FMO DATABASE

FMODB ID: V54V1

Calculation Name: 4S0U-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 4S0U

Chain ID: A

ChEMBL ID:

UniProt ID: P26718

Base Structure: X-ray

Registration Date: 2023-09-20

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	120
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 22 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-1118683.952511
FMO2-HF: Nuclear repulsion	1065951.513209
FMO2-HF: Total energy	-52732.439302
FMO2-MP2: Total energy	-52878.128647

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:92:THR)

Summations of interaction energy for fragment #1(A:92:THR)

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.
1.5	3.565	-0.021	-0.962	-1.082	0.002

Interaction energy analysis for fragmet #1(A:92:THR)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : 0.000 / q_NPA : -0.012

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	94	SER	0	-0.049	-0.020	3.812	1.103	3.168	-0.021	-0.962	-1.082	0.002
4	A	95	TYR	0	0.025	0.009	5.441	0.088	0.088	0.000	0.000	0.000	0.000
5	A	96	CYS	0	-0.054	0.008	9.248	0.324	0.324	0.000	0.000	0.000	0.000
6	A	97	GLY	0	0.010	0.015	11.753	-0.005	-0.005	0.000	0.000	0.000	0.000
7	A	98	PRO	0	-0.040	-0.027	15.089	0.020	0.020	0.000	0.000	0.000	0.000
8	A	99	CYS	0	0.041	0.001	17.525	-0.027	-0.027	0.000	0.000	0.000	0.000
9	A	100	PRO	0	0.022	0.027	19.686	-0.014	-0.014	0.000	0.000	0.000	0.000
10	A	101	LYS	1	0.963	0.965	21.911	0.290	0.290	0.000	0.000	0.000	0.000
11	A	102	ASN	0	-0.040	-0.023	21.213	-0.005	-0.005	0.000	0.000	0.000	0.000
12	A	103	TRP	0	0.043	0.028	20.858	0.029	0.029	0.000	0.000	0.000	0.000
13	A	104	ILE	0	-0.003	0.001	17.165	-0.062	-0.062	0.000	0.000	0.000	0.000
14	A	106	TYR	0	-0.087	-0.084	12.500	-0.088	-0.088	0.000	0.000	0.000	0.000
15	A	107	LYS	1	0.901	0.947	12.252	0.042	0.042	0.000	0.000	0.000	0.000
16	A	108	ASN	0	0.046	-0.010	11.976	-0.024	-0.024	0.000	0.000	0.000	0.000
17	A	109	ASN	0	-0.051	-0.004	14.675	0.018	0.018	0.000	0.000	0.000	0.000
18	A	111	TYR	0	-0.002	-0.012	18.311	0.060	0.060	0.000	0.000	0.000	0.000
19	A	112	GLN	0	0.024	0.030	21.807	-0.032	-0.032	0.000	0.000	0.000	0.000
20	A	113	PHE	0	-0.034	-0.027	22.083	0.025	0.025	0.000	0.000	0.000	0.000
21	A	114	PHE	0	-0.001	0.006	26.824	-0.013	-0.013	0.000	0.000	0.000	0.000
22	A	115	ASP	-1	-0.870	-0.954	30.198	-0.163	-0.163	0.000	0.000	0.000	0.000
23	A	116	GLU	-1	-0.905	-0.980	32.559	-0.153	-0.153	0.000	0.000	0.000	0.000
24	A	117	SER	0	-0.023	-0.013	35.706	0.004	0.004	0.000	0.000	0.000	0.000
25	A	118	LYS	1	0.927	0.983	36.265	0.122	0.122	0.000	0.000	0.000	0.000
26	A	119	ASN	0	0.003	0.046	38.468	0.000	0.000	0.000	0.000	0.000	0.000
27	A	120	TRP	0	0.028	0.009	35.458	-0.005	-0.005	0.000	0.000	0.000	0.000
28	A	121	TYR	0	0.041	0.008	37.727	-0.003	-0.003	0.000	0.000	0.000	0.000
29	A	122	GLU	-1	-0.916	-0.966	39.063	-0.090	-0.090	0.000	0.000	0.000	0.000
30	A	123	SER	0	-0.023	-0.027	34.397	-0.009	-0.009	0.000	0.000	0.000	0.000
31	A	124	GLN	0	0.018	0.015	34.080	-0.005	-0.005	0.000	0.000	0.000	0.000
32	A	125	ALA	0	-0.015	-0.020	34.732	-0.006	-0.006	0.000	0.000	0.000	0.000
33	A	126	SER	0	-0.049	-0.053	33.407	-0.007	-0.007	0.000	0.000	0.000	0.000
34	A	127	CYS	0	-0.004	0.039	27.187	0.006	0.006	0.000	0.000	0.000	0.000
35	A	128	MET	0	0.036	0.025	30.807	-0.006	-0.006	0.000	0.000	0.000	0.000
36	A	129	SER	0	-0.110	-0.054	32.678	-0.005	-0.005	0.000	0.000	0.000	0.000
37	A	130	GLN	0	-0.039	-0.019	28.878	-0.020	-0.020	0.000	0.000	0.000	0.000
38	A	131	ASN	0	-0.076	-0.035	28.093	-0.005	-0.005	0.000	0.000	0.000	0.000
39	A	132	ALA	0	-0.027	0.002	26.681	-0.009	-0.009	0.000	0.000	0.000	0.000
40	A	133	SER	0	0.023	0.015	27.799	0.012	0.012	0.000	0.000	0.000	0.000
41	A	134	LEU	0	-0.002	-0.004	28.530	-0.017	-0.017	0.000	0.000	0.000	0.000
42	A	135	LEU	0	-0.045	-0.021	24.636	0.004	0.004	0.000	0.000	0.000	0.000
43	A	136	LYS	1	0.923	0.982	26.513	0.063	0.063	0.000	0.000	0.000	0.000
44	A	137	VAL	0	-0.017	-0.016	25.505	-0.007	-0.007	0.000	0.000	0.000	0.000
45	A	138	TYR	0	-0.057	-0.034	18.939	-0.003	-0.003	0.000	0.000	0.000	0.000
46	A	139	SER	0	0.039	0.013	20.980	0.014	0.014	0.000	0.000	0.000	0.000
47	A	140	LYS	1	0.922	0.970	21.848	-0.023	-0.023	0.000	0.000	0.000	0.000
48	A	141	GLU	-1	-0.900	-0.948	17.824	0.065	0.065	0.000	0.000	0.000	0.000
49	A	142	ASP	-1	-0.887	-0.953	16.644	0.023	0.023	0.000	0.000	0.000	0.000
50	A	143	GLN	0	0.027	-0.005	17.386	-0.028	-0.028	0.000	0.000	0.000	0.000
51	A	144	ASP	-1	-0.784	-0.853	16.614	-0.053	-0.053	0.000	0.000	0.000	0.000
52	A	145	LEU	0	-0.012	-0.024	15.127	0.003	0.003	0.000	0.000	0.000	0.000
53	A	146	LEU	0	0.032	0.027	19.131	-0.019	-0.019	0.000	0.000	0.000	0.000
54	A	147	LYS	1	0.922	0.997	20.428	0.054	0.054	0.000	0.000	0.000	0.000
55	A	148	LEU	0	-0.038	0.012	19.345	0.012	0.012	0.000	0.000	0.000	0.000
56	A	149	VAL	0	0.003	0.036	23.073	-0.014	-0.014	0.000	0.000	0.000	0.000
57	A	150	LYS	1	0.988	0.988	25.170	0.146	0.146	0.000	0.000	0.000	0.000
58	A	151	SER	0	-0.024	-0.017	28.545	-0.004	-0.004	0.000	0.000	0.000	0.000
59	A	152	TYR	0	-0.017	-0.008	31.290	0.003	0.003	0.000	0.000	0.000	0.000
60	A	153	HIS	0	0.040	0.035	29.044	-0.006	-0.006	0.000	0.000	0.000	0.000
61	A	154	TRP	0	-0.061	-0.025	32.164	0.008	0.008	0.000	0.000	0.000	0.000
62	A	155	MET	0	-0.045	-0.003	30.263	-0.010	-0.010	0.000	0.000	0.000	0.000
63	A	156	GLY	0	0.056	0.007	30.998	0.003	0.003	0.000	0.000	0.000	0.000
64	A	157	LEU	0	-0.087	-0.033	32.743	0.006	0.006	0.000	0.000	0.000	0.000
65	A	158	VAL	0	0.031	0.001	34.729	-0.002	-0.002	0.000	0.000	0.000	0.000
66	A	159	HIS	0	-0.085	-0.035	38.516	0.005	0.005	0.000	0.000	0.000	0.000
67	A	160	ILE	0	0.015	-0.002	40.978	-0.001	-0.001	0.000	0.000	0.000	0.000
68	A	161	PRO	0	0.089	0.044	43.568	0.004	0.004	0.000	0.000	0.000	0.000
69	A	162	THR	0	-0.063	-0.030	47.036	0.002	0.002	0.000	0.000	0.000	0.000
70	A	163	ASN	0	0.006	-0.004	44.383	0.001	0.001	0.000	0.000	0.000	0.000
71	A	164	GLY	0	0.046	0.033	44.990	0.003	0.003	0.000	0.000	0.000	0.000
72	A	165	SER	0	-0.078	-0.045	40.457	0.001	0.001	0.000	0.000	0.000	0.000
73	A	166	TRP	0	0.046	0.016	36.889	-0.005	-0.005	0.000	0.000	0.000	0.000
74	A	167	GLN	0	0.019	-0.002	35.681	0.000	0.000	0.000	0.000	0.000	0.000
75	A	168	TRP	0	0.004	-0.004	30.181	-0.009	-0.009	0.000	0.000	0.000	0.000
76	A	169	GLU	-1	-0.735	-0.889	32.460	-0.093	-0.093	0.000	0.000	0.000	0.000
77	A	170	ASP	-1	-0.838	-0.857	30.095	-0.055	-0.055	0.000	0.000	0.000	0.000
78	A	171	GLY	0	0.014	0.015	33.383	0.004	0.004	0.000	0.000	0.000	0.000
79	A	172	SER	0	-0.151	-0.115	31.466	0.008	0.008	0.000	0.000	0.000	0.000
80	A	173	ILE	0	0.029	-0.002	33.634	-0.003	-0.003	0.000	0.000	0.000	0.000
81	A	174	LEU	0	-0.049	-0.017	31.525	-0.001	-0.001	0.000	0.000	0.000	0.000
82	A	175	SER	0	-0.028	-0.013	29.663	0.006	0.006	0.000	0.000	0.000	0.000
83	A	176	PRO	0	0.042	0.002	31.766	-0.003	-0.003	0.000	0.000	0.000	0.000
84	A	177	ASN	0	-0.009	-0.007	28.309	-0.002	-0.002	0.000	0.000	0.000	0.000
85	A	178	LEU	0	-0.009	0.014	26.079	0.003	0.003	0.000	0.000	0.000	0.000
86	A	179	LEU	0	0.006	-0.004	28.617	-0.006	-0.006	0.000	0.000	0.000	0.000
87	A	180	THR	0	-0.040	-0.010	31.253	0.008	0.008	0.000	0.000	0.000	0.000
88	A	181	ILE	0	0.010	0.009	34.146	-0.007	-0.007	0.000	0.000	0.000	0.000
89	A	182	ILE	0	-0.064	-0.033	36.815	0.004	0.004	0.000	0.000	0.000	0.000
90	A	183	GLU	-1	-0.829	-0.918	39.251	-0.035	-0.035	0.000	0.000	0.000	0.000
91	A	184	MET	0	-0.014	-0.020	41.894	0.001	0.001	0.000	0.000	0.000	0.000
92	A	185	GLN	0	-0.036	-0.025	44.730	0.001	0.001	0.000	0.000	0.000	0.000
93	A	186	LYS	1	0.908	0.962	44.540	0.039	0.039	0.000	0.000	0.000	0.000
94	A	187	GLY	0	0.003	-0.004	44.632	-0.002	-0.002	0.000	0.000	0.000	0.000
95	A	188	ASP	-1	-0.855	-0.910	42.558	-0.035	-0.035	0.000	0.000	0.000	0.000
96	A	189	CYS	0	0.032	0.038	38.536	-0.003	-0.003	0.000	0.000	0.000	0.000
97	A	190	ALA	0	0.020	0.010	34.747	0.001	0.001	0.000	0.000	0.000	0.000
98	A	191	LEU	0	0.015	0.008	34.237	-0.007	-0.007	0.000	0.000	0.000	0.000
99	A	192	TYR	0	-0.034	-0.074	25.708	0.012	0.012	0.000	0.000	0.000	0.000
100	A	193	ALA	0	0.014	-0.007	30.600	-0.006	-0.006	0.000	0.000	0.000	0.000
101	A	194	SER	0	-0.064	-0.056	26.270	0.012	0.012	0.000	0.000	0.000	0.000
102	A	195	SER	0	-0.050	-0.032	26.575	0.011	0.011	0.000	0.000	0.000	0.000
103	A	196	PHE	0	-0.029	-0.005	22.536	0.010	0.010	0.000	0.000	0.000	0.000
104	A	197	LYS	1	0.948	0.983	28.427	0.050	0.050	0.000	0.000	0.000	0.000
105	A	198	GLY	0	0.051	0.014	31.769	-0.009	-0.009	0.000	0.000	0.000	0.000
106	A	199	TYR	0	-0.038	-0.026	34.242	0.007	0.007	0.000	0.000	0.000	0.000
107	A	200	ILE	0	-0.005	0.011	37.184	-0.005	-0.005	0.000	0.000	0.000	0.000
108	A	201	GLU	-1	-0.875	-0.929	39.764	-0.053	-0.053	0.000	0.000	0.000	0.000
109	A	202	ASN	0	0.007	-0.013	41.510	-0.001	-0.001	0.000	0.000	0.000	0.000
110	A	204	SER	0	-0.032	-0.032	41.867	-0.004	-0.004	0.000	0.000	0.000	0.000
111	A	205	THR	0	-0.008	-0.009	41.615	-0.001	-0.001	0.000	0.000	0.000	0.000
112	A	206	PRO	0	-0.002	-0.013	40.486	-0.003	-0.003	0.000	0.000	0.000	0.000
113	A	207	ASN	0	-0.025	-0.019	35.952	0.001	0.001	0.000	0.000	0.000	0.000
114	A	208	THR	0	0.028	0.024	31.658	0.001	0.001	0.000	0.000	0.000	0.000
115	A	209	TYR	0	0.000	0.033	31.356	0.010	0.010	0.000	0.000	0.000	0.000
116	A	210	ILE	0	0.006	0.012	25.417	-0.012	-0.012	0.000	0.000	0.000	0.000
117	A	212	MET	0	-0.037	-0.029	21.694	-0.013	-0.013	0.000	0.000	0.000	0.000
118	A	213	GLN	0	-0.030	-0.030	22.616	-0.003	-0.003	0.000	0.000	0.000	0.000
119	A	214	ARG	1	0.933	0.978	19.767	0.067	0.067	0.000	0.000	0.000	0.000
120	A	215	THR	0	0.055	0.033	17.298	0.000	0.000	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:92:THR)