FMO DATABASE

FMODB ID: YVMM2

Calculation Name: 1ZHG-A-Xray372

Preferred Name: Fatty acid synthase

Target Type: SINGLE PROTEIN

Ligand Name:

ligand 3-letter code:

PDB ID: 1ZHG

Chain ID: A

ChEMBL ID: CHEMBL4512

UniProt ID: Q965D7

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	136
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-1178871.650689
FMO2-HF: Nuclear repulsion	1126693.381797
FMO2-HF: Total energy	-52178.268892
FMO2-MP2: Total energy	-52330.839461

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:94:LYS)

Summations of interaction energy for fragment #1(A:94:LYS)

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.
27.493	31.631	10.513	-7.589	-7.062	-0.07

Interaction energy analysis for fragmet #1(A:94:LYS)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 1 / q_Mulliken : 0.941 / q_NPA : 0.970

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	96	LEU	0	-0.015	-0.017	1.780	-50.703	-46.793	10.515	-7.535	-6.890	-0.070
4	A	97	PRO	0	0.018	-0.006	4.346	4.719	4.872	-0.001	-0.051	-0.101	0.000
5	A	98	HIS	0	-0.017	0.018	8.133	-0.427	-0.427	0.000	0.000	0.000	0.000
6	A	99	ARG	1	0.968	0.998	10.725	22.179	22.179	0.000	0.000	0.000	0.000
7	A	100	TYR	0	0.005	0.016	14.187	1.205	1.205	0.000	0.000	0.000	0.000
8	A	101	PRO	0	0.040	0.008	13.697	-1.458	-1.458	0.000	0.000	0.000	0.000
9	A	102	PHE	0	0.000	-0.005	12.243	-1.293	-1.293	0.000	0.000	0.000	0.000
10	A	103	LEU	0	0.023	0.013	6.174	0.268	0.268	0.000	0.000	0.000	0.000
11	A	104	LEU	0	-0.043	-0.029	10.306	1.219	1.219	0.000	0.000	0.000	0.000
12	A	105	VAL	0	0.000	-0.018	8.811	1.337	1.337	0.000	0.000	0.000	0.000
13	A	106	ASP	-1	-0.786	-0.873	8.171	-21.086	-21.086	0.000	0.000	0.000	0.000
14	A	107	LYS	1	0.922	0.946	7.464	17.517	17.517	0.000	0.000	0.000	0.000
15	A	108	VAL	0	0.040	0.023	7.666	1.188	1.188	0.000	0.000	0.000	0.000
16	A	109	ILE	0	-0.047	-0.034	9.446	-0.166	-0.166	0.000	0.000	0.000	0.000
17	A	110	TYR	0	0.041	0.019	12.218	0.862	0.862	0.000	0.000	0.000	0.000
18	A	111	MET	0	-0.022	-0.013	10.504	-1.525	-1.525	0.000	0.000	0.000	0.000
19	A	112	GLN	0	-0.014	0.005	13.116	0.356	0.356	0.000	0.000	0.000	0.000
20	A	113	PRO	0	0.065	0.021	12.853	0.197	0.197	0.000	0.000	0.000	0.000
21	A	114	ASN	0	-0.021	-0.018	14.909	1.315	1.315	0.000	0.000	0.000	0.000
22	A	115	LYS	1	0.947	0.985	17.100	14.622	14.622	0.000	0.000	0.000	0.000
23	A	116	THR	0	0.017	-0.004	17.389	0.209	0.209	0.000	0.000	0.000	0.000
24	A	117	ILE	0	-0.004	0.014	10.009	-0.887	-0.887	0.000	0.000	0.000	0.000
25	A	118	ILE	0	0.016	0.007	13.764	0.857	0.857	0.000	0.000	0.000	0.000
26	A	119	GLY	0	0.017	0.003	11.969	-1.306	-1.306	0.000	0.000	0.000	0.000
27	A	120	LEU	0	-0.081	-0.030	11.695	1.350	1.350	0.000	0.000	0.000	0.000
28	A	121	LYS	1	0.825	0.911	11.871	16.799	16.799	0.000	0.000	0.000	0.000
29	A	122	GLN	0	-0.011	0.000	13.401	1.555	1.555	0.000	0.000	0.000	0.000
30	A	123	VAL	0	-0.017	0.003	15.860	-0.461	-0.461	0.000	0.000	0.000	0.000
31	A	124	SER	0	0.047	0.034	16.601	0.772	0.772	0.000	0.000	0.000	0.000
32	A	125	THR	0	0.007	-0.020	18.977	-0.139	-0.139	0.000	0.000	0.000	0.000
33	A	126	ASN	0	-0.001	-0.012	17.653	0.503	0.503	0.000	0.000	0.000	0.000
34	A	127	GLU	-1	-0.802	-0.885	15.140	-16.981	-16.981	0.000	0.000	0.000	0.000
35	A	128	PRO	0	0.049	0.020	15.629	0.703	0.703	0.000	0.000	0.000	0.000
36	A	129	PHE	0	-0.020	-0.013	17.320	0.481	0.481	0.000	0.000	0.000	0.000
37	A	130	PHE	0	-0.018	-0.018	20.954	0.527	0.527	0.000	0.000	0.000	0.000
38	A	131	ASN	0	-0.038	0.002	21.111	1.020	1.020	0.000	0.000	0.000	0.000
39	A	132	GLY	0	0.048	0.019	23.826	-0.389	-0.389	0.000	0.000	0.000	0.000
40	A	133	HIS	0	-0.074	-0.033	26.543	0.375	0.375	0.000	0.000	0.000	0.000
41	A	134	PHE	0	0.025	0.006	28.692	-0.220	-0.220	0.000	0.000	0.000	0.000
42	A	135	PRO	0	-0.004	0.022	29.093	0.363	0.363	0.000	0.000	0.000	0.000
43	A	136	GLN	0	0.019	0.000	32.065	0.030	0.030	0.000	0.000	0.000	0.000
44	A	137	LYS	1	0.926	0.957	29.665	9.269	9.269	0.000	0.000	0.000	0.000
45	A	138	GLN	0	0.022	0.015	25.647	-0.062	-0.062	0.000	0.000	0.000	0.000
46	A	139	ILE	0	-0.010	-0.019	26.348	0.022	0.022	0.000	0.000	0.000	0.000
47	A	140	MET	0	-0.023	0.006	17.950	-0.055	-0.055	0.000	0.000	0.000	0.000
48	A	141	PRO	0	0.042	0.016	22.563	0.285	0.285	0.000	0.000	0.000	0.000
49	A	142	GLY	0	0.080	0.018	22.990	-0.512	-0.512	0.000	0.000	0.000	0.000
50	A	143	VAL	0	0.035	0.000	22.969	-0.417	-0.417	0.000	0.000	0.000	0.000
51	A	144	LEU	0	0.017	0.008	19.165	-0.531	-0.531	0.000	0.000	0.000	0.000
52	A	145	GLN	0	-0.013	-0.006	18.482	-0.720	-0.720	0.000	0.000	0.000	0.000
53	A	146	ILE	0	-0.020	-0.004	19.211	-0.421	-0.421	0.000	0.000	0.000	0.000
54	A	147	GLU	-1	-0.828	-0.909	15.467	-20.482	-20.482	0.000	0.000	0.000	0.000
55	A	148	ALA	0	-0.005	0.003	14.656	-1.285	-1.285	0.000	0.000	0.000	0.000
56	A	149	LEU	0	0.006	-0.014	14.393	-1.166	-1.166	0.000	0.000	0.000	0.000
57	A	150	ALA	0	0.008	0.013	15.824	-0.441	-0.441	0.000	0.000	0.000	0.000
58	A	151	GLN	0	-0.028	-0.016	10.948	-2.071	-2.071	0.000	0.000	0.000	0.000
59	A	152	LEU	0	-0.021	-0.003	10.797	-2.024	-2.024	0.000	0.000	0.000	0.000
60	A	153	ALA	0	0.042	0.007	11.735	-0.875	-0.875	0.000	0.000	0.000	0.000
61	A	154	GLY	0	0.037	0.030	11.552	-0.158	-0.158	0.000	0.000	0.000	0.000
62	A	155	ILE	0	-0.031	-0.017	6.719	-2.126	-2.126	0.000	0.000	0.000	0.000
63	A	156	LEU	0	-0.038	-0.008	8.945	-0.893	-0.893	0.000	0.000	0.000	0.000
64	A	157	CYS	0	-0.042	-0.014	11.843	0.885	0.885	0.000	0.000	0.000	0.000
65	A	158	LEU	0	-0.011	-0.009	6.343	-0.354	-0.354	0.000	0.000	0.000	0.000
66	A	159	LYS	1	0.916	0.950	4.439	39.100	39.175	-0.001	-0.003	-0.071	0.000
67	A	160	SER	0	-0.011	-0.012	9.907	1.849	1.849	0.000	0.000	0.000	0.000
68	A	161	ASP	-1	-0.879	-0.935	11.888	-21.971	-21.971	0.000	0.000	0.000	0.000
69	A	162	ASP	-1	-0.930	-0.948	11.797	-22.758	-22.758	0.000	0.000	0.000	0.000
70	A	163	SER	0	-0.024	-0.037	12.816	1.627	1.627	0.000	0.000	0.000	0.000
71	A	164	GLN	0	0.029	0.014	8.217	-1.842	-1.842	0.000	0.000	0.000	0.000
72	A	165	LYS	1	0.924	0.971	9.141	26.143	26.143	0.000	0.000	0.000	0.000
73	A	166	ASN	0	-0.091	-0.044	10.404	1.676	1.676	0.000	0.000	0.000	0.000
74	A	167	ASN	0	0.019	0.018	12.403	2.244	2.244	0.000	0.000	0.000	0.000
75	A	168	LEU	0	0.003	-0.010	10.009	-2.799	-2.799	0.000	0.000	0.000	0.000
76	A	169	PHE	0	0.062	0.047	11.806	1.750	1.750	0.000	0.000	0.000	0.000
77	A	170	LEU	0	-0.053	-0.026	13.914	-1.266	-1.266	0.000	0.000	0.000	0.000
78	A	171	PHE	0	-0.028	-0.021	16.353	0.830	0.830	0.000	0.000	0.000	0.000
79	A	172	ALA	0	0.017	0.001	18.132	0.384	0.384	0.000	0.000	0.000	0.000
80	A	173	GLY	0	0.027	0.019	21.659	0.731	0.731	0.000	0.000	0.000	0.000
81	A	174	VAL	0	-0.052	-0.026	22.555	-0.637	-0.637	0.000	0.000	0.000	0.000
82	A	175	ASP	-1	-0.852	-0.913	24.447	-10.897	-10.897	0.000	0.000	0.000	0.000
83	A	176	GLY	0	-0.007	-0.015	26.636	-0.206	-0.206	0.000	0.000	0.000	0.000
84	A	177	VAL	0	0.056	0.042	25.013	-0.196	-0.196	0.000	0.000	0.000	0.000
85	A	178	ARG	1	0.820	0.895	27.545	10.424	10.424	0.000	0.000	0.000	0.000
86	A	179	TRP	0	0.053	0.039	24.532	-0.084	-0.084	0.000	0.000	0.000	0.000
87	A	180	LYS	1	0.885	0.953	27.996	10.090	10.090	0.000	0.000	0.000	0.000
88	A	181	LYS	1	0.906	0.941	28.078	10.231	10.231	0.000	0.000	0.000	0.000
89	A	182	PRO	0	0.009	0.010	27.098	-0.354	-0.354	0.000	0.000	0.000	0.000
90	A	183	VAL	0	0.004	0.010	21.074	0.007	0.007	0.000	0.000	0.000	0.000
91	A	184	LEU	0	-0.015	-0.020	24.486	0.096	0.096	0.000	0.000	0.000	0.000
92	A	185	PRO	0	0.017	0.000	21.942	-0.336	-0.336	0.000	0.000	0.000	0.000
93	A	186	GLY	0	-0.026	-0.012	21.239	0.468	0.468	0.000	0.000	0.000	0.000
94	A	187	ASP	-1	-0.871	-0.920	21.940	-11.063	-11.063	0.000	0.000	0.000	0.000
95	A	188	THR	0	-0.017	-0.020	16.877	-0.368	-0.368	0.000	0.000	0.000	0.000
96	A	189	LEU	0	-0.039	-0.021	17.317	0.488	0.488	0.000	0.000	0.000	0.000
97	A	190	THR	0	-0.028	-0.017	16.425	-0.909	-0.909	0.000	0.000	0.000	0.000
98	A	191	MET	0	-0.022	-0.018	14.138	0.715	0.715	0.000	0.000	0.000	0.000
99	A	192	GLN	0	0.011	0.009	16.285	-0.249	-0.249	0.000	0.000	0.000	0.000
100	A	193	ALA	0	0.010	0.009	15.749	0.517	0.517	0.000	0.000	0.000	0.000
101	A	194	ASN	0	-0.016	-0.003	17.569	-0.639	-0.639	0.000	0.000	0.000	0.000
102	A	195	LEU	0	0.023	0.006	17.727	0.141	0.141	0.000	0.000	0.000	0.000
103	A	196	ILE	0	-0.030	0.002	19.598	0.559	0.559	0.000	0.000	0.000	0.000
104	A	197	SER	0	-0.076	-0.063	22.144	0.781	0.781	0.000	0.000	0.000	0.000
105	A	198	PHE	0	0.060	0.024	15.056	-0.518	-0.518	0.000	0.000	0.000	0.000
106	A	199	LYS	1	0.916	0.968	21.323	12.063	12.063	0.000	0.000	0.000	0.000
107	A	200	SER	0	0.075	0.040	22.416	0.016	0.016	0.000	0.000	0.000	0.000
108	A	201	SER	0	0.021	0.011	23.447	-0.233	-0.233	0.000	0.000	0.000	0.000
109	A	202	LEU	0	-0.021	-0.018	25.806	0.048	0.048	0.000	0.000	0.000	0.000
110	A	203	GLY	0	0.039	0.034	21.970	-0.151	-0.151	0.000	0.000	0.000	0.000
111	A	204	ILE	0	-0.050	-0.027	20.862	-0.609	-0.609	0.000	0.000	0.000	0.000
112	A	205	ALA	0	-0.022	-0.002	17.780	0.217	0.217	0.000	0.000	0.000	0.000
113	A	206	LYS	1	0.823	0.892	19.791	12.199	12.199	0.000	0.000	0.000	0.000
114	A	207	LEU	0	0.041	0.021	16.121	-0.103	-0.103	0.000	0.000	0.000	0.000
115	A	208	SER	0	0.061	0.048	20.370	0.288	0.288	0.000	0.000	0.000	0.000
116	A	209	GLY	0	0.002	-0.016	20.018	-0.864	-0.864	0.000	0.000	0.000	0.000
117	A	210	VAL	0	-0.056	-0.026	20.579	0.835	0.835	0.000	0.000	0.000	0.000
118	A	211	GLY	0	0.075	0.031	20.208	-0.762	-0.762	0.000	0.000	0.000	0.000
119	A	212	TYR	0	-0.019	-0.024	20.718	0.958	0.958	0.000	0.000	0.000	0.000
120	A	213	VAL	0	0.074	0.052	21.188	-0.487	-0.487	0.000	0.000	0.000	0.000
121	A	214	ASN	0	-0.004	-0.015	23.040	0.452	0.452	0.000	0.000	0.000	0.000
122	A	215	GLY	0	0.046	0.025	23.942	0.378	0.378	0.000	0.000	0.000	0.000
123	A	216	LYS	1	0.896	0.956	25.603	10.149	10.149	0.000	0.000	0.000	0.000
124	A	217	VAL	0	0.024	0.015	25.392	-0.239	-0.239	0.000	0.000	0.000	0.000
125	A	218	VAL	0	-0.050	-0.029	23.117	0.485	0.485	0.000	0.000	0.000	0.000
126	A	219	ILE	0	0.005	0.016	21.943	0.187	0.187	0.000	0.000	0.000	0.000
127	A	220	ASN	0	-0.025	-0.011	24.399	0.147	0.147	0.000	0.000	0.000	0.000
128	A	221	ILE	0	0.056	0.019	21.126	0.224	0.224	0.000	0.000	0.000	0.000
129	A	222	SER	0	-0.034	-0.015	24.140	-0.141	-0.141	0.000	0.000	0.000	0.000
130	A	223	GLU	-1	-0.823	-0.906	23.799	-12.166	-12.166	0.000	0.000	0.000	0.000
131	A	224	MET	0	-0.026	0.019	18.223	-0.039	-0.039	0.000	0.000	0.000	0.000
132	A	225	THR	0	0.011	-0.007	20.903	-0.060	-0.060	0.000	0.000	0.000	0.000
133	A	226	PHE	0	-0.028	-0.018	15.259	-0.454	-0.454	0.000	0.000	0.000	0.000
134	A	227	ALA	0	0.034	0.015	18.592	0.549	0.549	0.000	0.000	0.000	0.000
135	A	228	LEU	0	0.021	0.017	15.447	-1.201	-1.201	0.000	0.000	0.000	0.000
136	A	229	SER	0	-0.041	-0.021	15.657	0.693	0.693	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:94:LYS)