FMO DATABASE

FMODB ID: 66MGZ

Calculation Name: 4JHY-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 4JHY

Chain ID: A

ChEMBL ID:

UniProt ID: A6LHZ0

Base Structure: X-ray

Registration Date: 2023-06-20

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	155
LigandCharge	CYM=-1
Software	ABINIT-MP - Open Ver. 1 Rev. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-1516667.734633
FMO2-HF: Nuclear repulsion	1454006.298038
FMO2-HF: Total energy	-62661.436596
FMO2-MP2: Total energy	-62843.097495

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:27:GLU)

Summations of interaction energy for fragment #1(A:27:GLU)

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.
43.793	37.892	20.001	-8.053	-6.044	-0.002

Interaction energy analysis for fragmet #1(A:27:GLU)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : -1 / q_Mulliken : -0.965 / q_NPA : -0.992

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	29	ALA	0	0.030	0.007	3.477	-8.091	-5.861	-0.002	-1.085	-1.142	0.004
4	A	30	PRO	0	0.007	0.039	4.669	1.438	1.732	-0.001	-0.036	-0.257	0.000
5	A	31	MET	0	-0.016	-0.030	6.071	-2.991	-2.991	0.000	0.000	0.000	0.000
6	A	32	LYS	1	0.791	0.847	9.426	-18.027	-18.027	0.000	0.000	0.000	0.000
7	A	33	ASN	0	-0.039	-0.030	12.738	-0.335	-0.335	0.000	0.000	0.000	0.000
8	A	34	GLY	0	0.012	0.012	14.317	-0.827	-0.827	0.000	0.000	0.000	0.000
9	A	35	LYS	1	0.807	0.898	14.230	-15.760	-15.760	0.000	0.000	0.000	0.000
10	A	36	VAL	0	0.005	0.008	9.408	0.952	0.952	0.000	0.000	0.000	0.000
11	A	37	CYM	-1	-0.881	-0.874	10.139	16.818	16.818	0.000	0.000	0.000	0.000
12	A	38	TYR	0	0.014	0.016	6.810	0.716	0.716	0.000	0.000	0.000	0.000
13	A	39	SER	0	-0.039	-0.049	9.638	-2.034	-2.034	0.000	0.000	0.000	0.000
14	A	40	ASP	-1	-0.846	-0.912	10.594	21.735	21.735	0.000	0.000	0.000	0.000
15	A	41	ASP	-1	-0.887	-0.931	13.109	13.918	13.918	0.000	0.000	0.000	0.000
16	A	42	VAL	0	0.013	0.025	16.259	0.293	0.293	0.000	0.000	0.000	0.000
17	A	43	GLU	-1	-0.914	-0.965	18.502	11.668	11.668	0.000	0.000	0.000	0.000
18	A	44	ILE	0	-0.045	-0.042	21.525	0.358	0.358	0.000	0.000	0.000	0.000
19	A	45	GLU	-1	-0.897	-0.959	24.403	10.913	10.913	0.000	0.000	0.000	0.000
20	A	46	ASN	0	-0.042	-0.007	27.404	-0.381	-0.381	0.000	0.000	0.000	0.000
21	A	47	THR	0	0.036	0.035	28.235	-0.309	-0.309	0.000	0.000	0.000	0.000
22	A	48	SER	0	0.013	0.004	29.496	0.235	0.235	0.000	0.000	0.000	0.000
23	A	49	LYS	1	0.828	0.891	28.221	-9.956	-9.956	0.000	0.000	0.000	0.000
24	A	50	LEU	0	-0.077	-0.041	29.278	0.165	0.165	0.000	0.000	0.000	0.000
25	A	51	GLU	-1	-0.794	-0.895	31.159	9.119	9.119	0.000	0.000	0.000	0.000
26	A	52	ILE	0	0.053	0.035	24.459	0.165	0.165	0.000	0.000	0.000	0.000
27	A	53	PHE	0	-0.036	-0.029	26.552	0.107	0.107	0.000	0.000	0.000	0.000
28	A	54	ASN	0	-0.101	-0.078	28.031	0.076	0.076	0.000	0.000	0.000	0.000
29	A	55	ALA	0	0.050	0.044	27.344	-0.093	-0.093	0.000	0.000	0.000	0.000
30	A	56	ILE	0	0.079	0.042	22.118	0.040	0.040	0.000	0.000	0.000	0.000
31	A	57	ASN	0	0.003	-0.003	25.486	-0.038	-0.038	0.000	0.000	0.000	0.000
32	A	58	ALA	0	-0.068	-0.035	28.132	-0.165	-0.165	0.000	0.000	0.000	0.000
33	A	59	TRP	0	-0.004	0.000	20.201	-0.484	-0.484	0.000	0.000	0.000	0.000
34	A	60	ALA	0	0.037	0.026	24.890	0.041	0.041	0.000	0.000	0.000	0.000
35	A	61	LYS	1	0.834	0.899	25.955	-9.570	-9.570	0.000	0.000	0.000	0.000
36	A	62	LYS	1	0.926	0.968	25.608	-11.581	-11.581	0.000	0.000	0.000	0.000
37	A	63	SER	0	-0.020	-0.014	24.055	-0.118	-0.118	0.000	0.000	0.000	0.000
38	A	64	TYR	0	0.034	0.022	20.166	0.181	0.181	0.000	0.000	0.000	0.000
39	A	65	GLY	0	-0.032	-0.011	26.959	-0.240	-0.240	0.000	0.000	0.000	0.000
40	A	66	LYS	1	0.912	0.944	30.545	-8.781	-8.781	0.000	0.000	0.000	0.000
41	A	67	ASP	-1	-0.806	-0.857	26.849	10.702	10.702	0.000	0.000	0.000	0.000
42	A	68	VAL	0	-0.020	-0.018	29.726	0.140	0.140	0.000	0.000	0.000	0.000
43	A	69	PHE	0	-0.027	-0.014	31.873	-0.113	-0.113	0.000	0.000	0.000	0.000
44	A	70	LEU	0	-0.072	-0.025	26.525	0.014	0.014	0.000	0.000	0.000	0.000
45	A	71	SER	0	0.014	-0.013	25.339	0.703	0.703	0.000	0.000	0.000	0.000
46	A	72	ASN	0	-0.095	-0.045	26.270	-0.657	-0.657	0.000	0.000	0.000	0.000
47	A	73	VAL	0	0.049	0.019	26.182	0.415	0.415	0.000	0.000	0.000	0.000
48	A	74	ASN	0	-0.052	-0.027	27.409	-0.379	-0.379	0.000	0.000	0.000	0.000
49	A	75	SER	0	0.054	0.022	28.019	0.374	0.374	0.000	0.000	0.000	0.000
50	A	76	ASN	0	-0.051	-0.024	29.088	-0.528	-0.528	0.000	0.000	0.000	0.000
51	A	77	LYS	1	1.019	0.988	30.699	-8.155	-8.155	0.000	0.000	0.000	0.000
52	A	78	ASN	0	-0.028	-0.003	32.765	-0.002	-0.002	0.000	0.000	0.000	0.000
53	A	79	LYS	1	0.988	1.000	28.966	-9.606	-9.606	0.000	0.000	0.000	0.000
54	A	80	GLY	0	0.037	0.040	29.016	0.211	0.211	0.000	0.000	0.000	0.000
55	A	81	THR	0	-0.011	0.000	25.027	0.221	0.221	0.000	0.000	0.000	0.000
56	A	82	ILE	0	-0.025	-0.018	24.121	-0.516	-0.516	0.000	0.000	0.000	0.000
57	A	83	PHE	0	-0.046	-0.017	23.282	0.438	0.438	0.000	0.000	0.000	0.000
58	A	84	VAL	0	0.031	0.012	21.758	-0.505	-0.505	0.000	0.000	0.000	0.000
59	A	85	SER	0	-0.092	-0.049	22.077	0.268	0.268	0.000	0.000	0.000	0.000
60	A	86	SER	0	0.012	-0.001	21.308	-0.324	-0.324	0.000	0.000	0.000	0.000
61	A	87	LYS	1	0.891	0.943	21.702	-10.851	-10.851	0.000	0.000	0.000	0.000
62	A	88	VAL	0	0.043	0.035	19.718	-0.490	-0.490	0.000	0.000	0.000	0.000
63	A	89	GLU	-1	-0.800	-0.909	21.359	12.159	12.159	0.000	0.000	0.000	0.000
64	A	90	LEU	0	0.009	0.007	14.046	-0.112	-0.112	0.000	0.000	0.000	0.000
65	A	91	LEU	0	0.021	-0.004	18.380	-0.147	-0.147	0.000	0.000	0.000	0.000
66	A	92	LEU	0	-0.060	-0.014	14.697	0.975	0.975	0.000	0.000	0.000	0.000
67	A	93	ASN	0	0.026	0.010	15.110	0.322	0.322	0.000	0.000	0.000	0.000
68	A	94	ASP	-1	-0.876	-0.930	17.766	15.012	15.012	0.000	0.000	0.000	0.000
69	A	95	THR	0	-0.065	-0.036	21.286	-0.759	-0.759	0.000	0.000	0.000	0.000
70	A	96	ASP	-1	-0.774	-0.860	19.222	13.812	13.812	0.000	0.000	0.000	0.000
71	A	97	LYS	1	0.841	0.909	19.251	-12.506	-12.506	0.000	0.000	0.000	0.000
72	A	98	THR	0	0.020	0.000	16.890	-0.586	-0.586	0.000	0.000	0.000	0.000
73	A	99	ILE	0	-0.050	-0.004	20.051	0.031	0.031	0.000	0.000	0.000	0.000
74	A	100	ILE	0	0.004	0.013	14.479	0.351	0.351	0.000	0.000	0.000	0.000
75	A	101	LYS	1	0.921	0.961	18.969	-12.570	-12.570	0.000	0.000	0.000	0.000
76	A	102	TYR	0	0.046	0.025	16.813	0.725	0.725	0.000	0.000	0.000	0.000
77	A	103	LYS	1	0.847	0.918	18.273	-13.398	-13.398	0.000	0.000	0.000	0.000
78	A	104	MET	0	0.054	0.027	17.323	0.980	0.980	0.000	0.000	0.000	0.000
79	A	105	ARG	1	0.770	0.864	18.384	-14.532	-14.532	0.000	0.000	0.000	0.000
80	A	106	ILE	0	0.074	0.046	18.820	0.573	0.573	0.000	0.000	0.000	0.000
81	A	107	THR	0	-0.059	-0.032	21.074	-0.923	-0.923	0.000	0.000	0.000	0.000
82	A	108	CYS	0	0.019	0.045	22.578	0.400	0.400	0.000	0.000	0.000	0.000
83	A	109	PHE	0	-0.035	-0.032	22.222	-0.549	-0.549	0.000	0.000	0.000	0.000
84	A	110	ASP	-1	-0.831	-0.924	26.856	9.641	9.641	0.000	0.000	0.000	0.000
85	A	111	ASN	0	-0.005	0.009	27.095	-0.058	-0.058	0.000	0.000	0.000	0.000
86	A	112	ARG	1	0.856	0.910	19.347	-13.502	-13.502	0.000	0.000	0.000	0.000
87	A	113	TYR	0	-0.015	-0.012	17.371	-0.784	-0.784	0.000	0.000	0.000	0.000
88	A	114	THR	0	0.033	0.030	17.804	0.357	0.357	0.000	0.000	0.000	0.000
89	A	115	ILE	0	-0.002	-0.011	14.623	-0.922	-0.922	0.000	0.000	0.000	0.000
90	A	116	GLU	-1	-0.788	-0.861	14.214	16.111	16.111	0.000	0.000	0.000	0.000
91	A	117	ALA	0	0.022	0.009	13.413	-1.095	-1.095	0.000	0.000	0.000	0.000
92	A	118	SER	0	0.064	-0.004	13.099	0.806	0.806	0.000	0.000	0.000	0.000
93	A	119	ASP	-1	-0.890	-0.949	15.299	12.982	12.982	0.000	0.000	0.000	0.000
94	A	120	ILE	0	0.012	0.029	12.528	-0.726	-0.726	0.000	0.000	0.000	0.000
95	A	121	VAL	0	-0.059	-0.035	15.833	-0.028	-0.028	0.000	0.000	0.000	0.000
96	A	122	TYR	0	0.017	0.003	12.242	-0.434	-0.434	0.000	0.000	0.000	0.000
97	A	123	GLN	0	-0.050	-0.048	18.678	-0.817	-0.817	0.000	0.000	0.000	0.000
98	A	124	TYR	0	0.046	0.008	19.915	-0.012	-0.012	0.000	0.000	0.000	0.000
99	A	125	ASP	-1	-0.775	-0.901	22.064	10.463	10.463	0.000	0.000	0.000	0.000
100	A	126	PRO	0	-0.001	0.015	22.965	0.165	0.165	0.000	0.000	0.000	0.000
101	A	127	LEU	0	0.005	0.001	24.125	-0.045	-0.045	0.000	0.000	0.000	0.000
102	A	128	ASN	0	-0.056	-0.046	22.571	-0.035	-0.035	0.000	0.000	0.000	0.000
103	A	129	ASP	-1	-0.813	-0.875	26.370	9.179	9.179	0.000	0.000	0.000	0.000
104	A	130	LYS	1	0.824	0.905	26.789	-11.491	-11.491	0.000	0.000	0.000	0.000
105	A	131	LYS	1	0.802	0.896	28.923	-9.435	-9.435	0.000	0.000	0.000	0.000
106	A	132	TYR	0	-0.072	-0.045	24.471	-0.129	-0.129	0.000	0.000	0.000	0.000
107	A	133	LYS	1	0.852	0.930	24.149	-10.866	-10.866	0.000	0.000	0.000	0.000
108	A	134	THR	0	-0.009	0.001	22.426	0.346	0.346	0.000	0.000	0.000	0.000
109	A	135	TYR	0	0.038	0.017	18.331	-0.420	-0.420	0.000	0.000	0.000	0.000
110	A	136	LYS	1	0.861	0.919	17.447	-14.190	-14.190	0.000	0.000	0.000	0.000
111	A	137	ALA	0	0.061	0.033	12.040	0.211	0.211	0.000	0.000	0.000	0.000
112	A	138	GLU	-1	-0.795	-0.905	12.281	18.145	18.145	0.000	0.000	0.000	0.000
113	A	139	ASP	-1	-0.843	-0.894	13.662	14.824	14.824	0.000	0.000	0.000	0.000
114	A	140	VAL	0	-0.014	0.002	12.965	-0.373	-0.373	0.000	0.000	0.000	0.000
115	A	141	ILE	0	0.020	-0.016	8.254	0.584	0.584	0.000	0.000	0.000	0.000
116	A	142	ALA	0	0.062	0.032	7.624	2.891	2.891	0.000	0.000	0.000	0.000
117	A	143	ASN	0	-0.051	-0.044	6.639	0.775	0.775	0.000	0.000	0.000	0.000
118	A	144	ASN	0	0.076	0.029	1.861	-3.327	-12.129	20.003	-6.852	-4.348	-0.006
119	A	145	GLY	0	0.023	0.014	5.082	0.102	0.167	-0.001	-0.006	-0.057	0.000
120	A	146	ASP	-1	-0.859	-0.904	7.713	28.267	28.267	0.000	0.000	0.000	0.000
121	A	147	SER	0	-0.051	-0.037	10.038	-1.333	-1.333	0.000	0.000	0.000	0.000
122	A	148	ASN	0	0.005	0.019	12.158	-1.040	-1.040	0.000	0.000	0.000	0.000
123	A	149	THR	0	-0.048	-0.033	13.745	-0.951	-0.951	0.000	0.000	0.000	0.000
124	A	150	ILE	0	-0.032	-0.012	16.955	-1.011	-1.011	0.000	0.000	0.000	0.000
125	A	151	ALA	0	0.034	0.014	18.401	0.373	0.373	0.000	0.000	0.000	0.000
126	A	152	LEU	0	-0.043	-0.014	20.277	-0.040	-0.040	0.000	0.000	0.000	0.000
127	A	153	ILE	0	-0.057	-0.022	15.421	-0.223	-0.223	0.000	0.000	0.000	0.000
128	A	154	LYS	1	0.831	0.892	16.895	-14.711	-14.711	0.000	0.000	0.000	0.000
129	A	155	ASP	-1	-0.808	-0.896	14.938	17.441	17.441	0.000	0.000	0.000	0.000
130	A	156	PRO	0	0.027	0.021	11.371	0.797	0.797	0.000	0.000	0.000	0.000
131	A	157	LYS	1	0.841	0.886	6.877	-32.748	-32.748	0.000	0.000	0.000	0.000
132	A	158	LEU	0	-0.010	0.013	9.033	1.729	1.729	0.000	0.000	0.000	0.000
133	A	159	PHE	0	0.018	0.000	11.436	0.103	0.103	0.000	0.000	0.000	0.000
134	A	161	ASN	0	0.054	0.013	5.899	2.169	2.169	0.000	0.000	0.000	0.000
135	A	162	ALA	0	0.026	0.023	7.821	-0.164	-0.164	0.000	0.000	0.000	0.000
136	A	163	THR	0	-0.015	-0.021	9.953	-1.818	-1.818	0.000	0.000	0.000	0.000
137	A	164	PHE	0	0.010	0.014	4.400	-1.155	-0.843	0.002	-0.074	-0.240	0.000
138	A	165	PHE	0	0.029	0.009	7.317	-0.538	-0.538	0.000	0.000	0.000	0.000
139	A	166	PHE	0	-0.017	0.001	9.797	-1.714	-1.714	0.000	0.000	0.000	0.000
140	A	167	VAL	0	-0.016	-0.014	10.862	-1.203	-1.203	0.000	0.000	0.000	0.000
141	A	168	GLU	-1	-0.833	-0.929	7.277	26.045	26.045	0.000	0.000	0.000	0.000
142	A	169	ASN	0	-0.060	-0.038	10.705	-1.350	-1.350	0.000	0.000	0.000	0.000
143	A	170	LEU	0	-0.025	-0.004	13.522	-1.350	-1.350	0.000	0.000	0.000	0.000
144	A	171	PHE	0	-0.039	-0.031	10.829	-1.498	-1.498	0.000	0.000	0.000	0.000
145	A	172	ALA	0	0.039	0.026	14.174	-0.694	-0.694	0.000	0.000	0.000	0.000
146	A	173	ASP	-1	-0.844	-0.923	15.843	13.286	13.286	0.000	0.000	0.000	0.000
147	A	174	VAL	0	-0.067	-0.037	18.168	-0.915	-0.915	0.000	0.000	0.000	0.000
148	A	175	PHE	0	-0.005	0.011	17.352	-0.659	-0.659	0.000	0.000	0.000	0.000
149	A	176	ASP	-1	-0.851	-0.932	19.372	14.153	14.153	0.000	0.000	0.000	0.000
150	A	177	ALA	0	-0.088	-0.043	21.773	-0.800	-0.800	0.000	0.000	0.000	0.000
151	A	178	ALA	0	-0.033	-0.029	22.163	-0.635	-0.635	0.000	0.000	0.000	0.000
152	A	179	GLN	0	-0.018	-0.010	22.299	-0.519	-0.519	0.000	0.000	0.000	0.000
153	A	180	ASN	0	-0.116	-0.055	25.122	-0.693	-0.693	0.000	0.000	0.000	0.000
154	A	181	ALA	0	-0.063	-0.017	27.819	-0.437	-0.437	0.000	0.000	0.000	0.000
155	A	182	GLU	-1	-0.979	-0.994	29.647	8.961	8.961	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:27:GLU)