FMO DATABASE

FMODB ID: Q1G4Y

Calculation Name: 4IM9-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 4IM9

Chain ID: A

ChEMBL ID:

UniProt ID:

Base Structure: X-ray

Registration Date: 2023-06-19

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	-1150735.801392
FMO2-HF: Nuclear repulsion	1097599.90138
FMO2-HF: Total energy	-53135.900012
FMO2-MP2: Total energy	-53291.3153

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:12:THR)

Summations of interaction energy for fragment #1(A:12:THR)

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.
-17.202	-12.153	0.75	-2.14	-3.66	-0.004

Interaction energy analysis for fragmet #1(A:12:THR)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : -0.031 / q_NPA : -0.039

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	14	MET	0	-0.003	0.024	3.214	-2.168	-0.316	0.065	-0.741	-1.176	0.001
4	A	15	ARG	1	0.925	0.931	2.517	-2.037	-0.796	0.659	-0.545	-1.356	0.000
5	A	16	ASP	-1	-0.826	-0.892	3.463	-11.617	-10.008	0.028	-0.825	-0.812	-0.005
6	A	17	VAL	0	0.030	0.024	5.249	1.036	1.117	-0.001	-0.003	-0.077	0.000
7	A	18	ILE	0	-0.065	-0.048	6.905	0.378	0.378	0.000	0.000	0.000	0.000
8	A	19	ALA	0	-0.026	-0.011	7.590	0.241	0.241	0.000	0.000	0.000	0.000
9	A	20	LEU	0	0.065	0.028	9.117	0.322	0.322	0.000	0.000	0.000	0.000
10	A	21	LEU	0	-0.008	0.024	11.144	0.227	0.227	0.000	0.000	0.000	0.000
11	A	22	ILE	0	-0.037	-0.021	11.309	0.136	0.136	0.000	0.000	0.000	0.000
12	A	23	GLN	0	-0.049	-0.030	10.484	0.119	0.119	0.000	0.000	0.000	0.000
13	A	24	ASN	0	-0.053	-0.031	14.445	0.129	0.129	0.000	0.000	0.000	0.000
14	A	25	PRO	0	0.029	0.010	17.100	0.020	0.020	0.000	0.000	0.000	0.000
15	A	26	SER	0	0.069	0.027	18.624	0.033	0.033	0.000	0.000	0.000	0.000
16	A	27	TYR	0	0.023	-0.009	14.669	0.074	0.074	0.000	0.000	0.000	0.000
17	A	28	ALA	0	0.013	0.005	17.605	0.025	0.025	0.000	0.000	0.000	0.000
18	A	29	GLU	-1	-1.001	-0.998	18.555	-0.180	-0.180	0.000	0.000	0.000	0.000
19	A	30	LEU	0	-0.015	0.006	17.998	0.038	0.038	0.000	0.000	0.000	0.000
20	A	31	VAL	0	-0.043	-0.006	15.361	0.025	0.025	0.000	0.000	0.000	0.000
21	A	32	PRO	0	0.011	0.024	17.134	0.021	0.021	0.000	0.000	0.000	0.000
22	A	33	ASP	-1	-0.861	-0.956	18.988	0.089	0.089	0.000	0.000	0.000	0.000
23	A	34	LEU	0	0.031	0.012	14.787	0.029	0.029	0.000	0.000	0.000	0.000
24	A	35	ALA	0	-0.057	-0.030	18.878	0.053	0.053	0.000	0.000	0.000	0.000
25	A	36	SER	0	-0.037	-0.018	21.602	0.023	0.023	0.000	0.000	0.000	0.000
26	A	37	VAL	0	0.047	0.009	16.450	0.029	0.029	0.000	0.000	0.000	0.000
27	A	38	ARG	1	0.944	0.986	16.384	-0.089	-0.089	0.000	0.000	0.000	0.000
28	A	39	HIS	0	-0.031	0.000	16.917	0.011	0.011	0.000	0.000	0.000	0.000
29	A	40	LEU	0	-0.039	-0.011	15.223	0.039	0.039	0.000	0.000	0.000	0.000
30	A	41	MET	0	0.038	0.013	14.751	0.053	0.053	0.000	0.000	0.000	0.000
31	A	42	ILE	0	-0.020	-0.004	8.924	0.089	0.089	0.000	0.000	0.000	0.000
32	A	43	PRO	0	0.013	-0.009	7.220	-0.206	-0.206	0.000	0.000	0.000	0.000
33	A	44	GLY	0	0.026	0.012	7.355	0.535	0.535	0.000	0.000	0.000	0.000
34	A	45	LEU	0	0.048	0.031	8.424	-0.314	-0.314	0.000	0.000	0.000	0.000
35	A	46	ASP	-1	-0.848	-0.917	10.808	0.424	0.424	0.000	0.000	0.000	0.000
36	A	47	THR	0	-0.044	-0.022	9.950	-0.113	-0.113	0.000	0.000	0.000	0.000
37	A	48	PHE	0	0.037	0.003	9.624	-0.112	-0.112	0.000	0.000	0.000	0.000
38	A	49	SER	0	-0.045	-0.033	11.465	-0.087	-0.087	0.000	0.000	0.000	0.000
39	A	50	GLU	-1	-0.867	-0.920	14.778	0.020	0.020	0.000	0.000	0.000	0.000
40	A	51	VAL	0	-0.003	-0.009	12.855	-0.036	-0.036	0.000	0.000	0.000	0.000
41	A	52	LEU	0	0.019	0.003	15.056	-0.025	-0.025	0.000	0.000	0.000	0.000
42	A	53	GLU	-1	-1.002	-0.991	16.644	-0.003	-0.003	0.000	0.000	0.000	0.000
43	A	54	LYS	1	0.944	0.972	19.296	0.075	0.075	0.000	0.000	0.000	0.000
44	A	55	CYS	0	-0.052	-0.020	17.458	-0.026	-0.026	0.000	0.000	0.000	0.000
45	A	56	ARG	1	0.802	0.898	19.169	0.078	0.078	0.000	0.000	0.000	0.000
46	A	57	GLN	0	-0.035	-0.020	22.380	0.007	0.007	0.000	0.000	0.000	0.000
47	A	58	TYR	0	-0.093	-0.040	23.707	0.014	0.014	0.000	0.000	0.000	0.000
48	A	59	PRO	0	0.074	0.039	23.688	-0.023	-0.023	0.000	0.000	0.000	0.000
49	A	60	HIS	0	-0.023	-0.011	23.874	-0.035	-0.035	0.000	0.000	0.000	0.000
50	A	61	ILE	0	-0.051	0.000	21.425	-0.002	-0.002	0.000	0.000	0.000	0.000
51	A	62	THR	0	0.051	0.031	22.336	-0.034	-0.034	0.000	0.000	0.000	0.000
52	A	63	THR	0	0.079	0.009	16.913	0.030	0.030	0.000	0.000	0.000	0.000
53	A	64	GLY	0	-0.018	-0.007	19.456	0.013	0.013	0.000	0.000	0.000	0.000
54	A	65	GLN	0	0.004	-0.023	21.822	0.016	0.016	0.000	0.000	0.000	0.000
55	A	66	LEU	0	0.004	0.005	16.936	0.034	0.034	0.000	0.000	0.000	0.000
56	A	67	LEU	0	0.006	-0.005	16.109	0.029	0.029	0.000	0.000	0.000	0.000
57	A	68	GLU	-1	-0.850	-0.907	19.794	-0.161	-0.161	0.000	0.000	0.000	0.000
58	A	69	HIS	0	-0.071	-0.034	21.355	0.047	0.047	0.000	0.000	0.000	0.000
59	A	70	TRP	0	-0.069	-0.041	16.685	0.001	0.001	0.000	0.000	0.000	0.000
60	A	71	ARG	1	0.865	0.930	20.374	0.139	0.139	0.000	0.000	0.000	0.000
61	A	72	ASP	-1	-0.935	-0.962	22.203	-0.052	-0.052	0.000	0.000	0.000	0.000
62	A	73	SER	0	-0.052	-0.022	19.553	0.030	0.030	0.000	0.000	0.000	0.000
63	A	74	LYS	1	0.935	0.951	15.310	-0.268	-0.268	0.000	0.000	0.000	0.000
64	A	75	ASN	0	-0.055	-0.047	13.594	0.047	0.047	0.000	0.000	0.000	0.000
65	A	76	GLU	-1	-0.765	-0.856	14.382	-0.211	-0.211	0.000	0.000	0.000	0.000
66	A	77	THR	0	0.004	0.007	14.060	-0.069	-0.069	0.000	0.000	0.000	0.000
67	A	78	LEU	0	-0.062	-0.028	7.720	-0.064	-0.064	0.000	0.000	0.000	0.000
68	A	79	LEU	0	0.046	0.005	10.847	-0.178	-0.178	0.000	0.000	0.000	0.000
69	A	80	SER	0	0.002	-0.007	12.939	-0.099	-0.099	0.000	0.000	0.000	0.000
70	A	81	ARG	1	0.870	0.945	5.698	1.012	1.012	0.000	0.000	0.000	0.000
71	A	82	LEU	0	-0.041	-0.032	6.422	-0.130	-0.130	0.000	0.000	0.000	0.000
72	A	83	ALA	0	0.046	0.036	10.206	-0.184	-0.184	0.000	0.000	0.000	0.000
73	A	84	SER	0	-0.025	-0.025	12.605	0.066	0.066	0.000	0.000	0.000	0.000
74	A	85	TRP	0	-0.097	-0.042	4.062	1.097	1.363	-0.001	-0.026	-0.239	0.000
75	A	86	GLU	-1	-0.943	-0.981	6.793	-4.165	-4.165	0.000	0.000	0.000	0.000
76	A	87	ILE	0	0.038	0.046	10.329	-0.031	-0.031	0.000	0.000	0.000	0.000
77	A	88	PRO	0	-0.038	-0.001	13.088	0.077	0.077	0.000	0.000	0.000	0.000
78	A	89	LEU	0	-0.043	-0.032	15.443	0.082	0.082	0.000	0.000	0.000	0.000
79	A	90	VAL	0	-0.042	-0.031	18.744	0.063	0.063	0.000	0.000	0.000	0.000
80	A	91	GLU	-1	-0.866	-0.941	16.927	-0.886	-0.886	0.000	0.000	0.000	0.000
81	A	92	ASP	-1	-0.941	-0.971	18.753	-0.503	-0.503	0.000	0.000	0.000	0.000
82	A	93	ASN	0	-0.026	-0.021	16.261	0.079	0.079	0.000	0.000	0.000	0.000
83	A	94	GLN	0	0.017	0.021	12.721	-0.044	-0.044	0.000	0.000	0.000	0.000
84	A	95	GLU	-1	-0.908	-0.960	14.334	-0.561	-0.561	0.000	0.000	0.000	0.000
85	A	96	GLU	-1	-0.922	-0.959	15.829	-0.511	-0.511	0.000	0.000	0.000	0.000
86	A	97	LEU	0	0.016	0.020	8.866	-0.004	-0.004	0.000	0.000	0.000	0.000
87	A	98	PHE	0	-0.016	0.008	11.082	-0.205	-0.205	0.000	0.000	0.000	0.000
88	A	99	LEU	0	0.012	0.005	12.094	0.038	0.038	0.000	0.000	0.000	0.000
89	A	100	ASP	-1	-0.895	-0.938	11.648	-0.538	-0.538	0.000	0.000	0.000	0.000
90	A	101	SER	0	-0.089	-0.072	7.640	-0.128	-0.128	0.000	0.000	0.000	0.000
91	A	102	LEU	0	-0.039	-0.031	9.185	0.386	0.386	0.000	0.000	0.000	0.000
92	A	103	ASP	-1	-0.867	-0.927	11.448	0.138	0.138	0.000	0.000	0.000	0.000
93	A	104	LYS	1	0.908	0.951	7.274	0.574	0.574	0.000	0.000	0.000	0.000
94	A	105	ILE	0	-0.028	-0.010	6.034	0.580	0.580	0.000	0.000	0.000	0.000
95	A	106	LEU	0	0.001	-0.005	9.799	0.127	0.127	0.000	0.000	0.000	0.000
96	A	107	ALA	0	0.004	0.003	12.876	0.039	0.039	0.000	0.000	0.000	0.000
97	A	108	GLN	0	-0.005	-0.008	6.895	0.011	0.011	0.000	0.000	0.000	0.000
98	A	109	CYS	0	-0.068	-0.025	12.004	-0.010	-0.010	0.000	0.000	0.000	0.000
99	A	110	VAL	0	0.003	-0.005	14.333	-0.051	-0.051	0.000	0.000	0.000	0.000
100	A	111	GLU	-1	-0.937	-0.954	14.832	0.765	0.765	0.000	0.000	0.000	0.000
101	A	112	LYS	1	0.947	0.966	13.194	-1.112	-1.112	0.000	0.000	0.000	0.000
102	A	113	GLN	0	0.018	-0.001	16.566	-0.010	-0.010	0.000	0.000	0.000	0.000
103	A	114	ILE	0	-0.014	0.000	19.453	-0.056	-0.056	0.000	0.000	0.000	0.000
104	A	115	GLU	-1	-0.969	-0.979	17.969	0.606	0.606	0.000	0.000	0.000	0.000
105	A	116	ASN	0	-0.024	-0.017	18.821	-0.020	-0.020	0.000	0.000	0.000	0.000
106	A	117	LEU	0	-0.009	0.005	22.211	-0.038	-0.038	0.000	0.000	0.000	0.000
107	A	118	GLN	0	0.037	0.001	23.791	-0.045	-0.045	0.000	0.000	0.000	0.000
108	A	119	ALA	0	-0.064	-0.028	24.242	-0.022	-0.022	0.000	0.000	0.000	0.000
109	A	120	LYS	1	0.872	0.909	26.171	-0.243	-0.243	0.000	0.000	0.000	0.000
110	A	121	GLU	-1	-0.901	-0.950	28.386	0.187	0.187	0.000	0.000	0.000	0.000
111	A	122	ARG	1	0.924	0.967	24.974	-0.333	-0.333	0.000	0.000	0.000	0.000
112	A	123	SER	0	-0.082	-0.025	29.930	-0.018	-0.018	0.000	0.000	0.000	0.000
113	A	124	VAL	0	-0.035	-0.026	31.609	-0.011	-0.011	0.000	0.000	0.000	0.000
114	A	125	GLY	0	-0.005	0.020	32.793	-0.014	-0.014	0.000	0.000	0.000	0.000
115	A	126	LEU	0	-0.045	-0.024	28.733	0.005	0.005	0.000	0.000	0.000	0.000
116	A	127	SER	0	0.007	0.002	32.321	-0.017	-0.017	0.000	0.000	0.000	0.000
117	A	128	THR	0	0.013	-0.028	33.363	0.005	0.005	0.000	0.000	0.000	0.000
118	A	129	GLU	-1	-0.959	-0.976	30.761	0.121	0.121	0.000	0.000	0.000	0.000
119	A	130	GLU	-1	-0.735	-0.846	28.477	0.204	0.204	0.000	0.000	0.000	0.000
120	A	131	LYS	1	0.887	0.958	28.710	-0.165	-0.165	0.000	0.000	0.000	0.000
121	A	132	ARG	1	0.920	0.962	30.353	-0.109	-0.109	0.000	0.000	0.000	0.000
122	A	133	GLU	-1	-0.858	-0.924	24.175	0.239	0.239	0.000	0.000	0.000	0.000
123	A	134	LEU	0	0.009	-0.003	24.923	0.007	0.007	0.000	0.000	0.000	0.000
124	A	135	GLN	0	0.005	-0.022	25.873	0.005	0.005	0.000	0.000	0.000	0.000
125	A	136	ASP	-1	-0.907	-0.945	26.373	0.111	0.111	0.000	0.000	0.000	0.000
126	A	137	LEU	0	-0.060	-0.026	20.727	-0.005	-0.005	0.000	0.000	0.000	0.000
127	A	138	ILE	0	-0.026	-0.010	22.559	0.008	0.008	0.000	0.000	0.000	0.000
128	A	139	LEU	0	-0.079	-0.027	24.572	-0.010	-0.010	0.000	0.000	0.000	0.000
129	A	140	LYS	1	0.938	0.947	24.581	-0.095	-0.095	0.000	0.000	0.000	0.000
130	A	141	GLY	0	0.056	0.051	20.385	-0.014	-0.014	0.000	0.000	0.000	0.000
131	A	142	LEU	0	-0.075	-0.072	17.581	-0.014	-0.014	0.000	0.000	0.000	0.000
132	A	143	LYS	1	0.978	1.028	17.929	-0.101	-0.101	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:12:THR)