data_5068 #Corrected using PDB structure: 2HTXA # #N.B. (Observed* = Observed shift + Offset correction) # #After reference correction, the following residues still #have a HA chemical shift difference (obs*-pred) greater than 0.7ppm: #NUM AA CS Observed* Predicted # 74 N HA 3.73 5.03 # #The average CS difference between predicted and observed: #HA CA CB CO N HN #-0.04 N/A N/A N/A N/A 0.02 # #bmr5068.str.corr chemical shifts have been re-referenced with the following #offsets (these values have been added to the original bmr5068.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 +/-0.05 # #The Correlation Coefficients between predicted and observed #chemical shifts are: #HA CA CB CO N HN #0.879 N/A N/A N/A N/A 0.695 # #The RMSD between predicted and observed* (reference #corrected) chemical shifts are: #HA CA CB CO N HN #0.148 N/A N/A N/A N/A 0.280 # ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Recombinant hen lysozyme containing the extra N-terminal Met as the standard reference for the study of hen lysozyme variants ; 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_ _BMRB_accession_number 5068 _BMRB_flat_file_name bmr5068.str _Entry_type new _Submission_date 2001-07-04 _Accession_date 2001-07-05 _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' 670 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2003-05-22 update BMRB "addition of related entries" 2002-02-27 original author "original release" stop_ loop_ _Related_BMRB_accession_number _Relationship 5069 "hen egg white lysozyme (CYS mutants)" 5803 "Three-disulfide variant of hen lysozyme: C64A/C80A" 5804 "Three-disulfide variant of hen lysozyme: C76A/C94A" stop_ save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _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 _MEDLINE_UI_code 21830315 _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_volume 41 _Journal_issue 7 _Page_first 2130 _Page_last 2139 _Year 2002 loop_ _Keyword "Two-Disulfide Variant" "hen Lysozyme" "Protein Folding" "Disulfide Intermediate" stop_ 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" $metLYZ stop_ _System_physical_state native _System_oligomer_state monomer _System_paramagnetic no _System_thiol_state 'all disulfide bound' loop_ _Biological_function Hydrolase(O-Glycosyl) stop_ loop_ _Database_name _Database_accession_code _Database_entry_mol_name _Database_entry_details PDB 6LYZ ? "X-ray structure" stop_ save_ ######################## # Monomeric polymers # ######################## save_metLYZ _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common "hen egg white lysozyme" _Name_variant . _Abbreviation_common LYZ _Molecular_mass 14436 _Mol_thiol_state 'all disulfide bound' _Details "recombinant hen lysozyme containing the extra N-terminal Met" ############################## # Polymer residue sequence # ############################## _Residue_count 130 _Mol_residue_sequence ; MKVFGRCELAAAMKRHGLDN YRGYSLGNWVCAAKFESNFN TQATNRNTDGSTDYGILQIN SRWWCNDGRTPGSRNLCNIP CSALLSSDITASVNCAKKIV 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 CYS 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 CYS 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 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 1UIA "Analysis Of The Stabilization Of Hen LysozymeWith The Helix Dipole And Charged Side Chains" 102.36 127 98 98 1e-72 PDB 1UIB "Analysis Of The Stabilization Of Hen LysozymeWith The Helix Dipole And Charged Side Chains" 102.36 127 98 98 1e-72 PDB 132L "Lysozyme (E.C.3.2.1.17)" 100.78 129 100 100 1e-75 PDB 193L "The 1.33 A Structure Of Tetragonal Hen EggWhite Lysozyme" 100.78 129 100 100 1e-75 PDB 194L "The 1.40 A Structure Of Spacehab-01 Hen EggWhite Lysozyme" 100.78 129 100 100 1e-75 PDB 1AKI "The Structure Of The Orthorhombic Form Of HenEgg-White Lysozyme At 1.5 Angstroms Resolution" 100.78 129 100 100 1e-75 PDB 1AZF "Chicken Egg White Lysozyme Crystal Grown InBromide Solution" 100.78 129 100 100 1e-75 PDB 1B0D "A Chain A, Structural Effects Of MonovalentAnions On Polymorphic Lysozyme Crystals" 100.78 129 100 100 1e-75 PDB 1B2K "A Chain A, Structural Effects Of MonovalentAnions On Polymorphic Lysozyme Crystals" 100.78 129 100 100 1e-75 PDB 1BGI "Orthorhombic Lysozyme Crystallized At HighTemperature (310k)" 100.78 129 100 100 1e-75 PDB 1BHZ "Low Temperature Middle Resolution StructureOf Hen Egg White Lysozyme From Masc Data" 100.78 129 100 100 1e-75 PDB 1BVK "C Chain C, Humanized Anti-Lysozyme Fv ComplexedWith Lysozyme" 100.78 129 100 100 1e-75 PDB 1BVX "A Chain A, The 1.8 A Structure Of Gel GrownTetragonal Hen Egg White Lysozyme" 100.78 129 100 100 1e-75 PDB 1BWH "A Chain A, The 1.8 A Structure Of GroundControl Grown Tetragonal Hen Egg White Lysozyme" 100.78 129 100 100 1e-75 PDB 1BWI "A Chain A, The 1.8 A Structure Of MicrobatchOil Drop Grown Tetragonal Hen Egg White Lysozyme" 100.78 129 100 100 1e-75 PDB 1BWJ "A Chain A, The 1.8 A Structure Of MicrogravityGrown Tetragonal Hen Egg White Lysozyme" 100.78 129 100 100 1e-75 PDB 1C08 "C Chain C, Crystal Structure Of Hyhel-10 Fv-HenLysozyme Complex" 100.78 129 100 100 1e-75 PDB 1C10 "A Chain A, Crystal Structure Of Hew LysozymeUnder Pressure Of Xenon (8 Bar)" 100.78 129 100 100 1e-75 PDB 1DPW "A Chain A, Structure Of Hen Egg-White LysozymeIn Complex With Mpd" 100.78 129 100 100 1e-75 PDB 1DPX "A Chain A, Structure Of Hen Egg-White Lysozyme" 100.78 129 100 100 1e-75 PDB 1DQJ "C Chain C, Crystal Structure Of TheAnti-Lysozyme Antibody Hyhel-63 Complexed With Hen EggWhite Lysozyme" 100.78 129 100 100 1e-75 PDB 1E8L "A Chain A, Nmr Solution Structure Of HenLysozyme" 100.78 129 100 100 5e-75 PDB 1F0W "A Chain A, Crystal Structure Of OrthorhombicLysozyme Grown At Ph 6.5" 100.78 129 100 100 1e-75 PDB 1F10 "A Chain A, Crystal Structure Of OrthorhombicLysozyme Grown At Ph 6.5 At 88% Relative Humidity" 100.78 129 100 100 1e-75 PDB 1FDL "Y Chain Y, IgG1 Fab Fragment (Anti-LysozymeAntibody D1.3, Kappa) - Lysozyme (E.C.3.2.1.17) Complex" 100.78 129 100 100 1e-75 PDB 1G7H "C Chain C, Crystal Structure Of Hen Egg WhiteLysozyme (Hel) Complexed With The Mutant Anti-HelMonoclonal Antibody D1.3(Vlw92a)" 100.78 129 100 100 1e-75 PDB 1G7I "C Chain C, Crystal Structure Of Hen Egg WhiteLysozyme (Hel) Complexed With The Mutant Anti-HelMonoclonal Antibody D1.3 (Vlw92f)" 100.78 129 100 100 1e-75 PDB 1G7J "C Chain C, Crystal Structure Of Hen Egg WhiteLysozyme (Hel) Complexed With The Mutant Anti-HelMonoclonal Antibody D1.3 (Vlw92h)" 100.78 129 100 100 1e-75 PDB 1G7L "C Chain C, Crystal Structure Of Hen Egg WhiteLysozyme (Hel) Complexed With The Mutant Anti-HelMonoclonal Antibody D1.3 (Vlw92s)" 100.78 129 100 100 1e-75 PDB 1G7M "C Chain C, Crystal Structure Of Hen Egg WhiteLysozyme (Hel) Complexed With The Mutant Anti-HelMonoclonal Antibody D1.3 (Vlw92v)" 100.78 129 100 100 1e-75 PDB 1GPQ "C Chain C, Structure Of Ivy Complexed With ItsTarget, Hewl" 100.78 129 100 100 1e-75 PDB 1GWD "A Chain A, Tri-Iodide Derivative Of HenEgg-White Lysozyme" 100.78 129 100 100 1e-75 PDB 1GXV "2 Chain 2, Solution Structure Of Lysozyme AtLow And High Pressure" 100.78 129 100 100 5e-75 PDB 1GXX "A Chain A, Solution Structure Of Lysozyme AtLow And High Pressure" 100.78 129 100 100 5e-75 PDB 1H87 "A Chain A, Gadolinium Derivative Of TetragonalHen Egg-White Lysozyme At 1.7 A Resolution" 100.78 129 100 100 1e-75 PDB 1HEL "Hen Egg-White Lysozyme (E.C.3.2.1.17) WildType" 100.78 129 100 100 1e-75 PDB 1HEW "Lysozyme (E.C.3.2.1.17) Complexed With TheInhibitor Tri-N-Acetylchitotriose" 100.78 129 100 100 1e-75 PDB 1HF4 "A Chain A, Structural Effects Of MonovalentAnions On Polymorphic Lysozyme Crystals" 100.78 129 100 100 1e-75 PDB 1HSW "Lysozyme (Mucopeptide N-AcetylmuramylHydrolase)" 100.78 129 100 100 1e-75 PDB 1HSX "Lysozyme Grown At Basic Ph And Its LowHumidity Variant" 100.78 129 100 100 1e-75 PDB 1IC4 "Y Chain Y, Crystal Structure Of Hyhel-10 FvMutant(Hd32a)-Hen Lysozyme Complex" 100.78 129 100 100 1e-75 PDB 1IC5 "Y Chain Y, Crystal Structure Of Hyhel-10 FvMutant(Hd99a)-Hen Lysozyme Complex" 100.78 129 100 100 1e-75 PDB 1IC7 "Y Chain Y, Crystal Structure Of Hyhel-10 FvMutant(Hd32a99a)-Hen Lysozyme Complex" 100.78 129 100 100 1e-75 PDB 1IEE "A Chain A, Structure Of Tetragonal Hen EggWhite Lysozyme At 0.94 A From Crystals Grown By TheCounter-Diffusion Method" 100.78 129 100 100 1e-75 PDB 1IO5 "A Chain A, Hydrogen And Hydration Of HenEgg-White Lysozyme Determined By Neutron Diffraction" 100.78 129 100 100 1e-75 PDB 1J1O "Y Chain Y, Crystal Structure Of Hyhel-10 FvMutant Ly50f Complexed With Hen Egg White Lysozyme" 100.78 129 100 100 1e-75 PDB 1J1P "Y Chain Y, Crystal Structure Of Hyhel-10 FvMutant Ls91a Complexed With Hen Egg White Lysozyme" 100.78 129 100 100 1e-75 PDB 1J1X "Y Chain Y, Crystal Structure Of Hyhel-10 FvMutant Ls93a Complexed With Hen Egg White Lysozyme" 100.78 129 100 100 1e-75 PDB 1JA2 "A Chain A, Binding Of N-Acetylglucosamine ToChicken Egg Lysozyme: A Powder Diffraction Study" 100.78 129 100 100 1e-75 PDB 1JA4 "A Chain A, Binding Of N-Acetylglucosamine ToChicken Egg Lysozyme: A Powder Diffraction Study" 100.78 129 100 100 1e-75 PDB 1JA6 "A Chain A, Binding Of N-Acetylglucosamine ToChicken Egg Lysozyme: A Powder Diffraction Study" 100.78 129 100 100 1e-75 PDB 1JA7 "A Chain A, Binding Of N-Acetylglucosamine ToChicken Egg Lysozyme: A Powder Diffraction Study" 100.78 129 100 100 1e-75 PDB 1JIS "A Chain A, Crystal Structure Of TetragonalLysozyme Grown At Ph 4.6" 100.78 129 100 100 1e-75 PDB 1JIT "A Chain A, Crystal Structure Of TetragonalLysozyme Grown In Presence 30% Trehalose" 100.78 129 100 100 1e-75 PDB 1JIY "A Chain A, Crystal Structure Of TetragonalLysozyme Grown In Presence 20% Sorbitol" 100.78 129 100 100 1e-75 PDB 1JJ0 "A Chain A, Crystal Structure Of TetragonalLysozyme Grown In Presence Of 30% Sucrose" 100.78 129 100 100 1e-75 PDB 1JJ1 "A Chain A, Crystal Structure Of OrthorhombicLysozyme Grown At Ph 4.6 In Presence Of 5% Sorbitol" 100.78 129 100 100 1e-75 PDB 1JJ3 "A Chain A, Crystal Structure Of MonoclinicLysozyme Grown At Ph 4.6" 100.78 129 100 100 1e-75 PDB 1JPO "Low Temperature Orthorhombic Lysozyme" 100.78 129 100 100 1e-75 PDB 1JTO "L Chain L, Degenerate Interfaces InAntigen-Antibody Complexes" 100.78 129 100 100 1e-75 PDB 1JTT "L Chain L, Degenerate Interfaces InAntigen-Antibody Complexes" 100.78 129 100 100 1e-75 PDB 1KIP "C Chain C, Fv Mutant Y(B 32)a (Vh Domain) OfMouse Monoclonal Antibody D1.3 Complexed With Hen EggWhite Lysozyme" 100.78 129 100 100 1e-75 PDB 1KIQ "C Chain C, Fv Mutant Y(B 101)f (Vh Domain) OfMouse Monoclonal Antibody D1.3 Complexed With Hen EggWhite Lysozyme" 100.78 129 100 100 1e-75 PDB 1KIR "C Chain C, Fv Mutant Y(A 50)s (Vl Domain) OfMouse Monoclonal Antibody D1.3 Complexed With Hen EggWhite Lysozyme" 100.78 129 100 100 1e-75 PDB 1LCN "A Chain A, Monoclinic Hen Egg White Lysozyme,Thiocyanate Complex" 100.78 129 100 100 1e-75 PDB 1LJ3 "A Chain A, Crystal Structure Of MonoclinicLysozyme Grown At Ph 4.6" 100.78 129 100 100 1e-75 PDB 1LJ4 "A Chain A, Crystal Structure Of MonoclinicLysozyme Grown At Ph 4.6" 100.78 129 100 100 1e-75 PDB 1LJE "A Chain A, Crystal Structure Of MonoclinicLysozyme Grown In Presence Of 10% Sucrose" 100.78 129 100 100 1e-75 PDB 1LJF "A Chain A, Crystal Structure Of MonoclinicLysozyme Grown In Presence Of 10% Sucrose" 100.78 129 100 100 1e-75 PDB 1LJG "A Chain A, Crystal Structure Of MonoclinicLysozyme Grown In Presence Of 5% Glycerol" 100.78 129 100 100 1e-75 PDB 1LJH "A Chain A, Crystal Structure Of MonoclinicLysozyme Grown In Presence Of 5% Glycerol" 100.78 129 100 100 1e-75 PDB 1LJI "A Chain A, Crystal Structure Of MonoclinicLysozyme Grown In Presence 10% Sorbitol" 100.78 129 100 100 1e-75 PDB 1LJJ "A Chain A, Crystal Structure Of MonoclinicLysozyme Grown In Presence Of 10% Trehalose" 100.78 129 100 100 1e-75 PDB 1LJK "A Chain A, Crystal Structure Of MonoclinicLysozyme Grown In Presence Of 15% Trehalose" 100.78 129 100 100 1e-75 PDB 1LKR "A Chain A, Monoclinic Hen Egg White LysozymeIodide" 100.78 129 100 100 1e-75 PDB 1LKS "Hen Egg White Lysozyme Nitrate" 100.78 129 100 100 1e-75 PDB 1LMA "Lysozyme (E.C.3.2.1.17) (88 Percent Humidity)" 100.78 129 100 100 1e-75 PDB 1LPI "Hew Lysozyme: Trp...Na Cation-Pi Interaction" 100.78 129 100 100 1e-75 PDB 1LSA "Lysozyme (E.C.3.2.1.17) (120 K)" 100.78 129 100 100 1e-75 PDB 1LSB "Lysozyme (E.C.3.2.1.17) (180 K)" 100.78 129 100 100 1e-75 PDB 1LSC "Lysozyme (E.C.3.2.1.17) (250 K)" 100.78 129 100 100 1e-75 PDB 1LSD "Lysozyme (E.C.3.2.1.17) (280 K)" 100.78 129 100 100 1e-75 PDB 1LSE "Lysozyme (E.C.3.2.1.17) (295 K)" 100.78 129 100 100 1e-75 PDB 1LSF "Lysozyme (E.C.3.2.1.17) (95 K)" 100.78 129 100 100 1e-75 PDB 1LYO "Cross-Linked Lysozyme Crystal In Neat Water" 100.78 129 100 100 1e-75 PDB 1LYS "A Chain A, Lysozyme (E.C.3.2.1.17)" 100.78 129 100 100 1e-75 PDB 1LYZ "Lysozyme (E.C.3.2.1.17)" 100.78 129 100 100 1e-75 PDB 1LZ8 "A Chain A, Lysozyme Phased On Anomalous SignalOf Sulfurs And Chlorines" 100.78 129 100 100 1e-75 PDB 1LZ9 "A Chain A, Anomalous Signal Of Solvent BrominesUsed For Phasing Of Lysozyme" 100.78 129 100 100 1e-75 PDB 1LZA "Lysozyme (E.C.3.2.1.17)" 100.78 129 100 100 1e-75 PDB 1LZB "Lysozyme (E.C.3.2.1.17) Co-Crystallized WithTri-N-Acetyl-Chitotriose (Ph 4.7)" 100.78 129 100 100 1e-75 PDB 1LZC "Lysozyme (E.C.3.2.1.17) Co-Crystallized WithTetra-N-Acetyl-Chitotetraose (Ph 4.7)" 100.78 129 100 100 1e-75 PDB 1LZH "A Chain A, Lysozyme (Monoclinic) (E.C.3.2.1.17)" 100.78 129 100 100 1e-75 PDB 1LZN "A Chain A, Neutron Structure Of Hen Egg-WhiteLysozyme" 100.78 129 100 100 1e-75 PDB 1LZT "Lysozyme (E.C.3.2.1.17), Triclinic CrystalForm" 100.78 129 100 100 1e-75 PDB 1MEL "L Chain L, Crystal Structure Of A CamelSingle-Domain Vh Antibody Fragment In Complex WithLysozyme" 100.78 129 100 100 1e-75 PDB 1MLC "E Chain E, Monoclonal Antibody Fab D44.1 RaisedAgainst Chicken Egg-White Lysozyme Complexed WithLysozyme" 100.78 129 100 100 1e-75 PDB 1N4F "A Chain A, Para-Arsanilate Derivative Of HenEgg-White Lysozyme" 100.78 129 100 100 1e-75 PDB 1NDM "C Chain C, Crystal Structure Of Fab FragmentOf Antibody Hyhel-26 Complexed With Lysozyme" 100.78 129 100 100 1e-75 PDB 1P2C "C Chain C, Crystal Structure Analysis Of AnAnti-Lysozyme Antibody" 100.78 129 100 100 1e-75 PDB 1PS5 "A Chain A, Structure Of The Monoclinic C2 FormOf Hen Egg-White Lysozyme At 2.0 Angstroms Resolution" 100.78 129 100 100 1e-75 PDB 1QIO "A Chain A, Specific Chemical And StructuralDamage Caused By Intense Synchrotron Radiation To HenEgg White Lysozyme" 100.78 129 100 100 1e-75 PDB 1QTK "A Chain A, Crystal Structure Of Hew LysozymeUnder Pressure Of Krypton (55 Bar)" 100.78 129 100 100 1e-75 PDB 1RCM "A Chain A, Lysozyme (E.C.3.2.1.17) (PartiallyReduced, Carboxymethylated (6,127-Rcm))" 100.78 129 100 100 1e-75 PDB 1RFP "Analysis Of The Stabilization Of Hen LysozymeWith The Helix Dipole And Charged Side Chains" 100.78 129 100 100 1e-75 PDB 1SF4 "A Chain A, Binding Of N,N'-DiacetylchitobioseTo Hew Lysozyme: A Powder Diffraction Study" 100.78 129 100 100 1e-75 PDB 1SF6 "A Chain A, Binding OfN,N',N"-Triacetylchitotriose To Hew Lysozyme: A PowderDiffraction Study" 100.78 129 100 100 1e-75 PDB 1SF7 "A Chain A, Binding OfTetra-N-Acetylchitotetraose To Hew Lysozyme: A PowderDiffraction Study" 100.78 129 100 100 1e-75 PDB 1SFB "A Chain A, Binding OfPenta-N-Acetylchitopentaose To Hew Lysozyme: A PowderDiffraction Study" 100.78 129 100 100 1e-75 PDB 1SFG "A Chain A, Binding OfHexa-N-Acetylchitohexaose: A Powder Diffraction Study" 100.78 129 100 100 1e-75 PDB 1UA6 "Y Chain Y, Crystal Structure Of Hyhel-10 FvMutant Sfsf Complexed With Hen Egg White LysozymeComplex" 100.78 129 100 100 1e-75 PDB 1UC0 "A Chain A, Crystal Structure Of Wild-TypeHen-Egg White Lysozyme Singly Labeled With2',3'-Epoxypropyl Beta-Glycoside Of N- Acetyllactosamine" 100.78 129 100 100 1e-75 PDB 1UCO "A Chain A, Hen Egg-White Lysozyme, Low HumidityForm" 100.78 129 100 100 1e-75 PDB 1UIG "Analysis Of The Stabilization Of Hen LysozymeWith The Helix Dipole And Charged Side Chains" 100.78 129 100 100 1e-75 PDB 1UIH "Analysis Of The Stabilization Of Hen LysozymeWith The Helix Dipole And Charged Side Chains" 100.78 129 100 100 1e-75 PDB 1UUZ "C Chain C, Ivy:a New Family Of Protein" 100.78 129 100 100 1e-75 PDB 1V7S "A Chain A, Triclinic Hen Lysozyme CrystallizedAt 313k From A D2o Solution" 100.78 129 100 100 4e-75 PDB 1V7T "A Chain A, Triclinic Lysozyme With Low SolventContent Obtained By Phase Transition" 100.78 129 100 100 1e-75 PDB 1VDP "A Chain A, The Crystal Structure Of TheMonoclinic Form Of Hen Egg White Lysozyme At 1.7Angstroms Resolution In Space" 100.78 129 100 100 1e-75 PDB 1VDQ "A Chain A, The Crystal Structure Of TheOrthorhombic Form Of Hen Egg White Lysozyme At 1.5Angstroms Resolution" 100.78 129 100 100 1e-75 PDB 1VDS "A Chain A, The Crystal Structure Of TheTetragonal Form Of Hen Egg White Lysozyme At 1.6Angstroms Resolution In Space" 100.78 129 100 100 1e-75 PDB 1VDT "A Chain A, The Crystal Structure Of TheTetragonal Form Of Hen Egg White Lysozyme At 1.7Angstroms Resolution Under Basic Conditions In Space" 100.78 129 100 100 1e-75 PDB 1VED "A Chain A, The Crystal Structure Of TheOrthorhombic Form Of Hen Egg White Lysozyme At 1.9Angstroms Resolution In Space" 100.78 129 100 100 1e-75 PDB 1VFB "C Chain C, Fv Fragment Of Mouse MonoclonalAntibody D1.3 Complexed With Hen Egg Lysozyme" 100.78 129 100 100 1e-75 PDB 1XEI "The Crystal Structures Of Lysozyme At VeryLow Levels Of Hydration" 100.78 129 100 100 1e-75 PDB 1XEJ "The Crystal Structures Of Lysozyme At VeryLow Levels Of Hydration" 100.78 129 100 100 1e-75 PDB 1XEK "The Crystal Structures Of Lysozyme At VeryLow Levels Of Hydration" 100.78 129 100 100 1e-75 PDB 2CDS "A Chain A, Lysozyme" 100.78 129 100 100 1e-75 PDB 2LYM "Lysozyme (E.C.3.2.1.17) (1 Atmosphere, 1.4 MNaCl)" 100.78 129 100 100 1e-75 PDB 2LYO "Cross-Linked Chicken Lysozyme Crystal In 90%Acetonitrile-Water" 100.78 129 100 100 1e-75 PDB 2LYZ "Lysozyme (E.C.3.2.1.17)" 100.78 129 100 100 1e-75 PDB 2LZH "Lysozyme (Orthorhombic) (E.C.3.2.1.17)" 100.78 129 100 100 1e-75 PDB 2LZT "Lysozyme (E.C.3.2.1.17), Triclinic CrystalForm" 100.78 129 100 100 1e-75 PDB 3HFL "Y Chain Y, IgG1 Fab Fragment (HyHEL-5)Complexed With Lysozyme (E.C.3.2.1.17)" 100.78 129 100 100 1e-75 PDB 3HFM "Y Chain Y, IgG1 Fab Fragment (HyHEL-10) AndLysozyme (E.C.3.2.1.17) Complex" 100.78 129 100 100 1e-75 PDB 3LYM "Lysozyme (E.C.3.2.1.17) (1000 Atmospheres, 1.4M NaCl)" 100.78 129 100 100 1e-75 PDB 3LYO "Cross-Linked Chicken Lysozyme Crystal In 95%Acetonitrile-Water" 100.78 129 100 100 1e-75 PDB 3LYT "A Chain A, Lysozyme (E.C.3.2.1.17) (100 Kelvin)" 100.78 129 100 100 1e-75 PDB 3LYZ "Lysozyme (E.C.3.2.1.17)" 100.78 129 100 100 1e-75 PDB 3LZT "Refinement Of Triclinic Lysozyme At AtomicResolution" 100.78 129 100 100 1e-75 PDB 4LYM "Lysozyme (Mucopeptide N-AcetylmuramylHydrolase) (E.C.3.2.1.17)" 100.78 129 100 100 1e-75 PDB 4LYO "Cross-Linked Chicken Lysozyme Crystal In NeatAcetonitrile, Then Back-Soaked In Water" 100.78 129 100 100 1e-75 PDB 4LYT "A Chain A, Lysozyme (E.C.3.2.1.17) (298 Kelvin)" 100.78 129 100 100 1e-75 PDB 4LYZ "Lysozyme (E.C.3.2.1.17)" 100.78 129 100 100 1e-75 PDB 4LZT "Atomic Resolution Refinement Of Triclinic HewLysozyme At 295k" 100.78 129 100 100 1e-75 PDB 5LYM "A Chain A, Mol_id: 1; Molecule: Lysozyme;Chain: A, B; Ec: 3.2.1.17" 100.78 129 100 100 1e-75 PDB 5LYT "Lysozyme (E.C.3.2.1.17) (100 Kelvin)" 100.78 129 100 100 1e-75 PDB 5LYZ "Lysozyme (E.C.3.2.1.17)" 100.78 129 100 100 1e-75 PDB 6LYT "Lysozyme (E.C.3.2.1.17) (298 Kelvin)" 100.78 129 100 100 1e-75 PDB 6LYZ "Lysozyme (E.C.3.2.1.17)" 100.78 129 100 100 1e-75 PDB 7LYZ "Lysozyme (E.C.3.2.1.17) Triclinic Crystal Form" 100.78 129 100 100 1e-75 PDB 8LYZ "Lysozyme (E.C.3.2.1.17) Iodine-Inactivated" 100.78 129 100 100 1e-75 PDB 1A2Y "C Chain C, Hen Egg White Lysozyme, D18a Mutant,In Complex With Mouse Monoclonal Antibody D1.3" 100.78 129 99 99 10e-75 PDB 1AT6 "Hen Egg White Lysozyme With A IsoaspartateResidue" 100.78 129 99 99 9e-75 PDB 1FLQ "A Chain A, Hen Egg White Lysozyme Mutant WithAlanine Substituted For Glycine" 100.78 129 99 99 7e-75 PDB 1FLU "A Chain A, Hen Egg White Lysozyme Mutant WithAlanine Substituted For Glycine" 100.78 129 99 99 7e-75 PDB 1FLW "A Chain A, Hen Egg White Lysozyme Mutant WithAlanine Substituted For Glycine" 100.78 129 99 99 7e-75 PDB 1FLY "A Chain A, Hen Egg White Lysozyme Mutant WithAlanine Substituted For Glycine" 100.78 129 99 99 7e-75 PDB 1FN5 "A Chain A, Hen Egg White Lysozyme Mutant WithAlanine Substituted For Glycine" 100.78 129 99 99 7e-75 PDB 1H6M "A Chain A, Covalent Glycosyl-EnzymeIntermediate Of Hen Egg White Lysozyme" 100.78 129 99 100 3e-75 PDB 1HEM "Lysozyme (E.C.3.2.1.17) Mutant With Ser 91Replaced By Thr (S91t)" 100.78 129 99 100 3e-75 PDB 1HEO "Lysozyme (E.C.3.2.1.17) Mutant With Ile 55Replaced By Val (I55v)" 100.78 129 99 100 2e-75 PDB 1HER "Lysozyme (E.C.3.2.1.17) Mutant With Thr 40Replaced By Ser (T40s)" 100.78 129 99 100 4e-75 PDB 1IOS "A Chain A, Stabilization Of Hen Egg WhiteLysozyme By A Cavity-Filling Mutation" 100.78 129 99 99 5e-75 PDB 1IOT "A Chain A, Stabilization Of Hen Egg WhiteLysozyme By A Cavity-Filling Mutation" 100.78 129 99 100 3e-75 PDB 1IR7 "A Chain A, Im Mutant Of Lysozyme" 100.78 129 99 100 3e-75 PDB 1IR8 "A Chain A, Im Mutant Of Lysozyme" 100.78 129 99 100 3e-75 PDB 1IR9 "A Chain A, Im Mutant Of Lysozyme" 100.78 129 99 100 3e-75 PDB 1KXW "Analysis Of The Stabilization Of Hen LysozymeWith The Helix Dipole And Charged Side Chains" 100.78 129 99 100 5e-75 PDB 1KXY "Analysis Of The Stabilization Of Hen LysozymeWith The Helix Dipole And Charged Side Chains" 100.78 129 99 100 5e-75 PDB 1LZD "Lysozyme (E.C.3.2.1.17) Mutant With Trp 62Replaced By Tyr (W62y)" 100.78 129 99 100 2e-74 PDB 1LZE "Lysozyme (E.C.3.2.1.17) Mutant With Trp 62Replaced By Tyr (W62y) Co-Crystallized WithTri-N-Acetyl-Chitotriose (Ph 4.7)" 100.78 129 99 100 2e-74 PDB 1LZG "Lysozyme (E.C.3.2.1.17) Mutant With Trp 62Replaced By Phe (W62f) Co-Crystallized WithTri-N-Acetyl-Chitotriose (Ph 4.7)" 100.78 129 99 100 2e-74 PDB 1NBY "C Chain C, Crystal Structure Of Hyhel-63Complexed With Hel Mutant K96a" 100.78 129 99 99 7e-75 PDB 1NBZ "C Chain C, Crystal Structure Of Hyhel-63Complexed With Hel Mutant K96a" 100.78 129 99 99 7e-75 PDB 1NDG "C Chain C, Crystal Structure Of Fab FragmentOf Antibody Hyhel-8 Complexed With Its Antigen Lysozyme" 100.78 129 99 99 7e-75 PDB 1UIC "Analysis Of The Stabilization Of Hen LysozymeWith The Helix Dipole And Charged Side Chains" 100.78 129 99 99 2e-74 PDB 1UID "Analysis Of The Stabilization Of Hen LysozymeWith The Helix Dipole And Charged Side Chains" 100.78 129 99 99 2e-74 PDB 1UIE "Analysis Of The Stabilization Of Hen LysozymeWith The Helix Dipole And Charged Side Chains" 100.78 129 99 99 2e-74 PDB 1UIF "Analysis Of The Stabilization Of Hen LysozymeWith The Helix Dipole And Charged Side Chains" 100.78 129 99 99 3e-74 PDB 2IFF "Y Chain Y, Igg1 Fab Fragment (Hyhel-5) ComplexedWith Lysozyme Mutant With Arg 68 Replaced By Lys (R68k)" 100.78 129 99 100 3e-75 PDB 1AT5 "Hen Egg White Lysozyme With A SuccinimideResidue" 100.78 129 98 98 6e-74 PDB 1HEN "Lysozyme (E.C.3.2.1.17) Mutant With Ile 55Replaced By Val And Ser 91 Replaced By Thr (I55v,S91t)" 100.78 129 98 100 4e-75 PDB 1HEQ "Lysozyme (E.C.3.2.1.17) Mutant With Thr 40Replaced By Ser And Ser 91 Replaced By Thr (T40s,S91t)" 100.78 129 98 100 9e-75 PDB 1IOQ "A Chain A, Stabilization Of Hen Egg WhiteLysozyme By A Cavity-Filling Mutation" 100.78 129 98 98 2e-74 PDB 1IOR "A Chain A, Stabilization Of Hen Egg WhiteLysozyme By A Cavity-Filling Mutation" 100.78 129 98 99 9e-75 PDB 1KXX "Analysis Of The Stabilization Of Hen LysozymeWith The Helix Dipole And Charged Side Chains" 100.78 129 98 100 2e-74 PDB 1LSN "Lysozyme (E.C.3.2.1.17) Mutant With Ser 91Replaced By Ala (S91a)" 100.78 129 98 100 10e-75 PDB 1HEP "Lysozyme (E.C.3.2.1.17) Mutant With Thr 40Replaced By Ser, Ile 55 Replaced By Val, And Ser 91Replaced By Thr (T40s,I55v,S91t)" 100.78 129 98 100 10e-75 PDB 1LSM "Lysozyme (E.C.3.2.1.17) Mutant With Ile 55Replaced By Leu, Ser 91 Replaced By Thr, And Asp 101Replaced By Ser (I55l,S91t,D101s)" 100.78 129 98 99 3e-74 PDB 1LSG "Lysozyme, Fibrinogen Mol_id: 1; Molecule:Lysozyme Modified With Human Fibrinogen Gamma; Chain:Null; Engineered; The 14-Residue C-Terminus (Residues398 - 411) Of The Human Fibrinogen Gamma Chain Fused ToThe C-Terminus Of Chicken Egg White Lysozyme; Mutation:N-Term Met" 90.28 144 100 100 4e-76 PDB 1LSY "Lysozyme (E.C.3.2.1.17) Mutant With Asp 52Replaced By Ser (D52s)" 88.44 147 99 99 7e-75 PDB 1LSZ "Lysozyme (E.C.3.2.1.17) Mutant With Asp 52Replaced By Ser (D52s) Complexed With Glcnac4(Tetra-N-Acetyl Chitotetraose)" 88.44 147 99 99 7e-75 EMBL CAA23711.1 "unnamed protein product [Gallus gallus]" 88.44 147 98 99 2e-74 GenBank AAA48943.1 "lysozyme (" 88.44 147 100 100 1e-75 GenBank AAL69327.1 "egg white lysozyme [Gallus gallus]" 88.44 147 100 100 1e-75 PIR LZCH "lysozyme (EC 3.2.1.17) c precursor [validated] -chicken" 88.44 147 100 100 1e-75 PRF 630460A lysozyme 100.78 129 99 100 5e-75 REF NP_990612.1 "lysozyme C [Gallus gallus]" 88.44 147 98 99 2e-74 SWISS-PROT P00698 "LYC_CHICK Lysozyme C precursor(1,4-beta-N-acetylmuramidase C) (Allergen Gal d 4) (Gald IV)" 88.44 147 100 100 1e-75 stop_ save_ ######################################## # Molecular bond linkage definitions # ######################################## save_crosslink_bonds _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 "hen lysozyme" 7 CYS SG "hen lysozyme" 128 CYS SG single disulfide "hen lysozyme" 31 CYS SG "hen lysozyme" 116 CYS SG single disulfide "hen lysozyme" 65 CYS SG "hen lysozyme" 81 CYS SG single disulfide "hen lysozyme" 77 CYS SG "hen lysozyme" 95 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 _Tissue $metLYZ 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 $metLYZ 'recombinant technology' "E. coli" Escherichia coli . plasmid . 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 _Concentration_min_value _Concentration_max_value _Isotopic_labeling $metLYZ . mM 1.0 1.2 "[U-15N]" stop_ save_ ############################ # Computer software used # ############################ save_XWINNMR _Saveframe_category software _Name XWINNMR _Version 2.6 save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model DRX _Field_strength 600 save_ ############################# # NMR applied experiments # ############################# save_NMR_applied_experiment _Saveframe_category NMR_applied_experiment _Experiment_name ; DQF-COSY NOESY HOHAHA 15N 3D-NOESY-HSQC 15N 3D-TOCSY-HSQC 1H-15N HSQC ; save_ ####################### # Sample conditions # ####################### save_EX-cond_1 _Saveframe_category sample_conditions loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 3.8 0.2 n/a temperature 298 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 DSS H 1 'methyl protons' ppm 0.00 external direct . . . . 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 "hen lysozyme" 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 1 LYS H H 8.82 0.02 1 2 1 LYS HA H 4.36 0.02 1 3 1 LYS HB2 H 1.76 0.02 2 4 1 LYS HB3 H 1.51 0.02 2 5 2 VAL H H 8.83 0.02 1 6 2 VAL HA H 4.82 0.02 1 7 2 VAL HB H 2.01 0.02 1 8 2 VAL HG1 H 1.05 0.02 2 9 2 VAL HG2 H 0.95 0.02 2 10 3 PHE H H 8.66 0.02 1 11 3 PHE HA H 4.27 0.02 1 12 3 PHE HB2 H 3.18 0.02 2 13 3 PHE HB3 H 2.66 0.02 2 14 3 PHE HD1 H 6.98 0.02 1 15 3 PHE HD2 H 6.98 0.02 1 16 3 PHE HE1 H 7.22 0.02 1 17 3 PHE HE2 H 7.22 0.02 1 18 3 PHE HZ H 7.48 0.02 1 19 4 GLY H H 8.45 0.02 1 20 4 GLY HA2 H 4.32 0.02 2 21 4 GLY HA3 H 3.95 0.02 2 22 5 ARG H H 8.58 0.02 1 23 5 ARG HA H 3.36 0.02 1 24 5 ARG HB2 H 2.12 0.02 2 25 5 ARG HD2 H 3.86 0.02 2 26 5 ARG HE H 7.58 0.02 1 27 6 CYS H H 8.72 0.02 1 28 6 CYS HA H 4.74 0.02 1 29 6 CYS HB2 H 3.22 0.02 2 30 6 CYS HB3 H 2.78 0.02 2 31 7 GLU H H 8.28 0.02 1 32 7 GLU HA H 4.09 0.02 1 33 7 GLU HB2 H 2.27 0.02 2 34 7 GLU HB3 H 2.18 0.02 2 35 7 GLU HG2 H 2.35 0.02 2 36 7 GLU HG3 H 2.51 0.02 2 37 8 LEU H H 8.62 0.02 1 38 8 LEU HA H 3.75 0.02 1 39 8 LEU HB2 H 1.59 0.02 2 40 8 LEU HG H 1.53 0.02 1 41 8 LEU HD1 H 0.59 0.02 2 42 8 LEU HD2 H 0.00 0.02 2 43 9 ALA H H 8.45 0.02 1 44 9 ALA HA H 3.60 0.02 1 45 9 ALA HB H 1.58 0.02 1 46 10 ALA H H 8.19 0.02 1 47 10 ALA HA H 3.98 0.02 1 48 10 ALA HB H 1.55 0.02 1 49 11 ALA H H 7.79 0.02 1 50 11 ALA HA H 4.28 0.02 1 51 11 ALA HB H 1.51 0.02 1 52 12 MET H H 9.16 0.02 1 53 12 MET HA H 3.46 0.02 1 54 12 MET HB2 H 1.89 0.02 2 55 12 MET HB3 H 1.56 0.02 2 56 12 MET HG2 H 2.76 0.02 2 57 12 MET HG3 H 1.34 0.02 2 58 13 LYS H H 8.55 0.02 1 59 13 LYS HA H 3.98 0.02 1 60 13 LYS HB2 H 2.22 0.02 2 61 13 LYS HB3 H 1.95 0.02 2 62 13 LYS HG2 H 1.52 0.02 2 63 13 LYS HG3 H 1.50 0.02 2 64 13 LYS HD2 H 1.74 0.02 2 65 13 LYS HD3 H 3.03 0.02 2 66 14 ARG H H 8.28 0.02 1 67 14 ARG HA H 4.13 0.02 1 68 14 ARG HB2 H 1.97 0.02 2 69 14 ARG HD2 H 3.15 0.02 2 70 14 ARG HE H 7.16 0.02 1 71 15 HIS H H 7.34 0.02 1 72 15 HIS HA H 4.57 0.02 1 73 15 HIS HB2 H 3.72 0.02 2 74 15 HIS HB3 H 2.58 0.02 2 75 15 HIS HD2 H 7.54 0.02 1 76 15 HIS HE1 H 8.86 0.02 1 77 16 GLY H H 7.62 0.02 1 78 16 GLY HA2 H 3.94 0.02 2 79 16 GLY HA3 H 4.13 0.02 2 80 17 LEU H H 7.18 0.02 1 81 17 LEU HA H 3.91 0.02 1 82 17 LEU HB2 H 0.72 0.02 2 83 17 LEU HB3 H 0.26 0.02 2 84 17 LEU HG H 0.69 0.02 1 85 17 LEU HD1 H -0.68 0.02 2 86 17 LEU HD2 H -0.11 0.02 2 87 18 ASP H H 8.82 0.02 1 88 18 ASP HA H 4.26 0.02 1 89 18 ASP HB2 H 3.03 0.02 2 90 18 ASP HB3 H 2.39 0.02 2 91 19 ASN H H 8.42 0.02 1 92 19 ASN HA H 3.96 0.02 1 93 19 ASN HB2 H 2.86 0.02 2 94 19 ASN HB3 H 3.06 0.02 2 95 19 ASN HD21 H 7.47 0.02 2 96 19 ASN HD22 H 6.63 0.02 2 97 20 TYR H H 8.15 0.02 1 98 20 TYR HA H 4.22 0.02 1 99 20 TYR HB2 H 3.05 0.02 2 100 20 TYR HB3 H 3.23 0.02 2 101 20 TYR HD1 H 7.18 0.02 1 102 20 TYR HD2 H 7.18 0.02 1 103 20 TYR HE1 H 6.96 0.02 1 104 20 TYR HE2 H 6.96 0.02 1 105 21 ARG H H 9.02 0.02 1 106 21 ARG HA H 3.63 0.02 1 107 21 ARG HB2 H 1.87 0.02 2 108 21 ARG HB3 H 2.19 0.02 2 109 21 ARG HG2 H 1.42 0.02 2 110 21 ARG HG3 H 1.23 0.02 2 111 21 ARG HD2 H 3.08 0.02 2 112 21 ARG HE H 7.16 0.02 1 113 22 GLY H H 7.63 0.02 1 114 22 GLY HA2 H 3.87 0.02 2 115 22 GLY HA3 H 3.49 0.02 2 116 23 TYR H H 7.67 0.02 1 117 23 TYR HA H 4.56 0.02 1 118 23 TYR HB2 H 3.30 0.02 2 119 23 TYR HB3 H 2.46 0.02 2 120 23 TYR HD1 H 7.03 0.02 1 121 23 TYR HD2 H 7.03 0.02 1 122 23 TYR HE1 H 6.71 0.02 1 123 23 TYR HE2 H 6.71 0.02 1 124 24 SER H H 9.10 0.02 1 125 24 SER HA H 4.51 0.02 1 126 24 SER HB2 H 4.19 0.02 2 127 24 SER HB3 H 4.37 0.02 2 128 25 LEU H H 9.12 0.02 1 129 25 LEU HA H 4.38 0.02 1 130 25 LEU HB2 H 1.65 0.02 2 131 25 LEU HG H 1.60 0.02 1 132 25 LEU HD1 H 0.87 0.02 2 133 25 LEU HD2 H 1.01 0.02 2 134 26 GLY H H 9.66 0.02 1 135 26 GLY HA2 H 4.18 0.02 2 136 26 GLY HA3 H 3.67 0.02 2 137 27 ASN H H 8.20 0.02 1 138 27 ASN HA H 4.19 0.02 1 139 27 ASN HB2 H 2.88 0.02 2 140 27 ASN HB3 H 2.32 0.02 2 141 27 ASN HD21 H 7.76 0.02 2 142 27 ASN HD22 H 7.85 0.02 2 143 28 TRP H H 7.19 0.02 1 144 28 TRP HA H 3.74 0.02 1 145 28 TRP HB2 H 3.27 0.02 2 146 28 TRP HD1 H 7.27 0.02 1 147 28 TRP HE1 H 9.33 0.02 1 148 28 TRP HE3 H 6.70 0.02 1 149 28 TRP HZ2 H 7.44 0.02 1 150 28 TRP HZ3 H 6.20 0.02 1 151 28 TRP HH2 H 6.77 0.02 1 152 29 VAL H H 7.57 0.02 1 153 29 VAL HA H 3.44 0.02 1 154 29 VAL HB H 1.95 0.02 1 155 29 VAL HG1 H 1.26 0.02 2 156 29 VAL HG2 H 0.95 0.02 2 157 30 CYS H H 8.05 0.02 1 158 30 CYS HA H 2.52 0.02 1 159 30 CYS HB2 H 2.94 0.02 2 160 30 CYS HB3 H 2.63 0.02 2 161 31 ALA H H 8.16 0.02 1 162 31 ALA HA H 3.70 0.02 1 163 31 ALA HB H 1.00 0.02 1 164 32 ALA H H 7.58 0.02 1 165 32 ALA HA H 4.02 0.02 1 166 32 ALA HB H 1.31 0.02 1 167 33 LYS H H 8.00 0.02 1 168 33 LYS HA H 2.53 0.02 1 169 33 LYS HB2 H 1.06 0.02 2 170 33 LYS HG2 H 0.43 0.02 2 171 33 LYS HG3 H -0.50 0.02 2 172 33 LYS HD2 H 0.69 0.02 2 173 33 LYS HD3 H 0.62 0.02 2 174 33 LYS HE2 H 2.65 0.02 2 175 33 LYS HE3 H 2.30 0.02 2 176 33 LYS HZ H 7.33 0.02 1 177 34 PHE H H 7.42 0.02 1 178 34 PHE HA H 4.31 0.02 1 179 34 PHE HB2 H 2.28 0.02 2 180 34 PHE HB3 H 3.18 0.02 2 181 34 PHE HD1 H 7.22 0.02 1 182 34 PHE HD2 H 7.22 0.02 1 183 34 PHE HE1 H 7.37 0.02 1 184 34 PHE HE2 H 7.37 0.02 1 185 34 PHE HZ H 7.51 0.02 1 186 35 GLU H H 8.60 0.02 1 187 35 GLU HA H 4.45 0.02 1 188 35 GLU HB2 H 2.05 0.02 2 189 36 SER H H 8.04 0.02 1 190 36 SER HA H 4.56 0.02 1 191 36 SER HB2 H 4.43 0.02 2 192 36 SER HB3 H 3.58 0.02 2 193 37 ASN H H 8.18 0.02 1 194 37 ASN HA H 4.52 0.02 1 195 37 ASN HB2 H 3.29 0.02 2 196 37 ASN HB3 H 2.46 0.02 2 197 37 ASN HD21 H 7.38 0.02 2 198 37 ASN HD22 H 6.72 0.02 2 199 38 PHE H H 7.36 0.02 1 200 38 PHE HA H 3.87 0.02 1 201 38 PHE HB2 H 3.84 0.02 2 202 38 PHE HB3 H 3.62 0.02 2 203 38 PHE HD1 H 6.97 0.02 1 204 38 PHE HD2 H 6.97 0.02 1 205 38 PHE HE1 H 7.42 0.02 1 206 38 PHE HE2 H 7.42 0.02 1 207 38 PHE HZ H 6.97 0.02 1 208 39 ASN H H 7.60 0.02 1 209 39 ASN HA H 4.95 0.02 1 210 39 ASN HB2 H 3.43 0.02 2 211 39 ASN HB3 H 2.96 0.02 2 212 39 ASN HD21 H 7.61 0.02 2 213 39 ASN HD22 H 7.03 0.02 2 214 41 GLN H H 8.05 0.02 1 215 41 GLN HA H 4.52 0.02 1 216 41 GLN HB2 H 2.46 0.02 2 217 41 GLN HB3 H 1.91 0.02 2 218 41 GLN HE21 H 7.66 0.02 2 219 41 GLN HE22 H 6.84 0.02 2 220 42 ALA H H 6.85 0.02 1 221 42 ALA HA H 4.12 0.02 1 222 42 ALA HB H 1.33 0.02 1 223 43 THR H H 8.38 0.02 1 224 43 THR HA H 5.14 0.02 1 225 43 THR HB H 3.73 0.02 1 226 43 THR HG2 H 1.05 0.02 1 227 44 ASN H H 8.16 0.02 1 228 44 ASN HA H 5.02 0.02 1 229 44 ASN HB2 H 2.69 0.02 2 230 44 ASN HD21 H 7.42 0.02 2 231 44 ASN HD22 H 6.91 0.02 2 232 45 ARG H H 8.94 0.02 1 233 45 ARG HA H 4.50 0.02 1 234 45 ARG HB2 H 1.71 0.02 2 235 45 ARG HB3 H 1.83 0.02 2 236 45 ARG HG2 H 1.63 0.02 2 237 45 ARG HD2 H 3.14 0.02 2 238 45 ARG HE H 7.10 0.02 1 239 46 ASN H H 8.96 0.02 1 240 46 ASN HA H 5.12 0.02 1 241 46 ASN HB2 H 2.83 0.02 2 242 46 ASN HD21 H 6.96 0.02 2 243 46 ASN HD22 H 6.88 0.02 2 244 47 THR H H 8.88 0.02 1 245 47 THR HA H 4.11 0.02 1 246 47 THR HB H 4.37 0.02 1 247 47 THR HG2 H 1.35 0.02 1 248 48 ASP H H 7.87 0.02 1 249 48 ASP HA H 4.58 0.02 1 250 48 ASP HB2 H 2.68 0.02 2 251 48 ASP HB3 H 3.10 0.02 2 252 49 GLY H H 7.91 0.02 1 253 49 GLY HA2 H 4.41 0.02 2 254 49 GLY HA3 H 3.74 0.02 2 255 50 SER H H 8.30 0.02 1 256 50 SER HA H 4.57 0.02 1 257 50 SER HB2 H 3.78 0.02 2 258 50 SER HB3 H 4.26 0.02 2 259 51 THR H H 9.23 0.02 1 260 51 THR HA H 4.89 0.02 1 261 51 THR HB H 3.78 0.02 1 262 51 THR HG2 H 0.31 0.02 1 263 52 ASP H H 8.79 0.02 1 264 52 ASP HA H 5.20 0.02 1 265 52 ASP HB2 H 2.63 0.02 2 266 52 ASP HB3 H 2.01 0.02 2 267 53 TYR H H 9.04 0.02 1 268 53 TYR HA H 4.78 0.02 1 269 53 TYR HB2 H 2.96 0.02 2 270 53 TYR HB3 H 2.63 0.02 2 271 53 TYR HD1 H 7.10 0.02 1 272 53 TYR HD2 H 7.10 0.02 1 273 53 TYR HE1 H 6.83 0.02 1 274 53 TYR HE2 H 6.83 0.02 1 275 54 GLY H H 9.15 0.02 1 276 54 GLY HA2 H 4.46 0.02 2 277 54 GLY HA3 H 4.09 0.02 2 278 55 ILE H H 9.47 0.02 1 279 55 ILE HA H 4.28 0.02 1 280 55 ILE HB H 1.65 0.02 1 281 55 ILE HG12 H 1.08 0.02 2 282 55 ILE HG13 H 1.49 0.02 2 283 55 ILE HG2 H 0.92 0.02 1 284 55 ILE HD1 H 0.76 0.02 1 285 56 LEU H H 8.98 0.02 1 286 56 LEU HA H 4.42 0.02 1 287 56 LEU HB2 H 1.70 0.02 2 288 56 LEU HB3 H 1.53 0.02 2 289 56 LEU HG H 1.19 0.02 1 290 56 LEU HD1 H 0.53 0.02 2 291 56 LEU HD2 H 0.30 0.02 2 292 57 GLN H H 8.01 0.02 1 293 57 GLN HA H 3.38 0.02 1 294 57 GLN HB2 H 2.13 0.02 2 295 57 GLN HB3 H 2.22 0.02 2 296 57 GLN HG2 H 0.82 0.02 2 297 57 GLN HE21 H 5.23 0.02 2 298 57 GLN HE22 H 8.25 0.02 2 299 58 ILE H H 7.67 0.02 1 300 58 ILE HA H 4.03 0.02 1 301 58 ILE HB H 1.85 0.02 1 302 58 ILE HG12 H 1.78 0.02 2 303 58 ILE HG2 H 1.06 0.02 1 304 58 ILE HD1 H 0.97 0.02 1 305 59 ASN H H 8.65 0.02 1 306 59 ASN HA H 5.65 0.02 1 307 59 ASN HB2 H 3.05 0.02 2 308 59 ASN HB3 H 3.38 0.02 2 309 59 ASN HD21 H 7.70 0.02 2 310 59 ASN HD22 H 8.68 0.02 2 311 60 SER H H 9.18 0.02 1 312 60 SER HA H 5.19 0.02 1 313 61 ARG H H 8.78 0.02 1 314 61 ARG HA H 4.10 0.02 1 315 61 ARG HB2 H 1.73 0.02 2 316 61 ARG HB3 H 1.46 0.02 2 317 61 ARG HG2 H 0.98 0.02 2 318 61 ARG HG3 H 0.65 0.02 2 319 61 ARG HD2 H 2.87 0.02 2 320 61 ARG HE H 6.78 0.02 1 321 62 TRP H H 7.25 0.02 1 322 62 TRP HA H 4.39 0.02 1 323 62 TRP HB2 H 1.83 0.02 2 324 62 TRP HB3 H 1.90 0.02 2 325 62 TRP HD1 H 7.08 0.02 1 326 62 TRP HE1 H 10.20 0.02 1 327 62 TRP HE3 H 7.11 0.02 1 328 62 TRP HZ2 H 7.45 0.02 1 329 62 TRP HZ3 H 7.04 0.02 1 330 62 TRP HH2 H 7.19 0.02 1 331 63 TRP H H 7.41 0.02 1 332 63 TRP HA H 4.98 0.02 1 333 63 TRP HB2 H 3.38 0.02 2 334 63 TRP HD1 H 7.65 0.02 1 335 63 TRP HE1 H 10.27 0.02 1 336 63 TRP HE3 H 7.78 0.02 1 337 63 TRP HZ2 H 7.26 0.02 1 338 63 TRP HZ3 H 6.84 0.02 1 339 63 TRP HH2 H 7.10 0.02 1 340 64 CYS H H 7.62 0.02 1 341 64 CYS HA H 5.83 0.02 1 342 64 CYS HB2 H 3.03 0.02 2 343 64 CYS HB3 H 2.54 0.02 2 344 65 ASN H H 8.36 0.02 1 345 65 ASN HA H 5.56 0.02 1 346 65 ASN HB2 H 2.84 0.02 2 347 65 ASN HB3 H 2.47 0.02 2 348 65 ASN HD21 H 7.64 0.02 2 349 65 ASN HD22 H 7.08 0.02 2 350 66 ASP H H 9.85 0.02 1 351 66 ASP HA H 4.98 0.02 1 352 66 ASP HB2 H 3.28 0.02 2 353 66 ASP HB3 H 2.23 0.02 2 354 67 GLY H H 8.32 0.02 1 355 67 GLY HA2 H 4.14 0.02 2 356 67 GLY HA3 H 3.86 0.02 2 357 68 ARG H H 8.11 0.02 1 358 68 ARG HA H 4.78 0.02 1 359 68 ARG HB2 H 1.83 0.02 2 360 68 ARG HG2 H 1.47 0.02 2 361 68 ARG HD2 H 3.12 0.02 2 362 68 ARG HD3 H 3.18 0.02 2 363 68 ARG HE H 7.06 0.02 1 364 69 THR H H 8.28 0.02 1 365 69 THR HA H 4.59 0.02 1 366 69 THR HB H 4.19 0.02 1 367 69 THR HG2 H 0.90 0.02 1 368 70 PRO HB2 H 1.87 0.02 2 369 70 PRO HB3 H 2.29 0.02 2 370 70 PRO HD2 H 3.63 0.02 2 371 70 PRO HD3 H 4.04 0.02 2 372 71 GLY H H 8.77 0.02 1 373 71 GLY HA2 H 3.82 0.02 2 374 71 GLY HA3 H 3.66 0.02 2 375 72 SER H H 7.31 0.02 1 376 72 SER HA H 4.58 0.02 1 377 73 ARG H H 8.06 0.02 1 378 73 ARG HA H 4.23 0.02 1 379 73 ARG HB2 H 1.81 0.02 2 380 73 ARG HG2 H 1.67 0.02 2 381 73 ARG HG3 H 1.52 0.02 2 382 73 ARG HD2 H 2.88 0.02 2 383 73 ARG HE H 7.03 0.02 1 384 74 ASN H H 8.37 0.02 1 385 74 ASN HA H 3.77 0.02 1 386 74 ASN HB2 H 3.08 0.02 2 387 74 ASN HB3 H 2.01 0.02 2 388 74 ASN HD21 H 7.33 0.02 2 389 74 ASN HD22 H 6.24 0.02 2 390 75 LEU H H 9.09 0.02 1 391 75 LEU HA H 4.09 0.02 1 392 75 LEU HB2 H 2.12 0.02 2 393 75 LEU HB3 H 1.48 0.02 2 394 75 LEU HG H 1.65 0.02 1 395 75 LEU HD1 H 0.51 0.02 2 396 75 LEU HD2 H 0.86 0.02 2 397 76 CYS H H 9.54 0.02 1 398 76 CYS HA H 4.45 0.02 1 399 76 CYS HB2 H 3.65 0.02 2 400 77 ASN H H 8.06 0.02 1 401 77 ASN HA H 4.21 0.02 1 402 77 ASN HB2 H 2.50 0.02 2 403 77 ASN HB3 H 3.17 0.02 2 404 77 ASN HD21 H 7.47 0.02 2 405 77 ASN HD22 H 6.80 0.02 2 406 78 ILE H H 8.87 0.02 1 407 78 ILE HA H 4.98 0.02 1 408 78 ILE HB H 1.68 0.02 1 409 78 ILE HG12 H 1.07 0.02 2 410 78 ILE HG13 H 1.48 0.02 2 411 78 ILE HG2 H 0.88 0.02 1 412 78 ILE HD1 H 0.90 0.02 1 413 79 PRO HA H 5.17 0.02 1 414 79 PRO HB2 H 2.35 0.02 2 415 79 PRO HB3 H 2.02 0.02 2 416 79 PRO HG2 H 2.10 0.02 2 417 79 PRO HG3 H 2.03 0.02 2 418 79 PRO HD2 H 3.83 0.02 2 419 79 PRO HD3 H 3.66 0.02 2 420 80 CYS H H 8.28 0.02 1 421 80 CYS HA H 3.88 0.02 1 422 80 CYS HB2 H 1.73 0.02 2 423 80 CYS HB3 H 1.27 0.02 2 424 81 SER H H 8.61 0.02 1 425 81 SER HA H 3.78 0.02 1 426 82 ALA H H 7.62 0.02 1 427 82 ALA HA H 4.23 0.02 1 428 82 ALA HB H 1.49 0.02 1 429 83 LEU H H 7.86 0.02 1 430 83 LEU HA H 4.27 0.02 1 431 83 LEU HB2 H 2.07 0.02 2 432 83 LEU HB3 H 1.58 0.02 2 433 83 LEU HG H 1.65 0.02 1 434 83 LEU HD1 H 0.72 0.02 2 435 83 LEU HD2 H 1.03 0.02 2 436 84 LEU H H 7.10 0.02 1 437 84 LEU HA H 5.00 0.02 1 438 84 LEU HB2 H 1.92 0.02 2 439 84 LEU HB3 H 1.73 0.02 2 440 84 LEU HG H 1.68 0.02 1 441 84 LEU HD1 H 0.97 0.02 2 442 84 LEU HD2 H 1.04 0.02 2 443 85 SER H H 6.87 0.02 1 444 85 SER HA H 4.51 0.02 1 445 85 SER HB2 H 4.13 0.02 2 446 85 SER HB3 H 3.83 0.02 2 447 86 SER H H 8.48 0.02 1 448 86 SER HA H 4.22 0.02 1 449 86 SER HB2 H 3.83 0.02 2 450 86 SER HB3 H 3.93 0.02 2 451 87 ASP H H 8.22 0.02 1 452 87 ASP HA H 4.93 0.02 1 453 87 ASP HB2 H 2.94 0.02 2 454 87 ASP HB3 H 2.63 0.02 2 455 88 ILE H H 8.11 0.02 1 456 88 ILE HA H 4.69 0.02 1 457 88 ILE HB H 1.82 0.02 1 458 88 ILE HG12 H 0.35 0.02 2 459 88 ILE HG13 H 1.14 0.02 2 460 88 ILE HG2 H 0.78 0.02 1 461 88 ILE HD1 H 0.20 0.02 1 462 89 THR H H 8.44 0.02 1 463 89 THR HA H 3.05 0.02 1 464 89 THR HB H 4.04 0.02 1 465 89 THR HG2 H 1.16 0.02 1 466 90 ALA H H 9.20 0.02 1 467 90 ALA HA H 4.08 0.02 1 468 90 ALA HB H 1.35 0.02 1 469 91 SER H H 7.77 0.02 1 470 91 SER HA H 4.09 0.02 1 471 91 SER HB2 H 3.98 0.02 2 472 91 SER HB3 H 3.47 0.02 2 473 92 VAL H H 8.42 0.02 1 474 92 VAL HA H 3.10 0.02 1 475 92 VAL HB H 1.90 0.02 1 476 92 VAL HG1 H 0.48 0.02 2 477 92 VAL HG2 H 0.62 0.02 2 478 93 ASN H H 8.70 0.02 1 479 93 ASN HA H 4.26 0.02 1 480 93 ASN HB2 H 2.90 0.02 2 481 93 ASN HB3 H 2.77 0.02 2 482 93 ASN HD21 H 7.68 0.02 2 483 93 ASN HD22 H 6.99 0.02 2 484 94 CYS H H 7.88 0.02 1 485 94 CYS HA H 5.01 0.02 1 486 94 CYS HB2 H 3.38 0.02 2 487 94 CYS HB3 H 2.72 0.02 2 488 95 ALA H H 8.76 0.02 1 489 95 ALA HA H 4.10 0.02 1 490 95 ALA HB H 1.53 0.02 1 491 96 LYS H H 8.06 0.02 1 492 96 LYS HA H 3.72 0.02 1 493 96 LYS HB2 H 1.67 0.02 2 494 96 LYS HB3 H 1.10 0.02 2 495 96 LYS HG2 H -0.48 0.02 2 496 96 LYS HD2 H 1.27 0.02 2 497 96 LYS HE2 H 2.05 0.02 2 498 97 LYS H H 7.22 0.02 1 499 97 LYS HA H 4.14 0.02 1 500 97 LYS HB2 H 2.18 0.02 2 501 98 ILE H H 8.01 0.02 1 502 98 ILE HA H 2.78 0.02 1 503 98 ILE HB H 1.48 0.02 1 504 98 ILE HG12 H -2.12 0.02 2 505 98 ILE HG13 H 0.67 0.02 2 506 98 ILE HG2 H -0.30 0.02 1 507 98 ILE HD1 H -0.03 0.02 1 508 99 VAL H H 8.35 0.02 1 509 99 VAL HA H 3.89 0.02 1 510 99 VAL HB H 2.42 0.02 1 511 99 VAL HG1 H 1.16 0.02 2 512 99 VAL HG2 H 1.36 0.02 2 513 100 SER H H 7.61 0.02 1 514 100 SER HA H 4.48 0.02 1 515 101 ASP H H 7.99 0.02 1 516 101 ASP HA H 4.78 0.02 1 517 101 ASP HB2 H 3.12 0.02 2 518 102 GLY H H 8.24 0.02 1 519 102 GLY HA2 H 3.93 0.02 2 520 102 GLY HA3 H 4.24 0.02 2 521 103 ASN H H 8.21 0.02 1 522 103 ASN HA H 4.98 0.02 1 523 103 ASN HB2 H 2.72 0.02 2 524 103 ASN HB3 H 2.82 0.02 2 525 103 ASN HD21 H 7.56 0.02 2 526 103 ASN HD22 H 6.93 0.02 2 527 104 GLY H H 8.31 0.02 1 528 104 GLY HA2 H 4.09 0.02 2 529 104 GLY HA3 H 4.24 0.02 2 530 105 MET H H 7.14 0.02 1 531 105 MET HA H 3.83 0.02 1 532 105 MET HB2 H -1.05 0.02 2 533 105 MET HB3 H 0.44 0.02 2 534 105 MET HG2 H 0.52 0.02 2 535 105 MET HG3 H -0.07 0.02 2 536 106 ASN H H 7.70 0.02 1 537 106 ASN HA H 4.46 0.02 1 538 106 ASN HB2 H 3.06 0.02 2 539 106 ASN HB3 H 2.81 0.02 2 540 106 ASN HD21 H 7.54 0.02 2 541 106 ASN HD22 H 7.18 0.02 2 542 107 ALA H H 6.71 0.02 1 543 107 ALA HA H 3.84 0.02 1 544 107 ALA HB H 0.62 0.02 1 545 108 TRP H H 7.90 0.02 1 546 108 TRP HA H 4.66 0.02 1 547 108 TRP HB2 H 3.37 0.02 2 548 108 TRP HB3 H 3.26 0.02 2 549 108 TRP HD1 H 7.06 0.02 1 550 108 TRP HE1 H 10.04 0.02 1 551 108 TRP HE3 H 7.37 0.02 1 552 108 TRP HZ2 H 6.92 0.02 1 553 108 TRP HZ3 H 6.48 0.02 1 554 108 TRP HH2 H 7.25 0.02 1 555 109 VAL H H 8.99 0.02 1 556 109 VAL HA H 3.62 0.02 1 557 109 VAL HB H 2.17 0.02 1 558 109 VAL HG1 H 1.03 0.02 2 559 109 VAL HG2 H 1.12 0.02 2 560 110 ALA H H 8.03 0.02 1 561 110 ALA HA H 4.26 0.02 1 562 110 ALA HB H 1.31 0.02 1 563 111 TRP H H 7.25 0.02 1 564 111 TRP HA H 3.71 0.02 1 565 111 TRP HB2 H 4.08 0.02 2 566 111 TRP HB3 H 2.78 0.02 2 567 111 TRP HD1 H 7.03 0.02 1 568 111 TRP HE1 H 10.44 0.02 1 569 111 TRP HE3 H 7.28 0.02 1 570 111 TRP HZ2 H 7.51 0.02 1 571 111 TRP HZ3 H 7.04 0.02 1 572 111 TRP HH2 H 7.37 0.02 1 573 112 ARG H H 8.29 0.02 1 574 112 ARG HA H 3.37 0.02 1 575 112 ARG HB2 H 1.97 0.02 2 576 112 ARG HB3 H 2.12 0.02 2 577 112 ARG HG2 H 1.82 0.02 2 578 112 ARG HD2 H 3.36 0.02 2 579 112 ARG HD3 H 3.44 0.02 2 580 112 ARG HE H 7.31 0.02 1 581 113 ASN H H 8.01 0.02 1 582 113 ASN HA H 4.50 0.02 1 583 113 ASN HB2 H 2.68 0.02 2 584 113 ASN HD21 H 7.61 0.02 2 585 113 ASN HD22 H 6.88 0.02 2 586 114 ARG H H 7.67 0.02 1 587 114 ARG HA H 4.31 0.02 1 588 114 ARG HB2 H 1.17 0.02 2 589 114 ARG HB3 H 0.57 0.02 2 590 114 ARG HG2 H 1.07 0.02 2 591 114 ARG HG3 H 1.01 0.02 2 592 114 ARG HD2 H 2.63 0.02 2 593 114 ARG HD3 H 2.76 0.02 2 594 114 ARG HE H 7.03 0.02 1 595 115 CYS H H 7.36 0.02 1 596 115 CYS HA H 4.53 0.02 1 597 115 CYS HB2 H 2.48 0.02 2 598 115 CYS HB3 H 2.59 0.02 2 599 116 LYS H H 7.08 0.02 1 600 116 LYS HA H 3.44 0.02 1 601 116 LYS HB2 H 1.23 0.02 2 602 116 LYS HB3 H -0.24 0.02 2 603 116 LYS HG2 H 1.05 0.02 2 604 117 GLY H H 8.75 0.02 1 605 117 GLY HA2 H 4.13 0.02 2 606 117 GLY HA3 H 3.80 0.02 2 607 118 THR H H 7.67 0.02 1 608 118 THR HA H 4.75 0.02 1 609 118 THR HB H 4.30 0.02 1 610 118 THR HG2 H 0.95 0.02 1 611 119 ASP H H 8.74 0.02 1 612 119 ASP HA H 5.00 0.02 1 613 119 ASP HB2 H 2.74 0.02 2 614 119 ASP HB3 H 2.95 0.02 2 615 120 VAL H H 8.17 0.02 1 616 120 VAL HA H 4.35 0.02 1 617 120 VAL HB H 2.17 0.02 1 618 120 VAL HG1 H 1.08 0.02 2 619 120 VAL HG2 H 1.12 0.02 2 620 121 GLN H H 8.50 0.02 1 621 121 GLN HA H 4.33 0.02 1 622 121 GLN HB2 H 2.25 0.02 2 623 121 GLN HE21 H 7.73 0.02 2 624 121 GLN HE22 H 6.96 0.02 2 625 122 ALA H H 7.72 0.02 1 626 122 ALA HA H 3.81 0.02 1 627 122 ALA HB H 1.16 0.02 1 628 123 TRP H H 7.62 0.02 1 629 123 TRP HA H 4.10 0.02 1 630 123 TRP HB2 H 3.41 0.02 2 631 123 TRP HB3 H 3.50 0.02 2 632 123 TRP HD1 H 7.56 0.02 1 633 123 TRP HE1 H 10.79 0.02 1 634 123 TRP HE3 H 7.49 0.02 1 635 123 TRP HZ2 H 7.78 0.02 1 636 123 TRP HZ3 H 7.13 0.02 1 637 123 TRP HH2 H 7.11 0.02 1 638 124 ILE H H 7.56 0.02 1 639 124 ILE HA H 4.75 0.02 1 640 124 ILE HB H 2.22 0.02 1 641 124 ILE HG12 H 1.24 0.02 2 642 124 ILE HG13 H 1.44 0.02 2 643 124 ILE HG2 H 0.82 0.02 1 644 124 ILE HD1 H 0.96 0.02 1 645 125 ARG H H 7.34 0.02 1 646 125 ARG HA H 4.15 0.02 1 647 125 ARG HB2 H 1.81 0.02 2 648 125 ARG HB3 H 2.00 0.02 2 649 125 ARG HD2 H 3.15 0.02 2 650 125 ARG HD3 H 3.19 0.02 2 651 125 ARG HE H 7.35 0.02 1 652 126 GLY H H 9.20 0.02 1 653 126 GLY HA2 H 4.29 0.02 2 654 126 GLY HA3 H 3.74 0.02 2 655 127 CYS H H 7.47 0.02 1 656 127 CYS HA H 4.91 0.02 1 657 127 CYS HB2 H 3.09 0.02 2 658 127 CYS HB3 H 2.63 0.02 2 659 128 ARG H H 8.98 0.02 1 660 128 ARG HA H 4.34 0.02 1 661 128 ARG HB2 H 1.79 0.02 2 662 128 ARG HD2 H 3.21 0.02 2 663 128 ARG HE H 7.17 0.02 1 664 129 LEU H H 8.03 0.02 1 665 129 LEU HA H 4.28 0.02 1 666 129 LEU HB2 H 1.66 0.02 2 667 129 LEU HB3 H 1.46 0.02 2 668 129 LEU HG H 1.40 0.02 1 669 129 LEU HD1 H 0.74 0.02 2 670 129 LEU HD2 H 0.86 0.02 2 stop_ save_