data_18509 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Structure and chemical shifts of Cu(I),Zn(II) superoxide dismutase by solid-state NMR ; _BMRB_accession_number 18509 _BMRB_flat_file_name bmr18509.str _Entry_type original _Submission_date 2012-06-08 _Accession_date 2012-06-08 _Entry_origination author _NMR_STAR_version 2.1.1 _Experimental_method NMR _Details 'Solid-state NMR structure using paramagnetic restraints' loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Knight Michael J. . 2 Pell Andrew J. . 3 Bertini Ivano . . 4 Felli Isabella C. . 5 Gonnelli Leonardo . . 6 Pierattelli Roberta . . 7 Herrmann Torsten . . 8 Emsley Lyndon . . 9 Pintacuda Guido . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 136 "13C chemical shifts" 245 "15N chemical shifts" 136 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2012-08-29 original author . stop_ _Original_release_date 2012-08-29 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title 'Structure and backbone dynamics of a microcrystalline metalloprotein by solid-state NMR' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 22723345 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Knight Michael J. . 2 Pell Andrew J. . 3 Bertini Ivano . . 4 Felli Isabella C. . 5 Gonnelli Leonardo . . 6 Pierattelli Roberta . . 7 Herrmann Torsten . . 8 Emsley Lyndon . . 9 Pintacuda Guido . . stop_ _Journal_abbreviation 'Proc. Natl. Acad. Sci. U.S.A.' _Journal_volume 109 _Journal_issue 28 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 11095 _Page_last 11100 _Year 2012 _Details . save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name 'Cu(I),Zn(II) superoxide dismutase' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label Superoxide_dismutase_C6A/C111S_thermostable_mutant $Superoxide_dismutase_C6A-C111S_thermostable_mutant CU2 $CU 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_Superoxide_dismutase_C6A-C111S_thermostable_mutant _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common Superoxide_dismutase_C6A-C111S_thermostable_mutant _Molecular_mass 15779.566 _Mol_thiol_state 'all disulfide bound' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 153 _Mol_residue_sequence ; ATKAVAVLKGDGPVQGIINF EQKESNGPVKVWGSIKGLTE GLHGFHVHEFGDNTAGCTSA GPHFNPLSRKHGGPKDEERH VGDLGNVTADKDGVADVSIE DSVISLSGDHSIIGRTLVVH 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 PHE 51 GLY 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 SER 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 2015-08-12 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 98.04 98.69 1.90e-100 BMRB 15712 SOD1 100.00 153 97.39 98.04 1.24e-99 BMRB 15713 SOD1 100.00 153 97.39 98.04 2.19e-99 BMRB 15714 SOD1 100.00 153 97.39 98.04 2.26e-99 BMRB 18708 SUPEROXIDE_DISMUTASE_CU-ZN 100.00 153 100.00 100.00 3.83e-103 BMRB 18968 SOD1 100.00 153 98.04 98.69 1.90e-100 BMRB 19962 L126Z-sod1 81.70 125 98.40 98.40 5.34e-81 BMRB 26570 SOD1 100.00 153 100.00 100.00 3.83e-103 BMRB 4202 "Superoxide Dismutase" 100.00 153 98.04 98.69 2.23e-100 PDB 1AZV "Familial Als Mutant G37r Cuznsod (Human)" 100.00 153 98.04 98.04 1.22e-100 PDB 1BA9 "The Solution Structure Of Reduced Monomeric Superoxide Dismutase, Nmr, 36 Structures" 99.35 153 98.03 98.68 1.03e-99 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 97.37 4.71e-98 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 99.35 100.00 1.26e-102 PDB 1HL4 "The Structure Of Apo Type Human Cu, Zn Superoxide Dismutase" 100.00 154 98.69 98.69 1.15e-101 PDB 1HL5 "The Structure Of Holo Type Human Cu, Zn Superoxide Dismutase" 100.00 153 98.69 98.69 1.11e-101 PDB 1KMG "The Solution Structure Of Monomeric Copper-Free Superoxide Dismutase" 100.00 153 98.04 98.69 2.23e-100 PDB 1L3N "The Solution Structure Of Reduced Dimeric Copper Zinc Sod: The Structural Effects Of Dimerization" 100.00 153 100.00 100.00 3.83e-103 PDB 1MFM "Monomeric Human Sod Mutant F50eG51EE133Q AT ATOMIC Resolution" 100.00 153 98.04 98.69 2.23e-100 PDB 1N18 "Thermostable Mutant Of Human Superoxide Dismutase, C6a, C111s" 100.00 154 100.00 100.00 3.05e-103 PDB 1N19 "Structure Of The Hsod A4v Mutant" 100.00 154 99.35 99.35 1.27e-102 PDB 1OEZ "Zn His46arg Mutant Of Human Cu, Zn Superoxide Dismutase" 100.00 153 98.04 98.04 1.01e-100 PDB 1OZT "Crystal Structure Of Apo-H46r Familial Als Mutant Human Cu, Zn Superoxide Dismutase (Cuznsod) To 2.5a Resolution" 100.00 153 98.04 98.04 1.01e-100 PDB 1OZU "Crystal Structure Of Familial Als Mutant S134n Of Human Cu, Zn Superoxide Dismutase (Cuznsod) To 1.3a Resolution" 100.00 153 98.04 98.69 3.89e-101 PDB 1P1V "Crystal Structure Of Fals-Associated Human Copper-Zinc Superoxide Dismutase (Cuznsod) Mutant D125h To 1.4a" 100.00 153 98.04 98.04 1.51e-100 PDB 1PTZ "Crystal Structure Of The Human Cu, Zn Superoxide Dismutase, Familial Amyotrophic Lateral Sclerosis (Fals) Mutant H43r" 100.00 153 99.35 99.35 2.70e-102 PDB 1PU0 "Structure Of Human Cu,Zn Superoxide Dismutase" 100.00 153 98.69 98.69 1.11e-101 PDB 1RK7 "Solution Structure Of Apo Cu,Zn Superoxide Dismutase: Role Of Metal Ions In Protein Folding" 100.00 153 98.04 98.69 2.23e-100 PDB 1SOS "Atomic Structures Of Wild-type And Thermostable Mutant Recombinant Human Cu, Zn Superoxide Dismutase" 100.00 154 100.00 100.00 3.96e-103 PDB 1SPD "Amyotrophic Lateral Sclerosis And Structural Defects In Cu,Zn Superoxide Dismutase" 100.00 154 98.69 98.69 1.15e-101 PDB 1UXL "I113t Mutant Of Human Sod1" 100.00 153 98.04 98.04 5.83e-101 PDB 1UXM "A4v Mutant Of Human Sod1" 100.00 153 98.04 98.04 5.22e-101 PDB 2AF2 "Solution Structure Of Disulfide Reduced And Copper Depleted Human Superoxide Dismutase" 100.00 153 100.00 100.00 3.83e-103 PDB 2C9S "1.24 Angstroms Resolution Structure Of Zn-Zn Human Superoxide Dismutase" 100.00 153 98.69 98.69 1.06e-101 PDB 2C9U "1.24 Angstroms Resolution Structure Of As-Isolated Cu-Zn Human Superoxide Dismutase" 100.00 153 98.69 98.69 1.11e-101 PDB 2C9V "Atomic Resolution Structure Of Cu-Zn Human Superoxide Dismutase" 100.00 153 98.69 98.69 1.11e-101 PDB 2GBT "C6aC111A CUZN SUPEROXIDE DISMUTASE" 100.00 153 99.35 100.00 8.97e-103 PDB 2GBU "C6a/c111a/c57a/c146a Apo Cuzn Superoxide Dismutase" 100.00 153 98.04 98.69 1.10e-100 PDB 2GBV "C6aC111AC57AC146A HOLO CUZN SUPEROXIDE DISMUTASE" 100.00 153 98.04 98.69 1.10e-100 PDB 2LU5 "Structure And Chemical Shifts Of Cu(I),Zn(Ii) Superoxide Dismutase By Solid-State Nmr" 100.00 153 100.00 100.00 3.83e-103 PDB 2MP3 "Truncated L126z-sod1 In Dpc Micelle" 81.70 132 98.40 98.40 1.59e-80 PDB 2NNX "Crystal Structure Of The H46r, H48q Double Mutant Of Human [cu-Zn] Superoxide Dismutase" 100.00 154 97.39 97.39 6.31e-100 PDB 2R27 "Constitutively Zinc-Deficient Mutant Of Human Superoxide Dismutase (Sod), C6a, H80s, H83s, C111s" 100.00 154 98.69 98.69 1.35e-101 PDB 2V0A "Atomic Resolution Crystal Structure Of Human Superoxide Dismutase" 100.00 153 98.69 98.69 1.11e-101 PDB 2VR6 "Crystal Structure Of G85r Als Mutant Of Human Cu,Zn Superoxide Dismutase (Cuznsod) At 1.3 A Resolution" 100.00 153 98.04 98.04 1.22e-100 PDB 2VR7 "Crystal Structure Of G85r Als Mutant Of Human Cu,Zn Superoxide Dismutase (Cuznsod) At 1.58 A Resolution" 100.00 154 98.04 98.04 1.27e-100 PDB 2VR8 "Crystal Structure Of G85r Als Mutant Of Human Cu,Zn Superoxide Dismutase (Cuznsod) At 1.36 A Resolution" 100.00 154 98.04 98.04 1.23e-100 PDB 2WKO "Structure Of Metal Loaded Pathogenic Sod1 Mutant G93a" 100.00 154 98.04 98.04 4.44e-101 PDB 2WYT "1.0 A Resolution Structure Of L38v Sod1 Mutant" 100.00 153 98.04 98.69 3.64e-101 PDB 2WYZ "L38v Sod1 Mutant Complexed With Ump" 100.00 153 98.04 98.69 3.89e-101 PDB 2WZ0 "L38v Sod1 Mutant Complexed With Aniline." 100.00 153 98.04 98.69 3.64e-101 PDB 2WZ5 "L38v Sod1 Mutant Complexed With L-Methionine" 100.00 153 98.04 98.69 3.64e-101 PDB 2WZ6 "G93a Sod1 Mutant Complexed With Quinazoline" 100.00 153 98.04 98.04 4.29e-101 PDB 2XJK "Monomeric Human Cu,Zn Superoxide Dismutase" 100.00 153 98.04 98.69 1.90e-100 PDB 2ZKW "Crystal Structure Of Human Cu-Zn Superoxide Dismutase Mutant G85r In Space Group P21" 100.00 159 98.04 98.04 1.15e-100 PDB 2ZKX "Crystal Structure Of Human Cu-Zn Superoxide Dismutase Mutant G85r In Space Group I212121" 100.00 159 98.04 98.04 1.15e-100 PDB 2ZKY "Crystal Structure Of Human Cu-Zn Superoxide Dismutase Mutant G93a" 100.00 159 98.04 98.04 4.09e-101 PDB 3CQP "Human Sod1 G85r Variant, Structure I" 100.00 153 98.04 98.04 1.22e-100 PDB 3CQQ "Human Sod1 G85r Variant, Structure Ii" 100.00 153 98.04 98.04 1.19e-100 PDB 3ECU "Crystal Structure Of Human Apo Cu,Zn Superoxide Dismutase (Sod1)" 100.00 153 98.69 98.69 1.11e-101 PDB 3ECV "Crystal Structure Of The Als-Related Pathological Mutant I113t Of Human Apo Cu,Zn Superoxide Dismutase (Sod1)" 100.00 153 98.04 98.04 5.83e-101 PDB 3ECW "Crystal Structure Of The Als-Related Pathological Mutant T54r Of Human Apo Cu,Zn Superoxide Dismutase (Sod1)" 100.00 153 98.04 98.04 9.12e-101 PDB 3GQF "Structural And Biophysical Properties Of The Pathogenic Sod1 Variant H46rH48Q" 100.00 153 97.39 97.39 6.10e-100 PDB 3GZO "Human Sod1 G93a Variant" 100.00 154 98.04 98.04 4.44e-101 PDB 3GZP "Human Sod1 G93a Metal-Free Variant" 100.00 153 98.04 98.04 4.29e-101 PDB 3GZQ "Human Sod1 A4v Metal-Free Variant" 100.00 154 98.04 98.04 5.40e-101 PDB 3H2P "Human Sod1 D124v Variant" 100.00 153 98.04 98.04 1.66e-100 PDB 3H2Q "Human Sod1 H80r Variant, P21 Crystal Form" 100.00 153 98.04 98.04 1.01e-100 PDB 3K91 "Polysulfane Bridge In Cu-Zn Superoxide Dismutase" 100.00 153 97.39 97.39 6.10e-100 PDB 3KH3 "Crystal Structure Of Human CuZN SUPEROXIDE DISMUTASE RECOMBINANTLY Produced In Leishmania Tarantolae; P212121 Crystal Form Cont" 100.00 153 98.69 98.69 1.11e-101 PDB 3KH4 "Crystal Structure Of Human CuZN SUPEROXIDE DISMUTASE RECOMBINANTLY Produced In Leishmania Tarantolae; P6522 Crystal Form Contai" 100.00 153 98.69 98.69 1.11e-101 PDB 3QQD "Human Sod1 H80r Variant, P212121 Crystal Form" 100.00 154 98.04 98.04 1.12e-100 PDB 3RE0 "Crystal Structure Of Human Apo Cu,zn Superoxide Dismutase (sod1) Complexed With Cisplatin" 100.00 153 98.69 98.69 1.11e-101 PDB 3T5W "2me Modified Human Sod1" 100.00 153 98.69 98.69 1.06e-101 PDB 4A7G "Structure Of Human I113t Sod1 Mutant Complexed With 4- Methylpiperazin-1-yl)quinazoline In The P21 Space Group." 100.00 153 98.04 98.04 5.83e-101 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 98.04 98.04 5.83e-101 PDB 4A7S "Structure Of Human I113t Sod1 Mutant Complexed With 5- Fluorouridine In The P21 Space Group" 100.00 153 98.04 98.04 5.83e-101 PDB 4A7T "Structure Of Human I113t Sod1 Mutant Complexed With Isoproteranol In The P21 Space Group" 100.00 153 98.04 98.04 5.83e-101 PDB 4A7U "Structure Of Human I113t Sod1 Complexed With Adrenaline In The P21 Space Group." 100.00 153 98.04 98.04 5.83e-101 PDB 4A7V "Structure Of Human I113t Sod1 Mutant Complexed With Dopamine In The P21 Space Group" 100.00 153 98.04 98.04 5.83e-101 PDB 4B3E "Structure Of Copper-Zinc Superoxide Dismutase Complexed With Bicarbonate." 100.00 154 98.69 98.69 8.53e-102 PDB 4BCY "Monomeric Human Cu,zn Superoxide Dismutase, Mutation H43f" 100.00 153 97.39 98.04 3.62e-99 PDB 4FF9 "Crystal Structure Of Cysteinylated Wt Sod1" 100.00 153 98.69 98.69 1.11e-101 PDB 4MCM "Human Sod1 C57s Mutant, As-isolated" 100.00 153 98.04 98.04 2.87e-100 PDB 4MCN "Human Sod1 C57s Mutant, Metal-free" 100.00 153 98.04 98.04 2.87e-100 PDB 4OH2 "Crystal Structure Of Cu/zn Superoxide Dismutase I149t" 100.00 153 99.35 99.35 1.52e-102 DBJ BAA14373 "unnamed protein product [Schizosaccharomyces pombe]" 98.69 179 98.68 98.68 4.27e-100 DBJ BAC20345 "Cu,Zn-superoxide dismutase [Pan troglodytes]" 100.00 154 98.69 98.69 8.53e-102 DBJ BAG35052 "unnamed protein product [Homo sapiens]" 100.00 154 98.69 98.69 8.53e-102 DBJ BAG73767 "superoxide dismutase 1, soluble [synthetic construct]" 100.00 154 98.69 98.69 8.53e-102 EMBL CAA26182 "unnamed protein product [Homo sapiens]" 100.00 154 98.69 98.69 8.53e-102 EMBL CAG29351 "SOD1 [Homo sapiens]" 100.00 154 98.69 98.69 8.53e-102 EMBL CAG46542 "SOD1 [Homo sapiens]" 100.00 154 98.69 98.69 8.53e-102 GB AAA72747 "CuZn superoxide dismutase [synthetic construct]" 100.00 154 100.00 100.00 3.05e-103 GB AAA80237 "HSOD-GlyProGly-A+, partial [synthetic construct]" 100.00 171 100.00 100.00 1.11e-102 GB AAB05661 "Cu/Zn-superoxide dismutase [Homo sapiens]" 100.00 154 98.69 98.69 8.53e-102 GB AAB05662 "Cu/Zn-superoxide dismutase [Homo sapiens]" 100.00 154 98.04 98.04 1.32e-100 GB AAB27818 "Cu,Zn superoxide dismutase, SOD=SOD1 gene product {A to V single-site mutation} [human, Peptide Mutant, 153 aa]" 100.00 153 98.04 98.04 5.22e-101 REF NP_000445 "superoxide dismutase [Cu-Zn] [Homo sapiens]" 100.00 154 98.69 98.69 8.53e-102 REF NP_001009025 "superoxide dismutase [Cu-Zn] [Pan troglodytes]" 100.00 154 98.69 98.69 8.53e-102 REF XP_003813274 "PREDICTED: superoxide dismutase [Cu-Zn] [Pan paniscus]" 100.00 154 98.69 98.69 8.53e-102 REF XP_004062735 "PREDICTED: superoxide dismutase [Cu-Zn] [Gorilla gorilla gorilla]" 100.00 154 98.04 98.04 8.18e-101 REF XP_004062736 "PREDICTED: superoxide dismutase [Cu-Zn] [Gorilla gorilla gorilla]" 100.00 154 98.04 98.04 8.18e-101 SP P00441 "RecName: Full=Superoxide dismutase [Cu-Zn]; AltName: Full=Superoxide dismutase 1; Short=hSod1" 100.00 154 98.69 98.69 8.53e-102 SP P60052 "RecName: Full=Superoxide dismutase [Cu-Zn]" 100.00 154 98.69 98.69 8.53e-102 stop_ save_ ############# # Ligands # ############# save_CU _Saveframe_category ligand _Mol_type "non-polymer (NON-POLYMER)" _Name_common 'COPPER (II) ION' _BMRB_code CU _PDB_code CU _Molecular_mass 63.546 _Mol_charge 2 _Mol_paramagnetic . _Mol_aromatic no _Details . loop_ _Atom_name _PDB_atom_name _Atom_type _Atom_chirality _Atom_charge _Atom_oxidation_number _Atom_unpaired_electrons CU CU CU . 2 . ? stop_ _Mol_thiol_state . _Sequence_homology_query_date . save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $Superoxide_dismutase_C6A-C111S_thermostable_mutant 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 $Superoxide_dismutase_C6A-C111S_thermostable_mutant 'recombinant technology' . Escherichia coli . pPHSOD1lac1 stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Saveframe_category sample _Sample_type 'polycrystalline powder' _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $Superoxide_dismutase_C6A-C111S_thermostable_mutant 3.5 mg '[U-13C; U-15N; U-2H]' 'Sodium Citrate' 20 mM 'natural abundance' 'Polyethylene Glycol 6000' .20 w/v 'natural abundance' stop_ save_ ############################ # Computer software used # ############################ save_CYANA _Saveframe_category software _Name CYANA _Version . loop_ _Vendor _Address _Electronic_address 'Guntert, Mumenthaler and Wuthrich' . . stop_ loop_ _Task 'structure solution' stop_ _Details . save_ save_UNIO _Saveframe_category software _Name UNIO _Version 2.5.0 loop_ _Vendor _Address _Electronic_address 'Herrmann, Guntert and Wuthrich' . . stop_ loop_ _Task 'chemical shift assignment' collection 'peak picking' stop_ _Details 'Using ATNOS/CANDID module in UNIO for automated peak picking and cross peak assignment' save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model Avance _Field_strength 850 _Details . save_ ############################# # NMR applied experiments # ############################# save_2D_CP-HSQC_1 _Saveframe_category NMR_applied_experiment _Experiment_name '2D CP-HSQC' _Sample_label $sample_1 save_ save_2D_R1_15N_2 _Saveframe_category NMR_applied_experiment _Experiment_name '2D R1_15N' _Sample_label $sample_1 save_ save_2D_R1_13C_3 _Saveframe_category NMR_applied_experiment _Experiment_name '2D R1_13C' _Sample_label $sample_1 save_ save_2D_(H)NHH_RFDR_4 _Saveframe_category NMR_applied_experiment _Experiment_name '2D (H)NHH_RFDR' _Sample_label $sample_1 save_ save_3D_(H)CONH_5 _Saveframe_category NMR_applied_experiment _Experiment_name '3D (H)CONH' _Sample_label $sample_1 save_ save_2D_NCA_6 _Saveframe_category NMR_applied_experiment _Experiment_name '2D NCA' _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' 0.02 . M pH 5 . pH pressure 1 . atm temperature 286 . 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 TMS C 13 'methyl protons' ppm 0 external indirect . . . . TMS H 1 'methyl protons' ppm 0 external direct . . . 1 TMS N 15 'methyl protons' ppm 0 external indirect . . . . 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 CP-HSQC' '3D (H)CONH' '2D NCA' 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 Superoxide_dismutase_C6A/C111S_thermostable_mutant _Text_data_format . _Text_data . loop_ _Atom_shift_assign_ID _Residue_author_seq_code _Residue_seq_code _Residue_label _Atom_name _Atom_type _Chem_shift_value _Chem_shift_value_error _Chem_shift_ambiguity_code 1 2 2 THR C C 170.139 0.40 1 2 3 3 LYS H H 8.666 0.02 1 3 3 3 LYS C C 171.607 0.40 1 4 3 3 LYS CA C 51.178 0.40 1 5 3 3 LYS N N 123.998 0.40 1 6 4 4 ALA H H 9.116 0.02 1 7 4 4 ALA C C 172.145 0.40 1 8 4 4 ALA CA C 47.504 0.40 1 9 4 4 ALA N N 123.295 0.40 1 10 5 5 VAL H H 9.545 0.02 1 11 5 5 VAL C C 167.836 0.40 1 12 5 5 VAL CA C 56.875 0.40 1 13 5 5 VAL N N 121.466 0.40 1 14 6 6 ALA H H 9.177 0.02 1 15 6 6 ALA C C 171.607 0.40 1 16 6 6 ALA CA C 47.471 0.40 1 17 6 6 ALA N N 125.984 0.40 1 18 7 7 VAL H H 9.116 0.02 1 19 7 7 VAL C C 172.244 0.40 1 20 7 7 VAL CA C 58.476 0.40 1 21 7 7 VAL N N 123.600 0.40 1 22 8 8 LEU H H 8.916 0.02 1 23 8 8 LEU C C 172.557 0.40 1 24 8 8 LEU CA C 51.052 0.40 1 25 8 8 LEU N N 126.455 0.40 1 26 9 9 LYS H H 8.315 0.02 1 27 9 9 LYS C C 172.509 0.40 1 28 9 9 LYS CA C 51.897 0.40 1 29 9 9 LYS N N 120.820 0.40 1 30 10 10 GLY H H 8.968 0.02 1 31 10 10 GLY C C 169.847 0.40 1 32 10 10 GLY CA C 42.275 0.40 1 33 10 10 GLY N N 111.249 0.40 1 34 11 11 ASP H H 8.745 0.02 1 35 11 11 ASP C C 173.132 0.40 1 36 11 11 ASP CA C 51.317 0.40 1 37 11 11 ASP N N 120.904 0.40 1 38 12 12 GLY H H 7.985 0.02 1 39 12 12 GLY CA C 41.200 0.40 1 40 12 12 GLY N N 109.862 0.40 1 41 13 13 PRO C C 173.640 0.40 1 42 14 14 VAL H H 7.476 0.02 1 43 14 14 VAL C C 172.804 0.40 1 44 14 14 VAL CA C 59.884 0.40 1 45 14 14 VAL N N 120.414 0.40 1 46 15 15 GLN H H 7.938 0.02 1 47 15 15 GLN C C 171.168 0.40 1 48 15 15 GLN CA C 50.679 0.40 1 49 15 15 GLN N N 122.664 0.40 1 50 16 16 GLY H H 8.288 0.02 1 51 16 16 GLY C C 167.726 0.40 1 52 16 16 GLY CA C 43.625 0.40 1 53 16 16 GLY N N 107.018 0.40 1 54 17 17 ILE H H 7.948 0.02 1 55 17 17 ILE C C 171.194 0.40 1 56 17 17 ILE CA C 58.497 0.40 1 57 17 17 ILE N N 120.248 0.40 1 58 18 18 ILE H H 8.725 0.02 1 59 18 18 ILE C C 168.889 0.40 1 60 18 18 ILE CA C 53.431 0.40 1 61 18 18 ILE N N 125.851 0.40 1 62 19 19 ASN H H 8.727 0.02 1 63 19 19 ASN C C 168.903 0.40 1 64 19 19 ASN CA C 49.088 0.40 1 65 19 19 ASN N N 123.256 0.40 1 66 20 20 PHE H H 8.399 0.02 1 67 20 20 PHE C C 173.219 0.40 1 68 20 20 PHE CA C 52.058 0.40 1 69 20 20 PHE N N 113.849 0.40 1 70 21 21 GLU H H 9.526 0.02 1 71 21 21 GLU C C 170.280 0.40 1 72 21 21 GLU CA C 53.044 0.40 1 73 21 21 GLU N N 121.454 0.40 1 74 22 22 GLN H H 9.305 0.02 1 75 22 22 GLN CA C 51.180 0.40 1 76 22 22 GLN N N 130.340 0.40 1 77 23 23 LYS H H 9.088 0.02 1 78 23 23 LYS CA C 57.241 0.40 1 79 23 23 LYS N N 128.657 0.40 1 80 24 24 GLU CA C 51.392 0.40 1 81 25 25 SER CA C 58.078 0.40 1 82 27 27 GLY H H 8.032 0.02 1 83 27 27 GLY CA C 42.925 0.40 1 84 27 27 GLY N N 108.125 0.40 1 85 28 28 PRO C C 173.128 0.40 1 86 29 29 VAL H H 9.089 0.02 1 87 29 29 VAL C C 172.198 0.40 1 88 29 29 VAL CA C 57.720 0.40 1 89 29 29 VAL N N 121.267 0.40 1 90 30 30 LYS H H 9.200 0.02 1 91 30 30 LYS C C 172.098 0.40 1 92 30 30 LYS CA C 52.642 0.40 1 93 30 30 LYS N N 127.589 0.40 1 94 31 31 VAL H H 9.282 0.02 1 95 31 31 VAL C C 172.244 0.40 1 96 31 31 VAL CA C 57.139 0.40 1 97 31 31 VAL N N 126.037 0.40 1 98 32 32 TRP H H 8.983 0.02 1 99 32 32 TRP C C 170.156 0.40 1 100 32 32 TRP CA C 53.137 0.40 1 101 32 32 TRP N N 125.414 0.40 1 102 33 33 GLY H H 8.360 0.02 1 103 33 33 GLY C C 168.400 0.40 1 104 33 33 GLY CA C 41.567 0.40 1 105 33 33 GLY N N 107.848 0.40 1 106 34 34 SER H H 7.838 0.02 1 107 34 34 SER C C 169.618 0.40 1 108 34 34 SER CA C 53.875 0.40 1 109 34 34 SER N N 114.377 0.40 1 110 35 35 ILE H H 8.496 0.02 1 111 35 35 ILE C C 169.713 0.40 1 112 35 35 ILE CA C 56.769 0.40 1 113 35 35 ILE N N 123.149 0.40 1 114 36 36 LYS H H 9.091 0.02 1 115 36 36 LYS C C 172.260 0.40 1 116 36 36 LYS CA C 51.150 0.40 1 117 36 36 LYS N N 123.803 0.40 1 118 37 37 GLY H H 8.237 0.02 1 119 37 37 GLY C C 171.641 0.40 1 120 37 37 GLY CA C 42.361 0.40 1 121 37 37 GLY N N 105.495 0.40 1 122 38 38 LEU H H 8.156 0.02 1 123 38 38 LEU C C 174.112 0.40 1 124 38 38 LEU CA C 50.471 0.40 1 125 38 38 LEU N N 120.966 0.40 1 126 39 39 THR H H 8.660 0.02 1 127 39 39 THR C C 173.102 0.40 1 128 39 39 THR CA C 58.194 0.40 1 129 39 39 THR N N 110.363 0.40 1 130 40 40 GLU H H 8.804 0.02 1 131 40 40 GLU C C 173.134 0.40 1 132 40 40 GLU CA C 54.356 0.40 1 133 40 40 GLU N N 125.818 0.40 1 134 41 41 GLY H H 8.763 0.02 1 135 41 41 GLY C C 170.046 0.40 1 136 41 41 GLY CA C 40.054 0.40 1 137 41 41 GLY N N 113.875 0.40 1 138 42 42 LEU H H 8.313 0.02 1 139 42 42 LEU C C 174.218 0.40 1 140 42 42 LEU CA C 52.155 0.40 1 141 42 42 LEU N N 120.137 0.40 1 142 43 43 HIS H H 8.712 0.02 1 143 43 43 HIS C C 171.504 0.40 1 144 43 43 HIS CA C 50.985 0.40 1 145 43 43 HIS N N 114.385 0.40 1 146 44 44 GLY H H 8.875 0.02 1 147 44 44 GLY C C 168.656 0.40 1 148 44 44 GLY CA C 44.195 0.40 1 149 44 44 GLY N N 108.872 0.40 1 150 45 45 PHE H H 8.111 0.02 1 151 45 45 PHE CA C 53.098 0.40 1 152 45 45 PHE N N 126.439 0.40 1 153 46 46 HIS H H 8.107 0.02 1 154 46 46 HIS C C 172.415 0.40 1 155 46 46 HIS CA C 49.206 0.40 1 156 46 46 HIS N N 115.353 0.40 1 157 47 47 VAL H H 9.366 0.02 1 158 47 47 VAL C C 173.900 0.40 1 159 47 47 VAL CA C 58.792 0.40 1 160 47 47 VAL N N 120.548 0.40 1 161 48 48 HIS H H 10.210 0.02 1 162 48 48 HIS C C 171.084 0.40 1 163 48 48 HIS CA C 52.756 0.40 1 164 48 48 HIS N N 129.236 0.40 1 165 49 49 GLU H H 8.492 0.02 1 166 49 49 GLU C C 171.635 0.40 1 167 49 49 GLU CA C 57.759 0.40 1 168 49 49 GLU N N 118.119 0.40 1 169 50 50 PHE H H 8.580 0.02 1 170 50 50 PHE C C 175.252 0.40 1 171 50 50 PHE CA C 52.900 0.40 1 172 50 50 PHE N N 110.329 0.40 1 173 51 51 GLY H H 10.208 0.02 1 174 51 51 GLY C C 168.248 0.40 1 175 51 51 GLY N N 119.251 0.40 1 176 52 52 ASP H H 5.834 0.02 1 177 52 52 ASP CA C 48.891 0.40 1 178 52 52 ASP N N 114.958 0.40 1 179 53 53 ASN H H 9.360 0.02 1 180 53 53 ASN CA C 48.233 0.40 1 181 53 53 ASN N N 128.224 0.40 1 182 54 54 THR C C 168.656 0.40 1 183 55 55 ALA H H 8.390 0.02 1 184 55 55 ALA C C 174.185 0.40 1 185 55 55 ALA CA C 46.155 0.40 1 186 55 55 ALA N N 126.661 0.40 1 187 56 56 GLY H H 7.282 0.02 1 188 56 56 GLY C C 171.578 0.40 1 189 56 56 GLY CA C 42.580 0.40 1 190 56 56 GLY N N 107.903 0.40 1 191 57 57 CYS H H 8.900 0.02 1 192 57 57 CYS C C 175.209 0.40 1 193 57 57 CYS CA C 49.088 0.40 1 194 57 57 CYS N N 117.952 0.40 1 195 58 58 THR H H 8.505 0.02 1 196 58 58 THR CA C 58.239 0.40 1 197 58 58 THR N N 119.852 0.40 1 198 59 59 SER C C 170.763 0.40 1 199 59 59 SER CA C 55.609 0.40 1 200 60 60 ALA H H 6.898 0.02 1 201 60 60 ALA CA C 49.940 0.40 1 202 60 60 ALA N N 119.753 0.40 1 203 61 61 GLY H H 7.730 0.02 1 204 61 61 GLY CA C 42.805 0.40 1 205 61 61 GLY N N 101.351 0.40 1 206 62 62 PRO C C 172.276 0.40 1 207 63 63 HIS H H 7.474 0.02 1 208 63 63 HIS CA C 52.119 0.40 1 209 63 63 HIS N N 115.023 0.40 1 210 64 64 PHE C C 171.731 0.40 1 211 65 65 ASN H H 9.426 0.02 1 212 65 65 ASN CA C 47.753 0.40 1 213 65 65 ASN N N 126.978 0.40 1 214 67 67 LEU H H 7.720 0.02 1 215 67 67 LEU C C 172.580 0.40 1 216 67 67 LEU CA C 50.911 0.40 1 217 67 67 LEU N N 117.937 0.40 1 218 68 68 SER H H 7.428 0.02 1 219 68 68 SER CA C 55.953 0.40 1 220 68 68 SER N N 110.842 0.40 1 221 69 69 ARG H H 8.508 0.02 1 222 69 69 ARG C C 173.381 0.40 1 223 69 69 ARG CA C 50.543 0.40 1 224 69 69 ARG N N 120.782 0.40 1 225 70 70 LYS H H 8.745 0.02 1 226 70 70 LYS C C 169.994 0.40 1 227 70 70 LYS CA C 52.596 0.40 1 228 70 70 LYS N N 118.055 0.40 1 229 71 71 HIS H H 7.152 0.02 1 230 71 71 HIS C C 171.534 0.40 1 231 71 71 HIS CA C 52.549 0.40 1 232 71 71 HIS N N 111.871 0.40 1 233 72 72 GLY H H 7.209 0.02 1 234 72 72 GLY C C 168.634 0.40 1 235 72 72 GLY CA C 41.274 0.40 1 236 72 72 GLY N N 112.910 0.40 1 237 73 73 GLY H H 8.789 0.02 1 238 73 73 GLY CA C 41.221 0.40 1 239 73 73 GLY N N 105.207 0.40 1 240 74 74 PRO C C 175.753 0.40 1 241 75 75 LYS H H 8.651 0.02 1 242 75 75 LYS C C 173.640 0.40 1 243 75 75 LYS CA C 51.103 0.40 1 244 75 75 LYS N N 114.868 0.40 1 245 76 76 ASP H H 7.461 0.02 1 246 76 76 ASP C C 172.557 0.40 1 247 76 76 ASP CA C 51.309 0.40 1 248 76 76 ASP N N 120.414 0.40 1 249 77 77 GLU H H 8.315 0.02 1 250 77 77 GLU C C 174.101 0.40 1 251 77 77 GLU CA C 55.513 0.40 1 252 77 77 GLU N N 120.820 0.40 1 253 78 78 GLU H H 8.109 0.02 1 254 78 78 GLU C C 168.285 0.40 1 255 78 78 GLU CA C 52.078 0.40 1 256 78 78 GLU N N 119.251 0.40 1 257 79 79 ARG H H 6.999 0.02 1 258 79 79 ARG C C 172.123 0.40 1 259 79 79 ARG CA C 51.074 0.40 1 260 79 79 ARG N N 118.991 0.40 1 261 80 80 HIS H H 8.355 0.02 1 262 80 80 HIS CA C 49.953 0.40 1 263 80 80 HIS N N 118.000 0.40 1 264 81 81 VAL C C 173.460 0.40 1 265 82 82 GLY H H 8.487 0.02 1 266 82 82 GLY C C 170.370 0.40 1 267 82 82 GLY CA C 42.688 0.40 1 268 82 82 GLY N N 97.322 0.40 1 269 83 83 ASP H H 7.127 0.02 1 270 83 83 ASP C C 168.737 0.40 1 271 83 83 ASP CA C 52.918 0.40 1 272 83 83 ASP N N 120.890 0.40 1 273 84 84 LEU H H 7.128 0.02 1 274 84 84 LEU C C 173.212 0.40 1 275 84 84 LEU CA C 50.433 0.40 1 276 84 84 LEU N N 120.154 0.40 1 277 85 85 GLY H H 8.260 0.02 1 278 85 85 GLY C C 167.654 0.40 1 279 85 85 GLY CA C 43.011 0.40 1 280 85 85 GLY N N 106.867 0.40 1 281 86 86 ASN H H 8.041 0.02 1 282 86 86 ASN C C 173.942 0.40 1 283 86 86 ASN CA C 49.266 0.40 1 284 86 86 ASN N N 117.454 0.40 1 285 87 87 VAL H H 8.960 0.02 1 286 87 87 VAL C C 171.526 0.40 1 287 87 87 VAL CA C 55.708 0.40 1 288 87 87 VAL N N 113.370 0.40 1 289 88 88 THR H H 8.681 0.02 1 290 88 88 THR C C 170.367 0.40 1 291 88 88 THR CA C 58.694 0.40 1 292 88 88 THR N N 117.939 0.40 1 293 89 89 ALA H H 9.377 0.02 1 294 89 89 ALA C C 174.480 0.40 1 295 89 89 ALA CA C 46.369 0.40 1 296 89 89 ALA N N 128.674 0.40 1 297 90 90 ASP H H 8.455 0.02 1 298 90 90 ASP C C 173.825 0.40 1 299 90 90 ASP CA C 49.347 0.40 1 300 90 90 ASP N N 124.235 0.40 1 301 91 91 LYS H H 8.231 0.02 1 302 91 91 LYS C C 174.101 0.40 1 303 91 91 LYS CA C 55.279 0.40 1 304 91 91 LYS N N 114.942 0.40 1 305 92 92 ASP H H 8.109 0.02 1 306 92 92 ASP C C 173.020 0.40 1 307 92 92 ASP CA C 51.127 0.40 1 308 92 92 ASP N N 119.251 0.40 1 309 93 93 GLY H H 8.405 0.02 1 310 93 93 GLY C C 169.706 0.40 1 311 93 93 GLY CA C 43.763 0.40 1 312 93 93 GLY N N 110.868 0.40 1 313 94 94 VAL H H 7.814 0.02 1 314 94 94 VAL C C 173.510 0.40 1 315 94 94 VAL CA C 58.185 0.40 1 316 94 94 VAL N N 118.755 0.40 1 317 95 95 ALA H H 9.763 0.02 1 318 95 95 ALA C C 171.635 0.40 1 319 95 95 ALA CA C 46.914 0.40 1 320 95 95 ALA N N 131.313 0.40 1 321 96 96 ASP H H 8.515 0.02 1 322 96 96 ASP C C 172.336 0.40 1 323 96 96 ASP N N 125.170 0.40 1 324 97 97 VAL H H 8.703 0.02 1 325 97 97 VAL C C 173.488 0.40 1 326 97 97 VAL CA C 58.243 0.40 1 327 97 97 VAL N N 125.879 0.40 1 328 98 98 SER H H 8.784 0.02 1 329 98 98 SER C C 169.715 0.40 1 330 98 98 SER CA C 55.068 0.40 1 331 98 98 SER N N 123.017 0.40 1 332 99 99 ILE H H 9.411 0.02 1 333 99 99 ILE C C 171.321 0.40 1 334 99 99 ILE CA C 57.155 0.40 1 335 99 99 ILE N N 125.807 0.40 1 336 100 100 GLU H H 8.652 0.02 1 337 100 100 GLU C C 172.098 0.40 1 338 100 100 GLU CA C 52.290 0.40 1 339 100 100 GLU N N 124.068 0.40 1 340 101 101 ASP H H 9.317 0.02 1 341 101 101 ASP C C 171.144 0.40 1 342 101 101 ASP CA C 51.419 0.40 1 343 101 101 ASP N N 126.109 0.40 1 344 102 102 SER H H 8.933 0.02 1 345 102 102 SER C C 171.596 0.40 1 346 102 102 SER CA C 55.245 0.40 1 347 102 102 SER N N 118.470 0.40 1 348 103 103 VAL H H 8.148 0.02 1 349 103 103 VAL CA C 61.450 0.40 1 350 103 103 VAL N N 123.179 0.40 1 351 104 104 ILE C C 169.576 0.40 1 352 104 104 ILE CA C 60.194 0.40 1 353 105 105 SER H H 6.988 0.02 1 354 105 105 SER C C 170.046 0.40 1 355 105 105 SER CA C 52.550 0.40 1 356 105 105 SER N N 107.618 0.40 1 357 106 106 LEU H H 8.313 0.02 1 358 106 106 LEU N N 120.137 0.40 1 359 107 107 SER C C 170.701 0.40 1 360 107 107 SER CA C 54.540 0.40 1 361 108 108 GLY H H 8.717 0.02 1 362 108 108 GLY C C 173.128 0.40 1 363 108 108 GLY CA C 41.287 0.40 1 364 108 108 GLY N N 107.603 0.40 1 365 109 109 ASP H H 9.019 0.02 1 366 109 109 ASP C C 171.904 0.40 1 367 109 109 ASP N N 120.664 0.40 1 368 110 110 HIS H H 9.283 0.02 1 369 110 110 HIS N N 116.324 0.40 1 370 111 111 SER H H 7.156 0.02 1 371 111 111 SER CA C 54.681 0.40 1 372 111 111 SER N N 110.225 0.40 1 373 112 112 ILE H H 7.837 0.02 1 374 112 112 ILE C C 171.419 0.40 1 375 112 112 ILE CA C 57.239 0.40 1 376 112 112 ILE N N 117.053 0.40 1 377 113 113 ILE H H 7.592 0.02 1 378 113 113 ILE C C 173.604 0.40 1 379 113 113 ILE CA C 58.318 0.40 1 380 113 113 ILE N N 121.032 0.40 1 381 114 114 GLY H H 9.575 0.02 1 382 114 114 GLY C C 169.739 0.40 1 383 114 114 GLY CA C 41.910 0.40 1 384 114 114 GLY N N 112.661 0.40 1 385 115 115 ARG H H 7.464 0.02 1 386 115 115 ARG C C 171.079 0.40 1 387 115 115 ARG CA C 51.663 0.40 1 388 115 115 ARG N N 118.398 0.40 1 389 116 116 THR H H 6.677 0.02 1 390 116 116 THR C C 169.821 0.40 1 391 116 116 THR CA C 59.633 0.40 1 392 116 116 THR N N 112.218 0.40 1 393 117 117 LEU H H 8.799 0.02 1 394 117 117 LEU C C 171.126 0.40 1 395 117 117 LEU CA C 50.415 0.40 1 396 117 117 LEU N N 129.477 0.40 1 397 118 118 VAL H H 8.906 0.02 1 398 118 118 VAL C C 170.267 0.40 1 399 118 118 VAL CA C 58.139 0.40 1 400 118 118 VAL N N 125.091 0.40 1 401 119 119 VAL H H 7.982 0.02 1 402 119 119 VAL C C 171.175 0.40 1 403 119 119 VAL CA C 55.271 0.40 1 404 119 119 VAL N N 120.716 0.40 1 405 120 120 HIS H H 8.935 0.02 1 406 120 120 HIS C C 172.599 0.40 1 407 120 120 HIS CA C 53.394 0.40 1 408 120 120 HIS N N 125.052 0.40 1 409 121 121 GLU H H 9.178 0.02 1 410 121 121 GLU C C 172.304 0.40 1 411 121 121 GLU CA C 56.090 0.40 1 412 121 121 GLU N N 121.453 0.40 1 413 122 122 LYS H H 8.478 0.02 1 414 122 122 LYS C C 171.523 0.40 1 415 122 122 LYS CA C 50.619 0.40 1 416 122 122 LYS N N 115.248 0.40 1 417 123 123 ALA H H 7.796 0.02 1 418 123 123 ALA C C 173.219 0.40 1 419 123 123 ALA CA C 48.850 0.40 1 420 123 123 ALA N N 120.866 0.40 1 421 124 124 ASP H H 10.165 0.02 1 422 124 124 ASP C C 174.458 0.40 1 423 124 124 ASP CA C 49.408 0.40 1 424 124 124 ASP N N 121.799 0.40 1 425 125 125 ASP H H 10.055 0.02 1 426 125 125 ASP C C 175.231 0.40 1 427 125 125 ASP CA C 50.939 0.40 1 428 125 125 ASP N N 129.369 0.40 1 429 126 126 LEU H H 10.483 0.02 1 430 126 126 LEU C C 173.964 0.40 1 431 126 126 LEU N N 117.190 0.40 1 432 127 127 GLY H H 8.637 0.02 1 433 127 127 GLY CA C 42.878 0.40 1 434 127 127 GLY N N 103.809 0.40 1 435 128 128 LYS H H 7.158 0.02 1 436 128 128 LYS CA C 51.740 0.40 1 437 128 128 LYS N N 118.290 0.40 1 438 129 129 GLY H H 8.913 0.02 1 439 129 129 GLY C C 171.524 0.40 1 440 129 129 GLY CA C 42.113 0.40 1 441 129 129 GLY N N 108.507 0.40 1 442 130 130 GLY H H 8.723 0.02 1 443 130 130 GLY C C 169.994 0.40 1 444 130 130 GLY CA C 42.419 0.40 1 445 130 130 GLY N N 108.537 0.40 1 446 131 131 ASN H H 7.152 0.02 1 447 131 131 ASN C C 172.236 0.40 1 448 131 131 ASN N N 111.951 0.40 1 449 132 132 GLU H H 8.935 0.02 1 450 132 132 GLU C C 171.084 0.40 1 451 132 132 GLU N N 120.461 0.40 1 452 133 133 GLU H H 8.775 0.02 1 453 133 133 GLU C C 176.239 0.40 1 454 133 133 GLU N N 120.137 0.40 1 455 134 134 SER H H 8.117 0.02 1 456 134 134 SER CA C 59.046 0.40 1 457 134 134 SER N N 114.981 0.40 1 458 135 135 THR H H 7.206 0.02 1 459 135 135 THR C C 172.804 0.40 1 460 135 135 THR CA C 60.029 0.40 1 461 135 135 THR N N 102.263 0.40 1 462 136 136 LYS H H 7.884 0.02 1 463 136 136 LYS N N 122.108 0.40 1 464 137 137 THR H H 8.630 0.02 1 465 137 137 THR N N 105.718 0.40 1 466 138 138 GLY H H 7.426 0.02 1 467 138 138 GLY CA C 42.483 0.40 1 468 138 138 GLY N N 111.372 0.40 1 469 139 139 ASN H H 7.545 0.02 1 470 139 139 ASN N N 107.496 0.40 1 471 140 140 ALA H H 6.368 0.02 1 472 140 140 ALA C C 173.571 0.40 1 473 140 140 ALA N N 114.542 0.40 1 474 141 141 GLY H H 8.271 0.02 1 475 141 141 GLY C C 173.542 0.40 1 476 141 141 GLY N N 105.287 0.40 1 477 142 142 SER H H 9.196 0.02 1 478 142 142 SER C C 170.188 0.40 1 479 142 142 SER N N 118.771 0.40 1 480 143 143 ARG H H 8.943 0.02 1 481 143 143 ARG C C 171.596 0.40 1 482 143 143 ARG N N 120.189 0.40 1 483 144 144 LEU H H 8.395 0.02 1 484 144 144 LEU C C 174.393 0.40 1 485 144 144 LEU CA C 53.375 0.40 1 486 144 144 LEU N N 122.907 0.40 1 487 145 145 ALA H H 7.356 0.02 1 488 145 145 ALA C C 171.752 0.40 1 489 145 145 ALA CA C 48.129 0.40 1 490 145 145 ALA N N 114.159 0.40 1 491 146 146 CYS H H 9.008 0.02 1 492 146 146 CYS C C 170.087 0.40 1 493 146 146 CYS CA C 51.077 0.40 1 494 146 146 CYS N N 110.738 0.40 1 495 147 147 GLY H H 8.018 0.02 1 496 147 147 GLY C C 167.909 0.40 1 497 147 147 GLY CA C 42.674 0.40 1 498 147 147 GLY N N 106.461 0.40 1 499 148 148 VAL H H 8.434 0.02 1 500 148 148 VAL C C 172.084 0.40 1 501 148 148 VAL CA C 59.635 0.40 1 502 148 148 VAL N N 124.054 0.40 1 503 149 149 ILE H H 8.613 0.02 1 504 149 149 ILE C C 171.804 0.40 1 505 149 149 ILE CA C 59.184 0.40 1 506 149 149 ILE N N 126.918 0.40 1 507 150 150 GLY H H 9.283 0.02 1 508 150 150 GLY C C 170.188 0.40 1 509 150 150 GLY CA C 40.120 0.40 1 510 150 150 GLY N N 116.493 0.40 1 511 151 151 ILE H H 8.943 0.02 1 512 151 151 ILE C C 172.231 0.40 1 513 151 151 ILE CA C 60.372 0.40 1 514 151 151 ILE N N 120.189 0.40 1 515 152 152 ALA H H 8.170 0.02 1 516 152 152 ALA CA C 46.772 0.40 1 517 152 152 ALA N N 129.719 0.40 1 stop_ save_