data_6336 #Corrected using PDB structure: 1XSCA # #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 # 11 C HA 5.53 4.75 # 31 F HA 5.41 6.30 # 32 L HA 4.35 3.31 # 57 L HA 3.49 2.69 #102 E HA 3.62 4.85 # #After reference correction, the following residues still #have a CB chemical shift difference (obs*-pred) greater than 5.0ppm: #NUM AA CS Observed* Predicted # 44 T CB 66.64 72.09 #136 M CB 37.64 32.16 #152 A CB 20.14 26.30 # #After reference correction, the following residues still #have a N chemical shift difference (obs*-pred) greater than 10.0ppm: #NUM AA CS Observed* Predicted # 89 A N 107.50 132.18 #132 Q N 110.20 122.73 # #The average CS difference between predicted and observed: #HA CA CB CO N HN #0.06 -0.21 -0.06 -0.21 -0.40 -0.00 # #bmr6336.str.corr chemical shifts have been re-referenced with the following #offsets (these values have been added to the original bmr6336.str file): #HA CA CB CO N HN #N/A -0.14 -0.14 -0.21 -0.40 N/A # #The 95% confidence intervals for the above recommended offsets are: # HA CA CB CO N HN #+/-0.03 +/-0.15 +/-0.15 +/-0.13 +/-0.36 +/-0.05 # #The Correlation Coefficients between predicted and observed #chemical shifts are: #HA CA CB CO N HN #0.798 0.955 0.989 0.811 0.729 0.556 # #The RMSD between predicted and observed* (reference #corrected) chemical shifts are: #HA CA CB CO N HN #0.168 0.929 0.880 0.790 2.156 0.332 # ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Assignment of human AP4A hydrolase in complex with ATP ; loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Swarbrick James D. . stop_ _BMRB_accession_number 6336 _BMRB_flat_file_name bmr6336.str _Entry_type new _Submission_date 2004-10-05 _Accession_date 2004-10-05 _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' 899 '15N chemical shifts' 157 '13C chemical shifts' 652 stop_ loop_ _Related_BMRB_accession_number _Relationship 6330 "assignment of apo AP4A hydrolase monomer" stop_ save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_title ; Letter to the Editor: 1H, 13C, and 15N resonance assignments of the 17 kDa Ap4A hydrolase from Homo sapiens in the presence and absence of ATP ; _Citation_status published _Citation_type journal _PubMed_ID . loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Swarbrick James D. . 2 Buyya S. . . 3 Gunawardana D. . . 4 Fletcher Jamie L. . 5 Branson Kim . . 6 Smith Brian . . 7 Pepe Salvatore . . 8 McLennan A. G. . 9 Gayler K. R. . 10 Gooley Paul R. . stop_ _Journal_abbreviation "J. Biomol. NMR" _Journal_volume 31 _Journal_issue 2 _Page_first 181 _Page_last 182 _Year 2005 loop_ _Keyword "NMR nudix assignment AP4A" stop_ save_ ################################## # Molecular system description # ################################## save_molecular_system_AP4A _Saveframe_category molecular_system _Mol_system_name "AP4A hydrolase with ATP" _Abbreviation_common "AP4A hydrolase with ATP" _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label "AP4A hydrolase monomer" $AP4A_hydrolase ATP $ATP stop_ _System_molecular_weight 17280.85 _System_physical_state native _System_oligomer_state monomer _System_paramagnetic no _System_thiol_state "all free" save_ ######################## # Monomeric polymers # ######################## save_AP4A_hydrolase _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common AP4A _Name_variant . _Abbreviation_common AP4A _Mol_thiol_state "all free" ############################## # Polymer residue sequence # ############################## _Residue_count 153 _Mol_residue_sequence ; GPLGSMALRACGLIIFRRCL IPKVDNNAIEFLLLQASDGI HHWTPPKGHVEPGEDDLETA LRATQEEAGIEAGQLTIIEG FKRELNYVARNKPKTVIYWL AEVKDYDVEIRLSHEHQAYR WLGLEEACQLAQFKEMKAAL QEGHQFLCSIEAL ; loop_ _Residue_seq_code _Residue_label 1 GLY 2 PRO 3 LEU 4 GLY 5 SER 6 MET 7 ALA 8 LEU 9 ARG 10 ALA 11 CYS 12 GLY 13 LEU 14 ILE 15 ILE 16 PHE 17 ARG 18 ARG 19 CYS 20 LEU 21 ILE 22 PRO 23 LYS 24 VAL 25 ASP 26 ASN 27 ASN 28 ALA 29 ILE 30 GLU 31 PHE 32 LEU 33 LEU 34 LEU 35 GLN 36 ALA 37 SER 38 ASP 39 GLY 40 ILE 41 HIS 42 HIS 43 TRP 44 THR 45 PRO 46 PRO 47 LYS 48 GLY 49 HIS 50 VAL 51 GLU 52 PRO 53 GLY 54 GLU 55 ASP 56 ASP 57 LEU 58 GLU 59 THR 60 ALA 61 LEU 62 ARG 63 ALA 64 THR 65 GLN 66 GLU 67 GLU 68 ALA 69 GLY 70 ILE 71 GLU 72 ALA 73 GLY 74 GLN 75 LEU 76 THR 77 ILE 78 ILE 79 GLU 80 GLY 81 PHE 82 LYS 83 ARG 84 GLU 85 LEU 86 ASN 87 TYR 88 VAL 89 ALA 90 ARG 91 ASN 92 LYS 93 PRO 94 LYS 95 THR 96 VAL 97 ILE 98 TYR 99 TRP 100 LEU 101 ALA 102 GLU 103 VAL 104 LYS 105 ASP 106 TYR 107 ASP 108 VAL 109 GLU 110 ILE 111 ARG 112 LEU 113 SER 114 HIS 115 GLU 116 HIS 117 GLN 118 ALA 119 TYR 120 ARG 121 TRP 122 LEU 123 GLY 124 LEU 125 GLU 126 GLU 127 ALA 128 CYS 129 GLN 130 LEU 131 ALA 132 GLN 133 PHE 134 LYS 135 GLU 136 MET 137 LYS 138 ALA 139 ALA 140 LEU 141 GLN 142 GLU 143 GLY 144 HIS 145 GLN 146 PHE 147 LEU 148 CYS 149 SER 150 ILE 151 GLU 152 ALA 153 LEU stop_ _Sequence_homology_query_date 2005-09-22 _Sequence_homology_query_revised_last_date 2005-08-25 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 1XSA "A Chain A, Structure Of The Nudix Enzyme Ap4aHydrolase From Homo Sapiens (E63a Mutant)" 100.00 153 100 100 2e-85 PDB 1XSB "A Chain A, Structure Of The Nudix Enzyme Ap4aHydrolase From Homo Sapiens (E63a Mutant) In ComplexWith Atp. No Atp Restraints Included" 100.00 153 100 100 2e-85 PDB 1XSC "A Chain A, Structure Of The Nudix Enzyme Ap4aHydrolase From Homo Sapiens (E63a Mutant) In ComplexWith Atp" 100.00 153 100 100 2e-85 EMBL CAI15964.1 "nudix (nucleoside diphosphate linkedmoiety X)-type motif 2 [Homo sapiens]" 104.08 147 99 99 2e-81 GenBank AAH04926.1 "Nudix-type motif 2 [Homo sapiens]" 104.08 147 99 99 2e-81 GenBank AAX36304.1 "nudix-type motif 2 [synthetic construct]" 104.08 147 99 99 2e-81 GenBank AAX41136.1 "nudix-type motif 2 [synthetic construct]" 104.08 147 99 99 2e-81 GenBank AAX36755.1 "nudix-type motif 2 [synthetic construct]" 103.38 148 99 99 8e-82 GenBank AAX42702.1 "nudix-type motif 2 [synthetic construct]" 103.38 148 99 99 8e-82 REF NP_001152.1 "nudix-type motif 2 [Homo sapiens]" 104.08 147 99 99 2e-81 REF NP_671701.1 "nudix-type motif 2 [Homo sapiens]" 104.08 147 99 99 2e-81 REF NP_671702.1 "nudix-type motif 2 [Homo sapiens]" 104.08 147 99 99 2e-81 REF XP_520541.1 "PREDICTED: similar toBis(5-nucleosyl)-tetraphosphatase [Asymmetrical](Diadenosine 5,5-P1,P4-tetraphosphate asymmetricalhydrolase) (Diadenosine tetraphosphatase) (Ap4Ahydrolase) (Ap4AASE) [Pan troglodytes]" 104.08 147 99 99 2e-81 SWISS-PROT P50583 "AP4A_HUMAN Bis(5'-nucleosyl)-tetraphosphatase[Asymmetrical] (Diadenosine 5',5'''-P1,P4-tetraphosphateasymmetrical hydrolase) (Diadenosine tetraphosphatase)(Ap4A hydrolase) (Ap4Aase) (Nucleosidediphosphate-linked moiety X motif 2) (Nudix motif 2)" 104.08 147 99 99 2e-81 stop_ save_ ############# # Ligands # ############# save_ATP _Saveframe_category ligand _Mol_type non-polymer _Name_common 'ADENOSINE-5'-TRIPHOSPHATE' _Abbreviation_common ATP _Name_IUPAC . _BMRB_code ATP _PDB_code ATP _Mol_empirical_formula 'C10 H16 N5 O13 P3' _Mol_paramagnetic no _Mol_aromatic yes _Details . loop_ _Atom_name _PDB_atom_name _Atom_type _Atom_chirality _Atom_charge _Atom_oxidation_number _Atom_unpaired_electrons PG PG P ? 0 ? ? O1G O1G O ? 0 ? ? O2G O2G O ? 0 ? ? O3G O3G O ? 0 ? ? PB PB P ? 0 ? ? O1B O1B O ? 0 ? ? O2B O2B O ? 0 ? ? O3B O3B O ? 0 ? ? PA PA P ? 0 ? ? O1A O1A O ? 0 ? ? O2A O2A O ? 0 ? ? O3A O3A O ? 0 ? ? "O5'" O5* O ? 0 ? ? "C5'" C5* C ? 0 ? ? "C4'" C4* C ? 0 ? ? "O4'" O4* O ? 0 ? ? "C3'" C3* C ? 0 ? ? "O3'" O3* O ? 0 ? ? "C2'" C2* C ? 0 ? ? "O2'" O2* O ? 0 ? ? "C1'" C1* C ? 0 ? ? N9 N9 N ? 0 ? ? C8 C8 C ? 0 ? ? N7 N7 N ? 0 ? ? C5 C5 C ? 0 ? ? C6 C6 C ? 0 ? ? N6 N6 N ? 0 ? ? N1 N1 N ? 0 ? ? C2 C2 C ? 0 ? ? N3 N3 N ? 0 ? ? C4 C4 C ? 0 ? ? HO2G 2HOG H ? 0 ? ? HO3G 3HOG H ? 0 ? ? HO2B 2HOB H ? 0 ? ? HO2A 2HOA H ? 0 ? ? "H51'" "1H5*" H ? 0 ? ? "H52'" "2H5*" H ? 0 ? ? "H4'" "H4*" H ? 0 ? ? "H3'" "H3*" H ? 0 ? ? "HO3'" "*HO3" H ? 0 ? ? "H2'" "H2*" H ? 0 ? ? "HO2'" "*HO2" H ? 0 ? ? "H1'" "H1*" H ? 0 ? ? H8 H8 H ? 0 ? ? H2 H2 H ? 0 ? ? H61 1HN6 H ? 0 ? ? H62 2HN6 H ? 0 ? ? 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 SING PG O3B PG O3B DOUB PG O1G PG O1G SING PG O2G PG O2G SING PG O3G PG O3G SING O2G HO2G O2G 2HOG SING O3G HO3G O3G 3HOG DOUB PB O1B PB O1B SING PB O2B PB O2B SING PB O3B PB O3B SING PB O3A PB O3A SING O2B HO2B O2B 2HOB DOUB PA O1A PA O1A SING PA O2A PA O2A SING PA O3A PA O3A SING PA "O5'" PA "O5*" SING O2A HO2A O2A 2HOA SING "O5'" "C5'" "O5*" "C5*" SING "C5'" "C4'" "C5*" "C4*" SING "C5'" "H51'" "C5*" "1H5*" SING "C5'" "H52'" "C5*" "2H5*" SING "C4'" "O4'" "C4*" "O4*" SING "C4'" "C3'" "C4*" "C3*" SING "C4'" "H4'" "C4*" "H4*" SING "O4'" "C1'" "O4*" "C1*" SING "C3'" "O3'" "C3*" "O3*" SING "C3'" "C2'" "C3*" "C2*" SING "C3'" "H3'" "C3*" "H3*" SING "O3'" "HO3'" "O3*" "*HO3" SING "C2'" "O2'" "C2*" "O2*" SING "C2'" "C1'" "C2*" "C1*" SING "C2'" "H2'" "C2*" "H2*" SING "O2'" "HO2'" "O2*" "*HO2" SING "C1'" N9 "C1*" N9 SING "C1'" "H1'" "C1*" "H1*" SING N9 C8 N9 C8 SING N9 C4 N9 C4 DOUB C8 N7 C8 N7 SING C8 H8 C8 H8 SING N7 C5 N7 C5 SING C5 C6 C5 C6 DOUB C5 C4 C5 C4 SING C6 N6 C6 N6 DOUB C6 N1 C6 N1 SING N6 H61 N6 1HN6 SING N6 H62 N6 2HN6 SING N1 C2 N1 C2 DOUB C2 N3 C2 N3 SING C2 H2 C2 H2 SING N3 C4 N3 C4 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $AP4A_hydrolase Human 9606 Eukaryota Metazoa Homo sapiens 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 $AP4A_hydrolase "recombinant technology" "E. coli" . . . . 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 $AP4A_hydrolase 1.0 mM "[U-95% 13C; U-95% 15N]" $ATP 1.5 mM "[U-95% 13C; U-95% 15N]" stop_ save_ ############################ # Computer software used # ############################ save_nmrPipe _Saveframe_category software _Name nmrPipe _Version 2.1 loop_ _Vendor _Address _Electronic_address "F. Delaglio" "NIH :aboratory of CHemical Physics NIDDK" . stop_ save_ save_software _Saveframe_category software _Name XEASY _Version 1.4 loop_ _Vendor _Address _Electronic_address "Kurt Wuthrich" . . stop_ _Details "xeasy software ETH" save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model Inova _Field_strength 600 save_ save_NMR_spectrometer_2 _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model Inova _Field_strength 500 save_ ####################### # Sample conditions # ####################### save_sample_conditions _Saveframe_category sample_conditions loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 6.5 0.1 pH temperature 293 1 K "ionic strength" 40 2 mM 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 . . . 1.0 DSS C 13 "methyl protons" ppm 0.0 . indirect . . . 0.251449530 DSS N 15 "methyl protons" ppm 0.0 . indirect . . . 0.101329118 stop_ save_ ################################### # Assigned chemical shift lists # ################################### ################################################################### # Chemical Shift Ambiguity Index Value Definitions # # # # Index Value Definition # # # # 1 Unique (geminal atoms and geminal methyl # # groups with identical chemical shifts # # are assumed to be assigned to # # stereospecific atoms) # # 2 Ambiguity of geminal atoms or geminal methyl # # proton groups # # 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) # # 9 Ambiguous, specific ambiguity not defined # # # ################################################################### save_assigned_chemical_shifts _Saveframe_category assigned_chemical_shifts loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $sample_conditions _Chem_shift_reference_set_label $chemical_shift_reference _Mol_system_component_name "AP4A hydrolase monomer" 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 GLY CA C 43.46 . 1 2 1 GLY HA2 H 3.87 . 1 3 1 GLY HA3 H 3.87 . 1 4 2 PRO CD C 49.66 . 1 5 2 PRO CA C 62.86 . 1 6 2 PRO HA H 4.37 . 1 7 2 PRO CB C 32.26 . 1 8 2 PRO HB2 H 2.21 . 2 9 2 PRO HB3 H 1.85 . 2 10 2 PRO CG C 26.96 . 1 11 2 PRO HG2 H 1.92 . 1 12 2 PRO HG3 H 1.92 . 1 13 2 PRO HD2 H 3.46 . 1 14 2 PRO HD3 H 3.46 . 1 15 2 PRO C C 176.99 . 1 16 3 LEU N N 122.10 . 1 17 3 LEU H H 8.48 . 1 18 3 LEU CA C 55.36 . 1 19 3 LEU HA H 4.23 . 1 20 3 LEU CB C 42.16 . 1 21 3 LEU HB2 H 1.57 . 2 22 3 LEU HB3 H 1.50 . 2 23 3 LEU CG C 27.06 . 1 24 3 LEU HG H 1.55 . 1 25 3 LEU HD1 H 0.78 . 2 26 3 LEU HD2 H 0.83 . 2 27 3 LEU CD1 C 23.46 . 1 28 3 LEU CD2 C 24.96 . 1 29 3 LEU C C 177.99 . 1 30 4 GLY N N 109.20 . 1 31 4 GLY H H 8.35 . 1 32 4 GLY CA C 45.26 . 1 33 4 GLY HA2 H 3.86 . 1 34 4 GLY HA3 H 3.86 . 1 35 4 GLY C C 174.19 . 1 36 5 SER N N 114.90 . 1 37 5 SER H H 8.11 . 1 38 5 SER CA C 58.26 . 1 39 5 SER HA H 4.30 . 1 40 5 SER CB C 63.76 . 1 41 5 SER HB2 H 3.79 . 2 42 5 SER HB3 H 3.72 . 2 43 5 SER C C 174.59 . 1 44 6 MET N N 121.70 . 1 45 6 MET H H 8.30 . 1 46 6 MET CA C 55.16 . 1 47 6 MET HA H 4.36 . 1 48 6 MET CB C 32.76 . 1 49 6 MET HB2 H 2.01 . 2 50 6 MET HB3 H 1.92 . 2 51 6 MET CG C 32.06 . 1 52 6 MET HG2 H 2.44 . 2 53 6 MET HG3 H 2.51 . 2 54 6 MET HE H 2.00 . 1 55 6 MET CE C 16.96 . 1 56 6 MET C C 175.39 . 1 57 7 ALA N N 123.30 . 1 58 7 ALA H H 7.94 . 1 59 7 ALA CA C 51.86 . 1 60 7 ALA HA H 4.19 . 1 61 7 ALA HB H 1.13 . 1 62 7 ALA CB C 19.66 . 1 63 7 ALA C C 177.29 . 1 64 8 LEU N N 122.30 . 1 65 8 LEU H H 8.26 . 1 66 8 LEU CA C 54.76 . 1 67 8 LEU HA H 4.30 . 1 68 8 LEU CB C 43.16 . 1 69 8 LEU HB2 H 1.45 . 1 70 8 LEU HB3 H 1.45 . 1 71 8 LEU CG C 27.16 . 1 72 8 LEU HG H 1.42 . 1 73 8 LEU HD1 H 0.70 . 2 74 8 LEU HD2 H 0.65 . 2 75 8 LEU CD1 C 25.36 . 1 76 8 LEU CD2 C 23.66 . 1 77 8 LEU C C 175.39 . 1 78 9 ARG N N 124.40 . 1 79 9 ARG H H 8.32 . 1 80 9 ARG CA C 55.06 . 1 81 9 ARG HA H 5.04 . 1 82 9 ARG CB C 28.76 . 1 83 9 ARG HB2 H 1.62 . 2 84 9 ARG HB3 H 1.49 . 2 85 9 ARG CG C 33.06 . 1 86 9 ARG HG2 H 1.37 . 2 87 9 ARG HG3 H 1.19 . 2 88 9 ARG CD C 43.16 . 1 89 9 ARG HD2 H 2.98 . 1 90 9 ARG HD3 H 2.98 . 1 91 9 ARG C C 174.29 . 1 92 10 ALA N N 127.90 . 1 93 10 ALA H H 8.98 . 1 94 10 ALA CA C 50.06 . 1 95 10 ALA HA H 5.20 . 1 96 10 ALA HB H 0.93 . 1 97 10 ALA CB C 23.36 . 1 98 10 ALA C C 175.39 . 1 99 11 CYS N N 115.30 . 1 100 11 CYS H H 8.63 . 1 101 11 CYS CA C 55.56 . 1 102 11 CYS HA H 5.47 . 1 103 11 CYS CB C 33.26 . 1 104 11 CYS HB2 H 3.10 . 2 105 11 CYS HB3 H 2.48 . 2 106 11 CYS HG H 1.64 . 1 107 11 CYS C C 173.79 . 1 108 12 GLY N N 110.40 . 1 109 12 GLY H H 9.29 . 1 110 12 GLY CA C 45.46 . 1 111 12 GLY HA2 H 4.51 . 1 112 12 GLY HA3 H 4.51 . 1 113 12 GLY C C 171.39 . 1 114 13 LEU N N 114.90 . 1 115 13 LEU H H 7.52 . 1 116 13 LEU CA C 52.56 . 1 117 13 LEU HA H 5.38 . 1 118 13 LEU CB C 45.36 . 1 119 13 LEU HB2 H 1.74 . 1 120 13 LEU HB3 H 1.74 . 1 121 13 LEU CG C 27.56 . 1 122 13 LEU HG H 1.37 . 1 123 13 LEU HD1 H 0.71 . 2 124 13 LEU HD2 H 0.90 . 2 125 13 LEU CD1 C 26.36 . 1 126 13 LEU CD2 C 25.66 . 1 127 13 LEU C C 174.99 . 1 128 14 ILE N N 122.00 . 1 129 14 ILE H H 9.52 . 1 130 14 ILE CA C 61.76 . 1 131 14 ILE HA H 4.17 . 1 132 14 ILE CB C 37.66 . 1 133 14 ILE HB H 1.83 . 1 134 14 ILE HG2 H 0.82 . 1 135 14 ILE CG2 C 19.06 . 1 136 14 ILE CG1 C 27.76 . 1 137 14 ILE HG12 H 0.23 . 1 138 14 ILE HG13 H 0.23 . 1 139 14 ILE HD1 H 0.40 . 1 140 14 ILE CD1 C 13.16 . 1 141 14 ILE C C 174.59 . 1 142 15 ILE N N 130.50 . 1 143 15 ILE H H 7.82 . 1 144 15 ILE CA C 59.06 . 1 145 15 ILE HA H 5.30 . 1 146 15 ILE CB C 38.96 . 1 147 15 ILE HB H 1.63 . 1 148 15 ILE HG2 H 0.81 . 1 149 15 ILE CG2 C 18.96 . 1 150 15 ILE CG1 C 27.76 . 1 151 15 ILE HG12 H 1.48 . 2 152 15 ILE HG13 H 1.22 . 2 153 15 ILE HD1 H 0.73 . 1 154 15 ILE CD1 C 13.96 . 1 155 15 ILE C C 176.59 . 1 156 16 PHE N N 126.10 . 1 157 16 PHE H H 9.17 . 1 158 16 PHE CA C 55.36 . 1 159 16 PHE HA H 6.24 . 1 160 16 PHE CB C 43.26 . 1 161 16 PHE HB2 H 2.71 . 2 162 16 PHE HB3 H 2.56 . 2 163 16 PHE HD1 H 6.74 . 1 164 16 PHE HD2 H 6.74 . 1 165 16 PHE HE1 H 6.91 . 1 166 16 PHE HE2 H 6.91 . 1 167 16 PHE CD1 C 128.46 . 1 168 16 PHE CE1 C 130.46 . 1 169 16 PHE CZ C 131.86 . 1 170 16 PHE HZ H 7.19 . 1 171 16 PHE C C 171.39 . 1 172 17 ARG N N 115.50 . 1 173 17 ARG H H 9.26 . 1 174 17 ARG CA C 52.46 . 1 175 17 ARG HA H 4.82 . 1 176 17 ARG CB C 34.06 . 1 177 17 ARG HB2 H 1.23 . 1 178 17 ARG HB3 H 1.23 . 1 179 17 ARG C C 173.69 . 1 180 18 ARG N N 120.00 . 1 181 18 ARG H H 8.58 . 1 182 18 ARG CA C 54.46 . 1 183 18 ARG HA H 5.09 . 1 184 18 ARG CB C 28.06 . 1 185 18 ARG HB2 H 1.52 . 2 186 18 ARG HB3 H 1.47 . 2 187 18 ARG CG C 32.46 . 1 188 18 ARG HG2 H 1.70 . 2 189 18 ARG HG3 H 1.60 . 2 190 18 ARG CD C 43.56 . 1 191 18 ARG HD2 H 3.11 . 1 192 18 ARG HD3 H 3.11 . 1 193 18 ARG C C 175.39 . 1 194 19 CYS N N 121.80 . 1 195 19 CYS H H 8.63 . 1 196 19 CYS CA C 58.26 . 1 197 19 CYS HA H 4.10 . 1 198 19 CYS CB C 27.66 . 1 199 19 CYS HB2 H 2.71 . 1 200 19 CYS HB3 H 2.71 . 1 201 19 CYS C C 174.99 . 1 202 20 LEU N N 125.70 . 1 203 20 LEU H H 8.24 . 1 204 20 LEU CA C 55.96 . 1 205 20 LEU HA H 4.07 . 1 206 20 LEU CB C 41.76 . 1 207 20 LEU HB2 H 1.39 . 1 208 20 LEU HB3 H 1.39 . 1 209 20 LEU CG C 26.96 . 1 210 20 LEU HG H 1.40 . 1 211 20 LEU HD1 H 0.72 . 2 212 20 LEU HD2 H 0.67 . 2 213 20 LEU CD1 C 24.76 . 1 214 20 LEU CD2 C 23.16 . 1 215 20 LEU C C 177.09 . 1 216 21 ILE N N 119.50 . 1 217 21 ILE H H 7.65 . 1 218 21 ILE CA C 58.06 . 1 219 21 ILE HA H 4.32 . 1 220 21 ILE CB C 38.46 . 1 221 21 ILE HB H 1.68 . 1 222 21 ILE HG2 H 0.74 . 1 223 21 ILE CG2 C 17.36 . 1 224 21 ILE CG1 C 26.76 . 1 225 21 ILE HG12 H 1.27 . 2 226 21 ILE HG13 H 0.92 . 2 227 21 ILE HD1 H 0.69 . 1 228 21 ILE CD1 C 12.76 . 1 229 22 PRO CD C 50.66 . 1 230 22 PRO CA C 63.36 . 1 231 22 PRO HA H 4.23 . 1 232 22 PRO CB C 31.96 . 1 233 22 PRO HB2 H 2.05 . 2 234 22 PRO HB3 H 1.79 . 2 235 22 PRO CG C 27.46 . 1 236 22 PRO HG2 H 1.95 . 2 237 22 PRO HG3 H 1.79 . 2 238 22 PRO HD2 H 3.69 . 2 239 22 PRO HD3 H 3.54 . 2 240 22 PRO C C 176.69 . 1 241 23 LYS N N 120.10 . 1 242 23 LYS H H 8.33 . 1 243 23 LYS CA C 56.16 . 1 244 23 LYS HA H 4.23 . 1 245 23 LYS CB C 33.46 . 1 246 23 LYS HB2 H 1.82 . 2 247 23 LYS HB3 H 1.70 . 2 248 23 LYS HG2 H 1.36 . 2 249 23 LYS HG3 H 1.33 . 2 250 23 LYS CD C 29.16 . 1 251 23 LYS HD2 H 1.59 . 1 252 23 LYS HD3 H 1.59 . 1 253 23 LYS CE C 41.96 . 1 254 23 LYS HE2 H 2.89 . 1 255 23 LYS HE3 H 2.89 . 1 256 23 LYS C C 176.79 . 1 257 24 VAL N N 118.50 . 1 258 24 VAL H H 8.01 . 1 259 24 VAL CA C 62.86 . 1 260 24 VAL HA H 3.92 . 1 261 24 VAL CB C 32.46 . 1 262 24 VAL HB H 2.01 . 1 263 24 VAL CG2 C 20.96 . 1 264 24 VAL HG1 H 0.85 . 1 265 24 VAL HG2 H 0.85 . 1 266 24 VAL C C 175.89 . 1 267 25 ASP N N 120.10 . 1 268 25 ASP H H 8.21 . 1 269 25 ASP CA C 54.56 . 1 270 25 ASP HA H 4.40 . 1 271 25 ASP CB C 40.56 . 1 272 25 ASP HB2 H 2.66 . 1 273 25 ASP HB3 H 2.66 . 1 274 25 ASP C C 175.79 . 1 275 26 ASN N N 116.30 . 1 276 26 ASN H H 8.10 . 1 277 26 ASN CA C 53.36 . 1 278 26 ASN HA H 4.61 . 1 279 26 ASN CB C 39.26 . 1 280 26 ASN HB2 H 2.78 . 2 281 26 ASN HB3 H 2.71 . 2 282 26 ASN ND2 N 112.50 . 1 283 26 ASN HD21 H 7.48 . 2 284 26 ASN HD22 H 6.81 . 2 285 26 ASN C C 174.79 . 1 286 27 ASN N N 118.30 . 1 287 27 ASN H H 8.39 . 1 288 27 ASN CA C 52.96 . 1 289 27 ASN HA H 4.81 . 1 290 27 ASN CB C 39.26 . 1 291 27 ASN HB2 H 2.78 . 2 292 27 ASN HB3 H 2.72 . 2 293 27 ASN ND2 N 114.40 . 1 294 27 ASN HD21 H 7.90 . 2 295 27 ASN HD22 H 7.01 . 2 296 27 ASN C C 174.49 . 1 297 28 ALA N N 124.00 . 1 298 28 ALA H H 8.35 . 1 299 28 ALA CA C 53.76 . 1 300 28 ALA HA H 4.25 . 1 301 28 ALA HB H 1.42 . 1 302 28 ALA CB C 19.56 . 1 303 28 ALA C C 177.09 . 1 304 29 ILE N N 117.30 . 1 305 29 ILE H H 7.75 . 1 306 29 ILE CA C 60.06 . 1 307 29 ILE HA H 4.60 . 1 308 29 ILE CB C 39.86 . 1 309 29 ILE HB H 1.59 . 1 310 29 ILE HG2 H 0.19 . 1 311 29 ILE CG2 C 17.96 . 1 312 29 ILE CG1 C 27.66 . 1 313 29 ILE HG12 H 1.24 . 2 314 29 ILE HG13 H 0.79 . 2 315 29 ILE HD1 H 0.36 . 1 316 29 ILE CD1 C 13.16 . 1 317 29 ILE C C 175.49 . 1 318 30 GLU N N 123.50 . 1 319 30 GLU H H 8.55 . 1 320 30 GLU CA C 53.76 . 1 321 30 GLU HA H 4.73 . 1 322 30 GLU CB C 34.76 . 1 323 30 GLU HB2 H 1.28 . 1 324 30 GLU HB3 H 1.28 . 1 325 30 GLU C C 174.89 . 1 326 31 PHE N N 119.10 . 1 327 31 PHE H H 9.79 . 1 328 31 PHE CA C 57.46 . 1 329 31 PHE HA H 5.35 . 1 330 31 PHE CB C 42.16 . 1 331 31 PHE HB2 H 3.03 . 2 332 31 PHE HB3 H 2.51 . 2 333 31 PHE HD1 H 7.11 . 1 334 31 PHE HD2 H 7.11 . 1 335 31 PHE HE1 H 6.86 . 1 336 31 PHE HE2 H 6.86 . 1 337 31 PHE CD1 C 132.26 . 1 338 31 PHE CE1 C 130.16 . 1 339 31 PHE HZ H 6.72 . 1 340 31 PHE C C 175.19 . 1 341 32 LEU N N 122.90 . 1 342 32 LEU H H 7.74 . 1 343 32 LEU CA C 53.66 . 1 344 32 LEU HA H 4.29 . 1 345 32 LEU CB C 41.96 . 1 346 32 LEU HB2 H 1.17 . 2 347 32 LEU HB3 H -0.29 . 2 348 32 LEU CG C 26.86 . 1 349 32 LEU HG H 0.73 . 1 350 32 LEU HD1 H -0.33 . 2 351 32 LEU HD2 H 0.21 . 2 352 32 LEU CD1 C 22.36 . 1 353 32 LEU CD2 C 25.96 . 1 354 32 LEU C C 175.49 . 1 355 33 LEU N N 123.80 . 1 356 33 LEU H H 8.57 . 1 357 33 LEU CA C 53.16 . 1 358 33 LEU HA H 4.68 . 1 359 33 LEU CB C 46.76 . 1 360 33 LEU HB2 H 1.62 . 2 361 33 LEU HB3 H 1.39 . 2 362 33 LEU CG C 27.66 . 1 363 33 LEU HG H 1.42 . 1 364 33 LEU HD1 H 0.63 . 2 365 33 LEU HD2 H 0.66 . 2 366 33 LEU CD1 C 26.86 . 1 367 33 LEU CD2 C 23.36 . 1 368 33 LEU C C 174.29 . 1 369 34 LEU N N 119.60 . 1 370 34 LEU H H 8.78 . 1 371 34 LEU CA C 52.96 . 1 372 34 LEU HA H 4.89 . 1 373 34 LEU CB C 43.46 . 1 374 34 LEU HB2 H 1.25 . 2 375 34 LEU HB3 H 0.65 . 2 376 34 LEU CG C 27.56 . 1 377 34 LEU HG H 1.27 . 1 378 34 LEU HD1 H 0.23 . 2 379 34 LEU HD2 H 0.40 . 2 380 34 LEU CD1 C 25.26 . 1 381 34 LEU CD2 C 23.66 . 1 382 34 LEU C C 175.89 . 1 383 35 GLN N N 123.80 . 1 384 35 GLN H H 8.28 . 1 385 35 GLN CA C 53.66 . 1 386 35 GLN HA H 3.78 . 1 387 35 GLN CB C 26.66 . 1 388 35 GLN HB2 H 1.43 . 2 389 35 GLN HB3 H -1.42 . 2 390 35 GLN CG C 36.96 . 1 391 35 GLN HG2 H 0.63 . 1 392 35 GLN HG3 H 0.63 . 1 393 35 GLN C C 176.09 . 1 394 36 ALA N N 132.00 . 1 395 36 ALA H H 8.80 . 1 396 36 ALA CA C 53.36 . 1 397 36 ALA HA H 4.17 . 1 398 36 ALA HB H 1.36 . 1 399 36 ALA CB C 19.46 . 1 400 36 ALA C C 178.19 . 1 401 37 SER N N 116.30 . 1 402 37 SER H H 8.15 . 1 403 37 SER CA C 58.66 . 1 404 37 SER HA H 4.36 . 1 405 37 SER CB C 63.96 . 1 406 37 SER HB2 H 3.82 . 2 407 37 SER HB3 H 3.44 . 2 408 37 SER C C 172.29 . 1 409 38 ASP N N 121.60 . 1 410 38 ASP H H 7.83 . 1 411 38 ASP CA C 51.56 . 1 412 38 ASP HA H 4.64 . 1 413 38 ASP CB C 42.76 . 1 414 38 ASP HB2 H 2.60 . 2 415 38 ASP HB3 H 2.62 . 2 416 38 ASP C C 174.79 . 1 417 39 GLY N N 105.00 . 1 418 39 GLY H H 8.17 . 1 419 39 GLY CA C 46.86 . 1 420 39 GLY HA2 H 3.66 . 2 421 39 GLY HA3 H 3.53 . 2 422 39 GLY C C 175.39 . 1 423 40 ILE N N 118.80 . 1 424 40 ILE H H 8.69 . 1 425 40 ILE CA C 60.56 . 1 426 40 ILE HA H 4.29 . 1 427 40 ILE CB C 37.76 . 1 428 40 ILE HB H 2.19 . 1 429 40 ILE HG2 H 0.86 . 1 430 40 ILE CG2 C 17.86 . 1 431 40 ILE CG1 C 26.86 . 1 432 40 ILE HG12 H 1.31 . 2 433 40 ILE HG13 H 1.15 . 2 434 40 ILE HD1 H 0.87 . 1 435 40 ILE CD1 C 14.56 . 1 436 40 ILE C C 176.99 . 1 437 41 HIS N N 116.40 . 1 438 41 HIS H H 8.44 . 1 439 41 HIS CA C 56.36 . 1 440 41 HIS HA H 4.36 . 1 441 41 HIS CB C 25.56 . 1 442 41 HIS HB2 H 3.47 . 2 443 41 HIS HB3 H 2.71 . 2 444 41 HIS CD2 C 120.96 . 1 445 41 HIS CE1 C 136.26 . 1 446 41 HIS HD2 H 6.96 . 1 447 41 HIS HE1 H 8.19 . 1 448 41 HIS C C 173.59 . 1 449 42 HIS N N 116.50 . 1 450 42 HIS H H 8.19 . 1 451 42 HIS CA C 56.26 . 1 452 42 HIS HA H 4.85 . 1 453 42 HIS CB C 31.06 . 1 454 42 HIS HB2 H 3.39 . 2 455 42 HIS HB3 H 2.91 . 2 456 42 HIS CD2 C 117.06 . 1 457 42 HIS CE1 C 141.06 . 1 458 42 HIS HD2 H 6.94 . 1 459 42 HIS HE1 H 7.91 . 1 460 43 TRP N N 120.50 . 1 461 43 TRP H H 8.81 . 1 462 43 TRP CA C 55.86 . 1 463 43 TRP HA H 5.48 . 1 464 43 TRP CB C 31.46 . 1 465 43 TRP HB2 H 2.76 . 2 466 43 TRP HB3 H 2.58 . 2 467 43 TRP CD1 C 128.66 . 1 468 43 TRP CE3 C 121.36 . 1 469 43 TRP NE1 N 132.10 . 1 470 43 TRP HD1 H 7.31 . 1 471 43 TRP HE3 H 6.87 . 1 472 43 TRP CZ3 C 120.76 . 1 473 43 TRP CZ2 C 115.16 . 1 474 43 TRP HE1 H 10.32 . 1 475 43 TRP HZ3 H 6.53 . 1 476 43 TRP CH2 C 123.06 . 1 477 43 TRP HZ2 H 7.14 . 1 478 43 TRP HH2 H 6.61 . 1 479 44 THR N N 112.30 . 1 480 44 THR H H 9.00 . 1 481 44 THR CA C 59.66 . 1 482 44 THR HA H 5.02 . 1 483 44 THR CB C 66.56 . 1 484 44 THR HB H 4.66 . 1 485 44 THR HG2 H 1.43 . 1 486 44 THR CG2 C 21.06 . 1 487 45 PRO CD C 51.36 . 1 488 45 PRO CA C 61.96 . 1 489 45 PRO HA H 4.99 . 1 490 45 PRO HD2 H 3.81 . 2 491 45 PRO HD3 H 3.55 . 2 492 46 PRO CD C 48.96 . 1 493 46 PRO CA C 62.86 . 1 494 46 PRO HA H 4.40 . 1 495 46 PRO CB C 32.26 . 1 496 46 PRO HB2 H 1.95 . 1 497 46 PRO HB3 H 1.95 . 1 498 46 PRO CG C 28.36 . 1 499 46 PRO HG2 H 2.26 . 2 500 46 PRO HG3 H 1.61 . 2 501 46 PRO HD2 H 4.48 . 2 502 46 PRO HD3 H 3.31 . 2 503 46 PRO C C 175.29 . 1 504 47 LYS N N 115.00 . 1 505 47 LYS H H 8.01 . 1 506 47 LYS CA C 55.66 . 1 507 47 LYS HA H 4.87 . 1 508 47 LYS CB C 34.06 . 1 509 47 LYS HB2 H 1.93 . 2 510 47 LYS HB3 H 1.02 . 2 511 47 LYS HG2 H 1.34 . 2 512 47 LYS HG3 H 1.05 . 2 513 47 LYS CD C 32.76 . 1 514 47 LYS HD2 H 1.82 . 2 515 47 LYS HD3 H 1.49 . 2 516 47 LYS CE C 42.26 . 1 517 47 LYS HE2 H 3.04 . 2 518 47 LYS HE3 H 2.87 . 2 519 47 LYS C C 174.69 . 1 520 48 GLY N N 106.60 . 1 521 48 GLY H H 8.41 . 1 522 48 GLY CA C 44.56 . 1 523 48 GLY HA2 H 4.53 . 2 524 48 GLY HA3 H 3.66 . 2 525 49 HIS N N 117.70 . 1 526 49 HIS H H 8.50 . 1 527 49 HIS CA C 55.76 . 1 528 49 HIS HA H 4.70 . 1 529 49 HIS CB C 29.66 . 1 530 49 HIS HB2 H 3.11 . 1 531 49 HIS HB3 H 3.11 . 1 532 49 HIS CD2 C 121.66 . 1 533 49 HIS CE1 C 137.96 . 1 534 49 HIS HD2 H 6.97 . 1 535 49 HIS C C 174.89 . 1 536 50 VAL N N 122.30 . 1 537 50 VAL H H 8.12 . 1 538 50 VAL CA C 62.26 . 1 539 50 VAL HA H 4.05 . 1 540 50 VAL CB C 33.26 . 1 541 50 VAL HB H 1.85 . 1 542 50 VAL HG1 H 0.97 . 2 543 50 VAL HG2 H 0.89 . 2 544 50 VAL CG1 C 22.06 . 1 545 50 VAL CG2 C 21.36 . 1 546 50 VAL C C 176.69 . 1 547 51 GLU N N 129.30 . 1 548 51 GLU H H 8.28 . 1 549 51 GLU CA C 53.66 . 1 550 51 GLU HA H 4.64 . 1 551 51 GLU CB C 29.06 . 1 552 51 GLU HB2 H 1.97 . 2 553 51 GLU HB3 H 1.48 . 2 554 51 GLU CG C 35.36 . 1 555 51 GLU HG2 H 2.26 . 2 556 51 GLU HG3 H 2.18 . 2 557 51 GLU C C 177.79 . 1 558 52 PRO CD C 50.46 . 1 559 52 PRO CA C 64.36 . 1 560 52 PRO HA H 4.15 . 1 561 52 PRO CB C 31.46 . 1 562 52 PRO HB2 H 2.19 . 2 563 52 PRO HB3 H 1.80 . 2 564 52 PRO CG C 27.96 . 1 565 52 PRO HG2 H 2.08 . 2 566 52 PRO HG3 H 1.90 . 2 567 52 PRO HD2 H 3.80 . 2 568 52 PRO HD3 H 3.63 . 2 569 53 GLY N N 112.50 . 1 570 53 GLY H H 8.59 . 1 571 53 GLY CA C 45.16 . 1 572 53 GLY HA2 H 4.16 . 2 573 53 GLY HA3 H 3.56 . 2 574 53 GLY C C 174.59 . 1 575 54 GLU N N 120.10 . 1 576 54 GLU H H 7.87 . 1 577 54 GLU CA C 55.96 . 1 578 54 GLU HA H 4.30 . 1 579 54 GLU CB C 31.06 . 1 580 54 GLU HB2 H 2.07 . 2 581 54 GLU HB3 H 1.98 . 2 582 54 GLU CG C 37.36 . 1 583 54 GLU HG2 H 2.18 . 2 584 54 GLU HG3 H 2.05 . 2 585 54 GLU C C 176.59 . 1 586 55 ASP N N 122.40 . 1 587 55 ASP H H 8.66 . 1 588 55 ASP CA C 53.26 . 1 589 55 ASP HA H 4.62 . 1 590 55 ASP CB C 42.96 . 1 591 55 ASP HB2 H 2.65 . 2 592 55 ASP HB3 H 2.54 . 2 593 55 ASP C C 176.49 . 1 594 56 ASP N N 123.50 . 1 595 56 ASP H H 8.41 . 1 596 56 ASP CA C 58.16 . 1 597 56 ASP HA H 4.40 . 1 598 56 ASP CB C 41.66 . 1 599 56 ASP HB2 H 3.27 . 2 600 56 ASP HB3 H 2.75 . 2 601 56 ASP C C 177.29 . 1 602 57 LEU N N 119.60 . 1 603 57 LEU H H 8.02 . 1 604 57 LEU CA C 57.26 . 1 605 57 LEU HA H 3.43 . 1 606 57 LEU CB C 40.86 . 1 607 57 LEU HB2 H 1.31 . 2 608 57 LEU HB3 H 0.70 . 2 609 57 LEU CG C 26.66 . 1 610 57 LEU HG H 0.93 . 1 611 57 LEU HD1 H -0.17 . 2 612 57 LEU HD2 H 0.23 . 2 613 57 LEU CD1 C 21.76 . 1 614 57 LEU CD2 C 24.66 . 1 615 57 LEU C C 178.99 . 1 616 58 GLU N N 117.70 . 1 617 58 GLU H H 7.58 . 1 618 58 GLU CA C 59.36 . 1 619 58 GLU HA H 3.76 . 1 620 58 GLU CB C 29.26 . 1 621 58 GLU HB2 H 2.20 . 2 622 58 GLU HB3 H 2.02 . 2 623 58 GLU CG C 36.46 . 1 624 58 GLU HG2 H 2.35 . 2 625 58 GLU HG3 H 2.14 . 2 626 58 GLU C C 180.39 . 1 627 59 THR N N 117.90 . 1 628 59 THR H H 8.22 . 1 629 59 THR CA C 67.66 . 1 630 59 THR HA H 3.66 . 1 631 59 THR CB C 67.96 . 1 632 59 THR HB H 4.20 . 1 633 59 THR HG2 H 1.01 . 1 634 59 THR CG2 C 22.26 . 1 635 59 THR C C 175.39 . 1 636 60 ALA N N 123.30 . 1 637 60 ALA H H 7.70 . 1 638 60 ALA CA C 55.66 . 1 639 60 ALA HA H 3.79 . 1 640 60 ALA HB H 1.36 . 1 641 60 ALA CB C 18.26 . 1 642 60 ALA C C 180.69 . 1 643 61 LEU N N 118.90 . 1 644 61 LEU H H 8.32 . 1 645 61 LEU CA C 57.86 . 1 646 61 LEU HA H 3.78 . 1 647 61 LEU CB C 42.36 . 1 648 61 LEU HB2 H 1.78 . 2 649 61 LEU HB3 H 1.27 . 2 650 61 LEU CG C 27.36 . 1 651 61 LEU HG H 1.49 . 1 652 61 LEU HD1 H 0.68 . 2 653 61 LEU HD2 H 0.69 . 2 654 61 LEU CD1 C 25.56 . 1 655 61 LEU CD2 C 23.46 . 1 656 61 LEU C C 179.79 . 1 657 62 ARG N N 123.70 . 1 658 62 ARG H H 8.42 . 1 659 62 ARG CA C 59.76 . 1 660 62 ARG HA H 4.02 . 1 661 62 ARG CB C 28.86 . 1 662 62 ARG HB2 H 1.92 . 2 663 62 ARG HB3 H 1.76 . 2 664 62 ARG CG C 26.16 . 1 665 62 ARG HG2 H 1.51 . 2 666 62 ARG HG3 H 1.52 . 2 667 62 ARG CD C 42.26 . 1 668 62 ARG HD2 H 3.26 . 2 669 62 ARG HD3 H 2.99 . 2 670 62 ARG C C 178.59 . 1 671 63 ALA N N 120.50 . 1 672 63 ALA H H 9.00 . 1 673 63 ALA CA C 54.66 . 1 674 63 ALA HA H 4.07 . 1 675 63 ALA HB H 1.18 . 1 676 63 ALA CB C 17.86 . 1 677 63 ALA C C 179.69 . 1 678 64 THR N N 114.40 . 1 679 64 THR H H 7.58 . 1 680 64 THR CA C 68.46 . 1 681 64 THR HA H 3.60 . 1 682 64 THR CB C 67.86 . 1 683 64 THR HB H 4.11 . 1 684 64 THR HG2 H 1.05 . 1 685 64 THR HG1 H 4.00 . 1 686 64 THR CG2 C 22.26 . 1 687 64 THR C C 176.19 . 1 688 65 GLN N N 124.20 . 1 689 65 GLN H H 7.78 . 1 690 65 GLN CA C 60.06 . 1 691 65 GLN HA H 3.77 . 1 692 65 GLN CB C 27.86 . 1 693 65 GLN HB2 H 2.23 . 1 694 65 GLN HB3 H 2.23 . 1 695 65 GLN CG C 33.86 . 1 696 65 GLN HG2 H 2.12 . 1 697 65 GLN HG3 H 2.12 . 1 698 65 GLN C C 179.29 . 1 699 66 GLU N N 118.60 . 1 700 66 GLU H H 8.81 . 1 701 66 GLU CA C 59.56 . 1 702 66 GLU HA H 3.85 . 1 703 66 GLU CB C 30.16 . 1 704 66 GLU HB2 H 2.12 . 2 705 66 GLU HB3 H 1.99 . 2 706 66 GLU CG C 36.76 . 1 707 66 GLU HG2 H 2.53 . 2 708 66 GLU HG3 H 2.22 . 2 709 66 GLU C C 179.89 . 1 710 67 GLU N N 113.70 . 1 711 67 GLU H H 8.83 . 1 712 67 GLU CA C 56.56 . 1 713 67 GLU HA H 4.48 . 1 714 67 GLU CB C 33.16 . 1 715 67 GLU HB2 H 1.89 . 2 716 67 GLU HB3 H 1.84 . 2 717 67 GLU CG C 37.56 . 1 718 67 GLU HG2 H 2.76 . 2 719 67 GLU HG3 H 2.57 . 2 720 67 GLU C C 176.79 . 1 721 68 ALA N N 115.40 . 1 722 68 ALA H H 7.70 . 1 723 68 ALA CA C 50.86 . 1 724 68 ALA HA H 4.59 . 1 725 68 ALA HB H 1.15 . 1 726 68 ALA CB C 20.36 . 1 727 68 ALA C C 177.19 . 1 728 69 GLY N N 107.10 . 1 729 69 GLY H H 7.55 . 1 730 69 GLY CA C 46.16 . 1 731 69 GLY HA2 H 3.95 . 1 732 69 GLY HA3 H 3.95 . 1 733 69 GLY C C 173.99 . 1 734 70 ILE N N 119.30 . 1 735 70 ILE H H 6.49 . 1 736 70 ILE CA C 60.66 . 1 737 70 ILE HA H 4.02 . 1 738 70 ILE CB C 39.66 . 1 739 70 ILE HB H 1.17 . 1 740 70 ILE HG2 H 0.72 . 1 741 70 ILE CG2 C 18.26 . 1 742 70 ILE CG1 C 26.36 . 1 743 70 ILE HG12 H 1.35 . 2 744 70 ILE HG13 H 0.59 . 2 745 70 ILE HD1 H 0.49 . 1 746 70 ILE CD1 C 13.36 . 1 747 70 ILE C C 174.79 . 1 748 71 GLU N N 126.10 . 1 749 71 GLU H H 8.72 . 1 750 71 GLU CA C 55.56 . 1 751 71 GLU HA H 4.11 . 1 752 71 GLU CB C 31.26 . 1 753 71 GLU HB2 H 2.12 . 2 754 71 GLU HB3 H 1.86 . 2 755 71 GLU CG C 36.26 . 1 756 71 GLU HG2 H 2.22 . 1 757 71 GLU HG3 H 2.22 . 1 758 71 GLU C C 177.59 . 1 759 72 ALA N N 123.40 . 1 760 72 ALA H H 8.22 . 1 761 72 ALA CA C 55.56 . 1 762 72 ALA HA H 3.76 . 1 763 72 ALA HB H 1.34 . 1 764 72 ALA CB C 18.76 . 1 765 72 ALA C C 180.09 . 1 766 73 GLY N N 101.60 . 1 767 73 GLY H H 8.46 . 1 768 73 GLY CA C 45.66 . 1 769 73 GLY HA2 H 4.00 . 2 770 73 GLY HA3 H 3.71 . 2 771 73 GLY C C 175.19 . 1 772 74 GLN N N 116.90 . 1 773 74 GLN H H 7.91 . 1 774 74 GLN CA C 55.36 . 1 775 74 GLN HA H 4.26 . 1 776 74 GLN CB C 30.36 . 1 777 74 GLN HB2 H 2.29 . 2 778 74 GLN HB3 H 2.24 . 2 779 74 GLN CG C 35.06 . 1 780 74 GLN HG2 H 2.24 . 2 781 74 GLN HG3 H 2.22 . 2 782 74 GLN NE2 N 112.60 . 1 783 74 GLN HE21 H 7.64 . 2 784 74 GLN HE22 H 6.96 . 2 785 74 GLN C C 174.69 . 1 786 75 LEU N N 119.40 . 1 787 75 LEU H H 7.62 . 1 788 75 LEU CA C 53.56 . 1 789 75 LEU HA H 5.04 . 1 790 75 LEU CB C 46.46 . 1 791 75 LEU HB2 H 1.53 . 2 792 75 LEU HB3 H 1.01 . 2 793 75 LEU CG C 25.56 . 1 794 75 LEU HG H 1.44 . 1 795 75 LEU HD1 H 0.52 . 2 796 75 LEU HD2 H 0.53 . 2 797 75 LEU CD1 C 25.56 . 1 798 75 LEU CD2 C 25.56 . 1 799 75 LEU C C 175.39 . 1 800 76 THR N N 116.70 . 1 801 76 THR H H 8.68 . 1 802 76 THR CA C 61.06 . 1 803 76 THR HA H 4.40 . 1 804 76 THR CB C 70.56 . 1 805 76 THR HB H 3.85 . 1 806 76 THR HG2 H 1.10 . 1 807 76 THR CG2 C 21.86 . 1 808 76 THR C C 173.99 . 1 809 77 ILE N N 127.80 . 1 810 77 ILE H H 8.88 . 1 811 77 ILE CA C 60.56 . 1 812 77 ILE HA H 4.26 . 1 813 77 ILE CB C 36.46 . 1 814 77 ILE HB H 1.86 . 1 815 77 ILE HG2 H 0.82 . 1 816 77 ILE CG2 C 17.26 . 1 817 77 ILE CG1 C 11.46 . 1 818 77 ILE HG12 H 1.34 . 2 819 77 ILE HG13 H 1.25 . 2 820 77 ILE HD1 H 0.61 . 1 821 77 ILE CD1 C 11.76 . 1 822 77 ILE C C 176.39 . 1 823 78 ILE N N 130.40 . 1 824 78 ILE H H 8.80 . 1 825 78 ILE CA C 58.36 . 1 826 78 ILE HA H 4.21 . 1 827 78 ILE CB C 35.56 . 1 828 78 ILE HB H 2.29 . 1 829 78 ILE HG2 H 1.12 . 1 830 78 ILE CG2 C 17.86 . 1 831 78 ILE CG1 C 27.66 . 1 832 78 ILE HG12 H 1.78 . 2 833 78 ILE HG13 H 1.50 . 2 834 78 ILE HD1 H 0.93 . 1 835 78 ILE CD1 C 9.06 . 1 836 78 ILE C C 176.19 . 1 837 79 GLU N N 128.30 . 1 838 79 GLU H H 8.72 . 1 839 79 GLU CA C 57.36 . 1 840 79 GLU HA H 4.32 . 1 841 79 GLU CB C 30.36 . 1 842 79 GLU HB2 H 2.03 . 2 843 79 GLU HB3 H 2.04 . 2 844 79 GLU CG C 36.46 . 1 845 79 GLU HG2 H 2.34 . 2 846 79 GLU HG3 H 2.27 . 2 847 79 GLU C C 177.49 . 1 848 80 GLY N N 107.50 . 1 849 80 GLY H H 8.55 . 1 850 80 GLY CA C 45.56 . 1 851 80 GLY HA2 H 4.38 . 2 852 80 GLY HA3 H 3.69 . 2 853 80 GLY C C 172.99 . 1 854 81 PHE N N 118.40 . 1 855 81 PHE H H 6.87 . 1 856 81 PHE CA C 57.06 . 1 857 81 PHE HA H 4.21 . 1 858 81 PHE CB C 40.76 . 1 859 81 PHE HB2 H 2.54 . 2 860 81 PHE HB3 H 1.27 . 2 861 81 PHE HD1 H 6.68 . 1 862 81 PHE HD2 H 6.68 . 1 863 81 PHE HE1 H 6.82 . 1 864 81 PHE HE2 H 6.82 . 1 865 81 PHE CD1 C 132.66 . 1 866 81 PHE CE1 C 130.36 . 1 867 81 PHE HZ H 6.94 . 1 868 81 PHE C C 173.19 . 1 869 82 LYS N N 128.00 . 1 870 82 LYS H H 7.25 . 1 871 82 LYS CA C 55.56 . 1 872 82 LYS HA H 4.23 . 1 873 82 LYS CB C 34.56 . 1 874 82 LYS HB2 H 1.09 . 1 875 82 LYS HB3 H 1.09 . 1 876 82 LYS CG C 23.46 . 1 877 82 LYS HG2 H 0.37 . 2 878 82 LYS HG3 H 0.15 . 2 879 82 LYS CD C 29.26 . 1 880 82 LYS HD2 H 1.17 . 1 881 82 LYS HD3 H 1.17 . 1 882 82 LYS CE C 41.46 . 1 883 82 LYS HE2 H 2.48 . 2 884 82 LYS HE3 H 2.38 . 2 885 82 LYS C C 174.69 . 1 886 83 ARG N N 125.50 . 1 887 83 ARG H H 8.61 . 1 888 83 ARG CA C 53.46 . 1 889 83 ARG HA H 4.38 . 1 890 83 ARG CB C 34.96 . 1 891 83 ARG HB2 H 1.56 . 2 892 83 ARG HB3 H 1.33 . 2 893 83 ARG CG C 28.16 . 1 894 83 ARG HG2 H 1.16 . 2 895 83 ARG HG3 H 0.95 . 2 896 83 ARG CD C 42.36 . 1 897 83 ARG HD2 H 3.22 . 2 898 83 ARG HD3 H 3.03 . 2 899 83 ARG C C 172.99 . 1 900 84 GLU N N 123.80 . 1 901 84 GLU H H 8.50 . 1 902 84 GLU CA C 54.36 . 1 903 84 GLU HA H 5.01 . 1 904 84 GLU CB C 31.66 . 1 905 84 GLU HB2 H 1.68 . 2 906 84 GLU HB3 H 1.66 . 2 907 84 GLU CG C 36.86 . 1 908 84 GLU HG2 H 1.85 . 2 909 84 GLU HG3 H 1.72 . 2 910 84 GLU C C 175.39 . 1 911 85 LEU N N 128.60 . 1 912 85 LEU H H 9.88 . 1 913 85 LEU CA C 54.66 . 1 914 85 LEU HA H 4.75 . 1 915 85 LEU CB C 44.86 . 1 916 85 LEU HB2 H 1.69 . 2 917 85 LEU HB3 H 1.68 . 2 918 85 LEU CG C 29.86 . 1 919 85 LEU HG H 1.81 . 1 920 85 LEU HD1 H 0.94 . 2 921 85 LEU HD2 H 0.95 . 2 922 85 LEU CD1 C 26.76 . 1 923 85 LEU CD2 C 25.36 . 1 924 85 LEU C C 175.19 . 1 925 86 ASN N N 118.50 . 1 926 86 ASN H H 8.64 . 1 927 86 ASN CA C 52.56 . 1 928 86 ASN HA H 5.52 . 1 929 86 ASN CB C 42.46 . 1 930 86 ASN HB2 H 2.46 . 1 931 86 ASN HB3 H 2.46 . 1 932 86 ASN ND2 N 116.10 . 1 933 86 ASN HD21 H 7.52 . 2 934 86 ASN HD22 H 7.42 . 2 935 86 ASN C C 173.49 . 1 936 87 TYR N N 118.40 . 1 937 87 TYR H H 8.29 . 1 938 87 TYR CA C 55.66 . 1 939 87 TYR HA H 4.60 . 1 940 87 TYR CB C 38.56 . 1 941 87 TYR HB2 H 2.73 . 2 942 87 TYR HB3 H 2.32 . 2 943 87 TYR HD1 H 5.84 . 1 944 87 TYR HD2 H 5.84 . 1 945 87 TYR HE1 H 5.92 . 1 946 87 TYR HE2 H 5.92 . 1 947 87 TYR CD1 C 132.76 . 1 948 87 TYR CE1 C 116.26 . 1 949 87 TYR C C 172.39 . 1 950 88 VAL N N 119.80 . 1 951 88 VAL H H 8.30 . 1 952 88 VAL CA C 62.06 . 1 953 88 VAL HA H 4.08 . 1 954 88 VAL CB C 31.86 . 1 955 88 VAL HB H 1.79 . 1 956 88 VAL HG1 H 0.70 . 2 957 88 VAL HG2 H 0.57 . 2 958 88 VAL CG1 C 21.36 . 1 959 88 VAL CG2 C 21.06 . 1 960 88 VAL C C 174.39 . 1 961 89 ALA N N 107.50 . 1 962 89 ALA H H 8.67 . 1 963 89 ALA CA C 49.96 . 1 964 89 ALA HA H 4.59 . 1 965 89 ALA HB H 1.07 . 1 966 89 ALA CB C 21.76 . 1 967 89 ALA C C 176.39 . 1 968 90 ARG N N 123.60 . 1 969 90 ARG H H 9.42 . 1 970 90 ARG CA C 57.26 . 1 971 90 ARG HA H 3.72 . 1 972 90 ARG CB C 28.26 . 1 973 90 ARG HB2 H 1.47 . 2 974 90 ARG HB3 H 1.32 . 2 975 90 ARG CG C 26.96 . 1 976 90 ARG HG2 H 1.87 . 2 977 90 ARG HG3 H 1.71 . 2 978 90 ARG CD C 43.26 . 1 979 90 ARG HD2 H 3.19 . 2 980 90 ARG HD3 H 3.03 . 2 981 90 ARG C C 175.69 . 1 982 91 ASN N N 108.80 . 1 983 91 ASN H H 8.51 . 1 984 91 ASN CA C 54.66 . 1 985 91 ASN HA H 3.96 . 1 986 91 ASN CB C 38.06 . 1 987 91 ASN HB2 H 2.91 . 2 988 91 ASN HB3 H 2.90 . 2 989 91 ASN ND2 N 112.70 . 1 990 91 ASN HD21 H 7.40 . 2 991 91 ASN HD22 H 6.78 . 2 992 91 ASN C C 173.99 . 1 993 92 LYS N N 120.50 . 1 994 92 LYS H H 7.70 . 1 995 92 LYS CA C 53.06 . 1 996 92 LYS HA H 4.78 . 1 997 92 LYS CB C 34.26 . 1 998 92 LYS HB2 H 1.66 . 1 999 92 LYS HB3 H 1.66 . 1 1000 92 LYS CG C 24.56 . 1 1001 92 LYS HG2 H 1.38 . 2 1002 92 LYS HG3 H 1.31 . 2 1003 92 LYS CE C 42.46 . 1 1004 92 LYS HE2 H 2.90 . 1 1005 92 LYS HE3 H 2.90 . 1 1006 93 PRO CA C 63.46 . 1 1007 93 PRO HA H 4.20 . 1 1008 93 PRO CB C 31.76 . 1 1009 93 PRO HB2 H 2.07 . 2 1010 93 PRO HB3 H 1.72 . 2 1011 93 PRO CG C 27.66 . 1 1012 93 PRO HG2 H 1.97 . 2 1013 93 PRO HG3 H 1.81 . 2 1014 93 PRO HD2 H 3.74 . 2 1015 93 PRO HD3 H 3.57 . 2 1016 93 PRO C C 175.09 . 1 1017 94 LYS N N 125.30 . 1 1018 94 LYS H H 8.67 . 1 1019 94 LYS CA C 54.96 . 1 1020 94 LYS HA H 4.68 . 1 1021 94 LYS CB C 34.36 . 1 1022 94 LYS HB2 H 1.06 . 1 1023 94 LYS HB3 H 1.06 . 1 1024 94 LYS CE C 41.26 . 1 1025 94 LYS HE2 H 2.26 . 2 1026 94 LYS HE3 H 2.17 . 2 1027 94 LYS C C 173.89 . 1 1028 95 THR N N 122.60 . 1 1029 95 THR H H 8.13 . 1 1030 95 THR CA C 60.76 . 1 1031 95 THR HA H 4.90 . 1 1032 95 THR CB C 67.76 . 1 1033 95 THR HB H 3.53 . 1 1034 95 THR HG2 H 0.95 . 1 1035 95 THR CG2 C 21.76 . 1 1036 95 THR C C 172.79 . 1 1037 96 VAL N N 125.40 . 1 1038 96 VAL H H 8.91 . 1 1039 96 VAL CA C 59.36 . 1 1040 96 VAL HA H 4.84 . 1 1041 96 VAL CB C 34.56 . 1 1042 96 VAL HB H 1.58 . 1 1043 96 VAL HG1 H 0.09 . 2 1044 96 VAL HG2 H 0.56 . 2 1045 96 VAL CG1 C 21.66 . 1 1046 96 VAL CG2 C 21.96 . 1 1047 96 VAL C C 173.79 . 1 1048 97 ILE N N 126.80 . 1 1049 97 ILE H H 8.17 . 1 1050 97 ILE CA C 59.26 . 1 1051 97 ILE HA H 4.54 . 1 1052 97 ILE CB C 38.86 . 1 1053 97 ILE HB H 1.72 . 1 1054 97 ILE HG2 H -0.03 . 1 1055 97 ILE CG2 C 18.66 . 1 1056 97 ILE CG1 C 28.36 . 1 1057 97 ILE HG12 H 1.16 . 2 1058 97 ILE HG13 H 0.93 . 2 1059 97 ILE HD1 H 0.55 . 1 1060 97 ILE CD1 C 13.16 . 1 1061 98 TYR N N 121.70 . 1 1062 98 TYR H H 8.61 . 1 1063 98 TYR CA C 57.26 . 1 1064 98 TYR HA H 5.39 . 1 1065 98 TYR CB C 43.16 . 1 1066 98 TYR HB2 H 2.97 . 2 1067 98 TYR HB3 H 2.34 . 2 1068 98 TYR HD1 H 6.71 . 1 1069 98 TYR HD2 H 6.71 . 1 1070 98 TYR HE1 H 6.51 . 1 1071 98 TYR HE2 H 6.51 . 1 1072 98 TYR CD1 C 132.46 . 1 1073 98 TYR CE1 C 117.96 . 1 1074 99 TRP N N 120.70 . 1 1075 99 TRP H H 7.75 . 1 1076 99 TRP CA C 58.26 . 1 1077 99 TRP HA H 4.95 . 1 1078 99 TRP CB C 32.16 . 1 1079 99 TRP HB2 H 3.67 . 2 1080 99 TRP HB3 H 2.92 . 2 1081 99 TRP CD1 C 127.36 . 1 1082 99 TRP CE3 C 121.96 . 1 1083 99 TRP NE1 N 126.60 . 1 1084 99 TRP HD1 H 7.50 . 1 1085 99 TRP HE3 H 7.76 . 1 1086 99 TRP CZ2 C 113.26 . 1 1087 99 TRP HE1 H 9.79 . 1 1088 99 TRP HZ3 H 6.72 . 1 1089 99 TRP CH2 C 123.46 . 1 1090 99 TRP HZ2 H 7.31 . 1 1091 99 TRP HH2 H 7.01 . 1 1092 99 TRP C C 175.19 . 1 1093 100 LEU N N 122.70 . 1 1094 100 LEU H H 10.23 . 1 1095 100 LEU CA C 54.66 . 1 1096 100 LEU HA H 5.26 . 1 1097 100 LEU CB C 45.46 . 1 1098 100 LEU HB2 H 1.80 . 2 1099 100 LEU HB3 H 1.64 . 2 1100 100 LEU CG C 26.96 . 1 1101 100 LEU HG H 1.47 . 1 1102 100 LEU HD1 H 0.39 . 2 1103 100 LEU HD2 H 0.58 . 2 1104 100 LEU CD1 C 25.46 . 1 1105 100 LEU CD2 C 23.86 . 1 1106 100 LEU C C 176.29 . 1 1107 101 ALA N N 122.60 . 1 1108 101 ALA H H 8.95 . 1 1109 101 ALA CA C 51.16 . 1 1110 101 ALA HA H 5.28 . 1 1111 101 ALA HB H 1.18 . 1 1112 101 ALA CB C 25.26 . 1 1113 101 ALA C C 172.89 . 1 1114 102 GLU N N 123.40 . 1 1115 102 GLU H H 8.59 . 1 1116 102 GLU CA C 53.56 . 1 1117 102 GLU HA H 3.56 . 1 1118 102 GLU CB C 32.46 . 1 1119 102 GLU HB2 H 1.51 . 1 1120 102 GLU HB3 H 1.51 . 1 1121 102 GLU CG C 35.76 . 1 1122 102 GLU HG2 H 1.97 . 2 1123 102 GLU HG3 H 1.31 . 2 1124 102 GLU C C 178.29 . 1 1125 103 VAL N N 119.50 . 1 1126 103 VAL H H 7.99 . 1 1127 103 VAL CA C 60.96 . 1 1128 103 VAL HA H 4.51 . 1 1129 103 VAL CB C 31.66 . 1 1130 103 VAL HB H 2.15 . 1 1131 103 VAL HG1 H 0.93 . 2 1132 103 VAL HG2 H 0.82 . 2 1133 103 VAL CG1 C 23.16 . 1 1134 103 VAL CG2 C 20.26 . 1 1135 103 VAL C C 175.89 . 1 1136 104 LYS N N 123.60 . 1 1137 104 LYS H H 8.00 . 1 1138 104 LYS CA C 58.36 . 1 1139 104 LYS HA H 3.89 . 1 1140 104 LYS CB C 32.96 . 1 1141 104 LYS HB2 H 1.70 . 2 1142 104 LYS HB3 H 1.48 . 2 1143 104 LYS CG C 29.16 . 1 1144 104 LYS HG2 H 1.51 . 1 1145 104 LYS HG3 H 1.51 . 1 1146 104 LYS CD C 26.06 . 1 1147 104 LYS HD2 H 1.24 . 2 1148 104 LYS HD3 H 1.08 . 2 1149 104 LYS CE C 42.06 . 1 1150 104 LYS HE2 H 2.68 . 1 1151 104 LYS HE3 H 2.68 . 1 1152 104 LYS C C 176.49 . 1 1153 105 ASP N N 118.40 . 1 1154 105 ASP H H 8.20 . 1 1155 105 ASP CA C 52.16 . 1 1156 105 ASP HA H 4.68 . 1 1157 105 ASP CB C 41.96 . 1 1158 105 ASP HB2 H 2.62 . 2 1159 105 ASP HB3 H 2.33 . 2 1160 105 ASP C C 174.69 . 1 1161 106 TYR N N 125.90 . 1 1162 106 TYR H H 8.43 . 1 1163 106 TYR CA C 61.56 . 1 1164 106 TYR HA H 3.37 . 1 1165 106 TYR CB C 39.76 . 1 1166 106 TYR HB2 H 2.98 . 2 1167 106 TYR HB3 H 2.66 . 2 1168 106 TYR HD1 H 6.79 . 1 1169 106 TYR HD2 H 6.79 . 1 1170 106 TYR HE1 H 6.44 . 1 1171 106 TYR HE2 H 6.44 . 1 1172 106 TYR CD1 C 133.76 . 1 1173 106 TYR CE1 C 118.16 . 1 1174 106 TYR C C 175.29 . 1 1175 107 ASP N N 113.40 . 1 1176 107 ASP H H 7.95 . 1 1177 107 ASP CA C 53.06 . 1 1178 107 ASP HA H 4.54 . 1 1179 107 ASP CB C 40.76 . 1 1180 107 ASP HB2 H 2.78 . 2 1181 107 ASP HB3 H 2.38 . 2 1182 107 ASP C C 175.49 . 1 1183 108 VAL N N 120.90 . 1 1184 108 VAL H H 7.23 . 1 1185 108 VAL CA C 61.96 . 1 1186 108 VAL HA H 3.75 . 1 1187 108 VAL CB C 31.36 . 1 1188 108 VAL HB H 2.48 . 1 1189 108 VAL HG1 H 0.92 . 2 1190 108 VAL HG2 H 0.93 . 2 1191 108 VAL CG1 C 19.46 . 1 1192 108 VAL CG2 C 22.36 . 1 1193 108 VAL C C 173.39 . 1 1194 109 GLU N N 127.10 . 1 1195 109 GLU H H 8.28 . 1 1196 109 GLU CA C 56.26 . 1 1197 109 GLU HA H 4.08 . 1 1198 109 GLU CB C 30.16 . 1 1199 109 GLU HB2 H 1.84 . 1 1200 109 GLU HB3 H 1.84 . 1 1201 109 GLU CG C 36.36 . 1 1202 109 GLU HG2 H 2.20 . 2 1203 109 GLU HG3 H 1.95 . 2 1204 109 GLU C C 174.99 . 1 1205 110 ILE N N 126.40 . 1 1206 110 ILE H H 8.01 . 1 1207 110 ILE CA C 57.86 . 1 1208 110 ILE HA H 4.17 . 1 1209 110 ILE CB C 35.96 . 1 1210 110 ILE HB H 0.84 . 1 1211 110 ILE HG2 H 0.02 . 1 1212 110 ILE CG2 C 16.96 . 1 1213 110 ILE CG1 C 26.66 . 1 1214 110 ILE HG12 H 1.27 . 2 1215 110 ILE HG13 H 0.57 . 2 1216 110 ILE HD1 H 0.42 . 1 1217 110 ILE CD1 C 11.46 . 1 1218 110 ILE C C 175.79 . 1 1219 111 ARG N N 128.10 . 1 1220 111 ARG H H 7.63 . 1 1221 111 ARG CA C 54.46 . 1 1222 111 ARG HA H 4.37 . 1 1223 111 ARG CB C 31.96 . 1 1224 111 ARG HB2 H 1.55 . 2 1225 111 ARG HB3 H 1.44 . 2 1226 111 ARG CG C 26.96 . 1 1227 111 ARG HG2 H 1.47 . 2 1228 111 ARG HG3 H 1.38 . 2 1229 111 ARG CD C 43.46 . 1 1230 111 ARG HD2 H 3.15 . 2 1231 111 ARG HD3 H 3.07 . 2 1232 111 ARG C C 174.49 . 1 1233 112 LEU N N 122.90 . 1 1234 112 LEU H H 8.35 . 1 1235 112 LEU CA C 54.16 . 1 1236 112 LEU HA H 4.58 . 1 1237 112 LEU CB C 42.96 . 1 1238 112 LEU HB2 H 1.65 . 1 1239 112 LEU HB3 H 1.65 . 1 1240 112 LEU CG C 26.66 . 1 1241 112 LEU HG H 1.67 . 1 1242 112 LEU HD1 H 0.71 . 2 1243 112 LEU HD2 H 0.72 . 2 1244 112 LEU CD1 C 25.46 . 1 1245 112 LEU CD2 C 23.66 . 1 1246 113 SER N N 118.60 . 1 1247 113 SER H H 8.73 . 1 1248 113 SER CA C 56.86 . 1 1249 113 SER HA H 4.77 . 1 1250 113 SER CB C 66.26 . 1 1251 113 SER HB2 H 4.26 . 2 1252 113 SER HB3 H 4.14 . 2 1253 113 SER C C 174.89 . 1 1254 114 HIS N N 114.40 . 1 1255 114 HIS H H 8.56 . 1 1256 114 HIS CA C 57.76 . 1 1257 114 HIS HA H 4.36 . 1 1258 114 HIS CB C 28.76 . 1 1259 114 HIS HB2 H 3.19 . 2 1260 114 HIS HB3 H 3.13 . 2 1261 114 HIS CD2 C 119.76 . 1 1262 114 HIS CE1 C 137.76 . 1 1263 114 HIS HD2 H 7.18 . 1 1264 114 HIS HE1 H 8.16 . 1 1265 114 HIS C C 176.19 . 1 1266 115 GLU N N 117.90 . 1 1267 115 GLU H H 7.74 . 1 1268 115 GLU CA C 57.66 . 1 1269 115 GLU HA H 3.79 . 1 1270 115 GLU CB C 29.86 . 1 1271 115 GLU HB2 H 1.50 . 1 1272 115 GLU HB3 H 1.50 . 1 1273 115 GLU CG C 36.06 . 1 1274 115 GLU HG2 H 1.90 . 2 1275 115 GLU HG3 H 1.85 . 2 1276 115 GLU C C 176.09 . 1 1277 116 HIS N N 116.20 . 1 1278 116 HIS H H 7.69 . 1 1279 116 HIS CA C 56.86 . 1 1280 116 HIS HA H 5.16 . 1 1281 116 HIS CB C 33.46 . 1 1282 116 HIS HB2 H 3.02 . 2 1283 116 HIS HB3 H 2.91 . 2 1284 116 HIS CD2 C 117.76 . 1 1285 116 HIS CE1 C 137.06 . 1 1286 116 HIS HD2 H 6.22 . 1 1287 116 HIS HE1 H 7.58 . 1 1288 116 HIS C C 172.89 . 1 1289 117 GLN N N 112.50 . 1 1290 117 GLN H H 8.55 . 1 1291 117 GLN CA C 53.66 . 1 1292 117 GLN HA H 4.64 . 1 1293 117 GLN HB2 H 1.73 . 2 1294 117 GLN HB3 H 1.60 . 2 1295 117 GLN HG2 H 1.99 . 2 1296 117 GLN HG3 H 1.77 . 2 1297 117 GLN C C 174.69 . 1 1298 118 ALA N N 121.40 . 1 1299 118 ALA H H 7.45 . 1 1300 118 ALA CA C 51.56 . 1 1301 118 ALA HA H 4.47 . 1 1302 118 ALA HB H 1.33 . 1 1303 118 ALA CB C 22.26 . 1 1304 118 ALA C C 174.79 . 1 1305 119 TYR N N 115.40 . 1 1306 119 TYR H H 8.30 . 1 1307 119 TYR CA C 56.06 . 1 1308 119 TYR HA H 5.80 . 1 1309 119 TYR CB C 42.16 . 1 1310 119 TYR HB2 H 2.74 . 2 1311 119 TYR HB3 H 2.66 . 2 1312 119 TYR HD1 H 6.51 . 1 1313 119 TYR HD2 H 6.51 . 1 1314 119 TYR HE1 H 6.82 . 1 1315 119 TYR HE2 H 6.82 . 1 1316 119 TYR CD1 C 133.16 . 1 1317 119 TYR CE1 C 118.66 . 1 1318 119 TYR C C 173.29 . 1 1319 120 ARG N N 119.30 . 1 1320 120 ARG H H 8.97 . 1 1321 120 ARG CA C 55.46 . 1 1322 120 ARG HA H 4.32 . 1 1323 120 ARG CB C 36.06 . 1 1324 120 ARG HB2 H 1.55 . 2 1325 120 ARG HB3 H 1.13 . 2 1326 120 ARG CG C 28.06 . 1 1327 120 ARG HG2 H 1.55 . 1 1328 120 ARG HG3 H 1.55 . 1 1329 120 ARG CD C 43.26 . 1 1330 120 ARG HD2 H 2.87 . 2 1331 120 ARG HD3 H 2.68 . 2 1332 120 ARG C C 173.59 . 1 1333 121 TRP N N 121.70 . 1 1334 121 TRP H H 8.40 . 1 1335 121 TRP CA C 55.76 . 1 1336 121 TRP HA H 5.24 . 1 1337 121 TRP CB C 30.66 . 1 1338 121 TRP HB2 H 2.86 . 1 1339 121 TRP HB3 H 2.86 . 1 1340 121 TRP CD1 C 128.66 . 1 1341 121 TRP CE3 C 120.16 . 1 1342 121 TRP NE1 N 128.60 . 1 1343 121 TRP HD1 H 7.26 . 1 1344 121 TRP HE3 H 6.97 . 1 1345 121 TRP CZ3 C 121.96 . 1 1346 121 TRP CZ2 C 113.96 . 1 1347 121 TRP HE1 H 9.75 . 1 1348 121 TRP HZ3 H 6.69 . 1 1349 121 TRP CH2 C 122.36 . 1 1350 121 TRP HZ2 H 7.01 . 1 1351 121 TRP HH2 H 6.61 . 1 1352 121 TRP C C 177.49 . 1 1353 122 LEU N N 124.30 . 1 1354 122 LEU H H 9.40 . 1 1355 122 LEU CA C 53.76 . 1 1356 122 LEU HA H 4.84 . 1 1357 122 LEU CB C 47.46 . 1 1358 122 LEU HB2 H 1.54 . 1 1359 122 LEU HB3 H 1.54 . 1 1360 122 LEU CG C 29.76 . 1 1361 122 LEU HG H 1.22 . 1 1362 122 LEU HD1 H 0.41 . 2 1363 122 LEU HD2 H 0.57 . 2 1364 122 LEU CD1 C 27.86 . 1 1365 122 LEU CD2 C 24.16 . 1 1366 122 LEU C C 176.79 . 1 1367 123 GLY N N 108.90 . 1 1368 123 GLY H H 9.00 . 1 1369 123 GLY CA C 44.56 . 1 1370 123 GLY HA2 H 4.49 . 2 1371 123 GLY HA3 H 3.89 . 2 1372 123 GLY C C 172.89 . 1 1373 124 LEU N N 118.10 . 1 1374 124 LEU H H 8.94 . 1 1375 124 LEU CA C 59.36 . 1 1376 124 LEU HA H 3.84 . 1 1377 124 LEU CB C 41.56 . 1 1378 124 LEU HB2 H 1.49 . 2 1379 124 LEU HB3 H 1.21 . 2 1380 124 LEU HD1 H 0.44 . 2 1381 124 LEU HD2 H 0.37 . 2 1382 124 LEU CD1 C 23.76 . 1 1383 124 LEU CD2 C 24.86 . 1 1384 124 LEU C C 177.89 . 1 1385 125 GLU N N 116.80 . 1 1386 125 GLU H H 8.71 . 1 1387 125 GLU CA C 60.26 . 1 1388 125 GLU HA H 3.77 . 1 1389 125 GLU CB C 28.76 . 1 1390 125 GLU HB2 H 1.91 . 2 1391 125 GLU HB3 H 1.86 . 2 1392 125 GLU CG C 36.06 . 1 1393 125 GLU HG2 H 2.14 . 1 1394 125 GLU HG3 H 2.14 . 1 1395 125 GLU C C 179.69 . 1 1396 126 GLU N N 120.30 . 1 1397 126 GLU H H 8.37 . 1 1398 126 GLU CA C 59.36 . 1 1399 126 GLU HA H 3.82 . 1 1400 126 GLU CB C 29.76 . 1 1401 126 GLU HB2 H 1.89 . 2 1402 126 GLU HB3 H 1.79 . 2 1403 126 GLU CG C 37.36 . 1 1404 126 GLU HG2 H 2.18 . 2 1405 126 GLU HG3 H 2.15 . 2 1406 126 GLU C C 178.59 . 1 1407 127 ALA N N 121.60 . 1 1408 127 ALA H H 9.18 . 1 1409 127 ALA CA C 54.96 . 1 1410 127 ALA HA H 3.63 . 1 1411 127 ALA HB H 1.28 . 1 1412 127 ALA CB C 17.66 . 1 1413 127 ALA C C 179.19 . 1 1414 128 CYS N N 114.00 . 1 1415 128 CYS H H 8.33 . 1 1416 128 CYS CA C 64.96 . 1 1417 128 CYS HA H 3.65 . 1 1418 128 CYS CB C 26.86 . 1 1419 128 CYS HB2 H 3.04 . 2 1420 128 CYS HB3 H 2.38 . 2 1421 128 CYS C C 176.09 . 1 1422 129 GLN N N 117.70 . 1 1423 129 GLN H H 7.49 . 1 1424 129 GLN CA C 58.36 . 1 1425 129 GLN HA H 3.74 . 1 1426 129 GLN CB C 27.96 . 1 1427 129 GLN HB2 H 1.96 . 2 1428 129 GLN CG C 33.36 . 1 1429 129 GLN HG2 H 2.30 . 2 1430 129 GLN HG3 H 2.23 . 2 1431 129 GLN NE2 N 111.70 . 1 1432 129 GLN HE21 H 7.38 . 2 1433 129 GLN HE22 H 6.66 . 2 1434 129 GLN C C 178.99 . 1 1435 130 LEU N N 118.00 . 1 1436 130 LEU H H 7.61 . 1 1437 130 LEU CA C 56.66 . 1 1438 130 LEU HA H 3.76 . 1 1439 130 LEU CB C 40.86 . 1 1440 130 LEU HB2 H 0.92 . 2 1441 130 LEU HB3 H 0.55 . 2 1442 130 LEU CG C 26.46 . 1 1443 130 LEU HG H 0.91 . 1 1444 130 LEU HD1 H -0.26 . 2 1445 130 LEU HD2 H -0.16 . 2 1446 130 LEU CD1 C 23.96 . 1 1447 130 LEU CD2 C 22.76 . 1 1448 130 LEU C C 178.59 . 1 1449 131 ALA N N 120.00 . 1 1450 131 ALA H H 8.28 . 1 1451 131 ALA CA C 54.66 . 1 1452 131 ALA HA H 4.17 . 1 1453 131 ALA HB H 1.22 . 1 1454 131 ALA CB C 18.36 . 1 1455 131 ALA C C 180.99 . 1 1456 132 GLN N N 110.20 . 1 1457 132 GLN H H 7.31 . 1 1458 132 GLN CA C 61.86 . 1 1459 132 GLN HA H 3.51 . 1 1460 132 GLN CB C 28.36 . 1 1461 132 GLN HB2 H 1.68 . 1 1462 132 GLN HB3 H 1.68 . 1 1463 132 GLN CG C 33.66 . 1 1464 132 GLN HG2 H 1.87 . 2 1465 132 GLN HG3 H 1.61 . 2 1466 132 GLN NE2 N 111.20 . 1 1467 132 GLN HE21 H 7.20 . 2 1468 132 GLN HE22 H 6.42 . 2 1469 132 GLN C C 175.49 . 1 1470 133 PHE N N 124.10 . 1 1471 133 PHE H H 9.21 . 1 1472 133 PHE CA C 58.46 . 1 1473 133 PHE HA H 4.30 . 1 1474 133 PHE CB C 40.46 . 1 1475 133 PHE HB2 H 3.31 . 2 1476 133 PHE HB3 H 2.38 . 2 1477 133 PHE HD1 H 6.93 . 1 1478 133 PHE HD2 H 6.93 . 1 1479 133 PHE HE1 H 6.59 . 1 1480 133 PHE HE2 H 6.59 . 1 1481 133 PHE CD1 C 131.36 . 1 1482 133 PHE CE1 C 129.76 . 1 1483 133 PHE C C 178.19 . 1 1484 134 LYS N N 125.50 . 1 1485 134 LYS H H 9.28 . 1 1486 134 LYS CA C 60.46 . 1 1487 134 LYS HA H 3.79 . 1 1488 134 LYS CB C 32.76 . 1 1489 134 LYS HB2 H 2.01 . 2 1490 134 LYS HB3 H 1.86 . 2 1491 134 LYS CG C 24.46 . 1 1492 134 LYS HG2 H 1.46 . 1 1493 134 LYS HG3 H 1.46 . 1 1494 134 LYS CD C 29.36 . 1 1495 134 LYS HD2 H 1.71 . 1 1496 134 LYS HD3 H 1.71 . 1 1497 134 LYS CE C 41.86 . 1 1498 134 LYS HE2 H 2.99 . 1 1499 134 LYS HE3 H 2.99 . 1 1500 134 LYS C C 178.79 . 1 1501 135 GLU N N 117.10 . 1 1502 135 GLU H H 9.68 . 1 1503 135 GLU CA C 59.86 . 1 1504 135 GLU HA H 4.25 . 1 1505 135 GLU CB C 29.56 . 1 1506 135 GLU HB2 H 2.17 . 2 1507 135 GLU HB3 H 2.08 . 2 1508 135 GLU CG C 37.26 . 1 1509 135 GLU HG2 H 2.61 . 2 1510 135 GLU HG3 H 2.54 . 2 1511 135 GLU C C 178.79 . 1 1512 136 MET N N 117.70 . 1 1513 136 MET H H 7.08 . 1 1514 136 MET CA C 55.86 . 1 1515 136 MET HA H 4.63 . 1 1516 136 MET CB C 37.56 . 1 1517 136 MET HB2 H 1.99 . 1 1518 136 MET HB3 H 1.99 . 1 1519 136 MET CG C 32.06 . 1 1520 136 MET HG2 H 3.44 . 2 1521 136 MET HG3 H 1.95 . 2 1522 136 MET HE H 1.65 . 1 1523 136 MET CE C 19.16 . 1 1524 136 MET C C 177.59 . 1 1525 137 LYS N N 117.40 . 1 1526 137 LYS H H 8.04 . 1 1527 137 LYS CA C 60.46 . 1 1528 137 LYS HA H 3.79 . 1 1529 137 LYS CB C 32.36 . 1 1530 137 LYS HB2 H 1.78 . 2 1531 137 LYS HB3 H 1.63 . 2 1532 137 LYS CG C 25.46 . 1 1533 137 LYS HG2 H 1.39 . 2 1534 137 LYS HG3 H 1.25 . 2 1535 137 LYS CD C 30.06 . 1 1536 137 LYS HD3 H 1.42 . 2 1537 137 LYS CE C 41.26 . 1 1538 137 LYS HE2 H 2.67 . 1 1539 137 LYS HE3 H 2.67 . 1 1540 137 LYS C C 177.99 . 1 1541 138 ALA N N 118.00 . 1 1542 138 ALA H H 7.84 . 1 1543 138 ALA CA C 54.96 . 1 1544 138 ALA HA H 4.05 . 1 1545 138 ALA HB H 1.41 . 1 1546 138 ALA CB C 17.96 . 1 1547 138 ALA C C 178.89 . 1 1548 139 ALA N N 118.70 . 1 1549 139 ALA H H 7.43 . 1 1550 139 ALA CA C 55.86 . 1 1551 139 ALA HA H 3.92 . 1 1552 139 ALA HB H 1.33 . 1 1553 139 ALA CB C 17.96 . 1 1554 139 ALA C C 179.39 . 1 1555 140 LEU N N 115.70 . 1 1556 140 LEU H H 7.66 . 1 1557 140 LEU CA C 57.96 . 1 1558 140 LEU HA H 3.41 . 1 1559 140 LEU CB C 41.36 . 1 1560 140 LEU HB2 H 1.75 . 2 1561 140 LEU HB3 H 0.38 . 2 1562 140 LEU CG C 26.26 . 1 1563 140 LEU HG H 1.44 . 1 1564 140 LEU HD1 H 0.36 . 2 1565 140 LEU HD2 H -0.09 . 2 1566 140 LEU CD1 C 25.86 . 1 1567 140 LEU CD2 C 21.76 . 1 1568 140 LEU C C 178.49 . 1 1569 141 GLN N N 117.50 . 1 1570 141 GLN H H 8.28 . 1 1571 141 GLN CA C 59.56 . 1 1572 141 GLN HA H 3.72 . 1 1573 141 GLN CB C 27.96 . 1 1574 141 GLN HB2 H 2.16 . 2 1575 141 GLN HB3 H 2.04 . 2 1576 141 GLN CG C 34.26 . 1 1577 141 GLN HG2 H 2.50 . 2 1578 141 GLN HG3 H 2.23 . 2 1579 141 GLN NE2 N 111.00 . 1 1580 141 GLN HE21 H 6.95 . 2 1581 141 GLN HE22 H 6.77 . 2 1582 141 GLN C C 179.49 . 1 1583 142 GLU N N 119.60 . 1 1584 142 GLU H H 9.01 . 1 1585 142 GLU CA C 59.16 . 1 1586 142 GLU HA H 4.04 . 1 1587 142 GLU CB C 29.06 . 1 1588 142 GLU HB2 H 2.18 . 1 1589 142 GLU HB3 H 2.18 . 1 1590 142 GLU CG C 36.86 . 1 1591 142 GLU HG2 H 2.62 . 2 1592 142 GLU HG3 H 2.36 . 2 1593 142 GLU C C 180.49 . 1 1594 143 GLY N N 110.90 . 1 1595 143 GLY H H 8.80 . 1 1596 143 GLY CA C 47.26 . 1 1597 143 GLY HA2 H 2.93 . 1 1598 143 GLY HA3 H 2.93 . 1 1599 143 GLY C C 173.79 . 1 1600 144 HIS N N 121.40 . 1 1601 144 HIS H H 8.70 . 1 1602 144 HIS CA C 62.36 . 1 1603 144 HIS HA H 3.81 . 1 1604 144 HIS CB C 31.26 . 1 1605 144 HIS HB2 H 3.23 . 1 1606 144 HIS HB3 H 3.23 . 1 1607 144 HIS CD2 C 120.26 . 1 1608 144 HIS CE1 C 139.76 . 1 1609 144 HIS HD2 H 6.88 . 1 1610 144 HIS C C 177.19 . 1 1611 145 GLN N N 117.80 . 1 1612 145 GLN H H 8.37 . 1 1613 145 GLN CA C 58.96 . 1 1614 145 GLN HA H 3.90 . 1 1615 145 GLN CB C 28.16 . 1 1616 145 GLN HB2 H 2.23 . 2 1617 145 GLN HB3 H 2.12 . 2 1618 145 GLN CG C 33.66 . 1 1619 145 GLN HG2 H 2.49 . 2 1620 145 GLN HG3 H 2.40 . 2 1621 145 GLN C C 178.79 . 1 1622 146 PHE N N 121.10 . 1 1623 146 PHE H H 8.24 . 1 1624 146 PHE CA C 61.56 . 1 1625 146 PHE HA H 4.02 . 1 1626 146 PHE CB C 39.26 . 1 1627 146 PHE HB2 H 3.18 . 2 1628 146 PHE HB3 H 2.92 . 2 1629 146 PHE HD1 H 6.95 . 1 1630 146 PHE HD2 H 6.95 . 1 1631 146 PHE HE1 H 7.12 . 1 1632 146 PHE HE2 H 7.12 . 1 1633 146 PHE CD1 C 131.66 . 1 1634 146 PHE CE1 C 131.86 . 1 1635 146 PHE CZ C 130.76 . 1 1636 146 PHE HZ H 7.43 . 1 1637 146 PHE C C 178.49 . 1 1638 147 LEU N N 118.70 . 1 1639 147 LEU H H 8.02 . 1 1640 147 LEU CA C 56.96 . 1 1641 147 LEU HA H 3.71 . 1 1642 147 LEU CB C 41.96 . 1 1643 147 LEU HB2 H 1.61 . 2 1644 147 LEU HB3 H 0.89 . 2 1645 147 LEU CG C 25.86 . 1 1646 147 LEU HG H 1.64 . 1 1647 147 LEU HD1 H -0.31 . 2 1648 147 LEU HD2 H 0.55 . 2 1649 147 LEU CD1 C 23.66 . 1 1650 147 LEU CD2 C 23.36 . 1 1651 147 LEU C C 179.69 . 1 1652 148 CYS N N 115.40 . 1 1653 148 CYS H H 7.73 . 1 1654 148 CYS CA C 61.86 . 1 1655 148 CYS HA H 4.07 . 1 1656 148 CYS CB C 27.16 . 1 1657 148 CYS HB2 H 2.72 . 1 1658 148 CYS HB3 H 2.72 . 1 1659 148 CYS C C 175.39 . 1 1660 149 SER N N 114.80 . 1 1661 149 SER H H 7.60 . 1 1662 149 SER CA C 59.16 . 1 1663 149 SER HA H 4.26 . 1 1664 149 SER CB C 63.76 . 1 1665 149 SER HB2 H 3.77 . 1 1666 149 SER HB3 H 3.77 . 1 1667 149 SER C C 174.29 . 1 1668 150 ILE N N 119.80 . 1 1669 150 ILE H H 7.13 . 1 1670 150 ILE CA C 61.66 . 1 1671 150 ILE HA H 3.94 . 1 1672 150 ILE CB C 38.46 . 1 1673 150 ILE HB H 1.69 . 1 1674 150 ILE HG2 H 0.65 . 1 1675 150 ILE CG2 C 17.16 . 1 1676 150 ILE CG1 C 26.66 . 1 1677 150 ILE HG12 H 1.25 . 2 1678 150 ILE HG13 H 0.90 . 2 1679 150 ILE HD1 H 0.69 . 1 1680 150 ILE CD1 C 13.66 . 1 1681 150 ILE C C 176.09 . 1 1682 151 GLU N N 124.40 . 1 1683 151 GLU H H 7.96 . 1 1684 151 GLU CA C 56.26 . 1 1685 151 GLU HA H 4.16 . 1 1686 151 GLU CB C 35.96 . 1 1687 151 GLU HB2 H 2.19 . 2 1688 151 GLU HB3 H 2.13 . 2 1689 151 GLU CG C 30.26 . 1 1690 151 GLU HG2 H 1.96 . 2 1691 151 GLU HG3 H 1.80 . 2 1692 151 GLU C C 174.99 . 1 1693 152 ALA N N 130.90 . 1 1694 152 ALA H H 7.83 . 1 1695 152 ALA CA C 53.76 . 1 1696 152 ALA HA H 4.01 . 1 1697 152 ALA HB H 1.25 . 1 1698 152 ALA CB C 20.06 . 1 1699 152 ALA C C 176.09 . 1 1700 153 LEU N N 124.60 . 1 1701 153 LEU H H 8.00 . 1 1702 153 LEU CA C 56.36 . 1 1703 153 LEU HA H 4.53 . 1 1704 153 LEU CB C 40.26 . 1 1705 153 LEU HB2 H 1.59 . 1 1706 153 LEU HB3 H 1.59 . 1 1707 153 LEU HD1 H 0.74 . 2 1708 153 LEU CD1 C 16.86 . 1 stop_ save_ ####################################### # Cited references within the entry # ####################################### save_citation _Saveframe_category citation _Citation_title ; Structure and substrate-binding mechanism of human AP4A hydrolase ; _Citation_type journal _PubMed_ID 15596429 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Swarbrick James D. . 2 Buyya S. . . 3 Gunawardana D. . . 4 Gayler K. R. . 5 McLennan A. G. . 6 Gooley Paul R. . stop_ _Journal_abbreviation "J. Biol. Chem." _Journal_volume 280 _Journal_issue 9 _Page_first 8471 _Page_last 8481 _Year 2005 save_