data_5190 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Backbone NMR assignments of Ribosome Recycling Factors from Escherichia coli ; _BMRB_accession_number 5190 _BMRB_flat_file_name bmr5190.str _Entry_type original _Submission_date 2001-10-30 _Accession_date 2001-10-30 _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 Yoshida Takuya . . 2 Kijima Hiroyuki . . 3 Oka Shinichiro . . 4 Uchiyama Susumu . . 5 Nakano Hiroaki . . 6 Ohkubo Tadayasu . . 7 Kobayashi Yuji . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 175 "13C chemical shifts" 366 "15N chemical shifts" 175 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2002-05-07 original author . stop_ _Original_release_date 2002-05-07 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; Letter to the Editor: Backbone NMR Assignments of Ribosome Recycling Factors from Escherichia coli and Thermotoga maritima ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code 21880670 _PubMed_ID 11883785 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Yoshida Takuya . . 2 Kijima Hiroyuki . . 3 Oka Shinichiro . . 4 Uchiyama Susumu . . 5 Nakano Hiroaki . . 6 Ohkubo Tadayasu . . 7 Kobayashi Yuji . . stop_ _Journal_abbreviation 'J. Biomol. NMR' _Journal_volume 22 _Journal_issue 2 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 195 _Page_last 196 _Year 2002 _Details . save_ ################################## # Molecular system description # ################################## save_system_RRF _Saveframe_category molecular_system _Mol_system_name 'ribosome recycling factor' _Abbreviation_common RRF _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'ribosome recycling factor' $RRF stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state monomer _System_paramagnetic no _System_thiol_state 'all free' _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_RRF _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'ribosome recycling factor' _Abbreviation_common RRF _Molecular_mass . _Mol_thiol_state 'all free' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 185 _Mol_residue_sequence ; MISDIRKDAEVRMDKCVEAF KTQISKIRTGRASPSLLDGI VVEYYGTPTPLRQLASVTVE DSRTLKINVFDRSMSPAVEK AIMASDLGLNPNSAGSDIRV PLPPLTEERRKDLTKIVRGE AEQARVAVRNVRRDANDKVK ALLKDKEISEDDDRRSQDDV QKLTDAAIKKIEAALADKEA ELMQF ; loop_ _Residue_seq_code _Residue_label 1 MET 2 ILE 3 SER 4 ASP 5 ILE 6 ARG 7 LYS 8 ASP 9 ALA 10 GLU 11 VAL 12 ARG 13 MET 14 ASP 15 LYS 16 CYS 17 VAL 18 GLU 19 ALA 20 PHE 21 LYS 22 THR 23 GLN 24 ILE 25 SER 26 LYS 27 ILE 28 ARG 29 THR 30 GLY 31 ARG 32 ALA 33 SER 34 PRO 35 SER 36 LEU 37 LEU 38 ASP 39 GLY 40 ILE 41 VAL 42 VAL 43 GLU 44 TYR 45 TYR 46 GLY 47 THR 48 PRO 49 THR 50 PRO 51 LEU 52 ARG 53 GLN 54 LEU 55 ALA 56 SER 57 VAL 58 THR 59 VAL 60 GLU 61 ASP 62 SER 63 ARG 64 THR 65 LEU 66 LYS 67 ILE 68 ASN 69 VAL 70 PHE 71 ASP 72 ARG 73 SER 74 MET 75 SER 76 PRO 77 ALA 78 VAL 79 GLU 80 LYS 81 ALA 82 ILE 83 MET 84 ALA 85 SER 86 ASP 87 LEU 88 GLY 89 LEU 90 ASN 91 PRO 92 ASN 93 SER 94 ALA 95 GLY 96 SER 97 ASP 98 ILE 99 ARG 100 VAL 101 PRO 102 LEU 103 PRO 104 PRO 105 LEU 106 THR 107 GLU 108 GLU 109 ARG 110 ARG 111 LYS 112 ASP 113 LEU 114 THR 115 LYS 116 ILE 117 VAL 118 ARG 119 GLY 120 GLU 121 ALA 122 GLU 123 GLN 124 ALA 125 ARG 126 VAL 127 ALA 128 VAL 129 ARG 130 ASN 131 VAL 132 ARG 133 ARG 134 ASP 135 ALA 136 ASN 137 ASP 138 LYS 139 VAL 140 LYS 141 ALA 142 LEU 143 LEU 144 LYS 145 ASP 146 LYS 147 GLU 148 ILE 149 SER 150 GLU 151 ASP 152 ASP 153 ASP 154 ARG 155 ARG 156 SER 157 GLN 158 ASP 159 ASP 160 VAL 161 GLN 162 LYS 163 LEU 164 THR 165 ASP 166 ALA 167 ALA 168 ILE 169 LYS 170 LYS 171 ILE 172 GLU 173 ALA 174 ALA 175 LEU 176 ALA 177 ASP 178 LYS 179 GLU 180 ALA 181 GLU 182 LEU 183 MET 184 GLN 185 PHE stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2014-11-16 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 1EK8 "Crystal Structure Of The Ribosome Recycling Factor (Rrf) From Escherichia Coli" 100.00 185 100.00 100.00 7.26e-127 PDB 1ISE "Crystal Structure Of A Mutant Of Ribosome Recycling Factor From Escherichia Coli, Arg132gly" 100.00 185 99.46 99.46 1.12e-125 PDB 1ZN0 "Coordinates Of Rrf And Ef-G Fitted Into Cryo-Em Map Of The 50s Subunit Bound With Both Ef-G (Gdpnp) And Rrf" 100.00 185 100.00 100.00 7.26e-127 PDB 1ZN1 "Coordinates Of Rrf Fitted Into Cryo-Em Map Of The 70s Post- Termination Complex" 100.00 185 100.00 100.00 7.26e-127 PDB 2RDO "50s Subunit With Ef-G(Gdpnp) And Rrf Bound" 100.00 185 100.00 100.00 7.26e-127 PDB 4GAS "Allosteric Control Of The Ribosome By Small-Molecule Antibiotics" 100.00 185 100.00 100.00 7.26e-127 PDB 4GD1 "Structures Of The Bacterial Ribosome In Classical And Hybrid States Of Trna Binding" 98.38 183 100.00 100.00 9.73e-124 DBJ BAA02599 "ribosome releasing factor (FRR) [Escherichia coli]" 100.00 185 100.00 100.00 7.26e-127 DBJ BAB33597 "ribosome releasing factor [Escherichia coli O157:H7 str. Sakai]" 100.00 185 100.00 100.00 7.26e-127 DBJ BAB96748 "ribosome recycling factor [Escherichia coli str. K-12 substr. W3110]" 100.00 185 100.00 100.00 7.26e-127 DBJ BAG75695 "ribosome releasing factor [Escherichia coli SE11]" 100.00 185 100.00 100.00 7.26e-127 DBJ BAI23533 "ribosome recycling factor [Escherichia coli O26:H11 str. 11368]" 100.00 185 100.00 100.00 7.26e-127 EMBL CAP74741 "ribosome recycling factor [Escherichia coli LF82]" 100.00 185 100.00 100.00 7.26e-127 EMBL CAQ30686 "ribosome recycling factor [Escherichia coli BL21(DE3)]" 100.00 185 100.00 100.00 7.26e-127 EMBL CAQ87775 "ribosome recycling factor [Escherichia fergusonii ATCC 35469]" 100.00 185 100.00 100.00 7.26e-127 EMBL CAQ97058 "ribosome recycling factor [Escherichia coli IAI1]" 100.00 185 100.00 100.00 7.26e-127 EMBL CAR01547 "ribosome recycling factor [Escherichia coli S88]" 100.00 185 100.00 100.00 7.26e-127 GB AAA24607 "ribosome releasing factor (gtg start codon) [Escherichia coli]" 100.00 185 100.00 100.00 7.26e-127 GB AAB08601 "ribosome release factor [Escherichia coli]" 100.00 185 100.00 100.00 7.26e-127 GB AAC73283 "ribosome recycling factor [Escherichia coli str. K-12 substr. MG1655]" 100.00 185 100.00 100.00 7.26e-127 GB AAG54474 "ribosome releasing factor [Escherichia coli O157:H7 str. EDL933]" 100.00 185 100.00 100.00 7.26e-127 GB AAN41824 "ribosome releasing factor [Shigella flexneri 2a str. 301]" 100.00 185 100.00 100.00 7.26e-127 REF NP_285866 "ribosome recycling factor [Escherichia coli O157:H7 str. EDL933]" 100.00 185 100.00 100.00 7.26e-127 REF NP_308201 "ribosome recycling factor [Escherichia coli O157:H7 str. Sakai]" 100.00 185 100.00 100.00 7.26e-127 REF NP_414714 "ribosome recycling factor [Escherichia coli str. K-12 substr. MG1655]" 100.00 185 100.00 100.00 7.26e-127 REF NP_706117 "ribosome recycling factor [Shigella flexneri 2a str. 301]" 100.00 185 100.00 100.00 7.26e-127 REF NP_752158 "ribosome recycling factor [Escherichia coli CFT073]" 100.00 185 100.00 100.00 7.26e-127 SP A7ZHR2 "RecName: Full=Ribosome-recycling factor; Short=RRF; AltName: Full=Ribosome-releasing factor [Escherichia coli E24377A]" 100.00 185 100.00 100.00 7.26e-127 SP A7ZWB8 "RecName: Full=Ribosome-recycling factor; Short=RRF; AltName: Full=Ribosome-releasing factor [Escherichia coli HS]" 100.00 185 100.00 100.00 7.26e-127 SP B1IQG9 "RecName: Full=Ribosome-recycling factor; Short=RRF; AltName: Full=Ribosome-releasing factor [Escherichia coli ATCC 8739]" 100.00 185 100.00 100.00 7.26e-127 SP B1LGX4 "RecName: Full=Ribosome-recycling factor; Short=RRF; AltName: Full=Ribosome-releasing factor [Escherichia coli SMS-3-5]" 100.00 185 100.00 100.00 7.26e-127 SP B1XD41 "RecName: Full=Ribosome-recycling factor; Short=RRF; AltName: Full=Ribosome-releasing factor [Escherichia coli str. K-12 substr." 100.00 185 100.00 100.00 7.26e-127 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $RRF 'E. coli' 562 Eubacteria . 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 $RRF 'recombinant technology' . . . . . 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 $RRF 0.5 mM . stop_ save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model INOVA _Field_strength 600 _Details . save_ ####################### # Sample conditions # ####################### save_Ex-cond_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 5.0 0.1 n/a temperature 298 0.1 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 DSS H 1 'methyl protons' ppm 0.0 internal direct . . . 1.0 DSS N 15 'methyl protons' ppm 0.0 . indirect . . . 0.101329118 DSS C 13 'methyl protons' ppm 0.0 . indirect . . . 0.251449530 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 . loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $Ex-cond_1 _Chem_shift_reference_set_label $chemical_shift_reference _Mol_system_component_name 'ribosome recycling factor' _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 ILE C C 177.54 0.05 1 2 . 2 ILE CA C 65.62 0.05 1 3 . 3 SER H H 8.55 0.01 1 4 . 3 SER C C 176.58 0.05 1 5 . 3 SER CA C 60.72 0.05 1 6 . 3 SER N N 114.96 0.05 1 7 . 4 ASP H H 7.41 0.01 1 8 . 4 ASP C C 178.19 0.05 1 9 . 4 ASP CA C 56.64 0.05 1 10 . 4 ASP N N 120.92 0.05 1 11 . 5 ILE H H 7.51 0.01 1 12 . 5 ILE C C 178.56 0.05 1 13 . 5 ILE CA C 64.19 0.05 1 14 . 5 ILE N N 122.28 0.05 1 15 . 6 ARG H H 8.25 0.01 1 16 . 6 ARG C C 177.85 0.05 1 17 . 6 ARG CA C 59.52 0.05 1 18 . 6 ARG N N 120.76 0.05 1 19 . 7 LYS H H 7.85 0.01 1 20 . 7 LYS C C 178.24 0.05 1 21 . 7 LYS CA C 58.66 0.05 1 22 . 7 LYS N N 119.01 0.05 1 23 . 8 ASP H H 7.83 0.01 1 24 . 8 ASP C C 177.92 0.05 1 25 . 8 ASP CA C 56.76 0.05 1 26 . 8 ASP N N 118.00 0.05 1 27 . 9 ALA H H 8.20 0.01 1 28 . 9 ALA C C 178.76 0.05 1 29 . 9 ALA CA C 54.47 0.05 1 30 . 9 ALA N N 120.36 0.05 1 31 . 10 GLU H H 8.34 0.01 1 32 . 10 GLU C C 179.00 0.05 1 33 . 10 GLU CA C 59.54 0.05 1 34 . 10 GLU N N 118.63 0.05 1 35 . 11 VAL H H 8.17 0.01 1 36 . 11 VAL C C 179.60 0.05 1 37 . 11 VAL CA C 65.62 0.05 1 38 . 11 VAL N N 119.08 0.05 1 39 . 12 ARG H H 8.46 0.01 1 40 . 12 ARG C C 180.82 0.05 1 41 . 12 ARG CA C 59.90 0.05 1 42 . 12 ARG N N 119.07 0.05 1 43 . 13 MET H H 9.03 0.01 1 44 . 13 MET C C 178.04 0.05 1 45 . 13 MET CA C 61.25 0.05 1 46 . 13 MET N N 119.81 0.05 1 47 . 14 ASP H H 8.26 0.01 1 48 . 14 ASP C C 179.18 0.05 1 49 . 14 ASP CA C 57.42 0.05 1 50 . 14 ASP N N 119.94 0.05 1 51 . 15 LYS H H 8.13 0.01 1 52 . 15 LYS C C 179.99 0.05 1 53 . 15 LYS CA C 59.16 0.05 1 54 . 15 LYS N N 119.18 0.05 1 55 . 16 CYS H H 7.85 0.01 1 56 . 16 CYS C C 178.16 0.05 1 57 . 16 CYS CA C 62.86 0.05 1 58 . 16 CYS N N 119.01 0.05 1 59 . 17 VAL H H 7.98 0.01 1 60 . 17 VAL C C 178.08 0.05 1 61 . 17 VAL CA C 66.70 0.05 1 62 . 17 VAL N N 121.34 0.05 1 63 . 18 GLU H H 8.62 0.01 1 64 . 18 GLU C C 179.20 0.05 1 65 . 18 GLU CA C 58.68 0.05 1 66 . 18 GLU N N 119.10 0.05 1 67 . 19 ALA H H 8.41 0.01 1 68 . 19 ALA C C 180.45 0.05 1 69 . 19 ALA CA C 54.83 0.05 1 70 . 19 ALA N N 122.10 0.05 1 71 . 20 PHE H H 7.55 0.01 1 72 . 20 PHE C C 176.58 0.05 1 73 . 20 PHE CA C 59.41 0.05 1 74 . 20 PHE N N 119.56 0.05 1 75 . 21 LYS H H 8.34 0.01 1 76 . 21 LYS C C 180.04 0.05 1 77 . 21 LYS CA C 59.90 0.05 1 78 . 21 LYS N N 118.63 0.05 1 79 . 22 THR H H 8.66 0.01 1 80 . 22 THR C C 177.17 0.05 1 81 . 22 THR CA C 66.22 0.05 1 82 . 22 THR N N 117.26 0.05 1 83 . 23 GLN H H 8.11 0.01 1 84 . 23 GLN C C 180.55 0.05 1 85 . 23 GLN CA C 59.20 0.05 1 86 . 23 GLN N N 122.86 0.05 1 87 . 24 ILE H H 8.14 0.01 1 88 . 24 ILE C C 178.37 0.05 1 89 . 24 ILE CA C 63.93 0.05 1 90 . 24 ILE N N 112.75 0.05 1 91 . 25 SER H H 7.59 0.01 1 92 . 25 SER C C 175.10 0.05 1 93 . 25 SER CA C 60.34 0.05 1 94 . 25 SER N N 117.84 0.05 1 95 . 26 LYS H H 7.07 0.01 1 96 . 26 LYS C C 176.41 0.05 1 97 . 26 LYS CA C 55.96 0.05 1 98 . 26 LYS N N 118.13 0.05 1 99 . 27 ILE H H 7.14 0.01 1 100 . 27 ILE C C 175.04 0.05 1 101 . 27 ILE CA C 59.97 0.05 1 102 . 27 ILE N N 119.89 0.05 1 103 . 28 ARG H H 8.48 0.01 1 104 . 28 ARG C C 175.58 0.05 1 105 . 28 ARG CA C 55.37 0.05 1 106 . 28 ARG N N 129.13 0.05 1 107 . 29 THR H H 8.30 0.01 1 108 . 29 THR C C 174.44 0.05 1 109 . 29 THR CA C 60.45 0.05 1 110 . 29 THR N N 113.39 0.05 1 111 . 30 GLY H H 8.59 0.01 1 112 . 30 GLY C C 173.31 0.05 1 113 . 30 GLY CA C 44.98 0.05 1 114 . 30 GLY N N 108.01 0.05 1 115 . 31 ARG H H 7.80 0.01 1 116 . 31 ARG C C 176.00 0.05 1 117 . 31 ARG CA C 54.69 0.05 1 118 . 31 ARG N N 119.69 0.05 1 119 . 32 ALA H H 8.50 0.01 1 120 . 32 ALA C C 175.71 0.05 1 121 . 32 ALA CA C 52.73 0.05 1 122 . 32 ALA N N 126.53 0.05 1 123 . 33 SER H H 7.11 0.01 1 124 . 33 SER C C 173.43 0.05 1 125 . 33 SER CA C 54.36 0.05 1 126 . 33 SER N N 114.90 0.05 1 127 . 34 PRO C C 176.98 0.05 1 128 . 34 PRO CA C 64.65 0.05 1 129 . 35 SER H H 7.74 0.01 1 130 . 35 SER C C 176.19 0.05 1 131 . 35 SER CA C 59.22 0.05 1 132 . 35 SER N N 111.05 0.05 1 133 . 36 LEU H H 7.55 0.01 1 134 . 36 LEU C C 177.40 0.05 1 135 . 36 LEU CA C 57.11 0.05 1 136 . 36 LEU N N 122.94 0.05 1 137 . 37 LEU H H 7.52 0.01 1 138 . 37 LEU C C 177.18 0.05 1 139 . 37 LEU CA C 52.90 0.05 1 140 . 37 LEU N N 111.97 0.05 1 141 . 38 ASP H H 7.55 0.01 1 142 . 38 ASP C C 177.36 0.05 1 143 . 38 ASP CA C 56.68 0.05 1 144 . 38 ASP N N 119.56 0.05 1 145 . 39 GLY H H 8.71 0.01 1 146 . 39 GLY C C 174.44 0.05 1 147 . 39 GLY CA C 44.45 0.05 1 148 . 39 GLY N N 107.72 0.05 1 149 . 40 ILE H H 7.32 0.01 1 150 . 40 ILE C C 175.52 0.05 1 151 . 40 ILE CA C 60.30 0.05 1 152 . 40 ILE N N 120.70 0.05 1 153 . 41 VAL H H 8.50 0.01 1 154 . 41 VAL C C 174.24 0.05 1 155 . 41 VAL CA C 60.05 0.05 1 156 . 41 VAL N N 127.12 0.05 1 157 . 42 VAL H H 8.92 0.01 1 158 . 42 VAL C C 175.37 0.05 1 159 . 42 VAL CA C 59.51 0.05 1 160 . 42 VAL N N 123.90 0.05 1 161 . 43 GLU H H 8.74 0.01 1 162 . 43 GLU C C 174.58 0.05 1 163 . 43 GLU CA C 56.77 0.05 1 164 . 43 GLU N N 127.76 0.05 1 165 . 44 TYR H H 8.18 0.01 1 166 . 44 TYR C C 174.57 0.05 1 167 . 44 TYR CA C 56.06 0.05 1 168 . 44 TYR N N 128.55 0.05 1 169 . 45 TYR H H 8.86 0.01 1 170 . 45 TYR C C 176.53 0.05 1 171 . 45 TYR CA C 59.23 0.05 1 172 . 45 TYR N N 126.69 0.05 1 173 . 46 GLY H H 8.33 0.01 1 174 . 46 GLY C C 174.35 0.05 1 175 . 46 GLY CA C 44.99 0.05 1 176 . 46 GLY N N 102.83 0.05 1 177 . 47 THR H H 7.76 0.01 1 178 . 47 THR C C 173.42 0.05 1 179 . 47 THR CA C 59.35 0.05 1 180 . 47 THR N N 117.16 0.05 1 181 . 48 PRO C C 176.05 0.05 1 182 . 48 PRO CA C 63.17 0.05 1 183 . 49 THR H H 9.17 0.01 1 184 . 49 THR C C 171.03 0.05 1 185 . 49 THR CA C 60.37 0.05 1 186 . 49 THR N N 126.44 0.05 1 187 . 50 PRO C C 177.50 0.05 1 188 . 50 PRO CA C 63.06 0.05 1 189 . 51 LEU H H 8.11 0.01 1 190 . 51 LEU C C 178.20 0.05 1 191 . 51 LEU CA C 58.44 0.05 1 192 . 51 LEU N N 124.25 0.05 1 193 . 52 ARG H H 8.71 0.01 1 194 . 52 ARG C C 176.87 0.05 1 195 . 52 ARG CA C 57.41 0.05 1 196 . 52 ARG N N 113.23 0.05 1 197 . 53 GLN H H 7.78 0.01 1 198 . 53 GLN C C 176.16 0.05 1 199 . 53 GLN CA C 56.36 0.05 1 200 . 53 GLN N N 115.39 0.05 1 201 . 54 LEU H H 7.80 0.01 1 202 . 54 LEU C C 175.00 0.05 1 203 . 54 LEU CA C 53.84 0.05 1 204 . 54 LEU N N 116.89 0.05 1 205 . 55 ALA H H 7.51 0.01 1 206 . 55 ALA C C 174.63 0.05 1 207 . 55 ALA CA C 50.09 0.05 1 208 . 55 ALA N N 122.28 0.05 1 209 . 56 SER H H 8.05 0.01 1 210 . 56 SER C C 174.21 0.05 1 211 . 56 SER CA C 55.94 0.05 1 212 . 56 SER N N 113.25 0.05 1 213 . 57 VAL H H 8.55 0.01 1 214 . 57 VAL C C 175.05 0.05 1 215 . 57 VAL CA C 61.02 0.05 1 216 . 57 VAL N N 126.30 0.05 1 217 . 58 THR H H 9.14 0.01 1 218 . 58 THR C C 173.03 0.05 1 219 . 58 THR CA C 59.18 0.05 1 220 . 58 THR N N 118.52 0.05 1 221 . 59 VAL H H 8.66 0.01 1 222 . 59 VAL C C 175.79 0.05 1 223 . 59 VAL CA C 62.18 0.05 1 224 . 59 VAL N N 121.50 0.05 1 225 . 60 GLU H H 8.58 0.01 1 226 . 60 GLU C C 176.16 0.05 1 227 . 60 GLU CA C 56.92 0.05 1 228 . 60 GLU N N 130.02 0.05 1 229 . 61 ASP H H 8.39 0.01 1 230 . 61 ASP C C 175.52 0.05 1 231 . 61 ASP CA C 53.06 0.05 1 232 . 61 ASP N N 116.07 0.05 1 233 . 62 SER H H 8.40 0.01 1 234 . 62 SER C C 174.38 0.05 1 235 . 62 SER CA C 61.25 0.05 1 236 . 62 SER N N 109.23 0.05 1 237 . 63 ARG H H 8.37 0.01 1 238 . 63 ARG C C 175.18 0.05 1 239 . 63 ARG CA C 55.03 0.05 1 240 . 63 ARG N N 117.96 0.05 1 241 . 64 THR H H 7.61 0.01 1 242 . 64 THR C C 173.83 0.05 1 243 . 64 THR CA C 62.55 0.05 1 244 . 64 THR N N 116.44 0.05 1 245 . 65 LEU H H 8.37 0.01 1 246 . 65 LEU C C 174.76 0.05 1 247 . 65 LEU CA C 52.74 0.05 1 248 . 65 LEU N N 125.59 0.05 1 249 . 66 LYS H H 9.22 0.01 1 250 . 66 LYS C C 174.20 0.05 1 251 . 66 LYS CA C 54.75 0.05 1 252 . 66 LYS N N 122.92 0.05 1 253 . 67 ILE H H 9.39 0.01 1 254 . 67 ILE C C 174.41 0.05 1 255 . 67 ILE CA C 59.46 0.05 1 256 . 67 ILE N N 126.90 0.05 1 257 . 68 ASN H H 8.67 0.01 1 258 . 68 ASN C C 173.84 0.05 1 259 . 68 ASN CA C 51.85 0.05 1 260 . 68 ASN N N 126.32 0.05 1 261 . 69 VAL H H 8.65 0.01 1 262 . 69 VAL C C 176.45 0.05 1 263 . 69 VAL CA C 61.54 0.05 1 264 . 69 VAL N N 123.93 0.05 1 265 . 70 PHE H H 7.80 0.01 1 266 . 70 PHE C C 176.60 0.05 1 267 . 70 PHE CA C 58.39 0.05 1 268 . 70 PHE N N 125.03 0.05 1 269 . 71 ASP H H 8.83 0.01 1 270 . 71 ASP C C 176.76 0.05 1 271 . 71 ASP CA C 51.59 0.05 1 272 . 71 ASP N N 119.05 0.05 1 273 . 72 ARG H H 8.89 0.01 1 274 . 72 ARG C C 178.86 0.05 1 275 . 72 ARG CA C 58.76 0.05 1 276 . 72 ARG N N 124.71 0.05 1 277 . 73 SER H H 8.63 0.01 1 278 . 73 SER C C 176.02 0.05 1 279 . 73 SER CA C 60.72 0.05 1 280 . 73 SER N N 115.95 0.05 1 281 . 74 MET H H 8.31 0.01 1 282 . 74 MET C C 177.07 0.05 1 283 . 74 MET CA C 53.63 0.05 1 284 . 74 MET N N 118.63 0.05 1 285 . 75 SER H H 7.72 0.01 1 286 . 75 SER C C 173.21 0.05 1 287 . 75 SER CA C 64.10 0.05 1 288 . 75 SER N N 115.76 0.05 1 289 . 76 PRO C C 179.39 0.05 1 290 . 76 PRO CA C 65.87 0.05 1 291 . 77 ALA H H 7.57 0.01 1 292 . 77 ALA C C 181.35 0.05 1 293 . 77 ALA CA C 54.53 0.05 1 294 . 77 ALA N N 119.77 0.05 1 295 . 78 VAL H H 8.23 0.01 1 296 . 78 VAL C C 177.12 0.05 1 297 . 78 VAL CA C 66.35 0.05 1 298 . 78 VAL N N 120.22 0.05 1 299 . 79 GLU H H 8.55 0.01 1 300 . 79 GLU C C 178.24 0.05 1 301 . 79 GLU CA C 60.44 0.05 1 302 . 79 GLU N N 119.19 0.05 1 303 . 80 LYS H H 8.16 0.01 1 304 . 80 LYS C C 178.76 0.05 1 305 . 80 LYS CA C 59.04 0.05 1 306 . 80 LYS N N 117.64 0.05 1 307 . 81 ALA H H 7.80 0.01 1 308 . 81 ALA C C 180.78 0.05 1 309 . 81 ALA CA C 54.35 0.05 1 310 . 81 ALA N N 121.36 0.05 1 311 . 82 ILE H H 8.05 0.01 1 312 . 82 ILE C C 179.07 0.05 1 313 . 82 ILE CA C 64.76 0.05 1 314 . 82 ILE N N 117.26 0.05 1 315 . 83 MET H H 8.23 0.01 1 316 . 83 MET C C 176.99 0.05 1 317 . 83 MET CA C 58.53 0.05 1 318 . 83 MET N N 120.21 0.05 1 319 . 84 ALA H H 7.91 0.01 1 320 . 84 ALA C C 177.97 0.05 1 321 . 84 ALA CA C 52.28 0.05 1 322 . 84 ALA N N 118.54 0.05 1 323 . 85 SER H H 7.26 0.01 1 324 . 85 SER C C 174.53 0.05 1 325 . 85 SER CA C 59.02 0.05 1 326 . 85 SER N N 113.42 0.05 1 327 . 86 ASP H H 8.45 0.01 1 328 . 86 ASP C C 176.40 0.05 1 329 . 86 ASP CA C 54.34 0.05 1 330 . 86 ASP N N 120.80 0.05 1 331 . 87 LEU H H 7.88 0.01 1 332 . 87 LEU C C 177.80 0.05 1 333 . 87 LEU CA C 55.49 0.05 1 334 . 87 LEU N N 118.43 0.05 1 335 . 88 GLY H H 8.06 0.01 1 336 . 88 GLY C C 174.20 0.05 1 337 . 88 GLY CA C 46.21 0.05 1 338 . 88 GLY N N 107.83 0.05 1 339 . 89 LEU H H 7.99 0.01 1 340 . 89 LEU C C 175.85 0.05 1 341 . 89 LEU CA C 52.97 0.05 1 342 . 89 LEU N N 118.41 0.05 1 343 . 90 ASN H H 8.94 0.01 1 344 . 90 ASN C C 172.44 0.05 1 345 . 90 ASN CA C 50.07 0.05 1 346 . 90 ASN N N 119.31 0.05 1 347 . 91 PRO C C 175.22 0.05 1 348 . 91 PRO CA C 61.80 0.05 1 349 . 92 ASN H H 8.95 0.01 1 350 . 92 ASN C C 174.22 0.05 1 351 . 92 ASN CA C 52.28 0.05 1 352 . 92 ASN N N 117.38 0.05 1 353 . 93 SER H H 8.79 0.01 1 354 . 93 SER C C 173.67 0.05 1 355 . 93 SER CA C 57.51 0.05 1 356 . 93 SER N N 118.48 0.05 1 357 . 94 ALA H H 8.45 0.01 1 358 . 94 ALA C C 177.37 0.05 1 359 . 94 ALA CA C 51.55 0.05 1 360 . 94 ALA N N 127.46 0.05 1 361 . 95 GLY H H 8.72 0.01 1 362 . 95 GLY C C 175.01 0.05 1 363 . 95 GLY CA C 46.02 0.05 1 364 . 95 GLY N N 112.44 0.05 1 365 . 96 SER H H 8.86 0.01 1 366 . 96 SER C C 173.16 0.05 1 367 . 96 SER CA C 58.80 0.05 1 368 . 96 SER N N 120.85 0.05 1 369 . 97 ASP H H 7.90 0.01 1 370 . 97 ASP C C 175.19 0.05 1 371 . 97 ASP CA C 53.25 0.05 1 372 . 97 ASP N N 119.91 0.05 1 373 . 98 ILE H H 8.61 0.01 1 374 . 98 ILE C C 174.94 0.05 1 375 . 98 ILE CA C 60.26 0.05 1 376 . 98 ILE N N 121.89 0.05 1 377 . 99 ARG H H 8.92 0.01 1 378 . 99 ARG C C 175.63 0.05 1 379 . 99 ARG CA C 54.28 0.05 1 380 . 99 ARG N N 126.53 0.05 1 381 . 100 VAL H H 9.02 0.01 1 382 . 100 VAL C C 172.42 0.05 1 383 . 100 VAL CA C 58.41 0.05 1 384 . 100 VAL N N 121.18 0.05 1 385 . 101 PRO C C 176.45 0.05 1 386 . 101 PRO CA C 61.26 0.05 1 387 . 102 LEU H H 8.80 0.01 1 388 . 102 LEU C C 175.22 0.05 1 389 . 102 LEU CA C 51.24 0.05 1 390 . 102 LEU N N 124.62 0.05 1 391 . 104 PRO C C 177.38 0.05 1 392 . 104 PRO CA C 61.89 0.05 1 393 . 105 LEU H H 8.81 0.01 1 394 . 105 LEU C C 177.79 0.05 1 395 . 105 LEU CA C 54.55 0.05 1 396 . 105 LEU N N 122.92 0.05 1 397 . 106 THR H H 7.66 0.01 1 398 . 106 THR C C 175.24 0.05 1 399 . 106 THR CA C 60.07 0.05 1 400 . 106 THR N N 112.94 0.05 1 401 . 107 GLU H H 9.00 0.01 1 402 . 107 GLU C C 178.98 0.05 1 403 . 107 GLU CA C 59.23 0.05 1 404 . 107 GLU N N 121.63 0.05 1 405 . 108 GLU H H 8.70 0.01 1 406 . 108 GLU C C 178.56 0.05 1 407 . 108 GLU CA C 59.29 0.05 1 408 . 108 GLU N N 117.84 0.05 1 409 . 109 ARG H H 7.70 0.01 1 410 . 109 ARG C C 178.63 0.05 1 411 . 109 ARG CA C 57.84 0.05 1 412 . 109 ARG N N 119.72 0.05 1 413 . 110 ARG H H 8.60 0.01 1 414 . 110 ARG C C 179.76 0.05 1 415 . 110 ARG CA C 60.34 0.05 1 416 . 110 ARG N N 119.45 0.05 1 417 . 111 LYS H H 8.19 0.01 1 418 . 111 LYS C C 179.57 0.05 1 419 . 111 LYS CA C 59.67 0.05 1 420 . 111 LYS N N 120.70 0.05 1 421 . 112 ASP H H 8.14 0.01 1 422 . 112 ASP C C 179.17 0.05 1 423 . 112 ASP CA C 57.22 0.05 1 424 . 112 ASP N N 121.58 0.05 1 425 . 113 LEU H H 8.74 0.01 1 426 . 113 LEU C C 179.07 0.05 1 427 . 113 LEU CA C 57.35 0.05 1 428 . 113 LEU N N 118.80 0.05 1 429 . 114 THR H H 8.14 0.01 1 430 . 114 THR C C 175.82 0.05 1 431 . 114 THR CA C 67.01 0.05 1 432 . 114 THR N N 116.08 0.05 1 433 . 115 LYS H H 7.61 0.01 1 434 . 115 LYS C C 180.25 0.05 1 435 . 115 LYS CA C 59.76 0.05 1 436 . 115 LYS N N 121.24 0.05 1 437 . 116 ILE H H 7.93 0.01 1 438 . 116 ILE C C 179.62 0.05 1 439 . 116 ILE CA C 64.69 0.05 1 440 . 116 ILE N N 120.83 0.05 1 441 . 117 VAL H H 8.44 0.01 1 442 . 117 VAL C C 178.37 0.05 1 443 . 117 VAL CA C 65.70 0.05 1 444 . 117 VAL N N 117.94 0.05 1 445 . 118 ARG H H 8.34 0.01 1 446 . 118 ARG C C 180.39 0.05 1 447 . 118 ARG CA C 60.17 0.05 1 448 . 118 ARG N N 120.42 0.05 1 449 . 119 GLY H H 8.33 0.01 1 450 . 119 GLY C C 177.18 0.05 1 451 . 119 GLY CA C 46.73 0.05 1 452 . 119 GLY N N 109.57 0.05 1 453 . 120 GLU H H 8.41 0.01 1 454 . 120 GLU C C 179.58 0.05 1 455 . 120 GLU CA C 58.36 0.05 1 456 . 120 GLU N N 122.55 0.05 1 457 . 121 ALA H H 8.59 0.01 1 458 . 121 ALA C C 178.81 0.05 1 459 . 121 ALA CA C 54.41 0.05 1 460 . 121 ALA N N 124.44 0.05 1 461 . 122 GLU H H 7.77 0.01 1 462 . 122 GLU C C 178.36 0.05 1 463 . 122 GLU CA C 58.50 0.05 1 464 . 122 GLU N N 118.61 0.05 1 465 . 123 GLN H H 7.80 0.01 1 466 . 123 GLN C C 178.93 0.05 1 467 . 123 GLN CA C 58.43 0.05 1 468 . 123 GLN N N 116.89 0.05 1 469 . 124 ALA H H 7.71 0.01 1 470 . 124 ALA C C 178.73 0.05 1 471 . 124 ALA CA C 54.48 0.05 1 472 . 124 ALA N N 123.09 0.05 1 473 . 125 ARG H H 8.37 0.01 1 474 . 125 ARG C C 178.83 0.05 1 475 . 125 ARG CA C 60.20 0.05 1 476 . 125 ARG N N 117.95 0.05 1 477 . 126 VAL H H 8.33 0.01 1 478 . 126 VAL C C 178.23 0.05 1 479 . 126 VAL CA C 65.98 0.05 1 480 . 126 VAL N N 118.98 0.05 1 481 . 127 ALA H H 7.96 0.01 1 482 . 127 ALA C C 181.45 0.05 1 483 . 127 ALA CA C 55.21 0.05 1 484 . 127 ALA N N 122.32 0.05 1 485 . 128 VAL H H 8.35 0.01 1 486 . 128 VAL C C 178.45 0.05 1 487 . 128 VAL CA C 67.05 0.05 1 488 . 128 VAL N N 119.55 0.05 1 489 . 129 ARG H H 8.45 0.01 1 490 . 129 ARG C C 179.62 0.05 1 491 . 129 ARG CA C 59.94 0.05 1 492 . 129 ARG N N 119.59 0.05 1 493 . 130 ASN H H 8.66 0.01 1 494 . 130 ASN C C 177.82 0.05 1 495 . 130 ASN CA C 55.32 0.05 1 496 . 130 ASN N N 121.49 0.05 1 497 . 131 VAL H H 7.80 0.01 1 498 . 131 VAL C C 177.85 0.05 1 499 . 131 VAL CA C 66.26 0.05 1 500 . 131 VAL N N 122.76 0.05 1 501 . 132 ARG H H 7.66 0.01 1 502 . 132 ARG C C 176.72 0.05 1 503 . 132 ARG CA C 58.97 0.05 1 504 . 132 ARG N N 120.13 0.05 1 505 . 133 ARG H H 7.78 0.01 1 506 . 133 ARG C C 178.08 0.05 1 507 . 133 ARG CA C 58.71 0.05 1 508 . 133 ARG N N 117.87 0.05 1 509 . 134 ASP H H 7.98 0.01 1 510 . 134 ASP C C 178.26 0.05 1 511 . 134 ASP CA C 57.03 0.05 1 512 . 134 ASP N N 118.79 0.05 1 513 . 135 ALA H H 8.54 0.01 1 514 . 135 ALA C C 179.13 0.05 1 515 . 135 ALA CA C 54.82 0.05 1 516 . 135 ALA N N 121.45 0.05 1 517 . 136 ASN H H 8.47 0.01 1 518 . 136 ASN C C 179.54 0.05 1 519 . 136 ASN CA C 54.99 0.05 1 520 . 136 ASN N N 115.72 0.05 1 521 . 137 ASP H H 8.63 0.01 1 522 . 137 ASP C C 179.59 0.05 1 523 . 137 ASP CA C 57.16 0.05 1 524 . 137 ASP N N 122.04 0.05 1 525 . 138 LYS H H 8.17 0.01 1 526 . 138 LYS C C 179.97 0.05 1 527 . 138 LYS CA C 59.43 0.05 1 528 . 138 LYS N N 122.57 0.05 1 529 . 139 VAL H H 8.11 0.01 1 530 . 139 VAL C C 178.07 0.05 1 531 . 139 VAL CA C 66.94 0.05 1 532 . 139 VAL N N 121.39 0.05 1 533 . 140 LYS H H 8.26 0.01 1 534 . 140 LYS C C 179.75 0.05 1 535 . 140 LYS CA C 57.89 0.05 1 536 . 140 LYS N N 119.65 0.05 1 537 . 141 ALA H H 7.70 0.01 1 538 . 141 ALA C C 180.22 0.05 1 539 . 141 ALA CA C 54.79 0.05 1 540 . 141 ALA N N 121.72 0.05 1 541 . 142 LEU H H 7.40 0.01 1 542 . 142 LEU C C 179.53 0.05 1 543 . 142 LEU CA C 57.08 0.05 1 544 . 142 LEU N N 117.94 0.05 1 545 . 143 LEU H H 7.90 0.01 1 546 . 143 LEU C C 181.11 0.05 1 547 . 143 LEU CA C 57.53 0.05 1 548 . 143 LEU N N 121.04 0.05 1 549 . 144 LYS H H 8.43 0.01 1 550 . 144 LYS C C 177.87 0.05 1 551 . 144 LYS CA C 58.90 0.05 1 552 . 144 LYS N N 122.91 0.05 1 553 . 145 ASP H H 7.50 0.01 1 554 . 145 ASP C C 174.61 0.05 1 555 . 145 ASP CA C 53.47 0.05 1 556 . 145 ASP N N 115.84 0.05 1 557 . 146 LYS H H 8.18 0.01 1 558 . 146 LYS C C 176.42 0.05 1 559 . 146 LYS CA C 57.05 0.05 1 560 . 146 LYS N N 114.14 0.05 1 561 . 147 GLU H H 8.47 0.01 1 562 . 147 GLU C C 176.22 0.05 1 563 . 147 GLU CA C 57.20 0.05 1 564 . 147 GLU N N 115.72 0.05 1 565 . 148 ILE H H 7.16 0.01 1 566 . 148 ILE C C 173.78 0.05 1 567 . 148 ILE CA C 58.30 0.05 1 568 . 148 ILE N N 108.86 0.05 1 569 . 149 SER H H 9.10 0.01 1 570 . 149 SER C C 175.74 0.05 1 571 . 149 SER CA C 56.08 0.05 1 572 . 149 SER N N 116.02 0.05 1 573 . 150 GLU H H 9.09 0.01 1 574 . 150 GLU C C 179.21 0.05 1 575 . 150 GLU CA C 59.58 0.05 1 576 . 150 GLU N N 120.40 0.05 1 577 . 151 ASP H H 8.33 0.01 1 578 . 151 ASP C C 178.20 0.05 1 579 . 151 ASP CA C 57.12 0.05 1 580 . 151 ASP N N 119.40 0.05 1 581 . 152 ASP H H 7.93 0.01 1 582 . 152 ASP C C 178.97 0.05 1 583 . 152 ASP CA C 56.90 0.05 1 584 . 152 ASP N N 120.41 0.05 1 585 . 153 ASP H H 7.84 0.01 1 586 . 153 ASP C C 176.94 0.05 1 587 . 153 ASP CA C 57.06 0.05 1 588 . 153 ASP N N 120.42 0.05 1 589 . 154 ARG H H 8.08 0.01 1 590 . 154 ARG C C 179.19 0.05 1 591 . 154 ARG CA C 59.54 0.05 1 592 . 154 ARG N N 119.74 0.05 1 593 . 155 ARG H H 8.22 0.01 1 594 . 155 ARG C C 178.86 0.05 1 595 . 155 ARG CA C 58.96 0.05 1 596 . 155 ARG N N 118.84 0.05 1 597 . 156 SER H H 8.10 0.01 1 598 . 156 SER C C 177.17 0.05 1 599 . 156 SER CA C 60.93 0.05 1 600 . 156 SER N N 113.97 0.05 1 601 . 157 GLN H H 8.40 0.01 1 602 . 157 GLN C C 180.19 0.05 1 603 . 157 GLN CA C 59.34 0.05 1 604 . 157 GLN N N 119.37 0.05 1 605 . 158 ASP H H 7.77 0.01 1 606 . 158 ASP C C 178.32 0.05 1 607 . 158 ASP CA C 57.07 0.05 1 608 . 158 ASP N N 120.68 0.05 1 609 . 159 ASP H H 8.36 0.01 1 610 . 159 ASP C C 179.75 0.05 1 611 . 159 ASP CA C 57.36 0.05 1 612 . 159 ASP N N 121.71 0.05 1 613 . 160 VAL H H 9.14 0.01 1 614 . 160 VAL C C 179.75 0.05 1 615 . 160 VAL CA C 66.06 0.05 1 616 . 160 VAL N N 120.09 0.05 1 617 . 161 GLN H H 8.66 0.01 1 618 . 161 GLN C C 177.60 0.05 1 619 . 161 GLN CA C 58.69 0.05 1 620 . 161 GLN N N 125.92 0.05 1 621 . 162 LYS H H 8.11 0.01 1 622 . 162 LYS C C 180.91 0.05 1 623 . 162 LYS CA C 59.70 0.05 1 624 . 162 LYS N N 120.10 0.05 1 625 . 163 LEU H H 7.78 0.01 1 626 . 163 LEU C C 179.31 0.05 1 627 . 163 LEU CA C 57.56 0.05 1 628 . 163 LEU N N 119.92 0.05 1 629 . 164 THR H H 8.08 0.01 1 630 . 164 THR C C 175.81 0.05 1 631 . 164 THR CA C 66.73 0.05 1 632 . 164 THR N N 118.65 0.05 1 633 . 165 ASP H H 8.69 0.01 1 634 . 165 ASP C C 179.16 0.05 1 635 . 165 ASP CA C 56.95 0.05 1 636 . 165 ASP N N 120.84 0.05 1 637 . 166 ALA H H 7.89 0.01 1 638 . 166 ALA C C 180.20 0.05 1 639 . 166 ALA CA C 54.58 0.05 1 640 . 166 ALA N N 121.48 0.05 1 641 . 167 ALA H H 8.06 0.01 1 642 . 167 ALA C C 180.00 0.05 1 643 . 167 ALA CA C 55.05 0.05 1 644 . 167 ALA N N 122.47 0.05 1 645 . 168 ILE H H 8.70 0.01 1 646 . 168 ILE C C 178.56 0.05 1 647 . 168 ILE CA C 63.94 0.05 1 648 . 168 ILE N N 117.84 0.05 1 649 . 169 LYS H H 8.18 0.01 1 650 . 169 LYS C C 179.93 0.05 1 651 . 169 LYS CA C 59.75 0.05 1 652 . 169 LYS N N 119.88 0.05 1 653 . 170 LYS H H 7.67 0.01 1 654 . 170 LYS C C 180.95 0.05 1 655 . 170 LYS CA C 59.79 0.05 1 656 . 170 LYS N N 119.08 0.05 1 657 . 171 ILE H H 8.06 0.01 1 658 . 171 ILE C C 177.24 0.05 1 659 . 171 ILE CA C 65.54 0.05 1 660 . 171 ILE N N 122.47 0.05 1 661 . 172 GLU H H 8.77 0.01 1 662 . 172 GLU C C 180.02 0.05 1 663 . 172 GLU CA C 58.47 0.05 1 664 . 172 GLU N N 117.68 0.05 1 665 . 173 ALA H H 8.34 0.01 1 666 . 173 ALA C C 179.78 0.05 1 667 . 173 ALA CA C 54.55 0.05 1 668 . 173 ALA N N 122.75 0.05 1 669 . 174 ALA H H 7.77 0.01 1 670 . 174 ALA C C 180.89 0.05 1 671 . 174 ALA CA C 54.18 0.05 1 672 . 174 ALA N N 120.68 0.05 1 673 . 175 LEU H H 8.93 0.01 1 674 . 175 LEU C C 177.38 0.05 1 675 . 175 LEU CA C 58.00 0.05 1 676 . 175 LEU N N 120.51 0.05 1 677 . 176 ALA H H 8.36 0.01 1 678 . 176 ALA C C 181.52 0.05 1 679 . 176 ALA CA C 54.74 0.05 1 680 . 176 ALA N N 120.96 0.05 1 681 . 177 ASP H H 7.99 0.01 1 682 . 177 ASP C C 178.56 0.05 1 683 . 177 ASP CA C 56.72 0.05 1 684 . 177 ASP N N 118.41 0.05 1 685 . 178 LYS H H 7.89 0.01 1 686 . 178 LYS C C 178.73 0.05 1 687 . 178 LYS CA C 56.18 0.05 1 688 . 178 LYS N N 121.47 0.05 1 689 . 179 GLU H H 9.11 0.01 1 690 . 179 GLU C C 179.01 0.05 1 691 . 179 GLU CA C 60.30 0.05 1 692 . 179 GLU N N 118.29 0.05 1 693 . 180 ALA H H 7.93 0.01 1 694 . 180 ALA C C 180.58 0.05 1 695 . 180 ALA CA C 54.72 0.05 1 696 . 180 ALA N N 120.40 0.05 1 697 . 181 GLU H H 7.72 0.01 1 698 . 181 GLU C C 179.52 0.05 1 699 . 181 GLU CA C 58.89 0.05 1 700 . 181 GLU N N 119.18 0.05 1 701 . 182 LEU H H 8.09 0.01 1 702 . 182 LEU C C 177.38 0.05 1 703 . 182 LEU CA C 56.63 0.05 1 704 . 182 LEU N N 117.97 0.05 1 705 . 183 MET H H 7.59 0.01 1 706 . 183 MET C C 176.95 0.05 1 707 . 183 MET CA C 55.42 0.05 1 708 . 183 MET N N 114.52 0.05 1 709 . 184 GLN H H 7.61 0.01 1 710 . 184 GLN C C 174.98 0.05 1 711 . 184 GLN CA C 56.06 0.05 1 712 . 184 GLN N N 118.00 0.05 1 713 . 185 PHE H H 7.67 0.01 1 714 . 185 PHE C C 180.15 0.05 1 715 . 185 PHE CA C 58.94 0.05 1 716 . 185 PHE N N 124.98 0.05 1 stop_ save_