data_11341 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Solution structure of the RING domain of the human tripartite motif-containing protein 39 ; _BMRB_accession_number 11341 _BMRB_flat_file_name bmr11341.str _Entry_type original _Submission_date 2010-08-10 _Accession_date 2010-08-10 _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 Miyamoto K. . . 2 Sato M. . . 3 Koshiba S. . . 4 Watanabe S. . . 5 Harada T. . . 6 Kigawa T. . . 7 Yokoyama S. . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 309 "13C chemical shifts" 234 "15N chemical shifts" 53 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2011-08-19 original author . stop_ _Original_release_date 2011-08-19 save_ ############################# # Citation for this entry # ############################# save_citation_1 _Saveframe_category entry_citation _Citation_full . _Citation_title ; Solution structure of the RING domain of the human tripartite motif-containing protein 39 ; _Citation_status 'in preparation' _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 Miyamoto K. . . 2 Sato M. . . 3 Koshiba S. . . 4 Watanabe S. . . 5 Harada T. . . 6 Kigawa T. . . 7 Yokoyama S. . . stop_ _Journal_abbreviation . _Journal_volume . _Journal_issue . _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first . _Page_last . _Year . _Details . save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name 'Tripartite motif-containing protein 39' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'RING domain' $entity_1 'ZINC ION no.1' $ZN 'ZINC ION no.2' $ZN 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_entity_1 _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'RING domain' _Molecular_mass . _Mol_thiol_state 'all other bound' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 58 _Mol_residue_sequence ; GSSGSSGALENLQVEASCSV CLEYLKEPVIIECGHNFCKA CITRWWEDLERDFPCPVC ; loop_ _Residue_seq_code _Residue_label 1 GLY 2 SER 3 SER 4 GLY 5 SER 6 SER 7 GLY 8 ALA 9 LEU 10 GLU 11 ASN 12 LEU 13 GLN 14 VAL 15 GLU 16 ALA 17 SER 18 CYS 19 SER 20 VAL 21 CYS 22 LEU 23 GLU 24 TYR 25 LEU 26 LYS 27 GLU 28 PRO 29 VAL 30 ILE 31 ILE 32 GLU 33 CYS 34 GLY 35 HIS 36 ASN 37 PHE 38 CYS 39 LYS 40 ALA 41 CYS 42 ILE 43 THR 44 ARG 45 TRP 46 TRP 47 GLU 48 ASP 49 LEU 50 GLU 51 ARG 52 ASP 53 PHE 54 PRO 55 CYS 56 PRO 57 VAL 58 CYS stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-07-08 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 PDB 2ECJ "Solution Structure Of The Ring Domain Of The Human Tripartite Motif-Containing Protein 39" 100.00 58 100.00 100.00 2.01e-33 DBJ BAB16374 "testis-abundant finger protein [Homo sapiens]" 86.21 518 100.00 100.00 5.28e-27 DBJ BAB16375 "testis-abundant finger protein [Mus musculus]" 86.21 488 100.00 100.00 4.53e-27 DBJ BAC35409 "unnamed protein product [Mus musculus]" 86.21 264 100.00 100.00 5.26e-28 DBJ BAD13703 "TRIM39 protein [Homo sapiens]" 86.21 518 100.00 100.00 4.91e-27 DBJ BAD13704 "TRIM39 protein [Homo sapiens]" 86.21 518 100.00 100.00 5.01e-27 EMBL CAE84052 "tripartite motif-containing 39 [Rattus norvegicus]" 86.21 488 100.00 100.00 4.35e-27 EMBL CAH90337 "hypothetical protein [Pongo abelii]" 86.21 488 100.00 100.00 4.13e-27 GB AAH07661 "TRIM39 protein [Homo sapiens]" 86.21 488 100.00 100.00 3.58e-27 GB AAH31540 "Trim39 protein [Mus musculus]" 86.21 496 100.00 100.00 5.76e-27 GB AAH34985 "Tripartite motif-containing 39 [Homo sapiens]" 86.21 488 100.00 100.00 3.58e-27 GB AAP36034 "tripartite motif-containing 39 [Homo sapiens]" 86.21 488 100.00 100.00 3.58e-27 GB AAP36295 "Homo sapiens tripartite motif-containing 39 [synthetic construct]" 86.21 489 100.00 100.00 3.58e-27 REF NP_001065263 "E3 ubiquitin-protein ligase TRIM39 [Pan troglodytes]" 86.21 518 100.00 100.00 5.33e-27 REF NP_001121951 "tripartite motif-containing protein 39 [Sus scrofa]" 86.21 488 100.00 100.00 3.66e-27 REF NP_001125160 "tripartite motif-containing protein 39 [Pongo abelii]" 86.21 488 100.00 100.00 4.13e-27 REF NP_001186048 "TRIM39-RPP21 protein [Homo sapiens]" 86.21 503 100.00 100.00 2.89e-27 REF NP_067076 "E3 ubiquitin-protein ligase TRIM39 isoform 1 [Homo sapiens]" 86.21 518 100.00 100.00 5.01e-27 SP Q1XHU0 "RecName: Full=E3 ubiquitin-protein ligase TRIM39; AltName: Full=Tripartite motif-containing protein 39" 86.21 518 100.00 100.00 5.07e-27 SP Q6MFZ5 "RecName: Full=E3 ubiquitin-protein ligase TRIM39; AltName: Full=RING finger protein 23; AltName: Full=Tripartite motif-containi" 86.21 488 100.00 100.00 4.35e-27 SP Q9ESN2 "RecName: Full=E3 ubiquitin-protein ligase TRIM39; AltName: Full=RING finger protein 23; AltName: Full=Testis-abundant finger pr" 86.21 488 100.00 100.00 4.53e-27 SP Q9HCM9 "RecName: Full=E3 ubiquitin-protein ligase TRIM39; AltName: Full=RING finger protein 23; AltName: Full=Testis-abundant finger pr" 86.21 518 100.00 100.00 5.01e-27 stop_ save_ ############# # Ligands # ############# save_ZN _Saveframe_category ligand _Mol_type non-polymer _Name_common "ZN (ZINC ION)" _BMRB_code . _PDB_code ZN _Molecular_mass 65.409 _Mol_charge 2 _Mol_paramagnetic . _Mol_aromatic no _Details ; Information obtained from PDB's Chemical Component Dictionary at http://wwpdb-remediation.rutgers.edu/downloads.html Downloaded on Tue Jun 9 16:52:42 2009 ; loop_ _Atom_name _PDB_atom_name _Atom_type _Atom_chirality _Atom_charge _Atom_oxidation_number _Atom_unpaired_electrons ZN ZN ZN . 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 $entity_1 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_type _Vector_name $entity_1 'cell free synthesis' 'E. coli' Escherichia coli . plasmid P060828-17 stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Saveframe_category sample _Sample_type solution _Details ; 1.06mM RING domain U-13C, {15N;} 20mM {d-Tris-HCl(pH7.0);} 100mM {NaCl;} 1mM {d-DTT;} 0.02% {NaN3;} 0.05mM {ZNCl2;} 1.0mM {IDA;} 90% H2O, 10% D2O ; loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $entity_1 1.06 mM '[U-13C; U-15N]' d-Tris-HCl 20 mM 'natural abundance' NaCl 100 mM 'natural abundance' d-DTT 1 mM 'natural abundance' NaN3 0.02 % 'natural abundance' ZnCl2 0.05 mM 'natural abundance' IDA 1.0 mM 'natural abundance' H2O 90 % . D2O 10 % . stop_ save_ ############################ # Computer software used # ############################ save_XWINNMR _Saveframe_category software _Name xwinnmr _Version 3.5 loop_ _Vendor _Address _Electronic_address Bruker . . stop_ loop_ _Task collection stop_ _Details . save_ save_NMRPipe _Saveframe_category software _Name NMRPipe _Version 20031121 loop_ _Vendor _Address _Electronic_address 'Delaglio, F.' . . stop_ loop_ _Task processing stop_ _Details . save_ save_NMRView _Saveframe_category software _Name NMRView _Version 5.0.4 loop_ _Vendor _Address _Electronic_address 'Johnson, B. A.' . . stop_ loop_ _Task 'data analysis' stop_ _Details . save_ save_Kujira _Saveframe_category software _Name Kujira _Version 0.9820 loop_ _Vendor _Address _Electronic_address 'Kobayashi, N.' . . stop_ loop_ _Task 'data analysis' stop_ _Details . save_ save_CYANA _Saveframe_category software _Name CYANA _Version 2.0.17 loop_ _Vendor _Address _Electronic_address 'Guntert, P.' . . stop_ loop_ _Task refinement 'structure solution' stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model AVANCE _Field_strength 800 _Details . save_ ############################# # NMR applied experiments # ############################# save_3D_13C-separated_NOESY_1 _Saveframe_category NMR_applied_experiment _Experiment_name '3D 13C-separated NOESY' _Sample_label $sample_1 save_ save_3D_15N-separated_NOESY_2 _Saveframe_category NMR_applied_experiment _Experiment_name '3D 15N-separated NOESY' _Sample_label $sample_1 save_ ####################### # Sample conditions # ####################### save_condition_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units 'ionic strength' 120 0.1 mM pH 7.0 0.05 pH pressure 1 0.001 atm temperature 298 0.1 K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_reference_1 _Saveframe_category chemical_shift_reference _Details ; Chemical shift reference of 1H was based on the proton of water (4.784ppm at 298K) and then those of 15N and 13C were calculated based on their gyromagnetic ratios. ; loop_ _Mol_common_name _Atom_type _Atom_isotope_number _Atom_group _Chem_shift_units _Chem_shift_value _Reference_method _Reference_type _External_reference_sample_geometry _External_reference_location _External_reference_axis _Indirect_shift_ratio DSS C 13 'methyl protons' ppm 0.0 . indirect . . . 0.251449530 DSS H 1 'methyl protons' ppm 0.0 . indirect . . . 1.0 DSS N 15 'methyl protons' ppm 0.0 . 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_chemical_shift_1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Software_label $XWINNMR $NMRPipe $NMRView $Kujira $CYANA stop_ loop_ _Experiment_label '3D 13C-separated NOESY' '3D 15N-separated NOESY' stop_ loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $condition_1 _Chem_shift_reference_set_label $reference_1 _Mol_system_component_name 'RING domain' _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 7 7 GLY HA2 H 3.974 0.030 1 2 7 7 GLY HA3 H 3.974 0.030 1 3 7 7 GLY C C 173.941 0.300 1 4 7 7 GLY CA C 45.388 0.300 1 5 8 8 ALA H H 8.115 0.030 1 6 8 8 ALA HA H 4.327 0.030 1 7 8 8 ALA HB H 1.403 0.030 1 8 8 8 ALA C C 177.930 0.300 1 9 8 8 ALA CA C 52.624 0.300 1 10 8 8 ALA CB C 19.293 0.300 1 11 8 8 ALA N N 123.751 0.300 1 12 9 9 LEU H H 8.227 0.030 1 13 9 9 LEU HA H 4.327 0.030 1 14 9 9 LEU HB2 H 1.594 0.030 2 15 9 9 LEU HB3 H 1.660 0.030 2 16 9 9 LEU HD1 H 0.929 0.030 1 17 9 9 LEU HD2 H 0.870 0.030 1 18 9 9 LEU HG H 1.669 0.030 1 19 9 9 LEU C C 177.634 0.300 1 20 9 9 LEU CA C 55.368 0.300 1 21 9 9 LEU CB C 42.279 0.300 1 22 9 9 LEU CD1 C 25.069 0.300 2 23 9 9 LEU CD2 C 23.507 0.300 2 24 9 9 LEU CG C 27.043 0.300 1 25 9 9 LEU N N 121.016 0.300 1 26 10 10 GLU H H 8.329 0.030 1 27 10 10 GLU HA H 4.244 0.030 1 28 10 10 GLU HB2 H 1.970 0.030 2 29 10 10 GLU HB3 H 2.151 0.030 2 30 10 10 GLU HG2 H 2.262 0.030 2 31 10 10 GLU HG3 H 2.168 0.030 2 32 10 10 GLU C C 176.157 0.300 1 33 10 10 GLU CA C 56.727 0.300 1 34 10 10 GLU CB C 29.794 0.300 1 35 10 10 GLU CG C 36.660 0.300 1 36 10 10 GLU N N 120.913 0.300 1 37 11 11 ASN H H 8.389 0.030 1 38 11 11 ASN HA H 4.695 0.030 1 39 11 11 ASN HB2 H 2.858 0.030 2 40 11 11 ASN HB3 H 2.734 0.030 2 41 11 11 ASN HD21 H 7.583 0.030 2 42 11 11 ASN HD22 H 6.896 0.030 2 43 11 11 ASN C C 174.943 0.300 1 44 11 11 ASN CA C 53.222 0.300 1 45 11 11 ASN CB C 38.668 0.300 1 46 11 11 ASN N N 119.030 0.300 1 47 11 11 ASN ND2 N 112.720 0.300 1 48 12 12 LEU H H 8.147 0.030 1 49 12 12 LEU HA H 4.332 0.030 1 50 12 12 LEU HB2 H 1.588 0.030 2 51 12 12 LEU HB3 H 1.653 0.030 2 52 12 12 LEU HD1 H 0.867 0.030 1 53 12 12 LEU HD2 H 0.939 0.030 1 54 12 12 LEU HG H 1.594 0.030 1 55 12 12 LEU C C 177.175 0.300 1 56 12 12 LEU CA C 55.335 0.300 1 57 12 12 LEU CB C 42.403 0.300 1 58 12 12 LEU CD1 C 23.602 0.300 2 59 12 12 LEU CD2 C 25.024 0.300 2 60 12 12 LEU CG C 27.069 0.300 1 61 12 12 LEU N N 122.467 0.300 1 62 13 13 GLN H H 8.344 0.030 1 63 13 13 GLN HA H 4.378 0.030 1 64 13 13 GLN HB2 H 2.100 0.030 2 65 13 13 GLN HB3 H 1.996 0.030 2 66 13 13 GLN HE21 H 6.845 0.030 2 67 13 13 GLN HE22 H 7.550 0.030 2 68 13 13 GLN HG2 H 2.344 0.030 1 69 13 13 GLN HG3 H 2.344 0.030 1 70 13 13 GLN C C 175.676 0.300 1 71 13 13 GLN CA C 55.720 0.300 1 72 13 13 GLN CB C 29.335 0.300 1 73 13 13 GLN CG C 33.850 0.300 1 74 13 13 GLN N N 121.482 0.300 1 75 13 13 GLN NE2 N 112.584 0.300 1 76 14 14 VAL H H 8.111 0.030 1 77 14 14 VAL HA H 4.121 0.030 1 78 14 14 VAL HB H 2.063 0.030 1 79 14 14 VAL HG1 H 0.920 0.030 1 80 14 14 VAL HG2 H 0.923 0.030 1 81 14 14 VAL C C 175.921 0.300 1 82 14 14 VAL CA C 62.206 0.300 1 83 14 14 VAL CB C 32.931 0.300 1 84 14 14 VAL CG1 C 21.218 0.300 2 85 14 14 VAL CG2 C 20.366 0.300 2 86 14 14 VAL N N 121.604 0.300 1 87 15 15 GLU H H 8.384 0.030 1 88 15 15 GLU HA H 4.358 0.030 1 89 15 15 GLU HB2 H 1.868 0.030 2 90 15 15 GLU HB3 H 2.056 0.030 2 91 15 15 GLU HG2 H 2.249 0.030 1 92 15 15 GLU HG3 H 2.249 0.030 1 93 15 15 GLU C C 175.569 0.300 1 94 15 15 GLU CA C 56.372 0.300 1 95 15 15 GLU CB C 30.721 0.300 1 96 15 15 GLU CG C 36.403 0.300 1 97 15 15 GLU N N 124.503 0.300 1 98 16 16 ALA H H 8.378 0.030 1 99 16 16 ALA HA H 4.431 0.030 1 100 16 16 ALA HB H 1.355 0.030 1 101 16 16 ALA C C 175.885 0.300 1 102 16 16 ALA CA C 51.975 0.300 1 103 16 16 ALA CB C 20.322 0.300 1 104 16 16 ALA N N 125.199 0.300 1 105 17 17 SER H H 7.984 0.030 1 106 17 17 SER HA H 5.025 0.030 1 107 17 17 SER HB2 H 3.319 0.030 2 108 17 17 SER HB3 H 3.237 0.030 2 109 17 17 SER C C 173.119 0.300 1 110 17 17 SER CA C 56.248 0.300 1 111 17 17 SER CB C 65.882 0.300 1 112 17 17 SER N N 113.153 0.300 1 113 18 18 CYS H H 8.648 0.030 1 114 18 18 CYS HA H 3.861 0.030 1 115 18 18 CYS HB2 H 2.813 0.030 2 116 18 18 CYS HB3 H 3.426 0.030 2 117 18 18 CYS C C 177.644 0.300 1 118 18 18 CYS CA C 60.153 0.300 1 119 18 18 CYS CB C 31.202 0.300 1 120 18 18 CYS N N 123.957 0.300 1 121 19 19 SER H H 8.775 0.030 1 122 19 19 SER HA H 4.078 0.030 1 123 19 19 SER HB2 H 3.305 0.030 2 124 19 19 SER HB3 H 3.762 0.030 2 125 19 19 SER C C 173.246 0.300 1 126 19 19 SER CA C 62.088 0.300 1 127 19 19 SER CB C 64.135 0.300 1 128 19 19 SER N N 125.978 0.300 1 129 20 20 VAL H H 9.074 0.030 1 130 20 20 VAL HA H 4.058 0.030 1 131 20 20 VAL HB H 2.695 0.030 1 132 20 20 VAL HG1 H 1.004 0.030 1 133 20 20 VAL HG2 H 0.928 0.030 1 134 20 20 VAL C C 176.524 0.300 1 135 20 20 VAL CA C 65.066 0.300 1 136 20 20 VAL CB C 32.597 0.300 1 137 20 20 VAL CG1 C 21.800 0.300 2 138 20 20 VAL CG2 C 22.114 0.300 2 139 20 20 VAL N N 122.114 0.300 1 140 21 21 CYS H H 8.405 0.030 1 141 21 21 CYS HA H 4.750 0.030 1 142 21 21 CYS HB2 H 3.305 0.030 2 143 21 21 CYS HB3 H 2.710 0.030 2 144 21 21 CYS C C 176.519 0.300 1 145 21 21 CYS CA C 60.011 0.300 1 146 21 21 CYS CB C 31.859 0.300 1 147 21 21 CYS N N 119.186 0.300 1 148 22 22 LEU H H 7.601 0.030 1 149 22 22 LEU HA H 4.195 0.030 1 150 22 22 LEU HB2 H 1.657 0.030 2 151 22 22 LEU HB3 H 2.133 0.030 2 152 22 22 LEU HD1 H 0.853 0.030 1 153 22 22 LEU HD2 H 0.772 0.030 1 154 22 22 LEU HG H 1.380 0.030 1 155 22 22 LEU C C 176.142 0.300 1 156 22 22 LEU CA C 57.224 0.300 1 157 22 22 LEU CB C 38.418 0.300 1 158 22 22 LEU CD1 C 25.104 0.300 2 159 22 22 LEU CD2 C 22.535 0.300 2 160 22 22 LEU CG C 27.520 0.300 1 161 22 22 LEU N N 116.918 0.300 1 162 23 23 GLU H H 8.122 0.030 1 163 23 23 GLU HA H 4.217 0.030 1 164 23 23 GLU HB2 H 1.977 0.030 2 165 23 23 GLU HB3 H 2.162 0.030 2 166 23 23 GLU HG2 H 2.366 0.030 2 167 23 23 GLU HG3 H 2.535 0.030 2 168 23 23 GLU C C 176.506 0.300 1 169 23 23 GLU CA C 57.136 0.300 1 170 23 23 GLU CB C 31.021 0.300 1 171 23 23 GLU CG C 36.931 0.300 1 172 23 23 GLU N N 121.721 0.300 1 173 24 24 TYR H H 8.498 0.030 1 174 24 24 TYR HA H 4.618 0.030 1 175 24 24 TYR HB2 H 2.979 0.030 2 176 24 24 TYR HB3 H 2.952 0.030 2 177 24 24 TYR HD1 H 7.116 0.030 1 178 24 24 TYR HD2 H 7.116 0.030 1 179 24 24 TYR HE1 H 6.801 0.030 1 180 24 24 TYR HE2 H 6.801 0.030 1 181 24 24 TYR C C 176.283 0.300 1 182 24 24 TYR CA C 59.062 0.300 1 183 24 24 TYR CB C 38.421 0.300 1 184 24 24 TYR CD1 C 133.159 0.300 1 185 24 24 TYR CD2 C 133.159 0.300 1 186 24 24 TYR CE1 C 118.140 0.300 1 187 24 24 TYR CE2 C 118.140 0.300 1 188 24 24 TYR N N 122.329 0.300 1 189 25 25 LEU H H 8.143 0.030 1 190 25 25 LEU HA H 4.455 0.030 1 191 25 25 LEU HB2 H 0.989 0.030 2 192 25 25 LEU HB3 H 1.457 0.030 2 193 25 25 LEU HD1 H 0.619 0.030 1 194 25 25 LEU HD2 H 0.734 0.030 1 195 25 25 LEU HG H 1.514 0.030 1 196 25 25 LEU C C 175.078 0.300 1 197 25 25 LEU CA C 53.770 0.300 1 198 25 25 LEU CB C 43.973 0.300 1 199 25 25 LEU CD1 C 25.792 0.300 2 200 25 25 LEU CD2 C 24.135 0.300 2 201 25 25 LEU CG C 26.179 0.300 1 202 25 25 LEU N N 124.512 0.300 1 203 26 26 LYS H H 8.181 0.030 1 204 26 26 LYS HA H 4.303 0.030 1 205 26 26 LYS HB2 H 1.897 0.030 2 206 26 26 LYS HB3 H 1.845 0.030 2 207 26 26 LYS HD2 H 1.772 0.030 1 208 26 26 LYS HD3 H 1.772 0.030 1 209 26 26 LYS HE2 H 3.066 0.030 1 210 26 26 LYS HE3 H 3.066 0.030 1 211 26 26 LYS HG2 H 1.579 0.030 2 212 26 26 LYS HG3 H 1.524 0.030 2 213 26 26 LYS C C 175.077 0.300 1 214 26 26 LYS CA C 57.209 0.300 1 215 26 26 LYS CB C 33.313 0.300 1 216 26 26 LYS CD C 29.023 0.300 1 217 26 26 LYS CE C 42.208 0.300 1 218 26 26 LYS CG C 25.113 0.300 1 219 26 26 LYS N N 122.802 0.300 1 220 27 27 GLU H H 8.104 0.030 1 221 27 27 GLU HA H 4.740 0.030 1 222 27 27 GLU HB2 H 1.940 0.030 2 223 27 27 GLU HB3 H 2.035 0.030 2 224 27 27 GLU HG2 H 2.202 0.030 2 225 27 27 GLU HG3 H 2.144 0.030 2 226 27 27 GLU CA C 53.586 0.300 1 227 27 27 GLU CB C 30.295 0.300 1 228 27 27 GLU CG C 36.214 0.300 1 229 27 27 GLU N N 117.489 0.300 1 230 28 28 PRO HA H 4.280 0.030 1 231 28 28 PRO HB2 H 1.894 0.030 2 232 28 28 PRO HB3 H 1.770 0.030 2 233 28 28 PRO HD2 H 3.184 0.030 2 234 28 28 PRO HD3 H 3.701 0.030 2 235 28 28 PRO HG2 H 1.969 0.030 2 236 28 28 PRO HG3 H 1.830 0.030 2 237 28 28 PRO C C 176.416 0.300 1 238 28 28 PRO CA C 63.171 0.300 1 239 28 28 PRO CB C 32.865 0.300 1 240 28 28 PRO CD C 50.483 0.300 1 241 28 28 PRO CG C 26.891 0.300 1 242 29 29 VAL H H 8.893 0.030 1 243 29 29 VAL HA H 4.147 0.030 1 244 29 29 VAL HB H 2.053 0.030 1 245 29 29 VAL HG1 H 0.936 0.030 1 246 29 29 VAL HG2 H 0.975 0.030 1 247 29 29 VAL C C 175.055 0.300 1 248 29 29 VAL CA C 63.081 0.300 1 249 29 29 VAL CB C 32.029 0.300 1 250 29 29 VAL CG1 C 21.202 0.300 2 251 29 29 VAL CG2 C 20.814 0.300 2 252 29 29 VAL N N 122.730 0.300 1 253 30 30 ILE H H 8.534 0.030 1 254 30 30 ILE HA H 4.747 0.030 1 255 30 30 ILE HB H 1.707 0.030 1 256 30 30 ILE HD1 H 0.858 0.030 1 257 30 30 ILE HG12 H 1.431 0.030 2 258 30 30 ILE HG13 H 0.990 0.030 2 259 30 30 ILE HG2 H 0.880 0.030 1 260 30 30 ILE C C 177.209 0.300 1 261 30 30 ILE CA C 61.153 0.300 1 262 30 30 ILE CB C 39.306 0.300 1 263 30 30 ILE CD1 C 13.818 0.300 1 264 30 30 ILE CG1 C 27.316 0.300 1 265 30 30 ILE CG2 C 17.134 0.300 1 266 30 30 ILE N N 128.293 0.300 1 267 31 31 ILE H H 7.831 0.030 1 268 31 31 ILE HA H 4.909 0.030 1 269 31 31 ILE HB H 2.559 0.030 1 270 31 31 ILE HD1 H 1.069 0.030 1 271 31 31 ILE HG12 H 2.140 0.030 2 272 31 31 ILE HG13 H 1.585 0.030 2 273 31 31 ILE HG2 H 1.129 0.030 1 274 31 31 ILE C C 178.761 0.300 1 275 31 31 ILE CA C 60.716 0.300 1 276 31 31 ILE CB C 38.092 0.300 1 277 31 31 ILE CD1 C 13.912 0.300 1 278 31 31 ILE CG1 C 27.069 0.300 1 279 31 31 ILE CG2 C 18.921 0.300 1 280 31 31 ILE N N 122.084 0.300 1 281 32 32 GLU H H 8.909 0.030 1 282 32 32 GLU HA H 4.008 0.030 1 283 32 32 GLU HB2 H 2.204 0.030 2 284 32 32 GLU HB3 H 2.126 0.030 2 285 32 32 GLU HG2 H 2.437 0.030 2 286 32 32 GLU HG3 H 2.401 0.030 2 287 32 32 GLU C C 176.601 0.300 1 288 32 32 GLU CA C 61.010 0.300 1 289 32 32 GLU CB C 29.660 0.300 1 290 32 32 GLU CG C 36.435 0.300 1 291 32 32 GLU N N 121.427 0.300 1 292 33 33 CYS H H 7.730 0.030 1 293 33 33 CYS HA H 4.492 0.030 1 294 33 33 CYS HB2 H 2.908 0.030 1 295 33 33 CYS HB3 H 2.908 0.030 1 296 33 33 CYS C C 176.373 0.300 1 297 33 33 CYS CA C 58.105 0.300 1 298 33 33 CYS CB C 30.714 0.300 1 299 33 33 CYS N N 114.842 0.300 1 300 34 34 GLY H H 8.432 0.030 1 301 34 34 GLY HA2 H 3.511 0.030 2 302 34 34 GLY HA3 H 4.234 0.030 2 303 34 34 GLY C C 174.439 0.300 1 304 34 34 GLY CA C 44.809 0.300 1 305 34 34 GLY N N 111.285 0.300 1 306 35 35 HIS H H 8.366 0.030 1 307 35 35 HIS HA H 4.423 0.030 1 308 35 35 HIS HB2 H 2.752 0.030 2 309 35 35 HIS HB3 H 3.241 0.030 2 310 35 35 HIS HD2 H 7.227 0.030 1 311 35 35 HIS HE1 H 8.023 0.030 1 312 35 35 HIS C C 173.268 0.300 1 313 35 35 HIS CA C 61.173 0.300 1 314 35 35 HIS CB C 31.010 0.300 1 315 35 35 HIS CD2 C 118.655 0.300 1 316 35 35 HIS CE1 C 138.421 0.300 1 317 35 35 HIS N N 122.889 0.300 1 318 36 36 ASN H H 8.390 0.030 1 319 36 36 ASN HA H 5.472 0.030 1 320 36 36 ASN HB2 H 2.134 0.030 2 321 36 36 ASN HB3 H 2.773 0.030 2 322 36 36 ASN HD21 H 7.024 0.030 2 323 36 36 ASN HD22 H 6.596 0.030 2 324 36 36 ASN C C 175.229 0.300 1 325 36 36 ASN CA C 51.604 0.300 1 326 36 36 ASN CB C 41.957 0.300 1 327 36 36 ASN N N 117.092 0.300 1 328 36 36 ASN ND2 N 109.382 0.300 1 329 37 37 PHE H H 9.342 0.030 1 330 37 37 PHE HA H 5.814 0.030 1 331 37 37 PHE HB2 H 2.482 0.030 2 332 37 37 PHE HB3 H 3.457 0.030 2 333 37 37 PHE HD1 H 7.096 0.030 1 334 37 37 PHE HD2 H 7.096 0.030 1 335 37 37 PHE HE1 H 7.091 0.030 1 336 37 37 PHE HE2 H 7.091 0.030 1 337 37 37 PHE HZ H 7.674 0.030 1 338 37 37 PHE C C 174.869 0.300 1 339 37 37 PHE CA C 57.298 0.300 1 340 37 37 PHE CB C 45.807 0.300 1 341 37 37 PHE CD1 C 131.528 0.300 1 342 37 37 PHE CD2 C 131.528 0.300 1 343 37 37 PHE CE1 C 131.641 0.300 1 344 37 37 PHE CE2 C 131.641 0.300 1 345 37 37 PHE CZ C 130.174 0.300 1 346 37 37 PHE N N 118.993 0.300 1 347 38 38 CYS H H 9.334 0.030 1 348 38 38 CYS HA H 5.048 0.030 1 349 38 38 CYS HB2 H 3.021 0.030 2 350 38 38 CYS HB3 H 3.440 0.030 2 351 38 38 CYS C C 175.978 0.300 1 352 38 38 CYS CA C 56.727 0.300 1 353 38 38 CYS CB C 31.785 0.300 1 354 38 38 CYS N N 120.326 0.300 1 355 39 39 LYS H H 8.642 0.030 1 356 39 39 LYS HA H 3.923 0.030 1 357 39 39 LYS HB2 H 1.900 0.030 1 358 39 39 LYS HB3 H 1.900 0.030 1 359 39 39 LYS HD2 H 1.720 0.030 1 360 39 39 LYS HD3 H 1.720 0.030 1 361 39 39 LYS HE2 H 3.012 0.030 1 362 39 39 LYS HE3 H 3.012 0.030 1 363 39 39 LYS HG2 H 1.444 0.030 2 364 39 39 LYS HG3 H 1.538 0.030 2 365 39 39 LYS C C 179.280 0.300 1 366 39 39 LYS CA C 59.613 0.300 1 367 39 39 LYS CB C 32.409 0.300 1 368 39 39 LYS CD C 29.203 0.300 1 369 39 39 LYS CE C 42.004 0.300 1 370 39 39 LYS CG C 25.469 0.300 1 371 39 39 LYS N N 120.001 0.300 1 372 40 40 ALA H H 8.471 0.030 1 373 40 40 ALA HA H 4.146 0.030 1 374 40 40 ALA HB H 1.618 0.030 1 375 40 40 ALA C C 180.902 0.300 1 376 40 40 ALA CA C 55.825 0.300 1 377 40 40 ALA CB C 18.697 0.300 1 378 40 40 ALA N N 123.681 0.300 1 379 41 41 CYS H H 9.199 0.030 1 380 41 41 CYS HA H 4.105 0.030 1 381 41 41 CYS HB2 H 3.011 0.030 2 382 41 41 CYS HB3 H 3.232 0.030 2 383 41 41 CYS C C 178.789 0.300 1 384 41 41 CYS CA C 65.728 0.300 1 385 41 41 CYS CB C 29.897 0.300 1 386 41 41 CYS N N 122.333 0.300 1 387 42 42 ILE H H 7.894 0.030 1 388 42 42 ILE HA H 3.841 0.030 1 389 42 42 ILE HB H 1.463 0.030 1 390 42 42 ILE HD1 H -0.081 0.030 1 391 42 42 ILE HG12 H 0.569 0.030 2 392 42 42 ILE HG13 H 0.374 0.030 2 393 42 42 ILE HG2 H 0.752 0.030 1 394 42 42 ILE C C 176.517 0.300 1 395 42 42 ILE CA C 61.457 0.300 1 396 42 42 ILE CB C 37.242 0.300 1 397 42 42 ILE CD1 C 12.305 0.300 1 398 42 42 ILE CG1 C 28.224 0.300 1 399 42 42 ILE CG2 C 18.179 0.300 1 400 42 42 ILE N N 118.624 0.300 1 401 43 43 THR H H 7.839 0.030 1 402 43 43 THR HA H 4.016 0.030 1 403 43 43 THR HB H 4.268 0.030 1 404 43 43 THR HG2 H 1.313 0.030 1 405 43 43 THR C C 176.272 0.300 1 406 43 43 THR CA C 66.579 0.300 1 407 43 43 THR CB C 68.801 0.300 1 408 43 43 THR CG2 C 21.465 0.300 1 409 43 43 THR N N 116.301 0.300 1 410 44 44 ARG H H 7.599 0.030 1 411 44 44 ARG HA H 4.022 0.030 1 412 44 44 ARG HB2 H 1.760 0.030 2 413 44 44 ARG HB3 H 1.868 0.030 2 414 44 44 ARG HD2 H 3.095 0.030 2 415 44 44 ARG HD3 H 3.020 0.030 2 416 44 44 ARG HG2 H 1.444 0.030 2 417 44 44 ARG HG3 H 1.341 0.030 2 418 44 44 ARG C C 178.214 0.300 1 419 44 44 ARG CA C 58.936 0.300 1 420 44 44 ARG CB C 30.106 0.300 1 421 44 44 ARG CD C 43.196 0.300 1 422 44 44 ARG CG C 27.158 0.300 1 423 44 44 ARG N N 119.921 0.300 1 424 45 45 TRP H H 7.592 0.030 1 425 45 45 TRP HA H 4.599 0.030 1 426 45 45 TRP HB2 H 3.077 0.030 2 427 45 45 TRP HB3 H 3.239 0.030 2 428 45 45 TRP HD1 H 7.129 0.030 1 429 45 45 TRP HE1 H 9.786 0.030 1 430 45 45 TRP HE3 H 7.706 0.030 1 431 45 45 TRP HH2 H 7.252 0.030 1 432 45 45 TRP HZ2 H 7.384 0.030 1 433 45 45 TRP HZ3 H 7.185 0.030 1 434 45 45 TRP C C 176.924 0.300 1 435 45 45 TRP CA C 59.379 0.300 1 436 45 45 TRP CB C 29.864 0.300 1 437 45 45 TRP CD1 C 126.744 0.300 1 438 45 45 TRP CE3 C 121.177 0.300 1 439 45 45 TRP CH2 C 124.876 0.300 1 440 45 45 TRP CZ2 C 114.495 0.300 1 441 45 45 TRP CZ3 C 122.459 0.300 1 442 45 45 TRP N N 118.010 0.300 1 443 45 45 TRP NE1 N 127.705 0.300 1 444 46 46 TRP H H 8.327 0.030 1 445 46 46 TRP HA H 4.753 0.030 1 446 46 46 TRP HB2 H 3.378 0.030 2 447 46 46 TRP HB3 H 3.304 0.030 2 448 46 46 TRP HD1 H 7.023 0.030 1 449 46 46 TRP HE1 H 10.277 0.030 1 450 46 46 TRP HE3 H 7.474 0.030 1 451 46 46 TRP HH2 H 7.189 0.030 1 452 46 46 TRP HZ2 H 7.490 0.030 1 453 46 46 TRP HZ3 H 7.030 0.030 1 454 46 46 TRP C C 176.587 0.300 1 455 46 46 TRP CA C 56.679 0.300 1 456 46 46 TRP CB C 28.898 0.300 1 457 46 46 TRP CD1 C 123.787 0.300 1 458 46 46 TRP CE3 C 121.062 0.300 1 459 46 46 TRP CH2 C 124.764 0.300 1 460 46 46 TRP CZ2 C 114.868 0.300 1 461 46 46 TRP CZ3 C 121.578 0.300 1 462 46 46 TRP N N 120.477 0.300 1 463 46 46 TRP NE1 N 128.243 0.300 1 464 47 47 GLU H H 7.933 0.030 1 465 47 47 GLU HA H 4.171 0.030 1 466 47 47 GLU HB2 H 2.084 0.030 1 467 47 47 GLU HB3 H 2.084 0.030 1 468 47 47 GLU HG2 H 2.270 0.030 2 469 47 47 GLU HG3 H 2.451 0.030 2 470 47 47 GLU CA C 58.172 0.300 1 471 47 47 GLU CB C 30.475 0.300 1 472 47 47 GLU CG C 36.745 0.300 1 473 47 47 GLU N N 120.505 0.300 1 474 48 48 ASP H H 7.972 0.030 1 475 48 48 ASP HA H 4.695 0.030 1 476 48 48 ASP HB2 H 2.596 0.030 2 477 48 48 ASP HB3 H 2.838 0.030 2 478 48 48 ASP C C 176.785 0.300 1 479 48 48 ASP CA C 53.541 0.300 1 480 48 48 ASP CB C 40.771 0.300 1 481 48 48 ASP N N 118.533 0.300 1 482 49 49 LEU H H 8.242 0.030 1 483 49 49 LEU HA H 3.993 0.030 1 484 49 49 LEU HB2 H 1.441 0.030 2 485 49 49 LEU HB3 H 1.627 0.030 2 486 49 49 LEU HD1 H 0.792 0.030 1 487 49 49 LEU HD2 H 0.513 0.030 1 488 49 49 LEU HG H 1.537 0.030 1 489 49 49 LEU C C 177.888 0.300 1 490 49 49 LEU CA C 56.023 0.300 1 491 49 49 LEU CB C 41.716 0.300 1 492 49 49 LEU CD1 C 25.202 0.300 2 493 49 49 LEU CD2 C 22.535 0.300 2 494 49 49 LEU CG C 26.980 0.300 1 495 49 49 LEU N N 123.750 0.300 1 496 50 50 GLU H H 8.320 0.030 1 497 50 50 GLU HA H 4.243 0.030 1 498 50 50 GLU HB2 H 1.971 0.030 2 499 50 50 GLU HB3 H 2.150 0.030 2 500 50 50 GLU HG2 H 2.262 0.030 2 501 50 50 GLU HG3 H 2.170 0.030 2 502 50 50 GLU C C 176.157 0.300 1 503 50 50 GLU CA C 56.598 0.300 1 504 50 50 GLU CB C 29.713 0.300 1 505 50 50 GLU CG C 36.581 0.300 1 506 50 50 GLU N N 117.962 0.300 1 507 51 51 ARG H H 7.538 0.030 1 508 51 51 ARG HA H 4.332 0.030 1 509 51 51 ARG HB2 H 1.725 0.030 2 510 51 51 ARG HB3 H 1.597 0.030 2 511 51 51 ARG HD2 H 2.898 0.030 1 512 51 51 ARG HD3 H 2.898 0.030 1 513 51 51 ARG HG2 H 1.444 0.030 2 514 51 51 ARG HG3 H 1.332 0.030 2 515 51 51 ARG C C 175.484 0.300 1 516 51 51 ARG CA C 55.087 0.300 1 517 51 51 ARG CB C 31.925 0.300 1 518 51 51 ARG CD C 43.160 0.300 1 519 51 51 ARG CG C 26.627 0.300 1 520 51 51 ARG N N 119.062 0.300 1 521 52 52 ASP H H 8.304 0.030 1 522 52 52 ASP HA H 4.542 0.030 1 523 52 52 ASP HB2 H 2.574 0.030 2 524 52 52 ASP HB3 H 2.494 0.030 2 525 52 52 ASP C C 175.593 0.300 1 526 52 52 ASP CA C 54.560 0.300 1 527 52 52 ASP CB C 41.129 0.300 1 528 52 52 ASP N N 119.576 0.300 1 529 53 53 PHE H H 7.781 0.030 1 530 53 53 PHE HA H 4.293 0.030 1 531 53 53 PHE HB2 H 2.708 0.030 2 532 53 53 PHE HB3 H 2.236 0.030 2 533 53 53 PHE HD1 H 7.021 0.030 1 534 53 53 PHE HD2 H 7.021 0.030 1 535 53 53 PHE HE1 H 7.139 0.030 1 536 53 53 PHE HE2 H 7.139 0.030 1 537 53 53 PHE HZ H 6.902 0.030 1 538 53 53 PHE C C 174.136 0.300 1 539 53 53 PHE CA C 55.151 0.300 1 540 53 53 PHE CB C 39.640 0.300 1 541 53 53 PHE CD1 C 131.906 0.300 1 542 53 53 PHE CD2 C 131.906 0.300 1 543 53 53 PHE CE1 C 131.581 0.300 1 544 53 53 PHE CE2 C 131.581 0.300 1 545 53 53 PHE CZ C 129.275 0.300 1 546 53 53 PHE N N 121.448 0.300 1 547 54 54 PRO HA H 4.537 0.030 1 548 54 54 PRO HB2 H 2.161 0.030 2 549 54 54 PRO HB3 H 2.004 0.030 2 550 54 54 PRO HD2 H 3.170 0.030 2 551 54 54 PRO HD3 H 3.735 0.030 2 552 54 54 PRO HG2 H 2.023 0.030 1 553 54 54 PRO HG3 H 2.023 0.030 1 554 54 54 PRO C C 176.184 0.300 1 555 54 54 PRO CA C 62.644 0.300 1 556 54 54 PRO CB C 31.154 0.300 1 557 54 54 PRO CD C 50.722 0.300 1 558 54 54 PRO CG C 27.220 0.300 1 559 55 55 CYS H H 7.871 0.030 1 560 55 55 CYS HA H 4.355 0.030 1 561 55 55 CYS HB2 H 3.105 0.030 2 562 55 55 CYS HB3 H 2.921 0.030 2 563 55 55 CYS C C 175.718 0.300 1 564 55 55 CYS CA C 56.249 0.300 1 565 55 55 CYS CB C 31.880 0.300 1 566 55 55 CYS N N 123.330 0.300 1 567 56 56 PRO HA H 3.973 0.030 1 568 56 56 PRO HB2 H 1.346 0.030 2 569 56 56 PRO HB3 H 0.959 0.030 2 570 56 56 PRO HD2 H 3.731 0.030 2 571 56 56 PRO HD3 H 2.723 0.030 2 572 56 56 PRO HG2 H 1.253 0.030 2 573 56 56 PRO HG3 H 0.912 0.030 2 574 56 56 PRO CA C 63.340 0.300 1 575 56 56 PRO CB C 31.443 0.300 1 576 56 56 PRO CD C 50.467 0.300 1 577 56 56 PRO CG C 26.091 0.300 1 578 57 57 VAL H H 8.927 0.030 1 579 57 57 VAL HA H 4.076 0.030 1 580 57 57 VAL HB H 1.375 0.030 1 581 57 57 VAL HG1 H 0.509 0.030 1 582 57 57 VAL HG2 H 0.313 0.030 1 583 57 57 VAL C C 176.542 0.300 1 584 57 57 VAL CA C 62.726 0.300 1 585 57 57 VAL CB C 33.209 0.300 1 586 57 57 VAL CG1 C 21.503 0.300 2 587 57 57 VAL CG2 C 20.540 0.300 2 588 57 57 VAL N N 121.428 0.300 1 589 58 58 CYS H H 8.014 0.030 1 590 58 58 CYS HA H 3.983 0.030 1 591 58 58 CYS HB2 H 2.696 0.030 2 592 58 58 CYS HB3 H 3.091 0.030 2 593 58 58 CYS C C 180.297 0.300 1 594 58 58 CYS CA C 66.807 0.300 1 595 58 58 CYS CB C 31.059 0.300 1 596 58 58 CYS N N 131.281 0.300 1 stop_ save_