data_1672 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; 1H and 15N NMR Resonance Assignments and Preliminary Structural Characterization of Escherichia coli Apocytochrome b562 ; _BMRB_accession_number 1672 _BMRB_flat_file_name bmr1672.str _Entry_type update _Submission_date 1995-07-31 _Accession_date 1996-04-13 _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 Feng Yiqing . . 2 Wand A. Joshua . 3 Sligar Stephen G. . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 498 "15N chemical shifts" 108 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2010-06-15 revision BMRB 'Complete natural source information' 1999-06-14 revision BMRB 'Converted to BMRB NMR-STAR V 2.1 format' 1996-04-13 revision BMRB 'Link to the Protein Data Bank added' 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 ; Feng, Yiqing, Wand, A. Joshua, Sligar, Stephen G., "1H and 15N NMR Resonance Assignments and Preliminary Structural Characterization of Escherichia coli Apocytochrome b562," Biochemistry 30 (31), 7711-7717 (1991). ; _Citation_title ; 1H and 15N NMR Resonance Assignments and Preliminary Structural Characterization of Escherichia coli Apocytochrome b562 ; _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 Feng Yiqing . . 2 Wand A. Joshua . 3 Sligar Stephen G. . stop_ _Journal_abbreviation Biochemistry _Journal_volume 30 _Journal_issue 31 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 7711 _Page_last 7717 _Year 1991 _Details . save_ ################################## # Molecular system description # ################################## save_system_cytochrome_b562 _Saveframe_category molecular_system _Mol_system_name 'cytochrome b562' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'cytochrome b562' $cytochrome_b562 stop_ _System_molecular_weight . _System_oligomer_state ? _System_paramagnetic ? _System_thiol_state . _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_cytochrome_b562 _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'cytochrome b562' _Name_variant 'apo form' _Molecular_mass . _Mol_thiol_state . _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 106 _Mol_residue_sequence ; ADLEDNMETLNDNLKVIEKA DNAAQVKDALTKMRAAALDA QKATPPKLEDKSPDSPEMKD FRHGFDILVGQIDDALKLAN EGKVKEAQAAAEQLKTTRNA YHQKYR ; loop_ _Residue_seq_code _Residue_label 1 ALA 2 ASP 3 LEU 4 GLU 5 ASP 6 ASN 7 MET 8 GLU 9 THR 10 LEU 11 ASN 12 ASP 13 ASN 14 LEU 15 LYS 16 VAL 17 ILE 18 GLU 19 LYS 20 ALA 21 ASP 22 ASN 23 ALA 24 ALA 25 GLN 26 VAL 27 LYS 28 ASP 29 ALA 30 LEU 31 THR 32 LYS 33 MET 34 ARG 35 ALA 36 ALA 37 ALA 38 LEU 39 ASP 40 ALA 41 GLN 42 LYS 43 ALA 44 THR 45 PRO 46 PRO 47 LYS 48 LEU 49 GLU 50 ASP 51 LYS 52 SER 53 PRO 54 ASP 55 SER 56 PRO 57 GLU 58 MET 59 LYS 60 ASP 61 PHE 62 ARG 63 HIS 64 GLY 65 PHE 66 ASP 67 ILE 68 LEU 69 VAL 70 GLY 71 GLN 72 ILE 73 ASP 74 ASP 75 ALA 76 LEU 77 LYS 78 LEU 79 ALA 80 ASN 81 GLU 82 GLY 83 LYS 84 VAL 85 LYS 86 GLU 87 ALA 88 GLN 89 ALA 90 ALA 91 ALA 92 GLU 93 GLN 94 LEU 95 LYS 96 THR 97 THR 98 ARG 99 ASN 100 ALA 101 TYR 102 HIS 103 GLN 104 LYS 105 TYR 106 ARG stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-10-28 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 1APC "Solution Structure Of Apocytochrome B562" 100.00 106 100.00 100.00 2.90e-68 PDB 1LM3 "A Multi-Generation Analysis Of Cytochrome B562 Redox Variants: Evolutionary Strategies For Modulating Redox Potential Revealed " 99.06 106 98.10 99.05 7.32e-66 PDB 1M6T "Crystal Structure Of B562ril, A Redesigned Four Helix Bundle" 99.06 106 98.10 98.10 7.55e-65 PDB 1QPU "Solution Structure Of Oxidized Escherichia Coli Cytochrome B562" 100.00 106 100.00 100.00 2.90e-68 PDB 1QQ3 "The Solution Structure Of The Heme Binding Variant Arg98cys Of Oxidized Escherichia Coli Cytochrome B562" 100.00 106 99.06 99.06 4.74e-67 PDB 256B "Improvement Of The 2.5 Angstroms Resolution Model Of Cytochrome B562 By Redetermining The Primary Structure And Using Molecular" 100.00 106 100.00 100.00 2.90e-68 PDB 2BC5 "Crystal Structure Of E. Coli Cytochrome B562 With Engineered C-Type Heme Linkages" 100.00 106 97.17 97.17 3.97e-65 PDB 3U8P "Cytochrome B562 Integral Fusion With Egfp" 100.00 347 100.00 100.00 2.38e-65 PDB 4EA3 "Structure Of The NOFQ OPIOID RECEPTOR IN COMPLEX WITH A PEPTIDE Mimetic" 99.06 434 98.10 98.10 2.88e-64 PDB 4EIY "Crystal Structure Of The Chimeric Protein Of A2aar-Bril In Complex With Zm241385 At 1.8a Resolution" 99.06 447 98.10 98.10 3.88e-64 PDB 4IAQ "Crystal Structure Of The Chimeric Protein Of 5-ht1b-bril In Complex With Dihydroergotamine (psi Community Target)" 99.06 403 98.10 98.10 1.37e-64 PDB 4IAR "Crystal Structure Of The Chimeric Protein Of 5-ht1b-bril In Complex With Ergotamine (psi Community Target)" 99.06 401 98.10 98.10 1.30e-64 PDB 4IB4 "Crystal Structure Of The Chimeric Protein Of 5-ht2b-bril In Complex With Ergotamine" 99.06 430 98.10 98.10 7.65e-63 PDB 4JKV "Structure Of The Human Smoothened 7tm Receptor In Complex With An Antitumor Agent" 99.06 475 98.10 98.10 7.24e-64 PDB 4L6R "Structure Of The Class B Human Glucagon G Protein Coupled Receptor" 99.06 425 98.10 98.10 3.28e-64 PDB 4N4W "Structure Of The Human Smoothened Receptor In Complex With Sant-1" 99.06 475 98.10 98.10 7.24e-64 PDB 4N6H "1.8 A Structure Of The Human Delta Opioid 7tm Receptor (psi Community Target)" 99.06 414 98.10 98.10 1.79e-64 PDB 4NC3 "Crystal Structure Of The 5-ht2b Receptor Solved Using Serial Femtosecond Crystallography In Lipidic Cubic Phase" 99.06 430 98.10 98.10 7.65e-63 PDB 4NTJ "Structure Of The Human P2y12 Receptor In Complex With An Antithrombotic Drug" 99.06 466 98.10 98.10 6.18e-63 PDB 4O9R "Human Smoothened Receptor Structure In Complex With Cyclopamine" 99.06 468 98.10 98.10 6.21e-64 PDB 4OR2 "Human Class C G Protein-coupled Metabotropic Glutamate Receptor 1 In Complex With A Negative Allosteric Modulator" 99.06 389 98.10 98.10 9.66e-65 PDB 4PXZ "Crystal Structure Of P2y12 Receptor In Complex With 2mesadp" 99.06 466 98.10 98.10 6.18e-63 PDB 4PY0 "Crystal Structure Of P2y12 Receptor In Complex With 2mesatp" 99.06 466 98.10 98.10 6.18e-63 PDB 4QIM "Structure Of The Human Smoothened Receptor In Complex With Anta Xv" 99.06 468 98.10 98.10 6.21e-64 PDB 4QIN "Structure Of The Human Smoothened Receptor In Complex With Sag1.5" 99.06 468 98.10 98.10 6.21e-64 PDB 4RWA "Synchrotron Structure Of The Human Delta Opioid Receptor In Complex With A Bifunctional Peptide (psi Community Target)" 99.06 411 98.10 98.10 1.66e-64 PDB 4RWD "Xfel Structure Of The Human Delta Opioid Receptor In Complex With A Bifunctional Peptide" 99.06 411 98.10 98.10 1.66e-64 PDB 4YAY "Xfel Structure Of Human Angiotensin Receptor" 99.06 414 98.10 98.10 1.79e-64 PDB 4Z34 "Crystal Structure Of Human Lysophosphatidic Acid Receptor 1 In Complex With Ono9780307" 99.06 464 98.10 98.10 5.69e-64 PDB 4Z35 "Crystal Structure Of Human Lysophosphatidic Acid Receptor 1 In Complex With Ono-9910539" 99.06 464 98.10 98.10 5.69e-64 PDB 4ZUD "Crystal Structure Of Human Angiotensin Receptor In Complex With Inverse Agonist Olmesartan At 2.8a Resolution" 99.06 410 98.10 98.10 1.62e-64 PDB 5AWI "Domain-swapped Cytochrome Cb562 Dimer" 100.00 106 98.11 98.11 6.28e-66 PDB 5DHG "The Crystal Structure Of Nociceptin/orphanin Fq Peptide Receptor (nop) In Complex With C-35 (psi Community Target)" 99.06 424 98.10 98.10 2.76e-64 PDB 5DHH "The Crystal Structure Of Nociceptin/orphanin Fq Peptide Receptor (nop) In Complex With Sb-612111 (psi Community Target)" 99.06 424 98.10 98.10 2.76e-64 DBJ BAB38636 "cytochrome b(562) [Escherichia coli O157:H7 str. Sakai]" 94.34 100 97.00 100.00 6.98e-63 DBJ BAG80065 "cytochrome b562 [Escherichia coli SE11]" 100.00 128 100.00 100.00 6.61e-69 DBJ BAI28542 "cytochrome b562 [Escherichia coli O26:H11 str. 11368]" 98.11 130 99.04 99.04 1.03e-65 DBJ BAI33713 "cytochrome b562 [Escherichia coli O103:H2 str. 12009]" 100.00 128 99.06 99.06 3.87e-68 DBJ BAI38842 "cytochrome b562 [Escherichia coli O111:H- str. 11128]" 100.00 128 100.00 100.00 6.61e-69 EMBL CAA47706 "cytochrome b562 [Escherichia coli]" 100.00 128 100.00 100.00 6.61e-69 EMBL CAP78754 "Soluble cytochrome b562 [Escherichia coli LF82]" 100.00 128 97.17 98.11 3.17e-67 EMBL CAQ34585 "cytochrome b562 (soluble) [Escherichia coli BL21(DE3)]" 94.34 100 100.00 100.00 4.19e-64 EMBL CAQ91733 "soluble cytochrome b562 [Escherichia fergusonii ATCC 35469]" 100.00 128 98.11 99.06 9.05e-68 EMBL CAR01210 "soluble cytochrome b562 [Escherichia coli IAI1]" 100.00 128 100.00 100.00 6.61e-69 GB AAA97133 "cytochrome b562 [Escherichia coli str. K-12 substr. MG1655]" 94.34 100 97.00 100.00 6.98e-63 GB AAB20782 "cytochrome b562 [Escherichia coli]" 100.00 128 100.00 100.00 6.61e-69 GB AAG59433 "cytochrome b (562) [Escherichia coli O157:H7 str. EDL933]" 94.34 100 97.00 100.00 6.98e-63 GB AAN45672 "Soluble cytochrome B562 precursor [Shigella flexneri 2a str. 301]" 80.19 114 98.82 98.82 5.83e-51 GB AAN83756 "Soluble cytochrome b562 precursor [Escherichia coli CFT073]" 100.00 128 97.17 98.11 3.17e-67 PIR E86121 "cytochrome b (562) [imported] - Escherichia coli (strain O157:H7, substrain EDL933)" 94.34 100 97.00 100.00 6.98e-63 PIR E91280 "cytochrome b(562) [imported] - Escherichia coli (strain O157:H7, substrain RIMD 0509952)" 94.34 100 97.00 100.00 6.98e-63 REF NP_313240 "cytochrome b(562) [Escherichia coli O157:H7 str. Sakai]" 100.00 128 97.17 100.00 1.27e-67 REF NP_709965 "soluble cytochrome B562 [Shigella flexneri 2a str. 301]" 80.19 114 98.82 98.82 5.83e-51 REF WP_000112424 "cytochrome b562, partial [Escherichia coli]" 96.23 102 100.00 100.00 1.36e-65 REF WP_000315974 "cytochrome b562, partial [Escherichia coli]" 96.23 103 100.00 100.00 1.20e-65 REF WP_000319497 "cytochrome b562, partial [Escherichia coli]" 98.11 106 99.04 99.04 2.63e-66 SP P0ABE7 "RecName: Full=Soluble cytochrome b562; Short=Cytochrome b-562; Flags: Precursor" 100.00 128 100.00 100.00 6.61e-69 SP P0ABE8 "RecName: Full=Soluble cytochrome b562; Short=Cytochrome b-562; Flags: Precursor" 100.00 128 97.17 100.00 1.27e-67 SP Q8CVG7 "RecName: Full=Soluble cytochrome b562; Short=Cytochrome b-562; Flags: Precursor" 100.00 128 97.17 98.11 3.17e-67 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 $cytochrome_b562 . 354 Bacteria . Azotobacter vinelandii 'ATCC 13705' 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 $cytochrome_b562 'not available' . Escherichia coli TB-1 . 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_list _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 5.2 . na temperature 293 . 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 . . . 0 . . . . . $entry_citation $entry_citation 'external [15]NH4Cl' N . . . 24.93 . . . . . $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 'cytochrome b562' _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 ALA HA H 4.18 . 1 2 . 1 ALA HB H 1.57 . 1 3 . 2 ASP H H 8.98 . 1 4 . 2 ASP HA H 4.68 . 1 5 . 2 ASP HB2 H 2.91 . 2 6 . 2 ASP HB3 H 3.04 . 2 7 . 2 ASP N N 124 . 1 8 . 3 LEU H H 8.76 . 1 9 . 3 LEU HA H 4.09 . 1 10 . 3 LEU HB2 H 1.62 . 2 11 . 3 LEU HB3 H 1.92 . 2 12 . 3 LEU HG H 1.73 . 1 13 . 3 LEU HD1 H 1.04 . 2 14 . 3 LEU HD2 H 1.18 . 2 15 . 3 LEU N N 126.4 . 1 16 . 4 GLU H H 8.77 . 1 17 . 4 GLU HA H 4.1 . 1 18 . 4 GLU HB2 H 2.05 . 2 19 . 4 GLU HB3 H 2.52 . 2 20 . 4 GLU N N 121.6 . 1 21 . 5 ASP H H 8.06 . 1 22 . 5 ASP HA H 4.52 . 1 23 . 5 ASP HB2 H 2.83 . 1 24 . 5 ASP HB3 H 2.83 . 1 25 . 5 ASP N N 123.9 . 1 26 . 6 ASN H H 8.08 . 1 27 . 6 ASN HA H 4.61 . 1 28 . 6 ASN HB2 H 2.61 . 2 29 . 6 ASN HB3 H 2.77 . 2 30 . 6 ASN ND2 N 118.5 . 1 31 . 6 ASN HD21 H 6.37 . 2 32 . 6 ASN HD22 H 8.42 . 2 33 . 6 ASN N N 121.9 . 1 34 . 7 MET H H 8.67 . 1 35 . 7 MET HA H 4.55 . 1 36 . 7 MET HB2 H 2.41 . 1 37 . 7 MET HB3 H 2.41 . 1 38 . 7 MET N N 122.3 . 1 39 . 8 GLU H H 8.35 . 1 40 . 8 GLU HA H 4.28 . 1 41 . 8 GLU HB2 H 2.33 . 2 42 . 8 GLU HB3 H 2.57 . 2 43 . 8 GLU N N 126.3 . 1 44 . 9 THR H H 8.43 . 1 45 . 9 THR HA H 4.12 . 1 46 . 9 THR HB H 4.46 . 1 47 . 9 THR HG2 H 1.2 . 1 48 . 9 THR N N 121.6 . 1 49 . 10 LEU H H 8.24 . 1 50 . 10 LEU HA H 4.06 . 1 51 . 10 LEU HB2 H 1.98 . 2 52 . 10 LEU HB3 H 2.23 . 2 53 . 10 LEU HD1 H 1.01 . 1 54 . 10 LEU HD2 H 1.01 . 1 55 . 10 LEU N N 126.8 . 1 56 . 11 ASN H H 8.14 . 1 57 . 11 ASN HA H 4.46 . 1 58 . 11 ASN HB2 H 2.9 . 2 59 . 11 ASN HB3 H 3.02 . 2 60 . 11 ASN ND2 N 118.8 . 1 61 . 11 ASN HD21 H 7.09 . 2 62 . 11 ASN HD22 H 7.9 . 2 63 . 11 ASN N N 121.5 . 1 64 . 12 ASP H H 9.32 . 1 65 . 12 ASP HA H 4.43 . 1 66 . 12 ASP HB2 H 2.75 . 2 67 . 12 ASP HB3 H 2.9 . 2 68 . 12 ASP N N 123.6 . 1 69 . 13 ASN H H 7.94 . 1 70 . 13 ASN HA H 4.58 . 1 71 . 13 ASN HB2 H 2.58 . 2 72 . 13 ASN HB3 H 2.71 . 2 73 . 13 ASN N N 120.9 . 1 74 . 14 LEU H H 8.15 . 1 75 . 14 LEU HA H 4.15 . 1 76 . 14 LEU HB2 H 1.76 . 2 77 . 14 LEU HB3 H 1.87 . 2 78 . 14 LEU N N 127.1 . 1 79 . 15 LYS H H 7.42 . 1 80 . 15 LYS HA H 4.17 . 1 81 . 15 LYS HB2 H 1.94 . 2 82 . 15 LYS HB3 H 2.07 . 2 83 . 15 LYS N N 122 . 1 84 . 16 VAL H H 7.3 . 1 85 . 16 VAL HA H 3.6 . 1 86 . 16 VAL HB H 2.47 . 1 87 . 16 VAL HG1 H .99 . 2 88 . 16 VAL HG2 H 1.15 . 2 89 . 16 VAL N N 122.6 . 1 90 . 17 ILE H H 7.97 . 1 91 . 17 ILE HA H 3.43 . 1 92 . 17 ILE HB H 2.17 . 1 93 . 17 ILE HG2 H 1.01 . 1 94 . 17 ILE HD1 H .89 . 1 95 . 17 ILE N N 123.2 . 1 96 . 18 GLU H H 8.05 . 1 97 . 18 GLU HA H 3.98 . 1 98 . 18 GLU HB2 H 2.34 . 1 99 . 18 GLU HB3 H 2.34 . 1 100 . 18 GLU N N 121.5 . 1 101 . 19 LYS H H 7.26 . 1 102 . 19 LYS HA H 4.48 . 1 103 . 19 LYS HB2 H 1.82 . 2 104 . 19 LYS HB3 H 2.04 . 2 105 . 19 LYS HG2 H 1.57 . 2 106 . 19 LYS HG3 H 1.71 . 2 107 . 19 LYS N N 118.9 . 1 108 . 20 ALA H H 7.37 . 1 109 . 20 ALA HA H 4.2 . 1 110 . 20 ALA HB H 1.52 . 1 111 . 20 ALA N N 127.5 . 1 112 . 21 ASP H H 8.83 . 1 113 . 21 ASP HA H 4.85 . 1 114 . 21 ASP HB2 H 2.73 . 2 115 . 21 ASP HB3 H 2.87 . 2 116 . 21 ASP N N 120.1 . 1 117 . 22 ASN H H 7.73 . 1 118 . 22 ASN HA H 5.01 . 1 119 . 22 ASN HB2 H 2.95 . 2 120 . 22 ASN HB3 H 3.04 . 2 121 . 22 ASN N N 116.4 . 1 122 . 23 ALA H H 9.13 . 1 123 . 23 ALA HA H 3.83 . 1 124 . 23 ALA HB H 1.55 . 1 125 . 23 ALA N N 126.1 . 1 126 . 24 ALA H H 8.53 . 1 127 . 24 ALA HA H 4.09 . 1 128 . 24 ALA HB H 1.54 . 1 129 . 24 ALA N N 125.8 . 1 130 . 25 GLN H H 8.16 . 1 131 . 25 GLN HA H 4.19 . 1 132 . 25 GLN HB2 H 2.4 . 1 133 . 25 GLN HB3 H 2.4 . 1 134 . 25 GLN HG2 H 1.95 . 2 135 . 25 GLN HG3 H 2.67 . 2 136 . 25 GLN NE2 N 114.9 . 1 137 . 25 GLN HE21 H 7.16 . 2 138 . 25 GLN HE22 H 7.47 . 2 139 . 25 GLN N N 121.1 . 1 140 . 26 VAL H H 7.26 . 1 141 . 26 VAL HA H 3.55 . 1 142 . 26 VAL HB H 2.22 . 1 143 . 26 VAL HG1 H .94 . 2 144 . 26 VAL HG2 H 1.11 . 2 145 . 26 VAL N N 121.9 . 1 146 . 27 LYS H H 8.86 . 1 147 . 27 LYS HA H 3.78 . 1 148 . 27 LYS HB2 H 1.83 . 2 149 . 27 LYS HB3 H 2.03 . 2 150 . 27 LYS HG2 H 1.34 . 2 151 . 27 LYS HG3 H 1.37 . 2 152 . 27 LYS HD2 H 1.69 . 1 153 . 27 LYS HD3 H 1.69 . 1 154 . 27 LYS HE2 H 2.97 . 1 155 . 27 LYS HE3 H 2.97 . 1 156 . 27 LYS N N 123.3 . 1 157 . 28 ASP H H 8.31 . 1 158 . 28 ASP HA H 4.4 . 1 159 . 28 ASP HB2 H 2.73 . 2 160 . 28 ASP HB3 H 2.85 . 2 161 . 28 ASP N N 124.5 . 1 162 . 29 ALA H H 7.64 . 1 163 . 29 ALA HA H 4.25 . 1 164 . 29 ALA HB H 1.63 . 1 165 . 29 ALA N N 125.3 . 1 166 . 30 LEU H H 8.63 . 1 167 . 30 LEU HA H 4.18 . 1 168 . 30 LEU HB2 H 2.14 . 1 169 . 30 LEU HB3 H 2.14 . 1 170 . 30 LEU HG H 1.35 . 1 171 . 30 LEU HD1 H .74 . 2 172 . 30 LEU HD2 H .99 . 2 173 . 30 LEU N N 121.8 . 1 174 . 31 THR H H 8.42 . 1 175 . 31 THR HA H 3.82 . 1 176 . 31 THR HB H 4.53 . 1 177 . 31 THR HG2 H 1.34 . 1 178 . 31 THR N N 120.3 . 1 179 . 32 LYS H H 7.76 . 1 180 . 32 LYS HA H 4.15 . 1 181 . 32 LYS HB2 H 1.68 . 2 182 . 32 LYS HB3 H 1.78 . 2 183 . 32 LYS N N 126.8 . 1 184 . 33 MET H H 8.5 . 1 185 . 33 MET HA H 3.78 . 1 186 . 33 MET HB2 H 2.45 . 1 187 . 33 MET HB3 H 2.45 . 1 188 . 33 MET HG2 H 2.21 . 1 189 . 33 MET HG3 H 2.21 . 1 190 . 33 MET N N 122.9 . 1 191 . 34 ARG H H 8.7 . 1 192 . 34 ARG HA H 3.7 . 1 193 . 34 ARG HB2 H 2.08 . 1 194 . 34 ARG HB3 H 2.08 . 1 195 . 34 ARG HG2 H 1.95 . 1 196 . 34 ARG HG3 H 1.95 . 1 197 . 34 ARG N N 124.6 . 1 198 . 35 ALA H H 7.3 . 1 199 . 35 ALA HA H 4.13 . 1 200 . 35 ALA HB H 1.56 . 1 201 . 35 ALA N N 121.4 . 1 202 . 36 ALA H H 7.74 . 1 203 . 36 ALA HA H 4.2 . 1 204 . 36 ALA HB H 1.56 . 1 205 . 36 ALA N N 124.6 . 1 206 . 37 ALA H H 8.6 . 1 207 . 37 ALA HA H 3.92 . 1 208 . 37 ALA HB H 1.54 . 1 209 . 37 ALA N N 124.4 . 1 210 . 38 LEU H H 7.86 . 1 211 . 38 LEU HA H 3.98 . 1 212 . 38 LEU HB2 H 1.88 . 1 213 . 38 LEU HB3 H 1.88 . 1 214 . 38 LEU HD1 H .94 . 1 215 . 38 LEU HD2 H .94 . 1 216 . 38 LEU N N 119.9 . 1 217 . 39 ASP H H 7.82 . 1 218 . 39 ASP HA H 4.42 . 1 219 . 39 ASP HB2 H 2.68 . 2 220 . 39 ASP HB3 H 2.73 . 2 221 . 39 ASP N N 123.7 . 1 222 . 40 ALA H H 8.38 . 1 223 . 40 ALA HA H 3.82 . 1 224 . 40 ALA HB H .94 . 1 225 . 40 ALA N N 127.6 . 1 226 . 41 GLN H H 7.09 . 1 227 . 41 GLN HA H 3.36 . 1 228 . 41 GLN HB2 H 2.2 . 2 229 . 41 GLN HB3 H 1.79 . 2 230 . 41 GLN HG2 H 2.48 . 1 231 . 41 GLN HG3 H 2.48 . 1 232 . 41 GLN N N 116.9 . 1 233 . 42 LYS H H 7.12 . 1 234 . 42 LYS HA H 4.33 . 1 235 . 42 LYS HB2 H 1.91 . 2 236 . 42 LYS HB3 H 2.08 . 2 237 . 42 LYS HG2 H 1.54 . 2 238 . 42 LYS HG3 H 1.73 . 2 239 . 42 LYS N N 118.1 . 1 240 . 43 ALA H H 7.83 . 1 241 . 43 ALA HA H 4.45 . 1 242 . 43 ALA HB H 1.61 . 1 243 . 43 ALA N N 127.7 . 1 244 . 44 THR H H 8.21 . 1 245 . 44 THR HA H 4.37 . 1 246 . 44 THR HB H 3.95 . 1 247 . 44 THR HG2 H 1.14 . 1 248 . 44 THR N N 118.1 . 1 249 . 46 PRO HA H 4.35 . 1 250 . 46 PRO HB2 H 2.03 . 2 251 . 46 PRO HB3 H 2.44 . 2 252 . 46 PRO HG2 H 2.16 . 1 253 . 46 PRO HG3 H 2.16 . 1 254 . 46 PRO HD2 H 3.81 . 1 255 . 46 PRO HD3 H 3.81 . 1 256 . 47 LYS H H 8.59 . 1 257 . 47 LYS HA H 4.23 . 1 258 . 47 LYS HB2 H 1.94 . 2 259 . 47 LYS HB3 H 2 . 2 260 . 47 LYS N N 118.6 . 1 261 . 48 LEU H H 7.89 . 1 262 . 48 LEU HA H 4.55 . 1 263 . 48 LEU HB2 H 1.69 . 1 264 . 48 LEU HB3 H 1.69 . 1 265 . 48 LEU HG H 1.46 . 1 266 . 48 LEU HD1 H .72 . 2 267 . 48 LEU HD2 H .83 . 2 268 . 48 LEU N N 121.8 . 1 269 . 49 GLU HA H 3.98 . 1 270 . 50 ASP H H 8.5 . 1 271 . 50 ASP HA H 4.7 . 1 272 . 50 ASP HB2 H 2.83 . 1 273 . 50 ASP HB3 H 2.83 . 1 274 . 50 ASP N N 120.2 . 1 275 . 51 LYS H H 7.77 . 1 276 . 51 LYS HA H 4.55 . 1 277 . 51 LYS HB2 H 2.02 . 1 278 . 51 LYS HB3 H 2.02 . 1 279 . 51 LYS N N 123.6 . 1 280 . 52 SER H H 8.85 . 1 281 . 52 SER HA H 4.79 . 1 282 . 52 SER HB2 H 4.23 . 2 283 . 52 SER HB3 H 4.01 . 2 284 . 52 SER N N 121.1 . 1 285 . 54 ASP H H 8.05 . 1 286 . 54 ASP HA H 4.83 . 1 287 . 54 ASP HB2 H 2.66 . 2 288 . 54 ASP HB3 H 2.84 . 2 289 . 54 ASP N N 117.8 . 1 290 . 55 SER H H 7.9 . 1 291 . 55 SER HA H 4.64 . 1 292 . 55 SER N N 120.5 . 1 293 . 56 PRO HA H 4 . 1 294 . 57 GLU H H 9.62 . 1 295 . 57 GLU HA H 4.22 . 1 296 . 57 GLU HB2 H 2.08 . 1 297 . 57 GLU HB3 H 2.08 . 1 298 . 57 GLU HG2 H 2.47 . 1 299 . 57 GLU HG3 H 2.47 . 1 300 . 57 GLU N N 120.5 . 1 301 . 58 MET H H 7.84 . 1 302 . 58 MET HA H 4.8 . 1 303 . 58 MET N N 123.3 . 1 304 . 59 LYS H H 8.68 . 1 305 . 59 LYS HA H 4.11 . 1 306 . 59 LYS HB2 H 1.68 . 2 307 . 59 LYS HB3 H 1.97 . 2 308 . 59 LYS N N 124.7 . 1 309 . 60 ASP H H 8.52 . 1 310 . 60 ASP HA H 4.64 . 1 311 . 60 ASP HB2 H 2.94 . 1 312 . 60 ASP HB3 H 2.94 . 1 313 . 60 ASP N N 124.2 . 1 314 . 61 PHE H H 8.23 . 1 315 . 61 PHE HA H 4.4 . 1 316 . 61 PHE HB2 H 3.29 . 2 317 . 61 PHE HB3 H 3.49 . 2 318 . 61 PHE HD1 H 7.23 . 1 319 . 61 PHE HD2 H 7.23 . 1 320 . 61 PHE HE1 H 7.49 . 1 321 . 61 PHE HE2 H 7.49 . 1 322 . 61 PHE HZ H 7.29 . 1 323 . 61 PHE N N 125.4 . 1 324 . 62 ARG H H 8.73 . 1 325 . 62 ARG HA H 4.05 . 1 326 . 62 ARG HB2 H 2.19 . 2 327 . 62 ARG HB3 H 2.39 . 2 328 . 62 ARG HG2 H 2.05 . 1 329 . 62 ARG HG3 H 2.05 . 1 330 . 62 ARG N N 121.3 . 1 331 . 63 HIS H H 8.85 . 1 332 . 63 HIS HA H 4.71 . 1 333 . 63 HIS HB2 H 3.57 . 2 334 . 63 HIS HB3 H 3.62 . 2 335 . 63 HIS HD2 H 7.49 . 1 336 . 63 HIS HE1 H 8.77 . 1 337 . 63 HIS N N 122.9 . 1 338 . 64 GLY H H 8.1 . 1 339 . 64 GLY HA2 H 3.3 . 2 340 . 64 GLY HA3 H 3.64 . 2 341 . 64 GLY N N 109.5 . 1 342 . 65 PHE H H 7.1 . 1 343 . 65 PHE HA H 4.2 . 1 344 . 65 PHE HB2 H 2.8 . 2 345 . 65 PHE HB3 H 3.02 . 2 346 . 65 PHE HD1 H 6.94 . 1 347 . 65 PHE HD2 H 6.94 . 1 348 . 65 PHE HE1 H 6.69 . 1 349 . 65 PHE HE2 H 6.69 . 1 350 . 65 PHE HZ H 7.04 . 1 351 . 65 PHE N N 121.2 . 1 352 . 66 ASP H H 7.7 . 1 353 . 66 ASP HA H 4.5 . 1 354 . 66 ASP HB2 H 2.76 . 2 355 . 66 ASP HB3 H 2.89 . 2 356 . 66 ASP N N 125.5 . 1 357 . 67 ILE H H 7.66 . 1 358 . 67 ILE HA H 3.69 . 1 359 . 67 ILE HB H 1.85 . 1 360 . 67 ILE HG12 H .95 . 2 361 . 67 ILE HG13 H 1.2 . 2 362 . 67 ILE HG2 H .84 . 1 363 . 67 ILE HD1 H .7 . 1 364 . 67 ILE N N 124 . 1 365 . 68 LEU H H 7.46 . 1 366 . 68 LEU HA H 4.26 . 1 367 . 68 LEU HB2 H 1.72 . 2 368 . 68 LEU HB3 H 1.82 . 2 369 . 68 LEU HD1 H .93 . 1 370 . 68 LEU HD2 H .93 . 1 371 . 68 LEU N N 124.8 . 1 372 . 69 VAL H H 8.78 . 1 373 . 69 VAL HA H 3.48 . 1 374 . 69 VAL HB H 2.25 . 1 375 . 69 VAL HG1 H .99 . 2 376 . 69 VAL HG2 H 1.12 . 2 377 . 69 VAL N N 122.6 . 1 378 . 70 GLY H H 7.94 . 1 379 . 70 GLY HA2 H 3.94 . 2 380 . 70 GLY HA3 H 3.96 . 2 381 . 70 GLY N N 109.7 . 1 382 . 71 GLN H H 7.99 . 1 383 . 71 GLN HA H 4.23 . 1 384 . 71 GLN HB2 H 2.52 . 2 385 . 71 GLN HB3 H 1.99 . 2 386 . 71 GLN HG2 H 2.38 . 1 387 . 71 GLN HG3 H 2.38 . 1 388 . 71 GLN NE2 N 111.5 . 1 389 . 71 GLN HE21 H 6.26 . 2 390 . 71 GLN HE22 H 7.37 . 2 391 . 71 GLN N N 124.8 . 1 392 . 72 ILE H H 8.77 . 1 393 . 72 ILE HA H 3.56 . 1 394 . 72 ILE HB H 2.13 . 1 395 . 72 ILE HG2 H 1.01 . 1 396 . 72 ILE HD1 H .75 . 1 397 . 72 ILE N N 127.2 . 1 398 . 73 ASP H H 9.09 . 1 399 . 73 ASP HA H 4.65 . 1 400 . 73 ASP HB2 H 2.65 . 2 401 . 73 ASP HB3 H 2.96 . 2 402 . 73 ASP N N 125.6 . 1 403 . 74 ASP H H 8.21 . 1 404 . 74 ASP HA H 4.53 . 1 405 . 74 ASP HB2 H 2.73 . 2 406 . 74 ASP HB3 H 2.9 . 2 407 . 74 ASP N N 126.2 . 1 408 . 75 ALA H H 7.96 . 1 409 . 75 ALA HA H 4.13 . 1 410 . 75 ALA HB H 1.54 . 1 411 . 75 ALA N N 127.1 . 1 412 . 76 LEU H H 9.27 . 1 413 . 76 LEU HA H 3.88 . 1 414 . 76 LEU HB2 H 1.7 . 2 415 . 76 LEU HB3 H 2.04 . 2 416 . 76 LEU HG H 1.34 . 1 417 . 76 LEU HD1 H .74 . 2 418 . 76 LEU HD2 H .99 . 2 419 . 76 LEU N N 125.2 . 1 420 . 77 LYS H H 7.94 . 1 421 . 77 LYS HA H 4.09 . 1 422 . 77 LYS HB2 H 2.05 . 2 423 . 77 LYS HB3 H 1.64 . 2 424 . 77 LYS HG2 H 1.77 . 1 425 . 77 LYS HG3 H 1.77 . 1 426 . 77 LYS N N 124.2 . 1 427 . 78 LEU H H 7.12 . 1 428 . 78 LEU HA H 4.15 . 1 429 . 78 LEU HB2 H 2.05 . 1 430 . 78 LEU HB3 H 2.05 . 1 431 . 78 LEU HD1 H .83 . 1 432 . 78 LEU HD2 H .83 . 1 433 . 78 LEU N N 121.3 . 1 434 . 79 ALA H H 8.58 . 1 435 . 79 ALA HA H 3.73 . 1 436 . 79 ALA HB H 1.4 . 1 437 . 79 ALA N N 125.9 . 1 438 . 80 ASN H H 9.01 . 1 439 . 80 ASN HA H 4.52 . 1 440 . 80 ASN HB2 H 2.88 . 2 441 . 80 ASN HB3 H 3.04 . 2 442 . 80 ASN ND2 N 114.7 . 1 443 . 80 ASN HD21 H 6.95 . 2 444 . 80 ASN HD22 H 7.46 . 2 445 . 80 ASN N N 122.1 . 1 446 . 81 GLU H H 7.57 . 1 447 . 81 GLU HA H 4.48 . 1 448 . 81 GLU HB2 H 2.26 . 2 449 . 81 GLU HB3 H 2.68 . 2 450 . 81 GLU HG2 H 2.48 . 1 451 . 81 GLU HG3 H 2.48 . 1 452 . 81 GLU N N 121.3 . 1 453 . 82 GLY H H 7.98 . 1 454 . 82 GLY HA2 H 3.61 . 2 455 . 82 GLY HA3 H 4.34 . 2 456 . 82 GLY N N 110.8 . 1 457 . 83 LYS H H 7.99 . 1 458 . 83 LYS HA H 4.55 . 1 459 . 83 LYS HB2 H 1.83 . 1 460 . 83 LYS HB3 H 1.83 . 1 461 . 83 LYS HG2 H 1.35 . 1 462 . 83 LYS HG3 H 1.35 . 1 463 . 83 LYS N N 127.6 . 1 464 . 84 VAL H H 7.73 . 1 465 . 84 VAL HA H 3.28 . 1 466 . 84 VAL HB H 2.1 . 1 467 . 84 VAL HG1 H .8 . 2 468 . 84 VAL HG2 H .92 . 2 469 . 84 VAL N N 125.8 . 1 470 . 85 LYS H H 8.64 . 1 471 . 85 LYS HA H 4.51 . 1 472 . 85 LYS HB2 H 1.94 . 2 473 . 85 LYS HB3 H 1.83 . 2 474 . 85 LYS N N 123.6 . 1 475 . 86 GLU H H 9.45 . 1 476 . 86 GLU HA H 4.1 . 1 477 . 86 GLU HB2 H 2.09 . 2 478 . 86 GLU HB3 H 2.13 . 2 479 . 86 GLU HG2 H 2.38 . 2 480 . 86 GLU HG3 H 2.58 . 2 481 . 86 GLU N N 125.1 . 1 482 . 87 ALA H H 8.59 . 1 483 . 87 ALA HA H 4.12 . 1 484 . 87 ALA HB H 1.52 . 1 485 . 87 ALA N N 128.2 . 1 486 . 88 GLN H H 8.77 . 1 487 . 88 GLN HA H 3.78 . 1 488 . 88 GLN HB2 H 2.54 . 1 489 . 88 GLN HB3 H 2.54 . 1 490 . 88 GLN N N 120.5 . 1 491 . 89 ALA H H 8.21 . 1 492 . 89 ALA HA H 4.23 . 1 493 . 89 ALA HB H 1.56 . 1 494 . 89 ALA N N 126.2 . 1 495 . 90 ALA H H 8.16 . 1 496 . 90 ALA HA H 4.2 . 1 497 . 90 ALA HB H 1.55 . 1 498 . 90 ALA N N 125.3 . 1 499 . 91 ALA H H 8.42 . 1 500 . 91 ALA HA H 4 . 1 501 . 91 ALA HB H 1.54 . 1 502 . 91 ALA N N 124.6 . 1 503 . 92 GLU H H 7.8 . 1 504 . 92 GLU HA H 4.14 . 1 505 . 92 GLU N N 119.6 . 1 506 . 93 GLN H H 7.53 . 1 507 . 93 GLN HA H 4.25 . 1 508 . 93 GLN HB2 H 2.29 . 2 509 . 93 GLN HB3 H 2.16 . 2 510 . 93 GLN HG2 H 2.51 . 2 511 . 93 GLN HG3 H 2.57 . 2 512 . 93 GLN NE2 N 116 . 1 513 . 93 GLN HE21 H 6.99 . 2 514 . 93 GLN HE22 H 7.61 . 2 515 . 93 GLN N N 120.3 . 1 516 . 94 LEU H H 7.84 . 1 517 . 94 LEU HA H 4.19 . 1 518 . 94 LEU HB2 H 2.01 . 1 519 . 94 LEU HB3 H 2.01 . 1 520 . 94 LEU N N 122.9 . 1 521 . 95 LYS H H 7.78 . 1 522 . 95 LYS HA H 4 . 1 523 . 95 LYS HB2 H 1.98 . 1 524 . 95 LYS HB3 H 1.98 . 1 525 . 95 LYS N N 121.6 . 1 526 . 96 THR H H 7.72 . 1 527 . 96 THR HA H 4.22 . 1 528 . 96 THR HB H 4.44 . 1 529 . 96 THR HG2 H 1.28 . 1 530 . 96 THR N N 116.4 . 1 531 . 97 THR H H 7.82 . 1 532 . 97 THR HA H 4.12 . 1 533 . 97 THR HB H 4.24 . 1 534 . 97 THR HG2 H 1.16 . 1 535 . 97 THR N N 121.6 . 1 536 . 98 ARG H H 8.46 . 1 537 . 98 ARG HA H 4.12 . 1 538 . 98 ARG HB2 H 1.82 . 2 539 . 98 ARG HB3 H 1.97 . 2 540 . 98 ARG N N 125.1 . 1 541 . 99 ASN H H 8.37 . 1 542 . 99 ASN HA H 4.58 . 1 543 . 99 ASN HB2 H 2.92 . 1 544 . 99 ASN HB3 H 2.92 . 1 545 . 99 ASN N N 122 . 1 546 . 100 ALA H H 8.07 . 1 547 . 100 ALA HA H 4.14 . 1 548 . 100 ALA HB H 1.3 . 1 549 . 100 ALA N N 126.3 . 1 550 . 101 TYR H H 8.15 . 1 551 . 101 TYR HA H 4.39 . 1 552 . 101 TYR HB2 H 2.92 . 2 553 . 101 TYR HB3 H 3.18 . 2 554 . 101 TYR HD1 H 7.16 . 1 555 . 101 TYR HD2 H 7.16 . 1 556 . 101 TYR HE1 H 6.74 . 1 557 . 101 TYR HE2 H 6.74 . 1 558 . 101 TYR N N 120.6 . 1 559 . 102 HIS H H 8.25 . 1 560 . 102 HIS HA H 4.56 . 1 561 . 102 HIS HB2 H 3.38 . 2 562 . 102 HIS HB3 H 3.42 . 2 563 . 102 HIS HD2 H 7.34 . 1 564 . 102 HIS HE1 H 8.44 . 1 565 . 102 HIS N N 122.8 . 1 566 . 103 GLN H H 8.2 . 1 567 . 103 GLN HA H 4.14 . 1 568 . 103 GLN HB2 H 2.07 . 1 569 . 103 GLN HB3 H 2.07 . 1 570 . 103 GLN HG2 H 2.37 . 1 571 . 103 GLN HG3 H 2.37 . 1 572 . 103 GLN NE2 N 114.7 . 1 573 . 103 GLN HE21 H 6.63 . 2 574 . 103 GLN HE22 H 7.44 . 2 575 . 103 GLN N N 121.9 . 1 576 . 104 LYS H H 7.84 . 1 577 . 104 LYS HA H 4.13 . 1 578 . 104 LYS HB2 H 1.49 . 1 579 . 104 LYS HB3 H 1.49 . 1 580 . 104 LYS HG2 H 1.21 . 1 581 . 104 LYS HG3 H 1.21 . 1 582 . 104 LYS HD2 H 1.58 . 1 583 . 104 LYS HD3 H 1.58 . 1 584 . 104 LYS HE2 H 2.9 . 1 585 . 104 LYS HE3 H 2.9 . 1 586 . 104 LYS N N 122.9 . 1 587 . 105 TYR H H 8.09 . 1 588 . 105 TYR HA H 4.74 . 1 589 . 105 TYR HB2 H 2.85 . 2 590 . 105 TYR HB3 H 3.28 . 2 591 . 105 TYR HD1 H 7.21 . 1 592 . 105 TYR HD2 H 7.21 . 1 593 . 105 TYR HE1 H 6.91 . 1 594 . 105 TYR HE2 H 6.91 . 1 595 . 105 TYR N N 122.1 . 1 596 . 106 ARG H H 7.59 . 1 597 . 106 ARG HA H 4.21 . 1 598 . 106 ARG HB2 H 1.61 . 2 599 . 106 ARG HB3 H 1.74 . 2 600 . 106 ARG HG2 H 1.81 . 1 601 . 106 ARG HG3 H 1.81 . 1 602 . 106 ARG NE N 89.1 . 1 603 . 106 ARG HD2 H 3.15 . 1 604 . 106 ARG HD3 H 3.15 . 1 605 . 106 ARG HE H 7.35 . 1 606 . 106 ARG N N 129.2 . 1 stop_ save_