data_18 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Stereospecific assignments of side-chain protons and characterization of torsion angles in Eglin c ; _BMRB_accession_number 18 _BMRB_flat_file_name bmr18.str _Entry_type update _Submission_date 1995-07-31 _Accession_date 1996-04-12 _Entry_origination BMRB _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 Hyberts Sven G. . 2 Marki Walter . . 3 Wagner Gerhard . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 223 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2010-06-09 revision BMRB 'Complete natural source information' 2008-09-23 revision BMRB 'Updating non-standard residue' 1999-06-14 revision BMRB 'Converted to BMRB NMR-STAR V 2.1 format' 1996-04-12 revision BMRB 'Error corrected in abrreviations given to non-polymers' 1996-03-25 reformat BMRB 'Converted to the BMRB 1996-03-01 STAR flat-file format' 1995-07-31 original BMRB 'Last release in original BMRB flat-file format' stop_ save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full ; Hyberts, Sven G., Marki, Walter, Wagner, Gerhard, "Stereospecific assignments of side-chain protons and characterization of torsion angles in Eglin c," Eur. J. Biochem. 164, 625-635 (1987). ; _Citation_title ; Stereospecific assignments of side-chain protons and characterization of torsion angles in Eglin c ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID ? loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Hyberts Sven G. . 2 Marki Walter . . 3 Wagner Gerhard . . stop_ _Journal_abbreviation 'Eur. J. Biochem.' _Journal_volume 164 _Journal_issue . _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 625 _Page_last 635 _Year 1987 _Details . save_ ################################## # Molecular system description # ################################## save_system_eglin_c _Saveframe_category molecular_system _Mol_system_name 'eglin c' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'eglin c' $eglin_c stop_ _System_molecular_weight . _System_oligomer_state ? _System_paramagnetic ? _System_thiol_state . _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_eglin_c _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'eglin c' _Molecular_mass . _Mol_thiol_state . _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 70 _Mol_residue_sequence ; XEFGSELKSFPEVVGKTVDQ AREYFTLHYPQYDVYFLPEG SPVTLDLRYNRVRVFYNPGT NVVNHVPHVG ; loop_ _Residue_seq_code _Residue_label 1 THC 2 GLU 3 PHE 4 GLY 5 SER 6 GLU 7 LEU 8 LYS 9 SER 10 PHE 11 PRO 12 GLU 13 VAL 14 VAL 15 GLY 16 LYS 17 THR 18 VAL 19 ASP 20 GLN 21 ALA 22 ARG 23 GLU 24 TYR 25 PHE 26 THR 27 LEU 28 HIS 29 TYR 30 PRO 31 GLN 32 TYR 33 ASP 34 VAL 35 TYR 36 PHE 37 LEU 38 PRO 39 GLU 40 GLY 41 SER 42 PRO 43 VAL 44 THR 45 LEU 46 ASP 47 LEU 48 ARG 49 TYR 50 ASN 51 ARG 52 VAL 53 ARG 54 VAL 55 PHE 56 TYR 57 ASN 58 PRO 59 GLY 60 THR 61 ASN 62 VAL 63 VAL 64 ASN 65 HIS 66 VAL 67 PRO 68 HIS 69 VAL 70 GLY stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-11-04 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 BMRB 289 "eglin c" 98.57 70 100.00 100.00 2.72e-41 PDB 1ACB "Crystal And Molecular Structure Of The Bovine Alpha-Chymotrypsin-Eglin C Complex At 2.0 Angstroms Resolution" 98.57 70 100.00 100.00 2.19e-41 PDB 1CSE "The High-Resolution X-Ray Crystal Structure Of The Complex Formed Between Subtilisin Carlsberg And Eglin C, An Elastase Inhibit" 98.57 70 98.55 100.00 1.05e-40 PDB 1EGL "The Solution Structure Of Eglin C Based On Measurements Of Many Noes And Coupling Constants And Its Comparison With X- Ray Stru" 98.57 70 100.00 100.00 2.19e-41 PDB 1EGP "Proteinase Inhibitor Eglin C With Hydrolysed Reactive Center" 62.86 45 97.73 100.00 3.54e-21 PDB 1MEE "The Complex Between The Subtilisin From A Mesophilic Bacterium And The Leech Inhibitor Eglin-C" 91.43 64 98.44 100.00 9.99e-37 PDB 1SBN "Refined Crystal Structures Of Subtilisin Novo In Complex With Wild-Type And Two Mutant Eglins. Comparison With Other Serine Pro" 98.57 70 97.10 98.55 1.05e-39 PDB 1SIB "Refined Crystal Structures Of Subtilisin Novo In Complex With Wild-Type And Two Mutant Eglins. Comparison With Other Serine Pro" 98.57 70 98.55 100.00 5.64e-41 PDB 1TEC "Crystallographic Refinement By Incorporation Of Molecular Dynamics. The Thermostable Serine Protease Thermitase Complexed With " 98.57 70 100.00 100.00 2.19e-41 PDB 2SEC "Structural Comparison Of Two Serine Proteinase-Protein Inhibitor Complexes. Eglin-C-Subtilisin Carlsberg And Ci-2- Subtilisin N" 98.57 70 98.55 100.00 1.05e-40 PDB 2TEC "Molecular Dynamics Refinement Of A Thermitase-Eglin-C Complex At 1.98 Angstroms Resolution And Comparison Of Two Crystal Forms " 98.57 70 100.00 100.00 2.19e-41 PDB 3TEC "Calcium Binding To Thermitase. Crystallographic Studies Of Thermitase At 0, 5 And 100 Mm Calcium" 98.57 70 100.00 100.00 2.19e-41 PDB 4B1T "Structure Of The Factor Xa-like Trypsin Variant Triple-ala ( Ta) In Complex With Eglin C" 98.57 70 98.55 98.55 1.89e-40 PDB 4B2A "Structure Of The Factor Xa-like Trypsin Variant Triple-ala (tga) In Complex With Eglin C" 94.29 66 98.48 98.48 5.41e-38 PDB 4B2B "Structure Of The Factor Xa-like Trypsin Variant Triple-ala (tgpa) In Complex With Eglin C" 98.57 71 98.55 98.55 2.07e-40 PDB 4B2C "Structure Of The Factor Xa-like Trypsin Variant Triple-ala (tpa) In Complex With Eglin C" 98.57 71 98.55 98.55 2.07e-40 PDB 4H4F "Crystal Structure Of Human Chymotrypsin C (ctrc) Bound To Inhibitor Eglin C From Hirudo Medicinalis" 98.57 70 97.10 97.10 3.99e-40 EMBL CAA25380 "eglin c [synthetic construct]" 98.57 71 100.00 100.00 1.95e-41 PRF 0905140A "eglin c" 98.57 70 100.00 100.00 2.19e-41 SP P01051 "RecName: Full=Eglin C" 98.57 70 100.00 100.00 2.19e-41 stop_ save_ ###################### # Polymer residues # ###################### save_chem_comp_THC _Saveframe_category polymer_residue _Mol_type 'L-PEPTIDE LINKING' _Name_common N-METHYLCARBONYLTHREONINE _BMRB_code THC _PDB_code THC _Standard_residue_derivative . _Molecular_mass 161.156 _Mol_paramagnetic . _Details . loop_ _Atom_name _PDB_atom_name _Atom_type _Atom_chirality _Atom_charge _Atom_oxidation_number _Atom_unpaired_electrons N N N . 0 . ? CN CN C . 0 . ? ON ON O . 0 . ? CM CM C . 0 . ? CA CA C . 0 . ? CB CB C . 0 . ? OG1 OG1 O . 0 . ? CG2 CG2 C . 0 . ? C C C . 0 . ? O O O . 0 . ? OXT OXT O . 0 . ? H H H . 0 . ? HM1 HM1 H . 0 . ? HM2 HM2 H . 0 . ? HM3 HM3 H . 0 . ? HA HA H . 0 . ? HB HB H . 0 . ? HG1 HG1 H . 0 . ? HG21 HG21 H . 0 . ? HG22 HG22 H . 0 . ? HG23 HG23 H . 0 . ? HXT HXT H . 0 . ? stop_ loop_ _Bond_order _Bond_atom_one_atom_name _Bond_atom_two_atom_name _PDB_bond_atom_one_atom_name _PDB_bond_atom_two_atom_name SING N CN ? ? SING N CA ? ? SING N H ? ? DOUB CN ON ? ? SING CN CM ? ? SING CM HM1 ? ? SING CM HM2 ? ? SING CM HM3 ? ? SING CA CB ? ? SING CA C ? ? SING CA HA ? ? SING CB OG1 ? ? SING CB CG2 ? ? SING CB HB ? ? SING OG1 HG1 ? ? SING CG2 HG21 ? ? SING CG2 HG22 ? ? SING CG2 HG23 ? ? DOUB C O ? ? SING C OXT ? ? SING OXT HXT ? ? 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 $eglin_c leech 6421 Eukaryota Metazoa Hirudo medicinalis generic 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 $eglin_c 'not available' . Escherichia coli generic . stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_one _Saveframe_category sample _Sample_type solution _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer unknown _Model unknown _Field_strength 0 _Details 'spectrometer information not available' save_ ############################# # NMR applied experiments # ############################# save__1 _Saveframe_category NMR_applied_experiment _Sample_label $sample_one save_ ####################### # Sample conditions # ####################### save_sample_condition_set_one _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 3 . na temperature 309 . K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chem_shift_reference_par_set_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 _Indirect_shift_ratio_citation_label _Correction_value_citation_label TSP H . . ppm 0 . . . . . $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_chemical_shift_assignment_data_set_one _Saveframe_category assigned_chemical_shifts _Details . loop_ _Sample_label $sample_one stop_ _Sample_conditions_label $sample_condition_set_one _Chem_shift_reference_set_label $chem_shift_reference_par_set_one _Mol_system_component_name 'eglin c' _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 GLU H H 8.32 . 1 2 . 2 GLU HA H 4.3 . 1 3 . 2 GLU HB2 H 1.94 . 1 4 . 2 GLU HB3 H 1.86 . 1 5 . 3 PHE H H 8.17 . 1 6 . 3 PHE HA H 4.62 . 1 7 . 3 PHE HB2 H 3.19 . 1 8 . 3 PHE HB3 H 2.99 . 1 9 . 5 SER H H 8.1 . 1 10 . 5 SER HA H 4.36 . 1 11 . 5 SER HB2 H 3.88 . 1 12 . 5 SER HB3 H 3.81 . 1 13 . 6 GLU H H 8.27 . 1 14 . 6 GLU HA H 4.38 . 1 15 . 6 GLU HB2 H 2 . 2 16 . 6 GLU HB3 H 2.19 . 2 17 . 7 LEU H H 8.07 . 1 18 . 7 LEU HA H 4.42 . 1 19 . 7 LEU HB2 H 1.56 . 2 20 . 7 LEU HB3 H 1.69 . 2 21 . 8 LYS H H 7.89 . 1 22 . 8 LYS HA H 4.12 . 1 23 . 8 LYS HB2 H 1.6 . 2 24 . 8 LYS HB3 H 1.66 . 2 25 . 9 SER H H 7.89 . 1 26 . 9 SER HA H 5.1 . 1 27 . 9 SER HB2 H 3.69 . 2 28 . 9 SER HB3 H 3.71 . 2 29 . 10 PHE H H 7.66 . 1 30 . 10 PHE HA H 5.31 . 1 31 . 10 PHE HB2 H 2.82 . 2 32 . 10 PHE HB3 H 2.97 . 2 33 . 12 GLU H H 9.53 . 1 34 . 12 GLU HA H 4.16 . 1 35 . 12 GLU HB2 H 1.94 . 1 36 . 12 GLU HB3 H 1.78 . 1 37 . 13 VAL H H 7.09 . 1 38 . 13 VAL HA H 3.82 . 1 39 . 13 VAL HB H 2.23 . 1 40 . 13 VAL HG1 H .96 . 1 41 . 13 VAL HG2 H .7 . 1 42 . 14 VAL H H 7.18 . 1 43 . 14 VAL HA H 3.53 . 1 44 . 14 VAL HB H 2.04 . 1 45 . 14 VAL HG1 H .92 . 1 46 . 14 VAL HG2 H .99 . 1 47 . 16 LYS H H 7.84 . 1 48 . 16 LYS HA H 4.63 . 1 49 . 16 LYS HB2 H 2.08 . 1 50 . 16 LYS HB3 H 2.08 . 1 51 . 18 VAL H H 8.07 . 1 52 . 18 VAL HA H 3.1 . 1 53 . 18 VAL HB H 1.5 . 1 54 . 18 VAL HG1 H -.2 . 1 55 . 18 VAL HG2 H .11 . 1 56 . 19 ASP H H 8.39 . 1 57 . 19 ASP HA H 4.18 . 1 58 . 19 ASP HB2 H 2.56 . 2 59 . 19 ASP HB3 H 2.65 . 2 60 . 20 GLN H H 7.7 . 1 61 . 20 GLN HA H 4.12 . 1 62 . 20 GLN HB2 H 2.49 . 1 63 . 20 GLN HB3 H 2.49 . 1 64 . 22 ARG H H 9.06 . 1 65 . 22 ARG HA H 4.24 . 1 66 . 22 ARG HB2 H 1.72 . 2 67 . 22 ARG HB3 H 1.89 . 2 68 . 23 GLU H H 7.59 . 1 69 . 23 GLU HA H 4.15 . 1 70 . 23 GLU HB2 H 2.18 . 2 71 . 23 GLU HB3 H 2.24 . 2 72 . 24 TYR H H 8.11 . 1 73 . 24 TYR HA H 4.19 . 1 74 . 24 TYR HB2 H 3.11 . 1 75 . 24 TYR HB3 H 3.21 . 1 76 . 25 PHE H H 8.62 . 1 77 . 25 PHE HA H 4.12 . 1 78 . 25 PHE HB2 H 3.15 . 2 79 . 25 PHE HB3 H 3.36 . 2 80 . 27 LEU H H 7.74 . 1 81 . 27 LEU HA H 4.06 . 1 82 . 27 LEU HB2 H 1 . 1 83 . 27 LEU HB3 H 1.41 . 1 84 . 28 HIS H H 7.8 . 1 85 . 28 HIS HA H 4.29 . 1 86 . 28 HIS HB2 H 2.36 . 1 87 . 28 HIS HB3 H 2.22 . 1 88 . 29 TYR H H 8.38 . 1 89 . 29 TYR HA H 5.21 . 1 90 . 29 TYR HB2 H 3.57 . 1 91 . 29 TYR HB3 H 2.88 . 1 92 . 31 GLN H H 9.53 . 1 93 . 31 GLN HA H 4.27 . 1 94 . 31 GLN HB2 H 1.98 . 1 95 . 31 GLN HB3 H 1.98 . 1 96 . 32 TYR H H 7.35 . 1 97 . 32 TYR HA H 4.9 . 1 98 . 32 TYR HB2 H 2.54 . 2 99 . 32 TYR HB3 H 2.61 . 2 100 . 33 ASP H H 9.04 . 1 101 . 33 ASP HA H 4.7 . 1 102 . 33 ASP HB2 H 2.73 . 1 103 . 33 ASP HB3 H 2.73 . 1 104 . 34 VAL H H 8.1 . 1 105 . 34 VAL HA H 4.54 . 1 106 . 34 VAL HB H 1.47 . 1 107 . 34 VAL HG1 H -.13 . 1 108 . 34 VAL HG2 H .23 . 1 109 . 35 TYR H H 8.23 . 1 110 . 35 TYR HA H 4.59 . 1 111 . 35 TYR HB2 H 2.34 . 2 112 . 35 TYR HB3 H 2.84 . 2 113 . 36 PHE H H 8.84 . 1 114 . 36 PHE HA H 5.27 . 1 115 . 36 PHE HB2 H 2.78 . 1 116 . 36 PHE HB3 H 2.98 . 1 117 . 37 LEU H H 9.25 . 1 118 . 37 LEU HA H 5.08 . 1 119 . 37 LEU HB2 H 1.15 . 1 120 . 37 LEU HB3 H 1.15 . 1 121 . 39 GLU H H 7.3 . 1 122 . 39 GLU HA H 4.49 . 1 123 . 39 GLU HB2 H 2.25 . 2 124 . 39 GLU HB3 H 1.88 . 2 125 . 41 SER H H 7.72 . 1 126 . 41 SER HA H 4.61 . 1 127 . 41 SER HB2 H 3.86 . 2 128 . 41 SER HB3 H 3.96 . 2 129 . 43 VAL H H 8.07 . 1 130 . 43 VAL HA H 4.57 . 1 131 . 43 VAL HB H 2.11 . 1 132 . 43 VAL HG1 H .84 . 1 133 . 43 VAL HG2 H .95 . 1 134 . 45 LEU H H 8.6 . 1 135 . 45 LEU HA H 4.46 . 1 136 . 45 LEU HB2 H 1.63 . 2 137 . 45 LEU HB3 H 1.7 . 2 138 . 46 ASP H H 8.16 . 1 139 . 46 ASP HA H 4.45 . 1 140 . 46 ASP HB2 H 2.65 . 2 141 . 46 ASP HB3 H 2.74 . 2 142 . 47 LEU H H 8.13 . 1 143 . 47 LEU HA H 4.72 . 1 144 . 47 LEU HB2 H 1.4 . 2 145 . 47 LEU HB3 H 1.42 . 2 146 . 48 ARG H H 8.82 . 1 147 . 48 ARG HA H 4.56 . 1 148 . 48 ARG HB2 H 1.56 . 2 149 . 48 ARG HB3 H 1.82 . 2 150 . 49 TYR H H 8.46 . 1 151 . 49 TYR HA H 4.28 . 1 152 . 49 TYR HB2 H 3.31 . 1 153 . 49 TYR HB3 H 2.85 . 1 154 . 50 ASN H H 7.94 . 1 155 . 50 ASN HA H 4.96 . 1 156 . 50 ASN HB2 H 2.63 . 2 157 . 50 ASN HB3 H 3.25 . 2 158 . 51 ARG H H 7.29 . 1 159 . 51 ARG HA H 5.37 . 1 160 . 51 ARG HB2 H 1.44 . 2 161 . 51 ARG HB3 H 2.28 . 2 162 . 52 VAL H H 8.37 . 1 163 . 52 VAL HA H 4.13 . 1 164 . 52 VAL HB H 1.2 . 1 165 . 52 VAL HG1 H .19 . 1 166 . 52 VAL HG2 H .19 . 1 167 . 53 ARG H H 8.62 . 1 168 . 53 ARG HA H 4.43 . 1 169 . 53 ARG HB2 H 1.49 . 2 170 . 53 ARG HB3 H 1.75 . 2 171 . 54 VAL H H 8.69 . 1 172 . 54 VAL HA H 4.13 . 1 173 . 54 VAL HB H 1.41 . 1 174 . 54 VAL HG1 H .18 . 2 175 . 54 VAL HG2 H .98 . 2 176 . 55 PHE H H 9.21 . 1 177 . 55 PHE HA H 6.08 . 1 178 . 55 PHE HB2 H 2.83 . 2 179 . 55 PHE HB3 H 2.72 . 2 180 . 56 TYR H H 8.13 . 1 181 . 56 TYR HA H 5.55 . 1 182 . 56 TYR HB2 H 2.64 . 1 183 . 56 TYR HB3 H 2.48 . 1 184 . 57 ASN H H 8.6 . 1 185 . 57 ASN HA H 5.01 . 1 186 . 57 ASN HB2 H 2.81 . 2 187 . 57 ASN HB3 H 3.43 . 2 188 . 61 ASN H H 8.89 . 1 189 . 61 ASN HA H 4.35 . 1 190 . 61 ASN HB2 H 3.01 . 2 191 . 61 ASN HB3 H 3.06 . 2 192 . 62 VAL H H 7.41 . 1 193 . 62 VAL HA H 4.4 . 1 194 . 62 VAL HB H 1.88 . 1 195 . 62 VAL HG1 H .75 . 1 196 . 62 VAL HG2 H .86 . 1 197 . 63 VAL H H 8.87 . 1 198 . 63 VAL HA H 4.17 . 1 199 . 63 VAL HB H 2.62 . 1 200 . 63 VAL HG1 H 1.23 . 1 201 . 63 VAL HG2 H .95 . 1 202 . 64 ASN H H 8.91 . 1 203 . 64 ASN HA H 5.01 . 1 204 . 64 ASN HB2 H 2.56 . 2 205 . 64 ASN HB3 H 2.83 . 2 206 . 65 HIS H H 7.77 . 1 207 . 65 HIS HA H 4.92 . 1 208 . 65 HIS HB2 H 3.14 . 2 209 . 65 HIS HB3 H 3.27 . 2 210 . 66 VAL H H 9.17 . 1 211 . 66 VAL HA H 3.79 . 1 212 . 66 VAL HB H 2.21 . 1 213 . 66 VAL HG1 H .92 . 2 214 . 66 VAL HG2 H 1.18 . 2 215 . 68 HIS H H 8.82 . 1 216 . 68 HIS HA H 5.68 . 1 217 . 68 HIS HB2 H 3.17 . 1 218 . 68 HIS HB3 H 3.29 . 1 219 . 69 VAL H H 8.53 . 1 220 . 69 VAL HA H 4.67 . 1 221 . 69 VAL HB H 2.15 . 1 222 . 69 VAL HG1 H 1.18 . 1 223 . 69 VAL HG2 H 1.09 . 1 stop_ save_