data_4377 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; The Solution Structure of the Type X Cellulose Binding Domain from Pseudomonas xylanase A ; _BMRB_accession_number 4377 _BMRB_flat_file_name bmr4377.str _Entry_type original _Submission_date 1999-08-17 _Accession_date 1999-08-17 _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 Raghothama Srinivasarao . . 2 Simpson Peter J . 3 Szabo L . . 4 Nagy T . . 5 Gilbert Harry J . 6 Williamson Mike P . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 266 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2000-03-02 original author . stop_ _Original_release_date 2000-03-02 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; Solution structure of the CBM10 cellulose binding module from Pseudomonas Xylanase A ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code 20120586 _PubMed_ID 10653641 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Raghothama Srinivasarao . . 2 Simpson Peter J . 3 Szabo L . . 4 Nagy T . . 5 Gilbert Harry J . 6 Williamson Mike P . stop_ _Journal_abbreviation Biochemistry _Journal_name_full 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 978 _Page_last 984 _Year 2000 _Details . save_ ####################################### # Cited references within the entry # ####################################### save_ref._1 _Saveframe_category citation _Citation_full ; Ferreira, LMA, Durrant, AJ, Hall, J, Hazlewood, GP, Gilbert, HJ (1990) Biochem. J., 307, 191-195 ; _Citation_title 'A modular xylanase containing a novel non-catalytic xylan-specific binding domain.' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 7717975 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Black 'G W' W. . 2 Hazlewood 'G P' P. . 3 Millward-Sadler 'S J' J. . 4 Laurie 'J I' I. . 5 Gilbert 'H J' J. . stop_ _Journal_abbreviation 'Biochem. J.' _Journal_name_full 'The Biochemical journal' _Journal_volume '307 ( Pt 1)' _Journal_issue . _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 191 _Page_last 195 _Year 1995 _Details ; Xylanase D (XYLD) from Cellulomonas fimi contains a C-terminal cellulose-binding domain (CBD) and an internal domain that exhibits 65% sequence identity with the C-terminal CBD. Full-length XYLD binds to both cellulose and xylan. Deletion of the C-terminal CBD from XYLD abolishes the capacity of the enzyme to bind to cellulose, although the truncated xylanase retains its xylan-binding properties. A derivative of XYLD lacking both the C-terminal CBD and the internal CBD homologue did not bind to either cellulose or xylan. A fusion protein consisting of the XYLD internal CBD homologue linked to the C-terminus of glutathione S-transferase (GST) bound to xylan, but not to cellulose, while GST bound to neither of the polysaccharides. The Km and specific activity of full-length XYLD and truncated derivatives of the enzyme lacking the C-terminal CBD (XYLDcbd), and both the CBD and the internal CBD homologue (XYLDcd), were determined with soluble and insoluble xylan as the substrates. The data showed that the specific activities of the three enzymes were similar for both substrates, as were the Km values for soluble substrate. However, the Km values of XYLD and XYLDcbd for insoluble xylan were significantly lower than the Km of XYLDcd. Overall, these data indicate that the internal CBD homologue in XYLD constitutes a discrete xylan-binding domain which influences the affinity of the enzyme for insoluble xylan but does not directly affect the catalytic activity of the xylanase. The rationale for the evolution of this domain is discussed. ; save_ save_ref._2 _Saveframe_category citation _Citation_full ; Hall, J, Hazlewood, GP, Huskisson, NS, Durrant, AJ, Gilbert, HJ (1989) Mol. Microbiol., 3, 1211-1219 ; _Citation_title 'Conserved serine-rich sequences in xylanase and cellulase from Pseudomonas fluorescens subspecies cellulosa: internal signal sequence and unusual protein processing.' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 2507868 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Hall J . . 2 Hazlewood 'G P' P. . 3 Huskisson 'N S' S. . 4 Durrant 'A J' J. . 5 Gilbert 'H J' J. . stop_ _Journal_abbreviation 'Mol. Microbiol.' _Journal_name_full 'Molecular microbiology' _Journal_volume 3 _Journal_issue 9 _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 1211 _Page_last 1219 _Year 1989 _Details ; The complete nucleotide sequence of the xynA gene coding for a xylanase (XYLA) expressed by Pseudomonas fluorescens subspecies cellulosa, has been determined. The structural gene consists of an open reading frame of 1833 bp followed by a TAA stop codon. Confirmation of the nucleotide sequence was obtained by comparing the predicted amino acid sequence with that derived by N-terminal analysis of purified forms of the xylanase. The signal peptide present at the N terminus of mature XYLA closely resembles signal peptides of other secreted proteins. Truncated forms of the xylanase gene, in which the sequence encoding the N-terminal signal peptide had been deleted, still expressed coli. XYLA contains domains which are homologous to an endoglucanase expressed by the same organism. These structures include serine-rich sequences. Bal31 deletions of xynA revealed the extent to which these conserved sequences, in XYLA, were essential for xylanase activity. Downstream of the TAA stop codon is a G + C-rich region of dyad symmetry (delta G = 24 kcal) characteristic of E. coli Rho-independent transcription terminators. ; save_ ################################## # Molecular system description # ################################## save_system_CBDX _Saveframe_category molecular_system _Mol_system_name 'type X cellulose binding domain from Pseudomonas xylanase A' _Abbreviation_common CBDX _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label CBDX $CBDX stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state monomer _System_paramagnetic no _System_thiol_state 'all disulfide bound' _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_CBDX _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'type X cellulose binding domain from Pseudomonas xylanase A' _Name_variant Xyl10A _Abbreviation_common CBDX _Molecular_mass . _Mol_thiol_state . _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 75 _Mol_residue_sequence ; HHHHHHHHHHSSGHIAGRHM GNQQCNWYGTLYPLCVTTTN GWGWEDQRSCIARSTCAAQP APFGIVGSGHHHHHH ; loop_ _Residue_seq_code _Residue_label 1 HIS 2 HIS 3 HIS 4 HIS 5 HIS 6 HIS 7 HIS 8 HIS 9 HIS 10 HIS 11 SER 12 SER 13 GLY 14 HIS 15 ILE 16 ALA 17 GLY 18 ARG 19 HIS 20 MET 21 GLY 22 ASN 23 GLN 24 GLN 25 CYS 26 ASN 27 TRP 28 TYR 29 GLY 30 THR 31 LEU 32 TYR 33 PRO 34 LEU 35 CYS 36 VAL 37 THR 38 THR 39 THR 40 ASN 41 GLY 42 TRP 43 GLY 44 TRP 45 GLU 46 ASP 47 GLN 48 ARG 49 SER 50 CYS 51 ILE 52 ALA 53 ARG 54 SER 55 THR 56 CYS 57 ALA 58 ALA 59 GLN 60 PRO 61 ALA 62 PRO 63 PHE 64 GLY 65 ILE 66 VAL 67 GLY 68 SER 69 GLY 70 HIS 71 HIS 72 HIS 73 HIS 74 HIS 75 HIS stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-03-16 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 1E8R "Solution Structure Of Type X Cbd" 66.67 50 100.00 100.00 8.58e-30 PDB 1QLD "Solution Structure Of Type X Cbm" 66.67 50 100.00 100.00 8.58e-30 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 $CBDX 'P. fluorescens' 29436 Eubacteria . Pseudomonas fluorescens cellulosa 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 $CBDX 'recombinant technology' 'E. coli' Escherichia coli BL21 . stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_one _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $CBDX 1 mM . stop_ save_ ############################ # Computer software used # ############################ save_FELIX _Saveframe_category software _Name FELIX _Version 97.0 _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer_one _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model DRX _Field_strength 500 _Details . save_ save_NMR_spectrometer_two _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model DRX _Field_strength 600 _Details . save_ ############################# # NMR applied experiments # ############################# save_Homonuclear_1 _Saveframe_category NMR_applied_experiment _Experiment_name Homonuclear _Sample_label . save_ save_TOCSY_2 _Saveframe_category NMR_applied_experiment _Experiment_name TOCSY _Sample_label . save_ save_NOESY_3 _Saveframe_category NMR_applied_experiment _Experiment_name NOESY _Sample_label . save_ save_DQFC_4 _Saveframe_category NMR_applied_experiment _Experiment_name DQFC _Sample_label . save_ save_E.COSY_5 _Saveframe_category NMR_applied_experiment _Experiment_name E.COSY _Sample_label . save_ save_NMR_spec_expt__0_1 _Saveframe_category NMR_applied_experiment _Experiment_name Homonuclear _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_2 _Saveframe_category NMR_applied_experiment _Experiment_name TOCSY _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_3 _Saveframe_category NMR_applied_experiment _Experiment_name NOESY _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_4 _Saveframe_category NMR_applied_experiment _Experiment_name DQFC _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_5 _Saveframe_category NMR_applied_experiment _Experiment_name E.COSY _BMRB_pulse_sequence_accession_number . _Details . save_ ####################### # Sample conditions # ####################### save_experimental_conditions_one _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH* 4.5 0.2 n/a temperature 323 1 K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference_set_one _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 TSP H 1 'methyl protons' ppm 0.00 internal direct . . . 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_assigned_chemical_shifts_set_one _Saveframe_category assigned_chemical_shifts _Details . loop_ _Sample_label $sample_one stop_ _Sample_conditions_label $experimental_conditions_one _Chem_shift_reference_set_label $chemical_shift_reference_set_one _Mol_system_component_name CBDX _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 . 21 GLY H H 8.48 0.015 1 2 . 21 GLY HA2 H 3.98 0.015 1 3 . 21 GLY HA3 H 3.98 0.015 1 4 . 22 ASN H H 8.24 0.015 1 5 . 22 ASN HA H 4.75 0.015 1 6 . 22 ASN HB2 H 2.76 0.015 2 7 . 22 ASN HB3 H 2.85 0.015 2 8 . 23 GLN H H 8.10 0.015 1 9 . 23 GLN HA H 4.85 0.015 1 10 . 23 GLN HB2 H 1.92 0.015 1 11 . 23 GLN HB3 H 1.98 0.015 1 12 . 23 GLN HG2 H 2.24 0.015 2 13 . 23 GLN HG3 H 2.36 0.015 2 14 . 23 GLN HE21 H 6.78 0.015 2 15 . 23 GLN HE22 H 7.31 0.015 2 16 . 24 GLN H H 8.70 0.015 1 17 . 24 GLN HA H 4.73 0.015 1 18 . 24 GLN HB2 H 1.75 0.015 4 19 . 24 GLN HB3 H 2.10 0.015 4 20 . 24 GLN HG2 H 2.15 0.015 4 21 . 24 GLN HG3 H 2.15 0.015 4 22 . 24 GLN HE21 H 6.45 0.015 2 23 . 24 GLN HE22 H 7.14 0.015 2 24 . 25 CYS H H 9.73 0.015 1 25 . 25 CYS HA H 4.99 0.015 1 26 . 25 CYS HB2 H 3.07 0.015 1 27 . 25 CYS HB3 H 2.68 0.015 1 28 . 26 ASN H H 9.12 0.015 1 29 . 26 ASN HA H 4.77 0.015 1 30 . 26 ASN HB2 H 2.50 0.015 1 31 . 26 ASN HB3 H 3.46 0.015 1 32 . 26 ASN HD21 H 6.82 0.015 2 33 . 26 ASN HD22 H 7.30 0.015 2 34 . 27 TRP H H 9.22 0.015 1 35 . 27 TRP HA H 5.12 0.015 1 36 . 27 TRP HB2 H 2.70 0.015 1 37 . 27 TRP HB3 H 3.85 0.015 1 38 . 27 TRP HD1 H 7.21 0.015 1 39 . 27 TRP HE1 H 9.53 0.015 1 40 . 27 TRP HE3 H 7.57 0.015 1 41 . 27 TRP HZ2 H 7.46 0.015 1 42 . 27 TRP HZ3 H 6.90 0.015 1 43 . 27 TRP HH2 H 7.22 0.015 1 44 . 28 TYR H H 8.05 0.015 1 45 . 28 TYR HA H 1.20 0.015 1 46 . 28 TYR HB2 H 2.17 0.015 1 47 . 28 TYR HB3 H 2.72 0.015 1 48 . 28 TYR HD1 H 5.57 0.015 1 49 . 28 TYR HD2 H 5.57 0.015 1 50 . 28 TYR HE1 H 5.88 0.015 1 51 . 28 TYR HE2 H 5.88 0.015 1 52 . 29 GLY H H 7.15 0.015 1 53 . 29 GLY HA2 H 3.90 0.015 1 54 . 29 GLY HA3 H 3.90 0.015 1 55 . 30 THR H H 8.05 0.015 1 56 . 30 THR HA H 4.55 0.015 1 57 . 30 THR HB H 4.30 0.015 1 58 . 30 THR HG2 H 1.13 0.015 1 59 . 31 LEU H H 8.27 0.015 1 60 . 31 LEU HA H 5.29 0.015 1 61 . 31 LEU HB2 H 1.20 0.015 2 62 . 31 LEU HB3 H 1.63 0.015 2 63 . 31 LEU HG H 1.62 0.015 1 64 . 31 LEU HD1 H 0.70 0.015 2 65 . 31 LEU HD2 H 0.82 0.015 2 66 . 32 TYR H H 9.22 0.015 1 67 . 32 TYR HA H 4.86 0.015 1 68 . 32 TYR HB2 H 2.30 0.015 1 69 . 32 TYR HB3 H 2.92 0.015 1 70 . 32 TYR HD1 H 7.22 0.015 1 71 . 32 TYR HD2 H 7.22 0.015 1 72 . 32 TYR HE1 H 6.98 0.015 1 73 . 32 TYR HE2 H 6.98 0.015 1 74 . 33 PRO HA H 4.63 0.015 1 75 . 33 PRO HB2 H 1.75 0.015 2 76 . 33 PRO HB3 H 2.36 0.015 2 77 . 33 PRO HG2 H 1.93 0.015 2 78 . 33 PRO HG3 H 2.07 0.015 2 79 . 33 PRO HD2 H 3.86 0.015 2 80 . 33 PRO HD3 H 4.10 0.015 2 81 . 34 LEU H H 8.22 0.015 1 82 . 34 LEU HA H 5.27 0.015 1 83 . 34 LEU HB2 H 1.32 0.015 2 84 . 34 LEU HB3 H 1.60 0.015 2 85 . 34 LEU HG H 1.49 0.015 1 86 . 34 LEU HD1 H 0.80 0.015 1 87 . 34 LEU HD2 H 0.80 0.015 1 88 . 35 CYS H H 8.10 0.015 1 89 . 35 CYS HA H 4.56 0.015 1 90 . 35 CYS HB2 H 2.27 0.015 2 91 . 35 CYS HB3 H 3.72 0.015 2 92 . 36 VAL H H 10.79 0.015 1 93 . 36 VAL HA H 4.18 0.015 1 94 . 36 VAL HB H 2.10 0.015 1 95 . 36 VAL HG1 H 0.92 0.015 1 96 . 36 VAL HG2 H 0.98 0.015 1 97 . 37 THR H H 8.94 0.015 1 98 . 37 THR HA H 4.35 0.015 1 99 . 37 THR HB H 4.22 0.015 1 100 . 37 THR HG2 H 1.20 0.015 1 101 . 38 THR H H 7.69 0.015 1 102 . 38 THR HA H 4.27 0.015 1 103 . 38 THR HB H 3.81 0.015 1 104 . 38 THR HG2 H 1.02 0.015 1 105 . 39 THR H H 8.47 0.015 1 106 . 39 THR HA H 4.22 0.015 4 107 . 39 THR HB H 4.22 0.015 4 108 . 39 THR HG2 H 1.21 0.015 1 109 . 40 ASN H H 7.42 0.015 1 110 . 40 ASN HA H 4.52 0.015 1 111 . 40 ASN HB2 H 2.60 0.015 1 112 . 40 ASN HB3 H 2.60 0.015 1 113 . 41 GLY H H 8.43 0.015 1 114 . 41 GLY HA2 H 3.59 0.015 2 115 . 41 GLY HA3 H 4.12 0.015 2 116 . 42 TRP H H 8.14 0.015 1 117 . 42 TRP HA H 4.87 0.015 1 118 . 42 TRP HB2 H 2.86 0.015 1 119 . 42 TRP HB3 H 3.30 0.015 1 120 . 42 TRP HD1 H 6.99 0.015 1 121 . 42 TRP HE1 H 8.52 0.015 1 122 . 42 TRP HE3 H 7.24 0.015 1 123 . 42 TRP HZ2 H 5.62 0.015 1 124 . 42 TRP HZ3 H 6.02 0.015 1 125 . 42 TRP HH2 H 5.60 0.015 1 126 . 43 GLY H H 9.02 0.015 1 127 . 43 GLY HA2 H 3.80 0.015 2 128 . 43 GLY HA3 H 4.81 0.015 2 129 . 44 TRP H H 8.49 0.015 1 130 . 44 TRP HA H 5.26 0.015 1 131 . 44 TRP HB2 H 2.91 0.015 1 132 . 44 TRP HB3 H 3.25 0.015 1 133 . 44 TRP HD1 H 7.07 0.015 1 134 . 44 TRP HE1 H 9.75 0.015 1 135 . 44 TRP HE3 H 7.46 0.015 1 136 . 44 TRP HZ2 H 7.30 0.015 1 137 . 44 TRP HZ3 H 7.12 0.015 1 138 . 44 TRP HH2 H 7.20 0.015 1 139 . 45 GLU H H 8.20 0.015 1 140 . 45 GLU HA H 4.51 0.015 1 141 . 45 GLU HB2 H 1.58 0.015 2 142 . 45 GLU HB3 H 1.92 0.015 2 143 . 45 GLU HG2 H 2.20 0.015 2 144 . 45 GLU HG3 H 2.38 0.015 2 145 . 46 ASP H H 9.00 0.015 1 146 . 46 ASP HA H 4.15 0.015 1 147 . 46 ASP HB2 H 2.48 0.015 2 148 . 46 ASP HB3 H 2.86 0.015 2 149 . 47 GLN H H 8.15 0.015 1 150 . 47 GLN HA H 3.03 0.015 1 151 . 47 GLN HB2 H 2.15 0.015 4 152 . 47 GLN HB3 H 2.15 0.015 4 153 . 47 GLN HG2 H 2.28 0.015 4 154 . 47 GLN HG3 H 2.28 0.015 4 155 . 47 GLN HE21 H 6.71 0.015 2 156 . 47 GLN HE22 H 7.30 0.015 2 157 . 48 ARG H H 6.72 0.015 1 158 . 48 ARG HA H 4.04 0.015 1 159 . 48 ARG HB2 H 1.76 0.015 1 160 . 48 ARG HB3 H 1.76 0.015 1 161 . 48 ARG HG2 H 1.41 0.015 2 162 . 48 ARG HG3 H 1.58 0.015 2 163 . 48 ARG HD2 H 3.05 0.015 2 164 . 48 ARG HD3 H 3.15 0.015 2 165 . 48 ARG HE H 7.20 0.015 1 166 . 49 SER H H 8.03 0.015 1 167 . 49 SER HA H 5.07 0.015 1 168 . 49 SER HB2 H 4.10 0.015 1 169 . 49 SER HB3 H 4.03 0.015 1 170 . 50 CYS H H 8.55 0.015 1 171 . 50 CYS HA H 5.11 0.015 1 172 . 50 CYS HB2 H 2.90 0.015 1 173 . 50 CYS HB3 H 2.80 0.015 1 174 . 51 ILE H H 8.30 0.015 1 175 . 51 ILE HA H 3.82 0.015 1 176 . 51 ILE HB H 0.34 0.015 1 177 . 51 ILE HG12 H -0.95 0.015 2 178 . 51 ILE HG13 H 0.00 0.015 2 179 . 51 ILE HG2 H 0.30 0.015 1 180 . 51 ILE HD1 H -0.75 0.015 1 181 . 52 ALA H H 8.17 0.015 1 182 . 52 ALA HA H 4.03 0.015 1 183 . 52 ALA HB H 1.11 0.015 1 184 . 53 ARG H H 8.89 0.015 1 185 . 53 ARG HA H 3.70 0.015 1 186 . 53 ARG HB2 H 1.86 0.015 1 187 . 53 ARG HB3 H 1.86 0.015 1 188 . 53 ARG HG2 H 1.58 0.015 2 189 . 53 ARG HG3 H 1.69 0.015 2 190 . 53 ARG HD2 H 3.27 0.015 1 191 . 53 ARG HD3 H 3.27 0.015 1 192 . 53 ARG HE H 7.41 0.015 1 193 . 54 SER H H 8.94 0.015 1 194 . 54 SER HA H 4.07 0.015 1 195 . 54 SER HB2 H 3.94 0.015 2 196 . 54 SER HB3 H 4.00 0.015 2 197 . 55 THR H H 6.82 0.015 1 198 . 55 THR HA H 4.07 0.015 1 199 . 55 THR HB H 3.75 0.015 1 200 . 55 THR HG2 H 1.22 0.015 1 201 . 56 CYS H H 8.49 0.015 1 202 . 56 CYS HA H 4.26 0.015 1 203 . 56 CYS HB2 H 2.69 0.015 1 204 . 56 CYS HB3 H 3.32 0.015 1 205 . 57 ALA H H 8.28 0.015 1 206 . 57 ALA HA H 4.36 0.015 1 207 . 57 ALA HB H 1.50 0.015 1 208 . 58 ALA H H 7.17 0.015 1 209 . 58 ALA HA H 4.48 0.015 1 210 . 58 ALA HB H 1.60 0.015 1 211 . 59 GLN H H 7.10 0.015 1 212 . 59 GLN HA H 4.25 0.015 1 213 . 59 GLN HB2 H 1.42 0.015 2 214 . 59 GLN HB3 H 1.52 0.015 2 215 . 59 GLN HG2 H 1.95 0.015 2 216 . 59 GLN HG3 H 2.56 0.015 2 217 . 59 GLN HE21 H 7.25 0.015 2 218 . 59 GLN HE22 H 7.92 0.015 2 219 . 60 PRO HA H 4.58 0.015 1 220 . 60 PRO HB2 H 2.10 0.015 2 221 . 60 PRO HB3 H 2.30 0.015 2 222 . 60 PRO HG2 H 2.22 0.015 1 223 . 60 PRO HG3 H 2.22 0.015 1 224 . 60 PRO HD2 H 3.58 0.015 2 225 . 60 PRO HD3 H 3.80 0.015 2 226 . 61 ALA H H 7.95 0.015 1 227 . 61 ALA HA H 4.22 0.015 1 228 . 61 ALA HB H 1.25 0.015 1 229 . 62 PRO HA H 4.38 0.015 1 230 . 62 PRO HB2 H 1.76 0.015 2 231 . 62 PRO HB3 H 2.15 0.015 2 232 . 62 PRO HG2 H 0.52 0.015 2 233 . 62 PRO HG3 H 1.52 0.015 2 234 . 62 PRO HD2 H 3.02 0.015 1 235 . 62 PRO HD3 H 3.02 0.015 1 236 . 63 PHE H H 7.89 0.015 1 237 . 63 PHE HA H 4.52 0.015 1 238 . 63 PHE HB2 H 2.38 0.015 2 239 . 63 PHE HB3 H 3.60 0.015 2 240 . 63 PHE HD1 H 6.84 0.015 1 241 . 63 PHE HD2 H 6.84 0.015 1 242 . 63 PHE HE1 H 7.22 0.015 1 243 . 63 PHE HE2 H 7.22 0.015 1 244 . 63 PHE HZ H 7.16 0.015 1 245 . 64 GLY H H 7.93 0.015 1 246 . 64 GLY HA2 H 3.78 0.015 2 247 . 64 GLY HA3 H 4.71 0.015 2 248 . 65 ILE H H 8.66 0.015 1 249 . 65 ILE HA H 4.29 0.015 1 250 . 65 ILE HB H 1.75 0.015 1 251 . 65 ILE HG12 H 0.99 0.015 2 252 . 65 ILE HG13 H 1.09 0.015 2 253 . 65 ILE HG2 H 0.90 0.015 1 254 . 65 ILE HD1 H 1.57 0.015 1 255 . 66 VAL H H 8.81 0.015 1 256 . 66 VAL HA H 4.56 0.015 1 257 . 66 VAL HB H 2.14 0.015 1 258 . 66 VAL HG1 H 0.97 0.015 1 259 . 66 VAL HG2 H 0.85 0.015 1 260 . 67 GLY H H 8.35 0.015 1 261 . 67 GLY HA2 H 4.15 0.015 1 262 . 67 GLY HA3 H 4.15 0.015 1 263 . 68 SER H H 8.19 0.015 1 264 . 68 SER HA H 4.49 0.015 1 265 . 68 SER HB2 H 3.82 0.015 2 266 . 68 SER HB3 H 3.88 0.015 2 stop_ save_