data_27362 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Backbone (HN, N) Resonance Assignment and 15N T1, T2 Relaxation Parameters for doubly phosphorylated Abl1 SH3 pY89/pY134 ; _BMRB_accession_number 27362 _BMRB_flat_file_name bmr27362.str _Entry_type original _Submission_date 2018-01-16 _Accession_date 2018-01-16 _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 Toke Orsolya . . 2 Mero Balazs . . 3 Radnai Laszlo . . 4 Buday Laszlo . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 T1_relaxation 1 T2_relaxation 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 49 "15N chemical shifts" 49 "T1 relaxation values" 49 "T2 relaxation values" 49 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2019-03-26 update BMRB 'update entry citation' 2019-01-18 original author 'original release' stop_ loop_ _Related_BMRB_accession_number _Relationship 27359 'Abl1 SH3 monomer' stop_ _Original_release_date 2018-01-16 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; Structural insights into the tyrosine phosphorylation-mediated inhibition of SH3 domain-ligand interactions ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 30659095 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Mero Balazs . . 2 Radnai Laszlo . . 3 Gogl Gergo . . 4 Toke Orsolya . . 5 Leveles Ibolya . . 6 Koprivanacz Kitti . . 7 Szeder Balint . . 8 Dulk Metta . . 9 Kudlik Gyongyi . . 10 Vas Virag . . 11 Cserkaszky Anna . . 12 Sipeki Szabolcs . . 13 Nyitray Laszlo . . 14 Vertessy Beata G. . 15 Buday Laszlo . . stop_ _Journal_abbreviation 'J. Biol. Chem.' _Journal_volume 294 _Journal_issue 12 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 4608 _Page_last 4620 _Year 2019 _Details . loop_ _Keyword 3BP2 Abl1 Abl2 'NMR spectroscopy' SH3 'X-ray crystallography' 'circular dichroism' 'in vitro phosphorylation' 'ligand binding' regulation 'small angle X-ray scattering' stop_ save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name 'Abl1 SH3 pY89pY134 monomer' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'Src homology domain 3' $Abl1_SH3_pY89pY134 stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state ? _System_paramagnetic no _System_thiol_state . _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_Abl1_SH3_pY89pY134 _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common Abl1_SH3_pY89pY134 _Molecular_mass . _Mol_thiol_state 'not reported' loop_ _Biological_function 'regulation of signal transduction pathways' stop_ _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 58 _Mol_residue_sequence ; MNLFVALXDFVASGDNTLSI TKGEKLRVLGYNHNGEWCEA QTKNGQGWVPSNXITPVN ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 -1 MET 2 0 ASN 3 1 LEU 4 2 PHE 5 3 VAL 6 4 ALA 7 5 LEU 8 6 PTR 9 7 ASP 10 8 PHE 11 9 VAL 12 10 ALA 13 11 SER 14 12 GLY 15 13 ASP 16 14 ASN 17 15 THR 18 16 LEU 19 17 SER 20 18 ILE 21 19 THR 22 20 LYS 23 21 GLY 24 22 GLU 25 23 LYS 26 24 LEU 27 25 ARG 28 26 VAL 29 27 LEU 30 28 GLY 31 29 TYR 32 30 ASN 33 31 HIS 34 32 ASN 35 33 GLY 36 34 GLU 37 35 TRP 38 36 CYS 39 37 GLU 40 38 ALA 41 39 GLN 42 40 THR 43 41 LYS 44 42 ASN 45 43 GLY 46 44 GLN 47 45 GLY 48 46 TRP 49 47 VAL 50 48 PRO 51 49 SER 52 50 ASN 53 51 PTR 54 52 ILE 55 53 THR 56 54 PRO 57 55 VAL 58 56 ASN stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date . save_ ###################### # Polymer residues # ###################### save_chem_comp_PTR _Saveframe_category polymer_residue _Mol_type 'L-PEPTIDE LINKING' _Name_common O-PHOSPHOTYROSINE _BMRB_code PTR _PDB_code PTR _Standard_residue_derivative . _Molecular_mass 261.168 _Mol_paramagnetic . _Details . loop_ _Atom_name _PDB_atom_name _Atom_type _Atom_chirality _Atom_charge _Atom_oxidation_number _Atom_unpaired_electrons N N N . 0 . ? CA CA C . 0 . ? C C C . 0 . ? O O O . 0 . ? OXT OXT O . 0 . ? CB CB C . 0 . ? CG CG C . 0 . ? CD1 CD1 C . 0 . ? CD2 CD2 C . 0 . ? CE1 CE1 C . 0 . ? CE2 CE2 C . 0 . ? CZ CZ C . 0 . ? OH OH O . 0 . ? P P P . 0 . ? O1P O1P O . 0 . ? O2P O2P O . 0 . ? O3P O3P O . 0 . ? H H H . 0 . ? HN2 HN2 H . 0 . ? HA HA H . 0 . ? HXT HXT H . 0 . ? HB2 HB2 H . 0 . ? HB3 HB3 H . 0 . ? HD1 HD1 H . 0 . ? HD2 HD2 H . 0 . ? HE1 HE1 H . 0 . ? HE2 HE2 H . 0 . ? HO2P HO2P H . 0 . ? HO3P HO3P H . 0 . ? stop_ loop_ _Bond_order _Bond_atom_one_atom_name _Bond_atom_two_atom_name _PDB_bond_atom_one_atom_name _PDB_bond_atom_two_atom_name SING N CA ? ? SING N H ? ? SING N HN2 ? ? SING CA C ? ? SING CA CB ? ? SING CA HA ? ? DOUB C O ? ? SING C OXT ? ? SING OXT HXT ? ? SING CB CG ? ? SING CB HB2 ? ? SING CB HB3 ? ? DOUB CG CD1 ? ? SING CG CD2 ? ? SING CD1 CE1 ? ? SING CD1 HD1 ? ? DOUB CD2 CE2 ? ? SING CD2 HD2 ? ? DOUB CE1 CZ ? ? SING CE1 HE1 ? ? SING CE2 CZ ? ? SING CE2 HE2 ? ? SING CZ OH ? ? SING OH P ? ? DOUB P O1P ? ? SING P O2P ? ? SING P O3P ? ? SING O2P HO2P ? ? SING O3P HO3P ? ? stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $Abl1_SH3_pY89pY134 Human 9606 Eukaryota Metazoa Homo sapiens 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 $Abl1_SH3_pY89pY134 'recombinant technology' . Escherichia coli . 'modified pET' 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 _Concentration_min_value _Concentration_max_value _Isotopic_labeling $Abl1_SH3_pY89pY134 1.0 mM 0.9 1.1 [U-15N] NaN3 3 mM . . 'natural abundance' TCEP 0.5 mM . . 'natural abundance' stop_ save_ ############################ # Computer software used # ############################ save_VNMRJ _Saveframe_category software _Name VNMRJ _Version . loop_ _Vendor _Address _Electronic_address Varian . . stop_ loop_ _Task 'data collection' stop_ _Details . save_ save_Felix _Saveframe_category software _Name Felix _Version . loop_ _Vendor _Address _Electronic_address Accelrys . . stop_ loop_ _Task 'chemical shift assignment' stop_ _Details . save_ save_CcpNMR _Saveframe_category software _Name CcpNMR _Version . loop_ _Vendor _Address _Electronic_address CCPN . . stop_ loop_ _Task 'data analysis' stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model 'Varian NMR System' _Field_strength 600 _Details . save_ ############################# # NMR applied experiments # ############################# save_2D_1H-15N_HSQC_1 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-15N HSQC' _Sample_label $sample_1 save_ save_2D_1H-1H_TOCSY_2 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-1H TOCSY' _Sample_label $sample_1 save_ save_2D_1H-1H_NOESY_3 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-1H NOESY' _Sample_label $sample_1 save_ save_3D_1H-15N_TOCSY_4 _Saveframe_category NMR_applied_experiment _Experiment_name '3D 1H-15N TOCSY' _Sample_label $sample_1 save_ save_3D_1H-15N_NOESY_5 _Saveframe_category NMR_applied_experiment _Experiment_name '3D 1H-15N NOESY' _Sample_label $sample_1 save_ save_2D_1H-13C_HSQC_6 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-13C HSQC' _Sample_label $sample_1 save_ save_2D_1H-15N_HSQC_T1_relaxation_7 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-15N HSQC T1 relaxation' _Sample_label $sample_1 save_ save_2D_1H-15N_HSQC_T2_relaxation_8 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-15N HSQC T2 relaxation' _Sample_label $sample_1 save_ ####################### # Sample conditions # ####################### save_sample_conditions_1 _Saveframe_category sample_conditions _Details ; PBS buffer pH 7.2, 3mM NaN3, 0,5 mM TCEP, 25 C ; loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units 'ionic strength' 70 . mM pH 7.2 . pH pressure 1 . atm temperature 298 . K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference_1 _Saveframe_category chemical_shift_reference _Details . loop_ _Mol_common_name _Atom_type _Atom_isotope_number _Atom_group _Chem_shift_units _Chem_shift_value _Reference_method _Reference_type _External_reference_sample_geometry _External_reference_location _External_reference_axis _Indirect_shift_ratio DSS H 1 'methyl protons' ppm 0.0 external direct . . . 1 DSS N 15 'methyl protons' ppm 0.0 external 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_assigned_chem_shift_list_1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Experiment_label '2D 1H-15N HSQC' '2D 1H-1H TOCSY' '2D 1H-1H NOESY' '3D 1H-15N TOCSY' '3D 1H-15N NOESY' '2D 1H-13C HSQC' stop_ loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $sample_conditions_1 _Chem_shift_reference_set_label $chemical_shift_reference_1 _Mol_system_component_name 'Src homology domain 3' _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 3 LEU H H 8.04 0.03 1 2 1 3 LEU N N 121.3 0.2 1 3 2 4 PHE H H 9.31 0.03 1 4 2 4 PHE N N 125.0 0.2 1 5 3 5 VAL H H 9.47 0.03 1 6 3 5 VAL N N 117.3 0.2 1 7 4 6 ALA H H 8.39 0.03 1 8 4 6 ALA N N 126.8 0.2 1 9 5 7 LEU H H 9.59 0.03 1 10 5 7 LEU N N 127.8 0.2 1 11 6 8 PTR H H 7.21 0.03 1 12 6 8 PTR N N 112.8 0.2 1 13 7 9 ASP H H 8.29 0.03 1 14 7 9 ASP N N 117.0 0.2 1 15 8 10 PHE H H 8.77 0.03 1 16 8 10 PHE N N 121.2 0.2 1 17 9 11 VAL H H 8.01 0.03 1 18 9 11 VAL N N 128.9 0.2 1 19 10 12 ALA H H 8.27 0.03 1 20 10 12 ALA N N 129.4 0.2 1 21 11 13 SER H H 8.03 0.03 1 22 11 13 SER N N 115.3 0.2 1 23 14 16 ASN H H 8.60 0.03 1 24 14 16 ASN N N 116.0 0.2 1 25 15 17 THR H H 7.81 0.03 1 26 15 17 THR N N 108.9 0.2 1 27 16 18 LEU H H 8.29 0.03 1 28 16 18 LEU N N 125.8 0.2 1 29 17 19 SER H H 8.17 0.03 1 30 17 19 SER N N 120.7 0.2 1 31 18 20 ILE H H 9.04 0.03 1 32 18 20 ILE N N 117.8 0.2 1 33 19 21 THR H H 9.00 0.03 1 34 19 21 THR N N 119.0 0.2 1 35 20 22 LYS H H 8.96 0.03 1 36 20 22 LYS N N 124.6 0.2 1 37 21 23 GLY H H 8.97 0.03 1 38 21 23 GLY N N 115.1 0.2 1 39 23 25 LYS H H 8.35 0.03 1 40 23 25 LYS N N 122.0 0.2 1 41 24 26 LEU H H 9.17 0.03 1 42 24 26 LEU N N 119.8 0.2 1 43 25 27 ARG H H 8.30 0.03 1 44 25 27 ARG N N 120.0 0.2 1 45 26 28 VAL H H 8.58 0.03 1 46 26 28 VAL N N 124.5 0.2 1 47 27 29 LEU H H 9.26 0.03 1 48 27 29 LEU N N 128.5 0.2 1 49 28 30 GLY H H 6.96 0.03 1 50 28 30 GLY N N 105.5 0.2 1 51 29 31 TYR H H 8.75 0.03 1 52 29 31 TYR N N 116.9 0.2 1 53 30 32 ASN H H 8.92 0.03 1 54 30 32 ASN N N 120.2 0.2 1 55 32 34 ASN H H 6.56 0.03 1 56 32 34 ASN N N 113.5 0.2 1 57 33 35 GLY H H 7.65 0.03 1 58 33 35 GLY N N 107.4 0.2 1 59 34 36 GLU H H 8.41 0.03 1 60 34 36 GLU N N 121.8 0.2 1 61 35 37 TRP H H 8.30 0.03 1 62 35 37 TRP N N 118.8 0.2 1 63 36 38 CYS H H 8.53 0.03 1 64 36 38 CYS N N 123.8 0.2 1 65 37 39 GLU H H 8.08 0.03 1 66 37 39 GLU N N 128.0 0.2 1 67 38 40 ALA H H 9.00 0.03 1 68 38 40 ALA N N 130.7 0.2 1 69 39 41 GLN H H 8.79 0.03 1 70 39 41 GLN N N 117.1 0.2 1 71 40 42 THR H H 9.09 0.03 1 72 40 42 THR N N 117.8 0.2 1 73 42 44 ASN H H 8.25 0.03 1 74 42 44 ASN N N 114.0 0.2 1 75 43 45 GLY H H 7.50 0.03 1 76 43 45 GLY N N 108.2 0.2 1 77 44 46 GLN H H 8.28 0.03 1 78 44 46 GLN N N 119.6 0.2 1 79 45 47 GLY H H 8.71 0.03 1 80 45 47 GLY N N 112.2 0.2 1 81 46 48 TRP H H 8.88 0.03 1 82 46 48 TRP N N 121.1 0.2 1 83 47 49 VAL H H 9.71 0.03 1 84 47 49 VAL N N 116.3 0.2 1 85 49 51 SER H H 8.30 0.03 1 86 49 51 SER N N 120.6 0.2 1 87 50 52 ASN H H 8.43 0.03 1 88 50 52 ASN N N 114.1 0.2 1 89 51 53 PTR H H 7.78 0.03 1 90 51 53 PTR N N 118.4 0.2 1 91 52 54 ILE H H 7.45 0.03 1 92 52 54 ILE N N 112.3 0.2 1 93 53 55 THR H H 8.75 0.03 1 94 53 55 THR N N 116.0 0.2 1 95 55 57 VAL H H 8.02 0.03 1 96 55 57 VAL N N 120.9 0.2 1 97 56 58 ASN H H 7.90 0.03 1 98 56 58 ASN N N 127.6 0.2 1 stop_ save_ save_heteronuclear_T1_list_1 _Saveframe_category T1_relaxation _Details . loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $sample_conditions_1 _Spectrometer_frequency_1H 600 _T1_coherence_type Iz _T1_value_units s-1 _Mol_system_component_name 'Src homology domain 3' _Text_data_format . _Text_data . loop_ _T1_ID _Residue_seq_code _Residue_label _Atom_name _T1_value _T1_value_error 1 3 LEU N 2.22 0.10 2 4 PHE N 2.43 0.08 3 5 VAL N 2.40 0.06 4 6 ALA N 2.52 0.09 5 7 LEU N 2.48 0.09 6 8 PTR N 2.15 0.06 7 9 ASP N 2.13 0.08 8 10 PHE N 2.23 0.04 9 11 VAL N 2.24 0.06 10 12 ALA N 2.36 0.11 11 13 SER N 1.77 0.23 12 16 ASN N 2.10 0.10 13 17 THR N 2.58 0.17 14 18 LEU N 2.32 0.11 15 19 SER N 2.21 0.12 16 20 ILE N 2.31 0.10 17 21 THR N 2.46 0.07 18 22 LYS N 2.31 0.10 19 23 GLY N 2.40 0.08 20 25 LYS N 2.30 0.09 21 26 LEU N 2.31 0.09 22 27 ARG N 2.24 0.09 23 28 VAL N 2.13 0.03 24 29 LEU N 2.38 0.08 25 30 GLY N 2.22 0.06 26 31 TYR N 2.17 0.07 27 32 ASN N 2.39 0.09 28 34 ASN N 2.42 0.24 29 35 GLY N 2.41 0.16 30 36 GLU N 2.42 0.12 31 37 TRP N 2.52 0.06 32 38 CYS N 2.42 0.03 33 39 GLU N 2.20 0.08 34 40 ALA N 2.36 0.08 35 41 GLN N 2.13 0.05 36 42 THR N 2.36 0.18 37 44 ASN N 2.51 0.14 38 45 GLY N 2.02 0.12 39 46 GLN N 2.17 0.07 40 47 GLY N 2.43 0.07 41 48 TRP N 2.37 0.19 42 49 VAL N 2.43 0.07 43 51 SER N 2.57 0.07 44 52 ASN N 2.61 0.09 45 53 PTR N 2.25 0.15 46 54 ILE N 2.27 0.15 47 55 THR N 2.50 0.10 48 57 VAL N 2.25 0.08 49 58 ASN N 1.74 0.09 stop_ save_ save_heteronuclear_T2_list_1 _Saveframe_category T2_relaxation _Details . loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $sample_conditions_1 _Spectrometer_frequency_1H 600 _T2_coherence_type I(+,-) _T2_value_units s-1 _Mol_system_component_name 'Src homology domain 3' _Text_data_format . _Text_data . loop_ _T2_ID _Residue_seq_code _Residue_label _Atom_name _T2_value _T2_value_error _Rex_value _Rex_error 1 3 LEU N 4.84 0.23 . . 2 4 PHE N 5.62 0.38 . . 3 5 VAL N 5.49 0.15 . . 4 6 ALA N 5.52 0.31 . . 5 7 LEU N 5.47 0.25 . . 6 8 PTR N 5.11 0.10 . . 7 9 ASP N 5.10 0.19 . . 8 10 PHE N 5.41 0.27 . . 9 11 VAL N 5.77 0.40 . . 10 12 ALA N 5.30 0.23 . . 11 13 SER N 4.63 0.22 . . 12 16 ASN N 5.63 0.45 . . 13 17 THR N 5.83 0.32 . . 14 18 LEU N 5.27 0.16 . . 15 19 SER N 5.25 0.20 . . 16 20 ILE N 6.11 0.35 . . 17 21 THR N 5.65 0.24 . . 18 22 LYS N 5.39 0.16 . . 19 23 GLY N 5.68 0.21 . . 20 25 LYS N 5.09 0.21 . . 21 26 LEU N 5.33 0.19 . . 22 27 ARG N 5.43 0.29 . . 23 28 VAL N 5.48 0.22 . . 24 29 LEU N 5.69 0.40 . . 25 30 GLY N 4.86 0.23 . . 26 31 TYR N 5.32 0.23 . . 27 32 ASN N 5.96 0.21 . . 28 34 ASN N 9.88 1.04 . . 29 35 GLY N 6.00 0.55 . . 30 36 GLU N 5.50 0.31 . . 31 37 TRP N 5.69 0.41 . . 32 38 CYS N 6.16 0.20 . . 33 39 GLU N 5.84 0.28 . . 34 40 ALA N 5.65 0.30 . . 35 41 GLN N 5.31 0.17 . . 36 42 THR N 5.55 0.19 . . 37 44 ASN N 5.23 0.20 . . 38 45 GLY N 4.98 0.32 . . 39 46 GLN N 5.03 0.19 . . 40 47 GLY N 5.71 0.30 . . 41 48 TRP N 5.28 0.18 . . 42 49 VAL N 5.81 0.21 . . 43 51 SER N 5.73 0.13 . . 44 52 ASN N 5.67 0.34 . . 45 53 PTR N 5.90 0.35 . . 46 54 ILE N 8.87 1.15 . . 47 55 THR N 5.89 0.31 . . 48 57 VAL N 4.85 0.19 . . 49 58 ASN N 3.33 0.24 . . stop_ save_