data_4020 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Solution Structure of the Immunodominant Region of Protein G of Bovine Respiratory Syncytial Virus ; _BMRB_accession_number 4020 _BMRB_flat_file_name bmr4020.str _Entry_type update _Submission_date 1996-10-21 _Accession_date 1997-04-24 _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 Doreleijers Jurgen F. . 2 Langedijk Johannes PM. . 3 Herd Karl . . 4 Boelens Rolf . . 5 Rullmann Johan AC. . 6 Schaaper Wim M. . 7 'van Oirschot' Jan T. . 8 Kaptein Robert . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 183 "13C chemical shifts" 73 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2003-01-02 correction author 'Correction of typos.' 1999-10-16 reformat BMRB 'Format updated to NMR-STAR version 2.1.' 1997-05-07 original author 'original release.' stop_ save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full ; Doreleijers, J.F., Langedijk, J.P.M., Herd, K., Boelens, R., Rullmann, J.A.C., Schaaper, W. M., van Oirschot, J.T., and Kaptein, R., "Solution Structure of the Immunodominant Region of Protein G of Bovine Respiratory Syncytial Virus," Biochemistry 35, 14684-14688 (1996). ; _Citation_title ; Solution Structure of the Immunodominant Region of Protein G of Bovine Respiratory Syncytial Virus ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code 97098087 _PubMed_ID ? loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Doreleijers Jurgen F. . 2 Langedijk Johannes PM. . 3 Herd Karl . . 4 Boelens Rolf . . 5 Rullmann Johan AC. . 6 Schaaper Wim M. . 7 'van Oirschot' Jan T. . 8 Kaptein Robert . . stop_ _Journal_abbreviation Biochemistry _Journal_volume 35 _Journal_issue 47 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 14684 _Page_last 14688 _Year 1996 _Details ; ABSTRACT The three-dimensional solution structure of the immunodominant central conserved region of the attachment protein G (BRSV-G) of bovine respiratory syncytial virus has been determined by nuclear magnetic resonance (NMR) spectroscopy. In the 32-residue peptide studied, 19 residues form a small rigid core composed of two short helices, connected by a type I' turn, and linked by two disulfide bridges. This unique fold is among the smallest stable tertiary structures known and could therefore serve as an ideal building block for the design of de novo proteins and as a test case for modeling studies. A characteristic hydrophobic pocket, lined by conserved residues lies at the surface of the peptide and may play a role in receptor binding. This work provides a structural basis for further peptide vaccine development against the severe diseases associated with the respiratory syncytial viruses both in cattle and man. Bovine respiratory syncytial virus (BRSV) accounts for a high proportion of morbidity and mortality in cattle (Stott & Taylor, 1985; Baker et al., 1986) resulting in considerable economic losses. Furthermore, human RSV (HRSV) is a major cause of serious respiratory infections including bronchiolitis and pneumonia in infants and young children: these conditions are responsible for almost 100,000 hospitalizations yearly in the USA alone (Heilman, 1990). The development of efficacious vaccines against HRSV infections has a very high priority according to the World Health Organization (World Health Organization, 1995), and has lately received much attention (Hall, 1994; McIntosh & Chanock, 1990). Respiratory syncytial virus carries two glycoproteins on its surface: the fusion protein F and the attachment protein G. The latter is an integral membrane protein and is functionally distinct from other viral attachment proteins. The focus of the present study is the small conserved hydrophobic domain (Figure 1) that is located in the ectodomain and is presumably flanked in the intact protein G by two extended mucin-like regions (Langedijk et al., 1996b). This domain contains four conserved cysteines which form two disulfide bridges. Peptides based on this domain were found to be immunodominant in protein G of both HRSV (Norrby et al., 1987; Ekerlind-Stopner et al., 1990) and BRSV (Langedijk et al., 1996b); they can be used as antigens in highly specific and sensitive immunoassays (Langedijk et al., 1996a) and have conferred protection against HRSV challenge in mice (Trudel et al., 1991). We have studied a 32-residue synthetic peptide representing the conserved central region of protein G of BRSV using two-dimensional (2D) NMR, distance geometry (DG), and restrained molecular dynamics (RMD). ; loop_ _Keyword 'respiratory Syncytial virus' Peptides glycoproteins Pneumoviruses virus synthetic NMR stop_ save_ ################################## # Molecular system description # ################################## save_system_BRSV-G _Saveframe_category molecular_system _Mol_system_name 'Bovine Syncytial Respiratory Virus-G' _Abbreviation_common BRSV-G _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label BRSV-G $BRSV-G stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state monomer _System_paramagnetic no _System_thiol_state 'fully oxidized' _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_BRSV-G _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'Bovine Syncytial Respiratory Virus-G' _Abbreviation_common BRSV-G _Molecular_mass 3600 _Mol_thiol_state . _Details ; Studied peptide was 32 AA in size. The NMR models of the 19 AA forming the structured part (171-189) are submitted to the PDB. ; ############################## # Polymer residue sequence # ############################## _Residue_count 32 _Mol_residue_sequence ; NHQDHNNFQTLPYVPCSTCE GNLACLSLCHIE ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 158 ASN 2 159 HIS 3 160 GLN 4 161 ASP 5 162 HIS 6 163 ASN 7 164 ASN 8 165 PHE 9 166 GLN 10 167 THR 11 168 LEU 12 169 PRO 13 170 TYR 14 171 VAL 15 172 PRO 16 173 CYS 17 174 SER 18 175 THR 19 176 CYS 20 177 GLU 21 178 GLY 22 179 ASN 23 180 LEU 24 181 ALA 25 182 CYS 26 183 LEU 27 184 SER 28 185 LEU 29 186 CYS 30 187 HIS 31 188 ILE 32 189 GLU stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-06-02 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 1BRV "Solution Nmr Structure Of The Immunodominant Region Of Protein G Of Bovine Respiratory Syncytial Virus, 48 Structures" 100.00 32 100.00 100.00 6.10e-14 GB AAA42810 "G protein [Bovine respiratory syncytial virus]" 100.00 257 100.00 100.00 1.32e-14 GB AAF22721 "glycoprotein, partial [Bovine respiratory syncytial virus]" 100.00 106 100.00 100.00 5.77e-15 SP P22261 "RecName: Full=Major surface glycoprotein G; AltName: Full=Attachment glycoprotein G; AltName: Full=Membrane-bound glycoprotein;" 100.00 257 100.00 100.00 1.32e-14 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species _Strain $BRSV-G 'Bovine Respiratory Syncytial Virus' 11246 Viruses . . . 391-2 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 $BRSV-G 'chemical synthesis' . . . . . stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_one _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $BRSV-G 6.1 mM . TSP . mM . NaN3 . mM . stop_ save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer_one _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model AMX _Field_strength 600 _Details . save_ ####################### # Sample conditions # ####################### save_sample_conditions_one _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 4.6 . na temperature 285 . K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference_one _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 _Reference_correction_type _Correction_value TSP H 1 'methyl protons' ppm -0.01 internal direct . . . pH 0.005 TSP C 13 'methyl carbons' ppm -0.12 internal direct . . . pH 0.030 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_assigned_chemical_shifts_one _Saveframe_category assigned_chemical_shifts _Details . loop_ _Sample_label $sample_one stop_ _Sample_conditions_label $sample_conditions_one _Chem_shift_reference_set_label $chemical_shift_reference_one _Mol_system_component_name BRSV-G _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 ASN H H 8.32 0.005 1 2 . 1 ASN HA H 4.69 0.005 1 3 . 1 ASN HB2 H 2.91 0.005 2 4 . 1 ASN HB3 H 2.83 0.005 2 5 . 1 ASN CB C 38.6 0.05 1 6 . 1 ASN HD21 H 7.6 0.005 2 7 . 1 ASN HD22 H 6.95 0.005 2 8 . 2 HIS H H 8.58 0.005 1 9 . 2 HIS HA H 4.68 0.005 1 10 . 2 HIS HB2 H 3.3 0.005 2 11 . 2 HIS HB3 H 3.17 0.005 2 12 . 2 HIS CB C 28.8 0.05 1 13 . 2 HIS HD2 H 7.28 0.005 1 14 . 2 HIS HE1 H 8.59 0.005 1 15 . 3 GLN H H 8.64 0.005 1 16 . 3 GLN HA H 4.3 0.005 1 17 . 3 GLN HB2 H 2.09 0.005 2 18 . 3 GLN HB3 H 2.00 0.005 2 19 . 3 GLN CA C 56.3 0.05 1 20 . 3 GLN CB C 30.4 0.05 1 21 . 3 GLN HG2 H 2.36 0.005 1 22 . 3 GLN HG3 H 2.36 0.005 1 23 . 3 GLN CG C 36.1 0.05 1 24 . 3 GLN HE21 H 7.68 0.005 2 25 . 3 GLN HE22 H 7.2 0.005 2 26 . 4 ASP H H 8.51 0.005 1 27 . 4 ASP HA H 4.55 0.005 1 28 . 4 ASP HB2 H 2.68 0.005 2 29 . 4 ASP HB3 H 2.62 0.005 2 30 . 4 ASP CA C 54.4 0.05 1 31 . 4 ASP CB C 41.3 0.05 1 32 . 5 HIS H H 8.74 0.005 1 33 . 5 HIS HA H 4.68 0.005 1 34 . 5 HIS HB2 H 3.3 0.005 2 35 . 5 HIS HB3 H 3.18 0.005 2 36 . 5 HIS CB C 28.8 0.05 1 37 . 5 HIS HD2 H 7.27 0.005 1 38 . 5 HIS HE1 H 8.69 0.005 1 39 . 6 ASN H H 8.58 0.005 1 40 . 6 ASN HA H 4.64 0.005 1 41 . 6 ASN HB2 H 2.69 0.005 1 42 . 6 ASN HB3 H 2.69 0.005 1 43 . 6 ASN CA C 55.1 0.05 1 44 . 6 ASN CB C 38.9 0.05 1 45 . 6 ASN HD21 H 7.7 0.005 2 46 . 6 ASN HD22 H 7.00 0.005 2 47 . 7 ASN H H 8.46 0.005 1 48 . 7 ASN HA H 4.67 0.005 1 49 . 7 ASN HB2 H 2.76 0.005 2 50 . 7 ASN HB3 H 2.67 0.005 2 51 . 7 ASN CB C 38.8 0.05 1 52 . 7 ASN HD21 H 7.63 0.005 2 53 . 7 ASN HD22 H 6.94 0.005 2 54 . 8 PHE H H 8.26 0.005 1 55 . 8 PHE HA H 4.6 0.005 1 56 . 8 PHE HB2 H 3.16 0.005 2 57 . 8 PHE HB3 H 3.04 0.005 2 58 . 8 PHE CB C 39.3 0.05 1 59 . 8 PHE HD1 H 7.23 0.005 1 60 . 8 PHE HD2 H 7.23 0.005 1 61 . 8 PHE HE1 H 7.2 0.005 1 62 . 8 PHE HE2 H 7.2 0.005 1 63 . 8 PHE HZ H 7.34 0.005 1 64 . 9 GLN H H 8.31 0.005 1 65 . 9 GLN HA H 4.34 0.005 1 66 . 9 GLN HB2 H 2.06 0.005 2 67 . 9 GLN HB3 H 1.95 0.005 2 68 . 9 GLN CB C 30.3 0.05 1 69 . 9 GLN HG2 H 2.28 0.005 1 70 . 9 GLN HG3 H 2.28 0.005 1 71 . 9 GLN HE21 H 7.59 0.005 2 72 . 9 GLN HE22 H 6.91 0.005 2 73 . 10 THR H H 8.24 0.005 1 74 . 10 THR HA H 4.29 0.005 1 75 . 10 THR HB H 4.16 0.005 1 76 . 10 THR CA C 62.1 0.05 1 77 . 10 THR CB C 69.8 0.05 1 78 . 10 THR HG2 H 1.21 0.005 1 79 . 10 THR CG2 C 21.9 0.05 1 80 . 11 LEU H H 8.32 0.005 1 81 . 11 LEU HA H 4.61 0.005 1 82 . 11 LEU HB2 H 1.61 0.005 2 83 . 11 LEU HB3 H 1.43 0.005 2 84 . 11 LEU CB C 42.00 0.05 1 85 . 11 LEU HG H 1.67 0.005 1 86 . 11 LEU CG C 27.1 0.05 1 87 . 11 LEU HD1 H 0.93 0.005 2 88 . 11 LEU HD2 H 0.9 0.005 2 89 . 12 PRO HA H 4.4 0.005 1 90 . 12 PRO HB2 H 2.19 0.005 2 91 . 12 PRO HB3 H 1.85 0.005 2 92 . 12 PRO CA C 63.2 0.05 1 93 . 12 PRO CB C 31.9 0.05 1 94 . 12 PRO HG2 H 1.95 0.005 2 95 . 12 PRO HG3 H 1.99 0.005 2 96 . 12 PRO HD2 H 3.8 0.005 2 97 . 12 PRO HD3 H 3.58 0.005 2 98 . 12 PRO CD C 50.5 0.05 1 99 . 13 TYR H H 7.94 0.005 1 100 . 13 TYR HA H 4.6 0.005 1 101 . 13 TYR HB2 H 2.89 0.005 2 102 . 13 TYR HB3 H 2.84 0.005 2 103 . 13 TYR CB C 39.2 0.05 1 104 . 13 TYR HD1 H 6.91 0.005 1 105 . 13 TYR HD2 H 6.91 0.005 1 106 . 13 TYR HE1 H 6.7 0.005 1 107 . 13 TYR HE2 H 6.7 0.005 1 108 . 14 VAL H H 8.46 0.005 1 109 . 14 VAL HA H 4.42 0.005 1 110 . 14 VAL HB H 1.95 0.005 1 111 . 14 VAL CA C 60.7 0.05 1 112 . 14 VAL CB C 33.6 0.05 1 113 . 14 VAL HG1 H 0.85 0.005 1 114 . 14 VAL HG2 H 0.85 0.005 1 115 . 14 VAL CG1 C 21.3 0.05 2 116 . 14 VAL CG2 C 20.4 0.05 2 117 . 15 PRO HA H 4.99 0.005 1 118 . 15 PRO HB2 H 2.51 0.005 1 119 . 15 PRO HB3 H 2.51 0.005 1 120 . 15 PRO CB C 32.2 0.05 1 121 . 15 PRO HG2 H 2.19 0.005 2 122 . 15 PRO HG3 H 2.02 0.005 2 123 . 15 PRO CG C 27.9 0.05 1 124 . 15 PRO HD2 H 3.95 0.005 2 125 . 15 PRO HD3 H 3.64 0.005 2 126 . 15 PRO CD C 51.3 0.05 1 127 . 16 CYS H H 8.86 0.005 1 128 . 16 CYS HA H 4.65 0.005 1 129 . 16 CYS HB2 H 2.85 0.005 1 130 . 16 CYS HB3 H 3.13 0.005 1 131 . 16 CYS CB C 40.2 0.05 1 132 . 17 SER H H 8.8 0.005 1 133 . 17 SER HA H 4.26 0.005 1 134 . 17 SER HB2 H 4.07 0.005 2 135 . 17 SER HB3 H 3.98 0.005 2 136 . 17 SER CA C 60.8 0.05 1 137 . 17 SER CB C 62.3 0.05 1 138 . 18 THR H H 7.79 0.005 1 139 . 18 THR HA H 4.65 0.005 1 140 . 18 THR HB H 4.44 0.005 1 141 . 18 THR CB C 70.1 0.05 1 142 . 18 THR HG2 H 1.28 0.005 1 143 . 18 THR CG2 C 21.8 0.05 1 144 . 19 CYS H H 7.6 0.005 1 145 . 19 CYS HA H 4.69 0.005 1 146 . 19 CYS HB2 H 2.98 0.005 1 147 . 19 CYS HB3 H 3.23 0.005 1 148 . 19 CYS CB C 35.2 0.05 1 149 . 20 GLU H H 9.05 0.005 1 150 . 20 GLU HA H 3.94 0.005 1 151 . 20 GLU HB2 H 2.25 0.005 2 152 . 20 GLU HB3 H 2.08 0.005 2 153 . 20 GLU CA C 56.8 0.05 1 154 . 20 GLU CB C 27.5 0.05 1 155 . 20 GLU HG2 H 2.34 0.005 2 156 . 20 GLU HG3 H 2.25 0.005 2 157 . 20 GLU CG C 35.5 0.05 1 158 . 21 GLY H H 8.8 0.005 1 159 . 21 GLY CA C 45.4 0.05 1 160 . 21 GLY HA2 H 3.56 0.005 1 161 . 21 GLY HA3 H 4.1 0.005 1 162 . 22 ASN H H 7.76 0.005 1 163 . 22 ASN HA H 4.57 0.005 1 164 . 22 ASN HB2 H 2.92 0.005 1 165 . 22 ASN HB3 H 2.83 0.005 1 166 . 22 ASN CA C 54.4 0.05 1 167 . 22 ASN CB C 39.6 0.05 1 168 . 22 ASN HD21 H 7.99 0.005 2 169 . 22 ASN HD22 H 7.21 0.005 2 170 . 23 LEU H H 8.86 0.005 1 171 . 23 LEU HA H 3.96 0.005 1 172 . 23 LEU HB2 H 1.78 0.005 1 173 . 23 LEU HB3 H 1.53 0.005 1 174 . 23 LEU CA C 58.5 0.05 1 175 . 23 LEU CB C 41.7 0.05 1 176 . 23 LEU HG H 1.82 0.005 1 177 . 23 LEU CG C 27.2 0.05 1 178 . 23 LEU HD1 H 0.97 0.005 2 179 . 23 LEU HD2 H 0.89 0.005 2 180 . 23 LEU CD1 C 25.1 0.05 1 181 . 23 LEU CD2 C 25.1 0.05 1 182 . 24 ALA H H 8.24 0.005 1 183 . 24 ALA HA H 4.15 0.005 1 184 . 24 ALA HB H 1.48 0.005 1 185 . 24 ALA CA C 55.3 0.05 1 186 . 24 ALA CB C 17.5 0.05 1 187 . 25 CYS H H 8.27 0.005 1 188 . 25 CYS HA H 4.12 0.005 1 189 . 25 CYS HB2 H 2.9 0.005 1 190 . 25 CYS HB3 H 3.3 0.005 1 191 . 25 CYS CA C 59.3 0.05 1 192 . 25 CYS CB C 33.8 0.05 1 193 . 26 LEU H H 8.48 0.005 1 194 . 26 LEU HA H 4.36 0.005 1 195 . 26 LEU HB2 H 1.47 0.005 1 196 . 26 LEU HB3 H 1.85 0.005 1 197 . 26 LEU CA C 57.4 0.05 1 198 . 26 LEU CB C 41.8 0.05 1 199 . 26 LEU HG H 1.62 0.005 1 200 . 26 LEU CG C 27.5 0.05 1 201 . 26 LEU HD1 H 0.94 0.005 1 202 . 26 LEU HD2 H 0.76 0.005 1 203 . 26 LEU CD1 C 25.3 0.05 2 204 . 26 LEU CD2 C 23.00 0.05 2 205 . 27 SER H H 7.8 0.005 1 206 . 27 SER HA H 4.43 0.005 1 207 . 27 SER HB2 H 4.01 0.005 1 208 . 27 SER HB3 H 4.01 0.005 1 209 . 27 SER CA C 59.6 0.05 1 210 . 27 SER CB C 63.8 0.05 1 211 . 28 LEU H H 7.37 0.005 1 212 . 28 LEU HA H 4.65 0.005 1 213 . 28 LEU HB2 H 1.72 0.005 2 214 . 28 LEU HB3 H 1.66 0.005 2 215 . 28 LEU CA C 57.3 0.05 1 216 . 28 LEU CB C 43.8 0.05 1 217 . 28 LEU HG H 1.78 0.005 1 218 . 28 LEU CG C 26.4 0.05 1 219 . 28 LEU HD1 H 0.87 0.005 1 220 . 28 LEU HD2 H 0.87 0.005 1 221 . 28 LEU CD1 C 24.3 0.05 2 222 . 28 LEU CD2 C 24.7 0.05 2 223 . 29 CYS H H 7.87 0.005 1 224 . 29 CYS HA H 4.85 0.005 1 225 . 29 CYS HB2 H 3.16 0.005 1 226 . 29 CYS HB3 H 3.43 0.005 1 227 . 29 CYS CA C 56.9 0.05 1 228 . 29 CYS CB C 43.9 0.05 1 229 . 30 HIS H H 8.74 0.005 1 230 . 30 HIS HA H 4.9 0.005 1 231 . 30 HIS HB2 H 2.9 0.005 1 232 . 30 HIS HB3 H 3.1 0.005 1 233 . 30 HIS CB C 30.4 0.05 1 234 . 30 HIS HD2 H 7.05 0.005 1 235 . 30 HIS HE1 H 8.45 0.005 1 236 . 31 ILE H H 8.62 0.005 1 237 . 31 ILE HA H 4.06 0.005 1 238 . 31 ILE HB H 1.82 0.005 1 239 . 31 ILE CA C 62.00 0.05 1 240 . 31 ILE CB C 38.9 0.05 1 241 . 31 ILE HG12 H 1.56 0.005 2 242 . 31 ILE HG13 H 1.15 0.005 2 243 . 31 ILE CG1 C 28.00 0.05 1 244 . 31 ILE HG2 H 0.92 0.005 1 245 . 31 ILE CG2 C 17.5 0.05 1 246 . 31 ILE HD1 H 0.88 0.005 1 247 . 31 ILE CD1 C 13.4 0.05 1 248 . 32 GLU H H 8.51 0.005 1 249 . 32 GLU HA H 4.33 0.005 1 250 . 32 GLU HB2 H 2.05 0.005 2 251 . 32 GLU HB3 H 1.93 0.005 2 252 . 32 GLU CA C 55.9 0.05 1 253 . 32 GLU CB C 29.6 0.05 1 254 . 32 GLU HG2 H 2.32 0.005 1 255 . 32 GLU HG3 H 2.32 0.005 1 256 . 32 GLU CG C 34.9 0.05 1 stop_ save_