data_4602 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Solution Structure of Oxidized Microsomal Rabbit Cytochrome b5. Factors Determining the Heterogeneous Binding of the Heme ; _BMRB_accession_number 4602 _BMRB_flat_file_name bmr4602.str _Entry_type original _Submission_date 2000-05-05 _Accession_date 2000-09-07 _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 Banci L. . . 2 Bertini I. . . 3 Rosato A. . . 4 Scacchieri S. . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 464 "15N chemical shifts" 70 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2000-12-06 original author . stop_ _Original_release_date 2000-12-06 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; Solution structure of oxidized microsomal rabbit cytochrome b5. Factors determining the heterogeneous binding of the heme ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code 20117684 _PubMed_ID 10651812 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Banci L. . . 2 Bertini I. . . 3 Rosato A. . . 4 Scacchieri S. . . stop_ _Journal_abbreviation 'Eur. J. Biochem.' _Journal_volume 267 _Journal_issue . _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 755 _Page_last 766 _Year 2000 _Details . loop_ _Keyword CYTOCHROME HEME stop_ save_ ####################################### # Cited references within the entry # ####################################### save_ref_1 _Saveframe_category citation _Citation_full ; Guntert P, Mumenthaler C, Wuthrich K. Torsion angle dynamics for NMR structure calculation with the new program DYANA. J Mol Biol. 1997 Oct 17;273(1):283-98. ; _Citation_title 'Torsion angle dynamics for NMR structure calculation with the new program DYANA.' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 9367762 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Guentert P . . 2 Mumenthaler C . . 3 Wuethrich K . . stop_ _Journal_abbreviation 'J. Mol. Biol.' _Journal_name_full 'Journal of molecular biology' _Journal_volume 273 _Journal_issue 1 _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 283 _Page_last 298 _Year 1997 _Details ; The new program DYANA (DYnamics Algorithm for Nmr Applications) for efficient calculation of three-dimensional protein and nucleic acid structures from distance constraints and torsion angle constraints collected by nuclear magnetic resonance (NMR) experiments performs simulated annealing by molecular dynamics in torsion angle space and uses a fast recursive algorithm to integrate the equations of motions. Torsion angle dynamics can be more efficient than molecular dynamics in Cartesian coordinate space because of the reduced number of degrees of freedom and the concomitant absence of high-frequency bond and angle vibrations, which allows for the use of longer time-steps and/or higher temperatures in the structure calculation. It also represents a significant advance over the variable target function method in torsion angle space with the REDAC strategy used by the predecessor program DIANA. DYANA computation times per accepted conformer in the "bundle" used to represent the NMR structure compare favorably with those of other presently available structure calculation algorithms, and are of the order of 160 seconds for a protein of 165 amino acid residues when using a DEC Alpha 8400 5/300 computer. Test calculations starting from conformers with random torsion angle values further showed that DYANA is capable of efficient calculation of high-quality protein structures with up to 400 amino acid residues, and of nucleic acid structures. ; save_ ################################## # Molecular system description # ################################## save_system_Cyt_B5 _Saveframe_category molecular_system _Mol_system_name 'CYTOCHROME B5' _Abbreviation_common 'CYTOCHROME B5' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'CYTOCHROME B5' $Cyt_B5 heme $HEM stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state monomer _System_paramagnetic yes _System_thiol_state 'not present' _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_Cyt_B5 _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'CYTOCHROME B5' _Molecular_mass . _Mol_thiol_state 'not present' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 94 _Mol_residue_sequence ; DKDVKYYTLEEIKKHNHSKS TWLILHHKVYDLTKFLEEHP GGEEVLREQAGGDATENFED VGHSTDARELSKTFIIGELH PDDRSKLSKPMETL ; loop_ _Residue_seq_code _Residue_label 1 ASP 2 LYS 3 ASP 4 VAL 5 LYS 6 TYR 7 TYR 8 THR 9 LEU 10 GLU 11 GLU 12 ILE 13 LYS 14 LYS 15 HIS 16 ASN 17 HIS 18 SER 19 LYS 20 SER 21 THR 22 TRP 23 LEU 24 ILE 25 LEU 26 HIS 27 HIS 28 LYS 29 VAL 30 TYR 31 ASP 32 LEU 33 THR 34 LYS 35 PHE 36 LEU 37 GLU 38 GLU 39 HIS 40 PRO 41 GLY 42 GLY 43 GLU 44 GLU 45 VAL 46 LEU 47 ARG 48 GLU 49 GLN 50 ALA 51 GLY 52 GLY 53 ASP 54 ALA 55 THR 56 GLU 57 ASN 58 PHE 59 GLU 60 ASP 61 VAL 62 GLY 63 HIS 64 SER 65 THR 66 ASP 67 ALA 68 ARG 69 GLU 70 LEU 71 SER 72 LYS 73 THR 74 PHE 75 ILE 76 ILE 77 GLY 78 GLU 79 LEU 80 HIS 81 PRO 82 ASP 83 ASP 84 ARG 85 SER 86 LYS 87 LEU 88 SER 89 LYS 90 PRO 91 MET 92 GLU 93 THR 94 LEU stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-08-11 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 18919 Full-length_cytochrome_b5 100.00 134 100.00 100.00 4.95e-61 BMRB 295 "cytochrome b5" 87.23 82 97.56 100.00 5.28e-51 PDB 1DO9 "Solution Structure Of Oxidized Microsomal Rabbit Cytochrome B5. Factors Determining The Heterogeneous Binding Of The Heme" 100.00 94 100.00 100.00 2.09e-60 PDB 2M33 "Solution Nmr Structure Of Full-length Oxidized Microsomal Rabbit Cytochrome B5" 100.00 104 100.00 100.00 7.32e-61 DBJ BAA01712 "soluble cytochrome b5 [Oryctolagus cuniculus]" 97.87 98 100.00 100.00 2.60e-59 GB AAB03878 "cytochrome b-5 [Oryctolagus cuniculus]" 100.00 134 100.00 100.00 4.95e-61 GB AAB32285 "peditoxin, pedin=cytochrome b-like heme protein [Toxopneustes pileolus=sea urchins, Lamarck, Peptide, 82 aa]" 86.17 82 98.77 100.00 1.69e-50 PRF 1205244A "cytochrome b5" 91.49 90 97.67 98.84 5.17e-53 PRF 1908210A "cytochrome b5" 100.00 134 100.00 100.00 4.95e-61 REF NP_001164734 "soluble cytochrome b5 [Oryctolagus cuniculus]" 97.87 98 100.00 100.00 2.60e-59 REF NP_001164735 "cytochrome b5 [Oryctolagus cuniculus]" 100.00 134 100.00 100.00 4.95e-61 SP P00169 "RecName: Full=Cytochrome b5" 100.00 134 100.00 100.00 4.95e-61 stop_ save_ ############# # Ligands # ############# save_HEM _Saveframe_category ligand _Mol_type non-polymer _Name_common "HEM (PROTOPORPHYRIN IX CONTAINING FE)" _BMRB_code . _PDB_code HEM _Molecular_mass 616.487 _Mol_charge 0 _Mol_paramagnetic . _Mol_aromatic yes _Details ; Information obtained from PDB's Chemical Component Dictionary at http://wwpdb-remediation.rutgers.edu/downloads.html Downloaded on Fri Jul 15 14:00:24 2011 ; loop_ _Atom_name _PDB_atom_name _Atom_type _Atom_chirality _Atom_charge _Atom_oxidation_number _Atom_unpaired_electrons CHA CHA C . 0 . ? CHB CHB C . 0 . ? CHC CHC C . 0 . ? CHD CHD C . 0 . ? C1A C1A C . 0 . ? C2A C2A C . 0 . ? C3A C3A C . 0 . ? C4A C4A C . 0 . ? CMA CMA C . 0 . ? CAA CAA C . 0 . ? CBA CBA C . 0 . ? CGA CGA C . 0 . ? O1A O1A O . 0 . ? O2A O2A O . 0 . ? C1B C1B C . 0 . ? C2B C2B C . 0 . ? C3B C3B C . 0 . ? C4B C4B C . 0 . ? CMB CMB C . 0 . ? CAB CAB C . 0 . ? CBB CBB C . 0 . ? C1C C1C C . 0 . ? C2C C2C C . 0 . ? C3C C3C C . 0 . ? C4C C4C C . 0 . ? CMC CMC C . 0 . ? CAC CAC C . 0 . ? CBC CBC C . 0 . ? C1D C1D C . 0 . ? C2D C2D C . 0 . ? C3D C3D C . 0 . ? C4D C4D C . 0 . ? CMD CMD C . 0 . ? CAD CAD C . 0 . ? CBD CBD C . 0 . ? CGD CGD C . 0 . ? O1D O1D O . 0 . ? O2D O2D O . 0 . ? NA NA N . 0 . ? NB NB N . 0 . ? NC NC N . 0 . ? ND ND N . 0 . ? FE FE FE . 0 . ? HHB HHB H . 0 . ? HHC HHC H . 0 . ? HHD HHD H . 0 . ? HMA HMA H . 0 . ? HMAA HMAA H . 0 . ? HMAB HMAB H . 0 . ? HAA HAA H . 0 . ? HAAA HAAA H . 0 . ? HBA HBA H . 0 . ? HBAA HBAA H . 0 . ? HMB HMB H . 0 . ? HMBA HMBA H . 0 . ? HMBB HMBB H . 0 . ? HAB HAB H . 0 . ? HBB HBB H . 0 . ? HBBA HBBA H . 0 . ? HMC HMC H . 0 . ? HMCA HMCA H . 0 . ? HMCB HMCB H . 0 . ? HAC HAC H . 0 . ? HBC HBC H . 0 . ? HBCA HBCA H . 0 . ? HMD HMD H . 0 . ? HMDA HMDA H . 0 . ? HMDB HMDB H . 0 . ? HAD HAD H . 0 . ? HADA HADA H . 0 . ? HBD HBD H . 0 . ? HBDA HBDA H . 0 . ? H2A H2A H . 0 . ? H2D H2D H . 0 . ? HHA HHA 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 CHA C1A ? ? DOUB CHA C4D ? ? SING CHA HHA ? ? SING CHB C4A ? ? DOUB CHB C1B ? ? SING CHB HHB ? ? SING CHC C4B ? ? DOUB CHC C1C ? ? SING CHC HHC ? ? DOUB CHD C4C ? ? SING CHD C1D ? ? SING CHD HHD ? ? DOUB C1A C2A ? ? SING C1A NA ? ? SING C2A C3A ? ? SING C2A CAA ? ? DOUB C3A C4A ? ? SING C3A CMA ? ? SING C4A NA ? ? SING CMA HMA ? ? SING CMA HMAA ? ? SING CMA HMAB ? ? SING CAA CBA ? ? SING CAA HAA ? ? SING CAA HAAA ? ? SING CBA CGA ? ? SING CBA HBA ? ? SING CBA HBAA ? ? DOUB CGA O1A ? ? SING CGA O2A ? ? SING C1B C2B ? ? SING C1B NB ? ? DOUB C2B C3B ? ? SING C2B CMB ? ? SING C3B C4B ? ? SING C3B CAB ? ? DOUB C4B NB ? ? SING CMB HMB ? ? SING CMB HMBA ? ? SING CMB HMBB ? ? DOUB CAB CBB ? ? SING CAB HAB ? ? SING CBB HBB ? ? SING CBB HBBA ? ? SING C1C C2C ? ? SING C1C NC ? ? DOUB C2C C3C ? ? SING C2C CMC ? ? SING C3C C4C ? ? SING C3C CAC ? ? SING C4C NC ? ? SING CMC HMC ? ? SING CMC HMCA ? ? SING CMC HMCB ? ? DOUB CAC CBC ? ? SING CAC HAC ? ? SING CBC HBC ? ? SING CBC HBCA ? ? SING C1D C2D ? ? DOUB C1D ND ? ? DOUB C2D C3D ? ? SING C2D CMD ? ? SING C3D C4D ? ? SING C3D CAD ? ? SING C4D ND ? ? SING CMD HMD ? ? SING CMD HMDA ? ? SING CMD HMDB ? ? SING CAD CBD ? ? SING CAD HAD ? ? SING CAD HADA ? ? SING CBD CGD ? ? SING CBD HBD ? ? SING CBD HBDA ? ? DOUB CGD O1D ? ? SING CGD O2D ? ? SING O2A H2A ? ? SING O2D H2D ? ? SING FE NA ? ? SING FE NB ? ? SING FE NC ? ? SING FE ND ? ? 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 $Cyt_B5 'European Rabbit' 9986 Eukaryota Metazoa Oryctolagus cuniculus 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 $Cyt_B5 'recombinant technology' 'E. coli' Escherichia coli . pKK223 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 $Cyt_B5 . mM 2 3 [U-15N] 'phosphate buffer' 1 mM . . . stop_ save_ ############################ # Computer software used # ############################ save_DYANA _Saveframe_category software _Name DYANA _Version '1.5 MODIFIED FOR USING PSEUDOCONTACT SHIFTS AS CONSTRAINTS' loop_ _Task 'STRUCTURE SOLUTION' stop_ _Details . _Citation_label $ref_1 save_ save_AMBER _Saveframe_category software _Name AMBER _Version 4.0 loop_ _Task REFINEMENT stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model Avance _Field_strength 800 _Details . save_ ############################# # NMR applied experiments # ############################# save_2D_NOESY_1 _Saveframe_category NMR_applied_experiment _Experiment_name '2D NOESY' _Sample_label $sample_1 save_ save_3D_15N-SEPARATED_NOESY_2 _Saveframe_category NMR_applied_experiment _Experiment_name '3D 15N-SEPARATED_NOESY' _Sample_label $sample_1 save_ save_2D_TOCSY_3 _Saveframe_category NMR_applied_experiment _Experiment_name '2D TOCSY' _Sample_label $sample_1 save_ save_3D_15N-SEPARATED_TOCSY_4 _Saveframe_category NMR_applied_experiment _Experiment_name '3D 15N-SEPARATED_TOCSY' _Sample_label $sample_1 save_ ####################### # Sample conditions # ####################### save_sample_cond_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 7 . pH temperature 298 . K pressure 1 . atm stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_ref_1 _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 . H 1 . . . . . . . . . N 15 . . . . . . . . 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_set_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_ref_1 _Mol_system_component_name 'CYTOCHROME B5' _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 LYS H H 8.17 . 1 2 . 2 LYS HA H 4.45 . 1 3 . 2 LYS HB2 H 2.45 . 1 4 . 2 LYS HB3 H 2.45 . 1 5 . 3 ASP HA H 4.49 . 1 6 . 4 VAL N N 129.3 . 1 7 . 4 VAL H H 7.65 . 1 8 . 4 VAL HA H 3.70 . 1 9 . 4 VAL HB H 1.54 . 1 10 . 4 VAL HG1 H 0.63 . 2 11 . 4 VAL HG2 H 0.26 . 2 12 . 5 LYS N N 134.3 . 1 13 . 5 LYS H H 8.09 . 1 14 . 5 LYS HA H 4.03 . 1 15 . 5 LYS HB2 H 1.53 . 1 16 . 5 LYS HB3 H 1.53 . 1 17 . 5 LYS HG2 H 1.04 . 2 18 . 5 LYS HG3 H 1.15 . 2 19 . 5 LYS HE2 H 2.87 . 1 20 . 5 LYS HE3 H 2.87 . 1 21 . 6 TYR N N 128.9 . 1 22 . 6 TYR H H 8.11 . 1 23 . 6 TYR HA H 5.62 . 1 24 . 6 TYR HB2 H 2.57 . 2 25 . 6 TYR HB3 H 2.78 . 2 26 . 6 TYR HD1 H 6.78 . 1 27 . 6 TYR HD2 H 6.78 . 1 28 . 6 TYR HE1 H 6.55 . 1 29 . 6 TYR HE2 H 6.55 . 1 30 . 7 TYR N N 125.4 . 1 31 . 7 TYR H H 8.58 . 1 32 . 7 TYR HA H 5.11 . 1 33 . 7 TYR HB2 H 3.09 . 2 34 . 7 TYR HB3 H 2.36 . 2 35 . 7 TYR HD1 H 6.81 . 1 36 . 7 TYR HD2 H 6.81 . 1 37 . 7 TYR HE1 H 6.45 . 1 38 . 7 TYR HE2 H 6.45 . 1 39 . 8 THR N N 122.4 . 1 40 . 8 THR H H 9.13 . 1 41 . 8 THR HA H 4.52 . 1 42 . 8 THR HB H 4.80 . 1 43 . 8 THR HG2 H 1.15 . 1 44 . 9 LEU N N 130.8 . 1 45 . 9 LEU H H 9.67 . 1 46 . 9 LEU HA H 3.93 . 1 47 . 9 LEU HB2 H 1.60 . 1 48 . 9 LEU HB3 H 1.60 . 1 49 . 9 LEU HG H 1.53 . 1 50 . 9 LEU HD1 H 0.99 . 2 51 . 9 LEU HD2 H 0.87 . 2 52 . 10 GLU N N 123.7 . 1 53 . 10 GLU H H 8.32 . 1 54 . 10 GLU HA H 3.78 . 1 55 . 10 GLU HB2 H 1.95 . 2 56 . 10 GLU HB3 H 1.79 . 2 57 . 10 GLU HG2 H 2.25 . 2 58 . 10 GLU HG3 H 2.16 . 2 59 . 11 GLU N N 125.7 . 1 60 . 11 GLU H H 7.66 . 1 61 . 11 GLU HA H 4.04 . 1 62 . 11 GLU HB2 H 2.36 . 2 63 . 11 GLU HB3 H 2.23 . 2 64 . 11 GLU HG2 H 2.68 . 1 65 . 11 GLU HG3 H 2.68 . 1 66 . 12 ILE N N 128.5 . 1 67 . 12 ILE H H 8.45 . 1 68 . 12 ILE HA H 3.54 . 1 69 . 12 ILE HB H 1.76 . 1 70 . 12 ILE HG2 H 1.99 . 1 71 . 12 ILE HG12 H 0.66 . 1 72 . 12 ILE HG13 H 0.66 . 1 73 . 13 LYS N N 123.8 . 1 74 . 13 LYS H H 7.93 . 1 75 . 13 LYS HA H 4.30 . 1 76 . 13 LYS HB2 H 2.23 . 1 77 . 13 LYS HB3 H 2.23 . 1 78 . 13 LYS HG2 H 1.53 . 1 79 . 13 LYS HG3 H 1.53 . 1 80 . 13 LYS HD2 H 1.77 . 1 81 . 13 LYS HD3 H 1.77 . 1 82 . 13 LYS HE2 H 3.53 . 1 83 . 13 LYS HE3 H 3.53 . 1 84 . 14 LYS N N 121.4 . 1 85 . 14 LYS H H 7.07 . 1 86 . 14 LYS HA H 3.95 . 1 87 . 14 LYS HB2 H 1.55 . 1 88 . 14 LYS HB3 H 1.55 . 1 89 . 14 LYS HG2 H 1.27 . 1 90 . 14 LYS HG3 H 1.27 . 1 91 . 14 LYS HD2 H 1.39 . 1 92 . 14 LYS HD3 H 1.39 . 1 93 . 14 LYS HE2 H 2.87 . 1 94 . 14 LYS HE3 H 2.87 . 1 95 . 15 HIS H H 7.79 . 1 96 . 15 HIS HA H 3.95 . 1 97 . 15 HIS HB2 H 2.24 . 2 98 . 15 HIS HB3 H 1.78 . 2 99 . 15 HIS HD2 H 6.81 . 1 100 . 16 ASN N N 125.3 . 1 101 . 16 ASN H H 7.43 . 1 102 . 16 ASN HA H 4.65 . 1 103 . 16 ASN HB2 H 2.23 . 2 104 . 16 ASN HB3 H 2.93 . 2 105 . 17 HIS N N 124.3 . 1 106 . 17 HIS H H 7.49 . 1 107 . 17 HIS HA H 5.09 . 1 108 . 17 HIS HB2 H 3.28 . 2 109 . 17 HIS HB3 H 2.92 . 2 110 . 17 HIS HD2 H 7.22 . 1 111 . 19 LYS N N 125.3 . 1 112 . 19 LYS H H 8.37 . 1 113 . 19 LYS HA H 4.52 . 1 114 . 19 LYS HB2 H 2.13 . 2 115 . 19 LYS HB3 H 1.88 . 2 116 . 19 LYS HG2 H 1.63 . 1 117 . 19 LYS HD2 H 1.51 . 1 118 . 19 LYS HD3 H 1.51 . 1 119 . 20 SER N N 122.6 . 1 120 . 20 SER H H 7.03 . 1 121 . 20 SER HA H 4.69 . 1 122 . 20 SER HB2 H 3.87 . 2 123 . 20 SER HB3 H 3.23 . 2 124 . 21 THR N N 132.2 . 1 125 . 21 THR H H 8.86 . 1 126 . 21 THR HA H 4.23 . 1 127 . 21 THR HB H 3.60 . 1 128 . 21 THR HG2 H 0.75 . 1 129 . 22 TRP N N 134.3 . 1 130 . 22 TRP H H 8.79 . 1 131 . 22 TRP HA H 6.10 . 1 132 . 22 TRP HB2 H 2.92 . 1 133 . 22 TRP HB3 H 2.66 . 1 134 . 22 TRP HD1 H 6.75 . 1 135 . 22 TRP HE3 H 6.51 . 1 136 . 22 TRP HE1 H 8.66 . 1 137 . 22 TRP HZ2 H 6.58 . 1 138 . 22 TRP HZ3 H 5.69 . 1 139 . 22 TRP HH2 H 6.30 . 1 140 . 23 LEU N N 123.4 . 1 141 . 23 LEU H H 8.41 . 1 142 . 23 LEU HA H 4.40 . 1 143 . 23 LEU HB2 H 1.10 . 1 144 . 23 LEU HB3 H 1.10 . 1 145 . 23 LEU HG H 0.67 . 1 146 . 23 LEU HD1 H -0.64 . 2 147 . 23 LEU HD2 H -0.80 . 2 148 . 24 ILE N N 128.1 . 1 149 . 24 ILE H H 7.98 . 1 150 . 24 ILE HA H 4.93 . 1 151 . 24 ILE HB H 1.31 . 2 152 . 24 ILE HG2 H 1.20 . 1 153 . 24 ILE HG12 H 0.61 . 1 154 . 24 ILE HG13 H 0.46 . 2 155 . 25 LEU N N 128.9 . 1 156 . 25 LEU H H 8.30 . 1 157 . 25 LEU HA H 4.35 . 1 158 . 25 LEU HB2 H 1.24 . 2 159 . 25 LEU HB3 H 0.09 . 2 160 . 25 LEU HG H -0.22 . 1 161 . 25 LEU HD1 H -2.17 . 2 162 . 25 LEU HD2 H -0.90 . 2 163 . 26 HIS N N 132.4 . 1 164 . 26 HIS H H 9.29 . 1 165 . 26 HIS HA H 3.80 . 1 166 . 26 HIS HB2 H 3.12 . 1 167 . 26 HIS HB3 H 3.12 . 1 168 . 26 HIS HD2 H 7.08 . 1 169 . 27 HIS N N 115.6 . 1 170 . 27 HIS H H 8.58 . 1 171 . 27 HIS HA H 3.81 . 1 172 . 27 HIS HB2 H 3.62 . 2 173 . 27 HIS HB3 H 3.17 . 2 174 . 27 HIS HD2 H 7.07 . 1 175 . 27 HIS HE1 H 7.93 . 1 176 . 28 LYS N N 129.3 . 1 177 . 28 LYS H H 8.21 . 1 178 . 28 LYS HA H 4.71 . 1 179 . 28 LYS HB2 H 2.06 . 1 180 . 28 LYS HB3 H 2.06 . 1 181 . 28 LYS HG2 H 1.30 . 1 182 . 28 LYS HG3 H 1.30 . 1 183 . 28 LYS HD2 H 1.85 . 1 184 . 28 LYS HD3 H 1.85 . 1 185 . 29 VAL N N 128.1 . 1 186 . 29 VAL H H 8.21 . 1 187 . 29 VAL HA H 4.01 . 1 188 . 29 VAL HB H 0.97 . 1 189 . 29 VAL HG1 H -0.01 . 2 190 . 29 VAL HG2 H 0.50 . 2 191 . 30 TYR N N 134.0 . 1 192 . 30 TYR H H 8.79 . 1 193 . 30 TYR HA H 4.35 . 1 194 . 30 TYR HB2 H 1.99 . 2 195 . 30 TYR HB3 H 1.78 . 2 196 . 30 TYR HD1 H 6.53 . 1 197 . 30 TYR HD2 H 6.53 . 1 198 . 30 TYR HE1 H 6.40 . 1 199 . 30 TYR HE2 H 6.40 . 1 200 . 31 ASP H H 8.11 . 1 201 . 31 ASP HA H 4.94 . 1 202 . 31 ASP HB2 H 2.88 . 2 203 . 31 ASP HB3 H 1.76 . 2 204 . 32 LEU N N 129.0 . 1 205 . 32 LEU H H 8.34 . 1 206 . 32 LEU HA H 4.22 . 1 207 . 32 LEU HB2 H 1.63 . 2 208 . 32 LEU HB3 H 0.99 . 2 209 . 32 LEU HD1 H 0.87 . 1 210 . 32 LEU HD2 H 0.87 . 1 211 . 33 THR N N 126.4 . 1 212 . 33 THR H H 8.64 . 1 213 . 33 THR HA H 3.66 . 1 214 . 33 THR HB H 4.29 . 1 215 . 33 THR HG2 H 1.30 . 1 216 . 34 LYS N N 124.2 . 1 217 . 34 LYS H H 8.88 . 1 218 . 34 LYS HA H 4.55 . 1 219 . 34 LYS HB2 H 2.18 . 2 220 . 34 LYS HB3 H 1.97 . 2 221 . 34 LYS HG2 H 1.66 . 1 222 . 34 LYS HG3 H 1.66 . 1 223 . 34 LYS HD2 H 1.86 . 1 224 . 34 LYS HD3 H 1.86 . 1 225 . 35 PHE N N 127.3 . 1 226 . 35 PHE H H 8.10 . 1 227 . 35 PHE HA H 5.16 . 1 228 . 35 PHE HB2 H 2.86 . 2 229 . 35 PHE HB3 H 2.55 . 2 230 . 35 PHE HD1 H 7.58 . 1 231 . 35 PHE HD2 H 7.58 . 1 232 . 35 PHE HE1 H 8.34 . 1 233 . 35 PHE HE2 H 8.34 . 1 234 . 35 PHE HZ H 8.34 . 1 235 . 36 LEU N N 126.7 . 1 236 . 36 LEU H H 7.87 . 1 237 . 36 LEU HA H 4.86 . 1 238 . 36 LEU HB2 H 2.47 . 2 239 . 36 LEU HB3 H 2.39 . 2 240 . 36 LEU HG H 2.12 . 1 241 . 36 LEU HD1 H 1.28 . 2 242 . 36 LEU HD2 H 1.19 . 2 243 . 37 GLU N N 119.5 . 1 244 . 37 GLU H H 8.58 . 1 245 . 37 GLU HA H 4.94 . 1 246 . 37 GLU HB2 H 2.54 . 2 247 . 37 GLU HB3 H 2.38 . 2 248 . 37 GLU HG2 H 2.67 . 1 249 . 37 GLU HG3 H 2.67 . 1 250 . 38 GLU H H 8.34 . 1 251 . 38 GLU HA H 4.93 . 1 252 . 38 GLU HB2 H 2.49 . 2 253 . 38 GLU HB3 H 2.41 . 2 254 . 38 GLU HG2 H 2.65 . 1 255 . 38 GLU HG3 H 2.57 . 1 256 . 39 HIS H H 9.06 . 1 257 . 39 HIS HA H 6.81 . 1 258 . 39 HIS HB2 H 16.61 . 1 259 . 39 HIS HB3 H 7.42 . 1 260 . 39 HIS HD1 H 13.1 . 1 261 . 40 PRO HA H 4.06 . 1 262 . 40 PRO HB2 H 0.61 . 2 263 . 40 PRO HB3 H -3.41 . 2 264 . 40 PRO HG2 H 1.20 . 2 265 . 40 PRO HG3 H -0.62 . 2 266 . 41 GLY HA2 H 6.15 . 1 267 . 41 GLY HA3 H 6.15 . 1 268 . 42 GLY N N 119.9 . 1 269 . 42 GLY H H 6.59 . 1 270 . 42 GLY HA2 H 6.14 . 9 271 . 42 GLY HA3 H 5.80 . 9 272 . 43 GLU N N 128.4 . 1 273 . 43 GLU H H 10.04 . 1 274 . 43 GLU HA H 5.93 . 1 275 . 43 GLU HB2 H 2.94 . 2 276 . 43 GLU HB3 H 2.82 . 2 277 . 44 GLU N N 131.3 . 1 278 . 44 GLU H H 9.60 . 1 279 . 44 GLU HA H 4.25 . 1 280 . 44 GLU HB2 H 2.53 . 2 281 . 44 GLU HB3 H 2.37 . 2 282 . 44 GLU HG2 H 2.64 . 9 283 . 44 GLU HG3 H 2.64 . 9 284 . 45 VAL N N 119.5 . 1 285 . 45 VAL H H 9.41 . 1 286 . 45 VAL HA H 4.04 . 1 287 . 45 VAL HB H 2.16 . 1 288 . 45 VAL HG1 H 1.56 . 2 289 . 45 VAL HG2 H 1.51 . 2 290 . 46 LEU N N 123.4 . 1 291 . 46 LEU H H 7.37 . 1 292 . 46 LEU HA H 3.05 . 1 293 . 46 LEU HB2 H 2.74 . 1 294 . 46 LEU HB3 H 2.74 . 1 295 . 46 LEU HG H 2.47 . 1 296 . 46 LEU HD1 H 0.75 . 2 297 . 46 LEU HD2 H 0.54 . 2 298 . 47 ARG N N 126.0 . 1 299 . 47 ARG H H 8.50 . 1 300 . 47 ARG HA H 3.83 . 1 301 . 47 ARG HB2 H 2.05 . 1 302 . 47 ARG HB3 H 2.05 . 1 303 . 47 ARG HD2 H 3.36 . 1 304 . 47 ARG HD3 H 3.36 . 1 305 . 48 GLU N N 123.8 . 1 306 . 48 GLU H H 8.14 . 1 307 . 48 GLU HA H 3.93 . 1 308 . 48 GLU HB2 H 1.96 . 2 309 . 48 GLU HB3 H 1.86 . 2 310 . 48 GLU HG2 H 2.38 . 2 311 . 48 GLU HG3 H 2.24 . 2 312 . 49 GLN N N 119.9 . 1 313 . 49 GLN H H 6.59 . 1 314 . 49 GLN HA H 4.09 . 1 315 . 49 GLN HB2 H 1.26 . 2 316 . 49 GLN HB3 H 0.75 . 2 317 . 49 GLN HG2 H 1.95 . 2 318 . 49 GLN HG3 H 1.70 . 2 319 . 50 ALA N N 128.3 . 1 320 . 50 ALA H H 6.87 . 1 321 . 50 ALA HA H 3.67 . 1 322 . 50 ALA HB H 1.36 . 1 323 . 51 GLY N N 118.5 . 1 324 . 51 GLY H H 9.34 . 1 325 . 51 GLY HA2 H 3.84 . 9 326 . 51 GLY HA3 H 3.52 . 9 327 . 52 GLY N N 112.3 . 1 328 . 52 GLY H H 7.35 . 1 329 . 52 GLY HA2 H 4.15 . 9 330 . 52 GLY HA3 H 3.50 . 9 331 . 53 ASP N N 124.6 . 1 332 . 53 ASP H H 8.27 . 1 333 . 53 ASP HA H 4.70 . 1 334 . 53 ASP HB2 H 2.65 . 2 335 . 53 ASP HB3 H 2.17 . 2 336 . 54 ALA N N 136.3 . 1 337 . 54 ALA H H 8.21 . 1 338 . 54 ALA HA H 4.35 . 1 339 . 54 ALA HB H 0.01 . 1 340 . 55 THR N N 124.6 . 1 341 . 55 THR H H 7.83 . 1 342 . 55 THR HA H 2.85 . 1 343 . 55 THR HB H 3.82 . 1 344 . 55 THR HG2 H 0.38 . 1 345 . 56 GLU N N 126.3 . 1 346 . 56 GLU H H 8.50 . 1 347 . 56 GLU HA H 3.90 . 1 348 . 56 GLU HB2 H 2.15 . 2 349 . 56 GLU HB3 H 2.10 . 2 350 . 56 GLU HG2 H 1.87 . 2 351 . 56 GLU HG3 H 1.80 . 2 352 . 57 ASN N N 123.5 . 1 353 . 57 ASN H H 7.65 . 1 354 . 57 ASN HA H 4.22 . 1 355 . 57 ASN HB2 H 2.03 . 2 356 . 57 ASN HB3 H 1.61 . 2 357 . 57 ASN HD21 H 6.68 . 9 358 . 57 ASN HD22 H 7.40 . 9 359 . 58 PHE H H 7.90 . 1 360 . 58 PHE HA H 3.19 . 1 361 . 58 PHE HB2 H 2.79 . 2 362 . 58 PHE HB3 H 0.75 . 2 363 . 59 GLU N N 127.2 . 2 364 . 59 GLU H H 8.76 . 1 365 . 59 GLU HA H 5.48 . 1 366 . 59 GLU HB2 H 2.78 . 2 367 . 59 GLU HB3 H 2.40 . 2 368 . 59 GLU HG2 H 3.14 . 9 369 . 59 GLU HG3 H 3.04 . 9 370 . 60 ASP N N 128.9 . 1 371 . 60 ASP H H 8.93 . 1 372 . 60 ASP HA H 4.85 . 1 373 . 60 ASP HB2 H 2.98 . 2 374 . 60 ASP HB3 H 2.85 . 2 375 . 61 VAL N N 123.4 . 1 376 . 61 VAL H H 8.18 . 1 377 . 61 VAL HA H 4.46 . 1 378 . 61 VAL HB H 2.62 . 1 379 . 61 VAL HG2 H 1.97 . 1 380 . 62 GLY N N 116.4 . 1 381 . 62 GLY H H 9.06 . 1 382 . 62 GLY HA2 H 5.21 . 9 383 . 62 GLY HA3 H 4.93 . 9 384 . 63 HIS H H 11.45 . 1 385 . 63 HIS HA H 7.54 . 1 386 . 63 HIS HB2 H 10.45 . 2 387 . 63 HIS HB3 H 10.01 . 2 388 . 63 HIS HD2 H 13 . 1 389 . 63 HIS HE1 H -14.0 . 1 390 . 64 SER H H 11.80 . 1 391 . 64 SER HA H 4.98 . 1 392 . 64 SER HB2 H 4.52 . 2 393 . 64 SER HB3 H 4.21 . 2 394 . 65 THR N N 124.2 . 1 395 . 65 THR H H 9.37 . 1 396 . 65 THR HA H 4.79 . 1 397 . 65 THR HB H 1.57 . 1 398 . 66 ASP N N 129.3 . 1 399 . 66 ASP H H 8.38 . 1 400 . 66 ASP HA H 4.46 . 1 401 . 66 ASP HB2 H 2.57 . 2 402 . 66 ASP HB3 H 2.48 . 2 403 . 67 ALA N N 132.0 . 1 404 . 67 ALA H H 8.90 . 1 405 . 67 ALA HA H 4.08 . 1 406 . 67 ALA HB H 2.51 . 1 407 . 68 ARG N N 126.5 . 1 408 . 68 ARG H H 9.36 . 1 409 . 68 ARG HA H 4.68 . 1 410 . 68 ARG HB2 H 2.93 . 2 411 . 68 ARG HB3 H 2.70 . 2 412 . 68 ARG HG2 H 2.63 . 9 413 . 68 ARG HG3 H 2.63 . 9 414 . 68 ARG HD2 H 3.22 . 9 415 . 68 ARG HD3 H 3.22 . 9 416 . 69 GLU N N 130.8 . 1 417 . 69 GLU H H 9.07 . 1 418 . 69 GLU HA H 4.25 . 1 419 . 69 GLU HB2 H 2.28 . 2 420 . 69 GLU HB3 H 2.18 . 2 421 . 69 GLU HG2 H 2.57 . 9 422 . 69 GLU HG3 H 2.43 . 9 423 . 70 LEU H H 8.34 . 1 424 . 70 LEU HA H 4.17 . 1 425 . 70 LEU HB2 H 2.00 . 2 426 . 70 LEU HB3 H 1.67 . 2 427 . 70 LEU HD1 H 1.33 . 1 428 . 70 LEU HD2 H 1.33 . 1 429 . 71 SER N N 122.2 . 1 430 . 71 SER H H 8.48 . 1 431 . 71 SER HA H 3.82 . 1 432 . 71 SER HB2 H 3.43 . 1 433 . 71 SER HB3 H 3.43 . 1 434 . 72 LYS N N 127.7 . 1 435 . 72 LYS H H 7.18 . 1 436 . 72 LYS HA H 4.02 . 1 437 . 72 LYS HB2 H 1.91 . 2 438 . 72 LYS HB3 H 1.76 . 2 439 . 73 THR N N 117.1 . 1 440 . 73 THR H H 7.63 . 1 441 . 73 THR HA H 3.91 . 1 442 . 73 THR HB H 3.70 . 1 443 . 73 THR HG2 H 1.01 . 1 444 . 74 PHE N N 125.4 . 1 445 . 74 PHE H H 7.27 . 1 446 . 74 PHE HA H 3.55 . 1 447 . 74 PHE HB2 H 2.47 . 1 448 . 74 PHE HB3 H 2.47 . 1 449 . 74 PHE HD1 H 6.97 . 9 450 . 74 PHE HD2 H 6.97 . 9 451 . 74 PHE HE1 H 6.71 . 9 452 . 74 PHE HE2 H 6.71 . 9 453 . 74 PHE HZ H 7.10 . 1 454 . 75 ILE N N 127.7 . 1 455 . 75 ILE H H 6.78 . 1 456 . 75 ILE HA H 3.39 . 1 457 . 75 ILE HB H 1.38 . 1 458 . 75 ILE HG2 H 1.28 . 9 459 . 75 ILE HG12 H 0.78 . 9 460 . 75 ILE HG13 H 0.68 . 1 461 . 75 ILE HD1 H -0.35 . 1 462 . 76 ILE N N 127.3 . 1 463 . 76 ILE H H 8.59 . 1 464 . 76 ILE HA H 4.15 . 1 465 . 76 ILE HB H 1.72 . 1 466 . 76 ILE HG2 H 0.10 . 9 467 . 76 ILE HG12 H -0.15 . 9 468 . 76 ILE HG13 H 0.66 . 1 469 . 76 ILE HD1 H -1.21 . 1 470 . 77 GLY N N 117.9 . 1 471 . 77 GLY H H 7.30 . 1 472 . 77 GLY HA2 H 4.31 . 9 473 . 77 GLY HA3 H 4.01 . 9 474 . 78 GLU N N 125.7 . 1 475 . 78 GLU H H 8.99 . 1 476 . 78 GLU HA H 5.06 . 1 477 . 78 GLU HB2 H 1.67 . 1 478 . 78 GLU HB3 H 1.67 . 1 479 . 78 GLU HG2 H 2.13 . 9 480 . 78 GLU HG3 H 2.13 . 9 481 . 79 LEU N N 130.4 . 1 482 . 79 LEU H H 8.69 . 1 483 . 79 LEU HA H 4.53 . 1 484 . 79 LEU HB2 H 2.13 . 1 485 . 79 LEU HB3 H 2.13 . 1 486 . 80 HIS N N 137.8 . 1 487 . 80 HIS H H 9.00 . 1 488 . 80 HIS HA H 3.73 . 1 489 . 80 HIS HB2 H 2.81 . 2 490 . 80 HIS HB3 H 2.53 . 2 491 . 80 HIS HD2 H 6.95 . 1 492 . 80 HIS HE1 H 7.39 . 1 493 . 81 PRO HA H 3.66 . 1 494 . 81 PRO HB2 H 2.13 . 2 495 . 81 PRO HB3 H 1.69 . 2 496 . 81 PRO HG2 H 1.35 . 9 497 . 81 PRO HG3 H 1.49 . 9 498 . 82 ASP N N 128.5 . 1 499 . 82 ASP H H 11.00 . 1 500 . 82 ASP HA H 4.40 . 1 501 . 82 ASP HB2 H 2.59 . 2 502 . 82 ASP HB3 H 2.66 . 2 503 . 83 ASP N N 124.9 . 1 504 . 83 ASP H H 8.11 . 1 505 . 83 ASP HA H 4.86 . 1 506 . 83 ASP HB2 H 2.88 . 2 507 . 83 ASP HB3 H 2.61 . 2 508 . 84 ARG N N 126.9 . 1 509 . 84 ARG H H 7.28 . 1 510 . 84 ARG HA H 4.18 . 1 511 . 84 ARG HB2 H 1.01 . 2 512 . 84 ARG HB3 H 1.67 . 2 513 . 85 SER H H 7.89 . 1 514 . 85 SER HA H 4.77 . 1 515 . 86 LYS H H 7.65 . 1 516 . 86 LYS HA H 4.24 . 1 517 . 86 LYS HB2 H 2.99 . 2 518 . 86 LYS HB3 H 1.93 . 2 519 . 86 LYS HG2 H 1.38 . 9 520 . 86 LYS HG3 H 1.38 . 9 521 . 87 LEU N N 122.5 . 1 522 . 87 LEU H H 7.38 . 1 523 . 87 LEU HA H 4.24 . 1 524 . 87 LEU HB2 H 1.81 . 1 525 . 87 LEU HB3 H 1.81 . 1 526 . 87 LEU HG H 1.49 . 1 527 . 87 LEU HD1 H 0.86 . 9 528 . 87 LEU HD2 H 0.86 . 9 529 . 88 SER H H 7.51 . 1 530 . 88 SER HA H 4.35 . 1 531 . 88 SER HB2 H 3.87 . 2 532 . 88 SER HB3 H 3.24 . 2 533 . 89 LYS H H 8.31 . 1 534 . 89 LYS HA H 4.40 . 1 stop_ save_