data_5318 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Backbone and Sidechain 1H, 13C and 15N resonance assignments for PLC-gamma 1 C-terminal SH2 domain ; _BMRB_accession_number 5318 _BMRB_flat_file_name bmr5318.str _Entry_type original _Submission_date 2002-03-13 _Accession_date 2002-03-13 _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 Forman-Kay Julie D . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 98 "15N chemical shifts" 98 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2002-05-01 original author . stop_ loop_ _Related_BMRB_accession_number _Relationship 5310 'Protein in complex form with a PDGFR-derived phosphopeptide.' stop_ _Original_release_date 2002-05-01 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; Nuclear magnetic resonance structure of an SH2 domain of phospholipase C-gamma 1 complexed with a high affinity binding peptide ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 8181064 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Pascal Steve M. . 2 Gish Gerry . . 3 Yamazaki Toshio . . 4 Singer Alex U. . 5 Shoelson Steven E. . 6 Pawson Tony . . 7 Kay Lewis E. . 8 Forman-Kay Julie D. . stop_ _Journal_abbreviation Cell _Journal_volume 77 _Journal_issue 3 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 461 _Page_last 472 _Year 1994 _Details . save_ ####################################### # Cited references within the entry # ####################################### save_ref_1 _Saveframe_category citation _Citation_full ; Stahl ML, Ferenz CR, Kelleher KL, Kriz RW, Knopf JL. Sequence similarity of phospholipase C with the non-catalytic region of src. Nature. 1988 Mar 17;332(6161):269-72. ; _Citation_title . _Citation_status . _Citation_type . _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 88156963 _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 ; Piccione E, Case RD, Domchek SM, Hu P, Chaudhuri M, Backer JM, Schlessinger J, Shoelson SE. Phosphatidylinositol 3-kinase p85 SH2 domain specificity defined by direct phosphopeptide/SH2 domain binding. Biochemistry. 1993 Apr 6;32(13):3197-202. ; _Citation_title . _Citation_status . _Citation_type . _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 93213786 _Journal_abbreviation . _Journal_name_full . _Journal_volume . _Journal_issue . _Journal_CSD . _Book_title . _Book_chapter_title . _Book_volume . _Book_series . _Book_publisher . _Book_publisher_city . _Book_ISBN . _Conference_title . _Conference_site . _Conference_state_province . _Conference_country . _Conference_start_date . _Conference_end_date . _Conference_abstract_number . _Thesis_institution . _Thesis_institution_city . _Thesis_institution_country . _Page_first . _Page_last . _Year . _Details . save_ save_ref_3 _Saveframe_category citation _Citation_full ; Brunger, A.T. (1992) X-PLOR Version 3.1: A System for X-Ray Crystallography and NMR (New Haven, Connecticut: Yale University Press). ; _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 ; Miguel Giacchella R. [The history of the discovery of anesthesia. Progress is the attainment of utopia] Rev Soc Odontol La Plata. 1988 Apr;1(1):29-30. ; _Citation_title . _Citation_status . _Citation_type . _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 90212257 _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_PLCC_SH2 _Saveframe_category molecular_system _Mol_system_name 'phospholipase C gamma-1 C-terminal SH2 domain' _Abbreviation_common 'PLCC SH2' _Enzyme_commission_number 3.1.4.3 loop_ _Mol_system_component_name _Mol_label 'PLCC SH2 domain' $PLCC_SH2 stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state complex _System_paramagnetic no _System_thiol_state 'all free' loop_ _Biological_function 'Binds cell surface receptors and participates in intracellular signalling.' stop_ _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_PLCC_SH2 _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'PLCC SH2' _Abbreviation_common 'PLCC SH2' _Molecular_mass . _Mol_thiol_state 'all free' _Details ; Residues 663 to 759 of PLC gamma-1, with five add'l N-term and three add'l C-term residues. ; ############################## # Polymer residue sequence # ############################## _Residue_count 105 _Mol_residue_sequence ; GSPGIHESKEWYHASLTRAQ AEHMLMRVPRDGAFLVRKRN EPNSYAISFRAEGKIKHCRV QQEGQTVMLGNSEFDSLVDL ISYYEKHPLYRKMKLRYPIN EENSS ; loop_ _Residue_seq_code _Residue_label 1 GLY 2 SER 3 PRO 4 GLY 5 ILE 6 HIS 7 GLU 8 SER 9 LYS 10 GLU 11 TRP 12 TYR 13 HIS 14 ALA 15 SER 16 LEU 17 THR 18 ARG 19 ALA 20 GLN 21 ALA 22 GLU 23 HIS 24 MET 25 LEU 26 MET 27 ARG 28 VAL 29 PRO 30 ARG 31 ASP 32 GLY 33 ALA 34 PHE 35 LEU 36 VAL 37 ARG 38 LYS 39 ARG 40 ASN 41 GLU 42 PRO 43 ASN 44 SER 45 TYR 46 ALA 47 ILE 48 SER 49 PHE 50 ARG 51 ALA 52 GLU 53 GLY 54 LYS 55 ILE 56 LYS 57 HIS 58 CYS 59 ARG 60 VAL 61 GLN 62 GLN 63 GLU 64 GLY 65 GLN 66 THR 67 VAL 68 MET 69 LEU 70 GLY 71 ASN 72 SER 73 GLU 74 PHE 75 ASP 76 SER 77 LEU 78 VAL 79 ASP 80 LEU 81 ILE 82 SER 83 TYR 84 TYR 85 GLU 86 LYS 87 HIS 88 PRO 89 LEU 90 TYR 91 ARG 92 LYS 93 MET 94 LYS 95 LEU 96 ARG 97 TYR 98 PRO 99 ILE 100 ASN 101 GLU 102 GLU 103 ASN 104 SER 105 SER stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-01-28 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 2FCI "Structural Basis For The Requirement Of Two Phosphotyrosines In Signaling Mediated By Syk Tyrosine Kinase" 100.00 105 100.00 100.00 5.26e-72 PDB 2PLD "Nuclear Magnetic Resonance Structure Of An Sh2 Domain Of Phospholipase C-gamma1 Complexed With A High Affinity Binding Peptide" 100.00 105 100.00 100.00 5.26e-72 PDB 2PLE "Nuclear Magnetic Resonance Structure Of An Sh2 Domain Of Phospholipase C-Gamma1 Complexed With A High Affinity Binding Peptide" 100.00 105 100.00 100.00 5.26e-72 PDB 4K44 "Auto-inhibition And Phosphorylation-induced Activation Of Plc-gamma Isozymes" 91.43 106 100.00 100.00 5.46e-65 PDB 4K45 "Auto-inhibition And Phosphorylation-induced Activation Of Plc-gamma Isozymes" 91.43 106 100.00 100.00 5.46e-65 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $PLCC_SH2 Cow 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 _Details $PLCC_SH2 'recombinant technology' 'E. coli' Escherichia coli BL21 . '50 mg protein/L of E.coli culture.' 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 $PLCC_SH2 1.5 mM '[U-99% 15N]' 'sodium phosphate' 100 mM . stop_ save_ ############################ # Computer software used # ############################ save_X-PLOR _Saveframe_category software _Name X-PLOR _Version . loop_ _Task 'combined distance geometry-simulated annealing calculations' stop_ _Details . _Citation_label $ref_3 save_ save_STEREOSEARCH _Saveframe_category software _Name STEREOSEARCH _Version . loop_ _Task 'extraction of torsion angle restraint values' stop_ _Details . _Citation_label $ref_4 save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model UNITY _Field_strength 500 _Details . save_ ############################# # NMR applied experiments # ############################# save_3D_13C-_or_15N-edited_NOESY-HSQC_1 _Saveframe_category NMR_applied_experiment _Experiment_name '3D 13C- or 15N-edited NOESY-HSQC' _Sample_label $sample_1 save_ save_3D_15N-edited_TOCSY-HSQC_2 _Saveframe_category NMR_applied_experiment _Experiment_name '3D 15N-edited TOCSY-HSQC' _Sample_label $sample_1 save_ save_CN_NOESY-HSQC_3 _Saveframe_category NMR_applied_experiment _Experiment_name 'CN NOESY-HSQC' _Sample_label $sample_1 save_ save_HBCBCA(CO)NNH_4 _Saveframe_category NMR_applied_experiment _Experiment_name HBCBCA(CO)NNH _Sample_label $sample_1 save_ save_HNCACB_5 _Saveframe_category NMR_applied_experiment _Experiment_name HNCACB _Sample_label $sample_1 save_ save_(HB)CB(CGCD)HD_6 _Saveframe_category NMR_applied_experiment _Experiment_name (HB)CB(CGCD)HD _Sample_label $sample_1 save_ save_(HB)CB(CGCDCE)HE_7 _Saveframe_category NMR_applied_experiment _Experiment_name (HB)CB(CGCDCE)HE _Sample_label $sample_1 save_ save_HMQC_J_8 _Saveframe_category NMR_applied_experiment _Experiment_name 'HMQC J' _Sample_label $sample_1 save_ ####################### # Sample conditions # ####################### save_condition_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 6.4 0.2 n/a temperature 303 1 K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference _Saveframe_category chemical_shift_reference _Details . loop_ _Mol_common_name _Atom_type _Atom_isotope_number _Atom_group _Chem_shift_units _Chem_shift_value _Reference_method _Reference_type _External_reference_sample_geometry _External_reference_location _External_reference_axis _Indirect_shift_ratio _Reference_correction_type water H 1 protons ppm 4.725 internal direct cylindrical internal parallel 1.0 temperature urea N 15 'amino nitrogens' ppm 78.98 external direct cylindrical external parallel 1.0 . 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_shift_set_1 _Saveframe_category assigned_chemical_shifts _Details 'Some protons (e.g Arg Nh) unobservable due to line broadening or overlap with similar species.' loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $condition_1 _Chem_shift_reference_set_label $chemical_shift_reference _Mol_system_component_name 'PLCC SH2 domain' _Text_data_format . _Text_data . loop_ _Atom_shift_assign_ID _Residue_author_seq_code _Residue_seq_code _Residue_label _Atom_name _Atom_type _Chem_shift_value _Chem_shift_value_error _Chem_shift_ambiguity_code 1 . 4 GLY H H 8.45 0.02 1 2 . 4 GLY N N 109.28 0.02 1 3 . 5 ILE H H 8.03 0.02 1 4 . 5 ILE N N 120.52 0.02 1 5 . 6 HIS H H 8.20 0.02 1 6 . 6 HIS N N 119.89 0.02 1 7 . 7 GLU H H 7.66 0.02 1 8 . 7 GLU N N 120.01 0.02 1 9 . 8 SER H H 7.54 0.02 1 10 . 8 SER N N 113.73 0.02 1 11 . 9 LYS H H 7.63 0.02 1 12 . 9 LYS N N 122.10 0.02 1 13 . 10 GLU H H 8.67 0.02 1 14 . 10 GLU N N 120.51 0.02 1 15 . 11 TRP H H 6.21 0.02 1 16 . 11 TRP N N 109.55 0.02 1 17 . 12 TYR H H 7.67 0.02 1 18 . 12 TYR N N 123.60 0.02 1 19 . 13 HIS H H 8.55 0.02 1 20 . 13 HIS N N 127.82 0.02 1 21 . 14 ALA H H 8.19 0.02 1 22 . 14 ALA N N 125.09 0.02 1 23 . 15 SER H H 8.20 0.02 1 24 . 15 SER N N 111.59 0.02 1 25 . 16 LEU H H 7.95 0.02 1 26 . 16 LEU N N 126.36 0.02 1 27 . 17 THR H H 8.67 0.02 1 28 . 17 THR N N 116.94 0.02 1 29 . 18 ARG H H 9.08 0.02 1 30 . 18 ARG N N 122.59 0.02 1 31 . 19 ALA H H 8.32 0.02 1 32 . 19 ALA N N 119.72 0.02 1 33 . 20 GLN H H 7.73 0.02 1 34 . 20 GLN N N 118.26 0.02 1 35 . 21 ALA H H 8.58 0.02 1 36 . 21 ALA N N 122.72 0.02 1 37 . 22 GLU H H 8.45 0.02 1 38 . 22 GLU N N 116.54 0.02 1 39 . 23 HIS H H 7.92 0.02 1 40 . 23 HIS N N 116.93 0.02 1 41 . 24 MET H H 7.90 0.02 1 42 . 24 MET N N 117.99 0.02 1 43 . 25 LEU H H 7.98 0.02 1 44 . 25 LEU N N 117.80 0.02 1 45 . 26 MET H H 7.99 0.02 1 46 . 26 MET N N 118.71 0.02 1 47 . 27 ARG H H 7.02 0.02 1 48 . 27 ARG N N 116.29 0.02 1 49 . 28 VAL H H 7.01 0.02 1 50 . 28 VAL N N 119.15 0.02 1 51 . 30 ARG H H 7.86 0.02 1 52 . 30 ARG N N 121.78 0.02 1 53 . 31 ASP H H 8.69 0.02 1 54 . 31 ASP N N 124.58 0.02 1 55 . 32 GLY H H 9.45 0.02 1 56 . 32 GLY N N 109.84 0.02 1 57 . 33 ALA H H 7.86 0.02 1 58 . 33 ALA N N 126.42 0.02 1 59 . 34 PHE H H 8.59 0.02 1 60 . 34 PHE N N 117.53 0.02 1 61 . 35 LEU H H 9.22 0.02 1 62 . 35 LEU N N 114.53 0.02 1 63 . 36 VAL H H 9.44 0.02 1 64 . 36 VAL N N 120.69 0.02 1 65 . 37 ARG H H 9.48 0.02 1 66 . 37 ARG N N 123.06 0.02 1 67 . 38 LYS H H 8.01 0.02 1 68 . 38 LYS N N 124.82 0.02 1 69 . 39 ARG H H 7.98 0.02 1 70 . 39 ARG N N 127.09 0.02 1 71 . 40 ASN H H 8.49 0.02 1 72 . 40 ASN N N 118.32 0.02 1 73 . 41 GLU H H 7.31 0.02 1 74 . 41 GLU N N 120.00 0.02 1 75 . 43 ASN H H 8.78 0.02 1 76 . 43 ASN N N 116.16 0.02 1 77 . 44 SER H H 7.61 0.02 1 78 . 44 SER N N 109.49 0.02 1 79 . 45 TYR H H 9.06 0.02 1 80 . 45 TYR N N 124.37 0.02 1 81 . 46 ALA H H 9.43 0.02 1 82 . 46 ALA N N 121.29 0.02 1 83 . 47 ILE H H 9.03 0.02 1 84 . 47 ILE N N 121.21 0.02 1 85 . 48 SER H H 9.06 0.02 1 86 . 48 SER N N 126.60 0.02 1 87 . 49 PHE H H 8.83 0.02 1 88 . 49 PHE N N 121.38 0.02 1 89 . 50 ARG H H 8.24 0.02 1 90 . 50 ARG N N 119.43 0.02 1 91 . 51 ALA H H 8.87 0.02 1 92 . 51 ALA N N 126.95 0.02 1 93 . 52 GLU H H 9.23 0.02 1 94 . 52 GLU N N 121.64 0.02 1 95 . 53 GLY H H 9.32 0.02 1 96 . 53 GLY N N 105.80 0.02 1 97 . 54 LYS H H 7.83 0.02 1 98 . 54 LYS N N 120.78 0.02 1 99 . 55 ILE H H 8.21 0.02 1 100 . 55 ILE N N 119.84 0.02 1 101 . 56 LYS H H 8.48 0.02 1 102 . 56 LYS N N 128.99 0.02 1 103 . 57 HIS H H 7.89 0.02 1 104 . 57 HIS N N 115.65 0.02 1 105 . 58 CYS H H 9.44 0.02 1 106 . 58 CYS N N 121.40 0.02 1 107 . 59 ARG H H 8.86 0.02 1 108 . 59 ARG N N 126.13 0.02 1 109 . 60 VAL H H 8.87 0.02 1 110 . 60 VAL N N 123.90 0.02 1 111 . 61 GLN H H 8.54 0.02 1 112 . 61 GLN N N 125.83 0.02 1 113 . 62 GLN H H 8.66 0.02 1 114 . 62 GLN N N 125.56 0.02 1 115 . 63 GLU H H 8.70 0.02 1 116 . 63 GLU N N 129.78 0.02 1 117 . 64 GLY H H 8.87 0.02 1 118 . 64 GLY N N 116.06 0.02 1 119 . 65 GLN H H 8.99 0.02 1 120 . 65 GLN N N 126.41 0.02 1 121 . 66 THR H H 7.69 0.02 1 122 . 66 THR N N 113.11 0.02 1 123 . 67 VAL H H 8.69 0.02 1 124 . 67 VAL N N 117.21 0.02 1 125 . 68 MET H H 8.98 0.02 1 126 . 68 MET N N 121.56 0.02 1 127 . 69 LEU H H 8.44 0.02 1 128 . 69 LEU N N 125.65 0.02 1 129 . 70 GLY H H 9.31 0.02 1 130 . 70 GLY N N 118.27 0.02 1 131 . 71 ASN H H 8.79 0.02 1 132 . 71 ASN N N 124.77 0.02 1 133 . 72 SER H H 8.20 0.02 1 134 . 72 SER N N 118.12 0.02 1 135 . 73 GLU H H 7.90 0.02 1 136 . 73 GLU N N 124.10 0.02 1 137 . 74 PHE H H 9.02 0.02 1 138 . 74 PHE N N 120.29 0.02 1 139 . 75 ASP H H 9.34 0.02 1 140 . 75 ASP N N 119.71 0.02 1 141 . 76 SER H H 7.32 0.02 1 142 . 76 SER N N 105.72 0.02 1 143 . 77 LEU H H 9.17 0.02 1 144 . 77 LEU N N 122.71 0.02 1 145 . 78 VAL H H 7.83 0.02 1 146 . 78 VAL N N 116.69 0.02 1 147 . 79 ASP H H 7.70 0.02 1 148 . 79 ASP N N 121.61 0.02 1 149 . 80 LEU H H 7.29 0.02 1 150 . 80 LEU N N 123.37 0.02 1 151 . 81 ILE H H 7.76 0.02 1 152 . 81 ILE N N 119.52 0.02 1 153 . 82 SER H H 7.98 0.02 1 154 . 82 SER N N 112.73 0.02 1 155 . 83 TYR H H 7.82 0.02 1 156 . 83 TYR N N 121.94 0.02 1 157 . 84 TYR H H 7.63 0.02 1 158 . 84 TYR N N 118.88 0.02 1 159 . 85 GLU H H 7.40 0.02 1 160 . 85 GLU N N 117.13 0.02 1 161 . 86 LYS H H 7.07 0.02 1 162 . 86 LYS N N 116.67 0.02 1 163 . 87 HIS H H 7.72 0.02 1 164 . 87 HIS N N 120.01 0.02 1 165 . 89 LEU H H 8.38 0.02 1 166 . 89 LEU N N 123.90 0.02 1 167 . 90 TYR H H 6.80 0.02 1 168 . 90 TYR N N 118.04 0.02 1 169 . 91 ARG H H 8.86 0.02 1 170 . 91 ARG N N 125.86 0.02 1 171 . 92 LYS H H 8.30 0.02 1 172 . 92 LYS N N 119.53 0.02 1 173 . 93 MET H H 8.76 0.02 1 174 . 93 MET N N 124.41 0.02 1 175 . 94 LYS H H 7.94 0.02 1 176 . 94 LYS N N 127.34 0.02 1 177 . 95 LEU H H 8.24 0.02 1 178 . 95 LEU N N 119.48 0.02 1 179 . 96 ARG H H 8.40 0.02 1 180 . 96 ARG N N 121.45 0.02 1 181 . 97 TYR H H 7.68 0.02 1 182 . 97 TYR N N 117.95 0.02 1 183 . 99 ILE H H 8.24 0.02 1 184 . 99 ILE N N 124.05 0.02 1 185 . 100 ASN H H 8.46 0.02 1 186 . 100 ASN N N 125.30 0.02 1 187 . 101 GLU H H 8.47 0.02 1 188 . 101 GLU N N 120.18 0.02 1 189 . 102 GLU H H 8.39 0.02 1 190 . 102 GLU N N 121.28 0.02 1 191 . 103 ASN H H 8.33 0.02 1 192 . 103 ASN N N 119.12 0.02 1 193 . 104 SER H H 8.06 0.02 1 194 . 104 SER N N 115.20 0.02 1 195 . 105 SER H H 7.82 0.02 1 196 . 105 SER N N 123.22 0.02 1 stop_ save_