data_4742 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Proton and nitrogen chemical shift assignments for the chitin-binding domain of Bacillus circulans WL-12 Chitinase A1 ; _BMRB_accession_number 4742 _BMRB_flat_file_name bmr4742.str _Entry_type original _Submission_date 2000-05-22 _Accession_date 2000-05-23 _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 Ikegami Takahisa . . 2 Okada Terumasa . . 3 Hashimoto Masayuki . . 4 Seino Shizuka . . 5 Watanabe Takeshi . . 6 Shirakawa Masahiro . . 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" 245 "15N chemical shifts" 51 "coupling constants" 36 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2000-06-15 original author . stop_ _Original_release_date 2000-06-15 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; Solution Structure of the Chitin-Binding Domain of Bacillus circulans WL-12 Chitinase A1 ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code 20250925 _PubMed_ID ? loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Ikegami Takahisa . . 2 Okada Terumasa . . 3 Hashimoto Masayuki . . 4 Seino Shizuka . . 5 Watanabe Takeshi . . 6 Shirakawa Masahiro . . stop_ _Journal_abbreviation 'J. Biol. Chem.' _Journal_volume 275 _Journal_issue 18 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 13654 _Page_last 13661 _Year 2000 _Details . loop_ _Keyword 'twisted beta-sandwich' CBD cellulose ChBD chitin 'binding domain' ChiA1 'chitinase A1' NMR stop_ save_ ####################################### # Cited references within the entry # ####################################### save_ref_1 _Saveframe_category citation _Citation_full . _Citation_title 'Solution structure of the chitin-binding domain of Bacillus circulans WL-12 chitinase A1.' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 10788483 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Ikegami T . . 2 Okada T . . 3 Hashimoto M . . 4 Seino S . . 5 Watanabe T . . 6 Shirakawa M . . stop_ _Journal_abbreviation 'J. Biol. Chem.' _Journal_name_full 'The Journal of biological chemistry' _Journal_volume 275 _Journal_issue 18 _Journal_CSD . _Book_title . _Book_chapter_title . _Book_volume . _Book_series . _Book_publisher . _Book_publisher_city . _Book_ISBN . _Conference_title . _Conference_site . _Conference_state_province . _Conference_country . _Conference_start_date . _Conference_end_date . _Conference_abstract_number . _Thesis_institution . _Thesis_institution_city . _Thesis_institution_country . _Page_first 13654 _Page_last 13661 _Year 2000 _Details ; The three-dimensional structure of the chitin-binding domain (ChBD) of chitinase A1 (ChiA1) from a Gram-positive bacterium, Bacillus circulans WL-12, was determined by means of multidimensional heteronuclear NMR methods. ChiA1 is a glycosidase that hydrolyzes chitin and is composed of an N-terminal catalytic domain, two fibronectin type III-like domains, and C-terminal ChBD(ChiA1) (45 residues, Ala(655)-Gln(699)), which binds specifically to insoluble chitin. ChBD(ChiA1) has a compact and globular structure with the topology of a twisted beta-sandwich. This domain contains two antiparallel beta-sheets, one composed of three strands and the other of two strands. The core region formed by the hydrophobic and aromatic residues makes the overall structure rigid and compact. The overall topology of ChBD(ChiA1) is similar to that of the cellulose-binding domain (CBD) of Erwinia chrysanthemi endoglucanase Z (CBD(EGZ)). However, ChBD(ChiA1) lacks the three aromatic residues aligned linearly and exposed to the solvent, which probably interact with cellulose in CBDs. Therefore, the binding mechanism of a group of ChBDs including ChBD(ChiA1) may be different from that proposed for CBDs. ; save_ ################################## # Molecular system description # ################################## save_ChBD _Saveframe_category molecular_system _Mol_system_name ChBD-ChiA1 _Abbreviation_common ChBD _Enzyme_commission_number 3.2.1.14 loop_ _Mol_system_component_name _Mol_label 'CHITINASE A1, Chitin-binding domain' $ChiA1 stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state monomer _System_paramagnetic no _System_thiol_state 'all free' loop_ _Biological_function 'chitin binding domain of a chitinase' stop_ _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_ChiA1 _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'CHITINASE A1' _Abbreviation_common ChiA1 _Molecular_mass 5018 _Mol_thiol_state 'all free' _Details ; The protein has a T7 tag consisting of 14 residues (H2N-Met-Ala-Ser-Met-Thr-Gly-Gly-Gly-Gly-Met-Gly-Arg-Gly-Ser-) derived from the expression vector at its N-terminus. The calculated weight of the molecule, without the T7 tag region, is 5,018 ; ############################## # Polymer residue sequence # ############################## _Residue_count 59 _Mol_residue_sequence ; MASMTGGGGMGRGSAWQVNT AYTAGQLVTYNGKTYKCLQP HTSLAGWEPSNVPALWQLQ ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 . MET 2 . ALA 3 . SER 4 . MET 5 . THR 6 . GLY 7 . GLY 8 . GLY 9 . GLY 10 . MET 11 . GLY 12 . ARG 13 . GLY 14 . SER 15 655 ALA 16 656 TRP 17 657 GLN 18 658 VAL 19 659 ASN 20 660 THR 21 661 ALA 22 662 TYR 23 663 THR 24 664 ALA 25 665 GLY 26 666 GLN 27 667 LEU 28 668 VAL 29 669 THR 30 670 TYR 31 671 ASN 32 672 GLY 33 673 LYS 34 674 THR 35 675 TYR 36 676 LYS 37 677 CYS 38 678 LEU 39 679 GLN 40 680 PRO 41 681 HIS 42 682 THR 43 683 SER 44 684 LEU 45 685 ALA 46 686 GLY 47 687 TRP 48 688 GLU 49 689 PRO 50 690 SER 51 691 ASN 52 692 VAL 53 693 PRO 54 694 ALA 55 695 LEU 56 696 TRP 57 697 GLN 58 698 LEU 59 699 GLN stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-10-06 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 BMRB 4588 "CHITINASE A1" 100.00 59 100.00 100.00 9.46e-34 PDB 1ED7 "Solution Structure Of The Chitin-Binding Domain Of Bacillus Circulans Wl-12 Chitinase A1" 76.27 45 100.00 100.00 1.18e-23 EMBL CAG28938 "intein-CBD, partial [synthetic construct]" 77.97 517 100.00 100.00 8.85e-25 EMBL CAG28939 "intein-CBD, partial [synthetic construct]" 77.97 518 100.00 100.00 5.47e-25 EMBL CDK12648 "DnaB-Ano fusion protein [synthetic construct]" 77.97 287 100.00 100.00 7.39e-25 EMBL CDK12649 "GyrA-Ano fusion protein [synthetic construct]" 77.97 331 100.00 100.00 1.73e-24 EMBL CDK12650 "RIR1-Ano fusion protein [synthetic construct]" 77.97 267 100.00 100.00 4.23e-24 GB AAA81528 "chitinase A1 [Bacillus circulans]" 77.97 699 100.00 100.00 1.50e-22 GB AAD49604 "chitin binding domain [Expression vector pNam]" 77.97 52 100.00 100.00 3.27e-24 GB AAN07183 "RNA polymerase beta prime subunit/intein-CBD fusion protein [Cloning vector pIA423]" 77.97 1929 100.00 100.00 6.43e-25 GB AAY41169 "SspDnaE-C/CBD fusion protein [Expression vector pSFBAD09]" 77.97 93 100.00 100.00 1.46e-24 GB ABQ96889 "glutaryl 7-aminocephalosporanic acid acylase/modified chitin binding domain fusion protein [synthetic construct]" 77.97 746 97.83 100.00 1.39e-21 REF WP_053782577 "chitinase [Paenibacillus sp. A59]" 77.97 699 97.83 97.83 5.59e-22 SP P20533 "RecName: Full=Chitinase A1; Flags: Precursor" 77.97 699 100.00 100.00 1.50e-22 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species _Strain _Gene_mnemonic $ChiA1 'soil bacteria' 1397 Eubacteria . Bacillus circulans WL12 chiA1 stop_ save_ ######################### # Experimental source # ######################### save_experimental_source _Saveframe_category experimental_source loop_ _Mol_label _Production_method _Host_organism_name_common _Genus _Species _Strain _Vector_type _Vector_name $ChiA1 'recombinant technology' Bacteria Escherichia coli BL21(DE3) plasmid PET3A 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 $ChiA1 2.0 mM [U-15N] KH2PO4-K2HPO4 10 mM . DTT 10 mM [U-2H] H2O 90 % . D2O 10 % . stop_ save_ save_sample_2 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $ChiA1 1.2 mM [U-15N] KH2PO4-K2HPO4 100 mM . DTT 10 mM [U-2H] D2O 99.8 % . stop_ save_ ############################ # Computer software used # ############################ save_X-PLOR _Saveframe_category software _Name X-PLOR _Version 3.851 loop_ _Task refinement stop_ _Details Brunger save_ save_DYANA _Saveframe_category software _Name DYANA _Version 1.5 loop_ _Task 'structure solution' stop_ _Details Guentert save_ save_NMRPipe _Saveframe_category software _Name NMRPipe _Version 1.7 loop_ _Task processing stop_ _Details Delaglio save_ save_XWINNMR _Saveframe_category software _Name XWINNMR _Version 2.0 loop_ _Task collection stop_ _Details Bruker save_ save_nmrPipp _Saveframe_category software _Name nmrPipp _Version 4.2.4 loop_ _Task 'data analysis' stop_ _Details Garrett save_ save_Molmol _Saveframe_category software _Name Molmol _Version 2.3 loop_ _Task 'structure analysis' stop_ _Details Koradi save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model DRX _Field_strength 800 _Details . save_ save_NMR_spectrometer_2 _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_ save_3D_15N-separated_NOESY_2 _Saveframe_category NMR_applied_experiment _Experiment_name '3D 15N-separated_NOESY' _Sample_label . save_ save_HMQC-J_3 _Saveframe_category NMR_applied_experiment _Experiment_name HMQC-J _Sample_label . save_ save_3D_(H)NNH-TOCSY_4 _Saveframe_category NMR_applied_experiment _Experiment_name '3D (H)NNH-TOCSY' _Sample_label . save_ save_2D_H(NN)H-TOCSY_5 _Saveframe_category NMR_applied_experiment _Experiment_name '2D H(NN)H-TOCSY' _Sample_label . save_ save_NMR_spec_expt__0_1 _Saveframe_category NMR_applied_experiment _Experiment_name '2D NOESY' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_2 _Saveframe_category NMR_applied_experiment _Experiment_name '3D 15N-separated_NOESY' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_3 _Saveframe_category NMR_applied_experiment _Experiment_name HMQC-J _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_4 _Saveframe_category NMR_applied_experiment _Experiment_name '3D (H)NNH-TOCSY' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_5 _Saveframe_category NMR_applied_experiment _Experiment_name '2D H(NN)H-TOCSY' _BMRB_pulse_sequence_accession_number . _Details . save_ ####################### # Sample conditions # ####################### save_sample_cond_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 6.0 0.1 n/a temperature 310 0.5 K 'ionic strength' 10 . mM stop_ save_ save_sample_cond_2 _Saveframe_category sample_conditions _Details 'Samples adjusted to pH 6.0 in H2O was lyophilized and then dissolved in the same amount of D2O.' loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 6.0 0.1 n/a temperature 310 0.5 K 'ionic strength' 100 . mM 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 0.00 external direct cylindrical external_to_the_sample parallel_to_Bo . DSS N 15 'methyl protons' ppm 0.0 . indirect . . . 0.101329118 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_ _Sample_label $sample_1 stop_ _Sample_conditions_label $sample_cond_1 _Chem_shift_reference_set_label $chemical_shift_reference _Mol_system_component_name 'CHITINASE A1, Chitin-binding 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 . 15 ALA H H 8.36 0.03 1 2 . 15 ALA HA H 4.69 0.03 1 3 . 15 ALA HB H 1.52 0.03 1 4 . 15 ALA N N 125.17 0.25 1 5 . 16 TRP H H 8.93 0.03 1 6 . 16 TRP HA H 4.29 0.03 1 7 . 16 TRP HB2 H 3.27 0.03 2 8 . 16 TRP HB3 H 2.64 0.03 2 9 . 16 TRP HE1 H 11.12 0.03 1 10 . 16 TRP HD1 H 6.30 0.03 1 11 . 16 TRP HH2 H 7.07 0.03 1 12 . 16 TRP HE3 H 7.46 0.03 1 13 . 16 TRP N N 125.36 0.25 1 14 . 16 TRP NE1 N 130.21 0.25 1 15 . 17 GLN H H 7.59 0.03 1 16 . 17 GLN HA H 4.38 0.03 1 17 . 17 GLN HB2 H 1.71 0.03 2 18 . 17 GLN HB3 H 1.93 0.03 2 19 . 17 GLN HG2 H 2.34 0.03 1 20 . 17 GLN HG3 H 2.34 0.03 1 21 . 17 GLN HE21 H 6.79 0.03 2 22 . 17 GLN HE22 H 7.36 0.03 2 23 . 17 GLN N N 125.35 0.25 1 24 . 17 GLN NE2 N 111.91 0.25 1 25 . 18 VAL H H 7.87 0.03 1 26 . 18 VAL HA H 3.24 0.03 1 27 . 18 VAL HB H 1.96 0.03 1 28 . 18 VAL HG1 H 0.94 0.03 1 29 . 18 VAL HG2 H 0.94 0.03 1 30 . 18 VAL N N 119.02 0.25 1 31 . 19 ASN H H 7.57 0.03 1 32 . 19 ASN HA H 4.39 0.03 1 33 . 19 ASN HB2 H 3.04 0.03 2 34 . 19 ASN HB3 H 2.70 0.03 2 35 . 19 ASN HD21 H 7.52 0.03 2 36 . 19 ASN HD22 H 6.73 0.03 2 37 . 19 ASN N N 122.94 0.25 1 38 . 19 ASN ND2 N 112.09 0.25 1 39 . 20 THR H H 8.26 0.03 1 40 . 20 THR HA H 4.18 0.03 1 41 . 20 THR HB H 3.36 0.03 1 42 . 20 THR HG2 H 0.45 0.03 1 43 . 20 THR N N 115.05 0.25 1 44 . 21 ALA H H 8.24 0.03 1 45 . 21 ALA HA H 4.54 0.03 1 46 . 21 ALA HB H 1.21 0.03 1 47 . 21 ALA N N 129.51 0.25 1 48 . 22 TYR H H 8.72 0.03 1 49 . 22 TYR HA H 5.13 0.03 1 50 . 22 TYR HB2 H 3.15 0.03 2 51 . 22 TYR HB3 H 2.23 0.03 2 52 . 22 TYR HD1 H 7.17 0.03 3 53 . 22 TYR HE1 H 6.74 0.03 3 54 . 22 TYR N N 124.37 0.25 1 55 . 23 THR H H 8.74 0.03 1 56 . 23 THR HA H 4.50 0.03 1 57 . 23 THR HB H 4.30 0.03 1 58 . 23 THR HG2 H 1.25 0.03 1 59 . 23 THR N N 114.00 0.25 1 60 . 24 ALA H H 8.30 0.03 1 61 . 24 ALA HA H 3.67 0.03 1 62 . 24 ALA HB H 1.27 0.03 1 63 . 24 ALA N N 123.30 0.25 1 64 . 25 GLY H H 9.31 0.03 1 65 . 25 GLY HA2 H 3.41 0.03 1 66 . 25 GLY HA3 H 4.55 0.03 2 67 . 25 GLY N N 111.67 0.25 1 68 . 26 GLN H H 7.78 0.03 1 69 . 26 GLN HA H 4.31 0.03 1 70 . 26 GLN HB2 H 2.27 0.03 2 71 . 26 GLN HB3 H 2.50 0.03 2 72 . 26 GLN HG2 H 2.63 0.03 2 73 . 26 GLN HG3 H 2.77 0.03 2 74 . 26 GLN HE21 H 7.15 0.03 2 75 . 26 GLN HE22 H 7.78 0.03 2 76 . 26 GLN N N 121.11 0.25 1 77 . 26 GLN NE2 N 110.55 0.25 1 78 . 27 LEU H H 8.66 0.03 1 79 . 27 LEU HA H 5.86 0.03 1 80 . 27 LEU HB2 H 1.89 0.03 2 81 . 27 LEU HB3 H 1.33 0.03 2 82 . 27 LEU HD1 H 0.97 0.03 1 83 . 27 LEU HD2 H 0.90 0.03 1 84 . 27 LEU N N 123.79 0.25 1 85 . 28 VAL H H 9.20 0.03 1 86 . 28 VAL HA H 5.53 0.03 1 87 . 28 VAL HB H 2.33 0.03 1 88 . 28 VAL HG1 H 0.94 0.03 1 89 . 28 VAL HG2 H 0.29 0.03 1 90 . 28 VAL N N 114.95 0.25 1 91 . 29 THR H H 8.38 0.03 1 92 . 29 THR HA H 5.60 0.03 1 93 . 29 THR HB H 4.01 0.03 1 94 . 29 THR HG2 H 1.13 0.03 1 95 . 29 THR N N 112.03 0.25 1 96 . 30 TYR H H 9.39 0.03 1 97 . 30 TYR HA H 4.77 0.03 1 98 . 30 TYR HB2 H 2.69 0.03 2 99 . 30 TYR HB3 H 2.48 0.03 2 100 . 30 TYR HD1 H 7.01 0.03 3 101 . 30 TYR HE1 H 6.79 0.03 3 102 . 30 TYR N N 122.42 0.25 1 103 . 31 ASN HD21 H 6.52 0.03 2 104 . 31 ASN HD22 H 7.04 0.03 2 105 . 31 ASN ND2 N 109.90 0.25 1 106 . 32 GLY HA2 H 3.63 0.03 2 107 . 32 GLY HA3 H 4.16 0.03 2 108 . 33 LYS H H 7.63 0.03 1 109 . 33 LYS HA H 4.68 0.03 1 110 . 33 LYS HB2 H 1.76 0.03 1 111 . 33 LYS HB3 H 1.76 0.03 1 112 . 33 LYS HG2 H 1.43 0.03 1 113 . 33 LYS HG3 H 1.43 0.03 1 114 . 33 LYS HD2 H 1.60 0.03 1 115 . 33 LYS HD3 H 1.60 0.03 1 116 . 33 LYS HE2 H 3.07 0.03 1 117 . 33 LYS HE3 H 3.07 0.03 1 118 . 33 LYS N N 120.52 0.25 1 119 . 34 THR H H 8.72 0.03 1 120 . 34 THR HA H 5.13 0.03 1 121 . 34 THR HB H 3.87 0.03 1 122 . 34 THR HG2 H 1.22 0.03 1 123 . 34 THR N N 118.17 0.25 1 124 . 35 TYR H H 9.37 0.03 1 125 . 35 TYR HA H 5.33 0.03 1 126 . 35 TYR HB2 H 2.89 0.03 2 127 . 35 TYR HB3 H 2.44 0.03 2 128 . 35 TYR HD1 H 6.69 0.03 3 129 . 35 TYR HE1 H 6.87 0.03 3 130 . 35 TYR N N 122.42 0.25 1 131 . 36 LYS H H 9.35 0.03 1 132 . 36 LYS HA H 5.39 0.03 1 133 . 36 LYS HB2 H 1.86 0.03 2 134 . 36 LYS HB3 H 1.72 0.03 2 135 . 36 LYS HG2 H 1.29 0.03 1 136 . 36 LYS HG3 H 1.29 0.03 1 137 . 36 LYS HD2 H 1.52 0.03 1 138 . 36 LYS HD3 H 1.52 0.03 1 139 . 36 LYS HE2 H 2.96 0.03 1 140 . 36 LYS HE3 H 2.96 0.03 1 141 . 36 LYS N N 121.59 0.25 1 142 . 37 CYS H H 9.48 0.03 1 143 . 37 CYS HA H 3.64 0.03 1 144 . 37 CYS HB2 H 2.86 0.03 2 145 . 37 CYS HB3 H 2.56 0.03 2 146 . 37 CYS N N 129.28 0.25 1 147 . 38 LEU H H 8.97 0.03 1 148 . 38 LEU HA H 4.42 0.03 1 149 . 38 LEU HB2 H 1.59 0.03 2 150 . 38 LEU HB3 H 1.47 0.03 2 151 . 38 LEU HD1 H 0.81 0.03 1 152 . 38 LEU HD2 H 0.81 0.03 1 153 . 38 LEU N N 130.58 0.25 1 154 . 39 GLN H H 7.02 0.03 1 155 . 39 GLN HA H 4.93 0.03 1 156 . 39 GLN HB2 H 1.98 0.03 2 157 . 39 GLN HB3 H 1.75 0.03 2 158 . 39 GLN HG2 H 2.27 0.03 1 159 . 39 GLN HG3 H 2.27 0.03 1 160 . 39 GLN HE21 H 6.79 0.03 2 161 . 39 GLN HE22 H 7.19 0.03 2 162 . 39 GLN N N 116.87 0.25 1 163 . 39 GLN NE2 N 110.86 0.25 1 164 . 40 PRO HA H 4.69 0.03 1 165 . 40 PRO HB2 H 2.19 0.03 2 166 . 40 PRO HB3 H 2.32 0.03 2 167 . 40 PRO HG2 H 1.27 0.03 1 168 . 40 PRO HG3 H 1.27 0.03 1 169 . 40 PRO HD2 H 3.67 0.03 2 170 . 40 PRO HD3 H 3.96 0.03 2 171 . 41 HIS H H 8.28 0.03 1 172 . 41 HIS HA H 4.84 0.03 1 173 . 41 HIS HB2 H 3.43 0.03 2 174 . 41 HIS HB3 H 3.28 0.03 2 175 . 41 HIS HD2 H 7.03 0.03 1 176 . 41 HIS HE1 H 7.23 0.03 1 177 . 41 HIS N N 117.71 0.25 1 178 . 42 THR H H 8.52 0.03 1 179 . 42 THR HA H 5.05 0.03 1 180 . 42 THR HB H 3.97 0.03 1 181 . 42 THR HG2 H 1.05 0.03 1 182 . 42 THR N N 116.85 0.25 1 183 . 43 SER H H 9.45 0.03 1 184 . 43 SER HA H 4.78 0.03 1 185 . 43 SER HB2 H 4.54 0.03 2 186 . 43 SER HB3 H 4.65 0.03 2 187 . 43 SER N N 124.09 0.25 1 188 . 44 LEU H H 6.79 0.03 1 189 . 44 LEU HA H 4.70 0.03 1 190 . 44 LEU HB2 H 1.40 0.03 1 191 . 44 LEU HB3 H 1.40 0.03 1 192 . 44 LEU HG H 0.89 0.03 1 193 . 44 LEU HD2 H 0.65 0.03 1 194 . 44 LEU HD1 H 0.29 0.03 1 195 . 44 LEU N N 118.25 0.25 1 196 . 45 ALA H H 8.61 0.03 1 197 . 45 ALA HA H 4.44 0.03 1 198 . 45 ALA HB H 1.51 0.03 1 199 . 45 ALA N N 124.72 0.25 1 200 . 46 GLY H H 9.54 0.03 1 201 . 46 GLY HA2 H 4.52 0.03 2 202 . 46 GLY HA3 H 3.97 0.03 2 203 . 46 GLY N N 114.78 0.25 1 204 . 47 TRP H H 8.46 0.03 1 205 . 47 TRP HA H 5.11 0.03 1 206 . 47 TRP HB2 H 3.81 0.03 2 207 . 47 TRP HB3 H 3.54 0.03 2 208 . 47 TRP HE1 H 10.04 0.03 1 209 . 47 TRP HD1 H 7.05 0.03 1 210 . 47 TRP HZ2 H 7.51 0.03 1 211 . 47 TRP HH2 H 7.32 0.03 1 212 . 47 TRP HZ3 H 7.25 0.03 1 213 . 47 TRP HE3 H 7.66 0.03 1 214 . 47 TRP N N 121.76 0.25 1 215 . 47 TRP NE1 N 127.55 0.25 1 216 . 48 GLU H H 8.68 0.03 1 217 . 48 GLU HA H 4.47 0.03 1 218 . 48 GLU HB2 H 0.12 0.03 2 219 . 48 GLU HB3 H 1.23 0.03 2 220 . 48 GLU HG2 H 1.47 0.03 2 221 . 48 GLU HG3 H 2.19 0.03 2 222 . 48 GLU N N 120.02 0.25 1 223 . 49 PRO HD2 H 3.79 0.03 2 224 . 49 PRO HD3 H 4.05 0.03 2 225 . 50 SER H H 5.62 0.03 1 226 . 50 SER HA H 3.97 0.03 1 227 . 50 SER HB2 H 3.81 0.03 2 228 . 50 SER HB3 H 4.06 0.03 2 229 . 50 SER N N 102.76 0.25 1 230 . 51 ASN H H 7.94 0.03 1 231 . 51 ASN HA H 4.98 0.03 1 232 . 51 ASN HB2 H 2.98 0.03 2 233 . 51 ASN HB3 H 2.75 0.03 2 234 . 51 ASN HD21 H 6.88 0.03 2 235 . 51 ASN HD22 H 7.51 0.03 2 236 . 51 ASN N N 117.95 0.25 1 237 . 51 ASN ND2 N 114.45 0.25 1 238 . 52 VAL H H 6.72 0.03 1 239 . 52 VAL HA H 4.88 0.03 1 240 . 52 VAL HB H 2.01 0.03 1 241 . 52 VAL HG2 H 0.95 0.03 1 242 . 52 VAL HG1 H 0.73 0.03 1 243 . 52 VAL N N 112.80 0.25 1 244 . 53 PRO HD2 H 3.40 0.03 2 245 . 53 PRO HD3 H 3.81 0.03 2 246 . 54 ALA H H 8.10 0.03 1 247 . 54 ALA HA H 4.16 0.03 1 248 . 54 ALA HB H 1.23 0.03 1 249 . 54 ALA N N 116.81 0.25 1 250 . 55 LEU H H 7.59 0.03 1 251 . 55 LEU HA H 4.15 0.03 1 252 . 55 LEU HB2 H 1.45 0.03 2 253 . 55 LEU HB3 H 0.72 0.03 2 254 . 55 LEU HG H 1.03 0.03 1 255 . 55 LEU HD2 H 0.15 0.03 1 256 . 55 LEU HD1 H -0.11 0.03 1 257 . 55 LEU N N 113.72 0.25 1 258 . 56 TRP H H 7.61 0.03 1 259 . 56 TRP HA H 5.31 0.03 1 260 . 56 TRP HB2 H 2.85 0.03 1 261 . 56 TRP HB3 H 2.85 0.03 1 262 . 56 TRP HE1 H 10.54 0.03 1 263 . 56 TRP HD1 H 6.86 0.03 1 264 . 56 TRP HZ2 H 7.33 0.03 1 265 . 56 TRP HH2 H 6.14 0.03 1 266 . 56 TRP HZ3 H 7.11 0.03 1 267 . 56 TRP HE3 H 7.14 0.03 1 268 . 56 TRP N N 118.40 0.25 1 269 . 56 TRP NE1 N 127.47 0.25 1 270 . 57 GLN H H 9.53 0.03 1 271 . 57 GLN HA H 5.11 0.03 1 272 . 57 GLN HB2 H 2.23 0.03 2 273 . 57 GLN HB3 H 2.16 0.03 2 274 . 57 GLN HG2 H 2.50 0.03 1 275 . 57 GLN HG3 H 2.50 0.03 1 276 . 57 GLN HE21 H 6.85 0.03 2 277 . 57 GLN HE22 H 7.71 0.03 2 278 . 57 GLN N N 122.74 0.25 1 279 . 57 GLN NE2 N 112.24 0.25 1 280 . 58 LEU H H 9.29 0.03 1 281 . 58 LEU HA H 3.91 0.03 1 282 . 58 LEU HB2 H 0.88 0.03 2 283 . 58 LEU HB3 H 1.39 0.03 2 284 . 58 LEU HD2 H 0.84 0.03 1 285 . 58 LEU HD1 H 0.59 0.03 1 286 . 58 LEU N N 135.42 0.25 1 287 . 59 GLN H H 8.52 0.03 1 288 . 59 GLN HA H 4.26 0.03 1 289 . 59 GLN HB2 H 2.13 0.03 2 290 . 59 GLN HB3 H 1.71 0.03 2 291 . 59 GLN HG2 H 2.30 0.03 1 292 . 59 GLN HG3 H 2.30 0.03 1 293 . 59 GLN HE21 H 7.22 0.03 2 294 . 59 GLN HE22 H 6.92 0.03 2 295 . 59 GLN N N 131.69 0.25 1 296 . 59 GLN NE2 N 115.55 0.25 1 stop_ save_ ######################## # Coupling constants # ######################## save_J_values_set_1 _Saveframe_category coupling_constants _Details . loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $sample_cond_1 _Spectrometer_frequency_1H 800 _Mol_system_component_name 'CHITINASE A1, Chitin-binding 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 16 TRP H 16 TRP HA 0.0 . . 0.5 2 3JHNHA 17 GLN H 17 GLN HA 9.6 . . 0.5 3 3JHNHA 18 VAL H 18 VAL HA 4.4 . . 0.5 4 3JHNHA 19 ASN H 19 ASN HA 8.1 . . 0.5 5 3JHNHA 20 THR H 20 THR HA 10.9 . . 0.5 6 3JHNHA 21 ALA H 21 ALA HA 7.5 . . 0.5 7 3JHNHA 22 TYR H 22 TYR HA 10.5 . . 0.5 8 3JHNHA 23 THR H 23 THR HA 10.7 . . 0.5 9 3JHNHA 24 ALA H 24 ALA HA 0.0 . . 0.5 10 3JHNHA 26 GLN H 26 GLN HA 4.1 . . 0.5 11 3JHNHA 27 LEU H 27 LEU HA 9.9 . . 0.5 12 3JHNHA 28 VAL H 28 VAL HA 10.4 . . 0.5 13 3JHNHA 29 THR H 29 THR HA 11.4 . . 0.5 14 3JHNHA 30 TYR H 30 TYR HA 9.2 . . 0.5 15 3JHNHA 33 LYS H 33 LYS HA 10.9 . . 0.5 16 3JHNHA 34 THR H 34 THR HA 10.4 . . 0.5 17 3JHNHA 35 TYR H 35 TYR HA 9.2 . . 0.5 18 3JHNHA 36 LYS H 36 LYS HA 10.6 . . 0.5 19 3JHNHA 37 CYS H 37 CYS HA 2.4 . . 0.5 20 3JHNHA 38 LEU H 38 LEU HA 9.1 . . 0.5 21 3JHNHA 39 GLN H 39 GLN HA 8.9 . . 0.5 22 3JHNHA 41 HIS H 41 HIS HA 5.1 . . 0.5 23 3JHNHA 42 THR H 42 THR HA 10.8 . . 0.5 24 3JHNHA 43 SER H 43 SER HA 0.0 . . 0.5 25 3JHNHA 44 LEU H 44 LEU HA 9.7 . . 0.5 26 3JHNHA 45 ALA H 45 ALA HA 0.0 . . 0.5 27 3JHNHA 47 TRP H 47 TRP HA 10.5 . . 0.5 28 3JHNHA 48 GLU H 48 GLU HA 0.0 . . 0.5 29 3JHNHA 50 SER H 50 SER HA 5.9 . . 0.5 30 3JHNHA 51 ASN H 51 ASN HA 9.7 . . 0.5 31 3JHNHA 52 VAL H 52 VAL HA 11.3 . . 0.5 32 3JHNHA 54 ALA H 54 ALA HA 4.6 . . 0.5 33 3JHNHA 55 LEU H 55 LEU HA 11.0 . . 0.5 34 3JHNHA 56 TRP H 56 TRP HA 10.5 . . 0.5 35 3JHNHA 57 GLN H 57 GLN HA 10.1 . . 0.5 36 3JHNHA 59 GLN H 59 GLN HA 9.9 . . 0.5 stop_ save_