data_18448 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Chemical Shift Assignment of the NIPP1 FHA Domain ; _BMRB_accession_number 18448 _BMRB_flat_file_name bmr18448.str _Entry_type original _Submission_date 2012-05-07 _Accession_date 2012-05-07 _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 O'Connell Nichole . . 2 Peti Wolfgang . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 121 "13C chemical shifts" 258 "15N chemical shifts" 121 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2013-02-14 original author . stop_ _Original_release_date 2013-02-14 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title 'NIPP1 maintains EZH2 phosphorylation and promoter occupancy at proliferation-related target genes' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 23241245 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Minnebo Nikki . . 2 Gornemann Janina . . 3 O'Connell Nichole . . 4 'Van Dessel' Nele . . 5 Derua Rita . . 6 Vermunt Marit W. . 7 Page Rebecca . . 8 Beullens Monique . . 9 Peti Wolfgang . . 10 'Van Eynde' Aleyde . . 11 Bollen Mathieu . . stop_ _Journal_abbreviation 'Nucleic Acids Res.' _Journal_volume 41 _Journal_issue 2 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 842 _Page_last 854 _Year 2013 _Details . save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name 'NIPP1 1-143' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'NIPP1 1-143' $NIPP1_FHA stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state ? _System_paramagnetic no _System_thiol_state . _Database_query_date . _Details 'Residues 1-2 are cloning artifacts. The NIPP1 FHA primary sequence residue 1 is residue 3 herein.' save_ ######################## # Monomeric polymers # ######################## save_NIPP1_FHA _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common NIPP1_FHA _Molecular_mass . _Mol_thiol_state 'all free' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 145 _Mol_residue_sequence ; GHMAAAANSGSSLPLFDCPT WAGKPPPGLHLDVVKGDKLI EKLIIDEKKYYLFGRNPDLC DFTIDHQSCSRVHAALVYHK HLKRVFLIDLNSTHGTFLGH IRLEPHKPQQIPIDSTVSFG ASTRAYTLREKPQTLPSAVK GDEKM ; loop_ _Residue_seq_code _Residue_label 1 GLY 2 HIS 3 MET 4 ALA 5 ALA 6 ALA 7 ALA 8 ASN 9 SER 10 GLY 11 SER 12 SER 13 LEU 14 PRO 15 LEU 16 PHE 17 ASP 18 CYS 19 PRO 20 THR 21 TRP 22 ALA 23 GLY 24 LYS 25 PRO 26 PRO 27 PRO 28 GLY 29 LEU 30 HIS 31 LEU 32 ASP 33 VAL 34 VAL 35 LYS 36 GLY 37 ASP 38 LYS 39 LEU 40 ILE 41 GLU 42 LYS 43 LEU 44 ILE 45 ILE 46 ASP 47 GLU 48 LYS 49 LYS 50 TYR 51 TYR 52 LEU 53 PHE 54 GLY 55 ARG 56 ASN 57 PRO 58 ASP 59 LEU 60 CYS 61 ASP 62 PHE 63 THR 64 ILE 65 ASP 66 HIS 67 GLN 68 SER 69 CYS 70 SER 71 ARG 72 VAL 73 HIS 74 ALA 75 ALA 76 LEU 77 VAL 78 TYR 79 HIS 80 LYS 81 HIS 82 LEU 83 LYS 84 ARG 85 VAL 86 PHE 87 LEU 88 ILE 89 ASP 90 LEU 91 ASN 92 SER 93 THR 94 HIS 95 GLY 96 THR 97 PHE 98 LEU 99 GLY 100 HIS 101 ILE 102 ARG 103 LEU 104 GLU 105 PRO 106 HIS 107 LYS 108 PRO 109 GLN 110 GLN 111 ILE 112 PRO 113 ILE 114 ASP 115 SER 116 THR 117 VAL 118 SER 119 PHE 120 GLY 121 ALA 122 SER 123 THR 124 ARG 125 ALA 126 TYR 127 THR 128 LEU 129 ARG 130 GLU 131 LYS 132 PRO 133 GLN 134 THR 135 LEU 136 PRO 137 SER 138 ALA 139 VAL 140 LYS 141 GLY 142 ASP 143 GLU 144 LYS 145 MET stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-10-14 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 15242 FHA_domain 91.03 140 99.24 99.24 3.54e-91 PDB 2JPE "Fha Domain Of Nipp1" 91.03 140 99.24 99.24 3.54e-91 DBJ BAC27653 "unnamed protein product [Mus musculus]" 67.59 306 100.00 100.00 2.38e-63 DBJ BAF84766 "unnamed protein product [Homo sapiens]" 98.62 351 100.00 100.00 9.37e-99 DBJ BAG65401 "unnamed protein product [Homo sapiens]" 98.62 199 100.00 100.00 6.98e-100 DBJ BAG73611 "protein phosphatase 1, regulatory (inhibitor) subunit 8 [synthetic construct]" 98.62 351 100.00 100.00 9.37e-99 EMBL CAA90625 "NIPP-1, nuclear inhibitor of protein phosphatase-1 [Bos taurus]" 98.62 351 100.00 100.00 8.78e-99 GB AAD22486 "nuclear inhibitor of phosphatase-1 [Homo sapiens]" 98.62 351 100.00 100.00 9.37e-99 GB AAD24669 "nuclear inhibitor of protein phosphatase-1 alpha [Homo sapiens]" 98.62 351 100.00 100.00 9.37e-99 GB AAD31541 "nuclear inhibitor of protein phosphatase-1 alpha [Homo sapiens]" 98.62 351 100.00 100.00 9.37e-99 GB AAH01597 "PPP1R8 protein, partial [Homo sapiens]" 75.86 318 100.00 100.00 4.42e-72 GB AAH25479 "Protein phosphatase 1, regulatory (inhibitor) subunit 8 [Mus musculus]" 98.62 351 99.30 99.30 4.24e-98 REF NP_001026062 "nuclear inhibitor of protein phosphatase 1 [Gallus gallus]" 89.66 354 97.69 99.23 5.76e-87 REF NP_001101381 "nuclear inhibitor of protein phosphatase 1 [Rattus norvegicus]" 98.62 351 99.30 99.30 5.81e-98 REF NP_001230343 "nuclear inhibitor of protein phosphatase 1 [Sus scrofa]" 98.62 351 100.00 100.00 8.22e-99 REF NP_001253391 "nuclear inhibitor of protein phosphatase 1 [Macaca mulatta]" 98.62 351 100.00 100.00 9.37e-99 REF NP_001277654 "nuclear inhibitor of protein phosphatase 1 isoform 2 [Mus musculus]" 98.62 350 99.30 99.30 4.11e-98 SP Q12972 "RecName: Full=Nuclear inhibitor of protein phosphatase 1; Short=NIPP-1; AltName: Full=Protein phosphatase 1 regulatory inhibito" 98.62 351 100.00 100.00 9.37e-99 SP Q28147 "RecName: Full=Nuclear inhibitor of protein phosphatase 1; Short=NIPP-1; AltName: Full=Protein phosphatase 1 regulatory inhibito" 98.62 351 100.00 100.00 8.78e-99 SP Q8R3G1 "RecName: Full=Nuclear inhibitor of protein phosphatase 1; Short=NIPP-1; AltName: Full=Protein phosphatase 1 regulatory inhibito" 98.62 351 99.30 99.30 4.24e-98 TPG DAA32062 "TPA: nuclear inhibitor of protein phosphatase 1 [Bos taurus]" 98.62 351 100.00 100.00 9.37e-99 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $NIPP1_FHA Human 9606 Eukaryota Metazoa Homo sapiens stop_ save_ ######################### # Experimental source # ######################### save_experimental_source _Saveframe_category experimental_source loop_ _Mol_label _Production_method _Host_organism_name_common _Genus _Species _Strain _Vector_name $NIPP1_FHA 'recombinant technology' . Escherichia coli . 'pET M30-MBP' stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Saveframe_category sample _Sample_type solution _Details ; 1mM NIPP1 1-143 20 mM Bis Tris pH 6.5 50 mM NaCl 5 mM DTT 0.25 mM PMSF ; loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $NIPP1_FHA 1 mM '[U-99% 13C; U-99% 15N]' PMSF 0.25 mM 'natural abundance' 'sodium chloride' 50 mM 'natural abundance' DTT 5 mM 'natural abundance' BisTris 20 mM 'natural abundance' H2O 90 % 'natural abundance' D2O 10 % 'natural abundance' stop_ save_ save_sample_2 _Saveframe_category sample _Sample_type solution _Details ; 1mM NIPP1 1-143 20 mM Bis Tris pH 6.5 50 mM NaCl 5 mM DTT 0.25 mM PMSF ; loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $NIPP1_FHA 1 mM '[U-99% 15N]' PMSF 0.25 mM 'natural abundance' 'sodium chloride' 50 mM 'natural abundance' DTT 5 mM 'natural abundance' BisTris 20 mM 'natural abundance' H2O 90 % 'natural abundance' D2O 10 % 'natural abundance' stop_ save_ ############################ # Computer software used # ############################ save_TOPSPIN _Saveframe_category software _Name TOPSPIN _Version 2.1 loop_ _Vendor _Address _Electronic_address 'Bruker Biospin' . . stop_ loop_ _Task collection processing stop_ _Details . save_ save_XEASY _Saveframe_category software _Name XEASY _Version 1.8.4 loop_ _Vendor _Address _Electronic_address 'Keller and Wuthrich' . . stop_ loop_ _Task 'chemical shift assignment' 'peak picking' stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model Avance _Field_strength 500 _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_2 save_ save_3D_HNCA_2 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCA' _Sample_label $sample_1 save_ save_3D_HNCACB_3 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCACB' _Sample_label $sample_1 save_ save_3D_C(CO)NH_4 _Saveframe_category NMR_applied_experiment _Experiment_name '3D C(CO)NH' _Sample_label $sample_1 save_ save_3D_CBCA(CO)NH_5 _Saveframe_category NMR_applied_experiment _Experiment_name '3D CBCA(CO)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' 50 . 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 . 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 na indirect . . . 0.251449530 DSS H 1 'methyl protons' ppm 0.00 internal direct . . . 1.000000000 DSS N 15 'methyl protons' ppm 0.00 na 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 HNCA' '3D HNCACB' '3D C(CO)NH' '3D CBCA(CO)NH' stop_ loop_ _Sample_label $sample_2 $sample_1 stop_ _Sample_conditions_label $sample_conditions_1 _Chem_shift_reference_set_label $chemical_shift_reference_1 _Mol_system_component_name 'NIPP1 1-143' _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 ALA CA C 52.757 0.414 1 2 7 7 ALA CB C 18.922 0.414 1 3 8 8 ASN H H 8.351 0.007 1 4 8 8 ASN CA C 52.947 0.414 1 5 8 8 ASN CB C 38.743 0.414 1 6 8 8 ASN N N 117.67 0.095 1 7 9 9 SER H H 8.15 0.007 1 8 9 9 SER CA C 58.388 0.414 1 9 9 9 SER CB C 63.907 0.414 1 10 9 9 SER N N 116.02 0.095 1 11 10 10 GLY H H 7.974 0.007 1 12 10 10 GLY CA C 45.312 0.414 1 13 10 10 GLY N N 116.86 0.095 1 14 11 11 SER H H 8.088 0.007 1 15 11 11 SER CA C 58.17 0.414 1 16 11 11 SER CB C 63.844 0.414 1 17 11 11 SER N N 115.36 0.095 1 18 12 12 SER H H 8.239 0.007 1 19 12 12 SER CA C 58.17 0.414 1 20 12 12 SER CB C 63.822 0.414 1 21 12 12 SER N N 117.97 0.095 1 22 13 13 LEU H H 8.071 0.007 1 23 13 13 LEU CA C 53.023 0.414 1 24 13 13 LEU CB C 41.576 0.414 1 25 13 13 LEU N N 124.9 0.095 1 26 14 14 PRO CA C 62.722 0.414 1 27 14 14 PRO CB C 31.53 0.414 1 28 15 15 LEU H H 8.288 0.007 1 29 15 15 LEU CA C 55.912 0.414 1 30 15 15 LEU CB C 42.269 0.414 1 31 15 15 LEU N N 122.45 0.095 1 32 16 16 PHE H H 7.676 0.007 1 33 16 16 PHE CA C 56.729 0.414 1 34 16 16 PHE CB C 40.85 0.414 1 35 16 16 PHE N N 117.76 0.095 1 36 17 17 ASP H H 7.782 0.007 1 37 17 17 ASP CA C 51.775 0.414 1 38 17 17 ASP CB C 40.392 0.414 1 39 17 17 ASP N N 128.22 0.095 1 40 18 18 CYS H H 7.688 0.007 1 41 18 18 CYS CA C 56.944 0.414 1 42 18 18 CYS CB C 26.76 0.414 1 43 18 18 CYS N N 125.27 0.095 1 44 19 19 PRO CA C 62.331 0.414 1 45 19 19 PRO CB C 31.009 0.414 1 46 20 20 THR H H 8.588 0.007 1 47 20 20 THR CA C 64.153 0.414 1 48 20 20 THR CB C 68.441 0.414 1 49 20 20 THR N N 114.07 0.095 1 50 21 21 TRP H H 6.329 0.007 1 51 21 21 TRP CA C 53.358 0.414 1 52 21 21 TRP CB C 28.332 0.414 1 53 21 21 TRP N N 114.17 0.095 1 54 22 22 ALA H H 6.765 0.007 1 55 22 22 ALA CA C 52.215 0.414 1 56 22 22 ALA CB C 20.604 0.414 1 57 22 22 ALA N N 123.58 0.095 1 58 23 23 GLY H H 8.96 0.007 1 59 23 23 GLY CA C 44.52 0.414 1 60 23 23 GLY N N 109.12 0.095 1 61 27 27 PRO CA C 63.146 0.414 1 62 27 27 PRO CB C 31.963 0.414 1 63 28 28 GLY H H 10.741 0.007 1 64 28 28 GLY CA C 45.418 0.414 1 65 28 28 GLY N N 113.31 0.095 1 66 29 29 LEU H H 7.112 0.007 1 67 29 29 LEU CA C 56.325 0.414 1 68 29 29 LEU CB C 42.546 0.414 1 69 29 29 LEU N N 126.55 0.095 1 70 30 30 HIS H H 8.839 0.007 1 71 30 30 HIS CA C 55.288 0.414 1 72 30 30 HIS CB C 31.015 0.414 1 73 30 30 HIS N N 120.59 0.095 1 74 31 31 LEU H H 9.102 0.007 1 75 31 31 LEU CA C 52.406 0.414 1 76 31 31 LEU CB C 44.235 0.414 1 77 31 31 LEU N N 117.33 0.095 1 78 32 32 ASP H H 9.032 0.007 1 79 32 32 ASP CA C 53.847 0.414 1 80 32 32 ASP CB C 42 0.414 1 81 32 32 ASP N N 124.81 0.095 1 82 33 33 VAL H H 8.587 0.007 1 83 33 33 VAL CA C 61.484 0.414 1 84 33 33 VAL CB C 31.468 0.414 1 85 33 33 VAL N N 124.25 0.095 1 86 34 34 VAL H H 8.748 0.007 1 87 34 34 VAL CA C 59.627 0.414 1 88 34 34 VAL CB C 35.137 0.414 1 89 34 34 VAL N N 126.46 0.095 1 90 38 38 LYS CA C 58.286 0.414 1 91 38 38 LYS CB C 32.931 0.414 1 92 39 39 LEU H H 8.356 0.007 1 93 39 39 LEU CA C 55.093 0.414 1 94 39 39 LEU CB C 41.681 0.414 1 95 39 39 LEU N N 126.51 0.095 1 96 40 40 ILE H H 9.274 0.007 1 97 40 40 ILE CA C 62.004 0.414 1 98 40 40 ILE CB C 39.317 0.414 1 99 40 40 ILE N N 126.22 0.095 1 100 41 41 GLU H H 7.545 0.007 1 101 41 41 GLU CA C 55.152 0.414 1 102 41 41 GLU CB C 31.973 0.414 1 103 41 41 GLU N N 116.04 0.095 1 104 42 42 LYS H H 8.248 0.007 1 105 42 42 LYS CA C 55.179 0.414 1 106 42 42 LYS CB C 35.294 0.414 1 107 42 42 LYS N N 118.9 0.095 1 108 43 43 LEU H H 9.27 0.007 1 109 43 43 LEU CA C 52.596 0.414 1 110 43 43 LEU CB C 41.744 0.414 1 111 43 43 LEU N N 123.43 0.095 1 112 44 44 ILE H H 8.797 0.007 1 113 44 44 ILE CA C 61.896 0.414 1 114 44 44 ILE CB C 36.938 0.414 1 115 44 44 ILE N N 126.13 0.095 1 116 45 45 ILE H H 7.328 0.007 1 117 45 45 ILE CA C 59.557 0.414 1 118 45 45 ILE CB C 37.274 0.414 1 119 45 45 ILE N N 120.4 0.095 1 120 46 46 ASP H H 6.794 0.007 1 121 46 46 ASP CA C 52.596 0.414 1 122 46 46 ASP CB C 42 0.414 1 123 46 46 ASP N N 114.97 0.095 1 124 47 47 GLU H H 7.574 0.007 1 125 47 47 GLU CA C 57.137 0.414 1 126 47 47 GLU CB C 33.058 0.414 1 127 47 47 GLU N N 115.36 0.095 1 128 48 48 LYS H H 7.374 0.007 1 129 48 48 LYS CA C 55.288 0.414 1 130 48 48 LYS CB C 34.91 0.414 1 131 48 48 LYS N N 116.81 0.095 1 132 49 49 LYS H H 7.98 0.007 1 133 49 49 LYS CA C 57.681 0.414 1 134 49 49 LYS CB C 33.314 0.414 1 135 49 49 LYS N N 115.3 0.095 1 136 50 50 TYR H H 6.569 0.007 1 137 50 50 TYR CA C 56.049 0.414 1 138 50 50 TYR CB C 41.808 0.414 1 139 50 50 TYR N N 109.22 0.095 1 140 51 51 TYR H H 9.11 0.007 1 141 51 51 TYR CA C 56.947 0.414 1 142 51 51 TYR CB C 43.98 0.414 1 143 51 51 TYR N N 117.05 0.095 1 144 52 52 LEU H H 9.698 0.007 1 145 52 52 LEU CA C 53.629 0.414 1 146 52 52 LEU CB C 45.768 0.414 1 147 52 52 LEU N N 120.57 0.095 1 148 53 53 PHE H H 9.085 0.007 1 149 53 53 PHE CA C 55.478 0.414 1 150 53 53 PHE CB C 42.128 0.414 1 151 53 53 PHE N N 120.78 0.095 1 152 54 54 GLY H H 8.206 0.007 1 153 54 54 GLY CA C 47.212 0.414 1 154 54 54 GLY N N 109.2 0.095 1 155 55 55 ARG H H 8.443 0.007 1 156 55 55 ARG CA C 56.947 0.414 1 157 55 55 ARG CB C 32.356 0.414 1 158 55 55 ARG N N 119.6 0.095 1 159 56 56 ASN H H 8.106 0.007 1 160 56 56 ASN CA C 50.937 0.414 1 161 56 56 ASN CB C 39.637 0.414 1 162 56 56 ASN N N 117.19 0.095 1 163 57 57 PRO CA C 63.989 0.414 1 164 57 57 PRO CB C 32.025 0.414 1 165 58 58 ASP H H 7.917 0.007 1 166 58 58 ASP CA C 55.778 0.414 1 167 58 58 ASP CB C 40.339 0.414 1 168 58 58 ASP N N 116.37 0.095 1 169 59 59 LEU H H 7.006 0.007 1 170 59 59 LEU CA C 54.636 0.414 1 171 59 59 LEU CB C 45.321 0.414 1 172 59 59 LEU N N 115.63 0.095 1 173 60 60 CYS H H 6.969 0.007 1 174 60 60 CYS CA C 58.361 0.414 1 175 60 60 CYS CB C 29.673 0.414 1 176 60 60 CYS N N 113.33 0.095 1 177 61 61 ASP H H 7.709 0.007 1 178 61 61 ASP CA C 57.028 0.414 1 179 61 61 ASP CB C 42.83 0.414 1 180 61 61 ASP N N 120.97 0.095 1 181 62 62 PHE H H 7.383 0.007 1 182 62 62 PHE CA C 55.043 0.414 1 183 62 62 PHE CB C 40.786 0.414 1 184 62 62 PHE N N 115.68 0.095 1 185 63 63 THR H H 8.496 0.007 1 186 63 63 THR CA C 60.482 0.414 1 187 63 63 THR CB C 69.655 0.414 1 188 63 63 THR N N 116.66 0.095 1 189 64 64 ILE H H 7.774 0.007 1 190 64 64 ILE CA C 60.273 0.414 1 191 64 64 ILE CB C 38.945 0.414 1 192 64 64 ILE N N 125.28 0.095 1 193 65 65 ASP H H 8.284 0.007 1 194 65 65 ASP CA C 53.819 0.414 1 195 65 65 ASP CB C 40.053 0.414 1 196 65 65 ASP N N 123.38 0.095 1 197 66 66 HIS H H 7.563 0.007 1 198 66 66 HIS CA C 59.332 0.414 1 199 66 66 HIS CB C 33.683 0.414 1 200 66 66 HIS N N 122.04 0.095 1 201 67 67 GLN H H 8.376 0.007 1 202 67 67 GLN CA C 58.33 0.414 1 203 67 67 GLN CB C 27.937 0.414 1 204 67 67 GLN N N 125.02 0.095 1 205 68 68 SER H H 8.924 0.007 1 206 68 68 SER CA C 59.421 0.414 1 207 68 68 SER CB C 63.587 0.414 1 208 68 68 SER N N 115.11 0.095 1 209 69 69 CYS CA C 60.019 0.414 1 210 69 69 CYS CB C 28.477 0.414 1 211 70 70 SER H H 11.69 0.007 1 212 70 70 SER CA C 60.494 0.414 1 213 70 70 SER CB C 64.824 0.414 1 214 70 70 SER N N 125.18 0.095 1 215 71 71 ARG H H 8.793 0.007 1 216 71 71 ARG CA C 61.461 0.414 1 217 71 71 ARG CB C 30.376 0.414 1 218 71 71 ARG N N 124.56 0.095 1 219 72 72 VAL H H 7.201 0.007 1 220 72 72 VAL CA C 64.37 0.414 1 221 72 72 VAL CB C 32.994 0.414 1 222 72 72 VAL N N 113.94 0.095 1 223 73 73 HIS H H 9.231 0.007 1 224 73 73 HIS CA C 59.582 0.414 1 225 73 73 HIS CB C 36.446 0.414 1 226 73 73 HIS N N 129.02 0.095 1 227 74 74 ALA H H 8.049 0.007 1 228 74 74 ALA CA C 51.318 0.414 1 229 74 74 ALA CB C 23.925 0.414 1 230 74 74 ALA N N 114.97 0.095 1 231 75 75 ALA H H 8.96 0.007 1 232 75 75 ALA CA C 49.795 0.414 1 233 75 75 ALA CB C 22.903 0.414 1 234 75 75 ALA N N 121.07 0.095 1 235 76 76 LEU H H 9.456 0.007 1 236 76 76 LEU CA C 54.645 0.414 1 237 76 76 LEU CB C 46.769 0.414 1 238 76 76 LEU N N 126.26 0.095 1 239 77 77 VAL H H 9.574 0.007 1 240 77 77 VAL CA C 60.629 0.414 1 241 77 77 VAL CB C 36.73 0.414 1 242 77 77 VAL N N 123.94 0.095 1 243 78 78 TYR H H 8.843 0.007 1 244 78 78 TYR CA C 58.832 0.414 1 245 78 78 TYR CB C 39.112 0.414 1 246 78 78 TYR N N 128.45 0.095 1 247 79 79 HIS H H 8.696 0.007 1 248 79 79 HIS CA C 55.843 0.414 1 249 79 79 HIS CB C 33.342 0.414 1 250 79 79 HIS N N 130.04 0.095 1 251 80 80 LYS H H 8.546 0.007 1 252 80 80 LYS CA C 58.565 0.414 1 253 80 80 LYS CB C 33.291 0.414 1 254 80 80 LYS N N 125.85 0.095 1 255 81 81 HIS H H 8.48 0.007 1 256 81 81 HIS CA C 57.572 0.414 1 257 81 81 HIS CB C 31.717 0.414 1 258 81 81 HIS N N 118.12 0.095 1 259 82 82 LEU H H 9.008 0.007 1 260 82 82 LEU CA C 55.071 0.414 1 261 82 82 LEU CB C 41.744 0.414 1 262 82 82 LEU N N 120.03 0.095 1 263 83 83 LYS H H 8.048 0.007 1 264 83 83 LYS CA C 57.056 0.414 1 265 83 83 LYS CB C 28.46 0.414 1 266 83 83 LYS N N 116.34 0.095 1 267 84 84 ARG H H 6.376 0.007 1 268 84 84 ARG CA C 53.004 0.414 1 269 84 84 ARG CB C 35.102 0.414 1 270 84 84 ARG N N 114.01 0.095 1 271 85 85 VAL H H 8.944 0.007 1 272 85 85 VAL CA C 62.722 0.414 1 273 85 85 VAL CB C 32.368 0.414 1 274 85 85 VAL N N 123.38 0.095 1 275 86 86 PHE H H 9.46 0.007 1 276 86 86 PHE CA C 56.729 0.414 1 277 86 86 PHE CB C 43.788 0.414 1 278 86 86 PHE N N 124.04 0.095 1 279 87 87 LEU H H 9.095 0.007 1 280 87 87 LEU CA C 52.786 0.414 1 281 87 87 LEU CB C 46.726 0.414 1 282 87 87 LEU N N 123 0.095 1 283 88 88 ILE H H 9.377 0.007 1 284 88 88 ILE CA C 60.074 0.414 1 285 88 88 ILE CB C 41.361 0.414 1 286 88 88 ILE N N 123.24 0.095 1 287 89 89 ASP H H 9.987 0.007 1 288 89 89 ASP CA C 55.009 0.414 1 289 89 89 ASP CB C 43.945 0.414 1 290 89 89 ASP N N 128.2 0.095 1 291 90 90 LEU H H 8.283 0.007 1 292 90 90 LEU CA C 52.562 0.414 1 293 90 90 LEU CB C 37.576 0.414 1 294 90 90 LEU N N 129.34 0.095 1 295 91 91 ASN H H 7.559 0.007 1 296 91 91 ASN CA C 53.385 0.414 1 297 91 91 ASN CB C 37.314 0.414 1 298 91 91 ASN N N 118.01 0.095 1 299 92 92 SER H H 8.363 0.007 1 300 92 92 SER CA C 59.013 0.414 1 301 92 92 SER CB C 60.585 0.414 1 302 92 92 SER N N 116.82 0.095 1 303 93 93 THR H H 7.031 0.007 1 304 93 93 THR CA C 66.219 0.414 1 305 93 93 THR CB C 68.952 0.414 1 306 93 93 THR N N 117.57 0.095 1 307 94 94 HIS H H 9.453 0.007 1 308 94 94 HIS CA C 56.729 0.414 1 309 94 94 HIS CB C 30.44 0.414 1 310 94 94 HIS N N 115.87 0.095 1 311 95 95 GLY H H 7.233 0.007 1 312 95 95 GLY CA C 45.2 0.414 1 313 95 95 GLY N N 108.49 0.095 1 314 96 96 THR H H 8.204 0.007 1 315 96 96 THR CA C 63.772 0.414 1 316 96 96 THR CB C 69.719 0.414 1 317 96 96 THR N N 122.3 0.095 1 318 97 97 PHE H H 8.735 0.007 1 319 97 97 PHE CA C 56.915 0.414 1 320 97 97 PHE CB C 41.784 0.414 1 321 97 97 PHE N N 123.85 0.095 1 322 98 98 LEU H H 8.493 0.007 1 323 98 98 LEU CA C 52.655 0.414 1 324 98 98 LEU CB C 43.724 0.414 1 325 98 98 LEU N N 123.19 0.095 1 326 99 99 GLY H H 8.484 0.007 1 327 99 99 GLY CA C 47.403 0.414 1 328 99 99 GLY N N 117.66 0.095 1 329 100 100 HIS H H 8.772 0.007 1 330 100 100 HIS CA C 55.914 0.414 1 331 100 100 HIS CB C 28.971 0.414 1 332 100 100 HIS N N 122.73 0.095 1 333 101 101 ILE H H 8.08 0.007 1 334 101 101 ILE CA C 60.658 0.414 1 335 101 101 ILE CB C 38.184 0.414 1 336 101 101 ILE N N 123.05 0.095 1 337 102 102 ARG H H 8.564 0.007 1 338 102 102 ARG CA C 55.617 0.414 1 339 102 102 ARG CB C 30.792 0.414 1 340 102 102 ARG N N 129.31 0.095 1 341 103 103 LEU H H 8.569 0.007 1 342 103 103 LEU CA C 56.298 0.414 1 343 103 103 LEU CB C 40.84 0.414 1 344 103 103 LEU N N 130.03 0.095 1 345 104 104 GLU H H 9.012 0.007 1 346 104 104 GLU CA C 53.82 0.414 1 347 104 104 GLU CB C 29.929 0.414 1 348 104 104 GLU N N 123.19 0.095 1 349 105 105 PRO CA C 63.826 0.414 1 350 105 105 PRO CB C 32.472 0.414 1 351 106 106 HIS H H 9.088 0.007 1 352 106 106 HIS CA C 59.122 0.414 1 353 106 106 HIS CB C 27.949 0.414 1 354 106 106 HIS N N 114.2 0.095 1 355 107 107 LYS H H 7.657 0.007 1 356 107 107 LYS CA C 53.2 0.414 1 357 107 107 LYS CB C 33.06 0.414 1 358 107 107 LYS N N 121.82 0.095 1 359 108 108 PRO CA C 63.873 0.414 1 360 108 108 PRO CB C 32.508 0.414 1 361 109 109 GLN H H 9.188 0.007 1 362 109 109 GLN CA C 53.383 0.414 1 363 109 109 GLN CB C 31.368 0.414 1 364 109 109 GLN N N 126.74 0.095 1 365 110 110 GLN H H 8.873 0.007 1 366 110 110 GLN CA C 56.328 0.414 1 367 110 110 GLN CB C 28.04 0.414 1 368 110 110 GLN N N 130.06 0.095 1 369 111 111 ILE H H 8.45 0.007 1 370 111 111 ILE CA C 55.5 0.414 1 371 111 111 ILE CB C 35.276 0.414 1 372 111 111 ILE N N 125.46 0.095 1 373 112 112 PRO CA C 62.073 0.414 1 374 112 112 PRO CB C 31.835 0.414 1 375 113 113 ILE H H 8.319 0.007 1 376 113 113 ILE CA C 61.923 0.414 1 377 113 113 ILE CB C 35.207 0.414 1 378 113 113 ILE N N 122.76 0.095 1 379 114 114 ASP H H 8.889 0.007 1 380 114 114 ASP CA C 57.355 0.414 1 381 114 114 ASP CB C 38.078 0.414 1 382 114 114 ASP N N 121.06 0.095 1 383 115 115 SER H H 7.787 0.007 1 384 115 115 SER CA C 59.639 0.414 1 385 115 115 SER CB C 64.143 0.414 1 386 115 115 SER N N 115.96 0.095 1 387 116 116 THR H H 7.969 0.007 1 388 116 116 THR CA C 62.358 0.414 1 389 116 116 THR CB C 71.124 0.414 1 390 116 116 THR N N 115.99 0.095 1 391 117 117 VAL H H 9.206 0.007 1 392 117 117 VAL CA C 58.198 0.414 1 393 117 117 VAL CB C 34.527 0.414 1 394 117 117 VAL N N 123.02 0.095 1 395 118 118 SER H H 8.414 0.007 1 396 118 118 SER CA C 57.572 0.414 1 397 118 118 SER CB C 65.811 0.414 1 398 118 118 SER N N 113.79 0.095 1 399 119 119 PHE H H 8.979 0.007 1 400 119 119 PHE CA C 56.512 0.414 1 401 119 119 PHE CB C 42.064 0.414 1 402 119 119 PHE N N 118.05 0.095 1 403 120 120 GLY H H 9.285 0.007 1 404 120 120 GLY CA C 46.804 0.414 1 405 120 120 GLY N N 110.86 0.095 1 406 121 121 ALA H H 8.994 0.007 1 407 121 121 ALA CA C 50.113 0.414 1 408 121 121 ALA CB C 18.504 0.414 1 409 121 121 ALA N N 127.31 0.095 1 410 122 122 SER H H 7.353 0.007 1 411 122 122 SER CA C 58.143 0.414 1 412 122 122 SER CB C 62.757 0.414 1 413 122 122 SER N N 112.91 0.095 1 414 123 123 THR H H 8.214 0.007 1 415 123 123 THR CA C 61.923 0.414 1 416 123 123 THR CB C 68.697 0.414 1 417 123 123 THR N N 116.62 0.095 1 418 124 124 ARG H H 7.489 0.007 1 419 124 124 ARG CA C 56.838 0.414 1 420 124 124 ARG CB C 31.973 0.414 1 421 124 124 ARG N N 121.35 0.095 1 422 125 125 ALA H H 8.73 0.007 1 423 125 125 ALA CA C 50.93 0.414 1 424 125 125 ALA CB C 21.384 0.414 1 425 125 125 ALA N N 128.02 0.095 1 426 126 126 TYR H H 8.713 0.007 1 427 126 126 TYR CA C 56.561 0.414 1 428 126 126 TYR CB C 39.361 0.414 1 429 126 126 TYR N N 121.35 0.095 1 430 127 127 THR H H 9.329 0.007 1 431 127 127 THR CA C 61.352 0.414 1 432 127 127 THR CB C 70.613 0.414 1 433 127 127 THR N N 121.62 0.095 1 434 128 128 LEU H H 8.115 0.007 1 435 128 128 LEU CA C 55.699 0.414 1 436 128 128 LEU CB C 42.504 0.414 1 437 128 128 LEU N N 129.71 0.095 1 438 129 129 ARG H H 8.794 0.007 1 439 129 129 ARG CA C 52.788 0.414 1 440 129 129 ARG CB C 33.891 0.414 1 441 129 129 ARG N N 125.56 0.095 1 442 130 130 GLU H H 8.019 0.007 1 443 130 130 GLU CA C 54.119 0.414 1 444 130 130 GLU CB C 32.484 0.414 1 445 130 130 GLU N N 116.58 0.095 1 446 131 131 LYS H H 8.456 0.007 1 447 131 131 LYS CA C 54.391 0.414 1 448 131 131 LYS CB C 33.129 0.414 1 449 131 131 LYS N N 122.69 0.095 1 450 132 132 PRO CA C 63.134 0.414 1 451 132 132 PRO CB C 32.007 0.414 1 452 133 133 GLN H H 8.547 0.007 1 453 133 133 GLN CA C 55.706 0.414 1 454 133 133 GLN CB C 29.46 0.414 1 455 133 133 GLN N N 121.55 0.095 1 456 134 134 THR H H 8.131 0.007 1 457 134 134 THR CA C 61.705 0.414 1 458 134 134 THR CB C 69.91 0.414 1 459 134 134 THR N N 116.58 0.095 1 460 135 135 LEU H H 8.315 0.007 1 461 135 135 LEU CA C 52.994 0.414 1 462 135 135 LEU CB C 41.784 0.414 1 463 135 135 LEU N N 126.6 0.095 1 464 136 136 PRO CA C 63.137 0.414 1 465 136 136 PRO CB C 31.884 0.414 1 466 137 137 SER H H 8.183 0.007 1 467 137 137 SER CA C 58.17 0.414 1 468 137 137 SER CB C 63.843 0.414 1 469 137 137 SER N N 115.45 0.095 1 470 138 138 ALA H H 8.219 0.007 1 471 138 138 ALA CA C 52.375 0.414 1 472 138 138 ALA CB C 19.282 0.414 1 473 138 138 ALA N N 126.08 0.095 1 474 139 139 VAL H H 7.974 0.007 1 475 139 139 VAL CA C 62.14 0.414 1 476 139 139 VAL CB C 32.739 0.414 1 477 139 139 VAL N N 119.57 0.095 1 478 140 140 LYS H H 8.421 0.007 1 479 140 140 LYS CA C 56.502 0.414 1 480 140 140 LYS CB C 32.838 0.414 1 481 140 140 LYS N N 125.88 0.095 1 482 141 141 GLY H H 8.414 0.007 1 483 141 141 GLY CA C 45.254 0.414 1 484 141 141 GLY N N 110.75 0.095 1 485 142 142 ASP H H 8.152 0.007 1 486 142 142 ASP CA C 54.119 0.414 1 487 142 142 ASP CB C 40.914 0.414 1 488 142 142 ASP N N 120.3 0.095 1 489 143 143 GLU H H 8.35 0.007 1 490 143 143 GLU CA C 56.945 0.414 1 491 143 143 GLU CB C 29.929 0.414 1 492 143 143 GLU N N 121.12 0.095 1 493 144 144 LYS H H 8.238 0.007 1 494 144 144 LYS CA C 56.119 0.414 1 495 144 144 LYS CB C 32.645 0.414 1 496 144 144 LYS N N 122.49 0.095 1 497 145 145 MET H H 7.887 0.007 1 498 145 145 MET CA C 56.925 0.414 1 499 145 145 MET CB C 33.544 0.414 1 500 145 145 MET N N 127.11 0.095 1 stop_ save_