data_7317 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Backbone 1HN, 15N, and 13C Chemical Shift Assignments for wt Im7* (* denotes his-tag) and its variants, Im7*L53AI54A and Im7*YY ; _BMRB_accession_number 7317 _BMRB_flat_file_name bmr7317.str _Entry_type original _Submission_date 2006-10-17 _Accession_date 2006-10-17 _Entry_origination author _NMR_STAR_version 2.1.1 _Experimental_method NMR _Details 'The variants of wt Im7* (L53AI54A and YY) show biochemical and biophysical properties resembling the kinetic protein folding intermediate of wt Im7*. These variants have therefore been studied by NMR to obtain structural and dynamic information of the protein folding intermediate. This entry consists of backbone 1HN, 15N and 13C chemical shifts of the three proteins.' loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Whittaker Sara B.-M. . 2 Spence Graham R. . 3 Grossmann Guenter J. . 4 Radford Sheena E. . 5 Moore Geoffrey R. . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 65 "13C chemical shifts" 195 "15N chemical shifts" 65 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2007-05-04 original author . stop_ _Original_release_date 2007-05-04 save_ ############################# # Citation for this entry # ############################# save_citation_1 _Saveframe_category entry_citation _Citation_full . _Citation_title ; NMR analysis of the conformational properties of the trapped on-pathway folding intermediate of the bacterial immunity protein Im7. ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 17188712 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Whittaker Sara B.-M. . 2 Spence Graham R. . 3 Grossmann Guenter J. . 4 Radford Sheena E. . 5 Moore Geoffrey R. . stop_ _Journal_abbreviation 'J. Mol. Biol.' _Journal_volume 366 _Journal_issue 3 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 1001 _Page_last 1015 _Year 2007 _Details . loop_ _Keyword Im7 intermediate NMR 'partially folded' 'Protein folding' SAXS stop_ save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name Monomer _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label Monomer $L53AI54A_variant_of_Im7* stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state protein _System_paramagnetic no _System_thiol_state 'not present' loop_ _Biological_function 'Inhibitor protein of the endonuclease Colicin E7.' stop_ _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_L53AI54A_variant_of_Im7* _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common L53AI54A _Molecular_mass . _Mol_thiol_state 'not present' loop_ _Biological_function 'Trapped protein folding intermediate of Im7*' stop_ _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 94 _Mol_residue_sequence ; MEHHHHHHELKNSISDYTEA EFVQLLKEIEKENVAATDDV LDVLLEHFVKITEHPDGTDA AYYPSDNRDDSPEGIVKEIK EWRAANGKPGFKQG ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 -8 MET 2 -7 GLU 3 -6 HIS 4 -5 HIS 5 -4 HIS 6 -3 HIS 7 -2 HIS 8 -1 HIS 9 2 GLU 10 3 LEU 11 4 LYS 12 5 ASN 13 6 SER 14 7 ILE 15 8 SER 16 9 ASP 17 10 TYR 18 11 THR 19 12 GLU 20 13 ALA 21 14 GLU 22 15 PHE 23 16 VAL 24 17 GLN 25 18 LEU 26 19 LEU 27 20 LYS 28 21 GLU 29 22 ILE 30 23 GLU 31 24 LYS 32 25 GLU 33 26 ASN 34 27 VAL 35 28 ALA 36 29 ALA 37 30 THR 38 31 ASP 39 32 ASP 40 33 VAL 41 34 LEU 42 35 ASP 43 36 VAL 44 37 LEU 45 38 LEU 46 39 GLU 47 40 HIS 48 41 PHE 49 42 VAL 50 43 LYS 51 44 ILE 52 45 THR 53 46 GLU 54 47 HIS 55 48 PRO 56 49 ASP 57 50 GLY 58 51 THR 59 52 ASP 60 53 ALA 61 54 ALA 62 55 TYR 63 56 TYR 64 57 PRO 65 58 SER 66 59 ASP 67 60 ASN 68 61 ARG 69 62 ASP 70 63 ASP 71 64 SER 72 65 PRO 73 66 GLU 74 67 GLY 75 68 ILE 76 69 VAL 77 70 LYS 78 71 GLU 79 72 ILE 80 73 LYS 81 74 GLU 82 75 TRP 83 76 ARG 84 77 ALA 85 78 ALA 86 79 ASN 87 80 GLY 88 81 LYS 89 82 PRO 90 83 GLY 91 84 PHE 92 85 LYS 93 86 GLN 94 87 GLY stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2014-10-18 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 7188 Im7 91.49 87 97.67 97.67 2.98e-53 BMRB 7316 colicin_E7_inhibitor_polypeptide 100.00 94 97.87 97.87 8.21e-60 PDB 1AYI "Colicin E7 Immunity Protein Im7" 91.49 87 97.67 97.67 2.98e-53 PDB 1CEI "Structure Determination Of The Colicin E7 Immunity Protein (Imme7) That Binds Specifically To The Dnase-Type Colicin E7 And Inh" 91.49 94 97.67 97.67 3.99e-53 PDB 1MZ8 "Crystal Structures Of The Nuclease Domain Of Cole7IM7 IN Complex With A Phosphate Ion And A Zinc Ion" 91.49 87 97.67 97.67 2.98e-53 PDB 1UNK "Structure Of Colicin E7 Immunity Protein" 91.49 87 97.67 97.67 2.98e-53 PDB 1ZNV "How A His-Metal Finger Endonuclease Cole7 Binds And Cleaves Dna With A Transition Metal Ion Cofactor" 91.49 93 97.67 97.67 9.77e-53 PDB 2JAZ "Crystal Structure Of The Mutant N560d Of The Nuclease Domain Of Cole7 In Complex With Im7" 91.49 87 97.67 97.67 2.98e-53 PDB 2JB0 "Crystal Structure Of The Mutant H573a Of The Nuclease Domain Of Cole7 In Complex With Im7" 91.49 87 97.67 97.67 2.98e-53 PDB 2JBG "Crystal Structure Of The Mutant N560a Of The Nuclease Domain Of Cole7 In Complex With Im7" 91.49 87 97.67 97.67 2.98e-53 PDB 7CEI "The Endonuclease Domain Of Colicin E7 In Complex With Its Inhibitor Im7 Protein" 91.49 87 97.67 97.67 2.98e-53 EMBL CAA45165 "immunity protein [Escherichia coli]" 91.49 87 97.67 97.67 2.98e-53 EMBL CDK50318 "Colicin immunity protein/pyocin immunity protein [Escherichia coli IS5]" 91.49 87 97.67 97.67 2.98e-53 GB AIC79148 "colicin E7 immunity protein [Escherichia coli]" 91.49 87 97.67 97.67 2.98e-53 GB ELE46623 "colicin-E7 immunity protein [Escherichia coli KTE72]" 91.49 87 97.67 97.67 2.98e-53 GB EOW15734 "colicin-E7 immunity protein [Escherichia coli KTE107]" 91.49 87 97.67 97.67 2.98e-53 GB EQR11492 "colicin-E7 immunity protein [Escherichia coli HVH 118 (4-7345399)]" 91.49 87 97.67 97.67 2.98e-53 GB ESD96397 "colicin-E7 immunity protein [Escherichia coli 908616]" 91.49 87 97.67 97.67 2.98e-53 REF WP_001560791 "colicin-E7 immunity protein [Escherichia coli]" 91.49 87 97.67 97.67 2.98e-53 REF WP_032277812 "colicin transporter, partial [Escherichia coli]" 54.26 53 100.00 100.00 9.07e-26 REF YP_009060494 "colicin E7 immunity protein [Escherichia coli]" 91.49 87 97.67 97.67 2.98e-53 SP Q03708 "RecName: Full=Colicin-E7 immunity protein; AltName: Full=ImmE7; AltName: Full=Microcin-E7 immunity protein [Escherichia coli]" 91.49 87 97.67 97.67 2.98e-53 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $L53AI54A_variant_of_Im7* 'Escherichia coli' 562 Bacteria . Escherichia coli stop_ save_ ######################### # Experimental source # ######################### save_experimental_source _Saveframe_category experimental_source loop_ _Mol_label _Production_method _Host_organism_name_common _Genus _Species _Strain _Vector_name $L53AI54A_variant_of_Im7* 'recombinant technology' 'E. coli' Escherichia coli . . stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Saveframe_category sample _Sample_type solution _Details 'doubly-labelled (13C/15N) Im7*L53AI54A sample for backbone resonance assignments.' loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $L53AI54A_variant_of_Im7* 1 mM '[U-13C; U-15N]' 'potassium phosphate buffer' 50 mM . 'sodium sulphate' 400 mM . H2O 90 % . D2O 10 % . stop_ save_ save_sample_2 _Saveframe_category sample _Sample_type solution _Details 'singly-labelled (15N) Im7*L53AI54A sample for relaxation data measurement and 15N-edited NOESY experiment.' loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $L53AI54A_variant_of_Im7* 1 mM '[U-99% 15N]' 'potassium phosphate buffer' 50 mM . 'sodium sulphate' 400 mM . H2O 90 % . D2O 10 % . stop_ save_ ############################ # Computer software used # ############################ save_VNMR _Saveframe_category software _Name VNMR _Version 6.1C loop_ _Vendor _Address _Electronic_address Varian . . stop_ loop_ _Task 'Data acquisition' stop_ _Details . save_ save_NMRView _Saveframe_category software _Name NMRView _Version 5.1.1 loop_ _Vendor _Address _Electronic_address Varian . . stop_ loop_ _Task 'Data analysis' stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model Inova _Field_strength 500 _Details . save_ save_spectrometer_2 _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model Inova _Field_strength 600 _Details . save_ save_spectrometer_3 _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model Inova _Field_strength 750 _Details . save_ ############################# # NMR applied experiments # ############################# save_1H15N_HSQC_1 _Saveframe_category NMR_applied_experiment _Experiment_name '1H15N HSQC' _Sample_label . save_ save_HNCO_2 _Saveframe_category NMR_applied_experiment _Experiment_name HNCO _Sample_label . save_ save_HNCA_3 _Saveframe_category NMR_applied_experiment _Experiment_name HNCA _Sample_label . save_ save_HNCOCA_4 _Saveframe_category NMR_applied_experiment _Experiment_name HNCOCA _Sample_label . save_ save_CBCACONH_5 _Saveframe_category NMR_applied_experiment _Experiment_name CBCACONH _Sample_label . save_ save_HNCACB_6 _Saveframe_category NMR_applied_experiment _Experiment_name HNCACB _Sample_label $sample_1 save_ save_1H-1H-15N_NOESY-HSQC_7 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-1H-15N NOESY-HSQC' _Sample_label $sample_2 save_ ####################### # Sample conditions # ####################### save_conditions_1 _Saveframe_category sample_conditions _Details 'Used for all NMR experiments.' loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 7 0.2 pH temperature 298 0.1 K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_referencing _Saveframe_category chemical_shift_reference _Details ; 1H chemical shifts referenced directly against external DSS; 15N and 13C referenced indirectly to DSS using absolute frequency ratios at 298K. ; 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 _Indirect_shift_ratio_citation_label _Correction_value_citation_label DSS C 13 'methyl protons' ppm 0.0 . indirect . . . 0.251449530 $citation_1 $citation_1 DSS H 1 'methyl protons' ppm 0.0 internal direct . . . 1.000000000 $citation_1 $citation_1 DSS N 15 'methyl protons' ppm 0.0 . indirect . . . 0.101329118 $citation_1 $citation_1 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_Im7*_L53AI54A_chemical_shifts _Saveframe_category assigned_chemical_shifts _Details 'Backbone HN, N and C chemical shifts.' loop_ _Software_label $NMRView stop_ loop_ _Experiment_label 1H15N_HSQC HNCO HNCA HNCOCA CBCACONH 1H-1H-15N_NOESY-HSQC stop_ loop_ _Sample_label $sample_1 $sample_2 stop_ _Sample_conditions_label $conditions_1 _Chem_shift_reference_set_label $chemical_shift_referencing _Mol_system_component_name Monomer _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 2 9 GLU C C 176.150 0.2 1 2 2 9 GLU CA C 56.170 0.2 1 3 2 9 GLU CB C 29.990 0.2 1 4 3 10 LEU H H 8.210 0.01 1 5 3 10 LEU C C 177.570 0.2 1 6 3 10 LEU CA C 55.150 0.2 1 7 3 10 LEU CB C 42.340 0.2 1 8 3 10 LEU N N 123.870 0.1 1 9 4 11 LYS H H 7.990 0.01 1 10 4 11 LYS C C 175.910 0.2 1 11 4 11 LYS CA C 56.220 0.2 1 12 4 11 LYS N N 121.400 0.1 1 13 5 12 ASN H H 8.400 0.01 1 14 5 12 ASN C C 175.240 0.2 1 15 5 12 ASN CA C 55.860 0.2 1 16 5 12 ASN CB C 39.710 0.2 1 17 5 12 ASN N N 116.700 0.1 1 18 6 13 SER H H 8.200 0.01 1 19 6 13 SER CA C 56.320 0.2 1 20 6 13 SER N N 112.120 0.1 1 21 8 15 SER C C 174.100 0.2 1 22 8 15 SER CA C 59.870 0.2 1 23 8 15 SER CB C 63.020 0.2 1 24 9 16 ASP H H 7.770 0.01 1 25 9 16 ASP C C 175.800 0.2 1 26 9 16 ASP CA C 55.250 0.2 1 27 9 16 ASP CB C 42.390 0.2 1 28 9 16 ASP N N 118.410 0.1 1 29 10 17 TYR H H 8.130 0.01 1 30 10 17 TYR C C 177.430 0.2 1 31 10 17 TYR CA C 58.130 0.2 1 32 10 17 TYR CB C 40.970 0.2 1 33 10 17 TYR N N 120.140 0.1 1 34 11 18 THR H H 8.800 0.01 1 35 11 18 THR C C 175.690 0.2 1 36 11 18 THR CA C 60.690 0.2 1 37 11 18 THR CB C 70.540 0.2 1 38 11 18 THR N N 112.180 0.1 1 39 12 19 GLU H H 9.090 0.01 1 40 12 19 GLU C C 178.040 0.2 1 41 12 19 GLU CA C 60.670 0.2 1 42 12 19 GLU CB C 29.530 0.2 1 43 12 19 GLU N N 122.880 0.1 1 44 13 20 ALA H H 8.310 0.01 1 45 13 20 ALA C C 181.500 0.2 1 46 13 20 ALA CA C 55.140 0.2 1 47 13 20 ALA CB C 18.430 0.2 1 48 13 20 ALA N N 118.610 0.1 1 49 14 21 GLU H H 7.970 0.01 1 50 14 21 GLU C C 179.430 0.2 1 51 14 21 GLU CA C 58.800 0.2 1 52 14 21 GLU CB C 31.290 0.2 1 53 14 21 GLU N N 118.870 0.1 1 54 15 22 PHE H H 8.520 0.01 1 55 15 22 PHE C C 177.030 0.2 1 56 15 22 PHE CA C 62.160 0.2 1 57 15 22 PHE CB C 40.120 0.2 1 58 15 22 PHE N N 123.730 0.1 1 59 16 23 VAL H H 8.480 0.01 1 60 16 23 VAL C C 177.600 0.2 1 61 16 23 VAL CA C 67.350 0.2 1 62 16 23 VAL CB C 31.770 0.2 1 63 16 23 VAL N N 118.320 0.1 1 64 17 24 GLN H H 7.560 0.01 1 65 17 24 GLN C C 177.870 0.2 1 66 17 24 GLN CA C 59.020 0.2 1 67 17 24 GLN CB C 27.910 0.2 1 68 17 24 GLN N N 117.650 0.1 1 69 18 25 LEU H H 7.640 0.01 1 70 18 25 LEU C C 178.360 0.2 1 71 18 25 LEU CA C 58.290 0.2 1 72 18 25 LEU CB C 41.180 0.2 1 73 18 25 LEU N N 121.520 0.1 1 74 19 26 LEU H H 7.750 0.01 1 75 19 26 LEU C C 179.820 0.2 1 76 19 26 LEU CA C 57.980 0.2 1 77 19 26 LEU CB C 41.070 0.2 1 78 19 26 LEU N N 117.500 0.1 1 79 20 27 LYS H H 8.180 0.01 1 80 20 27 LYS C C 179.520 0.2 1 81 20 27 LYS CA C 59.620 0.2 1 82 20 27 LYS CB C 32.540 0.2 1 83 20 27 LYS N N 119.360 0.1 1 84 21 28 GLU H H 8.130 0.01 1 85 21 28 GLU C C 179.270 0.2 1 86 21 28 GLU CA C 59.200 0.2 1 87 21 28 GLU CB C 29.560 0.2 1 88 21 28 GLU N N 120.730 0.1 1 89 22 29 ILE H H 8.070 0.01 1 90 22 29 ILE C C 178.280 0.2 1 91 22 29 ILE CA C 64.560 0.2 1 92 22 29 ILE CB C 37.680 0.2 1 93 22 29 ILE N N 119.760 0.1 1 94 23 30 GLU H H 7.920 0.01 1 95 23 30 GLU C C 178.230 0.2 1 96 23 30 GLU CA C 59.020 0.2 1 97 23 30 GLU CB C 29.910 0.2 1 98 23 30 GLU N N 120.410 0.1 1 99 24 31 LYS H H 7.680 0.01 1 100 24 31 LYS C C 177.970 0.2 1 101 24 31 LYS CA C 58.260 0.2 1 102 24 31 LYS N N 118.280 0.1 1 103 25 32 GLU H H 7.930 0.01 1 104 25 32 GLU C C 176.840 0.2 1 105 25 32 GLU CA C 57.220 0.2 1 106 25 32 GLU CB C 29.760 0.2 1 107 25 32 GLU N N 117.700 0.1 1 108 26 33 ASN H H 7.990 0.01 1 109 26 33 ASN CA C 53.560 0.2 1 110 26 33 ASN N N 117.720 0.1 1 111 28 35 ALA C C 177.040 0.2 1 112 28 35 ALA CA C 52.590 0.2 1 113 28 35 ALA CB C 19.340 0.2 1 114 29 36 ALA H H 8.110 0.01 1 115 29 36 ALA C C 177.970 0.2 1 116 29 36 ALA CA C 52.590 0.2 1 117 29 36 ALA CB C 19.180 0.2 1 118 29 36 ALA N N 122.250 0.1 1 119 30 37 THR H H 8.010 0.01 1 120 30 37 THR C C 175.040 0.2 1 121 30 37 THR CA C 62.740 0.2 1 122 30 37 THR N N 112.120 0.1 1 123 31 38 ASP H H 8.300 0.01 1 124 31 38 ASP CA C 55.830 0.2 1 125 31 38 ASP N N 121.110 0.1 1 126 32 39 ASP C C 177.490 0.2 1 127 32 39 ASP CA C 55.520 0.2 1 128 32 39 ASP CB C 40.940 0.2 1 129 33 40 VAL H H 7.840 0.01 1 130 33 40 VAL C C 177.300 0.2 1 131 33 40 VAL CA C 65.240 0.2 1 132 33 40 VAL N N 120.080 0.1 1 133 34 41 LEU H H 8.280 0.01 1 134 34 41 LEU C C 178.130 0.2 1 135 34 41 LEU CA C 57.940 0.2 1 136 34 41 LEU CB C 41.410 0.2 1 137 34 41 LEU N N 120.710 0.1 1 138 35 42 ASP H H 7.910 0.01 1 139 35 42 ASP C C 178.740 0.2 1 140 35 42 ASP CA C 57.730 0.2 1 141 35 42 ASP CB C 40.710 0.2 1 142 35 42 ASP N N 118.110 0.1 1 143 36 43 VAL H H 7.530 0.01 1 144 36 43 VAL C C 178.630 0.2 1 145 36 43 VAL CA C 65.580 0.2 1 146 36 43 VAL CB C 31.830 0.2 1 147 36 43 VAL N N 118.710 0.1 1 148 37 44 LEU H H 7.930 0.01 1 149 37 44 LEU C C 178.870 0.2 1 150 37 44 LEU CA C 58.080 0.2 1 151 37 44 LEU CB C 42.380 0.2 1 152 37 44 LEU N N 120.910 0.1 1 153 38 45 LEU H H 8.540 0.01 1 154 38 45 LEU CA C 57.720 0.2 1 155 38 45 LEU N N 118.550 0.1 1 156 49 56 ASP C C 177.080 0.2 1 157 49 56 ASP CA C 54.430 0.2 1 158 49 56 ASP CB C 41.160 0.2 1 159 50 57 GLY H H 8.310 0.01 1 160 50 57 GLY C C 174.770 0.2 1 161 50 57 GLY CA C 45.640 0.2 1 162 50 57 GLY N N 109.100 0.1 1 163 51 58 THR H H 8.110 0.01 1 164 51 58 THR C C 174.530 0.2 1 165 51 58 THR CA C 62.470 0.2 1 166 51 58 THR CB C 69.530 0.2 1 167 51 58 THR N N 113.490 0.1 1 168 52 59 ASP H H 8.360 0.01 1 169 52 59 ASP C C 175.980 0.2 1 170 52 59 ASP CA C 54.620 0.2 1 171 52 59 ASP CB C 41.260 0.2 1 172 52 59 ASP N N 122.310 0.1 1 173 53 60 ALA H H 8.040 0.01 1 174 53 60 ALA CA C 52.700 0.2 1 175 53 60 ALA N N 124.130 0.1 1 176 54 61 ALA C C 176.920 0.2 1 177 54 61 ALA CA C 52.510 0.2 1 178 54 61 ALA CB C 19.450 0.2 1 179 55 62 TYR H H 7.840 0.01 1 180 55 62 TYR C C 174.140 0.2 1 181 55 62 TYR CA C 57.620 0.2 1 182 55 62 TYR CB C 38.910 0.2 1 183 55 62 TYR N N 118.890 0.1 1 184 56 63 TYR H H 7.680 0.01 1 185 56 63 TYR CA C 55.160 0.2 1 186 56 63 TYR N N 124.890 0.1 1 187 57 64 PRO C C 176.650 0.2 1 188 57 64 PRO CA C 62.900 0.2 1 189 57 64 PRO CB C 31.990 0.2 1 190 58 65 SER H H 8.390 0.01 1 191 58 65 SER C C 174.780 0.2 1 192 58 65 SER CA C 58.680 0.2 1 193 58 65 SER CB C 63.890 0.2 1 194 58 65 SER N N 116.720 0.1 1 195 59 66 ASP H H 8.420 0.01 1 196 59 66 ASP C C 176.090 0.2 1 197 59 66 ASP CA C 54.820 0.2 1 198 59 66 ASP CB C 41.110 0.2 1 199 59 66 ASP N N 121.730 0.1 1 200 60 67 ASN H H 8.270 0.01 1 201 60 67 ASN C C 174.830 0.2 1 202 60 67 ASN CA C 53.080 0.2 1 203 60 67 ASN CB C 38.740 0.2 1 204 60 67 ASN N N 117.740 0.1 1 205 61 68 ARG H H 7.940 0.01 1 206 61 68 ARG C C 175.700 0.2 1 207 61 68 ARG CA C 56.650 0.2 1 208 61 68 ARG CB C 31.190 0.2 1 209 61 68 ARG N N 120.810 0.1 1 210 62 69 ASP H H 8.420 0.01 1 211 62 69 ASP C C 175.220 0.2 1 212 62 69 ASP CA C 54.040 0.2 1 213 62 69 ASP CB C 41.220 0.2 1 214 62 69 ASP N N 122.700 0.1 1 215 63 70 ASP H H 8.110 0.01 1 216 63 70 ASP C C 175.900 0.2 1 217 63 70 ASP CA C 53.670 0.2 1 218 63 70 ASP CB C 40.640 0.2 1 219 63 70 ASP N N 122.500 0.1 1 220 64 71 SER H H 8.250 0.01 1 221 64 71 SER CA C 57.090 0.2 1 222 64 71 SER CB C 63.730 0.2 1 223 64 71 SER N N 116.340 0.1 1 224 65 72 PRO C C 177.480 0.2 1 225 65 72 PRO CA C 65.890 0.2 1 226 65 72 PRO CB C 34.590 0.2 1 227 66 73 GLU H H 9.100 0.01 1 228 66 73 GLU C C 179.470 0.2 1 229 66 73 GLU CA C 60.780 0.2 1 230 66 73 GLU CB C 28.650 0.2 1 231 66 73 GLU N N 115.290 0.1 1 232 67 74 GLY H H 8.170 0.01 1 233 67 74 GLY C C 176.820 0.2 1 234 67 74 GLY CA C 47.100 0.2 1 235 67 74 GLY N N 110.920 0.1 1 236 68 75 ILE H H 8.420 0.01 1 237 68 75 ILE C C 178.320 0.2 1 238 68 75 ILE CA C 64.700 0.2 1 239 68 75 ILE CB C 37.700 0.2 1 240 68 75 ILE N N 124.180 0.1 1 241 69 76 VAL H H 8.070 0.01 1 242 69 76 VAL C C 177.310 0.2 1 243 69 76 VAL CA C 67.820 0.2 1 244 69 76 VAL CB C 31.530 0.2 1 245 69 76 VAL N N 119.110 0.1 1 246 70 77 LYS H H 7.710 0.01 1 247 70 77 LYS C C 178.600 0.2 1 248 70 77 LYS CA C 60.230 0.2 1 249 70 77 LYS CB C 32.580 0.2 1 250 70 77 LYS N N 119.880 0.1 1 251 71 78 GLU H H 7.840 0.01 1 252 71 78 GLU C C 179.980 0.2 1 253 71 78 GLU CA C 59.630 0.2 1 254 71 78 GLU CB C 29.620 0.2 1 255 71 78 GLU N N 118.990 0.1 1 256 72 79 ILE H H 8.680 0.01 1 257 72 79 ILE C C 177.980 0.2 1 258 72 79 ILE CA C 65.510 0.2 1 259 72 79 ILE CB C 37.980 0.2 1 260 72 79 ILE N N 120.830 0.1 1 261 73 80 LYS H H 8.780 0.01 1 262 73 80 LYS C C 180.180 0.2 1 263 73 80 LYS CA C 60.680 0.2 1 264 73 80 LYS CB C 32.850 0.2 1 265 73 80 LYS N N 120.130 0.1 1 266 74 81 GLU H H 8.200 0.01 1 267 74 81 GLU C C 178.920 0.2 1 268 74 81 GLU CA C 59.460 0.2 1 269 74 81 GLU CB C 29.530 0.2 1 270 74 81 GLU N N 119.360 0.1 1 271 75 82 TRP H H 8.530 0.01 1 272 75 82 TRP C C 179.210 0.2 1 273 75 82 TRP CA C 61.350 0.2 1 274 75 82 TRP CB C 29.350 0.2 1 275 75 82 TRP N N 123.150 0.1 1 276 76 83 ARG H H 8.830 0.01 1 277 76 83 ARG C C 178.360 0.2 1 278 76 83 ARG CA C 58.730 0.2 1 279 76 83 ARG N N 118.510 0.1 1 280 77 84 ALA H H 7.740 0.01 1 281 77 84 ALA C C 181.500 0.2 1 282 77 84 ALA CA C 55.190 0.2 1 283 77 84 ALA N N 120.670 0.1 1 284 78 85 ALA H H 8.120 0.01 1 285 78 85 ALA C C 178.530 0.2 1 286 78 85 ALA CA C 54.430 0.2 1 287 78 85 ALA CB C 18.430 0.2 1 288 78 85 ALA N N 121.120 0.1 1 289 79 86 ASN H H 7.160 0.01 1 290 79 86 ASN C C 174.560 0.2 1 291 79 86 ASN CA C 53.370 0.2 1 292 79 86 ASN CB C 39.900 0.2 1 293 79 86 ASN N N 113.650 0.1 1 294 80 87 GLY H H 7.720 0.01 1 295 80 87 GLY C C 174.450 0.2 1 296 80 87 GLY CA C 47.090 0.2 1 297 80 87 GLY N N 108.830 0.1 1 298 81 88 LYS H H 8.000 0.01 1 299 81 88 LYS CA C 52.670 0.2 1 300 81 88 LYS N N 119.460 0.1 1 301 82 89 PRO C C 176.600 0.2 1 302 82 89 PRO CA C 62.750 0.2 1 303 82 89 PRO CB C 32.440 0.2 1 304 83 90 GLY H H 8.280 0.01 1 305 83 90 GLY C C 173.930 0.2 1 306 83 90 GLY CA C 43.530 0.2 1 307 83 90 GLY N N 109.900 0.1 1 308 84 91 PHE H H 8.080 0.01 1 309 84 91 PHE C C 176.430 0.2 1 310 84 91 PHE CA C 59.610 0.2 1 311 84 91 PHE CB C 39.850 0.2 1 312 84 91 PHE N N 119.300 0.1 1 313 85 92 LYS H H 8.450 0.01 1 314 85 92 LYS C C 176.590 0.2 1 315 85 92 LYS CA C 57.290 0.2 1 316 85 92 LYS CB C 32.870 0.2 1 317 85 92 LYS N N 123.880 0.1 1 318 86 93 GLN H H 8.650 0.01 1 319 86 93 GLN C C 175.470 0.2 1 320 86 93 GLN CA C 56.360 0.2 1 321 86 93 GLN CB C 29.680 0.2 1 322 86 93 GLN N N 124.450 0.1 1 323 87 94 GLY H H 8.050 0.01 1 324 87 94 GLY CA C 46.510 0.2 1 325 87 94 GLY N N 116.860 0.1 1 stop_ save_