FMO DATABASE

FMODB ID: VQ661

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

Total energy (hartree)

FMO2-HF: Electronic energy	-1179709.531486
FMO2-HF: Nuclear repulsion	1127530.757242
FMO2-HF: Total energy	-52178.774244
FMO2-MP2: Total energy	-52331.324119

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.
31.406	33.834	11.267	-6.749	-6.947	-0.069

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 : 0.946 / q_NPA : 0.974

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	-0.027	-0.019	1.779	-50.559	-48.283	11.268	-6.709	-6.835	-0.069
4	A	97	PRO	0	0.047	0.020	4.297	5.148	5.300	-0.001	-0.040	-0.112	0.000
5	A	98	HIS	0	-0.028	0.010	7.821	1.151	1.151	0.000	0.000	0.000	0.000
6	A	99	ARG	1	0.880	0.929	10.422	23.825	23.825	0.000	0.000	0.000	0.000
7	A	100	TYR	0	0.037	0.033	13.772	1.340	1.340	0.000	0.000	0.000	0.000
8	A	101	PRO	0	0.015	0.003	13.643	-1.635	-1.635	0.000	0.000	0.000	0.000
9	A	102	PHE	0	0.003	-0.005	11.917	-1.145	-1.145	0.000	0.000	0.000	0.000
10	A	103	LEU	0	0.011	0.008	5.890	0.114	0.114	0.000	0.000	0.000	0.000
11	A	104	LEU	0	-0.031	-0.017	10.009	1.549	1.549	0.000	0.000	0.000	0.000
12	A	105	VAL	0	-0.001	-0.015	8.976	1.395	1.395	0.000	0.000	0.000	0.000
13	A	106	ASP	-1	-0.763	-0.862	8.238	-20.737	-20.737	0.000	0.000	0.000	0.000
14	A	107	LYS	1	0.917	0.947	7.376	17.878	17.878	0.000	0.000	0.000	0.000
15	A	108	VAL	0	0.022	0.016	7.439	1.340	1.340	0.000	0.000	0.000	0.000
16	A	109	ILE	0	-0.054	-0.038	9.249	-0.051	-0.051	0.000	0.000	0.000	0.000
17	A	110	TYR	0	0.034	0.022	12.145	0.725	0.725	0.000	0.000	0.000	0.000
18	A	111	MET	0	-0.003	-0.011	10.476	-1.534	-1.534	0.000	0.000	0.000	0.000
19	A	112	GLN	0	0.004	0.012	13.569	0.725	0.725	0.000	0.000	0.000	0.000
20	A	113	PRO	0	0.062	0.023	12.995	0.122	0.122	0.000	0.000	0.000	0.000
21	A	114	ASN	0	-0.017	-0.017	15.041	1.345	1.345	0.000	0.000	0.000	0.000
22	A	115	LYS	1	0.897	0.963	17.090	14.793	14.793	0.000	0.000	0.000	0.000
23	A	116	THR	0	-0.012	-0.023	17.127	0.287	0.287	0.000	0.000	0.000	0.000
24	A	117	ILE	0	-0.001	0.004	9.970	-0.862	-0.862	0.000	0.000	0.000	0.000
25	A	118	ILE	0	0.023	0.015	13.909	0.860	0.860	0.000	0.000	0.000	0.000
26	A	119	GLY	0	0.044	0.008	11.836	-1.373	-1.373	0.000	0.000	0.000	0.000
27	A	120	LEU	0	-0.063	-0.017	11.824	1.330	1.330	0.000	0.000	0.000	0.000
28	A	121	LYS	1	0.780	0.888	11.921	16.565	16.565	0.000	0.000	0.000	0.000
29	A	122	GLN	0	0.011	0.018	13.786	1.388	1.388	0.000	0.000	0.000	0.000
30	A	123	VAL	0	0.015	0.012	16.086	-0.528	-0.528	0.000	0.000	0.000	0.000
31	A	124	SER	0	0.017	0.005	16.568	0.785	0.785	0.000	0.000	0.000	0.000
32	A	125	THR	0	0.003	-0.025	18.950	-0.185	-0.185	0.000	0.000	0.000	0.000
33	A	126	ASN	0	-0.001	0.004	17.409	0.649	0.649	0.000	0.000	0.000	0.000
34	A	127	GLU	-1	-0.781	-0.881	15.042	-17.066	-17.066	0.000	0.000	0.000	0.000
35	A	128	PRO	0	0.024	0.005	15.593	0.728	0.728	0.000	0.000	0.000	0.000
36	A	129	PHE	0	-0.001	-0.008	17.086	0.540	0.540	0.000	0.000	0.000	0.000
37	A	130	PHE	0	-0.021	-0.010	20.635	0.527	0.527	0.000	0.000	0.000	0.000
38	A	131	ASN	0	-0.056	-0.019	21.249	0.993	0.993	0.000	0.000	0.000	0.000
39	A	132	GLY	0	0.054	0.022	23.916	-0.372	-0.372	0.000	0.000	0.000	0.000
40	A	133	HIS	0	-0.081	-0.027	26.325	0.350	0.350	0.000	0.000	0.000	0.000
41	A	134	PHE	0	0.030	0.007	28.528	-0.220	-0.220	0.000	0.000	0.000	0.000
42	A	135	PRO	0	0.003	0.021	29.238	0.369	0.369	0.000	0.000	0.000	0.000
43	A	136	GLN	0	0.010	-0.004	31.565	-0.064	-0.064	0.000	0.000	0.000	0.000
44	A	137	LYS	1	0.916	0.958	29.896	9.384	9.384	0.000	0.000	0.000	0.000
45	A	138	GLN	0	0.040	0.023	25.720	-0.120	-0.120	0.000	0.000	0.000	0.000
46	A	139	ILE	0	-0.017	-0.025	26.094	0.089	0.089	0.000	0.000	0.000	0.000
47	A	140	MET	0	-0.024	0.007	17.701	-0.073	-0.073	0.000	0.000	0.000	0.000
48	A	141	PRO	0	0.036	0.018	22.262	0.216	0.216	0.000	0.000	0.000	0.000
49	A	142	GLY	0	0.065	0.021	22.833	-0.524	-0.524	0.000	0.000	0.000	0.000
50	A	143	VAL	0	0.034	-0.003	22.798	-0.348	-0.348	0.000	0.000	0.000	0.000
51	A	144	LEU	0	0.020	0.010	18.865	-0.557	-0.557	0.000	0.000	0.000	0.000
52	A	145	GLN	0	-0.010	-0.007	18.400	-0.744	-0.744	0.000	0.000	0.000	0.000
53	A	146	ILE	0	-0.011	0.005	19.231	-0.333	-0.333	0.000	0.000	0.000	0.000
54	A	147	GLU	-1	-0.787	-0.892	15.029	-21.324	-21.324	0.000	0.000	0.000	0.000
55	A	148	ALA	0	-0.017	-0.005	14.497	-1.343	-1.343	0.000	0.000	0.000	0.000
56	A	149	LEU	0	0.011	-0.009	14.241	-1.118	-1.118	0.000	0.000	0.000	0.000
57	A	150	ALA	0	0.014	0.012	15.860	-0.528	-0.528	0.000	0.000	0.000	0.000
58	A	151	GLN	0	-0.037	-0.035	11.163	-1.998	-1.998	0.000	0.000	0.000	0.000
59	A	152	LEU	0	-0.021	-0.003	10.970	-2.091	-2.091	0.000	0.000	0.000	0.000
60	A	153	ALA	0	0.029	-0.003	12.056	-0.642	-0.642	0.000	0.000	0.000	0.000
61	A	154	GLY	0	0.045	0.031	11.675	0.034	0.034	0.000	0.000	0.000	0.000
62	A	155	ILE	0	-0.032	-0.019	6.859	-1.983	-1.983	0.000	0.000	0.000	0.000
63	A	156	LEU	0	-0.013	0.003	8.977	-0.633	-0.633	0.000	0.000	0.000	0.000
64	A	157	CYS	0	-0.048	-0.003	12.006	0.804	0.804	0.000	0.000	0.000	0.000
65	A	158	LEU	0	-0.020	-0.020	6.418	-0.459	-0.459	0.000	0.000	0.000	0.000
66	A	159	LYS	1	0.918	0.960	4.967	36.266	36.266	0.000	0.000	0.000	0.000
67	A	160	SER	0	-0.007	-0.019	10.015	2.102	2.102	0.000	0.000	0.000	0.000
68	A	161	ASP	-1	-0.787	-0.868	11.627	-21.930	-21.930	0.000	0.000	0.000	0.000
69	A	162	ASP	-1	-0.937	-0.953	11.744	-22.050	-22.050	0.000	0.000	0.000	0.000
70	A	163	SER	0	-0.061	-0.056	13.604	1.085	1.085	0.000	0.000	0.000	0.000
71	A	164	GLN	0	0.023	0.005	8.380	-1.483	-1.483	0.000	0.000	0.000	0.000
72	A	165	LYS	1	0.910	0.963	8.772	27.440	27.440	0.000	0.000	0.000	0.000
73	A	166	ASN	0	-0.070	-0.039	10.063	1.551	1.551	0.000	0.000	0.000	0.000
74	A	167	ASN	0	-0.039	-0.008	12.180	2.480	2.480	0.000	0.000	0.000	0.000
75	A	168	LEU	0	0.015	-0.010	9.527	-3.037	-3.037	0.000	0.000	0.000	0.000
76	A	169	PHE	0	0.043	0.029	11.700	1.733	1.733	0.000	0.000	0.000	0.000
77	A	170	LEU	0	-0.054	-0.025	13.305	-1.598	-1.598	0.000	0.000	0.000	0.000
78	A	171	PHE	0	-0.021	-0.020	15.851	1.129	1.129	0.000	0.000	0.000	0.000
79	A	172	ALA	0	0.003	-0.005	17.799	0.162	0.162	0.000	0.000	0.000	0.000
80	A	173	GLY	0	0.033	0.022	21.331	0.796	0.796	0.000	0.000	0.000	0.000
81	A	174	VAL	0	-0.057	-0.035	22.575	-0.641	-0.641	0.000	0.000	0.000	0.000
82	A	175	ASP	-1	-0.835	-0.908	24.521	-11.361	-11.361	0.000	0.000	0.000	0.000
83	A	176	GLY	0	0.026	0.002	26.800	-0.146	-0.146	0.000	0.000	0.000	0.000
84	A	177	VAL	0	0.036	0.031	24.934	-0.073	-0.073	0.000	0.000	0.000	0.000
85	A	178	ARG	1	0.828	0.904	27.339	10.472	10.472	0.000	0.000	0.000	0.000
86	A	179	TRP	0	0.058	0.034	24.396	0.041	0.041	0.000	0.000	0.000	0.000
87	A	180	LYS	1	0.900	0.956	27.790	10.143	10.143	0.000	0.000	0.000	0.000
88	A	181	LYS	1	0.863	0.923	28.253	10.181	10.181	0.000	0.000	0.000	0.000
89	A	182	PRO	0	0.004	0.014	27.427	-0.314	-0.314	0.000	0.000	0.000	0.000
90	A	183	VAL	0	0.028	0.018	21.284	-0.036	-0.036	0.000	0.000	0.000	0.000
91	A	184	LEU	0	-0.011	-0.020	24.221	0.084	0.084	0.000	0.000	0.000	0.000
92	A	185	PRO	0	-0.009	-0.013	22.016	-0.363	-0.363	0.000	0.000	0.000	0.000
93	A	186	GLY	0	0.001	0.010	21.500	0.525	0.525	0.000	0.000	0.000	0.000
94	A	187	ASP	-1	-0.856	-0.917	21.816	-11.284	-11.284	0.000	0.000	0.000	0.000
95	A	188	THR	0	-0.019	-0.021	16.836	-0.406	-0.406	0.000	0.000	0.000	0.000
96	A	189	LEU	0	-0.018	-0.008	17.492	0.458	0.458	0.000	0.000	0.000	0.000
97	A	190	THR	0	-0.022	-0.009	16.466	-0.910	-0.910	0.000	0.000	0.000	0.000
98	A	191	MET	0	-0.049	-0.033	14.015	0.627	0.627	0.000	0.000	0.000	0.000
99	A	192	GLN	0	0.021	0.020	16.029	-0.218	-0.218	0.000	0.000	0.000	0.000
100	A	193	ALA	0	0.018	0.010	15.924	0.410	0.410	0.000	0.000	0.000	0.000
101	A	194	ASN	0	-0.002	-0.007	17.560	-0.604	-0.604	0.000	0.000	0.000	0.000
102	A	195	LEU	0	-0.007	0.009	18.007	0.180	0.180	0.000	0.000	0.000	0.000
103	A	196	ILE	0	-0.015	0.011	19.810	0.546	0.546	0.000	0.000	0.000	0.000
104	A	197	SER	0	-0.075	-0.063	22.062	0.806	0.806	0.000	0.000	0.000	0.000
105	A	198	PHE	0	0.052	0.025	14.856	-0.544	-0.544	0.000	0.000	0.000	0.000
106	A	199	LYS	1	0.947	0.989	21.067	12.136	12.136	0.000	0.000	0.000	0.000
107	A	200	SER	0	0.053	0.025	21.964	0.189	0.189	0.000	0.000	0.000	0.000
108	A	201	SER	0	0.021	0.003	22.939	-0.227	-0.227	0.000	0.000	0.000	0.000
109	A	202	LEU	0	-0.023	-0.014	25.158	0.354	0.354	0.000	0.000	0.000	0.000
110	A	203	GLY	0	0.018	0.025	21.512	-0.125	-0.125	0.000	0.000	0.000	0.000
111	A	204	ILE	0	-0.032	-0.019	20.624	-0.635	-0.635	0.000	0.000	0.000	0.000
112	A	205	ALA	0	-0.016	0.002	17.553	0.295	0.295	0.000	0.000	0.000	0.000
113	A	206	LYS	1	0.824	0.892	19.585	12.525	12.525	0.000	0.000	0.000	0.000
114	A	207	LEU	0	0.031	0.015	16.231	-0.031	-0.031	0.000	0.000	0.000	0.000
115	A	208	SER	0	0.064	0.047	20.497	0.228	0.228	0.000	0.000	0.000	0.000
116	A	209	GLY	0	0.002	-0.013	20.111	-0.883	-0.883	0.000	0.000	0.000	0.000
117	A	210	VAL	0	-0.044	-0.023	20.270	0.864	0.864	0.000	0.000	0.000	0.000
118	A	211	GLY	0	0.064	0.030	19.877	-0.789	-0.789	0.000	0.000	0.000	0.000
119	A	212	TYR	0	-0.028	-0.035	20.292	0.971	0.971	0.000	0.000	0.000	0.000
120	A	213	VAL	0	0.064	0.038	21.037	-0.490	-0.490	0.000	0.000	0.000	0.000
121	A	214	ASN	0	0.008	-0.005	22.923	0.457	0.457	0.000	0.000	0.000	0.000
122	A	215	GLY	0	0.052	0.033	23.793	0.419	0.419	0.000	0.000	0.000	0.000
123	A	216	LYS	1	0.879	0.945	25.462	10.153	10.153	0.000	0.000	0.000	0.000
124	A	217	VAL	0	0.028	0.017	25.175	-0.266	-0.266	0.000	0.000	0.000	0.000
125	A	218	VAL	0	-0.033	-0.020	22.891	0.472	0.472	0.000	0.000	0.000	0.000
126	A	219	ILE	0	-0.005	0.010	21.704	0.207	0.207	0.000	0.000	0.000	0.000
127	A	220	ASN	0	-0.005	-0.003	24.075	0.145	0.145	0.000	0.000	0.000	0.000
128	A	221	ILE	0	0.030	0.005	20.958	0.227	0.227	0.000	0.000	0.000	0.000
129	A	222	SER	0	-0.038	-0.018	24.095	-0.164	-0.164	0.000	0.000	0.000	0.000
130	A	223	GLU	-1	-0.826	-0.910	23.722	-12.333	-12.333	0.000	0.000	0.000	0.000
131	A	224	MET	0	-0.043	0.004	18.366	-0.058	-0.058	0.000	0.000	0.000	0.000
132	A	225	THR	0	0.029	0.012	21.054	-0.045	-0.045	0.000	0.000	0.000	0.000
133	A	226	PHE	0	-0.018	-0.016	15.209	-0.413	-0.413	0.000	0.000	0.000	0.000
134	A	227	ALA	0	0.055	0.039	18.526	0.328	0.328	0.000	0.000	0.000	0.000
135	A	228	LEU	0	-0.008	0.007	15.301	-1.396	-1.396	0.000	0.000	0.000	0.000
136	A	229	SER	0	-0.017	-0.011	15.641	0.873	0.873	0.000	0.000	0.000	0.000

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