data_4182 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Solution Structure of Reduced Clostridium pasteurianum Rubredoxin ; _BMRB_accession_number 4182 _BMRB_flat_file_name bmr4182.str _Entry_type original _Submission_date 1998-08-13 _Accession_date 1998-08-13 _Entry_origination author _NMR_STAR_version 2.1.1 _Experimental_method NMR _Details . loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Bertini Ivano . . 2 Kurtz Donald M. Jr. 3 Eidsness Marly K. . 4 Liu Gaohua . . 5 Luchinat Claudio . . 6 Rosato Antonio . . 7 Scott R. A. . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 261 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2001-08-09 original author . stop_ loop_ _Related_BMRB_accession_number _Relationship 4181 ferredoxin stop_ _Original_release_date 2001-08-09 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title 'Solution Structure of Reduced Clostridium pasteurianum Rubredoxin' _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 Bertini Ivano . . 2 Kurtz Donald M. Jr. 3 Eidsness Marly K. . 4 Liu Gaohua . . 5 Luchinat Claudio . . 6 Rosato Antonio . . 7 Scott Robert A. . stop_ _Journal_abbreviation 'J. Biol. Inorg. Chem.' _Journal_name_full 'Journal of Biological Inorganic Chemistry' _Journal_volume 3 _Journal_issue 4 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 401 _Page_last 410 _Year 1998 _Details . loop_ _Keyword 'nuclear relaxation' paramagnetism rubredoxin 'solution structure' stop_ save_ ################################## # Molecular system description # ################################## save_system_reduced_rubredoxin _Saveframe_category molecular_system _Mol_system_name 'reduced rubredoxin' _Abbreviation_common cprd _Enzyme_commission_number 1.18.1.1 loop_ _Mol_system_component_name _Mol_label cprd $cprd Fe $FE2 stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state monomer _System_paramagnetic yes _System_thiol_state 'other bound and free' _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_cprd _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'reduced rubredoxin' _Abbreviation_common cprd _Molecular_mass . _Mol_thiol_state 'other bound and free' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 54 _Mol_residue_sequence ; MKKYTCTVCGYIYNPEDGDP DNGVNPGTDFKDIPDDWVCP LCGVGKDQFEEVEE ; loop_ _Residue_seq_code _Residue_label 1 MET 2 LYS 3 LYS 4 TYR 5 THR 6 CYS 7 THR 8 VAL 9 CYS 10 GLY 11 TYR 12 ILE 13 TYR 14 ASN 15 PRO 16 GLU 17 ASP 18 GLY 19 ASP 20 PRO 21 ASP 22 ASN 23 GLY 24 VAL 25 ASN 26 PRO 27 GLY 28 THR 29 ASP 30 PHE 31 LYS 32 ASP 33 ILE 34 PRO 35 ASP 36 ASP 37 TRP 38 VAL 39 CYS 40 PRO 41 LEU 42 CYS 43 GLY 44 VAL 45 GLY 46 LYS 47 ASP 48 GLN 49 PHE 50 GLU 51 GLU 52 VAL 53 GLU 54 GLU stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-10-13 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 4050 "rubredoxin peptide" 100.00 54 100.00 100.00 6.32e-30 BMRB 4051 "rubredoxin peptide" 100.00 54 100.00 100.00 6.32e-30 BMRB 4066 rubredoxin 100.00 54 100.00 100.00 6.32e-30 BMRB 4137 rubredoxin 100.00 54 100.00 100.00 6.32e-30 BMRB 4319 "rubredoxin peptide" 100.00 54 100.00 100.00 6.32e-30 BMRB 4320 "rubredoxin peptide" 100.00 54 100.00 100.00 6.32e-30 PDB 1B13 "Clostridium Pasteurianum Rubredoxin G10a Mutant" 100.00 54 98.15 98.15 1.91e-29 PDB 1B2J "Clostridium Pasteurianum Rubredoxin G43a Mutant" 100.00 54 98.15 98.15 1.91e-29 PDB 1BE7 "Clostridium Pasteurianum Rubredoxin C42s Mutant" 100.00 54 98.15 98.15 4.65e-29 PDB 1BFY "Solution Structure Of Reduced Clostridium Pasteurianum Rubredoxin, Nmr, 20 Structures" 98.15 54 100.00 100.00 6.80e-29 PDB 1C09 "Rubredoxin V44a Cp" 100.00 54 98.15 98.15 1.54e-29 PDB 1FHH "X-Ray Crystal Structure Of Oxidized Rubredoxin" 100.00 54 100.00 100.00 6.32e-30 PDB 1FHM "X-Ray Crystal Structure Of Reduced Rubredoxin" 100.00 54 100.00 100.00 6.32e-30 PDB 1IRN "Rubredoxin (zn-substituted) At 1.2 Angstroms Resolution" 100.00 54 100.00 100.00 6.32e-30 PDB 1IRO "Rubredoxin (Oxidized, Fe(Iii)) At 1.1 Angstroms Resolution" 100.00 54 100.00 100.00 6.32e-30 PDB 1R0F "Gallium-Substituted Rubredoxin" 100.00 54 100.00 100.00 6.32e-30 PDB 1R0G "Mercury-Substituted Rubredoxin" 100.00 54 100.00 100.00 6.32e-30 PDB 1R0H "Cobalt-Substituted Rubredoxin" 100.00 54 100.00 100.00 6.32e-30 PDB 1R0I "Cadmium-Substituted Rubredoxin" 100.00 54 100.00 100.00 6.32e-30 PDB 1R0J "Nickel-Substituted Rubredoxin" 100.00 54 100.00 100.00 6.32e-30 PDB 1SMM "Crystal Structure Of Cp Rd L41a Mutant In Oxidized State" 100.00 54 98.15 98.15 3.22e-29 PDB 1SMU "Crystal Structure Of Cp Rd L41a Mutant In Reduced State 1 (Drop-Reduced)" 100.00 54 98.15 98.15 3.22e-29 PDB 1SMW "Crystal Structure Of Cp Rd L41a Mutant In Reduced State 2 (Soaked)" 100.00 54 98.15 98.15 3.22e-29 PDB 1T9O "Crystal Structure Of V44g Cp Rubredoxin" 100.00 54 98.15 98.15 8.01e-29 PDB 1T9Q "Crystal Structure Of V44l Cp Rubredoxin" 100.00 54 98.15 100.00 1.27e-29 PDB 4MBS "Crystal Structure Of The Ccr5 Chemokine Receptor" 100.00 414 100.00 100.00 3.30e-35 PDB 4XNV "The Human P2y1 Receptor In Complex With Bptu" 100.00 421 100.00 100.00 4.50e-35 PDB 4XNW "The Human P2y1 Receptor In Complex With Mrs2500" 100.00 421 100.00 100.00 4.50e-35 GB AAA23279 "rubredoxin [Clostridium pasteurianum]" 100.00 54 100.00 100.00 6.32e-30 GB AJA49845 "rubredoxin [Clostridium pasteurianum DSM 525 = ATCC 6013]" 100.00 54 100.00 100.00 6.32e-30 GB AJA53833 "rubredoxin [Clostridium pasteurianum DSM 525 = ATCC 6013]" 100.00 54 100.00 100.00 6.32e-30 GB ELP57804 "Rubredoxin [Clostridium pasteurianum DSM 525 = ATCC 6013]" 100.00 54 100.00 100.00 6.32e-30 GB KER11884 "Rubredoxin domain containing protein [Clostridium pasteurianum DSM 525 = ATCC 6013]" 100.00 54 100.00 100.00 6.32e-30 REF WP_003447684 "rubredoxin [Clostridium pasteurianum]" 100.00 54 100.00 100.00 6.32e-30 SP P00268 "RecName: Full=Rubredoxin; Short=Rd" 100.00 54 100.00 100.00 6.32e-30 stop_ save_ ############# # Ligands # ############# save_FE2 _Saveframe_category ligand _Mol_type non-polymer _Name_common "FE2 (FE (II) ION)" _BMRB_code . _PDB_code FE2 _Molecular_mass 55.845 _Mol_charge 2 _Mol_paramagnetic . _Mol_aromatic no _Details ; Information obtained from PDB's Chemical Component Dictionary at http://wwpdb-remediation.rutgers.edu/downloads.html Downloaded on Wed Jul 13 13:51:02 2011 ; loop_ _Atom_name _PDB_atom_name _Atom_type _Atom_chirality _Atom_charge _Atom_oxidation_number _Atom_unpaired_electrons FE FE FE . 2 . ? stop_ _Mol_thiol_state . _Sequence_homology_query_date . save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $cprd 'clostridium pasteurianum' 1501 Eubacteria . clostridium pasteurianum 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 $cprd . . . . . . 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 _Concentration_min_value _Concentration_max_value _Isotopic_labeling $cprd . mM 3.5 4 . stop_ save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer_one _Saveframe_category NMR_spectrometer _Manufacturer Brucker _Model Avance _Field_strength 800 _Details . save_ save_NMR_spectrometer_two _Saveframe_category NMR_spectrometer _Manufacturer Brucker _Model AMX _Field_strength 600 _Details . save_ ############################# # NMR applied experiments # ############################# save_NOESY_1 _Saveframe_category NMR_applied_experiment _Experiment_name NOESY _Sample_label $sample_one save_ save_TOCSY_2 _Saveframe_category NMR_applied_experiment _Experiment_name TOCSY _Sample_label $sample_one save_ save_DQF-COSY_3 _Saveframe_category NMR_applied_experiment _Experiment_name DQF-COSY _Sample_label $sample_one save_ save_IR-NOESY_4 _Saveframe_category NMR_applied_experiment _Experiment_name IR-NOESY _Sample_label $sample_one save_ ####################### # Sample conditions # ####################### save_sample_conditions_one _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units 'ionic strength' 0.1 . M pH 6.8 0.1 n/a temperature 298 0.1 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 _Indirect_shift_ratio_citation_label _Correction_value_citation_label H2O H 1 proton ppm 4.81 internal direct . . . $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_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 cprd _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 HA H 4.224 . . 2 . 1 MET HB3 H 2.335 . . 3 . 1 MET HB2 H 2.085 . . 4 . 1 MET HG2 H 2.785 . . 5 . 1 MET HG3 H 2.677 . . 6 . 2 LYS H H 9.122 . . 7 . 2 LYS HA H 4.545 . . 8 . 2 LYS HB2 H 1.932 . . 9 . 2 LYS HB3 H 1.932 . . 10 . 2 LYS HG3 H 1.649 . . 11 . 2 LYS HG2 H 1.548 . . 12 . 2 LYS HD2 H 1.751 . . 13 . 2 LYS HD3 H 1.751 . . 14 . 2 LYS HE2 H 3.093 . . 15 . 2 LYS HE3 H 3.093 . . 16 . 3 LYS H H 8.801 . . 17 . 3 LYS HA H 4.964 . . 18 . 3 LYS HB2 H 1.665 . . 19 . 3 LYS HG3 H 1.748 . . 20 . 3 LYS HG2 H 1.405 . . 21 . 3 LYS HB3 H 1.825 . . 22 . 3 LYS HD2 H 1.651 . . 23 . 3 LYS HD3 H 1.651 . . 24 . 3 LYS HE2 H 2.896 . . 25 . 3 LYS HE3 H 2.896 . . 26 . 4 TYR H H 8.521 . . 27 . 4 TYR HA H 5.506 . . 28 . 4 TYR HB3 H 2.809 . . 29 . 4 TYR HB2 H 2.606 . . 30 . 4 TYR HD1 H 6.737 . . 31 . 4 TYR HD2 H 6.737 . . 32 . 4 TYR HE1 H 6.850 . . 33 . 4 TYR HE2 H 6.850 . . 34 . 5 THR H H 10.418 . . 35 . 5 THR HB H 3.118 . . 36 . 5 THR HG2 H 2.421 . . 37 . 11 TYR HB2 H 3.224 . . 38 . 11 TYR HB3 H 3.224 . . 39 . 11 TYR HE1 H 6.925 . . 40 . 11 TYR HD1 H 7.213 . . 41 . 11 TYR HE2 H 6.925 . . 42 . 11 TYR HD2 H 7.213 . . 43 . 12 ILE HA H 4.557 . . 44 . 12 ILE HB H 1.076 . . 45 . 12 ILE HG2 H 0.586 . . 46 . 12 ILE HG12 H 0.920 . . 47 . 12 ILE HG13 H 0.920 . . 48 . 12 ILE HD1 H 0.384 . . 49 . 13 TYR H H 9.440 . . 50 . 13 TYR HA H 4.023 . . 51 . 13 TYR HB2 H 3.077 . . 52 . 13 TYR HB3 H 3.077 . . 53 . 13 TYR HD1 H 7.064 . . 54 . 13 TYR HE1 H 6.372 . . 55 . 13 TYR HD2 H 7.064 . . 56 . 13 TYR HE2 H 6.372 . . 57 . 13 TYR HH H 9.084 . . 58 . 14 ASN H H 8.211 . . 59 . 14 ASN HA H 5.002 . . 60 . 14 ASN HB3 H 2.842 . . 61 . 14 ASN HB2 H 2.315 . . 62 . 14 ASN HD21 H 7.339 . . 63 . 14 ASN HD22 H 7.071 . . 64 . 15 PRO HA H 4.023 . . 65 . 15 PRO HB3 H 2.596 . . 66 . 15 PRO HB2 H 1.927 . . 67 . 15 PRO HG3 H 2.179 . . 68 . 15 PRO HG2 H 1.982 . . 69 . 15 PRO HD3 H 3.971 . . 70 . 15 PRO HD2 H 3.929 . . 71 . 16 GLU H H 7.532 . . 72 . 16 GLU HA H 3.808 . . 73 . 16 GLU HB3 H 1.845 . . 74 . 16 GLU HB2 H 1.747 . . 75 . 16 GLU HG3 H 2.248 . . 76 . 16 GLU HG2 H 2.173 . . 77 . 17 ASP H H 7.086 . . 78 . 17 ASP HA H 4.566 . . 79 . 17 ASP HB3 H 2.544 . . 80 . 17 ASP HB2 H 2.446 . . 81 . 18 GLY H H 7.884 . . 82 . 18 GLY HA2 H 3.943 . . 83 . 18 GLY HA3 H 3.506 . . 84 . 19 ASP H H 8.507 . . 85 . 19 ASP HA H 4.998 . . 86 . 19 ASP HB2 H 2.893 . . 87 . 19 ASP HB3 H 2.893 . . 88 . 20 PRO HA H 4.116 . . 89 . 20 PRO HB3 H 2.327 . . 90 . 20 PRO HB2 H 2.126 . . 91 . 20 PRO HG2 H 2.031 . . 92 . 20 PRO HG3 H 2.031 . . 93 . 20 PRO HD2 H 3.814 . . 94 . 20 PRO HD3 H 3.768 . . 95 . 21 ASP H H 9.315 . . 96 . 21 ASP HA H 4.491 . . 97 . 21 ASP HB3 H 2.750 . . 98 . 21 ASP HB2 H 2.651 . . 99 . 22 ASN H H 7.769 . . 100 . 22 ASN HA H 5.317 . . 101 . 22 ASN HB3 H 3.321 . . 102 . 22 ASN HB2 H 3.173 . . 103 . 22 ASN HD22 H 7.277 . . 104 . 22 ASN HD21 H 9.428 . . 105 . 23 GLY H H 7.696 . . 106 . 23 GLY HA3 H 4.254 . . 107 . 23 GLY HA2 H 3.913 . . 108 . 24 VAL H H 7.510 . . 109 . 24 VAL HA H 4.230 . . 110 . 24 VAL HB H 1.924 . . 111 . 24 VAL HG1 H 0.813 . . 112 . 24 VAL HG2 H 0.754 . . 113 . 25 ASN H H 8.873 . . 114 . 25 ASN HA H 4.783 . . 115 . 25 ASN HB3 H 2.762 . . 116 . 25 ASN HB2 H 2.458 . . 117 . 25 ASN HD22 H 7.028 . . 118 . 25 ASN HD21 H 7.693 . . 119 . 26 PRO HA H 3.682 . . 120 . 26 PRO HB3 H 2.407 . . 121 . 26 PRO HB2 H 1.757 . . 122 . 26 PRO HG2 H 2.095 . . 123 . 26 PRO HG3 H 1.976 . . 124 . 26 PRO HD2 H 3.616 . . 125 . 26 PRO HD3 H 3.616 . . 126 . 27 GLY H H 8.659 . . 127 . 27 GLY HA3 H 4.160 . . 128 . 27 GLY HA2 H 3.439 . . 129 . 28 THR H H 7.041 . . 130 . 28 THR HA H 4.193 . . 131 . 28 THR HB H 3.800 . . 132 . 28 THR HG2 H 1.075 . . 133 . 28 THR HG1 H 6.506 . . 134 . 29 ASP H H 9.437 . . 135 . 29 ASP HA H 4.623 . . 136 . 29 ASP HB2 H 2.714 . . 137 . 29 ASP HB3 H 2.668 . . 138 . 30 PHE H H 9.566 . . 139 . 30 PHE HA H 3.322 . . 140 . 30 PHE HB2 H 2.786 . . 141 . 30 PHE HB3 H 2.296 . . 142 . 30 PHE HZ H 6.925 . . 143 . 30 PHE HE1 H 6.622 . . 144 . 30 PHE HE2 H 6.622 . . 145 . 30 PHE HD1 H 6.055 . . 146 . 30 PHE HD2 H 6.055 . . 147 . 31 LYS H H 8.997 . . 148 . 31 LYS HA H 3.860 . . 149 . 31 LYS HB2 H 1.832 . . 150 . 31 LYS HB3 H 1.832 . . 151 . 31 LYS HG3 H 1.449 . . 152 . 31 LYS HG2 H 1.386 . . 153 . 31 LYS HD2 H 1.754 . . 154 . 31 LYS HD3 H 1.754 . . 155 . 31 LYS HE2 H 3.082 . . 156 . 31 LYS HE3 H 3.082 . . 157 . 32 ASP H H 7.760 . . 158 . 32 ASP HA H 4.615 . . 159 . 32 ASP HB3 H 2.801 . . 160 . 32 ASP HB2 H 2.533 . . 161 . 33 ILE H H 6.917 . . 162 . 33 ILE HA H 3.669 . . 163 . 33 ILE HB H 0.695 . . 164 . 33 ILE HG2 H 0.384 . . 165 . 33 ILE HG13 H 1.064 . . 166 . 33 ILE HG12 H 0.150 . . 167 . 34 PRO HA H 4.383 . . 168 . 34 PRO HB3 H 2.515 . . 169 . 34 PRO HB2 H 2.201 . . 170 . 34 PRO HG2 H 2.242 . . 171 . 34 PRO HG3 H 2.062 . . 172 . 34 PRO HD3 H 3.880 . . 173 . 34 PRO HD2 H 3.436 . . 174 . 35 ASP H H 8.450 . . 175 . 35 ASP HA H 4.321 . . 176 . 35 ASP HB3 H 2.776 . . 177 . 35 ASP HB2 H 2.663 . . 178 . 36 ASP H H 8.371 . . 179 . 36 ASP HA H 4.740 . . 180 . 36 ASP HB2 H 3.043 . . 181 . 36 ASP HB3 H 2.761 . . 182 . 37 TRP H H 7.885 . . 183 . 37 TRP HA H 4.662 . . 184 . 37 TRP HB2 H 3.257 . . 185 . 37 TRP HB3 H 3.207 . . 186 . 37 TRP HD1 H 7.428 . . 187 . 37 TRP HE3 H 7.176 . . 188 . 37 TRP HE1 H 11.811 . . 189 . 37 TRP HZ3 H 6.932 . . 190 . 37 TRP HZ2 H 7.350 . . 191 . 37 TRP HH2 H 7.068 . . 192 . 38 VAL H H 7.217 . . 193 . 38 VAL HA H 4.496 . . 194 . 38 VAL HB H 1.963 . . 195 . 40 PRO HB2 H 2.039 . . 196 . 40 PRO HB3 H 1.964 . . 197 . 40 PRO HG2 H 1.295 . . 198 . 40 PRO HD2 H 3.485 . . 199 . 40 PRO HD3 H 3.485 . . 200 . 41 LEU HG H 1.743 . . 201 . 41 LEU HD1 H 0.940 . . 202 . 41 LEU HD2 H 1.125 . . 203 . 43 GLY H H 8.047 . . 204 . 43 GLY HA2 H 4.388 . . 205 . 45 GLY H H 6.946 . . 206 . 45 GLY HA2 H 4.415 . . 207 . 45 GLY HA3 H 3.615 . . 208 . 46 LYS H H 8.424 . . 209 . 46 LYS HA H 4.137 . . 210 . 46 LYS HB2 H 1.903 . . 211 . 46 LYS HB3 H 1.903 . . 212 . 46 LYS HG2 H 1.188 . . 213 . 46 LYS HG3 H 1.188 . . 214 . 46 LYS HD2 H 1.449 . . 215 . 46 LYS HD3 H 1.336 . . 216 . 46 LYS HE2 H 2.319 . . 217 . 46 LYS HE3 H 1.672 . . 218 . 46 LYS HZ H 7.001 . . 219 . 47 ASP H H 8.545 . . 220 . 47 ASP HA H 4.388 . . 221 . 47 ASP HB2 H 2.525 . . 222 . 47 ASP HB3 H 2.525 . . 223 . 48 GLN H H 7.228 . . 224 . 48 GLN HA H 3.891 . . 225 . 49 PHE HA H 6.517 . . 226 . 49 PHE HB3 H 4.049 . . 227 . 49 PHE HB2 H 3.121 . . 228 . 49 PHE HE1 H 7.155 . . 229 . 49 PHE HZ H 7.403 . . 230 . 49 PHE HE2 H 7.150 . . 231 . 49 PHE HD1 H 6.870 . . 232 . 49 PHE HD2 H 6.870 . . 233 . 50 GLU H H 10.076 . . 234 . 50 GLU HA H 5.184 . . 235 . 50 GLU HB3 H 2.392 . . 236 . 50 GLU HB2 H 2.339 . . 237 . 50 GLU HG2 H 2.750 . . 238 . 50 GLU HG3 H 2.630 . . 239 . 51 GLU H H 9.044 . . 240 . 51 GLU HA H 3.489 . . 241 . 51 GLU HB2 H 1.814 . . 242 . 51 GLU HB3 H 1.814 . . 243 . 51 GLU HG3 H 2.039 . . 244 . 51 GLU HG2 H 1.942 . . 245 . 52 VAL H H 8.482 . . 246 . 52 VAL HA H 4.239 . . 247 . 52 VAL HB H 2.064 . . 248 . 52 VAL HG2 H 1.118 . . 249 . 52 VAL HG1 H 1.077 . . 250 . 53 GLU H H 8.785 . . 251 . 53 GLU HA H 4.473 . . 252 . 53 GLU HB2 H 2.183 . . 253 . 53 GLU HB3 H 2.058 . . 254 . 53 GLU HG3 H 2.457 . . 255 . 53 GLU HG2 H 2.390 . . 256 . 54 GLU H H 8.140 . . 257 . 54 GLU HA H 4.262 . . 258 . 54 GLU HB2 H 1.961 . . 259 . 54 GLU HB3 H 1.961 . . 260 . 54 GLU HG2 H 2.276 . . 261 . 54 GLU HG3 H 2.120 . . stop_ save_