data_6317 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; 1H, 15N and 13C resonance assigment of the transcription factor CylR2 from Enterococcus faecalis ; _BMRB_accession_number 6317 _BMRB_flat_file_name bmr6317.str _Entry_type original _Submission_date 2004-09-20 _Accession_date 2004-09-20 _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 Rumpel Sigrun . . 2 Vijayan Vinesh . . 3 Zweckstetter Markus . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 434 "13C chemical shifts" 327 "15N chemical shifts" 73 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2004-12-22 original author . stop_ _Original_release_date 2004-12-22 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; Structure and DNA-binding properties of the cytolysin regulator CylR2 from Enterococcus faecalis ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 15359276 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Rumpel Sigrun . . 2 Razeto Adelia . . 3 Pillar Chris M. . 4 Vijayan Vinesh . . 5 Taylor Austin . . 6 Giller Karin . . 7 Gilmore Michael S. . 8 Becker Stefan . . 9 Zweckstetter Markus . . stop_ _Journal_abbreviation 'EMBO J.' _Journal_volume 23 _Journal_issue 18 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 3632 _Page_last 3642 _Year 2004 _Details . loop_ _Keyword 'antibiotic-resistant infection' CylR2 'DNA complex' 'NMR spectroscopy' quorum-sensing 'signal transduction' stop_ save_ ################################## # Molecular system description # ################################## save_system_CylR2 _Saveframe_category molecular_system _Mol_system_name 'CylR2 dimer' _Abbreviation_common CylR2 _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'CylR2 subunit 1' $CylR2 'CylR2 subunit 2' $CylR2 stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state dimer _System_paramagnetic no _System_thiol_state 'not present' loop_ _Magnetic_equivalence_ID _Magnetically_equivalent_system_component 1 'CylR2 subunit 1' 1 'CylR2 subunit 2' stop_ loop_ _Biological_function 'repression of cytolysin genes' 'transcription factor' stop_ _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_CylR2 _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'cytolysin regulator R2' _Abbreviation_common CylR2 _Molecular_mass 15431 _Mol_thiol_state 'not present' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 66 _Mol_residue_sequence ; MIINNLKLIREKKKISQSEL AALLEVSRQTINGIEKNKYN PSLQLALKIAYYLNTPLEDI FQWQPE ; loop_ _Residue_seq_code _Residue_label 1 MET 2 ILE 3 ILE 4 ASN 5 ASN 6 LEU 7 LYS 8 LEU 9 ILE 10 ARG 11 GLU 12 LYS 13 LYS 14 LYS 15 ILE 16 SER 17 GLN 18 SER 19 GLU 20 LEU 21 ALA 22 ALA 23 LEU 24 LEU 25 GLU 26 VAL 27 SER 28 ARG 29 GLN 30 THR 31 ILE 32 ASN 33 GLY 34 ILE 35 GLU 36 LYS 37 ASN 38 LYS 39 TYR 40 ASN 41 PRO 42 SER 43 LEU 44 GLN 45 LEU 46 ALA 47 LEU 48 LYS 49 ILE 50 ALA 51 TYR 52 TYR 53 LEU 54 ASN 55 THR 56 PRO 57 LEU 58 GLU 59 ASP 60 ILE 61 PHE 62 GLN 63 TRP 64 GLN 65 PRO 66 GLU stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-01-28 loop_ _Database_name _Database_accession_code _Database_entry_mol_name _Sequence_query_to_submitted_percentage _Sequence_subject_length _Sequence_identity _Sequence_positive _Sequence_homology_expectation_value BMRB 17892 "CylR2, strand 1" 100.00 66 100.00 100.00 1.49e-37 BMRB 17893 CylR2_homodimer 100.00 66 100.00 100.00 1.49e-37 BMRB 17894 CylR2 100.00 66 100.00 100.00 1.49e-37 BMRB 17895 CylR2 100.00 66 100.00 100.00 1.49e-37 BMRB 17896 CylR2 100.00 66 100.00 100.00 1.49e-37 BMRB 17897 CylR2 100.00 66 100.00 100.00 1.49e-37 BMRB 17898 CylR2 100.00 66 100.00 100.00 1.49e-37 PDB 1UTX "Regulation Of Cytolysin Expression By Enterococcus Faecalis: Role Of Cylr2" 100.00 66 100.00 100.00 1.49e-37 PDB 2GZU "High-Resolution Structure Determination Of The Cylr2 Homodimer Using Intermonomer Distances From Paramagnetic Relaxation Enhanc" 100.00 66 100.00 100.00 1.49e-37 PDB 2LYJ "Noe-based 3d Structure Of The Cylr2 Homodimer At 298k" 100.00 66 100.00 100.00 1.49e-37 PDB 2LYK "Noe-based 3d Structure Of The Cylr2 Homodimer At 270k (-3 Celsius Degrees)" 100.00 66 100.00 100.00 1.49e-37 PDB 2LYL "Noe-based 3d Structure Of The Predissociated Homodimer Of Cylr2 In Equilibrium With Monomer At 266k (-7 Celsius Degrees)" 100.00 66 100.00 100.00 1.49e-37 PDB 2LYP "Noe-based 3d Structure Of The Monomer Of Cylr2 In Equilibrium With Predissociated Homodimer At 266k (-7 Celsius Degrees)" 100.00 66 100.00 100.00 1.49e-37 PDB 2LYQ "Noe-based 3d Structure Of The Monomeric Intermediate Of Cylr2 At 262k (-11 Celsius Degrees)" 100.00 66 100.00 100.00 1.49e-37 PDB 2LYR "Noe-based 3d Structure Of The Monomeric Partially-folded Intermediate Of Cylr2 At 259k (-14 Celsius Degrees)" 100.00 66 100.00 100.00 1.49e-37 PDB 2LYS "Noe-based 3d Structure Of The Monomeric Partially-folded Intermediate Of Cylr2 At 257k (-16 Celsius Degrees)" 100.00 66 100.00 100.00 1.49e-37 PDB 2XI8 "High Resolution Structure Of Native Cylr2" 100.00 66 100.00 100.00 1.49e-37 PDB 2XIU "High Resolution Structure Of Mtsl-Tagged Cylr2" 100.00 66 98.48 98.48 8.94e-37 PDB 2XJ3 "High Resolution Structure Of The T55c Mutant Of Cylr2." 100.00 66 98.48 98.48 8.94e-37 GB AAL59476 "putative transcription regulator [Enterococcus faecalis]" 100.00 66 100.00 100.00 1.49e-37 GB AAL60140 "CylR2 [Enterococcus faecalis]" 100.00 66 100.00 100.00 1.49e-37 GB AAM75247 "EF0042 [Enterococcus faecalis]" 100.00 66 98.48 100.00 5.19e-37 GB AAO80372 "transcriptional regulator, Cro/CI family [Enterococcus faecalis V583]" 100.00 66 98.48 100.00 5.19e-37 GB AIL03173 "helix-turn-helix family protein [Enterococcus faecalis ATCC 29212]" 100.00 66 100.00 100.00 1.49e-37 REF NP_814301 "Cro/CI family transcriptional regulator [Enterococcus faecalis V583]" 100.00 66 98.48 100.00 5.19e-37 REF WP_002358483 "Cro/Cl family transcriptional regulator [Enterococcus faecalis]" 100.00 66 100.00 100.00 1.49e-37 REF WP_002370931 "Cro/Cl family transcriptional regulator [Enterococcus faecalis]" 100.00 66 98.48 100.00 5.19e-37 REF WP_010773902 "transcriptional regulator [Enterococcus faecalis]" 100.00 66 98.48 100.00 1.05e-36 REF YP_009077231 "CylR2 [Enterococcus faecalis]" 100.00 66 100.00 100.00 1.49e-37 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $CylR2 'Enterococcus faecalis' 1351 Eubacteria . Enterococcus faecalis 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 $CylR2 'recombinant technology' 'E. coli' Escherichia coli BL21(DE3) plasmid pET32a 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 _Concentration_min_value _Concentration_max_value _Isotopic_labeling $CylR2 . mM 1.0 3.0 '[U-95% 13C; U-90% 15N]' stop_ save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer _Saveframe_category NMR_spectrometer _Manufacturer unknown _Model unknown _Field_strength 0 _Details 'spectrometer information not available' save_ ############################# # NMR applied experiments # ############################# save__1 _Saveframe_category NMR_applied_experiment _Sample_label $sample_1 save_ ####################### # Sample conditions # ####################### save_cond_set_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 7.0 0.2 n/a temperature 298 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 _Indirect_shift_ratio_citation_label _Correction_value_citation_label DSS C 13 'methyl protons' ppm 0.0 . indirect . . . 0.251449530 $entry_citation $entry_citation DSS H 1 'methyl protons' ppm 0.0 internal direct . . . 1.0 $entry_citation $entry_citation DSS N 15 'methyl protons' ppm 0.0 . indirect . . . 0.101329118 $entry_citation $entry_citation 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 $cond_set_1 _Chem_shift_reference_set_label $chemical_shift_reference _Mol_system_component_name 'CylR2 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 55.241 0.2 1 2 . 1 MET HA H 4.299 0.02 1 3 . 1 MET CB C 33.509 0.2 1 4 . 1 MET HB3 H 2.445 0.02 2 5 . 1 MET HB2 H 2.510 0.02 2 6 . 1 MET CG C 30.643 0.2 1 7 . 1 MET HG3 H 2.129 0.02 2 8 . 1 MET HG2 H 2.230 0.02 2 9 . 1 MET C C 181.468 0.2 1 10 . 2 ILE N N 124.025 0.2 1 11 . 2 ILE H H 8.857 0.02 1 12 . 2 ILE CA C 60.218 0.2 1 13 . 2 ILE HA H 5.012 0.02 1 14 . 2 ILE CB C 39.481 0.2 1 15 . 2 ILE HB H 2.071 0.02 1 16 . 2 ILE CG1 C 28.096 0.2 2 17 . 2 ILE HG13 H 1.255 0.02 1 18 . 2 ILE HG12 H 1.908 0.02 1 19 . 2 ILE CD1 C 13.078 0.2 1 20 . 2 ILE HD1 H 0.918 0.02 1 21 . 2 ILE CG2 C 17.481 0.2 2 22 . 2 ILE HG2 H 0.996 0.02 1 23 . 2 ILE C C 175.793 0.2 1 24 . 3 ILE N N 129.491 0.2 1 25 . 3 ILE H H 9.355 0.02 1 26 . 3 ILE CA C 60.736 0.2 1 27 . 3 ILE HA H 4.338 0.02 1 28 . 3 ILE CB C 38.975 0.2 1 29 . 3 ILE HB H 2.001 0.02 1 30 . 3 ILE CG1 C 27.840 0.2 2 31 . 3 ILE HG13 H 1.241 0.02 9 32 . 3 ILE HG12 H 1.512 0.02 9 33 . 3 ILE CD1 C 12.841 0.2 1 34 . 3 ILE HD1 H 0.820 0.02 1 35 . 3 ILE CG2 C 17.742 0.2 2 36 . 3 ILE HG2 H 0.935 0.02 4 37 . 3 ILE C C 174.467 0.2 1 38 . 4 ASN N N 124.380 0.2 1 39 . 4 ASN H H 8.828 0.02 1 40 . 4 ASN CA C 51.675 0.2 1 41 . 4 ASN HA H 5.481 0.02 1 42 . 4 ASN CB C 41.325 0.2 1 43 . 4 ASN HB3 H 2.765 0.02 2 44 . 4 ASN HB2 H 3.223 0.02 2 45 . 4 ASN CG C 176.624 0.2 1 46 . 4 ASN ND2 N 112.452 0.2 1 47 . 4 ASN HD21 H 8.111 0.02 2 48 . 4 ASN HD22 H 6.749 0.02 2 49 . 4 ASN C C 174.536 0.2 1 50 . 5 ASN N N 122.091 0.2 1 51 . 5 ASN H H 9.355 0.02 1 52 . 5 ASN CA C 51.708 0.2 1 53 . 5 ASN HA H 5.393 0.02 1 54 . 5 ASN CB C 39.789 0.2 1 55 . 5 ASN HB3 H 2.790 0.02 2 56 . 5 ASN HB2 H 3.213 0.02 2 57 . 5 ASN CG C 176.960 0.2 1 58 . 5 ASN ND2 N 112.071 0.2 1 59 . 5 ASN HD21 H 6.984 0.02 2 60 . 5 ASN HD22 H 6.720 0.02 2 61 . 5 ASN C C 175.679 0.2 1 62 . 6 LEU N N 121.038 0.2 1 63 . 6 LEU H H 8.418 0.02 1 64 . 6 LEU CA C 59.840 0.2 1 65 . 6 LEU HA H 3.799 0.02 1 66 . 6 LEU CB C 41.205 0.2 1 67 . 6 LEU HB3 H 1.142 0.02 2 68 . 6 LEU HB2 H 1.904 0.02 2 69 . 6 LEU CG C 26.166 0.2 1 70 . 6 LEU HG H 2.044 0.02 1 71 . 6 LEU CD1 C 27.475 0.2 1 72 . 6 LEU HD1 H 1.034 0.02 2 73 . 6 LEU CD2 C 24.337 0.2 1 74 . 6 LEU HD2 H 0.898 0.02 2 75 . 6 LEU C C 176.296 0.2 1 76 . 7 LYS N N 118.336 0.2 1 77 . 7 LYS H H 8.828 0.02 1 78 . 7 LYS CA C 60.680 0.2 1 79 . 7 LYS HA H 3.927 0.02 1 80 . 7 LYS CB C 32.703 0.2 1 81 . 7 LYS HB3 H 1.739 0.02 2 82 . 7 LYS HB2 H 1.809 0.02 2 83 . 7 LYS CG C 24.670 0.2 1 84 . 7 LYS HG3 H 1.268 0.02 2 85 . 7 LYS HG2 H 1.382 0.02 2 86 . 7 LYS CD C 30.128 0.2 1 87 . 7 LYS HD3 H 1.666 0.02 2 88 . 7 LYS HD2 H 1.734 0.02 2 89 . 7 LYS CE C 42.310 0.2 1 90 . 7 LYS HE3 H 2.998 0.02 2 91 . 7 LYS HE2 H 3.051 0.02 2 92 . 7 LYS C C 177.342 0.2 1 93 . 8 LEU N N 116.825 0.2 1 94 . 8 LEU H H 7.443 0.02 1 95 . 8 LEU CA C 57.965 0.2 1 96 . 8 LEU HA H 4.132 0.02 1 97 . 8 LEU CB C 42.175 0.2 1 98 . 8 LEU HB3 H 1.712 0.02 2 99 . 8 LEU HB2 H 1.763 0.02 2 100 . 8 LEU CG C 27.217 0.2 1 101 . 8 LEU HG H 1.832 0.02 1 102 . 8 LEU CD1 C 24.992 0.2 1 103 . 8 LEU HD1 H 1.022 0.02 2 104 . 8 LEU CD2 C 23.964 0.2 1 105 . 8 LEU HD2 H 0.942 0.02 2 106 . 8 LEU C C 180.234 0.2 1 107 . 9 ILE N N 119.168 0.2 1 108 . 9 ILE H H 8.137 0.02 1 109 . 9 ILE CA C 63.329 0.2 1 110 . 9 ILE HA H 3.807 0.02 1 111 . 9 ILE CB C 36.629 0.2 1 112 . 9 ILE HB H 1.936 0.02 1 113 . 9 ILE CG1 C 28.349 0.2 2 114 . 9 ILE HG13 H 1.476 0.02 9 115 . 9 ILE HG12 H 1.664 0.02 9 116 . 9 ILE CD1 C 11.350 0.2 1 117 . 9 ILE HD1 H 0.764 0.02 1 118 . 9 ILE CG2 C 18.245 0.2 2 119 . 9 ILE HG2 H 0.925 0.02 1 120 . 9 ILE C C 178.032 0.2 1 121 . 10 ARG N N 120.304 0.2 1 122 . 10 ARG H H 9.116 0.02 1 123 . 10 ARG CA C 61.051 0.2 1 124 . 10 ARG HA H 3.884 0.02 1 125 . 10 ARG CB C 28.884 0.2 1 126 . 10 ARG HB3 H 1.718 0.02 2 127 . 10 ARG HB2 H 2.109 0.02 2 128 . 10 ARG CG C 28.125 0.2 1 129 . 10 ARG HG3 H 1.346 0.02 2 130 . 10 ARG HG2 H 2.159 0.02 2 131 . 10 ARG CD C 41.609 0.2 1 132 . 10 ARG HD3 H 2.789 0.02 2 133 . 10 ARG HD2 H 3.025 0.02 2 134 . 10 ARG C C 179.088 0.2 1 135 . 11 GLU N N 116.636 0.2 1 136 . 11 GLU H H 8.556 0.02 1 137 . 11 GLU CA C 59.964 0.2 1 138 . 11 GLU HA H 4.140 0.02 1 139 . 11 GLU CB C 29.379 0.2 1 140 . 11 GLU HB3 H 2.033 0.02 2 141 . 11 GLU HB2 H 2.303 0.02 2 142 . 11 GLU CG C 37.688 0.2 1 143 . 11 GLU HG3 H 2.161 0.02 2 144 . 11 GLU HG2 H 2.762 0.02 2 145 . 11 GLU C C 181.542 0.2 1 146 . 12 LYS N N 122.547 0.2 1 147 . 12 LYS H H 8.155 0.02 1 148 . 12 LYS CA C 59.597 0.2 1 149 . 12 LYS HA H 4.204 0.02 1 150 . 12 LYS CB C 32.398 0.2 1 151 . 12 LYS HB3 H 2.108 0.02 2 152 . 12 LYS HB2 H 2.156 0.02 2 153 . 12 LYS CG C 25.409 0.2 1 154 . 12 LYS HG3 H 1.600 0.02 2 155 . 12 LYS HG2 H 1.739 0.02 2 156 . 12 LYS CD C 29.538 0.2 1 157 . 12 LYS HD3 H 1.775 0.02 2 158 . 12 LYS HD2 H 1.689 0.02 2 159 . 12 LYS CE C 42.268 0.2 1 160 . 12 LYS HE3 H 3.063 0.02 1 161 . 12 LYS HE2 H 3.063 0.02 1 162 . 12 LYS C C 178.789 0.2 1 163 . 13 LYS N N 116.805 0.2 1 164 . 13 LYS H H 7.762 0.02 1 165 . 13 LYS CA C 55.156 0.2 1 166 . 13 LYS HA H 4.272 0.02 1 167 . 13 LYS CB C 31.804 0.2 1 168 . 13 LYS HB3 H 1.945 0.02 2 169 . 13 LYS HB2 H 2.126 0.02 2 170 . 13 LYS CG C 25.027 0.2 1 171 . 13 LYS HG3 H 1.691 0.02 2 172 . 13 LYS HG2 H 1.728 0.02 2 173 . 13 LYS CD C 28.111 0.2 1 174 . 13 LYS HD3 H 1.645 0.02 2 175 . 13 LYS HD2 H 1.739 0.02 2 176 . 13 LYS CE C 42.157 0.2 1 177 . 13 LYS HE3 H 2.978 0.02 2 178 . 13 LYS HE2 H 3.197 0.02 2 179 . 13 LYS C C 175.291 0.2 1 180 . 14 LYS N N 115.488 0.2 1 181 . 14 LYS H H 8.008 0.02 1 182 . 14 LYS CA C 57.333 0.2 1 183 . 14 LYS HA H 3.953 0.02 1 184 . 14 LYS CB C 30.041 0.2 1 185 . 14 LYS HB3 H 1.995 0.02 2 186 . 14 LYS HB2 H 2.183 0.02 2 187 . 14 LYS CG C 24.941 0.2 1 188 . 14 LYS HG3 H 1.433 0.02 2 189 . 14 LYS HG2 H 1.462 0.02 2 190 . 14 LYS CD C 28.973 0.2 1 191 . 14 LYS HD3 H 1.762 0.02 2 192 . 14 LYS HD2 H 1.841 0.02 2 193 . 14 LYS CE C 42.555 0.2 1 194 . 14 LYS HE3 H 2.975 0.02 2 195 . 14 LYS HE2 H 3.197 0.02 2 196 . 14 LYS C C 175.084 0.2 1 197 . 15 ILE N N 118.790 0.2 1 198 . 15 ILE H H 7.525 0.02 1 199 . 15 ILE CA C 59.421 0.2 1 200 . 15 ILE HA H 4.592 0.02 1 201 . 15 ILE CB C 41.051 0.2 1 202 . 15 ILE HB H 1.610 0.02 1 203 . 15 ILE CG1 C 27.858 0.2 2 204 . 15 ILE HG13 H 1.139 0.02 1 205 . 15 ILE HG12 H 1.605 0.02 1 206 . 15 ILE CD1 C 13.409 0.2 1 207 . 15 ILE HD1 H 0.827 0.02 1 208 . 15 ILE CG2 C 17.480 0.2 2 209 . 15 ILE HG2 H 1.001 0.02 1 210 . 15 ILE C C 175.684 0.2 1 211 . 16 SER N N 124.886 0.2 1 212 . 16 SER H H 9.209 0.02 1 213 . 16 SER CA C 57.640 0.2 1 214 . 16 SER HA H 4.564 0.02 1 215 . 16 SER CB C 65.673 0.2 1 216 . 16 SER HB3 H 4.060 0.02 2 217 . 16 SER HB2 H 4.410 0.02 2 218 . 16 SER C C 175.504 0.2 1 219 . 17 GLN N N 120.667 0.2 1 220 . 17 GLN H H 9.355 0.02 1 221 . 17 GLN CA C 61.063 0.2 1 222 . 17 GLN HA H 3.754 0.02 1 223 . 17 GLN CB C 29.451 0.2 1 224 . 17 GLN HB3 H 1.998 0.02 2 225 . 17 GLN HB2 H 2.315 0.02 2 226 . 17 GLN CG C 34.356 0.2 1 227 . 17 GLN HG3 H 2.155 0.02 2 228 . 17 GLN HG2 H 2.798 0.02 2 229 . 17 GLN CD C 178.829 0.2 1 230 . 17 GLN NE2 N 112.430 0.2 1 231 . 17 GLN HE21 H 7.756 0.02 2 232 . 17 GLN HE22 H 7.328 0.02 2 233 . 17 GLN C C 178.749 0.2 1 234 . 18 SER N N 112.918 0.2 1 235 . 18 SER H H 8.686 0.02 1 236 . 18 SER CA C 62.389 0.2 1 237 . 18 SER HA H 4.267 0.02 1 238 . 18 SER CB C 64.128 0.2 1 239 . 18 SER HB3 H 3.934 0.02 2 240 . 18 SER HB2 H 4.020 0.02 2 241 . 18 SER C C 177.013 0.2 1 242 . 19 GLU N N 124.491 0.2 1 243 . 19 GLU H H 8.142 0.02 1 244 . 19 GLU CA C 59.064 0.2 1 245 . 19 GLU HA H 4.095 0.02 1 246 . 19 GLU CB C 30.041 0.2 1 247 . 19 GLU HB3 H 1.992 0.02 2 248 . 19 GLU HB2 H 2.319 0.02 2 249 . 19 GLU CG C 37.041 0.2 1 250 . 19 GLU HG3 H 2.195 0.02 2 251 . 19 GLU HG2 H 2.343 0.02 2 252 . 19 GLU C C 179.204 0.2 1 253 . 20 LEU N N 119.872 0.2 1 254 . 20 LEU H H 8.165 0.02 1 255 . 20 LEU CA C 57.482 0.2 1 256 . 20 LEU HA H 4.130 0.02 1 257 . 20 LEU CB C 41.405 0.2 1 258 . 20 LEU HB3 H 1.404 0.02 2 259 . 20 LEU HB2 H 1.908 0.02 2 260 . 20 LEU CG C 22.508 0.2 1 261 . 20 LEU HG H 1.404 0.02 1 262 . 20 LEU CD1 C 26.892 0.2 1 263 . 20 LEU HD1 H 1.684 0.02 2 264 . 20 LEU CD2 C 26.892 0.2 1 265 . 20 LEU HD2 H 0.981 0.02 2 266 . 20 LEU C C 177.689 0.2 1 267 . 21 ALA N N 120.124 0.2 1 268 . 21 ALA H H 8.454 0.02 1 269 . 21 ALA CA C 55.837 0.2 1 270 . 21 ALA HA H 3.696 0.02 1 271 . 21 ALA CB C 17.254 0.2 1 272 . 21 ALA HB H 1.471 0.02 1 273 . 21 ALA C C 178.899 0.2 1 274 . 22 ALA N N 118.077 0.2 1 275 . 22 ALA H H 7.723 0.02 1 276 . 22 ALA CA C 54.516 0.2 1 277 . 22 ALA HA H 4.218 0.02 1 278 . 22 ALA CB C 17.891 0.2 1 279 . 22 ALA HB H 1.545 0.02 1 280 . 22 ALA C C 181.495 0.2 1 281 . 23 LEU N N 118.948 0.2 1 282 . 23 LEU H H 7.568 0.02 1 283 . 23 LEU CA C 57.500 0.2 1 284 . 23 LEU HA H 3.953 0.02 1 285 . 23 LEU CB C 41.729 0.2 1 286 . 23 LEU HB3 H 0.590 0.02 2 287 . 23 LEU HB2 H 1.669 0.02 2 288 . 23 LEU CG C 26.392 0.2 1 289 . 23 LEU HG H 1.733 0.02 1 290 . 23 LEU CD1 C 24.874 0.2 2 291 . 23 LEU HD1 H 0.843 0.02 1 292 . 23 LEU CD2 C 22.551 0.2 2 293 . 23 LEU HD2 H 0.843 0.02 1 294 . 23 LEU C C 178.218 0.2 1 295 . 24 LEU N N 114.829 0.2 1 296 . 24 LEU H H 7.455 0.02 1 297 . 24 LEU CA C 55.023 0.2 1 298 . 24 LEU HA H 4.304 0.02 1 299 . 24 LEU CB C 43.883 0.2 1 300 . 24 LEU HB3 H 1.509 0.02 2 301 . 24 LEU HB2 H 1.818 0.02 2 302 . 24 LEU CG C 29.040 0.2 1 303 . 24 LEU HG H 1.871 0.02 1 304 . 24 LEU CD1 C 24.159 0.2 1 305 . 24 LEU HD1 H 0.852 0.02 2 306 . 24 LEU CD2 C 24.159 0.2 1 307 . 24 LEU HD2 H 0.808 0.02 2 308 . 24 LEU C C 175.299 0.2 1 309 . 25 GLU N N 115.526 0.2 1 310 . 25 GLU H H 7.989 0.02 1 311 . 25 GLU CA C 57.469 0.2 1 312 . 25 GLU HA H 3.963 0.02 1 313 . 25 GLU CB C 27.393 0.2 1 314 . 25 GLU HB3 H 2.210 0.02 2 315 . 25 GLU HB2 H 2.364 0.02 2 316 . 25 GLU CG C 37.035 0.2 1 317 . 25 GLU HG3 H 2.204 0.02 1 318 . 25 GLU HG2 H 2.204 0.02 1 319 . 25 GLU C C 176.039 0.2 1 320 . 26 VAL N N 110.193 0.2 1 321 . 26 VAL H H 7.920 0.02 1 322 . 26 VAL CA C 58.536 0.2 1 323 . 26 VAL HA H 4.876 0.02 1 324 . 26 VAL CB C 35.467 0.2 1 325 . 26 VAL HB H 2.369 0.02 1 326 . 26 VAL CG2 C 18.657 0.2 2 327 . 26 VAL HG2 H 0.818 0.02 2 328 . 26 VAL CG1 C 21.763 0.2 2 329 . 26 VAL HG1 H 0.940 0.02 2 330 . 26 VAL C C 174.652 0.2 1 331 . 27 SER N N 114.577 0.2 1 332 . 27 SER H H 8.403 0.02 1 333 . 27 SER CA C 50.056 0.2 1 334 . 27 SER HA H 4.515 0.02 1 335 . 27 SER CB C 61.938 0.2 1 336 . 27 SER HB3 H 3.909 0.02 2 337 . 27 SER HB2 H 4.012 0.02 2 338 . 27 SER C C 176.026 0.2 1 339 . 28 ARG N N 115.323 0.2 1 340 . 28 ARG H H 8.133 0.02 1 341 . 28 ARG CA C 60.400 0.2 1 342 . 28 ARG HA H 3.757 0.02 1 343 . 28 ARG CB C 29.566 0.2 1 344 . 28 ARG HB3 H 1.855 0.02 2 345 . 28 ARG HB2 H 1.948 0.02 2 346 . 28 ARG CG C 27.541 0.2 1 347 . 28 ARG HG3 H 1.569 0.02 2 348 . 28 ARG HG2 H 1.655 0.02 2 349 . 28 ARG CD C 43.582 0.2 1 350 . 28 ARG HD3 H 3.205 0.02 2 351 . 28 ARG HD2 H 3.293 0.02 2 352 . 28 ARG C C 178.319 0.2 1 353 . 29 GLN N N 117.714 0.2 1 354 . 29 GLN H H 8.673 0.02 1 355 . 29 GLN CA C 59.339 0.2 1 356 . 29 GLN HA H 4.144 0.02 1 357 . 29 GLN CB C 28.023 0.2 1 358 . 29 GLN HB3 H 2.098 0.02 2 359 . 29 GLN HB2 H 2.172 0.02 2 360 . 29 GLN CG C 34.239 0.2 1 361 . 29 GLN HG3 H 2.546 0.02 2 362 . 29 GLN HG2 H 2.605 0.02 2 363 . 29 GLN CD C 180.622 0.2 1 364 . 29 GLN NE2 N 111.925 0.2 1 365 . 29 GLN HE21 H 7.598 0.02 2 366 . 29 GLN HE22 H 6.969 0.02 2 367 . 29 GLN C C 178.966 0.2 1 368 . 30 THR N N 119.948 0.2 1 369 . 30 THR H H 8.000 0.02 1 370 . 30 THR CA C 66.847 0.2 1 371 . 30 THR HA H 4.409 0.02 1 372 . 30 THR CB C 68.142 0.2 1 373 . 30 THR HB H 3.933 0.02 1 374 . 30 THR CG2 C 21.273 0.2 1 375 . 30 THR HG2 H 0.935 0.02 1 376 . 30 THR C C 175.869 0.2 1 377 . 31 ILE N N 119.206 0.2 1 378 . 31 ILE H H 7.130 0.02 1 379 . 31 ILE CA C 62.074 0.2 1 380 . 31 ILE HA H 3.786 0.02 1 381 . 31 ILE CB C 35.477 0.2 1 382 . 31 ILE HB H 2.188 0.02 1 383 . 31 ILE CG1 C 27.126 0.2 2 384 . 31 ILE HG13 H 1.366 0.02 1 385 . 31 ILE HG12 H 1.646 0.02 9 386 . 31 ILE CD1 C 9.364 0.2 1 387 . 31 ILE HD1 H 0.652 0.02 1 388 . 31 ILE CG2 C 18.319 0.2 2 389 . 31 ILE HG2 H 0.969 0.02 1 390 . 31 ILE C C 177.469 0.2 1 391 . 32 ASN N N 118.587 0.2 1 392 . 32 ASN H H 8.556 0.02 1 393 . 32 ASN CA C 57.530 0.2 1 394 . 32 ASN HA H 4.361 0.02 1 395 . 32 ASN CB C 39.130 0.2 1 396 . 32 ASN HB3 H 2.761 0.02 2 397 . 32 ASN HB2 H 2.846 0.02 2 398 . 32 ASN C C 176.969 0.2 1 399 . 33 GLY N N 105.132 0.2 1 400 . 33 GLY H H 8.495 0.02 1 401 . 33 GLY CA C 47.310 0.2 1 402 . 33 GLY HA3 H 3.768 0.02 2 403 . 33 GLY HA2 H 3.959 0.02 2 404 . 33 GLY C C 176.613 0.2 1 405 . 34 ILE N N 122.727 0.2 1 406 . 34 ILE H H 8.180 0.02 1 407 . 34 ILE CA C 65.112 0.2 1 408 . 34 ILE HA H 4.297 0.02 1 409 . 34 ILE CB C 38.908 0.2 1 410 . 34 ILE HB H 2.057 0.02 1 411 . 34 ILE CG1 C 29.321 0.2 2 412 . 34 ILE HG13 H 0.952 0.02 1 413 . 34 ILE HG12 H 2.217 0.02 1 414 . 34 ILE CD1 C 14.800 0.2 1 415 . 34 ILE HD1 H 0.835 0.02 1 416 . 34 ILE CG2 C 18.220 0.2 2 417 . 34 ILE HG2 H 1.156 0.02 1 418 . 34 ILE C C 180.597 0.2 1 419 . 35 GLU N N 121.104 0.2 1 420 . 35 GLU H H 8.552 0.02 1 421 . 35 GLU CA C 60.376 0.2 1 422 . 35 GLU HA H 4.186 0.02 1 423 . 35 GLU CB C 29.797 0.2 1 424 . 35 GLU HB3 H 2.018 0.02 2 425 . 35 GLU HB2 H 2.279 0.02 2 426 . 35 GLU CG C 38.106 0.2 1 427 . 35 GLU HG3 H 2.281 0.02 2 428 . 35 GLU HG2 H 2.739 0.02 2 429 . 35 GLU C C 178.359 0.2 1 430 . 36 LYS N N 116.278 0.2 1 431 . 36 LYS H H 7.992 0.02 1 432 . 36 LYS CA C 55.667 0.2 1 433 . 36 LYS HA H 4.456 0.02 1 434 . 36 LYS CB C 32.230 0.2 1 435 . 36 LYS HB3 H 1.771 0.02 2 436 . 36 LYS HB2 H 2.188 0.02 2 437 . 36 LYS CG C 25.345 0.2 1 438 . 36 LYS HG3 H 1.589 0.02 2 439 . 36 LYS HG2 H 1.655 0.02 2 440 . 36 LYS CD C 28.710 0.2 1 441 . 36 LYS HD3 H 1.706 0.02 2 442 . 36 LYS HD2 H 1.732 0.02 2 443 . 36 LYS CE C 42.431 0.2 1 444 . 36 LYS HE3 H 3.115 0.02 1 445 . 36 LYS HE2 H 3.115 0.02 1 446 . 36 LYS C C 175.582 0.2 1 447 . 37 ASN N N 115.096 0.2 1 448 . 37 ASN H H 8.119 0.02 1 449 . 37 ASN CA C 54.790 0.2 1 450 . 37 ASN HA H 4.677 0.02 1 451 . 37 ASN CB C 37.324 0.2 1 452 . 37 ASN HB3 H 3.014 0.02 2 453 . 37 ASN HB2 H 3.275 0.02 2 454 . 37 ASN CG C 178.428 0.2 1 455 . 37 ASN ND2 N 112.725 0.2 1 456 . 37 ASN HD21 H 7.621 0.02 2 457 . 37 ASN HD22 H 7.138 0.02 2 458 . 37 ASN C C 174.965 0.2 1 459 . 38 LYS N N 115.684 0.2 1 460 . 38 LYS H H 8.594 0.02 1 461 . 38 LYS CA C 56.748 0.2 1 462 . 38 LYS HA H 4.409 0.02 1 463 . 38 LYS CB C 33.443 0.2 1 464 . 38 LYS HB3 H 1.577 0.02 2 465 . 38 LYS HB2 H 1.884 0.02 2 466 . 38 LYS CG C 24.898 0.2 1 467 . 38 LYS HG3 H 1.379 0.02 2 468 . 38 LYS HG2 H 1.511 0.02 2 469 . 38 LYS CD C 28.782 0.2 1 470 . 38 LYS HD3 H 1.716 0.02 1 471 . 38 LYS HD2 H 1.716 0.02 1 472 . 38 LYS CE C 42.247 0.2 1 473 . 38 LYS HE3 H 3.062 0.02 1 474 . 38 LYS HE2 H 3.062 0.02 1 475 . 38 LYS C C 175.871 0.2 1 476 . 39 TYR N N 116.888 0.2 1 477 . 39 TYR H H 7.027 0.02 1 478 . 39 TYR CA C 55.614 0.2 1 479 . 39 TYR HA H 4.673 0.02 1 480 . 39 TYR CB C 40.067 0.2 1 481 . 39 TYR HB3 H 2.853 0.02 2 482 . 39 TYR HB2 H 2.909 0.02 2 483 . 39 TYR CD1 C 133.155 0.2 1 484 . 39 TYR HD1 H 6.920 0.02 1 485 . 39 TYR CE1 C 117.889 0.2 1 486 . 39 TYR HE1 H 6.810 0.02 1 487 . 39 TYR CE2 C 117.889 0.2 1 488 . 39 TYR HE2 H 6.810 0.02 1 489 . 39 TYR CD2 C 133.155 0.2 1 490 . 39 TYR HD2 H 6.920 0.02 1 491 . 39 TYR C C 173.982 0.2 1 492 . 40 ASN N N 123.469 0.2 1 493 . 40 ASN H H 8.623 0.02 1 494 . 40 ASN CA C 50.256 0.2 1 495 . 40 ASN HA H 5.182 0.02 1 496 . 40 ASN CB C 38.876 0.2 1 497 . 40 ASN HB3 H 2.571 0.02 2 498 . 40 ASN HB2 H 2.655 0.02 2 499 . 40 ASN CG C 175.704 0.2 1 500 . 40 ASN ND2 N 112.168 0.2 1 501 . 40 ASN HD21 H 7.584 0.02 2 502 . 40 ASN HD22 H 6.910 0.02 2 503 . 40 ASN C C 174.012 0.2 1 504 . 41 PRO CA C 62.651 0.2 1 505 . 41 PRO HA H 3.833 0.02 1 506 . 41 PRO CB C 31.842 0.2 1 507 . 41 PRO HB3 H 1.829 0.02 2 508 . 41 PRO HB2 H 2.102 0.02 2 509 . 41 PRO CG C 26.661 0.2 1 510 . 41 PRO HG3 H 1.461 0.02 2 511 . 41 PRO HG2 H 1.805 0.02 2 512 . 41 PRO CD C 50.208 0.2 1 513 . 41 PRO HD3 H 2.603 0.02 2 514 . 41 PRO HD2 H 3.245 0.02 2 515 . 41 PRO C C 176.026 0.2 1 516 . 42 SER N N 125.406 0.2 1 517 . 42 SER H H 7.803 0.02 1 518 . 42 SER CA C 57.833 0.2 1 519 . 42 SER HA H 5.531 0.02 1 520 . 42 SER CB C 64.479 0.2 1 521 . 42 SER HB3 H 4.158 0.02 2 522 . 42 SER HB2 H 4.338 0.02 2 523 . 42 SER C C 173.884 0.2 1 524 . 43 LEU N N 121.283 0.2 1 525 . 43 LEU H H 9.135 0.02 1 526 . 43 LEU CA C 58.734 0.2 1 527 . 43 LEU HA H 3.922 0.02 1 528 . 43 LEU CB C 41.092 0.2 1 529 . 43 LEU HB3 H 1.193 0.02 2 530 . 43 LEU HB2 H 1.765 0.02 2 531 . 43 LEU CG C 27.069 0.2 1 532 . 43 LEU HG H 1.355 0.02 1 533 . 43 LEU CD1 C 25.307 0.2 2 534 . 43 LEU HD1 H 0.309 0.02 2 535 . 43 LEU CD2 C 22.978 0.2 2 536 . 43 LEU HD2 H 0.699 0.02 2 537 . 43 LEU C C 177.724 0.2 1 538 . 44 GLN N N 115.940 0.2 1 539 . 44 GLN H H 8.752 0.02 1 540 . 44 GLN CA C 60.626 0.2 1 541 . 44 GLN HA H 3.712 0.02 1 542 . 44 GLN CB C 28.795 0.2 1 543 . 44 GLN HB3 H 2.026 0.02 1 544 . 44 GLN HB2 H 2.026 0.02 1 545 . 44 GLN CG C 34.796 0.2 1 546 . 44 GLN HG3 H 2.178 0.02 1 547 . 44 GLN HG2 H 2.178 0.02 1 548 . 44 GLN CD C 179.906 0.2 1 549 . 44 GLN NE2 N 112.386 0.2 1 550 . 44 GLN HE21 H 7.506 0.02 2 551 . 44 GLN HE22 H 6.964 0.02 2 552 . 44 GLN C C 176.813 0.2 1 553 . 45 LEU N N 119.538 0.2 1 554 . 45 LEU H H 7.895 0.02 1 555 . 45 LEU CA C 57.741 0.2 1 556 . 45 LEU HA H 3.994 0.02 1 557 . 45 LEU CB C 40.936 0.2 1 558 . 45 LEU HB3 H 1.675 0.02 2 559 . 45 LEU HB2 H 1.822 0.02 2 560 . 45 LEU CG C 26.455 0.2 1 561 . 45 LEU HG H 1.604 0.02 1 562 . 45 LEU CD1 C 25.574 0.2 1 563 . 45 LEU HD1 H 1.024 0.02 2 564 . 45 LEU CD2 C 20.698 0.2 1 565 . 45 LEU HD2 H 1.057 0.02 2 566 . 45 LEU C C 178.515 0.2 1 567 . 46 ALA N N 120.828 0.2 1 568 . 46 ALA H H 8.442 0.02 1 569 . 46 ALA CA C 55.851 0.2 1 570 . 46 ALA HA H 4.022 0.02 1 571 . 46 ALA CB C 19.862 0.2 1 572 . 46 ALA HB H 1.364 0.02 1 573 . 46 ALA C C 178.834 0.2 1 574 . 47 LEU N N 116.494 0.2 1 575 . 47 LEU H H 8.553 0.02 1 576 . 47 LEU CA C 57.734 0.2 1 577 . 47 LEU HA H 4.169 0.02 1 578 . 47 LEU CB C 42.479 0.2 1 579 . 47 LEU HB3 H 1.588 0.02 2 580 . 47 LEU HB2 H 1.980 0.02 2 581 . 47 LEU CG C 23.511 0.2 1 582 . 47 LEU HG H 1.095 0.02 1 583 . 47 LEU CD1 C 26.949 0.2 1 584 . 47 LEU HD1 H 1.826 0.02 2 585 . 47 LEU CD2 C 26.949 0.2 1 586 . 47 LEU HD2 H 0.855 0.02 2 587 . 47 LEU C C 180.515 0.2 1 588 . 48 LYS N N 121.033 0.2 1 589 . 48 LYS H H 7.882 0.02 1 590 . 48 LYS CA C 60.385 0.2 1 591 . 48 LYS HA H 3.569 0.02 1 592 . 48 LYS CB C 32.985 0.2 1 593 . 48 LYS HB3 H 1.451 0.02 2 594 . 48 LYS HB2 H 1.655 0.02 2 595 . 48 LYS CG C 24.160 0.2 1 596 . 48 LYS HG3 H 0.636 0.02 1 597 . 48 LYS HG2 H 0.636 0.02 1 598 . 48 LYS CD C 30.129 0.2 1 599 . 48 LYS HD3 H 1.315 0.02 1 600 . 48 LYS HD2 H 1.315 0.02 1 601 . 48 LYS CE C 41.861 0.2 1 602 . 48 LYS HE3 H 2.646 0.02 1 603 . 48 LYS HE2 H 2.646 0.02 1 604 . 48 LYS C C 178.189 0.2 1 605 . 49 ILE N N 120.346 0.2 1 606 . 49 ILE H H 8.627 0.02 1 607 . 49 ILE CA C 67.138 0.2 1 608 . 49 ILE HA H 3.611 0.02 1 609 . 49 ILE CB C 38.619 0.2 1 610 . 49 ILE HB H 2.379 0.02 1 611 . 49 ILE CG1 C 32.230 0.2 2 612 . 49 ILE HG13 H 0.913 0.02 1 613 . 49 ILE HG12 H 2.238 0.02 1 614 . 49 ILE CD1 C 19.259 0.2 1 615 . 49 ILE HD1 H 0.962 0.02 1 616 . 49 ILE CG2 C 13.767 0.2 1 617 . 49 ILE HG2 H 1.055 0.02 1 618 . 49 ILE C C 176.738 0.2 1 619 . 50 ALA N N 120.810 0.2 1 620 . 50 ALA H H 8.038 0.02 1 621 . 50 ALA CA C 55.971 0.2 1 622 . 50 ALA HA H 4.025 0.02 1 623 . 50 ALA CB C 18.444 0.2 1 624 . 50 ALA HB H 1.771 0.02 1 625 . 50 ALA C C 178.985 0.2 1 626 . 51 TYR N N 117.562 0.2 1 627 . 51 TYR H H 8.132 0.02 1 628 . 51 TYR CA C 61.658 0.2 1 629 . 51 TYR HA H 4.313 0.02 1 630 . 51 TYR CB C 38.658 0.2 1 631 . 51 TYR HB3 H 3.232 0.02 2 632 . 51 TYR HB2 H 3.351 0.02 2 633 . 51 TYR CD1 C 133.818 0.2 1 634 . 51 TYR HD1 H 6.589 0.02 1 635 . 51 TYR CE1 C 117.889 0.2 1 636 . 51 TYR HE1 H 6.732 0.02 1 637 . 51 TYR CE2 C 117.889 0.2 1 638 . 51 TYR HE2 H 6.732 0.02 1 639 . 51 TYR CD2 C 133.818 0.2 1 640 . 51 TYR HD2 H 6.589 0.02 1 641 . 51 TYR C C 180.444 0.2 1 642 . 52 TYR N N 118.527 0.2 1 643 . 52 TYR H H 8.883 0.02 1 644 . 52 TYR CA C 62.940 0.2 1 645 . 52 TYR HA H 4.663 0.02 1 646 . 52 TYR CB C 37.906 0.2 1 647 . 52 TYR HB3 H 3.011 0.02 2 648 . 52 TYR HB2 H 3.271 0.02 2 649 . 52 TYR CD1 C 133.818 0.2 1 650 . 52 TYR HD1 H 7.421 0.02 1 651 . 52 TYR CE1 C 117.889 0.2 1 652 . 52 TYR HE1 H 6.979 0.02 1 653 . 52 TYR CE2 C 117.889 0.2 1 654 . 52 TYR HE2 H 6.979 0.02 1 655 . 52 TYR CD2 C 133.818 0.2 1 656 . 52 TYR HD2 H 7.421 0.02 1 657 . 52 TYR C C 177.873 0.2 1 658 . 53 LEU N N 115.783 0.2 1 659 . 53 LEU H H 8.193 0.02 1 660 . 53 LEU CA C 54.344 0.2 1 661 . 53 LEU HA H 4.499 0.02 1 662 . 53 LEU CB C 40.553 0.2 1 663 . 53 LEU HB3 H 1.537 0.02 2 664 . 53 LEU HB2 H 1.810 0.02 2 665 . 53 LEU CG C 23.497 0.2 1 666 . 53 LEU HG H 0.831 0.02 1 667 . 53 LEU CD1 C 26.342 0.2 1 668 . 53 LEU HD1 H 1.907 0.02 2 669 . 53 LEU CD2 C 26.342 0.2 1 670 . 53 LEU HD2 H 0.759 0.02 2 671 . 53 LEU C C 176.601 0.2 1 672 . 54 ASN N N 122.175 0.2 1 673 . 54 ASN H H 8.052 0.02 1 674 . 54 ASN CA C 53.984 0.2 1 675 . 54 ASN HA H 4.411 0.02 1 676 . 54 ASN CB C 38.091 0.2 1 677 . 54 ASN HB3 H 2.556 0.02 2 678 . 54 ASN HB2 H 3.065 0.02 2 679 . 54 ASN CG C 178.146 0.2 1 680 . 54 ASN ND2 N 111.618 0.2 1 681 . 54 ASN HD21 H 7.541 0.02 2 682 . 54 ASN HD22 H 6.827 0.02 2 683 . 54 ASN C C 174.077 0.2 1 684 . 55 THR N N 115.431 0.2 1 685 . 55 THR H H 8.122 0.02 1 686 . 55 THR CA C 60.451 0.2 1 687 . 55 THR HA H 4.909 0.02 1 688 . 55 THR CB C 74.928 0.2 1 689 . 55 THR HB H 3.577 0.02 1 690 . 55 THR CG2 C 20.677 0.2 1 691 . 55 THR HG2 H 1.415 0.02 1 692 . 55 THR C C 173.934 0.2 1 693 . 56 PRO CA C 62.879 0.2 1 694 . 56 PRO HA H 4.596 0.02 1 695 . 56 PRO CB C 32.318 0.2 1 696 . 56 PRO HB3 H 1.907 0.02 2 697 . 56 PRO HB2 H 2.543 0.02 2 698 . 56 PRO CG C 28.165 0.2 1 699 . 56 PRO HG3 H 1.995 0.02 2 700 . 56 PRO HG2 H 2.201 0.02 2 701 . 56 PRO CD C 51.538 0.2 1 702 . 56 PRO HD3 H 3.846 0.02 2 703 . 56 PRO HD2 H 3.985 0.02 2 704 . 56 PRO C C 178.492 0.2 1 705 . 57 LEU N N 127.834 0.2 1 706 . 57 LEU H H 9.777 0.02 1 707 . 57 LEU CA C 60.457 0.2 1 708 . 57 LEU HA H 4.032 0.02 1 709 . 57 LEU CB C 42.070 0.2 1 710 . 57 LEU HB3 H 1.872 0.02 1 711 . 57 LEU HB2 H 1.872 0.02 1 712 . 57 LEU CG C 27.560 0.2 1 713 . 57 LEU HG H 1.182 0.02 1 714 . 57 LEU CD1 C 26.517 0.2 1 715 . 57 LEU HD1 H 1.176 0.02 2 716 . 57 LEU CD2 C 26.517 0.2 1 717 . 57 LEU HD2 H 2.052 0.02 2 718 . 57 LEU C C 179.938 0.2 1 719 . 58 GLU N N 117.482 0.2 1 720 . 58 GLU H H 10.072 0.02 1 721 . 58 GLU CA C 59.055 0.2 1 722 . 58 GLU HA H 4.853 0.02 1 723 . 58 GLU CB C 29.599 0.2 1 724 . 58 GLU HB3 H 2.132 0.02 2 725 . 58 GLU HB2 H 2.422 0.02 2 726 . 58 GLU CG C 38.929 0.2 1 727 . 58 GLU HG3 H 2.424 0.02 2 728 . 58 GLU HG2 H 2.673 0.02 2 729 . 58 GLU C C 177.148 0.2 1 730 . 59 ASP N N 118.018 0.2 1 731 . 59 ASP H H 7.922 0.02 1 732 . 59 ASP CA C 56.032 0.2 1 733 . 59 ASP HA H 4.622 0.02 1 734 . 59 ASP CB C 40.225 0.2 1 735 . 59 ASP HB3 H 2.539 0.02 2 736 . 59 ASP HB2 H 2.862 0.02 2 737 . 59 ASP C C 176.767 0.2 1 738 . 60 ILE N N 119.581 0.2 1 739 . 60 ILE H H 8.111 0.02 1 740 . 60 ILE CA C 64.206 0.2 1 741 . 60 ILE HA H 3.575 0.02 1 742 . 60 ILE CB C 39.843 0.2 1 743 . 60 ILE HB H 1.808 0.02 1 744 . 60 ILE CG1 C 27.695 0.2 2 745 . 60 ILE HG13 H 0.543 0.02 1 746 . 60 ILE HG12 H 1.893 0.02 1 747 . 60 ILE CD1 C 18.636 0.2 1 748 . 60 ILE HD1 H 0.059 0.02 1 749 . 60 ILE CG2 C 14.955 0.2 1 750 . 60 ILE HG2 H 0.837 0.02 1 751 . 60 ILE C C 174.271 0.2 1 752 . 61 PHE N N 116.526 0.2 1 753 . 61 PHE H H 8.477 0.02 1 754 . 61 PHE CA C 55.746 0.2 1 755 . 61 PHE HA H 5.453 0.02 1 756 . 61 PHE CB C 42.522 0.2 1 757 . 61 PHE HB3 H 2.897 0.02 1 758 . 61 PHE HB2 H 2.897 0.02 1 759 . 61 PHE CD1 C 133.155 0.2 1 760 . 61 PHE HD1 H 7.259 0.02 1 761 . 61 PHE CE1 C 130.500 0.2 1 762 . 61 PHE HE1 H 7.207 0.02 1 763 . 61 PHE CZ C 127.845 0.2 1 764 . 61 PHE HZ H 7.020 0.02 1 765 . 61 PHE CE2 C 130.500 0.2 1 766 . 61 PHE HE2 H 7.207 0.02 1 767 . 61 PHE CD2 C 133.155 0.2 1 768 . 61 PHE HD2 H 7.259 0.02 1 769 . 61 PHE C C 172.748 0.2 1 770 . 62 GLN N N 117.327 0.2 1 771 . 62 GLN H H 8.574 0.02 1 772 . 62 GLN CA C 54.371 0.2 1 773 . 62 GLN HA H 5.009 0.02 1 774 . 62 GLN CB C 32.171 0.2 1 775 . 62 GLN HB3 H 2.101 0.02 2 776 . 62 GLN HB2 H 2.148 0.02 2 777 . 62 GLN CG C 34.044 0.2 1 778 . 62 GLN HG3 H 2.361 0.02 2 779 . 62 GLN HG2 H 2.505 0.02 2 780 . 62 GLN CD C 180.733 0.2 1 781 . 62 GLN NE2 N 110.470 0.2 1 782 . 62 GLN HE21 H 7.584 0.02 2 783 . 62 GLN HE22 H 6.672 0.02 2 784 . 62 GLN C C 174.971 0.2 1 785 . 63 TRP N N 125.747 0.2 1 786 . 63 TRP H H 9.267 0.02 1 787 . 63 TRP CA C 56.920 0.2 1 788 . 63 TRP HA H 5.248 0.02 1 789 . 63 TRP CB C 31.245 0.2 1 790 . 63 TRP HB3 H 3.029 0.02 2 791 . 63 TRP HB2 H 3.101 0.02 2 792 . 63 TRP CD1 C 126.517 0.2 2 793 . 63 TRP HD1 H 6.885 0.02 1 794 . 63 TRP NE1 N 128.863 0.2 1 795 . 63 TRP HE1 H 11.445 0.02 2 796 . 63 TRP CZ2 C 114.570 0.2 2 797 . 63 TRP HZ2 H 7.562 0.02 2 798 . 63 TRP CH2 C 124.526 0.2 1 799 . 63 TRP HH2 H 7.242 0.02 1 800 . 63 TRP CZ3 C 120.544 0.2 2 801 . 63 TRP HZ3 H 6.649 0.02 2 802 . 63 TRP CE3 C 118.552 0.2 2 803 . 63 TRP HE3 H 6.920 0.02 2 804 . 63 TRP C C 174.628 0.2 1 805 . 64 GLN N N 126.738 0.2 1 806 . 64 GLN H H 7.847 0.02 1 807 . 64 GLN CA C 51.779 0.2 1 808 . 64 GLN HA H 4.215 0.02 1 809 . 64 GLN CB C 31.014 0.2 1 810 . 64 GLN HB3 H 1.591 0.02 2 811 . 64 GLN HB2 H 1.796 0.02 2 812 . 64 GLN CG C 33.382 0.2 1 813 . 64 GLN HG3 H 2.113 0.02 1 814 . 64 GLN HG2 H 2.113 0.02 1 815 . 64 GLN CD C 180.418 0.2 1 816 . 64 GLN NE2 N 111.035 0.2 1 817 . 64 GLN HE21 H 7.430 0.02 2 818 . 64 GLN HE22 H 6.766 0.02 2 819 . 64 GLN C C 174.782 0.2 1 820 . 65 PRO CA C 61.772 0.2 1 821 . 65 PRO HA H 4.620 0.02 1 822 . 65 PRO CB C 31.998 0.2 1 823 . 65 PRO HB3 H 2.004 0.02 2 824 . 65 PRO HB2 H 2.146 0.02 2 825 . 65 PRO CG C 27.920 0.2 1 826 . 65 PRO HG3 H 1.586 0.02 2 827 . 65 PRO HG2 H 1.650 0.02 2 828 . 65 PRO CD C 49.998 0.2 1 829 . 65 PRO HD3 H 3.591 0.02 2 830 . 65 PRO HD2 H 3.863 0.02 2 831 . 66 GLU N N 129.446 0.2 1 832 . 66 GLU H H 10.152 0.02 1 833 . 66 GLU CA C 56.131 0.2 1 834 . 66 GLU CB C 33.416 0.2 1 stop_ save_