data_814 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Investigation of Copper-Zinc Superoxide Dismutase Ser-137 and Ala-137 Mutants ; _BMRB_accession_number 814 _BMRB_flat_file_name bmr814.str _Entry_type update _Submission_date 1995-07-31 _Accession_date 1996-04-12 _Entry_origination BMRB _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 Banci Lucia . . 2 Bertini Ivano . . 3 Cabelli Diane . . 4 Hallewell Robert A. . 5 Luchinat Claudio . . 6 Viezzoli Maria Silvia . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 15 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2010-06-11 revision BMRB 'Complete natural source information' 2008-09-30 revision BMRB 'Updating non-standard residue' 1999-06-14 revision BMRB 'Converted to BMRB NMR-STAR V 2.1 format' 1996-04-12 revision BMRB 'Error corrected in abrreviations given to non-polymers' 1996-03-25 reformat BMRB 'Converted to the BMRB 1996-03-01 STAR flat-file format' 1995-07-31 original BMRB 'Last release in original BMRB flat-file format' stop_ save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full ; Banci, Lucia, Bertini, Ivano, Cabelli, Diane, Hallewell, Robert A., Luchinat, Claudio, Viezzoli, Maria Silvia, "Investigation of Copper-Zinc Superoxide Dismutase Ser-137 and Ala-137 Mutants," Inorg. Chem. 29, 2398-2403 (1990). ; _Citation_title 'Investigation of Copper-Zinc Superoxide Dismutase Ser-137 and Ala-137 Mutants' _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 Banci Lucia . . 2 Bertini Ivano . . 3 Cabelli Diane . . 4 Hallewell Robert A. . 5 Luchinat Claudio . . 6 Viezzoli Maria Silvia . stop_ _Journal_abbreviation 'Inorg. Chem.' _Journal_volume 29 _Journal_issue . _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 2398 _Page_last 2403 _Year 1990 _Details . save_ ################################## # Molecular system description # ################################## save_system_copper-zinc_superoxide_dismutase _Saveframe_category molecular_system _Mol_system_name 'copper-zinc superoxide dismutase' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'copper-zinc superoxide dismutase' $copper-zinc_superoxide_dismutase stop_ _System_molecular_weight . _System_oligomer_state ? _System_paramagnetic ? _System_thiol_state . _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_copper-zinc_superoxide_dismutase _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'copper-zinc superoxide dismutase' _Name_variant I137 _Molecular_mass . _Mol_thiol_state . _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 153 _Mol_residue_sequence ; XTKAVAVLKGDGPVQGIINF EQKESNGPVKVWGSIKGLTE GLHGFHVHEFGDNTAGCTSA GPHFNPLSRKHGGPKDEERH VGDLGNVTADKDGVADVSIE DSVISLSGDHSIIGRTLVVH EKADDLGKGGNEESTKIGNA GSRLACGVIGIAQ ; loop_ _Residue_seq_code _Residue_label 1 AYA 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 ILE 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 2015-01-28 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 99.35 153 97.37 98.03 7.10e-99 BMRB 18509 Superoxide_dismutase_C6A-C111S_thermostable_mutant 99.35 153 99.34 99.34 7.86e-102 BMRB 18708 SUPEROXIDE_DISMUTASE_CU-ZN 99.35 153 99.34 99.34 7.86e-102 BMRB 4202 Q133M2_SOD 99.35 153 97.37 98.03 7.18e-99 BMRB 6821 dismutase 99.35 153 99.34 99.34 7.86e-102 BMRB 813 copper-zinc_superoxide_dismutase 99.35 153 99.34 99.34 9.89e-102 PDB 1AZV "Familial Als Mutant G37r Cuznsod (Human)" 99.35 153 97.37 97.37 3.73e-99 PDB 1BA9 "The Solution Structure Of Reduced Monomeric Superoxide Dismutase, Nmr, 36 Structures" 99.35 153 97.37 98.03 8.00e-99 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)" 99.35 153 98.68 99.34 3.22e-101 PDB 1HL4 "The Structure Of Apo Type Human Cu, Zn Superoxide Dismutase" 99.35 154 98.03 98.03 3.80e-100 PDB 1HL5 "The Structure Of Holo Type Human Cu, Zn Superoxide Dismutase" 99.35 153 98.03 98.03 3.68e-100 PDB 1KMG "The Solution Structure Of Monomeric Copper-Free Superoxide Dismutase" 99.35 153 97.37 98.03 7.18e-99 PDB 1L3N "The Solution Structure Of Reduced Dimeric Copper Zinc Sod: The Structural Effects Of Dimerization" 99.35 153 99.34 99.34 7.86e-102 PDB 1MFM "Monomeric Human Sod Mutant F50eG51EE133Q AT ATOMIC Resolution" 99.35 153 97.37 98.03 7.18e-99 PDB 1N18 "Thermostable Mutant Of Human Superoxide Dismutase, C6a, C111s" 99.35 154 99.34 99.34 7.29e-102 PDB 1N19 "Structure Of The Hsod A4v Mutant" 99.35 154 98.68 98.68 4.77e-101 PDB 1OEZ "Zn His46arg Mutant Of Human Cu, Zn Superoxide Dismutase" 99.35 153 97.37 97.37 2.71e-99 PDB 1OZT "Crystal Structure Of Apo-H46r Familial Als Mutant Human Cu, Zn Superoxide Dismutase (Cuznsod) To 2.5a Resolution" 99.35 153 97.37 97.37 2.71e-99 PDB 1OZU "Crystal Structure Of Familial Als Mutant S134n Of Human Cu, Zn Superoxide Dismutase (Cuznsod) To 1.3a Resolution" 99.35 153 97.37 98.03 1.11e-99 PDB 1P1V "Crystal Structure Of Fals-Associated Human Copper-Zinc Superoxide Dismutase (Cuznsod) Mutant D125h To 1.4a" 99.35 153 97.37 97.37 4.84e-99 PDB 1PTZ "Crystal Structure Of The Human Cu, Zn Superoxide Dismutase, Familial Amyotrophic Lateral Sclerosis (Fals) Mutant H43r" 99.35 153 98.68 98.68 8.51e-101 PDB 1PU0 "Structure Of Human Cu,Zn Superoxide Dismutase" 99.35 153 98.03 98.03 3.68e-100 PDB 1RK7 "Solution Structure Of Apo Cu,Zn Superoxide Dismutase: Role Of Metal Ions In Protein Folding" 99.35 153 97.37 98.03 7.18e-99 PDB 1SOS "Atomic Structures Of Wild-type And Thermostable Mutant Recombinant Human Cu, Zn Superoxide Dismutase" 99.35 154 99.34 99.34 8.13e-102 PDB 1SPD "Amyotrophic Lateral Sclerosis And Structural Defects In Cu,Zn Superoxide Dismutase" 99.35 154 98.03 98.03 3.80e-100 PDB 1UXL "I113t Mutant Of Human Sod1" 99.35 153 97.37 97.37 1.22e-99 PDB 1UXM "A4v Mutant Of Human Sod1" 99.35 153 97.37 97.37 1.54e-99 PDB 2AF2 "Solution Structure Of Disulfide Reduced And Copper Depleted Human Superoxide Dismutase" 99.35 153 99.34 99.34 7.86e-102 PDB 2C9S "1.24 Angstroms Resolution Structure Of Zn-Zn Human Superoxide Dismutase" 99.35 153 98.03 98.03 3.33e-100 PDB 2C9U "1.24 Angstroms Resolution Structure Of As-Isolated Cu-Zn Human Superoxide Dismutase" 99.35 153 98.03 98.03 3.68e-100 PDB 2C9V "Atomic Resolution Structure Of Cu-Zn Human Superoxide Dismutase" 99.35 153 98.03 98.03 3.68e-100 PDB 2GBT "C6aC111A CUZN SUPEROXIDE DISMUTASE" 99.35 153 98.68 99.34 2.10e-101 PDB 2GBU "C6a/c111a/c57a/c146a Apo Cuzn Superoxide Dismutase" 99.35 153 97.37 98.03 3.73e-99 PDB 2GBV "C6aC111AC57AC146A HOLO CUZN SUPEROXIDE DISMUTASE" 99.35 153 97.37 98.03 3.73e-99 PDB 2LU5 "Structure And Chemical Shifts Of Cu(I),Zn(Ii) Superoxide Dismutase By Solid-State Nmr" 99.35 153 99.34 99.34 7.86e-102 PDB 2R27 "Constitutively Zinc-Deficient Mutant Of Human Superoxide Dismutase (Sod), C6a, H80s, H83s, C111s" 99.35 154 98.03 98.03 5.40e-100 PDB 2V0A "Atomic Resolution Crystal Structure Of Human Superoxide Dismutase" 99.35 153 98.03 98.03 3.68e-100 PDB 2VR6 "Crystal Structure Of G85r Als Mutant Of Human Cu,Zn Superoxide Dismutase (Cuznsod) At 1.3 A Resolution" 99.35 153 97.37 97.37 3.73e-99 PDB 2VR7 "Crystal Structure Of G85r Als Mutant Of Human Cu,Zn Superoxide Dismutase (Cuznsod) At 1.58 A Resolution" 99.35 154 97.37 97.37 3.85e-99 PDB 2VR8 "Crystal Structure Of G85r Als Mutant Of Human Cu,Zn Superoxide Dismutase (Cuznsod) At 1.36 A Resolution" 99.35 154 97.37 97.37 3.06e-99 PDB 2WKO "Structure Of Metal Loaded Pathogenic Sod1 Mutant G93a" 99.35 154 97.37 97.37 1.40e-99 PDB 2WYT "1.0 A Resolution Structure Of L38v Sod1 Mutant" 99.35 153 97.37 98.03 1.17e-99 PDB 2WYZ "L38v Sod1 Mutant Complexed With Ump" 99.35 153 97.37 98.03 1.16e-99 PDB 2WZ0 "L38v Sod1 Mutant Complexed With Aniline." 99.35 153 97.37 98.03 1.17e-99 PDB 2WZ5 "L38v Sod1 Mutant Complexed With L-Methionine" 99.35 153 97.37 98.03 1.17e-99 PDB 2WZ6 "G93a Sod1 Mutant Complexed With Quinazoline" 99.35 153 97.37 97.37 1.41e-99 PDB 2XJK "Monomeric Human Cu,Zn Superoxide Dismutase" 99.35 153 97.37 98.03 7.10e-99 PDB 2ZKW "Crystal Structure Of Human Cu-Zn Superoxide Dismutase Mutant G85r In Space Group P21" 99.35 159 97.37 97.37 3.08e-99 PDB 2ZKX "Crystal Structure Of Human Cu-Zn Superoxide Dismutase Mutant G85r In Space Group I212121" 99.35 159 97.37 97.37 3.08e-99 PDB 2ZKY "Crystal Structure Of Human Cu-Zn Superoxide Dismutase Mutant G93a" 99.35 159 97.37 97.37 1.39e-99 PDB 3CQP "Human Sod1 G85r Variant, Structure I" 99.35 153 97.37 97.37 3.73e-99 PDB 3CQQ "Human Sod1 G85r Variant, Structure Ii" 99.35 153 97.37 97.37 2.96e-99 PDB 3ECU "Crystal Structure Of Human Apo Cu,Zn Superoxide Dismutase (Sod1)" 99.35 153 98.03 98.03 3.68e-100 PDB 3ECV "Crystal Structure Of The Als-Related Pathological Mutant I113t Of Human Apo Cu,Zn Superoxide Dismutase (Sod1)" 99.35 153 97.37 97.37 1.22e-99 PDB 3ECW "Crystal Structure Of The Als-Related Pathological Mutant T54r Of Human Apo Cu,Zn Superoxide Dismutase (Sod1)" 99.35 153 97.37 97.37 2.49e-99 PDB 3GZO "Human Sod1 G93a Variant" 99.35 154 97.37 97.37 1.46e-99 PDB 3GZP "Human Sod1 G93a Metal-Free Variant" 99.35 153 97.37 97.37 1.41e-99 PDB 3GZQ "Human Sod1 A4v Metal-Free Variant" 99.35 154 97.37 97.37 1.59e-99 PDB 3H2P "Human Sod1 D124v Variant" 99.35 153 97.37 97.37 5.77e-99 PDB 3H2Q "Human Sod1 H80r Variant, P21 Crystal Form" 99.35 153 97.37 97.37 2.71e-99 PDB 3KH3 "Crystal Structure Of Human CuZN SUPEROXIDE DISMUTASE RECOMBINANTLY Produced In Leishmania Tarantolae; P212121 Crystal Form Cont" 99.35 153 98.03 98.03 3.68e-100 PDB 3KH4 "Crystal Structure Of Human CuZN SUPEROXIDE DISMUTASE RECOMBINANTLY Produced In Leishmania Tarantolae; P6522 Crystal Form Contai" 99.35 153 98.03 98.03 3.68e-100 PDB 3QQD "Human Sod1 H80r Variant, P212121 Crystal Form" 99.35 154 97.37 97.37 2.63e-99 PDB 3RE0 "Crystal Structure Of Human Apo Cu,zn Superoxide Dismutase (sod1) Complexed With Cisplatin" 99.35 153 98.03 98.03 3.68e-100 PDB 3T5W "2me Modified Human Sod1" 99.35 153 98.03 98.03 3.33e-100 PDB 4A7G "Structure Of Human I113t Sod1 Mutant Complexed With 4- Methylpiperazin-1-yl)quinazoline In The P21 Space Group." 99.35 153 97.37 97.37 1.22e-99 PDB 4A7Q "Structure Of Human I113t Sod1 Mutant Complexed With 4-(4- Methyl-1,4-diazepan-1-yl)quinazoline In The P21 Space Group." 99.35 153 97.37 97.37 1.22e-99 PDB 4A7S "Structure Of Human I113t Sod1 Mutant Complexed With 5- Fluorouridine In The P21 Space Group" 99.35 153 97.37 97.37 1.22e-99 PDB 4A7T "Structure Of Human I113t Sod1 Mutant Complexed With Isoproteranol In The P21 Space Group" 99.35 153 97.37 97.37 1.22e-99 PDB 4A7U "Structure Of Human I113t Sod1 Complexed With Adrenaline In The P21 Space Group." 99.35 153 97.37 97.37 1.22e-99 PDB 4A7V "Structure Of Human I113t Sod1 Mutant Complexed With Dopamine In The P21 Space Group" 99.35 153 97.37 97.37 1.22e-99 PDB 4B3E "Structure Of Copper-Zinc Superoxide Dismutase Complexed With Bicarbonate." 99.35 154 98.03 98.03 2.51e-100 PDB 4FF9 "Crystal Structure Of Cysteinylated Wt Sod1" 99.35 153 98.03 98.03 3.68e-100 PDB 4MCM "Human Sod1 C57s Mutant, As-isolated" 99.35 153 97.37 97.37 9.96e-99 PDB 4MCN "Human Sod1 C57s Mutant, Metal-free" 99.35 153 97.37 97.37 9.96e-99 PDB 4OH2 "Crystal Structure Of Cu/zn Superoxide Dismutase I149t" 99.35 153 98.68 98.68 3.71e-101 DBJ BAA14373 "unnamed protein product [Schizosaccharomyces pombe]" 98.04 179 98.00 98.00 1.24e-98 DBJ BAC20345 "Cu,Zn-superoxide dismutase [Pan troglodytes]" 99.35 154 98.03 98.03 2.51e-100 DBJ BAG35052 "unnamed protein product [Homo sapiens]" 99.35 154 98.03 98.03 2.51e-100 DBJ BAG73767 "superoxide dismutase 1, soluble [synthetic construct]" 99.35 154 98.03 98.03 2.51e-100 EMBL CAA26182 "unnamed protein product [Homo sapiens]" 99.35 154 98.03 98.03 2.51e-100 EMBL CAG29351 "SOD1 [Homo sapiens]" 99.35 154 98.03 98.03 2.51e-100 EMBL CAG46542 "SOD1 [Homo sapiens]" 99.35 154 98.03 98.03 2.51e-100 GB AAA72747 "CuZn superoxide dismutase [synthetic construct]" 99.35 154 99.34 99.34 7.29e-102 GB AAA80237 "HSOD-GlyProGly-A+, partial [synthetic construct]" 99.35 171 99.34 99.34 2.72e-101 GB AAB05661 "Cu/Zn-superoxide dismutase [Homo sapiens]" 99.35 154 98.03 98.03 2.51e-100 GB AAB05662 "Cu/Zn-superoxide dismutase [Homo sapiens]" 99.35 154 97.37 97.37 3.31e-99 GB AAB27818 "Cu,Zn superoxide dismutase, SOD=SOD1 gene product {A to V single-site mutation} [human, Peptide Mutant, 153 aa]" 99.35 153 97.37 97.37 1.54e-99 REF NP_000445 "superoxide dismutase [Cu-Zn] [Homo sapiens]" 99.35 154 98.03 98.03 2.51e-100 REF NP_001009025 "superoxide dismutase [Cu-Zn] [Pan troglodytes]" 99.35 154 98.03 98.03 2.51e-100 REF XP_003813274 "PREDICTED: superoxide dismutase [Cu-Zn] [Pan paniscus]" 99.35 154 98.03 98.03 2.51e-100 REF XP_004062735 "PREDICTED: superoxide dismutase [Cu-Zn] [Gorilla gorilla gorilla]" 99.35 154 97.37 97.37 2.18e-99 REF XP_004062736 "PREDICTED: superoxide dismutase [Cu-Zn] [Gorilla gorilla gorilla]" 99.35 154 97.37 97.37 2.18e-99 SP P00441 "RecName: Full=Superoxide dismutase [Cu-Zn]; AltName: Full=Superoxide dismutase 1; Short=hSod1 [Homo sapiens]" 99.35 154 98.03 98.03 2.51e-100 SP P60052 "RecName: Full=Superoxide dismutase [Pan troglodytes]" 99.35 154 98.03 98.03 2.51e-100 stop_ save_ ###################### # Polymer residues # ###################### save_chem_comp_AYA _Saveframe_category polymer_residue _Mol_type 'L-PEPTIDE LINKING' _Name_common N-ACETYLALANINE _BMRB_code AYA _PDB_code AYA _Standard_residue_derivative . _Molecular_mass 131.130 _Mol_paramagnetic . _Details . loop_ _Atom_name _PDB_atom_name _Atom_type _Atom_chirality _Atom_charge _Atom_oxidation_number _Atom_unpaired_electrons N N N . 0 . ? CA CA C . 0 . ? CB CB C . 0 . ? C C C . 0 . ? O O O . 0 . ? OXT OXT O . 0 . ? CT CT C . 0 . ? OT OT O . 0 . ? CM CM C . 0 . ? H H H . 0 . ? HA HA H . 0 . ? HB1 HB1 H . 0 . ? HB2 HB2 H . 0 . ? HB3 HB3 H . 0 . ? HXT HXT H . 0 . ? HM1 HM1 H . 0 . ? HM2 HM2 H . 0 . ? HM3 HM3 H . 0 . ? stop_ loop_ _Bond_order _Bond_atom_one_atom_name _Bond_atom_two_atom_name _PDB_bond_atom_one_atom_name _PDB_bond_atom_two_atom_name SING N CA ? ? SING N CT ? ? SING N H ? ? SING CA CB ? ? SING CA C ? ? SING CA HA ? ? SING CB HB1 ? ? SING CB HB2 ? ? SING CB HB3 ? ? DOUB C O ? ? SING C OXT ? ? SING OXT HXT ? ? DOUB CT OT ? ? SING CT CM ? ? SING CM HM1 ? ? SING CM HM2 ? ? SING CM HM3 ? ? stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species _Strain $copper-zinc_superoxide_dismutase human 9606 Eukaryota Metazoa Homo sapiens generic 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 $copper-zinc_superoxide_dismutase 'not available' yeast Saccharomyces cerevisiae 2150-2-3 . stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_one _Saveframe_category sample _Sample_type solution _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_list _Saveframe_category NMR_spectrometer _Manufacturer unknown _Model unknown _Field_strength 0 _Details 'spectrometer information not available' save_ ############################# # NMR applied experiments # ############################# save__1 _Saveframe_category NMR_applied_experiment _Sample_label $sample_one save_ ####################### # Sample conditions # ####################### save_sample_condition_set_one _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 5.3 . na temperature 300 . K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chem_shift_reference_par_set_one _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_citation_label _Correction_value_citation_label TMS H . . ppm 0 . . . . . $entry_citation $entry_citation 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_chemical_shift_assignment_data_set_one _Saveframe_category assigned_chemical_shifts _Details . loop_ _Sample_label $sample_one stop_ _Sample_conditions_label $sample_condition_set_one _Chem_shift_reference_set_label $chem_shift_reference_par_set_one _Mol_system_component_name 'copper-zinc superoxide dismutase' _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 . 46 HIS HB2 H 16.7 . 1 2 . 46 HIS HD2 H 47.7 . 1 3 . 46 HIS HE1 H 20.2 . 1 4 . 46 HIS HE2 H 48.8 . 1 5 . 48 HIS HD1 H 38.5 . 1 6 . 48 HIS HD2 H 37.9 . 1 7 . 48 HIS HE1 H 22.4 . 1 8 . 63 HIS HD2 H 64.7 . 1 9 . 71 HIS HD2 H 50.2 . 1 10 . 80 HIS HD2 H 47.7 . 1 11 . 83 ASP HB2 H 36.5 . 1 12 . 83 ASP HB3 H 36.5 . 1 13 . 120 HIS HD1 H 57.6 . 1 14 . 120 HIS HD2 H 23.8 . 1 15 . 120 HIS HE1 H 43.8 . 1 stop_ save_