data_4083 #Corrected using PDB structure: 1UDRD # #N.B. (Observed* = Observed shift + Offset correction) # #After reference correction, the following residues still #have a CA chemical shift difference (obs*-pred) greater than 5.0ppm: #NUM AA CS Observed* Predicted # 61 N CA 59.10 53.66 # #The average CS difference between predicted and observed: #HA CA CB CO N HN #-0.02 0.10 0.24 N/A 1.35 -0.04 # #bmr4083.str.corr chemical shifts have been re-referenced with the following #offsets (these values have been added to the original bmr4083.str file): #HA CA CB CO N HN #N/A +0.17 +0.17 N/A +1.35 N/A # #The 95% confidence intervals for the above recommended offsets are: # HA CA CB CO N HN #+/-0.03 +/-0.13 +/-0.16 N/A +/-0.31 +/-0.06 # #The Correlation Coefficients between predicted and observed #chemical shifts are: #HA CA CB CO N HN #0.902 0.968 0.994 N/A 0.908 0.685 # #The RMSD between predicted and observed* (reference #corrected) chemical shifts are: #HA CA CB CO N HN #0.145 0.712 0.820 N/A 1.651 0.310 # ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Assignments, Secondary Structure, Global Fold, and Dynamics of Chemotaxis Y Protein Using Three- and Four-Dimensional Heteronuclear (13C, 15N) NMR Spectroscopy ; loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Moy Frankln L. . 2 Lowry David F. . 3 Matsumura Philip . . 4 Dahlquist Frederick W. . 5 Krywko James E. . 6 Domaille Peter J. . stop_ _BMRB_accession_number 4083 _BMRB_flat_file_name bmr4083.str _Entry_type reformat _Submission_date 1997-12-23 _Accession_date 1997-12-23 _Entry_origination BMRB _NMR_STAR_version 2.1 _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' 722 '13C chemical shifts' 423 '15N chemical shifts' 127 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2001-02-17 reformat BMRB 'Format updated to NMR-STAR version 2.1' stop_ save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full ; Moy, F. L., Lowry, D. F., Matsumura, P., Dahlquist, F. W., Krywko, J. E., and Domaille, P. J., "Assignments, Secondary Structure, Global Fold, and Dynamics of Chemotaxis Y Protein Using Three- and Four-Dimensional Heteronuclear (13C, 15N) NMR Spectroscopy," Biochemistry 33, 10731-10742 (1994). ; _Citation_title ; Assignments, Secondary Structure, Global Fold, and Dynamics of Chemotaxis Y Protein Using Three- and Four-Dimensional Heteronuclear (13C, 15N) NMR Spectroscopy ; _Citation_status published _Citation_type journal _MEDLINE_UI_code . _PubMed_ID . loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Moy Frankln L. . 2 Lowry David F. . 3 Matsumura Philip . . 4 Dahlquist Frederick W. . 5 Krywko James E. . 6 Domaille Peter J. . stop_ _Journal_abbreviation Biochemistry _Journal_volume 33 _Journal_issue 35 _Page_first 10731 _Page_last 10742 _Year 1994 loop_ _Keyword NMR 'nuclear magnetic resonance' CheY 'chemotaxis Y protein' stop_ save_ ################################## # Molecular system description # ################################## save_system_CheY _Saveframe_category molecular_system _Mol_system_name CheY _Abbreviation_common CheY loop_ _Mol_system_component_name _Mol_label CheY $CheY stop_ _System_physical_state native _System_oligomer_state monomer _System_paramagnetic no _System_thiol_state 'not present' loop_ _Biological_function ; Recombinant E. coli CheY, a 128 residue protein is involved in regulating bacterial chemotaxis by binding to the flagellar motor of a bacteria. ; stop_ save_ ######################## # Monomeric polymers # ######################## save_CheY _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'E. coli CheY' _Abbreviation_common 'CheY' _Mol_thiol_state 'not present' ############################## # Polymer residue sequence # ############################## _Residue_count 128 _Mol_residue_sequence ; ADKELKFLVVDDFSTMRRIV RNLLKELGFNNVEEAEDGVD ALNKLQAGGYGFVISDWNMP NMDGLELLKTIRADGAMSAL PVLMVTAEAKKENIIAAAQA GASGYVVKPFTAATLEEKLN KIFEKLGM ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 2 ALA 2 3 ASP 3 4 LYS 4 5 GLU 5 6 LEU 6 7 LYS 7 8 PHE 8 9 LEU 9 10 VAL 10 11 VAL 11 12 ASP 12 13 ASP 13 14 PHE 14 15 SER 15 16 THR 16 17 MET 17 18 ARG 18 19 ARG 19 20 ILE 20 21 VAL 21 22 ARG 22 23 ASN 23 24 LEU 24 25 LEU 25 26 LYS 26 27 GLU 27 28 LEU 28 29 GLY 29 30 PHE 30 31 ASN 31 32 ASN 32 33 VAL 33 34 GLU 34 35 GLU 35 36 ALA 36 37 GLU 37 38 ASP 38 39 GLY 39 40 VAL 40 41 ASP 41 42 ALA 42 43 LEU 43 44 ASN 44 45 LYS 45 46 LEU 46 47 GLN 47 48 ALA 48 49 GLY 49 50 GLY 50 51 TYR 51 52 GLY 52 53 PHE 53 54 VAL 54 55 ILE 55 56 SER 56 57 ASP 57 58 TRP 58 59 ASN 59 60 MET 60 61 PRO 61 62 ASN 62 63 MET 63 64 ASP 64 65 GLY 65 66 LEU 66 67 GLU 67 68 LEU 68 69 LEU 69 70 LYS 70 71 THR 71 72 ILE 72 73 ARG 73 74 ALA 74 75 ASP 75 76 GLY 76 77 ALA 77 78 MET 78 79 SER 79 80 ALA 80 81 LEU 81 82 PRO 82 83 VAL 83 84 LEU 84 85 MET 85 86 VAL 86 87 THR 87 88 ALA 88 89 GLU 89 90 ALA 90 91 LYS 91 92 LYS 92 93 GLU 93 94 ASN 94 95 ILE 95 96 ILE 96 97 ALA 97 98 ALA 98 99 ALA 99 100 GLN 100 101 ALA 101 102 GLY 102 103 ALA 103 104 SER 104 105 GLY 105 106 TYR 106 107 VAL 107 108 VAL 108 109 LYS 109 110 PRO 110 111 PHE 111 112 THR 112 113 ALA 113 114 ALA 114 115 THR 115 116 LEU 116 117 GLU 117 118 GLU 118 119 LYS 119 120 LEU 120 121 ASN 121 122 LYS 122 123 ILE 123 124 PHE 124 125 GLU 125 126 LYS 126 127 LEU 127 128 GLY 128 129 MET 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 1AB5 "A Chain A, Structure Of Chey Mutant F14n, V21t" 102.40 125 98 98 1e-62 PDB 1AB6 "A Chain A, Structure Of Chey Mutant F14n, V86t" 102.40 125 98 98 1e-62 PDB 1E6L "A Chain A, Two-Component Signal TransductionSystem D13a Mutant Of Chey" 100.79 127 99 99 10e-65 PDB 1A0O "A Chain A, Chey-Binding Domain Of Chea InComplex With Chey" 100.00 128 100 100 6e-66 PDB 1BDJ "A Chain A, Complex Structure Of Hpt Domain AndChey" 100.00 128 100 100 6e-66 PDB 1CEY "Chey Complexed With Magnesium (Nmr, 46Structures)" 100.00 128 100 100 2e-65 PDB 1CHN "Chey Complexed With Mg2+ In The Active Site" 100.00 128 100 100 6e-66 PDB 1EAY "A Chain A, Chey-Binding (P2) Domain Of Chea InComplex With Chey From Escherichia Coli" 100.00 128 100 100 6e-66 PDB 1F4V "A Chain A, Crystal Structure Of Activated CheyBound To The N-Terminus Of Flim" 100.00 128 100 100 6e-66 PDB 1FFG "A Chain A, Chey-Binding Domain Of Chea InComplex With Chey At 2.1 A Resolution" 100.00 128 100 100 6e-66 PDB 1FFS "A Chain A, Chey-Binding Domain Of Chea InComplex With Chey From Crystals Soaked In AcetylPhosphate" 100.00 128 100 100 6e-66 PDB 1FFW "A Chain A, Chey-Binding Domain Of Chea InComplex With Chey With A Bound Imido Diphosphate" 100.00 128 100 100 6e-66 PDB 1FQW "A Chain A, Crystal Structure Of Activated Chey" 100.00 128 100 100 6e-66 PDB 3CHY CheY 100.00 128 100 100 6e-66 PDB 1C4W "A Chain A, 1.9 A Structure Of A-ThiophosphonateModified Chey D57c" 100.00 128 99 99 4e-65 PDB 1D4Z "A Chain A, Crystal Structure Of Chey-95iv, AHyperactive Chey Mutant" 100.00 128 99 100 8e-66 PDB 1EHC "Structure Of Signal Transduction Protein Chey" 100.00 128 99 99 4e-65 PDB 1VLZ "A Chain A, Chey Mutant With Thr 87 Replaced ByIle (T87i)" 100.00 128 99 99 3e-65 PDB 5CHY "Structure Of Chemotaxis Protein Chey" 100.00 128 99 100 2e-65 PDB 1E6M "A Chain A, Two-Component Signal TransductionSystem D57a Mutant Of Chey" 100.00 128 98 99 10e-65 PDB 1JBE "A Chain A, 1.08 A Structure Of Apo-CheyReveals Meta-Active Conformation" 100.00 128 98 98 3e-64 PDB 6CHY "A Chain A, Structure Of Chemotaxis Protein Chey" 100.00 128 98 99 10e-65 PDB 2CHE "Chey Complexed With Mg2+" 100.00 128 98 99 10e-65 PDB 2CHF Chey 100.00 128 98 99 10e-65 PDB 1DJM "A Chain A, Solution Structure Of Bef3-ActivatedChey From Escherichia Coli" 99.22 129 100 100 6e-66 PDB 1KMI "Y Chain Y, Crystal Structure Of An E.ColiChemotaxis Protein, Chez" 99.22 129 100 100 6e-66 PDB 1CYE "Chey Mutant With Met 1 Deleted, Arg 1Inserted, And Ala 2 Replaced By Ser(Del(M1),Ins(R1),A2s) (Nmr, 20 Structures)" 99.22 129 99 100 10e-66 PDB 1MIH "A Chain A, A Role For Chey Glu 89 InChez-Mediated Dephosphorylation Of The E. ColiChemotaxis Response Regulator Chey" 99.22 129 99 99 3e-65 PDB 1E6K "A Chain A, Two-Component Signal TransductionSystem D12a Mutant Of Chey" 98.46 130 98 99 10e-65 PDB 1YMU "A Chain A, Signal Transduction Protein CheyMutant With Met 17 Replaced By Gly (M17g)" 98.46 130 98 99 10e-65 DBJ BAA15698.1 "Chemotaxis protein CheY [Escherichiacoli]" 99.22 129 100 100 6e-66 DBJ BAB36015.1 "chemotaxis protein CheY [Escherichiacoli O157:H7]" 99.22 129 100 100 6e-66 EMBL CAD05667.1 "chemotaxis protein CheY [Salmonellaenterica subsp. enterica serovar Typhi]" 99.22 129 98 99 10e-65 GenBank AAA23577.1 "CheY [Escherichia coli]" 99.22 129 100 100 6e-66 GenBank AAC74952.1 "chemotaxis regulator transmitschemoreceptor signals to flagelllar motor components;chemotactic response regulator in two-componentregulatory system with CheA, transmits signals to FliMflagelllar motor component [Escherichia coli K12]" 99.22 129 100 100 6e-66 GenBank AAG56872.1 "chemotaxis regulator transmitschemoreceptor signals to flagelllar motor components[Escherichia coli O157:H7 EDL933]" 99.22 129 100 100 6e-66 GenBank AAN43484.1 "chemotaxis regulator transmitschemoreceptor signals to flagelllar motor components[Shigella flexneri 2a str. 301]" 99.22 129 100 100 6e-66 GenBank AAP17314.1 "chemotaxis protein CheY [Shigellaflexneri 2a str. 2457T]" 99.22 129 100 100 6e-66 PIR D85801 "chemotaxis protein cheY [validated] -Escherichia coli (strain O157:H7, substrain EDL933)" 99.22 129 100 100 6e-66 PIR H90952 "chemotaxis protein CheY [imported] -Escherichia coli (strain O157:H7, substrain RIMD0509952)" 99.22 129 100 100 6e-66 PIR QRECCY "chemotaxis protein cheY [validated] -Escherichia coli (strain K-12)" 99.22 129 100 100 6e-66 PIR AH0745 "chemotaxis protein CheY [imported] -Salmonella enterica subsp. enterica serovar Typhi(strain CT18)" 99.22 129 98 99 10e-65 PIR QREBCY "chemotaxis protein cheY [validated] -Salmonella typhimurium" 99.22 129 98 99 10e-65 REF NP_288319.1 "chemotaxis regulator transmitschemoreceptor signals to flagelllar motor components[Escherichia coli O157:H7 EDL933]" 99.22 129 100 100 6e-66 REF NP_310619.1 "CheY [Escherichia coli O157:H7]" 99.22 129 100 100 6e-66 REF NP_416396.1 "chemotaxis regulator transmitschemoreceptor signals to flagelllar motor components;chemotactic response regulator in two-componentregulatory system with CheA, transmits signals to FliMflagelllar motor component [Escherichia coli K12]" 99.22 129 100 100 6e-66 REF NP_707777.1 "chemotaxis regulator transmitschemoreceptor signals to flagelllar motor components[Shigella flexneri 2a str. 301]" 99.22 129 100 100 6e-66 REF NP_837505.1 "chemotaxis protein CheY [Shigellaflexneri 2a str. 2457T]" 99.22 129 100 100 6e-66 SWISS-PROT P06143 "CHEY_ECOLI Chemotaxis protein cheY" 99.22 129 100 100 6e-66 SWISS-PROT Q8FGP6 "CHEY_ECOL6 Chemotaxis protein cheY" 99.22 129 99 100 10e-66 SWISS-PROT P06657 "CHEY_SALTY Chemotaxis protein cheY" 99.22 129 98 99 10e-65 stop_ save_ ############# # Ligands # ############# save_Mg2+ _Saveframe_category ligand _Mol_type non-polymer _Name_common magnesium _Abbreviation_common Mg2+ _Mol_paramagnetic no save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $CheY 'E. coli' 562 Eubacteria . Escherichia coli stop_ save_ ######################### # Experimental source # ######################### save_experimental_source _Saveframe_category experimental_source loop_ _Mol_label _Production_method _Host_organism_name_common _Genus _Species $CheY 'recombinant technology' 'E. coli' Escherichia coli stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_one _Saveframe_category sample _Sample_type solution loop_ _Mol_label _Concentration_value _Concentration_value_units _Concentration_min_value _Concentration_max_value _Isotopic_labeling $CheY . mM 1.0 4.0 '[U-15N]' 'sodium phosphate' 100 mM . . . 'magnesium chloride' . mM 4 5 . 'sodium azide' 0.02 % . . . D2O 10 % . . . H2O 90 % . . . stop_ save_ save_sample_two _Saveframe_category sample _Sample_type solution loop_ _Mol_label _Concentration_value _Concentration_value_units _Concentration_min_value _Concentration_max_value _Isotopic_labeling $CheY . mM 1.0 4.0 '[U-13C; U-15N]' 'sodium phosphate' 100 mM . . . 'magnesium chloride' . mM 4 5 . 'sodium azide' 0.02 % . . . D2O 10 % . . . H2O 90 % . . . stop_ save_ save_sample_three _Saveframe_category sample _Sample_type solution loop_ _Mol_label _Concentration_value _Concentration_value_units _Concentration_min_value _Concentration_max_value _Isotopic_labeling $CheY . mM 1.0 4.0 '[U-13C; U-15N]' 'sodium phosphate' 100 mM . . . 'magnesium chloride' . mM 4 5 . 'sodium azide' 0.02 % . . . D2O 99.8 % . . . stop_ save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer_one _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model AMX _Field_strength 600 save_ ####################### # Sample conditions # ####################### save_sample_conditions _Saveframe_category sample_conditions loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 6.75 0.05 n/a temperature 303 . K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chem_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 _Indirect_shift_ratio TSP H 1 'methyl protons' ppm 0.00 external . . TSP C 13 'methyl carbons' ppm 0.00 external . . 'liquid ammonia' N 15 nitrogen ppm 0.00 external . . 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_assignment _Saveframe_category assigned_chemical_shifts loop_ _Sample_label $sample_three stop_ _Sample_conditions_label $sample_conditions _Chem_shift_reference_set_label $chem_shift_reference _Mol_system_component_name CheY 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 1 ALA HA H 3.90 . 1 2 1 ALA HB H 0.81 . 1 3 1 ALA CA C 51.07 . 1 4 1 ALA CB C 18.67 . 1 5 2 ASP HA H 4.49 . 1 6 2 ASP HB2 H 2.73 . 2 7 2 ASP HB3 H 2.64 . 2 8 2 ASP CA C 53.87 . 1 9 2 ASP CB C 41.77 . 1 10 3 LYS H H 8.48 . 1 11 3 LYS HA H 4.26 . 1 12 3 LYS HB2 H 1.98 . 2 13 3 LYS HB3 H 1.77 . 2 14 3 LYS HG2 H 1.38 . 2 15 3 LYS HG3 H 1.27 . 2 16 3 LYS HD2 H 1.19 . 2 17 3 LYS HD3 H 1.15 . 2 18 3 LYS HE2 H 2.78 . 1 19 3 LYS HE3 H 2.78 . 1 20 3 LYS CA C 57.17 . 1 21 3 LYS CB C 30.67 . 1 22 3 LYS CG C 24.67 . 1 23 3 LYS CD C 27.97 . 1 24 3 LYS CE C 42.17 . 1 25 3 LYS N N 122.15 . 1 26 4 GLU H H 8.68 . 1 27 4 GLU HA H 4.48 . 1 28 4 GLU HB2 H 2.27 . 2 29 4 GLU HB3 H 1.97 . 2 30 4 GLU HG2 H 2.35 . 1 31 4 GLU HG3 H 2.35 . 1 32 4 GLU CA C 55.87 . 1 33 4 GLU CB C 29.17 . 1 34 4 GLU CG C 36.47 . 1 35 4 GLU N N 119.25 . 1 36 5 LEU H H 7.51 . 1 37 5 LEU HA H 3.84 . 1 38 5 LEU HB2 H 1.80 . 2 39 5 LEU HB3 H 1.63 . 2 40 5 LEU HG H 1.21 . 1 41 5 LEU HD1 H 0.81 . 2 42 5 LEU HD2 H 0.65 . 2 43 5 LEU CA C 56.57 . 1 44 5 LEU CB C 43.27 . 1 45 5 LEU CG C 26.37 . 1 46 5 LEU CD1 C 25.17 . 2 47 5 LEU CD2 C 26.67 . 2 48 5 LEU N N 124.05 . 1 49 6 LYS H H 8.47 . 1 50 6 LYS HA H 5.10 . 1 51 6 LYS HB2 H 1.88 . 2 52 6 LYS HB3 H 1.50 . 2 53 6 LYS HG2 H 1.13 . 1 54 6 LYS HG3 H 1.13 . 1 55 6 LYS HD2 H 1.16 . 2 56 6 LYS HD3 H 0.83 . 2 57 6 LYS HE2 H 2.47 . 2 58 6 LYS HE3 H 2.22 . 2 59 6 LYS CA C 56.27 . 1 60 6 LYS CB C 33.67 . 1 61 6 LYS CD C 29.27 . 1 62 6 LYS CE C 41.37 . 1 63 6 LYS N N 126.05 . 1 64 7 PHE H H 9.20 . 1 65 7 PHE HA H 5.41 . 1 66 7 PHE HB2 H 3.21 . 2 67 7 PHE HB3 H 2.54 . 2 68 7 PHE HD1 H 7.02 . 1 69 7 PHE HD2 H 7.02 . 1 70 7 PHE HE1 H 6.21 . 1 71 7 PHE HE2 H 6.21 . 1 72 7 PHE HZ H 5.66 . 1 73 7 PHE CA C 57.27 . 1 74 7 PHE CB C 43.57 . 1 75 7 PHE CD1 C 131.07 . 1 76 7 PHE CD2 C 131.07 . 1 77 7 PHE CE1 C 131.37 . 1 78 7 PHE CE2 C 131.37 . 1 79 7 PHE CZ C 128.17 . 1 80 7 PHE N N 128.55 . 1 81 8 LEU H H 8.78 . 1 82 8 LEU HA H 5.13 . 1 83 8 LEU HB2 H 1.70 . 2 84 8 LEU HB3 H 1.09 . 2 85 8 LEU HG H 1.16 . 1 86 8 LEU HD1 H 0.56 . 2 87 8 LEU HD2 H 0.38 . 2 88 8 LEU CA C 53.07 . 1 89 8 LEU CB C 44.07 . 1 90 8 LEU CD1 C 22.87 . 2 91 8 LEU CD2 C 27.27 . 2 92 8 LEU N N 121.85 . 1 93 9 VAL H H 9.04 . 1 94 9 VAL HA H 4.80 . 1 95 9 VAL HB H 1.99 . 1 96 9 VAL HG1 H 0.99 . 1 97 9 VAL HG2 H 0.99 . 1 98 9 VAL CA C 61.57 . 1 99 9 VAL CB C 33.17 . 1 100 9 VAL CG1 C 21.27 . 1 101 9 VAL CG2 C 21.27 . 1 102 9 VAL N N 127.45 . 1 103 10 VAL H H 9.21 . 1 104 10 VAL HA H 4.82 . 1 105 10 VAL HB H 2.27 . 1 106 10 VAL HG1 H 0.65 . 2 107 10 VAL HG2 H 0.68 . 2 108 10 VAL CA C 59.87 . 1 109 10 VAL CB C 32.77 . 1 110 10 VAL CG1 C 21.57 . 2 111 10 VAL CG2 C 21.47 . 2 112 10 VAL N N 127.55 . 1 113 11 ASP H H 8.11 . 1 114 11 ASP HA H 4.65 . 1 115 11 ASP HB2 H 2.74 . 2 116 11 ASP HB3 H 2.53 . 2 117 11 ASP CA C 55.57 . 1 118 11 ASP CB C 43.77 . 1 119 11 ASP N N 124.75 . 1 120 12 ASP H H 9.38 . 1 121 12 ASP HA H 5.08 . 1 122 12 ASP HB2 H 2.98 . 2 123 12 ASP HB3 H 2.80 . 2 124 12 ASP CA C 55.17 . 1 125 12 ASP CB C 40.27 . 1 126 12 ASP N N 124.25 . 1 127 13 PHE HA H 5.26 . 1 128 13 PHE HB2 H 3.22 . 1 129 13 PHE HB3 H 3.22 . 1 130 13 PHE HD1 H 7.42 . 1 131 13 PHE HD2 H 7.42 . 1 132 13 PHE HE1 H 7.36 . 1 133 13 PHE HE2 H 7.36 . 1 134 13 PHE HZ H 6.71 . 1 135 13 PHE CA C 54.47 . 1 136 13 PHE CB C 38.27 . 1 137 13 PHE CD1 C 130.67 . 1 138 13 PHE CD2 C 130.67 . 1 139 13 PHE CE1 C 128.97 . 1 140 13 PHE CE2 C 128.97 . 1 141 13 PHE CZ C 128.67 . 1 142 15 THR HA H 3.77 . 1 143 15 THR HB H 3.23 . 1 144 15 THR HG2 H 1.15 . 1 145 15 THR CA C 65.57 . 1 146 15 THR CB C 68.27 . 1 147 15 THR CG2 C 21.67 . 1 148 16 MET H H 6.49 . 1 149 16 MET HA H 4.51 . 1 150 16 MET HB2 H 2.18 . 1 151 16 MET HB3 H 2.18 . 1 152 16 MET HG2 H 2.76 . 2 153 16 MET HG3 H 2.66 . 2 154 16 MET CA C 56.07 . 1 155 16 MET CB C 31.27 . 1 156 16 MET CG C 32.77 . 1 157 16 MET N N 119.15 . 1 158 17 ARG H H 7.57 . 1 159 17 ARG HA H 3.82 . 1 160 17 ARG HB2 H 2.03 . 2 161 17 ARG HB3 H 1.81 . 2 162 17 ARG HG2 H 1.38 . 2 163 17 ARG HG3 H 1.28 . 2 164 17 ARG HD2 H 2.92 . 1 165 17 ARG HD3 H 2.92 . 1 166 17 ARG CA C 60.67 . 1 167 17 ARG CB C 30.67 . 1 168 17 ARG CG C 24.47 . 1 169 17 ARG CD C 41.57 . 1 170 17 ARG N N 117.15 . 1 171 18 ARG H H 7.62 . 1 172 18 ARG HA H 3.93 . 1 173 18 ARG HB2 H 1.93 . 1 174 18 ARG HB3 H 1.93 . 1 175 18 ARG HG2 H 1.70 . 2 176 18 ARG HG3 H 1.63 . 2 177 18 ARG HD2 H 3.22 . 2 178 18 ARG HD3 H 3.05 . 2 179 18 ARG CA C 58.97 . 1 180 18 ARG CB C 29.57 . 1 181 18 ARG CG C 27.37 . 1 182 18 ARG CD C 43.27 . 1 183 18 ARG N N 116.95 . 1 184 19 ILE H H 7.76 . 1 185 19 ILE HA H 3.72 . 1 186 19 ILE HB H 2.11 . 1 187 19 ILE HG12 H 1.80 . 2 188 19 ILE HG13 H 1.09 . 2 189 19 ILE HG2 H 0.79 . 1 190 19 ILE HD1 H 0.81 . 1 191 19 ILE CA C 65.57 . 1 192 19 ILE CB C 37.97 . 1 193 19 ILE CG1 C 29.47 . 1 194 19 ILE CG2 C 16.47 . 1 195 19 ILE CD1 C 13.37 . 1 196 19 ILE N N 120.35 . 1 197 20 VAL H H 8.28 . 1 198 20 VAL HA H 3.43 . 1 199 20 VAL HB H 2.15 . 1 200 20 VAL HG1 H 1.16 . 2 201 20 VAL HG2 H 0.94 . 2 202 20 VAL CA C 67.37 . 1 203 20 VAL CB C 31.17 . 1 204 20 VAL CG1 C 23.57 . 2 205 20 VAL CG2 C 22.77 . 2 206 20 VAL N N 119.15 . 1 207 21 ARG H H 8.60 . 1 208 21 ARG HA H 3.82 . 1 209 21 ARG HB2 H 2.03 . 2 210 21 ARG HB3 H 1.80 . 2 211 21 ARG HG2 H 1.52 . 1 212 21 ARG HG3 H 1.52 . 1 213 21 ARG HD2 H 3.27 . 2 214 21 ARG HD3 H 3.10 . 2 215 21 ARG CA C 60.57 . 1 216 21 ARG CB C 30.67 . 1 217 21 ARG CG C 27.57 . 1 218 21 ARG CD C 43.97 . 1 219 21 ARG N N 119.55 . 1 220 22 ASN H H 8.42 . 1 221 22 ASN HA H 4.56 . 1 222 22 ASN HB2 H 3.03 . 2 223 22 ASN HB3 H 2.84 . 2 224 22 ASN HD21 H 7.53 . 2 225 22 ASN HD22 H 7.02 . 2 226 22 ASN CA C 55.87 . 1 227 22 ASN CB C 37.67 . 1 228 22 ASN N N 119.05 . 1 229 22 ASN ND2 N 109.70 . 1 230 23 LEU H H 8.44 . 1 231 23 LEU HA H 4.16 . 1 232 23 LEU HB2 H 2.06 . 2 233 23 LEU HB3 H 1.16 . 2 234 23 LEU HD1 H 0.73 . 2 235 23 LEU HD2 H 0.87 . 2 236 23 LEU CA C 58.17 . 1 237 23 LEU CB C 42.47 . 1 238 23 LEU CD1 C 26.67 . 2 239 23 LEU CD2 C 22.57 . 2 240 23 LEU N N 123.15 . 1 241 24 LEU H H 8.33 . 1 242 24 LEU HA H 3.83 . 1 243 24 LEU HB2 H 1.83 . 2 244 24 LEU HB3 H 1.34 . 2 245 24 LEU HG H 1.42 . 1 246 24 LEU HD1 H 0.17 . 2 247 24 LEU HD2 H -0.14 . 2 248 24 LEU CA C 58.37 . 1 249 24 LEU CB C 40.27 . 1 250 24 LEU CG C 26.67 . 1 251 24 LEU CD1 C 26.87 . 2 252 24 LEU CD2 C 22.47 . 2 253 24 LEU N N 117.95 . 1 254 25 LYS H H 7.94 . 1 255 25 LYS HA H 3.75 . 1 256 25 LYS HB2 H 2.07 . 1 257 25 LYS HB3 H 2.07 . 1 258 25 LYS HG2 H 1.63 . 2 259 25 LYS HG3 H 1.41 . 2 260 25 LYS HD2 H 1.79 . 1 261 25 LYS HD3 H 1.79 . 1 262 25 LYS HE2 H 2.98 . 1 263 25 LYS HE3 H 2.98 . 1 264 25 LYS CA C 59.97 . 1 265 25 LYS CB C 31.77 . 1 266 25 LYS CG C 24.87 . 1 267 25 LYS CD C 29.77 . 1 268 25 LYS CE C 41.57 . 1 269 25 LYS N N 120.55 . 1 270 26 GLU H H 7.95 . 1 271 26 GLU HA H 3.99 . 1 272 26 GLU HB2 H 2.30 . 2 273 26 GLU HB3 H 2.17 . 2 274 26 GLU HG2 H 2.45 . 1 275 26 GLU HG3 H 2.45 . 1 276 26 GLU CA C 59.47 . 1 277 26 GLU CB C 28.97 . 1 278 26 GLU CG C 36.17 . 1 279 26 GLU N N 122.25 . 1 280 27 LEU H H 7.43 . 1 281 27 LEU HA H 4.28 . 1 282 27 LEU HB2 H 2.16 . 2 283 27 LEU HB3 H 1.83 . 2 284 27 LEU HD1 H 0.88 . 1 285 27 LEU HD2 H 0.88 . 1 286 27 LEU CA C 54.47 . 1 287 27 LEU CB C 42.37 . 1 288 27 LEU CG C 26.27 . 1 289 27 LEU CD1 C 24.97 . 2 290 27 LEU CD2 C 21.97 . 2 291 27 LEU N N 117.05 . 1 292 28 GLY H H 7.74 . 1 293 28 GLY HA2 H 3.94 . 2 294 28 GLY HA3 H 3.54 . 2 295 28 GLY CA C 44.77 . 1 296 28 GLY N N 106.25 . 1 297 29 PHE H H 8.17 . 1 298 29 PHE HA H 4.86 . 1 299 29 PHE HB2 H 3.08 . 2 300 29 PHE HB3 H 2.45 . 2 301 29 PHE HD1 H 7.29 . 1 302 29 PHE HD2 H 7.29 . 1 303 29 PHE HE1 H 7.31 . 1 304 29 PHE HE2 H 7.31 . 1 305 29 PHE CA C 57.27 . 1 306 29 PHE CB C 38.77 . 1 307 29 PHE CD1 C 133.07 . 1 308 29 PHE CD2 C 133.07 . 1 309 29 PHE CE1 C 130.97 . 1 310 29 PHE CE2 C 130.97 . 1 311 29 PHE N N 121.05 . 1 312 30 ASN H H 8.28 . 1 313 30 ASN HA H 4.68 . 1 314 30 ASN HB2 H 2.83 . 2 315 30 ASN HB3 H 2.66 . 2 316 30 ASN HD21 H 7.39 . 2 317 30 ASN HD22 H 6.88 . 2 318 30 ASN CA C 53.77 . 1 319 30 ASN CB C 40.67 . 1 320 30 ASN N N 118.15 . 1 321 30 ASN ND2 N 111.80 . 1 322 31 ASN H H 9.82 . 1 323 31 ASN HA H 5.01 . 1 324 31 ASN HB2 H 3.27 . 2 325 31 ASN HB3 H 2.88 . 2 326 31 ASN HD21 H 7.56 . 2 327 31 ASN HD22 H 7.00 . 2 328 31 ASN CA C 52.27 . 1 329 31 ASN CB C 36.57 . 1 330 31 ASN N N 124.35 . 1 331 31 ASN ND2 N 109.20 . 1 332 32 VAL H H 7.53 . 1 333 32 VAL HA H 4.99 . 1 334 32 VAL HB H 1.85 . 1 335 32 VAL HG1 H 0.83 . 1 336 32 VAL HG2 H 0.83 . 1 337 32 VAL CA C 60.97 . 1 338 32 VAL CB C 36.47 . 1 339 32 VAL CG1 C 22.77 . 1 340 32 VAL CG2 C 22.77 . 1 341 32 VAL N N 122.15 . 1 342 33 GLU H H 9.06 . 1 343 33 GLU HA H 4.93 . 1 344 33 GLU HB2 H 2.31 . 2 345 33 GLU HB3 H 2.16 . 2 346 33 GLU HG2 H 2.57 . 1 347 33 GLU HG3 H 2.45 . 2 348 33 GLU CA C 53.97 . 1 349 33 GLU CB C 34.17 . 1 350 33 GLU CG C 36.37 . 1 351 33 GLU N N 126.75 . 1 352 34 GLU H H 8.92 . 1 353 34 GLU HA H 5.44 . 1 354 34 GLU HB2 H 1.90 . 1 355 34 GLU HB3 H 1.90 . 1 356 34 GLU HG2 H 2.15 . 1 357 34 GLU HG3 H 2.06 . 2 358 34 GLU CA C 54.87 . 1 359 34 GLU CB C 34.97 . 1 360 34 GLU CG C 35.67 . 1 361 34 GLU N N 120.95 . 1 362 35 ALA H H 8.84 . 1 363 35 ALA HA H 4.81 . 1 364 35 ALA HB H 1.30 . 1 365 35 ALA CA C 50.27 . 1 366 35 ALA CB C 22.87 . 1 367 35 ALA N N 120.35 . 1 368 36 GLU H H 9.48 . 1 369 36 GLU HA H 4.62 . 1 370 36 GLU HB2 H 2.06 . 1 371 36 GLU HB3 H 2.06 . 1 372 36 GLU HG2 H 2.20 . 1 373 36 GLU HG3 H 2.20 . 1 374 36 GLU CA C 56.87 . 1 375 36 GLU CB C 31.97 . 1 376 36 GLU CG C 35.87 . 1 377 36 GLU N N 117.45 . 1 378 37 ASP H H 7.49 . 1 379 37 ASP HA H 5.30 . 1 380 37 ASP HB2 H 3.51 . 2 381 37 ASP HB3 H 3.30 . 2 382 37 ASP CA C 53.87 . 1 383 37 ASP CB C 41.47 . 1 384 37 ASP N N 110.25 . 1 385 38 GLY H H 8.08 . 1 386 38 GLY HA2 H 3.75 . 2 387 38 GLY HA3 H 3.61 . 2 388 38 GLY CA C 48.57 . 1 389 38 GLY N N 102.15 . 1 390 39 VAL H H 7.95 . 1 391 39 VAL HA H 3.50 . 1 392 39 VAL HB H 2.26 . 1 393 39 VAL HG1 H 0.90 . 1 394 39 VAL HG2 H 0.90 . 1 395 39 VAL CA C 66.07 . 1 396 39 VAL CB C 31.57 . 1 397 39 VAL CG1 C 21.27 . 1 398 39 VAL CG2 C 21.27 . 1 399 39 VAL N N 122.75 . 1 400 40 ASP H H 8.57 . 1 401 40 ASP HA H 4.44 . 1 402 40 ASP HB2 H 2.97 . 2 403 40 ASP HB3 H 2.60 . 2 404 40 ASP CA C 56.57 . 1 405 40 ASP CB C 42.57 . 1 406 40 ASP N N 121.15 . 1 407 41 ALA H H 8.30 . 1 408 41 ALA HA H 3.61 . 1 409 41 ALA HB H 1.36 . 1 410 41 ALA CA C 55.17 . 1 411 41 ALA CB C 19.97 . 1 412 41 ALA N N 116.95 . 1 413 42 LEU H H 8.12 . 1 414 42 LEU HA H 3.75 . 1 415 42 LEU HB2 H 1.74 . 2 416 42 LEU HB3 H 1.51 . 2 417 42 LEU CA C 58.37 . 1 418 42 LEU CB C 41.37 . 1 419 42 LEU N N 118.45 . 1 420 43 ASN H H 7.85 . 1 421 43 ASN HA H 4.39 . 1 422 43 ASN HB2 H 3.05 . 2 423 43 ASN HB3 H 2.88 . 2 424 43 ASN HD21 H 7.78 . 2 425 43 ASN HD22 H 6.83 . 2 426 43 ASN CA C 56.17 . 1 427 43 ASN CB C 38.17 . 1 428 43 ASN N N 116.95 . 1 429 43 ASN ND2 N 111.10 . 1 430 44 LYS H H 7.92 . 1 431 44 LYS HA H 4.11 . 1 432 44 LYS HB2 H 1.76 . 1 433 44 LYS HB3 H 1.76 . 1 434 44 LYS HG2 H 1.43 . 1 435 44 LYS HG3 H 1.43 . 1 436 44 LYS HD2 H 1.69 . 1 437 44 LYS HD3 H 1.69 . 1 438 44 LYS HE2 H 2.96 . 1 439 44 LYS HE3 H 2.96 . 1 440 44 LYS CA C 60.17 . 1 441 44 LYS CB C 32.07 . 1 442 44 LYS CG C 24.67 . 1 443 44 LYS CD C 29.17 . 1 444 44 LYS CE C 41.87 . 1 445 44 LYS N N 120.35 . 1 446 45 LEU H H 8.75 . 1 447 45 LEU HA H 3.83 . 1 448 45 LEU HB2 H 1.75 . 2 449 45 LEU HB3 H 1.41 . 2 450 45 LEU HD1 H 0.53 . 2 451 45 LEU HD2 H 0.36 . 2 452 45 LEU CA C 57.37 . 1 453 45 LEU CB C 42.27 . 1 454 45 LEU CD1 C 25.47 . 2 455 45 LEU CD2 C 22.77 . 2 456 45 LEU N N 118.65 . 1 457 46 GLN H H 7.84 . 1 458 46 GLN HA H 4.03 . 1 459 46 GLN HB2 H 2.15 . 1 460 46 GLN HB3 H 2.15 . 1 461 46 GLN HG2 H 2.56 . 1 462 46 GLN HG3 H 2.56 . 1 463 46 GLN HE21 H 6.83 . 2 464 46 GLN HE22 H 6.78 . 2 465 46 GLN CA C 57.87 . 1 466 46 GLN CB C 28.27 . 1 467 46 GLN CG C 33.97 . 1 468 46 GLN N N 116.65 . 1 469 46 GLN NE2 N 107.90 . 1 470 47 ALA H H 7.60 . 1 471 47 ALA HA H 4.31 . 1 472 47 ALA HB H 1.67 . 1 473 47 ALA CA C 53.47 . 1 474 47 ALA CB C 19.17 . 1 475 47 ALA N N 120.45 . 1 476 48 GLY H H 7.58 . 1 477 48 GLY HA2 H 4.31 . 2 478 48 GLY HA3 H 4.08 . 2 479 48 GLY CA C 44.67 . 1 480 48 GLY N N 104.05 . 1 481 49 GLY H H 8.34 . 1 482 49 GLY HA2 H 3.94 . 2 483 49 GLY HA3 H 3.67 . 2 484 49 GLY CA C 45.37 . 1 485 49 GLY N N 103.85 . 1 486 50 TYR H H 8.07 . 1 487 50 TYR HA H 4.07 . 1 488 50 TYR HB2 H 3.05 . 2 489 50 TYR HB3 H 2.53 . 2 490 50 TYR HD1 H 6.93 . 1 491 50 TYR HD2 H 6.93 . 1 492 50 TYR HE1 H 6.69 . 1 493 50 TYR HE2 H 6.69 . 1 494 50 TYR CA C 60.77 . 1 495 50 TYR CB C 39.17 . 1 496 50 TYR N N 118.55 . 1 497 51 GLY H H 9.53 . 1 498 51 GLY HA2 H 4.51 . 2 499 51 GLY HA3 H 3.44 . 2 500 51 GLY CA C 44.47 . 1 501 51 GLY N N 107.05 . 1 502 52 PHE H H 7.55 . 1 503 52 PHE HA H 4.10 . 1 504 52 PHE HB2 H 2.01 . 1 505 52 PHE HB3 H 2.01 . 1 506 52 PHE HD1 H 6.89 . 1 507 52 PHE HD2 H 6.89 . 1 508 52 PHE HE1 H 6.87 . 1 509 52 PHE HE2 H 6.87 . 1 510 52 PHE HZ H 6.79 . 1 511 52 PHE CA C 58.17 . 1 512 52 PHE CB C 43.57 . 1 513 52 PHE CD1 C 132.17 . 1 514 52 PHE CD2 C 132.17 . 1 515 52 PHE CE1 C 130.17 . 1 516 52 PHE CE2 C 130.17 . 1 517 52 PHE CZ C 128.57 . 1 518 52 PHE N N 121.45 . 1 519 53 VAL H H 8.21 . 1 520 53 VAL HA H 5.13 . 1 521 53 VAL HB H 2.09 . 1 522 53 VAL HG1 H 0.83 . 2 523 53 VAL HG2 H 0.74 . 2 524 53 VAL CA C 61.27 . 1 525 53 VAL CB C 34.77 . 1 526 53 VAL CG1 C 22.47 . 2 527 53 VAL CG2 C 20.77 . 2 528 53 VAL N N 126.95 . 1 529 54 ILE H H 9.23 . 1 530 54 ILE HA H 5.10 . 1 531 54 ILE HB H 1.87 . 1 532 54 ILE HG12 H 2.01 . 2 533 54 ILE HG13 H 1.21 . 2 534 54 ILE HG2 H 0.91 . 1 535 54 ILE HD1 H 0.77 . 1 536 54 ILE CA C 60.57 . 1 537 54 ILE CB C 40.27 . 1 538 54 ILE CG1 C 27.97 . 1 539 54 ILE CG2 C 17.87 . 1 540 54 ILE CD1 C 14.17 . 1 541 54 ILE N N 128.05 . 1 542 55 SER H H 8.93 . 1 543 55 SER HA H 5.40 . 1 544 55 SER HB2 H 3.64 . 2 545 55 SER HB3 H 3.06 . 2 546 55 SER CA C 56.37 . 1 547 55 SER CB C 65.97 . 1 548 55 SER N N 118.75 . 1 549 56 ASP H H 8.44 . 1 550 56 ASP HA H 5.10 . 1 551 56 ASP HB2 H 3.26 . 2 552 56 ASP HB3 H 2.92 . 2 553 56 ASP CA C 54.67 . 1 554 56 ASP CB C 38.87 . 1 555 56 ASP N N 126.75 . 1 556 57 TRP HA H 4.21 . 1 557 57 TRP HB2 H 3.60 . 2 558 57 TRP HB3 H 3.51 . 2 559 57 TRP HD1 H 7.27 . 1 560 57 TRP HE1 H 10.30 . 1 561 57 TRP HE3 H 7.42 . 1 562 57 TRP HZ2 H 7.47 . 3 563 57 TRP HZ3 H 6.79 . 3 564 57 TRP HH2 H 7.28 . 1 565 57 TRP CA C 59.97 . 1 566 57 TRP CB C 30.77 . 1 567 57 TRP CD1 C 126.77 . 1 568 57 TRP CD2 C 126.77 . 1 569 57 TRP CE2 C 118.67 . 1 570 57 TRP CZ2 C 114.87 . 1 571 57 TRP CZ3 C 120.17 . 1 572 57 TRP CH2 C 124.37 . 1 573 57 TRP NE1 N 129.40 . 1 574 58 ASN H H 8.14 . 1 575 58 ASN HA H 5.12 . 1 576 58 ASN HB2 H 2.86 . 1 577 58 ASN HB3 H 2.86 . 1 578 58 ASN CA C 54.87 . 1 579 58 ASN N N 116.35 . 1 580 59 MET H H 7.36 . 1 581 59 MET HA H 4.80 . 1 582 59 MET HB2 H 2.20 . 2 583 59 MET HB3 H 2.07 . 2 584 59 MET CA C 53.97 . 1 585 59 MET CB C 34.47 . 1 586 59 MET N N 123.85 . 1 587 60 PRO HA H 4.42 . 1 588 60 PRO HB2 H 1.94 . 1 589 60 PRO HB3 H 1.94 . 1 590 60 PRO HG2 H 2.14 . 1 591 60 PRO HG3 H 2.14 . 1 592 60 PRO HD2 H 3.80 . 2 593 60 PRO HD3 H 3.64 . 2 594 60 PRO CA C 62.27 . 1 595 60 PRO CB C 32.87 . 1 596 60 PRO CG C 26.97 . 1 597 60 PRO CD C 50.37 . 1 598 61 ASN H H 8.62 . 1 599 61 ASN HA H 4.05 . 1 600 61 ASN HB2 H 3.28 . 2 601 61 ASN HB3 H 2.65 . 2 602 61 ASN HD21 H 7.91 . 2 603 61 ASN HD22 H 7.02 . 2 604 61 ASN CA C 59.17 . 1 605 61 ASN CB C 37.67 . 1 606 61 ASN N N 111.95 . 1 607 61 ASN ND2 N 115.10 . 1 608 62 MET H H 9.27 . 1 609 62 MET HA H 4.21 . 1 610 62 MET HB2 H 2.19 . 1 611 62 MET HB3 H 2.19 . 1 612 62 MET HE H 2.41 . 1 613 62 MET CA C 57.07 . 1 614 62 MET CB C 35.67 . 1 615 62 MET CG C 31.17 . 1 616 62 MET N N 123.05 . 1 617 63 ASP H H 8.60 . 1 618 63 ASP HA H 4.49 . 1 619 63 ASP HB2 H 3.72 . 2 620 63 ASP HB3 H 2.92 . 2 621 63 ASP CA C 53.17 . 1 622 63 ASP CB C 40.67 . 1 623 63 ASP N N 127.15 . 1 624 64 GLY H H 8.63 . 1 625 64 GLY HA2 H 3.99 . 2 626 64 GLY HA3 H 3.48 . 2 627 64 GLY CA C 47.37 . 1 628 64 GLY N N 103.45 . 1 629 65 LEU H H 7.56 . 1 630 65 LEU HA H 3.74 . 1 631 65 LEU HB2 H 1.49 . 2 632 65 LEU HB3 H 0.86 . 2 633 65 LEU HG H 1.16 . 1 634 65 LEU HD1 H 0.73 . 1 635 65 LEU HD2 H 0.73 . 1 636 65 LEU CA C 57.07 . 1 637 65 LEU CB C 40.67 . 1 638 65 LEU CG C 26.97 . 1 639 65 LEU CD1 C 24.47 . 1 640 65 LEU CD2 C 24.47 . 1 641 65 LEU N N 121.85 . 1 642 66 GLU H H 8.19 . 1 643 66 GLU HA H 3.84 . 1 644 66 GLU HB2 H 1.97 . 2 645 66 GLU HB3 H 1.86 . 2 646 66 GLU HG2 H 2.31 . 1 647 66 GLU HG3 H 2.31 . 1 648 66 GLU CA C 59.07 . 1 649 66 GLU CB C 29.07 . 1 650 66 GLU CG C 36.17 . 1 651 66 GLU N N 119.85 . 1 652 67 LEU H H 8.32 . 1 653 67 LEU HA H 4.09 . 1 654 67 LEU HB2 H 2.07 . 2 655 67 LEU HB3 H 1.15 . 2 656 67 LEU HG H 1.35 . 1 657 67 LEU HD1 H 0.78 . 2 658 67 LEU HD2 H 0.90 . 2 659 67 LEU CA C 58.77 . 1 660 67 LEU CB C 41.17 . 1 661 67 LEU CG C 26.87 . 1 662 67 LEU CD1 C 26.07 . 2 663 67 LEU CD2 C 22.57 . 2 664 67 LEU N N 123.75 . 1 665 68 LEU H H 8.20 . 1 666 68 LEU HA H 3.78 . 1 667 68 LEU HB2 H 2.11 . 2 668 68 LEU HB3 H 1.60 . 2 669 68 LEU HD1 H 0.83 . 2 670 68 LEU HD2 H 0.65 . 2 671 68 LEU CA C 58.47 . 1 672 68 LEU CB C 41.17 . 1 673 68 LEU CD1 C 27.67 . 2 674 68 LEU CD2 C 22.37 . 2 675 68 LEU N N 120.75 . 1 676 69 LYS H H 8.36 . 1 677 69 LYS HA H 3.80 . 1 678 69 LYS HB2 H 1.86 . 2 679 69 LYS HB3 H 1.77 . 2 680 69 LYS HG2 H 1.41 . 1 681 69 LYS HG3 H 1.41 . 1 682 69 LYS HD2 H 1.67 . 1 683 69 LYS HD3 H 1.67 . 1 684 69 LYS HE2 H 2.96 . 1 685 69 LYS HE3 H 2.96 . 1 686 69 LYS CA C 59.97 . 1 687 69 LYS CB C 32.17 . 1 688 69 LYS CG C 24.67 . 1 689 69 LYS CD C 29.17 . 1 690 69 LYS CE C 41.87 . 1 691 69 LYS N N 116.05 . 1 692 70 THR H H 8.00 . 1 693 70 THR HA H 3.81 . 1 694 70 THR HB H 4.35 . 1 695 70 THR HG2 H 1.20 . 1 696 70 THR CA C 67.27 . 1 697 70 THR CB C 68.27 . 1 698 70 THR CG2 C 22.37 . 1 699 70 THR N N 117.35 . 1 700 71 ILE H H 8.45 . 1 701 71 ILE HA H 3.39 . 1 702 71 ILE HB H 1.88 . 1 703 71 ILE HG12 H 1.68 . 2 704 71 ILE HG13 H 0.81 . 2 705 71 ILE HG2 H 0.74 . 1 706 71 ILE HD1 H 0.56 . 1 707 71 ILE CA C 65.87 . 1 708 71 ILE CB C 38.77 . 1 709 71 ILE CG1 C 29.47 . 1 710 71 ILE CG2 C 17.27 . 1 711 71 ILE CD1 C 14.67 . 1 712 71 ILE N N 123.55 . 1 713 72 ARG H H 8.12 . 1 714 72 ARG HA H 4.01 . 1 715 72 ARG HB2 H 1.98 . 2 716 72 ARG HB3 H 1.64 . 2 717 72 ARG CA C 57.17 . 1 718 72 ARG CB C 29.17 . 1 719 72 ARG N N 113.35 . 1 720 73 ALA H H 7.28 . 1 721 73 ALA HA H 4.34 . 1 722 73 ALA HB H 1.42 . 1 723 73 ALA CA C 51.87 . 1 724 73 ALA CB C 19.27 . 1 725 73 ALA N N 118.95 . 1 726 74 ASP H H 7.40 . 1 727 74 ASP HA H 4.58 . 1 728 74 ASP HB2 H 2.90 . 1 729 74 ASP HB3 H 2.60 . 1 730 74 ASP CA C 53.97 . 1 731 74 ASP CB C 43.97 . 1 732 74 ASP N N 121.75 . 1 733 75 GLY H H 8.74 . 1 734 75 GLY HA2 H 3.90 . 1 735 75 GLY HA3 H 3.90 . 1 736 75 GLY CA C 47.37 . 1 737 75 GLY N N 112.45 . 1 738 76 ALA H H 8.57 . 1 739 76 ALA HA H 4.50 . 1 740 76 ALA HB H 1.49 . 1 741 76 ALA CA C 53.47 . 1 742 76 ALA CB C 19.57 . 1 743 76 ALA N N 121.85 . 1 744 77 MET H H 8.48 . 1 745 77 MET HA H 4.59 . 1 746 77 MET HB2 H 2.23 . 2 747 77 MET HB3 H 2.13 . 2 748 77 MET HG2 H 2.62 . 2 749 77 MET HG3 H 2.39 . 2 750 77 MET CA C 55.97 . 1 751 77 MET CB C 34.37 . 1 752 77 MET CG C 34.17 . 1 753 77 MET N N 116.05 . 1 754 78 SER H H 7.45 . 1 755 78 SER HA H 4.38 . 1 756 78 SER HB2 H 4.07 . 2 757 78 SER HB3 H 3.98 . 2 758 78 SER CA C 61.97 . 1 759 78 SER CB C 63.47 . 1 760 78 SER N N 112.65 . 1 761 79 ALA H H 8.20 . 1 762 79 ALA HA H 4.45 . 1 763 79 ALA HB H 1.33 . 1 764 79 ALA CA C 51.07 . 1 765 79 ALA CB C 18.87 . 1 766 79 ALA N N 123.15 . 1 767 80 LEU H H 7.83 . 1 768 80 LEU HA H 4.16 . 1 769 80 LEU HB2 H 1.54 . 2 770 80 LEU HB3 H 1.29 . 2 771 80 LEU HG H 1.54 . 1 772 80 LEU HD1 H 0.71 . 1 773 80 LEU HD2 H 0.71 . 1 774 80 LEU CA C 53.77 . 1 775 80 LEU CB C 42.97 . 1 776 80 LEU CG C 26.67 . 1 777 80 LEU CD1 C 25.17 . 1 778 80 LEU CD2 C 25.17 . 1 779 80 LEU N N 123.95 . 1 780 81 PRO HA H 4.01 . 1 781 81 PRO HB2 H 1.39 . 2 782 81 PRO HB3 H 0.42 . 2 783 81 PRO HG2 H 1.86 . 2 784 81 PRO HG3 H 1.68 . 2 785 81 PRO HD2 H 3.88 . 2 786 81 PRO HD3 H 3.56 . 2 787 81 PRO CA C 62.47 . 1 788 81 PRO CB C 31.57 . 1 789 81 PRO CG C 27.97 . 1 790 81 PRO CD C 51.27 . 1 791 82 VAL H H 7.68 . 1 792 82 VAL HA H 4.79 . 1 793 82 VAL HB H 1.68 . 1 794 82 VAL HG1 H 0.68 . 1 795 82 VAL HG2 H 0.68 . 1 796 82 VAL CA C 60.37 . 1 797 82 VAL CB C 36.07 . 1 798 82 VAL CG1 C 20.67 . 1 799 82 VAL CG2 C 20.67 . 1 800 82 VAL N N 118.85 . 1 801 83 LEU H H 9.10 . 1 802 83 LEU HA H 4.55 . 1 803 83 LEU HB2 H 2.11 . 2 804 83 LEU HB3 H 1.15 . 2 805 83 LEU HG H 1.31 . 1 806 83 LEU HD1 H 0.51 . 1 807 83 LEU HD2 H 0.51 . 1 808 83 LEU CA C 52.67 . 1 809 83 LEU CB C 45.57 . 1 810 83 LEU CG C 26.87 . 1 811 83 LEU CD1 C 25.97 . 1 812 83 LEU CD2 C 25.97 . 1 813 83 LEU N N 130.35 . 1 814 84 MET H H 8.09 . 1 815 84 MET HA H 5.53 . 1 816 84 MET HB2 H 2.14 . 2 817 84 MET HB3 H 2.06 . 2 818 84 MET HG2 H 2.45 . 1 819 84 MET HG3 H 2.45 . 1 820 84 MET CA C 52.87 . 1 821 84 MET CB C 32.07 . 1 822 84 MET CG C 32.07 . 1 823 84 MET N N 124.75 . 1 824 85 VAL H H 9.11 . 1 825 85 VAL HA H 4.99 . 1 826 85 VAL HB H 2.14 . 1 827 85 VAL HG1 H 1.11 . 2 828 85 VAL HG2 H 0.82 . 2 829 85 VAL CA C 61.07 . 1 830 85 VAL CB C 33.17 . 1 831 85 VAL CG1 C 22.87 . 2 832 85 VAL CG2 C 20.47 . 2 833 85 VAL N N 123.75 . 1 834 86 THR H H 8.50 . 1 835 86 THR HA H 5.10 . 1 836 86 THR HB H 4.07 . 1 837 86 THR HG2 H 0.92 . 1 838 86 THR CA C 58.77 . 1 839 86 THR CB C 70.57 . 1 840 86 THR CG2 C 19.57 . 1 841 86 THR N N 116.55 . 1 842 87 ALA H H 8.81 . 1 843 87 ALA HA H 4.63 . 1 844 87 ALA HB H 1.53 . 1 845 87 ALA CA C 52.67 . 1 846 87 ALA CB C 19.87 . 1 847 87 ALA N N 126.15 . 1 848 88 GLU H H 7.97 . 1 849 88 GLU HA H 4.32 . 1 850 88 GLU HB2 H 1.90 . 1 851 88 GLU HB3 H 1.90 . 1 852 88 GLU HG2 H 2.10 . 1 853 88 GLU HG3 H 2.10 . 1 854 88 GLU CA C 56.17 . 1 855 88 GLU CB C 29.37 . 1 856 88 GLU N N 116.65 . 1 857 89 ALA HA H 4.21 . 1 858 89 ALA HB H 1.28 . 1 859 89 ALA CA C 51.47 . 1 860 89 ALA CB C 17.57 . 1 861 90 LYS H H 7.38 . 1 862 90 LYS HA H 4.40 . 1 863 90 LYS HB2 H 1.78 . 2 864 90 LYS HB3 H 1.55 . 2 865 90 LYS HG2 H 1.30 . 1 866 90 LYS HG3 H 1.30 . 1 867 90 LYS HD2 H 1.60 . 1 868 90 LYS HD3 H 1.60 . 1 869 90 LYS HE2 H 2.90 . 1 870 90 LYS HE3 H 2.90 . 1 871 90 LYS CA C 55.27 . 1 872 90 LYS CB C 33.17 . 1 873 90 LYS CG C 24.97 . 1 874 90 LYS CD C 29.07 . 1 875 90 LYS CE C 41.87 . 1 876 90 LYS N N 121.15 . 1 877 91 LYS HA H 3.76 . 1 878 91 LYS HB2 H 1.87 . 2 879 91 LYS HB3 H 1.77 . 2 880 91 LYS HG2 H 1.40 . 1 881 91 LYS HG3 H 1.40 . 1 882 91 LYS HD2 H 1.66 . 1 883 91 LYS HD3 H 1.66 . 1 884 91 LYS HE2 H 2.92 . 1 885 91 LYS HE3 H 2.92 . 1 886 91 LYS CA C 59.97 . 1 887 91 LYS CB C 32.07 . 1 888 91 LYS CG C 24.67 . 1 889 91 LYS CD C 29.17 . 1 890 91 LYS CE C 41.97 . 1 891 92 GLU H H 9.59 . 1 892 92 GLU HA H 3.95 . 1 893 92 GLU HB2 H 1.93 . 1 894 92 GLU HB3 H 1.93 . 1 895 92 GLU HG2 H 2.27 . 1 896 92 GLU HG3 H 2.27 . 1 897 92 GLU CA C 59.97 . 1 898 92 GLU CB C 28.67 . 1 899 92 GLU CG C 36.47 . 1 900 92 GLU N N 116.25 . 1 901 93 ASN H H 7.23 . 1 902 93 ASN HA H 4.56 . 1 903 93 ASN HB2 H 2.56 . 2 904 93 ASN HB3 H 2.05 . 2 905 93 ASN HD21 H 7.30 . 2 906 93 ASN HD22 H 6.85 . 2 907 93 ASN CA C 54.87 . 1 908 93 ASN CB C 37.07 . 1 909 93 ASN N N 118.05 . 1 910 93 ASN ND2 N 109.40 . 1 911 94 ILE H H 7.44 . 1 912 94 ILE HA H 3.17 . 1 913 94 ILE HB H 1.67 . 1 914 94 ILE HG12 H 1.00 . 2 915 94 ILE HG13 H 0.26 . 2 916 94 ILE HG2 H 0.55 . 1 917 94 ILE HD1 H 0.38 . 1 918 94 ILE CA C 64.97 . 1 919 94 ILE CB C 37.47 . 1 920 94 ILE CG1 C 27.97 . 1 921 94 ILE CG2 C 16.87 . 1 922 94 ILE CD1 C 12.47 . 1 923 94 ILE N N 121.65 . 1 924 95 ILE H H 7.96 . 1 925 95 ILE HA H 3.79 . 1 926 95 ILE HB H 1.67 . 1 927 95 ILE HG12 H 1.59 . 2 928 95 ILE HG13 H 1.17 . 2 929 95 ILE HG2 H 0.90 . 1 930 95 ILE HD1 H 0.81 . 1 931 95 ILE CA C 64.47 . 1 932 95 ILE CB C 37.77 . 1 933 95 ILE CG1 C 28.77 . 1 934 95 ILE CG2 C 16.97 . 1 935 95 ILE CD1 C 12.97 . 1 936 95 ILE N N 119.65 . 1 937 96 ALA H H 7.64 . 1 938 96 ALA HA H 4.21 . 1 939 96 ALA HB H 1.72 . 1 940 96 ALA CA C 55.17 . 1 941 96 ALA CB C 18.27 . 1 942 96 ALA N N 121.85 . 1 943 97 ALA H H 8.46 . 1 944 97 ALA HA H 3.92 . 1 945 97 ALA HB H 1.53 . 1 946 97 ALA CA C 54.97 . 1 947 97 ALA CB C 17.07 . 1 948 97 ALA N N 119.25 . 1 949 98 ALA H H 8.16 . 1 950 98 ALA HA H 4.21 . 1 951 98 ALA HB H 1.59 . 1 952 98 ALA CA C 55.47 . 1 953 98 ALA CB C 17.87 . 1 954 98 ALA N N 121.85 . 1 955 99 GLN H H 8.70 . 1 956 99 GLN HA H 4.04 . 1 957 99 GLN HB2 H 2.19 . 2 958 99 GLN HB3 H 2.10 . 2 959 99 GLN HG2 H 2.63 . 2 960 99 GLN HG3 H 2.44 . 2 961 99 GLN HE21 H 7.36 . 2 962 99 GLN HE22 H 6.77 . 2 963 99 GLN CA C 58.67 . 1 964 99 GLN CB C 28.27 . 1 965 99 GLN CG C 34.37 . 1 966 99 GLN N N 118.85 . 1 967 99 GLN NE2 N 109.80 . 1 968 100 ALA H H 7.56 . 1 969 100 ALA HA H 4.35 . 1 970 100 ALA HB H 1.43 . 1 971 100 ALA CA C 51.87 . 1 972 100 ALA CB C 19.27 . 1 973 100 ALA N N 118.35 . 1 974 101 GLY H H 7.59 . 1 975 101 GLY HA2 H 4.22 . 2 976 101 GLY HA3 H 3.89 . 2 977 101 GLY CA C 45.77 . 1 978 101 GLY N N 102.45 . 1 979 102 ALA H H 8.72 . 1 980 102 ALA HA H 3.94 . 1 981 102 ALA HB H 1.37 . 1 982 102 ALA CA C 53.67 . 1 983 102 ALA CB C 18.57 . 1 984 102 ALA N N 124.95 . 1 985 103 SER H H 9.04 . 1 986 103 SER HA H 4.42 . 1 987 103 SER HB2 H 3.98 . 2 988 103 SER HB3 H 3.27 . 2 989 103 SER CA C 60.17 . 1 990 103 SER CB C 61.17 . 1 991 103 SER N N 117.95 . 1 992 104 GLY H H 7.64 . 1 993 104 GLY HA2 H 4.14 . 2 994 104 GLY HA3 H 3.85 . 2 995 104 GLY CA C 44.87 . 1 996 104 GLY N N 102.65 . 1 997 105 TYR H H 8.44 . 1 998 105 TYR HA H 5.88 . 1 999 105 TYR HB2 H 2.81 . 1 1000 105 TYR HB3 H 2.81 . 1 1001 105 TYR HD1 H 6.78 . 1 1002 105 TYR HD2 H 6.78 . 1 1003 105 TYR HE1 H 6.60 . 1 1004 105 TYR HE2 H 6.60 . 1 1005 105 TYR CA C 56.17 . 1 1006 105 TYR CB C 41.47 . 1 1007 105 TYR CD1 C 133.17 . 1 1008 105 TYR CD2 C 133.17 . 1 1009 105 TYR CE1 C 117.47 . 1 1010 105 TYR CE2 C 117.47 . 1 1011 105 TYR N N 119.25 . 1 1012 106 VAL H H 8.95 . 1 1013 106 VAL HA H 4.29 . 1 1014 106 VAL HB H 1.49 . 1 1015 106 VAL HG1 H 0.48 . 2 1016 106 VAL HG2 H 0.40 . 2 1017 106 VAL CA C 59.57 . 1 1018 106 VAL CB C 35.37 . 1 1019 106 VAL CG1 C 21.77 . 2 1020 106 VAL CG2 C 20.77 . 2 1021 106 VAL N N 120.25 . 1 1022 107 VAL H H 8.11 . 1 1023 107 VAL HA H 4.99 . 1 1024 107 VAL HB H 1.86 . 1 1025 107 VAL HG1 H 0.82 . 1 1026 107 VAL HG2 H 0.82 . 1 1027 107 VAL CA C 60.57 . 1 1028 107 VAL CB C 36.47 . 1 1029 107 VAL CG1 C 22.77 . 1 1030 107 VAL CG2 C 22.77 . 1 1031 107 VAL N N 126.45 . 1 1032 108 LYS H H 8.45 . 1 1033 108 LYS HA H 4.64 . 1 1034 108 LYS HB2 H 1.72 . 1 1035 108 LYS HB3 H 1.72 . 1 1036 108 LYS HG2 H 1.33 . 1 1037 108 LYS HG3 H 1.33 . 1 1038 108 LYS HD2 H 1.62 . 1 1039 108 LYS HD3 H 1.62 . 1 1040 108 LYS HE2 H 2.93 . 1 1041 108 LYS HE3 H 2.93 . 1 1042 108 LYS CA C 53.57 . 1 1043 108 LYS CB C 33.07 . 1 1044 108 LYS CG C 24.57 . 1 1045 108 LYS CD C 29.57 . 1 1046 108 LYS CE C 41.37 . 1 1047 108 LYS N N 123.85 . 1 1048 109 PRO HA H 4.39 . 1 1049 109 PRO HB2 H 2.27 . 2 1050 109 PRO HB3 H 1.99 . 2 1051 109 PRO HG2 H 1.93 . 1 1052 109 PRO HG3 H 1.93 . 1 1053 109 PRO HD2 H 3.67 . 2 1054 109 PRO HD3 H 3.48 . 2 1055 109 PRO CA C 62.37 . 1 1056 109 PRO CB C 34.57 . 1 1057 109 PRO CG C 24.57 . 1 1058 109 PRO CD C 50.17 . 1 1059 110 PHE H H 7.75 . 1 1060 110 PHE HA H 5.50 . 1 1061 110 PHE HB2 H 3.39 . 2 1062 110 PHE HB3 H 2.99 . 2 1063 110 PHE HD1 H 7.09 . 1 1064 110 PHE HD2 H 7.09 . 1 1065 110 PHE HE1 H 7.08 . 1 1066 110 PHE HE2 H 7.08 . 1 1067 110 PHE HZ H 7.00 . 1 1068 110 PHE CA C 53.77 . 1 1069 110 PHE CB C 40.77 . 1 1070 110 PHE CD1 C 133.17 . 1 1071 110 PHE CD2 C 133.17 . 1 1072 110 PHE CE1 C 130.47 . 1 1073 110 PHE CE2 C 130.47 . 1 1074 110 PHE CZ C 128.07 . 1 1075 110 PHE N N 115.85 . 1 1076 111 THR H H 7.86 . 1 1077 111 THR HA H 4.54 . 1 1078 111 THR HB H 4.80 . 1 1079 111 THR HG2 H 1.34 . 1 1080 111 THR CA C 59.47 . 1 1081 111 THR CB C 71.87 . 1 1082 111 THR CG2 C 21.77 . 1 1083 111 THR N N 108.65 . 1 1084 112 ALA H H 9.20 . 1 1085 112 ALA HA H 3.97 . 1 1086 112 ALA HB H 1.50 . 1 1087 112 ALA CA C 55.97 . 1 1088 112 ALA CB C 17.27 . 1 1089 112 ALA N N 123.05 . 1 1090 113 ALA H H 8.21 . 1 1091 113 ALA HA H 4.25 . 1 1092 113 ALA HB H 1.47 . 1 1093 113 ALA CA C 55.07 . 1 1094 113 ALA CB C 18.17 . 1 1095 113 ALA N N 118.45 . 1 1096 114 THR H H 7.81 . 1 1097 114 THR HA H 4.06 . 1 1098 114 THR HB H 4.30 . 1 1099 114 THR HG2 H 1.22 . 1 1100 114 THR CA C 65.97 . 1 1101 114 THR CB C 68.47 . 1 1102 114 THR CG2 C 22.47 . 1 1103 114 THR N N 116.85 . 1 1104 115 LEU H H 8.24 . 1 1105 115 LEU HA H 3.65 . 1 1106 115 LEU HB2 H 2.07 . 2 1107 115 LEU HB3 H 1.43 . 2 1108 115 LEU HG H 1.33 . 1 1109 115 LEU HD1 H 0.74 . 2 1110 115 LEU HD2 H 0.45 . 2 1111 115 LEU CA C 58.27 . 1 1112 115 LEU CB C 41.07 . 1 1113 115 LEU CG C 26.87 . 1 1114 115 LEU CD2 C 21.37 . 1 1115 115 LEU N N 122.05 . 1 1116 116 GLU H H 8.89 . 1 1117 116 GLU HA H 3.64 . 1 1118 116 GLU HB2 H 2.25 . 1 1119 116 GLU HB3 H 2.25 . 1 1120 116 GLU HG2 H 2.41 . 1 1121 116 GLU HG3 H 2.21 . 2 1122 116 GLU CA C 60.07 . 1 1123 116 GLU CB C 29.77 . 1 1124 116 GLU CG C 35.67 . 1 1125 116 GLU N N 119.05 . 1 1126 117 GLU H H 7.66 . 1 1127 117 GLU HA H 4.07 . 1 1128 117 GLU HB2 H 2.20 . 1 1129 117 GLU HB3 H 2.20 . 1 1130 117 GLU HG2 H 2.46 . 1 1131 117 GLU HG3 H 2.46 . 1 1132 117 GLU CA C 59.57 . 1 1133 117 GLU CB C 29.47 . 1 1134 117 GLU CG C 36.17 . 1 1135 117 GLU N N 117.95 . 1 1136 118 LYS H H 7.84 . 1 1137 118 LYS HA H 3.95 . 1 1138 118 LYS HB2 H 1.92 . 2 1139 118 LYS HB3 H 1.42 . 2 1140 118 LYS HG2 H 1.09 . 1 1141 118 LYS HG3 H 1.09 . 1 1142 118 LYS HD2 H 1.61 . 1 1143 118 LYS HD3 H 1.61 . 1 1144 118 LYS HE2 H 2.87 . 1 1145 118 LYS HE3 H 2.87 . 1 1146 118 LYS CA C 57.67 . 1 1147 118 LYS CB C 31.67 . 1 1148 118 LYS CG C 24.67 . 1 1149 118 LYS CD C 27.67 . 1 1150 118 LYS CE C 41.77 . 1 1151 118 LYS N N 116.95 . 1 1152 119 LEU H H 8.55 . 1 1153 119 LEU HA H 3.41 . 1 1154 119 LEU HB2 H 1.64 . 2 1155 119 LEU HB3 H 0.83 . 2 1156 119 LEU HG H 1.45 . 1 1157 119 LEU HD1 H 0.38 . 2 1158 119 LEU HD2 H 0.08 . 2 1159 119 LEU CA C 57.97 . 1 1160 119 LEU CB C 40.57 . 1 1161 119 LEU CG C 26.27 . 1 1162 119 LEU CD1 C 25.87 . 1 1163 119 LEU CD2 C 25.87 . 1 1164 119 LEU N N 118.15 . 1 1165 120 ASN H H 8.58 . 1 1166 120 ASN HA H 4.56 . 1 1167 120 ASN HB2 H 3.03 . 2 1168 120 ASN HB3 H 2.86 . 2 1169 120 ASN HD21 H 7.53 . 2 1170 120 ASN HD22 H 6.86 . 2 1171 120 ASN CA C 56.17 . 1 1172 120 ASN CB C 37.47 . 1 1173 120 ASN N N 115.85 . 1 1174 120 ASN ND2 N 110.10 . 1 1175 121 LYS H H 7.78 . 1 1176 121 LYS HA H 4.15 . 1 1177 121 LYS HB2 H 1.95 . 1 1178 121 LYS HB3 H 1.95 . 1 1179 121 LYS HD2 H 1.60 . 1 1180 121 LYS HD3 H 1.60 . 1 1181 121 LYS HE2 H 2.97 . 1 1182 121 LYS HE3 H 2.97 . 1 1183 121 LYS CA C 58.87 . 1 1184 121 LYS CB C 32.17 . 1 1185 121 LYS CG C 25.27 . 1 1186 121 LYS CD C 28.47 . 1 1187 121 LYS CE C 41.97 . 1 1188 121 LYS N N 119.25 . 1 1189 122 ILE H H 7.51 . 1 1190 122 ILE HA H 3.73 . 1 1191 122 ILE HB H 1.89 . 1 1192 122 ILE HG12 H 1.87 . 2 1193 122 ILE HG13 H 0.86 . 2 1194 122 ILE HG2 H 0.91 . 1 1195 122 ILE HD1 H 0.68 . 1 1196 122 ILE CA C 65.57 . 1 1197 122 ILE CB C 37.87 . 1 1198 122 ILE CG1 C 29.97 . 1 1199 122 ILE CG2 C 17.97 . 1 1200 122 ILE CD1 C 15.37 . 1 1201 122 ILE N N 121.85 . 1 1202 123 PHE H H 9.14 . 1 1203 123 PHE HA H 4.67 . 1 1204 123 PHE HB2 H 3.48 . 2 1205 123 PHE HB3 H 3.33 . 2 1206 123 PHE HD1 H 7.48 . 1 1207 123 PHE HD2 H 7.48 . 1 1208 123 PHE HE1 H 7.26 . 1 1209 123 PHE HE2 H 7.26 . 1 1210 123 PHE HZ H 6.69 . 1 1211 123 PHE CA C 58.87 . 1 1212 123 PHE CB C 37.37 . 1 1213 123 PHE CD1 C 130.97 . 1 1214 123 PHE CD2 C 130.97 . 1 1215 123 PHE CE1 C 130.97 . 1 1216 123 PHE CE2 C 130.97 . 1 1217 123 PHE CZ C 128.57 . 1 1218 123 PHE N N 118.65 . 1 1219 124 GLU H H 8.32 . 1 1220 124 GLU HA H 4.24 . 1 1221 124 GLU HB2 H 2.27 . 2 1222 124 GLU HB3 H 2.20 . 2 1223 124 GLU HG2 H 2.46 . 1 1224 124 GLU HG3 H 2.46 . 1 1225 124 GLU CA C 59.37 . 1 1226 124 GLU CB C 29.97 . 1 1227 124 GLU CG C 36.17 . 1 1228 124 GLU N N 117.85 . 1 1229 125 LYS H H 7.75 . 1 1230 125 LYS HA H 4.18 . 1 1231 125 LYS HB2 H 2.07 . 2 1232 125 LYS HB3 H 1.91 . 2 1233 125 LYS HG2 H 1.65 . 1 1234 125 LYS HG3 H 1.65 . 1 1235 125 LYS HD2 H 1.74 . 1 1236 125 LYS HD3 H 1.74 . 1 1237 125 LYS HE2 H 3.03 . 1 1238 125 LYS HE3 H 3.03 . 1 1239 125 LYS CA C 58.57 . 1 1240 125 LYS CB C 32.37 . 1 1241 125 LYS CG C 25.17 . 1 1242 125 LYS CD C 28.77 . 1 1243 125 LYS CE C 41.97 . 1 1244 125 LYS N N 120.05 . 1 1245 126 LEU H H 7.96 . 1 1246 126 LEU HA H 4.42 . 1 1247 126 LEU HB2 H 1.83 . 2 1248 126 LEU HB3 H 1.76 . 2 1249 126 LEU HG H 1.93 . 1 1250 126 LEU HD1 H 0.93 . 1 1251 126 LEU HD2 H 0.93 . 1 1252 126 LEU CA C 54.77 . 1 1253 126 LEU CB C 42.67 . 1 1254 126 LEU CG C 27.17 . 1 1255 126 LEU CD1 C 22.17 . 1 1256 126 LEU CD2 C 22.17 . 1 1257 126 LEU N N 116.45 . 1 1258 127 GLY H H 7.97 . 1 1259 127 GLY HA2 H 4.01 . 1 1260 127 GLY HA3 H 4.01 . 1 1261 127 GLY CA C 46.67 . 1 1262 127 GLY N N 110.15 . 1 1263 128 MET H H 8.25 . 1 1264 128 MET HA H 4.21 . 1 1265 128 MET HB2 H 2.18 . 2 1266 128 MET HB3 H 1.85 . 2 1267 128 MET HG2 H 2.60 . 2 1268 128 MET HG3 H 2.44 . 2 1269 128 MET CA C 57.17 . 1 1270 128 MET CB C 35.67 . 1 1271 128 MET CG C 32.57 . 1 1272 128 MET N N 124.45 . 1 stop_ save_