data_7316 ####################### # 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 7316 _BMRB_flat_file_name bmr7316.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" 80 "13C chemical shifts" 247 "15N chemical shifts" 80 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 $colicin_E7_inhibitor_polypeptide 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_colicin_E7_inhibitor_polypeptide _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common Im7* _Molecular_mass . _Mol_thiol_state 'not present' loop_ _Biological_function 'Dnase inhibitor' stop_ _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 94 _Mol_residue_sequence ; MEHHHHHHELKNSISDYTEA EFVQLLKEIEKENVAATDDV LDVLLEHFVKITEHPDGTDL IYYPSDNRDDSPEGIVKEIK 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 LEU 61 54 ILE 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 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 BMRB 7188 Im7 91.49 87 100.00 100.00 1.06e-54 BMRB 7317 L53AI54A_variant_of_Im7* 100.00 94 97.87 97.87 9.00e-60 PDB 1AYI "Colicin E7 Immunity Protein Im7" 91.49 87 100.00 100.00 1.06e-54 PDB 1CEI "Structure Determination Of The Colicin E7 Immunity Protein (Imme7) That Binds Specifically To The Dnase-Type Colicin E7 And Inh" 91.49 94 100.00 100.00 1.49e-54 PDB 1MZ8 "Crystal Structures Of The Nuclease Domain Of Cole7IM7 IN Complex With A Phosphate Ion And A Zinc Ion" 91.49 87 100.00 100.00 1.06e-54 PDB 1UJZ "Crystal Structure Of The E7_cIM7_C COMPLEX; A Computationally Designed Interface Between The Colicin E7 Dnase And The Im7 Immun" 91.49 87 98.84 98.84 2.11e-53 PDB 1UNK "Structure Of Colicin E7 Immunity Protein" 91.49 87 100.00 100.00 1.06e-54 PDB 1ZNV "How A His-Metal Finger Endonuclease Cole7 Binds And Cleaves Dna With A Transition Metal Ion Cofactor" 91.49 93 100.00 100.00 3.43e-54 PDB 2ERH "Crystal Structure Of The E7_gIM7_G COMPLEX; A DESIGNED Interface Between The Colicin E7 Dnase And The Im7 Immunity Protein" 91.49 87 97.67 97.67 1.48e-52 PDB 2JAZ "Crystal Structure Of The Mutant N560d Of The Nuclease Domain Of Cole7 In Complex With Im7" 91.49 87 100.00 100.00 1.06e-54 PDB 2JB0 "Crystal Structure Of The Mutant H573a Of The Nuclease Domain Of Cole7 In Complex With Im7" 91.49 87 100.00 100.00 1.06e-54 PDB 2JBG "Crystal Structure Of The Mutant N560a Of The Nuclease Domain Of Cole7 In Complex With Im7" 91.49 87 100.00 100.00 1.06e-54 PDB 7CEI "The Endonuclease Domain Of Colicin E7 In Complex With Its Inhibitor Im7 Protein" 91.49 87 100.00 100.00 1.06e-54 EMBL CAA45165 "immunity protein [Escherichia coli]" 91.49 87 100.00 100.00 1.06e-54 EMBL CDK50318 "Colicin immunity protein/pyocin immunity protein [Escherichia coli IS5]" 91.49 87 100.00 100.00 1.06e-54 GB AAA23071 "immunity protein [Plasmid ColE7]" 91.49 87 97.67 98.84 6.34e-53 GB AIC79148 "colicin E7 immunity protein [Escherichia coli]" 91.49 87 100.00 100.00 1.06e-54 GB ELE46623 "colicin-E7 immunity protein [Escherichia coli KTE72]" 91.49 87 100.00 100.00 1.06e-54 GB EOW15734 "colicin-E7 immunity protein [Escherichia coli KTE107]" 91.49 87 100.00 100.00 1.06e-54 GB EQR11492 "colicin-E7 immunity protein [Escherichia coli HVH 118 (4-7345399)]" 91.49 87 100.00 100.00 1.06e-54 REF WP_001560791 "colicin-E7 immunity protein [Escherichia coli]" 91.49 87 100.00 100.00 1.06e-54 REF WP_032277812 "colicin transporter, partial [Escherichia coli]" 55.32 53 100.00 100.00 3.06e-26 REF YP_009060494 "colicin E7 immunity protein [Escherichia coli]" 91.49 87 100.00 100.00 1.06e-54 SP Q03708 "RecName: Full=Colicin-E7 immunity protein; AltName: Full=ImmE7; AltName: Full=Microcin-E7 immunity protein [Escherichia coli]" 91.49 87 100.00 100.00 1.06e-54 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $colicin_E7_inhibitor_polypeptide '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 $colicin_E7_inhibitor_polypeptide '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* sample for backbone resonance assignments.' loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $colicin_E7_inhibitor_polypeptide 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* sample for relaxation data measurement.' loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $colicin_E7_inhibitor_polypeptide 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 $All_samples save_ save_HNCO_2 _Saveframe_category NMR_applied_experiment _Experiment_name HNCO _Sample_label $Samples_1_and_3_and_5 save_ save_HNCA_3 _Saveframe_category NMR_applied_experiment _Experiment_name HNCA _Sample_label $Samples_3_and_5 save_ save_HNCOCA_4 _Saveframe_category NMR_applied_experiment _Experiment_name HNCOCA _Sample_label $Samples_3_and_5_again save_ save_CBCACONH_5 _Saveframe_category NMR_applied_experiment _Experiment_name CBCACONH _Sample_label $Samples_3_and_5_again2 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*_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 HNCACB 1H-1H-15N_NOESY-HSQC stop_ loop_ _Sample_label $sample_1 $sample_2 $All_samples $Samples_1_and_3_and_5 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 175.954 0.2 1 2 2 9 GLU CA C 56.604 0.2 1 3 2 9 GLU CB C 29.911 0.2 1 4 3 10 LEU H H 8.096 0.01 1 5 3 10 LEU C C 176.953 0.2 1 6 3 10 LEU CA C 54.785 0.2 1 7 3 10 LEU CB C 41.244 0.2 1 8 3 10 LEU N N 123.506 0.1 1 9 4 11 LYS H H 7.694 0.01 1 10 4 11 LYS C C 176.204 0.2 1 11 4 11 LYS CA C 55.841 0.2 1 12 4 11 LYS CB C 33.562 0.2 1 13 4 11 LYS N N 122.331 0.1 1 14 5 12 ASN H H 8.542 0.01 1 15 5 12 ASN C C 174.968 0.2 1 16 5 12 ASN CA C 55.758 0.2 1 17 5 12 ASN CB C 40.510 0.2 1 18 5 12 ASN N N 116.676 0.1 1 19 6 13 SER H H 8.143 0.01 1 20 6 13 SER C C 175.148 0.2 1 21 6 13 SER CA C 56.788 0.2 1 22 6 13 SER CB C 65.970 0.2 1 23 6 13 SER N N 112.236 0.1 1 24 7 14 ILE H H 9.336 0.01 1 25 7 14 ILE C C 175.514 0.2 1 26 7 14 ILE CA C 64.947 0.2 1 27 7 14 ILE CB C 37.109 0.2 1 28 7 14 ILE N N 126.322 0.1 1 29 8 15 SER H H 7.499 0.01 1 30 8 15 SER C C 174.307 0.2 1 31 8 15 SER CA C 59.486 0.2 1 32 8 15 SER CB C 63.272 0.2 1 33 8 15 SER N N 112.560 0.1 1 34 9 16 ASP H H 7.797 0.01 1 35 9 16 ASP C C 176.015 0.2 1 36 9 16 ASP CA C 55.224 0.2 1 37 9 16 ASP CB C 43.277 0.2 1 38 9 16 ASP N N 118.003 0.1 1 39 10 17 TYR H H 8.291 0.01 1 40 10 17 TYR C C 177.512 0.2 1 41 10 17 TYR CA C 58.612 0.2 1 42 10 17 TYR CB C 41.144 0.2 1 43 10 17 TYR N N 120.697 0.1 1 44 11 18 THR H H 8.809 0.01 1 45 11 18 THR C C 176.191 0.2 1 46 11 18 THR CA C 60.817 0.2 1 47 11 18 THR CB C 71.059 0.2 1 48 11 18 THR N N 112.249 0.1 1 49 12 19 GLU H H 9.177 0.01 1 50 12 19 GLU C C 178.445 0.2 1 51 12 19 GLU CA C 60.890 0.2 1 52 12 19 GLU CB C 29.458 0.2 1 53 12 19 GLU N N 122.255 0.1 1 54 13 20 ALA H H 8.350 0.01 1 55 13 20 ALA C C 181.835 0.2 1 56 13 20 ALA CA C 55.389 0.2 1 57 13 20 ALA CB C 18.427 0.2 1 58 13 20 ALA N N 118.781 0.1 1 59 14 21 GLU H H 8.030 0.01 1 60 14 21 GLU C C 179.623 0.2 1 61 14 21 GLU CA C 58.937 0.2 1 62 14 21 GLU CB C 31.660 0.2 1 63 14 21 GLU N N 119.109 0.1 1 64 15 22 PHE H H 8.639 0.01 1 65 15 22 PHE C C 177.528 0.2 1 66 15 22 PHE CA C 62.234 0.2 1 67 15 22 PHE CB C 40.526 0.2 1 68 15 22 PHE N N 124.944 0.1 1 69 16 23 VAL H H 8.658 0.01 1 70 16 23 VAL C C 177.895 0.2 1 71 16 23 VAL CA C 67.894 0.2 1 72 16 23 VAL CB C 31.590 0.2 1 73 16 23 VAL N N 119.945 0.1 1 74 17 24 GLN H H 7.586 0.01 1 75 17 24 GLN C C 178.352 0.2 1 76 17 24 GLN CA C 59.323 0.2 1 77 17 24 GLN CB C 27.816 0.2 1 78 17 24 GLN N N 117.802 0.1 1 79 18 25 LEU H H 7.503 0.01 1 80 18 25 LEU C C 178.464 0.2 1 81 18 25 LEU CA C 58.644 0.2 1 82 18 25 LEU CB C 40.533 0.2 1 83 18 25 LEU N N 122.243 0.1 1 84 19 26 LEU H H 7.745 0.01 1 85 19 26 LEU C C 180.136 0.2 1 86 19 26 LEU CA C 57.875 0.2 1 87 19 26 LEU CB C 40.937 0.2 1 88 19 26 LEU N N 118.942 0.1 1 89 20 27 LYS H H 8.392 0.01 1 90 20 27 LYS C C 179.575 0.2 1 91 20 27 LYS CA C 59.604 0.2 1 92 20 27 LYS CB C 31.914 0.2 1 93 20 27 LYS N N 120.914 0.1 1 94 21 28 GLU H H 8.145 0.01 1 95 21 28 GLU C C 179.161 0.2 1 96 21 28 GLU CA C 59.517 0.2 1 97 21 28 GLU CB C 29.050 0.2 1 98 21 28 GLU N N 122.826 0.1 1 99 22 29 ILE H H 8.048 0.01 1 100 22 29 ILE C C 177.129 0.2 1 101 22 29 ILE CA C 66.517 0.2 1 102 22 29 ILE CB C 38.066 0.2 1 103 22 29 ILE N N 120.644 0.1 1 104 23 30 GLU H H 7.798 0.01 1 105 23 30 GLU C C 179.208 0.2 1 106 23 30 GLU CA C 59.391 0.2 1 107 23 30 GLU CB C 29.796 0.2 1 108 23 30 GLU N N 118.955 0.1 1 109 24 31 LYS H H 7.677 0.01 1 110 24 31 LYS C C 179.485 0.2 1 111 24 31 LYS CA C 59.260 0.2 1 112 24 31 LYS CB C 32.687 0.2 1 113 24 31 LYS N N 119.147 0.1 1 114 25 32 GLU H H 8.237 0.01 1 115 25 32 GLU C C 178.133 0.2 1 116 25 32 GLU CA C 57.513 0.2 1 117 25 32 GLU CB C 29.436 0.2 1 118 25 32 GLU N N 118.919 0.1 1 119 26 33 ASN H H 8.394 0.01 1 120 26 33 ASN C C 176.744 0.2 1 121 26 33 ASN CA C 55.696 0.2 1 122 26 33 ASN CB C 39.242 0.2 1 123 26 33 ASN N N 118.706 0.1 1 124 27 34 VAL H H 7.343 0.01 1 125 27 34 VAL C C 176.259 0.2 1 126 27 34 VAL CA C 62.284 0.2 1 127 27 34 VAL CB C 31.915 0.2 1 128 27 34 VAL N N 112.963 0.1 1 129 28 35 ALA H H 7.541 0.01 1 130 28 35 ALA C C 177.291 0.2 1 131 28 35 ALA CA C 52.683 0.2 1 132 28 35 ALA CB C 20.138 0.2 1 133 28 35 ALA N N 124.454 0.1 1 134 29 36 ALA H H 8.447 0.01 1 135 29 36 ALA C C 178.102 0.2 1 136 29 36 ALA CA C 53.922 0.2 1 137 29 36 ALA CB C 19.263 0.2 1 138 29 36 ALA N N 121.744 0.1 1 139 30 37 THR H H 8.016 0.01 1 140 30 37 THR C C 174.692 0.2 1 141 30 37 THR CA C 60.418 0.2 1 142 30 37 THR CB C 70.635 0.2 1 143 30 37 THR N N 109.500 0.1 1 144 31 38 ASP H H 8.501 0.01 1 145 31 38 ASP C C 175.975 0.2 1 146 31 38 ASP CA C 54.562 0.2 1 147 31 38 ASP CB C 41.255 0.2 1 148 31 38 ASP N N 121.759 0.1 1 149 32 39 ASP H H 8.297 0.01 1 150 32 39 ASP C C 177.823 0.2 1 151 32 39 ASP CA C 56.958 0.2 1 152 32 39 ASP CB C 40.783 0.2 1 153 32 39 ASP N N 118.710 0.1 1 154 33 40 VAL H H 7.996 0.01 1 155 33 40 VAL C C 177.577 0.2 1 156 33 40 VAL CA C 65.328 0.2 1 157 33 40 VAL CB C 32.058 0.2 1 158 33 40 VAL N N 119.685 0.1 1 159 34 41 LEU H H 8.595 0.01 1 160 34 41 LEU C C 177.689 0.2 1 161 34 41 LEU CA C 58.536 0.2 1 162 34 41 LEU CB C 41.643 0.2 1 163 34 41 LEU N N 122.166 0.1 1 164 35 42 ASP H H 8.277 0.01 1 165 35 42 ASP C C 179.453 0.2 1 166 35 42 ASP CA C 58.127 0.2 1 167 35 42 ASP CB C 40.631 0.2 1 168 35 42 ASP N N 115.768 0.1 1 169 36 43 VAL H H 7.248 0.01 1 170 36 43 VAL C C 179.380 0.2 1 171 36 43 VAL CA C 66.118 0.2 1 172 36 43 VAL CB C 32.253 0.2 1 173 36 43 VAL N N 119.772 0.1 1 174 37 44 LEU H H 8.120 0.01 1 175 37 44 LEU C C 179.622 0.2 1 176 37 44 LEU CA C 58.124 0.2 1 177 37 44 LEU CB C 42.301 0.2 1 178 37 44 LEU N N 120.634 0.1 1 179 38 45 LEU H H 9.008 0.01 1 180 38 45 LEU C C 179.380 0.2 1 181 38 45 LEU CA C 58.068 0.2 1 182 38 45 LEU CB C 41.563 0.2 1 183 38 45 LEU N N 118.941 0.1 1 184 39 46 GLU H H 7.968 0.01 1 185 39 46 GLU C C 179.029 0.2 1 186 39 46 GLU CA C 59.793 0.2 1 187 39 46 GLU CB C 29.604 0.2 1 188 39 46 GLU N N 119.797 0.1 1 189 40 47 HIS H H 8.013 0.01 1 190 40 47 HIS C C 176.073 0.2 1 191 40 47 HIS CA C 60.085 0.2 1 192 40 47 HIS CB C 30.358 0.2 1 193 40 47 HIS N N 119.803 0.1 1 194 41 48 PHE H H 8.787 0.01 1 195 41 48 PHE C C 178.015 0.2 1 196 41 48 PHE CA C 62.785 0.2 1 197 41 48 PHE CB C 39.742 0.2 1 198 41 48 PHE N N 118.402 0.1 1 199 42 49 VAL H H 8.372 0.01 1 200 42 49 VAL C C 178.290 0.2 1 201 42 49 VAL CA C 67.280 0.2 1 202 42 49 VAL CB C 32.326 0.2 1 203 42 49 VAL N N 121.032 0.1 1 204 43 50 LYS H H 8.077 0.01 1 205 43 50 LYS CA C 59.557 0.2 1 206 43 50 LYS CB C 32.919 0.2 1 207 43 50 LYS N N 121.003 0.1 1 208 44 51 ILE C C 178.162 0.2 1 209 44 51 ILE CA C 62.040 0.2 1 210 44 51 ILE CB C 37.299 0.2 1 211 45 52 THR H H 7.551 0.01 1 212 45 52 THR C C 176.300 0.2 1 213 45 52 THR CA C 65.732 0.2 1 214 45 52 THR CB C 69.648 0.2 1 215 45 52 THR N N 109.421 0.1 1 216 46 53 GLU H H 7.272 0.01 1 217 46 53 GLU C C 173.427 0.2 1 218 46 53 GLU CA C 57.661 0.2 1 219 46 53 GLU CB C 29.099 0.2 1 220 46 53 GLU N N 113.929 0.1 1 221 47 54 HIS H H 7.095 0.01 1 222 47 54 HIS CA C 55.784 0.2 1 223 47 54 HIS CB C 32.309 0.2 1 224 47 54 HIS N N 119.649 0.1 1 225 48 55 PRO C C 177.895 0.2 1 226 48 55 PRO CA C 64.769 0.2 1 227 48 55 PRO CB C 32.268 0.2 1 228 49 56 ASP H H 10.753 0.01 1 229 49 56 ASP C C 177.764 0.2 1 230 49 56 ASP CA C 55.403 0.2 1 231 49 56 ASP CB C 40.784 0.2 1 232 49 56 ASP N N 121.302 0.1 1 233 50 57 GLY H H 8.011 0.01 1 234 50 57 GLY C C 175.505 0.2 1 235 50 57 GLY CA C 47.325 0.2 1 236 50 57 GLY N N 107.990 0.1 1 237 51 58 THR H H 9.182 0.01 1 238 51 58 THR C C 176.565 0.2 1 239 51 58 THR CA C 64.711 0.2 1 240 51 58 THR CB C 68.134 0.2 1 241 51 58 THR N N 114.603 0.1 1 242 52 59 ASP H H 8.709 0.01 1 243 52 59 ASP C C 177.745 0.2 1 244 52 59 ASP CA C 57.750 0.2 1 245 52 59 ASP CB C 39.374 0.2 1 246 52 59 ASP N N 125.873 0.1 1 247 53 60 LEU H H 7.274 0.01 1 248 53 60 LEU C C 177.408 0.2 1 249 53 60 LEU CA C 57.642 0.2 1 250 53 60 LEU CB C 43.805 0.2 1 251 53 60 LEU N N 115.706 0.1 1 252 54 61 ILE H H 6.957 0.01 1 253 54 61 ILE C C 177.302 0.2 1 254 54 61 ILE CA C 62.904 0.2 1 255 54 61 ILE CB C 39.451 0.2 1 256 54 61 ILE N N 113.534 0.1 1 257 55 62 TYR H H 7.149 0.01 1 258 55 62 TYR C C 175.381 0.2 1 259 55 62 TYR CA C 60.847 0.2 1 260 55 62 TYR CB C 40.179 0.2 1 261 55 62 TYR N N 114.578 0.1 1 262 56 63 TYR H H 8.535 0.01 1 263 56 63 TYR CA C 55.645 0.2 1 264 56 63 TYR CB C 39.298 0.2 1 265 56 63 TYR N N 118.274 0.1 1 266 57 64 PRO C C 177.447 0.2 1 267 57 64 PRO CA C 63.124 0.2 1 268 57 64 PRO CB C 32.470 0.2 1 269 58 65 SER H H 8.566 0.01 1 270 58 65 SER C C 174.884 0.2 1 271 58 65 SER CA C 58.207 0.2 1 272 58 65 SER CB C 64.416 0.2 1 273 58 65 SER N N 116.772 0.1 1 274 59 66 ASP H H 8.522 0.01 1 275 59 66 ASP C C 176.514 0.2 1 276 59 66 ASP CA C 55.559 0.2 1 277 59 66 ASP CB C 40.861 0.2 1 278 59 66 ASP N N 121.743 0.1 1 279 60 67 ASN H H 8.299 0.01 1 280 60 67 ASN C C 174.269 0.2 1 281 60 67 ASN CA C 53.606 0.2 1 282 60 67 ASN CB C 38.710 0.2 1 283 60 67 ASN N N 115.647 0.1 1 284 61 68 ARG H H 7.593 0.01 1 285 61 68 ARG C C 175.052 0.2 1 286 61 68 ARG CA C 54.955 0.2 1 287 61 68 ARG CB C 31.940 0.2 1 288 61 68 ARG N N 116.975 0.1 1 289 62 69 ASP H H 8.526 0.01 1 290 62 69 ASP C C 175.931 0.2 1 291 62 69 ASP CA C 54.897 0.2 1 292 62 69 ASP CB C 41.628 0.2 1 293 62 69 ASP N N 121.058 0.1 1 294 63 70 ASP H H 8.566 0.01 1 295 63 70 ASP C C 174.620 0.2 1 296 63 70 ASP CA C 52.908 0.2 1 297 63 70 ASP CB C 39.481 0.2 1 298 63 70 ASP N N 123.903 0.1 1 299 64 71 SER H H 7.937 0.01 1 300 64 71 SER CA C 56.518 0.2 1 301 64 71 SER CB C 63.814 0.2 1 302 64 71 SER N N 117.162 0.1 1 303 65 72 PRO C C 177.748 0.2 1 304 65 72 PRO CA C 65.944 0.2 1 305 65 72 PRO CB C 32.856 0.2 1 306 66 73 GLU H H 9.000 0.01 1 307 66 73 GLU C C 179.662 0.2 1 308 66 73 GLU CA C 61.311 0.2 1 309 66 73 GLU CB C 28.591 0.2 1 310 66 73 GLU N N 115.944 0.1 1 311 67 74 GLY H H 8.432 0.01 1 312 67 74 GLY C C 176.520 0.2 1 313 67 74 GLY CA C 47.031 0.2 1 314 67 74 GLY N N 111.602 0.1 1 315 68 75 ILE H H 8.231 0.01 1 316 68 75 ILE C C 178.230 0.2 1 317 68 75 ILE CA C 66.220 0.2 1 318 68 75 ILE CB C 38.113 0.2 1 319 68 75 ILE N N 124.137 0.1 1 320 69 76 VAL H H 8.304 0.01 1 321 69 76 VAL C C 177.120 0.2 1 322 69 76 VAL CA C 68.238 0.2 1 323 69 76 VAL CB C 31.658 0.2 1 324 69 76 VAL N N 118.860 0.1 1 325 70 77 LYS H H 7.971 0.01 1 326 70 77 LYS C C 178.189 0.2 1 327 70 77 LYS CA C 60.515 0.2 1 328 70 77 LYS CB C 32.732 0.2 1 329 70 77 LYS N N 120.029 0.1 1 330 71 78 GLU H H 7.757 0.01 1 331 71 78 GLU C C 179.578 0.2 1 332 71 78 GLU CA C 59.763 0.2 1 333 71 78 GLU CB C 28.957 0.2 1 334 71 78 GLU N N 119.167 0.1 1 335 72 79 ILE H H 8.544 0.01 1 336 72 79 ILE C C 177.658 0.2 1 337 72 79 ILE CA C 65.836 0.2 1 338 72 79 ILE CB C 38.170 0.2 1 339 72 79 ILE N N 119.097 0.1 1 340 73 80 LYS H H 9.206 0.01 1 341 73 80 LYS C C 180.285 0.2 1 342 73 80 LYS CA C 60.279 0.2 1 343 73 80 LYS CB C 33.336 0.2 1 344 73 80 LYS N N 119.989 0.1 1 345 74 81 GLU H H 8.510 0.01 1 346 74 81 GLU C C 179.240 0.2 1 347 74 81 GLU CA C 59.624 0.2 1 348 74 81 GLU CB C 29.647 0.2 1 349 74 81 GLU N N 119.199 0.1 1 350 75 82 TRP H H 8.785 0.01 1 351 75 82 TRP C C 179.837 0.2 1 352 75 82 TRP CA C 63.198 0.2 1 353 75 82 TRP CB C 29.418 0.2 1 354 75 82 TRP N N 122.430 0.1 1 355 76 83 ARG H H 9.140 0.01 1 356 76 83 ARG C C 178.169 0.2 1 357 76 83 ARG CA C 60.935 0.2 1 358 76 83 ARG CB C 28.646 0.2 1 359 76 83 ARG N N 118.530 0.1 1 360 77 84 ALA H H 7.796 0.01 1 361 77 84 ALA C C 181.486 0.2 1 362 77 84 ALA CA C 55.266 0.2 1 363 77 84 ALA CB C 18.275 0.2 1 364 77 84 ALA N N 120.372 0.1 1 365 78 85 ALA H H 7.944 0.01 1 366 78 85 ALA C C 178.352 0.2 1 367 78 85 ALA CA C 54.249 0.2 1 368 78 85 ALA CB C 18.363 0.2 1 369 78 85 ALA N N 120.621 0.1 1 370 79 86 ASN H H 7.041 0.01 1 371 79 86 ASN C C 174.157 0.2 1 372 79 86 ASN CA C 53.333 0.2 1 373 79 86 ASN CB C 39.399 0.2 1 374 79 86 ASN N N 113.486 0.1 1 375 80 87 GLY H H 7.559 0.01 1 376 80 87 GLY C C 174.494 0.2 1 377 80 87 GLY CA C 47.257 0.2 1 378 80 87 GLY N N 108.358 0.1 1 379 81 88 LYS H H 8.062 0.01 1 380 81 88 LYS CA C 53.359 0.2 1 381 81 88 LYS CB C 32.704 0.2 1 382 81 88 LYS N N 119.309 0.1 1 383 82 89 PRO C C 176.742 0.2 1 384 82 89 PRO CA C 63.399 0.2 1 385 82 89 PRO CB C 32.926 0.2 1 386 83 90 GLY H H 8.371 0.01 1 387 83 90 GLY C C 173.425 0.2 1 388 83 90 GLY CA C 43.413 0.2 1 389 83 90 GLY N N 110.587 0.1 1 390 84 91 PHE H H 7.833 0.01 1 391 84 91 PHE C C 177.031 0.2 1 392 84 91 PHE CA C 59.265 0.2 1 393 84 91 PHE CB C 40.004 0.2 1 394 84 91 PHE N N 116.323 0.1 1 395 85 92 LYS H H 8.575 0.01 1 396 85 92 LYS C C 176.586 0.2 1 397 85 92 LYS CA C 57.295 0.2 1 398 85 92 LYS CB C 32.912 0.2 1 399 85 92 LYS N N 123.774 0.1 1 400 86 93 GLN H H 8.658 0.01 1 401 86 93 GLN C C 175.407 0.2 1 402 86 93 GLN CA C 56.540 0.2 1 403 86 93 GLN CB C 29.760 0.2 1 404 86 93 GLN N N 125.163 0.1 1 405 87 94 GLY H H 8.065 0.01 1 406 87 94 GLY CA C 46.302 0.2 1 407 87 94 GLY N N 116.814 0.1 1 stop_ save_