FMO DATABASE

FMODB ID: 535NZ

Calculation Name: 3CXJ-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 3CXJ

Chain ID: A

ChEMBL ID:

UniProt ID: O27461

Base Structure: X-ray

Registration Date: 2023-03-14

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	144
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-1392648.547487
FMO2-HF: Nuclear repulsion	1332928.952285
FMO2-HF: Total energy	-59719.595203
FMO2-MP2: Total energy	-59892.343773

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:3:LEU)

Summations of interaction energy for fragment #1(A:3:LEU)

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.
-4.313	0.727	1.119	-1.983	-4.176	-0.001

Interaction energy analysis for fragmet #1(A:3:LEU)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : 0.034 / q_NPA : 0.008

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	5	GLN	0	0.082	0.035	2.691	-5.201	-2.129	0.493	-1.292	-2.274	0.004
4	A	6	GLU	-1	-0.916	-0.948	2.722	-3.272	-1.817	0.622	-0.603	-1.474	-0.005
5	A	7	MET	0	-0.037	-0.017	3.729	0.423	0.936	0.004	-0.088	-0.428	0.000
6	A	8	ILE	0	-0.007	0.008	6.468	0.353	0.353	0.000	0.000	0.000	0.000
7	A	9	LYS	1	0.886	0.952	6.787	0.756	0.756	0.000	0.000	0.000	0.000
8	A	10	LYS	1	0.882	0.929	7.921	0.978	0.978	0.000	0.000	0.000	0.000
9	A	11	TRP	0	-0.026	-0.036	8.408	0.103	0.103	0.000	0.000	0.000	0.000
10	A	12	LEU	0	0.000	0.000	11.399	0.091	0.091	0.000	0.000	0.000	0.000
11	A	13	ASP	-1	-0.805	-0.912	12.968	-0.321	-0.321	0.000	0.000	0.000	0.000
12	A	14	GLU	-1	-0.902	-0.916	12.692	-0.495	-0.495	0.000	0.000	0.000	0.000
13	A	15	GLU	-1	-0.891	-0.936	15.729	-0.192	-0.192	0.000	0.000	0.000	0.000
14	A	16	GLY	0	-0.030	-0.008	17.794	0.031	0.031	0.000	0.000	0.000	0.000
15	A	17	PHE	0	-0.062	-0.041	16.770	0.030	0.030	0.000	0.000	0.000	0.000
16	A	18	LEU	0	-0.051	-0.023	11.814	0.033	0.033	0.000	0.000	0.000	0.000
17	A	19	ARG	1	0.867	0.961	15.848	0.132	0.132	0.000	0.000	0.000	0.000
18	A	20	MET	0	-0.026	-0.017	15.867	-0.004	-0.004	0.000	0.000	0.000	0.000
19	A	21	GLU	-1	-0.840	-0.923	9.778	-0.252	-0.252	0.000	0.000	0.000	0.000
20	A	22	VAL	0	-0.036	-0.026	13.573	-0.002	-0.002	0.000	0.000	0.000	0.000
21	A	23	PRO	0	-0.003	-0.002	14.333	0.028	0.028	0.000	0.000	0.000	0.000
22	A	24	ASP	-1	-0.771	-0.895	14.659	0.192	0.192	0.000	0.000	0.000	0.000
23	A	25	GLU	-1	-0.931	-0.965	15.613	0.164	0.164	0.000	0.000	0.000	0.000
24	A	26	ASN	0	-0.120	-0.055	17.252	0.001	0.001	0.000	0.000	0.000	0.000
25	A	27	ALA	0	-0.013	-0.011	13.321	0.020	0.020	0.000	0.000	0.000	0.000
26	A	28	ARG	1	0.840	0.946	8.451	-0.864	-0.864	0.000	0.000	0.000	0.000
27	A	29	PHE	0	-0.003	-0.021	6.514	-0.059	-0.059	0.000	0.000	0.000	0.000
28	A	30	HIS	0	-0.010	-0.025	10.017	-0.012	-0.012	0.000	0.000	0.000	0.000
29	A	31	TYR	0	-0.075	-0.042	6.594	-0.128	-0.128	0.000	0.000	0.000	0.000
30	A	32	VAL	0	0.043	0.030	13.293	0.024	0.024	0.000	0.000	0.000	0.000
31	A	33	VAL	0	0.000	-0.012	15.209	-0.035	-0.035	0.000	0.000	0.000	0.000
32	A	34	ASN	0	-0.011	-0.011	17.736	0.011	0.011	0.000	0.000	0.000	0.000
33	A	35	TYR	0	-0.003	0.047	21.197	-0.014	-0.014	0.000	0.000	0.000	0.000
34	A	36	PRO	0	-0.035	-0.026	22.968	0.012	0.012	0.000	0.000	0.000	0.000
35	A	37	GLU	-1	-0.863	-0.970	25.658	-0.057	-0.057	0.000	0.000	0.000	0.000
36	A	38	ASP	-1	-0.909	-0.950	25.130	-0.065	-0.065	0.000	0.000	0.000	0.000
37	A	39	HIS	0	-0.068	-0.051	24.444	0.016	0.016	0.000	0.000	0.000	0.000
38	A	40	VAL	0	0.021	0.009	21.096	-0.011	-0.011	0.000	0.000	0.000	0.000
39	A	41	ILE	0	-0.085	-0.036	18.879	0.010	0.010	0.000	0.000	0.000	0.000
40	A	42	ASP	-1	-0.861	-0.933	17.351	0.025	0.025	0.000	0.000	0.000	0.000
41	A	43	ILE	0	-0.059	-0.032	11.943	0.010	0.010	0.000	0.000	0.000	0.000
42	A	44	ILE	0	0.059	0.026	12.955	0.008	0.008	0.000	0.000	0.000	0.000
43	A	45	GLN	0	-0.024	0.006	8.076	0.263	0.263	0.000	0.000	0.000	0.000
44	A	46	PRO	0	0.037	-0.003	11.702	0.020	0.020	0.000	0.000	0.000	0.000
45	A	47	ALA	0	0.028	0.025	13.029	0.092	0.092	0.000	0.000	0.000	0.000
46	A	48	GLY	0	-0.059	-0.033	13.580	0.094	0.094	0.000	0.000	0.000	0.000
47	A	49	LYS	1	0.926	0.963	13.824	-0.366	-0.366	0.000	0.000	0.000	0.000
48	A	50	ASP	-1	-0.890	-0.941	8.512	1.407	1.407	0.000	0.000	0.000	0.000
49	A	51	ASP	-1	-0.865	-0.934	8.650	1.044	1.044	0.000	0.000	0.000	0.000
50	A	52	MET	0	-0.040	-0.010	11.012	-0.194	-0.194	0.000	0.000	0.000	0.000
51	A	53	ILE	0	-0.015	-0.007	9.786	0.126	0.126	0.000	0.000	0.000	0.000
52	A	54	LEU	0	-0.016	-0.015	12.553	-0.054	-0.054	0.000	0.000	0.000	0.000
53	A	55	ILE	0	-0.021	-0.019	15.718	-0.019	-0.019	0.000	0.000	0.000	0.000
54	A	56	ALA	0	0.033	0.022	17.599	-0.002	-0.002	0.000	0.000	0.000	0.000
55	A	57	CYS	0	0.044	0.027	20.410	-0.020	-0.020	0.000	0.000	0.000	0.000
56	A	58	ALA	0	0.026	0.032	23.220	0.003	0.003	0.000	0.000	0.000	0.000
57	A	59	THR	0	-0.020	-0.015	25.810	-0.011	-0.011	0.000	0.000	0.000	0.000
58	A	60	SER	0	0.043	0.009	29.205	0.006	0.006	0.000	0.000	0.000	0.000
59	A	61	VAL	0	-0.078	-0.048	32.087	-0.005	-0.005	0.000	0.000	0.000	0.000
60	A	62	SER	0	0.038	0.022	35.586	0.001	0.001	0.000	0.000	0.000	0.000
61	A	63	PRO	0	0.014	-0.005	37.413	0.001	0.001	0.000	0.000	0.000	0.000
62	A	64	GLU	-1	-0.902	-0.963	40.623	0.000	0.000	0.000	0.000	0.000	0.000
63	A	65	HIS	0	0.042	0.015	38.815	0.001	0.001	0.000	0.000	0.000	0.000
64	A	66	GLN	0	-0.123	-0.063	37.843	0.002	0.002	0.000	0.000	0.000	0.000
65	A	67	ALA	0	0.034	0.021	41.931	0.001	0.001	0.000	0.000	0.000	0.000
66	A	68	GLY	0	0.037	0.007	45.055	0.001	0.001	0.000	0.000	0.000	0.000
67	A	69	ILE	0	-0.027	-0.019	40.601	0.001	0.001	0.000	0.000	0.000	0.000
68	A	70	ARG	1	0.962	0.985	42.151	-0.018	-0.018	0.000	0.000	0.000	0.000
69	A	71	ALA	0	-0.034	-0.002	46.871	0.000	0.000	0.000	0.000	0.000	0.000
70	A	72	LEU	0	-0.058	-0.013	46.269	0.000	0.000	0.000	0.000	0.000	0.000
71	A	73	SER	0	0.004	-0.016	49.968	0.001	0.001	0.000	0.000	0.000	0.000
72	A	74	MET	0	0.065	0.027	46.364	0.000	0.000	0.000	0.000	0.000	0.000
73	A	75	GLU	-1	-0.861	-0.909	48.527	0.018	0.018	0.000	0.000	0.000	0.000
74	A	76	LYS	1	0.904	0.912	48.823	-0.011	-0.011	0.000	0.000	0.000	0.000
75	A	77	ARG	1	0.849	0.951	44.898	-0.019	-0.019	0.000	0.000	0.000	0.000
76	A	78	THR	0	0.023	0.001	44.059	0.002	0.002	0.000	0.000	0.000	0.000
77	A	79	GLU	-1	-0.881	-0.917	43.930	0.014	0.014	0.000	0.000	0.000	0.000
78	A	80	PHE	0	-0.003	-0.011	39.358	0.000	0.000	0.000	0.000	0.000	0.000
79	A	81	ILE	0	-0.001	-0.004	38.777	0.000	0.000	0.000	0.000	0.000	0.000
80	A	82	TRP	0	0.026	0.002	39.245	0.003	0.003	0.000	0.000	0.000	0.000
81	A	83	LYS	1	0.914	0.968	40.151	-0.014	-0.014	0.000	0.000	0.000	0.000
82	A	84	VAL	0	0.021	0.026	35.066	0.000	0.000	0.000	0.000	0.000	0.000
83	A	85	ARG	1	0.923	0.980	35.503	-0.038	-0.038	0.000	0.000	0.000	0.000
84	A	86	PHE	0	-0.033	-0.028	35.484	0.003	0.003	0.000	0.000	0.000	0.000
85	A	87	THR	0	-0.032	-0.033	34.978	-0.001	-0.001	0.000	0.000	0.000	0.000
86	A	88	LEU	0	0.064	0.036	29.998	-0.002	-0.002	0.000	0.000	0.000	0.000
87	A	89	ASN	0	-0.051	-0.002	31.073	0.006	0.006	0.000	0.000	0.000	0.000
88	A	90	ARG	1	0.898	0.940	32.847	-0.025	-0.025	0.000	0.000	0.000	0.000
89	A	91	PHE	0	-0.040	-0.022	28.593	-0.005	-0.005	0.000	0.000	0.000	0.000
90	A	92	GLY	0	-0.048	-0.006	27.154	-0.002	-0.002	0.000	0.000	0.000	0.000
91	A	93	VAL	0	-0.018	0.002	24.324	0.003	0.003	0.000	0.000	0.000	0.000
92	A	94	ASP	-1	-0.841	-0.899	24.623	0.105	0.105	0.000	0.000	0.000	0.000
93	A	95	PHE	0	-0.067	-0.067	26.125	-0.006	-0.006	0.000	0.000	0.000	0.000
94	A	96	GLN	0	-0.024	-0.002	27.873	0.001	0.001	0.000	0.000	0.000	0.000
95	A	97	LEU	0	-0.034	-0.017	29.856	-0.006	-0.006	0.000	0.000	0.000	0.000
96	A	98	ASP	-1	-0.784	-0.874	32.951	0.043	0.043	0.000	0.000	0.000	0.000
97	A	99	HIS	0	0.000	-0.040	34.716	-0.003	-0.003	0.000	0.000	0.000	0.000
98	A	100	PRO	0	0.035	0.025	38.069	0.000	0.000	0.000	0.000	0.000	0.000
99	A	101	GLU	-1	-0.929	-0.953	40.669	0.027	0.027	0.000	0.000	0.000	0.000
100	A	102	ASN	0	-0.036	-0.035	41.828	-0.001	-0.001	0.000	0.000	0.000	0.000
101	A	103	VAL	0	-0.013	-0.001	41.116	-0.002	-0.002	0.000	0.000	0.000	0.000
102	A	104	LEU	0	-0.039	-0.013	34.995	0.002	0.002	0.000	0.000	0.000	0.000
103	A	105	ASN	0	-0.013	-0.008	34.944	-0.007	-0.007	0.000	0.000	0.000	0.000
104	A	106	SER	0	-0.005	0.005	31.022	-0.002	-0.002	0.000	0.000	0.000	0.000
105	A	107	TYR	0	-0.033	-0.037	30.399	0.001	0.001	0.000	0.000	0.000	0.000
106	A	108	LEU	0	-0.016	0.013	23.272	-0.005	-0.005	0.000	0.000	0.000	0.000
107	A	109	VAL	0	-0.003	-0.012	24.984	0.004	0.004	0.000	0.000	0.000	0.000
108	A	110	THR	0	0.017	-0.019	20.483	0.002	0.002	0.000	0.000	0.000	0.000
109	A	111	ASP	-1	-0.822	-0.879	20.480	0.065	0.065	0.000	0.000	0.000	0.000
110	A	112	GLU	-1	-0.881	-0.934	17.193	0.218	0.218	0.000	0.000	0.000	0.000
111	A	113	ILE	0	-0.065	-0.010	14.013	-0.036	-0.036	0.000	0.000	0.000	0.000
112	A	114	PHE	0	0.014	0.002	13.955	0.059	0.059	0.000	0.000	0.000	0.000
113	A	115	PHE	0	0.029	-0.023	7.112	-0.088	-0.088	0.000	0.000	0.000	0.000
114	A	116	ASP	-1	-0.943	-0.945	10.796	0.232	0.232	0.000	0.000	0.000	0.000
115	A	117	GLY	0	-0.021	-0.019	13.083	-0.054	-0.054	0.000	0.000	0.000	0.000
116	A	118	LEU	0	-0.050	-0.002	7.912	-0.047	-0.047	0.000	0.000	0.000	0.000
117	A	119	SER	0	0.012	-0.004	10.919	-0.050	-0.050	0.000	0.000	0.000	0.000
118	A	120	LYS	1	0.836	0.906	11.866	0.353	0.353	0.000	0.000	0.000	0.000
119	A	121	ASP	-1	-0.923	-0.963	13.140	-0.072	-0.072	0.000	0.000	0.000	0.000
120	A	122	ARG	1	0.940	0.983	14.624	-0.028	-0.028	0.000	0.000	0.000	0.000
121	A	123	LEU	0	0.002	-0.008	11.856	0.024	0.024	0.000	0.000	0.000	0.000
122	A	124	ILE	0	0.015	-0.009	15.246	0.027	0.027	0.000	0.000	0.000	0.000
123	A	125	SER	0	-0.041	-0.023	17.911	0.016	0.016	0.000	0.000	0.000	0.000
124	A	126	SER	0	0.009	-0.034	18.213	0.007	0.007	0.000	0.000	0.000	0.000
125	A	127	ILE	0	0.011	0.023	15.541	0.009	0.009	0.000	0.000	0.000	0.000
126	A	128	LYS	1	0.899	0.947	19.937	0.094	0.094	0.000	0.000	0.000	0.000
127	A	129	ASN	0	-0.061	-0.038	22.973	-0.003	-0.003	0.000	0.000	0.000	0.000
128	A	130	VAL	0	0.077	0.042	21.266	0.002	0.002	0.000	0.000	0.000	0.000
129	A	131	PHE	0	-0.010	-0.001	24.048	0.001	0.001	0.000	0.000	0.000	0.000
130	A	132	ARG	1	0.960	0.967	25.456	0.029	0.029	0.000	0.000	0.000	0.000
131	A	133	ALA	0	0.006	0.016	27.273	0.001	0.001	0.000	0.000	0.000	0.000
132	A	134	LYS	1	0.874	0.935	27.129	0.006	0.006	0.000	0.000	0.000	0.000
133	A	135	LEU	0	-0.032	-0.002	29.466	-0.001	-0.001	0.000	0.000	0.000	0.000
134	A	136	GLN	0	0.022	0.001	31.331	0.002	0.002	0.000	0.000	0.000	0.000
135	A	137	VAL	0	-0.001	0.005	32.732	0.000	0.000	0.000	0.000	0.000	0.000
136	A	138	MET	0	0.035	0.026	32.189	0.000	0.000	0.000	0.000	0.000	0.000
137	A	139	TRP	0	0.005	-0.014	34.647	-0.001	-0.001	0.000	0.000	0.000	0.000
138	A	140	MET	0	-0.020	0.012	36.573	0.000	0.000	0.000	0.000	0.000	0.000
139	A	141	ILE	0	0.000	0.009	36.194	0.001	0.001	0.000	0.000	0.000	0.000
140	A	142	GLN	0	0.000	-0.008	36.404	0.000	0.000	0.000	0.000	0.000	0.000
141	A	143	GLU	-1	-0.875	-0.913	40.573	0.001	0.001	0.000	0.000	0.000	0.000
142	A	144	ARG	1	0.714	0.846	42.182	-0.006	-0.006	0.000	0.000	0.000	0.000
143	A	145	PHE	0	-0.039	-0.040	42.473	0.000	0.000	0.000	0.000	0.000	0.000
144	A	146	GLY	0	0.016	0.042	41.551	-0.001	-0.001	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:3:LEU)