FMO DATABASE

FMODB ID: G6RN1

Calculation Name: 1VHX-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 1VHX

Chain ID: A

ChEMBL ID:

UniProt ID: O34634

Base Structure: X-ray

Registration Date: 2023-06-22

Reference: C. Watanabe, N. Tani, K. Kamisaka, T. Honma et al., Interaction energy analysis of Apo structure dataset on FMODB, To be published.

DOI:

Apendix: None

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	140
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-1207681.708256
FMO2-HF: Nuclear repulsion	1153256.645646
FMO2-HF: Total energy	-54425.06261
FMO2-MP2: Total energy	-54582.138556

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:SER)

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

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.
-24.83	-29.73	28.075	-13.522	-9.652	-0.069

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

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : -0.029 / q_NPA : -0.046

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	2	ARG	1	0.753	0.848	2.915	7.391	11.259	0.196	-1.884	-2.179	0.007
4	A	3	ILE	0	0.009	0.003	5.210	-0.177	-0.104	-0.001	-0.009	-0.062	0.000
5	A	4	LEU	0	0.028	0.012	8.863	-0.151	-0.151	0.000	0.000	0.000	0.000
6	A	5	GLY	0	0.022	0.015	11.419	0.163	0.163	0.000	0.000	0.000	0.000
7	A	6	LEU	0	-0.035	-0.012	14.522	-0.041	-0.041	0.000	0.000	0.000	0.000
8	A	7	ASP	-1	-0.911	-0.967	17.917	-0.186	-0.186	0.000	0.000	0.000	0.000
9	A	8	LEU	0	0.046	0.028	21.594	-0.016	-0.016	0.000	0.000	0.000	0.000
10	A	9	GLY	0	0.037	0.023	24.683	0.025	0.025	0.000	0.000	0.000	0.000
11	A	10	THR	0	-0.014	-0.023	27.622	-0.008	-0.008	0.000	0.000	0.000	0.000
12	A	11	LYS	1	0.875	0.921	29.416	0.149	0.149	0.000	0.000	0.000	0.000
13	A	12	THR	0	-0.039	-0.023	24.944	0.004	0.004	0.000	0.000	0.000	0.000
14	A	13	LEU	0	0.019	0.040	19.679	0.017	0.017	0.000	0.000	0.000	0.000
15	A	14	GLY	0	-0.044	-0.014	20.227	-0.022	-0.022	0.000	0.000	0.000	0.000
16	A	15	VAL	0	0.027	-0.005	13.870	0.005	0.005	0.000	0.000	0.000	0.000
17	A	16	ALA	0	-0.005	-0.006	13.408	0.012	0.012	0.000	0.000	0.000	0.000
18	A	17	LEU	0	0.047	0.025	7.430	0.038	0.038	0.000	0.000	0.000	0.000
19	A	18	SER	0	0.018	0.023	5.651	0.137	0.137	0.000	0.000	0.000	0.000
20	A	19	ASP	-1	-0.754	-0.852	6.257	-1.076	-1.076	0.000	0.000	0.000	0.000
21	A	20	GLU	-1	-0.757	-0.843	1.634	-32.520	-42.682	27.874	-11.238	-6.474	-0.077
22	A	21	MET	0	-0.070	-0.026	3.577	2.121	2.303	-0.001	0.037	-0.218	0.000
23	A	22	GLY	0	0.008	0.026	6.448	0.129	0.129	0.000	0.000	0.000	0.000
24	A	23	TRP	0	-0.046	-0.013	8.017	-0.085	-0.085	0.000	0.000	0.000	0.000
25	A	24	THR	0	-0.052	-0.059	10.060	-0.056	-0.056	0.000	0.000	0.000	0.000
26	A	25	ALA	0	0.011	0.004	10.122	-0.146	-0.146	0.000	0.000	0.000	0.000
27	A	26	GLN	0	0.011	0.005	8.354	-0.288	-0.288	0.000	0.000	0.000	0.000
28	A	27	GLY	0	-0.008	-0.016	11.943	-0.046	-0.046	0.000	0.000	0.000	0.000
29	A	28	ILE	0	-0.041	-0.005	10.334	-0.027	-0.027	0.000	0.000	0.000	0.000
30	A	29	GLU	-1	-0.780	-0.876	14.331	-0.399	-0.399	0.000	0.000	0.000	0.000
31	A	30	THR	0	-0.083	-0.050	17.758	0.022	0.022	0.000	0.000	0.000	0.000
32	A	31	ILE	0	0.038	0.044	17.573	0.035	0.035	0.000	0.000	0.000	0.000
33	A	32	LYS	1	0.840	0.905	21.602	0.241	0.241	0.000	0.000	0.000	0.000
34	A	33	ILE	0	0.045	0.051	23.552	-0.007	-0.007	0.000	0.000	0.000	0.000
35	A	34	ASN	0	-0.078	-0.049	26.437	0.025	0.025	0.000	0.000	0.000	0.000
36	A	35	GLU	-1	-0.707	-0.833	29.185	-0.152	-0.152	0.000	0.000	0.000	0.000
37	A	36	ALA	0	-0.073	-0.018	31.036	0.005	0.005	0.000	0.000	0.000	0.000
38	A	37	GLU	-1	-0.916	-0.957	31.897	-0.117	-0.117	0.000	0.000	0.000	0.000
39	A	38	GLY	0	-0.011	0.000	31.249	0.000	0.000	0.000	0.000	0.000	0.000
40	A	39	ASP	-1	-0.890	-0.940	26.318	-0.229	-0.229	0.000	0.000	0.000	0.000
41	A	40	TYR	0	0.021	-0.014	24.481	0.005	0.005	0.000	0.000	0.000	0.000
42	A	41	GLY	0	0.033	-0.002	22.308	-0.022	-0.022	0.000	0.000	0.000	0.000
43	A	42	LEU	0	0.044	0.017	19.904	-0.032	-0.032	0.000	0.000	0.000	0.000
44	A	43	SER	0	-0.006	0.013	18.841	-0.037	-0.037	0.000	0.000	0.000	0.000
45	A	44	ARG	1	0.788	0.859	17.877	0.417	0.417	0.000	0.000	0.000	0.000
46	A	45	LEU	0	0.017	-0.006	14.853	-0.048	-0.048	0.000	0.000	0.000	0.000
47	A	46	SER	0	0.019	-0.002	14.300	-0.089	-0.089	0.000	0.000	0.000	0.000
48	A	47	GLU	-1	-0.916	-0.949	13.635	-0.459	-0.459	0.000	0.000	0.000	0.000
49	A	48	LEU	0	-0.058	-0.027	12.816	-0.065	-0.065	0.000	0.000	0.000	0.000
50	A	49	ILE	0	-0.001	-0.004	9.346	-0.195	-0.195	0.000	0.000	0.000	0.000
51	A	50	LYS	1	0.909	0.978	8.547	0.230	0.230	0.000	0.000	0.000	0.000
52	A	51	ASP	-1	-0.937	-0.965	8.000	-0.560	-0.560	0.000	0.000	0.000	0.000
53	A	52	TYR	0	-0.045	-0.015	4.020	-0.303	-0.057	-0.001	-0.032	-0.214	0.000
54	A	53	THR	0	-0.044	-0.027	3.563	1.231	2.124	0.008	-0.396	-0.505	0.001
55	A	54	ILE	0	0.009	0.000	5.287	-0.696	-0.696	0.000	0.000	0.000	0.000
56	A	55	ASP	-1	-0.788	-0.890	8.106	0.202	0.202	0.000	0.000	0.000	0.000
57	A	56	LYS	1	0.814	0.905	10.049	0.083	0.083	0.000	0.000	0.000	0.000
58	A	57	ILE	0	0.004	0.000	11.773	-0.139	-0.139	0.000	0.000	0.000	0.000
59	A	58	VAL	0	0.017	0.019	13.803	0.071	0.071	0.000	0.000	0.000	0.000
60	A	59	LEU	0	-0.032	-0.018	16.222	-0.054	-0.054	0.000	0.000	0.000	0.000
61	A	60	GLY	0	0.007	-0.003	19.589	0.033	0.033	0.000	0.000	0.000	0.000
62	A	61	PHE	0	-0.027	-0.022	22.058	0.000	0.000	0.000	0.000	0.000	0.000
63	A	62	PRO	0	-0.051	-0.010	25.341	0.009	0.009	0.000	0.000	0.000	0.000
64	A	63	LYS	1	0.822	0.868	28.573	0.095	0.095	0.000	0.000	0.000	0.000
65	A	64	ASN	0	0.043	0.021	30.811	-0.005	-0.005	0.000	0.000	0.000	0.000
66	A	65	MET	0	-0.005	0.002	33.274	0.004	0.004	0.000	0.000	0.000	0.000
67	A	66	ASN	0	-0.016	-0.018	36.701	0.004	0.004	0.000	0.000	0.000	0.000
68	A	67	GLY	0	0.027	0.020	35.211	0.004	0.004	0.000	0.000	0.000	0.000
69	A	68	THR	0	-0.036	-0.014	35.743	-0.001	-0.001	0.000	0.000	0.000	0.000
70	A	69	VAL	0	0.005	0.015	31.937	-0.003	-0.003	0.000	0.000	0.000	0.000
71	A	70	GLY	0	0.050	0.024	33.744	0.004	0.004	0.000	0.000	0.000	0.000
72	A	71	PRO	0	0.001	-0.015	33.560	-0.006	-0.006	0.000	0.000	0.000	0.000
73	A	72	ARG	1	0.817	0.868	28.493	0.153	0.153	0.000	0.000	0.000	0.000
74	A	73	GLY	0	0.060	0.055	29.365	-0.011	-0.011	0.000	0.000	0.000	0.000
75	A	74	GLU	-1	-0.746	-0.870	29.233	-0.113	-0.113	0.000	0.000	0.000	0.000
76	A	75	ALA	0	-0.024	-0.008	29.725	-0.005	-0.005	0.000	0.000	0.000	0.000
77	A	76	SER	0	0.027	-0.006	25.368	-0.017	-0.017	0.000	0.000	0.000	0.000
78	A	77	GLN	0	-0.045	-0.024	25.276	-0.009	-0.009	0.000	0.000	0.000	0.000
79	A	78	THR	0	-0.037	-0.021	26.502	-0.001	-0.001	0.000	0.000	0.000	0.000
80	A	79	PHE	0	0.018	0.006	20.691	-0.005	-0.005	0.000	0.000	0.000	0.000
81	A	80	ALA	0	0.041	0.016	21.923	-0.020	-0.020	0.000	0.000	0.000	0.000
82	A	81	LYS	1	0.841	0.913	22.140	0.108	0.108	0.000	0.000	0.000	0.000
83	A	82	VAL	0	0.002	0.022	22.307	-0.001	-0.001	0.000	0.000	0.000	0.000
84	A	83	LEU	0	-0.004	0.013	17.514	-0.017	-0.017	0.000	0.000	0.000	0.000
85	A	84	GLU	-1	-0.868	-0.937	18.398	-0.182	-0.182	0.000	0.000	0.000	0.000
86	A	85	THR	0	-0.076	-0.063	19.430	-0.003	-0.003	0.000	0.000	0.000	0.000
87	A	86	THR	0	-0.085	-0.047	18.162	0.012	0.012	0.000	0.000	0.000	0.000
88	A	87	TYR	0	-0.055	-0.051	14.253	-0.029	-0.029	0.000	0.000	0.000	0.000
89	A	88	ASN	0	-0.057	-0.015	14.946	-0.011	-0.011	0.000	0.000	0.000	0.000
90	A	89	VAL	0	-0.008	0.001	11.939	0.016	0.016	0.000	0.000	0.000	0.000
91	A	90	PRO	0	-0.004	0.000	14.768	-0.002	-0.002	0.000	0.000	0.000	0.000
92	A	91	VAL	0	-0.019	0.001	15.927	-0.038	-0.038	0.000	0.000	0.000	0.000
93	A	92	VAL	0	-0.041	-0.020	16.519	0.038	0.038	0.000	0.000	0.000	0.000
94	A	93	LEU	0	-0.018	-0.010	18.972	-0.023	-0.023	0.000	0.000	0.000	0.000
95	A	94	TRP	0	-0.010	-0.009	19.693	0.017	0.017	0.000	0.000	0.000	0.000
96	A	95	ASP	-1	-0.781	-0.879	21.766	-0.109	-0.109	0.000	0.000	0.000	0.000
97	A	96	GLU	-1	-0.865	-0.905	22.017	-0.038	-0.038	0.000	0.000	0.000	0.000
98	A	97	ARG	1	0.928	0.963	21.356	0.156	0.156	0.000	0.000	0.000	0.000
99	A	98	LEU	0	0.051	0.026	22.444	0.014	0.014	0.000	0.000	0.000	0.000
100	A	99	THR	0	0.048	0.028	24.436	-0.016	-0.016	0.000	0.000	0.000	0.000
101	A	100	THR	0	0.041	-0.002	27.394	-0.003	-0.003	0.000	0.000	0.000	0.000
102	A	101	MET	0	-0.016	-0.002	29.018	0.004	0.004	0.000	0.000	0.000	0.000
103	A	102	ALA	0	0.026	0.018	28.442	0.006	0.006	0.000	0.000	0.000	0.000
104	A	103	ALA	0	0.045	0.020	26.896	0.002	0.002	0.000	0.000	0.000	0.000
105	A	104	GLU	-1	-0.776	-0.881	28.671	-0.101	-0.101	0.000	0.000	0.000	0.000
106	A	105	LYS	1	0.919	0.960	32.083	0.070	0.070	0.000	0.000	0.000	0.000
107	A	106	MET	0	0.023	0.014	26.030	0.003	0.003	0.000	0.000	0.000	0.000
108	A	107	LEU	0	-0.017	-0.008	27.845	-0.002	-0.002	0.000	0.000	0.000	0.000
109	A	108	ILE	0	-0.063	-0.042	31.546	0.002	0.002	0.000	0.000	0.000	0.000
110	A	109	ALA	0	-0.032	-0.011	33.537	0.003	0.003	0.000	0.000	0.000	0.000
111	A	110	ALA	0	0.006	0.011	31.842	0.002	0.002	0.000	0.000	0.000	0.000
112	A	111	ASP	-1	-0.899	-0.934	33.770	-0.075	-0.075	0.000	0.000	0.000	0.000
113	A	112	VAL	0	-0.066	-0.018	30.773	-0.004	-0.004	0.000	0.000	0.000	0.000
114	A	113	SER	0	0.048	0.012	34.108	0.001	0.001	0.000	0.000	0.000	0.000
115	A	114	ARG	1	1.008	0.991	34.740	0.079	0.079	0.000	0.000	0.000	0.000
116	A	115	GLN	0	0.022	0.006	34.733	-0.009	-0.009	0.000	0.000	0.000	0.000
117	A	116	LYS	1	0.964	0.986	29.993	0.126	0.126	0.000	0.000	0.000	0.000
118	A	117	ARG	1	0.834	0.894	30.249	0.084	0.084	0.000	0.000	0.000	0.000
119	A	118	LYS	1	0.861	0.909	29.808	0.136	0.136	0.000	0.000	0.000	0.000
120	A	119	LYS	1	0.971	0.973	29.123	0.150	0.150	0.000	0.000	0.000	0.000
121	A	120	VAL	0	-0.045	-0.019	25.584	-0.018	-0.018	0.000	0.000	0.000	0.000
122	A	121	ILE	0	0.004	-0.002	24.988	-0.015	-0.015	0.000	0.000	0.000	0.000
123	A	122	ASP	-1	-0.837	-0.886	25.518	-0.170	-0.170	0.000	0.000	0.000	0.000
124	A	123	LYS	1	0.923	0.963	21.788	0.260	0.260	0.000	0.000	0.000	0.000
125	A	124	MET	0	0.002	0.003	18.954	-0.036	-0.036	0.000	0.000	0.000	0.000
126	A	125	ALA	0	-0.005	0.021	20.585	-0.006	-0.006	0.000	0.000	0.000	0.000
127	A	126	ALA	0	0.068	0.025	17.535	0.014	0.014	0.000	0.000	0.000	0.000
128	A	127	VAL	0	0.013	0.012	15.727	-0.011	-0.011	0.000	0.000	0.000	0.000
129	A	128	MET	0	-0.066	-0.034	17.025	0.030	0.030	0.000	0.000	0.000	0.000
130	A	129	ILE	0	-0.034	-0.017	17.835	0.030	0.030	0.000	0.000	0.000	0.000
131	A	130	LEU	0	0.017	0.015	11.028	0.032	0.032	0.000	0.000	0.000	0.000
132	A	131	GLN	0	-0.041	-0.033	14.503	-0.041	-0.041	0.000	0.000	0.000	0.000
133	A	132	GLY	0	0.019	0.014	15.956	0.038	0.038	0.000	0.000	0.000	0.000
134	A	133	TYR	0	0.011	-0.001	12.653	0.033	0.033	0.000	0.000	0.000	0.000
135	A	134	LEU	0	-0.023	-0.016	10.320	0.028	0.028	0.000	0.000	0.000	0.000
136	A	135	ASP	-1	-0.856	-0.914	13.965	-0.035	-0.035	0.000	0.000	0.000	0.000
137	A	136	SER	0	-0.060	-0.051	17.023	0.037	0.037	0.000	0.000	0.000	0.000
138	A	137	LEU	0	-0.082	-0.040	11.474	0.021	0.021	0.000	0.000	0.000	0.000
139	A	138	ASN	0	-0.087	-0.068	11.959	0.105	0.105	0.000	0.000	0.000	0.000
140	A	139	GLU	-1	-1.020	-0.980	15.558	0.088	0.088	0.000	0.000	0.000	0.000

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