FMO DATABASE

FMODB ID: 149ZZ

Calculation Name: 4CZD-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 4CZD

Chain ID: A

ChEMBL ID:

UniProt ID: B8J364

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:

Apendix: None

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	145
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-1138156.300482
FMO2-HF: Nuclear repulsion	1081409.966209
FMO2-HF: Total energy	-56746.334273
FMO2-MP2: Total energy	-56912.682849

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:22:ASP)

Summations of interaction energy for fragment #1(A:22:ASP)

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.
-138.335	-137.844	14.063	-8.305	-6.249	0.093

Interaction energy analysis for fragmet #1(A:22:ASP)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : -1 / q_Mulliken : -0.848 / q_NPA : -0.924

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	24	ASP	-1	-0.745	-0.822	3.902	33.377	35.139	-0.012	-0.792	-0.958	0.004
4	A	25	SER	0	0.008	-0.015	6.736	-0.443	-0.443	0.000	0.000	0.000	0.000
5	A	26	MET	0	0.002	0.041	9.408	-2.466	-2.466	0.000	0.000	0.000	0.000
6	A	27	ASP	-1	-0.769	-0.893	7.480	36.292	36.292	0.000	0.000	0.000	0.000
7	A	28	ARG	1	0.816	0.882	3.330	-49.859	-49.552	0.010	-0.072	-0.245	0.000
8	A	29	GLN	0	0.014	0.001	9.592	-2.806	-2.806	0.000	0.000	0.000	0.000
9	A	30	LEU	0	-0.001	0.009	12.061	-1.505	-1.505	0.000	0.000	0.000	0.000
10	A	31	LEU	0	-0.006	-0.019	7.836	-1.275	-1.275	0.000	0.000	0.000	0.000
11	A	32	ASP	-1	-0.941	-0.946	12.105	16.548	16.548	0.000	0.000	0.000	0.000
12	A	33	ILE	0	0.031	0.022	14.499	-1.351	-1.351	0.000	0.000	0.000	0.000
13	A	34	ILE	0	-0.047	-0.040	13.464	-0.889	-0.889	0.000	0.000	0.000	0.000
14	A	35	GLN	0	-0.102	-0.057	12.134	-0.556	-0.556	0.000	0.000	0.000	0.000
15	A	36	THR	0	-0.049	-0.024	16.449	-1.014	-1.014	0.000	0.000	0.000	0.000
16	A	37	GLY	0	-0.009	-0.018	19.566	-0.862	-0.862	0.000	0.000	0.000	0.000
17	A	38	PHE	0	-0.036	-0.006	18.412	0.210	0.210	0.000	0.000	0.000	0.000
18	A	39	PRO	0	-0.026	-0.005	20.741	-0.592	-0.592	0.000	0.000	0.000	0.000
19	A	40	LEU	0	-0.009	0.000	23.927	-0.066	-0.066	0.000	0.000	0.000	0.000
20	A	41	SER	0	-0.016	-0.031	26.895	-0.416	-0.416	0.000	0.000	0.000	0.000
21	A	42	PRO	0	0.001	-0.011	27.690	0.303	0.303	0.000	0.000	0.000	0.000
22	A	43	ARG	1	0.829	0.889	27.173	-11.523	-11.523	0.000	0.000	0.000	0.000
23	A	44	PRO	0	0.037	0.044	23.046	0.219	0.219	0.000	0.000	0.000	0.000
24	A	45	TYR	0	0.039	0.003	18.485	0.672	0.672	0.000	0.000	0.000	0.000
25	A	46	ALA	0	0.070	0.035	21.880	0.465	0.465	0.000	0.000	0.000	0.000
26	A	47	GLU	-1	-0.833	-0.877	24.299	12.364	12.364	0.000	0.000	0.000	0.000
27	A	48	LEU	0	-0.019	-0.021	17.762	0.186	0.186	0.000	0.000	0.000	0.000
28	A	49	GLY	0	0.034	0.022	20.111	0.498	0.498	0.000	0.000	0.000	0.000
29	A	50	GLN	0	-0.035	-0.043	21.154	-0.026	-0.026	0.000	0.000	0.000	0.000
30	A	51	ARG	1	0.831	0.912	21.475	-13.873	-13.873	0.000	0.000	0.000	0.000
31	A	52	LEU	0	-0.042	-0.017	15.703	0.401	0.401	0.000	0.000	0.000	0.000
32	A	53	GLY	0	-0.002	0.015	18.352	0.516	0.516	0.000	0.000	0.000	0.000
33	A	54	LEU	0	-0.066	-0.037	15.317	0.398	0.398	0.000	0.000	0.000	0.000
34	A	55	ASP	-1	-0.779	-0.896	19.542	14.334	14.334	0.000	0.000	0.000	0.000
35	A	56	GLU	-1	-0.813	-0.889	19.650	13.384	13.384	0.000	0.000	0.000	0.000
36	A	57	GLN	0	-0.044	-0.044	18.965	-0.306	-0.306	0.000	0.000	0.000	0.000
37	A	58	GLU	-1	-0.774	-0.888	14.282	22.916	22.916	0.000	0.000	0.000	0.000
38	A	59	VAL	0	0.001	-0.001	15.310	1.579	1.579	0.000	0.000	0.000	0.000
39	A	60	LEU	0	-0.032	-0.013	16.112	0.719	0.719	0.000	0.000	0.000	0.000
40	A	61	ASP	-1	-0.795	-0.884	14.633	18.688	18.688	0.000	0.000	0.000	0.000
41	A	62	ARG	1	0.771	0.867	10.025	-27.067	-27.067	0.000	0.000	0.000	0.000
42	A	63	VAL	0	0.000	-0.001	12.022	1.435	1.435	0.000	0.000	0.000	0.000
43	A	64	ARG	1	0.805	0.898	14.417	-17.071	-17.071	0.000	0.000	0.000	0.000
44	A	65	GLY	0	0.050	0.021	10.533	0.069	0.069	0.000	0.000	0.000	0.000
45	A	66	LEU	0	0.032	-0.004	7.070	2.009	2.009	0.000	0.000	0.000	0.000
46	A	67	LYS	1	0.886	0.971	9.579	-19.175	-19.175	0.000	0.000	0.000	0.000
47	A	68	ALA	0	-0.019	-0.009	11.419	-0.757	-0.757	0.000	0.000	0.000	0.000
48	A	69	ARG	1	0.817	0.869	1.726	-98.894	-100.540	14.066	-7.429	-4.991	0.089
49	A	70	LYS	1	0.861	0.930	8.247	-21.123	-21.123	0.000	0.000	0.000	0.000
50	A	71	ILE	0	0.025	0.030	4.312	-1.642	-1.574	-0.001	-0.012	-0.055	0.000
51	A	72	ILE	0	-0.031	-0.006	8.151	-1.828	-1.828	0.000	0.000	0.000	0.000
52	A	73	ARG	1	0.975	0.981	11.680	-17.651	-17.651	0.000	0.000	0.000	0.000
53	A	74	ARG	1	0.835	0.896	13.675	-14.465	-14.465	0.000	0.000	0.000	0.000
54	A	75	LEU	0	0.029	0.019	16.199	0.619	0.619	0.000	0.000	0.000	0.000
55	A	76	GLY	0	0.022	0.007	18.414	-0.494	-0.494	0.000	0.000	0.000	0.000
56	A	77	ALA	0	0.017	0.024	21.736	0.220	0.220	0.000	0.000	0.000	0.000
57	A	78	ASN	0	0.022	0.010	20.254	0.259	0.259	0.000	0.000	0.000	0.000
58	A	79	PHE	0	0.050	0.020	24.352	-0.162	-0.162	0.000	0.000	0.000	0.000
59	A	80	GLN	0	0.015	0.019	27.759	-0.119	-0.119	0.000	0.000	0.000	0.000
60	A	81	SER	0	0.076	0.022	29.684	-0.227	-0.227	0.000	0.000	0.000	0.000
61	A	82	ALA	0	0.077	0.043	32.235	-0.220	-0.220	0.000	0.000	0.000	0.000
62	A	83	LYS	1	0.866	0.920	33.003	-8.855	-8.855	0.000	0.000	0.000	0.000
63	A	84	LEU	0	-0.030	-0.005	31.505	-0.028	-0.028	0.000	0.000	0.000	0.000
64	A	85	GLY	0	0.007	0.012	35.522	-0.131	-0.131	0.000	0.000	0.000	0.000
65	A	86	PHE	0	-0.019	0.008	35.128	-0.117	-0.117	0.000	0.000	0.000	0.000
66	A	87	VAL	0	-0.030	-0.016	36.854	0.080	0.080	0.000	0.000	0.000	0.000
67	A	88	SER	0	0.013	-0.001	32.798	0.041	0.041	0.000	0.000	0.000	0.000
68	A	89	THR	0	-0.030	-0.024	35.895	-0.150	-0.150	0.000	0.000	0.000	0.000
69	A	90	LEU	0	-0.014	0.022	33.979	0.250	0.250	0.000	0.000	0.000	0.000
70	A	91	CYS	0	-0.013	0.011	36.673	-0.275	-0.275	0.000	0.000	0.000	0.000
71	A	92	ALA	0	0.015	0.010	38.071	0.198	0.198	0.000	0.000	0.000	0.000
72	A	93	ALA	0	0.023	0.005	40.522	-0.201	-0.201	0.000	0.000	0.000	0.000
73	A	94	LYS	1	0.929	0.974	42.376	-6.209	-6.209	0.000	0.000	0.000	0.000
74	A	95	VAL	0	0.011	0.013	42.159	-0.157	-0.157	0.000	0.000	0.000	0.000
75	A	96	PRO	0	0.017	0.029	44.469	0.100	0.100	0.000	0.000	0.000	0.000
76	A	97	GLN	0	0.036	-0.016	42.555	0.103	0.103	0.000	0.000	0.000	0.000
77	A	98	ASP	-1	-0.895	-0.943	46.345	6.197	6.197	0.000	0.000	0.000	0.000
78	A	99	LYS	1	0.877	0.935	46.968	-6.067	-6.067	0.000	0.000	0.000	0.000
79	A	100	MET	0	-0.031	0.008	40.647	0.162	0.162	0.000	0.000	0.000	0.000
80	A	101	ASP	-1	-0.865	-0.938	41.051	7.436	7.436	0.000	0.000	0.000	0.000
81	A	102	ALA	0	0.000	0.002	41.720	0.102	0.102	0.000	0.000	0.000	0.000
82	A	103	PHE	0	0.036	0.005	40.739	0.077	0.077	0.000	0.000	0.000	0.000
83	A	104	VAL	0	-0.005	-0.006	36.655	0.142	0.142	0.000	0.000	0.000	0.000
84	A	105	ALA	0	-0.026	-0.007	38.251	0.198	0.198	0.000	0.000	0.000	0.000
85	A	106	GLU	-1	-0.858	-0.917	39.726	7.053	7.053	0.000	0.000	0.000	0.000
86	A	107	VAL	0	-0.010	-0.003	36.727	0.047	0.047	0.000	0.000	0.000	0.000
87	A	108	ASN	0	0.015	0.005	34.884	0.220	0.220	0.000	0.000	0.000	0.000
88	A	109	ALA	0	-0.043	0.006	36.021	0.176	0.176	0.000	0.000	0.000	0.000
89	A	110	LYS	1	0.809	0.873	37.096	-7.555	-7.555	0.000	0.000	0.000	0.000
90	A	111	PRO	0	0.011	-0.002	34.518	0.183	0.183	0.000	0.000	0.000	0.000
91	A	112	GLY	0	0.024	0.026	33.716	0.215	0.215	0.000	0.000	0.000	0.000
92	A	113	VAL	0	-0.026	-0.007	33.798	0.035	0.035	0.000	0.000	0.000	0.000
93	A	114	THR	0	-0.027	-0.027	28.672	0.083	0.083	0.000	0.000	0.000	0.000
94	A	115	HIS	0	-0.025	-0.005	25.664	0.091	0.091	0.000	0.000	0.000	0.000
95	A	116	ASN	0	0.039	-0.002	30.376	-0.338	-0.338	0.000	0.000	0.000	0.000
96	A	117	TYR	0	-0.013	-0.006	26.352	0.313	0.313	0.000	0.000	0.000	0.000
97	A	118	LEU	0	0.069	0.046	33.109	-0.209	-0.209	0.000	0.000	0.000	0.000
98	A	119	ARG	1	0.805	0.898	29.724	-8.933	-8.933	0.000	0.000	0.000	0.000
99	A	120	GLU	-1	-0.914	-0.953	35.877	7.835	7.835	0.000	0.000	0.000	0.000
100	A	121	HIS	0	-0.010	0.002	38.062	0.024	0.024	0.000	0.000	0.000	0.000
101	A	122	ASP	-1	-0.887	-0.950	41.080	6.574	6.574	0.000	0.000	0.000	0.000
102	A	123	TYR	0	-0.046	-0.036	41.272	-0.134	-0.134	0.000	0.000	0.000	0.000
103	A	124	ASN	0	0.048	0.033	39.649	0.183	0.183	0.000	0.000	0.000	0.000
104	A	125	ILE	0	0.011	0.012	37.453	0.235	0.235	0.000	0.000	0.000	0.000
105	A	126	TRP	0	-0.023	-0.033	35.129	-0.097	-0.097	0.000	0.000	0.000	0.000
106	A	127	PHE	0	0.011	-0.008	34.047	0.243	0.243	0.000	0.000	0.000	0.000
107	A	128	THR	0	-0.030	-0.011	30.676	-0.214	-0.214	0.000	0.000	0.000	0.000
108	A	129	LEU	0	0.000	0.003	33.888	-0.012	-0.012	0.000	0.000	0.000	0.000
109	A	130	ILE	0	-0.057	-0.036	31.358	-0.019	-0.019	0.000	0.000	0.000	0.000
110	A	131	SER	0	-0.005	-0.002	35.894	-0.076	-0.076	0.000	0.000	0.000	0.000
111	A	132	PRO	0	0.024	0.004	38.598	0.106	0.106	0.000	0.000	0.000	0.000
112	A	133	SER	0	0.018	0.000	40.429	-0.099	-0.099	0.000	0.000	0.000	0.000
113	A	134	ARG	1	0.865	0.914	38.823	-7.344	-7.344	0.000	0.000	0.000	0.000
114	A	135	GLU	-1	-0.828	-0.920	44.085	6.541	6.541	0.000	0.000	0.000	0.000
115	A	136	GLU	-1	-0.832	-0.889	43.174	7.033	7.033	0.000	0.000	0.000	0.000
116	A	137	THR	0	-0.063	-0.046	40.339	0.108	0.108	0.000	0.000	0.000	0.000
117	A	138	GLN	0	-0.035	-0.029	42.499	0.155	0.155	0.000	0.000	0.000	0.000
118	A	139	ALA	0	0.047	0.028	45.659	-0.033	-0.033	0.000	0.000	0.000	0.000
119	A	140	ILE	0	-0.025	-0.013	40.552	-0.016	-0.016	0.000	0.000	0.000	0.000
120	A	141	LEU	0	-0.035	-0.020	41.043	0.029	0.029	0.000	0.000	0.000	0.000
121	A	142	ASP	-1	-0.810	-0.895	44.645	6.195	6.195	0.000	0.000	0.000	0.000
122	A	143	GLY	0	-0.008	-0.001	47.368	-0.108	-0.108	0.000	0.000	0.000	0.000
123	A	144	ILE	0	0.014	0.005	41.338	-0.039	-0.039	0.000	0.000	0.000	0.000
124	A	145	THR	0	-0.045	-0.023	45.647	-0.039	-0.039	0.000	0.000	0.000	0.000
125	A	146	GLN	0	-0.049	-0.030	48.382	-0.155	-0.155	0.000	0.000	0.000	0.000
126	A	147	ALA	0	-0.028	-0.006	47.243	-0.101	-0.101	0.000	0.000	0.000	0.000
127	A	148	THR	0	-0.032	-0.033	45.440	0.006	0.006	0.000	0.000	0.000	0.000
128	A	149	GLY	0	0.006	0.007	48.933	-0.062	-0.062	0.000	0.000	0.000	0.000
129	A	150	VAL	0	-0.036	-0.019	45.738	-0.055	-0.055	0.000	0.000	0.000	0.000
130	A	151	PRO	0	0.018	0.016	47.592	0.080	0.080	0.000	0.000	0.000	0.000
131	A	152	ILE	0	-0.012	-0.002	42.341	0.120	0.120	0.000	0.000	0.000	0.000
132	A	153	LEU	0	-0.037	-0.007	43.322	-0.106	-0.106	0.000	0.000	0.000	0.000
133	A	154	ASN	0	0.046	0.017	41.973	0.368	0.368	0.000	0.000	0.000	0.000
134	A	155	LEU	0	-0.036	-0.021	39.617	-0.148	-0.148	0.000	0.000	0.000	0.000
135	A	156	PRO	0	0.021	0.021	38.968	0.235	0.235	0.000	0.000	0.000	0.000
136	A	157	ALA	0	-0.001	-0.004	36.246	-0.097	-0.097	0.000	0.000	0.000	0.000
137	A	158	THR	0	-0.010	-0.013	38.302	-0.046	-0.046	0.000	0.000	0.000	0.000
138	A	159	LYS	1	0.910	0.951	38.509	-7.121	-7.121	0.000	0.000	0.000	0.000
139	A	160	LEU	0	0.011	0.011	30.887	0.086	0.086	0.000	0.000	0.000	0.000
140	A	161	PHE	0	0.027	0.009	33.317	-0.099	-0.099	0.000	0.000	0.000	0.000
141	A	162	LYS	1	0.964	0.978	25.499	-10.742	-10.742	0.000	0.000	0.000	0.000
142	A	163	ILE	0	0.016	0.013	26.172	-0.193	-0.193	0.000	0.000	0.000	0.000
143	A	164	ARG	1	0.835	0.910	19.691	-13.453	-13.453	0.000	0.000	0.000	0.000
144	A	165	VAL	0	-0.004	-0.011	21.467	-0.222	-0.222	0.000	0.000	0.000	0.000
145	A	166	ASP	-1	-0.808	-0.876	15.417	14.105	14.105	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:22:ASP)