data_4460 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; 1H, 15N and 13C Resonance Assignments for the C-terminal Protein Interaction Region of the 32 kDa Subunit of Human Replication Protein A ; _BMRB_accession_number 4460 _BMRB_flat_file_name bmr4460.str _Entry_type original _Submission_date 1999-11-16 _Accession_date 1999-11-16 _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 Mer Georges . . 2 Edwards Aled M. . 3 Chazin Walter J. . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 543 "13C chemical shifts" 277 "15N chemical shifts" 104 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2005-04-25 original author . stop_ loop_ _Related_BMRB_accession_number _Relationship 6534 'RPA32C (172-270) -Tag-OBD (131-259)' stop_ _Original_release_date 2005-04-25 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; 1H, 15N and 13C Resonance Assignments for the C-terminal Protein Interaction Region of the 32 kDa Subunit of Human Replication Protein A ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code 20377251 _PubMed_ID ? loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Mer Georges . . 2 Edwards Aled M. . 3 Chazin Walter J. . stop_ _Journal_abbreviation 'J. Biomol. NMR' _Journal_name_full 'Journal of Biomolecular NMR' _Journal_volume 17 _Journal_issue 2 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 179 _Page_last 180 _Year 2000 _Details . loop_ _Keyword 'DNA replication' 'DNA recombination' 'DNA repair' stop_ save_ ####################################### # Cited references within the entry # ####################################### save_citation_1 _Saveframe_category citation _Citation_full ; Erdile, L.F., Wold, M.S., and Kelly, T.J. "The primary structure of the 32-kDA subunit of human replication protein A". J. Biol. Chem. (1990) 265:3177-3182. ; _Citation_title 'The primary structure of the 32-kDa subunit of human replication protein A.' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 2406247 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Erdile 'L F' F. . 2 Wold 'M S' S. . 3 Kelly 'T J' J. . stop_ _Journal_abbreviation 'J. Biol. Chem.' _Journal_name_full 'The Journal of biological chemistry' _Journal_volume 265 _Journal_issue 6 _Journal_CSD . _Book_title . _Book_chapter_title . _Book_volume . _Book_series . _Book_publisher . _Book_publisher_city . _Book_ISBN . _Conference_title . _Conference_site . _Conference_state_province . _Conference_country . _Conference_start_date . _Conference_end_date . _Conference_abstract_number . _Thesis_institution . _Thesis_institution_city . _Thesis_institution_country . _Page_first 3177 _Page_last 3182 _Year 1990 _Details ; Replication protein A (RP-A) is a complex of three polypeptides of molecular mass 70, 32, and 14 kDa, which is absolutely required for simian virus 40 DNA replication in vitro. We have isolated a cDNA coding for the 32-kDa subunit of RP-A. An oligonucleotide probe was constructed based upon a tryptic peptide sequence derived from whole RP-A, and clones were isolated from a lambda gt11 library containing HeLa cDNA inserts. The amino acid sequence predicted from the cDNA contains the peptide sequence obtained from whole RP-A along with two sequences obtained from tryptic peptides derived from sodium dodecyl sulfate-polyacrylamide gel-purified 32-kDa subunit. The coding sequence predicts a protein of 29,228 daltons, in good agreement with the electrophoretically determined molecular mass of the 32-kDa subunit. No significant homology was found with any of the sequences in the GenBank data base. The protein predicted from the cDNA has an N-terminal region rich in glycine and serine along with two acidic and two basic segments. Monoclonal antibodies have been raised against the 70- and 32-kDa subunits of RP-A. The cloned cDNA has been overexpressed in bacteria using an inducible T7 expression system. The protein made in bacteria is recognized by a monoclonal antibody that is specific for the 32-kDa subunit of RP-A. This monoclonal antibody against the 32-kDa subunit inhibits DNA replication in vitro. ; save_ ################################## # Molecular system description # ################################## save_RPA32 _Saveframe_category molecular_system _Mol_system_name 'Replication Protein A 32kDa subunit' _Abbreviation_common RPA32 _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label RPA32 $RPA32(172-270) stop_ _System_molecular_weight 13532.19 _System_physical_state native _System_oligomer_state monomer _System_paramagnetic no _System_thiol_state 'fully reduced' _Database_query_date . _Details 'Involved in interactions with DNA repair and DNA recombination proteins' save_ ######################## # Monomeric polymers # ######################## save_RPA32(172-270) _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'Replication Protein A' _Abbreviation_common RPA32 _Molecular_mass . _Mol_thiol_state 'fully reduced' _Details ; The first 4 residues (GSHM) do not belong to the protein. First residue (Ser 172), last residue (Glu 270) ; ############################## # Polymer residue sequence # ############################## _Residue_count 103 _Mol_residue_sequence ; GSHMANSQPSAGRAPISNPG MSEAGNFGGNSFMPANGLTV AQNQVLNLIKACPRPEGLNF QDLKNQLKHMSVSSIKQAVD FLSNEGHIYSTVDDDHFKST DAE ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 -4 GLY 2 -3 SER 3 -2 HIS 4 -1 MET 5 172 ALA 6 173 ASN 7 174 SER 8 175 GLN 9 176 PRO 10 177 SER 11 178 ALA 12 179 GLY 13 180 ARG 14 181 ALA 15 182 PRO 16 183 ILE 17 184 SER 18 185 ASN 19 186 PRO 20 187 GLY 21 188 MET 22 189 SER 23 190 GLU 24 191 ALA 25 192 GLY 26 193 ASN 27 194 PHE 28 195 GLY 29 196 GLY 30 197 ASN 31 198 SER 32 199 PHE 33 200 MET 34 201 PRO 35 202 ALA 36 203 ASN 37 204 GLY 38 205 LEU 39 206 THR 40 207 VAL 41 208 ALA 42 209 GLN 43 210 ASN 44 211 GLN 45 212 VAL 46 213 LEU 47 214 ASN 48 215 LEU 49 216 ILE 50 217 LYS 51 218 ALA 52 219 CYS 53 220 PRO 54 221 ARG 55 222 PRO 56 223 GLU 57 224 GLY 58 225 LEU 59 226 ASN 60 227 PHE 61 228 GLN 62 229 ASP 63 230 LEU 64 231 LYS 65 232 ASN 66 233 GLN 67 234 LEU 68 235 LYS 69 236 HIS 70 237 MET 71 238 SER 72 239 VAL 73 240 SER 74 241 SER 75 242 ILE 76 243 LYS 77 244 GLN 78 245 ALA 79 246 VAL 80 247 ASP 81 248 PHE 82 249 LEU 83 250 SER 84 251 ASN 85 252 GLU 86 253 GLY 87 254 HIS 88 255 ILE 89 256 TYR 90 257 SER 91 258 THR 92 259 VAL 93 260 ASP 94 261 ASP 95 262 ASP 96 263 HIS 97 264 PHE 98 265 LYS 99 266 SER 100 267 THR 101 268 ASP 102 269 ALA 103 270 GLU stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-02-04 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 17060 RPA32C 94.17 97 100.00 100.00 2.96e-64 PDB 1DPU "Solution Structure Of The C-Terminal Domain Of Human Rpa32 Complexed With Ung2(73-88)" 96.12 99 100.00 100.00 1.39e-65 PDB 1Z1D "Structural Model For The Interaction Between Rpa32 C- Terminal Domain And Sv40 T Antigen Origin Binding Domain" 100.00 103 100.00 100.00 8.01e-69 PDB 2PI2 "Full-Length Replication Protein A Subunits Rpa14 And Rpa32" 96.12 270 100.00 100.00 3.19e-64 PDB 2Z6K "Crystal Structure Of Full-Length Human Rpa1432 HETERODIMER" 96.12 270 100.00 100.00 3.19e-64 PDB 4MQV "Crystal Complex Of Rpa32c And Smarcal1 N-terminus" 66.99 69 100.00 100.00 2.79e-42 PDB 4OU0 "Crystal Structure Of Rpa32c" 66.99 73 98.55 98.55 2.14e-40 DBJ BAG35795 "unnamed protein product [Homo sapiens]" 96.12 270 98.99 100.00 9.72e-64 DBJ BAG59456 "unnamed protein product [Homo sapiens]" 96.12 104 100.00 100.00 1.02e-65 DBJ BAG60901 "unnamed protein product [Homo sapiens]" 96.12 264 100.00 100.00 2.68e-64 DBJ BAG62374 "unnamed protein product [Homo sapiens]" 96.12 174 100.00 100.00 2.01e-65 DBJ BAI47325 "replication protein A2, 32kDa [synthetic construct]" 96.12 270 100.00 100.00 3.19e-64 EMBL CAG29344 "RPA2 [Homo sapiens]" 96.12 270 100.00 100.00 3.19e-64 EMBL CAH90667 "hypothetical protein [Pongo abelii]" 96.12 270 97.98 100.00 2.36e-63 GB AAA36560 "replication protein A [Homo sapiens]" 96.12 270 100.00 100.00 3.19e-64 GB AAH01630 "Replication protein A2, 32kDa [Homo sapiens]" 96.12 270 100.00 100.00 3.19e-64 GB AAH12157 "Replication protein A2, 32kDa [Homo sapiens]" 96.12 270 100.00 100.00 3.19e-64 GB AAH21257 "Replication protein A2, 32kDa [Homo sapiens]" 96.12 270 100.00 100.00 3.19e-64 GB AAX84514 "replication protein A2, 32kDa [Homo sapiens]" 96.12 270 100.00 100.00 3.19e-64 REF NP_001125362 "replication protein A 32 kDa subunit [Pongo abelii]" 96.12 343 97.98 100.00 5.84e-63 REF NP_001247563 "replication protein A 32 kDa subunit [Macaca mulatta]" 96.12 270 98.99 100.00 1.06e-63 REF NP_001273005 "replication protein A 32 kDa subunit isoform 2 [Homo sapiens]" 96.12 174 100.00 100.00 2.01e-65 REF NP_001284487 "replication protein A 32 kDa subunit isoform 3 [Homo sapiens]" 96.12 278 100.00 100.00 3.68e-64 REF NP_002937 "replication protein A 32 kDa subunit isoform 1 [Homo sapiens]" 96.12 270 100.00 100.00 3.19e-64 SP P15927 "RecName: Full=Replication protein A 32 kDa subunit; Short=RP-A p32; AltName: Full=Replication factor A protein 2; Short=RF-A pr" 96.12 270 100.00 100.00 3.19e-64 SP Q5RC43 "RecName: Full=Replication protein A 32 kDa subunit; Short=RP-A p32; AltName: Full=Replication factor A protein 2; Short=RF-A pr" 96.12 270 97.98 100.00 2.36e-63 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species _Organelle $RPA32(172-270) human 9606 Eukaryota Metazoa Homo sapiens nucleus stop_ save_ ######################### # Experimental source # ######################### save_experimental_source _Saveframe_category experimental_source loop_ _Mol_label _Production_method _Host_organism_name_common _Genus _Species _Strain _Vector_type _Vector_name _Vendor_name $RPA32(172-270) 'recombinant technology' 'E. coli' Escherichia coli BL21(DE3) plasmid pET15b Novagen 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 $RPA32(172-270) 1 mM '[U-13C; U-15N]' 'phosphate buffer' 25 mM . DTT 5 mM . H2O 93 % . D2O 7 % . stop_ save_ save_sample_2 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $RPA32(172-270) 1 mM '[U-10% 13C; U-15N]' 'phosphate buffer' 25 mM . DTT 5 mM . H2O 93 % . D2O 7 % . stop_ save_ save_sample_3 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $RPA32(172-270) 1 mM [U-15N] 'phosphate buffer' 25 mM . DTT 5 mM . H2O 93 % . D2O 7 % . stop_ save_ save_sample_4 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $RPA32(172-270) 1 mM NA 'phosphate buffer' 25 mM . DTT 5 mM . H2O 93 % . D2O 7 % . stop_ save_ ############################ # Computer software used # ############################ save_FELIX _Saveframe_category software _Name FELIX _Version 97 loop_ _Vendor _Address _Electronic_address MSI . . stop_ loop_ _Task 'spectra Processing' 'spectra Analysis' stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model AMX _Field_strength 500 _Details . save_ save_NMR_spectrometer_2 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model AMX _Field_strength 600 _Details . save_ save_NMR_spectrometer_3 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model DRX _Field_strength 600 _Details . save_ save_NMR_spectrometer_4 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model DMX _Field_strength 750 _Details . save_ save_NMR_spectrometer_5 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model DRX _Field_strength 800 _Details . save_ ############################# # NMR applied experiments # ############################# save_2D_1H-15N_HSQC_1 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-15N HSQC' _Sample_label . save_ save_2D_1H-13C_HSQC_2 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-13C HSQC' _Sample_label . save_ save_2D_NOESY_3 _Saveframe_category NMR_applied_experiment _Experiment_name '2D NOESY' _Sample_label . save_ save_2D_DQF-COSY_4 _Saveframe_category NMR_applied_experiment _Experiment_name '2D DQF-COSY' _Sample_label . save_ save_2D_TOCSY_5 _Saveframe_category NMR_applied_experiment _Experiment_name '2D TOCSY' _Sample_label . save_ save_2D_2Q_6 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 2Q' _Sample_label . save_ save_3D_HNCACB_7 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCACB' _Sample_label . save_ save_3D_CBCA(CO)NH_8 _Saveframe_category NMR_applied_experiment _Experiment_name '3D CBCA(CO)NH' _Sample_label . save_ save_3D_C(CO)NH-TOCSY_9 _Saveframe_category NMR_applied_experiment _Experiment_name '3D C(CO)NH-TOCSY' _Sample_label . save_ save_3D_H(CCO)NH-TOCSY_10 _Saveframe_category NMR_applied_experiment _Experiment_name '3D H(CCO)NH-TOCSY' _Sample_label . save_ save_3D_HBHA(CBCACO)NH_11 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HBHA(CBCACO)NH' _Sample_label . save_ save_3D_HNHA_12 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNHA' _Sample_label . save_ save_3D_HNHB_13 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNHB' _Sample_label . save_ save_3D_HACAHB-COSY_14 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HACAHB-COSY' _Sample_label . save_ save_3D_15N_edited_TOCSY_15 _Saveframe_category NMR_applied_experiment _Experiment_name '3D 15N edited TOCSY' _Sample_label . save_ save_3D_15N_edited_NOESY_16 _Saveframe_category NMR_applied_experiment _Experiment_name '3D 15N edited NOESY' _Sample_label . save_ save_3D_13C_edited_NOESY_17 _Saveframe_category NMR_applied_experiment _Experiment_name '3D 13C edited NOESY' _Sample_label . save_ save_NMR_spec_expt__0_1 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-15N HSQC' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_2 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-13C HSQC' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_3 _Saveframe_category NMR_applied_experiment _Experiment_name '2D NOESY' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_4 _Saveframe_category NMR_applied_experiment _Experiment_name '2D DQF-COSY' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_5 _Saveframe_category NMR_applied_experiment _Experiment_name '2D TOCSY' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_6 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 2Q' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_7 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCACB' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_8 _Saveframe_category NMR_applied_experiment _Experiment_name '3D CBCA(CO)NH' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_9 _Saveframe_category NMR_applied_experiment _Experiment_name '3D C(CO)NH-TOCSY' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_10 _Saveframe_category NMR_applied_experiment _Experiment_name '3D H(CCO)NH-TOCSY' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_11 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HBHA(CBCACO)NH' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_12 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNHA' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_13 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNHB' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_14 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HACAHB-COSY' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_15 _Saveframe_category NMR_applied_experiment _Experiment_name '3D 15N edited TOCSY' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_16 _Saveframe_category NMR_applied_experiment _Experiment_name '3D 15N edited NOESY' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_17 _Saveframe_category NMR_applied_experiment _Experiment_name '3D 13C edited NOESY' _BMRB_pulse_sequence_accession_number . _Details . save_ ####################### # Sample conditions # ####################### save_sample_conditions_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 7.0 . n/a temperature 298 . K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference _Saveframe_category chemical_shift_reference _Details . loop_ _Mol_common_name _Atom_type _Atom_isotope_number _Atom_group _Chem_shift_units _Chem_shift_value _Reference_method _Reference_type _External_reference_sample_geometry _External_reference_location _External_reference_axis _Indirect_shift_ratio DSS H 1 'methyl protons' ppm 0.0 internal direct . . . . DSS N 15 'methyl protons' ppm 0.0 . indirect . . . 0.101329118 DSS C 13 'methyl protons' ppm 0.0 . indirect . . . 0.251449530 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_chemical_shifts_label _Saveframe_category assigned_chemical_shifts _Details . loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $sample_conditions_1 _Chem_shift_reference_set_label $chemical_shift_reference _Mol_system_component_name RPA32 _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 . 4 MET HA H 4.345 . 1 2 . 4 MET HB2 H 2.032 . 2 3 . 4 MET HB3 H 1.906 . 2 4 . 4 MET HG2 H 2.434 . 1 5 . 4 MET HG3 H 2.434 . 1 6 . 4 MET CA C 55.24 . 1 7 . 4 MET CB C 32.78 . 1 8 . 4 MET CG C 31.81 . 1 9 . 5 ALA H H 8.329 . 1 10 . 5 ALA HA H 4.232 . 1 11 . 5 ALA HB H 1.354 . 1 12 . 5 ALA CA C 52.40 . 1 13 . 5 ALA CB C 19.62 . 1 14 . 5 ALA N N 125.53 . 1 15 . 6 ASN H H 7.906 . 1 16 . 6 ASN HA H 4.468 . 1 17 . 6 ASN HB2 H 2.840 . 2 18 . 6 ASN HB3 H 2.741 . 2 19 . 6 ASN CA C 54.69 . 1 20 . 6 ASN CB C 41.00 . 1 21 . 6 ASN N N 122.83 . 1 22 . 7 SER HA H 4.360 . 1 23 . 7 SER HB2 H 3.793 . 1 24 . 7 SER HB3 H 3.793 . 1 25 . 7 SER CA C 58.34 . 1 26 . 7 SER CB C 63.88 . 1 27 . 8 GLN H H 8.337 . 1 28 . 8 GLN HA H 4.621 . 1 29 . 8 GLN HB2 H 2.115 . 2 30 . 8 GLN HB3 H 1.963 . 2 31 . 8 GLN HG2 H 2.391 . 2 32 . 8 GLN HG3 H 2.343 . 2 33 . 8 GLN HE21 H 7.517 . 2 34 . 8 GLN HE22 H 6.861 . 2 35 . 8 GLN CA C 53.84 . 1 36 . 8 GLN CB C 29.09 . 1 37 . 8 GLN N N 122.83 . 1 38 . 8 GLN NE2 N 112.33 . 1 39 . 9 PRO HA H 4.369 . 1 40 . 9 PRO HB2 H 2.284 . 2 41 . 9 PRO HB3 H 1.918 . 2 42 . 9 PRO HG2 H 2.021 . 1 43 . 9 PRO HG3 H 2.021 . 1 44 . 9 PRO HD2 H 3.731 . 2 45 . 9 PRO HD3 H 3.610 . 2 46 . 9 PRO CA C 63.41 . 1 47 . 9 PRO CB C 32.07 . 1 48 . 9 PRO CG C 27.40 . 1 49 . 9 PRO CD C 50.62 . 1 50 . 10 SER H H 8.438 . 1 51 . 10 SER HA H 4.330 . 1 52 . 10 SER HB2 H 3.814 . 1 53 . 10 SER HB3 H 3.814 . 1 54 . 10 SER CA C 58.39 . 1 55 . 10 SER CB C 63.81 . 1 56 . 10 SER N N 116.41 . 1 57 . 11 ALA H H 8.344 . 1 58 . 11 ALA HA H 4.289 . 1 59 . 11 ALA HB H 1.415 . 1 60 . 11 ALA CA C 52.64 . 1 61 . 11 ALA CB C 19.32 . 1 62 . 11 ALA N N 126.22 . 1 63 . 12 GLY H H 8.370 . 1 64 . 12 GLY HA2 H 3.933 . 1 65 . 12 GLY HA3 H 3.933 . 1 66 . 12 GLY CA C 45.26 . 1 67 . 12 GLY N N 108.49 . 1 68 . 13 ARG H H 8.060 . 1 69 . 13 ARG HA H 4.295 . 1 70 . 13 ARG HB2 H 1.822 . 2 71 . 13 ARG HB3 H 1.710 . 2 72 . 13 ARG HG2 H 1.607 . 1 73 . 13 ARG HG3 H 1.607 . 1 74 . 13 ARG HD2 H 3.156 . 1 75 . 13 ARG HD3 H 3.156 . 1 76 . 13 ARG CA C 55.58 . 1 77 . 13 ARG CB C 31.10 . 1 78 . 13 ARG CG C 27.09 . 1 79 . 13 ARG CD C 43.33 . 1 80 . 13 ARG N N 120.66 . 1 81 . 14 ALA H H 8.349 . 1 82 . 14 ALA HA H 4.581 . 1 83 . 14 ALA HB H 1.356 . 1 84 . 14 ALA CA C 50.62 . 1 85 . 14 ALA CB C 18.17 . 1 86 . 14 ALA N N 127.11 . 1 87 . 15 PRO HA H 4.364 . 1 88 . 15 PRO HB2 H 2.237 . 2 89 . 15 PRO HB3 H 1.877 . 2 90 . 15 PRO HG2 H 1.998 . 1 91 . 15 PRO HG3 H 1.998 . 1 92 . 15 PRO HD2 H 3.736 . 2 93 . 15 PRO HD3 H 3.583 . 2 94 . 15 PRO CA C 62.95 . 1 95 . 15 PRO CB C 32.02 . 1 96 . 15 PRO CG C 27.48 . 1 97 . 15 PRO CD C 50.43 . 1 98 . 16 ILE H H 8.257 . 1 99 . 16 ILE HA H 4.155 . 1 100 . 16 ILE HB H 1.846 . 1 101 . 16 ILE HG12 H 1.475 . 2 102 . 16 ILE HG13 H 1.196 . 2 103 . 16 ILE HD1 H 0.882 . 1 104 . 16 ILE CA C 61.04 . 1 105 . 16 ILE CB C 38.72 . 1 106 . 16 ILE CG1 C 27.37 . 1 107 . 16 ILE CG2 C 17.66 . 1 108 . 16 ILE CD1 C 17.66 . 1 109 . 16 ILE N N 120.91 . 1 110 . 17 SER H H 8.327 . 1 111 . 17 SER HA H 4.474 . 1 112 . 17 SER HB2 H 3.804 . 1 113 . 17 SER HB3 H 3.804 . 1 114 . 17 SER CA C 58.13 . 1 115 . 17 SER CB C 63.94 . 1 116 . 17 SER N N 119.84 . 1 117 . 19 PRO HA H 4.391 . 1 118 . 19 PRO HB2 H 2.266 . 2 119 . 19 PRO HB3 H 2.006 . 2 120 . 19 PRO HD2 H 3.745 . 1 121 . 19 PRO HD3 H 3.745 . 1 122 . 19 PRO CA C 63.79 . 1 123 . 19 PRO CB C 32.04 . 1 124 . 19 PRO CG C 27.25 . 1 125 . 19 PRO CD C 50.65 . 1 126 . 20 GLY H H 8.457 . 1 127 . 20 GLY HA2 H 3.929 . 1 128 . 20 GLY HA3 H 3.929 . 1 129 . 20 GLY CA C 45.43 . 1 130 . 20 GLY N N 108.71 . 1 131 . 21 MET H H 8.064 . 1 132 . 21 MET HA H 4.507 . 1 133 . 21 MET HB2 H 2.138 . 2 134 . 21 MET HB3 H 2.008 . 2 135 . 21 MET HG2 H 2.560 . 1 136 . 21 MET HG3 H 2.560 . 1 137 . 21 MET CA C 55.52 . 1 138 . 21 MET CB C 33.04 . 1 139 . 21 MET CG C 32.07 . 1 140 . 21 MET N N 119.85 . 1 141 . 22 SER H H 8.332 . 1 142 . 22 SER HA H 4.448 . 1 143 . 22 SER HB2 H 3.876 . 1 144 . 22 SER HB3 H 3.876 . 1 145 . 22 SER CA C 58.56 . 1 146 . 22 SER CB C 63.87 . 1 147 . 22 SER N N 116.84 . 1 148 . 23 GLU H H 8.487 . 1 149 . 23 GLU HA H 4.290 . 1 150 . 23 GLU HB2 H 2.094 . 1 151 . 23 GLU HB3 H 1.969 . 1 152 . 23 GLU HG2 H 2.267 . 1 153 . 23 GLU HG3 H 2.267 . 1 154 . 23 GLU CA C 56.88 . 1 155 . 23 GLU CB C 30.12 . 1 156 . 23 GLU CG C 36.32 . 1 157 . 23 GLU N N 123.11 . 1 158 . 24 ALA H H 8.253 . 1 159 . 24 ALA HA H 4.284 . 1 160 . 24 ALA HB H 1.380 . 1 161 . 24 ALA CA C 52.86 . 1 162 . 24 ALA CB C 19.23 . 1 163 . 24 ALA N N 124.33 . 1 164 . 25 GLY H H 8.223 . 1 165 . 25 GLY HA2 H 3.841 . 1 166 . 25 GLY HA3 H 3.841 . 1 167 . 25 GLY CA C 45.36 . 1 168 . 25 GLY N N 107.42 . 1 169 . 26 ASN H H 8.087 . 1 170 . 26 ASN HA H 4.601 . 1 171 . 26 ASN HB2 H 2.748 . 2 172 . 26 ASN HB3 H 2.660 . 2 173 . 26 ASN HD21 H 8.087 . 2 174 . 26 ASN HD22 H 6.848 . 2 175 . 26 ASN CA C 52.91 . 1 176 . 26 ASN CB C 38.83 . 1 177 . 26 ASN N N 118.34 . 1 178 . 26 ASN ND2 N 112.15 . 1 179 . 27 PHE H H 8.271 . 1 180 . 27 PHE HA H 4.616 . 1 181 . 27 PHE HB2 H 3.177 . 2 182 . 27 PHE HB3 H 3.022 . 2 183 . 27 PHE CA C 57.90 . 1 184 . 27 PHE CB C 39.28 . 1 185 . 27 PHE N N 120.91 . 1 186 . 28 GLY H H 8.348 . 1 187 . 28 GLY HA2 H 3.901 . 1 188 . 28 GLY HA3 H 3.901 . 1 189 . 28 GLY CA C 45.57 . 1 190 . 28 GLY N N 110.63 . 1 191 . 29 GLY H H 8.041 . 1 192 . 29 GLY HA2 H 3.921 . 1 193 . 29 GLY HA3 H 3.921 . 1 194 . 29 GLY CA C 45.56 . 1 195 . 29 GLY N N 108.49 . 1 196 . 30 ASN HA H 4.629 . 1 197 . 30 ASN HB2 H 2.749 . 1 198 . 30 ASN HB3 H 2.749 . 1 199 . 30 ASN HD21 H 7.591 . 2 200 . 30 ASN HD22 H 6.905 . 2 201 . 30 ASN CA C 53.20 . 1 202 . 30 ASN CB C 38.98 . 1 203 . 30 ASN ND2 N 112.15 . 1 204 . 31 SER H H 8.127 . 1 205 . 31 SER HA H 4.370 . 1 206 . 31 SER HB2 H 3.787 . 1 207 . 31 SER HB3 H 3.787 . 1 208 . 31 SER CA C 58.54 . 1 209 . 31 SER CB C 63.79 . 1 210 . 31 SER N N 116.07 . 1 211 . 32 PHE H H 8.084 . 1 212 . 32 PHE HA H 4.604 . 1 213 . 32 PHE HB2 H 3.049 . 1 214 . 32 PHE HB3 H 3.049 . 1 215 . 32 PHE HD1 H 7.194 . 1 216 . 32 PHE HD2 H 7.194 . 1 217 . 32 PHE CA C 57.71 . 1 218 . 32 PHE CB C 39.52 . 1 219 . 32 PHE N N 121.55 . 1 220 . 33 MET H H 8.113 . 1 221 . 33 MET HA H 4.740 . 1 222 . 33 MET HB2 H 1.971 . 1 223 . 33 MET HB3 H 1.876 . 1 224 . 33 MET HG2 H 2.472 . 1 225 . 33 MET HG3 H 2.472 . 1 226 . 33 MET CA C 52.70 . 1 227 . 33 MET CB C 32.75 . 1 228 . 33 MET N N 123.69 . 1 229 . 34 PRO HA H 4.311 . 1 230 . 34 PRO HB2 H 2.268 . 2 231 . 34 PRO HB3 H 1.945 . 2 232 . 34 PRO HD2 H 3.657 . 1 233 . 34 PRO HD3 H 3.657 . 1 234 . 34 PRO CA C 62.96 . 1 235 . 34 PRO CB C 32.32 . 1 236 . 34 PRO CG C 27.51 . 1 237 . 34 PRO CD C 50.62 . 1 238 . 35 ALA H H 8.491 . 1 239 . 35 ALA HA H 4.309 . 1 240 . 35 ALA HB H 1.400 . 1 241 . 35 ALA CA C 52.49 . 1 242 . 35 ALA CB C 18.77 . 1 243 . 35 ALA N N 125.08 . 1 244 . 36 ASN H H 8.213 . 1 245 . 36 ASN HA H 4.663 . 1 246 . 36 ASN HB2 H 3.011 . 2 247 . 36 ASN HB3 H 2.831 . 2 248 . 36 ASN HD21 H 7.628 . 2 249 . 36 ASN HD22 H 7.346 . 2 250 . 36 ASN CA C 53.03 . 1 251 . 36 ASN CB C 38.66 . 1 252 . 36 ASN N N 116.63 . 1 253 . 36 ASN ND2 N 111.80 . 1 254 . 37 GLY H H 8.301 . 1 255 . 37 GLY HA2 H 4.057 . 2 256 . 37 GLY HA3 H 3.841 . 2 257 . 37 GLY CA C 45.57 . 1 258 . 37 GLY N N 108.07 . 1 259 . 38 LEU H H 7.706 . 1 260 . 38 LEU HA H 4.659 . 1 261 . 38 LEU HB2 H 1.682 . 1 262 . 38 LEU HB3 H 1.550 . 1 263 . 38 LEU HD1 H 0.563 . 1 264 . 38 LEU HD2 H 0.790 . 1 265 . 38 LEU CA C 54.06 . 1 266 . 38 LEU CB C 42.82 . 1 267 . 38 LEU CG C 25.68 . 1 268 . 38 LEU CD1 C 25.68 . 1 269 . 38 LEU CD2 C 23.48 . 1 270 . 38 LEU N N 120.73 . 1 271 . 39 THR H H 8.062 . 1 272 . 39 THR HA H 4.352 . 1 273 . 39 THR HB H 4.655 . 1 274 . 39 THR HG2 H 1.141 . 1 275 . 39 THR CA C 61.02 . 1 276 . 39 THR CB C 70.97 . 1 277 . 39 THR CG2 C 21.45 . 1 278 . 39 THR N N 111.06 . 1 279 . 40 VAL H H 8.623 . 1 280 . 40 VAL HA H 3.687 . 1 281 . 40 VAL HB H 2.009 . 1 282 . 40 VAL HG1 H 0.924 . 1 283 . 40 VAL HG2 H 1.097 . 1 284 . 40 VAL CA C 67.10 . 1 285 . 40 VAL CB C 31.77 . 1 286 . 40 VAL CG1 C 20.83 . 1 287 . 40 VAL CG2 C 22.65 . 1 288 . 40 VAL N N 121.33 . 1 289 . 41 ALA H H 8.346 . 1 290 . 41 ALA HA H 4.111 . 1 291 . 41 ALA HB H 1.347 . 1 292 . 41 ALA CA C 55.24 . 1 293 . 41 ALA CB C 19.06 . 1 294 . 41 ALA N N 121.12 . 1 295 . 42 GLN H H 7.476 . 1 296 . 42 GLN HA H 3.647 . 1 297 . 42 GLN HB2 H 2.312 . 1 298 . 42 GLN HB3 H 1.749 . 1 299 . 42 GLN HG2 H 2.312 . 2 300 . 42 GLN HG3 H 2.200 . 2 301 . 42 GLN HE21 H 6.955 . 2 302 . 42 GLN HE22 H 5.479 . 2 303 . 42 GLN CA C 59.10 . 1 304 . 42 GLN CB C 27.90 . 1 305 . 42 GLN CG C 33.98 . 1 306 . 42 GLN N N 114.70 . 1 307 . 42 GLN NE2 N 108.07 . 1 308 . 43 ASN H H 8.645 . 1 309 . 43 ASN HA H 4.351 . 1 310 . 43 ASN HB2 H 2.740 . 2 311 . 43 ASN HB3 H 2.665 . 2 312 . 43 ASN HD21 H 7.125 . 1 313 . 43 ASN HD22 H 7.125 . 1 314 . 43 ASN CA C 56.60 . 1 315 . 43 ASN CB C 39.48 . 1 316 . 43 ASN N N 116.84 . 1 317 . 43 ASN ND2 N 114.91 . 1 318 . 44 GLN H H 8.390 . 1 319 . 44 GLN HA H 4.026 . 1 320 . 44 GLN HB2 H 2.311 . 1 321 . 44 GLN HB3 H 2.010 . 1 322 . 44 GLN HG2 H 2.664 . 2 323 . 44 GLN HG3 H 2.311 . 2 324 . 44 GLN HE21 H 7.159 . 1 325 . 44 GLN HE22 H 6.789 . 1 326 . 44 GLN CA C 59.62 . 1 327 . 44 GLN CB C 28.45 . 1 328 . 44 GLN CG C 34.80 . 1 329 . 44 GLN N N 119.62 . 1 330 . 44 GLN NE2 N 110.42 . 1 331 . 45 VAL H H 7.691 . 1 332 . 45 VAL HA H 3.411 . 1 333 . 45 VAL HB H 2.008 . 1 334 . 45 VAL HG1 H 0.706 . 1 335 . 45 VAL HG2 H 0.924 . 1 336 . 45 VAL CA C 66.83 . 1 337 . 45 VAL CB C 31.77 . 1 338 . 45 VAL CG1 C 22.37 . 1 339 . 45 VAL CG2 C 23.48 . 1 340 . 45 VAL N N 118.77 . 1 341 . 46 LEU H H 8.302 . 1 342 . 46 LEU HA H 3.823 . 1 343 . 46 LEU HB2 H 1.964 . 2 344 . 46 LEU HB3 H 1.461 . 2 345 . 46 LEU HD1 H 0.922 . 1 346 . 46 LEU HD2 H 0.795 . 1 347 . 46 LEU CA C 57.99 . 1 348 . 46 LEU CB C 41.42 . 1 349 . 46 LEU CG C 25.96 . 1 350 . 46 LEU CD1 C 23.64 . 1 351 . 46 LEU CD2 C 25.96 . 1 352 . 46 LEU N N 119.19 . 1 353 . 47 ASN H H 8.606 . 1 354 . 47 ASN HA H 4.351 . 1 355 . 47 ASN HB2 H 2.876 . 1 356 . 47 ASN HB3 H 2.701 . 1 357 . 47 ASN HD21 H 7.519 . 2 358 . 47 ASN HD22 H 6.774 . 2 359 . 47 ASN CA C 56.06 . 1 360 . 47 ASN CB C 37.83 . 1 361 . 47 ASN N N 116.20 . 1 362 . 47 ASN ND2 N 111.06 . 1 363 . 48 LEU H H 7.389 . 1 364 . 48 LEU HA H 4.097 . 1 365 . 48 LEU HB2 H 1.834 . 1 366 . 48 LEU HB3 H 1.357 . 1 367 . 48 LEU HD1 H 0.879 . 1 368 . 48 LEU HD2 H 0.857 . 1 369 . 48 LEU CA C 58.00 . 1 370 . 48 LEU CB C 41.71 . 1 371 . 48 LEU CG C 26.24 . 1 372 . 48 LEU CD1 C 26.24 . 1 373 . 48 LEU CD2 C 23.49 . 1 374 . 48 LEU N N 120.26 . 1 375 . 49 ILE H H 7.737 . 1 376 . 49 ILE HA H 3.665 . 1 377 . 49 ILE HB H 1.926 . 1 378 . 49 ILE HG12 H 1.966 . 2 379 . 49 ILE HG13 H 0.880 . 2 380 . 49 ILE HG2 H 0.877 . 1 381 . 49 ILE HD1 H 0.663 . 1 382 . 49 ILE CA C 66.00 . 1 383 . 49 ILE CB C 38.66 . 1 384 . 49 ILE CG1 C 30.67 . 1 385 . 49 ILE CG2 C 17.13 . 1 386 . 49 ILE CD1 C 15.47 . 1 387 . 49 ILE N N 120.26 . 1 388 . 50 LYS H H 8.996 . 1 389 . 50 LYS HA H 4.135 . 1 390 . 50 LYS HB2 H 1.878 . 1 391 . 50 LYS HB3 H 1.878 . 1 392 . 50 LYS HG2 H 1.661 . 1 393 . 50 LYS HG3 H 1.661 . 1 394 . 50 LYS HD2 H 1.560 . 1 395 . 50 LYS HD3 H 1.560 . 1 396 . 50 LYS HE2 H 2.986 . 2 397 . 50 LYS HE3 H 2.887 . 2 398 . 50 LYS CA C 59.65 . 1 399 . 50 LYS CB C 33.23 . 1 400 . 50 LYS CG C 26.06 . 1 401 . 50 LYS CD C 29.90 . 1 402 . 50 LYS CE C 41.83 . 1 403 . 50 LYS N N 120.48 . 1 404 . 51 ALA H H 7.303 . 1 405 . 51 ALA HA H 4.265 . 1 406 . 51 ALA HB H 1.487 . 1 407 . 51 ALA CA C 52.47 . 1 408 . 51 ALA CB C 19.20 . 1 409 . 51 ALA N N 117.70 . 1 410 . 52 CYS H H 7.304 . 1 411 . 52 CYS HA H 4.744 . 1 412 . 52 CYS HB2 H 3.138 . 1 413 . 52 CYS HB3 H 3.138 . 1 414 . 52 CYS CA C 56.73 . 1 415 . 52 CYS CB C 28.47 . 1 416 . 52 CYS N N 120.79 . 1 417 . 53 PRO HA H 4.746 . 1 418 . 53 PRO HB2 H 2.171 . 1 419 . 53 PRO HB3 H 2.171 . 1 420 . 53 PRO HG2 H 1.908 . 1 421 . 53 PRO HG3 H 1.908 . 1 422 . 53 PRO HD2 H 4.226 . 2 423 . 53 PRO HD3 H 3.961 . 2 424 . 53 PRO CA C 63.49 . 1 425 . 53 PRO CB C 32.21 . 1 426 . 53 PRO CG C 26.41 . 1 427 . 53 PRO CD C 51.02 . 1 428 . 54 ARG H H 7.649 . 1 429 . 54 ARG HA H 4.565 . 1 430 . 54 ARG HB2 H 2.098 . 1 431 . 54 ARG HB3 H 2.098 . 1 432 . 54 ARG HG2 H 1.705 . 1 433 . 54 ARG HG3 H 1.705 . 1 434 . 54 ARG HD2 H 3.267 . 1 435 . 54 ARG HD3 H 3.267 . 1 436 . 54 ARG CA C 54.96 . 1 437 . 54 ARG CB C 29.35 . 1 438 . 54 ARG N N 122.40 . 1 439 . 55 PRO HA H 4.268 . 1 440 . 55 PRO HB2 H 1.965 . 1 441 . 55 PRO HB3 H 2.399 . 1 442 . 55 PRO HG2 H 2.220 . 2 443 . 55 PRO HG3 H 2.095 . 2 444 . 55 PRO HD2 H 3.965 . 2 445 . 55 PRO HD3 H 3.875 . 2 446 . 55 PRO CA C 65.46 . 1 447 . 55 PRO CB C 31.80 . 1 448 . 55 PRO CG C 27.63 . 1 449 . 55 PRO CD C 50.82 . 1 450 . 56 GLU H H 9.905 . 1 451 . 56 GLU HA H 4.194 . 1 452 . 56 GLU HB2 H 1.876 . 2 453 . 56 GLU HB3 H 1.819 . 2 454 . 56 GLU HG2 H 2.486 . 2 455 . 56 GLU HG3 H 2.183 . 2 456 . 56 GLU CA C 57.16 . 1 457 . 56 GLU CB C 28.45 . 1 458 . 56 GLU CG C 35.62 . 1 459 . 56 GLU N N 115.77 . 1 460 . 57 GLY H H 7.519 . 1 461 . 57 GLY HA2 H 4.311 . 2 462 . 57 GLY HA3 H 3.725 . 2 463 . 57 GLY CA C 44.47 . 1 464 . 57 GLY N N 108.16 . 1 465 . 58 LEU H H 8.517 . 1 466 . 58 LEU HA H 4.657 . 1 467 . 58 LEU HB2 H 1.531 . 1 468 . 58 LEU HB3 H 1.878 . 1 469 . 58 LEU HD1 H 1.011 . 1 470 . 58 LEU HD2 H 0.836 . 1 471 . 58 LEU CA C 54.13 . 1 472 . 58 LEU CB C 45.30 . 1 473 . 58 LEU CG C 27.28 . 1 474 . 58 LEU CD1 C 25.12 . 1 475 . 58 LEU CD2 C 27.62 . 1 476 . 58 LEU N N 119.91 . 1 477 . 59 ASN H H 8.777 . 1 478 . 59 ASN HA H 5.133 . 1 479 . 59 ASN HB2 H 2.658 . 1 480 . 59 ASN HB3 H 1.922 . 1 481 . 59 ASN HD21 H 7.002 . 2 482 . 59 ASN HD22 H 6.908 . 2 483 . 59 ASN CA C 51.63 . 1 484 . 59 ASN CB C 39.77 . 1 485 . 59 ASN N N 122.40 . 1 486 . 59 ASN ND2 N 112.56 . 1 487 . 60 PHE H H 8.778 . 1 488 . 60 PHE HA H 4.038 . 1 489 . 60 PHE HB2 H 3.311 . 1 490 . 60 PHE HB3 H 3.179 . 1 491 . 60 PHE HD1 H 7.239 . 1 492 . 60 PHE HD2 H 7.239 . 1 493 . 60 PHE HE1 H 7.185 . 1 494 . 60 PHE HE2 H 7.185 . 1 495 . 60 PHE HZ H 7.279 . 1 496 . 60 PHE CA C 62.41 . 1 497 . 60 PHE CB C 39.92 . 1 498 . 60 PHE N N 122.89 . 1 499 . 61 GLN H H 8.473 . 1 500 . 61 GLN HA H 3.842 . 1 501 . 61 GLN HB2 H 2.094 . 1 502 . 61 GLN HB3 H 2.094 . 1 503 . 61 GLN HG2 H 2.442 . 2 504 . 61 GLN HG3 H 2.394 . 2 505 . 61 GLN HE21 H 7.635 . 2 506 . 61 GLN HE22 H 6.985 . 2 507 . 61 GLN CA C 58.82 . 1 508 . 61 GLN CB C 27.90 . 1 509 . 61 GLN CG C 33.70 . 1 510 . 61 GLN N N 117.05 . 1 511 . 61 GLN NE2 N 112.84 . 1 512 . 62 ASP H H 7.953 . 1 513 . 62 ASP HA H 4.468 . 1 514 . 62 ASP HB2 H 2.919 . 1 515 . 62 ASP HB3 H 2.659 . 1 516 . 62 ASP CA C 57.43 . 1 517 . 62 ASP CB C 41.15 . 1 518 . 62 ASP N N 119.19 . 1 519 . 63 LEU H H 7.735 . 1 520 . 63 LEU HA H 3.830 . 1 521 . 63 LEU HB2 H 1.663 . 1 522 . 63 LEU HB3 H 1.458 . 1 523 . 63 LEU HG H 1.487 . 1 524 . 63 LEU HD1 H 0.707 . 1 525 . 63 LEU HD2 H 0.707 . 1 526 . 63 LEU CA C 58.28 . 1 527 . 63 LEU CB C 41.98 . 1 528 . 63 LEU CG C 26.81 . 1 529 . 63 LEU CD1 C 25.411 . 1 530 . 63 LEU CD2 C 25.844 . 1 531 . 63 LEU N N 120.14 . 1 532 . 64 LYS H H 7.972 . 1 533 . 64 LYS HA H 3.647 . 1 534 . 64 LYS HB2 H 1.620 . 1 535 . 64 LYS HB3 H 1.620 . 1 536 . 64 LYS HG2 H 1.313 . 1 537 . 64 LYS HG3 H 1.313 . 1 538 . 64 LYS HE2 H 2.919 . 1 539 . 64 LYS HE3 H 2.919 . 1 540 . 64 LYS CA C 58.89 . 1 541 . 64 LYS CB C 31.75 . 1 542 . 64 LYS CG C 24.31 . 1 543 . 64 LYS CD C 29.72 . 1 544 . 64 LYS CE C 41.97 . 1 545 . 64 LYS N N 117.27 . 1 546 . 65 ASN H H 7.848 . 1 547 . 65 ASN HA H 4.447 . 1 548 . 65 ASN HB2 H 2.950 . 1 549 . 65 ASN HB3 H 2.877 . 1 550 . 65 ASN HD21 H 7.768 . 2 551 . 65 ASN HD22 H 7.001 . 2 552 . 65 ASN CA C 54.96 . 1 553 . 65 ASN CB C 38.66 . 1 554 . 65 ASN N N 115.34 . 1 555 . 65 ASN ND2 N 112.56 . 1 556 . 66 GLN H H 7.650 . 1 557 . 66 GLN HA H 4.351 . 1 558 . 66 GLN HB2 H 2.008 . 1 559 . 66 GLN HB3 H 2.267 . 1 560 . 66 GLN HG2 H 2.616 . 2 561 . 66 GLN HG3 H 2.401 . 2 562 . 66 GLN HE21 H 7.266 . 2 563 . 66 GLN HE22 H 6.677 . 2 564 . 66 GLN CA C 57.16 . 1 565 . 66 GLN CB C 30.65 . 1 566 . 66 GLN CG C 34.80 . 1 567 . 66 GLN N N 116.63 . 1 568 . 66 GLN NE2 N 109.99 . 1 569 . 67 LEU H H 7.694 . 1 570 . 67 LEU HA H 4.663 . 1 571 . 67 LEU HB2 H 1.661 . 1 572 . 67 LEU HB3 H 1.128 . 1 573 . 67 LEU HG H 1.487 . 1 574 . 67 LEU HD1 H 0.751 . 1 575 . 67 LEU HD2 H 0.834 . 1 576 . 67 LEU CA C 54.47 . 1 577 . 67 LEU CB C 40.05 . 1 578 . 67 LEU CG C 25.68 . 1 579 . 67 LEU CD1 C 27.89 . 1 580 . 67 LEU CD2 C 23.49 . 1 581 . 67 LEU N N 123.55 . 1 582 . 68 LYS H H 7.562 . 1 583 . 68 LYS HA H 4.091 . 1 584 . 68 LYS HB2 H 1.859 . 1 585 . 68 LYS HB3 H 1.859 . 1 586 . 68 LYS HG2 H 1.486 . 1 587 . 68 LYS HG3 H 1.486 . 1 588 . 68 LYS HD2 H 1.723 . 1 589 . 68 LYS HD3 H 1.723 . 1 590 . 68 LYS HE2 H 3.066 . 1 591 . 68 LYS HE3 H 3.066 . 1 592 . 68 LYS CA C 59.10 . 1 593 . 68 LYS CB C 32.32 . 1 594 . 68 LYS CG C 25.14 . 1 595 . 68 LYS CD C 29.31 . 1 596 . 68 LYS CE C 42.15 . 1 597 . 68 LYS N N 118.34 . 1 598 . 69 HIS H H 8.520 . 1 599 . 69 HIS HA H 4.565 . 1 600 . 69 HIS HB2 H 3.224 . 2 601 . 69 HIS HB3 H 2.962 . 2 602 . 69 HIS HD2 H 6.963 . 1 603 . 69 HIS HE1 H 7.684 . 1 604 . 69 HIS CA C 56.33 . 1 605 . 69 HIS CB C 30.11 . 1 606 . 69 HIS N N 114.49 . 1 607 . 70 MET H H 7.606 . 1 608 . 70 MET HA H 4.506 . 1 609 . 70 MET HB2 H 1.924 . 2 610 . 70 MET HB3 H 1.658 . 2 611 . 70 MET HG2 H 2.269 . 2 612 . 70 MET HG3 H 1.618 . 2 613 . 70 MET HE H 1.908 . 1 614 . 70 MET CA C 54.68 . 1 615 . 70 MET CB C 35.36 . 1 616 . 70 MET CG C 31.76 . 1 617 . 70 MET CE C 16.87 . 1 618 . 70 MET N N 122.29 . 1 619 . 71 SER H H 8.515 . 1 620 . 71 SER HA H 4.467 . 1 621 . 71 SER HB2 H 4.309 . 2 622 . 71 SER HB3 H 4.049 . 2 623 . 71 SER CA C 56.89 . 1 624 . 71 SER CB C 64.60 . 1 625 . 71 SER N N 117.27 . 1 626 . 72 VAL H H 8.933 . 1 627 . 72 VAL HA H 3.646 . 1 628 . 72 VAL HB H 2.183 . 1 629 . 72 VAL HG1 H 1.096 . 1 630 . 72 VAL HG2 H 1.177 . 1 631 . 72 VAL CA C 67.38 . 1 632 . 72 VAL CB C 31.48 . 1 633 . 72 VAL CG1 C 21.27 . 1 634 . 72 VAL CG2 C 23.20 . 1 635 . 72 VAL N N 122.40 . 1 636 . 73 SER H H 8.398 . 1 637 . 73 SER HA H 4.214 . 1 638 . 73 SER HB2 H 3.918 . 2 639 . 73 SER HB3 H 3.665 . 2 640 . 73 SER CA C 61.58 . 1 641 . 73 SER CB C 62.40 . 1 642 . 73 SER N N 114.06 . 1 643 . 74 SER H H 7.988 . 1 644 . 74 SER HA H 4.253 . 1 645 . 74 SER HB2 H 3.875 . 1 646 . 74 SER HB3 H 3.962 . 1 647 . 74 SER CA C 62.13 . 1 648 . 74 SER CB C 62.86 . 1 649 . 74 SER N N 119.62 . 1 650 . 75 ILE H H 8.170 . 1 651 . 75 ILE HA H 3.490 . 1 652 . 75 ILE HB H 1.880 . 1 653 . 75 ILE HG12 H 1.836 . 2 654 . 75 ILE HG13 H 0.705 . 2 655 . 75 ILE HG2 H 0.706 . 1 656 . 75 ILE HD1 H 0.706 . 1 657 . 75 ILE CA C 66.27 . 1 658 . 75 ILE CB C 38.12 . 1 659 . 75 ILE CG1 C 29.28 . 1 660 . 75 ILE CG2 C 18.79 . 1 661 . 75 ILE CD1 C 14.65 . 1 662 . 75 ILE N N 124.76 . 1 663 . 76 LYS H H 8.691 . 1 664 . 76 LYS HA H 3.998 . 1 665 . 76 LYS HB2 H 2.052 . 2 666 . 76 LYS HB3 H 1.923 . 2 667 . 76 LYS HG2 H 1.465 . 2 668 . 76 LYS HG3 H 1.358 . 2 669 . 76 LYS HD2 H 1.620 . 2 670 . 76 LYS HD3 H 1.357 . 2 671 . 76 LYS HE2 H 2.790 . 2 672 . 76 LYS HE3 H 2.747 . 2 673 . 76 LYS CA C 59.65 . 1 674 . 76 LYS CB C 32.04 . 1 675 . 76 LYS CG C 25.13 . 1 676 . 76 LYS CD C 28.46 . 1 677 . 76 LYS CE C 41.98 . 1 678 . 76 LYS N N 120.48 . 1 679 . 77 GLN H H 8.212 . 1 680 . 77 GLN HA H 4.155 . 1 681 . 77 GLN HB2 H 2.139 . 1 682 . 77 GLN HB3 H 2.139 . 1 683 . 77 GLN HG2 H 2.659 . 2 684 . 77 GLN HG3 H 2.443 . 2 685 . 77 GLN HE21 H 7.409 . 2 686 . 77 GLN HE22 H 6.768 . 2 687 . 77 GLN CA C 59.10 . 1 688 . 77 GLN CB C 28.45 . 1 689 . 77 GLN CG C 34.26 . 1 690 . 77 GLN N N 117.05 . 1 691 . 77 GLN NE2 N 111.49 . 1 692 . 78 ALA H H 7.781 . 1 693 . 78 ALA HA H 4.309 . 1 694 . 78 ALA HB H 1.445 . 1 695 . 78 ALA CA C 55.51 . 1 696 . 78 ALA CB C 17.95 . 1 697 . 78 ALA N N 122.40 . 1 698 . 79 VAL H H 8.562 . 1 699 . 79 VAL HA H 3.295 . 1 700 . 79 VAL HB H 1.965 . 1 701 . 79 VAL HG1 H 0.273 . 1 702 . 79 VAL HG2 H 0.706 . 1 703 . 79 VAL CA C 67.10 . 1 704 . 79 VAL CB C 31.49 . 1 705 . 79 VAL CG1 C 21.53 . 1 706 . 79 VAL CG2 C 23.20 . 1 707 . 79 VAL N N 118.12 . 1 708 . 80 ASP H H 8.644 . 1 709 . 80 ASP HA H 4.350 . 1 710 . 80 ASP HB2 H 2.790 . 2 711 . 80 ASP HB3 H 2.701 . 2 712 . 80 ASP CA C 57.72 . 1 713 . 80 ASP CB C 40.05 . 1 714 . 80 ASP N N 121.98 . 1 715 . 81 PHE H H 8.041 . 1 716 . 81 PHE HA H 4.292 . 1 717 . 81 PHE HB2 H 3.354 . 1 718 . 81 PHE HB3 H 3.179 . 1 719 . 81 PHE HD1 H 7.076 . 1 720 . 81 PHE HD2 H 7.076 . 1 721 . 81 PHE HE1 H 7.271 . 1 722 . 81 PHE HE2 H 7.271 . 1 723 . 81 PHE HZ H 7.335 . 1 724 . 81 PHE CA C 62.14 . 1 725 . 81 PHE CB C 39.58 . 1 726 . 81 PHE N N 121.12 . 1 727 . 82 LEU H H 8.780 . 1 728 . 82 LEU HA H 3.881 . 1 729 . 82 LEU HB2 H 2.051 . 1 730 . 82 LEU HB3 H 1.315 . 1 731 . 82 LEU HG H 2.268 . 1 732 . 82 LEU HD1 H 0.880 . 1 733 . 82 LEU HD2 H 0.925 . 1 734 . 82 LEU CA C 57.99 . 1 735 . 82 LEU CB C 43.08 . 1 736 . 82 LEU CG C 26.30 . 1 737 . 82 LEU CD1 C 26.30 . 1 738 . 82 LEU CD2 C 24.27 . 1 739 . 82 LEU N N 117.91 . 1 740 . 83 SER H H 8.604 . 1 741 . 83 SER HA H 4.526 . 1 742 . 83 SER HB2 H 4.016 . 2 743 . 83 SER HB3 H 3.961 . 2 744 . 83 SER CA C 61.03 . 1 745 . 83 SER CB C 63.04 . 1 746 . 83 SER N N 115.77 . 1 747 . 84 ASN H H 8.434 . 1 748 . 84 ASN HA H 4.429 . 1 749 . 84 ASN HB2 H 2.961 . 1 750 . 84 ASN HB3 H 2.789 . 1 751 . 84 ASN HD21 H 7.659 . 2 752 . 84 ASN HD22 H 6.909 . 2 753 . 84 ASN CA C 56.35 . 1 754 . 84 ASN CB C 38.66 . 1 755 . 84 ASN N N 123.26 . 1 756 . 84 ASN ND2 N 113.63 . 1 757 . 85 GLU H H 7.952 . 1 758 . 85 GLU HA H 4.067 . 1 759 . 85 GLU HB2 H 1.443 . 1 760 . 85 GLU HB3 H 2.029 . 1 761 . 85 GLU HG2 H 1.617 . 2 762 . 85 GLU HG3 H 1.543 . 2 763 . 85 GLU CA C 56.06 . 1 764 . 85 GLU CB C 30.38 . 1 765 . 85 GLU CG C 36.03 . 1 766 . 85 GLU N N 115.22 . 1 767 . 86 GLY H H 7.520 . 1 768 . 86 GLY HA2 H 4.091 . 2 769 . 86 GLY HA3 H 3.916 . 2 770 . 86 GLY CA C 45.85 . 1 771 . 86 GLY N N 105.25 . 1 772 . 87 HIS H H 8.387 . 1 773 . 87 HIS HA H 4.624 . 1 774 . 87 HIS HB2 H 2.965 . 1 775 . 87 HIS HB3 H 3.266 . 1 776 . 87 HIS HD2 H 6.732 . 1 777 . 87 HIS HE1 H 7.773 . 1 778 . 87 HIS CA C 58.27 . 1 779 . 87 HIS CB C 33.42 . 1 780 . 87 HIS N N 118.34 . 1 781 . 88 ILE H H 7.393 . 1 782 . 88 ILE HA H 5.504 . 1 783 . 88 ILE HB H 1.966 . 1 784 . 88 ILE HG12 H 1.226 . 2 785 . 88 ILE HG13 H 0.576 . 2 786 . 88 ILE HG2 H 0.796 . 1 787 . 88 ILE HD1 H 0.532 . 1 788 . 88 ILE CA C 58.55 . 1 789 . 88 ILE CB C 42.50 . 1 790 . 88 ILE CG1 C 23.76 . 1 791 . 88 ILE CG2 C 18.50 . 1 792 . 88 ILE CD1 C 14.37 . 1 793 . 88 ILE N N 109.14 . 1 794 . 89 TYR H H 9.126 . 1 795 . 89 TYR HA H 5.151 . 1 796 . 89 TYR HB2 H 3.180 . 1 797 . 89 TYR HB3 H 2.964 . 1 798 . 89 TYR HD1 H 6.973 . 1 799 . 89 TYR HD2 H 6.973 . 1 800 . 89 TYR HE1 H 6.593 . 1 801 . 89 TYR HE2 H 6.593 . 1 802 . 89 TYR CA C 55.79 . 1 803 . 89 TYR CB C 40.60 . 1 804 . 89 TYR N N 117.27 . 1 805 . 90 SER H H 8.648 . 1 806 . 90 SER HA H 5.425 . 1 807 . 90 SER HB2 H 4.178 . 1 808 . 90 SER HB3 H 3.786 . 1 809 . 90 SER CA C 56.62 . 1 810 . 90 SER CB C 64.65 . 1 811 . 90 SER N N 116.73 . 1 812 . 91 THR H H 7.871 . 1 813 . 91 THR HA H 4.448 . 1 814 . 91 THR HB H 4.352 . 1 815 . 91 THR HG2 H 0.879 . 1 816 . 91 THR CA C 59.65 . 1 817 . 91 THR CB C 67.94 . 1 818 . 91 THR CG2 C 22.37 . 1 819 . 91 THR N N 111.28 . 1 820 . 92 VAL H H 8.865 . 1 821 . 92 VAL HA H 3.881 . 1 822 . 92 VAL HB H 2.096 . 1 823 . 92 VAL HG1 H 0.837 . 1 824 . 92 VAL HG2 H 0.446 . 1 825 . 92 VAL CA C 62.97 . 1 826 . 92 VAL CB C 31.50 . 1 827 . 92 VAL CG1 C 21.55 . 1 828 . 92 VAL CG2 C 18.25 . 1 829 . 92 VAL N N 117.48 . 1 830 . 93 ASP H H 7.867 . 1 831 . 93 ASP HA H 4.409 . 1 832 . 93 ASP HB2 H 3.048 . 1 833 . 93 ASP HB3 H 3.048 . 1 834 . 93 ASP CA C 53.02 . 1 835 . 93 ASP CB C 40.87 . 1 836 . 93 ASP N N 117.05 . 1 837 . 94 ASP H H 8.084 . 1 838 . 94 ASP HA H 4.482 . 1 839 . 94 ASP HB2 H 2.574 . 1 840 . 94 ASP HB3 H 2.834 . 1 841 . 94 ASP CA C 55.51 . 1 842 . 94 ASP CB C 40.88 . 1 843 . 94 ASP N N 114.36 . 1 844 . 95 ASP H H 8.430 . 1 845 . 95 ASP HA H 4.800 . 1 846 . 95 ASP HB2 H 2.529 . 1 847 . 95 ASP HB3 H 2.877 . 1 848 . 95 ASP CA C 53.85 . 1 849 . 95 ASP CB C 43.03 . 1 850 . 95 ASP N N 117.06 . 1 851 . 96 HIS H H 6.941 . 1 852 . 96 HIS HA H 4.802 . 1 853 . 96 HIS HB2 H 3.069 . 2 854 . 96 HIS HB3 H 2.701 . 2 855 . 96 HIS HD2 H 6.619 . 1 856 . 96 HIS HE1 H 8.024 . 1 857 . 96 HIS CA C 55.49 . 1 858 . 96 HIS CB C 40.86 . 1 859 . 96 HIS N N 116.20 . 1 860 . 97 PHE H H 8.387 . 1 861 . 97 PHE HA H 5.392 . 1 862 . 97 PHE HB2 H 2.529 . 1 863 . 97 PHE HB3 H 2.877 . 1 864 . 97 PHE HD1 H 6.811 . 1 865 . 97 PHE HD2 H 6.811 . 1 866 . 97 PHE HE1 H 7.059 . 1 867 . 97 PHE HE2 H 7.059 . 1 868 . 97 PHE HZ H 7.298 . 1 869 . 97 PHE CA C 56.62 . 1 870 . 97 PHE CB C 44.74 . 1 871 . 97 PHE N N 117.27 . 1 872 . 98 LYS H H 8.518 . 1 873 . 98 LYS HA H 4.569 . 1 874 . 98 LYS HB2 H 0.837 . 1 875 . 98 LYS HB3 H 1.444 . 1 876 . 98 LYS HG2 H 1.359 . 1 877 . 98 LYS HG3 H 1.359 . 1 878 . 98 LYS HD2 H 1.706 . 2 879 . 98 LYS HD3 H 1.594 . 2 880 . 98 LYS HE2 H 3.050 . 1 881 . 98 LYS HE3 H 3.050 . 1 882 . 98 LYS CA C 54.13 . 1 883 . 98 LYS CB C 37.29 . 1 884 . 98 LYS CG C 25.14 . 1 885 . 98 LYS CD C 29.00 . 1 886 . 98 LYS CE C 41.98 . 1 887 . 98 LYS N N 120.26 . 1 888 . 99 SER H H 8.647 . 1 889 . 99 SER HA H 4.917 . 1 890 . 99 SER HB2 H 4.092 . 1 891 . 99 SER HB3 H 3.789 . 1 892 . 99 SER CA C 57.99 . 1 893 . 99 SER CB C 64.34 . 1 894 . 99 SER N N 114.70 . 1 895 . 100 THR H H 8.206 . 1 896 . 100 THR HA H 4.233 . 1 897 . 100 THR HB H 4.311 . 1 898 . 100 THR HG2 H 1.198 . 1 899 . 100 THR CA C 63.52 . 1 900 . 100 THR CB C 69.32 . 1 901 . 100 THR CG2 C 22.92 . 1 902 . 100 THR N N 118.84 . 1 903 . 101 ASP H H 8.518 . 1 904 . 101 ASP HA H 4.700 . 1 905 . 101 ASP HB2 H 2.775 . 2 906 . 101 ASP HB3 H 2.659 . 2 907 . 101 ASP CA C 54.24 . 1 908 . 101 ASP CB C 41.16 . 1 909 . 101 ASP N N 122.19 . 1 910 . 102 ALA H H 8.170 . 1 911 . 102 ALA HA H 4.388 . 1 912 . 102 ALA HB H 1.453 . 1 913 . 102 ALA CA C 52.47 . 1 914 . 102 ALA CB C 20.05 . 1 915 . 102 ALA N N 125.19 . 1 916 . 103 GLU H H 8.009 . 1 917 . 103 GLU HA H 4.113 . 1 918 . 103 GLU HB2 H 2.048 . 2 919 . 103 GLU HB3 H 1.922 . 2 920 . 103 GLU HG2 H 2.224 . 1 921 . 103 GLU HG3 H 2.224 . 1 922 . 103 GLU CA C 58.16 . 1 923 . 103 GLU CB C 31.21 . 1 924 . 103 GLU N N 125.40 . 1 stop_ save_