FMO DATABASE

FMODB ID: 7GN8K

Calculation Name: 2WP7-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 2WP7

Chain ID: A

ChEMBL ID:

UniProt ID: Q9CQT7

Base Structure: X-ray

Registration Date: 2023-03-14

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	158
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-1487212.41616
FMO2-HF: Nuclear repulsion	1427006.894642
FMO2-HF: Total energy	-60205.521517
FMO2-MP2: Total energy	-60383.373984

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:4:PRO)

Summations of interaction energy for fragment #1(A:4:PRO)

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.
-10.642	-5.277	2.981	-3.603	-4.741	-0.029

Interaction energy analysis for fragmet #1(A:4:PRO)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : 0.019 / q_NPA : -0.005

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	6	LEU	0	-0.009	0.004	2.999	-1.223	0.860	0.039	-0.779	-1.343	0.002
4	A	7	TYR	0	0.009	0.000	4.840	0.733	0.824	-0.001	-0.010	-0.079	0.000
5	A	8	PRO	0	-0.003	-0.007	8.360	-0.053	-0.053	0.000	0.000	0.000	0.000
6	A	9	VAL	0	0.013	0.001	10.819	0.078	0.078	0.000	0.000	0.000	0.000
7	A	10	LYS	1	0.838	0.907	13.440	0.506	0.506	0.000	0.000	0.000	0.000
8	A	11	LEU	0	0.041	0.025	17.132	0.004	0.004	0.000	0.000	0.000	0.000
9	A	12	TYR	0	-0.031	-0.010	20.360	0.009	0.009	0.000	0.000	0.000	0.000
10	A	13	VAL	0	-0.014	-0.013	23.310	0.003	0.003	0.000	0.000	0.000	0.000
11	A	14	TYR	0	-0.009	-0.039	26.328	0.014	0.014	0.000	0.000	0.000	0.000
12	A	15	ASP	-1	-0.782	-0.860	30.115	-0.122	-0.122	0.000	0.000	0.000	0.000
13	A	16	LEU	0	0.027	-0.003	33.059	0.008	0.008	0.000	0.000	0.000	0.000
14	A	17	SER	0	-0.098	-0.063	35.482	0.009	0.009	0.000	0.000	0.000	0.000
15	A	18	LYS	1	0.847	0.907	32.866	0.132	0.132	0.000	0.000	0.000	0.000
16	A	19	GLY	0	-0.015	-0.012	37.594	0.004	0.004	0.000	0.000	0.000	0.000
17	A	20	LEU	0	-0.031	-0.015	39.303	0.003	0.003	0.000	0.000	0.000	0.000
18	A	21	ALA	0	0.076	0.025	38.867	0.003	0.003	0.000	0.000	0.000	0.000
19	A	22	ARG	1	0.875	0.981	36.631	0.115	0.115	0.000	0.000	0.000	0.000
20	A	23	ARG	1	0.936	0.962	40.614	0.080	0.080	0.000	0.000	0.000	0.000
21	A	24	LEU	0	0.018	0.007	44.104	0.003	0.003	0.000	0.000	0.000	0.000
22	A	25	SER	0	0.028	0.011	41.766	0.002	0.002	0.000	0.000	0.000	0.000
23	A	26	PRO	0	-0.006	-0.005	43.907	0.002	0.002	0.000	0.000	0.000	0.000
24	A	27	ILE	0	-0.033	-0.017	46.540	0.002	0.002	0.000	0.000	0.000	0.000
25	A	28	MET	0	-0.060	-0.015	45.516	0.002	0.002	0.000	0.000	0.000	0.000
26	A	29	LEU	0	-0.014	-0.018	41.952	0.000	0.000	0.000	0.000	0.000	0.000
27	A	30	GLY	0	-0.018	0.011	46.112	0.000	0.000	0.000	0.000	0.000	0.000
28	A	31	LYS	1	0.795	0.879	40.201	0.108	0.108	0.000	0.000	0.000	0.000
29	A	32	GLN	0	-0.088	-0.048	40.226	0.004	0.004	0.000	0.000	0.000	0.000
30	A	33	LEU	0	0.020	-0.001	37.274	-0.005	-0.005	0.000	0.000	0.000	0.000
31	A	34	GLU	-1	-0.833	-0.930	34.879	-0.111	-0.111	0.000	0.000	0.000	0.000
32	A	35	GLY	0	-0.003	0.003	34.879	0.001	0.001	0.000	0.000	0.000	0.000
33	A	36	ILE	0	-0.044	-0.019	35.182	-0.001	-0.001	0.000	0.000	0.000	0.000
34	A	37	TRP	0	0.008	0.001	29.501	0.000	0.000	0.000	0.000	0.000	0.000
35	A	38	HIS	0	0.066	0.046	27.849	0.002	0.002	0.000	0.000	0.000	0.000
36	A	39	THR	0	-0.072	-0.069	24.370	-0.010	-0.010	0.000	0.000	0.000	0.000
37	A	40	SER	0	0.012	-0.018	23.363	0.006	0.006	0.000	0.000	0.000	0.000
38	A	41	ILE	0	0.012	0.006	16.701	-0.016	-0.016	0.000	0.000	0.000	0.000
39	A	42	VAL	0	-0.024	-0.003	17.620	0.021	0.021	0.000	0.000	0.000	0.000
40	A	43	VAL	0	0.025	0.008	12.273	-0.065	-0.065	0.000	0.000	0.000	0.000
41	A	44	HIS	1	0.845	0.941	9.889	0.653	0.653	0.000	0.000	0.000	0.000
42	A	45	LYS	1	0.877	0.936	14.150	0.245	0.245	0.000	0.000	0.000	0.000
43	A	46	ASP	-1	-0.862	-0.915	17.604	-0.147	-0.147	0.000	0.000	0.000	0.000
44	A	47	GLU	-1	-0.762	-0.846	19.014	-0.241	-0.241	0.000	0.000	0.000	0.000
45	A	48	PHE	0	0.021	0.008	18.105	0.022	0.022	0.000	0.000	0.000	0.000
46	A	49	PHE	0	-0.007	-0.024	21.939	-0.016	-0.016	0.000	0.000	0.000	0.000
47	A	50	PHE	0	-0.016	0.004	24.803	0.003	0.003	0.000	0.000	0.000	0.000
48	A	51	GLY	0	0.066	0.019	27.355	0.000	0.000	0.000	0.000	0.000	0.000
49	A	52	SER	0	-0.003	0.000	31.159	-0.001	-0.001	0.000	0.000	0.000	0.000
50	A	53	SER	0	-0.064	-0.031	32.393	0.009	0.009	0.000	0.000	0.000	0.000
51	A	54	GLY	0	0.016	0.014	29.969	0.004	0.004	0.000	0.000	0.000	0.000
52	A	55	ILE	0	-0.016	-0.010	22.957	-0.002	-0.002	0.000	0.000	0.000	0.000
53	A	56	SER	0	-0.040	-0.007	25.917	0.019	0.019	0.000	0.000	0.000	0.000
54	A	57	SER	0	-0.030	-0.005	23.091	-0.019	-0.019	0.000	0.000	0.000	0.000
55	A	58	CYS	0	-0.004	-0.009	24.172	0.020	0.020	0.000	0.000	0.000	0.000
56	A	59	THR	0	0.091	0.057	23.605	-0.013	-0.013	0.000	0.000	0.000	0.000
57	A	60	PRO	0	-0.029	-0.025	21.059	0.003	0.003	0.000	0.000	0.000	0.000
58	A	61	GLY	0	-0.011	-0.002	23.822	0.013	0.013	0.000	0.000	0.000	0.000
59	A	62	GLY	0	-0.060	-0.004	26.915	0.014	0.014	0.000	0.000	0.000	0.000
60	A	63	THR	0	0.017	-0.008	28.645	0.006	0.006	0.000	0.000	0.000	0.000
61	A	64	LEU	0	-0.024	-0.017	31.277	0.003	0.003	0.000	0.000	0.000	0.000
62	A	65	LEU	0	-0.039	-0.010	30.310	0.005	0.005	0.000	0.000	0.000	0.000
63	A	66	GLY	0	-0.022	0.002	32.716	0.001	0.001	0.000	0.000	0.000	0.000
64	A	67	PRO	0	-0.004	-0.022	29.232	-0.008	-0.008	0.000	0.000	0.000	0.000
65	A	68	PRO	0	-0.027	0.010	25.369	0.005	0.005	0.000	0.000	0.000	0.000
66	A	69	ASP	-1	-0.813	-0.902	28.427	-0.129	-0.129	0.000	0.000	0.000	0.000
67	A	70	SER	0	-0.056	-0.033	26.171	-0.003	-0.003	0.000	0.000	0.000	0.000
68	A	71	VAL	0	0.019	0.008	20.623	-0.004	-0.004	0.000	0.000	0.000	0.000
69	A	72	VAL	0	-0.012	0.008	20.275	-0.003	-0.003	0.000	0.000	0.000	0.000
70	A	73	ASP	-1	-0.891	-0.941	15.037	-0.621	-0.621	0.000	0.000	0.000	0.000
71	A	74	VAL	0	0.013	0.013	14.658	0.024	0.024	0.000	0.000	0.000	0.000
72	A	75	GLY	0	0.029	0.017	12.147	-0.015	-0.015	0.000	0.000	0.000	0.000
73	A	76	ASN	0	-0.065	-0.032	7.265	0.124	0.124	0.000	0.000	0.000	0.000
74	A	77	THR	0	0.008	-0.007	7.362	-0.001	-0.001	0.000	0.000	0.000	0.000
75	A	78	GLU	-1	-0.893	-0.956	2.566	-10.202	-7.050	2.944	-2.814	-3.282	-0.031
76	A	79	VAL	0	-0.032	0.001	5.261	0.329	0.368	-0.001	0.000	-0.037	0.000
77	A	80	THR	0	-0.026	-0.053	8.220	-0.027	-0.027	0.000	0.000	0.000	0.000
78	A	81	GLU	-1	-0.856	-0.953	10.178	-0.315	-0.315	0.000	0.000	0.000	0.000
79	A	82	GLU	-1	-0.830	-0.897	12.917	-0.108	-0.108	0.000	0.000	0.000	0.000
80	A	83	ILE	0	0.041	0.024	10.373	-0.012	-0.012	0.000	0.000	0.000	0.000
81	A	84	PHE	0	-0.025	-0.016	13.380	-0.031	-0.031	0.000	0.000	0.000	0.000
82	A	85	LEU	0	0.009	0.004	15.082	0.020	0.020	0.000	0.000	0.000	0.000
83	A	86	GLU	-1	-0.926	-0.962	16.788	-0.141	-0.141	0.000	0.000	0.000	0.000
84	A	87	TYR	0	-0.015	-0.012	16.407	0.003	0.003	0.000	0.000	0.000	0.000
85	A	88	LEU	0	-0.013	-0.011	18.335	0.018	0.018	0.000	0.000	0.000	0.000
86	A	89	SER	0	-0.044	-0.030	20.720	0.020	0.020	0.000	0.000	0.000	0.000
87	A	90	SER	0	0.020	0.017	21.388	0.006	0.006	0.000	0.000	0.000	0.000
88	A	91	LEU	0	0.013	0.021	20.761	0.010	0.010	0.000	0.000	0.000	0.000
89	A	92	GLY	0	-0.005	0.006	23.921	0.012	0.012	0.000	0.000	0.000	0.000
90	A	93	GLU	-1	-0.890	-0.934	25.531	-0.116	-0.116	0.000	0.000	0.000	0.000
91	A	94	SER	0	-0.120	-0.075	25.759	0.009	0.009	0.000	0.000	0.000	0.000
92	A	95	LEU	0	0.000	-0.005	25.581	0.007	0.007	0.000	0.000	0.000	0.000
93	A	96	PHE	0	-0.016	-0.002	24.431	-0.001	-0.001	0.000	0.000	0.000	0.000
94	A	97	ARG	1	0.857	0.926	27.961	0.113	0.113	0.000	0.000	0.000	0.000
95	A	98	GLY	0	0.013	-0.004	30.926	-0.003	-0.003	0.000	0.000	0.000	0.000
96	A	99	GLU	-1	-0.907	-0.968	33.450	-0.108	-0.108	0.000	0.000	0.000	0.000
97	A	100	ALA	0	0.035	0.036	31.483	0.003	0.003	0.000	0.000	0.000	0.000
98	A	101	TYR	0	-0.026	0.000	30.869	-0.008	-0.008	0.000	0.000	0.000	0.000
99	A	102	ASN	0	0.016	-0.013	33.519	0.005	0.005	0.000	0.000	0.000	0.000
100	A	103	LEU	0	0.004	0.004	34.010	-0.008	-0.008	0.000	0.000	0.000	0.000
101	A	104	PHE	0	-0.051	-0.030	34.463	-0.007	-0.007	0.000	0.000	0.000	0.000
102	A	105	GLU	-1	-0.862	-0.929	33.185	-0.125	-0.125	0.000	0.000	0.000	0.000
103	A	106	HIS	0	-0.031	-0.009	27.734	-0.011	-0.011	0.000	0.000	0.000	0.000
104	A	107	ASN	0	0.052	0.029	29.680	-0.005	-0.005	0.000	0.000	0.000	0.000
105	A	108	CYS	0	0.014	0.001	27.458	-0.009	-0.009	0.000	0.000	0.000	0.000
106	A	109	ASN	0	-0.007	0.002	25.747	-0.023	-0.023	0.000	0.000	0.000	0.000
107	A	110	THR	0	0.005	0.012	25.099	-0.020	-0.020	0.000	0.000	0.000	0.000
108	A	111	PHE	0	0.042	0.029	21.686	-0.021	-0.021	0.000	0.000	0.000	0.000
109	A	112	SER	0	0.002	-0.006	21.397	-0.031	-0.031	0.000	0.000	0.000	0.000
110	A	113	ASN	0	-0.030	-0.021	20.232	-0.049	-0.049	0.000	0.000	0.000	0.000
111	A	114	GLU	-1	-0.883	-0.952	19.892	-0.291	-0.291	0.000	0.000	0.000	0.000
112	A	115	VAL	0	0.000	0.009	16.866	-0.043	-0.043	0.000	0.000	0.000	0.000
113	A	116	ALA	0	0.003	-0.003	15.902	-0.069	-0.069	0.000	0.000	0.000	0.000
114	A	117	GLN	0	-0.005	0.006	15.032	-0.061	-0.061	0.000	0.000	0.000	0.000
115	A	118	PHE	0	-0.019	-0.008	13.804	-0.072	-0.072	0.000	0.000	0.000	0.000
116	A	119	LEU	0	-0.023	0.003	11.623	-0.091	-0.091	0.000	0.000	0.000	0.000
117	A	120	THR	0	-0.044	-0.035	10.201	-0.178	-0.178	0.000	0.000	0.000	0.000
118	A	121	GLY	0	0.013	0.021	11.757	-0.024	-0.024	0.000	0.000	0.000	0.000
119	A	122	ARG	1	0.817	0.903	13.545	0.753	0.753	0.000	0.000	0.000	0.000
120	A	123	LYS	1	0.908	0.959	16.649	0.270	0.270	0.000	0.000	0.000	0.000
121	A	124	ILE	0	0.001	0.009	20.149	-0.003	-0.003	0.000	0.000	0.000	0.000
122	A	125	PRO	0	0.014	-0.010	21.990	0.018	0.018	0.000	0.000	0.000	0.000
123	A	126	SER	0	0.054	0.017	24.983	0.001	0.001	0.000	0.000	0.000	0.000
124	A	127	TYR	0	-0.019	0.012	27.331	0.003	0.003	0.000	0.000	0.000	0.000
125	A	128	ILE	0	-0.031	-0.011	25.151	0.012	0.012	0.000	0.000	0.000	0.000
126	A	129	THR	0	-0.016	-0.044	25.641	0.001	0.001	0.000	0.000	0.000	0.000
127	A	130	ASP	-1	-0.793	-0.878	28.613	-0.185	-0.185	0.000	0.000	0.000	0.000
128	A	131	LEU	0	-0.007	0.021	31.912	0.012	0.012	0.000	0.000	0.000	0.000
129	A	132	PRO	0	0.059	0.028	32.689	0.011	0.011	0.000	0.000	0.000	0.000
130	A	133	SER	0	-0.018	-0.017	35.043	0.009	0.009	0.000	0.000	0.000	0.000
131	A	134	GLU	-1	-0.858	-0.901	35.777	-0.116	-0.116	0.000	0.000	0.000	0.000
132	A	135	VAL	0	-0.002	-0.004	38.156	0.008	0.008	0.000	0.000	0.000	0.000
133	A	136	LEU	0	0.021	0.021	38.291	0.007	0.007	0.000	0.000	0.000	0.000
134	A	137	SER	0	-0.076	-0.035	40.170	0.006	0.006	0.000	0.000	0.000	0.000
135	A	138	THR	0	-0.006	-0.020	42.757	0.003	0.003	0.000	0.000	0.000	0.000
136	A	139	PRO	0	0.019	-0.008	45.555	0.000	0.000	0.000	0.000	0.000	0.000
137	A	140	PHE	0	0.035	0.020	43.540	0.001	0.001	0.000	0.000	0.000	0.000
138	A	141	GLY	0	0.025	0.012	43.766	0.001	0.001	0.000	0.000	0.000	0.000
139	A	142	GLN	0	-0.065	-0.045	44.182	0.002	0.002	0.000	0.000	0.000	0.000
140	A	143	ALA	0	-0.033	-0.015	46.882	0.001	0.001	0.000	0.000	0.000	0.000
141	A	144	LEU	0	-0.012	-0.003	45.998	0.003	0.003	0.000	0.000	0.000	0.000
142	A	145	ARG	1	0.777	0.871	39.200	0.103	0.103	0.000	0.000	0.000	0.000
143	A	146	PRO	0	0.036	0.003	44.010	-0.002	-0.002	0.000	0.000	0.000	0.000
144	A	147	PHE	0	-0.012	0.004	45.199	0.000	0.000	0.000	0.000	0.000	0.000
145	A	148	LEU	0	0.001	-0.009	41.128	-0.002	-0.002	0.000	0.000	0.000	0.000
146	A	149	ASP	-1	-0.750	-0.854	40.150	-0.104	-0.104	0.000	0.000	0.000	0.000
147	A	150	SER	0	-0.073	-0.035	40.503	-0.001	-0.001	0.000	0.000	0.000	0.000
148	A	151	ILE	0	-0.087	-0.026	38.266	0.001	0.001	0.000	0.000	0.000	0.000
149	A	152	GLN	0	-0.023	-0.020	36.826	-0.008	-0.008	0.000	0.000	0.000	0.000
150	A	153	ILE	0	-0.032	-0.016	33.404	0.004	0.004	0.000	0.000	0.000	0.000
151	A	154	GLN	0	0.065	0.025	30.574	-0.009	-0.009	0.000	0.000	0.000	0.000
152	A	155	PRO	0	-0.015	0.003	30.393	0.009	0.009	0.000	0.000	0.000	0.000
153	A	156	PRO	0	-0.009	0.008	32.129	-0.002	-0.002	0.000	0.000	0.000	0.000
154	A	157	GLY	0	0.017	-0.011	32.087	-0.001	-0.001	0.000	0.000	0.000	0.000
155	A	158	GLY	0	0.003	0.014	28.785	0.000	0.000	0.000	0.000	0.000	0.000
156	A	159	ASN	0	-0.096	-0.048	27.330	0.010	0.010	0.000	0.000	0.000	0.000
157	A	160	SER	0	0.048	0.014	27.430	-0.009	-0.009	0.000	0.000	0.000	0.000
158	A	161	VAL	0	-0.006	0.013	21.963	0.008	0.008	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:4:PRO)