data_5784 #Corrected using PDB structure: 2GITE # #N.B. (Observed* = Observed shift + Offset correction) # #The average CS difference between predicted and observed: #HA CA CB CO N HN #-0.00 N/A N/A N/A N/A 0.06 # #bmr5784.str.corr chemical shifts have been re-referenced with the following #offsets (these values have been added to the original bmr5784.str file): #HA CA CB CO N HN #N/A N/A N/A N/A N/A N/A # #The 95% confidence intervals for the above recommended offsets are: # HA CA CB CO N HN #+/-0.03 N/A N/A N/A N/A +/-0.06 # #The Correlation Coefficients between predicted and observed #chemical shifts are: #HA CA CB CO N HN #0.906 N/A N/A N/A N/A 0.786 # #The RMSD between predicted and observed* (reference #corrected) chemical shifts are: #HA CA CB CO N HN #0.128 N/A N/A N/A N/A 0.253 # ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; 1H assignment of a human variant of beta2-microglobulin where His 31 was replaced by a Tyr ; loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Pettirossi Fabio . . 2 Corazza Alessandra . . 3 Viglino Paolo . . 4 Verdone Giuliana . . 5 Esposito Gennaro . . stop_ _BMRB_accession_number 5784 _BMRB_flat_file_name bmr5784.str _Entry_type new _Submission_date 2003-04-24 _Accession_date 2003-04-24 _Entry_origination author _NMR_STAR_version 2.1.1 _Experimental_method NMR loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count '1H chemical shifts' 461 stop_ loop_ _Related_BMRB_accession_number _Relationship 5169 "beta2-microglobulin with the first 3 residues" 5782 "DN3 beta2-microglobulin (without the first 3 residue)" 5783 "DN3 beta2-microglobulin (R3A mutant with the first 3 residue)" stop_ save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_title ; Properties of some variants of human beta2-microglobulin and amyloidogenesis ; _Citation_status published _Citation_type journal _MEDLINE_UI_code . _PubMed_ID 14660575 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Corazza Alessandra . . 2 Pettirossi Fabio . . 3 Viglino Paolo . . 4 Verdone Giuliana . . 5 Garcia Julian . . 6 Dumy Pascal . . 7 Giorgetti Sofia . . 8 Mangione Palma . . 9 Andreola Alessia . . 10 Stoppini Monica . . 11 Bellotti Vittorio . . 12 Esposito Gennaro . . stop_ _Journal_abbreviation "J. Biol. Chem." _Journal_volume ? _Journal_issue ? _Page_first ? _Page_last ? _Year ? loop_ _Keyword "beta2-microglobulin" "amyloidosis" stop_ save_ ################################## # Molecular system description # ################################## save_system_H31Yb2-m _Saveframe_category molecular_system _Mol_system_name "His31Tyrbeta2-microglobulin" _Abbreviation_common H31Yb2-m _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label "H31Ybeta2-microglobulin" $H31Ybeta2-m stop_ _System_physical_state native _System_oligomer_state monomer _System_paramagnetic no _System_thiol_state 'all disulfide bound' save_ ######################## # Monomeric polymers # ######################## save_H31Ybeta2-m _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common beta2-microglobulin _Name_variant H31Ybeta2-microglobulin _Abbreviation_common H31Ybeta2-m _Mol_thiol_state 'all disulfide bound' ############################## # Polymer residue sequence # ############################## _Residue_count 100 _Mol_residue_sequence ; MIQRTPKIQVYSRHPAENGK SNFLNCYVSGFYPSDIEVDL LKNGERIEKVEHSDLSFSKD WSFYLLYYTEFTPTEKDEYA CRVNHVTLSQPKIVKWDRDM ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 0 MET 2 1 ILE 3 2 GLN 4 3 ARG 5 4 THR 6 5 PRO 7 6 LYS 8 7 ILE 9 8 GLN 10 9 VAL 11 10 TYR 12 11 SER 13 12 ARG 14 13 HIS 15 14 PRO 16 15 ALA 17 16 GLU 18 17 ASN 19 18 GLY 20 19 LYS 21 20 SER 22 21 ASN 23 22 PHE 24 23 LEU 25 24 ASN 26 25 CYS 27 26 TYR 28 27 VAL 29 28 SER 30 29 GLY 31 30 PHE 32 31 TYR 33 32 PRO 34 33 SER 35 34 ASP 36 35 ILE 37 36 GLU 38 37 VAL 39 38 ASP 40 39 LEU 41 40 LEU 42 41 LYS 43 42 ASN 44 43 GLY 45 44 GLU 46 45 ARG 47 46 ILE 48 47 GLU 49 48 LYS 50 49 VAL 51 50 GLU 52 51 HIS 53 52 SER 54 53 ASP 55 54 LEU 56 55 SER 57 56 PHE 58 57 SER 59 58 LYS 60 59 ASP 61 60 TRP 62 61 SER 63 62 PHE 64 63 TYR 65 64 LEU 66 65 LEU 67 66 TYR 68 67 TYR 69 68 THR 70 69 GLU 71 70 PHE 72 71 THR 73 72 PRO 74 73 THR 75 74 GLU 76 75 LYS 77 76 ASP 78 77 GLU 79 78 TYR 80 79 ALA 81 80 CYS 82 81 ARG 83 82 VAL 84 83 ASN 85 84 HIS 86 85 VAL 87 86 THR 88 87 LEU 89 88 SER 90 89 GLN 91 90 PRO 92 91 LYS 93 92 ILE 94 93 VAL 95 94 LYS 96 95 TRP 97 96 ASP 98 97 ARG 99 98 ASP 100 99 MET stop_ _Sequence_homology_query_date 2004-07-29 _Sequence_homology_query_revised_last_date 2004-07-16 loop_ _Database_name _Database_accession_code _Database_entry_mol_name _Sequence_query_to_submitted_percentage _Sequence_subject_length _Sequence_identity _Sequence_positive _Sequence_homology_expectation_value PDB 1HLA "M Chain M, Human Class I HistocompatibilityAntigen A2 (HLA-A2, Human Leucocyte Antigen)" 103.09 97 99 100 1e-52 PDB 1A1M "B Chain B, Mhc Class I Molecule B5301 ComplexedWith Peptide Typdinqml From Gag Protein Of Hiv2" 101.01 99 99 100 8e-54 PDB 1A1N "B Chain B, Mhc Class I Molecule B3501 ComplexedWith Peptide Vplrpmty From The Nef Protein (75-82) OfHiv1" 101.01 99 99 100 8e-54 PDB 1A1O "B Chain B, Mhc Class I Molecule B5301 ComplexedWith Peptide Ls6 (Kpivqydnf) From The Malaria ParasiteP. Falciparum" 101.01 99 99 100 8e-54 PDB 1A6Z "B Chain B, Hfe (Human) Hemochromatosis Protein" 101.01 99 99 100 8e-54 PDB 1AGB "B Chain B, Antagonist Hiv-1 Gag Peptides InduceStructural Changes In Hla B8 - Hiv-1 Gag Peptide(Ggrkkykl - 3r Mutation)" 101.01 99 99 100 8e-54 PDB 1AGC "B Chain B, Antagonist Hiv-1 Gag Peptides InduceStructural Changes In Hla B8 - Hiv-1 Gag Peptide(Ggkkkyql - 7q Mutation)" 101.01 99 99 100 8e-54 PDB 1AGD "B Chain B, Antagonist Hiv-1 Gag Peptides InduceStructural Changes In Hla B8 - Hiv-1 Gag Peptide(Ggkkkykl - Index Peptide)" 101.01 99 99 100 8e-54 PDB 1AGE "B Chain B, Antagonist Hiv-1 Gag Peptides InduceStructural Changes In Hla B8 - Hiv-1 Gag Peptide(Ggkkkyrl - 7r Mutation)" 101.01 99 99 100 8e-54 PDB 1AGF "B Chain B, Antagonist Hiv-1 Gag Peptides InduceStructural Changes In Hla B8 - Hiv-1 Gag Peptide(Ggkkrykl - 5r Mutation)" 101.01 99 99 100 8e-54 PDB 1AKJ "B Chain B, Complex Of The Human Mhc Class IGlycoprotein Hla-A2 And The T Cell Coreceptor Cd8" 101.01 99 99 100 8e-54 PDB 1C16 "B Chain B, Crystal Structure Analysis Of TheGammaDELTA T CELL LIGAND T22" 101.01 99 99 100 8e-54 PDB 1DE4 "B Chain B, Hemochromatosis Protein HfeComplexed With Transferrin Receptor" 101.01 99 99 100 8e-54 PDB 1E27 "B Chain B, Nonstandard Peptide Binding OfHla-B5101 Complexed With Hiv Immunodominant EpitopeKm1(Lppvvakei)" 101.01 99 99 100 8e-54 PDB 1E28 "B Chain B, Nonstandard Peptide Binding OfHla-B5101 Complexed With Hiv Immunodominant EpitopeKm2(Taftipsi)" 101.01 99 99 100 8e-54 PDB 1EXU "B Chain B, Crystal Structure Of The HumanMhc-Related Fc Receptor" 101.01 99 99 100 8e-54 PDB 1HSA "B Chain B, Human Class I HistocompatibilityAntigen HLA-B(Asterisk)2705" 101.01 99 99 100 8e-54 PDB 1HSB "B Chain B, Class I Histocompatibility AntigenAw68.1 (Leucocyte Antigen)" 101.01 99 99 100 8e-54 PDB 1M05 "B Chain B, Hla B8 In Complex With An EpsteinBarr Virus Determinant" 101.01 99 99 100 8e-54 PDB 1M6O "B Chain B, Crystal Structure Of Hla B4402 InComplex With Hla Dpa0201 Peptide" 101.01 99 99 100 8e-54 PDB 1MI5 "B Chain B, The Crystal Structure Of Lc13 TcrIn Complex With Hlab8-Ebv Peptide Complex" 101.01 99 99 100 8e-54 PDB 1N2R "B Chain B, A Natural Selected Dimorphism InHla B44 Alters Self, Peptide Reportoire And T CellRecognition." 101.01 99 99 100 8e-54 PDB 1ONQ "B Chain B, Crystal Structure Of Cd1a InComplex With A Sulfatide" 101.01 99 99 100 8e-54 PDB 1P7Q "B Chain B, Crystal Structure Of Hla-A2 BoundTo Lir-1, A Host And Viral Mhc Receptor" 101.01 99 99 100 8e-54 PDB 1QLF "B Chain B, Mhc Class I H-2db Complexed WithGlycopeptide K3g" 101.01 99 99 100 8e-54 PDB 1R3H "B Chain B, Crystal Structure Of T10" 101.01 99 99 100 8e-54 PDB 2HLA "B Chain B, Human Class I HistocompatibilityAntigen Aw 68.1 (HLA-Aw 68.1, Human Leucocyte Antigen)" 101.01 99 99 100 8e-54 PDB 3HLA "B Chain B, Human Class I HistocompatibilityAntigen A2.1 (HLA-A2.1 Human Leucocyte Antigen)" 101.01 99 99 100 8e-54 PDB 1QQD "B Chain B, Crystal Structure Of Hla-Cw4, ALigand For The Kir2d Natural Killer Cell InhibitoryReceptor" 101.01 99 98 99 5e-53 PDB 1PY4 "A Chain A, Beta2 Microglobulin Mutant H31yDisplays Hints For Amyloid Formations" 100.00 100 100 100 5e-55 PDB 1A9B "B Chain B, Decamer-Like Conformation Of ANano-Peptide Bound To Hla-B 3501 Due To NonstandardPositioning Of The C-Terminus" 100.00 100 99 100 2e-54 PDB 1A9E "B Chain B, Decamer-Like Conformation Of ANano-Peptide Bound To Hla-B 3501 Due To NonstandardPositioning Of The C-Terminus" 100.00 100 99 100 2e-54 PDB 1B0G "B Chain B, Crystal Structure Of Human Class IMhc (Hla-A2.1) Complexed With Beta 2-Microglobulin AndHuman Peptide P1049" 100.00 100 99 100 2e-54 PDB 1B0R "B Chain B, Crystal Structure Of Hla-A0201Complexed With A Peptide With The Carboxyl-TerminalGroup Substituted By A Methyl Group" 100.00 100 99 100 2e-54 PDB 1BD2 "B Chain B, Complex Between Human T-CellReceptor B7, Viral Peptide (Tax) And Mhc Class IMolecule Hla-A 0201" 100.00 100 99 100 2e-54 PDB 1CG9 "B Chain B, Complex Recognition Of TheSupertypic Bw6-Determinant On Hla-B And-C Molecules ByThe Monoclonal Antibody Sfr8-B6" 100.00 100 99 100 2e-54 PDB 1DUY "B Chain B, Crystal Structure OfHla-A0201OCTAMERIC TAX PEPTIDE Complex" 100.00 100 99 100 2e-54 PDB 1DUZ "B Chain B, Human Class I HistocompatibilityAntigen (Hla-A 0201) In Complex With A Nonameric PeptideFrom Htlv-1 Tax Protein" 100.00 100 99 100 2e-54 PDB 1EEY "B Chain B, Crystal Structure Determination OfHla A2 Complexed To Peptide Gp2 With The Substitution(I2lV5LL9V)" 100.00 100 99 100 2e-54 PDB 1EEZ "B Chain B, Crystal Structure Determination OfHla-A2.1 Complexed To Gp2 Peptide Variant(I2lV5L)" 100.00 100 99 100 2e-54 PDB 1EFX "B Chain B, Structure Of A Complex Between TheHuman Natural Killer Cell Receptor Kir2dl2 And A Class IMhc Ligand Hla-Cw3" 100.00 100 99 100 2e-54 PDB 1GZP "B Chain B, Cd1b In Complex With Gm2Ganglioside" 100.00 100 99 100 2e-54 PDB 1GZQ "B Chain B, Cd1b In Complex WithPhophatidylinositol" 100.00 100 99 100 2e-54 PDB 1HHG "B Chain B, Human Class I HistocompatibilityAntigen (Hla-A 0201) Complex With A Nonameric PeptideFrom Hiv-1 Gp120 Envelope Protein (Residues 195-207)" 100.00 100 99 100 2e-54 PDB 1HHH "B Chain B, Human Class I HistocompatibilityAntigen (Hla-A 0201) Complex With A Decameric PeptideFrom Hepatitis B Nucleocapsid Protein (Residues 18-27)" 100.00 100 99 100 2e-54 PDB 1HHI "B Chain B, Human Class I HistocompatibilityAntigen (Hla-A 0201) Complex With A Nonameric PeptideFrom Influenza A Matrix Protein M1 (Residues 58-66)" 100.00 100 99 100 2e-54 PDB 1HHJ "B Chain B, Human Class I HistocompatibilityAntigen (Hla-A 0201) Complex With A Nonameric PeptideFrom Hiv-1 Reverse Transcriptase (Residues 309-317)" 100.00 100 99 100 2e-54 PDB 1HHK "B Chain B, Human Class I HistocompatibilityAntigen (Hla-A 0201) Complex With A Nonameric PeptideFrom Htlv-1 Tax Protein (Residues 11-19)" 100.00 100 99 100 2e-54 PDB 1I1F "B Chain B, Crystal Structure Of Human Class IMhc (Hla-A2.1) Complexed With Beta 2- Microglobulin AndHiv-Rt Variant Peptide I1y" 100.00 100 99 100 2e-54 PDB 1I1Y "B Chain B, Crystal Structure Of Human Class IMhc (Hla-A2.1) Complexed With Beta 2-Microglobulin AndHiv-Rt Variant Peptide I1y" 100.00 100 99 100 2e-54 PDB 1I4F "B Chain B, Crystal Structure OfHla-A0201MAGE-A4-Peptide Complex" 100.00 100 99 100 2e-54 PDB 1I7R "B Chain B, Crystal Structure Of Class I Mhc A2In Complex With Peptide P1058" 100.00 100 99 100 2e-54 PDB 1I7T "B Chain B, Crystal Structure Of Class I Mhc A2In Complex With Peptide P1049-5v" 100.00 100 99 100 2e-54 PDB 1I7U "B Chain B, Crystal Structure Of Class I Mhc A2In Complex With Peptide P1049-6v" 100.00 100 99 100 2e-54 PDB 1IM3 "B Chain B, Crystal Structure Of The HumanCytomegalovirus Protein Us2 Bound To The Mhc Class IMolecule Hla-A2TAX" 100.00 100 99 100 2e-54 PDB 1IM9 "B Chain B, Crystal Structure Of The HumanNatural Killer Cell Inhibitory Receptor Kir2dl1 Bound ToIts Mhc Ligand Hla-Cw4" 100.00 100 99 100 2e-54 PDB 1JF1 "B Chain B, Crystal Structure Of Hla-A20201 InComplex With A Decameric Altered Peptide Ligand From TheMart-1MELAN-A" 100.00 100 99 100 2e-54 PDB 1JGD "B Chain B, Hla-B2709 Bound To Deca-PeptideS10r" 100.00 100 99 100 2e-54 PDB 1JGE "B Chain B, Hla-B2705 Bound To Nona-Peptide M9" 100.00 100 99 100 2e-54 PDB 1JHT "B Chain B, Crystal Structure Of Hla-A20201 InComplex With A Nonameric Altered Peptide Ligand(Algigiltv) From The Mart- 1MELAN-A." 100.00 100 99 100 2e-54 PDB 1JNJ "A Chain A, Nmr Solution Structure Of The HumanBeta2-Microglobulin" 100.00 100 99 100 2e-54 PDB 1K5N "B Chain B, Hla-B2709 Bound To Nona-Peptide M9" 100.00 100 99 100 2e-54 PDB 1KPR "B Chain B, The Human Non-Classical MajorHistocompatibility Complex Molecule Hla-E" 100.00 100 99 100 2e-54 PDB 1KTL "B Chain B, The Human Non-Classical MajorHistocompatibility Complex Molecule Hla-E" 100.00 100 99 100 2e-54 PDB 1LDS "A Chain A, Crystal Structure Of MonomericHuman Beta-2-Microglobulin" 100.00 100 99 100 2e-54 PDB 1LP9 "B Chain B, Xenoreactive Complex Ahiii 12.2 TcrBound To P1049HLA-A2.1" 100.00 100 99 100 2e-54 PDB 1MHE "B Chain B, The Human Non-Classical MajorHistocompatibility Complex Molecule Hla-E" 100.00 100 99 100 2e-54 PDB 1OF2 "B Chain B, Crystal Structure Of Hla-B2709Complexed With The Vasoactive Intestinal Peptide Type 1Receptor (Vipr) Peptide (Residues 400-408)" 100.00 100 99 100 2e-54 PDB 1OGA "B Chain B, A Structural Basis ForImmunodominant Human T-Cell Receptor Recognition." 100.00 100 99 100 2e-54 PDB 1OGT "B Chain B, Crystal Structure Of Hla-B2705Complexed With The Vasoactive Intestinal Peptide Type 1Receptor (Vipr) Peptide (Residues 400-408)" 100.00 100 99 100 2e-54 PDB 1Q94 "B Chain B, Structures Of Hla-A1101 In ComplexWith Immunodominant Nonamer And Decamer Hiv-1 EpitopesClearly Reveal The Presence Of A Middle Anchor Residue" 100.00 100 99 100 2e-54 PDB 1QEW "B Chain B, Human Class I HistocompatibilityAntigen (Hla-A 0201) Complex With A Nonameric PeptideFrom Melanoma-Associated Antigen 3 (Residues 271-279)" 100.00 100 99 100 2e-54 PDB 1QR1 "B Chain B, Poor Binding Of A Her-2NEU EPITOPE(GP2) TO HLA-A2.1 Is Due To A Lack Of Interactions InThe Center Of The Peptide" 100.00 100 99 100 2e-54 PDB 1QRN "B Chain B, Crystal Structure Of Human A6 TcrComplexed With Hla-A2 Bound To Altered Htlv-1 TaxPeptide P6a" 100.00 100 99 100 2e-54 PDB 1QSE "B Chain B, Structure Of Human A6-Tcr Bound ToHla-A2 Complexed With Altered Htlv-1 Tax Peptide V7r" 100.00 100 99 100 2e-54 PDB 1QSF "B Chain B, Structure Of A6-Tcr Bound To Hla-A2Complexed With Altered Htlv-1 Tax Peptide Y8a" 100.00 100 99 100 2e-54 PDB 1QVO "B Chain B, Structures Of Hla-A1101 In ComplexWith Immunodominant Nonamer And Decamer Hiv-1 EpitopesClearly Reveal The Presence Of A Middle Anchor Residue" 100.00 100 99 100 2e-54 PDB 1TMC "B Chain B, Truncated Human Class IHistocompatibility Antigen Hla-Aw68 Complexed With ADecameric Peptide (Evappeyhrk)" 100.00 100 99 100 2e-54 PDB 1UQS "B Chain B, The Crystal Structure Of Human Cd1bWith A Bound Bacterial Glycolipid" 100.00 100 99 100 2e-54 PDB 2CLR "B Chain B, Human Class I HistocompatibilityAntigen (Hla-A 0201) Complexed With A Decameric PeptideFrom Calreticulin" 100.00 100 99 100 2e-54 PDB 1CE6 "B Chain B, Mhc Class I H-2db Complexed With ASendai Virus Nucleoprotein Peptide" 92.59 108 99 100 8e-54 DBJ BAA35182.1 "beta 2-microglobulin [Homo sapiens]" 84.03 119 99 100 8e-54 EMBL CAA23830.1 "beta-2 microglobulin [Homo sapiens]" 90.91 110 99 100 8e-54 EMBL CAG33347.1 "B2M [Homo sapiens]" 84.03 119 98 100 2e-53 GenBank AAA87972.1 beta-2-microglobulin 84.03 119 99 100 8e-54 GenBank AAA88008.1 beta-2-microglobulin 84.03 119 99 100 8e-54 GenBank AAD48083.1 "beta-2 microglobulin [Homo sapiens]" 84.03 119 99 100 8e-54 GenBank AAG02006.1 "similar to Homo sapiens mRNA for beta2-microglobulin with GenBank Accession Number AB021288" 84.03 119 99 100 8e-54 GenBank AAH32589.1 "Beta-2-microglobulin, precursor [Homosapiens]" 84.03 119 99 100 8e-54 PIR I36963 "beta-2-microglobulin precursor - chimpanzee" 84.03 119 99 100 8e-54 PIR I37063 "beta-2-microglobulin precursor - gorilla" 84.03 119 99 100 8e-54 PIR MGHUB2 "beta-2-microglobulin precursor [validated] -human" 84.03 119 99 100 8e-54 REF NP_004039.1 "beta-2-microglobulin precursor [Homosapiens]" 84.03 119 99 100 8e-54 SWISS-PROT P61769 "B2MG_HUMAN Beta-2-microglobulin precursor(HDCMA22P)" 84.03 119 99 100 8e-54 SWISS-PROT P61770 "B2MG_PANTR Beta-2-microglobulin precursor" 84.03 119 99 100 8e-54 SWISS-PROT P61771 "B2MG_GORGO Beta-2-microglobulin precursor" 84.03 119 99 100 8e-54 stop_ save_ ######################################## # Molecular bond linkage definitions # ######################################## save_crosslink_bond_definitions _Saveframe_category crosslink_bonds loop_ _Bond_order _Bond_type _Atom_one_mol_system_component_name _Atom_one_residue_seq_code _Atom_one_residue_label _Atom_one_atom_name _Atom_two_mol_system_component_name _Atom_two_residue_seq_code _Atom_two_residue_label _Atom_two_atom_name single disulfide "H31Ybeta2-microglobulin" 26 CYS SG "H31Ybeta2-microglobulin" 81 CYS SG stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $H31Ybeta2-m 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 $H31Ybeta2-m 'recombinant technology' "E. coli" Escherichia coli . . stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Saveframe_category sample _Sample_type solution loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $H31Ybeta2-m 0.8 mM . "sodium phosphate" 70 mM . "sodium chloride" 100 mM . H2O 100 % . stop_ save_ ############################ # Computer software used # ############################ save_FELIX _Saveframe_category software _Name FELIX _Version 2000 save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model Avance _Field_strength 500 save_ ############################# # NMR applied experiments # ############################# save_NMR_applied_experiment _Saveframe_category NMR_applied_experiment _Experiment_name ; 1H-1H TOCSY 1H-1H NOESY ; save_ ####################### # Sample conditions # ####################### save_Ex-cond_1 _Saveframe_category sample_conditions loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 6.5 0.1 n/a temperature 303 0.1 K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference _Saveframe_category chemical_shift_reference 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 Dioxane H 1 'methylene protons' ppm 3.53 internal direct . . . 1.0 stop_ save_ ################################### # Assigned chemical shift lists # ################################### ################################################################### # Chemical Shift Ambiguity Index Value Definitions # # # # Index Value Definition # # # # 1 Unique # # 2 Ambiguity of geminal atoms or geminal methyl # # proton groups # # 3 Aromatic atoms on opposite sides of the ring # # (e.g. Tyr HE1 and HE2 protons) # # 4 Intraresidue ambiguities (e.g. Lys HG and # # HD protons) # # 5 Interresidue ambiguities (Lys 12 vs. Lys 27) # # 9 Ambiguous, specific ambiguity not defined # # # ################################################################### save_shift_set_1 _Saveframe_category assigned_chemical_shifts loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $Ex-cond_1 _Chem_shift_reference_set_label $chemical_shift_reference _Mol_system_component_name "H31Ybeta2-microglobulin" loop_ _Atom_shift_assign_ID _Residue_seq_code _Residue_label _Atom_name _Atom_type _Chem_shift_value _Chem_shift_value_error _Chem_shift_ambiguity_code 1 4 ARG H H 9.34 0.02 1 2 4 ARG HA H 4.86 0.02 1 3 4 ARG HB3 H 2.25 0.02 1 4 4 ARG HD2 H 3.15 0.02 1 5 4 ARG HG2 H 1.75 0.02 1 6 5 THR H H 8.39 0.02 1 7 5 THR HA H 5.00 0.02 1 8 5 THR HB H 4.08 0.02 1 9 5 THR HG2 H 1.31 0.02 1 10 6 PRO HA H 4.39 0.02 1 11 6 PRO HB2 H 1.51 0.02 1 12 6 PRO HD2 H 3.62 0.02 2 13 6 PRO HD3 H 3.08 0.02 2 14 6 PRO HG2 H 1.10 0.02 2 15 6 PRO HG3 H 1.64 0.02 2 16 7 LYS H H 9.20 0.02 1 17 7 LYS HA H 4.49 0.02 1 18 7 LYS HB2 H 1.77 0.02 2 19 7 LYS HB3 H 1.51 0.02 2 20 7 LYS HG2 H 1.41 0.02 1 21 8 ILE H H 8.38 0.02 1 22 8 ILE HA H 4.73 0.02 1 23 8 ILE HB H 1.63 0.02 1 24 8 ILE HG12 H 1.31 0.02 1 25 8 ILE HG2 H 0.76 0.02 1 26 9 GLN H H 9.03 0.02 1 27 9 GLN HA H 4.92 0.02 1 28 9 GLN HB2 H 2.19 0.02 2 29 9 GLN HB3 H 2.35 0.02 2 30 9 GLN HE21 H 7.49 0.02 2 31 9 GLN HE22 H 6.79 0.02 2 32 9 GLN HG2 H 2.43 0.02 1 33 10 VAL H H 9.05 0.02 1 34 10 VAL HA H 5.32 0.02 1 35 10 VAL HB H 2.02 0.02 1 36 10 VAL HG1 H 0.91 0.02 2 37 10 VAL HG2 H 0.96 0.02 2 38 11 TYR H H 8.45 0.02 1 39 11 TYR HA H 5.30 0.02 1 40 11 TYR HB2 H 3.39 0.02 2 41 11 TYR HB3 H 3.10 0.02 2 42 11 TYR HD1 H 6.79 0.02 1 43 11 TYR HE1 H 6.58 0.02 1 44 12 SER H H 9.33 0.02 1 45 12 SER HA H 5.32 0.02 1 46 12 SER HB2 H 3.67 0.02 2 47 12 SER HB3 H 4.44 0.02 2 48 13 ARG H H 8.84 0.02 1 49 13 ARG HA H 3.92 0.02 1 50 13 ARG HB2 H 1.98 0.02 2 51 13 ARG HB3 H 1.73 0.02 2 52 13 ARG HG2 H 1.38 0.02 1 53 14 HIS H H 8.31 0.02 1 54 14 HIS HA H 5.33 0.02 1 55 14 HIS HB2 H 3.23 0.02 2 56 14 HIS HB3 H 2.89 0.02 2 57 14 HIS HD2 H 7.06 0.02 1 58 14 HIS HE1 H 7.84 0.02 1 59 15 PRO HA H 4.50 0.02 1 60 15 PRO HB2 H 1.92 0.02 2 61 15 PRO HB3 H 2.42 0.02 2 62 15 PRO HD2 H 4.07 0.02 2 63 15 PRO HD3 H 3.81 0.02 2 64 15 PRO HG2 H 2.07 0.02 2 65 15 PRO HG3 H 2.24 0.02 2 66 16 ALA H H 9.03 0.02 1 67 16 ALA HA H 4.10 0.02 1 68 16 ALA HB H 1.67 0.02 1 69 17 GLU H H 8.86 0.02 1 70 17 GLU HA H 4.39 0.02 1 71 17 GLU HB2 H 1.85 0.02 1 72 17 GLU HG2 H 2.14 0.02 1 73 18 ASN H H 8.77 0.02 1 74 18 ASN HA H 4.47 0.02 1 75 18 ASN HB2 H 2.75 0.02 2 76 18 ASN HB3 H 2.67 0.02 2 77 18 ASN HD21 H 7.53 0.02 2 78 18 ASN HD22 H 7.12 0.02 2 79 19 GLY H H 8.82 0.02 1 80 19 GLY HA2 H 4.17 0.02 2 81 19 GLY HA3 H 3.51 0.02 2 82 20 LYS H H 7.84 0.02 1 83 20 LYS HA H 4.64 0.02 1 84 20 LYS HB2 H 1.82 0.02 2 85 20 LYS HB3 H 1.76 0.02 2 86 20 LYS HD2 H 1.57 0.02 1 87 20 LYS HE2 H 2.91 0.02 1 88 20 LYS HG2 H 1.29 0.02 1 89 21 SER H H 8.35 0.02 1 90 21 SER HA H 4.24 0.02 1 91 21 SER HB2 H 3.73 0.02 1 92 22 ASN H H 8.89 0.02 1 93 22 ASN HA H 4.88 0.02 1 94 22 ASN HB2 H 2.54 0.02 2 95 22 ASN HB3 H 2.72 0.02 2 96 23 PHE H H 10.33 0.02 1 97 23 PHE HA H 5.42 0.02 1 98 23 PHE HB2 H 2.67 0.02 2 99 23 PHE HB3 H 2.62 0.02 2 100 23 PHE HD1 H 7.00 0.02 1 101 23 PHE HE1 H 7.32 0.02 1 102 23 PHE HZ H 7.39 0.02 1 103 24 LEU H H 8.98 0.02 1 104 24 LEU HA H 3.68 0.02 1 105 24 LEU HB2 H 0.80 0.02 2 106 24 LEU HB3 H -0.82 0.02 2 107 24 LEU HD1 H -0.00 0.02 2 108 24 LEU HD2 H -0.57 0.02 2 109 24 LEU HG H 0.65 0.02 1 110 25 ASN H H 8.19 0.02 1 111 25 ASN HA H 5.37 0.02 1 112 25 ASN HB2 H 1.82 0.02 2 113 25 ASN HB3 H 1.39 0.02 2 114 26 CYS H H 9.63 0.02 1 115 26 CYS HA H 5.11 0.02 1 116 26 CYS HB2 H 2.52 0.02 2 117 26 CYS HB3 H 3.27 0.02 2 118 27 TYR H H 9.66 0.02 1 119 27 TYR HA H 5.40 0.02 1 120 27 TYR HB2 H 3.21 0.02 1 121 27 TYR HD1 H 7.18 0.02 1 122 27 TYR HE1 H 6.64 0.02 1 123 28 VAL H H 8.81 0.02 1 124 28 VAL HA H 5.12 0.02 1 125 28 VAL HB H 1.92 0.02 1 126 28 VAL HG1 H 0.73 0.02 2 127 28 VAL HG2 H 0.89 0.02 2 128 29 SER H H 8.99 0.02 1 129 29 SER HA H 5.66 0.02 1 130 29 SER HB2 H 3.81 0.02 2 131 29 SER HB3 H 3.36 0.02 2 132 36 ILE H H 7.94 0.02 1 133 36 ILE HA H 4.56 0.02 1 134 36 ILE HB H 1.35 0.02 1 135 36 ILE HD1 H -0.53 0.02 1 136 36 ILE HG13 H 0.63 0.02 2 137 36 ILE HG12 H 1.49 0.02 2 138 36 ILE HG2 H 0.58 0.02 1 139 37 GLU H H 8.02 0.02 1 140 37 GLU HA H 4.56 0.02 1 141 37 GLU HB2 H 1.90 0.02 2 142 37 GLU HB3 H 1.71 0.02 2 143 37 GLU HG3 H 2.03 0.02 1 144 38 VAL H H 7.96 0.02 1 145 38 VAL HA H 4.62 0.02 1 146 38 VAL HB H 0.43 0.02 1 147 38 VAL HG1 H 0.23 0.02 2 148 38 VAL HG2 H 0.48 0.02 2 149 39 ASP H H 8.83 0.02 1 150 39 ASP HA H 4.93 0.02 1 151 39 ASP HB2 H 2.37 0.02 2 152 39 ASP HB3 H 2.16 0.02 2 153 40 LEU H H 9.04 0.02 1 154 40 LEU HA H 4.99 0.02 1 155 40 LEU HB2 H 1.67 0.02 2 156 40 LEU HB3 H 1.20 0.02 2 157 40 LEU HD1 H 0.73 0.02 1 158 41 LEU H H 8.97 0.02 1 159 41 LEU HA H 4.98 0.02 1 160 41 LEU HB2 H 1.56 0.02 2 161 41 LEU HB3 H 0.80 0.02 2 162 41 LEU HD1 H 0.38 0.02 2 163 41 LEU HD2 H 0.58 0.02 2 164 41 LEU HG H 1.19 0.02 1 165 42 LYS H H 8.82 0.02 1 166 42 LYS HA H 4.40 0.02 1 167 42 LYS HB2 H 1.72 0.02 2 168 42 LYS HG2 H 0.57 0.02 2 169 43 ASN H H 9.72 0.02 1 170 43 ASN HA H 4.34 0.02 1 171 43 ASN HB2 H 2.86 0.02 2 172 43 ASN HB3 H 2.92 0.02 2 173 43 ASN HD21 H 7.70 0.02 2 174 43 ASN HD22 H 7.97 0.02 2 175 44 GLY H H 8.80 0.02 1 176 44 GLY HA2 H 3.30 0.02 2 177 44 GLY HA3 H 4.15 0.02 2 178 45 GLU H H 7.81 0.02 1 179 45 GLU HA H 4.56 0.02 1 180 45 GLU HB2 H 1.93 0.02 2 181 45 GLU HB3 H 2.02 0.02 2 182 45 GLU HG2 H 2.15 0.02 2 183 45 GLU HG3 H 2.28 0.02 2 184 46 ARG H H 8.65 0.02 1 185 46 ARG HA H 4.15 0.02 1 186 46 ARG HB2 H 1.61 0.02 1 187 46 ARG HD2 H 3.10 0.02 1 188 46 ARG HD3 H 3.06 0.02 1 189 46 ARG HG2 H 1.53 0.02 2 190 46 ARG HG3 H 1.32 0.02 2 191 47 ILE H H 8.79 0.02 1 192 47 ILE HA H 3.97 0.02 1 193 47 ILE HB H 1.52 0.02 1 194 47 ILE HD1 H 0.84 0.02 1 195 47 ILE HG13 H 1.05 0.02 2 196 47 ILE HG12 H 1.69 0.02 2 197 47 ILE HG2 H 0.95 0.02 1 198 48 GLU H H 8.48 0.02 1 199 48 GLU HA H 4.16 0.02 1 200 48 GLU HB2 H 2.07 0.02 2 201 48 GLU HB3 H 2.00 0.02 2 202 48 GLU HG2 H 2.22 0.02 2 203 48 GLU HG3 H 2.35 0.02 2 204 49 LYS H H 7.96 0.02 1 205 49 LYS HA H 4.51 0.02 1 206 49 LYS HB2 H 1.93 0.02 2 207 49 LYS HB3 H 1.77 0.02 2 208 49 LYS HE2 H 3.12 0.02 2 209 49 LYS HE3 H 3.02 0.02 2 210 49 LYS HG2 H 1.38 0.02 2 211 49 LYS HG3 H 1.44 0.02 2 212 50 VAL H H 7.80 0.02 1 213 50 VAL HA H 4.39 0.02 1 214 50 VAL HB H 2.10 0.02 1 215 50 VAL HG1 H 1.01 0.02 2 216 50 VAL HG2 H 1.07 0.02 2 217 51 GLU H H 8.43 0.02 1 218 51 GLU HA H 4.46 0.02 1 219 51 GLU HB2 H 0.73 0.02 2 220 51 GLU HB3 H 1.55 0.02 2 221 51 GLU HG2 H 2.05 0.02 1 222 52 HIS H H 8.09 0.02 1 223 52 HIS HA H 5.48 0.02 1 224 52 HIS HB2 H 2.42 0.02 2 225 52 HIS HB3 H 1.96 0.02 2 226 52 HIS HD2 H 6.97 0.02 1 227 52 HIS HE1 H 8.47 0.02 1 228 53 SER H H 9.14 0.02 1 229 53 SER HA H 4.67 0.02 1 230 53 SER HB2 H 4.48 0.02 2 231 53 SER HB3 H 4.08 0.02 2 232 54 ASP H H 8.68 0.02 1 233 54 ASP HA H 4.79 0.02 1 234 54 ASP HB2 H 2.71 0.02 2 235 54 ASP HB3 H 2.57 0.02 2 236 55 LEU H H 8.72 0.02 1 237 55 LEU HA H 4.34 0.02 1 238 55 LEU HB2 H 1.84 0.02 1 239 55 LEU HD1 H 1.06 0.02 2 240 55 LEU HD2 H 0.94 0.02 2 241 55 LEU HG H 1.67 0.02 1 242 56 SER H H 8.10 0.02 1 243 56 SER HA H 4.80 0.02 1 244 56 SER HB2 H 3.39 0.02 2 245 56 SER HB3 H 2.69 0.02 2 246 57 PHE H H 8.18 0.02 1 247 57 PHE HA H 4.99 0.02 1 248 57 PHE HB2 H 2.59 0.02 1 249 57 PHE HD1 H 6.30 0.02 1 250 57 PHE HE1 H 6.88 0.02 1 251 57 PHE HZ H 6.82 0.02 1 252 59 LYS HA H 3.75 0.02 1 253 59 LYS HB2 H 1.71 0.02 1 254 59 LYS HD2 H 1.61 0.02 1 255 59 LYS HE2 H 2.95 0.02 1 256 59 LYS HG2 H 1.37 0.02 1 257 60 ASP H H 7.66 0.02 1 258 60 ASP HA H 4.35 0.02 1 259 60 ASP HB2 H 2.29 0.02 1 260 63 PHE HA H 5.32 0.02 1 261 63 PHE HB2 H 2.41 0.02 2 262 63 PHE HB3 H 1.52 0.02 2 263 63 PHE HD1 H 7.30 0.02 1 264 63 PHE HE1 H 7.21 0.02 1 265 64 TYR H H 8.23 0.02 1 266 64 TYR HA H 5.51 0.02 1 267 64 TYR HB2 H 3.03 0.02 2 268 64 TYR HB3 H 2.83 0.02 2 269 64 TYR HD1 H 7.04 0.02 1 270 64 TYR HE1 H 6.64 0.02 1 271 65 LEU H H 9.17 0.02 1 272 65 LEU HA H 4.63 0.02 1 273 65 LEU HB2 H 2.03 0.02 1 274 65 LEU HD1 H 1.05 0.02 2 275 65 LEU HD2 H 0.95 0.02 2 276 65 LEU HG H 1.77 0.02 1 277 66 LEU H H 8.14 0.02 1 278 66 LEU HA H 5.46 0.02 1 279 66 LEU HB3 H 1.96 0.02 1 280 66 LEU HD1 H 1.05 0.02 2 281 66 LEU HD2 H 0.78 0.02 2 282 66 LEU HG H 1.57 0.02 1 283 67 TYR H H 9.10 0.02 1 284 67 TYR HA H 5.35 0.02 1 285 67 TYR HB2 H 2.66 0.02 2 286 67 TYR HB3 H 3.04 0.02 2 287 67 TYR HD1 H 6.97 0.02 1 288 67 TYR HE1 H 6.64 0.02 1 289 68 TYR H H 8.92 0.02 1 290 68 TYR HA H 5.94 0.02 1 291 68 TYR HB2 H 2.65 0.02 2 292 68 TYR HB3 H 3.22 0.02 2 293 68 TYR HD1 H 6.68 0.02 1 294 68 TYR HE1 H 6.53 0.02 1 295 69 THR H H 8.30 0.02 1 296 69 THR HA H 4.84 0.02 1 297 69 THR HB H 4.10 0.02 1 298 69 THR HG2 H 0.93 0.02 1 299 70 GLU H H 8.48 0.02 1 300 70 GLU HA H 4.29 0.02 1 301 70 GLU HB2 H 1.81 0.02 2 302 70 GLU HB3 H 1.70 0.02 2 303 70 GLU HG2 H 1.87 0.02 1 304 71 PHE H H 8.74 0.02 1 305 71 PHE HA H 4.82 0.02 1 306 71 PHE HB2 H 2.79 0.02 2 307 71 PHE HB3 H 2.69 0.02 2 308 71 PHE HD1 H 6.19 0.02 1 309 71 PHE HZ H 5.69 0.02 1 310 72 THR H H 8.21 0.02 1 311 72 THR HA H 4.46 0.02 1 312 72 THR HB H 3.86 0.02 1 313 72 THR HG2 H 0.84 0.02 1 314 73 PRO HA H 4.57 0.02 1 315 73 PRO HB2 H 2.13 0.02 2 316 73 PRO HB3 H 2.39 0.02 2 317 73 PRO HD2 H 2.22 0.02 2 318 73 PRO HD3 H 3.96 0.02 2 319 73 PRO HG2 H 1.98 0.02 2 320 73 PRO HG3 H 1.40 0.02 2 321 74 THR H H 8.04 0.02 1 322 74 THR HA H 4.66 0.02 1 323 74 THR HB H 4.53 0.02 1 324 74 THR HG2 H 1.31 0.02 1 325 75 GLU H H 9.07 0.02 1 326 75 GLU HA H 4.19 0.02 1 327 75 GLU HB2 H 2.06 0.02 1 328 75 GLU HG2 H 2.26 0.02 2 329 75 GLU HG3 H 2.33 0.02 2 330 76 LYS H H 7.79 0.02 1 331 76 LYS HA H 4.43 0.02 1 332 76 LYS HB2 H 1.85 0.02 2 333 76 LYS HB3 H 1.76 0.02 2 334 76 LYS HD2 H 1.65 0.02 1 335 76 LYS HE2 H 2.97 0.02 1 336 76 LYS HG2 H 1.38 0.02 1 337 77 ASP H H 7.11 0.02 1 338 77 ASP HA H 5.11 0.02 1 339 77 ASP HB2 H 2.80 0.02 2 340 77 ASP HB3 H 2.14 0.02 2 341 78 GLU H H 8.60 0.02 1 342 78 GLU HA H 4.79 0.02 1 343 78 GLU HB2 H 1.97 0.02 2 344 78 GLU HB3 H 2.07 0.02 2 345 78 GLU HG3 H 2.35 0.02 1 346 79 TYR H H 9.48 0.02 1 347 79 TYR HA H 5.59 0.02 1 348 79 TYR HB2 H 2.81 0.02 2 349 79 TYR HB3 H 2.71 0.02 2 350 79 TYR HD1 H 7.07 0.02 1 351 79 TYR HE1 H 6.87 0.02 1 352 80 ALA H H 8.78 0.02 1 353 80 ALA HA H 5.03 0.02 1 354 80 ALA HB H 1.18 0.02 1 355 81 CYS H H 9.10 0.02 1 356 81 CYS HA H 5.11 0.02 1 357 81 CYS HB2 H 2.61 0.02 2 358 81 CYS HB3 H 3.04 0.02 2 359 82 ARG H H 9.39 0.02 1 360 82 ARG HA H 5.38 0.02 1 361 82 ARG HB2 H 1.78 0.02 2 362 82 ARG HB3 H 1.17 0.02 2 363 83 VAL H H 9.01 0.02 1 364 83 VAL HA H 4.96 0.02 1 365 83 VAL HB H 1.67 0.02 1 366 83 VAL HG1 H 0.58 0.02 2 367 83 VAL HG2 H 0.79 0.02 2 368 84 ASN H H 9.00 0.02 1 369 84 ASN HA H 5.17 0.02 1 370 84 ASN HB2 H 2.79 0.02 2 371 84 ASN HB3 H 2.37 0.02 2 372 84 ASN HD21 H 7.38 0.02 2 373 84 ASN HD22 H 6.61 0.02 2 374 85 HIS H H 7.72 0.02 1 375 85 HIS HA H 4.53 0.02 1 376 85 HIS HB2 H 2.88 0.02 2 377 85 HIS HB3 H 2.38 0.02 2 378 85 HIS HD2 H 7.52 0.02 1 379 85 HIS HE1 H 8.02 0.02 1 380 86 VAL H H 8.02 0.02 1 381 86 VAL HA H 3.96 0.02 1 382 86 VAL HB H 1.92 0.02 1 383 86 VAL HG1 H 0.53 0.02 2 384 86 VAL HG2 H 0.84 0.02 2 385 87 THR H H 7.53 0.02 1 386 87 THR HA H 4.12 0.02 1 387 87 THR HB H 4.48 0.02 1 388 87 THR HG1 H 7.65 0.02 1 389 87 THR HG2 H 1.44 0.02 1 390 88 LEU H H 8.01 0.02 1 391 88 LEU HA H 4.74 0.02 1 392 88 LEU HB2 H 2.01 0.02 1 393 88 LEU HD1 H 0.93 0.02 1 394 88 LEU HG H 1.70 0.02 1 395 89 SER HA H 4.23 0.02 1 396 89 SER HB2 H 3.95 0.02 1 397 90 GLN H H 7.53 0.02 1 398 90 GLN HA H 4.72 0.02 1 399 90 GLN HB2 H 2.14 0.02 2 400 90 GLN HB3 H 1.87 0.02 2 401 90 GLN HG2 H 2.27 0.02 2 402 90 GLN HG3 H 2.01 0.02 2 403 91 PRO HA H 4.48 0.02 1 404 91 PRO HB2 H 1.86 0.02 2 405 91 PRO HB3 H 1.44 0.02 2 406 91 PRO HD2 H 3.71 0.02 2 407 91 PRO HD3 H 3.50 0.02 2 408 91 PRO HG2 H 1.98 0.02 2 409 91 PRO HG3 H 1.77 0.02 2 410 92 LYS H H 8.71 0.02 1 411 92 LYS HA H 4.50 0.02 1 412 92 LYS HB2 H 1.70 0.02 2 413 92 LYS HB3 H 1.62 0.02 2 414 92 LYS HG2 H 1.40 0.02 2 415 92 LYS HG3 H 1.30 0.02 2 416 93 ILE H H 8.48 0.02 1 417 93 ILE HA H 4.78 0.02 1 418 93 ILE HB H 1.68 0.02 1 419 93 ILE HG2 H 0.60 0.02 1 420 93 ILE HD1 H 0.73 0.02 1 421 93 ILE HG12 H 1.40 0.02 1 422 94 VAL H H 9.04 0.02 1 423 94 VAL HA H 4.30 0.02 1 424 94 VAL HB H 1.86 0.02 1 425 94 VAL HG1 H 0.91 0.02 2 426 94 VAL HG2 H 1.02 0.02 2 427 95 LYS H H 8.78 0.02 1 428 95 LYS HA H 4.43 0.02 1 429 95 LYS HB2 H 1.82 0.02 2 430 95 LYS HG2 H 1.51 0.02 2 431 95 LYS HG3 H 1.43 0.02 2 432 96 TRP H H 8.68 0.02 1 433 96 TRP HA H 4.61 0.02 1 434 96 TRP HB2 H 3.47 0.02 2 435 96 TRP HB3 H 2.60 0.02 2 436 96 TRP HD1 H 7.11 0.02 1 437 96 TRP HE1 H 10.39 0.02 1 438 96 TRP HE3 H 7.96 0.02 1 439 96 TRP HH2 H 6.95 0.02 1 440 96 TRP HZ2 H 7.62 0.02 1 441 96 TRP HZ3 H 7.46 0.02 1 442 97 ASP H H 8.38 0.02 1 443 97 ASP HA H 4.46 0.02 1 444 97 ASP HB2 H 2.44 0.02 2 445 97 ASP HB3 H 2.72 0.02 2 446 98 ARG H H 7.45 0.02 1 447 98 ARG HA H 3.37 0.02 1 448 98 ARG HB2 H 1.38 0.02 2 449 98 ARG HB3 H 1.12 0.02 2 450 98 ARG HD2 H 2.94 0.02 1 451 98 ARG HG2 H 0.95 0.02 1 452 99 ASP H H 8.18 0.02 1 453 99 ASP HA H 4.62 0.02 1 454 99 ASP HB2 H 2.75 0.02 2 455 99 ASP HB3 H 2.58 0.02 2 456 100 MET H H 7.58 0.02 1 457 100 MET HA H 4.26 0.02 1 458 100 MET HB2 H 2.13 0.02 2 459 100 MET HB3 H 1.99 0.02 2 460 100 MET HG2 H 2.51 0.02 2 461 100 MET HG3 H 2.55 0.02 2 stop_ save_ ####################################### # Cited references within the entry # ####################################### save_ref_1 _Saveframe_category citation _PubMed_ID 11847272 _Citation_full ; Verdone G, Corazza A, Viglino P, Pettirossi F, Giorgetti S, Mangione P, Andreola A, Stoppini M, Bellotti V, Esposito G. Protein Sci 2002 11(3):487-99 The solution structure of human beta2-microglobulin reveals the prodromes of its amyloid transition. ; save_ save_ref_2 _Saveframe_category citation _PubMed_ID 10850793 _Citation_full ; Esposito G, Michelutti R, Verdone G, Viglino P, Hernandez H, Robinson CV, Amoresano A, Dal Piaz F, Monti M, Pucci P, Mangione P, Stoppini M, Merlini G, Ferri G, Bellotti V. Protein Sci 2000 9(5):831-45 Removal of the N-terminal hexapeptide from human beta2-microglobulin facilitates protein aggregation and fibril formation. ; save_