FMO DATABASE

FMODB ID: 7GKLK

Calculation Name: 4B0M-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 4B0M

Chain ID: A

ChEMBL ID:

UniProt ID: P26949

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	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	134
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-1110594.503341
FMO2-HF: Nuclear repulsion	1056737.895825
FMO2-HF: Total energy	-53856.607516
FMO2-MP2: Total energy	-54012.957231

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:ALA)

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

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.
-1.933	0.166	-0.014	-1.159	-0.926	0.005

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

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : 0.011 / q_NPA : 0.005

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	THR	0	-0.051	-0.033	3.870	-0.696	1.403	-0.014	-1.159	-0.926	0.005
4	A	4	PHE	0	-0.014	-0.004	6.493	-0.113	-0.113	0.000	0.000	0.000	0.000
5	A	5	ASP	-1	-0.837	-0.895	10.273	-0.564	-0.564	0.000	0.000	0.000	0.000
6	A	6	SER	0	0.023	-0.019	13.555	-0.018	-0.018	0.000	0.000	0.000	0.000
7	A	7	THR	0	-0.070	-0.047	16.889	0.060	0.060	0.000	0.000	0.000	0.000
8	A	8	MET	0	-0.092	-0.048	17.614	0.007	0.007	0.000	0.000	0.000	0.000
9	A	9	LEU	0	-0.004	0.006	16.241	0.002	0.002	0.000	0.000	0.000	0.000
10	A	10	ASP	-1	-0.899	-0.945	20.320	-0.218	-0.218	0.000	0.000	0.000	0.000
11	A	11	THR	0	-0.067	-0.030	22.081	0.016	0.016	0.000	0.000	0.000	0.000
12	A	12	ASN	0	-0.046	-0.054	24.542	0.007	0.007	0.000	0.000	0.000	0.000
13	A	13	SER	0	-0.070	-0.040	28.216	0.008	0.008	0.000	0.000	0.000	0.000
14	A	14	GLY	0	0.022	0.010	27.508	0.009	0.009	0.000	0.000	0.000	0.000
15	A	15	GLU	-1	-0.875	-0.919	24.757	-0.152	-0.152	0.000	0.000	0.000	0.000
16	A	16	SER	0	-0.049	-0.017	22.379	0.002	0.002	0.000	0.000	0.000	0.000
17	A	17	ILE	0	0.025	0.023	18.325	0.010	0.010	0.000	0.000	0.000	0.000
18	A	18	ASP	-1	-0.772	-0.840	15.936	-0.229	-0.229	0.000	0.000	0.000	0.000
19	A	19	VAL	0	-0.015	-0.020	12.597	0.000	0.000	0.000	0.000	0.000	0.000
20	A	20	SER	0	-0.086	-0.076	12.112	-0.027	-0.027	0.000	0.000	0.000	0.000
21	A	21	LEU	0	0.012	0.002	11.190	0.009	0.009	0.000	0.000	0.000	0.000
22	A	22	PHE	0	0.031	0.020	11.222	0.059	0.059	0.000	0.000	0.000	0.000
23	A	23	ASN	0	0.002	0.000	7.412	-0.222	-0.222	0.000	0.000	0.000	0.000
24	A	24	GLN	0	-0.049	-0.019	6.619	0.058	0.058	0.000	0.000	0.000	0.000
25	A	25	GLY	0	-0.028	-0.007	8.634	0.185	0.185	0.000	0.000	0.000	0.000
26	A	26	LEU	0	-0.082	-0.029	9.212	0.040	0.040	0.000	0.000	0.000	0.000
27	A	27	GLN	0	0.013	-0.009	13.035	-0.084	-0.084	0.000	0.000	0.000	0.000
28	A	28	LEU	0	0.046	0.027	15.909	0.021	0.021	0.000	0.000	0.000	0.000
29	A	29	PRO	0	0.002	0.007	18.859	0.013	0.013	0.000	0.000	0.000	0.000
30	A	30	GLY	0	0.027	0.021	21.920	-0.016	-0.016	0.000	0.000	0.000	0.000
31	A	31	ASN	0	-0.043	-0.035	25.223	0.015	0.015	0.000	0.000	0.000	0.000
32	A	32	TYR	0	-0.019	-0.024	20.371	-0.014	-0.014	0.000	0.000	0.000	0.000
33	A	33	PHE	0	-0.023	-0.005	25.918	0.008	0.008	0.000	0.000	0.000	0.000
34	A	34	VAL	0	0.014	0.006	24.983	-0.001	-0.001	0.000	0.000	0.000	0.000
35	A	35	ASN	0	-0.026	-0.014	27.290	-0.002	-0.002	0.000	0.000	0.000	0.000
36	A	36	VAL	0	0.029	0.017	27.982	0.008	0.008	0.000	0.000	0.000	0.000
37	A	37	PHE	0	-0.018	-0.029	28.698	-0.005	-0.005	0.000	0.000	0.000	0.000
38	A	38	VAL	0	0.056	0.030	30.506	0.006	0.006	0.000	0.000	0.000	0.000
39	A	39	ASN	0	-0.001	-0.010	31.882	-0.001	-0.001	0.000	0.000	0.000	0.000
40	A	40	GLY	0	-0.004	0.006	30.612	0.000	0.000	0.000	0.000	0.000	0.000
41	A	41	ARG	1	0.890	0.946	31.620	-0.055	-0.055	0.000	0.000	0.000	0.000
42	A	42	LYS	1	0.837	0.910	31.633	-0.022	-0.022	0.000	0.000	0.000	0.000
43	A	43	VAL	0	-0.058	-0.031	33.486	-0.002	-0.002	0.000	0.000	0.000	0.000
44	A	44	ASP	-1	-0.734	-0.853	33.171	0.017	0.017	0.000	0.000	0.000	0.000
45	A	45	SER	0	-0.045	-0.025	31.926	0.004	0.004	0.000	0.000	0.000	0.000
46	A	46	GLY	0	0.006	0.017	31.393	-0.003	-0.003	0.000	0.000	0.000	0.000
47	A	47	ASN	0	-0.006	0.015	30.297	-0.001	-0.001	0.000	0.000	0.000	0.000
48	A	48	ILE	0	-0.008	0.002	28.456	0.004	0.004	0.000	0.000	0.000	0.000
49	A	49	ASP	-1	-0.856	-0.930	27.804	0.001	0.001	0.000	0.000	0.000	0.000
50	A	50	PHE	0	-0.008	-0.005	23.373	0.014	0.014	0.000	0.000	0.000	0.000
51	A	51	ARG	1	0.949	0.967	23.989	-0.064	-0.064	0.000	0.000	0.000	0.000
52	A	52	LEU	0	0.007	-0.005	17.723	0.013	0.013	0.000	0.000	0.000	0.000
53	A	53	GLU	-1	-0.771	-0.852	21.030	0.081	0.081	0.000	0.000	0.000	0.000
54	A	54	LYS	1	0.850	0.921	17.194	-0.196	-0.196	0.000	0.000	0.000	0.000
55	A	55	HIS	1	0.809	0.884	20.360	-0.154	-0.154	0.000	0.000	0.000	0.000
56	A	56	ASN	0	0.010	0.001	20.638	0.017	0.017	0.000	0.000	0.000	0.000
57	A	57	GLY	0	0.044	0.033	18.368	0.032	0.032	0.000	0.000	0.000	0.000
58	A	58	LYS	1	0.932	0.967	15.518	-0.302	-0.302	0.000	0.000	0.000	0.000
59	A	59	GLU	-1	-0.807	-0.889	15.558	0.126	0.126	0.000	0.000	0.000	0.000
60	A	60	LEU	0	-0.069	-0.043	16.396	0.037	0.037	0.000	0.000	0.000	0.000
61	A	61	LEU	0	0.024	0.026	18.661	-0.016	-0.016	0.000	0.000	0.000	0.000
62	A	62	TRP	0	0.023	-0.005	20.883	0.019	0.019	0.000	0.000	0.000	0.000
63	A	63	PRO	0	-0.029	-0.004	24.462	-0.011	-0.011	0.000	0.000	0.000	0.000
64	A	64	CYS	0	-0.079	-0.024	27.353	0.003	0.003	0.000	0.000	0.000	0.000
65	A	65	LEU	0	-0.029	-0.015	30.441	-0.004	-0.004	0.000	0.000	0.000	0.000
66	A	66	SER	0	0.083	0.026	33.162	0.001	0.001	0.000	0.000	0.000	0.000
67	A	67	SER	0	0.060	0.018	36.968	0.002	0.002	0.000	0.000	0.000	0.000
68	A	68	LEU	0	0.035	0.030	39.515	0.001	0.001	0.000	0.000	0.000	0.000
69	A	69	GLN	0	0.021	0.030	33.386	-0.001	-0.001	0.000	0.000	0.000	0.000
70	A	70	LEU	0	0.038	0.016	34.216	0.001	0.001	0.000	0.000	0.000	0.000
71	A	71	THR	0	0.021	0.003	37.502	0.001	0.001	0.000	0.000	0.000	0.000
72	A	72	LYS	1	0.814	0.906	36.822	-0.021	-0.021	0.000	0.000	0.000	0.000
73	A	73	TYR	0	-0.071	-0.063	33.271	0.000	0.000	0.000	0.000	0.000	0.000
74	A	74	GLY	0	-0.001	0.012	37.638	0.004	0.004	0.000	0.000	0.000	0.000
75	A	75	ILE	0	-0.019	-0.009	34.637	0.003	0.003	0.000	0.000	0.000	0.000
76	A	76	ASP	-1	-0.843	-0.914	39.277	0.042	0.042	0.000	0.000	0.000	0.000
77	A	77	ILE	0	0.002	-0.022	39.515	0.003	0.003	0.000	0.000	0.000	0.000
78	A	78	ASP	-1	-0.881	-0.923	41.735	0.037	0.037	0.000	0.000	0.000	0.000
79	A	79	LYS	1	0.741	0.858	42.607	-0.052	-0.052	0.000	0.000	0.000	0.000
80	A	80	TYR	0	-0.022	-0.014	39.214	0.003	0.003	0.000	0.000	0.000	0.000
81	A	81	PRO	0	0.069	0.031	40.717	0.000	0.000	0.000	0.000	0.000	0.000
82	A	82	ASP	-1	-0.849	-0.923	38.637	0.059	0.059	0.000	0.000	0.000	0.000
83	A	83	LEU	0	-0.024	-0.004	35.917	0.002	0.002	0.000	0.000	0.000	0.000
84	A	84	ILE	0	-0.029	-0.001	37.597	-0.001	-0.001	0.000	0.000	0.000	0.000
85	A	85	LYS	1	0.788	0.861	36.082	-0.064	-0.064	0.000	0.000	0.000	0.000
86	A	86	SER	0	-0.039	-0.023	39.609	-0.003	-0.003	0.000	0.000	0.000	0.000
87	A	87	GLY	0	0.050	0.019	41.295	0.001	0.001	0.000	0.000	0.000	0.000
88	A	88	THR	0	-0.084	-0.043	39.211	-0.002	-0.002	0.000	0.000	0.000	0.000
89	A	89	GLU	-1	-0.844	-0.917	33.509	0.023	0.023	0.000	0.000	0.000	0.000
90	A	90	GLN	0	-0.078	-0.053	36.534	0.001	0.001	0.000	0.000	0.000	0.000
91	A	92	VAL	0	0.002	-0.003	34.206	0.002	0.002	0.000	0.000	0.000	0.000
92	A	93	ASP	-1	-0.821	-0.898	32.674	0.081	0.081	0.000	0.000	0.000	0.000
93	A	94	LEU	0	-0.019	-0.032	29.311	0.002	0.002	0.000	0.000	0.000	0.000
94	A	95	LEU	0	-0.039	-0.014	28.066	0.007	0.007	0.000	0.000	0.000	0.000
95	A	96	ALA	0	-0.020	0.006	32.098	0.002	0.002	0.000	0.000	0.000	0.000
96	A	97	ILE	0	-0.032	0.000	33.949	-0.004	-0.004	0.000	0.000	0.000	0.000
97	A	98	PRO	0	0.013	0.025	33.670	0.007	0.007	0.000	0.000	0.000	0.000
98	A	99	HIS	0	-0.058	-0.062	32.703	0.003	0.003	0.000	0.000	0.000	0.000
99	A	100	SER	0	-0.027	-0.013	31.015	0.001	0.001	0.000	0.000	0.000	0.000
100	A	101	ASP	-1	-0.859	-0.922	24.591	0.189	0.189	0.000	0.000	0.000	0.000
101	A	102	VAL	0	-0.022	-0.016	25.603	-0.015	-0.015	0.000	0.000	0.000	0.000
102	A	103	GLN	0	-0.053	-0.037	20.170	0.029	0.029	0.000	0.000	0.000	0.000
103	A	104	PHE	0	0.010	0.009	20.680	-0.012	-0.012	0.000	0.000	0.000	0.000
104	A	105	TYR	0	0.022	0.000	19.352	0.017	0.017	0.000	0.000	0.000	0.000
105	A	106	PHE	0	0.059	0.034	16.810	-0.013	-0.013	0.000	0.000	0.000	0.000
106	A	107	ASN	0	0.008	0.006	14.093	-0.013	-0.013	0.000	0.000	0.000	0.000
107	A	108	GLN	0	-0.005	-0.005	18.290	-0.016	-0.016	0.000	0.000	0.000	0.000
108	A	109	GLN	0	-0.006	-0.012	20.596	-0.004	-0.004	0.000	0.000	0.000	0.000
109	A	110	LYS	1	0.834	0.940	22.824	-0.111	-0.111	0.000	0.000	0.000	0.000
110	A	111	LEU	0	0.035	0.025	23.695	0.015	0.015	0.000	0.000	0.000	0.000
111	A	112	SER	0	-0.027	-0.028	24.877	-0.005	-0.005	0.000	0.000	0.000	0.000
112	A	113	LEU	0	0.015	0.015	26.480	0.008	0.008	0.000	0.000	0.000	0.000
113	A	114	ILE	0	-0.030	-0.023	26.876	-0.004	-0.004	0.000	0.000	0.000	0.000
114	A	115	VAL	0	0.040	0.015	30.480	0.003	0.003	0.000	0.000	0.000	0.000
115	A	116	PRO	0	0.057	0.059	33.891	-0.001	-0.001	0.000	0.000	0.000	0.000
116	A	117	PRO	0	0.022	0.002	36.530	-0.005	-0.005	0.000	0.000	0.000	0.000
117	A	118	GLN	0	0.038	0.003	39.374	-0.004	-0.004	0.000	0.000	0.000	0.000
118	A	119	ALA	0	-0.022	-0.002	38.087	-0.005	-0.005	0.000	0.000	0.000	0.000
119	A	120	LEU	0	-0.049	-0.017	36.650	-0.002	-0.002	0.000	0.000	0.000	0.000
120	A	121	LEU	0	0.009	0.008	40.703	-0.002	-0.002	0.000	0.000	0.000	0.000
121	A	122	PRO	0	-0.021	-0.015	43.226	0.001	0.001	0.000	0.000	0.000	0.000
122	A	123	ARG	1	0.851	0.916	41.957	-0.043	-0.043	0.000	0.000	0.000	0.000
123	A	124	PHE	0	0.044	0.030	45.442	0.001	0.001	0.000	0.000	0.000	0.000
124	A	125	ASP	-1	-0.838	-0.928	47.257	0.036	0.036	0.000	0.000	0.000	0.000
125	A	126	GLY	0	-0.002	-0.013	46.017	-0.001	-0.001	0.000	0.000	0.000	0.000
126	A	127	ILE	0	-0.079	-0.026	40.141	0.000	0.000	0.000	0.000	0.000	0.000
127	A	128	MET	0	-0.010	-0.002	38.124	0.002	0.002	0.000	0.000	0.000	0.000
128	A	129	PRO	0	-0.017	-0.002	42.278	-0.003	-0.003	0.000	0.000	0.000	0.000
129	A	130	MET	0	0.019	0.002	45.442	0.000	0.000	0.000	0.000	0.000	0.000
130	A	131	GLN	0	-0.029	-0.001	46.519	-0.003	-0.003	0.000	0.000	0.000	0.000
131	A	132	LEU	0	-0.030	-0.023	40.257	0.002	0.002	0.000	0.000	0.000	0.000
132	A	133	TRP	0	0.003	0.005	40.736	-0.002	-0.002	0.000	0.000	0.000	0.000
133	A	134	ASP	-1	-0.890	-0.947	40.734	0.071	0.071	0.000	0.000	0.000	0.000
134	A	135	ASP	-1	-0.923	-0.949	36.143	0.097	0.097	0.000	0.000	0.000	0.000

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