FMO DATABASE

FMODB ID: YZ622

Calculation Name: 5FR7-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 5FR7

Chain ID: A

ChEMBL ID:

UniProt ID: D4I047

Base Structure: X-ray

Registration Date: 2023-06-21

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	144
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-1287055.634402
FMO2-HF: Nuclear repulsion	1229220.010202
FMO2-HF: Total energy	-57835.6242
FMO2-MP2: Total energy	-57998.122619

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:0:ALA)

Summations of interaction energy for fragment #1(A:0:ALA)

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.
0.022	2.419	0.171	-1.164	-1.405	0

Interaction energy analysis for fragmet #1(A:0:ALA)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : -0.008 / q_NPA : -0.020

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].
3	A	2	GLY	0	-0.018	0.005	2.542	-1.023	1.266	0.172	-1.161	-1.300
4	A	3	MET	0	-0.026	-0.008	4.302	0.409	0.517	-0.001	-0.003	-0.105
5	A	4	VAL	0	0.019	0.005	7.245	-0.105	-0.105	0.000	0.000	0.000
6	A	5	SER	0	-0.030	-0.022	10.180	0.055	0.055	0.000	0.000	0.000
7	A	6	LEU	0	-0.031	-0.003	11.663	-0.011	-0.011	0.000	0.000	0.000
8	A	7	VAL	0	0.020	0.008	15.012	-0.024	-0.024	0.000	0.000	0.000
9	A	8	VAL	0	0.014	0.006	18.538	0.024	0.024	0.000	0.000	0.000
10	A	9	PRO	0	-0.054	-0.009	20.085	-0.015	-0.015	0.000	0.000	0.000
11	A	10	ASP	-1	-0.773	-0.893	22.906	0.069	0.069	0.000	0.000	0.000
12	A	11	LEU	0	0.038	-0.010	26.059	0.001	0.001	0.000	0.000	0.000
13	A	12	ASP	-1	-0.815	-0.886	28.325	0.038	0.038	0.000	0.000	0.000
14	A	13	VAL	0	-0.120	-0.042	21.900	-0.006	-0.006	0.000	0.000	0.000
15	A	14	LEU	0	-0.014	-0.007	22.756	-0.003	-0.003	0.000	0.000	0.000
16	A	15	ARG	1	0.869	0.922	25.070	-0.047	-0.047	0.000	0.000	0.000
17	A	16	ARG	1	1.008	1.022	21.555	-0.029	-0.029	0.000	0.000	0.000
18	A	17	TRP	0	-0.048	-0.047	18.135	-0.009	-0.009	0.000	0.000	0.000
19	A	18	LEU	0	0.041	0.013	23.068	-0.003	-0.003	0.000	0.000	0.000
20	A	19	ASP	-1	-0.851	-0.915	25.461	0.015	0.015	0.000	0.000	0.000
21	A	20	GLN	0	-0.142	-0.078	22.182	-0.016	-0.016	0.000	0.000	0.000
22	A	21	GLN	0	-0.069	-0.029	21.342	-0.003	-0.003	0.000	0.000	0.000
23	A	22	SER	0	-0.061	-0.028	23.986	-0.003	-0.003	0.000	0.000	0.000
24	A	23	ILE	0	-0.020	0.002	24.359	0.002	0.002	0.000	0.000	0.000
25	A	24	THR	0	-0.001	-0.011	28.351	0.000	0.000	0.000	0.000	0.000
26	A	25	TRP	0	-0.010	-0.011	29.772	0.008	0.008	0.000	0.000	0.000
27	A	26	PHE	0	-0.028	-0.017	32.581	-0.005	-0.005	0.000	0.000	0.000
28	A	27	GLU	-1	-0.878	-0.960	34.752	0.045	0.045	0.000	0.000	0.000
29	A	28	CYS	0	-0.131	-0.034	37.179	0.003	0.003	0.000	0.000	0.000
30	A	29	ASP	-1	-0.884	-0.923	39.903	0.032	0.032	0.000	0.000	0.000
31	A	30	SER	0	-0.010	-0.009	42.240	0.001	0.001	0.000	0.000	0.000
32	A	32	GLN	0	0.046	0.018	34.329	0.002	0.002	0.000	0.000	0.000
33	A	33	ALA	0	0.030	0.024	32.393	0.002	0.002	0.000	0.000	0.000
34	A	34	LEU	0	-0.034	-0.012	28.502	-0.006	-0.006	0.000	0.000	0.000
35	A	35	HIS	1	0.765	0.824	31.423	-0.048	-0.048	0.000	0.000	0.000
36	A	36	LEU	0	0.014	0.002	28.078	-0.004	-0.004	0.000	0.000	0.000
37	A	37	PRO	0	0.019	0.013	32.427	0.001	0.001	0.000	0.000	0.000
38	A	38	HIS	0	-0.043	-0.036	28.173	-0.005	-0.005	0.000	0.000	0.000
39	A	39	MET	0	0.005	0.011	29.702	0.000	0.000	0.000	0.000	0.000
40	A	40	GLN	0	-0.020	-0.021	32.934	0.002	0.002	0.000	0.000	0.000
41	A	41	ASN	0	-0.054	-0.018	34.101	-0.003	-0.003	0.000	0.000	0.000
42	A	42	PHE	0	-0.044	-0.008	29.960	-0.001	-0.001	0.000	0.000	0.000
43	A	43	ASP	-1	-0.883	-0.944	35.599	0.036	0.036	0.000	0.000	0.000
44	A	44	GLY	0	-0.002	-0.013	37.705	0.004	0.004	0.000	0.000	0.000
45	A	45	VAL	0	-0.077	-0.029	34.168	0.002	0.002	0.000	0.000	0.000
46	A	46	PHE	0	-0.028	-0.020	37.382	-0.003	-0.003	0.000	0.000	0.000
47	A	47	ASP	-1	-0.817	-0.902	36.959	0.052	0.052	0.000	0.000	0.000
48	A	48	ALA	0	0.012	0.005	31.532	0.005	0.005	0.000	0.000	0.000
49	A	49	LYS	1	0.885	0.956	31.578	-0.078	-0.078	0.000	0.000	0.000
50	A	50	ILE	0	0.028	0.023	25.452	0.010	0.010	0.000	0.000	0.000
51	A	51	ASP	-1	-0.866	-0.935	28.713	0.073	0.073	0.000	0.000	0.000
52	A	52	LEU	0	-0.027	-0.020	25.174	0.012	0.012	0.000	0.000	0.000
53	A	53	MET	0	0.016	0.004	27.921	-0.010	-0.010	0.000	0.000	0.000
54	A	54	ASP	-1	-0.925	-0.944	28.175	0.113	0.113	0.000	0.000	0.000
55	A	55	GLY	0	-0.026	-0.019	25.046	0.009	0.009	0.000	0.000	0.000
56	A	56	VAL	0	-0.048	-0.032	23.390	0.023	0.023	0.000	0.000	0.000
57	A	57	ILE	0	0.029	0.031	21.036	-0.017	-0.017	0.000	0.000	0.000
58	A	58	LEU	0	-0.026	-0.034	24.217	0.017	0.017	0.000	0.000	0.000
59	A	59	PHE	0	0.027	0.009	24.546	-0.012	-0.012	0.000	0.000	0.000
60	A	60	SER	0	-0.030	-0.023	27.120	0.004	0.004	0.000	0.000	0.000
61	A	61	ALA	0	0.050	0.023	30.450	-0.006	-0.006	0.000	0.000	0.000
62	A	62	LEU	0	-0.043	-0.025	32.931	0.004	0.004	0.000	0.000	0.000
63	A	63	ALA	0	0.090	0.051	36.605	-0.003	-0.003	0.000	0.000	0.000
64	A	64	GLU	-1	-0.897	-0.957	39.132	0.044	0.044	0.000	0.000	0.000
65	A	65	VAL	0	0.002	0.003	41.440	-0.001	-0.001	0.000	0.000	0.000
66	A	66	LYS	1	0.920	0.961	43.923	-0.041	-0.041	0.000	0.000	0.000
67	A	67	PRO	0	0.069	0.018	47.169	0.002	0.002	0.000	0.000	0.000
68	A	68	THR	0	-0.073	-0.044	49.572	0.001	0.001	0.000	0.000	0.000
69	A	69	ALA	0	0.030	0.026	44.842	0.000	0.000	0.000	0.000	0.000
70	A	70	LEU	0	0.020	0.022	43.981	0.003	0.003	0.000	0.000	0.000
71	A	71	ILE	0	-0.022	-0.018	44.635	0.003	0.003	0.000	0.000	0.000
72	A	72	PRO	0	-0.026	-0.034	45.237	0.002	0.002	0.000	0.000	0.000
73	A	73	LEU	0	0.098	0.070	38.481	0.002	0.002	0.000	0.000	0.000
74	A	74	ALA	0	-0.041	-0.029	40.332	0.005	0.005	0.000	0.000	0.000
75	A	75	GLY	0	-0.053	-0.027	40.839	0.004	0.004	0.000	0.000	0.000
76	A	76	ASP	-1	-0.872	-0.924	38.482	0.068	0.068	0.000	0.000	0.000
77	A	77	LEU	0	-0.036	-0.017	36.165	0.006	0.006	0.000	0.000	0.000
78	A	78	SER	0	-0.021	-0.018	34.660	0.008	0.008	0.000	0.000	0.000
79	A	79	GLN	0	0.002	0.000	33.416	0.007	0.007	0.000	0.000	0.000
80	A	80	ILE	0	0.064	0.035	32.377	0.006	0.006	0.000	0.000	0.000
81	A	81	ASN	0	-0.048	-0.010	30.249	0.014	0.014	0.000	0.000	0.000
82	A	82	ALA	0	-0.047	-0.022	28.769	0.012	0.012	0.000	0.000	0.000
83	A	83	SER	0	-0.090	-0.044	28.320	0.007	0.007	0.000	0.000	0.000
84	A	84	SER	0	0.038	0.006	25.178	0.008	0.008	0.000	0.000	0.000
85	A	85	LEU	0	-0.053	-0.037	19.619	0.007	0.007	0.000	0.000	0.000
86	A	86	THR	0	-0.066	-0.048	19.590	0.016	0.016	0.000	0.000	0.000
87	A	87	VAL	0	-0.015	0.006	22.754	-0.006	-0.006	0.000	0.000	0.000
88	A	88	LYS	1	0.951	0.979	26.141	-0.141	-0.141	0.000	0.000	0.000
89	A	89	ALA	0	-0.007	-0.019	29.128	-0.006	-0.006	0.000	0.000	0.000
90	A	90	PHE	0	-0.044	-0.027	32.330	0.002	0.002	0.000	0.000	0.000
91	A	91	LEU	0	0.034	0.008	36.026	-0.002	-0.002	0.000	0.000	0.000
92	A	92	ASP	-1	-0.880	-0.943	39.347	0.065	0.065	0.000	0.000	0.000
93	A	93	ILE	0	-0.040	-0.031	41.054	-0.003	-0.003	0.000	0.000	0.000
94	A	94	GLN	0	0.019	0.026	43.278	0.000	0.000	0.000	0.000	0.000
95	A	95	ASP	-1	-0.951	-0.975	47.470	0.042	0.042	0.000	0.000	0.000
96	A	96	ASP	-1	-0.961	-0.983	49.226	0.040	0.040	0.000	0.000	0.000
97	A	97	ASN	0	-0.090	-0.044	46.876	0.001	0.001	0.000	0.000	0.000
98	A	98	LEU	0	0.008	0.009	46.620	0.000	0.000	0.000	0.000	0.000
99	A	99	PRO	0	-0.029	-0.002	44.427	0.002	0.002	0.000	0.000	0.000
100	A	100	LYS	1	0.920	0.962	39.923	-0.059	-0.059	0.000	0.000	0.000
101	A	101	LEU	0	0.002	0.012	36.124	0.002	0.002	0.000	0.000	0.000
102	A	102	ILE	0	-0.034	-0.017	33.072	-0.002	-0.002	0.000	0.000	0.000
103	A	103	VAL	0	0.035	0.025	29.853	0.005	0.005	0.000	0.000	0.000
104	A	104	CYS	0	-0.070	-0.045	28.591	-0.002	-0.002	0.000	0.000	0.000
105	A	105	GLN	0	0.104	0.064	20.045	-0.010	-0.010	0.000	0.000	0.000
106	A	106	SER	0	-0.049	-0.029	23.579	-0.009	-0.009	0.000	0.000	0.000
107	A	107	LEU	0	0.020	0.016	16.576	0.025	0.025	0.000	0.000	0.000
108	A	108	SER	0	-0.023	-0.021	19.385	-0.028	-0.028	0.000	0.000	0.000
109	A	109	ALA	0	0.049	0.014	18.483	0.028	0.028	0.000	0.000	0.000
110	A	110	ALA	0	-0.004	-0.004	20.086	-0.004	-0.004	0.000	0.000	0.000
111	A	111	ALA	0	-0.037	-0.005	16.932	-0.011	-0.011	0.000	0.000	0.000
112	A	112	GLY	0	-0.011	-0.005	16.665	0.013	0.013	0.000	0.000	0.000
113	A	113	LEU	0	-0.013	-0.008	14.667	0.041	0.041	0.000	0.000	0.000
114	A	114	THR	0	0.006	-0.002	10.656	-0.053	-0.053	0.000	0.000	0.000
115	A	115	TYR	0	0.050	0.016	14.003	0.018	0.018	0.000	0.000	0.000
116	A	116	GLY	0	0.013	-0.003	12.998	0.000	0.000	0.000	0.000	0.000
117	A	117	GLN	0	0.024	0.001	10.463	-0.051	-0.051	0.000	0.000	0.000
118	A	118	PHE	0	0.051	0.025	14.034	0.008	0.008	0.000	0.000	0.000
119	A	119	VAL	0	0.016	0.014	16.561	-0.006	-0.006	0.000	0.000	0.000
120	A	120	HIS	0	-0.020	-0.010	14.490	-0.035	-0.035	0.000	0.000	0.000
121	A	121	PHE	0	0.036	0.026	16.614	-0.002	-0.002	0.000	0.000	0.000
122	A	122	MET	0	-0.027	0.017	18.907	-0.008	-0.008	0.000	0.000	0.000
123	A	123	LYS	1	0.929	0.956	18.505	-0.064	-0.064	0.000	0.000	0.000
124	A	124	GLU	-1	-0.857	-0.909	17.975	0.307	0.307	0.000	0.000	0.000
125	A	125	SER	0	-0.007	-0.030	20.815	-0.006	-0.006	0.000	0.000	0.000
126	A	126	GLU	-1	-0.855	-0.913	23.649	0.054	0.054	0.000	0.000	0.000
127	A	127	GLU	-1	-0.970	-0.982	21.744	0.115	0.115	0.000	0.000	0.000
128	A	128	GLN	0	0.040	0.032	23.135	-0.007	-0.007	0.000	0.000	0.000
129	A	129	ILE	0	-0.023	-0.021	25.997	-0.007	-0.007	0.000	0.000	0.000
130	A	130	SER	0	-0.042	-0.019	28.471	-0.008	-0.008	0.000	0.000	0.000
131	A	131	MET	0	0.020	0.013	26.930	-0.004	-0.004	0.000	0.000	0.000
132	A	132	ILE	0	-0.011	0.012	29.769	-0.006	-0.006	0.000	0.000	0.000
133	A	133	VAL	0	-0.027	-0.018	32.346	-0.006	-0.006	0.000	0.000	0.000
134	A	134	MET	0	0.013	-0.005	33.498	-0.005	-0.005	0.000	0.000	0.000
135	A	135	GLU	-1	-0.934	-0.947	34.115	0.069	0.069	0.000	0.000	0.000
136	A	136	ALA	0	-0.018	-0.014	36.128	-0.004	-0.004	0.000	0.000	0.000
137	A	137	PHE	0	-0.014	-0.018	38.374	-0.004	-0.004	0.000	0.000	0.000
138	A	138	ALA	0	0.000	-0.002	38.950	-0.004	-0.004	0.000	0.000	0.000
139	A	139	ASN	0	-0.037	0.000	38.885	-0.005	-0.005	0.000	0.000	0.000
140	A	140	HIS	0	-0.073	-0.038	42.117	-0.001	-0.001	0.000	0.000	0.000
141	A	141	LEU	0	-0.003	-0.016	40.346	-0.002	-0.002	0.000	0.000	0.000
142	A	142	LEU	0	-0.032	-0.007	38.663	0.001	0.001	0.000	0.000	0.000
143	A	143	MET	0	-0.086	-0.039	43.407	-0.004	-0.004	0.000	0.000	0.000
144	A	144	ILE	0	0.020	0.017	43.531	0.001	0.001	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:0:ALA)