data_5250 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; 1H, 13C and 15N resonance assignment of the RNA-binding domain dimer form Bacillus subtilis transcriptional antiterminator GlcT ; _BMRB_accession_number 5250 _BMRB_flat_file_name bmr5250.str _Entry_type original _Submission_date 2002-01-08 _Accession_date 2002-01-08 _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 Stoldt Matthias . . 2 Langbein Ines . . 3 Stuelke Joerg . . 4 Gorlach Matthias . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 409 "13C chemical shifts" 298 "15N chemical shifts" 71 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2002-09-26 original author . stop_ _Original_release_date 2002-09-26 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; 1H, 13C and 15N resonance assignment of the RNA-binding domain dimer form Bacillus subtilis transcriptional antiterminator GlcT ; _Citation_status published _Citation_type 'BMRB only' _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID ? loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Stoldt Matthias . . 2 Langbein Ines . . 3 Stuelke Joerg . . 4 Gorlach Matthias . . stop_ _Journal_abbreviation . _Journal_volume . _Journal_issue . _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first . _Page_last . _Year . _Details . save_ ################################## # Molecular system description # ################################## save_system_GlcT-RBD _Saveframe_category molecular_system _Mol_system_name 'GlcT-RBD dimer' _Abbreviation_common GlcT-RBD _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'GlcT-RBD subunit 1' $GlcT-RBD 'GlcT-RBD subunit 2' $GlcT-RBD 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 'GlcT-RBD subunit 1' 1 'GlcT-RBD subunit 2' stop_ loop_ _Biological_function 'transcriptional antiterminator' stop_ _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_GlcT-RBD _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'RNA-binding domain of transcriptional antiterminator GlcT' _Abbreviation_common GlcT-RBD _Molecular_mass . _Mol_thiol_state 'not present' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 74 _Mol_residue_sequence ; MRGSHHHHHHGSVDVNGSFT VKKVLNNNVLIASHHKYSEV VLIGKGIGFGKKQDDVIEDK GYDKMFILKDEKEQ ; loop_ _Residue_seq_code _Residue_label 1 MET 2 ARG 3 GLY 4 SER 5 HIS 6 HIS 7 HIS 8 HIS 9 HIS 10 HIS 11 GLY 12 SER 13 VAL 14 ASP 15 VAL 16 ASN 17 GLY 18 SER 19 PHE 20 THR 21 VAL 22 LYS 23 LYS 24 VAL 25 LEU 26 ASN 27 ASN 28 ASN 29 VAL 30 LEU 31 ILE 32 ALA 33 SER 34 HIS 35 HIS 36 LYS 37 TYR 38 SER 39 GLU 40 VAL 41 VAL 42 LEU 43 ILE 44 GLY 45 LYS 46 GLY 47 ILE 48 GLY 49 PHE 50 GLY 51 LYS 52 LYS 53 GLN 54 ASP 55 ASP 56 VAL 57 ILE 58 GLU 59 ASP 60 LYS 61 GLY 62 TYR 63 ASP 64 LYS 65 MET 66 PHE 67 ILE 68 LEU 69 LYS 70 ASP 71 GLU 72 LYS 73 GLU 74 GLN 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 3RIO "Crystal Structure Of Glct Cat-Prdi" 81.08 180 100.00 100.00 1.13e-31 DBJ BAI84997 "BglG family transcriptional antiterminator [Bacillus subtilis subsp. natto BEST195]" 81.08 288 100.00 100.00 1.50e-31 DBJ BAM52031 "transcriptional antiterminator BglG family [Synechocystis sp. PCC 6803]" 81.08 288 100.00 100.00 1.56e-31 DBJ BAM57608 "transcriptional antiterminator BglG family [Bacillus subtilis BEST7003]" 81.08 281 98.33 100.00 4.46e-31 DBJ GAK78204 "transcriptional antiterminator [Bacillus subtilis Miyagi-4]" 81.08 288 100.00 100.00 1.50e-31 EMBL CAA72077 "transcription antiterminator [Bacillus subtilis subsp. subtilis str. 168]" 81.08 281 98.33 100.00 4.46e-31 EMBL CAB13261 "transcriptional antiterminator (BglG family) [Bacillus subtilis subsp. subtilis str. 168]" 81.08 288 100.00 100.00 1.56e-31 EMBL CCU57949 "transcriptional antiterminator (BglG family) [Bacillus subtilis E1]" 81.08 288 100.00 100.00 1.50e-31 EMBL CEI56549 "BglG family transcription antiterminator [Bacillus subtilis]" 81.08 281 98.33 100.00 4.46e-31 EMBL CEJ76972 "BglG family transcription antiterminator [Bacillus sp.]" 81.08 281 98.33 100.00 4.46e-31 GB ADM37475 "transcriptional antiterminator (BglG family) protein [Bacillus subtilis subsp. spizizenii str. W23]" 81.08 288 100.00 100.00 1.50e-31 GB ADV96407 "transcriptional antiterminator (BglG family) protein [Bacillus subtilis BSn5]" 81.08 288 100.00 100.00 1.50e-31 GB AEP86362 "transcription antiterminator, GlcT [Bacillus subtilis subsp. spizizenii TU-B-10]" 81.08 281 98.33 100.00 4.75e-31 GB AEP90533 "transcription antiterminator, GlcT [Bacillus subtilis subsp. subtilis str. RO-NN-1]" 81.08 288 100.00 100.00 1.50e-31 GB AFI28059 "transcriptional antiterminator (BglG family) protein [Bacillus sp. JS]" 81.08 288 100.00 100.00 1.54e-31 REF NP_389271 "BglG family transcription antiterminator [Bacillus subtilis subsp. subtilis str. 168]" 81.08 288 100.00 100.00 1.56e-31 REF WP_003218635 "MULTISPECIES: transcriptional antiterminator (BglG family) protein [Bacillales]" 81.08 288 100.00 100.00 1.50e-31 REF WP_003232429 "transcriptional antiterminator (BglG family) protein [Bacillus subtilis]" 81.08 288 100.00 100.00 1.59e-31 REF WP_003238961 "transcriptional antiterminator (BglG family) protein [Bacillus subtilis]" 81.08 281 98.33 100.00 5.06e-31 REF WP_009967114 "BglG family transcriptional antiterminator [Bacillus subtilis]" 81.08 288 100.00 100.00 1.56e-31 SP O31691 "RecName: Full=PtsGHI operon antiterminator; AltName: Full=RNA-binding antitermination protein GlcT [Bacillus subtilis subsp. su" 81.08 281 98.33 100.00 4.46e-31 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $GlcT-RBD 'Bacillus subtilis' 1423 Eubacteria . Bacillus subtilis 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 $GlcT-RBD 'recombinant technology' . . . . . stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Concentration_min_value _Concentration_max_value _Isotopic_labeling $GlcT-RBD . mM 2.0 3.0 '[U-13C; U-15N]' stop_ save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model UnityINOVA _Field_strength 600 _Details . save_ save_NMR_spectrometer_2 _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model UnityINOVA _Field_strength 750 _Details . save_ ####################### # Sample conditions # ####################### save_cond_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 6.5 0.1 n/a temperature 298 0.2 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 DSS H 1 'methyl protons' ppm 0.0 internal direct . . . 1.0 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_set_1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $cond_1 _Chem_shift_reference_set_label $chemical_shift_reference _Mol_system_component_name 'GlcT-RBD 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 55.6 0.05 1 2 . 1 MET HA H 4.01 0.02 1 3 . 1 MET CB C 33.9 0.05 1 4 . 1 MET HB2 H 2.06 0.02 1 5 . 1 MET HB3 H 2.06 0.02 1 6 . 1 MET CG C 31.3 0.05 1 7 . 1 MET HG2 H 2.53 0.02 1 8 . 1 MET HG3 H 2.53 0.02 1 9 . 1 MET HE H 2.02 0.02 1 10 . 1 MET CE C 17.1 0.05 1 11 . 2 ARG CA C 56.8 0.05 1 12 . 2 ARG HA H 4.34 0.02 1 13 . 2 ARG CB C 31.0 0.05 1 14 . 2 ARG HB2 H 1.76 0.02 2 15 . 2 ARG HB3 H 1.82 0.02 2 16 . 2 ARG CG C 27.3 0.05 1 17 . 2 ARG HG2 H 1.61 0.02 2 18 . 2 ARG HG3 H 1.63 0.02 2 19 . 2 ARG CD C 43.6 0.05 1 20 . 2 ARG HD2 H 3.14 0.02 1 21 . 2 ARG HD3 H 3.14 0.02 1 22 . 3 GLY N N 114.4 0.05 1 23 . 3 GLY H H 8.59 0.02 1 24 . 3 GLY CA C 45.5 0.05 1 25 . 3 GLY HA2 H 3.92 0.02 1 26 . 3 GLY HA3 H 3.92 0.02 1 27 . 4 SER N N 119.3 0.05 1 28 . 4 SER H H 8.22 0.02 1 29 . 4 SER CA C 58.6 0.05 1 30 . 4 SER HA H 4.46 0.02 1 31 . 4 SER CB C 64.2 0.05 1 32 . 4 SER HB2 H 3.81 0.02 1 33 . 4 SER HB3 H 3.81 0.02 1 34 . 4 SER C C 176.8 0.05 1 35 . 5 HIS C C 174.2 0.05 1 36 . 10 HIS CA C 56.5 0.05 1 37 . 10 HIS HA H 4.58 0.02 1 38 . 10 HIS CB C 30.4 0.05 1 39 . 10 HIS HB2 H 3.04 0.02 2 40 . 10 HIS HB3 H 3.14 0.02 2 41 . 10 HIS C C 175.7 0.05 1 42 . 11 GLY N N 113.9 0.05 1 43 . 11 GLY H H 8.43 0.02 1 44 . 11 GLY CA C 45.5 0.05 1 45 . 11 GLY HA2 H 3.95 0.02 1 46 . 11 GLY HA3 H 3.95 0.02 1 47 . 11 GLY C C 174.3 0.05 1 48 . 12 SER N N 118.7 0.05 1 49 . 12 SER H H 8.18 0.02 1 50 . 12 SER CA C 58.6 0.05 1 51 . 12 SER HA H 4.36 0.02 1 52 . 12 SER CB C 64.1 0.05 1 53 . 12 SER HB2 H 3.73 0.02 2 54 . 12 SER HB3 H 3.76 0.02 2 55 . 12 SER C C 174.9 0.05 1 56 . 13 VAL N N 124.3 0.05 1 57 . 13 VAL H H 8.11 0.02 1 58 . 13 VAL CA C 62.4 0.05 1 59 . 13 VAL HA H 4.09 0.02 1 60 . 13 VAL CB C 33.1 0.05 1 61 . 13 VAL HB H 2.02 0.02 1 62 . 13 VAL HG1 H 0.83 0.02 1 63 . 13 VAL HG2 H 0.83 0.02 1 64 . 13 VAL CG1 C 21.4 0.05 1 65 . 13 VAL CG2 C 20.6 0.05 1 66 . 13 VAL C C 175.9 0.05 1 67 . 14 ASP N N 127.3 0.05 1 68 . 14 ASP H H 8.33 0.02 1 69 . 14 ASP CA C 54.4 0.05 1 70 . 14 ASP HA H 4.57 0.02 1 71 . 14 ASP CB C 41.5 0.05 1 72 . 14 ASP HB2 H 2.50 0.02 2 73 . 14 ASP HB3 H 2.64 0.02 2 74 . 14 ASP C C 176.6 0.05 1 75 . 15 VAL N N 123.8 0.05 1 76 . 15 VAL H H 8.04 0.02 1 77 . 15 VAL CA C 62.7 0.05 1 78 . 15 VAL HA H 4.00 0.02 1 79 . 15 VAL CB C 32.7 0.05 1 80 . 15 VAL HB H 2.00 0.02 1 81 . 15 VAL HG1 H 0.79 0.02 1 82 . 15 VAL HG2 H 0.79 0.02 1 83 . 15 VAL CG1 C 20.3 0.05 1 84 . 15 VAL CG2 C 21.4 0.05 1 85 . 15 VAL C C 176.3 0.05 1 86 . 16 ASN N N 124.6 0.05 1 87 . 16 ASN H H 8.41 0.02 1 88 . 16 ASN CA C 53.9 0.05 1 89 . 16 ASN HA H 4.64 0.02 1 90 . 16 ASN CB C 39.4 0.05 1 91 . 16 ASN HB2 H 2.71 0.02 1 92 . 16 ASN HB3 H 2.71 0.02 1 93 . 16 ASN ND2 N 116.8 0.05 1 94 . 16 ASN HD21 H 6.84 0.02 2 95 . 16 ASN HD22 H 7.62 0.02 2 96 . 16 ASN C C 176.0 0.05 1 97 . 17 GLY N N 112.8 0.05 1 98 . 17 GLY H H 8.21 0.02 1 99 . 17 GLY CA C 45.8 0.05 1 100 . 17 GLY HA2 H 3.86 0.02 2 101 . 17 GLY HA3 H 3.90 0.02 2 102 . 17 GLY C C 173.4 0.05 1 103 . 18 SER N N 117.4 0.05 1 104 . 18 SER H H 7.69 0.02 1 105 . 18 SER CA C 58.3 0.05 1 106 . 18 SER HA H 4.61 0.02 1 107 . 18 SER CB C 65.2 0.05 1 108 . 18 SER HB2 H 3.66 0.02 2 109 . 18 SER HB3 H 3.77 0.02 2 110 . 18 SER C C 173.3 0.05 1 111 . 19 PHE N N 122.6 0.05 1 112 . 19 PHE H H 8.76 0.02 1 113 . 19 PHE CA C 56.7 0.05 1 114 . 19 PHE HA H 5.32 0.02 1 115 . 19 PHE CB C 42.0 0.05 1 116 . 19 PHE HB2 H 2.78 0.02 2 117 . 19 PHE HB3 H 2.91 0.02 2 118 . 19 PHE CD1 C 131.8 0.05 1 119 . 19 PHE HD1 H 7.11 0.02 1 120 . 19 PHE CE1 C 132.0 0.05 1 121 . 19 PHE HE1 H 7.24 0.02 1 122 . 19 PHE CZ C 130.5 0.05 1 123 . 19 PHE HZ H 7.16 0.02 1 124 . 19 PHE C C 175.7 0.05 1 125 . 20 THR N N 120.1 0.05 1 126 . 20 THR H H 8.40 0.02 1 127 . 20 THR CA C 61.8 0.05 1 128 . 20 THR HA H 5.08 0.02 1 129 . 20 THR CB C 69.9 0.05 1 130 . 20 THR HB H 4.01 0.02 1 131 . 20 THR HG2 H 1.09 0.02 1 132 . 20 THR CG2 C 21.9 0.05 1 133 . 20 THR C C 175.2 0.05 1 134 . 21 VAL N N 130.3 0.05 1 135 . 21 VAL H H 9.57 0.02 1 136 . 21 VAL CA C 66.2 0.05 1 137 . 21 VAL HA H 3.41 0.02 1 138 . 21 VAL CB C 32.4 0.05 1 139 . 21 VAL HB H 2.31 0.02 1 140 . 21 VAL HG1 H 0.61 0.02 2 141 . 21 VAL HG2 H 0.94 0.02 2 142 . 21 VAL CG1 C 22.6 0.05 1 143 . 21 VAL CG2 C 24.0 0.05 1 144 . 21 VAL C C 176.3 0.05 1 145 . 22 LYS N N 133.1 0.05 1 146 . 22 LYS H H 9.72 0.02 1 147 . 22 LYS CA C 57.7 0.05 1 148 . 22 LYS HA H 4.56 0.02 1 149 . 22 LYS CB C 33.9 0.05 1 150 . 22 LYS HB2 H 1.46 0.02 2 151 . 22 LYS HB3 H 1.77 0.02 2 152 . 22 LYS CG C 25.0 0.05 1 153 . 22 LYS HG2 H 1.38 0.02 2 154 . 22 LYS HG3 H 1.56 0.02 2 155 . 22 LYS CD C 29.1 0.05 1 156 . 22 LYS HD2 H 1.59 0.02 2 157 . 22 LYS HD3 H 1.70 0.02 2 158 . 22 LYS CE C 41.9 0.05 1 159 . 22 LYS HE2 H 2.94 0.02 1 160 . 22 LYS HE3 H 2.94 0.02 1 161 . 22 LYS C C 175.8 0.05 1 162 . 23 LYS N N 120.0 0.05 1 163 . 23 LYS H H 7.77 0.02 1 164 . 23 LYS CA C 56.1 0.05 1 165 . 23 LYS HA H 4.36 0.02 1 166 . 23 LYS CB C 36.7 0.05 1 167 . 23 LYS HB2 H 1.52 0.02 2 168 . 23 LYS HB3 H 1.66 0.02 2 169 . 23 LYS CG C 25.0 0.05 1 170 . 23 LYS HG2 H 1.14 0.02 2 171 . 23 LYS HG3 H 1.22 0.02 2 172 . 23 LYS CD C 29.3 0.05 1 173 . 23 LYS HD2 H 1.59 0.02 1 174 . 23 LYS HD3 H 1.59 0.02 1 175 . 23 LYS CE C 42.2 0.05 1 176 . 23 LYS HE2 H 2.88 0.02 2 177 . 23 LYS HE3 H 2.90 0.02 2 178 . 23 LYS C C 174.2 0.05 1 179 . 24 VAL N N 131.2 0.05 1 180 . 24 VAL H H 9.11 0.02 1 181 . 24 VAL CA C 63.1 0.05 1 182 . 24 VAL HA H 3.98 0.02 1 183 . 24 VAL CB C 32.3 0.05 1 184 . 24 VAL HB H 1.97 0.02 1 185 . 24 VAL HG1 H 0.70 0.02 2 186 . 24 VAL HG2 H 0.83 0.02 2 187 . 24 VAL CG1 C 21.7 0.05 1 188 . 24 VAL CG2 C 22.3 0.05 1 189 . 24 VAL C C 176.2 0.05 1 190 . 25 LEU N N 131.6 0.05 1 191 . 25 LEU H H 8.37 0.02 1 192 . 25 LEU CA C 57.2 0.05 1 193 . 25 LEU HA H 4.30 0.02 1 194 . 25 LEU CB C 42.2 0.05 1 195 . 25 LEU HB2 H 1.18 0.02 2 196 . 25 LEU HB3 H 1.43 0.02 2 197 . 25 LEU CG C 28.2 0.05 1 198 . 25 LEU HG H 1.39 0.02 1 199 . 25 LEU HD1 H 0.59 0.02 2 200 . 25 LEU HD2 H 0.64 0.02 2 201 . 25 LEU CD1 C 25.7 0.05 1 202 . 25 LEU CD2 C 23.7 0.05 1 203 . 25 LEU C C 177.5 0.05 1 204 . 26 ASN N N 117.5 0.05 1 205 . 26 ASN H H 8.44 0.02 1 206 . 26 ASN CA C 53.1 0.05 1 207 . 26 ASN HA H 4.44 0.02 1 208 . 26 ASN CB C 37.5 0.05 1 209 . 26 ASN HB2 H 3.24 0.02 2 210 . 26 ASN HB3 H 3.31 0.02 2 211 . 26 ASN ND2 N 114.4 0.05 1 212 . 26 ASN HD21 H 6.49 0.02 2 213 . 26 ASN HD22 H 7.72 0.02 2 214 . 26 ASN C C 174.1 0.05 1 215 . 27 ASN N N 115.1 0.05 1 216 . 27 ASN H H 8.33 0.02 1 217 . 27 ASN CA C 56.3 0.05 1 218 . 27 ASN HA H 4.18 0.02 1 219 . 27 ASN CB C 38.8 0.05 1 220 . 27 ASN HB2 H 2.69 0.02 1 221 . 27 ASN HB3 H 2.69 0.02 1 222 . 27 ASN ND2 N 115.6 0.05 1 223 . 27 ASN HD21 H 7.05 0.02 2 224 . 27 ASN HD22 H 7.58 0.02 2 225 . 27 ASN C C 176.2 0.05 1 226 . 28 ASN N N 118.5 0.05 1 227 . 28 ASN H H 8.98 0.02 1 228 . 28 ASN CA C 52.4 0.05 1 229 . 28 ASN HA H 5.63 0.02 1 230 . 28 ASN CB C 41.8 0.05 1 231 . 28 ASN HB2 H 2.69 0.02 2 232 . 28 ASN HB3 H 3.20 0.02 2 233 . 28 ASN ND2 N 118.2 0.05 1 234 . 28 ASN HD21 H 6.86 0.02 2 235 . 28 ASN HD22 H 7.56 0.02 2 236 . 28 ASN C C 173.9 0.05 1 237 . 29 VAL N N 121.2 0.05 1 238 . 29 VAL H H 7.10 0.02 1 239 . 29 VAL CA C 61.6 0.05 1 240 . 29 VAL HA H 5.14 0.02 1 241 . 29 VAL CB C 35.4 0.05 1 242 . 29 VAL HB H 1.60 0.02 1 243 . 29 VAL HG1 H 0.52 0.02 2 244 . 29 VAL HG2 H 0.91 0.02 2 245 . 29 VAL CG1 C 22.0 0.05 1 246 . 29 VAL CG2 C 21.5 0.05 1 247 . 29 VAL C C 174.5 0.05 1 248 . 30 LEU N N 126.2 0.05 1 249 . 30 LEU H H 8.81 0.02 1 250 . 30 LEU CA C 53.6 0.05 1 251 . 30 LEU HA H 4.90 0.02 1 252 . 30 LEU CB C 47.0 0.05 1 253 . 30 LEU HB2 H 1.65 0.02 1 254 . 30 LEU HB3 H 1.65 0.02 1 255 . 30 LEU CG C 26.0 0.05 1 256 . 30 LEU HG H 1.57 0.02 1 257 . 30 LEU HD1 H 0.68 0.02 2 258 . 30 LEU HD2 H 0.74 0.02 2 259 . 30 LEU CD1 C 26.1 0.05 1 260 . 30 LEU CD2 C 28.6 0.05 1 261 . 30 LEU C C 173.9 0.05 1 262 . 31 ILE N N 123.6 0.05 1 263 . 31 ILE H H 9.01 0.02 1 264 . 31 ILE CA C 60.4 0.05 1 265 . 31 ILE HA H 4.93 0.02 1 266 . 31 ILE CB C 39.5 0.05 1 267 . 31 ILE HB H 1.56 0.02 1 268 . 31 ILE HG2 H 0.88 0.02 1 269 . 31 ILE CG2 C 17.6 0.05 1 270 . 31 ILE CG1 C 28.1 0.05 1 271 . 31 ILE HG12 H 0.64 0.02 2 272 . 31 ILE HG13 H 1.36 0.02 2 273 . 31 ILE HD1 H 0.63 0.02 1 274 . 31 ILE CD1 C 13.7 0.05 1 275 . 31 ILE C C 175.9 0.05 1 276 . 32 ALA N N 134.8 0.05 1 277 . 32 ALA H H 9.45 0.02 1 278 . 32 ALA CA C 50.6 0.05 1 279 . 32 ALA HA H 5.33 0.02 1 280 . 32 ALA HB H 1.14 0.02 1 281 . 32 ALA CB C 24.4 0.05 1 282 . 32 ALA C C 175.1 0.05 1 283 . 33 SER N N 118.1 0.05 1 284 . 33 SER H H 9.44 0.02 1 285 . 33 SER CA C 57.6 0.05 1 286 . 33 SER HA H 5.17 0.02 1 287 . 33 SER CB C 66.1 0.05 1 288 . 33 SER HB2 H 3.87 0.02 2 289 . 33 SER HB3 H 4.03 0.02 2 290 . 33 SER C C 173.3 0.05 1 291 . 34 HIS N N 124.3 0.05 1 292 . 34 HIS H H 7.80 0.02 1 293 . 34 HIS CA C 57.3 0.05 1 294 . 34 HIS HA H 4.70 0.02 1 295 . 34 HIS CB C 36.8 0.05 1 296 . 34 HIS HB2 H 2.82 0.02 2 297 . 34 HIS HB3 H 3.15 0.02 2 298 . 34 HIS CD2 C 120.1 0.05 1 299 . 34 HIS CE1 C 138.8 0.05 1 300 . 34 HIS HD2 H 5.90 0.02 1 301 . 34 HIS HE1 H 7.21 0.02 1 302 . 35 HIS CA C 59.7 0.05 1 303 . 35 HIS HA H 4.22 0.02 1 304 . 35 HIS CB C 29.9 0.05 1 305 . 35 HIS HB2 H 2.86 0.02 2 306 . 35 HIS HB3 H 2.99 0.02 2 307 . 35 HIS CD2 C 120.3 0.05 1 308 . 35 HIS CE1 C 138.2 0.05 1 309 . 35 HIS HD2 H 6.76 0.02 1 310 . 35 HIS HE1 H 7.78 0.02 1 311 . 35 HIS C C 175.7 0.05 1 312 . 36 LYS N N 125.5 0.05 1 313 . 36 LYS H H 9.25 0.02 1 314 . 36 LYS CA C 57.4 0.05 1 315 . 36 LYS HA H 4.16 0.02 1 316 . 36 LYS CB C 34.4 0.05 1 317 . 36 LYS HB2 H 1.10 0.02 2 318 . 36 LYS HB3 H 1.18 0.02 2 319 . 36 LYS CG C 25.1 0.05 1 320 . 36 LYS HG2 H 0.65 0.02 2 321 . 36 LYS HG3 H 1.01 0.02 2 322 . 36 LYS CD C 29.5 0.05 1 323 . 36 LYS HD2 H 1.31 0.02 2 324 . 36 LYS HD3 H 1.43 0.02 2 325 . 36 LYS CE C 42.3 0.05 1 326 . 36 LYS HE2 H 2.81 0.02 1 327 . 36 LYS HE3 H 2.81 0.02 1 328 . 36 LYS C C 177.6 0.05 1 329 . 37 TYR N N 121.0 0.05 1 330 . 37 TYR H H 7.97 0.02 1 331 . 37 TYR CA C 57.4 0.05 1 332 . 37 TYR HA H 4.72 0.02 1 333 . 37 TYR CB C 40.4 0.05 1 334 . 37 TYR HB2 H 2.24 0.02 2 335 . 37 TYR HB3 H 3.31 0.02 2 336 . 37 TYR CD1 C 133.1 0.05 1 337 . 37 TYR HD1 H 6.59 0.02 1 338 . 37 TYR CE1 C 117.9 0.05 1 339 . 37 TYR HE1 H 6.58 0.02 1 340 . 37 TYR C C 176.3 0.05 1 341 . 38 SER N N 118.7 0.05 1 342 . 38 SER H H 8.41 0.02 1 343 . 38 SER CA C 63.2 0.05 1 344 . 38 SER HA H 4.20 0.02 1 345 . 38 SER CB C 62.5 0.05 1 346 . 38 SER HB2 H 4.13 0.02 2 347 . 38 SER HB3 H 4.23 0.02 2 348 . 38 SER C C 175.8 0.05 1 349 . 39 GLU N N 125.8 0.05 1 350 . 39 GLU H H 8.15 0.02 1 351 . 39 GLU CA C 56.7 0.05 1 352 . 39 GLU HA H 5.17 0.02 1 353 . 39 GLU CB C 34.9 0.05 1 354 . 39 GLU HB2 H 1.99 0.02 2 355 . 39 GLU HB3 H 2.13 0.02 2 356 . 39 GLU CG C 38.2 0.05 1 357 . 39 GLU HG2 H 2.20 0.02 2 358 . 39 GLU HG3 H 2.23 0.02 2 359 . 39 GLU C C 174.4 0.05 1 360 . 40 VAL N N 119.6 0.05 1 361 . 40 VAL H H 9.16 0.02 1 362 . 40 VAL CA C 58.7 0.05 1 363 . 40 VAL HA H 5.41 0.02 1 364 . 40 VAL CB C 36.2 0.05 1 365 . 40 VAL HB H 2.00 0.02 1 366 . 40 VAL HG1 H 0.59 0.02 2 367 . 40 VAL HG2 H 0.88 0.02 2 368 . 40 VAL CG1 C 20.1 0.05 1 369 . 40 VAL CG2 C 23.6 0.05 1 370 . 40 VAL C C 174.4 0.05 1 371 . 41 VAL N N 124.1 0.05 1 372 . 41 VAL H H 8.57 0.02 1 373 . 41 VAL CA C 61.0 0.05 1 374 . 41 VAL HA H 4.52 0.02 1 375 . 41 VAL CB C 33.9 0.05 1 376 . 41 VAL HB H 1.20 0.02 1 377 . 41 VAL HG1 H -0.50 0.02 2 378 . 41 VAL HG2 H 0.32 0.02 2 379 . 41 VAL CG1 C 19.4 0.05 1 380 . 41 VAL CG2 C 21.3 0.05 1 381 . 41 VAL C C 175.1 0.05 1 382 . 42 LEU N N 128.9 0.05 1 383 . 42 LEU H H 8.75 0.02 1 384 . 42 LEU CA C 52.9 0.05 1 385 . 42 LEU HA H 4.95 0.02 1 386 . 42 LEU CB C 45.2 0.05 1 387 . 42 LEU HB2 H 0.74 0.02 2 388 . 42 LEU HB3 H 1.33 0.02 2 389 . 42 LEU CG C 26.3 0.05 1 390 . 42 LEU HG H 0.88 0.02 1 391 . 42 LEU HD1 H -0.30 0.02 2 392 . 42 LEU HD2 H -0.17 0.02 2 393 . 42 LEU CD1 C 22.3 0.05 1 394 . 42 LEU CD2 C 24.6 0.05 1 395 . 42 LEU C C 175.5 0.05 1 396 . 43 ILE N N 122.2 0.05 1 397 . 43 ILE H H 8.41 0.02 1 398 . 43 ILE CA C 59.9 0.05 1 399 . 43 ILE HA H 5.39 0.02 1 400 . 43 ILE CB C 41.0 0.05 1 401 . 43 ILE HB H 1.72 0.02 1 402 . 43 ILE HG2 H 0.91 0.02 1 403 . 43 ILE CG2 C 16.4 0.05 1 404 . 43 ILE CG1 C 27.6 0.05 1 405 . 43 ILE HG12 H 1.15 0.02 2 406 . 43 ILE HG13 H 1.55 0.02 2 407 . 43 ILE HD1 H 0.68 0.02 1 408 . 43 ILE CD1 C 14.0 0.05 1 409 . 43 ILE C C 176.9 0.05 1 410 . 44 GLY N N 119.4 0.05 1 411 . 44 GLY H H 9.11 0.02 1 412 . 44 GLY CA C 46.1 0.05 1 413 . 44 GLY HA2 H 4.01 0.02 2 414 . 44 GLY HA3 H 4.32 0.02 2 415 . 44 GLY C C 172.6 0.05 1 416 . 45 LYS N N 127.4 0.05 1 417 . 45 LYS H H 8.61 0.02 1 418 . 45 LYS CA C 58.2 0.05 1 419 . 45 LYS HA H 4.14 0.02 1 420 . 45 LYS CB C 31.6 0.05 1 421 . 45 LYS HB2 H 1.75 0.02 1 422 . 45 LYS HB3 H 1.75 0.02 1 423 . 45 LYS CG C 24.8 0.05 1 424 . 45 LYS HG2 H 1.27 0.02 2 425 . 45 LYS HG3 H 1.42 0.02 2 426 . 45 LYS CD C 29.3 0.05 1 427 . 45 LYS HD2 H 1.66 0.02 1 428 . 45 LYS HD3 H 1.66 0.02 1 429 . 45 LYS CE C 42.4 0.05 1 430 . 45 LYS HE2 H 2.96 0.02 1 431 . 45 LYS HE3 H 2.96 0.02 1 432 . 45 LYS C C 178.8 0.05 1 433 . 46 GLY N N 120.4 0.05 1 434 . 46 GLY H H 9.29 0.02 1 435 . 46 GLY CA C 47.2 0.05 1 436 . 46 GLY HA2 H 3.81 0.02 2 437 . 46 GLY HA3 H 4.07 0.02 2 438 . 46 GLY C C 177.2 0.05 1 439 . 47 ILE N N 121.8 0.05 1 440 . 47 ILE H H 7.54 0.02 1 441 . 47 ILE CA C 64.3 0.05 1 442 . 47 ILE HA H 4.04 0.02 1 443 . 47 ILE CB C 38.6 0.05 1 444 . 47 ILE HB H 1.73 0.02 1 445 . 47 ILE HG2 H 0.73 0.02 1 446 . 47 ILE CG2 C 17.6 0.05 1 447 . 47 ILE CG1 C 27.1 0.05 1 448 . 47 ILE HG12 H 1.23 0.02 1 449 . 47 ILE HG13 H 1.23 0.02 1 450 . 47 ILE HD1 H 0.68 0.02 1 451 . 47 ILE CD1 C 15.2 0.05 1 452 . 47 ILE C C 175.6 0.05 1 453 . 48 GLY N N 109.1 0.05 1 454 . 48 GLY H H 8.39 0.02 1 455 . 48 GLY CA C 45.0 0.05 1 456 . 48 GLY HA2 H 3.50 0.02 2 457 . 48 GLY HA3 H 3.96 0.02 2 458 . 48 GLY C C 174.7 0.05 1 459 . 49 PHE N N 125.8 0.05 1 460 . 49 PHE H H 7.42 0.02 1 461 . 49 PHE CA C 59.9 0.05 1 462 . 49 PHE HA H 4.24 0.02 1 463 . 49 PHE CB C 39.1 0.05 1 464 . 49 PHE HB2 H 3.01 0.02 2 465 . 49 PHE HB3 H 3.10 0.02 2 466 . 49 PHE CD1 C 132.1 0.05 1 467 . 49 PHE HD1 H 7.22 0.02 1 468 . 49 PHE CE1 C 132.2 0.05 1 469 . 49 PHE HE1 H 7.35 0.02 1 470 . 49 PHE CZ C 130.3 0.05 1 471 . 49 PHE HZ H 7.30 0.02 1 472 . 49 PHE C C 177.4 0.05 1 473 . 50 GLY N N 119.8 0.05 1 474 . 50 GLY H H 8.61 0.02 1 475 . 50 GLY CA C 46.0 0.05 1 476 . 50 GLY HA2 H 3.41 0.02 2 477 . 50 GLY HA3 H 3.72 0.02 2 478 . 50 GLY C C 174.2 0.05 1 479 . 51 LYS N N 120.8 0.05 1 480 . 51 LYS H H 7.26 0.02 1 481 . 51 LYS CA C 54.1 0.05 1 482 . 51 LYS HA H 4.69 0.02 1 483 . 51 LYS CB C 34.7 0.05 1 484 . 51 LYS HB2 H 1.56 0.02 2 485 . 51 LYS HB3 H 1.79 0.02 2 486 . 51 LYS CG C 25.2 0.05 1 487 . 51 LYS HG2 H 1.23 0.02 2 488 . 51 LYS HG3 H 1.53 0.02 2 489 . 51 LYS CD C 28.3 0.05 1 490 . 51 LYS HD2 H 1.52 0.02 2 491 . 51 LYS HD3 H 1.62 0.02 2 492 . 51 LYS CE C 42.9 0.05 1 493 . 51 LYS HE2 H 2.93 0.02 2 494 . 51 LYS HE3 H 3.12 0.02 2 495 . 51 LYS C C 175.6 0.05 1 496 . 52 LYS N N 122.9 0.05 1 497 . 52 LYS H H 8.79 0.02 1 498 . 52 LYS CA C 54.3 0.05 1 499 . 52 LYS HA H 4.47 0.02 1 500 . 52 LYS CB C 36.2 0.05 1 501 . 52 LYS HB2 H 1.72 0.02 1 502 . 52 LYS HB3 H 1.72 0.02 1 503 . 52 LYS CG C 23.5 0.05 1 504 . 52 LYS HG2 H 1.23 0.02 2 505 . 52 LYS HG3 H 1.42 0.02 2 506 . 52 LYS CD C 29.4 0.05 1 507 . 52 LYS HD2 H 1.61 0.02 1 508 . 52 LYS HD3 H 1.61 0.02 1 509 . 52 LYS CE C 42.5 0.05 1 510 . 52 LYS HE2 H 2.99 0.02 1 511 . 52 LYS HE3 H 2.99 0.02 1 512 . 52 LYS C C 174.9 0.05 1 513 . 53 GLN N N 122.5 0.05 1 514 . 53 GLN H H 8.30 0.02 1 515 . 53 GLN CA C 58.5 0.05 1 516 . 53 GLN HA H 3.44 0.02 1 517 . 53 GLN CB C 29.1 0.05 1 518 . 53 GLN HB2 H 1.83 0.02 2 519 . 53 GLN HB3 H 2.00 0.02 2 520 . 53 GLN CG C 33.9 0.05 1 521 . 53 GLN HG2 H 2.30 0.02 2 522 . 53 GLN HG3 H 2.46 0.02 2 523 . 53 GLN NE2 N 115.3 0.05 1 524 . 53 GLN HE21 H 6.82 0.02 2 525 . 53 GLN HE22 H 7.57 0.02 2 526 . 53 GLN C C 176.2 0.05 1 527 . 54 ASP N N 121.6 0.05 1 528 . 54 ASP H H 8.98 0.02 1 529 . 54 ASP CA C 58.2 0.05 1 530 . 54 ASP HA H 4.16 0.02 1 531 . 54 ASP CB C 39.1 0.05 1 532 . 54 ASP HB2 H 2.82 0.02 2 533 . 54 ASP HB3 H 3.30 0.02 2 534 . 54 ASP C C 176.0 0.05 1 535 . 55 ASP N N 124.6 0.05 1 536 . 55 ASP H H 7.98 0.02 1 537 . 55 ASP CA C 56.0 0.05 1 538 . 55 ASP HA H 4.64 0.02 1 539 . 55 ASP CB C 41.7 0.05 1 540 . 55 ASP HB2 H 2.60 0.02 2 541 . 55 ASP HB3 H 2.81 0.02 2 542 . 55 ASP C C 175.4 0.05 1 543 . 56 VAL N N 124.3 0.05 1 544 . 56 VAL H H 8.46 0.02 1 545 . 56 VAL CA C 62.0 0.05 1 546 . 56 VAL HA H 4.90 0.02 1 547 . 56 VAL CB C 33.5 0.05 1 548 . 56 VAL HB H 1.90 0.02 1 549 . 56 VAL HG1 H 0.85 0.02 2 550 . 56 VAL HG2 H 0.96 0.02 2 551 . 56 VAL CG1 C 21.8 0.05 1 552 . 56 VAL CG2 C 21.6 0.05 1 553 . 56 VAL C C 177.1 0.05 1 554 . 57 ILE N N 127.7 0.05 1 555 . 57 ILE H H 9.05 0.02 1 556 . 57 ILE CA C 59.4 0.05 1 557 . 57 ILE HA H 4.66 0.02 1 558 . 57 ILE CB C 40.7 0.05 1 559 . 57 ILE HB H 1.97 0.02 1 560 . 57 ILE HG2 H 0.93 0.02 1 561 . 57 ILE CG2 C 17.6 0.05 1 562 . 57 ILE CG1 C 27.0 0.05 1 563 . 57 ILE HG12 H 1.05 0.02 2 564 . 57 ILE HG13 H 1.47 0.02 2 565 . 57 ILE HD1 H 0.68 0.02 1 566 . 57 ILE CD1 C 13.2 0.05 1 567 . 57 ILE C C 175.3 0.05 1 568 . 58 GLU N N 126.4 0.05 1 569 . 58 GLU H H 8.68 0.02 1 570 . 58 GLU CA C 56.6 0.05 1 571 . 58 GLU HA H 4.40 0.02 1 572 . 58 GLU CB C 31.6 0.05 1 573 . 58 GLU HB2 H 1.93 0.02 2 574 . 58 GLU HB3 H 2.08 0.02 2 575 . 58 GLU CG C 37.1 0.05 1 576 . 58 GLU HG2 H 2.27 0.02 2 577 . 58 GLU HG3 H 2.33 0.02 2 578 . 58 GLU C C 176.3 0.05 1 579 . 59 ASP N N 122.5 0.05 1 580 . 59 ASP H H 8.36 0.02 1 581 . 59 ASP CA C 54.5 0.05 1 582 . 59 ASP HA H 4.82 0.02 1 583 . 59 ASP CB C 40.2 0.05 1 584 . 59 ASP HB2 H 2.57 0.02 2 585 . 59 ASP HB3 H 2.73 0.02 2 586 . 59 ASP C C 175.8 0.05 1 587 . 60 LYS N N 122.4 0.05 1 588 . 60 LYS H H 8.20 0.02 1 589 . 60 LYS CA C 56.3 0.05 1 590 . 60 LYS HA H 4.21 0.02 1 591 . 60 LYS CB C 33.1 0.05 1 592 . 60 LYS HB2 H 1.71 0.02 2 593 . 60 LYS HB3 H 1.89 0.02 2 594 . 60 LYS CG C 24.5 0.05 1 595 . 60 LYS HG2 H 1.23 0.02 1 596 . 60 LYS HG3 H 1.23 0.02 1 597 . 60 LYS CD C 29.4 0.05 1 598 . 60 LYS HD2 H 1.56 0.02 2 599 . 60 LYS HD3 H 1.61 0.02 2 600 . 60 LYS CE C 42.5 0.05 1 601 . 60 LYS HE2 H 2.92 0.02 1 602 . 60 LYS HE3 H 2.92 0.02 1 603 . 60 LYS C C 176.6 0.05 1 604 . 61 GLY N N 110.9 0.05 1 605 . 61 GLY H H 8.27 0.02 1 606 . 61 GLY CA C 46.5 0.05 1 607 . 61 GLY HA2 H 3.79 0.02 2 608 . 61 GLY HA3 H 3.85 0.02 2 609 . 61 GLY C C 173.4 0.05 1 610 . 62 TYR N N 117.6 0.05 1 611 . 62 TYR H H 6.89 0.02 1 612 . 62 TYR CA C 55.1 0.05 1 613 . 62 TYR HA H 4.69 0.02 1 614 . 62 TYR CB C 39.8 0.05 1 615 . 62 TYR HB2 H 2.52 0.02 2 616 . 62 TYR HB3 H 2.92 0.02 2 617 . 62 TYR CD1 C 134.0 0.05 1 618 . 62 TYR HD1 H 6.50 0.02 1 619 . 62 TYR CE1 C 118.3 0.05 1 620 . 62 TYR HE1 H 6.78 0.02 1 621 . 62 TYR C C 173.7 0.05 1 622 . 63 ASP N N 123.6 0.05 1 623 . 63 ASP H H 9.37 0.02 1 624 . 63 ASP CA C 56.1 0.05 1 625 . 63 ASP HA H 4.76 0.02 1 626 . 63 ASP CB C 43.1 0.05 1 627 . 63 ASP HB2 H 2.63 0.02 2 628 . 63 ASP HB3 H 2.77 0.02 2 629 . 63 ASP C C 176.7 0.05 1 630 . 64 LYS N N 120.5 0.05 1 631 . 64 LYS H H 8.15 0.02 1 632 . 64 LYS CA C 55.8 0.05 1 633 . 64 LYS HA H 4.63 0.02 1 634 . 64 LYS CB C 39.1 0.05 1 635 . 64 LYS HB2 H 1.41 0.02 2 636 . 64 LYS HB3 H 1.48 0.02 2 637 . 64 LYS CG C 26.3 0.05 1 638 . 64 LYS HG2 H 1.26 0.02 1 639 . 64 LYS HG3 H 1.26 0.02 1 640 . 64 LYS CD C 30.4 0.05 1 641 . 64 LYS HD2 H 1.53 0.02 2 642 . 64 LYS HD3 H 1.58 0.02 2 643 . 64 LYS CE C 42.3 0.05 1 644 . 64 LYS HE2 H 2.82 0.02 1 645 . 64 LYS HE3 H 2.82 0.02 1 646 . 64 LYS C C 173.3 0.05 1 647 . 65 MET N N 125.1 0.05 1 648 . 65 MET H H 8.42 0.02 1 649 . 65 MET CA C 54.4 0.05 1 650 . 65 MET HA H 4.89 0.02 1 651 . 65 MET CB C 36.5 0.05 1 652 . 65 MET HB2 H 1.23 0.02 2 653 . 65 MET HB3 H 1.63 0.02 2 654 . 65 MET CG C 31.8 0.05 1 655 . 65 MET HG2 H 1.66 0.02 2 656 . 65 MET HG3 H 1.84 0.02 2 657 . 65 MET HE H 1.65 0.02 1 658 . 65 MET CE C 17.6 0.05 1 659 . 65 MET C C 173.2 0.05 1 660 . 66 PHE N N 128.2 0.05 1 661 . 66 PHE H H 9.26 0.02 1 662 . 66 PHE CA C 55.2 0.05 1 663 . 66 PHE HA H 5.12 0.02 1 664 . 66 PHE CB C 42.1 0.05 1 665 . 66 PHE HB2 H 2.54 0.02 2 666 . 66 PHE HB3 H 2.63 0.02 2 667 . 66 PHE CD1 C 131.5 0.05 1 668 . 66 PHE HD1 H 6.86 0.02 1 669 . 66 PHE CE1 C 132.0 0.05 1 670 . 66 PHE HE1 H 6.86 0.02 1 671 . 66 PHE CZ C 130.0 0.05 1 672 . 66 PHE HZ H 7.24 0.02 1 673 . 66 PHE C C 176.0 0.05 1 674 . 67 ILE N N 120.9 0.05 1 675 . 67 ILE H H 9.29 0.02 1 676 . 67 ILE CA C 60.1 0.05 1 677 . 67 ILE HA H 4.86 0.02 1 678 . 67 ILE CB C 41.0 0.05 1 679 . 67 ILE HB H 1.82 0.02 1 680 . 67 ILE HG2 H 0.34 0.02 1 681 . 67 ILE CG2 C 18.4 0.05 1 682 . 67 ILE CG1 C 26.6 0.05 1 683 . 67 ILE HG12 H 0.77 0.02 2 684 . 67 ILE HG13 H 1.36 0.02 2 685 . 67 ILE HD1 H 0.63 0.02 1 686 . 67 ILE CD1 C 14.4 0.05 1 687 . 67 ILE C C 175.9 0.05 1 688 . 68 LEU N N 129.7 0.05 1 689 . 68 LEU H H 8.32 0.02 1 690 . 68 LEU CA C 56.8 0.05 1 691 . 68 LEU HA H 3.53 0.02 1 692 . 68 LEU CB C 42.7 0.05 1 693 . 68 LEU HB2 H 1.35 0.02 2 694 . 68 LEU HB3 H 1.69 0.02 2 695 . 68 LEU CG C 26.7 0.05 1 696 . 68 LEU HG H 1.24 0.02 1 697 . 68 LEU HD1 H 0.26 0.02 2 698 . 68 LEU HD2 H 0.63 0.02 2 699 . 68 LEU CD1 C 23.1 0.05 1 700 . 68 LEU CD2 C 26.0 0.05 1 701 . 68 LEU C C 176.7 0.05 1 702 . 69 LYS N N 130.7 0.05 1 703 . 69 LYS H H 8.58 0.02 1 704 . 69 LYS CA C 56.4 0.05 1 705 . 69 LYS HA H 4.26 0.02 1 706 . 69 LYS CB C 33.9 0.05 1 707 . 69 LYS HB2 H 1.38 0.02 2 708 . 69 LYS HB3 H 1.68 0.02 2 709 . 69 LYS CG C 24.9 0.05 1 710 . 69 LYS HG2 H 1.23 0.02 1 711 . 69 LYS HG3 H 1.23 0.02 1 712 . 69 LYS CD C 29.3 0.05 1 713 . 69 LYS HD2 H 1.47 0.02 2 714 . 69 LYS HD3 H 1.63 0.02 2 715 . 69 LYS CE C 42.5 0.05 1 716 . 69 LYS HE2 H 2.95 0.02 1 717 . 69 LYS HE3 H 2.95 0.02 1 718 . 69 LYS C C 175.5 0.05 1 719 . 70 ASP N N 126.7 0.05 1 720 . 70 ASP H H 8.36 0.02 1 721 . 70 ASP CA C 54.3 0.05 1 722 . 70 ASP HA H 4.68 0.02 1 723 . 70 ASP CB C 42.5 0.05 1 724 . 70 ASP HB2 H 2.56 0.02 2 725 . 70 ASP HB3 H 2.67 0.02 2 726 . 70 ASP C C 175.9 0.05 1 727 . 71 GLU N N 125.6 0.05 1 728 . 71 GLU H H 8.34 0.02 1 729 . 71 GLU CA C 56.5 0.05 1 730 . 71 GLU HA H 4.46 0.02 1 731 . 71 GLU CB C 31.0 0.05 1 732 . 71 GLU HB2 H 1.93 0.02 2 733 . 71 GLU HB3 H 2.13 0.02 2 734 . 71 GLU CG C 36.6 0.05 1 735 . 71 GLU HG2 H 2.24 0.02 1 736 . 71 GLU HG3 H 2.24 0.02 1 737 . 71 GLU C C 176.3 0.05 1 738 . 72 LYS N N 125.3 0.05 1 739 . 72 LYS H H 8.23 0.02 1 740 . 72 LYS CA C 56.9 0.05 1 741 . 72 LYS HA H 4.26 0.02 1 742 . 72 LYS CB C 33.3 0.05 1 743 . 72 LYS HB2 H 1.82 0.02 1 744 . 72 LYS HB3 H 1.82 0.02 1 745 . 72 LYS CG C 25.0 0.05 1 746 . 72 LYS HG2 H 1.41 0.02 1 747 . 72 LYS HG3 H 1.41 0.02 1 748 . 72 LYS CD C 29.5 0.05 1 749 . 72 LYS HD2 H 1.64 0.02 1 750 . 72 LYS HD3 H 1.64 0.02 1 751 . 72 LYS CE C 42.4 0.05 1 752 . 72 LYS HE2 H 2.98 0.02 1 753 . 72 LYS HE3 H 2.98 0.02 1 754 . 72 LYS C C 176.8 0.05 1 755 . 73 GLU N N 126.0 0.05 1 756 . 73 GLU H H 8.37 0.02 1 757 . 73 GLU CA C 56.9 0.05 1 758 . 73 GLU HA H 4.28 0.02 1 759 . 73 GLU CB C 30.6 0.05 1 760 . 73 GLU HB2 H 1.92 0.02 2 761 . 73 GLU HB3 H 2.06 0.02 2 762 . 73 GLU CG C 36.6 0.05 1 763 . 73 GLU HG2 H 2.28 0.02 1 764 . 73 GLU HG3 H 2.28 0.02 1 765 . 73 GLU C C 175.9 0.05 1 766 . 74 GLN N N 129.8 0.05 1 767 . 74 GLN H H 7.98 0.02 1 768 . 74 GLN CA C 57.7 0.05 1 769 . 74 GLN HA H 4.12 0.02 1 770 . 74 GLN CB C 30.7 0.05 1 771 . 74 GLN HB2 H 1.90 0.02 2 772 . 74 GLN HB3 H 2.08 0.02 2 773 . 74 GLN CG C 34.5 0.05 1 774 . 74 GLN HG2 H 2.28 0.02 1 775 . 74 GLN HG3 H 2.28 0.02 1 776 . 74 GLN NE2 N 115.8 0.05 1 777 . 74 GLN HE21 H 6.78 0.02 2 778 . 74 GLN HE22 H 7.51 0.02 2 stop_ save_