data_6354 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; 1H, 13C and 15N resonance assignments and 15N-1H residual dipolar couplings for NECAP1 protein ; _BMRB_accession_number 6354 _BMRB_flat_file_name bmr6354.str _Entry_type original _Submission_date 2004-10-13 _Accession_date 2004-10-14 _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 Denisov Alexei Yu. . 2 Gehring Kalle . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 residual_dipolar_couplings 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 531 "13C chemical shifts" 498 "15N chemical shifts" 124 "residual dipolar couplings" 121 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2008-07-01 update BMRB 'update entry citation' 2006-01-08 original author 'original release' stop_ save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title 'Solution structure of NECAP1 protein' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 17762867 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Ritter Brigitte . . 2 Denisov Alexey Yu. . 3 Philie Jacynthe . . 4 Allaire Patrick D . 5 Legendre-Guillemin Valerie . . 6 Zylbergold Peter . . 7 Gehring Kalle . . 8 McPherson Peter S. . stop_ _Journal_abbreviation 'EMBO J.' _Journal_volume 26 _Journal_issue 18 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 4066 _Page_last 4077 _Year 2007 _Details . loop_ _Keyword NECAP1 'NMR assignments' RDC stop_ save_ ################################## # Molecular system description # ################################## save_system_NECAP1 _Saveframe_category molecular_system _Mol_system_name 'N-terminal domain of NECAP1 protein' _Abbreviation_common NECAP1 _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'NECAP1 monomer' $NECAP1_monomer 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_NECAP1_monomer _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'NECAP1 protein' _Abbreviation_common NECAP1 _Molecular_mass . _Mol_thiol_state 'all free' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 133 _Mol_residue_sequence ; MAAELEYESVLCVKPDVSVY RIPPRASNRGYRASDWKLDQ PDWTGRLRITSKGKIAYIKL EDKVSGELFAQAPVEQYPGI AVETVTDSSRYFVIRIQDGT GRSAFIGIGFTDRGDAFDFN VSLQDHFKWVKQE ; loop_ _Residue_seq_code _Residue_label 1 MET 2 ALA 3 ALA 4 GLU 5 LEU 6 GLU 7 TYR 8 GLU 9 SER 10 VAL 11 LEU 12 CYS 13 VAL 14 LYS 15 PRO 16 ASP 17 VAL 18 SER 19 VAL 20 TYR 21 ARG 22 ILE 23 PRO 24 PRO 25 ARG 26 ALA 27 SER 28 ASN 29 ARG 30 GLY 31 TYR 32 ARG 33 ALA 34 SER 35 ASP 36 TRP 37 LYS 38 LEU 39 ASP 40 GLN 41 PRO 42 ASP 43 TRP 44 THR 45 GLY 46 ARG 47 LEU 48 ARG 49 ILE 50 THR 51 SER 52 LYS 53 GLY 54 LYS 55 ILE 56 ALA 57 TYR 58 ILE 59 LYS 60 LEU 61 GLU 62 ASP 63 LYS 64 VAL 65 SER 66 GLY 67 GLU 68 LEU 69 PHE 70 ALA 71 GLN 72 ALA 73 PRO 74 VAL 75 GLU 76 GLN 77 TYR 78 PRO 79 GLY 80 ILE 81 ALA 82 VAL 83 GLU 84 THR 85 VAL 86 THR 87 ASP 88 SER 89 SER 90 ARG 91 TYR 92 PHE 93 VAL 94 ILE 95 ARG 96 ILE 97 GLN 98 ASP 99 GLY 100 THR 101 GLY 102 ARG 103 SER 104 ALA 105 PHE 106 ILE 107 GLY 108 ILE 109 GLY 110 PHE 111 THR 112 ASP 113 ARG 114 GLY 115 ASP 116 ALA 117 PHE 118 ASP 119 PHE 120 ASN 121 VAL 122 SER 123 LEU 124 GLN 125 ASP 126 HIS 127 PHE 128 LYS 129 TRP 130 VAL 131 LYS 132 GLN 133 GLU 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 tpg|DAA01433.1| DAA01433 'TPA_exp: adaptin-ear-binding coat-associated protein 1 [Mus musculus]' 100.00 275 100.00 100.00 8.25e-74 SWISS-PROT Q9CR95 'Adaptin ear-binding coat-associated protein 1 (NECAP endocytosis-associated protein 1) (NECAP-1)' 100.00 275 100.00 100.00 8.25e-74 SWISS-PROT Q8NC96 'Adaptin ear-binding coat-associated protein 1 (NECAP endocytosis-associated protein 1) (NECAP-1)' 100.00 275 98.50 98.50 1.36e-72 SWISS-PROT Q5R630 'Adaptin ear-binding coat-associated protein 1 (NECAP endocytosis-associated protein 1) (NECAP-1)' 100.00 275 99.25 99.25 3.70e-73 SWISS-PROT P69682 'Adaptin ear-binding coat-associated protein 1 (NECAP endocytosis-associated protein 1) (NECAP-1)' 100.00 277 99.25 99.25 2.36e-73 REF XP_001113344 'PREDICTED: similar to adaptin-ear-binding coat-associated protein 1 isoform 2 [Macaca mulatta]' 100.00 275 100.00 100.00 1.35e-73 REF XP_001113313 'PREDICTED: similar to adaptin-ear-binding coat-associated protein 1 isoform 1 [Macaca mulatta]' 100.00 275 100.00 100.00 1.35e-73 REF NP_080543 'NECAP endocytosis associated 1 [Mus musculus]' 100.00 275 100.00 100.00 8.25e-74 REF NP_056324 'NECAP endocytosis associated 1 [Homo sapiens]' 100.00 275 98.50 98.50 1.36e-72 REF NP_001025090 'adaptin ear-binding clathrin-associated protein [Rattus norvegicus]' 100.00 277 99.25 99.25 2.36e-73 GenBank AAI20842 'NECAP endocytosis associated 1 [Mus musculus]' 100.00 275 100.00 100.00 8.25e-74 GenBank AAI19134 'NECAP endocytosis associated 1 [Mus musculus]' 100.00 275 100.00 100.00 8.25e-74 GenBank AAI10877 'NECAP endocytosis associated 1 [Homo sapiens]' 100.00 275 98.50 98.50 1.36e-72 GenBank AAH97496 'NECAP endocytosis associated 1 [Rattus norvegicus]' 100.00 277 99.25 99.25 2.36e-73 GenBank AAH11466 'NECAP endocytosis associated 1 [Mus musculus]' 100.00 275 100.00 100.00 8.25e-74 EMBL CAH92786 'hypothetical protein [Pongo abelii]' 100.00 275 99.25 99.25 3.70e-73 EMBL CAH92713 'hypothetical protein [Pongo abelii]' 100.00 275 99.25 99.25 3.96e-73 DBJ BAC11296 'unnamed protein product [Homo sapiens]' 100.00 275 98.50 98.50 1.36e-72 DBJ BAC11264 'unnamed protein product [Homo sapiens]' 100.00 275 98.50 98.50 1.42e-72 DBJ BAC11250 'unnamed protein product [Homo sapiens]' 100.00 275 98.50 98.50 1.35e-72 DBJ BAB23915 'unnamed protein product [Mus musculus]' 100.00 275 100.00 100.00 8.25e-74 DBJ BAB23577 'unnamed protein product [Mus musculus]' 100.00 275 100.00 100.00 8.25e-74 PDB 1TQZ 'Solution Structure Of Necap1 Protein' 100.00 133 100.00 100.00 2.00e-72 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $NECAP1_monomer Mouse 10090 Eukaryota Metazoa Mus musculus stop_ save_ ######################### # Experimental source # ######################### save_experimental_source _Saveframe_category experimental_source loop_ _Mol_label _Production_method _Host_organism_name_common _Genus _Species _Strain _Vector_type _Vector_name $NECAP1_monomer 'recombinant technology' 'E. coli' Escherichia coli BL21Gold plasmid pGEX-4T1 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 _Isotopic_labeling $NECAP1_monomer 1.4 mM '[U-99% 13C; U-99% 15N]' 'sodium phosphate buffer' 25 mM . NaCl 75 mM . stop_ save_ save_sample_2 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $NECAP1_monomer 1.4 mM '[U-99% 15N]' 'sodium phosphate buffer' 25 mM . NaCl 75 mM . stop_ save_ save_sample_3 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $NECAP1_monomer 0.6 mM '[U-99% 15N]' 'sodium phosphate buffer' 25 mM . NaCl 75 mM . 'Pf1 phage' 8.0 mg/mL . stop_ save_ ############################ # Computer software used # ############################ save_XWINNMR _Saveframe_category software _Name XWINNMR _Version 3.5 loop_ _Task 'collection, processing' stop_ _Details 'Bruker firm' save_ save_XEASY _Saveframe_category software _Name XEASY _Version 1.3.13 loop_ _Task 'data analysis' stop_ _Details 'Bartels et al.' save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model DRX _Field_strength 600 _Details . save_ ############################# # NMR applied experiments # ############################# save_IPAP-HSQC_1 _Saveframe_category NMR_applied_experiment _Experiment_name IPAP-HSQC _Sample_label . save_ ####################### # Sample conditions # ####################### save_Ex-cond_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 7.2 0.1 pH temperature 303 0.5 K 'ionic strength' 0.10 . M 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 0.0 internal direct . . . 1.0 $entry_citation $entry_citation DSS N 15 'methyl protons' ppm 0.0 . 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_ _Sample_label $sample_1 $sample_2 stop_ _Sample_conditions_label $Ex-cond_1 _Chem_shift_reference_set_label $chemical_shift_reference _Mol_system_component_name 'NECAP1 monomer' _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 . 1 MET CB C 32.5 0.20 1 2 . 1 MET CA C 55.5 0.20 1 3 . 1 MET CG C 31.8 0.20 1 4 . 1 MET C C 175.9 0.20 1 5 . 1 MET HA H 4.43 0.01 1 6 . 1 MET HB2 H 1.96 0.01 2 7 . 1 MET HG2 H 2.50 0.01 2 8 . 2 ALA N N 124.8 0.25 1 9 . 2 ALA H H 8.26 0.01 1 10 . 2 ALA CB C 18.8 0.20 1 11 . 2 ALA CA C 52.7 0.20 1 12 . 2 ALA C C 177.5 0.20 1 13 . 2 ALA HA H 4.18 0.01 1 14 . 2 ALA HB H 1.31 0.01 1 15 . 3 ALA N N 122.6 0.25 1 16 . 3 ALA H H 8.15 0.01 1 17 . 3 ALA CB C 18.9 0.20 1 18 . 3 ALA CA C 52.8 0.20 1 19 . 3 ALA C C 177.9 0.20 1 20 . 3 ALA HA H 4.20 0.01 1 21 . 3 ALA HB H 1.31 0.01 1 22 . 4 GLU N N 118.8 0.25 1 23 . 4 GLU H H 8.25 0.01 1 24 . 4 GLU CB C 29.9 0.20 1 25 . 4 GLU CA C 56.7 0.20 1 26 . 4 GLU CG C 36.3 0.20 1 27 . 4 GLU C C 176.5 0.20 1 28 . 4 GLU HA H 4.18 0.01 1 29 . 4 GLU HB2 H 1.95 0.01 2 30 . 4 GLU HG2 H 2.22 0.01 2 31 . 5 LEU N N 121.8 0.25 1 32 . 5 LEU H H 7.99 0.01 1 33 . 5 LEU CB C 42.2 0.20 1 34 . 5 LEU CA C 55.1 0.20 1 35 . 5 LEU CG C 26.8 0.20 1 36 . 5 LEU CD1 C 24.9 0.20 2 37 . 5 LEU CD2 C 23.2 0.20 2 38 . 5 LEU C C 177.0 0.20 1 39 . 5 LEU HA H 4.23 0.01 1 40 . 5 LEU HG H 1.53 0.01 1 41 . 5 LEU HD1 H 0.82 0.01 2 42 . 6 GLU N N 120.2 0.25 1 43 . 6 GLU H H 8.04 0.01 1 44 . 6 GLU CB C 30.4 0.20 1 45 . 6 GLU CA C 56.1 0.20 1 46 . 6 GLU CG C 36.3 0.20 1 47 . 6 GLU C C 175.5 0.20 1 48 . 6 GLU HA H 4.23 0.01 1 49 . 6 GLU HB2 H 1.86 0.01 2 50 . 6 GLU HG2 H 2.10 0.01 2 51 . 7 TYR N N 120.9 0.25 1 52 . 7 TYR H H 7.99 0.01 1 53 . 7 TYR CB C 39.0 0.20 1 54 . 7 TYR CA C 57.7 0.20 1 55 . 7 TYR C C 174.7 0.20 1 56 . 7 TYR HA H 4.50 0.01 1 57 . 7 TYR HB2 H 2.93 0.01 2 58 . 7 TYR HD1 H 7.02 0.01 3 59 . 8 GLU N N 123.7 0.25 1 60 . 8 GLU H H 8.21 0.01 1 61 . 8 GLU CB C 31.7 0.20 1 62 . 8 GLU CA C 55.1 0.20 1 63 . 8 GLU CG C 36.4 0.20 1 64 . 8 GLU C C 175.5 0.20 1 65 . 8 GLU HA H 4.89 0.01 1 66 . 8 GLU HB2 H 1.74 0.01 2 67 . 8 GLU HG2 H 2.03 0.01 2 68 . 9 SER N N 119.7 0.25 1 69 . 9 SER H H 8.55 0.01 1 70 . 9 SER CB C 64.4 0.20 1 71 . 9 SER CA C 57.3 0.20 1 72 . 9 SER C C 173.2 0.20 1 73 . 9 SER HA H 4.64 0.01 1 74 . 9 SER HB2 H 3.76 0.01 2 75 . 10 VAL N N 123.4 0.25 1 76 . 10 VAL H H 8.69 0.01 1 77 . 10 VAL CB C 32.0 0.20 1 78 . 10 VAL CA C 63.1 0.20 1 79 . 10 VAL CG1 C 21.5 0.20 1 80 . 10 VAL C C 175.8 0.20 1 81 . 10 VAL HA H 4.09 0.01 1 82 . 10 VAL HB H 1.99 0.01 1 83 . 10 VAL HG1 H 0.86 0.01 2 84 . 11 LEU N N 126.6 0.25 1 85 . 11 LEU H H 9.17 0.01 1 86 . 11 LEU CB C 42.7 0.20 1 87 . 11 LEU CA C 55.5 0.20 1 88 . 11 LEU CG C 27.1 0.20 1 89 . 11 LEU CD1 C 24.5 0.20 2 90 . 11 LEU CD2 C 22.0 0.20 2 91 . 11 LEU C C 177.2 0.20 1 92 . 11 LEU HA H 4.38 0.01 1 93 . 11 LEU HB2 H 1.34 0.01 2 94 . 11 LEU HD1 H 0.66 0.01 2 95 . 11 LEU HD2 H 0.50 0.01 2 96 . 12 CYS N N 116.5 0.25 1 97 . 12 CYS H H 7.42 0.01 1 98 . 12 CYS CB C 29.2 0.20 1 99 . 12 CYS CA C 58.6 0.20 1 100 . 12 CYS C C 172.1 0.20 1 101 . 12 CYS HA H 4.48 0.01 1 102 . 12 CYS HB2 H 3.16 0.01 2 103 . 12 CYS HB3 H 2.24 0.01 2 104 . 13 VAL N N 128.1 0.25 1 105 . 13 VAL H H 8.73 0.01 1 106 . 13 VAL CB C 34.5 0.20 1 107 . 13 VAL CA C 61.7 0.20 1 108 . 13 VAL CG1 C 20.7 0.20 1 109 . 13 VAL C C 175.2 0.20 1 110 . 13 VAL HA H 4.88 0.01 1 111 . 13 VAL HB H 1.96 0.01 1 112 . 13 VAL HG1 H 0.87 0.01 2 113 . 14 LYS N N 126.0 0.25 1 114 . 14 LYS H H 9.62 0.01 1 115 . 14 LYS CB C 34.0 0.20 1 116 . 14 LYS CA C 49.8 0.20 1 117 . 14 LYS C C 174.1 0.20 1 118 . 14 LYS HA H 5.21 0.01 1 119 . 14 LYS HB2 H 1.55 0.01 2 120 . 15 PRO CB C 32.7 0.20 1 121 . 15 PRO CA C 63.7 0.20 1 122 . 15 PRO CG C 26.6 0.20 1 123 . 15 PRO CD C 51.1 0.20 1 124 . 15 PRO C C 175.0 0.20 1 125 . 15 PRO HA H 4.38 0.01 1 126 . 15 PRO HB2 H 2.04 0.01 2 127 . 15 PRO HB3 H 2.17 0.01 2 128 . 16 ASP N N 115.5 0.25 1 129 . 16 ASP H H 7.85 0.01 1 130 . 16 ASP CB C 43.4 0.20 1 131 . 16 ASP CA C 54.3 0.20 1 132 . 16 ASP C C 174.2 0.20 1 133 . 16 ASP HA H 4.93 0.01 1 134 . 16 ASP HB2 H 2.51 0.01 2 135 . 17 VAL N N 124.8 0.25 1 136 . 17 VAL H H 8.84 0.01 1 137 . 17 VAL CB C 34.5 0.20 1 138 . 17 VAL CA C 60.9 0.20 1 139 . 17 VAL CG1 C 22.3 0.20 1 140 . 17 VAL CG2 C 20.6 0.20 1 141 . 17 VAL C C 173.0 0.20 1 142 . 17 VAL HA H 4.36 0.01 1 143 . 17 VAL HB H 1.62 0.01 1 144 . 17 VAL HG1 H 0.87 0.01 2 145 . 17 VAL HG2 H 0.54 0.01 2 146 . 18 SER N N 119.9 0.25 1 147 . 18 SER H H 8.04 0.01 1 148 . 18 SER CB C 66.3 0.20 1 149 . 18 SER CA C 57.8 0.20 1 150 . 18 SER C C 172.0 0.20 1 151 . 18 SER HA H 5.02 0.01 1 152 . 18 SER HB2 H 3.62 0.01 2 153 . 18 SER HB3 H 3.47 0.01 2 154 . 19 VAL N N 121.5 0.25 1 155 . 19 VAL H H 8.50 0.01 1 156 . 19 VAL CB C 34.7 0.20 1 157 . 19 VAL CA C 60.3 0.20 1 158 . 19 VAL CG1 C 24.2 0.20 1 159 . 19 VAL CG2 C 21.3 0.20 1 160 . 19 VAL C C 173.2 0.20 1 161 . 19 VAL HA H 5.07 0.01 1 162 . 19 VAL HB H 1.98 0.01 1 163 . 19 VAL HG1 H 0.91 0.01 2 164 . 19 VAL HG2 H 0.65 0.01 2 165 . 20 TYR N N 124.4 0.25 1 166 . 20 TYR H H 8.99 0.01 1 167 . 20 TYR CB C 41.5 0.20 1 168 . 20 TYR CA C 56.3 0.20 1 169 . 20 TYR C C 175.3 0.20 1 170 . 20 TYR HA H 4.82 0.01 1 171 . 20 TYR HB2 H 2.77 0.01 2 172 . 21 ARG N N 123.7 0.25 1 173 . 21 ARG H H 8.74 0.01 1 174 . 21 ARG CB C 29.0 0.20 1 175 . 21 ARG CA C 56.1 0.20 1 176 . 21 ARG CG C 27.4 0.20 1 177 . 21 ARG CD C 43.3 0.20 1 178 . 21 ARG C C 176.4 0.20 1 179 . 21 ARG HA H 4.43 0.01 1 180 . 21 ARG HB2 H 2.03 0.01 2 181 . 21 ARG HG2 H 1.51 0.01 2 182 . 21 ARG HD2 H 3.14 0.01 2 183 . 22 ILE N N 119.8 0.25 1 184 . 22 ILE H H 7.99 0.01 1 185 . 22 ILE CB C 38.4 0.20 1 186 . 22 ILE CA C 58.5 0.20 1 187 . 22 ILE C C 173.7 0.20 1 188 . 22 ILE HA H 4.36 0.01 1 189 . 22 ILE HG2 H 0.29 0.01 1 190 . 22 ILE HD1 H -0.30 0.01 1 191 . 24 PRO CB C 31.7 0.20 1 192 . 24 PRO CA C 62.7 0.20 1 193 . 24 PRO CG C 27.5 0.20 1 194 . 24 PRO CD C 50.1 0.20 1 195 . 24 PRO C C 176.6 0.20 1 196 . 24 PRO HA H 4.43 0.01 1 197 . 24 PRO HB2 H 2.31 0.01 2 198 . 24 PRO HB3 H 2.03 0.01 2 199 . 24 PRO HD2 H 3.81 0.01 2 200 . 24 PRO HD3 H 3.60 0.01 2 201 . 25 ARG N N 122.0 0.25 1 202 . 25 ARG H H 8.15 0.01 1 203 . 25 ARG CB C 30.9 0.20 1 204 . 25 ARG CA C 56.3 0.20 1 205 . 25 ARG C C 176.0 0.20 1 206 . 25 ARG HA H 4.04 0.01 1 207 . 25 ARG HB2 H 1.79 0.01 2 208 . 25 ARG HG2 H 1.53 0.01 2 209 . 28 ASN CB C 37.7 0.20 1 210 . 28 ASN CA C 53.3 0.20 1 211 . 28 ASN C C 174.7 0.20 1 212 . 28 ASN HA H 4.48 0.01 1 213 . 28 ASN HB2 H 2.75 0.01 2 214 . 29 ARG N N 118.3 0.25 1 215 . 29 ARG H H 7.68 0.01 1 216 . 29 ARG CB C 31.0 0.20 1 217 . 29 ARG CA C 55.8 0.20 1 218 . 29 ARG CG C 26.7 0.20 1 219 . 29 ARG CD C 43.2 0.20 1 220 . 29 ARG C C 175.9 0.20 1 221 . 29 ARG HA H 4.27 0.01 1 222 . 29 ARG HB2 H 1.77 0.01 2 223 . 29 ARG HG2 H 1.54 0.01 2 224 . 29 ARG HD2 H 3.08 0.01 2 225 . 30 GLY N N 107.8 0.25 1 226 . 30 GLY H H 8.10 0.01 1 227 . 30 GLY CA C 44.4 0.20 1 228 . 30 GLY C C 173.7 0.20 1 229 . 30 GLY HA2 H 3.75 0.01 2 230 . 31 TYR N N 119.8 0.25 1 231 . 31 TYR H H 8.84 0.01 1 232 . 31 TYR CB C 41.3 0.20 1 233 . 31 TYR CA C 59.0 0.20 1 234 . 31 TYR C C 175.0 0.20 1 235 . 31 TYR HA H 4.50 0.01 1 236 . 31 TYR HB2 H 2.93 0.01 2 237 . 31 TYR HD1 H 7.34 0.01 3 238 . 32 ARG N N 121.4 0.25 1 239 . 32 ARG H H 8.36 0.01 1 240 . 32 ARG CB C 31.9 0.20 1 241 . 32 ARG CA C 54.8 0.20 1 242 . 32 ARG CG C 26.8 0.20 1 243 . 32 ARG CD C 43.6 0.20 1 244 . 32 ARG C C 175.3 0.20 1 245 . 32 ARG HA H 4.34 0.01 1 246 . 32 ARG HB2 H 2.17 0.01 2 247 . 32 ARG HG2 H 1.29 0.01 2 248 . 32 ARG HD2 H 2.94 0.01 2 249 . 33 ALA N N 131.7 0.25 1 250 . 33 ALA H H 10.45 0.01 1 251 . 33 ALA CB C 16.4 0.20 1 252 . 33 ALA CA C 53.1 0.20 1 253 . 33 ALA C C 179.1 0.20 1 254 . 33 ALA HA H 1.53 0.01 1 255 . 33 ALA HB H -0.04 0.01 1 256 . 34 SER N N 109.4 0.25 1 257 . 34 SER H H 8.54 0.01 1 258 . 34 SER CB C 62.6 0.20 1 259 . 34 SER CA C 60.3 0.20 1 260 . 34 SER C C 175.3 0.20 1 261 . 34 SER HA H 3.79 0.01 1 262 . 34 SER HB2 H 3.65 0.01 2 263 . 35 ASP N N 119.2 0.25 1 264 . 35 ASP H H 7.11 0.01 1 265 . 35 ASP CB C 40.6 0.20 1 266 . 35 ASP CA C 55.1 0.20 1 267 . 35 ASP C C 176.2 0.20 1 268 . 35 ASP HA H 4.61 0.01 1 269 . 35 ASP HB2 H 2.92 0.01 2 270 . 36 TRP N N 123.7 0.25 1 271 . 36 TRP H H 7.90 0.01 1 272 . 36 TRP NE1 N 126.4 0.25 1 273 . 36 TRP HE1 H 9.68 0.01 1 274 . 36 TRP CB C 29.0 0.20 1 275 . 36 TRP CA C 53.7 0.20 1 276 . 36 TRP C C 175.9 0.20 1 277 . 36 TRP HA H 4.84 0.01 1 278 . 36 TRP HB2 H 2.96 0.01 2 279 . 36 TRP HB3 H 2.80 0.01 2 280 . 36 TRP HD1 H 6.53 0.01 1 281 . 37 LYS N N 122.5 0.25 1 282 . 37 LYS H H 8.92 0.01 1 283 . 37 LYS CB C 28.8 0.20 1 284 . 37 LYS CA C 54.4 0.20 1 285 . 37 LYS CG C 24.4 0.20 1 286 . 37 LYS CE C 42.1 0.20 1 287 . 37 LYS C C 177.4 0.20 1 288 . 37 LYS HA H 4.57 0.01 1 289 . 37 LYS HB2 H 1.94 0.01 2 290 . 37 LYS HG2 H 1.54 0.01 2 291 . 37 LYS HD2 H 1.72 0.01 2 292 . 37 LYS HE2 H 3.02 0.01 2 293 . 38 LEU N N 120.1 0.25 1 294 . 38 LEU H H 7.49 0.01 1 295 . 38 LEU CB C 41.4 0.20 1 296 . 38 LEU CA C 57.4 0.20 1 297 . 38 LEU CG C 25.9 0.20 1 298 . 38 LEU CD1 C 24.5 0.20 2 299 . 38 LEU CD2 C 22.3 0.20 2 300 . 38 LEU C C 178.6 0.20 1 301 . 38 LEU HA H 3.95 0.01 1 302 . 38 LEU HB2 H 1.58 0.01 2 303 . 38 LEU HG H 1.30 0.01 1 304 . 38 LEU HD1 H 0.35 0.01 2 305 . 38 LEU HD2 H -0.01 0.01 2 306 . 39 ASP N N 114.8 0.25 1 307 . 39 ASP H H 8.79 0.01 1 308 . 39 ASP CB C 40.0 0.20 1 309 . 39 ASP CA C 53.8 0.20 1 310 . 39 ASP C C 175.5 0.20 1 311 . 39 ASP HA H 4.57 0.01 1 312 . 39 ASP HB2 H 2.75 0.01 2 313 . 40 GLN N N 119.0 0.25 1 314 . 40 GLN H H 7.99 0.01 1 315 . 40 GLN CB C 29.8 0.20 1 316 . 40 GLN CA C 52.9 0.20 1 317 . 40 GLN C C 171.8 0.20 1 318 . 40 GLN HA H 4.82 0.01 1 319 . 40 GLN HB2 H 1.85 0.01 2 320 . 40 GLN HG2 H 2.13 0.01 2 321 . 41 PRO CB C 31.5 0.20 1 322 . 41 PRO CA C 63.5 0.20 1 323 . 41 PRO CG C 26.8 0.20 1 324 . 41 PRO CD C 50.1 0.20 1 325 . 41 PRO C C 176.7 0.20 1 326 . 41 PRO HB2 H 1.85 0.01 2 327 . 41 PRO HG2 H 1.61 0.01 2 328 . 41 PRO HD2 H 3.50 0.01 2 329 . 42 ASP N N 122.7 0.25 1 330 . 42 ASP H H 8.59 0.01 1 331 . 42 ASP CB C 43.1 0.20 1 332 . 42 ASP CA C 56.8 0.20 1 333 . 42 ASP C C 175.6 0.20 1 334 . 42 ASP HA H 4.45 0.01 1 335 . 42 ASP HB2 H 2.64 0.01 2 336 . 42 ASP HB3 H 2.21 0.01 2 337 . 43 TRP N N 117.8 0.25 1 338 . 43 TRP H H 7.65 0.01 1 339 . 43 TRP NE1 N 129.6 0.25 1 340 . 43 TRP HE1 H 10.11 0.01 1 341 . 43 TRP CB C 30.7 0.20 1 342 . 43 TRP CA C 58.1 0.20 1 343 . 43 TRP C C 173.2 0.20 1 344 . 43 TRP HA H 4.29 0.01 1 345 . 43 TRP HB2 H 3.00 0.01 2 346 . 43 TRP HB3 H 2.02 0.01 2 347 . 43 TRP HD1 H 6.82 0.01 1 348 . 44 THR N N 117.1 0.25 1 349 . 44 THR H H 6.62 0.01 1 350 . 44 THR CB C 71.8 0.20 1 351 . 44 THR CA C 60.1 0.20 1 352 . 44 THR CG2 C 21.2 0.20 1 353 . 44 THR C C 171.5 0.20 1 354 . 44 THR HA H 4.66 0.01 1 355 . 44 THR HB H 3.75 0.01 1 356 . 44 THR HG2 H 0.92 0.01 1 357 . 45 GLY N N 109.8 0.25 1 358 . 45 GLY H H 7.55 0.01 1 359 . 45 GLY CA C 46.9 0.20 1 360 . 45 GLY C C 170.0 0.20 1 361 . 45 GLY HA2 H 3.47 0.01 2 362 . 46 ARG N N 121.4 0.25 1 363 . 46 ARG H H 8.94 0.01 1 364 . 46 ARG CB C 33.0 0.20 1 365 . 46 ARG CA C 54.3 0.20 1 366 . 46 ARG CG C 27.0 0.20 1 367 . 46 ARG CD C 44.1 0.20 1 368 . 46 ARG C C 173.5 0.20 1 369 . 46 ARG HA H 4.80 0.01 1 370 . 46 ARG HB2 H 1.92 0.01 2 371 . 46 ARG HG2 H 1.54 0.01 2 372 . 46 ARG HD2 H 3.18 0.01 2 373 . 46 ARG HD3 H 2.99 0.01 2 374 . 47 LEU N N 123.5 0.25 1 375 . 47 LEU H H 8.84 0.01 1 376 . 47 LEU CB C 46.7 0.20 1 377 . 47 LEU CA C 53.4 0.20 1 378 . 47 LEU CG C 27.6 0.20 1 379 . 47 LEU CD1 C 25.9 0.20 2 380 . 47 LEU C C 175.1 0.20 1 381 . 47 LEU HA H 5.62 0.01 1 382 . 47 LEU HB2 H 1.66 0.01 2 383 . 47 LEU HD1 H 0.85 0.01 2 384 . 48 ARG N N 124.3 0.25 1 385 . 48 ARG H H 9.46 0.01 1 386 . 48 ARG CB C 35.0 0.20 1 387 . 48 ARG CA C 55.0 0.20 1 388 . 48 ARG CG C 28.4 0.20 1 389 . 48 ARG CD C 44.1 0.20 1 390 . 48 ARG C C 174.8 0.20 1 391 . 48 ARG HA H 5.43 0.01 1 392 . 48 ARG HB2 H 1.90 0.01 2 393 . 48 ARG HG2 H 1.60 0.01 2 394 . 48 ARG HD2 H 3.14 0.01 2 395 . 49 ILE N N 121.4 0.25 1 396 . 49 ILE H H 8.89 0.01 1 397 . 49 ILE CB C 39.1 0.20 1 398 . 49 ILE CA C 59.5 0.20 1 399 . 49 ILE CG2 C 17.5 0.20 2 400 . 49 ILE CD1 C 13.4 0.20 1 401 . 49 ILE C C 176.2 0.20 1 402 . 49 ILE HA H 5.52 0.01 1 403 . 49 ILE HD1 H 0.62 0.01 1 404 . 50 THR N N 119.6 0.25 1 405 . 50 THR H H 9.28 0.01 1 406 . 50 THR CB C 70.8 0.20 1 407 . 50 THR CA C 59.1 0.20 1 408 . 50 THR CG2 C 22.1 0.20 1 409 . 50 THR C C 173.3 0.20 1 410 . 50 THR HA H 5.37 0.01 1 411 . 50 THR HB H 4.29 0.01 1 412 . 50 THR HG2 H 0.89 0.01 1 413 . 51 SER N N 111.5 0.25 1 414 . 51 SER H H 8.93 0.01 1 415 . 51 SER CB C 66.1 0.20 1 416 . 51 SER CA C 56.9 0.20 1 417 . 51 SER C C 173.8 0.20 1 418 . 51 SER HA H 5.16 0.01 1 419 . 51 SER HB2 H 3.60 0.01 2 420 . 51 SER HB3 H 3.28 0.01 2 421 . 52 LYS N N 123.0 0.25 1 422 . 52 LYS H H 8.54 0.01 1 423 . 52 LYS CB C 34.5 0.20 1 424 . 52 LYS CA C 56.3 0.20 1 425 . 52 LYS CG C 25.1 0.20 1 426 . 52 LYS CD C 29.5 0.20 1 427 . 52 LYS CE C 41.9 0.20 1 428 . 52 LYS C C 176.4 0.20 1 429 . 52 LYS HA H 4.62 0.01 1 430 . 52 LYS HB2 H 1.92 0.01 2 431 . 52 LYS HG2 H 1.32 0.01 2 432 . 52 LYS HD2 H 1.56 0.01 2 433 . 52 LYS HE2 H 2.79 0.01 2 434 . 53 GLY N N 116.8 0.25 1 435 . 53 GLY H H 9.11 0.01 1 436 . 53 GLY CA C 46.8 0.20 1 437 . 53 GLY C C 174.9 0.20 1 438 . 53 GLY HA2 H 4.05 0.01 2 439 . 53 GLY HA3 H 3.73 0.01 2 440 . 54 LYS N N 123.3 0.25 1 441 . 54 LYS H H 8.94 0.01 1 442 . 54 LYS CB C 32.3 0.20 1 443 . 54 LYS CA C 57.3 0.20 1 444 . 54 LYS CG C 25.2 0.20 1 445 . 54 LYS CD C 29.2 0.20 1 446 . 54 LYS CE C 42.0 0.20 1 447 . 54 LYS C C 176.4 0.20 1 448 . 54 LYS HA H 4.18 0.01 1 449 . 54 LYS HB2 H 1.77 0.01 2 450 . 54 LYS HG2 H 1.35 0.01 2 451 . 54 LYS HD2 H 1.60 0.01 2 452 . 54 LYS HE2 H 2.90 0.01 2 453 . 55 ILE N N 121.1 0.25 1 454 . 55 ILE H H 7.70 0.01 1 455 . 55 ILE CB C 39.0 0.20 1 456 . 55 ILE CA C 61.0 0.20 1 457 . 55 ILE CG2 C 16.6 0.20 2 458 . 55 ILE CD1 C 12.2 0.20 1 459 . 55 ILE C C 173.9 0.20 1 460 . 55 ILE HA H 4.29 0.01 1 461 . 55 ILE HB H 1.83 0.01 1 462 . 55 ILE HG12 H 1.54 0.01 2 463 . 55 ILE HG2 H 0.82 0.01 1 464 . 55 ILE HD1 H 0.36 0.01 1 465 . 56 ALA N N 125.8 0.25 1 466 . 56 ALA H H 7.77 0.01 1 467 . 56 ALA CB C 19.9 0.20 1 468 . 56 ALA CA C 49.1 0.20 1 469 . 56 ALA C C 174.6 0.20 1 470 . 56 ALA HA H 4.96 0.01 1 471 . 56 ALA HB H 0.66 0.01 1 472 . 57 TYR N N 117.3 0.25 1 473 . 57 TYR H H 9.20 0.01 1 474 . 57 TYR CB C 40.4 0.20 1 475 . 57 TYR CA C 56.9 0.20 1 476 . 57 TYR C C 174.8 0.20 1 477 . 57 TYR HA H 4.84 0.01 1 478 . 57 TYR HB2 H 3.03 0.01 2 479 . 57 TYR HB3 H 2.26 0.01 2 480 . 57 TYR HD1 H 6.63 0.01 3 481 . 58 ILE N N 121.8 0.25 1 482 . 58 ILE H H 8.57 0.01 1 483 . 58 ILE CB C 38.4 0.20 1 484 . 58 ILE CA C 61.0 0.20 1 485 . 58 ILE CG2 C 17.5 0.20 2 486 . 58 ILE CD1 C 14.9 0.20 1 487 . 58 ILE C C 174.7 0.20 1 488 . 58 ILE HA H 4.38 0.01 1 489 . 58 ILE HB H 1.99 0.01 1 490 . 58 ILE HD1 H 0.88 0.01 1 491 . 59 LYS N N 126.8 0.25 1 492 . 59 LYS H H 9.60 0.01 1 493 . 59 LYS CB C 34.3 0.20 1 494 . 59 LYS CA C 56.1 0.20 1 495 . 59 LYS CG C 25.8 0.20 1 496 . 59 LYS CD C 29.9 0.20 1 497 . 59 LYS CE C 42.2 0.20 1 498 . 59 LYS C C 174.1 0.20 1 499 . 59 LYS HA H 4.68 0.01 1 500 . 59 LYS HB2 H 1.89 0.01 2 501 . 59 LYS HG2 H 1.38 0.01 2 502 . 60 LEU N N 124.0 0.25 1 503 . 60 LEU H H 8.53 0.01 1 504 . 60 LEU CB C 41.0 0.20 1 505 . 60 LEU CA C 53.1 0.20 1 506 . 60 LEU CG C 26.1 0.20 1 507 . 60 LEU CD1 C 24.3 0.20 2 508 . 60 LEU C C 175.8 0.20 1 509 . 60 LEU HA H 5.36 0.01 1 510 . 60 LEU HB2 H 1.70 0.01 2 511 . 60 LEU HG H 1.46 0.01 1 512 . 60 LEU HD1 H 0.70 0.01 2 513 . 61 GLU N N 123.7 0.25 1 514 . 61 GLU H H 9.29 0.01 1 515 . 61 GLU CB C 29.4 0.20 1 516 . 61 GLU CA C 53.8 0.20 1 517 . 61 GLU CG C 36.2 0.20 1 518 . 61 GLU C C 174.6 0.20 1 519 . 61 GLU HA H 5.14 0.01 1 520 . 61 GLU HB2 H 2.01 0.01 2 521 . 62 ASP N N 122.4 0.25 1 522 . 62 ASP H H 8.91 0.01 1 523 . 62 ASP CB C 43.8 0.20 1 524 . 62 ASP CA C 55.2 0.20 1 525 . 62 ASP C C 178.2 0.20 1 526 . 62 ASP HA H 4.77 0.01 1 527 . 62 ASP HB2 H 3.00 0.01 2 528 . 62 ASP HB3 H 2.84 0.01 2 529 . 63 LYS N N 124.3 0.25 1 530 . 63 LYS H H 8.95 0.01 1 531 . 63 LYS CB C 33.0 0.20 1 532 . 63 LYS CA C 59.1 0.20 1 533 . 63 LYS CG C 25.2 0.20 1 534 . 63 LYS CD C 29.6 0.20 1 535 . 63 LYS CE C 41.7 0.20 1 536 . 63 LYS C C 176.4 0.20 1 537 . 63 LYS HA H 3.84 0.01 1 538 . 63 LYS HG2 H 1.55 0.01 2 539 . 63 LYS HD2 H 1.72 0.01 2 540 . 63 LYS HE2 H 2.84 0.01 2 541 . 64 VAL N N 118.9 0.25 1 542 . 64 VAL H H 8.53 0.01 1 543 . 64 VAL CB C 32.3 0.20 1 544 . 64 VAL CA C 64.6 0.20 1 545 . 64 VAL CG1 C 21.8 0.20 1 546 . 64 VAL CG2 C 20.7 0.20 1 547 . 64 VAL C C 177.8 0.20 1 548 . 64 VAL HA H 3.95 0.01 1 549 . 64 VAL HB H 2.11 0.01 1 550 . 64 VAL HG1 H 0.90 0.01 2 551 . 65 SER N N 114.3 0.25 1 552 . 65 SER H H 9.06 0.01 1 553 . 65 SER CB C 65.4 0.20 1 554 . 65 SER CA C 58.6 0.20 1 555 . 65 SER C C 176.6 0.20 1 556 . 65 SER HA H 4.43 0.01 1 557 . 65 SER HB2 H 4.07 0.01 2 558 . 65 SER HB3 H 3.86 0.01 2 559 . 66 GLY N N 110.9 0.25 1 560 . 66 GLY H H 7.87 0.01 1 561 . 66 GLY CA C 45.8 0.20 1 562 . 66 GLY C C 173.2 0.20 1 563 . 66 GLY HA2 H 4.11 0.01 2 564 . 66 GLY HA3 H 3.75 0.01 2 565 . 67 GLU N N 119.6 0.25 1 566 . 67 GLU H H 7.84 0.01 1 567 . 67 GLU CB C 30.4 0.20 1 568 . 67 GLU CA C 56.8 0.20 1 569 . 67 GLU CG C 36.3 0.20 1 570 . 67 GLU C C 176.9 0.20 1 571 . 67 GLU HA H 4.02 0.01 1 572 . 67 GLU HB2 H 1.92 0.01 2 573 . 67 GLU HG2 H 2.18 0.01 2 574 . 68 LEU N N 126.7 0.25 1 575 . 68 LEU H H 8.68 0.01 1 576 . 68 LEU CB C 42.5 0.20 1 577 . 68 LEU CA C 56.4 0.20 1 578 . 68 LEU CG C 26.1 0.20 1 579 . 68 LEU CD1 C 24.0 0.20 2 580 . 68 LEU C C 175.9 0.20 1 581 . 68 LEU HA H 4.14 0.01 1 582 . 68 LEU HB2 H 1.57 0.01 2 583 . 68 LEU HD1 H 0.90 0.01 2 584 . 68 LEU HD2 H 0.72 0.01 2 585 . 69 PHE N N 131.2 0.25 1 586 . 69 PHE H H 9.59 0.01 1 587 . 69 PHE CB C 39.7 0.20 1 588 . 69 PHE CA C 58.9 0.20 1 589 . 69 PHE C C 175.2 0.20 1 590 . 69 PHE HA H 4.30 0.01 1 591 . 69 PHE HB2 H 2.76 0.01 2 592 . 69 PHE HB3 H 1.93 0.01 2 593 . 70 ALA N N 116.2 0.25 1 594 . 70 ALA H H 7.64 0.01 1 595 . 70 ALA CB C 22.4 0.20 1 596 . 70 ALA CA C 51.4 0.20 1 597 . 70 ALA C C 174.0 0.20 1 598 . 70 ALA HA H 4.13 0.01 1 599 . 70 ALA HB H 0.89 0.01 1 600 . 71 GLN N N 115.4 0.25 1 601 . 71 GLN H H 8.85 0.01 1 602 . 71 GLN CB C 33.5 0.20 1 603 . 71 GLN CA C 53.6 0.20 1 604 . 71 GLN C C 172.9 0.20 1 605 . 71 GLN HA H 5.62 0.01 1 606 . 71 GLN HB2 H 2.06 0.01 2 607 . 71 GLN HG2 H 2.26 0.01 2 608 . 72 ALA N N 124.9 0.25 1 609 . 72 ALA H H 9.21 0.01 1 610 . 72 ALA CB C 22.7 0.20 1 611 . 72 ALA CA C 48.1 0.20 1 612 . 72 ALA C C 174.6 0.20 1 613 . 72 ALA HA H 5.39 0.01 1 614 . 72 ALA HB H 1.23 0.01 1 615 . 73 PRO CB C 31.8 0.20 1 616 . 73 PRO CA C 61.8 0.20 1 617 . 73 PRO CG C 27.5 0.20 1 618 . 73 PRO CD C 51.1 0.20 1 619 . 73 PRO C C 177.0 0.20 1 620 . 73 PRO HA H 3.96 0.01 1 621 . 73 PRO HB2 H 2.22 0.01 2 622 . 73 PRO HG2 H 2.00 0.01 2 623 . 74 VAL N N 126.6 0.25 1 624 . 74 VAL H H 9.53 0.01 1 625 . 74 VAL CB C 33.0 0.20 1 626 . 74 VAL CA C 62.2 0.20 1 627 . 74 VAL CG1 C 22.7 0.20 1 628 . 74 VAL CG2 C 20.0 0.20 1 629 . 74 VAL C C 173.9 0.20 1 630 . 74 VAL HA H 3.98 0.01 1 631 . 74 VAL HB H 2.04 0.01 1 632 . 74 VAL HG1 H 0.78 0.01 2 633 . 75 GLU N N 123.9 0.25 1 634 . 75 GLU H H 8.79 0.01 1 635 . 75 GLU CB C 31.0 0.20 1 636 . 75 GLU CA C 56.6 0.20 1 637 . 75 GLU CG C 37.2 0.20 1 638 . 75 GLU C C 175.5 0.20 1 639 . 75 GLU HA H 4.62 0.01 1 640 . 75 GLU HB2 H 1.93 0.01 2 641 . 75 GLU HG2 H 2.20 0.01 2 642 . 76 GLN N N 115.9 0.25 1 643 . 76 GLN H H 7.14 0.01 1 644 . 76 GLN CB C 31.9 0.20 1 645 . 76 GLN CA C 55.0 0.20 1 646 . 76 GLN CG C 33.5 0.20 1 647 . 76 GLN C C 172.4 0.20 1 648 . 76 GLN HA H 3.86 0.01 1 649 . 76 GLN HB2 H 1.92 0.01 2 650 . 76 GLN HG2 H 2.24 0.01 2 651 . 77 TYR N N 123.0 0.25 1 652 . 77 TYR H H 7.46 0.01 1 653 . 77 TYR CB C 42.2 0.20 1 654 . 77 TYR CA C 55.7 0.20 1 655 . 77 TYR C C 172.5 0.20 1 656 . 77 TYR HA H 4.20 0.01 1 657 . 77 TYR HB2 H 3.86 0.01 2 658 . 77 TYR HD1 H 6.79 0.01 3 659 . 78 PRO CB C 33.9 0.20 1 660 . 78 PRO CA C 63.1 0.20 1 661 . 78 PRO CG C 25.2 0.20 1 662 . 78 PRO CD C 49.8 0.20 1 663 . 78 PRO C C 175.6 0.20 1 664 . 78 PRO HA H 3.74 0.01 1 665 . 78 PRO HB2 H 2.20 0.01 2 666 . 78 PRO HB3 H 2.02 0.01 2 667 . 78 PRO HG2 H 1.73 0.01 2 668 . 78 PRO HG3 H 1.46 0.01 2 669 . 78 PRO HD2 H 3.37 0.01 2 670 . 78 PRO HD3 H 3.19 0.01 2 671 . 79 GLY N N 108.8 0.25 1 672 . 79 GLY H H 8.73 0.01 1 673 . 79 GLY CA C 46.0 0.20 1 674 . 79 GLY C C 172.7 0.20 1 675 . 79 GLY HA2 H 4.02 0.01 2 676 . 80 ILE N N 115.6 0.25 1 677 . 80 ILE H H 8.01 0.01 1 678 . 80 ILE CB C 39.1 0.20 1 679 . 80 ILE CA C 62.2 0.20 1 680 . 80 ILE CG1 C 28.0 0.20 2 681 . 80 ILE CG2 C 17.5 0.20 2 682 . 80 ILE CD1 C 13.8 0.20 1 683 . 80 ILE C C 176.0 0.20 1 684 . 80 ILE HA H 4.16 0.01 1 685 . 80 ILE HB H 2.02 0.01 1 686 . 80 ILE HG12 H 1.56 0.01 2 687 . 80 ILE HG13 H 1.37 0.01 2 688 . 80 ILE HD1 H 1.00 0.01 1 689 . 81 ALA N N 120.8 0.25 1 690 . 81 ALA H H 8.61 0.01 1 691 . 81 ALA CB C 21.4 0.20 1 692 . 81 ALA CA C 54.5 0.20 1 693 . 81 ALA C C 176.9 0.20 1 694 . 81 ALA HA H 4.27 0.01 1 695 . 81 ALA HB H 1.75 0.01 1 696 . 82 VAL N N 111.8 0.25 1 697 . 82 VAL H H 7.29 0.01 1 698 . 82 VAL CB C 35.2 0.20 1 699 . 82 VAL CA C 61.3 0.20 1 700 . 82 VAL CG1 C 21.1 0.20 1 701 . 82 VAL C C 173.4 0.20 1 702 . 82 VAL HA H 4.98 0.01 1 703 . 82 VAL HB H 2.22 0.01 1 704 . 82 VAL HG1 H 1.00 0.01 2 705 . 83 GLU N N 126.4 0.25 1 706 . 83 GLU H H 9.51 0.01 1 707 . 83 GLU CB C 33.7 0.20 1 708 . 83 GLU CA C 55.0 0.20 1 709 . 83 GLU CG C 36.7 0.20 1 710 . 83 GLU C C 176.1 0.20 1 711 . 83 GLU HA H 5.18 0.01 1 712 . 83 GLU HB2 H 2.20 0.01 2 713 . 83 GLU HG2 H 2.58 0.01 2 714 . 84 THR N N 114.8 0.25 1 715 . 84 THR H H 8.53 0.01 1 716 . 84 THR CB C 69.9 0.20 1 717 . 84 THR CA C 61.8 0.20 1 718 . 84 THR CG2 C 22.4 0.20 1 719 . 84 THR C C 175.0 0.20 1 720 . 84 THR HA H 4.50 0.01 1 721 . 84 THR HB H 4.68 0.01 1 722 . 84 THR HG2 H 1.50 0.01 1 723 . 85 VAL N N 112.5 0.25 1 724 . 85 VAL H H 7.61 0.01 1 725 . 85 VAL CB C 32.3 0.20 1 726 . 85 VAL CA C 60.7 0.20 1 727 . 85 VAL CG1 C 21.5 0.20 1 728 . 85 VAL C C 176.8 0.20 1 729 . 85 VAL HA H 4.71 0.01 1 730 . 85 VAL HB H 2.18 0.01 1 731 . 85 VAL HG1 H 0.95 0.01 2 732 . 85 VAL HG2 H 0.62 0.01 2 733 . 86 THR N N 108.4 0.25 1 734 . 86 THR H H 8.60 0.01 1 735 . 86 THR CB C 69.8 0.20 1 736 . 86 THR CA C 63.7 0.20 1 737 . 86 THR CG2 C 21.7 0.20 1 738 . 86 THR C C 176.3 0.20 1 739 . 86 THR HA H 4.18 0.01 1 740 . 86 THR HB H 4.33 0.01 1 741 . 86 THR HG2 H 1.29 0.01 1 742 . 87 ASP N N 117.6 0.25 1 743 . 87 ASP H H 9.33 0.01 1 744 . 87 ASP CB C 40.7 0.20 1 745 . 87 ASP CA C 52.9 0.20 1 746 . 87 ASP C C 175.1 0.20 1 747 . 87 ASP HA H 4.61 0.01 1 748 . 87 ASP HB2 H 2.83 0.01 2 749 . 87 ASP HB3 H 2.27 0.01 2 750 . 88 SER N N 112.7 0.25 1 751 . 88 SER H H 7.04 0.01 1 752 . 88 SER CB C 64.3 0.20 1 753 . 88 SER CA C 57.5 0.20 1 754 . 88 SER C C 173.4 0.20 1 755 . 88 SER HA H 4.64 0.01 1 756 . 88 SER HB2 H 3.99 0.01 2 757 . 89 SER CB C 64.4 0.20 1 758 . 89 SER CA C 58.8 0.20 1 759 . 89 SER C C 174.8 0.20 1 760 . 89 SER HA H 4.61 0.01 1 761 . 89 SER HB2 H 3.98 0.01 2 762 . 90 ARG N N 116.9 0.25 1 763 . 90 ARG H H 8.26 0.01 1 764 . 90 ARG CB C 31.1 0.20 1 765 . 90 ARG CA C 56.8 0.20 1 766 . 90 ARG CG C 29.8 0.20 1 767 . 90 ARG CD C 42.8 0.20 1 768 . 90 ARG C C 173.1 0.20 1 769 . 90 ARG HA H 4.29 0.01 1 770 . 90 ARG HB2 H 2.11 0.01 2 771 . 90 ARG HG2 H 1.66 0.01 2 772 . 90 ARG HD2 H 3.02 0.01 2 773 . 91 TYR N N 111.7 0.25 1 774 . 91 TYR H H 6.17 0.01 1 775 . 91 TYR CB C 42.3 0.20 1 776 . 91 TYR CA C 55.8 0.20 1 777 . 91 TYR C C 173.7 0.20 1 778 . 91 TYR HA H 5.80 0.01 1 779 . 91 TYR HB2 H 3.08 0.01 2 780 . 91 TYR HB3 H 2.15 0.01 2 781 . 91 TYR HD1 H 6.93 0.01 3 782 . 92 PHE N N 116.5 0.25 1 783 . 92 PHE H H 9.15 0.01 1 784 . 92 PHE CB C 43.8 0.20 1 785 . 92 PHE CA C 56.1 0.20 1 786 . 92 PHE C C 173.7 0.20 1 787 . 92 PHE HA H 5.30 0.01 1 788 . 92 PHE HB2 H 3.14 0.01 2 789 . 92 PHE HB3 H 2.54 0.01 2 790 . 92 PHE HD1 H 6.98 0.01 3 791 . 93 VAL N N 121.2 0.25 1 792 . 93 VAL H H 9.59 0.01 1 793 . 93 VAL CB C 33.7 0.20 1 794 . 93 VAL CA C 61.9 0.20 1 795 . 93 VAL CG1 C 21.2 0.20 1 796 . 93 VAL C C 176.8 0.20 1 797 . 93 VAL HA H 5.02 0.01 1 798 . 93 VAL HB H 1.60 0.01 1 799 . 93 VAL HG1 H 0.66 0.01 2 800 . 93 VAL HG2 H 0.29 0.01 2 801 . 94 ILE N N 121.6 0.25 1 802 . 94 ILE H H 9.34 0.01 1 803 . 94 ILE CB C 41.2 0.20 1 804 . 94 ILE CA C 57.9 0.20 1 805 . 94 ILE CG2 C 17.4 0.20 2 806 . 94 ILE CD1 C 13.5 0.20 1 807 . 94 ILE C C 173.6 0.20 1 808 . 94 ILE HA H 5.78 0.01 1 809 . 94 ILE HB H 2.21 0.01 1 810 . 94 ILE HG12 H 1.31 0.01 2 811 . 94 ILE HG2 H 1.02 0.01 1 812 . 94 ILE HD1 H 0.72 0.01 1 813 . 95 ARG N N 123.9 0.25 1 814 . 95 ARG H H 8.34 0.01 1 815 . 95 ARG CB C 31.2 0.20 1 816 . 95 ARG CA C 53.6 0.20 1 817 . 95 ARG CG C 26.8 0.20 1 818 . 95 ARG CD C 43.6 0.20 1 819 . 95 ARG C C 176.4 0.20 1 820 . 95 ARG HA H 4.71 0.01 1 821 . 95 ARG HB2 H 2.01 0.01 2 822 . 96 ILE N N 120.9 0.25 1 823 . 96 ILE H H 8.46 0.01 1 824 . 96 ILE CB C 39.2 0.20 1 825 . 96 ILE CA C 60.2 0.20 1 826 . 96 ILE CG2 C 18.4 0.20 2 827 . 96 ILE CD1 C 13.2 0.20 1 828 . 96 ILE C C 175.4 0.20 1 829 . 96 ILE HA H 4.57 0.01 1 830 . 96 ILE HB H 1.76 0.01 1 831 . 96 ILE HG12 H 1.25 0.01 2 832 . 96 ILE HG2 H 0.81 0.01 1 833 . 96 ILE HD1 H 0.59 0.01 1 834 . 97 GLN N N 117.2 0.25 1 835 . 97 GLN H H 8.20 0.01 1 836 . 97 GLN CB C 33.0 0.20 1 837 . 97 GLN CA C 54.7 0.20 1 838 . 97 GLN CG C 34.3 0.20 1 839 . 97 GLN C C 176.4 0.20 1 840 . 97 GLN HA H 5.14 0.01 1 841 . 97 GLN HB2 H 1.99 0.01 2 842 . 97 GLN HB3 H 1.75 0.01 2 843 . 97 GLN HG2 H 2.24 0.01 2 844 . 98 ASP N N 124.9 0.25 1 845 . 98 ASP H H 8.34 0.01 1 846 . 98 ASP CB C 41.2 0.20 1 847 . 98 ASP CA C 52.5 0.20 1 848 . 98 ASP C C 177.7 0.20 1 849 . 98 ASP HA H 4.73 0.01 1 850 . 98 ASP HB2 H 3.10 0.01 2 851 . 98 ASP HB3 H 2.53 0.01 2 852 . 99 GLY CA C 46.3 0.20 1 853 . 99 GLY C C 175.1 0.20 1 854 . 99 GLY HA2 H 3.94 0.01 2 855 . 100 THR N N 111.1 0.25 1 856 . 100 THR H H 8.43 0.01 1 857 . 100 THR CB C 70.0 0.20 1 858 . 100 THR CA C 61.6 0.20 1 859 . 100 THR CG2 C 21.3 0.20 1 860 . 100 THR C C 175.2 0.20 1 861 . 100 THR HA H 4.48 0.01 1 862 . 100 THR HB H 4.35 0.01 1 863 . 100 THR HG2 H 1.12 0.01 1 864 . 101 GLY N N 109.6 0.25 1 865 . 101 GLY H H 8.12 0.01 1 866 . 101 GLY CA C 44.8 0.20 1 867 . 101 GLY C C 174.1 0.20 1 868 . 101 GLY HA2 H 4.35 0.01 2 869 . 101 GLY HA3 H 3.52 0.01 2 870 . 102 ARG N N 121.9 0.25 1 871 . 102 ARG H H 7.79 0.01 1 872 . 102 ARG CB C 30.5 0.20 1 873 . 102 ARG CA C 56.3 0.20 1 874 . 102 ARG CG C 27.1 0.20 1 875 . 102 ARG CD C 43.3 0.20 1 876 . 102 ARG C C 176.1 0.20 1 877 . 102 ARG HA H 4.38 0.01 1 878 . 102 ARG HB2 H 1.75 0.01 2 879 . 102 ARG HG2 H 1.54 0.01 2 880 . 102 ARG HD2 H 3.11 0.01 2 881 . 103 SER N N 118.5 0.25 1 882 . 103 SER H H 8.42 0.01 1 883 . 103 SER CB C 66.0 0.20 1 884 . 103 SER CA C 57.4 0.20 1 885 . 103 SER C C 173.0 0.20 1 886 . 103 SER HA H 5.35 0.01 1 887 . 103 SER HB2 H 3.53 0.01 2 888 . 104 ALA N N 123.7 0.25 1 889 . 104 ALA H H 8.40 0.01 1 890 . 104 ALA CB C 21.8 0.20 1 891 . 104 ALA CA C 51.1 0.20 1 892 . 104 ALA C C 174.2 0.20 1 893 . 104 ALA HA H 4.41 0.01 1 894 . 104 ALA HB H 1.18 0.01 1 895 . 105 PHE N N 117.8 0.25 1 896 . 105 PHE H H 8.44 0.01 1 897 . 105 PHE CB C 40.4 0.20 1 898 . 105 PHE CA C 57.1 0.20 1 899 . 105 PHE C C 175.7 0.20 1 900 . 105 PHE HA H 5.50 0.01 1 901 . 105 PHE HB2 H 2.77 0.01 2 902 . 105 PHE HB3 H 2.67 0.01 2 903 . 105 PHE HD1 H 7.21 0.01 3 904 . 106 ILE N N 116.1 0.25 1 905 . 106 ILE H H 8.85 0.01 1 906 . 106 ILE CB C 42.0 0.20 1 907 . 106 ILE CA C 59.4 0.20 1 908 . 106 ILE CG2 C 17.5 0.20 2 909 . 106 ILE CD1 C 14.2 0.20 1 910 . 106 ILE C C 173.3 0.20 1 911 . 106 ILE HA H 4.59 0.01 1 912 . 106 ILE HB H 1.77 0.01 1 913 . 106 ILE HD1 H 0.70 0.01 1 914 . 107 GLY N N 109.7 0.25 1 915 . 107 GLY H H 8.65 0.01 1 916 . 107 GLY CA C 44.7 0.20 1 917 . 107 GLY C C 173.5 0.20 1 918 . 107 GLY HA2 H 5.12 0.01 2 919 . 107 GLY HA3 H 2.66 0.01 2 920 . 108 ILE N N 116.1 0.25 1 921 . 108 ILE H H 9.69 0.01 1 922 . 108 ILE CB C 42.2 0.20 1 923 . 108 ILE CA C 58.6 0.20 1 924 . 108 ILE CG1 C 26.5 0.20 2 925 . 108 ILE CG2 C 17.5 0.20 2 926 . 108 ILE CD1 C 13.4 0.20 1 927 . 108 ILE C C 175.7 0.20 1 928 . 108 ILE HA H 6.03 0.01 1 929 . 108 ILE HB H 1.75 0.01 1 930 . 108 ILE HG12 H 1.48 0.01 2 931 . 108 ILE HG2 H 0.79 0.01 1 932 . 108 ILE HD1 H 0.31 0.01 1 933 . 109 GLY N N 105.9 0.25 1 934 . 109 GLY H H 8.81 0.01 1 935 . 109 GLY CA C 46.5 0.20 1 936 . 109 GLY C C 171.3 0.20 1 937 . 109 GLY HA2 H 4.96 0.01 2 938 . 109 GLY HA3 H 3.73 0.01 2 939 . 110 PHE N N 118.7 0.25 1 940 . 110 PHE H H 7.81 0.01 1 941 . 110 PHE CB C 41.8 0.20 1 942 . 110 PHE CA C 56.1 0.20 1 943 . 110 PHE C C 176.0 0.20 1 944 . 110 PHE HA H 4.96 0.01 1 945 . 110 PHE HB2 H 3.51 0.01 2 946 . 110 PHE HB3 H 2.58 0.01 2 947 . 110 PHE HD1 H 7.40 0.01 3 948 . 111 THR N N 117.1 0.25 1 949 . 111 THR H H 8.94 0.01 1 950 . 111 THR CB C 69.0 0.20 1 951 . 111 THR CA C 65.3 0.20 1 952 . 111 THR CG2 C 22.1 0.20 1 953 . 111 THR C C 174.1 0.20 1 954 . 111 THR HA H 3.90 0.01 1 955 . 111 THR HB H 4.20 0.01 1 956 . 111 THR HG2 H 1.28 0.01 1 957 . 112 ASP N N 119.7 0.25 1 958 . 112 ASP H H 8.53 0.01 1 959 . 112 ASP CB C 43.7 0.20 1 960 . 112 ASP CA C 52.8 0.20 1 961 . 112 ASP C C 176.7 0.20 1 962 . 112 ASP HA H 4.91 0.01 1 963 . 112 ASP HB2 H 2.86 0.01 2 964 . 112 ASP HB3 H 2.62 0.01 2 965 . 113 ARG N N 124.8 0.25 1 966 . 113 ARG H H 9.05 0.01 1 967 . 113 ARG CB C 30.2 0.20 1 968 . 113 ARG CA C 59.9 0.20 1 969 . 113 ARG CG C 27.2 0.20 1 970 . 113 ARG CD C 43.4 0.20 1 971 . 113 ARG C C 178.3 0.20 1 972 . 113 ARG HA H 3.16 0.01 1 973 . 113 ARG HB2 H 1.77 0.01 2 974 . 113 ARG HG2 H 1.63 0.01 2 975 . 113 ARG HD2 H 3.19 0.01 2 976 . 114 GLY N N 109.0 0.25 1 977 . 114 GLY H H 8.91 0.01 1 978 . 114 GLY CA C 46.9 0.20 1 979 . 114 GLY C C 176.0 0.20 1 980 . 114 GLY HA2 H 3.88 0.01 2 981 . 115 ASP N N 120.7 0.25 1 982 . 115 ASP H H 7.52 0.01 1 983 . 115 ASP CB C 40.6 0.20 1 984 . 115 ASP CA C 57.5 0.20 1 985 . 115 ASP C C 176.8 0.20 1 986 . 115 ASP HA H 4.18 0.01 1 987 . 115 ASP HB2 H 2.91 0.01 2 988 . 115 ASP HB3 H 2.31 0.01 2 989 . 116 ALA N N 120.6 0.25 1 990 . 116 ALA H H 6.79 0.01 1 991 . 116 ALA CB C 19.6 0.20 1 992 . 116 ALA CA C 54.5 0.20 1 993 . 116 ALA C C 178.5 0.20 1 994 . 116 ALA HA H 3.33 0.01 1 995 . 116 ALA HB H 1.71 0.01 1 996 . 117 PHE N N 119.2 0.25 1 997 . 117 PHE H H 8.16 0.01 1 998 . 117 PHE CB C 38.5 0.20 1 999 . 117 PHE CA C 61.3 0.20 1 1000 . 117 PHE C C 177.2 0.20 1 1001 . 117 PHE HA H 4.34 0.01 1 1002 . 117 PHE HB2 H 3.34 0.01 2 1003 . 117 PHE HB3 H 3.23 0.01 2 1004 . 117 PHE HD1 H 7.36 0.01 3 1005 . 118 ASP N N 119.0 0.25 1 1006 . 118 ASP H H 8.08 0.01 1 1007 . 118 ASP CB C 40.9 0.20 1 1008 . 118 ASP CA C 57.0 0.20 1 1009 . 118 ASP C C 178.8 0.20 1 1010 . 118 ASP HA H 4.30 0.01 1 1011 . 118 ASP HB2 H 2.69 0.01 2 1012 . 119 PHE N N 122.0 0.25 1 1013 . 119 PHE H H 7.73 0.01 1 1014 . 119 PHE CB C 39.0 0.20 1 1015 . 119 PHE CA C 61.0 0.20 1 1016 . 119 PHE C C 174.5 0.20 1 1017 . 119 PHE HA H 3.93 0.01 1 1018 . 119 PHE HB2 H 3.05 0.01 2 1019 . 119 PHE HB3 H 2.58 0.01 2 1020 . 119 PHE HD1 H 6.65 0.01 3 1021 . 120 ASN N N 116.6 0.25 1 1022 . 120 ASN H H 7.66 0.01 1 1023 . 120 ASN CB C 39.4 0.20 1 1024 . 120 ASN CA C 56.5 0.20 1 1025 . 120 ASN C C 177.2 0.20 1 1026 . 120 ASN HA H 3.88 0.01 1 1027 . 120 ASN HB2 H 2.90 0.01 2 1028 . 121 VAL N N 118.2 0.25 1 1029 . 121 VAL H H 8.60 0.01 1 1030 . 121 VAL CB C 31.2 0.20 1 1031 . 121 VAL CA C 66.1 0.20 1 1032 . 121 VAL CG1 C 22.9 0.20 1 1033 . 121 VAL CG2 C 21.2 0.20 1 1034 . 121 VAL C C 177.5 0.20 1 1035 . 121 VAL HA H 3.47 0.01 1 1036 . 121 VAL HB H 1.80 0.01 1 1037 . 121 VAL HG1 H 0.78 0.01 2 1038 . 121 VAL HG2 H 0.66 0.01 2 1039 . 122 SER N N 115.5 0.25 1 1040 . 122 SER H H 7.89 0.01 1 1041 . 122 SER CB C 62.8 0.20 1 1042 . 122 SER CA C 62.5 0.20 1 1043 . 122 SER C C 176.8 0.20 1 1044 . 122 SER HA H 4.09 0.01 1 1045 . 122 SER HB2 H 3.74 0.01 2 1046 . 123 LEU N N 120.4 0.25 1 1047 . 123 LEU H H 6.76 0.01 1 1048 . 123 LEU CB C 41.5 0.20 1 1049 . 123 LEU CA C 57.5 0.20 1 1050 . 123 LEU CD1 C 25.4 0.20 2 1051 . 123 LEU CD2 C 23.1 0.20 2 1052 . 123 LEU C C 178.1 0.20 1 1053 . 123 LEU HA H 3.70 0.01 1 1054 . 123 LEU HD1 H 0.32 0.01 2 1055 . 123 LEU HD2 H -0.04 0.01 2 1056 . 124 GLN N N 117.9 0.25 1 1057 . 124 GLN H H 8.21 0.01 1 1058 . 124 GLN CB C 28.8 0.20 1 1059 . 124 GLN CA C 59.6 0.20 1 1060 . 124 GLN CG C 34.3 0.20 1 1061 . 124 GLN C C 179.5 0.20 1 1062 . 124 GLN HA H 3.91 0.01 1 1063 . 124 GLN HB2 H 2.27 0.01 2 1064 . 124 GLN HG2 H 2.57 0.01 2 1065 . 125 ASP N N 118.8 0.25 1 1066 . 125 ASP H H 8.98 0.01 1 1067 . 125 ASP CB C 39.8 0.20 1 1068 . 125 ASP CA C 57.2 0.20 1 1069 . 125 ASP C C 178.8 0.20 1 1070 . 125 ASP HA H 4.36 0.01 1 1071 . 125 ASP HB2 H 2.79 0.01 2 1072 . 125 ASP HB3 H 2.54 0.01 2 1073 . 126 HIS N N 119.1 0.25 1 1074 . 126 HIS H H 7.40 0.01 1 1075 . 126 HIS CB C 29.8 0.20 1 1076 . 126 HIS CA C 60.0 0.20 1 1077 . 126 HIS C C 176.8 0.20 1 1078 . 126 HIS HA H 4.20 0.01 1 1079 . 126 HIS HB2 H 2.84 0.01 2 1080 . 126 HIS HB3 H 2.70 0.01 2 1081 . 127 PHE N N 112.9 0.25 1 1082 . 127 PHE H H 7.51 0.01 1 1083 . 127 PHE CB C 38.5 0.20 1 1084 . 127 PHE CA C 61.2 0.20 1 1085 . 127 PHE C C 176.4 0.20 1 1086 . 127 PHE HA H 4.04 0.01 1 1087 . 127 PHE HB2 H 3.49 0.01 2 1088 . 127 PHE HB3 H 2.80 0.01 2 1089 . 128 LYS N N 120.6 0.25 1 1090 . 128 LYS H H 7.69 0.01 1 1091 . 128 LYS CB C 31.9 0.20 1 1092 . 128 LYS CA C 58.5 0.20 1 1093 . 128 LYS CG C 24.4 0.20 1 1094 . 128 LYS CD C 29.2 0.20 1 1095 . 128 LYS CE C 42.0 0.20 1 1096 . 128 LYS C C 177.0 0.20 1 1097 . 128 LYS HA H 4.09 0.01 1 1098 . 128 LYS HB2 H 1.80 0.01 2 1099 . 128 LYS HG2 H 1.21 0.01 2 1100 . 128 LYS HD2 H 1.57 0.01 2 1101 . 128 LYS HE2 H 2.80 0.01 2 1102 . 129 TRP N N 118.5 0.25 1 1103 . 129 TRP H H 7.56 0.01 1 1104 . 129 TRP NE1 N 129.0 0.25 1 1105 . 129 TRP HE1 H 10.00 0.01 1 1106 . 129 TRP CB C 28.9 0.20 1 1107 . 129 TRP CA C 57.6 0.20 1 1108 . 129 TRP C C 176.9 0.20 1 1109 . 129 TRP HA H 4.55 0.01 1 1110 . 129 TRP HB2 H 3.34 0.01 2 1111 . 129 TRP HB3 H 3.20 0.01 2 1112 . 129 TRP HD1 H 7.23 0.01 1 1113 . 130 VAL N N 120.2 0.25 1 1114 . 130 VAL H H 7.51 0.01 1 1115 . 130 VAL CB C 32.2 0.20 1 1116 . 130 VAL CA C 63.1 0.20 1 1117 . 130 VAL CG1 C 21.0 0.20 1 1118 . 130 VAL CG2 C 20.1 0.20 1 1119 . 130 VAL C C 175.8 0.20 1 1120 . 130 VAL HA H 3.66 0.01 1 1121 . 130 VAL HB H 1.97 0.01 1 1122 . 130 VAL HG1 H 0.82 0.01 2 1123 . 130 VAL HG2 H 0.64 0.01 2 1124 . 131 LYS N N 123.0 0.25 1 1125 . 131 LYS H H 7.91 0.01 1 1126 . 131 LYS CB C 32.7 0.20 1 1127 . 131 LYS CA C 56.2 0.20 1 1128 . 131 LYS CG C 24.7 0.20 1 1129 . 131 LYS CD C 29.1 0.20 1 1130 . 131 LYS CE C 42.1 0.20 1 1131 . 131 LYS C C 176.1 0.20 1 1132 . 131 LYS HA H 4.20 0.01 1 1133 . 131 LYS HB2 H 1.94 0.01 2 1134 . 131 LYS HG2 H 1.44 0.01 2 1135 . 131 LYS HD2 H 1.73 0.01 2 1136 . 131 LYS HE2 H 3.00 0.01 2 1137 . 132 GLN N N 122.0 0.25 1 1138 . 132 GLN H H 8.18 0.01 1 1139 . 132 GLN CB C 29.0 0.20 1 1140 . 132 GLN CA C 55.8 0.20 1 1141 . 132 GLN CG C 33.7 0.20 1 1142 . 132 GLN C C 174.8 0.20 1 1143 . 132 GLN HA H 4.29 0.01 1 1144 . 132 GLN HB2 H 2.05 0.01 2 1145 . 132 GLN HG2 H 2.31 0.01 2 1146 . 133 GLU N N 127.1 0.25 1 1147 . 133 GLU H H 7.93 0.01 1 1148 . 133 GLU CB C 30.8 0.20 1 1149 . 133 GLU CA C 57.9 0.20 1 1150 . 133 GLU C C 180.9 0.20 1 1151 . 133 GLU HA H 4.08 0.01 1 1152 . 133 GLU HB2 H 2.07 0.01 2 1153 . 133 GLU HG2 H 1.86 0.01 2 stop_ save_ save_D_values_set_1 _Saveframe_category residual_dipolar_couplings loop_ _Sample_label $sample_3 stop_ _Details . _Sample_conditions_label $Ex-cond_1 _Spectrometer_frequency_1H 600 _Text_data_format . _Text_data . loop_ _Residual_dipolar_coupling_ID _Atom_one_residue_seq_code _Atom_one_residue_label _Atom_one_atom_name _Atom_two_residue_seq_code _Atom_two_residue_label _Atom_two_atom_name _Residual_dipolar_coupling_value _Atom_one_mol_system_component_name _Atom_two_mol_system_component_name _Residual_dipolar_coupling_min_value _Residual_dipolar_coupling_max_value _Residual_dipolar_coupling_value_error 1DNH 2 ALA N 2 ALA H 0.9 ? ? . . . 1DNH 3 ALA N 3 ALA H 3.2 ? ? . . . 1DNH 4 GLU N 4 GLU H 1.6 ? ? . . . 1DNH 5 LEU N 5 LEU H -0.9 ? ? . . . 1DNH 6 GLU N 6 GLU H -1.8 ? ? . . . 1DNH 7 TYR N 7 TYR H 6.4 ? ? . . . 1DNH 8 GLU N 8 GLU H -2.1 ? ? . . . 1DNH 9 SER N 9 SER H -13.6 ? ? . . . 1DNH 10 VAL N 10 VAL H -25.2 ? ? . . . 1DNH 11 LEU N 11 LEU H -13.1 ? ? . . . 1DNH 12 CYS N 12 CYS H -1.5 ? ? . . . 1DNH 13 VAL N 13 VAL H -6.6 ? ? . . . 1DNH 14 LYS N 14 LYS H -6.1 ? ? . . . 1DNH 16 ASP N 16 ASP H 13.6 ? ? . . . 1DNH 17 VAL N 17 VAL H 8.8 ? ? . . . 1DNH 18 SER N 18 SER H 13.1 ? ? . . . 1DNH 19 VAL N 19 VAL H 18.8 ? ? . . . 1DNH 20 TYR N 20 TYR H 24.5 ? ? . . . 1DNH 21 ARG N 21 ARG H 22.3 ? ? . . . 1DNH 22 ILE N 22 ILE H 9.7 ? ? . . . 1DNH 25 ARG N 25 ARG H 3.7 ? ? . . . 1DNH 29 ARG N 29 ARG H 3.5 ? ? . . . 1DNH 30 GLY N 30 GLY H 0.5 ? ? . . . 1DNH 31 TYR N 31 TYR H 6.0 ? ? . . . 1DNH 32 ARG N 32 ARG H -0.7 ? ? . . . 1DNH 33 ALA N 33 ALA H 7.5 ? ? . . . 1DNH 34 SER N 34 SER H 19.7 ? ? . . . 1DNH 35 ASP N 35 ASP H 19.0 ? ? . . . 1DNH 36 TRP N 36 TRP H 0.4 ? ? . . . 1DNH 37 LYS N 37 LYS H 5.6 ? ? . . . 1DNH 38 LEU N 38 LEU H -6.1 ? ? . . . 1DNH 39 ASP N 39 ASP H -24.4 ? ? . . . 1DNH 40 GLN N 40 GLN H 4.0 ? ? . . . 1DNH 42 ASP N 42 ASP H 19.8 ? ? . . . 1DNH 43 TRP N 43 TRP H 10.4 ? ? . . . 1DNH 44 THR N 44 THR H 11.3 ? ? . . . 1DNH 45 GLY N 45 GLY H 5.4 ? ? . . . 1DNH 46 ARG N 46 ARG H 2.4 ? ? . . . 1DNH 47 LEU N 47 LEU H -10.3 ? ? . . . 1DNH 48 ARG N 48 ARG H -18.4 ? ? . . . 1DNH 49 ILE N 49 ILE H -22.2 ? ? . . . 1DNH 50 THR N 50 THR H -27.0 ? ? . . . 1DNH 51 SER N 51 SER H -25.7 ? ? . . . 1DNH 52 LYS N 52 LYS H -22.1 ? ? . . . 1DNH 53 GLY N 53 GLY H -22.7 ? ? . . . 1DNH 54 LYS N 54 LYS H 1.2 ? ? . . . 1DNH 55 ILE N 55 ILE H -8.6 ? ? . . . 1DNH 56 ALA N 56 ALA H -25.8 ? ? . . . 1DNH 57 TYR N 57 TYR H -29.2 ? ? . . . 1DNH 58 ILE N 58 ILE H -23.2 ? ? . . . 1DNH 59 LYS N 59 LYS H -13.9 ? ? . . . 1DNH 60 LEU N 60 LEU H -9.1 ? ? . . . 1DNH 61 GLU N 61 GLU H 0.4 ? ? . . . 1DNH 62 ASP N 62 ASP H 3.0 ? ? . . . 1DNH 63 LYS N 63 LYS H -12.6 ? ? . . . 1DNH 64 VAL N 64 VAL H -23.8 ? ? . . . 1DNH 65 SER N 65 SER H -18.4 ? ? . . . 1DNH 66 GLY N 66 GLY H 4.5 ? ? . . . 1DNH 67 GLU N 67 GLU H 19.5 ? ? . . . 1DNH 68 LEU N 68 LEU H 5.5 ? ? . . . 1DNH 69 PHE N 69 PHE H -1.6 ? ? . . . 1DNH 70 ALA N 70 ALA H -19.1 ? ? . . . 1DNH 71 GLN N 71 GLN H -17.7 ? ? . . . 1DNH 72 ALA N 72 ALA H -21.5 ? ? . . . 1DNH 74 VAL N 74 VAL H -24.7 ? ? . . . 1DNH 75 GLU N 75 GLU H -19.0 ? ? . . . 1DNH 76 GLN N 76 GLN H 17.2 ? ? . . . 1DNH 77 TYR N 77 TYR H 13.9 ? ? . . . 1DNH 79 GLY N 79 GLY H 17.4 ? ? . . . 1DNH 80 ILE N 80 ILE H 14.0 ? ? . . . 1DNH 81 ALA N 81 ALA H 14.5 ? ? . . . 1DNH 82 VAL N 82 VAL H 14.4 ? ? . . . 1DNH 83 GLU N 83 GLU H 18.9 ? ? . . . 1DNH 84 THR N 84 THR H 16.2 ? ? . . . 1DNH 85 VAL N 85 VAL H -22.0 ? ? . . . 1DNH 86 THR N 86 THR H -9.9 ? ? . . . 1DNH 87 ASP N 87 ASP H 7.7 ? ? . . . 1DNH 88 SER N 88 SER H 8.5 ? ? . . . 1DNH 90 ARG N 90 ARG H -2.3 ? ? . . . 1DNH 91 TYR N 91 TYR H 6.5 ? ? . . . 1DNH 92 PHE N 92 PHE H 16.7 ? ? . . . 1DNH 93 VAL N 93 VAL H 17.9 ? ? . . . 1DNH 94 ILE N 94 ILE H 20.6 ? ? . . . 1DNH 95 ARG N 95 ARG H 10.3 ? ? . . . 1DNH 96 ILE N 96 ILE H -9.4 ? ? . . . 1DNH 97 GLN N 97 GLN H -27.6 ? ? . . . 1DNH 98 ASP N 98 ASP H -23.7 ? ? . . . 1DNH 100 THR N 100 THR H 10.5 ? ? . . . 1DNH 101 GLY N 101 GLY H -13.7 ? ? . . . 1DNH 102 ARG N 102 ARG H -1.9 ? ? . . . 1DNH 103 SER N 103 SER H -18.7 ? ? . . . 1DNH 104 ALA N 104 ALA H -20.3 ? ? . . . 1DNH 105 PHE N 105 PHE H -16.3 ? ? . . . 1DNH 106 ILE N 106 ILE H 7.8 ? ? . . . 1DNH 107 GLY N 107 GLY H 19.0 ? ? . . . 1DNH 108 ILE N 108 ILE H 13.3 ? ? . . . 1DNH 109 GLY N 109 GLY H 9.7 ? ? . . . 1DNH 110 PHE N 110 PHE H 0.7 ? ? . . . 1DNH 111 THR N 111 THR H -4.3 ? ? . . . 1DNH 112 ASP N 112 ASP H 3.2 ? ? . . . 1DNH 113 ARG N 113 ARG H 3.5 ? ? . . . 1DNH 114 GLY N 114 GLY H 13.6 ? ? . . . 1DNH 115 ASP N 115 ASP H 14.8 ? ? . . . 1DNH 116 ALA N 116 ALA H 12.8 ? ? . . . 1DNH 117 PHE N 117 PHE H 14.4 ? ? . . . 1DNH 118 ASP N 118 ASP H 19.9 ? ? . . . 1DNH 119 PHE N 119 PHE H 16.1 ? ? . . . 1DNH 120 ASN N 120 ASN H 13.6 ? ? . . . 1DNH 121 VAL N 121 VAL H 17.4 ? ? . . . 1DNH 122 SER N 122 SER H 19.3 ? ? . . . 1DNH 123 LEU N 123 LEU H 13.1 ? ? . . . 1DNH 124 GLN N 124 GLN H 14.9 ? ? . . . 1DNH 125 ASP N 125 ASP H 20.5 ? ? . . . 1DNH 126 HIS N 126 HIS H 15.3 ? ? . . . 1DNH 127 PHE N 127 PHE H 16.7 ? ? . . . 1DNH 128 LYS N 128 LYS H 7.6 ? ? . . . 1DNH 129 TRP N 129 TRP H 15.0 ? ? . . . 1DNH 130 VAL N 130 VAL H 6.8 ? ? . . . 1DNH 131 LYS N 131 LYS H 3.7 ? ? . . . 1DNH 132 GLN N 132 GLN H 2.1 ? ? . . . 1DNH 133 GLU N 133 GLU H 1.3 ? ? . . . stop_ save_