FMO DATABASE

FMODB ID: 4JVJN

Calculation Name: 1ZHV-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 1ZHV

Chain ID: A

ChEMBL ID:

UniProt ID: A9CJY8

Base Structure: X-ray

Registration Date: 2023-09-23

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	134
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-1078224.418831
FMO2-HF: Nuclear repulsion	1027897.192751
FMO2-HF: Total energy	-50327.22608
FMO2-MP2: Total energy	-50476.517159

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:ALA)

Summations of interaction energy for fragment #1(A:2: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.
0.18	2.187	0.024	-0.839	-1.193	0.003

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

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : 0.044 / q_NPA : 0.021

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	ARG	1	0.918	0.974	3.895	1.843	3.371	-0.002	-0.726	-0.800	0.003
4	A	5	ILE	0	-0.029	-0.003	5.938	0.615	0.615	0.000	0.000	0.000	0.000
5	A	6	LYS	1	0.882	0.943	8.206	0.961	0.961	0.000	0.000	0.000	0.000
6	A	7	LEU	0	0.003	-0.002	9.812	0.074	0.074	0.000	0.000	0.000	0.000
7	A	8	LYS	1	0.848	0.934	13.795	0.293	0.293	0.000	0.000	0.000	0.000
8	A	9	ILE	0	-0.004	0.028	17.573	0.014	0.014	0.000	0.000	0.000	0.000
9	A	10	LEU	0	-0.043	-0.033	19.779	0.000	0.000	0.000	0.000	0.000	0.000
10	A	11	ASN	0	0.016	0.002	22.940	0.008	0.008	0.000	0.000	0.000	0.000
11	A	12	GLY	0	0.034	0.033	26.345	0.004	0.004	0.000	0.000	0.000	0.000
12	A	13	SER	0	-0.033	-0.011	26.595	-0.003	-0.003	0.000	0.000	0.000	0.000
13	A	14	TYR	0	-0.014	-0.020	25.065	0.001	0.001	0.000	0.000	0.000	0.000
14	A	15	GLY	0	0.027	0.004	27.324	0.006	0.006	0.000	0.000	0.000	0.000
15	A	16	ILE	0	-0.020	0.000	24.290	-0.006	-0.006	0.000	0.000	0.000	0.000
16	A	17	ALA	0	0.027	0.016	28.377	0.008	0.008	0.000	0.000	0.000	0.000
17	A	18	ARG	1	0.754	0.854	31.414	-0.005	-0.005	0.000	0.000	0.000	0.000
18	A	19	LEU	0	0.014	0.012	33.331	0.003	0.003	0.000	0.000	0.000	0.000
19	A	20	SER	0	0.003	-0.020	35.822	0.004	0.004	0.000	0.000	0.000	0.000
20	A	21	ALA	0	0.067	0.038	36.388	-0.003	-0.003	0.000	0.000	0.000	0.000
21	A	22	SER	0	-0.039	-0.015	37.422	-0.001	-0.001	0.000	0.000	0.000	0.000
22	A	23	GLU	-1	-0.858	-0.912	39.097	-0.020	-0.020	0.000	0.000	0.000	0.000
23	A	24	ALA	0	0.008	0.007	39.277	-0.001	-0.001	0.000	0.000	0.000	0.000
24	A	25	ILE	0	0.032	0.009	34.945	0.000	0.000	0.000	0.000	0.000	0.000
25	A	26	PRO	0	-0.009	0.018	36.632	0.000	0.000	0.000	0.000	0.000	0.000
26	A	27	ALA	0	0.011	-0.021	38.102	-0.003	-0.003	0.000	0.000	0.000	0.000
27	A	28	TRP	0	0.057	0.033	33.774	-0.003	-0.003	0.000	0.000	0.000	0.000
28	A	29	ALA	0	0.005	0.008	33.873	-0.004	-0.004	0.000	0.000	0.000	0.000
29	A	30	ASP	-1	-0.857	-0.913	32.787	-0.089	-0.089	0.000	0.000	0.000	0.000
30	A	31	GLY	0	-0.007	-0.009	33.272	0.004	0.004	0.000	0.000	0.000	0.000
31	A	32	GLY	0	-0.030	-0.024	31.575	-0.004	-0.004	0.000	0.000	0.000	0.000
32	A	33	GLY	0	0.043	0.025	28.157	0.006	0.006	0.000	0.000	0.000	0.000
33	A	34	PHE	0	-0.003	-0.012	22.144	-0.004	-0.004	0.000	0.000	0.000	0.000
34	A	35	VAL	0	0.011	-0.001	25.930	0.011	0.011	0.000	0.000	0.000	0.000
35	A	36	SER	0	-0.011	-0.005	24.675	-0.009	-0.009	0.000	0.000	0.000	0.000
36	A	37	ILE	0	0.004	0.018	26.798	0.009	0.009	0.000	0.000	0.000	0.000
37	A	38	THR	0	-0.052	-0.039	26.637	-0.004	-0.004	0.000	0.000	0.000	0.000
38	A	39	ARG	1	0.802	0.887	29.421	0.026	0.026	0.000	0.000	0.000	0.000
39	A	40	THR	0	0.005	0.004	29.422	-0.001	-0.001	0.000	0.000	0.000	0.000
40	A	41	ASP	-1	-0.908	-0.960	32.388	0.015	0.015	0.000	0.000	0.000	0.000
41	A	42	ASP	-1	-0.860	-0.914	33.460	0.015	0.015	0.000	0.000	0.000	0.000
42	A	43	GLU	-1	-0.855	-0.895	29.846	-0.006	-0.006	0.000	0.000	0.000	0.000
43	A	44	LEU	0	-0.037	-0.021	33.109	-0.002	-0.002	0.000	0.000	0.000	0.000
44	A	45	SER	0	0.032	0.001	28.384	-0.002	-0.002	0.000	0.000	0.000	0.000
45	A	46	ILE	0	-0.066	-0.041	30.177	-0.005	-0.005	0.000	0.000	0.000	0.000
46	A	47	VAL	0	-0.014	0.014	24.420	0.001	0.001	0.000	0.000	0.000	0.000
47	A	48	CYS	0	-0.012	-0.012	27.752	-0.004	-0.004	0.000	0.000	0.000	0.000
48	A	49	LEU	0	-0.005	0.004	28.624	0.001	0.001	0.000	0.000	0.000	0.000
49	A	50	ILE	0	0.019	-0.002	29.490	0.007	0.007	0.000	0.000	0.000	0.000
50	A	51	ASP	-1	-0.919	-0.960	32.319	-0.071	-0.071	0.000	0.000	0.000	0.000
51	A	52	ARG	1	0.742	0.861	31.877	0.083	0.083	0.000	0.000	0.000	0.000
52	A	53	ILE	0	-0.018	-0.002	31.383	0.003	0.003	0.000	0.000	0.000	0.000
53	A	54	PRO	0	-0.010	0.001	36.061	0.001	0.001	0.000	0.000	0.000	0.000
54	A	55	GLN	0	-0.028	-0.024	37.814	0.003	0.003	0.000	0.000	0.000	0.000
55	A	56	ASP	-1	-0.922	-0.958	40.548	-0.023	-0.023	0.000	0.000	0.000	0.000
56	A	57	VAL	0	-0.050	-0.016	35.870	0.003	0.003	0.000	0.000	0.000	0.000
57	A	58	ARG	1	0.863	0.922	35.460	0.008	0.008	0.000	0.000	0.000	0.000
58	A	59	VAL	0	0.035	0.007	31.413	-0.002	-0.002	0.000	0.000	0.000	0.000
59	A	60	ASP	-1	-0.799	-0.831	27.616	-0.015	-0.015	0.000	0.000	0.000	0.000
60	A	61	PRO	0	0.026	0.001	28.607	-0.008	-0.008	0.000	0.000	0.000	0.000
61	A	62	GLY	0	0.011	0.009	27.951	0.005	0.005	0.000	0.000	0.000	0.000
62	A	63	TRP	0	-0.061	-0.027	20.491	-0.003	-0.003	0.000	0.000	0.000	0.000
63	A	64	SER	0	0.048	0.024	21.431	0.002	0.002	0.000	0.000	0.000	0.000
64	A	65	CYS	0	-0.030	0.007	20.024	-0.004	-0.004	0.000	0.000	0.000	0.000
65	A	66	PHE	0	0.047	0.016	15.766	-0.015	-0.015	0.000	0.000	0.000	0.000
66	A	67	LYS	1	0.899	0.969	17.377	0.348	0.348	0.000	0.000	0.000	0.000
67	A	68	PHE	0	0.033	0.008	9.965	-0.063	-0.063	0.000	0.000	0.000	0.000
68	A	69	GLN	0	-0.005	-0.014	13.998	0.096	0.096	0.000	0.000	0.000	0.000
69	A	70	GLY	0	0.013	0.007	14.617	-0.089	-0.089	0.000	0.000	0.000	0.000
70	A	71	PRO	0	0.015	-0.004	16.374	0.003	0.003	0.000	0.000	0.000	0.000
71	A	72	PHE	0	-0.014	-0.015	11.954	-0.115	-0.115	0.000	0.000	0.000	0.000
72	A	73	ALA	0	0.008	0.019	13.754	0.083	0.083	0.000	0.000	0.000	0.000
73	A	74	PHE	0	-0.058	-0.034	9.039	-0.207	-0.207	0.000	0.000	0.000	0.000
74	A	75	ASP	-1	-0.872	-0.933	9.453	-0.383	-0.383	0.000	0.000	0.000	0.000
75	A	76	GLU	-1	-0.921	-0.966	9.569	0.041	0.041	0.000	0.000	0.000	0.000
76	A	77	THR	0	-0.065	-0.021	5.229	0.011	0.011	0.000	0.000	0.000	0.000
77	A	78	GLY	0	0.051	0.015	6.860	-0.184	-0.184	0.000	0.000	0.000	0.000
78	A	79	ILE	0	0.014	0.005	6.964	-0.004	-0.004	0.000	0.000	0.000	0.000
79	A	80	VAL	0	0.068	0.046	7.495	-0.078	-0.078	0.000	0.000	0.000	0.000
80	A	81	LEU	0	0.006	0.009	7.443	-0.008	-0.008	0.000	0.000	0.000	0.000
81	A	82	SER	0	-0.031	-0.038	3.113	-0.302	-0.055	0.028	-0.078	-0.198	0.000
82	A	83	VAL	0	0.010	0.023	4.926	-0.167	-0.131	-0.001	-0.001	-0.034	0.000
83	A	84	ILE	0	0.053	0.008	7.795	0.081	0.081	0.000	0.000	0.000	0.000
84	A	85	SER	0	-0.014	0.025	7.036	0.087	0.087	0.000	0.000	0.000	0.000
85	A	86	PRO	0	0.029	0.026	6.637	0.049	0.049	0.000	0.000	0.000	0.000
86	A	87	LEU	0	0.017	0.026	9.332	-0.018	-0.018	0.000	0.000	0.000	0.000
87	A	88	SER	0	0.014	-0.015	12.348	0.007	0.007	0.000	0.000	0.000	0.000
88	A	89	THR	0	-0.104	-0.073	11.075	0.001	0.001	0.000	0.000	0.000	0.000
89	A	90	ASN	0	-0.069	-0.036	12.410	0.005	0.005	0.000	0.000	0.000	0.000
90	A	91	GLY	0	-0.010	0.003	15.657	-0.030	-0.030	0.000	0.000	0.000	0.000
91	A	92	ILE	0	-0.054	-0.013	15.312	-0.018	-0.018	0.000	0.000	0.000	0.000
92	A	93	GLY	0	-0.002	0.006	16.883	0.015	0.015	0.000	0.000	0.000	0.000
93	A	94	ILE	0	-0.037	-0.023	14.074	-0.028	-0.028	0.000	0.000	0.000	0.000
94	A	95	PHE	0	0.040	0.017	17.412	0.020	0.020	0.000	0.000	0.000	0.000
95	A	96	VAL	0	-0.012	-0.018	14.642	-0.028	-0.028	0.000	0.000	0.000	0.000
96	A	97	VAL	0	0.002	0.003	17.658	0.020	0.020	0.000	0.000	0.000	0.000
97	A	98	SER	0	-0.001	-0.021	16.232	-0.016	-0.016	0.000	0.000	0.000	0.000
98	A	99	THR	0	-0.099	-0.061	18.439	0.019	0.019	0.000	0.000	0.000	0.000
99	A	100	PHE	0	0.010	0.002	19.798	-0.006	-0.006	0.000	0.000	0.000	0.000
100	A	101	ASP	-1	-0.905	-0.947	20.244	-0.225	-0.225	0.000	0.000	0.000	0.000
101	A	102	GLY	0	-0.003	0.005	16.172	-0.051	-0.051	0.000	0.000	0.000	0.000
102	A	103	ASP	-1	-0.836	-0.903	13.875	-0.201	-0.201	0.000	0.000	0.000	0.000
103	A	104	HIS	0	-0.001	-0.013	16.024	-0.049	-0.049	0.000	0.000	0.000	0.000
104	A	105	LEU	0	-0.023	-0.006	12.731	0.021	0.021	0.000	0.000	0.000	0.000
105	A	106	LEU	0	-0.016	-0.013	16.373	-0.012	-0.012	0.000	0.000	0.000	0.000
106	A	107	VAL	0	0.028	0.013	16.235	0.015	0.015	0.000	0.000	0.000	0.000
107	A	108	ARG	1	0.894	0.916	19.331	0.015	0.015	0.000	0.000	0.000	0.000
108	A	109	SER	0	0.017	-0.017	21.672	-0.006	-0.006	0.000	0.000	0.000	0.000
109	A	110	ASN	0	-0.061	-0.027	23.615	-0.007	-0.007	0.000	0.000	0.000	0.000
110	A	111	ASP	-1	-0.838	-0.934	19.139	-0.014	-0.014	0.000	0.000	0.000	0.000
111	A	112	LEU	0	-0.002	0.019	18.628	-0.012	-0.012	0.000	0.000	0.000	0.000
112	A	113	GLU	-1	-0.876	-0.940	18.107	-0.160	-0.160	0.000	0.000	0.000	0.000
113	A	114	LYS	1	0.907	0.943	17.586	0.000	0.000	0.000	0.000	0.000	0.000
114	A	115	THR	0	0.012	-0.016	14.042	0.005	0.005	0.000	0.000	0.000	0.000
115	A	116	ALA	0	-0.010	-0.007	13.279	-0.053	-0.053	0.000	0.000	0.000	0.000
116	A	117	ASP	-1	-0.888	-0.937	13.315	-0.211	-0.211	0.000	0.000	0.000	0.000
117	A	118	LEU	0	-0.035	-0.014	11.471	-0.034	-0.034	0.000	0.000	0.000	0.000
118	A	119	LEU	0	-0.029	-0.013	8.838	-0.040	-0.040	0.000	0.000	0.000	0.000
119	A	120	ALA	0	0.017	0.008	8.348	-0.218	-0.218	0.000	0.000	0.000	0.000
120	A	121	ASN	0	-0.086	-0.060	9.094	-0.097	-0.097	0.000	0.000	0.000	0.000
121	A	122	ALA	0	-0.036	-0.005	5.275	0.083	0.083	0.000	0.000	0.000	0.000
122	A	123	GLY	0	-0.046	-0.017	4.085	-0.831	-0.692	0.000	-0.029	-0.111	0.000
123	A	124	HIS	0	-0.003	-0.004	4.526	-0.648	-0.591	-0.001	-0.005	-0.050	0.000
124	A	125	SER	0	-0.055	-0.020	7.829	0.229	0.229	0.000	0.000	0.000	0.000
125	A	126	LEU	0	0.030	0.009	11.388	0.024	0.024	0.000	0.000	0.000	0.000
126	A	127	LEU	0	-0.032	-0.009	14.435	0.032	0.032	0.000	0.000	0.000	0.000
127	A	128	LEU	0	0.054	0.003	17.290	0.015	0.015	0.000	0.000	0.000	0.000
128	A	129	GLU	-1	-0.875	-0.926	20.361	-0.258	-0.258	0.000	0.000	0.000	0.000
129	A	130	HIS	0	-0.026	-0.038	23.566	-0.009	-0.009	0.000	0.000	0.000	0.000
130	A	131	HIS	0	0.003	0.003	25.978	0.009	0.009	0.000	0.000	0.000	0.000
131	A	132	HIS	0	0.019	0.008	28.340	0.001	0.001	0.000	0.000	0.000	0.000
132	A	133	HIS	0	-0.023	0.005	30.165	0.005	0.005	0.000	0.000	0.000	0.000
133	A	134	HIS	0	-0.012	-0.005	33.760	-0.001	-0.001	0.000	0.000	0.000	0.000
134	A	135	HIS	0	0.017	0.010	35.120	0.004	0.004	0.000	0.000	0.000	0.000

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