data_15170 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Backbone assignments of DNA methyltransferase M.HhaI ; _BMRB_accession_number 15170 _BMRB_flat_file_name bmr15170.str _Entry_type original _Submission_date 2007-03-09 _Accession_date 2007-03-09 _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 Zhou Hongjun . . 2 Shatz Whitney . . 3 Purdy Matthew . . 4 Fera Nick . . 5 Dahlquist Frederick . . 6 Reich Norbert . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 242 "13C chemical shifts" 483 "15N chemical shifts" 242 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2008-07-02 update BMRB 'complete entry citation' 2007-06-06 original author 'original release' stop_ save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title 'Long-range structural and dynamical changes induced by cofactor binding in DNA methyltransferase M.HhaI.' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 17523600 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Zhou Hongjun . . 2 Shatz Whitney . . 3 Purdy Matthew . . 4 Fera Nick . . 5 Dahlquist Frederick . . 6 Reich Norbert . . stop_ _Journal_abbreviation Biochemistry _Journal_volume 46 _Journal_issue 24 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 7261 _Page_last 7268 _Year 2007 _Details . loop_ _Keyword 'DNA binding' HhaI methyltransferase SAH stop_ save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name 'M.HhaI monomer' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label monomer $M.HhaI SAH $SAH stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state ? _System_paramagnetic no _System_thiol_state . _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_M.HhaI _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common M.HhaI _Molecular_mass . _Mol_thiol_state 'all free' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 331 _Mol_residue_sequence ; MIEIKDKQLTGLRFIDLFAG LGGFRLALESCGAECVYSNE WDKYAQEVYEMNFGEKPEGD ITQVNEKTIPDHDILCAGFP CQAFSISGKQKGFEDSRGTL FFDIARIVREKKPKVVFMEN VKNFASHDNGNTLEVVKNTM NELDYSFHAKVLNALDYGIP QKRERIYMICFRNDLNIQNF QFPKPFELNTFVKDLLLPDS EVEHLVIDRKDLVMTNQEIE QTTPKTVRLGIVGKGGQGER IYSTRGIAITLSAYGGGIFA KTGGYLVNGKTRKLHPRECA RVMGYPDSYKVHPSTSQAYK QFGNSVVINVLQYIAYNIGS SLNLEHHHHHH ; loop_ _Residue_seq_code _Residue_label 1 MET 2 ILE 3 GLU 4 ILE 5 LYS 6 ASP 7 LYS 8 GLN 9 LEU 10 THR 11 GLY 12 LEU 13 ARG 14 PHE 15 ILE 16 ASP 17 LEU 18 PHE 19 ALA 20 GLY 21 LEU 22 GLY 23 GLY 24 PHE 25 ARG 26 LEU 27 ALA 28 LEU 29 GLU 30 SER 31 CYS 32 GLY 33 ALA 34 GLU 35 CYS 36 VAL 37 TYR 38 SER 39 ASN 40 GLU 41 TRP 42 ASP 43 LYS 44 TYR 45 ALA 46 GLN 47 GLU 48 VAL 49 TYR 50 GLU 51 MET 52 ASN 53 PHE 54 GLY 55 GLU 56 LYS 57 PRO 58 GLU 59 GLY 60 ASP 61 ILE 62 THR 63 GLN 64 VAL 65 ASN 66 GLU 67 LYS 68 THR 69 ILE 70 PRO 71 ASP 72 HIS 73 ASP 74 ILE 75 LEU 76 CYS 77 ALA 78 GLY 79 PHE 80 PRO 81 CYS 82 GLN 83 ALA 84 PHE 85 SER 86 ILE 87 SER 88 GLY 89 LYS 90 GLN 91 LYS 92 GLY 93 PHE 94 GLU 95 ASP 96 SER 97 ARG 98 GLY 99 THR 100 LEU 101 PHE 102 PHE 103 ASP 104 ILE 105 ALA 106 ARG 107 ILE 108 VAL 109 ARG 110 GLU 111 LYS 112 LYS 113 PRO 114 LYS 115 VAL 116 VAL 117 PHE 118 MET 119 GLU 120 ASN 121 VAL 122 LYS 123 ASN 124 PHE 125 ALA 126 SER 127 HIS 128 ASP 129 ASN 130 GLY 131 ASN 132 THR 133 LEU 134 GLU 135 VAL 136 VAL 137 LYS 138 ASN 139 THR 140 MET 141 ASN 142 GLU 143 LEU 144 ASP 145 TYR 146 SER 147 PHE 148 HIS 149 ALA 150 LYS 151 VAL 152 LEU 153 ASN 154 ALA 155 LEU 156 ASP 157 TYR 158 GLY 159 ILE 160 PRO 161 GLN 162 LYS 163 ARG 164 GLU 165 ARG 166 ILE 167 TYR 168 MET 169 ILE 170 CYS 171 PHE 172 ARG 173 ASN 174 ASP 175 LEU 176 ASN 177 ILE 178 GLN 179 ASN 180 PHE 181 GLN 182 PHE 183 PRO 184 LYS 185 PRO 186 PHE 187 GLU 188 LEU 189 ASN 190 THR 191 PHE 192 VAL 193 LYS 194 ASP 195 LEU 196 LEU 197 LEU 198 PRO 199 ASP 200 SER 201 GLU 202 VAL 203 GLU 204 HIS 205 LEU 206 VAL 207 ILE 208 ASP 209 ARG 210 LYS 211 ASP 212 LEU 213 VAL 214 MET 215 THR 216 ASN 217 GLN 218 GLU 219 ILE 220 GLU 221 GLN 222 THR 223 THR 224 PRO 225 LYS 226 THR 227 VAL 228 ARG 229 LEU 230 GLY 231 ILE 232 VAL 233 GLY 234 LYS 235 GLY 236 GLY 237 GLN 238 GLY 239 GLU 240 ARG 241 ILE 242 TYR 243 SER 244 THR 245 ARG 246 GLY 247 ILE 248 ALA 249 ILE 250 THR 251 LEU 252 SER 253 ALA 254 TYR 255 GLY 256 GLY 257 GLY 258 ILE 259 PHE 260 ALA 261 LYS 262 THR 263 GLY 264 GLY 265 TYR 266 LEU 267 VAL 268 ASN 269 GLY 270 LYS 271 THR 272 ARG 273 LYS 274 LEU 275 HIS 276 PRO 277 ARG 278 GLU 279 CYS 280 ALA 281 ARG 282 VAL 283 MET 284 GLY 285 TYR 286 PRO 287 ASP 288 SER 289 TYR 290 LYS 291 VAL 292 HIS 293 PRO 294 SER 295 THR 296 SER 297 GLN 298 ALA 299 TYR 300 LYS 301 GLN 302 PHE 303 GLY 304 ASN 305 SER 306 VAL 307 VAL 308 ILE 309 ASN 310 VAL 311 LEU 312 GLN 313 TYR 314 ILE 315 ALA 316 TYR 317 ASN 318 ILE 319 GLY 320 SER 321 SER 322 LEU 323 ASN 324 LEU 325 GLU 326 HIS 327 HIS 328 HIS 329 HIS 330 HIS 331 HIS stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-10-07 loop_ _Database_name _Database_accession_code _Database_entry_mol_name _Sequence_query_to_submitted_percentage _Sequence_subject_length _Sequence_identity _Sequence_positive _Sequence_homology_expectation_value BMRB 16395 M.HhaI 100.00 331 100.00 100.00 0.00e+00 PDB 10MH "Ternary Structure Of Hhai Methyltransferase With Adohcy And Hemimethylated Dna Containing 5,6-Dihydro-5-Azacytosine At The Targ" 98.79 327 98.78 99.39 0.00e+00 PDB 1FJX "Structure Of Ternary Complex Of Hhai Methyltransferase Mutant (T250g) In Complex With Dna And Adohcy" 98.79 327 98.47 99.08 0.00e+00 PDB 1HMY "Crystal Structure Of The Hhai Dna Methyltransferase Complexed With S- Adenosyl-L-Methionine" 98.79 327 98.78 99.39 0.00e+00 PDB 1M0E "Zebularine: A Novel Dna Methylation Inhibitor That Forms A Covalent Complex With Dna Methyltransferase" 98.79 327 98.78 99.39 0.00e+00 PDB 1MHT "Covalent Ternary Structure Of Hhai Methyltransferase, Dna And S-Adenosyl-L-Homocysteine" 98.79 327 98.78 99.39 0.00e+00 PDB 1SKM "Hhai Methyltransferase In Complex With Dna Containing An Abasic South Carbocyclic Sugar At Its Target Site" 98.79 327 98.78 99.39 0.00e+00 PDB 1SVU "Structure Of The Q237w Mutant Of Hhai Dna Methyltransferase: An Insight Into Protein-Protein Interactions" 98.79 327 98.47 99.08 0.00e+00 PDB 2C7O "Hhai Dna Methyltransferase Complex With 13mer Oligonucleotide Containing 2-aminopurine Adjacent To The Target Base (pcgc:gmgc) " 98.79 327 98.78 99.39 0.00e+00 PDB 2C7P "Hhai Dna Methyltransferase Complex With Oligonucleotide Containing 2-aminopurine Opposite To The Target Base (gcgc:gmpc) And Sa" 98.79 327 98.78 99.39 0.00e+00 PDB 2C7Q "Hhai Dna Methyltransferase Complex With Oligonucleotide Containing 2-aminopurine Outside The Recognition Sequence (paired With " 98.79 327 98.78 99.39 0.00e+00 PDB 2C7R "Hhai Dna Methyltransferase (t250g Mutant) Complex With Oligonucleotide Containing 2-aminopurine As A Target Base (gpgc:gmgc) An" 98.79 327 98.47 99.08 0.00e+00 PDB 2HMY "Binary Complex Of Hhai Methyltransferase With Adomet Formed In The Presence Of A Short Nonpsecific Dna Oligonucleotide" 98.79 327 98.78 99.39 0.00e+00 PDB 2HR1 "Ternary Structure Of Wt M.hhai C5-cytosine Dna Methyltransferase With Unmodified Dna And Adohcy" 98.79 327 98.78 99.39 0.00e+00 PDB 2I9K "Engineered Extrahelical Base Destabilization Enhances Sequence Discrimination Of Dna Methyltransferase M.Hhai" 98.79 327 98.47 99.08 0.00e+00 PDB 2UYC "Hhai Dna Methyltransferase R163n Mutant Complex With 13mer Gcgc-Gmgc Oligonucleotide And Sah" 98.79 327 98.47 99.08 0.00e+00 PDB 2UYH "Hhai Dna Methyltransferase S87q-Q237s Mutant Complex With 13mer Gcgc-Gmgc Oligonucleotide And Sah" 98.79 327 98.17 98.78 0.00e+00 PDB 2UZ4 "Hhai Dna Methyltransferase R165n Mutant Complex With 13mer Gcgc-Gmgc Oligonucleotide And Sah" 98.79 327 98.47 99.08 0.00e+00 PDB 2Z6A "S-Adenosyl-L-Methionine-Dependent Methyl Transfer: Observable Precatalytic Intermediates During Dna Cytosine Methylation" 98.79 327 98.47 99.08 0.00e+00 PDB 2Z6Q "Ternary Structure Of Arg165ala M.Hhai C5-Cytosine Dna Methyltransferase With Unmodified Dna And Adohcy" 98.79 327 98.47 99.08 0.00e+00 PDB 2Z6U "Ternary Structure Of The Glu119ala M.Hhai, C5-Cytosine Dna Methyltransferase, With Unmodified Dna And Adohcy" 98.79 327 98.47 99.08 0.00e+00 PDB 2ZCJ "Ternary Structure Of The Glu119gln M.Hhai, C5-Cytosine Dna Methyltransferase, With Unmodified Dna And Adohcy" 98.79 327 98.47 99.39 0.00e+00 PDB 3EEO "M. Hhai Co-Crystallized With Synthetic Dsdna Containing A Propane Diol In Place Of The Deoxycytidine Residue Targeted For Methy" 98.79 327 98.78 99.39 0.00e+00 PDB 3MHT "Ternary Structure Of Hhai Methyltransferase With Unmodified Dna And Adohcy" 98.79 327 98.78 99.39 0.00e+00 PDB 4MHT "Ternary Structure Of Hhai Methyltransferase With Native Dna And Adohcy" 98.79 327 98.78 99.39 0.00e+00 PDB 5MHT "Ternary Structure Of Hhai Methyltransferase With Hemimethylated Dna And Adohcy" 98.79 327 98.78 99.39 0.00e+00 PDB 6MHT "Ternary Structure Of Hhai Methyltransferase With Adohcy And Dna Containing 4'-Thio-2'deoxycytidine At The Target" 98.79 327 98.78 99.39 0.00e+00 PDB 7MHT "Cytosine-Specific Methyltransferase HhaiDNA COMPLEX" 98.79 327 98.78 99.39 0.00e+00 PDB 8MHT "Cytosine-Specific Methyltransferase HhaiDNA COMPLEX" 98.79 327 98.78 99.39 0.00e+00 PDB 9MHT "Cytosine-specific Methyltransferase Hhai/dna Complex" 98.79 327 98.78 99.39 0.00e+00 GB AAA24989 "DNA methylase [Haemophilus haemolyticus]" 98.79 327 98.78 99.39 0.00e+00 GB EIJ69210 "modification methylase HhaI [Haemophilus parahaemolyticus HK385]" 98.79 327 98.78 99.39 0.00e+00 REF WP_005706946 "restriction endonuclease subunit M [Haemophilus parahaemolyticus]" 98.79 327 98.78 99.39 0.00e+00 SP P05102 "RecName: Full=Modification methylase HhaI; Short=M.HhaI; AltName: Full=Cytosine-specific methyltransferase HhaI" 98.79 327 98.78 99.39 0.00e+00 stop_ save_ ############# # Ligands # ############# save_SAH _Saveframe_category ligand _Mol_type non-polymer _Name_common "SAH (S-ADENOSYL-L-HOMOCYSTEINE)" _BMRB_code . _PDB_code SAH _Molecular_mass 384.411 _Mol_charge 0 _Mol_paramagnetic . _Mol_aromatic . _Details ; Information obtained from PDB's Chemical Component Dictionary at http://wwpdb-remediation.rutgers.edu/downloads.html Downloaded on Wed Dec 20 05:07:21 2006 ; loop_ _Atom_name _PDB_atom_name _Atom_type _Atom_chirality _Atom_charge _Atom_oxidation_number _Atom_unpaired_electrons C C C N 0 . ? C1' C1' C R 0 . ? C2 C2 C N 0 . ? C2' C2' C R 0 . ? C3' C3' C S 0 . ? C4 C4 C N 0 . ? C4' C4' C S 0 . ? C5 C5 C N 0 . ? C5' C5' C N 0 . ? C6 C6 C N 0 . ? C8 C8 C N 0 . ? CA CA C S 0 . ? CB CB C N 0 . ? CG CG C N 0 . ? H1' H1' H N 0 . ? H2 H2 H N 0 . ? H2' H2' H N 0 . ? H3' H3' H N 0 . ? H4' H4' H N 0 . ? H5'1 H5'1 H N 0 . ? H5'2 H5'2 H N 0 . ? H8 H8 H N 0 . ? HA HA H N 0 . ? HB1 HB1 H N 0 . ? HB2 HB2 H N 0 . ? HG1 HG1 H N 0 . ? HG2 HG2 H N 0 . ? HN1 HN1 H N 0 . ? HN2 HN2 H N 0 . ? HN61 HN61 H N 0 . ? HN62 HN62 H N 0 . ? HO2' HO2' H N 0 . ? HO3' HO3' H N 0 . ? HXT HXT H N 0 . ? N N N N 0 . ? N1 N1 N N 0 . ? N3 N3 N N 0 . ? N6 N6 N N 0 . ? N7 N7 N N 0 . ? N9 N9 N N 0 . ? O O O N 0 . ? O2' O2' O N 0 . ? O3' O3' O N 0 . ? O4' O4' O N 0 . ? OXT OXT O N 0 . ? SD SD S N 0 . ? stop_ loop_ _Bond_order _Bond_atom_one_atom_name _Bond_atom_two_atom_name _PDB_bond_atom_one_atom_name _PDB_bond_atom_two_atom_name SING N CA ? ? SING N HN1 ? ? SING N HN2 ? ? SING CA CB ? ? SING CA C ? ? SING CA HA ? ? SING CB CG ? ? SING CB HB1 ? ? SING CB HB2 ? ? SING CG SD ? ? SING CG HG1 ? ? SING CG HG2 ? ? SING SD C5' ? ? DOUB C O ? ? SING C OXT ? ? SING OXT HXT ? ? SING C5' C4' ? ? SING C5' H5'1 ? ? SING C5' H5'2 ? ? SING C4' O4' ? ? SING C4' C3' ? ? SING C4' H4' ? ? SING O4' C1' ? ? SING C3' O3' ? ? SING C3' C2' ? ? SING C3' H3' ? ? SING O3' HO3' ? ? SING C2' O2' ? ? SING C2' C1' ? ? SING C2' H2' ? ? SING O2' HO2' ? ? SING C1' N9 ? ? SING C1' H1' ? ? SING N9 C8 ? ? SING N9 C4 ? ? DOUB C8 N7 ? ? SING C8 H8 ? ? SING N7 C5 ? ? SING C5 C6 ? ? DOUB C5 C4 ? ? SING C6 N6 ? ? DOUB C6 N1 ? ? SING N6 HN61 ? ? SING N6 HN62 ? ? SING N1 C2 ? ? DOUB C2 N3 ? ? SING C2 H2 ? ? SING N3 C4 ? ? 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 $M.HhaI 'E. coli' 562 Bacteria . Escherichia coli 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 $M.HhaI 'recombinant technology' . Escherichia coli . pET28a 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 $M.HhaI . mM 0.3 0.6 '[U-13C; U-15N; U-2H]' 'sodium phosphate' 50 mM . . 'natural abundance' DTT 5 mM . . 'natural abundance' 'sodium chloride' 100 mM . . 'natural abundance' Arg 50 mM . . 'natural abundance' Glu 50 mM . . 'natural abundance' 'sodium azide' 0.02 % . . 'natural abundance' glycerol 0.75 % . . 'natural abundance' stop_ save_ ############################ # Computer software used # ############################ save_NMRPipe _Saveframe_category software _Name NMRPipe _Version . loop_ _Vendor _Address _Electronic_address 'Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax' . . stop_ loop_ _Task processing stop_ _Details . save_ save_ANSIG _Saveframe_category software _Name ANSIG _Version . loop_ _Vendor _Address _Electronic_address Kraulis . . stop_ loop_ _Task 'chemical shift assignment' stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model INOVA _Field_strength 600 _Details . save_ ############################# # NMR applied experiments # ############################# save_2D_1H-15N_HSQC_1 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-15N HSQC' _Sample_label $sample_1 save_ save_3D_HNCA_2 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCA' _Sample_label $sample_1 save_ save_3D_HN(CO)CA_3 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HN(CO)CA' _Sample_label $sample_1 save_ save_3D_HNCACB_4 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCACB' _Sample_label $sample_1 save_ save_3D_HN(COCA)CB_5 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HN(COCA)CB' _Sample_label $sample_1 save_ save_3D_HNCO_6 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCO' _Sample_label $sample_1 save_ save_3D_HCACO_7 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HCACO' _Sample_label $sample_1 save_ ####################### # Sample conditions # ####################### save_sample_conditions_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units 'ionic strength' 0.1 . M pH 6.5 . pH pressure 1 . atm temperature 298 . K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference_1 _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 TSP C 13 'methyl protons' ppm 0 external indirect . . . 0.251449530 TSP H 1 'methyl protons' ppm 0 external direct . . . 1 TSP N 15 'methyl protons' ppm 0 external 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_assigned_chem_shift_list_1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Experiment_label '2D 1H-15N HSQC' '3D HNCA' '3D HN(CO)CA' '3D HNCACB' '3D HN(COCA)CB' stop_ loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $sample_conditions_1 _Chem_shift_reference_set_label $chemical_shift_reference_1 _Mol_system_component_name monomer _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 8 8 GLN CA C 57.03 . 1 2 8 8 GLN CB C 29.46 . 1 3 9 9 LEU H H 8.136 . 1 4 9 9 LEU CA C 52.80 . 1 5 9 9 LEU CB C 40.54 . 1 6 9 9 LEU N N 114.44 . 1 7 10 10 THR H H 7.168 . 1 8 10 10 THR CA C 64.87 . 1 9 10 10 THR CB C 68.60 . 1 10 10 10 THR N N 115.96 . 1 11 11 11 GLY H H 8.759 . 1 12 11 11 GLY CA C 44.60 . 1 13 11 11 GLY N N 116.48 . 1 14 12 12 LEU H H 7.964 . 1 15 12 12 LEU CA C 53.71 . 1 16 12 12 LEU CB C 41.60 . 1 17 12 12 LEU N N 120.42 . 1 18 13 13 ARG H H 9.917 . 1 19 13 13 ARG CA C 53.71 . 1 20 13 13 ARG CB C 32.93 . 1 21 13 13 ARG N N 122.17 . 1 22 14 14 PHE H H 9.748 . 1 23 14 14 PHE CA C 54.45 . 1 24 14 14 PHE CB C 44.28 . 1 25 14 14 PHE N N 122.57 . 1 26 18 18 PHE CA C 58.33 . 1 27 18 18 PHE CB C 34.80 . 1 28 19 19 ALA H H 8.602 . 1 29 19 19 ALA CA C 56.44 . 1 30 19 19 ALA CB C 19.33 . 1 31 19 19 ALA N N 119.39 . 1 32 20 20 GLY H H 10.039 . 1 33 20 20 GLY CA C 46.84 . 1 34 20 20 GLY N N 110.46 . 1 35 21 21 LEU H H 7.805 . 1 36 21 21 LEU CA C 54.36 . 1 37 21 21 LEU CB C 41.36 . 1 38 21 21 LEU N N 122.39 . 1 39 22 22 GLY H H 9.338 . 1 40 22 22 GLY CA C 46.66 . 1 41 22 22 GLY N N 105.28 . 1 42 23 23 GLY H H 7.875 . 1 43 23 23 GLY CA C 48.41 . 1 44 23 23 GLY N N 110.95 . 1 45 24 24 PHE H H 9.210 . 1 46 24 24 PHE CA C 62.09 . 1 47 24 24 PHE N N 117.40 . 1 48 25 25 ARG CA C 58.29 . 1 49 26 26 LEU H H 8.336 . 1 50 26 26 LEU CA C 57.40 . 1 51 26 26 LEU CB C 41.84 . 1 52 26 26 LEU N N 118.38 . 1 53 27 27 ALA H H 7.662 . 1 54 27 27 ALA CA C 54.48 . 1 55 27 27 ALA CB C 18.56 . 1 56 27 27 ALA N N 118.34 . 1 57 28 28 LEU H H 8.551 . 1 58 28 28 LEU N N 121.83 . 1 59 30 30 SER CA C 58.88 . 1 60 31 31 CYS H H 6.922 . 1 61 31 31 CYS CA C 58.12 . 1 62 31 31 CYS CB C 29.01 . 1 63 31 31 CYS N N 122.89 . 1 64 32 32 GLY H H 8.547 . 1 65 32 32 GLY CA C 44.47 . 1 66 32 32 GLY N N 111.28 . 1 67 33 33 ALA H H 7.218 . 1 68 33 33 ALA CA C 51.50 . 1 69 33 33 ALA CB C 19.86 . 1 70 33 33 ALA N N 122.86 . 1 71 34 34 GLU H H 8.689 . 1 72 34 34 GLU CA C 53.91 . 1 73 34 34 GLU CB C 32.41 . 1 74 34 34 GLU N N 119.75 . 1 75 35 35 CYS H H 9.705 . 1 76 35 35 CYS CA C 57.83 . 1 77 35 35 CYS CB C 27.00 . 1 78 35 35 CYS N N 130.09 . 1 79 36 36 VAL H H 8.439 . 1 80 36 36 VAL CA C 59.96 . 1 81 36 36 VAL CB C 31.84 . 1 82 36 36 VAL N N 119.92 . 1 83 37 37 TYR H H 7.326 . 1 84 37 37 TYR CA C 59.48 . 1 85 37 37 TYR CB C 39.89 . 1 86 37 37 TYR N N 121.30 . 1 87 38 38 SER H H 7.275 . 1 88 38 38 SER CA C 56.14 . 1 89 38 38 SER CB C 66.42 . 1 90 38 38 SER N N 122.05 . 1 91 39 39 ASN H H 7.825 . 1 92 39 39 ASN CA C 53.19 . 1 93 39 39 ASN CB C 43.75 . 1 94 39 39 ASN N N 120.02 . 1 95 40 40 GLU H H 8.848 . 1 96 40 40 GLU CA C 55.97 . 1 97 40 40 GLU CB C 31.62 . 1 98 40 40 GLU N N 128.57 . 1 99 41 41 TRP H H 7.602 . 1 100 41 41 TRP CA C 54.91 . 1 101 41 41 TRP CB C 29.22 . 1 102 41 41 TRP N N 125.75 . 1 103 42 42 ASP H H 10.429 . 1 104 42 42 ASP CA C 54.23 . 1 105 42 42 ASP CB C 42.43 . 1 106 42 42 ASP N N 129.44 . 1 107 43 43 LYS H H 8.518 . 1 108 43 43 LYS CA C 58.55 . 1 109 43 43 LYS CB C 31.14 . 1 110 43 43 LYS N N 127.71 . 1 111 44 44 TYR H H 7.335 . 1 112 44 44 TYR CA C 59.37 . 1 113 44 44 TYR CB C 35.73 . 1 114 44 44 TYR N N 119.07 . 1 115 45 45 ALA H H 8.634 . 1 116 45 45 ALA CA C 54.53 . 1 117 45 45 ALA CB C 16.10 . 1 118 45 45 ALA N N 126.24 . 1 119 46 46 GLN H H 8.828 . 1 120 46 46 GLN CA C 59.40 . 1 121 46 46 GLN CB C 27.63 . 1 122 46 46 GLN N N 115.77 . 1 123 47 47 GLU H H 7.541 . 1 124 47 47 GLU CA C 58.95 . 1 125 47 47 GLU CB C 29.21 . 1 126 47 47 GLU N N 117.88 . 1 127 48 48 VAL H H 7.673 . 1 128 48 48 VAL CA C 64.05 . 1 129 48 48 VAL CB C 31.94 . 1 130 48 48 VAL N N 120.77 . 1 131 49 49 TYR H H 9.116 . 1 132 49 49 TYR CA C 62.13 . 1 133 49 49 TYR CB C 38.65 . 1 134 49 49 TYR N N 129.29 . 1 135 50 50 GLU H H 8.574 . 1 136 50 50 GLU CA C 59.31 . 1 137 50 50 GLU CB C 28.74 . 1 138 50 50 GLU N N 120.50 . 1 139 51 51 MET H H 7.852 . 1 140 51 51 MET CA C 58.52 . 1 141 51 51 MET CB C 32.93 . 1 142 51 51 MET N N 118.84 . 1 143 52 52 ASN H H 7.124 . 1 144 52 52 ASN CA C 55.58 . 1 145 52 52 ASN CB C 40.72 . 1 146 52 52 ASN N N 114.16 . 1 147 53 53 PHE H H 8.747 . 1 148 53 53 PHE CA C 57.57 . 1 149 53 53 PHE CB C 38.89 . 1 150 53 53 PHE N N 116.07 . 1 151 54 54 GLY H H 8.179 . 1 152 54 54 GLY CA C 45.72 . 1 153 54 54 GLY N N 108.64 . 1 154 55 55 GLU H H 6.912 . 1 155 55 55 GLU CA C 53.26 . 1 156 55 55 GLU CB C 32.23 . 1 157 55 55 GLU N N 115.52 . 1 158 56 56 LYS H H 8.545 . 1 159 56 56 LYS N N 123.01 . 1 160 57 57 PRO CA C 62.10 . 1 161 57 57 PRO CB C 32.32 . 1 162 58 58 GLU H H 7.184 . 1 163 58 58 GLU CA C 56.30 . 1 164 58 58 GLU CB C 29.04 . 1 165 58 58 GLU N N 121.60 . 1 166 59 59 GLY H H 7.667 . 1 167 59 59 GLY CA C 43.35 . 1 168 59 59 GLY N N 106.65 . 1 169 60 60 ASP H H 7.552 . 1 170 60 60 ASP CA C 53.99 . 1 171 60 60 ASP CB C 41.65 . 1 172 60 60 ASP N N 110.99 . 1 173 61 61 ILE H H 9.447 . 1 174 61 61 ILE CA C 61.35 . 1 175 61 61 ILE CB C 36.18 . 1 176 61 61 ILE N N 132.85 . 1 177 62 62 THR H H 8.098 . 1 178 62 62 THR CA C 63.72 . 1 179 62 62 THR CB C 68.79 . 1 180 62 62 THR N N 112.64 . 1 181 63 63 GLN H H 7.465 . 1 182 63 63 GLN CA C 53.76 . 1 183 63 63 GLN CB C 28.72 . 1 184 63 63 GLN N N 117.36 . 1 185 64 64 VAL H H 7.272 . 1 186 64 64 VAL CA C 61.87 . 1 187 64 64 VAL CB C 31.94 . 1 188 64 64 VAL N N 122.81 . 1 189 65 65 ASN H H 9.054 . 1 190 65 65 ASN CA C 53.70 . 1 191 65 65 ASN CB C 38.52 . 1 192 65 65 ASN N N 128.33 . 1 193 66 66 GLU H H 10.180 . 1 194 66 66 GLU CA C 58.57 . 1 195 66 66 GLU CB C 27.36 . 1 196 66 66 GLU N N 129.82 . 1 197 67 67 LYS H H 8.177 . 1 198 67 67 LYS CA C 58.16 . 1 199 67 67 LYS CB C 31.11 . 1 200 67 67 LYS N N 118.09 . 1 201 68 68 THR H H 7.595 . 1 202 68 68 THR CA C 61.23 . 1 203 68 68 THR CB C 68.96 . 1 204 68 68 THR N N 107.95 . 1 205 69 69 ILE H H 6.575 . 1 206 69 69 ILE CA C 56.29 . 1 207 69 69 ILE CB C 35.94 . 1 208 69 69 ILE N N 125.82 . 1 209 77 77 ALA H H 6.731 . 1 210 77 77 ALA CA C 53.20 . 1 211 77 77 ALA CB C 22.46 . 1 212 77 77 ALA N N 120.79 . 1 213 78 78 GLY H H 8.882 . 1 214 78 78 GLY CA C 45.88 . 1 215 78 78 GLY N N 118.19 . 1 216 79 79 PHE H H 5.961 . 1 217 79 79 PHE CA C 52.48 . 1 218 79 79 PHE CB C 38.22 . 1 219 79 79 PHE N N 113.84 . 1 220 80 80 PRO CA C 62.18 . 1 221 80 80 PRO CB C 31.09 . 1 222 81 81 CYS H H 8.439 . 1 223 81 81 CYS CA C 59.48 . 1 224 81 81 CYS CB C 24.59 . 1 225 81 81 CYS N N 125.46 . 1 226 82 82 GLN H H 8.750 . 1 227 82 82 GLN CA C 54.06 . 1 228 82 82 GLN CB C 28.76 . 1 229 82 82 GLN N N 131.10 . 1 230 83 83 ALA H H 8.093 . 1 231 83 83 ALA CA C 50.80 . 1 232 83 83 ALA CB C 17.80 . 1 233 83 83 ALA N N 120.94 . 1 234 84 84 PHE H H 9.538 . 1 235 84 84 PHE CA C 56.56 . 1 236 84 84 PHE CB C 39.25 . 1 237 84 84 PHE N N 122.44 . 1 238 85 85 SER H H 9.122 . 1 239 85 85 SER CA C 57.03 . 1 240 85 85 SER CB C 62.20 . 1 241 85 85 SER N N 119.49 . 1 242 86 86 ILE H H 7.958 . 1 243 86 86 ILE CA C 60.56 . 1 244 86 86 ILE CB C 37.57 . 1 245 86 86 ILE N N 124.27 . 1 246 87 87 SER H H 8.659 . 1 247 87 87 SER CA C 58.14 . 1 248 87 87 SER CB C 63.85 . 1 249 87 87 SER N N 121.94 . 1 250 88 88 GLY H H 8.410 . 1 251 88 88 GLY CA C 44.74 . 1 252 88 88 GLY N N 112.85 . 1 253 89 89 LYS H H 8.224 . 1 254 89 89 LYS CA C 56.25 . 1 255 89 89 LYS CB C 32.03 . 1 256 89 89 LYS N N 120.38 . 1 257 90 90 GLN H H 8.248 . 1 258 90 90 GLN CA C 55.92 . 1 259 90 90 GLN CB C 28.00 . 1 260 90 90 GLN N N 119.82 . 1 261 91 91 LYS H H 8.196 . 1 262 91 91 LYS CA C 55.38 . 1 263 91 91 LYS CB C 31.98 . 1 264 91 91 LYS N N 121.45 . 1 265 92 92 GLY H H 8.821 . 1 266 92 92 GLY CA C 45.05 . 1 267 92 92 GLY N N 110.78 . 1 268 93 93 PHE H H 8.881 . 1 269 93 93 PHE CA C 60.87 . 1 270 93 93 PHE CB C 39.35 . 1 271 93 93 PHE N N 123.81 . 1 272 94 94 GLU H H 8.664 . 1 273 94 94 GLU CA C 58.05 . 1 274 94 94 GLU CB C 28.44 . 1 275 94 94 GLU N N 116.95 . 1 276 95 95 ASP H H 7.917 . 1 277 95 95 ASP CA C 55.67 . 1 278 95 95 ASP CB C 40.63 . 1 279 95 95 ASP N N 118.78 . 1 280 96 96 SER H H 7.653 . 1 281 96 96 SER CA C 58.91 . 1 282 96 96 SER CB C 64.47 . 1 283 96 96 SER N N 112.76 . 1 284 97 97 ARG CA C 58.85 . 1 285 97 97 ARG CB C 28.23 . 1 286 98 98 GLY H H 7.982 . 1 287 98 98 GLY CA C 44.44 . 1 288 98 98 GLY N N 108.53 . 1 289 99 99 THR H H 7.634 . 1 290 99 99 THR CA C 60.00 . 1 291 99 99 THR CB C 72.78 . 1 292 99 99 THR N N 109.02 . 1 293 100 100 LEU H H 9.073 . 1 294 100 100 LEU CA C 56.16 . 1 295 100 100 LEU N N 124.28 . 1 296 101 101 PHE H H 7.865 . 1 297 101 101 PHE CA C 60.95 . 1 298 101 101 PHE N N 118.80 . 1 299 102 102 PHE H H 7.443 . 1 300 102 102 PHE C C 176.41 . 1 301 102 102 PHE CA C 60.77 . 1 302 102 102 PHE CB C 37.66 . 1 303 102 102 PHE N N 119.50 . 1 304 103 103 ASP H H 7.044 . 1 305 103 103 ASP C C 177.57 . 1 306 103 103 ASP CA C 57.92 . 1 307 103 103 ASP CB C 40.78 . 1 308 103 103 ASP N N 116.02 . 1 309 104 104 ILE H H 6.488 . 1 310 104 104 ILE CA C 65.08 . 1 311 104 104 ILE N N 116.64 . 1 312 105 105 ALA H H 7.487 . 1 313 105 105 ALA CA C 54.85 . 1 314 105 105 ALA CB C 16.72 . 1 315 105 105 ALA N N 121.62 . 1 316 106 106 ARG H H 8.384 . 1 317 106 106 ARG CA C 58.05 . 1 318 106 106 ARG CB C 27.80 . 1 319 106 106 ARG N N 116.39 . 1 320 123 123 ASN CA C 51.73 . 1 321 124 124 PHE H H 7.685 . 1 322 124 124 PHE CA C 62.06 . 1 323 124 124 PHE CB C 40.20 . 1 324 124 124 PHE N N 123.26 . 1 325 125 125 ALA H H 9.100 . 1 326 125 125 ALA CA C 53.70 . 1 327 125 125 ALA CB C 18.05 . 1 328 125 125 ALA N N 115.34 . 1 329 126 126 SER H H 7.501 . 1 330 126 126 SER CA C 56.85 . 1 331 126 126 SER CB C 63.66 . 1 332 126 126 SER N N 109.74 . 1 333 127 127 HIS H H 7.235 . 1 334 127 127 HIS CA C 59.18 . 1 335 127 127 HIS CB C 30.71 . 1 336 127 127 HIS N N 125.83 . 1 337 128 128 ASP H H 8.675 . 1 338 128 128 ASP CA C 54.57 . 1 339 128 128 ASP CB C 39.06 . 1 340 128 128 ASP N N 129.86 . 1 341 129 129 ASN H H 8.405 . 1 342 129 129 ASN CA C 54.27 . 1 343 129 129 ASN CB C 37.14 . 1 344 129 129 ASN N N 114.29 . 1 345 130 130 GLY H H 7.114 . 1 346 130 130 GLY CA C 44.67 . 1 347 130 130 GLY N N 105.83 . 1 348 131 131 ASN H H 8.013 . 1 349 131 131 ASN CA C 56.00 . 1 350 131 131 ASN CB C 38.67 . 1 351 131 131 ASN N N 119.85 . 1 352 132 132 THR H H 6.946 . 1 353 132 132 THR CA C 64.67 . 1 354 132 132 THR CB C 66.57 . 1 355 132 132 THR N N 117.16 . 1 356 133 133 LEU H H 9.069 . 1 357 133 133 LEU CA C 57.32 . 1 358 133 133 LEU CB C 39.64 . 1 359 133 133 LEU N N 122.19 . 1 360 134 134 GLU H H 7.164 . 1 361 134 134 GLU CA C 59.62 . 1 362 134 134 GLU CB C 28.62 . 1 363 134 134 GLU N N 118.22 . 1 364 135 135 VAL H H 8.054 . 1 365 135 135 VAL C C 179.83 . 1 366 135 135 VAL CA C 65.63 . 1 367 135 135 VAL CB C 30.63 . 1 368 135 135 VAL N N 118.65 . 1 369 136 136 VAL H H 7.557 . 1 370 136 136 VAL CA C 66.16 . 1 371 136 136 VAL CB C 30.60 . 1 372 136 136 VAL N N 123.83 . 1 373 146 146 SER CA C 56.53 . 1 374 146 146 SER CB C 64.51 . 1 375 147 147 PHE H H 8.187 . 1 376 147 147 PHE CA C 58.63 . 1 377 147 147 PHE CB C 42.24 . 1 378 147 147 PHE N N 119.39 . 1 379 148 148 HIS H H 8.034 . 1 380 148 148 HIS CA C 54.20 . 1 381 148 148 HIS CB C 31.14 . 1 382 148 148 HIS N N 128.55 . 1 383 149 149 ALA H H 8.890 . 1 384 149 149 ALA CA C 50.47 . 1 385 149 149 ALA CB C 22.38 . 1 386 149 149 ALA N N 125.33 . 1 387 150 150 LYS H H 8.228 . 1 388 150 150 LYS CA C 56.20 . 1 389 150 150 LYS CB C 34.59 . 1 390 150 150 LYS N N 122.51 . 1 391 151 151 VAL H H 8.422 . 1 392 151 151 VAL CA C 61.28 . 1 393 151 151 VAL CB C 30.71 . 1 394 151 151 VAL N N 127.10 . 1 395 152 152 LEU H H 8.593 . 1 396 152 152 LEU CA C 53.00 . 1 397 152 152 LEU CB C 43.35 . 1 398 152 152 LEU N N 125.87 . 1 399 153 153 ASN H H 10.275 . 1 400 153 153 ASN CA C 50.57 . 1 401 153 153 ASN CB C 39.71 . 1 402 153 153 ASN N N 127.23 . 1 403 154 154 ALA H H 7.832 . 1 404 154 154 ALA CA C 55.94 . 1 405 154 154 ALA CB C 18.04 . 1 406 154 154 ALA N N 130.91 . 1 407 155 155 LEU H H 6.775 . 1 408 155 155 LEU CA C 56.29 . 1 409 155 155 LEU CB C 39.80 . 1 410 155 155 LEU N N 113.75 . 1 411 156 156 ASP H H 7.660 . 1 412 156 156 ASP CA C 54.76 . 1 413 156 156 ASP CB C 42.12 . 1 414 156 156 ASP N N 120.81 . 1 415 157 157 TYR H H 7.462 . 1 416 157 157 TYR CA C 56.97 . 1 417 157 157 TYR CB C 38.01 . 1 418 157 157 TYR N N 116.68 . 1 419 158 158 GLY H H 9.156 . 1 420 158 158 GLY CA C 45.44 . 1 421 158 158 GLY N N 109.43 . 1 422 159 159 ILE H H 6.940 . 1 423 159 159 ILE CA C 52.38 . 1 424 159 159 ILE CB C 37.95 . 1 425 159 159 ILE N N 120.48 . 1 426 170 170 CYS CA C 54.80 . 1 427 170 170 CYS CB C 30.96 . 1 428 171 171 PHE H H 7.786 . 1 429 171 171 PHE CA C 56.01 . 1 430 171 171 PHE CB C 41.53 . 1 431 171 171 PHE N N 120.43 . 1 432 172 172 ARG CA C 57.55 . 1 433 172 172 ARG CB C 29.76 . 1 434 173 173 ASN H H 9.108 . 1 435 173 173 ASN CA C 55.99 . 1 436 173 173 ASN CB C 37.20 . 1 437 173 173 ASN N N 126.73 . 1 438 174 174 ASP H H 8.682 . 1 439 174 174 ASP CA C 54.87 . 1 440 174 174 ASP CB C 38.39 . 1 441 174 174 ASP N N 118.14 . 1 442 175 175 LEU H H 7.469 . 1 443 175 175 LEU CA C 55.06 . 1 444 175 175 LEU CB C 40.86 . 1 445 175 175 LEU N N 118.87 . 1 446 176 176 ASN H H 7.774 . 1 447 176 176 ASN CA C 53.30 . 1 448 176 176 ASN CB C 36.80 . 1 449 176 176 ASN N N 115.56 . 1 450 177 177 ILE H H 8.678 . 1 451 177 177 ILE CA C 59.41 . 1 452 177 177 ILE CB C 34.16 . 1 453 177 177 ILE N N 120.16 . 1 454 178 178 GLN H H 8.571 . 1 455 178 178 GLN CA C 55.09 . 1 456 178 178 GLN CB C 38.10 . 1 457 178 178 GLN N N 126.88 . 1 458 179 179 ASN H H 8.035 . 1 459 179 179 ASN CA C 52.21 . 1 460 179 179 ASN CB C 38.79 . 1 461 179 179 ASN N N 117.78 . 1 462 180 180 PHE H H 7.916 . 1 463 180 180 PHE CA C 58.73 . 1 464 180 180 PHE CB C 38.71 . 1 465 180 180 PHE N N 121.93 . 1 466 181 181 GLN H H 7.048 . 1 467 181 181 GLN CA C 52.60 . 1 468 181 181 GLN CB C 30.47 . 1 469 181 181 GLN N N 126.72 . 1 470 182 182 PHE H H 8.457 . 1 471 182 182 PHE CA C 57.85 . 1 472 182 182 PHE CB C 37.16 . 1 473 182 182 PHE N N 120.65 . 1 474 185 185 PRO CA C 61.67 . 1 475 185 185 PRO CB C 33.59 . 1 476 186 186 PHE H H 7.843 . 1 477 186 186 PHE CA C 54.94 . 1 478 186 186 PHE CB C 40.01 . 1 479 186 186 PHE N N 115.64 . 1 480 187 187 GLU H H 8.611 . 1 481 187 187 GLU CA C 56.85 . 1 482 187 187 GLU CB C 29.67 . 1 483 187 187 GLU N N 123.76 . 1 484 188 188 LEU H H 8.334 . 1 485 188 188 LEU CA C 55.24 . 1 486 188 188 LEU CB C 40.65 . 1 487 188 188 LEU N N 128.61 . 1 488 189 189 ASN H H 8.541 . 1 489 189 189 ASN CA C 52.05 . 1 490 189 189 ASN CB C 39.90 . 1 491 189 189 ASN N N 123.70 . 1 492 190 190 THR H H 6.300 . 1 493 190 190 THR CA C 61.25 . 1 494 190 190 THR CB C 71.06 . 1 495 190 190 THR N N 117.81 . 1 496 191 191 PHE H H 9.131 . 1 497 191 191 PHE CA C 57.23 . 1 498 191 191 PHE CB C 40.53 . 1 499 191 191 PHE N N 121.95 . 1 500 192 192 VAL H H 8.094 . 1 501 192 192 VAL CA C 68.70 . 1 502 192 192 VAL CB C 29.64 . 1 503 192 192 VAL N N 121.80 . 1 504 193 193 LYS H H 9.005 . 1 505 193 193 LYS CA C 57.39 . 1 506 193 193 LYS CB C 29.54 . 1 507 193 193 LYS N N 112.92 . 1 508 194 194 ASP H H 7.528 . 1 509 194 194 ASP CA C 56.21 . 1 510 194 194 ASP CB C 41.43 . 1 511 194 194 ASP N N 119.45 . 1 512 195 195 LEU H H 7.939 . 1 513 195 195 LEU CA C 53.44 . 1 514 195 195 LEU CB C 41.36 . 1 515 195 195 LEU N N 118.13 . 1 516 196 196 LEU H H 6.458 . 1 517 196 196 LEU CA C 54.37 . 1 518 196 196 LEU CB C 40.52 . 1 519 196 196 LEU N N 117.63 . 1 520 197 197 LEU H H 10.084 . 1 521 197 197 LEU CA C 52.73 . 1 522 197 197 LEU N N 125.76 . 1 523 198 198 PRO CA C 62.19 . 1 524 198 198 PRO CB C 31.43 . 1 525 199 199 ASP H H 8.474 . 1 526 199 199 ASP CA C 56.69 . 1 527 199 199 ASP CB C 39.77 . 1 528 199 199 ASP N N 122.06 . 1 529 200 200 SER H H 8.277 . 1 530 200 200 SER CA C 60.29 . 1 531 200 200 SER CB C 61.72 . 1 532 200 200 SER N N 112.71 . 1 533 201 201 GLU H H 7.744 . 1 534 201 201 GLU CA C 56.38 . 1 535 201 201 GLU CB C 30.57 . 1 536 201 201 GLU N N 119.92 . 1 537 202 202 VAL H H 7.258 . 1 538 202 202 VAL CA C 60.01 . 1 539 202 202 VAL CB C 32.18 . 1 540 202 202 VAL N N 107.33 . 1 541 203 203 GLU H H 7.637 . 1 542 203 203 GLU CA C 58.94 . 1 543 203 203 GLU CB C 28.83 . 1 544 203 203 GLU N N 123.01 . 1 545 204 204 HIS CA C 57.27 . 1 546 204 204 HIS CB C 28.58 . 1 547 205 205 LEU H H 7.659 . 1 548 205 205 LEU CA C 53.91 . 1 549 205 205 LEU CB C 40.98 . 1 550 205 205 LEU N N 121.88 . 1 551 206 206 VAL H H 7.029 . 1 552 206 206 VAL CA C 63.17 . 1 553 206 206 VAL CB C 31.50 . 1 554 206 206 VAL N N 121.08 . 1 555 207 207 ILE H H 8.554 . 1 556 207 207 ILE CA C 58.90 . 1 557 207 207 ILE CB C 39.43 . 1 558 207 207 ILE N N 129.05 . 1 559 208 208 ASP H H 8.611 . 1 560 208 208 ASP CA C 52.62 . 1 561 208 208 ASP CB C 41.13 . 1 562 208 208 ASP N N 127.88 . 1 563 209 209 ARG H H 8.872 . 1 564 209 209 ARG CB C 30.09 . 1 565 209 209 ARG N N 124.76 . 1 566 210 210 LYS CA C 56.51 . 1 567 210 210 LYS CB C 30.87 . 1 568 211 211 ASP H H 8.788 . 1 569 211 211 ASP CA C 52.20 . 1 570 211 211 ASP CB C 38.23 . 1 571 211 211 ASP N N 117.91 . 1 572 212 212 LEU H H 6.690 . 1 573 212 212 LEU CA C 55.33 . 1 574 212 212 LEU CB C 41.50 . 1 575 212 212 LEU N N 121.02 . 1 576 213 213 VAL H H 9.149 . 1 577 213 213 VAL CA C 61.26 . 1 578 213 213 VAL CB C 33.41 . 1 579 213 213 VAL N N 131.26 . 1 580 214 214 MET H H 8.584 . 1 581 214 214 MET CA C 53.09 . 1 582 214 214 MET CB C 29.09 . 1 583 214 214 MET N N 125.43 . 1 584 215 215 THR H H 8.964 . 1 585 215 215 THR CA C 61.76 . 1 586 215 215 THR CB C 68.76 . 1 587 215 215 THR N N 118.14 . 1 588 216 216 ASN H H 8.044 . 1 589 216 216 ASN CA C 51.96 . 1 590 216 216 ASN CB C 41.97 . 1 591 216 216 ASN N N 121.55 . 1 592 217 217 GLN H H 8.095 . 1 593 217 217 GLN CA C 54.49 . 1 594 217 217 GLN CB C 29.21 . 1 595 217 217 GLN N N 119.20 . 1 596 218 218 GLU H H 8.072 . 1 597 218 218 GLU CA C 55.60 . 1 598 218 218 GLU CB C 28.87 . 1 599 218 218 GLU N N 121.52 . 1 600 219 219 ILE H H 8.995 . 1 601 219 219 ILE CA C 60.24 . 1 602 219 219 ILE CB C 38.60 . 1 603 219 219 ILE N N 123.25 . 1 604 220 220 GLU H H 8.309 . 1 605 220 220 GLU CA C 56.85 . 1 606 220 220 GLU CB C 29.95 . 1 607 220 220 GLU N N 119.71 . 1 608 221 221 GLN H H 7.471 . 1 609 221 221 GLN CA C 53.64 . 1 610 221 221 GLN CB C 29.47 . 1 611 221 221 GLN N N 117.92 . 1 612 222 222 THR H H 7.561 . 1 613 222 222 THR CA C 59.62 . 1 614 222 222 THR CB C 68.35 . 1 615 222 222 THR N N 112.47 . 1 616 223 223 THR H H 7.637 . 1 617 223 223 THR CA C 57.04 . 1 618 223 223 THR CB C 70.69 . 1 619 223 223 THR N N 116.40 . 1 620 224 224 PRO CA C 61.57 . 1 621 224 224 PRO CB C 27.27 . 1 622 225 225 LYS H H 8.538 . 1 623 225 225 LYS CA C 54.43 . 1 624 225 225 LYS CB C 35.47 . 1 625 225 225 LYS N N 120.21 . 1 626 226 226 THR H H 8.530 . 1 627 226 226 THR CA C 59.78 . 1 628 226 226 THR CB C 68.73 . 1 629 226 226 THR N N 113.83 . 1 630 227 227 VAL H H 9.463 . 1 631 227 227 VAL CA C 61.17 . 1 632 227 227 VAL CB C 32.87 . 1 633 227 227 VAL N N 128.15 . 1 634 228 228 ARG H H 8.751 . 1 635 228 228 ARG CA C 56.00 . 1 636 228 228 ARG CB C 29.60 . 1 637 228 228 ARG N N 129.92 . 1 638 229 229 LEU H H 9.285 . 1 639 229 229 LEU CA C 54.43 . 1 640 229 229 LEU N N 126.62 . 1 641 230 230 GLY H H 7.406 . 1 642 230 230 GLY CA C 45.96 . 1 643 230 230 GLY N N 103.87 . 1 644 231 231 ILE H H 8.728 . 1 645 231 231 ILE CA C 58.83 . 1 646 231 231 ILE CB C 43.13 . 1 647 231 231 ILE N N 113.22 . 1 648 232 232 VAL H H 8.117 . 1 649 232 232 VAL CA C 58.40 . 1 650 232 232 VAL CB C 33.33 . 1 651 232 232 VAL N N 112.17 . 1 652 233 233 GLY H H 7.934 . 1 653 233 233 GLY CA C 46.93 . 1 654 233 233 GLY N N 108.76 . 1 655 234 234 LYS H H 8.480 . 1 656 234 234 LYS CA C 55.34 . 1 657 234 234 LYS CB C 31.46 . 1 658 234 234 LYS N N 124.89 . 1 659 235 235 GLY H H 8.726 . 1 660 235 235 GLY CA C 47.51 . 1 661 235 235 GLY N N 110.30 . 1 662 236 236 GLY H H 9.162 . 1 663 236 236 GLY CA C 43.53 . 1 664 236 236 GLY N N 110.93 . 1 665 237 237 GLN H H 8.488 . 1 666 237 237 GLN CA C 57.73 . 1 667 237 237 GLN CB C 27.58 . 1 668 237 237 GLN N N 120.47 . 1 669 238 238 GLY H H 8.925 . 1 670 238 238 GLY CA C 45.54 . 1 671 238 238 GLY N N 114.05 . 1 672 239 239 GLU H H 8.053 . 1 673 239 239 GLU CA C 54.31 . 1 674 239 239 GLU N N 118.10 . 1 675 240 240 ARG H H 7.968 . 1 676 240 240 ARG CA C 54.91 . 1 677 240 240 ARG CB C 33.83 . 1 678 240 240 ARG N N 118.57 . 1 679 241 241 ILE H H 7.993 . 1 680 241 241 ILE CA C 57.99 . 1 681 241 241 ILE CB C 38.18 . 1 682 241 241 ILE N N 121.37 . 1 683 242 242 TYR H H 8.739 . 1 684 242 242 TYR CA C 57.06 . 1 685 242 242 TYR CB C 40.40 . 1 686 242 242 TYR N N 127.66 . 1 687 243 243 SER H H 8.547 . 1 688 243 243 SER CA C 57.13 . 1 689 243 243 SER CB C 62.94 . 1 690 243 243 SER N N 111.17 . 1 691 246 246 GLY H H 6.635 . 1 692 246 246 GLY CA C 44.10 . 1 693 246 246 GLY N N 104.63 . 1 694 247 247 ILE H H 7.276 . 1 695 247 247 ILE CA C 58.16 . 1 696 247 247 ILE CB C 38.46 . 1 697 247 247 ILE N N 112.12 . 1 698 248 248 ALA H H 7.900 . 1 699 248 248 ALA CA C 51.02 . 1 700 248 248 ALA CB C 17.65 . 1 701 248 248 ALA N N 122.67 . 1 702 249 249 ILE H H 6.844 . 1 703 249 249 ILE CA C 58.97 . 1 704 249 249 ILE N N 115.09 . 1 705 250 250 THR H H 7.071 . 1 706 250 250 THR CA C 62.32 . 1 707 250 250 THR CB C 69.57 . 1 708 250 250 THR N N 115.22 . 1 709 251 251 LEU H H 7.845 . 1 710 251 251 LEU CA C 55.39 . 1 711 251 251 LEU CB C 40.25 . 1 712 251 251 LEU N N 128.18 . 1 713 252 252 SER H H 8.289 . 1 714 252 252 SER CA C 55.77 . 1 715 252 252 SER CB C 65.03 . 1 716 252 252 SER N N 116.89 . 1 717 253 253 ALA H H 8.453 . 1 718 253 253 ALA CA C 52.20 . 1 719 253 253 ALA CB C 19.27 . 1 720 253 253 ALA N N 124.08 . 1 721 254 254 TYR H H 7.898 . 1 722 254 254 TYR CA C 56.14 . 1 723 254 254 TYR CB C 39.90 . 1 724 254 254 TYR N N 116.73 . 1 725 255 255 GLY CA C 44.62 . 1 726 256 256 GLY H H 8.052 . 1 727 256 256 GLY CA C 43.68 . 1 728 256 256 GLY N N 109.59 . 1 729 257 257 GLY H H 8.003 . 1 730 257 257 GLY CA C 43.41 . 1 731 257 257 GLY N N 107.17 . 1 732 258 258 ILE H H 7.659 . 1 733 258 258 ILE CA C 62.25 . 1 734 258 258 ILE CB C 36.93 . 1 735 258 258 ILE N N 121.27 . 1 736 259 259 PHE H H 8.931 . 1 737 259 259 PHE CA C 54.77 . 1 738 259 259 PHE CB C 36.08 . 1 739 259 259 PHE N N 120.51 . 1 740 260 260 ALA CA C 53.16 . 1 741 260 260 ALA CB C 19.60 . 1 742 261 261 LYS H H 8.589 . 1 743 261 261 LYS CA C 60.36 . 1 744 261 261 LYS N N 115.15 . 1 745 262 262 THR H H 8.076 . 1 746 262 262 THR CA C 61.28 . 1 747 262 262 THR CB C 70.18 . 1 748 262 262 THR N N 106.37 . 1 749 263 263 GLY H H 7.453 . 1 750 263 263 GLY CA C 44.36 . 1 751 263 263 GLY N N 109.13 . 1 752 264 264 GLY H H 6.474 . 1 753 264 264 GLY CA C 42.84 . 1 754 264 264 GLY N N 103.90 . 1 755 265 265 TYR H H 8.478 . 1 756 265 265 TYR CA C 56.71 . 1 757 265 265 TYR CB C 41.64 . 1 758 265 265 TYR N N 119.00 . 1 759 266 266 LEU H H 7.271 . 1 760 266 266 LEU CA C 52.95 . 1 761 266 266 LEU CB C 41.70 . 1 762 266 266 LEU N N 123.45 . 1 763 267 267 VAL H H 9.295 . 1 764 267 267 VAL CA C 60.88 . 1 765 267 267 VAL CB C 32.10 . 1 766 267 267 VAL N N 129.62 . 1 767 268 268 ASN H H 9.426 . 1 768 268 268 ASN CA C 53.71 . 1 769 268 268 ASN CB C 36.86 . 1 770 268 268 ASN N N 128.08 . 1 771 269 269 GLY H H 8.274 . 1 772 269 269 GLY CA C 45.01 . 1 773 269 269 GLY N N 102.6 . 1 774 270 270 LYS H H 7.676 . 1 775 270 270 LYS CA C 53.81 . 1 776 270 270 LYS CB C 33.89 . 1 777 270 270 LYS N N 121.68 . 1 778 271 271 THR H H 8.788 . 1 779 271 271 THR CA C 58.21 . 1 780 271 271 THR CB C 69.42 . 1 781 271 271 THR N N 111.75 . 1 782 272 272 ARG H H 8.777 . 1 783 272 272 ARG CA C 53.65 . 1 784 272 272 ARG CB C 34.59 . 1 785 272 272 ARG N N 119.35 . 1 786 273 273 LYS H H 7.358 . 1 787 273 273 LYS CB C 33.47 . 1 788 273 273 LYS N N 117.85 . 1 789 278 278 GLU CA C 58.54 . 1 790 278 278 GLU CB C 25.16 . 1 791 279 279 CYS H H 7.949 . 1 792 279 279 CYS CA C 62.63 . 1 793 279 279 CYS N N 117.03 . 1 794 280 280 ALA H H 7.328 . 1 795 280 280 ALA CA C 54.27 . 1 796 280 280 ALA CB C 16.63 . 1 797 280 280 ALA N N 121.04 . 1 798 281 281 ARG H H 7.764 . 1 799 281 281 ARG CA C 59.82 . 1 800 281 281 ARG N N 119.52 . 1 801 282 282 VAL H H 8.237 . 1 802 282 282 VAL CA C 63.98 . 1 803 282 282 VAL CB C 30.58 . 1 804 282 282 VAL N N 120.29 . 1 805 283 283 MET H H 6.976 . 1 806 283 283 MET CA C 52.88 . 1 807 283 283 MET CB C 30.80 . 1 808 283 283 MET N N 114.66 . 1 809 284 284 GLY H H 7.941 . 1 810 284 284 GLY CA C 45.18 . 1 811 284 284 GLY N N 106.86 . 1 812 285 285 TYR H H 8.943 . 1 813 285 285 TYR CA C 57.39 . 1 814 285 285 TYR CB C 36.19 . 1 815 285 285 TYR N N 123.65 . 1 816 286 286 PRO CA C 61.56 . 1 817 286 286 PRO CB C 31.69 . 1 818 287 287 ASP H H 8.908 . 1 819 287 287 ASP CA C 55.74 . 1 820 287 287 ASP CB C 38.49 . 1 821 287 287 ASP N N 121.23 . 1 822 288 288 SER H H 7.407 . 1 823 288 288 SER CA C 57.90 . 1 824 288 288 SER CB C 62.25 . 1 825 288 288 SER N N 110.50 . 1 826 289 289 TYR H H 8.001 . 1 827 289 289 TYR CA C 58.24 . 1 828 289 289 TYR CB C 38.95 . 1 829 289 289 TYR N N 127.43 . 1 830 290 290 LYS H H 9.366 . 1 831 290 290 LYS CA C 56.05 . 1 832 290 290 LYS CB C 31.86 . 1 833 290 290 LYS N N 134.15 . 1 834 291 291 VAL H H 7.424 . 1 835 291 291 VAL CA C 59.61 . 1 836 291 291 VAL CB C 32.15 . 1 837 291 291 VAL N N 115.22 . 1 838 292 292 HIS H H 8.402 . 1 839 292 292 HIS CA C 57.99 . 1 840 292 292 HIS CB C 30.52 . 1 841 292 292 HIS N N 124.35 . 1 842 293 293 PRO CA C 63.74 . 1 843 293 293 PRO CB C 31.27 . 1 844 294 294 SER H H 10.661 . 1 845 294 294 SER CA C 56.00 . 1 846 294 294 SER CB C 61.10 . 1 847 294 294 SER N N 119.71 . 1 848 295 295 THR H H 8.632 . 1 849 295 295 THR CA C 65.95 . 1 850 295 295 THR CB C 67.71 . 1 851 295 295 THR N N 127.67 . 1 852 296 296 SER H H 8.132 . 1 853 296 296 SER CA C 61.06 . 1 854 296 296 SER CB C 61.67 . 1 855 296 296 SER N N 114.01 . 1 856 297 297 GLN H H 7.251 . 1 857 297 297 GLN CA C 56.78 . 1 858 297 297 GLN CB C 26.03 . 1 859 297 297 GLN N N 121.63 . 1 860 298 298 ALA H H 8.537 . 1 861 298 298 ALA CA C 54.95 . 1 862 298 298 ALA CB C 16.90 . 1 863 298 298 ALA N N 122.69 . 1 864 299 299 TYR H H 8.209 . 1 865 299 299 TYR CA C 59.28 . 1 866 299 299 TYR CB C 37.00 . 1 867 299 299 TYR N N 115.03 . 1 868 300 300 LYS H H 7.160 . 1 869 300 300 LYS CA C 59.34 . 1 870 300 300 LYS CB C 31.65 . 1 871 300 300 LYS N N 119.77 . 1 872 301 301 GLN H H 8.363 . 1 873 301 301 GLN CA C 57.98 . 1 874 301 301 GLN CB C 26.24 . 1 875 301 301 GLN N N 117.03 . 1 876 302 302 PHE H H 8.714 . 1 877 302 302 PHE CA C 63.33 . 1 878 302 302 PHE CB C 37.24 . 1 879 302 302 PHE N N 116.92 . 1 880 303 303 GLY H H 7.936 . 1 881 303 303 GLY CA C 46.53 . 1 882 303 303 GLY N N 104.80 . 1 883 304 304 ASN H H 7.080 . 1 884 304 304 ASN CA C 51.47 . 1 885 304 304 ASN CB C 40.08 . 1 886 304 304 ASN N N 117.68 . 1 887 305 305 SER H H 6.973 . 1 888 305 305 SER CA C 55.04 . 1 889 305 305 SER CB C 63.90 . 1 890 305 305 SER N N 112.38 . 1 891 306 306 VAL CA C 57.95 . 1 892 306 306 VAL CB C 33.19 . 1 893 307 307 VAL H H 7.803 . 1 894 307 307 VAL CA C 59.58 . 1 895 307 307 VAL CB C 29.97 . 1 896 307 307 VAL N N 117.59 . 1 897 308 308 ILE H H 8.191 . 1 898 308 308 ILE CA C 63.52 . 1 899 308 308 ILE CB C 35.06 . 1 900 308 308 ILE N N 127.15 . 1 901 309 309 ASN H H 8.053 . 1 902 309 309 ASN CA C 56.81 . 1 903 309 309 ASN CB C 36.21 . 1 904 309 309 ASN N N 111.95 . 1 905 310 310 VAL H H 6.395 . 1 906 310 310 VAL CA C 66.23 . 1 907 310 310 VAL CB C 31.22 . 1 908 310 310 VAL N N 112.71 . 1 909 311 311 LEU H H 6.781 . 1 910 311 311 LEU CA C 57.62 . 1 911 311 311 LEU CB C 41.09 . 1 912 311 311 LEU N N 115.00 . 1 913 312 312 GLN H H 8.203 . 1 914 312 312 GLN CA C 60.39 . 1 915 312 312 GLN CB C 30.57 . 1 916 312 312 GLN N N 117.15 . 1 917 313 313 TYR H H 7.559 . 1 918 313 313 TYR CA C 61.79 . 1 919 313 313 TYR CB C 36.92 . 1 920 313 313 TYR N N 116.22 . 1 921 314 314 ILE H H 7.837 . 1 922 314 314 ILE CA C 66.13 . 1 923 314 314 ILE CB C 36.87 . 1 924 314 314 ILE N N 118.19 . 1 925 315 315 ALA H H 9.032 . 1 926 315 315 ALA CA C 54.91 . 1 927 315 315 ALA CB C 17.25 . 1 928 315 315 ALA N N 122.86 . 1 929 316 316 TYR H H 8.469 . 1 930 316 316 TYR CA C 62.29 . 1 931 316 316 TYR CB C 37.46 . 1 932 316 316 TYR N N 119.32 . 1 933 317 317 ASN H H 7.448 . 1 934 317 317 ASN CA C 55.39 . 1 935 317 317 ASN CB C 36.13 . 1 936 317 317 ASN N N 121.95 . 1 937 318 318 ILE H H 8.873 . 1 938 318 318 ILE CA C 66.37 . 1 939 318 318 ILE CB C 36.82 . 1 940 318 318 ILE N N 124.79 . 1 941 319 319 GLY H H 8.118 . 1 942 319 319 GLY CA C 47.92 . 1 943 319 319 GLY N N 106.64 . 1 944 320 320 SER H H 8.326 . 1 945 320 320 SER CA C 60.79 . 1 946 320 320 SER CB C 62.12 . 1 947 320 320 SER N N 117.94 . 1 948 322 322 LEU H H 7.863 . 1 949 322 322 LEU CA C 56.43 . 1 950 322 322 LEU CB C 41.15 . 1 951 322 322 LEU N N 120.16 . 1 952 323 323 ASN H H 7.712 . 1 953 323 323 ASN CA C 53.51 . 1 954 323 323 ASN CB C 38.12 . 1 955 323 323 ASN N N 116.03 . 1 956 324 324 LEU H H 7.811 . 1 957 324 324 LEU CA C 56.00 . 1 958 324 324 LEU CB C 41.01 . 1 959 324 324 LEU N N 121.95 . 1 960 325 325 GLU H H 8.035 . 1 961 325 325 GLU CA C 56.50 . 1 962 325 325 GLU CB C 28.96 . 1 963 325 325 GLU N N 119.71 . 1 964 326 326 HIS H H 7.988 . 1 965 326 326 HIS CA C 55.54 . 1 966 326 326 HIS CB C 29.02 . 1 967 326 326 HIS N N 119.20 . 1 stop_ save_