FMO DATABASE

FMODB ID: 7GQ7K

Calculation Name: 3K77-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 3K77

Chain ID: A

ChEMBL ID:

UniProt ID: P18887

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	152
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-1447578.110592
FMO2-HF: Nuclear repulsion	1388565.946766
FMO2-HF: Total energy	-59012.163826
FMO2-MP2: Total energy	-59183.903975

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:2:PRO)

Summations of interaction energy for fragment #1(A:2: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.
-13.709	-5.084	5.885	-5.616	-8.898	-0.041

Interaction energy analysis for fragmet #1(A:2:PRO)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : 0.013 / q_NPA : -0.009

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	4	ILE	0	-0.029	-0.013	3.805	-0.889	0.494	-0.010	-0.526	-0.848	0.003
4	A	5	ARG	1	0.924	0.971	5.585	1.148	1.148	0.000	0.000	0.000	0.000
5	A	6	LEU	0	-0.022	-0.006	8.414	-0.093	-0.093	0.000	0.000	0.000	0.000
6	A	7	ARG	1	0.947	0.980	11.910	0.501	0.501	0.000	0.000	0.000	0.000
7	A	8	HIS	0	-0.011	-0.024	14.692	0.056	0.056	0.000	0.000	0.000	0.000
8	A	9	VAL	0	0.060	0.037	17.526	-0.061	-0.061	0.000	0.000	0.000	0.000
9	A	10	VAL	0	-0.074	-0.038	19.193	0.025	0.025	0.000	0.000	0.000	0.000
10	A	11	SER	0	-0.013	-0.011	21.750	0.032	0.032	0.000	0.000	0.000	0.000
11	A	12	CYS	0	0.005	0.006	23.113	-0.014	-0.014	0.000	0.000	0.000	0.000
12	A	13	SER	0	-0.029	-0.004	25.476	0.010	0.010	0.000	0.000	0.000	0.000
13	A	14	SER	0	-0.001	-0.017	27.603	0.016	0.016	0.000	0.000	0.000	0.000
14	A	15	GLN	0	0.045	0.029	25.705	-0.019	-0.019	0.000	0.000	0.000	0.000
15	A	16	ASP	-1	-0.798	-0.884	28.034	-0.044	-0.044	0.000	0.000	0.000	0.000
16	A	17	SER	0	-0.032	-0.016	28.687	-0.006	-0.006	0.000	0.000	0.000	0.000
17	A	18	THR	0	-0.058	-0.027	28.614	0.004	0.004	0.000	0.000	0.000	0.000
18	A	19	HIS	0	-0.062	-0.037	25.430	0.001	0.001	0.000	0.000	0.000	0.000
19	A	20	CYS	0	0.012	0.007	24.737	-0.005	-0.005	0.000	0.000	0.000	0.000
20	A	21	ALA	0	0.098	0.006	21.793	-0.001	-0.001	0.000	0.000	0.000	0.000
21	A	22	GLU	-1	-0.887	-0.950	20.165	-0.197	-0.197	0.000	0.000	0.000	0.000
22	A	23	ASN	0	-0.094	-0.062	19.118	0.000	0.000	0.000	0.000	0.000	0.000
23	A	24	LEU	0	-0.041	-0.020	16.739	0.021	0.021	0.000	0.000	0.000	0.000
24	A	25	LEU	0	-0.038	-0.003	14.677	-0.055	-0.055	0.000	0.000	0.000	0.000
25	A	26	LYS	1	0.960	0.968	11.175	-0.177	-0.177	0.000	0.000	0.000	0.000
26	A	27	ALA	0	0.030	0.013	11.495	0.041	0.041	0.000	0.000	0.000	0.000
27	A	28	ASP	-1	-0.903	-0.964	12.147	0.403	0.403	0.000	0.000	0.000	0.000
28	A	29	THR	0	-0.074	-0.025	14.176	0.024	0.024	0.000	0.000	0.000	0.000
29	A	30	TYR	0	-0.020	-0.006	16.292	0.011	0.011	0.000	0.000	0.000	0.000
30	A	31	ARG	1	0.909	0.966	19.168	-0.001	-0.001	0.000	0.000	0.000	0.000
31	A	32	LYS	1	0.944	0.994	19.834	-0.033	-0.033	0.000	0.000	0.000	0.000
32	A	33	TRP	0	-0.003	0.011	21.094	-0.013	-0.013	0.000	0.000	0.000	0.000
33	A	34	ARG	1	0.841	0.898	23.201	0.036	0.036	0.000	0.000	0.000	0.000
34	A	35	ALA	0	0.024	0.022	26.598	-0.006	-0.006	0.000	0.000	0.000	0.000
35	A	36	ALA	0	0.018	0.016	29.293	0.012	0.012	0.000	0.000	0.000	0.000
36	A	37	LYS	1	0.933	0.944	32.155	0.066	0.066	0.000	0.000	0.000	0.000
37	A	38	ALA	0	-0.024	0.011	33.167	-0.005	-0.005	0.000	0.000	0.000	0.000
38	A	39	GLY	0	0.027	-0.001	34.624	-0.001	-0.001	0.000	0.000	0.000	0.000
39	A	40	GLU	-1	-0.871	-0.904	31.930	-0.111	-0.111	0.000	0.000	0.000	0.000
40	A	41	LYS	1	0.921	0.939	31.832	0.103	0.103	0.000	0.000	0.000	0.000
41	A	42	THR	0	-0.068	-0.038	27.966	0.002	0.002	0.000	0.000	0.000	0.000
42	A	43	ILE	0	0.046	0.042	25.272	0.004	0.004	0.000	0.000	0.000	0.000
43	A	44	SER	0	-0.022	-0.023	23.448	-0.017	-0.017	0.000	0.000	0.000	0.000
44	A	45	VAL	0	0.060	0.037	19.542	0.022	0.022	0.000	0.000	0.000	0.000
45	A	46	VAL	0	-0.007	0.006	19.393	-0.033	-0.033	0.000	0.000	0.000	0.000
46	A	47	LEU	0	0.006	0.004	15.387	0.036	0.036	0.000	0.000	0.000	0.000
47	A	48	GLN	0	-0.030	-0.037	14.738	-0.002	-0.002	0.000	0.000	0.000	0.000
48	A	49	LEU	0	0.013	0.011	9.480	0.027	0.027	0.000	0.000	0.000	0.000
49	A	50	GLU	-1	-0.963	-0.975	10.223	-0.431	-0.431	0.000	0.000	0.000	0.000
50	A	51	LYS	1	0.922	0.955	7.266	1.814	1.814	0.000	0.000	0.000	0.000
51	A	52	GLU	-1	-0.922	-0.953	10.542	-0.980	-0.980	0.000	0.000	0.000	0.000
52	A	53	GLU	-1	-0.990	-1.020	5.145	-3.884	-3.872	-0.001	-0.001	-0.009	0.000
53	A	54	GLN	0	0.007	0.017	7.747	0.155	0.155	0.000	0.000	0.000	0.000
54	A	55	ILE	0	0.004	-0.009	6.720	-0.891	-0.891	0.000	0.000	0.000	0.000
55	A	56	HIS	0	-0.017	-0.007	5.077	0.282	0.282	0.000	0.000	0.000	0.000
56	A	57	SER	0	-0.037	-0.031	6.318	0.578	0.578	0.000	0.000	0.000	0.000
57	A	58	VAL	0	0.052	0.019	7.816	-0.361	-0.361	0.000	0.000	0.000	0.000
58	A	59	ASP	-1	-0.837	-0.910	9.648	0.381	0.381	0.000	0.000	0.000	0.000
59	A	60	ILE	0	0.015	0.004	11.940	-0.073	-0.073	0.000	0.000	0.000	0.000
60	A	61	GLY	0	0.039	0.011	15.417	0.070	0.070	0.000	0.000	0.000	0.000
61	A	62	ASN	0	-0.022	-0.010	17.830	-0.043	-0.043	0.000	0.000	0.000	0.000
62	A	63	ASP	-1	-0.784	-0.912	21.224	-0.005	-0.005	0.000	0.000	0.000	0.000
63	A	64	GLY	0	0.051	0.038	24.291	-0.007	-0.007	0.000	0.000	0.000	0.000
64	A	65	SER	0	-0.041	-0.006	24.012	-0.005	-0.005	0.000	0.000	0.000	0.000
65	A	66	ALA	0	-0.014	-0.018	25.903	0.011	0.011	0.000	0.000	0.000	0.000
66	A	67	PHE	0	-0.043	-0.042	24.508	0.008	0.008	0.000	0.000	0.000	0.000
67	A	68	VAL	0	0.029	0.009	18.987	0.003	0.003	0.000	0.000	0.000	0.000
68	A	69	GLU	-1	-0.912	-0.946	20.247	-0.270	-0.270	0.000	0.000	0.000	0.000
69	A	70	VAL	0	0.015	0.008	14.243	-0.007	-0.007	0.000	0.000	0.000	0.000
70	A	71	LEU	0	-0.019	-0.008	17.713	-0.006	-0.006	0.000	0.000	0.000	0.000
71	A	72	VAL	0	-0.002	-0.002	13.899	-0.043	-0.043	0.000	0.000	0.000	0.000
72	A	73	GLY	0	0.053	0.022	16.963	0.072	0.072	0.000	0.000	0.000	0.000
73	A	74	SER	0	0.064	0.022	17.022	-0.067	-0.067	0.000	0.000	0.000	0.000
74	A	75	SER	0	-0.096	-0.082	17.961	0.070	0.070	0.000	0.000	0.000	0.000
75	A	76	ALA	0	-0.020	-0.012	20.217	0.053	0.053	0.000	0.000	0.000	0.000
76	A	77	GLY	0	-0.012	-0.002	22.022	0.004	0.004	0.000	0.000	0.000	0.000
77	A	78	GLY	0	-0.040	-0.013	24.685	0.020	0.020	0.000	0.000	0.000	0.000
78	A	79	ALA	0	0.009	-0.002	22.502	-0.024	-0.024	0.000	0.000	0.000	0.000
79	A	80	GLY	0	-0.029	-0.024	24.505	0.021	0.021	0.000	0.000	0.000	0.000
80	A	81	GLU	-1	-0.938	-0.991	25.889	-0.248	-0.248	0.000	0.000	0.000	0.000
81	A	82	GLN	0	-0.079	-0.049	26.526	-0.023	-0.023	0.000	0.000	0.000	0.000
82	A	83	ASP	-1	-0.827	-0.892	24.325	-0.349	-0.349	0.000	0.000	0.000	0.000
83	A	84	TYR	0	-0.088	-0.029	19.525	-0.052	-0.052	0.000	0.000	0.000	0.000
84	A	85	GLU	-1	-0.815	-0.907	18.981	-0.416	-0.416	0.000	0.000	0.000	0.000
85	A	86	VAL	0	-0.003	-0.002	19.522	-0.031	-0.031	0.000	0.000	0.000	0.000
86	A	87	LEU	0	0.006	0.002	11.824	-0.014	-0.014	0.000	0.000	0.000	0.000
87	A	88	LEU	0	-0.029	-0.009	15.338	0.010	0.010	0.000	0.000	0.000	0.000
88	A	89	VAL	0	0.062	0.028	17.159	0.024	0.024	0.000	0.000	0.000	0.000
89	A	90	THR	0	0.035	0.019	20.567	0.008	0.008	0.000	0.000	0.000	0.000
90	A	91	SER	0	-0.042	-0.026	19.892	0.025	0.025	0.000	0.000	0.000	0.000
91	A	92	SER	0	-0.033	-0.022	21.974	0.008	0.008	0.000	0.000	0.000	0.000
92	A	93	PHE	0	-0.041	-0.026	17.988	0.014	0.014	0.000	0.000	0.000	0.000
93	A	94	MET	0	-0.014	0.022	23.852	0.016	0.016	0.000	0.000	0.000	0.000
94	A	95	SER	0	0.009	0.022	27.522	-0.011	-0.011	0.000	0.000	0.000	0.000
95	A	96	PRO	0	0.052	0.019	30.832	0.001	0.001	0.000	0.000	0.000	0.000
96	A	97	SER	0	0.032	0.006	33.954	-0.001	-0.001	0.000	0.000	0.000	0.000
97	A	98	GLU	-1	-0.827	-0.904	29.281	0.005	0.005	0.000	0.000	0.000	0.000
98	A	99	SER	0	-0.007	-0.023	30.933	-0.001	-0.001	0.000	0.000	0.000	0.000
99	A	100	ARG	1	0.919	0.960	32.482	0.027	0.027	0.000	0.000	0.000	0.000
100	A	101	SER	0	-0.016	0.003	35.580	0.003	0.003	0.000	0.000	0.000	0.000
101	A	102	GLY	0	0.054	0.037	32.453	0.004	0.004	0.000	0.000	0.000	0.000
102	A	103	SER	0	-0.042	-0.036	31.877	0.009	0.009	0.000	0.000	0.000	0.000
103	A	104	ASN	0	-0.053	-0.037	27.136	0.007	0.007	0.000	0.000	0.000	0.000
104	A	105	PRO	0	0.056	0.018	27.004	-0.006	-0.006	0.000	0.000	0.000	0.000
105	A	106	ASN	0	0.019	-0.004	23.529	-0.024	-0.024	0.000	0.000	0.000	0.000
106	A	107	ARG	1	0.821	0.936	21.655	-0.003	-0.003	0.000	0.000	0.000	0.000
107	A	108	VAL	0	0.062	0.024	15.766	-0.029	-0.029	0.000	0.000	0.000	0.000
108	A	109	ARG	1	0.813	0.914	16.939	0.085	0.085	0.000	0.000	0.000	0.000
109	A	110	MET	0	0.039	0.026	11.121	0.013	0.013	0.000	0.000	0.000	0.000
110	A	111	PHE	0	-0.076	-0.041	12.231	0.054	0.054	0.000	0.000	0.000	0.000
111	A	112	GLY	0	0.071	0.043	10.259	-0.107	-0.107	0.000	0.000	0.000	0.000
112	A	113	PRO	0	0.087	0.024	9.350	-0.035	-0.035	0.000	0.000	0.000	0.000
113	A	114	ASP	-1	-0.986	-0.987	11.776	-0.126	-0.126	0.000	0.000	0.000	0.000
114	A	115	LYS	1	0.885	0.936	14.596	0.128	0.128	0.000	0.000	0.000	0.000
115	A	116	LEU	0	-0.012	0.013	10.730	0.011	0.011	0.000	0.000	0.000	0.000
116	A	117	VAL	0	-0.046	-0.017	15.345	0.044	0.044	0.000	0.000	0.000	0.000
117	A	118	ARG	1	1.018	0.980	15.383	0.275	0.275	0.000	0.000	0.000	0.000
118	A	119	ALA	0	0.028	0.035	16.597	-0.037	-0.037	0.000	0.000	0.000	0.000
119	A	120	ALA	0	0.032	-0.001	16.853	-0.031	-0.031	0.000	0.000	0.000	0.000
120	A	121	ALA	0	-0.040	-0.021	12.526	-0.081	-0.081	0.000	0.000	0.000	0.000
121	A	122	GLU	-1	-0.955	-0.970	12.044	-0.810	-0.810	0.000	0.000	0.000	0.000
122	A	123	LYS	1	0.838	0.940	13.389	0.478	0.478	0.000	0.000	0.000	0.000
123	A	124	ARG	1	0.900	0.953	8.168	1.529	1.529	0.000	0.000	0.000	0.000
124	A	125	TRP	0	0.047	0.018	12.178	0.197	0.197	0.000	0.000	0.000	0.000
125	A	126	ASP	-1	-0.749	-0.859	12.116	-0.887	-0.887	0.000	0.000	0.000	0.000
126	A	127	ARG	1	0.866	0.972	13.878	0.527	0.527	0.000	0.000	0.000	0.000
127	A	128	VAL	0	0.023	0.012	12.654	-0.048	-0.048	0.000	0.000	0.000	0.000
128	A	129	LYS	1	0.943	0.991	16.072	0.362	0.362	0.000	0.000	0.000	0.000
129	A	130	ILE	0	0.016	0.013	15.585	-0.012	-0.012	0.000	0.000	0.000	0.000
130	A	131	VAL	0	-0.009	-0.008	19.387	0.036	0.036	0.000	0.000	0.000	0.000
131	A	132	CYS	0	0.003	0.024	22.249	0.005	0.005	0.000	0.000	0.000	0.000
132	A	133	SER	0	0.004	-0.012	24.268	0.009	0.009	0.000	0.000	0.000	0.000
133	A	134	GLN	0	0.038	0.008	27.552	0.006	0.006	0.000	0.000	0.000	0.000
134	A	135	PRO	0	-0.040	-0.038	30.136	0.004	0.004	0.000	0.000	0.000	0.000
135	A	136	TYR	0	-0.067	-0.029	30.623	0.005	0.005	0.000	0.000	0.000	0.000
136	A	137	SER	0	0.018	0.022	33.835	0.005	0.005	0.000	0.000	0.000	0.000
137	A	138	LYS	1	0.935	0.956	34.283	0.061	0.061	0.000	0.000	0.000	0.000
138	A	139	ASP	-1	-0.845	-0.910	36.596	-0.031	-0.031	0.000	0.000	0.000	0.000
139	A	140	SER	0	-0.057	-0.039	33.059	0.006	0.006	0.000	0.000	0.000	0.000
140	A	141	PRO	0	-0.036	-0.011	31.041	-0.006	-0.006	0.000	0.000	0.000	0.000
141	A	142	PHE	0	-0.020	-0.004	26.467	0.010	0.010	0.000	0.000	0.000	0.000
142	A	143	GLY	0	0.028	0.000	24.629	-0.010	-0.010	0.000	0.000	0.000	0.000
143	A	144	LEU	0	-0.013	0.000	17.727	0.001	0.001	0.000	0.000	0.000	0.000
144	A	145	SER	0	-0.044	-0.033	19.570	0.009	0.009	0.000	0.000	0.000	0.000
145	A	146	PHE	0	0.021	-0.003	13.119	0.024	0.024	0.000	0.000	0.000	0.000
146	A	147	VAL	0	0.008	-0.002	12.750	0.012	0.012	0.000	0.000	0.000	0.000
147	A	148	ARG	1	0.902	0.969	8.056	-0.297	-0.297	0.000	0.000	0.000	0.000
148	A	149	PHE	0	0.042	0.028	7.806	0.170	0.170	0.000	0.000	0.000	0.000
149	A	150	HIS	0	0.004	0.005	2.864	-0.415	0.242	0.047	-0.200	-0.505	0.000
150	A	151	SER	0	0.043	0.026	2.267	-2.026	0.766	1.772	-1.798	-2.767	-0.015
151	A	152	PRO	0	-0.036	-0.028	2.637	-4.703	-2.324	1.392	-1.682	-2.090	-0.021
152	A	153	PRO	0	-0.015	0.008	2.057	-4.329	-2.927	2.685	-1.409	-2.679	-0.008

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Interactive mode: IFIE and PIEDA for fragment #1(A:2:PRO)