data_5656 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Resonance Assignments for the Z Domain of Staphylococcal Protein A using a 2H, 13C, 15N enriched, selective methyl protonated sample ; loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Zheng Deyou . . 2 Swapna G.V.T. . . 3 Hunter Moseley N.B. . 4 Montelione Gaetano T. . stop_ _BMRB_accession_number 5656 _BMRB_flat_file_name bmr5656.str _Entry_type new _Submission_date 2003-01-09 _Accession_date 2003-01-13 _Entry_origination author _NMR_STAR_version 2.1 _Experimental_method NMR loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count '1H chemical shifts' 122 '13C chemical shifts' 235 '15N chemical shifts' 83 stop_ save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_title ; Rapid and automated protein fold determination using a minimal NOE and residual dipolar coupling constraint strategy ; _Citation_status submitted _Citation_type journal _MEDLINE_UI_code . _PubMed_ID . loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Zheng Deyou . . 2 Huang Yuanpeng J. . 3 Moseley Hunter N. B. 4 Xiao Rong . . 5 Aramini James . . 6 Swapna G.V.T. . . 7 Montelione Gaetano T. . stop_ _Journal_abbreviation 'Protein Sci.' _Journal_volume ? _Journal_issue ? _Page_first ? _Page_last ? _Year ? save_ ################################## # Molecular system description # ################################## save_system_staphylococcal_protein_A_Z_domain _Saveframe_category molecular_system _Mol_system_name 'staphylococcal protein A Z domain' _Abbreviation_common 'staphylococcal protein A Z domain' loop_ _Mol_system_component_name _Mol_label 'staphylococcal protein A Z domain' $staphylococcal_protein_A_Z_domain stop_ _System_physical_state native _System_oligomer_state monomer _System_paramagnetic no _System_thiol_state 'not present' save_ ######################## # Monomeric polymers # ######################## save_staphylococcal_protein_A_Z_domain _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'staphylococcal protein A Z domain' _Name_variant . _Abbreviation_common 'staphylococcal protein A Z domain' _Mol_thiol_state 'not present' _Residue_count 71 _Mol_residue_sequence ; KAIFVLNAQHDEAVDNKFNK EQQNAFYEILHLPNLNEEQR NAFIQSLKDDPSQSANLLAE AKKLNDAQAPK ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 -13 LYS 2 -12 ALA 3 -11 ILE 4 -10 PHE 5 -9 VAL 6 -8 LEU 7 -7 ASN 8 -6 ALA 9 -5 GLN 10 -4 HIS 11 -3 ASP 12 -2 GLU 13 -1 ALA 14 1 VAL 15 2 ASP 16 3 ASN 17 4 LYS 18 5 PHE 19 6 ASN 20 7 LYS 21 8 GLU 22 9 GLN 23 10 GLN 24 11 ASN 25 12 ALA 26 13 PHE 27 14 TYR 28 15 GLU 29 16 ILE 30 17 LEU 31 18 HIS 32 19 LEU 33 20 PRO 34 21 ASN 35 22 LEU 36 23 ASN 37 24 GLU 38 25 GLU 39 26 GLN 40 27 ARG 41 28 ASN 42 29 ALA 43 30 PHE 44 31 ILE 45 32 GLN 46 33 SER 47 34 LEU 48 35 LYS 49 36 ASP 50 37 ASP 51 38 PRO 52 39 SER 53 40 GLN 54 41 SER 55 42 ALA 56 43 ASN 57 44 LEU 58 45 LEU 59 46 ALA 60 47 GLU 61 48 ALA 62 49 LYS 63 50 LYS 64 51 LEU 65 52 ASN 66 53 ASP 67 54 ALA 68 55 GLN 69 56 ALA 70 57 PRO 71 58 LYS stop_ _Sequence_homology_query_date 2003-03-09 _Sequence_homology_query_revised_last_date 2003-03-09 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 2SPZ "A Chain A, Staphylococcal Protein A, Z-Domain, Nmr, 10 Structures" 122.41% 58 100% 100% 2e-26 PDB 1BDC "Staphylococcus Aureus Protein A, Immunoglobulin-Binding B Domain, Nmr, 10 Structures" 118.33% 60 98% 98% 1e-25 PDB 1BDD "Staphylococcus Aureus Protein A, Immunoglobulin-Binding B Domain, Nmr, Minimized Average Structure" 118.33% 60 98% 98% 1e-25 EMBL CAA65431.1 "protein A [synthetic construct]" 22.33% 318 100% 100% 3e-30 EMBL CAA49867.1 "staphylococcal protein A [synthetic construct]" 80.68% 88 98% 98% 1e-25 GenBank AAA73085.1 "protein A signal fusion protein" 29.46% 241 100% 100% 3e-30 GenBank AAB00807.1 "ZZ:beta-Gal' IgG-binding fusion protein" 33.02% 215 100% 100% 1e-29 GenBank AAA72944.1 "bifunctional fusion protein" 23.05% 308 98% 98% 1e-25 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $staphylococcal_protein_A_Z_domain 'S. aureus' 1280 Eubacteria . Staphylococcus aureus stop_ save_ ######################### # Experimental source # ######################### save_experimental_source _Saveframe_category experimental_source loop_ _Mol_label _Production_method _Host_organism_name_common _Genus _Species _Strain $staphylococcal_protein_A_Z_domain "recombinant technology" "E. coli" Escherichia coli . stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_one _Saveframe_category sample _Sample_type solution loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $staphylococcal_protein_A_Z_domain 1.1 mM "[U-13C; U-15N; U-2H] with Val, Leu, Ile(delta) methyl protonated" stop_ save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer_one _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model INOVA _Field_strength 600 save_ ############################# # NMR applied experiments # ############################# save_NMR_applied_experiment _Saveframe_category NMR_applied_experiment _Experiment_name ; 1H-15N HSQC 1H-13C HSQC HNCO HN(CA)CO HNCACB HN(CO)CACB H(CCCO)NH-TOCSY (H)CC(CO)NH-TOCSY ; save_ ############################ # Computer software used # ############################ save_AutoAssign _Saveframe_category software _Name AutoAssign _Version 1.9 loop_ _Task "automated backbone assignments" stop_ _Details ; 1. Moseley, H.N., Monleon, D., and Montelione, G.T. (2001) Methods Enzymol. 339: 91-108. 2. Zimmerman, D.E., Kulikowski, C.A., Huang, Y., Feng, W., Tashiro, M., Shimotakahara, S., Chien, C., Powers, R., and Montelione, G.T. (1997). J. Mol. Biol. 269: 592-610. ; save_ ####################### # Sample conditions # ####################### save_sample_conditions_one _Saveframe_category sample_conditions loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 6.5 . n/a temperature 303 . K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference_one _Saveframe_category chemical_shift_reference loop_ _Mol_common_name _Atom_type _Atom_isotope_number _Atom_group _Chem_shift_units _Chem_shift_value _Reference_method _Indirect_shift_ratio DSS H 1 'methyl protons' ppm 0.00 . 1.0 DSS C 13 'methyl protons' ppm 0.00 indirect 0.25144953 DSS N 15 'methyl protons' ppm 0.00 indirect 0.101329118 stop_ save_ ################################### # Assigned chemical shift lists # ################################### ################################################################### # Chemical Shift Ambiguity Index Value Definitions # # # # Index Value Definition # # # # 1 Unique # # 2 Ambiguity of geminal atoms or geminal methyl # # proton groups # # 3 Aromatic atoms on opposite sides of the ring # # (e.g. Tyr HE1 and HE2 protons) # # 4 Intraresidue ambiguities (e.g. Lys HG and # # HD protons) # # 5 Interresidue ambiguities (Lys 12 vs. Lys 27) # # 9 Ambiguous, specific ambiguity not defined # # # ################################################################### save_assigned_chemical_shifts_one _Saveframe_category assigned_chemical_shifts loop_ _Sample_label $sample_one stop_ _Sample_conditions_label $sample_conditions_one _Chem_shift_reference_set_label $chemical_shift_reference_one _Mol_system_component_name 'staphylococcal protein A Z domain' loop_ _Atom_shift_assign_ID _Residue_seq_code _Residue_label _Atom_name _Atom_type _Chem_shift_value _Chem_shift_value_error _Chem_shift_ambiguity_code 1 1 LYS C C 175.7 . 1 2 1 LYS CA C 56.08 . 1 3 1 LYS CB C 32.40 . 1 4 2 ALA H H 8.41 . 1 5 2 ALA C C 177.3 . 1 6 2 ALA CA C 52.02 . 1 7 2 ALA CB C 18.66 . 1 8 2 ALA N N 126.4 . 1 9 3 ILE H H 8.05 . 1 10 3 ILE C C 175.8 . 1 11 3 ILE CA C 60.66 . 1 12 3 ILE CB C 38.18 . 1 13 3 ILE CD1 C 12.63 . 1 14 3 ILE HD1 H 0.77 . 1 15 3 ILE N N 120.0 . 1 16 4 PHE H H 8.25 . 1 17 4 PHE C C 175.1 . 1 18 4 PHE CA C 57.16 . 1 19 4 PHE CB C 39.24 . 1 20 4 PHE N N 124.2 . 1 21 5 VAL H H 8.01 . 1 22 5 VAL C C 175.4 . 1 23 5 VAL CA C 61.66 . 1 24 5 VAL CB C 32.76 . 1 25 5 VAL CG1 C 20.51 . 2 26 5 VAL CG2 C 20.89 . 2 27 5 VAL HG1 H 0.83 . 2 28 5 VAL HG2 H 0.82 . 2 29 5 VAL N N 123.2 . 1 30 6 LEU H H 8.25 . 1 31 6 LEU C C 177.0 . 1 32 6 LEU CA C 55.17 . 1 33 6 LEU CB C 41.50 . 1 34 6 LEU CD1 C 23.78 . 2 35 6 LEU CD2 C 25.09 . 2 36 6 LEU HD1 H 0.84 . 2 37 6 LEU HD2 H 0.86 . 2 38 6 LEU N N 126.0 . 1 39 7 ASN H H 8.43 . 1 40 7 ASN C C 174.8 . 1 41 7 ASN CA C 53.03 . 1 42 7 ASN CB C 38.31 . 1 43 7 ASN HD21 H 6.90 . 2 44 7 ASN HD22 H 7.60 . 2 45 7 ASN ND2 N 112.89 . 1 46 7 ASN N N 119.5 . 1 47 8 ALA H H 8.22 . 1 48 8 ALA C C 177.6 . 1 49 8 ALA CA C 52.39 . 1 50 8 ALA CB C 18.56 . 1 51 8 ALA N N 124.0 . 1 52 9 GLN H H 8.29 . 1 53 9 GLN C C 175.9 . 1 54 9 GLN CA C 55.69 . 1 55 9 GLN CB C 28.69 . 1 56 9 GLN HE21 H 7.56 . 2 57 9 GLN HE22 H 6.86 . 2 58 9 GLN NE2 N 112.8 . 1 59 9 GLN N N 118.7 . 1 60 10 HIS H H 8.23 . 1 61 10 HIS C C 174.1 . 1 62 10 HIS CA C 55.29 . 1 63 10 HIS CB C 29.03 . 1 64 10 HIS N N 119.6 . 1 65 11 ASP H H 8.39 . 1 66 11 ASP C C 176.2 . 1 67 11 ASP CA C 54.01 . 1 68 11 ASP CB C 40.96 . 1 69 11 ASP N N 122.0 . 1 70 12 GLU H H 8.54 . 1 71 12 GLU C C 176.5 . 1 72 12 GLU CA C 56.83 . 1 73 12 GLU CB C 29.42 . 1 74 12 GLU N N 122.1 . 1 75 13 ALA H H 8.28 . 1 76 13 ALA C C 178.2 . 1 77 13 ALA CA C 52.60 . 1 78 13 ALA CB C 18.32 . 1 79 13 ALA N N 123.8 . 1 80 14 VAL H H 7.85 . 1 81 14 VAL C C 176.1 . 1 82 14 VAL CA C 62.40 . 1 83 14 VAL CB C 32.17 . 1 84 14 VAL CG1 C 20.51 . 2 85 14 VAL CG2 C 20.68 . 2 86 14 VAL HG1 H 0.70 . 2 87 14 VAL HG2 H 0.73 . 2 88 14 VAL N N 118.2 . 1 89 15 ASP H H 8.00 . 1 90 15 ASP C C 176.5 . 1 91 15 ASP CA C 54.40 . 1 92 15 ASP CB C 40.60 . 1 93 15 ASP N N 122.0 . 1 94 16 ASN H H 8.13 . 1 95 16 ASN C C 175.4 . 1 96 16 ASN CA C 53.82 . 1 97 16 ASN CB C 38.31 . 1 98 16 ASN HD21 H 7.50 . 2 99 16 ASN HD22 H 6.82 . 2 100 16 ASN ND2 N 112.69 . 1 101 16 ASN N N 118.9 . 1 102 17 LYS H H 8.21 . 1 103 17 LYS C C 176.8 . 1 104 17 LYS CA C 56.58 . 1 105 17 LYS CB C 31.40 . 1 106 17 LYS N N 119.4 . 1 107 18 PHE H H 7.87 . 1 108 18 PHE C C 177.0 . 1 109 18 PHE CA C 55.06 . 1 110 18 PHE CB C 39.12 . 1 111 18 PHE N N 118.8 . 1 112 19 ASN H H 8.43 . 1 113 19 ASN C C 175.8 . 1 114 19 ASN CA C 51.79 . 1 115 19 ASN CB C 37.64 . 1 116 19 ASN HD21 H 7.48 . 2 117 19 ASN HD22 H 6.91 . 2 118 19 ASN ND2 N 110.38 . 1 119 19 ASN N N 120.4 . 1 120 20 LYS H H 8.33 . 1 121 20 LYS C C 178.6 . 1 122 20 LYS CA C 59.67 . 1 123 20 LYS CB C 31.30 . 1 124 20 LYS N N 118.5 . 1 125 21 GLU H H 8.22 . 1 126 21 GLU C C 180.2 . 1 127 21 GLU CA C 59.47 . 1 128 21 GLU CB C 28.36 . 1 129 21 GLU N N 119.5 . 1 130 22 GLN H H 8.52 . 1 131 22 GLN C C 177.8 . 1 132 22 GLN CA C 58.44 . 1 133 22 GLN CB C 26.35 . 1 134 22 GLN HE21 H 6.96 . 2 135 22 GLN HE22 H 7.27 . 2 136 22 GLN NE2 N 111.06 . 1 137 22 GLN N N 121.4 . 1 138 23 GLN H H 8.75 . 1 139 23 GLN C C 178.4 . 1 140 23 GLN CA C 58.66 . 1 141 23 GLN CB C 27.86 . 1 142 23 GLN HE21 H 6.88 . 2 143 23 GLN HE22 H 7.24 . 2 144 23 GLN NE2 N 111.88 . 1 145 23 GLN N N 118.8 . 1 146 24 ASN H H 8.29 . 1 147 24 ASN C C 177.5 . 1 148 24 ASN CA C 55.99 . 1 149 24 ASN CB C 37.76 . 1 150 24 ASN HD21 H 7.74 . 2 151 24 ASN HD22 H 7.07 . 2 152 24 ASN ND2 N 112.69 . 1 153 24 ASN N N 117.4 . 1 154 25 ALA H H 7.88 . 1 155 25 ALA C C 178.2 . 1 156 25 ALA CA C 55.20 . 1 157 25 ALA CB C 17.50 . 1 158 25 ALA N N 122.1 . 1 159 26 PHE H H 8.13 . 1 160 26 PHE C C 176.2 . 1 161 26 PHE CA C 60.82 . 1 162 26 PHE CB C 38.31 . 1 163 26 PHE N N 117.8 . 1 164 27 TYR H H 8.15 . 1 165 27 TYR C C 178.9 . 1 166 27 TYR CA C 61.88 . 1 167 27 TYR CB C 37.64 . 1 168 27 TYR N N 116.6 . 1 169 28 GLU H H 8.54 . 1 170 28 GLU C C 180.6 . 1 171 28 GLU CA C 60.08 . 1 172 28 GLU CB C 29.35 . 1 173 28 GLU N N 119.0 . 1 174 29 ILE H H 8.41 . 1 175 29 ILE C C 178.1 . 1 176 29 ILE CA C 65.36 . 1 177 29 ILE CB C 36.74 . 1 178 29 ILE CD1 C 12.38 . 1 179 29 ILE HD1 H 0.47 . 1 180 29 ILE N N 119.5 . 1 181 30 LEU H H 7.88 . 1 182 30 LEU C C 177.1 . 1 183 30 LEU CA C 56.94 . 1 184 30 LEU CB C 41.09 . 1 185 30 LEU CD1 C 23.52 . 2 186 30 LEU CD2 C 24.57 . 2 187 30 LEU HD1 H 0.60 . 2 188 30 LEU HD2 H 0.50 . 2 189 30 LEU N N 117.4 . 1 190 31 HIS H H 7.19 . 1 191 31 HIS C C 174.7 . 1 192 31 HIS CA C 55.39 . 1 193 31 HIS CB C 28.89 . 1 194 31 HIS N N 111.4 . 1 195 32 LEU H H 7.19 . 1 196 32 LEU C C 177.7 . 1 197 32 LEU CA C 53.26 . 1 198 32 LEU CB C 39.61 . 1 199 32 LEU CD1 C 23.15 . 2 200 32 LEU CD2 C 27.07 . 2 201 32 LEU HD1 H 0.82 . 2 202 32 LEU HD2 H 0.63 . 2 203 32 LEU N N 124.2 . 1 204 33 PRO C C 178.2 . 1 205 33 PRO CA C 64.74 . 1 206 33 PRO CB C 31.84 . 1 207 34 ASN H H 8.89 . 1 208 34 ASN C C 176.4 . 1 209 34 ASN CA C 52.46 . 1 210 34 ASN CB C 38.22 . 1 211 34 ASN HD21 H 6.96 . 2 212 34 ASN HD22 H 7.44 . 2 213 34 ASN ND2 N 114.88 . 1 214 34 ASN N N 113.6 . 1 215 35 LEU H H 6.48 . 1 216 35 LEU C C 176.6 . 1 217 35 LEU CA C 54.09 . 1 218 35 LEU CB C 42.22 . 1 219 35 LEU CD1 C 22.15 . 2 220 35 LEU CD2 C 26.42 . 2 221 35 LEU HD1 H 0.84 . 2 222 35 LEU HD2 H 0.92 . 2 223 35 LEU N N 117.2 . 1 224 36 ASN H H 8.54 . 1 225 36 ASN C C 175.8 . 1 226 36 ASN CA C 51.15 . 1 227 36 ASN CB C 38.28 . 1 228 36 ASN HD21 H 7.05 . 2 229 36 ASN HD22 H 7.51 . 2 230 36 ASN ND2 N 112.18 . 1 231 36 ASN N N 119.0 . 1 232 37 GLU H H 8.61 . 1 233 37 GLU C C 178.3 . 1 234 37 GLU CA C 59.41 . 1 235 37 GLU CB C 28.77 . 1 236 37 GLU N N 118.0 . 1 237 38 GLU H H 8.23 . 1 238 38 GLU C C 178.3 . 1 239 38 GLU CA C 59.47 . 1 240 38 GLU CB C 28.36 . 1 241 38 GLU N N 119.6 . 1 242 39 GLN H H 8.50 . 1 243 39 GLN C C 178.6 . 1 244 39 GLN CA C 57.69 . 1 245 39 GLN CB C 28.37 . 1 246 39 GLN HE21 H 7.67 . 2 247 39 GLN HE22 H 8.25 . 2 248 39 GLN NE2 N 113.01 . 1 249 39 GLN N N 119.6 . 1 250 40 ARG H H 8.54 . 1 251 40 ARG C C 177.9 . 1 252 40 ARG CA C 60.11 . 1 253 40 ARG CB C 29.35 . 1 254 40 ARG N N 118.7 . 1 255 41 ASN H H 8.45 . 1 256 41 ASN C C 177.9 . 1 257 41 ASN CA C 55.72 . 1 258 41 ASN CB C 37.55 . 1 259 41 ASN HD21 H 7.64 . 2 260 41 ASN HD22 H 7.01 . 2 261 41 ASN ND2 N 112.46 . 1 262 41 ASN N N 114.8 . 1 263 42 ALA H H 7.84 . 1 264 42 ALA C C 181.0 . 1 265 42 ALA CA C 54.89 . 1 266 42 ALA CB C 17.19 . 1 267 42 ALA N N 123.0 . 1 268 43 PHE H H 7.95 . 1 269 43 PHE C C 178.2 . 1 270 43 PHE CA C 62.07 . 1 271 43 PHE CB C 39.11 . 1 272 43 PHE N N 116.8 . 1 273 44 ILE H H 8.24 . 1 274 44 ILE C C 177.8 . 1 275 44 ILE CA C 63.73 . 1 276 44 ILE CB C 35.83 . 1 277 44 ILE CD1 C 11.60 . 1 278 44 ILE HD1 H 0.56 . 1 279 44 ILE N N 118.1 . 1 280 45 GLN H H 8.40 . 1 281 45 GLN C C 178.4 . 1 282 45 GLN CA C 58.33 . 1 283 45 GLN CB C 27.53 . 1 284 45 GLN HE21 H 7.86 . 2 285 45 GLN HE22 H 6.95 . 2 286 45 GLN NE2 N 116.61 . 1 287 45 GLN N N 119.2 . 1 288 46 SER H H 8.05 . 1 289 46 SER C C 176.2 . 1 290 46 SER CA C 62.19 . 1 291 46 SER CB C 62.16 . 1 292 46 SER N N 114.9 . 1 293 47 LEU H H 8.09 . 1 294 47 LEU C C 177.5 . 1 295 47 LEU CA C 57.42 . 1 296 47 LEU CB C 41.54 . 1 297 47 LEU CD1 C 25.05 . 2 298 47 LEU CD2 C 26.07 . 2 299 47 LEU HD1 H 0.74 . 2 300 47 LEU HD2 H 0.71 . 2 301 47 LEU N N 124.1 . 1 302 48 LYS H H 7.98 . 1 303 48 LYS C C 179.2 . 1 304 48 LYS CA C 59.37 . 1 305 48 LYS CB C 31.80 . 1 306 48 LYS N N 115.4 . 1 307 49 ASP H H 8.15 . 1 308 49 ASP C C 177.5 . 1 309 49 ASP CA C 56.43 . 1 310 49 ASP CB C 40.41 . 1 311 49 ASP N N 117.8 . 1 312 50 ASP H H 7.56 . 1 313 50 ASP CA C 51.61 . 1 314 50 ASP CB C 39.84 . 1 315 50 ASP N N 113.6 . 1 316 51 PRO C C 178.5 . 1 317 51 PRO CA C 64.33 . 1 318 51 PRO CB C 31.18 . 1 319 52 SER H H 7.98 . 1 320 52 SER C C 176.4 . 1 321 52 SER CA C 60.90 . 1 322 52 SER CB C 61.97 . 1 323 52 SER N N 112.5 . 1 324 53 GLN H H 7.85 . 1 325 53 GLN C C 176.4 . 1 326 53 GLN CA C 54.78 . 1 327 53 GLN CB C 27.46 . 1 328 53 GLN HE21 H 7.59 . 2 329 53 GLN HE22 H 6.86 . 2 330 53 GLN NE2 N 114.41 . 1 331 53 GLN N N 120.3 . 1 332 54 SER H H 7.76 . 1 333 54 SER C C 174.3 . 1 334 54 SER CA C 63.13 . 1 335 54 SER CB C 62.22 . 1 336 54 SER N N 115.3 . 1 337 55 ALA H H 8.47 . 1 338 55 ALA C C 181.2 . 1 339 55 ALA CA C 55.26 . 1 340 55 ALA CB C 17.29 . 1 341 55 ALA N N 122.8 . 1 342 56 ASN H H 7.91 . 1 343 56 ASN C C 178.0 . 1 344 56 ASN CA C 55.58 . 1 345 56 ASN CB C 37.67 . 1 346 56 ASN HD21 H 7.77 . 2 347 56 ASN HD22 H 7.01 . 2 348 56 ASN ND2 N 113.13 . 1 349 56 ASN N N 118.4 . 1 350 57 LEU H H 8.59 . 1 351 57 LEU C C 178.5 . 1 352 57 LEU CA C 57.49 . 1 353 57 LEU CB C 41.60 . 1 354 57 LEU CD1 C 23.07 . 2 355 57 LEU CD2 C 26.02 . 2 356 57 LEU HD1 H 1.08 . 2 357 57 LEU HD2 H 0.74 . 2 358 57 LEU N N 121.3 . 1 359 58 LEU H H 8.40 . 1 360 58 LEU C C 178.1 . 1 361 58 LEU CA C 57.52 . 1 362 58 LEU CB C 41.17 . 1 363 58 LEU CD1 C 23.51 . 2 364 58 LEU CD2 C 24.41 . 2 365 58 LEU HD1 H 0.87 . 2 366 58 LEU HD2 H 0.90 . 2 367 58 LEU N N 118.5 . 1 368 59 ALA H H 7.58 . 1 369 59 ALA C C 181.4 . 1 370 59 ALA CA C 54.95 . 1 371 59 ALA CB C 17.20 . 1 372 59 ALA N N 119.2 . 1 373 60 GLU H H 8.06 . 1 374 60 GLU C C 179.1 . 1 375 60 GLU CA C 58.80 . 1 376 60 GLU CB C 28.88 . 1 377 60 GLU N N 119.2 . 1 378 61 ALA H H 8.45 . 1 379 61 ALA C C 179.7 . 1 380 61 ALA CA C 55.01 . 1 381 61 ALA CB C 16.68 . 1 382 61 ALA N N 123.8 . 1 383 62 LYS H H 8.47 . 1 384 62 LYS C C 178.9 . 1 385 62 LYS CA C 60.01 . 1 386 62 LYS CB C 31.29 . 1 387 62 LYS N N 117.9 . 1 388 63 LYS H H 7.66 . 1 389 63 LYS C C 179.9 . 1 390 63 LYS CA C 59.47 . 1 391 63 LYS CB C 31.58 . 1 392 63 LYS N N 119.9 . 1 393 64 LEU H H 7.89 . 1 394 64 LEU C C 178.2 . 1 395 64 LEU CA C 57.20 . 1 396 64 LEU CB C 41.21 . 1 397 64 LEU CD1 C 23.48 . 2 398 64 LEU CD2 C 24.68 . 2 399 64 LEU HD1 H 0.95 . 2 400 64 LEU HD2 H 0.98 . 2 401 64 LEU N N 122.0 . 1 402 65 ASN H H 8.54 . 1 403 65 ASN C C 177.7 . 1 404 65 ASN CA C 57.46 . 1 405 65 ASN CB C 41.20 . 1 406 65 ASN HD21 H 7.94 . 2 407 65 ASN HD22 H 6.85 . 2 408 65 ASN ND2 N 116.30 . 1 409 65 ASN N N 116.7 . 1 410 66 ASP H H 8.24 . 1 411 66 ASP C C 179.1 . 1 412 66 ASP CA C 56.79 . 1 413 66 ASP CB C 39.46 . 1 414 66 ASP N N 118.6 . 1 415 67 ALA H H 8.00 . 1 416 67 ALA C C 179.5 . 1 417 67 ALA CA C 54.11 . 1 418 67 ALA CB C 17.88 . 1 419 67 ALA N N 122.7 . 1 420 68 GLN H H 7.51 . 1 421 68 GLN C C 174.2 . 1 422 68 GLN CA C 54.66 . 1 423 68 GLN CB C 27.46 . 1 424 68 GLN HE21 H 8.75 . 2 425 68 GLN HE22 H 7.27 . 2 426 68 GLN NE2 N 111.17 . 1 427 68 GLN N N 114.8 . 1 428 69 ALA H H 7.08 . 1 429 69 ALA C C 175.6 . 1 430 69 ALA CA C 50.77 . 1 431 69 ALA CB C 17.23 . 1 432 69 ALA N N 124.2 . 1 433 70 PRO C C 176.3 . 1 434 70 PRO CA C 63.02 . 1 435 70 PRO CB C 31.21 . 1 436 71 LYS H H 8.08 . 1 437 71 LYS C C 181.7 . 1 438 71 LYS CA C 57.13 . 1 439 71 LYS CB C 32.96 . 1 440 71 LYS N N 127.4 . 1 stop_ save_