data_26570 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Backbone and sidechain 1H, 13C and 15N chemical shifts for human superoxide dismutase (hSOD1) lacking bound metal and the intrasubunit disulfide bond ; _BMRB_accession_number 26570 _BMRB_flat_file_name bmr26570.str _Entry_type original _Submission_date 2015-05-04 _Accession_date 2015-05-04 _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 Kay Lewis E. . 2 Sekhar Ashok . . 3 Rumfeldt Jessica A.O. . 4 Broom Helen R. . 5 Doyle Colleen M. . 6 Meiering Elizabeth M. . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 673 "13C chemical shifts" 546 "15N chemical shifts" 136 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2015-06-26 update author 'update entry citation' 2015-06-08 original author 'original release' stop_ _Original_release_date 2015-06-08 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; Thermal Fluctuations of Immature SOD1 Lead to Separate Folding and Misfolding Pathways ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 26099300 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Sekhar Ashok . . 2 Rumfeldt Jessica A.O. . 3 Broom Helen R. . 4 Doyle Colleen M. . 5 Meiering Elizabeth M. . 6 Kay Lewis E. . stop_ _Journal_abbreviation ELife _Journal_volume 4 _Journal_issue . _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first e07296 _Page_last e07296 _Year 2015 _Details . loop_ _Keyword SOD1 'aberrant oligomerization' misfolding 'superoxide dismutase' 'transiently populated conformations' stop_ save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name 'SOD1 monomer' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'SOD1 monomer' $SOD1 stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state ? _System_paramagnetic no _System_thiol_state . _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_SOD1 _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common SOD1 _Molecular_mass . _Mol_thiol_state 'all free' _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 2015-08-05 loop_ _Database_name _Database_accession_code _Database_entry_mol_name _Sequence_query_to_submitted_percentage _Sequence_subject_length _Sequence_identity _Sequence_positive _Sequence_homology_expectation_value BMRB 15711 SOD1 100.00 153 98.04 98.69 1.85e-100 BMRB 15712 SOD1 100.00 153 97.39 98.04 1.21e-99 BMRB 15713 SOD1 100.00 153 97.39 98.04 2.13e-99 BMRB 15714 SOD1 100.00 153 97.39 98.04 2.20e-99 BMRB 18509 Superoxide_dismutase_C6A-C111S_thermostable_mutant 100.00 153 100.00 100.00 3.73e-103 BMRB 18708 SUPEROXIDE_DISMUTASE_CU-ZN 100.00 153 100.00 100.00 3.73e-103 BMRB 18968 SOD1 100.00 153 98.04 98.69 1.85e-100 BMRB 19962 L126Z-sod1 81.70 125 98.40 98.40 5.20e-81 BMRB 4202 "Superoxide Dismutase" 100.00 153 98.04 98.69 2.17e-100 PDB 1AZV "Familial Als Mutant G37r Cuznsod (Human)" 100.00 153 98.04 98.04 1.19e-100 PDB 1BA9 "The Solution Structure Of Reduced Monomeric Superoxide Dismutase, Nmr, 36 Structures" 99.35 153 98.03 98.68 1.00e-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 4.59e-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 1.23e-102 PDB 1HL4 "The Structure Of Apo Type Human Cu, Zn Superoxide Dismutase" 100.00 154 98.69 98.69 1.11e-101 PDB 1HL5 "The Structure Of Holo Type Human Cu, Zn Superoxide Dismutase" 100.00 153 98.69 98.69 1.08e-101 PDB 1KMG "The Solution Structure Of Monomeric Copper-Free Superoxide Dismutase" 100.00 153 98.04 98.69 2.17e-100 PDB 1L3N "The Solution Structure Of Reduced Dimeric Copper Zinc Sod: The Structural Effects Of Dimerization" 100.00 153 100.00 100.00 3.73e-103 PDB 1MFM "Monomeric Human Sod Mutant F50eG51EE133Q AT ATOMIC Resolution" 100.00 153 98.04 98.69 2.17e-100 PDB 1N18 "Thermostable Mutant Of Human Superoxide Dismutase, C6a, C111s" 100.00 154 100.00 100.00 2.96e-103 PDB 1N19 "Structure Of The Hsod A4v Mutant" 100.00 154 99.35 99.35 1.24e-102 PDB 1OEZ "Zn His46arg Mutant Of Human Cu, Zn Superoxide Dismutase" 100.00 153 98.04 98.04 9.79e-101 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 9.79e-101 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 3.79e-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 1.47e-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 2.63e-102 PDB 1PU0 "Structure Of Human Cu,Zn Superoxide Dismutase" 100.00 153 98.69 98.69 1.08e-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 2.17e-100 PDB 1SOS "Atomic Structures Of Wild-type And Thermostable Mutant Recombinant Human Cu, Zn Superoxide Dismutase" 100.00 154 100.00 100.00 3.85e-103 PDB 1SPD "Amyotrophic Lateral Sclerosis And Structural Defects In Cu,Zn Superoxide Dismutase" 100.00 154 98.69 98.69 1.11e-101 PDB 1UXL "I113t Mutant Of Human Sod1" 100.00 153 98.04 98.04 5.67e-101 PDB 1UXM "A4v Mutant Of Human Sod1" 100.00 153 98.04 98.04 5.08e-101 PDB 2AF2 "Solution Structure Of Disulfide Reduced And Copper Depleted Human Superoxide Dismutase" 100.00 153 100.00 100.00 3.73e-103 PDB 2C9S "1.24 Angstroms Resolution Structure Of Zn-Zn Human Superoxide Dismutase" 100.00 153 98.69 98.69 1.03e-101 PDB 2C9U "1.24 Angstroms Resolution Structure Of As-Isolated Cu-Zn Human Superoxide Dismutase" 100.00 153 98.69 98.69 1.08e-101 PDB 2C9V "Atomic Resolution Structure Of Cu-Zn Human Superoxide Dismutase" 100.00 153 98.69 98.69 1.08e-101 PDB 2GBT "C6aC111A CUZN SUPEROXIDE DISMUTASE" 100.00 153 99.35 100.00 8.73e-103 PDB 2GBU "C6a/c111a/c57a/c146a Apo Cuzn Superoxide Dismutase" 100.00 153 98.04 98.69 1.07e-100 PDB 2GBV "C6aC111AC57AC146A HOLO CUZN SUPEROXIDE DISMUTASE" 100.00 153 98.04 98.69 1.07e-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 3.73e-103 PDB 2MP3 "Truncated L126z-sod1 In Dpc Micelle" 81.70 132 98.40 98.40 1.54e-80 PDB 2NNX "Crystal Structure Of The H46r, H48q Double Mutant Of Human [cu-Zn] Superoxide Dismutase" 100.00 154 97.39 97.39 6.14e-100 PDB 2R27 "Constitutively Zinc-Deficient Mutant Of Human Superoxide Dismutase (Sod), C6a, H80s, H83s, C111s" 100.00 154 98.69 98.69 1.31e-101 PDB 2V0A "Atomic Resolution Crystal Structure Of Human Superoxide Dismutase" 100.00 153 98.69 98.69 1.08e-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 1.19e-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 1.23e-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 1.19e-100 PDB 2WKO "Structure Of Metal Loaded Pathogenic Sod1 Mutant G93a" 100.00 154 98.04 98.04 4.32e-101 PDB 2WYT "1.0 A Resolution Structure Of L38v Sod1 Mutant" 100.00 153 98.04 98.69 3.55e-101 PDB 2WYZ "L38v Sod1 Mutant Complexed With Ump" 100.00 153 98.04 98.69 3.79e-101 PDB 2WZ0 "L38v Sod1 Mutant Complexed With Aniline." 100.00 153 98.04 98.69 3.55e-101 PDB 2WZ5 "L38v Sod1 Mutant Complexed With L-Methionine" 100.00 153 98.04 98.69 3.55e-101 PDB 2WZ6 "G93a Sod1 Mutant Complexed With Quinazoline" 100.00 153 98.04 98.04 4.18e-101 PDB 2XJK "Monomeric Human Cu,Zn Superoxide Dismutase" 100.00 153 98.04 98.69 1.85e-100 PDB 2ZKW "Crystal Structure Of Human Cu-Zn Superoxide Dismutase Mutant G85r In Space Group P21" 100.00 159 98.04 98.04 1.12e-100 PDB 2ZKX "Crystal Structure Of Human Cu-Zn Superoxide Dismutase Mutant G85r In Space Group I212121" 100.00 159 98.04 98.04 1.12e-100 PDB 2ZKY "Crystal Structure Of Human Cu-Zn Superoxide Dismutase Mutant G93a" 100.00 159 98.04 98.04 3.98e-101 PDB 3CQP "Human Sod1 G85r Variant, Structure I" 100.00 153 98.04 98.04 1.19e-100 PDB 3CQQ "Human Sod1 G85r Variant, Structure Ii" 100.00 153 98.04 98.04 1.15e-100 PDB 3ECU "Crystal Structure Of Human Apo Cu,Zn Superoxide Dismutase (Sod1)" 100.00 153 98.69 98.69 1.08e-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 5.67e-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 8.88e-101 PDB 3GQF "Structural And Biophysical Properties Of The Pathogenic Sod1 Variant H46rH48Q" 100.00 153 97.39 97.39 5.94e-100 PDB 3GZO "Human Sod1 G93a Variant" 100.00 154 98.04 98.04 4.32e-101 PDB 3GZP "Human Sod1 G93a Metal-Free Variant" 100.00 153 98.04 98.04 4.18e-101 PDB 3GZQ "Human Sod1 A4v Metal-Free Variant" 100.00 154 98.04 98.04 5.26e-101 PDB 3H2P "Human Sod1 D124v Variant" 100.00 153 98.04 98.04 1.62e-100 PDB 3H2Q "Human Sod1 H80r Variant, P21 Crystal Form" 100.00 153 98.04 98.04 9.79e-101 PDB 3K91 "Polysulfane Bridge In Cu-Zn Superoxide Dismutase" 100.00 153 97.39 97.39 5.94e-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 1.08e-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 1.08e-101 PDB 3QQD "Human Sod1 H80r Variant, P212121 Crystal Form" 100.00 154 98.04 98.04 1.09e-100 PDB 3RE0 "Crystal Structure Of Human Apo Cu,zn Superoxide Dismutase (sod1) Complexed With Cisplatin" 100.00 153 98.69 98.69 1.08e-101 PDB 3T5W "2me Modified Human Sod1" 100.00 153 98.69 98.69 1.03e-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 5.67e-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 5.67e-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 5.67e-101 PDB 4A7T "Structure Of Human I113t Sod1 Mutant Complexed With Isoproteranol In The P21 Space Group" 100.00 153 98.04 98.04 5.67e-101 PDB 4A7U "Structure Of Human I113t Sod1 Complexed With Adrenaline In The P21 Space Group." 100.00 153 98.04 98.04 5.67e-101 PDB 4A7V "Structure Of Human I113t Sod1 Mutant Complexed With Dopamine In The P21 Space Group" 100.00 153 98.04 98.04 5.67e-101 PDB 4B3E "Structure Of Copper-Zinc Superoxide Dismutase Complexed With Bicarbonate." 100.00 154 98.69 98.69 8.30e-102 PDB 4BCY "Monomeric Human Cu,zn Superoxide Dismutase, Mutation H43f" 100.00 153 97.39 98.04 3.52e-99 PDB 4FF9 "Crystal Structure Of Cysteinylated Wt Sod1" 100.00 153 98.69 98.69 1.08e-101 PDB 4MCM "Human Sod1 C57s Mutant, As-isolated" 100.00 153 98.04 98.04 2.79e-100 PDB 4MCN "Human Sod1 C57s Mutant, Metal-free" 100.00 153 98.04 98.04 2.79e-100 PDB 4OH2 "Crystal Structure Of Cu/zn Superoxide Dismutase I149t" 100.00 153 99.35 99.35 1.48e-102 DBJ BAA14373 "unnamed protein product [Schizosaccharomyces pombe]" 98.69 179 98.68 98.68 4.16e-100 DBJ BAC20345 "Cu,Zn-superoxide dismutase [Pan troglodytes]" 100.00 154 98.69 98.69 8.30e-102 DBJ BAG35052 "unnamed protein product [Homo sapiens]" 100.00 154 98.69 98.69 8.30e-102 DBJ BAG73767 "superoxide dismutase 1, soluble [synthetic construct]" 100.00 154 98.69 98.69 8.30e-102 EMBL CAA26182 "unnamed protein product [Homo sapiens]" 100.00 154 98.69 98.69 8.30e-102 EMBL CAG29351 "SOD1 [Homo sapiens]" 100.00 154 98.69 98.69 8.30e-102 EMBL CAG46542 "SOD1 [Homo sapiens]" 100.00 154 98.69 98.69 8.30e-102 GB AAA72747 "CuZn superoxide dismutase [synthetic construct]" 100.00 154 100.00 100.00 2.96e-103 GB AAA80237 "HSOD-GlyProGly-A+, partial [synthetic construct]" 100.00 171 100.00 100.00 1.08e-102 GB AAB05661 "Cu/Zn-superoxide dismutase [Homo sapiens]" 100.00 154 98.69 98.69 8.30e-102 GB AAB05662 "Cu/Zn-superoxide dismutase [Homo sapiens]" 100.00 154 98.04 98.04 1.29e-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 5.08e-101 REF NP_000445 "superoxide dismutase [Cu-Zn] [Homo sapiens]" 100.00 154 98.69 98.69 8.30e-102 REF NP_001009025 "superoxide dismutase [Cu-Zn] [Pan troglodytes]" 100.00 154 98.69 98.69 8.30e-102 REF XP_003813274 "PREDICTED: superoxide dismutase [Cu-Zn] [Pan paniscus]" 100.00 154 98.69 98.69 8.30e-102 REF XP_004062735 "PREDICTED: superoxide dismutase [Cu-Zn] [Gorilla gorilla gorilla]" 100.00 154 98.04 98.04 7.96e-101 REF XP_004062736 "PREDICTED: superoxide dismutase [Cu-Zn] [Gorilla gorilla gorilla]" 100.00 154 98.04 98.04 7.96e-101 SP P00441 "RecName: Full=Superoxide dismutase [Cu-Zn]; AltName: Full=Superoxide dismutase 1; Short=hSod1" 100.00 154 98.69 98.69 8.30e-102 SP P60052 "RecName: Full=Superoxide dismutase [Cu-Zn]" 100.00 154 98.69 98.69 8.30e-102 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species _Details $SOD1 Human 9606 Eukaryota Metazoa Homo sapiens 'human SOD1 overexpressed and purified from 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 $SOD1 'recombinant technology' . Escherichia coli . pHSOD1ASlacIq stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $SOD1 1.5 mM '[U-99% 13C; U-99% 15N]' HEPES 20 mM 'natural abundance' NaN3 1 mM 'natural abundance' TCEP 1 mM 'natural abundance' stop_ save_ ############################ # Computer software used # ############################ save_SPARKY _Saveframe_category software _Name SPARKY _Version . loop_ _Vendor _Address _Electronic_address Goddard . . stop_ loop_ _Task 'chemical shift assignment' stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model INOVA _Field_strength 800 _Details . save_ save_spectrometer_2 _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model INOVA _Field_strength 600 _Details . save_ ############################# # NMR applied experiments # ############################# save_2D_1H-15N_HSQC_1 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-15N HSQC' _Sample_label $sample_1 save_ save_3D_HNCACB_2 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCACB' _Sample_label $sample_1 save_ save_3D_HNCO_3 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCO' _Sample_label $sample_1 save_ save_3D_CBCA(CO)NH_4 _Saveframe_category NMR_applied_experiment _Experiment_name '3D CBCA(CO)NH' _Sample_label $sample_1 save_ save_3D_HBHA(CO)NH_5 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HBHA(CO)NH' _Sample_label $sample_1 save_ save_3D_C(CO)NH_6 _Saveframe_category NMR_applied_experiment _Experiment_name '3D C(CO)NH' _Sample_label $sample_1 save_ save_3D_H(CCO)NH_7 _Saveframe_category NMR_applied_experiment _Experiment_name '3D H(CCO)NH' _Sample_label $sample_1 save_ ####################### # Sample conditions # ####################### save_sample_conditions_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units 'ionic strength' 0.02 . M pH 7.4 . pH pressure 1 . atm temperature 298 . K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference_1 _Saveframe_category chemical_shift_reference _Details '1H chemical shifts were referenced to water and indirect chemical shift referencing was used for 13C and 15N.' 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 water C 13 protons ppm 4.773 internal indirect . . . 0.2514953 water H 1 protons ppm 4.773 internal direct . . . 1.0 water N 15 protons ppm 4.773 internal indirect . . . 0.101329118 stop_ save_ ################################### # Assigned chemical shift lists # ################################### ################################################################### # Chemical Shift Ambiguity Index Value Definitions # # # # The values other than 1 are used for those atoms with different # # chemical shifts that cannot be assigned to stereospecific atoms # # or to specific residues or chains. # # # # Index Value Definition # # # # 1 Unique (including isolated methyl protons, # # geminal atoms, and geminal methyl # # groups with identical chemical shifts) # # (e.g. ILE HD11, HD12, HD13 protons) # # 2 Ambiguity of geminal atoms or geminal methyl # # proton groups (e.g. ASP HB2 and HB3 # # protons, LEU CD1 and CD2 carbons, or # # LEU HD11, HD12, HD13 and HD21, HD22, # # HD23 methyl protons) # # 3 Aromatic atoms on opposite sides of # # symmetrical rings (e.g. TYR HE1 and HE2 # # protons) # # 4 Intraresidue ambiguities (e.g. LYS HG and # # HD protons or TRP HZ2 and HZ3 protons) # # 5 Interresidue ambiguities (LYS 12 vs. LYS 27) # # 6 Intermolecular ambiguities (e.g. ASP 31 CA # # in monomer 1 and ASP 31 CA in monomer 2 # # of an asymmetrical homodimer, duplex # # DNA assignments, or other assignments # # that may apply to atoms in one or more # # molecule in the molecular assembly) # # 9 Ambiguous, specific ambiguity not defined # # # ################################################################### save_assigned_chem_shift_list_1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Experiment_label '2D 1H-15N HSQC' '3D HNCACB' '3D HNCO' '3D CBCA(CO)NH' '3D HBHA(CO)NH' '3D C(CO)NH' '3D H(CCO)NH' stop_ loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $sample_conditions_1 _Chem_shift_reference_set_label $chemical_shift_reference_1 _Mol_system_component_name 'SOD1 monomer' _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 4.294 . 1 2 1 1 ALA HB H 1.543 . 1 3 1 1 ALA C C 173.835 . 1 4 1 1 ALA CA C 51.964 . 1 5 1 1 ALA CB C 20.380 . 1 6 2 2 THR H H 8.513 . 1 7 2 2 THR HA H 4.558 . 1 8 2 2 THR HB H 3.949 . 1 9 2 2 THR HG2 H 1.262 . 1 10 2 2 THR C C 172.337 . 1 11 2 2 THR CA C 62.618 . 1 12 2 2 THR CB C 70.355 . 1 13 2 2 THR CG2 C 22.778 . 1 14 2 2 THR N N 116.176 . 1 15 3 3 LYS H H 8.727 . 1 16 3 3 LYS HA H 5.331 . 1 17 3 3 LYS HB2 H 1.765 . 2 18 3 3 LYS HB3 H 1.983 . 2 19 3 3 LYS HG2 H 1.482 . 2 20 3 3 LYS HG3 H 1.482 . 2 21 3 3 LYS HD2 H 1.735 . 2 22 3 3 LYS HD3 H 1.735 . 2 23 3 3 LYS HE2 H 2.956 . 2 24 3 3 LYS HE3 H 2.956 . 2 25 3 3 LYS C C 174.444 . 1 26 3 3 LYS CA C 54.990 . 1 27 3 3 LYS CB C 36.578 . 1 28 3 3 LYS CG C 25.508 . 1 29 3 3 LYS CD C 29.634 . 1 30 3 3 LYS CE C 42.069 . 1 31 3 3 LYS N N 126.078 . 1 32 4 4 ALA H H 9.143 . 1 33 4 4 ALA HA H 5.264 . 1 34 4 4 ALA HB H 1.046 . 1 35 4 4 ALA C C 175.209 . 1 36 4 4 ALA CA C 50.654 . 1 37 4 4 ALA CB C 23.750 . 1 38 4 4 ALA N N 123.024 . 1 39 5 5 VAL H H 9.448 . 1 40 5 5 VAL HA H 5.347 . 1 41 5 5 VAL HB H 1.980 . 1 42 5 5 VAL HG1 H 0.824 . 2 43 5 5 VAL HG2 H 0.824 . 2 44 5 5 VAL C C 173.113 . 1 45 5 5 VAL CA C 60.387 . 1 46 5 5 VAL CB C 36.440 . 1 47 5 5 VAL CG1 C 19.827 . 2 48 5 5 VAL CG2 C 21.886 . 2 49 5 5 VAL N N 120.773 . 1 50 6 6 ALA H H 9.393 . 1 51 6 6 ALA HA H 4.916 . 1 52 6 6 ALA HB H 1.127 . 1 53 6 6 ALA C C 174.483 . 1 54 6 6 ALA CA C 50.927 . 1 55 6 6 ALA CB C 23.606 . 1 56 6 6 ALA N N 128.976 . 1 57 7 7 VAL H H 9.212 . 1 58 7 7 VAL HA H 4.288 . 1 59 7 7 VAL HB H 2.033 . 1 60 7 7 VAL HG1 H 0.918 . 2 61 7 7 VAL HG2 H 0.918 . 2 62 7 7 VAL C C 175.651 . 1 63 7 7 VAL CA C 61.976 . 1 64 7 7 VAL CB C 31.785 . 1 65 7 7 VAL CG1 C 21.161 . 2 66 7 7 VAL CG2 C 21.161 . 2 67 7 7 VAL N N 125.247 . 1 68 8 8 LEU H H 8.741 . 1 69 8 8 LEU HA H 4.261 . 1 70 8 8 LEU HB2 H 1.493 . 2 71 8 8 LEU HB3 H 0.878 . 2 72 8 8 LEU HG H 1.395 . 1 73 8 8 LEU HD1 H 0.549 . 2 74 8 8 LEU C C 175.967 . 1 75 8 8 LEU CA C 54.120 . 1 76 8 8 LEU CB C 42.902 . 1 77 8 8 LEU CG C 27.064 . 1 78 8 8 LEU CD1 C 23.718 . 2 79 8 8 LEU CD2 C 26.758 . 2 80 8 8 LEU N N 126.437 . 1 81 9 9 LYS H H 8.308 . 1 82 9 9 LYS HA H 4.840 . 1 83 9 9 LYS HB2 H 2.034 . 2 84 9 9 LYS HB3 H 1.891 . 2 85 9 9 LYS HG2 H 1.502 . 2 86 9 9 LYS HG3 H 1.502 . 2 87 9 9 LYS HD2 H 1.735 . 2 88 9 9 LYS HD3 H 1.843 . 2 89 9 9 LYS HE2 H 3.006 . 2 90 9 9 LYS HE3 H 3.006 . 2 91 9 9 LYS C C 175.475 . 1 92 9 9 LYS CA C 55.277 . 1 93 9 9 LYS CB C 36.466 . 1 94 9 9 LYS CG C 24.504 . 1 95 9 9 LYS CD C 29.269 . 1 96 9 9 LYS CE C 42.238 . 1 97 9 9 LYS N N 121.390 . 1 98 10 10 GLY H H 8.715 . 1 99 10 10 GLY HA2 H 4.118 . 2 100 10 10 GLY HA3 H 4.542 . 2 101 10 10 GLY C C 172.589 . 1 102 10 10 GLY CA C 45.409 . 1 103 10 10 GLY N N 112.647 . 1 104 11 11 ASP H H 8.744 . 1 105 11 11 ASP HA H 4.732 . 1 106 11 11 ASP HB2 H 2.761 . 2 107 11 11 ASP HB3 H 2.563 . 2 108 11 11 ASP C C 176.685 . 1 109 11 11 ASP CA C 54.702 . 1 110 11 11 ASP CB C 41.017 . 1 111 11 11 ASP N N 121.075 . 1 112 12 12 GLY H H 8.112 . 1 113 12 12 GLY C C 173.486 . 1 114 12 12 GLY CA C 44.387 . 1 115 12 12 GLY N N 110.318 . 1 116 13 13 PRO HA H 4.514 . 1 117 13 13 PRO HB2 H 2.135 . 2 118 13 13 PRO HB3 H 2.135 . 2 119 13 13 PRO HG2 H 2.008 . 2 120 13 13 PRO HG3 H 2.052 . 2 121 13 13 PRO HD2 H 3.574 . 2 122 13 13 PRO HD3 H 3.835 . 2 123 13 13 PRO C C 176.572 . 1 124 13 13 PRO CA C 63.446 . 1 125 13 13 PRO CB C 32.626 . 1 126 13 13 PRO CG C 26.340 . 1 127 13 13 PRO CD C 49.890 . 1 128 14 14 VAL H H 7.385 . 1 129 14 14 VAL HA H 4.564 . 1 130 14 14 VAL HB H 1.655 . 1 131 14 14 VAL HG1 H 0.483 . 2 132 14 14 VAL HG2 H 0.762 . 2 133 14 14 VAL C C 175.968 . 1 134 14 14 VAL CA C 63.027 . 1 135 14 14 VAL CB C 30.682 . 1 136 14 14 VAL CG1 C 22.382 . 2 137 14 14 VAL CG2 C 22.030 . 2 138 14 14 VAL N N 120.693 . 1 139 15 15 GLN H H 8.059 . 1 140 15 15 GLN HA H 4.857 . 1 141 15 15 GLN HB2 H 2.179 . 2 142 15 15 GLN HB3 H 2.030 . 2 143 15 15 GLN HG2 H 2.329 . 2 144 15 15 GLN HG3 H 2.027 . 2 145 15 15 GLN C C 174.235 . 1 146 15 15 GLN CA C 54.050 . 1 147 15 15 GLN CB C 32.450 . 1 148 15 15 GLN CG C 32.928 . 1 149 15 15 GLN N N 123.401 . 1 150 16 16 GLY H H 8.230 . 1 151 16 16 GLY HA2 H 4.347 . 2 152 16 16 GLY HA3 H 4.449 . 2 153 16 16 GLY C C 170.848 . 1 154 16 16 GLY CA C 46.703 . 1 155 16 16 GLY N N 107.679 . 1 156 17 17 ILE H H 7.995 . 1 157 17 17 ILE HA H 4.722 . 1 158 17 17 ILE HB H 1.713 . 1 159 17 17 ILE HG12 H 1.025 . 2 160 17 17 ILE HG13 H 1.570 . 2 161 17 17 ILE HG2 H 0.730 . 1 162 17 17 ILE HD1 H 0.873 . 1 163 17 17 ILE C C 174.084 . 1 164 17 17 ILE CA C 61.286 . 1 165 17 17 ILE CB C 40.840 . 1 166 17 17 ILE CG1 C 28.354 . 1 167 17 17 ILE CG2 C 17.187 . 1 168 17 17 ILE CD1 C 13.775 . 1 169 17 17 ILE N N 120.753 . 1 170 18 18 ILE H H 8.818 . 1 171 18 18 ILE HA H 4.250 . 1 172 18 18 ILE HB H 1.676 . 1 173 18 18 ILE HG12 H 1.183 . 2 174 18 18 ILE HG13 H 1.335 . 2 175 18 18 ILE HG2 H 0.150 . 1 176 18 18 ILE HD1 H 0.403 . 1 177 18 18 ILE C C 172.554 . 1 178 18 18 ILE CA C 56.830 . 1 179 18 18 ILE CB C 37.565 . 1 180 18 18 ILE CG1 C 25.792 . 1 181 18 18 ILE CG2 C 18.363 . 1 182 18 18 ILE CD1 C 7.936 . 1 183 18 18 ILE N N 126.636 . 1 184 19 19 ASN H H 8.753 . 1 185 19 19 ASN HA H 4.802 . 1 186 19 19 ASN HB2 H 1.463 . 2 187 19 19 ASN HB3 H 0.327 . 2 188 19 19 ASN C C 172.143 . 1 189 19 19 ASN CA C 52.317 . 1 190 19 19 ASN CB C 40.430 . 1 191 19 19 ASN N N 124.358 . 1 192 20 20 PHE H H 8.482 . 1 193 20 20 PHE HA H 5.776 . 1 194 20 20 PHE HB2 H 2.665 . 2 195 20 20 PHE HB3 H 2.642 . 2 196 20 20 PHE C C 176.335 . 1 197 20 20 PHE CA C 55.265 . 1 198 20 20 PHE CB C 43.267 . 1 199 20 20 PHE N N 115.019 . 1 200 21 21 GLU H H 9.599 . 1 201 21 21 GLU HA H 5.316 . 1 202 21 21 GLU HB2 H 2.302 . 2 203 21 21 GLU HB3 H 2.302 . 2 204 21 21 GLU HG2 H 2.107 . 2 205 21 21 GLU HG3 H 2.225 . 2 206 21 21 GLU C C 173.667 . 1 207 21 21 GLU CA C 56.150 . 1 208 21 21 GLU CB C 34.496 . 1 209 21 21 GLU CG C 37.477 . 1 210 21 21 GLU N N 122.179 . 1 211 22 22 GLN H H 9.183 . 1 212 22 22 GLN HA H 4.937 . 1 213 22 22 GLN HG2 H 2.226 . 1 214 22 22 GLN HG3 H 2.226 . 1 215 22 22 GLN C C 174.661 . 1 216 22 22 GLN CA C 54.464 . 1 217 22 22 GLN CB C 32.779 . 1 218 22 22 GLN N N 129.820 . 1 219 23 23 LYS H H 9.204 . 1 220 23 23 LYS HA H 4.103 . 1 221 23 23 LYS HB2 H 1.941 . 2 222 23 23 LYS HB3 H 1.941 . 2 223 23 23 LYS HG2 H 1.446 . 2 224 23 23 LYS HG3 H 1.446 . 2 225 23 23 LYS HD2 H 1.619 . 2 226 23 23 LYS HD3 H 1.689 . 2 227 23 23 LYS HE2 H 2.978 . 2 228 23 23 LYS HE3 H 2.978 . 2 229 23 23 LYS C C 176.181 . 1 230 23 23 LYS CA C 59.738 . 1 231 23 23 LYS CB C 33.244 . 1 232 23 23 LYS CG C 25.583 . 1 233 23 23 LYS CD C 29.338 . 1 234 23 23 LYS CE C 42.007 . 1 235 23 23 LYS N N 130.178 . 1 236 24 24 GLU H H 8.154 . 1 237 24 24 GLU HA H 4.684 . 1 238 24 24 GLU HB2 H 2.145 . 2 239 24 24 GLU HB3 H 1.807 . 2 240 24 24 GLU HG2 H 2.217 . 2 241 24 24 GLU HG3 H 2.217 . 2 242 24 24 GLU C C 177.214 . 1 243 24 24 GLU CA C 54.311 . 1 244 24 24 GLU CB C 32.489 . 1 245 24 24 GLU CG C 35.627 . 1 246 24 24 GLU N N 115.810 . 1 247 25 25 SER H H 8.817 . 1 248 25 25 SER HA H 3.962 . 1 249 25 25 SER HB2 H 3.791 . 2 250 25 25 SER HB3 H 3.791 . 2 251 25 25 SER C C 174.586 . 1 252 25 25 SER CA C 61.092 . 1 253 25 25 SER CB C 62.767 . 1 254 25 25 SER N N 118.302 . 1 255 26 26 ASN H H 8.343 . 1 256 26 26 ASN HA H 4.734 . 1 257 26 26 ASN HB2 H 2.915 . 2 258 26 26 ASN HB3 H 2.915 . 2 259 26 26 ASN C C 175.065 . 1 260 26 26 ASN CA C 53.065 . 1 261 26 26 ASN CB C 38.144 . 1 262 26 26 ASN N N 117.176 . 1 263 27 27 GLY H H 7.941 . 1 264 27 27 GLY C C 172.016 . 1 265 27 27 GLY CA C 44.621 . 1 266 27 27 GLY N N 108.060 . 1 267 28 28 PRO HA H 4.622 . 1 268 28 28 PRO HB2 H 2.161 . 2 269 28 28 PRO HB3 H 1.741 . 2 270 28 28 PRO HG2 H 1.975 . 2 271 28 28 PRO HG3 H 2.023 . 2 272 28 28 PRO HD2 H 3.638 . 2 273 28 28 PRO HD3 H 3.704 . 2 274 28 28 PRO C C 176.162 . 1 275 28 28 PRO CA C 63.068 . 1 276 28 28 PRO CB C 32.917 . 1 277 28 28 PRO CG C 27.440 . 1 278 28 28 PRO CD C 49.740 . 1 279 29 29 VAL H H 8.984 . 1 280 29 29 VAL HA H 4.553 . 1 281 29 29 VAL HB H 2.069 . 1 282 29 29 VAL HG1 H 0.861 . 2 283 29 29 VAL HG2 H 0.970 . 2 284 29 29 VAL C C 175.207 . 1 285 29 29 VAL CA C 61.110 . 1 286 29 29 VAL CB C 33.554 . 1 287 29 29 VAL CG1 C 23.292 . 2 288 29 29 VAL CG2 C 23.292 . 2 289 29 29 VAL N N 121.580 . 1 290 30 30 LYS H H 9.155 . 1 291 30 30 LYS HA H 4.955 . 1 292 30 30 LYS HB2 H 2.027 . 2 293 30 30 LYS HB3 H 1.969 . 2 294 30 30 LYS HG2 H 1.439 . 2 295 30 30 LYS HG3 H 1.439 . 2 296 30 30 LYS HD2 H 1.596 . 2 297 30 30 LYS HD3 H 1.596 . 2 298 30 30 LYS HE2 H 2.595 . 2 299 30 30 LYS HE3 H 2.663 . 2 300 30 30 LYS C C 175.301 . 1 301 30 30 LYS CA C 55.876 . 1 302 30 30 LYS CB C 34.376 . 1 303 30 30 LYS CG C 25.723 . 1 304 30 30 LYS CD C 29.330 . 1 305 30 30 LYS CE C 41.967 . 1 306 30 30 LYS N N 128.367 . 1 307 31 31 VAL H H 9.234 . 1 308 31 31 VAL HA H 4.974 . 1 309 31 31 VAL HB H 2.014 . 1 310 31 31 VAL HG1 H 0.234 . 2 311 31 31 VAL HG2 H 0.826 . 2 312 31 31 VAL C C 175.402 . 1 313 31 31 VAL CA C 60.455 . 1 314 31 31 VAL CB C 33.531 . 1 315 31 31 VAL CG1 C 20.843 . 2 316 31 31 VAL CG2 C 20.843 . 2 317 31 31 VAL N N 126.731 . 1 318 32 32 TRP H H 9.003 . 1 319 32 32 TRP HA H 5.540 . 1 320 32 32 TRP HB2 H 3.478 . 2 321 32 32 TRP HB3 H 3.331 . 2 322 32 32 TRP C C 173.401 . 1 323 32 32 TRP CA C 56.155 . 1 324 32 32 TRP CB C 32.382 . 1 325 32 32 TRP N N 125.563 . 1 326 33 33 GLY H H 8.467 . 1 327 33 33 GLY HA2 H 3.914 . 2 328 33 33 GLY HA3 H 4.940 . 2 329 33 33 GLY C C 171.312 . 1 330 33 33 GLY CA C 44.707 . 1 331 33 33 GLY N N 108.523 . 1 332 34 34 SER H H 7.814 . 1 333 34 34 SER HA H 5.470 . 1 334 34 34 SER HB2 H 3.724 . 2 335 34 34 SER HB3 H 3.724 . 2 336 34 34 SER C C 172.855 . 1 337 34 34 SER CA C 57.030 . 1 338 34 34 SER CB C 65.389 . 1 339 34 34 SER N N 114.048 . 1 340 35 35 ILE H H 8.643 . 1 341 35 35 ILE HA H 4.569 . 1 342 35 35 ILE HB H 1.401 . 1 343 35 35 ILE HG12 H 0.529 . 2 344 35 35 ILE HG13 H 0.529 . 2 345 35 35 ILE HG2 H 0.656 . 1 346 35 35 ILE HD1 H 0.380 . 1 347 35 35 ILE C C 173.128 . 1 348 35 35 ILE CA C 60.154 . 1 349 35 35 ILE CB C 41.278 . 1 350 35 35 ILE CG1 C 27.505 . 1 351 35 35 ILE CG2 C 19.150 . 1 352 35 35 ILE CD1 C 14.550 . 1 353 35 35 ILE N N 124.079 . 1 354 36 36 LYS H H 9.021 . 1 355 36 36 LYS HA H 5.283 . 1 356 36 36 LYS HB2 H 1.834 . 2 357 36 36 LYS HB3 H 1.834 . 2 358 36 36 LYS HG2 H 1.364 . 2 359 36 36 LYS HG3 H 1.450 . 2 360 36 36 LYS HD2 H 1.620 . 2 361 36 36 LYS HD3 H 1.620 . 2 362 36 36 LYS HE2 H 2.894 . 2 363 36 36 LYS HE3 H 2.894 . 2 364 36 36 LYS C C 175.556 . 1 365 36 36 LYS CA C 54.483 . 1 366 36 36 LYS CB C 35.263 . 1 367 36 36 LYS CG C 24.670 . 1 368 36 36 LYS CD C 29.580 . 1 369 36 36 LYS CE C 42.174 . 1 370 36 36 LYS N N 124.241 . 1 371 37 37 GLY H H 8.284 . 1 372 37 37 GLY HA2 H 3.958 . 2 373 37 37 GLY HA3 H 4.239 . 2 374 37 37 GLY C C 174.719 . 1 375 37 37 GLY CA C 45.621 . 1 376 37 37 GLY N N 106.342 . 1 377 38 38 LEU H H 8.310 . 1 378 38 38 LEU HA H 4.042 . 1 379 38 38 LEU HB2 H 1.326 . 2 380 38 38 LEU HB3 H 0.686 . 2 381 38 38 LEU HG H 1.181 . 1 382 38 38 LEU HD1 H 0.061 . 2 383 38 38 LEU HD2 H 0.314 . 2 384 38 38 LEU C C 177.050 . 1 385 38 38 LEU CA C 53.535 . 1 386 38 38 LEU CB C 44.270 . 1 387 38 38 LEU CG C 26.460 . 1 388 38 38 LEU CD1 C 23.834 . 2 389 38 38 LEU CD2 C 26.626 . 2 390 38 38 LEU N N 120.783 . 1 391 39 39 THR H H 8.157 . 1 392 39 39 THR HA H 4.272 . 1 393 39 39 THR HB H 4.184 . 1 394 39 39 THR HG2 H 1.342 . 1 395 39 39 THR C C 175.816 . 1 396 39 39 THR CA C 61.297 . 1 397 39 39 THR CB C 69.664 . 1 398 39 39 THR CG2 C 22.854 . 1 399 39 39 THR N N 110.802 . 1 400 40 40 GLU H H 8.711 . 1 401 40 40 GLU HA H 3.721 . 1 402 40 40 GLU HB2 H 1.871 . 2 403 40 40 GLU HB3 H 1.871 . 2 404 40 40 GLU HG2 H 2.046 . 2 405 40 40 GLU HG3 H 2.105 . 2 406 40 40 GLU C C 175.983 . 1 407 40 40 GLU CA C 57.594 . 1 408 40 40 GLU CB C 30.456 . 1 409 40 40 GLU CG C 35.097 . 1 410 40 40 GLU N N 126.258 . 1 411 41 41 GLY H H 8.674 . 1 412 41 41 GLY HA2 H 3.728 . 2 413 41 41 GLY HA3 H 4.604 . 2 414 41 41 GLY C C 173.080 . 1 415 41 41 GLY CA C 43.248 . 1 416 41 41 GLY N N 113.673 . 1 417 42 42 LEU H H 8.278 . 1 418 42 42 LEU HA H 4.825 . 1 419 42 42 LEU HB2 H 1.580 . 1 420 42 42 LEU HB3 H 1.051 . 1 421 42 42 LEU C C 177.421 . 1 422 42 42 LEU CA C 55.240 . 1 423 42 42 LEU CB C 44.681 . 1 424 42 42 LEU N N 120.602 . 1 425 43 43 HIS H H 8.804 . 1 426 43 43 HIS HA H 4.367 . 1 427 43 43 HIS HB2 H 2.481 . 1 428 43 43 HIS HB3 H 3.531 . 1 429 43 43 HIS C C 173.800 . 1 430 43 43 HIS CA C 54.618 . 1 431 43 43 HIS CB C 31.768 . 1 432 43 43 HIS N N 116.385 . 1 433 44 44 GLY H H 8.719 . 1 434 44 44 GLY HA2 H 3.556 . 2 435 44 44 GLY HA3 H 4.573 . 2 436 44 44 GLY C C 172.105 . 1 437 44 44 GLY CA C 46.321 . 1 438 44 44 GLY N N 112.285 . 1 439 45 45 PHE H H 8.707 . 1 440 45 45 PHE HA H 5.783 . 1 441 45 45 PHE HB2 H 2.762 . 2 442 45 45 PHE HB3 H 3.383 . 2 443 45 45 PHE C C 173.597 . 1 444 45 45 PHE CA C 55.046 . 1 445 45 45 PHE CB C 41.710 . 1 446 45 45 PHE N N 127.665 . 1 447 46 46 HIS H H 8.748 . 1 448 46 46 HIS HA H 5.355 . 1 449 46 46 HIS HB2 H 2.963 . 1 450 46 46 HIS HB3 H 3.069 . 1 451 46 46 HIS C C 173.208 . 1 452 46 46 HIS CA C 53.579 . 1 453 46 46 HIS CB C 35.465 . 1 454 46 46 HIS N N 121.362 . 1 455 47 47 VAL H H 9.016 . 1 456 47 47 VAL HA H 4.612 . 1 457 47 47 VAL HB H 1.831 . 1 458 47 47 VAL HG1 H 0.709 . 2 459 47 47 VAL HG2 H 0.709 . 2 460 47 47 VAL C C 175.582 . 1 461 47 47 VAL CA C 61.540 . 1 462 47 47 VAL CB C 32.494 . 1 463 47 47 VAL CG1 C 21.298 . 2 464 47 47 VAL CG2 C 22.843 . 2 465 47 47 VAL N N 121.590 . 1 466 48 48 HIS H H 9.531 . 1 467 48 48 HIS C C 174.724 . 1 468 48 48 HIS CA C 55.668 . 1 469 48 48 HIS CB C 33.092 . 1 470 48 48 HIS N N 128.487 . 1 471 50 50 PHE HA H 4.684 . 1 472 50 50 PHE HB2 H 3.165 . 2 473 50 50 PHE HB3 H 2.959 . 2 474 50 50 PHE C C 176.282 . 1 475 50 50 PHE CA C 57.931 . 1 476 50 50 PHE CB C 39.978 . 1 477 51 51 GLY H H 8.440 . 1 478 51 51 GLY HA2 H 3.928 . 2 479 51 51 GLY HA3 H 3.928 . 2 480 51 51 GLY C C 173.442 . 1 481 51 51 GLY CA C 45.283 . 1 482 51 51 GLY N N 110.274 . 1 483 52 52 ASP H H 8.188 . 1 484 52 52 ASP HA H 4.583 . 1 485 52 52 ASP HB2 H 2.667 . 2 486 52 52 ASP HB3 H 2.614 . 2 487 52 52 ASP C C 176.184 . 1 488 52 52 ASP CA C 54.191 . 1 489 52 52 ASP CB C 41.321 . 1 490 52 52 ASP N N 120.323 . 1 491 53 53 ASN H H 8.512 . 1 492 53 53 ASN HA H 4.735 . 1 493 53 53 ASN HB2 H 2.835 . 2 494 53 53 ASN HB3 H 2.759 . 2 495 53 53 ASN C C 175.752 . 1 496 53 53 ASN CA C 53.472 . 1 497 53 53 ASN CB C 38.672 . 1 498 53 53 ASN N N 119.573 . 1 499 54 54 THR H H 8.185 . 1 500 54 54 THR HA H 4.428 . 1 501 54 54 THR HB H 4.243 . 1 502 54 54 THR HG2 H 1.158 . 1 503 54 54 THR C C 174.776 . 1 504 54 54 THR CA C 62.502 . 1 505 54 54 THR CB C 69.722 . 1 506 54 54 THR CG2 C 21.710 . 1 507 54 54 THR N N 113.921 . 1 508 55 55 ALA H H 8.248 . 1 509 55 55 ALA HA H 4.264 . 1 510 55 55 ALA HB H 1.364 . 1 511 55 55 ALA C C 178.175 . 1 512 55 55 ALA CA C 52.942 . 1 513 55 55 ALA CB C 19.020 . 1 514 55 55 ALA N N 125.724 . 1 515 56 56 GLY H H 8.281 . 1 516 56 56 GLY HA2 H 3.910 . 2 517 56 56 GLY HA3 H 3.910 . 2 518 56 56 GLY C C 174.234 . 1 519 56 56 GLY CA C 45.378 . 1 520 56 56 GLY N N 107.740 . 1 521 57 57 CYS H H 8.132 . 1 522 57 57 CYS HA H 4.540 . 1 523 57 57 CYS HB2 H 2.904 . 2 524 57 57 CYS HB3 H 2.904 . 2 525 57 57 CYS C C 175.070 . 1 526 57 57 CYS CA C 58.666 . 1 527 57 57 CYS CB C 28.073 . 1 528 57 57 CYS N N 118.741 . 1 529 58 58 THR H H 8.304 . 1 530 58 58 THR HA H 4.425 . 1 531 58 58 THR HB H 4.303 . 1 532 58 58 THR HG2 H 1.182 . 1 533 58 58 THR C C 174.688 . 1 534 58 58 THR CA C 62.001 . 1 535 58 58 THR CB C 69.750 . 1 536 58 58 THR CG2 C 21.670 . 1 537 58 58 THR N N 116.101 . 1 538 59 59 SER H H 8.252 . 1 539 59 59 SER HA H 4.375 . 1 540 59 59 SER HB2 H 3.813 . 2 541 59 59 SER HB3 H 3.813 . 2 542 59 59 SER C C 173.970 . 1 543 59 59 SER CA C 58.431 . 1 544 59 59 SER CB C 63.770 . 1 545 59 59 SER N N 117.850 . 1 546 60 60 ALA H H 8.207 . 1 547 60 60 ALA HA H 4.342 . 1 548 60 60 ALA HB H 1.329 . 1 549 60 60 ALA C C 177.563 . 1 550 60 60 ALA CA C 52.431 . 1 551 60 60 ALA CB C 19.602 . 1 552 60 60 ALA N N 125.333 . 1 553 61 61 GLY H H 8.099 . 1 554 61 61 GLY C C 172.052 . 1 555 61 61 GLY CA C 44.660 . 1 556 61 61 GLY N N 107.983 . 1 557 66 66 PRO HA H 4.232 . 1 558 66 66 PRO HB2 H 2.259 . 2 559 66 66 PRO HB3 H 1.918 . 2 560 66 66 PRO HG2 H 1.950 . 2 561 66 66 PRO HG3 H 1.950 . 2 562 66 66 PRO HD2 H 3.616 . 2 563 66 66 PRO HD3 H 3.689 . 2 564 66 66 PRO C C 177.110 . 1 565 66 66 PRO CA C 63.780 . 1 566 66 66 PRO CB C 32.151 . 1 567 66 66 PRO CG C 27.156 . 1 568 66 66 PRO CD C 50.728 . 1 569 67 67 LEU H H 8.050 . 1 570 67 67 LEU HA H 4.254 . 1 571 67 67 LEU HB2 H 1.619 . 2 572 67 67 LEU HB3 H 1.562 . 2 573 67 67 LEU HG H 1.578 . 1 574 67 67 LEU HD1 H 0.811 . 2 575 67 67 LEU HD2 H 0.865 . 2 576 67 67 LEU C C 177.625 . 1 577 67 67 LEU CA C 55.361 . 1 578 67 67 LEU CB C 41.672 . 1 579 67 67 LEU CG C 27.235 . 1 580 67 67 LEU CD1 C 23.126 . 2 581 67 67 LEU CD2 C 25.048 . 2 582 67 67 LEU N N 119.318 . 1 583 68 68 SER H H 7.869 . 1 584 68 68 SER HA H 4.331 . 1 585 68 68 SER HB2 H 3.830 . 2 586 68 68 SER HB3 H 3.830 . 2 587 68 68 SER C C 174.561 . 1 588 68 68 SER CA C 58.507 . 1 589 68 68 SER CB C 63.761 . 1 590 68 68 SER N N 115.101 . 1 591 69 69 ARG H H 8.146 . 1 592 69 69 ARG HA H 4.307 . 1 593 69 69 ARG HB2 H 1.825 . 2 594 69 69 ARG HB3 H 1.698 . 2 595 69 69 ARG HG2 H 1.553 . 2 596 69 69 ARG HG3 H 1.553 . 2 597 69 69 ARG HD2 H 3.128 . 2 598 69 69 ARG HD3 H 3.128 . 2 599 69 69 ARG C C 176.118 . 1 600 69 69 ARG CA C 56.048 . 1 601 69 69 ARG CB C 30.696 . 1 602 69 69 ARG CG C 27.100 . 1 603 69 69 ARG CD C 43.324 . 1 604 69 69 ARG N N 122.660 . 1 605 70 70 LYS H H 8.253 . 1 606 70 70 LYS C C 176.301 . 1 607 70 70 LYS CA C 56.325 . 1 608 70 70 LYS CB C 33.072 . 1 609 70 70 LYS N N 122.188 . 1 610 71 71 HIS H H 8.464 . 1 611 71 71 HIS HA H 4.630 . 1 612 71 71 HIS HB2 H 3.055 . 1 613 71 71 HIS HB3 H 3.130 . 1 614 71 71 HIS C C 175.538 . 1 615 71 71 HIS CA C 56.084 . 1 616 71 71 HIS CB C 30.549 . 1 617 72 72 GLY H H 8.466 . 1 618 72 72 GLY HA2 H 3.956 . 2 619 72 72 GLY HA3 H 3.956 . 2 620 72 72 GLY C C 174.211 . 1 621 72 72 GLY CA C 45.184 . 1 622 72 72 GLY N N 110.606 . 1 623 73 73 GLY H H 8.289 . 1 624 73 73 GLY C C 172.049 . 1 625 73 73 GLY CA C 44.555 . 1 626 73 73 GLY N N 109.198 . 1 627 74 74 PRO HA H 4.391 . 1 628 74 74 PRO HB2 H 2.271 . 2 629 74 74 PRO HB3 H 1.921 . 2 630 74 74 PRO HG2 H 1.986 . 2 631 74 74 PRO HG3 H 1.986 . 2 632 74 74 PRO HD2 H 3.579 . 2 633 74 74 PRO HD3 H 3.623 . 2 634 74 74 PRO C C 177.465 . 1 635 74 74 PRO CA C 63.631 . 1 636 74 74 PRO CB C 32.217 . 1 637 74 74 PRO CG C 27.302 . 1 638 74 74 PRO CD C 49.763 . 1 639 75 75 LYS H H 8.458 . 1 640 75 75 LYS HA H 4.273 . 1 641 75 75 LYS HB2 H 1.834 . 2 642 75 75 LYS HB3 H 1.721 . 2 643 75 75 LYS HG2 H 1.394 . 2 644 75 75 LYS HG3 H 1.394 . 2 645 75 75 LYS HD2 H 1.653 . 2 646 75 75 LYS HD3 H 1.653 . 2 647 75 75 LYS HE2 H 2.960 . 2 648 75 75 LYS HE3 H 2.960 . 2 649 75 75 LYS C C 176.588 . 1 650 75 75 LYS CA C 56.482 . 1 651 75 75 LYS CB C 32.719 . 1 652 75 75 LYS CG C 24.767 . 1 653 75 75 LYS CD C 29.082 . 1 654 75 75 LYS CE C 42.091 . 1 655 75 75 LYS N N 120.344 . 1 656 76 76 ASP H H 8.210 . 1 657 76 76 ASP HA H 4.537 . 1 658 76 76 ASP HB2 H 2.690 . 2 659 76 76 ASP HB3 H 2.599 . 2 660 76 76 ASP C C 176.315 . 1 661 76 76 ASP CA C 54.872 . 1 662 76 76 ASP CB C 41.114 . 1 663 76 76 ASP N N 120.924 . 1 664 77 77 GLU H H 8.318 . 1 665 77 77 GLU HA H 4.233 . 1 666 77 77 GLU HB2 H 2.047 . 2 667 77 77 GLU HB3 H 1.902 . 2 668 77 77 GLU HG2 H 2.233 . 2 669 77 77 GLU HG3 H 2.233 . 2 670 77 77 GLU C C 176.416 . 1 671 77 77 GLU CA C 56.796 . 1 672 77 77 GLU CB C 30.343 . 1 673 77 77 GLU CG C 36.316 . 1 674 77 77 GLU N N 120.385 . 1 675 78 78 GLU H H 8.279 . 1 676 78 78 GLU HA H 4.200 . 1 677 78 78 GLU HB2 H 1.951 . 2 678 78 78 GLU HB3 H 1.951 . 2 679 78 78 GLU C C 176.220 . 1 680 78 78 GLU CA C 56.574 . 1 681 78 78 GLU CB C 30.357 . 1 682 78 78 GLU CG C 36.351 . 1 683 78 78 GLU N N 121.495 . 1 684 79 79 ARG H H 8.228 . 1 685 79 79 ARG C C 175.869 . 1 686 79 79 ARG CA C 56.013 . 1 687 79 79 ARG CB C 31.091 . 1 688 79 79 ARG N N 121.479 . 1 689 84 84 LEU HA H 4.254 . 1 690 84 84 LEU HB2 H 1.691 . 2 691 84 84 LEU HB3 H 1.589 . 2 692 84 84 LEU HG H 1.611 . 1 693 84 84 LEU HD1 H 0.827 . 2 694 84 84 LEU HD2 H 0.876 . 2 695 84 84 LEU C C 176.469 . 1 696 84 84 LEU CA C 55.501 . 1 697 84 84 LEU CB C 42.100 . 1 698 84 84 LEU CG C 27.037 . 1 699 84 84 LEU CD1 C 23.279 . 2 700 84 84 LEU CD2 C 25.061 . 2 701 85 85 GLY H H 8.469 . 1 702 85 85 GLY HA2 H 3.749 . 2 703 85 85 GLY HA3 H 4.251 . 2 704 85 85 GLY C C 172.249 . 1 705 85 85 GLY CA C 44.867 . 1 706 85 85 GLY N N 108.948 . 1 707 86 86 ASN H H 8.278 . 1 708 86 86 ASN HA H 5.440 . 1 709 86 86 ASN HB2 H 2.538 . 2 710 86 86 ASN HB3 H 2.330 . 2 711 86 86 ASN C C 176.951 . 1 712 86 86 ASN CA C 52.641 . 1 713 86 86 ASN CB C 41.969 . 1 714 86 86 ASN N N 117.162 . 1 715 87 87 VAL H H 9.033 . 1 716 87 87 VAL HA H 4.568 . 1 717 87 87 VAL HB H 1.756 . 1 718 87 87 VAL HG1 H 0.165 . 2 719 87 87 VAL HG2 H 0.411 . 2 720 87 87 VAL C C 174.632 . 1 721 87 87 VAL CA C 59.158 . 1 722 87 87 VAL CB C 32.783 . 1 723 87 87 VAL CG1 C 18.156 . 2 724 87 87 VAL CG2 C 21.711 . 2 725 87 87 VAL N N 114.866 . 1 726 88 88 THR H H 8.582 . 1 727 88 88 THR HA H 4.598 . 1 728 88 88 THR HB H 3.911 . 1 729 88 88 THR HG2 H 1.001 . 1 730 88 88 THR C C 173.546 . 1 731 88 88 THR CA C 61.785 . 1 732 88 88 THR CB C 69.970 . 1 733 88 88 THR CG2 C 21.471 . 1 734 88 88 THR N N 118.447 . 1 735 89 89 ALA H H 9.235 . 1 736 89 89 ALA HA H 4.651 . 1 737 89 89 ALA HB H 1.268 . 1 738 89 89 ALA C C 177.551 . 1 739 89 89 ALA CA C 49.536 . 1 740 89 89 ALA CB C 21.267 . 1 741 89 89 ALA N N 129.293 . 1 742 90 90 ASP H H 8.494 . 1 743 90 90 ASP HA H 4.545 . 1 744 90 90 ASP HB2 H 3.327 . 2 745 90 90 ASP HB3 H 2.838 . 2 746 90 90 ASP C C 177.123 . 1 747 90 90 ASP CA C 52.563 . 1 748 90 90 ASP CB C 41.640 . 1 749 90 90 ASP N N 125.015 . 1 750 91 91 LYS H H 8.172 . 1 751 91 91 LYS HA H 3.987 . 1 752 91 91 LYS HB2 H 1.876 . 2 753 91 91 LYS HB3 H 1.798 . 2 754 91 91 LYS HG2 H 1.351 . 2 755 91 91 LYS HG3 H 1.417 . 2 756 91 91 LYS HD2 H 1.641 . 2 757 91 91 LYS HD3 H 1.641 . 2 758 91 91 LYS HE2 H 3.003 . 2 759 91 91 LYS HE3 H 3.003 . 2 760 91 91 LYS C C 177.260 . 1 761 91 91 LYS CA C 58.528 . 1 762 91 91 LYS CB C 31.810 . 1 763 91 91 LYS CG C 23.943 . 1 764 91 91 LYS CD C 29.205 . 1 765 91 91 LYS CE C 42.129 . 1 766 91 91 LYS N N 115.168 . 1 767 92 92 ASP H H 8.164 . 1 768 92 92 ASP HA H 4.785 . 1 769 92 92 ASP HB2 H 2.858 . 2 770 92 92 ASP HB3 H 2.789 . 2 771 92 92 ASP C C 176.294 . 1 772 92 92 ASP CA C 54.366 . 1 773 92 92 ASP CB C 41.550 . 1 774 92 92 ASP N N 119.787 . 1 775 93 93 GLY H H 8.422 . 1 776 93 93 GLY HA2 H 3.797 . 2 777 93 93 GLY HA3 H 3.932 . 2 778 93 93 GLY C C 172.891 . 1 779 93 93 GLY CA C 46.948 . 1 780 93 93 GLY N N 111.512 . 1 781 94 94 VAL H H 7.947 . 1 782 94 94 VAL HA H 4.702 . 1 783 94 94 VAL HB H 2.174 . 1 784 94 94 VAL HG1 H 0.768 . 2 785 94 94 VAL HG2 H 0.844 . 2 786 94 94 VAL C C 176.548 . 1 787 94 94 VAL CA C 61.603 . 1 788 94 94 VAL CB C 32.929 . 1 789 94 94 VAL CG1 C 21.769 . 2 790 94 94 VAL CG2 C 21.360 . 2 791 94 94 VAL N N 119.430 . 1 792 95 95 ALA H H 9.581 . 1 793 95 95 ALA HA H 5.071 . 1 794 95 95 ALA HB H 0.777 . 1 795 95 95 ALA C C 174.857 . 1 796 95 95 ALA CA C 50.137 . 1 797 95 95 ALA CB C 20.981 . 1 798 95 95 ALA N N 131.343 . 1 799 96 96 ASP H H 8.597 . 1 800 96 96 ASP HA H 5.003 . 1 801 96 96 ASP HB2 H 2.641 . 2 802 96 96 ASP HB3 H 2.496 . 2 803 96 96 ASP C C 175.589 . 1 804 96 96 ASP CA C 54.110 . 1 805 96 96 ASP CB C 41.825 . 1 806 96 96 ASP N N 125.322 . 1 807 97 97 VAL H H 8.625 . 1 808 97 97 VAL HA H 4.126 . 1 809 97 97 VAL HB H 1.617 . 1 810 97 97 VAL HG1 H 0.464 . 2 811 97 97 VAL HG2 H 0.716 . 2 812 97 97 VAL C C 176.616 . 1 813 97 97 VAL CA C 61.981 . 1 814 97 97 VAL CB C 33.708 . 1 815 97 97 VAL CG1 C 20.961 . 2 816 97 97 VAL CG2 C 20.961 . 2 817 97 97 VAL N N 125.080 . 1 818 98 98 SER H H 8.834 . 1 819 98 98 SER HA H 5.116 . 1 820 98 98 SER HB2 H 3.856 . 2 821 98 98 SER HB3 H 3.856 . 2 822 98 98 SER C C 173.060 . 1 823 98 98 SER CA C 58.265 . 1 824 98 98 SER CB C 62.601 . 1 825 98 98 SER N N 123.684 . 1 826 99 99 ILE H H 9.385 . 1 827 99 99 ILE HA H 4.710 . 1 828 99 99 ILE HB H 1.801 . 1 829 99 99 ILE HG12 H 1.194 . 2 830 99 99 ILE HG13 H 1.479 . 2 831 99 99 ILE HG2 H 1.027 . 1 832 99 99 ILE HD1 H 0.959 . 1 833 99 99 ILE C C 174.494 . 1 834 99 99 ILE CA C 60.276 . 1 835 99 99 ILE CB C 44.230 . 1 836 99 99 ILE CG1 C 27.501 . 1 837 99 99 ILE CG2 C 18.016 . 1 838 99 99 ILE CD1 C 14.952 . 1 839 99 99 ILE N N 126.109 . 1 840 100 100 GLU H H 8.620 . 1 841 100 100 GLU HA H 5.254 . 1 842 100 100 GLU HB2 H 1.934 . 2 843 100 100 GLU HB3 H 1.934 . 2 844 100 100 GLU HG2 H 2.080 . 2 845 100 100 GLU HG3 H 2.080 . 2 846 100 100 GLU C C 174.836 . 1 847 100 100 GLU CA C 55.702 . 1 848 100 100 GLU CB C 32.511 . 1 849 100 100 GLU CG C 37.549 . 1 850 100 100 GLU N N 124.568 . 1 851 101 101 ASP H H 9.159 . 1 852 101 101 ASP HA H 5.064 . 1 853 101 101 ASP HB2 H 2.550 . 2 854 101 101 ASP HB3 H 2.323 . 2 855 101 101 ASP C C 174.996 . 1 856 101 101 ASP CA C 54.073 . 1 857 101 101 ASP CB C 46.591 . 1 858 101 101 ASP N N 126.773 . 1 859 102 102 SER H H 8.888 . 1 860 102 102 SER HA H 4.767 . 1 861 102 102 SER HB2 H 3.928 . 2 862 102 102 SER HB3 H 3.928 . 2 863 102 102 SER C C 173.641 . 1 864 102 102 SER CA C 58.609 . 1 865 102 102 SER CB C 64.132 . 1 866 102 102 SER N N 119.256 . 1 867 103 103 VAL H H 8.828 . 1 868 103 103 VAL HA H 4.031 . 1 869 103 103 VAL HB H 2.340 . 1 870 103 103 VAL HG1 H 0.900 . 2 871 103 103 VAL HG2 H 0.900 . 2 872 103 103 VAL C C 178.001 . 1 873 103 103 VAL CA C 64.319 . 1 874 103 103 VAL CB C 32.383 . 1 875 103 103 VAL CG1 C 21.875 . 2 876 103 103 VAL CG2 C 21.875 . 2 877 103 103 VAL N N 123.335 . 1 878 104 104 ILE H H 7.836 . 1 879 104 104 ILE HA H 4.240 . 1 880 104 104 ILE HB H 1.793 . 1 881 104 104 ILE HG12 H 1.036 . 2 882 104 104 ILE HG13 H 1.213 . 2 883 104 104 ILE HG2 H 0.877 . 1 884 104 104 ILE HD1 H 0.798 . 1 885 104 104 ILE C C 172.710 . 1 886 104 104 ILE CA C 61.701 . 1 887 104 104 ILE CB C 39.790 . 1 888 104 104 ILE CG1 C 24.460 . 1 889 104 104 ILE CG2 C 17.996 . 1 890 104 104 ILE CD1 C 14.447 . 1 891 104 104 ILE N N 113.144 . 1 892 105 105 SER H H 7.352 . 1 893 105 105 SER HA H 4.488 . 1 894 105 105 SER HB2 H 3.802 . 2 895 105 105 SER HB3 H 3.506 . 2 896 105 105 SER C C 173.403 . 1 897 105 105 SER CA C 55.945 . 1 898 105 105 SER CB C 65.457 . 1 899 105 105 SER N N 108.584 . 1 900 106 106 LEU H H 8.294 . 1 901 106 106 LEU HA H 4.521 . 1 902 106 106 LEU HB2 H 1.812 . 2 903 106 106 LEU HB3 H 1.606 . 2 904 106 106 LEU HG H 1.437 . 1 905 106 106 LEU HD1 H 0.409 . 2 906 106 106 LEU HD2 H 0.665 . 2 907 106 106 LEU C C 175.020 . 1 908 106 106 LEU CA C 54.064 . 1 909 106 106 LEU CB C 40.940 . 1 910 106 106 LEU CG C 26.897 . 1 911 106 106 LEU CD1 C 21.729 . 2 912 106 106 LEU CD2 C 26.159 . 2 913 106 106 LEU N N 121.629 . 1 914 107 107 SER H H 8.186 . 1 915 107 107 SER HA H 4.669 . 1 916 107 107 SER HB2 H 3.806 . 2 917 107 107 SER HB3 H 3.806 . 2 918 107 107 SER C C 173.792 . 1 919 107 107 SER CA C 57.583 . 1 920 107 107 SER CB C 65.610 . 1 921 107 107 SER N N 111.938 . 1 922 108 108 GLY H H 8.645 . 1 923 108 108 GLY HA2 H 3.852 . 2 924 108 108 GLY HA3 H 4.223 . 2 925 108 108 GLY C C 175.548 . 1 926 108 108 GLY CA C 45.023 . 1 927 108 108 GLY N N 108.122 . 1 928 109 109 ASP H H 8.650 . 1 929 109 109 ASP HA H 4.217 . 1 930 109 109 ASP HB2 H 2.309 . 1 931 109 109 ASP HB3 H 2.396 . 1 932 109 109 ASP C C 177.239 . 1 933 109 109 ASP CA C 56.675 . 1 934 109 109 ASP CB C 40.419 . 1 935 109 109 ASP N N 120.397 . 1 936 110 110 HIS H H 8.879 . 1 937 110 110 HIS HA H 4.729 . 1 938 110 110 HIS HB2 H 3.368 . 2 939 110 110 HIS HB3 H 2.977 . 2 940 110 110 HIS C C 173.720 . 1 941 110 110 HIS CA C 53.919 . 1 942 110 110 HIS CB C 28.042 . 1 943 110 110 HIS N N 116.662 . 1 944 111 111 SER H H 7.014 . 1 945 111 111 SER HA H 3.898 . 1 946 111 111 SER HB2 H 3.599 . 2 947 111 111 SER HB3 H 3.599 . 2 948 111 111 SER C C 176.926 . 1 949 111 111 SER CA C 57.628 . 1 950 111 111 SER CB C 64.203 . 1 951 111 111 SER N N 112.470 . 1 952 112 112 ILE H H 7.879 . 1 953 112 112 ILE HA H 4.088 . 1 954 112 112 ILE HB H 1.931 . 1 955 112 112 ILE HG12 H 0.702 . 2 956 112 112 ILE HG13 H 1.106 . 2 957 112 112 ILE HG2 H 0.921 . 1 958 112 112 ILE HD1 H 0.247 . 1 959 112 112 ILE C C 175.439 . 1 960 112 112 ILE CA C 61.341 . 1 961 112 112 ILE CB C 37.315 . 1 962 112 112 ILE CG1 C 25.032 . 1 963 112 112 ILE CG2 C 17.807 . 1 964 112 112 ILE CD1 C 15.032 . 1 965 112 112 ILE N N 116.132 . 1 966 113 113 ILE H H 7.854 . 1 967 113 113 ILE HA H 3.261 . 1 968 113 113 ILE HB H 1.810 . 1 969 113 113 ILE HG12 H 1.148 . 2 970 113 113 ILE HG13 H 1.355 . 2 971 113 113 ILE HG2 H 0.902 . 1 972 113 113 ILE HD1 H 0.583 . 1 973 113 113 ILE C C 177.548 . 1 974 113 113 ILE CA C 62.274 . 1 975 113 113 ILE CB C 34.642 . 1 976 113 113 ILE CG1 C 27.703 . 1 977 113 113 ILE CG2 C 17.811 . 1 978 113 113 ILE CD1 C 11.438 . 1 979 113 113 ILE N N 122.181 . 1 980 114 114 GLY H H 9.087 . 1 981 114 114 GLY HA2 H 3.504 . 2 982 114 114 GLY HA3 H 4.417 . 2 983 114 114 GLY C C 174.757 . 1 984 114 114 GLY CA C 45.037 . 1 985 114 114 GLY N N 116.637 . 1 986 115 115 ARG H H 7.878 . 1 987 115 115 ARG HA H 4.513 . 1 988 115 115 ARG HB2 H 1.886 . 2 989 115 115 ARG HB3 H 1.886 . 2 990 115 115 ARG C C 173.931 . 1 991 115 115 ARG CA C 55.783 . 1 992 115 115 ARG CB C 30.346 . 1 993 115 115 ARG CG C 28.880 . 1 994 115 115 ARG CD C 43.508 . 1 995 115 115 ARG N N 119.653 . 1 996 116 116 THR H H 8.514 . 1 997 116 116 THR HA H 4.589 . 1 998 116 116 THR HB H 3.794 . 1 999 116 116 THR HG2 H 0.997 . 1 1000 116 116 THR C C 172.868 . 1 1001 116 116 THR CA C 62.872 . 1 1002 116 116 THR CB C 70.386 . 1 1003 116 116 THR CG2 C 21.935 . 1 1004 116 116 THR N N 115.000 . 1 1005 117 117 LEU H H 9.149 . 1 1006 117 117 LEU HA H 4.718 . 1 1007 117 117 LEU HB2 H 1.787 . 2 1008 117 117 LEU HB3 H 0.989 . 2 1009 117 117 LEU HG H 1.229 . 1 1010 117 117 LEU HD1 H 0.229 . 2 1011 117 117 LEU HD2 H 0.778 . 2 1012 117 117 LEU C C 174.640 . 1 1013 117 117 LEU CA C 53.829 . 1 1014 117 117 LEU CB C 43.780 . 1 1015 117 117 LEU CG C 27.503 . 1 1016 117 117 LEU CD1 C 22.487 . 2 1017 117 117 LEU CD2 C 27.250 . 2 1018 117 117 LEU N N 130.580 . 1 1019 118 118 VAL H H 9.059 . 1 1020 118 118 VAL HA H 4.842 . 1 1021 118 118 VAL HB H 1.859 . 1 1022 118 118 VAL HG1 H 0.425 . 2 1023 118 118 VAL HG2 H 0.729 . 2 1024 118 118 VAL C C 174.619 . 1 1025 118 118 VAL CA C 60.812 . 1 1026 118 118 VAL CB C 36.031 . 1 1027 118 118 VAL CG1 C 21.005 . 2 1028 118 118 VAL CG2 C 22.380 . 2 1029 118 118 VAL N N 124.253 . 1 1030 119 119 VAL H H 8.082 . 1 1031 119 119 VAL HA H 5.348 . 1 1032 119 119 VAL HB H 1.791 . 1 1033 119 119 VAL HG1 H 0.867 . 2 1034 119 119 VAL HG2 H 0.867 . 2 1035 119 119 VAL C C 174.519 . 1 1036 119 119 VAL CA C 59.334 . 1 1037 119 119 VAL CB C 34.285 . 1 1038 119 119 VAL CG1 C 21.241 . 2 1039 119 119 VAL CG2 C 22.623 . 2 1040 119 119 VAL N N 122.421 . 1 1041 120 120 HIS H H 9.306 . 1 1042 120 120 HIS HA H 5.020 . 1 1043 120 120 HIS HB2 H 2.982 . 2 1044 120 120 HIS HB3 H 3.572 . 2 1045 120 120 HIS C C 175.551 . 1 1046 120 120 HIS CA C 56.341 . 1 1047 120 120 HIS CB C 32.846 . 1 1048 120 120 HIS N N 127.801 . 1 1049 121 121 GLU H H 8.896 . 1 1050 121 121 GLU C C 176.423 . 1 1051 121 121 GLU CA C 59.092 . 1 1052 121 121 GLU CB C 31.345 . 1 1053 121 121 GLU N N 122.614 . 1 1054 122 122 LYS H H 8.850 . 1 1055 122 122 LYS HA H 4.483 . 1 1056 122 122 LYS HB2 H 1.863 . 2 1057 122 122 LYS HB3 H 1.684 . 2 1058 122 122 LYS HG2 H 1.340 . 2 1059 122 122 LYS HG3 H 1.340 . 2 1060 122 122 LYS HD2 H 1.634 . 2 1061 122 122 LYS HD3 H 1.634 . 2 1062 122 122 LYS HE2 H 2.957 . 2 1063 122 122 LYS HE3 H 2.957 . 2 1064 122 122 LYS C C 176.040 . 1 1065 122 122 LYS CA C 55.009 . 1 1066 122 122 LYS CB C 34.129 . 1 1067 122 122 LYS CG C 24.811 . 1 1068 122 122 LYS CD C 29.130 . 1 1069 122 122 LYS CE C 42.110 . 1 1070 122 122 LYS N N 119.313 . 1 1071 123 123 ALA H H 8.277 . 1 1072 123 123 ALA HA H 4.068 . 1 1073 123 123 ALA HB H 1.180 . 1 1074 123 123 ALA C C 177.268 . 1 1075 123 123 ALA CA C 51.914 . 1 1076 123 123 ALA CB C 20.086 . 1 1077 123 123 ALA N N 124.533 . 1 1078 124 124 ASP H H 9.009 . 1 1079 124 124 ASP HA H 4.505 . 1 1080 124 124 ASP HB2 H 2.688 . 2 1081 124 124 ASP HB3 H 2.523 . 2 1082 124 124 ASP C C 176.337 . 1 1083 124 124 ASP CA C 54.353 . 1 1084 124 124 ASP CB C 41.324 . 1 1085 124 124 ASP N N 120.755 . 1 1086 125 125 ASP H H 8.490 . 1 1087 125 125 ASP HA H 4.556 . 1 1088 125 125 ASP HB2 H 2.608 . 2 1089 125 125 ASP HB3 H 2.664 . 2 1090 125 125 ASP C C 176.480 . 1 1091 125 125 ASP CA C 54.102 . 1 1092 125 125 ASP CB C 41.311 . 1 1093 125 125 ASP N N 122.600 . 1 1094 126 126 LEU H H 8.427 . 1 1095 126 126 LEU HA H 4.218 . 1 1096 126 126 LEU HB2 H 1.685 . 2 1097 126 126 LEU HB3 H 1.564 . 2 1098 126 126 LEU HG H 1.542 . 1 1099 126 126 LEU HD1 H 0.797 . 2 1100 126 126 LEU HD2 H 0.833 . 2 1101 126 126 LEU C C 178.126 . 1 1102 126 126 LEU CA C 55.663 . 1 1103 126 126 LEU CB C 41.593 . 1 1104 126 126 LEU CG C 27.050 . 1 1105 126 126 LEU CD1 C 23.286 . 2 1106 126 126 LEU CD2 C 25.130 . 2 1107 126 126 LEU N N 122.303 . 1 1108 127 127 GLY H H 8.508 . 1 1109 127 127 GLY HA2 H 3.915 . 2 1110 127 127 GLY HA3 H 3.915 . 2 1111 127 127 GLY C C 174.685 . 1 1112 127 127 GLY CA C 45.605 . 1 1113 127 127 GLY N N 108.831 . 1 1114 128 128 LYS H H 8.081 . 1 1115 128 128 LYS HA H 4.319 . 1 1116 128 128 LYS HB2 H 1.877 . 2 1117 128 128 LYS HB3 H 1.742 . 2 1118 128 128 LYS HG2 H 1.347 . 2 1119 128 128 LYS HG3 H 1.425 . 2 1120 128 128 LYS HD2 H 1.660 . 2 1121 128 128 LYS HD3 H 1.660 . 2 1122 128 128 LYS HE2 H 2.971 . 2 1123 128 128 LYS HE3 H 2.971 . 2 1124 128 128 LYS C C 177.278 . 1 1125 128 128 LYS CA C 56.336 . 1 1126 128 128 LYS CB C 32.841 . 1 1127 128 128 LYS CG C 24.719 . 1 1128 128 128 LYS CD C 29.038 . 1 1129 128 128 LYS CE C 42.179 . 1 1130 128 128 LYS N N 120.391 . 1 1131 129 129 GLY H H 8.506 . 1 1132 129 129 GLY HA2 H 3.950 . 2 1133 129 129 GLY HA3 H 3.950 . 2 1134 129 129 GLY C C 174.703 . 1 1135 129 129 GLY CA C 45.399 . 1 1136 129 129 GLY N N 109.660 . 1 1137 130 130 GLY H H 8.326 . 1 1138 130 130 GLY HA2 H 3.955 . 2 1139 130 130 GLY HA3 H 3.955 . 2 1140 130 130 GLY C C 174.073 . 1 1141 130 130 GLY CA C 45.374 . 1 1142 130 130 GLY N N 108.723 . 1 1143 131 131 ASN H H 8.362 . 1 1144 131 131 ASN HA H 4.719 . 1 1145 131 131 ASN HB2 H 2.852 . 2 1146 131 131 ASN HB3 H 2.776 . 2 1147 131 131 ASN C C 175.525 . 1 1148 131 131 ASN CA C 53.257 . 1 1149 131 131 ASN CB C 39.028 . 1 1150 131 131 ASN N N 118.445 . 1 1151 132 132 GLU H H 8.578 . 1 1152 132 132 GLU HA H 4.229 . 1 1153 132 132 GLU HB2 H 2.063 . 2 1154 132 132 GLU HB3 H 1.956 . 2 1155 132 132 GLU HG2 H 2.253 . 2 1156 132 132 GLU HG3 H 2.253 . 2 1157 132 132 GLU C C 176.915 . 1 1158 132 132 GLU CA C 57.393 . 1 1159 132 132 GLU CB C 29.908 . 1 1160 132 132 GLU CG C 36.377 . 1 1161 132 132 GLU N N 120.936 . 1 1162 133 133 GLU H H 8.450 . 1 1163 133 133 GLU HA H 4.231 . 1 1164 133 133 GLU HB2 H 2.048 . 2 1165 133 133 GLU HB3 H 1.990 . 2 1166 133 133 GLU HG2 H 2.254 . 2 1167 133 133 GLU HG3 H 2.254 . 2 1168 133 133 GLU C C 177.202 . 1 1169 133 133 GLU CA C 57.308 . 1 1170 133 133 GLU CB C 29.979 . 1 1171 133 133 GLU CG C 36.327 . 1 1172 133 133 GLU N N 120.972 . 1 1173 134 134 SER H H 8.284 . 1 1174 134 134 SER HA H 4.411 . 1 1175 134 134 SER HB2 H 3.899 . 2 1176 134 134 SER HB3 H 3.899 . 2 1177 134 134 SER C C 175.272 . 1 1178 134 134 SER CA C 59.194 . 1 1179 134 134 SER CB C 63.617 . 1 1180 134 134 SER N N 115.859 . 1 1181 135 135 THR H H 8.025 . 1 1182 135 135 THR HA H 4.362 . 1 1183 135 135 THR HB H 4.282 . 1 1184 135 135 THR HG2 H 1.189 . 1 1185 135 135 THR C C 174.889 . 1 1186 135 135 THR CA C 62.367 . 1 1187 135 135 THR CB C 69.426 . 1 1188 135 135 THR CG2 C 21.818 . 1 1189 135 135 THR N N 114.665 . 1 1190 136 136 LYS H H 8.172 . 1 1191 136 136 LYS HA H 4.363 . 1 1192 136 136 LYS HB2 H 1.864 . 2 1193 136 136 LYS HB3 H 1.793 . 2 1194 136 136 LYS HG2 H 1.381 . 2 1195 136 136 LYS HG3 H 1.443 . 2 1196 136 136 LYS HD2 H 1.633 . 2 1197 136 136 LYS HD3 H 1.633 . 2 1198 136 136 LYS HE2 H 2.946 . 2 1199 136 136 LYS HE3 H 2.946 . 2 1200 136 136 LYS C C 176.927 . 1 1201 136 136 LYS CA C 56.792 . 1 1202 136 136 LYS CB C 32.922 . 1 1203 136 136 LYS CG C 24.874 . 1 1204 136 136 LYS CD C 29.181 . 1 1205 136 136 LYS CE C 42.189 . 1 1206 136 136 LYS N N 122.742 . 1 1207 137 137 THR H H 8.076 . 1 1208 137 137 THR HA H 4.310 . 1 1209 137 137 THR HB H 4.235 . 1 1210 137 137 THR HG2 H 1.160 . 1 1211 137 137 THR C C 175.275 . 1 1212 137 137 THR CA C 62.004 . 1 1213 137 137 THR CB C 69.894 . 1 1214 137 137 THR CG2 C 21.638 . 1 1215 137 137 THR N N 113.196 . 1 1216 138 138 GLY H H 8.368 . 1 1217 138 138 GLY HA2 H 3.954 . 2 1218 138 138 GLY HA3 H 3.954 . 2 1219 138 138 GLY C C 174.031 . 1 1220 138 138 GLY CA C 45.531 . 1 1221 138 138 GLY N N 111.038 . 1 1222 139 139 ASN H H 8.313 . 1 1223 139 139 ASN HA H 4.667 . 1 1224 139 139 ASN HB2 H 2.785 . 2 1225 139 139 ASN HB3 H 2.785 . 2 1226 139 139 ASN C C 175.025 . 1 1227 139 139 ASN CA C 53.349 . 1 1228 139 139 ASN CB C 39.099 . 1 1229 139 139 ASN N N 118.452 . 1 1230 140 140 ALA H H 8.318 . 1 1231 140 140 ALA HA H 4.181 . 1 1232 140 140 ALA HB H 1.167 . 1 1233 140 140 ALA C C 177.708 . 1 1234 140 140 ALA CA C 52.936 . 1 1235 140 140 ALA CB C 18.463 . 1 1236 140 140 ALA N N 123.754 . 1 1237 141 141 GLY H H 8.234 . 1 1238 141 141 GLY HA2 H 3.916 . 2 1239 141 141 GLY HA3 H 4.046 . 2 1240 141 141 GLY C C 174.814 . 1 1241 141 141 GLY CA C 45.261 . 1 1242 141 141 GLY N N 106.429 . 1 1243 142 142 SER H H 8.630 . 1 1244 142 142 SER HA H 4.412 . 1 1245 142 142 SER HB2 H 3.895 . 2 1246 142 142 SER HB3 H 3.895 . 2 1247 142 142 SER C C 174.218 . 1 1248 142 142 SER CA C 59.122 . 1 1249 142 142 SER CB C 64.066 . 1 1250 142 142 SER N N 117.063 . 1 1251 143 143 ARG H H 8.604 . 1 1252 143 143 ARG HA H 3.965 . 1 1253 143 143 ARG HB2 H 1.800 . 2 1254 143 143 ARG HB3 H 1.384 . 2 1255 143 143 ARG HG2 H 1.212 . 2 1256 143 143 ARG HG3 H 1.377 . 2 1257 143 143 ARG HD2 H 2.951 . 2 1258 143 143 ARG HD3 H 3.031 . 2 1259 143 143 ARG C C 175.537 . 1 1260 143 143 ARG CA C 56.195 . 1 1261 143 143 ARG CB C 30.148 . 1 1262 143 143 ARG CG C 27.083 . 1 1263 143 143 ARG CD C 43.839 . 1 1264 143 143 ARG N N 121.605 . 1 1265 144 144 LEU H H 8.576 . 1 1266 144 144 LEU HA H 4.343 . 1 1267 144 144 LEU HB2 H 1.261 . 1 1268 144 144 LEU HB3 H 1.460 . 1 1269 144 144 LEU HD1 H 0.781 . 2 1270 144 144 LEU HD2 H 0.781 . 2 1271 144 144 LEU C C 177.000 . 1 1272 144 144 LEU CA C 55.938 . 1 1273 144 144 LEU CB C 43.537 . 1 1274 144 144 LEU CG C 27.020 . 1 1275 144 144 LEU CD1 C 22.927 . 2 1276 144 144 LEU CD2 C 27.056 . 2 1277 144 144 LEU N N 123.582 . 1 1278 145 145 ALA H H 7.498 . 1 1279 145 145 ALA HA H 4.454 . 1 1280 145 145 ALA HB H 0.937 . 1 1281 145 145 ALA C C 175.154 . 1 1282 145 145 ALA CA C 51.513 . 1 1283 145 145 ALA CB C 21.726 . 1 1284 145 145 ALA N N 116.745 . 1 1285 146 146 CYS H H 8.555 . 1 1286 146 146 CYS HA H 5.932 . 1 1287 146 146 CYS HB2 H 2.808 . 2 1288 146 146 CYS HB3 H 2.808 . 2 1289 146 146 CYS C C 174.409 . 1 1290 146 146 CYS CA C 55.862 . 1 1291 146 146 CYS CB C 32.468 . 1 1292 146 146 CYS N N 114.487 . 1 1293 147 147 GLY H H 8.568 . 1 1294 147 147 GLY HA2 H 3.996 . 2 1295 147 147 GLY HA3 H 4.447 . 2 1296 147 147 GLY C C 171.478 . 1 1297 147 147 GLY CA C 46.440 . 1 1298 147 147 GLY N N 108.921 . 1 1299 148 148 VAL H H 8.795 . 1 1300 148 148 VAL HA H 4.249 . 1 1301 148 148 VAL HB H 1.916 . 1 1302 148 148 VAL HG1 H 0.781 . 2 1303 148 148 VAL HG2 H 0.788 . 2 1304 148 148 VAL C C 176.130 . 1 1305 148 148 VAL CA C 62.895 . 1 1306 148 148 VAL CB C 32.406 . 1 1307 148 148 VAL CG1 C 20.946 . 2 1308 148 148 VAL CG2 C 22.284 . 2 1309 148 148 VAL N N 125.078 . 1 1310 149 149 ILE H H 8.720 . 1 1311 149 149 ILE HA H 3.989 . 1 1312 149 149 ILE HB H 1.780 . 1 1313 149 149 ILE HG12 H 0.516 . 2 1314 149 149 ILE HG13 H 0.516 . 2 1315 149 149 ILE HG2 H 0.076 . 1 1316 149 149 ILE HD1 H 0.421 . 1 1317 149 149 ILE C C 175.760 . 1 1318 149 149 ILE CA C 62.221 . 1 1319 149 149 ILE CB C 37.556 . 1 1320 149 149 ILE CG1 C 28.333 . 1 1321 149 149 ILE CG2 C 18.332 . 1 1322 149 149 ILE CD1 C 15.163 . 1 1323 149 149 ILE N N 128.983 . 1 1324 150 150 GLY H H 8.848 . 1 1325 150 150 GLY HA2 H 3.811 . 2 1326 150 150 GLY HA3 H 4.765 . 2 1327 150 150 GLY C C 172.492 . 1 1328 150 150 GLY CA C 43.651 . 1 1329 150 150 GLY N N 117.675 . 1 1330 151 151 ILE H H 8.536 . 1 1331 151 151 ILE HA H 4.191 . 1 1332 151 151 ILE HB H 1.848 . 1 1333 151 151 ILE HG12 H 1.352 . 2 1334 151 151 ILE HG13 H 1.665 . 2 1335 151 151 ILE HG2 H 1.005 . 1 1336 151 151 ILE HD1 H 0.947 . 1 1337 151 151 ILE C C 175.474 . 1 1338 151 151 ILE CA C 61.498 . 1 1339 151 151 ILE CB C 38.335 . 1 1340 151 151 ILE CG1 C 28.367 . 1 1341 151 151 ILE CG2 C 17.650 . 1 1342 151 151 ILE CD1 C 12.381 . 1 1343 151 151 ILE N N 121.153 . 1 1344 152 152 ALA H H 8.313 . 1 1345 152 152 ALA HA H 4.577 . 1 1346 152 152 ALA HB H 1.231 . 1 1347 152 152 ALA C C 175.399 . 1 1348 152 152 ALA CA C 51.172 . 1 1349 152 152 ALA CB C 20.555 . 1 1350 152 152 ALA N N 131.163 . 1 1351 153 153 GLN H H 8.037 . 1 1352 153 153 GLN C C 172.718 . 1 1353 153 153 GLN CA C 57.346 . 1 1354 153 153 GLN CB C 30.637 . 1 1355 153 153 GLN N N 124.923 . 1 stop_ save_