data_5903 #Corrected using PDB structure: 1UUHB # #N.B. (Observed* = Observed shift + Offset correction) # #After reference correction, the following residues still #have a CO chemical shift difference (obs*-pred) greater than 5.0ppm: #NUM AA CS Observed* Predicted #142 E C 170.35 176.14 # #After reference correction, the following residues still #have a N chemical shift difference (obs*-pred) greater than 10.0ppm: #NUM AA CS Observed* Predicted # 64 I N 110.83 122.33 # #The average CS difference between predicted and observed: #HA CA CB CO N HN #N/A 0.04 N/A -0.15 -0.57 -0.03 # #bmr5903.str.corr chemical shifts have been re-referenced with the following #offsets (these values have been added to the original bmr5903.str file): #HA CA CB CO N HN #N/A +0.04 N/A -0.15 -0.57 N/A # #The 95% confidence intervals for the above recommended offsets are: # HA CA CB CO N HN # N/A +/-0.16 N/A +/-0.13 +/-0.35 +/-0.06 # #The Correlation Coefficients between predicted and observed #chemical shifts are: #HA CA CB CO N HN #N/A 0.954 N/A 0.808 0.818 0.624 # #The RMSD between predicted and observed* (reference #corrected) chemical shifts are: #HA CA CB CO N HN #N/A 0.924 N/A 0.743 2.028 0.346 # ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; 1H,13C and 15N backbone resonance assignment of the Hyaluronan-binding domain of CD44 ; loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Takeda Mitsuhiro . . 2 Terasawa Hiroaki . . 3 Sakakura Masayosh . . 4 Yamaguchi Yoshiki . . 5 Kajiwara Masahiro . . 6 Kawashima Hiroto . . 7 Miyasaka Masayuki . . 8 Shimada Ichio . . stop_ _BMRB_accession_number 5903 _BMRB_flat_file_name bmr5903.str _Entry_type new _Submission_date 2003-08-15 _Accession_date 2003-08-15 _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' 144 '15N chemical shifts' 144 '13C chemical shifts' 284 stop_ save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_title ; Letter to the Editor: 1H, 13C and 15N backbone resonance assignments of the Hyaluronan-binding domain of CD44 ; _Citation_status published _Citation_type journal _MEDLINE_UI_code . _PubMed_ID 15017146 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Takeda Mitsuhiro . . 2 Terasawa Hiroaki . . 3 Sakakura Masayoshi . . 4 Yamaguchi Yoshiki . . 5 Kajiwara Masahiro . . 6 Kawashima Hiroto . . 7 Miyasaka Masayuki . . 8 Shimada Ichio . . stop_ _Journal_abbreviation "J. Biomol. NMR" _Journal_volume 29 _Journal_issue 1 _Page_first 97 _Page_last 98 _Year 2004 save_ ################################## # Molecular system description # ################################## save_system_CD44 _Saveframe_category molecular_system _Mol_system_name "CD44 hyaluronan-binding domain" _Abbreviation_common CD44 _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label "CD44 hyaluronan binding domain" $CD44_hyaluronan-binding_domain stop_ _System_physical_state native _System_oligomer_state monomer _System_paramagnetic no _System_thiol_state 'all disulfide bound' save_ ######################## # Monomeric polymers # ######################## save_CD44_hyaluronan-binding_domain _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common "CD44 hyaluronan-binding domain" _Name_variant . _Abbreviation_common CD44 _Mol_thiol_state 'all disulfide bound' ############################## # Polymer residue sequence # ############################## _Residue_count 160 _Mol_residue_sequence ; MAQIDLNITCRFAGVFHVEK NGRYSISRTEAADLCKAFNS TLPTMAQMEKALSIGFETCR YGFIEGHVVIPRIHPNSICA ANNTGVYILTSNTSQYDTYC FNASAPPEEDCTSVTDLPNA FDGPITITIVNRDGTRYVQK GEYRTNPEDIYPSNPTDDDV ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 -2 MET 2 -1 ALA 3 21 GLN 4 22 ILE 5 23 ASP 6 24 LEU 7 25 ASN 8 26 ILE 9 27 THR 10 28 CYS 11 29 ARG 12 30 PHE 13 31 ALA 14 32 GLY 15 33 VAL 16 34 PHE 17 35 HIS 18 36 VAL 19 37 GLU 20 38 LYS 21 39 ASN 22 40 GLY 23 41 ARG 24 42 TYR 25 43 SER 26 44 ILE 27 45 SER 28 46 ARG 29 47 THR 30 48 GLU 31 49 ALA 32 50 ALA 33 51 ASP 34 52 LEU 35 53 CYS 36 54 LYS 37 55 ALA 38 56 PHE 39 57 ASN 40 58 SER 41 59 THR 42 60 LEU 43 61 PRO 44 62 THR 45 63 MET 46 64 ALA 47 65 GLN 48 66 MET 49 67 GLU 50 68 LYS 51 69 ALA 52 70 LEU 53 71 SER 54 72 ILE 55 73 GLY 56 74 PHE 57 75 GLU 58 76 THR 59 77 CYS 60 78 ARG 61 79 TYR 62 80 GLY 63 81 PHE 64 82 ILE 65 83 GLU 66 84 GLY 67 85 HIS 68 86 VAL 69 87 VAL 70 88 ILE 71 89 PRO 72 90 ARG 73 91 ILE 74 92 HIS 75 93 PRO 76 94 ASN 77 95 SER 78 96 ILE 79 97 CYS 80 98 ALA 81 99 ALA 82 100 ASN 83 101 ASN 84 102 THR 85 103 GLY 86 104 VAL 87 105 TYR 88 106 ILE 89 107 LEU 90 108 THR 91 109 SER 92 110 ASN 93 111 THR 94 112 SER 95 113 GLN 96 114 TYR 97 115 ASP 98 116 THR 99 117 TYR 100 118 CYS 101 119 PHE 102 120 ASN 103 121 ALA 104 122 SER 105 123 ALA 106 124 PRO 107 125 PRO 108 126 GLU 109 127 GLU 110 128 ASP 111 129 CYS 112 130 THR 113 131 SER 114 132 VAL 115 133 THR 116 134 ASP 117 135 LEU 118 136 PRO 119 137 ASN 120 138 ALA 121 139 PHE 122 140 ASP 123 141 GLY 124 142 PRO 125 143 ILE 126 144 THR 127 145 ILE 128 146 THR 129 147 ILE 130 148 VAL 131 149 ASN 132 150 ARG 133 151 ASP 134 152 GLY 135 153 THR 136 154 ARG 137 155 TYR 138 156 VAL 139 157 GLN 140 158 LYS 141 159 GLY 142 160 GLU 143 161 TYR 144 162 ARG 145 163 THR 146 164 ASN 147 165 PRO 148 166 GLU 149 167 ASP 150 168 ILE 151 169 TYR 152 170 PRO 153 171 SER 154 172 ASN 155 173 PRO 156 174 THR 157 175 ASP 158 176 ASP 159 177 ASP 160 178 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 1POZ "A Chain A, Solution Structure Of TheHyaluronan Binding Domain Of Human Cd44" 100.63 159 100 100 9e-91 PDB 1UUH "A Chain A, Hyaluronan Binding Domain Of HumanCd44" 100.63 159 99 99 2e-89 EMBL CAD89965.1 "hypothetical protein [Homo sapiens]" 44.32 361 99 100 5e-91 EMBL CAA40133.1 "CD44R1 [Homo sapiens]" 32.45 493 99 100 5e-91 EMBL CAA38951.1 "CD44E (epithelial form) [Homo sapiens]" 32.45 493 99 99 3e-90 EMBL CAA47271.1 "epican [Homo sapiens]" 22.89 699 99 100 5e-91 EMBL CAB61878.1 "transmembrane glycoprotein [Homosapiens]" 21.56 742 99 99 3e-90 GenBank AAH67348.1 "CD44 antigen, isoform 4 precursor [Homosapiens]" 44.32 361 99 100 5e-91 GenBank AAM50041.1 "CD44 antigen [Homo sapiens]" 44.32 361 99 100 5e-91 GenBank AAB13626.1 "cell surface glycoprotein CD44" 23.95 668 99 100 5e-91 GenBank AAB13623.1 "cell surface glycoprotein CD44" 23.70 675 99 100 5e-91 GenBank AAB13628.1 "cell surface glycoprotein CD44" 21.56 742 99 100 5e-91 PIR I77371 "CD44R5 - human" 40.51 395 99 100 5e-91 PIR JH0518 "lymphocyte homing receptor CD44, splice formCD44R1 - human" 37.56 426 99 100 5e-91 PIR S13530 "CD44E protein, epithelial - human" 32.45 493 99 99 3e-90 PIR I37369 "epican - human" 22.89 699 99 100 5e-91 PIR A47195 "lymphocyte homing receptor isoform CD44 -human" 21.56 742 99 100 5e-91 REF NP_001001391.1 "CD44 antigen isoform 4 precursor;cell surface glycoprotein CD44; Lutheran inhibitor,dominant; homing function and Indian blood group system;monoclonal antibody A3D8; antigen gp90 homing receptor;CDW44 antigen; phagocytic glycoprotein I; extracellularmatrix receptor-III; GP90 lymphocyte homing/adhesionreceptor; hermes antigen; hyaluronate receptor; heparansulfate proteoglycan; cell adhesion molecule (CD44)[Homo sapiens]" 44.32 361 99 100 5e-91 REF NP_001001390.1 "CD44 antigen isoform 3 precursor;cell surface glycoprotein CD44; Lutheran inhibitor,dominant; homing function and Indian blood group system;monoclonal antibody A3D8; antigen gp90 homing receptor;CDW44 antigen; phagocytic glycoprotein I; extracellularmatrix receptor-III; GP90 lymphocyte homing/adhesionreceptor; hermes antigen; hyaluronate receptor; heparansulfate proteoglycan; cell adhesion molecule (CD44)[Homo sapiens]" 32.45 493 99 100 5e-91 REF NP_001001389.1 "CD44 antigen isoform 2 precursor;cell surface glycoprotein CD44; Lutheran inhibitor,dominant; homing function and Indian blood group system;monoclonal antibody A3D8; antigen gp90 homing receptor;CDW44 antigen; phagocytic glycoprotein I; extracellularmatrix receptor-III; GP90 lymphocyte homing/adhesionreceptor; hermes antigen; hyaluronate receptor; heparansulfate proteoglycan; cell adhesion molecule (CD44)[Homo sapiens]" 22.89 699 99 100 5e-91 REF NP_000601.3 "CD44 antigen isoform 1 precursor; cellsurface glycoprotein CD44; Lutheran inhibitor, dominant;homing function and Indian blood group system;monoclonal antibody A3D8; antigen gp90 homing receptor;CDW44 antigen; phagocytic glycoprotein I; extracellularmatrix receptor-III; GP90 lymphocyte homing/adhesionreceptor; hermes antigen; hyaluronate receptor; heparansulfate proteoglycan; cell adhesion molecule (CD44)[Homo sapiens]" 21.56 742 99 100 5e-91 SWISS-PROT P16070 "CD44_HUMAN CD44 antigen precursor (Phagocyticglycoprotein I) (PGP-1) (HUTCH-I) (Extracellular matrixreceptor-III) (ECMR-III) (GP90 lymphocytehoming/adhesion receptor) (Hermes antigen) (Hyaluronatereceptor) (Heparan sulfate proteoglycan) (Epican)(CDw44)" 21.56 742 99 100 5e-91 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 "CD44 hyaluronan binding domain" 10 CYS SG "CD44 hyaluronan binding domain" 111 CYS SG single disulfide "CD44 hyaluronan binding domain" 35 CYS SG "CD44 hyaluronan binding domain" 100 CYS SG single disulfide "CD44 hyaluronan binding domain" 59 CYS SG "CD44 hyaluronan binding domain" 79 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 $CD44_hyaluronan-binding_domain 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 $CD44_hyaluronan-binding_domain '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 $CD44_hyaluronan-binding_domain 2.0 mM "[U-98% 13C; U-98% 15N]" stop_ save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model Avance _Field_strength 600 save_ ############################# # NMR applied experiments # ############################# save_NMR_applied_experiment _Saveframe_category NMR_applied_experiment _Experiment_name ; 1H-15N HSQC 3D HNCA 3D HN(CO)CA 3D HNCACB 3D CBCA(CO)NH ; save_ ####################### # Sample conditions # ####################### save_EX-condition _Saveframe_category sample_conditions loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 6.7 0.1 n/a temperature 298 0.1 K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference _Saveframe_category chemical_shift_reference loop_ _Mol_common_name _Atom_type _Atom_isotope_number _Atom_group _Chem_shift_units _Chem_shift_value _Reference_method _Reference_type _External_reference_sample_geometry _External_reference_location _External_reference_axis _Indirect_shift_ratio DSS H 1 'methyl protons' ppm 0.0 internal . . . . 1.0 DSS C 13 'methyl protons' ppm 0.0 indirect . . . . 0.251449500 DSS N 15 'methyl protons' ppm 0.0 indirect . . . . 0.101329051 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-condition _Chem_shift_reference_set_label $chemical_shift_reference _Mol_system_component_name "CD44 hyaluronan binding domain" 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 3 GLN C C 174.65 0.2 1 2 4 ILE H H 8.67 0.01 1 3 4 ILE C C 172.95 0.2 1 4 4 ILE CA C 61.64 0.4 1 5 4 ILE N N 123.93 0.7 1 6 5 ASP H H 8.76 0.01 1 7 5 ASP C C 174.55 0.2 1 8 5 ASP CA C 52.74 0.4 1 9 5 ASP N N 128.33 0.7 1 10 6 LEU H H 9.46 0.01 1 11 6 LEU C C 174.35 0.2 1 12 6 LEU CA C 52.64 0.4 1 13 6 LEU N N 123.33 0.7 1 14 7 ASN H H 8.97 0.01 1 15 7 ASN C C 173.65 0.2 1 16 7 ASN CA C 52.74 0.4 1 17 7 ASN N N 123.43 0.7 1 18 8 ILE H H 8.34 0.01 1 19 8 ILE C C 176.05 0.2 1 20 8 ILE CA C 59.24 0.4 1 21 8 ILE N N 120.23 0.7 1 22 9 THR H H 7.99 0.01 1 23 9 THR C C 176.55 0.2 1 24 9 THR CA C 61.64 0.4 1 25 9 THR N N 111.53 0.7 1 26 10 CYS H H 8.97 0.01 1 27 10 CYS C C 172.35 0.2 1 28 10 CYS CA C 59.34 0.4 1 29 10 CYS N N 114.23 0.7 1 30 11 ARG H H 8.53 0.01 1 31 11 ARG C C 175.75 0.2 1 32 11 ARG CA C 55.24 0.4 1 33 11 ARG N N 120.83 0.7 1 34 12 PHE H H 9.81 0.01 1 35 12 PHE C C 173.95 0.2 1 36 12 PHE CA C 56.94 0.4 1 37 12 PHE N N 123.33 0.7 1 38 13 ALA H H 8.04 0.01 1 39 13 ALA C C 176.95 0.2 1 40 13 ALA CA C 53.24 0.4 1 41 13 ALA N N 127.83 0.7 1 42 14 GLY H H 8.86 0.01 1 43 14 GLY C C 173.75 0.2 1 44 14 GLY CA C 46.54 0.4 1 45 14 GLY N N 102.03 0.7 1 46 15 VAL H H 7.92 0.01 1 47 15 VAL C C 174.95 0.2 1 48 15 VAL CA C 62.04 0.4 1 49 15 VAL N N 122.53 0.7 1 50 16 PHE H H 9.18 0.01 1 51 16 PHE C C 171.95 0.2 1 52 16 PHE CA C 54.54 0.4 1 53 16 PHE N N 120.33 0.7 1 54 17 HIS H H 8.92 0.01 1 55 17 HIS C C 172.75 0.2 1 56 17 HIS CA C 55.14 0.4 1 57 17 HIS N N 121.73 0.7 1 58 18 VAL H H 8.39 0.01 1 59 18 VAL C C 172.25 0.2 1 60 18 VAL CA C 61.04 0.4 1 61 18 VAL N N 125.63 0.7 1 62 19 GLU H H 8.11 0.01 1 63 19 GLU C C 174.55 0.2 1 64 19 GLU CA C 53.84 0.4 1 65 19 GLU N N 125.63 0.7 1 66 20 LYS H H 9.91 0.01 1 67 20 LYS C C 175.05 0.2 1 68 20 LYS CA C 54.64 0.4 1 69 20 LYS N N 134.13 0.7 1 70 21 ASN H H 9.75 0.01 1 71 21 ASN C C 175.15 0.2 1 72 21 ASN CA C 54.34 0.4 1 73 21 ASN N N 122.33 0.7 1 74 22 GLY H H 8.95 0.01 1 75 22 GLY C C 173.45 0.2 1 76 22 GLY CA C 46.54 0.4 1 77 22 GLY N N 104.93 0.7 1 78 23 ARG H H 7.96 0.01 1 79 23 ARG C C 175.25 0.2 1 80 23 ARG CA C 54.54 0.4 1 81 23 ARG N N 116.23 0.7 1 82 24 TYR H H 8.48 0.01 1 83 24 TYR C C 177.35 0.2 1 84 24 TYR CA C 58.44 0.4 1 85 24 TYR N N 121.83 0.7 1 86 25 SER H H 8.02 0.01 1 87 25 SER C C 172.65 0.2 1 88 25 SER CA C 59.04 0.4 1 89 25 SER N N 118.43 0.7 1 90 26 ILE H H 9.35 0.01 1 91 26 ILE C C 174.75 0.2 1 92 26 ILE CA C 62.04 0.4 1 93 26 ILE N N 125.63 0.7 1 94 27 SER H H 8.18 0.01 1 95 27 SER C C 174.35 0.2 1 96 27 SER CA C 56.94 0.4 1 97 27 SER N N 123.33 0.7 1 98 28 ARG H H 9.02 0.01 1 99 28 ARG C C 179.05 0.2 1 100 28 ARG CA C 59.74 0.4 1 101 28 ARG N N 121.23 0.7 1 102 29 THR H H 7.76 0.01 1 103 29 THR C C 177.35 0.2 1 104 29 THR CA C 63.94 0.4 1 105 29 THR N N 107.13 0.7 1 106 30 GLU H H 8.08 0.01 1 107 30 GLU C C 177.45 0.2 1 108 30 GLU CA C 59.74 0.4 1 109 30 GLU N N 126.73 0.7 1 110 31 ALA H H 8.80 0.01 1 111 31 ALA C C 178.05 0.2 1 112 31 ALA CA C 56.14 0.4 1 113 31 ALA N N 123.53 0.7 1 114 32 ALA H H 7.05 0.01 1 115 32 ALA C C 180.75 0.2 1 116 32 ALA CA C 55.34 0.4 1 117 32 ALA N N 116.33 0.7 1 118 33 ASP H H 7.32 0.01 1 119 33 ASP C C 178.75 0.2 1 120 33 ASP CA C 57.34 0.4 1 121 33 ASP N N 120.03 0.7 1 122 34 LEU H H 9.53 0.01 1 123 34 LEU C C 178.55 0.2 1 124 34 LEU CA C 57.74 0.4 1 125 34 LEU N N 126.73 0.7 1 126 35 CYS H H 8.66 0.01 1 127 35 CYS C C 178.95 0.2 1 128 35 CYS CA C 56.64 0.4 1 129 35 CYS N N 114.63 0.7 1 130 36 LYS H H 8.20 0.01 1 131 36 LYS C C 180.35 0.2 1 132 36 LYS CA C 60.44 0.4 1 133 36 LYS N N 122.53 0.7 1 134 37 ALA H H 8.17 0.01 1 135 37 ALA C C 177.55 0.2 1 136 37 ALA CA C 55.64 0.4 1 137 37 ALA N N 125.23 0.7 1 138 38 PHE H H 7.67 0.01 1 139 38 PHE C C 176.85 0.2 1 140 38 PHE CA C 59.44 0.4 1 141 38 PHE N N 114.83 0.7 1 142 39 ASN H H 9.01 0.01 1 143 39 ASN C C 173.65 0.2 1 144 39 ASN CA C 54.64 0.4 1 145 39 ASN N N 122.83 0.7 1 146 40 SER H H 8.23 0.01 1 148 40 SER CA C 58.74 0.4 1 149 40 SER N N 111.63 0.7 1 150 41 THR H H 9.09 0.01 1 151 41 THR C C 175.15 0.2 1 154 42 LEU H H 9.08 0.01 1 155 42 LEU CA C 54.14 0.4 1 156 42 LEU N N 124.53 0.7 1 157 43 PRO C C 175.45 0.2 1 158 44 THR H H 8.46 0.01 1 159 44 THR C C 176.25 0.2 1 160 44 THR CA C 60.14 0.4 1 161 44 THR N N 111.33 0.7 1 162 45 MET H H 8.96 0.01 1 163 45 MET C C 177.95 0.2 1 164 45 MET CA C 57.74 0.4 1 165 45 MET N N 121.23 0.7 1 166 46 ALA H H 8.40 0.01 1 167 46 ALA C C 181.55 0.2 1 168 46 ALA CA C 55.04 0.4 1 169 46 ALA N N 120.53 0.7 1 170 47 GLN H H 7.70 0.01 1 171 47 GLN C C 179.85 0.2 1 172 47 GLN CA C 58.54 0.4 1 173 47 GLN N N 119.13 0.7 1 174 48 MET H H 8.11 0.01 1 175 48 MET C C 177.85 0.2 1 176 48 MET CA C 56.34 0.4 1 177 48 MET N N 119.53 0.7 1 178 49 GLU H H 8.80 0.01 1 179 49 GLU C C 179.75 0.2 1 180 49 GLU CA C 59.84 0.4 1 181 49 GLU N N 120.23 0.7 1 182 50 LYS H H 7.94 0.01 1 183 50 LYS C C 179.55 0.2 1 184 50 LYS CA C 58.44 0.4 1 185 50 LYS N N 121.33 0.7 1 186 51 ALA H H 7.81 0.01 1 187 51 ALA C C 179.75 0.2 1 188 51 ALA CA C 55.64 0.4 1 189 51 ALA N N 123.53 0.7 1 190 52 LEU H H 8.60 0.01 1 191 52 LEU C C 180.85 0.2 1 192 52 LEU CA C 58.34 0.4 1 193 52 LEU N N 121.63 0.7 1 194 53 SER H H 7.92 0.01 1 195 53 SER C C 175.05 0.2 1 196 53 SER CA C 61.54 0.4 1 197 53 SER N N 114.63 0.7 1 198 54 ILE H H 7.43 0.01 1 199 54 ILE C C 175.85 0.2 1 200 54 ILE CA C 60.54 0.4 1 201 54 ILE N N 114.83 0.7 1 202 55 GLY H H 7.76 0.01 1 203 55 GLY C C 173.95 0.2 1 204 55 GLY CA C 45.14 0.4 1 205 55 GLY N N 106.73 0.7 1 206 56 PHE H H 7.89 0.01 1 207 56 PHE C C 170.65 0.2 1 208 56 PHE CA C 57.34 0.4 1 209 56 PHE N N 124.43 0.7 1 210 57 GLU H H 6.89 0.01 1 211 57 GLU C C 174.55 0.2 1 212 57 GLU CA C 54.14 0.4 1 213 57 GLU N N 119.53 0.7 1 214 58 THR H H 7.94 0.01 1 215 58 THR C C 172.45 0.2 1 216 58 THR CA C 59.04 0.4 1 217 58 THR N N 110.33 0.7 1 218 59 CYS H H 8.96 0.01 1 219 59 CYS C C 175.05 0.2 1 220 59 CYS CA C 55.84 0.4 1 221 59 CYS N N 120.03 0.7 1 222 60 ARG H H 7.90 0.01 1 223 60 ARG C C 179.05 0.2 1 224 60 ARG CA C 52.94 0.4 1 225 60 ARG N N 119.23 0.7 1 226 61 TYR H H 8.41 0.01 1 227 61 TYR C C 176.25 0.2 1 228 61 TYR CA C 57.94 0.4 1 229 61 TYR N N 123.13 0.7 1 230 62 GLY H H 9.21 0.01 1 231 62 GLY C C 171.75 0.2 1 232 62 GLY CA C 44.84 0.4 1 233 62 GLY N N 105.63 0.7 1 234 63 PHE H H 7.86 0.01 1 235 63 PHE C C 175.15 0.2 1 236 63 PHE CA C 61.54 0.4 1 237 63 PHE N N 120.63 0.7 1 238 64 ILE H H 8.78 0.01 1 239 64 ILE C C 175.55 0.2 1 240 64 ILE CA C 60.94 0.4 1 241 64 ILE N N 110.83 0.7 1 242 65 GLU H H 9.20 0.01 1 243 65 GLU C C 176.95 0.2 1 244 65 GLU CA C 58.94 0.4 1 245 65 GLU N N 122.83 0.7 1 246 66 GLY H H 8.62 0.01 1 247 66 GLY C C 173.25 0.2 1 248 66 GLY CA C 46.04 0.4 1 249 66 GLY N N 116.53 0.7 1 250 67 HIS H H 7.13 0.01 1 251 67 HIS C C 172.15 0.2 1 252 67 HIS CA C 55.24 0.4 1 253 67 HIS N N 114.43 0.7 1 254 68 VAL H H 8.89 0.01 1 256 68 VAL CA C 62.84 0.4 1 257 68 VAL N N 122.93 0.7 1 258 69 VAL H H 8.67 0.01 1 259 69 VAL C C 175.05 0.2 1 262 70 ILE H H 8.51 0.01 1 263 70 ILE CA C 57.74 0.4 1 264 70 ILE N N 116.73 0.7 1 265 71 PRO C C 174.15 0.2 1 266 72 ARG H H 8.46 0.01 1 268 72 ARG CA C 52.24 0.4 1 269 72 ARG N N 120.73 0.7 1 270 73 ILE H H 9.55 0.01 1 274 74 HIS H H 9.13 0.01 1 277 78 ILE H H 7.88 0.01 1 278 78 ILE C C 175.75 0.2 1 279 78 ILE CA C 61.64 0.4 1 280 78 ILE N N 115.33 0.7 1 281 79 CYS H H 7.55 0.01 1 282 79 CYS C C 171.75 0.2 1 283 79 CYS CA C 52.84 0.4 1 284 79 CYS N N 118.93 0.7 1 285 80 ALA H H 9.08 0.01 1 286 80 ALA C C 176.25 0.2 1 287 80 ALA CA C 52.84 0.4 1 288 80 ALA N N 123.93 0.7 1 289 81 ALA H H 8.24 0.01 1 290 81 ALA C C 175.45 0.2 1 291 81 ALA CA C 53.24 0.4 1 292 81 ALA N N 119.13 0.7 1 293 82 ASN H H 7.42 0.01 1 294 82 ASN C C 174.45 0.2 1 295 82 ASN CA C 55.14 0.4 1 296 82 ASN N N 109.83 0.7 1 297 83 ASN H H 7.78 0.01 1 298 83 ASN C C 174.65 0.2 1 299 83 ASN CA C 54.84 0.4 1 300 83 ASN N N 117.33 0.7 1 301 84 THR H H 8.32 0.01 1 302 84 THR C C 174.05 0.2 1 303 84 THR CA C 60.44 0.4 1 304 84 THR N N 107.63 0.7 1 305 85 GLY H H 9.01 0.01 1 306 85 GLY C C 173.15 0.2 1 307 85 GLY CA C 43.84 0.4 1 308 85 GLY N N 108.83 0.7 1 309 86 VAL H H 8.73 0.01 1 310 86 VAL C C 173.65 0.2 1 311 86 VAL CA C 62.74 0.4 1 312 86 VAL N N 121.23 0.7 1 313 87 TYR H H 8.23 0.01 1 314 87 TYR C C 174.35 0.2 1 315 87 TYR CA C 58.54 0.4 1 316 87 TYR N N 130.43 0.7 1 317 88 ILE H H 7.42 0.01 1 318 88 ILE C C 174.45 0.2 1 319 88 ILE CA C 60.84 0.4 1 320 88 ILE N N 127.23 0.7 1 321 89 LEU H H 8.44 0.01 1 323 89 LEU CA C 53.54 0.4 1 324 89 LEU N N 129.33 0.7 1 325 90 THR H H 8.46 0.01 1 329 91 SER H H 7.87 0.01 1 330 91 SER CA C 57.24 0.4 1 331 91 SER N N 118.63 0.7 1 332 93 THR H H 8.19 0.01 1 333 93 THR C C 174.55 0.2 1 334 93 THR CA C 62.14 0.4 1 335 93 THR N N 113.13 0.7 1 336 94 SER H H 8.12 0.01 1 337 94 SER C C 173.15 0.2 1 338 94 SER CA C 58.24 0.4 1 339 94 SER N N 116.43 0.7 1 340 95 GLN H H 7.27 0.01 1 341 95 GLN C C 173.55 0.2 1 342 95 GLN CA C 54.84 0.4 1 343 95 GLN N N 118.73 0.7 1 344 96 TYR H H 8.65 0.01 1 346 96 TYR CA C 57.94 0.4 1 347 96 TYR N N 119.53 0.7 1 348 97 ASP H H 7.82 0.01 1 349 97 ASP C C 175.05 0.2 1 350 97 ASP CA C 54.54 0.4 1 351 97 ASP N N 120.03 0.7 1 352 98 THR H H 8.07 0.01 1 353 98 THR CA C 62.64 0.4 1 354 98 THR N N 110.93 0.7 1 355 99 TYR H H 8.61 0.01 1 356 99 TYR C C 174.55 0.2 1 357 99 TYR CA C 56.84 0.4 1 358 99 TYR N N 123.13 0.7 1 359 100 CYS H H 8.52 0.01 1 360 100 CYS C C 172.15 0.2 1 361 100 CYS CA C 51.64 0.4 1 362 100 CYS N N 113.63 0.7 1 363 101 PHE H H 9.95 0.01 1 364 101 PHE C C 172.65 0.2 1 365 101 PHE CA C 56.44 0.4 1 366 101 PHE N N 120.63 0.7 1 367 102 ASN H H 9.06 0.01 1 368 102 ASN C C 174.45 0.2 1 369 102 ASN CA C 51.74 0.4 1 370 102 ASN N N 128.43 0.7 1 371 103 ALA H H 8.75 0.01 1 373 103 ALA CA C 54.04 0.4 1 374 103 ALA N N 127.83 0.7 1 375 104 SER H H 8.13 0.01 1 379 105 ALA H H 6.90 0.01 1 382 107 PRO C C 175.75 0.2 1 383 108 GLU H H 7.86 0.01 1 384 108 GLU C C 174.55 0.2 1 385 108 GLU CA C 55.34 0.4 1 386 108 GLU N N 116.13 0.7 1 387 109 GLU H H 8.31 0.01 1 388 109 GLU C C 173.05 0.2 1 389 109 GLU CA C 56.34 0.4 1 390 109 GLU N N 123.43 0.7 1 391 110 ASP H H 9.45 0.01 1 392 110 ASP C C 176.35 0.2 1 393 110 ASP CA C 53.24 0.4 1 394 110 ASP N N 127.33 0.7 1 395 111 CYS H H 9.34 0.01 1 396 111 CYS C C 175.15 0.2 1 397 111 CYS CA C 52.64 0.4 1 398 111 CYS N N 124.63 0.7 1 399 112 THR H H 8.18 0.01 1 400 112 THR C C 175.05 0.2 1 401 112 THR CA C 64.74 0.4 1 402 112 THR N N 119.13 0.7 1 403 113 SER H H 8.72 0.01 1 404 113 SER C C 173.55 0.2 1 405 113 SER CA C 60.14 0.4 1 406 113 SER N N 122.23 0.7 1 407 114 VAL H H 8.87 0.01 1 408 114 VAL C C 175.95 0.2 1 409 114 VAL CA C 62.74 0.4 1 410 114 VAL N N 128.43 0.7 1 411 115 THR H H 8.06 0.01 1 413 115 THR CA C 60.84 0.4 1 414 115 THR N N 113.73 0.7 1 415 116 ASP H H 7.38 0.01 1 419 117 LEU H H 8.85 0.01 1 420 117 LEU CA C 51.44 0.4 1 421 117 LEU N N 119.53 0.7 1 422 119 ASN H H 8.19 0.01 1 423 119 ASN C C 176.05 0.2 1 424 119 ASN CA C 51.24 0.4 1 425 119 ASN N N 113.13 0.7 1 426 120 ALA H H 7.17 0.01 1 427 120 ALA C C 175.25 0.2 1 428 120 ALA CA C 52.74 0.4 1 429 120 ALA N N 121.93 0.7 1 430 121 PHE H H 8.16 0.01 1 432 121 PHE CA C 54.14 0.4 1 433 121 PHE N N 119.13 0.7 1 434 122 ASP H H 8.50 0.01 1 435 122 ASP C C 175.95 0.2 1 438 123 GLY H H 7.97 0.01 1 439 123 GLY CA C 45.44 0.4 1 440 123 GLY N N 108.63 0.7 1 441 124 PRO C C 176.85 0.2 1 442 125 ILE H H 8.21 0.01 1 443 125 ILE C C 176.85 0.2 1 444 125 ILE CA C 59.94 0.4 1 445 125 ILE N N 125.03 0.7 1 446 126 THR H H 8.34 0.01 1 447 126 THR C C 172.65 0.2 1 448 126 THR CA C 63.94 0.4 1 449 126 THR N N 122.23 0.7 1 450 127 ILE H H 9.44 0.01 1 451 127 ILE C C 174.55 0.2 1 452 127 ILE CA C 60.34 0.4 1 453 127 ILE N N 134.03 0.7 1 454 128 THR H H 9.16 0.01 1 455 128 THR C C 175.65 0.2 1 456 128 THR CA C 61.14 0.4 1 457 128 THR N N 123.33 0.7 1 458 129 ILE H H 9.44 0.01 1 459 129 ILE C C 174.65 0.2 1 460 129 ILE CA C 60.94 0.4 1 461 129 ILE N N 127.13 0.7 1 462 130 VAL H H 9.22 0.01 1 463 130 VAL C C 175.85 0.2 1 464 130 VAL CA C 61.94 0.4 1 465 130 VAL N N 127.53 0.7 1 466 131 ASN H H 8.58 0.01 1 467 131 ASN C C 177.15 0.2 1 468 131 ASN CA C 53.74 0.4 1 469 131 ASN N N 124.03 0.7 1 470 132 ARG H H 9.32 0.01 1 471 132 ARG C C 176.95 0.2 1 472 132 ARG CA C 58.44 0.4 1 473 132 ARG N N 123.43 0.7 1 474 133 ASP H H 7.99 0.01 1 475 133 ASP C C 176.75 0.2 1 476 133 ASP CA C 53.64 0.4 1 477 133 ASP N N 116.43 0.7 1 478 134 GLY H H 8.27 0.01 1 479 134 GLY C C 174.85 0.2 1 480 134 GLY CA C 44.84 0.4 1 481 134 GLY N N 108.73 0.7 1 482 135 THR H H 8.35 0.01 1 483 135 THR C C 173.95 0.2 1 484 135 THR CA C 63.44 0.4 1 485 135 THR N N 116.03 0.7 1 486 136 ARG H H 8.18 0.01 1 487 136 ARG C C 174.95 0.2 1 488 136 ARG CA C 54.34 0.4 1 489 136 ARG N N 124.13 0.7 1 490 137 TYR H H 8.84 0.01 1 491 137 TYR C C 173.65 0.2 1 492 137 TYR CA C 57.54 0.4 1 493 137 TYR N N 122.93 0.7 1 494 138 VAL H H 8.57 0.01 1 495 138 VAL C C 175.05 0.2 1 496 138 VAL CA C 61.14 0.4 1 497 138 VAL N N 122.83 0.7 1 498 139 GLN H H 9.48 0.01 1 499 139 GLN C C 172.85 0.2 1 500 139 GLN CA C 54.34 0.4 1 501 139 GLN N N 127.73 0.7 1 502 140 LYS H H 8.64 0.01 1 503 140 LYS C C 177.35 0.2 1 504 140 LYS CA C 53.94 0.4 1 505 140 LYS N N 124.13 0.7 1 506 141 GLY H H 9.15 0.01 1 507 141 GLY C C 169.35 0.2 1 508 141 GLY CA C 46.84 0.4 1 509 141 GLY N N 114.83 0.7 1 510 142 GLU H H 8.00 0.01 1 511 142 GLU C C 170.35 0.2 1 512 142 GLU CA C 54.84 0.4 1 513 142 GLU N N 118.63 0.7 1 514 143 TYR H H 8.79 0.01 1 515 143 TYR C C 173.85 0.2 1 516 143 TYR CA C 57.24 0.4 1 517 143 TYR N N 116.63 0.7 1 518 144 ARG H H 8.96 0.01 1 520 144 ARG CA C 57.04 0.4 1 521 144 ARG N N 127.93 0.7 1 522 145 THR H H 8.83 0.01 1 523 145 THR C C 174.75 0.2 1 526 146 ASN H H 8.81 0.01 1 527 146 ASN CA C 49.94 0.4 1 528 146 ASN N N 125.03 0.7 1 529 147 PRO C C 177.85 0.2 1 530 148 GLU H H 7.95 0.01 1 531 148 GLU C C 177.55 0.2 1 532 148 GLU CA C 58.14 0.4 1 533 148 GLU N N 115.23 0.7 1 534 149 ASP H H 7.83 0.01 1 536 149 ASP CA C 55.54 0.4 1 537 149 ASP N N 115.03 0.7 1 538 150 ILE H H 7.13 0.01 1 539 150 ILE C C 175.55 0.2 1 542 151 TYR H H 7.95 0.01 1 543 151 TYR CA C 54.84 0.4 1 544 151 TYR N N 120.13 0.7 1 546 153 SER H H 8.75 0.01 1 547 153 SER C C 173.95 0.2 1 550 154 ASN H H 8.54 0.01 1 551 154 ASN CA C 51.34 0.4 1 552 154 ASN N N 121.23 0.7 1 553 155 PRO C C 177.05 0.2 1 554 156 THR H H 8.34 0.01 1 555 156 THR C C 174.45 0.2 1 556 156 THR CA C 61.64 0.4 1 557 156 THR N N 113.53 0.7 1 558 157 ASP H H 8.33 0.01 1 559 157 ASP C C 175.75 0.2 1 560 157 ASP CA C 54.64 0.4 1 561 157 ASP N N 122.33 0.7 1 562 158 ASP H H 8.35 0.01 1 564 158 ASP CA C 54.44 0.4 1 565 158 ASP N N 121.33 0.7 1 566 159 ASP H H 8.28 0.01 1 570 160 VAL H H 7.63 0.01 1 stop_ save_