FMO DATABASE

FMODB ID: Q19LY

Calculation Name: 1WRJ-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 1WRJ

Chain ID: A

ChEMBL ID:

UniProt ID: Q973C7

Base Structure: X-ray

Registration Date: 2023-06-21

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	149
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-1510543.803327
FMO2-HF: Nuclear repulsion	1450219.987119
FMO2-HF: Total energy	-60323.816208
FMO2-MP2: Total energy	-60499.814445

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:MET)

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

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.
-15.076	-12.778	19.049	-8.66	-12.684	-0.059

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

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : -0.026 / q_NPA : -0.010

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	VAL	0	-0.001	0.020	2.512	-2.570	0.774	2.001	-1.921	-3.423	-0.003
4	A	4	TYR	0	-0.019	-0.054	4.049	0.325	0.396	0.004	-0.002	-0.073	0.000
5	A	5	GLY	0	0.057	0.021	7.786	0.095	0.095	0.000	0.000	0.000	0.000
6	A	6	LEU	0	-0.087	-0.042	10.054	0.014	0.014	0.000	0.000	0.000	0.000
7	A	7	TYR	0	-0.018	-0.028	13.874	0.047	0.047	0.000	0.000	0.000	0.000
8	A	8	LYS	1	0.942	0.952	16.504	0.317	0.317	0.000	0.000	0.000	0.000
9	A	9	SER	0	0.041	0.032	20.347	0.031	0.031	0.000	0.000	0.000	0.000
10	A	10	PRO	0	0.016	-0.003	22.430	0.004	0.004	0.000	0.000	0.000	0.000
11	A	11	PHE	0	-0.026	-0.018	24.644	0.014	0.014	0.000	0.000	0.000	0.000
12	A	12	GLY	0	0.012	0.020	23.878	-0.005	-0.005	0.000	0.000	0.000	0.000
13	A	13	PRO	0	-0.027	-0.004	19.409	-0.002	-0.002	0.000	0.000	0.000	0.000
14	A	14	ILE	0	-0.022	-0.015	15.767	0.000	0.000	0.000	0.000	0.000	0.000
15	A	15	THR	0	0.001	0.003	12.525	-0.026	-0.026	0.000	0.000	0.000	0.000
16	A	16	VAL	0	-0.043	-0.027	9.972	0.048	0.048	0.000	0.000	0.000	0.000
17	A	17	ALA	0	0.034	0.017	7.394	-0.083	-0.083	0.000	0.000	0.000	0.000
18	A	18	LYS	1	0.896	0.965	4.112	1.243	1.440	-0.001	-0.021	-0.175	0.000
19	A	19	ASN	0	0.068	0.030	2.684	-2.101	-0.403	0.486	-0.841	-1.342	-0.002
20	A	20	GLU	-1	-0.787	-0.884	1.811	-10.575	-15.459	16.041	-5.142	-6.015	-0.044
21	A	21	LYS	1	0.781	0.886	4.189	1.623	1.916	0.008	-0.047	-0.253	0.000
22	A	22	GLY	0	0.017	-0.006	6.762	0.508	0.508	0.000	0.000	0.000	0.000
23	A	23	PHE	0	-0.005	-0.014	6.948	-0.658	-0.658	0.000	0.000	0.000	0.000
24	A	24	VAL	0	-0.051	-0.028	7.573	0.132	0.132	0.000	0.000	0.000	0.000
25	A	25	MET	0	-0.054	-0.030	10.025	0.226	0.226	0.000	0.000	0.000	0.000
26	A	26	LEU	0	-0.003	0.007	11.261	-0.071	-0.071	0.000	0.000	0.000	0.000
27	A	27	ASP	-1	-0.761	-0.855	14.116	-0.495	-0.495	0.000	0.000	0.000	0.000
28	A	28	PHE	0	0.032	0.016	17.205	-0.018	-0.018	0.000	0.000	0.000	0.000
29	A	29	CYS	0	-0.108	-0.073	16.387	0.067	0.067	0.000	0.000	0.000	0.000
30	A	30	ASP	-1	-0.885	-0.930	17.729	-0.554	-0.554	0.000	0.000	0.000	0.000
31	A	32	ALA	0	0.036	0.028	11.840	-0.097	-0.097	0.000	0.000	0.000	0.000
32	A	33	GLU	-1	-0.822	-0.879	10.065	-1.253	-1.253	0.000	0.000	0.000	0.000
33	A	34	ARG	1	0.942	0.955	10.428	0.335	0.335	0.000	0.000	0.000	0.000
34	A	35	SER	0	-0.001	-0.005	10.503	0.098	0.098	0.000	0.000	0.000	0.000
35	A	36	SER	0	-0.065	-0.036	5.662	-0.033	-0.033	0.000	0.000	0.000	0.000
36	A	37	LEU	0	-0.060	-0.008	6.663	-0.499	-0.499	0.000	0.000	0.000	0.000
37	A	38	ASP	-1	-0.825	-0.921	6.098	-0.349	-0.349	0.000	0.000	0.000	0.000
38	A	39	ASN	0	0.020	-0.018	7.168	-0.346	-0.346	0.000	0.000	0.000	0.000
39	A	40	ASP	-1	-0.836	-0.897	8.920	-0.217	-0.217	0.000	0.000	0.000	0.000
40	A	41	TYR	0	-0.060	-0.030	2.837	-1.988	-0.409	0.510	-0.686	-1.403	-0.010
41	A	42	PHE	0	-0.072	-0.047	6.320	0.016	0.016	0.000	0.000	0.000	0.000
42	A	43	THR	0	0.021	0.021	9.331	0.050	0.050	0.000	0.000	0.000	0.000
43	A	44	ASP	-1	-0.860	-0.937	12.382	-0.071	-0.071	0.000	0.000	0.000	0.000
44	A	45	PHE	0	-0.090	-0.034	12.090	-0.007	-0.007	0.000	0.000	0.000	0.000
45	A	46	PHE	0	0.011	-0.006	11.471	-0.002	-0.002	0.000	0.000	0.000	0.000
46	A	47	TYR	0	0.071	0.046	15.349	0.031	0.031	0.000	0.000	0.000	0.000
47	A	48	LYS	1	0.802	0.880	14.674	0.302	0.302	0.000	0.000	0.000	0.000
48	A	49	LEU	0	-0.019	-0.011	16.217	0.007	0.007	0.000	0.000	0.000	0.000
49	A	50	ASP	-1	-0.814	-0.883	19.321	-0.239	-0.239	0.000	0.000	0.000	0.000
50	A	51	LEU	0	-0.024	-0.009	21.529	0.015	0.015	0.000	0.000	0.000	0.000
51	A	52	TYR	0	-0.058	-0.051	21.954	0.005	0.005	0.000	0.000	0.000	0.000
52	A	53	PHE	0	-0.005	-0.027	20.226	0.003	0.003	0.000	0.000	0.000	0.000
53	A	54	GLU	-1	-0.873	-0.915	25.005	-0.121	-0.121	0.000	0.000	0.000	0.000
54	A	55	GLY	0	0.004	0.008	27.125	0.014	0.014	0.000	0.000	0.000	0.000
55	A	56	LYS	1	0.775	0.882	26.565	0.137	0.137	0.000	0.000	0.000	0.000
56	A	57	LYS	1	0.906	0.949	26.456	0.111	0.111	0.000	0.000	0.000	0.000
57	A	58	VAL	0	-0.013	0.001	21.411	0.014	0.014	0.000	0.000	0.000	0.000
58	A	59	ASP	-1	-0.831	-0.897	20.539	-0.256	-0.256	0.000	0.000	0.000	0.000
59	A	60	LEU	0	-0.015	-0.022	18.300	-0.007	-0.007	0.000	0.000	0.000	0.000
60	A	61	THR	0	-0.095	-0.061	16.878	-0.062	-0.062	0.000	0.000	0.000	0.000
61	A	62	GLU	-1	-0.755	-0.889	11.540	-0.391	-0.391	0.000	0.000	0.000	0.000
62	A	63	PRO	0	-0.009	0.003	10.158	-0.031	-0.031	0.000	0.000	0.000	0.000
63	A	64	VAL	0	-0.006	-0.002	10.766	-0.141	-0.141	0.000	0.000	0.000	0.000
64	A	65	ASP	-1	-0.825	-0.895	8.115	-1.690	-1.690	0.000	0.000	0.000	0.000
65	A	66	PHE	0	0.003	-0.041	10.629	0.015	0.015	0.000	0.000	0.000	0.000
66	A	67	LYS	1	0.952	0.979	9.424	1.224	1.224	0.000	0.000	0.000	0.000
67	A	68	PRO	0	0.005	0.011	11.780	0.105	0.105	0.000	0.000	0.000	0.000
68	A	69	PHE	0	-0.041	-0.004	14.208	0.108	0.108	0.000	0.000	0.000	0.000
69	A	70	ASN	0	0.053	0.013	17.654	0.007	0.007	0.000	0.000	0.000	0.000
70	A	71	GLU	-1	-0.828	-0.917	20.565	-0.227	-0.227	0.000	0.000	0.000	0.000
71	A	72	PHE	0	0.029	0.010	22.559	0.000	0.000	0.000	0.000	0.000	0.000
72	A	73	ARG	1	0.910	0.964	21.268	0.399	0.399	0.000	0.000	0.000	0.000
73	A	74	ILE	0	0.010	0.020	17.698	-0.001	-0.001	0.000	0.000	0.000	0.000
74	A	75	ARG	1	0.831	0.909	20.692	0.213	0.213	0.000	0.000	0.000	0.000
75	A	76	VAL	0	0.008	0.007	24.037	0.011	0.011	0.000	0.000	0.000	0.000
76	A	77	PHE	0	-0.008	-0.018	18.375	0.015	0.015	0.000	0.000	0.000	0.000
77	A	78	LYS	1	0.926	0.968	17.067	0.409	0.409	0.000	0.000	0.000	0.000
78	A	79	GLU	-1	-0.854	-0.881	21.893	-0.169	-0.169	0.000	0.000	0.000	0.000
79	A	80	VAL	0	0.005	-0.017	23.100	0.016	0.016	0.000	0.000	0.000	0.000
80	A	81	MET	0	-0.053	-0.021	16.491	-0.003	-0.003	0.000	0.000	0.000	0.000
81	A	82	ARG	1	0.818	0.885	21.933	0.207	0.207	0.000	0.000	0.000	0.000
82	A	83	ILE	0	-0.077	-0.011	25.115	0.022	0.022	0.000	0.000	0.000	0.000
83	A	84	LYS	1	0.911	0.942	25.607	0.120	0.120	0.000	0.000	0.000	0.000
84	A	85	TRP	0	0.036	0.034	24.605	0.003	0.003	0.000	0.000	0.000	0.000
85	A	86	GLY	0	0.030	0.008	27.004	0.016	0.016	0.000	0.000	0.000	0.000
86	A	87	GLU	-1	-0.863	-0.900	29.539	-0.144	-0.144	0.000	0.000	0.000	0.000
87	A	88	VAL	0	0.039	0.013	29.803	-0.015	-0.015	0.000	0.000	0.000	0.000
88	A	89	ARG	1	0.829	0.903	30.732	0.164	0.164	0.000	0.000	0.000	0.000
89	A	90	THR	0	-0.007	-0.011	32.164	-0.011	-0.011	0.000	0.000	0.000	0.000
90	A	91	TYR	0	0.002	-0.016	29.280	0.003	0.003	0.000	0.000	0.000	0.000
91	A	92	LYS	1	0.822	0.897	32.731	0.124	0.124	0.000	0.000	0.000	0.000
92	A	93	GLN	0	0.058	0.029	34.152	-0.004	-0.004	0.000	0.000	0.000	0.000
93	A	94	VAL	0	0.045	0.020	28.176	0.002	0.002	0.000	0.000	0.000	0.000
94	A	95	ALA	0	-0.037	-0.023	31.224	-0.004	-0.004	0.000	0.000	0.000	0.000
95	A	96	ASP	-1	-0.793	-0.868	33.100	-0.128	-0.128	0.000	0.000	0.000	0.000
96	A	97	ALA	0	-0.020	0.008	31.108	0.007	0.007	0.000	0.000	0.000	0.000
97	A	98	VAL	0	0.004	-0.003	27.502	0.005	0.005	0.000	0.000	0.000	0.000
98	A	99	LYS	1	0.831	0.916	30.635	0.137	0.137	0.000	0.000	0.000	0.000
99	A	100	THR	0	0.008	0.013	30.804	-0.002	-0.002	0.000	0.000	0.000	0.000
100	A	101	SER	0	0.023	0.021	33.871	0.008	0.008	0.000	0.000	0.000	0.000
101	A	102	PRO	0	0.076	0.012	33.455	-0.013	-0.013	0.000	0.000	0.000	0.000
102	A	103	ARG	1	0.992	0.993	32.772	0.154	0.154	0.000	0.000	0.000	0.000
103	A	104	ALA	0	-0.005	0.020	30.883	-0.014	-0.014	0.000	0.000	0.000	0.000
104	A	105	VAL	0	0.055	0.033	28.319	-0.021	-0.021	0.000	0.000	0.000	0.000
105	A	106	GLY	0	0.025	0.011	27.835	-0.021	-0.021	0.000	0.000	0.000	0.000
106	A	107	THR	0	-0.023	-0.031	27.941	-0.021	-0.021	0.000	0.000	0.000	0.000
107	A	108	ALA	0	-0.025	0.001	25.133	-0.028	-0.028	0.000	0.000	0.000	0.000
108	A	109	LEU	0	0.041	0.002	23.380	-0.041	-0.041	0.000	0.000	0.000	0.000
109	A	110	SER	0	-0.089	-0.038	23.401	-0.028	-0.028	0.000	0.000	0.000	0.000
110	A	111	LYS	1	0.863	0.925	18.720	0.608	0.608	0.000	0.000	0.000	0.000
111	A	112	ASN	0	0.027	-0.002	18.335	-0.115	-0.115	0.000	0.000	0.000	0.000
112	A	113	ASN	0	0.018	0.000	14.739	0.071	0.071	0.000	0.000	0.000	0.000
113	A	114	VAL	0	0.042	0.014	12.859	-0.075	-0.075	0.000	0.000	0.000	0.000
114	A	115	LEU	0	-0.032	-0.006	15.502	0.071	0.071	0.000	0.000	0.000	0.000
115	A	116	LEU	0	0.005	0.006	17.638	0.052	0.052	0.000	0.000	0.000	0.000
116	A	117	ILE	0	0.051	0.040	12.579	0.033	0.033	0.000	0.000	0.000	0.000
117	A	118	ILE	0	-0.032	-0.008	16.557	0.049	0.049	0.000	0.000	0.000	0.000
118	A	119	PRO	0	0.025	0.035	19.113	-0.011	-0.011	0.000	0.000	0.000	0.000
119	A	120	CYS	0	-0.065	-0.029	22.162	0.028	0.028	0.000	0.000	0.000	0.000
120	A	121	HIS	0	0.019	-0.007	23.042	0.000	0.000	0.000	0.000	0.000	0.000
121	A	122	ARG	1	0.832	0.889	23.275	0.273	0.273	0.000	0.000	0.000	0.000
122	A	123	VAL	0	-0.029	-0.007	26.737	0.018	0.018	0.000	0.000	0.000	0.000
123	A	124	ILE	0	0.024	0.026	29.348	-0.009	-0.009	0.000	0.000	0.000	0.000
124	A	125	GLY	0	-0.009	-0.021	32.645	0.002	0.002	0.000	0.000	0.000	0.000
125	A	126	GLU	-1	-0.848	-0.931	35.831	-0.136	-0.136	0.000	0.000	0.000	0.000
126	A	127	LYS	1	0.963	0.985	39.072	0.139	0.139	0.000	0.000	0.000	0.000
127	A	128	SER	0	-0.018	-0.010	37.695	0.000	0.000	0.000	0.000	0.000	0.000
128	A	129	LEU	0	0.127	0.067	33.427	-0.003	-0.003	0.000	0.000	0.000	0.000
129	A	130	GLY	0	0.013	0.020	32.781	-0.010	-0.010	0.000	0.000	0.000	0.000
130	A	131	GLY	0	0.005	0.001	30.641	-0.003	-0.003	0.000	0.000	0.000	0.000
131	A	132	TYR	0	0.062	0.002	22.107	0.002	0.002	0.000	0.000	0.000	0.000
132	A	133	SER	0	0.001	0.004	21.772	0.026	0.026	0.000	0.000	0.000	0.000
133	A	134	ARG	1	0.853	0.907	20.198	0.475	0.475	0.000	0.000	0.000	0.000
134	A	135	GLY	0	0.035	0.026	25.174	0.016	0.016	0.000	0.000	0.000	0.000
135	A	136	VAL	0	-0.011	-0.023	28.782	-0.003	-0.003	0.000	0.000	0.000	0.000
136	A	137	GLU	-1	-0.835	-0.900	31.386	-0.202	-0.202	0.000	0.000	0.000	0.000
137	A	138	LEU	0	0.074	0.039	24.017	0.008	0.008	0.000	0.000	0.000	0.000
138	A	139	LYS	1	0.738	0.860	27.781	0.242	0.242	0.000	0.000	0.000	0.000
139	A	140	ARG	1	0.798	0.855	28.757	0.173	0.173	0.000	0.000	0.000	0.000
140	A	141	LYS	1	0.861	0.931	29.268	0.217	0.217	0.000	0.000	0.000	0.000
141	A	142	LEU	0	-0.008	-0.005	23.904	0.004	0.004	0.000	0.000	0.000	0.000
142	A	143	LEU	0	-0.048	-0.022	27.645	0.006	0.006	0.000	0.000	0.000	0.000
143	A	144	GLU	-1	-0.762	-0.845	30.454	-0.159	-0.159	0.000	0.000	0.000	0.000
144	A	145	LEU	0	-0.031	0.005	25.664	0.009	0.009	0.000	0.000	0.000	0.000
145	A	146	GLU	-1	-0.741	-0.817	25.634	-0.237	-0.237	0.000	0.000	0.000	0.000
146	A	147	GLY	0	0.009	0.000	29.747	0.009	0.009	0.000	0.000	0.000	0.000
147	A	148	ILE	0	-0.100	-0.043	30.289	0.009	0.009	0.000	0.000	0.000	0.000
148	A	149	ASP	-1	-0.911	-0.952	34.312	-0.124	-0.124	0.000	0.000	0.000	0.000
149	A	150	VAL	0	-0.064	-0.031	34.935	-0.002	-0.002	0.000	0.000	0.000	0.000

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