data_4581 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Site-site Communication in the EF-hand Ca2+ Binding Protein Calbindin D9k ; _BMRB_accession_number 4581 _BMRB_flat_file_name bmr4581.str _Entry_type original _Submission_date 2000-02-02 _Accession_date 2000-02-02 _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 Maler L. . . 2 Blankenship J. . . 3 Rance M. . . 4 Chazin W. J. . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 402 "15N chemical shifts" 70 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2000-12-18 original author . stop_ _Original_release_date 2000-12-18 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title 'Site-site Communication in the EF-hand Ca2+ Binding Protein Calbindin D9k' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code 20165185 _PubMed_ID ? loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Maler L. . . 2 Blankenship J. . . 3 Rance M. . . 4 Chazin W. J. . stop_ _Journal_abbreviation 'Nat. Struct. Biol.' _Journal_name_full 'Nature Structural Biology' _Journal_volume 7 _Journal_issue . _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 245 _Page_last 250 _Year 2000 _Details . loop_ _Keyword EF-hand 'Calcium-binding protein' NMR 'signal transduction' stop_ save_ ####################################### # Cited references within the entry # ####################################### save_ref_1 _Saveframe_category citation _Citation_full ; Wimberly, B.; Thulin, E. and Chazin W.J. Protein Science (1995) 4 1045-1055 ; _Citation_title 'Characterization of the N-terminal half-saturated state of calbindin D9k: NMR studies of the N56A mutant.' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 7549869 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Wimberly B. . . 2 Thulin E. . . 3 Chazin W.J. J. . stop_ _Journal_abbreviation 'Protein Sci.' _Journal_name_full 'Protein science : a publication of the Protein Society' _Journal_volume 4 _Journal_issue 6 _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 1045 _Page_last 1055 _Year 1995 _Details ; Calbindin D9k is a small EF-hand protein that binds two calcium ions with positive cooperativity. The molecular basis of cooperativity for the binding pathway where the first ion binds in the N-terminal site (1) is investigated by NMR experiments on the half-saturated state of the N56A mutant, which exhibits sequential yet cooperative binding (Linse S, Chazin WJ, 1995, Protein Sci 4:1038-1044). Analysis of calcium-induced changes in chemical shifts, amide proton exchange rates, and NOEs indicates that ion binding to the N-terminal binding loop causes significant changes in conformation and/or dynamics throughout the protein. In particular, all three parameters indicate that the hydrophobic core undergoes a change in packing to a conformation very similar to the calcium-loaded state. These results are similar to those observed for the (Cd2+)1 state of the wild-type protein, a model for the complementary half-saturated state with an ion bound in the C-terminal site (II). Thus, with respect to cooperativity in either of the binding pathways, binding of the first ion drives the conformation and dynamics of the protein far toward the (Ca2+)2 state, thereby facilitating binding of the second ion. Comparison with the half-saturated state of the analogous E65Q mutant confirms that mutation of this critical bidentate calcium ligand at position 12 of the consensus EF-hand binding loop causes very significant structural perturbations. This result has important implications regarding numerous studies that have utilized mutation of this critical residue for site deactivation. ; save_ ################################## # Molecular system description # ################################## save_system_N56A _Saveframe_category molecular_system _Mol_system_name 'CALBINDIN D9K' _Abbreviation_common 'calbindin N56A' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'CALBINDIN D9K' $calbindin_N56A 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_calbindin_N56A _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'CALBINDIN D9K' _Name_variant N56A _Abbreviation_common 'calbindin N56A' _Molecular_mass . _Mol_thiol_state 'not present' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 75 _Mol_residue_sequence ; KSPEELKGIFEKYAAKEGDP NQLSKEELKLLLQTEFPSLL KGMSTLDELFEELDKAGDGE VSFEEFQVLVKKISQ ; loop_ _Residue_seq_code _Residue_label 1 LYS 2 SER 3 PRO 4 GLU 5 GLU 6 LEU 7 LYS 8 GLY 9 ILE 10 PHE 11 GLU 12 LYS 13 TYR 14 ALA 15 ALA 16 LYS 17 GLU 18 GLY 19 ASP 20 PRO 21 ASN 22 GLN 23 LEU 24 SER 25 LYS 26 GLU 27 GLU 28 LEU 29 LYS 30 LEU 31 LEU 32 LEU 33 GLN 34 THR 35 GLU 36 PHE 37 PRO 38 SER 39 LEU 40 LEU 41 LYS 42 GLY 43 MET 44 SER 45 THR 46 LEU 47 ASP 48 GLU 49 LEU 50 PHE 51 GLU 52 GLU 53 LEU 54 ASP 55 LYS 56 ALA 57 GLY 58 ASP 59 GLY 60 GLU 61 VAL 62 SER 63 PHE 64 GLU 65 GLU 66 PHE 67 GLN 68 VAL 69 LEU 70 VAL 71 LYS 72 LYS 73 ILE 74 SER 75 GLN stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-02-04 loop_ _Database_name _Database_accession_code _Database_entry_mol_name _Sequence_query_to_submitted_percentage _Sequence_subject_length _Sequence_identity _Sequence_positive _Sequence_homology_expectation_value BMRB 15594 calbindin_in_presence_of_Yb3+ 100.00 75 98.67 98.67 4.14e-41 BMRB 16340 Calbindin_D9K 100.00 76 97.33 97.33 8.27e-40 BMRB 16758 calbindin 100.00 75 98.67 98.67 1.53e-40 BMRB 247 calbindin 100.00 76 97.33 97.33 1.11e-39 BMRB 325 calbindin 100.00 76 97.33 97.33 1.11e-39 BMRB 326 calbindin 100.00 76 97.33 97.33 8.27e-40 BMRB 327 calbindin 100.00 76 97.33 97.33 8.27e-40 PDB 1B1G "Solvated Refinement Of Ca-Loaded Calbindin D9k" 100.00 75 97.33 97.33 1.15e-39 PDB 1CDN "Solution Structure Of (Cd2+)1-Calbindin D9k Reveals Details Of The Stepwise Structural Changes Along The Apo--> (Ca2+) Ii1--> (" 100.00 76 97.33 97.33 8.27e-40 PDB 1CLB "Determination Of The Solution Structure Of Apo Calbindin D9k By Nmr Spectroscopy" 100.00 76 97.33 97.33 8.27e-40 PDB 1D1O "Cooperativity In Ef-Hand Ca2+-Binding Proteins: Evidence Of Site-Site Communication From Binding-Induced Changes In Structure A" 100.00 75 100.00 100.00 5.08e-42 PDB 1HT9 "Domain Swapping Ef-Hands" 100.00 76 97.33 97.33 1.58e-40 PDB 1IG5 "Bovine Calbindin D9k Binding Mg2+" 100.00 75 97.33 97.33 1.12e-39 PDB 1IGV "Bovine Calbindin D9k Binding Mn2+" 100.00 75 97.33 97.33 1.12e-39 PDB 1KCY "Nmr Solution Structure Of Apo Calbindin D9k (F36g + P43m Mutant)" 100.00 75 97.33 97.33 9.17e-40 PDB 1KQV "Family Of Nmr Solution Structures Of Ca Ln Calbindin D9k" 100.00 79 98.67 98.67 2.57e-41 PDB 1KSM "Average Nmr Solution Structure Of Ca Ln Calbindin D9k" 100.00 79 98.67 98.67 2.57e-41 PDB 1N65 "Family Of Nmr Solution Structures Of Ca Ce Calbindin D9k In Denaturating Conditions" 100.00 75 98.67 98.67 4.14e-41 PDB 2BCA "High-Resolution Solution Structure Of Calcium-Loaded Calbindin D9k" 100.00 76 97.33 97.33 8.27e-40 PDB 2BCB "High-Resolution Solution Structure Of Calcium-Loaded Calbindin D9k" 100.00 75 97.33 97.33 1.15e-39 PDB 2MAZ "Backbone 1h, 13c, And 15n Chemical Shift Assignments For Bovine Apo Calbindin" 100.00 75 98.67 98.67 4.14e-41 PDB 3ICB "The Refined Structure Of Vitamin D-Dependent Calcium- Binding Protein From Bovine Intestine. Molecular Details, Ion Binding, An" 100.00 75 97.33 97.33 1.12e-39 PDB 4ICB "Proline Cis-trans Isomers In Calbindin D9k Observed By X-ray Crystallography" 100.00 76 97.33 97.33 1.11e-39 GB AAA30420 "calcium-binding protein [Bos taurus]" 100.00 79 97.33 97.33 7.62e-40 GB AAA72542 "intestinal calcium binding protein (ICaBP), minor A form [synthetic construct]" 100.00 76 97.33 97.33 1.11e-39 GB AAI18481 "S100 calcium binding protein G [Bos taurus]" 100.00 79 97.33 97.33 7.62e-40 PRF 0707237A:PDB=3ICB "protein,Ca binding" 100.00 75 97.33 97.33 1.12e-39 REF NP_776682 "protein S100-G [Bos taurus]" 100.00 79 97.33 97.33 7.62e-40 REF XP_004021986 "PREDICTED: protein S100-G [Ovis aries]" 100.00 79 97.33 97.33 7.62e-40 REF XP_005701114 "PREDICTED: protein S100-G [Capra hircus]" 100.00 79 97.33 97.33 7.62e-40 REF XP_005888771 "PREDICTED: protein S100-G [Bos mutus]" 100.00 79 97.33 97.33 7.62e-40 REF XP_005982038 "PREDICTED: protein S100-G [Pantholops hodgsonii]" 100.00 79 97.33 97.33 7.62e-40 SP P02633 "RecName: Full=Protein S100-G; AltName: Full=Calbindin-D9k; AltName: Full=S100 calcium-binding protein G; AltName: Full=Vitamin " 100.00 79 97.33 97.33 7.62e-40 TPG DAA12577 "TPA: protein S100-G [Bos taurus]" 100.00 79 97.33 97.33 7.62e-40 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $calbindin_N56A Bovine 9913 Eukaryota Metazoa Bos taurus 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 $calbindin_N56A 'recombinant technology' bacteria . . . . 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 $calbindin_N56A 4 mM . stop_ save_ save_sample_2 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $calbindin_N56A 4 mM [U-15N] stop_ save_ ############################ # Computer software used # ############################ save_FELIX _Saveframe_category software _Name FELIX _Version 97.0 loop_ _Task 'resonance assignments, bookkeeping' stop_ _Details 'MSI, SAN DIEGO, CA' save_ save_DIANA _Saveframe_category software _Name DIANA _Version 2.8 loop_ _Task 'structure solution' stop_ _Details 'GUNTERT, BRAUN, BILLETER, WUTHRICH' save_ save_AMBER _Saveframe_category software _Name AMBER _Version 4.1 loop_ _Task refinement stop_ _Details 'PEARLMAN, CASE, CALDWELL, ROSS, CHEATHAM, FERGUSON, SEIBEL, SINGH, WEINER, KOLLMAN' save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer1 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model AMX _Field_strength 500 _Details . save_ save_NMR_spectrometer2 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model DRX _Field_strength 600 _Details . save_ save_NMR_spectrometer3 _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model Inova _Field_strength 600 _Details . save_ ############################# # NMR applied experiments # ############################# save_2D_NOESY_1 _Saveframe_category NMR_applied_experiment _Experiment_name '2D NOESY' _Sample_label . save_ save_3D_15N-SEPARATED_NOESY_2 _Saveframe_category NMR_applied_experiment _Experiment_name '3D 15N-SEPARATED NOESY' _Sample_label . save_ save_HSQC-J_3 _Saveframe_category NMR_applied_experiment _Experiment_name HSQC-J _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-SEPARATED NOESY' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_3 _Saveframe_category NMR_applied_experiment _Experiment_name HSQC-J _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 0.2 n/a temperature 300 1 K 'ionic strength' 0 . mM pressure 1 . atm stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference _Saveframe_category chemical_shift_reference _Details . loop_ _Mol_common_name _Atom_type _Atom_isotope_number _Atom_group _Chem_shift_units _Chem_shift_value _Reference_method _Reference_type _External_reference_sample_geometry _External_reference_location _External_reference_axis _Indirect_shift_ratio 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_ _Sample_label $sample_1 $sample_2 stop_ _Sample_conditions_label $sample_cond_1 _Chem_shift_reference_set_label $chemical_shift_reference _Mol_system_component_name 'CALBINDIN D9K' _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 LYS H H 7.94 0.01 1 2 . 1 LYS HA H 4.64 0.01 1 3 . 1 LYS HB2 H 1.80 0.01 2 4 . 1 LYS HB3 H 2.00 0.01 2 5 . 1 LYS HG2 H 1.50 0.01 2 6 . 1 LYS HG3 H 1.59 0.01 2 7 . 1 LYS HD2 H 1.71 0.01 2 8 . 1 LYS HE2 H 2.92 0.01 2 9 . 1 LYS N N 124.8 0.1 1 10 . 2 SER H H 9.02 0.01 1 11 . 2 SER HA H 4.70 0.01 1 12 . 2 SER HB2 H 4.09 0.01 2 13 . 2 SER HB3 H 4.39 0.01 2 14 . 2 SER N N 119.3 0.1 1 15 . 3 PRO HA H 4.32 0.01 1 16 . 3 PRO HB2 H 2.01 0.01 2 17 . 3 PRO HB3 H 2.48 0.01 2 18 . 3 PRO HG2 H 2.20 0.01 2 19 . 3 PRO HD2 H 3.73 0.01 2 20 . 4 GLU H H 8.79 0.01 1 21 . 4 GLU HA H 4.035 0.01 1 22 . 4 GLU HB2 H 1.97 0.01 2 23 . 4 GLU HB3 H 2.05 0.01 2 24 . 4 GLU HG2 H 2.255 0.01 2 25 . 4 GLU HG3 H 2.44 0.01 2 26 . 4 GLU N N 117.4 0.1 1 27 . 5 GLU H H 8.04 0.01 1 28 . 5 GLU HA H 4.14 0.01 1 29 . 5 GLU HB2 H 2.05 0.01 2 30 . 5 GLU HB3 H 2.26 0.01 2 31 . 5 GLU HG2 H 2.41 0.01 1 32 . 5 GLU HG3 H 2.41 0.01 1 33 . 5 GLU N N 122.4 0.1 1 34 . 6 LEU H H 8.60 0.01 1 35 . 6 LEU HA H 4.29 0.01 1 36 . 6 LEU HB2 H 1.80 0.01 2 37 . 6 LEU HB3 H 2.20 0.01 2 38 . 6 LEU HG H 1.90 0.01 1 39 . 6 LEU HD1 H 0.93 0.01 2 40 . 6 LEU HD2 H 0.98 0.01 2 41 . 6 LEU N N 120.1 0.1 1 42 . 7 LYS H H 8.39 0.01 1 43 . 7 LYS HA H 3.98 0.01 1 44 . 7 LYS HB2 H 1.645 0.01 2 45 . 7 LYS HB3 H 1.85 0.01 2 46 . 7 LYS HG2 H 0.83 0.01 1 47 . 7 LYS HG3 H 0.83 0.01 1 48 . 7 LYS HD2 H 1.23 0.01 2 49 . 7 LYS N N 121.7 0.1 1 50 . 8 GLY H H 7.855 0.01 1 51 . 8 GLY HA2 H 3.925 0.01 1 52 . 8 GLY HA3 H 3.925 0.01 1 53 . 8 GLY N N 105.6 0.1 1 54 . 9 ILE H H 7.96 0.01 1 55 . 9 ILE HA H 3.915 0.01 1 56 . 9 ILE HB H 2.19 0.01 1 57 . 9 ILE HG12 H 1.83 0.01 2 58 . 9 ILE HG2 H 1.19 0.01 1 59 . 9 ILE HD1 H 0.98 0.01 1 60 . 9 ILE N N 122.2 0.1 1 61 . 10 PHE H H 8.65 0.01 1 62 . 10 PHE HA H 3.535 0.01 1 63 . 10 PHE HB2 H 2.86 0.01 2 64 . 10 PHE HB3 H 3.36 0.01 2 65 . 10 PHE HD1 H 6.52 0.01 3 66 . 10 PHE HE1 H 7.13 0.01 3 67 . 10 PHE HZ H 7.46 0.01 1 68 . 10 PHE N N 120.1 0.1 1 69 . 11 GLU H H 8.60 0.01 1 70 . 11 GLU HA H 3.78 0.01 1 71 . 11 GLU HB2 H 1.95 0.01 2 72 . 11 GLU HB3 H 2.10 0.01 2 73 . 11 GLU HG2 H 2.34 0.01 2 74 . 11 GLU HG3 H 2.66 0.01 2 75 . 11 GLU N N 115.5 0.1 1 76 . 12 LYS H H 7.62 0.01 1 77 . 12 LYS HA H 3.84 0.01 1 78 . 12 LYS HB2 H 1.77 0.01 2 79 . 12 LYS HB3 H 1.85 0.01 2 80 . 12 LYS HG2 H 0.58 0.01 2 81 . 12 LYS HG3 H 1.14 0.01 2 82 . 12 LYS HD2 H 1.47 0.01 2 83 . 12 LYS N N 118.9 0.1 1 84 . 13 TYR H H 7.27 0.01 1 85 . 13 TYR HA H 4.03 0.01 1 86 . 13 TYR HB2 H 2.41 0.01 2 87 . 13 TYR HB3 H 2.815 0.01 2 88 . 13 TYR HD1 H 6.73 0.01 3 89 . 13 TYR HE1 H 7.44 0.01 3 90 . 13 TYR N N 115.1 0.1 1 91 . 14 ALA H H 8.37 0.01 1 92 . 14 ALA HA H 3.88 0.01 1 93 . 14 ALA HB H 0.425 0.01 1 94 . 14 ALA N N 119.5 0.1 1 95 . 15 ALA H H 6.935 0.01 1 96 . 15 ALA HA H 4.29 0.01 1 97 . 15 ALA HB H 1.39 0.01 1 98 . 15 ALA N N 117.2 0.1 1 99 . 16 LYS H H 7.225 0.01 1 100 . 16 LYS HA H 3.83 0.01 1 101 . 16 LYS HB2 H 1.95 0.01 2 102 . 16 LYS HB3 H 2.10 0.01 2 103 . 16 LYS HG2 H 1.49 0.01 2 104 . 16 LYS HD2 H 1.69 0.01 2 105 . 16 LYS HD3 H 1.82 0.01 2 106 . 16 LYS HE2 H 2.76 0.01 2 107 . 16 LYS N N 120.3 0.1 1 108 . 17 GLU H H 9.69 0.01 1 109 . 17 GLU HA H 4.70 0.01 1 110 . 17 GLU HB2 H 1.87 0.01 2 111 . 17 GLU HB3 H 1.95 0.01 2 112 . 17 GLU HG2 H 2.09 0.01 2 113 . 17 GLU HG3 H 2.15 0.01 2 114 . 17 GLU N N 116.4 0.1 1 115 . 18 GLY H H 8.98 0.01 1 116 . 18 GLY HA2 H 3.68 0.01 2 117 . 18 GLY HA3 H 3.94 0.01 2 118 . 18 GLY N N 113.2 0.1 1 119 . 19 ASP H H 8.25 0.01 1 120 . 19 ASP HA H 4.45 0.01 1 121 . 19 ASP HB2 H 2.48 0.01 2 122 . 19 ASP HB3 H 2.71 0.01 2 123 . 19 ASP N N 126.0 0.1 1 124 . 20 PRO HA H 4.85 0.01 1 125 . 20 PRO HB2 H 2.03 0.01 2 126 . 20 PRO HB3 H 2.20 0.01 2 127 . 20 PRO HG2 H 1.87 0.01 2 128 . 20 PRO HG3 H 2.06 0.01 2 129 . 20 PRO HD2 H 3.98 0.01 2 130 . 21 ASN H H 9.15 0.01 1 131 . 21 ASN HA H 4.99 0.01 1 132 . 21 ASN HB2 H 2.66 0.01 2 133 . 21 ASN HB3 H 3.02 0.01 2 134 . 21 ASN N N 115.9 0.1 1 135 . 22 GLN H H 7.27 0.01 1 136 . 22 GLN HA H 5.00 0.01 1 137 . 22 GLN HB2 H 1.68 0.01 2 138 . 22 GLN HB3 H 1.97 0.01 2 139 . 22 GLN HG2 H 2.02 0.01 2 140 . 22 GLN HG3 H 2.27 0.01 2 141 . 22 GLN N N 114.9 0.1 1 142 . 23 LEU H H 9.77 0.01 1 143 . 23 LEU HA H 5.36 0.01 1 144 . 23 LEU HB2 H 1.70 0.01 2 145 . 23 LEU HB3 H 1.83 0.01 2 146 . 23 LEU HG H 1.34 0.01 1 147 . 23 LEU HD1 H 0.42 0.01 1 148 . 23 LEU HD2 H 0.58 0.01 1 149 . 23 LEU N N 127.5 0.1 1 150 . 24 SER H H 10.21 0.01 1 151 . 24 SER HA H 4.95 0.01 1 152 . 24 SER HB2 H 4.08 0.01 2 153 . 24 SER HB3 H 4.39 0.01 2 154 . 24 SER N N 122.7 0.1 1 155 . 25 LYS H H 8.695 0.01 1 156 . 25 LYS HA H 3.50 0.01 1 157 . 25 LYS HB2 H 1.80 0.01 2 158 . 25 LYS N N 119.9 0.1 1 159 . 26 GLU H H 8.12 0.01 1 160 . 26 GLU HA H 3.925 0.01 1 161 . 26 GLU HB2 H 1.93 0.01 2 162 . 26 GLU HG2 H 2.22 0.01 2 163 . 26 GLU HG3 H 2.31 0.01 2 164 . 26 GLU N N 117.4 0.1 1 165 . 27 GLU H H 7.83 0.01 1 166 . 27 GLU HA H 3.925 0.01 1 167 . 27 GLU HB2 H 1.90 0.01 2 168 . 27 GLU HB3 H 2.54 0.01 2 169 . 27 GLU HG2 H 2.36 0.01 2 170 . 27 GLU HG3 H 2.54 0.01 2 171 . 27 GLU N N 120.8 0.1 1 172 . 28 LEU H H 8.77 0.01 1 173 . 28 LEU HA H 3.98 0.01 1 174 . 28 LEU HB2 H 1.54 0.01 2 175 . 28 LEU HB3 H 2.23 0.01 2 176 . 28 LEU HG H 1.68 0.01 1 177 . 28 LEU HD1 H 1.085 0.01 1 178 . 28 LEU HD2 H 1.085 0.01 1 179 . 28 LEU N N 119.3 0.1 1 180 . 29 LYS H H 8.42 0.01 1 181 . 29 LYS HA H 3.665 0.01 1 182 . 29 LYS HB2 H 1.84 0.01 2 183 . 29 LYS HB3 H 1.95 0.01 2 184 . 29 LYS HG2 H 1.39 0.01 2 185 . 29 LYS HD2 H 1.64 0.01 2 186 . 29 LYS HE2 H 2.96 0.01 1 187 . 29 LYS HE3 H 2.96 0.01 1 188 . 29 LYS N N 119.9 0.1 1 189 . 30 LEU H H 7.56 0.01 1 190 . 30 LEU HA H 4.035 0.01 1 191 . 30 LEU HB2 H 1.80 0.01 2 192 . 30 LEU HD1 H 1.01 0.01 1 193 . 30 LEU HD2 H 1.01 0.01 1 194 . 30 LEU N N 118.7 0.1 1 195 . 31 LEU H H 8.15 0.01 1 196 . 31 LEU HA H 2.31 0.01 1 197 . 31 LEU HB2 H 1.19 0.01 2 198 . 31 LEU HB3 H 1.75 0.01 2 199 . 31 LEU HD1 H 0.93 0.01 2 200 . 31 LEU HD2 H 0.98 0.01 2 201 . 31 LEU N N 124.35 0.1 1 202 . 32 LEU H H 8.875 0.01 1 203 . 32 LEU HA H 3.88 0.01 1 204 . 32 LEU HB2 H 1.34 0.01 2 205 . 32 LEU HB3 H 1.97 0.01 2 206 . 32 LEU HG H 2.15 0.01 1 207 . 32 LEU HD1 H 0.93 0.01 1 208 . 32 LEU HD2 H 1.14 0.01 1 209 . 32 LEU N N 120.35 0.1 1 210 . 33 GLN H H 8.44 0.01 1 211 . 33 GLN HA H 3.88 0.01 2 212 . 33 GLN HB2 H 1.95 0.01 2 213 . 33 GLN HB3 H 2.15 0.01 2 214 . 33 GLN HG2 H 2.36 0.01 2 215 . 33 GLN HG3 H 2.51 0.01 2 216 . 33 GLN N N 114.5 0.1 1 217 . 34 THR H H 7.67 0.01 1 218 . 34 THR HA H 4.035 0.01 1 219 . 34 THR HB H 4.19 0.01 1 220 . 34 THR HG2 H 1.235 0.01 1 221 . 34 THR N N 111.5 0.1 1 222 . 35 GLU H H 8.56 0.01 1 223 . 35 GLU HA H 4.19 0.01 1 224 . 35 GLU HB2 H 1.43 0.01 2 225 . 35 GLU HB3 H 1.495 0.01 2 226 . 35 GLU HG2 H 2.36 0.01 2 227 . 35 GLU N N 116.4 0.1 1 228 . 36 PHE H H 7.87 0.01 1 229 . 36 PHE HA H 5.15 0.01 1 230 . 36 PHE HB2 H 2.815 0.01 2 231 . 36 PHE HB3 H 3.32 0.01 2 232 . 36 PHE HD1 H 7.13 0.01 3 233 . 36 PHE HE1 H 7.18 0.01 3 234 . 36 PHE HZ H 7.02 0.01 1 235 . 36 PHE N N 115.7 0.1 1 236 . 37 PRO HA H 4.24 0.01 1 237 . 37 PRO HB2 H 2.44 0.01 2 238 . 38 SER H H 8.375 0.01 1 239 . 38 SER HA H 4.24 0.01 1 240 . 38 SER HB2 H 3.93 0.01 2 241 . 38 SER HB3 H 4.00 0.01 2 242 . 38 SER N N 113.4 0.1 1 243 . 39 LEU H H 7.94 0.01 1 244 . 39 LEU HA H 4.13 0.01 1 245 . 39 LEU HB2 H 1.78 0.01 2 246 . 39 LEU HB3 H 1.90 0.01 2 247 . 39 LEU HG H 1.44 0.01 1 248 . 39 LEU HD1 H 0.73 0.01 1 249 . 39 LEU HD2 H 0.73 0.01 1 250 . 39 LEU N N 123.1 0.1 1 251 . 40 LEU H H 7.69 0.01 1 252 . 40 LEU HA H 4.295 0.01 1 253 . 40 LEU HB2 H 1.75 0.01 2 254 . 40 LEU HB3 H 1.90 0.01 2 255 . 40 LEU HG H 1.44 0.01 1 256 . 40 LEU HD1 H 0.81 0.01 1 257 . 40 LEU HD2 H 0.90 0.01 1 258 . 40 LEU N N 120.2 0.1 1 259 . 41 LYS H H 7.46 0.01 1 260 . 41 LYS HA H 4.36 0.01 1 261 . 41 LYS HB2 H 1.80 0.01 2 262 . 41 LYS HB3 H 1.98 0.01 2 263 . 41 LYS HG2 H 1.38 0.01 2 264 . 41 LYS HG3 H 1.45 0.01 2 265 . 41 LYS HE2 H 3.01 0.01 1 266 . 41 LYS HE3 H 3.01 0.01 1 267 . 41 LYS N N 119.9 0.1 1 268 . 42 GLY H H 8.07 0.01 1 269 . 42 GLY HA2 H 3.93 0.01 2 270 . 42 GLY HA3 H 4.18 0.01 2 271 . 42 GLY N N 108.6 0.1 1 272 . 43 MET H H 8.00 0.01 1 273 . 43 MET HA H 4.68 0.01 1 274 . 43 MET HB2 H 2.09 0.01 2 275 . 43 MET HG2 H 2.58 0.01 2 276 . 43 MET HG3 H 2.63 0.01 2 277 . 44 SER H H 8.40 0.01 1 278 . 44 SER HA H 4.56 0.01 1 279 . 44 SER HB2 H 3.88 0.01 1 280 . 44 SER HB3 H 3.88 0.01 1 281 . 44 SER N N 115.9 0.1 1 282 . 45 THR H H 7.96 0.01 1 283 . 45 THR HA H 4.39 0.01 1 284 . 45 THR HB H 4.54 0.01 1 285 . 45 THR HG2 H 1.29 0.01 1 286 . 45 THR N N 114.0 0.1 1 287 . 46 LEU H H 8.08 0.01 1 288 . 46 LEU HA H 4.14 0.01 1 289 . 46 LEU HB2 H 1.79 0.01 2 290 . 46 LEU HG H 1.95 0.01 1 291 . 46 LEU HD1 H 0.97 0.01 1 292 . 46 LEU HD2 H 0.97 0.01 1 293 . 46 LEU N N 122.0 0.1 1 294 . 47 ASP H H 8.21 0.01 1 295 . 47 ASP HA H 4.035 0.01 1 296 . 47 ASP HB2 H 2.48 0.01 2 297 . 47 ASP HB3 H 2.71 0.01 2 298 . 47 ASP N N 114.5 0.1 1 299 . 48 GLU H H 7.895 0.01 1 300 . 48 GLU HA H 4.035 0.01 1 301 . 48 GLU HB2 H 2.15 0.01 2 302 . 48 GLU HG2 H 2.31 0.01 2 303 . 48 GLU N N 119.5 0.1 1 304 . 49 LEU H H 8.08 0.01 1 305 . 49 LEU HA H 4.23 0.01 1 306 . 49 LEU HB2 H 1.55 0.01 2 307 . 49 LEU HB3 H 1.65 0.01 2 308 . 49 LEU HG H 1.63 0.01 1 309 . 49 LEU HD1 H 0.72 0.01 2 310 . 49 LEU HD2 H 0.78 0.01 2 311 . 49 LEU N N 121.0 0.01 1 312 . 50 PHE H H 8.65 0.01 1 313 . 50 PHE HA H 3.83 0.01 1 314 . 50 PHE HB2 H 3.07 0.01 2 315 . 50 PHE HB3 H 3.17 0.01 2 316 . 50 PHE HD1 H 7.14 0.01 3 317 . 50 PHE HE1 H 7.14 0.01 3 318 . 50 PHE HZ H 7.14 0.01 1 319 . 50 PHE N N 118.9 0.1 1 320 . 51 GLU H H 7.92 0.01 1 321 . 51 GLU HA H 4.035 0.01 2 322 . 51 GLU HB2 H 2.10 0.01 2 323 . 51 GLU HG2 H 2.31 0.01 2 324 . 51 GLU HG3 H 2.46 0.01 2 325 . 51 GLU N N 117.2 0.1 1 326 . 52 GLU H H 7.71 0.01 1 327 . 52 GLU HA H 3.98 0.01 1 328 . 52 GLU HB2 H 2.10 0.01 2 329 . 52 GLU HG2 H 2.05 0.01 2 330 . 52 GLU HG3 H 2.31 0.01 2 331 . 52 GLU N N 118.5 0.1 1 332 . 53 LEU H H 7.67 0.01 1 333 . 53 LEU HA H 4.14 0.01 1 334 . 53 LEU HB2 H 1.295 0.01 2 335 . 53 LEU HB3 H 1.65 0.01 2 336 . 53 LEU HG H 1.92 0.01 1 337 . 53 LEU HD1 H 0.80 0.01 1 338 . 53 LEU HD2 H 0.73 0.01 1 339 . 53 LEU N N 117.3 0.1 1 340 . 54 ASP H H 8.10 0.01 1 341 . 54 ASP HA H 4.445 0.01 1 342 . 54 ASP HB2 H 2.56 0.01 2 343 . 54 ASP HB3 H 2.67 0.01 2 344 . 54 ASP N N 119.5 0.1 1 345 . 55 LYS H H 8.145 0.01 1 346 . 55 LYS HA H 4.14 0.01 1 347 . 55 LYS HB2 H 1.64 0.01 2 348 . 55 LYS HG2 H 1.79 0.01 2 349 . 55 LYS HE2 H 3.06 0.01 2 350 . 55 LYS N N 121.2 0.1 1 351 . 56 ALA H H 8.04 0.01 1 352 . 56 ALA HA H 4.24 0.01 1 353 . 56 ALA HB H 1.49 0.01 1 354 . 56 ALA N N 119.7 0.1 1 355 . 57 GLY H H 8.00 0.01 1 356 . 57 GLY HA2 H 3.88 0.01 1 357 . 57 GLY HA3 H 3.88 0.01 1 358 . 57 GLY N N 107.5 0.1 1 359 . 58 ASP H H 8.52 0.01 1 360 . 58 ASP HA H 4.70 0.01 1 361 . 58 ASP HB2 H 2.61 0.01 2 362 . 58 ASP HB3 H 2.92 0.01 2 363 . 58 ASP N N 119.3 0.1 1 364 . 59 GLY H H 8.71 0.01 1 365 . 59 GLY HA2 H 3.75 0.01 2 366 . 59 GLY HA3 H 4.14 0.01 2 367 . 59 GLY N N 112.4 0.1 1 368 . 60 GLU H H 7.83 0.01 1 369 . 60 GLU HA H 5.05 0.01 1 370 . 60 GLU HB2 H 1.645 0.01 2 371 . 60 GLU HB3 H 1.95 0.01 2 372 . 60 GLU HG2 H 2.15 0.01 2 373 . 60 GLU N N 118.2 0.1 1 374 . 61 VAL H H 9.55 0.01 1 375 . 61 VAL HA H 5.05 0.01 1 376 . 61 VAL HB H 2.36 0.01 1 377 . 61 VAL HG1 H 0.57 0.01 2 378 . 61 VAL HG2 H 1.04 0.01 2 379 . 61 VAL N N 121.4 0.1 1 380 . 62 SER H H 9.33 0.01 1 381 . 62 SER HA H 4.86 0.01 1 382 . 62 SER HB2 H 4.18 0.01 2 383 . 62 SER HB3 H 4.49 0.01 2 384 . 62 SER N N 123.7 0.1 1 385 . 63 PHE H H 9.38 0.01 1 386 . 63 PHE HA H 3.37 0.01 1 387 . 63 PHE HB2 H 2.255 0.01 2 388 . 63 PHE HB3 H 2.56 0.01 2 389 . 63 PHE HD1 H 6.67 0.01 3 390 . 63 PHE HE1 H 7.13 0.01 3 391 . 63 PHE HZ H 7.34 0.01 1 392 . 63 PHE N N 122.7 0.1 1 393 . 64 GLU H H 8.60 0.01 1 394 . 64 GLU HA H 3.73 0.01 1 395 . 64 GLU HB2 H 1.85 0.01 2 396 . 64 GLU HB3 H 2.00 0.01 2 397 . 64 GLU HG2 H 2.255 0.01 2 398 . 64 GLU N N 118.7 0.1 1 399 . 65 GLU H H 7.69 0.01 1 400 . 65 GLU HA H 3.98 0.01 1 401 . 65 GLU HB2 H 1.85 0.01 2 402 . 65 GLU HG2 H 2.08 0.01 2 403 . 65 GLU HG3 H 2.41 0.01 2 404 . 65 GLU N N 120.1 0.1 1 405 . 66 PHE H H 8.85 0.01 1 406 . 66 PHE HA H 4.035 0.01 1 407 . 66 PHE HB2 H 3.17 0.01 2 408 . 66 PHE HB3 H 3.27 0.01 2 409 . 66 PHE HD1 H 7.03 0.01 3 410 . 66 PHE HE1 H 7.12 0.01 3 411 . 66 PHE HZ H 7.35 0.01 1 412 . 66 PHE N N 120.8 0.1 1 413 . 67 GLN H H 7.87 0.01 1 414 . 67 GLN HA H 3.22 0.01 1 415 . 67 GLN HB2 H 1.70 0.01 2 416 . 67 GLN HB3 H 1.95 0.01 2 417 . 67 GLN HG2 H 2.10 0.01 2 418 . 67 GLN HG3 H 2.30 0.01 2 419 . 67 GLN N N 117.4 0.1 1 420 . 68 VAL H H 7.10 0.01 1 421 . 68 VAL HA H 3.49 0.01 1 422 . 68 VAL HB H 2.10 0.01 1 423 . 68 VAL HG1 H 0.98 0.01 1 424 . 68 VAL HG2 H 0.84 0.01 1 425 . 68 VAL N N 118.7 0.1 1 426 . 69 LEU H H 7.13 0.01 1 427 . 69 LEU HA H 3.73 0.01 1 428 . 69 LEU HB2 H 1.20 0.01 2 429 . 69 LEU HB3 H 1.34 0.01 2 430 . 69 LEU HG H 1.38 0.01 1 431 . 69 LEU HD1 H 0.80 0.01 2 432 . 69 LEU HD2 H 0.70 0.01 2 433 . 69 LEU N N 120.5 0.1 1 434 . 70 VAL H H 7.64 0.01 1 435 . 70 VAL HA H 3.12 0.01 1 436 . 70 VAL HB H 1.85 0.01 1 437 . 70 VAL HG1 H 0.51 0.01 1 438 . 70 VAL HG2 H 0.68 0.01 1 439 . 70 VAL N N 116.3 0.1 1 440 . 71 LYS H H 7.44 0.01 1 441 . 71 LYS HA H 3.93 0.01 1 442 . 71 LYS HB2 H 1.75 0.01 2 443 . 71 LYS HB3 H 1.80 0.01 2 444 . 71 LYS HG2 H 1.44 0.01 2 445 . 71 LYS HD2 H 1.59 0.01 2 446 . 71 LYS HE2 H 2.91 0.01 2 447 . 71 LYS N N 119.5 0.1 1 448 . 72 LYS H H 7.51 0.01 1 449 . 72 LYS HA H 4.15 0.01 1 450 . 72 LYS HB2 H 1.85 0.01 2 451 . 72 LYS HG2 H 1.49 0.01 2 452 . 72 LYS HD2 H 1.46 0.01 2 453 . 72 LYS HE2 H 2.72 0.01 2 454 . 73 ILE H H 7.54 0.01 1 455 . 73 ILE HA H 4.18 0.01 1 456 . 73 ILE HB H 1.85 0.01 1 457 . 73 ILE HG12 H 0.92 0.01 2 458 . 73 ILE HG13 H 1.23 0.01 2 459 . 73 ILE HG2 H 0.64 0.01 1 460 . 73 ILE HD1 H 0.30 0.01 1 461 . 73 ILE N N 113.0 0.1 1 462 . 74 SER H H 7.64 0.01 1 463 . 74 SER HA H 4.44 0.01 1 464 . 74 SER HB2 H 4.13 0.01 2 465 . 74 SER HB3 H 4.83 0.01 2 466 . 74 SER N N 117.0 0.1 1 467 . 75 GLN H H 7.60 0.01 1 468 . 75 GLN HA H 4.14 0.01 1 469 . 75 GLN HB2 H 1.93 0.01 2 470 . 75 GLN HB3 H 2.10 0.01 2 471 . 75 GLN HG2 H 2.31 0.01 2 472 . 75 GLN N N 126.4 0.1 1 stop_ save_