data_7125 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Chemical Shifts Assignments of Human Adult Hemoglobin in the Carbonmonoxy Form ; _BMRB_accession_number 7125 _BMRB_flat_file_name bmr7125.str _Entry_type original _Submission_date 2006-05-22 _Accession_date 2006-05-22 _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 Fan Jing-song . . 2 Yang Daiwen . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 2 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 1261 "13C chemical shifts" 856 "15N chemical shifts" 270 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2006-11-13 original author . stop_ _Original_release_date 2006-11-13 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title 'A new strategy for structure determination of large proteins in solution without deuteration' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 17060917 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Xu Y. . . 2 Zheng Y. . . 3 Fan J.S. . . 4 Yang D. . . stop_ _Journal_abbreviation 'Nature Methods' _Journal_volume 3 _Journal_issue 11 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 931 _Page_last 937 _Year 2006 _Details . save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name 'HbCO A' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'globin subunit alpha, 1' $globin_subunit_alpha 'globin subunit alpha, 2' $globin_subunit_alpha 'globin subunit beta, 1' $globin_subunit_beta 'globin subunit beta, 2' $globin_subunit_beta 'HEME 1' $entity_HEM_red 'HEME 2' $entity_HEM_red 'HEME 3' $entity_HEM_red 'HEME 4' $entity_HEM_red stop_ _System_molecular_weight 65336 _System_physical_state native _System_oligomer_state 'protein-ligand system' _System_paramagnetic no _System_thiol_state 'all free' loop_ _Biological_function 'Oxygen transportation' stop_ _Database_query_date . _Details 'human normal adult hemoglobin carbonmonoxy form' save_ ######################## # Monomeric polymers # ######################## save_globin_subunit_alpha _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'alpha chain' _Molecular_mass . _Mol_thiol_state 'all free' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 141 _Mol_residue_sequence ; VLSPADKTNVKAAWGKVGAH AGEYGAEALERMFLSFPTTK TYFPHFDLSHGSAQVKGHGK KVADALTNAVAHVDDMPNAL SALSDLHAHKLRVDPVNFKL LSHCLLVTLAAHLPAEFTPA VHASLDKFLASVSTVLTSKY R ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 1 VAL 2 2 LEU 3 3 SER 4 4 PRO 5 5 ALA 6 6 ASP 7 7 LYS 8 8 THR 9 9 ASN 10 10 VAL 11 11 LYS 12 12 ALA 13 13 ALA 14 14 TRP 15 15 GLY 16 16 LYS 17 17 VAL 18 18 GLY 19 19 ALA 20 20 HIS 21 21 ALA 22 22 GLY 23 23 GLU 24 24 TYR 25 25 GLY 26 26 ALA 27 27 GLU 28 28 ALA 29 29 LEU 30 30 GLU 31 31 ARG 32 32 MET 33 33 PHE 34 34 LEU 35 35 SER 36 36 PHE 37 37 PRO 38 38 THR 39 39 THR 40 40 LYS 41 41 THR 42 42 TYR 43 43 PHE 44 44 PRO 45 45 HIS 46 46 PHE 47 47 ASP 48 48 LEU 49 49 SER 50 50 HIS 51 51 GLY 52 52 SER 53 53 ALA 54 54 GLN 55 55 VAL 56 56 LYS 57 57 GLY 58 58 HIS 59 59 GLY 60 60 LYS 61 61 LYS 62 62 VAL 63 63 ALA 64 64 ASP 65 65 ALA 66 66 LEU 67 67 THR 68 68 ASN 69 69 ALA 70 70 VAL 71 71 ALA 72 72 HIS 73 73 VAL 74 74 ASP 75 75 ASP 76 76 MET 77 77 PRO 78 78 ASN 79 79 ALA 80 80 LEU 81 81 SER 82 82 ALA 83 83 LEU 84 84 SER 85 85 ASP 86 86 LEU 87 87 HIS 88 88 ALA 89 89 HIS 90 90 LYS 91 91 LEU 92 92 ARG 93 93 VAL 94 94 ASP 95 95 PRO 96 96 VAL 97 97 ASN 98 98 PHE 99 99 LYS 100 100 LEU 101 101 LEU 102 102 SER 103 103 HIS 104 104 CYS 105 105 LEU 106 106 LEU 107 107 VAL 108 108 THR 109 109 LEU 110 110 ALA 111 111 ALA 112 112 HIS 113 113 LEU 114 114 PRO 115 115 ALA 116 116 GLU 117 117 PHE 118 118 THR 119 119 PRO 120 120 ALA 121 121 VAL 122 122 HIS 123 123 ALA 124 124 SER 125 125 LEU 126 126 ASP 127 127 LYS 128 128 PHE 129 129 LEU 130 130 ALA 131 131 SER 132 132 VAL 133 133 SER 134 134 THR 135 135 VAL 136 136 LEU 137 137 THR 138 138 SER 139 139 LYS 140 140 TYR 141 141 ARG stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-01-28 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 BMRB 1053 "hemoglobin A beta chain" 100.00 146 100.00 100.00 6.17e-101 BMRB 1102 "hemoglobin A beta chain" 100.00 146 100.00 100.00 6.17e-101 BMRB 2006 "hemoglobin A beta chain" 100.00 146 100.00 100.00 6.17e-101 BMRB 2708 "hemoglobin A beta chain" 100.00 146 100.00 100.00 6.17e-101 BMRB 2710 "hemoglobin A beta chain" 100.00 146 100.00 100.00 6.17e-101 BMRB 5856 beta_subunit 100.00 146 100.00 100.00 6.17e-101 BMRB 6230 bHb 100.00 146 100.00 100.00 6.17e-101 BMRB 6683 human_normal_adult_hemoglobin_beta_chain_in_deoxy_form 100.00 146 100.00 100.00 6.17e-101 BMRB 908 "hemoglobin A beta chain" 100.00 146 100.00 100.00 6.17e-101 PDB 1A00 "Hemoglobin (Val Beta1 Met, Trp Beta37 Tyr) Mutant" 100.00 146 98.63 100.00 1.02e-99 PDB 1A01 "Hemoglobin (Val Beta1 Met, Trp Beta37 Ala) Mutant" 100.00 146 98.63 99.32 4.99e-99 PDB 1A0U "Hemoglobin (Val Beta1 Met) Mutant" 100.00 146 99.32 100.00 1.37e-100 PDB 1A0Z "Hemoglobin (Val Beta1 Met) Mutant" 100.00 146 99.32 100.00 1.37e-100 PDB 1A3N "Deoxy Human Hemoglobin" 100.00 146 100.00 100.00 6.17e-101 PDB 1A3O "Artificial Mutant (Alpha Y42h) Of Deoxy Hemoglobin" 100.00 146 100.00 100.00 6.17e-101 PDB 1ABW "Deoxy Rhb1.1 (Recombinant Hemoglobin)" 100.00 146 98.63 99.32 1.23e-99 PDB 1ABY "Cyanomet Rhb1.1 (Recombinant Hemoglobin)" 100.00 146 98.63 99.32 1.23e-99 PDB 1AJ9 "R-State Human Carbonmonoxyhemoglobin Alpha-A53s" 100.00 146 100.00 100.00 6.17e-101 PDB 1B86 "Human Deoxyhaemoglobin-2,3-Diphosphoglycerate Complex" 100.00 146 100.00 100.00 6.17e-101 PDB 1BAB "Hemoglobin Thionville: An Alpha-Chain Variant With A Substitution Of A Glutamate For Valine At Na-1 And Having An Acetylated Me" 100.00 146 100.00 100.00 6.17e-101 PDB 1BBB "A Third Quaternary Structure Of Human Hemoglobin A At 1.7-angstroms Resolution" 100.00 146 100.00 100.00 6.17e-101 PDB 1BIJ "Crosslinked, Deoxy Human Hemoglobin A" 100.00 146 100.00 100.00 6.17e-101 PDB 1BUW "Crystal Structure Of S-Nitroso-Nitrosyl Human Hemoglobin A" 100.00 146 99.32 99.32 1.91e-99 PDB 1BZ0 "Hemoglobin A (Human, Deoxy, High Salt)" 100.00 146 100.00 100.00 6.17e-101 PDB 1BZ1 "Hemoglobin (Alpha + Met) Variant" 100.00 146 100.00 100.00 6.17e-101 PDB 1BZZ "Hemoglobin (Alpha V1m) Mutant" 100.00 146 100.00 100.00 6.17e-101 PDB 1C7B "Deoxy Rhb1.0 (Recombinant Hemoglobin)" 100.00 146 98.63 99.32 1.23e-99 PDB 1C7C "Deoxy Rhb1.1 (Recombinant Hemoglobin)" 100.00 146 98.63 99.32 1.23e-99 PDB 1C7D "Deoxy Rhb1.2 (Recombinant Hemoglobin)" 100.00 146 98.63 99.32 1.23e-99 PDB 1CBL "The 1.9 Angstrom Structure Of Deoxy-Beta4 Hemoglobin: Analysis Of The Partitioning Of Quaternary-Associated And Ligand-Induced " 100.00 146 100.00 100.00 6.17e-101 PDB 1CBM "The 1.8 Angstrom Structure Of Carbonmonoxy-Beta4 Hemoglobin: Analysis Of A Homotetramer With The R Quaternary Structure Of Liga" 100.00 146 100.00 100.00 6.17e-101 PDB 1CLS "Cross-Linked Human Hemoglobin Deoxy" 100.00 146 100.00 100.00 6.17e-101 PDB 1CMY "The Mutation Beta99 Asp-Tyr Stabilizes Y-A New, Composite Quaternary State Of Human Hemoglobin" 100.00 146 99.32 99.32 1.44e-99 PDB 1COH "Structure Of Haemoglobin In The Deoxy Quaternary State With Ligand Bound At The Alpha Haems" 100.00 146 100.00 100.00 6.17e-101 PDB 1DKE "Ni Beta Heme Human Hemoglobin" 100.00 146 100.00 100.00 6.17e-101 PDB 1DXT "High-Resolution X-Ray Study Of Deoxy Recombinant Human Hemoglobins Synthesized From Beta-Globins Having Mutated Amino Termini" 100.00 147 100.00 100.00 5.85e-101 PDB 1DXU "High-Resolution X-Ray Study Of Deoxy Recombinant Human Hemoglobins Synthesized From Beta-Globins Having Mutated Amino Termini" 100.00 146 99.32 100.00 1.37e-100 PDB 1DXV "High-resolution X-ray Study Of Deoxy Recombinant Human Hemoglobins Synthesized From Beta-globins Having Mutated Amino Termini" 99.32 146 100.00 100.00 1.97e-100 PDB 1FN3 "Crystal Structure Of Nickel Reconstituted Hemoglobin-A Case For Permanent, T-State Hemoglobin" 100.00 146 100.00 100.00 6.17e-101 PDB 1G9V "High Resolution Crystal Structure Of Deoxy Hemoglobin Complexed With A Potent Allosteric Effector" 100.00 146 100.00 100.00 6.17e-101 PDB 1GBU "Deoxy (Beta-(C93a,C112g)) Human Hemoglobin" 100.00 146 98.63 98.63 3.20e-98 PDB 1GBV "(Alpha-Oxy, Beta-(C112g)deoxy) T-State Human Hemoglobin" 100.00 146 99.32 99.32 2.92e-99 PDB 1GLI "Deoxyhemoglobin T38w (alpha Chains), V1g (alpha And Beta Chains)" 100.00 146 99.32 100.00 1.37e-100 PDB 1GZX "Oxy T State Haemoglobin: Oxygen Bound At All Four Haems" 100.00 146 100.00 100.00 6.17e-101 PDB 1HAB "Crosslinked Haemoglobin" 100.00 146 100.00 100.00 6.17e-101 PDB 1HAC "Crosslinked Haemoglobin" 100.00 146 100.00 100.00 6.17e-101 PDB 1HBA "High-Resolution X-Ray Study Of Deoxyhemoglobin Rothschild 37beta Trp-> Arg: A Mutation That Creates An Intersubunit Chloride-Bi" 100.00 146 99.32 99.32 2.59e-99 PDB 1HBB "High-Resolution X-Ray Study Of Deoxyhemoglobin Rothschild 37beta Trp-> Arg: A Mutation That Creates An Intersubunit Chloride-Bi" 100.00 146 100.00 100.00 6.17e-101 PDB 1HBS "Refined Crystal Structure Of Deoxyhemoglobin S. I. Restrained Least-Squares Refinement At 3.0-Angstroms Resolution" 100.00 146 99.32 99.32 8.59e-100 PDB 1HCO "The Structure Of Human Carbonmonoxy Haemoglobin At 2.7 Angstroms Resolution" 100.00 146 100.00 100.00 6.17e-101 PDB 1HDB "Analysis Of The Crystal Structure, Molecular Modeling And Infrared Spectroscopy Of The Distal Beta-Heme Pocket Valine67(E11)-Th" 100.00 146 99.32 99.32 1.90e-100 PDB 1HGA "High Resolution Crystal Structures And Comparisons Of T State Deoxyhaemoglobin And Two Liganded T-state Haemoglobins: T(alpha-o" 100.00 146 100.00 100.00 6.17e-101 PDB 1HGB "High Resolution Crystal Structures And Comparisons Of T State Deoxyhaemoglobin And Two Liganded T-State Haemoglobins: T(Alpha-O" 100.00 146 100.00 100.00 6.17e-101 PDB 1HGC "High Resolution Crystal Structures And Comparisons Of T State Deoxyhaemoglobin And Two Liganded T-state Haemoglobins: T(alpha-o" 100.00 146 100.00 100.00 6.17e-101 PDB 1HHO "Structure Of Human Oxyhaemoglobin At 2.1 Angstroms Resolution" 100.00 146 100.00 100.00 6.17e-101 PDB 1IRD "Crystal Structure Of Human Carbonmonoxy-Haemoglobin At 1.25 A Resolution" 100.00 146 100.00 100.00 6.17e-101 PDB 1J3Y "Direct Observation Of Photolysis-Induced Tertiary Structural Changes In Human Hemoglobin; Crystal Structure Of Alpha(Fe)-Beta(N" 100.00 146 100.00 100.00 6.17e-101 PDB 1J3Z "Direct Observation Of Photolysis-Induced Tertiary Structural Changes In Human Haemoglobin; Crystal Structure Of Alpha(Fe-Co)-Be" 100.00 146 100.00 100.00 6.17e-101 PDB 1J40 "Direct Observation Of Photolysis-Induced Tertiary Structural Changes In Human Haemoglobin; Crystal Structure Of Alpha(Ni)-Beta(" 100.00 146 100.00 100.00 6.17e-101 PDB 1J41 "Direct Observation Of Photolysis-Induced Tertiary Structural Changes In Human Haemoglobin; Crystal Structure Of Alpha(Ni)-Beta(" 100.00 146 100.00 100.00 6.17e-101 PDB 1J7S "Crystal Structure Of Deoxy Hbalphayq, A Mutant Of Hba" 100.00 146 99.32 100.00 1.37e-100 PDB 1J7W "Crystal Structure Of Deoxy Hbbetayq, A Site Directed Mutant Of Hba" 100.00 146 97.95 98.63 4.57e-99 PDB 1J7Y "Crystal Structure Of Partially Ligated Mutant Of Hba" 100.00 146 97.95 98.63 4.57e-99 PDB 1JY7 "The Structure Of Human Methemoglobin. The Variation Of A Theme" 100.00 146 100.00 100.00 6.17e-101 PDB 1K0Y "X-ray Crystallographic Analyses Of Symmetrical Allosteric Effectors Of Hemoglobin. Compounds Designed To Link Primary And Secon" 100.00 146 100.00 100.00 6.17e-101 PDB 1K1K "Structure Of Mutant Human Carbonmonoxyhemoglobin C (beta E6k) At 2.0 Angstrom Resolution In Phosphate Buffer." 100.00 146 99.32 100.00 3.04e-100 PDB 1KD2 "Crystal Structure Of Human Deoxyhemoglobin In Absence Of Any Anions" 100.00 146 100.00 100.00 6.17e-101 PDB 1LFL "Deoxy Hemoglobin (90% Relative Humidity)" 100.00 146 100.00 100.00 6.17e-101 PDB 1LFQ "Oxy Hemoglobin (93% Relative Humidity)" 100.00 146 100.00 100.00 6.17e-101 PDB 1LFT "Oxy Hemoglobin (90% Relative Humidity)" 100.00 146 100.00 100.00 6.17e-101 PDB 1LFV "Oxy Hemoglobin (88% Relative Humidity)" 100.00 146 100.00 100.00 6.17e-101 PDB 1LFY "Oxy Hemoglobin (84% Relative Humidity)" 100.00 146 100.00 100.00 6.17e-101 PDB 1LFZ "Oxy Hemoglobin (25% Methanol)" 100.00 146 100.00 100.00 6.17e-101 PDB 1LJW "Crystal Structure Of Human Carbonmonoxy Hemoglobin At 2.16 A: A Snapshot Of The Allosteric Transition" 100.00 146 100.00 100.00 6.17e-101 PDB 1M9P "Crystalline Human Carbonmonoxy Hemoglobin C Exhibits The R2 Quaternary State At Neutral Ph In The Presence Of Polyethylene Glyc" 100.00 146 99.32 100.00 3.04e-100 PDB 1MKO "A Fourth Quaternary Structure Of Human Hemoglobin A At 2.18 A Resolution" 100.00 146 100.00 100.00 6.17e-101 PDB 1NEJ "Crystalline Human Carbonmonoxy Hemoglobin S (liganded Sickle Cell Hemoglobin) Exhibits The R2 Quaternary State At Neutral Ph In" 100.00 146 99.32 99.32 8.59e-100 PDB 1NIH "Structure Of Deoxy-Quaternary Haemoglobin With Liganded Beta Subunits" 100.00 146 100.00 100.00 6.17e-101 PDB 1NQP "Crystal Structure Of Human Hemoglobin E At 1.73 A Resolution" 100.00 146 99.32 100.00 3.04e-100 PDB 1O1I "Cyanomet Hemoglobin (a-gly-c:v1m,l29f,h58q; B,d:v1m,l106w)" 100.00 146 98.63 99.32 2.35e-99 PDB 1O1J "Deoxy Hemoglobin (a-gly-c:v1m,l29f,h58q; B,d:v1m,l106w)" 100.00 146 98.63 99.32 2.35e-99 PDB 1O1K "Deoxy Hemoglobin (A,C:v1m; B,D:v1m,V67w)" 100.00 146 98.63 99.32 2.89e-99 PDB 1O1L "Deoxy Hemoglobin (A-Gly-C:v1m,L29w,H58q; B,D:v1m)" 100.00 146 99.32 100.00 1.37e-100 PDB 1O1M "Deoxy Hemoglobin (a-glyglygly-c:v1m,l29f,h58q B,d:v1m,v67w)" 100.00 146 98.63 99.32 2.89e-99 PDB 1O1N "Deoxy Hemoglobin (A-Glyglygly-C:v1m,L29w; B,D:v1m)" 100.00 146 99.32 100.00 1.37e-100 PDB 1O1O "Deoxy Hemoglobin (A,C:v1m,V62l; B,D:v1m,V67l)" 100.00 146 98.63 100.00 4.13e-100 PDB 1O1P "Deoxy Hemoglobin (A-Gly-C:v1m; B,D:v1m,C93a,N108k)" 100.00 146 97.95 98.63 2.00e-98 PDB 1QI8 "Deoxygenated Structure Of A Distal Pocket Hemoglobin Mutant" 100.00 146 97.95 98.63 4.57e-99 PDB 1QSH "Magnesium(Ii)-And Zinc(Ii)-Protoporphyrin Ix's Stabilize The Lowest Oxygen Affinity State Of Human Hemoglobin Even More Strongl" 100.00 146 100.00 100.00 6.17e-101 PDB 1QSI "Magnesium(Ii)-And Zinc(Ii)-Protoporphyrin Ix's Stabilize The Lowest Oxygen Affinity State Of Human Hemoglobin Even More Strongl" 100.00 146 100.00 100.00 6.17e-101 PDB 1QXD "Structural Basis For The Potent Antisickling Effect Of A Novel Class Of 5-Membered Heterocyclic Aldehydic Compounds" 100.00 146 100.00 100.00 6.17e-101 PDB 1QXE "Structural Basis For The Potent Antisickling Effect Of A Novel Class Of 5-Membered Heterocyclic Aldehydic Compounds" 100.00 146 100.00 100.00 6.17e-101 PDB 1R1X "Crystal Structure Of Oxy-Human Hemoglobin Bassett At 2.15 Angstrom" 100.00 146 100.00 100.00 6.17e-101 PDB 1R1Y "Crystal Structure Of Deoxy-Human Hemoglobin Bassett At 1.8 Angstrom" 100.00 146 100.00 100.00 6.17e-101 PDB 1RPS "Crystallographic Analysis Of The Interaction Of Nitric Oxide With Quaternary-T Human Hemoglobin. Hemoglobin Exposed To No Under" 100.00 146 100.00 100.00 6.17e-101 PDB 1RQ3 "Crystallographic Analysis Of The Interaction Of Nitric Oxide With Quaternary-T Human Deoxyhemoglobin, Deoxyhemoglobin" 100.00 146 100.00 100.00 6.17e-101 PDB 1RQ4 "Crystallographic Analysis Of The Interaction Of Nitric Oxide With Quaternary-T Human Hemoglobin, Hemoglobin Exposed To No Under" 100.00 146 99.32 99.32 1.91e-99 PDB 1RQA "Crystallographic Analysis Of The Interaction Of Nitric Oxide With Quaternary-T Human Hemoglobin. Beta W73e Hemoglobin Exposed T" 100.00 146 98.63 99.32 7.31e-99 PDB 1RVW "R State Human Hemoglobin [alpha V96w], Carbonmonoxy" 100.00 146 100.00 100.00 6.17e-101 PDB 1SDK "Cross-linked, Carbonmonoxy Hemoglobin A" 100.00 146 100.00 100.00 6.17e-101 PDB 1SDL "Cross-Linked, Carbonmonoxy Hemoglobin A" 100.00 146 100.00 100.00 6.17e-101 PDB 1THB "Refinement Of A Partially Oxygenated T State Haemoglobin At 1.5 Angstroms Resolution" 100.00 146 100.00 100.00 6.17e-101 PDB 1UIW "Crystal Structures Of Unliganded And Half-Liganded Human Hemoglobin Derivatives Cross-Linked Between Lys 82beta1 And Lys 82beta" 100.00 146 100.00 100.00 6.17e-101 PDB 1VWT "T State Human Hemoglobin [alpha V96w], Alpha Aquomet, Beta Deoxy" 100.00 146 100.00 100.00 6.17e-101 PDB 1XXT "The T-To-T High Transitions In Human Hemoglobin: Wild-Type Deoxy Hb A (Low Salt, One Test Set)" 100.00 146 100.00 100.00 6.17e-101 PDB 1XY0 "T-To-Thigh Transitions In Human Hemoglobin: Alphak40g Deoxy Low-Salt" 100.00 146 100.00 100.00 6.17e-101 PDB 1XYE "T-to-thigh Transitions In Human Hemoglobin: Alpha Y42a Deoxy Low Salt" 100.00 146 100.00 100.00 6.17e-101 PDB 1XZ2 "Wild-Type Hemoglobin Deoxy No-Salt" 100.00 146 100.00 100.00 6.17e-101 PDB 1XZ4 "Intersubunit Interactions Associated With Tyr42alpha Stabilize The Quaternary-T Tetramer But Are Not Major Quaternary Constrain" 100.00 146 100.00 100.00 6.17e-101 PDB 1XZ5 "T-To-Thigh Quaternary Transitions In Human Hemoglobin: Alphal91a Deoxy Low-Salt" 100.00 146 100.00 100.00 6.17e-101 PDB 1XZ7 "T-To-Thigh Quaternary Transitions In Human Hemoglobin: Alphar92a Deoxy Low-Salt" 100.00 146 100.00 100.00 6.17e-101 PDB 1XZU "T-To-Thigh Quaternary Transitions In Human Hemoglobin: Alphad94g Deoxy Low-Salt" 100.00 146 100.00 100.00 6.17e-101 PDB 1XZV "T-To-Thigh Quaternary Transitions In Human Hemoglobin: Alphap95a Deoxy Low-Salt" 100.00 146 100.00 100.00 6.17e-101 PDB 1Y09 "T-To-T(High) Quaternary Transitions In Human Hemoglobin: Alphan97a Deoxy Low-Salt" 100.00 146 100.00 100.00 6.17e-101 PDB 1Y0A "T-To-Thigh Quaternary Transitions In Human Hemoglobin: Alphay140a Deoxy Low-Salt" 100.00 146 100.00 100.00 6.17e-101 PDB 1Y0C "T-To-Thigh Quaternary Transitions In Human Hemoglobin: Alphay140f Deoxy Low-Salt" 100.00 146 100.00 100.00 6.17e-101 PDB 1Y0D "T-To-Thigh Quaternary Transitions In Human Hemoglobin: Desarg141alpha Deoxy Low-Salt" 100.00 146 100.00 100.00 6.17e-101 PDB 1Y0T "T-To-T(High) Quaternary Transitions In Human Hemoglobin: Betav1m Deoxy Low-Salt (1 Test Set)" 100.00 146 99.32 100.00 1.37e-100 PDB 1Y0W "T-To-Thigh Quaternary Transitions In Human Hemoglobin: Betav1m Deoxy Low-Salt (10 Test Sets)" 100.00 146 99.32 100.00 1.37e-100 PDB 1Y22 "T-To-T(High) Quaternary Transitions In Human Hemoglobin: Betav33a Deoxy Low-Salt (1 Test Set)" 100.00 146 98.63 99.32 4.87e-100 PDB 1Y2Z "T-To-T(High) Quaternary Transitions In Human Hemoglobin: Betav34g Deoxy Low-Salt (1 Test Set)" 100.00 146 98.63 99.32 1.85e-99 PDB 1Y31 "T-To-T(High) Quaternary Transitions In Human Hemoglobin: Betay35a Deoxy Low-Salt (1 Test Set)" 100.00 146 98.63 99.32 2.40e-99 PDB 1Y35 "T-To-T(High) Quaternary Transitions In Human Hemoglobin: Betay35f Deoxy Low-Salt (1 Test Set)" 100.00 146 98.63 100.00 7.46e-100 PDB 1Y45 "T-To-T(High) Quaternary Transitions In Human Hemoglobin: Betap36a Deoxy Low-Salt (10 Test Sets)" 100.00 146 98.63 99.32 1.66e-99 PDB 1Y46 "T-To-T(High) Quaternary Transitions In Human Hemoglobin: Betaw37y Deoxy Low-Salt (10 Test Sets)" 100.00 146 98.63 100.00 1.02e-99 PDB 1Y4B "T-To-T(High) Quaternary Transitions In Human Hemoglobin: Betaw37h Deoxy Low-Salt (10 Test Sets)" 100.00 146 98.63 99.32 1.04e-98 PDB 1Y4F "T-To-T(High) Quaternary Transitions In Human Hemoglobin: Betaw37a Deoxy Low-Salt (10 Test Sets)" 100.00 146 98.63 99.32 4.99e-99 PDB 1Y4G "T-To-T(High) Quaternary Transitions In Human Hemoglobin: Betaw37g Deoxy Low-Salt (10 Test Sets)" 100.00 146 98.63 99.32 9.40e-99 PDB 1Y4P "T-To-T(High) Quaternary Transitions In Human Hemoglobin: Betaw37e Deoxy Low-Salt (10 Test Sets)" 100.00 146 98.63 99.32 7.31e-99 PDB 1Y4Q "T-To-T(High) Quaternary Transitions In Human Hemoglobin: Betaf42a Deoxy Low-Salt (1 Test Set)" 100.00 146 98.63 99.32 1.81e-99 PDB 1Y4R "T-To-T(High) Quaternary Transitions In Human Hemoglobin: Betaf45a Deoxy Low-Salt (1 Test Set)" 100.00 146 98.63 99.32 1.81e-99 PDB 1Y4V "T-To-T(High) Quaternary Transitions In Human Hemoglobin: Betac93a Deoxy Low-Salt (1 Test Set)" 100.00 146 98.63 99.32 2.53e-99 PDB 1Y5F "T-To-T(High) Quaternary Transitions In Human Hemoglobin: Betal96a Deoxy Low-Salt (1 Test Set)" 100.00 146 98.63 99.32 7.96e-100 PDB 1Y5J "T-to-t(high) Quaternary Transitions In Human Hemoglobin: Betah97a Deoxy Low-salt (1 Test Set)" 100.00 146 98.63 99.32 1.95e-99 PDB 1Y5K "T-to-t(high) Quaternary Transitions In Human Hemoglobin: Betad99a Deoxy Low-salt (10 Test Sets)" 100.00 146 98.63 99.32 1.75e-99 PDB 1Y7C "T-To-T(High) Quaternary Transitions In Human Hemoglobin: Betap100a Deoxy Low-Salt (1 Test Set)" 100.00 146 98.63 99.32 1.66e-99 PDB 1Y7D "T-to-t(high) Quaternary Transitions In Human Hemoglobin: Betap100g Deoxy Low-salt (1 Test Set)" 100.00 146 98.63 99.32 2.86e-99 PDB 1Y7G "T-To-T(High) Quaternary Transitions In Human Hemoglobin: Betan102a Deoxy Low-Salt (1 Test Set)" 100.00 146 98.63 99.32 1.87e-99 PDB 1Y7Z "T-To-T(High) Quaternary Transitions In Human Hemoglobin: Betan108a Deoxy Low-Salt (1 Test Set)" 100.00 146 98.63 99.32 1.87e-99 PDB 1Y83 "T-To-T(High) Quaternary Transitions In Human Hemoglobin: Betay145g Deoxy Low-Salt (1 Test Set)" 100.00 146 98.63 99.32 4.72e-99 PDB 1Y85 "T-To-T(High) Quaternary Transitions In Human Hemoglobin: Deshis146beta Deoxy Low-Salt" 99.32 145 100.00 100.00 4.66e-100 PDB 1Y8W "T-To-T(High) Quaternary Transitions In Human Hemoglobin: Alphar92a Oxy (2mm Ihp, 20% Peg) (10 Test Sets)" 100.00 146 100.00 100.00 6.17e-101 PDB 1YDZ "T-To-T(High) Quaternary Transitions In Human Hemoglobin: Alphay140f Oxy (2mm Ihp, 20% Peg) (1 Test Set)" 100.00 146 100.00 100.00 6.17e-101 PDB 1YE0 "T-To-T(High) Quaternary Transitions In Human Hemoglobin: Betav33a Oxy (2mm Ihp, 20% Peg) (1 Test Set)" 100.00 146 98.63 99.32 4.87e-100 PDB 1YE1 "T-To-T(High) Quaternary Transitions In Human Hemoglobin: Betay35a Oxy (2mm Ihp, 20% Peg) (1 Test Set)" 100.00 146 98.63 99.32 2.40e-99 PDB 1YE2 "T-To-T(High) Quaternary Transitions In Human Hemoglobin: Betay35f Oxy (2mm Ihp, 20% Peg) (1 Test Set)" 100.00 146 98.63 100.00 7.46e-100 PDB 1YEN "T-To-T(High) Quaternary Transitions In Human Hemoglobin: Betap36a Oxy (2mm Ihp, 20% Peg) (10 Test Sets)" 100.00 146 98.63 99.32 1.66e-99 PDB 1YEO "T-To-T(High) Quaternary Transitions In Human Hemoglobin: Betaw37a Oxy (10 Test Sets)" 100.00 146 98.63 99.32 4.99e-99 PDB 1YEQ "T-To-T(High) Quaternary Transitions In Human Hemoglobin: Betaw37y Oxy (10 Test Sets)" 100.00 146 98.63 100.00 1.02e-99 PDB 1YEU "T-To-T(High) Quaternary Transitions In Human Hemoglobin: Betaw37g Oxy (10 Test Sets)" 100.00 146 98.63 99.32 9.40e-99 PDB 1YEV "T-To-T(High) Quaternary Transitions In Human Hemoglobin: Betaw37e Oxy (10 Test Sets)" 100.00 146 98.63 99.32 7.31e-99 PDB 1YFF "Structure Of Human Carbonmonoxyhemoglobin C (beta E6k): Two Quaternary States (r2 And R3) In One Crystal" 100.00 146 99.32 100.00 3.04e-100 PDB 1YG5 "T-To-T(High) Quaternary Transitions In Human Hemoglobin: Betaw37h Oxy (2mm Ihp, 20% Peg) (10 Test Sets)" 100.00 146 98.63 99.32 1.04e-98 PDB 1YGD "T-to-t(high) Quaternary Transitions In Human Hemoglobin: Betaw37e Alpha Zinc Beta Oxy (10 Test Sets)" 100.00 146 98.63 99.32 7.31e-99 PDB 1YGF "T-To-T(High) Quaternary Transitions In Human Hemoglobin: Betah97a Oxy (2mm Ihp, 20% Peg) (1 Test Set)" 100.00 146 98.63 99.32 1.95e-99 PDB 1YH9 "T-To-T(High) Quaternary Transitions In Human Hemoglobin: Hba Oxy (2mm Ihp, 20% Peg) (10 Test Sets)" 100.00 146 100.00 100.00 6.17e-101 PDB 1YHE "T-To-T(High) Quaternary Transitions In Human Hemoglobin: Hba Oxy (5.0mm Ihp, 20% Peg) (10 Test Sets)" 100.00 146 100.00 100.00 6.17e-101 PDB 1YHR "T-To-T(High) Quaternary Transitions In Human Hemoglobin: Hba Oxy (10.0mm Ihp, 20% Peg) (10 Test Sets)" 100.00 146 100.00 100.00 6.17e-101 PDB 1YIE "T-to-thigh Quaternary Transitions In Human Hemoglobin: Betaw37a Oxy (2.2mm Ihp, 13% Peg) (1 Test Set)" 100.00 146 98.63 99.32 4.99e-99 PDB 1YIH "T-To-T(High) Quaternary Transitions In Human Hemoglobin: Betap100a Oxy (2.2mm Ihp, 20% Peg) (1 Test Set)" 100.00 146 98.63 99.32 1.66e-99 PDB 1YVQ "The Low Salt (Peg) Crystal Structure Of Co Hemoglobin E (Betae26k) Approaching Physiological Ph (Ph 7.5)" 100.00 146 99.32 100.00 3.04e-100 PDB 1YVT "The High Salt (Phosphate) Crystal Structure Of Co Hemoglobin E (Glu26lys) At Physiological Ph (Ph 7.35)" 100.00 146 99.32 100.00 3.04e-100 PDB 1YZI "A Novel Quaternary Structure Of Human Carbonmonoxy Hemoglobin" 100.00 146 100.00 100.00 6.17e-101 PDB 2D5Z "Crystal Structure Of T-State Human Hemoglobin Complexed With Three L35 Molecules" 100.00 146 100.00 100.00 6.17e-101 PDB 2D60 "Crystal Structure Of Deoxy Human Hemoglobin Complexed With Two L35 Molecules" 100.00 146 100.00 100.00 6.17e-101 PDB 2DN1 "1.25a Resolution Crystal Structure Of Human Hemoglobin In The Oxy Form" 100.00 146 100.00 100.00 6.17e-101 PDB 2DN2 "1.25a Resolution Crystal Structure Of Human Hemoglobin In The Deoxy Form" 100.00 146 100.00 100.00 6.17e-101 PDB 2DN3 "1.25a Resolution Crystal Structure Of Human Hemoglobin In The Carbonmonoxy Form" 100.00 146 100.00 100.00 6.17e-101 PDB 2DXM "Neutron Structure Analysis Of Deoxy Human Hemoglobin" 100.00 146 100.00 100.00 6.17e-101 PDB 2H35 "Solution Structure Of Human Normal Adult Hemoglobin" 100.00 146 100.00 100.00 6.17e-101 PDB 2HBC "High Resolution X-ray Structures Of Myoglobin-and Hemoglobin-alkyl Isocyanide Complexes" 100.00 146 100.00 100.00 6.17e-101 PDB 2HBD "High Resolution X-Ray Structures Of Myoglobin-And Hemoglobin-Alkyl Isocyanide Complexes" 100.00 146 100.00 100.00 6.17e-101 PDB 2HBE "High Resolution X-Ray Structures Of Myoglobin-And Hemoglobin-Alkyl Isocyanide Complexes" 100.00 146 100.00 100.00 6.17e-101 PDB 2HBF "High Resolution X-Ray Structures Of Myoglobin-And Hemoglobin-Alkyl Isocyanide Complexes" 100.00 146 100.00 100.00 6.17e-101 PDB 2HBS "The High Resolution Crystal Structure Of Deoxyhemoglobin S" 100.00 146 99.32 99.32 8.59e-100 PDB 2HCO "The Structure Of Human Carbonmonoxy Haemoglobin At 2.7 Angstroms Resolution" 100.00 146 100.00 100.00 6.17e-101 PDB 2HHB "The Crystal Structure Of Human Deoxyhaemoglobin At 1.74 Angstroms Resolution" 100.00 146 100.00 100.00 6.17e-101 PDB 2HHD "Oxygen Affinity Modulation By The N-Termini Of The Beta- Chains In Human And Bovine Hemoglobin" 100.00 146 100.00 100.00 6.17e-101 PDB 2HHE "Oxygen Affinity Modulation By The N-Termini Of The Beta Chains In Human And Bovine Hemoglobin" 98.63 145 100.00 100.00 1.48e-99 PDB 2M6Z "Refined Solution Structure Of Human Adult Hemoglobin In The Carbonmonoxy Form" 100.00 146 100.00 100.00 6.17e-101 PDB 2W6V "Structure Of Human Deoxy Hemoglobin A In Complex With Xenon" 100.00 146 100.00 100.00 6.17e-101 PDB 2W72 "Deoxygenated Structure Of A Distal Site Hemoglobin Mutant Plus Xe" 100.00 146 97.95 98.63 4.57e-99 PDB 2YRS "Human Hemoglobin D Los Angeles: Crystal Structure" 100.00 146 99.32 100.00 1.61e-100 PDB 3B75 "Crystal Structure Of Glycated Human Haemoglobin" 100.00 146 100.00 100.00 6.17e-101 PDB 3D17 "A Triply Ligated Crystal Structure Of Relaxed State Human Hemoglobin" 100.00 146 100.00 100.00 6.17e-101 PDB 3D7O "Human Hemoglobin, Nitrogen Dioxide Anion Modified" 100.00 146 100.00 100.00 6.17e-101 PDB 3DUT "The High Salt (Phosphate) Crystal Structure Of Deoxy Hemoglobin E (Glu26lys) At Physiological Ph (Ph 7.35)" 100.00 146 99.32 100.00 3.04e-100 PDB 3HHB "The Crystal Structure Of Human Deoxyhaemoglobin At 1.74 Angstroms Resolution" 100.00 146 100.00 100.00 6.17e-101 PDB 3HXN "The Structure Of Human Carbonmonoxyhemoglobin Complex To Ihp At 2.0 Angstrons Resolution." 100.00 146 100.00 100.00 6.17e-101 PDB 3IC0 "Crystal Structure Of Liganded Hemoglobin In Complex With A Potent Antisickling Agent, Inn-298" 100.00 146 100.00 100.00 6.17e-101 PDB 3IC2 "Crystal Structure Of Liganded Hemoglobin In Complex With A Potent Antisickling Agent, Inn-266" 100.00 146 100.00 100.00 6.17e-101 PDB 3KMF "Room Temperature Time-Of-Flight Neutron Diffraction Study Of Deoxy Human Normal Adult Hemoglobin" 99.32 146 100.00 100.00 3.55e-100 PDB 3NL7 "Human Hemoglobin A Mutant Beta H63w Carbonmonoxy-Form" 100.00 146 99.32 99.32 2.27e-99 PDB 3NMM "Human Hemoglobin A Mutant Alpha H58w Deoxy-Form" 100.00 146 100.00 100.00 6.17e-101 PDB 3ODQ "Structure Of A Crystal Form Of Human Methemoglobin Indicative Of Fiber Formation" 100.00 146 100.00 100.00 6.17e-101 PDB 3ONZ "Human Tetrameric Hemoglobin: Proximal Nitrite Ligand At Beta" 100.00 146 100.00 100.00 6.17e-101 PDB 3OO4 "R-State Human Hemoglobin: Nitriheme Modified At Alpha" 100.00 146 100.00 100.00 6.17e-101 PDB 3OO5 "R-State Human Hemoglobin: Nitriheme Modified" 100.00 146 100.00 100.00 6.17e-101 PDB 3P5Q "Ferric R-State Human Aquomethemoglobin" 100.00 146 100.00 100.00 6.17e-101 PDB 3QJB "Human Hemoglobin A Mutant Alpha H58l Carbonmonoxy-Form" 100.00 146 100.00 100.00 6.17e-101 PDB 3QJC "Human Hemoglobin A Mutant Beta H63l Carbonmonoxy-Form" 100.00 146 99.32 99.32 1.53e-99 PDB 3QJD "Human Hemoglobin A Mutant Alpha H58l Deoxy-Form" 100.00 146 100.00 100.00 6.17e-101 PDB 3QJE "Human Hemoglobin A Mutant Beta H63l Deoxy-Form" 100.00 146 99.32 99.32 1.53e-99 PDB 3R5I "Crystal Structure Of Liganded Hemoglobin Complexed With A Potent Antisickling Agent, Inn-312" 100.00 146 100.00 100.00 6.17e-101 PDB 3S65 "Structures And Oxygen Affinities Of Crystalline Human Hemoglobin C (Beta6 Lys) In The R2 Quaternary Structures" 100.00 146 99.32 100.00 3.04e-100 PDB 3S66 "Structures And Oxygen Affinities Of Crystalline Human Hemoglobin C (Beta6 Lys) In The R Quaternary Structures" 100.00 146 99.32 100.00 3.04e-100 PDB 3SZK "Crystal Structure Of Human Methaemoglobin Complexed With The First Neat Domain Of Isdh From Staphylococcus Aureus" 100.00 146 100.00 100.00 6.17e-101 PDB 3W4U "Human Zeta-2 Beta-2-s Hemoglobin" 100.00 146 99.32 99.32 8.59e-100 PDB 3WCP "Deoxyhemoglobin Sh-drug Complex" 100.00 146 99.32 99.32 1.91e-99 PDB 3WHM "Structure Of Hemoglobin Complex With 18-crown-6" 100.00 146 100.00 100.00 6.17e-101 PDB 4FC3 "Crystal Structure Of Human Methaemoglobin Complexed With The Second Neat Domain Of Isdh From Staphylococcus Aureus" 100.00 146 100.00 100.00 6.17e-101 PDB 4HHB "The Crystal Structure Of Human Deoxyhaemoglobin At 1.74 Angstroms Resolution" 100.00 146 100.00 100.00 6.17e-101 PDB 4IJ2 "Human Methemoglobin In Complex With The Second And Third Neat Domains Of Isdh From Staphylococcus Aureus" 100.00 146 100.00 100.00 6.17e-101 PDB 4L7Y "Deoxygenated Hb In Complex With The Allosteric Effectors, Irl2500 And 2,3-dpg" 100.00 146 100.00 100.00 6.17e-101 PDB 4M4A "Human Hemoglobin Nitromethane Modified" 100.00 146 100.00 100.00 6.17e-101 PDB 4M4B "Human Hemoglobin Nitroethane Modified" 100.00 146 100.00 100.00 6.17e-101 PDB 4MQC "Carbonmonoxy Structure Of Hemoglobin Evans Alphav62mbetawt" 100.00 146 100.00 100.00 6.17e-101 PDB 4MQG "Structure Of Carbonmonoxy Adult Hemoglobin Bristol-alesha Alphawtbetav67m" 100.00 146 99.32 100.00 1.37e-100 PDB 4MQH "Structure Of Aquomet Hemoglobin Evans Alphav62mbetawt" 100.00 146 100.00 100.00 6.17e-101 PDB 4MQI "Structure Of Aquomet Hemoglobin Bristol-alesha Alphawtbetav67m" 100.00 146 99.32 100.00 1.37e-100 PDB 4N7N "Capturing The Haemoglobin Allosteric Transition In A Single Crystal Form; Crystal Structure Of Full-liganded Human Haemoglobin " 100.00 146 100.00 100.00 6.17e-101 PDB 4N7O "Capturing The Haemoglobin Allosteric Transition In A Single Crystal Form; Crystal Structure Of Half-liganded Human Haemoglobin " 100.00 146 100.00 100.00 6.17e-101 PDB 4N7P "Capturing The Haemoglobin Allosteric Transition In A Single Crystal Form; Crystal Structure Of Half-liganded Human Haemoglobin " 100.00 146 100.00 100.00 6.17e-101 PDB 4N8T "Human Hemoglobin Nitric Oxide Adduct" 100.00 146 100.00 100.00 6.17e-101 PDB 4NI0 "Quaternary R3 Co-liganded Hemoglobin Structure In Complex With A Thiol Containing Compound" 100.00 146 100.00 100.00 6.17e-101 PDB 4NI1 "Qauternary R Co-liganded Hemoglobin Structure In Complex With A Thiol Containing Compound" 100.00 146 100.00 100.00 6.17e-101 PDB 4WJG "Structure Of T. Brucei Haptoglobin-hemoglobin Receptor Binding To Human Haptoglobin-hemoglobin" 100.00 146 100.00 100.00 6.17e-101 PDB 6HBW "Crystal Structure Of Deoxy-human Hemoglobin Beta6 Glu->trp" 100.00 146 99.32 99.32 1.73e-99 DBJ BAG34767 "unnamed protein product [Homo sapiens]" 100.00 147 100.00 100.00 5.85e-101 EMBL CAA23756 "unnamed protein product [Homo sapiens]" 100.00 147 100.00 100.00 5.85e-101 EMBL CAA23758 "beta globin [Homo sapiens]" 100.00 147 100.00 100.00 5.85e-101 EMBL CAA23759 "unnamed protein product [Homo sapiens]" 100.00 147 98.63 98.63 5.05e-99 EMBL CAA43421 "beta-globin [Gorilla gorilla]" 82.19 121 99.17 100.00 4.37e-80 EMBL CAG38767 "HBB [Homo sapiens]" 100.00 147 100.00 100.00 5.85e-101 GB AAA16334 "beta-globin [Homo sapiens]" 100.00 147 100.00 100.00 5.85e-101 GB AAA21100 "beta-globin [Homo sapiens]" 100.00 147 100.00 100.00 5.85e-101 GB AAA21101 "beta-globin [Homo sapiens]" 100.00 147 100.00 100.00 5.85e-101 GB AAA21102 "beta-globin [Homo sapiens]" 100.00 147 100.00 100.00 5.85e-101 GB AAA21103 "beta-globin [Homo sapiens]" 100.00 147 100.00 100.00 5.85e-101 PRF 0404170B "hemoglobin beta" 100.00 146 98.63 98.63 5.69e-99 PRF 0907233B "hemoglobin beta" 100.00 146 100.00 100.00 6.17e-101 REF NP_000509 "hemoglobin subunit beta [Homo sapiens]" 100.00 147 100.00 100.00 5.85e-101 REF XP_002822173 "PREDICTED: hemoglobin subunit beta isoform X2 [Pongo abelii]" 100.00 147 98.63 98.63 5.39e-99 REF XP_003819077 "PREDICTED: hemoglobin subunit beta [Pan paniscus]" 100.00 147 100.00 100.00 5.85e-101 REF XP_004050595 "PREDICTED: hemoglobin subunit beta [Gorilla gorilla gorilla]" 95.21 143 99.28 100.00 4.51e-95 REF XP_004090697 "PREDICTED: LOW QUALITY PROTEIN: hemoglobin subunit beta [Nomascus leucogenys]" 100.00 147 97.95 97.95 2.96e-98 SP P02024 "RecName: Full=Hemoglobin subunit beta; AltName: Full=Beta-globin; AltName: Full=Hemoglobin beta chain [Gorilla gorilla gorilla]" 100.00 147 99.32 100.00 2.34e-100 SP P02025 "RecName: Full=Hemoglobin subunit beta; AltName: Full=Beta-globin; AltName: Full=Hemoglobin beta chain [Hylobates lar]" 100.00 146 98.63 98.63 4.99e-99 SP P02032 "RecName: Full=Hemoglobin subunit beta; AltName: Full=Beta-globin; AltName: Full=Hemoglobin beta chain [Semnopithecus entellus]" 100.00 146 97.26 98.63 4.58e-98 SP P68871 "RecName: Full=Hemoglobin subunit beta; AltName: Full=Beta-globin; AltName: Full=Hemoglobin beta chain; Contains: RecName: Full=" 100.00 147 100.00 100.00 5.85e-101 SP P68872 "RecName: Full=Hemoglobin subunit beta; AltName: Full=Beta-globin; AltName: Full=Hemoglobin beta chain [Pan paniscus]" 100.00 147 100.00 100.00 5.85e-101 stop_ save_ save_globin_subunit_beta _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'beta chain' _Molecular_mass . _Mol_thiol_state 'all free' _Details . _Residue_count 146 _Mol_residue_sequence ; VHLTPEEKSAVTALWGKVNV DEVGGEALGRLLVVYPWTQR FFESFGDLSTPDAVMGNPKV KAHGKKVLGAFSDGLAHLDN LKGTFATLSELHCDKLHVDP ENFRLLGNVLVCVLAHHFGK EFTPPVQAAYQKVVAGVANA LAHKYH ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 1 VAL 2 2 HIS 3 3 LEU 4 4 THR 5 5 PRO 6 6 GLU 7 7 GLU 8 8 LYS 9 9 SER 10 10 ALA 11 11 VAL 12 12 THR 13 13 ALA 14 14 LEU 15 15 TRP 16 16 GLY 17 17 LYS 18 18 VAL 19 19 ASN 20 20 VAL 21 21 ASP 22 22 GLU 23 23 VAL 24 24 GLY 25 25 GLY 26 26 GLU 27 27 ALA 28 28 LEU 29 29 GLY 30 30 ARG 31 31 LEU 32 32 LEU 33 33 VAL 34 34 VAL 35 35 TYR 36 36 PRO 37 37 TRP 38 38 THR 39 39 GLN 40 40 ARG 41 41 PHE 42 42 PHE 43 43 GLU 44 44 SER 45 45 PHE 46 46 GLY 47 47 ASP 48 48 LEU 49 49 SER 50 50 THR 51 51 PRO 52 52 ASP 53 53 ALA 54 54 VAL 55 55 MET 56 56 GLY 57 57 ASN 58 58 PRO 59 59 LYS 60 60 VAL 61 61 LYS 62 62 ALA 63 63 HIS 64 64 GLY 65 65 LYS 66 66 LYS 67 67 VAL 68 68 LEU 69 69 GLY 70 70 ALA 71 71 PHE 72 72 SER 73 73 ASP 74 74 GLY 75 75 LEU 76 76 ALA 77 77 HIS 78 78 LEU 79 79 ASP 80 80 ASN 81 81 LEU 82 82 LYS 83 83 GLY 84 84 THR 85 85 PHE 86 86 ALA 87 87 THR 88 88 LEU 89 89 SER 90 90 GLU 91 91 LEU 92 92 HIS 93 93 CYS 94 94 ASP 95 95 LYS 96 96 LEU 97 97 HIS 98 98 VAL 99 99 ASP 100 100 PRO 101 101 GLU 102 102 ASN 103 103 PHE 104 104 ARG 105 105 LEU 106 106 LEU 107 107 GLY 108 108 ASN 109 109 VAL 110 110 LEU 111 111 VAL 112 112 CYS 113 113 VAL 114 114 LEU 115 115 ALA 116 116 HIS 117 117 HIS 118 118 PHE 119 119 GLY 120 120 LYS 121 121 GLU 122 122 PHE 123 123 THR 124 124 PRO 125 125 PRO 126 126 VAL 127 127 GLN 128 128 ALA 129 129 ALA 130 130 TYR 131 131 GLN 132 132 LYS 133 133 VAL 134 134 VAL 135 135 ALA 136 136 GLY 137 137 VAL 138 138 ALA 139 139 ASN 140 140 ALA 141 141 LEU 142 142 ALA 143 143 HIS 144 144 LYS 145 145 TYR 146 146 HIS stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date . save_ ############# # Ligands # ############# save_HEM_red _Saveframe_category ligand _Mol_type "non-polymer (fragment)" _Name_common 'PROTOPORPHYRIN IX CONTAINING FE' _Abbreviation_common heme _BMRB_code HEM_red _PDB_code HEM _Molecular_mass . _Mol_charge . _Mol_paramagnetic no _Mol_aromatic yes _Details . _Synonym HEME loop_ _Atom_name _PDB_atom_name _Atom_type _Atom_chirality _Atom_charge _Atom_oxidation_number _Atom_unpaired_electrons C1A C1A C . 0 . ? C1B C1B C . 0 . ? C1C C1C C . 0 . ? C1D C1D C . 0 . ? C2A C2A C . 0 . ? C2B C2B C . 0 . ? C2C C2C C . 0 . ? C2D C2D C . 0 . ? C3A C3A C . 0 . ? C3B C3B C . 0 . ? C3C C3C C . 0 . ? C3D C3D C . 0 . ? C4A C4A C . 0 . ? C4B C4B C . 0 . ? C4C C4C C . 0 . ? C4D C4D C . 0 . ? CAA CAA C . 0 . ? CAB CAB C . 0 . ? CAC CAC C . 0 . ? CAD CAD C . 0 . ? CBA CBA C . 0 . ? CBB CBB C . 0 . ? CBC CBC C . 0 . ? CBD CBD C . 0 . ? CGA CGA C . 0 . ? CGD CGD C . 0 . ? CHA CHA C . 0 . ? CHB CHB C . 0 . ? CHC CHC C . 0 . ? CHD CHD C . 0 . ? CMA CMA C . 0 . ? CMB CMB C . 0 . ? CMC CMC C . 0 . ? CMD CMD C . 0 . ? FE FE FE . 2+ 2+ ? 1HAA 1HAA H . 0 . ? 1HAD 1HAD H . 0 . ? 1HBA 1HBA H . 0 . ? 1HBB 1HBB H . 0 . ? 1HBC 1HBC H . 0 . ? 1HBD 1HBD H . 0 . ? 1HMA 1HMA H . 0 . ? 1HMB 1HMB H . 0 . ? 1HMC 1HMC H . 0 . ? 1HMD 1HMD H . 0 . ? 2HAA 2HAA H . 0 . ? 2HAD 2HAD H . 0 . ? 2HBA 2HBA H . 0 . ? 2HBB 2HBB H . 0 . ? 2HBC 2HBC H . 0 . ? 2HBD 2HBD H . 0 . ? 2HMA 2HMA H . 0 . ? 2HMB 2HMB H . 0 . ? 2HMC 2HMC H . 0 . ? 2HMD 2HMD H . 0 . ? 3HMA 3HMA H . 0 . ? 3HMB 3HMB H . 0 . ? 3HMC 3HMC H . 0 . ? 3HMD 3HMD H . 0 . ? H2A H2A H . 0 . ? H2D H2D H . 0 . ? HAB HAB H . 0 . ? HAC HAC H . 0 . ? HHA HHA H . 0 . ? HHB HHB H . 0 . ? HHC HHC H . 0 . ? HHD HHD H . 0 . ? NA 'N A' N . 0 . ? NB 'N B' N . 0 . ? NC 'N C' N . 0 . ? ND 'N D' N . 0 . ? O1A O1A O . 0 . ? O1D O1D O . 0 . ? O2A O2A O . 0 . ? O2D O2D O . 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 FE NA ? ? SING FE NB ? ? SING FE NC ? ? SING FE ND ? ? DOUB CHA C1A ? ? SING CHA C4D ? ? SING CHA HHA ? ? DOUB CHB C4A ? ? SING CHB C1B ? ? SING CHB HHB ? ? DOUB CHC C4B ? ? SING CHC C1C ? ? SING CHC HHC ? ? SING CHD C4C ? ? DOUB CHD C1D ? ? SING CHD HHD ? ? SING NA C1A ? ? SING NA C4A ? ? SING C1A C2A ? ? DOUB C2A C3A ? ? SING C2A CAA ? ? SING C3A C4A ? ? SING C3A CMA ? ? SING CMA 1HMA ? ? SING CMA 2HMA ? ? SING CMA 3HMA ? ? SING CAA CBA ? ? SING CAA 1HAA ? ? SING CAA 2HAA ? ? SING CBA CGA ? ? SING CBA 1HBA ? ? SING CBA 2HBA ? ? DOUB CGA O1A ? ? SING CGA O2A ? ? SING O2A H2A ? ? DOUB NB C1B ? ? SING NB C4B ? ? SING C1B C2B ? ? DOUB C2B C3B ? ? SING C2B CMB ? ? SING C3B C4B ? ? SING C3B CAB ? ? SING CMB 1HMB ? ? SING CMB 2HMB ? ? SING CMB 3HMB ? ? DOUB CAB CBB ? ? SING CAB HAB ? ? SING CBB 1HBB ? ? SING CBB 2HBB ? ? SING NC C1C ? ? SING NC C4C ? ? DOUB C1C C2C ? ? SING C2C C3C ? ? SING C2C CMC ? ? DOUB C3C C4C ? ? SING C3C CAC ? ? SING CMC 1HMC ? ? SING CMC 2HMC ? ? SING CMC 3HMC ? ? DOUB CAC CBC ? ? SING CAC HAC ? ? SING CBC 1HBC ? ? SING CBC 2HBC ? ? SING ND C1D ? ? DOUB ND C4D ? ? SING C1D C2D ? ? DOUB C2D C3D ? ? SING C2D CMD ? ? SING C3D C4D ? ? SING C3D CAD ? ? SING CMD 1HMD ? ? SING CMD 2HMD ? ? SING CMD 3HMD ? ? SING CAD CBD ? ? SING CAD 1HAD ? ? SING CAD 2HAD ? ? SING CBD CGD ? ? SING CBD 1HBD ? ? SING CBD 2HBD ? ? DOUB CGD O1D ? ? SING CGD O2D ? ? SING O2D H2D ? ? 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 _Tissue $globin_subunit_alpha Human 9606 Eukaryota Metazoa Homo sapiens 7125 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 $globin_subunit_alpha 'recombinant technology' . . . . . 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 _Isotopic_labeling $globin_subunit_alpha 1.2 mM '[U-13C; U-15N]' $globin_subunit_beta 1.0 mM '[U-13C; U-15N]' stop_ save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_800Mhz _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model avance _Field_strength 800 _Details 'US2 spectrometer' save_ save_500Mhz _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model avance _Field_strength 500 _Details 'US2 spectrometer with cyrpoprobe' save_ ############################# # NMR applied experiments # ############################# save_4D_13C,_15N-edited_NOESY_1 _Saveframe_category NMR_applied_experiment _Experiment_name '4D 13C, 15N-edited NOESY' _Sample_label $sample_1 save_ save_4D_13C,_13C-edited_NOESY_2 _Saveframe_category NMR_applied_experiment _Experiment_name '4D 13C, 13C-edited NOESY' _Sample_label $sample_1 save_ save_3D_MQ-CCH-TOCSY_3 _Saveframe_category NMR_applied_experiment _Experiment_name '3D MQ-CCH-TOCSY' _Sample_label $sample_1 save_ ####################### # Sample conditions # ####################### save_conditions_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 7.0 . pH temperature 308 0.1 K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_referencing _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 DSS C 13 'methyl protons' ppm 0.0 . indirect . . . 0.251449530 DSS H 1 'methyl protons' ppm 0.0 internal direct . . . 1.0 DSS N 15 'methyl protons' ppm 0.0 . indirect . . . 0.101329118 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_chem_shift_list_1_1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $conditions_1 _Chem_shift_reference_set_label $chemical_shift_referencing _Mol_system_component_name 'globin subunit alpha, 1' _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 1 VAL HG1 H 0.712 0.016 2 2 1 1 VAL CG1 C 20.596 0.045 2 3 2 2 LEU HA H 4.619 0.004 1 4 2 2 LEU HB2 H 1.762 0.022 2 5 2 2 LEU HB3 H 1.550 0.009 2 6 2 2 LEU HG H 1.846 0.008 1 7 2 2 LEU HD1 H 0.889 0.013 2 8 2 2 LEU HD2 H 1.017 0.010 2 9 2 2 LEU CA C 54.825 0.079 1 10 2 2 LEU CB C 43.310 0.079 1 11 2 2 LEU CG C 28.300 0.156 1 12 2 2 LEU CD1 C 24.724 0.103 2 13 2 2 LEU CD2 C 26.410 0.051 2 14 3 3 SER H H 9.855 0.011 1 15 3 3 SER CA C 56.771 0.000 1 16 3 3 SER N N 121.907 0.051 1 17 5 5 ALA HA H 4.067 0.004 1 18 5 5 ALA HB H 1.298 0.011 1 19 5 5 ALA CA C 55.050 0.134 1 20 5 5 ALA CB C 18.425 0.085 1 21 6 6 ASP H H 8.199 0.010 1 22 6 6 ASP HA H 4.700 0.000 1 23 6 6 ASP HB2 H 3.142 0.000 2 24 6 6 ASP HB3 H 2.611 0.000 2 25 6 6 ASP CA C 57.720 0.098 1 26 6 6 ASP CB C 42.291 0.014 1 27 6 6 ASP N N 118.496 0.056 1 28 7 7 LYS H H 8.066 0.009 1 29 7 7 LYS HA H 3.653 0.012 1 30 7 7 LYS HB2 H 1.892 0.051 2 31 7 7 LYS HD2 H 1.638 0.000 2 32 7 7 LYS HE2 H 2.759 0.012 2 33 7 7 LYS CA C 61.360 0.089 1 34 7 7 LYS CB C 31.936 0.168 1 35 7 7 LYS CD C 29.794 0.000 1 36 7 7 LYS CE C 42.069 0.029 1 37 7 7 LYS N N 118.779 0.061 1 38 8 8 THR H H 8.040 0.010 1 39 8 8 THR HA H 3.806 0.006 1 40 8 8 THR HB H 4.216 0.004 1 41 8 8 THR HG2 H 1.209 0.020 1 42 8 8 THR CA C 66.926 0.096 1 43 8 8 THR CB C 68.798 0.060 1 44 8 8 THR CG2 C 22.093 0.062 1 45 8 8 THR N N 115.941 0.035 1 46 9 9 ASN H H 8.431 0.019 1 47 9 9 ASN HA H 4.511 0.011 1 48 9 9 ASN HB2 H 3.205 0.032 2 49 9 9 ASN HB3 H 2.514 0.000 2 50 9 9 ASN CA C 55.787 0.168 1 51 9 9 ASN CB C 38.215 0.081 1 52 9 9 ASN N N 121.249 0.056 1 53 10 10 VAL H H 8.492 0.006 1 54 10 10 VAL HA H 3.426 0.014 1 55 10 10 VAL HB H 1.848 0.007 1 56 10 10 VAL HG1 H 0.817 0.016 2 57 10 10 VAL HG2 H 0.133 0.005 2 58 10 10 VAL CA C 67.317 0.080 1 59 10 10 VAL CB C 31.659 0.068 1 60 10 10 VAL CG1 C 24.146 0.128 2 61 10 10 VAL CG2 C 21.105 0.103 2 62 10 10 VAL N N 119.653 0.054 1 63 11 11 LYS H H 8.027 0.010 1 64 11 11 LYS HA H 3.797 0.017 1 65 11 11 LYS HB2 H 1.840 0.013 2 66 11 11 LYS HG2 H 1.488 0.019 2 67 11 11 LYS HG3 H 1.308 0.001 2 68 11 11 LYS HD2 H 1.600 0.017 2 69 11 11 LYS HD3 H 1.807 0.002 2 70 11 11 LYS HE2 H 2.876 0.003 2 71 11 11 LYS CA C 60.534 0.084 1 72 11 11 LYS CB C 32.730 0.095 1 73 11 11 LYS CG C 26.532 0.096 1 74 11 11 LYS CD C 29.907 0.081 1 75 11 11 LYS CE C 42.266 0.058 1 76 11 11 LYS N N 118.608 0.053 1 77 12 12 ALA H H 8.247 0.006 1 78 12 12 ALA HA H 4.137 0.023 1 79 12 12 ALA HB H 1.541 0.005 1 80 12 12 ALA CA C 55.086 0.088 1 81 12 12 ALA CB C 18.299 0.096 1 82 12 12 ALA N N 121.859 0.033 1 83 13 13 ALA H H 8.276 0.004 1 84 13 13 ALA HA H 4.112 0.013 1 85 13 13 ALA HB H 1.497 0.016 1 86 13 13 ALA CA C 55.424 0.146 1 87 13 13 ALA CB C 18.477 0.077 1 88 13 13 ALA N N 120.871 0.030 1 89 14 14 TRP H H 9.104 0.005 1 90 14 14 TRP HA H 4.224 0.020 1 91 14 14 TRP HB2 H 3.190 0.040 2 92 14 14 TRP HB3 H 3.303 0.000 2 93 14 14 TRP HD1 H 7.269 0.004 1 94 14 14 TRP HE1 H 10.418 0.010 1 95 14 14 TRP HE3 H 7.218 0.005 1 96 14 14 TRP HZ2 H 7.492 0.005 1 97 14 14 TRP HZ3 H 6.886 0.015 1 98 14 14 TRP HH2 H 6.922 0.006 1 99 14 14 TRP CA C 60.104 0.073 1 100 14 14 TRP CB C 29.331 0.142 1 101 14 14 TRP CD1 C 126.651 0.147 1 102 14 14 TRP CE3 C 119.535 0.025 1 103 14 14 TRP CZ2 C 114.716 0.120 1 104 14 14 TRP CZ3 C 120.451 0.045 1 105 14 14 TRP CH2 C 122.811 0.086 1 106 14 14 TRP N N 117.681 0.077 1 107 14 14 TRP NE1 N 129.654 0.023 1 108 15 15 GLY H H 8.036 0.012 1 109 15 15 GLY HA2 H 3.915 0.001 2 110 15 15 GLY CA C 46.894 0.067 1 111 15 15 GLY N N 105.952 0.055 1 112 16 16 LYS H H 7.333 0.009 1 113 16 16 LYS HA H 4.135 0.008 1 114 16 16 LYS HB2 H 1.992 0.012 2 115 16 16 LYS HB3 H 1.856 0.001 2 116 16 16 LYS HG2 H 1.537 0.008 2 117 16 16 LYS HG3 H 1.492 0.018 2 118 16 16 LYS HD2 H 1.632 0.005 2 119 16 16 LYS HD3 H 1.575 0.000 2 120 16 16 LYS HE2 H 2.946 0.010 2 121 16 16 LYS CA C 56.998 0.071 1 122 16 16 LYS CB C 32.049 0.110 1 123 16 16 LYS CG C 25.020 0.134 1 124 16 16 LYS CD C 28.335 0.049 1 125 16 16 LYS CE C 42.237 0.031 1 126 16 16 LYS N N 119.990 0.026 1 127 17 17 VAL H H 7.515 0.007 1 128 17 17 VAL HA H 3.277 0.010 1 129 17 17 VAL HB H 1.554 0.011 1 130 17 17 VAL HG1 H 0.529 0.010 2 131 17 17 VAL HG2 H -0.017 0.008 2 132 17 17 VAL CA C 66.444 0.055 1 133 17 17 VAL CB C 31.037 0.089 1 134 17 17 VAL CG1 C 22.606 0.091 2 135 17 17 VAL CG2 C 20.377 0.106 2 136 17 17 VAL N N 121.012 0.042 1 137 18 18 GLY H H 7.202 0.007 1 138 18 18 GLY HA2 H 3.607 0.018 2 139 18 18 GLY CA C 47.329 0.067 1 140 18 18 GLY N N 102.927 0.038 1 141 19 19 ALA HA H 4.096 0.007 1 142 19 19 ALA HB H 1.158 0.012 1 143 19 19 ALA CA C 53.424 0.065 1 144 19 19 ALA CB C 18.346 0.074 1 145 20 20 HIS H H 7.775 0.009 1 146 20 20 HIS HA H 4.336 0.016 1 147 20 20 HIS HB2 H 2.367 0.008 2 148 20 20 HIS HB3 H 1.993 0.000 2 149 20 20 HIS HD2 H 7.110 0.011 1 150 20 20 HIS HE1 H 8.079 0.000 1 151 20 20 HIS CA C 55.806 0.154 1 152 20 20 HIS CB C 29.046 0.059 1 153 20 20 HIS CD2 C 121.690 0.093 1 154 20 20 HIS CE1 C 137.887 0.000 1 155 20 20 HIS N N 115.262 0.057 1 156 21 21 ALA H H 7.026 0.007 1 157 21 21 ALA HA H 3.133 0.011 1 158 21 21 ALA HB H 1.272 0.010 1 159 21 21 ALA CA C 56.702 0.072 1 160 21 21 ALA CB C 18.621 0.124 1 161 21 21 ALA N N 121.980 0.060 1 162 22 22 GLY H H 8.487 0.009 1 163 22 22 GLY HA2 H 3.652 0.038 2 164 22 22 GLY CA C 47.598 0.205 1 165 22 22 GLY N N 104.309 0.148 1 166 23 23 GLU H H 7.747 0.007 1 167 23 23 GLU HA H 3.926 0.005 1 168 23 23 GLU HB2 H 1.976 0.018 2 169 23 23 GLU HB3 H 1.918 0.006 2 170 23 23 GLU HG2 H 2.207 0.016 2 171 23 23 GLU HG3 H 2.162 0.000 2 172 23 23 GLU CA C 59.204 0.074 1 173 23 23 GLU CB C 29.158 0.100 1 174 23 23 GLU CG C 36.198 0.091 1 175 23 23 GLU N N 124.174 0.064 1 176 24 24 TYR H H 8.012 0.012 1 177 24 24 TYR HA H 4.313 0.008 1 178 24 24 TYR HD1 H 6.321 0.009 3 179 24 24 TYR HE1 H 6.101 0.003 3 180 24 24 TYR CA C 57.295 0.074 1 181 24 24 TYR CD1 C 130.717 0.171 3 182 24 24 TYR CE1 C 117.524 0.065 3 183 24 24 TYR N N 120.893 0.087 1 184 25 25 GLY H H 8.843 0.009 1 185 25 25 GLY HA2 H 3.237 0.001 2 186 25 25 GLY HA3 H 3.634 0.013 2 187 25 25 GLY CA C 46.897 0.094 1 188 25 25 GLY N N 107.738 0.046 1 189 26 26 ALA H H 7.772 0.004 1 190 26 26 ALA HA H 3.587 0.013 1 191 26 26 ALA HB H 1.416 0.012 1 192 26 26 ALA CA C 55.071 0.069 1 193 26 26 ALA CB C 19.366 0.088 1 194 26 26 ALA N N 121.351 0.024 1 195 27 27 GLU H H 7.903 0.008 1 196 27 27 GLU HA H 3.938 0.008 1 197 27 27 GLU HB2 H 2.211 0.014 2 198 27 27 GLU HG2 H 2.408 0.000 2 199 27 27 GLU CA C 59.248 0.099 1 200 27 27 GLU CB C 29.494 0.048 1 201 27 27 GLU CG C 37.646 0.000 1 202 27 27 GLU N N 119.488 0.039 1 203 28 28 ALA H H 8.371 0.007 1 204 28 28 ALA HA H 3.470 0.019 1 205 28 28 ALA HB H 1.130 0.008 1 206 28 28 ALA CA C 55.939 0.083 1 207 28 28 ALA CB C 17.804 0.111 1 208 28 28 ALA N N 121.871 0.054 1 209 29 29 LEU H H 7.076 0.007 1 210 29 29 LEU HA H 2.934 0.010 1 211 29 29 LEU HB2 H 1.370 0.000 2 212 29 29 LEU HB3 H 1.444 0.000 2 213 29 29 LEU HG H 0.966 0.005 1 214 29 29 LEU HD1 H -0.221 0.006 2 215 29 29 LEU HD2 H -0.851 0.009 2 216 29 29 LEU CA C 57.627 0.143 1 217 29 29 LEU CB C 40.606 0.084 1 218 29 29 LEU CG C 25.906 0.187 1 219 29 29 LEU CD1 C 26.459 0.103 2 220 29 29 LEU CD2 C 21.185 0.059 2 221 29 29 LEU N N 115.704 0.044 1 222 30 30 GLU H H 7.838 0.003 1 223 30 30 GLU HA H 3.797 0.015 1 224 30 30 GLU HB2 H 1.999 0.011 2 225 30 30 GLU HG2 H 2.409 0.014 2 226 30 30 GLU HG3 H 1.967 0.011 2 227 30 30 GLU CA C 60.610 0.141 1 228 30 30 GLU CB C 29.695 0.089 1 229 30 30 GLU CG C 36.901 0.124 1 230 30 30 GLU N N 118.191 0.057 1 231 31 31 ARG H H 8.711 0.004 1 232 31 31 ARG HA H 3.688 0.052 1 233 31 31 ARG CA C 60.694 0.016 1 234 31 31 ARG N N 116.389 0.049 1 235 32 32 MET H H 7.981 0.004 1 236 32 32 MET HA H 4.044 0.011 1 237 32 32 MET HE H 1.151 0.010 1 238 32 32 MET CA C 60.566 0.074 1 239 32 32 MET CE C 16.122 0.089 1 240 32 32 MET N N 123.049 0.036 1 241 33 33 PHE H H 8.427 0.008 1 242 33 33 PHE HA H 4.300 0.001 1 243 33 33 PHE HB2 H 2.871 0.000 2 244 33 33 PHE HB3 H 2.860 0.000 2 245 33 33 PHE HD1 H 6.923 0.000 3 246 33 33 PHE CA C 58.757 0.109 1 247 33 33 PHE CB C 38.125 0.005 1 248 33 33 PHE CD1 C 131.065 0.000 3 249 33 33 PHE N N 118.363 0.081 1 250 34 34 LEU H H 7.683 0.010 1 251 34 34 LEU HA H 4.161 0.014 1 252 34 34 LEU HB2 H 1.294 0.011 2 253 34 34 LEU HB3 H 1.543 0.017 2 254 34 34 LEU HG H 1.709 0.013 1 255 34 34 LEU HD1 H 0.713 0.013 2 256 34 34 LEU HD2 H 0.735 0.013 2 257 34 34 LEU CA C 56.883 0.121 1 258 34 34 LEU CB C 43.305 0.108 1 259 34 34 LEU CG C 27.268 0.136 1 260 34 34 LEU CD1 C 25.605 0.078 2 261 34 34 LEU CD2 C 23.591 0.093 2 262 34 34 LEU N N 114.109 0.050 1 263 35 35 SER H H 7.983 0.012 1 264 35 35 SER HA H 3.824 0.014 1 265 35 35 SER HB2 H 3.389 0.036 2 266 35 35 SER CA C 62.956 0.100 1 267 35 35 SER CB C 64.530 0.071 1 268 35 35 SER N N 112.887 0.064 1 269 36 36 PHE H H 8.381 0.007 1 270 36 36 PHE HA H 5.366 0.009 1 271 36 36 PHE HB2 H 3.233 0.000 2 272 36 36 PHE HD1 H 7.323 0.051 3 273 36 36 PHE CA C 54.600 0.131 1 274 36 36 PHE CB C 39.552 0.000 1 275 36 36 PHE CD1 C 134.665 0.501 3 276 36 36 PHE N N 117.621 0.048 1 277 37 37 PRO HG2 H 2.070 0.020 2 278 37 37 PRO HD2 H 3.418 0.005 2 279 37 37 PRO HD3 H 3.804 0.022 2 280 37 37 PRO CG C 27.602 0.099 1 281 37 37 PRO CD C 50.837 0.137 1 282 38 38 THR H H 8.376 0.008 1 283 38 38 THR HA H 4.105 0.014 1 284 38 38 THR HB H 4.484 0.007 1 285 38 38 THR HG2 H 1.348 0.013 1 286 38 38 THR CA C 65.837 0.054 1 287 38 38 THR CB C 68.101 0.011 1 288 38 38 THR CG2 C 23.270 0.092 1 289 38 38 THR N N 113.016 0.107 1 290 39 39 THR H H 8.885 0.005 1 291 39 39 THR HA H 4.471 0.012 1 292 39 39 THR HB H 4.571 0.010 1 293 39 39 THR HG2 H 1.815 0.007 1 294 39 39 THR CA C 66.703 0.103 1 295 39 39 THR CB C 70.912 0.062 1 296 39 39 THR CG2 C 23.180 0.061 1 297 39 39 THR N N 115.055 0.096 1 298 40 40 LYS H H 7.791 0.007 1 299 40 40 LYS HA H 3.904 0.009 1 300 40 40 LYS HB2 H 2.003 0.000 2 301 40 40 LYS HB3 H 1.747 0.000 2 302 40 40 LYS HG2 H 1.075 0.000 2 303 40 40 LYS HG3 H 1.811 0.000 2 304 40 40 LYS HD2 H 1.662 0.000 2 305 40 40 LYS HD3 H 1.731 0.000 2 306 40 40 LYS HE2 H 2.880 0.017 2 307 40 40 LYS CA C 59.840 0.055 1 308 40 40 LYS CB C 29.569 0.036 1 309 40 40 LYS CG C 26.450 0.009 1 310 40 40 LYS CD C 29.771 0.029 1 311 40 40 LYS CE C 41.798 0.017 1 312 40 40 LYS N N 118.342 0.047 1 313 41 41 THR H H 7.833 0.006 1 314 41 41 THR HA H 4.050 0.024 1 315 41 41 THR HB H 4.255 0.014 1 316 41 41 THR HG2 H 1.183 0.007 1 317 41 41 THR CA C 64.608 0.047 1 318 41 41 THR CB C 69.505 0.027 1 319 41 41 THR CG2 C 21.443 0.112 1 320 41 41 THR N N 111.203 0.086 1 321 42 42 TYR H H 7.512 0.007 1 322 42 42 TYR HA H 4.474 0.010 1 323 42 42 TYR HD1 H 7.699 0.008 3 324 42 42 TYR HE1 H 7.120 0.003 3 325 42 42 TYR CA C 60.613 0.029 1 326 42 42 TYR CD1 C 133.178 0.164 3 327 42 42 TYR CE1 C 121.710 0.042 3 328 42 42 TYR N N 116.894 0.037 1 329 43 43 PHE H H 7.835 0.009 1 330 43 43 PHE HA H 4.861 0.000 1 331 43 43 PHE HB2 H 2.337 0.004 2 332 43 43 PHE HD1 H 6.098 0.000 3 333 43 43 PHE CA C 55.335 0.015 1 334 43 43 PHE CB C 40.195 0.060 1 335 43 43 PHE CD1 C 132.720 0.000 3 336 43 43 PHE N N 116.967 0.080 1 337 44 44 PRO HA H 4.457 0.000 1 338 44 44 PRO HG2 H 2.058 0.000 2 339 44 44 PRO HD2 H 3.793 0.052 2 340 44 44 PRO CA C 65.444 0.036 1 341 44 44 PRO CG C 27.490 0.000 1 342 44 44 PRO CD C 50.697 0.016 1 343 45 45 HIS H H 9.554 0.012 1 344 45 45 HIS HA H 4.830 0.014 1 345 45 45 HIS HB2 H 3.275 0.026 2 346 45 45 HIS HB3 H 3.184 0.000 2 347 45 45 HIS HE1 H 7.902 0.007 1 348 45 45 HIS CA C 55.482 0.104 1 349 45 45 HIS CB C 30.010 0.030 1 350 45 45 HIS CE1 C 138.606 0.029 1 351 45 45 HIS N N 116.698 0.080 1 352 46 46 PHE H H 7.501 0.004 1 353 46 46 PHE HA H 4.614 0.028 1 354 46 46 PHE HB2 H 2.263 0.000 2 355 46 46 PHE HB3 H 3.086 0.000 2 356 46 46 PHE HD1 H 6.439 0.018 3 357 46 46 PHE HE1 H 6.769 0.010 3 358 46 46 PHE CA C 55.952 0.079 1 359 46 46 PHE CB C 40.294 0.005 1 360 46 46 PHE CD1 C 129.576 0.139 3 361 46 46 PHE CE1 C 131.690 0.076 3 362 46 46 PHE N N 122.647 0.077 1 363 47 47 ASP H H 7.930 0.005 1 364 47 47 ASP HA H 4.555 0.015 1 365 47 47 ASP HB2 H 2.748 0.036 2 366 47 47 ASP HB3 H 2.770 0.000 2 367 47 47 ASP CA C 53.658 0.059 1 368 47 47 ASP CB C 40.234 0.158 1 369 47 47 ASP N N 119.257 0.063 1 370 48 48 LEU H H 8.528 0.008 1 371 48 48 LEU HA H 4.361 0.081 1 372 48 48 LEU HB2 H 1.312 0.033 2 373 48 48 LEU HG H 1.282 0.008 1 374 48 48 LEU HD1 H -0.113 0.011 2 375 48 48 LEU HD2 H 0.258 0.009 2 376 48 48 LEU CA C 53.589 0.049 1 377 48 48 LEU CB C 40.677 0.122 1 378 48 48 LEU CG C 25.700 0.050 1 379 48 48 LEU CD1 C 23.987 0.117 2 380 48 48 LEU CD2 C 25.796 0.087 2 381 48 48 LEU N N 128.099 0.038 1 382 49 49 SER H H 8.194 0.007 1 383 49 49 SER HA H 4.085 0.009 1 384 49 49 SER HB2 H 3.888 0.023 2 385 49 49 SER HB3 H 3.807 0.000 2 386 49 49 SER CA C 59.294 0.042 1 387 49 49 SER CB C 64.211 0.038 1 388 49 49 SER N N 117.233 0.060 1 389 50 50 HIS HA H 4.306 0.009 1 390 50 50 HIS HB2 H 3.129 0.006 2 391 50 50 HIS HB3 H 2.983 0.009 2 392 50 50 HIS HD2 H 7.003 0.001 1 393 50 50 HIS HE1 H 8.025 0.000 1 394 50 50 HIS CA C 58.051 0.040 1 395 50 50 HIS CB C 28.953 0.038 1 396 50 50 HIS CD2 C 121.651 0.037 1 397 50 50 HIS CE1 C 138.349 0.000 1 398 51 51 GLY H H 9.002 0.008 1 399 51 51 GLY HA2 H 3.771 0.010 2 400 51 51 GLY HA3 H 3.350 0.022 2 401 51 51 GLY CA C 45.301 0.078 1 402 51 51 GLY N N 116.049 0.042 1 403 52 52 SER H H 7.433 0.006 1 404 52 52 SER HA H 4.046 0.013 1 405 52 52 SER HB2 H 4.071 0.020 2 406 52 52 SER HB3 H 3.631 0.005 2 407 52 52 SER CA C 57.185 0.061 1 408 52 52 SER CB C 64.964 0.123 1 409 52 52 SER N N 114.415 0.026 1 410 53 53 ALA H H 9.088 0.013 1 411 53 53 ALA HA H 4.006 0.026 1 412 53 53 ALA HB H 1.415 0.015 1 413 53 53 ALA CA C 54.943 0.099 1 414 53 53 ALA CB C 18.293 0.084 1 415 53 53 ALA N N 131.667 0.068 1 416 54 54 GLN H H 8.298 0.008 1 417 54 54 GLN HA H 3.885 0.013 1 418 54 54 GLN HB2 H 1.721 0.031 2 419 54 54 GLN HB3 H 1.252 0.015 2 420 54 54 GLN HG2 H 2.108 0.017 2 421 54 54 GLN HG3 H 1.685 0.011 2 422 54 54 GLN HE21 H 6.645 0.000 2 423 54 54 GLN HE22 H 7.270 0.018 2 424 54 54 GLN CA C 59.033 0.067 1 425 54 54 GLN CB C 28.800 0.106 1 426 54 54 GLN CG C 34.239 0.071 1 427 54 54 GLN N N 120.096 0.080 1 428 54 54 GLN NE2 N 113.068 0.112 1 429 55 55 VAL H H 7.540 0.007 1 430 55 55 VAL HA H 3.212 0.012 1 431 55 55 VAL HB H 1.964 0.017 1 432 55 55 VAL HG1 H 0.764 0.006 2 433 55 55 VAL HG2 H 0.961 0.006 2 434 55 55 VAL CA C 67.423 0.116 1 435 55 55 VAL CB C 31.825 0.119 1 436 55 55 VAL CG1 C 22.032 0.110 2 437 55 55 VAL CG2 C 24.524 0.105 2 438 55 55 VAL N N 121.775 0.062 1 439 56 56 LYS H H 7.735 0.009 1 440 56 56 LYS HA H 3.770 0.023 1 441 56 56 LYS HB2 H 1.728 0.018 2 442 56 56 LYS HB3 H 1.683 0.008 2 443 56 56 LYS HG2 H 1.337 0.019 2 444 56 56 LYS HG3 H 1.176 0.006 2 445 56 56 LYS HD2 H 1.475 0.016 2 446 56 56 LYS HE2 H 2.784 0.020 2 447 56 56 LYS CA C 60.067 0.070 1 448 56 56 LYS CB C 32.208 0.071 1 449 56 56 LYS CG C 25.460 0.082 1 450 56 56 LYS CD C 29.348 0.080 1 451 56 56 LYS CE C 41.978 0.030 1 452 56 56 LYS N N 120.062 0.092 1 453 57 57 GLY H H 8.256 0.003 1 454 57 57 GLY HA2 H 3.857 0.018 2 455 57 57 GLY HA3 H 3.985 0.000 2 456 57 57 GLY CA C 46.985 0.064 1 457 57 57 GLY N N 106.072 0.055 1 458 58 58 HIS H H 8.185 0.008 1 459 58 58 HIS HA H 3.902 0.031 1 460 58 58 HIS HB2 H 2.952 0.016 2 461 58 58 HIS HB3 H 2.251 0.010 2 462 58 58 HIS HD2 H 4.500 0.005 1 463 58 58 HIS HE1 H 8.269 0.004 1 464 58 58 HIS CA C 60.148 0.114 1 465 58 58 HIS CB C 31.116 0.125 1 466 58 58 HIS CD2 C 114.291 0.000 1 467 58 58 HIS CE1 C 139.059 0.040 1 468 58 58 HIS N N 124.485 0.067 1 469 59 59 GLY H H 8.556 0.008 1 470 59 59 GLY HA2 H 3.164 0.037 2 471 59 59 GLY HA3 H 2.741 0.002 2 472 59 59 GLY CA C 46.493 0.146 1 473 59 59 GLY N N 105.531 0.129 1 474 60 60 LYS H H 7.072 0.010 1 475 60 60 LYS HA H 3.944 0.012 1 476 60 60 LYS HB2 H 1.994 0.005 2 477 60 60 LYS HB3 H 1.817 0.000 2 478 60 60 LYS HG2 H 1.421 0.004 2 479 60 60 LYS HD2 H 1.757 0.000 2 480 60 60 LYS HD3 H 1.567 0.000 2 481 60 60 LYS HE2 H 3.032 0.000 2 482 60 60 LYS CA C 59.699 0.156 1 483 60 60 LYS CB C 32.224 0.091 1 484 60 60 LYS CG C 25.270 0.093 1 485 60 60 LYS CD C 29.046 0.034 1 486 60 60 LYS CE C 42.315 0.000 1 487 60 60 LYS N N 120.115 0.026 1 488 61 61 LYS H H 6.982 0.008 1 489 61 61 LYS HA H 4.297 0.011 1 490 61 61 LYS HB2 H 1.967 0.000 2 491 61 61 LYS HB3 H 1.558 0.000 2 492 61 61 LYS HG2 H 1.644 0.000 2 493 61 61 LYS HE2 H 3.096 0.000 2 494 61 61 LYS CA C 60.359 0.040 1 495 61 61 LYS CB C 32.181 0.078 1 496 61 61 LYS CG C 26.141 0.000 1 497 61 61 LYS CE C 42.556 0.000 1 498 61 61 LYS N N 118.339 0.048 1 499 62 62 VAL H H 7.751 0.006 1 500 62 62 VAL HA H 3.637 0.020 1 501 62 62 VAL HB H 1.222 0.012 1 502 62 62 VAL HG1 H -1.763 0.011 2 503 62 62 VAL HG2 H 0.100 0.006 2 504 62 62 VAL CA C 67.140 0.057 1 505 62 62 VAL CB C 31.590 0.105 1 506 62 62 VAL CG1 C 21.526 0.122 2 507 62 62 VAL CG2 C 19.117 0.114 2 508 62 62 VAL N N 120.323 0.072 1 509 63 63 ALA H H 8.145 0.012 1 510 63 63 ALA HA H 4.174 0.014 1 511 63 63 ALA HB H 1.516 0.018 1 512 63 63 ALA CA C 56.071 0.100 1 513 63 63 ALA CB C 19.501 0.128 1 514 63 63 ALA N N 120.978 0.028 1 515 64 64 ASP H H 8.913 0.007 1 516 64 64 ASP HA H 4.592 0.012 1 517 64 64 ASP HB2 H 3.023 0.007 2 518 64 64 ASP HB3 H 2.827 0.022 2 519 64 64 ASP CA C 57.765 0.093 1 520 64 64 ASP CB C 40.032 0.140 1 521 64 64 ASP N N 119.821 0.033 1 522 65 65 ALA H H 8.331 0.007 1 523 65 65 ALA HA H 4.682 0.021 1 524 65 65 ALA HB H 2.431 0.007 1 525 65 65 ALA CA C 55.588 0.099 1 526 65 65 ALA CB C 20.331 0.090 1 527 65 65 ALA N N 124.579 0.036 1 528 66 66 LEU H H 8.482 0.007 1 529 66 66 LEU HA H 4.186 0.012 1 530 66 66 LEU HB2 H 0.775 0.000 2 531 66 66 LEU HB3 H 2.263 0.003 2 532 66 66 LEU HG H 2.231 0.000 1 533 66 66 LEU HD1 H 0.943 0.017 2 534 66 66 LEU HD2 H 0.873 0.023 2 535 66 66 LEU CA C 58.446 0.092 1 536 66 66 LEU CB C 41.561 0.081 1 537 66 66 LEU CG C 27.200 0.000 1 538 66 66 LEU CD1 C 23.285 0.160 2 539 66 66 LEU CD2 C 26.841 0.180 2 540 66 66 LEU N N 119.336 0.075 1 541 67 67 THR H H 9.123 0.010 1 542 67 67 THR HA H 3.839 0.011 1 543 67 67 THR HB H 4.684 0.025 1 544 67 67 THR HG2 H 1.441 0.012 1 545 67 67 THR CA C 67.329 0.075 1 546 67 67 THR CB C 68.787 0.027 1 547 67 67 THR CG2 C 22.819 0.045 1 548 67 67 THR N N 118.175 0.081 1 549 68 68 ASN H H 8.118 0.009 1 550 68 68 ASN HA H 4.719 0.010 1 551 68 68 ASN HB2 H 3.163 0.023 2 552 68 68 ASN HB3 H 3.079 0.020 2 553 68 68 ASN HD21 H 6.917 0.008 1 554 68 68 ASN HD22 H 7.782 0.007 1 555 68 68 ASN CA C 56.645 0.075 1 556 68 68 ASN CB C 38.918 0.054 1 557 68 68 ASN N N 121.266 0.030 1 558 68 68 ASN ND2 N 112.723 0.053 1 559 69 69 ALA H H 8.562 0.008 1 560 69 69 ALA HA H 3.873 0.010 1 561 69 69 ALA HB H 1.730 0.008 1 562 69 69 ALA CA C 56.170 0.090 1 563 69 69 ALA CB C 18.505 0.052 1 564 69 69 ALA N N 123.259 0.050 1 565 70 70 VAL H H 8.257 0.013 1 566 70 70 VAL HA H 3.190 0.021 1 567 70 70 VAL HB H 1.939 0.009 1 568 70 70 VAL HG1 H 0.151 0.011 2 569 70 70 VAL HG2 H 0.733 0.014 2 570 70 70 VAL CA C 67.172 0.062 1 571 70 70 VAL CB C 32.084 0.072 1 572 70 70 VAL CG1 C 23.115 0.133 2 573 70 70 VAL CG2 C 22.588 0.131 2 574 70 70 VAL N N 116.721 0.056 1 575 71 71 ALA H H 7.721 0.014 1 576 71 71 ALA HA H 4.021 0.009 1 577 71 71 ALA HB H 1.371 0.005 1 578 71 71 ALA CA C 54.395 0.074 1 579 71 71 ALA CB C 18.258 0.105 1 580 71 71 ALA N N 120.193 0.063 1 581 72 72 HIS H H 7.699 0.006 1 582 72 72 HIS HA H 4.883 0.009 1 583 72 72 HIS HB2 H 2.561 0.000 2 584 72 72 HIS HB3 H 3.434 0.000 2 585 72 72 HIS HD2 H 7.403 0.024 1 586 72 72 HIS HE1 H 8.277 0.004 1 587 72 72 HIS CA C 55.111 0.061 1 588 72 72 HIS CB C 28.473 0.096 1 589 72 72 HIS CD2 C 122.232 0.096 1 590 72 72 HIS CE1 C 137.512 0.032 1 591 72 72 HIS N N 116.005 0.070 1 592 73 73 VAL H H 6.665 0.010 1 593 73 73 VAL HA H 4.123 0.009 1 594 73 73 VAL HB H 2.527 0.008 1 595 73 73 VAL HG1 H 0.976 0.006 2 596 73 73 VAL HG2 H 1.131 0.007 2 597 73 73 VAL CA C 65.464 0.107 1 598 73 73 VAL CB C 32.218 0.056 1 599 73 73 VAL CG1 C 20.481 0.091 2 600 73 73 VAL CG2 C 22.814 0.079 2 601 73 73 VAL N N 119.790 0.028 1 602 74 74 ASP H H 8.242 0.009 1 603 74 74 ASP HA H 4.830 0.019 1 604 74 74 ASP HB2 H 2.511 0.014 2 605 74 74 ASP HB3 H 2.916 0.030 2 606 74 74 ASP CA C 55.383 0.109 1 607 74 74 ASP CB C 41.453 0.125 1 608 74 74 ASP N N 119.560 0.030 1 609 75 75 ASP H H 8.351 0.004 1 610 75 75 ASP HA H 5.042 0.012 1 611 75 75 ASP HB2 H 2.471 0.005 2 612 75 75 ASP HB3 H 2.688 0.000 2 613 75 75 ASP CA C 53.184 0.063 1 614 75 75 ASP CB C 41.848 0.019 1 615 75 75 ASP N N 122.432 0.053 1 616 76 76 MET H H 8.672 0.009 1 617 76 76 MET HA H 4.036 0.013 1 618 76 76 MET HB2 H 2.919 0.008 2 619 76 76 MET HB3 H 2.325 0.011 2 620 76 76 MET HG2 H 1.796 0.010 2 621 76 76 MET HG3 H 2.342 0.011 2 622 76 76 MET HE H 2.063 0.009 1 623 76 76 MET CA C 62.211 0.042 1 624 76 76 MET CB C 33.988 0.087 1 625 76 76 MET CG C 33.080 0.090 1 626 76 76 MET CE C 17.261 0.065 1 627 76 76 MET N N 121.791 0.088 1 628 77 77 PRO HD2 H 3.757 0.000 1 629 77 77 PRO CA C 66.096 0.000 1 630 77 77 PRO CD C 50.274 0.000 1 631 78 78 ASN H H 7.461 0.006 1 632 78 78 ASN HA H 4.549 0.012 1 633 78 78 ASN HB2 H 2.762 0.019 2 634 78 78 ASN HB3 H 2.692 0.001 2 635 78 78 ASN HD21 H 6.912 0.000 2 636 78 78 ASN HD22 H 8.460 0.000 2 637 78 78 ASN CA C 55.803 0.128 1 638 78 78 ASN CB C 38.961 0.051 1 639 78 78 ASN N N 113.172 0.083 1 640 78 78 ASN ND2 N 115.698 0.001 1 641 79 79 ALA H H 7.904 0.008 1 642 79 79 ALA HA H 4.041 0.016 1 643 79 79 ALA HB H 1.207 0.033 1 644 79 79 ALA CA C 54.884 0.090 1 645 79 79 ALA CB C 18.767 0.097 1 646 79 79 ALA N N 121.971 0.040 1 647 80 80 LEU H H 8.091 0.012 1 648 80 80 LEU HA H 4.629 0.016 1 649 80 80 LEU HB2 H 1.608 0.012 2 650 80 80 LEU HG H 1.693 0.016 1 651 80 80 LEU HD1 H 0.888 0.009 2 652 80 80 LEU HD2 H 0.808 0.012 2 653 80 80 LEU CA C 53.965 0.109 1 654 80 80 LEU CB C 41.544 0.000 1 655 80 80 LEU CG C 27.811 0.079 1 656 80 80 LEU CD1 C 22.948 0.106 2 657 80 80 LEU CD2 C 26.517 0.092 2 658 80 80 LEU N N 113.630 0.070 1 659 81 81 SER H H 7.102 0.009 1 660 81 81 SER HA H 4.027 0.018 1 661 81 81 SER HB2 H 3.961 0.000 2 662 81 81 SER CA C 62.705 0.131 1 663 81 81 SER CB C 62.777 0.000 1 664 81 81 SER N N 116.611 0.039 1 665 82 82 ALA HA H 4.153 0.011 1 666 82 82 ALA HB H 1.400 0.014 1 667 82 82 ALA CA C 55.212 0.047 1 668 82 82 ALA CB C 18.004 0.071 1 669 83 83 LEU H H 7.506 0.008 1 670 83 83 LEU HA H 3.704 0.018 1 671 83 83 LEU HB2 H 1.674 0.027 2 672 83 83 LEU HB3 H 0.435 0.019 2 673 83 83 LEU HG H 1.556 0.021 1 674 83 83 LEU HD1 H 0.747 0.005 2 675 83 83 LEU HD2 H 1.190 0.007 2 676 83 83 LEU CA C 56.177 0.088 1 677 83 83 LEU CB C 41.913 0.122 1 678 83 83 LEU CG C 26.812 0.127 1 679 83 83 LEU CD1 C 23.657 0.121 2 680 83 83 LEU CD2 C 26.838 0.141 2 681 83 83 LEU N N 117.731 0.043 1 682 84 84 SER H H 8.238 0.005 1 683 84 84 SER HA H 4.045 0.006 1 684 84 84 SER HB2 H 3.833 0.007 2 685 84 84 SER CA C 60.857 0.054 1 686 84 84 SER CB C 62.207 0.009 1 687 84 84 SER N N 121.307 0.068 1 688 85 85 ASP H H 7.622 0.008 1 689 85 85 ASP HA H 4.067 0.013 1 690 85 85 ASP HB2 H 2.543 0.012 2 691 85 85 ASP HB3 H 2.502 0.000 2 692 85 85 ASP CA C 57.984 0.089 1 693 85 85 ASP CB C 40.898 0.066 1 694 85 85 ASP N N 121.403 0.040 1 695 86 86 LEU H H 7.072 0.006 1 696 86 86 LEU HA H 3.721 0.014 1 697 86 86 LEU HB2 H 1.282 0.000 2 698 86 86 LEU HG H -0.147 0.007 1 699 86 86 LEU HD1 H 0.607 0.014 2 700 86 86 LEU HD2 H -0.040 0.006 2 701 86 86 LEU CA C 57.826 0.088 1 702 86 86 LEU CB C 42.197 0.000 1 703 86 86 LEU CG C 26.367 0.016 1 704 86 86 LEU CD1 C 23.050 0.058 2 705 86 86 LEU CD2 C 27.227 0.056 2 706 86 86 LEU N N 116.255 0.060 1 707 87 87 HIS H H 7.238 0.004 1 708 87 87 HIS HB3 H 2.263 0.000 2 709 87 87 HIS HD1 H 9.433 0.007 1 710 87 87 HIS HD2 H 1.000 0.000 1 711 87 87 HIS HE1 H 1.436 0.008 1 712 87 87 HIS CA C 61.268 0.000 1 713 87 87 HIS CB C 31.087 0.000 1 714 87 87 HIS CD2 C 122.957 0.000 1 715 87 87 HIS CE1 C 132.612 0.108 1 716 87 87 HIS N N 112.288 0.085 1 717 87 87 HIS ND1 N 163.386 0.073 1 718 87 87 HIS NE2 N 218.348 0.000 1 719 88 88 ALA HA H 4.387 0.009 1 720 88 88 ALA HB H 0.779 0.031 1 721 88 88 ALA CA C 53.506 0.073 1 722 88 88 ALA CB C 19.243 0.101 1 723 89 89 HIS H H 7.216 0.009 1 724 89 89 HIS HA H 4.492 0.006 1 725 89 89 HIS HB2 H 3.293 0.035 1 726 89 89 HIS HB3 H 3.162 0.000 1 727 89 89 HIS HD2 H 6.925 0.000 1 728 89 89 HIS HE1 H 7.704 0.000 1 729 89 89 HIS CA C 58.336 0.056 1 730 89 89 HIS CB C 31.158 0.064 1 731 89 89 HIS CD2 C 115.699 0.000 1 732 89 89 HIS CE1 C 138.208 0.000 1 733 89 89 HIS N N 114.928 0.019 1 734 90 90 LYS H H 7.430 0.008 1 735 90 90 LYS HA H 4.110 0.006 1 736 90 90 LYS HB2 H 1.940 0.008 2 737 90 90 LYS HG2 H 1.337 0.002 2 738 90 90 LYS HG3 H 1.195 0.002 1 739 90 90 LYS HD2 H 1.513 0.003 2 740 90 90 LYS HE2 H 2.865 0.005 2 741 90 90 LYS CA C 59.003 0.052 1 742 90 90 LYS CB C 32.434 0.063 1 743 90 90 LYS CG C 25.366 0.031 1 744 90 90 LYS CD C 29.103 0.024 1 745 90 90 LYS CE C 42.243 0.066 1 746 90 90 LYS N N 117.273 0.070 1 747 91 91 LEU HA H 4.105 0.009 1 748 91 91 LEU HG H 1.089 0.009 1 749 91 91 LEU HD1 H 0.942 0.005 2 750 91 91 LEU HD2 H -0.654 0.011 2 751 91 91 LEU CA C 55.968 0.066 1 752 91 91 LEU CG C 26.303 0.052 1 753 91 91 LEU CD1 C 22.366 0.072 2 754 91 91 LEU CD2 C 25.302 0.051 2 755 92 92 ARG H H 6.488 0.010 1 756 92 92 ARG HA H 3.884 0.027 1 757 92 92 ARG HB2 H 1.356 0.000 2 758 92 92 ARG HB3 H 1.720 0.000 2 759 92 92 ARG HG2 H 0.283 0.000 2 760 92 92 ARG HG3 H 0.974 0.000 2 761 92 92 ARG HD2 H 3.068 0.000 2 762 92 92 ARG CA C 57.342 0.065 1 763 92 92 ARG CB C 27.795 0.024 1 764 92 92 ARG CG C 21.836 0.021 1 765 92 92 ARG CD C 44.535 0.000 1 766 92 92 ARG N N 111.608 0.052 1 767 93 93 VAL H H 7.486 0.015 1 768 93 93 VAL HA H 3.774 0.008 1 769 93 93 VAL HB H 1.402 0.021 1 770 93 93 VAL HG1 H 0.547 0.086 2 771 93 93 VAL HG2 H 0.284 0.014 2 772 93 93 VAL CA C 63.614 0.055 1 773 93 93 VAL CB C 32.500 0.086 1 774 93 93 VAL CG1 C 22.306 0.200 2 775 93 93 VAL CG2 C 22.118 0.041 2 776 93 93 VAL N N 115.834 0.050 1 777 94 94 ASP H H 7.674 0.022 1 778 94 94 ASP N N 129.626 0.049 1 779 96 96 VAL H H 8.970 0.009 1 780 96 96 VAL HA H 3.800 0.011 1 781 96 96 VAL HB H 2.052 0.012 1 782 96 96 VAL HG1 H 0.870 0.006 2 783 96 96 VAL HG2 H 0.925 0.008 2 784 96 96 VAL CA C 66.199 0.064 1 785 96 96 VAL CB C 31.450 0.094 1 786 96 96 VAL CG1 C 20.339 0.075 2 787 96 96 VAL CG2 C 21.021 0.108 2 788 96 96 VAL N N 120.185 0.071 1 789 97 97 ASN H H 8.343 0.008 1 790 97 97 ASN HA H 4.442 0.024 1 791 97 97 ASN HB2 H 2.536 0.000 2 792 97 97 ASN CA C 56.937 0.059 1 793 97 97 ASN CB C 40.380 0.000 1 794 97 97 ASN N N 116.564 0.071 1 795 98 98 PHE H H 7.900 0.008 1 796 98 98 PHE HA H 4.486 0.004 1 797 98 98 PHE HB2 H 3.248 0.000 2 798 98 98 PHE HD1 H 7.523 0.006 3 799 98 98 PHE HE1 H 6.287 0.007 3 800 98 98 PHE CA C 63.087 0.028 1 801 98 98 PHE CB C 37.034 0.000 1 802 98 98 PHE CD1 C 131.314 0.200 3 803 98 98 PHE CD2 C 131.002 0.000 1 804 98 98 PHE CE1 C 132.781 0.036 3 805 98 98 PHE N N 118.456 0.082 1 806 99 99 LYS H H 7.475 0.020 1 807 99 99 LYS HA H 4.366 0.016 1 808 99 99 LYS HB2 H 2.059 0.075 2 809 99 99 LYS HB3 H 1.930 0.020 2 810 99 99 LYS HG2 H 1.595 0.025 2 811 99 99 LYS HD2 H 1.726 0.008 2 812 99 99 LYS HE2 H 2.989 0.015 2 813 99 99 LYS CA C 59.661 0.051 1 814 99 99 LYS CB C 32.067 0.145 1 815 99 99 LYS CG C 25.825 0.016 1 816 99 99 LYS CD C 29.839 0.024 1 817 99 99 LYS CE C 42.173 0.054 1 818 99 99 LYS N N 121.173 0.080 1 819 100 100 LEU H H 7.359 0.005 1 820 100 100 LEU HA H 3.868 0.028 1 821 100 100 LEU HB2 H 1.814 0.000 2 822 100 100 LEU HG H 1.807 0.014 1 823 100 100 LEU HD1 H 0.678 0.010 2 824 100 100 LEU HD2 H -0.187 0.018 2 825 100 100 LEU CA C 57.841 0.071 1 826 100 100 LEU CB C 43.204 0.000 1 827 100 100 LEU CG C 25.280 0.101 1 828 100 100 LEU CD1 C 24.765 0.078 1 829 100 100 LEU CD2 C 19.500 0.090 1 830 100 100 LEU N N 119.418 0.053 1 831 101 101 LEU H H 8.197 0.008 1 832 101 101 LEU HA H 3.995 0.016 1 833 101 101 LEU HB2 H 1.736 0.000 2 834 101 101 LEU HB3 H 1.953 0.000 2 835 101 101 LEU HG H 1.411 0.025 1 836 101 101 LEU HD1 H 0.218 0.008 2 837 101 101 LEU HD2 H 0.358 0.010 2 838 101 101 LEU CA C 58.935 0.084 1 839 101 101 LEU CB C 41.489 0.313 1 840 101 101 LEU CG C 28.151 0.044 1 841 101 101 LEU CD1 C 26.420 0.111 2 842 101 101 LEU CD2 C 22.764 0.120 2 843 101 101 LEU N N 120.829 0.087 1 844 102 102 SER H H 8.379 0.005 1 845 102 102 SER HA H 4.171 0.038 1 846 102 102 SER HB2 H 4.188 0.000 1 847 102 102 SER CA C 63.694 0.654 1 848 102 102 SER CB C 63.853 0.000 1 849 102 102 SER N N 114.839 0.083 1 850 103 103 HIS H H 7.806 0.008 1 851 103 103 HIS HA H 4.551 0.010 1 852 103 103 HIS HB2 H 3.331 0.029 2 853 103 103 HIS HD2 H 6.725 0.005 1 854 103 103 HIS HE1 H 8.130 0.010 1 855 103 103 HIS HE2 H 12.080 0.009 1 856 103 103 HIS CA C 60.095 0.044 1 857 103 103 HIS CB C 31.279 0.076 1 858 103 103 HIS CD2 C 115.747 0.032 1 859 103 103 HIS CE1 C 139.214 0.038 1 860 103 103 HIS N N 119.663 0.096 1 861 103 103 HIS NE2 N 163.856 0.000 1 862 104 104 CYS H H 7.882 0.006 1 863 104 104 CYS HA H 3.764 0.023 1 864 104 104 CYS CA C 66.052 0.155 1 865 104 104 CYS N N 114.982 0.078 1 866 105 105 LEU H H 8.904 0.009 1 867 105 105 LEU HA H 3.964 0.011 1 868 105 105 LEU HB2 H 1.613 0.003 2 869 105 105 LEU HB3 H 1.864 0.021 2 870 105 105 LEU HG H 1.517 0.016 1 871 105 105 LEU HD1 H 0.849 0.014 2 872 105 105 LEU HD2 H 0.872 0.001 2 873 105 105 LEU CA C 58.822 0.175 1 874 105 105 LEU CB C 42.013 0.096 1 875 105 105 LEU CG C 27.922 0.083 1 876 105 105 LEU CD1 C 24.998 0.127 2 877 105 105 LEU CD2 C 25.208 0.029 2 878 105 105 LEU N N 125.054 0.039 1 879 106 106 LEU HA H 3.926 0.088 1 880 106 106 LEU HD1 H 0.972 0.000 2 881 106 106 LEU HD2 H 1.273 0.000 2 882 106 106 LEU CA C 59.277 0.184 1 883 106 106 LEU CD1 C 24.598 0.049 2 884 106 106 LEU CD2 C 27.218 0.000 2 885 107 107 VAL H H 8.224 0.007 1 886 107 107 VAL HA H 2.939 0.008 1 887 107 107 VAL HB H 1.700 0.020 1 888 107 107 VAL HG1 H 0.675 0.007 2 889 107 107 VAL HG2 H 0.518 0.010 2 890 107 107 VAL CA C 67.153 0.124 1 891 107 107 VAL CB C 32.279 0.151 1 892 107 107 VAL CG1 C 21.380 0.099 2 893 107 107 VAL CG2 C 25.542 0.078 2 894 107 107 VAL N N 117.605 0.028 1 895 108 108 THR H H 7.164 0.004 1 896 108 108 THR HA H 3.433 0.011 1 897 108 108 THR HB H 4.235 0.018 1 898 108 108 THR HG2 H 1.066 0.014 1 899 108 108 THR CA C 68.102 0.083 1 900 108 108 THR CB C 68.941 0.109 1 901 108 108 THR CG2 C 20.532 0.124 1 902 108 108 THR N N 114.891 0.059 1 903 109 109 LEU H H 8.028 0.005 1 904 109 109 LEU HA H 3.476 0.005 1 905 109 109 LEU HB2 H 1.664 0.005 2 906 109 109 LEU HB3 H 1.043 0.000 2 907 109 109 LEU HG H 1.844 0.007 1 908 109 109 LEU HD1 H 0.932 0.007 2 909 109 109 LEU HD2 H 0.678 0.008 2 910 109 109 LEU CA C 58.794 0.127 1 911 109 109 LEU CB C 41.315 0.056 1 912 109 109 LEU CG C 27.595 0.102 1 913 109 109 LEU CD1 C 25.989 0.071 2 914 109 109 LEU CD2 C 23.644 0.117 2 915 109 109 LEU N N 120.418 0.048 1 916 110 110 ALA H H 7.878 0.005 1 917 110 110 ALA HA H 2.748 0.017 1 918 110 110 ALA HB H 0.360 0.009 1 919 110 110 ALA CA C 55.455 0.117 1 920 110 110 ALA CB C 18.381 0.100 1 921 110 110 ALA N N 121.784 0.071 1 922 111 111 ALA H H 7.423 0.006 1 923 111 111 ALA HA H 3.959 0.017 1 924 111 111 ALA HB H 0.955 0.006 1 925 111 111 ALA CA C 53.483 0.070 1 926 111 111 ALA CB C 18.091 0.092 1 927 111 111 ALA N N 113.280 0.060 1 928 112 112 HIS H H 7.230 0.005 1 929 112 112 HIS HA H 4.310 0.005 1 930 112 112 HIS HB2 H 3.108 0.003 1 931 112 112 HIS HD2 H 7.153 0.000 1 932 112 112 HIS HE1 H 8.252 0.001 1 933 112 112 HIS CA C 57.409 0.056 1 934 112 112 HIS CB C 31.152 0.000 1 935 112 112 HIS CD2 C 121.245 0.000 1 936 112 112 HIS CE1 C 136.449 0.000 1 937 112 112 HIS N N 112.348 0.078 1 938 113 113 LEU H H 8.246 0.004 1 939 113 113 LEU HA H 4.965 0.024 1 940 113 113 LEU HB2 H 1.713 0.000 2 941 113 113 LEU HB3 H 1.674 0.000 2 942 113 113 LEU HG H 1.503 0.009 1 943 113 113 LEU HD1 H 0.770 0.012 2 944 113 113 LEU HD2 H 0.846 0.009 2 945 113 113 LEU CA C 52.595 0.061 1 946 113 113 LEU CB C 42.233 0.223 1 947 113 113 LEU CG C 26.620 0.018 1 948 113 113 LEU CD1 C 27.339 0.085 2 949 113 113 LEU CD2 C 24.590 0.071 2 950 113 113 LEU N N 121.163 0.073 1 951 114 114 PRO HG2 H 1.944 0.000 2 952 114 114 PRO HD2 H 3.604 0.011 2 953 114 114 PRO HD3 H 2.981 0.027 2 954 114 114 PRO CA C 65.922 0.000 1 955 114 114 PRO CG C 27.593 0.000 1 956 114 114 PRO CD C 50.501 0.138 1 957 115 115 ALA H H 8.308 0.005 1 958 115 115 ALA HA H 4.084 0.012 1 959 115 115 ALA HB H 1.325 0.009 1 960 115 115 ALA CA C 54.555 0.100 1 961 115 115 ALA CB C 18.511 0.090 1 962 115 115 ALA N N 118.796 0.034 1 963 116 116 GLU H H 7.739 0.010 1 964 116 116 GLU HA H 4.327 0.012 1 965 116 116 GLU HB2 H 2.090 0.016 1 966 116 116 GLU HG2 H 2.244 0.057 1 967 116 116 GLU HG3 H 2.193 0.002 1 968 116 116 GLU CA C 56.830 0.054 1 969 116 116 GLU CB C 29.402 0.155 1 970 116 116 GLU CG C 37.116 0.108 1 971 116 116 GLU N N 113.865 0.062 1 972 117 117 PHE H H 7.630 0.005 1 973 117 117 PHE HA H 4.276 0.013 1 974 117 117 PHE HB2 H 2.564 0.000 2 975 117 117 PHE HB3 H 3.109 0.000 2 976 117 117 PHE HD1 H 6.623 0.021 3 977 117 117 PHE HD2 H 7.724 0.000 3 978 117 117 PHE HE1 H 7.743 0.000 3 979 117 117 PHE CA C 57.775 0.094 1 980 117 117 PHE CB C 37.936 0.005 1 981 117 117 PHE CD1 C 131.844 0.019 3 982 117 117 PHE N N 122.853 0.067 1 983 118 118 THR H H 7.885 0.006 1 984 118 118 THR HA H 4.498 0.013 1 985 118 118 THR HB H 4.603 0.009 1 986 118 118 THR HG2 H 1.184 0.007 1 987 118 118 THR CA C 60.521 0.108 1 988 118 118 THR CB C 67.661 0.180 1 989 118 118 THR CG2 C 22.426 0.072 1 990 118 118 THR N N 114.809 0.035 1 991 119 119 PRO HA H 3.827 0.009 1 992 119 119 PRO CA C 66.734 0.149 1 993 120 120 ALA H H 8.360 0.011 1 994 120 120 ALA HA H 3.808 0.016 1 995 120 120 ALA HB H 1.248 0.006 1 996 120 120 ALA CA C 54.983 0.100 1 997 120 120 ALA CB C 18.927 0.104 1 998 120 120 ALA N N 116.163 0.053 1 999 121 121 VAL H H 7.280 0.011 1 1000 121 121 VAL HA H 3.311 0.005 1 1001 121 121 VAL HB H 2.048 0.034 1 1002 121 121 VAL HG1 H 0.923 0.009 2 1003 121 121 VAL HG2 H 0.854 0.007 2 1004 121 121 VAL CA C 67.472 0.079 1 1005 121 121 VAL CB C 32.079 0.083 1 1006 121 121 VAL CG1 C 24.214 0.111 2 1007 121 121 VAL CG2 C 21.618 0.129 2 1008 121 121 VAL N N 119.866 0.056 1 1009 122 122 HIS H H 8.428 0.004 1 1010 122 122 HIS HA H 3.667 0.023 1 1011 122 122 HIS HB2 H 2.403 0.000 2 1012 122 122 HIS HD2 H 6.935 0.000 1 1013 122 122 HIS HE1 H 7.278 0.006 1 1014 122 122 HIS CA C 57.845 0.026 1 1015 122 122 HIS CE1 C 137.908 0.000 1 1016 122 122 HIS N N 121.647 0.094 1 1017 123 123 ALA H H 7.971 0.005 1 1018 123 123 ALA HA H 3.834 0.013 1 1019 123 123 ALA HB H 1.331 0.013 1 1020 123 123 ALA CA C 55.996 0.087 1 1021 123 123 ALA CB C 18.302 0.057 1 1022 123 123 ALA N N 120.213 0.048 1 1023 124 124 SER H H 8.103 0.011 1 1024 124 124 SER HA H 4.195 0.000 1 1025 124 124 SER HB2 H 3.329 0.002 1 1026 124 124 SER CA C 63.236 0.021 1 1027 124 124 SER CB C 67.264 0.026 1 1028 124 124 SER N N 115.409 0.048 1 1029 125 125 LEU H H 9.150 0.007 1 1030 125 125 LEU HA H 4.186 0.005 1 1031 125 125 LEU HB3 H 1.898 0.375 2 1032 125 125 LEU HG H 1.817 0.008 1 1033 125 125 LEU HD1 H 0.967 0.009 2 1034 125 125 LEU HD2 H 0.889 0.007 2 1035 125 125 LEU CA C 58.366 0.036 1 1036 125 125 LEU CB C 43.134 0.063 1 1037 125 125 LEU CG C 27.382 0.075 1 1038 125 125 LEU CD1 C 23.113 0.159 2 1039 125 125 LEU CD2 C 27.008 0.088 2 1040 125 125 LEU N N 121.332 0.062 1 1041 126 126 ASP H H 8.648 0.012 1 1042 126 126 ASP HA H 4.510 0.006 1 1043 126 126 ASP HB2 H 2.663 0.012 2 1044 126 126 ASP HB3 H 2.841 0.000 2 1045 126 126 ASP CA C 59.102 0.117 1 1046 126 126 ASP CB C 43.415 0.000 1 1047 126 126 ASP N N 120.637 0.042 1 1048 127 127 LYS H H 7.955 0.009 1 1049 127 127 LYS HA H 4.140 0.019 1 1050 127 127 LYS HB2 H 1.914 0.021 2 1051 127 127 LYS HG2 H 1.971 0.016 2 1052 127 127 LYS HG3 H 1.536 0.001 2 1053 127 127 LYS HD2 H 0.871 0.006 2 1054 127 127 LYS HE2 H 3.015 0.009 2 1055 127 127 LYS CA C 59.974 0.080 1 1056 127 127 LYS CB C 32.748 0.035 1 1057 127 127 LYS CG C 25.449 0.128 1 1058 127 127 LYS CD C 24.296 0.038 1 1059 127 127 LYS CE C 42.570 0.037 1 1060 127 127 LYS N N 118.245 0.051 1 1061 128 128 PHE H H 8.892 0.007 1 1062 128 128 PHE HA H 4.235 0.021 1 1063 128 128 PHE HB2 H 3.332 0.000 2 1064 128 128 PHE HD1 H 6.971 0.007 3 1065 128 128 PHE HE1 H 6.339 0.000 3 1066 128 128 PHE CA C 61.584 0.110 1 1067 128 128 PHE CB C 40.415 0.000 1 1068 128 128 PHE CD1 C 131.326 0.054 1 1069 128 128 PHE N N 122.132 0.030 1 1070 129 129 LEU H H 8.983 0.007 1 1071 129 129 LEU HA H 3.762 0.014 1 1072 129 129 LEU HG H 2.162 0.006 1 1073 129 129 LEU HD1 H 0.933 0.017 2 1074 129 129 LEU HD2 H 1.154 0.015 2 1075 129 129 LEU CA C 58.328 0.116 1 1076 129 129 LEU CG C 28.249 0.125 1 1077 129 129 LEU CD1 C 22.994 0.103 2 1078 129 129 LEU CD2 C 26.852 0.124 2 1079 129 129 LEU N N 120.943 0.079 1 1080 130 130 ALA H H 8.558 0.017 1 1081 130 130 ALA HA H 4.279 0.029 1 1082 130 130 ALA HB H 1.618 0.009 1 1083 130 130 ALA CA C 55.652 0.086 1 1084 130 130 ALA CB C 17.946 0.087 1 1085 130 130 ALA N N 125.565 0.053 1 1086 131 131 SER H H 8.194 0.002 1 1087 131 131 SER HA H 4.124 0.017 1 1088 131 131 SER HB2 H 4.085 0.010 1 1089 131 131 SER HB3 H 3.868 0.023 1 1090 131 131 SER CA C 62.989 0.102 1 1091 131 131 SER CB C 62.899 0.232 1 1092 131 131 SER N N 118.251 0.072 1 1093 132 132 VAL H H 8.224 0.005 1 1094 132 132 VAL HA H 3.230 0.005 1 1095 132 132 VAL HB H 1.944 0.006 1 1096 132 132 VAL HG1 H 0.351 0.005 2 1097 132 132 VAL HG2 H 0.847 0.007 2 1098 132 132 VAL CA C 66.975 0.105 1 1099 132 132 VAL CB C 32.309 0.073 1 1100 132 132 VAL CG1 C 23.265 0.089 2 1101 132 132 VAL CG2 C 22.183 0.079 2 1102 132 132 VAL N N 122.863 0.093 1 1103 133 133 SER H H 8.200 0.009 1 1104 133 133 SER HA H 3.602 0.008 1 1105 133 133 SER CA C 63.368 0.063 1 1106 133 133 SER N N 115.171 0.115 1 1107 134 134 THR H H 8.108 0.013 1 1108 134 134 THR HA H 3.484 0.021 1 1109 134 134 THR HB H 4.173 0.006 1 1110 134 134 THR HG2 H 1.046 0.009 1 1111 134 134 THR CA C 66.851 0.031 1 1112 134 134 THR CB C 68.701 0.036 1 1113 134 134 THR CG2 C 21.747 0.052 1 1114 134 134 THR N N 119.594 0.070 1 1115 135 135 VAL H H 7.432 0.012 1 1116 135 135 VAL HA H 3.379 0.012 1 1117 135 135 VAL HB H 2.014 0.006 1 1118 135 135 VAL HG1 H 0.753 0.000 2 1119 135 135 VAL HG2 H 0.786 0.006 2 1120 135 135 VAL CA C 67.138 0.079 1 1121 135 135 VAL CB C 31.099 0.050 1 1122 135 135 VAL CG1 C 24.208 0.000 2 1123 135 135 VAL CG2 C 23.453 0.129 2 1124 135 135 VAL N N 122.485 0.050 1 1125 136 136 LEU H H 7.681 0.001 1 1126 136 136 LEU HD1 H 0.011 0.006 2 1127 136 136 LEU HD2 H -0.542 0.010 2 1128 136 136 LEU CD1 C 25.329 0.029 2 1129 136 136 LEU CD2 C 23.749 0.117 2 1130 136 136 LEU N N 109.527 0.077 1 1131 137 137 THR H H 6.703 0.020 1 1132 137 137 THR HA H 3.951 0.020 1 1133 137 137 THR HB H 4.228 0.000 1 1134 137 137 THR HG2 H 0.357 0.010 1 1135 137 137 THR CA C 60.520 0.147 1 1136 137 137 THR CB C 69.917 0.000 1 1137 137 137 THR CG2 C 22.835 0.057 1 1138 137 137 THR N N 101.553 0.222 1 1139 138 138 SER H H 7.182 0.011 1 1140 138 138 SER HA H 4.500 0.018 1 1141 138 138 SER HB2 H 3.905 0.000 2 1142 138 138 SER CA C 59.305 0.024 1 1143 138 138 SER CB C 65.125 0.000 1 1144 138 138 SER N N 117.966 0.041 1 1145 141 141 ARG H H 7.341 0.033 1 1146 141 141 ARG HA H 4.140 0.011 1 1147 141 141 ARG HB2 H 1.728 0.048 2 1148 141 141 ARG HB3 H 1.595 0.009 2 1149 141 141 ARG HG2 H 1.424 0.006 2 1150 141 141 ARG HD2 H 3.046 0.016 2 1151 141 141 ARG CA C 57.644 0.062 1 1152 141 141 ARG CB C 32.002 0.077 1 1153 141 141 ARG CG C 27.298 0.064 1 1154 141 141 ARG CD C 43.784 0.055 1 1155 141 141 ARG N N 125.253 0.122 1 stop_ save_ save_chem_shift_list_1_3 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $conditions_1 _Chem_shift_reference_set_label $chemical_shift_referencing _Mol_system_component_name 'globin subunit beta, 1' _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 1 VAL HG1 H 0.986 0.000 2 2 1 1 VAL HG2 H 0.863 0.000 2 3 1 1 VAL CG1 C 21.730 0.000 2 4 1 1 VAL CG2 C 21.506 0.000 2 5 2 2 HIS HA H 4.723 0.000 1 6 2 2 HIS HB2 H 3.005 0.000 2 7 2 2 HIS HB3 H 2.979 0.000 2 8 2 2 HIS HE1 H 8.034 0.000 1 9 2 2 HIS CA C 55.795 0.000 1 10 2 2 HIS CB C 31.044 0.000 1 11 2 2 HIS CE1 C 137.545 0.000 1 12 3 3 LEU H H 8.138 0.011 1 13 3 3 LEU HA H 4.736 0.013 1 14 3 3 LEU HB2 H 1.454 0.013 2 15 3 3 LEU HG H 1.509 0.000 1 16 3 3 LEU HD1 H 0.585 0.005 2 17 3 3 LEU HD2 H 0.718 0.018 2 18 3 3 LEU CA C 53.504 0.000 1 19 3 3 LEU CB C 44.072 0.023 1 20 3 3 LEU CG C 27.728 0.000 1 21 3 3 LEU CD1 C 26.049 0.102 2 22 3 3 LEU CD2 C 24.153 0.099 2 23 3 3 LEU N N 126.048 0.066 1 24 4 4 THR H H 9.219 0.012 1 25 4 4 THR HA H 4.480 0.000 1 26 4 4 THR HB H 4.736 0.000 1 27 4 4 THR HG2 H 1.328 0.012 1 28 4 4 THR CA C 60.800 0.000 1 29 4 4 THR CB C 67.838 0.000 1 30 4 4 THR CG2 C 22.007 0.022 1 31 4 4 THR N N 115.319 0.038 1 32 5 5 PRO HA H 4.147 0.018 1 33 5 5 PRO HB2 H 2.413 0.000 2 34 5 5 PRO HB3 H 1.858 0.000 2 35 5 5 PRO HD2 H 3.910 0.000 2 36 5 5 PRO CA C 66.420 0.086 1 37 5 5 PRO CB C 31.667 0.026 1 38 5 5 PRO CD C 50.109 0.000 1 39 6 6 GLU H H 8.719 0.010 1 40 6 6 GLU HA H 4.009 0.012 1 41 6 6 GLU HB2 H 1.935 0.003 2 42 6 6 GLU HB3 H 1.858 0.000 2 43 6 6 GLU HG2 H 2.366 0.000 2 44 6 6 GLU HG3 H 2.234 0.021 2 45 6 6 GLU CA C 60.212 0.076 1 46 6 6 GLU CB C 28.934 0.025 1 47 6 6 GLU CG C 36.919 0.093 1 48 6 6 GLU N N 117.569 0.057 1 49 7 7 GLU H H 7.769 0.011 1 50 7 7 GLU HA H 3.855 0.021 1 51 7 7 GLU HB2 H 2.437 0.009 2 52 7 7 GLU HB3 H 1.652 0.000 2 53 7 7 GLU HG2 H 2.033 0.000 2 54 7 7 GLU CA C 59.209 0.074 1 55 7 7 GLU CB C 31.662 0.097 1 56 7 7 GLU CG C 37.584 0.000 1 57 7 7 GLU N N 121.612 0.095 1 58 8 8 LYS H H 8.798 0.007 1 59 8 8 LYS HA H 3.587 0.017 1 60 8 8 LYS HB2 H 1.821 0.004 2 61 8 8 LYS HG2 H 1.276 0.002 2 62 8 8 LYS HD2 H 1.566 0.020 2 63 8 8 LYS HE2 H 2.867 0.000 2 64 8 8 LYS CA C 60.299 0.083 1 65 8 8 LYS CB C 32.169 0.033 1 66 8 8 LYS CG C 25.876 0.009 1 67 8 8 LYS CD C 29.504 0.005 1 68 8 8 LYS CE C 42.092 0.000 1 69 8 8 LYS N N 119.141 0.039 1 70 9 9 SER H H 8.186 0.006 1 71 9 9 SER HA H 4.105 0.006 1 72 9 9 SER HB2 H 3.907 0.006 2 73 9 9 SER CA C 61.599 0.142 1 74 9 9 SER CB C 62.734 0.086 1 75 9 9 SER N N 115.088 0.058 1 76 10 10 ALA H H 7.651 0.006 1 77 10 10 ALA HA H 4.168 0.005 1 78 10 10 ALA HB H 1.450 0.004 1 79 10 10 ALA CA C 55.166 0.026 1 80 10 10 ALA CB C 18.547 0.011 1 81 10 10 ALA N N 123.919 0.090 1 82 11 11 VAL H H 8.404 0.008 1 83 11 11 VAL HA H 3.811 0.069 1 84 11 11 VAL HB H 1.917 0.012 1 85 11 11 VAL HG1 H 0.492 0.014 2 86 11 11 VAL HG2 H 0.425 0.024 2 87 11 11 VAL CA C 66.119 0.079 1 88 11 11 VAL CB C 31.829 0.029 1 89 11 11 VAL CG1 C 22.887 0.045 2 90 11 11 VAL CG2 C 21.140 0.023 2 91 11 11 VAL N N 115.746 0.069 1 92 12 12 THR H H 8.403 0.008 1 93 12 12 THR HA H 3.923 0.006 1 94 12 12 THR HB H 4.272 0.000 1 95 12 12 THR HG2 H 1.251 0.018 1 96 12 12 THR CA C 66.429 0.119 1 97 12 12 THR CB C 68.906 0.012 1 98 12 12 THR CG2 C 21.751 0.045 1 99 12 12 THR N N 115.532 0.049 1 100 13 13 ALA H H 8.264 0.014 1 101 13 13 ALA HA H 4.162 0.015 1 102 13 13 ALA HB H 1.474 0.016 1 103 13 13 ALA CA C 55.321 0.000 1 104 13 13 ALA CB C 18.234 0.059 1 105 13 13 ALA N N 125.746 0.084 1 106 14 14 LEU H H 7.232 0.012 1 107 14 14 LEU HA H 3.839 0.019 1 108 14 14 LEU HB2 H 1.669 0.025 2 109 14 14 LEU HG H 1.100 0.000 1 110 14 14 LEU HD1 H 0.473 0.010 2 111 14 14 LEU HD2 H 0.415 0.016 2 112 14 14 LEU CA C 57.955 0.064 1 113 14 14 LEU CB C 41.704 0.053 1 114 14 14 LEU CG C 27.246 0.000 1 115 14 14 LEU CD1 C 25.148 0.052 2 116 14 14 LEU CD2 C 25.022 0.070 2 117 14 14 LEU N N 117.083 0.049 1 118 15 15 TRP H H 8.159 0.008 1 119 15 15 TRP HA H 4.259 0.015 1 120 15 15 TRP HB2 H 3.631 0.009 2 121 15 15 TRP HB3 H 3.147 0.004 2 122 15 15 TRP HD1 H 7.108 0.001 1 123 15 15 TRP HE1 H 10.118 0.006 1 124 15 15 TRP HZ2 H 7.539 0.007 1 125 15 15 TRP HZ3 H 8.042 0.002 1 126 15 15 TRP HH2 H 6.815 0.010 1 127 15 15 TRP CA C 60.098 0.036 1 128 15 15 TRP CB C 29.496 0.096 1 129 15 15 TRP CD1 C 126.845 0.012 1 130 15 15 TRP CZ2 C 113.650 0.059 1 131 15 15 TRP CZ3 C 121.740 0.053 1 132 15 15 TRP CH2 C 123.382 0.059 1 133 15 15 TRP N N 119.157 0.058 1 134 15 15 TRP NE1 N 127.683 0.062 1 135 16 16 GLY H H 7.813 0.018 1 136 16 16 GLY HA2 H 3.990 0.013 2 137 16 16 GLY CA C 46.466 0.091 1 138 16 16 GLY N N 101.518 0.032 1 139 17 17 LYS H H 7.726 0.012 1 140 17 17 LYS HA H 4.415 0.009 1 141 17 17 LYS HB2 H 2.113 0.000 2 142 17 17 LYS HB3 H 2.006 0.000 2 143 17 17 LYS HG2 H 1.538 0.003 2 144 17 17 LYS HD2 H 1.672 0.024 2 145 17 17 LYS HE2 H 2.911 0.000 2 146 17 17 LYS CA C 56.011 0.042 1 147 17 17 LYS CB C 33.718 0.093 1 148 17 17 LYS CG C 25.338 0.073 1 149 17 17 LYS CD C 29.951 0.023 1 150 17 17 LYS CE C 42.142 0.000 1 151 17 17 LYS N N 118.173 0.074 1 152 18 18 VAL H H 7.247 0.010 1 153 18 18 VAL HA H 3.425 0.002 1 154 18 18 VAL HB H 1.536 0.001 1 155 18 18 VAL HG1 H 0.542 0.028 2 156 18 18 VAL HG2 H 0.030 0.010 2 157 18 18 VAL CA C 63.458 0.004 1 158 18 18 VAL CB C 32.250 0.047 1 159 18 18 VAL CG1 C 23.237 0.093 2 160 18 18 VAL CG2 C 20.558 0.058 2 161 18 18 VAL N N 121.555 0.037 1 162 19 19 ASN H H 8.345 0.009 1 163 19 19 ASN HA H 4.691 0.004 1 164 19 19 ASN HB2 H 2.710 0.004 2 165 19 19 ASN HB3 H 2.864 0.006 2 166 19 19 ASN HD21 H 7.482 0.000 2 167 19 19 ASN HD22 H 6.989 0.004 2 168 19 19 ASN CA C 52.229 0.071 1 169 19 19 ASN CB C 37.071 0.011 1 170 19 19 ASN N N 124.948 0.051 1 171 19 19 ASN ND2 N 112.191 0.028 1 172 20 20 VAL H H 8.191 0.007 1 173 20 20 VAL HA H 3.476 0.012 1 174 20 20 VAL HB H 2.154 0.004 1 175 20 20 VAL HG1 H 0.875 0.004 2 176 20 20 VAL HG2 H 0.887 0.000 2 177 20 20 VAL CA C 64.261 0.042 1 178 20 20 VAL CB C 31.248 0.011 1 179 20 20 VAL CG1 C 21.449 0.031 2 180 20 20 VAL CG2 C 19.331 0.009 2 181 20 20 VAL N N 124.178 0.047 1 182 21 21 ASP H H 7.949 0.004 1 183 21 21 ASP HA H 4.414 0.006 1 184 21 21 ASP HB2 H 2.628 0.004 2 185 21 21 ASP CA C 56.559 0.000 1 186 21 21 ASP CB C 41.333 0.009 1 187 21 21 ASP N N 119.232 0.047 1 188 22 22 GLU H H 7.224 0.006 1 189 22 22 GLU HA H 4.352 0.017 1 190 22 22 GLU HB2 H 1.499 0.016 2 191 22 22 GLU HB3 H 2.004 0.029 2 192 22 22 GLU HG2 H 2.085 0.033 2 193 22 22 GLU HG3 H 1.973 0.000 2 194 22 22 GLU CA C 57.206 0.011 1 195 22 22 GLU CB C 32.785 0.117 1 196 22 22 GLU CG C 35.571 0.000 1 197 22 22 GLU N N 117.441 0.038 1 198 23 23 VAL H H 7.802 0.014 1 199 23 23 VAL HA H 3.270 0.008 1 200 23 23 VAL HB H 1.335 0.021 1 201 23 23 VAL HG1 H 0.432 0.014 2 202 23 23 VAL HG2 H 0.409 0.029 2 203 23 23 VAL CA C 66.972 0.040 1 204 23 23 VAL CB C 31.180 0.069 1 205 23 23 VAL CG1 C 24.144 0.045 2 206 23 23 VAL CG2 C 20.588 0.053 2 207 23 23 VAL N N 118.284 0.055 1 208 24 24 GLY H H 8.590 0.006 1 209 24 24 GLY HA2 H 3.538 0.000 2 210 24 24 GLY HA3 H 3.127 0.000 2 211 24 24 GLY CA C 47.570 0.025 1 212 24 24 GLY N N 108.589 0.110 1 213 25 25 GLY H H 7.515 0.007 1 214 25 25 GLY HA2 H 3.760 0.020 2 215 25 25 GLY HA3 H 3.335 0.000 2 216 25 25 GLY CA C 47.589 0.034 1 217 25 25 GLY N N 108.766 0.036 1 218 26 26 GLU H H 7.610 0.012 1 219 26 26 GLU HA H 3.772 0.034 1 220 26 26 GLU HB2 H 2.030 0.000 2 221 26 26 GLU HB3 H 1.958 0.000 2 222 26 26 GLU HG3 H 2.139 0.009 2 223 26 26 GLU CA C 59.109 0.044 1 224 26 26 GLU CB C 29.672 0.048 1 225 26 26 GLU CG C 36.928 0.084 1 226 26 26 GLU N N 121.951 0.059 1 227 27 27 ALA H H 8.053 0.007 1 228 27 27 ALA HA H 3.739 0.000 1 229 27 27 ALA HB H 1.071 0.013 1 230 27 27 ALA CA C 54.743 0.000 1 231 27 27 ALA CB C 16.998 0.042 1 232 27 27 ALA N N 119.996 0.057 1 233 28 28 LEU H H 7.861 0.014 1 234 28 28 LEU HA H 3.340 0.008 1 235 28 28 LEU HB2 H 1.139 0.009 2 236 28 28 LEU HB3 H 0.342 0.000 2 237 28 28 LEU HD1 H -0.722 0.015 1 238 28 28 LEU HD2 H -0.213 0.003 1 239 28 28 LEU CA C 56.886 0.081 1 240 28 28 LEU CB C 41.608 0.019 1 241 28 28 LEU CD1 C 21.343 0.093 2 242 28 28 LEU CD2 C 26.075 0.012 2 243 28 28 LEU N N 116.456 0.048 1 244 29 29 GLY H H 8.064 0.011 1 245 29 29 GLY HA2 H 3.527 0.000 2 246 29 29 GLY HA3 H 3.125 0.000 2 247 29 29 GLY CA C 47.587 0.090 1 248 29 29 GLY N N 104.306 0.086 1 249 30 30 ARG H H 7.921 0.011 1 250 30 30 ARG HA H 3.530 0.011 1 251 30 30 ARG HB2 H 1.772 0.000 2 252 30 30 ARG CA C 60.645 0.019 1 253 30 30 ARG CB C 31.862 0.000 1 254 30 30 ARG N N 116.977 0.094 1 255 31 31 LEU H H 7.757 0.008 1 256 31 31 LEU HA H 3.805 0.000 1 257 31 31 LEU HB3 H 1.560 0.000 2 258 31 31 LEU HD1 H 0.745 0.000 2 259 31 31 LEU HD2 H 1.059 0.017 2 260 31 31 LEU CA C 59.438 0.000 1 261 31 31 LEU CB C 41.647 0.000 1 262 31 31 LEU CD1 C 26.557 0.000 2 263 31 31 LEU CD2 C 24.822 0.032 2 264 31 31 LEU N N 121.166 0.076 1 265 32 32 LEU H H 7.051 0.004 1 266 32 32 LEU HG H 1.464 0.000 1 267 32 32 LEU HD1 H 0.214 0.020 2 268 32 32 LEU HD2 H 0.427 0.015 2 269 32 32 LEU CG C 27.663 0.000 1 270 32 32 LEU CD1 C 25.221 0.074 2 271 32 32 LEU CD2 C 23.711 0.000 2 272 32 32 LEU N N 115.477 0.037 1 273 33 33 VAL H H 7.494 0.012 1 274 33 33 VAL HA H 3.431 0.006 1 275 33 33 VAL HB H 1.598 0.020 1 276 33 33 VAL HG1 H 0.501 0.008 2 277 33 33 VAL HG2 H 0.746 0.003 2 278 33 33 VAL CA C 64.811 0.010 1 279 33 33 VAL CB C 33.093 0.032 1 280 33 33 VAL CG1 C 21.233 0.017 2 281 33 33 VAL CG2 C 22.933 0.057 2 282 33 33 VAL N N 116.348 0.072 1 283 34 34 VAL H H 8.582 0.009 1 284 34 34 VAL HA H 2.989 0.008 1 285 34 34 VAL HB H 1.070 0.003 1 286 34 34 VAL HG2 H -0.251 0.012 2 287 34 34 VAL CA C 65.254 0.066 1 288 34 34 VAL CB C 32.081 0.039 1 289 34 34 VAL CG2 C 20.939 0.076 1 290 34 34 VAL N N 119.158 0.085 1 291 35 35 TYR H H 7.475 0.006 1 292 35 35 TYR HA H 4.330 0.000 1 293 35 35 TYR HB2 H 2.560 0.000 2 294 35 35 TYR HB3 H 1.477 0.000 2 295 35 35 TYR CA C 53.307 0.000 1 296 35 35 TYR CB C 35.571 0.000 1 297 35 35 TYR N N 117.735 0.034 1 298 36 36 PRO HA H 4.493 0.000 1 299 36 36 PRO HD2 H 3.508 0.000 2 300 36 36 PRO CA C 65.780 0.000 1 301 36 36 PRO CD C 50.862 0.000 1 302 37 37 TRP H H 7.112 0.007 1 303 37 37 TRP HA H 4.619 0.000 1 304 37 37 TRP HB2 H 1.944 0.000 2 305 37 37 TRP HD1 H 7.401 0.015 1 306 37 37 TRP HE1 H 10.652 0.008 1 307 37 37 TRP HZ2 H 7.529 0.007 1 308 37 37 TRP CA C 61.139 0.000 1 309 37 37 TRP CB C 27.174 0.000 1 310 37 37 TRP CD1 C 127.137 0.044 1 311 37 37 TRP CZ2 C 116.372 0.047 1 312 37 37 TRP N N 117.401 0.090 1 313 37 37 TRP NE1 N 133.634 0.067 1 314 38 38 THR H H 8.213 0.012 1 315 38 38 THR HA H 4.447 0.013 1 316 38 38 THR HG2 H 1.205 0.009 1 317 38 38 THR CA C 65.743 0.086 1 318 38 38 THR CG2 C 21.953 0.031 1 319 38 38 THR N N 117.248 0.027 1 320 39 39 GLN H H 7.751 0.012 1 321 39 39 GLN N N 118.091 0.018 1 322 40 40 ARG H H 7.779 0.009 1 323 40 40 ARG HA H 4.065 0.030 1 324 40 40 ARG HB2 H 2.208 0.000 2 325 40 40 ARG HG2 H 1.498 0.000 2 326 40 40 ARG HD3 H 2.920 0.000 2 327 40 40 ARG CA C 59.321 0.190 1 328 40 40 ARG CB C 31.338 0.000 1 329 40 40 ARG CG C 27.705 0.000 1 330 40 40 ARG CD C 42.113 0.000 1 331 40 40 ARG N N 118.215 0.064 1 332 41 41 PHE H H 7.498 0.010 1 333 41 41 PHE HA H 4.441 0.007 1 334 41 41 PHE HD1 H 7.979 0.019 3 335 41 41 PHE CA C 60.406 0.003 1 336 41 41 PHE CD1 C 132.161 0.054 1 337 41 41 PHE N N 112.422 0.051 1 338 42 42 PHE H H 7.594 0.009 1 339 42 42 PHE HA H 4.404 0.004 1 340 42 42 PHE HB2 H 2.543 0.009 2 341 42 42 PHE HB3 H 2.022 0.000 2 342 42 42 PHE HD1 H 6.287 0.025 3 343 42 42 PHE HE1 H 6.342 0.002 3 344 42 42 PHE CA C 57.199 0.026 1 345 42 42 PHE CB C 39.867 0.009 1 346 42 42 PHE CD1 C 132.816 0.024 3 347 42 42 PHE CE1 C 128.828 0.071 3 348 42 42 PHE N N 116.396 0.075 1 349 43 43 GLU H H 7.388 0.010 1 350 43 43 GLU HA H 4.173 0.022 1 351 43 43 GLU HB2 H 2.150 0.008 2 352 43 43 GLU HG2 H 2.441 0.020 2 353 43 43 GLU HG3 H 2.372 0.000 2 354 43 43 GLU CA C 59.683 0.049 1 355 43 43 GLU CB C 30.000 0.049 1 356 43 43 GLU CG C 36.325 0.046 1 357 43 43 GLU N N 121.043 0.059 1 358 44 44 SER H H 8.727 0.014 1 359 44 44 SER HA H 4.425 0.020 1 360 44 44 SER HB3 H 4.106 0.008 2 361 44 44 SER CA C 60.139 0.071 1 362 44 44 SER CB C 63.275 0.005 1 363 44 44 SER N N 113.220 0.065 1 364 45 45 PHE H H 8.578 0.009 1 365 45 45 PHE HA H 4.522 0.022 1 366 45 45 PHE HB2 H 3.576 0.016 1 367 45 45 PHE HB3 H 3.103 0.016 1 368 45 45 PHE HD1 H 6.869 0.001 3 369 45 45 PHE HE1 H 6.787 0.004 3 370 45 45 PHE CA C 56.893 0.013 1 371 45 45 PHE CB C 36.631 0.188 1 372 45 45 PHE CD1 C 129.673 0.044 3 373 45 45 PHE CE1 C 131.536 0.045 3 374 45 45 PHE N N 122.163 0.086 1 375 46 46 GLY CA C 44.881 0.063 1 376 46 46 GLY HA2 H 3.636 0.018 2 377 46 46 GLY HA3 H 4.289 0.001 2 378 46 46 GLY H H 7.763 0.007 1 379 46 46 GLY N N 108.128 0.024 1 380 47 47 ASP H H 8.439 0.004 1 381 47 47 ASP HA H 4.298 0.010 1 382 47 47 ASP HB2 H 2.874 0.000 2 383 47 47 ASP HB3 H 2.549 0.000 2 384 47 47 ASP CA C 55.689 0.088 1 385 47 47 ASP CB C 40.516 0.112 1 386 47 47 ASP N N 122.418 0.068 1 387 48 48 LEU H H 8.401 0.007 1 388 48 48 LEU HA H 4.484 0.010 1 389 48 48 LEU HG H 1.657 0.000 1 390 48 48 LEU HD1 H 0.783 0.008 2 391 48 48 LEU HD2 H 0.671 0.014 2 392 48 48 LEU CA C 52.762 0.029 1 393 48 48 LEU CG C 25.910 0.000 1 394 48 48 LEU CD1 C 26.815 0.039 2 395 48 48 LEU CD2 C 23.539 0.064 2 396 48 48 LEU N N 128.504 0.086 1 397 49 49 SER H H 8.190 0.006 1 398 49 49 SER HA H 3.989 0.004 1 399 49 49 SER HB2 H 3.921 0.011 2 400 49 49 SER CA C 62.221 0.004 1 401 49 49 SER CB C 64.198 0.017 1 402 49 49 SER N N 112.811 0.051 1 403 50 50 THR H H 7.130 0.006 1 404 50 50 THR HA H 4.865 0.000 1 405 50 50 THR HB H 4.444 0.008 1 406 50 50 THR HG2 H 1.183 0.027 1 407 50 50 THR CA C 58.324 0.000 1 408 50 50 THR CB C 70.543 0.033 1 409 50 50 THR CG2 C 21.922 0.097 1 410 50 50 THR N N 111.489 0.053 1 411 51 51 PRO HA H 3.887 0.016 1 412 51 51 PRO HB2 H 1.891 0.045 2 413 51 51 PRO HB3 H 2.040 0.000 2 414 51 51 PRO HG2 H 2.033 0.000 2 415 51 51 PRO HG3 H 1.384 0.000 2 416 51 51 PRO HD2 H 3.829 0.010 2 417 51 51 PRO CA C 65.815 0.027 1 418 51 51 PRO CB C 31.619 0.000 1 419 51 51 PRO CG C 28.077 0.039 1 420 51 51 PRO CD C 50.299 0.000 1 421 52 52 ASP H H 7.958 0.006 1 422 52 52 ASP HA H 4.127 0.016 1 423 52 52 ASP HB3 H 2.422 0.003 2 424 52 52 ASP CA C 57.126 0.029 1 425 52 52 ASP CB C 40.319 0.001 1 426 52 52 ASP N N 114.667 0.053 1 427 53 53 ALA H H 7.815 0.006 1 428 53 53 ALA HA H 3.969 0.013 1 429 53 53 ALA HB H 1.286 0.018 1 430 53 53 ALA CA C 54.762 0.001 1 431 53 53 ALA CB C 18.452 0.070 1 432 53 53 ALA N N 123.758 0.076 1 433 54 54 VAL H H 7.835 0.015 1 434 54 54 VAL HA H 3.303 0.012 1 435 54 54 VAL HB H 1.836 0.004 1 436 54 54 VAL HG1 H 0.796 0.019 2 437 54 54 VAL HG2 H 0.745 0.013 2 438 54 54 VAL CA C 67.028 0.026 1 439 54 54 VAL CB C 32.023 0.034 1 440 54 54 VAL CG1 C 24.011 0.121 2 441 54 54 VAL CG2 C 22.961 0.092 2 442 54 54 VAL N N 116.672 0.060 1 443 55 55 MET H H 7.923 0.012 1 444 55 55 MET HA H 4.092 0.008 1 445 55 55 MET HB2 H 1.923 0.000 2 446 55 55 MET HG2 H 2.643 0.000 2 447 55 55 MET HE H 1.942 0.013 1 448 55 55 MET CA C 55.321 0.000 1 449 55 55 MET CB C 29.003 0.000 1 450 55 55 MET CG C 30.815 0.000 1 451 55 55 MET CE C 15.763 0.055 1 452 55 55 MET N N 111.923 0.042 1 453 56 56 GLY H H 7.405 0.004 1 454 56 56 GLY HA2 H 3.527 0.003 2 455 56 56 GLY HA3 H 4.191 0.018 2 456 56 56 GLY CA C 44.314 0.077 1 457 56 56 GLY N N 103.328 0.035 1 458 57 57 ASN H H 7.179 0.006 1 459 57 57 ASN HA H 4.765 0.000 1 460 57 57 ASN HB2 H 3.338 0.000 2 461 57 57 ASN HB3 H 2.826 0.000 2 462 57 57 ASN CA C 51.887 0.000 1 463 57 57 ASN CB C 38.951 0.037 1 464 57 57 ASN N N 123.465 0.040 1 465 58 58 PRO HA H 4.167 0.015 1 466 58 58 PRO HB2 H 2.382 0.000 2 467 58 58 PRO HB3 H 1.869 0.000 2 468 58 58 PRO HG2 H 2.044 0.000 2 469 58 58 PRO HD2 H 3.785 0.000 2 470 58 58 PRO CA C 65.046 0.060 1 471 58 58 PRO CB C 32.184 0.123 1 472 58 58 PRO CG C 27.501 0.000 1 473 58 58 PRO CD C 51.348 0.000 1 474 59 59 LYS H H 8.120 0.008 1 475 59 59 LYS HA H 3.836 0.006 1 476 59 59 LYS HB2 H 0.648 0.011 2 477 59 59 LYS HB3 H 1.496 0.000 2 478 59 59 LYS HG2 H 1.376 0.005 2 479 59 59 LYS HG3 H 1.089 0.000 2 480 59 59 LYS HD2 H 1.468 0.006 2 481 59 59 LYS HD3 H 1.485 0.000 2 482 59 59 LYS HE2 H 2.807 0.000 2 483 59 59 LYS CA C 59.226 0.089 1 484 59 59 LYS CB C 30.999 0.071 1 485 59 59 LYS CG C 26.393 0.090 1 486 59 59 LYS CD C 29.510 0.073 1 487 59 59 LYS CE C 42.257 0.000 1 488 59 59 LYS N N 119.345 0.064 1 489 60 60 VAL H H 7.482 0.008 1 490 60 60 VAL HA H 3.075 0.024 1 491 60 60 VAL HB H 2.277 0.003 1 492 60 60 VAL HG1 H 0.677 0.011 2 493 60 60 VAL HG2 H 0.414 0.013 2 494 60 60 VAL CA C 66.514 0.019 1 495 60 60 VAL CB C 31.561 0.031 1 496 60 60 VAL CG1 C 23.475 0.031 2 497 60 60 VAL CG2 C 20.603 0.070 2 498 60 60 VAL N N 122.434 0.082 1 499 61 61 LYS H H 7.346 0.013 1 500 61 61 LYS HA H 3.557 0.015 1 501 61 61 LYS HB2 H 1.734 0.003 2 502 61 61 LYS HG2 H 1.389 0.012 2 503 61 61 LYS HD2 H 1.550 0.000 2 504 61 61 LYS HE2 H 2.871 0.010 2 505 61 61 LYS CA C 60.458 0.104 1 506 61 61 LYS CB C 32.257 0.030 1 507 61 61 LYS CG C 25.275 0.070 1 508 61 61 LYS CD C 29.398 0.002 1 509 61 61 LYS CE C 41.971 0.013 1 510 61 61 LYS N N 118.639 0.037 1 511 62 62 ALA H H 7.854 0.011 1 512 62 62 ALA HA H 3.992 0.011 1 513 62 62 ALA HB H 1.385 0.002 1 514 62 62 ALA CA C 54.988 0.081 1 515 62 62 ALA CB C 18.407 0.003 1 516 62 62 ALA N N 120.836 0.064 1 517 63 63 HIS H H 8.339 0.002 1 518 63 63 HIS HA H 3.869 0.020 1 519 63 63 HIS HB2 H 2.901 0.000 2 520 63 63 HIS HB3 H 2.219 0.014 2 521 63 63 HIS HD2 H 4.568 0.000 1 522 63 63 HIS HE1 H 8.379 0.005 1 523 63 63 HIS CA C 59.950 0.091 1 524 63 63 HIS CB C 31.359 0.088 1 525 63 63 HIS CD2 C 114.964 0.000 1 526 63 63 HIS CE1 C 138.660 0.008 1 527 63 63 HIS N N 120.455 0.038 1 528 64 64 GLY H H 8.214 0.012 1 529 64 64 GLY HA2 H 2.998 0.001 2 530 64 64 GLY HA3 H 2.562 0.000 2 531 64 64 GLY CA C 46.131 0.154 1 532 64 64 GLY N N 105.417 0.086 1 533 65 65 LYS H H 7.098 0.012 1 534 65 65 LYS HA H 4.071 0.038 1 535 65 65 LYS HB2 H 1.865 0.033 2 536 65 65 LYS HB3 H 1.751 0.000 2 537 65 65 LYS HG2 H 1.537 0.000 2 538 65 65 LYS HD2 H 1.659 0.000 2 539 65 65 LYS HE2 H 2.917 0.000 2 540 65 65 LYS CA C 60.149 0.059 1 541 65 65 LYS CB C 32.247 0.075 1 542 65 65 LYS CG C 25.612 0.000 1 543 65 65 LYS CD C 29.655 0.000 1 544 65 65 LYS CE C 42.303 0.000 1 545 65 65 LYS N N 120.844 0.060 1 546 66 66 LYS H H 6.966 0.011 1 547 66 66 LYS HA H 4.169 0.004 1 548 66 66 LYS HB2 H 1.927 0.000 2 549 66 66 LYS HB3 H 1.540 0.000 2 550 66 66 LYS HG2 H 1.561 0.010 2 551 66 66 LYS HD2 H 1.908 0.000 2 552 66 66 LYS HD3 H 1.758 0.000 2 553 66 66 LYS HE2 H 3.114 0.000 2 554 66 66 LYS CA C 59.581 0.033 1 555 66 66 LYS CB C 31.892 0.175 1 556 66 66 LYS CG C 25.689 0.043 1 557 66 66 LYS CD C 30.127 0.132 1 558 66 66 LYS CE C 42.395 0.000 1 559 66 66 LYS N N 120.201 0.048 1 560 67 67 VAL H H 7.312 0.008 1 561 67 67 VAL HA H 3.523 0.006 1 562 67 67 VAL HB H 1.431 0.004 1 563 67 67 VAL HG1 H -1.827 0.013 2 564 67 67 VAL HG2 H 0.179 0.006 2 565 67 67 VAL CA C 66.721 0.092 1 566 67 67 VAL CB C 30.801 0.141 1 567 67 67 VAL CG1 C 21.606 0.017 2 568 67 67 VAL CG2 C 19.856 0.045 2 569 67 67 VAL N N 121.046 0.037 1 570 68 68 LEU H H 8.198 0.009 1 571 68 68 LEU HA H 4.386 0.004 1 572 68 68 LEU HB2 H 1.533 0.012 2 573 68 68 LEU HB3 H 1.992 0.008 2 574 68 68 LEU HG H 1.986 0.001 1 575 68 68 LEU HD1 H 0.743 0.009 2 576 68 68 LEU HD2 H 0.755 0.008 2 577 68 68 LEU CA C 58.332 0.048 1 578 68 68 LEU CB C 41.390 0.042 1 579 68 68 LEU CG C 27.442 0.058 1 580 68 68 LEU CD1 C 25.257 0.053 2 581 68 68 LEU CD2 C 25.402 0.105 2 582 68 68 LEU N N 119.594 0.079 1 583 69 69 GLY CA C 47.475 0.027 1 584 69 69 GLY HA2 H 4.152 0.011 2 585 69 69 GLY H H 8.373 0.012 1 586 69 69 GLY N N 107.883 0.045 1 587 70 70 ALA H H 8.135 0.006 1 588 70 70 ALA HA H 4.843 0.023 1 589 70 70 ALA HB H 2.415 0.005 1 590 70 70 ALA CA C 55.321 0.000 1 591 70 70 ALA CB C 19.446 0.041 1 592 70 70 ALA N N 125.146 0.084 1 593 71 71 PHE H H 8.532 0.005 1 594 71 71 PHE HA H 4.209 0.005 1 595 71 71 PHE HB2 H 3.091 0.018 2 596 71 71 PHE HB3 H 3.620 0.001 2 597 71 71 PHE HD1 H 7.303 0.001 3 598 71 71 PHE CA C 64.731 0.056 1 599 71 71 PHE CB C 40.003 0.026 1 600 71 71 PHE CD1 C 131.800 0.011 3 601 71 71 PHE N N 118.247 0.048 1 602 72 72 SER H H 9.179 0.006 1 603 72 72 SER HA H 4.131 0.018 1 604 72 72 SER HB2 H 4.541 0.046 2 605 72 72 SER HB3 H 4.252 0.054 2 606 72 72 SER CA C 62.636 0.071 1 607 72 72 SER CB C 62.996 0.100 1 608 72 72 SER N N 116.183 0.069 1 609 73 73 ASP H H 8.313 0.015 1 610 73 73 ASP HA H 4.600 0.004 1 611 73 73 ASP HB2 H 3.011 0.009 2 612 73 73 ASP HB3 H 2.649 0.003 2 613 73 73 ASP CA C 57.561 0.021 1 614 73 73 ASP CB C 40.450 0.060 1 615 73 73 ASP N N 123.788 0.052 1 616 74 74 GLY H H 8.591 0.006 1 617 74 74 GLY HA2 H 3.588 0.006 2 618 74 74 GLY CA C 47.903 0.077 1 619 74 74 GLY N N 108.305 0.067 1 620 75 75 LEU H H 8.079 0.008 1 621 75 75 LEU HA H 3.714 0.027 1 622 75 75 LEU HB2 H 1.556 0.009 2 623 75 75 LEU HB3 H 1.171 0.015 2 624 75 75 LEU HG H 1.270 0.007 1 625 75 75 LEU HD1 H 0.348 0.004 2 626 75 75 LEU HD2 H -0.110 0.011 2 627 75 75 LEU CA C 57.733 0.034 1 628 75 75 LEU CB C 41.797 0.151 1 629 75 75 LEU CG C 27.270 0.028 1 630 75 75 LEU CD1 C 24.481 0.020 2 631 75 75 LEU CD2 C 23.672 0.045 2 632 75 75 LEU N N 119.879 0.095 1 633 76 76 ALA H H 7.364 0.009 1 634 76 76 ALA HA H 4.130 0.014 1 635 76 76 ALA HB H 1.284 0.004 1 636 76 76 ALA CA C 52.610 0.112 1 637 76 76 ALA CB C 19.031 0.015 1 638 76 76 ALA N N 118.691 0.049 1 639 77 77 HIS H H 7.659 0.008 1 640 77 77 HIS HA H 4.901 0.024 1 641 77 77 HIS HB2 H 3.229 0.007 2 642 77 77 HIS HB3 H 2.727 0.019 2 643 77 77 HIS HD2 H 7.362 0.004 1 644 77 77 HIS HE1 H 8.422 0.001 1 645 77 77 HIS CA C 54.503 0.085 1 646 77 77 HIS CB C 29.682 0.036 1 647 77 77 HIS CD2 C 121.407 0.030 1 648 77 77 HIS CE1 C 136.371 0.009 1 649 77 77 HIS N N 118.360 0.036 1 650 78 78 LEU H H 7.802 0.007 1 651 78 78 LEU HA H 3.875 0.013 1 652 78 78 LEU HB2 H 1.623 0.033 2 653 78 78 LEU HG H 2.053 0.014 1 654 78 78 LEU HD1 H 0.804 0.023 2 655 78 78 LEU HD2 H 0.826 0.004 2 656 78 78 LEU CA C 58.240 0.094 1 657 78 78 LEU CB C 42.070 0.006 1 658 78 78 LEU CG C 26.515 0.055 1 659 78 78 LEU CD1 C 26.032 0.020 2 660 78 78 LEU CD2 C 24.501 0.097 2 661 78 78 LEU N N 120.943 0.052 1 662 79 79 ASP H H 8.596 0.006 1 663 79 79 ASP HA H 4.497 0.004 1 664 79 79 ASP HB2 H 2.706 0.007 2 665 79 79 ASP CA C 54.183 0.009 1 666 79 79 ASP CB C 40.462 0.082 1 667 79 79 ASP N N 114.595 0.056 1 668 80 80 ASN H H 8.105 0.010 1 669 80 80 ASN HA H 5.109 0.017 1 670 80 80 ASN HB3 H 2.606 0.004 2 671 80 80 ASN CA C 52.014 0.021 1 672 80 80 ASN CB C 38.174 0.003 1 673 80 80 ASN N N 119.150 0.047 1 674 81 81 LEU H H 8.537 0.007 1 675 81 81 LEU HA H 3.958 0.026 1 676 81 81 LEU HD1 H 0.840 0.006 2 677 81 81 LEU HD2 H 0.808 0.031 2 678 81 81 LEU CA C 58.593 0.041 1 679 81 81 LEU CD1 C 24.623 0.000 2 680 81 81 LEU CD2 C 26.134 0.059 2 681 82 82 LYS H H 8.658 0.005 1 682 82 82 LYS HA H 3.626 0.002 1 683 82 82 LYS HB2 H 1.360 0.011 2 684 82 82 LYS HB3 H 1.651 0.005 2 685 82 82 LYS HG2 H 1.147 0.010 2 686 82 82 LYS HG3 H 0.829 0.007 2 687 82 82 LYS HD2 H 1.244 0.002 2 688 82 82 LYS CA C 60.995 0.012 1 689 82 82 LYS CB C 31.619 0.033 1 690 82 82 LYS CG C 25.751 0.065 1 691 82 82 LYS CD C 29.321 0.055 1 692 82 82 LYS N N 118.370 0.068 1 693 83 83 GLY H H 7.510 0.006 1 694 83 83 GLY HA2 H 3.789 0.000 2 695 83 83 GLY CA C 47.046 0.000 1 696 83 83 GLY N N 104.045 0.072 1 697 84 84 THR H H 7.577 0.018 1 698 84 84 THR HA H 3.704 0.005 1 699 84 84 THR HB H 3.771 0.012 1 700 84 84 THR HG2 H 0.494 0.007 1 701 84 84 THR CA C 66.407 0.035 1 702 84 84 THR CB C 68.924 0.047 1 703 84 84 THR CG2 C 20.478 0.038 1 704 84 84 THR N N 118.273 0.028 1 705 85 85 PHE H H 7.704 0.013 1 706 85 85 PHE HA H 4.671 0.009 1 707 85 85 PHE HB2 H 3.111 0.000 2 708 85 85 PHE HB3 H 2.606 0.000 2 709 85 85 PHE HD1 H 7.197 0.005 3 710 85 85 PHE HE1 H 7.193 0.002 3 711 85 85 PHE CA C 58.195 0.067 1 712 85 85 PHE CB C 38.347 0.005 1 713 85 85 PHE CD1 C 130.775 0.083 3 714 85 85 PHE CE1 C 131.212 0.068 3 715 85 85 PHE N N 115.814 0.071 1 716 86 86 ALA H H 7.114 0.005 1 717 86 86 ALA HA H 4.122 0.028 1 718 86 86 ALA HB H 1.528 0.009 1 719 86 86 ALA CA C 57.366 0.106 1 720 86 86 ALA CB C 18.399 0.060 1 721 86 86 ALA N N 124.988 0.052 1 722 87 87 THR H H 8.400 0.003 1 723 87 87 THR HA H 3.937 0.014 1 724 87 87 THR HB H 4.105 0.016 1 725 87 87 THR HG2 H 1.159 0.000 1 726 87 87 THR CA C 66.184 0.053 1 727 87 87 THR CB C 68.135 0.038 1 728 87 87 THR CG2 C 22.304 0.000 1 729 87 87 THR N N 114.294 0.077 1 730 88 88 LEU H H 7.848 0.007 1 731 88 88 LEU HA H 3.570 0.030 1 732 88 88 LEU HB2 H 0.324 0.029 2 733 88 88 LEU HB3 H 1.486 0.003 2 734 88 88 LEU HG H 1.400 0.000 1 735 88 88 LEU HD1 H 0.975 0.003 2 736 88 88 LEU HD2 H 0.585 0.014 2 737 88 88 LEU CA C 56.942 0.107 1 738 88 88 LEU CB C 42.154 0.131 1 739 88 88 LEU CG C 26.611 0.000 1 740 88 88 LEU CD1 C 25.934 0.042 2 741 88 88 LEU CD2 C 23.718 0.047 2 742 88 88 LEU N N 123.344 0.041 1 743 89 89 SER H H 8.990 0.007 1 744 89 89 SER HA H 3.784 0.001 1 745 89 89 SER HB3 H 3.816 0.003 2 746 89 89 SER CA C 60.880 0.065 1 747 89 89 SER CB C 64.094 0.147 1 748 89 89 SER N N 119.729 0.059 1 749 90 90 GLU CA C 60.206 0.124 1 750 90 90 GLU CB C 29.301 0.041 1 751 90 90 GLU CG C 36.367 0.070 1 752 90 90 GLU HA H 3.538 0.016 1 753 90 90 GLU HB2 H 1.965 0.010 2 754 90 90 GLU HG2 H 2.271 0.011 2 755 90 90 GLU HG3 H 1.968 0.016 2 756 90 90 GLU H H 7.548 0.012 1 757 90 90 GLU N N 120.234 0.072 1 758 91 91 LEU H H 7.253 0.010 1 759 91 91 LEU HA H 3.617 0.011 1 760 91 91 LEU HB2 H 1.342 0.000 2 761 91 91 LEU HB3 H 0.824 0.023 2 762 91 91 LEU HD1 H 0.530 0.019 2 763 91 91 LEU HD2 H -0.096 0.007 2 764 91 91 LEU CA C 57.789 0.097 1 765 91 91 LEU CB C 41.719 0.069 1 766 91 91 LEU CD1 C 22.768 0.047 2 767 91 91 LEU CD2 C 26.137 0.056 2 768 91 91 LEU N N 117.386 0.034 1 769 92 92 HIS H H 7.091 0.008 1 770 92 92 HIS HA H 2.627 0.001 1 771 92 92 HIS HD1 H 9.353 0.010 1 772 92 92 HIS HD2 H 0.889 0.000 1 773 92 92 HIS HE1 H 1.405 0.002 1 774 92 92 HIS CA C 60.597 0.006 1 775 92 92 HIS CD2 C 122.753 0.000 1 776 92 92 HIS CE1 C 132.239 0.016 1 777 92 92 HIS N N 112.027 0.044 1 778 92 92 HIS ND1 N 163.539 0.042 1 779 93 93 CYS H H 7.910 0.014 1 780 93 93 CYS HA H 4.188 0.009 1 781 93 93 CYS HB3 H 1.982 0.000 2 782 93 93 CYS CA C 60.334 0.079 1 783 93 93 CYS CB C 28.144 0.000 1 784 93 93 CYS N N 114.878 0.043 1 785 94 94 ASP H H 7.292 0.009 1 786 94 94 ASP HA H 4.267 0.010 1 787 94 94 ASP HB3 H 2.575 0.065 2 788 94 94 ASP CA C 56.785 0.088 1 789 94 94 ASP CB C 41.159 0.125 1 790 94 94 ASP N N 117.010 0.106 1 791 95 95 LYS H H 6.826 0.010 1 792 95 95 LYS HA H 4.272 0.013 1 793 95 95 LYS HB2 H 1.893 0.017 2 794 95 95 LYS HG2 H 1.211 0.009 2 795 95 95 LYS HD2 H 1.487 0.000 2 796 95 95 LYS HE2 H 2.862 0.000 2 797 95 95 LYS CA C 57.590 0.002 1 798 95 95 LYS CB C 32.070 0.007 1 799 95 95 LYS CG C 25.297 0.043 1 800 95 95 LYS CD C 28.956 0.000 1 801 95 95 LYS CE C 42.230 0.000 1 802 95 95 LYS N N 115.242 0.046 1 803 96 96 LEU H H 7.253 0.009 1 804 96 96 LEU HA H 4.199 0.003 1 805 96 96 LEU HG H 0.986 0.000 1 806 96 96 LEU HD1 H 0.928 0.020 2 807 96 96 LEU HD2 H -0.690 0.016 2 808 96 96 LEU CA C 55.321 0.000 1 809 96 96 LEU CG C 25.861 0.000 1 810 96 96 LEU CD1 C 22.147 0.065 2 811 96 96 LEU CD2 C 24.575 0.067 2 812 96 96 LEU N N 114.337 0.063 1 813 97 97 HIS H H 6.387 0.012 1 814 97 97 HIS HA H 4.505 0.010 1 815 97 97 HIS HB2 H 3.281 0.036 2 816 97 97 HIS HB3 H 3.695 0.013 2 817 97 97 HIS HD2 H 7.102 0.004 1 818 97 97 HIS HE1 H 8.323 0.005 1 819 97 97 HIS CA C 56.319 0.008 1 820 97 97 HIS CB C 26.443 0.103 1 821 97 97 HIS CD2 C 120.692 0.020 1 822 97 97 HIS CE1 C 137.103 0.011 1 823 97 97 HIS N N 110.856 0.055 1 824 98 98 VAL H H 8.057 0.012 1 825 98 98 VAL HA H 3.813 0.007 1 826 98 98 VAL HB H 1.325 0.000 1 827 98 98 VAL HG1 H 0.633 0.008 2 828 98 98 VAL HG2 H 0.130 0.019 2 829 98 98 VAL CA C 62.774 0.001 1 830 98 98 VAL CB C 32.753 0.000 1 831 98 98 VAL CG1 C 21.765 0.070 2 832 98 98 VAL CG2 C 21.348 0.078 2 833 98 98 VAL N N 119.491 0.049 1 834 99 99 ASP H H 9.297 0.012 1 835 99 99 ASP HA H 4.589 0.000 1 836 99 99 ASP HB2 H 2.721 0.000 2 837 99 99 ASP CA C 54.254 0.000 1 838 99 99 ASP CB C 43.365 0.000 1 839 99 99 ASP N N 130.974 0.056 1 840 100 100 PRO HA H 3.503 0.004 1 841 100 100 PRO HB2 H 2.036 0.000 2 842 100 100 PRO HB3 H 2.162 0.000 2 843 100 100 PRO HD2 H 3.612 0.081 2 844 100 100 PRO HD3 H 3.311 0.002 2 845 100 100 PRO CA C 64.327 0.052 1 846 100 100 PRO CB C 32.340 0.000 1 847 100 100 PRO CD C 51.282 0.000 1 848 101 101 GLU H H 9.088 0.015 1 849 101 101 GLU HA H 4.261 0.020 1 850 101 101 GLU HB2 H 1.935 0.020 2 851 101 101 GLU HB3 H 2.182 0.000 2 852 101 101 GLU HG2 H 2.292 0.007 2 853 101 101 GLU HG3 H 2.726 0.003 2 854 101 101 GLU CA C 59.397 0.057 1 855 101 101 GLU CB C 29.005 0.034 1 856 101 101 GLU CG C 35.700 0.050 1 857 101 101 GLU N N 123.745 0.111 1 858 102 102 ASN H H 8.200 0.009 1 859 102 102 ASN HA H 4.693 0.000 1 860 102 102 ASN CA C 56.774 0.000 1 861 102 102 ASN N N 112.413 0.072 1 862 103 103 PHE H H 7.610 0.014 1 863 103 103 PHE HA H 5.471 0.000 1 864 103 103 PHE HB2 H 3.539 0.000 2 865 103 103 PHE CA C 59.056 0.000 1 866 103 103 PHE CB C 38.320 0.000 1 867 103 103 PHE N N 117.932 0.063 1 868 104 104 ARG H H 7.349 0.007 1 869 104 104 ARG HA H 4.184 0.033 1 870 104 104 ARG HB2 H 2.097 0.047 2 871 104 104 ARG HG2 H 1.754 0.000 2 872 104 104 ARG HD2 H 3.277 0.000 2 873 104 104 ARG CA C 59.305 0.050 1 874 104 104 ARG CB C 30.029 0.033 1 875 104 104 ARG CG C 27.789 0.000 1 876 104 104 ARG CD C 43.495 0.000 1 877 104 104 ARG N N 119.480 0.044 1 878 105 105 LEU H H 8.007 0.017 1 879 105 105 LEU HA H 4.119 0.017 1 880 105 105 LEU HB2 H 1.952 0.000 2 881 105 105 LEU HB3 H 1.024 0.000 2 882 105 105 LEU HG H 1.907 0.000 1 883 105 105 LEU HD1 H 0.647 0.011 2 884 105 105 LEU HD2 H 0.583 0.016 2 885 105 105 LEU CA C 58.490 0.059 1 886 105 105 LEU CB C 40.578 0.005 1 887 105 105 LEU CG C 25.843 0.000 1 888 105 105 LEU CD1 C 24.762 0.023 2 889 105 105 LEU CD2 C 21.554 0.060 2 890 105 105 LEU N N 118.552 0.047 1 891 106 106 LEU H H 8.243 0.010 1 892 106 106 LEU HA H 4.213 0.008 1 893 106 106 LEU HB2 H 2.018 0.000 2 894 106 106 LEU HB3 H 2.621 0.000 2 895 106 106 LEU HG H 1.575 0.010 1 896 106 106 LEU HD1 H 0.567 0.011 2 897 106 106 LEU HD2 H 0.501 0.007 2 898 106 106 LEU CA C 58.907 0.001 1 899 106 106 LEU CB C 40.710 0.043 1 900 106 106 LEU CG C 28.641 0.059 1 901 106 106 LEU CD1 C 23.647 0.049 2 902 106 106 LEU CD2 C 25.401 0.065 2 903 106 106 LEU N N 118.358 0.115 1 904 107 107 GLY H H 8.178 0.014 1 905 107 107 GLY HA2 H 4.325 0.000 2 906 107 107 GLY HA3 H 3.843 0.000 2 907 107 107 GLY CA C 48.382 0.048 1 908 107 107 GLY N N 105.468 0.017 1 909 108 108 ASN H H 8.169 0.006 1 910 108 108 ASN HA H 4.704 0.036 1 911 108 108 ASN HB2 H 3.012 0.000 2 912 108 108 ASN CA C 55.321 0.000 1 913 108 108 ASN CB C 36.952 0.000 1 914 108 108 ASN N N 120.515 0.083 1 915 109 109 VAL H H 8.966 0.013 1 916 109 109 VAL HA H 3.801 0.003 1 917 109 109 VAL HB H 2.385 0.012 1 918 109 109 VAL HG1 H 1.075 0.029 2 919 109 109 VAL HG2 H 1.301 0.014 2 920 109 109 VAL CA C 68.271 0.073 1 921 109 109 VAL CB C 31.608 0.011 1 922 109 109 VAL CG1 C 25.276 0.042 2 923 109 109 VAL CG2 C 24.956 0.129 2 924 109 109 VAL N N 123.527 0.044 1 925 110 110 LEU H H 8.749 0.007 1 926 110 110 LEU HA H 3.776 0.028 1 927 110 110 LEU HB2 H 2.254 0.000 2 928 110 110 LEU HB3 H 1.047 0.015 2 929 110 110 LEU HG H 1.259 0.000 1 930 110 110 LEU HD1 H 0.128 0.022 2 931 110 110 LEU HD2 H 0.481 0.004 2 932 110 110 LEU CA C 58.906 0.077 1 933 110 110 LEU CB C 40.806 0.099 1 934 110 110 LEU CG C 27.250 0.000 1 935 110 110 LEU CD1 C 24.480 0.001 2 936 110 110 LEU CD2 C 22.928 0.015 1 937 110 110 LEU N N 121.078 0.054 1 938 111 111 VAL H H 7.986 0.012 1 939 111 111 VAL HA H 3.308 0.020 1 940 111 111 VAL HB H 2.661 0.007 1 941 111 111 VAL HG1 H 1.305 0.022 2 942 111 111 VAL HG2 H 1.373 0.011 2 943 111 111 VAL CA C 68.310 0.093 1 944 111 111 VAL CB C 31.434 0.066 1 945 111 111 VAL CG1 C 24.000 0.038 2 946 111 111 VAL CG2 C 21.810 0.018 2 947 111 111 VAL N N 118.598 0.075 1 948 112 112 CYS H H 8.104 0.012 1 949 112 112 CYS HA H 3.750 0.018 1 950 112 112 CYS HB2 H 3.450 0.007 2 951 112 112 CYS HB3 H 2.425 0.008 2 952 112 112 CYS CA C 65.257 0.104 1 953 112 112 CYS CB C 26.800 0.018 1 954 112 112 CYS N N 117.395 0.059 1 955 113 113 VAL H H 8.422 0.012 1 956 113 113 VAL HA H 3.510 0.015 1 957 113 113 VAL HB H 2.208 0.000 1 958 113 113 VAL HG1 H 0.862 0.003 2 959 113 113 VAL HG2 H 0.893 0.007 2 960 113 113 VAL CA C 66.831 0.052 1 961 113 113 VAL CB C 31.572 0.000 1 962 113 113 VAL CG1 C 22.945 0.002 2 963 113 113 VAL CG2 C 23.812 0.027 2 964 113 113 VAL N N 120.365 0.045 1 965 114 114 LEU H H 8.385 0.007 1 966 114 114 LEU HA H 3.678 0.023 1 967 114 114 LEU HG H 1.646 0.000 1 968 114 114 LEU HD1 H 0.320 0.007 2 969 114 114 LEU HD2 H 0.565 0.012 2 970 114 114 LEU CA C 58.114 0.120 1 971 114 114 LEU CG C 26.233 0.000 1 972 114 114 LEU CD1 C 25.510 0.017 2 973 114 114 LEU CD2 C 22.551 0.195 2 974 114 114 LEU N N 121.042 0.061 1 975 115 115 ALA H H 7.428 0.008 1 976 115 115 ALA HA H 3.324 0.015 1 977 115 115 ALA HB H 1.242 0.012 1 978 115 115 ALA CA C 55.217 0.104 1 979 115 115 ALA CB C 19.770 0.027 1 980 115 115 ALA N N 121.656 0.096 1 981 116 116 HIS H H 7.967 0.012 1 982 116 116 HIS HA H 4.022 0.021 1 983 116 116 HIS HB2 H 2.993 0.007 2 984 116 116 HIS HB3 H 3.463 0.030 2 985 116 116 HIS HD2 H 7.209 0.006 1 986 116 116 HIS CA C 58.035 0.019 1 987 116 116 HIS CB C 31.418 0.072 1 988 116 116 HIS CD2 C 117.438 0.035 1 989 116 116 HIS CE1 C 138.341 0.000 1 990 116 116 HIS N N 116.999 0.086 1 991 117 117 HIS H H 8.169 0.024 1 992 117 117 HIS HA H 3.800 0.010 1 993 117 117 HIS HB2 H 2.617 0.001 2 994 117 117 HIS HB3 H 2.147 0.005 2 995 117 117 HIS HD2 H 6.386 0.006 1 996 117 117 HIS CA C 59.110 0.059 1 997 117 117 HIS CB C 30.595 0.073 1 998 117 117 HIS CD2 C 119.883 0.110 1 999 117 117 HIS CE1 C 137.775 0.000 1 1000 117 117 HIS N N 115.765 0.083 1 1001 118 118 PHE H H 8.368 0.011 1 1002 118 118 PHE HA H 4.584 0.008 1 1003 118 118 PHE HB2 H 3.211 0.000 2 1004 118 118 PHE HB3 H 2.734 0.000 2 1005 118 118 PHE HD1 H 7.358 0.006 3 1006 118 118 PHE CA C 59.383 0.041 1 1007 118 118 PHE CB C 39.762 0.017 1 1008 118 118 PHE CD1 C 131.718 0.085 3 1009 118 118 PHE N N 114.887 0.079 1 1010 119 119 GLY H H 8.483 0.014 1 1011 119 119 GLY HA2 H 3.902 0.018 2 1012 119 119 GLY CA C 48.089 0.012 1 1013 119 119 GLY N N 113.592 0.066 1 1014 120 120 LYS H H 8.702 0.005 1 1015 120 120 LYS HA H 3.794 0.010 1 1016 120 120 LYS HB3 H 1.765 0.010 2 1017 120 120 LYS HG3 H 1.361 0.007 2 1018 120 120 LYS HD2 H 1.596 0.022 2 1019 120 120 LYS CA C 58.206 0.034 1 1020 120 120 LYS CB C 32.037 0.043 1 1021 120 120 LYS CG C 24.394 0.026 1 1022 120 120 LYS CD C 29.352 0.003 1 1023 120 120 LYS N N 125.030 0.097 1 1024 121 121 GLU H H 7.805 0.007 1 1025 121 121 GLU HA H 4.210 0.005 1 1026 121 121 GLU HB2 H 2.122 0.011 2 1027 121 121 GLU HG2 H 2.344 0.009 2 1028 121 121 GLU CA C 57.582 0.001 1 1029 121 121 GLU CB C 30.370 0.032 1 1030 121 121 GLU CG C 37.327 0.047 1 1031 121 121 GLU N N 116.831 0.047 1 1032 122 122 PHE H H 8.537 0.007 1 1033 122 122 PHE HA H 4.452 0.014 1 1034 122 122 PHE HB2 H 3.506 0.000 2 1035 122 122 PHE HB3 H 2.400 0.009 2 1036 122 122 PHE HD1 H 6.836 0.033 3 1037 122 122 PHE CA C 56.954 0.006 1 1038 122 122 PHE CB C 37.886 0.002 1 1039 122 122 PHE CD1 C 131.932 0.042 3 1040 122 122 PHE N N 126.301 0.086 1 1041 123 123 THR H H 7.165 0.013 1 1042 123 123 THR HA H 4.468 0.000 1 1043 123 123 THR HB H 4.374 0.000 1 1044 123 123 THR HG2 H 1.263 0.007 1 1045 123 123 THR CA C 60.822 0.000 1 1046 123 123 THR CB C 67.449 0.000 1 1047 123 123 THR CG2 C 22.662 0.068 1 1048 123 123 THR N N 113.320 0.053 1 1049 125 125 PRO HA H 4.204 0.008 1 1050 125 125 PRO HG3 H 1.857 0.000 2 1051 125 125 PRO HD2 H 3.565 0.022 2 1052 125 125 PRO CA C 66.124 0.075 1 1053 125 125 PRO CG C 28.486 0.000 1 1054 125 125 PRO CD C 50.144 0.000 1 1055 126 126 VAL H H 6.916 0.013 1 1056 126 126 VAL HA H 3.439 0.005 1 1057 126 126 VAL HB H 1.901 0.014 1 1058 126 126 VAL HG1 H 0.786 0.019 2 1059 126 126 VAL HG2 H 0.949 0.008 2 1060 126 126 VAL CA C 66.819 0.059 1 1061 126 126 VAL CB C 31.294 0.012 1 1062 126 126 VAL CG1 C 22.316 0.070 2 1063 126 126 VAL CG2 C 24.108 0.058 2 1064 126 126 VAL N N 120.999 0.072 1 1065 127 127 GLN H H 8.295 0.008 1 1066 127 127 GLN HA H 3.487 0.000 1 1067 127 127 GLN HB2 H 1.970 0.000 2 1068 127 127 GLN CA C 59.368 0.000 1 1069 127 127 GLN CB C 26.133 0.000 1 1070 127 127 GLN N N 119.741 0.066 1 1071 128 128 ALA H H 8.156 0.009 1 1072 128 128 ALA HA H 3.934 0.012 1 1073 128 128 ALA HB H 1.255 0.009 1 1074 128 128 ALA CA C 55.648 0.077 1 1075 128 128 ALA CB C 17.810 0.040 1 1076 128 128 ALA N N 121.720 0.051 1 1077 129 129 ALA H H 7.274 0.012 1 1078 129 129 ALA HA H 3.899 0.002 1 1079 129 129 ALA HB H 1.359 0.010 1 1080 129 129 ALA CA C 55.321 0.000 1 1081 129 129 ALA CB C 18.416 0.090 1 1082 129 129 ALA N N 120.077 0.116 1 1083 130 130 TYR H H 8.264 0.013 1 1084 130 130 TYR HA H 3.912 0.015 1 1085 130 130 TYR HD1 H 7.182 0.012 3 1086 130 130 TYR HE1 H 6.897 0.005 3 1087 130 130 TYR CA C 65.055 0.091 1 1088 130 130 TYR CD1 C 132.254 0.067 3 1089 130 130 TYR CE1 C 121.892 0.043 3 1090 130 130 TYR N N 116.203 0.040 1 1091 131 131 GLN H H 9.523 0.007 1 1092 131 131 GLN HA H 4.407 0.006 1 1093 131 131 GLN CA C 58.558 0.058 1 1094 131 131 GLN N N 119.142 0.095 1 1095 132 132 LYS H H 7.618 0.008 1 1096 132 132 LYS HA H 4.217 0.023 1 1097 132 132 LYS HB2 H 1.646 0.000 2 1098 132 132 LYS HB3 H 2.169 0.000 2 1099 132 132 LYS HG2 H 1.432 0.000 2 1100 132 132 LYS HG3 H 1.851 0.000 2 1101 132 132 LYS HD2 H 1.657 0.000 2 1102 132 132 LYS HE2 H 2.935 0.003 2 1103 132 132 LYS CA C 60.521 0.098 1 1104 132 132 LYS CB C 32.546 0.056 1 1105 132 132 LYS CG C 26.289 0.197 1 1106 132 132 LYS CD C 30.412 0.000 1 1107 132 132 LYS CE C 42.248 0.115 1 1108 132 132 LYS N N 121.039 0.119 1 1109 133 133 VAL H H 7.571 0.008 1 1110 133 133 VAL HA H 3.546 0.001 1 1111 133 133 VAL HB H 2.347 0.005 1 1112 133 133 VAL HG1 H 0.812 0.011 2 1113 133 133 VAL HG2 H 0.906 0.018 2 1114 133 133 VAL CA C 67.739 0.021 1 1115 133 133 VAL CB C 31.976 0.022 1 1116 133 133 VAL CG1 C 20.715 0.052 2 1117 133 133 VAL CG2 C 22.891 0.050 2 1118 133 133 VAL N N 119.223 0.056 1 1119 134 134 VAL H H 9.102 0.010 1 1120 134 134 VAL HA H 4.192 0.019 1 1121 134 134 VAL HB H 2.607 0.010 1 1122 134 134 VAL HG1 H 1.342 0.011 2 1123 134 134 VAL HG2 H 1.321 0.024 2 1124 134 134 VAL CA C 67.081 0.050 1 1125 134 134 VAL CB C 31.391 0.024 1 1126 134 134 VAL CG1 C 21.443 0.081 2 1127 134 134 VAL CG2 C 19.959 0.065 2 1128 134 134 VAL N N 113.878 0.049 1 1129 135 135 ALA H H 8.118 0.008 1 1130 135 135 ALA HA H 4.408 0.010 1 1131 135 135 ALA HB H 1.666 0.001 1 1132 135 135 ALA CA C 55.321 0.000 1 1133 135 135 ALA CB C 18.363 0.004 1 1134 135 135 ALA N N 124.553 0.095 1 1135 136 136 GLY H H 8.023 0.007 1 1136 136 136 GLY HA2 H 4.008 0.006 2 1137 136 136 GLY HA3 H 3.533 0.004 2 1138 136 136 GLY CA C 47.273 0.195 1 1139 136 136 GLY N N 106.850 0.059 1 1140 137 137 VAL H H 8.668 0.008 1 1141 137 137 VAL HA H 3.214 0.010 1 1142 137 137 VAL HB H 2.158 0.015 1 1143 137 137 VAL HG1 H 0.961 0.005 2 1144 137 137 VAL HG2 H 0.380 0.019 2 1145 137 137 VAL CA C 67.473 0.070 1 1146 137 137 VAL CB C 31.861 0.009 1 1147 137 137 VAL CG1 C 22.347 0.072 2 1148 137 137 VAL CG2 C 20.605 0.032 2 1149 137 137 VAL N N 124.249 0.064 1 1150 138 138 ALA H H 8.358 0.009 1 1151 138 138 ALA HA H 3.804 0.001 1 1152 138 138 ALA HB H 1.609 0.008 1 1153 138 138 ALA CA C 56.065 0.037 1 1154 138 138 ALA CB C 17.927 0.129 1 1155 138 138 ALA N N 121.232 0.057 1 1156 139 139 ASN H H 8.270 0.007 1 1157 139 139 ASN HA H 4.406 0.011 1 1158 139 139 ASN HB2 H 2.790 0.009 2 1159 139 139 ASN CA C 56.137 0.069 1 1160 139 139 ASN CB C 38.653 0.035 1 1161 139 139 ASN N N 114.855 0.062 1 1162 140 140 ALA H H 7.900 0.010 1 1163 140 140 ALA HA H 3.996 0.002 1 1164 140 140 ALA HB H 1.324 0.022 1 1165 140 140 ALA CA C 54.858 0.048 1 1166 140 140 ALA CB C 18.715 0.071 1 1167 140 140 ALA N N 122.549 0.064 1 1168 141 141 LEU H H 8.117 0.006 1 1169 141 141 LEU HA H 3.230 0.006 1 1170 141 141 LEU HB2 H 0.643 0.026 2 1171 141 141 LEU HB3 H -0.360 0.010 2 1172 141 141 LEU HG H 0.305 0.022 1 1173 141 141 LEU HD1 H -0.827 0.026 2 1174 141 141 LEU HD2 H -1.048 0.013 2 1175 141 141 LEU CA C 56.620 0.089 1 1176 141 141 LEU CB C 39.916 0.065 1 1177 141 141 LEU CG C 26.881 0.096 1 1178 141 141 LEU CD1 C 24.549 0.032 2 1179 141 141 LEU CD2 C 22.885 0.015 2 1180 141 141 LEU N N 120.557 0.067 1 1181 142 142 ALA H H 7.369 0.008 1 1182 142 142 ALA HA H 4.300 0.000 1 1183 142 142 ALA HB H 1.588 0.007 1 1184 142 142 ALA CA C 52.312 0.000 1 1185 142 142 ALA CB C 19.823 0.051 1 1186 142 142 ALA N N 118.780 0.071 1 1187 143 143 HIS H H 7.129 0.005 1 1188 143 143 HIS HA H 4.072 0.014 1 1189 143 143 HIS HB2 H 2.972 0.023 2 1190 143 143 HIS HB3 H 3.328 0.017 2 1191 143 143 HIS HD2 H 6.906 0.000 1 1192 143 143 HIS CA C 60.362 0.062 1 1193 143 143 HIS CB C 30.115 0.068 1 1194 143 143 HIS CD2 C 122.798 0.000 1 1195 143 143 HIS CE1 C 136.988 0.023 1 1196 143 143 HIS N N 118.257 0.058 1 1197 144 144 LYS H H 7.053 0.013 1 1198 144 144 LYS HA H 3.870 0.008 1 1199 144 144 LYS HB2 H 1.572 0.000 2 1200 144 144 LYS HB3 H 1.323 0.010 2 1201 144 144 LYS HG2 H 1.017 0.000 2 1202 144 144 LYS HG3 H 0.984 0.005 2 1203 144 144 LYS HD2 H 1.505 0.000 2 1204 144 144 LYS HD3 H 1.473 0.000 2 1205 144 144 LYS HE3 H 2.836 0.020 2 1206 144 144 LYS CA C 56.265 0.063 1 1207 144 144 LYS CB C 30.234 0.081 1 1208 144 144 LYS CG C 24.525 0.155 1 1209 144 144 LYS CD C 27.276 0.028 1 1210 144 144 LYS CE C 41.715 0.111 1 1211 144 144 LYS N N 115.563 0.130 1 1212 145 145 TYR H H 7.770 0.008 1 1213 145 145 TYR HA H 4.527 0.008 1 1214 145 145 TYR HB2 H 3.149 0.021 2 1215 145 145 TYR HB3 H 2.748 0.015 2 1216 145 145 TYR HD1 H 7.061 0.004 3 1217 145 145 TYR HE1 H 6.811 0.018 3 1218 145 145 TYR CA C 58.623 0.001 1 1219 145 145 TYR CB C 38.496 0.078 1 1220 145 145 TYR CD1 C 132.375 0.045 3 1221 145 145 TYR CE1 C 119.023 0.063 3 1222 145 145 TYR N N 118.084 0.059 1 1223 146 146 HIS H H 7.474 0.005 1 1224 146 146 HIS HA H 4.510 0.000 1 1225 146 146 HIS HB2 H 3.063 0.000 2 1226 146 146 HIS HD2 H 6.898 0.043 1 1227 146 146 HIS HE1 H 7.876 0.044 1 1228 146 146 HIS CA C 56.638 0.000 1 1229 146 146 HIS CB C 31.314 0.000 1 1230 146 146 HIS CD2 C 119.662 0.146 1 1231 146 146 HIS CE1 C 137.466 0.827 1 1232 146 146 HIS N N 124.445 0.050 1 stop_ save_