data_4528 #Corrected using PDB structure: 1KRWA # #N.B. (Observed* = Observed shift + Offset correction) # #After reference correction, the following residues still #have a HA chemical shift difference (obs*-pred) greater than 0.7ppm: #NUM AA CS Observed* Predicted # 7 W HA 6.41 5.58 # 54 D HA 5.80 4.33 # 57 M HA 4.71 3.38 # 62 G HA 3.70 5.02 # 75 M HA 4.55 5.51 # 77 P HA 4.41 5.25 # 81 M HA 5.46 4.07 # 90 A HA 3.12 4.13 #106 F HA 5.12 4.34 #107 D HA 4.83 3.98 # #After reference correction, the following residues still #have a CA chemical shift difference (obs*-pred) greater than 5.0ppm: #NUM AA CS Observed* Predicted # 81 M CA 52.99 58.07 # #After reference correction, the following residues still #have a N chemical shift difference (obs*-pred) greater than 10.0ppm: #NUM AA CS Observed* Predicted # 13 S N 123.67 104.76 # 17 W N 116.77 129.95 # 56 R N 120.27 133.25 # 57 M N 129.97 112.35 # 59 G N 112.57 102.52 # 62 G N 104.77 117.98 #108 I N 128.27 117.42 # #After reference correction, the following residues still #have a HN chemical shift difference (obs*-pred) greater than 2.0ppm: #NUM AA CS Observed* Predicted # 12 D H 10.12 7.93 # 62 G H 10.20 7.41 # #The average CS difference between predicted and observed: #HA CA CB CO N HN #-0.11 0.29 0.02 N/A -0.23 -0.14 # #bmr4528.str.corr chemical shifts have been re-referenced with the following #offsets (these values have been added to the original bmr4528.str file): #HA CA CB CO N HN #N/A +0.15 +0.15 N/A -0.23 N/A # #The 95% confidence intervals for the above recommended offsets are: # HA CA CB CO N HN #+/-0.03 +/-0.18 +/-0.21 N/A +/-0.39 +/-0.07 # #The Correlation Coefficients between predicted and observed #chemical shifts are: #HA CA CB CO N HN #0.752 0.949 0.994 N/A 0.652 0.441 # #The RMSD between predicted and observed* (reference #corrected) chemical shifts are: #HA CA CB CO N HN #0.162 0.951 1.060 N/A 1.955 0.372 # ####################### # 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) ; 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_ _BMRB_accession_number 4528 _BMRB_flat_file_name bmr4528.str _Entry_type new _Submission_date 1999-11-05 _Accession_date 1999-12-06 _Entry_origination author _NMR_STAR_version 2.1.1 _Experimental_method NMR loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count '1H chemical shifts' 600 '13C chemical shifts' 363 '15N chemical shifts' 113 stop_ loop_ _Related_BMRB_accession_number _Relationship 4527 'phosphorylated form' stop_ save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_title ; Structure of a Transiently Phosphorylated "Switch" in Bacterial Signal Transduction ; _Citation_status published _Citation_type journal _MEDLINE_UI_code 20085967 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 _Page_first 894 _Page_last 898 _Year 1999 loop_ _Keyword 'RECEIVER DOMAIN' 'PHOSPHORYLATION' 'SIGNAL TRANSDUCTION' 'CONFORMATIONAL REARRANGEMENT' 'TWO-COMPONENT SYSTEM' stop_ 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 stop_ _System_physical_state native _System_oligomer_state monomer _System_paramagnetic no _System_thiol_state 'all free' loop_ _Database_name _Database_accession_code _Database_entry_mol_name _Database_entry_details PDB 1NTR "Solution Structure Of The N-Terminal Receiver Domain Of Ntrc" . PDB 1DC7 'A Chain A, Structure Of A Transiently Phosphorylated "switch" In Bacterial Signal Transduction' . PDB 1DC8 'A Chain A, Structure Of A Transiently Phosphorylated "switch" In Bacterial Signal Transduction' . stop_ save_ ######################## # Monomeric polymers # ######################## save_P-NtrCr _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common "NITROGEN REGULATION PROTEIN" _Name_variant . _Abbreviation_common P-NtrCr _Mol_thiol_state 'all free' ############################## # 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 2004-07-29 _Sequence_homology_query_revised_last_date 2004-07-16 loop_ _Database_name _Database_accession_code _Database_entry_mol_name _Sequence_query_to_submitted_percentage _Sequence_subject_length _Sequence_identity _Sequence_positive _Sequence_homology_expectation_value PDB 1DC7 'A Chain A, Structure Of A TransientlyPhosphorylated "switch" In Bacterial Signal Transduction' 100.00 124 100 100 9e-65 PDB 1J56 "A Chain A, Minimized Average Structure OfBeryllofluoride-Activated Ntrc Receiver Domain: ModelStructure Incorporating Active Site Contacts" 100.00 124 100 100 2e-65 PDB 1KRW "A Chain A, Solution Structure And BackboneDynamics Of Beryllofluoride- Activated Ntrc ReceiverDomain" 100.00 124 100 100 2e-65 PDB 1KRX "A Chain A, Solution Structure OfBeryllofluoride-Activated Ntrc Receiver Domain: ModelStructures Incorporating Active Site Contacts" 100.00 124 100 100 2e-65 PDB 1NTR "Solution Structure Of The N-Terminal ReceiverDomain Of Ntrc" 100.00 124 100 100 2e-65 PDB 1DC8 'A Chain A, Structure Of A TransientlyPhosphorylated "switch" In Bacterial Signal Transduction' 100.00 124 99 99 6e-64 DBJ BAB38213.1 "response regulator for gln GlnG[Escherichia coli O157:H7]" 26.44 469 98 98 7e-64 EMBL CAA28808.1 "unnamed protein product [Escherichia coli]" 26.50 468 98 98 7e-64 EMBL CAA59425.1 "nitrogen regulatory protein C [Salmonellatyphimurium]" 26.44 469 100 100 2e-65 EMBL CAD03095.1 "Two-component system, responseregulator [Salmonella enterica subsp. enterica serovarTyphi]" 26.44 469 99 99 10e-65 GenBank AAL22844.1 "EBP family response regulator intwo-component regulatory system with GlnL [Salmonellatyphimurium LT2]" 26.44 469 100 100 2e-65 GenBank AAO71117.1 "two-component system, response regulator[Salmonella enterica subsp. enterica serovar Typhi Ty2]" 26.44 469 99 99 10e-65 GenBank AAB03002.1 "CG Site No. 702 [Escherichia coli]" 26.44 469 98 98 7e-64 GenBank AAC76865.1 "response regulator for gln (sensor glnL)(nitrogen regulator I, NRI); response regulator intwo-component regulatory system with GlnL, nitrogenregulation (EBP family) [Escherichia coli K12]" 26.44 469 98 98 7e-64 GenBank AAG59057.1 "response regulator for gln (sensor glnL)(nitrogen regulator I, NRI) [Escherichia coli O157:H7EDL933]" 26.44 469 98 98 6e-64 PIR RGECGG "nitrogen regulation protein I ntrC -Escherichia coli (strain K-12)" 26.50 468 98 98 7e-64 PIR S53024 "nitrogen regulation protein I ntrC -Salmonella typhimurium" 26.44 469 100 100 2e-65 PIR AC0950 "Two-component system, response regulatorSTY3876 [imported] - Salmonella enterica subsp. entericaserovar Typhi (strain CT18)" 26.44 469 99 99 10e-65 PIR E86074 "hypothetical protein glnG [imported] -Escherichia coli (strain O157:H7, substrain EDL933)" 26.44 469 98 98 6e-64 PIR F91227 "response regulator for gln GlnG [imported]- Escherichia coli (strain O157:H7, substrain RIMD0509952)" 26.44 469 98 98 7e-64 REF NP_462885.1 "response regulator [Salmonellatyphimurium LT2]" 26.44 469 100 100 2e-65 REF NP_458044.1 "Two-component system, responseregulator [Salmonella enterica subsp. enterica serovarTyphi str. CT18]" 26.44 469 99 99 10e-65 REF NP_807257.1 "two-component system, responseregulator [Salmonella enterica subsp. enterica serovarTyphi Ty2]" 26.44 469 99 99 10e-65 REF NP_290493.1 "response regulator for gln (sensorglnL) (nitrogen regulator I, NRI) [Escherichia coliO157:H7 EDL933]" 26.44 469 98 98 6e-64 REF NP_312817.1 "GlnG; response regulator for gln[Escherichia coli O157:H7]" 26.44 469 98 98 7e-64 SWISS-PROT P41789 "NTRC_SALTY Nitrogen regulation protein NR(I)" 26.44 469 100 100 2e-65 SWISS-PROT P06713 "NTRC_ECOLI Nitrogen regulation protein NR(I)" 26.44 469 98 98 7e-64 stop_ save_ ############# # Ligands # ############# save_PO4 _Saveframe_category ligand _Abbreviation_common PO4 _Name_IUPAC phosphate _Mol_paramagnetic no _Mol_aromatic no save_ ######################################## # Molecular bond linkage definitions # ######################################## save_crosslink_bond_definitions _Saveframe_category crosslink_bonds loop_ _Bond_order _Bond_type _Atom_one_mol_system_component_name _Atom_one_residue_seq_code _Atom_one_residue_label _Atom_one_atom_name _Atom_two_mol_system_component_name _Atom_two_residue_seq_code _Atom_two_residue_label _Atom_two_atom_name single 'phosphoester' PO4 . . P P-NtrCr 54 ASP OG stop_ 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 Eubacteria . 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 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 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 save_ ############################# # NMR applied experiments # ############################# save_NMR_applied_experiment _Saveframe_category NMR_applied_experiment _Experiment_name ; 3D 15N-SEPARATED_NOESY 3D 13C-SEPARATED_NOESY 2D NOESY ; save_ ####################### # Sample conditions # ####################### save_sample_cond_1 _Saveframe_category sample_conditions 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 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 # # # # Index Value Definition # # # # 1 Unique # # 2 Ambiguity of geminal atoms or geminal methyl # # proton groups # # 3 Aromatic atoms on opposite sides of the ring # # (e.g. Tyr HE1 and HE2 protons) # # 4 Intraresidue ambiguities (e.g. Lys HG and # # HD protons) # # 5 Interresidue ambiguities (Lys 12 vs. Lys 27) # # 9 Ambiguous, specific ambiguity not defined # # # ################################################################### save_chemical_shift_set_1 _Saveframe_category assigned_chemical_shifts 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 loop_ _Atom_shift_assign_ID _Residue_seq_code _Residue_label _Atom_name _Atom_type _Chem_shift_value _Chem_shift_value_error _Chem_shift_ambiguity_code 1 2 GLN CA C 55.75 . 1 2 2 GLN HA H 4.52 . 1 3 2 GLN CG C 34.05 . 1 4 2 GLN HG2 H 2.38 . 2 5 2 GLN HG3 H 2.36 . 2 6 3 ARG N N 121.67 . 1 7 3 ARG H H 8.59 . 1 8 3 ARG CA C 56.25 . 1 9 3 ARG HA H 4.45 . 1 11 3 ARG HB2 H 1.89 . 2 12 3 ARG HB3 H 1.78 . 2 13 3 ARG CG C 27.55 . 1 14 3 ARG HG2 H 1.71 . 2 15 3 ARG HG3 H 1.65 . 2 16 3 ARG CD C 43.35 . 1 17 3 ARG HD2 H 3.21 . 1 18 3 ARG HD3 H 3.21 . 1 19 4 GLY N N 108.37 . 1 20 4 GLY H H 8.24 . 1 21 4 GLY CA C 45.55 . 1 22 4 GLY HA3 H 3.89 . 2 23 4 GLY HA2 H 4.03 . 2 24 5 ILE N N 122.47 . 1 25 5 ILE H H 9.69 . 1 26 5 ILE CA C 60.85 . 1 27 5 ILE HA H 4.77 . 1 28 5 ILE CB C 39.95 . 1 29 5 ILE HB H 1.65 . 1 30 5 ILE HG2 H 0.97 . 1 31 5 ILE CG2 C 18.65 . 1 32 5 ILE CG1 C 27.55 . 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 13.65 . 1 37 6 VAL N N 126.97 . 1 38 6 VAL H H 9.23 . 1 39 6 VAL CA C 59.25 . 1 40 6 VAL HA H 4.98 . 1 41 6 VAL CB C 34.75 . 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 21.45 . 1 46 6 VAL CG2 C 21.45 . 1 47 7 TRP N N 127.27 . 1 48 7 TRP H H 8.63 . 1 49 7 TRP CA C 52.95 . 1 50 7 TRP HA H 6.52 . 1 51 7 TRP CB C 33.45 . 1 52 7 TRP HB2 H 3.20 . 2 53 7 TRP HB3 H 3.21 . 2 54 7 TRP CD1 C 123.55 . 1 55 7 TRP CE3 C 119.95 . 1 56 7 TRP NE1 N 127.50 . 1 57 7 TRP HD1 H 7.27 . 1 58 7 TRP HE3 H 6.97 . 1 59 7 TRP CZ3 C 122.05 . 1 60 7 TRP CZ2 C 113.65 . 1 61 7 TRP HE1 H 10.28 . 1 62 7 TRP HZ3 H 6.91 . 1 63 7 TRP CH2 C 126.25 . 1 64 7 TRP HZ2 H 7.24 . 1 65 7 TRP HH2 H 7.01 . 1 66 8 VAL N N 122.27 . 1 67 8 VAL H H 8.76 . 1 68 8 VAL CA C 60.65 . 1 69 8 VAL HA H 5.18 . 1 70 8 VAL CB C 36.05 . 1 71 8 VAL HB H 1.85 . 1 72 8 VAL HG1 H 0.92 . 2 73 8 VAL CG1 C 21.85 . 1 74 9 VAL N N 126.27 . 1 75 9 VAL H H 9.19 . 1 76 9 VAL CA C 58.55 . 1 77 9 VAL HA H 5.25 . 1 78 9 VAL CB C 33.25 . 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 20.45 . 1 83 9 VAL CG2 C 21.65 . 1 84 10 ASP N N 124.97 . 1 85 10 ASP H H 8.09 . 1 86 10 ASP CA C 55.55 . 1 87 10 ASP HA H 4.51 . 1 89 10 ASP HB2 H 2.56 . 2 90 10 ASP HB3 H 2.45 . 2 91 11 ASP N N 121.97 . 1 92 11 ASP H H 9.07 . 1 93 11 ASP CA C 55.55 . 1 94 11 ASP HA H 4.69 . 1 95 12 ASP N N 124.57 . 1 96 12 ASP H H 10.26 . 1 97 12 ASP CA C 53.25 . 1 98 12 ASP HA H 4.87 . 1 99 12 ASP CB C 41.45 . 1 100 12 ASP HB2 H 3.08 . 2 101 12 ASP HB3 H 2.65 . 2 102 13 SER N N 123.67 . 1 103 13 SER H H 9.17 . 1 104 13 SER CA C 61.55 . 1 105 13 SER HA H 3.78 . 1 106 13 SER CB C 62.85 . 1 107 13 SER HB2 H 3.98 . 2 108 13 SER HB3 H 3.88 . 2 109 14 SER N N 118.57 . 1 110 14 SER H H 8.56 . 1 111 14 SER CA C 61.85 . 1 112 14 SER HA H 4.35 . 1 113 14 SER CB C 62.75 . 1 114 14 SER HB2 H 4.04 . 1 115 14 SER HB3 H 4.04 . 1 116 15 ILE N N 122.47 . 1 117 15 ILE H H 7.08 . 1 118 15 ILE CA C 60.85 . 1 119 15 ILE HA H 4.07 . 1 120 15 ILE CB C 36.15 . 1 121 15 ILE HB H 2.17 . 1 122 15 ILE HG2 H 0.99 . 1 123 15 ILE CG2 C 18.05 . 1 124 15 ILE CG1 C 27.55 . 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 9.25 . 1 129 16 ARG N N 116.77 . 1 130 16 ARG H H 7.45 . 1 131 16 ARG CA C 61.95 . 1 132 16 ARG HA H 3.77 . 1 133 16 ARG CB C 30.55 . 1 134 16 ARG HB2 H 2.16 . 1 135 16 ARG HB3 H 2.16 . 1 136 16 ARG CG C 29.15 . 1 137 16 ARG HG2 H 2.12 . 1 138 16 ARG HG3 H 2.12 . 1 139 17 TRP N N 116.77 . 1 140 17 TRP H H 8.03 . 1 141 17 TRP CA C 60.75 . 1 142 17 TRP HA H 4.53 . 1 143 17 TRP CB C 29.65 . 1 144 17 TRP HB2 H 3.52 . 2 145 17 TRP HB3 H 3.46 . 2 146 17 TRP CD1 C 127.45 . 1 147 17 TRP CE3 C 121.35 . 1 148 17 TRP NE1 N 129.20 . 1 149 17 TRP HD1 H 7.35 . 1 150 17 TRP HE3 H 7.66 . 1 151 17 TRP CZ3 C 121.55 . 1 152 17 TRP CZ2 C 114.45 . 1 153 17 TRP HE1 H 10.21 . 1 154 17 TRP HZ3 H 7.15 . 1 155 17 TRP CH2 C 124.45 . 1 156 17 TRP HZ2 H 7.49 . 1 157 17 TRP HH2 H 7.22 . 1 158 18 VAL N N 116.67 . 1 159 18 VAL H H 8.18 . 1 160 18 VAL CA C 66.15 . 1 161 18 VAL HA H 3.68 . 1 162 18 VAL CB C 32.15 . 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 22.65 . 1 167 18 VAL CG2 C 21.35 . 1 168 19 LEU N N 119.17 . 1 169 19 LEU H H 8.14 . 1 170 19 LEU CA C 57.95 . 1 171 19 LEU HA H 4.14 . 1 172 19 LEU CB C 41.85 . 1 173 19 LEU HB2 H 2.13 . 2 174 19 LEU HB3 H 1.23 . 2 175 19 LEU CG C 28.05 . 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 27.45 . 1 180 19 LEU CD2 C 22.15 . 1 181 20 GLU N N 120.07 . 1 182 20 GLU H H 8.51 . 1 183 20 GLU CA C 60.85 . 1 184 20 GLU HA H 4.08 . 1 185 20 GLU CB C 29.15 . 1 186 20 GLU HB2 H 2.12 . 1 187 20 GLU HB3 H 2.12 . 1 188 20 GLU CG C 36.15 . 1 189 20 GLU HG2 H 2.22 . 1 190 20 GLU HG3 H 2.22 . 1 192 21 ARG H H 7.67 . 1 193 21 ARG CA C 58.75 . 1 194 21 ARG HA H 3.96 . 1 195 21 ARG CB C 30.15 . 1 196 21 ARG HB2 H 1.69 . 2 197 21 ARG HB3 H 1.52 . 2 198 21 ARG CG C 26.65 . 1 199 21 ARG HG2 H 1.33 . 1 200 21 ARG HG3 H 1.33 . 1 201 21 ARG CD C 43.15 . 1 202 21 ARG HD2 H 2.74 . 1 203 21 ARG HD3 H 2.74 . 1 204 22 ALA CA C 54.95 . 1 205 22 ALA HA H 4.17 . 1 206 22 ALA HB H 1.46 . 1 207 22 ALA CB C 19.55 . 1 208 23 LEU N N 118.17 . 1 209 23 LEU H H 8.96 . 1 210 23 LEU CA C 58.05 . 1 211 23 LEU HA H 4.07 . 1 212 23 LEU CB C 40.05 . 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 27.05 . 1 218 23 LEU CD2 C 24.65 . 1 219 24 ALA N N 121.97 . 1 220 24 ALA H H 8.36 . 1 221 24 ALA CA C 55.05 . 1 222 24 ALA HA H 4.74 . 1 223 24 ALA HB H 1.58 . 1 225 25 GLY N N 106.87 . 1 226 25 GLY H H 8.01 . 1 227 25 GLY CA C 46.75 . 1 228 25 GLY HA3 H 3.93 . 2 229 25 GLY HA2 H 3.97 . 2 230 26 ALA N N 121.57 . 1 231 26 ALA H H 7.39 . 1 232 26 ALA CA C 51.75 . 1 233 26 ALA HA H 4.58 . 1 234 26 ALA HB H 1.53 . 1 236 27 GLY N N 106.07 . 1 237 27 GLY H H 7.97 . 1 238 27 GLY CA C 45.65 . 1 239 27 GLY HA3 H 3.82 . 2 240 27 GLY HA2 H 4.34 . 2 241 28 LEU N N 119.87 . 1 242 28 LEU H H 7.72 . 1 243 28 LEU CA C 53.95 . 1 244 28 LEU HA H 4.65 . 1 245 28 LEU CB C 42.85 . 1 246 28 LEU HB2 H 1.50 . 2 247 28 LEU HB3 H 1.23 . 2 248 28 LEU CG C 28.15 . 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 26.25 . 1 253 28 LEU CD2 C 23.75 . 1 254 29 THR N N 118.07 . 1 255 29 THR H H 8.71 . 1 256 29 THR CA C 62.75 . 1 257 29 THR HA H 4.41 . 1 258 29 THR CB C 69.65 . 1 259 29 THR HB H 4.21 . 1 260 29 THR HG2 H 1.33 . 1 261 29 THR CG2 C 21.95 . 1 262 30 CYS N N 128.47 . 1 263 30 CYS H H 9.19 . 1 264 30 CYS CA C 56.65 . 1 265 30 CYS HA H 6.06 . 1 266 30 CYS CB C 29.85 . 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 126.27 . 1 271 31 THR H H 8.57 . 1 272 31 THR CA C 62.15 . 1 273 31 THR HA H 4.51 . 1 274 31 THR CB C 70.75 . 1 275 31 THR HB H 3.45 . 1 276 31 THR HG2 H 0.50 . 1 277 31 THR CG2 C 22.75 . 1 278 32 THR N N 115.87 . 1 279 32 THR H H 8.45 . 1 280 32 THR CA C 59.35 . 1 281 32 THR HA H 5.52 . 1 282 32 THR CB C 71.35 . 1 283 32 THR HB H 3.99 . 1 284 32 THR HG2 H 1.20 . 1 285 32 THR CG2 C 22.15 . 1 286 33 PHE N N 117.27 . 1 287 33 PHE H H 8.90 . 1 288 33 PHE CA C 56.75 . 1 289 33 PHE HA H 4.75 . 1 290 33 PHE CB C 43.45 . 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 131.15 . 1 298 33 PHE CE1 C 131.05 . 1 299 34 GLU N N 118.07 . 1 300 34 GLU H H 9.20 . 1 301 34 GLU CA C 56.85 . 1 302 34 GLU HA H 4.50 . 1 303 34 GLU CB C 32.05 . 1 304 34 GLU HB2 H 2.15 . 2 305 34 GLU HB3 H 2.07 . 2 306 34 GLU CG C 36.75 . 1 307 34 GLU HG2 H 2.37 . 2 308 34 GLU HG3 H 2.22 . 2 309 35 ASN N N 107.97 . 1 310 35 ASN H H 7.35 . 1 311 35 ASN CA C 52.55 . 1 312 35 ASN HA H 5.04 . 1 314 35 ASN HB2 H 3.09 . 2 315 35 ASN ND2 N 116.50 . 1 316 35 ASN HD21 H 7.12 . 2 317 35 ASN HD22 H 7.83 . 2 318 36 GLY N N 104.67 . 1 319 36 GLY H H 9.52 . 1 320 36 GLY CA C 47.75 . 1 321 36 GLY HA3 H 3.73 . 2 322 36 GLY HA2 H 3.80 . 2 323 37 ASN N N 120.37 . 1 324 37 ASN H H 8.53 . 1 325 37 ASN CA C 57.05 . 1 326 37 ASN HA H 4.42 . 1 327 37 ASN CB C 37.85 . 1 328 37 ASN HB2 H 2.91 . 2 329 37 ASN HB3 H 2.79 . 2 330 37 ASN ND2 N 112.00 . 1 331 37 ASN HD21 H 6.92 . 2 332 37 ASN HD22 H 7.77 . 2 333 38 GLU N N 119.07 . 1 334 38 GLU H H 8.21 . 1 335 38 GLU CA C 59.05 . 1 336 38 GLU HA H 4.13 . 1 337 38 GLU CB C 30.85 . 1 338 38 GLU HB2 H 2.36 . 1 339 38 GLU HB3 H 2.36 . 1 340 38 GLU CG C 36.65 . 1 341 38 GLU HG2 H 2.68 . 2 342 38 GLU HG3 H 2.42 . 2 343 39 VAL N N 118.97 . 1 344 39 VAL H H 6.94 . 1 345 39 VAL CA C 65.45 . 1 346 39 VAL HA H 2.65 . 1 347 39 VAL CB C 31.25 . 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 21.55 . 1 352 39 VAL CG2 C 23.25 . 1 353 40 LEU N N 118.07 . 1 354 40 LEU H H 7.84 . 1 355 40 LEU CA C 58.25 . 1 356 40 LEU HA H 4.00 . 1 357 40 LEU CB C 41.05 . 1 358 40 LEU HB2 H 1.82 . 2 359 40 LEU HB3 H 1.55 . 2 360 40 LEU CG C 27.05 . 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 25.95 . 1 365 40 LEU CD2 C 23.05 . 1 366 41 ALA N N 119.87 . 1 367 41 ALA H H 7.78 . 1 368 41 ALA CA C 55.05 . 1 369 41 ALA HA H 4.23 . 1 370 41 ALA HB H 1.52 . 1 371 41 ALA CB C 17.95 . 1 372 42 ALA N N 122.47 . 1 373 42 ALA H H 7.64 . 1 374 42 ALA CA C 55.25 . 1 375 42 ALA HA H 4.29 . 1 376 42 ALA HB H 1.39 . 1 377 42 ALA CB C 19.85 . 1 378 43 LEU N N 119.17 . 1 379 43 LEU H H 8.40 . 1 380 43 LEU CA C 55.55 . 1 381 43 LEU HA H 5.34 . 1 382 43 LEU CB C 43.05 . 1 383 43 LEU HB2 H 2.01 . 2 384 43 LEU HB3 H 1.77 . 2 385 43 LEU CG C 27.05 . 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 26.25 . 1 390 43 LEU CD2 C 25.05 . 1 391 44 ALA N N 118.77 . 1 392 44 ALA H H 7.38 . 1 393 44 ALA CA C 54.55 . 1 394 44 ALA HA H 4.31 . 1 395 44 ALA HB H 1.63 . 1 396 44 ALA CB C 18.85 . 1 397 45 SER N N 108.17 . 1 398 45 SER H H 7.84 . 1 399 45 SER CA C 58.95 . 1 400 45 SER HA H 4.82 . 1 401 45 SER CB C 65.65 . 1 402 45 SER HB2 H 4.05 . 2 403 45 SER HB3 H 3.95 . 2 404 46 LYS N N 122.87 . 1 405 46 LYS H H 8.17 . 1 406 46 LYS CA C 55.85 . 1 407 46 LYS HA H 4.68 . 1 408 46 LYS CB C 36.65 . 1 409 46 LYS HB2 H 2.09 . 2 410 46 LYS HB3 H 1.99 . 2 411 46 LYS CG C 24.95 . 1 412 46 LYS HG2 H 1.59 . 2 413 46 LYS HG3 H 1.56 . 2 414 46 LYS CD C 29.45 . 1 415 46 LYS HD2 H 1.90 . 1 416 46 LYS HD3 H 1.90 . 1 417 46 LYS CE C 42.35 . 1 418 46 LYS HE2 H 3.11 . 1 419 46 LYS HE3 H 3.11 . 1 421 47 THR H H 7.86 . 1 422 47 THR CA C 58.05 . 1 423 47 THR HA H 4.36 . 1 424 47 THR CB C 70.85 . 1 425 47 THR HB H 3.69 . 1 426 47 THR HG2 H 0.84 . 1 427 47 THR CG2 C 21.55 . 1 428 48 PRO CD C 48.05 . 1 429 48 PRO CA C 61.25 . 1 430 48 PRO HA H 4.01 . 1 431 48 PRO CB C 30.65 . 1 432 48 PRO HB2 H -0.28 . 2 433 48 PRO HB3 H 1.50 . 2 434 48 PRO CG C 26.35 . 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 114.67 . 1 440 49 ASP H H 8.62 . 1 441 49 ASP CA C 56.65 . 1 442 49 ASP HA H 4.53 . 1 443 49 ASP CB C 43.15 . 1 444 49 ASP HB2 H 2.63 . 1 445 49 ASP HB3 H 2.63 . 1 446 50 VAL N N 111.27 . 1 447 50 VAL H H 7.25 . 1 448 50 VAL CA C 60.55 . 1 449 50 VAL HA H 4.40 . 1 450 50 VAL CB C 34.55 . 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 21.65 . 1 455 50 VAL CG2 C 22.15 . 1 456 51 LEU N N 127.37 . 1 457 51 LEU H H 8.14 . 1 458 51 LEU CA C 53.35 . 1 459 51 LEU HA H 5.44 . 1 460 51 LEU CB C 46.85 . 1 461 51 LEU HB2 H 1.85 . 2 462 51 LEU HB3 H 1.15 . 2 463 51 LEU CG C 28.65 . 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 25.95 . 1 468 51 LEU CD2 C 27.15 . 1 469 52 LEU N N 128.67 . 1 470 52 LEU H H 9.35 . 1 471 52 LEU CA C 54.35 . 1 472 52 LEU HA H 5.38 . 1 473 52 LEU CB C 44.35 . 1 474 52 LEU HB2 H 1.85 . 2 475 52 LEU HB3 H 1.35 . 2 476 52 LEU CG C 29.55 . 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 25.05 . 1 481 52 LEU CD2 C 26.35 . 1 482 53 SER N N 116.47 . 1 483 53 SER H H 9.35 . 1 484 53 SER CA C 56.55 . 1 485 53 SER HA H 5.49 . 1 486 53 SER CB C 66.15 . 1 487 53 SER HB2 H 3.67 . 2 488 53 SER HB3 H 3.16 . 2 489 54 ASP N N 126.57 . 1 490 54 ASP H H 8.35 . 1 492 54 ASP HA H 5.91 . 1 494 54 ASP HB2 H 3.23 . 2 495 54 ASP HB3 H 4.22 . 2 496 55 ILE N N 117.27 . 1 497 55 ILE H H 8.08 . 1 498 56 ARG N N 120.27 . 1 499 56 ARG H H 10.05 . 1 501 57 MET H H 7.63 . 1 502 57 MET CA C 54.05 . 1 503 57 MET HA H 4.82 . 1 504 57 MET CG C 32.95 . 1 505 57 MET HG2 H 2.83 . 2 506 57 MET HG3 H 2.23 . 2 507 58 PRO CD C 50.75 . 1 508 58 PRO CA C 63.25 . 1 509 58 PRO HA H 4.44 . 1 511 58 PRO HB2 H 2.39 . 2 512 58 PRO HB3 H 2.01 . 2 513 58 PRO CG C 27.85 . 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 112.57 . 1 519 59 GLY H H 8.84 . 1 520 59 GLY CA C 46.65 . 1 521 59 GLY HA3 H 3.57 . 2 522 59 GLY HA2 H 4.30 . 2 523 60 MET N N 124.07 . 1 524 60 MET H H 7.89 . 1 525 60 MET CA C 56.25 . 1 526 60 MET HA H 4.40 . 1 527 60 MET CB C 35.15 . 1 528 60 MET HB2 H 2.22 . 2 529 60 MET HB3 H 1.81 . 2 530 61 ASP N N 125.17 . 1 531 61 ASP H H 8.54 . 1 532 61 ASP CA C 53.65 . 1 533 61 ASP HA H 4.94 . 1 535 61 ASP HB2 H 3.42 . 2 536 61 ASP HB3 H 2.86 . 2 537 62 GLY N N 104.77 . 1 538 62 GLY H H 10.34 . 1 539 62 GLY CA C 46.85 . 1 540 62 GLY HA3 H 3.81 . 2 541 63 LEU N N 120.07 . 1 542 63 LEU H H 8.19 . 1 543 63 LEU CA C 57.35 . 1 544 63 LEU HA H 4.37 . 1 545 63 LEU CB C 40.15 . 1 546 63 LEU HB2 H 1.52 . 2 547 63 LEU HB3 H 2.11 . 2 548 63 LEU CG C 27.85 . 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 25.45 . 1 553 63 LEU CD2 C 24.25 . 1 554 64 ALA N N 126.17 . 1 555 64 ALA H H 8.40 . 1 557 64 ALA HA H 4.17 . 1 558 64 ALA HB H 1.58 . 1 560 65 LEU N N 119.87 . 1 561 65 LEU H H 8.52 . 1 562 66 LEU N N 120.57 . 1 563 66 LEU H H 8.25 . 1 564 66 LEU CA C 58.85 . 1 565 66 LEU HA H 3.92 . 1 566 67 LYS N N 116.77 . 1 567 67 LYS H H 7.77 . 1 568 67 LYS CA C 60.05 . 1 569 67 LYS HA H 4.10 . 1 570 67 LYS CB C 32.65 . 1 571 67 LYS HB2 H 2.00 . 2 572 67 LYS HB3 H 2.01 . 2 573 67 LYS CG C 25.15 . 1 574 67 LYS HG2 H 1.65 . 2 575 67 LYS HG3 H 1.43 . 2 576 67 LYS CD C 29.75 . 1 577 67 LYS HD2 H 1.75 . 1 578 67 LYS HD3 H 1.75 . 1 579 67 LYS CE C 42.15 . 1 580 67 LYS HE2 H 2.99 . 1 581 67 LYS HE3 H 2.99 . 1 582 68 GLN N N 116.67 . 1 583 68 GLN H H 7.79 . 1 584 68 GLN CA C 58.95 . 1 585 68 GLN HA H 4.10 . 1 586 68 GLN CB C 28.85 . 1 587 68 GLN HB2 H 2.26 . 2 588 68 GLN HB3 H 2.22 . 2 589 68 GLN CG C 34.25 . 1 590 68 GLN HG2 H 2.52 . 2 591 68 GLN NE2 N 111.10 . 1 592 68 GLN HE21 H 6.86 . 2 593 68 GLN HE22 H 7.35 . 2 594 69 ILE N N 120.37 . 1 595 69 ILE H H 9.05 . 1 596 69 ILE CA C 65.55 . 1 597 69 ILE HA H 3.63 . 1 598 69 ILE CB C 37.35 . 1 599 69 ILE HB H 2.05 . 1 600 69 ILE HG2 H 0.94 . 1 601 69 ILE CG2 C 18.15 . 1 602 69 ILE HD1 H 0.71 . 1 603 69 ILE CD1 C 14.15 . 1 604 70 LYS N N 117.67 . 1 605 70 LYS H H 8.67 . 1 606 70 LYS CA C 57.55 . 1 607 70 LYS HA H 4.01 . 1 608 70 LYS CB C 31.55 . 1 609 70 LYS HB2 H 2.13 . 1 610 70 LYS HB3 H 2.13 . 1 611 70 LYS CG C 24.55 . 1 612 70 LYS HG2 H 1.74 . 2 613 70 LYS HG3 H 1.69 . 2 614 70 LYS CD C 28.05 . 1 615 70 LYS HD2 H 1.88 . 2 616 70 LYS HD3 H 1.75 . 2 617 71 GLN N N 114.77 . 1 618 71 GLN H H 7.38 . 1 619 71 GLN CA C 58.35 . 1 620 71 GLN HA H 4.14 . 1 621 71 GLN CB C 28.85 . 1 622 71 GLN HB2 H 2.24 . 2 623 71 GLN HB3 H 2.19 . 2 624 71 GLN CG C 34.25 . 1 625 71 GLN HG2 H 2.61 . 2 626 71 GLN HG3 H 2.45 . 2 627 71 GLN NE2 N 111.50 . 1 628 71 GLN HE21 H 6.92 . 2 629 71 GLN HE22 H 7.49 . 2 630 72 ARG N N 115.87 . 1 631 72 ARG H H 7.34 . 1 632 72 ARG CA C 57.35 . 1 633 72 ARG HA H 4.21 . 1 634 72 ARG CB C 32.85 . 1 635 72 ARG HB2 H 1.60 . 1 636 72 ARG HB3 H 1.60 . 1 637 72 ARG CG C 27.65 . 1 638 72 ARG HG2 H 1.65 . 2 639 72 ARG HG3 H 1.54 . 2 640 72 ARG CD C 43.55 . 1 641 72 ARG HD2 H 3.20 . 2 642 72 ARG HD3 H 3.07 . 2 644 73 HIS H H 8.94 . 1 645 73 HIS CA C 53.45 . 1 646 73 HIS HA H 5.06 . 1 647 73 HIS CB C 30.75 . 1 648 73 HIS HB2 H 3.02 . 1 649 73 HIS HB3 H 3.02 . 1 650 73 HIS CD2 C 121.05 . 1 651 73 HIS CE1 C 139.15 . 1 652 73 HIS HD2 H 6.71 . 1 653 73 HIS HE1 H 7.96 . 1 654 74 PRO CD C 50.25 . 1 655 74 PRO CA C 65.55 . 1 656 74 PRO HA H 4.51 . 1 657 74 PRO CB C 32.55 . 1 658 74 PRO HB3 H 2.60 . 2 659 74 PRO CG C 27.45 . 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 114.47 . 1 665 75 MET H H 8.78 . 1 666 75 MET CA C 54.45 . 1 667 75 MET HA H 4.66 . 1 668 75 MET CB C 31.65 . 1 669 75 MET HB2 H 2.30 . 2 670 75 MET HB3 H 2.06 . 2 671 75 MET CG C 32.85 . 1 672 75 MET HG2 H 2.76 . 2 673 75 MET HG3 H 2.52 . 2 675 76 LEU H H 7.44 . 1 676 76 LEU CA C 53.55 . 1 677 76 LEU HA H 4.34 . 1 678 76 LEU CB C 43.65 . 1 679 76 LEU HB2 H 1.87 . 2 680 76 LEU HB3 H 1.35 . 2 681 76 LEU CG C 27.25 . 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 25.35 . 1 686 76 LEU CD2 C 25.45 . 1 687 77 PRO CD C 51.25 . 1 688 77 PRO CA C 63.05 . 1 689 77 PRO HA H 4.52 . 1 690 77 PRO CB C 32.15 . 1 691 77 PRO HB2 H 1.77 . 2 692 77 PRO HB3 H 1.40 . 2 693 77 PRO CG C 28.55 . 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 122.57 . 1 699 78 VAL H H 8.53 . 1 700 78 VAL CA C 60.25 . 1 701 78 VAL HA H 5.13 . 1 702 78 VAL CB C 34.55 . 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 21.55 . 1 707 78 VAL CG2 C 21.55 . 1 708 79 ILE N N 128.67 . 1 709 79 ILE H H 9.54 . 1 710 79 ILE CA C 60.15 . 1 711 79 ILE HA H 4.53 . 1 712 79 ILE CB C 40.45 . 1 713 79 ILE HB H 1.68 . 1 714 79 ILE HG2 H 0.68 . 1 715 79 ILE CG2 C 18.45 . 1 716 79 ILE HD1 H 0.78 . 1 717 79 ILE CD1 C 15.05 . 1 718 80 ILE N N 128.37 . 1 719 80 ILE H H 7.98 . 1 720 80 ILE CA C 56.35 . 1 721 80 ILE HA H 5.24 . 1 722 80 ILE CB C 38.15 . 1 723 80 ILE HB H 1.93 . 1 724 80 ILE HG2 H 0.91 . 1 725 80 ILE CG2 C 18.35 . 1 726 80 ILE HD1 H 0.76 . 1 727 80 ILE CD1 C 9.15 . 1 728 81 MET N N 123.77 . 1 729 81 MET H H 9.05 . 1 730 81 MET CA C 52.85 . 1 731 81 MET HA H 5.57 . 1 732 81 MET CB C 36.55 . 1 733 81 MET HB2 H 1.95 . 2 734 81 MET HB3 H 1.84 . 2 735 81 MET CG C 32.45 . 1 736 81 MET HG2 H 2.59 . 2 737 81 MET HG3 H 2.35 . 2 739 82 THR H H 7.20 . 1 740 82 THR CA C 60.55 . 1 741 82 THR HA H 5.57 . 1 742 82 THR CB C 68.95 . 1 743 82 THR HB H 4.43 . 1 744 82 THR HG2 H 1.14 . 1 745 82 THR CG2 C 18.25 . 1 746 83 ALA H H 9.52 . 1 748 83 ALA HA H 4.67 . 1 749 83 ALA HB H 1.33 . 1 751 84 HIS CD2 C 119.85 . 1 752 84 HIS CE1 C 138.55 . 1 753 84 HIS HD2 H 7.30 . 1 754 84 HIS HE1 H 8.23 . 1 756 85 SER HA H 4.42 . 1 758 85 SER HB2 H 4.00 . 2 759 87 LEU CA C 57.35 . 1 760 87 LEU HA H 4.17 . 1 761 87 LEU CB C 42.45 . 1 762 87 LEU HB2 H 1.69 . 2 763 87 LEU CG C 27.15 . 1 764 87 LEU HG H 1.71 . 1 765 88 ASP N N 117.57 . 1 766 88 ASP H H 8.24 . 1 767 88 ASP CA C 56.55 . 1 768 88 ASP HA H 4.45 . 1 769 88 ASP CB C 40.55 . 1 770 88 ASP HB2 H 2.70 . 1 771 88 ASP HB3 H 2.70 . 1 772 89 ALA N N 122.87 . 1 773 89 ALA H H 8.08 . 1 774 89 ALA CA C 55.05 . 1 775 89 ALA HA H 4.14 . 1 776 89 ALA HB H 1.57 . 1 777 89 ALA CB C 19.05 . 1 778 90 ALA N N 119.67 . 1 779 90 ALA H H 7.60 . 1 780 90 ALA CA C 55.35 . 1 781 90 ALA HA H 3.23 . 1 782 90 ALA HB H 0.98 . 1 783 90 ALA CB C 18.15 . 1 784 91 VAL N N 116.87 . 1 785 91 VAL H H 8.07 . 1 786 91 VAL CA C 66.35 . 1 787 91 VAL HA H 3.69 . 1 788 91 VAL CB C 31.85 . 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 21.15 . 1 793 91 VAL CG2 C 22.75 . 1 794 92 SER N N 115.07 . 1 795 92 SER H H 8.07 . 1 796 92 SER CA C 61.75 . 1 797 92 SER HA H 4.28 . 1 798 92 SER CB C 63.25 . 1 799 92 SER HB2 H 4.03 . 2 800 92 SER HB3 H 3.94 . 2 802 93 ALA H H 8.32 . 1 804 93 ALA HA H 3.81 . 1 805 93 ALA HB H 1.33 . 1 807 95 GLN N N 120.27 . 1 808 95 GLN H H 8.78 . 1 809 95 GLN CA C 58.95 . 1 810 95 GLN HA H 4.03 . 1 812 95 GLN HB2 H 2.36 . 2 813 95 GLN CG C 34.35 . 1 814 95 GLN HG2 H 2.72 . 2 815 96 GLN N N 114.67 . 1 816 96 GLN H H 7.93 . 1 817 96 GLN CA C 55.55 . 1 818 96 GLN HA H 4.37 . 1 819 96 GLN CG C 34.45 . 1 820 96 GLN HG2 H 2.52 . 2 821 97 GLY N N 103.57 . 1 822 97 GLY H H 7.62 . 1 823 97 GLY CA C 45.65 . 1 824 97 GLY HA3 H 3.87 . 2 825 97 GLY HA2 H 4.36 . 2 826 98 ALA N N 123.17 . 1 827 98 ALA H H 8.51 . 1 828 98 ALA CA C 53.35 . 1 829 98 ALA HA H 4.30 . 1 830 98 ALA HB H 1.25 . 1 831 98 ALA CB C 18.65 . 1 832 99 PHE N N 123.47 . 1 833 99 PHE H H 9.61 . 1 834 99 PHE CA C 60.55 . 1 835 99 PHE HA H 4.32 . 1 836 99 PHE CB C 40.55 . 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 133.05 . 1 842 100 ASP H H 7.74 . 1 843 100 ASP CA C 52.75 . 1 844 100 ASP HA H 4.62 . 1 845 100 ASP CB C 45.15 . 1 846 100 ASP HB2 H 2.61 . 2 847 100 ASP HB3 H 2.50 . 2 848 101 TYR CA C 56.55 . 1 849 101 TYR HA H 5.39 . 1 850 101 TYR CB C 42.15 . 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 132.85 . 1 857 101 TYR CE1 C 117.85 . 1 859 102 LEU H H 9.10 . 1 860 102 LEU CA C 50.75 . 1 861 102 LEU HA H 4.77 . 1 863 102 LEU HB2 H 1.48 . 2 864 102 LEU HB3 H 0.82 . 2 865 102 LEU CG C 26.25 . 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 25.05 . 1 870 102 LEU CD2 C 23.15 . 1 871 103 PRO CD C 50.75 . 1 872 103 PRO CA C 62.25 . 1 873 103 PRO HA H 4.95 . 1 874 103 PRO HD2 H 3.75 . 2 875 103 PRO HD3 H 3.61 . 2 877 104 LYS H H 7.98 . 1 878 104 LYS CA C 53.35 . 1 879 104 LYS HA H 4.49 . 1 880 104 LYS CE C 41.45 . 1 881 104 LYS HE2 H 2.98 . 2 882 104 LYS HE3 H 2.86 . 2 883 105 PRO CD C 50.45 . 1 884 105 PRO CA C 62.45 . 1 885 105 PRO HA H 4.58 . 1 886 105 PRO CG C 25.05 . 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 53.35 . 1 892 106 PHE HA H 5.23 . 1 893 106 PHE CB C 40.65 . 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 133.65 . 1 901 106 PHE CE1 C 130.55 . 1 902 107 ASP N N 121.97 . 1 903 107 ASP H H 9.15 . 1 904 107 ASP CA C 53.45 . 1 905 107 ASP HA H 4.94 . 1 906 107 ASP CB C 42.55 . 1 907 107 ASP HB2 H 2.88 . 2 908 107 ASP HB3 H 2.74 . 2 909 108 ILE N N 128.27 . 1 910 108 ILE H H 9.07 . 1 911 108 ILE CA C 63.25 . 1 912 108 ILE HA H 4.02 . 1 913 108 ILE CB C 37.85 . 1 914 108 ILE HB H 2.04 . 1 915 108 ILE HG2 H 1.02 . 1 916 108 ILE CG2 C 18.95 . 1 917 108 ILE CG1 C 28.85 . 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 13.65 . 1 922 109 ASP N N 119.37 . 1 923 109 ASP H H 8.16 . 1 924 109 ASP CA C 57.65 . 1 925 109 ASP HA H 4.46 . 1 926 109 ASP CB C 40.15 . 1 927 109 ASP HB2 H 2.81 . 2 928 109 ASP HB3 H 2.68 . 2 929 110 GLU N N 121.67 . 1 930 110 GLU H H 8.19 . 1 931 110 GLU CA C 58.95 . 1 932 110 GLU HA H 4.16 . 1 933 110 GLU CB C 29.45 . 1 934 110 GLU HB2 H 2.27 . 2 935 110 GLU HB3 H 2.23 . 2 936 110 GLU CG C 36.45 . 1 937 110 GLU HG2 H 2.47 . 2 938 110 GLU HG3 H 2.33 . 2 939 111 ALA N N 122.17 . 1 940 111 ALA H H 8.01 . 1 941 111 ALA CA C 55.55 . 1 942 111 ALA HA H 3.83 . 1 943 111 ALA HB H 1.03 . 1 944 111 ALA CB C 18.25 . 1 945 112 VAL N N 116.37 . 1 946 112 VAL H H 8.14 . 1 947 112 VAL CA C 67.45 . 1 948 112 VAL HA H 3.25 . 1 949 112 VAL CB C 31.85 . 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 21.35 . 1 954 112 VAL CG2 C 23.05 . 1 955 113 ALA N N 119.87 . 1 956 113 ALA H H 7.82 . 1 957 113 ALA CA C 55.05 . 1 958 113 ALA HA H 4.25 . 1 959 113 ALA HB H 1.52 . 1 960 113 ALA CB C 18.05 . 1 961 114 LEU N N 120.67 . 1 962 114 LEU H H 8.04 . 1 963 114 LEU CA C 58.35 . 1 964 114 LEU HA H 4.18 . 1 965 114 LEU CB C 42.25 . 1 966 114 LEU HB2 H 1.85 . 1 967 114 LEU HB3 H 1.85 . 1 968 114 LEU CG C 27.75 . 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 26.25 . 1 973 114 LEU CD2 C 24.95 . 1 974 115 VAL N N 119.37 . 1 975 115 VAL H H 7.95 . 1 976 115 VAL CA C 67.45 . 1 977 115 VAL HA H 3.30 . 1 978 115 VAL CB C 31.15 . 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 24.05 . 1 983 115 VAL CG2 C 22.95 . 1 984 116 GLU N N 117.27 . 1 985 116 GLU H H 8.55 . 1 986 116 GLU CA C 60.15 . 1 987 116 GLU HA H 3.89 . 1 988 116 GLU CB C 29.55 . 1 989 116 GLU HB2 H 2.15 . 2 990 116 GLU HB3 H 2.04 . 2 991 116 GLU CG C 36.55 . 1 992 116 GLU HG2 H 2.55 . 2 993 116 GLU HG3 H 2.15 . 2 994 117 ARG N N 120.37 . 1 995 117 ARG H H 8.23 . 1 996 117 ARG CA C 59.65 . 1 997 117 ARG HA H 4.19 . 1 998 117 ARG CB C 30.55 . 1 999 117 ARG HB2 H 2.20 . 1 1000 117 ARG HB3 H 2.20 . 1 1001 117 ARG CG C 28.55 . 1 1002 117 ARG HG2 H 2.00 . 2 1003 117 ARG HG3 H 1.77 . 2 1004 117 ARG CD C 44.25 . 1 1005 117 ARG HD2 H 3.35 . 1 1006 117 ARG HD3 H 3.35 . 1 1007 118 ALA N N 122.17 . 1 1008 118 ALA H H 8.11 . 1 1009 118 ALA CA C 55.05 . 1 1010 118 ALA HA H 3.52 . 1 1011 118 ALA HB H 1.01 . 1 1012 118 ALA CB C 18.35 . 1 1013 119 ILE N N 115.57 . 1 1014 119 ILE H H 7.88 . 1 1015 119 ILE CA C 64.55 . 1 1016 119 ILE HA H 3.72 . 1 1017 119 ILE CB C 38.15 . 1 1018 119 ILE HB H 1.92 . 1 1019 119 ILE HG2 H 0.87 . 1 1020 119 ILE CG2 C 17.25 . 1 1021 119 ILE CG1 C 29.25 . 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 14.35 . 1 1026 120 SER N N 114.27 . 1 1027 120 SER H H 8.03 . 1 1028 120 SER CA C 60.35 . 1 1029 120 SER HA H 4.35 . 1 1030 120 SER CB C 63.65 . 1 1031 120 SER HB2 H 4.00 . 1 1032 120 SER HB3 H 4.00 . 1 1033 121 HIS N N 119.47 . 1 1034 121 HIS H H 8.12 . 1 1035 121 HIS CA C 57.75 . 1 1036 121 HIS HA H 4.47 . 1 1037 121 HIS CB C 29.45 . 1 1038 121 HIS HB2 H 3.21 . 2 1039 121 HIS HB3 H 3.31 . 2 1040 121 HIS CD2 C 120.25 . 1 1041 121 HIS CE1 C 137.55 . 1 1042 121 HIS HD2 H 6.76 . 1 1043 121 HIS HE1 H 8.32 . 1 1044 122 TYR N N 117.87 . 1 1045 122 TYR H H 7.84 . 1 1046 122 TYR CA C 58.85 . 1 1047 122 TYR HA H 4.52 . 1 1048 122 TYR CB C 38.75 . 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 133.55 . 1 1056 122 TYR CE1 C 118.35 . 1 1057 123 GLN N N 120.97 . 1 1058 123 GLN H H 7.95 . 1 1059 123 GLN CA C 55.95 . 1 1060 123 GLN HA H 4.36 . 1 1061 123 GLN CB C 29.95 . 1 1062 123 GLN HB2 H 2.15 . 2 1063 123 GLN HB3 H 2.02 . 2 1064 123 GLN CG C 33.95 . 1 1065 123 GLN HG2 H 2.40 . 1 1066 123 GLN HG3 H 2.40 . 1 1068 124 GLU H H 7.99 . 1 1070 124 GLU HA H 4.11 . 1 1072 124 GLU HB2 H 2.08 . 2 1073 124 GLU HB3 H 1.96 . 2 1074 124 GLU CG C 36.85 . 1 1075 124 GLU HG2 H 2.30 . 1 1076 124 GLU HG3 H 2.30 . 1 stop_ save_ ####################################### # Cited references within the entry # ####################################### save_ref_1 _Saveframe_category citation _MEDLINE_UI_code 7827089 save_