data_5766 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Solution Structure of the Lyase Domain of Human DNA Polymerase Lambda ; _BMRB_accession_number 5766 _BMRB_flat_file_name bmr5766.str _Entry_type original _Submission_date 2003-04-11 _Accession_date 2003-04-11 _Entry_origination author _NMR_STAR_version 2.1.1 _Experimental_method NMR _Details . loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 DeRose E. F. . 2 Kirby T. W. . 3 Mueller G. A. . 4 Bebenek K. . . 5 Garcia-Diaz M. . . 6 Blanco L. . . 7 Kunkel T. A. . 8 London R. E. . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 358 "13C chemical shifts" 328 "15N chemical shifts" 76 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2003-09-08 original author . stop_ _Original_release_date 2003-09-08 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title 'Solution Structure of the Lyase Domain of Human DNA Polymerase Lambda' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 12911298 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 DeRose E. F. . 2 Kirby T. W. . 3 Mueller G. A. . 4 Bebenek K. . . 5 Garcia-Diaz M. . . 6 Blanco L. . . 7 Kunkel T. A. . 8 London R. E. . stop_ _Journal_abbreviation Biochemistry _Journal_volume 42 _Journal_issue 32 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 9564 _Page_last 9574 _Year 2003 _Details . loop_ _Keyword 'DNA POLYMERASE LAMBDA' 'POL LAMBDA' 'LYASE DOMAIN' '8 kDa DOMAIN' 'POL BETA-LIKE' stop_ save_ ################################## # Molecular system description # ################################## save_system_lambda _Saveframe_category molecular_system _Mol_system_name 'DNA polymerase lambda (E.C.2.7.7.7)' _Abbreviation_common 'DNA polymerase lambda (E.C.2.7.7.7)' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label '50S Ribosomal Protein L18' $L18 stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state monomer _System_paramagnetic no _System_thiol_state 'all free' _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_L18 _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common '50S Ribosomal Protein L18' _Abbreviation_common '50S Ribosomal Protein L18' _Molecular_mass . _Mol_thiol_state 'all free' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 87 _Mol_residue_sequence ; MAQPSSQKATNHNLHITEKL EVLAKAYSVQGDKWRALGYA KAINALKSFHKPVTSYQEAC SIPGIGKRMAEKIIEILESG HLRKLDH ; loop_ _Residue_seq_code _Residue_label 1 MET 2 ALA 3 GLN 4 PRO 5 SER 6 SER 7 GLN 8 LYS 9 ALA 10 THR 11 ASN 12 HIS 13 ASN 14 LEU 15 HIS 16 ILE 17 THR 18 GLU 19 LYS 20 LEU 21 GLU 22 VAL 23 LEU 24 ALA 25 LYS 26 ALA 27 TYR 28 SER 29 VAL 30 GLN 31 GLY 32 ASP 33 LYS 34 TRP 35 ARG 36 ALA 37 LEU 38 GLY 39 TYR 40 ALA 41 LYS 42 ALA 43 ILE 44 ASN 45 ALA 46 LEU 47 LYS 48 SER 49 PHE 50 HIS 51 LYS 52 PRO 53 VAL 54 THR 55 SER 56 TYR 57 GLN 58 GLU 59 ALA 60 CYS 61 SER 62 ILE 63 PRO 64 GLY 65 ILE 66 GLY 67 LYS 68 ARG 69 MET 70 ALA 71 GLU 72 LYS 73 ILE 74 ILE 75 GLU 76 ILE 77 LEU 78 GLU 79 SER 80 GLY 81 HIS 82 LEU 83 ARG 84 LYS 85 LEU 86 ASP 87 HIS stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-01-28 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 1NZP "Solution Structure Of The Lyase Domain Of Human Dna Polymerase Lambda" 100.00 87 100.00 100.00 1.87e-56 PDB 1RZT "Crystal Structure Of Dna Polymerase Lambda Complexed With A Two Nucleotide Gap Dna Molecule" 95.40 331 100.00 100.00 4.46e-50 PDB 1XSL "Crystal Structure Of Human Dna Polymerase Lambda In Complex With A One Nucleotide Dna Gap" 100.00 335 100.00 100.00 1.57e-53 PDB 1XSN "Crystal Structure Of Human Dna Polymerase Lambda In Complex With A One Nucleotide Dna Gap And Ddttp" 100.00 335 100.00 100.00 1.40e-53 PDB 1XSP "Crystal Structure Of Human Dna Polymerase Lambda In Complex With Nicked Dna And Pyrophosphate" 100.00 335 100.00 100.00 1.40e-53 PDB 2BCQ "Dna Polymerase Lambda In Complex With A Dna Duplex Containing An Unpaired Dtmp" 100.00 335 100.00 100.00 1.57e-53 PDB 2BCR "Dna Polymerase Lambda In Complex With A Dna Duplex Containing An Unpaired Damp" 100.00 335 100.00 100.00 1.57e-53 PDB 2BCS "Dna Polymerase Lambda In Complex With A Dna Duplex Containing An Unpaired Dcmp" 100.00 335 100.00 100.00 1.57e-53 PDB 2BCU "Dna Polymerase Lambda In Complex With A Dna Duplex Containing An Unpaired Damp And A T:t Mismatch" 100.00 335 100.00 100.00 1.57e-53 PDB 2BCV "Dna Polymerase Lambda In Complex With Dttp And A Dna Duplex Containing An Unpaired Dtmp" 100.00 335 100.00 100.00 1.57e-53 PDB 2GWS "Crystal Structure Of Human Dna Polymerase Lambda With A GG MISMATCH In The Primer Terminus" 100.00 335 100.00 100.00 1.57e-53 PDB 2PFN "Na In The Active Site Of Dna Polymerase Lambda" 100.00 335 100.00 100.00 1.40e-53 PDB 2PFO "Dna Polymerase Lambda In Complex With Dna And Dupnpp" 100.00 335 100.00 100.00 1.40e-53 PDB 2PFP "Dna Polymerase Lambda In Complex With Dna And Dctp" 100.00 335 100.00 100.00 1.40e-53 PDB 2PFQ "Manganese Promotes Catalysis In A Dna Polymerase Lambda-Dna Crystal" 100.00 335 100.00 100.00 1.40e-53 PDB 3C5F "Structure Of A Binary Complex Of The R517a Pol Lambda Mutant" 100.00 335 100.00 100.00 1.44e-53 PDB 3C5G "Structure Of A Ternary Complex Of The R517k Pol Lambda Mutant" 100.00 335 100.00 100.00 1.44e-53 PDB 3HW8 "Ternary Complex Of Dna Polymerase Lambda Of A Two Nucleotide Gapped Dna Substrate With A C In The Scrunch Site" 100.00 335 100.00 100.00 1.40e-53 PDB 3HWT "Ternary Complex Of Dna Polymerase Lambda Bound To A Two Nucleotide Gapped Dna Substrate With A Scrunched Da" 100.00 335 100.00 100.00 1.40e-53 PDB 3HX0 "Ternary Complex Of L277a, H511a, R514 Mutant Pol Lambda Bound To A 2 Nucleotide Gapped Dna Substrate With A Scrunched Da" 100.00 335 98.85 98.85 7.92e-53 PDB 3MDA "Dna Polymerase Lambda In Complex With Arac" 87.36 325 100.00 100.00 3.04e-45 PDB 3MDC "Dna Polymerase Lambda In Complex With Dfdctp" 87.36 325 100.00 100.00 3.04e-45 PDB 3MGH "Binary Complex Of A Dna Polymerase Lambda Loop Mutant" 98.85 329 100.00 100.00 1.07e-52 PDB 3MGI "Ternary Complex Of A Dna Polymerase Lambda Loop Mutant" 98.85 329 100.00 100.00 1.07e-52 PDB 3PML "Crystal Structure Of A Polymerase Lambda Variant With A Dgtp Analog Opposite A Templating T" 98.85 329 100.00 100.00 1.07e-52 PDB 3PMN "Ternary Crystal Structure Of Polymerase Lambda Variant With A Gt Mispair At The Primer Terminus With Mn2+ In The Active Site" 98.85 329 100.00 100.00 1.07e-52 PDB 3PNC "Ternary Crystal Structure Of A Polymerase Lambda Variant With A Gt Mispair At The Primer Terminus And Sodium At Catalytic Metal" 98.85 329 100.00 100.00 1.07e-52 PDB 3UPQ "Crystal Structure Of The Pre-Catalytic Ternary Complex Of Polymerase Lambda With An Ratp Analog Opposite A Templating T." 98.85 329 100.00 100.00 1.07e-52 PDB 3UQ0 "Crystal Structure Of The Post-Catalytic Product Complex Of Polymerase Lambda With An Ramp At The Primer Terminus" 98.85 329 100.00 100.00 1.07e-52 PDB 3UQ2 "Crystal Structure Of The Post-Catalytic Product Complex Of Polymerase Lambda With An Rcmp Inserted Opposite A Templating G And " 98.85 329 100.00 100.00 9.75e-53 PDB 4FO6 "Crystal Structure Of The Pre-Catalytic Ternary Complex Of Polymerase Lambda With A Datp Analog Opposite A Templating T And An R" 98.85 329 100.00 100.00 9.75e-53 PDB 4K4G "Ternary Crystal Structures Of Human Dna Polymerase Lambda In Complex With Dna And L-dctp." 95.40 340 100.00 100.00 9.30e-50 PDB 4K4H "Ternary Crystal Structures Of A Human Dna Polymerase Lambda In Complex With Dna And (-)3tc-tp." 95.40 340 100.00 100.00 9.30e-50 PDB 4K4I "Ternary Crystal Structures Of A Human Dna Polymerase Lambda In Complex With Dna And (-)ftc-tp" 95.40 340 100.00 100.00 9.30e-50 DBJ BAB13852 "unnamed protein product [Homo sapiens]" 98.85 515 100.00 100.00 4.37e-51 DBJ BAB14050 "unnamed protein product [Homo sapiens]" 98.85 487 100.00 100.00 2.29e-51 DBJ BAE02437 "unnamed protein product [Macaca fascicularis]" 98.85 575 100.00 100.00 9.63e-51 DBJ BAG10573 "DNA polymerase lambda [synthetic construct]" 98.85 575 100.00 100.00 7.85e-51 DBJ BAK63678 "DNA polymerase lambda [Pan troglodytes]" 98.85 575 100.00 100.00 7.23e-51 EMBL CAB65074 "DNA polymerase lambda [Homo sapiens]" 98.85 575 100.00 100.00 7.85e-51 GB AAF27541 "DNA polymerase lambda [Homo sapiens]" 98.85 575 100.00 100.00 7.85e-51 GB AAG22519 "DNA polymerase beta2 [Homo sapiens]" 98.85 575 100.00 100.00 8.18e-51 GB AAH68529 "POLL protein [Homo sapiens]" 98.85 575 98.84 98.84 9.36e-50 GB AAM77696 "polymerase (DNA directed), lambda [Homo sapiens]" 98.85 575 100.00 100.00 7.85e-51 GB ADQ01128 "DNA polymerase lambda [Hylobates agilis]" 98.85 574 100.00 100.00 7.93e-51 REF NP_001167555 "DNA polymerase lambda isoform a [Homo sapiens]" 98.85 575 100.00 100.00 7.85e-51 REF NP_001253835 "DNA polymerase lambda [Macaca mulatta]" 98.85 575 100.00 100.00 8.97e-51 REF NP_001267179 "DNA polymerase lambda [Pan troglodytes]" 98.85 575 100.00 100.00 7.23e-51 REF NP_001270218 "DNA polymerase lambda [Macaca fascicularis]" 98.85 575 100.00 100.00 9.63e-51 REF NP_037406 "DNA polymerase lambda isoform a [Homo sapiens]" 98.85 575 100.00 100.00 7.85e-51 SP Q4R380 "RecName: Full=DNA polymerase lambda; Short=Pol Lambda [Macaca fascicularis]" 98.85 575 100.00 100.00 9.63e-51 SP Q9UGP5 "RecName: Full=DNA polymerase lambda; Short=Pol Lambda; AltName: Full=DNA polymerase beta-2; Short=Pol beta2; AltName: Full=DNA " 98.85 575 100.00 100.00 7.85e-51 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $L18 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 $L18 'recombinant technology' 'E. coli' Escherichia coli BLR(DE3) PET30A(+) stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Saveframe_category sample _Sample_type soultion _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $L18 2 mM '[U-15N; U-13C]' Tris-d11 5 mM . NaCl 100 mM . DTT 1 mM . NaN3 5 mM . H2O 90 % . D2O 10 % . stop_ save_ ############################ # Computer software used # ############################ save_VNMR _Saveframe_category software _Name VNMR _Version 6.1C loop_ _Task collection stop_ _Details 'Varian, Inc.' save_ save_NMRPipe _Saveframe_category software _Name NMRPipe _Version 2.1 loop_ _Task processing stop_ _Details 'F. Delaglio' save_ save_NMRView _Saveframe_category software _Name NMRView _Version 5.0.4 loop_ _Task 'data analysis' stop_ _Details 'B.A. Johnson' save_ save_CNS _Saveframe_category software _Name CNS _Version 1.0 loop_ _Task 'structure solution' stop_ _Details 'A.T., Brunger et al.' save_ save_ARIA _Saveframe_category software _Name ARIA _Version 1.1 loop_ _Task 'structure solution' refinement stop_ _Details 'M. Nilges' save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model INOVA _Field_strength 600 _Details . save_ ############################# # NMR applied experiments # ############################# save_3D_13C-separated_NOESY_1 _Saveframe_category NMR_applied_experiment _Experiment_name '3D 13C-separated NOESY' _Sample_label . save_ save_3D_15N-separated_NOESY_2 _Saveframe_category NMR_applied_experiment _Experiment_name '3D 15N-separated NOESY' _Sample_label . save_ save_NMR_spec_expt__0_1 _Saveframe_category NMR_applied_experiment _Experiment_name '3D 13C-separated NOESY' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_2 _Saveframe_category NMR_applied_experiment _Experiment_name '3D 15N-separated NOESY' _BMRB_pulse_sequence_accession_number . _Details . save_ ####################### # Sample conditions # ####################### save_sample_cond_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 7 . n/a temperature 298 . K 'ionic strength' 110 . mM pressure 1 . atm stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference _Saveframe_category chemical_shift_reference _Details . loop_ _Mol_common_name _Atom_type _Atom_isotope_number _Atom_group _Chem_shift_units _Chem_shift_value _Reference_method _Reference_type _External_reference_sample_geometry _External_reference_location _External_reference_axis _Indirect_shift_ratio DSS H 1 methl ppm 0.0 internal direct . . . 1.0 . N 15 . ppm . . . . . . . . C 13 . ppm . . . . . . . stop_ save_ ################################### # Assigned chemical shift lists # ################################### ################################################################### # Chemical Shift Ambiguity Index Value Definitions # # # # The values other than 1 are used for those atoms with different # # chemical shifts that cannot be assigned to stereospecific atoms # # or to specific residues or chains. # # # # Index Value Definition # # # # 1 Unique (including isolated methyl protons, # # geminal atoms, and geminal methyl # # groups with identical chemical shifts) # # (e.g. ILE HD11, HD12, HD13 protons) # # 2 Ambiguity of geminal atoms or geminal methyl # # proton groups (e.g. ASP HB2 and HB3 # # protons, LEU CD1 and CD2 carbons, or # # LEU HD11, HD12, HD13 and HD21, HD22, # # HD23 methyl protons) # # 3 Aromatic atoms on opposite sides of # # symmetrical rings (e.g. TYR HE1 and HE2 # # protons) # # 4 Intraresidue ambiguities (e.g. LYS HG and # # HD protons or TRP HZ2 and HZ3 protons) # # 5 Interresidue ambiguities (LYS 12 vs. LYS 27) # # 6 Intermolecular ambiguities (e.g. ASP 31 CA # # in monomer 1 and ASP 31 CA in monomer 2 # # of an asymmetrical homodimer, duplex # # DNA assignments, or other assignments # # that may apply to atoms in one or more # # molecule in the molecular assembly) # # 9 Ambiguous, specific ambiguity not defined # # # ################################################################### save_chemical_shift_set_1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $sample_cond_1 _Chem_shift_reference_set_label $chemical_shift_reference _Mol_system_component_name '50S Ribosomal Protein L18' _Text_data_format . _Text_data . loop_ _Atom_shift_assign_ID _Residue_author_seq_code _Residue_seq_code _Residue_label _Atom_name _Atom_type _Chem_shift_value _Chem_shift_value_error _Chem_shift_ambiguity_code 1 . 7 GLN C C 176.008 . 1 2 . 8 LYS CA C 56.351 . 1 3 . 8 LYS HA H 4.412 . 1 4 . 8 LYS CB C 33.309 . 1 5 . 8 LYS HB2 H 1.912 . 2 6 . 8 LYS CG C 24.771 . 1 7 . 8 LYS HG2 H 1.511 . 2 8 . 8 LYS CD C 29.229 . 1 9 . 8 LYS HD2 H 1.806 . 2 10 . 8 LYS CE C 42.324 . 1 11 . 8 LYS HE2 H 3.113 . 2 12 . 8 LYS C C 176.179 . 1 13 . 9 ALA N N 125.856 . 1 14 . 9 ALA H H 8.393 . 1 15 . 9 ALA CA C 52.373 . 1 16 . 9 ALA HA H 4.494 . 1 17 . 9 ALA CB C 19.529 . 1 18 . 9 ALA HB H 1.484 . 1 19 . 10 THR N N 117.364 . 1 20 . 10 THR H H 8.308 . 1 21 . 10 THR CA C 62.505 . 1 22 . 10 THR CB C 70.236 . 1 23 . 11 ASN CA C 51.856 . 1 24 . 11 ASN HA H 5.106 . 1 25 . 11 ASN CB C 38.141 . 1 26 . 11 ASN HB3 H 3.120 . 2 27 . 11 ASN HB2 H 2.921 . 2 28 . 11 ASN C C 176.087 . 1 29 . 12 HIS N N 126.684 . 1 30 . 12 HIS H H 9.383 . 1 31 . 12 HIS CA C 58.241 . 1 32 . 12 HIS HA H 4.509 . 1 33 . 12 HIS CB C 31.517 . 1 34 . 12 HIS HB3 H 3.042 . 2 35 . 12 HIS HB2 H 2.680 . 2 36 . 12 HIS C C 175.443 . 1 37 . 13 ASN N N 116.079 . 1 38 . 13 ASN H H 8.644 . 1 39 . 13 ASN CA C 53.947 . 1 40 . 13 ASN HA H 5.481 . 1 41 . 13 ASN CB C 41.988 . 1 42 . 13 ASN HB3 H 3.002 . 2 43 . 13 ASN HB2 H 2.433 . 2 44 . 13 ASN C C 175.946 . 1 45 . 14 LEU N N 124.952 . 1 46 . 14 LEU H H 7.617 . 1 47 . 14 LEU CA C 58.352 . 1 48 . 14 LEU HA H 4.557 . 1 49 . 14 LEU CB C 42.805 . 1 50 . 14 LEU HB2 H 1.871 . 2 51 . 14 LEU CG C 26.947 . 1 52 . 14 LEU HG H 1.715 . 1 53 . 14 LEU CD1 C 24.388 . 2 54 . 14 LEU HD1 H 1.057 . 4 55 . 14 LEU CD2 C 25.529 . 2 56 . 14 LEU C C 176.857 . 1 57 . 15 HIS N N 114.741 . 1 58 . 15 HIS H H 9.068 . 1 59 . 15 HIS CA C 58.579 . 1 60 . 15 HIS HA H 4.569 . 1 61 . 15 HIS CB C 29.222 . 1 62 . 15 HIS HB2 H 3.175 . 2 63 . 15 HIS CD2 C 118.388 . 1 64 . 15 HIS HD2 H 7.024 . 3 65 . 15 HIS C C 176.673 . 1 66 . 16 ILE N N 117.489 . 1 67 . 16 ILE H H 7.298 . 1 68 . 16 ILE CA C 63.280 . 1 69 . 16 ILE HA H 4.080 . 1 70 . 16 ILE CB C 40.261 . 1 71 . 16 ILE HB H 1.751 . 1 72 . 16 ILE CG1 C 27.617 . 2 73 . 16 ILE HG12 H 0.624 . 9 74 . 16 ILE CD1 C 14.503 . 1 75 . 16 ILE HD1 H 0.874 . 1 76 . 16 ILE CG2 C 19.579 . 2 77 . 16 ILE HG2 H 0.894 . 4 78 . 16 ILE C C 178.779 . 1 79 . 17 THR N N 112.459 . 1 80 . 17 THR H H 9.203 . 1 81 . 17 THR CA C 67.551 . 1 82 . 17 THR HA H 4.438 . 1 83 . 17 THR HB H 3.807 . 1 84 . 17 THR CG2 C 24.119 . 1 85 . 17 THR HG2 H 1.390 . 1 86 . 17 THR C C 176.992 . 1 87 . 18 GLU N N 121.146 . 1 88 . 18 GLU H H 8.674 . 1 89 . 18 GLU CA C 59.797 . 1 90 . 18 GLU HA H 4.260 . 1 91 . 18 GLU CB C 29.520 . 1 92 . 18 GLU HB3 H 2.253 . 2 93 . 18 GLU HB2 H 2.125 . 2 94 . 18 GLU CG C 36.737 . 1 95 . 18 GLU HG2 H 2.453 . 2 96 . 19 LYS N N 117.343 . 1 97 . 19 LYS H H 6.989 . 1 98 . 19 LYS CA C 58.284 . 1 99 . 19 LYS HA H 4.301 . 1 100 . 19 LYS CB C 32.789 . 1 101 . 19 LYS HB3 H 2.104 . 2 102 . 19 LYS HB2 H 1.997 . 2 103 . 19 LYS CG C 25.725 . 1 104 . 19 LYS HG2 H 1.639 . 2 105 . 19 LYS CD C 28.974 . 1 106 . 19 LYS HD2 H 1.797 . 2 107 . 19 LYS CE C 42.496 . 1 108 . 19 LYS HE2 H 3.148 . 2 109 . 19 LYS C C 180.163 . 1 110 . 20 LEU N N 119.049 . 1 111 . 20 LEU H H 8.175 . 1 112 . 20 LEU CA C 57.971 . 1 113 . 20 LEU CB C 42.709 . 1 114 . 20 LEU HB3 H 2.051 . 2 115 . 20 LEU HB2 H 1.962 . 2 116 . 20 LEU CG C 26.929 . 1 117 . 20 LEU HG H 1.514 . 1 118 . 20 LEU CD1 C 23.076 . 2 119 . 20 LEU HD1 H 0.845 . 4 120 . 20 LEU C C 178.851 . 1 121 . 21 GLU N N 119.181 . 1 122 . 21 GLU H H 8.707 . 1 123 . 21 GLU CA C 60.011 . 1 124 . 21 GLU HA H 4.018 . 1 125 . 21 GLU CB C 29.971 . 1 126 . 21 GLU HB3 H 2.293 . 2 127 . 21 GLU HB2 H 2.149 . 2 128 . 21 GLU CG C 37.396 . 1 129 . 21 GLU HG3 H 2.575 . 2 130 . 21 GLU HG2 H 2.403 . 2 131 . 21 GLU C C 179.122 . 1 132 . 22 VAL N N 118.919 . 1 133 . 22 VAL H H 7.105 . 1 134 . 22 VAL CA C 66.375 . 1 135 . 22 VAL HA H 3.718 . 1 136 . 22 VAL CB C 32.237 . 1 137 . 22 VAL HB H 2.259 . 1 138 . 22 VAL CG2 C 22.392 . 2 139 . 22 VAL HG2 H 1.232 . 4 140 . 22 VAL CG1 C 21.255 . 2 141 . 22 VAL HG1 H 1.031 . 4 142 . 22 VAL C C 179.067 . 1 143 . 23 LEU N N 120.860 . 1 144 . 23 LEU H H 7.304 . 1 145 . 23 LEU CA C 57.593 . 1 146 . 23 LEU HA H 3.940 . 1 147 . 23 LEU CB C 41.582 . 1 148 . 23 LEU HB2 H 1.778 . 2 149 . 23 LEU CG C 27.115 . 1 150 . 23 LEU HG H 1.203 . 1 151 . 23 LEU CD1 C 22.956 . 2 152 . 23 LEU HD1 H 0.890 . 4 153 . 23 LEU CD2 C 25.708 . 2 154 . 23 LEU HD2 H 0.998 . 4 155 . 23 LEU C C 178.181 . 1 156 . 24 ALA N N 120.577 . 1 157 . 24 ALA H H 8.531 . 1 158 . 24 ALA CA C 55.670 . 1 159 . 24 ALA HA H 3.806 . 1 160 . 24 ALA CB C 18.503 . 1 161 . 24 ALA HB H 1.579 . 1 162 . 24 ALA C C 179.713 . 1 163 . 25 LYS N N 116.858 . 1 164 . 25 LYS H H 7.795 . 1 165 . 25 LYS CA C 58.840 . 1 166 . 25 LYS HA H 4.116 . 1 167 . 25 LYS CB C 32.351 . 1 168 . 25 LYS HB2 H 1.970 . 2 169 . 25 LYS CG C 25.247 . 1 170 . 25 LYS HG2 H 1.542 . 2 171 . 25 LYS CD C 29.360 . 1 172 . 25 LYS HD2 H 1.781 . 2 173 . 25 LYS CE C 42.302 . 1 174 . 25 LYS HE2 H 3.049 . 2 175 . 25 LYS C C 178.259 . 1 176 . 26 ALA N N 122.123 . 1 177 . 26 ALA H H 7.671 . 1 178 . 26 ALA CA C 54.837 . 1 179 . 26 ALA HA H 4.197 . 1 180 . 26 ALA CB C 17.864 . 1 181 . 26 ALA HB H 1.357 . 1 182 . 26 ALA C C 180.594 . 1 183 . 27 TYR N N 116.913 . 1 184 . 27 TYR H H 8.215 . 1 185 . 27 TYR CA C 61.213 . 1 186 . 27 TYR HA H 4.494 . 1 187 . 27 TYR CB C 37.359 . 1 188 . 27 TYR HB3 H 3.365 . 2 189 . 27 TYR HB2 H 2.829 . 2 190 . 27 TYR CD1 C 132.808 . 2 191 . 27 TYR HD1 H 7.024 . 2 192 . 27 TYR CE1 C 118.518 . 2 193 . 27 TYR HE1 H 6.701 . 2 194 . 27 TYR C C 177.996 . 1 195 . 28 SER N N 115.508 . 1 196 . 28 SER H H 8.236 . 1 197 . 28 SER CA C 61.493 . 1 198 . 28 SER HA H 4.281 . 1 199 . 28 SER CB C 62.563 . 1 200 . 28 SER C C 178.039 . 1 201 . 29 VAL N N 121.634 . 1 202 . 29 VAL H H 8.301 . 1 203 . 29 VAL CA C 65.367 . 1 204 . 29 VAL HA H 3.967 . 1 205 . 29 VAL CB C 31.889 . 1 206 . 29 VAL HB H 2.287 . 1 207 . 29 VAL CG2 C 22.237 . 2 208 . 29 VAL HG2 H 1.122 . 4 209 . 29 VAL CG1 C 21.258 . 2 210 . 29 VAL HG1 H 1.031 . 4 211 . 29 VAL C C 177.736 . 1 212 . 30 GLN N N 117.640 . 1 213 . 30 GLN H H 7.788 . 1 214 . 30 GLN CA C 56.603 . 1 215 . 30 GLN HA H 4.403 . 1 216 . 30 GLN CB C 29.281 . 1 217 . 30 GLN HB3 H 2.394 . 2 218 . 30 GLN HB2 H 2.247 . 2 219 . 30 GLN CG C 34.269 . 1 220 . 30 GLN HG2 H 2.629 . 2 221 . 30 GLN C C 176.556 . 1 222 . 31 GLY N N 106.776 . 1 223 . 31 GLY H H 7.939 . 1 224 . 31 GLY CA C 45.567 . 1 225 . 31 GLY HA3 H 4.321 . 2 226 . 31 GLY HA2 H 3.905 . 2 227 . 31 GLY C C 174.265 . 1 228 . 32 ASP N N 122.276 . 1 229 . 32 ASP H H 8.309 . 1 230 . 32 ASP CA C 52.539 . 1 231 . 32 ASP HA H 5.027 . 1 232 . 32 ASP CB C 40.155 . 1 233 . 32 ASP HB3 H 3.088 . 2 234 . 32 ASP HB2 H 2.621 . 2 235 . 33 LYS N N 122.901 . 1 236 . 33 LYS H H 8.000 . 1 237 . 33 LYS CA C 59.117 . 1 238 . 33 LYS HA H 4.006 . 1 239 . 33 LYS CB C 32.421 . 1 240 . 33 LYS HB2 H 1.739 . 2 241 . 33 LYS CG C 24.703 . 1 242 . 33 LYS HG2 H 1.261 . 2 243 . 33 LYS CD C 29.217 . 1 244 . 33 LYS HD2 H 1.620 . 2 245 . 33 LYS CE C 42.088 . 1 246 . 33 LYS HE2 H 2.896 . 2 247 . 33 LYS C C 178.538 . 1 248 . 34 TRP N N 119.597 . 1 249 . 34 TRP H H 8.333 . 1 250 . 34 TRP CA C 60.007 . 1 251 . 34 TRP HA H 4.544 . 1 252 . 34 TRP CB C 28.824 . 1 253 . 34 TRP HB2 H 3.448 . 2 254 . 34 TRP CD1 C 127.662 . 2 255 . 34 TRP HD1 H 7.442 . 1 256 . 34 TRP NE1 N 129.468 . 1 257 . 34 TRP HE1 H 10.242 . 2 258 . 34 TRP C C 179.397 . 1 259 . 35 ARG N N 110.052 . 1 260 . 35 ARG H H 7.976 . 1 261 . 35 ARG CA C 59.320 . 1 262 . 35 ARG HA H 4.002 . 1 263 . 35 ARG CB C 30.045 . 1 264 . 35 ARG HB3 H 1.395 . 2 265 . 35 ARG HB2 H 1.105 . 2 266 . 35 ARG CG C 28.601 . 1 267 . 35 ARG HG3 H 1.661 . 2 268 . 35 ARG HG2 H 1.174 . 2 269 . 35 ARG CD C 43.333 . 1 270 . 35 ARG HD2 H 2.780 . 2 271 . 35 ARG C C 179.079 . 1 272 . 36 ALA N N 121.301 . 1 273 . 36 ALA H H 8.186 . 1 274 . 36 ALA CA C 56.370 . 1 275 . 36 ALA HA H 4.192 . 1 276 . 36 ALA CB C 18.606 . 1 277 . 36 ALA HB H 1.615 . 1 278 . 36 ALA C C 179.814 . 1 279 . 37 LEU N N 119.184 . 1 280 . 37 LEU H H 8.171 . 1 281 . 37 LEU CA C 57.618 . 1 282 . 37 LEU HA H 4.311 . 1 283 . 37 LEU CB C 41.972 . 1 284 . 37 LEU HB3 H 1.855 . 2 285 . 37 LEU HB2 H 1.762 . 2 286 . 37 LEU CG C 27.115 . 1 287 . 37 LEU HG H 1.772 . 1 288 . 37 LEU CD1 C 24.419 . 2 289 . 37 LEU HD1 H 0.992 . 4 290 . 37 LEU C C 179.320 . 1 291 . 38 GLY N N 107.245 . 1 292 . 38 GLY H H 7.939 . 1 293 . 38 GLY CA C 47.295 . 1 294 . 38 GLY HA3 H 3.971 . 2 295 . 38 GLY HA2 H 3.852 . 2 296 . 38 GLY C C 177.537 . 1 297 . 39 TYR N N 121.607 . 1 298 . 39 TYR H H 8.251 . 1 299 . 39 TYR CA C 62.889 . 1 300 . 39 TYR HA H 4.241 . 1 301 . 39 TYR CB C 38.492 . 1 302 . 39 TYR HB2 H 3.036 . 2 303 . 39 TYR CD1 C 132.460 . 2 304 . 39 TYR HD1 H 7.246 . 2 305 . 39 TYR CE1 C 118.806 . 2 306 . 39 TYR HE1 H 6.731 . 2 307 . 39 TYR C C 177.540 . 1 308 . 40 ALA N N 122.326 . 1 309 . 40 ALA H H 8.340 . 1 310 . 40 ALA CA C 55.881 . 1 311 . 40 ALA HA H 4.202 . 1 312 . 40 ALA CB C 18.044 . 1 313 . 40 ALA HB H 1.659 . 1 314 . 40 ALA C C 180.644 . 1 315 . 41 LYS N N 118.075 . 1 316 . 41 LYS H H 8.404 . 1 317 . 41 LYS CA C 59.683 . 1 318 . 41 LYS HA H 4.150 . 1 319 . 41 LYS CB C 32.617 . 1 320 . 41 LYS HB2 H 2.013 . 2 321 . 41 LYS CG C 25.532 . 1 322 . 41 LYS HG2 H 1.585 . 2 323 . 41 LYS CD C 29.585 . 1 324 . 41 LYS HD2 H 1.806 . 2 325 . 41 LYS CE C 42.184 . 1 326 . 41 LYS HE2 H 3.077 . 2 327 . 41 LYS C C 179.686 . 1 328 . 42 ALA N N 122.593 . 1 329 . 42 ALA H H 7.720 . 1 330 . 42 ALA CA C 55.103 . 1 331 . 42 ALA HA H 4.043 . 1 332 . 42 ALA CB C 18.746 . 1 333 . 42 ALA HB H 1.535 . 1 334 . 42 ALA C C 179.049 . 1 335 . 43 ILE N N 118.591 . 1 336 . 43 ILE H H 8.682 . 1 337 . 43 ILE CA C 66.521 . 1 338 . 43 ILE HA H 3.460 . 1 339 . 43 ILE CB C 38.390 . 1 340 . 43 ILE HB H 2.077 . 1 341 . 43 ILE CG1 C 32.238 . 2 342 . 43 ILE HG12 H 2.031 . 9 343 . 43 ILE CD1 C 13.977 . 1 344 . 43 ILE HD1 H 0.898 . 1 345 . 43 ILE CG2 C 17.942 . 2 346 . 43 ILE HG2 H 1.025 . 4 347 . 43 ILE C C 177.587 . 1 348 . 44 ASN N N 117.227 . 1 349 . 44 ASN H H 8.001 . 1 350 . 44 ASN CA C 56.615 . 1 351 . 44 ASN HA H 4.455 . 1 352 . 44 ASN CB C 38.286 . 1 353 . 44 ASN HB2 H 2.918 . 2 354 . 44 ASN C C 177.906 . 1 355 . 45 ALA N N 122.685 . 1 356 . 45 ALA H H 8.004 . 1 357 . 45 ALA CA C 54.893 . 1 358 . 45 ALA HA H 4.257 . 1 359 . 45 ALA CB C 18.775 . 1 360 . 45 ALA HB H 1.578 . 1 361 . 45 ALA C C 180.644 . 1 362 . 46 LEU N N 118.076 . 1 363 . 46 LEU H H 8.404 . 1 364 . 46 LEU CA C 57.829 . 1 365 . 46 LEU HA H 4.066 . 1 366 . 46 LEU CB C 42.824 . 1 367 . 46 LEU HB3 H 2.018 . 2 368 . 46 LEU HB2 H 1.256 . 2 369 . 46 LEU CG C 27.461 . 1 370 . 46 LEU HG H 1.819 . 1 371 . 46 LEU CD1 C 24.224 . 2 372 . 46 LEU HD1 H 0.760 . 4 373 . 46 LEU CD2 C 26.786 . 2 374 . 46 LEU HD2 H 0.765 . 2 375 . 46 LEU C C 179.806 . 1 376 . 47 LYS N N 118.993 . 1 377 . 47 LYS H H 8.643 . 1 378 . 47 LYS CA C 60.138 . 1 379 . 47 LYS HA H 4.187 . 1 380 . 47 LYS CB C 33.061 . 1 381 . 47 LYS HB3 H 2.071 . 2 382 . 47 LYS HB2 H 1.968 . 2 383 . 47 LYS CG C 26.979 . 1 384 . 47 LYS HG2 H 1.532 . 2 385 . 47 LYS CD C 30.301 . 1 386 . 47 LYS HD2 H 1.788 . 2 387 . 47 LYS CE C 42.258 . 1 388 . 47 LYS HE3 H 3.021 . 2 389 . 47 LYS HE2 H 2.898 . 2 390 . 47 LYS C C 177.680 . 1 391 . 48 SER N N 109.776 . 1 392 . 48 SER H H 7.391 . 1 393 . 48 SER CA C 58.486 . 1 394 . 48 SER HA H 4.691 . 1 395 . 48 SER CB C 64.504 . 1 396 . 48 SER HB2 H 4.145 . 2 397 . 48 SER C C 174.069 . 1 398 . 49 PHE N N 124.248 . 1 399 . 49 PHE H H 7.574 . 1 400 . 49 PHE CA C 59.383 . 1 401 . 49 PHE CB C 39.905 . 1 402 . 49 PHE HB3 H 3.007 . 2 403 . 49 PHE HB2 H 3.634 . 2 404 . 50 HIS CA C 58.091 . 1 405 . 50 HIS HA H 4.544 . 1 406 . 50 HIS CB C 30.793 . 1 407 . 50 HIS HB3 H 3.309 . 2 408 . 50 HIS HB2 H 2.999 . 2 409 . 50 HIS C C 172.393 . 1 410 . 51 LYS N N 116.998 . 1 411 . 51 LYS H H 6.744 . 1 412 . 51 LYS CA C 53.581 . 1 413 . 51 LYS CB C 31.149 . 1 414 . 52 PRO CA C 62.291 . 1 415 . 52 PRO HA H 4.640 . 1 416 . 52 PRO CB C 31.984 . 1 417 . 52 PRO HB3 H 2.504 . 2 418 . 52 PRO HB2 H 1.942 . 2 419 . 52 PRO CG C 28.120 . 1 420 . 52 PRO HG2 H 2.255 . 2 421 . 52 PRO CD C 51.153 . 1 422 . 52 PRO HD3 H 3.661 . 2 423 . 52 PRO HD2 H 3.582 . 2 424 . 52 PRO C C 176.911 . 1 425 . 53 VAL N N 126.991 . 1 426 . 53 VAL H H 9.570 . 1 427 . 53 VAL CA C 63.198 . 1 428 . 53 VAL HA H 4.182 . 1 429 . 53 VAL CB C 32.253 . 1 430 . 53 VAL HB H 1.875 . 1 431 . 53 VAL CG2 C 22.867 . 2 432 . 53 VAL HG2 H 0.871 . 4 433 . 53 VAL CG1 C 21.923 . 2 434 . 53 VAL HG1 H 0.876 . 4 435 . 53 VAL C C 176.923 . 1 436 . 54 THR N N 114.162 . 1 437 . 54 THR H H 9.237 . 1 438 . 54 THR CA C 61.512 . 1 439 . 54 THR HA H 4.764 . 1 440 . 54 THR CB C 71.422 . 1 441 . 54 THR HB H 4.542 . 1 442 . 54 THR CG2 C 21.593 . 1 443 . 54 THR HG2 H 1.227 . 1 444 . 54 THR C C 174.427 . 1 445 . 55 SER N N 113.980 . 1 446 . 55 SER H H 7.606 . 1 447 . 55 SER CA C 56.884 . 1 448 . 55 SER HA H 4.975 . 1 449 . 55 SER CB C 67.424 . 1 450 . 55 SER HB3 H 4.367 . 2 451 . 55 SER HB2 H 4.046 . 2 452 . 55 SER C C 173.877 . 1 453 . 56 TYR N N 123.859 . 1 454 . 56 TYR H H 9.542 . 1 455 . 56 TYR CA C 61.956 . 1 456 . 56 TYR HA H 4.026 . 1 457 . 56 TYR CB C 38.613 . 1 458 . 56 TYR HB3 H 3.285 . 2 459 . 56 TYR HB2 H 3.022 . 2 460 . 56 TYR CD1 C 132.825 . 2 461 . 56 TYR HD1 H 6.966 . 2 462 . 56 TYR CE1 C 119.255 . 2 463 . 56 TYR HE1 H 6.845 . 2 464 . 56 TYR C C 176.762 . 1 465 . 57 GLN N N 118.893 . 1 466 . 57 GLN H H 8.997 . 1 467 . 57 GLN CA C 59.540 . 1 468 . 57 GLN HA H 3.843 . 1 469 . 57 GLN CB C 27.886 . 1 470 . 57 GLN HB3 H 2.206 . 2 471 . 57 GLN HB2 H 2.086 . 2 472 . 57 GLN CG C 34.138 . 1 473 . 57 GLN HG2 H 2.593 . 2 474 . 57 GLN C C 178.797 . 1 475 . 58 GLU N N 118.956 . 1 476 . 58 GLU H H 7.782 . 1 477 . 58 GLU CA C 58.983 . 1 478 . 58 GLU HA H 4.053 . 1 479 . 58 GLU CB C 30.882 . 1 480 . 58 GLU HB2 H 2.241 . 2 481 . 58 GLU CG C 36.991 . 1 482 . 58 GLU HG2 H 2.340 . 2 483 . 58 GLU C C 179.430 . 1 484 . 59 ALA N N 121.950 . 1 485 . 59 ALA H H 8.144 . 1 486 . 59 ALA CA C 55.317 . 1 487 . 59 ALA HA H 3.803 . 1 488 . 59 ALA CB C 17.524 . 1 489 . 59 ALA HB H 1.372 . 1 490 . 59 ALA C C 177.653 . 1 491 . 60 CYS N N 109.664 . 1 492 . 60 CYS H H 7.840 . 1 493 . 60 CYS CA C 61.656 . 1 494 . 60 CYS HA H 3.938 . 1 495 . 60 CYS CB C 26.986 . 1 496 . 60 CYS HB3 H 2.690 . 2 497 . 60 CYS HB2 H 2.564 . 2 498 . 60 CYS C C 175.341 . 1 499 . 61 SER N N 114.429 . 1 500 . 61 SER H H 7.480 . 1 501 . 61 SER CA C 58.852 . 1 502 . 61 SER HA H 4.514 . 1 503 . 61 SER CB C 64.305 . 1 504 . 61 SER HB3 H 4.182 . 2 505 . 61 SER HB2 H 4.069 . 2 506 . 61 SER C C 173.732 . 1 507 . 62 ILE N N 126.829 . 1 508 . 62 ILE H H 7.210 . 1 509 . 62 ILE CA C 59.830 . 1 510 . 62 ILE CB C 38.435 . 1 511 . 62 ILE CD1 C 13.848 . 1 512 . 62 ILE HD1 H 0.074 . 1 513 . 62 ILE CG2 C 16.907 . 1 514 . 62 ILE HG2 H 0.734 . 1 515 . 63 PRO CA C 64.296 . 1 516 . 63 PRO HA H 4.305 . 1 517 . 63 PRO CB C 31.838 . 1 518 . 63 PRO HB3 H 2.418 . 2 519 . 63 PRO HB2 H 2.014 . 2 520 . 63 PRO CG C 28.037 . 1 521 . 63 PRO HG3 H 2.315 . 2 522 . 63 PRO HG2 H 2.126 . 2 523 . 63 PRO CD C 51.421 . 1 524 . 63 PRO HD2 H 3.793 . 2 525 . 63 PRO C C 177.326 . 1 526 . 64 GLY N N 110.995 . 1 527 . 64 GLY H H 8.592 . 1 528 . 64 GLY CA C 44.974 . 1 529 . 64 GLY HA3 H 4.265 . 2 530 . 64 GLY HA2 H 3.617 . 2 531 . 64 GLY C C 173.997 . 1 532 . 65 ILE N N 120.242 . 1 533 . 65 ILE H H 7.688 . 1 534 . 65 ILE CA C 61.134 . 1 535 . 65 ILE HA H 4.107 . 1 536 . 65 ILE CB C 36.348 . 1 537 . 65 ILE HB H 2.264 . 1 538 . 65 ILE CG1 C 27.339 . 2 539 . 65 ILE HG13 H 1.336 . 9 540 . 65 ILE HG12 H 0.913 . 9 541 . 65 ILE CD1 C 12.001 . 1 542 . 65 ILE HD1 H 0.729 . 1 543 . 65 ILE CG2 C 17.952 . 2 544 . 65 ILE HG2 H 0.745 . 4 545 . 65 ILE C C 175.530 . 1 546 . 66 GLY N N 112.037 . 1 547 . 66 GLY H H 7.991 . 1 548 . 66 GLY CA C 44.275 . 1 549 . 66 GLY HA3 H 4.310 . 2 550 . 66 GLY HA2 H 4.062 . 2 551 . 66 GLY C C 173.803 . 1 552 . 67 LYS N N 119.437 . 1 553 . 67 LYS H H 8.422 . 1 554 . 67 LYS CA C 60.677 . 1 555 . 67 LYS HA H 4.106 . 1 556 . 67 LYS CB C 32.984 . 1 557 . 67 LYS HB2 H 2.000 . 2 558 . 67 LYS CG C 25.250 . 1 559 . 67 LYS HG2 H 1.545 . 2 560 . 67 LYS CD C 29.863 . 1 561 . 67 LYS HD2 H 1.823 . 2 562 . 67 LYS CE C 42.331 . 1 563 . 67 LYS HE2 H 3.140 . 2 564 . 68 ARG N N 117.274 . 1 565 . 68 ARG H H 8.436 . 1 566 . 68 ARG CA C 59.783 . 1 567 . 68 ARG HA H 4.187 . 1 568 . 68 ARG CB C 29.655 . 1 569 . 68 ARG HB2 H 1.995 . 2 570 . 68 ARG CG C 27.484 . 1 571 . 68 ARG HG2 H 1.837 . 2 572 . 68 ARG CD C 43.208 . 1 573 . 68 ARG HD2 H 3.339 . 2 574 . 68 ARG C C 179.789 . 1 575 . 69 MET N N 119.422 . 1 576 . 69 MET H H 8.003 . 1 577 . 69 MET CA C 56.070 . 1 578 . 69 MET HA H 4.554 . 1 579 . 69 MET CB C 30.942 . 1 580 . 69 MET HB3 H 2.164 . 2 581 . 69 MET HB2 H 1.938 . 2 582 . 69 MET CG C 32.233 . 1 583 . 69 MET HG3 H 2.585 . 2 584 . 69 MET HG2 H 2.397 . 2 585 . 69 MET C C 178.162 . 1 586 . 70 ALA N N 123.316 . 1 587 . 70 ALA H H 8.652 . 1 588 . 70 ALA CA C 56.092 . 1 589 . 70 ALA HA H 3.849 . 1 590 . 70 ALA CB C 19.706 . 1 591 . 70 ALA HB H 1.381 . 1 592 . 70 ALA C C 179.240 . 1 593 . 71 GLU N N 116.117 . 1 594 . 71 GLU H H 8.098 . 1 595 . 71 GLU CA C 59.848 . 1 596 . 71 GLU HA H 4.092 . 1 597 . 71 GLU CB C 29.826 . 1 598 . 71 GLU HB2 H 2.336 . 2 599 . 71 GLU CG C 37.077 . 1 600 . 71 GLU HG2 H 2.774 . 2 601 . 71 GLU C C 179.479 . 1 602 . 72 LYS N N 120.563 . 1 603 . 72 LYS H H 7.664 . 1 604 . 72 LYS CA C 57.492 . 1 605 . 72 LYS HA H 4.311 . 1 606 . 72 LYS CB C 30.891 . 1 607 . 72 LYS HB2 H 2.183 . 2 608 . 72 LYS CG C 23.805 . 1 609 . 72 LYS HG2 H 1.560 . 2 610 . 72 LYS CD C 27.896 . 1 611 . 72 LYS HD2 H 1.892 . 2 612 . 72 LYS CE C 41.947 . 1 613 . 72 LYS HE2 H 3.055 . 2 614 . 72 LYS C C 178.401 . 1 615 . 73 ILE N N 119.438 . 1 616 . 73 ILE H H 8.422 . 1 617 . 73 ILE CA C 66.156 . 1 618 . 73 ILE HA H 3.519 . 1 619 . 73 ILE CB C 37.725 . 1 620 . 73 ILE HB H 2.079 . 1 621 . 73 ILE CG1 C 30.289 . 2 622 . 73 ILE HG12 H 1.891 . 9 623 . 73 ILE CD1 C 15.144 . 1 624 . 73 ILE HD1 H 0.817 . 1 625 . 73 ILE CG2 C 16.744 . 2 626 . 73 ILE HG2 H 0.860 . 4 627 . 73 ILE C C 176.994 . 1 628 . 74 ILE N N 118.540 . 1 629 . 74 ILE H H 7.980 . 1 630 . 74 ILE CA C 62.059 . 1 631 . 74 ILE HA H 4.049 . 1 632 . 74 ILE CB C 35.888 . 1 633 . 74 ILE HB H 2.222 . 1 634 . 74 ILE CG1 C 28.204 . 2 635 . 74 ILE HG13 H 1.958 . 9 636 . 74 ILE HG12 H 1.471 . 9 637 . 74 ILE CD1 C 10.090 . 1 638 . 74 ILE HD1 H 0.737 . 1 639 . 74 ILE CG2 C 18.460 . 2 640 . 74 ILE HG2 H 1.099 . 4 641 . 74 ILE C C 177.407 . 1 642 . 75 GLU N N 109.801 . 1 643 . 75 GLU H H 8.026 . 1 644 . 75 GLU CA C 59.802 . 1 645 . 75 GLU HA H 4.168 . 1 646 . 75 GLU CB C 29.855 . 1 647 . 75 GLU HB3 H 2.360 . 2 648 . 75 GLU HB2 H 2.273 . 2 649 . 75 GLU CG C 36.326 . 1 650 . 75 GLU HG2 H 2.528 . 2 651 . 75 GLU C C 180.189 . 1 652 . 76 ILE N N 120.338 . 1 653 . 76 ILE H H 8.163 . 1 654 . 76 ILE CA C 64.995 . 1 655 . 76 ILE HA H 3.805 . 1 656 . 76 ILE CB C 37.973 . 1 657 . 76 ILE HB H 2.178 . 1 658 . 76 ILE CG1 C 29.430 . 2 659 . 76 ILE HG13 H 1.923 . 9 660 . 76 ILE HG12 H 1.200 . 9 661 . 76 ILE CD1 C 14.503 . 1 662 . 76 ILE HD1 H 0.874 . 1 663 . 76 ILE CG2 C 18.312 . 2 664 . 76 ILE HG2 H 1.037 . 4 665 . 76 ILE C C 179.345 . 1 666 . 77 LEU N N 122.332 . 1 667 . 77 LEU H H 8.463 . 1 668 . 77 LEU CA C 58.101 . 1 669 . 77 LEU HA H 4.187 . 1 670 . 77 LEU CB C 42.641 . 1 671 . 77 LEU HB2 H 1.995 . 2 672 . 77 LEU CG C 27.047 . 1 673 . 77 LEU HG H 1.873 . 1 674 . 77 LEU CD1 C 24.291 . 2 675 . 77 LEU HD1 H 1.029 . 4 676 . 77 LEU CD2 C 24.989 . 2 677 . 77 LEU C C 179.451 . 1 678 . 78 GLU N N 116.976 . 1 679 . 78 GLU H H 8.630 . 1 680 . 78 GLU CA C 58.179 . 1 681 . 78 GLU HA H 4.308 . 1 682 . 78 GLU CB C 29.904 . 1 683 . 78 GLU HB2 H 2.215 . 2 684 . 78 GLU CG C 37.024 . 1 685 . 78 GLU HG3 H 2.596 . 2 686 . 78 GLU HG2 H 2.367 . 2 687 . 78 GLU C C 178.112 . 1 688 . 79 SER N N 114.286 . 1 689 . 79 SER H H 8.057 . 1 690 . 79 SER CA C 60.007 . 1 691 . 79 SER HA H 4.544 . 1 692 . 79 SER CB C 64.187 . 1 693 . 79 SER HB2 H 4.145 . 2 694 . 79 SER C C 175.666 . 1 695 . 80 GLY N N 110.066 . 1 696 . 80 GLY H H 8.225 . 1 697 . 80 GLY CA C 45.984 . 1 698 . 81 HIS N N 118.855 . 1 699 . 81 HIS H H 8.105 . 1 700 . 81 HIS CA C 56.493 . 1 701 . 81 HIS HA H 4.717 . 1 702 . 81 HIS CB C 31.090 . 1 703 . 81 HIS HB2 H 3.247 . 2 704 . 81 HIS C C 175.202 . 1 705 . 82 LEU N N 121.397 . 1 706 . 82 LEU H H 8.078 . 1 707 . 82 LEU CA C 55.200 . 1 708 . 82 LEU HA H 4.446 . 1 709 . 82 LEU CB C 42.574 . 1 710 . 82 LEU HB2 H 1.701 . 2 711 . 82 LEU CG C 27.084 . 1 712 . 82 LEU HG H 1.581 . 1 713 . 82 LEU CD1 C 23.880 . 2 714 . 82 LEU HD1 H 1.002 . 4 715 . 82 LEU CD2 C 25.384 . 2 716 . 82 LEU C C 177.116 . 1 717 . 83 ARG N N 121.927 . 1 718 . 83 ARG H H 8.339 . 1 719 . 83 ARG CA C 56.326 . 1 720 . 83 ARG HA H 4.385 . 1 721 . 83 ARG CB C 30.964 . 1 722 . 83 ARG HB2 H 1.905 . 2 723 . 83 ARG CG C 27.031 . 1 724 . 83 ARG HG2 H 1.720 . 2 725 . 83 ARG CD C 43.540 . 1 726 . 83 ARG HD2 H 3.270 . 2 727 . 83 ARG C C 175.838 . 1 728 . 84 LYS N N 123.358 . 1 729 . 84 LYS H H 8.353 . 1 730 . 84 LYS CA C 56.337 . 1 731 . 84 LYS HA H 4.401 . 1 732 . 84 LYS CB C 33.191 . 1 733 . 84 LYS HB2 H 1.895 . 2 734 . 84 LYS CG C 24.910 . 1 735 . 84 LYS HG2 H 1.503 . 2 736 . 84 LYS CD C 29.238 . 1 737 . 84 LYS HD2 H 1.787 . 2 738 . 84 LYS CE C 42.289 . 1 739 . 84 LYS HE2 H 3.081 . 2 740 . 84 LYS C C 176.360 . 1 741 . 85 LEU N N 123.775 . 1 742 . 85 LEU H H 8.386 . 1 743 . 85 LEU CA C 55.064 . 1 744 . 85 LEU HA H 4.488 . 1 745 . 85 LEU CB C 42.705 . 1 746 . 85 LEU HB2 H 1.699 . 2 747 . 85 LEU CG C 27.151 . 1 748 . 85 LEU HG H 1.624 . 1 749 . 85 LEU CD1 C 23.470 . 2 750 . 85 LEU HD1 H 0.961 . 4 751 . 85 LEU CD2 C 25.253 . 2 752 . 85 LEU C C 177.003 . 1 753 . 86 ASP N N 121.054 . 1 754 . 86 ASP H H 8.348 . 1 755 . 86 ASP CA C 54.398 . 1 756 . 86 ASP HA H 4.654 . 1 757 . 86 ASP CB C 41.396 . 1 758 . 86 ASP HB2 H 2.738 . 2 759 . 87 HIS N N 123.437 . 1 760 . 87 HIS H H 7.808 . 1 761 . 87 HIS CA C 57.659 . 1 762 . 87 HIS CB C 31.206 . 1 stop_ save_