data_19962 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Truncated L126Z-sod1 in DPC micelle ; _BMRB_accession_number 19962 _BMRB_flat_file_name bmr19962.str _Entry_type original _Submission_date 2015-05-18 _Accession_date 2015-05-18 _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 Lim 'Liang Zhong' . . 2 Song Jianxing . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 252 "13C chemical shifts" 230 "15N chemical shifts" 117 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2015-05-18 original BMRB . stop_ _Original_release_date 2015-05-18 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; Mechanism for transforming cytosolic SOD1 into integral membrane proteins of organelles by ALS-causing mutations ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID ? loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Lim Liangzhong . . 2 Lee Xiaowen . . 3 Song Jianxing . . stop_ _Journal_abbreviation 'Biochim. Biophys. Acta' _Journal_volume 1848 _Journal_issue 1 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 1 _Page_last 7 _Year 2015 _Details . save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name 'Truncated L126Z-sod1' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'Truncated L126Z-sod1' $L126Z-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_L126Z-sod1 _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common L126Z-sod1 _Molecular_mass 13153.691 _Mol_thiol_state 'all free' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 125 _Mol_residue_sequence ; ATKAVCVLKGDGPVQGIINF EQKESNGPVKVWGSIKGLTE GLHGFHVHEFGDNTAGCTSA GPHFNPLSRKHGGPKDEERH VGDLGNVTADKDGVADVSIE DSVISLSGDHCIIGRTLVVH EKADD ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 1 ALA 2 2 THR 3 3 LYS 4 4 ALA 5 5 VAL 6 6 CYS 7 7 VAL 8 8 LEU 9 9 LYS 10 10 GLY 11 11 ASP 12 12 GLY 13 13 PRO 14 14 VAL 15 15 GLN 16 16 GLY 17 17 ILE 18 18 ILE 19 19 ASN 20 20 PHE 21 21 GLU 22 22 GLN 23 23 LYS 24 24 GLU 25 25 SER 26 26 ASN 27 27 GLY 28 28 PRO 29 29 VAL 30 30 LYS 31 31 VAL 32 32 TRP 33 33 GLY 34 34 SER 35 35 ILE 36 36 LYS 37 37 GLY 38 38 LEU 39 39 THR 40 40 GLU 41 41 GLY 42 42 LEU 43 43 HIS 44 44 GLY 45 45 PHE 46 46 HIS 47 47 VAL 48 48 HIS 49 49 GLU 50 50 PHE 51 51 GLY 52 52 ASP 53 53 ASN 54 54 THR 55 55 ALA 56 56 GLY 57 57 CYS 58 58 THR 59 59 SER 60 60 ALA 61 61 GLY 62 62 PRO 63 63 HIS 64 64 PHE 65 65 ASN 66 66 PRO 67 67 LEU 68 68 SER 69 69 ARG 70 70 LYS 71 71 HIS 72 72 GLY 73 73 GLY 74 74 PRO 75 75 LYS 76 76 ASP 77 77 GLU 78 78 GLU 79 79 ARG 80 80 HIS 81 81 VAL 82 82 GLY 83 83 ASP 84 84 LEU 85 85 GLY 86 86 ASN 87 87 VAL 88 88 THR 89 89 ALA 90 90 ASP 91 91 LYS 92 92 ASP 93 93 GLY 94 94 VAL 95 95 ALA 96 96 ASP 97 97 VAL 98 98 SER 99 99 ILE 100 100 GLU 101 101 ASP 102 102 SER 103 103 VAL 104 104 ILE 105 105 SER 106 106 LEU 107 107 SER 108 108 GLY 109 109 ASP 110 110 HIS 111 111 CYS 112 112 ILE 113 113 ILE 114 114 GLY 115 115 ARG 116 116 THR 117 117 LEU 118 118 VAL 119 119 VAL 120 120 HIS 121 121 GLU 122 122 LYS 123 123 ALA 124 124 ASP 125 125 ASP 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 18509 Superoxide_dismutase_C6A-C111S_thermostable_mutant 100.00 153 98.40 98.40 4.25e-81 BMRB 18708 SUPEROXIDE_DISMUTASE_CU-ZN 100.00 153 98.40 98.40 4.25e-81 BMRB 26570 SOD1 100.00 153 98.40 98.40 4.25e-81 PDB 1AZV "Familial Als Mutant G37r Cuznsod (Human)" 100.00 153 99.20 99.20 2.97e-82 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 98.40 98.40 3.94e-81 PDB 1HL4 "The Structure Of Apo Type Human Cu, Zn Superoxide Dismutase" 100.00 154 100.00 100.00 2.33e-83 PDB 1HL5 "The Structure Of Holo Type Human Cu, Zn Superoxide Dismutase" 100.00 153 100.00 100.00 2.26e-83 PDB 1L3N "The Solution Structure Of Reduced Dimeric Copper Zinc Sod: The Structural Effects Of Dimerization" 100.00 153 98.40 98.40 4.25e-81 PDB 1N18 "Thermostable Mutant Of Human Superoxide Dismutase, C6a, C111s" 100.00 154 98.40 98.40 3.94e-81 PDB 1N19 "Structure Of The Hsod A4v Mutant" 100.00 154 97.60 97.60 2.25e-80 PDB 1OEZ "Zn His46arg Mutant Of Human Cu, Zn Superoxide Dismutase" 100.00 153 99.20 99.20 1.76e-82 PDB 1OZT "Crystal Structure Of Apo-H46r Familial Als Mutant Human Cu, Zn Superoxide Dismutase (Cuznsod) To 2.5a Resolution" 100.00 153 99.20 99.20 1.76e-82 PDB 1OZU "Crystal Structure Of Familial Als Mutant S134n Of Human Cu, Zn Superoxide Dismutase (Cuznsod) To 1.3a Resolution" 100.00 153 99.20 99.20 7.50e-82 PDB 1P1V "Crystal Structure Of Fals-Associated Human Copper-Zinc Superoxide Dismutase (Cuznsod) Mutant D125h To 1.4a" 99.20 153 99.19 99.19 4.69e-81 PDB 1PTZ "Crystal Structure Of The Human Cu, Zn Superoxide Dismutase, Familial Amyotrophic Lateral Sclerosis (Fals) Mutant H43r" 100.00 153 97.60 97.60 3.38e-80 PDB 1PU0 "Structure Of Human Cu,Zn Superoxide Dismutase" 100.00 153 100.00 100.00 2.26e-83 PDB 1SOS "Atomic Structures Of Wild-type And Thermostable Mutant Recombinant Human Cu, Zn Superoxide Dismutase" 100.00 154 98.40 98.40 4.39e-81 PDB 1SPD "Amyotrophic Lateral Sclerosis And Structural Defects In Cu,Zn Superoxide Dismutase" 100.00 154 100.00 100.00 2.33e-83 PDB 1UXL "I113t Mutant Of Human Sod1" 100.00 153 99.20 99.20 1.09e-82 PDB 1UXM "A4v Mutant Of Human Sod1" 100.00 153 99.20 99.20 1.31e-82 PDB 2AF2 "Solution Structure Of Disulfide Reduced And Copper Depleted Human Superoxide Dismutase" 100.00 153 98.40 98.40 4.25e-81 PDB 2C9S "1.24 Angstroms Resolution Structure Of Zn-Zn Human Superoxide Dismutase" 100.00 153 99.20 99.20 6.95e-82 PDB 2C9U "1.24 Angstroms Resolution Structure Of As-Isolated Cu-Zn Human Superoxide Dismutase" 100.00 153 100.00 100.00 2.26e-83 PDB 2C9V "Atomic Resolution Structure Of Cu-Zn Human Superoxide Dismutase" 100.00 153 100.00 100.00 2.26e-83 PDB 2GBT "C6aC111A CUZN SUPEROXIDE DISMUTASE" 100.00 153 98.40 98.40 3.65e-81 PDB 2GBU "C6a/c111a/c57a/c146a Apo Cuzn Superoxide Dismutase" 100.00 153 97.60 97.60 6.16e-81 PDB 2GBV "C6aC111AC57AC146A HOLO CUZN SUPEROXIDE DISMUTASE" 100.00 153 97.60 97.60 6.16e-81 PDB 2LU5 "Structure And Chemical Shifts Of Cu(I),Zn(Ii) Superoxide Dismutase By Solid-State Nmr" 100.00 153 98.40 98.40 4.25e-81 PDB 2MP3 "Truncated L126z-sod1 In Dpc Micelle" 100.00 132 100.00 100.00 1.21e-82 PDB 2NNX "Crystal Structure Of The H46r, H48q Double Mutant Of Human [cu-Zn] Superoxide Dismutase" 100.00 154 98.40 98.40 9.33e-82 PDB 2V0A "Atomic Resolution Crystal Structure Of Human Superoxide Dismutase" 100.00 153 100.00 100.00 2.26e-83 PDB 2VR6 "Crystal Structure Of G85r Als Mutant Of Human Cu,Zn Superoxide Dismutase (Cuznsod) At 1.3 A Resolution" 100.00 153 99.20 99.20 2.97e-82 PDB 2VR7 "Crystal Structure Of G85r Als Mutant Of Human Cu,Zn Superoxide Dismutase (Cuznsod) At 1.58 A Resolution" 100.00 154 99.20 99.20 3.06e-82 PDB 2VR8 "Crystal Structure Of G85r Als Mutant Of Human Cu,Zn Superoxide Dismutase (Cuznsod) At 1.36 A Resolution" 100.00 154 98.40 98.40 9.73e-81 PDB 2WKO "Structure Of Metal Loaded Pathogenic Sod1 Mutant G93a" 100.00 154 99.20 99.20 1.17e-82 PDB 2WYT "1.0 A Resolution Structure Of L38v Sod1 Mutant" 100.00 153 99.20 100.00 7.67e-83 PDB 2WYZ "L38v Sod1 Mutant Complexed With Ump" 100.00 153 98.40 99.20 2.38e-81 PDB 2WZ0 "L38v Sod1 Mutant Complexed With Aniline." 100.00 153 99.20 100.00 7.67e-83 PDB 2WZ5 "L38v Sod1 Mutant Complexed With L-Methionine" 100.00 153 99.20 100.00 7.67e-83 PDB 2WZ6 "G93a Sod1 Mutant Complexed With Quinazoline" 100.00 153 99.20 99.20 1.14e-82 PDB 2ZKW "Crystal Structure Of Human Cu-Zn Superoxide Dismutase Mutant G85r In Space Group P21" 100.00 159 99.20 99.20 3.42e-82 PDB 2ZKX "Crystal Structure Of Human Cu-Zn Superoxide Dismutase Mutant G85r In Space Group I212121" 100.00 159 99.20 99.20 3.42e-82 PDB 2ZKY "Crystal Structure Of Human Cu-Zn Superoxide Dismutase Mutant G93a" 100.00 159 99.20 99.20 1.24e-82 PDB 3CQP "Human Sod1 G85r Variant, Structure I" 100.00 153 99.20 99.20 2.97e-82 PDB 3CQQ "Human Sod1 G85r Variant, Structure Ii" 100.00 153 98.40 98.40 9.42e-81 PDB 3ECU "Crystal Structure Of Human Apo Cu,Zn Superoxide Dismutase (Sod1)" 100.00 153 100.00 100.00 2.26e-83 PDB 3ECV "Crystal Structure Of The Als-Related Pathological Mutant I113t Of Human Apo Cu,Zn Superoxide Dismutase (Sod1)" 100.00 153 99.20 99.20 1.09e-82 PDB 3ECW "Crystal Structure Of The Als-Related Pathological Mutant T54r Of Human Apo Cu,Zn Superoxide Dismutase (Sod1)" 100.00 153 99.20 99.20 2.14e-82 PDB 3GQF "Structural And Biophysical Properties Of The Pathogenic Sod1 Variant H46rH48Q" 100.00 153 98.40 98.40 9.03e-82 PDB 3GZO "Human Sod1 G93a Variant" 100.00 154 99.20 99.20 1.17e-82 PDB 3GZP "Human Sod1 G93a Metal-Free Variant" 100.00 153 99.20 99.20 1.14e-82 PDB 3GZQ "Human Sod1 A4v Metal-Free Variant" 100.00 154 99.20 99.20 1.35e-82 PDB 3H2P "Human Sod1 D124v Variant" 100.00 153 99.20 99.20 4.39e-82 PDB 3H2Q "Human Sod1 H80r Variant, P21 Crystal Form" 100.00 153 99.20 99.20 1.76e-82 PDB 3K91 "Polysulfane Bridge In Cu-Zn Superoxide Dismutase" 100.00 153 98.40 98.40 9.03e-82 PDB 3KH3 "Crystal Structure Of Human CuZN SUPEROXIDE DISMUTASE RECOMBINANTLY Produced In Leishmania Tarantolae; P212121 Crystal Form Cont" 100.00 153 100.00 100.00 2.26e-83 PDB 3KH4 "Crystal Structure Of Human CuZN SUPEROXIDE DISMUTASE RECOMBINANTLY Produced In Leishmania Tarantolae; P6522 Crystal Form Contai" 100.00 153 100.00 100.00 2.26e-83 PDB 3QQD "Human Sod1 H80r Variant, P212121 Crystal Form" 100.00 154 98.40 98.40 5.06e-81 PDB 3RE0 "Crystal Structure Of Human Apo Cu,zn Superoxide Dismutase (sod1) Complexed With Cisplatin" 100.00 153 100.00 100.00 2.26e-83 PDB 3T5W "2me Modified Human Sod1" 100.00 153 99.20 99.20 6.95e-82 PDB 4A7G "Structure Of Human I113t Sod1 Mutant Complexed With 4- Methylpiperazin-1-yl)quinazoline In The P21 Space Group." 100.00 153 99.20 99.20 1.09e-82 PDB 4A7Q "Structure Of Human I113t Sod1 Mutant Complexed With 4-(4- Methyl-1,4-diazepan-1-yl)quinazoline In The P21 Space Group." 100.00 153 99.20 99.20 1.09e-82 PDB 4A7S "Structure Of Human I113t Sod1 Mutant Complexed With 5- Fluorouridine In The P21 Space Group" 100.00 153 99.20 99.20 1.09e-82 PDB 4A7T "Structure Of Human I113t Sod1 Mutant Complexed With Isoproteranol In The P21 Space Group" 100.00 153 99.20 99.20 1.09e-82 PDB 4A7U "Structure Of Human I113t Sod1 Complexed With Adrenaline In The P21 Space Group." 100.00 153 99.20 99.20 1.09e-82 PDB 4A7V "Structure Of Human I113t Sod1 Mutant Complexed With Dopamine In The P21 Space Group" 100.00 153 99.20 99.20 1.09e-82 PDB 4B3E "Structure Of Copper-Zinc Superoxide Dismutase Complexed With Bicarbonate." 100.00 154 100.00 100.00 1.84e-83 PDB 4FF9 "Crystal Structure Of Cysteinylated Wt Sod1" 100.00 153 100.00 100.00 2.26e-83 PDB 4MCM "Human Sod1 C57s Mutant, As-isolated" 100.00 153 99.20 99.20 4.34e-82 PDB 4MCN "Human Sod1 C57s Mutant, Metal-free" 100.00 153 99.20 99.20 4.34e-82 PDB 4OH2 "Crystal Structure Of Cu/zn Superoxide Dismutase I149t" 100.00 153 98.40 98.40 3.53e-81 DBJ BAA14373 "unnamed protein product [Schizosaccharomyces pombe]" 100.00 179 100.00 100.00 3.62e-83 DBJ BAC20345 "Cu,Zn-superoxide dismutase [Pan troglodytes]" 100.00 154 100.00 100.00 1.84e-83 DBJ BAG35052 "unnamed protein product [Homo sapiens]" 100.00 154 100.00 100.00 1.84e-83 DBJ BAG73767 "superoxide dismutase 1, soluble [synthetic construct]" 100.00 154 100.00 100.00 1.84e-83 EMBL CAA26182 "unnamed protein product [Homo sapiens]" 100.00 154 100.00 100.00 1.84e-83 EMBL CAG29351 "SOD1 [Homo sapiens]" 100.00 154 100.00 100.00 1.84e-83 EMBL CAG46542 "SOD1 [Homo sapiens]" 100.00 154 100.00 100.00 1.84e-83 GB AAA72747 "CuZn superoxide dismutase [synthetic construct]" 100.00 154 98.40 98.40 3.94e-81 GB AAA80237 "HSOD-GlyProGly-A+, partial [synthetic construct]" 100.00 171 98.40 98.40 1.51e-80 GB AAB05661 "Cu/Zn-superoxide dismutase [Homo sapiens]" 100.00 154 100.00 100.00 1.84e-83 GB AAB05662 "Cu/Zn-superoxide dismutase [Homo sapiens]" 100.00 154 99.20 99.20 2.09e-82 GB AAB27818 "Cu,Zn superoxide dismutase, SOD=SOD1 gene product {A to V single-site mutation} [human, Peptide Mutant, 153 aa]" 100.00 153 99.20 99.20 1.31e-82 REF NP_000445 "superoxide dismutase [Cu-Zn] [Homo sapiens]" 100.00 154 100.00 100.00 1.84e-83 REF NP_001009025 "superoxide dismutase [Cu-Zn] [Pan troglodytes]" 100.00 154 100.00 100.00 1.84e-83 REF XP_003813274 "PREDICTED: superoxide dismutase [Cu-Zn] [Pan paniscus]" 100.00 154 100.00 100.00 1.84e-83 REF XP_004062735 "PREDICTED: superoxide dismutase [Cu-Zn] [Gorilla gorilla gorilla]" 100.00 154 99.20 99.20 2.49e-82 REF XP_004062736 "PREDICTED: superoxide dismutase [Cu-Zn] [Gorilla gorilla gorilla]" 100.00 154 99.20 99.20 2.49e-82 SP P00441 "RecName: Full=Superoxide dismutase [Cu-Zn]; AltName: Full=Superoxide dismutase 1; Short=hSod1" 100.00 154 100.00 100.00 1.84e-83 SP P60052 "RecName: Full=Superoxide dismutase [Cu-Zn]" 100.00 154 100.00 100.00 1.84e-83 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $L126Z-sod1 'E. coli' 562 Bacteria . Escherichia coli 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 $L126Z-sod1 'recombinant technology' . Escherichia coli 'BL21 (DE3)' pET28a 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 $L126Z-sod1 400 uM '[U-100% 13C; U-100% 15N]' 'dodecylphosphocholine (DPC)' 20 mM 'natural abundance' H2O 90 % 'natural abundance' D2O 10 % '[U-100% 2H]' stop_ save_ ############################ # Computer software used # ############################ save_Cyana _Saveframe_category software _Name Cyana _Version 2.1 loop_ _Vendor _Address _Electronic_address 'Guntert, Mumenthaler and Wuthrich' . . stop_ loop_ _Task 'structure solution' stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model Avance _Field_strength 800 _Details . save_ ############################# # NMR applied experiments # ############################# save_3D_CBCA(CO)NH_1 _Saveframe_category NMR_applied_experiment _Experiment_name '3D CBCA(CO)NH' _Sample_label $sample_1 save_ save_3D_HNCACB_2 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCACB' _Sample_label $sample_1 save_ save_3D_1H-15N_NOESY_3 _Saveframe_category NMR_applied_experiment _Experiment_name '3D 1H-15N NOESY' _Sample_label $sample_1 save_ save_3D_1H-15N_TOCSY_4 _Saveframe_category NMR_applied_experiment _Experiment_name '3D 1H-15N TOCSY' _Sample_label $sample_1 save_ ####################### # Sample conditions # ####################### save_sample_conditions_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 4 . pH pressure 1 . atm temperature 313 . 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 DSS H 1 'methyl protons' ppm 0.00 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 '3D CBCA(CO)NH' '3D HNCACB' '3D 1H-15N NOESY' '3D 1H-15N TOCSY' stop_ loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $sample_conditions_1 _Chem_shift_reference_set_label $chemical_shift_reference_1 _Mol_system_component_name 'Truncated L126Z-sod1' _Text_data_format . _Text_data . loop_ _Atom_shift_assign_ID _Residue_author_seq_code _Residue_seq_code _Residue_label _Atom_name _Atom_type _Chem_shift_value _Chem_shift_value_error _Chem_shift_ambiguity_code 1 1 1 ALA HA H 4.361 0.00 1 2 1 1 ALA H H 8.510 0.00 1 3 1 1 ALA CA C 52.648 0.00 1 4 1 1 ALA CB C 19.448 0.00 1 5 1 1 ALA N N 126.197 0.00 1 6 2 2 THR H H 8.114 0.00 1 7 2 2 THR HA H 4.279 0.00 1 8 2 2 THR CA C 62.284 0.00 1 9 2 2 THR CB C 69.857 0.00 1 10 2 2 THR N N 114.102 0.00 1 11 3 3 LYS H H 8.244 0.00 1 12 3 3 LYS HA H 4.281 0.00 1 13 3 3 LYS CA C 56.818 0.00 1 14 3 3 LYS CB C 33.007 0.00 1 15 3 3 LYS N N 123.285 0.00 1 16 4 4 ALA H H 8.043 0.00 1 17 4 4 ALA HA H 4.282 0.00 1 18 4 4 ALA CA C 52.906 0.00 1 19 4 4 ALA CB C 19.274 0.00 1 20 4 4 ALA N N 123.571 0.00 1 21 5 5 VAL H H 7.954 0.00 1 22 5 5 VAL HA H 4.005 0.00 1 23 5 5 VAL CA C 63.247 0.00 1 24 5 5 VAL CB C 32.563 0.00 1 25 5 5 VAL N N 117.713 0.00 1 26 6 6 CYS H H 8.159 0.00 1 27 6 6 CYS HA H 4.607 0.00 1 28 6 6 CYS CA C 59.415 0.00 1 29 6 6 CYS CB C 27.718 0.00 1 30 6 6 CYS N N 121.534 0.00 1 31 7 7 VAL H H 8.051 0.00 1 32 7 7 VAL HA H 4.264 0.00 1 33 7 7 VAL CA C 63.142 0.00 1 34 7 7 VAL CB C 32.454 0.00 1 35 7 7 VAL N N 121.442 0.00 1 36 8 8 LEU H H 8.028 0.00 1 37 8 8 LEU CA C 55.503 0.00 1 38 8 8 LEU CB C 42.320 0.00 1 39 8 8 LEU N N 122.905 0.00 1 40 9 9 LYS H H 8.005 0.00 1 41 9 9 LYS HA H 4.239 0.00 1 42 9 9 LYS CA C 56.817 0.00 1 43 9 9 LYS CB C 33.156 0.00 1 44 9 9 LYS N N 120.185 0.00 1 45 10 10 GLY H H 8.492 0.00 1 46 10 10 GLY HA2 H 3.829 0.00 1 47 10 10 GLY HA3 H 3.829 0.00 1 48 10 10 GLY CA C 45.474 0.00 1 49 10 10 GLY N N 108.482 0.00 1 50 11 11 ASP H H 8.177 0.00 1 51 11 11 ASP HA H 4.759 0.00 1 52 11 11 ASP CA C 53.202 0.00 1 53 11 11 ASP CB C 38.839 0.00 1 54 11 11 ASP N N 118.480 0.00 1 55 12 12 GLY H H 8.397 0.00 1 56 12 12 GLY HA2 H 4.125 0.00 1 57 12 12 GLY HA3 H 4.125 0.00 1 58 12 12 GLY CA C 46.143 0.00 1 59 12 12 GLY N N 109.077 0.00 1 60 13 13 PRO HA H 4.423 0.00 1 61 13 13 PRO CA C 64.749 0.00 1 62 13 13 PRO CB C 32.213 0.00 1 63 14 14 VAL H H 7.931 0.00 1 64 14 14 VAL HA H 3.763 0.00 1 65 14 14 VAL CA C 65.607 0.00 1 66 14 14 VAL CB C 31.548 0.00 1 67 14 14 VAL N N 116.976 0.00 1 68 15 15 GLN H H 8.184 0.00 1 69 15 15 GLN HA H 4.002 0.00 1 70 15 15 GLN CA C 58.533 0.00 1 71 15 15 GLN CB C 28.387 0.00 1 72 15 15 GLN N N 120.074 0.00 1 73 16 16 GLY H H 8.270 0.00 1 74 16 16 GLY HA2 H 3.903 0.00 1 75 16 16 GLY HA3 H 3.903 0.00 1 76 16 16 GLY CA C 46.945 0.00 1 77 16 16 GLY N N 127.937 0.00 1 78 17 17 ILE H H 7.934 0.00 1 79 17 17 ILE HA H 3.890 0.00 1 80 17 17 ILE CA C 64.622 0.00 1 81 17 17 ILE CB C 38.072 0.00 1 82 17 17 ILE N N 121.982 0.00 1 83 18 18 ILE H H 8.007 0.00 1 84 18 18 ILE HA H 3.763 0.00 1 85 18 18 ILE CA C 64.717 0.00 1 86 18 18 ILE CB C 37.833 0.00 1 87 18 18 ILE N N 120.869 0.00 1 88 19 19 ASN H H 8.388 0.00 1 89 19 19 ASN HA H 4.485 0.00 1 90 19 19 ASN CA C 55.719 0.00 1 91 19 19 ASN CB C 38.405 0.00 1 92 19 19 ASN N N 118.523 0.00 1 93 20 20 PHE H H 8.049 0.00 1 94 20 20 PHE HA H 4.306 0.00 1 95 20 20 PHE CA C 61.018 0.00 1 96 20 20 PHE CB C 39.469 0.00 1 97 20 20 PHE N N 120.599 0.00 1 98 21 21 GLU H H 8.415 0.00 1 99 21 21 GLU HA H 3.865 0.00 1 100 21 21 GLU CA C 58.894 0.00 1 101 21 21 GLU CB C 27.778 0.00 1 102 21 21 GLU N N 118.658 0.00 1 103 22 22 GLN H H 8.174 0.00 1 104 22 22 GLN HA H 4.018 0.00 1 105 22 22 GLN CA C 58.017 0.00 1 106 22 22 GLN CB C 29.013 0.00 1 107 22 22 GLN N N 117.512 0.00 1 108 23 23 LYS H H 7.752 0.00 1 109 23 23 LYS HA H 4.189 0.00 1 110 23 23 LYS CA C 57.620 0.00 1 111 23 23 LYS CB C 32.803 0.00 1 112 23 23 LYS N N 118.902 0.00 1 113 24 24 GLU H H 7.816 0.00 1 114 24 24 GLU HA H 4.263 0.00 1 115 24 24 GLU CA C 56.058 0.00 1 116 24 24 GLU CB C 28.542 0.00 1 117 24 24 GLU N N 117.945 0.00 1 118 25 25 SER H H 7.923 0.00 1 119 25 25 SER HA H 4.291 0.00 1 120 25 25 SER CA C 59.316 0.00 1 121 25 25 SER CB C 63.793 0.00 1 122 25 25 SER N N 114.711 0.00 1 123 26 26 ASN H H 8.122 0.00 1 124 26 26 ASN HA H 4.776 0.00 1 125 26 26 ASN CA C 53.446 0.00 1 126 26 26 ASN CB C 39.173 0.00 1 127 26 26 ASN N N 119.305 0.00 1 128 27 27 GLY H H 8.073 0.00 1 129 27 27 GLY HA2 H 4.072 0.00 1 130 27 27 GLY HA3 H 4.072 0.00 1 131 27 27 GLY CA C 45.810 0.00 1 132 27 27 GLY N N 108.196 0.00 1 133 28 28 PRO HA H 4.260 0.00 1 134 28 28 PRO CA C 63.997 0.00 1 135 28 28 PRO CB C 32.294 0.00 1 136 29 29 VAL H H 7.891 0.00 1 137 29 29 VAL HA H 3.956 0.00 1 138 29 29 VAL CA C 63.818 0.00 1 139 29 29 VAL CB C 32.351 0.00 1 140 29 29 VAL N N 120.509 0.00 1 141 30 30 LYS H H 8.276 0.00 1 142 30 30 LYS HA H 4.317 0.00 1 143 30 30 LYS CA C 57.432 0.00 1 144 30 30 LYS CB C 32.414 0.00 1 145 30 30 LYS N N 123.745 0.00 1 146 31 31 VAL H H 8.090 0.00 1 147 31 31 VAL HA H 3.877 0.00 1 148 31 31 VAL CA C 64.946 0.00 1 149 31 31 VAL CB C 32.163 0.00 1 150 31 31 VAL N N 119.301 0.00 1 151 32 32 TRP H H 8.123 0.00 1 152 32 32 TRP HA H 4.557 0.00 1 153 32 32 TRP CA C 59.291 0.00 1 154 32 32 TRP CB C 29.861 0.00 1 155 32 32 TRP N N 121.167 0.00 1 156 33 33 GLY H H 8.230 0.00 1 157 33 33 GLY HA2 H 3.840 0.00 1 158 33 33 GLY HA3 H 3.840 0.00 1 159 33 33 GLY CA C 46.948 0.00 1 160 33 33 GLY N N 126.289 0.00 1 161 34 34 SER H H 7.842 0.00 1 162 34 34 SER HA H 4.420 0.00 1 163 34 34 SER CA C 60.973 0.00 1 164 34 34 SER CB C 63.594 0.00 1 165 34 34 SER N N 116.831 0.00 1 166 35 35 ILE H H 7.962 0.00 1 167 35 35 ILE HA H 3.848 0.00 1 168 35 35 ILE CA C 63.911 0.00 1 169 35 35 ILE CB C 37.785 0.00 1 170 35 35 ILE N N 120.855 0.00 1 171 36 36 LYS CA C 59.341 0.00 1 172 36 36 LYS CB C 31.799 0.00 1 173 37 37 GLY H H 8.067 0.00 1 174 37 37 GLY HA2 H 3.858 0.00 1 175 37 37 GLY HA3 H 3.858 0.00 1 176 37 37 GLY CA C 46.624 0.00 1 177 37 37 GLY N N 127.648 0.00 1 178 38 38 LEU H H 7.838 0.00 1 179 38 38 LEU HA H 4.192 0.00 1 180 38 38 LEU CA C 57.365 0.00 1 181 38 38 LEU CB C 42.553 0.00 1 182 38 38 LEU N N 121.080 0.00 1 183 39 39 THR H H 7.887 0.00 1 184 39 39 THR HA H 4.286 0.00 1 185 39 39 THR CA C 64.464 0.00 1 186 39 39 THR CB C 69.053 0.00 1 187 39 39 THR N N 108.219 0.00 1 188 40 40 GLU H H 7.793 0.00 1 189 40 40 GLU HA H 4.187 0.00 1 190 40 40 GLU CA C 57.782 0.00 1 191 40 40 GLU CB C 28.112 0.00 1 192 40 40 GLU N N 120.404 0.00 1 193 41 41 GLY H H 8.117 0.00 1 194 41 41 GLY HA2 H 3.913 0.00 1 195 41 41 GLY HA3 H 3.913 0.00 1 196 41 41 GLY CA C 45.809 0.00 1 197 41 41 GLY N N 107.101 0.00 1 198 42 42 LEU H H 7.718 0.00 1 199 42 42 LEU HA H 4.262 0.00 1 200 42 42 LEU CA C 55.684 0.00 1 201 42 42 LEU CB C 42.060 0.00 1 202 42 42 LEU N N 119.986 0.00 1 203 43 43 HIS H H 8.142 0.00 1 204 43 43 HIS HA H 4.574 0.00 1 205 43 43 HIS CA C 56.492 0.00 1 206 43 43 HIS CB C 28.656 0.00 1 207 43 43 HIS N N 116.877 0.00 1 208 44 44 GLY H H 8.381 0.00 1 209 44 44 GLY HA2 H 3.850 0.00 1 210 44 44 GLY HA3 H 3.850 0.00 1 211 44 44 GLY CA C 45.566 0.00 1 212 44 44 GLY N N 108.027 0.00 1 213 45 45 PHE H H 7.799 0.00 1 214 45 45 PHE HA H 4.495 0.00 1 215 45 45 PHE CA C 58.237 0.00 1 216 45 45 PHE CB C 39.916 0.00 1 217 45 45 PHE N N 119.781 0.00 1 218 46 46 HIS H H 8.203 0.00 1 219 46 46 HIS HA H 4.611 0.00 1 220 46 46 HIS CA C 55.147 0.00 1 221 46 46 HIS CB C 29.233 0.00 1 222 46 46 HIS N N 119.576 0.00 1 223 47 47 VAL H H 8.178 0.00 1 224 47 47 VAL CA C 62.976 0.00 1 225 47 47 VAL CB C 32.303 0.00 1 226 47 47 VAL N N 120.726 0.00 1 227 48 48 HIS H H 8.439 0.00 1 228 48 48 HIS HA H 4.652 0.00 1 229 48 48 HIS CA C 55.094 0.00 1 230 48 48 HIS CB C 29.017 0.00 1 231 48 48 HIS N N 118.055 0.00 1 232 49 49 GLU H H 8.173 0.00 1 233 49 49 GLU HA H 4.358 0.00 1 234 49 49 GLU CA C 56.408 0.00 1 235 49 49 GLU CB C 28.978 0.00 1 236 49 49 GLU N N 119.231 0.00 1 237 50 50 PHE H H 8.045 0.00 1 238 50 50 PHE HA H 4.616 0.00 1 239 50 50 PHE CA C 57.761 0.00 1 240 50 50 PHE CB C 39.663 0.00 1 241 50 50 PHE N N 119.140 0.00 1 242 51 51 GLY H H 8.242 0.00 1 243 51 51 GLY HA2 H 3.929 0.00 1 244 51 51 GLY HA3 H 3.929 0.00 1 245 51 51 GLY CA C 45.456 0.00 1 246 51 51 GLY N N 108.952 0.00 1 247 52 52 ASP H H 8.251 0.00 1 248 52 52 ASP HA H 4.682 0.00 1 249 52 52 ASP CA C 53.572 0.00 1 250 52 52 ASP CB C 38.813 0.00 1 251 52 52 ASP N N 119.033 0.00 1 252 53 53 ASN H H 7.918 0.00 1 253 53 53 ASN HA H 4.618 0.00 1 254 53 53 ASN CA C 52.912 0.00 1 255 53 53 ASN CB C 38.973 0.00 1 256 53 53 ASN N N 120.466 0.00 1 257 54 54 THR H H 8.026 0.00 1 258 54 54 THR HA H 4.274 0.00 1 259 54 54 THR CA C 62.121 0.00 1 260 54 54 THR CB C 69.696 0.00 1 261 54 54 THR N N 113.893 0.00 1 262 55 55 ALA H H 8.176 0.00 1 263 55 55 ALA HA H 4.384 0.00 1 264 55 55 ALA CA C 52.655 0.00 1 265 55 55 ALA CB C 19.478 0.00 1 266 55 55 ALA N N 125.777 0.00 1 267 56 56 GLY H H 8.048 0.00 1 268 56 56 GLY HA2 H 4.049 0.00 1 269 56 56 GLY HA3 H 4.049 0.00 1 270 56 56 GLY CA C 44.634 0.00 1 271 56 56 GLY N N 107.810 0.00 1 272 57 57 CYS H H 8.122 0.00 1 273 57 57 CYS HA H 4.574 0.00 1 274 57 57 CYS CA C 58.627 0.00 1 275 57 57 CYS CB C 28.122 0.00 1 276 57 57 CYS N N 118.586 0.00 1 277 58 58 THR H H 8.201 0.00 1 278 58 58 THR HA H 4.382 0.00 1 279 58 58 THR CA C 62.006 0.00 1 280 58 58 THR CB C 69.822 0.00 1 281 58 58 THR N N 116.035 0.00 1 282 59 59 SER H H 8.173 0.00 1 283 59 59 SER HA H 4.425 0.00 1 284 59 59 SER CA C 58.376 0.00 1 285 59 59 SER CB C 63.969 0.00 1 286 59 59 SER N N 117.834 0.00 1 287 60 60 ALA H H 8.201 0.00 1 288 60 60 ALA HA H 4.360 0.00 1 289 60 60 ALA CA C 52.534 0.00 1 290 60 60 ALA CB C 19.583 0.00 1 291 60 60 ALA N N 125.777 0.00 1 292 61 61 GLY H H 7.958 0.00 1 293 61 61 GLY HA2 H 3.825 0.00 1 294 61 61 GLY HA3 H 3.825 0.00 1 295 61 61 GLY CA C 43.747 0.00 1 296 61 61 GLY N N 107.119 0.00 1 297 62 62 PRO HA H 4.452 0.00 1 298 62 62 PRO CA C 62.358 0.00 1 299 62 62 PRO CB C 32.638 0.00 1 300 63 63 HIS H H 8.642 0.00 1 301 63 63 HIS HA H 4.756 0.00 1 302 63 63 HIS CA C 54.997 0.00 1 303 63 63 HIS CB C 29.147 0.00 1 304 63 63 HIS N N 118.969 0.00 1 305 64 64 PHE H H 8.318 0.00 1 306 64 64 PHE HA H 4.597 0.00 1 307 64 64 PHE CA C 57.508 0.00 1 308 64 64 PHE CB C 40.011 0.00 1 309 64 64 PHE N N 121.743 0.00 1 310 65 65 ASN H H 8.314 0.00 1 311 65 65 ASN HA H 4.894 0.00 1 312 65 65 ASN CA C 50.669 0.00 1 313 65 65 ASN CB C 39.177 0.00 1 314 65 65 ASN N N 122.466 0.00 1 315 66 66 PRO CA C 63.748 0.00 1 316 66 66 PRO CB C 32.145 0.00 1 317 67 67 LEU H H 7.997 0.00 1 318 67 67 LEU HA H 4.273 0.00 1 319 67 67 LEU CA C 55.411 0.00 1 320 67 67 LEU CB C 41.729 0.00 1 321 67 67 LEU N N 119.364 0.00 1 322 68 68 SER H H 7.814 0.00 1 323 68 68 SER HA H 4.337 0.00 1 324 68 68 SER CA C 58.658 0.00 1 325 68 68 SER CB C 63.815 0.00 1 326 68 68 SER N N 115.077 0.00 1 327 69 69 ARG H H 8.043 0.00 1 328 69 69 ARG HA H 4.328 0.00 1 329 69 69 ARG CA C 56.056 0.00 1 330 69 69 ARG CB C 30.750 0.00 1 331 69 69 ARG N N 122.421 0.00 1 332 70 70 LYS H H 8.086 0.00 1 333 70 70 LYS HA H 4.238 0.00 1 334 70 70 LYS CA C 56.513 0.00 1 335 70 70 LYS CB C 33.011 0.00 1 336 70 70 LYS N N 121.683 0.00 1 337 71 71 HIS H H 8.410 0.00 1 338 71 71 HIS HA H 4.734 0.00 1 339 71 71 HIS CA C 55.212 0.00 1 340 71 71 HIS CB C 29.332 0.00 1 341 71 71 HIS N N 119.321 0.00 1 342 72 72 GLY H H 8.368 0.00 1 343 72 72 GLY HA2 H 4.014 0.00 1 344 72 72 GLY HA3 H 4.014 0.00 1 345 72 72 GLY CA C 45.117 0.00 1 346 72 72 GLY N N 110.453 0.00 1 347 73 73 GLY H H 8.149 0.00 1 348 73 73 GLY HA2 H 4.102 0.00 1 349 73 73 GLY HA3 H 4.102 0.00 1 350 73 73 GLY CA C 44.617 0.00 1 351 73 73 GLY N N 108.744 0.00 1 352 74 74 PRO HA H 4.404 0.00 1 353 74 74 PRO CA C 63.408 0.00 1 354 74 74 PRO CB C 32.193 0.00 1 355 75 75 LYS H H 8.351 0.00 1 356 75 75 LYS HA H 4.237 0.00 1 357 75 75 LYS CA C 56.722 0.00 1 358 75 75 LYS CB C 32.833 0.00 1 359 75 75 LYS N N 120.609 0.00 1 360 76 76 ASP H H 8.223 0.00 1 361 76 76 ASP HA H 4.624 0.00 1 362 76 76 ASP CA C 53.584 0.00 1 363 76 76 ASP CB C 39.083 0.00 1 364 76 76 ASP N N 119.583 0.00 1 365 77 77 GLU H H 8.279 0.00 1 366 77 77 GLU HA H 4.332 0.00 1 367 77 77 GLU CA C 56.224 0.00 1 368 77 77 GLU CB C 28.978 0.00 1 369 77 77 GLU N N 120.900 0.00 1 370 78 78 GLU H H 8.244 0.00 1 371 78 78 GLU HA H 4.268 0.00 1 372 78 78 GLU CA C 56.613 0.00 1 373 78 78 GLU CB C 28.913 0.00 1 374 78 78 GLU N N 120.207 0.00 1 375 79 79 ARG H H 8.129 0.00 1 376 79 79 ARG HA H 4.260 0.00 1 377 79 79 ARG CA C 56.185 0.00 1 378 79 79 ARG CB C 30.924 0.00 1 379 79 79 ARG N N 121.243 0.00 1 380 80 80 HIS H H 8.449 0.00 1 381 80 80 HIS HA H 4.739 0.00 1 382 80 80 HIS CA C 55.407 0.00 1 383 80 80 HIS CB C 29.241 0.00 1 384 80 80 HIS N N 119.446 0.00 1 385 81 81 VAL H H 8.170 0.00 1 386 81 81 VAL HA H 3.953 0.00 1 387 81 81 VAL CA C 62.886 0.00 1 388 81 81 VAL CB C 32.615 0.00 1 389 81 81 VAL N N 119.297 0.00 1 390 82 82 GLY H H 8.372 0.00 1 391 82 82 GLY HA2 H 4.012 0.00 1 392 82 82 GLY HA3 H 4.012 0.00 1 393 82 82 GLY CA C 45.465 0.00 1 394 82 82 GLY N N 111.075 0.00 1 395 83 83 ASP H H 8.230 0.00 1 396 83 83 ASP HA H 4.679 0.00 1 397 83 83 ASP CA C 53.309 0.00 1 398 83 83 ASP CB C 38.782 0.00 1 399 83 83 ASP N N 118.677 0.00 1 400 84 84 LEU H H 8.231 0.00 1 401 84 84 LEU HA H 4.268 0.00 1 402 84 84 LEU CA C 55.890 0.00 1 403 84 84 LEU CB C 42.175 0.00 1 404 84 84 LEU N N 121.711 0.00 1 405 85 85 GLY H H 8.215 0.00 1 406 85 85 GLY HA2 H 3.917 0.00 1 407 85 85 GLY HA3 H 3.917 0.00 1 408 85 85 GLY CA C 45.796 0.00 1 409 85 85 GLY N N 107.521 0.00 1 410 86 86 ASN H H 8.140 0.00 1 411 86 86 ASN HA H 4.727 0.00 1 412 86 86 ASN CA C 53.368 0.00 1 413 86 86 ASN CB C 38.795 0.00 1 414 86 86 ASN N N 118.522 0.00 1 415 87 87 VAL H H 7.977 0.00 1 416 87 87 VAL HA H 4.110 0.00 1 417 87 87 VAL CA C 63.404 0.00 1 418 87 87 VAL CB C 32.401 0.00 1 419 87 87 VAL N N 119.653 0.00 1 420 88 88 THR H H 7.996 0.00 1 421 88 88 THR HA H 4.302 0.00 1 422 88 88 THR CA C 62.737 0.00 1 423 88 88 THR CB C 69.424 0.00 1 424 88 88 THR N N 115.427 0.00 1 425 89 89 ALA H H 8.005 0.00 1 426 89 89 ALA HA H 4.281 0.00 1 427 89 89 ALA CA C 52.992 0.00 1 428 89 89 ALA CB C 19.151 0.00 1 429 89 89 ALA N N 125.054 0.00 1 430 90 90 ASP H H 8.173 0.00 1 431 90 90 ASP HA H 4.625 0.00 1 432 90 90 ASP CA C 53.478 0.00 1 433 90 90 ASP CB C 38.348 0.00 1 434 90 90 ASP N N 117.513 0.00 1 435 91 91 LYS H H 8.147 0.00 1 436 91 91 LYS HA H 4.226 0.00 1 437 91 91 LYS CA C 57.168 0.00 1 438 91 91 LYS CB C 32.670 0.00 1 439 91 91 LYS N N 120.988 0.00 1 440 92 92 ASP H H 8.279 0.00 1 441 92 92 ASP HA H 4.646 0.00 1 442 92 92 ASP CA C 53.659 0.00 1 443 92 92 ASP CB C 38.425 0.00 1 444 92 92 ASP N N 118.400 0.00 1 445 93 93 GLY H H 8.133 0.00 1 446 93 93 GLY HA2 H 3.946 0.00 1 447 93 93 GLY HA3 H 3.946 0.00 1 448 93 93 GLY CA C 45.880 0.00 1 449 93 93 GLY N N 107.991 0.00 1 450 94 94 VAL H H 7.840 0.00 1 451 94 94 VAL HA H 4.061 0.00 1 452 94 94 VAL CA C 62.865 0.00 1 453 94 94 VAL CB C 32.529 0.00 1 454 94 94 VAL N N 118.556 0.00 1 455 95 95 ALA H H 8.190 0.00 1 456 95 95 ALA HA H 4.308 0.00 1 457 95 95 ALA CA C 52.890 0.00 1 458 95 95 ALA CB C 19.276 0.00 1 459 95 95 ALA N N 125.410 0.00 1 460 96 96 ASP H H 8.253 0.00 1 461 96 96 ASP HA H 4.614 0.00 1 462 96 96 ASP CA C 54.145 0.00 1 463 96 96 ASP CB C 38.193 0.00 1 464 96 96 ASP N N 117.528 0.00 1 465 97 97 VAL H H 7.935 0.00 1 466 97 97 VAL HA H 4.048 0.00 1 467 97 97 VAL CA C 63.455 0.00 1 468 97 97 VAL CB C 32.564 0.00 1 469 97 97 VAL N N 119.362 0.00 1 470 98 98 SER H H 8.103 0.00 1 471 98 98 SER HA H 4.530 0.00 1 472 98 98 SER CA C 59.185 0.00 1 473 98 98 SER CB C 63.579 0.00 1 474 98 98 SER N N 117.866 0.00 1 475 99 99 ILE H H 8.395 0.00 1 476 99 99 ILE HA H 3.917 0.00 1 477 99 99 ILE CA C 64.000 0.00 1 478 99 99 ILE CB C 38.001 0.00 1 479 99 99 ILE N N 123.797 0.00 1 480 100 100 GLU H H 8.433 0.00 1 481 100 100 GLU HA H 4.251 0.00 1 482 100 100 GLU CA C 59.247 0.00 1 483 100 100 GLU CB C 28.160 0.00 1 484 100 100 GLU N N 120.053 0.00 1 485 101 101 ASP H H 8.339 0.00 1 486 101 101 ASP HA H 4.497 0.00 1 487 101 101 ASP CA C 55.395 0.00 1 488 101 101 ASP CB C 37.691 0.00 1 489 101 101 ASP N N 116.680 0.00 1 490 102 102 SER H H 7.999 0.00 1 491 102 102 SER HA H 4.335 0.00 1 492 102 102 SER CA C 61.843 0.00 1 493 102 102 SER CB C 63.396 0.00 1 494 102 102 SER N N 116.686 0.00 1 495 103 103 VAL H H 8.004 0.00 1 496 103 103 VAL HA H 3.816 0.00 1 497 103 103 VAL CA C 65.719 0.00 1 498 103 103 VAL CB C 31.920 0.00 1 499 103 103 VAL N N 120.346 0.00 1 500 104 104 ILE H H 8.009 0.00 1 501 104 104 ILE HA H 3.890 0.00 1 502 104 104 ILE CA C 63.862 0.00 1 503 104 104 ILE CB C 38.048 0.00 1 504 104 104 ILE N N 119.732 0.00 1 505 105 105 SER H H 7.995 0.00 1 506 105 105 SER HA H 4.501 0.00 1 507 105 105 SER CA C 60.533 0.00 1 508 105 105 SER CB C 63.459 0.00 1 509 105 105 SER N N 116.660 0.00 1 510 106 106 LEU H H 8.053 0.00 1 511 106 106 LEU CA C 56.562 0.00 1 512 106 106 LEU CB C 42.454 0.00 1 513 106 106 LEU N N 122.130 0.00 1 514 107 107 SER H H 7.996 0.00 1 515 107 107 SER HA H 4.269 0.00 1 516 107 107 SER CA C 60.287 0.00 1 517 107 107 SER CB C 63.893 0.00 1 518 107 107 SER N N 113.088 0.00 1 519 108 108 GLY H H 8.066 0.00 1 520 108 108 GLY HA2 H 3.970 0.00 1 521 108 108 GLY HA3 H 3.970 0.00 1 522 108 108 GLY CA C 45.944 0.00 1 523 108 108 GLY N N 109.156 0.00 1 524 109 109 ASP H H 8.119 0.00 1 525 109 109 ASP CA C 53.269 0.00 1 526 109 109 ASP CB C 38.170 0.00 1 527 109 109 ASP N N 118.500 0.00 1 528 110 110 HIS H H 8.302 0.00 1 529 110 110 HIS HA H 4.654 0.00 1 530 110 110 HIS CA C 56.094 0.00 1 531 110 110 HIS CB C 28.660 0.00 1 532 110 110 HIS N N 117.415 0.00 1 533 111 111 CYS H H 8.293 0.00 1 534 111 111 CYS HA H 4.502 0.00 1 535 111 111 CYS CA C 59.399 0.00 1 536 111 111 CYS CB C 27.674 0.00 1 537 111 111 CYS N N 118.550 0.00 1 538 112 112 ILE H H 8.265 0.00 1 539 112 112 ILE HA H 4.115 0.00 1 540 112 112 ILE CA C 62.697 0.00 1 541 112 112 ILE CB C 38.458 0.00 1 542 112 112 ILE N N 121.950 0.00 1 543 113 113 ILE H H 8.031 0.00 1 544 113 113 ILE HA H 4.027 0.00 1 545 113 113 ILE CA C 62.669 0.00 1 546 113 113 ILE CB C 38.270 0.00 1 547 113 113 ILE N N 121.561 0.00 1 548 114 114 GLY H H 8.265 0.00 1 549 114 114 GLY HA2 H 3.897 0.00 1 550 114 114 GLY HA3 H 3.897 0.00 1 551 114 114 GLY CA C 46.498 0.00 1 552 114 114 GLY N N 109.652 0.00 1 553 115 115 ARG H H 8.073 0.00 1 554 115 115 ARG HA H 4.215 0.00 1 555 115 115 ARG CA C 57.749 0.00 1 556 115 115 ARG CB C 30.641 0.00 1 557 115 115 ARG N N 119.514 0.00 1 558 116 116 THR H H 7.965 0.00 1 559 116 116 THR HA H 4.182 0.00 1 560 116 116 THR CA C 64.288 0.00 1 561 116 116 THR CB C 69.277 0.00 1 562 116 116 THR N N 113.665 0.00 1 563 117 117 LEU H H 8.009 0.00 1 564 117 117 LEU HA H 4.256 0.00 1 565 117 117 LEU CA C 56.750 0.00 1 566 117 117 LEU CB C 42.374 0.00 1 567 117 117 LEU N N 122.716 0.00 1 568 118 118 VAL H H 7.805 0.00 1 569 118 118 VAL HA H 3.923 0.00 1 570 118 118 VAL CA C 64.159 0.00 1 571 118 118 VAL CB C 32.290 0.00 1 572 118 118 VAL N N 118.610 0.00 1 573 119 119 VAL H H 7.971 0.00 1 574 119 119 VAL HA H 3.952 0.00 1 575 119 119 VAL CA C 64.233 0.00 1 576 119 119 VAL CB C 32.197 0.00 1 577 119 119 VAL N N 118.576 0.00 1 578 120 120 HIS H H 8.444 0.00 1 579 120 120 HIS HA H 4.618 0.00 1 580 120 120 HIS CA C 55.955 0.00 1 581 120 120 HIS CB C 28.903 0.00 1 582 120 120 HIS N N 119.988 0.00 1 583 121 121 GLU H H 8.188 0.00 1 584 121 121 GLU HA H 4.336 0.00 1 585 121 121 GLU CA C 56.096 0.00 1 586 121 121 GLU CB C 28.975 0.00 1 587 121 121 GLU N N 120.536 0.00 1 588 122 122 LYS CA C 56.787 0.00 1 589 122 122 LYS CB C 33.068 0.00 1 590 123 123 ALA H H 8.228 0.00 1 591 123 123 ALA HA H 4.265 0.00 1 592 123 123 ALA CA C 53.030 0.00 1 593 123 123 ALA CB C 19.238 0.00 1 594 123 123 ALA N N 124.596 0.00 1 595 124 124 ASP H H 8.169 0.00 1 596 124 124 ASP HA H 4.702 0.00 1 597 124 124 ASP CA C 53.276 0.00 1 598 124 124 ASP CB C 38.415 0.00 1 599 124 124 ASP N N 117.288 0.00 1 stop_ save_