data_5592 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Backbone resonance assignments for the human GMEB-1 SAND domain ; _BMRB_accession_number 5592 _BMRB_flat_file_name bmr5592.str _Entry_type update _Submission_date 2002-11-18 _Accession_date 2002-11-18 _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 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" 192 "13C chemical shifts" 270 "15N chemical shifts" 92 "coupling constants" 33 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2003-03-19 update author 'addition of PDB code' 2003-03-18 original author 'original release' stop_ save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; Letter to the Editor: 1H, 13C and 15N resonance assignments of the SAND domains from glucocorticoid modulatory element binding proteins-1 and -2 ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID ? loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Bottomley Matthew J. . 2 Sattler Michael . . stop_ _Journal_abbreviation 'J. Biomol. NMR' _Journal_volume 25 _Journal_issue 3 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 259 _Page_last 260 _Year 2003 _Details . loop_ _Keyword 'SAND domain' GMEB1 'KDWK motif' 'transcriptional regulation' 'glucocorticoid response' stop_ save_ ################################## # Molecular system description # ################################## save_system_GMEB1_SAND _Saveframe_category molecular_system _Mol_system_name 'human GMEB1 extended SAND domain' _Abbreviation_common 'GMEB1 SAND' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'Human GMEB1 extended SAND domain' $GMEB1_SAND 'ZINC (II) ION' $ZN stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state monomer _System_paramagnetic no _System_thiol_state 'other bound and free' loop_ _Biological_function 'DNA-binding domain' 'zinc-binding domain' 'Interacts with glucocorticoid receptor' stop_ _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_GMEB1_SAND _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'SAND domain from human GMEB1 protein' _Abbreviation_common 'GMEB1 SAND' _Molecular_mass 11022 _Mol_thiol_state 'other bound and free' _Details ; There is a tripeptide N-terminal tag (GAM) followed by 94 residues of the human GMEB1 protein, residues Glu 89 to Lys 182. Theoretical pI=9.35. The protein sequence given should be numbered according to its occurrence in the wild-type protein. Thus the first residue (G) should be numbered 86, and the last residue (K) 182. Nevertheless, it should be noted that the first three residues (GAM) are derived from an N-terminal tag. ; ############################## # Polymer residue sequence # ############################## _Residue_count 97 _Mol_residue_sequence ; GAMEDMEIAYPITCGESKAI LLWKKFVCPGINVKCVKFND QLISPKHFVHLAGKSTLKDW KRAIRLGGIMLRKMMDSGQI DFYQHDKVCSNTCRSTK ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 86 GLY 2 87 ALA 3 88 MET 4 89 GLU 5 90 ASP 6 91 MET 7 92 GLU 8 93 ILE 9 94 ALA 10 95 TYR 11 96 PRO 12 97 ILE 13 98 THR 14 99 CYS 15 100 GLY 16 101 GLU 17 102 SER 18 103 LYS 19 104 ALA 20 105 ILE 21 106 LEU 22 107 LEU 23 108 TRP 24 109 LYS 25 110 LYS 26 111 PHE 27 112 VAL 28 113 CYS 29 114 PRO 30 115 GLY 31 116 ILE 32 117 ASN 33 118 VAL 34 119 LYS 35 120 CYS 36 121 VAL 37 122 LYS 38 123 PHE 39 124 ASN 40 125 ASP 41 126 GLN 42 127 LEU 43 128 ILE 44 129 SER 45 130 PRO 46 131 LYS 47 132 HIS 48 133 PHE 49 134 VAL 50 135 HIS 51 136 LEU 52 137 ALA 53 138 GLY 54 139 LYS 55 140 SER 56 141 THR 57 142 LEU 58 143 LYS 59 144 ASP 60 145 TRP 61 146 LYS 62 147 ARG 63 148 ALA 64 149 ILE 65 150 ARG 66 151 LEU 67 152 GLY 68 153 GLY 69 154 ILE 70 155 MET 71 156 LEU 72 157 ARG 73 158 LYS 74 159 MET 75 160 MET 76 161 ASP 77 162 SER 78 163 GLY 79 164 GLN 80 165 ILE 81 166 ASP 82 167 PHE 83 168 TYR 84 169 GLN 85 170 HIS 86 171 ASP 87 172 LYS 88 173 VAL 89 174 CYS 90 175 SER 91 176 ASN 92 177 THR 93 178 CYS 94 179 ARG 95 180 SER 96 181 THR 97 182 LYS 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 Q9JL60 'Glucocorticoid modulatory element-binding protein 1 (GMEB-1)' 96.91 562 98.94 100.00 2.37e-53 SWISS-PROT Q9Y692 'Glucocorticoid modulatory element-binding protein 1 (GMEB-1) (Parvovirus initiation factor p96) (PIF p96) (DNA-binding protein p96PIF)' 98.97 573 98.96 98.96 9.23e-54 REF NP_077808 'glucocorticoid modulatory element binding protein 1 isoform 2 [Homo sapiens]' 98.97 563 98.96 98.96 9.23e-54 SWISS-PROT Q2HJ87 'Glucocorticoid modulatory element-binding protein 1 (GMEB-1)' 98.97 563 98.96 98.96 9.23e-54 REF NP_006573 'glucocorticoid modulatory element binding protein 1 isoform 1 [Homo sapiens]' 98.97 573 98.96 98.96 9.23e-54 REF NP_064669 'glucocorticoid modulatory element binding protein 1 [Mus musculus]' 96.91 562 98.94 100.00 2.37e-53 REF NP_001039940 'glucocorticoid modulatory element binding protein 1 [Bos taurus]' 98.97 563 98.96 98.96 9.23e-54 REF NP_001116464 'glucocorticoid modulatory element binding protein 1 [Mus musculus]' 96.91 562 98.94 100.00 2.37e-53 GenBank AAG01189 'glucocorticoid modulatory element binding protein 1 [Homo sapiens]' 98.97 563 98.96 98.96 9.23e-54 GenBank AAH01473 'Glucocorticoid modulatory element binding protein 1 [Homo sapiens]' 98.97 563 98.96 98.96 9.23e-54 GenBank AAD51352 'DNA binding protein p96PIF [Homo sapiens]' 98.97 563 98.96 98.96 9.23e-54 GenBank AAF72874 'glucocorticoid modulatory element binding protein 1; GMEB-1 [Mus musculus]' 96.91 562 98.94 100.00 2.37e-53 EMBL CAM14478 'glucocorticoid modulatory element binding protein 1 [Mus musculus]' 96.91 562 98.94 100.00 2.37e-53 GenBank AAD39355 'glucocorticoid modulatory element binding protein-1 [Homo sapiens]' 98.97 573 98.96 98.96 9.23e-54 EMBL CAH72427 'glucocorticoid modulatory element binding protein 1 [Homo sapiens]' 98.97 573 98.96 98.96 9.23e-54 EMBL CAH72428 'glucocorticoid modulatory element binding protein 1 [Homo sapiens]' 98.97 563 98.96 98.96 9.23e-54 DBJ BAG37824 'unnamed protein product [Homo sapiens]' 98.97 563 98.96 98.96 9.23e-54 EMBL CAH72426 'glucocorticoid modulatory element binding protein 1 [Homo sapiens]' 98.97 360 98.96 98.96 9.23e-54 DBJ BAE22107 'unnamed protein product [Mus musculus]' 96.91 563 98.94 100.00 2.37e-53 DBJ BAG37635 'unnamed protein product [Homo sapiens]' 98.97 573 98.96 98.96 9.23e-54 PDB 1OQJ 'Crystal Structure Of The Sand Domain From Glucocorticoid Modulatory Element Binding Protein-1 (Gmeb1)' 100.00 97 100.00 100.00 2.31e-51 DBJ BAA91410 'unnamed protein product [Homo sapiens]' 98.97 563 98.96 98.96 9.23e-54 stop_ save_ ############# # Ligands # ############# save_ZN _Saveframe_category ligand _Mol_type non-polymer _Name_common "ZN (ZINC ION)" _BMRB_code . _PDB_code ZN _Molecular_mass 65.409 _Mol_charge 2 _Mol_paramagnetic . _Mol_aromatic no _Details ; Information obtained from PDB's Chemical Component Dictionary at http://wwpdb-remediation.rutgers.edu/downloads.html Downloaded on Thu Jun 2 09:48:05 2011 ; loop_ _Atom_name _PDB_atom_name _Atom_type _Atom_chirality _Atom_charge _Atom_oxidation_number _Atom_unpaired_electrons ZN ZN ZN . 2 . ? stop_ _Mol_thiol_state . _Sequence_homology_query_date . save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $GMEB1_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 _Variant _Vector_type _Vector_name _Details $GMEB1_SAND 'recombinant technology' 'E. coli' Escherichia coli BL21 DE3 plasmid 'Modified pET-24d' ; Protein was expressed from an in-house modified pET-24d vector (originally supplied by NOVAGEN) in E. coli induced with IPTG at 23 degrees C for 12 hours. ; 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 _Concentration_min_value _Concentration_max_value _Isotopic_labeling $GMEB1_SAND 1.0 mM 0.8 1.2 '[U-98% 15N]' 'sodium phosphate' 20 mM . . . NaCl 0.2 M . . . DTT 3 mM . . . H2O 90 % . . . D2O 10 % . . . stop_ save_ save_Sample_2 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Concentration_min_value _Concentration_max_value _Isotopic_labeling $GMEB1_SAND 1.0 mM 0.8 1.2 '[U-98% 13C; U-98% 15N]' 'sodium phosphate' 20 mM . . . NaCl 0.2 M . . . DTT 3 mM . . . H2O 90 % . . . D2O 10 % . . . stop_ save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model DRX _Field_strength 500 _Details . save_ save_spectrometer_2 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model DRX _Field_strength 600 _Details . save_ ############################# # NMR applied experiments # ############################# save_2D_1H-15N_HSQC_1 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-15N HSQC' _Sample_label . save_ save_3D_HNCO_2 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCO' _Sample_label . save_ save_3D_HNCA_3 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCA' _Sample_label . save_ save_3D_HNHA_4 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNHA' _Sample_label . save_ save_3D_CBCANH_5 _Saveframe_category NMR_applied_experiment _Experiment_name '3D CBCANH' _Sample_label . save_ save_3D_CBCA(CO)NH_6 _Saveframe_category NMR_applied_experiment _Experiment_name '3D CBCA(CO)NH' _Sample_label . save_ save_3D_1H-1H-15N_NOESY_7 _Saveframe_category NMR_applied_experiment _Experiment_name '3D 1H-1H-15N NOESY' _Sample_label . save_ save_NMR_spec_expt__0_1 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-15N HSQC' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_2 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCO' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_3 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCA' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_4 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNHA' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_5 _Saveframe_category NMR_applied_experiment _Experiment_name '3D CBCANH' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_6 _Saveframe_category NMR_applied_experiment _Experiment_name '3D CBCA(CO)NH' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_7 _Saveframe_category NMR_applied_experiment _Experiment_name '3D 1H-1H-15N NOESY' _BMRB_pulse_sequence_accession_number . _Details . save_ ####################### # Sample conditions # ####################### save_condition_1 _Saveframe_category sample_conditions _Details ; Samples were also stored under either nitrogen or argon gas in order to limit oxidation of the numerous Cys residues (important in zinc-binding). ; loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 6.0 0.2 pH temperature 300 1.0 K 'ionic strength' 0.22 0.02 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 _Indirect_shift_ratio_citation_label _Correction_value_citation_label TSP H 1 'methyl protons' ppm 0.0 internal direct . internal . 1.0 $entry_citation $entry_citation TSP N 15 'methyl protons' ppm 0.0 external indirect . external . 0.101329118 $entry_citation $entry_citation TSP C 13 'methyl protons' ppm 0.0 external indirect . external . 0.251449530 $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_CSR_1 _Saveframe_category assigned_chemical_shifts _Details ; The first three N-terminal residues, GAM, were not derived from GMEB1 but from the linker resulting from cleavage of the N-terminal Histag. Signals for some residues, mostly occuring in flexible loops or solvent-exposed regions, were not observed in the NMR spectra and so no chemical shift information is given for these residues. ; loop_ _Sample_label $Sample_1 $Sample_2 stop_ _Sample_conditions_label $condition_1 _Chem_shift_reference_set_label $chemical_shift_reference _Mol_system_component_name 'Human GMEB1 extended 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 86 1 GLY H H 7.261 0.02 1 2 86 1 GLY N N 110.07 0.06 1 3 86 1 GLY CA C 40.95 0.14 1 4 86 1 GLY HA2 H 3.22 0.02 1 5 86 1 GLY C C 171.35 0.14 1 6 87 2 ALA H H 8.812 0.02 1 7 87 2 ALA N N 124.148 0.06 1 8 87 2 ALA CA C 50.95 0.14 1 9 87 2 ALA HA H 4.33 0.02 1 10 87 2 ALA C C 174.58 0.14 1 11 87 2 ALA CB C 16.96 0.14 1 12 88 3 MET H H 8.721 0.02 1 13 88 3 MET N N 118.663 0.06 1 14 88 3 MET CA C 54.14 0.14 1 15 88 3 MET HA H 4.37 0.02 1 16 88 3 MET C C 174.71 0.14 1 17 88 3 MET CB C 29.96 0.14 1 18 89 4 GLU H H 8.463 0.02 1 19 89 4 GLU N N 120.537 0.06 1 20 89 4 GLU CA C 55.4 0.14 1 21 89 4 GLU HA H 4.21 0.02 1 22 89 4 GLU C C 174.29 0.14 1 23 89 4 GLU CB C 27.33 0.14 1 24 90 5 ASP H H 8.234 0.02 1 25 90 5 ASP N N 119.961 0.06 1 26 90 5 ASP CA C 52.19 0.14 1 27 90 5 ASP HA H 4.57 0.02 1 28 90 5 ASP C C 173.79 0.14 1 29 90 5 ASP CB C 38.62 0.14 1 30 91 6 MET H H 7.895 0.02 1 31 91 6 MET N N 119.6 0.06 1 32 91 6 MET CA C 53.53 0.14 1 33 91 6 MET HA H 4.51 0.02 1 34 91 6 MET CB C 31.62 0.14 1 35 92 7 GLU HA H 4.3 0.02 1 36 92 7 GLU C C 177.84 0.14 1 37 93 8 ILE H H 8.775 0.02 1 38 93 8 ILE N N 122.804 0.06 1 39 93 8 ILE CA C 55.06 0.14 1 40 93 8 ILE HA H 4.41 0.02 1 41 93 8 ILE C C 175.63 0.14 1 42 93 8 ILE CB C 37.66 0.14 1 43 94 9 ALA H H 7.764 0.02 1 44 94 9 ALA N N 110.46 0.06 1 45 94 9 ALA CA C 40.67 0.14 1 46 94 9 ALA HA H 4.53 0.02 1 47 94 9 ALA CB C 23.84 0.14 1 48 95 10 TYR HA H 4.7 0.02 1 49 96 11 PRO CA C 60.69 0.14 1 50 96 11 PRO HA H 4.59 0.02 1 51 96 11 PRO C C 174.56 0.14 1 52 96 11 PRO CB C 29.2 0.14 1 53 97 12 ILE H H 8.678 0.02 1 54 97 12 ILE N N 117.913 0.06 1 55 97 12 ILE CA C 56.81 0.14 1 56 97 12 ILE HA H 5.63 0.02 1 57 97 12 ILE C C 173.4 0.14 1 58 97 12 ILE CB C 40.88 0.14 1 59 98 13 THR H H 9.357 0.02 1 60 98 13 THR N N 111.18 0.06 1 61 98 13 THR CA C 57.33 0.14 1 62 98 13 THR HA H 5.54 0.02 1 63 98 13 THR C C 171.8 0.14 1 64 98 13 THR CB C 70.56 0.14 1 65 99 14 CYS H H 8.278 0.02 1 66 99 14 CYS N N 120.343 0.06 1 67 99 14 CYS CA C 57.34 0.14 1 68 99 14 CYS HA H 4.45 0.02 1 69 99 14 CYS C C 174.13 0.14 1 70 99 14 CYS CB C 25.78 0.14 1 71 100 15 GLY H H 9.19 0.02 1 72 100 15 GLY N N 118.844 0.06 1 73 100 15 GLY CA C 44.97 0.14 1 74 100 15 GLY HA2 H 3.8 0.02 1 75 100 15 GLY HA3 H 4.0 0.02 1 76 100 15 GLY C C 169.81 0.14 1 77 101 16 GLU H H 8.984 0.02 1 78 101 16 GLU N N 127.07 0.06 1 79 101 16 GLU CA C 54.01 0.14 1 80 101 16 GLU HA H 4.45 0.02 1 81 101 16 GLU C C 174.31 0.14 1 82 101 16 GLU CB C 27.54 0.14 1 83 102 17 SER H H 8.483 0.02 1 84 102 17 SER N N 117.9 0.06 1 85 102 17 SER CA C 57.6 0.14 1 86 102 17 SER HA H 4.84 0.02 1 87 102 17 SER C C 170.5 0.14 1 88 102 17 SER CB C 62.46 0.14 1 89 103 18 LYS H H 9.0 0.02 1 90 103 18 LYS N N 124.38 0.06 1 91 103 18 LYS CA C 53.24 0.14 1 92 103 18 LYS HA H 5.21 0.02 1 93 103 18 LYS C C 172.21 0.14 1 94 103 18 LYS CB C 32.83 0.14 1 95 104 19 ALA H H 8.88 0.02 1 96 104 19 ALA N N 122.829 0.06 1 97 104 19 ALA CA C 48.59 0.14 1 98 104 19 ALA HA H 4.81 0.02 1 99 104 19 ALA C C 172.09 0.14 1 100 104 19 ALA CB C 21.46 0.14 1 101 105 20 ILE H H 7.772 0.02 1 102 105 20 ILE N N 116.492 0.06 1 103 105 20 ILE CA C 57.12 0.14 1 104 105 20 ILE HA H 4.93 0.02 1 105 105 20 ILE C C 171.6 0.14 1 106 105 20 ILE CB C 39.62 0.14 1 107 106 21 LEU H H 9.588 0.02 1 108 106 21 LEU N N 128.541 0.06 1 109 106 21 LEU CA C 51.63 0.14 1 110 106 21 LEU HA H 4.69 0.02 1 111 106 21 LEU C C 172.71 0.14 1 112 106 21 LEU CB C 42.49 0.14 1 113 107 22 LEU H H 9.052 0.02 1 114 107 22 LEU N N 129.332 0.06 1 115 107 22 LEU CA C 51.5 0.14 1 116 107 22 LEU HA H 4.62 0.02 1 117 107 22 LEU C C 172.2 0.14 1 118 107 22 LEU CB C 16.38 0.14 1 119 108 23 TRP H H 8.784 0.02 1 120 108 23 TRP N N 118.613 0.06 1 121 108 23 TRP CA C 53.52 0.14 1 122 108 23 TRP HA H 4.45 0.02 1 123 108 23 TRP C C 173.48 0.14 1 124 108 23 TRP CB C 24.08 0.14 1 125 108 23 TRP NE1 N 130.670 0.06 1 126 108 23 TRP HE1 H 11.074 0.02 1 127 109 24 LYS H H 8.569 0.02 1 128 109 24 LYS N N 121.678 0.06 1 129 109 24 LYS CA C 54.77 0.14 1 130 109 24 LYS HA H 4.24 0.02 1 131 109 24 LYS C C 173.29 0.14 1 132 109 24 LYS CB C 27.56 0.14 1 133 110 25 LYS H H 7.228 0.02 1 134 110 25 LYS N N 112.334 0.06 1 135 110 25 LYS CA C 52.69 0.14 1 136 110 25 LYS HA H 4.29 0.02 1 137 110 25 LYS C C 174.36 0.14 1 138 110 25 LYS CB C 31.53 0.14 1 139 111 26 PHE H H 8.083 0.02 1 140 111 26 PHE N N 126.756 0.06 1 141 111 26 PHE CA C 53.15 0.14 1 142 111 26 PHE HA H 4.9 0.02 1 143 111 26 PHE C C 170.22 0.14 1 144 111 26 PHE CB C 35.94 0.14 1 145 112 27 VAL H H 7.31 0.02 1 146 112 27 VAL N N 120.502 0.06 1 147 112 27 VAL CA C 57.42 0.14 1 148 112 27 VAL HA H 4.2 0.02 1 149 112 27 VAL C C 171.3 0.14 1 150 112 27 VAL CB C 31.36 0.14 1 151 113 28 CYS H H 8.785 0.02 1 152 113 28 CYS N N 126.78 0.06 1 153 113 28 CYS CA C 54.54 0.14 1 154 113 28 CYS HA H 4.74 0.02 1 155 113 28 CYS CB C 26.58 0.14 1 156 114 29 PRO CA C 62.65 0.14 1 157 114 29 PRO HA H 5.27 0.02 1 158 114 29 PRO C C 175.96 0.14 1 159 114 29 PRO CB C 30.22 0.14 1 160 115 30 GLY H H 9.108 0.02 1 161 115 30 GLY N N 118.357 0.06 1 162 115 30 GLY CA C 47.08 0.14 1 163 115 30 GLY HA2 H 3.24 0.02 1 164 115 30 GLY HA3 H 4.22 0.02 1 165 115 30 GLY C C 172.64 0.14 1 166 116 31 ILE H H 7.522 0.02 1 167 116 31 ILE N N 121.479 0.06 1 168 116 31 ILE CA C 62.13 0.14 1 169 116 31 ILE HA H 4.25 0.02 1 170 116 31 ILE C C 170.17 0.14 1 171 116 31 ILE CB C 36.41 0.14 1 172 117 32 ASN H H 7.776 0.02 1 173 117 32 ASN N N 114.57 0.06 1 174 117 32 ASN CA C 49.6 0.14 1 175 117 32 ASN HA H 5.02 0.02 1 176 117 32 ASN C C 172.55 0.14 1 177 117 32 ASN CB C 36.62 0.14 1 178 118 33 VAL H H 7.353 0.02 1 179 118 33 VAL N N 122.098 0.06 1 180 118 33 VAL CA C 58.98 0.14 1 181 118 33 VAL HA H 3.96 0.02 1 182 118 33 VAL C C 173.75 0.14 1 183 118 33 VAL CB C 30.68 0.14 1 184 119 34 LYS H H 8.872 0.02 1 185 119 34 LYS N N 125.493 0.06 1 186 119 34 LYS CA C 54.64 0.14 1 187 119 34 LYS HA H 3.84 0.02 1 188 119 34 LYS C C 171.82 0.14 1 189 119 34 LYS CB C 27.66 0.14 1 190 120 35 CYS H H 7.816 0.02 1 191 120 35 CYS N N 118.448 0.06 1 192 120 35 CYS CA C 54.29 0.14 1 193 120 35 CYS HA H 4.73 0.02 1 194 120 35 CYS C C 168.39 0.14 1 195 120 35 CYS CB C 26.75 0.14 1 196 121 36 VAL H H 9.123 0.02 1 197 121 36 VAL N N 125.241 0.06 1 198 121 36 VAL CA C 58.56 0.14 1 199 121 36 VAL HA H 4.86 0.02 1 200 121 36 VAL C C 171.85 0.14 1 201 121 36 VAL CB C 30.41 0.14 1 202 122 37 LYS H H 9.382 0.02 1 203 122 37 LYS N N 128.736 0.06 1 204 122 37 LYS CA C 52.38 0.14 1 205 122 37 LYS HA H 5.18 0.02 1 206 122 37 LYS C C 173.41 0.14 1 207 122 37 LYS CB C 30.89 0.14 1 208 123 38 PHE H H 9.15 0.02 1 209 123 38 PHE N N 130.795 0.06 1 210 123 38 PHE CA C 53.44 0.14 1 211 123 38 PHE HA H 4.98 0.02 1 212 123 38 PHE C C 172.03 0.14 1 213 123 38 PHE CB C 40.04 0.14 1 214 124 39 ASN H H 9.24 0.02 1 215 124 39 ASN N N 128.09 0.06 1 216 124 39 ASN CA C 52.15 0.14 1 217 124 39 ASN HA H 4.08 0.02 1 218 124 39 ASN C C 171.79 0.14 1 219 124 39 ASN CB C 33.88 0.14 1 220 125 40 ASP H H 8.763 0.02 1 221 125 40 ASP N N 113.183 0.06 1 222 125 40 ASP CA C 53.42 0.14 1 223 125 40 ASP HA H 4.13 0.02 1 224 125 40 ASP C C 172.1 0.14 1 225 125 40 ASP CB C 37.71 0.14 1 226 126 41 GLN H H 7.885 0.02 1 227 126 41 GLN N N 118.115 0.06 1 228 126 41 GLN CA C 51.91 0.14 1 229 126 41 GLN HA H 4.61 0.02 1 230 126 41 GLN C C 171.33 0.14 1 231 126 41 GLN CB C 30.16 0.14 1 232 127 42 LEU H H 8.508 0.02 1 233 127 42 LEU N N 124.293 0.06 1 234 127 42 LEU CA C 51.64 0.14 1 235 127 42 LEU HA H 5.18 0.02 1 236 127 42 LEU C C 173.79 0.14 1 237 127 42 LEU CB C 40.02 0.14 1 238 128 43 ILE H H 9.854 0.02 1 239 128 43 ILE N N 120.292 0.06 1 240 128 43 ILE CA C 56.59 0.14 1 241 128 43 ILE HA H 5.01 0.02 1 242 128 43 ILE C C 172.25 0.14 1 243 128 43 ILE CB C 41.19 0.14 1 244 129 44 SER H H 8.902 0.02 1 245 129 44 SER N N 117.363 0.06 1 246 129 44 SER CA C 53.06 0.14 1 247 129 44 SER HA H 5.67 0.02 1 248 129 44 SER CB C 61.31 0.14 1 249 130 45 PRO CA C 63.8 0.14 1 250 130 45 PRO HA H 4.3 0.02 1 251 130 45 PRO C C 175.08 0.14 1 252 130 45 PRO CB C 30.46 0.14 1 253 131 46 LYS H H 7.685 0.02 1 254 131 46 LYS N N 114.837 0.06 1 255 131 46 LYS CA C 57.84 0.14 1 256 131 46 LYS HA H 3.76 0.02 1 257 131 46 LYS C C 174.09 0.14 1 258 131 46 LYS CB C 30.43 0.14 1 259 132 47 HIS H H 8.352 0.02 1 260 132 47 HIS N N 120.822 0.06 1 261 132 47 HIS CA C 55.88 0.14 1 262 132 47 HIS HA H 4.61 0.02 1 263 132 47 HIS C C 175.06 0.14 1 264 132 47 HIS CB C 28.6 0.14 1 265 133 48 PHE H H 8.889 0.02 1 266 133 48 PHE N N 119.98 0.06 1 267 133 48 PHE CA C 57.21 0.14 1 268 133 48 PHE HA H 4.08 0.02 1 269 133 48 PHE C C 173.25 0.14 1 270 133 48 PHE CB C 36.33 0.14 1 271 134 49 VAL H H 8.296 0.02 1 272 134 49 VAL N N 117.431 0.06 1 273 134 49 VAL CA C 63.0 0.14 1 274 134 49 VAL HA H 3.47 0.02 1 275 134 49 VAL C C 177.41 0.14 1 276 134 49 VAL CB C 29.29 0.14 1 277 135 50 HIS H H 7.74 0.02 1 278 135 50 HIS N N 118.949 0.06 1 279 135 50 HIS CA C 56.7 0.14 1 280 135 50 HIS HA H 4.37 0.02 1 281 135 50 HIS C C 174.66 0.14 1 282 135 50 HIS CB C 26.93 0.14 1 283 136 51 LEU H H 8.515 0.02 1 284 136 51 LEU N N 121.089 0.06 1 285 136 51 LEU CA C 55.09 0.14 1 286 136 51 LEU HA H 3.88 0.02 1 287 136 51 LEU C C 176.64 0.14 1 288 136 51 LEU CB C 39.82 0.14 1 289 137 52 ALA H H 8.105 0.02 1 290 137 52 ALA N N 120.242 0.06 1 291 137 52 ALA CA C 50.3 0.14 1 292 137 52 ALA HA H 4.12 0.02 1 293 137 52 ALA C C 175.83 0.14 1 294 137 52 ALA CB C 17.14 0.14 1 295 138 53 GLY H H 7.847 0.02 1 296 138 53 GLY N N 105.906 0.06 1 297 138 53 GLY CA C 43.6 0.14 1 298 138 53 GLY HA2 H 3.96 0.02 1 299 138 53 GLY C C 172.96 0.14 1 300 139 54 LYS H H 7.987 0.02 1 301 139 54 LYS N N 118.662 0.06 1 302 139 54 LYS CA C 52.7 0.14 1 303 139 54 LYS HA H 4.57 0.02 1 304 139 54 LYS C C 176.1 0.14 1 305 139 54 LYS CB C 30.0 0.14 1 306 140 55 SER H H 8.407 0.02 1 307 140 55 SER N N 115.768 0.06 1 308 140 55 SER CA C 57.6 0.14 1 309 140 55 SER HA H 4.32 0.02 1 310 140 55 SER C C 173.84 0.14 1 311 140 55 SER CB C 60.93 0.14 1 312 141 56 THR H H 8.024 0.02 1 313 141 56 THR N N 112.854 0.06 1 314 141 56 THR CA C 60.48 0.14 1 315 141 56 THR HA H 4.14 0.02 1 316 141 56 THR C C 172.75 0.14 1 317 141 56 THR CB C 66.45 0.14 1 318 142 57 LEU H H 7.724 0.02 1 319 142 57 LEU N N 122.795 0.06 1 320 142 57 LEU CA C 53.26 0.14 1 321 142 57 LEU HA H 4.29 0.02 1 322 142 57 LEU C C 174.72 0.14 1 323 142 57 LEU CB C 39.3 0.14 1 324 143 58 LYS H H 8.11 0.02 1 325 143 58 LYS N N 119.637 0.06 1 326 143 58 LYS CA C 54.73 0.14 1 327 143 58 LYS HA H 4.15 0.02 1 328 143 58 LYS C C 173.86 0.14 1 329 143 58 LYS CB C 30.14 0.14 1 330 144 59 ASP H H 8.136 0.02 1 331 144 59 ASP N N 118.555 0.06 1 332 144 59 ASP CA C 51.28 0.14 1 333 144 59 ASP HA H 4.82 0.02 1 334 144 59 ASP C C 175.04 0.14 1 335 144 59 ASP CB C 39.14 0.14 1 336 145 60 TRP H H 8.792 0.02 1 337 145 60 TRP N N 128.521 0.06 1 338 145 60 TRP CA C 57.57 0.14 1 339 145 60 TRP HA H 4.53 0.02 1 340 145 60 TRP C C 173.63 0.14 1 341 145 60 TRP CB C 24.5 0.14 1 342 145 60 TRP NE1 N 131.933 0.06 1 343 145 60 TRP HE1 H 10.858 0.02 1 344 146 61 LYS H H 7.317 0.02 1 345 146 61 LYS N N 117.249 0.06 1 346 146 61 LYS CA C 56.22 0.14 1 347 146 61 LYS HA H 3.47 0.02 1 348 146 61 LYS C C 175.19 0.14 1 349 146 61 LYS CB C 29.26 0.14 1 350 147 62 ARG H H 7.492 0.02 1 351 147 62 ARG N N 116.345 0.06 1 352 147 62 ARG CA C 54.67 0.14 1 353 147 62 ARG HA H 4.37 0.02 1 354 147 62 ARG C C 175.6 0.14 1 355 147 62 ARG CB C 29.14 0.14 1 356 148 63 ALA H H 7.738 0.02 1 357 148 63 ALA N N 119.859 0.06 1 358 148 63 ALA CA C 51.1 0.14 1 359 148 63 ALA HA H 4.08 0.02 1 360 148 63 ALA C C 174.74 0.14 1 361 148 63 ALA CB C 18.44 0.14 1 362 149 64 ILE H H 7.182 0.02 1 363 149 64 ILE N N 117.375 0.06 1 364 149 64 ILE CA C 58.42 0.14 1 365 149 64 ILE HA H 4.47 0.02 1 366 149 64 ILE C C 171.89 0.14 1 367 149 64 ILE CB C 36.76 0.14 1 368 150 65 ARG H H 9.0 0.02 1 369 150 65 ARG N N 124.577 0.06 1 370 150 65 ARG CA C 51.6 0.14 1 371 150 65 ARG HA H 4.89 0.02 1 372 150 65 ARG C C 171.71 0.14 1 373 150 65 ARG CB C 31.25 0.14 1 374 151 66 LEU H H 9.13 0.02 1 375 151 66 LEU N N 124.44 0.06 1 376 151 66 LEU CA C 52.66 0.14 1 377 151 66 LEU HA H 4.81 0.02 1 378 151 66 LEU CB C 42.54 0.14 1 379 152 67 GLY HA2 H 3.73 0.02 1 380 153 68 GLY CA C 42.4 0.14 1 381 153 68 GLY HA2 H 3.44 0.02 1 382 153 68 GLY C C 171.1 0.14 1 383 154 69 ILE H H 7.716 0.02 1 384 154 69 ILE N N 123.889 0.06 1 385 154 69 ILE CA C 56.35 0.14 1 386 154 69 ILE HA H 4.37 0.02 1 387 154 69 ILE C C 173.45 0.14 1 388 154 69 ILE CB C 36.19 0.14 1 389 155 70 MET H H 9.009 0.02 1 390 155 70 MET N N 125.429 0.06 1 391 155 70 MET CA C 55.64 0.14 1 392 155 70 MET HA H 4.2 0.02 1 393 155 70 MET C C 174.45 0.14 1 394 155 70 MET CB C 31.61 0.14 1 395 156 71 LEU H H 9.294 0.02 1 396 156 71 LEU N N 127.856 0.06 1 397 156 71 LEU CA C 56.05 0.14 1 398 156 71 LEU HA H 4.61 0.02 1 399 156 71 LEU C C 174.29 0.14 1 400 156 71 LEU CB C 38.69 0.14 1 401 157 72 ARG H H 8.592 0.02 1 402 157 72 ARG N N 116.103 0.06 1 403 157 72 ARG CA C 56.56 0.14 1 404 157 72 ARG HA H 4.24 0.02 1 405 157 72 ARG C C 174.15 0.14 1 406 157 72 ARG CB C 28.62 0.14 1 407 158 73 LYS H H 6.891 0.02 1 408 158 73 LYS N N 116.728 0.06 1 409 158 73 LYS CA C 56.09 0.14 1 410 158 73 LYS HA H 5.1 0.02 1 411 158 73 LYS C C 174.25 0.14 1 412 158 73 LYS CB C 29.63 0.14 1 413 159 74 MET H H 7.677 0.02 1 414 159 74 MET N N 119.068 0.06 1 415 159 74 MET CA C 55.81 0.14 1 416 159 74 MET HA H 4.12 0.02 1 417 159 74 MET C C 176.27 0.14 1 418 159 74 MET CB C 29.65 0.14 1 419 160 75 MET H H 8.182 0.02 1 420 160 75 MET N N 121.605 0.06 1 421 160 75 MET CA C 60.23 0.14 1 422 160 75 MET HA H 4.17 0.02 1 423 160 75 MET CB C 30.37 0.14 1 424 161 76 ASP H H 8.548 0.02 1 425 161 76 ASP N N 123.557 0.06 1 426 161 76 ASP CA C 56.18 0.14 1 427 161 76 ASP HA H 4.44 0.02 1 428 161 76 ASP C C 175.67 0.14 1 429 161 76 ASP CB C 25.7 0.14 1 430 162 77 SER H H 8.522 0.02 1 431 162 77 SER N N 118.736 0.06 1 432 162 77 SER CA C 56.31 0.14 1 433 162 77 SER HA H 4.76 0.02 1 434 162 77 SER C C 173.02 0.14 1 435 162 77 SER CB C 61.43 0.14 1 436 163 78 GLY H H 7.78 0.02 1 437 163 78 GLY N N 109.896 0.06 1 438 163 78 GLY CA C 43.53 0.14 1 439 163 78 GLY HA2 H 3.93 0.02 1 440 163 78 GLY HA3 H 4.17 0.02 1 441 163 78 GLY C C 172.21 0.14 1 442 164 79 GLN H H 8.236 0.02 1 443 164 79 GLN N N 118.83 0.06 1 444 164 79 GLN CA C 55.5 0.14 1 445 164 79 GLN HA H 4.07 0.02 1 446 164 79 GLN C C 173.36 0.14 1 447 164 79 GLN CB C 27.42 0.14 1 448 165 80 ILE H H 7.316 0.02 1 449 165 80 ILE N N 115.351 0.06 1 450 165 80 ILE CA C 57.03 0.14 1 451 165 80 ILE HA H 4.23 0.02 1 452 165 80 ILE C C 169.2 0.14 1 453 165 80 ILE CB C 38.59 0.14 1 454 166 81 ASP H H 8.273 0.02 1 455 166 81 ASP N N 123.772 0.06 1 456 166 81 ASP CA C 48.8 0.14 1 457 166 81 ASP HA H 4.85 0.02 1 458 166 81 ASP C C 172.71 0.14 1 459 166 81 ASP CB C 41.72 0.14 1 460 167 82 PHE H H 8.44 0.02 1 461 167 82 PHE N N 118.698 0.06 1 462 167 82 PHE CA C 55.52 0.14 1 463 167 82 PHE HA H 4.53 0.02 1 464 167 82 PHE C C 174.31 0.14 1 465 167 82 PHE CB C 37.64 0.14 1 466 168 83 TYR H H 8.711 0.02 1 467 168 83 TYR N N 126.076 0.06 1 468 168 83 TYR CA C 56.8 0.14 1 469 168 83 TYR HA H 3.71 0.02 1 470 168 83 TYR C C 173.43 0.14 1 471 168 83 TYR CB C 35.56 0.14 1 472 169 84 GLN H H 8.512 0.02 1 473 169 84 GLN N N 121.82 0.06 1 474 169 84 GLN CA C 54.12 0.14 1 475 169 84 GLN HA H 3.75 0.02 1 476 169 84 GLN C C 174.72 0.14 1 477 169 84 GLN CB C 23.66 0.14 1 478 170 85 HIS H H 7.593 0.02 1 479 170 85 HIS N N 118.755 0.06 1 480 170 85 HIS CA C 53.06 0.14 1 481 170 85 HIS HA H 4.86 0.02 1 482 170 85 HIS C C 173.25 0.14 1 483 170 85 HIS CB C 27.44 0.14 1 484 171 86 ASP H H 8.892 0.02 1 485 171 86 ASP N N 112.008 0.06 1 486 171 86 ASP CA C 52.95 0.14 1 487 171 86 ASP HA H 4.16 0.02 1 488 171 86 ASP C C 173.88 0.14 1 489 171 86 ASP CB C 36.74 0.14 1 490 172 87 LYS H H 7.631 0.02 1 491 172 87 LYS N N 118.063 0.06 1 492 172 87 LYS CA C 54.17 0.14 1 493 172 87 LYS HA H 4.45 0.02 1 494 172 87 LYS C C 173.77 0.14 1 495 172 87 LYS CB C 32.87 0.14 1 496 173 88 VAL H H 8.447 0.02 1 497 173 88 VAL N N 122.483 0.06 1 498 173 88 VAL CA C 59.65 0.14 1 499 173 88 VAL HA H 4.16 0.02 1 500 173 88 VAL C C 170.67 0.14 1 501 173 88 VAL CB C 30.81 0.14 1 502 174 89 CYS H H 8.408 0.02 1 503 174 89 CYS N N 127.523 0.06 1 504 174 89 CYS CA C 56.39 0.14 1 505 174 89 CYS HA H 4.89 0.02 1 506 174 89 CYS C C 172.86 0.14 1 507 174 89 CYS CB C 29.12 0.14 1 508 175 90 SER H H 9.838 0.02 1 509 175 90 SER N N 129.372 0.06 1 510 175 90 SER CA C 57.34 0.14 1 511 175 90 SER HA H 4.41 0.02 1 512 175 90 SER C C 172.8 0.14 1 513 175 90 SER CB C 63.3 0.14 1 514 176 91 ASN H H 10.55 0.02 1 515 176 91 ASN N N 123.332 0.06 1 516 176 91 ASN CA C 52.43 0.14 1 517 176 91 ASN HA H 4.52 0.02 1 518 176 91 ASN C C 173.27 0.14 1 519 176 91 ASN CB C 35.61 0.14 1 520 177 92 THR H H 7.735 0.02 1 521 177 92 THR N N 107.035 0.06 1 522 177 92 THR CA C 59.44 0.14 1 523 177 92 THR HA H 4.73 0.02 1 524 177 92 THR C C 172.19 0.14 1 525 177 92 THR CB C 67.23 0.14 1 526 178 93 CYS H H 7.999 0.02 1 527 178 93 CYS N N 120.875 0.06 1 528 178 93 CYS CA C 54.98 0.14 1 529 178 93 CYS HA H 4.6 0.02 1 530 178 93 CYS C C 173.61 0.14 1 531 178 93 CYS CB C 29.06 0.14 1 532 179 94 ARG H H 8.041 0.02 1 533 179 94 ARG N N 121.656 0.06 1 534 179 94 ARG CA C 53.58 0.14 1 535 179 94 ARG HA H 4.61 0.02 1 536 179 94 ARG C C 173.37 0.14 1 537 179 94 ARG CB C 28.26 0.14 1 538 180 95 SER H H 8.204 0.02 1 539 180 95 SER N N 116.465 0.06 1 540 180 95 SER CA C 56.26 0.14 1 541 180 95 SER HA H 4.53 0.02 1 542 180 95 SER C C 173.15 0.14 1 543 180 95 SER CB C 61.52 0.14 1 544 181 96 THR H H 8.33 0.02 1 545 181 96 THR N N 116.464 0.06 1 546 181 96 THR CA C 59.4 0.14 1 547 181 96 THR HA H 4.41 0.02 1 548 181 96 THR C C 171.3 0.14 1 549 181 96 THR CB C 67.44 0.14 1 550 182 97 LYS H H 8.058 0.02 1 551 182 97 LYS N N 128.717 0.06 1 552 182 97 LYS CA C 55.48 0.14 1 553 182 97 LYS HA H 4.16 0.02 1 554 182 97 LYS CB C 31.27 0.14 1 stop_ save_ ######################## # Coupling constants # ######################## save_J_values_set_1 _Saveframe_category coupling_constants _Details . loop_ _Sample_label $Sample_1 $Sample_2 stop_ _Sample_conditions_label $condition_1 _Spectrometer_frequency_1H 600 _Mol_system_component_name 'Human GMEB1 extended 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 9 ALA H 9 ALA HA 8.88 . . 1 2 3JHNHA 12 ILE H 12 ILE HA 11.29 . . 1 3 3JHNHA 13 THR H 13 THR HA 8.73 . . 1 4 3JHNHA 16 GLU H 16 GLU HA 8.74 . . 1 5 3JHNHA 17 SER H 17 SER HA 7.42 . . 1 6 3JHNHA 18 LYS H 18 LYS HA 7.69 . . 1 7 3JHNHA 21 LEU H 21 LEU HA 8.14 . . 1 8 3JHNHA 26 PHE H 26 PHE HA 6.28 . . 1 9 3JHNHA 34 LYS H 34 LYS HA 5.31 . . 1 10 3JHNHA 35 CYS H 35 CYS HA 10.16 . . 1 11 3JHNHA 36 VAL H 36 VAL HA 7.99 . . 1 12 3JHNHA 37 LYS H 37 LYS HA 9.14 . . 1 13 3JHNHA 38 PHE H 38 PHE HA 8.65 . . 1 14 3JHNHA 41 GLN H 41 GLN HA 9.74 . . 1 15 3JHNHA 42 LEU H 42 LEU HA 8.19 . . 1 16 3JHNHA 43 ILE H 43 ILE HA 10.32 . . 1 17 3JHNHA 46 LYS H 46 LYS HA 4.21 . . 1 18 3JHNHA 47 HIS H 47 HIS HA 5.40 . . 1 19 3JHNHA 48 PHE H 48 PHE HA 3.28 . . 1 20 3JHNHA 49 VAL H 49 VAL HA 4.90 . . 1 21 3JHNHA 50 HIS H 50 HIS HA 4.11 . . 1 22 3JHNHA 51 LEU H 51 LEU HA 4.21 . . 1 23 3JHNHA 52 ALA H 52 ALA HA 6.39 . . 1 24 3JHNHA 55 SER H 55 SER HA 5.80 . . 1 25 3JHNHA 56 THR H 56 THR HA 6.35 . . 1 26 3JHNHA 60 TRP H 60 TRP HA 3.15 . . 1 27 3JHNHA 61 LYS H 61 LYS HA 5.77 . . 1 28 3JHNHA 64 ILE H 64 ILE HA 9.14 . . 1 29 3JHNHA 65 ARG H 65 ARG HA 9.04 . . 1 30 3JHNHA 66 LEU H 66 LEU HA 8.87 . . 1 31 3JHNHA 70 MET H 70 MET HA 3.35 . . 1 32 3JHNHA 71 LEU H 71 LEU HA 3.71 . . 1 33 3JHNHA 74 MET H 74 MET HA 5.27 . . 1 stop_ save_