data_4102 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; 1H, 13C and 15N NMR Backbone Assignments of 25.5 KDa Metallo-beta-lactamase ; _BMRB_accession_number 4102 _BMRB_flat_file_name bmr4102.str _Entry_type original _Submission_date 1998-01-28 _Accession_date 1998-02-02 _Entry_origination author _NMR_STAR_version 2.1.1 _Experimental_method NMR _Details ; The data reported here describes 1H/13C/15N resonance assignments for the mature form of the antibiotic resistant metallo-beta-lactamase from Bacteroides fragilis (residues 18-249) ; loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Scrofani Sergio D.B. . 2 Wright Peter E. . 3 Dyson Jane H. . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 2 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 435 "13C chemical shifts" 657 "15N chemical shifts" 213 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 1998-10-09 original author . stop_ _Original_release_date 1998-10-09 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full ; Scrofani, S. D.B., Wright, P. E., and Dyson, J. H., "1H, 13C and 15N NMR Backbone Assignments of 25.5 kDa Metallo-b-lactamase from Bacteroides fragilis," J. Biomol. NMR 12, 201-202 (1998). ; _Citation_title ; 1H, 13C and 15N NMR Backbone Assignments of 25.5 kDa Metallo-b-lactamase from Bacteroides fragilis ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code 98399499 _PubMed_ID ? loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Scrofani Sergio D.B. . 2 Wright Peter E. . 3 Dyson Jane H. . stop_ _Journal_abbreviation 'J. Biomol. NMR' _Journal_volume 12 _Journal_issue 1 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 201 _Page_last 202 _Year 1998 _Details . loop_ _Keyword 'Antibiotic Resistance' 'cocatalytic zinc' enzymatic metallo-beta-lactamase metalloprotein NMR stop_ save_ ################################## # Molecular system description # ################################## save_system_CcrA _Saveframe_category molecular_system _Mol_system_name metallo-beta-lactamase _Abbreviation_common CcrA _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label CcrA $CcrA Zn1 $entity_ZN Zn2 $entity_ZN stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state monomer _System_paramagnetic no _System_thiol_state . loop_ _Biological_function 'hydrolysis of beta-lactam antibiotics' stop_ _Database_query_date . _Details ; Metallo-beta-lactamase hydrolyzes beta-lactam based antibiotics (such as penicillins), and is the major source of antibiotic resistance in the human pathogen, Bacteroides fragilis. ; save_ ######################## # Monomeric polymers # ######################## save_CcrA _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common metallo-beta-lactamase _Abbreviation_common CcrA _Molecular_mass 25500 _Mol_thiol_state . _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 232 _Mol_residue_sequence ; AQKSVKISDDISITQLSDKV YTYVSLAEIEGWGMVPSNGM IVINNHQAALLDTPINDAQT EMLVNWVTDSLHAKVTTFIP DHWHGDCLGGLGYLQRKGVQ SYANQMTIDLAKEKGLPVPE HGFTDSLTVSLDGMPLQCYY LGGGHATDNIVVWLPTENIL FGGCMLKDNQATSIGNISDA DVTAWPKTLDKVKAKFPSAR YVVPGHGDYGGTELIEHTKQ IVNQYIESTSKP ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 18 ALA 2 19 GLN 3 20 LYS 4 21 SER 5 22 VAL 6 23 LYS 7 24 ILE 8 25 SER 9 26 ASP 10 27 ASP 11 28 ILE 12 29 SER 13 30 ILE 14 31 THR 15 32 GLN 16 33 LEU 17 34 SER 18 35 ASP 19 36 LYS 20 37 VAL 21 38 TYR 22 39 THR 23 40 TYR 24 41 VAL 25 42 SER 26 43 LEU 27 44 ALA 28 45 GLU 29 46 ILE 30 47 GLU 31 48 GLY 32 49 TRP 33 50 GLY 34 51 MET 35 52 VAL 36 53 PRO 37 54 SER 38 55 ASN 39 56 GLY 40 57 MET 41 58 ILE 42 59 VAL 43 60 ILE 44 61 ASN 45 62 ASN 46 63 HIS 47 64 GLN 48 65 ALA 49 66 ALA 50 67 LEU 51 68 LEU 52 69 ASP 53 70 THR 54 71 PRO 55 72 ILE 56 73 ASN 57 74 ASP 58 75 ALA 59 76 GLN 60 77 THR 61 78 GLU 62 79 MET 63 80 LEU 64 81 VAL 65 82 ASN 66 83 TRP 67 84 VAL 68 85 THR 69 86 ASP 70 87 SER 71 88 LEU 72 89 HIS 73 90 ALA 74 91 LYS 75 92 VAL 76 93 THR 77 94 THR 78 95 PHE 79 96 ILE 80 97 PRO 81 98 ASP 82 99 HIS 83 100 TRP 84 101 HIS 85 102 GLY 86 103 ASP 87 104 CYS 88 105 LEU 89 106 GLY 90 107 GLY 91 108 LEU 92 109 GLY 93 110 TYR 94 111 LEU 95 112 GLN 96 113 ARG 97 114 LYS 98 115 GLY 99 116 VAL 100 117 GLN 101 118 SER 102 119 TYR 103 120 ALA 104 121 ASN 105 122 GLN 106 123 MET 107 124 THR 108 125 ILE 109 126 ASP 110 127 LEU 111 128 ALA 112 129 LYS 113 130 GLU 114 131 LYS 115 132 GLY 116 133 LEU 117 134 PRO 118 135 VAL 119 136 PRO 120 137 GLU 121 138 HIS 122 139 GLY 123 140 PHE 124 141 THR 125 142 ASP 126 143 SER 127 144 LEU 128 145 THR 129 146 VAL 130 147 SER 131 148 LEU 132 149 ASP 133 150 GLY 134 151 MET 135 152 PRO 136 153 LEU 137 154 GLN 138 155 CYS 139 156 TYR 140 157 TYR 141 158 LEU 142 159 GLY 143 160 GLY 144 161 GLY 145 162 HIS 146 163 ALA 147 164 THR 148 165 ASP 149 166 ASN 150 167 ILE 151 168 VAL 152 169 VAL 153 170 TRP 154 171 LEU 155 172 PRO 156 173 THR 157 174 GLU 158 175 ASN 159 176 ILE 160 177 LEU 161 178 PHE 162 179 GLY 163 180 GLY 164 181 CYS 165 182 MET 166 183 LEU 167 184 LYS 168 185 ASP 169 186 ASN 170 187 GLN 171 188 ALA 172 189 THR 173 190 SER 174 191 ILE 175 192 GLY 176 193 ASN 177 194 ILE 178 195 SER 179 196 ASP 180 197 ALA 181 198 ASP 182 199 VAL 183 200 THR 184 201 ALA 185 202 TRP 186 203 PRO 187 204 LYS 188 205 THR 189 206 LEU 190 207 ASP 191 208 LYS 192 209 VAL 193 210 LYS 194 211 ALA 195 212 LYS 196 213 PHE 197 214 PRO 198 215 SER 199 216 ALA 200 217 ARG 201 218 TYR 202 219 VAL 203 220 VAL 204 221 PRO 205 222 GLY 206 223 HIS 207 224 GLY 208 225 ASP 209 226 TYR 210 227 GLY 211 228 GLY 212 229 THR 213 230 GLU 214 231 LEU 215 232 ILE 216 233 GLU 217 234 HIS 218 235 THR 219 236 LYS 220 237 GLN 221 238 ILE 222 239 VAL 223 240 ASN 224 241 GLN 225 242 TYR 226 243 ILE 227 244 GLU 228 245 SER 229 246 THR 230 247 SER 231 248 LYS 232 249 PRO stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-11-11 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 1A7T "Metallo-Beta-Lactamase With Mes" 100.00 232 98.28 99.57 2.83e-167 PDB 1A8T "Metallo-Beta-Lactamase In Complex With L-159,061" 100.00 232 98.28 99.57 2.83e-167 PDB 1HLK "Metallo-Beta-Lactamase From Bacteroides Fragilis In Complex With A Tricyclic Inhibitor" 97.84 227 99.12 100.00 1.85e-164 PDB 1KR3 "Crystal Structure Of The Metallo Beta-Lactamase From Bacteroides Fragilis (Cfia) In Complex With The Tricyclic Inhibitor Sb-236" 100.00 232 99.14 100.00 1.34e-168 PDB 1ZNB Metallo-Beta-Lactamase 100.00 232 97.84 99.14 2.95e-166 PDB 2BMI Metallo-Beta-Lactamase 100.00 232 99.14 100.00 1.34e-168 PDB 2ZNB "Metallo-Beta-Lactamase (Cadmium-Bound Form)" 100.00 232 97.84 99.14 2.95e-166 PDB 3ZNB "Metallo-Beta-Lactamase (Zn, Hg-Bound Form)" 100.00 232 97.84 99.14 2.95e-166 PDB 4ZNB "Metallo-Beta-Lactamase (C181s Mutant)" 100.00 232 97.41 98.71 3.65e-165 DBJ BAC06841 "metallo-beta-lactamase [Bacteroides fragilis]" 100.00 249 97.84 99.14 1.30e-166 DBJ BAC06842 "metallo-beta-lactamase [Bacteroides fragilis]" 100.00 249 97.84 99.14 1.30e-166 DBJ BAC06843 "metallo-beta-lactamase [Bacteroides fragilis]" 100.00 249 97.41 98.71 1.42e-165 DBJ BAC06844 "metallo-beta-lactamase [Bacteroides fragilis]" 100.00 249 97.84 99.14 1.30e-166 DBJ BAC06845 "metallo-beta-lactamase [Bacteroides fragilis]" 100.00 249 97.41 99.14 5.37e-166 EMBL CAH41960 "metallo-betalactamase [Bacteroides fragilis]" 100.00 249 97.84 99.14 1.30e-166 EMBL CAQ87572 "CFIA protein [Bacteroides fragilis]" 100.00 249 97.41 99.14 5.37e-166 EMBL CAQ87573 "CFIA protein [Bacteroides fragilis]" 100.00 244 99.14 100.00 7.79e-169 EMBL CAQ87574 "CFIA protein [Bacteroides fragilis]" 100.00 249 99.14 100.00 5.96e-169 EMBL CAQ87575 "CFIA protein [Bacteroides fragilis]" 80.17 203 98.39 99.46 1.36e-131 GB AAA22904 "beta-lactamase [Bacteroides fragilis]" 100.00 249 99.14 100.00 5.96e-169 GB AAA22907 "imipenem-cefoxitin-hydrolyzing enzyme precursor [Bacteroides fragilis]" 100.00 249 99.14 100.00 5.96e-169 GB AAM93063 "beta-lactamase [Bacteroides fragilis]" 100.00 249 98.28 99.57 2.93e-167 GB AAR04097 "metallo-beta-lactamase [Bacteroides fragilis]" 100.00 249 96.98 99.14 1.47e-165 GB AAR04099 "metallo-beta-lactamase [Bacteroides fragilis]" 100.00 249 97.41 99.14 9.59e-166 REF WP_005780969 "subclass B1 metallo-beta-lactamase CfiA14 [Bacteroides fragilis]" 100.00 249 98.28 99.57 2.93e-167 REF WP_005808062 "subclass B1 metallo-beta-lactamase CcrA [Bacteroides fragilis]" 100.00 249 99.14 100.00 5.96e-169 REF WP_005821510 "subclass B1 metallo-beta-lactamase CfiA4 [Bacteroides fragilis]" 100.00 249 97.41 99.14 5.37e-166 REF WP_015083750 "subclass B1 metallo-beta-lactamase CfiA2 [Bacteroides fragilis]" 100.00 249 97.84 99.14 1.30e-166 REF WP_032536010 "MULTISPECIES: CcrA family subclass B1 metallo-beta-lactamase [Bacteroides]" 100.00 249 98.71 100.00 3.11e-168 SP P25910 "RecName: Full=Beta-lactamase type II; AltName: Full=Cephalosporinase; AltName: Full=Imipenem-cefoxitin hydrolyzing enzyme; AltN" 100.00 249 99.14 100.00 5.96e-169 stop_ save_ ############# # Ligands # ############# save_ZN _Saveframe_category ligand _Mol_type "non-polymer (NON-POLYMER)" _Name_common 'ZINC ION' _BMRB_code ZN _PDB_code ZN _Molecular_mass 65.409 _Mol_charge 2 _Mol_paramagnetic . _Mol_aromatic no _Details . loop_ _Atom_name _PDB_atom_name _Atom_type _Atom_chirality _Atom_charge _Atom_oxidation_number _Atom_unpaired_electrons ZN ZN ZN . 2 . ? stop_ _Mol_thiol_state . _Sequence_homology_query_date . save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $CcrA 'B. fragilis' 817 Eubacteria . Bacteroides fragilis 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 $CcrA 'recombinant technology' 'E. coli' Escherichia coli . . stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_one _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Concentration_min_value _Concentration_max_value _Isotopic_labeling $CcrA . mM 0.2 1.0 [U-15N] HEPES 10 mM . . . 'zinc chloride' 10 uM . . . 'sodium azide' 0.01 % . . . D2O 5 % . . . H2O 95 % . . . stop_ save_ save_sample_two _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Concentration_min_value _Concentration_max_value _Isotopic_labeling $CcrA . mM 0.5 1.0 '[U-13C; U-15N]' HEPES 10 mM . . . 'zinc chloride' 10 uM . . . 'sodium azide' 0.01 % . . . D2O 5 % . . . H2O 95 % . . . stop_ save_ save_sample_three _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $CcrA 0.8 mM '[86%-2H; U-13C; U-15N]' 'sodium phosphate' 120 mM . D2O 5 % . H2O 95 % . stop_ save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer_one _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model AMX500 _Field_strength 500 _Details . save_ save_NMR_spectrometer_two _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model DMX600 _Field_strength 600 _Details . save_ ############################# # NMR applied experiments # ############################# save__1 _Saveframe_category NMR_applied_experiment _Sample_label . save_ ####################### # Sample conditions # ####################### save_sample_conditions _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 7.0 0.05 n/a temperature 295.0 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 _Indirect_shift_ratio_citation_label _Correction_value_citation_label DSS C 13 methyl ppm 0.00 external indirect . . . 0.25144952 $entry_citation $entry_citation DSS H 1 methyl ppm 0.00 external direct . . . 1.00000000 $entry_citation $entry_citation DSS N 15 methyl ppm 0.00 external indirect . . . 0.10132905 $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_chemical_shift_assignment_CcrA _Saveframe_category assigned_chemical_shifts _Details . loop_ _Sample_label $sample_two stop_ _Sample_conditions_label $sample_conditions _Chem_shift_reference_set_label $chemical_shift_reference _Mol_system_component_name CcrA _Text_data_format . _Text_data . loop_ _Atom_shift_assign_ID _Residue_author_seq_code _Residue_seq_code _Residue_label _Atom_name _Atom_type _Chem_shift_value _Chem_shift_value_error _Chem_shift_ambiguity_code 1 . 2 GLN HA H 4.47 0.02 1 2 . 2 GLN CA C 55.5 0.2 1 3 . 2 GLN CB C 29.7 0.2 1 4 . 2 GLN C C 175.7 0.2 1 5 . 3 LYS HA H 4.45 0.02 1 6 . 3 LYS H H 8.62 0.02 1 7 . 3 LYS CA C 56.6 0.2 1 8 . 3 LYS CB C 33.2 0.2 1 9 . 3 LYS C C 176.00 0.2 1 10 . 3 LYS N N 123.8 0.2 1 11 . 4 SER HA H 5.14 0.02 1 12 . 4 SER H H 8.41 0.02 1 13 . 4 SER CA C 57.4 0.2 1 14 . 4 SER CB C 65.00 0.2 1 15 . 4 SER C C 173.8 0.2 1 16 . 4 SER N N 119.4 0.2 1 17 . 5 VAL HA H 4.35 0.02 1 18 . 5 VAL H H 9.19 0.02 1 19 . 5 VAL CA C 60.9 0.2 1 20 . 5 VAL CB C 34.6 0.2 1 21 . 5 VAL C C 174.7 0.2 1 22 . 5 VAL N N 123.8 0.2 1 23 . 6 LYS HA H 4.61 0.02 1 24 . 6 LYS H H 8.72 0.02 1 25 . 6 LYS CA C 56.2 0.2 1 26 . 6 LYS CB C 32.2 0.2 1 27 . 6 LYS C C 177.00 0.2 1 28 . 6 LYS N N 127.5 0.2 1 29 . 7 ILE HA H 4.1 0.02 1 30 . 7 ILE H H 8.07 0.02 1 31 . 7 ILE CA C 62.4 0.2 1 32 . 7 ILE CB C 38.00 0.2 1 33 . 7 ILE C C 175.00 0.2 1 34 . 7 ILE N N 123.7 0.2 1 35 . 8 SER HA H 4.63 0.02 1 36 . 8 SER H H 8.44 0.02 1 37 . 8 SER CA C 56.6 0.2 1 38 . 8 SER CB C 64.8 0.2 1 39 . 8 SER C C 181.4 0.2 1 40 . 8 SER N N 116.1 0.2 1 41 . 9 ASP HA H 4.39 0.02 1 42 . 9 ASP H H 8.93 0.02 1 43 . 9 ASP CA C 57.4 0.2 1 44 . 9 ASP CB C 40.4 0.2 1 45 . 9 ASP C C 176.4 0.2 1 46 . 9 ASP N N 118.2 0.2 1 47 . 10 ASP HA H 4.67 0.02 1 48 . 10 ASP H H 8.28 0.02 1 49 . 10 ASP CA C 53.4 0.2 1 50 . 10 ASP CB C 42.3 0.2 1 51 . 10 ASP C C 175.00 0.2 1 52 . 10 ASP N N 113.2 0.2 1 53 . 11 ILE HA H 5.33 0.02 1 54 . 11 ILE H H 7.21 0.02 1 55 . 11 ILE CA C 60.9 0.2 1 56 . 11 ILE CB C 40.5 0.2 1 57 . 11 ILE C C 174.4 0.2 1 58 . 11 ILE N N 119.3 0.2 1 59 . 12 SER HA H 5.35 0.02 1 60 . 12 SER H H 8.74 0.02 1 61 . 12 SER CA C 56.6 0.2 1 62 . 12 SER CB C 66.4 0.2 1 63 . 12 SER C C 172.6 0.2 1 64 . 12 SER N N 122.7 0.2 1 65 . 13 ILE HA H 5.05 0.02 1 66 . 13 ILE H H 9.28 0.02 1 67 . 13 ILE CA C 60.00 0.2 1 68 . 13 ILE CB C 41.6 0.2 1 69 . 13 ILE C C 174.7 0.2 1 70 . 13 ILE N N 122.5 0.2 1 71 . 14 THR HA H 4.86 0.02 1 72 . 14 THR H H 9.36 0.02 1 73 . 14 THR CA C 62.00 0.2 1 74 . 14 THR CB C 71.4 0.2 1 75 . 14 THR C C 172.9 0.2 1 76 . 14 THR N N 123.8 0.2 1 77 . 15 GLN HA H 3.95 0.02 1 78 . 15 GLN H H 9.14 0.02 1 79 . 15 GLN CA C 56.8 0.2 1 80 . 15 GLN CB C 29.1 0.2 1 81 . 15 GLN C C 174.7 0.2 1 82 . 15 GLN N N 130.4 0.2 1 83 . 16 LEU HA H 4.24 0.02 1 84 . 16 LEU H H 8.72 0.02 1 85 . 16 LEU CA C 56.2 0.2 1 86 . 16 LEU CB C 43.00 0.2 1 87 . 16 LEU C C 176.3 0.2 1 88 . 16 LEU N N 127.5 0.2 1 89 . 17 SER HA H 4.76 0.02 1 90 . 17 SER H H 8.5 0.02 1 91 . 17 SER CA C 56.5 0.2 1 92 . 17 SER CB C 65.7 0.2 1 93 . 17 SER C C 173.4 0.2 1 94 . 17 SER N N 116.2 0.2 1 95 . 18 ASP HA H 4.81 0.02 1 96 . 18 ASP H H 8.69 0.02 1 97 . 18 ASP CA C 57.7 0.2 1 98 . 18 ASP CB C 40.4 0.2 1 99 . 18 ASP C C 176.7 0.2 1 100 . 18 ASP N N 117.7 0.2 1 101 . 19 LYS HA H 4.69 0.02 1 102 . 19 LYS H H 7.59 0.02 1 103 . 19 LYS CA C 56.00 0.2 1 104 . 19 LYS CB C 35.4 0.2 1 105 . 19 LYS C C 174.6 0.2 1 106 . 19 LYS N N 114.6 0.2 1 107 . 20 VAL HA H 5.03 0.02 1 108 . 20 VAL H H 7.05 0.02 1 109 . 20 VAL CA C 61.8 0.2 1 110 . 20 VAL CB C 33.8 0.2 1 111 . 20 VAL C C 173.2 0.2 1 112 . 20 VAL N N 116.8 0.2 1 113 . 21 TYR HA H 5.22 0.02 1 114 . 21 TYR H H 9.61 0.02 1 115 . 21 TYR CA C 55.5 0.2 1 116 . 21 TYR CB C 41.4 0.2 1 117 . 21 TYR C C 175.5 0.2 1 118 . 21 TYR N N 127.00 0.2 1 119 . 22 THR HA H 5.47 0.02 1 120 . 22 THR H H 9.6 0.02 1 121 . 22 THR CA C 58.9 0.2 1 122 . 22 THR CB C 71.3 0.2 1 123 . 22 THR C C 171.3 0.2 1 124 . 22 THR N N 116.4 0.2 1 125 . 23 TYR HA H 5.95 0.02 1 126 . 23 TYR H H 8.1 0.02 1 127 . 23 TYR CA C 55.00 0.2 1 128 . 23 TYR CB C 42.9 0.2 1 129 . 23 TYR C C 172.6 0.2 1 130 . 23 TYR N N 125.2 0.2 1 131 . 24 VAL HA H 5.01 0.02 1 132 . 24 VAL H H 8.93 0.02 1 133 . 24 VAL CA C 60.7 0.2 1 134 . 24 VAL CB C 34.3 0.2 1 135 . 24 VAL C C 175.6 0.2 1 136 . 24 VAL N N 121.7 0.2 1 137 . 25 SER HA H 5.69 0.02 1 138 . 25 SER H H 9.84 0.02 1 139 . 25 SER CA C 55.5 0.2 1 140 . 25 SER CB C 65.9 0.2 1 141 . 25 SER C C 174.2 0.2 1 142 . 25 SER N N 123.3 0.2 1 143 . 26 LEU HA H 4.91 0.02 1 144 . 26 LEU H H 9.05 0.02 1 145 . 26 LEU CA C 54.5 0.2 1 146 . 26 LEU CB C 43.9 0.2 1 147 . 26 LEU C C 176.00 0.2 1 148 . 26 LEU N N 128.00 0.2 1 149 . 27 ALA HA H 4.51 0.02 1 150 . 27 ALA H H 8.13 0.02 1 151 . 27 ALA CA C 51.7 0.2 1 152 . 27 ALA CB C 22.7 0.2 1 153 . 27 ALA C C 175.2 0.2 1 154 . 27 ALA N N 125.5 0.2 1 155 . 28 GLU HA H 4.66 0.02 1 156 . 28 GLU H H 8.57 0.02 1 157 . 28 GLU CA C 56.2 0.2 1 158 . 28 GLU CB C 29.9 0.2 1 159 . 28 GLU C C 176.00 0.2 1 160 . 28 GLU N N 123.00 0.2 1 161 . 29 ILE HA H 4.34 0.02 1 162 . 29 ILE H H 8.62 0.02 1 163 . 29 ILE CA C 60.00 0.2 1 164 . 29 ILE CB C 39.1 0.2 1 165 . 29 ILE C C 176.00 0.2 1 166 . 29 ILE N N 128.1 0.2 1 167 . 30 GLU HA H 4.08 0.02 1 168 . 30 GLU H H 9.01 0.02 1 169 . 30 GLU CA C 58.9 0.2 1 170 . 30 GLU CB C 29.1 0.2 1 171 . 30 GLU C C 177.1 0.2 1 172 . 30 GLU N N 130.9 0.2 1 173 . 31 GLY HA2 H 3.9 0.02 2 174 . 31 GLY HA3 H 3.9 0.02 2 175 . 31 GLY H H 8.95 0.02 1 176 . 31 GLY CA C 45.1 0.2 1 177 . 31 GLY C C 174.2 0.2 1 178 . 31 GLY N N 115.9 0.2 1 179 . 32 TRP HA H 4.76 0.02 1 180 . 32 TRP H H 8.54 0.02 1 181 . 32 TRP CA C 57.00 0.2 1 182 . 32 TRP CB C 31.4 0.2 1 183 . 32 TRP C C 175.9 0.2 1 184 . 32 TRP N N 120.9 0.2 1 185 . 33 GLY HA2 H 4.07 0.02 2 186 . 33 GLY HA3 H 4.07 0.02 2 187 . 33 GLY H H 8.37 0.02 1 188 . 33 GLY CA C 44.7 0.2 1 189 . 33 GLY C C 172.7 0.2 1 190 . 33 GLY N N 110.00 0.2 1 191 . 34 MET HA H 4.71 0.02 1 192 . 34 MET H H 8.5 0.02 1 193 . 34 MET CA C 54.5 0.2 1 194 . 34 MET CB C 30.9 0.2 1 195 . 34 MET C C 176.3 0.2 1 196 . 34 MET N N 121.9 0.2 1 197 . 35 VAL HA H 4.71 0.02 1 198 . 35 VAL H H 9.09 0.02 1 199 . 35 VAL CA C 59.3 0.2 1 200 . 35 VAL C C 174.5 0.2 1 201 . 35 VAL N N 129.5 0.2 1 202 . 36 PRO HA H 5.27 0.02 1 203 . 36 PRO CA C 61.7 0.2 1 204 . 36 PRO CB C 31.7 0.2 1 205 . 36 PRO C C 177.3 0.2 1 206 . 37 SER HA H 4.73 0.02 1 207 . 37 SER H H 9.39 0.02 1 208 . 37 SER CA C 59.00 0.2 1 209 . 37 SER CB C 65.4 0.2 1 210 . 37 SER C C 171.4 0.2 1 211 . 37 SER N N 121.7 0.2 1 212 . 38 ASN HA H 5.79 0.02 1 213 . 38 ASN H H 7.83 0.02 1 214 . 38 ASN CA C 50.9 0.2 1 215 . 38 ASN CB C 41.2 0.2 1 216 . 38 ASN C C 175.5 0.2 1 217 . 38 ASN N N 119.7 0.2 1 218 . 39 GLY H H 6.51 0.02 1 219 . 39 GLY CA C 45.4 0.2 1 220 . 39 GLY C C 173.4 0.2 1 221 . 39 GLY N N 103.1 0.2 1 222 . 40 MET HA H 5.79 0.02 1 223 . 40 MET H H 9.35 0.02 1 224 . 40 MET CA C 53.4 0.2 1 225 . 40 MET CB C 36.1 0.2 1 226 . 40 MET C C 173.6 0.2 1 227 . 40 MET N N 119.6 0.2 1 228 . 41 ILE HA H 5.12 0.02 1 229 . 41 ILE H H 9.16 0.02 1 230 . 41 ILE CA C 60.3 0.2 1 231 . 41 ILE CB C 41.8 0.2 1 232 . 41 ILE C C 173.8 0.2 1 233 . 41 ILE N N 122.9 0.2 1 234 . 42 VAL HA H 5.13 0.02 1 235 . 42 VAL H H 9.11 0.02 1 236 . 42 VAL CA C 60.2 0.2 1 237 . 42 VAL CB C 34.2 0.2 1 238 . 42 VAL C C 174.5 0.2 1 239 . 42 VAL N N 129.3 0.2 1 240 . 43 ILE HA H 5.22 0.02 1 241 . 43 ILE H H 9.37 0.02 1 242 . 43 ILE CA C 59.00 0.2 1 243 . 43 ILE CB C 40.5 0.2 1 244 . 43 ILE C C 174.8 0.2 1 245 . 43 ILE N N 125.3 0.2 1 246 . 44 ASN HA H 4.84 0.02 1 247 . 44 ASN H H 8.81 0.02 1 248 . 44 ASN CA C 53.5 0.2 1 249 . 44 ASN CB C 39.4 0.2 1 250 . 44 ASN C C 174.00 0.2 1 251 . 44 ASN N N 120.5 0.2 1 252 . 45 ASN HA H 3.75 0.02 1 253 . 45 ASN H H 9.06 0.02 1 254 . 45 ASN CA C 54.00 0.2 1 255 . 45 ASN CB C 36.5 0.2 1 256 . 45 ASN C C 175.00 0.2 1 257 . 45 ASN N N 125.9 0.2 1 258 . 46 HIS HA H 4.07 0.02 1 259 . 46 HIS H H 8.92 0.02 1 260 . 46 HIS CA C 58.2 0.2 1 261 . 46 HIS CB C 26.9 0.2 1 262 . 46 HIS C C 173.8 0.2 1 263 . 46 HIS N N 109.2 0.2 1 264 . 47 GLN HA H 5.21 0.02 1 265 . 47 GLN H H 8.27 0.02 1 266 . 47 GLN CA C 54.8 0.2 1 267 . 47 GLN CB C 31.5 0.2 1 268 . 47 GLN C C 173.2 0.2 1 269 . 47 GLN N N 122.00 0.2 1 270 . 48 ALA HA H 6.03 0.02 1 271 . 48 ALA H H 9.05 0.02 1 272 . 48 ALA CA C 49.00 0.2 1 273 . 48 ALA CB C 23.2 0.2 1 274 . 48 ALA C C 175.7 0.2 1 275 . 48 ALA N N 122.4 0.2 1 276 . 49 ALA HA H 5.59 0.02 1 277 . 49 ALA H H 9.69 0.02 1 278 . 49 ALA CA C 48.9 0.2 1 279 . 49 ALA CB C 22.1 0.2 1 280 . 49 ALA C C 175.3 0.2 1 281 . 49 ALA N N 122.9 0.2 1 282 . 50 LEU HA H 5.24 0.02 1 283 . 50 LEU H H 8.76 0.02 1 284 . 50 LEU CA C 53.3 0.2 1 285 . 50 LEU CB C 45.3 0.2 1 286 . 50 LEU C C 173.7 0.2 1 287 . 50 LEU N N 123.5 0.2 1 288 . 51 LEU HA H 5.15 0.02 1 289 . 51 LEU H H 9.25 0.02 1 290 . 51 LEU CA C 54.5 0.2 1 291 . 51 LEU CB C 39.0 0.2 1 292 . 51 LEU C C 176.2 0.2 1 293 . 51 LEU N N 128.1 0.2 1 294 . 52 ASP HA H 4.85 0.02 1 295 . 52 ASP H H 7.33 0.02 1 296 . 52 ASP CA C 58.3 0.2 1 297 . 52 ASP CB C 40.3 0.2 1 298 . 52 ASP C C 178.3 0.2 1 299 . 52 ASP N N 112.3 0.2 1 300 . 53 THR HA H 4.71 0.02 1 301 . 53 THR H H 8.22 0.02 1 302 . 53 THR CA C 59.5 0.2 1 303 . 53 THR C C 174.1 0.2 1 304 . 53 THR N N 112.8 0.2 1 305 . 54 PRO HA H 4.41 0.02 1 306 . 54 PRO CA C 62.2 0.2 1 307 . 54 PRO CB C 34.7 0.2 1 308 . 54 PRO C C 175.3 0.2 1 309 . 55 ILE HA H 4.55 0.02 1 310 . 55 ILE H H 7.94 0.02 1 311 . 55 ILE CA C 61.4 0.2 1 312 . 55 ILE CB C 39.5 0.2 1 313 . 55 ILE C C 174.5 0.2 1 314 . 55 ILE N N 112.2 0.2 1 315 . 56 ASN HA H 4.86 0.02 1 316 . 56 ASN H H 6.77 0.02 1 317 . 56 ASN CA C 50.7 0.2 1 318 . 56 ASN CB C 41.1 0.2 1 319 . 56 ASN C C 176.7 0.2 1 320 . 56 ASN N N 111.9 0.2 1 321 . 57 ASP HA H 4.31 0.02 1 322 . 57 ASP H H 9.1 0.02 1 323 . 57 ASP CA C 57.5 0.2 1 324 . 57 ASP CB C 40.9 0.2 1 325 . 57 ASP C C 177.7 0.2 1 326 . 57 ASP N N 123.1 0.2 1 327 . 58 ALA HA H 4.03 0.02 1 328 . 58 ALA H H 8.33 0.02 1 329 . 58 ALA CA C 55.7 0.2 1 330 . 58 ALA CB C 17.8 0.2 1 331 . 58 ALA C C 181.3 0.2 1 332 . 58 ALA N N 126.2 0.2 1 333 . 59 GLN HA H 4.04 0.02 1 334 . 59 GLN H H 8.97 0.02 1 335 . 59 GLN CA C 58.8 0.2 1 336 . 59 GLN CB C 29.9 0.2 1 337 . 59 GLN C C 178.4 0.2 1 338 . 59 GLN N N 117.8 0.2 1 339 . 60 THR HA H 3.42 0.02 1 340 . 60 THR H H 7.36 0.02 1 341 . 60 THR CA C 68.3 0.2 1 342 . 60 THR CB C 68.3 0.2 1 343 . 60 THR C C 174.5 0.2 1 344 . 60 THR N N 116.7 0.2 1 345 . 61 GLU HA H 3.29 0.02 1 346 . 61 GLU H H 8.24 0.02 1 347 . 61 GLU CA C 59.4 0.2 1 348 . 61 GLU C C 177.1 0.2 1 349 . 61 GLU N N 123.9 0.2 1 350 . 62 MET HA H 4.09 0.02 1 351 . 62 MET H H 7.34 0.02 1 352 . 62 MET CA C 58.8 0.2 1 353 . 62 MET CB C 31.9 0.2 1 354 . 62 MET C C 178.9 0.2 1 355 . 62 MET N N 118.00 0.2 1 356 . 63 LEU HA H 3.96 0.02 1 357 . 63 LEU H H 7.67 0.02 1 358 . 63 LEU CA C 58.00 0.2 1 359 . 63 LEU CB C 42.9 0.2 1 360 . 63 LEU C C 177.9 0.2 1 361 . 63 LEU N N 120.5 0.2 1 362 . 64 VAL HA H 3.46 0.02 1 363 . 64 VAL H H 8.84 0.02 1 364 . 64 VAL CA C 67.4 0.2 1 365 . 64 VAL CB C 30.8 0.2 1 366 . 64 VAL C C 178.6 0.2 1 367 . 64 VAL N N 120.00 0.2 1 368 . 65 ASN HA H 4.53 0.02 1 369 . 65 ASN H H 8.96 0.02 1 370 . 65 ASN CA C 55.6 0.2 1 371 . 65 ASN CB C 37.00 0.2 1 372 . 65 ASN C C 176.6 0.2 1 373 . 65 ASN N N 121.00 0.2 1 374 . 66 TRP HA H 4.26 0.02 1 375 . 66 TRP H H 7.83 0.02 1 376 . 66 TRP CA C 62.6 0.2 1 377 . 66 TRP CB C 28.1 0.2 1 378 . 66 TRP C C 178.3 0.2 1 379 . 66 TRP N N 122.8 0.2 1 380 . 67 VAL HA H 2.91 0.02 1 381 . 67 VAL H H 8.47 0.02 1 382 . 67 VAL CA C 66.7 0.2 1 383 . 67 VAL CB C 31.2 0.2 1 384 . 67 VAL C C 178.1 0.2 1 385 . 67 VAL N N 121.7 0.2 1 386 . 68 THR HA H 4.34 0.02 1 387 . 68 THR H H 8.23 0.02 1 388 . 68 THR CA C 65.9 0.2 1 389 . 68 THR CB C 69.3 0.2 1 390 . 68 THR C C 176.8 0.2 1 391 . 68 THR N N 116.00 0.2 1 392 . 69 ASP HA H 4.36 0.02 1 393 . 69 ASP H H 8.5 0.02 1 394 . 69 ASP CA C 56.8 0.2 1 395 . 69 ASP CB C 41.00 0.2 1 396 . 69 ASP C C 177.3 0.2 1 397 . 69 ASP N N 121.1 0.2 1 398 . 70 SER HA H 4.18 0.02 1 399 . 70 SER H H 8.57 0.02 1 400 . 70 SER CA C 60.1 0.2 1 401 . 70 SER CB C 63.00 0.2 1 402 . 70 SER C C 175.00 0.2 1 403 . 70 SER N N 113.5 0.2 1 404 . 71 LEU HA H 4.22 0.02 1 405 . 71 LEU H H 6.61 0.02 1 406 . 71 LEU CA C 53.6 0.2 1 407 . 71 LEU C C 176.6 0.2 1 408 . 71 LEU N N 116.00 0.2 1 409 . 72 HIS HA H 4.49 0.02 1 410 . 72 HIS H H 6.79 0.02 1 411 . 72 HIS CA C 55.5 0.2 1 412 . 72 HIS CB C 25.7 0.2 1 413 . 72 HIS C C 173.4 0.2 1 414 . 72 HIS N N 113.8 0.2 1 415 . 73 ALA HA H 4.91 0.02 1 416 . 73 ALA H H 7.36 0.02 1 417 . 73 ALA CA C 49.6 0.2 1 418 . 73 ALA CB C 22.2 0.2 1 419 . 73 ALA C C 174.3 0.2 1 420 . 73 ALA N N 120.3 0.2 1 421 . 74 LYS HA H 4.61 0.02 1 422 . 74 LYS H H 7.68 0.02 1 423 . 74 LYS CA C 53.9 0.2 1 424 . 74 LYS CB C 34.6 0.2 1 425 . 74 LYS C C 176.5 0.2 1 426 . 74 LYS N N 120.2 0.2 1 427 . 75 VAL HA H 4.41 0.02 1 428 . 75 VAL H H 9.00 0.02 1 429 . 75 VAL CA C 62.8 0.2 1 430 . 75 VAL CB C 30.4 0.2 1 431 . 75 VAL C C 175.7 0.2 1 432 . 75 VAL N N 127.6 0.2 1 433 . 76 THR HA H 4.87 0.02 1 434 . 76 THR H H 9.24 0.02 1 435 . 76 THR CA C 61.3 0.2 1 436 . 76 THR CB C 70.8 0.2 1 437 . 76 THR C C 176.3 0.2 1 438 . 76 THR N N 118.2 0.2 1 439 . 77 THR HA H 5.41 0.02 1 440 . 77 THR H H 7.74 0.02 1 441 . 77 THR CA C 63.4 0.2 1 442 . 77 THR CB C 73.2 0.2 1 443 . 77 THR C C 171.6 0.2 1 444 . 77 THR N N 121.2 0.2 1 445 . 78 PHE HA H 6.04 0.02 1 446 . 78 PHE H H 9.2 0.02 1 447 . 78 PHE CA C 56.2 0.2 1 448 . 78 PHE CB C 43.3 0.2 1 449 . 78 PHE C C 173.00 0.2 1 450 . 78 PHE N N 128.00 0.2 1 451 . 79 ILE HA H 5.27 0.02 1 452 . 79 ILE H H 7.53 0.02 1 453 . 79 ILE CA C 57.5 0.2 1 454 . 79 ILE C C 174.7 0.2 1 455 . 79 ILE N N 127.3 0.2 1 456 . 80 PRO HA H 5.12 0.02 1 457 . 80 PRO CA C 60.4 0.2 1 458 . 80 PRO C C 176.9 0.2 1 459 . 81 ASP HA H 4.46 0.02 1 460 . 81 ASP H H 10.09 0.02 1 461 . 81 ASP CA C 58.4 0.2 1 462 . 81 ASP CB C 42.00 0.2 1 463 . 81 ASP C C 174.4 0.2 1 464 . 81 ASP N N 120.4 0.2 1 465 . 82 HIS HA H 4.66 0.02 1 466 . 82 HIS H H 7.65 0.02 1 467 . 82 HIS CA C 56.4 0.2 1 468 . 82 HIS C C 175.8 0.2 1 469 . 82 HIS N N 106.9 0.2 1 470 . 83 TRP CA C 58.4 0.2 1 471 . 83 TRP CB C 28.4 0.2 1 472 . 83 TRP C C 173.7 0.2 1 473 . 84 HIS HA H 4.21 0.02 1 474 . 84 HIS H H 5.53 0.02 1 475 . 84 HIS CA C 54.3 0.2 1 476 . 84 HIS CB C 33.2 0.2 1 477 . 84 HIS C C 177.6 0.2 1 478 . 84 HIS N N 114.3 0.2 1 479 . 85 GLY H H 9.18 0.02 1 480 . 85 GLY CA C 48.00 0.2 1 481 . 85 GLY C C 173.6 0.2 1 482 . 85 GLY N N 111.00 0.2 1 483 . 86 ASP HA H 4.43 0.02 1 484 . 86 ASP H H 8.97 0.02 1 485 . 86 ASP CA C 53.5 0.2 1 486 . 86 ASP CB C 36.9 0.2 1 487 . 86 ASP C C 171.4 0.2 1 488 . 86 ASP N N 112.5 0.2 1 489 . 87 CYS HA H 4.56 0.02 1 490 . 87 CYS H H 7.87 0.02 1 491 . 87 CYS CA C 59.3 0.2 1 492 . 87 CYS CB C 31.7 0.2 1 493 . 87 CYS C C 176.7 0.2 1 494 . 87 CYS N N 113.9 0.2 1 495 . 88 LEU HA H 4.8 0.02 1 496 . 88 LEU H H 7.5 0.02 1 497 . 88 LEU CA C 61.00 0.2 1 498 . 88 LEU CB C 41.6 0.2 1 499 . 88 LEU C C 177.4 0.2 1 500 . 88 LEU N N 112.4 0.2 1 501 . 89 GLY H H 8.27 0.02 1 502 . 89 GLY CA C 47.8 0.2 1 503 . 89 GLY C C 174.9 0.2 1 504 . 89 GLY N N 114.00 0.2 1 505 . 90 GLY HA2 H 4.44 0.02 2 506 . 90 GLY HA3 H 4.44 0.02 2 507 . 90 GLY H H 8.65 0.02 1 508 . 90 GLY CA C 43.8 0.2 1 509 . 90 GLY C C 175.4 0.2 1 510 . 90 GLY N N 108.3 0.2 1 511 . 91 LEU HA H 4.8 0.02 1 512 . 91 LEU H H 7.95 0.02 1 513 . 91 LEU CA C 56.9 0.2 1 514 . 91 LEU CB C 41.7 0.2 1 515 . 91 LEU C C 176.9 0.2 1 516 . 91 LEU N N 121.7 0.2 1 517 . 92 GLY H H 9.32 0.02 1 518 . 92 GLY CA C 47.00 0.2 1 519 . 92 GLY C C 176.3 0.2 1 520 . 92 GLY N N 109.5 0.2 1 521 . 93 TYR HA H 3.93 0.02 1 522 . 93 TYR H H 7.36 0.02 1 523 . 93 TYR CA C 61.7 0.2 1 524 . 93 TYR CB C 37.5 0.2 1 525 . 93 TYR C C 176.6 0.2 1 526 . 93 TYR N N 123.00 0.2 1 527 . 94 LEU HA H 3.49 0.02 1 528 . 94 LEU H H 7.24 0.02 1 529 . 94 LEU CA C 57.1 0.2 1 530 . 94 LEU CB C 40.1 0.2 1 531 . 94 LEU C C 179.3 0.2 1 532 . 94 LEU N N 116.4 0.2 1 533 . 95 GLN HA H 4.03 0.02 1 534 . 95 GLN H H 8.69 0.02 1 535 . 95 GLN CA C 59.3 0.2 1 536 . 95 GLN CB C 27.3 0.2 1 537 . 95 GLN C C 180.2 0.2 1 538 . 95 GLN N N 119.00 0.2 1 539 . 96 ARG HA H 4.12 0.02 1 540 . 96 ARG H H 7.76 0.02 1 541 . 96 ARG CA C 59.00 0.2 1 542 . 96 ARG CB C 29.5 0.2 1 543 . 96 ARG C C 178.00 0.2 1 544 . 96 ARG N N 121.7 0.2 1 545 . 97 LYS HA H 4.27 0.02 1 546 . 97 LYS H H 7.25 0.02 1 547 . 97 LYS CA C 54.1 0.2 1 548 . 97 LYS CB C 31.3 0.2 1 549 . 97 LYS C C 177.1 0.2 1 550 . 97 LYS N N 117.5 0.2 1 551 . 98 GLY HA2 H 3.95 0.02 2 552 . 98 GLY HA3 H 3.95 0.02 2 553 . 98 GLY H H 7.76 0.02 1 554 . 98 GLY CA C 45.8 0.2 1 555 . 98 GLY C C 174.4 0.2 1 556 . 98 GLY N N 108.9 0.2 1 557 . 99 VAL HA H 3.69 0.02 1 558 . 99 VAL H H 7.6 0.02 1 559 . 99 VAL CA C 63.1 0.2 1 560 . 99 VAL CB C 32.2 0.2 1 561 . 99 VAL C C 175.6 0.2 1 562 . 99 VAL N N 122.1 0.2 1 563 . 100 GLN HA H 4.76 0.02 1 564 . 100 GLN H H 8.15 0.02 1 565 . 100 GLN CA C 55.7 0.2 1 566 . 100 GLN CB C 30.4 0.2 1 567 . 100 GLN C C 174.7 0.2 1 568 . 100 GLN N N 128.3 0.2 1 569 . 101 SER HA H 6.14 0.02 1 570 . 101 SER H H 8.3 0.02 1 571 . 101 SER CA C 56.00 0.2 1 572 . 101 SER CB C 67.4 0.2 1 573 . 101 SER C C 172.2 0.2 1 574 . 101 SER N N 116.6 0.2 1 575 . 102 TYR HA H 5.71 0.02 1 576 . 102 TYR H H 8.68 0.02 1 577 . 102 TYR CA C 55.6 0.2 1 578 . 102 TYR CB C 41.8 0.2 1 579 . 102 TYR C C 174.2 0.2 1 580 . 102 TYR N N 122.7 0.2 1 581 . 103 ALA HA H 4.68 0.02 1 582 . 103 ALA H H 9.03 0.02 1 583 . 103 ALA CA C 50.4 0.2 1 584 . 103 ALA CB C 24.00 0.2 1 585 . 103 ALA C C 174.3 0.2 1 586 . 103 ALA N N 118.1 0.2 1 587 . 104 ASN HA H 3.2 0.02 1 588 . 104 ASN H H 8.6 0.02 1 589 . 104 ASN CA C 51.9 0.2 1 590 . 104 ASN CB C 36.2 0.2 1 591 . 104 ASN C C 177.9 0.2 1 592 . 104 ASN N N 118.9 0.2 1 593 . 105 GLN HA H 4.08 0.02 1 594 . 105 GLN H H 9.57 0.02 1 595 . 105 GLN CA C 58.1 0.2 1 596 . 105 GLN CB C 27.6 0.2 1 597 . 105 GLN C C 177.1 0.2 1 598 . 105 GLN N N 133.2 0.2 1 599 . 106 MET HA H 4.38 0.02 1 600 . 106 MET H H 7.45 0.02 1 601 . 106 MET CA C 58.3 0.2 1 602 . 106 MET CB C 35.0 0.2 1 603 . 106 MET C C 178.4 0.2 1 604 . 106 MET N N 113.6 0.2 1 605 . 107 THR HA H 4.06 0.02 1 606 . 107 THR H H 7.15 0.02 1 607 . 107 THR CA C 65.7 0.2 1 608 . 107 THR C C 175.9 0.2 1 609 . 107 THR N N 117.1 0.2 1 610 . 108 ILE HA H 3.25 0.02 1 611 . 108 ILE H H 7.28 0.02 1 612 . 108 ILE CA C 66.6 0.2 1 613 . 108 ILE C C 176.5 0.2 1 614 . 108 ILE N N 122.5 0.2 1 615 . 109 ASP HA H 5.29 0.02 1 616 . 109 ASP CA C 57.6 0.2 1 617 . 109 ASP CB C 42.3 0.2 1 618 . 109 ASP C C 179.7 0.2 1 619 . 110 LEU HA H 4.18 0.02 1 620 . 110 LEU H H 7.69 0.02 1 621 . 110 LEU CA C 58.00 0.2 1 622 . 110 LEU CB C 41.5 0.2 1 623 . 110 LEU C C 177.9 0.2 1 624 . 110 LEU N N 122.6 0.2 1 625 . 111 ALA HA H 4.67 0.02 1 626 . 111 ALA H H 8.54 0.02 1 627 . 111 ALA CA C 55.7 0.2 1 628 . 111 ALA CB C 22.8 0.2 1 629 . 111 ALA C C 179.7 0.2 1 630 . 111 ALA N N 122.5 0.2 1 631 . 112 LYS HA H 3.88 0.02 1 632 . 112 LYS H H 8.61 0.02 1 633 . 112 LYS CA C 59.5 0.2 1 634 . 112 LYS CB C 32.3 0.2 1 635 . 112 LYS C C 180.3 0.2 1 636 . 112 LYS N N 117.2 0.2 1 637 . 113 GLU HA H 4.01 0.02 1 638 . 113 GLU H H 7.72 0.02 1 639 . 113 GLU CA C 58.8 0.2 1 640 . 113 GLU CB C 29.7 0.2 1 641 . 113 GLU C C 178.2 0.2 1 642 . 113 GLU N N 120.5 0.2 1 643 . 114 LYS HA H 4.25 0.02 1 644 . 114 LYS H H 7.8 0.02 1 645 . 114 LYS CA C 55.9 0.2 1 646 . 114 LYS CB C 33.7 0.2 1 647 . 114 LYS C C 176.7 0.2 1 648 . 114 LYS N N 116.7 0.2 1 649 . 115 GLY HA2 H 4.02 0.02 2 650 . 115 GLY HA3 H 4.02 0.02 2 651 . 115 GLY H H 7.76 0.02 1 652 . 115 GLY CA C 46.4 0.2 1 653 . 115 GLY C C 174.7 0.2 1 654 . 115 GLY N N 109.6 0.2 1 655 . 116 LEU HA H 4.67 0.02 1 656 . 116 LEU H H 8.17 0.02 1 657 . 116 LEU CA C 52.7 0.2 1 658 . 116 LEU C C 173.00 0.2 1 659 . 116 LEU N N 123.4 0.2 1 660 . 120 GLU HA H 3.86 0.02 1 661 . 120 GLU CA C 59.4 0.2 1 662 . 120 GLU CB C 30.7 0.2 1 663 . 120 GLU C C 176.4 0.2 1 664 . 121 HIS HA H 4.97 0.02 1 665 . 121 HIS H H 7.72 0.02 1 666 . 121 HIS CA C 54.8 0.2 1 667 . 121 HIS CB C 31.7 0.2 1 668 . 121 HIS C C 174.00 0.2 1 669 . 121 HIS N N 116.9 0.2 1 670 . 122 GLY HA2 H 5.69 0.02 2 671 . 122 GLY HA3 H 5.69 0.02 2 672 . 122 GLY H H 8.74 0.02 1 673 . 122 GLY CA C 44.1 0.2 1 674 . 122 GLY C C 174.1 0.2 1 675 . 122 GLY N N 112.00 0.2 1 676 . 123 PHE HA H 5.33 0.02 1 677 . 123 PHE H H 7.74 0.02 1 678 . 123 PHE CA C 55.6 0.2 1 679 . 123 PHE C C 173.3 0.2 1 680 . 123 PHE N N 116.2 0.2 1 681 . 124 THR HA H 4.2 0.02 1 682 . 124 THR H H 8.75 0.02 1 683 . 124 THR CA C 61.5 0.2 1 684 . 124 THR CB C 70.4 0.2 1 685 . 124 THR C C 173.3 0.2 1 686 . 124 THR N N 113.2 0.2 1 687 . 125 ASP HA H 5.2 0.02 1 688 . 125 ASP H H 9.06 0.02 1 689 . 125 ASP CA C 57.5 0.2 1 690 . 125 ASP CB C 41.8 0.2 1 691 . 125 ASP C C 175.00 0.2 1 692 . 125 ASP N N 122.5 0.2 1 693 . 126 SER HA H 4.99 0.02 1 694 . 126 SER H H 8.94 0.02 1 695 . 126 SER CA C 57.00 0.2 1 696 . 126 SER CB C 66.1 0.2 1 697 . 126 SER C C 172.00 0.2 1 698 . 126 SER N N 115.9 0.2 1 699 . 127 LEU HA H 4.25 0.02 1 700 . 127 LEU H H 7.7 0.02 1 701 . 127 LEU CA C 54.8 0.2 1 702 . 127 LEU CB C 45.8 0.2 1 703 . 127 LEU C C 174.7 0.2 1 704 . 127 LEU N N 121.8 0.2 1 705 . 128 THR HA H 4.85 0.02 1 706 . 128 THR H H 8.79 0.02 1 707 . 128 THR CA C 62.00 0.2 1 708 . 128 THR CB C 69.00 0.2 1 709 . 128 THR C C 173.5 0.2 1 710 . 128 THR N N 125.5 0.2 1 711 . 129 VAL HA H 3.78 0.02 1 712 . 129 VAL H H 8.94 0.02 1 713 . 129 VAL CA C 60.7 0.2 1 714 . 129 VAL CB C 33.1 0.2 1 715 . 129 VAL C C 173.7 0.2 1 716 . 129 VAL N N 131.1 0.2 1 717 . 130 SER HA H 4.61 0.02 1 718 . 130 SER H H 8.54 0.02 1 719 . 130 SER CA C 55.8 0.2 1 720 . 130 SER CB C 63.8 0.2 1 721 . 130 SER C C 174.1 0.2 1 722 . 130 SER N N 120.8 0.2 1 723 . 131 LEU HA H 4.64 0.02 1 724 . 131 LEU H H 9.29 0.02 1 725 . 131 LEU CA C 52.3 0.2 1 726 . 131 LEU CB C 42.1 0.2 1 727 . 131 LEU C C 174.9 0.2 1 728 . 131 LEU N N 133.0 0.2 1 729 . 132 ASP HA H 4.29 0.02 1 730 . 132 ASP H H 8.91 0.02 1 731 . 132 ASP CA C 54.8 0.2 1 732 . 132 ASP CB C 40.9 0.2 1 733 . 132 ASP C C 174.2 0.2 1 734 . 132 ASP N N 128.1 0.2 1 735 . 133 GLY HA2 H 3.84 0.02 2 736 . 133 GLY HA3 H 3.84 0.02 2 737 . 133 GLY H H 7.24 0.02 1 738 . 133 GLY CA C 44.6 0.2 1 739 . 133 GLY C C 174.00 0.2 1 740 . 133 GLY N N 102.7 0.2 1 741 . 134 MET HA H 4.84 0.02 1 742 . 134 MET H H 7.34 0.02 1 743 . 134 MET CA C 52.4 0.2 1 744 . 134 MET C C 174.8 0.2 1 745 . 134 MET N N 123.6 0.2 1 746 . 135 PRO HA H 4.59 0.02 1 747 . 135 PRO CA C 63.00 0.2 1 748 . 135 PRO CB C 32.7 0.2 1 749 . 135 PRO C C 176.00 0.2 1 750 . 136 LEU HA H 4.65 0.02 1 751 . 136 LEU H H 8.96 0.02 1 752 . 136 LEU CA C 54.6 0.2 1 753 . 136 LEU CB C 41.5 0.2 1 754 . 136 LEU C C 175.5 0.2 1 755 . 136 LEU N N 124.1 0.2 1 756 . 137 GLN HA H 4.79 0.02 1 757 . 137 GLN H H 9.02 0.02 1 758 . 137 GLN CA C 55.7 0.2 1 759 . 137 GLN CB C 29.8 0.2 1 760 . 137 GLN C C 173.9 0.2 1 761 . 137 GLN N N 121.7 0.2 1 762 . 138 CYS HA H 5.18 0.02 1 763 . 138 CYS H H 8.86 0.02 1 764 . 138 CYS CA C 56.9 0.2 1 765 . 138 CYS CB C 30.00 0.2 1 766 . 138 CYS C C 174.8 0.2 1 767 . 138 CYS N N 124.2 0.2 1 768 . 139 TYR HA H 4.41 0.02 1 769 . 139 TYR H H 8.91 0.02 1 770 . 139 TYR CA C 57.8 0.2 1 771 . 139 TYR CB C 42.8 0.2 1 772 . 139 TYR C C 174.4 0.2 1 773 . 139 TYR N N 118.5 0.2 1 774 . 140 TYR HA H 5.16 0.02 1 775 . 140 TYR H H 9.21 0.02 1 776 . 140 TYR CA C 57.7 0.2 1 777 . 140 TYR CB C 38.7 0.2 1 778 . 140 TYR C C 174.9 0.2 1 779 . 140 TYR N N 121.6 0.2 1 780 . 141 LEU HA H 4.52 0.02 1 781 . 141 LEU H H 9.62 0.02 1 782 . 141 LEU CA C 53.4 0.2 1 783 . 141 LEU C C 173.8 0.2 1 784 . 141 LEU N N 130.6 0.2 1 785 . 142 GLY H H 5.1 0.02 1 786 . 142 GLY CA C 43.6 0.2 1 787 . 142 GLY C C 174.00 0.2 1 788 . 142 GLY N N 130.8 0.2 1 789 . 143 GLY H H 8.44 0.02 1 790 . 143 GLY CA C 44.9 0.2 1 791 . 143 GLY C C 173.5 0.2 1 792 . 143 GLY N N 104.1 0.2 1 793 . 144 GLY H H 7.08 0.02 1 794 . 144 GLY CA C 46.6 0.2 1 795 . 144 GLY C C 171.9 0.2 1 796 . 144 GLY N N 106.8 0.2 1 797 . 145 HIS HA H 2.82 0.02 1 798 . 145 HIS H H 5.79 0.02 1 799 . 145 HIS CA C 58.00 0.2 1 800 . 145 HIS CB C 23.7 0.2 1 801 . 145 HIS C C 171.4 0.2 1 802 . 145 HIS N N 131.4 0.2 1 803 . 146 ALA HA H 4.61 0.02 1 804 . 146 ALA H H 7.35 0.02 1 805 . 146 ALA CA C 49.00 0.2 1 806 . 146 ALA CB C 17.2 0.2 1 807 . 146 ALA C C 179.4 0.2 1 808 . 146 ALA N N 115.00 0.2 1 809 . 147 THR HA H 3.91 0.02 1 810 . 147 THR H H 8.49 0.02 1 811 . 147 THR CA C 65.5 0.2 1 812 . 147 THR CB C 68.00 0.2 1 813 . 147 THR C C 173.6 0.2 1 814 . 147 THR N N 117.1 0.2 1 815 . 148 ASP HA H 4.46 0.02 1 816 . 148 ASP H H 10.57 0.02 1 817 . 148 ASP CA C 52.8 0.2 1 818 . 148 ASP CB C 40.6 0.2 1 819 . 148 ASP C C 176.1 0.2 1 820 . 148 ASP N N 115.7 0.2 1 821 . 149 ASN HA H 4.85 0.02 1 822 . 149 ASN H H 6.94 0.02 1 823 . 149 ASN CA C 53.9 0.2 1 824 . 149 ASN C C 176.2 0.2 1 825 . 149 ASN N N 116.3 0.2 1 826 . 150 ILE HA H 5.35 0.02 1 827 . 150 ILE CA C 60.1 0.2 1 828 . 150 ILE CB C 41.9 0.2 1 829 . 150 ILE C C 173.4 0.2 1 830 . 151 VAL HA H 4.91 0.02 1 831 . 151 VAL H H 8.54 0.02 1 832 . 151 VAL CA C 60.1 0.2 1 833 . 151 VAL CB C 34.5 0.2 1 834 . 151 VAL C C 175.3 0.2 1 835 . 151 VAL N N 105.8 0.2 1 836 . 152 VAL HA H 5.11 0.02 1 837 . 152 VAL H H 8.13 0.02 1 838 . 152 VAL CA C 61.5 0.2 1 839 . 152 VAL CB C 34.7 0.2 1 840 . 152 VAL C C 172.9 0.2 1 841 . 152 VAL N N 119.1 0.2 1 842 . 153 TRP HA H 5.41 0.02 1 843 . 153 TRP H H 10.12 0.02 1 844 . 153 TRP CA C 53.6 0.2 1 845 . 153 TRP CB C 35.2 0.2 1 846 . 153 TRP C C 173.8 0.2 1 847 . 153 TRP N N 131.00 0.2 1 848 . 154 LEU HA H 5.07 0.02 1 849 . 154 LEU H H 7.86 0.02 1 850 . 154 LEU CA C 50.5 0.2 1 851 . 154 LEU C C 175.2 0.2 1 852 . 154 LEU N N 127.3 0.2 1 853 . 155 PRO HA H 3.42 0.02 1 854 . 155 PRO CA C 64.2 0.2 1 855 . 155 PRO CB C 32.8 0.2 1 856 . 155 PRO C C 179.1 0.2 1 857 . 156 THR HA H 4.17 0.02 1 858 . 156 THR H H 8.43 0.02 1 859 . 156 THR CA C 64.00 0.2 1 860 . 156 THR CB C 67.7 0.2 1 861 . 156 THR C C 174.9 0.2 1 862 . 156 THR N N 107.8 0.2 1 863 . 157 GLU HA H 4.37 0.02 1 864 . 157 GLU H H 6.81 0.02 1 865 . 157 GLU CA C 53.7 0.2 1 866 . 157 GLU CB C 31.8 0.2 1 867 . 157 GLU C C 175.4 0.2 1 868 . 157 GLU N N 116.9 0.2 1 869 . 158 ASN HA H 3.84 0.02 1 870 . 158 ASN H H 7.62 0.02 1 871 . 158 ASN CA C 55.00 0.2 1 872 . 158 ASN CB C 37.3 0.2 1 873 . 158 ASN C C 174.2 0.2 1 874 . 158 ASN N N 114.2 0.2 1 875 . 159 ILE HA H 4.9 0.02 1 876 . 159 ILE H H 6.32 0.02 1 877 . 159 ILE CA C 60.7 0.2 1 878 . 159 ILE CB C 42.4 0.2 1 879 . 159 ILE C C 171.4 0.2 1 880 . 159 ILE N N 115.9 0.2 1 881 . 160 LEU HA H 5.29 0.02 1 882 . 160 LEU H H 8.78 0.02 1 883 . 160 LEU CA C 52.7 0.2 1 884 . 160 LEU CB C 46.8 0.2 1 885 . 160 LEU C C 175.00 0.2 1 886 . 160 LEU N N 129.1 0.2 1 887 . 161 PHE HA H 5.32 0.02 1 888 . 161 PHE H H 9.89 0.02 1 889 . 161 PHE CA C 55.2 0.2 1 890 . 161 PHE CB C 37.7 0.2 1 891 . 161 PHE C C 174.5 0.2 1 892 . 161 PHE N N 129.4 0.2 1 893 . 162 GLY H H 8.28 0.02 1 894 . 162 GLY CA C 44.5 0.2 1 895 . 162 GLY C C 172.3 0.2 1 896 . 162 GLY N N 113.3 0.2 1 897 . 163 GLY HA2 H 3.28 0.02 2 898 . 163 GLY HA3 H 3.28 0.02 2 899 . 163 GLY H H 6.38 0.02 1 900 . 163 GLY CA C 46.00 0.2 1 901 . 163 GLY C C 176.6 0.2 1 902 . 163 GLY N N 101.5 0.2 1 903 . 164 CYS HA H 4.09 0.02 1 904 . 164 CYS H H 6.49 0.02 1 905 . 164 CYS CA C 62.4 0.2 1 906 . 164 CYS C C 174.8 0.2 1 907 . 164 CYS N N 120.6 0.2 1 908 . 165 MET HA H 4.19 0.02 1 909 . 165 MET H H 9.7 0.02 1 910 . 165 MET CA C 57.6 0.2 1 911 . 165 MET CB C 32.6 0.2 1 912 . 165 MET C C 174.5 0.2 1 913 . 165 MET N N 118.5 0.2 1 914 . 166 LEU HA H 4.92 0.02 1 915 . 166 LEU H H 8.26 0.02 1 916 . 166 LEU CA C 52.4 0.2 1 917 . 166 LEU CB C 43.2 0.2 1 918 . 166 LEU C C 174.8 0.2 1 919 . 166 LEU N N 118.6 0.2 1 920 . 167 LYS HA H 4.84 0.02 1 921 . 167 LYS H H 8.9 0.02 1 922 . 167 LYS CA C 52.2 0.2 1 923 . 167 LYS CB C 33.2 0.2 1 924 . 167 LYS C C 174.2 0.2 1 925 . 167 LYS N N 121.7 0.2 1 926 . 168 ASP HA H 4.56 0.02 1 927 . 168 ASP H H 8.17 0.02 1 928 . 168 ASP CA C 52.7 0.2 1 929 . 168 ASP CB C 41.9 0.2 1 930 . 168 ASP C C 176.3 0.2 1 931 . 168 ASP N N 116.9 0.2 1 932 . 169 ASN HA H 3.85 0.02 1 933 . 169 ASN H H 8.82 0.02 1 934 . 169 ASN CA C 55.2 0.2 1 935 . 169 ASN CB C 38.7 0.2 1 936 . 169 ASN C C 176.2 0.2 1 937 . 169 ASN N N 116.1 0.2 1 938 . 170 GLN HA H 4.29 0.02 1 939 . 170 GLN H H 8.08 0.02 1 940 . 170 GLN CA C 55.6 0.2 1 941 . 170 GLN CB C 29.2 0.2 1 942 . 170 GLN C C 176.3 0.2 1 943 . 170 GLN N N 116.2 0.2 1 944 . 171 ALA HA H 4.38 0.02 1 945 . 171 ALA H H 7.65 0.02 1 946 . 171 ALA CA C 53.3 0.2 1 947 . 171 ALA C C 178.6 0.2 1 948 . 171 ALA N N 125.5 0.2 1 949 . 172 THR HA H 4.57 0.02 1 950 . 172 THR CA C 60.9 0.2 1 951 . 172 THR CB C 70.4 0.2 1 952 . 172 THR C C 174.1 0.2 1 953 . 173 SER HA H 5.03 0.02 1 954 . 173 SER H H 7.71 0.02 1 955 . 173 SER CA C 56.00 0.2 1 956 . 173 SER CB C 65.5 0.2 1 957 . 173 SER C C 174.4 0.2 1 958 . 173 SER N N 115.8 0.2 1 959 . 174 ILE HA H 3.62 0.02 1 960 . 174 ILE H H 9.03 0.02 1 961 . 174 ILE CA C 63.7 0.2 1 962 . 174 ILE CB C 39.8 0.2 1 963 . 174 ILE C C 175.6 0.2 1 964 . 174 ILE N N 124.8 0.2 1 965 . 175 GLY HA2 H 4.84 0.02 2 966 . 175 GLY HA3 H 4.84 0.02 2 967 . 175 GLY H H 8.12 0.02 1 968 . 175 GLY CA C 45.00 0.2 1 969 . 175 GLY C C 173.7 0.2 1 970 . 175 GLY N N 111.8 0.2 1 971 . 176 ASN H H 8.03 0.02 1 972 . 176 ASN CA C 53.8 0.2 1 973 . 176 ASN CB C 40.5 0.2 1 974 . 176 ASN C C 174.3 0.2 1 975 . 176 ASN N N 124.9 0.2 1 976 . 177 ILE HA H 4.65 0.02 1 977 . 177 ILE H H 8.09 0.02 1 978 . 177 ILE CA C 60.2 0.2 1 979 . 177 ILE CB C 38.3 0.2 1 980 . 177 ILE C C 177.6 0.2 1 981 . 177 ILE N N 119.5 0.2 1 982 . 178 SER H H 8.37 0.02 1 983 . 178 SER CA C 52.5 0.2 1 984 . 178 SER C C 174.5 0.2 1 985 . 178 SER N N 120.4 0.2 1 986 . 179 ASP HA H 4.78 0.02 1 987 . 179 ASP H H 8.1 0.02 1 988 . 179 ASP CA C 53.4 0.2 1 989 . 179 ASP CB C 43.4 0.2 1 990 . 179 ASP C C 174.00 0.2 1 991 . 179 ASP N N 119.4 0.2 1 992 . 180 ALA HA H 3.85 0.02 1 993 . 180 ALA H H 6.97 0.02 1 994 . 180 ALA CA C 51.9 0.2 1 995 . 180 ALA CB C 21.3 0.2 1 996 . 180 ALA C C 177.9 0.2 1 997 . 180 ALA N N 120.6 0.2 1 998 . 181 ASP HA H 4.91 0.02 1 999 . 181 ASP H H 8.17 0.02 1 1000 . 181 ASP CA C 51.6 0.2 1 1001 . 181 ASP CB C 41.00 0.2 1 1002 . 181 ASP C C 176.1 0.2 1 1003 . 181 ASP N N 120.2 0.2 1 1004 . 182 VAL HA H 3.94 0.02 1 1005 . 182 VAL H H 8.67 0.02 1 1006 . 182 VAL CA C 67.4 0.2 1 1007 . 182 VAL CB C 31.5 0.2 1 1008 . 182 VAL C C 175.9 0.2 1 1009 . 182 VAL N N 121.7 0.2 1 1010 . 183 THR HA H 4.1 0.02 1 1011 . 183 THR H H 7.97 0.02 1 1012 . 183 THR CA C 65.1 0.2 1 1013 . 183 THR CB C 68.5 0.2 1 1014 . 183 THR C C 176.8 0.2 1 1015 . 183 THR N N 110.1 0.2 1 1016 . 184 ALA HA H 4.32 0.02 1 1017 . 184 ALA H H 7.45 0.02 1 1018 . 184 ALA CA C 53.5 0.2 1 1019 . 184 ALA CB C 19.6 0.2 1 1020 . 184 ALA C C 178.6 0.2 1 1021 . 184 ALA N N 122.9 0.2 1 1022 . 185 TRP HA H 5.04 0.02 1 1023 . 185 TRP H H 7.88 0.02 1 1024 . 185 TRP CA C 60.4 0.2 1 1025 . 185 TRP C C 174.6 0.2 1 1026 . 185 TRP N N 119.9 0.2 1 1027 . 186 PRO CA C 67.1 0.2 1 1028 . 186 PRO CB C 31.1 0.2 1 1029 . 186 PRO C C 178.2 0.2 1 1030 . 187 LYS HA H 4.24 0.02 1 1031 . 187 LYS H H 7.1 0.02 1 1032 . 187 LYS CA C 58.8 0.2 1 1033 . 187 LYS CB C 31.5 0.2 1 1034 . 187 LYS C C 180.4 0.2 1 1035 . 187 LYS N N 117.5 0.2 1 1036 . 188 THR HA H 3.72 0.02 1 1037 . 188 THR H H 9.08 0.02 1 1038 . 188 THR CA C 66.2 0.2 1 1039 . 188 THR C C 176.8 0.2 1 1040 . 188 THR N N 122.3 0.2 1 1041 . 189 LEU HA H 4.21 0.02 1 1042 . 189 LEU H H 8.39 0.02 1 1043 . 189 LEU CA C 58.1 0.2 1 1044 . 189 LEU CB C 40.6 0.2 1 1045 . 189 LEU C C 178.6 0.2 1 1046 . 189 LEU N N 120.00 0.2 1 1047 . 190 ASP HA H 4.5 0.02 1 1048 . 190 ASP H H 7.84 0.02 1 1049 . 190 ASP CA C 57.5 0.2 1 1050 . 190 ASP CB C 39.6 0.2 1 1051 . 190 ASP C C 179.7 0.2 1 1052 . 190 ASP N N 120.4 0.2 1 1053 . 191 LYS HA H 4.03 0.02 1 1054 . 191 LYS H H 7.84 0.02 1 1055 . 191 LYS CA C 59.8 0.2 1 1056 . 191 LYS CB C 33.00 0.2 1 1057 . 191 LYS C C 179.1 0.2 1 1058 . 191 LYS N N 122.3 0.2 1 1059 . 192 VAL HA H 3.38 0.02 1 1060 . 192 VAL H H 8.28 0.02 1 1061 . 192 VAL CA C 66.5 0.2 1 1062 . 192 VAL CB C 31.6 0.2 1 1063 . 192 VAL C C 177.00 0.2 1 1064 . 192 VAL N N 121.8 0.2 1 1065 . 193 LYS HA H 3.91 0.02 1 1066 . 193 LYS H H 8.4 0.02 1 1067 . 193 LYS CA C 58.6 0.2 1 1068 . 193 LYS CB C 32.8 0.2 1 1069 . 193 LYS C C 178.8 0.2 1 1070 . 193 LYS N N 119.00 0.2 1 1071 . 194 ALA HA H 3.99 0.02 1 1072 . 194 ALA H H 7.5 0.02 1 1073 . 194 ALA CA C 53.5 0.2 1 1074 . 194 ALA CB C 18.4 0.2 1 1075 . 194 ALA C C 178.9 0.2 1 1076 . 194 ALA N N 117.5 0.2 1 1077 . 195 LYS HA H 3.59 0.02 1 1078 . 195 LYS H H 7.43 0.02 1 1079 . 195 LYS CA C 57.3 0.2 1 1080 . 195 LYS CB C 32.2 0.2 1 1081 . 195 LYS C C 176.00 0.2 1 1082 . 195 LYS N N 117.3 0.2 1 1083 . 196 PHE HA H 4.82 0.02 1 1084 . 196 PHE H H 6.74 0.02 1 1085 . 196 PHE CA C 53.2 0.2 1 1086 . 196 PHE C C 173.9 0.2 1 1087 . 196 PHE N N 114.1 0.2 1 1088 . 197 PRO HA H 4.55 0.02 1 1089 . 197 PRO CA C 64.6 0.2 1 1090 . 197 PRO CB C 31.5 0.2 1 1091 . 197 PRO C C 177.9 0.2 1 1092 . 198 SER HA H 4.66 0.02 1 1093 . 198 SER H H 8.15 0.02 1 1094 . 198 SER CA C 57.7 0.2 1 1095 . 198 SER CB C 63.9 0.2 1 1096 . 198 SER C C 174.2 0.2 1 1097 . 198 SER N N 113.3 0.2 1 1098 . 199 ALA HA H 4.25 0.02 1 1099 . 199 ALA H H 7.26 0.02 1 1100 . 199 ALA CA C 53.8 0.2 1 1101 . 199 ALA CB C 18.9 0.2 1 1102 . 199 ALA C C 176.00 0.2 1 1103 . 199 ALA N N 124.1 0.2 1 1104 . 200 ARG HA H 4.35 0.02 1 1105 . 200 ARG H H 9.46 0.02 1 1106 . 200 ARG CA C 57.1 0.2 1 1107 . 200 ARG CB C 31.1 0.2 1 1108 . 200 ARG C C 176.00 0.2 1 1109 . 200 ARG N N 125.5 0.2 1 1110 . 201 TYR HA H 5.64 0.02 1 1111 . 201 TYR H H 7.08 0.02 1 1112 . 201 TYR CA C 55.8 0.2 1 1113 . 201 TYR CB C 42.4 0.2 1 1114 . 201 TYR C C 174.1 0.2 1 1115 . 201 TYR N N 111.9 0.2 1 1116 . 202 VAL HA H 4.92 0.02 1 1117 . 202 VAL H H 9.68 0.02 1 1118 . 202 VAL CA C 61.2 0.2 1 1119 . 202 VAL CB C 33.2 0.2 1 1120 . 202 VAL C C 174.1 0.2 1 1121 . 202 VAL N N 124.4 0.2 1 1122 . 203 VAL HA H 4.85 0.02 1 1123 . 203 VAL H H 8.91 0.02 1 1124 . 203 VAL CA C 58.5 0.2 1 1125 . 203 VAL N N 127.5 0.2 1 1126 . 204 PRO HA H 4.78 0.02 1 1127 . 204 PRO CA C 61.5 0.2 1 1128 . 204 PRO CB C 33.2 0.2 1 1129 . 204 PRO C C 175.6 0.2 1 1130 . 205 GLY H H 6.64 0.02 1 1131 . 205 GLY CA C 47.9 0.2 1 1132 . 205 GLY C C 173.4 0.2 1 1133 . 205 GLY N N 106.1 0.2 1 1134 . 206 HIS HA H 4.39 0.02 1 1135 . 206 HIS H H 7.86 0.02 1 1136 . 206 HIS CA C 55.5 0.2 1 1137 . 206 HIS CB C 31.00 0.2 1 1138 . 206 HIS C C 174.2 0.2 1 1139 . 206 HIS N N 119.1 0.2 1 1140 . 207 GLY HA2 H 4.59 0.02 2 1141 . 207 GLY HA3 H 4.59 0.02 2 1142 . 207 GLY H H 9.74 0.02 1 1143 . 207 GLY CA C 43.5 0.2 1 1144 . 207 GLY C C 174.4 0.2 1 1145 . 207 GLY N N 113.2 0.2 1 1146 . 208 ASP HA H 4.4 0.02 1 1147 . 208 ASP H H 9.1 0.02 1 1148 . 208 ASP CA C 55.2 0.2 1 1149 . 208 ASP CB C 41.00 0.2 1 1150 . 208 ASP C C 176.6 0.2 1 1151 . 208 ASP N N 120.7 0.2 1 1152 . 209 TYR HA H 4.82 0.02 1 1153 . 209 TYR H H 7.13 0.02 1 1154 . 209 TYR CA C 56.1 0.2 1 1155 . 209 TYR CB C 39.6 0.2 1 1156 . 209 TYR C C 174.4 0.2 1 1157 . 209 TYR N N 116.8 0.2 1 1158 . 210 GLY H H 8.36 0.02 1 1159 . 210 GLY CA C 46.3 0.2 1 1160 . 210 GLY C C 172.4 0.2 1 1161 . 210 GLY N N 110.3 0.2 1 1162 . 211 GLY H H 9.55 0.02 1 1163 . 211 GLY CA C 44.6 0.2 1 1164 . 211 GLY C C 175.8 0.2 1 1165 . 211 GLY N N 118.00 0.2 1 1166 . 212 THR HA H 3.83 0.02 1 1167 . 212 THR H H 8.94 0.02 1 1168 . 212 THR CA C 65.1 0.2 1 1169 . 212 THR CB C 68.6 0.2 1 1170 . 212 THR C C 177.1 0.2 1 1171 . 212 THR N N 110.3 0.2 1 1172 . 213 GLU HA H 4.52 0.02 1 1173 . 213 GLU H H 10.16 0.02 1 1174 . 213 GLU CA C 59.2 0.2 1 1175 . 213 GLU CB C 26.5 0.2 1 1176 . 213 GLU C C 177.7 0.2 1 1177 . 213 GLU N N 127.8 0.2 1 1178 . 214 LEU HA H 4.38 0.02 1 1179 . 214 LEU H H 8.03 0.02 1 1180 . 214 LEU CA C 58.8 0.2 1 1181 . 214 LEU C C 180.8 0.2 1 1182 . 214 LEU N N 122.6 0.2 1 1183 . 215 ILE HA H 3.63 0.02 1 1184 . 215 ILE H H 8.2 0.02 1 1185 . 215 ILE CA C 66.3 0.2 1 1186 . 215 ILE C C 176.9 0.2 1 1187 . 215 ILE N N 122.2 0.2 1 1188 . 216 GLU HA H 4.15 0.02 1 1189 . 216 GLU H H 7.32 0.02 1 1190 . 216 GLU CA C 58.8 0.2 1 1191 . 216 GLU CB C 29.00 0.2 1 1192 . 216 GLU C C 178.7 0.2 1 1193 . 216 GLU N N 119.7 0.2 1 1194 . 217 HIS HA H 4.44 0.02 1 1195 . 217 HIS H H 8.48 0.02 1 1196 . 217 HIS CA C 59.3 0.2 1 1197 . 217 HIS CB C 29.1 0.2 1 1198 . 217 HIS C C 176.9 0.2 1 1199 . 217 HIS N N 118.6 0.2 1 1200 . 218 THR HA H 4.36 0.02 1 1201 . 218 THR H H 7.99 0.02 1 1202 . 218 THR CA C 68.1 0.2 1 1203 . 218 THR C C 175.1 0.2 1 1204 . 218 THR N N 114.7 0.2 1 1205 . 219 LYS HA H 3.35 0.02 1 1206 . 219 LYS H H 8.19 0.02 1 1207 . 219 LYS CA C 61.00 0.2 1 1208 . 219 LYS CB C 31.7 0.2 1 1209 . 219 LYS C C 177.2 0.2 1 1210 . 219 LYS N N 122.9 0.2 1 1211 . 220 GLN HA H 4.04 0.02 1 1212 . 220 GLN H H 7.84 0.02 1 1213 . 220 GLN CA C 59.00 0.2 1 1214 . 220 GLN CB C 27.4 0.2 1 1215 . 220 GLN C C 178.6 0.2 1 1216 . 220 GLN N N 117.9 0.2 1 1217 . 221 ILE HA H 3.58 0.02 1 1218 . 221 ILE H H 7.4 0.02 1 1219 . 221 ILE CA C 64.4 0.2 1 1220 . 221 ILE CB C 37.6 0.2 1 1221 . 221 ILE C C 178.9 0.2 1 1222 . 221 ILE N N 120.4 0.2 1 1223 . 222 VAL HA H 3.29 0.02 1 1224 . 222 VAL H H 8.17 0.02 1 1225 . 222 VAL CA C 66.4 0.2 1 1226 . 222 VAL CB C 30.9 0.2 1 1227 . 222 VAL C C 177.6 0.2 1 1228 . 222 VAL N N 122.00 0.2 1 1229 . 223 ASN HA H 4.56 0.02 1 1230 . 223 ASN H H 8.82 0.02 1 1231 . 223 ASN CA C 55.8 0.2 1 1232 . 223 ASN CB C 37.2 0.2 1 1233 . 223 ASN C C 178.6 0.2 1 1234 . 223 ASN N N 119.2 0.2 1 1235 . 224 GLN HA H 4.11 0.02 1 1236 . 224 GLN H H 8.29 0.02 1 1237 . 224 GLN CA C 59.2 0.2 1 1238 . 224 GLN CB C 27.8 0.2 1 1239 . 224 GLN C C 178.7 0.2 1 1240 . 224 GLN N N 120.9 0.2 1 1241 . 225 TYR HA H 4.2 0.02 1 1242 . 225 TYR H H 7.93 0.02 1 1243 . 225 TYR CA C 61.8 0.2 1 1244 . 225 TYR CB C 38.00 0.2 1 1245 . 225 TYR C C 175.6 0.2 1 1246 . 225 TYR N N 123.00 0.2 1 1247 . 226 ILE HA H 4.19 0.02 1 1248 . 226 ILE H H 8.62 0.02 1 1249 . 226 ILE CA C 65.9 0.2 1 1250 . 226 ILE CB C 38.04 0.2 1 1251 . 226 ILE C C 179.3 0.2 1 1252 . 226 ILE N N 123.6 0.2 1 1253 . 227 GLU HA H 4.04 0.02 1 1254 . 227 GLU H H 8.39 0.02 1 1255 . 227 GLU CA C 59.2 0.2 1 1256 . 227 GLU CB C 29.3 0.2 1 1257 . 227 GLU C C 178.7 0.2 1 1258 . 227 GLU N N 120.6 0.2 1 1259 . 228 SER HA H 4.36 0.02 1 1260 . 228 SER H H 8.04 0.02 1 1261 . 228 SER CA C 60.5 0.2 1 1262 . 228 SER CB C 63.5 0.2 1 1263 . 228 SER C C 175.4 0.2 1 1264 . 228 SER N N 115.00 0.2 1 1265 . 229 THR HA H 4.38 0.02 1 1266 . 229 THR H H 7.51 0.02 1 1267 . 229 THR CA C 62.3 0.2 1 1268 . 229 THR CB C 69.8 0.2 1 1269 . 229 THR C C 174.9 0.2 1 1270 . 229 THR N N 112.5 0.2 1 1271 . 230 SER HA H 4.54 0.02 1 1272 . 230 SER H H 7.71 0.02 1 1273 . 230 SER CA C 58.6 0.2 1 1274 . 230 SER CB C 63.7 0.2 1 1275 . 230 SER C C 173.7 0.2 1 1276 . 230 SER N N 118.4 0.2 1 1277 . 231 LYS HA H 4.62 0.02 1 1278 . 231 LYS H H 8.02 0.02 1 1279 . 231 LYS CA C 53.9 0.2 1 1280 . 231 LYS C C 173.4 0.2 1 1281 . 231 LYS N N 124.8 0.2 1 stop_ save_ save_chemical_shift_assignment_CcrA_2H _Saveframe_category assigned_chemical_shifts _Details ; This save frame contains the set of CB resonance assignments which could only be identified using [86% 2H; U-13C; U-15N]-labeled CcrA. Chemical shifts have not been corrected for the deuterium-isotope effect. ; loop_ _Sample_label $sample_three stop_ _Sample_conditions_label $sample_conditions _Chem_shift_reference_set_label $chemical_shift_reference _Mol_system_component_name CcrA _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 . 35 VAL CB C 34.2 0.2 1 2 . 53 THR CB C 67.9 0.2 1 3 . 61 GLU CB C 27.3 0.2 1 4 . 71 LEU CB C 38.8 0.2 1 5 . 79 ILE CB C 42.8 0.2 1 6 . 82 HIS CB C 26.2 0.2 1 7 . 107 THR CB C 66.7 0.2 1 8 . 108 ILE CB C 36.5 0.2 1 9 . 116 LEU CB C 40.3 0.2 1 10 . 123 PHE CB C 41.8 0.2 1 11 . 134 MET CB C 32.3 0.2 1 12 . 141 LEU CB C 41.7 0.2 1 13 . 149 ASN CB C 39.8 0.2 1 14 . 154 LEU CB C 39.1 0.2 1 15 . 164 CYS CB C 26.6 0.2 1 16 . 171 ALA CB C 18.6 0.2 1 17 . 178 SER CB C 62.9 0.2 1 18 . 185 TRP CB C 27.3 0.2 1 19 . 188 THR CB C 67.1 0.2 1 20 . 196 PHE CB C 36.8 0.2 1 21 . 203 VAL CB C 33.00 0.2 1 22 . 214 LEU CB C 40.9 0.2 1 23 . 218 THR CB C 62.4 0.2 1 24 . 231 LYS CB C 31.3 0.2 1 stop_ save_