data_4524 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Solution Structure of a Type-I Dockerin Domain, a Novel Prokaryotic, Extracellular Calcium-Binding Domain ; _BMRB_accession_number 4524 _BMRB_flat_file_name bmr4524.str _Entry_type original _Submission_date 1999-11-01 _Accession_date 1999-12-06 _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 Lytle B. L. . 2 Volkman B. F. . 3 Westler W. M. . 4 Heckman M. P. . 5 Wu J. H.D. . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 355 "15N chemical shifts" 69 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2002-03-29 original author . stop_ _Original_release_date 2002-03-29 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; Solution Structure of a Type I Dockerin Domain, a Novel Prokaryotic, Extracellular Calcium-binding Domain ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 11273698 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Lytle B. L. . 2 Volkman B. F. . 3 Westler W. M. . 4 Heckman M. P. . 5 Wu J. H.D. . stop_ _Journal_abbreviation 'J. Mol. Biol.' _Journal_volume 307 _Journal_issue . _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 745 _Page_last 753 _Year 2001 _Details . loop_ _Keyword 'cellulose degradation' cellulosome calcium-binding stop_ save_ ####################################### # Cited references within the entry # ####################################### save_ref-1 _Saveframe_category citation _Citation_full . _Citation_title . _Citation_status . _Citation_type . _CAS_abstract_code . _MEDLINE_UI_code 98035057 _PubMed_ID ? _Journal_abbreviation . _Journal_name_full . _Journal_volume . _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 . _Page_last . _Year . _Details . save_ save_ref-2 _Saveframe_category citation _Citation_full . _Citation_title . _Citation_status . _Citation_type . _CAS_abstract_code . _MEDLINE_UI_code 96088118 _PubMed_ID ? _Journal_abbreviation . _Journal_name_full . _Journal_volume . _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 . _Page_last . _Year . _Details . save_ save_ref-3 _Saveframe_category citation _Citation_full 'Bartels, C., Xia, T., Billeter, M., Guentert, P. and Wuethrich, K. J. Biomol. NMR 6, 1-10 (1995).' _Citation_title . _Citation_status . _Citation_type . _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID ? _Journal_abbreviation . _Journal_name_full . _Journal_volume . _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 . _Page_last . _Year . _Details . save_ ################################## # Molecular system description # ################################## save_CelS_DS _Saveframe_category molecular_system _Mol_system_name 'Endoglucanase SS dockerin domain' _Abbreviation_common Ct_Doc _Enzyme_commission_number 3.2.1.4 loop_ _Mol_system_component_name _Mol_label 'Dockerin domain' $Ct_Doc 'Ca 2+' $CA stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state monomer _System_paramagnetic no _System_thiol_state 'not present' loop_ _Biological_function 'Domain is responsible for docking the glycosidic subunits (in this case CelS) to the cohesin domains of CipA from Clostridium thermocellum, thus assembling them into the multiprotein complex (cellulosome)' stop_ _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_Ct_Doc _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'DOCKERIN DOMAIN' _Abbreviation_common Ct_Doc _Molecular_mass . _Mol_thiol_state 'not present' _Details 'N-terminal Met and C-terminal G introduced by cloning' ############################## # Polymer residue sequence # ############################## _Residue_count 71 _Mol_residue_sequence ; MSTKLYGDVNDDGKVNSTDA VALKRYVLRSGISINTDNAD LNEDGRVNSTDLGILKRYIL KEIDTLPYKNG ; loop_ _Residue_seq_code _Residue_label 1 MET 2 SER 3 THR 4 LYS 5 LEU 6 TYR 7 GLY 8 ASP 9 VAL 10 ASN 11 ASP 12 ASP 13 GLY 14 LYS 15 VAL 16 ASN 17 SER 18 THR 19 ASP 20 ALA 21 VAL 22 ALA 23 LEU 24 LYS 25 ARG 26 TYR 27 VAL 28 LEU 29 ARG 30 SER 31 GLY 32 ILE 33 SER 34 ILE 35 ASN 36 THR 37 ASP 38 ASN 39 ALA 40 ASP 41 LEU 42 ASN 43 GLU 44 ASP 45 GLY 46 ARG 47 VAL 48 ASN 49 SER 50 THR 51 ASP 52 LEU 53 GLY 54 ILE 55 LEU 56 LYS 57 ARG 58 TYR 59 ILE 60 LEU 61 LYS 62 GLU 63 ILE 64 ASP 65 THR 66 LEU 67 PRO 68 TYR 69 LYS 70 ASN 71 GLY stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-02-25 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 25158 entity_1 97.18 69 100.00 100.00 8.73e-39 PDB 1DAQ "Solution Structure Of The Type I Dockerin Domain From The Clostridium Thermocellum Cellulosome (Minimized Average Structure)" 98.59 71 100.00 100.00 1.62e-39 PDB 1DAV "Solution Structure Of The Type I Dockerin Domain From The Clostridium Thermocellum Cellulosome (20 Structures)" 98.59 71 100.00 100.00 1.62e-39 PDB 2MTE "Solution Structure Of Doc48s" 97.18 69 100.00 100.00 8.73e-39 EMBL CDG36590 "Endoglucanase SS [Ruminiclostridium thermocellum BC1]" 97.18 744 100.00 100.00 7.01e-37 GB AAA23226 "cellulase [Ruminiclostridium thermocellum]" 97.18 741 100.00 100.00 8.94e-37 GB AAB27404 "cellulase SS, extracellular cellulase complex subunit SS, cellulosome subunit SS, CelS [Ruminiclostridium thermocellum]" 94.37 67 100.00 100.00 2.26e-37 GB ABN53296 "glycoside hydrolase family 48 [Ruminiclostridium thermocellum ATCC 27405]" 97.18 741 100.00 100.00 8.94e-37 GB ADU75731 "glycoside hydrolase family 48 [Ruminiclostridium thermocellum DSM 1313]" 97.18 744 100.00 100.00 7.01e-37 GB AGG53971 "CelS HisX10 [Cloning vector pMC212]" 98.59 756 100.00 100.00 5.89e-38 REF WP_003514183 "endoglucanase [Ruminiclostridium thermocellum]" 97.18 744 100.00 100.00 1.06e-36 REF WP_003520216 "endoglucanase [Ruminiclostridium thermocellum]" 97.18 744 100.00 100.00 7.01e-37 REF WP_041734333 "endoglucanase [Ruminiclostridium thermocellum]" 97.18 744 100.00 100.00 9.11e-37 SP A3DH67 "RecName: Full=Cellulose 1,4-beta-cellobiosidase (reducing end) CelS; AltName: Full=Cellobiohydrolase CelS; AltName: Full=Cellul" 97.18 741 100.00 100.00 8.94e-37 SP P0C2S5 "RecName: Full=Cellulose 1,4-beta-cellobiosidase (reducing end) CelS; AltName: Full=Cellobiohydrolase CelS; AltName: Full=Cellul" 97.18 741 100.00 100.00 8.94e-37 stop_ save_ ############# # Ligands # ############# save_CA _Saveframe_category ligand _Mol_type non-polymer _Name_common "CA (CALCIUM ION)" _BMRB_code . _PDB_code CA _Molecular_mass 40.078 _Mol_charge 2 _Mol_paramagnetic . _Mol_aromatic no _Details ; Information obtained from PDB's Chemical Component Dictionary at http://wwpdb-remediation.rutgers.edu/downloads.html Downloaded on Fri Jul 15 11:29:19 2011 ; loop_ _Atom_name _PDB_atom_name _Atom_type _Atom_chirality _Atom_charge _Atom_oxidation_number _Atom_unpaired_electrons CA CA CA . 2 . ? stop_ _Mol_thiol_state . _Sequence_homology_query_date . save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $Ct_Doc 'Clostridium thermocellum' 1515 Bacteria . Clostridium thermocellum 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 $Ct_Doc 'recombinant technology' 'E. coli' Escherichia coli . PCYB2 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 $Ct_Doc 0.8 mM . 'potassium chloride' 100 mM . 'calcium chloride' 20 mM . 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 $Ct_Doc 1.0 mM [U-15N] 'potassium chloride' 100 mM . 'calcium chloride' 20 mM . D2O 10 % . H2O 90 % . stop_ save_ ############################ # Computer software used # ############################ save_DYANA _Saveframe_category software _Name DYANA _Version 1.5 loop_ _Task 'Structure solution' stop_ _Details . _Citation_label $ref-1 save_ save_XEASY _Saveframe_category software _Name XEASY _Version . loop_ _Task 'NOE assignment' stop_ _Details . _Citation_label $ref-3 save_ save_FELIX _Saveframe_category software _Name FELIX _Version 95.0 loop_ _Task Processing stop_ _Details . save_ save_NMRPIPE _Saveframe_category software _Name NMRPIPE _Version . loop_ _Task Processing stop_ _Details . _Citation_label $ref-2 save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer1 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model DMX _Field_strength 500 _Details . save_ save_NMR_spectrometer2 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model DMX _Field_strength 600 _Details . save_ save_NMR_spectrometer3 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model DMX _Field_strength 750 _Details . save_ ############################# # NMR applied experiments # ############################# save_3D_15N-separated_NOESY_1 _Saveframe_category NMR_applied_experiment _Experiment_name '3D 15N-separated NOESY' _Sample_label . save_ save_2D_NOESY_2 _Saveframe_category NMR_applied_experiment _Experiment_name '2D NOESY' _Sample_label . save_ save_3D_15N_separated_TOCSY_3 _Saveframe_category NMR_applied_experiment _Experiment_name '3D 15N separated TOCSY' _Sample_label . save_ save_NMR_spec_expt__0_1 _Saveframe_category NMR_applied_experiment _Experiment_name '3D 15N-separated NOESY' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_2 _Saveframe_category NMR_applied_experiment _Experiment_name '2D NOESY' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_3 _Saveframe_category NMR_applied_experiment _Experiment_name '2D NOESY' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_4 _Saveframe_category NMR_applied_experiment _Experiment_name '3D 15N separated 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 0.5 n/a temperature 328 1 K 'ionic strength' 100 . mM pressure 1 . atm stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_ref_1 _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 0.0 internal direct . . . 1.0 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_ _Experiment_label '3D 15N-separated NOESY' '2D NOESY' '3D 15N separated TOCSY' stop_ loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $sample_cond_1 _Chem_shift_reference_set_label $chemical_shift_ref_1 _Mol_system_component_name 'Dockerin 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 . 4 LYS N N 124.3 .2 1 2 . 4 LYS H H 8.01 0.02 1 3 . 4 LYS HA H 4.08 0.02 1 4 . 5 LEU N N 126.9 .2 1 5 . 5 LEU H H 7.59 0.02 1 6 . 5 LEU HA H 4.43 0.02 1 7 . 5 LEU HB2 H 1.75 0.02 1 8 . 5 LEU HB3 H 1.75 0.02 1 9 . 5 LEU HG H 1.20 0.02 1 10 . 5 LEU HD1 H 0.69 0.02 2 11 . 5 LEU HD2 H 0.84 0.02 2 12 . 6 TYR N N 122.4 .2 1 13 . 6 TYR H H 7.53 0.02 1 14 . 6 TYR HA H 3.61 0.02 1 15 . 6 TYR HB2 H 2.44 0.02 1 16 . 6 TYR HB3 H 2.44 0.02 1 17 . 6 TYR HD1 H 6.98 0.02 1 18 . 6 TYR HD2 H 6.98 0.02 1 19 . 6 TYR HE1 H 6.91 0.02 1 20 . 6 TYR HE2 H 6.91 0.02 1 21 . 7 GLY N N 108.4 .2 1 22 . 7 GLY H H 8.76 0.02 1 23 . 7 GLY HA2 H 4.18 0.02 2 24 . 7 GLY HA3 H 3.14 0.02 2 25 . 8 ASP N N 117.9 .2 1 26 . 8 ASP H H 7.86 0.02 1 27 . 8 ASP HA H 4.96 0.02 1 28 . 8 ASP HB2 H 2.96 0.02 2 29 . 8 ASP HB3 H 1.99 0.02 2 30 . 9 VAL N N 120.4 .2 1 31 . 9 VAL H H 8.14 0.02 1 32 . 9 VAL HA H 3.94 0.02 1 33 . 9 VAL HB H 2.22 0.02 1 34 . 9 VAL HG1 H 1.02 0.02 2 35 . 9 VAL HG2 H 0.76 0.02 2 36 . 10 ASN N N 115.5 .2 1 37 . 10 ASN H H 8.00 0.02 1 38 . 10 ASN HA H 4.93 0.02 1 39 . 10 ASN HB2 H 3.33 0.02 2 40 . 10 ASN HB3 H 2.21 0.02 2 41 . 10 ASN ND2 N 111.5 .2 1 42 . 10 ASN HD21 H 7.87 0.02 2 43 . 10 ASN HD22 H 6.56 0.02 2 44 . 11 ASP N N 116.1 .2 1 45 . 11 ASP H H 7.33 0.02 1 46 . 11 ASP HA H 4.41 0.02 1 47 . 11 ASP HB2 H 3.06 0.02 2 48 . 11 ASP HB3 H 2.36 0.02 2 49 . 12 ASP N N 118.2 .2 1 50 . 12 ASP H H 8.69 0.02 1 51 . 12 ASP HA H 4.76 0.02 1 52 . 12 ASP HB2 H 3.08 0.02 2 53 . 12 ASP HB3 H 2.32 0.02 2 54 . 13 GLY N N 112.3 .2 1 55 . 13 GLY H H 10.19 0.02 1 56 . 13 GLY HA2 H 3.36 0.02 2 57 . 13 GLY HA3 H 4.06 0.02 2 58 . 14 LYS N N 117.7 .2 1 59 . 14 LYS H H 7.78 0.02 1 60 . 14 LYS HA H 4.63 0.02 1 61 . 14 LYS HB2 H 1.62 0.02 1 62 . 14 LYS HB3 H 1.62 0.02 1 63 . 14 LYS HG2 H 1.24 0.02 1 64 . 14 LYS HG3 H 1.24 0.02 1 65 . 14 LYS HD2 H 1.51 0.02 1 66 . 14 LYS HD3 H 1.51 0.02 1 67 . 14 LYS HE2 H 2.91 0.02 1 68 . 14 LYS HE3 H 2.91 0.02 1 69 . 15 VAL N N 126.3 .2 1 70 . 15 VAL H H 8.87 0.02 1 71 . 15 VAL HA H 4.73 0.02 1 72 . 15 VAL HB H 2.11 0.02 1 73 . 15 VAL HG1 H 0.88 0.02 2 74 . 15 VAL HG2 H 0.72 0.02 2 75 . 16 ASN N N 126.3 .2 1 76 . 16 ASN H H 9.95 0.02 1 77 . 16 ASN HA H 4.78 0.02 1 78 . 16 ASN HB2 H 3.46 0.02 2 79 . 16 ASN HB3 H 3.12 0.02 2 80 . 16 ASN ND2 N 113.3 .2 1 81 . 16 ASN HD21 H 7.71 0.02 2 82 . 16 ASN HD22 H 7.29 0.02 2 83 . 17 SER N N 115.7 .2 1 84 . 17 SER H H 7.52 0.02 1 85 . 17 SER HB2 H 3.71 0.02 1 86 . 17 SER HB3 H 3.71 0.02 1 87 . 18 THR N N 113.1 .2 1 88 . 18 THR H H 7.92 0.02 1 89 . 18 THR HA H 4.26 0.02 1 90 . 18 THR HB H 3.96 0.02 1 91 . 18 THR HG2 H 1.18 0.02 1 92 . 19 ASP N N 120.1 .2 1 93 . 19 ASP H H 7.88 0.02 1 94 . 19 ASP HA H 4.34 0.02 1 95 . 19 ASP HB2 H 3.27 0.02 2 96 . 19 ASP HB3 H 3.06 0.02 2 97 . 20 ALA N N 119.8 .2 1 98 . 20 ALA H H 7.02 0.02 1 99 . 20 ALA HA H 4.02 0.02 1 100 . 20 ALA HB H 1.44 0.02 1 101 . 21 VAL N N 119.7 .2 1 102 . 21 VAL H H 7.71 0.02 1 103 . 21 VAL HA H 3.59 0.02 1 104 . 21 VAL HB H 2.16 0.02 1 105 . 21 VAL HG1 H 0.96 0.02 2 106 . 21 VAL HG2 H 1.09 0.02 2 107 . 22 ALA N N 121.7 .2 1 108 . 22 ALA H H 7.82 0.02 1 109 . 22 ALA HA H 4.00 0.02 1 110 . 22 ALA HB H 1.37 0.02 1 111 . 23 LEU N N 117.4 .2 1 112 . 23 LEU H H 8.43 0.02 1 113 . 23 LEU HA H 4.12 0.02 1 114 . 23 LEU HB2 H 1.98 0.02 1 115 . 23 LEU HB3 H 1.98 0.02 1 116 . 23 LEU HG H 1.57 0.02 1 117 . 23 LEU HD1 H 0.91 0.02 2 118 . 23 LEU HD2 H 0.86 0.02 2 119 . 24 LYS N N 120.2 .2 1 120 . 24 LYS H H 8.17 0.02 1 121 . 24 LYS HA H 3.88 0.02 1 122 . 24 LYS HB2 H 2.13 0.02 2 123 . 24 LYS HB3 H 1.92 0.02 2 124 . 24 LYS HG2 H 1.35 0.02 1 125 . 24 LYS HG3 H 1.35 0.02 1 126 . 24 LYS HD2 H 1.70 0.02 1 127 . 24 LYS HD3 H 1.70 0.02 1 128 . 24 LYS HE2 H 2.95 0.02 1 129 . 24 LYS HE3 H 2.95 0.02 1 130 . 25 ARG N N 116.5 .2 1 131 . 25 ARG H H 7.95 0.02 1 132 . 25 ARG HA H 3.90 0.02 1 133 . 25 ARG HB2 H 1.96 0.02 2 134 . 25 ARG HB3 H 1.61 0.02 2 135 . 25 ARG HG2 H 1.70 0.02 2 136 . 25 ARG HG3 H 1.85 0.02 2 137 . 25 ARG HD2 H 3.11 0.02 1 138 . 25 ARG HD3 H 3.11 0.02 1 139 . 26 TYR N N 120.9 .2 1 140 . 26 TYR H H 8.23 0.02 1 141 . 26 TYR HA H 4.15 0.02 1 142 . 26 TYR HB2 H 3.25 0.02 2 143 . 26 TYR HB3 H 2.91 0.02 2 144 . 26 TYR HD1 H 6.95 0.02 1 145 . 26 TYR HD2 H 6.95 0.02 1 146 . 26 TYR HE1 H 6.83 0.02 1 147 . 26 TYR HE2 H 6.83 0.02 1 148 . 27 VAL N N 119.6 .2 1 149 . 27 VAL H H 8.65 0.02 1 150 . 27 VAL HA H 3.75 0.02 1 151 . 27 VAL HB H 2.31 0.02 1 152 . 27 VAL HG1 H 0.99 0.02 2 153 . 27 VAL HG2 H 1.04 0.02 2 154 . 28 LEU N N 119.0 .2 1 155 . 28 LEU H H 7.78 0.02 1 156 . 28 LEU HA H 4.27 0.02 1 157 . 28 LEU HB2 H 1.75 0.02 1 158 . 28 LEU HB3 H 1.75 0.02 1 159 . 28 LEU HG H 1.62 0.02 1 160 . 28 LEU HD1 H 1.18 0.02 2 161 . 28 LEU HD2 H 0.83 0.02 2 162 . 29 ARG N N 115.5 .2 1 163 . 29 ARG H H 7.88 0.02 1 164 . 29 ARG HA H 4.07 0.02 1 165 . 29 ARG HB2 H 2.00 0.02 2 166 . 29 ARG HB3 H 1.90 0.02 2 167 . 29 ARG HG2 H 1.51 0.02 1 168 . 29 ARG HG3 H 1.51 0.02 1 169 . 29 ARG HD2 H 3.15 0.02 1 170 . 29 ARG HD3 H 3.15 0.02 1 171 . 31 GLY N N 109.3 .2 1 172 . 31 GLY H H 8.34 0.02 1 173 . 31 GLY HA2 H 4.09 0.02 2 174 . 31 GLY HA3 H 3.77 0.02 2 175 . 32 ILE N N 118.2 .2 1 176 . 32 ILE H H 7.24 0.02 1 177 . 32 ILE HA H 4.37 0.02 1 178 . 32 ILE HB H 1.87 0.02 1 179 . 32 ILE HG2 H 1.11 0.02 1 180 . 32 ILE HG12 H 1.45 0.02 1 181 . 32 ILE HG13 H 1.45 0.02 1 182 . 32 ILE HD1 H 0.90 0.02 1 183 . 33 SER N N 119.8 .2 1 184 . 33 SER H H 8.10 0.02 1 185 . 33 SER HA H 4.79 0.02 1 186 . 33 SER HB2 H 3.77 0.02 2 187 . 33 SER HB3 H 3.83 0.02 2 188 . 34 ILE N N 116.1 .2 1 189 . 34 ILE H H 7.60 0.02 1 190 . 34 ILE HA H 4.59 0.02 1 191 . 34 ILE HB H 1.64 0.02 1 192 . 34 ILE HG2 H 0.55 0.02 1 193 . 34 ILE HG12 H 0.16 0.02 1 194 . 34 ILE HG13 H 0.16 0.02 1 195 . 34 ILE HD1 H -0.01 0.02 1 196 . 35 ASN N N 118.5 .2 1 197 . 35 ASN H H 8.70 0.02 1 198 . 35 ASN HA H 4.70 0.02 1 199 . 35 ASN HB2 H 2.86 0.02 2 200 . 35 ASN HB3 H 2.69 0.02 2 201 . 35 ASN ND2 N 114.9 .2 1 202 . 35 ASN HD21 H 8.70 0.02 2 203 . 35 ASN HD22 H 6.59 0.02 2 204 . 36 THR N N 116.1 .2 1 205 . 36 THR H H 7.77 0.02 1 206 . 36 THR HA H 4.17 0.02 1 207 . 36 THR HB H 3.52 0.02 1 208 . 36 THR HG2 H 1.00 0.02 1 209 . 37 ASP N N 122.9 .2 1 210 . 37 ASP H H 7.84 0.02 1 211 . 37 ASP HA H 4.42 0.02 1 212 . 37 ASP HB2 H 2.73 0.02 2 213 . 37 ASP HB3 H 2.41 0.02 2 214 . 38 ASN N N 115.5 .2 1 215 . 38 ASN H H 7.14 0.02 1 216 . 38 ASN HA H 4.24 0.02 1 217 . 38 ASN HB2 H 2.69 0.02 2 218 . 38 ASN HB3 H 2.15 0.02 2 219 . 38 ASN ND2 N 109.8 .2 1 220 . 38 ASN HD21 H 7.60 0.02 2 221 . 38 ASN HD22 H 6.49 0.02 2 222 . 39 ALA N N 119.5 .2 1 223 . 39 ALA H H 7.09 0.02 1 224 . 39 ALA HA H 4.03 0.02 1 225 . 39 ALA HB H 1.25 0.02 1 226 . 40 ASP N N 114.8 .2 1 227 . 40 ASP H H 6.93 0.02 1 228 . 40 ASP HA H 4.91 0.02 1 229 . 40 ASP HB2 H 3.01 0.02 2 230 . 40 ASP HB3 H 2.30 0.02 2 231 . 41 LEU N N 123.4 .2 1 232 . 41 LEU H H 8.49 0.02 1 233 . 41 LEU HA H 4.04 0.02 1 234 . 41 LEU HB2 H 1.65 0.02 1 235 . 41 LEU HB3 H 1.65 0.02 1 236 . 41 LEU HG H 1.25 0.02 1 237 . 41 LEU HD1 H 0.97 0.02 2 238 . 41 LEU HD2 H 0.79 0.02 2 239 . 42 ASN N N 112.7 .2 1 240 . 42 ASN H H 7.97 0.02 1 241 . 42 ASN HA H 4.88 0.02 1 242 . 42 ASN HB2 H 3.34 0.02 2 243 . 42 ASN HB3 H 2.60 0.02 2 244 . 42 ASN ND2 N 113.1 .2 1 245 . 42 ASN HD21 H 8.18 0.02 2 246 . 42 ASN HD22 H 6.56 0.02 2 247 . 43 GLU N N 115.6 .2 1 248 . 43 GLU H H 7.52 0.02 1 249 . 43 GLU HA H 3.92 0.02 1 250 . 43 GLU HB2 H 2.04 0.02 2 251 . 43 GLU HB3 H 1.74 0.02 2 252 . 43 GLU HG2 H 2.21 0.02 1 253 . 43 GLU HG3 H 2.21 0.02 1 254 . 44 ASP N N 117.4 .2 1 255 . 44 ASP H H 8.39 0.02 1 256 . 44 ASP HA H 4.76 0.02 1 257 . 44 ASP HB2 H 3.10 0.02 2 258 . 44 ASP HB3 H 2.33 0.02 2 259 . 45 GLY N N 112.3 .2 1 260 . 45 GLY H H 10.04 0.02 1 261 . 45 GLY HA2 H 3.56 0.02 2 262 . 45 GLY HA3 H 4.16 0.02 2 263 . 46 ARG N N 117.9 .2 1 264 . 46 ARG H H 7.92 0.02 1 265 . 46 ARG HA H 4.76 0.02 1 266 . 46 ARG HB2 H 1.54 0.02 2 267 . 46 ARG HB3 H 1.70 0.02 2 268 . 46 ARG HG2 H 1.43 0.02 1 269 . 46 ARG HG3 H 1.43 0.02 1 270 . 46 ARG HD2 H 3.08 0.02 1 271 . 46 ARG HD3 H 3.08 0.02 1 272 . 47 VAL N N 126.3 .2 1 273 . 47 VAL H H 8.85 0.02 1 274 . 47 VAL HA H 4.78 0.02 1 275 . 47 VAL HB H 2.13 0.02 1 276 . 47 VAL HG1 H 0.76 0.02 1 277 . 47 VAL HG2 H 0.76 0.02 1 278 . 48 ASN N N 126.6 .2 1 279 . 48 ASN H H 9.94 0.02 1 280 . 48 ASN HA H 4.84 0.02 1 281 . 48 ASN HB2 H 3.60 0.02 2 282 . 48 ASN HB3 H 3.10 0.02 2 283 . 48 ASN ND2 N 112.9 .2 1 284 . 48 ASN HD21 H 7.76 0.02 2 285 . 48 ASN HD22 H 7.34 0.02 2 286 . 49 SER N N 112.8 .2 1 287 . 49 SER H H 7.99 0.02 1 288 . 49 SER HA H 4.29 0.02 1 289 . 49 SER HB2 H 3.82 0.02 2 290 . 49 SER HB3 H 3.85 0.02 2 291 . 50 THR N N 121.5 .2 1 292 . 50 THR H H 8.03 0.02 1 293 . 50 THR HA H 4.27 0.02 1 294 . 50 THR HB H 4.08 0.02 1 295 . 50 THR HG2 H 1.20 0.02 1 296 . 51 ASP N N 120.1 .2 1 297 . 51 ASP H H 7.48 0.02 1 298 . 51 ASP HA H 4.31 0.02 1 299 . 51 ASP HB2 H 3.09 0.02 2 300 . 51 ASP HB3 H 3.21 0.02 2 301 . 52 LEU N N 118.0 .2 1 302 . 52 LEU H H 7.06 0.02 1 303 . 52 LEU HA H 4.14 0.02 1 304 . 52 LEU HB2 H 2.22 0.02 2 305 . 52 LEU HB3 H 1.64 0.02 2 306 . 52 LEU HG H 1.21 0.02 1 307 . 52 LEU HD1 H 1.04 0.02 2 308 . 52 LEU HD2 H 0.93 0.02 2 309 . 53 GLY N N 105.7 .2 1 310 . 53 GLY H H 7.97 0.02 1 311 . 53 GLY HA2 H 4.02 0.02 2 312 . 53 GLY HA3 H 3.80 0.02 2 313 . 54 ILE N N 121.7 .2 1 314 . 54 ILE H H 7.63 0.02 1 315 . 54 ILE HA H 3.42 0.02 1 316 . 54 ILE HB H 1.84 0.02 1 317 . 54 ILE HG2 H 0.74 0.02 1 318 . 54 ILE HG12 H 1.24 0.02 1 319 . 54 ILE HG13 H 1.24 0.02 1 320 . 54 ILE HD1 H 0.70 0.02 1 321 . 55 LEU N N 120.8 .2 1 322 . 55 LEU H H 8.22 0.02 1 323 . 55 LEU HA H 3.90 0.02 1 324 . 55 LEU HB2 H 2.07 0.02 1 325 . 55 LEU HB3 H 2.07 0.02 1 326 . 55 LEU HG H 1.59 0.02 1 327 . 55 LEU HD1 H 0.88 0.02 2 328 . 55 LEU HD2 H 1.00 0.02 2 329 . 56 LYS N N 116.8 .2 1 330 . 56 LYS H H 8.28 0.02 1 331 . 56 LYS HA H 3.82 0.02 1 332 . 56 LYS HB2 H 1.89 0.02 1 333 . 56 LYS HB3 H 1.89 0.02 1 334 . 56 LYS HG2 H 1.34 0.02 1 335 . 56 LYS HG3 H 1.34 0.02 1 336 . 56 LYS HD2 H 1.69 0.02 1 337 . 56 LYS HD3 H 1.69 0.02 1 338 . 56 LYS HE2 H 2.91 0.02 1 339 . 56 LYS HE3 H 2.91 0.02 1 340 . 57 ARG N N 116.5 .2 1 341 . 57 ARG H H 7.47 0.02 1 342 . 57 ARG HA H 3.90 0.02 1 343 . 57 ARG HB2 H 2.02 0.02 2 344 . 57 ARG HB3 H 1.86 0.02 2 345 . 57 ARG HG2 H 1.72 0.02 2 346 . 57 ARG HG3 H 1.59 0.02 2 347 . 57 ARG HD2 H 3.07 0.02 1 348 . 57 ARG HD3 H 3.07 0.02 1 349 . 58 TYR N N 122.0 .2 1 350 . 58 TYR H H 8.48 0.02 1 351 . 58 TYR HA H 4.41 0.02 1 352 . 58 TYR HB2 H 3.25 0.02 2 353 . 58 TYR HB3 H 2.83 0.02 2 354 . 58 TYR HD1 H 6.73 0.02 1 355 . 58 TYR HD2 H 6.73 0.02 1 356 . 58 TYR HE1 H 6.61 0.02 1 357 . 58 TYR HE2 H 6.61 0.02 1 358 . 59 ILE N N 122.1 .2 1 359 . 59 ILE H H 8.64 0.02 1 360 . 59 ILE HA H 3.66 0.02 1 361 . 59 ILE HB H 1.96 0.02 1 362 . 59 ILE HG2 H 0.90 0.02 1 363 . 59 ILE HG12 H 1.69 0.02 2 364 . 59 ILE HG13 H 1.22 0.02 2 365 . 59 ILE HD1 H 0.75 0.02 1 366 . 60 LEU N N 118.4 .2 1 367 . 60 LEU H H 7.50 0.02 1 368 . 60 LEU HA H 4.19 0.02 1 369 . 60 LEU HB2 H 1.72 0.02 1 370 . 60 LEU HB3 H 1.72 0.02 1 371 . 60 LEU HD1 H 0.83 0.02 1 372 . 60 LEU HD2 H 0.83 0.02 1 373 . 61 LYS N N 113.2 .2 1 374 . 61 LYS H H 7.70 0.02 1 375 . 61 LYS HA H 3.92 0.02 1 376 . 61 LYS HB2 H 2.07 0.02 2 377 . 61 LYS HB3 H 1.93 0.02 2 378 . 61 LYS HG2 H 1.25 0.02 1 379 . 61 LYS HG3 H 1.25 0.02 1 380 . 61 LYS HD2 H 1.62 0.02 1 381 . 61 LYS HD3 H 1.62 0.02 1 382 . 61 LYS HE2 H 2.93 0.02 1 383 . 61 LYS HE3 H 2.93 0.02 1 384 . 62 GLU N N 117.5 .2 1 385 . 62 GLU H H 8.36 0.02 1 386 . 62 GLU HA H 4.13 0.02 1 387 . 62 GLU HB2 H 2.08 0.02 2 388 . 62 GLU HB3 H 1.80 0.02 2 389 . 62 GLU HG2 H 2.21 0.02 2 390 . 62 GLU HG3 H 2.17 0.02 2 391 . 63 ILE N N 112.1 .2 1 392 . 63 ILE H H 6.82 0.02 1 393 . 63 ILE HA H 4.37 0.02 1 394 . 63 ILE HB H 1.53 0.02 1 395 . 63 ILE HG2 H 0.58 0.02 1 396 . 63 ILE HG12 H 0.66 0.02 1 397 . 63 ILE HG13 H 0.66 0.02 1 398 . 63 ILE HD1 H 0.49 0.02 1 399 . 64 ASP N N 119.6 .2 1 400 . 64 ASP H H 8.36 0.02 1 401 . 64 ASP HA H 4.66 0.02 1 402 . 64 ASP HB2 H 2.79 0.02 2 403 . 64 ASP HB3 H 2.60 0.02 2 404 . 65 THR N N 113.0 .2 1 405 . 65 THR H H 7.32 0.02 1 406 . 65 THR HA H 4.65 0.02 1 407 . 65 THR HB H 4.02 0.02 1 408 . 65 THR HG2 H 1.16 0.02 1 409 . 66 LEU N N 120.6 .2 1 410 . 66 LEU H H 7.65 0.02 1 411 . 66 LEU HA H 4.18 0.02 1 412 . 66 LEU HB2 H 1.25 0.02 2 413 . 66 LEU HB3 H 0.78 0.02 2 414 . 66 LEU HG H 0.49 0.02 1 415 . 66 LEU HD1 H -0.02 0.02 2 416 . 66 LEU HD2 H 0.61 0.02 2 417 . 68 TYR N N 122.3 .2 1 418 . 68 TYR H H 8.46 0.02 1 419 . 68 TYR HB2 H 2.75 0.02 2 420 . 68 TYR HB3 H 2.87 0.02 2 421 . 68 TYR HD1 H 7.10 0.02 1 422 . 68 TYR HD2 H 7.10 0.02 1 423 . 68 TYR HE1 H 6.83 0.02 1 424 . 68 TYR HE2 H 6.83 0.02 1 stop_ save_