data_5217 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Solution Structure and DNA Binding Properties of the C-Terminal Domain of UvrC from E. coli ; _BMRB_accession_number 5217 _BMRB_flat_file_name bmr5217.str _Entry_type original _Submission_date 2001-11-23 _Accession_date 2001-11-26 _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 Singh Shanteri . . 2 Folkers Gert E . 3 Bonvin Alexandre 'M. J. J.' . 4 Wechselberger Rainer . . 5 Niztayev Alidin . . 6 Boelens Rolf . . 7 Kaptein Robert . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 373 "13C chemical shifts" 261 "15N chemical shifts" 67 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2003-01-14 original author . stop_ _Original_release_date 2003-01-14 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; Solution Structure and DNA-binding Properties of the C-Terminal Domain of UvrC from E. coli ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code 22313337 _PubMed_ID 12426397 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Singh Shanteri . . 2 Folkers Gert E. . 3 Bonvin Alexandre M. . 4 Boelens Rolf . . 5 Wechselberger Rainer . . 6 Niztayev Alidin . . 7 Kaptein Robert . . stop_ _Journal_abbreviation 'EMBO J.' _Journal_volume 21 _Journal_issue 22 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 6257 _Page_last 6266 _Year 2002 _Details . loop_ _Keyword 'DNA binding domain' 'Helix-hairpin-helix motif' 'NER Protein' 'UvrC CTD' stop_ save_ ################################## # Molecular system description # ################################## save_system_UvrC_CTD _Saveframe_category molecular_system _Mol_system_name 'UvrC C-terminal domain' _Abbreviation_common 'UvrC CTD' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'UvrC CTD' $UvrC stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state monomer _System_paramagnetic no _System_thiol_state 'not present' loop_ _Biological_function 'Binds to bubble DNA with minimum 6 unpaired bases in the middle' 'Non-Sequence Specific DNA binding' 'Participates in the 5- incision of the DNA in Nuclear Excision Repair' stop_ _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_UvrC _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'UV Repair protein C' _Name_variant UvrC _Abbreviation_common Exi-nuclease _Molecular_mass 8562.82 _Mol_thiol_state 'not present' _Details ; HhH domain, Binds to bubble type DNA with minimum 6 unpaired bubble Structurally resembles HhH domains of RuvA protein and DNA Ligase protein. ; ############################## # Polymer residue sequence # ############################## _Residue_count 78 _Mol_residue_sequence ; MGSSHHHHHHSSGLVPRGSH MNTSSLETIEGVGPKRRQML LKYMGGLQGLRNASVEEIAK VPGISQGLAEKIFWSLKH ; loop_ _Residue_seq_code _Residue_label 1 MET 2 GLY 3 SER 4 SER 5 HIS 6 HIS 7 HIS 8 HIS 9 HIS 10 HIS 11 SER 12 SER 13 GLY 14 LEU 15 VAL 16 PRO 17 ARG 18 GLY 19 SER 20 HIS 21 MET 22 ASN 23 THR 24 SER 25 SER 26 LEU 27 GLU 28 THR 29 ILE 30 GLU 31 GLY 32 VAL 33 GLY 34 PRO 35 LYS 36 ARG 37 ARG 38 GLN 39 MET 40 LEU 41 LEU 42 LYS 43 TYR 44 MET 45 GLY 46 GLY 47 LEU 48 GLN 49 GLY 50 LEU 51 ARG 52 ASN 53 ALA 54 SER 55 VAL 56 GLU 57 GLU 58 ILE 59 ALA 60 LYS 61 VAL 62 PRO 63 GLY 64 ILE 65 SER 66 GLN 67 GLY 68 LEU 69 ALA 70 GLU 71 LYS 72 ILE 73 PHE 74 TRP 75 SER 76 LEU 77 LYS 78 HIS stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2014-10-26 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 1KFT "Solution Structure Of The C-Terminal Domain Of Uvrc From E- Coli" 100.00 78 100.00 100.00 2.67e-47 GB AHR43889 "excinuclease ABC subunit C [Salmonella enterica subsp. enterica serovar Enteritidis str. SA20095440]" 51.28 40 100.00 100.00 8.65e-19 GB AHS24459 "excinuclease ABC subunit C [Salmonella enterica subsp. enterica serovar Enteritidis str. EC20120677]" 51.28 40 100.00 100.00 8.65e-19 GB AHS50436 "excinuclease ABC subunit C [Salmonella enterica subsp. enterica serovar Enteritidis str. EC20121004]" 51.28 40 100.00 100.00 8.65e-19 GB AHS52317 "excinuclease ABC subunit C [Salmonella enterica subsp. enterica serovar Enteritidis str. EC20121541]" 51.28 40 100.00 100.00 8.65e-19 GB EFZ51080 "uvrABC system C domain protein [Shigella sonnei 53G]" 51.28 40 100.00 100.00 8.65e-19 REF WP_001345512 "MULTISPECIES: excinuclease ABC subunit C [Enterobacteriaceae]" 51.28 40 100.00 100.00 8.65e-19 REF WP_023252848 "excinuclease ABC subunit C [Salmonella enterica]" 64.10 50 98.00 100.00 4.51e-26 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species _Strain _Plasmid _Gene_mnemonic _Details $UvrC 'Escherichia coli' 562 Eubacteria . Escherichia coli K-12 DE3 UvrC 'Nuclear Excision Repair protein C.' 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 $UvrC 'recombinant technology' . . . . . stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Saveframe_category sample _Sample_type solution _Details 'A complete protease inhibitor was added to the sample.' loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $UvrC 1.0 mM [U-15N] NaCl 300 mM . 'sodium phosphate buffer' 50 mM . stop_ save_ save_sample_2 _Saveframe_category sample _Sample_type solution _Details 'A complete protease inhibitor was added to the sample.' loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $UvrC 1.0 mM '[U-15N; U-13C]' NaCl 300 mM . 'sodium phosphate buffer' 50 mM . stop_ save_ ############################ # Computer software used # ############################ save_NMRPipe _Saveframe_category software _Name NMRPipe _Version 1.8 loop_ _Task 'NMR data processing' stop_ _Details 'Delaglio, F., Grzesiek, S., Vuister, G., Zhu, G., Pfeifer, J., and Bax, A.' save_ save_NmrView _Saveframe_category software _Name NMRView _Version 4.1.3 loop_ _Task 'NMR data analysis' stop_ _Details 'Bruce A. Johnson' save_ save_ARIA _Saveframe_category software _Name ARIA _Version 1.0 loop_ _Task 'ambiguous NOE assignment' 'structure calculation' stop_ _Details 'S.,Jens Linge, Michael Nilges' save_ save_CNS _Saveframe_category software _Name CNS _Version 1.0 loop_ _Task 'structure calculation' stop_ _Details ; A.T.Brunger, P.D.Adams, G.M.Clore, W.L.DeLano,P.Gros, R.W.Grosse-Kunstleve, J.-S.Jiang,J.Kuszewski, M.Nilges, N.S.Pannu, R.J.Read, L.M.Rice, T.Simonson, G.L.Warren. ; save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model DRX _Field_strength 500 _Details . save_ save_NMR_spectrometer_2 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model AMX _Field_strength 600 _Details . save_ save_NMR_spectrometer_3 _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model INOVA _Field_strength 750 _Details . save_ ############################# # NMR applied experiments # ############################# save_HNCA_1 _Saveframe_category NMR_applied_experiment _Experiment_name HNCA _Sample_label . save_ save_HNCO_2 _Saveframe_category NMR_applied_experiment _Experiment_name HNCO _Sample_label . save_ save_HN(CO)CA_3 _Saveframe_category NMR_applied_experiment _Experiment_name HN(CO)CA _Sample_label . save_ save_CBCANH_4 _Saveframe_category NMR_applied_experiment _Experiment_name CBCANH _Sample_label . save_ save_1H-15N_TOCSY_HSQC_5 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-15N TOCSY HSQC' _Sample_label . save_ save_1H-15N_NOESY_HSQC_6 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-15N NOESY HSQC' _Sample_label . save_ save_1H-13C-H(C)CH_TOCSY_7 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-13C-H(C)CH TOCSY' _Sample_label . save_ save_1H-13C-(H)CCH_TOCSY_8 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-13C-(H)CCH TOCSY' _Sample_label . save_ save_1H-15N_NOESY_HSQC_9 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-15N NOESY HSQC' _Sample_label . save_ save_2D-NOESY_10 _Saveframe_category NMR_applied_experiment _Experiment_name 2D-NOESY _Sample_label . save_ ####################### # Sample conditions # ####################### save_Ex-cond_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units 'ionic strength' 0.3 0.05 M pH 6.8 0.2 na temperature 300 1.0 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 C 13 'methyl protons' ppm 0.0 . indirect . . . 0.251449530 H2O H 1 protons ppm 4.75 internal direct . internal parallel 1.000000000 DSS N 15 'methyl protons' ppm 0.0 . 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_1 _Saveframe_category assigned_chemical_shifts _Details ; The unassigned signals may correspond to the residues from His-tag region. ; loop_ _Sample_label $sample_1 $sample_2 stop_ _Sample_conditions_label $Ex-cond_1 _Chem_shift_reference_set_label $chemical_shift_reference _Mol_system_component_name 'UvrC CTD' _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 . 12 SER N N 110.537 0.5 1 2 . 12 SER CA C 58.600 0.5 1 3 . 12 SER CB C 63.800 0.5 1 4 . 13 GLY N N 110.539 0.5 1 5 . 13 GLY H H 8.368 0.04 1 6 . 13 GLY CA C 45.352 0.5 1 7 . 13 GLY HA3 H 3.936 0.04 2 8 . 14 LEU N N 121.527 0.5 1 9 . 14 LEU H H 8.018 0.04 1 10 . 14 LEU CA C 55.133 0.5 1 11 . 14 LEU HA H 4.327 0.04 1 12 . 14 LEU CB C 42.324 0.5 1 13 . 14 LEU CG C 24.614 0.5 1 14 . 14 LEU HG H 1.527 0.04 1 15 . 14 LEU CD1 C 23.372 0.5 1 16 . 14 LEU HD1 H 0.830 0.04 2 17 . 14 LEU HD2 H 0.775 0.04 2 18 . 14 LEU C C 173.844 0.5 1 19 . 15 VAL N N 122.506 0.5 1 20 . 15 VAL H H 8.045 0.04 1 21 . 15 VAL CA C 59.681 0.5 1 22 . 15 VAL HA H 4.344 0.04 1 23 . 15 VAL CB C 32.645 0.5 1 24 . 15 VAL HB H 2.028 0.04 1 25 . 15 VAL CG2 C 20.300 0.5 1 26 . 15 VAL HG2 H 0.889 0.04 2 27 . 15 VAL C C 177.077 0.5 1 28 . 16 PRO CA C 63.084 0.5 1 29 . 16 PRO CB C 31.900 0.5 1 30 . 16 PRO HB3 H 2.227 0.04 2 31 . 16 PRO HB2 H 1.784 0.04 2 32 . 16 PRO CG C 27.300 0.5 1 33 . 16 PRO CD C 50.800 0.5 1 34 . 16 PRO HD3 H 3.820 0.04 2 35 . 16 PRO HD2 H 3.620 0.04 2 36 . 17 ARG N N 122.016 0.5 1 37 . 17 ARG H H 8.440 0.04 1 38 . 17 ARG CA C 56.335 0.5 1 39 . 17 ARG HA H 4.383 0.04 1 40 . 17 ARG CB C 30.890 0.5 1 41 . 17 ARG HB3 H 1.795 0.04 2 42 . 17 ARG HB2 H 1.700 0.04 2 43 . 17 ARG CG C 26.544 0.5 1 44 . 17 ARG CD C 43.451 0.5 1 45 . 17 ARG HD3 H 3.207 0.04 2 46 . 17 ARG HD2 H 3.166 0.04 2 47 . 17 ARG C C 176.870 0.5 1 48 . 18 GLY N N 110.207 0.5 1 49 . 18 GLY H H 8.453 0.04 1 50 . 18 GLY CA C 45.500 0.5 1 51 . 18 GLY HA3 H 4.136 0.04 2 52 . 18 GLY HA2 H 3.615 0.04 2 53 . 18 GLY C C 174.983 0.5 1 54 . 19 SER N N 115.658 0.5 1 55 . 19 SER H H 8.189 0.04 1 56 . 19 SER CA C 58.300 0.5 1 57 . 19 SER HA H 4.400 0.04 1 58 . 19 SER CB C 63.900 0.5 1 59 . 19 SER HB3 H 3.777 0.04 1 60 . 19 SER HB2 H 3.777 0.04 1 61 . 21 MET CA C 55.400 0.5 1 62 . 21 MET CB C 32.800 0.5 1 63 . 22 ASN N N 120.006 0.5 1 64 . 22 ASN CA C 53.500 0.5 1 65 . 22 ASN CB C 38.900 0.5 1 66 . 22 ASN HB3 H 2.872 0.04 2 67 . 22 ASN HB2 H 2.808 0.04 2 68 . 23 THR N N 113.929 0.5 1 69 . 23 THR H H 8.230 0.04 1 70 . 23 THR CA C 62.200 0.5 1 71 . 23 THR CB C 69.400 0.5 1 72 . 23 THR HB H 4.265 0.04 1 73 . 23 THR HG2 H 1.162 0.04 1 74 . 24 SER N N 118.280 0.5 1 75 . 24 SER H H 8.391 0.04 1 76 . 24 SER CA C 59.000 0.5 1 77 . 24 SER HA H 4.274 0.04 1 78 . 24 SER CB C 63.600 0.5 1 79 . 24 SER HB3 H 4.000 0.04 2 80 . 24 SER HB2 H 4.041 0.04 2 81 . 25 SER N N 117.507 0.5 1 82 . 25 SER H H 8.306 0.04 1 83 . 25 SER CA C 59.011 0.5 1 84 . 25 SER HA H 4.400 0.04 1 85 . 25 SER CB C 63.641 0.5 1 86 . 25 SER HB3 H 3.793 0.04 1 87 . 25 SER HB2 H 3.793 0.04 1 88 . 25 SER C C 174.973 0.5 1 89 . 26 LEU N N 122.457 0.5 1 90 . 26 LEU H H 8.279 0.04 1 91 . 26 LEU CA C 56.605 0.5 1 92 . 26 LEU HA H 4.143 0.04 1 93 . 26 LEU CB C 42.216 0.5 1 94 . 26 LEU HB3 H 1.600 0.04 1 95 . 26 LEU HB2 H 1.600 0.04 1 96 . 26 LEU CG C 27.500 0.5 1 97 . 26 LEU HG H 1.625 0.04 1 98 . 26 LEU CD1 C 25.100 0.5 1 99 . 26 LEU HD1 H 0.865 0.04 2 100 . 26 LEU CD2 C 25.100 0.5 1 101 . 26 LEU HD2 H 0.805 0.04 2 102 . 26 LEU C C 175.267 0.5 1 103 . 27 GLU N N 116.497 0.5 1 104 . 27 GLU H H 8.310 0.04 1 105 . 27 GLU CA C 58.200 0.5 1 106 . 27 GLU HA H 3.865 0.04 1 107 . 27 GLU CB C 29.600 0.5 1 108 . 27 GLU HB3 H 1.981 0.04 2 109 . 27 GLU HB2 H 1.853 0.04 2 110 . 27 GLU CG C 36.900 0.5 1 111 . 27 GLU HG3 H 2.294 0.04 2 112 . 27 GLU HG2 H 2.218 0.04 2 113 . 27 GLU C C 177.537 0.5 1 114 . 28 THR N N 109.239 0.5 1 115 . 28 THR H H 7.621 0.04 1 116 . 28 THR CA C 61.838 0.5 1 117 . 28 THR HA H 4.300 0.04 1 118 . 28 THR CB C 69.134 0.5 1 119 . 28 THR HB H 4.350 0.04 1 120 . 28 THR CG2 C 21.800 0.5 1 121 . 28 THR HG2 H 1.177 0.04 1 122 . 28 THR C C 176.808 0.5 1 123 . 29 ILE N N 123.557 0.5 1 124 . 29 ILE H H 7.566 0.04 1 125 . 29 ILE CA C 61.583 0.5 1 126 . 29 ILE HA H 4.007 0.04 1 127 . 29 ILE CB C 38.182 0.5 1 128 . 29 ILE HB H 1.743 0.04 1 129 . 29 ILE CG1 C 27.300 0.5 2 130 . 29 ILE HG13 H 1.000 0.04 1 131 . 29 ILE HG12 H 1.755 0.04 1 132 . 29 ILE CD1 C 14.600 0.5 1 133 . 29 ILE HD1 H 0.845 0.04 1 134 . 29 ILE CG2 C 17.600 0.5 1 135 . 29 ILE HG2 H 0.815 0.04 1 136 . 29 ILE C C 174.498 0.5 1 137 . 30 GLU N N 130.032 0.5 1 138 . 30 GLU H H 8.686 0.04 1 139 . 30 GLU CA C 58.144 0.5 1 140 . 30 GLU HA H 4.004 0.04 1 141 . 30 GLU CB C 29.688 0.5 1 142 . 30 GLU HB3 H 1.958 0.04 1 143 . 30 GLU HB2 H 1.958 0.04 1 144 . 30 GLU CG C 36.100 0.5 1 145 . 30 GLU HG3 H 2.290 0.04 2 146 . 30 GLU HG2 H 2.225 0.04 2 147 . 30 GLU C C 175.956 0.5 1 148 . 31 GLY N N 111.124 0.5 1 149 . 31 GLY H H 8.582 0.04 1 150 . 31 GLY CA C 44.987 0.5 1 151 . 31 GLY HA3 H 4.231 0.04 2 152 . 31 GLY HA2 H 3.717 0.04 2 153 . 31 GLY C C 176.813 0.5 1 154 . 32 VAL N N 119.904 0.5 1 155 . 32 VAL H H 7.754 0.04 1 156 . 32 VAL CA C 62.451 0.5 1 157 . 32 VAL HA H 4.077 0.04 1 158 . 32 VAL CB C 30.975 0.5 1 159 . 32 VAL HB H 2.290 0.04 1 160 . 32 VAL CG2 C 22.160 0.5 1 161 . 32 VAL HG2 H 0.848 0.04 2 162 . 32 VAL CG1 C 22.400 0.5 1 163 . 32 VAL HG1 H 0.756 0.04 2 164 . 32 VAL C C 174.158 0.5 1 165 . 33 GLY N N 111.949 0.5 1 166 . 33 GLY H H 7.967 0.04 1 167 . 33 GLY CA C 44.980 0.5 1 168 . 33 GLY HA3 H 4.320 0.04 2 169 . 33 GLY HA2 H 4.187 0.04 2 170 . 33 GLY C C 175.289 0.5 1 171 . 34 PRO CA C 65.900 0.5 1 172 . 34 PRO HA H 4.411 0.04 1 173 . 34 PRO CB C 32.300 0.5 1 174 . 34 PRO HB3 H 2.375 0.04 2 175 . 34 PRO HB2 H 1.987 0.04 2 176 . 34 PRO CG C 27.400 0.5 1 177 . 34 PRO HG3 H 2.162 0.04 2 178 . 34 PRO HG2 H 2.050 0.04 2 179 . 34 PRO CD C 49.500 0.5 1 180 . 34 PRO HD3 H 3.660 0.04 2 181 . 34 PRO HD2 H 3.825 0.04 2 182 . 35 LYS N N 118.766 0.5 1 183 . 35 LYS H H 8.203 0.04 1 184 . 35 LYS CA C 59.521 0.5 1 185 . 35 LYS HA H 4.158 0.04 1 186 . 35 LYS CB C 31.817 0.5 1 187 . 35 LYS HB3 H 1.963 0.04 2 188 . 35 LYS HB2 H 1.885 0.04 2 189 . 35 LYS CG C 29.200 0.5 1 190 . 35 LYS HG3 H 1.720 0.04 1 191 . 35 LYS HG2 H 1.720 0.04 1 192 . 35 LYS CD C 25.200 0.5 1 193 . 35 LYS HD3 H 1.400 0.04 2 194 . 35 LYS HD2 H 1.510 0.04 2 195 . 35 LYS CE C 42.200 0.5 1 196 . 35 LYS HE3 H 3.000 0.04 1 197 . 35 LYS HE2 H 3.000 0.04 1 198 . 35 LYS C C 179.206 0.5 1 199 . 36 ARG N N 120.327 0.5 1 200 . 36 ARG H H 8.099 0.04 1 201 . 36 ARG CA C 59.466 0.5 1 202 . 36 ARG HA H 4.074 0.04 1 203 . 36 ARG CB C 30.269 0.5 1 204 . 36 ARG HB3 H 1.913 0.04 2 205 . 36 ARG HB2 H 1.585 0.04 2 206 . 36 ARG CG C 28.800 0.5 1 207 . 36 ARG HG3 H 1.583 0.04 2 208 . 36 ARG HG2 H 1.878 0.04 2 209 . 36 ARG CD C 43.636 0.5 1 210 . 36 ARG HD3 H 3.420 0.04 2 211 . 36 ARG HD2 H 3.050 0.04 2 212 . 36 ARG C C 179.592 0.5 1 213 . 37 ARG N N 119.188 0.5 1 214 . 37 ARG H H 8.544 0.04 1 215 . 37 ARG CA C 60.594 0.5 1 216 . 37 ARG HA H 3.671 0.04 1 217 . 37 ARG CB C 29.903 0.5 1 218 . 37 ARG HB3 H 1.889 0.04 2 219 . 37 ARG HB2 H 1.831 0.04 2 220 . 37 ARG CG C 27.700 0.5 1 221 . 37 ARG HG3 H 1.580 0.04 2 222 . 37 ARG HG2 H 1.450 0.04 2 223 . 37 ARG CD C 43.800 0.5 1 224 . 37 ARG HD3 H 3.180 0.04 2 225 . 37 ARG HD2 H 3.132 0.04 2 226 . 37 ARG C C 178.213 0.5 1 227 . 38 GLN N N 116.587 0.5 1 228 . 38 GLN H H 7.780 0.04 1 229 . 38 GLN CA C 59.000 0.5 1 230 . 38 GLN HA H 4.014 0.04 1 231 . 38 GLN CB C 28.412 0.5 1 232 . 38 GLN HB3 H 2.211 0.04 1 233 . 38 GLN HB2 H 2.211 0.04 1 234 . 38 GLN CG C 33.900 0.5 1 235 . 38 GLN HG3 H 2.570 0.04 2 236 . 38 GLN HG2 H 2.435 0.04 2 237 . 38 GLN NE2 N 111.670 0.5 1 238 . 38 GLN HE21 H 7.409 0.04 2 239 . 38 GLN HE22 H 6.847 0.04 2 240 . 38 GLN C C 177.215 0.5 1 241 . 39 MET N N 119.254 0.5 1 242 . 39 MET H H 7.902 0.04 1 243 . 39 MET CA C 59.032 0.5 1 244 . 39 MET HA H 4.284 0.04 1 245 . 39 MET CB C 32.304 0.5 1 246 . 39 MET HB3 H 2.747 0.04 2 247 . 39 MET HB2 H 2.675 0.04 2 248 . 39 MET CG C 32.304 0.5 1 249 . 39 MET HG3 H 2.225 0.04 2 250 . 39 MET HG2 H 2.090 0.04 2 251 . 39 MET C C 178.950 0.5 1 252 . 40 LEU N N 120.411 0.5 1 253 . 40 LEU H H 8.487 0.04 1 254 . 40 LEU CA C 58.605 0.5 1 255 . 40 LEU HA H 3.960 0.04 1 256 . 40 LEU CB C 42.756 0.5 1 257 . 40 LEU HB3 H 1.908 0.04 2 258 . 40 LEU HB2 H 1.593 0.04 2 259 . 40 LEU CG C 27.300 0.5 1 260 . 40 LEU HG H 1.672 0.04 1 261 . 40 LEU CD1 C 25.810 0.5 1 262 . 40 LEU HD1 H 0.860 0.04 2 263 . 40 LEU CD2 C 25.200 0.5 1 264 . 40 LEU HD2 H 0.870 0.04 2 265 . 40 LEU C C 178.302 0.5 1 266 . 41 LEU N N 116.672 0.5 1 267 . 41 LEU H H 7.994 0.04 1 268 . 41 LEU CA C 58.270 0.5 1 269 . 41 LEU HA H 3.774 0.04 1 270 . 41 LEU CB C 41.242 0.5 1 271 . 41 LEU HB3 H 1.885 0.04 2 272 . 41 LEU HB2 H 1.460 0.04 2 273 . 41 LEU CG C 27.100 0.5 1 274 . 41 LEU HG H 1.765 0.04 1 275 . 41 LEU CD1 C 25.300 0.5 1 276 . 41 LEU HD1 H 0.859 0.04 2 277 . 41 LEU CD2 C 22.500 0.5 1 278 . 41 LEU HD2 H 0.692 0.04 2 279 . 41 LEU C C 178.198 0.5 1 280 . 42 LYS N N 120.081 0.5 1 281 . 42 LYS H H 8.119 0.04 1 282 . 42 LYS CA C 59.373 0.5 1 283 . 42 LYS HA H 4.093 0.04 1 284 . 42 LYS CB C 32.600 0.5 1 285 . 42 LYS HB3 H 2.000 0.04 1 286 . 42 LYS HB2 H 2.000 0.04 1 287 . 42 LYS CG C 29.230 0.5 1 288 . 42 LYS HG3 H 1.647 0.04 1 289 . 42 LYS HG2 H 1.647 0.04 1 290 . 42 LYS CD C 24.700 0.5 1 291 . 42 LYS HD3 H 1.450 0.04 2 292 . 42 LYS HD2 H 1.274 0.04 2 293 . 42 LYS CE C 42.300 0.5 1 294 . 42 LYS HE3 H 3.000 0.04 1 295 . 42 LYS HE2 H 3.000 0.04 1 296 . 42 LYS C C 175.651 0.5 1 297 . 43 TYR N N 118.667 0.5 1 298 . 43 TYR H H 8.612 0.04 1 299 . 43 TYR CA C 61.726 0.5 1 300 . 43 TYR HA H 4.118 0.04 1 301 . 43 TYR CB C 39.203 0.5 1 302 . 43 TYR HB3 H 3.181 0.04 2 303 . 43 TYR HB2 H 3.031 0.04 2 304 . 43 TYR HD1 H 7.309 0.04 1 305 . 43 TYR HE1 H 6.876 0.04 1 306 . 43 TYR HE2 H 6.876 0.04 1 307 . 43 TYR HD2 H 7.309 0.04 1 308 . 43 TYR C C 179.482 0.5 1 309 . 44 MET N N 112.842 0.5 1 310 . 44 MET H H 7.931 0.04 1 311 . 44 MET CA C 54.370 0.5 1 312 . 44 MET HA H 4.665 0.04 1 313 . 44 MET CB C 32.583 0.5 1 314 . 44 MET HB3 H 1.970 0.04 2 315 . 44 MET HB2 H 2.110 0.04 2 316 . 44 MET CG C 33.800 0.5 1 317 . 44 MET HG3 H 2.615 0.04 2 318 . 44 MET HG2 H 2.656 0.04 2 319 . 44 MET HE H 1.981 0.04 1 320 . 44 MET C C 178.101 0.5 1 321 . 45 GLY N N 107.234 0.5 1 322 . 45 GLY H H 7.536 0.04 1 323 . 45 GLY CA C 46.381 0.5 1 324 . 45 GLY HA3 H 4.100 0.04 2 325 . 45 GLY HA2 H 3.900 0.04 2 326 . 45 GLY C C 176.266 0.5 1 327 . 46 GLY N N 108.188 0.5 1 328 . 46 GLY H H 8.526 0.04 1 329 . 46 GLY CA C 43.889 0.5 1 330 . 46 GLY HA3 H 4.533 0.04 2 331 . 46 GLY HA2 H 3.688 0.04 2 332 . 46 GLY C C 175.537 0.5 1 333 . 47 LEU N N 121.189 0.5 1 334 . 47 LEU H H 8.674 0.04 1 335 . 47 LEU CA C 58.055 0.5 1 336 . 47 LEU HA H 3.875 0.04 1 337 . 47 LEU CB C 41.770 0.5 1 338 . 47 LEU HB3 H 1.683 0.04 2 339 . 47 LEU HB2 H 1.543 0.04 2 340 . 47 LEU CG C 27.200 0.5 1 341 . 47 LEU HG H 1.540 0.04 1 342 . 47 LEU CD1 C 25.100 0.5 1 343 . 47 LEU HD1 H 0.850 0.04 2 344 . 47 LEU CD2 C 23.600 0.5 1 345 . 47 LEU HD2 H 0.920 0.04 2 346 . 47 LEU C C 173.199 0.5 1 347 . 48 GLN N N 117.348 0.5 1 348 . 48 GLN H H 8.714 0.04 1 349 . 48 GLN CA C 58.909 0.5 1 350 . 48 GLN HA H 3.906 0.04 1 351 . 48 GLN CB C 27.818 0.5 1 352 . 48 GLN HB3 H 2.005 0.04 2 353 . 48 GLN HB2 H 2.075 0.04 2 354 . 48 GLN CG C 33.800 0.5 1 355 . 48 GLN HG3 H 2.391 0.04 1 356 . 48 GLN HG2 H 2.391 0.04 1 357 . 48 GLN NE2 N 113.123 0.5 1 358 . 48 GLN HE21 H 7.475 0.04 2 359 . 48 GLN HE22 H 6.932 0.04 2 360 . 48 GLN C C 178.603 0.5 1 361 . 49 GLY N N 106.202 0.5 1 362 . 49 GLY H H 7.379 0.04 1 363 . 49 GLY CA C 46.510 0.5 1 364 . 49 GLY HA3 H 4.154 0.04 2 365 . 49 GLY HA2 H 3.837 0.04 2 366 . 49 GLY C C 178.375 0.5 1 367 . 50 LEU N N 123.135 0.5 1 368 . 50 LEU H H 7.951 0.04 1 369 . 50 LEU CA C 57.704 0.5 1 370 . 50 LEU HA H 4.100 0.04 1 371 . 50 LEU CB C 41.756 0.5 1 372 . 50 LEU HB3 H 1.960 0.04 2 373 . 50 LEU HB2 H 1.285 0.04 2 374 . 50 LEU CG C 27.100 0.5 1 375 . 50 LEU HG H 1.554 0.04 1 376 . 50 LEU CD1 C 27.100 0.5 1 377 . 50 LEU HD1 H 0.790 0.04 2 378 . 50 LEU CD2 C 24.100 0.5 1 379 . 50 LEU HD2 H 0.880 0.04 2 380 . 50 LEU C C 177.365 0.5 1 381 . 51 ARG N N 116.649 0.5 1 382 . 51 ARG H H 8.338 0.04 1 383 . 51 ARG CA C 59.316 0.5 1 384 . 51 ARG HA H 3.840 0.04 1 385 . 51 ARG CB C 30.300 0.5 1 386 . 51 ARG HB3 H 1.830 0.04 1 387 . 51 ARG HB2 H 1.830 0.04 1 388 . 51 ARG CG C 28.800 0.5 1 389 . 51 ARG HG3 H 1.830 0.04 2 390 . 51 ARG HG2 H 1.575 0.04 2 391 . 51 ARG CD C 43.800 0.5 1 392 . 51 ARG HD3 H 3.114 0.04 1 393 . 51 ARG HD2 H 3.114 0.04 1 394 . 51 ARG C C 178.322 0.5 1 395 . 52 ASN N N 114.780 0.5 1 396 . 52 ASN H H 7.331 0.04 1 397 . 52 ASN CA C 52.776 0.5 1 398 . 52 ASN HA H 4.815 0.04 1 399 . 52 ASN CB C 39.801 0.5 1 400 . 52 ASN HB3 H 3.002 0.04 2 401 . 52 ASN HB2 H 2.700 0.04 2 402 . 52 ASN ND2 N 112.640 0.5 1 403 . 52 ASN HD21 H 7.598 0.04 2 404 . 52 ASN HD22 H 6.883 0.04 2 405 . 52 ASN C C 176.524 0.5 1 406 . 53 ALA N N 124.021 0.5 1 407 . 53 ALA H H 7.290 0.04 1 408 . 53 ALA CA C 52.316 0.5 1 409 . 53 ALA HA H 4.546 0.04 1 410 . 53 ALA CB C 20.665 0.5 1 411 . 53 ALA HB H 1.596 0.04 1 412 . 53 ALA C C 174.578 0.5 1 413 . 54 SER N N 116.936 0.5 1 414 . 54 SER H H 8.568 0.04 1 415 . 54 SER CA C 56.555 0.5 1 416 . 54 SER HA H 4.620 0.04 1 417 . 54 SER CB C 65.817 0.5 1 418 . 54 SER HB3 H 4.240 0.04 2 419 . 54 SER HB2 H 3.980 0.04 2 420 . 54 SER C C 177.335 0.5 1 421 . 55 VAL N N 120.830 0.5 1 422 . 55 VAL H H 8.163 0.04 1 423 . 55 VAL CA C 67.294 0.5 1 424 . 55 VAL HA H 3.244 0.04 1 425 . 55 VAL CB C 31.345 0.5 1 426 . 55 VAL HB H 1.448 0.04 1 427 . 55 VAL CG2 C 21.500 0.5 1 428 . 55 VAL HG2 H 0.715 0.04 2 429 . 55 VAL CG1 C 22.800 0.5 1 430 . 55 VAL HG1 H 0.419 0.04 2 431 . 55 VAL C C 175.091 0.5 1 432 . 56 GLU N N 116.610 0.5 1 433 . 56 GLU H H 8.241 0.04 1 434 . 56 GLU CA C 59.605 0.5 1 435 . 56 GLU HA H 3.865 0.04 1 436 . 56 GLU CB C 29.090 0.5 1 437 . 56 GLU HB3 H 1.820 0.04 2 438 . 56 GLU HB2 H 1.950 0.04 2 439 . 56 GLU CG C 37.100 0.5 1 440 . 56 GLU HG3 H 2.295 0.04 2 441 . 56 GLU HG2 H 2.250 0.04 2 442 . 56 GLU C C 176.965 0.5 1 443 . 57 GLU N N 117.791 0.5 1 444 . 57 GLU H H 7.493 0.04 1 445 . 57 GLU CA C 59.062 0.5 1 446 . 57 GLU HA H 3.903 0.04 1 447 . 57 GLU CB C 30.092 0.5 1 448 . 57 GLU HB3 H 2.306 0.04 2 449 . 57 GLU HB2 H 2.006 0.04 2 450 . 57 GLU CG C 36.900 0.5 1 451 . 57 GLU HG3 H 2.290 0.04 2 452 . 57 GLU HG2 H 2.210 0.04 2 453 . 57 GLU C C 178.867 0.5 1 454 . 58 ILE N N 121.646 0.5 1 455 . 58 ILE H H 8.018 0.04 1 456 . 58 ILE CA C 65.555 0.5 1 457 . 58 ILE HA H 3.485 0.04 1 458 . 58 ILE CB C 38.323 0.5 1 459 . 58 ILE HB H 1.825 0.04 1 460 . 58 ILE CG1 C 29.900 0.5 2 461 . 58 ILE HG13 H 2.040 0.04 1 462 . 58 ILE HG12 H 0.634 0.04 1 463 . 58 ILE CD1 C 13.600 0.5 1 464 . 58 ILE HD1 H 0.958 0.04 1 465 . 58 ILE CG2 C 18.700 0.5 1 466 . 58 ILE HG2 H 0.880 0.04 1 467 . 58 ILE C C 179.599 0.5 1 468 . 59 ALA N N 116.806 0.5 1 469 . 59 ALA H H 7.994 0.04 1 470 . 59 ALA CA C 52.916 0.5 1 471 . 59 ALA HA H 3.886 0.04 1 472 . 59 ALA CB C 17.894 0.5 1 473 . 59 ALA HB H 1.270 0.04 1 474 . 59 ALA C C 176.571 0.5 1 475 . 60 LYS N N 115.965 0.5 1 476 . 60 LYS H H 7.037 0.04 1 477 . 60 LYS CA C 56.396 0.5 1 478 . 60 LYS HA H 4.164 0.04 1 479 . 60 LYS CB C 32.791 0.5 1 480 . 60 LYS HB3 H 1.949 0.04 2 481 . 60 LYS HB2 H 1.800 0.04 2 482 . 60 LYS CG C 29.300 0.5 1 483 . 60 LYS HG3 H 1.710 0.04 1 484 . 60 LYS HG2 H 1.710 0.04 1 485 . 60 LYS CD C 25.300 0.5 1 486 . 60 LYS HD3 H 1.515 0.04 2 487 . 60 LYS HD2 H 1.420 0.04 2 488 . 60 LYS CE C 42.300 0.5 1 489 . 60 LYS HE3 H 2.931 0.04 1 490 . 60 LYS HE2 H 2.931 0.04 1 491 . 60 LYS C C 177.126 0.5 1 492 . 61 VAL N N 124.962 0.5 1 493 . 61 VAL H H 7.544 0.04 1 494 . 61 VAL CA C 61.193 0.5 1 495 . 61 VAL HA H 3.417 0.04 1 496 . 61 VAL CB C 31.441 0.5 1 497 . 61 VAL HB H 2.053 0.04 1 498 . 61 VAL CG2 C 23.330 0.5 1 499 . 61 VAL HG2 H 0.826 0.04 2 500 . 61 VAL CG1 C 19.910 0.5 1 501 . 61 VAL HG1 H 0.600 0.04 2 502 . 61 VAL C C 177.450 0.5 1 503 . 62 PRO CA C 64.050 0.5 1 504 . 62 PRO HA H 4.400 0.04 1 505 . 62 PRO CB C 31.700 0.5 1 506 . 62 PRO HB3 H 2.220 0.04 2 507 . 62 PRO HB2 H 1.757 0.04 2 508 . 62 PRO CG C 27.800 0.5 1 509 . 62 PRO HG3 H 2.011 0.04 2 510 . 62 PRO HG2 H 1.887 0.04 2 511 . 62 PRO CD C 51.100 0.5 1 512 . 62 PRO HD3 H 3.644 0.04 2 513 . 62 PRO HD2 H 2.936 0.04 2 514 . 63 GLY N N 109.923 0.5 1 515 . 63 GLY H H 8.399 0.04 1 516 . 63 GLY CA C 45.224 0.5 1 517 . 63 GLY HA3 H 4.138 0.04 2 518 . 63 GLY HA2 H 3.648 0.04 2 519 . 63 GLY C C 176.742 0.5 1 520 . 64 ILE N N 121.746 0.5 1 521 . 64 ILE H H 7.658 0.04 1 522 . 64 ILE CA C 58.876 0.5 1 523 . 64 ILE HA H 4.168 0.04 1 524 . 64 ILE CB C 35.231 0.5 1 525 . 64 ILE HB H 2.379 0.04 1 526 . 64 ILE CG1 C 26.600 0.5 2 527 . 64 ILE HG13 H 1.215 0.04 1 528 . 64 ILE HG12 H 1.124 0.04 1 529 . 64 ILE CD1 C 9.930 0.5 1 530 . 64 ILE HD1 H 0.570 0.04 1 531 . 64 ILE CG2 C 17.300 0.5 1 532 . 64 ILE HG2 H 0.772 0.04 1 533 . 64 ILE C C 174.358 0.5 1 534 . 65 SER N N 121.391 0.5 1 535 . 65 SER H H 7.614 0.04 1 536 . 65 SER CA C 57.046 0.5 1 537 . 65 SER HA H 4.510 0.04 1 538 . 65 SER CB C 65.538 0.5 1 539 . 65 SER HB3 H 4.325 0.04 2 540 . 65 SER HB2 H 4.060 0.04 2 541 . 65 SER C C 173.958 0.5 1 542 . 66 GLN N N 121.071 0.5 1 543 . 66 GLN H H 8.924 0.04 1 544 . 66 GLN CA C 59.638 0.5 1 545 . 66 GLN HA H 3.803 0.04 1 546 . 66 GLN CB C 27.778 0.5 1 547 . 66 GLN HB3 H 2.210 0.04 1 548 . 66 GLN HB2 H 2.210 0.04 1 549 . 66 GLN CG C 32.200 0.5 1 550 . 66 GLN HG3 H 2.325 0.04 1 551 . 66 GLN HG2 H 2.325 0.04 1 552 . 66 GLN NE2 N 111.670 0.5 1 553 . 66 GLN HE21 H 7.754 0.04 2 554 . 66 GLN HE22 H 6.439 0.04 2 555 . 66 GLN C C 174.278 0.5 1 556 . 67 GLY N N 104.866 0.5 1 557 . 67 GLY H H 8.586 0.04 1 558 . 67 GLY CA C 46.765 0.5 1 559 . 67 GLY HA3 H 3.826 0.04 1 560 . 67 GLY HA2 H 3.826 0.04 1 561 . 67 GLY C C 178.092 0.5 1 562 . 68 LEU N N 124.593 0.5 1 563 . 68 LEU H H 7.810 0.04 1 564 . 68 LEU CA C 57.135 0.5 1 565 . 68 LEU HA H 4.249 0.04 1 566 . 68 LEU CB C 41.483 0.5 1 567 . 68 LEU HB3 H 1.806 0.04 2 568 . 68 LEU HB2 H 1.594 0.04 2 569 . 68 LEU CG C 26.500 0.5 1 570 . 68 LEU HG H 0.971 0.04 1 571 . 68 LEU CD1 C 23.100 0.5 1 572 . 68 LEU HD1 H 0.979 0.04 1 573 . 68 LEU CD2 C 23.100 0.5 1 574 . 68 LEU HD2 H 0.979 0.04 1 575 . 68 LEU C C 177.111 0.5 1 576 . 69 ALA N N 122.621 0.5 1 577 . 69 ALA H H 8.724 0.04 1 578 . 69 ALA CA C 55.696 0.5 1 579 . 69 ALA HA H 3.800 0.04 1 580 . 69 ALA CB C 18.667 0.5 1 581 . 69 ALA HB H 1.450 0.04 1 582 . 69 ALA C C 178.135 0.5 1 583 . 70 GLU N N 116.169 0.5 1 584 . 70 GLU H H 7.949 0.04 1 585 . 70 GLU CA C 59.919 0.5 1 586 . 70 GLU HA H 3.946 0.04 1 587 . 70 GLU CB C 29.729 0.5 1 588 . 70 GLU HB3 H 2.204 0.04 2 589 . 70 GLU HB2 H 2.180 0.04 2 590 . 70 GLU CG C 37.000 0.5 1 591 . 70 GLU HG3 H 2.586 0.04 2 592 . 70 GLU HG2 H 2.340 0.04 2 593 . 70 GLU C C 179.305 0.5 1 594 . 71 LYS N N 119.355 0.5 1 595 . 71 LYS H H 7.567 0.04 1 596 . 71 LYS CA C 59.648 0.5 1 597 . 71 LYS HA H 4.265 0.04 1 598 . 71 LYS CB C 32.672 0.5 1 599 . 71 LYS HB3 H 2.070 0.04 2 600 . 71 LYS HB2 H 2.040 0.04 2 601 . 71 LYS CG C 29.300 0.5 1 602 . 71 LYS HG3 H 1.688 0.04 2 603 . 71 LYS HG2 H 1.710 0.04 2 604 . 71 LYS CD C 24.800 0.5 1 605 . 71 LYS HD3 H 1.470 0.04 2 606 . 71 LYS HD2 H 1.656 0.04 2 607 . 71 LYS CE C 42.300 0.5 1 608 . 71 LYS HE3 H 2.983 0.04 1 609 . 71 LYS HE2 H 2.983 0.04 1 610 . 71 LYS C C 178.138 0.5 1 611 . 72 ILE N N 121.661 0.5 1 612 . 72 ILE H H 8.940 0.04 1 613 . 72 ILE CA C 65.640 0.5 1 614 . 72 ILE HA H 3.515 0.04 1 615 . 72 ILE CB C 38.370 0.5 1 616 . 72 ILE HB H 1.920 0.04 1 617 . 72 ILE CG1 C 29.500 0.5 2 618 . 72 ILE HG13 H 1.900 0.04 1 619 . 72 ILE HG12 H 0.800 0.04 1 620 . 72 ILE CD1 C 15.000 0.5 1 621 . 72 ILE HD1 H 0.720 0.04 1 622 . 72 ILE CG2 C 17.300 0.5 1 623 . 72 ILE HG2 H 0.830 0.04 1 624 . 72 ILE C C 180.448 0.5 1 625 . 73 PHE N N 119.403 0.5 1 626 . 73 PHE H H 8.515 0.04 1 627 . 73 PHE CA C 61.864 0.5 1 628 . 73 PHE HA H 3.864 0.04 1 629 . 73 PHE CB C 40.630 0.5 1 630 . 73 PHE HB3 H 3.062 0.04 2 631 . 73 PHE HB2 H 2.938 0.04 2 632 . 73 PHE HD1 H 6.493 0.04 1 633 . 73 PHE HE1 H 6.858 0.04 1 634 . 73 PHE HZ H 7.063 0.04 1 635 . 73 PHE HE2 H 6.858 0.04 1 636 . 73 PHE HD2 H 6.493 0.04 1 637 . 73 PHE C C 176.784 0.5 1 638 . 74 TRP N N 116.497 0.5 1 639 . 74 TRP H H 8.310 0.04 1 640 . 74 TRP CA C 60.100 0.5 1 641 . 74 TRP HA H 4.352 0.04 1 642 . 74 TRP CB C 29.300 0.5 1 643 . 74 TRP HB3 H 3.477 0.04 2 644 . 74 TRP HB2 H 3.357 0.04 2 645 . 74 TRP HD1 H 7.517 0.04 1 646 . 74 TRP NE1 N 129.057 0.5 1 647 . 74 TRP HE1 H 10.383 0.04 4 648 . 74 TRP HZ2 H 7.473 0.04 4 649 . 74 TRP HH2 H 7.285 0.04 1 650 . 74 TRP HZ3 H 7.181 0.04 4 651 . 74 TRP HE3 H 7.672 0.04 4 652 . 74 TRP C C 179.287 0.5 1 653 . 75 SER N N 116.497 0.5 1 654 . 75 SER H H 8.310 0.04 1 655 . 75 SER CA C 61.861 0.5 1 656 . 75 SER HA H 4.368 0.04 1 657 . 75 SER CB C 62.925 0.5 1 658 . 75 SER HB3 H 3.486 0.04 2 659 . 75 SER HB2 H 3.362 0.04 2 660 . 75 SER C C 177.553 0.5 1 661 . 76 LEU N N 119.018 0.5 1 662 . 76 LEU H H 7.382 0.04 1 663 . 76 LEU CA C 55.452 0.5 1 664 . 76 LEU HA H 4.198 0.04 1 665 . 76 LEU CB C 42.070 0.5 1 666 . 76 LEU HB3 H 1.712 0.04 2 667 . 76 LEU HB2 H 1.380 0.04 2 668 . 76 LEU CG C 26.400 0.5 1 669 . 76 LEU HG H 1.830 0.04 1 670 . 76 LEU CD1 C 22.700 0.5 1 671 . 76 LEU HD1 H 0.699 0.04 2 672 . 76 LEU CD2 C 26.600 0.5 1 673 . 76 LEU HD2 H 0.655 0.04 2 674 . 76 LEU C C 175.651 0.5 1 675 . 77 LYS N N 118.240 0.5 1 676 . 77 LYS H H 7.175 0.04 1 677 . 77 LYS CA C 55.748 0.5 1 678 . 77 LYS HA H 4.144 0.04 1 679 . 77 LYS CB C 32.718 0.5 1 680 . 77 LYS HB3 H 1.740 0.04 2 681 . 77 LYS HB2 H 1.596 0.04 2 682 . 77 LYS CG C 28.400 0.5 1 683 . 77 LYS HG3 H 1.319 0.04 1 684 . 77 LYS HG2 H 1.319 0.04 1 685 . 77 LYS CD C 24.200 0.5 1 686 . 77 LYS HD3 H 1.150 0.04 1 687 . 77 LYS HD2 H 1.150 0.04 1 688 . 77 LYS CE C 42.200 0.5 1 689 . 77 LYS HE3 H 2.610 0.04 2 690 . 77 LYS HE2 H 2.290 0.04 2 691 . 77 LYS C C 177.227 0.5 1 692 . 78 HIS N N 124.116 0.5 1 693 . 78 HIS H H 7.601 0.04 1 694 . 78 HIS CA C 57.214 0.5 1 695 . 78 HIS HA H 4.381 0.04 1 696 . 78 HIS CB C 30.397 0.5 1 697 . 78 HIS HB3 H 3.173 0.04 2 698 . 78 HIS HB2 H 2.796 0.04 2 699 . 78 HIS HD2 H 6.442 0.04 4 700 . 78 HIS HE1 H 7.762 0.04 4 701 . 78 HIS C C 175.548 0.5 1 stop_ save_