data_4429 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; 1H and 15N Chemical Shift Assignments for ribosomal protein L7 ; _BMRB_accession_number 4429 _BMRB_flat_file_name bmr4429.str _Entry_type original _Submission_date 1999-10-03 _Accession_date 1999-10-04 _Entry_origination author _NMR_STAR_version 2.1.1 _Experimental_method NMR _Details ; The chemical shifts of L7 major form are presented. There are two forms of protein L7 in solution due to cis/trans (1/2) isomerization of the Gly43-Pro44 peptide bond in the flexible interdomain (hinge) region. In the HSQC spectrum the cross-peaks of residues Ala34-Val45 from hinge region are doublet. L7 is the N-terminal acetylated form of L12. ; loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Bocharov Eduard V. . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 coupling_constants 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 635 "15N chemical shifts" 120 "coupling constants" 118 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2002-07-12 update BMRB 'Modify the saveframe name.' 1999-12-23 original author 'Original release.' stop_ save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full 'Bocharov, E. V., Gudkov, A. T., and Arseniev, A. S., "Topology of the secondary structure elements of ribosomal protein L7/L12 from E.coli in solution," FEBS Lett. 379, 291-294 (1996).' _Citation_title ; Topology of the secondary structure elements of ribosomal protein L7/L12 from E.coli in solutio ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code 96184584 _PubMed_ID ? loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Bocharov Eduard V. . 2 Gudkov Anatolij T. . 3 Arseniev Alexandr S. . stop_ _Journal_abbreviation 'FEBS Lett.' _Journal_volume 379 _Journal_issue . _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 291 _Page_last 294 _Year 1996 _Details . loop_ _Keyword ribosome 'L7/L12 protein' 'sequence-specific NMR assignment' 'secondary structure' stop_ save_ ####################################### # Cited references within the entry # ####################################### save_ref_1 _Saveframe_category citation _Citation_full ; Bartels C., Xia T.-H., Billeter M., Guntert P. & Wuthrich K. The program XEASY for computer-supported NMR spectral analysis of biological macromolecules, J. Biomol. NMR (1995) 6, 1-10. ; _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_ save_ref_2 _Saveframe_category citation _Citation_full ; Guntert P., Mumenthaler C. & Wuthrich K. Torsion angle dynamics for NMR structure calculation with new program DYANA, J. Mol. Biol. (1997) 273, 283-298. ; _Citation_title 'Torsion angle dynamics for NMR structure calculation with the new program DYANA.' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 9367762 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Guntert P. . . 2 Mumenthaler C. . . 3 Wuthrich K. . . stop_ _Journal_abbreviation 'J. Mol. Biol.' _Journal_name_full 'Journal of molecular biology' _Journal_volume 273 _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 283 _Page_last 298 _Year 1997 _Details ; The new program DYANA (DYnamics Algorithm for Nmr Applications) for efficient calculation of three-dimensional protein and nucleic acid structures from distance constraints and torsion angle constraints collected by nuclear magnetic resonance (NMR) experiments performs simulated annealing by molecular dynamics in torsion angle space and uses a fast recursive algorithm to integrate the equations of motions. Torsion angle dynamics can be more efficient than molecular dynamics in Cartesian coordinate space because of the reduced number of degrees of freedom and the concomitant absence of high-frequency bond and angle vibrations, which allows for the use of longer time-steps and/or higher temperatures in the structure calculation. It also represents a significant advance over the variable target function method in torsion angle space with the REDAC strategy used by the predecessor program DIANA. DYANA computation times per accepted conformer in the "bundle" used to represent the NMR structure compare favorably with those of other presently available structure calculation algorithms, and are of the order of 160 seconds for a protein of 165 amino acid residues when using a DEC Alpha 8400 5/300 computer. Test calculations starting from conformers with random torsion angle values further showed that DYANA is capable of efficient calculation of high-quality protein structures with up to 400 amino acid residues, and of nucleic acid structures. ; save_ save_ref_3 _Saveframe_category citation _Citation_full ; Schaumann T., Braun W. & Wuthrich K. (1990) The program FANTOM for energy refinement of polypeptides and proteins using a Newton-Raphson minimizer in torsion angle space, Biopolymers 29, 679-694. ; _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_ save_ref_4 _Saveframe_category citation _Citation_full ; Koradi R., Billiter M. & Wutrich, K (1996) MOLMOL: a program for display and analysis of macromolecular structures, J. Mol. Graphics 14, 51-55. ; _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_system_L7 _Saveframe_category molecular_system _Mol_system_name 'ribosomal protein L7 from E. coli' _Abbreviation_common L7 _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'L7 dimer subunit A' $L7_L12 'L7 dimer subunit B' $L7_L12 stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state homodimer _System_paramagnetic no _System_thiol_state 'not present' loop_ _Magnetic_equivalence_ID _Magnetically_equivalent_system_component 1 'L7 dimer subunit A' 1 'L7 dimer subunit B' stop_ loop_ _Biological_function ; Protein L7/L12 is very important for the protein synthesis in ribosome. Two L7/L12 dimers are associated with 23S rRNA via protein L10 near from the A-site of ribosome. The following model of the L7/L12 dimer was derived: two N-terminal parts (Ser1-Ser33)*2 form a symmetrical four-helical bundle, and two independent identical globular C-terminal domains (Thr52-Lys120) are connected to the bundle via highly mobile hinge regions. The N-domain of the L7/L12 dimer is responsible for its incorporation into the ribosome. The C-domains of the L7/L12 dimer are crucial for inducing GTPase activity in EF-Tu and EF-G elongation factors. ; stop_ _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_L7_L12 _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'E.coli ribosomal protein L7/L12' _Abbreviation_common L7/L12 _Molecular_mass 12164 _Mol_thiol_state 'not present' _Details 'Two forms of L7/L12 presence in solution due to cis/trans (1/6) isomerization of the Val7-Pro8 peptide bond.' ############################## # Polymer residue sequence # ############################## _Residue_count 120 _Mol_residue_sequence ; SITKDQIIEAVAAMSVMDVV ELISAMEEKFGVSAAAAVAV AAGPVEAAEEKTEFDVILKA AGANKVAVIKAVRGATGLGL KEAKDLVESAPAALKEGVSK DDAEALKKALEEAGAEVEVK ; loop_ _Residue_seq_code _Residue_label 1 SER 2 ILE 3 THR 4 LYS 5 ASP 6 GLN 7 ILE 8 ILE 9 GLU 10 ALA 11 VAL 12 ALA 13 ALA 14 MET 15 SER 16 VAL 17 MET 18 ASP 19 VAL 20 VAL 21 GLU 22 LEU 23 ILE 24 SER 25 ALA 26 MET 27 GLU 28 GLU 29 LYS 30 PHE 31 GLY 32 VAL 33 SER 34 ALA 35 ALA 36 ALA 37 ALA 38 VAL 39 ALA 40 VAL 41 ALA 42 ALA 43 GLY 44 PRO 45 VAL 46 GLU 47 ALA 48 ALA 49 GLU 50 GLU 51 LYS 52 THR 53 GLU 54 PHE 55 ASP 56 VAL 57 ILE 58 LEU 59 LYS 60 ALA 61 ALA 62 GLY 63 ALA 64 ASN 65 LYS 66 VAL 67 ALA 68 VAL 69 ILE 70 LYS 71 ALA 72 VAL 73 ARG 74 GLY 75 ALA 76 THR 77 GLY 78 LEU 79 GLY 80 LEU 81 LYS 82 GLU 83 ALA 84 LYS 85 ASP 86 LEU 87 VAL 88 GLU 89 SER 90 ALA 91 PRO 92 ALA 93 ALA 94 LEU 95 LYS 96 GLU 97 GLY 98 VAL 99 SER 100 LYS 101 ASP 102 ASP 103 ALA 104 GLU 105 ALA 106 LEU 107 LYS 108 LYS 109 ALA 110 LEU 111 GLU 112 GLU 113 ALA 114 GLY 115 ALA 116 GLU 117 VAL 118 GLU 119 VAL 120 LYS stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-08-11 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 1CTF "Structure Of The C-Terminal Domain Of The Ribosomal Protein L7L12 FROM ESCHERICHIA COLI AT 1.7 ANGSTROMS" 61.67 74 100.00 100.00 1.48e-37 PDB 1RQS "Nmr Structure Of C-Terminal Domain Of Ribosomal Protein L7 From E.Coli" 61.67 74 100.00 100.00 1.48e-37 PDB 1RQU "Nmr Structure Of L7 Dimer From E.Coli" 100.00 120 100.00 100.00 7.35e-57 PDB 1RQV "Spatial Model Of L7 Dimer From E.Coli With One Hinge Region In Helical State" 100.00 120 100.00 100.00 7.35e-57 PDB 2BCW "Coordinates Of The N-Terminal Domain Of Ribosomal Protein L11,C-Terminal Domain Of Ribosomal Protein L7L12 AND A Portion Of The" 56.67 68 100.00 100.00 8.64e-34 PDB 2GYA "Structure Of The 50s Subunit Of A Pre-Translocational E. Coli Ribosome Obtained By Fitting Atomic Models For Rna And Protein Co" 99.17 119 100.00 100.00 4.02e-56 PDB 2GYC "Structure Of The 50s Subunit Of A Secm-Stalled E. Coli Ribosome Complex Obtained By Fitting Atomic Models For Rna And Protein C" 99.17 119 100.00 100.00 4.02e-56 PDB 2XTG "Trna Tranlocation On The 70s Ribosome: The Pre- Translocational Translocation Intermediate Ti(Pre)" 100.00 121 100.00 100.00 7.92e-57 PDB 2XUX "Trna Translocation On The 70s Ribosome: The Post- Translocational Translocation Intermediate Ti(Post)" 100.00 121 100.00 100.00 7.92e-57 PDB 3J5O "Visualization Of Two Trnas Trapped In Transit During Ef-g-mediated Translocation (50s Subunit)" 100.00 121 100.00 100.00 7.92e-57 PDB 3J5W "Structure Of The Ribosome With Elongation Factor G Trapped In The Pre- Translocation State (pre-translocation 70s*trna*ef-g Str" 100.00 120 100.00 100.00 7.35e-57 PDB 3J7Z "Structure Of The E. Coli 50s Subunit With Ermcl Nascent Chain" 100.00 121 100.00 100.00 7.92e-57 PDB 3SGF "Crystal Structure Of Release Factor Rf3 Trapped In The Gtp State On A Rotated Conformation Of The Ribosome" 100.00 121 100.00 100.00 7.92e-57 PDB 3UOS "Crystal Structure Of Release Factor Rf3 Trapped In The Gtp State On A Rotated Conformation Of The Ribosome (Without Viomycin)" 100.00 121 100.00 100.00 7.92e-57 PDB 4KIX "Control Of Ribosomal Subunit Rotation By Elongation Factor G" 100.00 121 100.00 100.00 7.92e-57 DBJ BAB38332 "50S ribosomal subunit protein L7/L12 [Escherichia coli O157:H7 str. Sakai]" 100.00 121 100.00 100.00 7.92e-57 DBJ BAE77334 "50S ribosomal subunit protein L7/L12 [Escherichia coli str. K12 substr. W3110]" 100.00 121 100.00 100.00 7.92e-57 DBJ BAG79797 "50S ribosomal protein L7/L12 [Escherichia coli SE11]" 100.00 121 100.00 100.00 7.92e-57 DBJ BAH61123 "50S ribosomal protein L7/L12 [Klebsiella pneumoniae subsp. pneumoniae NTUH-K2044]" 100.00 121 97.50 100.00 4.32e-56 DBJ BAI28246 "50S ribosomal subunit protein L7/L12 [Escherichia coli O26:H11 str. 11368]" 100.00 121 100.00 100.00 7.92e-57 EMBL CAA23624 "rplL (L7/L12) [Escherichia coli]" 100.00 121 100.00 100.00 7.92e-57 EMBL CAA37246 "unnamed protein product [Salmonella enterica subsp. enterica serovar Typhimurium]" 100.00 121 97.50 99.17 1.76e-54 EMBL CAD09488 "50S ribosomal subunit protein L7/L12 [Salmonella enterica subsp. enterica serovar Typhi str. CT18]" 100.00 121 97.50 99.17 1.76e-54 EMBL CAP78442 "50S ribosomal protein L7/L12 [Escherichia coli LF82]" 100.00 121 100.00 100.00 7.92e-57 EMBL CAQ34332 "50S ribosomal subunit protein L12, subunit of 50S ribosomal subunit protein L7/L12 dimer, 50S ribosomal protein complex L8, 50S" 100.00 121 100.00 100.00 7.92e-57 GB AAC43084 "50S ribosomal subunit protein L7/L12 [Escherichia coli str. K-12 substr. MG1655]" 100.00 121 100.00 100.00 7.92e-57 GB AAC76960 "50S ribosomal subunit protein L7/L12 [Escherichia coli str. K-12 substr. MG1655]" 100.00 121 100.00 100.00 7.92e-57 GB AAF33498 "Salmonella typhimurium 50S ribosomal protein L7 (RPLL) (SW:P18981); contains similarity to Pfam domain PF00542 (Ribosomal_L12)," 100.00 121 97.50 99.17 1.76e-54 GB AAG59182 "50S ribosomal subunit protein L7/L12 [Escherichia coli O157:H7 str. EDL933]" 100.00 121 100.00 100.00 7.92e-57 GB AAL22980 "50S ribosomal subunit protein L7/L12 [Salmonella enterica subsp. enterica serovar Typhimurium str. LT2]" 100.00 121 97.50 99.17 1.76e-54 PIR AF0933 "50S ribosomal chain protein L7/L12 [imported] - Salmonella enterica subsp. enterica serovar Typhi (strain CT18)" 100.00 121 97.50 99.17 1.76e-54 PRF 0601198A "polymerase beta,RNA" 56.67 253 100.00 100.00 3.56e-33 REF NP_312936 "50S ribosomal protein L7/L12 [Escherichia coli O157:H7 str. Sakai]" 100.00 121 100.00 100.00 7.92e-57 REF NP_418413 "50S ribosomal subunit protein L7/L12 [Escherichia coli str. K-12 substr. MG1655]" 100.00 121 100.00 100.00 7.92e-57 REF NP_457918 "50S ribosomal subunit protein L7/L12 [Salmonella enterica subsp. enterica serovar Typhi str. CT18]" 100.00 121 97.50 99.17 1.76e-54 REF NP_463021 "50S ribosomal protein L7/L12 [Salmonella enterica subsp. enterica serovar Typhimurium str. LT2]" 100.00 121 97.50 99.17 1.76e-54 REF NP_709781 "50S ribosomal protein L7/L12 [Shigella flexneri 2a str. 301]" 100.00 121 100.00 100.00 7.92e-57 SP A6TGN9 "RecName: Full=50S ribosomal protein L7/L12" 100.00 121 97.50 100.00 4.32e-56 SP A7ZUK0 "RecName: Full=50S ribosomal protein L7/L12" 100.00 121 100.00 100.00 7.92e-57 SP A8A785 "RecName: Full=50S ribosomal protein L7/L12" 100.00 121 100.00 100.00 7.92e-57 SP A8AKU0 "RecName: Full=50S ribosomal protein L7/L12" 100.00 121 98.33 100.00 2.59e-56 SP A9N0J3 "RecName: Full=50S ribosomal protein L7/L12" 100.00 121 97.50 99.17 1.76e-54 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species _Organelle $L7_L12 'E. coli' 562 Eubacteria . Escherichia coli ribosome 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 $L7_L12 'recombinant technology' 'E. coli' Escherichia coli XL1 plasmid . stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Saveframe_category sample _Sample_type solution _Details ; The protein L7/L12 degraded during 2-3 weeks due to spontaneous proteolysis in the hinge region. ; loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $L7_L12 1.0 mM '[U-95% 15N]' stop_ save_ ############################ # Computer software used # ############################ save_XEASY _Saveframe_category software _Name XEASY _Version 1.2.11 loop_ _Task 'peak assignments' stop_ _Details . _Citation_label $ref_1 save_ save_DYANA _Saveframe_category software _Name DYANA _Version 1.5 loop_ _Task 'structure calculation' stop_ _Details . _Citation_label $ref_2 save_ save_FANTOM _Saveframe_category software _Name FANTOM _Version 4 loop_ _Task 'energy minimization' stop_ _Details . _Citation_label $ref_3 save_ save_MOLMOL _Saveframe_category software _Name MOLMOL _Version 2.5.1 loop_ _Task 'visualization and structure analysis' stop_ _Details . _Citation_label $ref_4 save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model UNITY _Field_strength 600 _Details . save_ ############################# # NMR applied experiments # ############################# save_1H-15N_HMQC_1 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-15N HMQC' _Sample_label $sample_1 save_ save_1H-15N_HSQC_2 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-15N HSQC' _Sample_label $sample_1 save_ save_1H-15N_TOCSY-HSQC_3 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-15N TOCSY-HSQC' _Sample_label $sample_1 save_ save_1H-15N_NOESY-HSQC_4 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-15N NOESY-HSQC' _Sample_label $sample_1 save_ save_1H_TOCSY_5 _Saveframe_category NMR_applied_experiment _Experiment_name '1H TOCSY' _Sample_label $sample_1 save_ save_1H_NOESY_6 _Saveframe_category NMR_applied_experiment _Experiment_name '1H NOESY' _Sample_label $sample_1 save_ save_NMR_spec_expt__0_1 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-15N HMQC' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_2 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-15N HSQC' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_3 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-15N TOCSY-HSQC' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_4 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-15N NOESY-HSQC' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_5 _Saveframe_category NMR_applied_experiment _Experiment_name '1H TOCSY' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_6 _Saveframe_category NMR_applied_experiment _Experiment_name '1H NOESY' _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 6.9 0.1 n/a temperature 303 0.5 K 'ionic strength' 0.15 0.01 M stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chem_shift_ref _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_chem_shift_set_1 _Saveframe_category assigned_chemical_shifts _Details ; Several unassigned signals were observed in the 'random coil' region of HSQC spectrum that correspond to a minor conformations of interdomain flexible hinge region of L7 dimer. ; loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $sample_cond_1 _Chem_shift_reference_set_label $chem_shift_ref _Mol_system_component_name 'L7 dimer subunit A' _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 SER N N 123.3 0.1 1 2 . 1 SER H H 8.28 0.02 1 3 . 1 SER HA H 4.44 0.02 1 4 . 1 SER HB2 H 3.83 0.02 1 5 . 1 SER HB3 H 3.83 0.02 1 6 . 2 ILE N N 122.8 0.1 1 7 . 2 ILE H H 7.93 0.02 1 8 . 2 ILE HA H 4.48 0.02 1 9 . 2 ILE HB H 1.66 0.02 1 10 . 2 ILE HG2 H 0.80 0.02 1 11 . 2 ILE HG12 H 1.09 0.02 2 12 . 2 ILE HG13 H 1.45 0.02 2 13 . 2 ILE HD1 H 0.70 0.02 1 14 . 3 THR N N 117.1 0.1 1 15 . 3 THR H H 8.20 0.02 1 16 . 3 THR HA H 4.51 0.02 1 17 . 3 THR HB H 4.68 0.02 1 18 . 3 THR HG2 H 1.25 0.02 1 19 . 4 LYS N N 121.7 0.1 1 20 . 4 LYS H H 8.92 0.02 1 21 . 4 LYS HA H 3.79 0.02 1 22 . 4 LYS HB2 H 1.93 0.02 2 23 . 4 LYS HB3 H 1.81 0.02 2 24 . 4 LYS HG2 H 1.33 0.02 2 25 . 4 LYS HG3 H 1.53 0.02 2 26 . 4 LYS HD2 H 1.68 0.02 1 27 . 4 LYS HD3 H 1.68 0.02 1 28 . 4 LYS HE2 H 2.94 0.02 2 29 . 4 LYS HE3 H 2.99 0.02 2 30 . 5 ASP N N 117.7 0.1 1 31 . 5 ASP H H 8.18 0.02 1 32 . 5 ASP HA H 4.32 0.02 1 33 . 5 ASP HB2 H 2.47 0.02 2 34 . 5 ASP HB3 H 2.63 0.02 2 35 . 6 GLN N N 120.8 0.1 1 36 . 6 GLN H H 7.64 0.02 1 37 . 6 GLN HA H 4.05 0.02 1 38 . 6 GLN HB2 H 1.89 0.02 1 39 . 6 GLN HB3 H 1.89 0.02 1 40 . 6 GLN HG2 H 2.38 0.02 1 41 . 6 GLN HG3 H 2.38 0.02 1 42 . 6 GLN NE2 N 112.4 0.1 1 43 . 6 GLN HE21 H 7.54 0.02 2 44 . 6 GLN HE22 H 6.80 0.02 2 45 . 7 ILE N N 122.7 0.1 1 46 . 7 ILE H H 8.03 0.02 1 47 . 7 ILE HA H 3.44 0.02 1 48 . 7 ILE HB H 2.06 0.02 1 49 . 7 ILE HG2 H 0.79 0.02 1 50 . 7 ILE HG12 H 1.85 0.02 1 51 . 7 ILE HG13 H 1.85 0.02 1 52 . 7 ILE HD1 H 0.71 0.02 1 53 . 8 ILE N N 120.9 0.1 1 54 . 8 ILE H H 8.17 0.02 1 55 . 8 ILE HA H 3.60 0.02 1 56 . 8 ILE HB H 2.02 0.02 1 57 . 8 ILE HG2 H 0.93 0.02 1 58 . 8 ILE HG12 H 1.21 0.02 2 59 . 8 ILE HG13 H 1.67 0.02 2 60 . 8 ILE HD1 H 0.78 0.02 1 61 . 9 GLU N N 119.9 0.1 1 62 . 9 GLU H H 7.76 0.02 1 63 . 9 GLU HA H 4.03 0.02 1 64 . 9 GLU HB2 H 2.06 0.02 1 65 . 9 GLU HB3 H 2.06 0.02 1 66 . 9 GLU HG2 H 2.23 0.02 2 67 . 9 GLU HG3 H 2.37 0.02 2 68 . 10 ALA N N 123.3 0.1 1 69 . 10 ALA H H 7.86 0.02 1 70 . 10 ALA HA H 4.20 0.02 1 71 . 10 ALA HB H 1.51 0.02 1 72 . 11 VAL N N 119.6 0.1 1 73 . 11 VAL H H 8.48 0.02 1 74 . 11 VAL HA H 3.86 0.02 1 75 . 11 VAL HB H 2.19 0.02 1 76 . 11 VAL HG1 H 0.84 0.02 2 77 . 11 VAL HG2 H 1.06 0.02 2 78 . 12 ALA N N 122.7 0.1 1 79 . 12 ALA H H 7.81 0.02 1 80 . 12 ALA HA H 4.01 0.02 1 81 . 12 ALA HB H 1.58 0.02 1 82 . 13 ALA N N 119.0 0.1 1 83 . 13 ALA H H 7.16 0.02 1 84 . 13 ALA HA H 4.51 0.02 1 85 . 13 ALA HB H 1.49 0.02 1 86 . 14 MET N N 121.4 0.1 1 87 . 14 MET H H 7.55 0.02 1 88 . 14 MET HA H 4.44 0.02 1 89 . 14 MET HB2 H 2.18 0.02 2 90 . 14 MET HB3 H 2.27 0.02 2 91 . 14 MET HG2 H 2.69 0.02 2 92 . 14 MET HG3 H 2.91 0.02 2 93 . 14 MET HE H 1.89 0.02 1 94 . 15 SER N N 118.5 0.1 1 95 . 15 SER H H 8.96 0.02 1 96 . 15 SER HA H 4.55 0.02 1 97 . 15 SER HB2 H 4.27 0.02 2 98 . 15 SER HB3 H 4.05 0.02 2 99 . 16 VAL N N 123.0 0.1 1 100 . 16 VAL H H 8.69 0.02 1 101 . 16 VAL HA H 3.62 0.02 1 102 . 16 VAL HB H 2.10 0.02 1 103 . 16 VAL HG1 H 1.10 0.02 2 104 . 16 VAL HG2 H 0.99 0.02 2 105 . 17 MET N N 118.4 0.1 1 106 . 17 MET H H 8.14 0.02 1 107 . 17 MET HA H 4.24 0.02 1 108 . 17 MET HB2 H 2.02 0.02 2 109 . 17 MET HB3 H 2.06 0.02 2 110 . 17 MET HG2 H 2.63 0.02 2 111 . 17 MET HG3 H 2.69 0.02 2 112 . 17 MET HE H 2.12 0.02 1 113 . 18 ASP N N 121.8 0.1 1 114 . 18 ASP H H 7.61 0.02 1 115 . 18 ASP HA H 4.42 0.02 1 116 . 18 ASP HB2 H 2.66 0.02 2 117 . 18 ASP HB3 H 3.02 0.02 2 118 . 19 VAL N N 123.2 0.1 1 119 . 19 VAL H H 7.99 0.02 1 120 . 19 VAL HA H 3.48 0.02 1 121 . 19 VAL HB H 2.08 0.02 1 122 . 19 VAL HG1 H 0.75 0.02 2 123 . 19 VAL HG2 H 0.80 0.02 2 124 . 20 VAL N N 121.3 0.1 1 125 . 20 VAL H H 8.27 0.02 1 126 . 20 VAL HA H 3.52 0.02 1 127 . 20 VAL HB H 2.20 0.02 1 128 . 20 VAL HG1 H 0.95 0.02 2 129 . 20 VAL HG2 H 1.07 0.02 2 130 . 21 GLU N N 121.6 0.1 1 131 . 21 GLU H H 7.80 0.02 1 132 . 21 GLU HA H 4.04 0.02 1 133 . 21 GLU HB2 H 2.19 0.02 2 134 . 21 GLU HB3 H 2.11 0.02 2 135 . 21 GLU HG2 H 2.49 0.02 1 136 . 21 GLU HG3 H 2.49 0.02 1 137 . 22 LEU N N 123.7 0.1 1 138 . 22 LEU H H 8.18 0.02 1 139 . 22 LEU HA H 4.08 0.02 1 140 . 22 LEU HB2 H 1.79 0.02 2 141 . 22 LEU HB3 H 1.88 0.02 2 142 . 22 LEU HG H 1.70 0.02 1 143 . 22 LEU HD1 H 0.88 0.02 2 144 . 22 LEU HD2 H 0.92 0.02 2 145 . 23 ILE N N 121.3 0.1 1 146 . 23 ILE H H 8.80 0.02 1 147 . 23 ILE HA H 3.63 0.02 1 148 . 23 ILE HB H 1.89 0.02 1 149 . 23 ILE HG2 H 0.91 0.02 1 150 . 23 ILE HG12 H 1.04 0.02 2 151 . 23 ILE HG13 H 1.44 0.02 2 152 . 23 ILE HD1 H 0.83 0.02 1 153 . 24 SER N N 116.2 0.1 1 154 . 24 SER H H 8.12 0.02 1 155 . 24 SER HA H 4.25 0.02 1 156 . 24 SER HB2 H 3.98 0.02 2 157 . 24 SER HB3 H 4.02 0.02 2 158 . 25 ALA N N 125.3 0.1 1 159 . 25 ALA H H 8.01 0.02 1 160 . 25 ALA HA H 4.25 0.02 1 161 . 25 ALA HB H 1.54 0.02 1 162 . 26 MET N N 119.9 0.1 1 163 . 26 MET H H 8.50 0.02 1 164 . 26 MET HA H 4.00 0.02 1 165 . 26 MET HB2 H 1.98 0.02 2 166 . 26 MET HB3 H 2.21 0.02 2 167 . 26 MET HG2 H 2.93 0.02 2 168 . 26 MET HG3 H 2.40 0.02 2 169 . 26 MET HE H 1.94 0.02 1 170 . 27 GLU N N 120.3 0.1 1 171 . 27 GLU H H 8.59 0.02 1 172 . 27 GLU HA H 3.96 0.02 1 173 . 27 GLU HB2 H 2.23 0.02 2 174 . 27 GLU HB3 H 2.09 0.02 2 175 . 27 GLU HG2 H 2.26 0.02 2 176 . 27 GLU HG3 H 2.60 0.02 2 177 . 28 GLU N N 120.2 0.1 1 178 . 28 GLU H H 7.93 0.02 1 179 . 28 GLU HA H 4.05 0.02 1 180 . 28 GLU HB2 H 2.13 0.02 2 181 . 28 GLU HB3 H 2.09 0.02 2 182 . 28 GLU HG2 H 2.23 0.02 2 183 . 28 GLU HG3 H 2.37 0.02 2 184 . 29 LYS N N 119.3 0.1 1 185 . 29 LYS H H 7.77 0.02 1 186 . 29 LYS HA H 3.99 0.02 1 187 . 29 LYS HB2 H 1.58 0.02 2 188 . 29 LYS HB3 H 1.33 0.02 2 189 . 29 LYS HG2 H 1.00 0.02 2 190 . 29 LYS HG3 H 1.15 0.02 2 191 . 29 LYS HD2 H 1.46 0.02 1 192 . 29 LYS HD3 H 1.46 0.02 1 193 . 29 LYS HE2 H 2.83 0.02 2 194 . 29 LYS HE3 H 2.91 0.02 2 195 . 30 PHE N N 116.5 0.1 1 196 . 30 PHE H H 7.99 0.02 1 197 . 30 PHE HA H 4.72 0.02 1 198 . 30 PHE HB2 H 2.89 0.02 2 199 . 30 PHE HB3 H 3.35 0.02 2 200 . 30 PHE HD1 H 7.36 0.02 1 201 . 30 PHE HD2 H 7.36 0.02 1 202 . 30 PHE HE1 H 7.26 0.02 1 203 . 30 PHE HE2 H 7.26 0.02 1 204 . 30 PHE HZ H 7.33 0.02 1 205 . 31 GLY N N 110.5 0.1 1 206 . 31 GLY H H 7.92 0.02 1 207 . 31 GLY HA2 H 4.01 0.02 1 208 . 31 GLY HA3 H 4.01 0.02 1 209 . 32 VAL N N 118.7 0.1 1 210 . 32 VAL H H 7.74 0.02 1 211 . 32 VAL HA H 4.16 0.02 1 212 . 32 VAL HB H 2.09 0.02 1 213 . 32 VAL HG1 H 0.91 0.02 1 214 . 32 VAL HG2 H 0.91 0.02 1 215 . 33 SER N N 119.2 0.1 1 216 . 33 SER H H 8.33 0.02 1 217 . 33 SER HA H 4.45 0.02 1 218 . 33 SER HB2 H 3.87 0.02 1 219 . 33 SER HB3 H 3.87 0.02 1 220 . 34 ALA N N 127.7 0.1 1 221 . 34 ALA H H 8.46 0.02 1 222 . 34 ALA HA H 4.24 0.02 1 223 . 34 ALA HB H 1.36 0.02 1 224 . 35 ALA N N 123.4 0.1 1 225 . 35 ALA H H 8.10 0.02 1 226 . 35 ALA HA H 4.22 0.02 1 227 . 35 ALA HB H 1.38 0.02 1 228 . 36 ALA N N 123.7 0.1 1 229 . 36 ALA H H 8.03 0.02 1 230 . 36 ALA HA H 4.24 0.02 1 231 . 36 ALA HB H 1.41 0.02 1 232 . 37 ALA N N 124.1 0.1 1 233 . 37 ALA H H 8.03 0.02 1 234 . 37 ALA HA H 4.28 0.02 1 235 . 37 ALA HB H 1.41 0.02 1 236 . 38 VAL N N 120.0 0.1 1 237 . 38 VAL H H 7.88 0.02 1 238 . 38 VAL HA H 4.04 0.02 1 239 . 38 VAL HB H 2.07 0.02 1 240 . 38 VAL HG1 H 0.94 0.02 1 241 . 38 VAL HG2 H 0.94 0.02 1 242 . 39 ALA N N 128.7 0.1 1 243 . 39 ALA H H 8.16 0.02 1 244 . 39 ALA HA H 4.33 0.02 1 245 . 39 ALA HB H 1.37 0.02 1 246 . 40 VAL N N 121.0 0.1 1 247 . 40 VAL H H 8.02 0.02 1 248 . 40 VAL HA H 4.05 0.02 1 249 . 40 VAL HB H 2.06 0.02 1 250 . 40 VAL HG1 H 0.94 0.02 1 251 . 40 VAL HG2 H 0.94 0.02 1 252 . 41 ALA N N 129.4 0.1 1 253 . 41 ALA H H 8.27 0.02 1 254 . 41 ALA HA H 4.31 0.02 1 255 . 41 ALA HB H 1.38 0.02 1 256 . 42 ALA N N 125.4 0.1 1 257 . 42 ALA H H 8.23 0.02 1 258 . 42 ALA HA H 4.34 0.02 1 259 . 42 ALA HB H 1.41 0.02 1 260 . 43 GLY N N 110.0 0.1 1 261 . 43 GLY H H 8.15 0.02 1 262 . 43 GLY HA2 H 3.97 0.02 2 263 . 43 GLY HA3 H 4.20 0.02 2 264 . 44 PRO HA H 4.46 0.02 1 265 . 44 PRO HB2 H 1.92 0.02 2 266 . 44 PRO HB3 H 2.25 0.02 2 267 . 44 PRO HG2 H 2.04 0.02 2 268 . 44 PRO HG3 H 2.14 0.02 2 269 . 44 PRO HD2 H 3.63 0.02 1 270 . 44 PRO HD3 H 3.63 0.02 1 271 . 45 VAL N N 122.2 0.1 1 272 . 45 VAL H H 8.27 0.02 1 273 . 45 VAL HA H 4.08 0.02 1 274 . 45 VAL HB H 2.07 0.02 1 275 . 45 VAL HG1 H 0.94 0.02 1 276 . 45 VAL HG2 H 0.94 0.02 1 277 . 46 GLU N N 126.7 0.1 1 278 . 46 GLU H H 8.47 0.02 1 279 . 46 GLU HA H 4.28 0.02 1 280 . 46 GLU HB2 H 1.92 0.02 2 281 . 46 GLU HB3 H 2.02 0.02 2 282 . 46 GLU HG2 H 2.26 0.02 1 283 . 46 GLU HG3 H 2.26 0.02 1 284 . 47 ALA N N 127.5 0.1 1 285 . 47 ALA H H 8.35 0.02 1 286 . 47 ALA HA H 4.32 0.02 1 287 . 47 ALA HB H 1.38 0.02 1 288 . 48 ALA N N 125.6 0.1 1 289 . 48 ALA H H 8.29 0.02 1 290 . 48 ALA HA H 4.32 0.02 1 291 . 48 ALA HB H 1.39 0.02 1 292 . 49 GLU N N 121.9 0.1 1 293 . 49 GLU H H 8.37 0.02 1 294 . 49 GLU HA H 4.28 0.02 1 295 . 49 GLU HB2 H 1.93 0.02 2 296 . 49 GLU HB3 H 2.05 0.02 2 297 . 49 GLU HG2 H 2.27 0.02 1 298 . 49 GLU HG3 H 2.27 0.02 1 299 . 50 GLU N N 124.3 0.1 1 300 . 50 GLU H H 8.39 0.02 1 301 . 50 GLU HA H 4.31 0.02 1 302 . 50 GLU HB2 H 1.94 0.02 2 303 . 50 GLU HB3 H 2.03 0.02 2 304 . 50 GLU HG2 H 2.27 0.02 1 305 . 50 GLU HG3 H 2.27 0.02 1 306 . 51 LYS N N 125.9 0.1 1 307 . 51 LYS H H 8.34 0.02 1 308 . 51 LYS HA H 4.37 0.02 1 309 . 51 LYS HB2 H 1.70 0.02 1 310 . 51 LYS HB3 H 1.70 0.02 1 311 . 51 LYS HG2 H 1.17 0.02 2 312 . 51 LYS HG3 H 1.03 0.02 2 313 . 51 LYS HD2 H 1.56 0.02 1 314 . 51 LYS HD3 H 1.56 0.02 1 315 . 51 LYS HE2 H 2.69 0.02 2 316 . 51 LYS HE3 H 2.84 0.02 2 317 . 52 THR N N 113.9 0.1 1 318 . 52 THR H H 8.40 0.02 1 319 . 52 THR HA H 4.49 0.02 1 320 . 52 THR HB H 4.41 0.02 1 321 . 52 THR HG2 H 1.16 0.02 1 322 . 52 THR HG1 H 4.34 0.02 1 323 . 53 GLU N N 123.3 0.1 1 324 . 53 GLU H H 7.11 0.02 1 325 . 53 GLU HA H 4.68 0.02 1 326 . 53 GLU HB2 H 1.72 0.02 1 327 . 53 GLU HB3 H 1.72 0.02 1 328 . 53 GLU HG2 H 2.02 0.02 2 329 . 53 GLU HG3 H 2.04 0.02 2 330 . 54 PHE N N 121.9 0.1 1 331 . 54 PHE H H 9.57 0.02 1 332 . 54 PHE HA H 4.65 0.02 1 333 . 54 PHE HB2 H 2.34 0.02 2 334 . 54 PHE HB3 H 2.85 0.02 2 335 . 54 PHE HD1 H 7.11 0.02 1 336 . 54 PHE HD2 H 7.11 0.02 1 337 . 54 PHE HE1 H 7.18 0.02 1 338 . 54 PHE HE2 H 7.18 0.02 1 339 . 54 PHE HZ H 7.22 0.02 1 340 . 55 ASP N N 121.6 0.1 1 341 . 55 ASP H H 9.46 0.02 1 342 . 55 ASP HA H 5.42 0.02 1 343 . 55 ASP HB2 H 2.56 0.02 2 344 . 55 ASP HB3 H 2.60 0.02 2 345 . 56 VAL N N 120.7 0.1 1 346 . 56 VAL H H 8.67 0.02 1 347 . 56 VAL HA H 4.60 0.02 1 348 . 56 VAL HB H 1.94 0.02 1 349 . 56 VAL HG1 H 0.73 0.02 2 350 . 56 VAL HG2 H 0.95 0.02 2 351 . 57 ILE N N 131.0 0.1 1 352 . 57 ILE H H 9.56 0.02 1 353 . 57 ILE HA H 4.39 0.02 1 354 . 57 ILE HB H 2.07 0.02 1 355 . 57 ILE HG2 H 0.62 0.02 1 356 . 57 ILE HG12 H 1.32 0.02 2 357 . 57 ILE HG13 H 1.67 0.02 2 358 . 57 ILE HD1 H 0.77 0.02 1 359 . 58 LEU N N 129.9 0.1 1 360 . 58 LEU H H 8.96 0.02 1 361 . 58 LEU HA H 4.44 0.02 1 362 . 58 LEU HB2 H 1.11 0.02 2 363 . 58 LEU HB3 H 2.16 0.02 2 364 . 58 LEU HG H 1.33 0.02 1 365 . 58 LEU HD1 H 0.83 0.02 1 366 . 58 LEU HD2 H 0.83 0.02 1 367 . 59 LYS N N 131.2 0.1 1 368 . 59 LYS H H 8.80 0.02 1 369 . 59 LYS HA H 4.07 0.02 1 370 . 59 LYS HB2 H 1.46 0.02 2 371 . 59 LYS HB3 H 1.67 0.02 2 372 . 59 LYS HG2 H 1.31 0.02 2 373 . 59 LYS HG3 H 1.44 0.02 2 374 . 60 ALA N N 118.5 0.1 1 375 . 60 ALA H H 7.73 0.02 1 376 . 60 ALA HA H 4.38 0.02 1 377 . 60 ALA HB H 1.40 0.02 1 378 . 61 ALA N N 124.6 0.1 1 379 . 61 ALA H H 9.21 0.02 1 380 . 61 ALA HA H 4.10 0.02 1 381 . 61 ALA HB H 1.39 0.02 1 382 . 62 GLY N N 103.1 0.1 1 383 . 62 GLY H H 7.85 0.02 1 384 . 62 GLY HA2 H 3.68 0.02 2 385 . 62 GLY HA3 H 4.19 0.02 2 386 . 63 ALA N N 122.6 0.1 1 387 . 63 ALA H H 8.47 0.02 1 388 . 63 ALA HA H 4.24 0.02 1 389 . 63 ALA HB H 1.43 0.02 1 390 . 64 ASN N N 122.9 0.1 1 391 . 64 ASN H H 9.64 0.02 1 392 . 64 ASN HA H 5.04 0.02 1 393 . 64 ASN HB2 H 2.65 0.02 2 394 . 64 ASN HB3 H 3.36 0.02 2 395 . 64 ASN ND2 N 113.8 0.1 1 396 . 64 ASN HD21 H 7.54 0.02 2 397 . 64 ASN HD22 H 6.85 0.02 2 398 . 65 LYS N N 122.9 0.1 1 399 . 65 LYS H H 7.98 0.02 1 400 . 65 LYS HA H 3.62 0.02 1 401 . 65 LYS HB2 H 1.90 0.02 2 402 . 65 LYS HB3 H 1.76 0.02 2 403 . 65 LYS HG2 H 1.34 0.02 2 404 . 65 LYS HG3 H 1.42 0.02 2 405 . 65 LYS HD2 H 1.68 0.02 1 406 . 65 LYS HD3 H 1.68 0.02 1 407 . 65 LYS HE2 H 2.94 0.02 1 408 . 65 LYS HE3 H 2.94 0.02 1 409 . 66 VAL N N 118.7 0.1 1 410 . 66 VAL H H 8.24 0.02 1 411 . 66 VAL HA H 3.59 0.02 1 412 . 66 VAL HB H 2.11 0.02 1 413 . 66 VAL HG1 H 0.97 0.02 2 414 . 66 VAL HG2 H 1.08 0.02 2 415 . 67 ALA N N 123.7 0.1 1 416 . 67 ALA H H 7.37 0.02 1 417 . 67 ALA HA H 4.14 0.02 1 418 . 67 ALA HB H 1.56 0.02 1 419 . 68 VAL N N 122.4 0.1 1 420 . 68 VAL H H 7.93 0.02 1 421 . 68 VAL HA H 3.47 0.02 1 422 . 68 VAL HB H 2.19 0.02 1 423 . 68 VAL HG1 H 0.89 0.02 2 424 . 68 VAL HG2 H 1.23 0.02 2 425 . 69 ILE N N 123.1 0.1 1 426 . 69 ILE H H 8.79 0.02 1 427 . 69 ILE HA H 3.34 0.02 1 428 . 69 ILE HB H 1.96 0.02 1 429 . 69 ILE HG2 H 0.80 0.02 1 430 . 69 ILE HD1 H 0.70 0.02 1 431 . 70 LYS N N 120.5 0.1 1 432 . 70 LYS H H 7.82 0.02 1 433 . 70 LYS HA H 3.87 0.02 1 434 . 70 LYS HB2 H 1.93 0.02 1 435 . 70 LYS HB3 H 1.93 0.02 1 436 . 70 LYS HG2 H 1.39 0.02 2 437 . 70 LYS HG3 H 1.58 0.02 2 438 . 70 LYS HD2 H 1.66 0.02 1 439 . 70 LYS HD3 H 1.66 0.02 1 440 . 70 LYS HE2 H 2.94 0.02 1 441 . 70 LYS HE3 H 2.94 0.02 1 442 . 71 ALA N N 124.4 0.1 1 443 . 71 ALA H H 7.98 0.02 1 444 . 71 ALA HA H 4.24 0.02 1 445 . 71 ALA HB H 1.43 0.02 1 446 . 72 VAL N N 121.2 0.1 1 447 . 72 VAL H H 8.95 0.02 1 448 . 72 VAL HA H 3.44 0.02 1 449 . 72 VAL HB H 2.29 0.02 1 450 . 72 VAL HG1 H 0.92 0.02 2 451 . 72 VAL HG2 H 0.99 0.02 2 452 . 73 ARG N N 124.9 0.1 1 453 . 73 ARG H H 8.82 0.02 1 454 . 73 ARG HA H 3.86 0.02 1 455 . 73 ARG HB2 H 2.03 0.02 1 456 . 73 ARG HB3 H 2.03 0.02 1 457 . 73 ARG HG2 H 1.79 0.02 1 458 . 73 ARG HG3 H 1.79 0.02 1 459 . 73 ARG HD2 H 2.97 0.02 2 460 . 73 ARG HD3 H 3.11 0.02 2 461 . 74 GLY N N 108.0 0.1 1 462 . 74 GLY H H 8.25 0.02 1 463 . 74 GLY HA2 H 3.85 0.02 2 464 . 74 GLY HA3 H 3.96 0.02 2 465 . 75 ALA N N 121.0 0.1 1 466 . 75 ALA H H 7.67 0.02 1 467 . 75 ALA HA H 4.44 0.02 1 468 . 75 ALA HB H 1.44 0.02 1 469 . 76 THR N N 105.0 0.1 1 470 . 76 THR H H 7.71 0.02 1 471 . 76 THR HA H 4.62 0.02 1 472 . 76 THR HB H 4.29 0.02 1 473 . 76 THR HG2 H 1.23 0.02 1 474 . 76 THR HG1 H 4.49 0.02 1 475 . 77 GLY N N 113.4 0.1 1 476 . 77 GLY H H 8.38 0.02 1 477 . 77 GLY HA2 H 3.88 0.02 2 478 . 77 GLY HA3 H 4.21 0.02 2 479 . 78 LEU N N 122.4 0.1 1 480 . 78 LEU H H 7.64 0.02 1 481 . 78 LEU HA H 4.22 0.02 1 482 . 78 LEU HB2 H 1.42 0.02 2 483 . 78 LEU HB3 H 1.60 0.02 2 484 . 78 LEU HG H 1.63 0.02 1 485 . 78 LEU HD1 H 0.75 0.02 2 486 . 78 LEU HD2 H 0.86 0.02 2 487 . 79 GLY N N 108.1 0.1 1 488 . 79 GLY H H 8.43 0.02 1 489 . 79 GLY HA2 H 4.10 0.02 2 490 . 79 GLY HA3 H 3.98 0.02 2 491 . 80 LEU N N 121.6 0.1 1 492 . 80 LEU H H 8.48 0.02 1 493 . 80 LEU HA H 3.78 0.02 1 494 . 80 LEU HB2 H 1.53 0.02 2 495 . 80 LEU HB3 H 1.74 0.02 2 496 . 80 LEU HG H 1.58 0.02 1 497 . 80 LEU HD1 H 0.90 0.02 1 498 . 80 LEU HD2 H 0.90 0.02 1 499 . 81 LYS N N 120.1 0.1 1 500 . 81 LYS H H 8.41 0.02 1 501 . 81 LYS HA H 3.83 0.02 1 502 . 81 LYS HB2 H 1.84 0.02 2 503 . 81 LYS HB3 H 1.70 0.02 2 504 . 81 LYS HG2 H 1.37 0.02 2 505 . 81 LYS HG3 H 1.42 0.02 2 506 . 81 LYS HD2 H 1.53 0.02 2 507 . 82 GLU N N 119.8 0.1 1 508 . 82 GLU H H 8.60 0.02 1 509 . 82 GLU HA H 4.00 0.02 1 510 . 82 GLU HB2 H 2.15 0.02 2 511 . 82 GLU HB3 H 1.92 0.02 2 512 . 82 GLU HG2 H 2.28 0.02 2 513 . 82 GLU HG3 H 1.90 0.02 2 514 . 83 ALA N N 124.2 0.1 1 515 . 83 ALA H H 8.79 0.02 1 516 . 83 ALA HA H 3.96 0.02 1 517 . 83 ALA HB H 1.37 0.02 1 518 . 84 LYS N N 121.0 0.1 1 519 . 84 LYS H H 8.47 0.02 1 520 . 84 LYS HA H 3.73 0.02 1 521 . 84 LYS HB2 H 1.79 0.02 2 522 . 84 LYS HB3 H 2.07 0.02 2 523 . 84 LYS HG2 H 1.37 0.02 1 524 . 84 LYS HG3 H 1.37 0.02 1 525 . 84 LYS HD2 H 1.65 0.02 2 526 . 84 LYS HD3 H 1.64 0.02 2 527 . 84 LYS HE2 H 2.99 0.02 1 528 . 84 LYS HE3 H 2.99 0.02 1 529 . 85 ASP N N 120.2 0.1 1 530 . 85 ASP H H 8.32 0.02 1 531 . 85 ASP HA H 4.28 0.02 1 532 . 85 ASP HB2 H 2.71 0.02 2 533 . 85 ASP HB3 H 2.58 0.02 2 534 . 86 LEU N N 123.4 0.1 1 535 . 86 LEU H H 7.73 0.02 1 536 . 86 LEU HA H 3.99 0.02 1 537 . 86 LEU HB2 H 1.72 0.02 1 538 . 86 LEU HB3 H 1.72 0.02 1 539 . 86 LEU HG H 1.51 0.02 1 540 . 86 LEU HD1 H 0.87 0.02 2 541 . 86 LEU HD2 H 0.80 0.02 2 542 . 87 VAL N N 120.2 0.1 1 543 . 87 VAL H H 8.12 0.02 1 544 . 87 VAL HA H 3.38 0.02 1 545 . 87 VAL HB H 2.16 0.02 1 546 . 87 VAL HG1 H 0.88 0.02 2 547 . 87 VAL HG2 H 0.98 0.02 2 548 . 88 GLU N N 119.0 0.1 1 549 . 88 GLU H H 8.43 0.02 1 550 . 88 GLU HA H 4.12 0.02 1 551 . 88 GLU HB2 H 2.06 0.02 2 552 . 88 GLU HB3 H 2.16 0.02 2 553 . 88 GLU HG2 H 2.28 0.02 2 554 . 88 GLU HG3 H 2.52 0.02 2 555 . 89 SER N N 116.6 0.1 1 556 . 89 SER H H 7.64 0.02 1 557 . 89 SER HA H 4.58 0.02 1 558 . 89 SER HB2 H 3.95 0.02 2 559 . 89 SER HB3 H 4.04 0.02 2 560 . 89 SER HG H 4.76 0.02 1 561 . 90 ALA N N 124.4 0.1 1 562 . 90 ALA H H 6.87 0.02 1 563 . 90 ALA HA H 4.00 0.02 1 564 . 90 ALA HB H 1.27 0.02 1 565 . 91 PRO HA H 5.30 0.02 1 566 . 91 PRO HB2 H 2.31 0.02 2 567 . 91 PRO HB3 H 2.04 0.02 2 568 . 91 PRO HG2 H 1.98 0.02 2 569 . 91 PRO HG3 H 2.09 0.02 2 570 . 91 PRO HD2 H 3.67 0.02 2 571 . 92 ALA N N 127.1 0.1 1 572 . 92 ALA H H 8.45 0.02 1 573 . 92 ALA HA H 4.61 0.02 1 574 . 92 ALA HB H 1.23 0.02 1 575 . 93 ALA N N 125.9 0.1 1 576 . 93 ALA H H 8.79 0.02 1 577 . 93 ALA HA H 4.38 0.02 1 578 . 93 ALA HB H 1.22 0.02 1 579 . 94 LEU N N 124.3 0.1 1 580 . 94 LEU H H 7.33 0.02 1 581 . 94 LEU HA H 4.42 0.02 1 582 . 94 LEU HB2 H 1.48 0.02 2 583 . 94 LEU HB3 H 1.41 0.02 2 584 . 94 LEU HG H 1.67 0.02 1 585 . 94 LEU HD1 H 0.82 0.02 2 586 . 94 LEU HD2 H 0.77 0.02 2 587 . 95 LYS N N 124.3 0.1 1 588 . 95 LYS H H 9.03 0.02 1 589 . 95 LYS HA H 4.56 0.02 1 590 . 95 LYS HB2 H 1.38 0.02 2 591 . 95 LYS HB3 H 1.70 0.02 2 592 . 96 GLU N N 123.5 0.1 1 593 . 96 GLU H H 8.63 0.02 1 594 . 96 GLU HA H 5.01 0.02 1 595 . 96 GLU HB2 H 1.78 0.02 2 596 . 96 GLU HB3 H 1.94 0.02 2 597 . 96 GLU HG2 H 1.74 0.02 2 598 . 96 GLU HG3 H 1.99 0.02 2 599 . 97 GLY N N 115.4 0.1 1 600 . 97 GLY H H 8.57 0.02 1 601 . 97 GLY HA2 H 3.69 0.02 2 602 . 97 GLY HA3 H 3.87 0.02 2 603 . 98 VAL N N 116.1 0.1 1 604 . 98 VAL H H 9.23 0.02 1 605 . 98 VAL HA H 4.80 0.02 1 606 . 98 VAL HB H 2.54 0.02 1 607 . 98 VAL HG1 H 0.93 0.02 2 608 . 98 VAL HG2 H 0.84 0.02 2 609 . 99 SER N N 117.6 0.1 1 610 . 99 SER H H 8.96 0.02 1 611 . 99 SER HA H 4.73 0.02 1 612 . 99 SER HB2 H 4.45 0.02 2 613 . 99 SER HB3 H 4.18 0.02 2 614 . 99 SER HG H 4.75 0.02 1 615 . 100 LYS N N 123.5 0.1 1 616 . 100 LYS H H 9.14 0.02 1 617 . 100 LYS HA H 3.23 0.02 1 618 . 100 LYS HB2 H 1.73 0.02 1 619 . 100 LYS HB3 H 1.73 0.02 1 620 . 100 LYS HG2 H 0.86 0.02 2 621 . 100 LYS HG3 H 1.17 0.02 2 622 . 100 LYS HD2 H 1.31 0.02 2 623 . 100 LYS HD3 H 1.45 0.02 2 624 . 100 LYS HE2 H 2.79 0.02 1 625 . 100 LYS HE3 H 2.79 0.02 1 626 . 101 ASP N N 117.8 0.1 1 627 . 101 ASP H H 8.38 0.02 1 628 . 101 ASP HA H 4.29 0.02 1 629 . 101 ASP HB2 H 2.48 0.02 2 630 . 101 ASP HB3 H 2.62 0.02 2 631 . 102 ASP N N 123.7 0.1 1 632 . 102 ASP H H 7.82 0.02 1 633 . 102 ASP HA H 4.41 0.02 1 634 . 102 ASP HB2 H 2.82 0.02 2 635 . 102 ASP HB3 H 2.51 0.02 2 636 . 103 ALA N N 125.3 0.1 1 637 . 103 ALA H H 8.78 0.02 1 638 . 103 ALA HA H 3.77 0.02 1 639 . 103 ALA HB H 1.22 0.02 1 640 . 104 GLU N N 118.1 0.1 1 641 . 104 GLU H H 8.30 0.02 1 642 . 104 GLU HA H 3.87 0.02 1 643 . 104 GLU HB2 H 2.01 0.02 1 644 . 104 GLU HB3 H 2.01 0.02 1 645 . 104 GLU HG2 H 2.19 0.02 2 646 . 104 GLU HG3 H 2.33 0.02 2 647 . 105 ALA N N 123.6 0.1 1 648 . 105 ALA H H 7.80 0.02 1 649 . 105 ALA HA H 4.15 0.02 1 650 . 105 ALA HB H 1.52 0.02 1 651 . 106 LEU N N 122.5 0.1 1 652 . 106 LEU H H 7.82 0.02 1 653 . 106 LEU HA H 4.17 0.02 1 654 . 106 LEU HB2 H 1.81 0.02 2 655 . 106 LEU HB3 H 1.59 0.02 2 656 . 106 LEU HG H 1.68 0.02 1 657 . 106 LEU HD1 H 0.87 0.02 2 658 . 106 LEU HD2 H 0.83 0.02 2 659 . 107 LYS N N 121.1 0.1 1 660 . 107 LYS H H 8.42 0.02 1 661 . 107 LYS HA H 3.68 0.02 1 662 . 107 LYS HB2 H 1.97 0.02 1 663 . 107 LYS HB3 H 1.97 0.02 1 664 . 107 LYS HG2 H 1.16 0.02 2 665 . 107 LYS HG3 H 1.49 0.02 2 666 . 107 LYS HD2 H 1.52 0.02 1 667 . 107 LYS HD3 H 1.52 0.02 1 668 . 107 LYS HE2 H 3.02 0.02 1 669 . 107 LYS HE3 H 3.02 0.02 1 670 . 108 LYS N N 119.0 0.1 1 671 . 108 LYS H H 8.07 0.02 1 672 . 108 LYS HA H 4.10 0.02 1 673 . 108 LYS HB2 H 1.88 0.02 1 674 . 108 LYS HB3 H 1.88 0.02 1 675 . 108 LYS HG2 H 1.42 0.02 2 676 . 108 LYS HG3 H 1.54 0.02 2 677 . 108 LYS HD2 H 1.67 0.02 1 678 . 108 LYS HD3 H 1.67 0.02 1 679 . 108 LYS HE2 H 2.98 0.02 1 680 . 108 LYS HE3 H 2.98 0.02 1 681 . 109 ALA N N 121.7 0.1 1 682 . 109 ALA H H 7.63 0.02 1 683 . 109 ALA HA H 4.14 0.02 1 684 . 109 ALA HB H 1.49 0.02 1 685 . 110 LEU N N 119.5 0.1 1 686 . 110 LEU H H 8.15 0.02 1 687 . 110 LEU HA H 3.98 0.02 1 688 . 110 LEU HB2 H 1.93 0.02 2 689 . 110 LEU HB3 H 1.14 0.02 2 690 . 110 LEU HG H 1.76 0.02 1 691 . 110 LEU HD1 H 0.85 0.02 2 692 . 110 LEU HD2 H 0.71 0.02 2 693 . 111 GLU N N 122.6 0.1 1 694 . 111 GLU H H 8.89 0.02 1 695 . 111 GLU HA H 4.38 0.02 1 696 . 111 GLU HB2 H 2.21 0.02 2 697 . 111 GLU HB3 H 1.99 0.02 2 698 . 111 GLU HG2 H 2.33 0.02 2 699 . 111 GLU HG3 H 2.61 0.02 2 700 . 112 GLU N N 123.6 0.1 1 701 . 112 GLU H H 8.29 0.02 1 702 . 112 GLU HA H 4.08 0.02 1 703 . 112 GLU HB2 H 2.19 0.02 2 704 . 112 GLU HB3 H 2.07 0.02 2 705 . 112 GLU HG2 H 2.30 0.02 2 706 . 112 GLU HG3 H 2.52 0.02 2 707 . 113 ALA N N 120.4 0.1 1 708 . 113 ALA H H 7.03 0.02 1 709 . 113 ALA HA H 4.40 0.02 1 710 . 113 ALA HB H 1.45 0.02 1 711 . 114 GLY N N 107.6 0.1 1 712 . 114 GLY H H 7.77 0.02 1 713 . 114 GLY HA2 H 3.72 0.02 2 714 . 114 GLY HA3 H 4.50 0.02 2 715 . 115 ALA N N 123.3 0.1 1 716 . 115 ALA H H 7.63 0.02 1 717 . 115 ALA HA H 4.24 0.02 1 718 . 115 ALA HB H 1.24 0.02 1 719 . 116 GLU N N 119.8 0.1 1 720 . 116 GLU H H 8.27 0.02 1 721 . 116 GLU HA H 4.79 0.02 1 722 . 116 GLU HB2 H 1.85 0.02 2 723 . 116 GLU HB3 H 1.98 0.02 2 724 . 116 GLU HG2 H 2.32 0.02 2 725 . 116 GLU HG3 H 2.04 0.02 2 726 . 117 VAL N N 127.6 0.1 1 727 . 117 VAL H H 9.29 0.02 1 728 . 117 VAL HA H 5.03 0.02 1 729 . 117 VAL HB H 1.89 0.02 1 730 . 117 VAL HG1 H 0.83 0.02 2 731 . 117 VAL HG2 H 0.87 0.02 2 732 . 118 GLU N N 127.2 0.1 1 733 . 118 GLU H H 9.07 0.02 1 734 . 118 GLU HA H 4.74 0.02 1 735 . 118 GLU HB2 H 1.85 0.02 2 736 . 118 GLU HB3 H 1.91 0.02 2 737 . 118 GLU HG2 H 2.02 0.02 2 738 . 118 GLU HG3 H 2.18 0.02 2 739 . 119 VAL N N 127.7 0.1 1 740 . 119 VAL H H 8.64 0.02 1 741 . 119 VAL HA H 5.03 0.02 1 742 . 119 VAL HB H 1.94 0.02 1 743 . 119 VAL HG1 H 0.84 0.02 1 744 . 119 VAL HG2 H 0.84 0.02 1 745 . 120 LYS N N 134.4 0.1 1 746 . 120 LYS H H 9.07 0.02 1 747 . 120 LYS HA H 4.61 0.02 1 748 . 120 LYS HB2 H 1.74 0.02 2 749 . 120 LYS HB3 H 1.83 0.02 2 750 . 120 LYS HG2 H 1.36 0.02 2 751 . 120 LYS HG3 H 1.41 0.02 2 752 . 120 LYS HD2 H 1.68 0.02 1 753 . 120 LYS HD3 H 1.68 0.02 1 754 . 120 LYS HE2 H 2.95 0.02 1 755 . 120 LYS HE3 H 2.95 0.02 1 stop_ save_ ######################## # Coupling constants # ######################## save_coupling_constants_set_1 _Saveframe_category coupling_constants _Details 'The HN-HA J couplings of L7 dimer were measured using the HMQC experiment.' loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $sample_cond_1 _Spectrometer_frequency_1H 600 _Mol_system_component_name 'L7 dimer subunit A' _Text_data_format . _Text_data . loop_ _Coupling_constant_ID _Coupling_constant_code _Atom_one_residue_seq_code _Atom_one_residue_label _Atom_one_name _Atom_two_residue_seq_code _Atom_two_residue_label _Atom_two_name _Coupling_constant_value _Coupling_constant_min_value _Coupling_constant_max_value _Coupling_constant_value_error 1 3JHNHA 1 SER H 1 SER HA 9.8 . . 1.0 2 3JHNHA 2 ILE H 2 ILE HA 9.7 . . 1.0 3 3JHNHA 3 THR H 3 THR HA 8.5 . . 2.0 4 3JHNHA 4 LYS H 4 LYS HA 4.5 . . 1.5 5 3JHNHA 5 ASP H 5 ASP HA 3.7 . . 1.5 6 3JHNHA 6 GLN H 6 GLN HA 5.0 . . 2.0 7 3JHNHA 7 ILE H 7 ILE HA 5.0 . . 2.0 8 3JHNHA 8 ILE H 8 ILE HA 4.7 . . 1.0 9 3JHNHA 9 GLU H 9 GLU HA 5.5 . . 2.0 10 3JHNHA 10 ALA H 10 ALA HA 4.5 . . 1.5 11 3JHNHA 11 VAL H 11 VAL HA 8.0 . . 1.5 12 3JHNHA 12 ALA H 12 ALA HA 7.8 . . 1.5 13 3JHNHA 13 ALA H 13 ALA HA 11.0 . . 1.0 14 3JHNHA 14 MET H 14 MET HA 7.6 . . 1.5 15 3JHNHA 15 SER H 15 SER HA 9.0 . . 1.5 16 3JHNHA 16 VAL H 16 VAL HA 5.0 . . 2.0 17 3JHNHA 17 MET H 17 MET HA 3.6 . . 1.0 18 3JHNHA 18 ASP H 18 ASP HA 7.0 . . 1.5 19 3JHNHA 19 VAL H 19 VAL HA 6.1 . . 2.0 20 3JHNHA 20 VAL H 20 VAL HA 6.2 . . 2.0 21 3JHNHA 21 GLU H 21 GLU HA 5.4 . . 1.0 22 3JHNHA 22 LEU H 22 LEU HA 5.0 . . 1.5 23 3JHNHA 23 ILE H 23 ILE HA 6.2 . . 1.5 24 3JHNHA 24 SER H 24 SER HA 6.8 . . 1.5 25 3JHNHA 25 ALA H 25 ALA HA 4.5 . . 1.5 26 3JHNHA 26 MET H 26 MET HA 5.8 . . 1.5 27 3JHNHA 27 GLU H 27 GLU HA 5.7 . . 2.0 28 3JHNHA 28 GLU H 28 GLU HA 5.0 . . 1.5 29 3JHNHA 29 LYS H 29 LYS HA 3.9 . . 1.0 30 3JHNHA 30 PHE H 30 PHE HA 9.5 . . 1.0 31 3JHNHA 31 GLY H 31 GLY HA 6.0 . . 1.5 32 3JHNHA 32 VAL H 32 VAL HA 11.0 . . 1.5 33 3JHNHA 33 SER H 33 SER HA 9.0 . . 1.5 34 3JHNHA 34 ALA H 34 ALA HA 7.8 . . 1.5 35 3JHNHA 35 ALA H 35 ALA HA 7.0 . . 2.0 36 3JHNHA 36 ALA H 36 ALA HA 7.0 . . 2.0 37 3JHNHA 37 ALA H 37 ALA HA 6.8 . . 1.5 38 3JHNHA 38 VAL H 38 VAL HA 8.0 . . 1.5 39 3JHNHA 39 ALA H 39 ALA HA 6.8 . . 2.0 40 3JHNHA 40 VAL H 40 VAL HA 7.2 . . 1.5 41 3JHNHA 41 ALA H 41 ALA HA 8.4 . . 1.0 42 3JHNHA 42 ALA H 42 ALA HA 6.7 . . 1.5 43 3JHNHA 43 GLY H 43 GLY HA 7.0 . . 1.5 44 3JHNHA 45 VAL H 45 VAL HA 11.2 . . 1.5 45 3JHNHA 46 GLU H 46 GLU HA 9.0 . . 1.5 46 3JHNHA 47 ALA H 47 ALA HA 6.8 . . 1.5 47 3JHNHA 48 ALA H 48 ALA HA 6.8 . . 1.5 48 3JHNHA 49 GLU H 49 GLU HA 8.8 . . 1.5 49 3JHNHA 50 GLU H 50 GLU HA 9.4 . . 1.5 50 3JHNHA 51 LYS H 51 LYS HA 8.4 . . 1.5 51 3JHNHA 52 THR H 52 THR HA 11.5 . . 1.0 52 3JHNHA 53 GLU H 53 GLU HA 10.7 . . 1.0 53 3JHNHA 54 PHE H 54 PHE HA 11.4 . . 1.0 54 3JHNHA 55 ASP H 55 ASP HA 11.3 . . 1.0 55 3JHNHA 56 VAL H 56 VAL HA 11.1 . . 1.0 56 3JHNHA 57 ILE H 57 ILE HA 11.0 . . 1.0 57 3JHNHA 58 LEU H 58 LEU HA 9.7 . . 1.0 58 3JHNHA 59 LYS H 59 LYS HA 9.4 . . 1.0 59 3JHNHA 60 ALA H 60 ALA HA 8.1 . . 1.5 60 3JHNHA 61 ALA H 61 ALA HA 6.3 . . 1.5 61 3JHNHA 62 GLY H 62 GLY HA 8.0 . . 1.5 62 3JHNHA 63 ALA H 63 ALA HA 6.2 . . 1.5 63 3JHNHA 64 ASN H 64 ASN HA 11.0 . . 1.0 64 3JHNHA 65 LYS H 65 LYS HA 3.7 . . 1.0 65 3JHNHA 66 VAL H 66 VAL HA 3.5 . . 1.0 66 3JHNHA 67 ALA H 67 ALA HA 5.0 . . 1.5 67 3JHNHA 68 VAL H 68 VAL HA 5.5 . . 1.5 68 3JHNHA 69 ILE H 69 ILE HA 4.2 . . 1.5 69 3JHNHA 70 LYS H 70 LYS HA 3.9 . . 1.0 70 3JHNHA 71 ALA H 71 ALA HA 5.1 . . 1.0 71 3JHNHA 72 VAL H 72 VAL HA 4.6 . . 1.0 72 3JHNHA 73 ARG H 73 ARG HA 3.6 . . 1.0 73 3JHNHA 74 GLY H 74 GLY HA 6.0 . . 1.5 74 3JHNHA 75 ALA H 75 ALA HA 6.8 . . 1.5 75 3JHNHA 76 THR H 76 THR HA 11.3 . . 1.0 76 3JHNHA 77 GLY H 77 GLY HA 7.0 . . 1.5 77 3JHNHA 78 LEU H 78 LEU HA 3.3 . . 1.0 78 3JHNHA 79 GLY H 79 GLY HA 6.0 . . 1.5 79 3JHNHA 80 LEU H 80 LEU HA 3.3 . . 1.5 80 3JHNHA 81 LYS H 81 LYS HA 3.5 . . 1.0 81 3JHNHA 82 GLU H 82 GLU HA 3.4 . . 1.0 82 3JHNHA 83 ALA H 83 ALA HA 5.1 . . 1.5 83 3JHNHA 84 LYS H 84 LYS HA 3.4 . . 1.0 84 3JHNHA 85 ASP H 85 ASP HA 4.2 . . 1.5 85 3JHNHA 86 LEU H 86 LEU HA 4.3 . . 1.5 86 3JHNHA 87 VAL H 87 VAL HA 4.4 . . 1.0 87 3JHNHA 88 GLU H 88 GLU HA 6.3 . . 1.5 88 3JHNHA 89 SER H 89 SER HA 10.4 . . 1.0 89 3JHNHA 90 ALA H 90 ALA HA 3.2 . . 1.0 90 3JHNHA 92 ALA H 92 ALA HA 9.4 . . 1.0 91 3JHNHA 93 ALA H 93 ALA HA 6.4 . . 1.5 92 3JHNHA 94 LEU H 94 LEU HA 10.5 . . 1.0 93 3JHNHA 95 LYS H 95 LYS HA 8.5 . . 1.0 94 3JHNHA 96 GLU H 96 GLU HA 11.3 . . 1.0 95 3JHNHA 97 GLY H 97 GLY HA 6.5 . . 1.5 96 3JHNHA 98 VAL H 98 VAL HA 11.0 . . 1.0 97 3JHNHA 99 SER H 99 SER HA 3.4 . . 1.0 98 3JHNHA 100 LYS H 100 LYS HA 3.5 . . 1.0 99 3JHNHA 101 ASP H 101 ASP HA 3.6 . . 1.0 100 3JHNHA 102 ASP H 102 ASP HA 4.5 . . 1.5 101 3JHNHA 103 ALA H 103 ALA HA 3.3 . . 1.0 102 3JHNHA 104 GLU H 104 GLU HA 5.0 . . 1.0 103 3JHNHA 105 ALA H 105 ALA HA 4.9 . . 1.5 104 3JHNHA 106 LEU H 106 LEU HA 5.3 . . 1.0 105 3JHNHA 107 LYS H 107 LYS HA 3.3 . . 1.0 106 3JHNHA 108 LYS H 108 LYS HA 3.2 . . 1.0 107 3JHNHA 109 ALA H 109 ALA HA 3.0 . . 1.0 108 3JHNHA 110 LEU H 110 LEU HA 5.9 . . 1.5 109 3JHNHA 111 GLU H 111 GLU HA 4.0 . . 1.5 110 3JHNHA 112 GLU H 112 GLU HA 4.4 . . 1.5 111 3JHNHA 113 ALA H 113 ALA HA 9.7 . . 1.0 112 3JHNHA 114 GLY H 114 GLY HA 7.5 . . 1.5 113 3JHNHA 115 ALA H 115 ALA HA 9.1 . . 1.5 114 3JHNHA 116 GLU H 116 GLU HA 11.4 . . 1.0 115 3JHNHA 117 VAL H 117 VAL HA 11.5 . . 1.0 116 3JHNHA 118 GLU H 118 GLU HA 11.4 . . 1.0 117 3JHNHA 119 VAL H 119 VAL HA 11.0 . . 1.0 118 3JHNHA 120 LYS H 120 LYS HA 11.0 . . 1.0 stop_ save_