data_4057 #Corrected using PDB structure: 1AZ6_ # #N.B. (Observed* = Observed shift + Offset correction) # #After reference correction, the following residues still #have a HA chemical shift difference (obs*-pred) greater than 0.7ppm: #NUM AA CS Observed* Predicted # 1 T HA 3.48 4.47 # 17 T HA 4.65 3.94 # #After reference correction, the following residues still #have a HN chemical shift difference (obs*-pred) greater than 2.0ppm: #NUM AA CS Observed* Predicted # 15 G H 4.86 7.53 # #The average CS difference between predicted and observed: #HA CA CB CO N HN #-0.04 N/A N/A N/A N/A -0.10 # #bmr4057.str.corr chemical shifts have been re-referenced with the following #offsets (these values have been added to the original bmr4057.str file): #HA CA CB CO N HN #N/A N/A N/A N/A N/A N/A # #The 95% confidence intervals for the above recommended offsets are: # HA CA CB CO N HN #+/-0.07 N/A N/A N/A N/A +/-0.17 # #The Correlation Coefficients between predicted and observed #chemical shifts are: #HA CA CB CO N HN #0.648 N/A N/A N/A N/A 0.354 # #The RMSD between predicted and observed* (reference #corrected) chemical shifts are: #HA CA CB CO N HN #0.192 N/A N/A N/A N/A 0.479 # ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Three-Dimensional Structures of Three Engineered Cellulose-Binding Domains of Cellobiohydrolase I from Trichoderma reesei ; loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Mattinen Maija-Liisa M.-L.M. PhLic 2 Kontteli Maarit . . 3 Kerovuo Janne . . 4 Linder Markus . . 5 Annila Arto . . 6 Lindeberg Gunnar . . 7 Reinikainen Tapani . . 8 Drakenberg Torbjorn . . stop_ _BMRB_accession_number 4057 _BMRB_flat_file_name bmr4057.str _Entry_type new _Submission_date 1997-09-05 _Accession_date 1997-09-22 _Entry_origination author _NMR_STAR_version 2.1 _Experimental_method NMR loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count '1H chemical shifts' 185 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 1998-02-25 reformat BMRB 'converted to NMR-STAR version 2.1' stop_ save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full ; Mattinen, M-L. M., Kontteli, M., Kerovuo, J., Linder, M., Lindeberg, G., Reinikainen, T., and Drakenberg T., "Three-Dimensional Structures of Three Engineered Cellulose-Binding Domains of Cellobiohydrolase I from Trichoderma reesei," Protein Sci. 6, 294-303 (1997). ; _Citation_title ; Three-Dimensional Structures of Three Engineered Cellulose-Binding Domains of Cellobiohydrolase I from Trichoderma reesei ; _Citation_status published _Citation_type journal _MEDLINE_UI_code 97194052 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Mattinen Maija-Liisa M.-L.M. PhLic 2 Kontteli Maarit . . 3 Kerovuo Janne . . 4 Linder Markus . . 5 Annila Arto . . 6 Lindeberg Gunnar . . 7 Reinikainen Tapani . . 8 Drakenberg Torbjorn . . stop_ _Journal_abbreviation 'Protein Sci.' _Journal_name_full 'Protein Science' _Journal_volume 6 _Page_first 294 _Page_last 303 _Year 1997 loop_ _Keyword cellulase 'nuclear magnetic resonance spectroscopy' 'structure determination' 'cellulose binding domain (CBD)' stop_ save_ ################################## # Molecular system description # ################################## save_Y5A_CBD _Saveframe_category molecular_system _Mol_system_name Y5A_CBD_Cellobiohydrolase_I _Abbreviation_common Y5A_CBD loop_ _Mol_system_component_name _Mol_label Y5A $Y5A_CBD_Cellobiohydrolase_I stop_ _System_physical_state native _System_oligomer_state monomer _System_paramagnetic no save_ ######################## # Monomeric polymers # ######################## save_Y5A_CBD_Cellobiohydrolase_I _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'cellulose-binding domain' _Name_variant Y5A _Abbreviation_common CBD _Molecular_mass 4000 ############################## # Polymer residue sequence # ############################## _Residue_count 36 _Mol_residue_sequence ; TQSHAGQCGGIGYSGPTVCA SGTTCQVLNPAYSQCL ; loop_ _Residue_seq_code _Residue_label 1 THR 2 GLN 3 SER 4 HIS 5 ALA 6 GLY 7 GLN 8 CYS 9 GLY 10 GLY 11 ILE 12 GLY 13 TYR 14 SER 15 GLY 16 PRO 17 THR 18 VAL 19 CYS 20 ALA 21 SER 22 GLY 23 THR 24 THR 25 CYS 26 GLN 27 VAL 28 LEU 29 ASN 30 PRO 31 TYR 32 TYR 33 SER 34 GLN 35 CYS 36 LEU stop_ _Sequence_homology_query_date 2004-07-29 _Sequence_homology_query_revised_last_date 1999-12-06 save_ ######################################## # Molecular bond linkage definitions # ######################################## save_crosslink_bond_definitions _Saveframe_category crosslink_bonds loop_ _Bond_order _Bond_type _Atom_one_mol_system_component_name _Atom_one_residue_seq_code _Atom_one_atom_name _Atom_two_mol_system_component_name _Atom_two_residue_seq_code _Atom_two_atom_name single disulfide Y5A 8 SG Y5A 25 SG single disulfide Y5A 19 SG Y5A 35 SG stop_ loop_ _Deleted_atom_mol_system_component_name _Deleted_atom_residue_seq_code _Deleted_atom_residue_label _Deleted_atom_name Y5A 8 CYS HG Y5A 19 CYS HG Y5A 25 CYS HG Y5A 35 CYS HG stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species _Details $Y5A_CBD_Cellobiohydrolase_I fungus 51453 Eukaryota Fungi Hypocrea jecorina ; Three-engineered cellulose binding domain (Y5A, Y31A, and Y32A) of Cellobiohydrolase I from Trichoderma reesi ; stop_ save_ ######################### # Experimental source # ######################### save_experimental_source _Saveframe_category experimental_source loop_ _Mol_label _Production_method _Details $Y5A_CBD_Cellobiohydrolase_I 'chemical synthesis' ; The peptide was synthesized by automated solid-phase synthesis using Fmoc chemistry and purified as described Lindeberg et al 1991 (Int J Pept Protein Res 38: 253-259). ; stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_one _Saveframe_category sample _Sample_type solution loop_ _Mol_label _Concentration_value _Concentration_value_units $Y5A_CBD_Cellobiohydrolase_I 7 mg/ml stop_ save_ ####################### # Sample conditions # ####################### save_experimental_conditions_set_one _Saveframe_category sample_conditions loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 3.90 0.005 n/a temperature 15 . C stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chem_shift_reference_parameter_set_one _Saveframe_category chemical_shift_reference loop_ _Mol_common_name _Atom_type _Atom_isotope_number _Atom_group _Chem_shift_units _Chem_shift_value _Reference_method _Reference_type H2O H 1 proton ppm 4.88 internal direct stop_ save_ ################################### # Assigned chemical shift lists # ################################### ################################################################### # Chemical Shift Ambiguity Index Value Definitions # # # # Index Value Definition # # # # 1 Unique # # 2 Ambiguity of geminal atoms or geminal methyl # # proton groups # # 3 Aromatic atoms on opposite sides of the ring # # (e.g. Tyr HE1 and HE2 protons) # # 4 Intraresidue ambiguities (e.g. Lys HG and # # HD protons) # # 5 Interresidue ambiguities (Lys 12 vs. Lys 27) # # 9 Ambiguous, specific ambiguity not defined # # # ################################################################### save_chemical_shift_assignment_Y5A_CBD_Cellobiohydrolase_I _Saveframe_category assigned_chemical_shifts loop_ _Sample_label $sample_one stop_ _Sample_conditions_label $experimental_conditions_set_one _Chem_shift_reference_set_label $chem_shift_reference_parameter_set_one _Mol_system_component_name Y5A loop_ _Atom_shift_assign_ID _Residue_seq_code _Residue_label _Atom_name _Atom_type _Chem_shift_value _Chem_shift_value_error _Chem_shift_ambiguity_code 1 1 THR HA H 3.52 0.01 1 2 1 THR HB H 3.84 0.01 1 3 1 THR HG2 H 0.91 0.01 1 4 2 GLN H H 9.04 0.01 1 5 2 GLN HA H 4.61 0.01 1 6 2 GLN HB2 H 2.03 0.01 1 7 2 GLN HB3 H 1.89 0.01 1 8 2 GLN HG2 H 2.40 0.01 1 9 2 GLN HG3 H 2.22 0.01 1 10 2 GLN HE21 H 8.60 0.01 1 11 2 GLN HE22 H 7.91 0.01 1 12 3 SER H H 8.74 0.01 1 13 3 SER HA H 4.67 0.01 1 14 3 SER HB2 H 3.85 0.01 1 15 3 SER HB3 H 3.84 0.01 1 16 4 HIS H H 7.91 0.01 1 17 4 HIS HA H 4.58 0.01 1 18 4 HIS HB2 H 2.80 0.01 1 19 4 HIS HB3 H 2.41 0.01 1 20 4 HIS HD2 H 6.93 0.01 1 21 4 HIS HE1 H 7.73 0.01 1 22 5 ALA H H 8.52 0.01 1 23 5 ALA HA H 4.32 0.01 1 24 5 ALA HB H 1.39 0.01 1 25 6 GLY H H 8.69 0.01 1 26 6 GLY HA2 H 3.94 0.01 1 27 6 GLY HA3 H 3.44 0.01 1 28 7 GLN H H 8.10 0.01 1 29 7 GLN HA H 4.22 0.01 1 30 7 GLN HB2 H 2.05 0.01 1 31 7 GLN HB3 H 1.68 0.01 1 32 7 GLN HG2 H 2.25 0.01 1 33 7 GLN HG3 H 1.02 0.01 1 34 7 GLN HE21 H 7.03 0.01 1 35 7 GLN HE22 H 6.94 0.01 1 36 8 CYS H H 7.88 0.01 1 37 8 CYS HA H 5.10 0.01 1 38 8 CYS HB2 H 3.35 0.01 1 39 8 CYS HB3 H 2.93 0.01 1 40 9 GLY H H 6.67 0.01 1 41 9 GLY HA2 H 4.21 0.01 1 42 9 GLY HA3 H 3.79 0.01 1 43 10 GLY H H 8.68 0.01 1 44 10 GLY HA2 H 4.28 0.01 1 45 10 GLY HA3 H 3.80 0.01 1 46 11 ILE H H 8.46 0.01 1 47 11 ILE HA H 3.79 0.01 1 48 11 ILE HB H 1.25 0.01 1 49 11 ILE HG12 H 1.50 0.01 1 50 11 ILE HG13 H 0.95 0.01 1 51 11 ILE HG2 H 0.88 0.01 1 52 11 ILE HD1 H 0.48 0.01 1 53 12 GLY H H 9.13 0.01 1 54 12 GLY HA2 H 4.27 0.01 1 55 12 GLY HA3 H 3.71 0.01 1 56 13 TYR H H 7.92 0.01 1 57 13 TYR HA H 4.62 0.01 1 58 13 TYR HB2 H 2.90 0.01 1 59 13 TYR HB3 H 2.76 0.01 1 60 13 TYR HD1 H 6.89 0.01 1 61 13 TYR HD2 H 6.89 0.01 1 62 13 TYR HE1 H 6.42 0.01 1 63 13 TYR HE2 H 6.42 0.01 1 64 14 SER H H 8.54 0.01 1 65 14 SER HA H 4.51 0.01 1 66 14 SER HB2 H 3.78 0.01 1 67 14 SER HB3 H 3.59 0.01 1 68 15 GLY H H 4.96 0.01 1 69 15 GLY HA2 H 4.05 0.01 1 70 15 GLY HA3 H 3.55 0.01 1 71 16 PRO HA H 4.51 0.01 1 72 16 PRO HB2 H 2.36 0.01 1 73 16 PRO HB3 H 1.99 0.01 1 74 16 PRO HG2 H 2.09 0.01 1 75 16 PRO HG3 H 1.99 0.01 1 76 16 PRO HD2 H 3.61 0.01 1 77 16 PRO HD3 H 3.51 0.01 1 78 17 THR H H 8.72 0.01 1 79 17 THR HA H 4.69 0.01 1 80 17 THR HB H 4.18 0.01 1 81 17 THR HG2 H 1.27 0.01 1 82 18 VAL H H 6.94 0.01 1 83 18 VAL HA H 4.11 0.01 1 84 18 VAL HB H 1.99 0.01 1 85 18 VAL HG1 H 0.92 0.01 1 86 18 VAL HG2 H 0.92 0.01 1 87 19 CYS H H 8.63 0.01 1 88 19 CYS HA H 4.78 0.01 1 89 19 CYS HB2 H 3.58 0.01 1 90 19 CYS HB3 H 2.22 0.01 1 91 20 ALA H H 8.32 0.01 1 92 20 ALA HA H 4.17 0.01 1 93 20 ALA HB H 1.35 0.01 1 94 21 SER H H 8.59 0.01 1 95 21 SER HA H 4.17 0.01 1 96 21 SER HB2 H 3.85 0.01 1 97 21 SER HB3 H 3.85 0.01 1 98 22 GLY H H 8.92 0.01 1 99 22 GLY HA2 H 4.35 0.01 1 100 22 GLY HA3 H 3.65 0.01 1 101 23 THR H H 8.16 0.01 1 102 23 THR HA H 4.42 0.01 1 103 23 THR HB H 3.93 0.01 1 104 23 THR HG2 H 0.96 0.01 1 105 24 THR H H 9.26 0.01 1 106 24 THR HA H 4.53 0.01 1 107 24 THR HB H 4.03 0.01 1 108 24 THR HG2 H 1.12 0.01 1 109 25 CYS H H 8.89 0.01 1 110 25 CYS HA H 4.51 0.01 1 111 25 CYS HB2 H 3.11 0.01 1 112 25 CYS HB3 H 2.88 0.01 1 113 26 GLN H H 8.95 0.01 1 114 26 GLN HA H 4.44 0.01 1 115 26 GLN HB2 H 2.04 0.01 1 116 26 GLN HB3 H 1.95 0.01 1 117 26 GLN HG2 H 2.40 0.01 1 118 26 GLN HG3 H 2.23 0.01 1 119 26 GLN HE21 H 7.03 0.01 1 120 26 GLN HE22 H 6.78 0.01 1 121 27 VAL H H 8.68 0.01 1 122 27 VAL HA H 4.01 0.01 1 123 27 VAL HB H 1.88 0.01 1 124 27 VAL HG1 H 0.64 0.01 2 125 27 VAL HG2 H 0.88 0.01 2 126 28 LEU H H 8.64 0.01 1 127 28 LEU HA H 4.67 0.01 1 128 28 LEU HB2 H 1.84 0.01 1 129 28 LEU HB3 H 1.74 0.01 1 130 28 LEU HG H 1.75 0.01 1 131 28 LEU HD1 H 0.93 0.01 2 132 28 LEU HD2 H 0.92 0.01 2 133 29 ASN H H 8.60 0.01 1 134 29 ASN HA H 5.14 0.01 1 135 29 ASN HB2 H 3.14 0.01 1 136 29 ASN HB3 H 3.14 0.01 1 137 29 ASN HD21 H 7.79 0.01 1 138 29 ASN HD22 H 7.02 0.01 1 139 30 PRO HA H 4.15 0.01 1 140 30 PRO HB2 H 2.23 0.01 1 141 30 PRO HB3 H 1.18 0.01 1 142 30 PRO HG2 H 2.06 0.01 1 143 30 PRO HG3 H 1.86 0.01 1 144 30 PRO HD2 H 3.88 0.01 1 145 30 PRO HD3 H 3.70 0.01 1 146 31 TYR H H 8.60 0.01 1 147 31 TYR HA H 4.40 0.01 1 148 31 TYR HB2 H 3.35 0.01 1 149 31 TYR HB3 H 2.90 0.01 1 150 31 TYR HD1 H 7.11 0.01 1 151 31 TYR HD2 H 7.11 0.01 1 152 31 TYR HE1 H 6.79 0.01 1 153 31 TYR HE2 H 6.79 0.01 1 154 32 TYR H H 8.74 0.01 1 155 32 TYR HA H 4.59 0.01 1 156 32 TYR HB2 H 3.34 0.01 1 157 32 TYR HB3 H 3.19 0.01 1 158 32 TYR HD1 H 6.92 0.01 1 159 32 TYR HD2 H 6.92 0.01 1 160 32 TYR HE1 H 6.57 0.01 1 161 32 TYR HE2 H 6.57 0.01 1 162 33 SER H H 6.77 0.01 1 163 33 SER HA H 5.16 0.01 1 164 33 SER HB2 H 3.52 0.01 1 165 33 SER HB3 H 2.82 0.01 1 166 34 GLN H H 9.07 0.01 1 167 34 GLN HA H 4.79 0.01 1 168 34 GLN HB2 H 1.70 0.01 1 169 34 GLN HB3 H 1.70 0.01 1 170 34 GLN HG2 H 2.26 0.01 1 171 34 GLN HG3 H 2.19 0.01 1 172 34 GLN HE21 H 7.36 0.01 1 173 34 GLN HE22 H 6.86 0.01 1 174 35 CYS H H 8.58 0.01 1 175 35 CYS HA H 4.98 0.01 1 176 35 CYS HB2 H 3.03 0.01 1 177 35 CYS HB3 H 2.74 0.01 1 178 36 LEU H H 9.06 0.01 1 179 36 LEU HA H 4.49 0.01 1 180 36 LEU HB2 H 1.51 0.01 1 181 36 LEU HB3 H 1.51 0.01 1 182 36 LEU HG H 1.36 0.01 1 183 36 LEU HD1 H 0.84 0.01 2 184 36 LEU HD2 H 0.48 0.01 2 stop_ save_