FMO DATABASE

FMODB ID: Q5Q8Y

Calculation Name: 1UWF-A-Xray549

Preferred Name: Adhesin protein fimH

Target Type: SINGLE PROTEIN

Ligand Name: butyl alpha-d-mannopyranoside

Ligand 3-letter code: DEG

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 1UWF

Chain ID: A

ChEMBL ID: CHEMBL4837

UniProt ID: P08191

Base Structure: X-ray

Registration Date: 2025-10-11

Reference: Sci Data 11, 1164 (2024).

DOI: https://doi.org/10.1038/s41597-024-03999-2

Apendix: None

IFIE MAP

IFIE Diagram

Modeling method

Optimization	MOE:Amber10:EHT
Restraint	OptH
Protonation	MOE:Protonate 3D
Complement	ac.sh, 23 2024 Oct
Water	No
Procedure	Manual calculation
Remarks

FMO calculation

FMO method	FMO2-MP2/6-31G(d)
Fragmentation	Auto
Number of fragment	157
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230922

Total energy (hartree)

FMO2-HF: Electronic energy	-1429120.050678
FMO2-HF: Nuclear repulsion	1370505.496685
FMO2-HF: Total energy	-58614.553993
FMO2-MP2: Total energy	-58788.435484

3D Structure Molmil

Snapshot

Ligand structure

Ligand Interaction

Ligand binding energy

IFIE [kcal/mol]	PIEDA [kcal/mol]				Charge transfer value [e]
IFIE SUMIFIE SUM at MP2 level.	ESElectro static interaction energy.	EXExchange-repulsion energy.	CT+mixCharge transfer and mixing terms energy.	DI(MP2)Dispersion energy.	q(I=>J)Charge transfer value from I to J fragments.
N/A	N/A	N/A	N/A	N/A	N/A

Interactive mode: IFIE and PIEDA for fragment #1(A:1:PHE)

Summations of interaction energy for fragment #1(A:1:PHE)

IFIE [kcal/mol]	PIEDA [kcal/mol]				Charge transfer value [e]
IFIE SUMIFIE SUM at MP2 level.	ESElectro static interaction energy.	EXExchange-repulsion energy.	CT+mixCharge transfer and mixing terms energy.	DI(MP2)Dispersion energy.	q(I=>J)Charge transfer value from I to J fragments.
-161.052	-140.011	45.983	-25.037	-41.984	-0.196

Interaction energy analysis for fragmet #1(A:1:PHE)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 1 / q_Mulliken : 0.710 / q_NPA : 0.849

Distance from base fragment(s) [Å]

Dist

Interaction energy by IFIE and PIEDA
[kcal/mol]

| Total | > | ES | > | EX | >
| CT+mix | > | DI(MP2) | >

Fragment charge [e]

FCHARGE q_Mulliken
q_NPA q(I=>J)

Residue

Res # RES

Sort

Graph Options

X Axis Label
Y Axis Max Y Axis Min
Display ES EX CT+mix DI(MP2)

frag_NumFragment number.	ChainChain species.	Res #Residue number.	RES3-letter code of amino acid residue, ligand and solvent molecule.	FCHARGEFormal charge [e].	q_MullikenFragment charge evaluated by Mulliken charge [e].	q_NPAFragment charge evaluated by natural population analysis(NPA) charge [e].	DISTDistance from Ligand [Å].	TotalIFIE at MP2 level [kcal/mol].	ESElectro static interaction energy by PIEDA [kcal/mol].	EXExchange-repulsion energy by PIEDA [kcal/mol].	CT+mixCharge transfer and mixing terms energy by PIEDA [kcal/mol].	DI(MP2)Dispersion energy by PIEDA [kcal/mol].	q(I=>J)Charge transfer value from I to J fragmens [e].
3	A	3	CYS	0	-0.034	0.003	2.658	-0.777	1.367	7.961	-2.974	-7.131	0.012
13	A	13	ILE	0	0.041	0.005	2.505	-5.024	-4.067	0.340	-0.383	-0.914	-0.003
14	A	14	GLY	0	-0.001	0.006	4.626	7.507	7.718	-0.001	-0.018	-0.192	0.000
44	A	45	HIS	1	0.829	0.900	4.311	51.713	52.739	0.014	-0.276	-0.763	0.000
45	A	46	ASN	0	0.007	-0.026	2.193	-24.726	-22.450	5.882	-4.125	-4.032	-0.036
46	A	47	ASP	-1	-0.780	-0.886	1.749	-100.013	-101.551	13.505	-7.125	-4.843	-0.097
47	A	48	TYR	0	-0.010	0.003	3.921	9.851	9.986	0.000	-0.042	-0.092	0.000
53	A	54	ASP	-1	-0.781	-0.899	2.445	-95.023	-88.203	3.328	-4.496	-5.653	-0.052
54	A	55	TYR	0	-0.065	-0.049	4.836	5.078	5.200	-0.001	-0.007	-0.113	0.000
55	A	56	VAL	0	0.030	0.013	2.443	-1.654	-1.356	2.956	-0.653	-2.601	0.004
94	A	95	TYR	0	-0.044	-0.049	2.883	-1.253	0.612	1.091	-0.569	-2.386	-0.005
95	A	96	ASN	0	0.051	0.021	4.727	-5.018	-4.903	-0.001	-0.012	-0.102	0.000
130	A	131	LEU	0	0.014	0.016	2.561	-0.913	0.031	1.372	-0.429	-1.886	0.001
132	A	133	GLN	0	-0.030	-0.025	2.615	-6.660	-3.313	6.428	-2.562	-7.213	-0.004
133	A	134	THR	0	0.017	0.024	5.097	1.182	1.299	-0.001	-0.019	-0.097	0.000
141	A	142	PHE	0	0.002	0.014	4.137	1.641	1.844	-0.001	-0.012	-0.190	0.000
143	A	144	PHE	0	-0.007	-0.002	2.575	-4.455	-2.456	3.111	-1.335	-3.776	-0.016
4	A	4	LYS	1	0.886	0.932	5.610	27.672	27.672	0.000	0.000	0.000	0.000
5	A	5	THR	0	0.036	0.008	8.904	0.607	0.607	0.000	0.000	0.000	0.000
6	A	6	ALA	0	-0.002	0.002	11.520	-0.082	-0.082	0.000	0.000	0.000	0.000
7	A	7	ASN	0	-0.018	0.015	14.408	-0.247	-0.247	0.000	0.000	0.000	0.000
8	A	8	GLY	0	0.018	0.014	14.239	0.552	0.552	0.000	0.000	0.000	0.000
9	A	9	THR	0	-0.045	-0.033	12.741	-0.959	-0.959	0.000	0.000	0.000	0.000
10	A	10	ALA	0	-0.006	-0.014	9.611	-0.580	-0.580	0.000	0.000	0.000	0.000
11	A	11	ILE	0	-0.040	0.007	6.057	1.738	1.738	0.000	0.000	0.000	0.000
12	A	12	PRO	0	0.016	0.011	6.191	-4.526	-4.526	0.000	0.000	0.000	0.000
15	A	15	GLY	0	-0.025	-0.002	5.286	3.481	3.481	0.000	0.000	0.000	0.000
16	A	16	GLY	0	0.011	-0.009	6.029	1.885	1.885	0.000	0.000	0.000	0.000
17	A	17	SER	0	-0.040	-0.027	8.718	0.167	0.167	0.000	0.000	0.000	0.000
18	A	18	ALA	0	0.000	0.007	10.133	0.336	0.336	0.000	0.000	0.000	0.000
19	A	19	ASN	0	-0.006	0.000	11.730	-0.171	-0.171	0.000	0.000	0.000	0.000
20	A	20	VAL	0	-0.007	-0.009	11.581	-0.425	-0.425	0.000	0.000	0.000	0.000
21	A	21	TYR	0	0.004	0.008	14.655	0.315	0.315	0.000	0.000	0.000	0.000
22	A	22	VAL	0	0.030	0.019	16.795	-0.040	-0.040	0.000	0.000	0.000	0.000
23	A	23	ASN	0	0.025	0.016	19.427	0.401	0.401	0.000	0.000	0.000	0.000
24	A	24	LEU	0	-0.020	-0.006	21.374	-0.260	-0.260	0.000	0.000	0.000	0.000
25	A	25	ALA	0	0.049	0.024	24.331	0.239	0.239	0.000	0.000	0.000	0.000
26	A	26	PRO	0	0.026	0.009	27.274	0.043	0.043	0.000	0.000	0.000	0.000
27	A	27	VAL	0	-0.017	-0.003	30.255	0.205	0.205	0.000	0.000	0.000	0.000
28	A	28	VAL	0	-0.036	-0.015	27.754	-0.156	-0.156	0.000	0.000	0.000	0.000
29	A	29	ASN	0	0.017	-0.012	31.225	0.233	0.233	0.000	0.000	0.000	0.000
30	A	30	VAL	0	0.072	0.029	32.305	-0.226	-0.226	0.000	0.000	0.000	0.000
31	A	31	GLY	0	-0.003	0.009	32.432	0.176	0.176	0.000	0.000	0.000	0.000
32	A	32	GLN	0	-0.010	0.018	30.610	-0.100	-0.100	0.000	0.000	0.000	0.000
33	A	33	ASN	0	0.009	0.000	25.088	-0.001	-0.001	0.000	0.000	0.000	0.000
34	A	34	LEU	0	0.009	0.013	23.252	0.014	0.014	0.000	0.000	0.000	0.000
35	A	35	VAL	0	-0.036	-0.025	19.731	-0.241	-0.241	0.000	0.000	0.000	0.000
36	A	36	VAL	0	0.002	0.004	16.959	0.024	0.024	0.000	0.000	0.000	0.000
37	A	37	ASP	-1	-0.765	-0.864	14.628	-15.865	-15.865	0.000	0.000	0.000	0.000
38	A	38	LEU	0	-0.013	-0.016	11.259	0.003	0.003	0.000	0.000	0.000	0.000
39	A	39	SER	0	-0.068	-0.044	10.563	-1.092	-1.092	0.000	0.000	0.000	0.000
40	A	40	THR	0	-0.015	-0.025	11.651	-0.626	-0.626	0.000	0.000	0.000	0.000
41	A	41	GLN	0	-0.056	-0.027	12.428	0.093	0.093	0.000	0.000	0.000	0.000
42	A	42	ILE	0	-0.002	0.011	6.379	-0.452	-0.452	0.000	0.000	0.000	0.000
43	A	43	PHE	0	-0.017	-0.003	7.096	0.181	0.181	0.000	0.000	0.000	0.000
48	A	49	PRO	0	-0.010	0.004	6.457	1.766	1.766	0.000	0.000	0.000	0.000
49	A	50	GLU	-1	-0.785	-0.865	8.081	-27.730	-27.730	0.000	0.000	0.000	0.000
50	A	51	THR	0	-0.075	-0.038	9.396	2.842	2.842	0.000	0.000	0.000	0.000
51	A	52	ILE	0	0.002	0.028	4.915	1.261	1.261	0.000	0.000	0.000	0.000
52	A	53	THR	0	-0.050	-0.025	7.441	-0.019	-0.019	0.000	0.000	0.000	0.000
56	A	57	THR	0	-0.056	-0.040	5.447	1.538	1.538	0.000	0.000	0.000	0.000
57	A	58	LEU	0	0.005	0.014	7.264	-1.376	-1.376	0.000	0.000	0.000	0.000
58	A	59	GLN	0	0.048	0.025	9.676	0.381	0.381	0.000	0.000	0.000	0.000
59	A	60	ARG	1	0.969	0.973	11.491	16.753	16.753	0.000	0.000	0.000	0.000
60	A	61	GLY	0	0.043	0.023	12.645	-0.902	-0.902	0.000	0.000	0.000	0.000
61	A	62	SER	0	-0.035	-0.014	15.088	0.560	0.560	0.000	0.000	0.000	0.000
62	A	63	ALA	0	0.059	0.030	17.955	-0.319	-0.319	0.000	0.000	0.000	0.000
63	A	64	TYR	0	-0.008	-0.013	17.783	-0.010	-0.010	0.000	0.000	0.000	0.000
64	A	65	GLY	0	0.048	0.012	22.440	0.106	0.106	0.000	0.000	0.000	0.000
65	A	66	GLY	0	0.040	0.011	25.600	0.189	0.189	0.000	0.000	0.000	0.000
66	A	67	VAL	0	-0.007	-0.007	21.915	0.200	0.200	0.000	0.000	0.000	0.000
67	A	68	LEU	0	-0.061	-0.025	24.021	0.073	0.073	0.000	0.000	0.000	0.000
68	A	69	SER	0	-0.017	-0.013	25.723	0.109	0.109	0.000	0.000	0.000	0.000
69	A	70	ASN	0	-0.031	-0.011	28.798	0.405	0.405	0.000	0.000	0.000	0.000
70	A	71	PHE	0	-0.008	-0.004	25.881	0.104	0.104	0.000	0.000	0.000	0.000
71	A	72	SER	0	0.007	0.022	26.239	0.013	0.013	0.000	0.000	0.000	0.000
72	A	73	GLY	0	0.038	-0.002	23.443	0.003	0.003	0.000	0.000	0.000	0.000
73	A	74	THR	0	-0.059	-0.016	20.490	-0.066	-0.066	0.000	0.000	0.000	0.000
74	A	75	VAL	0	-0.007	0.004	14.217	-0.172	-0.172	0.000	0.000	0.000	0.000
75	A	76	LYS	1	0.927	0.973	16.231	12.572	12.572	0.000	0.000	0.000	0.000
76	A	77	TYR	0	0.037	-0.011	7.111	-0.693	-0.693	0.000	0.000	0.000	0.000
77	A	78	SER	0	0.003	-0.007	10.786	0.015	0.015	0.000	0.000	0.000	0.000
78	A	79	GLY	0	-0.034	-0.009	12.557	0.382	0.382	0.000	0.000	0.000	0.000
79	A	80	SER	0	0.004	0.014	15.631	0.956	0.956	0.000	0.000	0.000	0.000
80	A	81	SER	0	-0.030	-0.028	16.571	-0.351	-0.351	0.000	0.000	0.000	0.000
81	A	82	TYR	0	0.011	0.011	14.998	0.032	0.032	0.000	0.000	0.000	0.000
82	A	83	PRO	0	0.027	0.007	19.187	0.060	0.060	0.000	0.000	0.000	0.000
83	A	84	PHE	0	0.023	0.013	16.716	-0.679	-0.679	0.000	0.000	0.000	0.000
84	A	85	PRO	0	0.017	-0.005	19.591	0.371	0.371	0.000	0.000	0.000	0.000
85	A	86	THR	0	-0.018	0.011	15.074	0.055	0.055	0.000	0.000	0.000	0.000
86	A	87	THR	0	-0.002	-0.011	18.522	-0.132	-0.132	0.000	0.000	0.000	0.000
87	A	88	SER	0	-0.053	-0.021	18.237	0.173	0.173	0.000	0.000	0.000	0.000
88	A	89	GLU	-1	-0.787	-0.850	11.500	-20.345	-20.345	0.000	0.000	0.000	0.000
89	A	90	THR	0	-0.022	-0.008	11.027	0.353	0.353	0.000	0.000	0.000	0.000
90	A	91	PRO	0	0.008	-0.006	12.581	-0.743	-0.743	0.000	0.000	0.000	0.000
91	A	92	ARG	1	0.933	0.980	9.378	22.442	22.442	0.000	0.000	0.000	0.000
92	A	93	VAL	0	-0.006	0.007	6.655	1.081	1.081	0.000	0.000	0.000	0.000
93	A	94	VAL	0	0.028	0.015	6.322	-2.265	-2.265	0.000	0.000	0.000	0.000
96	A	97	SER	0	0.055	0.022	6.394	2.682	2.682	0.000	0.000	0.000	0.000
97	A	98	ARG	1	0.838	0.884	6.273	29.539	29.539	0.000	0.000	0.000	0.000
98	A	99	THR	0	-0.039	-0.012	7.719	1.072	1.072	0.000	0.000	0.000	0.000
99	A	100	ASP	-1	-0.843	-0.894	7.333	-33.633	-33.633	0.000	0.000	0.000	0.000
100	A	101	LYS	1	0.865	0.933	5.749	30.055	30.055	0.000	0.000	0.000	0.000
101	A	102	PRO	0	0.047	0.021	6.433	-1.932	-1.932	0.000	0.000	0.000	0.000
102	A	103	TRP	0	0.049	0.031	5.005	-1.099	-1.099	0.000	0.000	0.000	0.000
103	A	104	PRO	0	-0.045	-0.008	6.619	1.534	1.534	0.000	0.000	0.000	0.000
104	A	105	VAL	0	0.010	-0.007	9.726	0.915	0.915	0.000	0.000	0.000	0.000
105	A	106	ALA	0	0.038	0.021	11.428	0.087	0.087	0.000	0.000	0.000	0.000
106	A	107	LEU	0	-0.009	0.001	15.022	0.146	0.146	0.000	0.000	0.000	0.000
107	A	108	TYR	0	-0.026	-0.019	17.877	0.110	0.110	0.000	0.000	0.000	0.000
108	A	109	LEU	0	0.002	0.009	20.908	0.151	0.151	0.000	0.000	0.000	0.000
109	A	110	THR	0	-0.008	-0.019	23.824	0.197	0.197	0.000	0.000	0.000	0.000
110	A	111	PRO	0	0.003	0.006	27.668	-0.092	-0.092	0.000	0.000	0.000	0.000
111	A	112	VAL	0	-0.007	-0.001	30.164	0.134	0.134	0.000	0.000	0.000	0.000
112	A	113	SER	0	0.011	-0.020	32.372	0.035	0.035	0.000	0.000	0.000	0.000
113	A	114	SER	0	-0.010	0.003	35.734	0.142	0.142	0.000	0.000	0.000	0.000
114	A	115	ALA	0	-0.041	-0.008	32.794	0.019	0.019	0.000	0.000	0.000	0.000
115	A	116	GLY	0	0.054	0.011	34.793	0.124	0.124	0.000	0.000	0.000	0.000
116	A	117	GLY	0	-0.001	0.014	36.274	-0.017	-0.017	0.000	0.000	0.000	0.000
117	A	118	VAL	0	-0.033	-0.025	31.915	-0.163	-0.163	0.000	0.000	0.000	0.000
118	A	119	ALA	0	0.005	0.029	30.695	-0.048	-0.048	0.000	0.000	0.000	0.000
119	A	120	ILE	0	-0.006	-0.009	24.518	-0.272	-0.272	0.000	0.000	0.000	0.000
120	A	121	LYS	1	0.972	0.998	27.662	9.111	9.111	0.000	0.000	0.000	0.000
121	A	122	ALA	0	0.050	0.034	26.634	-0.419	-0.419	0.000	0.000	0.000	0.000
122	A	123	GLY	0	-0.004	0.001	24.479	0.168	0.168	0.000	0.000	0.000	0.000
123	A	124	SER	0	-0.093	-0.056	24.106	-0.229	-0.229	0.000	0.000	0.000	0.000
124	A	125	LEU	0	-0.008	0.001	17.450	-0.242	-0.242	0.000	0.000	0.000	0.000
125	A	126	ILE	0	-0.014	-0.010	19.196	0.410	0.410	0.000	0.000	0.000	0.000
126	A	127	ALA	0	0.008	-0.009	16.638	0.201	0.201	0.000	0.000	0.000	0.000
127	A	128	VAL	0	-0.011	0.012	13.310	-0.290	-0.290	0.000	0.000	0.000	0.000
128	A	129	LEU	0	-0.038	-0.010	11.073	0.432	0.432	0.000	0.000	0.000	0.000
129	A	130	ILE	0	-0.012	-0.010	8.843	-0.995	-0.995	0.000	0.000	0.000	0.000
131	A	132	ARG	1	0.752	0.824	5.886	21.255	21.255	0.000	0.000	0.000	0.000
134	A	135	ASN	0	0.029	-0.005	5.143	1.872	1.872	0.000	0.000	0.000	0.000
135	A	136	ASN	0	0.000	-0.002	7.111	0.646	0.646	0.000	0.000	0.000	0.000
136	A	137	TYR	0	-0.005	0.006	8.238	2.228	2.228	0.000	0.000	0.000	0.000
137	A	138	ASN	0	0.004	-0.010	7.417	1.194	1.194	0.000	0.000	0.000	0.000
138	A	139	SER	0	-0.012	-0.008	10.888	0.590	0.590	0.000	0.000	0.000	0.000
139	A	140	ASP	-1	-0.881	-0.919	6.019	-42.203	-42.203	0.000	0.000	0.000	0.000
140	A	141	ASP	-1	-0.825	-0.890	8.140	-24.555	-24.555	0.000	0.000	0.000	0.000
142	A	143	GLN	0	-0.040	-0.033	5.971	-0.071	-0.071	0.000	0.000	0.000	0.000
144	A	145	VAL	0	-0.030	-0.019	5.742	1.460	1.460	0.000	0.000	0.000	0.000
145	A	146	TRP	0	0.066	0.012	4.848	0.560	0.560	0.000	0.000	0.000	0.000
146	A	147	ASN	0	-0.002	-0.008	10.505	0.877	0.877	0.000	0.000	0.000	0.000
147	A	148	ILE	0	0.018	0.002	12.558	-0.036	-0.036	0.000	0.000	0.000	0.000
148	A	149	TYR	0	-0.003	-0.012	16.127	0.502	0.502	0.000	0.000	0.000	0.000
149	A	150	ALA	0	0.017	0.022	19.505	-0.212	-0.212	0.000	0.000	0.000	0.000
150	A	151	ASN	0	-0.013	-0.033	21.090	0.119	0.119	0.000	0.000	0.000	0.000
151	A	152	ASN	0	-0.067	-0.044	24.277	0.012	0.012	0.000	0.000	0.000	0.000
152	A	153	ASP	-1	-0.818	-0.907	26.999	-9.112	-9.112	0.000	0.000	0.000	0.000
153	A	154	VAL	0	-0.047	-0.020	26.496	-0.079	-0.079	0.000	0.000	0.000	0.000
154	A	155	VAL	0	-0.019	-0.019	29.744	0.092	0.092	0.000	0.000	0.000	0.000
155	A	156	VAL	0	0.004	0.006	31.873	-0.116	-0.116	0.000	0.000	0.000	0.000
156	A	157	PRO	0	-0.063	-0.043	34.237	0.130	0.130	0.000	0.000	0.000	0.000
157	A	158	THR	-1	-0.918	-0.932	37.818	-6.803	-6.803	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:1:PHE)