0.045 1 480 112 112 ILE N N 109.299 0.035 1 481 113 113 ILE H H 6.235 0.004 1 482 113 113 ILE C C 176.870 0.030 1 483 113 113 ILE CA C 61.530 0.050 1 484 113 113 ILE CB C 35.588 0.047 1 485 113 113 ILE N N 118.389 0.054 1 486 114 114 GLY H H 9.209 0.002 1 487 114 114 GLY C C 174.535 0.030 1 488 114 114 GLY CA C 45.107 0.034 1 489 114 114 GLY N N 116.778 0.031 1 490 115 115 ARG H H 7.764 0.003 1 491 115 115 ARG C C 176.192 0.030 1 492 115 115 ARG CA C 55.378 0.010 1 493 115 115 ARG CB C 30.291 0.030 1 494 115 115 ARG N N 119.024 0.040 1 495 116 116 THR C C 172.958 0.030 1 496 116 116 THR CA C 62.170 0.079 1 497 117 117 LEU H H 9.065 0.007 1 498 117 117 LEU C C 174.802 0.030 1 499 117 117 LEU CA C 53.544 0.036 1 500 117 117 LEU CB C 44.333 0.030 1 501 117 117 LEU N N 128.094 0.063 1 502 120 120 HIS C C 175.389 0.030 1 503 120 120 HIS CA C 56.434 0.030 1 504 121 121 GLU H H 8.915 0.008 1 505 121 121 GLU C C 176.499 0.030 1 506 121 121 GLU CA C 59.574 0.061 1 507 121 121 GLU CB C 31.582 0.030 1 508 121 121 GLU N N 122.290 0.048 1 509 122 122 LYS C C 176.043 0.030 1 510 122 122 LYS CA C 54.852 0.030 1 511 122 122 LYS CB C 33.099 0.030 1 512 123 123 ALA H H 8.266 0.003 1 513 123 123 ALA C C 177.282 0.030 1 514 123 123 ALA CA C 52.114 0.045 1 515 123 123 ALA CB C 20.012 0.030 1 516 123 123 ALA N N 123.990 0.045 1 517 124 124 ASP CB C 41.190 0.030 1 518 125 125 ASP C C 176.535 0.030 1 519 125 125 ASP CA C 54.069 0.014 1 520 125 125 ASP CB C 41.275 0.030 1 521 126 126 LEU H H 8.549 0.005 1 522 126 126 LEU C C 178.038 0.010 1 523 126 126 LEU CA C 55.810 0.042 1 524 126 126 LEU CB C 41.326 0.025 1 525 126 126 LEU N N 121.396 0.030 1 526 127 127 GLY H H 8.517 0.002 1 527 127 127 GLY C C 174.856 0.001 1 528 127 127 GLY CA C 45.635 0.013 1 529 127 127 GLY N N 108.639 0.054 1 530 128 128 LYS H H 8.044 0.003 1 531 128 128 LYS C C 177.294 0.011 1 532 128 128 LYS CA C 56.406 0.012 1 533 128 128 LYS CB C 32.812 0.005 1 534 128 128 LYS N N 120.399 0.017 1 535 129 129 GLY H H 8.511 0.001 1 536 129 129 GLY C C 174.712 0.013 1 537 129 129 GLY CA C 45.454 0.022 1 538 129 129 GLY N N 109.625 0.048 1 539 130 130 GLY H H 8.331 0.002 1 540 130 130 GLY C C 174.045 0.005 1 541 130 130 GLY CA C 45.439 0.018 1 542 130 130 GLY N N 108.636 0.042 1 543 131 131 ASN H H 8.317 0.004 1 544 131 131 ASN C C 175.542 0.010 1 545 131 131 ASN CA C 53.198 0.020 1 546 131 131 ASN CB C 39.075 0.014 1 547 131 131 ASN N N 118.176 0.020 1 548 132 132 GLU H H 8.603 0.002 1 549 132 132 GLU C C 177.023 0.006 1 550 132 132 GLU CA C 57.551 0.029 1 551 132 132 GLU CB C 29.901 0.022 1 552 132 132 GLU N N 120.891 0.045 1 553 133 133 GLU H H 8.453 0.003 1 554 133 133 GLU C C 177.317 0.026 1 555 133 133 GLU CA C 57.426 0.026 1 556 133 133 GLU CB C 29.333 0.869 1 557 133 133 GLU N N 120.816 0.050 1 558 134 134 SER H H 8.271 0.001 1 559 134 134 SER C C 175.422 0.002 1 560 134 134 SER CA C 59.362 0.018 1 561 134 134 SER CB C 63.666 0.051 1 562 134 134 SER N N 115.709 0.025 1 563 135 135 THR H H 8.012 0.005 1 564 135 135 THR C C 174.880 0.001 1 565 135 135 THR CA C 62.559 0.013 1 566 135 135 THR CB C 69.547 0.046 1 567 135 135 THR N N 114.354 0.013 1 568 136 136 LYS H H 8.157 0.004 1 569 136 136 LYS C C 176.944 0.002 1 570 136 136 LYS CA C 56.937 0.016 1 571 136 136 LYS CB C 33.095 0.029 1 572 136 136 LYS N N 122.515 0.021 1 573 137 137 THR H H 8.110 0.002 1 574 137 137 THR C C 175.303 0.003 1 575 137 137 THR CA C 61.999 0.030 1 576 137 137 THR CB C 70.139 0.058 1 577 137 137 THR N N 112.821 0.044 1 578 138 138 GLY H H 8.366 0.003 1 579 138 138 GLY C C 174.027 0.005 1 580 138 138 GLY CA C 45.631 0.017 1 581 138 138 GLY N N 111.267 0.048 1 582 139 139 ASN H H 8.269 0.005 1 583 139 139 ASN C C 174.988 0.007 1 584 139 139 ASN CA C 53.587 0.023 1 585 139 139 ASN CB C 38.995 0.039 1 586 139 139 ASN N N 117.639 0.059 1 587 140 140 ALA H H 8.261 0.010 1 588 140 140 ALA C C 177.566 0.014 1 589 140 140 ALA CA C 52.896 0.014 1 590 140 140 ALA CB C 18.567 0.030 1 591 140 140 ALA N N 123.420 0.023 1 592 141 141 GLY H H 8.248 0.006 1 593 141 141 GLY C C 174.945 0.005 1 594 141 141 GLY CA C 45.239 0.022 1 595 141 141 GLY N N 106.301 0.044 1 596 142 142 SER H H 8.782 0.004 1 597 142 142 SER C C 174.161 0.023 1 598 142 142 SER CA C 59.287 0.059 1 599 142 142 SER CB C 64.108 0.049 1 600 142 142 SER N N 117.506 0.057 1 601 143 143 ARG H H 8.687 0.004 1 602 143 143 ARG C C 175.467 0.030 1 603 143 143 ARG CA C 56.496 0.019 1 604 143 143 ARG CB C 30.629 0.030 1 605 143 143 ARG N N 122.099 0.041 1 606 145 145 ALA C C 175.067 0.030 1 607 145 145 ALA CA C 51.588 0.033 1 608 145 145 ALA CB C 21.680 0.010 1 609 146 146 CYS H H 8.634 0.004 1 610 146 146 CYS C C 173.570 0.017 1 611 146 146 CYS CA C 54.968 0.045 1 612 146 146 CYS CB C 44.921 0.030 1 613 146 146 CYS N N 116.199 0.053 1 614 147 147 GLY H H 8.669 0.004 1 615 147 147 GLY C C 174.201 0.030 1 616 147 147 GLY CA C 46.730 0.014 1 617 147 147 GLY N N 111.676 0.101 1 618 148 148 VAL H H 8.775 0.002 1 619 148 148 VAL C C 176.217 0.003 1 620 148 148 VAL CA C 62.643 0.029 1 621 148 148 VAL CB C 32.648 0.012 1 622 148 148 VAL N N 124.322 0.024 1 623 149 149 ILE H H 8.727 0.003 1 624 149 149 ILE C C 175.723 0.020 1 625 149 149 ILE CA C 62.481 0.045 1 626 149 149 ILE CB C 37.448 0.030 1 627 149 149 ILE N N 128.736 0.069 1 628 150 150 GLY H H 8.871 0.006 1 629 150 150 GLY C C 172.557 0.030 1 630 150 150 GLY CA C 43.732 0.032 1 631 150 150 GLY N N 117.859 0.063 1 632 151 151 ILE H H 8.561 0.001 1 633 151 151 ILE C C 175.479 0.042 1 634 151 151 ILE CA C 61.520 0.029 1 635 151 151 ILE CB C 38.337 0.003 1 636 151 151 ILE N N 121.153 0.042 1 637 152 152 ALA H H 8.315 0.002 1 638 152 152 ALA C C 175.413 0.030 1 639 152 152 ALA CA C 51.217 0.027 1 640 152 152 ALA CB C 20.560 0.025 1 641 152 152 ALA N N 131.080 0.048 1 642 153 153 GLN H H 8.046 0.002 1 643 153 153 GLN C C 180.732 0.030 1 644 153 153 GLN CA C 57.409 0.025 1 645 153 153 GLN CB C 30.599 0.030 1 646 153 153 GLN N N 124.912 0.027 1 stop_ save_