FMO DATABASE

FMODB ID: 2N32R

Calculation Name: 1X91-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 1X91

Chain ID: A

ChEMBL ID:

UniProt ID: Q9LNF2

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	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	147
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-1300425.787412
FMO2-HF: Nuclear repulsion	1242334.1243
FMO2-HF: Total energy	-58091.663112
FMO2-MP2: Total energy	-58254.878686

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:1:SER)

Summations of interaction energy for fragment #1(A:1: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.
-4.269	-1.636	0.082	-1.13	-1.585	0

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

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : 0.004 / q_NPA : -0.016

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	3	GLU	-1	-0.800	-0.913	3.497	-5.756	-4.068	0.008	-0.813	-0.883	0.002
4	A	4	MET	0	-0.047	-0.008	5.938	0.166	0.166	0.000	0.000	0.000	0.000
5	A	5	SER	0	-0.081	-0.054	3.140	-0.052	0.666	0.070	-0.284	-0.505	-0.002
6	A	6	THR	0	0.000	-0.008	3.605	0.203	0.430	0.004	-0.033	-0.197	0.000
7	A	7	ILE	0	0.013	0.012	6.246	0.284	0.284	0.000	0.000	0.000	0.000
8	A	8	CYS	0	0.028	0.018	9.170	0.272	0.272	0.000	0.000	0.000	0.000
9	A	9	ASP	-1	-0.866	-0.911	9.284	-1.756	-1.756	0.000	0.000	0.000	0.000
10	A	10	LYS	1	0.878	0.944	8.640	2.033	2.033	0.000	0.000	0.000	0.000
11	A	11	THR	0	-0.065	-0.036	14.024	0.138	0.138	0.000	0.000	0.000	0.000
12	A	12	LEU	0	0.074	0.020	16.663	-0.002	-0.002	0.000	0.000	0.000	0.000
13	A	13	ASN	0	-0.028	-0.004	19.076	0.020	0.020	0.000	0.000	0.000	0.000
14	A	14	PRO	0	0.084	0.044	14.478	0.027	0.027	0.000	0.000	0.000	0.000
15	A	15	SER	0	0.029	0.009	15.642	-0.009	-0.009	0.000	0.000	0.000	0.000
16	A	16	PHE	0	-0.032	-0.013	17.746	0.037	0.037	0.000	0.000	0.000	0.000
17	A	18	LEU	0	0.063	0.027	11.324	0.031	0.031	0.000	0.000	0.000	0.000
18	A	19	LYS	1	0.942	0.987	14.286	0.215	0.215	0.000	0.000	0.000	0.000
19	A	20	PHE	0	-0.016	-0.005	16.294	0.073	0.073	0.000	0.000	0.000	0.000
20	A	21	LEU	0	0.026	-0.008	10.990	0.061	0.061	0.000	0.000	0.000	0.000
21	A	22	ASN	0	-0.036	-0.033	12.356	0.174	0.174	0.000	0.000	0.000	0.000
22	A	23	THR	0	-0.079	-0.032	14.715	0.074	0.074	0.000	0.000	0.000	0.000
23	A	24	LYS	1	0.879	0.936	17.082	0.076	0.076	0.000	0.000	0.000	0.000
24	A	25	PHE	0	-0.034	0.007	11.883	0.022	0.022	0.000	0.000	0.000	0.000
25	A	26	ALA	0	0.036	0.023	11.850	0.036	0.036	0.000	0.000	0.000	0.000
26	A	27	SER	0	0.046	0.018	11.210	0.120	0.120	0.000	0.000	0.000	0.000
27	A	28	ALA	0	0.030	-0.002	7.344	-0.149	-0.149	0.000	0.000	0.000	0.000
28	A	29	ASN	0	-0.027	-0.003	9.197	-0.231	-0.231	0.000	0.000	0.000	0.000
29	A	30	LEU	0	0.101	0.034	10.174	0.007	0.007	0.000	0.000	0.000	0.000
30	A	31	GLN	0	0.051	0.033	13.280	-0.028	-0.028	0.000	0.000	0.000	0.000
31	A	32	ALA	0	-0.032	-0.023	15.240	0.008	0.008	0.000	0.000	0.000	0.000
32	A	33	LEU	0	-0.017	-0.013	11.785	0.008	0.008	0.000	0.000	0.000	0.000
33	A	34	ALA	0	0.038	0.026	15.466	-0.013	-0.013	0.000	0.000	0.000	0.000
34	A	35	LYS	1	0.895	0.946	17.924	0.049	0.049	0.000	0.000	0.000	0.000
35	A	36	THR	0	-0.008	-0.011	17.549	-0.004	-0.004	0.000	0.000	0.000	0.000
36	A	37	THR	0	-0.025	-0.037	17.070	-0.002	-0.002	0.000	0.000	0.000	0.000
37	A	38	LEU	0	0.062	0.045	19.708	0.001	0.001	0.000	0.000	0.000	0.000
38	A	39	ASP	-1	-0.820	-0.889	22.901	-0.036	-0.036	0.000	0.000	0.000	0.000
39	A	40	SER	0	-0.078	-0.043	22.088	0.014	0.014	0.000	0.000	0.000	0.000
40	A	41	THR	0	-0.022	-0.027	22.659	-0.004	-0.004	0.000	0.000	0.000	0.000
41	A	42	GLN	0	0.101	0.047	25.171	-0.002	-0.002	0.000	0.000	0.000	0.000
42	A	43	ALA	0	-0.042	-0.011	27.562	0.009	0.009	0.000	0.000	0.000	0.000
43	A	44	ARG	1	0.900	0.941	26.021	0.104	0.104	0.000	0.000	0.000	0.000
44	A	45	ALA	0	0.068	0.059	29.168	0.004	0.004	0.000	0.000	0.000	0.000
45	A	46	THR	0	0.037	0.016	31.154	0.007	0.007	0.000	0.000	0.000	0.000
46	A	47	GLN	0	-0.048	-0.039	30.000	-0.001	-0.001	0.000	0.000	0.000	0.000
47	A	48	THR	0	-0.005	-0.017	31.914	0.004	0.004	0.000	0.000	0.000	0.000
48	A	49	LEU	0	0.057	0.048	34.628	0.003	0.003	0.000	0.000	0.000	0.000
49	A	50	LYS	1	0.939	0.967	37.195	0.050	0.050	0.000	0.000	0.000	0.000
50	A	51	LYS	1	0.905	0.963	37.024	0.062	0.062	0.000	0.000	0.000	0.000
51	A	52	LEU	0	0.037	0.009	36.901	0.002	0.002	0.000	0.000	0.000	0.000
52	A	53	GLN	0	-0.041	-0.016	40.270	-0.001	-0.001	0.000	0.000	0.000	0.000
53	A	54	SER	0	-0.031	-0.007	42.212	0.003	0.003	0.000	0.000	0.000	0.000
54	A	55	ILE	0	-0.037	-0.018	40.125	0.002	0.002	0.000	0.000	0.000	0.000
55	A	56	ILE	0	-0.059	-0.039	43.500	0.002	0.002	0.000	0.000	0.000	0.000
56	A	57	ASP	-1	-0.901	-0.947	46.404	-0.043	-0.043	0.000	0.000	0.000	0.000
57	A	58	GLY	0	-0.046	-0.009	47.658	0.003	0.003	0.000	0.000	0.000	0.000
58	A	59	GLY	0	-0.027	0.002	49.157	0.002	0.002	0.000	0.000	0.000	0.000
59	A	60	VAL	0	-0.047	-0.016	46.055	-0.001	-0.001	0.000	0.000	0.000	0.000
60	A	61	ASP	-1	-0.803	-0.889	48.684	-0.064	-0.064	0.000	0.000	0.000	0.000
61	A	62	PRO	0	0.036	-0.015	49.458	-0.003	-0.003	0.000	0.000	0.000	0.000
62	A	63	ARG	1	0.933	0.979	46.813	0.077	0.077	0.000	0.000	0.000	0.000
63	A	64	SER	0	0.019	-0.023	44.977	-0.006	-0.006	0.000	0.000	0.000	0.000
64	A	65	LYS	1	0.901	0.965	44.861	0.052	0.052	0.000	0.000	0.000	0.000
65	A	66	LEU	0	-0.020	-0.008	46.010	-0.001	-0.001	0.000	0.000	0.000	0.000
66	A	67	ALA	0	0.035	0.020	41.691	-0.002	-0.002	0.000	0.000	0.000	0.000
67	A	68	TYR	0	0.060	0.007	39.777	-0.005	-0.005	0.000	0.000	0.000	0.000
68	A	69	ARG	1	0.941	0.960	41.448	0.060	0.060	0.000	0.000	0.000	0.000
69	A	70	SER	0	-0.044	-0.073	40.003	-0.001	-0.001	0.000	0.000	0.000	0.000
70	A	71	CYS	0	-0.010	0.014	33.960	0.007	0.007	0.000	0.000	0.000	0.000
71	A	72	VAL	0	-0.045	-0.025	37.643	-0.003	-0.003	0.000	0.000	0.000	0.000
72	A	73	ASP	-1	-0.848	-0.911	39.061	-0.082	-0.082	0.000	0.000	0.000	0.000
73	A	74	GLU	-1	-0.890	-0.955	35.232	-0.132	-0.132	0.000	0.000	0.000	0.000
74	A	75	TYR	0	-0.063	-0.079	30.997	-0.011	-0.011	0.000	0.000	0.000	0.000
75	A	76	GLU	-1	-0.960	-0.977	34.864	-0.073	-0.073	0.000	0.000	0.000	0.000
76	A	77	SER	0	0.008	0.013	35.869	0.001	0.001	0.000	0.000	0.000	0.000
77	A	78	ALA	0	-0.042	-0.027	30.896	-0.006	-0.006	0.000	0.000	0.000	0.000
78	A	79	ILE	0	-0.042	-0.019	31.148	-0.007	-0.007	0.000	0.000	0.000	0.000
79	A	80	GLY	0	0.088	0.047	32.267	0.002	0.002	0.000	0.000	0.000	0.000
80	A	81	ASN	0	-0.025	-0.014	30.169	0.002	0.002	0.000	0.000	0.000	0.000
81	A	82	LEU	0	-0.033	-0.036	25.918	-0.011	-0.011	0.000	0.000	0.000	0.000
82	A	83	GLU	-1	-0.973	-0.987	28.246	-0.075	-0.075	0.000	0.000	0.000	0.000
83	A	84	GLU	-1	-0.863	-0.938	30.251	-0.097	-0.097	0.000	0.000	0.000	0.000
84	A	85	ALA	0	-0.041	-0.015	25.178	-0.006	-0.006	0.000	0.000	0.000	0.000
85	A	86	PHE	0	-0.087	-0.058	25.101	-0.007	-0.007	0.000	0.000	0.000	0.000
86	A	87	GLU	-1	-0.916	-0.945	26.850	-0.059	-0.059	0.000	0.000	0.000	0.000
87	A	88	HIS	0	-0.055	-0.016	26.576	0.009	0.009	0.000	0.000	0.000	0.000
88	A	89	LEU	0	-0.018	-0.007	20.081	-0.003	-0.003	0.000	0.000	0.000	0.000
89	A	90	ALA	0	-0.024	-0.002	23.398	0.007	0.007	0.000	0.000	0.000	0.000
90	A	91	SER	0	-0.065	-0.037	25.805	0.015	0.015	0.000	0.000	0.000	0.000
91	A	92	GLY	0	-0.018	-0.013	21.984	0.004	0.004	0.000	0.000	0.000	0.000
92	A	93	ASP	-1	-0.842	-0.917	22.160	-0.222	-0.222	0.000	0.000	0.000	0.000
93	A	94	GLY	0	0.029	-0.001	20.504	-0.005	-0.005	0.000	0.000	0.000	0.000
94	A	95	MET	0	-0.017	-0.009	21.432	-0.015	-0.015	0.000	0.000	0.000	0.000
95	A	96	GLY	0	0.040	0.024	23.717	-0.001	-0.001	0.000	0.000	0.000	0.000
96	A	97	MET	0	-0.042	-0.015	19.956	0.004	0.004	0.000	0.000	0.000	0.000
97	A	98	ASN	0	-0.082	-0.038	20.097	0.018	0.018	0.000	0.000	0.000	0.000
98	A	99	MET	0	0.035	0.020	23.211	0.002	0.002	0.000	0.000	0.000	0.000
99	A	100	LYS	1	0.955	0.984	26.813	0.148	0.148	0.000	0.000	0.000	0.000
100	A	101	VAL	0	0.007	-0.010	22.228	0.009	0.009	0.000	0.000	0.000	0.000
101	A	102	SER	0	-0.032	-0.018	25.279	-0.003	-0.003	0.000	0.000	0.000	0.000
102	A	103	ALA	0	0.039	0.029	26.247	0.006	0.006	0.000	0.000	0.000	0.000
103	A	104	ALA	0	-0.006	-0.003	27.326	0.010	0.010	0.000	0.000	0.000	0.000
104	A	105	LEU	0	-0.071	-0.043	23.560	0.005	0.005	0.000	0.000	0.000	0.000
105	A	106	ASP	-1	-0.854	-0.925	27.443	-0.211	-0.211	0.000	0.000	0.000	0.000
106	A	107	GLY	0	0.034	0.043	30.588	0.010	0.010	0.000	0.000	0.000	0.000
107	A	108	ALA	0	-0.055	-0.039	28.789	0.009	0.009	0.000	0.000	0.000	0.000
108	A	109	ASP	-1	-0.837	-0.926	29.278	-0.222	-0.222	0.000	0.000	0.000	0.000
109	A	110	THR	0	0.034	0.023	31.130	0.006	0.006	0.000	0.000	0.000	0.000
110	A	112	LEU	0	-0.082	-0.058	29.819	0.007	0.007	0.000	0.000	0.000	0.000
111	A	113	ASP	-1	-0.938	-0.975	34.267	-0.163	-0.163	0.000	0.000	0.000	0.000
112	A	114	ASP	-1	-0.807	-0.826	36.477	-0.108	-0.108	0.000	0.000	0.000	0.000
113	A	115	VAL	0	-0.085	-0.061	36.766	0.010	0.010	0.000	0.000	0.000	0.000
114	A	116	LYS	1	0.921	0.979	37.342	0.144	0.144	0.000	0.000	0.000	0.000
115	A	117	ARG	1	0.878	0.930	38.844	0.114	0.114	0.000	0.000	0.000	0.000
116	A	118	LEU	0	-0.014	0.013	41.461	0.006	0.006	0.000	0.000	0.000	0.000
117	A	119	ARG	1	0.929	0.970	42.534	0.077	0.077	0.000	0.000	0.000	0.000
118	A	120	SER	0	-0.017	-0.020	42.866	-0.002	-0.002	0.000	0.000	0.000	0.000
119	A	121	VAL	0	0.031	0.025	38.166	0.001	0.001	0.000	0.000	0.000	0.000
120	A	122	ASP	-1	-0.754	-0.864	38.123	-0.073	-0.073	0.000	0.000	0.000	0.000
121	A	123	SER	0	0.011	-0.007	35.326	-0.006	-0.006	0.000	0.000	0.000	0.000
122	A	124	SER	0	-0.064	-0.043	33.870	-0.008	-0.008	0.000	0.000	0.000	0.000
123	A	125	VAL	0	0.079	0.039	33.401	-0.007	-0.007	0.000	0.000	0.000	0.000
124	A	126	VAL	0	0.008	0.015	32.422	-0.011	-0.011	0.000	0.000	0.000	0.000
125	A	127	ASN	0	-0.037	-0.036	30.070	-0.021	-0.021	0.000	0.000	0.000	0.000
126	A	128	ASN	0	-0.023	-0.027	28.812	-0.015	-0.015	0.000	0.000	0.000	0.000
127	A	129	SER	0	0.073	0.057	28.780	-0.009	-0.009	0.000	0.000	0.000	0.000
128	A	130	LYS	1	0.922	0.973	26.890	0.157	0.157	0.000	0.000	0.000	0.000
129	A	131	THR	0	-0.083	-0.042	24.198	-0.022	-0.022	0.000	0.000	0.000	0.000
130	A	132	ILE	0	0.027	0.014	23.984	-0.018	-0.018	0.000	0.000	0.000	0.000
131	A	133	LYS	1	0.897	0.953	24.595	0.235	0.235	0.000	0.000	0.000	0.000
132	A	134	ASN	0	-0.047	-0.030	20.818	-0.046	-0.046	0.000	0.000	0.000	0.000
133	A	135	LEU	0	-0.057	-0.027	19.925	-0.042	-0.042	0.000	0.000	0.000	0.000
134	A	136	CYS	0	0.014	0.018	20.185	-0.017	-0.017	0.000	0.000	0.000	0.000
135	A	137	GLY	0	0.037	0.022	19.950	-0.023	-0.023	0.000	0.000	0.000	0.000
136	A	138	ILE	0	-0.018	-0.019	14.690	-0.059	-0.059	0.000	0.000	0.000	0.000
137	A	139	ALA	0	0.012	0.004	16.111	-0.055	-0.055	0.000	0.000	0.000	0.000
138	A	140	LEU	0	-0.012	0.011	18.435	-0.011	-0.011	0.000	0.000	0.000	0.000
139	A	141	VAL	0	-0.002	-0.003	12.730	-0.034	-0.034	0.000	0.000	0.000	0.000
140	A	142	ILE	0	-0.010	-0.016	13.256	-0.060	-0.060	0.000	0.000	0.000	0.000
141	A	143	SER	0	-0.004	-0.023	14.769	-0.001	-0.001	0.000	0.000	0.000	0.000
142	A	144	ASN	0	-0.066	-0.024	16.165	-0.039	-0.039	0.000	0.000	0.000	0.000
143	A	145	MET	0	-0.040	-0.012	10.211	-0.086	-0.086	0.000	0.000	0.000	0.000
144	A	146	LEU	0	-0.051	0.002	14.241	0.004	0.004	0.000	0.000	0.000	0.000
145	A	147	PRO	0	-0.040	-0.026	15.392	-0.015	-0.015	0.000	0.000	0.000	0.000
146	A	148	ARG	1	0.986	0.996	15.827	0.442	0.442	0.000	0.000	0.000	0.000
147	A	149	ASN	0	0.024	0.018	20.716	0.039	0.039	0.000	0.000	0.000	0.000

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