FMO DATABASE

FMODB ID: QV69Y

Calculation Name: 4IPV-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 4IPV

Chain ID: A

ChEMBL ID:

UniProt ID: G3XCZ0

Base Structure: X-ray

Registration Date: 2023-09-23

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	128
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-1057686.327234
FMO2-HF: Nuclear repulsion	1009511.90038
FMO2-HF: Total energy	-48174.426854
FMO2-MP2: Total energy	-48315.50151

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:31:ASN)

Summations of interaction energy for fragment #1(A:31: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.
0.623	5.107	0.534	-1.92	-3.099	0.003

Interaction energy analysis for fragmet #1(A:31:ASN)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : 0.053 / q_NPA : 0.012

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	33	LEU	0	-0.016	-0.009	3.314	-1.591	0.485	-0.004	-0.904	-1.168	0.001
4	A	34	GLN	0	-0.029	-0.023	2.684	-0.808	0.072	0.296	-0.338	-0.839	0.000
5	A	35	SER	0	0.045	0.007	3.067	-0.789	0.739	0.242	-0.678	-1.092	0.002
6	A	36	ALA	0	0.014	0.018	5.588	0.624	0.624	0.000	0.000	0.000	0.000
7	A	37	ALA	0	-0.017	-0.016	7.857	0.387	0.387	0.000	0.000	0.000	0.000
8	A	38	GLU	-1	-0.855	-0.915	7.546	1.085	1.085	0.000	0.000	0.000	0.000
9	A	39	GLU	-1	-0.770	-0.828	8.098	-1.901	-1.901	0.000	0.000	0.000	0.000
10	A	40	LEU	0	-0.001	0.000	11.117	0.144	0.144	0.000	0.000	0.000	0.000
11	A	41	ASN	0	0.015	0.000	12.964	0.117	0.117	0.000	0.000	0.000	0.000
12	A	42	ALA	0	-0.021	-0.008	13.398	0.065	0.065	0.000	0.000	0.000	0.000
13	A	43	MET	0	-0.023	-0.005	15.183	0.049	0.049	0.000	0.000	0.000	0.000
14	A	44	LEU	0	0.011	0.003	17.083	0.050	0.050	0.000	0.000	0.000	0.000
15	A	45	GLN	0	-0.041	-0.036	17.567	0.040	0.040	0.000	0.000	0.000	0.000
16	A	46	TYR	0	-0.038	-0.027	19.157	0.007	0.007	0.000	0.000	0.000	0.000
17	A	47	ALA	0	0.038	0.014	20.894	0.017	0.017	0.000	0.000	0.000	0.000
18	A	48	ARG	1	0.894	0.955	23.130	0.069	0.069	0.000	0.000	0.000	0.000
19	A	49	SER	0	0.017	-0.006	23.245	0.012	0.012	0.000	0.000	0.000	0.000
20	A	50	GLU	-1	-0.815	-0.869	24.396	-0.118	-0.118	0.000	0.000	0.000	0.000
21	A	51	ALA	0	-0.003	0.011	26.741	0.009	0.009	0.000	0.000	0.000	0.000
22	A	52	VAL	0	-0.056	-0.035	28.462	0.011	0.011	0.000	0.000	0.000	0.000
23	A	53	SER	0	-0.055	-0.044	27.776	0.011	0.011	0.000	0.000	0.000	0.000
24	A	54	GLN	0	-0.008	-0.009	28.539	0.007	0.007	0.000	0.000	0.000	0.000
25	A	55	ARG	1	0.872	0.955	32.357	0.041	0.041	0.000	0.000	0.000	0.000
26	A	56	ARG	1	0.896	0.932	32.039	0.108	0.108	0.000	0.000	0.000	0.000
27	A	57	ALA	0	-0.017	-0.007	31.942	-0.003	-0.003	0.000	0.000	0.000	0.000
28	A	58	ILE	0	-0.038	0.006	26.361	-0.006	-0.006	0.000	0.000	0.000	0.000
29	A	59	SER	0	-0.019	-0.030	27.334	0.006	0.006	0.000	0.000	0.000	0.000
30	A	60	ILE	0	-0.022	-0.011	19.486	-0.011	-0.011	0.000	0.000	0.000	0.000
31	A	61	GLN	0	-0.035	-0.040	23.650	0.014	0.014	0.000	0.000	0.000	0.000
32	A	62	ALA	0	-0.004	-0.001	21.321	-0.033	-0.033	0.000	0.000	0.000	0.000
33	A	63	LEU	0	-0.023	-0.021	21.704	0.024	0.024	0.000	0.000	0.000	0.000
34	A	64	LYS	1	0.934	0.952	21.282	0.322	0.322	0.000	0.000	0.000	0.000
35	A	65	ASP	-1	-0.841	-0.907	21.856	-0.299	-0.299	0.000	0.000	0.000	0.000
36	A	66	LYS	1	0.891	0.945	22.691	0.214	0.214	0.000	0.000	0.000	0.000
37	A	67	ASP	-1	-0.784	-0.877	16.581	-0.466	-0.466	0.000	0.000	0.000	0.000
38	A	68	TRP	0	-0.006	-0.034	17.323	-0.030	-0.030	0.000	0.000	0.000	0.000
39	A	69	GLY	0	0.025	0.002	14.424	-0.047	-0.047	0.000	0.000	0.000	0.000
40	A	70	LYS	1	0.768	0.891	14.553	0.451	0.451	0.000	0.000	0.000	0.000
41	A	71	GLY	0	0.071	0.052	17.036	0.031	0.031	0.000	0.000	0.000	0.000
42	A	72	LEU	0	-0.045	-0.018	16.494	0.057	0.057	0.000	0.000	0.000	0.000
43	A	73	SER	0	0.003	-0.004	19.937	-0.029	-0.029	0.000	0.000	0.000	0.000
44	A	74	ILE	0	0.036	0.022	19.852	0.013	0.013	0.000	0.000	0.000	0.000
45	A	75	GLY	0	0.053	0.014	23.927	0.000	0.000	0.000	0.000	0.000	0.000
46	A	76	VAL	0	0.020	0.012	27.524	0.005	0.005	0.000	0.000	0.000	0.000
47	A	77	LEU	0	-0.016	0.005	29.340	-0.006	-0.006	0.000	0.000	0.000	0.000
48	A	78	ALA	0	-0.007	-0.016	31.669	0.012	0.012	0.000	0.000	0.000	0.000
49	A	79	SER	0	-0.012	-0.015	34.614	-0.005	-0.005	0.000	0.000	0.000	0.000
50	A	80	GLY	0	0.040	0.031	32.841	-0.002	-0.002	0.000	0.000	0.000	0.000
51	A	81	SER	0	0.002	0.011	30.083	-0.015	-0.015	0.000	0.000	0.000	0.000
52	A	82	ILE	0	-0.020	0.001	26.027	0.010	0.010	0.000	0.000	0.000	0.000
53	A	83	ALA	0	0.005	0.002	29.078	-0.012	-0.012	0.000	0.000	0.000	0.000
54	A	84	ALA	0	-0.009	-0.002	30.255	-0.003	-0.003	0.000	0.000	0.000	0.000
55	A	85	PRO	0	-0.068	-0.033	24.861	0.004	0.004	0.000	0.000	0.000	0.000
56	A	86	LEU	0	0.023	0.010	25.001	0.004	0.004	0.000	0.000	0.000	0.000
57	A	87	ARG	1	0.929	0.973	15.396	0.352	0.352	0.000	0.000	0.000	0.000
58	A	88	LYS	1	0.892	0.944	20.026	0.405	0.405	0.000	0.000	0.000	0.000
59	A	89	HIS	0	-0.049	-0.038	11.508	0.118	0.118	0.000	0.000	0.000	0.000
60	A	90	ASP	-1	-0.873	-0.938	15.223	-0.573	-0.573	0.000	0.000	0.000	0.000
61	A	91	GLY	0	-0.001	0.008	14.413	0.047	0.047	0.000	0.000	0.000	0.000
62	A	92	PHE	0	-0.069	-0.043	9.682	-0.142	-0.142	0.000	0.000	0.000	0.000
63	A	93	ARG	1	0.835	0.884	7.759	2.355	2.355	0.000	0.000	0.000	0.000
64	A	94	ALA	0	0.010	0.020	8.782	0.273	0.273	0.000	0.000	0.000	0.000
65	A	95	ALA	0	0.032	0.002	10.541	0.071	0.071	0.000	0.000	0.000	0.000
66	A	96	THR	0	-0.034	-0.032	10.862	0.021	0.021	0.000	0.000	0.000	0.000
67	A	97	LEU	0	-0.014	0.012	7.232	0.114	0.114	0.000	0.000	0.000	0.000
68	A	98	THR	0	-0.071	-0.038	11.363	0.021	0.021	0.000	0.000	0.000	0.000
69	A	99	ALA	0	0.013	-0.005	13.020	-0.007	-0.007	0.000	0.000	0.000	0.000
70	A	100	LYS	1	0.962	1.006	14.949	0.260	0.260	0.000	0.000	0.000	0.000
71	A	101	GLU	-1	-0.713	-0.868	18.178	-0.117	-0.117	0.000	0.000	0.000	0.000
72	A	102	LYS	1	0.906	0.953	20.709	0.079	0.079	0.000	0.000	0.000	0.000
73	A	103	SER	0	-0.077	-0.038	22.815	0.013	0.013	0.000	0.000	0.000	0.000
74	A	104	ALA	0	-0.046	-0.020	23.791	0.001	0.001	0.000	0.000	0.000	0.000
75	A	105	VAL	0	0.005	0.004	23.797	-0.002	-0.002	0.000	0.000	0.000	0.000
76	A	106	GLU	-1	-0.869	-0.929	23.847	-0.217	-0.217	0.000	0.000	0.000	0.000
77	A	107	HIS	0	0.013	0.000	25.162	-0.015	-0.015	0.000	0.000	0.000	0.000
78	A	108	LEU	0	-0.032	-0.006	22.779	0.016	0.016	0.000	0.000	0.000	0.000
79	A	109	THR	0	0.034	0.018	26.479	-0.015	-0.015	0.000	0.000	0.000	0.000
80	A	110	PHE	0	0.036	0.030	22.889	0.014	0.014	0.000	0.000	0.000	0.000
81	A	111	THR	0	0.019	-0.002	28.771	0.000	0.000	0.000	0.000	0.000	0.000
82	A	112	ALA	0	0.062	0.037	31.122	0.001	0.001	0.000	0.000	0.000	0.000
83	A	113	ASN	0	0.004	0.017	32.933	0.001	0.001	0.000	0.000	0.000	0.000
84	A	114	GLY	0	0.004	-0.001	28.878	0.008	0.008	0.000	0.000	0.000	0.000
85	A	115	THR	0	-0.015	-0.018	27.998	-0.004	-0.004	0.000	0.000	0.000	0.000
86	A	116	LEU	0	0.013	0.005	25.100	-0.008	-0.008	0.000	0.000	0.000	0.000
87	A	117	VAL	0	-0.019	0.016	29.370	0.010	0.010	0.000	0.000	0.000	0.000
88	A	118	PRO	0	0.027	-0.010	31.183	-0.008	-0.008	0.000	0.000	0.000	0.000
89	A	119	PRO	0	0.033	0.023	30.661	-0.007	-0.007	0.000	0.000	0.000	0.000
90	A	120	THR	0	-0.060	-0.042	28.756	0.006	0.006	0.000	0.000	0.000	0.000
91	A	121	GLU	-1	-0.905	-0.953	24.095	-0.042	-0.042	0.000	0.000	0.000	0.000
92	A	122	ARG	1	0.856	0.938	22.683	0.101	0.101	0.000	0.000	0.000	0.000
93	A	123	THR	0	-0.030	-0.031	18.960	0.017	0.017	0.000	0.000	0.000	0.000
94	A	124	PHE	0	0.032	0.014	16.261	-0.008	-0.008	0.000	0.000	0.000	0.000
95	A	125	ALA	0	0.000	0.012	14.695	0.019	0.019	0.000	0.000	0.000	0.000
96	A	126	ILE	0	-0.012	-0.009	9.448	-0.028	-0.028	0.000	0.000	0.000	0.000
97	A	127	CYS	0	0.021	0.004	10.616	0.048	0.048	0.000	0.000	0.000	0.000
98	A	128	GLN	0	0.096	0.059	6.824	-0.255	-0.255	0.000	0.000	0.000	0.000
99	A	129	ASN	0	-0.005	-0.018	10.229	0.012	0.012	0.000	0.000	0.000	0.000
100	A	130	GLY	0	-0.005	0.009	13.485	0.024	0.024	0.000	0.000	0.000	0.000
101	A	131	LYS	1	0.838	0.917	10.229	-0.101	-0.101	0.000	0.000	0.000	0.000
102	A	132	THR	0	0.035	-0.018	12.946	-0.016	-0.016	0.000	0.000	0.000	0.000
103	A	133	ASP	-1	-0.843	-0.889	11.672	0.159	0.159	0.000	0.000	0.000	0.000
104	A	134	GLY	0	0.023	0.009	8.119	0.013	0.013	0.000	0.000	0.000	0.000
105	A	135	GLY	0	-0.013	0.006	7.523	-0.125	-0.125	0.000	0.000	0.000	0.000
106	A	136	ARG	1	0.803	0.878	7.520	-0.015	-0.015	0.000	0.000	0.000	0.000
107	A	137	VAL	0	0.009	0.016	10.837	-0.033	-0.033	0.000	0.000	0.000	0.000
108	A	138	LEU	0	-0.008	0.000	13.703	0.027	0.027	0.000	0.000	0.000	0.000
109	A	139	SER	0	-0.010	-0.017	15.857	-0.018	-0.018	0.000	0.000	0.000	0.000
110	A	140	ILE	0	-0.002	-0.012	19.560	0.000	0.000	0.000	0.000	0.000	0.000
111	A	141	SER	0	0.082	0.048	22.554	-0.002	-0.002	0.000	0.000	0.000	0.000
112	A	142	GLN	0	0.053	0.018	25.658	-0.010	-0.010	0.000	0.000	0.000	0.000
113	A	143	ALA	0	-0.023	-0.006	28.399	-0.002	-0.002	0.000	0.000	0.000	0.000
114	A	144	GLY	0	-0.010	-0.004	26.300	0.000	0.000	0.000	0.000	0.000	0.000
115	A	145	ARG	1	0.829	0.905	23.770	0.000	0.000	0.000	0.000	0.000	0.000
116	A	146	ILE	0	0.026	0.030	17.898	-0.002	-0.002	0.000	0.000	0.000	0.000
117	A	147	GLN	0	-0.007	-0.011	17.670	0.038	0.038	0.000	0.000	0.000	0.000
118	A	148	LEU	0	-0.003	0.005	9.643	-0.035	-0.035	0.000	0.000	0.000	0.000
119	A	149	GLU	-1	-0.792	-0.869	14.317	0.106	0.106	0.000	0.000	0.000	0.000
120	A	150	PRO	0	0.054	0.031	12.697	-0.006	-0.006	0.000	0.000	0.000	0.000
121	A	151	SER	0	0.042	-0.003	8.871	-0.040	-0.040	0.000	0.000	0.000	0.000
122	A	152	SER	0	-0.026	-0.002	10.917	-0.022	-0.022	0.000	0.000	0.000	0.000
123	A	153	LYS	1	0.837	0.925	13.917	-0.046	-0.046	0.000	0.000	0.000	0.000
124	A	154	ALA	0	0.034	0.028	13.111	-0.027	-0.027	0.000	0.000	0.000	0.000
125	A	155	PRO	0	-0.026	-0.022	12.889	0.006	0.006	0.000	0.000	0.000	0.000
126	A	156	GLN	0	0.002	-0.003	15.830	0.004	0.004	0.000	0.000	0.000	0.000
127	A	157	SER	0	0.006	0.003	18.305	0.000	0.000	0.000	0.000	0.000	0.000
128	A	159	TYR	0	-0.001	0.001	17.167	-0.035	-0.035	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:31:ASN)