data_21033 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Solution structure of Lewis x (Gal-beta1,4-[Fuc-alpha1,3]-GlcNAc-beta) attached to a protein ; _BMRB_accession_number 21033 _BMRB_flat_file_name bmr21033.str _Entry_type new _Submission_date 2013-01-21 _Accession_date 2013-01-24 _Entry_origination author _NMR_STAR_version 2.1.1 _Experimental_method NMR _Details . loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Zierke Mirko . . 2 Ernst Beat . . 3 Allain Frederic . . 4 Schubert Mario . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 28 "13C chemical shifts" 20 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2013-09-26 original author 'original release, coordinate file annotated by PDBj' stop_ loop_ _Related_BMRB_accession_number _Relationship 21031 'Solution structure of Lewis a [Gal-beta1_3-(Fuc-alpha1_4-)GlcNAc-beta-Me]' 21032 'Solution structure of 1,3-Fucosylated chitobiose' 21034 'Solution structure of Lewisx (Gal-beta1,4-[Fuc-alpha1,3-]GlcNAc-beta-OMe)at 277 K' stop_ save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title 'Stabilization of Branched Oligosaccharides: Lewis(x) Benefits from a Nonconventional C-H...O Hydrogen Bond' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 24001318 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Zierke Mirko . . 2 Smiesko Martin . . 3 Rabbani Said . . 4 Aeschbacher Thomas . . 5 Cutting Brian . . 6 Allain Frederic H.-T. . 7 Schubert Mario . . 8 Ernst Beat . . stop_ _Journal_abbreviation 'J. Am. Chem. Soc.' _Journal_volume 135 _Journal_issue 36 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 13464 _Page_last 13472 _Year 2013 _Details . save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name Lewisx-FimH _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label Lewisx $SUGAR_(3-MER) 'Protein FimH' $FimH stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state ? _System_paramagnetic no _System_thiol_state . _Database_query_date . _Details 'The trisaccharide is linked to Cys78 of the protein FimH via a spacer (please see Figure).' save_ ######################## # Monomeric polymers # ######################## save_SUGAR_(3-MER) _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class carbohydrate _Name_common SUGAR_(3-MER) _Molecular_mass 543.521 _Mol_thiol_state 'not present' _Details ; D-Gal-beta1,4-[L-Fuc-alpha1,3]-D-GlcNAc-beta-sp8a the spacer (SP8a) is 3-(m-Maleimidobenzamido)propyl ; ############################## # Polymer residue sequence # ############################## _Residue_count 4 _Mol_residue_sequence XXXX loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 SP8a SP8a 2 NAG NAG 3 GAL GAL 4 FUC FUC stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date . save_ save_FimH _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common FimH _Molecular_mass . _Mol_thiol_state 'disulfide and other bound' _Details . _Residue_count 173 _Mol_residue_sequence ; FACKTANGTAIPIGGGSANV YVNLAPVVNVGQNLVVDLST QIFCHNDYPETITDYVTLQR GSAYGGVLSNFSGTVKYCGS SYPFPTTSETPRVVYNSRTD KPWPVALYLTPVSSAGGVAI KAGSLIAVLILRQTNNYNSD DFQFVWNIYANNDVVVPTGL VPRGSLEHHHHHH ; loop_ _Residue_seq_code _Residue_label 1 PHE 2 ALA 3 CYS 4 LYS 5 THR 6 ALA 7 ASN 8 GLY 9 THR 10 ALA 11 ILE 12 PRO 13 ILE 14 GLY 15 GLY 16 GLY 17 SER 18 ALA 19 ASN 20 VAL 21 TYR 22 VAL 23 ASN 24 LEU 25 ALA 26 PRO 27 VAL 28 VAL 29 ASN 30 VAL 31 GLY 32 GLN 33 ASN 34 LEU 35 VAL 36 VAL 37 ASP 38 LEU 39 SER 40 THR 41 GLN 42 ILE 43 PHE 44 CYS 45 HIS 46 ASN 47 ASP 48 TYR 49 PRO 50 GLU 51 THR 52 ILE 53 THR 54 ASP 55 TYR 56 VAL 57 THR 58 LEU 59 GLN 60 ARG 61 GLY 62 SER 63 ALA 64 TYR 65 GLY 66 GLY 67 VAL 68 LEU 69 SER 70 ASN 71 PHE 72 SER 73 GLY 74 THR 75 VAL 76 LYS 77 TYR 78 CYS 79 GLY 80 SER 81 SER 82 TYR 83 PRO 84 PHE 85 PRO 86 THR 87 THR 88 SER 89 GLU 90 THR 91 PRO 92 ARG 93 VAL 94 VAL 95 TYR 96 ASN 97 SER 98 ARG 99 THR 100 ASP 101 LYS 102 PRO 103 TRP 104 PRO 105 VAL 106 ALA 107 LEU 108 TYR 109 LEU 110 THR 111 PRO 112 VAL 113 SER 114 SER 115 ALA 116 GLY 117 GLY 118 VAL 119 ALA 120 ILE 121 LYS 122 ALA 123 GLY 124 SER 125 LEU 126 ILE 127 ALA 128 VAL 129 LEU 130 ILE 131 LEU 132 ARG 133 GLN 134 THR 135 ASN 136 ASN 137 TYR 138 ASN 139 SER 140 ASP 141 ASP 142 PHE 143 GLN 144 PHE 145 VAL 146 TRP 147 ASN 148 ILE 149 TYR 150 ALA 151 ASN 152 ASN 153 ASP 154 VAL 155 VAL 156 VAL 157 PRO 158 THR 159 GLY 160 LEU 161 VAL 162 PRO 163 ARG 164 GLY 165 SER 166 LEU 167 GLU 168 HIS 169 HIS 170 HIS 171 HIS 172 HIS 173 HIS stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-08-05 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 BMRB 19066 FIMH 91.33 158 99.37 99.37 1.38e-107 BMRB 19254 FIMH_Y48A_mutant 91.33 158 98.73 98.73 1.64e-106 BMRB 19255 FIMH_Y48A_mutant 91.33 158 98.73 98.73 1.64e-106 BMRB 19256 FIMH 91.33 158 99.37 99.37 1.38e-107 BMRB 26541 FimH-CRD 100.00 173 99.42 99.42 8.99e-121 PDB 1KIU "Fimh Adhesin Q133n Mutant-Fimc Chaperone Complex With Methyl-Alpha-D-Mannose" 91.91 279 98.74 98.74 2.18e-106 PDB 1KLF "Fimh Adhesin-Fimc Chaperone Complex With D-Mannose" 91.91 279 99.37 99.37 2.47e-107 PDB 1QUN "X-Ray Structure Of The Fimc-Fimh Chaperone Adhesin Complex From Uropathogenic E.Coli" 91.91 279 99.37 99.37 2.47e-107 PDB 1UWF "1.7 A Resolution Structure Of The Receptor Binding Domain Of The Fimh Adhesin From Uropathogenic E. Coli" 91.33 158 99.37 99.37 1.38e-107 PDB 2VCO "Crystal Structure Of The Fimbrial Adhesin Fimh In Complex With Its High-Mannose Epitope" 91.33 158 99.37 99.37 1.38e-107 PDB 3JWN "Complex Of Fimc, Fimf, Fimg And Fimh" 91.91 279 98.11 98.74 1.16e-105 PDB 3MCY "Crystal Structure Of Fimh Lectin Domain Bound To Biphenyl Mannoside Meta-Methyl Ester" 91.91 181 99.37 99.37 7.21e-108 PDB 3RFZ "Crystal Structure Of The Fimd Usher Bound To Its Cognate Fimc:fimh Substrate" 91.91 279 99.37 99.37 2.42e-107 PDB 3ZL1 "A Thiazolyl-mannoside Bound To Fimh, Monoclinic Space Group" 91.33 158 99.37 99.37 1.38e-107 PDB 3ZL2 "A Thiazolyl-mannoside Bound To Fimh, Orthorhombic Space Group" 91.33 158 99.37 99.37 1.38e-107 PDB 3ZPD "Solution Structure Of The Fimh Adhesin Carbohydrate-binding Domain" 91.33 158 99.37 99.37 1.38e-107 PDB 4ATT "Fimh Lectin Domain Co-crystal With A Alpha-d-mannoside O- Linked To A Propynyl Para Methoxy Phenyl" 91.33 158 99.37 99.37 1.38e-107 PDB 4AUJ "Fimh Lectin Domain Co-crystal With A Alpha-d-mannoside O- Linked To Para Hydroxypropargyl Phenyl" 91.33 158 99.37 99.37 1.38e-107 PDB 4AUU "Crystal Structure Of Apo Fimh Lectin Domain At 1.5 A Resolution" 91.33 158 99.37 99.37 1.38e-107 PDB 4AUY "Structure Of The Fimh Lectin Domain In The Trigonal Space Group, In Complex With An Hydroxyl Propynyl Phenyl Alpha-D- Mannoside" 91.33 158 99.37 99.37 1.38e-107 PDB 4AV0 "Structure Of The Fimh Lectin Domain In The Trigonal Space Group, In Complex With A Methoxy Phenyl Propynyl Alpha-D- Mannoside " 91.33 158 99.37 99.37 1.38e-107 PDB 4AV4 "Fimh Lectin Domain Co-Crystal With A Alpha-D-Mannoside O-Linked To A Propynyl Pyridine" 91.33 158 98.73 99.37 8.91e-107 PDB 4AV5 "Structure Of A Triclinic Crystal Of The Fimh Lectin Domain In Complex With A Propynyl Biphenyl Alpha-D-Mannoside, At 1.4 A Reso" 91.33 158 99.37 99.37 1.38e-107 PDB 4AVH "Structure Of The Fimh Lectin Domain In The Trigonal Space Group, In Complex With A Thioalkyl Alpha-D-Mannoside At 2.1 A Resolut" 91.33 158 99.37 99.37 1.38e-107 PDB 4AVI "Structure Of The Fimh Lectin Domain In The Trigonal Space Group, In Complex With A Methyl Ester Octyl Alpha-D- Mannoside At 2.4" 91.33 158 99.37 99.37 1.38e-107 PDB 4AVJ "Structure Of The Fimh Lectin Domain In The Trigonal Space Group, In Complex With A Methanol Triazol Ethyl Phenyl Alpha-D-Mannos" 91.33 158 99.37 99.37 1.38e-107 PDB 4AVK "Structure Of Trigonal Fimh Lectin Domain Crystal Soaked With An Alpha-D-Mannoside O-Linked To Propynyl Pyridine At 2.4 A Resolu" 91.33 158 99.37 99.37 1.38e-107 PDB 4BUQ "Crystal Structure Of Wild Type Fimh Lectin Domain In Complex With Heptyl Alpha-d-mannopyrannoside" 91.33 158 99.37 99.37 1.38e-107 PDB 4CA4 "Crystal Structure Of Fimh Lectin Domain With The Tyr48ala Mutation, In Complex With Heptyl Alpha-d-mannopyrannoside" 91.33 158 98.73 98.73 1.64e-106 PDB 4CSS "Crystal Structure Of Fimh In Complex With A Sulfonamide Biphenyl Alpha D-mannoside" 94.22 163 99.39 99.39 1.86e-111 PDB 4CST "Crystal Structure Of Fimh In Complex With 3'-chloro-4'- (alpha-d-mannopyranosyloxy)-biphenyl-4-carbonitrile" 93.64 163 99.38 99.38 1.67e-110 PDB 4J3O "Crystal Structure Of The Fimd Usher Traversed By The Pilus Tip Complex Assembly Composed Of Fimc:fimf:fimg:fimh" 91.91 279 99.37 99.37 2.47e-107 PDB 4LOV "Crystal Structure Of Fimh In Complex With Heptylmannoside" 91.33 158 99.37 99.37 1.38e-107 PDB 4X50 "Crystal Structure Of Fimh In Complex With Biphenyl Alpha-d- Mannopyranoside" 92.49 160 99.38 99.38 5.15e-109 PDB 4X5P "Crystal Structure Of Fimh In Complex With A Benzoyl-amidophenyl Alpha- D-mannopyranoside" 92.49 160 99.38 99.38 5.15e-109 PDB 4X5Q "Crystal Structure Of Fimh In Complex With 5-nitro-indolinylphenyl Alpha-d-mannopyranoside" 92.49 160 99.38 99.38 5.15e-109 PDB 4X5R "Crystal Structure Of Fimh In Complex With A Squaryl-phenyl Alpha-d- Mannopyranoside Derivative" 92.49 160 99.38 99.38 5.15e-109 DBJ BAB38702 "minor fimbrial subunit/D-mannose specific adhesin [Escherichia coli O157:H7 str. Sakai]" 91.91 300 98.11 98.11 7.36e-106 DBJ BAE78313 "minor component of type 1 fimbriae [Escherichia coli str. K12 substr. W3110]" 91.91 300 99.37 99.37 3.98e-107 DBJ BAG80117 "type-1 fimbrial minor subunit FimH [Escherichia coli SE11]" 91.91 300 98.74 98.74 1.29e-106 DBJ BAI28639 "minor component FimH of type 1 fimbriae [Escherichia coli O26:H11 str. 11368]" 91.91 300 97.48 97.48 2.62e-104 DBJ BAI33780 "minor component FimH of type 1 fimbriae [Escherichia coli O103:H2 str. 12009]" 91.91 300 98.74 98.74 1.29e-106 EMBL CAA12423 "type 1 fimbriae adhesin, precursor polypeptide [Escherichia coli]" 91.91 300 97.48 98.11 9.21e-105 EMBL CAA29156 "unnamed protein product [Escherichia coli]" 91.91 300 99.37 99.37 4.20e-107 EMBL CAH55784 "type 1 fimbrial adhesin subunit FimH [Escherichia coli]" 91.91 300 98.11 98.74 1.61e-105 EMBL CAM92099 "Type 1 fimbrial adhesin FimH [Escherichia coli]" 91.91 303 99.37 99.37 3.13e-107 EMBL CAP78801 "Protein fimH [Escherichia coli LF82]" 91.91 300 97.48 98.11 2.32e-104 GB AAA97216 "CG Site No. 18337 [Escherichia coli str. K-12 substr. MG1655]" 91.91 300 99.37 99.37 3.98e-107 GB AAB29812 "FimH subunit=mannose-sensitive type 1 fimbrial adhesin [Escherichia coli, CSH-50, HB101, Peptide, 300 aa]" 91.91 300 98.74 98.74 4.87e-106 GB AAC35864 "FimH [Escherichia coli]" 91.91 300 97.48 98.74 4.95e-105 GB AAC77276 "minor component of type 1 fimbriae [Escherichia coli str. K-12 substr. MG1655]" 91.91 300 99.37 99.37 3.98e-107 GB AAD44319 "FimH precursor [Escherichia coli]" 91.91 300 99.37 99.37 4.29e-107 REF NP_313306 "D-mannose specific adhesin [Escherichia coli O157:H7 str. Sakai]" 91.91 300 98.11 98.11 7.36e-106 REF NP_418740 "minor component of type 1 fimbriae [Escherichia coli str. K-12 substr. MG1655]" 91.91 300 99.37 99.37 3.98e-107 REF NP_709914 "minor fimbrial subunit, D-mannose specific adhesin [Shigella flexneri 2a str. 301]" 91.91 300 99.37 99.37 3.13e-107 REF WP_000816510 "fimbrial protein FimH [Shigella flexneri]" 91.91 300 99.37 99.37 3.41e-107 REF WP_000816511 "fimbrial protein FimH [Shigella flexneri]" 91.91 300 99.37 99.37 3.13e-107 SP P08191 "RecName: Full=Protein FimH; Flags: Precursor" 91.91 300 99.37 99.37 3.98e-107 stop_ save_ ###################### # Polymer residues # ###################### save_chem_comp_NAG _Saveframe_category polymer_residue _Mol_type D-SACCHARIDE _Name_common N-ACETYL-D-GLUCOSAMINE _BMRB_code NAG _PDB_code NAG _Standard_residue_derivative . _Molecular_mass 221.208 _Mol_paramagnetic . _Details . loop_ _Atom_name _PDB_atom_name _Atom_type _Atom_chirality _Atom_charge _Atom_oxidation_number _Atom_unpaired_electrons C1 C1 C . 0 . ? C2 C2 C . 0 . ? C3 C3 C . 0 . ? C4 C4 C . 0 . ? C5 C5 C . 0 . ? C6 C6 C . 0 . ? C7 C7 C . 0 . ? C8 C8 C . 0 . ? H1 H1 H . 0 . ? H2 H2 H . 0 . ? H3 H3 H . 0 . ? H4 H4 H . 0 . ? H5 H5 H . 0 . ? H61 H61 H . 0 . ? H62 H62 H . 0 . ? H81 H81 H . 0 . ? H82 H82 H . 0 . ? H83 H83 H . 0 . ? HN2 HN2 H . 0 . ? HO1 HO1 H . 0 . ? HO3 HO3 H . 0 . ? HO4 HO4 H . 0 . ? HO6 HO6 H . 0 . ? N2 N2 N . 0 . ? O1 O1 O . 0 . ? O3 O3 O . 0 . ? O4 O4 O . 0 . ? O5 O5 O . 0 . ? O6 O6 O . 0 . ? O7 O7 O . 0 . ? stop_ loop_ _Bond_order _Bond_atom_one_atom_name _Bond_atom_two_atom_name _PDB_bond_atom_one_atom_name _PDB_bond_atom_two_atom_name SING C1 C2 ? ? SING C1 O1 ? ? SING C1 O5 ? ? SING C1 H1 ? ? SING C2 C3 ? ? SING C2 N2 ? ? SING C2 H2 ? ? SING C3 C4 ? ? SING C3 O3 ? ? SING C3 H3 ? ? SING C4 C5 ? ? SING C4 O4 ? ? SING C4 H4 ? ? SING C5 C6 ? ? SING C5 O5 ? ? SING C5 H5 ? ? SING C6 O6 ? ? SING C6 H61 ? ? SING C6 H62 ? ? SING C7 C8 ? ? SING C7 N2 ? ? DOUB C7 O7 ? ? SING C8 H81 ? ? SING C8 H82 ? ? SING C8 H83 ? ? SING N2 HN2 ? ? SING O1 HO1 ? ? SING O3 HO3 ? ? SING O4 HO4 ? ? SING O6 HO6 ? ? stop_ save_ save_chem_comp_GAL _Saveframe_category polymer_residue _Mol_type D-SACCHARIDE _Name_common BETA-D-GALACTOSE _BMRB_code GAL _PDB_code GAL _Standard_residue_derivative . _Molecular_mass 180.156 _Mol_paramagnetic . _Details . loop_ _Atom_name _PDB_atom_name _Atom_type _Atom_chirality _Atom_charge _Atom_oxidation_number _Atom_unpaired_electrons C1 C1 C . 0 . ? C2 C2 C . 0 . ? C3 C3 C . 0 . ? C4 C4 C . 0 . ? C5 C5 C . 0 . ? C6 C6 C . 0 . ? H1 H1 H . 0 . ? H2 H2 H . 0 . ? H3 H3 H . 0 . ? H4 H4 H . 0 . ? H5 H5 H . 0 . ? H61 H61 H . 0 . ? H62 H62 H . 0 . ? HO1 HO1 H . 0 . ? HO2 HO2 H . 0 . ? HO3 HO3 H . 0 . ? HO4 HO4 H . 0 . ? HO6 HO6 H . 0 . ? O1 O1 O . 0 . ? O2 O2 O . 0 . ? O3 O3 O . 0 . ? O4 O4 O . 0 . ? O5 O5 O . 0 . ? O6 O6 O . 0 . ? stop_ loop_ _Bond_order _Bond_atom_one_atom_name _Bond_atom_two_atom_name _PDB_bond_atom_one_atom_name _PDB_bond_atom_two_atom_name SING C1 C2 ? ? SING C1 O1 ? ? SING C1 O5 ? ? SING C1 H1 ? ? SING C2 C3 ? ? SING C2 O2 ? ? SING C2 H2 ? ? SING C3 C4 ? ? SING C3 O3 ? ? SING C3 H3 ? ? SING C4 C5 ? ? SING C4 O4 ? ? SING C4 H4 ? ? SING C5 C6 ? ? SING C5 O5 ? ? SING C5 H5 ? ? SING C6 O6 ? ? SING C6 H61 ? ? SING C6 H62 ? ? SING O1 HO1 ? ? SING O2 HO2 ? ? SING O3 HO3 ? ? SING O4 HO4 ? ? SING O6 HO6 ? ? stop_ save_ save_chem_comp_FUC _Saveframe_category polymer_residue _Mol_type SACCHARIDE _Name_common ALPHA-L-FUCOSE _BMRB_code FUC _PDB_code FUC _Standard_residue_derivative . _Molecular_mass 164.156 _Mol_paramagnetic . _Details . loop_ _Atom_name _PDB_atom_name _Atom_type _Atom_chirality _Atom_charge _Atom_oxidation_number _Atom_unpaired_electrons C1 C1 C . 0 . ? C2 C2 C . 0 . ? C3 C3 C . 0 . ? C4 C4 C . 0 . ? C5 C5 C . 0 . ? C6 C6 C . 0 . ? H1 H1 H . 0 . ? H2 H2 H . 0 . ? H3 H3 H . 0 . ? H4 H4 H . 0 . ? H5 H5 H . 0 . ? H61 H61 H . 0 . ? H62 H62 H . 0 . ? H63 H63 H . 0 . ? HO1 HO1 H . 0 . ? HO2 HO2 H . 0 . ? HO3 HO3 H . 0 . ? HO4 HO4 H . 0 . ? O1 O1 O . 0 . ? O2 O2 O . 0 . ? O3 O3 O . 0 . ? O4 O4 O . 0 . ? O5 O5 O . 0 . ? stop_ loop_ _Bond_order _Bond_atom_one_atom_name _Bond_atom_two_atom_name _PDB_bond_atom_one_atom_name _PDB_bond_atom_two_atom_name SING C1 C2 ? ? SING C1 O1 ? ? SING C1 O5 ? ? SING C1 H1 ? ? SING C2 C3 ? ? SING C2 O2 ? ? SING C2 H2 ? ? SING C3 C4 ? ? SING C3 O3 ? ? SING C3 H3 ? ? SING C4 C5 ? ? SING C4 O4 ? ? SING C4 H4 ? ? SING C5 C6 ? ? SING C5 O5 ? ? SING C5 H5 ? ? SING C6 H61 ? ? SING C6 H62 ? ? SING C6 H63 ? ? SING O1 HO1 ? ? SING O2 HO2 ? ? SING O3 HO3 ? ? SING O4 HO4 ? ? stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $SUGAR_(3-MER) Human 9606 Eukaryota Metazoa Homo sapiens $FimH 'E. coli' 562 Eubacteria . Escherichia coli 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 $SUGAR_(3-MER) 'chemical synthesis' . . . . . $FimH 'recombinant technology' 'E. coli' . . . . stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $SUGAR_(3-MER) 0.5 mM 'natural abundance' $FimH 0.5 mM 'natural abundance' D2O 100 % . stop_ save_ save_sample_2 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $SUGAR_(3-MER) 0.5 mM 'natural abundance' $FimH 0.5 mM 'natural abundance' H2O 93 % . D2O 7 % . stop_ save_ ############################ # Computer software used # ############################ save_TOPSPIN _Saveframe_category software _Name TOPSPIN _Version . loop_ _Vendor _Address _Electronic_address 'Bruker Biospin' . . stop_ loop_ _Task collection processing stop_ _Details . save_ save_SPARKY _Saveframe_category software _Name SPARKY _Version . loop_ _Vendor _Address _Electronic_address Goddard . . stop_ loop_ _Task 'chemical shift assignment' processing stop_ _Details . save_ save_CYANA _Saveframe_category software _Name CYANA _Version . loop_ _Vendor _Address _Electronic_address 'Guntert, Mumenthaler and Wuthrich' . . stop_ loop_ _Task 'structure solution' stop_ _Details . save_ save_AMBER _Saveframe_category software _Name AMBER _Version . loop_ _Vendor _Address _Electronic_address 'Case, Darden, Cheatham, III, Simmerling, Wang, Duke, Luo, ... and Kollm' . . stop_ loop_ _Task refinement 'structure solution' stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model Avance _Field_strength 500 _Details . save_ save_spectrometer_2 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model Avance _Field_strength 900 _Details . save_ ############################# # NMR applied experiments # ############################# save_2D_1H-13C_HSQC_1 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-13C HSQC' _Sample_label $sample_1 save_ save_2D_F1_13C-filtered_1H-1H_TOCSY_2 _Saveframe_category NMR_applied_experiment _Experiment_name '2D F1 13C-filtered 1H-1H TOCSY' _Sample_label $sample_1 save_ save_2D_1H-13C_HMQC-COSY_3 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-13C HMQC-COSY' _Sample_label $sample_1 save_ save_2D_F1/F2_13C-filtered_1H-1H_NOESY_4 _Saveframe_category NMR_applied_experiment _Experiment_name '2D F1/F2 13C-filtered 1H-1H NOESY' _Sample_label $sample_1 save_ save_2D_F1/F2_15N-filtered_1H-1H_NOESY_5 _Saveframe_category NMR_applied_experiment _Experiment_name '2D F1/F2 15N-filtered 1H-1H NOESY' _Sample_label $sample_2 save_ save_2D_1H-13C_HSQC_6 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-13C HSQC' _Sample_label $sample_1 save_ ####################### # Sample conditions # ####################### save_sample_conditions_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units temperature 293 . K pH 7.0 . pH stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference_1 _Saveframe_category chemical_shift_reference _Details . loop_ _Mol_common_name _Atom_type _Atom_isotope_number _Atom_group _Chem_shift_units _Chem_shift_value _Reference_method _Reference_type _External_reference_sample_geometry _External_reference_location _External_reference_axis _Indirect_shift_ratio DSS H 1 'methyl protons' ppm 0.00 internal direct . 'separate tube (no insert) similar to the experimental sample tube' . 1.000000000 DSS C 13 'methyl protons' ppm 0.00 na indirect . . . 0.251449530 stop_ save_ ################################### # Assigned chemical shift lists # ################################### ################################################################### # Chemical Shift Ambiguity Index Value Definitions # # # # The values other than 1 are used for those atoms with different # # chemical shifts that cannot be assigned to stereospecific atoms # # or to specific residues or chains. # # # # Index Value Definition # # # # 1 Unique (including isolated methyl protons, # # geminal atoms, and geminal methyl # # groups with identical chemical shifts) # # (e.g. ILE HD11, HD12, HD13 protons) # # 2 Ambiguity of geminal atoms or geminal methyl # # proton groups (e.g. ASP HB2 and HB3 # # protons, LEU CD1 and CD2 carbons, or # # LEU HD11, HD12, HD13 and HD21, HD22, # # HD23 methyl protons) # # 3 Aromatic atoms on opposite sides of # # symmetrical rings (e.g. TYR HE1 and HE2 # # protons) # # 4 Intraresidue ambiguities (e.g. LYS HG and # # HD protons or TRP HZ2 and HZ3 protons) # # 5 Interresidue ambiguities (LYS 12 vs. LYS 27) # # 6 Intermolecular ambiguities (e.g. ASP 31 CA # # in monomer 1 and ASP 31 CA in monomer 2 # # of an asymmetrical homodimer, duplex # # DNA assignments, or other assignments # # that may apply to atoms in one or more # # molecule in the molecular assembly) # # 9 Ambiguous, specific ambiguity not defined # # # ################################################################### save_assigned_chem_shift_list_1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Experiment_label '2D 1H-13C HSQC' '2D F1 13C-filtered 1H-1H TOCSY' '2D 1H-13C HMQC-COSY' '2D F1/F2 13C-filtered 1H-1H NOESY' '2D F1/F2 15N-filtered 1H-1H NOESY' stop_ loop_ _Sample_label $sample_1 $sample_2 stop_ _Sample_conditions_label $sample_conditions_1 _Chem_shift_reference_set_label $chemical_shift_reference_1 _Mol_system_component_name Lewisx _Text_data_format . _Text_data . loop_ _Atom_shift_assign_ID _Residue_author_seq_code _Residue_seq_code _Residue_label _Atom_name _Atom_type _Chem_shift_value _Chem_shift_value_error _Chem_shift_ambiguity_code 1 1 1 SP8a C1 C 70.612 0.050 1 2 1 1 SP8a H11 H 3.963 0.005 2 3 1 1 SP8a H12 H 3.684 0.005 2 4 2 2 NAG C1 C 103.640 0.050 1 5 2 2 NAG C2 C 58.514 0.050 1 6 2 2 NAG C3 C 77.672 0.050 1 7 2 2 NAG C4 C 76.100 0.050 1 8 2 2 NAG C5 C 78.064 0.050 1 9 2 2 NAG C6 C 62.495 0.050 1 10 2 2 NAG C8 C 24.974 0.050 1 11 2 2 NAG H1 H 4.541 0.005 1 12 2 2 NAG H2 H 3.910 0.005 1 13 2 2 NAG H3 H 3.861 0.006 1 14 2 2 NAG H4 H 3.898 0.005 1 15 2 2 NAG H5 H 3.573 0.005 1 16 2 2 NAG H61 H 3.825 0.005 1 17 2 2 NAG H62 H 3.970 0.005 1 18 2 2 NAG H81 H 2.014 0.005 1 19 2 2 NAG H82 H 2.014 0.005 1 20 2 2 NAG H83 H 2.014 0.005 1 21 2 2 NAG HN2 H 8.442 0.005 1 22 3 3 GAL C1 C 104.565 0.050 1 23 3 3 GAL C2 C 73.749 0.050 1 24 3 3 GAL C3 C 75.149 0.050 1 25 3 3 GAL C4 C 71.059 0.050 1 26 3 3 GAL C5 C 77.612 0.050 1 27 3 3 GAL C6 C 64.225 0.050 1 28 3 3 GAL H1 H 4.438 0.005 1 29 3 3 GAL H2 H 3.493 0.005 1 30 3 3 GAL H3 H 3.646 0.005 1 31 3 3 GAL H4 H 3.892 0.005 1 32 3 3 GAL H5 H 3.588 0.005 1 33 3 3 GAL H61 H 3.715 0.005 2 34 3 3 GAL H62 H 3.715 0.005 2 35 4 4 FUC C1 C 101.384 0.050 1 36 4 4 FUC C2 C 70.426 0.050 1 37 4 4 FUC C3 C 71.930 0.050 1 38 4 4 FUC C4 C 74.679 0.050 1 39 4 4 FUC C5 C 69.421 0.050 1 40 4 4 FUC C6 C 18.085 0.050 1 41 4 4 FUC H1 H 5.109 0.005 1 42 4 4 FUC H2 H 3.693 0.006 1 43 4 4 FUC H3 H 3.901 0.005 1 44 4 4 FUC H4 H 3.790 0.005 1 45 4 4 FUC H5 H 4.841 0.005 1 46 4 4 FUC H61 H 1.175 0.005 1 47 4 4 FUC H62 H 1.175 0.005 1 48 4 4 FUC H63 H 1.175 0.005 1 stop_ save_