FMO DATABASE

FMODB ID: 229QR

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

Total energy (hartree)

FMO2-HF: Electronic energy	-1448554.318799
FMO2-HF: Nuclear repulsion	1389540.946274
FMO2-HF: Total energy	-59013.372525
FMO2-MP2: Total energy	-59185.16001

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.
-12.715	-3.359	4.258	-5.385	-8.23	-0.037

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 : 0.025 / q_NPA : -0.002

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	-0.025	-0.021	3.805	-1.098	0.343	-0.011	-0.555	-0.875	0.003
4	A	5	ARG	1	0.853	0.923	5.736	0.996	0.996	0.000	0.000	0.000	0.000
5	A	6	LEU	0	-0.025	-0.012	8.495	-0.108	-0.108	0.000	0.000	0.000	0.000
6	A	7	ARG	1	0.932	0.970	12.022	0.456	0.456	0.000	0.000	0.000	0.000
7	A	8	HIS	0	0.008	-0.011	14.778	0.051	0.051	0.000	0.000	0.000	0.000
8	A	9	VAL	0	0.055	0.034	17.659	-0.053	-0.053	0.000	0.000	0.000	0.000
9	A	10	VAL	0	-0.083	-0.041	19.284	0.019	0.019	0.000	0.000	0.000	0.000
10	A	11	SER	0	0.007	-0.004	21.902	0.019	0.019	0.000	0.000	0.000	0.000
11	A	12	CYS	0	-0.002	0.012	23.282	-0.009	-0.009	0.000	0.000	0.000	0.000
12	A	13	SER	0	-0.035	-0.012	25.645	0.008	0.008	0.000	0.000	0.000	0.000
13	A	14	SER	0	-0.030	-0.056	27.639	0.013	0.013	0.000	0.000	0.000	0.000
14	A	15	GLN	0	0.017	0.011	25.705	-0.018	-0.018	0.000	0.000	0.000	0.000
15	A	16	ASP	-1	-0.773	-0.857	28.028	-0.024	-0.024	0.000	0.000	0.000	0.000
16	A	17	SER	0	-0.082	-0.036	28.687	-0.003	-0.003	0.000	0.000	0.000	0.000
17	A	18	THR	0	-0.055	-0.037	28.600	0.004	0.004	0.000	0.000	0.000	0.000
18	A	19	HIS	0	-0.017	-0.026	25.404	0.001	0.001	0.000	0.000	0.000	0.000
19	A	20	CYS	0	-0.026	-0.014	24.538	-0.005	-0.005	0.000	0.000	0.000	0.000
20	A	21	ALA	0	0.109	0.019	21.942	0.003	0.003	0.000	0.000	0.000	0.000
21	A	22	GLU	-1	-0.850	-0.933	20.181	-0.157	-0.157	0.000	0.000	0.000	0.000
22	A	23	ASN	0	-0.080	-0.043	19.130	0.006	0.006	0.000	0.000	0.000	0.000
23	A	24	LEU	0	-0.028	-0.011	16.717	0.024	0.024	0.000	0.000	0.000	0.000
24	A	25	LEU	0	-0.054	-0.009	14.812	-0.043	-0.043	0.000	0.000	0.000	0.000
25	A	26	LYS	1	0.827	0.893	9.043	-0.308	-0.308	0.000	0.000	0.000	0.000
26	A	27	ALA	0	0.030	0.013	11.427	0.031	0.031	0.000	0.000	0.000	0.000
27	A	28	ASP	-1	-0.857	-0.928	11.504	0.371	0.371	0.000	0.000	0.000	0.000
28	A	29	THR	0	-0.031	-0.014	14.162	0.014	0.014	0.000	0.000	0.000	0.000
29	A	30	TYR	0	-0.023	-0.003	16.422	0.007	0.007	0.000	0.000	0.000	0.000
30	A	31	ARG	1	0.884	0.953	19.147	-0.023	-0.023	0.000	0.000	0.000	0.000
31	A	32	LYS	1	0.872	0.944	19.801	-0.055	-0.055	0.000	0.000	0.000	0.000
32	A	33	TRP	0	-0.013	0.001	21.430	-0.013	-0.013	0.000	0.000	0.000	0.000
33	A	34	ARG	1	0.815	0.860	23.201	0.007	0.007	0.000	0.000	0.000	0.000
34	A	35	ALA	0	0.017	0.022	26.644	-0.007	-0.007	0.000	0.000	0.000	0.000
35	A	36	ALA	0	0.016	0.018	29.348	0.011	0.011	0.000	0.000	0.000	0.000
36	A	37	LYS	1	0.858	0.910	32.163	0.050	0.050	0.000	0.000	0.000	0.000
37	A	38	ALA	0	0.011	0.023	33.224	-0.004	-0.004	0.000	0.000	0.000	0.000
38	A	39	GLY	0	0.030	0.002	34.662	-0.001	-0.001	0.000	0.000	0.000	0.000
39	A	40	GLU	-1	-0.817	-0.866	32.000	-0.084	-0.084	0.000	0.000	0.000	0.000
40	A	41	LYS	1	0.935	0.955	31.883	0.083	0.083	0.000	0.000	0.000	0.000
41	A	42	THR	0	-0.018	-0.026	28.150	0.002	0.002	0.000	0.000	0.000	0.000
42	A	43	ILE	0	-0.016	0.015	25.439	0.002	0.002	0.000	0.000	0.000	0.000
43	A	44	SER	0	-0.019	-0.021	23.382	-0.014	-0.014	0.000	0.000	0.000	0.000
44	A	45	VAL	0	0.066	0.042	19.722	0.018	0.018	0.000	0.000	0.000	0.000
45	A	46	VAL	0	0.012	0.011	19.607	-0.029	-0.029	0.000	0.000	0.000	0.000
46	A	47	LEU	0	-0.001	0.001	15.346	0.029	0.029	0.000	0.000	0.000	0.000
47	A	48	GLN	0	-0.032	-0.022	15.216	0.006	0.006	0.000	0.000	0.000	0.000
48	A	49	LEU	0	0.011	0.005	9.690	0.021	0.021	0.000	0.000	0.000	0.000
49	A	50	GLU	-1	-0.887	-0.943	10.237	-0.420	-0.420	0.000	0.000	0.000	0.000
50	A	51	LYS	1	0.846	0.900	6.719	2.088	2.088	0.000	0.000	0.000	0.000
51	A	52	GLU	-1	-0.852	-0.911	10.676	-0.996	-0.996	0.000	0.000	0.000	0.000
52	A	53	GLU	-1	-0.856	-0.921	5.831	-3.032	-3.032	0.000	0.000	0.000	0.000
53	A	54	GLN	0	-0.005	0.005	7.887	0.144	0.144	0.000	0.000	0.000	0.000
54	A	55	ILE	0	-0.021	-0.020	6.898	-0.800	-0.800	0.000	0.000	0.000	0.000
55	A	56	HIS	0	0.003	0.001	5.060	0.197	0.197	0.000	0.000	0.000	0.000
56	A	57	SER	0	-0.022	-0.023	6.534	0.593	0.593	0.000	0.000	0.000	0.000
57	A	58	VAL	0	0.022	0.002	7.857	-0.324	-0.324	0.000	0.000	0.000	0.000
58	A	59	ASP	-1	-0.820	-0.882	9.719	0.578	0.578	0.000	0.000	0.000	0.000
59	A	60	ILE	0	0.024	0.010	12.020	-0.075	-0.075	0.000	0.000	0.000	0.000
60	A	61	GLY	0	0.048	0.020	15.493	0.062	0.062	0.000	0.000	0.000	0.000
61	A	62	ASN	0	-0.012	-0.012	17.916	-0.044	-0.044	0.000	0.000	0.000	0.000
62	A	63	ASP	-1	-0.742	-0.857	21.305	0.032	0.032	0.000	0.000	0.000	0.000
63	A	64	GLY	0	0.054	0.038	24.372	-0.008	-0.008	0.000	0.000	0.000	0.000
64	A	65	SER	0	-0.030	-0.001	24.085	-0.009	-0.009	0.000	0.000	0.000	0.000
65	A	66	ALA	0	-0.024	-0.015	25.975	0.011	0.011	0.000	0.000	0.000	0.000
66	A	67	PHE	0	-0.035	-0.039	24.557	0.008	0.008	0.000	0.000	0.000	0.000
67	A	68	VAL	0	0.025	0.005	19.107	0.001	0.001	0.000	0.000	0.000	0.000
68	A	69	GLU	-1	-0.832	-0.887	20.247	-0.202	-0.202	0.000	0.000	0.000	0.000
69	A	70	VAL	0	0.013	0.008	14.372	-0.007	-0.007	0.000	0.000	0.000	0.000
70	A	71	LEU	0	-0.010	-0.005	17.735	-0.005	-0.005	0.000	0.000	0.000	0.000
71	A	72	VAL	0	0.002	0.002	13.798	-0.035	-0.035	0.000	0.000	0.000	0.000
72	A	73	GLY	0	0.060	0.027	16.945	0.064	0.064	0.000	0.000	0.000	0.000
73	A	74	SER	0	0.025	-0.002	17.218	-0.066	-0.066	0.000	0.000	0.000	0.000
74	A	75	SER	0	-0.095	-0.085	18.256	0.066	0.066	0.000	0.000	0.000	0.000
75	A	76	ALA	0	-0.026	-0.014	20.349	0.047	0.047	0.000	0.000	0.000	0.000
76	A	77	GLY	0	-0.007	-0.001	22.173	0.004	0.004	0.000	0.000	0.000	0.000
77	A	78	GLY	0	-0.036	-0.011	24.876	0.018	0.018	0.000	0.000	0.000	0.000
78	A	79	ALA	0	0.005	-0.001	22.682	-0.022	-0.022	0.000	0.000	0.000	0.000
79	A	80	GLY	0	-0.022	-0.026	24.693	0.020	0.020	0.000	0.000	0.000	0.000
80	A	81	GLU	-1	-0.861	-0.958	25.974	-0.230	-0.230	0.000	0.000	0.000	0.000
81	A	82	GLN	0	-0.083	-0.045	26.511	-0.013	-0.013	0.000	0.000	0.000	0.000
82	A	83	ASP	-1	-0.831	-0.897	24.629	-0.309	-0.309	0.000	0.000	0.000	0.000
83	A	84	TYR	0	-0.062	-0.019	19.885	-0.044	-0.044	0.000	0.000	0.000	0.000
84	A	85	GLU	-1	-0.769	-0.863	19.159	-0.400	-0.400	0.000	0.000	0.000	0.000
85	A	86	VAL	0	0.008	0.005	19.509	-0.024	-0.024	0.000	0.000	0.000	0.000
86	A	87	LEU	0	0.021	0.014	11.836	-0.015	-0.015	0.000	0.000	0.000	0.000
87	A	88	LEU	0	-0.045	-0.019	15.240	0.012	0.012	0.000	0.000	0.000	0.000
88	A	89	VAL	0	0.052	0.019	17.179	0.017	0.017	0.000	0.000	0.000	0.000
89	A	90	THR	0	-0.028	-0.032	20.601	0.019	0.019	0.000	0.000	0.000	0.000
90	A	91	SER	0	-0.043	-0.016	20.004	0.025	0.025	0.000	0.000	0.000	0.000
91	A	92	SER	0	-0.042	-0.024	22.024	0.007	0.007	0.000	0.000	0.000	0.000
92	A	93	PHE	0	-0.008	-0.008	18.142	0.017	0.017	0.000	0.000	0.000	0.000
93	A	94	MET	0	-0.025	0.016	23.926	0.015	0.015	0.000	0.000	0.000	0.000
94	A	95	SER	0	0.002	0.009	27.598	-0.011	-0.011	0.000	0.000	0.000	0.000
95	A	96	PRO	0	0.045	0.010	30.905	0.000	0.000	0.000	0.000	0.000	0.000
96	A	97	SER	0	0.025	0.008	34.024	-0.002	-0.002	0.000	0.000	0.000	0.000
97	A	98	GLU	-1	-0.718	-0.802	29.619	0.035	0.035	0.000	0.000	0.000	0.000
98	A	99	SER	0	-0.003	-0.021	31.019	-0.001	-0.001	0.000	0.000	0.000	0.000
99	A	100	ARG	1	0.923	0.967	32.559	0.009	0.009	0.000	0.000	0.000	0.000
100	A	101	SER	0	-0.029	-0.015	35.635	0.002	0.002	0.000	0.000	0.000	0.000
101	A	102	GLY	0	0.044	0.027	32.538	0.003	0.003	0.000	0.000	0.000	0.000
102	A	103	SER	0	-0.036	-0.018	31.966	0.009	0.009	0.000	0.000	0.000	0.000
103	A	104	ASN	0	-0.081	-0.056	27.251	0.005	0.005	0.000	0.000	0.000	0.000
104	A	105	PRO	0	0.037	0.016	27.091	-0.004	-0.004	0.000	0.000	0.000	0.000
105	A	106	ASN	0	0.018	-0.009	23.454	-0.017	-0.017	0.000	0.000	0.000	0.000
106	A	107	ARG	1	0.779	0.874	21.871	-0.031	-0.031	0.000	0.000	0.000	0.000
107	A	108	VAL	0	0.055	0.021	15.927	-0.026	-0.026	0.000	0.000	0.000	0.000
108	A	109	ARG	1	0.835	0.921	17.022	0.030	0.030	0.000	0.000	0.000	0.000
109	A	110	MET	0	0.027	0.017	11.098	0.016	0.016	0.000	0.000	0.000	0.000
110	A	111	PHE	0	-0.065	-0.037	12.292	0.024	0.024	0.000	0.000	0.000	0.000
111	A	112	GLY	0	0.084	0.051	10.304	-0.080	-0.080	0.000	0.000	0.000	0.000
112	A	113	PRO	0	0.089	0.023	9.247	-0.029	-0.029	0.000	0.000	0.000	0.000
113	A	114	ASP	-1	-0.900	-0.934	11.783	-0.055	-0.055	0.000	0.000	0.000	0.000
114	A	115	LYS	1	0.807	0.889	14.624	0.041	0.041	0.000	0.000	0.000	0.000
115	A	116	LEU	0	-0.001	0.022	10.843	0.006	0.006	0.000	0.000	0.000	0.000
116	A	117	VAL	0	-0.042	-0.026	15.356	0.035	0.035	0.000	0.000	0.000	0.000
117	A	118	ARG	1	0.971	0.966	15.342	0.215	0.215	0.000	0.000	0.000	0.000
118	A	119	ALA	0	0.022	0.031	16.848	-0.035	-0.035	0.000	0.000	0.000	0.000
119	A	120	ALA	0	0.058	0.021	16.995	-0.033	-0.033	0.000	0.000	0.000	0.000
120	A	121	ALA	0	-0.045	-0.032	12.402	-0.079	-0.079	0.000	0.000	0.000	0.000
121	A	122	GLU	-1	-0.941	-0.959	12.282	-0.726	-0.726	0.000	0.000	0.000	0.000
122	A	123	LYS	1	0.774	0.884	13.574	0.406	0.406	0.000	0.000	0.000	0.000
123	A	124	ARG	1	0.777	0.878	8.785	1.314	1.314	0.000	0.000	0.000	0.000
124	A	125	TRP	0	0.027	0.010	12.330	0.191	0.191	0.000	0.000	0.000	0.000
125	A	126	ASP	-1	-0.729	-0.827	12.296	-0.776	-0.776	0.000	0.000	0.000	0.000
126	A	127	ARG	1	0.876	0.969	14.049	0.472	0.472	0.000	0.000	0.000	0.000
127	A	128	VAL	0	0.014	0.003	12.623	-0.043	-0.043	0.000	0.000	0.000	0.000
128	A	129	LYS	1	0.851	0.952	16.089	0.308	0.308	0.000	0.000	0.000	0.000
129	A	130	ILE	0	0.021	0.018	15.691	-0.008	-0.008	0.000	0.000	0.000	0.000
130	A	131	VAL	0	-0.006	-0.005	19.416	0.029	0.029	0.000	0.000	0.000	0.000
131	A	132	CYS	0	0.005	0.024	22.312	0.000	0.000	0.000	0.000	0.000	0.000
132	A	133	SER	0	0.011	-0.005	24.317	0.004	0.004	0.000	0.000	0.000	0.000
133	A	134	GLN	0	0.028	0.005	27.610	0.006	0.006	0.000	0.000	0.000	0.000
134	A	135	PRO	0	-0.016	-0.020	30.235	0.002	0.002	0.000	0.000	0.000	0.000
135	A	136	TYR	0	-0.074	-0.042	30.820	0.003	0.003	0.000	0.000	0.000	0.000
136	A	137	SER	0	-0.015	-0.022	33.889	0.005	0.005	0.000	0.000	0.000	0.000
137	A	138	LYS	1	0.920	0.951	34.348	0.038	0.038	0.000	0.000	0.000	0.000
138	A	139	ASP	-1	-0.809	-0.872	36.663	-0.015	-0.015	0.000	0.000	0.000	0.000
139	A	140	SER	0	-0.032	-0.018	33.066	0.005	0.005	0.000	0.000	0.000	0.000
140	A	141	PRO	0	-0.020	-0.006	30.910	-0.005	-0.005	0.000	0.000	0.000	0.000
141	A	142	PHE	0	-0.048	-0.017	26.857	0.010	0.010	0.000	0.000	0.000	0.000
142	A	143	GLY	0	0.051	0.010	24.692	-0.011	-0.011	0.000	0.000	0.000	0.000
143	A	144	LEU	0	-0.034	-0.003	17.819	0.004	0.004	0.000	0.000	0.000	0.000
144	A	145	SER	0	-0.022	-0.024	19.549	0.011	0.011	0.000	0.000	0.000	0.000
145	A	146	PHE	0	-0.003	-0.014	12.694	0.020	0.020	0.000	0.000	0.000	0.000
146	A	147	VAL	0	0.023	0.005	12.687	0.008	0.008	0.000	0.000	0.000	0.000
147	A	148	ARG	1	0.862	0.937	8.099	-0.447	-0.447	0.000	0.000	0.000	0.000
148	A	149	PHE	0	0.048	0.031	7.849	0.142	0.142	0.000	0.000	0.000	0.000
149	A	150	HIS	0	-0.001	-0.005	2.982	-0.182	0.414	0.031	-0.182	-0.445	0.000
150	A	151	SER	0	0.028	0.019	2.414	-1.817	1.346	1.309	-1.801	-2.671	-0.013
151	A	152	PRO	0	-0.009	-0.018	2.586	-4.630	-2.079	0.885	-1.629	-1.808	-0.020
152	A	153	PRO	0	-0.022	0.007	2.103	-4.221	-2.616	2.044	-1.218	-2.431	-0.007

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