FMO DATABASE

FMODB ID: R57L8

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	OptH
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	-1186059.911949
FMO2-HF: Nuclear repulsion	1133360.833133
FMO2-HF: Total energy	-52699.078816
FMO2-MP2: Total energy	-52851.278265

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.
1.667	4.841	0.034	-0.947	-2.258	0

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 : -0.055 / q_NPA : -0.038

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	0.018	0.013	3.768	0.223	1.986	0.001	-0.592	-1.172	0.002
4	A	25	ILE	0	-0.010	-0.005	5.709	-1.174	-1.192	-0.001	-0.001	0.021	0.000
5	A	26	LYS	1	0.925	0.949	9.171	-1.789	-1.789	0.000	0.000	0.000	0.000
6	A	27	TRP	0	-0.027	-0.016	12.100	-0.074	-0.074	0.000	0.000	0.000	0.000
7	A	28	ASP	-1	-0.864	-0.934	15.743	0.573	0.573	0.000	0.000	0.000	0.000
8	A	29	ASP	-1	-0.919	-0.964	18.727	0.455	0.455	0.000	0.000	0.000	0.000
9	A	30	LYS	1	0.875	0.938	21.089	-0.428	-0.428	0.000	0.000	0.000	0.000
10	A	31	PHE	0	-0.051	-0.052	17.560	-0.043	-0.043	0.000	0.000	0.000	0.000
11	A	32	GLN	0	0.036	0.020	21.632	0.053	0.053	0.000	0.000	0.000	0.000
12	A	33	ASN	0	0.040	0.040	24.173	-0.048	-0.048	0.000	0.000	0.000	0.000
13	A	34	ASP	-1	-0.862	-0.932	26.905	0.298	0.298	0.000	0.000	0.000	0.000
14	A	35	THR	0	-0.050	-0.048	29.429	-0.028	-0.028	0.000	0.000	0.000	0.000
15	A	36	LEU	0	-0.017	0.000	25.889	-0.025	-0.025	0.000	0.000	0.000	0.000
16	A	37	SER	0	0.044	0.028	29.801	0.003	0.003	0.000	0.000	0.000	0.000
17	A	38	ILE	0	0.045	0.007	27.713	0.016	0.016	0.000	0.000	0.000	0.000
18	A	39	SER	0	-0.039	-0.040	27.339	0.004	0.004	0.000	0.000	0.000	0.000
19	A	40	GLU	-1	-0.991	-0.983	26.743	0.222	0.222	0.000	0.000	0.000	0.000
20	A	41	PHE	0	-0.032	0.012	22.265	0.028	0.028	0.000	0.000	0.000	0.000
21	A	42	LYS	1	0.929	0.944	20.207	-0.261	-0.261	0.000	0.000	0.000	0.000
22	A	43	CYS	0	-0.061	-0.003	17.019	0.043	0.043	0.000	0.000	0.000	0.000
23	A	44	SER	0	0.047	0.033	22.692	-0.008	-0.008	0.000	0.000	0.000	0.000
24	A	45	ALA	0	0.017	0.003	26.409	-0.004	-0.004	0.000	0.000	0.000	0.000
25	A	46	ALA	0	-0.025	-0.027	23.375	-0.006	-0.006	0.000	0.000	0.000	0.000
26	A	47	LEU	0	0.020	0.004	22.934	0.003	0.003	0.000	0.000	0.000	0.000
27	A	48	ALA	0	0.030	0.026	26.242	0.001	0.001	0.000	0.000	0.000	0.000
28	A	49	LYS	1	0.906	0.946	27.620	-0.148	-0.148	0.000	0.000	0.000	0.000
29	A	50	LEU	0	-0.019	0.005	23.305	0.001	0.001	0.000	0.000	0.000	0.000
30	A	51	GLY	0	0.086	0.051	27.643	0.022	0.022	0.000	0.000	0.000	0.000
31	A	52	PRO	0	-0.022	-0.016	30.633	-0.004	-0.004	0.000	0.000	0.000	0.000
32	A	53	ASP	-1	-0.821	-0.898	32.331	0.134	0.134	0.000	0.000	0.000	0.000
33	A	54	PRO	0	-0.042	-0.024	31.470	0.000	0.000	0.000	0.000	0.000	0.000
34	A	55	LYS	1	0.872	0.929	32.850	-0.119	-0.119	0.000	0.000	0.000	0.000
35	A	56	HIS	0	-0.075	-0.042	35.990	-0.014	-0.014	0.000	0.000	0.000	0.000
36	A	57	PRO	0	-0.019	-0.006	32.848	0.009	0.009	0.000	0.000	0.000	0.000
37	A	58	PRO	0	0.014	0.029	29.760	-0.003	-0.003	0.000	0.000	0.000	0.000
38	A	59	THR	0	-0.094	-0.054	32.423	-0.008	-0.008	0.000	0.000	0.000	0.000
39	A	60	LYS	1	0.886	0.936	31.068	-0.216	-0.216	0.000	0.000	0.000	0.000
40	A	61	LEU	0	-0.018	0.000	23.729	0.001	0.001	0.000	0.000	0.000	0.000
41	A	62	GLY	0	0.040	-0.003	27.380	0.016	0.016	0.000	0.000	0.000	0.000
42	A	63	GLU	-1	-0.889	-0.922	29.490	0.212	0.212	0.000	0.000	0.000	0.000
43	A	64	VAL	0	-0.073	-0.020	24.777	-0.012	-0.012	0.000	0.000	0.000	0.000
44	A	65	LEU	0	-0.017	-0.031	26.116	0.021	0.021	0.000	0.000	0.000	0.000
45	A	66	ASN	0	-0.063	-0.052	20.079	0.009	0.009	0.000	0.000	0.000	0.000
46	A	67	PHE	0	0.015	0.075	23.065	0.054	0.054	0.000	0.000	0.000	0.000
47	A	68	PRO	0	0.012	-0.010	23.552	-0.020	-0.020	0.000	0.000	0.000	0.000
48	A	69	HIS	0	-0.010	-0.025	19.495	0.070	0.070	0.000	0.000	0.000	0.000
49	A	70	PHE	0	-0.029	-0.012	18.925	0.008	0.008	0.000	0.000	0.000	0.000
50	A	71	VAL	0	0.010	-0.013	13.721	0.087	0.087	0.000	0.000	0.000	0.000
51	A	72	ALA	0	-0.015	0.019	15.529	-0.112	-0.112	0.000	0.000	0.000	0.000
52	A	73	ALA	0	0.023	-0.015	11.513	0.194	0.194	0.000	0.000	0.000	0.000
53	A	74	PRO	0	0.024	0.026	9.458	-0.110	-0.110	0.000	0.000	0.000	0.000
54	A	75	GLU	-1	-0.908	-0.956	12.766	0.001	0.001	0.000	0.000	0.000	0.000
55	A	76	ALA	0	-0.024	0.018	13.684	-0.078	-0.078	0.000	0.000	0.000	0.000
56	A	77	GLN	0	-0.004	-0.023	6.035	0.173	0.173	0.000	0.000	0.000	0.000
57	A	78	THR	0	-0.003	-0.005	10.959	0.132	0.132	0.000	0.000	0.000	0.000
58	A	79	GLU	-1	-0.875	-0.921	13.255	0.026	0.026	0.000	0.000	0.000	0.000
59	A	81	GLY	0	0.025	0.010	19.429	-0.029	-0.029	0.000	0.000	0.000	0.000
60	A	82	SER	0	-0.060	-0.029	15.738	0.031	0.031	0.000	0.000	0.000	0.000
61	A	83	CYS	0	-0.042	0.006	17.098	0.120	0.120	0.000	0.000	0.000	0.000
62	A	84	TRP	0	0.007	-0.002	8.405	0.031	0.031	0.000	0.000	0.000	0.000
63	A	85	LYS	1	0.905	0.959	13.045	-0.871	-0.871	0.000	0.000	0.000	0.000
64	A	86	LEU	0	-0.005	-0.006	9.800	0.234	0.234	0.000	0.000	0.000	0.000
65	A	87	ARG	1	0.953	0.971	9.859	-1.393	-1.393	0.000	0.000	0.000	0.000
66	A	88	TYR	0	-0.012	-0.047	9.311	0.606	0.606	0.000	0.000	0.000	0.000
67	A	89	LYS	1	0.854	0.919	10.897	-1.403	-1.403	0.000	0.000	0.000	0.000
68	A	90	GLY	0	-0.034	-0.014	12.931	0.001	0.001	0.000	0.000	0.000	0.000
69	A	91	ASN	0	-0.073	-0.035	14.818	-0.193	-0.193	0.000	0.000	0.000	0.000
70	A	92	HIS	0	-0.022	-0.036	14.112	0.215	0.215	0.000	0.000	0.000	0.000
71	A	93	ALA	0	-0.001	0.013	14.838	-0.115	-0.115	0.000	0.000	0.000	0.000
72	A	94	PHE	0	0.023	-0.001	15.154	0.107	0.107	0.000	0.000	0.000	0.000
73	A	95	VAL	0	0.025	0.008	13.759	-0.038	-0.038	0.000	0.000	0.000	0.000
74	A	96	THR	0	0.041	0.019	16.536	-0.014	-0.014	0.000	0.000	0.000	0.000
75	A	97	VAL	0	-0.043	-0.001	14.133	0.046	0.046	0.000	0.000	0.000	0.000
76	A	98	VAL	0	0.024	-0.004	17.009	-0.084	-0.084	0.000	0.000	0.000	0.000
77	A	99	ASP	-1	-0.735	-0.869	18.181	0.346	0.346	0.000	0.000	0.000	0.000
78	A	100	ARG	1	0.796	0.888	15.227	-0.235	-0.235	0.000	0.000	0.000	0.000
79	A	101	VAL	0	-0.009	0.006	12.110	0.035	0.035	0.000	0.000	0.000	0.000
80	A	102	GLU	-1	-0.897	-0.972	13.767	0.220	0.220	0.000	0.000	0.000	0.000
81	A	103	GLU	-1	-0.917	-0.945	9.584	0.241	0.241	0.000	0.000	0.000	0.000
82	A	104	ALA	0	-0.020	-0.015	6.990	0.129	0.129	0.000	0.000	0.000	0.000
83	A	105	ASN	0	-0.059	-0.047	3.530	-0.489	0.296	0.021	-0.254	-0.551	-0.002
84	A	106	LEU	0	0.032	0.024	5.714	1.625	1.625	0.000	0.000	0.000	0.000
85	A	107	PHE	0	0.029	-0.002	7.801	-0.498	-0.498	0.000	0.000	0.000	0.000
86	A	108	VAL	0	-0.012	-0.009	10.898	0.277	0.277	0.000	0.000	0.000	0.000
87	A	109	GLY	0	0.046	0.014	13.599	-0.132	-0.132	0.000	0.000	0.000	0.000
88	A	110	GLY	0	0.037	0.031	15.961	-0.018	-0.018	0.000	0.000	0.000	0.000
89	A	111	THR	0	0.044	-0.001	18.431	0.097	0.097	0.000	0.000	0.000	0.000
90	A	112	ASP	-1	-0.888	-0.942	19.495	0.614	0.614	0.000	0.000	0.000	0.000
91	A	113	LEU	0	-0.034	-0.004	15.936	0.040	0.040	0.000	0.000	0.000	0.000
92	A	114	VAL	0	0.001	0.002	13.924	0.083	0.083	0.000	0.000	0.000	0.000
93	A	115	LYS	1	0.960	1.006	16.114	-0.531	-0.531	0.000	0.000	0.000	0.000
94	A	116	ASN	0	-0.021	0.010	18.640	-0.015	-0.015	0.000	0.000	0.000	0.000
95	A	117	LEU	0	-0.026	0.012	11.897	0.013	0.013	0.000	0.000	0.000	0.000
96	A	118	THR	0	-0.067	-0.062	12.159	0.076	0.076	0.000	0.000	0.000	0.000
97	A	119	THR	0	0.034	-0.012	14.667	-0.033	-0.033	0.000	0.000	0.000	0.000
98	A	120	PHE	0	-0.038	-0.021	16.239	0.011	0.011	0.000	0.000	0.000	0.000
99	A	121	ASN	0	-0.036	-0.017	18.261	-0.041	-0.041	0.000	0.000	0.000	0.000
100	A	122	GLY	0	0.037	0.016	21.916	-0.037	-0.037	0.000	0.000	0.000	0.000
101	A	123	ALA	0	0.003	0.007	19.799	-0.022	-0.022	0.000	0.000	0.000	0.000
102	A	124	PRO	0	0.015	0.025	18.961	0.098	0.098	0.000	0.000	0.000	0.000
103	A	125	GLU	-1	-0.769	-0.833	14.732	1.135	1.135	0.000	0.000	0.000	0.000
104	A	126	GLY	0	0.034	-0.003	13.148	0.056	0.056	0.000	0.000	0.000	0.000
105	A	127	TYR	0	-0.051	-0.018	13.935	-0.010	-0.010	0.000	0.000	0.000	0.000
106	A	128	ASP	-1	-0.840	-0.932	16.967	0.660	0.660	0.000	0.000	0.000	0.000
107	A	129	TRP	0	-0.098	-0.036	11.641	-0.154	-0.154	0.000	0.000	0.000	0.000
108	A	130	GLY	0	0.030	0.021	14.638	-0.042	-0.042	0.000	0.000	0.000	0.000
109	A	131	THR	0	-0.085	-0.037	8.050	0.075	0.075	0.000	0.000	0.000	0.000
110	A	132	ALA	0	0.024	0.016	9.261	-0.220	-0.220	0.000	0.000	0.000	0.000
111	A	133	GLN	0	0.000	-0.003	3.749	3.026	3.549	0.014	-0.097	-0.439	0.000
112	A	134	LEU	0	-0.030	-0.017	5.171	-1.422	-1.422	0.000	0.000	0.000	0.000
113	A	135	PHE	0	-0.046	-0.020	4.837	0.728	0.849	-0.001	-0.003	-0.117	0.000
114	A	136	SER	0	-0.006	-0.020	5.795	0.248	0.248	0.000	0.000	0.000	0.000
115	A	137	ALA	0	0.013	0.006	6.678	-0.361	-0.361	0.000	0.000	0.000	0.000
116	A	138	TYR	0	-0.088	-0.100	7.523	-0.040	-0.040	0.000	0.000	0.000	0.000
117	A	139	GLN	0	0.002	0.013	10.238	-0.019	-0.019	0.000	0.000	0.000	0.000
118	A	140	VAL	0	-0.024	-0.025	13.419	-0.034	-0.034	0.000	0.000	0.000	0.000
119	A	141	ASP	-1	-0.754	-0.840	16.654	0.240	0.240	0.000	0.000	0.000	0.000
120	A	142	GLY	0	0.099	0.026	20.255	0.039	0.039	0.000	0.000	0.000	0.000
121	A	143	SER	0	-0.045	-0.024	21.609	0.025	0.025	0.000	0.000	0.000	0.000
122	A	144	CYS	0	-0.068	-0.027	19.619	0.013	0.013	0.000	0.000	0.000	0.000
123	A	146	GLN	0	0.004	-0.007	21.765	-0.040	-0.040	0.000	0.000	0.000	0.000
124	A	147	GLN	0	-0.020	-0.009	21.296	-0.049	-0.049	0.000	0.000	0.000	0.000
125	A	148	ASN	0	-0.005	-0.012	25.825	-0.002	-0.002	0.000	0.000	0.000	0.000
126	A	149	THR	0	-0.036	-0.045	23.701	-0.021	-0.021	0.000	0.000	0.000	0.000
127	A	150	GLY	0	-0.002	0.008	27.171	-0.018	-0.018	0.000	0.000	0.000	0.000
128	A	151	LYS	1	0.894	0.950	24.273	-0.180	-0.180	0.000	0.000	0.000	0.000
129	A	152	GLN	0	-0.006	0.003	27.091	-0.001	-0.001	0.000	0.000	0.000	0.000
130	A	154	GLY	0	-0.008	-0.006	22.785	0.001	0.001	0.000	0.000	0.000	0.000
131	A	155	ASP	-1	-0.896	-0.965	20.970	0.489	0.489	0.000	0.000	0.000	0.000
132	A	156	PRO	0	0.006	0.083	16.506	0.080	0.080	0.000	0.000	0.000	0.000

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