FMO DATABASE

FMODB ID: K34V3

Calculation Name: 3SUM-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 3SUM

Chain ID: A

ChEMBL ID:

UniProt ID: B2C3I4

Base Structure: X-ray

Registration Date: 2023-06-20

Reference: C. Watanabe, N. Tani, K. Kamisaka, T. Honma et al., Interaction energy analysis of Apo structure dataset on FMODB, To be published.

DOI:

IFIE MAP

IFIE Diagram

Modeling method

Optimization	MOE:Amber10:EHT
Restraint	OptAll
Protonation	MOE:Protonate 3D
Complement	MOE:Structure Preparation
Water	No
Procedure	Auto-FMO protocol ver. 2.20220422

FMO calculation

FMO method	FMO2-MP2/6-31G(d)
Fragmentation	Auto
Number of fragment	132
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-1179517.334874
FMO2-HF: Nuclear repulsion	1126816.84048
FMO2-HF: Total energy	-52700.494395
FMO2-MP2: Total energy	-52852.471688

3D Structure

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:22:ASN)

Summations of interaction energy for fragment #1(A:22:ASN)

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.
0.426	3.52	0.042	-0.881	-2.253	0.003

Interaction energy analysis for fragmet #1(A:22:ASN)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : -0.041 / q_NPA : -0.033

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	24	LEU	0	-0.002	0.003	3.364	0.935	3.055	0.041	-0.761	-1.399	0.003
4	A	25	ILE	0	-0.005	-0.002	5.466	-1.092	-1.100	-0.001	-0.002	0.011	0.000
5	A	26	LYS	1	0.926	0.951	9.154	-0.838	-0.838	0.000	0.000	0.000	0.000
6	A	27	TRP	0	-0.022	-0.020	12.208	-0.042	-0.042	0.000	0.000	0.000	0.000
7	A	28	ASP	-1	-0.831	-0.924	15.908	0.319	0.319	0.000	0.000	0.000	0.000
8	A	29	ASP	-1	-0.840	-0.921	19.023	0.361	0.361	0.000	0.000	0.000	0.000
9	A	30	LYS	1	0.836	0.910	21.424	-0.226	-0.226	0.000	0.000	0.000	0.000
10	A	31	PHE	0	-0.022	-0.035	17.900	-0.026	-0.026	0.000	0.000	0.000	0.000
11	A	32	GLN	0	-0.009	-0.019	21.628	0.068	0.068	0.000	0.000	0.000	0.000
12	A	33	ASN	0	-0.027	0.001	24.074	-0.039	-0.039	0.000	0.000	0.000	0.000
13	A	34	ASP	-1	-0.870	-0.949	26.955	0.221	0.221	0.000	0.000	0.000	0.000
14	A	35	THR	0	-0.036	-0.019	29.550	-0.022	-0.022	0.000	0.000	0.000	0.000
15	A	36	LEU	0	-0.024	0.000	26.029	-0.024	-0.024	0.000	0.000	0.000	0.000
16	A	37	SER	0	0.011	-0.008	29.946	0.009	0.009	0.000	0.000	0.000	0.000
17	A	38	ILE	0	0.020	-0.001	28.451	0.006	0.006	0.000	0.000	0.000	0.000
18	A	39	SER	0	-0.057	-0.050	28.250	-0.001	-0.001	0.000	0.000	0.000	0.000
19	A	40	GLU	-1	-0.909	-0.912	27.378	0.096	0.096	0.000	0.000	0.000	0.000
20	A	41	PHE	0	-0.016	-0.001	22.543	0.014	0.014	0.000	0.000	0.000	0.000
21	A	42	LYS	1	0.793	0.869	19.250	-0.043	-0.043	0.000	0.000	0.000	0.000
22	A	43	CYS	0	-0.029	0.024	17.658	0.044	0.044	0.000	0.000	0.000	0.000
23	A	44	SER	0	0.047	0.033	23.600	0.008	0.008	0.000	0.000	0.000	0.000
24	A	45	ALA	0	0.007	-0.006	27.284	0.007	0.007	0.000	0.000	0.000	0.000
25	A	46	ALA	0	-0.044	-0.026	24.145	-0.005	-0.005	0.000	0.000	0.000	0.000
26	A	47	LEU	0	0.027	0.013	23.730	0.010	0.010	0.000	0.000	0.000	0.000
27	A	48	ALA	0	0.011	-0.002	27.206	0.004	0.004	0.000	0.000	0.000	0.000
28	A	49	LYS	1	0.897	0.952	28.513	-0.109	-0.109	0.000	0.000	0.000	0.000
29	A	50	LEU	0	-0.005	0.005	24.241	0.006	0.006	0.000	0.000	0.000	0.000
30	A	51	GLY	0	0.089	0.059	28.486	0.021	0.021	0.000	0.000	0.000	0.000
31	A	52	PRO	0	-0.025	-0.023	31.456	-0.001	-0.001	0.000	0.000	0.000	0.000
32	A	53	ASP	-1	-0.819	-0.901	33.354	0.116	0.116	0.000	0.000	0.000	0.000
33	A	54	PRO	0	-0.022	-0.016	31.677	-0.005	-0.005	0.000	0.000	0.000	0.000
34	A	55	LYS	1	0.888	0.946	33.482	-0.109	-0.109	0.000	0.000	0.000	0.000
35	A	56	HIS	0	-0.109	-0.060	36.180	-0.016	-0.016	0.000	0.000	0.000	0.000
36	A	57	PRO	0	-0.029	-0.007	33.598	0.009	0.009	0.000	0.000	0.000	0.000
37	A	58	PRO	0	-0.010	0.028	30.458	-0.005	-0.005	0.000	0.000	0.000	0.000
38	A	59	THR	0	-0.057	-0.056	32.633	-0.007	-0.007	0.000	0.000	0.000	0.000
39	A	60	LYS	1	0.882	0.932	31.325	-0.160	-0.160	0.000	0.000	0.000	0.000
40	A	61	LEU	0	-0.004	0.010	23.915	0.007	0.007	0.000	0.000	0.000	0.000
41	A	62	GLY	0	0.024	-0.001	27.788	0.018	0.018	0.000	0.000	0.000	0.000
42	A	63	GLU	-1	-0.888	-0.912	29.781	0.164	0.164	0.000	0.000	0.000	0.000
43	A	64	VAL	0	-0.048	-0.020	25.695	-0.010	-0.010	0.000	0.000	0.000	0.000
44	A	65	LEU	0	-0.021	-0.021	27.125	0.022	0.022	0.000	0.000	0.000	0.000
45	A	66	ASN	0	-0.031	-0.027	20.623	-0.005	-0.005	0.000	0.000	0.000	0.000
46	A	67	PHE	0	0.021	0.052	23.238	0.050	0.050	0.000	0.000	0.000	0.000
47	A	68	PRO	0	-0.005	-0.007	23.267	-0.011	-0.011	0.000	0.000	0.000	0.000
48	A	69	HIS	0	0.003	-0.008	19.490	0.067	0.067	0.000	0.000	0.000	0.000
49	A	70	PHE	0	-0.036	-0.025	19.168	0.004	0.004	0.000	0.000	0.000	0.000
50	A	71	VAL	0	0.013	-0.017	13.769	0.077	0.077	0.000	0.000	0.000	0.000
51	A	72	ALA	0	0.008	0.023	15.813	-0.087	-0.087	0.000	0.000	0.000	0.000
52	A	73	ALA	0	0.002	-0.017	12.272	0.159	0.159	0.000	0.000	0.000	0.000
53	A	74	PRO	0	0.029	0.026	10.534	-0.063	-0.063	0.000	0.000	0.000	0.000
54	A	75	GLU	-1	-0.821	-0.894	13.592	0.002	0.002	0.000	0.000	0.000	0.000
55	A	76	ALA	0	-0.003	0.015	14.431	-0.110	-0.110	0.000	0.000	0.000	0.000
56	A	77	GLN	0	-0.070	-0.045	7.130	0.083	0.083	0.000	0.000	0.000	0.000
57	A	78	THR	0	-0.020	-0.030	11.432	0.190	0.190	0.000	0.000	0.000	0.000
58	A	79	GLU	-1	-0.849	-0.923	13.839	-0.070	-0.070	0.000	0.000	0.000	0.000
59	A	81	GLY	0	0.039	0.014	20.378	-0.021	-0.021	0.000	0.000	0.000	0.000
60	A	82	SER	0	-0.046	-0.029	16.673	0.043	0.043	0.000	0.000	0.000	0.000
61	A	83	CYS	0	-0.042	0.011	17.902	0.115	0.115	0.000	0.000	0.000	0.000
62	A	84	TRP	0	0.013	-0.003	9.167	0.028	0.028	0.000	0.000	0.000	0.000
63	A	85	LYS	1	0.834	0.936	13.684	-0.898	-0.898	0.000	0.000	0.000	0.000
64	A	86	LEU	0	0.006	0.004	9.891	0.241	0.241	0.000	0.000	0.000	0.000
65	A	87	ARG	1	0.917	0.957	9.521	-1.537	-1.537	0.000	0.000	0.000	0.000
66	A	88	TYR	0	-0.020	-0.037	8.901	0.667	0.667	0.000	0.000	0.000	0.000
67	A	89	LYS	1	0.807	0.898	10.468	-1.577	-1.577	0.000	0.000	0.000	0.000
68	A	90	GLY	0	0.003	0.009	12.477	-0.001	-0.001	0.000	0.000	0.000	0.000
69	A	91	ASN	0	-0.063	-0.029	14.435	-0.177	-0.177	0.000	0.000	0.000	0.000
70	A	92	HIS	0	0.007	-0.024	13.717	0.241	0.241	0.000	0.000	0.000	0.000
71	A	93	ALA	0	-0.009	0.006	14.598	-0.127	-0.127	0.000	0.000	0.000	0.000
72	A	94	PHE	0	0.035	0.008	15.201	0.109	0.109	0.000	0.000	0.000	0.000
73	A	95	VAL	0	0.013	0.004	14.200	-0.046	-0.046	0.000	0.000	0.000	0.000
74	A	96	THR	0	0.015	0.002	17.159	0.006	0.006	0.000	0.000	0.000	0.000
75	A	97	VAL	0	-0.023	-0.001	15.068	0.036	0.036	0.000	0.000	0.000	0.000
76	A	98	VAL	0	0.021	0.002	17.838	-0.068	-0.068	0.000	0.000	0.000	0.000
77	A	99	ASP	-1	-0.749	-0.878	18.970	0.145	0.145	0.000	0.000	0.000	0.000
78	A	100	ARG	1	0.767	0.865	16.163	-0.040	-0.040	0.000	0.000	0.000	0.000
79	A	101	VAL	0	-0.001	0.007	12.970	0.019	0.019	0.000	0.000	0.000	0.000
80	A	102	GLU	-1	-0.793	-0.901	14.652	-0.076	-0.076	0.000	0.000	0.000	0.000
81	A	103	GLU	-1	-0.949	-0.962	9.506	-0.393	-0.393	0.000	0.000	0.000	0.000
82	A	104	ALA	0	0.024	0.002	8.617	0.171	0.171	0.000	0.000	0.000	0.000
83	A	105	ASN	0	-0.049	-0.027	4.909	-0.493	-0.241	-0.001	-0.031	-0.219	0.000
84	A	106	LEU	0	-0.010	0.009	6.332	1.135	1.135	0.000	0.000	0.000	0.000
85	A	107	PHE	0	0.032	0.004	8.180	-0.272	-0.272	0.000	0.000	0.000	0.000
86	A	108	VAL	0	-0.015	-0.015	10.917	0.151	0.151	0.000	0.000	0.000	0.000
87	A	109	GLY	0	0.056	0.028	13.764	-0.087	-0.087	0.000	0.000	0.000	0.000
88	A	110	GLY	0	0.035	0.033	16.258	-0.013	-0.013	0.000	0.000	0.000	0.000
89	A	111	THR	0	-0.002	-0.009	18.531	0.093	0.093	0.000	0.000	0.000	0.000
90	A	112	ASP	-1	-0.781	-0.888	19.336	0.561	0.561	0.000	0.000	0.000	0.000
91	A	113	LEU	0	-0.019	0.023	16.010	0.034	0.034	0.000	0.000	0.000	0.000
92	A	114	VAL	0	0.001	-0.006	13.426	0.092	0.092	0.000	0.000	0.000	0.000
93	A	115	LYS	1	0.857	0.950	15.735	-0.429	-0.429	0.000	0.000	0.000	0.000
94	A	116	ASN	0	-0.065	-0.028	18.188	0.004	0.004	0.000	0.000	0.000	0.000
95	A	117	LEU	0	-0.021	0.001	11.682	0.026	0.026	0.000	0.000	0.000	0.000
96	A	118	THR	0	-0.052	-0.049	11.830	0.131	0.131	0.000	0.000	0.000	0.000
97	A	119	THR	0	0.011	0.006	14.479	-0.050	-0.050	0.000	0.000	0.000	0.000
98	A	120	PHE	0	0.001	-0.013	15.952	0.037	0.037	0.000	0.000	0.000	0.000
99	A	121	ASN	0	-0.045	-0.036	18.018	-0.029	-0.029	0.000	0.000	0.000	0.000
100	A	122	GLY	0	0.036	0.026	21.463	-0.057	-0.057	0.000	0.000	0.000	0.000
101	A	123	ALA	0	0.021	0.022	19.544	-0.027	-0.027	0.000	0.000	0.000	0.000
102	A	124	PRO	0	0.032	0.027	18.791	0.106	0.106	0.000	0.000	0.000	0.000
103	A	125	GLU	-1	-0.790	-0.865	14.452	1.225	1.225	0.000	0.000	0.000	0.000
104	A	126	GLY	0	0.017	0.001	12.920	0.014	0.014	0.000	0.000	0.000	0.000
105	A	127	TYR	0	-0.038	-0.017	13.541	-0.034	-0.034	0.000	0.000	0.000	0.000
106	A	128	ASP	-1	-0.838	-0.937	16.763	0.564	0.564	0.000	0.000	0.000	0.000
107	A	129	TRP	0	-0.071	-0.027	11.621	-0.160	-0.160	0.000	0.000	0.000	0.000
108	A	130	GLY	0	0.016	0.021	14.397	-0.013	-0.013	0.000	0.000	0.000	0.000
109	A	131	THR	0	-0.078	-0.048	8.468	-0.075	-0.075	0.000	0.000	0.000	0.000
110	A	132	ALA	0	0.020	0.018	8.819	-0.164	-0.164	0.000	0.000	0.000	0.000
111	A	133	GLN	0	-0.023	-0.010	4.076	1.205	1.767	0.004	-0.073	-0.493	0.000
112	A	134	LEU	0	-0.005	-0.001	5.097	-1.439	-1.439	0.000	0.000	0.000	0.000
113	A	135	PHE	0	-0.047	-0.021	4.327	1.266	1.434	-0.001	-0.014	-0.153	0.000
114	A	136	SER	0	0.011	-0.011	5.976	0.077	0.077	0.000	0.000	0.000	0.000
115	A	137	ALA	0	-0.018	-0.006	6.577	-0.481	-0.481	0.000	0.000	0.000	0.000
116	A	138	TYR	0	-0.055	-0.038	7.792	-0.001	-0.001	0.000	0.000	0.000	0.000
117	A	139	GLN	0	0.003	0.012	10.561	-0.070	-0.070	0.000	0.000	0.000	0.000
118	A	140	VAL	0	-0.026	-0.025	13.942	-0.004	-0.004	0.000	0.000	0.000	0.000
119	A	141	ASP	-1	-0.728	-0.823	17.197	0.236	0.236	0.000	0.000	0.000	0.000
120	A	142	GLY	0	0.092	0.025	20.941	0.034	0.034	0.000	0.000	0.000	0.000
121	A	143	SER	0	-0.037	-0.028	22.514	0.019	0.019	0.000	0.000	0.000	0.000
122	A	144	CYS	0	-0.100	-0.041	19.977	0.013	0.013	0.000	0.000	0.000	0.000
123	A	146	GLN	0	-0.007	-0.014	22.406	-0.055	-0.055	0.000	0.000	0.000	0.000
124	A	147	GLN	0	0.000	0.011	22.045	-0.049	-0.049	0.000	0.000	0.000	0.000
125	A	148	ASN	0	0.000	-0.015	26.725	0.007	0.007	0.000	0.000	0.000	0.000
126	A	149	THR	0	-0.050	-0.049	24.378	-0.022	-0.022	0.000	0.000	0.000	0.000
127	A	150	GLY	0	-0.013	0.002	27.828	-0.013	-0.013	0.000	0.000	0.000	0.000
128	A	151	LYS	1	0.841	0.925	24.132	-0.228	-0.228	0.000	0.000	0.000	0.000
129	A	152	GLN	0	-0.001	-0.003	27.298	0.001	0.001	0.000	0.000	0.000	0.000
130	A	154	GLY	0	0.024	0.009	22.663	0.010	0.010	0.000	0.000	0.000	0.000
131	A	155	ASP	-1	-0.847	-0.927	19.102	0.695	0.695	0.000	0.000	0.000	0.000
132	A	156	PRO	0	-0.022	0.009	16.080	0.124	0.124	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:22:ASN)