data_15711 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Backbone chemical shift assignements for monomeric apoSOD1 ; _BMRB_accession_number 15711 _BMRB_flat_file_name bmr15711.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 2 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 150 "13C chemical shifts" 442 "15N chemical shifts" 150 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 15712 'SOD1, mutant A4V' 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 1, proline cis conformer' $SOD1 'chain 2, proline trans conformer' $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 VGDLGNVTADKDGVADVSIE 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 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 15712 SOD1 100.00 153 99.35 99.35 1.88e-102 BMRB 15713 SOD1 100.00 153 99.35 99.35 3.43e-102 BMRB 15714 SOD1 100.00 153 99.35 99.35 3.71e-102 BMRB 18509 Superoxide_dismutase_C6A-C111S_thermostable_mutant 100.00 153 98.04 98.69 1.87e-100 BMRB 18708 SUPEROXIDE_DISMUTASE_CU-ZN 100.00 153 98.04 98.69 1.87e-100 BMRB 18968 SOD1 100.00 153 100.00 100.00 3.62e-103 BMRB 26570 SOD1 100.00 153 98.04 98.69 1.87e-100 BMRB 4202 "Superoxide Dismutase" 100.00 153 98.69 100.00 2.29e-102 PDB 1BA9 "The Solution Structure Of Reduced Monomeric Superoxide Dismutase, Nmr, 36 Structures" 99.35 153 98.68 100.00 1.09e-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 4.63e-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 1.04e-99 PDB 1HL4 "The Structure Of Apo Type Human Cu, Zn Superoxide Dismutase" 100.00 154 97.39 97.39 2.49e-99 PDB 1HL5 "The Structure Of Holo Type Human Cu, Zn Superoxide Dismutase" 100.00 153 97.39 97.39 2.41e-99 PDB 1KMG "The Solution Structure Of Monomeric Copper-Free Superoxide Dismutase" 100.00 153 98.69 100.00 2.29e-102 PDB 1L3N "The Solution Structure Of Reduced Dimeric Copper Zinc Sod: The Structural Effects Of Dimerization" 100.00 153 98.04 98.69 1.87e-100 PDB 1MFM "Monomeric Human Sod Mutant F50eG51EE133Q AT ATOMIC Resolution" 100.00 153 98.69 100.00 2.29e-102 PDB 1N18 "Thermostable Mutant Of Human Superoxide Dismutase, C6a, C111s" 100.00 154 98.04 98.69 1.66e-100 PDB 1N19 "Structure Of The Hsod A4v Mutant" 100.00 154 97.39 98.04 9.03e-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 1.72e-99 PDB 1PU0 "Structure Of Human Cu,Zn Superoxide Dismutase" 100.00 153 97.39 97.39 2.41e-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 2.29e-102 PDB 1SOS "Atomic Structures Of Wild-type And Thermostable Mutant Recombinant Human Cu, Zn Superoxide Dismutase" 100.00 154 98.04 98.69 1.94e-100 PDB 1SPD "Amyotrophic Lateral Sclerosis And Structural Defects In Cu,Zn Superoxide Dismutase" 100.00 154 97.39 97.39 2.49e-99 PDB 2AF2 "Solution Structure Of Disulfide Reduced And Copper Depleted Human Superoxide Dismutase" 100.00 153 98.04 98.69 1.87e-100 PDB 2C9S "1.24 Angstroms Resolution Structure Of Zn-Zn Human Superoxide Dismutase" 100.00 153 97.39 97.39 3.20e-99 PDB 2C9U "1.24 Angstroms Resolution Structure Of As-Isolated Cu-Zn Human Superoxide Dismutase" 100.00 153 97.39 97.39 2.41e-99 PDB 2C9V "Atomic Resolution Structure Of Cu-Zn Human Superoxide Dismutase" 100.00 153 97.39 97.39 2.41e-99 PDB 2GBT "C6aC111A CUZN SUPEROXIDE DISMUTASE" 100.00 153 98.69 98.69 8.71e-101 PDB 2GBU "C6a/c111a/c57a/c146a Apo Cuzn Superoxide Dismutase" 100.00 153 97.39 97.39 1.43e-98 PDB 2GBV "C6aC111AC57AC146A HOLO CUZN SUPEROXIDE DISMUTASE" 100.00 153 97.39 97.39 1.43e-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 1.87e-100 PDB 2V0A "Atomic Resolution Crystal Structure Of Human Superoxide Dismutase" 100.00 153 97.39 97.39 2.41e-99 PDB 2XJK "Monomeric Human Cu,Zn Superoxide Dismutase" 100.00 153 100.00 100.00 3.62e-103 PDB 2XJL "Monomeric Human Cu,Zn Superoxide Dismutase Without Cu Ligands" 100.00 153 98.04 98.04 2.54e-100 PDB 3ECU "Crystal Structure Of Human Apo Cu,Zn Superoxide Dismutase (Sod1)" 100.00 153 97.39 97.39 2.41e-99 PDB 3HFF "Monomeric Human Cu,Zn Superoxide Dismutase Without Zn Ligands" 100.00 153 97.39 97.39 1.46e-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 2.41e-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 2.41e-99 PDB 3RE0 "Crystal Structure Of Human Apo Cu,zn Superoxide Dismutase (sod1) Complexed With Cisplatin" 100.00 153 97.39 97.39 2.41e-99 PDB 3T5W "2me Modified Human Sod1" 100.00 153 97.39 97.39 3.20e-99 PDB 4B3E "Structure Of Copper-Zinc Superoxide Dismutase Complexed With Bicarbonate." 100.00 154 97.39 97.39 1.86e-99 PDB 4BCY "Monomeric Human Cu,zn Superoxide Dismutase, Mutation H43f" 100.00 153 99.35 99.35 4.51e-102 PDB 4FF9 "Crystal Structure Of Cysteinylated Wt Sod1" 100.00 153 97.39 97.39 2.41e-99 PDB 4OH2 "Crystal Structure Of Cu/zn Superoxide Dismutase I149t" 100.00 153 97.39 98.04 1.11e-99 DBJ BAA14373 "unnamed protein product [Schizosaccharomyces pombe]" 98.69 179 97.35 97.35 1.43e-97 DBJ BAC20345 "Cu,Zn-superoxide dismutase [Pan troglodytes]" 100.00 154 97.39 97.39 1.86e-99 DBJ BAG35052 "unnamed protein product [Homo sapiens]" 100.00 154 97.39 97.39 1.86e-99 DBJ BAG73767 "superoxide dismutase 1, soluble [synthetic construct]" 100.00 154 97.39 97.39 1.86e-99 EMBL CAA26182 "unnamed protein product [Homo sapiens]" 100.00 154 97.39 97.39 1.86e-99 EMBL CAG29351 "SOD1 [Homo sapiens]" 100.00 154 97.39 97.39 1.86e-99 EMBL CAG46542 "SOD1 [Homo sapiens]" 100.00 154 97.39 97.39 1.86e-99 GB AAA72747 "CuZn superoxide dismutase [synthetic construct]" 100.00 154 98.04 98.69 1.66e-100 GB AAA80237 "HSOD-GlyProGly-A+, partial [synthetic construct]" 100.00 171 98.04 98.69 7.22e-100 GB AAB05661 "Cu/Zn-superoxide dismutase [Homo sapiens]" 100.00 154 97.39 97.39 1.86e-99 GB AAD42179 "superoxide dismutase/HCV major epitope fusion protein [synthetic construct]" 100.00 839 97.39 97.39 1.09e-93 GB AAH01034 "Superoxide dismutase 1, soluble [Homo sapiens]" 100.00 154 97.39 97.39 1.86e-99 REF NP_000445 "superoxide dismutase [Cu-Zn] [Homo sapiens]" 100.00 154 97.39 97.39 1.86e-99 REF NP_001009025 "superoxide dismutase [Cu-Zn] [Pan troglodytes]" 100.00 154 97.39 97.39 1.86e-99 REF XP_003813274 "PREDICTED: superoxide dismutase [Cu-Zn] [Pan paniscus]" 100.00 154 97.39 97.39 1.86e-99 REF XP_008976454 "PREDICTED: superoxide dismutase [Cu-Zn] [Pan paniscus]" 100.00 154 97.39 97.39 1.86e-99 SP P00441 "RecName: Full=Superoxide dismutase [Cu-Zn]; AltName: Full=Superoxide dismutase 1; Short=hSod1" 100.00 154 97.39 97.39 1.86e-99 SP P60052 "RecName: Full=Superoxide dismutase [Cu-Zn]" 100.00 154 97.39 97.39 1.86e-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 . . 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_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 1, proline cis conformer' _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 173.668 0.015 1 2 1 1 ALA CA C 51.979 0.010 1 3 1 1 ALA CB C 20.319 0.028 1 4 2 2 THR H H 8.534 0.003 1 5 2 2 THR C C 172.406 0.016 1 6 2 2 THR CA C 62.600 0.029 1 7 2 2 THR N N 115.972 0.087 1 8 3 3 LYS H H 8.710 0.002 1 9 3 3 LYS C C 174.453 0.014 1 10 3 3 LYS CA C 55.020 0.029 1 11 3 3 LYS CB C 36.633 0.014 1 12 3 3 LYS N N 125.886 0.095 1 13 4 4 ALA H H 9.126 0.005 1 14 4 4 ALA C C 175.183 0.006 1 15 4 4 ALA CA C 50.654 0.025 1 16 4 4 ALA CB C 23.749 0.013 1 17 4 4 ALA N N 122.924 0.100 1 18 5 5 VAL H H 9.455 0.003 1 19 5 5 VAL C C 173.118 0.015 1 20 5 5 VAL CA C 60.381 0.014 1 21 5 5 VAL CB C 36.424 0.025 1 22 5 5 VAL N N 120.817 0.089 1 23 6 6 ALA H H 9.406 0.003 1 24 6 6 ALA C C 174.503 0.017 1 25 6 6 ALA CA C 50.966 0.028 1 26 6 6 ALA CB C 23.635 0.008 1 27 6 6 ALA N N 128.962 0.101 1 28 7 7 VAL H H 9.214 0.003 1 29 7 7 VAL C C 175.672 0.005 1 30 7 7 VAL CA C 61.998 0.064 1 31 7 7 VAL CB C 31.802 0.030 1 32 7 7 VAL N N 125.422 0.078 1 33 8 8 LEU H H 8.755 0.005 1 34 8 8 LEU C C 176.029 0.030 1 35 8 8 LEU CA C 54.107 0.031 1 36 8 8 LEU CB C 43.199 0.035 1 37 8 8 LEU N N 126.421 0.080 1 38 9 9 LYS H H 8.302 0.005 1 39 9 9 LYS C C 175.417 0.013 1 40 9 9 LYS CA C 55.330 0.064 1 41 9 9 LYS CB C 36.551 0.041 1 42 9 9 LYS N N 121.350 0.118 1 43 10 10 GLY H H 8.658 0.004 1 44 10 10 GLY C C 172.618 0.030 1 45 10 10 GLY CA C 45.386 0.006 1 46 10 10 GLY N N 112.394 0.067 1 47 11 11 ASP H H 8.749 0.006 1 48 11 11 ASP C C 176.819 0.009 1 49 11 11 ASP CA C 54.675 0.043 1 50 11 11 ASP CB C 41.045 0.008 1 51 11 11 ASP N N 121.266 0.101 1 52 12 12 GLY H H 8.169 0.005 1 53 12 12 GLY C C 173.609 0.030 1 54 12 12 GLY CA C 44.473 0.007 1 55 12 12 GLY N N 110.473 0.079 1 56 13 13 PRO C C 176.546 0.002 1 57 13 13 PRO CA C 63.468 0.002 1 58 13 13 PRO CB C 32.622 0.030 1 59 14 14 VAL H H 7.414 0.004 1 60 14 14 VAL C C 176.027 0.005 1 61 14 14 VAL CA C 63.030 0.032 1 62 14 14 VAL CB C 30.796 0.007 1 63 14 14 VAL N N 120.878 0.097 1 64 15 15 GLN H H 8.069 0.005 1 65 15 15 GLN C C 174.279 0.008 1 66 15 15 GLN CA C 54.159 0.016 1 67 15 15 GLN CB C 32.519 0.049 1 68 15 15 GLN N N 123.552 0.067 1 69 16 16 GLY H H 8.259 0.005 1 70 16 16 GLY C C 170.855 0.030 1 71 16 16 GLY CA C 46.761 0.015 1 72 16 16 GLY N N 107.824 0.084 1 73 17 17 ILE H H 8.014 0.004 1 74 17 17 ILE C C 174.086 0.011 1 75 17 17 ILE CA C 61.301 0.042 1 76 17 17 ILE CB C 40.851 0.035 1 77 17 17 ILE N N 120.840 0.090 1 78 18 18 ILE H H 8.824 0.003 1 79 18 18 ILE C C 172.609 0.010 1 80 18 18 ILE CA C 56.826 0.052 1 81 18 18 ILE CB C 37.555 0.021 1 82 18 18 ILE N N 126.685 0.085 1 83 19 19 ASN H H 8.779 0.003 1 84 19 19 ASN C C 172.197 0.012 1 85 19 19 ASN CA C 52.377 0.056 1 86 19 19 ASN CB C 40.498 0.020 1 87 19 19 ASN N N 124.498 0.085 1 88 20 20 PHE H H 8.508 0.003 1 89 20 20 PHE C C 176.373 0.016 1 90 20 20 PHE CA C 55.235 0.012 1 91 20 20 PHE CB C 43.291 0.050 1 92 20 20 PHE N N 115.094 0.088 1 93 21 21 GLU H H 9.620 0.003 1 94 21 21 GLU C C 173.688 0.019 1 95 21 21 GLU CA C 56.175 0.016 1 96 21 21 GLU CB C 34.537 0.008 1 97 21 21 GLU N N 122.243 0.097 1 98 22 22 GLN H H 9.170 0.004 1 99 22 22 GLN C C 174.666 0.022 1 100 22 22 GLN CA C 54.534 0.035 1 101 22 22 GLN CB C 32.811 0.017 1 102 22 22 GLN N N 129.803 0.097 1 103 23 23 LYS H H 9.223 0.003 1 104 23 23 LYS C C 176.188 0.006 1 105 23 23 LYS CA C 59.703 0.028 1 106 23 23 LYS CB C 33.164 0.065 1 107 23 23 LYS N N 130.123 0.086 1 108 24 24 GLU H H 8.141 0.004 1 109 24 24 GLU C C 177.297 0.003 1 110 24 24 GLU CA C 54.412 0.076 1 111 24 24 GLU CB C 32.479 0.013 1 112 24 24 GLU N N 115.730 0.095 1 113 25 25 SER H H 8.844 0.002 1 114 25 25 SER C C 174.528 0.020 1 115 25 25 SER CA C 61.267 0.108 1 116 25 25 SER CB C 62.830 0.072 1 117 25 25 SER N N 118.400 0.075 1 118 26 26 ASN H H 8.324 0.003 1 119 26 26 ASN C C 175.148 0.015 1 120 26 26 ASN CA C 52.973 0.043 1 121 26 26 ASN CB C 38.170 0.035 1 122 26 26 ASN N N 117.076 0.093 1 123 27 27 GLY H H 7.929 0.004 1 124 27 27 GLY C C 172.048 0.030 1 125 27 27 GLY CA C 44.611 0.004 1 126 27 27 GLY N N 108.128 0.086 1 127 28 28 PRO C C 176.189 0.030 1 128 28 28 PRO CA C 63.064 0.070 1 129 28 28 PRO CB C 33.023 0.030 1 130 29 29 VAL H H 8.966 0.012 1 131 29 29 VAL C C 175.242 0.058 1 132 29 29 VAL CA C 61.150 0.020 1 133 29 29 VAL CB C 33.658 0.030 1 134 29 29 VAL N N 121.556 0.104 1 135 30 30 LYS H H 9.167 0.003 1 136 30 30 LYS C C 175.298 0.019 1 137 30 30 LYS CA C 55.885 0.060 1 138 30 30 LYS CB C 34.462 0.021 1 139 30 30 LYS N N 128.498 0.074 1 140 31 31 VAL H H 9.243 0.004 1 141 31 31 VAL C C 175.383 0.003 1 142 31 31 VAL CA C 60.476 0.045 1 143 31 31 VAL CB C 33.665 0.049 1 144 31 31 VAL N N 126.787 0.081 1 145 32 32 TRP H H 9.026 0.004 1 146 32 32 TRP HE1 H 10.312 0.004 1 147 32 32 TRP C C 173.401 0.012 1 148 32 32 TRP CA C 56.133 0.024 1 149 32 32 TRP CB C 32.457 0.003 1 150 32 32 TRP N N 125.610 0.079 1 151 32 32 TRP NE1 N 130.011 0.070 1 152 33 33 GLY H H 8.479 0.005 1 153 33 33 GLY C C 171.341 0.008 1 154 33 33 GLY CA C 44.745 0.013 1 155 33 33 GLY N N 108.520 0.093 1 156 34 34 SER H H 7.833 0.004 1 157 34 34 SER C C 172.974 0.132 1 158 34 34 SER CA C 57.011 0.022 1 159 34 34 SER CB C 65.364 0.030 1 160 34 34 SER N N 114.137 0.078 1 161 35 35 ILE H H 8.653 0.004 1 162 35 35 ILE C C 173.139 0.030 1 163 35 35 ILE CA C 60.192 0.032 1 164 35 35 ILE CB C 41.380 0.030 1 165 35 35 ILE N N 123.982 0.135 1 166 36 36 LYS H H 9.027 0.003 1 167 36 36 LYS C C 175.575 0.016 1 168 36 36 LYS CA C 54.539 0.038 1 169 36 36 LYS CB C 35.311 0.006 1 170 36 36 LYS N N 124.324 0.080 1 171 37 37 GLY H H 8.294 0.004 1 172 37 37 GLY C C 176.015 0.030 1 173 37 37 GLY CA C 45.688 0.029 1 174 37 37 GLY N N 106.424 0.094 1 175 38 38 LEU H H 8.325 0.004 1 176 38 38 LEU C C 176.957 0.007 1 177 38 38 LEU CA C 53.528 0.035 1 178 38 38 LEU CB C 44.284 0.013 1 179 38 38 LEU N N 120.648 0.119 1 180 39 39 THR H H 8.013 0.012 1 181 39 39 THR C C 175.863 0.034 1 182 39 39 THR CA C 61.272 0.053 1 183 39 39 THR CB C 69.618 0.030 1 184 39 39 THR N N 110.624 0.117 1 185 40 40 GLU H H 8.728 0.004 1 186 40 40 GLU C C 176.004 0.038 1 187 40 40 GLU CA C 57.570 0.017 1 188 40 40 GLU CB C 30.472 0.037 1 189 40 40 GLU N N 126.442 0.049 1 190 41 41 GLY H H 8.685 0.004 1 191 41 41 GLY C C 172.941 0.002 1 192 41 41 GLY CA C 43.258 0.024 1 193 41 41 GLY N N 113.743 0.076 1 194 42 42 LEU H H 8.235 0.009 1 195 42 42 LEU C C 177.356 0.012 1 196 42 42 LEU CA C 55.103 0.032 1 197 42 42 LEU CB C 44.707 0.040 1 198 42 42 LEU N N 120.402 0.154 1 199 43 43 HIS H H 8.746 0.018 1 200 43 43 HIS C C 173.786 0.022 1 201 43 43 HIS CA C 54.538 0.055 1 202 43 43 HIS CB C 31.784 0.006 1 203 43 43 HIS N N 116.076 0.215 1 204 44 44 GLY H H 8.698 0.008 1 205 44 44 GLY C C 172.208 0.030 1 206 44 44 GLY CA C 46.284 0.011 1 207 44 44 GLY N N 112.523 0.020 1 208 45 45 PHE H H 8.774 0.013 1 209 45 45 PHE C C 173.810 0.018 1 210 45 45 PHE CA C 54.998 0.020 1 211 45 45 PHE CB C 41.677 0.007 1 212 45 45 PHE N N 127.721 0.052 1 213 46 46 HIS H H 8.836 0.017 1 214 46 46 HIS C C 173.358 0.018 1 215 46 46 HIS CA C 53.294 0.018 1 216 46 46 HIS CB C 35.243 0.033 1 217 46 46 HIS N N 121.476 0.063 1 218 47 47 VAL H H 9.108 0.028 1 219 47 47 VAL C C 175.844 0.028 1 220 47 47 VAL CA C 61.420 0.023 1 221 47 47 VAL CB C 32.715 0.072 1 222 47 47 VAL N N 122.081 0.058 1 223 48 48 HIS H H 9.679 0.003 1 224 48 48 HIS C C 174.594 0.010 1 225 48 48 HIS CA C 55.510 0.017 1 226 48 48 HIS CB C 31.802 0.029 1 227 48 48 HIS N N 128.313 0.190 1 228 49 49 GLU H H 8.950 0.010 1 229 49 49 GLU C C 175.572 0.017 1 230 49 49 GLU CA C 56.520 0.059 1 231 49 49 GLU CB C 30.471 0.060 1 232 49 49 GLU N N 123.659 0.075 1 233 50 50 GLU H H 8.752 0.019 1 234 50 50 GLU C C 176.130 0.005 1 235 50 50 GLU CA C 56.506 0.016 1 236 50 50 GLU CB C 30.444 0.030 1 237 50 50 GLU N N 122.310 0.158 1 238 51 51 GLU H H 8.572 0.013 1 239 51 51 GLU C C 175.949 0.036 1 240 51 51 GLU CA C 56.732 0.009 1 241 51 51 GLU CB C 30.556 0.010 1 242 51 51 GLU N N 121.644 0.162 1 243 52 52 ASP H H 8.285 0.005 1 244 52 52 ASP C C 176.027 0.026 1 245 52 52 ASP CA C 54.088 0.003 1 246 52 52 ASP CB C 41.246 0.014 1 247 52 52 ASP N N 120.284 0.119 1 248 53 53 ASN H H 8.472 0.006 1 249 53 53 ASN C C 175.957 0.041 1 250 53 53 ASN CA C 53.722 0.034 1 251 53 53 ASN CB C 38.749 0.002 1 252 53 53 ASN N N 119.462 0.170 1 253 54 54 THR H H 8.235 0.007 1 254 54 54 THR C C 174.827 0.014 1 255 54 54 THR CA C 62.783 0.068 1 256 54 54 THR CB C 69.656 0.093 1 257 54 54 THR N N 113.455 0.109 1 258 55 55 ALA H H 8.178 0.003 1 259 55 55 ALA C C 177.972 0.007 1 260 55 55 ALA CA C 52.797 0.010 1 261 55 55 ALA CB C 19.121 0.026 1 262 55 55 ALA N N 125.342 0.060 1 263 56 56 GLY H H 8.174 0.008 1 264 56 56 GLY C C 174.511 0.195 1 265 56 56 GLY CA C 45.512 0.007 1 266 56 56 GLY N N 107.500 0.055 1 267 57 57 CYS H H 8.539 0.003 1 268 57 57 CYS C C 174.636 0.058 1 269 57 57 CYS CA C 55.879 0.044 1 270 57 57 CYS CB C 41.126 0.013 1 271 57 57 CYS N N 118.869 0.065 1 272 58 58 THR H H 8.165 0.007 1 273 58 58 THR C C 174.343 0.168 1 274 58 58 THR CA C 62.032 0.030 1 275 58 58 THR CB C 69.933 0.030 1 276 58 58 THR N N 114.187 0.052 1 277 59 59 SER H H 8.391 0.005 1 278 59 59 SER C C 174.241 0.129 1 279 59 59 SER CA C 58.518 0.027 1 280 59 59 SER CB C 63.862 0.072 1 281 59 59 SER N N 118.239 0.102 1 282 60 60 ALA H H 8.227 0.004 6 283 60 60 ALA C C 177.590 0.007 6 284 60 60 ALA CA C 52.431 0.013 6 285 60 60 ALA CB C 19.708 0.023 6 286 60 60 ALA N N 125.478 0.036 6 287 61 61 GLY H H 8.128 0.002 6 288 61 61 GLY C C 171.899 0.030 6 289 61 61 GLY CA C 44.636 0.001 6 290 61 61 GLY N N 107.899 0.064 6 291 62 62 PRO C C 176.603 0.010 6 292 62 62 PRO CA C 62.613 0.007 6 293 62 62 PRO CB C 34.727 0.030 6 294 63 63 HIS H H 8.604 0.004 6 295 63 63 HIS C C 176.178 0.010 6 296 63 63 HIS CA C 56.521 0.027 6 297 63 63 HIS CB C 33.150 0.011 6 298 63 63 HIS N N 122.227 0.084 6 299 64 64 PHE H H 8.523 0.003 6 300 64 64 PHE C C 177.482 0.002 6 301 64 64 PHE CA C 54.793 0.012 6 302 64 64 PHE CB C 41.069 0.007 6 303 64 64 PHE N N 121.987 0.103 6 304 65 65 ASN H H 8.499 0.012 6 305 65 65 ASN CA C 59.288 0.030 6 306 65 65 ASN CB C 39.204 0.030 6 307 65 65 ASN N N 120.618 0.094 6 308 66 66 PRO C C 177.095 0.003 1 309 66 66 PRO CA C 63.698 0.037 1 310 66 66 PRO CB C 32.175 0.039 1 311 67 67 LEU H H 8.085 0.003 1 312 67 67 LEU C C 177.653 0.004 1 313 67 67 LEU CA C 55.353 0.035 1 314 67 67 LEU CB C 41.750 0.010 1 315 67 67 LEU N N 119.666 0.077 1 316 68 68 SER H H 7.919 0.002 1 317 68 68 SER C C 174.601 0.011 1 318 68 68 SER CA C 58.550 0.027 1 319 68 68 SER CB C 63.720 0.054 1 320 68 68 SER N N 115.385 0.066 1 321 69 69 ARG H H 8.186 0.005 1 322 69 69 ARG C C 176.242 0.116 1 323 69 69 ARG CA C 56.085 0.120 1 324 69 69 ARG CB C 30.804 0.007 1 325 69 69 ARG N N 122.812 0.077 1 326 70 70 LYS H H 8.297 0.003 1 327 70 70 LYS C C 176.411 0.030 1 328 70 70 LYS CA C 56.448 0.025 1 329 70 70 LYS CB C 33.033 0.002 1 330 70 70 LYS N N 122.225 0.122 1 331 71 71 HIS H H 8.502 0.019 1 332 71 71 HIS C C 175.082 0.011 1 333 71 71 HIS CA C 55.555 0.031 1 334 71 71 HIS CB C 29.766 0.018 1 335 71 71 HIS N N 119.973 0.226 1 336 72 72 GLY H H 8.530 0.008 6 337 72 72 GLY C C 174.194 0.011 6 338 72 72 GLY CA C 45.202 0.018 6 339 72 72 GLY N N 110.656 0.095 6 340 73 73 GLY H H 8.308 0.003 6 341 73 73 GLY C C 172.105 0.030 6 342 73 73 GLY CA C 44.596 0.004 6 343 73 73 GLY N N 109.227 0.113 6 344 74 74 PRO CA C 63.541 0.022 1 345 74 74 PRO CB C 32.247 0.030 1 346 75 75 LYS H H 8.486 0.003 1 347 75 75 LYS C C 176.642 0.004 1 348 75 75 LYS CA C 56.471 0.020 1 349 75 75 LYS CB C 32.784 0.026 1 350 75 75 LYS N N 120.560 0.080 1 351 76 76 ASP H H 8.244 0.004 1 352 76 76 ASP C C 176.421 0.030 1 353 76 76 ASP CA C 54.927 0.042 1 354 76 76 ASP CB C 41.096 0.002 1 355 76 76 ASP N N 121.094 0.091 1 356 77 77 GLU H H 8.337 0.003 1 357 77 77 GLU C C 176.523 0.030 1 358 77 77 GLU CA C 56.748 0.013 1 359 77 77 GLU CB C 30.328 0.016 1 360 77 77 GLU N N 120.435 0.047 1 361 78 78 GLU H H 8.263 0.005 1 362 78 78 GLU C C 176.466 0.118 1 363 78 78 GLU CA C 56.632 0.012 1 364 78 78 GLU CB C 30.286 0.001 1 365 78 78 GLU N N 121.416 0.111 1 366 79 79 ARG H H 8.197 0.003 1 367 79 79 ARG C C 176.056 0.021 1 368 79 79 ARG CA C 56.053 0.010 1 369 79 79 ARG CB C 30.955 0.024 1 370 79 79 ARG N N 121.460 0.132 1 371 80 80 HIS H H 8.665 0.006 1 372 80 80 HIS C C 174.637 0.014 1 373 80 80 HIS CA C 55.525 0.050 1 374 80 80 HIS CB C 29.157 0.027 1 375 80 80 HIS N N 120.005 0.326 1 376 81 81 VAL H H 8.136 0.008 1 377 81 81 VAL C C 176.007 0.023 1 378 81 81 VAL CA C 62.482 0.017 1 379 81 81 VAL CB C 33.005 0.030 1 380 81 81 VAL N N 122.190 0.194 1 381 82 82 GLY H H 8.760 0.005 1 382 82 82 GLY CA C 45.120 0.030 1 383 82 82 GLY N N 112.760 0.078 1 384 84 84 LEU C C 176.368 0.030 1 385 84 84 LEU CA C 55.333 0.030 1 386 84 84 LEU CB C 42.066 0.030 1 387 85 85 GLY H H 8.435 0.022 1 388 85 85 GLY C C 172.175 0.030 1 389 85 85 GLY CA C 44.642 0.018 1 390 85 85 GLY N N 108.973 0.208 1 391 86 86 ASN H H 8.310 0.008 1 392 86 86 ASN C C 177.203 0.004 1 393 86 86 ASN CA C 52.678 0.030 1 394 86 86 ASN CB C 41.964 0.011 1 395 86 86 ASN N N 116.866 0.147 1 396 87 87 VAL H H 9.023 0.002 1 397 87 87 VAL C C 174.642 0.019 1 398 87 87 VAL CA C 59.191 0.041 1 399 87 87 VAL CB C 32.729 0.001 1 400 87 87 VAL N N 114.827 0.150 1 401 88 88 THR H H 8.600 0.005 1 402 88 88 THR C C 173.572 0.023 1 403 88 88 THR CA C 61.726 0.037 1 404 88 88 THR CB C 70.055 0.030 1 405 88 88 THR N N 118.586 0.076 1 406 89 89 ALA H H 9.217 0.005 1 407 89 89 ALA C C 177.564 0.001 1 408 89 89 ALA CA C 49.553 0.024 1 409 89 89 ALA CB C 21.309 0.018 1 410 89 89 ALA N N 129.339 0.085 1 411 90 90 ASP H H 8.501 0.004 1 412 90 90 ASP C C 177.142 0.071 1 413 90 90 ASP CA C 52.580 0.036 1 414 90 90 ASP CB C 41.594 0.002 1 415 90 90 ASP N N 125.078 0.088 1 416 91 91 LYS H H 8.186 0.003 1 417 91 91 LYS C C 177.246 0.030 1 418 91 91 LYS CA C 58.544 0.015 1 419 91 91 LYS CB C 31.859 0.009 1 420 91 91 LYS N N 115.281 0.056 1 421 92 92 ASP H H 8.159 0.006 1 422 92 92 ASP C C 176.292 0.030 1 423 92 92 ASP CA C 54.362 0.004 1 424 92 92 ASP CB C 41.569 0.015 1 425 92 92 ASP N N 119.712 0.130 1 426 93 93 GLY H H 8.432 0.004 1 427 93 93 GLY C C 172.915 0.030 1 428 93 93 GLY CA C 46.935 0.007 1 429 93 93 GLY N N 111.536 0.108 1 430 94 94 VAL H H 7.950 0.007 1 431 94 94 VAL C C 176.543 0.003 1 432 94 94 VAL CA C 61.625 0.008 1 433 94 94 VAL CB C 32.981 0.018 1 434 94 94 VAL N N 119.525 0.099 1 435 95 95 ALA H H 9.581 0.002 1 436 95 95 ALA C C 174.885 0.011 1 437 95 95 ALA CA C 50.172 0.036 1 438 95 95 ALA CB C 21.117 0.017 1 439 95 95 ALA N N 131.370 0.101 1 440 96 96 ASP H H 8.617 0.003 1 441 96 96 ASP C C 175.577 0.012 1 442 96 96 ASP CA C 54.089 0.027 1 443 96 96 ASP CB C 41.825 0.007 1 444 96 96 ASP N N 125.337 0.101 1 445 97 97 VAL H H 8.638 0.008 1 446 97 97 VAL C C 176.623 0.003 1 447 97 97 VAL CA C 61.960 0.060 1 448 97 97 VAL CB C 33.746 0.002 1 449 97 97 VAL N N 125.112 0.083 1 450 98 98 SER H H 8.843 0.004 1 451 98 98 SER C C 173.069 0.022 1 452 98 98 SER CA C 58.295 0.037 1 453 98 98 SER CB C 62.595 0.009 1 454 98 98 SER N N 123.718 0.092 1 455 99 99 ILE H H 9.407 0.003 1 456 99 99 ILE C C 174.644 0.150 1 457 99 99 ILE CA C 60.285 0.058 1 458 99 99 ILE CB C 44.266 0.029 1 459 99 99 ILE N N 126.362 0.058 1 460 100 100 GLU H H 8.641 0.002 1 461 100 100 GLU C C 174.944 0.094 1 462 100 100 GLU CA C 55.690 0.038 1 463 100 100 GLU CB C 32.399 0.030 1 464 100 100 GLU N N 124.788 0.078 1 465 101 101 ASP H H 9.177 0.003 1 466 101 101 ASP C C 175.044 0.014 1 467 101 101 ASP CA C 53.932 0.034 1 468 101 101 ASP CB C 46.177 0.009 1 469 101 101 ASP N N 126.731 0.140 1 470 102 102 SER H H 8.922 0.008 1 471 102 102 SER C C 173.775 0.015 1 472 102 102 SER CA C 58.623 0.008 1 473 102 102 SER CB C 64.159 0.006 1 474 102 102 SER N N 119.413 0.053 1 475 103 103 VAL H H 8.817 0.022 1 476 103 103 VAL C C 177.795 0.005 1 477 103 103 VAL CA C 64.122 0.014 1 478 103 103 VAL CB C 32.437 0.030 1 479 103 103 VAL N N 122.809 0.268 1 480 104 104 ILE H H 7.793 0.026 1 481 104 104 ILE C C 173.034 0.020 1 482 104 104 ILE CA C 61.406 0.037 1 483 104 104 ILE CB C 40.055 0.052 1 484 104 104 ILE N N 113.520 0.174 1 485 105 105 SER H H 7.604 0.007 1 486 105 105 SER C C 173.897 0.015 1 487 105 105 SER CA C 56.261 0.063 1 488 105 105 SER CB C 65.374 0.032 1 489 105 105 SER N N 108.727 0.081 1 490 106 106 LEU H H 8.448 0.007 1 491 106 106 LEU C C 174.533 0.006 1 492 106 106 LEU CA C 54.621 0.019 1 493 106 106 LEU CB C 41.317 0.002 1 494 106 106 LEU N N 122.042 0.079 1 495 107 107 SER H H 8.217 0.004 1 496 107 107 SER C C 173.632 0.012 1 497 107 107 SER CA C 57.333 0.066 1 498 107 107 SER CB C 65.874 0.036 1 499 107 107 SER N N 112.458 0.084 1 500 108 108 GLY H H 8.617 0.003 1 501 108 108 GLY C C 175.340 0.030 1 502 108 108 GLY CA C 44.816 0.008 1 503 108 108 GLY N N 108.606 0.095 1 504 109 109 ASP H H 8.610 0.002 1 505 109 109 ASP C C 176.993 0.010 1 506 109 109 ASP CA C 56.459 0.025 1 507 109 109 ASP CB C 40.485 0.025 1 508 109 109 ASP N N 119.721 0.112 1 509 110 110 HIS H H 8.844 0.007 1 510 110 110 HIS C C 173.755 0.011 1 511 110 110 HIS CA C 53.707 0.051 1 512 110 110 HIS CB C 27.696 0.020 1 513 110 110 HIS N N 116.776 0.122 1 514 111 111 ALA H H 7.086 0.005 1 515 111 111 ALA C C 179.475 0.004 1 516 111 111 ALA CA C 52.319 0.019 1 517 111 111 ALA CB C 19.695 0.014 1 518 111 111 ALA N N 121.311 0.076 1 519 112 112 ILE H H 7.822 0.004 1 520 112 112 ILE C C 175.193 0.018 1 521 112 112 ILE CA C 61.776 0.177 1 522 112 112 ILE CB C 37.524 0.008 1 523 112 112 ILE N N 108.791 0.079 1 524 113 113 ILE H H 6.231 0.004 1 525 113 113 ILE C C 176.850 0.003 1 526 113 113 ILE CA C 61.565 0.010 1 527 113 113 ILE CB C 35.602 0.020 1 528 113 113 ILE N N 118.526 0.083 1 529 114 114 GLY H H 9.228 0.003 1 530 114 114 GLY C C 174.481 0.023 1 531 114 114 GLY CA C 45.131 0.015 1 532 114 114 GLY N N 116.963 0.091 1 533 115 115 ARG H H 7.795 0.003 1 534 115 115 ARG C C 174.195 0.012 1 535 115 115 ARG CA C 55.536 0.024 1 536 115 115 ARG CB C 30.329 0.030 1 537 115 115 ARG N N 119.041 0.123 1 538 116 116 THR H H 8.403 0.019 1 539 116 116 THR C C 173.139 0.002 1 540 116 116 THR CA C 62.117 0.036 1 541 116 116 THR N N 113.615 0.246 1 542 117 117 LEU H H 9.193 0.004 1 543 117 117 LEU C C 174.620 0.005 1 544 117 117 LEU CA C 53.679 0.010 1 545 117 117 LEU CB C 43.958 0.009 1 546 117 117 LEU N N 129.472 0.203 1 547 118 118 VAL H H 9.042 0.008 1 548 118 118 VAL C C 174.886 0.030 1 549 118 118 VAL CA C 60.466 0.019 1 550 118 118 VAL CB C 36.265 0.030 1 551 118 118 VAL N N 123.845 0.156 1 552 119 119 VAL C C 174.632 0.030 1 553 119 119 VAL CB C 34.044 0.030 1 554 120 120 HIS H H 9.381 0.020 1 555 120 120 HIS C C 175.212 0.006 1 556 120 120 HIS CA C 56.343 0.067 1 557 120 120 HIS CB C 32.323 0.030 1 558 120 120 HIS N N 128.101 0.039 1 559 121 121 GLU H H 8.838 0.012 1 560 121 121 GLU C C 176.840 0.008 1 561 121 121 GLU CA C 59.492 0.011 1 562 121 121 GLU CB C 31.468 0.075 1 563 121 121 GLU N N 122.406 0.165 1 564 122 122 LYS H H 8.752 0.034 1 565 122 122 LYS C C 176.222 0.002 1 566 122 122 LYS CA C 54.953 0.072 1 567 122 122 LYS CB C 34.153 0.003 1 568 122 122 LYS N N 118.556 0.402 1 569 123 123 ALA H H 8.278 0.008 1 570 123 123 ALA C C 177.399 0.018 1 571 123 123 ALA CA C 51.876 0.014 1 572 123 123 ALA CB C 20.171 0.036 1 573 123 123 ALA N N 124.495 0.146 1 574 124 124 ASP H H 9.220 0.060 1 575 124 124 ASP C C 176.399 0.008 1 576 124 124 ASP CA C 54.445 0.048 1 577 124 124 ASP CB C 41.034 0.011 1 578 124 124 ASP N N 120.948 0.077 1 579 125 125 ASP H H 8.553 0.014 1 580 125 125 ASP C C 176.377 0.012 1 581 125 125 ASP CA C 54.066 0.025 1 582 125 125 ASP CB C 41.366 0.027 1 583 125 125 ASP N N 122.828 0.022 1 584 126 126 LEU H H 8.407 0.008 1 585 126 126 LEU C C 178.105 0.004 1 586 126 126 LEU CA C 55.565 0.023 1 587 126 126 LEU CB C 41.669 0.014 1 588 126 126 LEU N N 122.528 0.053 1 589 127 127 GLY H H 8.506 0.005 1 590 127 127 GLY C C 174.668 0.030 1 591 127 127 GLY CA C 45.627 0.026 1 592 127 127 GLY N N 108.892 0.091 1 593 128 128 LYS H H 8.117 0.005 1 594 128 128 LYS C C 177.291 0.007 1 595 128 128 LYS CA C 56.355 0.039 1 596 128 128 LYS CB C 32.890 0.026 1 597 128 128 LYS N N 120.474 0.091 1 598 129 129 GLY H H 8.516 0.003 1 599 129 129 GLY C C 174.726 0.015 1 600 129 129 GLY CA C 45.399 0.011 1 601 129 129 GLY N N 109.759 0.079 1 602 130 130 GLY H H 8.330 0.005 1 603 130 130 GLY C C 174.103 0.016 1 604 130 130 GLY CA C 45.375 0.003 1 605 130 130 GLY N N 108.807 0.090 1 606 131 131 ASN H H 8.376 0.003 1 607 131 131 ASN C C 175.520 0.026 1 608 131 131 ASN CA C 53.287 0.016 1 609 131 131 ASN CB C 39.041 0.011 1 610 131 131 ASN N N 118.513 0.085 1 611 132 132 GLU H H 8.575 0.005 1 612 132 132 GLU C C 176.877 0.006 1 613 132 132 GLU CA C 57.355 0.030 1 614 132 132 GLU CB C 29.927 0.013 1 615 132 132 GLU N N 120.950 0.104 1 616 133 133 GLU H H 8.453 0.003 1 617 133 133 GLU C C 177.179 0.018 1 618 133 133 GLU CA C 57.265 0.044 1 619 133 133 GLU CB C 30.015 0.027 1 620 133 133 GLU N N 121.050 0.078 1 621 134 134 SER H H 8.300 0.002 1 622 134 134 SER C C 175.287 0.027 1 623 134 134 SER CA C 59.145 0.048 1 624 134 134 SER CB C 63.603 0.019 1 625 134 134 SER N N 115.926 0.078 1 626 135 135 THR H H 8.044 0.003 1 627 135 135 THR C C 174.845 0.099 1 628 135 135 THR CA C 62.378 0.049 1 629 135 135 THR CB C 69.452 0.084 1 630 135 135 THR N N 114.748 0.089 1 631 136 136 LYS H H 8.196 0.003 1 632 136 136 LYS C C 176.947 0.003 1 633 136 136 LYS CA C 56.789 0.043 1 634 136 136 LYS CB C 32.978 0.003 1 635 136 136 LYS N N 122.778 0.119 1 636 137 137 THR H H 8.084 0.003 1 637 137 137 THR C C 175.290 0.008 1 638 137 137 THR CA C 62.028 0.033 1 639 137 137 THR CB C 69.987 0.161 1 640 137 137 THR N N 113.282 0.101 1 641 138 138 GLY H H 8.381 0.003 1 642 138 138 GLY C C 174.003 0.012 1 643 138 138 GLY CA C 45.557 0.015 1 644 138 138 GLY N N 111.079 0.084 1 645 139 139 ASN H H 8.316 0.001 1 646 139 139 ASN C C 175.018 0.015 1 647 139 139 ASN CA C 53.291 0.170 1 648 139 139 ASN CB C 39.178 0.003 1 649 139 139 ASN N N 118.536 0.084 1 650 140 140 ALA H H 8.350 0.005 1 651 140 140 ALA C C 177.607 0.005 1 652 140 140 ALA CA C 52.870 0.013 1 653 140 140 ALA CB C 18.584 0.011 1 654 140 140 ALA N N 123.902 0.085 1 655 141 141 GLY H H 8.249 0.005 1 656 141 141 GLY C C 174.821 0.006 1 657 141 141 GLY CA C 45.238 0.020 1 658 141 141 GLY N N 106.442 0.113 1 659 142 142 SER H H 8.694 0.003 1 660 142 142 SER C C 174.229 0.016 1 661 142 142 SER CA C 59.179 0.042 1 662 142 142 SER CB C 64.002 0.029 1 663 142 142 SER N N 117.258 0.087 1 664 143 143 ARG H H 8.685 0.004 1 665 143 143 ARG C C 175.224 0.030 1 666 143 143 ARG CA C 56.281 0.009 1 667 143 143 ARG CB C 30.701 0.030 1 668 143 143 ARG N N 121.887 0.079 1 669 145 145 ALA C C 175.190 0.002 1 670 145 145 ALA CA C 51.522 0.021 1 671 145 145 ALA CB C 21.918 0.007 1 672 146 146 CYS H H 8.692 0.005 1 673 146 146 CYS C C 173.839 0.003 1 674 146 146 CYS CA C 54.994 0.041 1 675 146 146 CYS CB C 45.520 0.045 1 676 146 146 CYS N N 116.212 0.019 1 677 147 147 GLY H H 8.659 0.004 1 678 147 147 GLY C C 171.368 0.006 1 679 147 147 GLY CA C 46.665 0.015 1 680 147 147 GLY N N 110.851 0.025 1 681 148 148 VAL H H 8.796 0.002 1 682 148 148 VAL C C 176.156 0.004 1 683 148 148 VAL CA C 62.697 0.144 1 684 148 148 VAL CB C 32.608 0.010 1 685 148 148 VAL N N 124.646 0.113 1 686 149 149 ILE H H 8.692 0.006 1 687 149 149 ILE C C 175.708 0.009 1 688 149 149 ILE CA C 62.316 0.045 1 689 149 149 ILE CB C 37.620 0.027 1 690 149 149 ILE N N 128.755 0.103 1 691 150 150 GLY H H 8.904 0.004 1 692 150 150 GLY C C 172.541 0.030 1 693 150 150 GLY CA C 43.689 0.018 1 694 150 150 GLY N N 118.002 0.080 1 695 151 151 ILE H H 8.556 0.004 1 696 151 151 ILE C C 175.424 0.002 1 697 151 151 ILE CA C 61.494 0.034 1 698 151 151 ILE CB C 38.403 0.004 1 699 151 151 ILE N N 121.224 0.103 1 700 152 152 ALA H H 8.274 0.004 1 701 152 152 ALA C C 175.406 0.011 1 702 152 152 ALA CA C 51.196 0.049 1 703 152 152 ALA CB C 20.634 0.031 1 704 152 152 ALA N N 131.055 0.104 1 705 153 153 GLN H H 8.043 0.001 1 706 153 153 GLN C C 176.635 0.030 1 707 153 153 GLN CA C 57.352 0.006 1 708 153 153 GLN CB C 30.666 0.030 1 709 153 153 GLN N N 124.927 0.082 1 stop_ save_ save_assigned_chem_shift_list_1_2 _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 2, proline trans conformer' _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 60 60 ALA H H 8.351 0.004 6 2 60 60 ALA C C 177.581 0.004 6 3 60 60 ALA CA C 52.648 0.033 6 4 60 60 ALA CB C 19.551 0.028 6 5 60 60 ALA N N 125.650 0.055 6 6 61 61 GLY H H 8.053 0.003 6 7 61 61 GLY C C 171.745 0.000 6 8 61 61 GLY CA C 43.672 0.007 6 9 61 61 GLY N N 107.379 0.117 6 10 62 62 PRO C C 176.899 0.008 6 11 62 62 PRO CA C 63.229 0.042 6 12 62 62 PRO CB C 32.159 0.000 6 13 63 63 HIS H H 8.502 0.025 6 14 63 63 HIS C C 174.115 0.016 6 15 63 63 HIS CA C 55.316 0.003 6 16 63 63 HIS CB C 29.403 0.005 6 17 63 63 HIS N N 118.557 0.132 6 18 64 64 PHE H H 8.172 0.018 6 19 64 64 PHE C C 174.494 0.011 6 20 64 64 PHE CA C 57.637 0.039 6 21 64 64 PHE CB C 39.904 0.012 6 22 64 64 PHE N N 121.876 0.050 6 23 65 65 ASN H H 8.438 0.005 6 24 65 65 ASN CA C 50.450 0.002 6 25 65 65 ASN N N 123.202 0.081 6 26 72 72 GLY H H 8.441 0.007 6 27 72 72 GLY C C 174.088 0.011 6 28 72 72 GLY CA C 45.246 0.028 6 29 72 72 GLY N N 110.368 0.134 6 30 73 73 GLY H H 8.195 0.003 6 31 73 73 GLY C C 172.092 0.000 6 32 73 73 GLY CA C 44.265 0.015 6 33 73 73 GLY N N 108.829 0.115 6 stop_ save_