data_5362 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; 1H, 15N and 13C Backbone resonance assignments of the 40 kDa LicT-CAT-PRD1 protein ; _BMRB_accession_number 5362 _BMRB_flat_file_name bmr5362.str _Entry_type original _Submission_date 2002-05-03 _Accession_date 2002-05-03 _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 Ducat Thierry . . 2 Declerck Nathalie . . 3 Kochoyan Michel . . 4 Demene Helene . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 161 "13C chemical shifts" 481 "15N chemical shifts" 161 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2002-09-25 original author . stop_ _Original_release_date 2002-09-25 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; Letter to the Editor: 1H, 15N and 13C Backbone resonance assignments of the 40 kDa LicT-CAT-PRD1 protein ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID ? loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Ducat Thierry . . 2 Declerck Nathalie . . 3 Kochoyan Michel . . 4 Demene Helene . . stop_ _Journal_abbreviation 'J. Biomol. NMR' _Journal_volume 23 _Journal_issue 4 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 325 _Page_last 326 _Year 2002 _Details . loop_ _Keyword LicT 'Resonance assignments' 'Transcriptional antiterminator' stop_ save_ ################################## # Molecular system description # ################################## save_system_CAT-PRD1 _Saveframe_category molecular_system _Mol_system_name 'CAT-PRD1 domain of the transcriptional antiterminator LicT protein from Bacillus subtilis' _Abbreviation_common CAT-PRD1 _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'CAT-PRD1 subunit 1' $CAT-PRD1 'CAT-PRD1 subunit 2' $CAT-PRD1 stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state dimer _System_paramagnetic no _System_thiol_state 'all free' loop_ _Magnetic_equivalence_ID _Magnetically_equivalent_system_component 1 'CAT-PRD1 subunit 1' 1 'CAT-PRD1 subunit 2' stop_ loop_ _Biological_function 'Transcriptional antiterminator' stop_ _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_CAT-PRD1 _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'LicT CAT-PRD1' _Abbreviation_common CAT-PRD1 _Molecular_mass 19925.9 _Mol_thiol_state 'all free' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 175 _Mol_residue_sequence ; MKIAKVINNNVISVVNEQGK ELVVMGRGLAFQKKSGDDVD EARIEKVFTLDNKDVSEKFK TLLYDIPIECMEVSEEIISY AKLQLGKKLNDSIYVSLTDH INFAIQRNQKGLDIKNALLW ETKRLYKDEFAIGKEALVMV KNKTGVSLPEDEAGFIALHI VNAELNELQHHHHHH ; loop_ _Residue_seq_code _Residue_label 1 MET 2 LYS 3 ILE 4 ALA 5 LYS 6 VAL 7 ILE 8 ASN 9 ASN 10 ASN 11 VAL 12 ILE 13 SER 14 VAL 15 VAL 16 ASN 17 GLU 18 GLN 19 GLY 20 LYS 21 GLU 22 LEU 23 VAL 24 VAL 25 MET 26 GLY 27 ARG 28 GLY 29 LEU 30 ALA 31 PHE 32 GLN 33 LYS 34 LYS 35 SER 36 GLY 37 ASP 38 ASP 39 VAL 40 ASP 41 GLU 42 ALA 43 ARG 44 ILE 45 GLU 46 LYS 47 VAL 48 PHE 49 THR 50 LEU 51 ASP 52 ASN 53 LYS 54 ASP 55 VAL 56 SER 57 GLU 58 LYS 59 PHE 60 LYS 61 THR 62 LEU 63 LEU 64 TYR 65 ASP 66 ILE 67 PRO 68 ILE 69 GLU 70 CYS 71 MET 72 GLU 73 VAL 74 SER 75 GLU 76 GLU 77 ILE 78 ILE 79 SER 80 TYR 81 ALA 82 LYS 83 LEU 84 GLN 85 LEU 86 GLY 87 LYS 88 LYS 89 LEU 90 ASN 91 ASP 92 SER 93 ILE 94 TYR 95 VAL 96 SER 97 LEU 98 THR 99 ASP 100 HIS 101 ILE 102 ASN 103 PHE 104 ALA 105 ILE 106 GLN 107 ARG 108 ASN 109 GLN 110 LYS 111 GLY 112 LEU 113 ASP 114 ILE 115 LYS 116 ASN 117 ALA 118 LEU 119 LEU 120 TRP 121 GLU 122 THR 123 LYS 124 ARG 125 LEU 126 TYR 127 LYS 128 ASP 129 GLU 130 PHE 131 ALA 132 ILE 133 GLY 134 LYS 135 GLU 136 ALA 137 LEU 138 VAL 139 MET 140 VAL 141 LYS 142 ASN 143 LYS 144 THR 145 GLY 146 VAL 147 SER 148 LEU 149 PRO 150 GLU 151 ASP 152 GLU 153 ALA 154 GLY 155 PHE 156 ILE 157 ALA 158 LEU 159 HIS 160 ILE 161 VAL 162 ASN 163 ALA 164 GLU 165 LEU 166 ASN 167 GLU 168 LEU 169 GLN 170 HIS 171 HIS 172 HIS 173 HIS 174 HIS 175 HIS stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-01-28 loop_ _Database_name _Database_accession_code _Database_entry_mol_name _Sequence_query_to_submitted_percentage _Sequence_subject_length _Sequence_identity _Sequence_positive _Sequence_homology_expectation_value PDB 1H99 "Prd Of Lict Antiterminator From Bacillus Subtilis" 63.43 224 100.00 100.00 1.21e-71 PDB 1TLV "Structure Of The Native And Inactive Lict Prd From B. Subtilis" 63.43 221 99.10 99.10 8.34e-70 DBJ BAA11696 "LicT antiterminator [Bacillus subtilis]" 95.43 277 99.40 99.40 1.45e-112 DBJ BAI87589 "BglG family transcriptional antiterminator [Bacillus subtilis subsp. natto BEST195]" 95.43 277 100.00 100.00 1.22e-113 DBJ BAM55992 "transcriptional antiterminator BglG family [Bacillus subtilis BEST7613]" 95.43 277 100.00 100.00 1.22e-113 DBJ BAM60004 "transcriptional antiterminator BglG family [Bacillus subtilis BEST7003]" 95.43 277 100.00 100.00 1.22e-113 DBJ GAK81310 "transcriptional antiterminator [Bacillus subtilis Miyagi-4]" 95.43 277 100.00 100.00 1.22e-113 EMBL CAA82194 "antiterminator [Bacillus subtilis]" 95.43 277 100.00 100.00 1.22e-113 EMBL CAB15944 "transcriptional antiterminator (BglG family) [Bacillus subtilis subsp. subtilis str. 168]" 95.43 277 100.00 100.00 1.22e-113 EMBL CCF07176 "Transcription antiterminator licT [Bacillus amyloliquefaciens subsp. plantarum CAU B946]" 62.86 229 97.27 100.00 1.14e-69 EMBL CCU57030 "Beta-glucoside bgl operon antiterminator, BglG family [Bacillus subtilis E1]" 95.43 277 100.00 100.00 1.13e-113 EMBL CEI59719 "transcription antiterminator LicT [Bacillus subtilis]" 95.43 277 100.00 100.00 1.22e-113 GB ADM39914 "transcriptional antiterminator (BglG family) protein [Bacillus subtilis subsp. spizizenii str. W23]" 95.43 277 97.60 98.80 6.12e-111 GB ADV94733 "transcriptional antiterminator (BglG family) protein [Bacillus subtilis BSn5]" 95.43 277 100.00 100.00 1.22e-113 GB AEP88876 "transcription antiterminator LicT [Bacillus subtilis subsp. spizizenii TU-B-10]" 95.43 277 97.60 98.80 7.20e-111 GB AEP92976 "transcription antiterminator LicT [Bacillus subtilis subsp. subtilis str. RO-NN-1]" 95.43 277 100.00 100.00 1.22e-113 GB AFI30559 "transcriptional antiterminator BglG family [Bacillus sp. JS]" 95.43 277 99.40 99.40 4.88e-113 REF NP_391787 "transcription antiterminator LicT [Bacillus subtilis subsp. subtilis str. 168]" 95.43 277 100.00 100.00 1.22e-113 REF WP_003218864 "transcription antiterminator LicT [Bacillus subtilis]" 95.43 277 97.60 98.80 6.12e-111 REF WP_003236231 "transcription antiterminator LicT [Bacillus subtilis]" 95.43 277 98.20 99.40 1.00e-111 REF WP_003242598 "MULTISPECIES: transcription antiterminator LicT [Bacillales]" 95.43 277 100.00 100.00 1.22e-113 REF WP_014115714 "transcription antiterminator LicT [Bacillus subtilis]" 95.43 277 97.60 98.80 7.20e-111 SP P39805 "RecName: Full=Transcription antiterminator LicT [Bacillus subtilis subsp. subtilis str. 168]" 95.43 277 100.00 100.00 1.22e-113 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species _Gene_mnemonic $CAT-PRD1 'B. subtilis' 1423 Eubacteria . Bacillus subtilis licT stop_ save_ ######################### # Experimental source # ######################### save_experimental_source _Saveframe_category experimental_source loop_ _Mol_label _Production_method _Host_organism_name_common _Genus _Species _Strain _Vector_type _Vector_name _Details $CAT-PRD1 'recombinant technology' 'E. coli' Escherichia coli BL21(DE3) plasmid 'pET15 derivative' ; The 167 N-terminal residues of LicT protein were cloned into a pET15 derivative allowing expression of the LicT-CAT-PRD1 domain fused to a C-terminal His Tag (Leu-Glu-6xHis). The fusion protein was produced in E. coli BL21(DE3) ; 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 $CAT-PRD1 1.0 mM '[U-15N; U-13C; U-2H]' 'Na Phosphate Buffer' 10 mM . Na2SO4 50 mM . DTT 2 mM . EDTA 0.1 mM . Benzmidine 0.1 mM . H2O 90 % . D2O 10 % . stop_ save_ ############################ # Computer software used # ############################ save_Gifa _Saveframe_category software _Name Gifa _Version 4.4 loop_ _Task processing stop_ _Details 'Pons, J.L., Malliavin, T.E., Delsuc, M.A. (1996) J. Biomol. NMR, 8, 445-452' save_ save_NMRView _Saveframe_category software _Name NMRView _Version 5.0 loop_ _Task assignment stop_ _Details 'Johnson, B.A, and Blevins, R.A (1994), J. Biomol. NMR, 4, 603-614' save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer1 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model DMX _Field_strength 600 _Details . save_ save_NMR_spectrometer2 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model DRX _Field_strength 500 _Details . save_ save_NMR_spectrometer3 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model DMX _Field_strength 800 _Details . save_ save_NMR_spectrometer4 _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model INOVA _Field_strength 800 _Details . save_ ############################# # NMR applied experiments # ############################# save_1H-15N_TROSY-HSQC_1 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-15N TROSY-HSQC' _Sample_label . save_ save_TROSY-HNCA_2 _Saveframe_category NMR_applied_experiment _Experiment_name TROSY-HNCA _Sample_label . save_ save_TROSY-HN(CO)CA_3 _Saveframe_category NMR_applied_experiment _Experiment_name TROSY-HN(CO)CA _Sample_label . save_ save_TROSY-HNCACB_4 _Saveframe_category NMR_applied_experiment _Experiment_name TROSY-HNCACB _Sample_label . save_ save_TROSY-HN(CO)CACB_5 _Saveframe_category NMR_applied_experiment _Experiment_name TROSY-HN(CO)CACB _Sample_label . save_ save_TROSY-HNCO_6 _Saveframe_category NMR_applied_experiment _Experiment_name TROSY-HNCO _Sample_label . save_ save_TROSY-HN(CA)CO_7 _Saveframe_category NMR_applied_experiment _Experiment_name TROSY-HN(CA)CO _Sample_label . save_ save_15N_edited-NOESY_8 _Saveframe_category NMR_applied_experiment _Experiment_name '15N edited-NOESY' _Sample_label . save_ save_NMR_spec_expt__0_1 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-15N TROSY-HSQC' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_2 _Saveframe_category NMR_applied_experiment _Experiment_name TROSY-HNCA _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_3 _Saveframe_category NMR_applied_experiment _Experiment_name TROSY-HN(CO)CA _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_4 _Saveframe_category NMR_applied_experiment _Experiment_name TROSY-HNCACB _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_5 _Saveframe_category NMR_applied_experiment _Experiment_name TROSY-HN(CO)CACB _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_6 _Saveframe_category NMR_applied_experiment _Experiment_name TROSY-HNCO _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_7 _Saveframe_category NMR_applied_experiment _Experiment_name TROSY-HN(CA)CO _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_8 _Saveframe_category NMR_applied_experiment _Experiment_name '15N edited-NOESY' _BMRB_pulse_sequence_accession_number . _Details . save_ ####################### # Sample conditions # ####################### save_condition_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 6.4 0.2 na temperature 293 1 K 'ionic strength' 0.15 0.02 M 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 _Reference_correction_type TSP H 1 'methyl protons' ppm 0.00 internal direct . . . 1.00000000 TSP C 13 'methyl protons' ppm 0.00 external indirect . . . 0.25144953 TSP N 15 'methyl protons' ppm 0.00 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_shift_set_1 _Saveframe_category assigned_chemical_shifts _Details ; TROSY effects were corrected based on a JHN of 93Hz and 800 MHz 1H frequency. All chemical shifts were obtained from the 2H/13C/15N labeled sample and no correction was applied on the reported values for correction of 2H isotope effect. ; loop_ _Experiment_label '1H-15N TROSY-HSQC' TROSY-HNCA TROSY-HN(CO)CA TROSY-HNCACB TROSY-HN(CO)CACB TROSY-HNCO TROSY-HN(CA)CO '15N edited-NOESY' stop_ loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $condition_1 _Chem_shift_reference_set_label $chemical_shift_reference _Mol_system_component_name 'CAT-PRD1 subunit 1' _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 MET CA C 54.661 0.23 1 2 . 1 MET CB C 33.315 0.23 1 3 . 1 MET C C 171.416 0.11 1 4 . 2 LYS N N 124.425 0.22 1 5 . 2 LYS H H 8.886 0.012 1 6 . 2 LYS CA C 53.465 0.23 1 7 . 2 LYS CB C 34.130 0.23 1 8 . 2 LYS C C 176.689 0.11 1 9 . 3 ILE N N 121.370 0.22 1 10 . 3 ILE H H 8.816 0.012 1 11 . 3 ILE CA C 62.900 0.23 1 12 . 3 ILE CB C 37.828 0.23 1 13 . 3 ILE C C 176.847 0.11 1 14 . 4 ALA N N 133.698 0.22 1 15 . 4 ALA H H 9.338 0.012 1 16 . 4 ALA CA C 53.405 0.23 1 17 . 4 ALA CB C 16.587 0.23 1 18 . 4 ALA C C 177.023 0.11 1 19 . 5 LYS N N 117.711 0.22 1 20 . 5 LYS H H 7.646 0.012 1 21 . 5 LYS CA C 54.261 0.23 1 22 . 5 LYS CB C 34.457 0.23 1 23 . 5 LYS C C 174.968 0.11 1 24 . 6 VAL N N 124.308 0.22 1 25 . 6 VAL H H 8.852 0.012 1 26 . 6 VAL CA C 62.726 0.23 1 27 . 6 VAL CB C 31.197 0.23 1 28 . 6 VAL C C 175.643 0.11 1 29 . 7 ILE N N 130.561 0.22 1 30 . 7 ILE H H 8.361 0.012 1 31 . 7 ILE CA C 62.719 0.23 1 32 . 7 ILE CB C 35.633 0.23 1 33 . 7 ILE C C 176.132 0.11 1 34 . 8 ASN N N 113.914 0.22 1 35 . 8 ASN H H 8.618 0.012 1 36 . 8 ASN CA C 52.444 0.23 1 37 . 8 ASN CB C 37.089 0.23 1 38 . 8 ASN C C 174.066 0.11 1 39 . 9 ASN N N 111.966 0.22 1 40 . 9 ASN H H 8.416 0.012 1 41 . 9 ASN CA C 56.146 0.23 1 42 . 9 ASN CB C 37.144 0.23 1 43 . 9 ASN C C 175.276 0.11 1 44 . 10 ASN N N 112.180 0.22 1 45 . 10 ASN H H 9.004 0.012 1 46 . 10 ASN CA C 51.067 0.23 1 47 . 10 ASN CB C 40.793 0.23 1 48 . 10 ASN C C 173.822 0.11 1 49 . 11 VAL N N 118.996 0.22 1 50 . 11 VAL H H 7.299 0.012 1 51 . 11 VAL CA C 60.920 0.23 1 52 . 11 VAL CB C 33.929 0.23 1 53 . 11 VAL C C 173.987 0.11 1 54 . 12 ILE N N 118.676 0.22 1 55 . 12 ILE H H 8.952 0.012 1 56 . 12 ILE CA C 58.070 0.23 1 57 . 12 ILE CB C 40.703 0.23 1 58 . 12 ILE C C 174.028 0.11 1 59 . 13 SER N N 115.072 0.22 1 60 . 13 SER H H 9.219 0.012 1 61 . 13 SER CA C 55.808 0.23 1 62 . 13 SER CB C 64.905 0.23 1 63 . 13 SER C C 174.164 0.11 1 64 . 14 VAL N N 120.672 0.22 1 65 . 14 VAL H H 8.876 0.012 1 66 . 14 VAL CA C 59.754 0.23 1 67 . 14 VAL CB C 35.906 0.23 1 68 . 14 VAL C C 173.447 0.11 1 69 . 15 VAL N N 123.655 0.22 1 70 . 15 VAL H H 8.920 0.012 1 71 . 15 VAL CA C 60.242 0.23 1 72 . 15 VAL CB C 31.824 0.23 1 73 . 15 VAL C C 176.539 0.11 1 74 . 16 ASN N N 125.499 0.22 1 75 . 16 ASN H H 8.702 0.012 1 76 . 16 ASN CA C 50.437 0.23 1 77 . 16 ASN CB C 37.774 0.23 1 78 . 16 ASN C C 177.317 0.11 1 79 . 17 GLU N N 117.977 0.22 1 80 . 17 GLU H H 9.118 0.012 1 81 . 17 GLU CA C 58.393 0.23 1 82 . 17 GLU CB C 27.570 0.23 1 83 . 17 GLU C C 177.333 0.11 1 84 . 18 GLN N N 115.979 0.22 1 85 . 18 GLN H H 7.446 0.012 1 86 . 18 GLN CA C 55.082 0.23 1 87 . 18 GLN CB C 27.556 0.23 1 88 . 18 GLN C C 176.210 0.11 1 89 . 19 GLY N N 107.906 0.22 1 90 . 19 GLY H H 8.126 0.012 1 91 . 19 GLY CA C 44.612 0.23 1 92 . 19 GLY C C 174.018 0.11 1 93 . 20 LYS N N 121.793 0.22 1 94 . 20 LYS H H 7.822 0.012 1 95 . 20 LYS CA C 54.106 0.23 1 96 . 20 LYS CB C 31.728 0.23 1 97 . 20 LYS C C 174.809 0.11 1 98 . 21 GLU N N 124.278 0.22 1 99 . 21 GLU H H 8.566 0.012 1 100 . 21 GLU CA C 54.807 0.23 1 101 . 21 GLU CB C 29.864 0.23 1 102 . 21 GLU C C 175.483 0.11 1 103 . 22 LEU N N 127.566 0.22 1 104 . 22 LEU H H 9.405 0.012 1 105 . 22 LEU CA C 52.589 0.23 1 106 . 22 LEU CB C 42.792 0.23 1 107 . 22 LEU C C 176.138 0.11 1 108 . 23 VAL N N 121.545 0.22 1 109 . 23 VAL H H 8.354 0.012 1 110 . 23 VAL CA C 61.331 0.23 1 111 . 23 VAL CB C 31.827 0.23 1 112 . 23 VAL C C 174.269 0.11 1 113 . 24 VAL N N 126.875 0.22 1 114 . 24 VAL H H 9.112 0.012 1 115 . 24 VAL CA C 60.082 0.23 1 116 . 24 VAL CB C 32.610 0.23 1 117 . 24 VAL C C 173.096 0.11 1 118 . 25 MET N N 123.757 0.22 1 119 . 25 MET H H 9.051 0.012 1 120 . 25 MET CA C 52.159 0.23 1 121 . 25 MET CB C 37.251 0.23 1 122 . 25 MET C C 175.968 0.11 1 123 . 26 GLY N N 114.326 0.22 1 124 . 26 GLY H H 9.159 0.012 1 125 . 26 GLY CA C 45.291 0.23 1 126 . 26 GLY C C 172.759 0.11 1 127 . 27 ARG N N 124.880 0.22 1 128 . 27 ARG H H 8.886 0.012 1 129 . 27 ARG CA C 56.956 0.23 1 130 . 27 ARG CB C 27.351 0.23 1 131 . 27 ARG C C 178.600 0.11 1 132 . 28 GLY N N 114.133 0.22 1 133 . 28 GLY H H 9.271 0.012 1 134 . 28 GLY CA C 45.817 0.23 1 135 . 28 GLY C C 176.067 0.11 1 136 . 29 LEU N N 121.917 0.22 1 137 . 29 LEU H H 7.851 0.012 1 138 . 29 LEU CA C 56.705 0.23 1 139 . 29 LEU CB C 42.332 0.23 1 140 . 29 LEU C C 175.663 0.11 1 141 . 30 ALA N N 115.317 0.22 1 142 . 30 ALA H H 8.379 0.012 1 143 . 30 ALA CA C 48.935 0.23 1 144 . 30 ALA CB C 18.348 0.23 1 145 . 30 ALA C C 176.724 0.11 1 146 . 31 PHE N N 121.660 0.22 1 147 . 31 PHE H H 7.245 0.012 1 148 . 31 PHE CA C 58.544 0.23 1 149 . 31 PHE CB C 37.604 0.23 1 150 . 31 PHE C C 175.748 0.11 1 151 . 32 GLN N N 122.033 0.22 1 152 . 32 GLN H H 8.903 0.012 1 153 . 32 GLN CA C 56.508 0.23 1 154 . 32 GLN CB C 24.399 0.23 1 155 . 32 GLN C C 174.741 0.11 1 156 . 33 LYS N N 116.274 0.22 1 157 . 33 LYS H H 7.460 0.012 1 158 . 33 LYS CA C 52.857 0.23 1 159 . 33 LYS CB C 34.656 0.23 1 160 . 33 LYS C C 175.112 0.11 1 161 . 34 LYS N N 118.106 0.22 1 162 . 34 LYS H H 8.834 0.012 1 163 . 34 LYS CA C 53.082 0.23 1 164 . 34 LYS CB C 34.903 0.23 1 165 . 34 LYS C C 175.448 0.11 1 166 . 35 SER N N 112.836 0.22 1 167 . 35 SER H H 8.464 0.012 1 168 . 35 SER CA C 59.732 0.23 1 169 . 35 SER CB C 61.800 0.23 1 170 . 35 SER C C 175.451 0.11 1 171 . 36 GLY N N 114.932 0.22 1 172 . 36 GLY H H 9.200 0.012 1 173 . 36 GLY CA C 44.067 0.23 1 174 . 36 GLY C C 174.235 0.11 1 175 . 37 ASP N N 120.491 0.22 1 176 . 37 ASP H H 7.989 0.012 1 177 . 37 ASP CA C 53.712 0.23 1 178 . 37 ASP CB C 41.191 0.23 1 179 . 37 ASP C C 175.807 0.11 1 180 . 38 ASP N N 118.322 0.22 1 181 . 38 ASP H H 8.508 0.012 1 182 . 38 ASP CA C 53.805 0.23 1 183 . 38 ASP CB C 40.645 0.23 1 184 . 38 ASP C C 176.514 0.11 1 185 . 39 VAL N N 118.502 0.22 1 186 . 39 VAL H H 8.071 0.012 1 187 . 39 VAL CA C 60.386 0.23 1 188 . 39 VAL CB C 32.436 0.23 1 189 . 39 VAL C C 175.620 0.11 1 190 . 40 ASP N N 126.146 0.22 1 191 . 40 ASP H H 8.723 0.012 1 192 . 40 ASP CA C 52.184 0.23 1 193 . 40 ASP CB C 38.711 0.23 1 194 . 40 ASP C C 176.416 0.11 1 195 . 41 GLU N N 125.741 0.22 1 196 . 41 GLU H H 8.733 0.012 1 197 . 41 GLU CA C 58.295 0.23 1 198 . 41 GLU CB C 27.989 0.23 1 199 . 41 GLU C C 178.267 0.11 1 200 . 42 ALA N N 120.428 0.22 1 201 . 42 ALA H H 8.253 0.012 1 202 . 42 ALA CA C 53.071 0.23 1 203 . 42 ALA CB C 17.181 0.23 1 204 . 42 ALA C C 176.716 0.11 1 205 . 43 ARG N N 114.000 0.22 1 206 . 43 ARG H H 7.645 0.012 1 207 . 43 ARG CA C 60.082 0.23 1 208 . 43 ARG CB C 32.610 0.23 1 209 . 43 ARG C C 176.149 0.11 1 210 . 44 ILE N N 118.952 0.22 1 211 . 44 ILE H H 7.041 0.012 1 212 . 44 ILE CA C 63.681 0.23 1 213 . 44 ILE CB C 37.167 0.23 1 214 . 44 ILE C C 175.974 0.11 1 215 . 45 GLU N N 127.290 0.22 1 216 . 45 GLU H H 9.271 0.012 1 217 . 45 GLU CA C 56.455 0.23 1 218 . 45 GLU CB C 30.721 0.23 1 219 . 45 GLU C C 176.302 0.11 1 220 . 46 LYS N N 118.072 0.22 1 221 . 46 LYS H H 8.075 0.012 1 222 . 46 LYS CA C 53.956 0.23 1 223 . 46 LYS CB C 35.593 0.23 1 224 . 46 LYS C C 173.187 0.11 1 225 . 47 VAL N N 122.567 0.22 1 226 . 47 VAL H H 8.148 0.012 1 227 . 47 VAL CA C 60.576 0.23 1 228 . 47 VAL CB C 32.734 0.23 1 229 . 47 VAL C C 175.107 0.11 1 230 . 48 PHE N N 126.195 0.22 1 231 . 48 PHE H H 9.568 0.012 1 232 . 48 PHE CA C 56.088 0.23 1 233 . 49 THR CA C 59.774 0.23 1 234 . 49 THR CB C 68.155 0.23 1 235 . 49 THR C C 173.483 0.11 1 236 . 50 LEU N N 126.883 0.22 1 237 . 50 LEU H H 8.664 0.012 1 238 . 50 LEU CA C 53.182 0.23 1 239 . 50 LEU CB C 40.726 0.23 1 240 . 50 LEU C C 177.072 0.11 1 241 . 51 ASP N N 122.243 0.22 1 242 . 51 ASP H H 8.982 0.012 1 243 . 51 ASP CA C 55.244 0.23 1 244 . 51 ASP CB C 41.046 0.23 1 245 . 51 ASP C C 176.178 0.11 1 246 . 52 ASN N N 116.994 0.22 1 247 . 52 ASN H H 8.028 0.012 1 248 . 52 ASN CA C 52.426 0.23 1 249 . 52 ASN CB C 39.158 0.23 1 250 . 53 LYS CA C 58.041 0.23 1 251 . 53 LYS C C 177.824 0.11 1 252 . 54 ASP N N 119.634 0.22 1 253 . 54 ASP H H 8.174 0.012 1 254 . 54 ASP CA C 56.504 0.23 1 255 . 54 ASP CB C 39.479 0.23 1 256 . 54 ASP C C 178.992 0.11 1 257 . 55 VAL N N 120.079 0.22 1 258 . 55 VAL H H 7.957 0.012 1 259 . 55 VAL CA C 64.869 0.23 1 260 . 55 VAL CB C 30.535 0.23 1 261 . 55 VAL C C 177.636 0.11 1 262 . 56 SER N N 115.057 0.22 1 263 . 56 SER H H 8.300 0.012 1 264 . 56 SER CA C 61.546 0.23 1 265 . 56 SER C C 176.780 0.11 1 266 . 57 GLU N N 119.493 0.22 1 267 . 57 GLU H H 8.155 0.012 1 268 . 57 GLU CA C 58.532 0.23 1 269 . 57 GLU CB C 28.013 0.23 1 270 . 57 GLU C C 179.470 0.11 1 271 . 58 LYS N N 119.573 0.22 1 272 . 58 LYS H H 7.682 0.012 1 273 . 58 LYS CA C 58.386 0.23 1 274 . 58 LYS CB C 31.548 0.23 1 275 . 58 LYS C C 179.248 0.11 1 276 . 59 PHE CA C 59.449 0.23 1 277 . 59 PHE C C 176.189 0.11 1 278 . 60 LYS N N 116.345 0.22 1 279 . 60 LYS H H 8.182 0.012 1 280 . 60 LYS CA C 59.844 0.23 1 281 . 60 LYS CB C 30.805 0.23 1 282 . 60 LYS C C 177.957 0.11 1 283 . 61 THR N N 111.527 0.22 1 284 . 61 THR H H 7.586 0.012 1 285 . 61 THR CA C 65.153 0.23 1 286 . 61 THR CB C 68.143 0.23 1 287 . 61 THR C C 176.567 0.11 1 288 . 62 LEU N N 122.878 0.22 1 289 . 62 LEU H H 7.822 0.012 1 290 . 62 LEU CA C 56.596 0.23 1 291 . 62 LEU CB C 40.943 0.23 1 292 . 67 PRO CA C 61.869 0.23 1 293 . 67 PRO CB C 31.343 0.23 1 294 . 67 PRO C C 179.359 0.11 1 295 . 68 ILE N N 125.712 0.22 1 296 . 68 ILE H H 8.818 0.012 1 297 . 68 ILE CA C 62.756 0.23 1 298 . 68 ILE CB C 36.529 0.23 1 299 . 68 ILE C C 176.740 0.11 1 300 . 69 GLU N N 120.678 0.22 1 301 . 69 GLU H H 9.648 0.012 1 302 . 69 GLU CA C 59.312 0.23 1 303 . 69 GLU CB C 27.054 0.23 1 304 . 69 GLU C C 178.996 0.11 1 305 . 70 CYS N N 115.948 0.22 1 306 . 70 CYS H H 7.291 0.012 1 307 . 70 CYS CA C 60.642 0.23 1 308 . 70 CYS CB C 27.405 0.23 1 309 . 70 CYS C C 176.841 0.11 1 310 . 71 MET N N 120.491 0.22 1 311 . 71 MET H H 7.449 0.012 1 312 . 71 MET CA C 57.268 0.23 1 313 . 71 MET CB C 32.282 0.23 1 314 . 71 MET C C 178.100 0.11 1 315 . 72 GLU N N 117.187 0.22 1 316 . 72 GLU H H 8.772 0.012 1 317 . 72 GLU CA C 58.789 0.23 1 318 . 72 GLU CB C 28.623 0.23 1 319 . 72 GLU C C 179.411 0.11 1 320 . 73 VAL N N 117.470 0.22 1 321 . 73 VAL H H 8.033 0.012 1 322 . 73 VAL CA C 63.620 0.23 1 323 . 73 VAL CB C 30.345 0.23 1 324 . 73 VAL C C 176.236 0.11 1 325 . 74 SER N N 118.336 0.22 1 326 . 74 SER H H 7.878 0.012 1 327 . 74 SER CA C 62.017 0.23 1 328 . 74 SER C C 175.858 0.11 1 329 . 75 GLU N N 119.139 0.22 1 330 . 75 GLU H H 8.056 0.012 1 331 . 75 GLU CA C 59.272 0.23 1 332 . 75 GLU CB C 27.073 0.23 1 333 . 75 GLU C C 178.227 0.11 1 334 . 76 GLU N N 120.476 0.22 1 335 . 76 GLU H H 7.892 0.012 1 336 . 76 GLU CA C 58.853 0.23 1 337 . 76 GLU CB C 28.211 0.23 1 338 . 76 GLU C C 179.982 0.11 1 339 . 77 ILE N N 121.235 0.22 1 340 . 77 ILE H H 8.502 0.012 1 341 . 77 ILE CA C 64.941 0.23 1 342 . 77 ILE CB C 37.083 0.23 1 343 . 77 ILE C C 177.208 0.11 1 344 . 78 ILE N N 120.779 0.22 1 345 . 78 ILE H H 8.421 0.012 1 346 . 78 ILE CA C 65.883 0.23 1 347 . 78 ILE CB C 37.117 0.23 1 348 . 78 ILE C C 177.828 0.11 1 349 . 79 SER N N 114.953 0.22 1 350 . 79 SER H H 8.791 0.012 1 351 . 79 SER CA C 61.691 0.23 1 352 . 79 SER C C 177.099 0.11 1 353 . 80 TYR N N 123.337 0.22 1 354 . 80 TYR H H 7.938 0.012 1 355 . 80 TYR CA C 60.429 0.23 1 356 . 80 TYR CB C 37.651 0.23 1 357 . 80 TYR C C 177.012 0.11 1 358 . 81 ALA N N 121.544 0.22 1 359 . 81 ALA H H 9.018 0.012 1 360 . 81 ALA CA C 54.398 0.23 1 361 . 81 ALA CB C 17.006 0.23 1 362 . 81 ALA C C 179.282 0.11 1 363 . 82 LYS N N 115.755 0.22 1 364 . 82 LYS H H 8.346 0.012 1 365 . 82 LYS CA C 59.482 0.23 1 366 . 82 LYS CB C 31.988 0.23 1 367 . 82 LYS C C 179.765 0.11 1 368 . 83 LEU N N 119.194 0.22 1 369 . 83 LEU H H 7.567 0.012 1 370 . 83 LEU CA C 56.534 0.23 1 371 . 83 LEU CB C 40.894 0.23 1 372 . 83 LEU C C 179.408 0.11 1 373 . 84 GLN N N 116.347 0.22 1 374 . 84 GLN H H 8.252 0.012 1 375 . 84 GLN CA C 56.152 0.23 1 376 . 84 GLN CB C 28.005 0.23 1 377 . 84 GLN C C 178.481 0.11 1 378 . 85 LEU N N 115.209 0.22 1 379 . 85 LEU H H 8.158 0.012 1 380 . 85 LEU CA C 54.536 0.23 1 381 . 85 LEU CB C 41.629 0.23 1 382 . 85 LEU C C 178.455 0.11 1 383 . 86 GLY N N 106.982 0.22 1 384 . 86 GLY H H 7.783 0.012 1 385 . 86 GLY CA C 45.463 0.23 1 386 . 86 GLY C C 174.198 0.11 1 387 . 87 LYS N N 116.216 0.22 1 388 . 87 LYS H H 6.993 0.012 1 389 . 87 LYS CA C 53.580 0.23 1 390 . 87 LYS CB C 34.005 0.23 1 391 . 87 LYS C C 175.301 0.11 1 392 . 88 LYS N N 120.264 0.22 1 393 . 88 LYS H H 8.346 0.012 1 394 . 88 LYS CA C 55.443 0.23 1 395 . 88 LYS CB C 31.786 0.23 1 396 . 88 LYS C C 175.858 0.11 1 397 . 89 LEU N N 119.178 0.22 1 398 . 89 LEU H H 8.194 0.012 1 399 . 89 LEU CA C 51.995 0.23 1 400 . 89 LEU CB C 41.722 0.23 1 401 . 89 LEU C C 175.811 0.11 1 402 . 90 ASN N N 122.473 0.22 1 403 . 90 ASN H H 7.897 0.012 1 404 . 90 ASN CA C 54.044 0.23 1 405 . 90 ASN CB C 40.547 0.23 1 406 . 90 ASN C C 175.009 0.11 1 407 . 91 ASP N N 122.740 0.22 1 408 . 91 ASP H H 8.828 0.012 1 409 . 91 ASP CA C 56.258 0.23 1 410 . 91 ASP CB C 40.251 0.23 1 411 . 91 ASP C C 177.072 0.11 1 412 . 92 SER N N 116.520 0.22 1 413 . 92 SER H H 8.979 0.012 1 414 . 92 SER CA C 61.203 0.23 1 415 . 92 SER C C 176.756 0.11 1 416 . 93 ILE N N 124.457 0.22 1 417 . 93 ILE H H 8.165 0.012 1 418 . 93 ILE CA C 61.698 0.23 1 419 . 93 ILE CB C 36.830 0.23 1 420 . 93 ILE C C 175.669 0.11 1 421 . 94 TYR N N 119.152 0.22 1 422 . 94 TYR H H 7.830 0.012 1 423 . 94 TYR CA C 62.271 0.23 1 424 . 94 TYR CB C 35.178 0.23 1 425 . 94 TYR C C 177.909 0.11 1 426 . 98 THR N N 115.271 0.22 1 427 . 98 THR H H 6.532 0.012 1 428 . 98 THR CA C 65.351 0.23 1 429 . 98 THR CB C 66.759 0.23 1 430 . 98 THR C C 175.729 0.11 1 431 . 99 ASP N N 117.834 0.22 1 432 . 99 ASP H H 7.646 0.012 1 433 . 99 ASP CA C 59.315 0.23 1 434 . 99 ASP C C 177.529 0.11 1 435 . 100 HIS N N 115.273 0.22 1 436 . 100 HIS H H 7.634 0.012 1 437 . 100 HIS CA C 59.702 0.23 1 438 . 100 HIS CB C 27.234 0.23 1 439 . 100 HIS C C 176.519 0.11 1 440 . 101 ILE N N 118.724 0.22 1 441 . 101 ILE H H 8.807 0.012 1 442 . 101 ILE CA C 63.376 0.23 1 443 . 101 ILE CB C 34.849 0.23 1 444 . 101 ILE C C 176.918 0.11 1 445 . 102 ASN N N 116.653 0.22 1 446 . 102 ASN H H 7.690 0.012 1 447 . 102 ASN CA C 56.512 0.23 1 448 . 102 ASN CB C 38.478 0.23 1 449 . 102 ASN C C 176.871 0.11 1 450 . 103 PHE N N 118.980 0.22 1 451 . 103 PHE H H 7.854 0.012 1 452 . 103 PHE CA C 60.312 0.23 1 453 . 103 PHE CB C 37.726 0.23 1 454 . 103 PHE C C 177.303 0.11 1 455 . 104 ALA N N 121.806 0.22 1 456 . 104 ALA H H 8.736 0.012 1 457 . 104 ALA CA C 53.779 0.23 1 458 . 104 ALA CB C 16.873 0.23 1 459 . 104 ALA C C 180.817 0.11 1 460 . 105 ILE N N 117.220 0.22 1 461 . 105 ILE H H 8.194 0.012 1 462 . 105 ILE CA C 64.641 0.23 1 463 . 105 ILE CB C 36.673 0.23 1 464 . 105 ILE C C 177.879 0.11 1 465 . 106 GLN N N 118.677 0.22 1 466 . 106 GLN H H 7.756 0.012 1 467 . 106 GLN CA C 57.634 0.23 1 468 . 106 GLN CB C 27.440 0.23 1 469 . 106 GLN C C 178.360 0.11 1 470 . 107 ARG N N 118.295 0.22 1 471 . 107 ARG H H 8.157 0.012 1 472 . 107 ARG CA C 57.494 0.23 1 473 . 107 ARG CB C 28.098 0.23 1 474 . 107 ARG C C 177.781 0.11 1 475 . 108 ASN N N 118.034 0.22 1 476 . 108 ASN H H 7.695 0.012 1 477 . 108 ASN CA C 55.362 0.23 1 478 . 108 ASN CB C 38.672 0.23 1 479 . 108 ASN C C 177.310 0.11 1 480 . 109 GLN N N 118.745 0.22 1 481 . 109 GLN H H 8.336 0.012 1 482 . 109 GLN CA C 56.987 0.23 1 483 . 109 GLN CB C 27.654 0.23 1 484 . 109 GLN C C 177.512 0.11 1 485 . 110 LYS N N 117.237 0.22 1 486 . 110 LYS H H 7.911 0.012 1 487 . 110 LYS CA C 55.746 0.23 1 488 . 110 LYS CB C 31.839 0.23 1 489 . 110 LYS C C 177.093 0.11 1 490 . 111 GLY N N 108.884 0.22 1 491 . 111 GLY H H 7.886 0.012 1 492 . 111 GLY CA C 45.317 0.23 1 493 . 111 GLY C C 174.547 0.11 1 494 . 112 LEU N N 119.857 0.22 1 495 . 112 LEU H H 7.711 0.012 1 496 . 112 LEU CA C 53.862 0.23 1 497 . 112 LEU CB C 41.202 0.23 1 498 . 112 LEU C C 176.378 0.11 1 499 . 113 ASP N N 123.040 0.22 1 500 . 113 ASP H H 8.538 0.012 1 501 . 113 ASP CA C 53.163 0.23 1 502 . 113 ASP CB C 40.489 0.23 1 503 . 113 ASP C C 176.098 0.11 1 504 . 114 ILE N N 122.752 0.22 1 505 . 114 ILE H H 8.180 0.012 1 506 . 114 ILE CA C 60.197 0.23 1 507 . 114 ILE CB C 37.997 0.23 1 508 . 114 ILE C C 176.438 0.11 1 509 . 115 LYS N N 125.592 0.22 1 510 . 115 LYS H H 8.513 0.012 1 511 . 115 LYS CA C 56.889 0.23 1 512 . 115 LYS CB C 30.956 0.23 1 513 . 115 LYS C C 177.407 0.11 1 514 . 116 ASN N N 118.599 0.22 1 515 . 116 ASN H H 8.757 0.012 1 516 . 116 ASN CA C 52.688 0.23 1 517 . 116 ASN CB C 36.999 0.23 1 518 . 116 ASN C C 175.162 0.11 1 519 . 117 ALA N N 120.340 0.22 1 520 . 117 ALA H H 7.951 0.012 1 521 . 117 ALA CA C 54.774 0.23 1 522 . 117 ALA CB C 17.854 0.23 1 523 . 117 ALA C C 180.027 0.11 1 524 . 118 LEU N N 121.900 0.22 1 525 . 118 LEU H H 8.841 0.012 1 526 . 118 LEU CA C 56.694 0.23 1 527 . 118 LEU CB C 39.203 0.23 1 528 . 118 LEU C C 179.017 0.11 1 529 . 119 LEU N N 122.624 0.22 1 530 . 119 LEU H H 7.698 0.012 1 531 . 119 LEU CA C 57.127 0.23 1 532 . 119 LEU CB C 39.566 0.23 1 533 . 119 LEU C C 178.399 0.11 1 534 . 120 TRP N N 117.458 0.22 1 535 . 120 TRP H H 7.445 0.012 1 536 . 120 TRP CA C 57.387 0.23 1 537 . 120 TRP C C 178.767 0.11 1 538 . 121 GLU N N 123.147 0.22 1 539 . 121 GLU H H 8.137 0.012 1 540 . 121 GLU CA C 57.626 0.23 1 541 . 121 GLU CB C 28.392 0.23 1 542 . 121 GLU C C 178.540 0.11 1 543 . 122 THR N N 115.323 0.22 1 544 . 122 THR H H 7.745 0.012 1 545 . 122 THR CA C 66.378 0.23 1 546 . 122 THR C C 175.296 0.11 1 547 . 123 LYS N N 119.872 0.22 1 548 . 123 LYS H H 7.091 0.012 1 549 . 123 LYS CA C 58.528 0.23 1 550 . 123 LYS CB C 30.634 0.23 1 551 . 123 LYS C C 176.568 0.11 1 552 . 124 ARG N N 115.886 0.22 1 553 . 124 ARG H H 7.362 0.012 1 554 . 124 ARG CA C 57.801 0.23 1 555 . 124 ARG CB C 29.633 0.23 1 556 . 124 ARG C C 178.730 0.11 1 557 . 125 LEU N N 116.587 0.22 1 558 . 125 LEU H H 7.826 0.012 1 559 . 125 LEU CA C 55.516 0.23 1 560 . 125 LEU CB C 41.941 0.23 1 561 . 125 LEU C C 177.030 0.11 1 562 . 126 TYR N N 120.004 0.22 1 563 . 126 TYR H H 7.688 0.012 1 564 . 126 TYR CA C 53.659 0.23 1 565 . 126 TYR CB C 35.040 0.23 1 566 . 126 TYR C C 175.079 0.11 1 567 . 127 LYS N N 121.363 0.22 1 568 . 127 LYS H H 7.549 0.012 1 569 . 127 LYS CA C 59.778 0.23 1 570 . 127 LYS CB C 31.399 0.23 1 571 . 127 LYS C C 180.346 0.11 1 572 . 128 ASP N N 120.425 0.22 1 573 . 128 ASP H H 8.967 0.012 1 574 . 128 ASP CA C 56.583 0.23 1 575 . 128 ASP CB C 39.125 0.23 1 576 . 128 ASP C C 179.039 0.11 1 577 . 129 GLU N N 121.896 0.22 1 578 . 129 GLU H H 9.660 0.012 1 579 . 129 GLU CA C 61.228 0.23 1 580 . 129 GLU CB C 25.612 0.23 1 581 . 129 GLU C C 178.125 0.11 1 582 . 130 PHE N N 121.347 0.22 1 583 . 130 PHE H H 9.400 0.012 1 584 . 130 PHE CA C 61.531 0.23 1 585 . 130 PHE CB C 38.671 0.23 1 586 . 130 PHE C C 176.739 0.11 1 587 . 131 ALA N N 120.477 0.22 1 588 . 131 ALA H H 8.039 0.012 1 589 . 131 ALA CA C 54.759 0.23 1 590 . 131 ALA CB C 16.512 0.23 1 591 . 131 ALA C C 178.125 0.11 1 592 . 132 ILE N N 119.153 0.22 1 593 . 132 ILE H H 7.672 0.012 1 594 . 132 ILE CA C 64.030 0.23 1 595 . 132 ILE CB C 35.548 0.23 1 596 . 132 ILE C C 177.592 0.11 1 597 . 133 GLY N N 108.514 0.22 1 598 . 133 GLY H H 8.253 0.012 1 599 . 133 GLY CA C 46.706 0.23 1 600 . 133 GLY C C 174.403 0.11 1 601 . 134 LYS N N 119.816 0.22 1 602 . 134 LYS H H 8.381 0.012 1 603 . 134 LYS CA C 58.998 0.23 1 604 . 134 LYS CB C 30.412 0.23 1 605 . 134 LYS C C 180.312 0.11 1 606 . 135 GLU N N 121.912 0.22 1 607 . 135 GLU H H 7.802 0.012 1 608 . 135 GLU CA C 57.552 0.23 1 609 . 135 GLU CB C 27.448 0.23 1 610 . 135 GLU C C 179.683 0.11 1 611 . 136 ALA N N 121.796 0.22 1 612 . 136 ALA H H 9.107 0.012 1 613 . 136 ALA CA C 53.530 0.23 1 614 . 136 ALA CB C 17.722 0.23 1 615 . 136 ALA C C 179.343 0.11 1 616 . 137 LEU N N 114.530 0.22 1 617 . 137 LEU H H 7.457 0.012 1 618 . 137 LEU CA C 57.326 0.23 1 619 . 137 LEU CB C 38.675 0.23 1 620 . 137 LEU C C 181.178 0.11 1 621 . 138 VAL N N 122.639 0.22 1 622 . 138 VAL H H 7.209 0.012 1 623 . 138 VAL CA C 65.167 0.23 1 624 . 138 VAL CB C 30.365 0.23 1 625 . 138 VAL C C 178.036 0.11 1 626 . 139 MET N N 119.248 0.22 1 627 . 139 MET H H 7.691 0.012 1 628 . 139 MET CA C 58.681 0.23 1 629 . 139 MET CB C 31.024 0.23 1 630 . 139 MET C C 179.944 0.11 1 631 . 140 VAL N N 118.568 0.22 1 632 . 140 VAL H H 8.776 0.012 1 633 . 140 VAL CA C 66.677 0.23 1 634 . 140 VAL CB C 30.845 0.23 1 635 . 140 VAL C C 179.528 0.11 1 636 . 141 LYS N N 125.974 0.22 1 637 . 141 LYS H H 7.877 0.012 1 638 . 141 LYS CA C 58.772 0.23 1 639 . 141 LYS CB C 30.583 0.23 1 640 . 141 LYS C C 179.569 0.11 1 641 . 142 ASN N N 118.559 0.22 1 642 . 142 ASN H H 8.591 0.012 1 643 . 142 ASN CA C 54.937 0.23 1 644 . 142 ASN CB C 36.779 0.23 1 645 . 142 ASN C C 176.888 0.11 1 646 . 143 LYS N N 115.895 0.22 1 647 . 143 LYS H H 7.806 0.012 1 648 . 143 LYS CA C 56.324 0.23 1 649 . 143 LYS CB C 31.689 0.23 1 650 . 143 LYS C C 177.524 0.11 1 651 . 144 THR CA C 61.276 0.23 1 652 . 144 THR C C 175.810 0.11 1 653 . 145 GLY N N 111.527 0.22 1 654 . 145 GLY H H 8.190 0.012 1 655 . 145 GLY CA C 44.826 0.23 1 656 . 145 GLY C C 173.721 0.11 1 657 . 146 VAL N N 123.080 0.22 1 658 . 146 VAL H H 7.857 0.012 1 659 . 146 VAL CA C 61.961 0.23 1 660 . 146 VAL CB C 31.331 0.23 1 661 . 146 VAL C C 175.308 0.11 1 662 . 147 SER N N 124.051 0.22 1 663 . 147 SER H H 8.762 0.012 1 664 . 147 SER CA C 55.791 0.23 1 665 . 147 SER CB C 61.560 0.23 1 666 . 147 SER C C 173.467 0.11 1 667 . 148 LEU N N 126.844 0.22 1 668 . 148 LEU H H 8.636 0.012 1 669 . 148 LEU CA C 51.486 0.23 1 670 . 148 LEU CB C 39.524 0.23 1 671 . 148 LEU C C 173.848 0.11 1 672 . 149 PRO CA C 61.710 0.23 1 673 . 149 PRO CB C 31.189 0.23 1 674 . 149 PRO C C 176.947 0.11 1 675 . 150 GLU N N 119.613 0.22 1 676 . 150 GLU H H 8.676 0.012 1 677 . 150 GLU CA C 58.487 0.23 1 678 . 150 GLU CB C 28.417 0.23 1 679 . 150 GLU C C 176.519 0.11 1 680 . 151 ASP N N 114.986 0.22 1 681 . 151 ASP H H 8.803 0.012 1 682 . 151 ASP CA C 54.903 0.23 1 683 . 151 ASP CB C 39.378 0.23 1 684 . 151 ASP C C 179.475 0.11 1 685 . 152 GLU N N 117.886 0.22 1 686 . 152 GLU H H 8.418 0.012 1 687 . 152 GLU CA C 57.877 0.23 1 688 . 152 GLU CB C 27.306 0.23 1 689 . 152 GLU C C 178.390 0.11 1 690 . 153 ALA N N 122.109 0.22 1 691 . 153 ALA H H 7.965 0.012 1 692 . 153 ALA CA C 54.885 0.23 1 693 . 153 ALA CB C 16.240 0.23 1 694 . 153 ALA C C 179.657 0.11 1 695 . 154 GLY N N 103.196 0.22 1 696 . 154 GLY H H 7.423 0.012 1 697 . 154 GLY CA C 45.751 0.23 1 698 . 154 GLY C C 174.545 0.11 1 699 . 155 PHE N N 119.585 0.22 1 700 . 155 PHE H H 7.455 0.012 1 701 . 155 PHE CA C 61.650 0.23 1 702 . 155 PHE CB C 38.671 0.23 1 703 . 155 PHE C C 178.168 0.11 1 704 . 156 ILE N N 117.199 0.22 1 705 . 156 ILE H H 8.283 0.012 1 706 . 156 ILE CA C 65.371 0.23 1 707 . 156 ILE CB C 36.625 0.23 1 708 . 156 ILE C C 177.833 0.11 1 709 . 157 ALA N N 120.084 0.22 1 710 . 157 ALA H H 7.988 0.012 1 711 . 157 ALA CA C 55.132 0.23 1 712 . 157 ALA CB C 15.645 0.23 1 713 . 157 ALA C C 178.919 0.11 1 714 . 158 LEU N N 113.505 0.22 1 715 . 158 LEU H H 7.806 0.012 1 716 . 158 LEU CA C 56.943 0.23 1 717 . 158 LEU CB C 40.116 0.23 1 718 . 158 LEU C C 181.214 0.11 1 719 . 159 HIS N N 120.742 0.22 1 720 . 159 HIS H H 7.844 0.012 1 721 . 159 HIS CA C 60.901 0.23 1 722 . 159 HIS CB C 31.314 0.23 1 723 . 159 HIS C C 177.871 0.11 1 724 . 160 ILE N N 121.358 0.22 1 725 . 160 ILE H H 8.052 0.012 1 726 . 160 ILE CA C 64.843 0.23 1 727 . 160 ILE CB C 36.167 0.23 1 728 . 160 ILE C C 177.498 0.11 1 729 . 161 VAL N N 119.567 0.22 1 730 . 161 VAL H H 8.429 0.012 1 731 . 161 VAL CA C 65.598 0.23 1 732 . 161 VAL CB C 30.508 0.23 1 733 . 161 VAL C C 176.970 0.11 1 734 . 162 ASN N N 118.085 0.22 1 735 . 162 ASN H H 7.542 0.012 1 736 . 162 ASN CA C 56.585 0.23 1 737 . 162 ASN CB C 38.742 0.23 1 738 . 162 ASN C C 176.708 0.11 1 739 . 163 ALA N N 120.699 0.22 1 740 . 163 ALA H H 7.797 0.012 1 741 . 163 ALA CA C 53.780 0.23 1 742 . 163 ALA CB C 18.844 0.23 1 743 . 163 ALA C C 180.854 0.11 1 744 . 164 GLU N N 121.098 0.22 1 745 . 164 GLU H H 8.490 0.012 1 746 . 164 GLU CA C 58.186 0.23 1 747 . 164 GLU CB C 29.300 0.23 1 748 . 164 GLU C C 179.091 0.11 1 749 . 165 LEU N N 121.165 0.22 1 750 . 165 LEU H H 8.567 0.012 1 751 . 165 LEU CA C 56.941 0.23 1 752 . 165 LEU CB C 40.953 0.23 1 753 . 165 LEU C C 178.663 0.11 1 754 . 166 ASN N N 115.353 0.22 1 755 . 166 ASN H H 8.356 0.012 1 756 . 166 ASN CA C 54.396 0.23 1 757 . 166 ASN CB C 37.551 0.23 1 758 . 166 ASN C C 176.970 0.11 1 759 . 167 GLU N N 119.875 0.22 1 760 . 167 GLU H H 7.533 0.012 1 761 . 167 GLU CA C 56.971 0.23 1 762 . 167 GLU CB C 28.540 0.23 1 763 . 167 GLU C C 177.548 0.11 1 764 . 168 LEU N N 119.226 0.22 1 765 . 168 LEU H H 7.810 0.012 1 766 . 168 LEU CA C 55.603 0.23 1 767 . 168 LEU CB C 41.474 0.23 1 768 . 168 LEU C C 178.296 0.11 1 769 . 169 GLN N N 117.322 0.22 1 770 . 169 GLN H H 8.077 0.012 1 771 . 169 GLN CA C 55.726 0.23 1 772 . 169 GLN CB C 27.954 0.23 1 773 . 169 GLN C C 176.361 0.11 1 774 . 170 HIS N N 117.913 0.22 1 775 . 170 HIS H H 7.962 0.012 1 776 . 170 HIS CA C 55.398 0.23 1 777 . 170 HIS CB C 28.618 0.23 1 778 . 170 HIS C C 173.973 0.11 1 779 . 171 HIS N N 125.138 0.22 1 780 . 171 HIS H H 8.241 0.012 1 781 . 171 HIS CA C 56.487 0.23 1 782 . 171 HIS CB C 29.010 0.23 1 783 . 171 HIS C C 179.126 0.11 1 784 . 172 HIS N N 125.138 0.22 1 785 . 172 HIS H H 8.241 0.012 1 786 . 172 HIS CA C 56.487 0.23 1 787 . 172 HIS CB C 29.010 0.23 1 788 . 172 HIS C C 179.126 0.11 1 789 . 173 HIS N N 125.138 0.22 1 790 . 173 HIS H H 8.241 0.012 1 791 . 173 HIS CA C 56.487 0.23 1 792 . 173 HIS CB C 29.010 0.23 1 793 . 173 HIS C C 179.126 0.11 1 794 . 174 HIS N N 125.138 0.22 1 795 . 174 HIS H H 8.241 0.012 1 796 . 174 HIS CA C 56.487 0.23 1 797 . 174 HIS CB C 29.010 0.23 1 798 . 174 HIS C C 179.126 0.11 1 799 . 175 HIS N N 125.138 0.22 1 800 . 175 HIS H H 8.241 0.012 1 801 . 175 HIS CA C 56.487 0.23 1 802 . 175 HIS CB C 29.010 0.23 1 803 . 175 HIS C C 179.126 0.11 1 stop_ save_