data_5808 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Chemical shift assignments and relaxation parameters for the PAH2 domain of mSin3B bound to an extended SID of Mad1 ; _BMRB_accession_number 5808 _BMRB_flat_file_name bmr5808.str _Entry_type original _Submission_date 2003-05-22 _Accession_date 2003-05-22 _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 'van Ingen' Hugo . . 2 Jansen Jaap F.A. . 3 Spronk Chris A.E.M. . 4 Vuister Geerten W. . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 S2_parameters 1 T1_relaxation 1 heteronucl_NOE 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 472 "13C chemical shifts" 269 "15N chemical shifts" 90 "T1 relaxation values" 78 "order parameters" 77 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2004-02-12 original author . stop_ loop_ _Related_BMRB_accession_number _Relationship 5457 'chemical shift assignment of SID24' 4841 'chemical shift assignment of PAH2:SID13 complex' stop_ _Original_release_date 2004-02-12 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; Extension of the binding motif of the Sin3 Interacting Domain of the mad family proteins ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 14705930 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 'van Ingen' Hugo . . 2 Lasonder Edwin . . 3 Jansen Jaap F.A. . 4 Kaan Anita M. . 5 Spronk Chris A.E.M. . 6 Stunnenberg Henk G. . 7 Vuister Geerten W. . stop_ _Journal_abbreviation Biochemistry _Journal_volume 43 _Journal_issue 1 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 46 _Page_last 54 _Year 2004 _Details . loop_ _Keyword MAD Sin 'Interacting Domain' PAH Sin3 stop_ save_ ################################## # Molecular system description # ################################## save_system_PAH2_SID _Saveframe_category molecular_system _Mol_system_name 'PAH2-SID24 complex' _Abbreviation_common 'PAH2, SID24' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'PAH2 domain of mSin3B' $PAH2 'SID domain of Mad1' $SID24 stop_ _System_molecular_weight 15300 _System_physical_state native _System_oligomer_state complex _System_paramagnetic no _System_thiol_state 'not present' loop_ _Biological_function 'regulation of gene transcription' stop_ _Database_query_date . _Details '1:1 complex between PAH2 domain of mSin3B and extended SID domain of Mad1.' save_ ######################## # Monomeric polymers # ######################## save_PAH2 _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'PAH2 domain' _Abbreviation_common PAH2 _Molecular_mass . _Mol_thiol_state 'not present' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 105 _Mol_residue_sequence ; ESDSVEFNNAISYVNKIKTR FLDHPEIYRSFLEILHTYQK EQLHTKGRPFRGMSEEEVFT EVANLFRGQEDLLSEFGQFL PEAKRSLFTGNGSAEMNSGQ KNEEK ; loop_ _Residue_seq_code _Residue_label 1 GLU 2 SER 3 ASP 4 SER 5 VAL 6 GLU 7 PHE 8 ASN 9 ASN 10 ALA 11 ILE 12 SER 13 TYR 14 VAL 15 ASN 16 LYS 17 ILE 18 LYS 19 THR 20 ARG 21 PHE 22 LEU 23 ASP 24 HIS 25 PRO 26 GLU 27 ILE 28 TYR 29 ARG 30 SER 31 PHE 32 LEU 33 GLU 34 ILE 35 LEU 36 HIS 37 THR 38 TYR 39 GLN 40 LYS 41 GLU 42 GLN 43 LEU 44 HIS 45 THR 46 LYS 47 GLY 48 ARG 49 PRO 50 PHE 51 ARG 52 GLY 53 MET 54 SER 55 GLU 56 GLU 57 GLU 58 VAL 59 PHE 60 THR 61 GLU 62 VAL 63 ALA 64 ASN 65 LEU 66 PHE 67 ARG 68 GLY 69 GLN 70 GLU 71 ASP 72 LEU 73 LEU 74 SER 75 GLU 76 PHE 77 GLY 78 GLN 79 PHE 80 LEU 81 PRO 82 GLU 83 ALA 84 LYS 85 ARG 86 SER 87 LEU 88 PHE 89 THR 90 GLY 91 ASN 92 GLY 93 SER 94 ALA 95 GLU 96 MET 97 ASN 98 SER 99 GLY 100 GLN 101 LYS 102 ASN 103 GLU 104 GLU 105 LYS stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-01-28 loop_ _Database_name _Database_accession_code _Database_entry_mol_name _Sequence_query_to_submitted_percentage _Sequence_subject_length _Sequence_identity _Sequence_positive _Sequence_homology_expectation_value PDB 1G1E "Nmr Structure Of The Human Mad1 Transrepression Domain Sid In Complex With Mammalian Sin3a Pah2 Domain" 66.67 16 100.00 100.00 7.14e-01 PDB 1PD7 "Extended Sid Of Mad1 Bound To The Pah2 Domain Of Msin3b" 100.00 24 100.00 100.00 2.58e-06 PDB 1S5Q "Solution Structure Of Mad1 Sid-Msin3a Pah2 Complex" 66.67 16 100.00 100.00 7.14e-01 DBJ BAG35605 "unnamed protein product [Homo sapiens]" 100.00 221 100.00 100.00 2.55e-06 DBJ BAG73371 "MAX dimerization protein 1 [synthetic construct]" 100.00 221 100.00 100.00 2.55e-06 DBJ BAH13406 "unnamed protein product [Homo sapiens]" 100.00 105 100.00 100.00 1.73e-06 EMBL CAG38734 "MAD [Homo sapiens]" 100.00 221 100.00 100.00 2.55e-06 EMBL CAG46493 "MAD [Homo sapiens]" 100.00 221 100.00 100.00 2.55e-06 GB AAA36194 "antagonizer of myc transcriptional activity [Homo sapiens]" 100.00 221 100.00 100.00 2.55e-06 GB AAH69377 "MAX dimerization protein 1 [Homo sapiens]" 100.00 221 100.00 100.00 2.55e-06 GB AAH69433 "MAX dimerization protein 1 [Homo sapiens]" 100.00 221 100.00 100.00 2.55e-06 GB AAH98396 "MAX dimerization protein 1 [Homo sapiens]" 100.00 221 100.00 100.00 2.55e-06 GB AAI13532 "MAX dimerization protein 1 [Homo sapiens]" 100.00 221 100.00 100.00 2.55e-06 REF NP_001179309 "max dimerization protein 1 [Bos taurus]" 100.00 222 100.00 100.00 2.46e-06 REF NP_001189442 "max dimerization protein 1 isoform 2 [Homo sapiens]" 100.00 220 100.00 100.00 2.39e-06 REF NP_001189443 "max dimerization protein 1 isoform 3 [Homo sapiens]" 100.00 211 100.00 100.00 2.19e-06 REF NP_001247787 "max dimerization protein 1 [Macaca mulatta]" 100.00 221 100.00 100.00 2.64e-06 REF NP_002348 "max dimerization protein 1 isoform 1 [Homo sapiens]" 100.00 221 100.00 100.00 2.55e-06 SP Q05195 "RecName: Full=Max dimerization protein 1; Short=Max dimerizer 1; AltName: Full=Protein MAD [Homo sapiens]" 100.00 221 100.00 100.00 2.55e-06 TPG DAA24557 "TPA: MAX dimerization protein 1-like [Bos taurus]" 100.00 222 100.00 100.00 2.46e-06 stop_ save_ save_SID24 _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common Mad1 _Name_variant 'SID domain of Hs. Mad1' _Abbreviation_common SID _Molecular_mass 2973 _Mol_thiol_state 'not present' _Details . _Residue_count 24 _Mol_residue_sequence ; VRMNIQMLLEAADYLERRER EAEH ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 5 VAL 2 6 ARG 3 7 MET 4 8 ASN 5 9 ILE 6 10 GLN 7 11 MET 8 12 LEU 9 13 LEU 10 14 GLU 11 15 ALA 12 16 ALA 13 17 ASP 14 18 TYR 15 19 LEU 16 20 GLU 17 21 ARG 18 22 ARG 19 23 GLU 20 24 ARG 21 25 GLU 22 26 ALA 23 27 GLU 24 28 HIS stop_ _Sequence_homology_query_date 2008-08-19 _Sequence_homology_query_revised_last_date 2008-08-19 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 SWISS-PROT Q05195 'MAD protein (MAX dimerizer) (MAX dimerization protein 1)' 100.00 221 100.00 100.00 5.63e-05 REF XP_592508 'PREDICTED: similar to MAX dimerization protein 1 isoform 2 [Bos taurus]' 100.00 222 100.00 100.00 5.40e-05 REF XP_525776 'PREDICTED: MAX dimerization protein 1 isoform 2 [Pan troglodytes]' 100.00 221 100.00 100.00 5.63e-05 REF XP_001493078 'PREDICTED: similar to MAX dimerization protein 1 [Equus caballus]' 100.00 221 100.00 100.00 5.87e-05 REF XP_001098088 'PREDICTED: similar to MAX dimerization protein 1 [Macaca mulatta]' 100.00 221 100.00 100.00 5.77e-05 REF NP_002348 'MAX dimerization protein 1 [Homo sapiens]' 100.00 221 100.00 100.00 5.63e-05 GenBank AAI13532 'MAX dimerization protein 1 [Homo sapiens]' 100.00 221 100.00 100.00 5.63e-05 GenBank AAH98396 'MAX dimerization protein 1 [Homo sapiens]' 100.00 221 100.00 100.00 5.63e-05 GenBank AAH69433 'MAX dimerization protein 1 [Homo sapiens]' 100.00 221 100.00 100.00 5.63e-05 GenBank AAH69377 'MAX dimerization protein 1 [Homo sapiens]' 100.00 221 100.00 100.00 5.63e-05 GenBank AAA36194 'antagonizer of myc transcriptional activity' 100.00 221 100.00 100.00 5.63e-05 EMBL CAG46493 'MAD [Homo sapiens]' 100.00 221 100.00 100.00 5.63e-05 EMBL CAG38734 'MAD [Homo sapiens]' 100.00 221 100.00 100.00 5.63e-05 DBJ BAG35605 'unnamed protein product [Homo sapiens]' 100.00 221 100.00 100.00 5.63e-05 PDB 1PD7 'Extended Sid Of Mad1 Bound To The Pah2 Domain Of Msin3b' 100.00 24 100.00 100.00 2.57e-04 BMRB 5457 Mad1 100.00 24 100.00 100.00 2.57e-04 BMRB 4635 'MAD1 SID domain' 66.67 16 100.00 100.00 5.40e+00 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $PAH2 'house mouse' 10090 Eukaryota Metazoa Mus musculus $SID24 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 $PAH2 'recombinant technology' . . . . . $SID24 'solid phase synthesis' . . . . . stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Saveframe_category sample _Sample_type solution _Details 'The sample also contained trace amounts of sodium azide and Pefabloc.' loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $SID24 1.3 mM . $PAH2 1.3 mM '[U-13C; U-15N]' 'K2HPO4/KH2PO4 buffer' 50 mM . stop_ save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model UnityInova _Field_strength 500 _Details . save_ save_NMR_spectrometer_2 _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model UnityInova _Field_strength 600 _Details . save_ save_NMR_spectrometer_3 _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model UnityInova _Field_strength 750 _Details . save_ save_NMR_spectrometer_4 _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model UnityInova _Field_strength 800 _Details . save_ ############################# # NMR applied experiments # ############################# save_HNCA_1 _Saveframe_category NMR_applied_experiment _Experiment_name HNCA _Sample_label $sample_1 save_ save_HNCACB_2 _Saveframe_category NMR_applied_experiment _Experiment_name HNCACB _Sample_label $sample_1 save_ save_CBCACONH_3 _Saveframe_category NMR_applied_experiment _Experiment_name CBCACONH _Sample_label $sample_1 save_ save_(H)CCH-TOCSY_4 _Saveframe_category NMR_applied_experiment _Experiment_name (H)CCH-TOCSY _Sample_label $sample_1 save_ save_15N_NOESY_5 _Saveframe_category NMR_applied_experiment _Experiment_name '15N NOESY' _Sample_label $sample_1 save_ save_13C_NOESY_6 _Saveframe_category NMR_applied_experiment _Experiment_name '13C NOESY' _Sample_label $sample_1 save_ save_NMR_spec_expt__0_1 _Saveframe_category NMR_applied_experiment _Experiment_name HNCA _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_2 _Saveframe_category NMR_applied_experiment _Experiment_name HNCACB _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_3 _Saveframe_category NMR_applied_experiment _Experiment_name CBCACONH _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_4 _Saveframe_category NMR_applied_experiment _Experiment_name (H)CCH-TOCSY _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_5 _Saveframe_category NMR_applied_experiment _Experiment_name '15N NOESY' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_6 _Saveframe_category NMR_applied_experiment _Experiment_name '13C NOESY' _BMRB_pulse_sequence_accession_number . _Details . save_ ####################### # Sample conditions # ####################### save_Ex-cond_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 6.3 . n/a temperature 293 . K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference _Saveframe_category chemical_shift_reference _Details . loop_ _Mol_common_name _Atom_type _Atom_isotope_number _Atom_group _Chem_shift_units _Chem_shift_value _Reference_method _Reference_type _External_reference_sample_geometry _External_reference_location _External_reference_axis _Indirect_shift_ratio_citation_label _Correction_value_citation_label DSS H 1 'methyl protons' ppm . . . . . . $entry_citation $entry_citation DSS C 13 'methyl protons' ppm . . . . . . $entry_citation $entry_citation DSS N 15 'methyl protons' ppm . . . . . . $entry_citation $entry_citation stop_ save_ ################################### # Assigned chemical shift lists # ################################### ################################################################### # Chemical Shift Ambiguity Index Value Definitions # # # # The values other than 1 are used for those atoms with different # # chemical shifts that cannot be assigned to stereospecific atoms # # or to specific residues or chains. # # # # Index Value Definition # # # # 1 Unique (including isolated methyl protons, # # geminal atoms, and geminal methyl # # groups with identical chemical shifts) # # (e.g. ILE HD11, HD12, HD13 protons) # # 2 Ambiguity of geminal atoms or geminal methyl # # proton groups (e.g. ASP HB2 and HB3 # # protons, LEU CD1 and CD2 carbons, or # # LEU HD11, HD12, HD13 and HD21, HD22, # # HD23 methyl protons) # # 3 Aromatic atoms on opposite sides of # # symmetrical rings (e.g. TYR HE1 and HE2 # # protons) # # 4 Intraresidue ambiguities (e.g. LYS HG and # # HD protons or TRP HZ2 and HZ3 protons) # # 5 Interresidue ambiguities (LYS 12 vs. LYS 27) # # 6 Intermolecular ambiguities (e.g. ASP 31 CA # # in monomer 1 and ASP 31 CA in monomer 2 # # of an asymmetrical homodimer, duplex # # DNA assignments, or other assignments # # that may apply to atoms in one or more # # molecule in the molecular assembly) # # 9 Ambiguous, specific ambiguity not defined # # # ################################################################### save_shift_set_1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $Ex-cond_1 _Chem_shift_reference_set_label $chemical_shift_reference _Mol_system_component_name 'PAH2 domain of mSin3B' _Text_data_format . _Text_data . loop_ _Atom_shift_assign_ID _Residue_author_seq_code _Residue_seq_code _Residue_label _Atom_name _Atom_type _Chem_shift_value _Chem_shift_value_error _Chem_shift_ambiguity_code 1 . 1 GLU N N 123.132 0.02 1 2 . 1 GLU H H 8.900 0.003 1 3 . 1 GLU CA C 57.659 0.02 1 4 . 1 GLU HA H 4.199 0.002 1 5 . 1 GLU HB2 H 1.908 0.007 1 6 . 1 GLU HB3 H 2.019 0.002 1 7 . 1 GLU CG C 36.331 0.02 1 8 . 1 GLU HG2 H 2.233 0.003 1 9 . 2 SER N N 115.424 0.02 1 10 . 2 SER H H 8.166 0.006 1 11 . 2 SER CA C 58.821 0.02 1 12 . 2 SER HA H 4.206 0.004 1 13 . 2 SER CB C 63.449 0.02 1 14 . 2 SER HB2 H 3.674 0.005 1 15 . 2 SER HB3 H 3.791 0.002 1 16 . 2 SER HG H 4.789 0.002 1 17 . 3 ASP N N 121.939 0.02 1 18 . 3 ASP H H 8.108 0.006 1 19 . 3 ASP CA C 54.472 0.02 1 20 . 3 ASP HA H 4.664 0.003 1 21 . 3 ASP CB C 41.035 0.02 1 22 . 3 ASP HB2 H 2.680 0.003 1 23 . 4 SER N N 115.481 0.02 1 24 . 4 SER H H 8.028 0.002 1 25 . 4 SER CA C 58.132 0.02 1 26 . 4 SER HA H 4.535 0.002 1 27 . 4 SER CB C 64.304 0.02 1 28 . 4 SER HB2 H 4.020 0.003 1 29 . 4 SER HB3 H 4.162 0.004 1 30 . 5 VAL N N 125.145 0.02 1 31 . 5 VAL H H 8.610 0.002 1 32 . 5 VAL CA C 65.669 0.02 1 33 . 5 VAL HA H 3.798 0.005 1 34 . 5 VAL CB C 31.909 0.02 1 35 . 5 VAL HB H 2.042 0.002 1 36 . 5 VAL HG1 H 0.926 0.003 1 37 . 5 VAL HG2 H 1.039 0.003 1 38 . 5 VAL CG1 C 20.883 0.027 1 39 . 5 VAL CG2 C 22.015 0.02 1 40 . 6 GLU N N 120.288 0.02 1 41 . 6 GLU H H 9.015 0.006 1 42 . 6 GLU CA C 60.768 0.017 1 43 . 6 GLU HA H 4.023 0.003 1 44 . 6 GLU CB C 28.885 0.02 1 45 . 6 GLU HB2 H 1.852 0.005 1 46 . 6 GLU CG C 36.882 0.02 1 47 . 6 GLU HG2 H 2.289 0.006 1 48 . 6 GLU HG3 H 2.289 0.003 1 49 . 7 PHE N N 120.563 0.02 1 50 . 7 PHE H H 8.342 0.003 1 51 . 7 PHE CA C 60.969 0.035 1 52 . 7 PHE HA H 4.521 0.004 1 53 . 7 PHE CB C 39.130 0.02 1 54 . 7 PHE HB2 H 3.004 0.005 1 55 . 7 PHE HB3 H 3.188 0.003 1 56 . 7 PHE HD1 H 7.179 0.003 1 57 . 7 PHE HE1 H 7.179 0.003 1 58 . 7 PHE CD1 C 131.836 0.02 1 59 . 8 ASN N N 117.075 0.02 1 60 . 8 ASN H H 8.225 0.004 1 61 . 8 ASN CA C 56.551 0.02 1 62 . 8 ASN HA H 4.313 0.004 1 63 . 8 ASN CB C 38.120 0.02 1 64 . 8 ASN HB2 H 2.755 0.005 1 65 . 8 ASN HB3 H 2.937 0.004 1 66 . 8 ASN ND2 N 112.855 0.02 1 67 . 8 ASN HD21 H 7.006 0.002 1 68 . 8 ASN HD22 H 7.503 0.002 1 69 . 9 ASN N N 120.838 0.02 1 70 . 9 ASN H H 8.463 0.004 1 71 . 9 ASN CA C 55.807 0.02 1 72 . 9 ASN HA H 4.558 0.003 1 73 . 9 ASN CB C 37.735 0.02 1 74 . 9 ASN HB2 H 2.899 0.005 1 75 . 9 ASN HB3 H 3.166 0.003 1 76 . 9 ASN ND2 N 111.725 0.02 1 77 . 9 ASN HD21 H 6.967 0.006 1 78 . 9 ASN HD22 H 7.355 0.003 1 79 . 10 ALA N N 125.701 0.02 1 80 . 10 ALA H H 8.293 0.001 1 81 . 10 ALA CA C 55.878 0.052 1 82 . 10 ALA HA H 4.242 0.004 1 83 . 10 ALA HB H 1.503 0.004 1 84 . 10 ALA CB C 18.552 0.061 1 85 . 11 ILE N N 118.430 0.02 1 86 . 11 ILE H H 8.341 0.006 1 87 . 11 ILE CA C 65.692 0.006 1 88 . 11 ILE HA H 3.406 0.002 1 89 . 11 ILE CB C 38.120 0.02 1 90 . 11 ILE HB H 1.759 0.003 1 91 . 11 ILE HG2 H 0.863 0.005 1 92 . 11 ILE CG2 C 17.680 0.004 1 93 . 11 ILE CG1 C 28.813 0.035 1 94 . 11 ILE HG12 H 0.511 0.003 1 95 . 11 ILE HG13 H 1.133 0.004 1 96 . 11 ILE HD1 H 0.313 0.003 1 97 . 11 ILE CD1 C 13.953 0.014 1 98 . 12 SER N N 113.837 0.02 1 99 . 12 SER H H 8.061 0.005 1 100 . 12 SER CA C 61.695 0.02 1 101 . 12 SER HA H 4.166 0.004 1 102 . 13 TYR N N 122.654 0.02 1 103 . 13 TYR H H 8.080 0.005 1 104 . 13 TYR CA C 60.954 0.02 1 105 . 13 TYR HA H 4.445 0.003 1 106 . 13 TYR CB C 38.409 0.02 1 107 . 13 TYR HB2 H 2.918 0.008 1 108 . 13 TYR HB3 H 3.441 0.004 1 109 . 13 TYR HD1 H 6.958 0.005 1 110 . 13 TYR HE1 H 6.742 0.003 1 111 . 13 TYR CD1 C 133.083 0.02 1 112 . 13 TYR CE1 C 117.697 0.02 1 113 . 14 VAL N N 118.046 0.02 1 114 . 14 VAL H H 8.530 0.003 1 115 . 14 VAL CA C 67.463 0.02 1 116 . 14 VAL HA H 3.388 0.006 1 117 . 14 VAL CB C 31.145 0.038 1 118 . 14 VAL HB H 2.088 0.003 1 119 . 14 VAL HG1 H 1.157 0.003 1 120 . 14 VAL HG2 H 1.211 0.008 1 121 . 14 VAL CG1 C 23.957 0.02 1 122 . 14 VAL CG2 C 24.329 0.02 1 123 . 15 ASN N N 117.050 0.02 1 124 . 15 ASN H H 8.603 0.003 1 125 . 15 ASN CA C 56.279 0.02 1 126 . 15 ASN HA H 4.338 0.003 1 127 . 15 ASN CB C 39.086 0.02 1 128 . 15 ASN HB2 H 2.756 0.003 1 129 . 15 ASN ND2 N 112.579 0.02 1 130 . 15 ASN HD21 H 6.730 0.003 1 131 . 15 ASN HD22 H 7.490 0.002 1 132 . 16 LYS N N 123.601 0.02 1 133 . 16 LYS H H 7.983 0.006 1 134 . 16 LYS CA C 60.275 0.02 1 135 . 16 LYS HA H 3.838 0.003 1 136 . 16 LYS CB C 32.183 0.02 1 137 . 16 LYS HB2 H 1.952 0.003 1 138 . 16 LYS CG C 25.297 0.02 1 139 . 16 LYS HG2 H 1.108 0.005 1 140 . 16 LYS HG3 H 1.508 0.004 1 141 . 16 LYS CD C 30.365 0.02 1 142 . 16 LYS HD2 H 1.639 0.003 1 143 . 16 LYS CE C 41.633 0.02 1 144 . 16 LYS HE2 H 2.788 0.003 1 145 . 16 LYS HE3 H 2.861 0.003 1 146 . 17 ILE N N 120.163 0.02 1 147 . 17 ILE H H 7.640 0.004 1 148 . 17 ILE CA C 65.165 0.02 1 149 . 17 ILE HA H 3.104 0.003 1 150 . 17 ILE CB C 38.321 0.02 1 151 . 17 ILE HB H 1.798 0.005 1 152 . 17 ILE HG2 H 0.750 0.003 1 153 . 17 ILE CG2 C 18.421 0.02 1 154 . 17 ILE CG1 C 28.430 0.02 1 155 . 17 ILE HG12 H 0.309 0.003 1 156 . 17 ILE HG13 H 1.058 0.005 1 157 . 17 ILE HD1 H 0.030 0.005 1 158 . 17 ILE CD1 C 14.278 0.023 1 159 . 18 LYS N N 119.278 0.02 1 160 . 18 LYS H H 8.334 0.003 1 161 . 18 LYS CA C 59.885 0.02 1 162 . 18 LYS HA H 3.121 0.003 1 163 . 18 LYS CB C 32.604 0.009 1 164 . 18 LYS HB2 H 1.211 0.003 1 165 . 18 LYS HB3 H 1.568 0.002 1 166 . 18 LYS CG C 24.832 0.02 1 167 . 18 LYS HG2 H 0.502 0.002 1 168 . 18 LYS HG3 H 0.713 0.003 1 169 . 18 LYS CD C 29.533 0.022 1 170 . 18 LYS HD2 H 1.314 0.001 1 171 . 18 LYS HD3 H 1.410 0.002 1 172 . 18 LYS CE C 42.077 0.035 1 173 . 18 LYS HE2 H 2.762 0.003 1 174 . 19 THR N N 111.471 0.02 1 175 . 19 THR H H 8.100 0.008 1 176 . 19 THR CA C 65.689 0.02 1 177 . 19 THR HA H 3.732 0.004 1 178 . 19 THR CB C 68.828 0.02 1 179 . 19 THR HB H 4.052 0.003 1 180 . 19 THR HG2 H 1.131 0.006 1 181 . 19 THR CG2 C 21.250 0.02 1 182 . 20 ARG N N 124.572 0.02 1 183 . 20 ARG H H 7.947 0.005 1 184 . 20 ARG CA C 56.055 0.02 1 185 . 20 ARG HA H 3.773 0.005 1 186 . 20 ARG CB C 27.378 0.02 1 187 . 20 ARG HB2 H 1.085 0.003 1 188 . 20 ARG HB3 H 1.584 0.003 1 189 . 20 ARG CG C 24.350 0.02 1 190 . 20 ARG HG2 H 0.448 0.004 1 191 . 20 ARG HG3 H 0.867 0.005 1 192 . 20 ARG CD C 39.800 0.02 1 193 . 20 ARG HD2 H 2.988 0.011 1 194 . 21 PHE N N 113.130 0.02 1 195 . 21 PHE H H 7.162 0.002 1 196 . 21 PHE HA H 4.980 0.007 1 197 . 21 PHE CB C 38.159 0.02 1 198 . 21 PHE HB2 H 2.422 0.006 1 199 . 21 PHE HB3 H 3.900 0.005 1 200 . 21 PHE HD1 H 7.243 0.011 1 201 . 21 PHE HE1 H 6.823 0.003 1 202 . 21 PHE CD1 C 132.303 0.02 1 203 . 21 PHE CE1 C 131.016 0.02 1 204 . 21 PHE CZ C 129.541 0.02 1 205 . 21 PHE HZ H 7.125 0.002 1 206 . 22 LEU N N 126.344 0.02 1 207 . 22 LEU H H 7.212 0.002 1 208 . 22 LEU CA C 59.008 0.02 1 209 . 22 LEU HA H 3.990 0.004 1 210 . 22 LEU CB C 42.266 0.02 1 211 . 22 LEU HB2 H 1.561 0.003 1 212 . 22 LEU HB3 H 1.787 0.004 1 213 . 22 LEU CG C 26.533 0.02 1 214 . 22 LEU HG H 1.877 0.004 1 215 . 22 LEU HD1 H 0.892 0.003 1 216 . 22 LEU HD2 H 0.843 0.003 1 217 . 22 LEU CD1 C 24.568 0.02 1 218 . 22 LEU CD2 C 24.237 0.02 1 219 . 23 ASP N N 113.038 0.02 1 220 . 23 ASP H H 8.642 0.006 1 221 . 23 ASP CA C 54.151 0.02 1 222 . 23 ASP HA H 4.518 0.005 1 223 . 23 ASP CB C 40.135 0.02 1 224 . 23 ASP HB2 H 2.513 0.002 1 225 . 23 ASP HB3 H 2.548 0.002 1 226 . 24 HIS N N 117.175 0.02 1 227 . 24 HIS H H 7.703 0.004 1 228 . 24 HIS CA C 54.092 0.02 1 229 . 24 HIS HA H 5.173 0.003 1 230 . 24 HIS CB C 30.292 0.02 1 231 . 24 HIS HB2 H 2.959 0.006 1 232 . 24 HIS HB3 H 3.407 0.004 1 233 . 24 HIS CD2 C 120.166 0.02 1 234 . 24 HIS CE1 C 136.59 0.02 1 235 . 24 HIS HD2 H 7.350 0.002 1 236 . 24 HIS HE1 H 8.542 0.001 1 237 . 25 PRO CD C 50.414 0.02 1 238 . 25 PRO CA C 65.218 0.02 1 239 . 25 PRO HA H 4.427 0.004 1 240 . 25 PRO CB C 31.564 0.02 1 241 . 25 PRO HB2 H 2.162 0.002 1 242 . 25 PRO HB3 H 2.418 0.003 1 243 . 25 PRO CG C 27.637 0.02 1 244 . 25 PRO HG2 H 2.073 0.002 1 245 . 25 PRO HG3 H 2.147 0.002 1 246 . 25 PRO HD2 H 3.493 0.006 1 247 . 25 PRO HD3 H 3.702 0.004 1 248 . 26 GLU N N 121.633 0.02 1 249 . 26 GLU H H 10.308 0.001 1 250 . 26 GLU CA C 59.291 0.02 1 251 . 26 GLU HA H 4.195 0.004 1 252 . 26 GLU CB C 27.285 0.02 1 253 . 26 GLU HB2 H 2.024 0.006 1 254 . 26 GLU HB3 H 2.155 0.004 1 255 . 26 GLU CG C 35.353 0.02 1 256 . 26 GLU HG2 H 2.306 0.004 1 257 . 26 GLU HG3 H 2.529 0.006 1 258 . 27 ILE N N 123.675 0.02 1 259 . 27 ILE H H 8.209 0.005 1 260 . 27 ILE CA C 64.540 0.02 1 261 . 27 ILE HA H 3.646 0.003 1 262 . 27 ILE CB C 36.801 0.02 1 263 . 27 ILE HB H 1.508 0.004 1 264 . 27 ILE HG2 H -0.063 0.001 1 265 . 27 ILE CG2 C 15.457 0.02 1 266 . 27 ILE CG1 C 28.727 0.02 1 267 . 27 ILE HG12 H 1.124 0.004 1 268 . 27 ILE HG13 H 1.520 0.002 1 269 . 27 ILE HD1 H 0.714 0.006 1 270 . 27 ILE CD1 C 11.764 0.02 1 271 . 28 TYR N N 119.737 0.02 1 272 . 28 TYR H H 6.767 0.003 1 273 . 28 TYR CA C 61.181 0.02 1 274 . 28 TYR HA H 4.161 0.003 1 275 . 28 TYR CB C 39.017 0.02 1 276 . 28 TYR HB2 H 3.110 0.005 1 277 . 28 TYR HB3 H 3.216 0.004 1 278 . 28 TYR HD1 H 7.018 0.004 1 279 . 28 TYR HE1 H 6.720 0.005 1 280 . 28 TYR CD1 C 132.453 0.02 1 281 . 28 TYR CE1 C 118.008 0.02 1 282 . 29 ARG N N 116.129 0.02 1 283 . 29 ARG H H 8.171 0.005 1 284 . 29 ARG CA C 59.524 0.02 1 285 . 29 ARG HA H 3.747 0.003 1 286 . 29 ARG CB C 29.770 0.02 1 287 . 29 ARG HB2 H 1.867 0.002 1 288 . 29 ARG HB3 H 1.928 0.002 1 289 . 29 ARG CG C 27.404 0.02 1 290 . 29 ARG HG2 H 1.628 0.003 1 291 . 29 ARG HG3 H 1.856 0.002 1 292 . 29 ARG CD C 43.126 0.02 1 293 . 29 ARG HD2 H 3.152 0.002 1 294 . 29 ARG HD3 H 3.249 0.002 1 295 . 30 SER N N 116.988 0.02 1 296 . 30 SER H H 8.264 0.004 1 297 . 30 SER CA C 62.731 0.02 1 298 . 30 SER HA H 4.144 0.009 1 299 . 30 SER CB C 63.006 0.02 1 300 . 30 SER HB2 H 3.857 0.006 1 301 . 31 PHE N N 123.825 0.02 1 302 . 31 PHE H H 8.110 0.007 1 303 . 31 PHE CA C 60.902 0.02 1 304 . 31 PHE HA H 3.850 0.005 1 305 . 31 PHE CB C 38.278 0.001 1 306 . 31 PHE HB2 H 2.986 0.003 1 307 . 31 PHE HB3 H 3.451 0.007 1 308 . 31 PHE HD1 H 6.782 0.005 1 309 . 31 PHE HE1 H 6.782 0.005 1 310 . 31 PHE CD1 C 132.139 0.02 1 311 . 32 LEU N N 116.527 0.02 1 312 . 32 LEU H H 7.608 0.004 1 313 . 32 LEU CA C 57.482 0.023 1 314 . 32 LEU HA H 3.419 0.005 1 315 . 32 LEU CB C 40.958 0.02 1 316 . 32 LEU HB2 H 1.107 0.007 1 317 . 32 LEU HB3 H 1.737 0.003 1 318 . 32 LEU CG C 26.225 0.02 1 319 . 32 LEU HG H 1.344 0.003 1 320 . 32 LEU HD1 H 0.611 0.002 1 321 . 32 LEU HD2 H 0.560 0.002 1 322 . 32 LEU CD1 C 25.566 0.013 1 323 . 32 LEU CD2 C 21.615 0.02 1 324 . 33 GLU N N 119.591 0.02 1 325 . 33 GLU H H 8.038 0.002 1 326 . 33 GLU CA C 59.646 0.02 1 327 . 33 GLU HA H 4.068 0.002 1 328 . 33 GLU HB2 H 2.104 0.002 1 329 . 33 GLU HG2 H 2.274 0.002 1 330 . 34 ILE N N 122.447 0.02 1 331 . 34 ILE H H 8.011 0.003 1 332 . 34 ILE CA C 65.057 0.02 1 333 . 34 ILE HA H 3.689 0.003 1 334 . 34 ILE CB C 38.120 0.02 1 335 . 34 ILE HB H 1.762 0.006 1 336 . 34 ILE HG2 H 0.736 0.007 1 337 . 34 ILE CG2 C 17.827 0.02 1 338 . 34 ILE CG1 C 28.814 0.02 1 339 . 34 ILE HG12 H 1.024 0.004 1 340 . 34 ILE HG13 H 1.716 0.002 1 341 . 34 ILE HD1 H 0.681 0.001 1 342 . 34 ILE CD1 C 14.827 0.02 1 343 . 35 LEU N N 117.698 0.02 1 344 . 35 LEU H H 7.306 0.003 1 345 . 35 LEU CA C 58.085 0.001 1 346 . 35 LEU HA H 3.830 0.004 1 347 . 35 LEU CB C 40.120 0.047 1 348 . 35 LEU HB2 H 1.113 0.007 1 349 . 35 LEU HB3 H 1.683 0.006 1 350 . 35 LEU CG C 25.932 0.009 1 351 . 35 LEU HG H 1.349 0.008 1 352 . 35 LEU HD1 H 0.350 0.006 1 353 . 35 LEU HD2 H 0.513 0.005 1 354 . 35 LEU CD1 C 25.698 0.070 1 355 . 35 LEU CD2 C 21.393 0.067 1 356 . 36 HIS N N 117.224 0.02 1 357 . 36 HIS H H 8.754 0.004 1 358 . 36 HIS CA C 59.952 0.02 1 359 . 36 HIS HA H 4.208 0.006 1 360 . 36 HIS CB C 29.244 0.02 1 361 . 36 HIS HB2 H 3.150 0.004 1 362 . 36 HIS HB3 H 3.271 0.004 1 363 . 36 HIS CD2 C 120.493 0.02 1 364 . 36 HIS CE1 C 137.14 0.02 1 365 . 36 HIS HD2 H 7.064 0.005 1 366 . 36 HIS HE1 H 8.314 0.002 1 367 . 37 THR N N 119.094 0.02 1 368 . 37 THR H H 8.528 0.006 1 369 . 37 THR CA C 67.171 0.02 1 370 . 37 THR HA H 3.829 0.003 1 371 . 37 THR CB C 68.353 0.02 1 372 . 37 THR HB H 4.416 0.003 1 373 . 37 THR HG2 H 1.241 0.004 1 374 . 37 THR CG2 C 21.891 0.02 1 375 . 38 TYR N N 122.081 0.02 1 376 . 38 TYR H H 8.164 0.005 1 377 . 38 TYR CA C 61.841 0.02 1 378 . 38 TYR HA H 4.097 0.008 1 379 . 38 TYR CB C 38.230 0.02 1 380 . 38 TYR HB2 H 3.104 0.003 1 381 . 38 TYR HB3 H 3.182 0.004 1 382 . 38 TYR HD1 H 6.935 0.015 1 383 . 38 TYR HE1 H 6.711 0.003 1 384 . 38 TYR CD1 C 133.419 0.02 1 385 . 38 TYR CE1 C 118.420 0.02 1 386 . 39 GLN N N 118.544 0.02 1 387 . 39 GLN H H 8.352 0.005 1 388 . 39 GLN CA C 58.281 0.02 1 389 . 39 GLN HA H 3.840 0.004 1 390 . 39 GLN CB C 29.494 0.02 1 391 . 39 GLN HB2 H 2.085 0.002 1 392 . 39 GLN HB3 H 2.131 0.002 1 393 . 39 GLN CG C 33.906 0.031 1 394 . 39 GLN HG2 H 2.320 0.004 1 395 . 39 GLN HG3 H 2.376 0.001 1 396 . 39 GLN NE2 N 109.693 0.02 1 397 . 39 GLN HE21 H 6.794 0.002 1 398 . 39 GLN HE22 H 7.345 0.007 1 399 . 40 LYS N N 119.737 0.02 1 400 . 40 LYS H H 8.152 0.005 1 401 . 40 LYS CA C 59.152 0.02 1 402 . 40 LYS HA H 4.051 0.003 1 403 . 40 LYS CB C 32.378 0.02 1 404 . 40 LYS HB2 H 1.905 0.006 1 405 . 40 LYS HG2 H 1.483 0.002 1 406 . 40 LYS CD C 29.373 0.02 1 407 . 40 LYS HD2 H 1.630 0.003 1 408 . 40 LYS CE C 42.079 0.02 1 409 . 40 LYS HE2 H 2.904 0.003 1 410 . 41 GLU N N 117.626 0.02 1 411 . 41 GLU H H 7.827 0.001 1 412 . 41 GLU CA C 57.555 0.02 1 413 . 41 GLU HA H 4.195 0.004 1 414 . 41 GLU HB2 H 2.045 0.002 1 415 . 41 GLU HG2 H 2.309 0.002 1 416 . 42 GLN N N 116.984 0.02 1 417 . 42 GLN H H 7.621 0.003 1 418 . 42 GLN CA C 56.143 0.02 1 419 . 42 GLN HA H 4.062 0.004 1 420 . 42 GLN CB C 28.735 0.02 1 421 . 42 GLN HB2 H 1.877 0.004 1 422 . 42 GLN HB3 H 2.057 0.005 1 423 . 42 GLN CG C 33.249 0.02 1 424 . 42 GLN HG2 H 2.146 0.003 1 425 . 42 GLN NE2 N 115.149 0.02 1 426 . 42 GLN HE21 H 6.769 0.007 1 427 . 42 GLN HE22 H 6.992 0.001 1 428 . 43 LEU N N 119.553 0.02 1 429 . 43 LEU H H 7.488 0.001 1 430 . 43 LEU CA C 55.432 0.02 1 431 . 43 LEU HA H 4.236 0.004 1 432 . 43 LEU CB C 42.232 0.02 1 433 . 43 LEU HB2 H 1.454 0.002 1 434 . 43 LEU HB3 H 1.646 0.001 1 435 . 43 LEU CG C 26.722 0.02 1 436 . 43 LEU HG H 1.598 0.002 1 437 . 43 LEU HD1 H 0.874 0.002 1 438 . 43 LEU HD2 H 0.811 0.003 1 439 . 43 LEU CD1 C 25.138 0.02 1 440 . 43 LEU CD2 C 23.243 0.02 1 441 . 44 HIS N N 119.370 0.02 1 442 . 44 HIS H H 8.007 0.002 1 443 . 44 HIS CA C 55.661 0.02 1 444 . 44 HIS HA H 4.660 0.006 1 445 . 44 HIS HB2 H 3.054 0.002 1 446 . 44 HIS HB3 H 3.148 0.002 1 447 . 44 HIS CD2 C 120.028 0.02 1 448 . 44 HIS CE1 C 137.16 0.02 1 449 . 44 HIS HD2 H 7.052 0.002 1 450 . 44 HIS HE1 H 8.035 0.002 1 451 . 45 THR N N 114.687 0.02 1 452 . 45 THR H H 8.017 0.002 1 453 . 45 THR CA C 61.985 0.02 1 454 . 45 THR HA H 4.270 0.010 1 455 . 45 THR CB C 69.943 0.02 1 456 . 45 THR HB H 4.128 0.003 1 457 . 45 THR HG2 H 1.138 0.002 1 458 . 45 THR CG2 C 21.810 0.02 1 459 . 46 LYS N N 124.325 0.02 1 460 . 46 LYS H H 8.382 0.002 1 461 . 46 LYS CA C 57.408 0.02 1 462 . 46 LYS HA H 4.164 0.003 1 463 . 46 LYS CB C 32.461 0.02 1 464 . 46 LYS HB2 H 1.799 0.002 1 465 . 46 LYS CG C 24.751 0.02 1 466 . 46 LYS HG2 H 1.393 0.003 1 467 . 46 LYS CD C 29.146 0.02 1 468 . 46 LYS HD2 H 1.643 0.002 1 469 . 46 LYS CE C 42.481 0.02 1 470 . 46 LYS HE2 H 2.914 0.003 1 471 . 47 GLY N N 110.928 0.02 1 472 . 47 GLY H H 8.680 0.002 1 473 . 47 GLY CA C 45.449 0.02 1 474 . 47 GLY HA2 H 3.784 0.003 1 475 . 47 GLY HA3 H 4.049 0.002 1 476 . 48 ARG N N 120.761 0.02 1 477 . 48 ARG H H 7.847 0.005 1 478 . 48 ARG CA C 53.350 0.02 1 479 . 48 ARG HA H 4.676 0.001 1 480 . 48 ARG CB C 30.667 0.02 1 481 . 48 ARG HB2 H 1.673 0.001 1 482 . 48 ARG HB3 H 1.798 0.001 1 483 . 48 ARG CG C 26.722 0.02 1 484 . 48 ARG HG2 H 1.536 0.002 1 485 . 48 ARG HG3 H 1.581 0.003 1 486 . 48 ARG CD C 43.649 0.02 1 487 . 48 ARG HD2 H 3.130 0.004 1 488 . 49 PRO CD C 50.499 0.02 1 489 . 49 PRO CA C 63.263 0.02 1 490 . 49 PRO HA H 4.384 0.003 1 491 . 49 PRO CB C 31.662 0.02 1 492 . 49 PRO HB2 H 1.761 0.003 1 493 . 49 PRO HB3 H 2.160 0.003 1 494 . 49 PRO CG C 27.350 0.02 1 495 . 49 PRO HG2 H 1.936 0.003 1 496 . 49 PRO HD2 H 3.570 0.005 1 497 . 49 PRO HD3 H 3.736 0.003 1 498 . 50 PHE N N 120.563 0.02 1 499 . 50 PHE H H 8.178 0.003 1 500 . 50 PHE CA C 57.437 0.02 1 501 . 50 PHE HA H 4.588 0.003 1 502 . 50 PHE CB C 40.121 0.02 1 503 . 50 PHE HB2 H 3.006 0.004 1 504 . 50 PHE HD1 H 7.028 0.002 1 505 . 50 PHE HE1 H 7.230 0.002 1 506 . 50 PHE HD2 H 7.131 0.006 1 507 . 50 PHE HE2 H 7.131 0.006 1 508 . 50 PHE CD1 C 131.759 0.02 1 509 . 51 ARG N N 124.233 0.02 1 510 . 51 ARG H H 8.317 0.002 1 511 . 51 ARG CA C 55.861 0.02 1 512 . 51 ARG HA H 4.279 0.004 1 513 . 51 ARG CB C 31.219 0.02 1 514 . 51 ARG HB2 H 1.639 0.002 1 515 . 51 ARG HB3 H 1.780 0.004 1 516 . 51 ARG CG C 26.839 0.02 1 517 . 51 ARG HG2 H 1.529 0.004 1 518 . 51 ARG CD C 43.335 0.02 1 519 . 51 ARG HD2 H 3.090 0.003 1 520 . 52 GLY N N 109.722 0.02 1 521 . 52 GLY H H 7.714 0.005 1 522 . 52 GLY CA C 44.931 0.02 1 523 . 52 GLY HA2 H 3.748 0.003 1 524 . 52 GLY HA3 H 3.955 0.003 1 525 . 53 MET N N 121.085 0.02 1 526 . 53 MET H H 8.396 0.006 1 527 . 53 MET CA C 56.536 0.02 1 528 . 53 MET HA H 4.470 0.002 1 529 . 53 MET CB C 35.025 0.02 1 530 . 53 MET HB2 H 1.916 0.003 1 531 . 53 MET HB3 H 2.015 0.004 1 532 . 53 MET CG C 32.284 0.02 1 533 . 53 MET HG2 H 2.630 0.002 1 534 . 53 MET HG3 H 2.700 0.003 1 535 . 53 MET HE H 2.043 0.005 1 536 . 53 MET CE C 17.278 0.02 1 537 . 54 SER N N 120.930 0.02 1 538 . 54 SER H H 8.950 0.001 1 539 . 54 SER HA H 4.790 0.006 1 540 . 54 SER CB C 65.931 0.02 1 541 . 54 SER HB2 H 4.073 0.007 1 542 . 54 SER HB3 H 4.473 0.002 1 543 . 55 GLU N N 120.689 0.02 1 544 . 55 GLU H H 9.088 0.001 1 545 . 55 GLU CA C 60.831 0.02 1 546 . 55 GLU HA H 3.819 0.002 1 547 . 55 GLU CB C 29.425 0.02 1 548 . 55 GLU HB2 H 1.957 0.006 1 549 . 55 GLU HB3 H 2.101 0.002 1 550 . 55 GLU CG C 38.048 0.02 1 551 . 55 GLU HG2 H 2.303 0.007 1 552 . 55 GLU HG3 H 2.428 0.004 1 553 . 56 GLU N N 118.819 0.02 1 554 . 56 GLU H H 8.717 0.002 1 555 . 56 GLU CA C 60.192 0.02 1 556 . 56 GLU HA H 4.034 0.003 1 557 . 56 GLU HB2 H 2.065 0.002 1 558 . 56 GLU CG C 36.882 0.02 1 559 . 56 GLU HG2 H 2.347 0.007 1 560 . 57 GLU N N 121.010 0.02 1 561 . 57 GLU H H 7.905 0.004 1 562 . 57 GLU HA H 4.054 0.002 1 563 . 57 GLU HB2 H 2.073 0.002 1 564 . 57 GLU CG C 37.410 0.02 1 565 . 57 GLU HG2 H 2.359 0.003 1 566 . 58 VAL N N 120.163 0.02 1 567 . 58 VAL H H 8.034 0.003 1 568 . 58 VAL CA C 66.350 0.02 1 569 . 58 VAL HA H 3.556 0.004 1 570 . 58 VAL CB C 31.564 0.02 1 571 . 58 VAL HB H 2.108 0.003 1 572 . 58 VAL HG1 H 0.752 0.004 1 573 . 58 VAL HG2 H 0.802 0.003 1 574 . 58 VAL CG1 C 21.270 0.010 1 575 . 58 VAL CG2 C 23.740 0.02 1 576 . 59 PHE N N 120.196 0.02 1 577 . 59 PHE H H 8.306 0.003 1 578 . 59 PHE CA C 62.680 0.02 1 579 . 59 PHE HA H 3.954 0.004 1 580 . 59 PHE CB C 38.890 0.02 1 581 . 59 PHE HB2 H 3.064 0.004 1 582 . 59 PHE HB3 H 3.295 0.001 1 583 . 60 THR N N 114.930 0.02 1 584 . 60 THR H H 8.305 0.006 1 585 . 60 THR CA C 66.873 0.02 1 586 . 60 THR HA H 3.751 0.002 1 587 . 60 THR CB C 68.854 0.02 1 588 . 60 THR HB H 4.310 0.001 1 589 . 60 THR HG2 H 1.219 0.006 1 590 . 60 THR CG2 C 21.752 0.02 1 591 . 61 GLU N N 120.587 0.02 1 592 . 61 GLU H H 7.955 0.005 1 593 . 61 GLU HA H 4.048 0.002 1 594 . 61 GLU HB2 H 2.002 0.003 1 595 . 61 GLU HG2 H 2.334 0.002 1 596 . 62 VAL N N 122.214 0.02 1 597 . 62 VAL H H 8.306 0.004 1 598 . 62 VAL CA C 66.836 0.02 1 599 . 62 VAL HA H 2.936 0.005 1 600 . 62 VAL CB C 30.817 0.02 1 601 . 62 VAL HB H 1.466 0.003 1 602 . 62 VAL HG1 H -0.357 0.004 1 603 . 62 VAL HG2 H 0.509 0.003 1 604 . 62 VAL CG1 C 21.018 0.02 1 605 . 62 VAL CG2 C 23.150 0.02 1 606 . 63 ALA N N 122.306 0.02 1 607 . 63 ALA H H 8.724 0.009 1 608 . 63 ALA CA C 55.266 0.02 1 609 . 63 ALA HA H 3.719 0.003 1 610 . 63 ALA HB H 1.147 0.003 1 611 . 63 ALA CB C 17.592 0.02 1 612 . 64 ASN N N 114.582 0.02 1 613 . 64 ASN H H 7.507 0.005 1 614 . 64 ASN CA C 55.673 0.02 1 615 . 64 ASN HA H 4.416 0.002 1 616 . 64 ASN CB C 38.431 0.02 1 617 . 64 ASN HB2 H 2.783 0.005 1 618 . 64 ASN ND2 N 113.497 0.02 1 619 . 64 ASN HD21 H 6.890 0.002 1 620 . 64 ASN HD22 H 7.660 0.002 1 621 . 65 LEU N N 121.359 0.02 1 622 . 65 LEU H H 7.495 0.003 1 623 . 65 LEU CA C 57.161 0.02 1 624 . 65 LEU HA H 4.019 0.005 1 625 . 65 LEU CB C 42.294 0.02 1 626 . 65 LEU HB2 H 1.345 0.002 1 627 . 65 LEU HB3 H 1.459 0.002 1 628 . 65 LEU CG C 26.225 0.02 1 629 . 65 LEU HG H 1.581 0.003 1 630 . 65 LEU HD1 H 0.787 0.001 1 631 . 65 LEU HD2 H 0.756 0.003 1 632 . 65 LEU CD1 C 24.402 0.02 1 633 . 65 LEU CD2 C 24.237 0.02 1 634 . 66 PHE N N 115.332 0.02 1 635 . 66 PHE H H 8.224 0.007 1 636 . 66 PHE HA H 4.827 0.002 1 637 . 66 PHE CB C 36.133 0.02 1 638 . 66 PHE HB2 H 2.881 0.004 1 639 . 66 PHE HB3 H 3.664 0.009 1 640 . 66 PHE HD1 H 6.546 0.005 1 641 . 66 PHE HE1 H 6.596 0.005 1 642 . 66 PHE HD2 H 6.564 0.002 1 643 . 66 PHE HE2 H 6.564 0.002 1 644 . 66 PHE CD1 C 129.065 0.02 1 645 . 66 PHE CE1 C 130.429 0.02 1 646 . 66 PHE CZ C 129.086 0.02 1 647 . 66 PHE HZ H 5.881 0.007 1 648 . 67 ARG N N 121.384 0.02 1 649 . 67 ARG H H 6.952 0.005 1 650 . 67 ARG CA C 58.684 0.02 1 651 . 67 ARG HA H 4.098 0.004 1 652 . 67 ARG CB C 29.770 0.02 1 653 . 67 ARG HB2 H 1.825 0.012 1 654 . 67 ARG HB3 H 1.973 0.003 1 655 . 67 ARG CG C 26.839 0.02 1 656 . 67 ARG HG2 H 1.695 0.003 1 657 . 67 ARG HG3 H 1.800 0.002 1 658 . 67 ARG CD C 43.393 0.02 1 659 . 67 ARG HD2 H 3.247 0.002 1 660 . 67 ARG HD3 H 3.276 0.002 1 661 . 68 GLY N N 115.883 0.02 1 662 . 68 GLY H H 9.396 0.009 1 663 . 68 GLY CA C 45.447 0.02 1 664 . 68 GLY HA2 H 3.863 0.005 1 665 . 68 GLY HA3 H 4.313 0.003 1 666 . 69 GLN N N 120.471 0.02 1 667 . 69 GLN H H 8.488 0.004 1 668 . 69 GLN HA H 4.817 0.002 1 669 . 69 GLN HB2 H 1.836 0.002 1 670 . 69 GLN HG2 H 2.232 0.002 1 671 . 69 GLN NE2 N 111.081 0.02 1 672 . 69 GLN HE21 H 6.758 0.002 1 673 . 69 GLN HE22 H 7.498 0.001 1 674 . 70 GLU N N 120.413 0.02 1 675 . 70 GLU H H 8.580 0.006 1 676 . 70 GLU CA C 61.033 0.02 1 677 . 70 GLU HA H 3.898 0.003 1 678 . 70 GLU CB C 28.942 0.02 1 679 . 70 GLU HB2 H 2.111 0.003 1 680 . 70 GLU CG C 37.304 0.02 1 681 . 70 GLU HG2 H 2.358 0.003 1 682 . 70 GLU HG3 H 2.515 0.003 1 683 . 71 ASP N N 119.342 0.02 1 684 . 71 ASP H H 8.971 0.001 1 685 . 71 ASP CA C 56.467 0.02 1 686 . 71 ASP HA H 4.387 0.003 1 687 . 71 ASP CB C 38.317 0.02 1 688 . 71 ASP HB2 H 2.658 0.003 1 689 . 71 ASP HB3 H 2.822 0.003 1 690 . 72 LEU N N 119.491 0.02 1 691 . 72 LEU H H 7.772 0.004 1 692 . 72 LEU CA C 56.887 0.02 1 693 . 72 LEU HA H 4.298 0.003 1 694 . 72 LEU CB C 41.798 0.02 1 695 . 72 LEU HB2 H 1.014 0.004 1 696 . 72 LEU HB3 H 1.647 0.002 1 697 . 72 LEU CG C 26.317 0.02 1 698 . 72 LEU HG H 1.537 0.006 1 699 . 72 LEU HD1 H 0.153 0.003 1 700 . 72 LEU HD2 H 0.486 0.001 1 701 . 72 LEU CD1 C 26.095 0.02 1 702 . 72 LEU CD2 C 21.970 0.02 1 703 . 73 LEU N N 120.781 0.02 1 704 . 73 LEU H H 7.885 0.007 1 705 . 73 LEU CA C 57.538 0.02 1 706 . 73 LEU HA H 4.369 0.002 1 707 . 73 LEU CB C 42.053 0.02 1 708 . 73 LEU HB2 H 1.813 0.003 1 709 . 73 LEU HB3 H 2.018 0.003 1 710 . 73 LEU CG C 27.090 0.02 1 711 . 73 LEU HG H 1.840 0.002 1 712 . 73 LEU HD1 H 0.774 0.005 1 713 . 73 LEU HD2 H 0.848 0.004 1 714 . 73 LEU CD1 C 24.071 0.02 1 715 . 73 LEU CD2 C 24.568 0.02 1 716 . 74 SER N N 115.079 0.02 1 717 . 74 SER H H 8.311 0.005 1 718 . 74 SER CA C 61.695 0.02 1 719 . 74 SER HA H 4.297 0.009 1 720 . 74 SER CB C 68.897 0.02 1 721 . 74 SER HB2 H 4.045 0.003 1 722 . 75 GLU N N 120.114 0.02 1 723 . 75 GLU H H 7.889 0.007 1 724 . 75 GLU CA C 58.637 0.02 1 725 . 75 GLU HA H 4.053 0.005 1 726 . 75 GLU CB C 30.805 0.02 1 727 . 75 GLU HB2 H 1.802 0.003 1 728 . 75 GLU HB3 H 2.022 0.002 1 729 . 75 GLU CG C 36.995 0.02 1 730 . 75 GLU HG2 H 1.936 0.003 1 731 . 75 GLU HG3 H 2.288 0.004 1 732 . 76 PHE N N 119.553 0.02 1 733 . 76 PHE H H 7.650 0.003 1 734 . 76 PHE CA C 60.837 0.02 1 735 . 76 PHE HA H 4.379 0.007 1 736 . 76 PHE CB C 38.936 0.02 1 737 . 76 PHE HB2 H 3.277 0.003 1 738 . 76 PHE HB3 H 4.057 0.005 1 739 . 76 PHE HD1 H 7.337 0.003 1 740 . 76 PHE HE1 H 7.039 0.003 1 741 . 76 PHE CD1 C 131.541 0.02 1 742 . 76 PHE CE1 C 130.351 0.02 1 743 . 76 PHE CZ C 128.698 0.02 1 744 . 76 PHE HZ H 6.798 0.006 1 745 . 77 GLY N N 124.600 0.02 1 746 . 77 GLY H H 7.795 0.003 1 747 . 77 GLY CA C 46.814 0.02 1 748 . 77 GLY HA2 H 3.511 0.002 1 749 . 77 GLY HA3 H 3.869 0.003 1 750 . 78 GLN N N 117.167 0.02 1 751 . 78 GLN H H 7.387 0.004 1 752 . 78 GLN CA C 57.142 0.02 1 753 . 78 GLN HA H 3.884 0.005 1 754 . 78 GLN CB C 28.597 0.02 1 755 . 78 GLN HB2 H 1.643 0.012 1 756 . 78 GLN CG C 33.833 0.028 1 757 . 78 GLN HG2 H 1.872 0.004 1 758 . 78 GLN HG3 H 2.078 0.005 1 759 . 78 GLN NE2 N 111.725 0.02 1 760 . 78 GLN HE21 H 6.942 0.004 1 761 . 78 GLN HE22 H 7.340 0.002 1 762 . 79 PHE N N 115.057 0.02 1 763 . 79 PHE H H 7.665 0.006 1 764 . 79 PHE CA C 58.328 0.02 1 765 . 79 PHE HA H 4.055 0.002 1 766 . 79 PHE CB C 38.606 0.02 1 767 . 79 PHE HB2 H 2.505 0.001 1 768 . 79 PHE HB3 H 2.883 0.002 1 769 . 79 PHE HD1 H 7.236 0.003 1 770 . 79 PHE HE1 H 7.236 0.003 1 771 . 79 PHE CD1 C 132.458 0.02 1 772 . 80 LEU N N 118.370 0.02 1 773 . 80 LEU H H 6.893 0.005 1 774 . 80 LEU CA C 51.948 0.02 1 775 . 80 LEU HA H 4.650 0.001 1 776 . 80 LEU CB C 42.536 0.02 1 777 . 80 LEU HB2 H 1.429 0.004 1 778 . 80 LEU CG C 26.292 0.02 1 779 . 80 LEU HG H 1.249 0.004 1 780 . 80 LEU HD1 H 0.702 0.003 1 781 . 80 LEU HD2 H 0.654 0.004 1 782 . 80 LEU CD1 C 26.291 0.004 1 783 . 80 LEU CD2 C 23.852 0.035 1 784 . 81 PRO CD C 50.580 0.02 1 785 . 81 PRO CA C 63.941 0.02 1 786 . 81 PRO HA H 4.326 0.004 1 787 . 81 PRO CB C 32.185 0.02 1 788 . 81 PRO HB2 H 1.889 0.003 1 789 . 81 PRO HB3 H 2.318 0.003 1 790 . 81 PRO CG C 27.716 0.02 1 791 . 81 PRO HG2 H 2.053 0.003 1 792 . 81 PRO HD2 H 3.685 0.004 1 793 . 82 GLU N N 120.563 0.02 1 794 . 82 GLU H H 9.056 0.006 1 795 . 82 GLU CA C 57.583 0.02 1 796 . 82 GLU HA H 4.100 0.002 1 797 . 82 GLU CB C 29.597 0.02 1 798 . 82 GLU HB2 H 1.909 0.004 1 799 . 82 GLU HB3 H 2.033 0.003 1 800 . 82 GLU HG2 H 2.274 0.002 1 801 . 83 ALA N N 123.499 0.02 1 802 . 83 ALA H H 8.147 0.001 1 803 . 83 ALA CA C 52.879 0.02 1 804 . 83 ALA HA H 4.200 0.007 1 805 . 83 ALA HB H 1.319 0.003 1 806 . 83 ALA CB C 19.141 0.02 1 807 . 84 LYS N N 119.186 0.02 1 808 . 84 LYS H H 8.223 0.008 1 809 . 84 LYS CA C 56.369 0.02 1 810 . 84 LYS HA H 4.205 0.003 1 811 . 84 LYS CB C 32.668 0.02 1 812 . 84 LYS HB2 H 1.713 0.002 1 813 . 84 LYS HB3 H 1.826 0.003 1 814 . 84 LYS CG C 24.996 0.02 1 815 . 84 LYS HG2 H 1.367 0.002 1 816 . 84 LYS CD C 29.060 0.02 1 817 . 84 LYS HD2 H 1.628 0.003 1 818 . 84 LYS CE C 42.071 0.02 1 819 . 84 LYS HE2 H 2.911 0.002 1 820 . 85 ARG N N 120.746 0.02 1 821 . 85 ARG H H 8.065 0.010 1 822 . 85 ARG CA C 56.886 0.02 1 823 . 85 ARG HA H 4.152 0.004 1 824 . 85 ARG CB C 30.563 0.02 1 825 . 85 ARG HB2 H 1.702 0.002 1 826 . 85 ARG HB3 H 1.794 0.007 1 827 . 85 ARG CG C 27.109 0.02 1 828 . 85 ARG HG2 H 1.557 0.003 1 829 . 85 ARG HG3 H 1.611 0.002 1 830 . 85 ARG CD C 43.427 0.02 1 831 . 85 ARG HD2 H 3.064 0.002 1 stop_ save_ save_15N_T1_Set_1 _Saveframe_category T1_relaxation _Details . loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $Ex-cond_1 _Spectrometer_frequency_1H 600 _T1_coherence_type Nz _T1_value_units ms _Mol_system_component_name 'PAH2 domain of mSin3B' _Text_data_format . _Text_data . loop_ _T1_ID _Residue_seq_code _Residue_label _Atom_name _T1_value _T1_value_error 1 1 GLU N 0.708 0.028 2 2 SER N 0.602 0.024 3 3 ASP N 0.565 0.023 4 4 SER N 0.604 0.024 5 5 VAL N 0.666 0.027 6 7 PHE N 0.646 0.026 7 8 ASN N 0.663 0.026 8 9 ASN N 0.666 0.027 9 10 ALA N 0.657 0.026 10 12 SER N 0.660 0.027 11 13 TYR N 0.668 0.027 12 14 VAL N 0.657 0.026 13 15 ASN N 0.661 0.027 14 16 LYS N 0.689 0.028 15 17 ILE N 0.672 0.027 16 18 LYS N 0.650 0.026 17 19 THR N 0.727 0.029 18 20 ARG N 0.690 0.028 19 21 PHE N 0.697 0.028 20 22 LEU N 0.684 0.028 21 23 ASP N 0.707 0.028 22 24 HIS N 0.710 0.028 23 26 GLU N 0.683 0.028 24 27 ILE N 0.698 0.028 25 28 TYR N 0.746 0.032 26 29 ARG N 0.683 0.027 27 30 SER N 0.717 0.029 28 31 PHE N 0.707 0.029 29 32 LEU N 0.710 0.028 30 33 GLU N 0.670 0.027 31 34 ILE N 0.706 0.028 32 35 LEU N 0.690 0.028 33 36 HIS N 0.690 0.028 34 37 THR N 0.683 0.027 35 38 TYR N 0.712 0.028 36 41 GLU N 0.670 0.027 37 42 GLN N 0.677 0.027 38 43 LEU N 0.646 0.026 39 44 HIS N 0.573 0.023 40 46 LYS N 0.606 0.028 41 47 GLY N 0.678 0.122 42 50 PHE N 0.623 0.025 43 51 ARG N 0.590 0.024 44 52 GLY N 0.618 0.025 45 53 MET N 0.644 0.026 46 54 SER N 0.643 0.039 47 56 GLU N 0.748 0.035 48 58 VAL N 0.691 0.028 49 59 PHE N 0.693 0.028 50 61 GLU N 0.671 0.027 51 62 VAL N 0.699 0.028 52 63 ALA N 0.690 0.028 53 64 ASN N 0.715 0.029 54 65 LEU N 0.688 0.027 55 66 PHE N 0.743 0.030 56 67 ARG N 0.699 0.028 57 68 GLY N 0.713 0.043 58 69 GLN N 0.692 0.028 59 70 GLU N 0.685 0.027 60 71 ASP N 0.682 0.027 61 72 LEU N 0.669 0.027 62 75 GLU N 0.683 0.028 63 76 PHE N 0.659 0.026 64 77 GLY N 0.684 0.028 65 78 GLN N 0.661 0.027 66 79 PHE N 0.667 0.027 67 80 LEU N 0.701 0.028 68 83 ALA N 0.634 0.025 69 85 ARG N 0.602 0.024 70 94 ALA N 0.651 0.026 71 96 MET N 0.636 0.025 72 97 ASN N 0.611 0.025 73 99 GLY N 0.664 0.026 74 101 LYS N 0.694 0.028 75 102 ASN N 0.703 0.028 76 103 GLU N 0.741 0.030 77 104 GLU N 0.780 0.031 78 105 LYS N 1.016 0.040 stop_ save_ save_heteronuclear_NOE_1 _Saveframe_category heteronuclear_NOE _Details . loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $Ex-cond_1 _Spectrometer_frequency_1H 600 _Mol_system_component_name 'PAH2 domain of mSin3B' _Atom_one_atom_name N _Atom_two_atom_name H _Heteronuclear_NOE_value_type . _NOE_reference_value . _NOE_reference_description . _Text_data_format . _Text_data . loop_ _Residue_seq_code _Residue_label _Heteronuclear_NOE_value _Heteronuclear_NOE_value_error 1 GLU -0.266 0.082 2 SER 0.014 0.100 3 ASP 0.168 0.071 4 SER 0.275 0.048 5 VAL 0.599 0.025 7 PHE 0.755 0.030 8 ASN 0.733 0.029 9 ASN 0.818 0.033 10 ALA 0.796 0.032 12 SER 0.735 0.029 13 TYR 0.794 0.032 14 VAL 0.775 0.031 15 ASN 0.771 0.031 16 LYS 0.875 0.035 17 ILE 0.779 0.031 18 LYS 0.894 0.036 19 THR 0.761 0.030 20 ARG 0.816 0.033 21 PHE 0.778 0.031 22 LEU 0.728 0.029 23 ASP 0.752 0.030 24 HIS 0.712 0.028 26 GLU 0.747 0.030 27 ILE 0.757 0.030 28 TYR 0.733 0.029 29 ARG 0.788 0.032 30 SER 0.783 0.031 31 PHE 0.792 0.032 32 LEU 0.848 0.034 33 GLU 0.686 0.027 34 ILE 0.766 0.031 35 LEU 0.743 0.030 36 HIS 0.755 0.030 37 THR 0.796 0.032 38 TYR 0.735 0.029 41 GLU 0.701 0.028 42 GLN 0.689 0.028 43 LEU 0.567 0.030 44 HIS 0.167 0.148 46 LYS 0.369 0.059 47 GLY 0.363 0.107 50 PHE 0.379 0.050 51 ARG 0.391 0.053 52 GLY 0.358 0.084 53 MET 0.483 0.040 54 SER 0.706 0.031 56 GLU 0.756 0.030 58 VAL 0.719 0.029 59 PHE 0.772 0.031 61 GLU 0.722 0.029 62 VAL 0.763 0.031 63 ALA 0.744 0.030 64 ASN 0.782 0.031 65 LEU 0.810 0.032 66 PHE 0.750 0.030 67 ARG 0.706 0.028 68 GLY 0.690 0.028 69 GLN 0.836 0.033 70 GLU 0.629 0.025 71 ASP 0.773 0.031 72 LEU 0.688 0.028 75 GLU 0.688 0.028 76 PHE 0.711 0.028 77 GLY 0.729 0.029 78 GLN 0.746 0.030 79 PHE 0.765 0.031 80 LEU 0.671 0.027 83 ALA 0.516 0.054 85 ARG 0.400 0.060 94 ALA -0.316 0.079 96 MET -0.340 0.134 97 ASN -0.426 0.073 99 GLY -0.419 0.056 101 LYS -0.705 0.030 102 ASN -0.735 0.040 103 GLU -0.812 0.032 104 GLU -1.137 0.045 105 LYS -1.499 0.060 stop_ save_ save_S2_parameters_label _Saveframe_category S2_parameters _Details . loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $Ex-cond_1 _Mol_system_component_name 'PAH2 domain of mSin3B' _Tau_e_value_units . _Text_data_format . _Text_data . loop_ _Residue_seq_code _Residue_label _Atom_name _Model_fit _S2_value _S2_value_fit_error _Tau_e_value _Tau_e_value_fit_error _S2f_value _S2f_value_fit_error _S2s_value _S2s_value_fit_error _Tau_s_value _Tau_s_value_fit_error _S2H_value _S2H_value_fit_error _S2N_value _S2N_value_fit_error 1 GLU N . 0.136 . . . . . . . . . . . . . 2 SER N . 0.212 . . . . . . . . . . . . . 3 ASP N . 0.261 . . . . . . . . . . . . . 4 SER N . 0.363 . . . . . . . . . . . . . 5 VAL N . 0.841 . . . . . . . . . . . . . 7 PHE N . 0.900 . . . . . . . . . . . . . 8 ASN N . 0.879 . . . . . . . . . . . . . 9 ASN N . 0.940 . . . . . . . . . . . . . 10 ALA N . 0.939 . . . . . . . . . . . . . 12 SER N . 0.903 . . . . . . . . . . . . . 13 TYR N . 0.922 . . . . . . . . . . . . . 14 VAL N . 0.932 . . . . . . . . . . . . . 15 ASN N . 0.927 . . . . . . . . . . . . . 16 LYS N . 0.976 . . . . . . . . . . . . . 17 ILE N . 0.905 . . . . . . . . . . . . . 18 LYS N . 1.000 . . . . . . . . . . . . . 19 THR N . 0.886 . . . . . . . . . . . . . 20 ARG N . 0.933 . . . . . . . . . . . . . 21 PHE N . 0.863 . . . . . . . . . . . . . 22 LEU N . 0.894 . . . . . . . . . . . . . 23 ASP N . 0.881 . . . . . . . . . . . . . 24 HIS N . 0.827 . . . . . . . . . . . . . 26 GLU N . 0.891 . . . . . . . . . . . . . 27 ILE N . 0.940 . . . . . . . . . . . . . 28 TYR N . 0.876 . . . . . . . . . . . . . 29 ARG N . 0.934 . . . . . . . . . . . . . 30 SER N . 0.900 . . . . . . . . . . . . . 31 PHE N . 0.885 . . . . . . . . . . . . . 32 LEU N . 0.918 . . . . . . . . . . . . . 33 GLU N . 0.881 . . . . . . . . . . . . . 34 ILE N . 0.925 . . . . . . . . . . . . . 35 LEU N . 0.937 . . . . . . . . . . . . . 36 HIS N . 0.929 . . . . . . . . . . . . . 37 THR N . 0.935 . . . . . . . . . . . . . 38 TYR N . 0.875 . . . . . . . . . . . . . 41 GLU N . 0.898 . . . . . . . . . . . . . 42 GLN N . 0.900 . . . . . . . . . . . . . 43 LEU N . 0.687 . . . . . . . . . . . . . 44 HIS N . 0.324 . . . . . . . . . . . . . 46 LYS N . 0.521 . . . . . . . . . . . . . 47 GLY N . 0.330 . . . . . . . . . . . . . 50 PHE N . 0.497 . . . . . . . . . . . . . 51 ARG N . 0.518 . . . . . . . . . . . . . 52 GLY N . 0.551 . . . . . . . . . . . . . 53 MET N . 0.583 . . . . . . . . . . . . . 56 GLU N . 0.873 . . . . . . . . . . . . . 58 VAL N . 0.899 . . . . . . . . . . . . . 59 PHE N . 0.937 . . . . . . . . . . . . . 61 GLU N . 0.922 . . . . . . . . . . . . . 62 VAL N . 0.911 . . . . . . . . . . . . . 63 ALA N . 0.930 . . . . . . . . . . . . . 64 ASN N . 0.891 . . . . . . . . . . . . . 65 LEU N . 0.901 . . . . . . . . . . . . . 66 PHE N . 0.883 . . . . . . . . . . . . . 67 ARG N . 0.858 . . . . . . . . . . . . . 68 GLY N . 0.853 . . . . . . . . . . . . . 69 GLN N . 0.864 . . . . . . . . . . . . . 70 GLU N . 0.833 . . . . . . . . . . . . . 71 ASP N . 0.921 . . . . . . . . . . . . . 72 LEU N . 0.777 . . . . . . . . . . . . . 75 GLU N . 0.873 . . . . . . . . . . . . . 76 PHE N . 0.892 . . . . . . . . . . . . . 77 GLY N . 0.862 . . . . . . . . . . . . . 78 GLN N . 0.918 . . . . . . . . . . . . . 79 PHE N . 0.915 . . . . . . . . . . . . . 80 LEU N . 0.865 . . . . . . . . . . . . . 83 ALA N . 0.714 . . . . . . . . . . . . . 85 ARG N . 0.478 . . . . . . . . . . . . . 94 ALA N . 0.065 . . . . . . . . . . . . . 96 MET N . 0.070 . . . . . . . . . . . . . 97 ASN N . 0.055 . . . . . . . . . . . . . 99 GLY N . 0.054 . . . . . . . . . . . . . 101 LYS N . 0.035 . . . . . . . . . . . . . 102 ASN N . 0.063 . . . . . . . . . . . . . 103 GLU N . 0.024 . . . . . . . . . . . . . 104 GLU N . 0.021 . . . . . . . . . . . . . 105 LYS N . 0.024 . . . . . . . . . . . . . stop_ _Tau_s_value_units . save_