FMO DATABASE

FMODB ID: 98Y72

Calculation Name: 3LWG-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 3LWG

Chain ID: A

ChEMBL ID:

UniProt ID: D5MNX9

Base Structure: X-ray

Registration Date: 2023-09-20

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	OptHSide
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	120
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 22 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-959586.246861
FMO2-HF: Nuclear repulsion	912822.952388
FMO2-HF: Total energy	-46763.294473
FMO2-MP2: Total energy	-46896.701203

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:10:GLU)

Summations of interaction energy for fragment #1(A:10:GLU)

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.
10.945	14.314	0.091	-1.445	-2.016	0.006

Interaction energy analysis for fragmet #1(A:10:GLU)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : -1 / q_Mulliken : -0.938 / q_NPA : -0.979

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

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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	12	LEU	0	-0.024	-0.006	2.966	-9.506	-6.631	0.092	-1.341	-1.627	0.006
4	A	13	LEU	0	-0.075	-0.047	4.947	0.004	0.152	-0.001	-0.009	-0.139	0.000
5	A	14	VAL	0	-0.042	-0.023	7.571	-2.498	-2.498	0.000	0.000	0.000	0.000
6	A	15	CYS	0	0.001	0.004	8.556	1.268	1.268	0.000	0.000	0.000	0.000
7	A	16	THR	0	0.043	0.024	7.778	-0.109	-0.109	0.000	0.000	0.000	0.000
8	A	17	ARG	1	0.908	0.944	9.818	-17.414	-17.414	0.000	0.000	0.000	0.000
9	A	18	LEU	0	-0.009	0.005	11.618	-1.254	-1.254	0.000	0.000	0.000	0.000
10	A	19	ASP	-1	-0.801	-0.899	11.721	19.442	19.442	0.000	0.000	0.000	0.000
11	A	20	GLN	0	0.058	0.019	8.144	-0.841	-0.841	0.000	0.000	0.000	0.000
12	A	21	ASN	0	-0.016	-0.003	13.008	-0.887	-0.887	0.000	0.000	0.000	0.000
13	A	22	LEU	0	-0.028	-0.016	15.975	-1.028	-1.028	0.000	0.000	0.000	0.000
14	A	23	CYS	0	-0.108	-0.043	14.900	-0.746	-0.746	0.000	0.000	0.000	0.000
15	A	24	ALA	0	0.025	0.001	14.815	-0.891	-0.891	0.000	0.000	0.000	0.000
16	A	25	GLU	-1	-0.892	-0.939	11.873	20.908	20.908	0.000	0.000	0.000	0.000
17	A	26	LEU	0	-0.018	-0.012	5.812	-0.711	-0.711	0.000	0.000	0.000	0.000
18	A	27	ILE	0	-0.037	-0.009	9.105	1.210	1.210	0.000	0.000	0.000	0.000
19	A	28	SER	0	-0.026	-0.021	8.520	1.334	1.334	0.000	0.000	0.000	0.000
20	A	29	PHE	0	0.011	-0.007	3.927	-1.861	-1.515	0.000	-0.095	-0.250	0.000
21	A	30	GLY	0	0.030	0.026	8.823	1.723	1.723	0.000	0.000	0.000	0.000
22	A	31	SER	0	-0.053	-0.039	10.692	-1.004	-1.004	0.000	0.000	0.000	0.000
23	A	32	GLY	0	0.019	0.011	13.765	-1.014	-1.014	0.000	0.000	0.000	0.000
24	A	33	LYS	1	0.944	0.962	13.703	-17.813	-17.813	0.000	0.000	0.000	0.000
25	A	34	ALA	0	0.002	-0.003	11.322	1.608	1.608	0.000	0.000	0.000	0.000
26	A	35	THR	0	-0.005	0.007	11.812	-1.256	-1.256	0.000	0.000	0.000	0.000
27	A	36	VAL	0	-0.012	0.003	11.451	1.765	1.765	0.000	0.000	0.000	0.000
28	A	37	CYS	0	-0.013	0.002	13.535	-1.326	-1.326	0.000	0.000	0.000	0.000
29	A	38	LEU	0	-0.009	0.007	15.969	0.596	0.596	0.000	0.000	0.000	0.000
30	A	39	THR	0	0.063	0.022	18.509	-0.287	-0.287	0.000	0.000	0.000	0.000
31	A	40	PRO	0	-0.026	-0.005	20.573	0.208	0.208	0.000	0.000	0.000	0.000
32	A	41	LYS	1	0.918	0.934	17.400	-15.861	-15.861	0.000	0.000	0.000	0.000
33	A	42	GLU	-1	-0.709	-0.850	24.391	10.742	10.742	0.000	0.000	0.000	0.000
34	A	43	PHE	0	-0.070	-0.029	20.545	-0.250	-0.250	0.000	0.000	0.000	0.000
35	A	44	MET	0	-0.087	-0.022	19.785	-0.060	-0.060	0.000	0.000	0.000	0.000
36	A	45	LEU	0	-0.012	0.003	25.866	0.046	0.046	0.000	0.000	0.000	0.000
37	A	46	ALA	0	-0.096	-0.041	29.448	-0.004	-0.004	0.000	0.000	0.000	0.000
38	A	47	GLU	-1	-0.913	-0.951	31.882	7.966	7.966	0.000	0.000	0.000	0.000
39	A	48	ASP	-1	-0.968	-0.990	33.062	8.508	8.508	0.000	0.000	0.000	0.000
40	A	49	ASP	-1	-0.936	-0.973	33.463	8.539	8.539	0.000	0.000	0.000	0.000
41	A	50	VAL	0	-0.022	-0.009	30.958	0.087	0.087	0.000	0.000	0.000	0.000
42	A	51	VAL	0	-0.020	-0.006	24.788	0.096	0.096	0.000	0.000	0.000	0.000
43	A	52	HIS	0	0.043	0.017	27.125	-0.222	-0.222	0.000	0.000	0.000	0.000
44	A	53	ALA	0	0.054	0.009	26.319	0.423	0.423	0.000	0.000	0.000	0.000
45	A	54	GLY	0	-0.030	-0.009	25.173	0.319	0.319	0.000	0.000	0.000	0.000
46	A	55	PHE	0	0.024	0.009	21.107	0.461	0.461	0.000	0.000	0.000	0.000
47	A	56	ILE	0	0.013	0.027	21.208	0.629	0.629	0.000	0.000	0.000	0.000
48	A	57	VAL	0	0.021	-0.008	21.584	0.435	0.435	0.000	0.000	0.000	0.000
49	A	58	GLY	0	-0.002	0.021	19.862	0.422	0.422	0.000	0.000	0.000	0.000
50	A	59	ALA	0	0.056	0.023	16.988	0.852	0.852	0.000	0.000	0.000	0.000
51	A	60	ALA	0	0.000	0.006	16.531	0.862	0.862	0.000	0.000	0.000	0.000
52	A	61	SER	0	-0.027	-0.037	17.690	0.228	0.228	0.000	0.000	0.000	0.000
53	A	62	PHE	0	0.005	-0.011	9.293	0.457	0.457	0.000	0.000	0.000	0.000
54	A	63	ALA	0	0.071	0.039	13.049	1.166	1.166	0.000	0.000	0.000	0.000
55	A	64	ALA	0	-0.003	-0.012	13.886	0.520	0.520	0.000	0.000	0.000	0.000
56	A	65	LEU	0	0.003	-0.016	13.330	0.124	0.124	0.000	0.000	0.000	0.000
57	A	66	CYS	0	-0.056	-0.020	9.540	1.396	1.396	0.000	0.000	0.000	0.000
58	A	67	ALA	0	-0.013	0.009	10.779	0.944	0.944	0.000	0.000	0.000	0.000
59	A	68	LEU	0	-0.065	-0.034	13.375	-0.035	-0.035	0.000	0.000	0.000	0.000
60	A	69	ASN	0	0.016	0.018	7.475	0.632	0.632	0.000	0.000	0.000	0.000
61	A	70	LYS	1	0.939	0.973	11.026	-17.428	-17.428	0.000	0.000	0.000	0.000
62	A	71	LYS	1	0.986	0.990	11.484	-18.524	-18.524	0.000	0.000	0.000	0.000
63	A	72	ASN	0	-0.039	-0.014	12.818	-0.299	-0.299	0.000	0.000	0.000	0.000
64	A	73	SER	0	0.032	0.000	14.141	-0.842	-0.842	0.000	0.000	0.000	0.000
65	A	74	LEU	0	-0.009	-0.005	16.803	0.278	0.278	0.000	0.000	0.000	0.000
66	A	75	ILE	0	0.014	0.016	18.175	-0.221	-0.221	0.000	0.000	0.000	0.000
67	A	76	SER	0	-0.068	-0.056	20.997	-0.081	-0.081	0.000	0.000	0.000	0.000
68	A	77	SER	0	-0.039	-0.040	24.507	-0.481	-0.481	0.000	0.000	0.000	0.000
69	A	78	MET	0	0.006	0.006	23.222	0.442	0.442	0.000	0.000	0.000	0.000
70	A	79	LYS	1	0.927	0.987	26.375	-9.679	-9.679	0.000	0.000	0.000	0.000
71	A	80	VAL	0	-0.001	-0.014	26.045	0.235	0.235	0.000	0.000	0.000	0.000
72	A	81	ASN	0	-0.065	-0.036	28.119	-0.444	-0.444	0.000	0.000	0.000	0.000
73	A	82	LEU	0	0.004	-0.004	27.008	0.362	0.362	0.000	0.000	0.000	0.000
74	A	83	LEU	0	-0.053	-0.030	29.121	-0.308	-0.308	0.000	0.000	0.000	0.000
75	A	84	ALA	0	0.016	0.011	30.354	-0.305	-0.305	0.000	0.000	0.000	0.000
76	A	85	PRO	0	-0.003	0.006	30.135	0.290	0.290	0.000	0.000	0.000	0.000
77	A	86	ILE	0	0.010	0.015	24.789	0.141	0.141	0.000	0.000	0.000	0.000
78	A	87	GLU	-1	-0.859	-0.935	28.496	9.150	9.150	0.000	0.000	0.000	0.000
79	A	88	ILE	0	-0.039	-0.028	26.424	0.537	0.537	0.000	0.000	0.000	0.000
80	A	89	LYS	1	0.742	0.837	24.252	-11.428	-11.428	0.000	0.000	0.000	0.000
81	A	90	GLN	0	0.037	0.061	25.662	0.161	0.161	0.000	0.000	0.000	0.000
82	A	91	GLU	-1	-0.931	-0.957	20.540	14.667	14.667	0.000	0.000	0.000	0.000
83	A	92	ILE	0	-0.027	-0.019	21.146	-0.337	-0.337	0.000	0.000	0.000	0.000
84	A	93	TYR	0	-0.014	-0.026	16.785	1.132	1.132	0.000	0.000	0.000	0.000
85	A	94	PHE	0	0.018	0.002	17.134	-0.774	-0.774	0.000	0.000	0.000	0.000
86	A	95	ASN	0	-0.011	0.006	16.276	2.025	2.025	0.000	0.000	0.000	0.000
87	A	96	ALA	0	0.007	-0.002	15.418	-0.822	-0.822	0.000	0.000	0.000	0.000
88	A	97	THR	0	-0.009	-0.020	16.598	0.773	0.773	0.000	0.000	0.000	0.000
89	A	98	ILE	0	-0.044	-0.010	16.437	-0.567	-0.567	0.000	0.000	0.000	0.000
90	A	99	THR	0	-0.012	-0.007	19.785	-0.162	-0.162	0.000	0.000	0.000	0.000
91	A	100	HIS	0	-0.007	-0.006	23.257	-0.223	-0.223	0.000	0.000	0.000	0.000
92	A	101	THR	0	0.046	0.013	20.448	0.410	0.410	0.000	0.000	0.000	0.000
93	A	102	SER	0	-0.012	0.002	23.196	-0.412	-0.412	0.000	0.000	0.000	0.000
94	A	103	SER	0	-0.021	-0.006	20.443	-0.036	-0.036	0.000	0.000	0.000	0.000
95	A	104	LYS	1	0.924	0.956	20.506	-10.256	-10.256	0.000	0.000	0.000	0.000
96	A	105	LYS	1	0.906	0.950	22.605	-10.121	-10.121	0.000	0.000	0.000	0.000
97	A	106	SER	0	-0.010	-0.004	20.412	-0.001	-0.001	0.000	0.000	0.000	0.000
98	A	107	THR	0	0.006	0.013	22.457	-0.151	-0.151	0.000	0.000	0.000	0.000
99	A	108	ILE	0	-0.008	0.002	17.567	0.248	0.248	0.000	0.000	0.000	0.000
100	A	109	ARG	1	0.849	0.923	20.876	-11.056	-11.056	0.000	0.000	0.000	0.000
101	A	110	VAL	0	-0.026	-0.024	18.698	0.624	0.624	0.000	0.000	0.000	0.000
102	A	111	GLU	-1	-0.830	-0.912	20.946	10.345	10.345	0.000	0.000	0.000	0.000
103	A	112	GLY	0	0.027	0.016	20.984	0.681	0.681	0.000	0.000	0.000	0.000
104	A	113	GLU	-1	-0.892	-0.948	22.122	12.051	12.051	0.000	0.000	0.000	0.000
105	A	114	PHE	0	0.042	0.014	22.987	0.516	0.516	0.000	0.000	0.000	0.000
106	A	115	MET	0	-0.023	-0.020	24.985	-0.235	-0.235	0.000	0.000	0.000	0.000
107	A	116	GLU	-1	-0.925	-0.961	24.488	11.340	11.340	0.000	0.000	0.000	0.000
108	A	117	ILE	0	-0.038	-0.001	26.269	-0.302	-0.302	0.000	0.000	0.000	0.000
109	A	118	LYS	1	0.795	0.887	26.172	-10.136	-10.136	0.000	0.000	0.000	0.000
110	A	119	VAL	0	0.033	0.006	25.577	-0.334	-0.334	0.000	0.000	0.000	0.000
111	A	120	PHE	0	-0.012	-0.008	22.698	-0.083	-0.083	0.000	0.000	0.000	0.000
112	A	121	GLU	-1	-0.798	-0.886	25.225	9.951	9.951	0.000	0.000	0.000	0.000
113	A	122	GLY	0	0.022	0.008	24.672	-0.340	-0.340	0.000	0.000	0.000	0.000
114	A	123	ASP	-1	-0.907	-0.920	24.028	11.146	11.146	0.000	0.000	0.000	0.000
115	A	124	PHE	0	0.026	0.001	20.912	-0.214	-0.214	0.000	0.000	0.000	0.000
116	A	125	GLU	-1	-0.826	-0.860	22.573	10.641	10.641	0.000	0.000	0.000	0.000
117	A	126	ILE	0	0.003	-0.010	17.305	0.232	0.232	0.000	0.000	0.000	0.000
118	A	127	LEU	0	-0.031	-0.014	21.007	-0.280	-0.280	0.000	0.000	0.000	0.000
119	A	128	VAL	0	0.002	-0.009	16.929	0.686	0.686	0.000	0.000	0.000	0.000
120	A	129	PHE	0	-0.018	-0.002	18.939	-0.279	-0.279	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:10:GLU)