data_5803 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Three-disulfide variant of hen lysozyme: C64A/C80A ; _BMRB_accession_number 5803 _BMRB_flat_file_name bmr5803.str _Entry_type original _Submission_date 2003-05-19 _Accession_date 2003-05-20 _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 Yokota Atsushi . . 2 Hirai Kenichi . . 3 Miyauchi Hiroyo . . 4 Noda Yasuo . . 5 Inoue Kyouko . . 6 Akasaka Kazuyuki . . 7 Tachibana Hideki . . 8 Segawa Shin-ichi . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 572 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2004-09-14 original author . stop_ loop_ _Related_BMRB_accession_number _Relationship 5068 'Recombinant hen lysozyme with extra N-terminal Met' 5069 'Two-disulfide variant of hen lysozyme: 2SS[6-127, 30-115]' 5804 'Three-disulfide variant of hen lysozyme: C76A/C94A' stop_ _Original_release_date 2004-09-14 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; NMR characterization of three-disulfide variants of lysozyme, C64A/C80A, C76A/C94A, and C30A/C115A--a marginally stable state in folded proteins. ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 15157100 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Yokota Atsushi . . 2 Hirai Kenichi . . 3 Miyauchi Hiroyo . . 4 Iimura Satoshi . . 5 Noda Yasuo . . 6 Inoue Kyouko . . 7 Akasaka Kazuyuki . . 8 Tachibana Hideki . . 9 Segawa Shin-ichi . . stop_ _Journal_abbreviation Biochemistry _Journal_volume 43 _Journal_issue 21 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 6663 _Page_last 6669 _Year 2004 _Details . loop_ _Keyword 'Lysozyme Variants' NMR 'Protein Folding' 'Three-Disulfide Intermediate' stop_ save_ ####################################### # Cited references within the entry # ####################################### save_ref_1 _Saveframe_category citation _Citation_full ; van den Berg B, Chung EW, Robinson CV, Dobson CM. Characterisation of the dominant oxidative folding intermediate of hen lysozyme. J Mol Biol. 1999 Jul 16;290(3):781-96. ; _Citation_title 'Characterisation of the dominant oxidative folding intermediate of hen lysozyme.' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 10395829 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 'van den Berg' B . . 2 Chung 'E W' W. . 3 Robinson 'C V' V. . 4 Dobson 'C M' M. . stop_ _Journal_abbreviation 'J. Mol. Biol.' _Journal_name_full 'Journal of molecular biology' _Journal_volume 290 _Journal_issue 3 _Journal_CSD . _Book_title . _Book_chapter_title . _Book_volume . _Book_series . _Book_publisher . _Book_publisher_city . _Book_ISBN . _Conference_title . _Conference_site . _Conference_state_province . _Conference_country . _Conference_start_date . _Conference_end_date . _Conference_abstract_number . _Thesis_institution . _Thesis_institution_city . _Thesis_institution_country . _Page_first 781 _Page_last 796 _Year 1999 _Details ; Reduced denatured lysozyme has been oxidised and refolded at pH values close to neutral in an efficient way by dilution from buffers containing 8.0 M urea, and refolding intermediates were separated by reverse-phase HPLC at pH 2. By using peptic digestion in combination with high-resolution Fourier transform ion cyclotron resonance (FT-ICR) mass spectrometry (MS) and tandem MS/MS the dominant intermediate was identified to be des-[76-94]. This species has three of the four native disulphide bonds, but lacks the Cys76-Cys94 disulphide bond which connects the two folding domains in the native protein. Characterisation of des-[76-94] by 2D1H NMR shows that it has a highly native-like structure. This provides an explanation for the accumulation of this species during refolding as direct oxidation to the fully native protein will be restricted by the burial of Cys94 in the protein interior. ; save_ save_ref_2 _Saveframe_category citation _Citation_full ; Noda Y, Yokota A, Horii D, Tominaga T, Tanisaka Y, Tachibana H, Segawa S. NMR structural study of two-disulfide variant of hen lysozyme: 2SS[6-127, 30-115]--a disulfide intermediate with a partly unfolded structure. Biochemistry. 2002 Feb 19;41(7):2130-9. ; _Citation_title 'NMR structural study of two-disulfide variant of hen lysozyme: 2SS[6-127, 30-115]--a disulfide intermediate with a partly unfolded structure.' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 11841203 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Noda Yasuo . . 2 Yokota Atsushi . . 3 Horii Daisuke . . 4 Tominaga Takeshi . . 5 Tanisaka Yoshiaki . . 6 Tachibana Hideki . . 7 Segawa Shin-ichi . . stop_ _Journal_abbreviation Biochemistry _Journal_name_full Biochemistry _Journal_volume 41 _Journal_issue 7 _Journal_CSD . _Book_title . _Book_chapter_title . _Book_volume . _Book_series . _Book_publisher . _Book_publisher_city . _Book_ISBN . _Conference_title . _Conference_site . _Conference_state_province . _Conference_country . _Conference_start_date . _Conference_end_date . _Conference_abstract_number . _Thesis_institution . _Thesis_institution_city . _Thesis_institution_country . _Page_first 2130 _Page_last 2139 _Year 2002 _Details ; The 15N-labeled recombinant hen lysozyme and two species of two-disulfide variants, denoted as 2SS[6-127, 30-115] and 2SS[64-80, 76-94], were studied by means of NMR spectroscopy. The former variant contains two disulfide bridges in the alpha-domain, while the latter has one disulfide bridge in the beta-domain and the other one at the interface between two domains. Resonance assignments were performed using 3D TOCSY-HSQC and NOESY-HSQC spectra. The 15N-1H-HSQC spectrum of 2SS[6-127, 30-115] was similar to that of recombinant lysozyme as a whole, although a number of cross-peaks disappeared. On the other hand, the HSQC spectrum of 2SS[64-80, 76-94] was characteristic of unfolded proteins. The structure of 2SS[6-127, 30-115] was thoroughly examined on the basis of NOE contacts determined by NMR spectroscopy. The structure of the alpha-domain was quite similar to that of authentic lysozyme, while the beta-domain was largely unstructured. However, NMR data clearly demonstrated that some residual structures exist in the beta-domain. The beta1 and beta2 strands were maintained stably as an antiparallel beta-sheet. In addition, the residues 55 and 56 were located in the vicinity of the end of the B-helix. Further, the C-helix was properly set with side-chains of I88, V92, K96, and V99 facing toward the hydrophobic core in the alpha-domain. These residual structures inherent in the amino acid sequence were evaluated concerning the folding process of lysozyme. Our experiments imply that the establishment of the backbone conformation ranging from residues 76-99 plays a key role in attaining the cooperativity between two domains required for the folding transition. ; save_ ################################## # Molecular system description # ################################## save_system_HEWL _Saveframe_category molecular_system _Mol_system_name 'hen egg white lysozyme' _Abbreviation_common HEWL _Enzyme_commission_number 3.2.1.17 loop_ _Mol_system_component_name _Mol_label 'hen lysozyme Cys mutants, C64A/C80A' $HEWL stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state monomer _System_paramagnetic no _System_thiol_state 'all disulfide bound' loop_ _Biological_function Hydrolase(O-Glycosyl) stop_ _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_HEWL _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'three-disulfide variant of hen lysozyme' _Name_variant C64A/C80A _Abbreviation_common C64A/C80A _Molecular_mass 14374 _Mol_thiol_state 'all disulfide bound' _Details ; Hen lysozyme with Cys64 and Cys80 replaced by Ala and three disulfide bridges between Cys6 and Cys127, between Cys30 and Cys115, and between Cys76 and Cys94. ; ############################## # Polymer residue sequence # ############################## _Residue_count 130 _Mol_residue_sequence ; MKVFGRCELAAAMKRHGLDN YRGYSLGNWVCAAKFESNFN TQATNRNTDGSTDYGILQIN SRWWANDGRTPGSRNLCNIP ASALLSSDITASVNCAKKIV SDGNGMNAWVAWRNRCKGTD VQAWIRGCRL ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 0 MET 2 1 LYS 3 2 VAL 4 3 PHE 5 4 GLY 6 5 ARG 7 6 CYS 8 7 GLU 9 8 LEU 10 9 ALA 11 10 ALA 12 11 ALA 13 12 MET 14 13 LYS 15 14 ARG 16 15 HIS 17 16 GLY 18 17 LEU 19 18 ASP 20 19 ASN 21 20 TYR 22 21 ARG 23 22 GLY 24 23 TYR 25 24 SER 26 25 LEU 27 26 GLY 28 27 ASN 29 28 TRP 30 29 VAL 31 30 CYS 32 31 ALA 33 32 ALA 34 33 LYS 35 34 PHE 36 35 GLU 37 36 SER 38 37 ASN 39 38 PHE 40 39 ASN 41 40 THR 42 41 GLN 43 42 ALA 44 43 THR 45 44 ASN 46 45 ARG 47 46 ASN 48 47 THR 49 48 ASP 50 49 GLY 51 50 SER 52 51 THR 53 52 ASP 54 53 TYR 55 54 GLY 56 55 ILE 57 56 LEU 58 57 GLN 59 58 ILE 60 59 ASN 61 60 SER 62 61 ARG 63 62 TRP 64 63 TRP 65 64 ALA 66 65 ASN 67 66 ASP 68 67 GLY 69 68 ARG 70 69 THR 71 70 PRO 72 71 GLY 73 72 SER 74 73 ARG 75 74 ASN 76 75 LEU 77 76 CYS 78 77 ASN 79 78 ILE 80 79 PRO 81 80 ALA 82 81 SER 83 82 ALA 84 83 LEU 85 84 LEU 86 85 SER 87 86 SER 88 87 ASP 89 88 ILE 90 89 THR 91 90 ALA 92 91 SER 93 92 VAL 94 93 ASN 95 94 CYS 96 95 ALA 97 96 LYS 98 97 LYS 99 98 ILE 100 99 VAL 101 100 SER 102 101 ASP 103 102 GLY 104 103 ASN 105 104 GLY 106 105 MET 107 106 ASN 108 107 ALA 109 108 TRP 110 109 VAL 111 110 ALA 112 111 TRP 113 112 ARG 114 113 ASN 115 114 ARG 116 115 CYS 117 116 LYS 118 117 GLY 119 118 THR 120 119 ASP 121 120 VAL 122 121 GLN 123 122 ALA 124 123 TRP 125 124 ILE 126 125 ARG 127 126 GLY 128 127 CYS 129 128 ARG 130 129 LEU 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 SWISS-PROT P00698 'Lysozyme C precursor (1,4-beta-N-acetylmuramidase C) (Allergen Gal d 4) (Allergen Gal d IV)' 99.23 147 98.45 98.45 2.46e-68 GenBank AAL69327 'egg white lysozyme [Gallus gallus]' 99.23 147 98.45 98.45 2.46e-68 GenBank AAA48943 'lysozyme (' 99.23 147 98.45 98.45 2.46e-68 PDB 8LYZ 'An X-Ray Study Of The Structure And Binding Properties Of Iodine-Inactivated Lysozyme' 99.23 129 98.45 98.45 5.95e-68 PDB 7LYZ 'Protein Model Building By The Use Of A Constrained- Restrained Least-Squares Procedure' 99.23 129 98.45 98.45 5.95e-68 PDB 6LYZ 'Real-Space Refinement Of The Structure Of Hen Egg-White Lysozyme' 99.23 129 98.45 98.45 5.95e-68 PDB 6LYT 'Comparison Of Radiation-Induced Decay And Structure Refinement From X-Ray Data Collected From Lysozyme Crystals At Low And Ambient Temperatures' 99.23 129 98.45 98.45 5.95e-68 PDB 5LYZ 'Real-Space Refinement Of The Structure Of Hen Egg-White Lysozyme' 99.23 129 98.45 98.45 5.95e-68 PDB 5LYT 'Comparison Of Radiation-Induced Decay And Structure Refinement From X-Ray Data Collected From Lysozyme Crystals At Low And Ambient Temperatures' 99.23 129 98.45 98.45 5.95e-68 PDB 5LYM 'Studies Of Monoclinic Hen Egg White Lysozyme. Iv. X-Ray Refinement At 1.8 Angstrom Resolution And A Comparison Of The Variable Regions In The Polymorphic Forms' 99.23 129 98.45 98.45 5.95e-68 PDB 4LZT 'Atomic Resolution Refinement Of Triclinic Hew Lysozyme At 295k' 99.23 129 98.45 98.45 5.95e-68 PDB 4LYZ 'Real-Space Refinement Of The Structure Of Hen Egg-White Lysozyme' 99.23 129 98.45 98.45 5.95e-68 PDB 4LYT 'Comparison Of Radiation-Induced Decay And Structure Refinement From X-Ray Data Collected From Lysozyme Crystals At Low And Ambient Temperatures' 99.23 129 98.45 98.45 5.95e-68 PDB 4LYO 'Cross-Linked Chicken Lysozyme Crystal In Neat Acetonitrile, Then Back-Soaked In Water' 99.23 129 98.45 98.45 5.95e-68 PDB 4LYM 'Crystal Structure Of Low Humidity Tetragonal Lysozyme At 2.1-Angstroms Resolution. Variability In Hydration Shell And Its Structural Consequences' 99.23 129 98.45 98.45 5.95e-68 PDB 3LZT 'Refinement Of Triclinic Lysozyme At Atomic Resolution' 99.23 129 98.45 98.45 5.95e-68 PDB 3LYZ 'Real-Space Refinement Of The Structure Of Hen Egg-White Lysozyme' 99.23 129 98.45 98.45 5.95e-68 PDB 3LYT 'Comparison Of Radiation-Induced Decay And Structure Refinement From X-Ray Data Collected From Lysozyme Crystals At Low And Ambient Temperatures' 99.23 129 98.45 98.45 5.95e-68 PDB 3LYO 'Cross-Linked Chicken Lysozyme Crystal In 95% Acetonitrile- Water' 99.23 129 98.45 98.45 5.95e-68 PDB 3LYM 'Crystal Structure Of Hen Egg-White Lysozyme At A Hydrostatic Pressure Of 1000 Atmospheres' 99.23 129 98.45 98.45 5.95e-68 PDB 3HFM 'Structure Of An Antibody-Antigen Complex. Crystal Structure Of The HyHEL-10 Fab-Lysozyme Complex' 99.23 129 98.45 98.45 5.95e-68 PDB 3D9A 'High Resolution Crystal Structure Structure Of Hyhel10 Fab Complexed To Hen Egg Lysozyme' 99.23 129 98.45 98.45 5.95e-68 PDB 3B6L 'Crystal Structure Of Lysozyme Folded In Sds And 2-Methyl-2, 4-Pentanediol' 99.23 147 98.45 98.45 2.46e-68 PDB 2Z19 'Phase Transition Of Monoclinic Lysozyme Crystal Soaked In A Saturated Nacl Solution' 99.23 129 98.45 98.45 5.95e-68 PDB 2Z18 'Phase Transition Of Monoclinic Lysozyme Crystal Soaked In A 10% Nacl Solution' 99.23 129 98.45 98.45 5.95e-68 PDB 2Z12 'Structure Of The Transformed Monoclinic Lysozyme By Controlled Dehydration' 99.23 129 98.45 98.45 5.95e-68 PDB 2YVB 'High Resolution X-Ray Crystal Structure Of Tetragonal Hen Egg White Lysozyme' 99.23 129 98.45 98.45 5.95e-68 PDB 2YSS 'Crystal Structure Of Humanized Hyhel-10 Fv Mutant(Hq39kw47y)-Hen Lysozyme Complex' 99.23 129 98.45 98.45 5.95e-68 PDB 2VB1 'Hewl At 0.65 Angstrom Resolution' 99.23 129 98.45 98.45 5.95e-68 PDB 2Q0M 'Tricarbonylmanganese(I)-Lysozyme Complex : A Structurally Characterized Organometallic Protein' 99.23 129 98.45 98.45 5.95e-68 PDB 2PC2 'Lysozyme Cocrystallized With Tris-Dipicolinate Eu Complex' 99.23 129 98.45 98.45 5.95e-68 PDB 2LZT 'Refinement Of Triclinic Lysozyme. Ii. The Method Of Stereochemically Restrained Least-Squares' 99.23 129 98.45 98.45 5.95e-68 PDB 2LZH 'The Structures Of The Monoclinic And Orthorhombic Forms Of Hen Egg-White Lysozyme At 6 Angstroms Resolution.' 99.23 129 98.45 98.45 5.95e-68 PDB 2LYZ 'Real-Space Refinement Of The Structure Of Hen Egg-White Lysozyme' 99.23 129 98.45 98.45 5.95e-68 PDB 2LYO 'Cross-Linked Chicken Lysozyme Crystal In 90% Acetonitrile- Water' 99.23 129 98.45 98.45 5.95e-68 PDB 2LYM 'Crystal Structure Of Hen Egg-White Lysozyme At A Hydrostatic Pressure Of 1000 Atmospheres' 99.23 129 98.45 98.45 5.95e-68 PDB 2I6Z 'X-Ray Diffraction Studies Of Adducts Between Anticancer Platinum Drugs And Hen Egg White Lysozyme' 99.23 129 98.45 98.45 5.95e-68 PDB 2I26 'Crystal Structure Analysis Of The Nurse Shark New Antigen Receptor Ancestral Variable Domain In Complex With Lysozyme' 99.23 129 98.45 98.45 5.95e-68 PDB 2I25 'Crystal Structure Analysis Of The Nurse Shark New Antigen Receptor Pbla8 Variable Domain In Complex With Lysozyme' 99.23 129 98.45 98.45 5.95e-68 PDB 2HUB 'Structure Of Hen Egg-White Lysozyme Determined From Crystals Grown In Ph 7.5' 99.23 129 98.45 98.45 5.95e-68 PDB 2HU3 'Parent Structure Of Hen Egg White Lysozyme Grown In Acidic Ph 4.8. Refinement For Comparison With Crosslinked Molecules Of Lysozyme' 99.23 129 98.45 98.45 5.95e-68 PDB 2HU1 'Crystal Structure Analysis Of Hen Egg White Lyszoyme' 99.23 129 98.45 98.45 5.95e-68 PDB 2HTX 'Crystal Structure Analysis Of Hen Egg White Lysozyme Crosslinked By Polymerized Glutaraldehyde In Acidic Environment' 99.23 129 98.45 98.45 5.95e-68 PDB 2HSO 'Multipattern Rietveld Refinement With Protein Powder Data: An Approach To Higher Resolution' 99.23 129 98.45 98.45 5.95e-68 PDB 2HS9 'Multipattern Rietveld Refinement With Protein Powder Data: An Approach To Higher Resolution' 99.23 129 98.45 98.45 5.95e-68 PDB 2HS7 'Multipattern Rietveld Refinement With Protein Powder Data: An Approach To Higher Resolution' 99.23 129 98.45 98.45 5.95e-68 PDB 2H9K 'Structure Of Hen Egg White Lysozyme Soaked With Ni-Cyclam' 99.23 129 98.45 98.45 5.95e-68 PDB 2H9J 'Structure Of Hen Egg White Lysozyme Soaked With Ni2- Xylylbicyclam' 99.23 129 98.45 98.45 5.95e-68 PDB 2G4Q 'Anomalous Substructure Of Lysozyme At Ph 8.0' 99.23 129 98.45 98.45 5.95e-68 PDB 2G4P 'Anomalous Substructure Of Lysozyme At Ph 4.5' 99.23 129 98.45 98.45 5.95e-68 PDB 2FBB 'Crystal Structure Analysis Of Hexagonal Lysozyme' 99.23 129 98.45 98.45 5.95e-68 PDB 2F4G 'Triclinic Cross-Linked Lysozyme Soaked In Bromoethanol 1m' 99.23 129 98.45 98.45 5.95e-68 PDB 2F4A 'Triclinic Cross-Linked Lysozyme Soaked With Thiourea 1.5m' 99.23 129 98.45 98.45 5.95e-68 PDB 2F30 'Triclinic Cross-Linked Lysozyme Soaked With 4.5m Urea' 99.23 129 98.45 98.45 5.95e-68 PDB 2F2N 'Triclinic Hen Egg Lysozyme Cross-Linked By Glutaraldehyde' 99.23 129 98.45 98.45 5.95e-68 PDB 2EPE 'Crystal Structure Analysis Of Hen Egg White Lysozyme Grown By Capillary Method' 99.23 129 98.45 98.45 5.95e-68 PDB 2EKS 'Crystal Structure Of Humanized Hyhel-10 Fv-Hen Lysozyme Complex' 99.23 129 98.45 98.45 5.95e-68 PDB 2EIZ 'Crystal Structure Of Humanized Hyhel-10 Fv Mutant(Hw47y)- Hen Lysozyme Complex' 99.23 129 98.45 98.45 5.95e-68 PDB 2DQJ 'Crystal Structure Of Hyhel-10 Fv (Wild-Type) Complexed With Hen Egg Lysozyme At 1.8a Resolution' 99.23 129 98.45 98.45 5.95e-68 PDB 2DQI 'Crystal Structure Of Hyhel-10 Fv Mutant (Ly50a) Complexed With Hen Egg Lysozyme' 99.23 129 98.45 98.45 5.95e-68 PDB 2DQH 'Crystal Structure Of Hyhel-10 Fv Mutant (Hy58a) Complexed With Hen Egg Lysozyme' 99.23 129 98.45 98.45 5.95e-68 PDB 2DQG 'Crystal Structure Of Hyhel-10 Fv Mutant (Hy53f) Complexed With Hen Egg Lysozyme' 99.23 129 98.45 98.45 5.95e-68 PDB 2DQF 'Crystal Structure Of Hyhel-10 Fv Mutant (Y33ay53a) Complexed With Hen Egg Lysozyme' 99.23 129 98.45 98.45 5.95e-68 PDB 2DQE 'Crystal Structure Of Hyhel-10 Fv Mutant (Hy53a) Complexed With Hen Egg Lysozyme' 99.23 129 98.45 98.45 5.95e-68 PDB 2DQD 'Crystal Structure Of Hyhel-10 Fv Mutant (Hy50f) Complexed With Hen Egg Lysozyme' 99.23 129 98.45 98.45 5.95e-68 PDB 2DQC 'Crystal Structure Of Hyhel-10 Fv Mutant(Hy33f) Complexed With Hen Egg Lysozyme' 99.23 129 98.45 98.45 5.95e-68 PDB 2D91 'Structure Of Hyper-Vil-Lysozyme' 99.23 129 98.45 98.45 5.95e-68 PDB 2D6B 'Novel Bromate Species Trapped Within A Protein Crystal' 99.23 129 98.45 98.45 5.95e-68 PDB 2D4K 'Monoclinic Hen Egg-White Lysozyme Crystallized At 313k' 99.23 129 98.45 98.45 5.95e-68 PDB 2D4J 'Transformed Monoclinic Crystal Of Hen Egg-White Lysozyme From A Heavy Water Solution' 99.23 129 98.45 98.45 5.95e-68 PDB 2D4I 'Monoclinic Hen Egg-White Lysozyme Crystallized At Ph4.5 Form Heavy Water Solution' 99.23 129 98.45 98.45 5.95e-68 PDB 2CGI 'Siras Structure Of Tetragonal Lysosyme Using Derivative Data Collected At The High Energy Remote Holmium Kedge' 99.23 129 98.45 98.45 5.95e-68 PDB 2CDS Lysozyme 99.23 129 98.45 98.45 5.95e-68 PDB 2C8P 'Lysozyme (60sec) And Uv Laser Excited Fluorescence' 99.23 129 98.45 98.45 5.95e-68 PDB 2C8O 'Lysozyme (1sec) And Uv Lasr Excited Fluorescence' 99.23 129 98.45 98.45 5.95e-68 PDB 2BPU 'The Kedge Holmium Derivative Of Hen Egg-White Lysozyme At High Resolution From Single Wavelength Anomalous Diffraction' 99.23 129 98.45 98.45 5.95e-68 PDB 2BLY 'Hewl After A High Dose X-Ray "burn"' 99.23 129 98.45 98.45 5.95e-68 PDB 2BLX 'Hewl Before A High Dose X-Ray "burn"' 99.23 129 98.45 98.45 5.95e-68 PDB 2B5Z 'Hen Lysozyme Chemically Glycosylated' 99.23 129 98.45 98.45 5.95e-68 PDB 2AUB 'Lysozyme Structure Derived From Thin-Film-Based Crystals' 99.23 129 98.45 98.45 5.95e-68 PDB 2A7F 'On The Routine Use Of Soft X-Rays In Macromolecular Crystallography, Part Iii- The Optimal Data Collection Wavelength' 99.23 129 98.45 98.45 5.95e-68 PDB 2A7D 'On The Routine Use Of Soft X-Rays In Macromolecular Crystallography, Part Iii- The Optimal Data Collection Wavelength' 99.23 129 98.45 98.45 5.95e-68 PDB 2A6U 'Ph Evolution Of Tetragonal Hewl At 4 Degrees Celcius.' 99.23 129 98.45 98.45 5.95e-68 PDB 1ZVY 'Crystal Structure Of The Vhh D3-L11 In Complex With Hen Egg White Lysozyme' 99.23 129 98.45 98.45 5.95e-68 PDB 1ZVH 'Crystal Stucture Of The Vhh Domain D2-L24 In Complex With Hen Egg White Lysozyme' 99.23 129 98.45 98.45 5.95e-68 PDB 1ZV5 'Crystal Structure Of The Variable Domain Of The Camelid Heavy-Chain Antibody D2-L29 In Complex With Hen Egg White Lysozyme' 99.23 129 98.45 98.45 5.95e-68 PDB 1ZMY 'Cabbcii-10 Vhh Framework With Cdr Loops Of Cablys3 Grafted On It And In Complex With Hen Egg White Lysozyme' 99.23 129 98.45 98.45 5.95e-68 PDB 1Z55 'Effect Of Alcohols On Protein Hydration' 99.23 129 98.45 98.45 5.95e-68 PDB 1YQV 'The Crystal Structure Of The Antibody Fab Hyhel5 Complex With Lysozyme At 1.7a Resolution' 99.23 129 98.45 98.45 5.95e-68 PDB 1YL1 'Effect Of Alcohols On Protein Hydration' 99.23 129 98.45 98.45 5.95e-68 PDB 1YL0 'Effect Of Alcohols On Protein Hydration' 99.23 129 98.45 98.45 5.95e-68 PDB 1YKZ 'Effect Of Alcohols On Protein Hydration' 99.23 129 98.45 98.45 5.95e-68 PDB 1YKY 'Effect Of Alcohols On Protein Hydration' 99.23 129 98.45 98.45 5.95e-68 PDB 1YKX 'Effect Of Alcohols On Protein Hydration' 99.23 129 98.45 98.45 5.95e-68 PDB 1YIL 'Structure Of Hen Egg White Lysozyme Soaked With Cu2- Xylylbicyclam' 99.23 129 98.45 98.45 5.95e-68 PDB 1YIK 'Structure Of Hen Egg White Lysozyme Soaked With Cu-Cyclam' 99.23 129 98.45 98.45 5.95e-68 PDB 1XGU 'Structure For Antibody Hyhel-63 Y33f Mutant Complexed With Hen Egg Lysozyme' 99.23 129 98.45 98.45 5.95e-68 PDB 1XGT 'Structure For Antibody Hyhel-63 Y33l Mutant Complexed With Hen Egg Lysozyme' 99.23 129 98.45 98.45 5.95e-68 PDB 1XGR 'Structure For Antibody Hyhel-63 Y33i Mutant Complexed With Hen Egg Lysozyme' 99.23 129 98.45 98.45 5.95e-68 PDB 1XGQ 'Structure For Antibody Hyhel-63 Y33v Mutant Complexed With Hen Egg Lysozyme' 99.23 129 98.45 98.45 5.95e-68 PDB 1XGP 'Structure For Antibody Hyhel-63 Y33a Mutant Complexed With Hen Egg Lysozyme' 99.23 129 98.45 98.45 5.95e-68 PDB 1XFP 'Crystal Structure Of The Cdr2 Germline Reversion Mutant Of Cab-Lys3 In Complex With Hen Egg White Lysozyme' 99.23 129 98.45 98.45 5.95e-68 PDB 1XEK 'The Crystal Structures Of Lysozyme At Very Low Levels Of Hydration' 99.23 129 98.45 98.45 5.95e-68 PDB 1XEJ 'The Crystal Structures Of Lysozyme At Very Low Levels Of Hydration' 99.23 129 98.45 98.45 5.95e-68 PDB 1XEI 'The Crystal Structures Of Lysozyme At Very Low Levels Of Hydration' 99.23 129 98.45 98.45 5.95e-68 PDB 1WTN 'The Structure Of Hew Lysozyme Orthorhombic Crystal Growth Under A High Magnetic Field' 99.23 129 98.45 98.45 5.95e-68 PDB 1WTM 'X-Ray Structure Of Hew Lysozyme Orthorhombic Crystal Formed In The Earth's Magnetic Field' 99.23 129 98.45 98.45 5.95e-68 PDB 1W6Z 'High Energy Tetragonal Lysozyme X-Ray Structure' 99.23 129 98.45 98.45 5.95e-68 PDB 1VFB 'Bound Water Molecules And Conformational Stabilization Help Mediate An Antigen-Antibody Association' 99.23 129 98.45 98.45 5.95e-68 PDB 1VED 'The Crystal Structure Of The Orthorhombic Form Of Hen Egg White Lysozyme At 1.9 Angstroms Resolution In Space' 99.23 129 98.45 98.45 5.95e-68 PDB 1VDT 'The Crystal Structure Of The Tetragonal Form Of Hen Egg White Lysozyme At 1.7 Angstroms Resolution Under Basic Conditions In Space' 99.23 129 98.45 98.45 5.95e-68 PDB 1VDS 'The Crystal Structure Of The Tetragonal Form Of Hen Egg White Lysozyme At 1.6 Angstroms Resolution In Space' 99.23 129 98.45 98.45 5.95e-68 PDB 1VDQ 'The Crystal Structure Of The Orthorhombic Form Of Hen Egg White Lysozyme At 1.5 Angstroms Resolution' 99.23 129 98.45 98.45 5.95e-68 PDB 1VDP 'The Crystal Structure Of The Monoclinic Form Of Hen Egg White Lysozyme At 1.7 Angstroms Resolution In Space' 99.23 129 98.45 98.45 5.95e-68 PDB 1VAU 'Xenon Derivative Of Hen Egg-White Lysozyme' 99.23 129 98.45 98.45 5.95e-68 PDB 1VAT 'Iodine Derivative Of Hen Egg-White Lysozyme' 99.23 129 98.45 98.45 5.95e-68 PDB 1V7T 'Triclinic Lysozyme With Low Solvent Content Obtained By Phase Transition' 99.23 129 98.45 98.45 5.95e-68 PDB 1V7S 'Triclinic Hen Lysozyme Crystallized At 313k From A D2o Solution' 98.46 129 98.44 98.44 2.03e-67 PDB 1UUZ 'Ivy:a New Family Of Protein' 99.23 129 98.45 98.45 5.95e-68 PDB 1UIH 'Analysis Of The Stabilization Of Hen Lysozyme With The Helix Dipole And Charged Side Chains' 99.23 129 98.45 98.45 5.95e-68 PDB 1UIG 'Analysis Of The Stabilization Of Hen Lysozyme With The Helix Dipole And Charged Side Chains' 99.23 129 98.45 98.45 5.95e-68 PDB 1UCO 'Hen Egg-White Lysozyme, Low Humidity Form' 99.23 129 98.45 98.45 5.95e-68 PDB 1UC0 'Crystal Structure Of Wild-Type Hen-Egg White Lysozyme Singly Labeled With 2',3'-Epoxypropyl Beta-Glycoside Of N- Acetyllactosamine' 99.23 129 98.45 98.45 5.95e-68 PDB 1UA6 'Crystal Structure Of Hyhel-10 Fv Mutant Sfsf Complexed With Hen Egg White Lysozyme Complex' 99.23 129 98.45 98.45 5.95e-68 PDB 1T6V 'Crystal Structure Analysis Of The Nurse Shark New Antigen Receptor (Nar) Variable Domain In Complex With Lysozyme' 99.23 129 98.45 98.45 5.95e-68 PDB 1T3P 'Half-Sandwich Arene Ruthenium(Ii)-Enzyme Complex' 99.23 129 98.45 98.45 5.95e-68 PDB 1SQ2 'Crystal Structure Analysis Of The Nurse Shark New Antigen Receptor (Nar) Variable Domain In Complex With Lyxozyme' 99.23 129 98.45 98.45 5.95e-68 PDB 1SFG 'Binding Of Hexa-N-Acetylchitohexaose: A Powder Diffraction Study' 99.23 129 98.45 98.45 5.95e-68 PDB 1SFB 'Binding Of Penta-N-Acetylchitopentaose To Hew Lysozyme: A Powder Diffraction Study' 99.23 129 98.45 98.45 5.95e-68 PDB 1SF7 'Binding Of Tetra-N-Acetylchitotetraose To Hew Lysozyme: A Powder Diffraction Study' 99.23 129 98.45 98.45 5.95e-68 PDB 1SF6 'Binding Of N,N',N"-Triacetylchitotriose To Hew Lysozyme: A Powder Diffraction Study' 99.23 129 98.45 98.45 5.95e-68 PDB 1SF4 'Binding Of N,N'-Diacetylchitobiose To Hew Lysozyme: A Powder Diffraction Study' 99.23 129 98.45 98.45 5.95e-68 PDB 1RJC 'Crystal Structure Of The Camelid Single Domain Antibody Cab- Lys2 In Complex With Hen Egg White Lysozyme' 99.23 129 98.45 98.45 5.95e-68 PDB 1RI8 'Crystal Structure Of The Camelid Single Domain Antibody 1d2l19 In Complex With Hen Egg White Lysozyme' 99.23 129 98.45 98.45 5.95e-68 PDB 1RFP 'Analysis Of The Stabilization Of Hen Lysozyme With The Helix Dipole And Charged Side Chains' 99.23 129 98.45 98.45 5.95e-68 PDB 1RCM 'Crystal Structure Of A Ubiquitin-Dependent Degradation Substrate: A Three-Disulfide Form Of Lysozyme' 99.23 129 98.45 98.45 5.95e-68 PDB 1QTK 'Crystal Structure Of Hew Lysozyme Under Pressure Of Krypton (55 Bar)' 99.23 129 98.45 98.45 5.95e-68 PDB 1QIO 'Specific Chemical And Structural Damage Caused By Intense Synchrotron Radiation To Hen Egg White Lysozyme' 99.23 129 98.45 98.45 5.95e-68 PDB 1PS5 'Structure Of The Monoclinic C2 Form Of Hen Egg-White Lysozyme At 2.0 Angstroms Resolution' 99.23 129 98.45 98.45 5.95e-68 PDB 1P2C 'Crystal Structure Analysis Of An Anti-Lysozyme Antibody' 99.23 129 98.45 98.45 5.95e-68 PDB 1NDM 'Crystal Structure Of Fab Fragment Of Antibody Hyhel-26 Complexed With Lysozyme' 99.23 129 98.45 98.45 5.95e-68 PDB 1N4F 'Para-Arsanilate Derivative Of Hen Egg-White Lysozyme' 99.23 129 98.45 98.45 5.95e-68 PDB 1MLC 'Monoclonal Antibody Fab D44.1 Raised Against Chicken Egg- White Lysozyme Complexed With Lysozyme' 99.23 129 98.45 98.45 5.95e-68 PDB 1MEL 'Crystal Structure Of A Camel Single-Domain Vh Antibody Fragment In Complex With Lysozyme' 99.23 129 98.45 98.45 5.95e-68 PDB 1LZT 'Refinement Of Triclinic Lysozyme' 99.23 129 98.45 98.45 5.95e-68 PDB 1LZN 'Neutron Structure Of Hen Egg-White Lysozyme' 98.46 129 98.44 98.44 2.13e-67 PDB 1LZH 'The Structures Of The Monoclinic And Orthorhombic Forms Of Hen Egg-White Lysozyme At 6 Angstroms Resolution.' 99.23 129 98.45 98.45 5.95e-68 PDB 1LZC 'Dissection Of Protein-Carbohydrate Interactions In Mutant Hen Egg-White Lysozyme Complexes And Their Hydrolytic Activity' 99.23 129 98.45 98.45 5.95e-68 PDB 1LZB 'Dissection Of Protein-Carbohydrate Interactions In Mutant Hen Egg-White Lysozyme Complexes And Their Hydrolytic Activity' 99.23 129 98.45 98.45 5.95e-68 PDB 1LZA 'Dissection Of Protein-Carbohydrate Interactions In Mutant Hen Egg-White Lysozyme Complexes And Their Hydrolytic Activity' 99.23 129 98.45 98.45 5.95e-68 PDB 1LZ9 'Anomalous Signal Of Solvent Bromines Used For Phasing Of Lysozyme' 99.23 129 98.45 98.45 5.95e-68 PDB 1LZ8 'Lysozyme Phased On Anomalous Signal Of Sulfurs And Chlorines' 99.23 129 98.45 98.45 5.95e-68 PDB 1LYZ 'Real-Space Refinement Of The Structure Of Hen Egg-White Lysozyme' 99.23 129 98.45 98.45 5.95e-68 PDB 1LYS 'X-Ray Structure Of A Monoclinic Form Of Hen Egg-White Lysozyme Crystallized At 313k. Comparison Of Two Independent Molecules' 99.23 129 98.45 98.45 5.95e-68 PDB 1LYO 'Cross-Linked Lysozyme Crystal In Neat Water' 99.23 129 98.45 98.45 5.95e-68 PDB 1LSG 'Three-Dimensional Structure Of The Platelet Integrin Recognition Segment Of The Fibrinogen Gamma Chain Obtained By Carrier Protein-Driven Crystallization' 100.00 144 98.46 98.46 4.48e-69 PDB 1LSF 'The Influence Of Temperature On Lysozyme Crystals. Structure And Dynamics Of Protein And Water' 99.23 129 98.45 98.45 5.95e-68 PDB 1LSE 'The Influence Of Temperature On Lysozyme Crystals. Structure And Dynamics Of Protein And Water' 99.23 129 98.45 98.45 5.95e-68 PDB 1LSD 'The Influence Of Temperature On Lysozyme Crystals. Structure And Dynamics Of Protein And Water' 99.23 129 98.45 98.45 5.95e-68 PDB 1LSC 'The Influence Of Temperature On Lysozyme Crystals. Structure And Dynamics Of Protein And Water' 99.23 129 98.45 98.45 5.95e-68 PDB 1LSB 'The Influence Of Temperature On Lysozyme Crystals. Structure And Dynamics Of Protein And Water' 99.23 129 98.45 98.45 5.95e-68 PDB 1LSA 'The Influence Of Temperature On Lysozyme Crystals. Structure And Dynamics Of Protein And Water' 99.23 129 98.45 98.45 5.95e-68 PDB 1LPI 'Hew Lysozyme: Trp...Na Cation-Pi Interaction' 99.23 129 98.45 98.45 5.95e-68 PDB 1LMA 'Protein Hydration And Water Structure: X-Ray Analysis Of A Closely Packed Protein Crystal With Very Low Solvent Content' 99.23 129 98.45 98.45 5.95e-68 PDB 1LKS 'Hen Egg White Lysozyme Nitrate' 99.23 129 98.45 98.45 5.95e-68 PDB 1LKR 'Monoclinic Hen Egg White Lysozyme Iodide' 99.23 129 98.45 98.45 5.95e-68 PDB 1LJK 'Crystal Structure Of Monoclinic Lysozyme Grown In Presence Of 15% Trehalose' 99.23 129 98.45 98.45 5.95e-68 PDB 1LJJ 'Crystal Structure Of Monoclinic Lysozyme Grown In Presence Of 10% Trehalose' 99.23 129 98.45 98.45 5.95e-68 PDB 1LJI 'Crystal Structure Of Monoclinic Lysozyme Grown In Presence 10% Sorbitol' 99.23 129 98.45 98.45 5.95e-68 PDB 1LJH 'Crystal Structure Of Monoclinic Lysozyme Grown In Presence Of 5% Glycerol' 99.23 129 98.45 98.45 5.95e-68 PDB 1LJG 'Crystal Structure Of Monoclinic Lysozyme Grown In Presence Of 5% Glycerol' 99.23 129 98.45 98.45 5.95e-68 PDB 1LJF 'Crystal Structure Of Monoclinic Lysozyme Grown In Presence Of 10% Sucrose' 99.23 129 98.45 98.45 5.95e-68 PDB 1LJE 'Crystal Structure Of Monoclinic Lysozyme Grown In Presence Of 10% Sucrose' 99.23 129 98.45 98.45 5.95e-68 PDB 1LJ4 'Crystal Structure Of Monoclinic Lysozyme Grown At Ph 4.6' 99.23 129 98.45 98.45 5.95e-68 PDB 1LJ3 'Crystal Structure Of Monoclinic Lysozyme Grown At Ph 4.6' 99.23 129 98.45 98.45 5.95e-68 PDB 1LCN 'Monoclinic Hen Egg White Lysozyme, Thiocyanate Complex' 99.23 129 98.45 98.45 5.95e-68 PDB 1KIR 'Fv Mutant Y(A 50)s (Vl Domain) Of Mouse Monoclonal Antibody D1.3 Complexed With Hen Egg White Lysozyme' 99.23 129 98.45 98.45 5.95e-68 PDB 1KIQ 'Fv Mutant Y(B 101)f (Vh Domain) Of Mouse Monoclonal Antibody D1.3 Complexed With Hen Egg White Lysozyme' 99.23 129 98.45 98.45 5.95e-68 PDB 1KIP 'Fv Mutant Y(B 32)a (Vh Domain) Of Mouse Monoclonal Antibody D1.3 Complexed With Hen Egg White Lysozyme' 99.23 129 98.45 98.45 5.95e-68 PDB 1JTT 'Degenerate Interfaces In Antigen-Antibody Complexes' 99.23 129 98.45 98.45 5.95e-68 PDB 1JTO 'Degenerate Interfaces In Antigen-Antibody Complexes' 99.23 129 98.45 98.45 5.95e-68 PDB 1JPO 'Low Temperature Orthorhombic Lysozyme' 99.23 129 98.45 98.45 5.95e-68 PDB 1JJ3 'Crystal Structure Of Monoclinic Lysozyme Grown At Ph 4.6' 99.23 129 98.45 98.45 5.95e-68 PDB 1JJ1 'Crystal Structure Of Orthorhombic Lysozyme Grown At Ph 4.6 In Presence Of 5% Sorbitol' 99.23 129 98.45 98.45 5.95e-68 PDB 1JJ0 'Crystal Structure Of Tetragonal Lysozyme Grown In Presence Of 30% Sucrose' 99.23 129 98.45 98.45 5.95e-68 PDB 1JIY 'Crystal Structure Of Tetragonal Lysozyme Grown In Presence 20% Sorbitol' 99.23 129 98.45 98.45 5.95e-68 PDB 1JIT 'Crystal Structure Of Tetragonal Lysozyme Grown In Presence 30% Trehalose' 99.23 129 98.45 98.45 5.95e-68 PDB 1JIS 'Crystal Structure Of Tetragonal Lysozyme Grown At Ph 4.6' 99.23 129 98.45 98.45 5.95e-68 PDB 1JA7 'Binding Of N-Acetylglucosamine To Chicken Egg Lysozyme: A Powder Diffraction Study' 99.23 129 98.45 98.45 5.95e-68 PDB 1JA6 'Binding Of N-Acetylglucosamine To Chicken Egg Lysozyme: A Powder Diffraction Study' 99.23 129 98.45 98.45 5.95e-68 PDB 1JA4 'Binding Of N-Acetylglucosamine To Chicken Egg Lysozyme: A Powder Diffraction Study' 99.23 129 98.45 98.45 5.95e-68 PDB 1JA2 'Binding Of N-Acetylglucosamine To Chicken Egg Lysozyme: A Powder Diffraction Study' 99.23 129 98.45 98.45 5.95e-68 PDB 1J1X 'Crystal Structure Of Hyhel-10 Fv Mutant Ls93a Complexed With Hen Egg White Lysozyme' 99.23 129 98.45 98.45 5.95e-68 PDB 1J1P 'Crystal Structure Of Hyhel-10 Fv Mutant Ls91a Complexed With Hen Egg White Lysozyme' 99.23 129 98.45 98.45 5.95e-68 PDB 1J1O 'Crystal Structure Of Hyhel-10 Fv Mutant Ly50f Complexed With Hen Egg White Lysozyme' 99.23 129 98.45 98.45 5.95e-68 PDB 1IO5 'Hydrogen And Hydration Of Hen Egg-White Lysozyme Determined By Neutron Diffraction' 98.46 129 98.44 98.44 2.13e-67 PDB 1IEE 'Structure Of Tetragonal Hen Egg White Lysozyme At 0.94 A From Crystals Grown By The Counter-Diffusion Method' 99.23 129 98.45 98.45 5.95e-68 PDB 1IC7 'Crystal Structure Of Hyhel-10 Fv Mutant(Hd32a99a)-Hen Lysozyme Complex' 99.23 129 98.45 98.45 5.95e-68 PDB 1IC5 'Crystal Structure Of Hyhel-10 Fv Mutant(Hd99a)-Hen Lysozyme Complex' 99.23 129 98.45 98.45 5.95e-68 PDB 1IC4 'Crystal Structure Of Hyhel-10 Fv Mutant(Hd32a)-Hen Lysozyme Complex' 99.23 129 98.45 98.45 5.95e-68 PDB 1HSX 'Lysozyme Grown At Basic Ph And Its Low Humidity Variant' 99.23 129 98.45 98.45 5.95e-68 PDB 1HSW 'Lysozyme (Mucopeptide N-Acetylmuramyl Hydrolase)' 99.23 129 98.45 98.45 5.95e-68 PDB 1HF4 'Structural Effects Of Monovalent Anions On Polymorphic Lysozyme Crystals' 99.23 129 98.45 98.45 5.95e-68 PDB 1HEW 'Refinement Of An Enzyme Complex With Inhibitor Bound At Partial Occupancy. Hen Egg-White Lysozyme And Tri-N- Acetylchitotriose At 1.75 Angstroms Resolution' 99.23 129 98.45 98.45 5.95e-68 PDB 1HEL 'Structural And Thermodynamic Analysis Of Compensating Mutations Within The Core Of Chicken Egg White Lysozyme' 99.23 129 98.45 98.45 5.95e-68 PDB 1HC0 'Structure Of Lysozyme With Periodate' 99.23 129 98.45 98.45 5.95e-68 PDB 1H87 'Gadolinium Derivative Of Tetragonal Hen Egg-White Lysozyme At 1.7 A Resolution' 99.23 129 98.45 98.45 5.95e-68 PDB 1GXX 'Solution Structure Of Lysozyme At Low And High Pressure' 99.23 129 98.45 98.45 5.95e-68 PDB 1GXV 'Solution Structure Of Lysozyme At Low And High Pressure' 99.23 129 98.45 98.45 5.95e-68 PDB 1GWD 'Tri-Iodide Derivative Of Hen Egg-White Lysozyme' 99.23 129 98.45 98.45 5.95e-68 PDB 1GPQ 'Structure Of Ivy Complexed With Its Target, Hewl' 99.23 129 98.45 98.45 5.95e-68 PDB 1G7M 'Crystal Structure Of Hen Egg White Lysozyme (Hel) Complexed With The Mutant Anti-Hel Monoclonal Antibody D1.3 (Vlw92v)' 99.23 129 98.45 98.45 5.95e-68 PDB 1G7L 'Crystal Structure Of Hen Egg White Lysozyme (Hel) Complexed With The Mutant Anti-Hel Monoclonal Antibody D1.3 (Vlw92s)' 99.23 129 98.45 98.45 5.95e-68 PDB 1G7J 'Crystal Structure Of Hen Egg White Lysozyme (Hel) Complexed With The Mutant Anti-Hel Monoclonal Antibody D1.3 (Vlw92h)' 99.23 129 98.45 98.45 5.95e-68 PDB 1G7I 'Crystal Structure Of Hen Egg White Lysozyme (Hel) Complexed With The Mutant Anti-Hel Monoclonal Antibody D1.3 (Vlw92f)' 99.23 129 98.45 98.45 5.95e-68 PDB 1G7H 'Crystal Structure Of Hen Egg White Lysozyme (Hel) Complexed With The Mutant Anti-Hel Monoclonal Antibody D1.3(Vlw92a)' 99.23 129 98.45 98.45 5.95e-68 PDB 1FDL 'Crystallographic Refinement Of The Three-Dimensional Structure Of The Fab D1.3-Lysozyme Complex At 2.5- Angstroms Resolution' 99.23 129 98.45 98.45 5.95e-68 PDB 1F10 'Crystal Structure Of Orthorhombic Lysozyme Grown At Ph 6.5 At 88% Relative Humidity' 99.23 129 98.45 98.45 5.95e-68 PDB 1F0W 'Crystal Structure Of Orthorhombic Lysozyme Grown At Ph 6.5' 99.23 129 98.45 98.45 5.95e-68 PDB 1E8L 'Nmr Solution Structure Of Hen Lysozyme' 99.23 129 98.45 98.45 5.95e-68 PDB 1DQJ 'Crystal Structure Of The Anti-Lysozyme Antibody Hyhel-63 Complexed With Hen Egg White Lysozyme' 99.23 129 98.45 98.45 5.95e-68 PDB 1DPX 'Structure Of Hen Egg-White Lysozyme' 99.23 129 98.45 98.45 5.95e-68 PDB 1DPW 'Structure Of Hen Egg-White Lysozyme In Complex With Mpd' 99.23 129 98.45 98.45 5.95e-68 PDB 1C10 'Crystal Structure Of Hew Lysozyme Under Pressure Of Xenon (8 Bar)' 99.23 129 98.45 98.45 5.95e-68 PDB 1C08 'Crystal Structure Of Hyhel-10 Fv-Hen Lysozyme Complex' 99.23 129 98.45 98.45 5.95e-68 PDB 1BWJ 'The 1.8 A Structure Of Microgravity Grown Tetragonal Hen Egg White Lysozyme' 99.23 129 98.45 98.45 5.95e-68 PDB 1BWI 'The 1.8 A Structure Of Microbatch Oil Drop Grown Tetragonal Hen Egg White Lysozyme' 99.23 129 98.45 98.45 5.95e-68 PDB 1BWH 'The 1.8 A Structure Of Ground Control Grown Tetragonal Hen Egg White Lysozyme' 99.23 129 98.45 98.45 5.95e-68 PDB 1BVX 'The 1.8 A Structure Of Gel Grown Tetragonal Hen Egg White Lysozyme' 99.23 129 98.45 98.45 5.95e-68 PDB 1BVK 'Humanized Anti-Lysozyme Fv Complexed With Lysozyme' 99.23 129 98.45 98.45 5.95e-68 PDB 1BHZ 'Low Temperature Middle Resolution Structure Of Hen Egg White Lysozyme From Masc Data' 99.23 129 98.45 98.45 5.95e-68 PDB 1BGI 'Orthorhombic Lysozyme Crystallized At High Temperature (310k)' 99.23 129 98.45 98.45 5.95e-68 PDB 1B2K 'Structural Effects Of Monovalent Anions On Polymorphic Lysozyme Crystals' 99.23 129 98.45 98.45 5.95e-68 PDB 1B0D 'Structural Effects Of Monovalent Anions On Polymorphic Lysozyme Crystals' 99.23 129 98.45 98.45 5.95e-68 PDB 1AZF 'Chicken Egg White Lysozyme Crystal Grown In Bromide Solution' 99.23 129 98.45 98.45 5.95e-68 PDB 1AKI 'The Structure Of The Orthorhombic Form Of Hen Egg-White Lysozyme At 1.5 Angstroms Resolution' 99.23 129 98.45 98.45 5.95e-68 PDB 194L 'The 1.40 A Structure Of Spacehab-01 Hen Egg White Lysozyme' 99.23 129 98.45 98.45 5.95e-68 PDB 193L 'The 1.33 A Structure Of Tetragonal Hen Egg White Lysozyme' 99.23 129 98.45 98.45 5.95e-68 BMRB 5069 'hen egg white lysozyme variant' 100.00 130 98.46 98.46 1.21e-68 BMRB 5068 'hen egg white lysozyme' 100.00 130 98.46 98.46 9.56e-69 BMRB 4943 'Chicken Egg White Lysozyme' 99.23 133 98.45 98.45 5.52e-68 BMRB 4562 'hen egg white lysozyme' 99.23 129 98.45 98.45 5.95e-68 BMRB 1093 lysozyme 99.23 129 98.45 98.45 5.95e-68 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species _Tissue $HEWL Chicken 9031 Eukaryota Metazoa Gallus gallus 'egg white' stop_ save_ ######################### # Experimental source # ######################### save_experimental_source _Saveframe_category experimental_source loop_ _Mol_label _Production_method _Host_organism_name_common _Genus _Species _Strain _Vector_type _Vector_name $HEWL 'recombinant technology' 'E. coli' Escherichia coli AD18 plasmid . stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Concentration_min_value _Concentration_max_value _Isotopic_labeling $HEWL . mM 0.3 1.0 [U-15N] stop_ save_ ############################ # Computer software used # ############################ save_XWINNMR _Saveframe_category software _Name XWINNMR _Version 2.6 _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model DRX _Field_strength 600 _Details . save_ ############################# # NMR applied experiments # ############################# save_DQF-COSY_1 _Saveframe_category NMR_applied_experiment _Experiment_name DQF-COSY _Sample_label . save_ save_NOESY_2 _Saveframe_category NMR_applied_experiment _Experiment_name NOESY _Sample_label . save_ save_HOHAHA_3 _Saveframe_category NMR_applied_experiment _Experiment_name HOHAHA _Sample_label . save_ save_15N_3D-NOESY-HSQC_4 _Saveframe_category NMR_applied_experiment _Experiment_name '15N 3D-NOESY-HSQC' _Sample_label . save_ save_15N_3D-TOCSY-HSQC_5 _Saveframe_category NMR_applied_experiment _Experiment_name '15N 3D-TOCSY-HSQC' _Sample_label . save_ save_1H-15N_HSQC_6 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-15N HSQC' _Sample_label . save_ save_15N_3D-HSQC-NOESY-HSQC_7 _Saveframe_category NMR_applied_experiment _Experiment_name '15N 3D-HSQC-NOESY-HSQC' _Sample_label . save_ save_NMR_spec_expt__0_1 _Saveframe_category NMR_applied_experiment _Experiment_name DQF-COSY _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_2 _Saveframe_category NMR_applied_experiment _Experiment_name NOESY _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_3 _Saveframe_category NMR_applied_experiment _Experiment_name HOHAHA _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_4 _Saveframe_category NMR_applied_experiment _Experiment_name '15N 3D-NOESY-HSQC' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_5 _Saveframe_category NMR_applied_experiment _Experiment_name '15N 3D-TOCSY-HSQC' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_6 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-15N HSQC' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_7 _Saveframe_category NMR_applied_experiment _Experiment_name '15N 3D-HSQC-NOESY-HSQC' _BMRB_pulse_sequence_accession_number . _Details . save_ ####################### # Sample conditions # ####################### save_EX-cond_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 3.8 0.1 na temperature 298 0.1 K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference _Saveframe_category chemical_shift_reference _Details . loop_ _Mol_common_name _Atom_type _Atom_isotope_number _Atom_group _Chem_shift_units _Chem_shift_value _Reference_method _Reference_type _External_reference_sample_geometry _External_reference_location _External_reference_axis _Indirect_shift_ratio DSS H 1 'methyl protons' ppm 0.0 external 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_ _Experiment_label DQF-COSY NOESY HOHAHA '15N 3D-NOESY-HSQC' '15N 3D-TOCSY-HSQC' '1H-15N HSQC' '15N 3D-HSQC-NOESY-HSQC' stop_ loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $EX-cond_1 _Chem_shift_reference_set_label $chemical_shift_reference _Mol_system_component_name 'hen lysozyme Cys mutants, C64A/C80A' _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 2 LYS H H 8.84 0.02 1 2 1 2 LYS HA H 4.37 0.02 1 3 1 2 LYS HB2 H 1.75 0.02 2 4 1 2 LYS HB3 H 1.50 0.02 2 5 2 3 VAL H H 8.87 0.02 1 6 2 3 VAL HA H 4.84 0.02 1 7 2 3 VAL HB H 2.01 0.02 1 8 2 3 VAL HG1 H 1.04 0.02 2 9 2 3 VAL HG2 H 0.94 0.02 2 10 3 4 PHE H H 8.69 0.02 1 11 3 4 PHE HA H 4.26 0.02 1 12 3 4 PHE HB2 H 3.19 0.02 2 13 3 4 PHE HB3 H 2.67 0.02 2 14 3 4 PHE HD1 H 6.97 0.02 1 15 3 4 PHE HD2 H 6.97 0.02 1 16 3 4 PHE HE1 H 7.20 0.02 1 17 3 4 PHE HE2 H 7.20 0.02 1 18 3 4 PHE HZ H 7.48 0.02 1 19 4 5 GLY H H 8.46 0.02 1 20 4 5 GLY HA2 H 4.32 0.02 2 21 4 5 GLY HA3 H 3.97 0.02 2 22 5 6 ARG H H 8.58 0.02 1 23 5 6 ARG HA H 3.36 0.02 1 24 5 6 ARG HB2 H 2.08 0.02 2 25 5 6 ARG HD2 H 3.87 0.02 2 26 5 6 ARG HE H 7.58 0.02 1 27 6 7 CYS H H 8.71 0.02 1 28 6 7 CYS HA H 4.74 0.02 1 29 6 7 CYS HB2 H 3.22 0.02 2 30 6 7 CYS HB3 H 2.78 0.02 2 31 7 8 GLU H H 8.29 0.02 1 32 7 8 GLU HA H 4.10 0.02 1 33 7 8 GLU HB2 H 2.30 0.02 2 34 7 8 GLU HG2 H 2.34 0.02 2 35 7 8 GLU HG3 H 2.52 0.02 2 36 8 9 LEU H H 8.65 0.02 1 37 8 9 LEU HA H 3.78 0.02 1 38 8 9 LEU HB2 H 1.61 0.02 2 39 8 9 LEU HB3 H 0.93 0.02 2 40 8 9 LEU HG H 1.54 0.02 1 41 8 9 LEU HD1 H 0.59 0.02 2 42 8 9 LEU HD2 H -0.02 0.02 2 43 9 10 ALA H H 8.44 0.02 1 44 9 10 ALA HA H 3.60 0.02 1 45 9 10 ALA HB H 1.57 0.02 1 46 10 11 ALA H H 8.18 0.02 1 47 10 11 ALA HA H 3.98 0.02 1 48 10 11 ALA HB H 1.54 0.02 1 49 11 12 ALA H H 7.79 0.02 1 50 11 12 ALA HA H 4.27 0.02 1 51 11 12 ALA HB H 1.51 0.02 1 52 12 13 MET H H 9.16 0.02 1 53 12 13 MET HA H 3.45 0.02 1 54 12 13 MET HB2 H 1.91 0.02 2 55 12 13 MET HG2 H 2.76 0.02 2 56 12 13 MET HG3 H 1.34 0.02 2 57 12 13 MET HE H 1.66 0.02 1 58 13 14 LYS H H 8.54 0.02 1 59 13 14 LYS HA H 3.98 0.02 1 60 13 14 LYS HB2 H 2.23 0.02 2 61 13 14 LYS HB3 H 1.94 0.02 2 62 13 14 LYS HD2 H 1.75 0.02 2 63 13 14 LYS HD3 H 3.03 0.02 2 64 14 15 ARG H H 8.25 0.02 1 65 14 15 ARG HA H 4.13 0.02 1 66 14 15 ARG HB2 H 1.98 0.02 2 67 14 15 ARG HG2 H 1.58 0.02 2 68 14 15 ARG HD2 H 3.15 0.02 2 69 14 15 ARG HE H 7.16 0.02 1 70 15 16 HIS H H 7.36 0.02 1 71 15 16 HIS HA H 4.56 0.02 1 72 15 16 HIS HB2 H 3.71 0.02 2 73 15 16 HIS HB3 H 2.57 0.02 2 74 15 16 HIS HD2 H 7.53 0.02 1 75 15 16 HIS HE1 H 8.84 0.02 1 76 16 17 GLY H H 7.63 0.02 1 77 16 17 GLY HA2 H 3.91 0.02 2 78 16 17 GLY HA3 H 4.13 0.02 2 79 17 18 LEU H H 7.16 0.02 1 80 17 18 LEU HA H 3.93 0.02 1 81 17 18 LEU HB2 H 0.74 0.02 2 82 17 18 LEU HB3 H 0.27 0.02 2 83 17 18 LEU HG H 0.69 0.02 1 84 17 18 LEU HD1 H -0.69 0.02 2 85 17 18 LEU HD2 H -0.10 0.02 2 86 18 19 ASP H H 8.82 0.02 1 87 18 19 ASP HA H 4.26 0.02 1 88 18 19 ASP HB2 H 3.02 0.02 2 89 18 19 ASP HB3 H 2.39 0.02 2 90 19 20 ASN H H 8.40 0.02 1 91 19 20 ASN HA H 3.96 0.02 1 92 19 20 ASN HB2 H 2.85 0.02 2 93 19 20 ASN HB3 H 3.06 0.02 2 94 19 20 ASN HD21 H 7.47 0.02 2 95 19 20 ASN HD22 H 6.63 0.02 2 96 20 21 TYR H H 8.13 0.02 1 97 20 21 TYR HA H 4.22 0.02 1 98 20 21 TYR HB2 H 3.06 0.02 2 99 20 21 TYR HB3 H 3.22 0.02 2 100 20 21 TYR HD1 H 7.18 0.02 1 101 20 21 TYR HD2 H 7.18 0.02 1 102 20 21 TYR HE1 H 6.96 0.02 1 103 20 21 TYR HE2 H 6.96 0.02 1 104 21 22 ARG H H 9.02 0.02 1 105 21 22 ARG HA H 3.64 0.02 1 106 21 22 ARG HB2 H 1.90 0.02 2 107 21 22 ARG HB3 H 2.26 0.02 2 108 21 22 ARG HG2 H 1.23 0.02 2 109 21 22 ARG HD2 H 3.08 0.02 2 110 21 22 ARG HE H 7.16 0.02 1 111 22 23 GLY H H 7.62 0.02 1 112 22 23 GLY HA2 H 3.88 0.02 2 113 22 23 GLY HA3 H 3.49 0.02 2 114 23 24 TYR H H 7.68 0.02 1 115 23 24 TYR HA H 4.56 0.02 1 116 23 24 TYR HB2 H 3.30 0.02 2 117 23 24 TYR HB3 H 2.47 0.02 2 118 23 24 TYR HD1 H 7.03 0.02 1 119 23 24 TYR HD2 H 7.03 0.02 1 120 23 24 TYR HE1 H 6.71 0.02 1 121 23 24 TYR HE2 H 6.71 0.02 1 122 24 25 SER H H 9.08 0.02 1 123 24 25 SER HA H 4.51 0.02 1 124 24 25 SER HB2 H 4.21 0.02 2 125 24 25 SER HB3 H 4.37 0.02 2 126 25 26 LEU H H 9.13 0.02 1 127 25 26 LEU HA H 4.39 0.02 1 128 25 26 LEU HB2 H 1.63 0.02 2 129 25 26 LEU HG H 1.60 0.02 1 130 25 26 LEU HD1 H 0.87 0.02 2 131 25 26 LEU HD2 H 1.00 0.02 2 132 26 27 GLY H H 9.65 0.02 1 133 26 27 GLY HA2 H 4.19 0.02 2 134 26 27 GLY HA3 H 3.67 0.02 2 135 27 28 ASN H H 8.20 0.02 1 136 27 28 ASN HA H 4.18 0.02 1 137 27 28 ASN HB2 H 2.88 0.02 2 138 27 28 ASN HB3 H 2.29 0.02 2 139 27 28 ASN HD21 H 7.78 0.02 2 140 28 29 TRP H H 7.19 0.02 1 141 28 29 TRP HA H 3.76 0.02 1 142 28 29 TRP HB2 H 3.26 0.02 2 143 28 29 TRP HD1 H 7.27 0.02 1 144 28 29 TRP HE1 H 9.33 0.02 1 145 28 29 TRP HE3 H 6.66 0.02 1 146 28 29 TRP HZ2 H 7.42 0.02 1 147 28 29 TRP HZ3 H 6.06 0.02 1 148 28 29 TRP HH2 H 6.72 0.02 1 149 29 30 VAL H H 7.58 0.02 1 150 29 30 VAL HA H 3.45 0.02 1 151 29 30 VAL HB H 1.95 0.02 1 152 29 30 VAL HG1 H 1.27 0.02 2 153 29 30 VAL HG2 H 0.94 0.02 2 154 30 31 CYS H H 8.06 0.02 1 155 30 31 CYS HA H 2.51 0.02 1 156 30 31 CYS HB2 H 2.95 0.02 2 157 30 31 CYS HB3 H 2.63 0.02 2 158 31 32 ALA H H 8.15 0.02 1 159 31 32 ALA HA H 3.71 0.02 1 160 31 32 ALA HB H 1.02 0.02 1 161 32 33 ALA H H 7.60 0.02 1 162 32 33 ALA HA H 4.05 0.02 1 163 32 33 ALA HB H 1.32 0.02 1 164 33 34 LYS H H 7.99 0.02 1 165 33 34 LYS HA H 2.54 0.02 1 166 33 34 LYS HB2 H 1.08 0.02 2 167 33 34 LYS HG2 H 0.44 0.02 2 168 33 34 LYS HG3 H -0.48 0.02 2 169 33 34 LYS HD2 H 0.71 0.02 2 170 33 34 LYS HD3 H 0.61 0.02 2 171 33 34 LYS HE2 H 2.67 0.02 2 172 33 34 LYS HE3 H 2.32 0.02 2 173 33 34 LYS HZ H 7.33 0.02 1 174 34 35 PHE H H 7.41 0.02 1 175 34 35 PHE HA H 4.32 0.02 1 176 34 35 PHE HB2 H 2.30 0.02 2 177 34 35 PHE HB3 H 3.18 0.02 2 178 34 35 PHE HD1 H 7.23 0.02 1 179 34 35 PHE HD2 H 7.23 0.02 1 180 34 35 PHE HE1 H 7.37 0.02 1 181 34 35 PHE HE2 H 7.37 0.02 1 182 34 35 PHE HZ H 7.51 0.02 1 183 35 36 GLU H H 8.64 0.02 1 184 35 36 GLU HA H 4.47 0.02 1 185 35 36 GLU HB2 H 2.07 0.02 2 186 36 37 SER H H 8.07 0.02 1 187 36 37 SER HA H 4.57 0.02 1 188 36 37 SER HB2 H 4.46 0.02 2 189 36 37 SER HB3 H 3.59 0.02 2 190 37 38 ASN H H 8.17 0.02 1 191 37 38 ASN HA H 4.53 0.02 1 192 37 38 ASN HB2 H 3.30 0.02 2 193 37 38 ASN HB3 H 2.47 0.02 2 194 37 38 ASN HD21 H 7.39 0.02 2 195 37 38 ASN HD22 H 6.72 0.02 2 196 38 39 PHE H H 7.37 0.02 1 197 38 39 PHE HA H 3.88 0.02 1 198 38 39 PHE HB2 H 3.61 0.02 2 199 38 39 PHE HD1 H 6.96 0.02 1 200 38 39 PHE HD2 H 6.96 0.02 1 201 38 39 PHE HE1 H 7.41 0.02 1 202 38 39 PHE HE2 H 7.41 0.02 1 203 38 39 PHE HZ H 6.97 0.02 1 204 39 40 ASN H H 7.60 0.02 1 205 39 40 ASN HA H 4.98 0.02 1 206 39 40 ASN HB2 H 3.45 0.02 2 207 39 40 ASN HB3 H 2.97 0.02 2 208 39 40 ASN HD21 H 7.63 0.02 2 209 39 40 ASN HD22 H 7.03 0.02 2 210 41 42 GLN H H 8.09 0.02 1 211 41 42 GLN HA H 4.54 0.02 1 212 41 42 GLN HB2 H 2.48 0.02 2 213 41 42 GLN HB3 H 1.90 0.02 2 214 41 42 GLN HE21 H 7.64 0.02 2 215 41 42 GLN HE22 H 6.90 0.02 2 216 42 43 ALA H H 6.87 0.02 1 217 42 43 ALA HA H 4.14 0.02 1 218 42 43 ALA HB H 1.36 0.02 1 219 43 44 THR H H 8.44 0.02 1 220 43 44 THR HA H 5.14 0.02 1 221 43 44 THR HB H 3.73 0.02 1 222 43 44 THR HG2 H 1.08 0.02 1 223 44 45 ASN H H 8.21 0.02 1 224 44 45 ASN HA H 5.03 0.02 1 225 44 45 ASN HB2 H 2.66 0.02 2 226 44 45 ASN HD21 H 7.43 0.02 2 227 44 45 ASN HD22 H 6.92 0.02 2 228 45 46 ARG H H 8.93 0.02 1 229 45 46 ARG HA H 4.55 0.02 1 230 45 46 ARG HB2 H 1.69 0.02 2 231 45 46 ARG HB3 H 1.84 0.02 2 232 45 46 ARG HD2 H 3.16 0.02 2 233 45 46 ARG HE H 7.12 0.02 1 234 46 47 ASN H H 8.88 0.02 1 235 46 47 ASN HA H 5.11 0.02 1 236 46 47 ASN HB2 H 2.80 0.02 2 237 46 47 ASN HB3 H 2.88 0.02 2 238 46 47 ASN HD21 H 6.88 0.02 2 239 47 48 THR H H 8.88 0.02 1 240 47 48 THR HA H 4.09 0.02 1 241 47 48 THR HB H 4.37 0.02 1 242 47 48 THR HG2 H 1.34 0.02 1 243 48 49 ASP H H 7.85 0.02 1 244 48 49 ASP HA H 4.57 0.02 1 245 48 49 ASP HB2 H 2.65 0.02 2 246 48 49 ASP HB3 H 3.08 0.02 2 247 49 50 GLY H H 7.93 0.02 1 248 49 50 GLY HA2 H 4.40 0.02 2 249 49 50 GLY HA3 H 3.73 0.02 2 250 50 51 SER H H 8.27 0.02 1 251 50 51 SER HA H 4.63 0.02 1 252 50 51 SER HB2 H 3.76 0.02 2 253 50 51 SER HB3 H 4.19 0.02 2 254 51 52 THR H H 9.18 0.02 1 255 51 52 THR HA H 4.96 0.02 1 256 51 52 THR HG2 H 0.31 0.02 1 257 52 53 ASP HA H 5.26 0.02 1 258 52 53 ASP HB2 H 2.61 0.02 2 259 52 53 ASP HB3 H 2.02 0.02 2 260 53 54 TYR HA H 4.90 0.02 1 261 53 54 TYR HB2 H 2.66 0.02 2 262 53 54 TYR HD1 H 7.10 0.02 1 263 53 54 TYR HD2 H 7.10 0.02 1 264 53 54 TYR HE1 H 6.79 0.02 1 265 53 54 TYR HE2 H 6.79 0.02 1 266 54 55 GLY H H 9.19 0.02 1 267 54 55 GLY HA2 H 4.55 0.02 2 268 54 55 GLY HA3 H 4.14 0.02 2 269 55 56 ILE H H 9.48 0.02 1 270 55 56 ILE HA H 4.29 0.02 1 271 55 56 ILE HB H 1.63 0.02 1 272 55 56 ILE HG12 H 1.08 0.02 2 273 55 56 ILE HG13 H 1.48 0.02 2 274 55 56 ILE HG2 H 0.91 0.02 1 275 55 56 ILE HD1 H 0.75 0.02 1 276 56 57 LEU H H 9.00 0.02 1 277 56 57 LEU HA H 4.45 0.02 1 278 56 57 LEU HB2 H 1.75 0.02 2 279 56 57 LEU HB3 H 1.52 0.02 2 280 56 57 LEU HG H 1.21 0.02 1 281 56 57 LEU HD1 H 0.52 0.02 2 282 56 57 LEU HD2 H 0.33 0.02 2 283 57 58 GLN H H 8.01 0.02 1 284 57 58 GLN HA H 3.38 0.02 1 285 57 58 GLN HB2 H 2.01 0.02 2 286 57 58 GLN HB3 H 2.22 0.02 2 287 57 58 GLN HE21 H 5.26 0.02 2 288 58 59 ILE HB H 1.74 0.02 1 289 58 59 ILE HG2 H 0.87 0.02 1 290 59 60 ASN HA H 5.53 0.02 1 291 59 60 ASN HB2 H 3.07 0.02 2 292 59 60 ASN HB3 H 3.41 0.02 2 293 60 61 SER H H 9.09 0.02 1 294 60 61 SER HA H 5.13 0.02 1 295 61 62 ARG H H 8.64 0.02 1 296 61 62 ARG HA H 4.04 0.02 1 297 61 62 ARG HB2 H 1.63 0.02 2 298 61 62 ARG HB3 H 1.46 0.02 2 299 62 63 TRP H H 7.21 0.02 1 300 62 63 TRP HA H 4.40 0.02 1 301 62 63 TRP HB2 H 1.91 0.02 2 302 62 63 TRP HD1 H 6.99 0.02 1 303 62 63 TRP HE1 H 10.15 0.02 1 304 62 63 TRP HZ2 H 7.41 0.02 1 305 63 64 TRP HD1 H 6.99 0.02 1 306 63 64 TRP HE1 H 10.15 0.02 1 307 63 64 TRP HZ2 H 7.41 0.02 1 308 67 68 GLY H H 8.33 0.02 1 309 67 68 GLY HA2 H 4.03 0.02 2 310 68 69 ARG H H 8.14 0.02 1 311 68 69 ARG HA H 4.78 0.02 1 312 68 69 ARG HB2 H 1.80 0.02 2 313 68 69 ARG HG2 H 1.50 0.02 2 314 69 70 THR HA H 4.61 0.02 1 315 69 70 THR HB H 4.16 0.02 1 316 70 71 PRO HB2 H 1.88 0.02 2 317 70 71 PRO HB3 H 2.30 0.02 2 318 71 72 GLY H H 8.76 0.02 1 319 71 72 GLY HA2 H 3.83 0.02 2 320 73 74 ARG H H 8.37 0.02 1 321 73 74 ARG HA H 4.30 0.02 1 322 73 74 ARG HB2 H 1.76 0.02 2 323 73 74 ARG HG2 H 1.57 0.02 2 324 73 74 ARG HG3 H 1.36 0.02 2 325 73 74 ARG HD2 H 2.76 0.02 2 326 74 75 ASN HA H 3.76 0.02 1 327 74 75 ASN HB2 H 2.02 0.02 2 328 77 78 ASN HD21 H 7.48 0.02 2 329 77 78 ASN HD22 H 6.81 0.02 2 330 78 79 ILE HG12 H 1.08 0.02 2 331 78 79 ILE HG13 H 1.40 0.02 2 332 78 79 ILE HG2 H 0.85 0.02 1 333 82 83 ALA H H 7.59 0.02 1 334 82 83 ALA HA H 4.24 0.02 1 335 82 83 ALA HB H 1.44 0.02 1 336 84 85 LEU H H 7.02 0.02 1 337 84 85 LEU HA H 4.98 0.02 1 338 84 85 LEU HB2 H 1.91 0.02 2 339 84 85 LEU HB3 H 1.76 0.02 2 340 84 85 LEU HG H 1.68 0.02 1 341 84 85 LEU HD1 H 0.86 0.02 2 342 84 85 LEU HD2 H 0.93 0.02 2 343 85 86 SER H H 6.69 0.02 1 344 85 86 SER HA H 4.46 0.02 1 345 85 86 SER HB2 H 3.89 0.02 2 346 86 87 SER H H 8.44 0.02 1 347 86 87 SER HA H 4.21 0.02 1 348 86 87 SER HB2 H 3.82 0.02 2 349 86 87 SER HB3 H 3.91 0.02 2 350 87 88 ASP H H 8.23 0.02 1 351 87 88 ASP HA H 4.92 0.02 1 352 87 88 ASP HB2 H 2.96 0.02 2 353 87 88 ASP HB3 H 2.63 0.02 2 354 88 89 ILE H H 8.07 0.02 1 355 88 89 ILE HA H 4.69 0.02 1 356 88 89 ILE HB H 1.82 0.02 1 357 88 89 ILE HG12 H 0.33 0.02 2 358 88 89 ILE HG13 H 1.14 0.02 2 359 88 89 ILE HG2 H 0.78 0.02 1 360 88 89 ILE HD1 H 0.18 0.02 1 361 89 90 THR H H 8.38 0.02 1 362 89 90 THR HA H 3.04 0.02 1 363 89 90 THR HB H 4.03 0.02 1 364 89 90 THR HG2 H 1.15 0.02 1 365 90 91 ALA H H 9.11 0.02 1 366 90 91 ALA HA H 4.08 0.02 1 367 90 91 ALA HB H 1.33 0.02 1 368 91 92 SER H H 7.85 0.02 1 369 91 92 SER HA H 3.98 0.02 1 370 91 92 SER HB2 H 3.97 0.02 2 371 91 92 SER HB3 H 3.47 0.02 2 372 92 93 VAL H H 8.38 0.02 1 373 92 93 VAL HA H 3.12 0.02 1 374 92 93 VAL HB H 1.88 0.02 1 375 92 93 VAL HG1 H 0.48 0.02 2 376 92 93 VAL HG2 H 0.59 0.02 2 377 93 94 ASN H H 8.70 0.02 1 378 93 94 ASN HA H 4.27 0.02 1 379 93 94 ASN HB2 H 2.92 0.02 2 380 93 94 ASN HB3 H 2.75 0.02 2 381 93 94 ASN HD21 H 7.66 0.02 2 382 93 94 ASN HD22 H 6.99 0.02 2 383 94 95 CYS H H 8.03 0.02 1 384 94 95 CYS HA H 5.07 0.02 1 385 94 95 CYS HB2 H 3.34 0.02 2 386 94 95 CYS HB3 H 2.75 0.02 2 387 95 96 ALA H H 8.69 0.02 1 388 95 96 ALA HA H 4.13 0.02 1 389 95 96 ALA HB H 1.55 0.02 1 390 96 97 LYS HA H 3.71 0.02 1 391 96 97 LYS HB2 H 1.68 0.02 2 392 96 97 LYS HB3 H 1.12 0.02 2 393 96 97 LYS HG2 H -0.47 0.02 2 394 96 97 LYS HD2 H 1.26 0.02 2 395 96 97 LYS HE2 H 2.07 0.02 2 396 96 97 LYS HE3 H 2.15 0.02 2 397 97 98 LYS H H 7.24 0.02 1 398 97 98 LYS HA H 4.14 0.02 1 399 97 98 LYS HB2 H 2.15 0.02 2 400 98 99 ILE H H 8.11 0.02 1 401 98 99 ILE HA H 2.79 0.02 1 402 98 99 ILE HB H 1.49 0.02 1 403 98 99 ILE HG12 H -2.04 0.02 2 404 98 99 ILE HG13 H 0.68 0.02 2 405 98 99 ILE HG2 H -0.25 0.02 1 406 98 99 ILE HD1 H 0.00 0.02 1 407 99 100 VAL HA H 3.91 0.02 1 408 99 100 VAL HB H 2.45 0.02 1 409 99 100 VAL HG1 H 1.17 0.02 2 410 99 100 VAL HG2 H 1.36 0.02 2 411 100 101 SER H H 7.69 0.02 1 412 100 101 SER HA H 4.48 0.02 1 413 100 101 SER HB2 H 4.08 0.02 2 414 101 102 ASP H H 7.97 0.02 1 415 101 102 ASP HA H 4.76 0.02 1 416 101 102 ASP HB2 H 3.04 0.02 2 417 102 103 GLY H H 8.20 0.02 1 418 102 103 GLY HA2 H 3.95 0.02 2 419 102 103 GLY HA3 H 4.24 0.02 2 420 103 104 ASN H H 8.16 0.02 1 421 103 104 ASN HA H 4.99 0.02 1 422 103 104 ASN HB2 H 2.71 0.02 2 423 103 104 ASN HB3 H 2.81 0.02 2 424 104 105 GLY H H 8.32 0.02 1 425 104 105 GLY HA2 H 4.11 0.02 2 426 104 105 GLY HA3 H 4.26 0.02 2 427 105 106 MET H H 7.17 0.02 1 428 105 106 MET HA H 3.87 0.02 1 429 105 106 MET HB2 H -1.03 0.02 2 430 105 106 MET HB3 H 0.45 0.02 2 431 105 106 MET HG2 H 0.51 0.02 2 432 105 106 MET HG3 H -0.06 0.02 2 433 105 106 MET HE H -0.07 0.02 1 434 106 107 ASN H H 7.71 0.02 1 435 106 107 ASN HA H 4.48 0.02 1 436 106 107 ASN HB2 H 3.06 0.02 2 437 106 107 ASN HB3 H 2.82 0.02 2 438 106 107 ASN HD21 H 7.57 0.02 2 439 106 107 ASN HD22 H 7.18 0.02 2 440 107 108 ALA H H 6.75 0.02 1 441 107 108 ALA HA H 3.85 0.02 1 442 107 108 ALA HB H 0.63 0.02 1 443 108 109 TRP H H 7.93 0.02 1 444 108 109 TRP HA H 4.66 0.02 1 445 108 109 TRP HB2 H 3.37 0.02 2 446 108 109 TRP HB3 H 3.27 0.02 2 447 108 109 TRP HD1 H 7.07 0.02 1 448 108 109 TRP HE1 H 10.04 0.02 1 449 108 109 TRP HE3 H 7.37 0.02 1 450 108 109 TRP HZ2 H 6.94 0.02 1 451 108 109 TRP HZ3 H 6.52 0.02 1 452 108 109 TRP HH2 H 7.28 0.02 1 453 109 110 VAL H H 8.98 0.02 1 454 109 110 VAL HA H 3.62 0.02 1 455 109 110 VAL HB H 2.16 0.02 1 456 109 110 VAL HG1 H 1.03 0.02 2 457 109 110 VAL HG2 H 1.12 0.02 2 458 110 111 ALA H H 8.02 0.02 1 459 110 111 ALA HA H 4.27 0.02 1 460 110 111 ALA HB H 1.32 0.02 1 461 111 112 TRP H H 7.24 0.02 1 462 111 112 TRP HA H 3.72 0.02 1 463 111 112 TRP HB2 H 4.08 0.02 2 464 111 112 TRP HB3 H 2.78 0.02 2 465 111 112 TRP HD1 H 7.03 0.02 1 466 111 112 TRP HE1 H 10.43 0.02 1 467 111 112 TRP HE3 H 7.28 0.02 1 468 111 112 TRP HZ2 H 7.51 0.02 1 469 111 112 TRP HZ3 H 7.04 0.02 1 470 111 112 TRP HH2 H 7.37 0.02 1 471 112 113 ARG H H 8.30 0.02 1 472 112 113 ARG HA H 3.38 0.02 1 473 112 113 ARG HB2 H 1.99 0.02 2 474 112 113 ARG HB3 H 2.12 0.02 2 475 112 113 ARG HG2 H 1.82 0.02 2 476 112 113 ARG HD2 H 3.36 0.02 2 477 112 113 ARG HD3 H 3.46 0.02 2 478 112 113 ARG HE H 7.32 0.02 1 479 113 114 ASN H H 8.01 0.02 1 480 113 114 ASN HA H 4.50 0.02 1 481 113 114 ASN HB2 H 2.68 0.02 2 482 113 114 ASN HD21 H 7.63 0.02 2 483 113 114 ASN HD22 H 6.92 0.02 2 484 114 115 ARG H H 7.67 0.02 1 485 114 115 ARG HA H 4.32 0.02 1 486 114 115 ARG HB2 H 1.18 0.02 2 487 114 115 ARG HB3 H 0.57 0.02 2 488 114 115 ARG HG2 H 1.08 0.02 2 489 114 115 ARG HG3 H 1.02 0.02 2 490 114 115 ARG HD2 H 2.64 0.02 2 491 114 115 ARG HD3 H 2.77 0.02 2 492 114 115 ARG HE H 7.03 0.02 1 493 115 116 CYS H H 7.37 0.02 1 494 115 116 CYS HA H 4.52 0.02 1 495 115 116 CYS HB2 H 2.47 0.02 2 496 115 116 CYS HB3 H 2.61 0.02 2 497 116 117 LYS H H 7.08 0.02 1 498 116 117 LYS HA H 3.45 0.02 1 499 116 117 LYS HB2 H 1.24 0.02 2 500 116 117 LYS HB3 H -0.23 0.02 2 501 116 117 LYS HG2 H 1.06 0.02 2 502 116 117 LYS HG3 H 1.68 0.02 2 503 116 117 LYS HD2 H 1.55 0.02 2 504 116 117 LYS HE2 H 3.09 0.02 2 505 117 118 GLY H H 8.75 0.02 1 506 117 118 GLY HA2 H 4.13 0.02 2 507 117 118 GLY HA3 H 3.81 0.02 2 508 118 119 THR H H 7.68 0.02 1 509 118 119 THR HA H 4.75 0.02 1 510 118 119 THR HB H 4.31 0.02 1 511 118 119 THR HG2 H 0.95 0.02 1 512 119 120 ASP H H 8.74 0.02 1 513 119 120 ASP HA H 5.00 0.02 1 514 119 120 ASP HB2 H 2.74 0.02 2 515 119 120 ASP HB3 H 2.95 0.02 2 516 120 121 VAL H H 8.17 0.02 1 517 120 121 VAL HA H 4.36 0.02 1 518 120 121 VAL HB H 2.16 0.02 1 519 120 121 VAL HG1 H 1.08 0.02 2 520 120 121 VAL HG2 H 1.12 0.02 2 521 121 122 GLN H H 8.50 0.02 1 522 121 122 GLN HA H 4.34 0.02 1 523 121 122 GLN HB2 H 2.20 0.02 2 524 121 122 GLN HB3 H 2.25 0.02 2 525 121 122 GLN HG2 H 2.52 0.02 2 526 121 122 GLN HE21 H 7.74 0.02 2 527 121 122 GLN HE22 H 6.96 0.02 2 528 122 123 ALA H H 7.72 0.02 1 529 122 123 ALA HA H 3.81 0.02 1 530 122 123 ALA HB H 1.17 0.02 1 531 123 124 TRP H H 7.62 0.02 1 532 123 124 TRP HA H 4.11 0.02 1 533 123 124 TRP HB2 H 3.41 0.02 2 534 123 124 TRP HD1 H 7.55 0.02 1 535 123 124 TRP HE1 H 10.79 0.02 1 536 123 124 TRP HE3 H 7.50 0.02 1 537 123 124 TRP HZ2 H 7.78 0.02 1 538 123 124 TRP HZ3 H 7.13 0.02 1 539 123 124 TRP HH2 H 7.11 0.02 1 540 124 125 ILE H H 7.56 0.02 1 541 124 125 ILE HA H 4.74 0.02 1 542 124 125 ILE HB H 2.22 0.02 1 543 124 125 ILE HG12 H 1.24 0.02 2 544 124 125 ILE HG13 H 1.44 0.02 2 545 124 125 ILE HG2 H 0.82 0.02 1 546 124 125 ILE HD1 H 0.95 0.02 1 547 125 126 ARG H H 7.33 0.02 1 548 125 126 ARG HA H 4.16 0.02 1 549 125 126 ARG HB2 H 1.81 0.02 2 550 125 126 ARG HB3 H 2.00 0.02 2 551 125 126 ARG HD2 H 3.15 0.02 2 552 125 126 ARG HD3 H 3.20 0.02 2 553 125 126 ARG HE H 7.34 0.02 1 554 126 127 GLY H H 9.20 0.02 1 555 126 127 GLY HA2 H 4.31 0.02 2 556 126 127 GLY HA3 H 3.74 0.02 2 557 127 128 CYS H H 7.46 0.02 1 558 127 128 CYS HA H 4.92 0.02 1 559 127 128 CYS HB2 H 3.09 0.02 2 560 127 128 CYS HB3 H 2.62 0.02 2 561 128 129 ARG H H 8.98 0.02 1 562 128 129 ARG HA H 4.36 0.02 1 563 128 129 ARG HB2 H 1.77 0.02 2 564 128 129 ARG HD2 H 3.21 0.02 2 565 128 129 ARG HE H 7.17 0.02 1 566 129 130 LEU H H 8.03 0.02 1 567 129 130 LEU HA H 4.28 0.02 1 568 129 130 LEU HB2 H 1.66 0.02 2 569 129 130 LEU HB3 H 1.46 0.02 2 570 129 130 LEU HG H 1.40 0.02 1 571 129 130 LEU HD1 H 0.73 0.02 2 572 129 130 LEU HD2 H 0.85 0.02 2 stop_ save_