data_11529 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Solution structure of a regulatory domain of meiosis inhibitor ; _BMRB_accession_number 11529 _BMRB_flat_file_name bmr11529.str _Entry_type original _Submission_date 2013-07-04 _Accession_date 2013-07-15 _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 Shoji S . . 2 Muto Y . . 3 Ikeda M . . 4 He F . . 5 Tsuda K . . 6 Ohsawa N . . 7 Akasaka R . . 8 Terada T . . 9 Wakiyama M . . 10 Shirouzu M . . 11 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" 307 "13C chemical shifts" 225 "15N chemical shifts" 50 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2015-01-08 update BMRB 'update entry citation' 2014-07-14 original author 'original release' stop_ save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title 'The zinc-binding region (ZBR) fragment of Emi2 can inhibit APC/C by targeting its association with the coactivator Cdc20 and UBE2C-mediated ubiquitylation' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 25161877 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Shoji S. . . 2 Muto Y. . . 3 Ikeda M. . . 4 He F. . . 5 Tsuda K. . . 6 Ohsawa N. . . 7 Akasaka R. . . 8 Terada T. . . 9 Wakiyama M. . . 10 Shirouzu M. . . 11 Yokoyama S. . . stop_ _Journal_abbreviation 'FEBS OPEN BIO.' _Journal_volume 4 _Journal_issue . _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 689 _Page_last 703 _Year 2014 _Details . save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name 'a regulatory domain of meiosis inhibitor' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label entity_1 $entity_1 'ZINC ION_1' $entity_ZN 'ZINC ION_2' $entity_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 entity_1 _Molecular_mass 5830.834 _Mol_thiol_state . _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 59 _Mol_residue_sequence ; GSSGSSGTDEALKPCPRCQS PAKYQPHKKRGLCSRLACGF DFCVLCLCAYHGSEDCRRG ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 559 GLY 2 560 SER 3 561 SER 4 562 GLY 5 563 SER 6 564 SER 7 565 GLY 8 566 THR 9 567 ASP 10 568 GLU 11 569 ALA 12 570 LEU 13 571 LYS 14 572 PRO 15 573 CYS 16 574 PRO 17 575 ARG 18 576 CYS 19 577 GLN 20 578 SER 21 579 PRO 22 580 ALA 23 581 LYS 24 582 TYR 25 583 GLN 26 584 PRO 27 585 HIS 28 586 LYS 29 587 LYS 30 588 ARG 31 589 GLY 32 590 LEU 33 591 CYS 34 592 SER 35 593 ARG 36 594 LEU 37 595 ALA 38 596 CYS 39 597 GLY 40 598 PHE 41 599 ASP 42 600 PHE 43 601 CYS 44 602 VAL 45 603 LEU 46 604 CYS 47 605 LEU 48 606 CYS 49 607 ALA 50 608 TYR 51 609 HIS 52 610 GLY 53 611 SER 54 612 GLU 55 613 ASP 56 614 CYS 57 615 ARG 58 616 ARG 59 617 GLY stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-07-15 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 2RT9 "Solution Structure Of A Regulatory Domain Of Meiosis Inhibitor" 100.00 59 100.00 100.00 3.61e-33 DBJ BAC26733 "unnamed protein product [Mus musculus]" 88.14 640 100.00 100.00 1.02e-28 GB AAH26503 "Fbxo43 protein, partial [Mus musculus]" 88.14 247 100.00 100.00 5.08e-30 GB AAH82107 "Fbxo43 protein [Rattus norvegicus]" 88.14 664 100.00 100.00 1.67e-28 GB AAH98484 "F-box protein 43 [Mus musculus]" 88.14 641 100.00 100.00 9.78e-29 GB EDL08829 "mCG6563 [Mus musculus]" 88.14 641 100.00 100.00 9.49e-29 GB EDM16401 "F-box protein 43 [Rattus norvegicus]" 88.14 664 100.00 100.00 1.67e-28 REF NP_001012117 "F-box only protein 43 [Rattus norvegicus]" 88.14 664 100.00 100.00 1.67e-28 REF NP_001074722 "F-box only protein 43 [Mus musculus]" 88.14 641 100.00 100.00 9.49e-29 REF XP_006241597 "PREDICTED: F-box only protein 43 isoform X1 [Rattus norvegicus]" 88.14 664 100.00 100.00 1.67e-28 REF XP_006520259 "PREDICTED: F-box only protein 43 isoform X2 [Mus musculus]" 88.14 688 100.00 100.00 1.32e-28 REF XP_006520260 "PREDICTED: F-box only protein 43 isoform X1 [Mus musculus]" 88.14 641 100.00 100.00 9.49e-29 SP Q66H04 "RecName: Full=F-box only protein 43; AltName: Full=Endogenous meiotic inhibitor 2" 88.14 664 100.00 100.00 1.67e-28 SP Q8CDI2 "RecName: Full=F-box only protein 43; AltName: Full=Endogenous meiotic inhibitor 2" 88.14 640 100.00 100.00 9.35e-29 stop_ save_ ############# # Ligands # ############# save_ZN _Saveframe_category ligand _Mol_type "non-polymer (NON-POLYMER)" _Name_common 'ZINC ION' _BMRB_code ZN _PDB_code ZN _Molecular_mass 65.409 _Mol_charge 2 _Mol_paramagnetic . _Mol_aromatic no _Details . loop_ _Atom_name _PDB_atom_name _Atom_type _Atom_chirality _Atom_charge _Atom_oxidation_number _Atom_unpaired_electrons 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 _Gene_mnemonic $entity_1 Mouse 10090 Eukaryota Metazoa Mus musculus Fbxo43 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 $entity_1 'cell free synthesis' 'E. coli' Escherichia coli . PCR2.1 stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Saveframe_category sample _Sample_type solution _Details '20mM dTris-HCl(pH 6.5), 100mM NaCl, 1mM d-DTT, 50uM ZnCl2, 0.02% NaN3' loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $entity_1 0.47 mM '[U-100% 13C; U-100% 15N]' H2O 90 % . D2O 10 % . dTris-HCl 20 mM [U-2H] NaCl 100 mM 'natural abundance' d-DTT 1 mM [U-2H] ZnCl2 50 uM 'natural abundance' NaN3 0.02 % 'natural abundance' stop_ save_ ############################ # Computer software used # ############################ save_TOPSPIN _Saveframe_category software _Name TOPSPIN _Version . loop_ _Vendor _Address _Electronic_address 'Bruker Biospin' . . stop_ loop_ _Task collection stop_ _Details . save_ save_NMRPipe _Saveframe_category software _Name NMRPipe _Version . loop_ _Vendor _Address _Electronic_address 'Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax' . . stop_ loop_ _Task processing stop_ _Details . save_ save_NMRView _Saveframe_category software _Name NMRView _Version . loop_ _Vendor _Address _Electronic_address 'Johnson, One Moon Scientific' . . stop_ loop_ _Task 'data analysis' stop_ _Details . save_ save_Kujira _Saveframe_category software _Name Kujira _Version . loop_ _Vendor _Address _Electronic_address 'Kobayashi, N' . . stop_ loop_ _Task 'data analysis' stop_ _Details . save_ save_CYANA _Saveframe_category software _Name CYANA _Version . loop_ _Vendor _Address _Electronic_address 'Guntert, Mumenthaler and Wuthrich' . . stop_ loop_ _Task 'structure solution' stop_ _Details . save_ save_AMBER _Saveframe_category software _Name AMBER _Version . loop_ _Vendor _Address _Electronic_address 'Case, Darden, Cheatham, III, Simmerling, Wang, Duke, Luo, ... and Kollman' . . stop_ loop_ _Task refinement 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_1H-15N_NOESY_1 _Saveframe_category NMR_applied_experiment _Experiment_name '3D 1H-15N NOESY' _Sample_label $sample_1 save_ save_3D_1H-13C_NOESY_2 _Saveframe_category NMR_applied_experiment _Experiment_name '3D 1H-13C NOESY' _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' 120 . mM pH 6.5 . 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 'Chemical shift correction using NMRPipe Bruker program' loop_ _Mol_common_name _Atom_type _Atom_isotope_number _Atom_group _Chem_shift_units _Chem_shift_value _Reference_method _Reference_type _External_reference_sample_geometry _External_reference_location _External_reference_axis _Indirect_shift_ratio DSS C 13 'methyl protons' ppm 0.00 external indirect . . . 0.251449530 DSS H 1 'methyl protons' ppm 0.00 external direct . . . 1.000000000 DSS N 15 'methyl protons' ppm 0.00 external indirect . . . 0.101329118 stop_ save_ ################################### # Assigned chemical shift lists # ################################### ################################################################### # Chemical Shift Ambiguity Index Value Definitions # # # # The values other than 1 are used for those atoms with different # # chemical shifts that cannot be assigned to stereospecific atoms # # or to specific residues or chains. # # # # Index Value Definition # # # # 1 Unique (including isolated methyl protons, # # geminal atoms, and geminal methyl # # groups with identical chemical shifts) # # (e.g. ILE HD11, HD12, HD13 protons) # # 2 Ambiguity of geminal atoms or geminal methyl # # proton groups (e.g. ASP HB2 and HB3 # # protons, LEU CD1 and CD2 carbons, or # # LEU HD11, HD12, HD13 and HD21, HD22, # # HD23 methyl protons) # # 3 Aromatic atoms on opposite sides of # # symmetrical rings (e.g. TYR HE1 and HE2 # # protons) # # 4 Intraresidue ambiguities (e.g. LYS HG and # # HD protons or TRP HZ2 and HZ3 protons) # # 5 Interresidue ambiguities (LYS 12 vs. LYS 27) # # 6 Intermolecular ambiguities (e.g. ASP 31 CA # # in monomer 1 and ASP 31 CA in monomer 2 # # of an asymmetrical homodimer, duplex # # DNA assignments, or other assignments # # that may apply to atoms in one or more # # molecule in the molecular assembly) # # 9 Ambiguous, specific ambiguity not defined # # # ################################################################### save_assigned_chem_shift_list_1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Experiment_label '3D 1H-15N NOESY' '3D 1H-13C NOESY' 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 entity_1 _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 1 566 8 THR H H 8.010 . . 2 566 8 THR HA H 4.315 . . 3 566 8 THR HB H 4.192 . . 4 566 8 THR HG2 H 1.110 . . 5 566 8 THR C C 171.793 . . 6 566 8 THR CA C 61.775 . . 7 566 8 THR CB C 69.838 . . 8 566 8 THR CG2 C 21.544 . . 9 566 8 THR N N 113.136 . . 10 567 9 ASP H H 8.330 . . 11 567 9 ASP HA H 4.540 . . 12 567 9 ASP HB2 H 2.646 . . 13 567 9 ASP HB3 H 2.558 . . 14 567 9 ASP C C 173.619 . . 15 567 9 ASP CA C 54.576 . . 16 567 9 ASP CB C 41.152 . . 17 567 9 ASP N N 122.658 . . 18 568 10 GLU H H 8.239 . . 19 568 10 GLU HA H 4.194 . . 20 568 10 GLU HB2 H 1.976 . . 21 568 10 GLU HB3 H 1.843 . . 22 568 10 GLU HG2 H 2.201 . . 23 568 10 GLU HG3 H 2.159 . . 24 568 10 GLU C C 173.279 . . 25 568 10 GLU CA C 56.750 . . 26 568 10 GLU CB C 30.442 . . 27 568 10 GLU CG C 36.397 . . 28 568 10 GLU N N 121.414 . . 29 569 11 ALA H H 8.209 . . 30 569 11 ALA HA H 4.244 . . 31 569 11 ALA HB H 1.303 . . 32 569 11 ALA C C 174.599 . . 33 569 11 ALA CA C 52.332 . . 34 569 11 ALA CB C 19.434 . . 35 569 11 ALA N N 124.359 . . 36 570 12 LEU H H 7.915 . . 37 570 12 LEU HA H 4.538 . . 38 570 12 LEU HB2 H 1.544 . . 39 570 12 LEU HB3 H 1.351 . . 40 570 12 LEU HG H 1.505 . . 41 570 12 LEU HD1 H 0.809 . . 42 570 12 LEU HD2 H 0.703 . . 43 570 12 LEU C C 174.336 . . 44 570 12 LEU CA C 54.567 . . 45 570 12 LEU CB C 43.050 . . 46 570 12 LEU CG C 27.263 . . 47 570 12 LEU CD1 C 25.250 . . 48 570 12 LEU CD2 C 23.472 . . 49 570 12 LEU N N 120.973 . . 50 571 13 LYS H H 8.428 . . 51 571 13 LYS HA H 4.606 . . 52 571 13 LYS HB2 H 1.721 . . 53 571 13 LYS HB3 H 1.535 . . 54 571 13 LYS HG2 H 1.219 . . 55 571 13 LYS HG3 H 1.174 . . 56 571 13 LYS HD2 H 1.349 . . 57 571 13 LYS HD3 H 1.522 . . 58 571 13 LYS HE2 H 2.610 . . 59 571 13 LYS HE3 H 2.551 . . 60 571 13 LYS C C 171.375 . . 61 571 13 LYS CA C 53.398 . . 62 571 13 LYS CB C 33.608 . . 63 571 13 LYS CG C 24.803 . . 64 571 13 LYS CD C 28.914 . . 65 571 13 LYS CE C 41.998 . . 66 571 13 LYS N N 123.121 . . 67 572 14 PRO HA H 4.427 . . 68 572 14 PRO HB2 H 1.520 . . 69 572 14 PRO HB3 H 1.918 . . 70 572 14 PRO HG2 H 1.850 . . 71 572 14 PRO HG3 H 1.850 . . 72 572 14 PRO HD2 H 3.699 . . 73 572 14 PRO HD3 H 3.505 . . 74 572 14 PRO C C 172.879 . . 75 572 14 PRO CA C 62.060 . . 76 572 14 PRO CB C 32.078 . . 77 572 14 PRO CG C 27.035 . . 78 572 14 PRO CD C 50.224 . . 79 573 15 CYS H H 9.023 . . 80 573 15 CYS HA H 4.093 . . 81 573 15 CYS HB2 H 2.907 . . 82 573 15 CYS HB3 H 3.093 . . 83 573 15 CYS C C 174.116 . . 84 573 15 CYS CA C 56.920 . . 85 573 15 CYS CB C 32.104 . . 86 573 15 CYS N N 123.492 . . 87 574 16 PRO HA H 4.266 . . 88 574 16 PRO HB2 H 1.857 . . 89 574 16 PRO HB3 H 2.209 . . 90 574 16 PRO HG2 H 1.598 . . 91 574 16 PRO HG3 H 1.544 . . 92 574 16 PRO HD2 H 2.854 . . 93 574 16 PRO HD3 H 2.631 . . 94 574 16 PRO C C 175.089 . . 95 574 16 PRO CA C 63.862 . . 96 574 16 PRO CB C 32.476 . . 97 574 16 PRO CG C 27.910 . . 98 574 16 PRO CD C 49.593 . . 99 575 17 ARG H H 9.123 . . 100 575 17 ARG HA H 4.130 . . 101 575 17 ARG HB2 H 1.477 . . 102 575 17 ARG HB3 H 1.250 . . 103 575 17 ARG HG2 H 1.047 . . 104 575 17 ARG HG3 H 0.926 . . 105 575 17 ARG HD2 H 2.569 . . 106 575 17 ARG HD3 H 2.275 . . 107 575 17 ARG HE H 6.437 . . 108 575 17 ARG C C 174.817 . . 109 575 17 ARG CA C 58.165 . . 110 575 17 ARG CB C 31.575 . . 111 575 17 ARG CG C 27.024 . . 112 575 17 ARG CD C 43.267 . . 113 575 17 ARG N N 121.041 . . 114 575 17 ARG NE N 84.734 . . 115 576 18 CYS H H 8.408 . . 116 576 18 CYS HA H 4.942 . . 117 576 18 CYS HB2 H 2.512 . . 118 576 18 CYS HB3 H 3.097 . . 119 576 18 CYS C C 173.546 . . 120 576 18 CYS CA C 58.811 . . 121 576 18 CYS CB C 32.325 . . 122 576 18 CYS N N 118.974 . . 123 577 19 GLN H H 8.159 . . 124 577 19 GLN HA H 3.999 . . 125 577 19 GLN HB2 H 2.371 . . 126 577 19 GLN HB3 H 2.284 . . 127 577 19 GLN HG2 H 2.171 . . 128 577 19 GLN HG3 H 2.171 . . 129 577 19 GLN HE21 H 6.360 . . 130 577 19 GLN HE22 H 7.139 . . 131 577 19 GLN C C 172.358 . . 132 577 19 GLN CA C 58.648 . . 133 577 19 GLN CB C 25.775 . . 134 577 19 GLN CG C 34.375 . . 135 577 19 GLN N N 117.134 . . 136 577 19 GLN NE2 N 112.357 . . 137 578 20 SER H H 8.702 . . 138 578 20 SER HA H 4.642 . . 139 578 20 SER HB2 H 3.815 . . 140 578 20 SER HB3 H 4.026 . . 141 578 20 SER C C 167.908 . . 142 578 20 SER CA C 59.259 . . 143 578 20 SER CB C 61.399 . . 144 578 20 SER N N 120.402 . . 145 579 21 PRO HA H 4.300 . . 146 579 21 PRO HB2 H 1.758 . . 147 579 21 PRO HB3 H 2.252 . . 148 579 21 PRO HG2 H 2.061 . . 149 579 21 PRO HG3 H 1.950 . . 150 579 21 PRO HD2 H 3.873 . . 151 579 21 PRO HD3 H 3.487 . . 152 579 21 PRO C C 173.065 . . 153 579 21 PRO CA C 64.121 . . 154 579 21 PRO CB C 32.062 . . 155 579 21 PRO CG C 28.160 . . 156 579 21 PRO CD C 50.395 . . 157 580 22 ALA H H 9.012 . . 158 580 22 ALA HA H 4.991 . . 159 580 22 ALA HB H 1.302 . . 160 580 22 ALA C C 173.424 . . 161 580 22 ALA CA C 50.320 . . 162 580 22 ALA CB C 21.562 . . 163 580 22 ALA N N 127.768 . . 164 581 23 LYS H H 8.183 . . 165 581 23 LYS HA H 4.408 . . 166 581 23 LYS HB2 H 1.715 . . 167 581 23 LYS HB3 H 1.670 . . 168 581 23 LYS HG2 H 1.286 . . 169 581 23 LYS HG3 H 1.371 . . 170 581 23 LYS HD2 H 1.604 . . 171 581 23 LYS HD3 H 1.604 . . 172 581 23 LYS HE2 H 2.870 . . 173 581 23 LYS HE3 H 2.870 . . 174 581 23 LYS C C 173.216 . . 175 581 23 LYS CA C 55.586 . . 176 581 23 LYS CB C 33.530 . . 177 581 23 LYS CG C 24.992 . . 178 581 23 LYS CD C 29.013 . . 179 581 23 LYS CE C 42.072 . . 180 581 23 LYS N N 120.942 . . 181 582 24 TYR H H 8.712 . . 182 582 24 TYR HA H 5.105 . . 183 582 24 TYR HB2 H 2.792 . . 184 582 24 TYR HB3 H 2.742 . . 185 582 24 TYR HD1 H 6.917 . . 186 582 24 TYR HD2 H 6.917 . . 187 582 24 TYR HE1 H 6.621 . . 188 582 24 TYR HE2 H 6.621 . . 189 582 24 TYR C C 172.585 . . 190 582 24 TYR CA C 55.866 . . 191 582 24 TYR CB C 40.830 . . 192 582 24 TYR CD1 C 132.795 . . 193 582 24 TYR CD2 C 132.795 . . 194 582 24 TYR CE1 C 118.112 . . 195 582 24 TYR CE2 C 118.112 . . 196 582 24 TYR N N 124.407 . . 197 583 25 GLN H H 8.658 . . 198 583 25 GLN HA H 4.732 . . 199 583 25 GLN HB2 H 1.714 . . 200 583 25 GLN HB3 H 1.714 . . 201 583 25 GLN HG2 H 2.009 . . 202 583 25 GLN HG3 H 2.148 . . 203 583 25 GLN HE21 H 7.265 . . 204 583 25 GLN HE22 H 6.562 . . 205 583 25 GLN C C 172.099 . . 206 583 25 GLN CA C 52.257 . . 207 583 25 GLN CB C 29.424 . . 208 583 25 GLN CG C 33.066 . . 209 583 25 GLN N N 124.563 . . 210 583 25 GLN NE2 N 110.481 . . 211 584 26 PRO HA H 3.867 . . 212 584 26 PRO HB2 H 1.784 . . 213 584 26 PRO HB3 H 2.144 . . 214 584 26 PRO HG2 H 1.764 . . 215 584 26 PRO HG3 H 1.891 . . 216 584 26 PRO HD2 H 3.767 . . 217 584 26 PRO HD3 H 3.324 . . 218 584 26 PRO CA C 65.064 . . 219 584 26 PRO CB C 31.832 . . 220 584 26 PRO CG C 27.198 . . 221 584 26 PRO CD C 51.082 . . 222 585 27 HIS HA H 4.415 . . 223 585 27 HIS HB2 H 3.062 . . 224 585 27 HIS HB3 H 3.132 . . 225 585 27 HIS HD2 H 6.971 . . 226 585 27 HIS HE1 H 7.763 . . 227 585 27 HIS C C 173.514 . . 228 585 27 HIS CA C 58.237 . . 229 585 27 HIS CB C 29.264 . . 230 585 27 HIS CD2 C 119.015 . . 231 585 27 HIS CE1 C 138.707 . . 232 586 28 LYS H H 6.983 . . 233 586 28 LYS HA H 4.376 . . 234 586 28 LYS HB2 H 1.881 . . 235 586 28 LYS HB3 H 1.250 . . 236 586 28 LYS HG2 H 1.040 . . 237 586 28 LYS HG3 H 0.986 . . 238 586 28 LYS HD2 H 1.472 . . 239 586 28 LYS HD3 H 1.436 . . 240 586 28 LYS HE2 H 2.809 . . 241 586 28 LYS HE3 H 2.847 . . 242 586 28 LYS C C 172.393 . . 243 586 28 LYS CA C 54.781 . . 244 586 28 LYS CB C 33.878 . . 245 586 28 LYS CG C 24.775 . . 246 586 28 LYS CD C 28.597 . . 247 586 28 LYS CE C 42.149 . . 248 586 28 LYS N N 116.897 . . 249 587 29 LYS H H 7.846 . . 250 587 29 LYS HA H 3.751 . . 251 587 29 LYS HB2 H 2.157 . . 252 587 29 LYS HB3 H 1.896 . . 253 587 29 LYS HG2 H 1.375 . . 254 587 29 LYS HG3 H 1.375 . . 255 587 29 LYS HD2 H 1.536 . . 256 587 29 LYS HD3 H 1.715 . . 257 587 29 LYS HE2 H 2.960 . . 258 587 29 LYS HE3 H 2.960 . . 259 587 29 LYS C C 172.307 . . 260 587 29 LYS CA C 57.210 . . 261 587 29 LYS CB C 29.879 . . 262 587 29 LYS CG C 25.205 . . 263 587 29 LYS CD C 29.476 . . 264 587 29 LYS CE C 42.464 . . 265 587 29 LYS N N 116.833 . . 266 588 30 ARG H H 6.996 . . 267 588 30 ARG HA H 4.962 . . 268 588 30 ARG HB2 H 1.114 . . 269 588 30 ARG HB3 H 1.018 . . 270 588 30 ARG HG2 H 0.705 . . 271 588 30 ARG HG3 H 0.775 . . 272 588 30 ARG HD2 H 2.315 . . 273 588 30 ARG HD3 H 1.328 . . 274 588 30 ARG HE H 6.009 . . 275 588 30 ARG C C 170.887 . . 276 588 30 ARG CA C 54.741 . . 277 588 30 ARG CB C 36.486 . . 278 588 30 ARG CG C 25.821 . . 279 588 30 ARG CD C 43.714 . . 280 588 30 ARG N N 120.783 . . 281 589 31 GLY H H 8.696 . . 282 589 31 GLY HA2 H 4.455 . . 283 589 31 GLY HA3 H 1.685 . . 284 589 31 GLY C C 167.619 . . 285 589 31 GLY CA C 42.865 . . 286 589 31 GLY N N 115.268 . . 287 590 32 LEU H H 8.069 . . 288 590 32 LEU HA H 4.989 . . 289 590 32 LEU HB2 H 1.362 . . 290 590 32 LEU HB3 H 1.199 . . 291 590 32 LEU HG H 1.197 . . 292 590 32 LEU HD1 H 0.574 . . 293 590 32 LEU HD2 H 0.594 . . 294 590 32 LEU C C 173.671 . . 295 590 32 LEU CA C 53.063 . . 296 590 32 LEU CB C 44.414 . . 297 590 32 LEU CG C 26.903 . . 298 590 32 LEU CD1 C 24.446 . . 299 590 32 LEU CD2 C 25.089 . . 300 590 32 LEU N N 120.787 . . 301 591 33 CYS H H 9.042 . . 302 591 33 CYS HA H 3.923 . . 303 591 33 CYS HB2 H 3.041 . . 304 591 33 CYS HB3 H 3.473 . . 305 591 33 CYS C C 173.300 . . 306 591 33 CYS CA C 62.844 . . 307 591 33 CYS CB C 31.937 . . 308 591 33 CYS N N 130.534 . . 309 592 34 SER H H 8.248 . . 310 592 34 SER HA H 4.324 . . 311 592 34 SER HB2 H 3.985 . . 312 592 34 SER HB3 H 3.809 . . 313 592 34 SER C C 171.530 . . 314 592 34 SER CA C 59.705 . . 315 592 34 SER CB C 64.793 . . 316 592 34 SER N N 121.815 . . 317 593 35 ARG H H 9.425 . . 318 593 35 ARG HA H 4.374 . . 319 593 35 ARG HB2 H 2.211 . . 320 593 35 ARG HB3 H 1.791 . . 321 593 35 ARG HG2 H 1.308 . . 322 593 35 ARG HG3 H 1.729 . . 323 593 35 ARG HD2 H 3.334 . . 324 593 35 ARG HD3 H 3.193 . . 325 593 35 ARG C C 174.919 . . 326 593 35 ARG CA C 56.141 . . 327 593 35 ARG CB C 30.854 . . 328 593 35 ARG CG C 27.996 . . 329 593 35 ARG CD C 43.522 . . 330 593 35 ARG N N 130.025 . . 331 594 36 LEU H H 8.697 . . 332 594 36 LEU HA H 3.909 . . 333 594 36 LEU HB2 H 1.645 . . 334 594 36 LEU HB3 H 1.507 . . 335 594 36 LEU HG H 1.643 . . 336 594 36 LEU HD1 H 0.885 . . 337 594 36 LEU HD2 H 0.833 . . 338 594 36 LEU C C 176.016 . . 339 594 36 LEU CA C 58.498 . . 340 594 36 LEU CB C 41.441 . . 341 594 36 LEU CG C 27.142 . . 342 594 36 LEU CD1 C 24.486 . . 343 594 36 LEU CD2 C 23.820 . . 344 594 36 LEU N N 132.398 . . 345 595 37 ALA H H 8.118 . . 346 595 37 ALA HA H 4.069 . . 347 595 37 ALA HB H 1.273 . . 348 595 37 ALA C C 173.745 . . 349 595 37 ALA CA C 53.266 . . 350 595 37 ALA CB C 18.792 . . 351 595 37 ALA N N 116.744 . . 352 596 38 CYS H H 7.702 . . 353 596 38 CYS HA H 4.411 . . 354 596 38 CYS HB2 H 3.241 . . 355 596 38 CYS HB3 H 2.608 . . 356 596 38 CYS C C 173.195 . . 357 596 38 CYS CA C 59.927 . . 358 596 38 CYS CB C 31.917 . . 359 596 38 CYS N N 120.451 . . 360 597 39 GLY H H 8.175 . . 361 597 39 GLY HA2 H 3.919 . . 362 597 39 GLY HA3 H 3.814 . . 363 597 39 GLY C C 171.494 . . 364 597 39 GLY CA C 46.662 . . 365 597 39 GLY N N 106.187 . . 366 598 40 PHE H H 8.199 . . 367 598 40 PHE HA H 4.580 . . 368 598 40 PHE HB2 H 3.452 . . 369 598 40 PHE HB3 H 3.211 . . 370 598 40 PHE HD1 H 7.251 . . 371 598 40 PHE HD2 H 7.251 . . 372 598 40 PHE HE1 H 7.097 . . 373 598 40 PHE HE2 H 7.097 . . 374 598 40 PHE HZ H 7.176 . . 375 598 40 PHE C C 170.036 . . 376 598 40 PHE CA C 58.811 . . 377 598 40 PHE CB C 39.727 . . 378 598 40 PHE CD1 C 130.994 . . 379 598 40 PHE CD2 C 130.994 . . 380 598 40 PHE CE1 C 131.398 . . 381 598 40 PHE CE2 C 131.398 . . 382 598 40 PHE CZ C 129.363 . . 383 598 40 PHE N N 123.710 . . 384 599 41 ASP H H 7.245 . . 385 599 41 ASP HA H 5.233 . . 386 599 41 ASP HB2 H 2.829 . . 387 599 41 ASP HB3 H 2.335 . . 388 599 41 ASP C C 174.091 . . 389 599 41 ASP CA C 52.271 . . 390 599 41 ASP CB C 41.853 . . 391 599 41 ASP N N 128.918 . . 392 600 42 PHE H H 9.131 . . 393 600 42 PHE HA H 5.065 . . 394 600 42 PHE HB2 H 2.344 . . 395 600 42 PHE HB3 H 1.618 . . 396 600 42 PHE HD1 H 6.772 . . 397 600 42 PHE HD2 H 6.772 . . 398 600 42 PHE HE1 H 6.926 . . 399 600 42 PHE HE2 H 6.926 . . 400 600 42 PHE HZ H 6.867 . . 401 600 42 PHE C C 170.981 . . 402 600 42 PHE CA C 54.792 . . 403 600 42 PHE CB C 42.675 . . 404 600 42 PHE CD1 C 134.458 . . 405 600 42 PHE CD2 C 134.458 . . 406 600 42 PHE CE1 C 130.137 . . 407 600 42 PHE CE2 C 130.137 . . 408 600 42 PHE CZ C 129.326 . . 409 600 42 PHE N N 120.860 . . 410 601 43 CYS H H 8.711 . . 411 601 43 CYS HA H 4.918 . . 412 601 43 CYS HB2 H 3.433 . . 413 601 43 CYS HB3 H 2.544 . . 414 601 43 CYS C C 175.770 . . 415 601 43 CYS CA C 57.836 . . 416 601 43 CYS CB C 31.950 . . 417 601 43 CYS N N 121.689 . . 418 602 44 VAL H H 8.035 . . 419 602 44 VAL HA H 4.130 . . 420 602 44 VAL HB H 2.190 . . 421 602 44 VAL HG1 H 0.581 . . 422 602 44 VAL HG2 H 0.709 . . 423 602 44 VAL C C 172.195 . . 424 602 44 VAL CA C 63.963 . . 425 602 44 VAL CB C 30.748 . . 426 602 44 VAL CG1 C 21.141 . . 427 602 44 VAL CG2 C 19.147 . . 428 602 44 VAL N N 123.237 . . 429 603 45 LEU H H 9.245 . . 430 603 45 LEU HA H 4.382 . . 431 603 45 LEU HB2 H 1.975 . . 432 603 45 LEU HB3 H 1.451 . . 433 603 45 LEU HG H 1.602 . . 434 603 45 LEU HD1 H 0.915 . . 435 603 45 LEU HD2 H 0.810 . . 436 603 45 LEU C C 175.240 . . 437 603 45 LEU CA C 56.796 . . 438 603 45 LEU CB C 42.474 . . 439 603 45 LEU CG C 27.109 . . 440 603 45 LEU CD1 C 25.845 . . 441 603 45 LEU CD2 C 22.522 . . 442 603 45 LEU N N 122.963 . . 443 604 46 CYS H H 8.134 . . 444 604 46 CYS HA H 4.875 . . 445 604 46 CYS HB2 H 3.403 . . 446 604 46 CYS HB3 H 3.008 . . 447 604 46 CYS C C 173.280 . . 448 604 46 CYS CA C 58.330 . . 449 604 46 CYS CB C 32.247 . . 450 604 46 CYS N N 116.618 . . 451 605 47 LEU H H 8.101 . . 452 605 47 LEU HA H 4.310 . . 453 605 47 LEU HB2 H 2.241 . . 454 605 47 LEU HB3 H 1.547 . . 455 605 47 LEU HG H 1.425 . . 456 605 47 LEU HD1 H 0.881 . . 457 605 47 LEU HD2 H 0.874 . . 458 605 47 LEU C C 172.832 . . 459 605 47 LEU CA C 57.023 . . 460 605 47 LEU CB C 37.603 . . 461 605 47 LEU CG C 27.060 . . 462 605 47 LEU CD1 C 25.428 . . 463 605 47 LEU CD2 C 22.472 . . 464 605 47 LEU N N 118.428 . . 465 606 48 CYS H H 8.107 . . 466 606 48 CYS HA H 4.899 . . 467 606 48 CYS HB2 H 3.412 . . 468 606 48 CYS HB3 H 3.181 . . 469 606 48 CYS C C 170.192 . . 470 606 48 CYS CA C 58.504 . . 471 606 48 CYS CB C 30.446 . . 472 606 48 CYS N N 116.435 . . 473 607 49 ALA H H 8.691 . . 474 607 49 ALA HA H 4.098 . . 475 607 49 ALA HB H 1.535 . . 476 607 49 ALA C C 174.200 . . 477 607 49 ALA CA C 52.922 . . 478 607 49 ALA CB C 18.618 . . 479 607 49 ALA N N 121.863 . . 480 608 50 TYR H H 8.609 . . 481 608 50 TYR HA H 3.601 . . 482 608 50 TYR HB2 H 2.564 . . 483 608 50 TYR HB3 H 2.345 . . 484 608 50 TYR HD1 H 6.850 . . 485 608 50 TYR HD2 H 6.850 . . 486 608 50 TYR HE1 H 6.780 . . 487 608 50 TYR HE2 H 6.780 . . 488 608 50 TYR C C 173.279 . . 489 608 50 TYR CA C 61.543 . . 490 608 50 TYR CB C 38.266 . . 491 608 50 TYR CD1 C 133.486 . . 492 608 50 TYR CD2 C 133.486 . . 493 608 50 TYR CE1 C 118.384 . . 494 608 50 TYR CE2 C 118.384 . . 495 608 50 TYR N N 122.484 . . 496 609 51 HIS H H 7.335 . . 497 609 51 HIS HA H 4.692 . . 498 609 51 HIS HB2 H 3.219 . . 499 609 51 HIS HB3 H 2.705 . . 500 609 51 HIS HD2 H 6.681 . . 501 609 51 HIS HE1 H 7.950 . . 502 609 51 HIS C C 172.493 . . 503 609 51 HIS CA C 53.151 . . 504 609 51 HIS CB C 27.160 . . 505 609 51 HIS CD2 C 128.509 . . 506 609 51 HIS CE1 C 141.148 . . 507 609 51 HIS N N 124.096 . . 508 610 52 GLY H H 5.241 . . 509 610 52 GLY HA2 H 3.779 . . 510 610 52 GLY HA3 H 3.406 . . 511 610 52 GLY C C 171.156 . . 512 610 52 GLY CA C 46.648 . . 513 610 52 GLY N N 106.656 . . 514 611 53 SER H H 8.620 . . 515 611 53 SER HA H 4.367 . . 516 611 53 SER HB2 H 3.957 . . 517 611 53 SER HB3 H 3.823 . . 518 611 53 SER C C 171.656 . . 519 611 53 SER CA C 58.232 . . 520 611 53 SER CB C 63.543 . . 521 611 53 SER N N 117.678 . . 522 612 54 GLU H H 7.642 . . 523 612 54 GLU HA H 4.265 . . 524 612 54 GLU HB2 H 2.095 . . 525 612 54 GLU HB3 H 2.032 . . 526 612 54 GLU HG2 H 2.319 . . 527 612 54 GLU HG3 H 2.319 . . 528 612 54 GLU C C 173.984 . . 529 612 54 GLU CA C 56.062 . . 530 612 54 GLU CB C 30.507 . . 531 612 54 GLU CG C 36.323 . . 532 612 54 GLU N N 121.382 . . 533 613 55 ASP H H 8.546 . . 534 613 55 ASP HA H 4.558 . . 535 613 55 ASP HB2 H 2.649 . . 536 613 55 ASP HB3 H 2.455 . . 537 613 55 ASP C C 173.930 . . 538 613 55 ASP CA C 54.729 . . 539 613 55 ASP CB C 41.160 . . 540 613 55 ASP N N 122.109 . . 541 614 56 CYS H H 8.018 . . 542 614 56 CYS HA H 3.460 . . 543 614 56 CYS HB2 H 2.720 . . 544 614 56 CYS HB3 H 2.521 . . 545 614 56 CYS C C 173.274 . . 546 614 56 CYS CA C 60.044 . . 547 614 56 CYS CB C 30.947 . . 548 614 56 CYS N N 121.636 . . 549 615 57 ARG H H 8.423 . . 550 615 57 ARG HA H 4.130 . . 551 615 57 ARG HB2 H 1.725 . . 552 615 57 ARG HB3 H 1.628 . . 553 615 57 ARG HG2 H 1.512 . . 554 615 57 ARG HG3 H 1.484 . . 555 615 57 ARG HD2 H 3.079 . . 556 615 57 ARG HD3 H 3.079 . . 557 615 57 ARG C C 173.392 . . 558 615 57 ARG CA C 56.077 . . 559 615 57 ARG CB C 30.225 . . 560 615 57 ARG CG C 27.128 . . 561 615 57 ARG CD C 43.327 . . 562 615 57 ARG N N 122.051 . . 563 616 58 ARG H H 8.216 . . 564 616 58 ARG HA H 4.300 . . 565 616 58 ARG HB2 H 1.804 . . 566 616 58 ARG HB3 H 1.660 . . 567 616 58 ARG HG2 H 1.533 . . 568 616 58 ARG HG3 H 1.533 . . 569 616 58 ARG HD2 H 3.113 . . 570 616 58 ARG HD3 H 3.113 . . 571 616 58 ARG C C 172.974 . . 572 616 58 ARG CA C 55.787 . . 573 616 58 ARG CB C 31.026 . . 574 616 58 ARG CG C 26.989 . . 575 616 58 ARG CD C 43.305 . . 576 616 58 ARG N N 122.987 . . 577 617 59 GLY H H 7.943 . . 578 617 59 GLY HA2 H 3.651 . . 579 617 59 GLY HA3 H 3.681 . . 580 617 59 GLY C C 176.247 . . 581 617 59 GLY CA C 46.118 . . 582 617 59 GLY N N 116.364 . . stop_ save_