data_4925 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Structural Basis for the Functional switch of the E. Coli Ada Protein ; _BMRB_accession_number 4925 _BMRB_flat_file_name bmr4925.str _Entry_type original _Submission_date 2000-05-07 _Accession_date 2000-12-13 _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 Lin Yingxi . . 2 Dotsch Volker . . 3 Wintner T. . . 4 Peariso Katrina . . 5 Myers Lawrence C. . 6 Penner-Hahn James E. . 7 Verdine Gregory L. . 8 Wagner Gerhard . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 478 "13C chemical shifts" 85 "15N chemical shifts" 90 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2001-09-12 original author . stop_ _Original_release_date 2001-09-12 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title 'Structural Basis for the Functional switch of the E. Coli Ada Protein' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code 21181598 _PubMed_ID 11284682 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Lin Yingxi . . 2 Dotsch Volker . . 3 Wintner T. . . 4 Peariso Katrina . . 5 Myers Lawrence C. . 6 Penner-Hahn James E. . 7 Verdine Gregory L. . 8 Wagner Gerhard . . stop_ _Journal_abbreviation Biochemistry _Journal_name_full Biochemistry _Journal_volume 40 _Journal_issue 14 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 4261 _Page_last 4271 _Year 2001 _Details . loop_ _Keyword ADA 'DNA Repair' N-Ada10 NMR Structure stop_ save_ ################################## # Molecular system description # ################################## save_system_N-Ada10 _Saveframe_category molecular_system _Mol_system_name N-Ada10 _Abbreviation_common N-Ada10 _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'N-Ada10 subunit 1' $N-Ada10 Zn2+ $ZN stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state monomer _System_paramagnetic no _System_thiol_state 'other bound and free' _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_N-Ada10 _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common N-Ada10 _Abbreviation_common N-Ada10 _Molecular_mass . _Mol_thiol_state 'not reported' _Details ; Cys 6 and Cys 91 are free, Cys 38, 42, 69, and 72 are bound to the Zinc atom. ; ############################## # Polymer residue sequence # ############################## _Residue_count 92 _Mol_residue_sequence ; MKKATCLTDDQRWQSVLARD PNADGEFVFAVRTTGIFCRP SCRARHALRENVSFYANASE ALAAGFRPCKRCQPDKANPR QHRLDKITHACR ; loop_ _Residue_seq_code _Residue_label 1 MET 2 LYS 3 LYS 4 ALA 5 THR 6 CYS 7 LEU 8 THR 9 ASP 10 ASP 11 GLN 12 ARG 13 TRP 14 GLN 15 SER 16 VAL 17 LEU 18 ALA 19 ARG 20 ASP 21 PRO 22 ASN 23 ALA 24 ASP 25 GLY 26 GLU 27 PHE 28 VAL 29 PHE 30 ALA 31 VAL 32 ARG 33 THR 34 THR 35 GLY 36 ILE 37 PHE 38 CYS 39 ARG 40 PRO 41 SER 42 CYS 43 ARG 44 ALA 45 ARG 46 HIS 47 ALA 48 LEU 49 ARG 50 GLU 51 ASN 52 VAL 53 SER 54 PHE 55 TYR 56 ALA 57 ASN 58 ALA 59 SER 60 GLU 61 ALA 62 LEU 63 ALA 64 ALA 65 GLY 66 PHE 67 ARG 68 PRO 69 CYS 70 LYS 71 ARG 72 CYS 73 GLN 74 PRO 75 ASP 76 LYS 77 ALA 78 ASN 79 PRO 80 ARG 81 GLN 82 HIS 83 ARG 84 LEU 85 ASP 86 LYS 87 ILE 88 THR 89 HIS 90 ALA 91 CYS 92 ARG stop_ _Sequence_homology_query_date 2008-08-19 _Sequence_homology_query_revised_last_date 2008-08-19 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 REF YP_670153 'ADA regulatory protein [Escherichia coli 536]' 100.00 354 98.91 98.91 2.16e-48 REF YP_408500 'O6-methylguanine-DNA methyltransferase; transcription activator/repressor [Shigella boydii Sb227]' 100.00 354 98.91 98.91 2.11e-48 REF YP_311153 'O6-methylguanine-DNA methyltransferase [Shigella sonnei Ss046]' 100.00 354 98.91 98.91 2.11e-48 REF NP_837823 'O6-methylguanine-DNA methyltransferase; transcription activator/repressor [Shigella flexneri 2a str. 2457T]' 100.00 354 98.91 98.91 2.11e-48 REF NP_708108 'O6-methylguanine-DNA methyltransferase; transcription activator/repressor [Shigella flexneri 2a str. 301]' 100.00 354 98.91 98.91 2.11e-48 GenBank ABB66672 'O6-methylguanine-DNA methyltransferase; transcription activator/repressor [Shigella boydii Sb227]' 100.00 354 98.91 98.91 2.11e-48 GenBank AAZ88918 'O6-methylguanine-DNA methyltransferase [Shigella sonnei Ss046]' 100.00 354 98.91 98.91 2.11e-48 GenBank AAP17632 'O6-methylguanine-DNA methyltransferase; transcription activator/repressor [Shigella flexneri 2a str. 2457T]' 100.00 354 98.91 98.91 2.11e-48 GenBank AAN43815 'O6-methylguanine-DNA methyltransferase; transcription activator/repressor [Shigella flexneri 2a str. 301]' 100.00 354 98.91 98.91 2.11e-48 GenBank AAA23413 'Ada polyprotein' 100.00 354 100.00 100.00 5.37e-49 PDB 1ZGW 'Nmr Structure Of E. Coli Ada Protein In Complex With Dna' 100.00 139 98.91 98.91 3.42e-47 PDB 1U8B 'Crystal Structure Of The Methylated N-AdaDNA COMPLEX' 91.30 133 98.81 98.81 2.46e-42 PDB 1EYF 'Refined Structure Of The Dna Methyl Phosphotriester Repair Domain Of E. Coli Ada' 98.91 92 100.00 100.00 4.82e-47 PDB 1ADN 'Solution Structure Of The Dna Methylphosphotriester Repair Domain Of Escherichia Coli Ada' 100.00 92 100.00 100.00 1.82e-47 BMRB 6605 Ada 100.00 139 98.91 98.91 3.54e-47 stop_ save_ ############# # Ligands # ############# save_ZN _Saveframe_category ligand _Mol_type non-polymer _Name_common "ZN (ZINC ION)" _BMRB_code . _PDB_code ZN _Molecular_mass 65.409 _Mol_charge 2 _Mol_paramagnetic . _Mol_aromatic no _Details ; Information obtained from PDB's Chemical Component Dictionary at http://wwpdb-remediation.rutgers.edu/downloads.html Downloaded on Wed Jun 15 12:20:01 2011 ; loop_ _Atom_name _PDB_atom_name _Atom_type _Atom_chirality _Atom_charge _Atom_oxidation_number _Atom_unpaired_electrons ZN ZN ZN . 2 . ? stop_ _Mol_thiol_state . _Sequence_homology_query_date . save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $N-Ada10 'E. coli' 562 Bacteria . Escherichia coli 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 $N-Ada10 'recombinant technology' . . . . . stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Concentration_min_value _Concentration_max_value _Isotopic_labeling $N-Ada10 . mM 2 3 '[U-15N; U-13C]' stop_ save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer1 _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model Unity-plus _Field_strength 750 _Details . save_ save_NMR_spectrometer2 _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model Unity-plus _Field_strength 450 _Details . save_ save_NMR_spectrometer3 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model AMX _Field_strength 500 _Details . save_ save_NMR_spectrometer4 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model AMX _Field_strength 600 _Details . save_ ############################# # NMR applied experiments # ############################# save_1H-15N_NOESY_1 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-15N NOESY' _Sample_label $sample_1 save_ save_1H-15N_TOCSY_2 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-15N TOCSY' _Sample_label $sample_1 save_ save_2D_NOESY_3 _Saveframe_category NMR_applied_experiment _Experiment_name '2D NOESY' _Sample_label $sample_1 save_ save_HCCH-TOCSY_4 _Saveframe_category NMR_applied_experiment _Experiment_name HCCH-TOCSY _Sample_label $sample_1 save_ save_NMR_spec_expt__0_1 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-15N NOESY' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_2 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-15N TOCSY' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_3 _Saveframe_category NMR_applied_experiment _Experiment_name '2D NOESY' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_4 _Saveframe_category NMR_applied_experiment _Experiment_name HCCH-TOCSY _BMRB_pulse_sequence_accession_number . _Details . save_ ####################### # Sample conditions # ####################### save_Ex-cond1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 6.4 0.1 n/a temperature 298 1 K 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 _Indirect_shift_ratio_citation_label _Correction_value_citation_label DSS H 1 'methyl protons' ppm 0.00 external direct cylindrical external_to_the_sample parallel_to_Bo 1.0 $entry_citation $entry_citation DSS N 15 'methyl protons' ppm 0.00 . indirect . . . 0.101329118 $entry_citation $entry_citation DSS C 13 'methyl protons' ppm 0.0 . indirect . . . 0.251449530 $entry_citation $entry_citation 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_shift_set_1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Experiment_label '1H-15N NOESY' '1H-15N TOCSY' '2D NOESY' HCCH-TOCSY stop_ loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $Ex-cond1 _Chem_shift_reference_set_label $chemical_shift_reference _Mol_system_component_name 'N-Ada10 subunit 1' _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 . 4 ALA H H 8.453 0.02 1 2 . 4 ALA HA H 4.361 0.02 1 3 . 4 ALA HB H 1.401 0.02 1 4 . 4 ALA CA C 52.3 0.02 1 5 . 4 ALA N N 126.854 0.02 1 6 . 5 THR H H 8.453 0.02 1 7 . 5 THR HA H 4.316 0.02 1 8 . 5 THR HB H 4.198 0.02 1 9 . 5 THR HG2 H 1.2 0.02 1 10 . 5 THR CA C 62.24 0.02 1 11 . 5 THR N N 114.521 0.02 1 12 . 6 CYS H H 8.74 0.02 1 13 . 6 CYS HA H 4.493 0.02 1 14 . 6 CYS HB2 H 2.9 0.02 2 15 . 6 CYS HB3 H 2.702 0.02 2 16 . 6 CYS CA C 58.33 0.02 1 17 . 6 CYS N N 122.768 0.02 1 18 . 7 LEU H H 8.382 0.02 1 19 . 7 LEU HA H 4.444 0.02 1 20 . 7 LEU HB2 H 1.62 0.02 2 21 . 7 LEU HB3 H 1.503 0.02 2 22 . 7 LEU HD1 H 0.9 0.02 1 23 . 7 LEU HD2 H 0.8 0.02 1 24 . 7 LEU CA C 55.38 0.02 1 25 . 7 LEU N N 123.771 0.02 1 26 . 8 THR H H 7.943 0.02 1 27 . 8 THR HA H 4.48 0.02 1 28 . 8 THR HB H 4.534 0.02 1 29 . 8 THR HG2 H 1.191 0.02 1 30 . 8 THR CA C 60.03 0.02 1 31 . 8 THR N N 110.41 0.02 1 32 . 9 ASP H H 8.941 0.02 1 33 . 9 ASP HA H 3.8 0.02 1 34 . 9 ASP HB2 H 2.571 0.02 1 35 . 9 ASP HB3 H 2.571 0.02 1 36 . 9 ASP CA C 57.23 0.02 1 37 . 9 ASP N N 122.768 0.02 1 38 . 10 ASP H H 8.153 0.02 1 39 . 10 ASP HA H 4.467 0.02 1 40 . 10 ASP HB2 H 2.575 0.02 2 41 . 10 ASP HB3 H 2.694 0.02 2 42 . 10 ASP CA C 57.51 0.02 1 43 . 10 ASP N N 119.146 0.02 1 44 . 11 GLN H H 7.609 0.02 1 45 . 11 GLN HA H 4.001 0.02 1 46 . 11 GLN HB2 H 2.191 0.02 2 47 . 11 GLN HB3 H 2.049 0.02 2 48 . 11 GLN HG2 H 2.41 0.02 1 49 . 11 GLN HG3 H 2.41 0.02 1 50 . 11 GLN HE21 H 7.489 0.02 1 51 . 11 GLN HE22 H 6.778 0.02 1 52 . 11 GLN CA C 58.83 0.02 1 53 . 11 GLN N N 120.571 0.02 1 54 . 11 GLN NE2 N 111.5 0.02 1 55 . 12 ARG H H 8.042 0.02 1 56 . 12 ARG HA H 3.352 0.02 1 57 . 12 ARG HB2 H 0.531 0.02 2 58 . 12 ARG HB3 H -0.197 0.02 2 59 . 12 ARG HG2 H 1.126 0.02 2 60 . 12 ARG HG3 H 0.048 0.02 2 61 . 12 ARG HD2 H 2.07 0.02 2 62 . 12 ARG HD3 H 1.7 0.02 2 63 . 12 ARG CA C 59.13 0.02 1 64 . 12 ARG N N 120.7 0.02 1 65 . 13 TRP H H 8.372 0.02 1 66 . 13 TRP HA H 4.659 0.02 1 67 . 13 TRP HB2 H 3.319 0.02 1 68 . 13 TRP HB3 H 3.385 0.02 1 69 . 13 TRP HD1 H 7.238 0.02 1 70 . 13 TRP HE1 H 10.375 0.02 1 71 . 13 TRP HE3 H 7.334 0.02 1 72 . 13 TRP HZ2 H 7.468 0.02 1 73 . 13 TRP HZ3 H 6.447 0.02 1 74 . 13 TRP HH2 H 7.080 0.02 1 75 . 13 TRP CA C 58.95 0.02 1 76 . 13 TRP N N 119.146 0.02 1 77 . 13 TRP NE1 N 129.3 0.02 1 78 . 14 GLN H H 7.782 0.02 1 79 . 14 GLN HA H 3.71 0.02 1 80 . 14 GLN HB2 H 2.172 0.02 1 81 . 14 GLN HB3 H 2.172 0.02 1 82 . 14 GLN HG2 H 2.534 0.02 1 83 . 14 GLN HG3 H 2.534 0.02 1 84 . 14 GLN HE21 H 7.620 0.02 1 85 . 14 GLN HE22 H 6.884 0.02 1 86 . 14 GLN CA C 59.05 0.02 1 87 . 14 GLN N N 116.078 0.02 1 88 . 14 GLN NE2 N 113.0 0.02 1 89 . 15 SER H H 7.84 0.02 1 90 . 15 SER HA H 4.338 0.02 1 91 . 15 SER HB2 H 3.855 0.02 1 92 . 15 SER HB3 H 3.855 0.02 1 93 . 15 SER CA C 63.82 0.02 1 94 . 15 SER N N 117.089 0.02 1 95 . 16 VAL H H 7.707 0.02 1 96 . 16 VAL HA H 3.718 0.02 1 97 . 16 VAL HB H 1.852 0.02 1 98 . 16 VAL HG1 H 1.14 0.02 1 99 . 16 VAL HG2 H -0.202 0.02 1 100 . 16 VAL CA C 66.36 0.02 1 101 . 16 VAL N N 123.262 0.02 1 102 . 17 LEU H H 8.066 0.02 1 103 . 17 LEU HA H 3.309 0.02 1 104 . 17 LEU HB2 H 1.07 0.02 1 105 . 17 LEU HB3 H 1.434 0.02 1 106 . 17 LEU HG H 0.358 0.02 1 107 . 17 LEU HD1 H 0.555 0.02 1 108 . 17 LEU HD2 H 0.23 0.02 1 109 . 17 LEU CA C 57.51 0.02 1 110 . 17 LEU N N 110.143 0.02 1 111 . 18 ALA H H 7.387 0.02 1 112 . 18 ALA HA H 4.165 0.02 1 113 . 18 ALA HB H 1.405 0.02 1 114 . 18 ALA CA C 51.9 0.02 1 115 . 18 ALA N N 117.604 0.02 1 116 . 19 ARG H H 8.101 0.02 1 117 . 19 ARG HA H 4.255 0.02 1 118 . 19 ARG HB2 H 1.93 0.02 2 119 . 19 ARG HB3 H 1.545 0.02 2 120 . 19 ARG CA C 56 0.02 1 121 . 19 ARG N N 121.149 0.02 1 122 . 20 ASP H H 7.617 0.02 1 123 . 20 ASP HA H 4.578 0.02 1 124 . 20 ASP HB2 H 2.829 0.02 1 125 . 20 ASP HB3 H 2.556 0.02 1 126 . 20 ASP CA C 51.51 0.02 1 127 . 20 ASP N N 117.09 0.02 1 128 . 21 PRO HA H 4.371 0.02 1 129 . 21 PRO HB2 H 2.305 0.02 2 130 . 21 PRO HB3 H 2.009 0.02 2 131 . 21 PRO HG2 H 2.02 0.02 1 132 . 21 PRO HG3 H 2.02 0.02 1 133 . 21 PRO HD2 H 4.426 0.02 2 134 . 21 PRO HD3 H 4.014 0.02 2 135 . 21 PRO CA C 64 0.02 1 136 . 22 ASN H H 8.519 0.02 1 137 . 22 ASN HA H 4.515 0.02 1 138 . 22 ASN HB2 H 2.95 0.02 1 139 . 22 ASN HB3 H 2.752 0.02 1 140 . 22 ASN HD21 H 7.045 0.02 1 141 . 22 ASN HD22 H 8.130 0.02 1 142 . 22 ASN CA C 55.05 0.02 1 143 . 22 ASN N N 117.09 0.02 1 144 . 22 ASN ND2 N 115.7 0.02 1 145 . 23 ALA H H 7.755 0.02 1 146 . 23 ALA HA H 4.394 0.02 1 147 . 23 ALA HB H 1.472 0.02 1 148 . 23 ALA CA C 51.67 0.02 1 149 . 23 ALA N N 120.701 0.02 1 150 . 24 ASP H H 7.213 0.02 1 151 . 24 ASP HA H 4.4 0.02 1 152 . 24 ASP HB2 H 2.515 0.02 1 153 . 24 ASP HB3 H 2.943 0.02 1 154 . 24 ASP CA C 56.49 0.02 1 155 . 24 ASP N N 120.687 0.02 1 156 . 25 GLY H H 9.673 0.02 1 157 . 25 GLY HA2 H 4.291 0.02 2 158 . 25 GLY HA3 H 3.723 0.02 2 159 . 25 GLY CA C 45.11 0.02 1 160 . 25 GLY N N 111.951 0.02 1 161 . 26 GLU H H 8.376 0.02 1 162 . 26 GLU HA H 4.421 0.02 1 163 . 26 GLU HB2 H 2.397 0.02 2 164 . 26 GLU HB3 H 2.443 0.02 2 165 . 26 GLU HG2 H 2.505 0.02 2 166 . 26 GLU HG3 H 2.245 0.02 2 167 . 26 GLU CA C 57.89 0.02 1 168 . 26 GLU N N 121.241 0.02 1 169 . 27 PHE H H 7.295 0.02 1 170 . 27 PHE HA H 5.1 0.02 1 171 . 27 PHE HB2 H 3.582 0.02 1 172 . 27 PHE HB3 H 3.426 0.02 1 173 . 27 PHE HD1 H 7.247 0.02 1 174 . 27 PHE HD2 H 7.247 0.02 1 175 . 27 PHE HE1 H 7.325 0.02 1 176 . 27 PHE HE2 H 7.325 0.02 1 177 . 27 PHE HZ H 7.473 0.02 1 178 . 27 PHE CA C 56.17 0.02 1 179 . 27 PHE N N 110.431 0.02 1 180 . 28 VAL H H 9.038 0.02 1 181 . 28 VAL HA H 5.035 0.02 1 182 . 28 VAL HB H 2.358 0.02 1 183 . 28 VAL HG1 H 0.414 0.02 1 184 . 28 VAL HG2 H 0.856 0.02 1 185 . 28 VAL CA C 59.66 0.02 1 186 . 28 VAL N N 109.901 0.02 1 187 . 29 PHE H H 9.14 0.02 1 188 . 29 PHE HA H 5.962 0.02 1 189 . 29 PHE HB2 H 2.92 0.02 1 190 . 29 PHE HB3 H 3.085 0.02 1 191 . 29 PHE HD1 H 6.875 0.02 1 192 . 29 PHE HD2 H 6.875 0.02 1 193 . 29 PHE HE1 H 7.466 0.02 1 194 . 29 PHE HE2 H 7.466 0.02 1 195 . 29 PHE HZ H 7.636 0.02 1 196 . 29 PHE CA C 54.67 0.02 1 197 . 29 PHE N N 120.174 0.02 1 198 . 30 ALA H H 9.432 0.02 1 199 . 30 ALA HA H 4.826 0.02 1 200 . 30 ALA HB H 0.141 0.02 1 201 . 30 ALA CA C 49.71 0.02 1 202 . 30 ALA N N 125.826 0.02 1 203 . 31 VAL H H 8.167 0.02 1 204 . 31 VAL HA H 4.72 0.02 1 205 . 31 VAL HB H 2.411 0.02 1 206 . 31 VAL HG1 H 1.173 0.02 1 207 . 31 VAL HG2 H 1.207 0.02 1 208 . 31 VAL CA C 61.87 0.02 1 209 . 31 VAL N N 122.237 0.02 1 210 . 32 ARG H H 9.225 0.02 1 211 . 32 ARG HA H 4.279 0.02 1 212 . 32 ARG HB2 H 2.079 0.02 1 213 . 32 ARG HB3 H 2.079 0.02 1 214 . 32 ARG HG2 H 1.781 0.02 1 215 . 32 ARG HG3 H 1.781 0.02 1 216 . 32 ARG HD2 H 3.361 0.02 2 217 . 32 ARG HD3 H 3.324 0.02 2 218 . 32 ARG CA C 60.02 0.02 1 219 . 32 ARG N N 127.914 0.02 1 220 . 33 THR H H 7.508 0.02 1 221 . 33 THR HA H 4.32 0.02 1 222 . 33 THR HB H 4.21 0.02 1 223 . 33 THR HG2 H 1.277 0.02 1 224 . 33 THR CA C 63.46 0.02 1 225 . 33 THR N N 105.785 0.02 1 226 . 34 THR H H 7.153 0.02 1 227 . 34 THR HA H 4.57 0.02 1 228 . 34 THR HB H 4.348 0.02 1 229 . 34 THR HG2 H 1.228 0.02 1 230 . 34 THR CA C 61.54 0.02 1 231 . 34 THR N N 108.372 0.02 1 232 . 35 GLY H H 8.521 0.02 1 233 . 35 GLY HA2 H 4.314 0.02 2 234 . 35 GLY HA3 H 3.942 0.02 2 235 . 35 GLY CA C 46.48 0.02 1 236 . 35 GLY N N 109.896 0.02 1 237 . 36 ILE H H 7.683 0.02 1 238 . 36 ILE HA H 5.504 0.02 1 239 . 36 ILE HB H 1.786 0.02 1 240 . 36 ILE HG12 H 1.114 0.02 1 241 . 36 ILE HG13 H 1.476 0.02 1 242 . 36 ILE HG2 H 0.875 0.02 1 243 . 36 ILE HD1 H 0.821 0.02 1 244 . 36 ILE CA C 59.02 0.02 1 245 . 36 ILE N N 122.75 0.02 1 246 . 37 PHE H H 8.782 0.02 1 247 . 37 PHE HA H 5.816 0.02 1 248 . 37 PHE HB2 H 2.741 0.02 1 249 . 37 PHE HB3 H 2.251 0.02 1 250 . 37 PHE HD1 H 6.747 0.02 1 251 . 37 PHE HD2 H 6.747 0.02 1 252 . 37 PHE HE1 H 6.889 0.02 1 253 . 37 PHE HE2 H 6.889 0.02 1 254 . 37 PHE HZ H 7.011 0.02 1 255 . 37 PHE CA C 54.57 0.02 1 256 . 37 PHE N N 124.46 0.02 1 257 . 38 CYS H H 8.428 0.02 1 258 . 38 CYS HA H 4.208 0.02 1 259 . 38 CYS HB2 H 2.958 0.02 1 260 . 38 CYS HB3 H 0.82 0.02 1 261 . 38 CYS CA C 61.24 0.02 1 262 . 38 CYS N N 118.632 0.02 1 263 . 39 ARG H H 9.348 0.02 1 264 . 39 ARG HA H 4.897 0.02 1 265 . 39 ARG HB2 H 1.793 0.02 2 266 . 39 ARG HB3 H 1.896 0.02 2 267 . 39 ARG HG2 H 1.593 0.02 2 268 . 39 ARG HG3 H 1.563 0.02 2 269 . 39 ARG HD2 H 3.212 0.02 2 270 . 39 ARG HD3 H 3.165 0.02 2 271 . 39 ARG CA C 63.44 0.02 1 272 . 39 ARG N N 121.201 0.02 1 273 . 40 PRO HA H 4.436 0.02 1 274 . 40 PRO HB2 H 1.859 0.02 1 275 . 40 PRO HB3 H 1.859 0.02 1 276 . 40 PRO HG2 H 1.588 0.02 2 277 . 40 PRO HG3 H 0.945 0.02 2 278 . 40 PRO HD2 H 3.65 0.02 2 279 . 40 PRO HD3 H 4.066 0.02 2 280 . 40 PRO CA C 66.08 0.02 1 281 . 41 SER H H 8.604 0.02 1 282 . 41 SER HA H 3.72 0.02 1 283 . 41 SER HB2 H 4.003 0.02 2 284 . 41 SER HB3 H 3.411 0.02 2 285 . 41 SER CA C 58.59 0.02 1 286 . 41 SER N N 108.354 0.02 1 287 . 42 CYS H H 8.095 0.02 1 288 . 42 CYS HA H 3.942 0.02 1 289 . 42 CYS HB2 H 3.517 0.02 1 290 . 42 CYS HB3 H 3.215 0.02 1 291 . 42 CYS CA C 62.77 0.02 1 292 . 42 CYS N N 125.826 0.02 1 293 . 43 ARG H H 8.596 0.02 1 294 . 43 ARG HA H 3.992 0.02 1 295 . 43 ARG HB2 H 1.746 0.02 1 296 . 43 ARG HB3 H 2.066 0.02 1 297 . 43 ARG HG2 H 1.898 0.02 1 298 . 43 ARG HG3 H 1.898 0.02 1 299 . 43 ARG HD2 H 3.244 0.02 1 300 . 43 ARG HD3 H 3.244 0.02 1 301 . 43 ARG CA C 57.21 0.02 1 302 . 43 ARG N N 126.84 0.02 1 303 . 44 ALA H H 8.758 0.02 1 304 . 44 ALA HA H 4.187 0.02 1 305 . 44 ALA HB H 1.516 0.02 1 306 . 44 ALA CA C 53.13 0.02 1 307 . 44 ALA N N 125.52 0.02 1 308 . 45 ARG H H 8.464 0.02 1 309 . 45 ARG HA H 3.941 0.02 1 310 . 45 ARG HB2 H 1.827 0.02 2 311 . 45 ARG HB3 H 1.766 0.02 2 312 . 45 ARG HG2 H 1.73 0.02 1 313 . 45 ARG HG3 H 1.73 0.02 1 314 . 45 ARG HD2 H 3.238 0.02 1 315 . 45 ARG HD3 H 3.238 0.02 1 316 . 45 ARG CA C 56.52 0.02 1 317 . 45 ARG N N 121.201 0.02 1 318 . 46 HIS H H 8.842 0.02 1 319 . 46 HIS HA H 4.789 0.02 1 320 . 46 HIS HB2 H 3.267 0.02 2 321 . 46 HIS HB3 H 3.1 0.02 2 322 . 46 HIS HD2 H 7.19 0.02 1 323 . 46 HIS HE1 H 8.129 0.02 1 324 . 46 HIS N N 123.13 0.02 1 325 . 47 ALA H H 8.248 0.02 1 326 . 47 ALA HA H 4.562 0.02 1 327 . 47 ALA HB H 1.557 0.02 1 328 . 47 ALA CA C 50.53 0.02 1 329 . 47 ALA N N 125.312 0.02 1 330 . 48 LEU H H 8.131 0.02 1 331 . 48 LEU HA H 4.426 0.02 1 332 . 48 LEU HB2 H 1.602 0.02 2 333 . 48 LEU HB3 H 1.688 0.02 2 334 . 48 LEU HG H 1.808 0.02 1 335 . 48 LEU HD1 H 0.985 0.02 1 336 . 48 LEU HD2 H 0.95 0.02 1 337 . 48 LEU CA C 54.53 0.02 1 338 . 48 LEU N N 118.118 0.02 1 339 . 49 ARG H H 8.545 0.02 1 340 . 49 ARG HA H 2.62 0.02 1 341 . 49 ARG HB2 H 1.059 0.02 1 342 . 49 ARG HB3 H 1.374 0.02 1 343 . 49 ARG HG2 H 1.21 0.02 2 344 . 49 ARG HG3 H 0.6 0.02 2 345 . 49 ARG HD2 H 1.92 0.02 2 346 . 49 ARG HD3 H 1.6 0.02 2 347 . 49 ARG CA C 58.33 0.02 1 348 . 49 ARG N N 123.257 0.02 1 349 . 50 GLU H H 9.066 0.02 1 350 . 50 GLU HA H 4.094 0.02 1 351 . 50 GLU HB2 H 2.104 0.02 2 352 . 50 GLU HB3 H 1.97 0.02 2 353 . 50 GLU HG2 H 2.014 0.02 1 354 . 50 GLU HG3 H 2.014 0.02 1 355 . 50 GLU CA C 58.17 0.02 1 356 . 50 GLU N N 115.035 0.02 1 357 . 51 ASN H H 8.014 0.02 1 358 . 51 ASN HA H 5.08 0.02 1 359 . 51 ASN HB2 H 3.181 0.02 1 360 . 51 ASN HB3 H 2.807 0.02 1 361 . 51 ASN HD21 H 7.760 0.02 1 362 . 51 ASN HD22 H 7.427 0.02 1 363 . 51 ASN CA C 52.6 0.02 1 364 . 51 ASN N N 116.576 0.02 1 365 . 51 ASN ND2 N 124.1 0.02 1 366 . 52 VAL H H 7.591 0.02 1 367 . 52 VAL HA H 5.089 0.02 1 368 . 52 VAL HB H 1.662 0.02 1 369 . 52 VAL HG1 H 0.873 0.02 1 370 . 52 VAL HG2 H 0.585 0.02 1 371 . 52 VAL CA C 61.67 0.02 1 372 . 52 VAL N N 121.22 0.02 1 373 . 53 SER H H 8.852 0.02 1 374 . 53 SER HA H 4.45 0.02 1 375 . 53 SER HB2 H 3.665 0.02 1 376 . 53 SER HB3 H 3.427 0.02 1 377 . 53 SER CA C 56.4 0.02 1 378 . 53 SER N N 121.712 0.02 1 379 . 54 PHE H H 8.562 0.02 1 380 . 54 PHE HA H 5.375 0.02 1 381 . 54 PHE HB2 H 2.724 0.02 1 382 . 54 PHE HB3 H 2.823 0.02 1 383 . 54 PHE HD1 H 7.183 0.02 1 384 . 54 PHE HD2 H 7.183 0.02 1 385 . 54 PHE HE1 H 7.122 0.02 1 386 . 54 PHE HE2 H 7.122 0.02 1 387 . 54 PHE HZ H 7.159 0.02 1 388 . 54 PHE CA C 57.1 0.02 1 389 . 54 PHE N N 119.329 0.02 1 390 . 55 TYR H H 8.636 0.02 1 391 . 55 TYR HA H 4.729 0.02 1 392 . 55 TYR HB2 H 3.161 0.02 1 393 . 55 TYR HB3 H 2.212 0.02 1 394 . 55 TYR HD1 H 6.727 0.02 1 395 . 55 TYR HD2 H 6.727 0.02 1 396 . 55 TYR HE1 H 6.457 0.02 1 397 . 55 TYR HE2 H 6.457 0.02 1 398 . 55 TYR CA C 57.16 0.02 1 399 . 55 TYR N N 117.616 0.02 1 400 . 56 ALA H H 9.134 0.02 1 401 . 56 ALA HA H 4.3 0.02 1 402 . 56 ALA HB H 1.529 0.02 1 403 . 56 ALA CA C 54.59 0.02 1 404 . 56 ALA N N 122.77 0.02 1 405 . 57 ASN H H 7.197 0.02 1 406 . 57 ASN HA H 4.509 0.02 1 407 . 57 ASN HB2 H 3.024 0.02 1 408 . 57 ASN HB3 H 3.194 0.02 1 409 . 57 ASN HD21 H 7.053 0.02 1 410 . 57 ASN HD22 H 7.666 0.02 1 411 . 57 ASN N N 104.243 0.02 1 412 . 57 ASN ND2 N 115.7 0.02 1 413 . 58 ALA H H 8.93 0.02 1 414 . 58 ALA HA H 3.577 0.02 1 415 . 58 ALA HB H 1.534 0.02 1 416 . 58 ALA CA C 54.55 0.02 1 417 . 58 ALA N N 120.682 0.02 1 418 . 59 SER H H 8.31 0.02 1 419 . 59 SER HA H 4.073 0.02 1 420 . 59 SER HB2 H 3.9 0.02 1 421 . 59 SER HB3 H 3.9 0.02 1 422 . 59 SER CA C 62.38 0.02 1 423 . 59 SER N N 113.493 0.02 1 424 . 60 GLU H H 8.162 0.02 1 425 . 60 GLU HA H 3.986 0.02 1 426 . 60 GLU HB2 H 2.241 0.02 2 427 . 60 GLU HB3 H 2.047 0.02 2 428 . 60 GLU HG2 H 2.609 0.02 2 429 . 60 GLU HG3 H 2.361 0.02 2 430 . 60 GLU CA C 59.11 0.02 1 431 . 60 GLU N N 122.545 0.02 1 432 . 61 ALA H H 6.886 0.02 1 433 . 61 ALA HA H 2.674 0.02 1 434 . 61 ALA HB H -0.09 0.02 1 435 . 61 ALA CA C 54.35 0.02 1 436 . 61 ALA N N 122.229 0.02 1 437 . 62 LEU H H 8.222 0.02 1 438 . 62 LEU HA H 4.473 0.02 1 439 . 62 LEU HB2 H 1.834 0.02 2 440 . 62 LEU HB3 H 1.543 0.02 2 441 . 62 LEU HG H 1.776 0.02 1 442 . 62 LEU HD1 H 1.226 0.02 1 443 . 62 LEU HD2 H 1.005 0.02 1 444 . 62 LEU CA C 57.26 0.02 1 445 . 62 LEU N N 120.155 0.02 1 446 . 63 ALA H H 7.817 0.02 1 447 . 63 ALA HA H 4.087 0.02 1 448 . 63 ALA HB H 1.463 0.02 1 449 . 63 ALA CA C 54.37 0.02 1 450 . 63 ALA N N 122.743 0.02 1 451 . 64 ALA H H 7.141 0.02 1 452 . 64 ALA HA H 4.338 0.02 1 453 . 64 ALA HB H 1.446 0.02 1 454 . 64 ALA CA C 51.73 0.02 1 455 . 64 ALA N N 118.632 0.02 1 456 . 65 GLY H H 7.707 0.02 1 457 . 65 GLY HA2 H 4.041 0.02 2 458 . 65 GLY HA3 H 3.612 0.02 2 459 . 65 GLY CA C 44.75 0.02 1 460 . 65 GLY N N 105.302 0.02 1 461 . 66 PHE H H 7.701 0.02 1 462 . 66 PHE HA H 4.635 0.02 1 463 . 66 PHE HB2 H 2.521 0.02 1 464 . 66 PHE HB3 H 2.992 0.02 1 465 . 66 PHE HD1 H 6.956 0.02 1 466 . 66 PHE HD2 H 6.956 0.02 1 467 . 66 PHE HE1 H 7.278 0.02 1 468 . 66 PHE HE2 H 7.278 0.02 1 469 . 66 PHE HZ H 7.342 0.02 1 470 . 66 PHE CA C 58.03 0.02 1 471 . 66 PHE N N 119.148 0.02 1 472 . 67 ARG H H 9.158 0.02 1 473 . 67 ARG HA H 5.073 0.02 1 474 . 67 ARG HB2 H 1.845 0.02 1 475 . 67 ARG HB3 H 1.845 0.02 1 476 . 67 ARG HG2 H 1.75 0.02 1 477 . 67 ARG HG3 H 1.75 0.02 1 478 . 67 ARG HD2 H 3.208 0.02 1 479 . 67 ARG HD3 H 3.208 0.02 1 480 . 67 ARG CA C 52.37 0.02 1 481 . 67 ARG N N 120.174 0.02 1 482 . 68 PRO HA H 2.791 0.02 1 483 . 68 PRO HB2 H 1.637 0.02 2 484 . 68 PRO HB3 H 1.457 0.02 2 485 . 68 PRO HG2 H 1.96 0.02 2 486 . 68 PRO HG3 H 2.214 0.02 2 487 . 68 PRO HD2 H 3.704 0.02 1 488 . 68 PRO HD3 H 3.704 0.02 1 489 . 68 PRO CA C 62.07 0.02 1 490 . 69 CYS H H 7.946 0.02 1 491 . 69 CYS HA H 3.915 0.02 1 492 . 69 CYS HB2 H 3.233 0.02 1 493 . 69 CYS HB3 H 3.28 0.02 1 494 . 69 CYS CA C 60 0.02 1 495 . 69 CYS N N 127.368 0.02 1 496 . 70 LYS H H 8.908 0.02 1 497 . 70 LYS HA H 4.174 0.02 1 498 . 70 LYS HB2 H 1.935 0.02 2 499 . 70 LYS HB3 H 1.826 0.02 2 500 . 70 LYS CA C 57.79 0.02 1 501 . 70 LYS N N 127.882 0.02 1 502 . 71 ARG H H 9.698 0.02 1 503 . 71 ARG HA H 4.319 0.02 1 504 . 71 ARG HB2 H 1.862 0.02 2 505 . 71 ARG HB3 H 1.962 0.02 2 506 . 71 ARG HG2 H 1.676 0.02 2 507 . 71 ARG HG3 H 1.642 0.02 2 508 . 71 ARG HD2 H 3.167 0.02 2 509 . 71 ARG HD3 H 3.068 0.02 2 510 . 71 ARG CA C 58.07 0.02 1 511 . 71 ARG N N 122.745 0.02 1 512 . 72 CYS H H 8.538 0.02 1 513 . 72 CYS HA H 4.859 0.02 1 514 . 72 CYS HB2 H 3.11 0.02 1 515 . 72 CYS HB3 H 3.035 0.02 1 516 . 72 CYS CA C 59.19 0.02 1 517 . 72 CYS N N 118.118 0.02 1 518 . 73 GLN H H 7.542 0.02 1 519 . 73 GLN HA H 4.24 0.02 1 520 . 73 GLN HB2 H 2.17 0.02 2 521 . 73 GLN HB3 H 1.95 0.02 2 522 . 73 GLN HG2 H 2.27 0.02 2 523 . 73 GLN HG3 H 2.11 0.02 2 524 . 73 GLN HE21 H 7.39 0.02 1 525 . 73 GLN HE22 H 6.69 0.02 1 526 . 73 GLN CA C 56.23 0.02 1 527 . 73 GLN N N 117.64 0.02 1 528 . 73 GLN NE2 N 112.0 0.02 1 529 . 74 PRO HA H 4.27 0.02 1 530 . 74 PRO HB2 H 2.324 0.02 2 531 . 74 PRO HB3 H 1.91 0.02 2 532 . 74 PRO HG2 H 2.173 0.02 1 533 . 74 PRO HG3 H 2.173 0.02 1 534 . 74 PRO HD2 H 3.69 0.02 1 535 . 74 PRO HD3 H 3.69 0.02 1 536 . 74 PRO CA C 64.54 0.02 1 537 . 75 ASP H H 9.72 0.02 1 538 . 75 ASP HA H 4.372 0.02 1 539 . 75 ASP HB2 H 2.292 0.02 2 540 . 75 ASP HB3 H 2.843 0.02 2 541 . 75 ASP CA C 53.6 0.02 1 542 . 75 ASP N N 117.09 0.02 1 543 . 76 LYS H H 7.507 0.02 1 544 . 76 LYS HA H 4.425 0.02 1 545 . 76 LYS HB2 H 1.847 0.02 2 546 . 76 LYS HB3 H 1.738 0.02 2 547 . 76 LYS HG2 H 1.42 0.02 2 548 . 76 LYS HG3 H 1.33 0.02 2 549 . 76 LYS HD2 H 1.627 0.02 1 550 . 76 LYS HD3 H 1.627 0.02 1 551 . 76 LYS CA C 55 0.02 1 552 . 76 LYS N N 120.758 0.02 1 553 . 77 ALA H H 7.98 0.02 1 554 . 77 ALA HA H 4.279 0.02 1 555 . 77 ALA HB H 1.357 0.02 1 556 . 77 ALA CA C 52.39 0.02 1 557 . 77 ALA N N 124.982 0.02 1 558 . 78 ASN H H 8.38 0.02 1 559 . 78 ASN HA H 4.976 0.02 1 560 . 78 ASN HB2 H 2.84 0.02 2 561 . 78 ASN HB3 H 2.68 0.02 2 562 . 78 ASN HD21 H 7.674 0.02 1 563 . 78 ASN HD22 H 6.962 0.02 1 564 . 78 ASN CA C 51.19 0.02 1 565 . 78 ASN N N 119.366 0.02 1 566 . 78 ASN ND2 N 113.2 0.02 1 567 . 79 PRO HA H 4.436 0.02 1 568 . 79 PRO HB2 H 2.29 0.02 2 569 . 79 PRO HB3 H 1.94 0.02 2 570 . 79 PRO HG2 H 2.027 0.02 1 571 . 79 PRO HG3 H 2.027 0.02 1 572 . 79 PRO HD2 H 3.756 0.02 1 573 . 79 PRO HD3 H 3.756 0.02 1 574 . 79 PRO CA C 63.44 0.02 1 575 . 80 ARG H H 8.377 0.02 1 576 . 80 ARG HA H 4.274 0.02 1 577 . 80 ARG HB2 H 1.858 0.02 2 578 . 80 ARG HB3 H 1.753 0.02 2 579 . 80 ARG HG2 H 1.65 0.02 1 580 . 80 ARG HG3 H 1.65 0.02 1 581 . 80 ARG HD2 H 3.24 0.02 1 582 . 80 ARG HD3 H 3.24 0.02 1 583 . 80 ARG CA C 56.24 0.02 1 584 . 80 ARG N N 120.783 0.02 1 585 . 81 GLN H H 8.263 0.02 1 586 . 81 GLN HA H 4.261 0.02 1 587 . 81 GLN HB2 H 2.025 0.02 2 588 . 81 GLN HB3 H 1.974 0.02 2 589 . 81 GLN HG2 H 2.324 0.02 1 590 . 81 GLN HG3 H 2.324 0.02 1 591 . 81 GLN HE21 H 7.570 0.02 1 592 . 81 GLN HE22 H 6.906 0.02 1 593 . 81 GLN CA C 55.9 0.02 1 594 . 81 GLN N N 121.201 0.02 1 595 . 81 GLN NE2 N 112.7 0.02 1 596 . 82 HIS H H 8.43 0.02 1 597 . 82 HIS HA H 4.688 0.02 1 598 . 82 HIS HB2 H 3.2 0.02 2 599 . 82 HIS HB3 H 3.12 0.02 2 600 . 82 HIS CA C 55.56 0.02 1 601 . 82 HIS N N 120.82 0.02 1 602 . 83 ARG H H 8.357 0.02 1 603 . 83 ARG HA H 4.33 0.02 1 604 . 83 ARG HB2 H 1.84 0.02 2 605 . 83 ARG HB3 H 1.77 0.02 2 606 . 83 ARG HG2 H 1.457 0.02 1 607 . 83 ARG HG3 H 1.457 0.02 1 608 . 83 ARG HD2 H 3.02 0.02 1 609 . 83 ARG HD3 H 3.02 0.02 1 610 . 83 ARG CA C 56.26 0.02 1 611 . 83 ARG N N 124.771 0.02 1 612 . 84 LEU H H 8.468 0.02 1 613 . 84 LEU HA H 4.38 0.02 1 614 . 84 LEU HB2 H 1.631 0.02 1 615 . 84 LEU HB3 H 1.631 0.02 1 616 . 84 LEU HD1 H 0.95 0.02 1 617 . 84 LEU HD2 H 0.89 0.02 1 618 . 84 LEU CA C 55.05 0.02 1 619 . 84 LEU N N 123.257 0.02 1 620 . 85 ASP H H 8.326 0.02 1 621 . 85 ASP HA H 4.594 0.02 1 622 . 85 ASP HB2 H 2.679 0.02 2 623 . 85 ASP HB3 H 2.65 0.02 2 624 . 85 ASP CA C 54.26 0.02 1 625 . 85 ASP N N 120.687 0.02 1 626 . 86 LYS H H 8.153 0.02 1 627 . 86 LYS HA H 4.34 0.02 1 628 . 86 LYS HB2 H 1.88 0.02 2 629 . 86 LYS HB3 H 1.75 0.02 2 630 . 86 LYS CA C 56.12 0.02 1 631 . 86 LYS N N 121.307 0.02 1 632 . 87 ILE H H 8.17 0.02 1 633 . 87 ILE HA H 4.23 0.02 1 634 . 87 ILE HB H 1.86 0.02 1 635 . 87 ILE HG12 H 1.46 0.02 2 636 . 87 ILE HG13 H 1.20 0.02 2 637 . 87 ILE HG2 H 0.85 0.02 1 638 . 87 ILE HD1 H 0.65 0.02 1 639 . 87 ILE CA C 61.11 0.02 1 640 . 87 ILE N N 122.539 0.02 1 641 . 88 THR H H 8.22 0.02 1 642 . 88 THR HA H 4.35 0.02 1 643 . 88 THR HB H 4.21 0.02 1 644 . 88 THR HG2 H 1.19 0.02 1 645 . 88 THR CA C 61.73 0.02 1 646 . 88 THR N N 118.503 0.02 1 647 . 89 HIS H H 8.078 0.02 1 648 . 89 HIS HA H 4.48 0.02 1 649 . 89 HIS HB2 H 3.25 0.02 2 650 . 89 HIS HB3 H 3.11 0.02 2 651 . 89 HIS CA C 57 0.02 1 652 . 89 HIS N N 126.34 0.02 1 653 . 90 ALA CA C 54.72 0.02 1 stop_ save_