data_4528 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; 1H, 13C, and 15N Chemical Shift Assignments for the N-terminal receiver domain of NtrC (phosphorylated) ; _BMRB_accession_number 4528 _BMRB_flat_file_name bmr4528.str _Entry_type original _Submission_date 1999-11-05 _Accession_date 1999-12-06 _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 Kern D. . . 2 Volkman B. F. . 3 Luginbuhl P. . . 4 Nohaile M. J. . 5 Kustu S. . . 6 Wemmer D. E. . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 600 "13C chemical shifts" 363 "15N chemical shifts" 113 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2000-06-16 original author . stop_ loop_ _Related_BMRB_accession_number _Relationship 4527 'phosphorylated form' stop_ _Original_release_date 2000-06-16 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; Structure of a Transiently Phosphorylated "Switch" in Bacterial Signal Transduction ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code 20085967 _PubMed_ID ? loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Kern D. . . 2 Volkman B. F. . 3 Luginbuhl P. . . 4 Nohaile M. J. . 5 Kustu S. . . 6 Wemmer D. E. . stop_ _Journal_abbreviation Nature _Journal_name_full Nature _Journal_volume 402 _Journal_issue . _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 894 _Page_last 898 _Year 1999 _Details . loop_ _Keyword 'RECEIVER DOMAIN' PHOSPHORYLATION 'SIGNAL TRANSDUCTION' 'CONFORMATIONAL REARRANGEMENT' 'TWO-COMPONENT SYSTEM' stop_ save_ ####################################### # Cited references within the entry # ####################################### save_ref_1 _Saveframe_category citation _Citation_full . _Citation_title 'Three-dimensional solution structure of the N-terminal receiver domain of NTRC.' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 7827089 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Volkman 'B. F.' F. . 2 Nohaile 'M. J.' J. . 3 Amy 'N. K.' K. . 4 Kustu S. . . 5 Wemmer 'D. E.' E. . stop_ _Journal_abbreviation Biochemistry _Journal_name_full Biochemistry _Journal_volume 34 _Journal_issue 4 _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 1413 _Page_last 1424 _Year 1995 _Details ; NTRC is a transcriptional enhancer binding protein whose N-terminal domain is a member of the family of receiver domains of two-component regulatory systems. Using 3D and 4D NMR spectroscopy, we have completed the 1H, 15N, and 13C assignments and determined the solution structure of the N-terminal receiver domain of the NTRC protein. Determination of the three-dimensional structure was carried out with the program X-PLOR (Briinger, 1992) using a total of 915 NMR-derived distance and dihedral angle restraints. The resultant family of structures has an average root mean square deviation of 0.81 A from the average structure for the backbone atoms involved in well-defined secondary structure. The structure is comprised of five alpha-helices and a five-stranded parallel beta-sheet, in a (beta/alpha)5 topology. Comparison of the solution structure of the NTRC receiver domain with the crystal structures of the homologous protein CheY in both the Mg(2+)-free and Mg(2+)-bound forms [Stock, A.M., Mottonen, J. M., Stock, J. B., & Schutt, C. E. (1989) Nature 337, 745-749; Volz, K., & Matsumura, P. (1991) J. Biol. Chem. 296, 15511-15519; Stock, A. M., Martinez-Hackert, E., Rasmussen, B. F., West, A. H., Stock, J. B., Ringe, D., & Petsko, G. A. (1993) Biochemistry 32, 13375-13380; Bellsolell, L., Prieto, J., Serrano, L., & Coll, M. (1994) J. Mol. Biol. 238, 489-495] reveals a very similar fold, with the only significant difference occurring in the positioning of helix 4 relative to the rest of the protein. Examination of the conformation of consensus residues of the receiver domain superfamily [Volz, K. (1993) Biochemistry 32, 11741-11753] in the structures of the NTRC receiver domain and CheY establishes the structural importance of residues whose side chains are involved in hydrogen bonding or hydrophobic core interactions. The importance of some nonconsensus residues which may be conserved for their ability to fulfill helix capping roles is also discussed. ; save_ ################################## # Molecular system description # ################################## save_system_P-NtrCr _Saveframe_category molecular_system _Mol_system_name 'NITROGEN REGULATION PROTEIN C' _Abbreviation_common P-NtrCr _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label P-NtrCr $P-NtrCr PO4 $PO4 stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state monomer _System_paramagnetic no _System_thiol_state 'all free' _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_P-NtrCr _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'NITROGEN REGULATION PROTEIN' _Abbreviation_common P-NtrCr _Molecular_mass . _Mol_thiol_state 'all free' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 124 _Mol_residue_sequence ; MQRGIVWVVDDDSSIRWVLE RALAGAGLTCTTFENGNEVL AALASKTPDVLLSDIRMPGM DGLALLKQIKQRHPMLPVII MTAHSDLDAAVSAYQQGAFD YLPKPFDIDEAVALVERAIS HYQE ; loop_ _Residue_seq_code _Residue_label 1 MET 2 GLN 3 ARG 4 GLY 5 ILE 6 VAL 7 TRP 8 VAL 9 VAL 10 ASP 11 ASP 12 ASP 13 SER 14 SER 15 ILE 16 ARG 17 TRP 18 VAL 19 LEU 20 GLU 21 ARG 22 ALA 23 LEU 24 ALA 25 GLY 26 ALA 27 GLY 28 LEU 29 THR 30 CYS 31 THR 32 THR 33 PHE 34 GLU 35 ASN 36 GLY 37 ASN 38 GLU 39 VAL 40 LEU 41 ALA 42 ALA 43 LEU 44 ALA 45 SER 46 LYS 47 THR 48 PRO 49 ASP 50 VAL 51 LEU 52 LEU 53 SER 54 ASP 55 ILE 56 ARG 57 MET 58 PRO 59 GLY 60 MET 61 ASP 62 GLY 63 LEU 64 ALA 65 LEU 66 LEU 67 LYS 68 GLN 69 ILE 70 LYS 71 GLN 72 ARG 73 HIS 74 PRO 75 MET 76 LEU 77 PRO 78 VAL 79 ILE 80 ILE 81 MET 82 THR 83 ALA 84 HIS 85 SER 86 ASP 87 LEU 88 ASP 89 ALA 90 ALA 91 VAL 92 SER 93 ALA 94 TYR 95 GLN 96 GLN 97 GLY 98 ALA 99 PHE 100 ASP 101 TYR 102 LEU 103 PRO 104 LYS 105 PRO 106 PHE 107 ASP 108 ILE 109 ASP 110 GLU 111 ALA 112 VAL 113 ALA 114 LEU 115 VAL 116 GLU 117 ARG 118 ALA 119 ILE 120 SER 121 HIS 122 TYR 123 GLN 124 GLU stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-07-14 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 25124 Receiver_Domain_of_NtrC 100.00 124 100.00 100.00 1.52e-84 BMRB 25125 Receiver_Domain_of_NtrC 100.00 124 100.00 100.00 1.52e-84 BMRB 4527 "Nitrogen regulatory protein C N-terminal receiver domain" 100.00 124 100.00 100.00 1.52e-84 PDB 1DC7 'Structure Of A Transiently Phosphorylated "switch" In Bacterial Signal Transduction' 99.19 124 100.00 100.00 1.15e-83 PDB 1DC8 'Structure Of A Transiently Phosphorylated "switch" In Bacterial Signal Transduction' 99.19 124 99.19 99.19 1.09e-82 PDB 1J56 "Minimized Average Structure Of Beryllofluoride-Activated Ntrc Receiver Domain: Model Structure Incorporating Active Site Contac" 100.00 124 100.00 100.00 1.52e-84 PDB 1KRW "Solution Structure And Backbone Dynamics Of Beryllofluoride- Activated Ntrc Receiver Domain" 99.19 124 100.00 100.00 1.14e-83 PDB 1KRX "Solution Structure Of Beryllofluoride-Activated Ntrc Receiver Domain: Model Structures Incorporating Active Site Contacts" 100.00 124 100.00 100.00 1.52e-84 PDB 1NTR "Solution Structure Of The N-Terminal Receiver Domain Of Ntrc" 100.00 124 100.00 100.00 1.52e-84 PDB 2MSK "Solution Structure And Chemical Shift Assignments For Bef3 Activated Receiver Domain Of Nitrogen Regulatory Protein C (ntrc) At" 100.00 124 100.00 100.00 1.52e-84 PDB 2MSL "Solution Structure And Chemical Shift Assignments For The Apo Form Of The Receiver Domain Of Nitrogen Regulatory Protein C (ntr" 100.00 124 100.00 100.00 1.52e-84 DBJ BAB38213 "response regulator for gln GlnG [Escherichia coli O157:H7 str. Sakai]" 100.00 469 98.39 98.39 1.03e-78 DBJ BAE77441 "fused DNA-binding response regulator in two-component regulatory system with GlnL, nitrogen regulator I (NRI) [Escherichia coli" 100.00 469 98.39 98.39 1.03e-78 DBJ BAG79675 "two-component regulator protein [Escherichia coli SE11]" 100.00 469 98.39 98.39 1.12e-78 DBJ BAI27885 "fused DNA-binding response regulator GlnG in two-component regulatory system with GlnL: response regulator/sigma 54 interaction" 100.00 469 98.39 98.39 1.03e-78 DBJ BAI33008 "fused DNA-binding response regulator GlnG in two-component regulatory system with GlnL: response regulator/sigma 54 interaction" 100.00 469 98.39 98.39 1.12e-78 EMBL CAA28808 "unnamed protein product [Escherichia coli K-12]" 100.00 468 98.39 98.39 9.28e-79 EMBL CAA59425 "nitrogen regulatory protein C [Salmonella enterica subsp. enterica serovar Typhimurium]" 100.00 469 100.00 100.00 2.17e-80 EMBL CAD03095 "Two-component system, response regulator [Salmonella enterica subsp. enterica serovar Typhi str. CT18]" 100.00 469 99.19 99.19 1.82e-79 EMBL CAP78325 "Nitrogen regulation protein NR(I) [Escherichia coli LF82]" 100.00 469 98.39 98.39 1.36e-78 EMBL CAQ34219 "NtrC transcriptional dual regulator, subunit of NtrC-Phosphorylated transcriptional dual regulator [Escherichia coli BL21(DE3)]" 100.00 469 98.39 98.39 1.12e-78 GB AAB03002 "CG Site No. 702 [Escherichia coli str. K-12 substr. MG1655]" 100.00 469 98.39 98.39 1.03e-78 GB AAC76865 "fused DNA-binding response regulator in two-component regulatory system with GlnL: response regulator/sigma54 interaction prote" 100.00 469 98.39 98.39 1.03e-78 GB AAG59057 "response regulator for gln (sensor glnL) (nitrogen regulator I, NRI) [Escherichia coli O157:H7 str. EDL933]" 100.00 469 98.39 98.39 7.85e-79 GB AAL22844 "EBP family response regulator in two-component regulatory system with GlnL [Salmonella enterica subsp. enterica serovar Typhimu" 100.00 469 100.00 100.00 2.02e-80 GB AAN45373 "sensor glnL response regulator (nitrogen regulator I, NRI) [Shigella flexneri 2a str. 301]" 100.00 469 98.39 98.39 1.11e-78 PIR AC0950 "Two-component system, response regulator STY3876 [imported] - Salmonella enterica subsp. enterica serovar Typhi (strain CT18)" 100.00 469 99.19 99.19 1.82e-79 PIR E86074 "hypothetical protein glnG [imported] - Escherichia coli (strain O157:H7, substrain EDL933)" 100.00 469 98.39 98.39 7.85e-79 REF NP_312817 "nitrogen regulation protein NR(I) [Escherichia coli O157:H7 str. Sakai]" 100.00 469 98.39 98.39 1.03e-78 REF NP_418304 "fused DNA-binding response regulator in two-component regulatory system with GlnL: response regulator/sigma54 interaction prote" 100.00 469 98.39 98.39 1.03e-78 REF NP_458044 "two-component system response regulator [Salmonella enterica subsp. enterica serovar Typhi str. CT18]" 100.00 469 99.19 99.19 1.82e-79 REF NP_462885 "nitrogen regulation protein NR(I) [Salmonella enterica subsp. enterica serovar Typhimurium str. LT2]" 100.00 469 100.00 100.00 2.02e-80 REF NP_709666 "nitrogen regulation protein NR(I) [Shigella flexneri 2a str. 301]" 100.00 469 98.39 98.39 1.11e-78 SP P0AFB8 "RecName: Full=Nitrogen regulation protein NR(I)" 100.00 469 98.39 98.39 1.03e-78 SP P0AFB9 "RecName: Full=Nitrogen regulation protein NR(I)" 100.00 469 98.39 98.39 1.03e-78 SP P41789 "RecName: Full=Nitrogen regulation protein NR(I)" 100.00 469 100.00 100.00 2.02e-80 stop_ save_ ############# # Ligands # ############# save_PO4 _Saveframe_category ligand _Mol_type non-polymer _Name_common "PO4 (PHOSPHATE ION)" _BMRB_code . _PDB_code PO4 _Molecular_mass 94.971 _Mol_charge -3 _Mol_paramagnetic . _Mol_aromatic no _Details ; Information obtained from PDB's Chemical Component Dictionary at http://wwpdb-remediation.rutgers.edu/downloads.html Downloaded on Fri Jul 15 11:47:14 2011 ; loop_ _Atom_name _PDB_atom_name _Atom_type _Atom_chirality _Atom_charge _Atom_oxidation_number _Atom_unpaired_electrons P P P . 0 . ? O1 O1 O . 0 . ? O2 O2 O . -1 . ? O3 O3 O . -1 . ? O4 O4 O . -1 . ? stop_ loop_ _Bond_order _Bond_atom_one_atom_name _Bond_atom_two_atom_name _PDB_bond_atom_one_atom_name _PDB_bond_atom_two_atom_name DOUB P O1 ? ? SING P O2 ? ? SING P O3 ? ? SING P O4 ? ? stop_ _Mol_thiol_state . _Sequence_homology_query_date . save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $P-NtrCr 'Salmonella typhimurium' 602 Bacteria . Salmonella typhimurium 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 $P-NtrCr 'recombinant technology' Bacteria Escherichia coli BL21 . 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 $P-NtrCr 0.3 mM [U-15N] 'Na phosphate' 200 mM . MgCl2 50 mM . Carbamoylphosphate 200 mM . stop_ save_ save_sample_2 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $P-NtrCr 0.3 mM '[U-15N; U-13C]' 'Na phosphate' 200 mM . MgCl2 50 mM . Carbamoylphosphate 200 mM . stop_ save_ ############################ # Computer software used # ############################ save_DYANA _Saveframe_category software _Name DYANA _Version 1.5 loop_ _Task 'STRUCTURE SOLUTION' 'DATA ANALYSIS' stop_ _Details 'PETER GUENTERT' save_ save_FELIX _Saveframe_category software _Name FELIX _Version 95.0 loop_ _Task PROCESSING stop_ _Details MSI save_ save_XWINNMR _Saveframe_category software _Name XWINNMR _Version 1.5 loop_ _Task COLLECTION stop_ _Details BRUKER save_ save_XEASY _Saveframe_category software _Name XEASY _Version 1.3.13 loop_ _Task 'DATA ANALYSIS' stop_ _Details MUMENTHALER save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model DMX _Field_strength 750 _Details . save_ ############################# # NMR applied experiments # ############################# save_3D_15N-SEPARATED_NOESY_1 _Saveframe_category NMR_applied_experiment _Experiment_name '3D 15N-SEPARATED_NOESY' _Sample_label . save_ save_3D_13C-SEPARATED_NOESY_2 _Saveframe_category NMR_applied_experiment _Experiment_name '3D 13C-SEPARATED_NOESY' _Sample_label . save_ save_2D_NOESY_3 _Saveframe_category NMR_applied_experiment _Experiment_name '2D NOESY' _Sample_label . save_ save_NMR_spec_expt__0_1 _Saveframe_category NMR_applied_experiment _Experiment_name '3D 15N-SEPARATED_NOESY' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_2 _Saveframe_category NMR_applied_experiment _Experiment_name '3D 13C-SEPARATED_NOESY' _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_ ####################### # Sample conditions # ####################### save_sample_cond_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 6.75 0.3 n/a temperature 298 1 K 'ionic strength' 375 125 mM pressure 1 . atm 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_chemical_shift_set_1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $sample_cond_1 _Chem_shift_reference_set_label $chemical_shift_reference _Mol_system_component_name P-NtrCr _Text_data_format . _Text_data . loop_ _Atom_shift_assign_ID _Residue_author_seq_code _Residue_seq_code _Residue_label _Atom_name _Atom_type _Chem_shift_value _Chem_shift_value_error _Chem_shift_ambiguity_code 1 . 2 GLN CA C 55.6 . 1 2 . 2 GLN HA H 4.52 . 1 3 . 2 GLN CG C 33.9 . 1 4 . 2 GLN HG2 H 2.38 . 2 5 . 2 GLN HG3 H 2.36 . 2 6 . 3 ARG N N 121.9 . 1 7 . 3 ARG H H 8.59 . 1 8 . 3 ARG CA C 56.1 . 1 9 . 3 ARG HA H 4.45 . 1 10 . 3 ARG CB C 31.4 . 1 11 . 3 ARG HB2 H 1.89 . 2 12 . 3 ARG HB3 H 1.78 . 2 13 . 3 ARG CG C 27.4 . 1 14 . 3 ARG HG2 H 1.71 . 2 15 . 3 ARG HG3 H 1.65 . 2 16 . 3 ARG CD C 43.2 . 1 17 . 3 ARG HD2 H 3.21 . 1 18 . 3 ARG HD3 H 3.21 . 1 19 . 4 GLY N N 108.6 . 1 20 . 4 GLY H H 8.24 . 1 21 . 4 GLY CA C 45.4 . 1 22 . 4 GLY HA3 H 3.89 . 2 23 . 4 GLY HA2 H 4.03 . 2 24 . 5 ILE N N 122.7 . 1 25 . 5 ILE H H 9.69 . 1 26 . 5 ILE CA C 60.7 . 1 27 . 5 ILE HA H 4.77 . 1 28 . 5 ILE CB C 39.8 . 1 29 . 5 ILE HB H 1.65 . 1 30 . 5 ILE HG2 H 0.97 . 1 31 . 5 ILE CG2 C 18.5 . 1 32 . 5 ILE CG1 C 27.4 . 1 33 . 5 ILE HG12 H 1.09 . 1 34 . 5 ILE HG13 H 1.09 . 1 35 . 5 ILE HD1 H 0.98 . 1 36 . 5 ILE CD1 C 13.5 . 1 37 . 6 VAL N N 127.2 . 1 38 . 6 VAL H H 9.23 . 1 39 . 6 VAL CA C 59.1 . 1 40 . 6 VAL HA H 4.98 . 1 41 . 6 VAL CB C 34.6 . 1 42 . 6 VAL HB H 1.90 . 1 43 . 6 VAL HG1 H 0.93 . 2 44 . 6 VAL HG2 H 0.87 . 2 45 . 6 VAL CG1 C 21.3 . 1 46 . 6 VAL CG2 C 21.3 . 1 47 . 7 TRP N N 127.5 . 1 48 . 7 TRP H H 8.63 . 1 49 . 7 TRP CA C 52.8 . 1 50 . 7 TRP HA H 6.52 . 1 51 . 7 TRP CB C 33.3 . 1 52 . 7 TRP HB2 H 3.20 . 2 53 . 7 TRP HB3 H 3.21 . 2 54 . 7 TRP CD1 C 123.4 . 1 55 . 7 TRP CE3 C 119.8 . 1 56 . 7 TRP NE1 N 127.5 . 1 57 . 7 TRP HD1 H 7.27 . 1 58 . 7 TRP HE3 H 6.97 . 1 59 . 7 TRP CZ3 C 121.9 . 1 60 . 7 TRP CZ2 C 113.5 . 1 61 . 7 TRP HE1 H 10.28 . 1 62 . 7 TRP HZ3 H 6.91 . 1 63 . 7 TRP CH2 C 126.1 . 1 64 . 7 TRP HZ2 H 7.24 . 1 65 . 7 TRP HH2 H 7.01 . 1 66 . 8 VAL N N 122.5 . 1 67 . 8 VAL H H 8.76 . 1 68 . 8 VAL CA C 60.5 . 1 69 . 8 VAL HA H 5.18 . 1 70 . 8 VAL CB C 35.9 . 1 71 . 8 VAL HB H 1.85 . 1 72 . 8 VAL HG1 H 0.92 . 2 73 . 8 VAL CG1 C 21.7 . 1 74 . 9 VAL N N 126.5 . 1 75 . 9 VAL H H 9.19 . 1 76 . 9 VAL CA C 58.4 . 1 77 . 9 VAL HA H 5.25 . 1 78 . 9 VAL CB C 33.1 . 1 79 . 9 VAL HB H 2.19 . 1 80 . 9 VAL HG1 H 1.06 . 2 81 . 9 VAL HG2 H 0.74 . 2 82 . 9 VAL CG1 C 20.3 . 1 83 . 9 VAL CG2 C 21.5 . 1 84 . 10 ASP N N 125.2 . 1 85 . 10 ASP H H 8.09 . 1 86 . 10 ASP CA C 55.4 . 1 87 . 10 ASP HA H 4.51 . 1 88 . 10 ASP CB C 44.2 . 1 89 . 10 ASP HB2 H 2.56 . 2 90 . 10 ASP HB3 H 2.45 . 2 91 . 11 ASP N N 122.2 . 1 92 . 11 ASP H H 9.07 . 1 93 . 11 ASP CA C 55.4 . 1 94 . 11 ASP HA H 4.69 . 1 95 . 12 ASP N N 124.8 . 1 96 . 12 ASP H H 10.26 . 1 97 . 12 ASP CA C 53.1 . 1 98 . 12 ASP HA H 4.87 . 1 99 . 12 ASP CB C 41.3 . 1 100 . 12 ASP HB2 H 3.08 . 2 101 . 12 ASP HB3 H 2.65 . 2 102 . 13 SER N N 123.9 . 1 103 . 13 SER H H 9.17 . 1 104 . 13 SER CA C 61.4 . 1 105 . 13 SER HA H 3.78 . 1 106 . 13 SER CB C 62.7 . 1 107 . 13 SER HB2 H 3.98 . 2 108 . 13 SER HB3 H 3.88 . 2 109 . 14 SER N N 118.8 . 1 110 . 14 SER H H 8.56 . 1 111 . 14 SER CA C 61.7 . 1 112 . 14 SER HA H 4.35 . 1 113 . 14 SER CB C 62.6 . 1 114 . 14 SER HB2 H 4.04 . 1 115 . 14 SER HB3 H 4.04 . 1 116 . 15 ILE N N 122.7 . 1 117 . 15 ILE H H 7.08 . 1 118 . 15 ILE CA C 60.7 . 1 119 . 15 ILE HA H 4.07 . 1 120 . 15 ILE CB C 36.0 . 1 121 . 15 ILE HB H 2.17 . 1 122 . 15 ILE HG2 H 0.99 . 1 123 . 15 ILE CG2 C 17.9 . 1 124 . 15 ILE CG1 C 27.4 . 1 125 . 15 ILE HG12 H 1.55 . 2 126 . 15 ILE HG13 H 1.32 . 2 127 . 15 ILE HD1 H 0.71 . 1 128 . 15 ILE CD1 C 9.1 . 1 129 . 16 ARG N N 117.0 . 1 130 . 16 ARG H H 7.45 . 1 131 . 16 ARG CA C 61.8 . 1 132 . 16 ARG HA H 3.77 . 1 133 . 16 ARG CB C 30.4 . 1 134 . 16 ARG HB2 H 2.16 . 1 135 . 16 ARG HB3 H 2.16 . 1 136 . 16 ARG CG C 29.0 . 1 137 . 16 ARG HG2 H 2.12 . 1 138 . 16 ARG HG3 H 2.12 . 1 139 . 17 TRP N N 117.0 . 1 140 . 17 TRP H H 8.03 . 1 141 . 17 TRP CA C 60.6 . 1 142 . 17 TRP HA H 4.53 . 1 143 . 17 TRP CB C 29.5 . 1 144 . 17 TRP HB2 H 3.52 . 2 145 . 17 TRP HB3 H 3.46 . 2 146 . 17 TRP CD1 C 127.3 . 1 147 . 17 TRP CE3 C 121.2 . 1 148 . 17 TRP NE1 N 129.2 . 1 149 . 17 TRP HD1 H 7.35 . 1 150 . 17 TRP HE3 H 7.66 . 1 151 . 17 TRP CZ3 C 121.4 . 1 152 . 17 TRP CZ2 C 114.3 . 1 153 . 17 TRP HE1 H 10.21 . 1 154 . 17 TRP HZ3 H 7.15 . 1 155 . 17 TRP CH2 C 124.3 . 1 156 . 17 TRP HZ2 H 7.49 . 1 157 . 17 TRP HH2 H 7.22 . 1 158 . 18 VAL N N 116.9 . 1 159 . 18 VAL H H 8.18 . 1 160 . 18 VAL CA C 66.0 . 1 161 . 18 VAL HA H 3.68 . 1 162 . 18 VAL CB C 32.0 . 1 163 . 18 VAL HB H 2.30 . 1 164 . 18 VAL HG1 H 1.25 . 2 165 . 18 VAL HG2 H 1.17 . 2 166 . 18 VAL CG1 C 22.5 . 1 167 . 18 VAL CG2 C 21.2 . 1 168 . 19 LEU N N 119.4 . 1 169 . 19 LEU H H 8.14 . 1 170 . 19 LEU CA C 57.8 . 1 171 . 19 LEU HA H 4.14 . 1 172 . 19 LEU CB C 41.7 . 1 173 . 19 LEU HB2 H 2.13 . 2 174 . 19 LEU HB3 H 1.23 . 2 175 . 19 LEU CG C 27.9 . 1 176 . 19 LEU HG H 1.88 . 1 177 . 19 LEU HD1 H 0.90 . 2 178 . 19 LEU HD2 H 0.71 . 2 179 . 19 LEU CD1 C 27.3 . 1 180 . 19 LEU CD2 C 22.0 . 1 181 . 20 GLU N N 120.3 . 1 182 . 20 GLU H H 8.51 . 1 183 . 20 GLU CA C 60.7 . 1 184 . 20 GLU HA H 4.08 . 1 185 . 20 GLU CB C 29.0 . 1 186 . 20 GLU HB2 H 2.12 . 1 187 . 20 GLU HB3 H 2.12 . 1 188 . 20 GLU CG C 36.0 . 1 189 . 20 GLU HG2 H 2.22 . 1 190 . 20 GLU HG3 H 2.22 . 1 191 . 21 ARG N N 116.1 . 1 192 . 21 ARG H H 7.67 . 1 193 . 21 ARG CA C 58.6 . 1 194 . 21 ARG HA H 3.96 . 1 195 . 21 ARG CB C 30.0 . 1 196 . 21 ARG HB2 H 1.69 . 2 197 . 21 ARG HB3 H 1.52 . 2 198 . 21 ARG CG C 26.5 . 1 199 . 21 ARG HG2 H 1.33 . 1 200 . 21 ARG HG3 H 1.33 . 1 201 . 21 ARG CD C 43.0 . 1 202 . 21 ARG HD2 H 2.74 . 1 203 . 21 ARG HD3 H 2.74 . 1 204 . 22 ALA CA C 54.8 . 1 205 . 22 ALA HA H 4.17 . 1 206 . 22 ALA HB H 1.46 . 1 207 . 22 ALA CB C 19.4 . 1 208 . 23 LEU N N 118.4 . 1 209 . 23 LEU H H 8.96 . 1 210 . 23 LEU CA C 57.9 . 1 211 . 23 LEU HA H 4.07 . 1 212 . 23 LEU CB C 39.9 . 1 213 . 23 LEU HB2 H 2.01 . 2 214 . 23 LEU HB3 H 1.19 . 2 215 . 23 LEU HD1 H 0.85 . 2 216 . 23 LEU HD2 H 0.87 . 2 217 . 23 LEU CD1 C 26.9 . 1 218 . 23 LEU CD2 C 24.5 . 1 219 . 24 ALA N N 122.2 . 1 220 . 24 ALA H H 8.36 . 1 221 . 24 ALA CA C 54.9 . 1 222 . 24 ALA HA H 4.74 . 1 223 . 24 ALA HB H 1.58 . 1 224 . 24 ALA CB C 17.8 . 1 225 . 25 GLY N N 107.1 . 1 226 . 25 GLY H H 8.01 . 1 227 . 25 GLY CA C 46.6 . 1 228 . 25 GLY HA3 H 3.93 . 2 229 . 25 GLY HA2 H 3.97 . 2 230 . 26 ALA N N 121.8 . 1 231 . 26 ALA H H 7.39 . 1 232 . 26 ALA CA C 51.6 . 1 233 . 26 ALA HA H 4.58 . 1 234 . 26 ALA HB H 1.53 . 1 235 . 26 ALA CB C 18.9 . 1 236 . 27 GLY N N 106.3 . 1 237 . 27 GLY H H 7.97 . 1 238 . 27 GLY CA C 45.5 . 1 239 . 27 GLY HA3 H 3.82 . 2 240 . 27 GLY HA2 H 4.34 . 2 241 . 28 LEU N N 120.1 . 1 242 . 28 LEU H H 7.72 . 1 243 . 28 LEU CA C 53.8 . 1 244 . 28 LEU HA H 4.65 . 1 245 . 28 LEU CB C 42.7 . 1 246 . 28 LEU HB2 H 1.50 . 2 247 . 28 LEU HB3 H 1.23 . 2 248 . 28 LEU CG C 28.0 . 1 249 . 28 LEU HG H 1.52 . 1 250 . 28 LEU HD1 H 0.80 . 2 251 . 28 LEU HD2 H 0.72 . 2 252 . 28 LEU CD1 C 26.1 . 1 253 . 28 LEU CD2 C 23.6 . 1 254 . 29 THR N N 118.3 . 1 255 . 29 THR H H 8.71 . 1 256 . 29 THR CA C 62.6 . 1 257 . 29 THR HA H 4.41 . 1 258 . 29 THR CB C 69.5 . 1 259 . 29 THR HB H 4.21 . 1 260 . 29 THR HG2 H 1.33 . 1 261 . 29 THR CG2 C 21.8 . 1 262 . 30 CYS N N 128.7 . 1 263 . 30 CYS H H 9.19 . 1 264 . 30 CYS CA C 56.5 . 1 265 . 30 CYS HA H 6.06 . 1 266 . 30 CYS CB C 29.7 . 1 267 . 30 CYS HB2 H 2.88 . 2 268 . 30 CYS HB3 H 2.49 . 2 269 . 30 CYS HG H 1.38 . 1 270 . 31 THR N N 126.5 . 1 271 . 31 THR H H 8.57 . 1 272 . 31 THR CA C 62.0 . 1 273 . 31 THR HA H 4.51 . 1 274 . 31 THR CB C 70.6 . 1 275 . 31 THR HB H 3.45 . 1 276 . 31 THR HG2 H 0.50 . 1 277 . 31 THR CG2 C 22.6 . 1 278 . 32 THR N N 116.1 . 1 279 . 32 THR H H 8.45 . 1 280 . 32 THR CA C 59.2 . 1 281 . 32 THR HA H 5.52 . 1 282 . 32 THR CB C 71.2 . 1 283 . 32 THR HB H 3.99 . 1 284 . 32 THR HG2 H 1.20 . 1 285 . 32 THR CG2 C 22.0 . 1 286 . 33 PHE N N 117.5 . 1 287 . 33 PHE H H 8.90 . 1 288 . 33 PHE CA C 56.6 . 1 289 . 33 PHE HA H 4.75 . 1 290 . 33 PHE CB C 43.3 . 1 291 . 33 PHE HB2 H 3.21 . 2 292 . 33 PHE HB3 H 2.53 . 2 293 . 33 PHE HD1 H 6.92 . 1 294 . 33 PHE HD2 H 6.92 . 1 295 . 33 PHE HE1 H 6.37 . 1 296 . 33 PHE HE2 H 6.37 . 1 297 . 33 PHE CD1 C 131.0 . 1 298 . 33 PHE CE1 C 130.9 . 1 299 . 34 GLU N N 118.3 . 1 300 . 34 GLU H H 9.20 . 1 301 . 34 GLU CA C 56.7 . 1 302 . 34 GLU HA H 4.50 . 1 303 . 34 GLU CB C 31.9 . 1 304 . 34 GLU HB2 H 2.15 . 2 305 . 34 GLU HB3 H 2.07 . 2 306 . 34 GLU CG C 36.6 . 1 307 . 34 GLU HG2 H 2.37 . 2 308 . 34 GLU HG3 H 2.22 . 2 309 . 35 ASN N N 108.2 . 1 310 . 35 ASN H H 7.35 . 1 311 . 35 ASN CA C 52.4 . 1 312 . 35 ASN HA H 5.04 . 1 313 . 35 ASN CB C 40.8 . 1 314 . 35 ASN HB2 H 3.09 . 2 315 . 35 ASN ND2 N 116.5 . 1 316 . 35 ASN HD21 H 7.12 . 2 317 . 35 ASN HD22 H 7.83 . 2 318 . 36 GLY N N 104.9 . 1 319 . 36 GLY H H 9.52 . 1 320 . 36 GLY CA C 47.6 . 1 321 . 36 GLY HA3 H 3.73 . 2 322 . 36 GLY HA2 H 3.80 . 2 323 . 37 ASN N N 120.6 . 1 324 . 37 ASN H H 8.53 . 1 325 . 37 ASN CA C 56.9 . 1 326 . 37 ASN HA H 4.42 . 1 327 . 37 ASN CB C 37.7 . 1 328 . 37 ASN HB2 H 2.91 . 2 329 . 37 ASN HB3 H 2.79 . 2 330 . 37 ASN ND2 N 112.0 . 1 331 . 37 ASN HD21 H 6.92 . 2 332 . 37 ASN HD22 H 7.77 . 2 333 . 38 GLU N N 119.3 . 1 334 . 38 GLU H H 8.21 . 1 335 . 38 GLU CA C 58.9 . 1 336 . 38 GLU HA H 4.13 . 1 337 . 38 GLU CB C 30.7 . 1 338 . 38 GLU HB2 H 2.36 . 1 339 . 38 GLU HB3 H 2.36 . 1 340 . 38 GLU CG C 36.5 . 1 341 . 38 GLU HG2 H 2.68 . 2 342 . 38 GLU HG3 H 2.42 . 2 343 . 39 VAL N N 119.2 . 1 344 . 39 VAL H H 6.94 . 1 345 . 39 VAL CA C 65.3 . 1 346 . 39 VAL HA H 2.65 . 1 347 . 39 VAL CB C 31.1 . 1 348 . 39 VAL HB H 2.10 . 1 349 . 39 VAL HG1 H 0.94 . 2 350 . 39 VAL HG2 H 0.54 . 2 351 . 39 VAL CG1 C 21.4 . 1 352 . 39 VAL CG2 C 23.1 . 1 353 . 40 LEU N N 118.3 . 1 354 . 40 LEU H H 7.84 . 1 355 . 40 LEU CA C 58.1 . 1 356 . 40 LEU HA H 4.00 . 1 357 . 40 LEU CB C 40.9 . 1 358 . 40 LEU HB2 H 1.82 . 2 359 . 40 LEU HB3 H 1.55 . 2 360 . 40 LEU CG C 26.9 . 1 361 . 40 LEU HG H 1.74 . 1 362 . 40 LEU HD1 H 0.89 . 2 363 . 40 LEU HD2 H 0.82 . 2 364 . 40 LEU CD1 C 25.8 . 1 365 . 40 LEU CD2 C 22.9 . 1 366 . 41 ALA N N 120.1 . 1 367 . 41 ALA H H 7.78 . 1 368 . 41 ALA CA C 54.9 . 1 369 . 41 ALA HA H 4.23 . 1 370 . 41 ALA HB H 1.52 . 1 371 . 41 ALA CB C 17.8 . 1 372 . 42 ALA N N 122.7 . 1 373 . 42 ALA H H 7.64 . 1 374 . 42 ALA CA C 55.1 . 1 375 . 42 ALA HA H 4.29 . 1 376 . 42 ALA HB H 1.39 . 1 377 . 42 ALA CB C 19.7 . 1 378 . 43 LEU N N 119.4 . 1 379 . 43 LEU H H 8.40 . 1 380 . 43 LEU CA C 55.4 . 1 381 . 43 LEU HA H 5.34 . 1 382 . 43 LEU CB C 42.9 . 1 383 . 43 LEU HB2 H 2.01 . 2 384 . 43 LEU HB3 H 1.77 . 2 385 . 43 LEU CG C 26.9 . 1 386 . 43 LEU HG H 2.19 . 1 387 . 43 LEU HD1 H 0.89 . 2 388 . 43 LEU HD2 H 0.76 . 2 389 . 43 LEU CD1 C 26.1 . 1 390 . 43 LEU CD2 C 24.9 . 1 391 . 44 ALA N N 119.0 . 1 392 . 44 ALA H H 7.38 . 1 393 . 44 ALA CA C 54.4 . 1 394 . 44 ALA HA H 4.31 . 1 395 . 44 ALA HB H 1.63 . 1 396 . 44 ALA CB C 18.7 . 1 397 . 45 SER N N 108.4 . 1 398 . 45 SER H H 7.84 . 1 399 . 45 SER CA C 58.8 . 1 400 . 45 SER HA H 4.82 . 1 401 . 45 SER CB C 65.5 . 1 402 . 45 SER HB2 H 4.05 . 2 403 . 45 SER HB3 H 3.95 . 2 404 . 46 LYS N N 123.1 . 1 405 . 46 LYS H H 8.17 . 1 406 . 46 LYS CA C 55.7 . 1 407 . 46 LYS HA H 4.68 . 1 408 . 46 LYS CB C 36.5 . 1 409 . 46 LYS HB2 H 2.09 . 2 410 . 46 LYS HB3 H 1.99 . 2 411 . 46 LYS CG C 24.8 . 1 412 . 46 LYS HG2 H 1.59 . 2 413 . 46 LYS HG3 H 1.56 . 2 414 . 46 LYS CD C 29.3 . 1 415 . 46 LYS HD2 H 1.90 . 1 416 . 46 LYS HD3 H 1.90 . 1 417 . 46 LYS CE C 42.2 . 1 418 . 46 LYS HE2 H 3.11 . 1 419 . 46 LYS HE3 H 3.11 . 1 420 . 47 THR N N 111.7 . 1 421 . 47 THR H H 7.86 . 1 422 . 47 THR CA C 57.9 . 1 423 . 47 THR HA H 4.36 . 1 424 . 47 THR CB C 70.7 . 1 425 . 47 THR HB H 3.69 . 1 426 . 47 THR HG2 H 0.84 . 1 427 . 47 THR CG2 C 21.4 . 1 428 . 48 PRO CD C 47.9 . 1 429 . 48 PRO CA C 61.1 . 1 430 . 48 PRO HA H 4.01 . 1 431 . 48 PRO CB C 30.5 . 1 432 . 48 PRO HB2 H -0.28 . 2 433 . 48 PRO HB3 H 1.50 . 2 434 . 48 PRO CG C 26.2 . 1 435 . 48 PRO HG2 H 1.04 . 2 436 . 48 PRO HG3 H 0.83 . 2 437 . 48 PRO HD2 H 2.71 . 2 438 . 48 PRO HD3 H 1.25 . 2 439 . 49 ASP N N 114.9 . 1 440 . 49 ASP H H 8.62 . 1 441 . 49 ASP CA C 56.5 . 1 442 . 49 ASP HA H 4.53 . 1 443 . 49 ASP CB C 43.0 . 1 444 . 49 ASP HB2 H 2.63 . 1 445 . 49 ASP HB3 H 2.63 . 1 446 . 50 VAL N N 111.5 . 1 447 . 50 VAL H H 7.25 . 1 448 . 50 VAL CA C 60.4 . 1 449 . 50 VAL HA H 4.40 . 1 450 . 50 VAL CB C 34.4 . 1 451 . 50 VAL HB H 2.00 . 1 452 . 50 VAL HG1 H 0.85 . 2 453 . 50 VAL HG2 H 0.83 . 2 454 . 50 VAL CG1 C 21.5 . 1 455 . 50 VAL CG2 C 22.0 . 1 456 . 51 LEU N N 127.6 . 1 457 . 51 LEU H H 8.14 . 1 458 . 51 LEU CA C 53.2 . 1 459 . 51 LEU HA H 5.44 . 1 460 . 51 LEU CB C 46.7 . 1 461 . 51 LEU HB2 H 1.85 . 2 462 . 51 LEU HB3 H 1.15 . 2 463 . 51 LEU CG C 28.5 . 1 464 . 51 LEU HG H 1.54 . 1 465 . 51 LEU HD1 H 1.03 . 2 466 . 51 LEU HD2 H 0.89 . 2 467 . 51 LEU CD1 C 25.8 . 1 468 . 51 LEU CD2 C 27.0 . 1 469 . 52 LEU N N 128.9 . 1 470 . 52 LEU H H 9.35 . 1 471 . 52 LEU CA C 54.2 . 1 472 . 52 LEU HA H 5.38 . 1 473 . 52 LEU CB C 44.2 . 1 474 . 52 LEU HB2 H 1.85 . 2 475 . 52 LEU HB3 H 1.35 . 2 476 . 52 LEU CG C 29.4 . 1 477 . 52 LEU HG H 1.59 . 1 478 . 52 LEU HD1 H 0.77 . 2 479 . 52 LEU HD2 H 0.70 . 2 480 . 52 LEU CD1 C 24.9 . 1 481 . 52 LEU CD2 C 26.2 . 1 482 . 53 SER N N 116.7 . 1 483 . 53 SER H H 9.35 . 1 484 . 53 SER CA C 56.4 . 1 485 . 53 SER HA H 5.49 . 1 486 . 53 SER CB C 66.0 . 1 487 . 53 SER HB2 H 3.67 . 2 488 . 53 SER HB3 H 3.16 . 2 489 . 54 ASP N N 126.8 . 1 490 . 54 ASP H H 8.35 . 1 491 . 54 ASP CA C 52.6 . 1 492 . 54 ASP HA H 5.91 . 1 493 . 54 ASP CB C 43.9 . 1 494 . 54 ASP HB2 H 3.23 . 2 495 . 54 ASP HB3 H 4.22 . 2 496 . 55 ILE N N 117.5 . 1 497 . 55 ILE H H 8.08 . 1 498 . 56 ARG N N 120.5 . 1 499 . 56 ARG H H 10.05 . 1 500 . 57 MET N N 130.2 . 1 501 . 57 MET H H 7.63 . 1 502 . 57 MET CA C 53.9 . 1 503 . 57 MET HA H 4.82 . 1 504 . 57 MET CG C 32.8 . 1 505 . 57 MET HG2 H 2.83 . 2 506 . 57 MET HG3 H 2.23 . 2 507 . 58 PRO CD C 50.6 . 1 508 . 58 PRO CA C 63.1 . 1 509 . 58 PRO HA H 4.44 . 1 510 . 58 PRO CB C 32.1 . 1 511 . 58 PRO HB2 H 2.39 . 2 512 . 58 PRO HB3 H 2.01 . 2 513 . 58 PRO CG C 27.7 . 1 514 . 58 PRO HG2 H 2.26 . 2 515 . 58 PRO HG3 H 2.14 . 2 516 . 58 PRO HD2 H 3.88 . 2 517 . 58 PRO HD3 H 3.83 . 2 518 . 59 GLY N N 112.8 . 1 519 . 59 GLY H H 8.84 . 1 520 . 59 GLY CA C 46.5 . 1 521 . 59 GLY HA3 H 3.57 . 2 522 . 59 GLY HA2 H 4.30 . 2 523 . 60 MET N N 124.3 . 1 524 . 60 MET H H 7.89 . 1 525 . 60 MET CA C 56.1 . 1 526 . 60 MET HA H 4.40 . 1 527 . 60 MET CB C 35.0 . 1 528 . 60 MET HB2 H 2.22 . 2 529 . 60 MET HB3 H 1.81 . 2 530 . 61 ASP N N 125.4 . 1 531 . 61 ASP H H 8.54 . 1 532 . 61 ASP CA C 53.5 . 1 533 . 61 ASP HA H 4.94 . 1 534 . 61 ASP CB C 42.3 . 1 535 . 61 ASP HB2 H 3.42 . 2 536 . 61 ASP HB3 H 2.86 . 2 537 . 62 GLY N N 105.0 . 1 538 . 62 GLY H H 10.34 . 1 539 . 62 GLY CA C 46.7 . 1 540 . 62 GLY HA3 H 3.81 . 2 541 . 63 LEU N N 120.3 . 1 542 . 63 LEU H H 8.19 . 1 543 . 63 LEU CA C 57.2 . 1 544 . 63 LEU HA H 4.37 . 1 545 . 63 LEU CB C 40.0 . 1 546 . 63 LEU HB2 H 1.52 . 2 547 . 63 LEU HB3 H 2.11 . 2 548 . 63 LEU CG C 27.7 . 1 549 . 63 LEU HG H 1.71 . 1 550 . 63 LEU HD1 H 1.05 . 2 551 . 63 LEU HD2 H 0.87 . 2 552 . 63 LEU CD1 C 25.3 . 1 553 . 63 LEU CD2 C 24.1 . 1 554 . 64 ALA N N 126.4 . 1 555 . 64 ALA H H 8.40 . 1 556 . 64 ALA CA C 55.1 . 1 557 . 64 ALA HA H 4.17 . 1 558 . 64 ALA HB H 1.58 . 1 559 . 64 ALA CB C 18.2 . 1 560 . 65 LEU N N 120.1 . 1 561 . 65 LEU H H 8.52 . 1 562 . 66 LEU N N 120.8 . 1 563 . 66 LEU H H 8.25 . 1 564 . 66 LEU CA C 58.7 . 1 565 . 66 LEU HA H 3.92 . 1 566 . 67 LYS N N 117.0 . 1 567 . 67 LYS H H 7.77 . 1 568 . 67 LYS CA C 59.9 . 1 569 . 67 LYS HA H 4.10 . 1 570 . 67 LYS CB C 32.5 . 1 571 . 67 LYS HB2 H 2.00 . 2 572 . 67 LYS HB3 H 2.01 . 2 573 . 67 LYS CG C 25.0 . 1 574 . 67 LYS HG2 H 1.65 . 2 575 . 67 LYS HG3 H 1.43 . 2 576 . 67 LYS CD C 29.6 . 1 577 . 67 LYS HD2 H 1.75 . 1 578 . 67 LYS HD3 H 1.75 . 1 579 . 67 LYS CE C 42.0 . 1 580 . 67 LYS HE2 H 2.99 . 1 581 . 67 LYS HE3 H 2.99 . 1 582 . 68 GLN N N 116.9 . 1 583 . 68 GLN H H 7.79 . 1 584 . 68 GLN CA C 58.8 . 1 585 . 68 GLN HA H 4.10 . 1 586 . 68 GLN CB C 28.7 . 1 587 . 68 GLN HB2 H 2.26 . 2 588 . 68 GLN HB3 H 2.22 . 2 589 . 68 GLN CG C 34.1 . 1 590 . 68 GLN HG2 H 2.52 . 2 591 . 68 GLN NE2 N 111.1 . 1 592 . 68 GLN HE21 H 6.86 . 2 593 . 68 GLN HE22 H 7.35 . 2 594 . 69 ILE N N 120.6 . 1 595 . 69 ILE H H 9.05 . 1 596 . 69 ILE CA C 65.4 . 1 597 . 69 ILE HA H 3.63 . 1 598 . 69 ILE CB C 37.2 . 1 599 . 69 ILE HB H 2.05 . 1 600 . 69 ILE HG2 H 0.94 . 1 601 . 69 ILE CG2 C 18.0 . 1 602 . 69 ILE HD1 H 0.71 . 1 603 . 69 ILE CD1 C 14.0 . 1 604 . 70 LYS N N 117.9 . 1 605 . 70 LYS H H 8.67 . 1 606 . 70 LYS CA C 57.4 . 1 607 . 70 LYS HA H 4.01 . 1 608 . 70 LYS CB C 31.4 . 1 609 . 70 LYS HB2 H 2.13 . 1 610 . 70 LYS HB3 H 2.13 . 1 611 . 70 LYS CG C 24.4 . 1 612 . 70 LYS HG2 H 1.74 . 2 613 . 70 LYS HG3 H 1.69 . 2 614 . 70 LYS CD C 27.9 . 1 615 . 70 LYS HD2 H 1.88 . 2 616 . 70 LYS HD3 H 1.75 . 2 617 . 71 GLN N N 115.0 . 1 618 . 71 GLN H H 7.38 . 1 619 . 71 GLN CA C 58.2 . 1 620 . 71 GLN HA H 4.14 . 1 621 . 71 GLN CB C 28.7 . 1 622 . 71 GLN HB2 H 2.24 . 2 623 . 71 GLN HB3 H 2.19 . 2 624 . 71 GLN CG C 34.1 . 1 625 . 71 GLN HG2 H 2.61 . 2 626 . 71 GLN HG3 H 2.45 . 2 627 . 71 GLN NE2 N 111.5 . 1 628 . 71 GLN HE21 H 6.92 . 2 629 . 71 GLN HE22 H 7.49 . 2 630 . 72 ARG N N 116.1 . 1 631 . 72 ARG H H 7.34 . 1 632 . 72 ARG CA C 57.2 . 1 633 . 72 ARG HA H 4.21 . 1 634 . 72 ARG CB C 32.7 . 1 635 . 72 ARG HB2 H 1.60 . 1 636 . 72 ARG HB3 H 1.60 . 1 637 . 72 ARG CG C 27.5 . 1 638 . 72 ARG HG2 H 1.65 . 2 639 . 72 ARG HG3 H 1.54 . 2 640 . 72 ARG CD C 43.4 . 1 641 . 72 ARG HD2 H 3.20 . 2 642 . 72 ARG HD3 H 3.07 . 2 643 . 73 HIS N N 116.9 . 1 644 . 73 HIS H H 8.94 . 1 645 . 73 HIS CA C 53.3 . 1 646 . 73 HIS HA H 5.06 . 1 647 . 73 HIS CB C 30.6 . 1 648 . 73 HIS HB2 H 3.02 . 1 649 . 73 HIS HB3 H 3.02 . 1 650 . 73 HIS CD2 C 120.9 . 1 651 . 73 HIS CE1 C 139.0 . 1 652 . 73 HIS HD2 H 6.71 . 1 653 . 73 HIS HE1 H 7.96 . 1 654 . 74 PRO CD C 50.1 . 1 655 . 74 PRO CA C 65.4 . 1 656 . 74 PRO HA H 4.51 . 1 657 . 74 PRO CB C 32.4 . 1 658 . 74 PRO HB3 H 2.60 . 2 659 . 74 PRO CG C 27.3 . 1 660 . 74 PRO HG2 H 2.11 . 2 661 . 74 PRO HG3 H 2.01 . 2 662 . 74 PRO HD2 H 3.70 . 2 663 . 74 PRO HD3 H 3.31 . 2 664 . 75 MET N N 114.7 . 1 665 . 75 MET H H 8.78 . 1 666 . 75 MET CA C 54.3 . 1 667 . 75 MET HA H 4.66 . 1 668 . 75 MET CB C 31.5 . 1 669 . 75 MET HB2 H 2.30 . 2 670 . 75 MET HB3 H 2.06 . 2 671 . 75 MET CG C 32.7 . 1 672 . 75 MET HG2 H 2.76 . 2 673 . 75 MET HG3 H 2.52 . 2 674 . 76 LEU N N 125.8 . 1 675 . 76 LEU H H 7.44 . 1 676 . 76 LEU CA C 53.4 . 1 677 . 76 LEU HA H 4.34 . 1 678 . 76 LEU CB C 43.5 . 1 679 . 76 LEU HB2 H 1.87 . 2 680 . 76 LEU HB3 H 1.35 . 2 681 . 76 LEU CG C 27.1 . 1 682 . 76 LEU HG H 1.33 . 1 683 . 76 LEU HD1 H 0.45 . 2 684 . 76 LEU HD2 H 0.48 . 2 685 . 76 LEU CD1 C 25.2 . 1 686 . 76 LEU CD2 C 25.3 . 1 687 . 77 PRO CD C 51.1 . 1 688 . 77 PRO CA C 62.9 . 1 689 . 77 PRO HA H 4.52 . 1 690 . 77 PRO CB C 32.0 . 1 691 . 77 PRO HB2 H 1.77 . 2 692 . 77 PRO HB3 H 1.40 . 2 693 . 77 PRO CG C 28.4 . 1 694 . 77 PRO HG2 H 2.17 . 2 695 . 77 PRO HG3 H 1.75 . 2 696 . 77 PRO HD2 H 3.95 . 1 697 . 77 PRO HD3 H 3.95 . 1 698 . 78 VAL N N 122.8 . 1 699 . 78 VAL H H 8.53 . 1 700 . 78 VAL CA C 60.1 . 1 701 . 78 VAL HA H 5.13 . 1 702 . 78 VAL CB C 34.4 . 1 703 . 78 VAL HB H 1.94 . 1 704 . 78 VAL HG1 H 0.85 . 2 705 . 78 VAL HG2 H 0.98 . 2 706 . 78 VAL CG1 C 21.4 . 1 707 . 78 VAL CG2 C 21.4 . 1 708 . 79 ILE N N 128.9 . 1 709 . 79 ILE H H 9.54 . 1 710 . 79 ILE CA C 60.0 . 1 711 . 79 ILE HA H 4.53 . 1 712 . 79 ILE CB C 40.3 . 1 713 . 79 ILE HB H 1.68 . 1 714 . 79 ILE HG2 H 0.68 . 1 715 . 79 ILE CG2 C 18.3 . 1 716 . 79 ILE HD1 H 0.78 . 1 717 . 79 ILE CD1 C 14.9 . 1 718 . 80 ILE N N 128.6 . 1 719 . 80 ILE H H 7.98 . 1 720 . 80 ILE CA C 56.2 . 1 721 . 80 ILE HA H 5.24 . 1 722 . 80 ILE CB C 38.0 . 1 723 . 80 ILE HB H 1.93 . 1 724 . 80 ILE HG2 H 0.91 . 1 725 . 80 ILE CG2 C 18.2 . 1 726 . 80 ILE HD1 H 0.76 . 1 727 . 80 ILE CD1 C 9.0 . 1 728 . 81 MET N N 124.0 . 1 729 . 81 MET H H 9.05 . 1 730 . 81 MET CA C 52.7 . 1 731 . 81 MET HA H 5.57 . 1 732 . 81 MET CB C 36.4 . 1 733 . 81 MET HB2 H 1.95 . 2 734 . 81 MET HB3 H 1.84 . 2 735 . 81 MET CG C 32.3 . 1 736 . 81 MET HG2 H 2.59 . 2 737 . 81 MET HG3 H 2.35 . 2 738 . 82 THR N N 109.3 . 1 739 . 82 THR H H 7.20 . 1 740 . 82 THR CA C 60.4 . 1 741 . 82 THR HA H 5.57 . 1 742 . 82 THR CB C 68.8 . 1 743 . 82 THR HB H 4.43 . 1 744 . 82 THR HG2 H 1.14 . 1 745 . 82 THR CG2 C 18.1 . 1 746 . 83 ALA H H 9.52 . 1 747 . 83 ALA CA C 52.4 . 1 748 . 83 ALA HA H 4.67 . 1 749 . 83 ALA HB H 1.33 . 1 750 . 83 ALA CB C 19.5 . 1 751 . 84 HIS CD2 C 119.7 . 1 752 . 84 HIS CE1 C 138.4 . 1 753 . 84 HIS HD2 H 7.30 . 1 754 . 84 HIS HE1 H 8.23 . 1 755 . 85 SER CA C 58.7 . 1 756 . 85 SER HA H 4.42 . 1 757 . 85 SER CB C 63.2 . 1 758 . 85 SER HB2 H 4.00 . 2 759 . 87 LEU CA C 57.2 . 1 760 . 87 LEU HA H 4.17 . 1 761 . 87 LEU CB C 42.3 . 1 762 . 87 LEU HB2 H 1.69 . 2 763 . 87 LEU CG C 27.0 . 1 764 . 87 LEU HG H 1.71 . 1 765 . 88 ASP N N 117.8 . 1 766 . 88 ASP H H 8.24 . 1 767 . 88 ASP CA C 56.4 . 1 768 . 88 ASP HA H 4.45 . 1 769 . 88 ASP CB C 40.4 . 1 770 . 88 ASP HB2 H 2.70 . 1 771 . 88 ASP HB3 H 2.70 . 1 772 . 89 ALA N N 123.1 . 1 773 . 89 ALA H H 8.08 . 1 774 . 89 ALA CA C 54.9 . 1 775 . 89 ALA HA H 4.14 . 1 776 . 89 ALA HB H 1.57 . 1 777 . 89 ALA CB C 18.9 . 1 778 . 90 ALA N N 119.9 . 1 779 . 90 ALA H H 7.60 . 1 780 . 90 ALA CA C 55.2 . 1 781 . 90 ALA HA H 3.23 . 1 782 . 90 ALA HB H 0.98 . 1 783 . 90 ALA CB C 18.0 . 1 784 . 91 VAL N N 117.1 . 1 785 . 91 VAL H H 8.07 . 1 786 . 91 VAL CA C 66.2 . 1 787 . 91 VAL HA H 3.69 . 1 788 . 91 VAL CB C 31.7 . 1 789 . 91 VAL HB H 2.14 . 1 790 . 91 VAL HG1 H 0.99 . 2 791 . 91 VAL HG2 H 1.05 . 2 792 . 91 VAL CG1 C 21.0 . 1 793 . 91 VAL CG2 C 22.6 . 1 794 . 92 SER N N 115.3 . 1 795 . 92 SER H H 8.07 . 1 796 . 92 SER CA C 61.6 . 1 797 . 92 SER HA H 4.28 . 1 798 . 92 SER CB C 63.1 . 1 799 . 92 SER HB2 H 4.03 . 2 800 . 92 SER HB3 H 3.94 . 2 801 . 93 ALA N N 122.4 . 1 802 . 93 ALA H H 8.32 . 1 803 . 93 ALA CA C 55.4 . 1 804 . 93 ALA HA H 3.81 . 1 805 . 93 ALA HB H 1.33 . 1 806 . 93 ALA CB C 17.1 . 1 807 . 95 GLN N N 120.5 . 1 808 . 95 GLN H H 8.78 . 1 809 . 95 GLN CA C 58.8 . 1 810 . 95 GLN HA H 4.03 . 1 811 . 95 GLN CB C 28.4 . 1 812 . 95 GLN HB2 H 2.36 . 2 813 . 95 GLN CG C 34.2 . 1 814 . 95 GLN HG2 H 2.72 . 2 815 . 96 GLN N N 114.9 . 1 816 . 96 GLN H H 7.93 . 1 817 . 96 GLN CA C 55.4 . 1 818 . 96 GLN HA H 4.37 . 1 819 . 96 GLN CG C 34.3 . 1 820 . 96 GLN HG2 H 2.52 . 2 821 . 97 GLY N N 103.8 . 1 822 . 97 GLY H H 7.62 . 1 823 . 97 GLY CA C 45.5 . 1 824 . 97 GLY HA3 H 3.87 . 2 825 . 97 GLY HA2 H 4.36 . 2 826 . 98 ALA N N 123.4 . 1 827 . 98 ALA H H 8.51 . 1 828 . 98 ALA CA C 53.2 . 1 829 . 98 ALA HA H 4.30 . 1 830 . 98 ALA HB H 1.25 . 1 831 . 98 ALA CB C 18.5 . 1 832 . 99 PHE N N 123.7 . 1 833 . 99 PHE H H 9.61 . 1 834 . 99 PHE CA C 60.4 . 1 835 . 99 PHE HA H 4.32 . 1 836 . 99 PHE CB C 40.4 . 1 837 . 99 PHE HB2 H 3.48 . 2 838 . 99 PHE HD1 H 7.13 . 1 839 . 99 PHE HD2 H 7.13 . 1 840 . 99 PHE CD1 C 132.9 . 1 841 . 100 ASP N N 110.6 . 1 842 . 100 ASP H H 7.74 . 1 843 . 100 ASP CA C 52.6 . 1 844 . 100 ASP HA H 4.62 . 1 845 . 100 ASP CB C 45.0 . 1 846 . 100 ASP HB2 H 2.61 . 2 847 . 100 ASP HB3 H 2.50 . 2 848 . 101 TYR CA C 56.4 . 1 849 . 101 TYR HA H 5.39 . 1 850 . 101 TYR CB C 42.0 . 1 851 . 101 TYR HB2 H 2.89 . 2 852 . 101 TYR HD1 H 6.84 . 1 853 . 101 TYR HD2 H 6.84 . 1 854 . 101 TYR HE1 H 6.69 . 1 855 . 101 TYR HE2 H 6.69 . 1 856 . 101 TYR CD1 C 132.7 . 1 857 . 101 TYR CE1 C 117.7 . 1 858 . 102 LEU N N 130.3 . 1 859 . 102 LEU H H 9.10 . 1 860 . 102 LEU CA C 50.6 . 1 861 . 102 LEU HA H 4.77 . 1 862 . 102 LEU CB C 45.2 . 1 863 . 102 LEU HB2 H 1.48 . 2 864 . 102 LEU HB3 H 0.82 . 2 865 . 102 LEU CG C 26.1 . 1 866 . 102 LEU HG H 1.25 . 1 867 . 102 LEU HD1 H 0.18 . 2 868 . 102 LEU HD2 H 0.61 . 2 869 . 102 LEU CD1 C 24.9 . 1 870 . 102 LEU CD2 C 23.0 . 1 871 . 103 PRO CD C 50.6 . 1 872 . 103 PRO CA C 62.1 . 1 873 . 103 PRO HA H 4.95 . 1 874 . 103 PRO HD2 H 3.75 . 2 875 . 103 PRO HD3 H 3.61 . 2 876 . 104 LYS N N 119.0 . 1 877 . 104 LYS H H 7.98 . 1 878 . 104 LYS CA C 53.2 . 1 879 . 104 LYS HA H 4.49 . 1 880 . 104 LYS CE C 41.3 . 1 881 . 104 LYS HE2 H 2.98 . 2 882 . 104 LYS HE3 H 2.86 . 2 883 . 105 PRO CD C 50.3 . 1 884 . 105 PRO CA C 62.3 . 1 885 . 105 PRO HA H 4.58 . 1 886 . 105 PRO CG C 24.9 . 1 887 . 105 PRO HG2 H 1.96 . 1 888 . 105 PRO HG3 H 1.96 . 1 889 . 105 PRO HD2 H 3.69 . 2 890 . 105 PRO HD3 H 3.49 . 2 891 . 106 PHE CA C 53.2 . 1 892 . 106 PHE HA H 5.23 . 1 893 . 106 PHE CB C 40.5 . 1 894 . 106 PHE HB2 H 3.35 . 2 895 . 106 PHE HB3 H 3.17 . 2 896 . 106 PHE HD1 H 6.98 . 1 897 . 106 PHE HD2 H 6.98 . 1 898 . 106 PHE HE1 H 7.19 . 1 899 . 106 PHE HE2 H 7.19 . 1 900 . 106 PHE CD1 C 133.5 . 1 901 . 106 PHE CE1 C 130.4 . 1 902 . 107 ASP N N 122.2 . 1 903 . 107 ASP H H 9.15 . 1 904 . 107 ASP CA C 53.3 . 1 905 . 107 ASP HA H 4.94 . 1 906 . 107 ASP CB C 42.4 . 1 907 . 107 ASP HB2 H 2.88 . 2 908 . 107 ASP HB3 H 2.74 . 2 909 . 108 ILE N N 128.5 . 1 910 . 108 ILE H H 9.07 . 1 911 . 108 ILE CA C 63.1 . 1 912 . 108 ILE HA H 4.02 . 1 913 . 108 ILE CB C 37.7 . 1 914 . 108 ILE HB H 2.04 . 1 915 . 108 ILE HG2 H 1.02 . 1 916 . 108 ILE CG2 C 18.8 . 1 917 . 108 ILE CG1 C 28.7 . 1 918 . 108 ILE HG12 H 1.54 . 2 919 . 108 ILE HG13 H 1.46 . 2 920 . 108 ILE HD1 H 0.95 . 1 921 . 108 ILE CD1 C 13.5 . 1 922 . 109 ASP N N 119.6 . 1 923 . 109 ASP H H 8.16 . 1 924 . 109 ASP CA C 57.5 . 1 925 . 109 ASP HA H 4.46 . 1 926 . 109 ASP CB C 40.0 . 1 927 . 109 ASP HB2 H 2.81 . 2 928 . 109 ASP HB3 H 2.68 . 2 929 . 110 GLU N N 121.9 . 1 930 . 110 GLU H H 8.19 . 1 931 . 110 GLU CA C 58.8 . 1 932 . 110 GLU HA H 4.16 . 1 933 . 110 GLU CB C 29.3 . 1 934 . 110 GLU HB2 H 2.27 . 2 935 . 110 GLU HB3 H 2.23 . 2 936 . 110 GLU CG C 36.3 . 1 937 . 110 GLU HG2 H 2.47 . 2 938 . 110 GLU HG3 H 2.33 . 2 939 . 111 ALA N N 122.4 . 1 940 . 111 ALA H H 8.01 . 1 941 . 111 ALA CA C 55.4 . 1 942 . 111 ALA HA H 3.83 . 1 943 . 111 ALA HB H 1.03 . 1 944 . 111 ALA CB C 18.1 . 1 945 . 112 VAL N N 116.6 . 1 946 . 112 VAL H H 8.14 . 1 947 . 112 VAL CA C 67.3 . 1 948 . 112 VAL HA H 3.25 . 1 949 . 112 VAL CB C 31.7 . 1 950 . 112 VAL HB H 2.13 . 1 951 . 112 VAL HG1 H 0.85 . 2 952 . 112 VAL HG2 H 0.97 . 2 953 . 112 VAL CG1 C 21.2 . 1 954 . 112 VAL CG2 C 22.9 . 1 955 . 113 ALA N N 120.1 . 1 956 . 113 ALA H H 7.82 . 1 957 . 113 ALA CA C 54.9 . 1 958 . 113 ALA HA H 4.25 . 1 959 . 113 ALA HB H 1.52 . 1 960 . 113 ALA CB C 17.9 . 1 961 . 114 LEU N N 120.9 . 1 962 . 114 LEU H H 8.04 . 1 963 . 114 LEU CA C 58.2 . 1 964 . 114 LEU HA H 4.18 . 1 965 . 114 LEU CB C 42.1 . 1 966 . 114 LEU HB2 H 1.85 . 1 967 . 114 LEU HB3 H 1.85 . 1 968 . 114 LEU CG C 27.6 . 1 969 . 114 LEU HG H 1.77 . 1 970 . 114 LEU HD1 H 0.95 . 2 971 . 114 LEU HD2 H 1.06 . 2 972 . 114 LEU CD1 C 26.1 . 1 973 . 114 LEU CD2 C 24.8 . 1 974 . 115 VAL N N 119.6 . 1 975 . 115 VAL H H 7.95 . 1 976 . 115 VAL CA C 67.3 . 1 977 . 115 VAL HA H 3.30 . 1 978 . 115 VAL CB C 31.0 . 1 979 . 115 VAL HB H 2.25 . 1 980 . 115 VAL HG1 H 0.95 . 2 981 . 115 VAL HG2 H 0.81 . 2 982 . 115 VAL CG1 C 23.9 . 1 983 . 115 VAL CG2 C 22.8 . 1 984 . 116 GLU N N 117.5 . 1 985 . 116 GLU H H 8.55 . 1 986 . 116 GLU CA C 60.0 . 1 987 . 116 GLU HA H 3.89 . 1 988 . 116 GLU CB C 29.4 . 1 989 . 116 GLU HB2 H 2.15 . 2 990 . 116 GLU HB3 H 2.04 . 2 991 . 116 GLU CG C 36.4 . 1 992 . 116 GLU HG2 H 2.55 . 2 993 . 116 GLU HG3 H 2.15 . 2 994 . 117 ARG N N 120.6 . 1 995 . 117 ARG H H 8.23 . 1 996 . 117 ARG CA C 59.5 . 1 997 . 117 ARG HA H 4.19 . 1 998 . 117 ARG CB C 30.4 . 1 999 . 117 ARG HB2 H 2.20 . 1 1000 . 117 ARG HB3 H 2.20 . 1 1001 . 117 ARG CG C 28.4 . 1 1002 . 117 ARG HG2 H 2.00 . 2 1003 . 117 ARG HG3 H 1.77 . 2 1004 . 117 ARG CD C 44.1 . 1 1005 . 117 ARG HD2 H 3.35 . 1 1006 . 117 ARG HD3 H 3.35 . 1 1007 . 118 ALA N N 122.4 . 1 1008 . 118 ALA H H 8.11 . 1 1009 . 118 ALA CA C 54.9 . 1 1010 . 118 ALA HA H 3.52 . 1 1011 . 118 ALA HB H 1.01 . 1 1012 . 118 ALA CB C 18.2 . 1 1013 . 119 ILE N N 115.8 . 1 1014 . 119 ILE H H 7.88 . 1 1015 . 119 ILE CA C 64.4 . 1 1016 . 119 ILE HA H 3.72 . 1 1017 . 119 ILE CB C 38.0 . 1 1018 . 119 ILE HB H 1.92 . 1 1019 . 119 ILE HG2 H 0.87 . 1 1020 . 119 ILE CG2 C 17.1 . 1 1021 . 119 ILE CG1 C 29.1 . 1 1022 . 119 ILE HG12 H 1.72 . 2 1023 . 119 ILE HG13 H 1.14 . 2 1024 . 119 ILE HD1 H 0.71 . 1 1025 . 119 ILE CD1 C 14.2 . 1 1026 . 120 SER N N 114.5 . 1 1027 . 120 SER H H 8.03 . 1 1028 . 120 SER CA C 60.2 . 1 1029 . 120 SER HA H 4.35 . 1 1030 . 120 SER CB C 63.5 . 1 1031 . 120 SER HB2 H 4.00 . 1 1032 . 120 SER HB3 H 4.00 . 1 1033 . 121 HIS N N 119.7 . 1 1034 . 121 HIS H H 8.12 . 1 1035 . 121 HIS CA C 57.6 . 1 1036 . 121 HIS HA H 4.47 . 1 1037 . 121 HIS CB C 29.3 . 1 1038 . 121 HIS HB2 H 3.21 . 2 1039 . 121 HIS HB3 H 3.31 . 2 1040 . 121 HIS CD2 C 120.1 . 1 1041 . 121 HIS CE1 C 137.4 . 1 1042 . 121 HIS HD2 H 6.76 . 1 1043 . 121 HIS HE1 H 8.32 . 1 1044 . 122 TYR N N 118.1 . 1 1045 . 122 TYR H H 7.84 . 1 1046 . 122 TYR CA C 58.7 . 1 1047 . 122 TYR HA H 4.52 . 1 1048 . 122 TYR CB C 38.6 . 1 1049 . 122 TYR HB2 H 3.21 . 2 1050 . 122 TYR HB3 H 2.99 . 2 1051 . 122 TYR HD1 H 7.31 . 1 1052 . 122 TYR HD2 H 7.31 . 1 1053 . 122 TYR HE1 H 6.86 . 1 1054 . 122 TYR HE2 H 6.86 . 1 1055 . 122 TYR CD1 C 133.4 . 1 1056 . 122 TYR CE1 C 118.2 . 1 1057 . 123 GLN N N 121.2 . 1 1058 . 123 GLN H H 7.95 . 1 1059 . 123 GLN CA C 55.8 . 1 1060 . 123 GLN HA H 4.36 . 1 1061 . 123 GLN CB C 29.8 . 1 1062 . 123 GLN HB2 H 2.15 . 2 1063 . 123 GLN HB3 H 2.02 . 2 1064 . 123 GLN CG C 33.8 . 1 1065 . 123 GLN HG2 H 2.40 . 1 1066 . 123 GLN HG3 H 2.40 . 1 1067 . 124 GLU N N 127.5 . 1 1068 . 124 GLU H H 7.99 . 1 1069 . 124 GLU CA C 58.2 . 1 1070 . 124 GLU HA H 4.11 . 1 1071 . 124 GLU CB C 31.0 . 1 1072 . 124 GLU HB2 H 2.08 . 2 1073 . 124 GLU HB3 H 1.96 . 2 1074 . 124 GLU CG C 36.7 . 1 1075 . 124 GLU HG2 H 2.30 . 1 1076 . 124 GLU HG3 H 2.30 . 1 stop_ save_