data_5558 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Sp100b SAND domain chemical shift assignments ; _BMRB_accession_number 5558 _BMRB_flat_file_name bmr5558.str _Entry_type original _Submission_date 2002-10-15 _Accession_date 2002-10-15 _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 Bottomley Matthew J. . 2 Collard Michael W. . 3 Huggenvik Jodi I. . 4 Liu Zhihong . . 5 Gibson Toby J. . 6 Sattler Michael . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 coupling_constants 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 423 "13C chemical shifts" 296 "15N chemical shifts" 97 "coupling constants" 30 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2002-12-27 original author . stop_ _Original_release_date 2002-12-27 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; The SAND domain structure defines a novel DNA-binding fold in transcriptional regulation ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 11427895 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Bottomley Matthew J. . 2 Collard Michael W. . 3 Huggenvik Jodi I. . 4 Liu Zhihong . . 5 Gibson Toby J. . 6 Sattler Michael . . stop_ _Journal_abbreviation 'Nat. Struct. Biol.' _Journal_volume 8 _Journal_issue 7 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 626 _Page_last 633 _Year 2001 _Details . loop_ _Keyword 'SAND domain' Sp100b KDWK stop_ save_ ################################## # Molecular system description # ################################## save_system_Sp100b_SAND _Saveframe_category molecular_system _Mol_system_name 'Sp100b SAND domain' _Abbreviation_common 'Sp100b SAND' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'Sp100b SAND domain' $Sp100b_SAND stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state monomer _System_paramagnetic no _System_thiol_state 'all free' loop_ _Biological_function 'DNA binding domain' stop_ _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_Sp100b_SAND _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'SAND domain from human Sp100b protein' _Abbreviation_common 'Sp100b SAND' _Molecular_mass 12212 _Mol_thiol_state 'all free' _Details ; N-terminally His-tagged Sp100b SAND domain, including human Sp100b residues Asp 595 to Lys 688 (the 'real' C-terminus), total 104 residues, calculated pI 9.5. ; ############################## # Polymer residue sequence # ############################## _Residue_count 104 _Mol_residue_sequence ; MKHHHHHHPMDENINFKQSE LPVTCGEVKGTLYKERFKQG TSKKCIQSEDKKWFTPREFE IEGDRGASKNWKLSIRCGGY TLKVLMENKFLPEPPSTRKK VTIK ; loop_ _Residue_seq_code _Residue_label 1 MET 2 LYS 3 HIS 4 HIS 5 HIS 6 HIS 7 HIS 8 HIS 9 PRO 10 MET 11 ASP 12 GLU 13 ASN 14 ILE 15 ASN 16 PHE 17 LYS 18 GLN 19 SER 20 GLU 21 LEU 22 PRO 23 VAL 24 THR 25 CYS 26 GLY 27 GLU 28 VAL 29 LYS 30 GLY 31 THR 32 LEU 33 TYR 34 LYS 35 GLU 36 ARG 37 PHE 38 LYS 39 GLN 40 GLY 41 THR 42 SER 43 LYS 44 LYS 45 CYS 46 ILE 47 GLN 48 SER 49 GLU 50 ASP 51 LYS 52 LYS 53 TRP 54 PHE 55 THR 56 PRO 57 ARG 58 GLU 59 PHE 60 GLU 61 ILE 62 GLU 63 GLY 64 ASP 65 ARG 66 GLY 67 ALA 68 SER 69 LYS 70 ASN 71 TRP 72 LYS 73 LEU 74 SER 75 ILE 76 ARG 77 CYS 78 GLY 79 GLY 80 TYR 81 THR 82 LEU 83 LYS 84 VAL 85 LEU 86 MET 87 GLU 88 ASN 89 LYS 90 PHE 91 LEU 92 PRO 93 GLU 94 PRO 95 PRO 96 SER 97 THR 98 ARG 99 LYS 100 LYS 101 VAL 102 THR 103 ILE 104 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 1H5P "Solution Structure Of The Human Sp100b Sand Domain By Heteronuclear Nmr" 91.35 95 100.00 100.00 2.46e-62 EMBL CAH18143 "hypothetical protein [Homo sapiens]" 54.81 258 100.00 100.00 1.07e-30 GB AAC50743 "SP100-B [Homo sapiens]" 92.31 688 98.96 98.96 4.43e-58 GB AAY14879 "unknown [Homo sapiens]" 88.46 843 98.91 98.91 3.69e-55 GB EAW70929 "SP100 nuclear antigen, isoform CRA_c [Homo sapiens]" 88.46 844 98.91 98.91 3.78e-55 REF NP_001193630 "nuclear autoantigen Sp-100 isoform 3 [Homo sapiens]" 92.31 688 97.92 97.92 2.55e-57 REF XP_004033374 "PREDICTED: nuclear body protein SP140-like protein-like [Gorilla gorilla gorilla]" 75.96 352 97.47 98.73 4.88e-46 REF XP_009442793 "PREDICTED: nuclear autoantigen Sp-100 isoform X3 [Pan troglodytes]" 75.96 872 98.73 98.73 5.66e-45 REF XP_009442794 "PREDICTED: nuclear autoantigen Sp-100 isoform X4 [Pan troglodytes]" 75.96 866 98.73 98.73 3.88e-45 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $Sp100b_SAND 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 _Details $Sp100b_SAND 'recombinant technology' 'E. coli' Escherichia coli BL21-DE3 pET-9d ; Protein was expressed from an in-house modified pET-9d vector (originally supplied by NOVAGEN) in E. coli BL21-DE3 cells induced with IPTG at 23 degrees C. ; stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_Sample_1 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $Sp100b_SAND 1.2 mM '[U-95% 15N]' 'sodium phosphate' 20 mM . 'sodium chloride' 50 mM . DTT 4 mM . stop_ save_ save_Sample_2 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $Sp100b_SAND 1.2 mM '[U-95% 13C; U-15N]' 'sodium phosphate' 20 mM . 'sodium chloride' 50 mM . DTT 4 mM . stop_ save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model DRX _Field_strength 500 _Details . save_ save_NMR_spectrometer_2 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model DRX _Field_strength 600 _Details . save_ save_NMR_spectrometer_3 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model DRX _Field_strength 700 _Details . save_ ############################# # NMR applied experiments # ############################# save_HNCA_1 _Saveframe_category NMR_applied_experiment _Experiment_name HNCA _Sample_label . save_ save_CBCANH_2 _Saveframe_category NMR_applied_experiment _Experiment_name CBCANH _Sample_label . save_ save_CBCA(CO)NH_3 _Saveframe_category NMR_applied_experiment _Experiment_name CBCA(CO)NH _Sample_label . save_ save_H(C)CH_TOCSY_4 _Saveframe_category NMR_applied_experiment _Experiment_name 'H(C)CH TOCSY' _Sample_label . save_ save_CCH_TOCSY_5 _Saveframe_category NMR_applied_experiment _Experiment_name 'CCH TOCSY' _Sample_label . save_ save_15N-edited_NOESY_6 _Saveframe_category NMR_applied_experiment _Experiment_name '15N-edited NOESY' _Sample_label . save_ save_13C-edited_NOESY_7 _Saveframe_category NMR_applied_experiment _Experiment_name '13C-edited NOESY' _Sample_label . 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 CBCANH _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_3 _Saveframe_category NMR_applied_experiment _Experiment_name CBCA(CO)NH _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_4 _Saveframe_category NMR_applied_experiment _Experiment_name 'H(C)CH TOCSY' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_5 _Saveframe_category NMR_applied_experiment _Experiment_name 'CCH TOCSY' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_6 _Saveframe_category NMR_applied_experiment _Experiment_name '15N-edited NOESY' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_7 _Saveframe_category NMR_applied_experiment _Experiment_name '13C-edited NOESY' _BMRB_pulse_sequence_accession_number . _Details . save_ ####################### # Sample conditions # ####################### save_Sample_condition_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 6.5 0.2 n/a temperature 295 0.5 K 'ionic strength' 0.07 0.01 M 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 DSS H 1 'methyl protons' ppm 0.0 internal direct . . . 1.0 DSS N 15 'methyl protons' ppm 0.0 . indirect . . . 0.101329118 DSS C 13 'methyl protons' ppm 0.0 . indirect . . . 0.251449530 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 ; 584 should be added to the given residue number to derive the wild-type residue number of human Sp100b. The first eight N-terminal signals, which include the his tag and a linker and were not derived from Sp100b, were not observed in the NMR spectra and so no chemical shift information is given for these residues. The C-terminus of the protein is highly flexible, and therefore some chemical shifts in this region were not observable due to lack of NOEs and rapid solvent-exchange of the backbone NH, or because they are PRO. ; loop_ _Sample_label $Sample_1 $Sample_2 stop_ _Sample_conditions_label $Sample_condition_1 _Chem_shift_reference_set_label $chemical_shift_reference _Mol_system_component_name 'Sp100b SAND domain' _Text_data_format . _Text_data . loop_ _Atom_shift_assign_ID _Residue_author_seq_code _Residue_seq_code _Residue_label _Atom_name _Atom_type _Chem_shift_value _Chem_shift_value_error _Chem_shift_ambiguity_code 1 . 9 PRO CA C 60.709 0.02 1 2 . 9 PRO HA H 4.33 0.02 1 3 . 9 PRO CB C 29.646 0.02 1 4 . 9 PRO HB3 H 1.82 0.02 1 5 . 9 PRO CG C 24.986 0.02 1 6 . 9 PRO HG3 H 1.837 0.02 1 7 . 9 PRO CD C 48.284 0.02 1 8 . 9 PRO HD3 H 3.501 0.02 1 9 . 10 MET H H 8.17 0.006 1 10 . 10 MET N N 120.638 0.02 1 11 . 10 MET CA C 60.191 0.02 1 12 . 10 MET HA H 3.853 0.02 1 13 . 10 MET CB C 30.163 0.02 1 14 . 10 MET HB3 H 1.834 0.02 1 15 . 10 MET HG2 H 0.781 0.02 2 16 . 10 MET HG3 H 0.824 0.02 2 17 . 11 ASP CA C 51.908 0.02 1 18 . 11 ASP HA H 4.505 0.02 1 19 . 11 ASP CB C 38.965 0.02 1 20 . 11 ASP HB3 H 2.61 0.02 1 21 . 12 GLU H H 8.214 0.005 1 22 . 12 GLU N N 120.638 0.02 1 23 . 12 GLU CA C 54.496 0.02 1 24 . 12 GLU HA H 4.147 0.003 1 25 . 12 GLU CB C 28.093 0.02 1 26 . 12 GLU HB3 H 1.821 0.007 1 27 . 12 GLU CG C 33.787 0.02 1 28 . 12 GLU HG3 H 2.142 0.002 1 29 . 13 ASN H H 8.397 0.006 1 30 . 13 ASN N N 118.729 0.02 1 31 . 13 ASN CA C 50.872 0.02 1 32 . 13 ASN HA H 4.531 0.004 1 33 . 13 ASN CB C 36.376 0.02 1 34 . 13 ASN HB3 H 2.58 0.007 1 35 . 13 ASN ND2 N 113.316 0.02 1 36 . 13 ASN HD21 H 7.561 0.011 1 37 . 13 ASN HD22 H 6.846 0.013 1 38 . 14 ILE H H 7.71 0.005 1 39 . 14 ILE N N 121.409 0.02 1 40 . 14 ILE CA C 58.311 0.02 1 41 . 14 ILE HA H 3.704 0.02 1 42 . 14 ILE CB C 36.894 0.02 1 43 . 14 ILE HB H 1.259 0.02 1 44 . 14 ILE CG2 C 15.15 0.02 1 45 . 14 ILE CG1 C 25.504 0.02 1 46 . 14 ILE HG13 H 0.853 0.02 1 47 . 14 ILE CD1 C 11.16 0.02 1 48 . 14 ILE HD1 H 0.719 0.009 1 49 . 15 ASN H H 8.089 0.005 1 50 . 15 ASN N N 122.184 0.02 1 51 . 15 ASN CA C 49.044 0.02 1 52 . 15 ASN HA H 4.439 0.002 1 53 . 15 ASN CB C 35.341 0.02 1 54 . 15 ASN HB3 H 2.548 0.002 1 55 . 15 ASN ND2 N 111.26 0.02 1 56 . 15 ASN HD21 H 7.568 0.007 1 57 . 15 ASN HD22 H 6.848 0.003 1 58 . 16 PHE H H 7.861 0.007 1 59 . 16 PHE N N 122.174 0.02 1 60 . 16 PHE CA C 56.676 0.02 1 61 . 16 PHE HA H 4.118 0.02 1 62 . 16 PHE CB C 35.689 0.02 1 63 . 16 PHE HB3 H 1.747 0.02 1 64 . 16 PHE CD1 C 128.355 0.02 1 65 . 16 PHE HD1 H 6.676 0.02 1 66 . 16 PHE HE1 H 6.768 0.02 3 67 . 17 LYS H H 7.811 0.005 1 68 . 17 LYS N N 116.294 0.02 1 69 . 17 LYS CA C 54.496 0.02 1 70 . 17 LYS HA H 4.216 0.02 1 71 . 17 LYS CB C 29.966 0.02 1 72 . 17 LYS HB3 H 1.819 0.001 1 73 . 17 LYS CG C 23.433 0.02 1 74 . 17 LYS HG3 H 1.518 0.003 1 75 . 17 LYS CD C 26.695 0.02 1 76 . 17 LYS HD3 H 1.708 0.02 1 77 . 17 LYS CE C 39.482 0.02 1 78 . 17 LYS HE3 H 2.983 0.02 1 79 . 18 GLN H H 7.204 0.006 1 80 . 18 GLN N N 118.84 0.02 1 81 . 18 GLN CA C 53.678 0.02 1 82 . 18 GLN HA H 4.262 0.02 1 83 . 18 GLN CB C 27.057 0.02 1 84 . 18 GLN HB3 H 2.083 0.006 1 85 . 18 GLN CG C 31.717 0.02 1 86 . 18 GLN HG3 H 2.296 0.02 1 87 . 18 GLN NE2 N 120.125 0.02 1 88 . 19 SER H H 8.382 0.004 1 89 . 19 SER N N 113.187 0.02 1 90 . 19 SER CA C 58.311 0.02 1 91 . 19 SER HA H 4.194 0.02 1 92 . 19 SER CB C 61.582 0.02 1 93 . 19 SER HB3 H 3.95 0.002 1 94 . 20 GLU H H 7.353 0.005 1 95 . 20 GLU N N 120.743 0.02 1 96 . 20 GLU CA C 51.77 0.02 1 97 . 20 GLU HA H 4.923 0.006 1 98 . 20 GLU CB C 28.331 0.02 1 99 . 20 GLU HB3 H 1.213 0.02 1 100 . 20 GLU CG C 33.787 0.02 1 101 . 20 GLU HG3 H 1.689 0.02 1 102 . 21 LEU H H 8.792 0.006 1 103 . 21 LEU N N 121.801 0.02 1 104 . 21 LEU CA C 48.166 0.02 1 105 . 21 LEU HA H 4.831 0.02 1 106 . 21 LEU CB C 42.776 0.02 1 107 . 21 LEU HB3 H 1.359 0.02 1 108 . 21 LEU CG C 24.242 0.02 1 109 . 21 LEU CD1 C 23.697 0.02 1 110 . 21 LEU HD1 H 0.802 0.003 1 111 . 21 LEU HD2 H 0.776 0.02 1 112 . 21 LEU HG H 1.31 0.02 1 113 . 22 PRO CA C 60.199 0.02 1 114 . 22 PRO HA H 4.916 0.01 1 115 . 22 PRO CB C 29.128 0.02 1 116 . 22 PRO HB3 H 1.95 0.02 1 117 . 22 PRO CG C 24.986 0.02 1 118 . 22 PRO HG3 H 2.069 0.02 1 119 . 22 PRO CD C 47.954 0.02 1 120 . 22 PRO HD3 H 3.293 0.02 1 121 . 23 VAL H H 8.852 0.007 1 122 . 23 VAL N N 118.326 0.02 1 123 . 23 VAL CA C 55.858 0.02 1 124 . 23 VAL HA H 5.633 0.001 1 125 . 23 VAL CB C 34.054 0.02 1 126 . 23 VAL HB H 2.115 0.003 1 127 . 23 VAL CG1 C 20.327 0.02 1 128 . 23 VAL HG1 H 0.661 0.003 1 129 . 23 VAL CG2 C 16.338 0.02 1 130 . 23 VAL HG2 H 0.212 0.004 1 131 . 24 THR H H 9.161 0.006 1 132 . 24 THR N N 111.646 0.02 1 133 . 24 THR CA C 57.602 0.02 1 134 . 24 THR HA H 5.31 0.003 1 135 . 24 THR CB C 70.303 0.02 1 136 . 24 THR HB H 3.972 0.001 1 137 . 24 THR CG2 C 19.609 0.02 1 138 . 24 THR HG2 H 1.022 0.001 1 139 . 25 CYS H H 8.41 0.002 1 140 . 25 CYS N N 122.184 0.02 1 141 . 25 CYS CA C 56.676 0.02 1 142 . 25 CYS HA H 4.371 0.008 1 143 . 25 CYS CB C 25.332 0.02 1 144 . 25 CYS HB3 H 1.583 0.004 1 145 . 26 GLY H H 8.822 0.005 1 146 . 26 GLY N N 117.711 0.02 1 147 . 26 GLY CA C 44.659 0.02 1 148 . 26 GLY HA2 H 4.042 0.003 1 149 . 26 GLY HA3 H 3.513 0.02 1 150 . 27 GLU H H 9.15 0.005 1 151 . 27 GLU N N 126.42 0.02 1 152 . 27 GLU CA C 53.971 0.02 1 153 . 27 GLU HA H 4.238 0.004 1 154 . 27 GLU CB C 27.785 0.02 1 155 . 27 GLU HB3 H 1.73 0.001 1 156 . 27 GLU CG C 34.054 0.02 1 157 . 27 GLU HG3 H 2.124 0.02 1 158 . 28 VAL H H 8.038 0.005 1 159 . 28 VAL N N 121.024 0.02 1 160 . 28 VAL CA C 59.946 0.02 1 161 . 28 VAL HA H 4.09 0.02 1 162 . 28 VAL CB C 30.163 0.02 1 163 . 28 VAL HB H 1.757 0.002 1 164 . 28 VAL CG1 C 19.609 0.02 1 165 . 28 VAL HG1 H 0.661 0.006 1 166 . 29 LYS H H 8.422 0.008 1 167 . 29 LYS N N 124.695 0.02 1 168 . 29 LYS CA C 52.587 0.02 1 169 . 29 LYS HA H 5.073 0.002 1 170 . 29 LYS CB C 33.27 0.02 1 171 . 29 LYS HB3 H 1.607 0.02 1 172 . 29 LYS CG C 22.915 0.02 1 173 . 29 LYS HG3 H 1.301 0.02 1 174 . 29 LYS HD3 H 1.525 0.02 1 175 . 29 LYS CE C 40.0 0.02 1 176 . 29 LYS HE3 H 2.791 0.02 1 177 . 30 GLY H H 8.541 0.004 1 178 . 30 GLY N N 106.507 0.02 1 179 . 30 GLY CA C 43.321 0.02 1 180 . 30 GLY HA2 H 4.463 0.001 1 181 . 30 GLY HA3 H 3.111 0.001 1 182 . 31 THR H H 8.478 0.004 1 183 . 31 THR N N 117.838 0.02 1 184 . 31 THR CA C 59.156 0.02 1 185 . 31 THR HA H 4.704 0.006 1 186 . 31 THR CB C 68.474 0.02 1 187 . 31 THR HB H 3.7 0.003 1 188 . 31 THR CG2 C 19.064 0.02 1 189 . 31 THR HG2 H 0.428 0.016 1 190 . 32 LEU H H 9.665 0.008 1 191 . 32 LEU N N 129.134 0.02 1 192 . 32 LEU CA C 52.425 0.02 1 193 . 32 LEU HA H 4.616 0.02 1 194 . 32 LEU CB C 42.589 0.02 1 195 . 32 LEU HB3 H 1.172 0.02 1 196 . 32 LEU CG C 26.022 0.02 1 197 . 32 LEU CD1 C 24.242 0.02 1 198 . 32 LEU HD1 H 0.398 0.038 1 199 . 32 LEU CD2 C 22.398 0.02 1 200 . 32 LEU HD2 H 0.337 0.02 1 201 . 32 LEU HG H 1.228 0.02 1 202 . 33 TYR H H 8.933 0.005 1 203 . 33 TYR N N 126.873 0.02 1 204 . 33 TYR CA C 55.313 0.02 1 205 . 33 TYR HA H 4.653 0.015 1 206 . 33 TYR CB C 35.395 0.02 1 207 . 33 TYR HB3 H 3.021 0.001 1 208 . 33 TYR CD1 C 131.081 0.02 1 209 . 33 TYR HD1 H 7.255 0.02 1 210 . 33 TYR CE1 C 116.363 0.02 1 211 . 33 TYR HE1 H 6.525 0.02 1 212 . 34 LYS H H 8.738 0.006 1 213 . 34 LYS N N 128.071 0.02 1 214 . 34 LYS CA C 59.401 0.02 1 215 . 34 LYS HA H 3.705 0.02 1 216 . 34 LYS CB C 31.199 0.02 1 217 . 34 LYS HB3 H 1.85 0.02 1 218 . 34 LYS CG C 24.469 0.02 1 219 . 34 LYS HG3 H 1.082 0.02 1 220 . 34 LYS CD C 28.61 0.02 1 221 . 34 LYS HD3 H 1.749 0.02 1 222 . 34 LYS CE C 40.0 0.02 1 223 . 34 LYS HE3 H 3.036 0.02 1 224 . 35 GLU H H 9.584 0.007 1 225 . 35 GLU N N 115.835 0.02 1 226 . 35 GLU CA C 56.567 0.02 1 227 . 35 GLU HA H 4.025 0.006 1 228 . 35 GLU CB C 27.057 0.02 1 229 . 35 GLU HB3 H 1.967 0.02 1 230 . 35 GLU CG C 33.787 0.02 1 231 . 35 GLU HG3 H 2.298 0.02 1 232 . 36 ARG H H 6.943 0.004 1 233 . 36 ARG N N 115.371 0.02 1 234 . 36 ARG CA C 55.532 0.02 1 235 . 36 ARG HA H 4.219 0.02 1 236 . 36 ARG CB C 29.128 0.02 1 237 . 36 ARG HB3 H 1.794 0.02 1 238 . 36 ARG CG C 26.022 0.02 1 239 . 36 ARG HG3 H 1.665 0.02 1 240 . 36 ARG CD C 41.035 0.02 1 241 . 36 ARG HD3 H 2.796 0.02 1 242 . 37 PHE H H 8.184 0.006 1 243 . 37 PHE N N 121.643 0.02 1 244 . 37 PHE CA C 57.766 0.02 1 245 . 37 PHE HA H 4.237 0.02 1 246 . 37 PHE CB C 38.447 0.02 1 247 . 37 PHE HB3 H 2.992 0.02 1 248 . 37 PHE CD1 C 129.446 0.02 1 249 . 37 PHE HD1 H 7.181 0.02 3 250 . 37 PHE HE1 H 7.258 0.02 3 251 . 38 LYS H H 7.926 0.006 1 252 . 38 LYS N N 112.598 0.02 1 253 . 38 LYS CA C 55.532 0.02 1 254 . 38 LYS HA H 3.711 0.004 1 255 . 38 LYS CB C 30.163 0.02 1 256 . 38 LYS HB3 H 1.754 0.02 1 257 . 38 LYS CG C 21.88 0.02 1 258 . 38 LYS HG3 H 1.53 0.02 1 259 . 38 LYS HD3 H 1.178 0.005 1 260 . 38 LYS CE C 39.482 0.02 1 261 . 38 LYS HE3 H 2.897 0.02 1 262 . 39 GLN H H 7.26 0.007 1 263 . 39 GLN N N 115.38 0.02 1 264 . 39 GLN CA C 54.223 0.02 1 265 . 39 GLN HA H 4.072 0.008 1 266 . 39 GLN CB C 26.539 0.02 1 267 . 39 GLN HB3 H 1.978 0.02 1 268 . 39 GLN CG C 31.717 0.02 1 269 . 39 GLN HG3 H 2.315 0.006 1 270 . 39 GLN NE2 N 111.774 0.02 1 271 . 39 GLN HE21 H 7.353 0.003 1 272 . 39 GLN HE22 H 6.847 0.002 1 273 . 40 GLY H H 7.208 0.005 1 274 . 40 GLY N N 106.379 0.02 1 275 . 40 GLY CA C 42.589 0.02 1 276 . 40 GLY HA2 H 4.537 0.002 1 277 . 40 GLY HA3 H 3.715 0.02 1 278 . 41 THR H H 8.379 0.007 1 279 . 41 THR N N 111.121 0.02 1 280 . 41 THR CA C 61.582 0.02 1 281 . 41 THR HA H 3.815 0.02 1 282 . 41 THR CB C 65.886 0.02 1 283 . 41 THR HB H 4.292 0.02 1 284 . 41 THR CG2 C 20.427 0.02 1 285 . 41 THR HG2 H 1.129 0.002 1 286 . 42 SER H H 7.967 0.004 1 287 . 42 SER N N 113.573 0.02 1 288 . 42 SER CA C 55.532 0.02 1 289 . 42 SER HA H 4.505 0.004 1 290 . 42 SER CB C 60.709 0.02 1 291 . 42 SER HB3 H 3.796 0.003 1 292 . 43 LYS H H 7.178 0.008 1 293 . 43 LYS N N 121.409 0.02 1 294 . 43 LYS CA C 51.225 0.02 1 295 . 43 LYS HA H 4.199 0.02 1 296 . 43 LYS CB C 29.646 0.02 1 297 . 43 LYS HB3 H 1.512 0.02 1 298 . 43 LYS CG C 22.335 0.02 1 299 . 43 LYS HG3 H 1.144 0.02 1 300 . 43 LYS CD C 25.608 0.02 1 301 . 43 LYS HD3 H 1.335 0.02 1 302 . 43 LYS CE C 39.778 0.02 1 303 . 43 LYS HE3 H 2.685 0.02 1 304 . 44 LYS H H 8.592 0.01 1 305 . 44 LYS N N 122.437 0.02 1 306 . 44 LYS CA C 53.678 0.02 1 307 . 44 LYS HA H 3.751 0.003 1 308 . 44 LYS CB C 29.966 0.02 1 309 . 44 LYS HB3 H 1.435 0.001 1 310 . 44 LYS CG C 27.575 0.02 1 311 . 44 LYS HG3 H 1.337 0.02 1 312 . 44 LYS HD3 H 1.1 0.02 1 313 . 44 LYS HE3 H 2.775 0.02 1 314 . 45 CYS H H 8.12 0.007 1 315 . 45 CYS N N 116.784 0.02 1 316 . 45 CYS CA C 53.978 0.02 1 317 . 45 CYS HA H 4.941 0.02 1 318 . 45 CYS CB C 27.785 0.02 1 319 . 45 CYS HB3 H 2.524 0.002 1 320 . 46 ILE H H 8.733 0.003 1 321 . 46 ILE N N 125.495 0.02 1 322 . 46 ILE CA C 57.221 0.02 1 323 . 46 ILE HA H 5.237 0.001 1 324 . 46 ILE CB C 38.964 0.02 1 325 . 46 ILE HB H 1.184 0.005 1 326 . 46 ILE CG2 C 13.885 0.02 1 327 . 46 ILE CG1 C 26.695 0.02 1 328 . 46 ILE HG13 H 0.234 0.002 1 329 . 46 ILE CD1 C 12.043 0.02 1 330 . 46 ILE HD1 H 0.36 0.008 1 331 . 47 GLN H H 8.688 0.004 1 332 . 47 GLN N N 127.961 0.02 1 333 . 47 GLN CA C 49.837 0.02 1 334 . 47 GLN HA H 4.925 0.001 1 335 . 47 GLN CB C 27.785 0.02 1 336 . 47 GLN HB3 H -0.515 0.002 1 337 . 47 GLN CG C 31.199 0.02 1 338 . 47 GLN HG3 H 0.475 0.005 1 339 . 47 GLN NE2 N 110.49 0.02 1 340 . 47 GLN HE21 H 6.86 0.006 1 341 . 47 GLN HE22 H 6.111 0.008 1 342 . 48 SER H H 9.503 0.008 1 343 . 48 SER N N 123.954 0.02 1 344 . 48 SER CA C 55.532 0.02 1 345 . 48 SER HA H 4.833 0.001 1 346 . 48 SER CB C 62.78 0.02 1 347 . 48 SER HB3 H 4.023 0.02 1 348 . 49 GLU H H 8.768 0.005 1 349 . 49 GLU N N 121.997 0.02 1 350 . 49 GLU CA C 57.085 0.02 1 351 . 49 GLU HA H 3.999 0.02 1 352 . 49 GLU CB C 27.057 0.02 1 353 . 49 GLU HB3 H 2.001 0.02 1 354 . 49 GLU CG C 34.305 0.02 1 355 . 49 GLU HG3 H 2.219 0.02 1 356 . 50 ASP H H 7.969 0.003 1 357 . 50 ASP N N 115.5 0.02 1 358 . 50 ASP CA C 51.225 0.02 1 359 . 50 ASP HA H 4.576 0.02 1 360 . 50 ASP CB C 37.052 0.02 1 361 . 50 ASP HB3 H 2.63 0.002 1 362 . 51 LYS H H 7.826 0.005 1 363 . 51 LYS N N 110.508 0.02 1 364 . 51 LYS CA C 54.768 0.02 1 365 . 51 LYS HA H 3.471 0.005 1 366 . 51 LYS CB C 25.504 0.02 1 367 . 51 LYS HB3 H 1.778 0.008 1 368 . 51 LYS CG C 22.581 0.02 1 369 . 51 LYS HG3 H 1.069 0.02 1 370 . 51 LYS CD C 25.936 0.02 1 371 . 51 LYS HD3 H 1.477 0.02 1 372 . 51 LYS CE C 39.822 0.02 1 373 . 51 LYS HE3 H 2.875 0.02 1 374 . 52 LYS H H 7.176 0.008 1 375 . 52 LYS N N 120.382 0.02 1 376 . 52 LYS CA C 53.461 0.02 1 377 . 52 LYS HA H 4.237 0.002 1 378 . 52 LYS CB C 31.717 0.02 1 379 . 52 LYS HB3 H 1.38 0.02 1 380 . 52 LYS CG C 23.433 0.02 1 381 . 52 LYS HG3 H 1.043 0.02 1 382 . 52 LYS CD C 27.057 0.02 1 383 . 52 LYS HD3 H 1.535 0.02 1 384 . 52 LYS CE C 40.0 0.02 1 385 . 52 LYS HE3 H 2.826 0.02 1 386 . 53 TRP H H 8.238 0.005 1 387 . 53 TRP N N 119.508 0.02 1 388 . 53 TRP CA C 54.223 0.02 1 389 . 53 TRP HA H 5.267 0.002 1 390 . 53 TRP CB C 29.966 0.02 1 391 . 53 TRP HB3 H 2.768 0.001 1 392 . 53 TRP CD1 C 116.636 0.02 1 393 . 53 TRP HD1 H 7.023 0.058 1 394 . 53 TRP NE1 N 129.246 0.02 1 395 . 53 TRP HE1 H 9.884 0.005 1 396 . 53 TRP HE3 H 6.882 0.02 1 397 . 53 TRP CZ2 C 112.275 0.02 1 398 . 53 TRP CZ3 C 118.544 0.02 1 399 . 53 TRP CH2 C 122.087 0.02 1 400 . 53 TRP HH2 H 5.67 0.02 1 401 . 54 PHE H H 9.752 0.002 1 402 . 54 PHE N N 118.871 0.02 1 403 . 54 PHE CA C 55.04 0.02 1 404 . 54 PHE HA H 5.217 0.001 1 405 . 54 PHE CB C 42.231 0.02 1 406 . 54 PHE HB3 H 2.537 0.002 1 407 . 54 PHE CD1 C 129.446 0.02 1 408 . 54 PHE HD1 H 7.136 0.001 3 409 . 54 PHE HE1 H 7.323 0.02 3 410 . 55 THR H H 9.389 0.006 1 411 . 55 THR N N 115.871 0.02 1 412 . 55 THR CA C 58.311 0.02 1 413 . 55 THR HA H 4.951 0.02 1 414 . 55 THR CB C 65.368 0.02 1 415 . 55 THR HB H 4.537 0.002 1 416 . 55 THR CG2 C 19.291 0.02 1 417 . 55 THR HG2 H 0.98 0.003 1 418 . 56 PRO CA C 64.58 0.02 1 419 . 56 PRO HA H 3.799 0.02 1 420 . 56 PRO CB C 28.093 0.02 1 421 . 56 PRO HB3 H 0.333 0.02 1 422 . 56 PRO CG C 26.022 0.02 1 423 . 56 PRO HG3 H 1.073 0.02 1 424 . 56 PRO CD C 47.766 0.02 1 425 . 56 PRO HD3 H 3.67 0.02 1 426 . 57 ARG H H 8.116 0.002 1 427 . 57 ARG N N 116.142 0.02 1 428 . 57 ARG CA C 56.131 0.02 1 429 . 57 ARG HA H 4.101 0.005 1 430 . 57 ARG HB3 H 1.756 0.02 1 431 . 57 ARG HG3 H 1.552 0.02 1 432 . 57 ARG HD3 H 1.826 0.02 1 433 . 58 GLU H H 7.825 0.005 1 434 . 58 GLU N N 117.01 0.02 1 435 . 58 GLU CA C 56.567 0.02 1 436 . 58 GLU HA H 3.949 0.001 1 437 . 58 GLU CB C 28.331 0.02 1 438 . 58 GLU HB3 H 2.412 0.02 1 439 . 58 GLU CG C 34.823 0.02 1 440 . 58 GLU HG3 H 2.354 0.001 1 441 . 59 PHE H H 8.964 0.004 1 442 . 59 PHE N N 123.722 0.02 1 443 . 59 PHE CA C 58.856 0.02 1 444 . 59 PHE HA H 3.655 0.004 1 445 . 59 PHE CB C 37.411 0.02 1 446 . 59 PHE HB3 H 2.833 0.006 1 447 . 59 PHE CD1 C 128.628 0.02 1 448 . 59 PHE HD1 H 6.341 0.003 3 449 . 59 PHE CE1 C 128.335 0.02 1 450 . 59 PHE HE1 H 6.439 0.02 3 451 . 60 GLU H H 8.036 0.005 1 452 . 60 GLU N N 119.611 0.02 1 453 . 60 GLU CA C 56.403 0.02 1 454 . 60 GLU HA H 4.536 0.002 1 455 . 60 GLU CB C 28.093 0.02 1 456 . 60 GLU HB3 H 2.675 0.002 1 457 . 60 GLU CG C 35.858 0.02 1 458 . 60 GLU HG3 H 1.693 0.02 1 459 . 61 ILE H H 7.646 0.004 1 460 . 61 ILE N N 119.165 0.02 1 461 . 61 ILE CA C 62.78 0.02 1 462 . 61 ILE HA H 3.512 0.001 1 463 . 61 ILE CB C 36.234 0.02 1 464 . 61 ILE HB H 1.852 0.02 1 465 . 61 ILE CG2 C 14.632 0.02 1 466 . 61 ILE CG1 C 27.513 0.02 1 467 . 61 ILE HG13 H 0.877 0.02 1 468 . 61 ILE CD1 C 11.978 0.02 1 469 . 61 ILE HD1 H 0.797 0.004 1 470 . 62 GLU H H 7.97 0.006 1 471 . 62 GLU N N 123.85 0.02 1 472 . 62 GLU CA C 56.049 0.02 1 473 . 62 GLU HA H 3.924 0.001 1 474 . 62 GLU CB C 26.469 0.02 1 475 . 62 GLU HB3 H 1.384 0.02 1 476 . 62 GLU CG C 31.874 0.02 1 477 . 62 GLU HG3 H 1.76 0.02 1 478 . 63 GLY H H 7.709 0.004 1 479 . 63 GLY N N 103.295 0.02 1 480 . 63 GLY CA C 43.624 0.02 1 481 . 63 GLY HA2 H 3.825 0.001 1 482 . 63 GLY HA3 H 3.194 0.02 1 483 . 64 ASP H H 7.972 0.005 1 484 . 64 ASP N N 117.212 0.02 1 485 . 64 ASP CA C 52.315 0.02 1 486 . 64 ASP HA H 4.685 0.02 1 487 . 64 ASP CB C 38.142 0.02 1 488 . 64 ASP HB3 H 2.438 0.003 1 489 . 65 ARG H H 7.843 0.007 1 490 . 65 ARG N N 117.032 0.02 1 491 . 65 ARG CA C 52.587 0.02 1 492 . 65 ARG HA H 4.508 0.004 1 493 . 65 ARG CB C 26.539 0.02 1 494 . 65 ARG HB3 H 1.507 0.02 1 495 . 65 ARG CG C 24.986 0.02 1 496 . 65 ARG HG3 H 1.405 0.02 1 497 . 65 ARG CD C 40.518 0.02 1 498 . 65 ARG HD3 H 3.069 0.02 1 499 . 66 GLY H H 8.604 0.004 1 500 . 66 GLY N N 108.177 0.02 1 501 . 66 GLY CA C 44.142 0.02 1 502 . 66 GLY HA2 H 3.987 0.02 1 503 . 66 GLY HA3 H 3.487 0.02 1 504 . 67 ALA H H 8.298 0.006 1 505 . 67 ALA N N 121.649 0.02 1 506 . 67 ALA CA C 51.225 0.02 1 507 . 67 ALA HA H 4.096 0.02 1 508 . 67 ALA CB C 16.066 0.02 1 509 . 67 ALA HB H 1.265 0.02 1 510 . 68 SER H H 7.906 0.004 1 511 . 68 SER N N 113.958 0.02 1 512 . 68 SER CA C 57.766 0.02 1 513 . 68 SER HA H 3.975 0.02 1 514 . 68 SER CB C 60.709 0.02 1 515 . 68 SER HB3 H 3.705 0.02 1 516 . 69 LYS H H 7.476 0.017 1 517 . 69 LYS N N 112.417 0.02 1 518 . 69 LYS CA C 54.496 0.02 1 519 . 69 LYS HA H 3.95 0.02 1 520 . 69 LYS CB C 29.128 0.02 1 521 . 69 LYS HB3 H 1.572 0.004 1 522 . 69 LYS CG C 22.915 0.02 1 523 . 69 LYS HG3 H 1.214 0.02 1 524 . 69 LYS CD C 27.057 0.02 1 525 . 69 LYS HD3 H 1.544 0.02 1 526 . 69 LYS CE C 39.482 0.02 1 527 . 69 LYS HE3 H 2.852 0.02 1 528 . 70 ASN H H 10.443 0.003 1 529 . 70 ASN N N 119.449 0.02 1 530 . 70 ASN CA C 51.39 0.02 1 531 . 70 ASN HA H 4.454 0.005 1 532 . 70 ASN CB C 34.599 0.02 1 533 . 70 ASN HB3 H 2.65 0.02 1 534 . 70 ASN ND2 N 110.747 0.02 1 535 . 70 ASN HD21 H 7.598 0.007 1 536 . 70 ASN HD22 H 6.654 0.005 1 537 . 71 TRP H H 8.585 0.002 1 538 . 71 TRP N N 127.833 0.02 1 539 . 71 TRP CA C 57.602 0.02 1 540 . 71 TRP HA H 4.047 0.001 1 541 . 71 TRP CB C 25.878 0.02 1 542 . 71 TRP HB3 H 2.941 0.005 1 543 . 71 TRP CD1 C 126.72 0.02 1 544 . 71 TRP HD1 H 7.609 0.02 1 545 . 71 TRP NE1 N 130.659 0.02 1 546 . 71 TRP HE1 H 10.444 0.005 1 547 . 71 TRP CE3 C 119.089 0.02 1 548 . 71 TRP HE3 H 7.239 0.02 1 549 . 71 TRP CZ2 C 112.548 0.02 1 550 . 71 TRP CZ3 C 118.271 0.02 1 551 . 71 TRP CH2 C 120.724 0.02 1 552 . 71 TRP HH2 H 7.113 0.02 1 553 . 72 LYS H H 6.8 0.003 1 554 . 72 LYS N N 117.542 0.02 1 555 . 72 LYS CA C 56.567 0.02 1 556 . 72 LYS HA H 3.601 0.008 1 557 . 72 LYS CB C 29.646 0.02 1 558 . 72 LYS HB3 H 0.922 0.02 1 559 . 72 LYS CG C 21.517 0.02 1 560 . 72 LYS HG3 H -0.23 0.002 1 561 . 72 LYS CD C 27.24 0.02 1 562 . 72 LYS HD3 H 1.144 0.02 1 563 . 72 LYS CE C 39.232 0.02 1 564 . 72 LYS HE3 H 2.504 0.02 1 565 . 73 LEU H H 7.176 0.009 1 566 . 73 LEU N N 113.833 0.02 1 567 . 73 LEU CA C 52.042 0.02 1 568 . 73 LEU HA H 4.494 0.008 1 569 . 73 LEU CB C 40.868 0.02 1 570 . 73 LEU HB3 H 1.484 0.02 1 571 . 73 LEU CG C 24.986 0.02 1 572 . 73 LEU CD1 C 22.915 0.02 1 573 . 73 LEU HD1 H 0.784 0.009 1 574 . 73 LEU CD2 C 20.844 0.02 1 575 . 73 LEU HD2 H 0.757 0.02 1 576 . 73 LEU HG H 1.359 0.003 1 577 . 74 SER H H 8.134 0.005 1 578 . 74 SER N N 114.729 0.02 1 579 . 74 SER CA C 58.12 0.02 1 580 . 74 SER HA H 4.171 0.002 1 581 . 74 SER CB C 61.226 0.02 1 582 . 74 SER HB3 H 3.693 0.02 1 583 . 75 ILE H H 7.61 0.002 1 584 . 75 ILE N N 121.281 0.02 1 585 . 75 ILE CA C 58.856 0.02 1 586 . 75 ILE HA H 4.609 0.02 1 587 . 75 ILE CB C 35.341 0.02 1 588 . 75 ILE HB H 1.974 0.02 1 589 . 75 ILE CG2 C 15.521 0.02 1 590 . 75 ILE CG1 C 25.504 0.02 1 591 . 75 ILE HG13 H 2.267 0.001 1 592 . 75 ILE CD1 C 12.795 0.02 1 593 . 75 ILE HD1 H 1.263 0.02 1 594 . 76 ARG H H 8.718 0.006 1 595 . 76 ARG N N 123.231 0.02 1 596 . 76 ARG CA C 51.225 0.02 1 597 . 76 ARG HA H 5.171 0.001 1 598 . 76 ARG CB C 32.234 0.02 1 599 . 76 ARG HB3 H 1.216 0.02 1 600 . 76 ARG CG C 25.504 0.02 1 601 . 76 ARG HG3 H 1.118 0.002 1 602 . 76 ARG CD C 41.035 0.02 1 603 . 76 ARG HD3 H 2.742 0.02 1 604 . 77 CYS H H 9.403 0.004 1 605 . 77 CYS N N 120.399 0.02 1 606 . 77 CYS CA C 55.532 0.02 1 607 . 77 CYS HA H 4.769 0.002 1 608 . 77 CYS CB C 26.539 0.02 1 609 . 77 CYS HB3 H 2.461 0.02 1 610 . 78 GLY H H 9.429 0.005 1 611 . 78 GLY N N 117.812 0.02 1 612 . 78 GLY CA C 44.659 0.02 1 613 . 78 GLY HA2 H 4.017 0.001 1 614 . 78 GLY HA3 H 3.873 0.02 1 615 . 79 GLY H H 8.282 0.006 1 616 . 79 GLY N N 104.709 0.02 1 617 . 79 GLY CA C 42.231 0.02 1 618 . 79 GLY HA2 H 3.932 0.001 1 619 . 79 GLY HA3 H 3.447 0.02 1 620 . 80 TYR H H 7.83 0.005 1 621 . 80 TYR N N 120.767 0.02 1 622 . 80 TYR CA C 54.496 0.02 1 623 . 80 TYR HA H 4.802 0.02 1 624 . 80 TYR CB C 37.929 0.02 1 625 . 80 TYR HB3 H 2.805 0.002 1 626 . 80 TYR CD1 C 131.081 0.02 1 627 . 80 TYR HD1 H 7.112 0.02 1 628 . 80 TYR CE1 C 116.636 0.02 1 629 . 80 TYR HE1 H 6.774 0.02 1 630 . 81 THR H H 8.406 0.005 1 631 . 81 THR N N 111.774 0.02 1 632 . 81 THR CA C 59.401 0.02 1 633 . 81 THR HA H 4.368 0.005 1 634 . 81 THR CB C 66.921 0.02 1 635 . 81 THR HB H 5.193 0.002 1 636 . 81 THR CG2 C 20.154 0.02 1 637 . 81 THR HG2 H 1.408 0.003 1 638 . 82 LEU H H 8.0 0.004 1 639 . 82 LEU N N 118.965 0.02 1 640 . 82 LEU CA C 56.049 0.02 1 641 . 82 LEU HA H 3.95 0.02 1 642 . 82 LEU CB C 37.411 0.02 1 643 . 82 LEU HB3 H 1.304 0.02 1 644 . 82 LEU CG C 23.433 0.02 1 645 . 82 LEU CD1 C 23.433 0.02 1 646 . 82 LEU HD1 H 0.897 0.02 1 647 . 82 LEU CD2 C 18.774 0.02 1 648 . 82 LEU HD2 H 0.555 0.02 1 649 . 82 LEU HG H 1.923 0.02 1 650 . 83 LYS H H 8.614 0.009 1 651 . 83 LYS N N 117.684 0.02 1 652 . 83 LYS CA C 57.766 0.02 1 653 . 83 LYS HA H 3.736 0.004 1 654 . 83 LYS CB C 31.056 0.02 1 655 . 83 LYS HB3 H 1.387 0.02 1 656 . 83 LYS CG C 21.88 0.02 1 657 . 83 LYS HG3 H 1.19 0.02 1 658 . 83 LYS CD C 27.785 0.02 1 659 . 83 LYS HD3 H 1.445 0.02 1 660 . 83 LYS CE C 39.482 0.02 1 661 . 83 LYS HE3 H 2.782 0.02 1 662 . 84 VAL H H 7.483 0.003 1 663 . 84 VAL N N 119.611 0.02 1 664 . 84 VAL CA C 63.489 0.02 1 665 . 84 VAL HA H 3.73 0.02 1 666 . 84 VAL CB C 29.421 0.02 1 667 . 84 VAL HB H 2.168 0.02 1 668 . 84 VAL CG1 C 21.362 0.02 1 669 . 84 VAL HG1 H 1.019 0.004 1 670 . 84 VAL CG2 C 19.064 0.02 1 671 . 84 VAL HG2 H 0.815 0.003 1 672 . 85 LEU H H 7.644 0.003 1 673 . 85 LEU N N 121.152 0.02 1 674 . 85 LEU CA C 56.948 0.02 1 675 . 85 LEU HA H 3.903 0.002 1 676 . 85 LEU CB C 39.232 0.02 1 677 . 85 LEU HB3 H 1.194 0.002 1 678 . 85 LEU CG C 26.15 0.02 1 679 . 85 LEU CD1 C 23.433 0.02 1 680 . 85 LEU HD1 H 0.608 0.02 1 681 . 85 LEU CD2 C 21.362 0.02 1 682 . 85 LEU HD2 H 0.19 0.001 1 683 . 85 LEU HG H 1.491 0.001 1 684 . 86 MET H H 8.565 0.004 1 685 . 86 MET N N 119.316 0.02 1 686 . 86 MET CA C 56.567 0.02 1 687 . 86 MET HA H 4.513 0.001 1 688 . 86 MET CB C 30.681 0.02 1 689 . 86 MET HB3 H 2.523 0.02 1 690 . 86 MET CG C 30.722 0.02 1 691 . 86 MET HG3 H 2.041 0.001 1 692 . 86 MET CE C 14.976 0.02 1 693 . 86 MET HE H 2.148 0.02 1 694 . 87 GLU H H 8.411 0.003 1 695 . 87 GLU N N 122.694 0.02 1 696 . 87 GLU CA C 57.085 0.02 1 697 . 87 GLU HA H 3.923 0.02 1 698 . 87 GLU CB C 27.057 0.02 1 699 . 87 GLU HB3 H 1.898 0.002 1 700 . 87 GLU CG C 34.305 0.02 1 701 . 87 GLU HG3 H 2.194 0.02 1 702 . 88 ASN H H 7.579 0.004 1 703 . 88 ASN N N 114.316 0.02 1 704 . 88 ASN CA C 50.872 0.02 1 705 . 88 ASN HA H 4.486 0.02 1 706 . 88 ASN CB C 37.052 0.02 1 707 . 88 ASN HB3 H 2.305 0.007 1 708 . 88 ASN ND2 N 113.573 0.02 1 709 . 88 ASN HD21 H 7.146 0.008 1 710 . 88 ASN HD22 H 7.044 0.002 1 711 . 89 LYS H H 7.536 0.009 1 712 . 89 LYS N N 110.384 0.02 1 713 . 89 LYS CA C 55.313 0.02 1 714 . 89 LYS HA H 3.877 0.02 1 715 . 89 LYS CB C 25.566 0.02 1 716 . 89 LYS HB3 H 1.828 0.02 1 717 . 89 LYS CG C 22.523 0.02 1 718 . 89 LYS HG3 H 1.145 0.02 1 719 . 89 LYS CD C 26.539 0.02 1 720 . 89 LYS HD3 H 1.583 0.02 1 721 . 89 LYS HE3 H 2.832 0.02 1 722 . 90 PHE H H 8.135 0.004 1 723 . 90 PHE N N 117.17 0.02 1 724 . 90 PHE CA C 56.403 0.02 1 725 . 90 PHE HA H 4.486 0.001 1 726 . 90 PHE CB C 37.411 0.02 1 727 . 90 PHE HB3 H 2.415 0.02 1 728 . 90 PHE CD1 C 128.628 0.02 1 729 . 90 PHE HD1 H 6.827 0.02 3 730 . 90 PHE HE1 H 7.118 0.02 3 731 . 91 LEU H H 6.912 0.003 1 732 . 91 LEU N N 116.528 0.02 1 733 . 91 LEU CA C 48.499 0.02 1 734 . 91 LEU HA H 4.696 0.02 1 735 . 91 LEU CB C 43.624 0.02 1 736 . 91 LEU HB3 H 1.048 0.02 1 737 . 91 LEU CG C 24.469 0.02 1 738 . 91 LEU CD1 C 22.915 0.02 1 739 . 91 LEU HD1 H 0.556 0.02 1 740 . 91 LEU HG H 1.445 0.02 1 741 . 92 PRO HB3 H 1.782 0.02 1 742 . 92 PRO HG3 H 1.968 0.02 1 743 . 92 PRO HD3 H 3.564 0.02 1 744 . 93 GLU H H 8.123 0.004 1 745 . 93 GLU N N 119.381 0.02 1 746 . 93 GLU CA C 51.225 0.02 1 747 . 93 GLU HA H 4.707 0.02 1 748 . 93 GLU CB C 28.093 0.02 1 749 . 93 GLU HB3 H 1.793 0.02 1 750 . 93 GLU CG C 33.787 0.02 1 751 . 93 GLU HG3 H 2.218 0.02 1 752 . 95 PRO HA H 4.398 0.02 1 753 . 95 PRO HB3 H 1.89 0.02 1 754 . 96 SER H H 8.462 0.004 1 755 . 96 SER N N 116.142 0.02 1 756 . 96 SER CA C 55.532 0.02 1 757 . 96 SER HA H 4.535 0.02 1 758 . 96 SER CB C 61.582 0.02 1 759 . 96 SER HB3 H 3.782 0.02 1 760 . 97 THR H H 8.235 0.005 1 761 . 97 THR N N 116.656 0.02 1 762 . 97 THR CA C 59.673 0.02 1 763 . 97 THR HA H 4.291 0.02 1 764 . 97 THR CB C 67.439 0.02 1 765 . 97 THR HB H 4.144 0.02 1 766 . 97 THR CG2 C 19.291 0.02 1 767 . 97 THR HG2 H 1.089 0.02 1 768 . 98 ARG H H 8.301 0.009 1 769 . 98 ARG N N 123.612 0.02 1 770 . 98 ARG HA H 4.246 0.02 1 771 . 98 ARG HB3 H 1.675 0.02 1 772 . 99 LYS HA H 4.184 0.02 1 773 . 99 LYS HB3 H 1.647 0.02 1 774 . 100 LYS H H 8.347 0.006 1 775 . 100 LYS N N 123.887 0.02 1 776 . 100 LYS CA C 53.978 0.02 1 777 . 100 LYS HA H 4.229 0.02 1 778 . 100 LYS HG3 H 1.319 0.001 1 779 . 101 VAL H H 8.216 0.005 1 780 . 101 VAL N N 122.694 0.02 1 781 . 101 VAL CA C 59.673 0.02 1 782 . 101 VAL HA H 4.081 0.02 1 783 . 101 VAL CB C 30.681 0.02 1 784 . 101 VAL HB H 1.963 0.02 1 785 . 101 VAL CG1 C 18.256 0.02 1 786 . 101 VAL HG1 H 0.848 0.001 1 787 . 102 THR H H 8.237 0.009 1 788 . 102 THR N N 119.596 0.02 1 789 . 102 THR CA C 59.673 0.02 1 790 . 102 THR HA H 4.242 0.02 1 791 . 102 THR CB C 67.439 0.02 1 792 . 102 THR HB H 3.975 0.02 1 793 . 102 THR CG2 C 19.291 0.02 1 794 . 102 THR HG2 H 1.046 0.02 1 795 . 103 ILE H H 8.201 0.009 1 796 . 103 ILE N N 124.701 0.02 1 797 . 103 ILE CA C 58.638 0.02 1 798 . 103 ILE HA H 4.038 0.02 1 799 . 103 ILE CB C 36.376 0.02 1 800 . 103 ILE HB H 1.777 0.003 1 801 . 103 ILE CG2 C 15.15 0.02 1 802 . 103 ILE CG1 C 24.986 0.02 1 803 . 103 ILE HG13 H 1.069 0.02 1 804 . 103 ILE CD1 C 9.972 0.02 1 805 . 103 ILE HD1 H 0.705 0.02 1 806 . 104 LYS H H 7.871 0.001 1 807 . 104 LYS N N 130.372 0.02 1 808 . 104 LYS CA C 55.532 0.02 1 809 . 104 LYS HA H 3.998 0.02 1 810 . 104 LYS HB3 H 1.682 0.02 1 811 . 104 LYS CG C 22.398 0.02 1 812 . 104 LYS HG3 H 1.261 0.02 1 813 . 104 LYS CD C 26.539 0.02 1 814 . 104 LYS HD3 H 1.602 0.02 1 815 . 104 LYS CE C 39.482 0.02 1 816 . 104 LYS HE3 H 2.836 0.02 1 stop_ save_ ######################## # Coupling constants # ######################## save_J_values_set_1 _Saveframe_category coupling_constants _Details ; Add 584 to the given residue number to get the wild-type residue number as given in the PDB structure file 1H5P. ; loop_ _Sample_label $Sample_1 $Sample_2 stop_ _Sample_conditions_label $Sample_condition_1 _Spectrometer_frequency_1H 500 _Mol_system_component_name 'Sp100b SAND domain' _Text_data_format . _Text_data . loop_ _Coupling_constant_ID _Coupling_constant_code _Atom_one_residue_seq_code _Atom_one_residue_label _Atom_one_name _Atom_two_residue_seq_code _Atom_two_residue_label _Atom_two_name _Coupling_constant_value _Coupling_constant_min_value _Coupling_constant_max_value _Coupling_constant_value_error 1 3JHNHA 20 GLU H 20 GLU HA 10.57 . . 1 2 3JHNHA 23 VAL H 23 VAL HA 11.48 . . 1 3 3JHNHA 24 THR H 24 THR HA 10.28 . . 1 4 3JHNHA 29 LYS H 29 LYS HA 9.83 . . 1 5 3JHNHA 31 THR H 31 THR HA 11.03 . . 1 6 3JHNHA 32 LEU H 32 LEU HA 8.70 . . 1 7 3JHNHA 33 TYR H 33 TYR HA 9.92 . . 1 8 3JHNHA 45 CYS H 45 CYS HA 9.22 . . 1 9 3JHNHA 46 ILE H 46 ILE HA 10.16 . . 1 10 3JHNHA 47 GLN H 47 GLN HA 10.51 . . 1 11 3JHNHA 51 LYS H 51 LYS HA 8.54 . . 1 12 3JHNHA 52 LYS H 52 LYS HA 9.68 . . 1 13 3JHNHA 53 TRP H 53 TRP HA 9.77 . . 1 14 3JHNHA 54 PHE H 54 PHE HA 10.24 . . 1 15 3JHNHA 55 THR H 55 THR HA 8.05 . . 1 16 3JHNHA 57 ARG H 57 ARG HA 4.81 . . 1 17 3JHNHA 59 PHE H 59 PHE HA 5.64 . . 1 18 3JHNHA 60 GLU H 60 GLU HA 4.56 . . 1 19 3JHNHA 61 ILE H 61 ILE HA 5.61 . . 1 20 3JHNHA 62 GLU H 62 GLU HA 5.32 . . 1 21 3JHNHA 70 ASN H 70 ASN HA 4.67 . . 1 22 3JHNHA 71 TRP H 71 TRP HA 2.43 . . 1 23 3JHNHA 72 LYS H 72 LYS HA 5.90 . . 1 24 3JHNHA 76 ARG H 76 ARG HA 10.62 . . 1 25 3JHNHA 77 CYS H 77 CYS HA 9.67 . . 1 26 3JHNHA 82 LEU H 82 LEU HA 4.34 . . 1 27 3JHNHA 83 LYS H 83 LYS HA 2.74 . . 1 28 3JHNHA 84 VAL H 84 VAL HA 6.65 . . 1 29 3JHNHA 86 MET H 86 MET HA 5.92 . . 1 30 3JHNHA 87 GLU H 87 GLU HA 5.15 . . 1 stop_ save_