data_4656 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Design and Solution Structure of a Well-folded Stack of Two Beta-hairpins Based on the Amino-terminal Fragment of Human Granulin A ; _BMRB_accession_number 4656 _BMRB_flat_file_name bmr4656.str _Entry_type original _Submission_date 2000-10-17 _Accession_date 2001-03-16 _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 Tolkatchev D. . . 2 Ng A. . . 3 Vranken W. . . 4 Ni F. . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 166 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2001-05-10 original BMRB . stop_ _Original_release_date 2001-03-16 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; Design and Solution Structure of a Well-folded Stack of Two Beta-hairpins Based on the Amino-terminal Fragment of Human Granulin A ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 10956026 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Tolkatchev D. . . 2 Ng A. . . 3 Vranken W. . . 4 Ni F. . . stop_ _Journal_abbreviation Biochemistry _Journal_volume 39 _Journal_issue . _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 2878 _Page_last 2886 _Year 2000 _Details . loop_ _Keyword 'beta-hairpin stack' 'granulin/epithelin protein repeats' stop_ save_ ################################## # Molecular system description # ################################## save_system_GRANULIN_A _Saveframe_category molecular_system _Mol_system_name 'GRANULIN A' _Abbreviation_common HGA _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'GRANULIN A' $GRANULIN_A stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state monomer _System_paramagnetic no _System_thiol_state 'disulfide bound and free' _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_GRANULIN_A _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common GRANULIN_A _Abbreviation_common HGA _Molecular_mass . _Mol_thiol_state 'disulfide bound and free' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 31 _Mol_residue_sequence ; VVHCDMEVICPDGYTCCRLP SGAWGCCPFTQ ; loop_ _Residue_seq_code _Residue_label 1 VAL 2 VAL 3 HIS 4 CYS 5 ASP 6 MET 7 GLU 8 VAL 9 ILE 10 CYS 11 PRO 12 ASP 13 GLY 14 TYR 15 THR 16 CYS 17 CYS 18 ARG 19 LEU 20 PRO 21 SER 22 GLY 23 ALA 24 TRP 25 GLY 26 CYS 27 CYS 28 PRO 29 PHE 30 THR 31 GLN 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 PDB 1G26 'The Solution Structure Of A Well-Folded Peptide Based On The 31-Residue Amino-Terminal Subdomain Of Human Granulin A' 96.77 31 100.00 100.00 1.38e-09 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $GRANULIN_A 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 $GRANULIN_A . . . . . . 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 $GRANULIN_A 0.5 mM . 'sodium acetate' 20 mM [U-2H] D2O 10 % . H2O 90 % . stop_ save_ save_sample_2 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $GRANULIN_A 0.5 mM . 'sodium acetate' 20 mM [U-2H] D2O 100 % . stop_ save_ ############################ # Computer software used # ############################ save_X-PLOR _Saveframe_category software _Name X-PLOR _Version 3.1 loop_ _Task refinement 'structure solution' stop_ _Details Brunger save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model DRX _Field_strength 500 _Details . save_ ############################# # NMR applied experiments # ############################# save_2D_NOESY_1 _Saveframe_category NMR_applied_experiment _Experiment_name '2D NOESY' _Sample_label . save_ ####################### # Sample conditions # ####################### save_sample_cond_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 5.0 . pH pressure 1 . atm temperature 288 . K stop_ save_ save_sample_cond_2 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 5.0 . pH pressure 1 . atm temperature 298 . 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 . H 1 . ppm . . . . . . 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_chemical_shift_set_1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Experiment_label '2D NOESY' stop_ loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $sample_cond_1 _Chem_shift_reference_set_label $chemical_shift_reference _Mol_system_component_name 'GRANULIN A' _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 VAL HA H 3.87 . . 2 . 1 VAL HB H 2.07 . . 3 . 1 VAL HG1 H 0.90 . . 4 . 1 VAL HG2 H 0.74 . . 5 . 2 VAL H H 8.79 . . 6 . 2 VAL HA H 4.29 . . 7 . 2 VAL HB H 1.78 . . 8 . 2 VAL HG1 H 1.00 . . 9 . 2 VAL HG2 H 0.90 . . 10 . 3 HIS H H 9.20 . . 11 . 3 HIS HA H 4.56 . . 12 . 3 HIS HB2 H 3.07 . . 13 . 3 HIS HB3 H 3.07 . . 14 . 3 HIS HD2 H 7.28 . . 15 . 3 HIS HE1 H 8.60 . . 16 . 4 CYS H H 8.78 . . 17 . 4 CYS HA H 4.14 . . 18 . 4 CYS HB2 H 1.61 . . 19 . 4 CYS HB3 H 1.45 . . 20 . 5 ASP H H 7.68 . . 21 . 5 ASP HA H 4.30 . . 22 . 5 ASP HB2 H 3.13 . . 23 . 5 ASP HB3 H 2.94 . . 24 . 6 MET H H 8.46 . . 25 . 6 MET HA H 4.28 . . 26 . 6 MET HB2 H 2.58 . . 27 . 6 MET HB3 H 2.16 . . 28 . 6 MET HG2 H 2.72 . . 29 . 6 MET HG3 H 2.72 . . 30 . 7 GLU H H 8.60 . . 31 . 7 GLU HA H 4.49 . . 32 . 7 GLU HB2 H 2.16 . . 33 . 7 GLU HB3 H 2.09 . . 34 . 7 GLU HG2 H 2.27 . . 35 . 7 GLU HG3 H 2.27 . . 36 . 8 VAL H H 8.59 . . 37 . 8 VAL HA H 4.03 . . 38 . 8 VAL HB H 1.57 . . 39 . 8 VAL HG1 H 1.15 . . 40 . 8 VAL HG2 H 0.74 . . 41 . 9 ILE H H 8.22 . . 42 . 9 ILE HA H 4.18 . . 43 . 9 ILE HB H 1.46 . . 44 . 9 ILE HG12 H 1.25 . . 45 . 9 ILE HG13 H 1.25 . . 46 . 9 ILE HG2 H 0.65 . . 47 . 9 ILE HD1 H 0.42 . . 48 . 10 CYS H H 9.02 . . 49 . 10 CYS HA H 5.24 . . 50 . 10 CYS HB2 H 2.72 . . 51 . 10 CYS HB3 H 2.20 . . 52 . 11 PRO HA H 4.42 . . 53 . 11 PRO HB2 H 2.25 . . 54 . 11 PRO HB3 H 1.34 . . 55 . 11 PRO HG2 H 1.81 . . 56 . 11 PRO HG3 H 1.62 . . 57 . 11 PRO HD2 H 3.67 . . 58 . 11 PRO HD3 H 2.64 . . 59 . 12 ASP H H 8.34 . . 60 . 12 ASP HA H 4.46 . . 61 . 12 ASP HB2 H 2.66 . . 62 . 12 ASP HB3 H 2.48 . . 63 . 13 GLY H H 8.93 . . 64 . 13 GLY HA2 H 4.19 . . 65 . 13 GLY HA3 H 3.43 . . 66 . 14 TYR H H 8.03 . . 67 . 14 TYR HA H 5.04 . . 68 . 14 TYR HB2 H 3.31 . . 69 . 14 TYR HB3 H 2.54 . . 70 . 14 TYR HD1 H 6.77 . . 71 . 14 TYR HD2 H 6.77 . . 72 . 15 THR H H 9.33 . . 73 . 15 THR HA H 4.58 . . 74 . 15 THR HB H 4.00 . . 75 . 15 THR HG2 H 1.18 . . 76 . 16 CYS H H 8.36 . . 77 . 16 CYS HA H 5.26 . . 78 . 16 CYS HB2 H 2.93 . . 79 . 16 CYS HB3 H 2.73 . . 80 . 17 CYS H H 9.46 . . 81 . 17 CYS HA H 5.10 . . 82 . 17 CYS HB2 H 2.93 . . 83 . 17 CYS HB3 H 2.93 . . 84 . 18 ARG H H 9.06 . . 85 . 18 ARG HA H 4.02 . . 86 . 18 ARG HB2 H 1.42 . . 87 . 18 ARG HB3 H 1.20 . . 88 . 18 ARG HG2 H 1.03 . . 89 . 18 ARG HG3 H 0.90 . . 90 . 18 ARG HD2 H 2.35 . . 91 . 18 ARG HD3 H 2.08 . . 92 . 18 ARG HH11 H 6.53 . . 93 . 18 ARG HH12 H 6.53 . . 94 . 18 ARG HH21 H 6.40 . . 95 . 18 ARG HH22 H 6.40 . . 96 . 19 LEU H H 8.90 . . 97 . 19 LEU HA H 4.50 . . 98 . 19 LEU HB2 H 1.67 . . 99 . 19 LEU HB3 H 1.67 . . 100 . 19 LEU HG H 1.62 . . 101 . 19 LEU HD1 H 0.87 . . 102 . 19 LEU HD2 H 0.81 . . 103 . 20 PRO HA H 4.25 . . 104 . 20 PRO HB2 H 2.39 . . 105 . 20 PRO HB3 H 1.92 . . 106 . 20 PRO HG2 H 2.15 . . 107 . 20 PRO HG3 H 2.03 . . 108 . 20 PRO HD2 H 3.83 . . 109 . 20 PRO HD3 H 3.83 . . 110 . 21 SER H H 7.48 . . 111 . 21 SER HA H 4.22 . . 112 . 21 SER HB2 H 4.03 . . 113 . 21 SER HB3 H 3.88 . . 114 . 22 GLY H H 8.34 . . 115 . 22 GLY HA2 H 4.40 . . 116 . 22 GLY HA3 H 3.35 . . 117 . 23 ALA H H 7.32 . . 118 . 23 ALA HA H 4.33 . . 119 . 23 ALA HB H 1.35 . . 120 . 24 TRP H H 8.60 . . 121 . 24 TRP HA H 5.00 . . 122 . 24 TRP HB2 H 3.14 . . 123 . 24 TRP HB3 H 2.94 . . 124 . 24 TRP HD1 H 7.28 . . 125 . 24 TRP HE1 H 7.435 . . 126 . 24 TRP HE3 H 10.08 . . 127 . 24 TRP HZ2 H 7.48 . . 128 . 24 TRP HZ3 H 6.40 . . 129 . 25 GLY H H 9.44 . . 130 . 25 GLY HA2 H 4.64 . . 131 . 25 GLY HA3 H 3.76 . . 132 . 26 CYS H H 8.47 . . 133 . 26 CYS HA H 5.79 . . 134 . 26 CYS HB2 H 2.76 . . 135 . 26 CYS HB3 H 2.76 . . 136 . 27 CYS H H 9.66 . . 137 . 27 CYS HA H 5.32 . . 138 . 27 CYS HB2 H 3.18 . . 139 . 27 CYS HB3 H 2.88 . . 140 . 28 PRO HA H 3.68 . . 141 . 28 PRO HB2 H 1.71 . . 142 . 28 PRO HB3 H 2.01 . . 143 . 28 PRO HG2 H 1.92 . . 144 . 28 PRO HG3 H 1.92 . . 145 . 28 PRO HD2 H 3.88 . . 146 . 28 PRO HD3 H 3.88 . . 147 . 29 PHE H H 8.07 . . 148 . 29 PHE HA H 4.62 . . 149 . 29 PHE HB2 H 2.93 . . 150 . 29 PHE HB3 H 2.93 . . 151 . 29 PHE HD1 H 7.12 . . 152 . 29 PHE HD2 H 7.12 . . 153 . 29 PHE HE1 H 7.28 . . 154 . 29 PHE HE2 H 7.28 . . 155 . 30 THR H H 8.07 . . 156 . 30 THR HA H 4.21 . . 157 . 30 THR HB H 4.07 . . 158 . 30 THR HG2 H 1.10 . . 159 . 31 GLN H H 7.90 . . 160 . 31 GLN HA H 4.07 . . 161 . 31 GLN HB2 H 1.88 . . 162 . 31 GLN HB3 H 1.88 . . 163 . 31 GLN HG2 H 2.22 . . 164 . 31 GLN HG3 H 2.05 . . 165 . 31 GLN HE21 H 7.61 . . 166 . 31 GLN HE22 H 6.87 . . stop_ save_