data_5856 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Backbone Resonances Assignments of Human Adult Hemoglobin in the Carbonmonoxy Form ; _BMRB_accession_number 5856 _BMRB_flat_file_name bmr5856.str _Entry_type original _Submission_date 2003-07-03 _Accession_date 2003-07-03 _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 Lukin Jonathan A. . 2 Kontaxis Georg . . 3 Simplaceanu Virgil . . 4 Yuan Yue . . 5 Bax Ad . . 6 Ho Chien . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 2 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 263 "13C chemical shifts" 749 "15N chemical shifts" 263 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2004-02-11 original author . stop_ _Original_release_date 2004-02-11 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; Letter to the Editor: Backbone Resonance Assignments of Human Adult Hemoglobin in the Carbonmonoxy Form ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 14755170 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Lukin Jonathan A. . 2 Kontaxis Georg . . 3 Simplaceanu Virgil . . 4 Yuan Yue . . 5 Bax Ad . . 6 Ho Chien . . stop_ _Journal_abbreviation 'J. Biomol. NMR' _Journal_volume 28 _Journal_issue 2 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 203 _Page_last 204 _Year 2004 _Details . loop_ _Keyword 'backbone assignment' 'Hb A in carbonmonoxy form (HbCO A)' 'HbCO A' 'human normnal adult hemoglobin (Hb A)' NMR recombinant stop_ save_ ####################################### # Cited references within the entry # ####################################### save_reference_1 _Saveframe_category citation _Citation_full ; Wishart, S., Bigam, C. G., Yao, J., Abildgaard, F., Dyson, H. J., Oldfield, E., Markley, J. L., and Sykes, B. M. "1H, 13C and 15N chemical shift referencing in biomolecular NMR", J. Biomol. NMR. 6, 135-140 (1995). ; _Citation_title '1H, 13C and 15N chemical shift referencing in biomolecular NMR.' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 8589602 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Wishart 'D. S.' S. . 2 Bigam 'C. G.' G. . 3 Yao J. . . 4 Abildgaard F. . . 5 Dyson 'H. J.' J. . 6 Oldfield E. . . 7 Markley 'J. L.' L. . 8 Sykes 'B. D.' D. . stop_ _Journal_abbreviation 'J. Biomol. NMR' _Journal_name_full 'Journal of biomolecular NMR' _Journal_volume 6 _Journal_issue 2 _Journal_CSD . _Book_title . _Book_chapter_title . _Book_volume . _Book_series . _Book_publisher . _Book_publisher_city . _Book_ISBN . _Conference_title . _Conference_site . _Conference_state_province . _Conference_country . _Conference_start_date . _Conference_end_date . _Conference_abstract_number . _Thesis_institution . _Thesis_institution_city . _Thesis_institution_country . _Page_first 135 _Page_last 140 _Year 1995 _Details ; A considerable degree of variability exists in the way that 1H, 13C and 15N chemical shifts are reported and referenced for biomolecules. In this article we explore some of the reasons for this situation and propose guidelines for future chemical shift referencing and for conversion from many common 1H, 13C and 15N chemical shift standards, now used in biomolecular NMR, to those proposed here. ; save_ ################################## # Molecular system description # ################################## save_system_HbCO_A _Saveframe_category molecular_system _Mol_system_name 'human normal adult hemoglobin carbonmonoxy form' _Abbreviation_common 'HbCO A' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'globin subunit alpha, one' $alpha_subunit 'globin subunit alpha, two' $alpha_subunit 'globin subunit beta, one' $beta_subunit 'globin subunit beta, two' $beta_subunit 'heme unit, one' $HEM 'heme unit, two' $HEM 'carbon monoxide, one' $CMO 'carbon monoxide, two' $CMO stop_ _System_molecular_weight 65336 _System_physical_state native _System_oligomer_state tetramer _System_paramagnetic no _System_thiol_state 'all free' _Database_query_date . _Details ; Tetrameric hemoglobin is a homodimer of heterodimers: (alpha-one, beta-one)(alpha-two, bea-two) with overall C2 symmetry. The two alpha subunits are magnetically equivalent and the two beta subunits are also magnetically eqivalent. ; save_ ######################## # Monomeric polymers # ######################## save_alpha_subunit _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'globin subunit alpha' _Abbreviation_common 'globin subunit alpha' _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_label 1 VAL 2 LEU 3 SER 4 PRO 5 ALA 6 ASP 7 LYS 8 THR 9 ASN 10 VAL 11 LYS 12 ALA 13 ALA 14 TRP 15 GLY 16 LYS 17 VAL 18 GLY 19 ALA 20 HIS 21 ALA 22 GLY 23 GLU 24 TYR 25 GLY 26 ALA 27 GLU 28 ALA 29 LEU 30 GLU 31 ARG 32 MET 33 PHE 34 LEU 35 SER 36 PHE 37 PRO 38 THR 39 THR 40 LYS 41 THR 42 TYR 43 PHE 44 PRO 45 HIS 46 PHE 47 ASP 48 LEU 49 SER 50 HIS 51 GLY 52 SER 53 ALA 54 GLN 55 VAL 56 LYS 57 GLY 58 HIS 59 GLY 60 LYS 61 LYS 62 VAL 63 ALA 64 ASP 65 ALA 66 LEU 67 THR 68 ASN 69 ALA 70 VAL 71 ALA 72 HIS 73 VAL 74 ASP 75 ASP 76 MET 77 PRO 78 ASN 79 ALA 80 LEU 81 SER 82 ALA 83 LEU 84 SER 85 ASP 86 LEU 87 HIS 88 ALA 89 HIS 90 LYS 91 LEU 92 ARG 93 VAL 94 ASP 95 PRO 96 VAL 97 ASN 98 PHE 99 LYS 100 LEU 101 LEU 102 SER 103 HIS 104 CYS 105 LEU 106 LEU 107 VAL 108 THR 109 LEU 110 ALA 111 ALA 112 HIS 113 LEU 114 PRO 115 ALA 116 GLU 117 PHE 118 THR 119 PRO 120 ALA 121 VAL 122 HIS 123 ALA 124 SER 125 LEU 126 ASP 127 LYS 128 PHE 129 LEU 130 ALA 131 SER 132 VAL 133 SER 134 THR 135 VAL 136 LEU 137 THR 138 SER 139 LYS 140 TYR 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 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 7125 globin_subunit_beta 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_beta_subunit _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'globin subunit beta' _Abbreviation_common 'globin subunit beta' _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_label 1 VAL 2 HIS 3 LEU 4 THR 5 PRO 6 GLU 7 GLU 8 LYS 9 SER 10 ALA 11 VAL 12 THR 13 ALA 14 LEU 15 TRP 16 GLY 17 LYS 18 VAL 19 ASN 20 VAL 21 ASP 22 GLU 23 VAL 24 GLY 25 GLY 26 GLU 27 ALA 28 LEU 29 GLY 30 ARG 31 LEU 32 LEU 33 VAL 34 VAL 35 TYR 36 PRO 37 TRP 38 THR 39 GLN 40 ARG 41 PHE 42 PHE 43 GLU 44 SER 45 PHE 46 GLY 47 ASP 48 LEU 49 SER 50 THR 51 PRO 52 ASP 53 ALA 54 VAL 55 MET 56 GLY 57 ASN 58 PRO 59 LYS 60 VAL 61 LYS 62 ALA 63 HIS 64 GLY 65 LYS 66 LYS 67 VAL 68 LEU 69 GLY 70 ALA 71 PHE 72 SER 73 ASP 74 GLY 75 LEU 76 ALA 77 HIS 78 LEU 79 ASP 80 ASN 81 LEU 82 LYS 83 GLY 84 THR 85 PHE 86 ALA 87 THR 88 LEU 89 SER 90 GLU 91 LEU 92 HIS 93 CYS 94 ASP 95 LYS 96 LEU 97 HIS 98 VAL 99 ASP 100 PRO 101 GLU 102 ASN 103 PHE 104 ARG 105 LEU 106 LEU 107 GLY 108 ASN 109 VAL 110 LEU 111 VAL 112 CYS 113 VAL 114 LEU 115 ALA 116 HIS 117 HIS 118 PHE 119 GLY 120 LYS 121 GLU 122 PHE 123 THR 124 PRO 125 PRO 126 VAL 127 GLN 128 ALA 129 ALA 130 TYR 131 GLN 132 LYS 133 VAL 134 VAL 135 ALA 136 GLY 137 VAL 138 ALA 139 ASN 140 ALA 141 LEU 142 ALA 143 HIS 144 LYS 145 TYR 146 HIS stop_ _Sequence_homology_query_date 2008-08-19 _Sequence_homology_query_revised_last_date 2008-08-19 save_ ############# # Ligands # ############# save_HEM _Saveframe_category ligand _Mol_type non-polymer _Name_common "HEM (PROTOPORPHYRIN IX CONTAINING FE)" _BMRB_code . _PDB_code HEM _Molecular_mass 616.487 _Mol_charge 0 _Mol_paramagnetic . _Mol_aromatic yes _Details ; Information obtained from PDB's Chemical Component Dictionary at http://wwpdb-remediation.rutgers.edu/downloads.html Downloaded on Wed Jul 27 14:00:32 2011 ; loop_ _Atom_name _PDB_atom_name _Atom_type _Atom_chirality _Atom_charge _Atom_oxidation_number _Atom_unpaired_electrons CHA CHA C . 0 . ? CHB CHB C . 0 . ? CHC CHC C . 0 . ? CHD CHD C . 0 . ? C1A C1A C . 0 . ? C2A C2A C . 0 . ? C3A C3A C . 0 . ? C4A C4A C . 0 . ? CMA CMA C . 0 . ? CAA CAA C . 0 . ? CBA CBA C . 0 . ? CGA CGA C . 0 . ? O1A O1A O . 0 . ? O2A O2A O . 0 . ? C1B C1B C . 0 . ? C2B C2B C . 0 . ? C3B C3B C . 0 . ? C4B C4B C . 0 . ? CMB CMB C . 0 . ? CAB CAB C . 0 . ? CBB CBB C . 0 . ? C1C C1C C . 0 . ? C2C C2C C . 0 . ? C3C C3C C . 0 . ? C4C C4C C . 0 . ? CMC CMC C . 0 . ? CAC CAC C . 0 . ? CBC CBC C . 0 . ? C1D C1D C . 0 . ? C2D C2D C . 0 . ? C3D C3D C . 0 . ? C4D C4D C . 0 . ? CMD CMD C . 0 . ? CAD CAD C . 0 . ? CBD CBD C . 0 . ? CGD CGD C . 0 . ? O1D O1D O . 0 . ? O2D O2D O . 0 . ? NA NA N . 0 . ? NB NB N . 0 . ? NC NC N . 0 . ? ND ND N . 0 . ? FE FE FE . 0 . ? HHB HHB H . 0 . ? HHC HHC H . 0 . ? HHD HHD H . 0 . ? HMA HMA H . 0 . ? HMAA HMAA H . 0 . ? HMAB HMAB H . 0 . ? HAA HAA H . 0 . ? HAAA HAAA H . 0 . ? HBA HBA H . 0 . ? HBAA HBAA H . 0 . ? HMB HMB H . 0 . ? HMBA HMBA H . 0 . ? HMBB HMBB H . 0 . ? HAB HAB H . 0 . ? HBB HBB H . 0 . ? HBBA HBBA H . 0 . ? HMC HMC H . 0 . ? HMCA HMCA H . 0 . ? HMCB HMCB H . 0 . ? HAC HAC H . 0 . ? HBC HBC H . 0 . ? HBCA HBCA H . 0 . ? HMD HMD H . 0 . ? HMDA HMDA H . 0 . ? HMDB HMDB H . 0 . ? HAD HAD H . 0 . ? HADA HADA H . 0 . ? HBD HBD H . 0 . ? HBDA HBDA H . 0 . ? H2A H2A H . 0 . ? H2D H2D H . 0 . ? HHA HHA H . 0 . ? stop_ loop_ _Bond_order _Bond_atom_one_atom_name _Bond_atom_two_atom_name _PDB_bond_atom_one_atom_name _PDB_bond_atom_two_atom_name SING CHA C1A ? ? DOUB CHA C4D ? ? SING CHA HHA ? ? SING CHB C4A ? ? DOUB CHB C1B ? ? SING CHB HHB ? ? SING CHC C4B ? ? DOUB CHC C1C ? ? SING CHC HHC ? ? DOUB CHD C4C ? ? SING CHD C1D ? ? SING CHD HHD ? ? DOUB C1A C2A ? ? SING C1A NA ? ? SING C2A C3A ? ? SING C2A CAA ? ? DOUB C3A C4A ? ? SING C3A CMA ? ? SING C4A NA ? ? SING CMA HMA ? ? SING CMA HMAA ? ? SING CMA HMAB ? ? SING CAA CBA ? ? SING CAA HAA ? ? SING CAA HAAA ? ? SING CBA CGA ? ? SING CBA HBA ? ? SING CBA HBAA ? ? DOUB CGA O1A ? ? SING CGA O2A ? ? SING C1B C2B ? ? SING C1B NB ? ? DOUB C2B C3B ? ? SING C2B CMB ? ? SING C3B C4B ? ? SING C3B CAB ? ? DOUB C4B NB ? ? SING CMB HMB ? ? SING CMB HMBA ? ? SING CMB HMBB ? ? DOUB CAB CBB ? ? SING CAB HAB ? ? SING CBB HBB ? ? SING CBB HBBA ? ? SING C1C C2C ? ? SING C1C NC ? ? DOUB C2C C3C ? ? SING C2C CMC ? ? SING C3C C4C ? ? SING C3C CAC ? ? SING C4C NC ? ? SING CMC HMC ? ? SING CMC HMCA ? ? SING CMC HMCB ? ? DOUB CAC CBC ? ? SING CAC HAC ? ? SING CBC HBC ? ? SING CBC HBCA ? ? SING C1D C2D ? ? DOUB C1D ND ? ? DOUB C2D C3D ? ? SING C2D CMD ? ? SING C3D C4D ? ? SING C3D CAD ? ? SING C4D ND ? ? SING CMD HMD ? ? SING CMD HMDA ? ? SING CMD HMDB ? ? SING CAD CBD ? ? SING CAD HAD ? ? SING CAD HADA ? ? SING CBD CGD ? ? SING CBD HBD ? ? SING CBD HBDA ? ? DOUB CGD O1D ? ? SING CGD O2D ? ? SING O2A H2A ? ? SING O2D H2D ? ? SING FE NA ? ? SING FE NB ? ? SING FE NC ? ? SING FE ND ? ? stop_ _Mol_thiol_state . _Sequence_homology_query_date . save_ save_CMO _Saveframe_category ligand _Mol_type non-polymer _Name_common "CMO (CARBON MONOXIDE)" _BMRB_code . _PDB_code CMO _Molecular_mass 28.010 _Mol_charge 0 _Mol_paramagnetic . _Mol_aromatic no _Details ; Information obtained from PDB's Chemical Component Dictionary at http://wwpdb-remediation.rutgers.edu/downloads.html Downloaded on Wed Jul 27 14:02:43 2011 ; loop_ _Atom_name _PDB_atom_name _Atom_type _Atom_chirality _Atom_charge _Atom_oxidation_number _Atom_unpaired_electrons C C C . -1 . ? O O O . 1 . ? 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 TRIP C O ? ? 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 _Organ _Cell_type $alpha_subunit Human 9606 Eukaryota Metazoa Homo sapiens blood 'red blood cell' $beta_subunit Human 9606 Eukaryota Metazoa Homo sapiens blood 'red blood cell' stop_ save_ ######################### # Experimental source # ######################### save_experimental_source _Saveframe_category experimental_source loop_ _Mol_label _Production_method _Host_organism_name_common _Genus _Species _Strain _Vector_type _Vector_name $alpha_subunit 'recombinant technology' 'E. coli' Escherichia coli JM109 plasmid pHE2 $beta_subunit 'recombinant technology' 'E. coli' Escherichia coli JM109 plasmid pHE2 stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_one _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $alpha_subunit 1.0 mM '[U-2H; U-13C; U-15N]' $beta_subunit 1.0 mM '[U-2H; U-13C; U-15N]' 'Na phosphate' 0.1 M . H2O 90 % . D2O 10 % . stop_ save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_list _Saveframe_category NMR_spectrometer _Manufacturer unknown _Model unknown _Field_strength 0 _Details 'spectrometer information not available' save_ ############################# # NMR applied experiments # ############################# save__1 _Saveframe_category NMR_applied_experiment _Sample_label $sample_one save_ ####################### # Sample conditions # ####################### save_sample_conditions _Saveframe_category sample_conditions _Details 'Aqueous phosphate buffer.' loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 7.0 . n/a temperature 302.0 0.1 K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference _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 _Indirect_shift_ratio_citation_label DSS C 13 'methyl protons' ppm 0.0 internal indirect . . . 0.251449530 $reference_1 H2O H 1 protons ppm 4.76 internal direct . . . 1.0 $reference_1 DSS N 15 'methyl protons' ppm 0.0 internal indirect . . . 0.101329150 $reference_1 stop_ save_ ################################### # Assigned chemical shift lists # ################################### ################################################################### # Chemical Shift Ambiguity Index Value Definitions # # # # The values other than 1 are used for those atoms with different # # chemical shifts that cannot be assigned to stereospecific atoms # # or to specific residues or chains. # # # # Index Value Definition # # # # 1 Unique (including isolated methyl protons, # # geminal atoms, and geminal methyl # # groups with identical chemical shifts) # # (e.g. ILE HD11, HD12, HD13 protons) # # 2 Ambiguity of geminal atoms or geminal methyl # # proton groups (e.g. ASP HB2 and HB3 # # protons, LEU CD1 and CD2 carbons, or # # LEU HD11, HD12, HD13 and HD21, HD22, # # HD23 methyl protons) # # 3 Aromatic atoms on opposite sides of # # symmetrical rings (e.g. TYR HE1 and HE2 # # protons) # # 4 Intraresidue ambiguities (e.g. LYS HG and # # HD protons or TRP HZ2 and HZ3 protons) # # 5 Interresidue ambiguities (LYS 12 vs. LYS 27) # # 6 Intermolecular ambiguities (e.g. ASP 31 CA # # in monomer 1 and ASP 31 CA in monomer 2 # # of an asymmetrical homodimer, duplex # # DNA assignments, or other assignments # # that may apply to atoms in one or more # # molecule in the molecular assembly) # # 9 Ambiguous, specific ambiguity not defined # # # ################################################################### save_chemical_shift_1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Sample_label $sample_one stop_ _Sample_conditions_label $sample_conditions _Chem_shift_reference_set_label $chemical_shift_reference _Mol_system_component_name 'globin subunit alpha, one' _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 VAL CA C 57.250 0.100 1 2 . 1 VAL C C 178.050 0.100 1 3 . 2 LEU H H 7.010 0.030 1 4 . 2 LEU N N 116.590 0.050 1 5 . 2 LEU CA C 54.110 0.100 1 6 . 2 LEU CB C 40.250 0.100 1 7 . 2 LEU C C 176.470 0.100 1 8 . 3 SER H H 9.750 0.030 1 9 . 3 SER N N 122.080 0.050 1 10 . 3 SER CA C 56.270 0.100 1 11 . 3 SER C C 173.470 0.100 1 12 . 4 PRO CA C 65.840 0.100 1 13 . 4 PRO C C 179.440 0.100 1 14 . 5 ALA H H 7.900 0.030 1 15 . 5 ALA N N 119.940 0.050 1 16 . 5 ALA CA C 54.360 0.100 1 17 . 5 ALA C C 179.895 0.015 1 18 . 6 ASP H H 8.060 0.030 1 19 . 6 ASP N N 118.380 0.050 1 20 . 6 ASP CA C 57.040 0.070 1 21 . 6 ASP C C 178.720 0.100 1 22 . 7 LYS H H 8.080 0.030 1 23 . 7 LYS N N 119.050 0.050 1 24 . 7 LYS CA C 60.575 0.055 1 25 . 7 LYS CB C 31.240 0.010 1 26 . 7 LYS C C 178.410 0.030 1 27 . 8 THR H H 7.990 0.030 1 28 . 8 THR N N 116.110 0.050 1 29 . 8 THR CA C 66.190 0.000 1 30 . 8 THR CB C 68.050 0.100 1 31 . 8 THR C C 176.740 0.100 1 32 . 9 ASN H H 8.280 0.030 1 33 . 9 ASN N N 121.210 0.050 1 34 . 9 ASN CA C 55.090 0.100 1 35 . 9 ASN CB C 37.370 0.030 1 36 . 9 ASN C C 177.690 0.020 1 37 . 10 VAL H H 8.420 0.030 1 38 . 10 VAL N N 119.870 0.050 1 39 . 10 VAL CA C 66.475 0.025 1 40 . 10 VAL CB C 30.480 0.100 1 41 . 10 VAL C C 177.090 0.040 1 42 . 11 LYS H H 7.980 0.030 1 43 . 11 LYS N N 118.710 0.050 1 44 . 11 LYS CA C 59.700 0.020 1 45 . 11 LYS CB C 31.480 0.040 1 46 . 11 LYS C C 180.015 0.015 1 47 . 12 ALA H H 8.140 0.030 1 48 . 12 ALA N N 121.940 0.050 1 49 . 12 ALA CA C 54.300 0.010 1 50 . 12 ALA CB C 17.200 0.030 1 51 . 12 ALA C C 180.675 0.075 1 52 . 13 ALA H H 8.190 0.030 1 53 . 13 ALA N N 120.990 0.050 1 54 . 13 ALA CA C 54.860 0.000 1 55 . 13 ALA CB C 17.230 0.100 1 56 . 13 ALA C C 179.305 0.025 1 57 . 14 TRP H H 9.030 0.030 1 58 . 14 TRP N N 117.860 0.050 1 59 . 14 TRP CA C 59.360 0.050 1 60 . 14 TRP CB C 28.400 0.150 1 61 . 14 TRP C C 179.595 0.065 1 62 . 15 GLY H H 7.970 0.030 1 63 . 15 GLY N N 106.180 0.050 1 64 . 15 GLY CA C 46.200 0.020 1 65 . 15 GLY C C 175.980 0.010 1 66 . 16 LYS H H 7.250 0.030 1 67 . 16 LYS N N 120.260 0.050 1 68 . 16 LYS CA C 56.235 0.015 1 69 . 16 LYS CB C 30.785 0.055 1 70 . 16 LYS C C 178.490 0.030 1 71 . 17 VAL H H 7.440 0.030 1 72 . 17 VAL N N 121.220 0.050 1 73 . 17 VAL CA C 65.680 0.020 1 74 . 17 VAL CB C 29.855 0.005 1 75 . 17 VAL C C 177.470 0.030 1 76 . 18 GLY H H 7.110 0.030 1 77 . 18 GLY N N 103.020 0.050 1 78 . 18 GLY CA C 46.500 0.100 1 79 . 18 GLY C C 176.110 0.100 1 80 . 19 ALA CA C 52.740 0.100 1 81 . 19 ALA CB C 17.190 0.100 1 82 . 19 ALA C C 178.050 0.100 1 83 . 20 HIS H H 7.730 0.030 1 84 . 20 HIS N N 115.450 0.050 1 85 . 20 HIS CA C 55.120 0.010 1 86 . 20 HIS CB C 28.075 0.015 1 87 . 20 HIS C C 173.705 0.015 1 88 . 21 ALA H H 6.940 0.030 1 89 . 21 ALA N N 122.020 0.050 1 90 . 21 ALA CA C 55.860 0.050 1 91 . 21 ALA CB C 17.540 0.100 1 92 . 21 ALA C C 178.135 0.005 1 93 . 22 GLY H H 8.410 0.030 1 94 . 22 GLY N N 104.690 0.050 1 95 . 22 GLY CA C 46.920 0.010 1 96 . 22 GLY C C 176.330 0.030 1 97 . 23 GLU H H 7.690 0.030 1 98 . 23 GLU N N 124.370 0.050 1 99 . 23 GLU CA C 58.425 0.025 1 100 . 23 GLU CB C 27.925 0.005 1 101 . 23 GLU C C 179.650 0.010 1 102 . 24 TYR H H 7.950 0.030 1 103 . 24 TYR N N 121.080 0.050 1 104 . 24 TYR CA C 56.680 0.020 1 105 . 24 TYR CB C 33.950 0.000 1 106 . 24 TYR C C 178.410 0.030 1 107 . 25 GLY H H 8.760 0.030 1 108 . 25 GLY N N 107.830 0.050 1 109 . 25 GLY CA C 46.120 0.030 1 110 . 25 GLY C C 174.330 0.000 1 111 . 26 ALA H H 7.700 0.030 1 112 . 26 ALA N N 121.460 0.050 1 113 . 26 ALA CA C 54.245 0.005 1 114 . 26 ALA CB C 18.160 0.030 1 115 . 26 ALA C C 178.340 0.040 1 116 . 27 GLU H H 7.820 0.030 1 117 . 27 GLU N N 119.690 0.050 1 118 . 27 GLU CA C 58.480 0.010 1 119 . 27 GLU CB C 28.410 0.040 1 120 . 27 GLU C C 177.915 0.005 1 121 . 28 ALA H H 8.290 0.030 1 122 . 28 ALA N N 121.890 0.050 1 123 . 28 ALA CA C 55.210 0.010 1 124 . 28 ALA CB C 16.630 0.100 1 125 . 28 ALA C C 179.010 0.070 1 126 . 29 LEU H H 7.000 0.030 1 127 . 29 LEU N N 115.810 0.050 1 128 . 29 LEU CA C 56.835 0.045 1 129 . 29 LEU CB C 39.335 0.065 1 130 . 29 LEU C C 176.175 0.045 1 131 . 30 GLU H H 7.760 0.030 1 132 . 30 GLU N N 118.270 0.050 1 133 . 30 GLU CA C 59.690 0.010 1 134 . 30 GLU CB C 28.480 0.100 1 135 . 30 GLU C C 179.470 0.000 1 136 . 31 ARG H H 8.630 0.030 1 137 . 31 ARG N N 116.430 0.050 1 138 . 31 ARG CA C 59.895 0.055 1 139 . 31 ARG CB C 28.370 0.100 1 140 . 31 ARG C C 178.220 0.000 1 141 . 32 MET H H 7.900 0.030 1 142 . 32 MET N N 123.270 0.050 1 143 . 32 MET CA C 59.805 0.055 1 144 . 32 MET CB C 31.440 0.100 1 145 . 32 MET C C 177.145 0.065 1 146 . 33 PHE H H 8.360 0.030 1 147 . 33 PHE N N 118.510 0.050 1 148 . 33 PHE CA C 57.970 0.000 1 149 . 33 PHE CB C 37.180 0.100 1 150 . 33 PHE C C 178.120 0.020 1 151 . 34 LEU H H 7.610 0.030 1 152 . 34 LEU N N 114.110 0.050 1 153 . 34 LEU CA C 56.050 0.030 1 154 . 34 LEU CB C 41.950 0.100 1 155 . 34 LEU C C 179.020 0.100 1 156 . 35 SER H H 7.900 0.030 1 157 . 35 SER N N 113.110 0.050 1 158 . 35 SER CA C 62.350 0.060 1 159 . 35 SER CB C 63.490 0.100 1 160 . 35 SER C C 173.360 0.100 1 161 . 36 PHE H H 8.310 0.030 1 162 . 36 PHE N N 117.910 0.050 1 163 . 36 PHE CA C 53.930 0.100 1 164 . 36 PHE CB C 38.400 0.100 1 165 . 37 PRO CA C 64.940 0.100 1 166 . 37 PRO C C 179.660 0.100 1 167 . 38 THR H H 8.300 0.030 1 168 . 38 THR N N 113.010 0.050 1 169 . 38 THR CA C 65.205 0.025 1 170 . 38 THR C C 178.020 0.100 1 171 . 39 THR H H 8.810 0.030 1 172 . 39 THR N N 115.110 0.050 1 173 . 39 THR CA C 66.040 0.000 1 174 . 39 THR CB C 70.190 0.100 1 175 . 39 THR C C 177.050 0.100 1 176 . 40 LYS H H 7.690 0.030 1 177 . 40 LYS N N 118.460 0.050 1 178 . 40 LYS CA C 59.085 0.065 1 179 . 40 LYS CB C 31.000 0.100 1 180 . 40 LYS C C 179.875 0.015 1 181 . 41 THR H H 7.730 0.030 1 182 . 41 THR N N 111.200 0.050 1 183 . 41 THR CA C 63.890 0.010 1 184 . 41 THR C C 175.220 0.000 1 185 . 42 TYR H H 7.420 0.030 1 186 . 42 TYR N N 117.120 0.050 1 187 . 42 TYR CA C 59.940 0.010 1 188 . 42 TYR CB C 38.610 0.100 1 189 . 42 TYR C C 173.855 0.025 1 190 . 43 PHE H H 7.760 0.030 1 191 . 43 PHE N N 117.090 0.050 1 192 . 43 PHE CA C 54.680 0.100 1 193 . 43 PHE CB C 39.060 0.100 1 194 . 43 PHE C C 173.960 0.100 1 195 . 44 PRO CA C 64.830 0.100 1 196 . 44 PRO CB C 30.360 0.100 1 197 . 44 PRO C C 177.270 0.100 1 198 . 45 HIS H H 9.470 0.030 1 199 . 45 HIS N N 116.840 0.050 1 200 . 45 HIS CA C 54.915 0.015 1 201 . 45 HIS CB C 29.065 0.055 1 202 . 45 HIS C C 175.480 0.040 1 203 . 46 PHE H H 7.440 0.030 1 204 . 46 PHE N N 122.760 0.050 1 205 . 46 PHE CA C 55.280 0.010 1 206 . 46 PHE CB C 39.340 0.000 1 207 . 46 PHE C C 175.700 0.040 1 208 . 47 ASP H H 7.830 0.030 1 209 . 47 ASP N N 119.400 0.050 1 210 . 47 ASP CA C 52.985 0.035 1 211 . 47 ASP CB C 39.255 0.015 1 212 . 47 ASP C C 176.300 0.050 1 213 . 48 LEU H H 8.470 0.030 1 214 . 48 LEU N N 128.220 0.050 1 215 . 48 LEU CA C 52.950 0.020 1 216 . 48 LEU CB C 39.460 0.170 1 217 . 48 LEU C C 177.045 0.025 1 218 . 49 SER H H 8.110 0.030 1 219 . 49 SER N N 117.430 0.050 1 220 . 49 SER CA C 58.630 0.100 1 221 . 49 SER CB C 63.360 0.100 1 222 . 49 SER C C 174.325 0.055 1 223 . 50 HIS H H 8.570 0.030 1 224 . 50 HIS N N 121.580 0.050 1 225 . 50 HIS CA C 57.275 0.055 1 226 . 50 HIS CB C 27.760 0.100 1 227 . 50 HIS C C 176.990 0.100 1 228 . 51 GLY H H 8.920 0.030 1 229 . 51 GLY N N 116.290 0.050 1 230 . 51 GLY CA C 44.630 0.050 1 231 . 51 GLY C C 174.130 0.030 1 232 . 52 SER H H 7.370 0.030 1 233 . 52 SER N N 114.730 0.050 1 234 . 52 SER CA C 56.520 0.100 1 235 . 52 SER CB C 64.010 0.100 1 236 . 52 SER C C 176.430 0.010 1 237 . 53 ALA H H 9.010 0.030 1 238 . 53 ALA N N 131.580 0.050 1 239 . 53 ALA CA C 54.180 0.100 1 240 . 53 ALA C C 180.800 0.100 1 241 . 54 GLN H H 8.210 0.030 1 242 . 54 GLN N N 120.070 0.050 1 243 . 54 GLN CA C 58.220 0.100 1 244 . 54 GLN CB C 27.740 0.110 1 245 . 54 GLN C C 179.300 0.000 1 246 . 55 VAL H H 7.450 0.030 1 247 . 55 VAL N N 121.980 0.050 1 248 . 55 VAL CA C 66.585 0.075 1 249 . 55 VAL CB C 30.705 0.065 1 250 . 55 VAL C C 177.480 0.020 1 251 . 56 LYS H H 7.660 0.030 1 252 . 56 LYS N N 120.220 0.050 1 253 . 56 LYS CA C 59.270 0.110 1 254 . 56 LYS CB C 30.905 0.045 1 255 . 56 LYS C C 180.230 0.040 1 256 . 57 GLY H H 8.170 0.030 1 257 . 57 GLY N N 106.200 0.050 1 258 . 57 GLY CA C 46.220 0.020 1 259 . 57 GLY C C 176.625 0.015 1 260 . 58 HIS H H 8.090 0.030 1 261 . 58 HIS N N 124.610 0.050 1 262 . 58 HIS CA C 59.465 0.035 1 263 . 58 HIS CB C 30.365 0.005 1 264 . 58 HIS C C 177.190 0.020 1 265 . 59 GLY H H 8.480 0.030 1 266 . 59 GLY N N 105.800 0.050 1 267 . 59 GLY CA C 45.815 0.025 1 268 . 59 GLY C C 174.925 0.015 1 269 . 60 LYS H H 7.000 0.030 1 270 . 60 LYS N N 120.280 0.050 1 271 . 60 LYS CA C 58.880 0.050 1 272 . 60 LYS CB C 31.005 0.105 1 273 . 60 LYS C C 177.320 0.000 1 274 . 61 LYS H H 6.890 0.030 1 275 . 61 LYS N N 118.490 0.050 1 276 . 61 LYS CA C 59.575 0.055 1 277 . 61 LYS CB C 30.930 0.100 1 278 . 61 LYS C C 180.385 0.055 1 279 . 62 VAL H H 7.660 0.030 1 280 . 62 VAL N N 120.500 0.050 1 281 . 62 VAL CA C 66.280 0.020 1 282 . 62 VAL CB C 30.310 0.100 1 283 . 62 VAL C C 177.460 0.040 1 284 . 63 ALA H H 8.080 0.030 1 285 . 63 ALA N N 120.930 0.050 1 286 . 63 ALA CA C 55.240 0.000 1 287 . 63 ALA CB C 18.325 0.055 1 288 . 63 ALA C C 179.875 0.045 1 289 . 64 ASP H H 8.820 0.030 1 290 . 64 ASP N N 119.910 0.050 1 291 . 64 ASP CA C 57.065 0.025 1 292 . 64 ASP CB C 39.085 0.025 1 293 . 64 ASP C C 179.730 0.070 1 294 . 65 ALA H H 8.250 0.030 1 295 . 65 ALA N N 124.610 0.050 1 296 . 65 ALA CA C 54.850 0.010 1 297 . 65 ALA CB C 19.030 0.080 1 298 . 65 ALA C C 180.520 0.050 1 299 . 66 LEU H H 8.400 0.030 1 300 . 66 LEU N N 119.480 0.050 1 301 . 66 LEU CA C 57.565 0.065 1 302 . 66 LEU CB C 40.290 0.040 1 303 . 66 LEU C C 178.565 0.035 1 304 . 67 THR H H 9.060 0.030 1 305 . 67 THR N N 118.340 0.050 1 306 . 67 THR CA C 66.580 0.030 1 307 . 67 THR CB C 68.025 0.015 1 308 . 67 THR C C 176.940 0.100 1 309 . 68 ASN H H 8.060 0.030 1 310 . 68 ASN N N 121.440 0.050 1 311 . 68 ASN CA C 56.005 0.015 1 312 . 68 ASN CB C 38.075 0.035 1 313 . 68 ASN C C 177.240 0.030 1 314 . 69 ALA H H 8.470 0.030 1 315 . 69 ALA N N 123.330 0.050 1 316 . 69 ALA CA C 55.405 0.065 1 317 . 69 ALA CB C 17.230 0.020 1 318 . 69 ALA C C 178.115 0.015 1 319 . 70 VAL H H 8.160 0.030 1 320 . 70 VAL N N 116.870 0.050 1 321 . 70 VAL CA C 66.295 0.035 1 322 . 70 VAL CB C 30.950 0.100 1 323 . 70 VAL C C 178.550 0.030 1 324 . 71 ALA H H 7.630 0.030 1 325 . 71 ALA N N 120.300 0.050 1 326 . 71 ALA CA C 53.555 0.055 1 327 . 71 ALA CB C 17.200 0.070 1 328 . 71 ALA C C 178.520 0.030 1 329 . 72 HIS H H 7.620 0.030 1 330 . 72 HIS N N 116.240 0.050 1 331 . 72 HIS CA C 54.500 0.000 1 332 . 72 HIS CB C 27.740 0.050 1 333 . 72 HIS C C 176.390 0.000 1 334 . 73 VAL H H 6.600 0.030 1 335 . 73 VAL N N 120.120 0.050 1 336 . 73 VAL CA C 64.675 0.015 1 337 . 73 VAL CB C 30.970 0.070 1 338 . 73 VAL C C 176.290 0.040 1 339 . 74 ASP H H 8.190 0.030 1 340 . 74 ASP N N 119.670 0.050 1 341 . 74 ASP CA C 54.770 0.000 1 342 . 74 ASP CB C 40.395 0.035 1 343 . 74 ASP C C 175.655 0.015 1 344 . 75 ASP H H 8.270 0.030 1 345 . 75 ASP N N 122.600 0.050 1 346 . 75 ASP CA C 52.540 0.020 1 347 . 75 ASP CB C 40.760 0.010 1 348 . 75 ASP C C 175.870 0.040 1 349 . 76 MET H H 8.600 0.030 1 350 . 76 MET N N 122.000 0.050 1 351 . 76 MET CA C 61.310 0.100 1 352 . 76 MET CB C 31.780 0.100 1 353 . 76 MET C C 174.960 0.100 1 354 . 77 PRO CA C 65.550 0.100 1 355 . 77 PRO C C 178.830 0.100 1 356 . 78 ASN H H 7.360 0.030 1 357 . 78 ASN N N 113.160 0.050 1 358 . 78 ASN CA C 55.160 0.000 1 359 . 78 ASN CB C 38.075 0.055 1 360 . 78 ASN C C 177.500 0.080 1 361 . 79 ALA H H 7.840 0.030 1 362 . 79 ALA N N 122.150 0.050 1 363 . 79 ALA CA C 54.245 0.005 1 364 . 79 ALA CB C 17.530 0.100 1 365 . 79 ALA C C 179.255 0.045 1 366 . 80 LEU H H 8.010 0.030 1 367 . 80 LEU N N 113.820 0.050 1 368 . 80 LEU CA C 53.310 0.020 1 369 . 80 LEU CB C 40.165 0.035 1 370 . 80 LEU C C 177.255 0.015 1 371 . 81 SER H H 7.030 0.030 1 372 . 81 SER N N 116.780 0.050 1 373 . 81 SER CA C 61.770 0.100 1 374 . 81 SER C C 175.860 0.100 1 375 . 82 ALA H H 8.550 0.030 1 376 . 82 ALA N N 122.360 0.050 1 377 . 82 ALA CA C 54.490 0.100 1 378 . 82 ALA C C 180.910 0.100 1 379 . 83 LEU H H 7.450 0.030 1 380 . 83 LEU N N 118.040 0.050 1 381 . 83 LEU CA C 55.540 0.020 1 382 . 83 LEU CB C 40.590 0.100 1 383 . 83 LEU C C 180.440 0.100 1 384 . 84 SER H H 8.170 0.030 1 385 . 84 SER N N 121.460 0.050 1 386 . 84 SER CA C 60.190 0.010 1 387 . 84 SER C C 175.800 0.100 1 388 . 85 ASP H H 7.510 0.030 1 389 . 85 ASP N N 121.710 0.050 1 390 . 85 ASP CA C 57.055 0.215 1 391 . 85 ASP C C 174.660 0.100 1 392 . 86 LEU H H 7.310 0.030 1 393 . 86 LEU N N 125.290 0.050 1 394 . 86 LEU CA C 57.015 0.045 1 395 . 86 LEU C C 177.140 0.100 1 396 . 87 HIS H H 7.120 0.030 1 397 . 87 HIS N N 112.120 0.050 1 398 . 87 HIS CA C 60.470 0.100 1 399 . 87 HIS C C 174.390 0.100 1 400 . 88 ALA CA C 52.770 0.100 1 401 . 88 ALA C C 177.970 0.100 1 402 . 89 HIS H H 7.140 0.030 1 403 . 89 HIS N N 115.100 0.050 1 404 . 89 HIS CA C 57.540 0.020 1 405 . 89 HIS CB C 30.250 0.100 1 406 . 89 HIS C C 176.050 0.020 1 407 . 90 LYS H H 7.320 0.030 1 408 . 90 LYS N N 117.260 0.050 1 409 . 90 LYS CA C 58.150 0.100 1 410 . 90 LYS CB C 31.320 0.100 1 411 . 90 LYS C C 178.380 0.100 1 412 . 91 LEU CA C 55.200 0.100 1 413 . 91 LEU C C 176.910 0.100 1 414 . 92 ARG H H 6.420 0.030 1 415 . 92 ARG N N 112.030 0.050 1 416 . 92 ARG CA C 56.550 0.010 1 417 . 92 ARG CB C 27.970 0.100 1 418 . 92 ARG C C 174.340 0.010 1 419 . 93 VAL H H 7.500 0.030 1 420 . 93 VAL N N 116.070 0.050 1 421 . 93 VAL CA C 62.870 0.010 1 422 . 93 VAL CB C 27.350 0.100 1 423 . 93 VAL C C 176.940 0.000 1 424 . 94 ASP H H 7.670 0.030 1 425 . 94 ASP N N 129.790 0.050 1 426 . 94 ASP CA C 52.240 0.100 1 427 . 95 PRO CA C 64.370 0.100 1 428 . 95 PRO C C 179.860 0.100 1 429 . 96 VAL H H 8.820 0.030 1 430 . 96 VAL N N 119.920 0.050 1 431 . 96 VAL CA C 65.355 0.015 1 432 . 96 VAL C C 178.660 0.050 1 433 . 97 ASN H H 8.260 0.030 1 434 . 97 ASN N N 116.530 0.050 1 435 . 97 ASN CA C 56.170 0.080 1 436 . 97 ASN CB C 39.700 0.100 1 437 . 97 ASN C C 177.680 0.040 1 438 . 98 PHE H H 7.800 0.030 1 439 . 98 PHE N N 118.590 0.050 1 440 . 98 PHE CA C 62.345 0.035 1 441 . 98 PHE CB C 36.590 0.100 1 442 . 98 PHE C C 179.520 0.050 1 443 . 99 LYS H H 7.390 0.030 1 444 . 99 LYS N N 121.140 0.050 1 445 . 99 LYS CA C 58.840 0.070 1 446 . 99 LYS CB C 30.770 0.100 1 447 . 99 LYS C C 179.815 0.065 1 448 . 100 LEU H H 7.260 0.030 1 449 . 100 LEU N N 119.620 0.050 1 450 . 100 LEU CA C 57.075 0.015 1 451 . 100 LEU CB C 38.085 0.135 1 452 . 100 LEU C C 179.360 0.030 1 453 . 101 LEU H H 8.110 0.030 1 454 . 101 LEU N N 120.870 0.050 1 455 . 101 LEU CA C 58.140 0.060 1 456 . 101 LEU CB C 39.930 0.100 1 457 . 101 LEU C C 178.910 0.050 1 458 . 102 SER H H 8.280 0.030 1 459 . 102 SER N N 114.970 0.050 1 460 . 102 SER CA C 63.335 0.045 1 461 . 102 SER C C 175.000 0.100 1 462 . 103 HIS H H 7.720 0.030 1 463 . 103 HIS N N 119.850 0.050 1 464 . 103 HIS CA C 59.385 0.045 1 465 . 103 HIS CB C 30.320 0.100 1 466 . 103 HIS C C 176.495 0.005 1 467 . 104 CYS H H 7.800 0.030 1 468 . 104 CYS N N 114.970 0.050 1 469 . 104 CYS CA C 65.285 0.025 1 470 . 104 CYS CB C 27.300 0.100 1 471 . 104 CYS C C 177.590 0.040 1 472 . 105 LEU H H 8.830 0.030 1 473 . 105 LEU N N 125.180 0.050 1 474 . 105 LEU CA C 58.020 0.100 1 475 . 105 LEU C C 177.440 0.100 1 476 . 106 LEU CA C 58.470 0.100 1 477 . 106 LEU C C 177.890 0.100 1 478 . 107 VAL H H 8.140 0.030 1 479 . 107 VAL N N 117.650 0.050 1 480 . 107 VAL CA C 66.205 0.025 1 481 . 107 VAL CB C 31.060 0.100 1 482 . 107 VAL C C 176.215 0.005 1 483 . 108 THR H H 7.090 0.030 1 484 . 108 THR N N 115.000 0.050 1 485 . 108 THR CA C 67.245 0.055 1 486 . 108 THR CB C 68.370 0.100 1 487 . 108 THR C C 175.940 0.100 1 488 . 109 LEU H H 7.950 0.030 1 489 . 109 LEU N N 120.510 0.050 1 490 . 109 LEU CA C 57.870 0.080 1 491 . 109 LEU CB C 39.890 0.100 1 492 . 109 LEU C C 177.550 0.100 1 493 . 110 ALA H H 7.800 0.030 1 494 . 110 ALA N N 121.870 0.050 1 495 . 110 ALA CA C 54.555 0.035 1 496 . 110 ALA CB C 17.120 0.100 1 497 . 110 ALA C C 177.995 0.025 1 498 . 111 ALA H H 7.360 0.030 1 499 . 111 ALA N N 113.540 0.050 1 500 . 111 ALA CA C 52.710 0.010 1 501 . 111 ALA CB C 16.785 0.095 1 502 . 111 ALA C C 179.555 0.025 1 503 . 112 HIS H H 7.160 0.030 1 504 . 112 HIS N N 112.490 0.050 1 505 . 112 HIS CA C 56.710 0.010 1 506 . 112 HIS CB C 30.230 0.020 1 507 . 112 HIS C C 174.760 0.010 1 508 . 113 LEU H H 8.140 0.030 1 509 . 113 LEU N N 121.270 0.050 1 510 . 113 LEU CA C 51.860 0.100 1 511 . 113 LEU C C 173.600 0.100 1 512 . 114 PRO CA C 65.160 0.100 1 513 . 114 PRO CB C 29.480 0.100 1 514 . 114 PRO C C 180.250 0.100 1 515 . 115 ALA H H 8.250 0.030 1 516 . 115 ALA N N 118.860 0.050 1 517 . 115 ALA CA C 53.770 0.000 1 518 . 115 ALA CB C 17.450 0.100 1 519 . 115 ALA C C 179.270 0.080 1 520 . 116 GLU H H 7.650 0.030 1 521 . 116 GLU N N 114.050 0.050 1 522 . 116 GLU CA C 56.145 0.035 1 523 . 116 GLU CB C 28.385 0.035 1 524 . 116 GLU C C 177.575 0.025 1 525 . 117 PHE H H 7.570 0.030 1 526 . 117 PHE N N 123.000 0.050 1 527 . 117 PHE CA C 57.085 0.045 1 528 . 117 PHE CB C 36.880 0.020 1 529 . 117 PHE C C 175.190 0.030 1 530 . 118 THR H H 7.820 0.030 1 531 . 118 THR N N 115.010 0.050 1 532 . 118 THR CA C 59.880 0.100 1 533 . 118 THR CB C 67.050 0.100 1 534 . 118 THR C C 173.360 0.100 1 535 . 119 PRO CA C 66.180 0.100 1 536 . 119 PRO CB C 30.690 0.100 1 537 . 119 PRO C C 176.600 0.100 1 538 . 120 ALA H H 8.280 0.030 1 539 . 120 ALA N N 116.230 0.050 1 540 . 120 ALA CA C 54.210 0.010 1 541 . 120 ALA CB C 17.700 0.030 1 542 . 120 ALA C C 180.275 0.055 1 543 . 121 VAL H H 7.210 0.030 1 544 . 121 VAL N N 120.100 0.050 1 545 . 121 VAL CA C 66.610 0.020 1 546 . 121 VAL CB C 30.760 0.100 1 547 . 121 VAL C C 176.985 0.015 1 548 . 122 HIS H H 8.360 0.030 1 549 . 122 HIS N N 121.830 0.050 1 550 . 122 HIS CA C 57.055 0.035 1 551 . 122 HIS CB C 31.715 0.005 1 552 . 122 HIS C C 177.390 0.100 1 553 . 123 ALA H H 7.880 0.030 1 554 . 123 ALA N N 120.310 0.050 1 555 . 123 ALA CA C 55.110 0.000 1 556 . 123 ALA CB C 17.200 0.100 1 557 . 123 ALA C C 179.645 0.015 1 558 . 124 SER H H 8.040 0.030 1 559 . 124 SER N N 115.620 0.050 1 560 . 124 SER CA C 62.485 0.015 1 561 . 124 SER C C 175.910 0.100 1 562 . 125 LEU H H 9.080 0.030 1 563 . 125 LEU N N 121.470 0.050 1 564 . 125 LEU CA C 57.605 0.045 1 565 . 125 LEU CB C 41.825 0.125 1 566 . 125 LEU C C 178.750 0.030 1 567 . 126 ASP H H 8.580 0.030 1 568 . 126 ASP N N 120.750 0.050 1 569 . 126 ASP CA C 58.390 0.060 1 570 . 126 ASP CB C 42.490 0.100 1 571 . 126 ASP C C 178.980 0.040 1 572 . 127 LYS H H 7.910 0.030 1 573 . 127 LYS N N 118.470 0.050 1 574 . 127 LYS CA C 59.230 0.080 1 575 . 127 LYS C C 180.245 0.085 1 576 . 128 PHE H H 8.810 0.030 1 577 . 128 PHE N N 122.290 0.050 1 578 . 128 PHE CA C 60.700 0.020 1 579 . 128 PHE CB C 39.340 0.100 1 580 . 128 PHE C C 176.590 0.020 1 581 . 129 LEU H H 8.920 0.030 1 582 . 129 LEU N N 121.110 0.050 1 583 . 129 LEU CA C 57.450 0.050 1 584 . 129 LEU CB C 38.860 0.100 1 585 . 129 LEU C C 180.350 0.110 1 586 . 130 ALA H H 8.500 0.030 1 587 . 130 ALA N N 125.530 0.050 1 588 . 130 ALA CA C 54.895 0.015 1 589 . 130 ALA CB C 16.950 0.100 1 590 . 130 ALA C C 180.465 0.055 1 591 . 131 SER H H 8.110 0.030 1 592 . 131 SER N N 118.400 0.050 1 593 . 131 SER CA C 62.270 0.000 1 594 . 131 SER C C 176.860 0.100 1 595 . 132 VAL H H 8.140 0.030 1 596 . 132 VAL N N 123.100 0.050 1 597 . 132 VAL CA C 66.195 0.035 1 598 . 132 VAL CB C 31.060 0.100 1 599 . 132 VAL C C 177.800 0.000 1 600 . 133 SER H H 8.130 0.030 1 601 . 133 SER N N 115.260 0.050 1 602 . 133 SER CA C 62.645 0.015 1 603 . 133 SER C C 175.690 0.100 1 604 . 134 THR H H 8.070 0.030 1 605 . 134 THR N N 119.820 0.050 1 606 . 134 THR CA C 66.105 0.025 1 607 . 134 THR CB C 67.900 0.100 1 608 . 134 THR C C 176.030 0.100 1 609 . 135 VAL H H 7.380 0.030 1 610 . 135 VAL N N 122.480 0.050 1 611 . 135 VAL CA C 66.200 0.100 1 612 . 135 VAL C C 178.550 0.100 1 613 . 136 LEU C C 175.270 0.100 1 614 . 137 THR H H 6.670 0.030 1 615 . 137 THR N N 102.520 0.050 1 616 . 137 THR CA C 59.970 0.000 1 617 . 137 THR C C 175.190 0.100 1 618 . 138 SER H H 7.110 0.030 1 619 . 138 SER N N 118.180 0.050 1 620 . 138 SER CA C 59.180 0.100 1 621 . 138 SER C C 180.660 0.100 1 stop_ save_ save_chemical_shift_2 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Sample_label $sample_one stop_ _Sample_conditions_label $sample_conditions _Chem_shift_reference_set_label $chemical_shift_reference _Mol_system_component_name 'globin subunit beta, one' _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 VAL CA C 58.330 0.100 1 2 . 2 HIS H H 7.550 0.030 1 3 . 2 HIS N N 118.530 0.050 1 4 . 2 HIS CA C 55.220 0.100 1 5 . 2 HIS C C 174.020 0.100 1 6 . 3 LEU H H 8.100 0.030 1 7 . 3 LEU N N 126.090 0.050 1 8 . 3 LEU CA C 53.020 0.020 1 9 . 3 LEU CB C 42.950 0.100 1 10 . 3 LEU C C 177.240 0.030 1 11 . 4 THR H H 9.140 0.030 1 12 . 4 THR N N 115.420 0.050 1 13 . 4 THR CA C 60.200 0.100 1 14 . 4 THR CB C 67.260 0.100 1 15 . 4 THR C C 173.320 0.100 1 16 . 5 PRO CA C 65.800 0.100 1 17 . 5 PRO CB C 30.720 0.100 1 18 . 5 PRO C C 179.630 0.100 1 19 . 6 GLU H H 8.590 0.030 1 20 . 6 GLU N N 117.560 0.050 1 21 . 6 GLU CA C 59.495 0.025 1 22 . 6 GLU CB C 28.135 0.095 1 23 . 6 GLU C C 179.900 0.040 1 24 . 7 GLU H H 7.680 0.030 1 25 . 7 GLU N N 121.740 0.050 1 26 . 7 GLU CA C 58.505 0.015 1 27 . 7 GLU CB C 30.475 0.025 1 28 . 7 GLU C C 178.355 0.025 1 29 . 8 LYS H H 8.710 0.030 1 30 . 8 LYS N N 119.170 0.050 1 31 . 8 LYS CA C 59.645 0.035 1 32 . 8 LYS CB C 31.145 0.055 1 33 . 8 LYS C C 179.400 0.010 1 34 . 9 SER H H 8.080 0.030 1 35 . 9 SER N N 115.200 0.050 1 36 . 9 SER CA C 61.120 0.010 1 37 . 9 SER CB C 62.025 0.055 1 38 . 9 SER C C 176.270 0.100 1 39 . 10 ALA H H 7.570 0.030 1 40 . 10 ALA N N 123.950 0.050 1 41 . 10 ALA CA C 54.495 0.025 1 42 . 10 ALA CB C 17.540 0.100 1 43 . 10 ALA C C 180.900 0.040 1 44 . 11 VAL H H 8.330 0.030 1 45 . 11 VAL N N 115.940 0.050 1 46 . 11 VAL CA C 65.365 0.005 1 47 . 11 VAL CB C 30.800 0.100 1 48 . 11 VAL C C 179.910 0.030 1 49 . 12 THR H H 8.300 0.030 1 50 . 12 THR N N 115.680 0.050 1 51 . 12 THR CA C 65.790 0.100 1 52 . 12 THR CB C 68.060 0.100 1 53 . 12 THR C C 176.940 0.100 1 54 . 13 ALA H H 8.170 0.030 1 55 . 13 ALA N N 125.790 0.050 1 56 . 13 ALA CA C 54.600 0.010 1 57 . 13 ALA CB C 17.245 0.045 1 58 . 13 ALA C C 180.495 0.055 1 59 . 14 LEU H H 7.140 0.030 1 60 . 14 LEU N N 117.210 0.050 1 61 . 14 LEU CA C 57.340 0.100 1 62 . 14 LEU CB C 40.400 0.100 1 63 . 14 LEU C C 178.900 0.010 1 64 . 15 TRP H H 8.060 0.030 1 65 . 15 TRP N N 119.190 0.050 1 66 . 15 TRP CA C 59.530 0.030 1 67 . 15 TRP C C 179.190 0.000 1 68 . 16 GLY H H 7.720 0.030 1 69 . 16 GLY N N 101.630 0.050 1 70 . 16 GLY CA C 45.750 0.000 1 71 . 16 GLY C C 174.730 0.010 1 72 . 17 LYS H H 7.640 0.030 1 73 . 17 LYS N N 118.380 0.050 1 74 . 17 LYS CA C 55.500 0.000 1 75 . 17 LYS CB C 32.600 0.010 1 76 . 17 LYS C C 176.820 0.100 1 77 . 18 VAL H H 7.150 0.030 1 78 . 18 VAL N N 121.770 0.050 1 79 . 18 VAL CA C 62.770 0.020 1 80 . 18 VAL CB C 31.260 0.010 1 81 . 18 VAL C C 175.250 0.000 1 82 . 19 ASN H H 8.270 0.030 1 83 . 19 ASN N N 124.850 0.050 1 84 . 19 ASN CA C 51.770 0.020 1 85 . 19 ASN CB C 36.360 0.020 1 86 . 19 ASN C C 176.070 0.000 1 87 . 20 VAL H H 8.070 0.030 1 88 . 20 VAL N N 124.210 0.050 1 89 . 20 VAL CA C 63.510 0.010 1 90 . 20 VAL CB C 30.295 0.045 1 91 . 20 VAL C C 176.840 0.010 1 92 . 21 ASP H H 7.850 0.030 1 93 . 21 ASP N N 119.270 0.050 1 94 . 21 ASP CA C 55.940 0.010 1 95 . 21 ASP CB C 40.605 0.025 1 96 . 21 ASP C C 177.425 0.045 1 97 . 22 GLU H H 7.120 0.030 1 98 . 22 GLU N N 117.370 0.050 1 99 . 22 GLU CA C 56.650 0.090 1 100 . 22 GLU CB C 31.825 0.015 1 101 . 22 GLU C C 177.990 0.100 1 102 . 23 VAL H H 7.680 0.030 1 103 . 23 VAL N N 118.270 0.050 1 104 . 23 VAL CA C 66.345 0.015 1 105 . 23 VAL C C 176.860 0.100 1 106 . 24 GLY H H 8.500 0.030 1 107 . 24 GLY N N 108.610 0.050 1 108 . 24 GLY CA C 46.825 0.015 1 109 . 24 GLY C C 175.795 0.025 1 110 . 25 GLY H H 7.380 0.030 1 111 . 25 GLY N N 108.930 0.050 1 112 . 25 GLY CA C 46.905 0.025 1 113 . 25 GLY C C 175.795 0.025 1 114 . 26 GLU H H 7.520 0.030 1 115 . 26 GLU N N 122.020 0.050 1 116 . 26 GLU CA C 58.460 0.010 1 117 . 26 GLU CB C 28.720 0.100 1 118 . 26 GLU C C 178.200 0.010 1 119 . 27 ALA H H 7.930 0.030 1 120 . 27 ALA N N 119.980 0.050 1 121 . 27 ALA CA C 54.110 0.020 1 122 . 27 ALA CB C 15.960 0.020 1 123 . 27 ALA C C 177.220 0.030 1 124 . 28 LEU H H 7.760 0.030 1 125 . 28 LEU N N 116.510 0.050 1 126 . 28 LEU CA C 56.260 0.010 1 127 . 28 LEU CB C 40.450 0.050 1 128 . 28 LEU C C 177.260 0.040 1 129 . 29 GLY H H 7.960 0.030 1 130 . 29 GLY N N 104.270 0.050 1 131 . 29 GLY CA C 46.835 0.005 1 132 . 29 GLY C C 174.860 0.000 1 133 . 30 ARG H H 7.790 0.030 1 134 . 30 ARG N N 117.090 0.050 1 135 . 30 ARG CA C 60.030 0.010 1 136 . 30 ARG CB C 29.120 0.100 1 137 . 30 ARG C C 177.610 0.030 1 138 . 31 LEU H H 7.660 0.030 1 139 . 31 LEU N N 121.110 0.050 1 140 . 31 LEU CA C 58.985 0.055 1 141 . 31 LEU C C 176.410 0.100 1 142 . 32 LEU H H 6.950 0.030 1 143 . 32 LEU N N 115.460 0.050 1 144 . 32 LEU CA C 56.325 0.015 1 145 . 32 LEU C C 178.250 0.100 1 146 . 33 VAL H H 7.390 0.030 1 147 . 33 VAL N N 116.360 0.050 1 148 . 33 VAL CA C 64.085 0.065 1 149 . 33 VAL C C 176.785 0.015 1 150 . 34 VAL H H 8.480 0.030 1 151 . 34 VAL N N 119.240 0.050 1 152 . 34 VAL CA C 64.560 0.060 1 153 . 34 VAL C C 175.070 0.000 1 154 . 35 TYR H H 7.380 0.030 1 155 . 35 TYR N N 117.750 0.050 1 156 . 35 TYR CA C 52.770 0.100 1 157 . 36 PRO CA C 65.190 0.100 1 158 . 36 PRO C C 178.550 0.100 1 159 . 37 TRP H H 7.000 0.030 1 160 . 37 TRP N N 117.270 0.050 1 161 . 37 TRP CA C 60.680 0.000 1 162 . 37 TRP C C 179.970 0.100 1 163 . 38 THR H H 8.120 0.030 1 164 . 38 THR N N 117.410 0.050 1 165 . 38 THR CA C 65.410 0.000 1 166 . 38 THR C C 176.570 0.100 1 167 . 39 GLN H H 7.640 0.030 1 168 . 39 GLN N N 118.050 0.050 1 169 . 39 GLN CA C 58.200 0.100 1 170 . 39 GLN CB C 27.700 0.000 1 171 . 39 GLN C C 178.750 0.000 1 172 . 40 ARG H H 7.670 0.030 1 173 . 40 ARG N N 118.450 0.050 1 174 . 40 ARG CA C 58.590 0.100 1 175 . 40 ARG C C 177.440 0.100 1 176 . 41 PHE H H 7.400 0.030 1 177 . 41 PHE N N 112.450 0.050 1 178 . 41 PHE CA C 59.760 0.010 1 179 . 41 PHE CB C 39.520 0.100 1 180 . 41 PHE C C 175.125 0.015 1 181 . 42 PHE H H 7.490 0.030 1 182 . 42 PHE N N 116.500 0.050 1 183 . 42 PHE CA C 56.675 0.025 1 184 . 42 PHE CB C 39.010 0.080 1 185 . 42 PHE C C 175.520 0.030 1 186 . 43 GLU H H 7.330 0.030 1 187 . 43 GLU N N 121.240 0.050 1 188 . 43 GLU CA C 59.090 0.100 1 189 . 43 GLU CB C 29.030 0.100 1 190 . 43 GLU C C 178.500 0.100 1 191 . 44 SER H H 8.680 0.030 1 192 . 44 SER N N 113.770 0.050 1 193 . 44 SER CA C 59.560 0.100 1 194 . 44 SER CB C 62.450 0.100 1 195 . 44 SER C C 175.780 0.100 1 196 . 45 PHE H H 8.470 0.030 1 197 . 45 PHE N N 122.270 0.050 1 198 . 45 PHE CA C 56.440 0.010 1 199 . 45 PHE CB C 35.890 0.010 1 200 . 45 PHE C C 175.685 0.025 1 201 . 46 GLY H H 7.660 0.030 1 202 . 46 GLY N N 108.230 0.050 1 203 . 46 GLY CA C 44.290 0.020 1 204 . 46 GLY C C 172.760 0.010 1 205 . 47 ASP H H 8.360 0.030 1 206 . 47 ASP N N 122.540 0.050 1 207 . 47 ASP CA C 55.120 0.010 1 208 . 47 ASP CB C 39.765 0.065 1 209 . 47 ASP C C 175.705 0.015 1 210 . 48 LEU H H 8.320 0.030 1 211 . 48 LEU N N 128.530 0.050 1 212 . 48 LEU CA C 52.190 0.010 1 213 . 48 LEU CB C 40.200 0.100 1 214 . 48 LEU C C 177.830 0.030 1 215 . 49 SER H H 8.100 0.030 1 216 . 49 SER N N 112.870 0.050 1 217 . 49 SER CA C 61.630 0.020 1 218 . 49 SER CB C 63.470 0.160 1 219 . 49 SER C C 175.090 0.020 1 220 . 50 THR H H 7.020 0.030 1 221 . 50 THR N N 111.610 0.050 1 222 . 50 THR CA C 57.840 0.100 1 223 . 50 THR CB C 69.970 0.100 1 224 . 50 THR C C 173.070 0.100 1 225 . 51 PRO CA C 65.200 0.100 1 226 . 51 PRO CB C 30.480 0.100 1 227 . 51 PRO C C 177.610 0.100 1 228 . 52 ASP H H 7.890 0.030 1 229 . 52 ASP N N 114.660 0.050 1 230 . 52 ASP CA C 56.580 0.000 1 231 . 52 ASP CB C 39.500 0.000 1 232 . 52 ASP C C 178.940 0.060 1 233 . 53 ALA H H 7.720 0.030 1 234 . 53 ALA N N 123.860 0.050 1 235 . 53 ALA CA C 54.120 0.010 1 236 . 53 ALA CB C 17.470 0.010 1 237 . 53 ALA C C 180.190 0.030 1 238 . 54 VAL H H 7.750 0.030 1 239 . 54 VAL N N 116.880 0.050 1 240 . 54 VAL CA C 66.315 0.015 1 241 . 54 VAL CB C 31.060 0.030 1 242 . 54 VAL C C 178.035 0.035 1 243 . 55 MET H H 7.830 0.030 1 244 . 55 MET N N 111.990 0.050 1 245 . 55 MET CA C 54.810 0.020 1 246 . 55 MET CB C 27.875 0.005 1 247 . 55 MET C C 178.425 0.015 1 248 . 56 GLY H H 7.310 0.030 1 249 . 56 GLY N N 103.510 0.050 1 250 . 56 GLY CA C 43.770 0.020 1 251 . 56 GLY C C 173.785 0.015 1 252 . 57 ASN H H 7.090 0.030 1 253 . 57 ASN N N 123.580 0.050 1 254 . 57 ASN CA C 51.340 0.100 1 255 . 57 ASN CB C 38.220 0.100 1 256 . 57 ASN C C 174.960 0.100 1 257 . 58 PRO CA C 64.430 0.100 1 258 . 58 PRO CB C 31.260 0.100 1 259 . 58 PRO C C 179.630 0.100 1 260 . 59 LYS H H 8.010 0.030 1 261 . 59 LYS N N 119.360 0.050 1 262 . 59 LYS CA C 58.610 0.020 1 263 . 59 LYS CB C 29.950 0.100 1 264 . 59 LYS C C 179.430 0.040 1 265 . 60 VAL H H 7.400 0.030 1 266 . 60 VAL N N 122.540 0.050 1 267 . 60 VAL CA C 65.695 0.005 1 268 . 60 VAL CB C 30.540 0.000 1 269 . 60 VAL C C 177.785 0.015 1 270 . 61 LYS H H 7.240 0.030 1 271 . 61 LYS N N 118.730 0.050 1 272 . 61 LYS CA C 59.725 0.025 1 273 . 61 LYS CB C 31.065 0.025 1 274 . 61 LYS C C 179.435 0.025 1 275 . 62 ALA H H 7.760 0.030 1 276 . 62 ALA N N 120.840 0.050 1 277 . 62 ALA CA C 54.400 0.000 1 278 . 62 ALA CB C 17.435 0.015 1 279 . 62 ALA C C 180.765 0.055 1 280 . 63 HIS H H 8.250 0.030 1 281 . 63 HIS N N 120.610 0.050 1 282 . 63 HIS CA C 59.370 0.030 1 283 . 63 HIS CB C 30.590 0.020 1 284 . 63 HIS C C 177.790 0.010 1 285 . 64 GLY H H 8.120 0.030 1 286 . 64 GLY N N 105.650 0.050 1 287 . 64 GLY CA C 45.460 0.010 1 288 . 64 GLY C C 174.850 0.100 1 289 . 65 LYS H H 6.990 0.030 1 290 . 65 LYS N N 120.930 0.050 1 291 . 65 LYS CA C 59.550 0.030 1 292 . 65 LYS CB C 31.310 0.100 1 293 . 65 LYS C C 179.660 0.000 1 294 . 66 LYS H H 6.860 0.030 1 295 . 66 LYS N N 120.260 0.050 1 296 . 66 LYS CA C 58.985 0.035 1 297 . 66 LYS CB C 30.730 0.100 1 298 . 66 LYS C C 180.035 0.095 1 299 . 67 VAL H H 7.220 0.030 1 300 . 67 VAL N N 121.160 0.050 1 301 . 67 VAL CA C 66.000 0.000 1 302 . 67 VAL CB C 29.810 0.100 1 303 . 67 VAL C C 178.220 0.000 1 304 . 68 LEU H H 8.110 0.030 1 305 . 68 LEU N N 119.680 0.050 1 306 . 68 LEU CA C 57.725 0.025 1 307 . 68 LEU CB C 40.235 0.035 1 308 . 68 LEU C C 179.750 0.030 1 309 . 69 GLY H H 8.260 0.030 1 310 . 69 GLY N N 107.850 0.050 1 311 . 69 GLY CA C 46.900 0.000 1 312 . 69 GLY C C 176.050 0.000 1 313 . 70 ALA H H 8.050 0.030 1 314 . 70 ALA N N 125.230 0.050 1 315 . 70 ALA CA C 54.780 0.010 1 316 . 70 ALA CB C 18.500 0.100 1 317 . 70 ALA C C 180.675 0.065 1 318 . 71 PHE H H 8.450 0.030 1 319 . 71 PHE N N 118.290 0.050 1 320 . 71 PHE CA C 64.135 0.045 1 321 . 71 PHE CB C 39.110 0.100 1 322 . 71 PHE C C 178.230 0.020 1 323 . 72 SER H H 9.090 0.030 1 324 . 72 SER N N 116.250 0.050 1 325 . 72 SER CA C 62.045 0.045 1 326 . 72 SER C C 177.070 0.100 1 327 . 73 ASP H H 8.200 0.030 1 328 . 73 ASP N N 123.840 0.050 1 329 . 73 ASP CA C 56.930 0.000 1 330 . 73 ASP CB C 39.650 0.000 1 331 . 73 ASP C C 179.280 0.070 1 332 . 74 GLY H H 8.470 0.030 1 333 . 74 GLY N N 108.290 0.050 1 334 . 74 GLY CA C 47.335 0.005 1 335 . 74 GLY C C 174.520 0.000 1 336 . 75 LEU H H 7.980 0.030 1 337 . 75 LEU N N 119.850 0.050 1 338 . 75 LEU CA C 57.115 0.035 1 339 . 75 LEU CB C 40.495 0.045 1 340 . 75 LEU C C 178.230 0.040 1 341 . 76 ALA H H 7.270 0.030 1 342 . 76 ALA N N 118.740 0.050 1 343 . 76 ALA CA C 52.110 0.020 1 344 . 76 ALA CB C 18.220 0.100 1 345 . 76 ALA C C 177.370 0.010 1 346 . 77 HIS H H 7.540 0.030 1 347 . 77 HIS N N 118.580 0.050 1 348 . 77 HIS CA C 54.020 0.020 1 349 . 77 HIS CB C 28.980 0.100 1 350 . 77 HIS C C 175.465 0.005 1 351 . 78 LEU H H 7.710 0.030 1 352 . 78 LEU N N 121.040 0.050 1 353 . 78 LEU CA C 57.565 0.025 1 354 . 78 LEU CB C 40.970 0.100 1 355 . 78 LEU C C 177.620 0.010 1 356 . 79 ASP H H 8.490 0.030 1 357 . 79 ASP N N 114.660 0.050 1 358 . 79 ASP CA C 53.665 0.015 1 359 . 79 ASP CB C 39.585 0.045 1 360 . 79 ASP C C 176.135 0.025 1 361 . 80 ASN H H 8.010 0.030 1 362 . 80 ASN N N 119.340 0.050 1 363 . 80 ASN CA C 51.470 0.100 1 364 . 80 ASN CB C 37.450 0.100 1 365 . 81 LEU H H 8.850 0.030 1 366 . 81 LEU N N 126.050 0.050 1 367 . 81 LEU CA C 57.940 0.010 1 368 . 81 LEU C C 179.050 0.100 1 369 . 82 LYS H H 8.600 0.030 1 370 . 82 LYS N N 118.690 0.050 1 371 . 82 LYS CA C 60.245 0.005 1 372 . 82 LYS CB C 30.480 0.100 1 373 . 82 LYS C C 178.790 0.010 1 374 . 83 GLY H H 7.440 0.030 1 375 . 83 GLY N N 104.110 0.050 1 376 . 83 GLY CA C 46.370 0.010 1 377 . 83 GLY C C 176.895 0.015 1 378 . 84 THR H H 7.500 0.030 1 379 . 84 THR N N 118.470 0.050 1 380 . 84 THR CA C 65.845 0.015 1 381 . 84 THR C C 175.720 0.100 1 382 . 85 PHE H H 7.630 0.030 1 383 . 85 PHE N N 115.850 0.050 1 384 . 85 PHE CA C 57.765 0.045 1 385 . 85 PHE CB C 37.650 0.100 1 386 . 85 PHE C C 174.880 0.000 1 387 . 86 ALA H H 7.020 0.030 1 388 . 86 ALA N N 125.020 0.050 1 389 . 86 ALA CA C 56.700 0.020 1 390 . 86 ALA CB C 17.530 0.100 1 391 . 86 ALA C C 180.050 0.000 1 392 . 87 THR H H 8.310 0.030 1 393 . 87 THR N N 114.460 0.050 1 394 . 87 THR CA C 65.600 0.020 1 395 . 87 THR C C 177.520 0.100 1 396 . 88 LEU H H 7.770 0.030 1 397 . 88 LEU N N 123.480 0.050 1 398 . 88 LEU CA C 56.180 0.000 1 399 . 88 LEU CB C 40.790 0.100 1 400 . 88 LEU C C 179.975 0.015 1 401 . 89 SER H H 8.900 0.030 1 402 . 89 SER N N 119.970 0.050 1 403 . 89 SER CA C 60.300 0.010 1 404 . 89 SER C C 176.610 0.100 1 405 . 90 GLU H H 7.460 0.030 1 406 . 90 GLU N N 120.170 0.050 1 407 . 90 GLU CA C 59.425 0.045 1 408 . 90 GLU CB C 28.100 0.100 1 409 . 90 GLU C C 178.060 0.010 1 410 . 91 LEU H H 7.140 0.030 1 411 . 91 LEU N N 117.450 0.050 1 412 . 91 LEU CA C 57.190 0.010 1 413 . 91 LEU C C 177.640 0.100 1 414 . 92 HIS H H 7.000 0.030 1 415 . 92 HIS N N 112.170 0.050 1 416 . 92 HIS CA C 59.935 0.035 1 417 . 92 HIS C C 174.070 0.000 1 418 . 93 CYS H H 7.810 0.030 1 419 . 93 CYS N N 115.000 0.050 1 420 . 93 CYS CA C 59.735 0.145 1 421 . 93 CYS C C 175.310 0.010 1 422 . 94 ASP H H 7.230 0.030 1 423 . 94 ASP N N 116.860 0.050 1 424 . 94 ASP CA C 56.020 0.000 1 425 . 94 ASP CB C 40.270 0.100 1 426 . 94 ASP C C 176.420 0.000 1 427 . 95 LYS H H 6.730 0.030 1 428 . 95 LYS N N 115.230 0.050 1 429 . 95 LYS CA C 56.875 0.035 1 430 . 95 LYS CB C 30.770 0.090 1 431 . 95 LYS C C 178.040 0.010 1 432 . 96 LEU H H 7.130 0.030 1 433 . 96 LEU N N 114.440 0.050 1 434 . 96 LEU CA C 54.690 0.010 1 435 . 96 LEU CB C 42.520 0.100 1 436 . 96 LEU C C 176.800 0.100 1 437 . 97 HIS H H 6.300 0.030 1 438 . 97 HIS N N 111.190 0.050 1 439 . 97 HIS CA C 55.760 0.010 1 440 . 97 HIS CB C 26.040 0.100 1 441 . 97 HIS C C 174.790 0.040 1 442 . 98 VAL H H 7.920 0.030 1 443 . 98 VAL N N 119.410 0.050 1 444 . 98 VAL CA C 62.020 0.110 1 445 . 98 VAL CB C 30.370 0.100 1 446 . 98 VAL C C 177.345 0.015 1 447 . 99 ASP H H 9.160 0.030 1 448 . 99 ASP N N 130.720 0.050 1 449 . 99 ASP CA C 53.740 0.100 1 450 . 99 ASP C C 177.220 0.100 1 451 . 100 PRO CA C 63.540 0.100 1 452 . 100 PRO C C 178.750 0.100 1 453 . 101 GLU H H 9.060 0.030 1 454 . 101 GLU N N 123.890 0.050 1 455 . 101 GLU CA C 58.825 0.015 1 456 . 101 GLU C C 179.785 0.015 1 457 . 102 ASN H H 8.120 0.030 1 458 . 102 ASN N N 112.380 0.050 1 459 . 102 ASN CA C 56.230 0.010 1 460 . 102 ASN CB C 39.900 0.100 1 461 . 102 ASN C C 177.810 0.040 1 462 . 103 PHE H H 7.550 0.030 1 463 . 103 PHE N N 118.150 0.050 1 464 . 103 PHE CA C 58.370 0.030 1 465 . 103 PHE C C 179.080 0.000 1 466 . 104 ARG H H 7.250 0.030 1 467 . 104 ARG N N 119.670 0.050 1 468 . 104 ARG CA C 58.660 0.100 1 469 . 104 ARG C C 177.890 0.100 1 470 . 105 LEU H H 7.870 0.030 1 471 . 105 LEU N N 118.580 0.050 1 472 . 105 LEU CA C 57.700 0.020 1 473 . 105 LEU CB C 39.500 0.100 1 474 . 105 LEU C C 179.330 0.100 1 475 . 106 LEU H H 8.180 0.030 1 476 . 106 LEU N N 118.370 0.050 1 477 . 106 LEU CA C 58.340 0.100 1 478 . 106 LEU CB C 39.400 0.100 1 479 . 106 LEU C C 178.585 0.055 1 480 . 107 GLY H H 8.070 0.030 1 481 . 107 GLY N N 105.480 0.050 1 482 . 107 GLY CA C 47.610 0.020 1 483 . 107 GLY C C 174.800 0.020 1 484 . 108 ASN H H 8.050 0.030 1 485 . 108 ASN N N 120.460 0.050 1 486 . 108 ASN CA C 54.790 0.020 1 487 . 108 ASN CB C 36.360 0.100 1 488 . 108 ASN C C 179.285 0.015 1 489 . 109 VAL H H 8.850 0.030 1 490 . 109 VAL N N 123.490 0.050 1 491 . 109 VAL CA C 67.495 0.015 1 492 . 109 VAL CB C 30.450 0.100 1 493 . 109 VAL C C 178.105 0.025 1 494 . 110 LEU H H 8.660 0.030 1 495 . 110 LEU N N 121.160 0.050 1 496 . 110 LEU CA C 58.320 0.010 1 497 . 110 LEU C C 179.190 0.100 1 498 . 111 VAL H H 7.880 0.030 1 499 . 111 VAL N N 118.610 0.050 1 500 . 111 VAL CA C 67.710 0.020 1 501 . 111 VAL CB C 30.500 0.100 1 502 . 111 VAL C C 176.840 0.040 1 503 . 112 CYS H H 7.980 0.030 1 504 . 112 CYS N N 117.340 0.050 1 505 . 112 CYS CA C 64.650 0.000 1 506 . 112 CYS C C 176.275 0.025 1 507 . 113 VAL H H 8.330 0.030 1 508 . 113 VAL N N 120.330 0.050 1 509 . 113 VAL CA C 66.020 0.100 1 510 . 113 VAL C C 177.675 0.015 1 511 . 114 LEU H H 8.300 0.030 1 512 . 114 LEU N N 121.110 0.050 1 513 . 114 LEU CA C 57.360 0.020 1 514 . 114 LEU C C 178.470 0.100 1 515 . 115 ALA H H 7.330 0.030 1 516 . 115 ALA N N 121.770 0.050 1 517 . 115 ALA CA C 54.485 0.035 1 518 . 115 ALA CB C 18.730 0.100 1 519 . 115 ALA C C 178.160 0.030 1 520 . 116 HIS H H 7.880 0.030 1 521 . 116 HIS N N 117.390 0.050 1 522 . 116 HIS CA C 57.405 0.025 1 523 . 116 HIS CB C 30.560 0.010 1 524 . 116 HIS C C 178.260 0.040 1 525 . 117 HIS H H 8.140 0.030 1 526 . 117 HIS N N 116.140 0.050 1 527 . 117 HIS CA C 58.620 0.010 1 528 . 117 HIS CB C 29.940 0.100 1 529 . 117 HIS C C 177.150 0.040 1 530 . 118 PHE H H 8.290 0.030 1 531 . 118 PHE N N 114.810 0.050 1 532 . 118 PHE CA C 58.905 0.025 1 533 . 118 PHE CB C 38.920 0.010 1 534 . 118 PHE C C 177.415 0.055 1 535 . 119 GLY H H 8.440 0.030 1 536 . 119 GLY N N 114.050 0.050 1 537 . 119 GLY CA C 47.380 0.020 1 538 . 119 GLY C C 176.120 0.010 1 539 . 120 LYS H H 8.620 0.030 1 540 . 120 LYS N N 125.240 0.050 1 541 . 120 LYS CA C 57.565 0.025 1 542 . 120 LYS CB C 30.925 0.025 1 543 . 120 LYS C C 177.910 0.030 1 544 . 121 GLU H H 7.680 0.030 1 545 . 121 GLU N N 116.850 0.050 1 546 . 121 GLU CA C 57.065 0.045 1 547 . 121 GLU CB C 29.430 0.010 1 548 . 121 GLU C C 177.190 0.060 1 549 . 122 PHE H H 8.450 0.030 1 550 . 122 PHE N N 126.340 0.050 1 551 . 122 PHE CA C 56.290 0.020 1 552 . 122 PHE CB C 36.880 0.050 1 553 . 122 PHE C C 174.400 0.010 1 554 . 123 THR H H 7.040 0.030 1 555 . 123 THR N N 113.520 0.050 1 556 . 123 THR CA C 60.250 0.100 1 557 . 123 THR CB C 66.700 0.100 1 558 . 123 THR C C 172.970 0.100 1 559 . 125 PRO CA C 65.480 0.100 1 560 . 125 PRO CB C 30.370 0.100 1 561 . 125 PRO C C 179.800 0.100 1 562 . 126 VAL H H 6.830 0.030 1 563 . 126 VAL N N 121.150 0.050 1 564 . 126 VAL CA C 66.120 0.000 1 565 . 126 VAL CB C 30.285 0.085 1 566 . 126 VAL C C 177.855 0.025 1 567 . 127 GLN H H 8.220 0.030 1 568 . 127 GLN N N 119.850 0.050 1 569 . 127 GLN CA C 58.605 0.025 1 570 . 127 GLN CB C 24.980 0.030 1 571 . 127 GLN C C 177.800 0.020 1 572 . 128 ALA H H 8.040 0.030 1 573 . 128 ALA N N 121.660 0.050 1 574 . 128 ALA CA C 55.095 0.015 1 575 . 128 ALA CB C 16.920 0.100 1 576 . 128 ALA C C 179.795 0.025 1 577 . 129 ALA H H 7.170 0.030 1 578 . 129 ALA N N 120.010 0.050 1 579 . 129 ALA CA C 54.780 0.010 1 580 . 129 ALA CB C 17.470 0.100 1 581 . 129 ALA C C 179.495 0.005 1 582 . 130 TYR H H 8.180 0.030 1 583 . 130 TYR N N 116.300 0.050 1 584 . 130 TYR CA C 64.305 0.105 1 585 . 130 TYR C C 179.360 0.100 1 586 . 131 GLN H H 9.420 0.030 1 587 . 131 GLN N N 119.160 0.050 1 588 . 131 GLN CA C 57.780 0.060 1 589 . 131 GLN CB C 24.970 0.210 1 590 . 131 GLN C C 179.630 0.030 1 591 . 132 LYS H H 7.500 0.030 1 592 . 132 LYS N N 121.110 0.050 1 593 . 132 LYS CA C 59.810 0.020 1 594 . 132 LYS CB C 31.670 0.100 1 595 . 132 LYS C C 179.755 0.045 1 596 . 133 VAL H H 7.470 0.030 1 597 . 133 VAL N N 119.320 0.050 1 598 . 133 VAL CA C 67.000 0.020 1 599 . 133 VAL C C 177.990 0.080 1 600 . 134 VAL H H 9.010 0.030 1 601 . 134 VAL N N 113.810 0.050 1 602 . 134 VAL CA C 66.225 0.035 1 603 . 134 VAL CB C 30.460 0.100 1 604 . 134 VAL C C 179.050 0.000 1 605 . 135 ALA H H 8.010 0.030 1 606 . 135 ALA N N 124.680 0.050 1 607 . 135 ALA CA C 54.665 0.035 1 608 . 135 ALA CB C 17.450 0.100 1 609 . 135 ALA C C 180.095 0.045 1 610 . 136 GLY H H 7.930 0.030 1 611 . 136 GLY N N 107.110 0.050 1 612 . 136 GLY CA C 46.640 0.010 1 613 . 136 GLY C C 177.150 0.010 1 614 . 137 VAL H H 8.580 0.030 1 615 . 137 VAL N N 124.370 0.050 1 616 . 137 VAL CA C 66.695 0.035 1 617 . 137 VAL C C 176.495 0.005 1 618 . 138 ALA H H 8.220 0.030 1 619 . 138 ALA N N 121.110 0.050 1 620 . 138 ALA CA C 55.440 0.010 1 621 . 138 ALA C C 179.195 0.025 1 622 . 139 ASN H H 8.160 0.030 1 623 . 139 ASN N N 114.960 0.050 1 624 . 139 ASN CA C 55.585 0.025 1 625 . 139 ASN C C 177.650 0.040 1 626 . 140 ALA H H 7.800 0.030 1 627 . 140 ALA N N 122.660 0.050 1 628 . 140 ALA CA C 54.155 0.045 1 629 . 140 ALA C C 180.395 0.045 1 630 . 141 LEU H H 8.030 0.030 1 631 . 141 LEU N N 120.520 0.050 1 632 . 141 LEU CA C 55.800 0.010 1 633 . 141 LEU C C 178.120 0.040 1 634 . 142 ALA H H 7.280 0.030 1 635 . 142 ALA N N 118.940 0.050 1 636 . 142 ALA CA C 51.710 0.130 1 637 . 142 ALA C C 177.670 0.040 1 638 . 143 HIS H H 7.050 0.030 1 639 . 143 HIS N N 118.400 0.050 1 640 . 143 HIS CA C 59.815 0.095 1 641 . 143 HIS CB C 25.770 0.100 1 642 . 143 HIS C C 176.965 0.005 1 643 . 144 LYS H H 7.040 0.030 1 644 . 144 LYS N N 115.620 0.050 1 645 . 144 LYS CA C 55.610 0.050 1 646 . 144 LYS C C 177.025 0.025 1 647 . 145 TYR H H 7.660 0.030 1 648 . 145 TYR N N 118.270 0.050 1 649 . 145 TYR CA C 58.355 0.045 1 650 . 145 TYR C C 175.910 0.030 1 651 . 146 HIS H H 7.410 0.030 1 652 . 146 HIS N N 124.460 0.050 1 653 . 146 HIS CA C 57.275 1.035 1 654 . 146 HIS C C 177.845 1.905 1 stop_ save_