data_5809 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; 1H Chemical Shift Assignments for the cyanomet complex of the isolated alpha-chain from human hemoglobin A ; _BMRB_accession_number 5809 _BMRB_flat_file_name bmr5809.str _Entry_type original _Submission_date 2003-05-22 _Accession_date 2003-05-23 _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 Tran Anh-Tuyet T. . 2 Kolczak Urszula . . 3 'La Mar' Gerd N. . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 4 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 784 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2003-09-28 original BMRB . stop_ _Original_release_date 2003-05-23 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; Solution 1H NMR Study of the Active Site Molecular Structure and Magnetic Properties of the Cyanomet Complex of the Isolated Alpha-chain from Human Hemoglobin A ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code 22802787 _PubMed_ID 12922170 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Tran Anh-Tuyet T. . 2 Kolczak Urszula . . 3 'La Mar' Gerd N. . stop_ _Journal_abbreviation 'Biochim. Biophys. Acta' _Journal_volume 1650 _Journal_issue 1-2 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 59 _Page_last 72 _Year 2003 _Details . loop_ _Keyword NMR a-chain 'dipolar shifts' hemoglobin 'magnetic axes' stop_ save_ ################################## # Molecular system description # ################################## save_system_Hb_A _Saveframe_category molecular_system _Mol_system_name 'human hemglobin A' _Abbreviation_common 'Hb A' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'hemoglobin A alpha subunit1' $Hb_A 'hemoglobin A alpha subunit2' $Hb_A 'CYANIDE GROUP' $entity_CYN 'PROTOPORPHYRIN IX CONTAINING FE' $HEM_ox stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state dimer _System_paramagnetic yes _System_thiol_state 'not reported' loop_ _Magnetic_equivalence_ID _Magnetically_equivalent_system_component 1 'hemoglobin A alpha subunit1' 1 'hemoglobin A alpha subunit2' stop_ loop_ _Biological_function ; oxygen carrier oxygen transport ; stop_ _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_Hb_A _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'Human hemoglobin A' _Abbreviation_common 'Hb A' _Molecular_mass . _Mol_thiol_state 'not reported' _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 2008-08-19 _Sequence_homology_query_revised_last_date 2008-08-19 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 1101 'hemoglobin A alpha chain' 100.00 141 100.00 100.00 3.46e-75 BMRB 25 'hemoglobin A alpha chain' 100.00 141 100.00 100.00 3.46e-75 BMRB 2707 'hemoglobin A alpha chain' 100.00 141 100.00 100.00 3.46e-75 BMRB 2709 'hemoglobin A alpha chain' 100.00 141 100.00 100.00 3.46e-75 BMRB 2868 'hemoglobin A alpha chain' 100.00 141 100.00 100.00 3.46e-75 BMRB 3442 'hemoglobin A alpha chain' 100.00 141 100.00 100.00 3.46e-75 BMRB 5856 'globin subunit alpha' 100.00 141 100.00 100.00 3.46e-75 BMRB 7125 'alpha chain' 100.00 141 100.00 100.00 3.46e-75 BMRB 907 'hemoglobin A alpha chain' 100.00 141 100.00 100.00 3.46e-75 PDB 1A00 'Hemoglobin (Val Beta1 Met, Trp Beta37 Tyr) Mutant' 100.00 141 100.00 100.00 3.46e-75 PDB 1A01 'Hemoglobin (Val Beta1 Met, Trp Beta37 Ala) Mutant' 100.00 141 100.00 100.00 3.46e-75 PDB 1A0U 'Hemoglobin (Val Beta1 Met) Mutant' 100.00 141 100.00 100.00 3.46e-75 PDB 1A0Z 'Hemoglobin (Val Beta1 Met) Mutant' 100.00 141 100.00 100.00 3.46e-75 PDB 1A3N 'Deoxy Human Hemoglobin' 100.00 141 100.00 100.00 3.46e-75 PDB 1A3O 'Artificial Mutant (Alpha Y42h) Of Deoxy Hemoglobin' 100.00 141 99.29 100.00 1.98e-74 PDB 1A9W 'Human Embryonic Gower Ii Carbonmonoxy Hemoglobin' 100.00 141 100.00 100.00 3.46e-75 PDB 1ABW 'Deoxy Rhb1.1 (Recombinant Hemoglobin)' 100.00 283 99.29 100.00 9.10e-75 PDB 1ABY 'Cyanomet Rhb1.1 (Recombinant Hemoglobin)' 100.00 283 99.29 100.00 9.10e-75 PDB 1AJ9 'R-State Human Carbonmonoxyhemoglobin Alpha-A53s' 100.00 141 99.29 100.00 6.96e-75 PDB 1B86 'Human Deoxyhaemoglobin-2,3-Diphosphoglycerate Complex' 100.00 141 100.00 100.00 3.46e-75 PDB 1BAB ; Hemoglobin Thionville: An Alpha-Chain Variant With A Substitution Of A Glutamate For Valine At Na-1 And Having An Acetylated Methionine Nh2 Terminus ; 99.29 142 100.00 100.00 9.64e-75 PDB 1BBB 'A Third Quaternary Structure Of Human Hemoglobin A At 1.7- Angstroms Resolution' 100.00 141 100.00 100.00 3.46e-75 PDB 1BIJ 'Crosslinked, Deoxy Human Hemoglobin A' 100.00 141 100.00 100.00 3.46e-75 PDB 1BUW 'Crystal Structure Of S-Nitroso-Nitrosyl Human Hemoglobin A' 100.00 141 100.00 100.00 3.46e-75 PDB 1BZ0 'Hemoglobin A (Human, Deoxy, High Salt)' 100.00 141 100.00 100.00 3.46e-75 PDB 1BZ1 'Hemoglobin (Alpha + Met) Variant' 100.00 142 100.00 100.00 3.43e-75 PDB 1BZZ 'Hemoglobin (Alpha V1m) Mutant' 100.00 141 99.29 100.00 7.57e-75 PDB 1C7B 'Deoxy Rhb1.0 (Recombinant Hemoglobin)' 100.00 141 99.29 100.00 7.57e-75 PDB 1C7C 'Deoxy Rhb1.1 (Recombinant Hemoglobin)' 100.00 283 99.29 100.00 9.10e-75 PDB 1C7D 'Deoxy Rhb1.2 (Recombinant Hemoglobin)' 100.00 284 99.29 100.00 9.97e-75 PDB 1CLS 'Cross-Linked Human Hemoglobin Deoxy' 100.00 141 100.00 100.00 3.46e-75 PDB 1CMY 'The Mutation Beta99 Asp-Tyr Stabilizes Y-A New, Composite Quaternary State Of Human Hemoglobin' 100.00 141 100.00 100.00 3.46e-75 PDB 1COH 'Structure Of Haemoglobin In The Deoxy Quaternary State With Ligand Bound At The Alpha Haems' 100.00 141 100.00 100.00 3.46e-75 PDB 1DKE 'Ni Beta Heme Human Hemoglobin' 100.00 141 100.00 100.00 3.46e-75 PDB 1DXT 'High-Resolution X-Ray Study Of Deoxy Recombinant Human Hemoglobins Synthesized From Beta-Globins Having Mutated Amino Termini' 100.00 141 100.00 100.00 3.46e-75 PDB 1DXU 'High-Resolution X-Ray Study Of Deoxy Recombinant Human Hemoglobins Synthesized From Beta-Globins Having Mutated Amino Termini' 100.00 141 100.00 100.00 3.46e-75 PDB 1DXV 'High-Resolution X-Ray Study Of Deoxy Recombinant Human Hemoglobins Synthesized From Beta-Globins Having Mutated Amino Termini' 100.00 141 100.00 100.00 3.46e-75 PDB 1FDH 'Structure Of Human Foetal Deoxyhaemoglobin' 100.00 141 100.00 100.00 3.46e-75 PDB 1FN3 'Crystal Structure Of Nickel Reconstituted Hemoglobin-A Case For Permanent, T-State Hemoglobin' 100.00 141 100.00 100.00 3.46e-75 PDB 1G9V 'High Resolution Crystal Structure Of Deoxy Hemoglobin Complexed With A Potent Allosteric Effector' 100.00 141 100.00 100.00 3.46e-75 PDB 1GBU 'Deoxy (Beta-(C93a,C112g)) Human Hemoglobin' 100.00 141 100.00 100.00 3.46e-75 PDB 1GBV '(Alpha-Oxy, Beta-(C112g)deoxy) T-State Human Hemoglobin' 100.00 141 100.00 100.00 3.46e-75 PDB 1GLI 'Deoxyhemoglobin T38w (Alpha Chains), V1g (Alpha And Beta Chains)' 100.00 141 98.58 99.29 5.33e-74 PDB 1GZX 'Oxy T State Haemoglobin: Oxygen Bound At All Four Haems' 100.00 141 100.00 100.00 3.46e-75 PDB 1HAB 'Crosslinked Haemoglobin' 100.00 141 100.00 100.00 3.46e-75 PDB 1HAC 'Crosslinked Haemoglobin' 100.00 141 100.00 100.00 3.46e-75 PDB 1HBA ; High-Resolution X-Ray Study Of Deoxyhemoglobin Rothschild 37beta Trp-> Arg: A Mutation That Creates An Intersubunit Chloride-Binding Site ; 100.00 141 100.00 100.00 3.46e-75 PDB 1HBB ; High-Resolution X-Ray Study Of Deoxyhemoglobin Rothschild 37beta Trp-> Arg: A Mutation That Creates An Intersubunit Chloride-Binding Site ; 100.00 141 100.00 100.00 3.46e-75 PDB 1HBS 'Refined Crystal Structure Of Deoxyhemoglobin S. I. Restrained Least-Squares Refinement At 3.0-Angstroms Resolution' 100.00 141 100.00 100.00 3.46e-75 PDB 1HCO 'The Structure Of Human Carbonmonoxy Haemoglobin At 2.7 Angstroms Resolution' 100.00 141 100.00 100.00 3.46e-75 PDB 1HDB ; Analysis Of The Crystal Structure, Molecular Modeling And Infrared Spectroscopy Of The Distal Beta-Heme Pocket Valine67(E11)-Threonine Mutation Of Hemoglobin ; 100.00 141 100.00 100.00 3.46e-75 PDB 1HGA ; High Resolution Crystal Structures And Comparisons Of T State Deoxyhaemoglobin And Two Liganded T-State Haemoglobins: T(Alpha-Oxy)haemoglobin And T(Met)haemoglobin ; 100.00 141 100.00 100.00 3.46e-75 PDB 1HGB ; High Resolution Crystal Structures And Comparisons Of T State Deoxyhaemoglobin And Two Liganded T-State Haemoglobins: T(Alpha-Oxy)haemoglobin And T(Met)haemoglobin ; 100.00 141 100.00 100.00 3.46e-75 PDB 1HGC ; High Resolution Crystal Structures And Comparisons Of T State Deoxyhaemoglobin And Two Liganded T-State Haemoglobins: T(Alpha-Oxy)haemoglobin And T(Met)haemoglobin ; 100.00 141 100.00 100.00 3.46e-75 PDB 1HHO 'Structure Of Human Oxyhaemoglobin At 2.1 Angstroms Resolution' 100.00 141 100.00 100.00 3.46e-75 PDB 1IRD 'Crystal Structure Of Human Carbonmonoxy-Haemoglobin At 1.25 A Resolution' 100.00 141 100.00 100.00 3.46e-75 PDB 1J3Y ; Direct Observation Of Photolysis-Induced Tertiary Structural Changes In Human Hemoglobin; Crystal Structure Of Alpha(Fe)-Beta(Ni) Hemoglobin (Laser Photolysed) ; 100.00 141 100.00 100.00 3.46e-75 PDB 1J3Z ; Direct Observation Of Photolysis-Induced Tertiary Structural Changes In Human Haemoglobin; Crystal Structure Of Alpha(Fe-Co)-Beta(Ni) Hemoglobin (Laser Unphotolysed) ; 100.00 141 100.00 100.00 3.46e-75 PDB 1J40 ; Direct Observation Of Photolysis-Induced Tertiary Structural Changes In Human Haemoglobin; Crystal Structure Of Alpha(Ni)-Beta(Fe-Co) Hemoglobin (Laser Unphotolysed) ; 100.00 141 100.00 100.00 3.46e-75 PDB 1J41 ; Direct Observation Of Photolysis-Induced Tertiary Structural Changes In Human Haemoglobin; Crystal Structure Of Alpha(Ni)-Beta(Fe) Hemoglobin (Laser Photolysed) ; 100.00 141 100.00 100.00 3.46e-75 PDB 1J7W 'Crystal Structure Of Deoxy Hbbetayq, A Site Directed Mutant Of Hba' 100.00 141 99.29 100.00 7.57e-75 PDB 1JY7 'The Structure Of Human Methemoglobin. The Variation Of A Theme' 100.00 141 100.00 100.00 3.46e-75 PDB 1K0Y ; X-Ray Crystallographic Analyses Of Symmetrical Allosteric Effectors Of Hemoglobin. Compounds Designed To Link Primary And Secondary Binding Sites ; 100.00 141 100.00 100.00 3.46e-75 PDB 1K1K 'Structure Of Mutant Human Carbonmonoxyhemoglobin C (Beta E6k) At 2.0 Angstrom Resolution In Phosphate Buffer.' 100.00 141 100.00 100.00 3.46e-75 PDB 1KD2 'Crystal Structure Of Human Deoxyhemoglobin In Absence Of Any Anions' 100.00 141 100.00 100.00 3.46e-75 PDB 1LFL 'Deoxy Hemoglobin (90% Relative Humidity)' 100.00 141 100.00 100.00 3.46e-75 PDB 1LFQ 'Oxy Hemoglobin (93% Relative Humidity)' 100.00 141 100.00 100.00 3.46e-75 PDB 1LFT 'Oxy Hemoglobin (90% Relative Humidity)' 100.00 141 100.00 100.00 3.46e-75 PDB 1LFV 'Oxy Hemoglobin (88% Relative Humidity)' 100.00 141 100.00 100.00 3.46e-75 PDB 1LFY 'Oxy Hemoglobin (84% Relative Humidity)' 100.00 141 100.00 100.00 3.46e-75 PDB 1LFZ 'Oxy Hemoglobin (25% Methanol)' 100.00 141 100.00 100.00 3.46e-75 PDB 1LJW 'Crystal Structure Of Human Carbonmonoxy Hemoglobin At 2.16 A: A Snapshot Of The Allosteric Transition' 100.00 141 100.00 100.00 3.46e-75 PDB 1M9P ; Crystalline Human Carbonmonoxy Hemoglobin C Exhibits The R2 Quaternary State At Neutral Ph In The Presence Of Polyethylene Glycol: The 2.1 Angstrom Resolution Crystal Structure ; 100.00 141 100.00 100.00 3.46e-75 PDB 1MKO 'A Fourth Quaternary Structure Of Human Hemoglobin A At 2.18 A Resolution' 100.00 141 100.00 100.00 3.46e-75 PDB 1NEJ ; Crystalline Human Carbonmonoxy Hemoglobin S (Liganded Sickle Cell Hemoglobin) Exhibits The R2 Quaternary State At Neutral Ph In The Presence Of Polyethylene Glycol: The 2.1 Angstrom Resolution Crystal Structure ; 100.00 141 100.00 100.00 3.46e-75 PDB 1NIH 'Structure Of Deoxy-Quaternary Haemoglobin With Liganded Beta Subunits' 100.00 141 100.00 100.00 3.46e-75 PDB 1NQP 'Crystal Structure Of Human Hemoglobin E At 1.73 A Resolution' 100.00 141 100.00 100.00 3.46e-75 PDB 1O1K 'Deoxy Hemoglobin (A,C:v1m; B,D:v1m,V67w)' 100.00 141 99.29 100.00 7.57e-75 PDB 1O1N 'Deoxy Hemoglobin (A-Glyglygly-C:v1m,L29w; B,D:v1m)' 100.00 285 98.58 99.29 4.48e-74 PDB 1O1O 'Deoxy Hemoglobin (A,C:v1m,V62l; B,D:v1m,V67l)' 100.00 141 98.58 100.00 1.85e-74 PDB 1O1P 'Deoxy Hemoglobin (A-Gly-C:v1m; B,D:v1m,C93a,N108k)' 100.00 283 99.29 100.00 9.10e-75 PDB 1QSH ; Magnesium(Ii)-And Zinc(Ii)-Protoporphyrin Ix's Stabilize The Lowest Oxygen Affinity State Of Human Hemoglobin Even More Strongly Than Deoxyheme ; 100.00 141 100.00 100.00 3.46e-75 PDB 1QSI ; Magnesium(Ii)-And Zinc(Ii)-Protoporphyrin Ix's Stabilize The Lowest Oxygen Affinity State Of Human Hemoglobin Even More Strongly Than Deoxyheme ; 100.00 141 100.00 100.00 3.46e-75 PDB 1QXD 'Structural Basis For The Potent Antisickling Effect Of A Novel Class Of 5-Membered Heterocyclic Aldehydic Compounds' 100.00 141 100.00 100.00 3.46e-75 PDB 1QXE 'Structural Basis For The Potent Antisickling Effect Of A Novel Class Of 5-Membered Heterocyclic Aldehydic Compounds' 100.00 141 100.00 100.00 3.46e-75 PDB 1R1X 'Crystal Structure Of Oxy-Human Hemoglobin Bassett At 2.15 Angstrom' 100.00 141 99.29 99.29 2.85e-74 PDB 1R1Y 'Crystal Structure Of Deoxy-Human Hemoglobin Bassett At 1.8 Angstrom' 100.00 141 99.29 99.29 2.85e-74 PDB 1RPS ; Crystallographic Analysis Of The Interaction Of Nitric Oxide With Quaternary-T Human Hemoglobin. Hemoglobin Exposed To No Under Anerobic Conditions ; 100.00 141 100.00 100.00 3.46e-75 PDB 1RQ3 'Crystallographic Analysis Of The Interaction Of Nitric Oxide With Quaternary-T Human Deoxyhemoglobin, Deoxyhemoglobin' 100.00 141 100.00 100.00 3.46e-75 PDB 1RQ4 ; Crystallographic Analysis Of The Interaction Of Nitric Oxide With Quaternary-T Human Hemoglobin, Hemoglobin Exposed To No Under Aerobic Conditions ; 100.00 141 100.00 100.00 3.46e-75 PDB 1RQA ; Crystallographic Analysis Of The Interaction Of Nitric Oxide With Quaternary-T Human Hemoglobin. Beta W73e Hemoglobin Exposed To No Under Anaerobic Conditions ; 100.00 141 100.00 100.00 3.46e-75 PDB 1RVW 'R State Human Hemoglobin [alpha V96w], Carbonmonoxy' 100.00 141 99.29 99.29 2.60e-74 PDB 1SDK 'Cross-Linked, Carbonmonoxy Hemoglobin A' 100.00 141 100.00 100.00 3.46e-75 PDB 1SDL 'Cross-Linked, Carbonmonoxy Hemoglobin A' 100.00 141 100.00 100.00 3.46e-75 PDB 1SHR 'Crystal Structure Of Ferrocyanide Bound Human Hemoglobin A2 At 1.88a Resolution' 100.00 141 100.00 100.00 3.46e-75 PDB 1SI4 'Crystal Structure Of Human Hemoglobin A2 (In R2 State) At 2.2 A Resolution' 100.00 141 100.00 100.00 3.46e-75 PDB 1THB 'Refinement Of A Partially Oxygenated T State Haemoglobin At 1.5 Angstroms Resolution' 100.00 141 100.00 100.00 3.46e-75 PDB 1UIW 'Crystal Structures Of Unliganded And Half-Liganded Human Hemoglobin Derivatives Cross-Linked Between Lys 82beta1 And Lys 82beta2' 100.00 141 100.00 100.00 3.46e-75 PDB 1VWT 'T State Human Hemoglobin [alpha V96w], Alpha Aquomet, Beta Deoxy' 100.00 141 99.29 99.29 2.60e-74 PDB 1XXT 'The T-To-T High Transitions In Human Hemoglobin: Wild-Type Deoxy Hb A (Low Salt, One Test Set)' 100.00 141 100.00 100.00 3.46e-75 PDB 1XY0 'T-To-Thigh Transitions In Human Hemoglobin: Alphak40g Deoxy Low-Salt' 100.00 141 98.58 99.29 3.85e-74 PDB 1XYE 'T-To-Thigh Transitions In Human Hemoglobin: Alpha Y42a Deoxy Low Salt' 100.00 141 98.58 99.29 8.65e-74 PDB 1XZ2 'Wild-Type Hemoglobin Deoxy No-Salt' 100.00 141 100.00 100.00 3.46e-75 PDB 1XZ4 ; Intersubunit Interactions Associated With Tyr42alpha Stabilize The Quaternary-T Tetramer But Are Not Major Quaternary Constraints In Deoxyhemoglobin: Alphay42a Deoxyhemoglobin No-Salt ; 100.00 141 98.58 99.29 8.65e-74 PDB 1XZ5 'T-To-Thigh Quaternary Transitions In Human Hemoglobin: Alphal91a Deoxy Low-Salt' 100.00 141 98.58 99.29 2.95e-74 PDB 1XZ7 'T-To-Thigh Quaternary Transitions In Human Hemoglobin: Alphar92a Deoxy Low-Salt' 100.00 141 98.58 99.29 6.05e-74 PDB 1XZU 'T-To-Thigh Quaternary Transitions In Human Hemoglobin: Alphad94g Deoxy Low-Salt' 100.00 141 98.58 99.29 4.91e-74 PDB 1XZV 'T-To-Thigh Quaternary Transitions In Human Hemoglobin: Alphap95a Deoxy Low-Salt' 100.00 141 98.58 99.29 5.80e-74 PDB 1Y01 'Crystal Structure Of Ahsp Bound To Fe(Ii) Alpha-Hemoglobin' 100.00 142 100.00 100.00 3.43e-75 PDB 1Y09 'T-To-T(High) Quaternary Transitions In Human Hemoglobin: Alphan97a Deoxy Low-Salt' 100.00 141 98.58 99.29 6.97e-74 PDB 1Y0A 'T-To-Thigh Quaternary Transitions In Human Hemoglobin: Alphay140a Deoxy Low-Salt' 100.00 141 98.58 99.29 8.65e-74 PDB 1Y0C 'T-To-Thigh Quaternary Transitions In Human Hemoglobin: Alphay140f Deoxy Low-Salt' 100.00 141 98.58 100.00 2.22e-74 PDB 1Y0D 'T-To-Thigh Quaternary Transitions In Human Hemoglobin: Desarg141alpha Deoxy Low-Salt' 99.29 140 100.00 100.00 2.08e-74 PDB 1Y0T 'T-To-T(High) Quaternary Transitions In Human Hemoglobin: Betav1m Deoxy Low-Salt (1 Test Set)' 100.00 141 100.00 100.00 3.46e-75 PDB 1Y0W 'T-To-Thigh Quaternary Transitions In Human Hemoglobin: Betav1m Deoxy Low-Salt (10 Test Sets)' 100.00 141 100.00 100.00 3.46e-75 PDB 1Y22 'T-To-T(High) Quaternary Transitions In Human Hemoglobin: Betav33a Deoxy Low-Salt (1 Test Set)' 100.00 141 100.00 100.00 3.46e-75 PDB 1Y2Z 'T-To-T(High) Quaternary Transitions In Human Hemoglobin: Betav34g Deoxy Low-Salt (1 Test Set)' 100.00 141 100.00 100.00 3.46e-75 PDB 1Y31 'T-To-T(High) Quaternary Transitions In Human Hemoglobin: Betay35a Deoxy Low-Salt (1 Test Set)' 100.00 141 100.00 100.00 3.46e-75 PDB 1Y35 'T-To-T(High) Quaternary Transitions In Human Hemoglobin: Betay35f Deoxy Low-Salt (1 Test Set)' 100.00 141 100.00 100.00 3.46e-75 PDB 1Y45 'T-To-T(High) Quaternary Transitions In Human Hemoglobin: Betap36a Deoxy Low-Salt (10 Test Sets)' 100.00 141 100.00 100.00 3.46e-75 PDB 1Y46 'T-To-T(High) Quaternary Transitions In Human Hemoglobin: Betaw37y Deoxy Low-Salt (10 Test Sets)' 100.00 141 100.00 100.00 3.46e-75 PDB 1Y4B 'T-To-T(High) Quaternary Transitions In Human Hemoglobin: Betaw37h Deoxy Low-Salt (10 Test Sets)' 100.00 141 100.00 100.00 3.46e-75 PDB 1Y4F 'T-To-T(High) Quaternary Transitions In Human Hemoglobin: Betaw37a Deoxy Low-Salt (10 Test Sets)' 100.00 141 100.00 100.00 3.46e-75 PDB 1Y4G 'T-To-T(High) Quaternary Transitions In Human Hemoglobin: Betaw37g Deoxy Low-Salt (10 Test Sets)' 100.00 141 100.00 100.00 3.46e-75 PDB 1Y4P 'T-To-T(High) Quaternary Transitions In Human Hemoglobin: Betaw37e Deoxy Low-Salt (10 Test Sets)' 100.00 141 100.00 100.00 3.46e-75 PDB 1Y4Q 'T-To-T(High) Quaternary Transitions In Human Hemoglobin: Betaf42a Deoxy Low-Salt (1 Test Set)' 100.00 141 100.00 100.00 3.46e-75 PDB 1Y4R 'T-To-T(High) Quaternary Transitions In Human Hemoglobin: Betaf45a Deoxy Low-Salt (1 Test Set)' 100.00 141 100.00 100.00 3.46e-75 PDB 1Y4V 'T-To-T(High) Quaternary Transitions In Human Hemoglobin: Betac93a Deoxy Low-Salt (1 Test Set)' 100.00 141 100.00 100.00 3.46e-75 PDB 1Y5F 'T-To-T(High) Quaternary Transitions In Human Hemoglobin: Betal96a Deoxy Low-Salt (1 Test Set)' 100.00 141 100.00 100.00 3.46e-75 PDB 1Y5J 'T-To-T(High) Quaternary Transitions In Human Hemoglobin: Betah97a Deoxy Low-Salt (1 Test Set)' 100.00 141 100.00 100.00 3.46e-75 PDB 1Y5K 'T-To-T(High) Quaternary Transitions In Human Hemoglobin: Betad99a Deoxy Low-Salt (10 Test Sets)' 100.00 141 100.00 100.00 3.46e-75 PDB 1Y7C 'T-To-T(High) Quaternary Transitions In Human Hemoglobin: Betap100a Deoxy Low-Salt (1 Test Set)' 100.00 141 100.00 100.00 3.46e-75 PDB 1Y7D 'T-To-T(High) Quaternary Transitions In Human Hemoglobin: Betap100g Deoxy Low-Salt (1 Test Set)' 100.00 141 100.00 100.00 3.46e-75 PDB 1Y7G 'T-To-T(High) Quaternary Transitions In Human Hemoglobin: Betan102a Deoxy Low-Salt (1 Test Set)' 100.00 141 100.00 100.00 3.46e-75 PDB 1Y7Z 'T-To-T(High) Quaternary Transitions In Human Hemoglobin: Betan108a Deoxy Low-Salt (1 Test Set)' 100.00 141 100.00 100.00 3.46e-75 PDB 1Y83 'T-To-T(High) Quaternary Transitions In Human Hemoglobin: Betay145g Deoxy Low-Salt (1 Test Set)' 100.00 141 100.00 100.00 3.46e-75 PDB 1Y85 'T-To-T(High) Quaternary Transitions In Human Hemoglobin: Deshis146beta Deoxy Low-Salt' 100.00 141 100.00 100.00 3.46e-75 PDB 1Y8W 'T-To-T(High) Quaternary Transitions In Human Hemoglobin: Alphar92a Oxy (2mm Ihp, 20% Peg) (10 Test Sets)' 100.00 141 98.58 99.29 6.05e-74 PDB 1YDZ 'T-To-T(High) Quaternary Transitions In Human Hemoglobin: Alphay140f Oxy (2mm Ihp, 20% Peg) (1 Test Set)' 100.00 141 98.58 100.00 2.22e-74 PDB 1YE0 'T-To-T(High) Quaternary Transitions In Human Hemoglobin: Betav33a Oxy (2mm Ihp, 20% Peg) (1 Test Set)' 100.00 141 100.00 100.00 3.46e-75 PDB 1YE1 'T-To-T(High) Quaternary Transitions In Human Hemoglobin: Betay35a Oxy (2mm Ihp, 20% Peg) (1 Test Set)' 100.00 141 100.00 100.00 3.46e-75 PDB 1YE2 'T-To-T(High) Quaternary Transitions In Human Hemoglobin: Betay35f Oxy (2mm Ihp, 20% Peg) (1 Test Set)' 100.00 141 100.00 100.00 3.46e-75 PDB 1YEN 'T-To-T(High) Quaternary Transitions In Human Hemoglobin: Betap36a Oxy (2mm Ihp, 20% Peg) (10 Test Sets)' 100.00 141 100.00 100.00 3.46e-75 PDB 1YEO 'T-To-T(High) Quaternary Transitions In Human Hemoglobin: Betaw37a Oxy (10 Test Sets)' 100.00 141 100.00 100.00 3.46e-75 PDB 1YEQ 'T-To-T(High) Quaternary Transitions In Human Hemoglobin: Betaw37y Oxy (10 Test Sets)' 100.00 141 100.00 100.00 3.46e-75 PDB 1YEU 'T-To-T(High) Quaternary Transitions In Human Hemoglobin: Betaw37g Oxy (10 Test Sets)' 100.00 141 100.00 100.00 3.46e-75 PDB 1YEV 'T-To-T(High) Quaternary Transitions In Human Hemoglobin: Betaw37e Oxy (10 Test Sets)' 100.00 141 100.00 100.00 3.46e-75 PDB 1YFF 'Structure Of Human Carbonmonoxyhemoglobin C (Beta E6k): Two Quaternary States (R2 And R3) In One Crystal' 100.00 141 100.00 100.00 3.46e-75 PDB 1YG5 'T-To-T(High) Quaternary Transitions In Human Hemoglobin: Betaw37h Oxy (2mm Ihp, 20% Peg) (10 Test Sets)' 100.00 141 100.00 100.00 3.46e-75 PDB 1YGD 'T-To-T(High) Quaternary Transitions In Human Hemoglobin: Betaw37e Alpha Zinc Beta Oxy (10 Test Sets)' 100.00 141 100.00 100.00 3.46e-75 PDB 1YGF 'T-To-T(High) Quaternary Transitions In Human Hemoglobin: Betah97a Oxy (2mm Ihp, 20% Peg) (1 Test Set)' 100.00 141 100.00 100.00 3.46e-75 PDB 1YH9 'T-To-T(High) Quaternary Transitions In Human Hemoglobin: Hba Oxy (2mm Ihp, 20% Peg) (10 Test Sets)' 100.00 141 100.00 100.00 3.46e-75 PDB 1YHE 'T-To-T(High) Quaternary Transitions In Human Hemoglobin: Hba Oxy (5.0mm Ihp, 20% Peg) (10 Test Sets)' 100.00 141 100.00 100.00 3.46e-75 PDB 1YHR 'T-To-T(High) Quaternary Transitions In Human Hemoglobin: Hba Oxy (10.0mm Ihp, 20% Peg) (10 Test Sets)' 100.00 141 100.00 100.00 3.46e-75 PDB 1YIE 'T-To-Thigh Quaternary Transitions In Human Hemoglobin: Betaw37a Oxy (2.2mm Ihp, 13% Peg) (1 Test Set)' 100.00 141 100.00 100.00 3.46e-75 PDB 1YIH 'T-To-T(High) Quaternary Transitions In Human Hemoglobin: Betap100a Oxy (2.2mm Ihp, 20% Peg) (1 Test Set)' 100.00 141 100.00 100.00 3.46e-75 PDB 1YVQ 'The Low Salt (Peg) Crystal Structure Of Co Hemoglobin E (Betae26k) Approaching Physiological Ph (Ph 7.5)' 100.00 141 100.00 100.00 3.46e-75 PDB 1YVT 'The High Salt (Phosphate) Crystal Structure Of Co Hemoglobin E (Glu26lys) At Physiological Ph (Ph 7.35)' 100.00 141 100.00 100.00 3.46e-75 PDB 1YZI 'A Novel Quaternary Structure Of Human Carbonmonoxy Hemoglobin' 100.00 141 100.00 100.00 3.46e-75 PDB 1Z8U 'Crystal Structure Of Oxidized Alpha Hemoglobin Bound To Ahsp' 100.00 142 100.00 100.00 3.43e-75 PDB 2D5Z 'Crystal Structure Of T-State Human Hemoglobin Complexed With Three L35 Molecules' 100.00 141 100.00 100.00 3.46e-75 PDB 2D60 'Crystal Structure Of Deoxy Human Hemoglobin Complexed With Two L35 Molecules' 100.00 141 100.00 100.00 3.46e-75 PDB 2DN1 '1.25a Resolution Crystal Structure Of Human Hemoglobin In The Oxy Form' 100.00 141 100.00 100.00 3.46e-75 PDB 2DN2 '1.25a Resolution Crystal Structure Of Human Hemoglobin In The Deoxy Form' 100.00 141 100.00 100.00 3.46e-75 PDB 2DN3 '1.25a Resolution Crystal Structure Of Human Hemoglobin In The Carbonmonoxy Form' 100.00 141 100.00 100.00 3.46e-75 PDB 2DXM 'Neutron Structure Analysis Of Deoxy Human Hemoglobin' 99.29 141 100.00 100.00 2.08e-74 PDB 2H35 'Solution Structure Of Human Normal Adult Hemoglobin' 99.29 141 100.00 100.00 2.08e-74 PDB 2HBC 'High Resolution X-Ray Structures Of Myoglobin-And Hemoglobin-Alkyl Isocyanide Complexes' 100.00 141 100.00 100.00 3.46e-75 PDB 2HBD 'High Resolution X-Ray Structures Of Myoglobin-And Hemoglobin-Alkyl Isocyanide Complexes' 100.00 141 100.00 100.00 3.46e-75 PDB 2HBE 'High Resolution X-Ray Structures Of Myoglobin-And Hemoglobin-Alkyl Isocyanide Complexes' 100.00 141 100.00 100.00 3.46e-75 PDB 2HBF 'High Resolution X-Ray Structures Of Myoglobin-And Hemoglobin-Alkyl Isocyanide Complexes' 100.00 141 100.00 100.00 3.46e-75 PDB 2HBS 'The High Resolution Crystal Structure Of Deoxyhemoglobin S' 100.00 141 100.00 100.00 3.46e-75 PDB 2HCO 'The Structure Of Human Carbonmonoxy Haemoglobin At 2.7 Angstroms Resolution' 100.00 141 100.00 100.00 3.46e-75 PDB 2HHB 'The Crystal Structure Of Human Deoxyhaemoglobin At 1.74 Angstroms Resolution' 100.00 141 100.00 100.00 3.46e-75 PDB 2HHD 'Oxygen Affinity Modulation By The N-Termini Of The Beta- Chains In Human And Bovine Hemoglobin' 100.00 141 100.00 100.00 3.46e-75 PDB 2HHE 'Oxygen Affinity Modulation By The N-Termini Of The Beta Chains In Human And Bovine Hemoglobin' 100.00 141 100.00 100.00 3.46e-75 PDB 2YRS 'Human Hemoglobin D Los Angeles: Crystal Structure' 100.00 141 100.00 100.00 3.46e-75 PDB 3D17 'A Triply Ligated Crystal Structure Of Relaxed State Human Hemoglobin' 100.00 141 100.00 100.00 3.46e-75 PDB 3HHB 'The Crystal Structure Of Human Deoxyhaemoglobin At 1.74 Angstroms Resolution' 100.00 141 100.00 100.00 3.46e-75 PDB 4HHB 'The Crystal Structure Of Human Deoxyhaemoglobin At 1.74 Angstroms Resolution' 100.00 141 100.00 100.00 3.46e-75 PDB 6HBW 'Crystal Structure Of Deoxy-Human Hemoglobin Beta6 Glu->trp' 100.00 141 100.00 100.00 3.46e-75 DBJ BAD97112 'alpha 2 globin variant [Homo sapiens]' 100.00 142 99.29 100.00 1.91e-74 EMBL CAA23748 'alpha globin [Homo sapiens]' 100.00 142 100.00 100.00 3.43e-75 EMBL CAA23750 'alpha 1 globin [Homo sapiens]' 100.00 141 100.00 100.00 3.46e-75 EMBL CAA23752 'hemoglobin alpha chain [Homo sapiens]' 100.00 142 100.00 100.00 3.43e-75 EMBL CAA23774 'alpha-2-globin [Homo sapiens]' 100.00 141 100.00 100.00 3.46e-75 EMBL CAA25044 'unnamed protein product [Pan troglodytes]' 100.00 142 100.00 100.00 3.43e-75 GenBank AAB59407 'hemoglobin alpha 2 [Homo sapiens]' 100.00 142 100.00 100.00 3.43e-75 GenBank AAB59408 'hemoglobin alpha 1 [Homo sapiens]' 100.00 142 100.00 100.00 3.43e-75 GenBank AAC72839 'alpha-2 globin [Homo sapiens]' 100.00 142 100.00 100.00 3.43e-75 GenBank AAC97373 'alpha one globin [Homo sapiens]' 100.00 142 100.00 100.00 3.43e-75 GenBank AAF72612 'alpha-2-globin [Homo sapiens]' 100.00 142 99.29 100.00 9.25e-75 PRF 0907233A 'hemoglobin alpha' 100.00 141 100.00 100.00 3.46e-75 PRF 610524A 'hemoglobin alpha' 100.00 141 99.29 100.00 1.05e-74 PRF 620479A 'hemoglobin alpha' 100.00 141 100.00 100.00 3.46e-75 REF NP_000508 'alpha 2 globin [Homo sapiens]' 100.00 142 100.00 100.00 3.43e-75 REF NP_000549 'alpha 1 globin [Homo sapiens]' 100.00 142 100.00 100.00 3.43e-75 REF NP_001036091 'alpha 1 globin [Pan troglodytes]' 100.00 142 100.00 100.00 3.43e-75 REF NP_001036092 'alpha 2 globin [Pan troglodytes]' 100.00 142 100.00 100.00 3.43e-75 SWISS-PROT P01923 'Hemoglobin subunit alpha (Hemoglobin alpha chain) (Alpha-globin)' 100.00 141 99.29 100.00 1.05e-74 SWISS-PROT P69905 'Hemoglobin subunit alpha (Hemoglobin alpha chain) (Alpha-globin)' 100.00 142 100.00 100.00 3.43e-75 SWISS-PROT P69906 'Hemoglobin subunit alpha (Hemoglobin alpha chain) (Alpha-globin)' 100.00 142 100.00 100.00 3.43e-75 SWISS-PROT P69907 'Hemoglobin subunit alpha (Hemoglobin alpha chain) (Alpha-globin)' 100.00 142 100.00 100.00 3.43e-75 SWISS-PROT Q9TS35 'Hemoglobin subunit alpha-1 (Hemoglobin alpha-1 chain) (Alpha-1-globin)' 100.00 142 98.58 99.29 9.65e-74 stop_ save_ ############# # Ligands # ############# save_CYN _Saveframe_category ligand _Mol_type "non-polymer (NON-POLYMER)" _Name_common 'CYANIDE ION' _BMRB_code CYN _PDB_code CYN _Molecular_mass 26.017 _Mol_charge -1 _Mol_paramagnetic . _Mol_aromatic no _Details . loop_ _Atom_name _PDB_atom_name _Atom_type _Atom_chirality _Atom_charge _Atom_oxidation_number _Atom_unpaired_electrons C C C . -1 . ? N N N . 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 TRIP C N ? ? stop_ _Mol_thiol_state . _Sequence_homology_query_date . save_ save_HEM_ox _Saveframe_category ligand _Mol_type non-polymer _Name_common 'PROTOPORPHYRIN IX CONTAINING FE' _Abbreviation_common heme _BMRB_code HEM_ox _PDB_code HEM _Molecular_mass . _Mol_charge . _Mol_paramagnetic yes _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 . 3+ 3+ ? 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 $Hb_A Human 9606 Eukaryota Metazoa Homo sapiens 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 $Hb_A 'purified from the natural source' . . . . . stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample1 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Concentration_min_value _Concentration_max_value _Isotopic_labeling $Hb_A 2 mM 1 3 . stop_ save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model Avance _Field_strength 500 _Details . save_ save_NMR_spectrometer_2 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model Avance _Field_strength 600 _Details . save_ save_NMR_spectrometer_3 _Saveframe_category NMR_spectrometer _Manufacturer GE _Model Omega _Field_strength 600 _Details . save_ ############################# # NMR applied experiments # ############################# save_WEFT_1 _Saveframe_category NMR_applied_experiment _Experiment_name WEFT _Sample_label . save_ save_1H_NOESY_2 _Saveframe_category NMR_applied_experiment _Experiment_name '1H NOESY' _Sample_label . save_ save_1H_WEFT-NOESY_3 _Saveframe_category NMR_applied_experiment _Experiment_name '1H WEFT-NOESY' _Sample_label . save_ save_1H_TOCSY_4 _Saveframe_category NMR_applied_experiment _Experiment_name '1H TOCSY' _Sample_label . save_ ####################### # Sample conditions # ####################### save_Ex-cond_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 5.4 0.2 n/a temperature 303 1 K stop_ save_ save_Ex-cond_2 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 8.4 0.2 n/a temperature 303 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 DSS H 1 'methyl protons' ppm 0.0 internal direct . . . 1.0 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_shift_set_1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Sample_label $sample1 stop_ _Sample_conditions_label $Ex-cond_1 _Chem_shift_reference_set_label $chemical_shift_reference _Mol_system_component_name 'hemoglobin A alpha subunit1' _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 . 20 HIS H H 7.77 0.01 1 2 . 20 HIS HA H 4.41 0.01 1 3 . 20 HIS HB2 H 2.55 0.01 2 4 . 20 HIS HB3 H 2.05 0.01 2 5 . 20 HIS HD2 H 7.32 0.01 1 6 . 20 HIS HE1 H 8.72 0.01 1 7 . 21 ALA H H 7.06 0.01 1 8 . 21 ALA HA H 3.19 0.01 1 9 . 21 ALA HB H 1.18 0.01 1 10 . 22 GLY H H 8.52 0.01 1 11 . 22 GLY HA2 H 3.7 0.01 1 12 . 22 GLY HA3 H 3.72 0.01 1 13 . 23 GLU H H 7.89 0.01 1 14 . 23 GLU HA H 4.22 0.01 1 15 . 24 TYR H H 8.02 0.01 1 16 . 25 GLY H H 8.95 0.01 1 17 . 25 GLY HA2 H 4.4 0.01 2 18 . 25 GLY HA3 H 4.42 0.01 2 19 . 26 ALA H H 8.4 0.01 1 20 . 26 ALA HA H 5 0.01 1 21 . 26 ALA HB H 2.1 0.01 1 22 . 27 GLU H H 8.82 0.01 1 23 . 28 ALA H H 8.95 0.01 1 24 . 28 ALA HA H 5.08 0.01 1 25 . 28 ALA HB H 1.95 0.01 1 26 . 29 LEU H H 9.01 0.01 1 27 . 29 LEU HA H 6.55 0.01 1 28 . 29 LEU HB2 H 3.3 0.01 1 29 . 29 LEU HB3 H 2.6 0.01 1 30 . 29 LEU HG H 5 0.01 1 31 . 29 LEU HD1 H 5.28 0.01 1 32 . 29 LEU HD2 H 6.55 0.01 1 33 . 30 GLU H H 8.55 0.01 1 34 . 31 ARG H H 8.66 0.01 1 35 . 31 ARG HA H 4.1 0.01 1 36 . 32 MET H H 8.75 0.01 1 37 . 33 PHE H H 8.98 0.01 1 38 . 33 PHE HA H 4.8 0.01 1 39 . 33 PHE HB2 H 3.3 0.01 1 40 . 33 PHE HB3 H 3.68 0.01 1 41 . 33 PHE HD1 H 8 0.01 1 42 . 33 PHE HE1 H 7.51 0.01 1 43 . 33 PHE HZ H 7.9 0.01 1 44 . 34 LEU H H 8.5 0.01 1 45 . 34 LEU HA H 4.38 0.01 1 46 . 35 SER H H 8.3 0.01 1 47 . 35 SER HA H 4.05 0.01 1 48 . 35 SER HB2 H 3.32 0.01 2 49 . 35 SER HB3 H 3.35 0.01 2 50 . 36 PHE H H 8.33 0.01 1 51 . 36 PHE HA H 4.08 0.01 1 52 . 36 PHE HB2 H 2.63 0.01 2 53 . 36 PHE HB3 H 2.75 0.01 2 54 . 36 PHE HD1 H 7.12 0.01 1 55 . 36 PHE HE1 H 6.82 0.01 1 56 . 36 PHE HZ H 7.16 0.01 1 57 . 37 PRO HA H 3.9 0.01 1 58 . 38 THR H H 7.88 0.01 1 59 . 38 THR HA H 3.7 0.01 1 60 . 38 THR HB H 3.9 0.01 1 61 . 38 THR HG2 H 1.38 0.01 1 62 . 39 THR H H 8.65 0.01 1 63 . 39 THR HA H 3.95 0.01 1 64 . 39 THR HB H 4.15 0.01 1 65 . 39 THR HG2 H 1.08 0.01 1 66 . 40 LYS H H 6.23 0.01 1 67 . 40 LYS HA H 3.9 0.01 1 68 . 41 THR H H 7.55 0.01 1 69 . 41 THR HA H 3.4 0.01 1 70 . 41 THR HB H 3.78 0.01 5 71 . 41 THR HG2 H 0.6 0.01 1 72 . 42 TYR H H 6.88 0.01 1 73 . 42 TYR HA H 3.45 0.01 1 74 . 42 TYR HB2 H 1.4 0.01 1 75 . 42 TYR HB3 H 1.95 0.01 1 76 . 42 TYR HD1 H 6.17 0.01 1 77 . 42 TYR HE2 H 5.96 0.01 1 78 . 42 TYR HH H 6.88 0.01 2 79 . 43 PHE H H 7.88 0.01 1 80 . 43 PHE HA H 4.15 0.01 1 81 . 43 PHE HB2 H 3.2 0.01 1 82 . 43 PHE HB3 H 2.75 0.01 1 83 . 43 PHE HD1 H 6.84 0.2 1 84 . 43 PHE HE2 H 8.92 0.2 1 85 . 43 PHE HZ H 13.96 0.3 1 86 . 44 PRO HA H 4.55 0.01 1 87 . 45 HIS H H 8.95 0.01 1 88 . 45 HIS HA H 4.88 0.01 1 89 . 45 HIS HB2 H 3.35 0.01 1 90 . 45 HIS HB3 H 3.1 0.01 1 91 . 45 HIS HD2 H 7.18 0.01 1 92 . 46 PHE H H 7.7 0.01 1 93 . 46 PHE HA H 4.55 0.01 2 94 . 46 PHE HB2 H 3.78 0.01 1 95 . 46 PHE HB3 H 2.53 0.01 1 96 . 46 PHE HD1 H 7 0.01 1 97 . 46 PHE HE2 H 7.4 0.01 1 98 . 46 PHE HZ H 7.2 0.01 1 99 . 47 ASP H H 8.4 0.01 1 100 . 47 ASP HA H 4.55 0.01 2 101 . 47 ASP HB2 H 3.06 0.01 2 102 . 48 LEU H H 8.72 0.01 1 103 . 48 LEU HA H 4.7 0.01 2 104 . 49 SER H H 8.6 0.01 1 105 . 49 SER HA H 5.3 0.01 1 106 . 49 SER HB2 H 4.02 0.01 2 107 . 49 SER HB3 H 4.4 0.01 2 108 . 50 HIS H H 8.8 0.01 1 109 . 50 HIS HA H 5.3 0.01 1 110 . 50 HIS HB2 H 3.51 0.01 2 111 . 50 HIS HB3 H 3.11 0.01 2 112 . 50 HIS HD2 H 7.5 0.01 1 113 . 51 GLY H H 8.6 0.01 1 114 . 51 GLY HA2 H 4.1 0.01 1 115 . 51 GLY HA3 H 3.75 0.01 1 116 . 52 SER H H 7.8 0.01 1 117 . 52 SER HB2 H 4.4 0.01 2 118 . 52 SER HB3 H 4.1 0.01 2 119 . 53 ALA H H 9.1 0.01 1 120 . 53 ALA HA H 4.1 0.01 1 121 . 53 ALA HB H 1.4 0.01 1 122 . 54 GLN H H 8.6 0.01 1 123 . 54 GLN HA H 4.15 0.01 1 124 . 55 VAL H H 8.25 0.01 1 125 . 55 VAL HA H 5.08 0.01 1 126 . 55 VAL HB H 2.75 0.01 1 127 . 55 VAL HG1 H 2.4 0.01 2 128 . 55 VAL HG2 H 1.93 0.01 2 129 . 56 LYS H H 8.3 0.01 1 130 . 57 GLY H H 8.67 0.01 1 131 . 58 HIS H H 8.69 0.01 1 132 . 58 HIS HA H 3.98 0.01 1 133 . 58 HIS HB2 H 4.35 0.01 1 134 . 58 HIS HB3 H 3.75 0.01 1 135 . 58 HIS HD2 H 12.79 0.3 1 136 . 58 HIS HE1 H 0.75 0.3 1 137 . 59 GLY H H 9.84 0.01 1 138 . 59 GLY HA2 H 4.32 0.01 1 139 . 59 GLY HA3 H 5 0.01 1 140 . 60 LYS H H 7.37 0.01 1 141 . 60 LYS HA H 3.85 0.01 1 142 . 60 LYS HB2 H 1.35 0.01 2 143 . 61 LYS H H 6.62 0.01 1 144 . 61 LYS HA H 3.01 0.01 1 145 . 61 LYS HB3 H -0.62 0.01 4 146 . 61 LYS HG2 H 0.34 0.01 4 147 . 61 LYS HG3 H 0.02 0.01 4 148 . 61 LYS HD2 H 0.45 0.01 4 149 . 61 LYS HE2 H 1.6 0.01 4 150 . 61 LYS HE3 H 0.8 0.01 4 151 . 62 VAL H H 6.97 0.01 2 152 . 62 VAL HA H -0.4 0.01 1 153 . 62 VAL HB H 2.07 0.01 1 154 . 62 VAL HG1 H 0.2 0.3 1 155 . 62 VAL HG2 H 1.18 0.3 1 156 . 63 ALA H H 7.75 0.01 1 157 . 63 ALA HA H 3.7 0.01 1 158 . 63 ALA HB H 1.48 0.01 1 159 . 64 ASP H H 8.12 0.01 1 160 . 64 ASP HA H 4.02 0.01 1 161 . 64 ASP HB2 H 2.1 0.01 2 162 . 65 ALA H H 6.72 0.01 1 163 . 65 ALA HA H 3.62 0.01 1 164 . 65 ALA HB H 0.02 0.01 1 165 . 66 LEU H H 7.23 0.01 1 166 . 66 LEU HA H 3.48 0.01 1 167 . 67 THR H H 8.61 0.01 1 168 . 67 THR HA H 3.5 0.01 1 169 . 67 THR HB H 4.15 0.01 1 170 . 67 THR HG2 H 1.4 0.01 1 171 . 68 ASN H H 7.9 0.01 1 172 . 68 ASN HA H 4.38 0.01 1 173 . 68 ASN HB2 H 2.89 0.01 2 174 . 68 ASN HB3 H 2.7 0.01 2 175 . 69 ALA H H 8.2 0.01 1 176 . 69 ALA HA H 3.8 0.01 1 177 . 69 ALA HB H 1.42 0.01 1 178 . 70 VAL H H 8.02 0.01 1 179 . 70 VAL HA H 3.01 0.01 1 180 . 70 VAL HB H 1.75 0.01 1 181 . 70 VAL HG1 H 0.6 0.01 2 182 . 70 VAL HG2 H -0.13 0.01 2 183 . 71 ALA H H 7.58 0.01 1 184 . 71 ALA HA H 3.98 0.01 1 185 . 71 ALA HB H 1.38 0.01 1 186 . 72 HIS H H 7.55 0.01 1 187 . 72 HIS HB2 H 2.65 0.01 2 188 . 72 HIS HB3 H 2.55 0.01 2 189 . 72 HIS HD2 H 7.45 0.01 1 190 . 73 VAL H H 6.66 0.01 1 191 . 73 VAL HA H 4.06 0.01 1 192 . 73 VAL HB H 2.43 0.01 1 193 . 73 VAL HG1 H 1.08 0.01 2 194 . 73 VAL HG2 H 0.95 0.01 2 195 . 74 ASP H H 8.26 0.01 1 196 . 74 ASP HB2 H 2.56 0.01 2 197 . 75 ASP H H 8.4 0.01 1 198 . 75 ASP HB2 H 2.7 0.01 2 199 . 76 MET H H 8.68 0.01 1 200 . 76 MET HA H 4.1 0.01 1 201 . 77 PRO HA H 4.11 0.01 2 202 . 78 ASN H H 7.5 0.01 1 203 . 78 ASN HB2 H 2.9 0.01 2 204 . 78 ASN HB3 H 2.81 0.01 2 205 . 79 ALA H H 8.04 0.01 1 206 . 79 ALA HA H 4.11 0.01 1 207 . 79 ALA HB H 1.2 0.01 1 208 . 80 LEU H H 8.21 0.01 1 209 . 80 LEU HA H 4.15 0.01 1 210 . 81 SER H H 7.6 0.01 1 211 . 81 SER HA H 5.08 0.01 1 212 . 81 SER HB2 H 4.3 0.01 2 213 . 81 SER HB3 H 4.15 0.01 2 214 . 82 ALA H H 8.97 0.01 1 215 . 82 ALA HA H 5.08 0.01 1 216 . 82 ALA HB H 1.95 0.01 1 217 . 83 LEU H H 8.97 0.01 1 218 . 83 LEU HA H 7.38 0.01 1 219 . 83 LEU HB2 H 8.02 0.01 1 220 . 83 LEU HB3 H 3.63 0.01 1 221 . 83 LEU HG H 2.67 0.01 1 222 . 83 LEU HD1 H 5.08 0.01 1 223 . 83 LEU HD2 H 1.23 0.01 1 224 . 84 SER H H 10.53 0.01 1 225 . 84 SER HA H 6.94 0.01 1 226 . 84 SER HB2 H 5.13 0.01 1 227 . 84 SER HB3 H 5.2 0.01 1 228 . 85 ASP H H 9.24 0.01 1 229 . 85 ASP HA H 5.4 0.01 1 230 . 85 ASP HB2 H 3.76 0.01 1 231 . 85 ASP HB3 H 3.76 0.01 1 232 . 86 LEU H H 9.96 0.01 1 233 . 86 LEU HA H 5.74 0.01 1 234 . 86 LEU HB2 H 6.18 0.01 1 235 . 86 LEU HB3 H 3.81 0.01 1 236 . 86 LEU HG H 5.07 0.01 1 237 . 86 LEU HD1 H 1.98 0.01 1 238 . 86 LEU HD2 H 1.65 0.01 1 239 . 87 HIS H H 13.08 0.1 1 240 . 87 HIS HA H 7.83 0.4 1 241 . 87 HIS HB2 H 9.9 0.3 1 242 . 87 HIS HB3 H 6.76 0.6 1 243 . 87 HIS HD2 H 17.1 0.4 1 244 . 87 HIS HE1 H -2.2 3 1 245 . 87 HIS HE2 H 21.1 0.3 1 246 . 88 ALA H H 10.96 0.01 1 247 . 88 ALA HA H 5.2 0.01 1 248 . 88 ALA HB H 1.94 0.01 1 249 . 89 HIS H H 8.74 0.01 1 250 . 89 HIS HA H 5.33 0.01 1 251 . 89 HIS HB2 H 4.05 0.01 2 252 . 89 HIS HB3 H 4.9 0.01 2 253 . 89 HIS HD2 H 7.69 0.01 1 254 . 90 LYS H H 8.4 0.01 1 255 . 90 LYS HA H 5.33 0.01 1 256 . 91 LEU H H 9.09 0.01 1 257 . 91 LEU HA H 4.07 0.01 1 258 . 91 LEU HB2 H 0.85 0.01 2 259 . 91 LEU HB3 H 1.76 0.01 2 260 . 91 LEU HG H 2.06 0.01 1 261 . 91 LEU HD1 H 0.34 0.01 1 262 . 91 LEU HD2 H 0.73 0.01 1 263 . 92 ARG H H 7 0.01 1 264 . 92 ARG HA H 4.03 0.01 1 265 . 93 VAL H H 7.6 0.01 1 266 . 93 VAL HA H 2.17 0.01 1 267 . 93 VAL HB H 0.04 0.01 1 268 . 93 VAL HG1 H -3.14 0.3 1 269 . 93 VAL HG2 H -3 0.3 1 270 . 94 ASP H H 6.55 0.01 1 271 . 94 ASP HA H 4.08 0.01 1 272 . 94 ASP HB2 H 1.98 0.01 2 273 . 94 ASP HB3 H 3.6 0.01 2 274 . 95 PRO HA H 3.35 0.01 1 275 . 96 VAL H H 8.2 0.01 1 276 . 96 VAL HA H 3.4 0.01 1 277 . 96 VAL HB H 1.7 0.01 1 278 . 96 VAL HG1 H 0.53 0.01 2 279 . 96 VAL HG2 H 0.4 0.01 2 280 . 97 ASN H H 7.12 0.01 1 281 . 97 ASN HA H 3.35 0.01 1 282 . 97 ASN HB2 H 0.5 0.01 2 283 . 97 ASN HB3 H 0.9 0.01 2 284 . 98 PHE H H 6.5 0.01 1 285 . 98 PHE HA H 1.94 0.01 1 286 . 98 PHE HB2 H 2.2 0.01 2 287 . 98 PHE HB3 H 2.1 0.01 2 288 . 98 PHE HD1 H 5.32 0.01 1 289 . 98 PHE HE1 H 4.4 0.01 1 290 . 98 PHE HZ H 6.5 0.01 1 291 . 99 LYS H H 7.35 0.01 1 292 . 99 LYS HA H 3.59 0.01 1 293 . 100 LEU H H 7.56 0.01 1 294 . 100 LEU HA H 3.75 0.01 1 295 . 101 LEU H H 7.6 0.01 1 296 . 101 LEU HA H 4.44 0.01 1 297 . 101 LEU HB2 H 1.4 0.01 2 298 . 101 LEU HB3 H 2.75 0.01 2 299 . 101 LEU HG H 1.71 0.01 1 300 . 101 LEU HD1 H 2.06 0.01 2 301 . 101 LEU HD2 H 2 0.01 2 302 . 102 SER H H 7.6 0.01 1 303 . 102 SER HA H 4.05 0.01 1 304 . 102 SER HB2 H 3.8 0.01 2 305 . 102 SER HB3 H 3.25 0.01 2 306 . 103 HIS H H 7.86 0.01 1 307 . 103 HIS HA H 4.2 0.01 1 308 . 103 HIS HB2 H 2.82 0.01 2 309 . 103 HIS HB3 H 2.4 0.01 2 310 . 103 HIS HD2 H 7.5 0.01 1 311 . 128 PHE H H 8.94 0.01 1 312 . 128 PHE HA H 3.7 0.01 1 313 . 128 PHE HB2 H 3.25 0.01 2 314 . 128 PHE HD1 H 6.85 0.01 1 315 . 128 PHE HE2 H 6.62 0.01 1 316 . 129 LEU H H 8.48 0.01 1 317 . 129 LEU HA H 3.98 0.01 1 318 . 130 ALA H H 7.9 0.01 1 319 . 130 ALA HA H 3.95 0.01 1 320 . 130 ALA HB H 1.35 0.01 1 321 . 131 SER H H 7.9 0.01 1 322 . 131 SER HA H 4.14 0.01 1 323 . 131 SER HB2 H 3.8 0.01 1 324 . 131 SER HB3 H 3.45 0.01 1 325 . 132 VAL H H 8.02 0.01 1 326 . 132 VAL HA H 3.18 0.01 1 327 . 132 VAL HB H 1.48 0.01 1 328 . 132 VAL HG1 H 0.04 0.01 1 329 . 132 VAL HG2 H 0.36 0.01 1 330 . 133 SER H H 7.15 0.01 1 331 . 133 SER HA H 3.9 0.01 1 332 . 133 SER HB2 H 3.6 0.01 2 333 . 133 SER HB3 H 3.13 0.01 2 334 . 134 THR H H 8.02 0.01 1 335 . 134 THR HA H 3.72 0.01 1 336 . 134 THR HB H 4.01 0.01 1 337 . 134 THR HG2 H 1.36 0.01 1 338 . 135 VAL H H 7.88 0.01 1 339 . 135 VAL HA H 4.14 0.01 1 340 . 135 VAL HB H 2.3 0.01 1 341 . 135 VAL HG1 H 1.51 0.01 2 342 . 135 VAL HG2 H 0.9 0.01 2 343 . 136 LEU H H 8.2 0.01 1 344 . 136 LEU HA H 5.08 0.01 1 345 . 136 LEU HB2 H 3.2 0.01 2 346 . 136 LEU HB3 H 0.9 0.01 2 347 . 136 LEU HG H 1.8 0.01 1 348 . 136 LEU HD1 H 0.25 0.01 1 349 . 136 LEU HD2 H 2.3 0.01 1 350 . 137 THR H H 8.75 0.01 1 351 . 137 THR HG2 H 1.2 0.01 1 352 . 138 SER H H 7.8 0.01 1 353 . 138 SER HA H 4.42 0.01 1 354 . 138 SER HB2 H 4.05 0.01 2 355 . 138 SER HB3 H 4 0.01 2 356 . 139 LYS H H 8.7 0.01 1 357 . 140 TYR H H 8.3 0.01 1 358 . 140 TYR HA H 4.33 0.01 1 359 . 140 TYR HB2 H 3.3 0.01 2 360 . 140 TYR HB3 H 2.95 0.01 2 361 . 140 TYR HD1 H 7.58 0.01 1 362 . 140 TYR HE2 H 7.33 0.01 1 stop_ loop_ _Atom_shift_assign_ID_ambiguity 145 '146,147,148,149,150' stop_ save_ save_shift_set_2 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Sample_label $sample1 stop_ _Sample_conditions_label $Ex-cond_1 _Chem_shift_reference_set_label $chemical_shift_reference _Mol_system_component_name 'PROTOPORPHYRIN IX CONTAINING FE' _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 HEM_ox 1HMB H 16.35 0.2 1 2 . 1 HEM_ox 2HMB H 16.35 0.2 1 3 . 1 HEM_ox 3HMB H 16.35 0.2 1 4 . 1 HEM_ox 1HMC H 8.12 0.2 1 5 . 1 HEM_ox 2HMC H 8.12 0.2 1 6 . 1 HEM_ox 3HMC H 8.12 0.2 1 7 . 1 HEM_ox 1HMD H 22.01 0.2 1 8 . 1 HEM_ox 2HMD H 22.01 0.2 1 9 . 1 HEM_ox 3HMD H 22.01 0.2 1 10 . 1 HEM_ox 1HMA H 8.99 0.2 1 11 . 1 HEM_ox 2HMA H 8.99 0.2 1 12 . 1 HEM_ox 3HMA H 8.99 0.2 1 13 . 1 HEM_ox HAB H 14.26 0.2 1 14 . 1 HEM_ox 1HBB H -3.04 0.2 1 15 . 1 HEM_ox 2HBB H -2.87 0.2 1 16 . 1 HEM_ox HAC H 7.29 0.2 1 17 . 1 HEM_ox 1HBC H -0.29 0.2 1 18 . 1 HEM_ox 2HBC H 0.71 0.2 1 19 . 1 HEM_ox 1HAD H 14.73 0.2 1 20 . 1 HEM_ox 2HAD H 9.55 0.2 1 21 . 1 HEM_ox 1HBD H 0.08 0.2 1 22 . 1 HEM_ox 2HBD H -1.67 0.2 1 23 . 1 HEM_ox 1HAA H 1.53 0.2 1 24 . 1 HEM_ox 2HAA H 3.02 0.2 1 25 . 1 HEM_ox 1HBA H -0.76 0.2 1 26 . 1 HEM_ox 2HBA H -0.87 0.2 1 27 . 1 HEM_ox HHC H 1.56 0.4 1 28 . 1 HEM_ox HHD H 3.46 0.4 1 29 . 1 HEM_ox HHA H 3.5 0.4 1 30 . 1 HEM_ox HHB H 1.85 0.4 1 stop_ save_ save_shift_set_3 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Sample_label $sample1 stop_ _Sample_conditions_label $Ex-cond_2 _Chem_shift_reference_set_label $chemical_shift_reference _Mol_system_component_name 'hemoglobin A alpha subunit1' _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 . 20 HIS H H 7.76 0.01 1 2 . 20 HIS HA H 4.4 0.01 1 3 . 20 HIS HB2 H 2.38 0.01 1 4 . 20 HIS HB3 H 2.12 0.01 1 5 . 20 HIS HD2 H 7.3 0.01 1 6 . 21 ALA H H 6.98 0.01 1 7 . 21 ALA HA H 3.2 0.01 1 8 . 22 GLY H H 8.58 0.01 1 9 . 22 GLY HA2 H 3.72 0.01 1 10 . 22 GLY HA3 H 3.8 0.01 1 11 . 23 GLU H H 8 0.01 1 12 . 23 GLU HA H 4.25 0.01 1 13 . 24 TYR H H 7.94 0.01 1 14 . 25 GLY H H 9.08 0.01 1 15 . 25 GLY HA2 H 4.11 0.01 2 16 . 25 GLY HA3 H 4.16 0.01 2 17 . 26 ALA H H 8.28 0.01 1 18 . 26 ALA HA H 4.98 0.01 1 19 . 26 ALA HB H 2.07 0.01 1 20 . 27 GLU H H 8.81 0.01 1 21 . 27 GLU HA H 4.16 0.01 1 22 . 28 ALA H H 9.08 0.01 1 23 . 28 ALA HA H 5.05 0.01 1 24 . 28 ALA HB H 2.03 0.01 1 25 . 29 LEU H H 9.08 0.01 1 26 . 29 LEU HA H 6.52 0.01 1 27 . 29 LEU HB2 H 3.48 0.01 1 28 . 29 LEU HB3 H 2.69 0.01 1 29 . 29 LEU HG H 4.75 0.01 1 30 . 29 LEU HD1 H 5.26 0.01 1 31 . 29 LEU HD2 H 6.52 0.01 1 32 . 30 GLU H H 8.58 0.01 1 33 . 31 ARG H H 8.7 0.01 1 34 . 31 ARG HA H 4.12 0.01 1 35 . 32 MET H H 8.95 0.01 1 36 . 33 PHE H H 8.85 0.01 1 37 . 33 PHE HA H 4.85 0.01 1 38 . 33 PHE HB2 H 3.32 0.01 1 39 . 33 PHE HB3 H 3.59 0.01 1 40 . 33 PHE HD1 H 7.99 0.01 1 41 . 33 PHE HE1 H 7.45 0.01 1 42 . 33 PHE HZ H 7.9 0.01 1 43 . 34 LEU H H 8.6 0.01 1 44 . 34 LEU HA H 4.32 0.01 1 45 . 35 SER H H 8.3 0.01 1 46 . 35 SER HA H 4.14 0.01 1 47 . 35 SER HB2 H 3.32 0.01 2 48 . 35 SER HB3 H 3.38 0.01 2 49 . 36 PHE H H 8.3 0.01 1 50 . 36 PHE HA H 4.08 0.01 1 51 . 36 PHE HB2 H 2.5 0.01 2 52 . 36 PHE HB3 H 2.88 0.01 2 53 . 36 PHE HD1 H 6.98 0.01 1 54 . 36 PHE HE1 H 6.75 0.01 1 55 . 36 PHE HZ H 6.63 0.01 1 56 . 37 PRO HA H 3.89 0.01 1 57 . 38 THR H H 7.85 0.01 1 58 . 38 THR HA H 3.9 0.01 1 59 . 38 THR HB H 3.92 0.01 1 60 . 38 THR HG2 H 1.4 0.01 1 61 . 39 THR H H 8.7 0.01 1 62 . 39 THR HA H 3.78 0.01 1 63 . 39 THR HB H 4.15 0.01 1 64 . 39 THR HG2 H 0.95 0.01 1 65 . 40 LYS H H 6.28 0.01 1 66 . 40 LYS HA H 3.95 0.01 1 67 . 41 THR H H 7.55 0.01 1 68 . 41 THR HA H 3.45 0.01 1 69 . 41 THR HG2 H 0.52 0.01 1 70 . 42 TYR H H 6.85 0.01 1 71 . 42 TYR HA H 3.48 0.01 1 72 . 42 TYR HB2 H 1.35 0.01 1 73 . 42 TYR HB3 H 2 0.01 1 74 . 42 TYR HD1 H 6.15 0.01 1 75 . 42 TYR HE2 H 5.94 0.01 1 76 . 42 TYR HH H 6.85 0.01 2 77 . 43 PHE H H 7.5 0.01 1 78 . 43 PHE HA H 4.12 0.01 1 79 . 43 PHE HB2 H 3.45 0.01 1 80 . 43 PHE HB3 H 2.77 0.01 1 81 . 43 PHE HD1 H 6.68 0.2 1 82 . 43 PHE HE2 H 8.83 0.2 1 83 . 43 PHE HZ H 14.02 0.4 1 84 . 44 PRO HA H 4.45 0.01 1 85 . 45 HIS H H 8.98 0.01 1 86 . 45 HIS HA H 4.98 0.01 1 87 . 45 HIS HB2 H 3.7 0.01 1 88 . 45 HIS HB3 H 3.25 0.01 1 89 . 45 HIS HD2 H 7 0.01 1 90 . 46 PHE H H 7.62 0.01 1 91 . 46 PHE HA H 4.32 0.01 1 92 . 46 PHE HB2 H 3.7 0.01 1 93 . 46 PHE HB3 H 2.45 0.01 1 94 . 46 PHE HD1 H 7.33 0.01 1 95 . 46 PHE HE2 H 7.21 0.01 1 96 . 46 PHE HZ H 6.85 0.01 1 97 . 47 ASP H H 8.25 0.01 1 98 . 47 ASP HA H 4.57 0.01 1 99 . 47 ASP HB2 H 3.18 0.01 2 100 . 48 LEU H H 8.72 0.01 1 101 . 48 LEU HA H 4.95 0.01 1 102 . 49 SER H H 8.65 0.01 1 103 . 49 SER HA H 5.21 0.01 1 104 . 49 SER HB2 H 4 0.01 2 105 . 49 SER HB3 H 3.75 0.01 2 106 . 50 HIS H H 9 0.01 1 107 . 50 HIS HA H 5 0.01 1 108 . 50 HIS HB2 H 3.61 0.01 2 109 . 50 HIS HB3 H 3.18 0.01 2 110 . 50 HIS HD2 H 7.45 0.01 1 111 . 51 GLY H H 8.65 0.01 1 112 . 51 GLY HA2 H 4.1 0.01 1 113 . 51 GLY HA3 H 3.75 0.01 1 114 . 52 SER H H 7.82 0.01 1 115 . 52 SER HB2 H 4.4 0.01 2 116 . 52 SER HB3 H 4.1 0.01 2 117 . 53 ALA H H 9.15 0.01 1 118 . 53 ALA HA H 4.08 0.01 1 119 . 53 ALA HB H 1.45 0.01 1 120 . 54 GLN H H 8.58 0.01 1 121 . 54 GLN HA H 4.15 0.01 1 122 . 55 VAL H H 8.25 0.01 1 123 . 55 VAL HA H 5.1 0.01 1 124 . 55 VAL HB H 2.8 0.01 1 125 . 55 VAL HG1 H 2.45 0.01 2 126 . 55 VAL HG2 H 1.9 0.01 2 127 . 56 LYS H H 8.3 0.01 1 128 . 57 GLY H H 8.6 0.01 1 129 . 58 HIS H H 8.63 0.01 1 130 . 58 HIS HA H 3.97 0.01 1 131 . 58 HIS HB2 H 4.35 0.01 1 132 . 58 HIS HB3 H 3.74 0.01 1 133 . 58 HIS HD2 H 12.79 0.01 1 134 . 58 HIS HE1 H 0.19 0.01 1 135 . 58 HIS HE2 H 16.29 0.01 1 136 . 59 GLY H H 9.72 0.01 1 137 . 59 GLY HA2 H 4.5 0.01 1 138 . 59 GLY HA3 H 4.98 0.01 1 139 . 60 LYS H H 7.34 0.01 1 140 . 60 LYS HA H 3.93 0.01 1 141 . 60 LYS HB2 H 1.35 0.01 2 142 . 61 LYS H H 6.58 0.01 1 143 . 61 LYS HA H 3.01 0.01 1 144 . 61 LYS HB3 H -0.62 0.01 4 145 . 61 LYS HG2 H 0.54 0.01 4 146 . 61 LYS HG3 H 0 0.01 4 147 . 61 LYS HD2 H 0.61 0.01 4 148 . 61 LYS HE2 H 1.22 0.01 4 149 . 61 LYS HE3 H 0.81 0.01 4 150 . 62 VAL H H 6.95 0.01 2 151 . 62 VAL HA H -0.35 0.01 1 152 . 62 VAL HB H 2.11 0.01 1 153 . 62 VAL HG1 H 0.34 0.3 1 154 . 62 VAL HG2 H 1.17 0.4 1 155 . 63 ALA H H 7.72 0.01 1 156 . 63 ALA HA H 3.74 0.01 1 157 . 63 ALA HB H 1.38 0.01 1 158 . 64 ASP H H 8.09 0.01 1 159 . 64 ASP HA H 4 0.01 1 160 . 64 ASP HB2 H 2.11 0.01 2 161 . 65 ALA H H 6.76 0.01 1 162 . 65 ALA HA H 3.62 0.01 1 163 . 65 ALA HB H 0 0.01 1 164 . 66 LEU H H 7.25 0.01 1 165 . 66 LEU HA H 3.49 0.01 1 166 . 67 THR H H 8.51 0.01 1 167 . 67 THR HA H 3.52 0.01 1 168 . 67 THR HB H 4.25 0.01 1 169 . 67 THR HG2 H 1.5 0.01 1 170 . 68 ASN H H 7.72 0.01 1 171 . 68 ASN HA H 4.4 0.01 1 172 . 68 ASN HB2 H 2.72 0.01 2 173 . 68 ASN HB3 H 2.61 0.01 2 174 . 69 ALA H H 8.1 0.01 1 175 . 69 ALA HA H 4 0.01 1 176 . 69 ALA HB H 1.38 0.01 1 177 . 70 VAL H H 8.02 0.01 1 178 . 70 VAL HA H 3.01 0.01 1 179 . 70 VAL HB H 1.72 0.01 1 180 . 70 VAL HG1 H 0.55 0.01 2 181 . 70 VAL HG2 H -0.2 0.01 2 182 . 71 ALA H H 7.8 0.01 1 183 . 71 ALA HA H 3.88 0.01 1 184 . 71 ALA HB H 1.23 0.01 1 185 . 72 HIS H H 7.58 0.01 1 186 . 72 HIS HB2 H 2.67 0.01 2 187 . 72 HIS HB3 H 2.56 0.01 2 188 . 72 HIS HD2 H 7.4 0.01 1 189 . 73 VAL H H 6.6 0.01 1 190 . 73 VAL HA H 4.06 0.01 1 191 . 73 VAL HB H 2.51 0.01 1 192 . 73 VAL HG1 H 1.08 0.01 2 193 . 73 VAL HG2 H 0.9 0.01 2 194 . 74 ASP H H 8.3 0.01 1 195 . 74 ASP HA H 4.6 0.01 1 196 . 74 ASP HB2 H 2.48 0.01 2 197 . 75 ASP H H 8.3 0.01 1 198 . 75 ASP HB2 H 2.5 0.01 2 199 . 76 MET H H 8.7 0.01 1 200 . 76 MET HA H 4.13 0.01 1 201 . 77 PRO HA H 3.95 0.01 1 202 . 78 ASN H H 7.45 0.01 1 203 . 78 ASN HA H 5.05 0.01 1 204 . 78 ASN HB2 H 2.9 0.01 2 205 . 78 ASN HB3 H 2.75 0.01 2 206 . 79 ALA H H 7.95 0.01 1 207 . 79 ALA HA H 4.11 0.01 1 208 . 79 ALA HB H 1.4 0.01 1 209 . 80 LEU H H 8.29 0.01 1 210 . 80 LEU HA H 4.06 0.01 1 211 . 81 SER H H 7.55 0.01 1 212 . 81 SER HA H 5.08 0.01 1 213 . 81 SER HB2 H 4.3 0.01 2 214 . 81 SER HB3 H 4.15 0.01 2 215 . 82 ALA H H 8.96 0.01 1 216 . 82 ALA HA H 5.06 0.01 1 217 . 82 ALA HB H 2.08 0.01 1 218 . 83 LEU H H 8.96 0.01 1 219 . 83 LEU HA H 7.46 0.01 1 220 . 83 LEU HB2 H 8.02 0.01 1 221 . 83 LEU HB3 H 3.52 0.01 1 222 . 83 LEU HG H 2.78 0.01 1 223 . 83 LEU HD1 H 5.1 0.01 1 224 . 83 LEU HD2 H 1.25 0.01 1 225 . 84 SER H H 10.53 0.01 1 226 . 84 SER HA H 7 0.01 1 227 . 84 SER HB2 H 5.12 0.01 1 228 . 84 SER HB3 H 5.31 0.01 1 229 . 85 ASP H H 9.3 0.01 1 230 . 85 ASP HA H 5.45 0.01 1 231 . 85 ASP HB2 H 3.75 0.01 1 232 . 85 ASP HB3 H 3.41 0.01 1 233 . 86 LEU H H 9.9 0.01 1 234 . 86 LEU HA H 5.82 0.01 1 235 . 86 LEU HB2 H 6.39 0.01 1 236 . 86 LEU HB3 H 3.89 0.01 1 237 . 86 LEU HG H 4.9 0.01 1 238 . 86 LEU HD1 H 2.58 0.01 1 239 . 86 LEU HD2 H 1.62 0.01 1 240 . 87 HIS H H 13.18 0.1 1 241 . 87 HIS HA H 7.87 0.4 1 242 . 87 HIS HB2 H 9.9 0.3 1 243 . 87 HIS HB3 H 6.66 0.6 1 244 . 87 HIS HD2 H -3 0.4 1 245 . 87 HIS HE1 H 18 3 1 246 . 87 HIS HD1 H 21.2 0.3 1 247 . 88 ALA H H 11.02 0.01 1 248 . 88 ALA HA H 5.1 0.01 1 249 . 88 ALA HB H 1.9 0.01 1 250 . 89 HIS H H 8.59 0.01 1 251 . 89 HIS HA H 5.2 0.01 1 252 . 89 HIS HB2 H 4.03 0.01 2 253 . 89 HIS HB3 H 4.9 0.01 2 254 . 89 HIS HD2 H 7.91 0.01 1 255 . 90 LYS H H 8.58 0.01 1 256 . 90 LYS HA H 5.2 0.01 1 257 . 91 LEU H H 9.07 0.01 1 258 . 91 LEU HA H 4.06 0.01 1 259 . 91 LEU HB2 H 0.88 0.01 2 260 . 91 LEU HB3 H 1.73 0.01 2 261 . 91 LEU HG H 2.26 0.01 1 262 . 91 LEU HD1 H 0.35 0.01 1 263 . 91 LEU HD2 H 0.8 0.01 1 264 . 92 ARG H H 6.91 0.01 1 265 . 92 ARG HA H 3.86 0.01 1 266 . 93 VAL H H 7.57 0.01 1 267 . 93 VAL HA H 2.15 0.01 1 268 . 93 VAL HB H 0.02 0.01 1 269 . 93 VAL HG1 H -3.14 0.3 1 270 . 93 VAL HG2 H -3.04 0.3 1 271 . 94 ASP H H 6.56 0.01 1 272 . 94 ASP HA H 4.05 0.01 1 273 . 94 ASP HB2 H 1.8 0.01 2 274 . 95 PRO HA H 3.38 0.01 1 275 . 96 VAL H H 8.15 0.01 1 276 . 96 VAL HA H 3.48 0.01 1 277 . 96 VAL HB H 1.83 0.01 1 278 . 96 VAL HG1 H 0.95 0.01 2 279 . 96 VAL HG2 H 0.75 0.01 2 280 . 97 ASN H H 7 0.01 1 281 . 97 ASN HA H 3.35 0.01 1 282 . 97 ASN HB2 H 0.5 0.01 2 283 . 97 ASN HB3 H 0.95 0.01 2 284 . 98 PHE H H 6.5 0.01 1 285 . 98 PHE HA H 1.92 0.01 1 286 . 98 PHE HB2 H 2.2 0.01 2 287 . 98 PHE HB3 H 2.1 0.01 2 288 . 98 PHE HD1 H 5.29 0.01 1 289 . 98 PHE HE1 H 4.26 0.01 1 290 . 99 LYS H H 7.4 0.01 1 291 . 99 LYS HA H 3.49 0.01 1 292 . 100 LEU H H 7.57 0.01 1 293 . 100 LEU HA H 3.75 0.01 1 294 . 101 LEU H H 7.62 0.01 1 295 . 101 LEU HA H 4.41 0.01 1 296 . 101 LEU HB2 H 1.4 0.01 2 297 . 101 LEU HB3 H 2.78 0.01 2 298 . 101 LEU HG H 1.78 0.01 1 299 . 101 LEU HD1 H 2.06 0.01 2 300 . 101 LEU HD2 H 1.95 0.01 2 301 . 102 SER H H 7.75 0.01 1 302 . 102 SER HA H 4.1 0.01 1 303 . 102 SER HB2 H 3.62 0.01 2 304 . 102 SER HB3 H 3.32 0.01 2 305 . 103 HIS H H 7.86 0.01 1 306 . 103 HIS HA H 4.12 0.01 1 307 . 103 HIS HB2 H 2.78 0.01 2 308 . 103 HIS HB3 H 2.4 0.01 2 309 . 103 HIS HD2 H 7.25 0.01 1 310 . 128 PHE H H 8.98 0.01 1 311 . 128 PHE HA H 3.64 0.01 1 312 . 128 PHE HB2 H 3.18 0.01 2 313 . 128 PHE HB3 H 2.77 0.01 2 314 . 128 PHE HD1 H 6.88 0.01 1 315 . 128 PHE HE2 H 6.57 0.01 1 316 . 129 LEU H H 8.52 0.01 1 317 . 129 LEU HA H 3.93 0.01 1 318 . 130 ALA H H 7.9 0.01 1 319 . 130 ALA HA H 3.95 0.01 1 320 . 131 SER H H 7.88 0.01 1 321 . 131 SER HA H 4.14 0.01 1 322 . 131 SER HB2 H 3.81 0.01 1 323 . 131 SER HB3 H 3.41 0.01 1 324 . 132 VAL H H 8.01 0.01 1 325 . 132 VAL HA H 3 0.01 1 326 . 132 VAL HB H 1.75 0.01 1 327 . 132 VAL HG1 H 0.04 0.01 1 328 . 132 VAL HG2 H 0.54 0.01 1 329 . 133 SER H H 7.2 0.01 1 330 . 133 SER HA H 3.92 0.01 1 331 . 133 SER HB2 H 3.55 0.01 2 332 . 133 SER HB3 H 3.15 0.01 2 333 . 134 THR H H 8.01 0.01 1 334 . 134 THR HA H 3.71 0.01 1 335 . 134 THR HB H 4.04 0.01 1 336 . 134 THR HG2 H 1.38 0.01 1 337 . 135 VAL H H 7.8 0.01 1 338 . 135 VAL HA H 4.21 0.01 1 339 . 135 VAL HB H 2.3 0.01 1 340 . 135 VAL HG1 H 1.45 0.01 2 341 . 135 VAL HG2 H 0.9 0.01 2 342 . 136 LEU H H 8.25 0.01 1 343 . 136 LEU HA H 5.05 0.01 1 344 . 136 LEU HB2 H 3.2 0.01 2 345 . 136 LEU HB3 H 0.91 0.01 2 346 . 136 LEU HG H 1.7 0.01 1 347 . 136 LEU HD1 H 0.35 0.01 1 348 . 136 LEU HD2 H 2.3 0.01 1 349 . 137 THR H H 8.73 0.01 1 350 . 137 THR HA H 4.98 0.01 1 351 . 137 THR HG2 H 1.16 0.01 1 352 . 138 SER H H 7.78 0.01 1 353 . 138 SER HA H 4.4 0.01 1 354 . 138 SER HB2 H 4.1 0.01 1 355 . 138 SER HB3 H 4.1 0.01 1 356 . 139 LYS H H 8.5 0.01 1 357 . 140 TYR H H 8.2 0.01 1 358 . 140 TYR HA H 4.33 0.01 1 359 . 140 TYR HB2 H 3.25 0.01 2 360 . 140 TYR HB3 H 2.85 0.01 2 361 . 140 TYR HD1 H 7.47 0.01 1 362 . 140 TYR HE2 H 7.03 0.01 1 stop_ loop_ _Atom_shift_assign_ID_ambiguity 144 '145,146,147,148,149' stop_ save_ save_shift_set_4 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Sample_label $sample1 stop_ _Sample_conditions_label $Ex-cond_1 _Chem_shift_reference_set_label $chemical_shift_reference _Mol_system_component_name 'PROTOPORPHYRIN IX CONTAINING FE' _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 HEM_ox 1HMB H 16.15 0.2 1 2 . 1 HEM_ox 2HMB H 16.15 0.2 1 3 . 1 HEM_ox 3HMB H 16.15 0.2 1 4 . 1 HEM_ox 1HMC H 8.17 0.2 1 5 . 1 HEM_ox 2HMC H 8.17 0.2 1 6 . 1 HEM_ox 3HMC H 8.17 0.2 1 7 . 1 HEM_ox 1HMD H 21.83 0.2 1 8 . 1 HEM_ox 2HMD H 21.83 0.2 1 9 . 1 HEM_ox 3HMD H 21.83 0.2 1 10 . 1 HEM_ox 1HMA H 8.75 0.2 1 11 . 1 HEM_ox 2HMA H 8.75 0.2 1 12 . 1 HEM_ox 3HMA H 8.75 0.2 1 13 . 1 HEM_ox HAB H 13.96 0.2 1 14 . 1 HEM_ox 1HBB H -3.18 0.2 1 15 . 1 HEM_ox 2HBB H -2.9 0.2 1 16 . 1 HEM_ox HAC H 7.3 0.2 1 17 . 1 HEM_ox 1HBC H -0.13 0.2 1 18 . 1 HEM_ox 2HBC H 0.84 0.2 1 19 . 1 HEM_ox 1HAD H 12.63 0.2 1 20 . 1 HEM_ox 2HAD H 11.29 0.2 1 21 . 1 HEM_ox 1HBD H -0.25 0.2 1 22 . 1 HEM_ox 2HBD H -1.93 0.2 1 23 . 1 HEM_ox 1HAA H 1.62 0.2 1 24 . 1 HEM_ox 2HAA H 2.65 0.2 1 25 . 1 HEM_ox 1HBA H -0.7 0.2 1 26 . 1 HEM_ox 2HBA H -0.62 0.2 1 27 . 1 HEM_ox HHC H 1.81 0.4 1 28 . 1 HEM_ox HHD H 3.48 0.4 1 29 . 1 HEM_ox HHA H 3.52 0.4 1 30 . 1 HEM_ox HHB H 1.66 0.4 1 stop_ save_