data_5807 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Letter to the Editor: Assignments of 1H and 15N resonances of the bacteriophage lambda capsid stabilizing protein gpD ; _BMRB_accession_number 5807 _BMRB_flat_file_name bmr5807.str _Entry_type original _Submission_date 2003-05-22 _Accession_date 2003-05-22 _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 Iwai Hideo . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 571 "15N chemical shifts" 110 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2004-02-11 original author . stop_ _Original_release_date 2004-02-11 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; Lette to the Editor: Assignments of 1H and 15N resonances of the bacteriophage lambda capsid stabilizing protein gpD ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 14739644 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Iwai Hideo . . 2 Forrer Patrik . . 3 Pluckthun Andreas . . 4 Guntert Peter . . stop_ _Journal_abbreviation 'J. Biomol. NMR' _Journal_volume 28 _Journal_issue 1 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 89 _Page_last 90 _Year 2004 _Details . loop_ _Keyword 'bacteriophage lambda' capsid stop_ save_ ####################################### # Cited references within the entry # ####################################### save_ref_1 _Saveframe_category citation _Citation_full ; Yang F, Forrer P, Dauter Z, Conway JF, Cheng N, Cerritelli ME, Steven AC, Pluckthun A, Wlodawer A. Nat. Struct. Biol. 7, 230-237(2000). ; _Citation_title 'Novel fold and capsid-binding properties of the lambda-phage display platform protein gpD.' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 10700283 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Yang F . . 2 Forrer P . . 3 Dauter Z . . 4 Conway 'J F' F. . 5 Cheng N . . 6 Cerritelli 'M E' E. . 7 Steven 'A C' C. . 8 Pluckthun A . . 9 Wlodawer A . . stop_ _Journal_abbreviation 'Nat. Struct. Biol.' _Journal_name_full 'Nature structural biology' _Journal_volume 7 _Journal_issue 3 _Journal_CSD . _Book_title . _Book_chapter_title . _Book_volume . _Book_series . _Book_publisher . _Book_publisher_city . _Book_ISBN . _Conference_title . _Conference_site . _Conference_state_province . _Conference_country . _Conference_start_date . _Conference_end_date . _Conference_abstract_number . _Thesis_institution . _Thesis_institution_city . _Thesis_institution_country . _Page_first 230 _Page_last 237 _Year 2000 _Details ; The crystal structure of gpD, the capsid-stabilizing protein of bacteriophage lambda, was solved at 1.1 A resolution. Data were obtained from twinned crystals in space group P21 and refined with anisotropic temperature factors to an R-factor of 0.098 (Rfree = 0. 132). GpD (109 residues) has a novel fold with an unusually low content of regular secondary structure. Noncrystallographic trimers with substantial intersubunit interfaces were observed. The C-termini are well ordered and located on one side of the trimer, relatively far from its three-fold axis. The N-termini are disordered up to Ser 15, which is close to the three-fold axis and on the same side as the C-termini. A density map of the icosahedral viral capsid at 15 A resolution, obtained by cryo-electron microscopy and image reconstruction, reveals gpD trimers, seemingly indistinguishable from the ones seen in the crystals, at all three-fold sites. The map further reveals that the side of the trimer that binds to the capsid is the side on which both termini reside. Despite this orientation of the gpD trimer, fusion proteins connected by linker peptides to either terminus bind to the capsid, allowing protein and peptide display. ; save_ ################################## # Molecular system description # ################################## save_system_gpD _Saveframe_category molecular_system _Mol_system_name gpD _Abbreviation_common gpD _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label gpD $gpD stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state monomer _System_paramagnetic no _System_thiol_state 'not present' _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_gpD _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'bacteriophage lambda gpD' _Abbreviation_common gpD _Molecular_mass . _Mol_thiol_state 'not present' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 109 _Mol_residue_sequence ; TSKETFTHYQPQGNSDPAHT ATAPGGLSAKAPAMTPLMLD TSSRKLVAWDGTTDGAAVGI LAVAADQTSTTLTFYKSGTF RYEDVLWPEAASDETKKRTA FAGTAISIV ; loop_ _Residue_seq_code _Residue_label 1 THR 2 SER 3 LYS 4 GLU 5 THR 6 PHE 7 THR 8 HIS 9 TYR 10 GLN 11 PRO 12 GLN 13 GLY 14 ASN 15 SER 16 ASP 17 PRO 18 ALA 19 HIS 20 THR 21 ALA 22 THR 23 ALA 24 PRO 25 GLY 26 GLY 27 LEU 28 SER 29 ALA 30 LYS 31 ALA 32 PRO 33 ALA 34 MET 35 THR 36 PRO 37 LEU 38 MET 39 LEU 40 ASP 41 THR 42 SER 43 SER 44 ARG 45 LYS 46 LEU 47 VAL 48 ALA 49 TRP 50 ASP 51 GLY 52 THR 53 THR 54 ASP 55 GLY 56 ALA 57 ALA 58 VAL 59 GLY 60 ILE 61 LEU 62 ALA 63 VAL 64 ALA 65 ALA 66 ASP 67 GLN 68 THR 69 SER 70 THR 71 THR 72 LEU 73 THR 74 PHE 75 TYR 76 LYS 77 SER 78 GLY 79 THR 80 PHE 81 ARG 82 TYR 83 GLU 84 ASP 85 VAL 86 LEU 87 TRP 88 PRO 89 GLU 90 ALA 91 ALA 92 SER 93 ASP 94 GLU 95 THR 96 LYS 97 LYS 98 ARG 99 THR 100 ALA 101 PHE 102 ALA 103 GLY 104 THR 105 ALA 106 ILE 107 SER 108 ILE 109 VAL 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 1C5E "Bacteriophage Lambda Head Protein D" 87.16 95 100.00 100.00 7.87e-59 PDB 1TCZ "Crystal Structure Of A Truncated Version Of The Phage Lamda Protein Gpd" 87.16 95 100.00 100.00 7.87e-59 PDB 1VD0 "Capsid Stabilizing Protein Gpd, Nmr, 20 Structures" 100.00 109 100.00 100.00 4.43e-71 DBJ BAB35057 "major capsid protein [Escherichia coli O157:H7 str. Sakai]" 100.00 110 99.08 99.08 6.48e-70 DBJ BAB35598 "putative head decoration protein [Escherichia coli O157:H7 str. Sakai]" 100.00 110 99.08 99.08 6.48e-70 DBJ BAI23942 "putative head-DNA stabilization protein [Escherichia coli O26:H11 str. 11368]" 100.00 112 97.25 99.08 5.54e-69 DBJ BAI25490 "putative head-DNA stabilization protein [Escherichia coli O26:H11 str. 11368]" 100.00 112 99.08 99.08 5.73e-70 DBJ BAI29409 "putative head-DNA stabilization protein [Escherichia coli O103:H2 str. 12009]" 100.00 112 100.00 100.00 3.87e-71 EMBL CAQ31253 "enterobacteria phage lambda, head-DNA stabilization protein [Escherichia coli BL21(DE3)]" 100.00 110 100.00 100.00 4.24e-71 EMBL CAR12629 "Head decoration protein from bacteriophage origin [Escherichia coli UMN026]" 100.00 112 97.25 98.17 6.67e-69 EMBL CAU96661 "Head decoration protein from bacteriophage origin [Escherichia coli 55989]" 100.00 112 98.17 99.08 1.82e-69 EMBL CBG34517 "head decoration protein (major capsid protein) [Escherichia coli 042]" 100.00 110 99.08 99.08 6.48e-70 EMBL CBJ00729 "putative head-DNA stabilization phage protein [Escherichia coli ETEC H10407]" 100.00 110 97.25 98.17 1.75e-68 GB AAA96539 "D (head-DNA stabilization;110) [Enterobacteria phage lambda]" 100.00 110 100.00 100.00 4.24e-71 GB AAG55984 "putative head-DNA stabilization protein of prophage CP-933X, partial [Escherichia coli O157:H7 str. EDL933]" 88.99 115 96.91 97.94 7.07e-60 GB AAN81621 "Putative head-DNA stabilization protein of prophage [Escherichia coli CFT073]" 100.00 112 97.25 98.17 1.61e-68 GB AAQ93654 "pDfusion [Expression vector pAT222]" 82.57 131 100.00 100.00 2.32e-54 GB AAQ93658 "pDfusion [Expression vector pAT223]" 82.57 134 100.00 100.00 3.13e-54 REF NP_040586 "head-DNA stabilization protein [Enterobacteria phage lambda]" 100.00 110 100.00 100.00 4.24e-71 REF NP_287372 "head-DNA stabilization protein of prophage CP-933X, partial [Escherichia coli O157:H7 str. EDL933]" 88.99 115 96.91 97.94 7.07e-60 REF NP_309661 "major capsid protein [Escherichia coli O157:H7 str. Sakai]" 100.00 110 99.08 99.08 6.48e-70 REF NP_310202 "head decoration protein [Escherichia coli O157:H7 str. Sakai]" 100.00 110 99.08 99.08 6.48e-70 REF NP_755051 "head-DNA stabilization protein of prophage [Escherichia coli CFT073]" 100.00 112 97.25 98.17 1.61e-68 SP P03712 "RecName: Full=Capsid decoration protein; AltName: Full=Auxiliary protein D; AltName: Full=Gene product D; Short=gpD; AltName: F" 100.00 110 100.00 100.00 4.24e-71 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $gpD 'Bacteriophage lambda' 10710 virus . Bacteriophage lambda 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 $gpD '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 $gpD 1.5 mM . . '[U-98% 15N]' 'potassium phosphate' . mM 20 50 . stop_ save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model DRX _Field_strength 600 _Details . save_ save_NMR_spectrometer _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model Avance _Field_strength 800 _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 6.0 0.2 n/a temperature 298 1 K 'ionic strength' 0.02 0.01 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 DSS H 1 'methyl protons' ppm 0.0 internal direct . . . 1.0 DSS N 15 'methyl protons' ppm 0.0 . indirect . . . 0.101329118 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_shiftset_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 gpD _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 . 2 SER N N 121.3 0.2 1 2 . 2 SER H H 8.31 0.03 1 3 . 3 LYS N N 123.3 0.2 1 4 . 3 LYS H H 8.49 0.03 1 5 . 3 LYS HA H 4.42 0.03 1 6 . 3 LYS HB2 H 1.40 0.03 2 7 . 3 LYS HB3 H 1.70 0.03 2 8 . 4 GLU N N 121.8 0.2 1 9 . 4 GLU H H 8.44 0.03 1 10 . 4 GLU HA H 4.22 0.03 1 11 . 4 GLU HB2 H 1.81 0.03 1 12 . 4 GLU HB3 H 1.81 0.03 1 13 . 4 GLU HG2 H 2.12 0.03 1 14 . 4 GLU HG3 H 2.12 0.03 1 15 . 5 THR N N 116.0 0.2 1 16 . 5 THR H H 8.09 0.03 1 17 . 5 THR HA H 4.17 0.03 1 18 . 5 THR HB H 3.94 0.03 1 19 . 5 THR HG2 H 1.00 0.03 1 20 . 6 PHE N N 121.8 0.2 1 21 . 6 PHE H H 8.13 0.03 1 22 . 6 PHE HA H 4.62 0.03 1 23 . 6 PHE HB2 H 2.93 0.03 2 24 . 6 PHE HB3 H 3.04 0.03 2 25 . 6 PHE HD1 H 7.11 0.03 1 26 . 6 PHE HD2 H 7.11 0.03 1 27 . 7 THR N N 114.9 0.2 1 28 . 7 THR H H 8.12 0.03 1 29 . 7 THR HA H 4.22 0.03 1 30 . 7 THR HB H 4.04 0.03 1 31 . 7 THR HG2 H 1.04 0.03 1 32 . 8 HIS N N 123.1 0.2 1 33 . 8 HIS H H 8.23 0.03 1 34 . 8 HIS HA H 4.69 0.03 1 35 . 8 HIS HB2 H 2.45 0.03 2 36 . 8 HIS HB3 H 2.59 0.03 2 37 . 9 TYR N N 121.5 0.2 1 38 . 9 TYR H H 8.12 0.03 1 39 . 9 TYR HA H 4.58 0.03 1 40 . 9 TYR HB2 H 2.75 0.03 2 41 . 9 TYR HB3 H 2.87 0.03 2 42 . 9 TYR HD1 H 6.92 0.03 1 43 . 9 TYR HD2 H 6.92 0.03 1 44 . 9 TYR HE1 H 6.70 0.03 1 45 . 9 TYR HE2 H 6.70 0.03 1 46 . 10 GLN N N 124.6 0.2 1 47 . 10 GLN H H 8.07 0.03 1 48 . 10 GLN HA H 4.40 0.03 1 49 . 10 GLN HB2 H 1.74 0.03 2 50 . 10 GLN HB3 H 1.89 0.03 2 51 . 10 GLN HG2 H 2.18 0.03 1 52 . 10 GLN HG3 H 2.18 0.03 1 53 . 10 GLN NE2 N 112.0 0.2 1 54 . 10 GLN HE21 H 7.39 0.03 2 55 . 10 GLN HE22 H 6.75 0.03 2 56 . 11 PRO HA H 4.71 0.03 1 57 . 11 PRO HD2 H 2.76 0.03 2 58 . 11 PRO HD3 H 2.86 0.03 2 59 . 12 GLN N N 120.0 0.2 1 60 . 12 GLN H H 8.42 0.03 1 61 . 12 GLN HA H 4.24 0.03 1 62 . 12 GLN HB2 H 1.87 0.03 2 63 . 12 GLN HB3 H 2.02 0.03 2 64 . 12 GLN HG2 H 2.29 0.03 1 65 . 12 GLN HG3 H 2.29 0.03 1 66 . 12 GLN NE2 N 112.3 0.2 1 67 . 12 GLN HE21 H 7.41 0.03 2 68 . 12 GLN HE22 H 6.75 0.03 2 69 . 13 GLY N N 110.0 0.2 1 70 . 13 GLY H H 8.36 0.03 1 71 . 13 GLY HA2 H 3.86 0.03 2 72 . 13 GLY HA3 H 4.70 0.03 2 73 . 14 ASN N N 118.7 0.2 1 74 . 14 ASN H H 8.27 0.03 1 75 . 14 ASN HA H 4.69 0.03 1 76 . 14 ASN HB2 H 2.65 0.03 2 77 . 14 ASN HB3 H 2.68 0.03 2 78 . 14 ASN ND2 N 112.4 0.2 1 79 . 14 ASN HD21 H 7.45 0.03 2 80 . 14 ASN HD22 H 6.77 0.03 2 81 . 15 SER N N 115.5 0.2 1 82 . 15 SER H H 8.16 0.03 1 83 . 15 SER HA H 4.63 0.03 1 84 . 15 SER HB2 H 3.76 0.03 2 85 . 15 SER HB3 H 4.38 0.03 2 86 . 16 ASP N N 121.1 0.2 1 87 . 16 ASP H H 9.10 0.03 1 88 . 16 ASP HA H 4.47 0.03 1 89 . 16 ASP HB2 H 1.72 0.03 2 90 . 16 ASP HB3 H 2.06 0.03 2 91 . 17 PRO HA H 4.24 0.03 1 92 . 17 PRO HB2 H 1.87 0.03 2 93 . 17 PRO HB3 H 2.16 0.03 2 94 . 17 PRO HG2 H 1.83 0.03 2 95 . 17 PRO HG3 H 1.90 0.03 2 96 . 17 PRO HD2 H 3.45 0.03 2 97 . 17 PRO HD3 H 3.49 0.03 2 98 . 18 ALA N N 122.6 0.2 1 99 . 18 ALA H H 8.22 0.03 1 100 . 18 ALA HA H 4.22 0.03 1 101 . 18 ALA HB H 1.21 0.03 1 102 . 19 HIS N N 117.3 0.2 1 103 . 19 HIS H H 7.98 0.03 1 104 . 19 HIS HA H 4.90 0.03 1 105 . 19 HIS HB2 H 3.07 0.03 2 106 . 19 HIS HB3 H 3.32 0.03 2 107 . 19 HIS HD2 H 7.01 0.03 1 108 . 19 HIS HE1 H 7.96 0.03 1 109 . 20 THR N N 111.6 0.2 1 110 . 20 THR H H 8.13 0.03 1 111 . 20 THR HA H 5.06 0.03 1 112 . 20 THR HB H 3.74 0.03 1 113 . 20 THR HG2 H 0.68 0.03 1 114 . 21 ALA N N 123.6 0.2 1 115 . 21 ALA H H 8.64 0.03 1 116 . 21 ALA HA H 4.42 0.03 1 117 . 21 ALA HB H 0.80 0.03 1 118 . 22 THR N N 107.6 0.2 1 119 . 22 THR H H 7.77 0.03 1 120 . 22 THR HA H 5.88 0.03 1 121 . 22 THR HB H 3.86 0.03 1 122 . 22 THR HG2 H 1.04 0.03 1 123 . 23 ALA N N 123.0 0.2 1 124 . 23 ALA H H 8.58 0.03 1 125 . 23 ALA HA H 4.87 0.03 1 126 . 23 ALA HB H 1.44 0.03 1 127 . 24 PRO HA H 4.88 0.03 1 128 . 24 PRO HB2 H 2.44 0.03 2 129 . 24 PRO HB3 H 1.83 0.03 2 130 . 24 PRO HG2 H 1.44 0.03 2 131 . 24 PRO HG3 H 2.17 0.03 2 132 . 24 PRO HD2 H 3.67 0.03 2 133 . 24 PRO HD3 H 3.81 0.03 2 134 . 25 GLY N N 108.3 0.2 1 135 . 25 GLY H H 8.04 0.03 1 136 . 25 GLY HA2 H 4.54 0.03 2 137 . 25 GLY HA3 H 3.34 0.03 2 138 . 26 GLY N N 111.7 0.2 1 139 . 26 GLY H H 8.82 0.03 1 140 . 26 GLY HA2 H 3.08 0.03 2 141 . 26 GLY HA3 H 4.67 0.03 2 142 . 27 LEU N N 119.8 0.2 1 143 . 27 LEU H H 8.32 0.03 1 144 . 27 LEU HA H 4.28 0.03 1 145 . 27 LEU HB2 H 1.71 0.03 2 146 . 27 LEU HB3 H 1.29 0.03 2 147 . 27 LEU HG H 1.64 0.03 1 148 . 27 LEU HD1 H 0.73 0.03 2 149 . 27 LEU HD2 H 0.79 0.03 2 150 . 28 SER N N 112.7 0.2 1 151 . 28 SER H H 8.43 0.03 1 152 . 28 SER HA H 4.69 0.03 1 153 . 28 SER HB2 H 3.89 0.03 2 154 . 28 SER HB3 H 4.48 0.03 2 155 . 29 ALA N N 123.3 0.2 1 156 . 29 ALA H H 7.63 0.03 1 157 . 29 ALA HA H 4.47 0.03 1 158 . 29 ALA HB H 1.35 0.03 1 159 . 30 LYS N N 117.4 0.2 1 160 . 30 LYS H H 8.17 0.03 1 161 . 30 LYS HA H 4.32 0.03 1 162 . 30 LYS HB2 H 1.77 0.03 1 163 . 30 LYS HB3 H 1.77 0.03 1 164 . 30 LYS HG2 H 1.48 0.03 1 165 . 30 LYS HG3 H 1.48 0.03 1 166 . 30 LYS HD2 H 1.64 0.03 1 167 . 30 LYS HD3 H 1.64 0.03 1 168 . 30 LYS HE2 H 2.89 0.03 1 169 . 30 LYS HE3 H 2.89 0.03 1 170 . 31 ALA N N 127.4 0.2 1 171 . 31 ALA H H 8.96 0.03 1 172 . 31 ALA HA H 4.98 0.03 1 173 . 31 ALA HB H 1.25 0.03 1 174 . 32 PRO HA H 4.50 0.03 1 175 . 32 PRO HB2 H 1.95 0.03 2 176 . 32 PRO HB3 H 2.22 0.03 2 177 . 32 PRO HG2 H 1.77 0.03 2 178 . 32 PRO HG3 H 1.86 0.03 2 179 . 32 PRO HD2 H 3.51 0.03 2 180 . 32 PRO HD3 H 3.62 0.03 2 181 . 33 ALA N N 122.5 0.2 1 182 . 33 ALA H H 8.55 0.03 1 183 . 33 ALA HA H 3.48 0.03 1 184 . 33 ALA HB H 1.17 0.03 1 185 . 34 MET N N 106.3 0.2 1 186 . 34 MET H H 8.99 0.03 1 187 . 34 MET HA H 4.04 0.03 1 188 . 34 MET HB2 H 2.15 0.03 2 189 . 34 MET HB3 H 2.29 0.03 2 190 . 34 MET HG2 H 2.83 0.03 1 191 . 34 MET HG3 H 2.83 0.03 1 192 . 34 MET HE H 1.74 0.03 1 193 . 35 THR N N 118.6 0.2 1 194 . 35 THR H H 7.27 0.03 1 195 . 35 THR HA H 4.44 0.03 1 196 . 35 THR HB H 3.93 0.03 1 197 . 35 THR HG2 H 1.34 0.03 1 198 . 36 PRO HA H 4.86 0.03 1 199 . 36 PRO HB2 H 1.23 0.03 2 200 . 36 PRO HB3 H 2.08 0.03 2 201 . 36 PRO HG2 H 1.62 0.03 2 202 . 36 PRO HG3 H 2.33 0.03 2 203 . 36 PRO HD2 H 4.03 0.03 2 204 . 36 PRO HD3 H 4.21 0.03 2 205 . 37 LEU N N 124.1 0.2 1 206 . 37 LEU H H 8.74 0.03 1 207 . 37 LEU HA H 5.23 0.03 1 208 . 37 LEU HB2 H 0.99 0.03 2 209 . 37 LEU HB3 H 1.22 0.03 2 210 . 37 LEU HG H 1.67 0.03 1 211 . 37 LEU HD1 H 0.42 0.03 2 212 . 37 LEU HD2 H 0.49 0.03 2 213 . 38 MET N N 118.8 0.2 1 214 . 38 MET H H 9.68 0.03 1 215 . 38 MET HA H 4.95 0.03 1 216 . 38 MET HB2 H 2.39 0.03 2 217 . 38 MET HB3 H 1.51 0.03 2 218 . 38 MET HG2 H 2.09 0.03 1 219 . 38 MET HG3 H 2.09 0.03 1 220 . 38 MET HE H 2.15 0.03 1 221 . 39 LEU N N 122.1 0.2 1 222 . 39 LEU H H 8.88 0.03 1 223 . 39 LEU HA H 4.40 0.03 1 224 . 39 LEU HB2 H 1.22 0.03 2 225 . 39 LEU HB3 H 1.49 0.03 2 226 . 39 LEU HG H 1.39 0.03 1 227 . 39 LEU HD1 H 0.61 0.03 2 228 . 39 LEU HD2 H 0.75 0.03 2 229 . 40 ASP N N 125.4 0.2 1 230 . 40 ASP H H 8.67 0.03 1 231 . 40 ASP HA H 4.69 0.03 1 232 . 40 ASP HB2 H 2.56 0.03 2 233 . 40 ASP HB3 H 2.94 0.03 2 234 . 41 THR N N 118.7 0.2 1 235 . 41 THR H H 8.54 0.03 1 236 . 41 THR HA H 4.24 0.03 1 237 . 41 THR HB H 3.78 0.03 1 238 . 41 THR HG2 H 1.22 0.03 1 239 . 42 SER N N 116.1 0.2 1 240 . 42 SER H H 8.40 0.03 1 241 . 42 SER HA H 4.38 0.03 1 242 . 42 SER HB2 H 3.80 0.03 2 243 . 42 SER HB3 H 3.89 0.03 2 244 . 43 SER N N 115.1 0.2 1 245 . 43 SER H H 8.04 0.03 1 246 . 43 SER HA H 4.26 0.03 1 247 . 43 SER HB2 H 3.77 0.03 2 248 . 43 SER HB3 H 3.87 0.03 2 249 . 44 ARG N N 116.7 0.2 1 250 . 44 ARG H H 8.33 0.03 1 251 . 44 ARG HA H 3.77 0.03 1 252 . 44 ARG HB2 H 1.53 0.03 2 253 . 44 ARG HB3 H 1.98 0.03 2 254 . 44 ARG HG2 H 0.61 0.03 2 255 . 44 ARG HG3 H 1.44 0.03 2 256 . 44 ARG HD2 H 3.10 0.03 1 257 . 44 ARG HD3 H 3.10 0.03 1 258 . 44 ARG NE N 84.3 0.2 1 259 . 44 ARG HE H 7.14 0.03 1 260 . 45 LYS N N 116.9 0.2 1 261 . 45 LYS H H 7.52 0.03 1 262 . 45 LYS HA H 4.27 0.03 1 263 . 45 LYS HB2 H 1.23 0.03 2 264 . 45 LYS HB3 H 1.43 0.03 2 265 . 45 LYS HG2 H 0.95 0.03 1 266 . 45 LYS HG3 H 0.95 0.03 1 267 . 45 LYS HD2 H 1.18 0.03 1 268 . 45 LYS HD3 H 1.18 0.03 1 269 . 45 LYS HE2 H 2.87 0.03 1 270 . 45 LYS HE3 H 2.87 0.03 1 271 . 46 LEU N N 119.1 0.2 1 272 . 46 LEU H H 8.22 0.03 1 273 . 46 LEU HA H 4.74 0.03 1 274 . 46 LEU HB2 H 0.83 0.03 2 275 . 46 LEU HB3 H 1.60 0.03 2 276 . 46 LEU HG H 1.36 0.03 1 277 . 46 LEU HD1 H -0.02 0.03 2 278 . 46 LEU HD2 H 0.13 0.03 2 279 . 47 VAL N N 113.6 0.2 1 280 . 47 VAL H H 8.82 0.03 1 281 . 47 VAL HA H 4.42 0.03 1 282 . 47 VAL HB H 2.22 0.03 1 283 . 47 VAL HG1 H 0.75 0.03 2 284 . 47 VAL HG2 H 0.64 0.03 2 285 . 48 ALA N N 123.8 0.2 1 286 . 48 ALA H H 8.60 0.03 1 287 . 48 ALA HA H 4.28 0.03 1 288 . 48 ALA HB H 1.27 0.03 1 289 . 49 TRP N N 122.1 0.2 1 290 . 49 TRP H H 8.93 0.03 1 291 . 49 TRP HA H 4.44 0.03 1 292 . 49 TRP HB2 H 1.28 0.03 2 293 . 49 TRP HB3 H 3.03 0.03 2 294 . 49 TRP NE1 N 132.9 0.2 1 295 . 49 TRP HD1 H 7.59 0.03 1 296 . 49 TRP HE3 H 7.29 0.03 1 297 . 49 TRP HE1 H 10.94 0.03 1 298 . 49 TRP HZ3 H 7.24 0.03 1 299 . 49 TRP HZ2 H 7.43 0.03 1 300 . 49 TRP HH2 H 6.89 0.03 1 301 . 50 ASP N N 129.4 0.2 1 302 . 50 ASP H H 7.07 0.03 1 303 . 50 ASP HA H 3.94 0.03 1 304 . 50 ASP HB2 H 2.52 0.03 2 305 . 50 ASP HB3 H 2.73 0.03 2 306 . 51 GLY HA2 H 0.97 0.03 2 307 . 51 GLY HA3 H 3.09 0.03 2 308 . 52 THR N N 108.8 0.2 1 309 . 52 THR H H 7.60 0.03 1 310 . 52 THR HA H 4.15 0.03 1 311 . 52 THR HB H 3.96 0.03 1 312 . 52 THR HG2 H 0.80 0.03 1 313 . 53 THR N N 123.5 0.2 1 314 . 53 THR H H 9.46 0.03 1 315 . 53 THR HA H 4.18 0.03 1 316 . 53 THR HB H 4.27 0.03 1 317 . 53 THR HG2 H 1.21 0.03 1 318 . 54 ASP N N 129.4 0.2 1 319 . 54 ASP H H 8.68 0.03 1 320 . 54 ASP HA H 4.58 0.03 1 321 . 54 ASP HB2 H 2.51 0.03 2 322 . 54 ASP HB3 H 2.58 0.03 2 323 . 55 GLY N N 109.7 0.2 1 324 . 55 GLY H H 8.82 0.03 1 325 . 55 GLY HA2 H 3.93 0.03 2 326 . 55 GLY HA3 H 3.86 0.03 2 327 . 56 ALA N N 118.3 0.2 1 328 . 56 ALA H H 6.94 0.03 1 329 . 56 ALA HA H 4.46 0.03 1 330 . 56 ALA HB H 1.42 0.03 1 331 . 57 ALA N N 122.5 0.2 1 332 . 57 ALA H H 7.77 0.03 1 333 . 57 ALA HA H 4.16 0.03 1 334 . 57 ALA HB H -0.39 0.03 1 335 . 58 VAL N N 113.3 0.2 1 336 . 58 VAL H H 8.49 0.03 1 337 . 58 VAL HA H 4.56 0.03 1 338 . 58 VAL HB H 2.17 0.03 1 339 . 58 VAL HG1 H 0.75 0.03 2 340 . 58 VAL HG2 H 0.42 0.03 2 341 . 59 GLY N N 103.0 0.2 1 342 . 59 GLY H H 7.29 0.03 1 343 . 59 GLY HA2 H 4.59 0.03 2 344 . 59 GLY HA3 H 4.02 0.03 2 345 . 60 ILE N N 119.5 0.2 1 346 . 60 ILE H H 8.16 0.03 1 347 . 60 ILE HA H 4.28 0.03 1 348 . 60 ILE HB H 1.06 0.03 1 349 . 60 ILE HG2 H 0.17 0.03 1 350 . 60 ILE HG12 H 0.42 0.03 2 351 . 60 ILE HG13 H 0.91 0.03 2 352 . 60 ILE HD1 H -0.61 0.03 1 353 . 61 LEU N N 130.1 0.2 1 354 . 61 LEU H H 8.94 0.03 1 355 . 61 LEU HA H 3.92 0.03 1 356 . 61 LEU HB2 H 1.37 0.03 2 357 . 61 LEU HB3 H 1.93 0.03 2 358 . 61 LEU HG H 1.15 0.03 1 359 . 61 LEU HD1 H 0.86 0.03 2 360 . 61 LEU HD2 H 1.53 0.03 2 361 . 62 ALA N N 128.0 0.2 1 362 . 62 ALA H H 9.21 0.03 1 363 . 62 ALA HA H 4.45 0.03 1 364 . 62 ALA HB H 0.43 0.03 1 365 . 63 VAL N N 117.5 0.2 1 366 . 63 VAL H H 6.76 0.03 1 367 . 63 VAL HA H 4.04 0.03 1 368 . 63 VAL HB H 1.93 0.03 1 369 . 63 VAL HG1 H 0.74 0.03 2 370 . 63 VAL HG2 H 1.00 0.03 2 371 . 64 ALA N N 127.9 0.2 1 372 . 64 ALA H H 8.59 0.03 1 373 . 64 ALA HA H 4.23 0.03 1 374 . 64 ALA HB H 1.41 0.03 1 375 . 65 ALA N N 123.1 0.2 1 376 . 65 ALA H H 8.33 0.03 1 377 . 65 ALA HA H 4.64 0.03 1 378 . 65 ALA HB H 1.47 0.03 1 379 . 66 ASP N N 117.8 0.2 1 380 . 66 ASP H H 8.64 0.03 1 381 . 66 ASP HA H 4.69 0.03 1 382 . 66 ASP HB2 H 2.62 0.03 2 383 . 66 ASP HB3 H 2.90 0.03 2 384 . 67 GLN N N 118.2 0.2 1 385 . 67 GLN H H 9.34 0.03 1 386 . 67 GLN HA H 4.25 0.03 1 387 . 67 GLN HB2 H 2.02 0.03 2 388 . 67 GLN HB3 H 1.71 0.03 2 389 . 67 GLN HG2 H 2.16 0.03 2 390 . 67 GLN HG3 H 2.41 0.03 2 391 . 67 GLN NE2 N 111.3 0.2 1 392 . 67 GLN HE21 H 6.73 0.03 2 393 . 67 GLN HE22 H 7.51 0.03 2 394 . 68 THR N N 112.7 0.2 1 395 . 68 THR H H 8.94 0.03 1 396 . 68 THR HA H 4.69 0.03 1 397 . 68 THR HB H 4.30 0.03 1 398 . 68 THR HG2 H 1.12 0.03 1 399 . 69 SER N N 120.2 0.2 1 400 . 69 SER H H 7.69 0.03 1 401 . 69 SER HA H 4.46 0.03 1 402 . 69 SER HB2 H 3.92 0.03 2 403 . 69 SER HB3 H 3.94 0.03 2 404 . 69 SER HG H 5.56 0.03 1 405 . 70 THR N N 119.7 0.2 1 406 . 70 THR H H 8.50 0.03 1 407 . 70 THR HA H 4.69 0.03 1 408 . 70 THR HB H 4.26 0.03 1 409 . 70 THR HG2 H 1.28 0.03 1 410 . 71 THR N N 116.4 0.2 1 411 . 71 THR H H 7.86 0.03 1 412 . 71 THR HA H 4.71 0.03 1 413 . 71 THR HB H 3.79 0.03 1 414 . 71 THR HG2 H 1.03 0.03 1 415 . 72 LEU N N 122.8 0.2 1 416 . 72 LEU H H 9.15 0.03 1 417 . 72 LEU HA H 4.83 0.03 1 418 . 72 LEU HB2 H 1.48 0.03 2 419 . 72 LEU HB3 H 1.25 0.03 2 420 . 72 LEU HG H 1.03 0.03 1 421 . 72 LEU HD1 H 0.71 0.03 2 422 . 72 LEU HD2 H 0.78 0.03 2 423 . 73 THR N N 118.1 0.2 1 424 . 73 THR H H 9.17 0.03 1 425 . 73 THR HA H 5.04 0.03 1 426 . 73 THR HB H 3.74 0.03 1 427 . 73 THR HG2 H 0.89 0.03 1 428 . 74 PHE N N 123.8 0.2 1 429 . 74 PHE H H 9.20 0.03 1 430 . 74 PHE HA H 4.98 0.03 1 431 . 74 PHE HB2 H 2.51 0.03 2 432 . 74 PHE HB3 H 2.35 0.03 2 433 . 74 PHE HD1 H 6.73 0.03 1 434 . 74 PHE HD2 H 6.73 0.03 1 435 . 74 PHE HE1 H 6.97 0.03 1 436 . 74 PHE HE2 H 6.97 0.03 1 437 . 74 PHE HZ H 7.11 0.03 1 438 . 75 TYR N N 118.7 0.2 1 439 . 75 TYR H H 9.56 0.03 1 440 . 75 TYR HA H 4.92 0.03 1 441 . 75 TYR HB2 H 2.51 0.03 2 442 . 75 TYR HB3 H 3.21 0.03 2 443 . 75 TYR HD1 H 6.77 0.03 1 444 . 75 TYR HD2 H 6.77 0.03 1 445 . 75 TYR HE1 H 6.79 0.03 1 446 . 75 TYR HE2 H 6.79 0.03 1 447 . 76 LYS N N 120.4 0.2 1 448 . 76 LYS H H 8.74 0.03 1 449 . 76 LYS HA H 4.83 0.03 1 450 . 76 LYS HB2 H 1.56 0.03 2 451 . 76 LYS HB3 H 1.95 0.03 2 452 . 76 LYS HG2 H 1.19 0.03 1 453 . 76 LYS HG3 H 1.19 0.03 1 454 . 76 LYS HD2 H 1.35 0.03 1 455 . 76 LYS HD3 H 1.35 0.03 1 456 . 76 LYS HE2 H 2.86 0.03 1 457 . 76 LYS HE3 H 2.86 0.03 1 458 . 77 SER N N 113.4 0.2 1 459 . 77 SER H H 7.96 0.03 1 460 . 77 SER HA H 4.28 0.03 1 461 . 77 SER HB2 H 3.77 0.03 2 462 . 77 SER HB3 H 3.93 0.03 2 463 . 78 GLY N N 105.9 0.2 1 464 . 78 GLY H H 7.61 0.03 1 465 . 78 GLY HA2 H 3.45 0.03 2 466 . 78 GLY HA3 H 4.25 0.03 2 467 . 79 THR N N 114.9 0.2 1 468 . 79 THR H H 7.67 0.03 1 469 . 79 THR HA H 4.91 0.03 1 470 . 79 THR HB H 3.58 0.03 1 471 . 79 THR HG2 H 0.90 0.03 1 472 . 80 PHE N N 124.7 0.2 1 473 . 80 PHE H H 8.86 0.03 1 474 . 80 PHE HA H 4.48 0.03 1 475 . 80 PHE HB2 H 2.15 0.03 2 476 . 80 PHE HB3 H 2.49 0.03 2 477 . 80 PHE HD1 H 6.62 0.03 1 478 . 80 PHE HD2 H 6.62 0.03 1 479 . 80 PHE HE1 H 6.35 0.03 1 480 . 80 PHE HE2 H 6.35 0.03 1 481 . 80 PHE HZ H 6.13 0.03 1 482 . 81 ARG N N 121.0 0.2 1 483 . 81 ARG H H 9.02 0.03 1 484 . 81 ARG HA H 4.70 0.03 1 485 . 81 ARG HB2 H 1.74 0.03 2 486 . 81 ARG HB3 H 2.05 0.03 2 487 . 81 ARG HG2 H 1.51 0.03 2 488 . 81 ARG HG3 H 1.70 0.03 2 489 . 81 ARG HD2 H 3.14 0.03 1 490 . 81 ARG HD3 H 3.14 0.03 1 491 . 81 ARG NE N 83.8 0.2 1 492 . 81 ARG HE H 7.35 0.03 1 493 . 82 TYR N N 125.5 0.2 1 494 . 82 TYR H H 9.52 0.03 1 495 . 82 TYR HA H 4.11 0.03 1 496 . 82 TYR HB2 H 3.10 0.03 2 497 . 82 TYR HB3 H 3.04 0.03 2 498 . 82 TYR HD1 H 6.95 0.03 1 499 . 82 TYR HD2 H 6.95 0.03 1 500 . 82 TYR HE1 H 6.44 0.03 1 501 . 82 TYR HE2 H 6.44 0.03 1 502 . 83 GLU N N 114.8 0.2 1 503 . 83 GLU H H 9.88 0.03 1 504 . 83 GLU HA H 4.11 0.03 1 505 . 83 GLU HB2 H 2.02 0.03 2 506 . 83 GLU HB3 H 2.06 0.03 2 507 . 83 GLU HG2 H 2.37 0.03 2 508 . 83 GLU HG3 H 2.42 0.03 2 509 . 84 ASP N N 117.8 0.2 1 510 . 84 ASP H H 7.87 0.03 1 511 . 84 ASP HA H 4.67 0.03 1 512 . 84 ASP HB2 H 2.73 0.03 2 513 . 84 ASP HB3 H 2.81 0.03 2 514 . 85 VAL N N 120.2 0.2 1 515 . 85 VAL H H 6.69 0.03 1 516 . 85 VAL HA H 3.34 0.03 1 517 . 85 VAL HB H 0.88 0.03 1 518 . 85 VAL HG1 H -0.69 0.03 2 519 . 85 VAL HG2 H 0.41 0.03 2 520 . 86 LEU N N 128.6 0.2 1 521 . 86 LEU H H 7.54 0.03 1 522 . 86 LEU HA H 4.40 0.03 1 523 . 86 LEU HB2 H 1.29 0.03 2 524 . 86 LEU HB3 H 1.33 0.03 2 525 . 86 LEU HG H 1.19 0.03 1 526 . 86 LEU HD1 H 0.70 0.03 2 527 . 86 LEU HD2 H 0.84 0.03 2 528 . 87 TRP N N 124.3 0.2 1 529 . 87 TRP H H 7.31 0.03 1 530 . 87 TRP HA H 4.44 0.03 1 531 . 87 TRP HB2 H 2.99 0.03 2 532 . 87 TRP HB3 H 3.15 0.03 2 533 . 87 TRP NE1 N 130.8 0.2 1 534 . 87 TRP HD1 H 7.24 0.03 1 535 . 87 TRP HE3 H 7.62 0.03 1 536 . 87 TRP HE1 H 9.25 0.03 1 537 . 87 TRP HZ3 H 6.83 0.03 1 538 . 87 TRP HZ2 H 7.20 0.03 1 539 . 87 TRP HH2 H 7.33 0.03 1 540 . 88 PRO HA H 4.61 0.03 1 541 . 88 PRO HB2 H 1.81 0.03 2 542 . 88 PRO HB3 H 1.67 0.03 2 543 . 88 PRO HG2 H 1.91 0.03 2 544 . 88 PRO HG3 H 2.09 0.03 2 545 . 88 PRO HD2 H 2.56 0.03 2 546 . 88 PRO HD3 H 3.03 0.03 2 547 . 89 GLU N N 124.2 0.2 1 548 . 89 GLU H H 8.84 0.03 1 549 . 89 GLU HA H 3.84 0.03 1 550 . 89 GLU HB2 H 1.93 0.03 1 551 . 89 GLU HB3 H 1.93 0.03 1 552 . 89 GLU HG2 H 2.28 0.03 1 553 . 89 GLU HG3 H 2.28 0.03 1 554 . 90 ALA N N 116.7 0.2 1 555 . 90 ALA H H 8.07 0.03 1 556 . 90 ALA HA H 3.97 0.03 1 557 . 90 ALA HB H 1.22 0.03 1 558 . 91 ALA N N 119.5 0.2 1 559 . 91 ALA H H 7.24 0.03 1 560 . 91 ALA HA H 4.47 0.03 1 561 . 91 ALA HB H 1.23 0.03 1 562 . 92 SER N N 116.2 0.2 1 563 . 92 SER H H 7.78 0.03 1 564 . 92 SER HA H 4.29 0.03 1 565 . 92 SER HB2 H 3.68 0.03 2 566 . 92 SER HB3 H 3.93 0.03 2 567 . 93 ASP N N 122.2 0.2 1 568 . 93 ASP H H 8.10 0.03 1 569 . 93 ASP HA H 4.75 0.03 1 570 . 93 ASP HB2 H 2.55 0.03 2 571 . 93 ASP HB3 H 2.76 0.03 2 572 . 94 GLU N N 127.4 0.2 1 573 . 94 GLU H H 9.03 0.03 1 574 . 94 GLU HA H 3.76 0.03 1 575 . 94 GLU HB2 H 1.81 0.03 1 576 . 94 GLU HB3 H 1.81 0.03 1 577 . 94 GLU HG2 H 2.07 0.03 1 578 . 94 GLU HG3 H 2.07 0.03 1 579 . 95 THR N N 115.2 0.2 1 580 . 95 THR H H 8.18 0.03 1 581 . 95 THR HA H 3.79 0.03 1 582 . 95 THR HB H 4.19 0.03 1 583 . 95 THR HG2 H 1.12 0.03 1 584 . 96 LYS N N 122.8 0.2 1 585 . 96 LYS H H 7.96 0.03 1 586 . 96 LYS HA H 3.88 0.03 1 587 . 96 LYS HB2 H 1.56 0.03 2 588 . 96 LYS HB3 H 1.90 0.03 2 589 . 96 LYS HG2 H 1.39 0.03 1 590 . 96 LYS HG3 H 1.39 0.03 1 591 . 96 LYS HD2 H 1.50 0.03 1 592 . 96 LYS HD3 H 1.50 0.03 1 593 . 96 LYS HE2 H 2.77 0.03 1 594 . 96 LYS HE3 H 2.77 0.03 1 595 . 97 LYS N N 117.5 0.2 1 596 . 97 LYS H H 7.33 0.03 1 597 . 97 LYS HA H 3.55 0.03 1 598 . 97 LYS HB2 H 1.44 0.03 2 599 . 97 LYS HB3 H -0.24 0.03 2 600 . 97 LYS HG2 H 0.81 0.03 1 601 . 97 LYS HG3 H 0.81 0.03 1 602 . 97 LYS HD2 H 1.17 0.03 2 603 . 97 LYS HD3 H 0.61 0.03 2 604 . 97 LYS HE2 H 2.64 0.03 2 605 . 97 LYS HE3 H 2.19 0.03 2 606 . 98 ARG N N 113.8 0.2 1 607 . 98 ARG H H 8.24 0.03 1 608 . 98 ARG HA H 3.88 0.03 1 609 . 98 ARG HB2 H 1.73 0.03 2 610 . 98 ARG HB3 H 1.89 0.03 2 611 . 98 ARG HG2 H 1.41 0.03 2 612 . 98 ARG HG3 H 1.69 0.03 2 613 . 98 ARG HD2 H 2.85 0.03 2 614 . 98 ARG HD3 H 3.01 0.03 2 615 . 98 ARG NE N 84.8 0.2 1 616 . 98 ARG HE H 7.90 0.03 1 617 . 98 ARG HH22 H 6.11 0.03 2 618 . 99 THR N N 106.8 0.2 1 619 . 99 THR H H 7.50 0.03 1 620 . 99 THR HA H 4.70 0.03 1 621 . 99 THR HB H 4.57 0.03 1 622 . 99 THR HG2 H 1.20 0.03 1 623 . 100 ALA N N 126.3 0.2 1 624 . 100 ALA H H 7.44 0.03 1 625 . 100 ALA HA H 3.72 0.03 1 626 . 100 ALA HB H 0.56 0.03 1 627 . 101 PHE N N 111.4 0.2 1 628 . 101 PHE H H 8.27 0.03 1 629 . 101 PHE HA H 4.63 0.03 1 630 . 101 PHE HB2 H 2.60 0.03 2 631 . 101 PHE HB3 H 3.27 0.03 2 632 . 101 PHE HD1 H 7.04 0.03 1 633 . 101 PHE HD2 H 7.04 0.03 1 634 . 101 PHE HE1 H 6.90 0.03 1 635 . 101 PHE HE2 H 6.90 0.03 1 636 . 101 PHE HZ H 6.47 0.03 1 637 . 102 ALA N N 124.5 0.2 1 638 . 102 ALA H H 7.29 0.03 1 639 . 102 ALA HA H 4.17 0.03 1 640 . 102 ALA HB H 1.46 0.03 1 641 . 103 GLY N N 109.3 0.2 1 642 . 103 GLY H H 8.80 0.03 1 643 . 103 GLY HA2 H 4.14 0.03 2 644 . 103 GLY HA3 H 3.94 0.03 2 645 . 104 THR N N 110.8 0.2 1 646 . 104 THR H H 8.00 0.03 1 647 . 104 THR HA H 4.87 0.03 1 648 . 104 THR HB H 4.57 0.03 1 649 . 104 THR HG2 H 1.28 0.03 1 650 . 104 THR HG1 H 6.01 0.03 1 651 . 105 ALA N N 120.5 0.2 1 652 . 105 ALA H H 8.50 0.03 1 653 . 105 ALA HA H 4.56 0.03 1 654 . 105 ALA HB H 1.53 0.03 1 655 . 106 ILE N N 123.7 0.2 1 656 . 106 ILE H H 8.44 0.03 1 657 . 106 ILE HA H 4.51 0.03 1 658 . 106 ILE HB H 1.53 0.03 1 659 . 106 ILE HG2 H -0.14 0.03 1 660 . 106 ILE HG12 H 0.54 0.03 2 661 . 106 ILE HG13 H 1.25 0.03 2 662 . 106 ILE HD1 H 0.39 0.03 1 663 . 107 SER N N 122.9 0.2 1 664 . 107 SER H H 8.77 0.03 1 665 . 107 SER HA H 4.68 0.03 1 666 . 107 SER HB2 H 3.66 0.03 2 667 . 107 SER HB3 H 3.68 0.03 2 668 . 108 ILE N N 125.4 0.2 1 669 . 108 ILE H H 8.44 0.03 1 670 . 108 ILE HA H 5.32 0.03 1 671 . 108 ILE HB H 2.38 0.03 1 672 . 108 ILE HG2 H 1.71 0.03 1 673 . 108 ILE HG12 H 1.22 0.03 1 674 . 108 ILE HG13 H 1.22 0.03 1 675 . 108 ILE HD1 H 0.54 0.03 1 676 . 109 VAL N N 129.8 0.2 1 677 . 109 VAL H H 8.73 0.03 1 678 . 109 VAL HA H 4.35 0.03 1 679 . 109 VAL HB H 2.05 0.03 1 680 . 109 VAL HG1 H 0.67 0.03 2 681 . 109 VAL HG2 H 0.78 0.03 2 stop_ save_