data_3322 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Characterisation of a cellulosome dockerin domain from the anaerobic fungus Piromyces equi ; _BMRB_accession_number 3322 _BMRB_flat_file_name bmr3322.str _Entry_type original _Submission_date 2001-09-10 _Accession_date 2001-09-10 _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 Srinivasrao . . 2 Eberhardt Ruth Y . 3 Simpson Peter J . 4 Wigelsworth Darran . . 5 White Peter . . 6 Hazlewood Geoffrey P . 7 Nagy Tibor . . 8 Gilbert Harry J . 9 Williamson Michael P . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 281 "15N chemical shifts" 62 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2010-06-17 revision BMRB 'Complete natural source information' 1999-06-14 revision BMRB 'Converted to BMRB NMR-STAR V 2.1 format' 1996-03-25 reformat BMRB 'Converted to the BMRB 1996-03-01 STAR flat-file format' 1995-07-31 original BMRB 'Last release in original BMRB flat-file format' stop_ save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; Characterisation of a cellulosome dockerin domain from the anaerobic fungus Piromyces equi ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 11524680 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Raghothama Srinivasrao . . 2 Eberhardt Ruth Y . 3 Simpson Peter J . 4 Wigelsworth Darran . . 5 White Peter . . 6 Hazlewood Geoffrey P . 7 Nagy Tibor . . 8 Gilbert Harry J . 9 Williamson Michael P . stop_ _Journal_abbreviation 'Nat. Struct. Biol.' _Journal_volume 8 _Journal_issue 9 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 775 _Page_last 778 _Year 2001 _Details . loop_ _Keyword cellulase cellulosome dockerin stop_ save_ ################################## # Molecular system description # ################################## save_system_dockerin _Saveframe_category molecular_system _Mol_system_name 'endoglucanase Cel45A' _Abbreviation_common dockerin _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label dockerin $dockerin stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state monomer _System_paramagnetic no _System_thiol_state 'all disulfide bound' loop_ _Biological_function 'protein docking domain' stop_ _Database_query_date . _Details ; For structure calculations, only first 46 residues are considered. Also the N-terminal residue Gly is replaced by Ala. ; save_ ######################## # Monomeric polymers # ######################## save_dockerin _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common dockerin _Abbreviation_common dockerin _Molecular_mass . _Mol_thiol_state 'all disulfide bound' _Details ; For structure calculations, only first 46 residues are considered. Also the N-terminal residue Gly is replaced by Ala. ; ############################## # Polymer residue sequence # ############################## _Residue_count 52 _Mol_residue_sequence ; GSCWAQSQGYNCCNNPSSTK VEYTDASGQWGVQNGQWCGI DYSYGQNQGNES ; loop_ _Residue_seq_code _Residue_label 1 GLY 2 SER 3 CYS 4 TRP 5 ALA 6 GLN 7 SER 8 GLN 9 GLY 10 TYR 11 ASN 12 CYS 13 CYS 14 ASN 15 ASN 16 PRO 17 SER 18 SER 19 THR 20 LYS 21 VAL 22 GLU 23 TYR 24 THR 25 ASP 26 ALA 27 SER 28 GLY 29 GLN 30 TRP 31 GLY 32 VAL 33 GLN 34 ASN 35 GLY 36 GLN 37 TRP 38 CYS 39 GLY 40 ILE 41 ASP 42 TYR 43 SER 44 TYR 45 GLY 46 GLN 47 ASN 48 GLN 49 GLY 50 ASN 51 GLU 52 SER stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-02-04 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 1E8P "Characterisation Of The Cellulose Docking Domain From Piromyces Equi" 88.46 46 97.83 97.83 1.12e-22 PDB 1E8Q "Characterisation Of The Cellulose Docking Domain From Piromyces Equi" 88.46 46 97.83 97.83 1.12e-22 PDB 2J4M "Double Dockerin From Piromyces Equi Cel45a" 98.08 100 98.04 100.00 2.21e-25 PDB 2J4N "Double Dockerin From Piromyces Equi Cel45a" 98.08 100 98.04 100.00 2.21e-25 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $dockerin 'Piromyces equi' 99929 Eukaryota Fungi Piromyces equi 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 _Details $dockerin 'recombinant technology' 'E. coli' Escherichia coli BL21(DE3) plasmid pGEX-4T-2 'plasmid produces a GST fusion, which was cleaved.' 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 $dockerin 1 mM [U-15N] stop_ save_ ############################ # Computer software used # ############################ save_FELIX _Saveframe_category software _Name FELIX _Version . _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model DRX _Field_strength 500 _Details . save_ save_NMR_spectrometer_2 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model DRX _Field_strength 600 _Details . save_ ############################# # NMR applied experiments # ############################# save_3D-HSQC/NOESY_1 _Saveframe_category NMR_applied_experiment _Experiment_name 3D-HSQC/NOESY _Sample_label $Sample_1 save_ save_HNHA_2 _Saveframe_category NMR_applied_experiment _Experiment_name HNHA _Sample_label $Sample_1 save_ save_HNHB_3 _Saveframe_category NMR_applied_experiment _Experiment_name HNHB _Sample_label $Sample_1 save_ save_2D-HSQC_4 _Saveframe_category NMR_applied_experiment _Experiment_name 2D-HSQC _Sample_label $Sample_1 save_ save_15N_decoupled_NOESY_5 _Saveframe_category NMR_applied_experiment _Experiment_name '15N decoupled NOESY' _Sample_label $Sample_1 save_ save_TOCSY_6 _Saveframe_category NMR_applied_experiment _Experiment_name TOCSY _Sample_label $Sample_1 save_ save_DQF-COSY_7 _Saveframe_category NMR_applied_experiment _Experiment_name DQF-COSY _Sample_label $Sample_1 save_ save_E.COSY_8 _Saveframe_category NMR_applied_experiment _Experiment_name E.COSY _Sample_label $Sample_1 save_ save_NMR_spec_expt__0_1 _Saveframe_category NMR_applied_experiment _Experiment_name 3D-HSQC/NOESY _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_2 _Saveframe_category NMR_applied_experiment _Experiment_name HNHA _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_3 _Saveframe_category NMR_applied_experiment _Experiment_name HNHB _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_4 _Saveframe_category NMR_applied_experiment _Experiment_name 2D-HSQC _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_5 _Saveframe_category NMR_applied_experiment _Experiment_name '15N decoupled NOESY' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_6 _Saveframe_category NMR_applied_experiment _Experiment_name TOCSY _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_7 _Saveframe_category NMR_applied_experiment _Experiment_name DQF-COSY _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_8 _Saveframe_category NMR_applied_experiment _Experiment_name E.COSY _BMRB_pulse_sequence_accession_number . _Details . save_ ####################### # Sample conditions # ####################### save_condition_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 6.5 0.1 n/a temperature 298 1 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 _Indirect_shift_ratio _Indirect_shift_ratio_citation_label _Correction_value_citation_label TSP H 1 'methyl protons' ppm 0.0 internal direct . . . 1.0 $entry_citation $entry_citation TSP N 15 'methyl protons' ppm 0.0 . indirect . . . 0.101329118 $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_cs_1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Sample_label $Sample_1 stop_ _Sample_conditions_label $condition_1 _Chem_shift_reference_set_label $chemical_shift_reference _Mol_system_component_name dockerin _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 GLY HA2 H 4.08 0.02 1 2 . 1 GLY HA3 H 4.08 0.02 1 3 . 2 SER H H 8.31 0.02 1 4 . 2 SER HA H 4.63 0.02 1 5 . 2 SER HB2 H 3.92 0.02 1 6 . 2 SER HB3 H 3.92 0.02 1 7 . 2 SER N N 123.3 0.1 1 8 . 3 CYS H H 8.20 0.02 1 9 . 3 CYS HA H 5.22 0.02 1 10 . 3 CYS HB2 H 2.67 0.02 1 11 . 3 CYS HB3 H 3.11 0.02 1 12 . 3 CYS N N 116.3 0.1 1 13 . 4 TRP H H 9.44 0.02 1 14 . 4 TRP HA H 4.53 0.02 1 15 . 4 TRP HB3 H 3.31 0.02 1 16 . 4 TRP HB2 H 3.57 0.02 1 17 . 4 TRP HD1 H 7.39 0.02 1 18 . 4 TRP HE1 H 9.58 0.02 1 19 . 4 TRP HE3 H 7.06 0.02 1 20 . 4 TRP HZ2 H 7.33 0.02 1 21 . 4 TRP HZ3 H 6.53 0.02 1 22 . 4 TRP HH2 H 4.95 0.02 1 23 . 4 TRP N N 130.0 0.1 1 24 . 4 TRP NE1 N 128.1 0.1 1 25 . 5 ALA H H 5.80 0.02 1 26 . 5 ALA HA H 3.84 0.02 1 27 . 5 ALA HB H 0.21 0.02 1 28 . 5 ALA N N 122.6 0.1 1 29 . 6 GLN H H 7.29 0.02 1 30 . 6 GLN HA H 4.55 0.02 1 31 . 6 GLN HB3 H 2.11 0.02 1 32 . 6 GLN HB2 H 2.22 0.02 1 33 . 6 GLN HG2 H 2.51 0.02 1 34 . 6 GLN HG3 H 2.51 0.02 1 35 . 6 GLN HE21 H 6.93 0.02 2 36 . 6 GLN HE22 H 7.51 0.02 2 37 . 6 GLN N N 121.15 0.1 1 38 . 6 GLN NE2 N 111.9 0.1 1 39 . 7 SER H H 8.23 0.02 1 40 . 7 SER HA H 4.42 0.02 1 41 . 7 SER HB2 H 4.19 0.02 1 42 . 7 SER HB3 H 4.19 0.02 1 43 . 7 SER N N 110.3 0.1 1 44 . 8 GLN H H 7.78 0.02 1 45 . 8 GLN HA H 4.76 0.02 1 46 . 8 GLN HB2 H 2.43 0.02 1 47 . 8 GLN HB3 H 2.91 0.02 1 48 . 8 GLN HG2 H 2.71 0.02 1 49 . 8 GLN HG3 H 2.71 0.02 1 50 . 8 GLN HE21 H 7.20 0.02 2 51 . 8 GLN HE22 H 7.84 0.02 2 52 . 8 GLN N N 118.2 0.1 1 53 . 8 GLN NE2 N 111.0 0.1 1 54 . 9 GLY H H 7.84 0.02 1 55 . 9 GLY HA2 H 3.74 0.02 2 56 . 9 GLY HA3 H 4.10 0.02 2 57 . 9 GLY N N 105.7 0.1 1 58 . 10 TYR H H 7.55 0.02 1 59 . 10 TYR HA H 4.83 0.02 1 60 . 10 TYR HB2 H 2.57 0.02 1 61 . 10 TYR HB3 H 3.41 0.02 1 62 . 10 TYR HD1 H 7.27 0.02 1 63 . 10 TYR HD2 H 7.27 0.02 1 64 . 10 TYR HE1 H 6.92 0.02 1 65 . 10 TYR HE2 H 6.92 0.02 1 66 . 10 TYR N N 118.6 0.1 1 67 . 11 ASN H H 8.83 0.02 1 68 . 11 ASN HA H 4.77 0.02 1 69 . 11 ASN HB2 H 2.63 0.02 1 70 . 11 ASN HB3 H 2.86 0.02 1 71 . 11 ASN HD21 H 7.03 0.02 2 72 . 11 ASN HD22 H 7.62 0.02 2 73 . 11 ASN N N 115.8 0.1 1 74 . 11 ASN ND2 N 113.6 0.1 1 75 . 12 CYS H H 8.39 0.02 1 76 . 12 CYS HA H 5.06 0.02 1 77 . 12 CYS HB2 H 1.57 0.02 2 78 . 12 CYS HB3 H 3.16 0.02 2 79 . 12 CYS N N 116.8 0.1 1 80 . 13 CYS H H 8.48 0.02 1 81 . 13 CYS HA H 4.25 0.02 1 82 . 13 CYS HB2 H 1.95 0.02 1 83 . 13 CYS HB3 H 3.20 0.02 1 84 . 13 CYS N N 121.2 0.1 1 85 . 14 ASN H H 9.48 0.02 1 86 . 14 ASN HA H 4.70 0.02 1 87 . 14 ASN HB2 H 2.74 0.02 1 88 . 14 ASN HB3 H 2.74 0.02 1 89 . 14 ASN HD21 H 7.15 0.02 2 90 . 14 ASN HD22 H 7.67 0.02 2 91 . 14 ASN N N 123.4 0.1 1 92 . 14 ASN ND2 N 114.2 0.1 1 93 . 15 ASN H H 9.09 0.02 1 94 . 15 ASN HA H 4.69 0.02 1 95 . 15 ASN HB2 H 2.80 0.02 1 96 . 15 ASN HB3 H 2.94 0.02 1 97 . 15 ASN HD21 H 6.91 0.02 2 98 . 15 ASN HD22 H 7.65 0.02 2 99 . 15 ASN N N 115.2 0.1 1 100 . 15 ASN ND2 N 113.5 0.1 1 101 . 16 PRO HA H 3.89 0.02 1 102 . 16 PRO HB2 H 1.46 0.02 2 103 . 16 PRO HB3 H 2.11 0.02 2 104 . 16 PRO HG2 H 2.46 0.02 1 105 . 16 PRO HG3 H 2.46 0.02 1 106 . 16 PRO HD2 H 3.73 0.02 2 107 . 16 PRO HD3 H 3.96 0.02 2 108 . 17 SER H H 8.52 0.02 1 109 . 17 SER HA H 4.49 0.02 1 110 . 17 SER HB2 H 4.03 0.02 2 111 . 17 SER HB3 H 4.13 0.02 2 112 . 17 SER N N 111.4 0.1 1 113 . 18 SER H H 7.74 0.02 1 114 . 18 SER HA H 4.81 0.02 1 115 . 18 SER HB2 H 3.92 0.02 2 116 . 18 SER HB3 H 4.00 0.02 2 117 . 18 SER N N 114.4 0.1 1 118 . 19 THR H H 7.34 0.02 1 119 . 19 THR HA H 4.25 0.02 1 120 . 19 THR HB H 3.90 0.02 1 121 . 19 THR HG2 H 1.30 0.02 1 122 . 19 THR N N 120.4 0.1 1 123 . 20 LYS H H 8.74 0.02 1 124 . 20 LYS HA H 4.19 0.02 1 125 . 20 LYS HB2 H 1.87 0.02 2 126 . 20 LYS HB3 H 1.90 0.02 2 127 . 20 LYS HG2 H 1.29 0.02 2 128 . 20 LYS HG3 H 1.49 0.02 2 129 . 20 LYS HD2 H 1.75 0.02 1 130 . 20 LYS HD3 H 1.75 0.02 1 131 . 20 LYS HE2 H 3.05 0.02 1 132 . 20 LYS HE3 H 3.05 0.02 1 133 . 20 LYS N N 129.3 0.1 1 134 . 21 VAL H H 8.70 0.02 1 135 . 21 VAL HA H 3.85 0.02 1 136 . 21 VAL HB H 2.10 0.02 1 137 . 21 VAL HG1 H 0.97 0.02 1 138 . 21 VAL HG2 H 1.03 0.02 1 139 . 21 VAL N N 127.0 0.1 1 140 . 22 GLU H H 9.70 0.02 1 141 . 22 GLU HA H 4.73 0.02 1 142 . 22 GLU HB2 H 2.03 0.02 1 143 . 22 GLU HB3 H 2.53 0.02 1 144 . 22 GLU HG2 H 2.49 0.02 1 145 . 22 GLU HG3 H 2.49 0.02 1 146 . 22 GLU N N 130.1 0.1 1 147 . 23 TYR H H 8.11 0.02 1 148 . 23 TYR HA H 4.87 0.02 1 149 . 23 TYR HB3 H 2.77 0.02 1 150 . 23 TYR HB2 H 3.25 0.02 1 151 . 23 TYR HD1 H 6.70 0.02 1 152 . 23 TYR HD2 H 6.70 0.02 1 153 . 23 TYR HE1 H 6.17 0.02 1 154 . 23 TYR HE2 H 6.17 0.02 1 155 . 23 TYR N N 117.6 0.1 1 156 . 24 THR H H 7.83 0.02 1 157 . 24 THR HA H 5.15 0.02 1 158 . 24 THR HB H 3.87 0.02 1 159 . 24 THR HG2 H 1.18 0.02 1 160 . 24 THR N N 119.6 0.1 1 161 . 25 ASP H H 9.21 0.02 1 162 . 25 ASP HA H 4.72 0.02 1 163 . 25 ASP HB2 H 2.79 0.02 1 164 . 25 ASP HB3 H 3.36 0.02 1 165 . 25 ASP N N 127.6 0.1 1 166 . 26 ALA H H 8.23 0.02 1 167 . 26 ALA HA H 4.08 0.02 1 168 . 26 ALA HB H 1.46 0.02 1 169 . 26 ALA N N 118.3 0.1 1 170 . 27 SER H H 8.34 0.02 1 171 . 27 SER HA H 4.16 0.02 1 172 . 27 SER HB3 H 3.79 0.02 1 173 . 27 SER HB2 H 4.23 0.02 1 174 . 27 SER N N 113.1 0.1 1 175 . 28 GLY H H 7.48 0.02 1 176 . 28 GLY HA2 H 3.39 0.02 1 177 . 28 GLY HA3 H 3.39 0.02 1 178 . 28 GLY N N 107.1 0.1 1 179 . 29 GLN H H 8.24 0.02 1 180 . 29 GLN HA H 4.92 0.02 1 181 . 29 GLN HB3 H 2.08 0.02 1 182 . 29 GLN HB2 H 2.26 0.02 1 183 . 29 GLN HG2 H 2.55 0.02 1 184 . 29 GLN HG3 H 2.55 0.02 1 185 . 29 GLN HE21 H 7.00 0.02 2 186 . 29 GLN HE22 H 7.74 0.02 2 187 . 29 GLN N N 117.1 0.1 1 188 . 29 GLN NE2 N 112.3 0.1 1 189 . 30 TRP H H 9.12 0.02 1 190 . 30 TRP HA H 5.41 0.02 1 191 . 30 TRP HB2 H 2.73 0.02 1 192 . 30 TRP HB3 H 3.40 0.02 1 193 . 30 TRP HD1 H 6.81 0.02 1 194 . 30 TRP HE1 H 10.09 0.02 1 195 . 30 TRP HE3 H 7.20 0.02 1 196 . 30 TRP HZ2 H 7.61 0.02 1 197 . 30 TRP HZ3 H 6.09 0.02 1 198 . 30 TRP HH2 H 6.74 0.02 1 199 . 30 TRP N N 121.2 0.1 1 200 . 30 TRP NE1 N 130.25 0.1 1 201 . 31 GLY H H 9.52 0.02 1 202 . 31 GLY HA2 H 3.69 0.02 2 203 . 31 GLY HA3 H 4.99 0.02 2 204 . 31 GLY N N 111.0 0.1 1 205 . 32 VAL H H 8.88 0.02 1 206 . 32 VAL HA H 4.70 0.02 1 207 . 32 VAL HB H 1.61 0.02 1 208 . 32 VAL HG2 H 0.19 0.02 1 209 . 32 VAL HG1 H 0.43 0.02 1 210 . 32 VAL N N 118.3 0.1 1 211 . 33 GLN H H 8.81 0.02 1 212 . 33 GLN HA H 4.64 0.02 1 213 . 33 GLN HB2 H 1.95 0.02 1 214 . 33 GLN HB3 H 1.95 0.02 1 215 . 33 GLN HG2 H 2.44 0.02 1 216 . 33 GLN HG3 H 2.44 0.02 1 217 . 33 GLN HE21 H 7.39 0.02 2 218 . 33 GLN HE22 H 7.64 0.02 2 219 . 33 GLN N N 124.3 0.1 1 220 . 33 GLN NE2 N 112.9 0.1 1 221 . 34 ASN H H 8.16 0.02 1 222 . 34 ASN HA H 4.38 0.02 1 223 . 34 ASN HB2 H 2.83 0.02 2 224 . 34 ASN HB3 H 3.07 0.02 2 225 . 34 ASN N N 119.6 0.1 1 226 . 35 GLY H H 8.57 0.02 1 227 . 35 GLY HA2 H 3.48 0.02 2 228 . 35 GLY HA3 H 4.04 0.02 2 229 . 35 GLY N N 102.9 0.1 1 230 . 36 GLN H H 7.68 0.02 1 231 . 36 GLN HA H 4.76 0.02 1 232 . 36 GLN HB3 H 2.01 0.02 1 233 . 36 GLN HB2 H 2.28 0.02 1 234 . 36 GLN HG2 H 2.47 0.02 2 235 . 36 GLN HG3 H 2.54 0.02 2 236 . 36 GLN HE21 H 6.98 0.02 2 237 . 36 GLN HE22 H 7.65 0.02 2 238 . 36 GLN N N 119.3 0.1 1 239 . 36 GLN NE2 N 112.6 0.1 1 240 . 37 TRP H H 8.51 0.02 1 241 . 37 TRP HA H 5.28 0.02 1 242 . 37 TRP HB2 H 2.91 0.02 1 243 . 37 TRP HB3 H 3.16 0.02 1 244 . 37 TRP HD1 H 7.18 0.02 1 245 . 37 TRP HE1 H 9.76 0.02 1 246 . 37 TRP HE3 H 7.80 0.02 1 247 . 37 TRP HZ2 H 7.18 0.02 1 248 . 37 TRP HZ3 H 6.76 0.02 1 249 . 37 TRP HH2 H 6.98 0.02 1 250 . 37 TRP N N 123.9 0.1 1 251 . 37 TRP NE1 N 128.0 0.1 1 252 . 38 CYS H H 9.67 0.02 1 253 . 38 CYS HA H 5.33 0.02 1 254 . 38 CYS HB2 H 2.62 0.02 1 255 . 38 CYS HB3 H 2.97 0.02 1 256 . 38 CYS N N 117.1 0.1 1 257 . 39 GLY H H 8.58 0.02 1 258 . 39 GLY HA2 H 1.70 0.02 2 259 . 39 GLY HA3 H 3.59 0.02 2 260 . 39 GLY N N 109.2 0.1 1 261 . 40 ILE H H 8.93 0.02 1 262 . 40 ILE HA H 3.45 0.02 1 263 . 40 ILE HB H 1.81 0.02 1 264 . 40 ILE HG12 H 0.59 0.02 2 265 . 40 ILE HG13 H 1.64 0.02 2 266 . 40 ILE HG2 H 0.51 0.02 1 267 . 40 ILE HD1 H 0.74 0.02 1 268 . 40 ILE N N 128.4 0.1 1 269 . 41 ASP H H 8.86 0.02 1 270 . 41 ASP HA H 5.29 0.02 1 271 . 41 ASP HB2 H 2.12 0.02 1 272 . 41 ASP HB3 H 3.08 0.02 1 273 . 41 ASP N N 132.0 0.1 1 274 . 42 TYR H H 9.14 0.02 1 275 . 42 TYR HA H 4.23 0.02 1 276 . 42 TYR HB2 H 2.96 0.02 1 277 . 42 TYR HB3 H 3.34 0.02 1 278 . 42 TYR HD1 H 7.26 0.02 1 279 . 42 TYR HD2 H 7.26 0.02 1 280 . 42 TYR HE1 H 6.78 0.02 1 281 . 42 TYR HE2 H 6.78 0.02 1 282 . 42 TYR N N 125.2 0.1 1 283 . 43 SER H H 9.26 0.02 1 284 . 43 SER HA H 4.66 0.02 1 285 . 43 SER HB2 H 4.06 0.02 2 286 . 43 SER HB3 H 4.15 0.02 2 287 . 43 SER N N 116.4 0.1 1 288 . 44 TYR H H 7.96 0.02 1 289 . 44 TYR HA H 4.68 0.02 1 290 . 44 TYR HB3 H 3.09 0.02 1 291 . 44 TYR HB2 H 3.34 0.02 1 292 . 44 TYR HD1 H 7.14 0.02 1 293 . 44 TYR HD2 H 7.14 0.02 1 294 . 44 TYR HE1 H 6.80 0.02 1 295 . 44 TYR HE2 H 6.80 0.02 1 296 . 44 TYR N N 125.4 0.1 1 297 . 45 GLY H H 8.04 0.02 1 298 . 45 GLY HA2 H 3.67 0.02 2 299 . 45 GLY HA3 H 3.90 0.02 2 300 . 45 GLY N N 112.9 0.1 1 301 . 46 GLN H H 8.00 0.02 1 302 . 46 GLN HA H 4.39 0.02 1 303 . 46 GLN HB2 H 2.03 0.02 2 304 . 46 GLN HB3 H 2.17 0.02 2 305 . 46 GLN HG2 H 2.33 0.02 2 306 . 46 GLN HG3 H 2.41 0.02 2 307 . 46 GLN HE21 H 6.94 0.02 2 308 . 46 GLN HE22 H 7.61 0.02 2 309 . 46 GLN N N 119.3 0.1 1 310 . 46 GLN NE2 N 112.4 0.1 1 311 . 47 ASN H H 8.64 0.02 1 312 . 47 ASN HA H 4.75 0.02 1 313 . 47 ASN HB2 H 2.80 0.02 2 314 . 47 ASN HB3 H 2.90 0.02 2 315 . 47 ASN N N 120.2 0.1 1 316 . 48 GLN H H 8.55 0.02 1 317 . 48 GLN HA H 4.40 0.02 1 318 . 48 GLN HB2 H 2.01 0.02 2 319 . 48 GLN HB3 H 2.17 0.02 2 320 . 48 GLN HG2 H 2.33 0.02 1 321 . 48 GLN HG3 H 2.33 0.02 1 322 . 48 GLN N N 121.6 0.1 1 323 . 49 GLY H H 8.55 0.02 1 324 . 49 GLY HA2 H 4.03 0.02 1 325 . 49 GLY HA3 H 4.03 0.02 1 326 . 49 GLY N N 110.1 0.1 1 327 . 50 ASN H H 8.39 0.02 1 328 . 50 ASN HA H 4.81 0.02 1 329 . 50 ASN HB2 H 2.79 0.02 2 330 . 50 ASN HB3 H 2.89 0.02 2 331 . 50 ASN N N 118.7 0.1 1 332 . 51 GLU H H 8.53 0.02 1 333 . 51 GLU HA H 4.38 0.02 1 334 . 51 GLU HB2 H 2.03 0.02 2 335 . 51 GLU HB3 H 2.19 0.02 2 336 . 51 GLU HG2 H 2.39 0.02 1 337 . 51 GLU HG3 H 2.39 0.02 1 338 . 51 GLU N N 120.8 0.1 1 339 . 52 SER H H 8.03 0.02 1 340 . 52 SER HA H 4.31 0.02 1 341 . 52 SER HB2 H 3.89 0.02 1 342 . 52 SER HB3 H 3.89 0.02 1 343 . 52 SER N N 122.3 0.1 1 stop_ save_