FMO DATABASE

FMODB ID: VVG81

Calculation Name: 1QAH-A-Xray547

Preferred Name:

Target Type:

Ligand Name:

Ligand 3-letter code:

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 1QAH

Chain ID: A

ChEMBL ID:

UniProt ID: P52759

Base Structure: X-ray

Registration Date: 2025-10-03

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	OptAll
Protonation	MOE:Protonate 3D
Complement	MOE:Homology Modeling
Water	No
Procedure	Manual calculation
Remarks	ac.sh, 23 2024 Oct; Missing atoms/residues were imported from a 100% homology model, which was constructed by MOE.

FMO calculation

FMO method	FMO2-MP2/6-31G(d)
Fragmentation	Auto
Number of fragment	132
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230922

Total energy (hartree)

FMO2-HF: Electronic energy	-1039504.416013
FMO2-HF: Nuclear repulsion	991603.980349
FMO2-HF: Total energy	-47900.435664
FMO2-MP2: Total energy	-48042.067171

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:SER)

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

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.
-6.445	-4.462	0.031	-0.912	-1.103	-0.004

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

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 1 / q_Mulliken : 0.851 / q_NPA : 0.918

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	ILE	0	0.004	0.017	3.338	-10.511	-8.577	0.032	-0.906	-1.061	-0.004
4	A	4	ILE	0	0.054	0.027	4.917	5.000	5.049	-0.001	-0.006	-0.042	0.000
5	A	5	ARG	1	0.966	0.978	8.460	23.037	23.037	0.000	0.000	0.000	0.000
6	A	6	LYS	1	0.915	0.970	11.321	17.637	17.637	0.000	0.000	0.000	0.000
7	A	7	VAL	0	0.014	0.013	14.848	0.302	0.302	0.000	0.000	0.000	0.000
8	A	8	ILE	0	-0.052	-0.020	17.335	0.036	0.036	0.000	0.000	0.000	0.000
9	A	9	SER	0	-0.007	-0.016	20.442	0.605	0.605	0.000	0.000	0.000	0.000
10	A	10	THR	0	0.020	0.002	23.986	-0.055	-0.055	0.000	0.000	0.000	0.000
11	A	11	SER	0	0.025	0.022	26.912	0.077	0.077	0.000	0.000	0.000	0.000
12	A	12	LYS	1	0.906	0.959	29.536	10.450	10.450	0.000	0.000	0.000	0.000
13	A	13	ALA	0	0.017	0.018	28.715	0.196	0.196	0.000	0.000	0.000	0.000
14	A	14	PRO	0	-0.014	0.007	30.832	-0.053	-0.053	0.000	0.000	0.000	0.000
15	A	15	ALA	0	0.027	0.021	30.405	-0.410	-0.410	0.000	0.000	0.000	0.000
16	A	16	ALA	0	-0.007	0.007	27.967	0.141	0.141	0.000	0.000	0.000	0.000
17	A	17	ILE	0	-0.018	-0.017	30.113	0.226	0.226	0.000	0.000	0.000	0.000
18	A	18	GLY	0	0.016	-0.004	31.148	0.292	0.292	0.000	0.000	0.000	0.000
19	A	19	ALA	0	-0.025	-0.006	27.540	-0.242	-0.242	0.000	0.000	0.000	0.000
20	A	20	TYR	0	-0.002	0.004	24.959	-0.196	-0.196	0.000	0.000	0.000	0.000
21	A	21	SER	0	0.030	0.016	20.665	0.358	0.358	0.000	0.000	0.000	0.000
22	A	22	GLN	0	0.002	0.003	23.565	-0.307	-0.307	0.000	0.000	0.000	0.000
23	A	23	ALA	0	0.060	0.023	20.416	0.173	0.173	0.000	0.000	0.000	0.000
24	A	24	VAL	0	-0.050	-0.028	15.205	-0.170	-0.170	0.000	0.000	0.000	0.000
25	A	25	LEU	0	0.000	0.025	12.456	0.388	0.388	0.000	0.000	0.000	0.000
26	A	26	VAL	0	-0.030	-0.041	10.002	-0.806	-0.806	0.000	0.000	0.000	0.000
27	A	27	ASP	-1	-0.919	-0.959	7.113	-37.417	-37.417	0.000	0.000	0.000	0.000
28	A	28	ARG	1	0.875	0.933	8.677	24.770	24.770	0.000	0.000	0.000	0.000
29	A	29	THR	0	-0.006	0.012	11.711	2.454	2.454	0.000	0.000	0.000	0.000
30	A	30	ILE	0	-0.026	-0.020	14.094	-0.641	-0.641	0.000	0.000	0.000	0.000
31	A	31	TYR	0	0.020	0.009	14.680	0.363	0.363	0.000	0.000	0.000	0.000
32	A	32	VAL	0	-0.026	-0.028	19.311	-0.124	-0.124	0.000	0.000	0.000	0.000
33	A	33	SER	0	-0.001	-0.014	22.754	0.164	0.164	0.000	0.000	0.000	0.000
34	A	34	GLY	0	0.034	0.024	25.304	0.126	0.126	0.000	0.000	0.000	0.000
35	A	35	GLN	0	-0.087	-0.052	27.181	0.454	0.454	0.000	0.000	0.000	0.000
36	A	36	ILE	0	0.053	0.031	30.679	0.217	0.217	0.000	0.000	0.000	0.000
37	A	37	GLY	0	0.019	0.009	34.261	-0.129	-0.129	0.000	0.000	0.000	0.000
38	A	38	MET	0	-0.069	-0.035	32.962	0.280	0.280	0.000	0.000	0.000	0.000
39	A	39	ASP	-1	-0.734	-0.861	35.790	-8.414	-8.414	0.000	0.000	0.000	0.000
40	A	40	PRO	0	-0.058	-0.039	33.648	-0.046	-0.046	0.000	0.000	0.000	0.000
41	A	41	SER	0	-0.019	0.004	35.208	-0.160	-0.160	0.000	0.000	0.000	0.000
42	A	42	SER	0	-0.064	-0.059	37.896	0.077	0.077	0.000	0.000	0.000	0.000
43	A	43	GLY	0	-0.016	0.000	36.463	0.049	0.049	0.000	0.000	0.000	0.000
44	A	44	GLN	0	-0.032	-0.019	37.371	0.084	0.084	0.000	0.000	0.000	0.000
45	A	45	LEU	0	-0.027	-0.006	38.296	-0.141	-0.141	0.000	0.000	0.000	0.000
46	A	46	VAL	0	0.002	0.007	39.743	0.181	0.181	0.000	0.000	0.000	0.000
47	A	47	PRO	0	0.002	0.001	42.184	0.031	0.031	0.000	0.000	0.000	0.000
48	A	48	GLY	0	0.024	0.001	45.341	-0.033	-0.033	0.000	0.000	0.000	0.000
49	A	49	GLY	0	0.002	0.018	44.270	0.061	0.061	0.000	0.000	0.000	0.000
50	A	50	VAL	0	0.042	0.005	40.668	-0.129	-0.129	0.000	0.000	0.000	0.000
51	A	51	ALA	0	0.035	0.024	40.826	-0.199	-0.199	0.000	0.000	0.000	0.000
52	A	52	GLU	-1	-0.836	-0.902	41.506	-7.503	-7.503	0.000	0.000	0.000	0.000
53	A	53	GLU	-1	-0.812	-0.915	38.700	-8.088	-8.088	0.000	0.000	0.000	0.000
54	A	54	ALA	0	0.028	0.011	36.601	-0.288	-0.288	0.000	0.000	0.000	0.000
55	A	55	LYS	1	0.856	0.905	35.789	7.286	7.286	0.000	0.000	0.000	0.000
56	A	56	GLN	0	-0.061	-0.028	34.993	0.004	0.004	0.000	0.000	0.000	0.000
57	A	57	ALA	0	0.010	0.009	32.914	-0.277	-0.277	0.000	0.000	0.000	0.000
58	A	58	LEU	0	0.010	0.003	31.218	-0.434	-0.434	0.000	0.000	0.000	0.000
59	A	59	LYS	1	0.944	0.969	31.108	8.072	8.072	0.000	0.000	0.000	0.000
60	A	60	ASN	0	0.006	0.005	30.614	-0.188	-0.188	0.000	0.000	0.000	0.000
61	A	61	LEU	0	0.018	0.010	25.323	-0.405	-0.405	0.000	0.000	0.000	0.000
62	A	62	GLY	0	0.048	0.024	26.331	-0.486	-0.486	0.000	0.000	0.000	0.000
63	A	63	GLU	-1	-0.854	-0.942	26.787	-10.912	-10.912	0.000	0.000	0.000	0.000
64	A	64	ILE	0	-0.024	-0.011	23.217	-0.425	-0.425	0.000	0.000	0.000	0.000
65	A	65	LEU	0	-0.024	-0.015	21.618	-0.723	-0.723	0.000	0.000	0.000	0.000
66	A	66	LYS	1	0.902	0.962	21.961	10.099	10.099	0.000	0.000	0.000	0.000
67	A	67	ALA	0	-0.039	-0.017	22.943	-0.349	-0.349	0.000	0.000	0.000	0.000
68	A	68	ALA	0	-0.059	-0.037	18.272	-0.693	-0.693	0.000	0.000	0.000	0.000
69	A	69	GLY	0	-0.018	0.007	18.097	-1.047	-1.047	0.000	0.000	0.000	0.000
70	A	70	CYS	0	-0.088	-0.041	19.115	-0.719	-0.719	0.000	0.000	0.000	0.000
71	A	71	ASP	-1	-0.795	-0.876	21.646	-11.631	-11.631	0.000	0.000	0.000	0.000
72	A	72	PHE	0	0.009	-0.012	24.220	-0.391	-0.391	0.000	0.000	0.000	0.000
73	A	73	THR	0	-0.048	-0.039	25.304	-0.122	-0.122	0.000	0.000	0.000	0.000
74	A	74	ASN	0	0.005	-0.002	19.549	0.146	0.146	0.000	0.000	0.000	0.000
75	A	75	VAL	0	-0.040	-0.014	20.928	-0.718	-0.718	0.000	0.000	0.000	0.000
76	A	76	VAL	0	0.042	0.022	19.472	0.368	0.368	0.000	0.000	0.000	0.000
77	A	77	LYS	1	0.884	0.945	22.701	12.413	12.413	0.000	0.000	0.000	0.000
78	A	78	THR	0	-0.004	0.012	24.534	0.001	0.001	0.000	0.000	0.000	0.000
79	A	79	THR	0	-0.027	-0.017	27.312	0.063	0.063	0.000	0.000	0.000	0.000
80	A	80	VAL	0	-0.029	-0.012	29.578	-0.019	-0.019	0.000	0.000	0.000	0.000
81	A	81	LEU	0	0.030	0.023	31.156	0.226	0.226	0.000	0.000	0.000	0.000
82	A	82	LEU	0	0.019	0.001	34.855	0.068	0.068	0.000	0.000	0.000	0.000
83	A	83	ALA	0	0.036	0.016	38.622	0.014	0.014	0.000	0.000	0.000	0.000
84	A	84	ASP	-1	-0.870	-0.935	41.640	-6.700	-6.700	0.000	0.000	0.000	0.000
85	A	85	ILE	0	0.014	0.009	40.785	-0.174	-0.174	0.000	0.000	0.000	0.000
86	A	86	ASN	0	-0.060	-0.048	43.086	-0.041	-0.041	0.000	0.000	0.000	0.000
87	A	87	ASP	-1	-0.861	-0.930	42.418	-7.201	-7.201	0.000	0.000	0.000	0.000
88	A	88	PHE	0	-0.033	-0.024	36.599	-0.156	-0.156	0.000	0.000	0.000	0.000
89	A	89	GLY	0	0.031	0.016	40.471	-0.143	-0.143	0.000	0.000	0.000	0.000
90	A	90	THR	0	0.019	-0.003	42.300	-0.056	-0.056	0.000	0.000	0.000	0.000
91	A	91	VAL	0	0.012	0.006	37.006	-0.104	-0.104	0.000	0.000	0.000	0.000
92	A	92	ASN	0	-0.024	0.002	37.695	-0.480	-0.480	0.000	0.000	0.000	0.000
93	A	93	GLU	-1	-0.798	-0.879	38.331	-7.779	-7.779	0.000	0.000	0.000	0.000
94	A	94	ILE	0	-0.002	0.013	37.319	-0.050	-0.050	0.000	0.000	0.000	0.000
95	A	95	TYR	0	0.011	-0.007	29.991	-0.107	-0.107	0.000	0.000	0.000	0.000
96	A	96	LYS	1	0.846	0.889	34.459	7.529	7.529	0.000	0.000	0.000	0.000
97	A	97	THR	0	-0.077	-0.038	35.896	-0.083	-0.083	0.000	0.000	0.000	0.000
98	A	98	TYR	0	-0.032	-0.007	31.778	0.046	0.046	0.000	0.000	0.000	0.000
99	A	99	PHE	0	-0.039	-0.031	27.313	-0.346	-0.346	0.000	0.000	0.000	0.000
100	A	100	GLN	0	-0.011	-0.003	31.792	0.457	0.457	0.000	0.000	0.000	0.000
101	A	101	GLY	0	0.035	0.004	31.110	-0.036	-0.036	0.000	0.000	0.000	0.000
102	A	102	ASN	0	-0.027	-0.009	25.869	0.481	0.481	0.000	0.000	0.000	0.000
103	A	103	LEU	0	-0.016	0.001	28.041	-0.197	-0.197	0.000	0.000	0.000	0.000
104	A	104	PRO	0	-0.002	0.011	26.118	-0.240	-0.240	0.000	0.000	0.000	0.000
105	A	105	ALA	0	0.018	0.018	25.839	0.444	0.444	0.000	0.000	0.000	0.000
106	A	106	ARG	1	0.869	0.918	27.679	9.015	9.015	0.000	0.000	0.000	0.000
107	A	107	ALA	0	-0.016	0.005	30.099	0.159	0.159	0.000	0.000	0.000	0.000
108	A	108	ALA	0	-0.003	-0.012	31.569	-0.085	-0.085	0.000	0.000	0.000	0.000
109	A	109	TYR	0	0.011	0.009	31.779	0.071	0.071	0.000	0.000	0.000	0.000
110	A	110	GLN	0	0.000	0.016	37.242	-0.052	-0.052	0.000	0.000	0.000	0.000
111	A	111	VAL	0	-0.005	-0.007	35.610	-0.070	-0.070	0.000	0.000	0.000	0.000
112	A	112	ALA	0	-0.013	-0.013	39.039	0.152	0.152	0.000	0.000	0.000	0.000
113	A	113	ALA	0	-0.008	-0.007	39.941	0.201	0.201	0.000	0.000	0.000	0.000
114	A	114	LEU	0	0.010	0.022	35.393	-0.230	-0.230	0.000	0.000	0.000	0.000
115	A	115	PRO	0	0.051	0.025	33.748	0.275	0.275	0.000	0.000	0.000	0.000
116	A	116	LYS	1	0.904	0.950	37.020	8.331	8.331	0.000	0.000	0.000	0.000
117	A	117	GLY	0	0.014	0.025	39.851	0.184	0.184	0.000	0.000	0.000	0.000
118	A	118	SER	0	-0.040	-0.030	38.065	0.135	0.135	0.000	0.000	0.000	0.000
119	A	119	ARG	1	0.898	0.943	40.121	7.303	7.303	0.000	0.000	0.000	0.000
120	A	120	ILE	0	-0.025	-0.021	35.476	-0.010	-0.010	0.000	0.000	0.000	0.000
121	A	121	GLU	-1	-0.872	-0.942	31.063	-10.009	-10.009	0.000	0.000	0.000	0.000
122	A	122	ILE	0	-0.037	-0.021	29.339	0.029	0.029	0.000	0.000	0.000	0.000
123	A	123	GLU	-1	-0.867	-0.920	25.912	-11.878	-11.878	0.000	0.000	0.000	0.000
124	A	124	ALA	0	-0.026	-0.028	24.691	0.250	0.250	0.000	0.000	0.000	0.000
125	A	125	ILE	0	-0.009	0.001	18.825	-0.483	-0.483	0.000	0.000	0.000	0.000
126	A	126	ALA	0	0.006	0.008	19.418	0.587	0.587	0.000	0.000	0.000	0.000
127	A	127	VAL	0	-0.005	0.001	14.514	-1.067	-1.067	0.000	0.000	0.000	0.000
128	A	128	GLN	0	0.033	-0.005	13.630	-0.425	-0.425	0.000	0.000	0.000	0.000
129	A	129	GLY	0	0.004	0.001	15.426	-1.278	-1.278	0.000	0.000	0.000	0.000
130	A	130	PRO	0	-0.008	0.023	15.809	0.834	0.834	0.000	0.000	0.000	0.000
131	A	131	PHE	0	-0.027	-0.024	17.125	-1.382	-1.382	0.000	0.000	0.000	0.000
132	A	132	THR	-1	-0.915	-0.946	19.605	-13.454	-13.454	0.000	0.000	0.000	0.000

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