data_16395 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Assignments of M.HhaI bound with hemimethylated DNA ; _BMRB_accession_number 16395 _BMRB_flat_file_name bmr16395.str _Entry_type original _Submission_date 2009-07-07 _Accession_date 2009-07-07 _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 Murdy Matthew . . 3 Dahlquist Frederick . . 4 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" 276 "13C chemical shifts" 557 "15N chemical shifts" 276 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2009-09-04 original author . stop_ _Original_release_date 2009-09-04 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title 'The recognition Pathway for the DNA Cytosine Methyltransferase M.HhaI' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 19580326 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Zhou Hongjun . . 2 Murdy Matthew M. . 3 Dahlquist Frederick W. . 4 Reich Norbert O. . stop_ _Journal_abbreviation Biochemistry _Journal_volume 48 _Journal_issue 33 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 7807 _Page_last 7816 _Year 2009 _Details . loop_ _Keyword methyltransferase M.HhaI NMR stop_ save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name 'M.HhaI-DNA-cofactor ternary complex' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label protein $M.HhaI 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 15170 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_ #################### # 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 Eubacteria . 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 _Isotopic_labeling $M.HhaI 0.5 mM '[U-13C; U-15N; U-2H]' H2O 90 % 'natural abundance' D2O 10 % 'natural abundance' NaCl 100 mM 'natural abundance' NaPi 50 mM 'natural abundance' glycerol 0.75 % 'natural abundance' arg 50 mM 'natural abundance' Glu 50 mM 'natural abundance' stop_ save_ ############################ # Computer software used # ############################ save_ANSIG _Saveframe_category software _Name ANSIG _Version . loop_ _Vendor _Address _Electronic_address Kraulis . . stop_ loop_ _Task 'chemical shift assignment' stop_ _Details . save_ 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_ ######################### # 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_ ####################### # Sample conditions # ####################### save_sample_conditions_1 _Saveframe_category sample_conditions _Details '50 mM NaPi, 100 mM NaCl, 0.75% glycerol, 50 mM arg, 50mM Glu, pH 6.5' loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units 'ionic strength' 100 . mM 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 DSS C 13 'methyl protons' ppm 0 external indirect . . . 0.251449530 DSS H 1 'methyl protons' ppm 0 external direct . . . 1.000000000 DSS 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' 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 protein _Text_data_format . _Text_data . loop_ _Atom_shift_assign_ID _Residue_author_seq_code _Residue_seq_code _Residue_label _Atom_name _Atom_type _Chem_shift_value _Chem_shift_value_error _Chem_shift_ambiguity_code 1 1 1 MET CA C 54.87 . 1 2 1 1 MET CB C 33.14 . 1 3 2 2 ILE H H 9.258 . 1 4 2 2 ILE CA C 59.19 . 1 5 2 2 ILE CB C 39.53 . 1 6 2 2 ILE N N 119.53 . 1 7 3 3 GLU H H 8.385 . 1 8 3 3 GLU CA C 55.24 . 1 9 3 3 GLU CB C 29.55 . 1 10 3 3 GLU N N 122.82 . 1 11 4 4 ILE H H 8.664 . 1 12 4 4 ILE CA C 58.36 . 1 13 4 4 ILE CB C 36.12 . 1 14 4 4 ILE N N 128.60 . 1 15 5 5 LYS H H 8.532 . 1 16 5 5 LYS CA C 57.36 . 1 17 5 5 LYS CB C 31.93 . 1 18 5 5 LYS N N 127.57 . 1 19 6 6 ASP H H 7.854 . 1 20 6 6 ASP CA C 52.42 . 1 21 6 6 ASP CB C 40.24 . 1 22 6 6 ASP N N 119.32 . 1 23 7 7 LYS H H 8.341 . 1 24 7 7 LYS CA C 55.53 . 1 25 7 7 LYS CB C 29.48 . 1 26 7 7 LYS N N 124.01 . 1 27 8 8 GLN H H 8.149 . 1 28 8 8 GLN CA C 57.01 . 1 29 8 8 GLN CB C 29.49 . 1 30 8 8 GLN N N 122.11 . 1 31 9 9 LEU H H 8.183 . 1 32 9 9 LEU CA C 52.77 . 1 33 9 9 LEU CB C 40.65 . 1 34 9 9 LEU N N 114.61 . 1 35 10 10 THR H H 7.158 . 1 36 10 10 THR CA C 64.81 . 1 37 10 10 THR CB C 68.66 . 1 38 10 10 THR N N 115.90 . 1 39 11 11 GLY H H 8.789 . 1 40 11 11 GLY CA C 44.63 . 1 41 11 11 GLY N N 116.49 . 1 42 12 12 LEU H H 7.958 . 1 43 12 12 LEU CA C 53.66 . 1 44 12 12 LEU CB C 41.62 . 1 45 12 12 LEU N N 120.49 . 1 46 13 13 ARG H H 9.951 . 1 47 13 13 ARG CA C 53.69 . 1 48 13 13 ARG CB C 32.75 . 1 49 13 13 ARG N N 122.16 . 1 50 14 14 PHE H H 9.811 . 1 51 14 14 PHE CA C 54.39 . 1 52 14 14 PHE CB C 44.26 . 1 53 14 14 PHE N N 122.88 . 1 54 15 15 ILE H H 8.031 . 1 55 15 15 ILE CA C 58.15 . 1 56 15 15 ILE CB C 39.11 . 1 57 15 15 ILE N N 111.22 . 1 58 16 16 ASP H H 8.613 . 1 59 16 16 ASP CA C 51.62 . 1 60 16 16 ASP CB C 42.33 . 1 61 16 16 ASP N N 128.51 . 1 62 17 17 LEU CA C 53.54 . 1 63 17 17 LEU CB C 40.81 . 1 64 18 18 PHE H H 8.590 . 1 65 18 18 PHE CA C 58.08 . 1 66 18 18 PHE CB C 34.77 . 1 67 18 18 PHE N N 122.78 . 1 68 19 19 ALA H H 8.676 . 1 69 19 19 ALA CA C 56.37 . 1 70 19 19 ALA CB C 19.16 . 1 71 19 19 ALA N N 120.26 . 1 72 20 20 GLY H H 9.771 . 1 73 20 20 GLY CA C 47.00 . 1 74 20 20 GLY N N 109.55 . 1 75 21 21 LEU H H 7.853 . 1 76 21 21 LEU CA C 54.66 . 1 77 21 21 LEU CB C 42.70 . 1 78 21 21 LEU N N 122.83 . 1 79 22 22 GLY H H 9.451 . 1 80 22 22 GLY CA C 46.51 . 1 81 22 22 GLY N N 104.90 . 1 82 23 23 GLY H H 7.941 . 1 83 23 23 GLY CA C 48.46 . 1 84 23 23 GLY N N 111.78 . 1 85 24 24 PHE H H 9.316 . 1 86 24 24 PHE CA C 61.66 . 1 87 24 24 PHE CB C 37.26 . 1 88 24 24 PHE N N 116.96 . 1 89 25 25 ARG H H 6.530 . 1 90 25 25 ARG CA C 58.43 . 1 91 25 25 ARG CB C 28.10 . 1 92 25 25 ARG N N 120.01 . 1 93 26 26 LEU H H 8.584 . 1 94 26 26 LEU CA C 57.42 . 1 95 26 26 LEU CB C 41.75 . 1 96 26 26 LEU N N 118.56 . 1 97 27 27 ALA H H 7.557 . 1 98 27 27 ALA CA C 54.52 . 1 99 27 27 ALA CB C 18.75 . 1 100 27 27 ALA N N 118.18 . 1 101 28 28 LEU H H 8.569 . 1 102 28 28 LEU CA C 59.24 . 1 103 28 28 LEU N N 121.95 . 1 104 31 31 CYS H H 6.795 . 1 105 31 31 CYS CA C 59.04 . 1 106 31 31 CYS CB C 28.27 . 1 107 31 31 CYS N N 115.64 . 1 108 32 32 GLY H H 7.997 . 1 109 32 32 GLY CA C 44.44 . 1 110 32 32 GLY N N 108.64 . 1 111 33 33 ALA H H 7.248 . 1 112 33 33 ALA CA C 51.56 . 1 113 33 33 ALA CB C 19.84 . 1 114 33 33 ALA N N 122.99 . 1 115 34 34 GLU H H 8.707 . 1 116 34 34 GLU CA C 53.95 . 1 117 34 34 GLU CB C 32.42 . 1 118 34 34 GLU N N 119.59 . 1 119 35 35 CYS H H 9.720 . 1 120 35 35 CYS CA C 57.89 . 1 121 35 35 CYS CB C 26.90 . 1 122 35 35 CYS N N 130.13 . 1 123 36 36 VAL H H 8.440 . 1 124 36 36 VAL CA C 59.98 . 1 125 36 36 VAL CB C 31.90 . 1 126 36 36 VAL N N 119.84 . 1 127 37 37 TYR H H 7.362 . 1 128 37 37 TYR CA C 59.25 . 1 129 37 37 TYR CB C 39.89 . 1 130 37 37 TYR N N 121.37 . 1 131 38 38 SER H H 7.327 . 1 132 38 38 SER CA C 56.18 . 1 133 38 38 SER CB C 66.25 . 1 134 38 38 SER N N 122.01 . 1 135 39 39 ASN H H 7.729 . 1 136 39 39 ASN CA C 53.15 . 1 137 39 39 ASN CB C 43.87 . 1 138 39 39 ASN N N 119.81 . 1 139 40 40 GLU H H 9.044 . 1 140 40 40 GLU CA C 55.75 . 1 141 40 40 GLU CB C 31.93 . 1 142 40 40 GLU N N 129.06 . 1 143 41 41 TRP H H 7.853 . 1 144 41 41 TRP CA C 55.12 . 1 145 41 41 TRP CB C 29.10 . 1 146 41 41 TRP N N 125.55 . 1 147 42 42 ASP H H 10.391 . 1 148 42 42 ASP CA C 54.26 . 1 149 42 42 ASP CB C 42.60 . 1 150 42 42 ASP N N 129.30 . 1 151 43 43 LYS H H 8.614 . 1 152 43 43 LYS CA C 58.50 . 1 153 43 43 LYS CB C 31.30 . 1 154 43 43 LYS N N 127.68 . 1 155 44 44 TYR H H 7.119 . 1 156 44 44 TYR CA C 59.33 . 1 157 44 44 TYR CB C 35.31 . 1 158 44 44 TYR N N 118.99 . 1 159 45 45 ALA H H 9.091 . 1 160 45 45 ALA CA C 54.25 . 1 161 45 45 ALA CB C 16.08 . 1 162 45 45 ALA N N 126.75 . 1 163 46 46 GLN H H 8.723 . 1 164 46 46 GLN CA C 59.39 . 1 165 46 46 GLN CB C 27.24 . 1 166 46 46 GLN N N 116.34 . 1 167 47 47 GLU H H 7.517 . 1 168 47 47 GLU CA C 59.00 . 1 169 47 47 GLU CB C 29.25 . 1 170 47 47 GLU N N 117.88 . 1 171 48 48 VAL H H 8.013 . 1 172 48 48 VAL CA C 64.00 . 1 173 48 48 VAL CB C 31.96 . 1 174 48 48 VAL N N 121.21 . 1 175 49 49 TYR H H 8.899 . 1 176 49 49 TYR CA C 62.20 . 1 177 49 49 TYR CB C 38.51 . 1 178 49 49 TYR N N 130.24 . 1 179 50 50 GLU H H 8.524 . 1 180 50 50 GLU CA C 59.44 . 1 181 50 50 GLU CB C 28.70 . 1 182 50 50 GLU N N 121.20 . 1 183 51 51 MET H H 8.127 . 1 184 51 51 MET CA C 58.61 . 1 185 51 51 MET CB C 32.99 . 1 186 51 51 MET N N 119.42 . 1 187 52 52 ASN H H 7.172 . 1 188 52 52 ASN CA C 55.52 . 1 189 52 52 ASN CB C 40.55 . 1 190 52 52 ASN N N 114.17 . 1 191 53 53 PHE H H 8.785 . 1 192 53 53 PHE CA C 57.64 . 1 193 53 53 PHE CB C 39.28 . 1 194 53 53 PHE N N 116.06 . 1 195 54 54 GLY H H 8.292 . 1 196 54 54 GLY CA C 45.72 . 1 197 54 54 GLY N N 108.46 . 1 198 55 55 GLU H H 6.859 . 1 199 55 55 GLU CA C 53.33 . 1 200 55 55 GLU CB C 32.55 . 1 201 55 55 GLU N N 116.00 . 1 202 56 56 LYS H H 8.498 . 1 203 56 56 LYS CA C 52.82 . 1 204 56 56 LYS CB C 32.75 . 1 205 56 56 LYS N N 122.53 . 1 206 57 57 PRO CA C 62.21 . 1 207 57 57 PRO CB C 32.91 . 1 208 58 58 GLU H H 7.150 . 1 209 58 58 GLU CA C 56.03 . 1 210 58 58 GLU CB C 29.25 . 1 211 58 58 GLU N N 121.44 . 1 212 59 59 GLY H H 7.711 . 1 213 59 59 GLY CA C 43.49 . 1 214 59 59 GLY N N 106.71 . 1 215 60 60 ASP H H 7.592 . 1 216 60 60 ASP CA C 54.02 . 1 217 60 60 ASP CB C 41.79 . 1 218 60 60 ASP N N 110.58 . 1 219 61 61 ILE H H 9.602 . 1 220 61 61 ILE CA C 60.85 . 1 221 61 61 ILE CB C 36.48 . 1 222 61 61 ILE N N 105.32 . 1 223 62 62 THR H H 8.448 . 1 224 62 62 THR CA C 63.78 . 1 225 62 62 THR CB C 68.68 . 1 226 62 62 THR N N 113.91 . 1 227 63 63 GLN H H 7.596 . 1 228 63 63 GLN CA C 53.66 . 1 229 63 63 GLN CB C 28.83 . 1 230 63 63 GLN N N 118.15 . 1 231 64 64 VAL H H 7.147 . 1 232 64 64 VAL CA C 61.82 . 1 233 64 64 VAL CB C 32.23 . 1 234 64 64 VAL N N 123.16 . 1 235 65 65 ASN H H 8.962 . 1 236 65 65 ASN CA C 53.05 . 1 237 65 65 ASN CB C 37.85 . 1 238 65 65 ASN N N 127.46 . 1 239 66 66 GLU H H 10.448 . 1 240 66 66 GLU CA C 58.37 . 1 241 66 66 GLU CB C 27.60 . 1 242 66 66 GLU N N 131.04 . 1 243 67 67 LYS H H 8.050 . 1 244 67 67 LYS CA C 58.50 . 1 245 67 67 LYS CB C 31.36 . 1 246 67 67 LYS N N 118.56 . 1 247 68 68 THR H H 7.843 . 1 248 68 68 THR CA C 61.38 . 1 249 68 68 THR CB C 69.21 . 1 250 68 68 THR N N 107.97 . 1 251 69 69 ILE H H 6.612 . 1 252 69 69 ILE CA C 57.61 . 1 253 69 69 ILE CB C 36.73 . 1 254 69 69 ILE N N 126.33 . 1 255 70 70 PRO CA C 62.23 . 1 256 70 70 PRO CB C 31.70 . 1 257 71 71 ASP H H 8.576 . 1 258 71 71 ASP CA C 54.85 . 1 259 71 71 ASP CB C 39.38 . 1 260 71 71 ASP N N 122.91 . 1 261 72 72 HIS H H 8.046 . 1 262 72 72 HIS CA C 55.74 . 1 263 72 72 HIS CB C 29.63 . 1 264 72 72 HIS N N 115.49 . 1 265 73 73 ASP H H 8.310 . 1 266 73 73 ASP CA C 55.95 . 1 267 73 73 ASP CB C 45.01 . 1 268 73 73 ASP N N 116.48 . 1 269 76 76 CYS CA C 57.34 . 1 270 76 76 CYS CB C 29.34 . 1 271 77 77 ALA H H 7.899 . 1 272 77 77 ALA CA C 52.82 . 1 273 77 77 ALA CB C 22.06 . 1 274 77 77 ALA N N 120.74 . 1 275 78 78 GLY H H 9.238 . 1 276 78 78 GLY CA C 46.75 . 1 277 78 78 GLY N N 121.21 . 1 278 79 79 PHE H H 6.152 . 1 279 79 79 PHE CA C 54.08 . 1 280 79 79 PHE CB C 36.10 . 1 281 79 79 PHE N N 112.13 . 1 282 82 82 GLN CA C 60.72 . 1 283 82 82 GLN CB C 27.84 . 1 284 83 83 ALA H H 8.963 . 1 285 83 83 ALA CA C 52.15 . 1 286 83 83 ALA CB C 17.45 . 1 287 83 83 ALA N N 118.88 . 1 288 84 84 PHE H H 6.793 . 1 289 84 84 PHE CA C 55.80 . 1 290 84 84 PHE CB C 41.56 . 1 291 84 84 PHE N N 111.03 . 1 292 85 85 SER H H 6.872 . 1 293 85 85 SER CA C 57.63 . 1 294 85 85 SER CB C 62.78 . 1 295 85 85 SER N N 109.50 . 1 296 86 86 ILE H H 8.961 . 1 297 86 86 ILE CA C 61.67 . 1 298 86 86 ILE CB C 38.63 . 1 299 86 86 ILE N N 104.99 . 1 300 87 87 SER H H 8.161 . 1 301 87 87 SER CA C 56.29 . 1 302 87 87 SER CB C 63.55 . 1 303 87 87 SER N N 113.94 . 1 304 88 88 GLY H H 6.968 . 1 305 88 88 GLY CA C 43.61 . 1 306 88 88 GLY N N 103.94 . 1 307 90 90 GLN CA C 57.25 . 1 308 90 90 GLN CB C 27.07 . 1 309 91 91 LYS H H 8.803 . 1 310 91 91 LYS CA C 57.06 . 1 311 91 91 LYS CB C 30.81 . 1 312 91 91 LYS N N 118.92 . 1 313 92 92 GLY H H 8.190 . 1 314 92 92 GLY CA C 46.45 . 1 315 92 92 GLY N N 108.44 . 1 316 93 93 PHE H H 9.344 . 1 317 93 93 PHE CA C 57.91 . 1 318 93 93 PHE CB C 37.49 . 1 319 93 93 PHE N N 125.12 . 1 320 94 94 GLU H H 7.678 . 1 321 94 94 GLU CA C 56.12 . 1 322 94 94 GLU CB C 28.92 . 1 323 94 94 GLU N N 115.60 . 1 324 95 95 ASP H H 7.505 . 1 325 95 95 ASP CA C 52.12 . 1 326 95 95 ASP CB C 44.94 . 1 327 95 95 ASP N N 122.96 . 1 328 96 96 SER CA C 61.60 . 1 329 97 97 ARG H H 9.745 . 1 330 97 97 ARG CA C 55.02 . 1 331 97 97 ARG CB C 27.89 . 1 332 97 97 ARG N N 121.63 . 1 333 98 98 GLY H H 9.059 . 1 334 98 98 GLY CA C 44.66 . 1 335 98 98 GLY N N 112.01 . 1 336 99 99 THR H H 7.470 . 1 337 99 99 THR CA C 61.63 . 1 338 99 99 THR CB C 68.77 . 1 339 99 99 THR N N 107.66 . 1 340 100 100 LEU H H 6.526 . 1 341 100 100 LEU CA C 55.05 . 1 342 100 100 LEU CB C 39.32 . 1 343 100 100 LEU N N 125.87 . 1 344 101 101 PHE H H 9.458 . 1 345 101 101 PHE CA C 60.41 . 1 346 101 101 PHE CB C 38.22 . 1 347 101 101 PHE N N 120.39 . 1 348 102 102 PHE H H 7.613 . 1 349 102 102 PHE CA C 60.40 . 1 350 102 102 PHE CB C 35.61 . 1 351 102 102 PHE N N 116.48 . 1 352 103 103 ASP H H 7.441 . 1 353 103 103 ASP CA C 58.03 . 1 354 103 103 ASP CB C 40.54 . 1 355 103 103 ASP N N 122.97 . 1 356 104 104 ILE H H 7.027 . 1 357 104 104 ILE CA C 65.74 . 1 358 104 104 ILE CB C 35.78 . 1 359 104 104 ILE N N 119.06 . 1 360 105 105 ALA H H 7.619 . 1 361 105 105 ALA CA C 54.84 . 1 362 105 105 ALA CB C 16.41 . 1 363 105 105 ALA N N 120.86 . 1 364 106 106 ARG H H 7.435 . 1 365 106 106 ARG CA C 58.41 . 1 366 106 106 ARG CB C 29.23 . 1 367 106 106 ARG N N 119.38 . 1 368 119 119 GLU CA C 53.17 . 1 369 119 119 GLU CB C 31.41 . 1 370 120 120 ASN H H 8.174 . 1 371 120 120 ASN CA C 53.10 . 1 372 120 120 ASN CB C 40.75 . 1 373 120 120 ASN N N 121.96 . 1 374 121 121 VAL H H 9.097 . 1 375 121 121 VAL CA C 61.37 . 1 376 121 121 VAL CB C 31.92 . 1 377 121 121 VAL N N 114.39 . 1 378 122 122 LYS H H 7.449 . 1 379 122 122 LYS CA C 60.40 . 1 380 122 122 LYS CB C 31.45 . 1 381 122 122 LYS N N 121.69 . 1 382 123 123 ASN H H 7.601 . 1 383 123 123 ASN CA C 55.15 . 1 384 123 123 ASN CB C 39.04 . 1 385 123 123 ASN N N 112.28 . 1 386 124 124 PHE H H 7.936 . 1 387 124 124 PHE CA C 61.99 . 1 388 124 124 PHE CB C 40.44 . 1 389 124 124 PHE N N 119.92 . 1 390 125 125 ALA H H 7.373 . 1 391 125 125 ALA CA C 53.64 . 1 392 125 125 ALA CB C 17.98 . 1 393 125 125 ALA N N 113.74 . 1 394 126 126 SER H H 6.848 . 1 395 126 126 SER CA C 57.08 . 1 396 126 126 SER CB C 63.98 . 1 397 126 126 SER N N 108.45 . 1 398 127 127 HIS H H 7.845 . 1 399 127 127 HIS CA C 59.22 . 1 400 127 127 HIS CB C 31.20 . 1 401 127 127 HIS N N 124.18 . 1 402 128 128 ASP H H 8.687 . 1 403 128 128 ASP CA C 53.87 . 1 404 128 128 ASP CB C 38.66 . 1 405 128 128 ASP N N 128.76 . 1 406 129 129 ASN H H 9.071 . 1 407 129 129 ASN CA C 54.22 . 1 408 129 129 ASN CB C 37.18 . 1 409 129 129 ASN N N 117.01 . 1 410 130 130 GLY H H 7.203 . 1 411 130 130 GLY CA C 44.82 . 1 412 130 130 GLY N N 105.73 . 1 413 131 131 ASN H H 8.350 . 1 414 131 131 ASN CA C 55.67 . 1 415 131 131 ASN CB C 38.01 . 1 416 131 131 ASN N N 120.33 . 1 417 132 132 THR H H 6.883 . 1 418 132 132 THR CA C 66.20 . 1 419 132 132 THR N N 119.54 . 1 420 133 133 LEU H H 8.687 . 1 421 133 133 LEU CA C 56.94 . 1 422 133 133 LEU CB C 40.27 . 1 423 133 133 LEU N N 122.87 . 1 424 134 134 GLU H H 7.347 . 1 425 134 134 GLU CA C 58.87 . 1 426 134 134 GLU CB C 28.44 . 1 427 134 134 GLU N N 118.09 . 1 428 135 135 VAL H H 8.082 . 1 429 135 135 VAL CA C 66.17 . 1 430 135 135 VAL CB C 30.62 . 1 431 135 135 VAL N N 120.62 . 1 432 136 136 VAL H H 7.335 . 1 433 136 136 VAL CA C 65.56 . 1 434 136 136 VAL CB C 29.76 . 1 435 136 136 VAL N N 123.84 . 1 436 137 137 LYS CA C 59.28 . 1 437 137 137 LYS CB C 31.04 . 1 438 138 138 ASN H H 8.883 . 1 439 138 138 ASN CA C 55.74 . 1 440 138 138 ASN CB C 37.29 . 1 441 138 138 ASN N N 117.13 . 1 442 139 139 THR H H 8.252 . 1 443 139 139 THR CA C 66.93 . 1 444 139 139 THR CB C 68.07 . 1 445 139 139 THR N N 118.93 . 1 446 145 145 TYR CA C 57.15 . 1 447 145 145 TYR CB C 41.05 . 1 448 146 146 SER H H 9.078 . 1 449 146 146 SER CA C 56.64 . 1 450 146 146 SER CB C 64.38 . 1 451 146 146 SER N N 116.98 . 1 452 147 147 PHE H H 8.301 . 1 453 147 147 PHE CA C 58.43 . 1 454 147 147 PHE CB C 42.29 . 1 455 147 147 PHE N N 120.29 . 1 456 148 148 HIS H H 8.077 . 1 457 148 148 HIS CA C 54.09 . 1 458 148 148 HIS CB C 30.81 . 1 459 148 148 HIS N N 128.54 . 1 460 149 149 ALA H H 8.883 . 1 461 149 149 ALA CA C 50.32 . 1 462 149 149 ALA CB C 22.24 . 1 463 149 149 ALA N N 125.77 . 1 464 150 150 LYS H H 7.968 . 1 465 150 150 LYS CA C 55.82 . 1 466 150 150 LYS CB C 34.72 . 1 467 150 150 LYS N N 122.39 . 1 468 151 151 VAL H H 8.474 . 1 469 151 151 VAL CA C 60.86 . 1 470 151 151 VAL CB C 30.23 . 1 471 151 151 VAL N N 126.42 . 1 472 152 152 LEU H H 8.838 . 1 473 152 152 LEU CA C 52.88 . 1 474 152 152 LEU CB C 43.62 . 1 475 152 152 LEU N N 125.97 . 1 476 153 153 ASN H H 10.438 . 1 477 153 153 ASN CA C 50.85 . 1 478 153 153 ASN CB C 39.66 . 1 479 153 153 ASN N N 129.26 . 1 480 154 154 ALA H H 7.845 . 1 481 154 154 ALA CA C 55.96 . 1 482 154 154 ALA CB C 17.57 . 1 483 154 154 ALA N N 129.51 . 1 484 155 155 LEU H H 7.057 . 1 485 155 155 LEU CA C 56.27 . 1 486 155 155 LEU CB C 40.00 . 1 487 155 155 LEU N N 115.83 . 1 488 156 156 ASP H H 7.669 . 1 489 156 156 ASP CA C 54.85 . 1 490 156 156 ASP CB C 42.00 . 1 491 156 156 ASP N N 120.48 . 1 492 157 157 TYR H H 7.552 . 1 493 157 157 TYR CA C 57.00 . 1 494 157 157 TYR CB C 38.06 . 1 495 157 157 TYR N N 116.54 . 1 496 158 158 GLY H H 9.229 . 1 497 158 158 GLY CA C 45.49 . 1 498 158 158 GLY N N 110.00 . 1 499 159 159 ILE H H 6.871 . 1 500 159 159 ILE CA C 52.09 . 1 501 159 159 ILE CB C 38.65 . 1 502 159 159 ILE N N 120.66 . 1 503 160 160 PRO CA C 60.47 . 1 504 160 160 PRO CB C 27.18 . 1 505 161 161 GLN H H 8.661 . 1 506 161 161 GLN CA C 54.06 . 1 507 161 161 GLN CB C 31.11 . 1 508 161 161 GLN N N 126.58 . 1 509 162 162 LYS H H 8.548 . 1 510 162 162 LYS CA C 54.35 . 1 511 162 162 LYS CB C 26.26 . 1 512 162 162 LYS N N 129.90 . 1 513 163 163 ARG H H 7.651 . 1 514 163 163 ARG CA C 55.01 . 1 515 163 163 ARG CB C 29.71 . 1 516 163 163 ARG N N 124.66 . 1 517 164 164 GLU H H 9.528 . 1 518 164 164 GLU CA C 55.94 . 1 519 164 164 GLU CB C 30.92 . 1 520 164 164 GLU N N 105.01 . 1 521 165 165 ARG H H 8.583 . 1 522 165 165 ARG CA C 51.75 . 1 523 165 165 ARG CB C 32.02 . 1 524 165 165 ARG N N 126.39 . 1 525 172 172 ARG CA C 57.62 . 1 526 172 172 ARG CB C 29.76 . 1 527 173 173 ASN H H 9.045 . 1 528 173 173 ASN CA C 55.96 . 1 529 173 173 ASN CB C 37.27 . 1 530 173 173 ASN N N 126.42 . 1 531 174 174 ASP H H 8.741 . 1 532 174 174 ASP CA C 54.86 . 1 533 174 174 ASP CB C 38.28 . 1 534 174 174 ASP N N 118.17 . 1 535 175 175 LEU H H 7.522 . 1 536 175 175 LEU CA C 55.05 . 1 537 175 175 LEU CB C 40.83 . 1 538 175 175 LEU N N 118.95 . 1 539 176 176 ASN H H 7.787 . 1 540 176 176 ASN CA C 53.31 . 1 541 176 176 ASN CB C 36.82 . 1 542 176 176 ASN N N 115.59 . 1 543 177 177 ILE H H 8.626 . 1 544 177 177 ILE CA C 59.41 . 1 545 177 177 ILE CB C 34.21 . 1 546 177 177 ILE N N 120.08 . 1 547 178 178 GLN H H 8.576 . 1 548 178 178 GLN CA C 55.14 . 1 549 178 178 GLN CB C 29.63 . 1 550 178 178 GLN N N 126.80 . 1 551 179 179 ASN H H 7.996 . 1 552 179 179 ASN CA C 52.26 . 1 553 179 179 ASN CB C 38.94 . 1 554 179 179 ASN N N 117.70 . 1 555 180 180 PHE H H 7.932 . 1 556 180 180 PHE CA C 58.64 . 1 557 180 180 PHE CB C 38.88 . 1 558 180 180 PHE N N 122.11 . 1 559 181 181 GLN H H 7.066 . 1 560 181 181 GLN CA C 52.62 . 1 561 181 181 GLN CB C 30.48 . 1 562 181 181 GLN N N 126.73 . 1 563 182 182 PHE H H 8.503 . 1 564 182 182 PHE CA C 57.84 . 1 565 182 182 PHE CB C 37.20 . 1 566 182 182 PHE N N 120.75 . 1 567 183 183 PRO CA C 61.69 . 1 568 183 183 PRO CB C 31.32 . 1 569 184 184 LYS H H 8.862 . 1 570 184 184 LYS CA C 54.28 . 1 571 184 184 LYS CB C 31.57 . 1 572 184 184 LYS N N 128.58 . 1 573 185 185 PRO CA C 61.69 . 1 574 185 185 PRO CB C 33.74 . 1 575 186 186 PHE H H 7.940 . 1 576 186 186 PHE CA C 55.06 . 1 577 186 186 PHE CB C 39.93 . 1 578 186 186 PHE N N 115.86 . 1 579 187 187 GLU H H 8.628 . 1 580 187 187 GLU CA C 57.02 . 1 581 187 187 GLU CB C 29.75 . 1 582 187 187 GLU N N 123.81 . 1 583 188 188 LEU H H 8.367 . 1 584 188 188 LEU CA C 55.13 . 1 585 188 188 LEU CB C 40.73 . 1 586 188 188 LEU N N 128.66 . 1 587 189 189 ASN H H 8.426 . 1 588 189 189 ASN CA C 52.08 . 1 589 189 189 ASN CB C 39.85 . 1 590 189 189 ASN N N 123.37 . 1 591 190 190 THR H H 6.323 . 1 592 190 190 THR CA C 61.40 . 1 593 190 190 THR CB C 71.15 . 1 594 190 190 THR N N 117.71 . 1 595 191 191 PHE H H 9.142 . 1 596 191 191 PHE CA C 57.30 . 1 597 191 191 PHE CB C 40.41 . 1 598 191 191 PHE N N 122.10 . 1 599 192 192 VAL H H 8.062 . 1 600 192 192 VAL CA C 68.79 . 1 601 192 192 VAL CB C 29.71 . 1 602 192 192 VAL N N 121.71 . 1 603 193 193 LYS H H 8.929 . 1 604 193 193 LYS CA C 57.34 . 1 605 193 193 LYS CB C 29.53 . 1 606 193 193 LYS N N 112.64 . 1 607 194 194 ASP H H 7.541 . 1 608 194 194 ASP CA C 56.32 . 1 609 194 194 ASP CB C 41.47 . 1 610 194 194 ASP N N 119.44 . 1 611 195 195 LEU H H 7.897 . 1 612 195 195 LEU CA C 53.58 . 1 613 195 195 LEU CB C 41.44 . 1 614 195 195 LEU N N 118.15 . 1 615 196 196 LEU H H 6.438 . 1 616 196 196 LEU CA C 54.45 . 1 617 196 196 LEU CB C 40.33 . 1 618 196 196 LEU N N 116.77 . 1 619 197 197 LEU H H 10.169 . 1 620 197 197 LEU CA C 52.77 . 1 621 197 197 LEU CB C 40.44 . 1 622 197 197 LEU N N 125.63 . 1 623 198 198 PRO CA C 62.24 . 1 624 198 198 PRO CB C 31.46 . 1 625 199 199 ASP H H 8.479 . 1 626 199 199 ASP CA C 56.74 . 1 627 199 199 ASP CB C 39.82 . 1 628 199 199 ASP N N 122.09 . 1 629 200 200 SER H H 8.310 . 1 630 200 200 SER CA C 60.33 . 1 631 200 200 SER CB C 61.72 . 1 632 200 200 SER N N 112.81 . 1 633 201 201 GLU H H 7.781 . 1 634 201 201 GLU CA C 56.41 . 1 635 201 201 GLU CB C 30.54 . 1 636 201 201 GLU N N 120.01 . 1 637 202 202 VAL H H 7.284 . 1 638 202 202 VAL CA C 60.09 . 1 639 202 202 VAL CB C 32.26 . 1 640 202 202 VAL N N 107.39 . 1 641 203 203 GLU H H 7.633 . 1 642 203 203 GLU CA C 58.85 . 1 643 203 203 GLU CB C 28.89 . 1 644 203 203 GLU N N 122.90 . 1 645 204 204 HIS H H 8.737 . 1 646 204 204 HIS CA C 57.24 . 1 647 204 204 HIS CB C 28.62 . 1 648 204 204 HIS N N 115.17 . 1 649 205 205 LEU H H 7.649 . 1 650 205 205 LEU CA C 53.88 . 1 651 205 205 LEU CB C 40.79 . 1 652 205 205 LEU N N 121.95 . 1 653 206 206 VAL H H 7.013 . 1 654 206 206 VAL CA C 63.23 . 1 655 206 206 VAL CB C 31.44 . 1 656 206 206 VAL N N 120.74 . 1 657 207 207 ILE H H 8.630 . 1 658 207 207 ILE CA C 58.89 . 1 659 207 207 ILE CB C 39.65 . 1 660 207 207 ILE N N 130.35 . 1 661 208 208 ASP H H 8.710 . 1 662 208 208 ASP CA C 52.11 . 1 663 208 208 ASP CB C 41.09 . 1 664 208 208 ASP N N 128.55 . 1 665 209 209 ARG H H 9.013 . 1 666 209 209 ARG CA C 52.59 . 1 667 209 209 ARG CB C 29.87 . 1 668 209 209 ARG N N 125.55 . 1 669 210 210 LYS H H 9.006 . 1 670 210 210 LYS CA C 56.60 . 1 671 210 210 LYS CB C 30.83 . 1 672 210 210 LYS N N 123.56 . 1 673 211 211 ASP H H 9.092 . 1 674 211 211 ASP CA C 52.22 . 1 675 211 211 ASP CB C 38.04 . 1 676 211 211 ASP N N 118.13 . 1 677 212 212 LEU H H 6.627 . 1 678 212 212 LEU CA C 55.44 . 1 679 212 212 LEU CB C 41.34 . 1 680 212 212 LEU N N 120.81 . 1 681 213 213 VAL H H 9.308 . 1 682 213 213 VAL CA C 61.33 . 1 683 213 213 VAL CB C 33.30 . 1 684 213 213 VAL N N 104.51 . 1 685 214 214 MET H H 8.545 . 1 686 214 214 MET CA C 53.18 . 1 687 214 214 MET CB C 29.45 . 1 688 214 214 MET N N 125.18 . 1 689 215 215 THR H H 9.024 . 1 690 215 215 THR CA C 61.69 . 1 691 215 215 THR CB C 68.60 . 1 692 215 215 THR N N 118.67 . 1 693 216 216 ASN H H 8.066 . 1 694 216 216 ASN CA C 51.74 . 1 695 216 216 ASN CB C 41.96 . 1 696 216 216 ASN N N 121.58 . 1 697 217 217 GLN H H 8.098 . 1 698 217 217 GLN CA C 54.36 . 1 699 217 217 GLN CB C 29.37 . 1 700 217 217 GLN N N 119.08 . 1 701 218 218 GLU H H 8.065 . 1 702 218 218 GLU CA C 55.56 . 1 703 218 218 GLU CB C 28.84 . 1 704 218 218 GLU N N 121.59 . 1 705 219 219 ILE H H 9.065 . 1 706 219 219 ILE CA C 60.14 . 1 707 219 219 ILE CB C 38.80 . 1 708 219 219 ILE N N 123.21 . 1 709 220 220 GLU H H 8.314 . 1 710 220 220 GLU CA C 56.74 . 1 711 220 220 GLU CB C 30.05 . 1 712 220 220 GLU N N 119.40 . 1 713 221 221 GLN H H 7.478 . 1 714 221 221 GLN CA C 53.59 . 1 715 221 221 GLN CB C 29.53 . 1 716 221 221 GLN N N 117.91 . 1 717 222 222 THR H H 7.597 . 1 718 222 222 THR CA C 59.65 . 1 719 222 222 THR CB C 68.35 . 1 720 222 222 THR N N 112.35 . 1 721 223 223 THR H H 7.708 . 1 722 223 223 THR CA C 57.03 . 1 723 223 223 THR CB C 45.23 . 1 724 223 223 THR N N 116.57 . 1 725 224 224 PRO CA C 61.41 . 1 726 224 224 PRO CB C 27.41 . 1 727 225 225 LYS H H 8.562 . 1 728 225 225 LYS CA C 54.53 . 1 729 225 225 LYS CB C 35.28 . 1 730 225 225 LYS N N 120.31 . 1 731 226 226 THR H H 8.252 . 1 732 226 226 THR CA C 60.77 . 1 733 226 226 THR CB C 68.43 . 1 734 226 226 THR N N 113.71 . 1 735 227 227 VAL H H 9.473 . 1 736 227 227 VAL CA C 60.90 . 1 737 227 227 VAL CB C 32.75 . 1 738 227 227 VAL N N 128.01 . 1 739 228 228 ARG H H 9.017 . 1 740 228 228 ARG CA C 55.95 . 1 741 228 228 ARG CB C 29.59 . 1 742 228 228 ARG N N 129.85 . 1 743 229 229 LEU H H 9.405 . 1 744 229 229 LEU CA C 54.28 . 1 745 229 229 LEU CB C 43.24 . 1 746 229 229 LEU N N 128.51 . 1 747 230 230 GLY H H 7.415 . 1 748 230 230 GLY CA C 46.13 . 1 749 230 230 GLY N N 104.57 . 1 750 231 231 ILE H H 8.585 . 1 751 231 231 ILE CA C 58.85 . 1 752 231 231 ILE CB C 43.05 . 1 753 231 231 ILE N N 112.04 . 1 754 232 232 VAL H H 8.254 . 1 755 232 232 VAL CA C 58.17 . 1 756 232 232 VAL CB C 33.01 . 1 757 232 232 VAL N N 111.15 . 1 758 233 233 GLY H H 8.008 . 1 759 233 233 GLY CA C 47.32 . 1 760 233 233 GLY N N 108.47 . 1 761 234 234 LYS H H 8.393 . 1 762 234 234 LYS CA C 55.48 . 1 763 234 234 LYS CB C 31.39 . 1 764 234 234 LYS N N 125.36 . 1 765 235 235 GLY H H 8.951 . 1 766 235 235 GLY CA C 47.08 . 1 767 235 235 GLY N N 112.98 . 1 768 236 236 GLY H H 9.882 . 1 769 236 236 GLY CA C 43.92 . 1 770 236 236 GLY N N 113.57 . 1 771 237 237 GLN H H 8.706 . 1 772 237 237 GLN CA C 58.49 . 1 773 237 237 GLN CB C 29.71 . 1 774 237 237 GLN N N 120.00 . 1 775 238 238 GLY H H 7.976 . 1 776 238 238 GLY CA C 45.98 . 1 777 238 238 GLY N N 108.80 . 1 778 239 239 GLU H H 8.072 . 1 779 239 239 GLU CA C 53.98 . 1 780 239 239 GLU CB C 27.29 . 1 781 239 239 GLU N N 116.47 . 1 782 240 240 ARG H H 7.910 . 1 783 240 240 ARG CA C 54.46 . 1 784 240 240 ARG CB C 33.78 . 1 785 240 240 ARG N N 118.25 . 1 786 241 241 ILE H H 8.250 . 1 787 241 241 ILE CA C 58.57 . 1 788 241 241 ILE CB C 38.24 . 1 789 241 241 ILE N N 123.65 . 1 790 242 242 TYR H H 8.685 . 1 791 242 242 TYR CA C 57.27 . 1 792 242 242 TYR CB C 40.88 . 1 793 242 242 TYR N N 127.35 . 1 794 243 243 SER H H 8.491 . 1 795 243 243 SER CA C 57.30 . 1 796 243 243 SER CB C 62.91 . 1 797 243 243 SER N N 111.27 . 1 798 244 244 THR H H 10.939 . 1 799 244 244 THR CA C 62.98 . 1 800 244 244 THR CB C 68.37 . 1 801 244 244 THR N N 121.50 . 1 802 245 245 ARG H H 8.979 . 1 803 245 245 ARG CA C 57.12 . 1 804 245 245 ARG CB C 28.55 . 1 805 245 245 ARG N N 122.95 . 1 806 246 246 GLY H H 6.688 . 1 807 246 246 GLY CA C 44.31 . 1 808 246 246 GLY N N 104.89 . 1 809 247 247 ILE H H 7.279 . 1 810 247 247 ILE CA C 57.99 . 1 811 247 247 ILE CB C 38.36 . 1 812 247 247 ILE N N 113.35 . 1 813 248 248 ALA H H 7.892 . 1 814 248 248 ALA CA C 50.87 . 1 815 248 248 ALA CB C 18.09 . 1 816 248 248 ALA N N 122.64 . 1 817 249 249 ILE H H 6.515 . 1 818 249 249 ILE CA C 60.67 . 1 819 249 249 ILE CB C 37.34 . 1 820 249 249 ILE N N 111.00 . 1 821 250 250 THR H H 8.607 . 1 822 250 250 THR CA C 63.53 . 1 823 250 250 THR CB C 69.47 . 1 824 250 250 THR N N 115.60 . 1 825 251 251 LEU H H 7.274 . 1 826 251 251 LEU CA C 55.34 . 1 827 251 251 LEU CB C 40.00 . 1 828 251 251 LEU N N 128.88 . 1 829 252 252 SER H H 8.484 . 1 830 252 252 SER CA C 55.48 . 1 831 252 252 SER CB C 64.91 . 1 832 252 252 SER N N 115.67 . 1 833 253 253 ALA H H 7.166 . 1 834 253 253 ALA CA C 53.60 . 1 835 253 253 ALA CB C 22.83 . 1 836 253 253 ALA N N 121.53 . 1 837 254 254 TYR H H 10.881 . 1 838 254 254 TYR CA C 56.30 . 1 839 254 254 TYR CB C 36.94 . 1 840 254 254 TYR N N 118.28 . 1 841 255 255 GLY H H 6.629 . 1 842 255 255 GLY CA C 47.15 . 1 843 255 255 GLY N N 105.36 . 1 844 256 256 GLY H H 7.541 . 1 845 256 256 GLY CA C 42.77 . 1 846 256 256 GLY N N 111.41 . 1 847 257 257 GLY H H 8.328 . 1 848 257 257 GLY CA C 42.79 . 1 849 257 257 GLY N N 108.64 . 1 850 258 258 ILE H H 8.219 . 1 851 258 258 ILE CA C 60.52 . 1 852 258 258 ILE CB C 37.80 . 1 853 258 258 ILE N N 121.66 . 1 854 259 259 PHE H H 9.384 . 1 855 259 259 PHE CA C 55.35 . 1 856 259 259 PHE CB C 34.80 . 1 857 259 259 PHE N N 123.69 . 1 858 260 260 ALA H H 6.026 . 1 859 260 260 ALA CA C 53.40 . 1 860 260 260 ALA CB C 19.41 . 1 861 260 260 ALA N N 119.40 . 1 862 261 261 LYS H H 8.493 . 1 863 261 261 LYS CA C 60.94 . 1 864 261 261 LYS CB C 29.03 . 1 865 261 261 LYS N N 115.13 . 1 866 262 262 THR H H 8.203 . 1 867 262 262 THR CA C 61.09 . 1 868 262 262 THR CB C 69.67 . 1 869 262 262 THR N N 108.27 . 1 870 263 263 GLY H H 7.571 . 1 871 263 263 GLY CA C 44.33 . 1 872 263 263 GLY N N 109.26 . 1 873 264 264 GLY H H 6.638 . 1 874 264 264 GLY CA C 43.14 . 1 875 264 264 GLY N N 103.45 . 1 876 265 265 TYR H H 8.550 . 1 877 265 265 TYR CA C 56.51 . 1 878 265 265 TYR CB C 41.29 . 1 879 265 265 TYR N N 119.10 . 1 880 266 266 LEU H H 7.333 . 1 881 266 266 LEU CA C 53.08 . 1 882 266 266 LEU CB C 41.91 . 1 883 266 266 LEU N N 123.80 . 1 884 267 267 VAL H H 9.305 . 1 885 267 267 VAL CA C 60.88 . 1 886 267 267 VAL CB C 32.25 . 1 887 267 267 VAL N N 129.82 . 1 888 268 268 ASN H H 9.500 . 1 889 268 268 ASN CA C 53.71 . 1 890 268 268 ASN CB C 36.95 . 1 891 268 268 ASN N N 128.35 . 1 892 269 269 GLY H H 8.336 . 1 893 269 269 GLY CA C 45.05 . 1 894 269 269 GLY N N 130.13 . 1 895 270 270 LYS H H 7.680 . 1 896 270 270 LYS CA C 53.72 . 1 897 270 270 LYS CB C 34.10 . 1 898 270 270 LYS N N 121.57 . 1 899 271 271 THR H H 8.884 . 1 900 271 271 THR CA C 57.67 . 1 901 271 271 THR CB C 69.47 . 1 902 271 271 THR N N 110.98 . 1 903 272 272 ARG H H 8.977 . 1 904 272 272 ARG CA C 53.50 . 1 905 272 272 ARG CB C 34.77 . 1 906 272 272 ARG N N 120.02 . 1 907 273 273 LYS H H 7.237 . 1 908 273 273 LYS CA C 55.25 . 1 909 273 273 LYS CB C 33.32 . 1 910 273 273 LYS N N 117.81 . 1 911 274 274 LEU H H 7.205 . 1 912 274 274 LEU CA C 53.51 . 1 913 274 274 LEU CB C 41.72 . 1 914 274 274 LEU N N 114.42 . 1 915 275 275 HIS H H 10.140 . 1 916 275 275 HIS CA C 55.34 . 1 917 275 275 HIS CB C 33.35 . 1 918 275 275 HIS N N 126.25 . 1 919 276 276 PRO CA C 67.43 . 1 920 276 276 PRO CB C 31.64 . 1 921 277 277 ARG H H 12.285 . 1 922 277 277 ARG CA C 56.56 . 1 923 277 277 ARG CB C 27.01 . 1 924 277 277 ARG N N 121.23 . 1 925 278 278 GLU H H 7.340 . 1 926 278 278 GLU CA C 58.60 . 1 927 278 278 GLU CB C 28.72 . 1 928 278 278 GLU N N 118.58 . 1 929 279 279 CYS H H 8.043 . 1 930 279 279 CYS CA C 62.52 . 1 931 279 279 CYS CB C 24.95 . 1 932 279 279 CYS N N 117.31 . 1 933 280 280 ALA H H 7.293 . 1 934 280 280 ALA CA C 54.41 . 1 935 280 280 ALA CB C 16.82 . 1 936 280 280 ALA N N 120.96 . 1 937 281 281 ARG H H 7.750 . 1 938 281 281 ARG CA C 59.95 . 1 939 281 281 ARG CB C 30.48 . 1 940 281 281 ARG N N 119.61 . 1 941 282 282 VAL H H 8.395 . 1 942 282 282 VAL CA C 63.72 . 1 943 282 282 VAL CB C 30.41 . 1 944 282 282 VAL N N 120.20 . 1 945 283 283 MET H H 7.096 . 1 946 283 283 MET CA C 52.80 . 1 947 283 283 MET CB C 30.66 . 1 948 283 283 MET N N 115.25 . 1 949 284 284 GLY H H 8.048 . 1 950 284 284 GLY CA C 45.45 . 1 951 284 284 GLY N N 107.69 . 1 952 285 285 TYR H H 9.048 . 1 953 285 285 TYR CA C 57.14 . 1 954 285 285 TYR CB C 36.27 . 1 955 285 285 TYR N N 123.05 . 1 956 286 286 PRO CA C 61.70 . 1 957 286 286 PRO CB C 31.61 . 1 958 287 287 ASP H H 8.932 . 1 959 287 287 ASP CA C 55.76 . 1 960 287 287 ASP CB C 38.57 . 1 961 287 287 ASP N N 121.94 . 1 962 288 288 SER H H 7.421 . 1 963 288 288 SER CA C 57.94 . 1 964 288 288 SER CB C 62.37 . 1 965 288 288 SER N N 110.36 . 1 966 289 289 TYR H H 8.012 . 1 967 289 289 TYR CA C 59.18 . 1 968 289 289 TYR CB C 38.94 . 1 969 289 289 TYR N N 127.57 . 1 970 290 290 LYS H H 8.937 . 1 971 290 290 LYS CA C 55.96 . 1 972 290 290 LYS CB C 31.74 . 1 973 290 290 LYS N N 106.13 . 1 974 291 291 VAL H H 7.481 . 1 975 291 291 VAL CA C 60.08 . 1 976 291 291 VAL CB C 31.91 . 1 977 291 291 VAL N N 117.18 . 1 978 292 292 HIS H H 8.454 . 1 979 292 292 HIS CA C 57.99 . 1 980 292 292 HIS CB C 30.93 . 1 981 292 292 HIS N N 125.69 . 1 982 293 293 PRO CA C 63.82 . 1 983 293 293 PRO CB C 31.26 . 1 984 294 294 SER H H 10.721 . 1 985 294 294 SER CA C 56.10 . 1 986 294 294 SER CB C 60.83 . 1 987 294 294 SER N N 119.95 . 1 988 295 295 THR H H 8.691 . 1 989 295 295 THR CA C 65.62 . 1 990 295 295 THR CB C 67.45 . 1 991 295 295 THR N N 125.79 . 1 992 296 296 SER H H 7.940 . 1 993 296 296 SER CA C 61.06 . 1 994 296 296 SER N N 114.03 . 1 995 297 297 GLN H H 7.374 . 1 996 297 297 GLN CA C 56.65 . 1 997 297 297 GLN CB C 25.64 . 1 998 297 297 GLN N N 120.83 . 1 999 298 298 ALA H H 8.689 . 1 1000 298 298 ALA CA C 55.02 . 1 1001 298 298 ALA CB C 16.99 . 1 1002 298 298 ALA N N 123.78 . 1 1003 299 299 TYR H H 8.465 . 1 1004 299 299 TYR CA C 60.90 . 1 1005 299 299 TYR CB C 38.27 . 1 1006 299 299 TYR N N 115.03 . 1 1007 300 300 LYS H H 7.121 . 1 1008 300 300 LYS CA C 58.86 . 1 1009 300 300 LYS CB C 32.87 . 1 1010 300 300 LYS N N 121.37 . 1 1011 301 301 GLN H H 8.424 . 1 1012 301 301 GLN CA C 57.51 . 1 1013 301 301 GLN CB C 25.46 . 1 1014 301 301 GLN N N 115.48 . 1 1015 302 302 PHE H H 8.845 . 1 1016 302 302 PHE CA C 63.87 . 1 1017 302 302 PHE CB C 37.20 . 1 1018 302 302 PHE N N 118.66 . 1 1019 303 303 GLY H H 8.237 . 1 1020 303 303 GLY CA C 46.19 . 1 1021 303 303 GLY N N 106.25 . 1 1022 304 304 ASN H H 7.336 . 1 1023 304 304 ASN CA C 52.59 . 1 1024 304 304 ASN CB C 41.77 . 1 1025 304 304 ASN N N 119.78 . 1 1026 305 305 SER H H 7.057 . 1 1027 305 305 SER CA C 56.35 . 1 1028 305 305 SER CB C 64.48 . 1 1029 305 305 SER N N 110.50 . 1 1030 306 306 VAL H H 8.867 . 1 1031 306 306 VAL CA C 56.64 . 1 1032 306 306 VAL CB C 33.96 . 1 1033 306 306 VAL N N 114.26 . 1 1034 307 307 VAL H H 8.378 . 1 1035 307 307 VAL CA C 59.98 . 1 1036 307 307 VAL CB C 29.81 . 1 1037 307 307 VAL N N 119.12 . 1 1038 308 308 ILE H H 8.279 . 1 1039 308 308 ILE CA C 63.66 . 1 1040 308 308 ILE CB C 35.23 . 1 1041 308 308 ILE N N 129.10 . 1 1042 309 309 ASN H H 8.553 . 1 1043 309 309 ASN CA C 56.85 . 1 1044 309 309 ASN CB C 35.72 . 1 1045 309 309 ASN N N 111.90 . 1 1046 310 310 VAL H H 6.451 . 1 1047 310 310 VAL CA C 66.20 . 1 1048 310 310 VAL CB C 31.18 . 1 1049 310 310 VAL N N 112.28 . 1 1050 311 311 LEU H H 6.687 . 1 1051 311 311 LEU CA C 57.61 . 1 1052 311 311 LEU CB C 41.21 . 1 1053 311 311 LEU N N 115.06 . 1 1054 312 312 GLN H H 8.184 . 1 1055 312 312 GLN CA C 60.41 . 1 1056 312 312 GLN CB C 30.10 . 1 1057 312 312 GLN N N 117.69 . 1 1058 313 313 TYR H H 7.392 . 1 1059 313 313 TYR CA C 61.40 . 1 1060 313 313 TYR CB C 36.98 . 1 1061 313 313 TYR N N 116.00 . 1 1062 314 314 ILE H H 7.727 . 1 1063 314 314 ILE CA C 66.15 . 1 1064 314 314 ILE CB C 37.25 . 1 1065 314 314 ILE N N 117.90 . 1 1066 315 315 ALA H H 9.116 . 1 1067 315 315 ALA CA C 54.82 . 1 1068 315 315 ALA CB C 17.18 . 1 1069 315 315 ALA N N 122.55 . 1 1070 316 316 TYR H H 8.454 . 1 1071 316 316 TYR CA C 62.28 . 1 1072 316 316 TYR CB C 37.55 . 1 1073 316 316 TYR N N 119.57 . 1 1074 317 317 ASN H H 7.437 . 1 1075 317 317 ASN CA C 55.40 . 1 1076 317 317 ASN CB C 36.10 . 1 1077 317 317 ASN N N 121.86 . 1 1078 318 318 ILE H H 8.789 . 1 1079 318 318 ILE CA C 66.45 . 1 1080 318 318 ILE CB C 36.86 . 1 1081 318 318 ILE N N 124.64 . 1 1082 319 319 GLY H H 8.139 . 1 1083 319 319 GLY CA C 47.92 . 1 1084 319 319 GLY N N 106.69 . 1 1085 320 320 SER H H 8.344 . 1 1086 320 320 SER CA C 60.98 . 1 1087 320 320 SER CB C 62.03 . 1 1088 320 320 SER N N 118.10 . 1 1089 321 321 SER H H 7.840 . 1 1090 321 321 SER CA C 62.65 . 1 1091 321 321 SER N N 118.11 . 1 1092 322 322 LEU H H 7.846 . 1 1093 322 322 LEU CA C 56.43 . 1 1094 322 322 LEU CB C 41.21 . 1 1095 322 322 LEU N N 120.27 . 1 1096 323 323 ASN H H 7.708 . 1 1097 323 323 ASN CA C 53.44 . 1 1098 323 323 ASN CB C 38.14 . 1 1099 323 323 ASN N N 116.11 . 1 1100 324 324 LEU H H 7.816 . 1 1101 324 324 LEU CA C 55.98 . 1 1102 324 324 LEU CB C 41.01 . 1 1103 324 324 LEU N N 122.07 . 1 1104 325 325 GLU H H 8.059 . 1 1105 325 325 GLU CA C 56.44 . 1 1106 325 325 GLU CB C 29.02 . 1 1107 325 325 GLU N N 119.86 . 1 1108 326 326 HIS H H 8.008 . 1 1109 326 326 HIS N N 119.35 . 1 stop_ save_