FMO DATABASE

FMODB ID: 5JQ8Z

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:

Apendix: None

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	136
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-1178789.772192
FMO2-HF: Nuclear repulsion	1126612.259276
FMO2-HF: Total energy	-52177.512916
FMO2-MP2: Total energy	-52330.185579

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.
30.257	31.499	12.926	-7.297	-6.871	-0.087

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 : 0.902 / q_NPA : 0.936

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	-0.042	-0.024	1.775	-49.090	-48.108	12.928	-7.238	-6.672	-0.087
4	A	97	PRO	0	0.019	-0.009	4.417	4.347	4.506	-0.001	-0.051	-0.107	0.000
5	A	98	HIS	0	0.015	0.037	8.249	0.199	0.199	0.000	0.000	0.000	0.000
6	A	99	ARG	1	0.959	1.011	10.777	21.221	21.221	0.000	0.000	0.000	0.000
7	A	100	TYR	0	0.011	0.024	14.270	1.234	1.234	0.000	0.000	0.000	0.000
8	A	101	PRO	0	0.018	-0.001	13.709	-1.407	-1.407	0.000	0.000	0.000	0.000
9	A	102	PHE	0	0.014	0.001	12.384	-1.201	-1.201	0.000	0.000	0.000	0.000
10	A	103	LEU	0	0.014	0.012	5.798	0.099	0.099	0.000	0.000	0.000	0.000
11	A	104	LEU	0	-0.059	-0.045	10.066	1.118	1.118	0.000	0.000	0.000	0.000
12	A	105	VAL	0	0.014	-0.004	8.323	1.272	1.272	0.000	0.000	0.000	0.000
13	A	106	ASP	-1	-0.815	-0.884	7.943	-21.049	-21.049	0.000	0.000	0.000	0.000
14	A	107	LYS	1	0.906	0.939	7.391	17.924	17.924	0.000	0.000	0.000	0.000
15	A	108	VAL	0	0.031	0.022	7.388	1.272	1.272	0.000	0.000	0.000	0.000
16	A	109	ILE	0	-0.043	-0.036	9.439	-0.332	-0.332	0.000	0.000	0.000	0.000
17	A	110	TYR	0	0.024	0.007	12.099	0.866	0.866	0.000	0.000	0.000	0.000
18	A	111	MET	0	-0.023	-0.003	10.553	-1.482	-1.482	0.000	0.000	0.000	0.000
19	A	112	GLN	0	0.018	0.013	12.989	0.218	0.218	0.000	0.000	0.000	0.000
20	A	113	PRO	0	0.055	0.017	12.739	0.238	0.238	0.000	0.000	0.000	0.000
21	A	114	ASN	0	0.005	-0.007	14.829	1.137	1.137	0.000	0.000	0.000	0.000
22	A	115	LYS	1	0.934	0.978	17.018	14.573	14.573	0.000	0.000	0.000	0.000
23	A	116	THR	0	0.038	0.023	17.231	0.224	0.224	0.000	0.000	0.000	0.000
24	A	117	ILE	0	-0.001	0.016	9.833	-0.951	-0.951	0.000	0.000	0.000	0.000
25	A	118	ILE	0	0.011	0.009	13.593	0.872	0.872	0.000	0.000	0.000	0.000
26	A	119	GLY	0	0.022	0.002	12.028	-1.386	-1.386	0.000	0.000	0.000	0.000
27	A	120	LEU	0	-0.070	-0.026	11.709	1.381	1.381	0.000	0.000	0.000	0.000
28	A	121	LYS	1	0.867	0.930	11.790	16.862	16.862	0.000	0.000	0.000	0.000
29	A	122	GLN	0	-0.003	0.009	13.697	1.701	1.701	0.000	0.000	0.000	0.000
30	A	123	VAL	0	-0.011	0.015	15.622	-0.398	-0.398	0.000	0.000	0.000	0.000
31	A	124	SER	0	0.039	0.032	16.319	0.719	0.719	0.000	0.000	0.000	0.000
32	A	125	THR	0	0.001	-0.024	18.805	-0.123	-0.123	0.000	0.000	0.000	0.000
33	A	126	ASN	0	0.000	-0.014	18.142	0.216	0.216	0.000	0.000	0.000	0.000
34	A	127	GLU	-1	-0.793	-0.890	15.152	-16.572	-16.572	0.000	0.000	0.000	0.000
35	A	128	PRO	0	0.040	0.014	15.873	0.645	0.645	0.000	0.000	0.000	0.000
36	A	129	PHE	0	-0.018	-0.009	16.868	0.448	0.448	0.000	0.000	0.000	0.000
37	A	130	PHE	0	-0.028	-0.019	20.929	0.523	0.523	0.000	0.000	0.000	0.000
38	A	131	ASN	0	-0.004	0.011	20.831	0.809	0.809	0.000	0.000	0.000	0.000
39	A	132	GLY	0	0.023	0.014	24.006	-0.370	-0.370	0.000	0.000	0.000	0.000
40	A	133	HIS	0	-0.072	-0.032	26.724	0.395	0.395	0.000	0.000	0.000	0.000
41	A	134	PHE	0	0.022	0.004	28.777	-0.228	-0.228	0.000	0.000	0.000	0.000
42	A	135	PRO	0	-0.010	0.018	29.003	0.362	0.362	0.000	0.000	0.000	0.000
43	A	136	GLN	0	0.034	0.004	32.005	0.013	0.013	0.000	0.000	0.000	0.000
44	A	137	LYS	1	0.923	0.956	29.749	9.112	9.112	0.000	0.000	0.000	0.000
45	A	138	GLN	0	0.018	0.016	25.428	-0.005	-0.005	0.000	0.000	0.000	0.000
46	A	139	ILE	0	-0.009	-0.019	26.069	0.021	0.021	0.000	0.000	0.000	0.000
47	A	140	MET	0	-0.029	0.000	17.497	-0.033	-0.033	0.000	0.000	0.000	0.000
48	A	141	PRO	0	0.035	0.013	22.173	0.287	0.287	0.000	0.000	0.000	0.000
49	A	142	GLY	0	0.087	0.007	22.691	-0.500	-0.500	0.000	0.000	0.000	0.000
50	A	143	VAL	0	0.053	0.009	22.525	-0.406	-0.406	0.000	0.000	0.000	0.000
51	A	144	LEU	0	0.021	0.008	18.807	-0.506	-0.506	0.000	0.000	0.000	0.000
52	A	145	GLN	0	-0.010	-0.003	18.197	-0.687	-0.687	0.000	0.000	0.000	0.000
53	A	146	ILE	0	-0.019	-0.002	19.010	-0.440	-0.440	0.000	0.000	0.000	0.000
54	A	147	GLU	-1	-0.856	-0.934	15.517	-19.927	-19.927	0.000	0.000	0.000	0.000
55	A	148	ALA	0	-0.001	0.003	14.412	-1.289	-1.289	0.000	0.000	0.000	0.000
56	A	149	LEU	0	0.005	-0.017	14.224	-1.168	-1.168	0.000	0.000	0.000	0.000
57	A	150	ALA	0	0.014	0.014	15.873	-0.446	-0.446	0.000	0.000	0.000	0.000
58	A	151	GLN	0	-0.008	0.010	10.901	-1.910	-1.910	0.000	0.000	0.000	0.000
59	A	152	LEU	0	-0.009	-0.001	10.834	-2.052	-2.052	0.000	0.000	0.000	0.000
60	A	153	ALA	0	0.027	0.002	11.805	-0.906	-0.906	0.000	0.000	0.000	0.000
61	A	154	GLY	0	0.023	0.018	11.563	-0.186	-0.186	0.000	0.000	0.000	0.000
62	A	155	ILE	0	-0.037	-0.018	6.921	-2.140	-2.140	0.000	0.000	0.000	0.000
63	A	156	LEU	0	-0.031	-0.017	9.001	-0.957	-0.957	0.000	0.000	0.000	0.000
64	A	157	CYS	0	-0.017	0.005	11.919	0.853	0.853	0.000	0.000	0.000	0.000
65	A	158	LEU	0	0.002	-0.005	6.335	-0.622	-0.622	0.000	0.000	0.000	0.000
66	A	159	LYS	1	0.898	0.939	4.055	41.043	41.144	-0.001	-0.008	-0.092	0.000
67	A	160	SER	0	-0.029	-0.019	10.014	1.717	1.717	0.000	0.000	0.000	0.000
68	A	161	ASP	-1	-0.887	-0.927	11.913	-20.328	-20.328	0.000	0.000	0.000	0.000
69	A	162	ASP	-1	-0.924	-0.945	11.806	-22.594	-22.594	0.000	0.000	0.000	0.000
70	A	163	SER	0	-0.036	-0.039	12.776	1.365	1.365	0.000	0.000	0.000	0.000
71	A	164	GLN	0	0.030	0.008	8.165	-1.383	-1.383	0.000	0.000	0.000	0.000
72	A	165	LYS	1	0.928	0.971	9.477	25.375	25.375	0.000	0.000	0.000	0.000
73	A	166	ASN	0	-0.085	-0.043	10.741	1.625	1.625	0.000	0.000	0.000	0.000
74	A	167	ASN	0	0.035	0.016	12.719	1.799	1.799	0.000	0.000	0.000	0.000
75	A	168	LEU	0	-0.011	-0.008	10.599	-2.699	-2.699	0.000	0.000	0.000	0.000
76	A	169	PHE	0	0.070	0.047	12.261	1.691	1.691	0.000	0.000	0.000	0.000
77	A	170	LEU	0	-0.064	-0.045	14.034	-1.159	-1.159	0.000	0.000	0.000	0.000
78	A	171	PHE	0	-0.023	-0.024	16.475	0.781	0.781	0.000	0.000	0.000	0.000
79	A	172	ALA	0	0.023	0.002	18.206	0.375	0.375	0.000	0.000	0.000	0.000
80	A	173	GLY	0	0.021	0.018	21.749	0.712	0.712	0.000	0.000	0.000	0.000
81	A	174	VAL	0	-0.056	-0.026	22.559	-0.637	-0.637	0.000	0.000	0.000	0.000
82	A	175	ASP	-1	-0.820	-0.893	24.459	-10.745	-10.745	0.000	0.000	0.000	0.000
83	A	176	GLY	0	-0.037	-0.037	26.672	-0.192	-0.192	0.000	0.000	0.000	0.000
84	A	177	VAL	0	0.049	0.029	25.094	-0.188	-0.188	0.000	0.000	0.000	0.000
85	A	178	ARG	1	0.842	0.913	27.463	10.306	10.306	0.000	0.000	0.000	0.000
86	A	179	TRP	0	0.030	0.046	24.292	-0.086	-0.086	0.000	0.000	0.000	0.000
87	A	180	LYS	1	0.892	0.954	27.852	10.085	10.085	0.000	0.000	0.000	0.000
88	A	181	LYS	1	0.940	0.959	27.761	10.108	10.108	0.000	0.000	0.000	0.000
89	A	182	PRO	0	0.010	0.009	26.919	-0.344	-0.344	0.000	0.000	0.000	0.000
90	A	183	VAL	0	0.017	0.025	20.856	0.012	0.012	0.000	0.000	0.000	0.000
91	A	184	LEU	0	-0.028	-0.032	24.274	0.113	0.113	0.000	0.000	0.000	0.000
92	A	185	PRO	0	0.010	-0.007	21.682	-0.346	-0.346	0.000	0.000	0.000	0.000
93	A	186	GLY	0	-0.027	-0.011	21.009	0.459	0.459	0.000	0.000	0.000	0.000
94	A	187	ASP	-1	-0.872	-0.913	21.789	-11.065	-11.065	0.000	0.000	0.000	0.000
95	A	188	THR	0	-0.025	-0.031	16.990	-0.362	-0.362	0.000	0.000	0.000	0.000
96	A	189	LEU	0	-0.042	-0.027	17.094	0.471	0.471	0.000	0.000	0.000	0.000
97	A	190	THR	0	-0.014	-0.011	16.354	-0.994	-0.994	0.000	0.000	0.000	0.000
98	A	191	MET	0	-0.039	-0.027	13.711	0.706	0.706	0.000	0.000	0.000	0.000
99	A	192	GLN	0	-0.020	-0.015	16.206	-0.265	-0.265	0.000	0.000	0.000	0.000
100	A	193	ALA	0	-0.002	0.008	15.756	0.543	0.543	0.000	0.000	0.000	0.000
101	A	194	ASN	0	0.012	0.008	17.419	-0.937	-0.937	0.000	0.000	0.000	0.000
102	A	195	LEU	0	0.020	0.001	18.022	0.128	0.128	0.000	0.000	0.000	0.000
103	A	196	ILE	0	-0.031	-0.001	19.672	0.551	0.551	0.000	0.000	0.000	0.000
104	A	197	SER	0	-0.100	-0.068	22.256	0.762	0.762	0.000	0.000	0.000	0.000
105	A	198	PHE	0	0.069	0.027	15.421	-0.492	-0.492	0.000	0.000	0.000	0.000
106	A	199	LYS	1	0.920	0.968	21.594	11.898	11.898	0.000	0.000	0.000	0.000
107	A	200	SER	0	0.081	0.034	22.632	-0.167	-0.167	0.000	0.000	0.000	0.000
108	A	201	SER	0	0.008	0.009	23.664	-0.191	-0.191	0.000	0.000	0.000	0.000
109	A	202	LEU	0	-0.013	-0.016	26.180	0.040	0.040	0.000	0.000	0.000	0.000
110	A	203	GLY	0	0.043	0.036	22.246	-0.138	-0.138	0.000	0.000	0.000	0.000
111	A	204	ILE	0	-0.045	-0.023	21.205	-0.588	-0.588	0.000	0.000	0.000	0.000
112	A	205	ALA	0	-0.026	-0.002	18.200	0.227	0.227	0.000	0.000	0.000	0.000
113	A	206	LYS	1	0.868	0.933	20.160	12.013	12.013	0.000	0.000	0.000	0.000
114	A	207	LEU	0	0.031	0.017	16.210	-0.103	-0.103	0.000	0.000	0.000	0.000
115	A	208	SER	0	0.045	0.044	20.424	0.315	0.315	0.000	0.000	0.000	0.000
116	A	209	GLY	0	0.016	-0.010	20.090	-0.871	-0.871	0.000	0.000	0.000	0.000
117	A	210	VAL	0	-0.056	-0.025	20.339	0.828	0.828	0.000	0.000	0.000	0.000
118	A	211	GLY	0	0.069	0.027	20.193	-0.764	-0.764	0.000	0.000	0.000	0.000
119	A	212	TYR	0	-0.005	-0.022	20.719	0.954	0.954	0.000	0.000	0.000	0.000
120	A	213	VAL	0	0.072	0.049	21.135	-0.489	-0.489	0.000	0.000	0.000	0.000
121	A	214	ASN	0	-0.022	-0.019	23.031	0.370	0.370	0.000	0.000	0.000	0.000
122	A	215	GLY	0	0.043	0.021	23.969	0.370	0.370	0.000	0.000	0.000	0.000
123	A	216	LYS	1	0.904	0.958	25.649	10.058	10.058	0.000	0.000	0.000	0.000
124	A	217	VAL	0	0.014	0.011	25.359	-0.236	-0.236	0.000	0.000	0.000	0.000
125	A	218	VAL	0	-0.056	-0.033	22.868	0.452	0.452	0.000	0.000	0.000	0.000
126	A	219	ILE	0	0.001	0.012	21.787	0.189	0.189	0.000	0.000	0.000	0.000
127	A	220	ASN	0	-0.019	-0.009	24.328	0.177	0.177	0.000	0.000	0.000	0.000
128	A	221	ILE	0	0.042	0.016	21.231	0.233	0.233	0.000	0.000	0.000	0.000
129	A	222	SER	0	-0.036	-0.018	24.201	-0.133	-0.133	0.000	0.000	0.000	0.000
130	A	223	GLU	-1	-0.850	-0.933	23.866	-11.977	-11.977	0.000	0.000	0.000	0.000
131	A	224	MET	0	-0.039	0.010	18.357	-0.068	-0.068	0.000	0.000	0.000	0.000
132	A	225	THR	0	0.015	-0.009	20.930	-0.071	-0.071	0.000	0.000	0.000	0.000
133	A	226	PHE	0	-0.034	-0.019	15.105	-0.424	-0.424	0.000	0.000	0.000	0.000
134	A	227	ALA	0	0.037	0.013	18.945	0.536	0.536	0.000	0.000	0.000	0.000
135	A	228	LEU	0	0.034	0.027	15.571	-1.164	-1.164	0.000	0.000	0.000	0.000
136	A	229	SER	0	-0.047	-0.026	15.965	0.678	0.678	0.000	0.000	0.000	0.000

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