data_4584 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Solution Structure of the DNA-binding Domain of TraM ; _BMRB_accession_number 4584 _BMRB_flat_file_name bmr4584.str _Entry_type original _Submission_date 2000-05-05 _Accession_date 2000-09-07 _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 Stockner T. . . 2 Plugariu C. . . 3 Koraimann G. . . 4 Hoegenauer G. . . 5 Bermel W. . . 6 Prytulla S. . . 7 Sterk H. . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 327 "15N chemical shifts" 62 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2001-05-02 original author . stop_ _Original_release_date 2001-05-02 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title 'Solution Structure of the DNA-binding Domain of TraM' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code 21159140 _PubMed_ID 11258958 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Stockner T. . . 2 Plugariu C. . . 3 Koraimann G. . . 4 Hoegenauer G. . . 5 Bermel W. . . 6 Prytulla S. . . 7 Sterk H. . . stop_ _Journal_abbreviation Biochemistry _Journal_name_full Biochemistry _Journal_volume 40 _Journal_issue . _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 3370 _Page_last 3377 _Year 2001 _Details . loop_ _Keyword helix-loop-helix stop_ save_ ####################################### # Cited references within the entry # ####################################### save_ref_XPLOR_upto_v3.8 _Saveframe_category citation _Citation_full . _Citation_title 'X-PLOR, version 3.1: A system for X-ray crystallography and NMR' _Citation_status published _Citation_type book _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID ? loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Brunger Axel T. . stop_ _Journal_abbreviation . _Journal_name_full . _Journal_volume . _Journal_issue . _Journal_CSD . _Book_title 'X-PLOR, version 3.1: A system for X-ray crystallography and NMR' _Book_chapter_title . _Book_volume . _Book_series . _Book_publisher 'Yale University Press' _Book_publisher_city 'New Haven' _Book_ISBN 0300054025 _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 1992 _Details . loop_ _Keyword 'structure calculation' 'structure analysis' software stop_ save_ save_ref_NMRPipe _Saveframe_category citation _Citation_full ; Delaglio F, Grzesiek S, Vuister GW, Zhu G, Pfeifer J, Bax A. NMRPipe: a multidimensional spectral processing system based on UNIX pipes. J Biomol NMR. 1995 Nov;6(3):277-93. ; _Citation_title . _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code 96088118 _PubMed_ID ? loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Delaglio F. . . 2 Grzesiek S. . . 3 Vuister G. W. . 4 Zhu G. . . 5 Pfeifer J. . . 6 Bax A. . . stop_ _Journal_abbreviation 'J. Biomol. NMR' _Journal_name_full . _Journal_volume 6 _Journal_issue 3 _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 277 _Page_last 293 _Year 1995 _Details . save_ save_ref_MOLMOL _Saveframe_category citation _Citation_full ; Koradi R, Billeter M, Wuthrich K. MOLMOL: a program for display and analysis of macromolecular structures. J Mol Graph. 1996 Feb;14(1):51-5, 29-32. ; _Citation_title . _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code 96305672 _PubMed_ID ? loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Koradi R. . . 2 Billeter M. . . 3 Wuthrich K. . . stop_ _Journal_abbreviation 'J Mol Graph.' _Journal_name_full . _Journal_volume 14 _Journal_issue 1 _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 51 _Page_last 55 _Year 1996 _Details . save_ save_ref_ANSIG _Saveframe_category citation _Citation_full ; Kraulis PJ, Domaille PJ, Campbell-Burk SL, Van Aken T, Laue ED. Solution structure and dynamics of ras p21.GDP determined by heteronuclear three- and four-dimensional NMR spectroscopy. Biochemistry. 1994 Mar 29;33(12):3515-31. ; _Citation_title . _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code 94190870 _PubMed_ID ? loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Kraulis P. J. . 2 Domaille P. J. . 3 Campbell-Burk S. L. . 4 'Van Aken' T. . . 5 Laue E. D. . stop_ _Journal_abbreviation Biochemistry _Journal_name_full . _Journal_volume 33 _Journal_issue 12 _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 3515 _Page_last 3531 _Year 1994 _Details . save_ ################################## # Molecular system description # ################################## save_system_TRAM _Saveframe_category molecular_system _Mol_system_name 'DNA BINDING DOMAIN OF THE TRAM PROTEIN' _Abbreviation_common 'DNA BINDING DOMAIN OF THE TRAM PROTEIN' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'R1 PLASMID TRAM PROTEIN' $TRAM stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state monomer _System_paramagnetic no _System_thiol_state 'not present' _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_TRAM _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'R1 PLASMID TRAM PROTEIN' _Abbreviation_common 'DNA BINDING DOMAIN OF THE TRAM PROTEIN' _Molecular_mass . _Mol_thiol_state 'not present' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 55 _Mol_residue_sequence ; AKVQAYVSDEIVYKINKIVE RRRAEGAKSTDVSFSSISTM LLELGLRVYEAQMER ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 2 ALA 2 3 LYS 3 4 VAL 4 5 GLN 5 6 ALA 6 7 TYR 7 8 VAL 8 9 SER 9 10 ASP 10 11 GLU 11 12 ILE 12 13 VAL 13 14 TYR 14 15 LYS 15 16 ILE 16 17 ASN 17 18 LYS 18 19 ILE 19 20 VAL 20 21 GLU 21 22 ARG 22 23 ARG 23 24 ARG 24 25 ALA 25 26 GLU 26 27 GLY 27 28 ALA 28 29 LYS 29 30 SER 30 31 THR 31 32 ASP 32 33 VAL 33 34 SER 34 35 PHE 35 36 SER 36 37 SER 37 38 ILE 38 39 SER 39 40 THR 40 41 MET 41 42 LEU 42 43 LEU 43 44 GLU 44 45 LEU 45 46 GLY 46 47 LEU 47 48 ARG 48 49 VAL 49 50 TYR 50 51 GLU 51 52 ALA 52 53 GLN 53 54 MET 54 55 GLU 55 56 ARG stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-09-15 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 1DP3 "Solution Structure Of The Dna Binding Domain Of The Tram Protein" 100.00 55 100.00 100.00 3.08e-29 DBJ BAI57888 "TraM protein [Escherichia coli SE15]" 100.00 127 98.18 100.00 2.49e-28 EMBL CAQ87481 "Conjugal transfer protein [Escherichia coli UMN026]" 100.00 127 98.18 100.00 2.49e-28 EMBL CAU95771 "Protein traM [Escherichia coli 55989]" 100.00 127 98.18 98.18 3.67e-28 EMBL CBG27852 "conjugative transfer protein [Escherichia coli 042]" 100.00 127 100.00 100.00 7.61e-29 EMBL CBJ04497 "TraM protein [Escherichia coli ETEC H10407]" 100.00 127 98.18 100.00 3.56e-28 EMBL CCA64277 "conjugal transfer protein TraM [Escherichia coli]" 100.00 127 100.00 100.00 7.61e-29 GB AAA92656 "TraM, partial [Plasmid R1-19]" 100.00 126 100.00 100.00 7.66e-29 GB ABE10679 "tra operon transcriptional repressor [Escherichia coli UTI89]" 100.00 127 98.18 100.00 2.49e-28 GB ACQ42006 "TraM [Escherichia coli]" 100.00 127 100.00 100.00 7.61e-29 GB ACU68816 "IncF plasmid conjugative transfer mating signal transduction protein TraM [Escherichia coli]" 100.00 127 98.18 100.00 2.49e-28 GB ADL14025 "TraM [Escherichia coli]" 100.00 127 100.00 100.00 7.61e-29 PRF 1110195A "gene traM" 100.00 127 100.00 100.00 7.61e-29 REF WP_001151555 "conjugal transfer protein TraM [Escherichia coli]" 100.00 127 98.18 100.00 3.64e-28 REF WP_001151556 "conjugal transfer protein TraM [Escherichia coli]" 100.00 127 98.18 100.00 3.56e-28 REF WP_001151557 "conjugal transfer protein TraM [Escherichia coli]" 100.00 127 98.18 100.00 3.75e-28 REF WP_001151559 "conjugal transfer protein TraM [Escherichia coli]" 100.00 128 98.18 100.00 4.58e-28 REF WP_001151560 "conjugal transfer protein TraM [Escherichia coli]" 100.00 127 98.18 100.00 3.71e-28 SP P07294 "RecName: Full=Relaxosome protein TraM" 100.00 127 100.00 100.00 7.61e-29 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $TRAM 'E. coli' 562 Eubacteria . Escherichia coli 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 $TRAM 'recombinant technology' Bacteria Escherichia coli . pET28a(+) 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 $TRAM 4 mg/ml . 'phosphate buffer' 50 mM . H2O 95 % . D2O 5 % . stop_ save_ save_sample_2 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $TRAM 1.3 mg/ml [U-15N] 'phosphate buffer' 50 mM . H2O 95 % . D2O 5 % . stop_ save_ ############################ # Computer software used # ############################ save_XWINNMR _Saveframe_category software _Name XWINNMR _Version 2.5 loop_ _Task collection stop_ _Details 'Bruker Analytical GmbH' save_ save_NMRPipe _Saveframe_category software _Name NMRPipe _Version . loop_ _Task processing stop_ _Details . _Citation_label $ref_NMRPipe save_ save_ANSIG _Saveframe_category software _Name ANSIG _Version 3.3 loop_ _Task 'data analysis' stop_ _Details . _Citation_label $ref_ANSIG save_ save_X-PLOR _Saveframe_category software _Name X-PLOR _Version 3.851 loop_ _Task refinement stop_ _Details . _Citation_label $ref_XPLOR_upto_v3.8 save_ save_MOLMOL _Saveframe_category software _Name MOLMOL _Version 2.6 loop_ _Task 'data analysis' stop_ _Details . _Citation_label $ref_MOLMOL save_ save_VNMR _Saveframe_category software _Name VNMR _Version 5.2 loop_ _Task collection stop_ _Details 'Varian Inc.' save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer1 _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model UnityInova _Field_strength 600 _Details . save_ save_NMR_spectrometer2 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model Avance _Field_strength 600 _Details . save_ save_NMR_spectrometer3 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model Avance _Field_strength 800 _Details . save_ ############################# # NMR applied experiments # ############################# save_2D_NOESY_1 _Saveframe_category NMR_applied_experiment _Experiment_name '2D NOESY' _Sample_label . save_ save_3D-15N-NOESY-HSQC_2 _Saveframe_category NMR_applied_experiment _Experiment_name 3D-15N-NOESY-HSQC _Sample_label . save_ save_HNHA_3 _Saveframe_category NMR_applied_experiment _Experiment_name HNHA _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-NOESY-HSQC _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_3 _Saveframe_category NMR_applied_experiment _Experiment_name HNHA _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 4.0 . n/a temperature 300 . K 'ionic strength' 50 . 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 . H 1 . . . . . . . . . N 15 . . . . . . . . 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 '2D NOESY' 3D-15N-NOESY-HSQC HNHA stop_ _Sample_conditions_label $sample_cond_1 _Chem_shift_reference_set_label $chemical_shift_ref_1 _Mol_system_component_name 'R1 PLASMID TRAM PROTEIN' _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 ALA HB H 1.38 . . 2 . 1 ALA HA H 4.05 . . 3 . 2 LYS HB3 H 1.46 . . 4 . 2 LYS H H 8.56 . . 5 . 2 LYS HE2 H 2.75 . . 6 . 2 LYS HE3 H 2.75 . . 7 . 2 LYS HD2 H 1.47 . . 8 . 2 LYS HD3 H 1.47 . . 9 . 2 LYS HG2 H 0.92 . . 10 . 2 LYS HG3 H 0.92 . . 11 . 2 LYS HB2 H 1.55 . . 12 . 2 LYS HA H 4.69 . . 13 . 2 LYS N N 121.73 . . 14 . 3 VAL HB H 1.87 . . 15 . 3 VAL H H 8.86 . . 16 . 3 VAL HG1 H 0.73 . . 17 . 3 VAL HG2 H 0.73 . . 18 . 3 VAL HA H 4.34 . . 19 . 3 VAL N N 123.81 . . 20 . 4 GLN HB3 H 1.71 . . 21 . 4 GLN H H 8.04 . . 22 . 4 GLN HB2 H 1.79 . . 23 . 4 GLN HG2 H 2.05 . . 24 . 4 GLN HG3 H 2.00 . . 25 . 4 GLN HA H 5.21 . . 26 . 4 GLN HE21 H 6.81 . . 27 . 4 GLN HE22 H 7.30 . . 28 . 4 GLN N N 122.05 . . 29 . 4 GLN NE2 N 111.17 . . 30 . 5 ALA HB H 1.04 . . 31 . 5 ALA H H 8.52 . . 32 . 5 ALA HA H 4.53 . . 33 . 5 ALA N N 125.21 . . 34 . 6 TYR HB3 H 2.70 . . 35 . 6 TYR HB2 H 2.76 . . 36 . 6 TYR H H 8.33 . . 37 . 6 TYR HA H 5.17 . . 38 . 6 TYR HE1 H 6.68 . . 39 . 6 TYR HE2 H 6.68 . . 40 . 6 TYR HD1 H 6.90 . . 41 . 6 TYR HD2 H 6.90 . . 42 . 6 TYR N N 121.67 . . 43 . 7 VAL HB H 2.11 . . 44 . 7 VAL HG2 H 0.83 . . 45 . 7 VAL H H 8.68 . . 46 . 7 VAL HG1 H 0.73 . . 47 . 7 VAL HA H 4.81 . . 48 . 7 VAL N N 115.93 . . 49 . 8 SER HB3 H 3.97 . . 50 . 8 SER HB2 H 4.25 . . 51 . 8 SER H H 8.09 . . 52 . 8 SER HA H 4.47 . . 53 . 8 SER N N 116.64 . . 54 . 9 ASP HB3 H 2.49 . . 55 . 9 ASP HB2 H 2.57 . . 56 . 9 ASP H H 8.65 . . 57 . 9 ASP HA H 4.17 . . 58 . 9 ASP N N 121.62 . . 59 . 10 GLU HB3 H 1.90 . . 60 . 10 GLU H H 8.46 . . 61 . 10 GLU HG2 H 2.25 . . 62 . 10 GLU HG3 H 2.20 . . 63 . 10 GLU HA H 4.06 . . 64 . 10 GLU HB2 H 2.02 . . 65 . 10 GLU N N 119.43 . . 66 . 11 ILE HB H 2.13 . . 67 . 11 ILE HA H 3.61 . . 68 . 11 ILE HD1 H 0.79 . . 69 . 11 ILE H H 7.43 . . 70 . 11 ILE HG2 H 0.74 . . 71 . 11 ILE HG12 H 1.55 . . 72 . 11 ILE HG13 H 1.30 . . 73 . 11 ILE N N 120.37 . . 74 . 12 VAL HB H 2.14 . . 75 . 12 VAL H H 7.47 . . 76 . 12 VAL HA H 3.52 . . 77 . 12 VAL HG1 H 0.87 . . 78 . 12 VAL HG2 H 0.87 . . 79 . 12 VAL N N 119.77 . . 80 . 13 TYR HB3 H 3.12 . . 81 . 13 TYR H H 7.91 . . 82 . 13 TYR HB2 H 3.19 . . 83 . 13 TYR HA H 4.24 . . 84 . 13 TYR HE1 H 6.76 . . 85 . 13 TYR HE2 H 6.76 . . 86 . 13 TYR HD1 H 7.06 . . 87 . 13 TYR HD2 H 7.06 . . 88 . 13 TYR N N 119.14 . . 89 . 14 LYS HG2 H 1.73 . . 90 . 14 LYS HG3 H 1.73 . . 91 . 14 LYS HD2 H 1.89 . . 92 . 14 LYS HD3 H 1.89 . . 93 . 14 LYS HE2 H 2.94 . . 94 . 14 LYS HE3 H 2.94 . . 95 . 14 LYS HB3 H 1.89 . . 96 . 14 LYS HB2 H 2.00 . . 97 . 14 LYS HA H 3.79 . . 98 . 14 LYS H H 7.99 . . 99 . 14 LYS N N 118.93 . . 100 . 15 ILE HD1 H 0.10 . . 101 . 15 ILE HG13 H 0.36 . . 102 . 15 ILE HA H 3.35 . . 103 . 15 ILE HG2 H 0.10 . . 104 . 15 ILE HB H 1.66 . . 105 . 15 ILE HG12 H 0.50 . . 106 . 15 ILE H H 8.43 . . 107 . 15 ILE N N 120.64 . . 108 . 16 ASN HB3 H 2.70 . . 109 . 16 ASN HB2 H 2.92 . . 110 . 16 ASN H H 8.55 . . 111 . 16 ASN HA H 4.43 . . 112 . 16 ASN HD21 H 6.65 . . 113 . 16 ASN HD22 H 7.29 . . 114 . 16 ASN N N 118.74 . . 115 . 16 ASN ND2 N 111.44 . . 116 . 17 LYS HG2 H 1.17 . . 117 . 17 LYS HG3 H 1.17 . . 118 . 17 LYS HD2 H 1.30 . . 119 . 17 LYS HD3 H 1.30 . . 120 . 17 LYS HE3 H 2.73 . . 121 . 17 LYS HB3 H 1.73 . . 122 . 17 LYS HB2 H 1.82 . . 123 . 17 LYS HE2 H 2.86 . . 124 . 17 LYS H H 7.83 . . 125 . 17 LYS HA H 3.96 . . 126 . 17 LYS N N 119.74 . . 127 . 18 ILE HG12 H 1.88 . . 128 . 18 ILE HB H 1.90 . . 129 . 18 ILE HG13 H 0.93 . . 130 . 18 ILE H H 7.58 . . 131 . 18 ILE HG2 H 0.66 . . 132 . 18 ILE HD1 H 0.47 . . 133 . 18 ILE HA H 3.61 . . 134 . 18 ILE N N 122.47 . . 135 . 19 VAL HB H 2.33 . . 136 . 19 VAL HA H 3.11 . . 137 . 19 VAL H H 8.01 . . 138 . 19 VAL HG1 H 0.78 . . 139 . 19 VAL HG2 H 0.81 . . 140 . 19 VAL N N 119.87 . . 141 . 20 GLU HB3 H 2.03 . . 142 . 20 GLU HA H 3.82 . . 143 . 20 GLU HB2 H 2.17 . . 144 . 20 GLU HG2 H 2.35 . . 145 . 20 GLU HG3 H 2.35 . . 146 . 20 GLU H H 8.04 . . 147 . 20 GLU N N 116.79 . . 148 . 21 ARG HG3 H 1.61 . . 149 . 21 ARG HB2 H 1.93 . . 150 . 21 ARG HB3 H 1.93 . . 151 . 21 ARG HE H 7.35 . . 152 . 21 ARG HA H 4.05 . . 153 . 21 ARG HG2 H 1.69 . . 154 . 21 ARG HD2 H 3.16 . . 155 . 21 ARG HD3 H 3.16 . . 156 . 21 ARG H H 7.97 . . 157 . 21 ARG N N 121.38 . . 158 . 21 ARG NE N 85.13 . . 159 . 22 ARG HB3 H 1.90 . . 160 . 22 ARG H H 8.32 . . 161 . 22 ARG HA H 4.07 . . 162 . 22 ARG N N 117.80 . . 163 . 22 ARG NE N 83.80 . . 164 . 23 ARG HG2 H 1.52 . . 165 . 23 ARG HG3 H 1.52 . . 166 . 23 ARG H H 8.43 . . 167 . 23 ARG HE H 6.84 . . 168 . 23 ARG HB3 H 1.78 . . 169 . 23 ARG HD2 H 3.10 . . 170 . 23 ARG HB2 H 1.84 . . 171 . 23 ARG HD3 H 3.04 . . 172 . 23 ARG HA H 4.16 . . 173 . 23 ARG N N 119.69 . . 174 . 23 ARG NE N 83.95 . . 175 . 24 ALA HB H 1.50 . . 176 . 24 ALA H H 7.89 . . 177 . 24 ALA HA H 4.17 . . 178 . 24 ALA N N 122.58 . . 179 . 25 GLU HB3 H 2.07 . . 180 . 25 GLU H H 7.57 . . 181 . 25 GLU HG2 H 2.51 . . 182 . 25 GLU HG3 H 2.27 . . 183 . 25 GLU HB2 H 2.11 . . 184 . 25 GLU HA H 4.19 . . 185 . 25 GLU N N 116.66 . . 186 . 26 GLY HA3 H 3.74 . . 187 . 26 GLY HA2 H 4.20 . . 188 . 26 GLY H H 7.67 . . 189 . 26 GLY N N 106.71 . . 190 . 27 ALA HB H 1.26 . . 191 . 27 ALA HA H 4.25 . . 192 . 27 ALA H H 8.01 . . 193 . 27 ALA N N 124.01 . . 194 . 28 LYS HG3 H 1.44 . . 195 . 28 LYS HE2 H 2.95 . . 196 . 28 LYS HE3 H 2.95 . . 197 . 28 LYS H H 8.57 . . 198 . 28 LYS HD2 H 1.65 . . 199 . 28 LYS HD3 H 1.65 . . 200 . 28 LYS HG2 H 1.50 . . 201 . 28 LYS HB3 H 1.74 . . 202 . 28 LYS HB2 H 1.89 . . 203 . 28 LYS HA H 4.29 . . 204 . 28 LYS N N 120.26 . . 205 . 29 SER HB3 H 3.86 . . 206 . 29 SER HB2 H 3.90 . . 207 . 29 SER H H 8.56 . . 208 . 29 SER HA H 4.25 . . 209 . 29 SER N N 117.22 . . 210 . 30 THR HG2 H 1.16 . . 211 . 30 THR HA H 4.14 . . 212 . 30 THR HB H 4.22 . . 213 . 30 THR H H 7.43 . . 214 . 30 THR N N 110.93 . . 215 . 31 ASP HB3 H 2.63 . . 216 . 31 ASP HB2 H 2.69 . . 217 . 31 ASP H H 7.84 . . 218 . 31 ASP HA H 4.65 . . 219 . 31 ASP N N 120.87 . . 220 . 32 VAL HB H 1.86 . . 221 . 32 VAL HG1 H 0.82 . . 222 . 32 VAL HG2 H 0.82 . . 223 . 32 VAL H H 7.60 . . 224 . 32 VAL HA H 4.08 . . 225 . 32 VAL N N 119.90 . . 226 . 33 SER HA H 4.67 . . 227 . 33 SER H H 8.56 . . 228 . 33 SER N N 120.10 . . 229 . 34 PHE HB3 H 3.18 . . 230 . 34 PHE HB2 H 3.72 . . 231 . 34 PHE H H 9.42 . . 232 . 34 PHE HA H 4.67 . . 233 . 34 PHE HZ H 6.97 . . 234 . 34 PHE HD1 H 7.18 . . 235 . 34 PHE HD2 H 7.18 . . 236 . 34 PHE HE1 H 7.29 . . 237 . 34 PHE HE2 H 7.29 . . 238 . 34 PHE N N 123.27 . . 239 . 35 SER HB2 H 4.06 . . 240 . 35 SER HB3 H 4.06 . . 241 . 35 SER H H 8.77 . . 242 . 35 SER HA H 4.33 . . 243 . 35 SER N N 114.54 . . 244 . 36 SER HB3 H 3.88 . . 245 . 36 SER HA H 4.26 . . 246 . 36 SER HB2 H 4.06 . . 247 . 36 SER H H 8.38 . . 248 . 36 SER N N 122.39 . . 249 . 37 ILE HG12 H 1.73 . . 250 . 37 ILE HG13 H 0.97 . . 251 . 37 ILE HD1 H 0.55 . . 252 . 37 ILE HG2 H 0.57 . . 253 . 37 ILE H H 8.32 . . 254 . 37 ILE HA H 3.88 . . 255 . 37 ILE HB H 1.84 . . 256 . 37 ILE N N 125.82 . . 257 . 38 SER HB2 H 3.24 . . 258 . 38 SER HA H 3.71 . . 259 . 38 SER HB3 H 3.90 . . 260 . 38 SER H H 8.16 . . 261 . 38 SER N N 117.88 . . 262 . 39 THR HG2 H 1.26 . . 263 . 39 THR HB H 4.22 . . 264 . 39 THR H H 7.95 . . 265 . 39 THR HA H 3.57 . . 266 . 39 THR N N 117.82 . . 267 . 40 MET HB3 H 2.15 . . 268 . 40 MET HG2 H 2.72 . . 269 . 40 MET HA H 4.03 . . 270 . 40 MET HG3 H 2.39 . . 271 . 40 MET HB2 H 2.32 . . 272 . 40 MET H H 7.39 . . 273 . 40 MET HE H 1.63 . . 274 . 40 MET N N 121.86 . . 275 . 41 LEU HG H 1.20 . . 276 . 41 LEU HD2 H 0.49 . . 277 . 41 LEU H H 8.39 . . 278 . 41 LEU HD1 H 0.37 . . 279 . 41 LEU HB3 H 1.71 . . 280 . 41 LEU HB2 H 1.85 . . 281 . 41 LEU HA H 3.85 . . 282 . 41 LEU N N 120.15 . . 283 . 42 LEU HG H 1.50 . . 284 . 42 LEU HD1 H 0.67 . . 285 . 42 LEU HD2 H 0.67 . . 286 . 42 LEU H H 8.10 . . 287 . 42 LEU HB2 H 1.57 . . 288 . 42 LEU HB3 H 1.57 . . 289 . 42 LEU HA H 3.74 . . 290 . 42 LEU N N 121.74 . . 291 . 43 GLU HB3 H 1.99 . . 292 . 43 GLU H H 8.14 . . 293 . 43 GLU HA H 3.74 . . 294 . 43 GLU HG2 H 2.52 . . 295 . 43 GLU HG3 H 2.04 . . 296 . 43 GLU HB2 H 2.14 . . 297 . 43 GLU N N 117.44 . . 298 . 44 LEU HG H 1.58 . . 299 . 44 LEU HD1 H 0.95 . . 300 . 44 LEU HD2 H 0.99 . . 301 . 44 LEU HB2 H 1.83 . . 302 . 44 LEU HB3 H 1.67 . . 303 . 44 LEU H H 8.19 . . 304 . 44 LEU HA H 4.09 . . 305 . 44 LEU N N 121.64 . . 306 . 45 GLY HA3 H 3.37 . . 307 . 45 GLY H H 8.72 . . 308 . 45 GLY HA2 H 4.28 . . 309 . 45 GLY N N 107.07 . . 310 . 46 LEU HB2 H 1.53 . . 311 . 46 LEU HB3 H 1.53 . . 312 . 46 LEU HD1 H 0.79 . . 313 . 46 LEU HD2 H 0.84 . . 314 . 46 LEU HG H 1.57 . . 315 . 46 LEU H H 8.36 . . 316 . 46 LEU HA H 4.03 . . 317 . 46 LEU N N 121.19 . . 318 . 47 ARG HG3 H 1.66 . . 319 . 47 ARG HB2 H 2.04 . . 320 . 47 ARG HD3 H 3.14 . . 321 . 47 ARG HD2 H 3.19 . . 322 . 47 ARG H H 7.85 . . 323 . 47 ARG HE H 7.24 . . 324 . 47 ARG HA H 4.09 . . 325 . 47 ARG HB3 H 1.94 . . 326 . 47 ARG HG2 H 1.82 . . 327 . 47 ARG N N 118.83 . . 328 . 47 ARG NE N 84.40 . . 329 . 48 VAL HG2 H 1.05 . . 330 . 48 VAL HG1 H 0.91 . . 331 . 48 VAL H H 8.13 . . 332 . 48 VAL HB H 2.13 . . 333 . 48 VAL HA H 3.67 . . 334 . 48 VAL N N 120.19 . . 335 . 49 TYR HB3 H 2.89 . . 336 . 49 TYR HA H 3.83 . . 337 . 49 TYR HB2 H 2.94 . . 338 . 49 TYR H H 8.85 . . 339 . 49 TYR HE1 H 6.67 . . 340 . 49 TYR HE2 H 6.67 . . 341 . 49 TYR HD1 H 6.79 . . 342 . 49 TYR HD2 H 6.79 . . 343 . 49 TYR N N 122.87 . . 344 . 50 GLU HB3 H 1.95 . . 345 . 50 GLU HA H 3.85 . . 346 . 50 GLU HB2 H 2.13 . . 347 . 50 GLU HG3 H 2.20 . . 348 . 50 GLU HG2 H 2.62 . . 349 . 50 GLU H H 8.70 . . 350 . 50 GLU N N 116.73 . . 351 . 51 ALA HB H 1.45 . . 352 . 51 ALA H H 7.49 . . 353 . 51 ALA HA H 4.16 . . 354 . 51 ALA N N 120.27 . . 355 . 52 GLN HB2 H 1.94 . . 356 . 52 GLN HB3 H 1.94 . . 357 . 52 GLN H H 7.70 . . 358 . 52 GLN HA H 4.15 . . 359 . 52 GLN HG3 H 2.25 . . 360 . 52 GLN HG2 H 2.38 . . 361 . 52 GLN HE21 H 6.49 . . 362 . 52 GLN HE22 H 7.13 . . 363 . 52 GLN N N 115.68 . . 364 . 52 GLN NE2 N 109.92 . . 365 . 53 MET HB3 H 1.80 . . 366 . 53 MET HB2 H 1.89 . . 367 . 53 MET HG3 H 2.28 . . 368 . 53 MET HG2 H 2.35 . . 369 . 53 MET H H 7.62 . . 370 . 53 MET HA H 4.24 . . 371 . 53 MET N N 117.95 . . 372 . 54 GLU HB3 H 1.87 . . 373 . 54 GLU H H 7.82 . . 374 . 54 GLU HG3 H 2.17 . . 375 . 54 GLU HG2 H 2.25 . . 376 . 54 GLU HA H 4.17 . . 377 . 54 GLU HB2 H 2.01 . . 378 . 54 GLU N N 120.77 . . 379 . 55 ARG HB3 H 1.50 . . 380 . 55 ARG H H 7.65 . . 381 . 55 ARG HB2 H 1.63 . . 382 . 55 ARG HE H 7.07 . . 383 . 55 ARG HG2 H 1.77 . . 384 . 55 ARG HG3 H 1.77 . . 385 . 55 ARG HD2 H 3.10 . . 386 . 55 ARG HD3 H 3.10 . . 387 . 55 ARG HA H 4.09 . . 388 . 55 ARG N N 126.68 . . 389 . 55 ARG NE N 85.43 . . stop_ save_