FMO DATABASE

FMODB ID: 6YV6Z

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

Total energy (hartree)

FMO2-HF: Electronic energy	-1300506.713503
FMO2-HF: Nuclear repulsion	1242413.803591
FMO2-HF: Total energy	-58092.909912
FMO2-MP2: Total energy	-58256.056521

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.
-3.613	-0.967	0.04	-1.139	-1.547	0.001

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	-0.799	-0.916	3.600	-5.289	-3.501	0.000	-0.852	-0.936	0.003
4	A	4	MET	0	-0.037	0.000	6.126	0.419	0.419	0.000	0.000	0.000	0.000
5	A	5	SER	0	-0.040	-0.033	3.155	0.209	0.851	0.036	-0.255	-0.423	-0.002
6	A	6	THR	0	-0.042	-0.026	3.575	0.450	0.666	0.004	-0.032	-0.188	0.000
7	A	7	ILE	0	0.021	0.021	6.249	0.133	0.133	0.000	0.000	0.000	0.000
8	A	8	CYS	0	0.019	0.016	9.254	0.145	0.145	0.000	0.000	0.000	0.000
9	A	9	ASP	-1	-0.847	-0.892	9.978	-0.858	-0.858	0.000	0.000	0.000	0.000
10	A	10	LYS	1	0.871	0.930	8.634	1.318	1.318	0.000	0.000	0.000	0.000
11	A	11	THR	0	-0.067	-0.036	14.163	0.063	0.063	0.000	0.000	0.000	0.000
12	A	12	LEU	0	0.066	0.018	16.744	0.014	0.014	0.000	0.000	0.000	0.000
13	A	13	ASN	0	-0.019	0.002	19.108	0.035	0.035	0.000	0.000	0.000	0.000
14	A	14	PRO	0	0.098	0.048	14.469	0.017	0.017	0.000	0.000	0.000	0.000
15	A	15	SER	0	0.017	0.003	15.563	0.026	0.026	0.000	0.000	0.000	0.000
16	A	16	PHE	0	-0.024	-0.013	17.619	0.033	0.033	0.000	0.000	0.000	0.000
17	A	18	LEU	0	0.058	0.024	11.031	0.022	0.022	0.000	0.000	0.000	0.000
18	A	19	LYS	1	0.956	0.987	14.144	-0.014	-0.014	0.000	0.000	0.000	0.000
19	A	20	PHE	0	-0.011	0.008	16.196	0.043	0.043	0.000	0.000	0.000	0.000
20	A	21	LEU	0	0.024	-0.007	10.880	0.025	0.025	0.000	0.000	0.000	0.000
21	A	22	ASN	0	-0.040	-0.031	11.923	0.134	0.134	0.000	0.000	0.000	0.000
22	A	23	THR	0	-0.079	-0.050	14.489	0.030	0.030	0.000	0.000	0.000	0.000
23	A	24	LYS	1	0.855	0.928	16.938	-0.036	-0.036	0.000	0.000	0.000	0.000
24	A	25	PHE	0	-0.040	0.001	11.847	0.002	0.002	0.000	0.000	0.000	0.000
25	A	26	ALA	0	0.028	0.023	11.769	-0.002	-0.002	0.000	0.000	0.000	0.000
26	A	27	SER	0	0.053	0.014	11.227	0.087	0.087	0.000	0.000	0.000	0.000
27	A	28	ALA	0	0.038	0.006	7.360	-0.110	-0.110	0.000	0.000	0.000	0.000
28	A	29	ASN	0	-0.038	-0.010	9.208	-0.233	-0.233	0.000	0.000	0.000	0.000
29	A	30	LEU	0	0.101	0.035	10.094	0.032	0.032	0.000	0.000	0.000	0.000
30	A	31	GLN	0	0.056	0.033	13.280	-0.011	-0.011	0.000	0.000	0.000	0.000
31	A	32	ALA	0	-0.026	-0.020	15.284	0.021	0.021	0.000	0.000	0.000	0.000
32	A	33	LEU	0	-0.016	-0.010	11.827	0.022	0.022	0.000	0.000	0.000	0.000
33	A	34	ALA	0	0.037	0.031	15.485	0.009	0.009	0.000	0.000	0.000	0.000
34	A	35	LYS	1	0.887	0.933	17.984	0.033	0.033	0.000	0.000	0.000	0.000
35	A	36	THR	0	-0.003	-0.007	17.523	0.010	0.010	0.000	0.000	0.000	0.000
36	A	37	THR	0	-0.026	-0.039	17.155	0.015	0.015	0.000	0.000	0.000	0.000
37	A	38	LEU	0	0.058	0.046	19.697	0.007	0.007	0.000	0.000	0.000	0.000
38	A	39	ASP	-1	-0.814	-0.878	22.922	-0.001	-0.001	0.000	0.000	0.000	0.000
39	A	40	SER	0	-0.078	-0.046	21.836	0.017	0.017	0.000	0.000	0.000	0.000
40	A	41	THR	0	-0.017	-0.024	22.734	0.002	0.002	0.000	0.000	0.000	0.000
41	A	42	GLN	0	0.083	0.036	25.163	0.002	0.002	0.000	0.000	0.000	0.000
42	A	43	ALA	0	-0.035	-0.001	27.521	0.006	0.006	0.000	0.000	0.000	0.000
43	A	44	ARG	1	0.898	0.936	26.077	-0.002	-0.002	0.000	0.000	0.000	0.000
44	A	45	ALA	0	0.062	0.057	29.120	0.003	0.003	0.000	0.000	0.000	0.000
45	A	46	THR	0	0.029	0.006	31.145	0.003	0.003	0.000	0.000	0.000	0.000
46	A	47	GLN	0	-0.023	-0.019	30.061	0.001	0.001	0.000	0.000	0.000	0.000
47	A	48	THR	0	-0.006	-0.023	31.910	0.004	0.004	0.000	0.000	0.000	0.000
48	A	49	LEU	0	0.043	0.042	34.589	0.002	0.002	0.000	0.000	0.000	0.000
49	A	50	LYS	1	0.932	0.965	37.156	0.011	0.011	0.000	0.000	0.000	0.000
50	A	51	LYS	1	0.868	0.945	37.021	0.005	0.005	0.000	0.000	0.000	0.000
51	A	52	LEU	0	0.015	-0.001	36.934	0.001	0.001	0.000	0.000	0.000	0.000
52	A	53	GLN	0	-0.038	-0.022	40.240	-0.002	-0.002	0.000	0.000	0.000	0.000
53	A	54	SER	0	-0.017	0.002	42.118	0.002	0.002	0.000	0.000	0.000	0.000
54	A	55	ILE	0	-0.051	-0.023	39.917	0.001	0.001	0.000	0.000	0.000	0.000
55	A	56	ILE	0	-0.055	-0.035	43.480	0.000	0.000	0.000	0.000	0.000	0.000
56	A	57	ASP	-1	-0.879	-0.938	46.375	-0.009	-0.009	0.000	0.000	0.000	0.000
57	A	58	GLY	0	-0.037	-0.001	47.600	0.001	0.001	0.000	0.000	0.000	0.000
58	A	59	GLY	0	-0.038	-0.005	49.088	0.001	0.001	0.000	0.000	0.000	0.000
59	A	60	VAL	0	-0.049	-0.022	46.008	0.000	0.000	0.000	0.000	0.000	0.000
60	A	61	ASP	-1	-0.783	-0.867	48.618	-0.019	-0.019	0.000	0.000	0.000	0.000
61	A	62	PRO	0	0.050	-0.009	49.450	-0.001	-0.001	0.000	0.000	0.000	0.000
62	A	63	ARG	1	0.931	0.983	46.571	0.031	0.031	0.000	0.000	0.000	0.000
63	A	64	SER	0	-0.002	-0.045	44.977	-0.003	-0.003	0.000	0.000	0.000	0.000
64	A	65	LYS	1	0.876	0.956	44.863	0.014	0.014	0.000	0.000	0.000	0.000
65	A	66	LEU	0	-0.013	-0.005	46.026	-0.001	-0.001	0.000	0.000	0.000	0.000
66	A	67	ALA	0	0.033	0.019	41.823	-0.002	-0.002	0.000	0.000	0.000	0.000
67	A	68	TYR	0	0.050	-0.003	39.849	-0.002	-0.002	0.000	0.000	0.000	0.000
68	A	69	ARG	1	0.953	0.969	41.463	0.023	0.023	0.000	0.000	0.000	0.000
69	A	70	SER	0	0.049	0.021	40.544	0.000	0.000	0.000	0.000	0.000	0.000
70	A	71	CYS	0	-0.047	-0.008	34.029	0.006	0.006	0.000	0.000	0.000	0.000
71	A	72	VAL	0	-0.037	-0.022	37.679	-0.002	-0.002	0.000	0.000	0.000	0.000
72	A	73	ASP	-1	-0.859	-0.913	39.102	-0.041	-0.041	0.000	0.000	0.000	0.000
73	A	74	GLU	-1	-0.872	-0.944	35.288	-0.075	-0.075	0.000	0.000	0.000	0.000
74	A	75	TYR	0	-0.057	-0.070	31.042	-0.006	-0.006	0.000	0.000	0.000	0.000
75	A	76	GLU	-1	-0.963	-0.975	34.908	-0.033	-0.033	0.000	0.000	0.000	0.000
76	A	77	SER	0	0.004	0.006	36.019	-0.001	-0.001	0.000	0.000	0.000	0.000
77	A	78	ALA	0	-0.041	-0.027	30.978	-0.006	-0.006	0.000	0.000	0.000	0.000
78	A	79	ILE	0	-0.039	-0.020	31.221	-0.005	-0.005	0.000	0.000	0.000	0.000
79	A	80	GLY	0	0.090	0.052	32.328	0.000	0.000	0.000	0.000	0.000	0.000
80	A	81	ASN	0	-0.022	-0.014	30.247	-0.006	-0.006	0.000	0.000	0.000	0.000
81	A	82	LEU	0	-0.032	-0.031	25.946	-0.010	-0.010	0.000	0.000	0.000	0.000
82	A	83	GLU	-1	-0.969	-0.986	28.323	-0.044	-0.044	0.000	0.000	0.000	0.000
83	A	84	GLU	-1	-0.818	-0.900	30.341	-0.083	-0.083	0.000	0.000	0.000	0.000
84	A	85	ALA	0	-0.019	-0.009	25.297	-0.008	-0.008	0.000	0.000	0.000	0.000
85	A	86	PHE	0	-0.065	-0.048	24.919	-0.009	-0.009	0.000	0.000	0.000	0.000
86	A	87	GLU	-1	-0.913	-0.943	26.885	-0.054	-0.054	0.000	0.000	0.000	0.000
87	A	88	HIS	0	-0.075	-0.036	26.516	0.006	0.006	0.000	0.000	0.000	0.000
88	A	89	LEU	0	-0.027	-0.009	20.054	-0.009	-0.009	0.000	0.000	0.000	0.000
89	A	90	ALA	0	-0.017	0.005	23.398	-0.002	-0.002	0.000	0.000	0.000	0.000
90	A	91	SER	0	-0.060	-0.040	25.805	0.007	0.007	0.000	0.000	0.000	0.000
91	A	92	GLY	0	-0.025	-0.017	21.986	-0.003	-0.003	0.000	0.000	0.000	0.000
92	A	93	ASP	-1	-0.804	-0.882	22.160	-0.214	-0.214	0.000	0.000	0.000	0.000
93	A	94	GLY	0	0.030	-0.003	20.694	0.004	0.004	0.000	0.000	0.000	0.000
94	A	95	MET	0	-0.019	-0.009	21.632	-0.003	-0.003	0.000	0.000	0.000	0.000
95	A	96	GLY	0	0.039	0.018	23.946	0.006	0.006	0.000	0.000	0.000	0.000
96	A	97	MET	0	-0.047	-0.017	19.858	0.008	0.008	0.000	0.000	0.000	0.000
97	A	98	ASN	0	-0.083	-0.038	20.302	0.021	0.021	0.000	0.000	0.000	0.000
98	A	99	MET	0	0.040	0.018	23.395	0.008	0.008	0.000	0.000	0.000	0.000
99	A	100	LYS	1	0.877	0.939	27.006	0.110	0.110	0.000	0.000	0.000	0.000
100	A	101	VAL	0	-0.005	-0.017	22.216	0.013	0.013	0.000	0.000	0.000	0.000
101	A	102	SER	0	-0.016	-0.011	25.514	0.002	0.002	0.000	0.000	0.000	0.000
102	A	103	ALA	0	0.014	0.022	26.400	0.008	0.008	0.000	0.000	0.000	0.000
103	A	104	ALA	0	-0.001	-0.004	27.407	0.010	0.010	0.000	0.000	0.000	0.000
104	A	105	LEU	0	-0.076	-0.043	23.672	0.010	0.010	0.000	0.000	0.000	0.000
105	A	106	ASP	-1	-0.851	-0.922	27.538	-0.126	-0.126	0.000	0.000	0.000	0.000
106	A	107	GLY	0	0.053	0.056	30.702	0.008	0.008	0.000	0.000	0.000	0.000
107	A	108	ALA	0	-0.064	-0.040	28.831	0.008	0.008	0.000	0.000	0.000	0.000
108	A	109	ASP	-1	-0.814	-0.905	28.852	-0.107	-0.107	0.000	0.000	0.000	0.000
109	A	110	THR	0	0.001	0.003	31.202	0.005	0.005	0.000	0.000	0.000	0.000
110	A	112	LEU	0	-0.073	-0.051	29.783	0.007	0.007	0.000	0.000	0.000	0.000
111	A	113	ASP	-1	-0.799	-0.897	34.299	-0.068	-0.068	0.000	0.000	0.000	0.000
112	A	114	ASP	-1	-0.835	-0.889	36.536	-0.050	-0.050	0.000	0.000	0.000	0.000
113	A	115	VAL	0	-0.097	-0.064	36.742	0.006	0.006	0.000	0.000	0.000	0.000
114	A	116	LYS	1	0.753	0.880	37.214	0.071	0.071	0.000	0.000	0.000	0.000
115	A	117	ARG	1	0.881	0.938	38.865	0.046	0.046	0.000	0.000	0.000	0.000
116	A	118	LEU	0	-0.016	0.009	41.407	0.003	0.003	0.000	0.000	0.000	0.000
117	A	119	ARG	1	0.928	0.969	42.520	0.019	0.019	0.000	0.000	0.000	0.000
118	A	120	SER	0	0.004	-0.009	42.825	0.002	0.002	0.000	0.000	0.000	0.000
119	A	121	VAL	0	0.014	0.013	38.179	-0.001	-0.001	0.000	0.000	0.000	0.000
120	A	122	ASP	-1	-0.731	-0.842	38.037	-0.004	-0.004	0.000	0.000	0.000	0.000
121	A	123	SER	0	0.030	0.001	35.241	-0.003	-0.003	0.000	0.000	0.000	0.000
122	A	124	SER	0	-0.061	-0.053	33.779	-0.002	-0.002	0.000	0.000	0.000	0.000
123	A	125	VAL	0	0.090	0.047	33.339	-0.003	-0.003	0.000	0.000	0.000	0.000
124	A	126	VAL	0	0.016	0.026	32.532	-0.006	-0.006	0.000	0.000	0.000	0.000
125	A	127	ASN	0	-0.019	-0.028	29.985	-0.011	-0.011	0.000	0.000	0.000	0.000
126	A	128	ASN	0	0.004	-0.007	28.759	0.000	0.000	0.000	0.000	0.000	0.000
127	A	129	SER	0	0.054	0.025	28.754	-0.007	-0.007	0.000	0.000	0.000	0.000
128	A	130	LYS	1	0.897	0.968	26.806	0.026	0.026	0.000	0.000	0.000	0.000
129	A	131	THR	0	-0.091	-0.050	24.369	-0.007	-0.007	0.000	0.000	0.000	0.000
130	A	132	ILE	0	0.029	0.013	23.967	-0.009	-0.009	0.000	0.000	0.000	0.000
131	A	133	LYS	1	0.891	0.942	24.625	0.108	0.108	0.000	0.000	0.000	0.000
132	A	134	ASN	0	-0.046	-0.030	20.719	-0.031	-0.031	0.000	0.000	0.000	0.000
133	A	135	LEU	0	-0.062	-0.030	19.970	-0.023	-0.023	0.000	0.000	0.000	0.000
134	A	136	CYS	0	0.009	0.013	20.227	-0.018	-0.018	0.000	0.000	0.000	0.000
135	A	137	GLY	0	0.038	0.020	20.041	-0.025	-0.025	0.000	0.000	0.000	0.000
136	A	138	ILE	0	-0.021	-0.022	14.745	-0.042	-0.042	0.000	0.000	0.000	0.000
137	A	139	ALA	0	0.013	0.004	16.208	-0.053	-0.053	0.000	0.000	0.000	0.000
138	A	140	LEU	0	-0.009	0.024	18.569	-0.024	-0.024	0.000	0.000	0.000	0.000
139	A	141	VAL	0	0.008	0.001	12.921	-0.041	-0.041	0.000	0.000	0.000	0.000
140	A	142	ILE	0	-0.017	-0.017	13.341	-0.073	-0.073	0.000	0.000	0.000	0.000
141	A	143	SER	0	-0.004	-0.032	14.918	-0.029	-0.029	0.000	0.000	0.000	0.000
142	A	144	ASN	0	-0.067	-0.022	16.464	-0.049	-0.049	0.000	0.000	0.000	0.000
143	A	145	MET	0	-0.041	-0.020	10.258	-0.102	-0.102	0.000	0.000	0.000	0.000
144	A	146	LEU	0	-0.050	0.005	14.281	-0.036	-0.036	0.000	0.000	0.000	0.000
145	A	147	PRO	0	-0.049	-0.034	15.398	-0.017	-0.017	0.000	0.000	0.000	0.000
146	A	148	ARG	1	0.992	1.005	15.523	0.532	0.532	0.000	0.000	0.000	0.000
147	A	149	ASN	0	0.022	0.015	20.772	0.019	0.019	0.000	0.000	0.000	0.000

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