data_5142 #Corrected using PDB structure: 1IWTA # #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 # 5 R HA 4.30 3.37 # 33 K HA 4.15 2.76 # 66 N HA 5.66 4.91 # 75 N HA 3.86 5.03 # 95 C HA 4.94 4.19 # #After reference correction, the following residues still #have a CA chemical shift difference (obs*-pred) greater than 5.0ppm: #NUM AA CS Observed* Predicted # 6 C CA 54.39 59.71 #128 C CA 51.93 57.13 # #After reference correction, the following residues still #have a CB chemical shift difference (obs*-pred) greater than 5.0ppm: #NUM AA CS Observed* Predicted # 6 C CB 32.62 40.55 #128 C CB 35.10 40.63 # #After reference correction, the following residues still #have a N chemical shift difference (obs*-pred) greater than 10.0ppm: #NUM AA CS Observed* Predicted #112 W N 114.22 126.54 # #The average CS difference between predicted and observed: #HA CA CB CO N HN #-0.04 -0.63 -0.54 -0.13 -0.59 -0.09 # #bmr5142.str.corr chemical shifts have been re-referenced with the following #offsets (these values have been added to the original bmr5142.str file): #HA CA CB CO N HN #N/A -0.58 -0.58 -0.13 -0.59 N/A # #The 95% confidence intervals for the above recommended offsets are: # HA CA CB CO N HN #+/-0.02 +/-0.17 +/-0.17 +/-0.16 +/-0.30 +/-0.05 # #The Correlation Coefficients between predicted and observed #chemical shifts are: #HA CA CB CO N HN #0.860 0.957 0.992 0.773 0.858 0.752 # #The RMSD between predicted and observed* (reference #corrected) chemical shifts are: #HA CA CB CO N HN #0.124 0.953 0.913 0.897 1.696 0.295 # ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Assignment of 1H, 13C and 15N resonances of Human Lysozyme at 4 C ; loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Kumeta Hiroyuki . . 2 Kobashigawa Yoshihiro . . 3 Miura Kazunori . . 4 Nishimiya Yoshiyuki . . 5 Oka Chitoshi . . 6 Nemoto Nobuaki . . 7 Miura Ai . . 8 Nitta Katsutoshi . . 9 Tsuda Sakae . . stop_ _BMRB_accession_number 5142 _BMRB_flat_file_name bmr5142.str _Entry_type new _Submission_date 2001-09-06 _Accession_date 2001-09-07 _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' 584 '15N chemical shifts' 127 '13C chemical shifts' 374 stop_ loop_ _Related_BMRB_accession_number _Relationship 5130 "human lysozyme at 35 C" stop_ save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_title ; Letter to the Editor: Assignments of 1H, 13C and 15N Resonances of Human Lysozyme at 4 degrees C ; _Citation_status published _Citation_type journal _MEDLINE_UI_code 21880664 _PubMed_ID 11883780 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Kumeta Hiroyuki . . 2 Kobashigawa Yoshihiro . . 3 Miura Kazunori . . 4 Nishimiya Yoshiyuki . . 5 Oka Chitoshi . . 6 Nemoto Nobuaki . . 7 Miura Ai . . 8 Nitta Katsutoshi . . 9 Tsuda Sakae . . stop_ _Journal_abbreviation "J. Biomol. NMR" _Journal_volume 22 _Journal_issue 2 _Page_first 183 _Page_last 184 _Year 2002 save_ ################################## # Molecular system description # ################################## save_system_human_lysozyme _Saveframe_category molecular_system _Mol_system_name "human lysozyme" _Abbreviation_common "human lysozyme" _Enzyme_commission_number 3.2.1.17 loop_ _Mol_system_component_name _Mol_label "human lysozyme" $human_lysozyme stop_ _System_physical_state native _System_oligomer_state monomer _System_paramagnetic no _System_thiol_state 'all disulfide bound' save_ ######################## # Monomeric polymers # ######################## save_human_lysozyme _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common "human lysozyme" _Name_variant . _Abbreviation_common "human lysozyme" _Mol_thiol_state 'all disulfide bound' ############################## # Polymer residue sequence # ############################## _Residue_count 130 _Mol_residue_sequence ; KVFERCELARTLKRLGMDGY RGISLANWMCLAKWESGYNT RATNYNAGDRSTDYGIFQIN SRYWCNDGKTPGAVNACHLS CSALLQDNIADAVACAKRVV RDPQGIRAWVAWRNRCQNRD VRQYVQGCGV ; loop_ _Residue_seq_code _Residue_label 1 LYS 2 VAL 3 PHE 4 GLU 5 ARG 6 CYS 7 GLU 8 LEU 9 ALA 10 ARG 11 THR 12 LEU 13 LYS 14 ARG 15 LEU 16 GLY 17 MET 18 ASP 19 GLY 20 TYR 21 ARG 22 GLY 23 ILE 24 SER 25 LEU 26 ALA 27 ASN 28 TRP 29 MET 30 CYS 31 LEU 32 ALA 33 LYS 34 TRP 35 GLU 36 SER 37 GLY 38 TYR 39 ASN 40 THR 41 ARG 42 ALA 43 THR 44 ASN 45 TYR 46 ASN 47 ALA 48 GLY 49 ASP 50 ARG 51 SER 52 THR 53 ASP 54 TYR 55 GLY 56 ILE 57 PHE 58 GLN 59 ILE 60 ASN 61 SER 62 ARG 63 TYR 64 TRP 65 CYS 66 ASN 67 ASP 68 GLY 69 LYS 70 THR 71 PRO 72 GLY 73 ALA 74 VAL 75 ASN 76 ALA 77 CYS 78 HIS 79 LEU 80 SER 81 CYS 82 SER 83 ALA 84 LEU 85 LEU 86 GLN 87 ASP 88 ASN 89 ILE 90 ALA 91 ASP 92 ALA 93 VAL 94 ALA 95 CYS 96 ALA 97 LYS 98 ARG 99 VAL 100 VAL 101 ARG 102 ASP 103 PRO 104 GLN 105 GLY 106 ILE 107 ARG 108 ALA 109 TRP 110 VAL 111 ALA 112 TRP 113 ARG 114 ASN 115 ARG 116 CYS 117 GLN 118 ASN 119 ARG 120 ASP 121 VAL 122 ARG 123 GLN 124 TYR 125 VAL 126 GLN 127 GLY 128 CYS 129 GLY 130 VAL 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 1DI4 "A Chain A, Role Of Amino Acid Residues At TurnsIn The Conformational Stability And Folding Of HumanLysozyme" 101.56 128 98 98 7e-73 PDB 1DI5 "A Chain A, Role Of Amino Acid Residues At TurnsIn The Conformational Stability And Folding Of HumanLysozyme" 100.78 129 99 99 10e-74 PDB 1C43 "A Chain A, Mutant Human Lysozyme With ForeignN-Terminal Residues" 100.00 130 100 100 5e-75 PDB 1C45 "A Chain A, Mutant Human Lysozyme With ForeignN-Terminal Residues" 100.00 130 100 100 5e-75 PDB 1IWT "A Chain A, Crystal Structure Analysis Of HumanLysozyme At 113k." 100.00 130 100 100 1e-75 PDB 1IWU "A Chain A, Crystal Structure Analysis Of HumanLysozyme At 127k." 100.00 130 100 100 1e-75 PDB 1IWV "A Chain A, Crystal Structure Analysis Of HumanLysozyme At 147k." 100.00 130 100 100 1e-75 PDB 1IWW "A Chain A, Crystal Structure Analysis Of HumanLysozyme At 152k." 100.00 130 100 100 1e-75 PDB 1IWX "A Chain A, Crystal Structure Analysis Of HumanLysozyme At 161k." 100.00 130 100 100 1e-75 PDB 1IWY "A Chain A, Crystal Structure Analysis Of HumanLysozyme At 170k." 100.00 130 100 100 1e-75 PDB 1IWZ "A Chain A, Crystal Structure Analysis Of HumanLysozyme At 178k." 100.00 130 100 100 1e-75 PDB 1IY3 "A Chain A, Solution Structure Of The HumanLysozyme At 4 Degree C" 100.00 130 100 100 1e-75 PDB 1IY4 "A Chain A, Solution Structure Of The HumanLysozyme At 35 Degree C" 100.00 130 100 100 1e-75 PDB 1JSF "Full-Matrix Least-Squares Refinement Of HumanLysozyme" 100.00 130 100 100 1e-75 PDB 1JWR "A Chain A, Crystal Structure Of Human LysozymeAt 100 K" 100.00 130 100 100 1e-75 PDB 1LZ1 "Lysozyme (E.C.3.2.1.17)" 100.00 130 100 100 1e-75 PDB 1LZR "Lysozyme (Lz406) (E.C.3.2.1.17) ComplexedWith Tetra-Acetyl-Chitotetraose" 100.00 130 100 100 1e-75 PDB 1LZS "A Chain A, Lysozyme (Lz604) (E.C.3.2.1.17)Complexed With N-Acetylchitose Oligomers" 100.00 130 100 100 1e-75 PDB 1OP9 "B Chain B, Complex Of Human Lysozyme WithCamelid Vhh Hl6 Antibody Fragment" 100.00 130 100 100 1e-75 PDB 1OUF "Contribution Of Hydrophobic Residues To TheStability Of Human Lysozyme: X-Ray Structure Of TheV130a Mutant" 100.00 130 100 100 4e-75 PDB 1RE2 "A Chain A, Human Lysozyme Labelled With Two2',3'-Epoxypropyl Beta- Glycoside Of N-Acetyllactosamine" 100.00 130 100 100 1e-75 PDB 1REM "Human Lysozyme With Man-B1,4-GlcnacCovalently Attached To Asp53" 100.00 130 100 100 1e-75 PDB 1REX "Native Human Lysozyme" 100.00 130 100 100 1e-75 PDB 1REY "Human Lysozyme-N,N'-DiacetylchitobioseComplex" 100.00 130 100 100 1e-75 PDB 1REZ "Human Lysozyme-N-Acetyllactosamine Complex" 100.00 130 100 100 1e-75 PDB 133L "Lysozyme (E.C.3.2.1.17) Mutant With Arg 115Replaced By His (R115h)" 100.00 130 99 99 5e-75 PDB 134L "Lysozyme (E.C.3.2.1.17) Mutant With Arg 115Replaced By Glu (R115e)" 100.00 130 99 99 5e-75 PDB 1B5U "A Chain A, Contribution Of Hydrogen Bonds ToThe Conformational Stability Of Human Lysozyme:Calorimetry And X-Ray Analysis Of Six Ser->ala Mutant" 100.00 130 99 100 3e-75 PDB 1B5V "A Chain A, Contribution Of Hydrogen Bonds ToThe Conformational Stability Of Human Lysozyme:Calorimetry And X-Ray Analysis Of Six Ser->ala Mutants" 100.00 130 99 100 3e-75 PDB 1B5W "A Chain A, Contribution Of Hydrogen Bonds ToThe Conformational Stability Of Human Lysozyme:Calorimetry And X-Ray Analysis Of Six Ser->ala Mutants" 100.00 130 99 100 3e-75 PDB 1B5X "A Chain A, Contribution Of Hydrogen Bonds ToThe Conformational Stability Of Human Lysozyme:Calorimetry And X-Ray Analysis Of Six Ser->ala Mutants" 100.00 130 99 100 3e-75 PDB 1B5Y "A Chain A, Contribution Of Hydrogen Bonds ToThe Conformational Stability Of Human Lysozyme:Calorimetry And X-Ray Analysis Of Six Ser->ala Mutants" 100.00 130 99 100 3e-75 PDB 1B5Z "A Chain A, Contribution Of Hydrogen Bonds ToThe Conformational Stability Of Human Lysozyme:Calorimetry And X-Ray Analysis Of Six Ser->ala Mutants" 100.00 130 99 100 3e-75 PDB 1B7L "A Chain A, Verification Of Spmp Using MutantHuman Lysozymes" 100.00 130 99 99 5e-75 PDB 1B7M "A Chain A, Verification Of Spmp Using MutantHuman Lysozymes" 100.00 130 99 99 5e-75 PDB 1B7N "A Chain A, Verification Of Spmp Using MutantHuman Lysozymes" 100.00 130 99 99 10e-75 PDB 1B7O "A Chain A, Verification Of Spmp Using MutantHuman Lysozymes" 100.00 130 99 99 10e-75 PDB 1B7P "A Chain A, Verification Of Spmp Using MutantHuman Lysozymes" 100.00 130 99 99 2e-74 PDB 1B7Q "A Chain A, Verification Of Spmp Using MutantHuman Lysozymes" 100.00 130 99 99 2e-74 PDB 1B7R "A Chain A, Verification Of Spmp Using MutantHuman Lysozymes" 100.00 130 99 99 9e-75 PDB 1B7S "Verification Of Spmp Using Mutant HumanLysozymes" 100.00 130 99 99 7e-75 PDB 1BB3 "A Chain A, Human Lysozyme Mutant A96l" 100.00 130 99 99 5e-75 PDB 1BB5 "A Chain A, Human Lysozyme Mutant A96l ComplexedWith Chitotriose" 100.00 130 99 99 5e-75 PDB 1CJ6 "A Chain A, T11a Mutant Human Lysozyme" 100.00 130 99 99 5e-75 PDB 1CJ7 "A Chain A, T11v Mutant Human Lysozyme" 100.00 130 99 99 5e-75 PDB 1CJ8 "A Chain A, T40a Mutant Human Lysozyme" 100.00 130 99 99 5e-75 PDB 1CJ9 "A Chain A, T40v Mutant Human Lysozyme" 100.00 130 99 99 5e-75 PDB 1CKC "A Chain A, T43a Mutant Human Lysozyme" 100.00 130 99 99 5e-75 PDB 1CKD "A Chain A, T43v Mutant Human Lysozyme" 100.00 130 99 99 5e-75 PDB 1CKF "A Chain A, T52a Mutant Human Lysozyme" 100.00 130 99 99 5e-75 PDB 1CKG "A Chain A, T52v Mutant Human Lysozyme" 100.00 130 99 99 5e-75 PDB 1CKH "A Chain A, T70v Mutant Human Lysozyme" 100.00 130 99 99 5e-75 PDB 1D6P "A Chain A, Human Lysozyme L63 Mutant LabelledWith 2',3'-Epoxypropyl N, N'-Diacetylchitobiose" 100.00 130 99 99 10e-75 PDB 1D6Q "A Chain A, Human Lysozyme E102 Mutant LabelledWith 2',3'-Epoxypropyl Glycoside Of N-Acetyllactosamine" 100.00 130 99 100 4e-75 PDB 1DI3 "A Chain A, Role Of Amino Acid Residues At TurnsIn The Conformational Stability And Folding Of HumanLysozyme" 100.00 130 99 99 9e-75 PDB 1EQ4 "A Chain A, Crystal Structures Of Salt BridgeMutants Of Human Lysozyme" 100.00 130 99 100 3e-75 PDB 1EQ5 "A Chain A, Crystal Structures Of Salt BridgeMutants Of Human Lysozyme" 100.00 130 99 100 5e-75 PDB 1EQE "A Chain A, Crystal Structures Of Salt BridgeMutants Of Human Lysozyme" 100.00 130 99 100 5e-75 PDB 1GAY "A Chain A, Crystal Structure Of Mutant HumanLysozyme Substituted At The Surface Positions" 100.00 130 99 99 9e-75 PDB 1GAZ "A Chain A, Crystal Structure Of Mutant HumanLysozyme Substituted At The Surface Positions" 100.00 130 99 100 2e-75 PDB 1GB0 "A Chain A, Crystal Structure Of Mutant HumanLysozyme Substituted At The Surface Positions" 100.00 130 99 100 3e-75 PDB 1GB2 "A Chain A, Crystal Structure Of Mutant HumanLysozyme Substituted At The Surface Positions" 100.00 130 99 100 3e-75 PDB 1GB3 "A Chain A, Crystal Structure Of Mutant HumanLysozyme Substituted At The Surface Positions" 100.00 130 99 99 5e-75 PDB 1GB5 "A Chain A, Crystal Structure Of Mutant HumanLysozyme Substituted At The Surface Positions" 100.00 130 99 99 9e-75 PDB 1GB6 "A Chain A, Crystal Structure Of Mutant HumanLysozyme Substituted At The Surface Positions" 100.00 130 99 100 2e-75 PDB 1GB7 "A Chain A, Crystal Structure Of Mutant HumanLysozyme Substituted At The Surface Positions" 100.00 130 99 100 3e-75 PDB 1GB8 "A Chain A, Crystal Structure Of Mutant HumanLysozyme Substituted At The Surface Positions" 100.00 130 99 100 3e-75 PDB 1GB9 "A Chain A, Crystal Structure Of Mutant HumanLysozyme Substituted At The Surface Positions" 100.00 130 99 99 5e-75 PDB 1GBO "A Chain A, Crystal Structure Of Mutant HumanLysozyme Substituted At The Surface Positions" 100.00 130 99 99 9e-75 PDB 1GBW "A Chain A, Crystal Structure Of Mutant HumanLysozyme Substituted At The Surface Positions" 100.00 130 99 100 2e-75 PDB 1GBX "A Chain A, Crystal Structure Of Mutant HumanLysozyme Substituted At The Surface Positions" 100.00 130 99 100 3e-75 PDB 1GBY "A Chain A, Crystal Structure Of Mutant HumanLysozyme Substituted At The Surface Positions" 100.00 130 99 100 3e-75 PDB 1GBZ "A Chain A, Crystal Structure Of Mutant HumanLysozyme Substituted At The Surface Positions" 100.00 130 99 99 5e-75 PDB 1GDW "A Chain A, Crystal Structure Of Mutant HumanLysozyme Substituted At Left-Handed Helical Positions" 100.00 130 99 99 9e-75 PDB 1GDX "A Chain A, Crystal Structure Of Mutant HumanLysozyme Substituted At Left-Handed Helical Positions" 100.00 130 99 99 7e-75 PDB 1GE0 "A Chain A, Crystal Structure Of Mutant HumanLysozyme Substituted At Left-Handed Helical Positions" 100.00 130 99 99 2e-74 PDB 1GE1 "A Chain A, Crystal Structure Of Mutant HumanLysozyme Substituted At Left-Handed Helical Positions" 100.00 130 99 99 7e-75 PDB 1GE2 "A Chain A, Crystal Structure Of Mutant HumanLysozyme Substituted At Left-Handed Helical Positions" 100.00 130 99 99 2e-74 PDB 1GE3 "A Chain A, Crystal Structure Of Mutant HumanLysozyme Substituted At Left-Handed Helical Positions" 100.00 130 99 99 7e-75 PDB 1GE4 "A Chain A, Crystal Structure Of Mutant HumanLysozyme Substituted At Left-Handed Helical Positions" 100.00 130 99 99 10e-75 PDB 1GEV "A Chain A, Buried Polar Mutant Human Lysozyme" 100.00 130 99 99 5e-75 PDB 1GEZ "A Chain A, Buried Polar Mutant Human Lysozyme" 100.00 130 99 100 3e-75 PDB 1GF0 "A Chain A, Buried Polar Mutant Human Lysozyme" 100.00 130 99 100 3e-75 PDB 1GF3 "A Chain A, Buried Polar Mutant Human Lysozyme" 100.00 130 99 100 3e-75 PDB 1GF4 "A Chain A, Buried Polar Mutant Human Lysozyme" 100.00 130 99 99 4e-75 PDB 1GF5 "A Chain A, Buried Polar Mutant Human Lysozyme" 100.00 130 99 100 3e-75 PDB 1GF6 "A Chain A, Buried Polar Mutant Human Lysozyme" 100.00 130 99 99 4e-75 PDB 1GF7 "A Chain A, Buried Polar Mutant Human Lysozyme" 100.00 130 99 99 4e-75 PDB 1GF8 "A Chain A, Crystal Structure Of Mutant HumanLysozyme Substituted At The Surface Positions" 100.00 130 99 99 7e-75 PDB 1GF9 "A Chain A, Crystal Structure Of Mutant HumanLysozyme Substituted At The Surface Positions" 100.00 130 99 99 5e-75 PDB 1GFA "A Chain A, Crystal Structure Of Mutant HumanLysozyme Substituted At The Surface Positions" 100.00 130 99 99 9e-75 PDB 1GFE "A Chain A, Crystal Structure Of Mutant HumanLysozyme Substituted At The Surface Positions" 100.00 130 99 99 9e-75 PDB 1GFG "A Chain A, Crystal Structure Of Mutant HumanLysozyme Substituted At The Surface Positions" 100.00 130 99 99 9e-75 PDB 1GFH "A Chain A, Crystal Structure Of Mutant HumanLysozyme Substituted At The Surface Positions" 100.00 130 99 99 5e-75 PDB 1GFJ "A Chain A, Crystal Structure Of Mutant HumanLysozyme Substituted At The Surface Positions" 100.00 130 99 99 9e-75 PDB 1GFK "A Chain A, Crystal Structure Of Mutant HumanLysozyme Substituted At The Surface Positions" 100.00 130 99 99 9e-75 PDB 1GFR "A Chain A, Crystal Structure Of Mutant HumanLysozyme Substituted At The Surface Positions" 100.00 130 99 99 9e-75 PDB 1GFT "A Chain A, Crystal Structure Of Mutant HumanLysozyme Substituted At The Surface Positions" 100.00 130 99 99 5e-75 PDB 1GFU "A Chain A, Crystal Structure Of Mutant HumanLysozyme Substituted At The Surface Positions" 100.00 130 99 99 9e-75 PDB 1GFV "A Chain A, Crystal Structure Of Mutant HumanLysozyme Substituted At The Surface Positions" 100.00 130 99 99 9e-75 PDB 1HNL "Lysozyme (E.C.3.2.1.17) Mutant With Cys 77Replaced By Ala (C77a) Complexed With Glutathione" 100.00 130 99 99 2e-74 PDB 1I1Z "A Chain A, Mutant Human Lysozyme (Q86d)" 100.00 130 99 99 5e-75 PDB 1I20 "A Chain A, Mutant Human Lysozyme (A92d)" 100.00 130 99 99 7e-75 PDB 1INU "A Chain A, Crystal Structure Of Mutant HumanLysozyme Substituted At The Surface Positions" 100.00 130 99 99 9e-75 PDB 1IP1 "A Chain A, G37a Human Lysozyme" 100.00 130 99 99 7e-75 PDB 1IP2 "A Chain A, G48a Human Lysozyme" 100.00 130 99 99 7e-75 PDB 1IP3 "A Chain A, G68a Human Lysozyme" 100.00 130 99 99 7e-75 PDB 1IP4 "A Chain A, G72a Human Lysozyme" 100.00 130 99 99 7e-75 PDB 1IP5 "A Chain A, G105a Human Lysozyme" 100.00 130 99 99 7e-75 PDB 1IP6 "A Chain A, G127a Human Lysozyme" 100.00 130 99 99 7e-75 PDB 1IP7 "A Chain A, G129a Human Lysozyme" 100.00 130 99 99 7e-75 PDB 1JKA "Human Lysozyme Mutant With Glu 35 Replaced ByAsp" 100.00 130 99 100 3e-75 PDB 1JKB "Human Lysozyme Mutant With Glu 35 Replaced ByAla" 100.00 130 99 99 7e-75 PDB 1JKC "Human Lysozyme Mutant With Trp 109 ReplacedBy Phe" 100.00 130 99 100 2e-74 PDB 1JKD "Human Lysozyme Mutant With Trp 109 ReplacedBy Ala" 100.00 130 99 99 6e-74 PDB 1LAA "Lysozyme (E.C.3.2.1.17) Mutant With Asp 53Replaced By Glu (D53E)" 100.00 130 99 100 4e-75 PDB 1LHH "Lysozyme (E.C.3.2.1.17) Mutant With Val 110Replaced By Pro (V110p)" 100.00 130 99 99 7e-75 PDB 1LHI "Lysozyme (E.C.3.2.1.17) Mutant With Pro 71Replaced By Gly (P71g)" 100.00 130 99 99 2e-74 PDB 1LHJ "Lysozyme (E.C.3.2.1.17) Mutant With Pro 103Replaced By Gly (P103g)" 100.00 130 99 99 2e-74 PDB 1LHK "Lysozyme (E.C.3.2.1.17) Mutant With Asp 91Replaced By Pro (D91p)" 100.00 130 99 99 9e-75 PDB 1LHL "Lysozyme (E.C.3.2.1.17) Mutant With Ala 47Replaced By Proline (A47p)" 100.00 130 99 99 5e-75 PDB 1LOZ "Amyloidogenic Variant (I56t) Variant Of HumanLysozyme" 100.00 130 99 99 5e-75 PDB 1LYY "Amyloidogenic Variant (Asp67his) Of HumanLysozyme" 100.00 130 99 99 9e-75 PDB 1LZ4 "Lysozyme (E.C.3.2.1.17) Mutant With Cys 77Replaced By Ala (C77a)" 100.00 130 99 99 2e-74 PDB 1OUA "Contribution Of Hydrophobic Residues To TheStability Of Human Lysozyme: X-Ray Structure Of The I56tMutant" 100.00 130 99 99 5e-75 PDB 1OUB "Contribution Of Hydrophobic Residues To TheStability Of Human Lysozyme: X-Ray Structure Of TheV100a Mutant" 100.00 130 99 99 4e-75 PDB 1OUC "Contribution Of Hydrophobic Residues To TheStability Of Human Lysozyme: X-Ray Structure Of TheV110a Mutant" 100.00 130 99 99 4e-75 PDB 1OUD "Contribution Of Hydrophobic Residues To TheStability Of Human Lysozyme: X-Ray Structure Of TheV121a Mutant" 100.00 130 99 99 4e-75 PDB 1OUE "Contribution Of Hydrophobic Residues To TheStability Of Human Lysozyme: X-Ray Structure Of TheV125a Mutant" 100.00 130 99 99 4e-75 PDB 1OUG "Contribution Of Hydrophobic Residues To TheStability Of Human Lysozyme: X-Ray Structure Of The V2aMutant" 100.00 130 99 99 4e-75 PDB 1OUH "Contribution Of Hydrophobic Residues To TheStability Of Human Lysozyme: X-Ray Structure Of The V74aMutant" 100.00 130 99 99 4e-75 PDB 1OUI "Contribution Of Hydrophobic Residues To TheStability Of Human Lysozyme: X-Ray Structure Of The V93aMutant" 100.00 130 99 99 4e-75 PDB 1OUJ "Contribution Of Hydrophobic Residues To TheStability Of Human Lysozyme: X-Ray Structure Of The V99aMutant" 100.00 130 99 99 4e-75 PDB 1TAY "Lysozyme (E.C.3.2.1.17) Mutant With Tyr 63Replaced By Ala (Y63A)" 100.00 130 99 99 2e-74 PDB 1TBY "Lysozyme (E.C.3.2.1.17) Mutant With Tyr 63Replaced By Leu (Y63L)" 100.00 130 99 99 10e-75 PDB 1TCY "Lysozyme (E.C.3.2.1.17) Mutant With Tyr 63Replaced By Phe (Y63F)" 100.00 130 99 100 4e-75 PDB 1TDY "Lysozyme (E.C.3.2.1.17) Mutant With Tyr 63Replaced By Trp (Y63W)" 100.00 130 99 100 5e-75 PDB 1UBZ "A Chain A, Crystal Structure Of Glu102-MutantHuman Lysozyme Doubly Labeled With 2',3'-EpoxypropylBeta-Glycoside Of N- Acetyllactosamine" 100.00 130 99 100 4e-75 PDB 1WQM "Contribution Of Hydrogen Bonds To TheConformational Stability Of Human Lysozyme" 100.00 130 99 100 4e-75 PDB 1WQN "Contribution Of Hydrogen Bonds To TheConformational Stability Of Human Lysozyme" 100.00 130 99 100 4e-75 PDB 1WQO "Contribution Of Hydrogen Bonds To TheConformational Stability Of Human Lysozyme" 100.00 130 99 100 4e-75 PDB 1WQP "Contribution Of Hydrogen Bonds To TheConformational Stability Of Human Lysozyme" 100.00 130 99 100 4e-75 PDB 1WQQ "Contribution Of Hydrogen Bonds To TheConformational Stability Of Human Lysozyme" 100.00 130 99 100 4e-75 PDB 1WQR "Contribution Of Hydrogen Bonds To TheConformational Stability Of Human Lysozyme" 100.00 130 99 100 4e-75 PDB 1YAM "Mol_id: 1; Molecule: Lysozyme; Chain: Null;Ec: 3.2.1.17; Engineered: Yes; Mutation: I106v" 100.00 130 99 100 2e-75 PDB 1YAN "Mol_id: 1; Molecule: Lysozyme; Chain: Null;Ec: 3.2.1.17; Engineered: Yes; Mutation: I23v" 100.00 130 99 100 2e-75 PDB 1YAO "Mol_id: 1; Molecule: Lysozyme; Chain: Null;Ec: 3.2.1.17; Engineered: Yes; Mutation: I56v" 100.00 130 99 100 2e-75 PDB 1YAP "Mol_id: 1; Molecule: Lysozyme; Chain: Null;Ec: 3.2.1.17; Engineered: Yes; Mutation: I59v" 100.00 130 99 100 2e-75 PDB 1YAQ "Mol_id: 1; Molecule: Lysozyme; Chain: Null;Ec: 3.2.1.17; Engineered: Yes; Mutation: I89v" 100.00 130 99 100 2e-75 PDB 207L "A Chain A, Mutant Human Lysozyme C77a" 100.00 130 99 99 2e-74 PDB 208L "A Chain A, Mutant Human Lysozyme C77a" 100.00 130 99 99 2e-74 PDB 2HEA "Contribution Of Water Molecules In TheInterior Of A Protein To The Conformational Stability" 100.00 130 99 99 5e-75 PDB 2HEB "Contribution Of Water Molecules In TheInterior Of A Protein To The Conformational Stability" 100.00 130 99 99 5e-75 PDB 2HEC "Contribution Of Water Molecules In TheInterior Of A Protein To The Conformational Stability" 100.00 130 99 99 5e-75 PDB 2HED "Contribution Of Water Molecules In TheInterior Of A Protein To The Conformational Stability" 100.00 130 99 99 5e-75 PDB 2HEE "Contribution Of Water Molecules In TheInterior Of A Protein To The Conformational Stability" 100.00 130 99 99 10e-75 PDB 2HEF "Contribution Of Water Molecules In TheInterior Of A Protein To The Conformational Stability" 100.00 130 99 99 5e-75 PDB 2MEA "A Chain A, Changes In Conformational StabilityOf A Series Of Mutant Human Lysozymes At ConstantPositions" 100.00 130 99 99 4e-75 PDB 2MEB "Changes In Conformational Stability Of ASeries Of Mutant Human Lysozymes At Constant Positions" 100.00 130 99 100 2e-75 PDB 2MEC "A Chain A, Changes In Conformational StabilityOf A Series Of Mutant Human Lysozymes At ConstantPositions" 100.00 130 99 100 3e-75 PDB 2MED "Contribution Of Hydrophobic Effect To TheConformational Stability Of Human Lysozyme" 100.00 130 99 99 4e-75 PDB 2MEE "Contribution Of Hydrophobic Effect To TheConformational Stability Of Human Lysozyme" 100.00 130 99 100 2e-75 PDB 2MEF "Contribution Of Hydrophobic Effect To TheConformational Stability Of Human Lysozyme" 100.00 130 99 100 3e-75 PDB 2MEG "Changes In Conformational Stability Of ASeries Of Mutant Human Lysozymes At Constant Positions" 100.00 130 99 99 7e-75 PDB 2MEH "Contribution Of Hydrophobic Effect To TheConformational Stability Of Human Lysozyme" 100.00 130 99 99 5e-75 PDB 2MEI "Contribution Of Hydrophobic Effect To TheConformational Stability Of Human Lysozyme" 100.00 130 99 99 5e-75 PDB 1BB4 "A Chain A, Human Lysozyme Double Mutant A96l,W109h" 100.00 130 98 98 2e-73 PDB 1LHM "Lysozyme (E.C.3.2.1.17) (Mutant With Cys 77Replaced By Ala And Cys 95 Replaced By Ala) (C77A,C95A)" 100.00 130 98 98 2e-73 PDB 1QSW "A Chain A, Crystal Structure Analysis Of AHuman Lysozyme Mutant W64c C65a" 100.00 130 98 98 5e-73 PDB 2BQA "Contribution Of Hydrophobic Effect To TheConformational Stability Of Human Lysozyme" 100.00 130 98 98 2e-73 PDB 2BQK "Contribution Of Hydrophobic Effect To TheConformational Stability Of Human Lysozyme" 100.00 130 98 98 5e-73 PDB 2LHM "Lysozyme (E.C.3.2.1.17) (Apo) (Mutant With Gln86 Replaced B Asp And Ala 92 Replaced By Asp)(Q86D,A92D)" 100.00 130 98 98 3e-74 PDB 3LHM "Lysozyme (E.C.3.2.1.17) (Holo) (Mutant WithGln 86 Replaced By Asp And Ala 92 Replaced By Asp)(Q86D,A92D)" 100.00 130 98 98 3e-74 PDB 1I22 "A Chain A, Mutant Human Lysozyme(A83kQ86DA92D)" 100.00 130 98 98 10e-74 PDB 1IX0 "A Chain A, I59a-3ss Human Lysozyme" 100.00 130 98 98 7e-73 PDB 2BQB "Contribution Of Hydrophobic Effect To TheConformational Stability Of Human Lysozyme" 100.00 130 98 98 2e-73 PDB 2BQC "Contribution Of Hydrophobic Effect To TheConformational Stability Of Human Lysozyme" 100.00 130 98 98 2e-73 PDB 2BQD "Contribution Of Hydrophobic Effect To TheConformational Stability Of Human Lysozyme" 100.00 130 98 98 2e-73 PDB 2BQE "Contribution Of Hydrophobic Effect To TheConformational Stability Of Human Lysozyme" 100.00 130 98 98 2e-73 PDB 2BQF "Contribution Of Hydrophobic Effect To TheConformational Stability Of Human Lysozyme" 100.00 130 98 98 2e-73 PDB 2BQG "Contribution Of Hydrophobic Effect To TheConformational Stability Of Human Lysozyme" 100.00 130 98 98 5e-73 PDB 2BQH "Contribution Of Hydrophobic Effect To TheConformational Stability Of Human Lysozyme" 100.00 130 98 98 5e-73 PDB 2BQI "Contribution Of Hydrophobic Effect To TheConformational Stability Of Human Lysozyme" 100.00 130 98 98 5e-73 PDB 2BQJ "Contribution Of Hydrophobic Effect To TheConformational Stability Of Human Lysozyme" 100.00 130 98 98 5e-73 PDB 2BQL "Contribution Of Hydrophobic Effect To TheConformational Stability Of Human Lysozyme" 100.00 130 98 98 5e-73 PDB 2BQM "Contribution Of Hydrophobic Effect To TheConformational Stability Of Human Lysozyme" 100.00 130 98 98 5e-73 PDB 2BQN "Contribution Of Hydrophobic Effect To TheConformational Stability Of Human Lysozyme" 100.00 130 98 98 5e-73 PDB 2BQO "Contribution Of Hydrophobic Effect To TheConformational Stability Of Human Lysozyme" 100.00 130 98 98 5e-73 PDB 1C46 "A Chain A, Mutant Human Lysozyme With ForeignN-Terminal Residues" 99.24 131 100 100 1e-75 PDB 1C7P "A Chain A, Crystal Structure Of Mutant HumanLysozyme With Four Extra Residues (Eaea) At TheN-Terminal" 97.01 134 100 100 1e-75 PDB 1IOC "A Chain A, Crystal Structure Of Mutant HumanLysozyme, Eaea-I56t" 97.01 134 99 99 5e-75 DBJ BAA00314.1 "lysozyme [synthetic construct]" 99.24 131 99 99 10e-75 EMBL CAA32175.1 "lysozyme [Homo sapiens]" 100.00 130 100 100 1e-75 EMBL CAA53144.1 "lysozyme [synthetic construct]" 99.24 131 100 100 1e-75 GenBank AAA59535.1 "lysozyme precursor (EC 3.2.1.17)" 87.84 148 100 100 1e-75 GenBank AAA59536.1 "lysozyme precursor (EC 3.2.1.17)" 87.84 148 100 100 1e-75 GenBank AAB41205.1 "lysozyme c precursor [Gorilla gorilla]" 87.84 148 100 100 1e-75 GenBank AAB41209.1 "lysozyme c precursor [Pan troglodytes]" 87.84 148 100 100 1e-75 GenBank AAB41214.1 "lysozyme c precursor [Pan paniscus]" 87.84 148 100 100 1e-75 PIR LZHU "lysozyme (EC 3.2.1.17) c precursor [validated]- human" 87.84 148 100 100 1e-75 REF NP_000230.1 "lysozyme precursor [Homo sapiens]" 87.84 148 100 100 1e-75 SWISS-PROT P61626 "LYC_HUMAN Lysozyme C precursor(1,4-beta-N-acetylmuramidase C)" 87.84 148 100 100 1e-75 SWISS-PROT P61628 "LYC_PANTR Lysozyme C precursor(1,4-beta-N-acetylmuramidase C)" 87.84 148 100 100 1e-75 SWISS-PROT P79179 "LYC_GORGO Lysozyme C precursor(1,4-beta-N-acetylmuramidase C)" 87.84 148 100 100 1e-75 SWISS-PROT P79239 "LYC_PONPY Lysozyme C precursor(1,4-beta-N-acetylmuramidase C)" 87.84 148 99 99 5e-75 stop_ save_ ######################################## # Molecular bond linkage definitions # ######################################## save_crosslink_bond_definitions _Saveframe_category crosslink_bonds loop_ _Bond_order _Bond_type _Atom_one_mol_system_component_name _Atom_one_residue_seq_code _Atom_one_residue_label _Atom_one_atom_name _Atom_two_mol_system_component_name _Atom_two_residue_seq_code _Atom_two_residue_label _Atom_two_atom_name single disulfide "human lysozyme" 6 CYS SG "human lysozyme" 128 CYS SG single disulfide "human lysozyme" 30 CYS SG "human lysozyme" 116 CYS SG single disulfide "human lysozyme" 65 CYS SG "human lysozyme" 81 CYS SG single disulfide "human lysozyme" 77 CYS SG "human 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 $human_lysozyme Human 9606 Eukaryota Metazoa Homo sapiens stop_ save_ ######################### # Experimental source # ######################### save_experimental_source _Saveframe_category experimental_source loop_ _Mol_label _Production_method _Host_organism_name_common _Genus _Species _Strain _Vector_name $human_lysozyme 'recombinant technology' . . . . . stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Saveframe_category sample _Sample_type solution loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $human_lysozyme 1.0 mM . stop_ save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model Unity _Field_strength 500 save_ ############################# # NMR applied experiments # ############################# save_NMR_applied_experiment _Saveframe_category NMR_applied_experiment _Experiment_name ; 15N-edited NOESY 15N-edited TOCSY CBCA(CO)NNH HNCACB 13C-edited NOESY 1H-13C-1H HCCH-TOCSY 1H-15N HSQC ; save_ ####################### # Sample conditions # ####################### save_HL04-cond_1 _Saveframe_category sample_conditions loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 3.8 0.1 n/a temperature 277 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 0.0 internal direct . . . 1.0 stop_ save_ ################################### # Assigned chemical shift lists # ################################### ################################################################### # Chemical Shift Ambiguity Index Value Definitions # # # # Index Value Definition # # # # 1 Unique # # 2 Ambiguity of geminal atoms or geminal methyl # # proton groups # # 3 Aromatic atoms on opposite sides of the ring # # (e.g. Tyr HE1 and HE2 protons) # # 4 Intraresidue ambiguities (e.g. Lys HG and # # HD protons) # # 5 Interresidue ambiguities (Lys 12 vs. Lys 27) # # 9 Ambiguous, specific ambiguity not defined # # # ################################################################### save_shift_set_1 _Saveframe_category assigned_chemical_shifts loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $HL04-cond_1 _Chem_shift_reference_set_label $chemical_shift_reference _Mol_system_component_name "human 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 C C 171.12 . . 2 1 LYS CA C 55.54 . . 3 1 LYS HA H 3.90 . . 4 1 LYS CB C 33.88 . . 5 1 LYS HB2 H 1.68 . . 6 1 LYS HG3 H 0.96 . . 7 1 LYS HD2 H 0.63 . . 8 2 VAL N N 126.82 . . 9 2 VAL H H 9.08 . . 10 2 VAL C C 177.52 . . 11 2 VAL CA C 61.42 . . 12 2 VAL HA H 4.86 . . 13 2 VAL CB C 31.67 . . 14 2 VAL HB H 1.97 . . 15 2 VAL HG1 H 0.89 . . 16 2 VAL HG2 H 0.89 . . 17 3 PHE N N 127.45 . . 18 3 PHE H H 9.01 . . 19 3 PHE C C 176.14 . . 20 3 PHE CA C 59.37 . . 21 3 PHE HA H 4.08 . . 22 3 PHE CB C 41.34 . . 23 3 PHE HB2 H 2.98 . . 24 3 PHE HB3 H 2.76 . . 25 4 GLU N N 120.36 . . 26 4 GLU H H 8.47 . . 27 4 GLU C C 176.60 . . 28 4 GLU CA C 56.15 . . 29 4 GLU HA H 4.34 . . 30 4 GLU CB C 29.81 . . 31 4 GLU HB2 H 2.37 . . 32 4 GLU HB3 H 2.60 . . 33 4 GLU HG2 H 2.03 . . 34 4 GLU HG3 H 2.22 . . 35 5 ARG N N 125.49 . . 36 5 ARG H H 8.68 . . 37 5 ARG C C 176.87 . . 38 5 ARG CA C 60.82 . . 39 5 ARG HA H 4.34 . . 40 5 ARG CB C 32.11 . . 41 5 ARG HB2 H 2.47 . . 42 5 ARG HG2 H 1.92 . . 43 5 ARG HD3 H 3.19 . . 44 6 CYS N N 114.33 . . 45 6 CYS H H 8.97 . . 46 6 CYS C C 177.23 . . 47 6 CYS CA C 54.43 . . 48 6 CYS HA H 4.74 . . 49 6 CYS CB C 32.58 . . 50 6 CYS HB2 H 3.16 . . 51 6 CYS HB3 H 2.96 . . 52 7 GLU N N 123.55 . . 53 7 GLU H H 8.08 . . 54 7 GLU C C 180.26 . . 55 7 GLU CA C 58.90 . . 56 7 GLU HA H 4.12 . . 57 7 GLU CB C 29.58 . . 58 7 GLU HB2 H 2.62 . . 59 7 GLU HB3 H 2.48 . . 60 7 GLU HG2 H 2.21 . . 61 7 GLU HG3 H 2.09 . . 62 8 LEU N N 121.54 . . 63 8 LEU H H 8.60 . . 64 8 LEU C C 177.29 . . 65 8 LEU CA C 57.62 . . 66 8 LEU HA H 3.67 . . 67 8 LEU CB C 39.48 . . 68 8 LEU HB2 H 1.55 . . 69 8 LEU HG H 0.77 . . 70 8 LEU HD1 H -0.31 . . 71 8 LEU HD2 H 0.37 . . 72 9 ALA N N 122.65 . . 73 9 ALA H H 8.45 . . 74 9 ALA C C 179.21 . . 75 9 ALA CA C 56.53 . . 76 9 ALA HA H 3.99 . . 77 9 ALA CB C 17.76 . . 78 9 ALA HB H 1.50 . . 79 10 ARG N N 114.72 . . 80 10 ARG H H 8.46 . . 81 10 ARG C C 179.51 . . 82 10 ARG CA C 60.06 . . 83 10 ARG HA H 3.86 . . 84 10 ARG CB C 30.94 . . 85 10 ARG HB2 H 1.82 . . 86 10 ARG HG2 H 1.52 . . 87 10 ARG HD3 H 0.75 . . 88 11 THR N N 118.61 . . 89 11 THR H H 7.88 . . 90 11 THR C C 175.47 . . 91 11 THR CA C 67.25 . . 92 11 THR HA H 3.93 . . 93 11 THR CB C 68.77 . . 94 11 THR HB H 4.24 . . 95 11 THR HG2 H 1.20 . . 96 12 LEU N N 118.81 . . 97 12 LEU H H 8.89 . . 98 12 LEU C C 178.74 . . 99 12 LEU CA C 57.76 . . 100 12 LEU HA H 3.63 . . 101 12 LEU CB C 41.15 . . 102 12 LEU HB2 H 1.89 . . 103 12 LEU HB3 H 0.72 . . 104 12 LEU HG H 1.64 . . 105 12 LEU HD1 H 0.61 . . 106 12 LEU HD2 H 0.51 . . 107 13 LYS N N 118.90 . . 108 13 LYS H H 8.24 . . 109 13 LYS C C 180.60 . . 110 13 LYS CA C 58.84 . . 111 13 LYS HA H 4.06 . . 112 13 LYS CB C 32.78 . . 113 13 LYS HB2 H 2.17 . . 114 13 LYS HG3 H 1.91 . . 115 13 LYS HD2 H 0.98 . . 116 13 LYS HE2 H 3.85 . . 117 13 LYS HE3 H 3.62 . . 118 14 ARG N N 121.55 . . 119 14 ARG H H 8.04 . . 120 14 ARG C C 177.60 . . 121 14 ARG CA C 59.22 . . 122 14 ARG HA H 4.17 . . 123 14 ARG CB C 29.98 . . 124 14 ARG HB2 H 2.05 . . 125 14 ARG HG2 H 1.77 . . 126 14 ARG HD3 H 3.27 . . 127 15 LEU N N 116.52 . . 128 15 LEU H H 7.55 . . 129 15 LEU C C 176.58 . . 130 15 LEU CA C 54.42 . . 131 15 LEU HA H 4.40 . . 132 15 LEU CB C 41.67 . . 133 15 LEU HB2 H 1.51 . . 134 15 LEU HG H 1.81 . . 135 15 LEU HD1 H 0.71 . . 136 15 LEU HD2 H 0.83 . . 137 16 GLY N N 105.87 . . 138 16 GLY H H 7.57 . . 139 16 GLY C C 176.18 . . 140 16 GLY CA C 47.38 . . 141 16 GLY HA2 H 4.09 . . 142 16 GLY HA3 H 3.88 . . 143 17 MET N N 113.75 . . 144 17 MET H H 7.48 . . 145 17 MET C C 177.92 . . 146 17 MET CA C 56.99 . . 147 17 MET HA H 3.94 . . 148 17 MET CB C 34.36 . . 149 17 MET HB2 H 1.33 . . 150 17 MET HB3 H 1.23 . . 151 17 MET HG2 H 1.66 . . 152 17 MET HG3 H 1.45 . . 153 18 ASP N N 118.35 . . 154 18 ASP H H 9.19 . . 155 18 ASP C C 175.97 . . 156 18 ASP CA C 55.88 . . 157 18 ASP HA H 4.43 . . 158 18 ASP CB C 41.26 . . 159 18 ASP HB2 H 3.29 . . 160 18 ASP HB3 H 2.36 . . 161 19 GLY N N 119.61 . . 162 19 GLY H H 9.15 . . 163 19 GLY C C 175.30 . . 164 19 GLY CA C 45.71 . . 165 19 GLY HA2 H 4.20 . . 166 19 GLY HA3 H 3.33 . . 167 20 TYR N N 126.01 . . 168 20 TYR H H 8.00 . . 169 20 TYR C C 176.59 . . 170 20 TYR CA C 60.73 . . 171 20 TYR HA H 4.13 . . 172 20 TYR CB C 38.66 . . 173 20 TYR HB2 H 3.08 . . 174 20 TYR HB3 H 3.34 . . 175 21 ARG N N 125.43 . . 176 21 ARG H H 9.13 . . 177 21 ARG C C 175.98 . . 178 21 ARG CA C 56.28 . . 179 21 ARG HA H 3.58 . . 180 21 ARG CB C 27.04 . . 181 21 ARG HB2 H 2.03 . . 182 21 ARG HB3 H 1.67 . . 183 21 ARG HG2 H 1.09 . . 184 21 ARG HD3 H 2.94 . . 185 22 GLY N N 102.89 . . 186 22 GLY H H 7.87 . . 187 22 GLY C C 174.50 . . 188 22 GLY CA C 45.30 . . 189 22 GLY HA2 H 4.02 . . 190 22 GLY HA3 H 3.58 . . 191 23 ILE N N 124.63 . . 192 23 ILE H H 7.83 . . 193 23 ILE C C 175.52 . . 194 23 ILE CA C 61.00 . . 195 23 ILE HA H 3.81 . . 196 23 ILE CB C 38.10 . . 197 23 ILE HB H 1.99 . . 198 23 ILE HG12 H 1.30 . . 199 23 ILE HG2 H -0.32 . . 200 23 ILE HD1 H 0.59 . . 201 24 SER N N 122.78 . . 202 24 SER H H 8.98 . . 203 24 SER C C 174.91 . . 204 24 SER CA C 57.51 . . 205 24 SER HA H 4.42 . . 206 24 SER CB C 65.17 . . 207 24 SER HB2 H 3.80 . . 208 24 SER HB3 H 4.16 . . 209 25 LEU N N 121.24 . . 210 25 LEU H H 8.81 . . 211 25 LEU C C 177.98 . . 212 25 LEU CA C 58.12 . . 213 25 LEU HA H 4.21 . . 214 25 LEU CB C 42.34 . . 215 25 LEU HB2 H 2.00 . . 216 25 LEU HG H 1.35 . . 217 25 LEU HD1 H 0.98 . . 218 25 LEU HD2 H 1.00 . . 219 26 ALA N N 118.34 . . 220 26 ALA H H 8.99 . . 221 26 ALA C C 179.10 . . 222 26 ALA CA C 56.04 . . 223 26 ALA HA H 3.86 . . 224 26 ALA CB C 18.39 . . 225 26 ALA HB H 1.55 . . 226 27 ASN N N 116.71 . . 227 27 ASN H H 7.79 . . 228 27 ASN C C 177.73 . . 229 27 ASN CA C 58.31 . . 230 27 ASN HA H 4.58 . . 231 27 ASN CB C 40.70 . . 232 27 ASN HB2 H 3.06 . . 233 27 ASN HB3 H 2.12 . . 234 28 TRP N N 119.83 . . 235 28 TRP H H 7.89 . . 236 28 TRP C C 178.69 . . 237 28 TRP CA C 60.46 . . 238 28 TRP HA H 4.39 . . 239 28 TRP CB C 30.69 . . 240 28 TRP HB2 H 3.36 . . 241 28 TRP HB3 H 3.06 . . 242 29 MET N N 116.21 . . 243 29 MET H H 8.46 . . 244 29 MET C C 177.03 . . 245 29 MET CA C 55.31 . . 246 29 MET HA H 4.43 . . 247 29 MET CB C 30.81 . . 248 29 MET HB2 H 2.34 . . 249 29 MET HG3 H 2.06 . . 250 30 CYS N N 119.46 . . 251 30 CYS H H 8.10 . . 252 30 CYS C C 175.77 . . 253 30 CYS CA C 60.68 . . 254 30 CYS HA H 2.95 . . 255 30 CYS CB C 44.58 . . 256 30 CYS HB2 H 3.14 . . 257 31 LEU N N 117.90 . . 258 31 LEU H H 8.15 . . 259 31 LEU C C 177.39 . . 260 31 LEU CA C 58.95 . . 261 31 LEU HA H 4.00 . . 262 31 LEU CB C 42.15 . . 263 31 LEU HB2 H 2.42 . . 264 31 LEU HG H 1.49 . . 265 31 LEU HD1 H -0.14 . . 266 31 LEU HD2 H 0.48 . . 267 32 ALA N N 118.72 . . 268 32 ALA H H 8.44 . . 269 32 ALA C C 179.55 . . 270 32 ALA CA C 55.14 . . 271 32 ALA HA H 4.08 . . 272 32 ALA CB C 18.61 . . 273 32 ALA HB H 1.38 . . 274 33 LYS N N 119.45 . . 275 33 LYS H H 8.83 . . 276 33 LYS C C 180.07 . . 277 33 LYS CA C 60.74 . . 278 33 LYS HA H 4.19 . . 279 33 LYS CB C 30.81 . . 280 33 LYS HB2 H 2.13 . . 281 33 LYS HG2 H 0.68 . . 282 33 LYS HG3 H 0.46 . . 283 33 LYS HD2 H 1.48 . . 284 33 LYS HE3 H 2.66 . . 285 34 TRP N N 117.90 . . 286 34 TRP H H 7.82 . . 287 34 TRP C C 177.92 . . 288 34 TRP CA C 59.22 . . 289 34 TRP HA H 4.28 . . 290 34 TRP CB C 28.97 . . 291 34 TRP HB2 H 3.32 . . 292 34 TRP HB3 H 2.80 . . 293 35 GLU N N 116.20 . . 294 35 GLU H H 8.82 . . 295 35 GLU C C 177.02 . . 296 35 GLU CA C 57.66 . . 297 35 GLU HA H 4.45 . . 298 35 GLU CB C 27.53 . . 299 35 GLU HB2 H 2.05 . . 300 35 GLU HB3 H 1.94 . . 301 35 GLU HG3 H 2.69 . . 302 36 SER N N 107.69 . . 303 36 SER H H 7.96 . . 304 36 SER C C 176.81 . . 305 36 SER CA C 58.01 . . 306 36 SER HA H 4.66 . . 307 36 SER CB C 67.85 . . 308 36 SER HB2 H 4.44 . . 309 36 SER HB3 H 3.55 . . 310 37 GLY N N 115.66 . . 311 37 GLY H H 8.16 . . 312 37 GLY C C 174.50 . . 313 37 GLY CA C 47.53 . . 314 37 GLY HA2 H 3.72 . . 315 37 GLY HA3 H 3.45 . . 316 38 TYR N N 108.59 . . 317 38 TYR H H 7.40 . . 318 38 TYR C C 173.20 . . 319 38 TYR CA C 56.50 . . 320 38 TYR HA H 3.69 . . 321 38 TYR CB C 36.84 . . 322 38 TYR HB2 H 3.82 . . 323 38 TYR HB3 H 3.19 . . 324 39 ASN N N 116.90 . . 325 39 ASN H H 7.13 . . 326 39 ASN C C 176.60 . . 327 39 ASN CA C 51.47 . . 328 39 ASN HA H 5.53 . . 329 39 ASN CB C 40.32 . . 330 39 ASN HB2 H 3.51 . . 331 39 ASN HB3 H 2.72 . . 332 39 ASN HD21 H 7.87 . . 333 39 ASN HD22 H 7.24 . . 334 40 THR N N 115.15 . . 335 40 THR H H 9.27 . . 336 40 THR C C 174.27 . . 337 40 THR CA C 64.58 . . 338 40 THR HA H 4.05 . . 339 40 THR CB C 69.51 . . 340 40 THR HB H 1.55 . . 341 40 THR HG2 H 1.59 . . 342 41 ARG N N 113.88 . . 343 41 ARG H H 7.67 . . 344 41 ARG C C 176.50 . . 345 41 ARG CA C 55.10 . . 346 41 ARG HA H 4.46 . . 347 41 ARG CB C 29.99 . . 348 41 ARG HB2 H 1.68 . . 349 41 ARG HB3 H 1.57 . . 350 41 ARG HG2 H 2.09 . . 351 41 ARG HD3 H 3.22 . . 352 42 ALA N N 122.58 . . 353 42 ALA H H 6.83 . . 354 42 ALA C C 176.82 . . 355 42 ALA CA C 53.49 . . 356 42 ALA HA H 4.16 . . 357 42 ALA CB C 19.08 . . 358 42 ALA HB H 1.34 . . 359 43 THR N N 113.80 . . 360 43 THR H H 8.40 . . 361 43 THR C C 173.32 . . 362 43 THR CA C 60.35 . . 363 43 THR HA H 5.29 . . 364 43 THR CB C 72.70 . . 365 43 THR HB H 3.77 . . 366 43 THR HG2 H 1.12 . . 367 44 ASN N N 118.60 . . 368 44 ASN H H 8.13 . . 369 44 ASN C C 172.71 . . 370 44 ASN CA C 53.37 . . 371 44 ASN HA H 5.03 . . 372 44 ASN CB C 43.36 . . 373 44 ASN HB2 H 2.77 . . 374 44 ASN HD21 H 7.79 . . 375 44 ASN HD22 H 6.95 . . 376 45 TYR N N 127.39 . . 377 45 TYR H H 9.16 . . 378 45 TYR C C 173.76 . . 379 45 TYR CA C 57.62 . . 380 45 TYR HA H 4.84 . . 381 45 TYR CB C 39.96 . . 382 45 TYR HB2 H 3.02 . . 383 45 TYR HB3 H 2.79 . . 384 46 ASN N N 127.70 . . 385 46 ASN H H 8.96 . . 386 46 ASN C C 172.92 . . 387 46 ASN CA C 51.56 . . 388 46 ASN HA H 4.69 . . 389 46 ASN CB C 39.19 . . 390 46 ASN HB2 H 2.77 . . 391 46 ASN HB3 H 2.69 . . 392 46 ASN HD21 H 7.14 . . 393 46 ASN HD22 H 6.90 . . 394 47 ALA N N 124.98 . . 395 47 ALA H H 8.65 . . 396 47 ALA C C 179.55 . . 397 47 ALA CA C 54.48 . . 398 47 ALA HA H 3.69 . . 399 47 ALA CB C 18.39 . . 400 47 ALA HB H 1.45 . . 401 48 GLY N N 104.04 . . 402 48 GLY H H 8.66 . . 403 48 GLY C C 174.71 . . 404 48 GLY CA C 47.17 . . 405 48 GLY HA2 H 3.81 . . 406 49 ASP N N 116.28 . . 407 49 ASP H H 7.18 . . 408 49 ASP C C 175.21 . . 409 49 ASP CA C 52.28 . . 410 49 ASP HA H 4.71 . . 411 49 ASP CB C 40.51 . . 412 49 ASP HB2 H 2.93 . . 413 49 ASP HB3 H 2.42 . . 414 50 ARG N N 113.79 . . 415 50 ARG H H 7.91 . . 416 50 ARG C C 174.20 . . 417 50 ARG CA C 57.66 . . 418 50 ARG HA H 3.85 . . 419 50 ARG CB C 27.04 . . 420 50 ARG HB2 H 2.26 . . 421 50 ARG HB3 H 2.06 . . 422 50 ARG HG2 H 1.62 . . 423 50 ARG HD3 H 3.25 . . 424 51 SER N N 113.86 . . 425 51 SER H H 8.06 . . 426 51 SER C C 171.34 . . 427 51 SER CA C 57.37 . . 428 51 SER HA H 4.73 . . 429 51 SER CB C 66.37 . . 430 51 SER HB2 H 4.17 . . 431 51 SER HB3 H 3.59 . . 432 52 THR N N 115.74 . . 433 52 THR H H 9.17 . . 434 52 THR C C 171.73 . . 435 52 THR CA C 61.63 . . 436 52 THR HA H 5.04 . . 437 52 THR CB C 71.46 . . 438 52 THR HB H 3.86 . . 439 52 THR HG2 H 0.39 . . 440 53 ASP N N 123.67 . . 441 53 ASP H H 8.94 . . 442 53 ASP C C 175.39 . . 443 53 ASP CA C 52.00 . . 444 53 ASP HA H 5.25 . . 445 53 ASP CB C 41.97 . . 446 53 ASP HB2 H 2.72 . . 447 53 ASP HB3 H 2.05 . . 448 54 TYR N N 118.02 . . 449 54 TYR H H 9.24 . . 450 54 TYR C C 178.39 . . 451 54 TYR CA C 59.59 . . 452 54 TYR HA H 4.81 . . 453 54 TYR CB C 43.07 . . 454 54 TYR HB2 H 2.99 . . 455 54 TYR HB3 H 2.74 . . 456 55 GLY N N 112.23 . . 457 55 GLY H H 9.14 . . 458 55 GLY C C 177.13 . . 459 55 GLY CA C 46.61 . . 460 55 GLY HA2 H 4.59 . . 461 55 GLY HA3 H 4.47 . . 462 56 ILE N N 121.38 . . 463 56 ILE H H 9.30 . . 464 56 ILE C C 175.70 . . 465 56 ILE CA C 62.18 . . 466 56 ILE HA H 4.08 . . 467 56 ILE CB C 39.56 . . 468 56 ILE HB H 1.18 . . 469 56 ILE HG12 H 0.06 . . 470 56 ILE HG2 H 0.06 . . 471 57 PHE N N 115.11 . . 472 57 PHE H H 8.43 . . 473 57 PHE C C 173.11 . . 474 57 PHE CA C 56.03 . . 475 57 PHE HA H 4.64 . . 476 57 PHE CB C 39.64 . . 477 57 PHE HB2 H 2.68 . . 478 58 GLN N N 113.37 . . 479 58 GLN H H 7.91 . . 480 58 GLN C C 173.89 . . 481 58 GLN CA C 55.23 . . 482 58 GLN HA H 3.47 . . 483 58 GLN CB C 26.99 . . 484 58 GLN HB2 H 1.94 . . 485 58 GLN HB3 H 2.07 . . 486 58 GLN HG3 H 2.59 . . 487 59 ILE N N 122.30 . . 488 59 ILE H H 7.95 . . 489 59 ILE C C 177.22 . . 490 59 ILE CA C 61.46 . . 491 59 ILE HA H 4.38 . . 492 59 ILE CB C 39.40 . . 493 59 ILE HB H 1.93 . . 494 59 ILE HG12 H 1.09 . . 495 59 ILE HG2 H 1.09 . . 496 59 ILE HD1 H 1.09 . . 497 60 ASN N N 127.53 . . 498 60 ASN H H 8.67 . . 499 60 ASN C C 177.04 . . 500 60 ASN CA C 56.38 . . 501 60 ASN HA H 5.71 . . 502 60 ASN CB C 43.90 . . 503 60 ASN HB2 H 3.04 . . 504 60 ASN HB3 H 3.43 . . 505 61 SER N N 119.29 . . 506 61 SER H H 9.25 . . 507 61 SER C C 174.94 . . 508 61 SER CA C 60.75 . . 509 61 SER HA H 5.17 . . 510 61 SER CB C 64.68 . . 511 61 SER HB2 H 4.46 . . 512 62 ARG N N 123.11 . . 513 62 ARG H H 8.78 . . 514 62 ARG C C 177.20 . . 515 62 ARG CA C 58.77 . . 516 62 ARG HA H 4.17 . . 517 62 ARG CB C 30.08 . . 518 62 ARG HB2 H 1.78 . . 519 62 ARG HG2 H 1.42 . . 520 62 ARG HD3 H 1.06 . . 521 63 TYR N N 114.44 . . 522 63 TYR H H 7.44 . . 523 63 TYR C C 176.61 . . 524 63 TYR CA C 58.86 . . 525 63 TYR HA H 4.35 . . 526 63 TYR CB C 40.07 . . 527 63 TYR HB2 H 1.59 . . 528 64 TRP N N 114.18 . . 529 64 TRP H H 7.29 . . 530 64 TRP C C 174.46 . . 531 64 TRP CA C 58.89 . . 532 64 TRP HA H 5.03 . . 533 64 TRP CB C 33.94 . . 534 64 TRP HB2 H 3.36 . . 535 65 CYS N N 110.36 . . 536 65 CYS H H 7.45 . . 537 65 CYS C C 172.23 . . 538 65 CYS CA C 52.67 . . 539 65 CYS HA H 5.71 . . 540 65 CYS CB C 45.62 . . 541 65 CYS HB2 H 2.83 . . 542 65 CYS HB3 H 2.49 . . 543 66 ASN N N 118.55 . . 544 66 ASN H H 8.77 . . 545 66 ASN C C 176.70 . . 546 66 ASN CA C 51.28 . . 547 66 ASN HA H 5.70 . . 548 66 ASN CB C 40.58 . . 549 66 ASN HB2 H 2.89 . . 550 66 ASN HB3 H 2.49 . . 551 66 ASN HD21 H 7.74 . . 552 66 ASN HD22 H 7.17 . . 553 67 ASP N N 131.59 . . 554 67 ASP H H 10.60 . . 555 67 ASP C C 177.51 . . 556 67 ASP CA C 51.57 . . 557 67 ASP HA H 5.00 . . 558 67 ASP CB C 41.11 . . 559 67 ASP HB2 H 3.32 . . 560 67 ASP HB3 H 2.31 . . 561 68 GLY N N 108.06 . . 562 68 GLY H H 8.32 . . 563 68 GLY C C 174.22 . . 564 68 GLY CA C 46.46 . . 565 68 GLY HA2 H 4.11 . . 566 68 GLY HA3 H 3.87 . . 567 69 LYS N N 117.43 . . 568 69 LYS H H 8.25 . . 569 69 LYS C C 175.71 . . 570 69 LYS CA C 55.40 . . 571 69 LYS HA H 4.82 . . 572 69 LYS CB C 33.82 . . 573 69 LYS HB2 H 1.82 . . 574 69 LYS HB3 H 1.90 . . 575 69 LYS HG2 H 1.21 . . 576 69 LYS HG3 H 1.34 . . 577 69 LYS HD2 H 1.69 . . 578 69 LYS HE3 H 3.01 . . 579 70 THR N N 121.26 . . 580 70 THR H H 8.57 . . 581 70 THR CA C 60.19 . . 582 70 THR HA H 4.82 . . 583 70 THR CB C 70.39 . . 584 70 THR HB H 4.11 . . 585 70 THR HG2 H 1.06 . . 586 71 PRO C C 177.20 . . 587 71 PRO CA C 63.24 . . 588 71 PRO HA H 4.39 . . 589 71 PRO CB C 32.06 . . 590 71 PRO HB2 H 2.31 . . 591 71 PRO HG2 H 2.04 . . 592 71 PRO HD2 H 4.14 . . 593 71 PRO HD3 H 3.90 . . 594 72 GLY N N 109.78 . . 595 72 GLY H H 8.87 . . 596 72 GLY C C 174.52 . . 597 72 GLY CA C 46.18 . . 598 72 GLY HA2 H 3.81 . . 599 72 GLY HA3 H 3.69 . . 600 73 ALA N N 120.57 . . 601 73 ALA H H 7.22 . . 602 73 ALA C C 178.51 . . 603 73 ALA CA C 52.68 . . 604 73 ALA HA H 4.62 . . 605 73 ALA CB C 20.93 . . 606 73 ALA HB H 1.55 . . 607 74 VAL N N 119.50 . . 608 74 VAL H H 7.88 . . 609 74 VAL C C 175.93 . . 610 74 VAL CA C 62.60 . . 611 74 VAL HA H 3.92 . . 612 74 VAL CB C 33.97 . . 613 74 VAL HB H 1.92 . . 614 74 VAL HG1 H 0.93 . . 615 74 VAL HG2 H 0.71 . . 616 75 ASN N N 119.30 . . 617 75 ASN H H 8.82 . . 618 75 ASN C C 176.73 . . 619 75 ASN CA C 51.29 . . 620 75 ASN HA H 3.90 . . 621 75 ASN CB C 37.17 . . 622 75 ASN HB2 H 3.04 . . 623 75 ASN HD21 H 7.80 . . 624 75 ASN HD22 H 7.08 . . 625 76 ALA N N 120.19 . . 626 76 ALA H H 8.28 . . 627 76 ALA C C 180.00 . . 628 76 ALA CA C 55.19 . . 629 76 ALA HA H 4.03 . . 630 76 ALA CB C 19.40 . . 631 76 ALA HB H 1.47 . . 632 77 CYS N N 110.74 . . 633 77 CYS H H 9.44 . . 634 77 CYS C C 173.07 . . 635 77 CYS CA C 56.00 . . 636 77 CYS HA H 4.35 . . 637 77 CYS CB C 39.44 . . 638 77 CYS HB2 H 3.51 . . 639 78 HIS N N 117.58 . . 640 78 HIS H H 7.78 . . 641 78 HIS C C 173.32 . . 642 78 HIS CA C 55.99 . . 643 78 HIS HA H 3.98 . . 644 78 HIS CB C 25.78 . . 645 78 HIS HB2 H 3.45 . . 646 78 HIS HB3 H 3.27 . . 647 79 LEU N N 118.45 . . 648 79 LEU H H 8.91 . . 649 79 LEU C C 176.57 . . 650 79 LEU CA C 53.87 . . 651 79 LEU HA H 4.73 . . 652 79 LEU CB C 47.12 . . 653 79 LEU HB2 H 1.66 . . 654 79 LEU HB3 H 1.22 . . 655 79 LEU HG H 0.81 . . 656 79 LEU HD1 H 0.63 . . 657 79 LEU HD2 H 0.63 . . 658 80 SER N N 116.91 . . 659 80 SER H H 8.75 . . 660 80 SER C C 176.74 . . 661 80 SER CA C 57.57 . . 662 80 SER HA H 5.01 . . 663 80 SER CB C 63.41 . . 664 80 SER HB2 H 3.94 . . 665 81 CYS N N 125.84 . . 666 81 CYS H H 8.53 . . 667 81 CYS C C 176.54 . . 668 81 CYS CA C 57.33 . . 669 81 CYS HA H 3.94 . . 670 81 CYS CB C 37.48 . . 671 81 CYS HB2 H 1.86 . . 672 81 CYS HB3 H 1.09 . . 673 82 SER N N 114.43 . . 674 82 SER H H 8.51 . . 675 82 SER C C 177.43 . . 676 82 SER CA C 61.30 . . 677 82 SER HA H 3.89 . . 678 82 SER HB2 H 1.69 . . 679 83 ALA N N 125.91 . . 680 83 ALA H H 7.89 . . 681 83 ALA C C 179.16 . . 682 83 ALA CA C 54.49 . . 683 83 ALA HA H 4.38 . . 684 83 ALA CB C 18.29 . . 685 83 ALA HB H 1.69 . . 686 84 LEU N N 116.59 . . 687 84 LEU H H 7.97 . . 688 84 LEU C C 174.89 . . 689 84 LEU CA C 54.24 . . 690 84 LEU HA H 4.36 . . 691 84 LEU CB C 40.69 . . 692 84 LEU HB2 H 2.25 . . 693 84 LEU HG H 1.67 . . 694 84 LEU HD1 H 1.05 . . 695 84 LEU HD2 H 0.79 . . 696 85 LEU N N 117.26 . . 697 85 LEU H H 7.20 . . 698 85 LEU C C 177.69 . . 699 85 LEU CA C 53.35 . . 700 85 LEU HA H 5.73 . . 701 85 LEU CB C 42.84 . . 702 85 LEU HB2 H 1.80 . . 703 85 LEU HG H 1.12 . . 704 85 LEU HD1 H 1.04 . . 705 85 LEU HD2 H 1.04 . . 706 86 GLN N N 116.34 . . 707 86 GLN H H 6.78 . . 708 86 GLN C C 175.54 . . 709 86 GLN CA C 54.54 . . 710 86 GLN HA H 4.42 . . 711 86 GLN CB C 30.90 . . 712 86 GLN HB2 H 2.01 . . 713 86 GLN HB3 H 1.71 . . 714 86 GLN HG2 H 2.51 . . 715 86 GLN HG3 H 2.67 . . 716 86 GLN HE21 H 7.59 . . 717 86 GLN HE22 H 7.07 . . 718 87 ASP N N 120.18 . . 719 87 ASP H H 8.91 . . 720 87 ASP C C 176.00 . . 721 87 ASP CA C 57.04 . . 722 87 ASP HA H 4.17 . . 723 87 ASP CB C 40.07 . . 724 87 ASP HB2 H 2.50 . . 725 87 ASP HB3 H 2.64 . . 726 88 ASN N N 114.11 . . 727 88 ASN H H 7.59 . . 728 88 ASN C C 177.39 . . 729 88 ASN CA C 52.13 . . 730 88 ASN HA H 4.90 . . 731 88 ASN CB C 38.25 . . 732 88 ASN HB2 H 3.02 . . 733 88 ASN HB3 H 2.79 . . 734 88 ASN HD21 H 7.84 . . 735 88 ASN HD22 H 7.09 . . 736 89 ILE N N 119.08 . . 737 89 ILE H H 8.48 . . 738 89 ILE C C 175.17 . . 739 89 ILE CA C 61.45 . . 740 89 ILE HA H 4.59 . . 741 89 ILE CB C 38.72 . . 742 89 ILE HB H 2.13 . . 743 89 ILE HG12 H 1.01 . . 744 89 ILE HG2 H 1.02 . . 745 89 ILE HD1 H 0.25 . . 746 90 ALA N N 125.65 . . 747 90 ALA H H 8.35 . . 748 90 ALA C C 180.92 . . 749 90 ALA CA C 57.05 . . 750 90 ALA HA H 3.88 . . 751 90 ALA CB C 17.70 . . 752 90 ALA HB H 1.46 . . 753 91 ASP N N 118.38 . . 754 91 ASP H H 9.29 . . 755 91 ASP C C 176.86 . . 756 91 ASP CA C 56.91 . . 757 91 ASP HA H 4.50 . . 758 91 ASP CB C 38.14 . . 759 91 ASP HB2 H 2.71 . . 760 91 ASP HB3 H 2.48 . . 761 92 ALA N N 122.73 . . 762 92 ALA H H 7.68 . . 763 92 ALA C C 178.80 . . 764 92 ALA CA C 55.72 . . 765 92 ALA HA H 3.96 . . 766 92 ALA CB C 17.73 . . 767 92 ALA HB H 1.58 . . 768 93 VAL N N 117.88 . . 769 93 VAL H H 8.74 . . 770 93 VAL C C 176.40 . . 771 93 VAL CA C 66.96 . . 772 93 VAL HA H 3.25 . . 773 93 VAL CB C 31.13 . . 774 93 VAL HB H 2.17 . . 775 93 VAL HG1 H 0.82 . . 776 93 VAL HG2 H 0.82 . . 777 94 ALA N N 121.03 . . 778 94 ALA H H 8.10 . . 779 94 ALA C C 180.92 . . 780 94 ALA CA C 55.43 . . 781 94 ALA HA H 3.89 . . 782 94 ALA CB C 17.85 . . 783 94 ALA HB H 1.55 . . 784 95 CYS N N 115.90 . . 785 95 CYS H H 8.43 . . 786 95 CYS C C 174.79 . . 787 95 CYS CA C 55.26 . . 788 95 CYS HA H 4.98 . . 789 95 CYS CB C 34.90 . . 790 95 CYS HB2 H 3.37 . . 791 95 CYS HB3 H 2.69 . . 792 96 ALA N N 123.85 . . 793 96 ALA H H 8.89 . . 794 96 ALA C C 179.20 . . 795 96 ALA CA C 56.08 . . 796 96 ALA HA H 3.77 . . 797 96 ALA CB C 17.59 . . 798 96 ALA HB H 0.85 . . 799 97 LYS N N 114.07 . . 800 97 LYS H H 8.03 . . 801 97 LYS C C 177.41 . . 802 97 LYS CA C 59.95 . . 803 97 LYS HA H 3.63 . . 804 97 LYS CB C 33.06 . . 805 97 LYS HB2 H 1.73 . . 806 97 LYS HG2 H 1.03 . . 807 97 LYS HG3 H 1.22 . . 808 97 LYS HD2 H 0.82 . . 809 97 LYS HE2 H -0.49 . . 810 97 LYS HE3 H -0.05 . . 811 98 ARG N N 117.79 . . 812 98 ARG H H 7.13 . . 813 98 ARG C C 179.71 . . 814 98 ARG CA C 58.25 . . 815 98 ARG HA H 4.01 . . 816 98 ARG CB C 28.35 . . 817 98 ARG HB2 H 1.94 . . 818 98 ARG HG2 H 1.63 . . 819 98 ARG HD3 H 2.68 . . 820 99 VAL N N 122.84 . . 821 99 VAL H H 8.42 . . 822 99 VAL C C 180.15 . . 823 99 VAL CA C 65.77 . . 824 99 VAL HA H 2.48 . . 825 99 VAL CB C 30.56 . . 826 99 VAL HB H 1.91 . . 827 99 VAL HG1 H -0.37 . . 828 99 VAL HG2 H -0.63 . . 829 100 VAL N N 107.74 . . 830 100 VAL H H 7.54 . . 831 100 VAL C C 174.70 . . 832 100 VAL CA C 63.33 . . 833 100 VAL HA H 3.94 . . 834 100 VAL CB C 31.27 . . 835 100 VAL HB H 2.44 . . 836 100 VAL HG1 H 1.06 . . 837 100 VAL HG2 H 1.42 . . 838 101 ARG N N 118.81 . . 839 101 ARG H H 7.61 . . 840 101 ARG C C 177.51 . . 841 101 ARG CA C 58.73 . . 842 101 ARG HA H 4.18 . . 843 101 ARG CB C 31.23 . . 844 101 ARG HB2 H 2.19 . . 845 101 ARG HB3 H 1.95 . . 846 101 ARG HG2 H 1.33 . . 847 101 ARG HG3 H 2.66 . . 848 101 ARG HD2 H 3.54 . . 849 101 ARG HD3 H 3.31 . . 850 102 ASP N N 121.05 . . 851 102 ASP H H 7.42 . . 852 102 ASP CA C 53.83 . . 853 102 ASP HA H 4.94 . . 854 102 ASP CB C 38.84 . . 855 102 ASP HB2 H 3.06 . . 856 103 PRO C C 178.24 . . 857 103 PRO CA C 66.24 . . 858 103 PRO HA H 4.20 . . 859 103 PRO CB C 32.46 . . 860 103 PRO HB2 H 2.31 . . 861 103 PRO HG2 H 2.16 . . 862 103 PRO HG3 H 2.04 . . 863 103 PRO HD3 H 3.76 . . 864 104 GLN N N 113.19 . . 865 104 GLN H H 8.63 . . 866 104 GLN C C 177.09 . . 867 104 GLN CA C 57.51 . . 868 104 GLN HA H 4.10 . . 869 104 GLN CB C 29.00 . . 870 104 GLN HB2 H 1.98 . . 871 104 GLN HB3 H 1.81 . . 872 104 GLN HG3 H 2.31 . . 873 104 GLN HE21 H 7.56 . . 874 104 GLN HE22 H 6.87 . . 875 105 GLY N N 108.33 . . 876 105 GLY H H 8.09 . . 877 105 GLY C C 175.88 . . 878 105 GLY CA C 45.94 . . 879 105 GLY HA2 H 3.88 . . 880 106 ILE N N 126.70 . . 881 106 ILE H H 8.73 . . 882 106 ILE C C 173.96 . . 883 106 ILE CA C 62.74 . . 884 106 ILE HA H 3.97 . . 885 106 ILE CB C 38.77 . . 886 106 ILE HB H 0.90 . . 887 106 ILE HG12 H -0.47 . . 888 106 ILE HG2 H -0.48 . . 889 106 ILE HD1 H -0.71 . . 890 107 ARG N N 116.41 . . 891 107 ARG H H 7.35 . . 892 107 ARG C C 175.43 . . 893 107 ARG CA C 57.74 . . 894 107 ARG HA H 4.09 . . 895 107 ARG CB C 29.25 . . 896 107 ARG HB2 H 2.14 . . 897 107 ARG HG2 H 1.83 . . 898 107 ARG HD3 H 3.36 . . 899 108 ALA N N 119.52 . . 900 108 ALA H H 7.19 . . 901 108 ALA C C 178.16 . . 902 108 ALA CA C 54.17 . . 903 108 ALA HA H 3.82 . . 904 108 ALA CB C 19.00 . . 905 108 ALA HB H 0.90 . . 906 109 TRP N N 115.34 . . 907 109 TRP H H 7.51 . . 908 109 TRP C C 176.82 . . 909 109 TRP CA C 59.29 . . 910 109 TRP HA H 4.83 . . 911 109 TRP CB C 29.74 . . 912 109 TRP HB2 H 3.24 . . 913 110 VAL N N 128.54 . . 914 110 VAL H H 9.02 . . 915 110 VAL C C 177.43 . . 916 110 VAL CA C 66.38 . . 917 110 VAL HA H 3.62 . . 918 110 VAL CB C 31.84 . . 919 110 VAL HB H 2.18 . . 920 110 VAL HG1 H 1.12 . . 921 110 VAL HG2 H 1.04 . . 922 111 ALA N N 119.26 . . 923 111 ALA H H 8.94 . . 924 111 ALA C C 180.23 . . 925 111 ALA CA C 55.20 . . 926 111 ALA HA H 4.24 . . 927 111 ALA CB C 18.03 . . 928 111 ALA HB H 1.43 . . 929 112 TRP N N 114.22 . . 930 112 TRP H H 7.39 . . 931 112 TRP C C 179.18 . . 932 112 TRP CA C 62.70 . . 933 112 TRP HA H 3.68 . . 934 112 TRP CB C 28.64 . . 935 112 TRP HB2 H 3.82 . . 936 112 TRP HB3 H 3.11 . . 937 113 ARG N N 119.12 . . 938 113 ARG H H 7.78 . . 939 113 ARG C C 177.77 . . 940 113 ARG CA C 59.61 . . 941 113 ARG HA H 3.81 . . 942 113 ARG CB C 30.23 . . 943 113 ARG HB2 H 2.21 . . 944 113 ARG HG2 H 1.65 . . 945 113 ARG HG3 H 1.90 . . 946 113 ARG HD2 H 3.62 . . 947 113 ARG HD3 H 3.30 . . 948 114 ASN N N 112.97 . . 949 114 ASN H H 7.98 . . 950 114 ASN C C 176.81 . . 951 114 ASN CA C 54.71 . . 952 114 ASN HA H 4.46 . . 953 114 ASN CB C 39.02 . . 954 114 ASN HB2 H 2.63 . . 955 114 ASN HD21 H 7.56 . . 956 114 ASN HD22 H 7.06 . . 957 115 ARG N N 113.40 . . 958 115 ARG H H 7.88 . . 959 115 ARG C C 175.96 . . 960 115 ARG CA C 54.76 . . 961 115 ARG HA H 3.97 . . 962 115 ARG CB C 31.37 . . 963 115 ARG HB2 H 1.31 . . 964 115 ARG HG2 H 1.06 . . 965 115 ARG HD3 H 2.63 . . 966 116 CYS N N 114.44 . . 967 116 CYS H H 7.35 . . 968 116 CYS C C 173.50 . . 969 116 CYS CA C 55.01 . . 970 116 CYS HA H 4.32 . . 971 116 CYS CB C 44.15 . . 972 116 CYS HB2 H 2.49 . . 973 116 CYS HB3 H 1.61 . . 974 117 GLN N N 120.86 . . 975 117 GLN H H 6.71 . . 976 117 GLN CA C 57.16 . . 977 117 GLN HA H 3.11 . . 978 117 GLN CB C 28.40 . . 979 117 GLN HB2 H 1.65 . . 980 117 GLN HG3 H 0.59 . . 981 118 ASN N N 119.47 . . 982 118 ASN H H 9.36 . . 983 118 ASN C C 173.41 . . 984 118 ASN CA C 54.64 . . 985 118 ASN HA H 4.39 . . 986 118 ASN CB C 37.05 . . 987 118 ASN HB2 H 3.11 . . 988 119 ARG N N 116.12 . . 989 119 ARG H H 7.48 . . 990 119 ARG C C 174.83 . . 991 119 ARG CA C 53.97 . . 992 119 ARG HA H 4.57 . . 993 119 ARG CB C 32.51 . . 994 119 ARG HB2 H 1.74 . . 995 119 ARG HG2 H 1.31 . . 996 119 ARG HD2 H 2.92 . . 997 119 ARG HD3 H 2.63 . . 998 120 ASP N N 118.77 . . 999 120 ASP H H 8.60 . . 1000 120 ASP C C 177.69 . . 1001 120 ASP CA C 54.01 . . 1002 120 ASP HA H 4.70 . . 1003 120 ASP CB C 39.71 . . 1004 120 ASP HB2 H 2.92 . . 1005 120 ASP HB3 H 2.73 . . 1006 121 VAL N N 119.32 . . 1007 121 VAL H H 8.84 . . 1008 121 VAL C C 176.71 . . 1009 121 VAL CA C 61.03 . . 1010 121 VAL HA H 4.87 . . 1011 121 VAL CB C 32.22 . . 1012 121 VAL HB H 2.73 . . 1013 121 VAL HG1 H 1.17 . . 1014 121 VAL HG2 H 0.87 . . 1015 122 ARG N N 122.73 . . 1016 122 ARG H H 8.35 . . 1017 122 ARG C C 179.34 . . 1018 122 ARG CA C 59.67 . . 1019 122 ARG HA H 3.96 . . 1020 122 ARG CB C 29.99 . . 1021 122 ARG HB2 H 2.01 . . 1022 122 ARG HG2 H 1.88 . . 1023 122 ARG HD3 H 3.29 . . 1024 123 GLN N N 115.79 . . 1025 123 GLN H H 9.08 . . 1026 123 GLN C C 177.27 . . 1027 123 GLN CA C 57.78 . . 1028 123 GLN HA H 4.09 . . 1029 123 GLN CB C 27.59 . . 1030 123 GLN HB2 H 1.26 . . 1031 123 GLN HG2 H 1.88 . . 1032 123 GLN HG3 H 1.74 . . 1033 124 TYR N N 116.59 . . 1034 124 TYR H H 7.59 . . 1035 124 TYR C C 176.18 . . 1036 124 TYR CA C 62.27 . . 1037 124 TYR HA H 4.16 . . 1038 124 TYR CB C 38.92 . . 1039 124 TYR HB2 H 3.26 . . 1040 124 TYR HB3 H 2.96 . . 1041 125 VAL N N 103.40 . . 1042 125 VAL H H 7.23 . . 1043 125 VAL C C 175.90 . . 1044 125 VAL CA C 60.04 . . 1045 125 VAL HA H 4.52 . . 1046 125 VAL CB C 33.10 . . 1047 125 VAL HB H 2.35 . . 1048 125 VAL HG1 H 0.96 . . 1049 125 VAL HG2 H 0.80 . . 1050 126 GLN N N 124.32 . . 1051 126 GLN H H 7.37 . . 1052 126 GLN C C 176.71 . . 1053 126 GLN CA C 57.49 . . 1054 126 GLN HA H 4.23 . . 1055 126 GLN CB C 28.38 . . 1056 126 GLN HB2 H 2.10 . . 1057 126 GLN HB3 H 1.98 . . 1058 126 GLN HG3 H 2.40 . . 1059 127 GLY N N 113.02 . . 1060 127 GLY H H 9.35 . . 1061 127 GLY C C 175.84 . . 1062 127 GLY CA C 45.83 . . 1063 127 GLY HA2 H 4.23 . . 1064 127 GLY HA3 H 3.87 . . 1065 128 CYS N N 113.83 . . 1066 128 CYS H H 7.66 . . 1067 128 CYS C C 175.55 . . 1068 128 CYS CA C 51.97 . . 1069 128 CYS HA H 4.92 . . 1070 128 CYS CB C 35.06 . . 1071 128 CYS HB2 H 3.22 . . 1072 128 CYS HB3 H 2.69 . . 1073 129 GLY N N 111.68 . . 1074 129 GLY H H 9.01 . . 1075 129 GLY C C 174.55 . . 1076 129 GLY CA C 46.97 . . 1077 129 GLY HA2 H 3.91 . . 1078 130 VAL N N 116.06 . . 1079 130 VAL H H 7.63 . . 1080 130 VAL CA C 61.27 . . 1081 130 VAL HA H 4.30 . . 1082 130 VAL CB C 33.62 . . 1083 130 VAL HB H 2.21 . . 1084 130 VAL HG1 H 0.75 . . 1085 130 VAL HG2 H 0.75 . . stop_ save_