FMO DATABASE

FMODB ID: KGGY3

Calculation Name: 1Z94-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 1Z94

Chain ID: A

ChEMBL ID:

UniProt ID: Q7NY36

Base Structure: X-ray

Registration Date: 2023-09-21

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	143
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-1292354.950933
FMO2-HF: Nuclear repulsion	1237175.794995
FMO2-HF: Total energy	-55179.155938
FMO2-MP2: Total energy	-55340.264977

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:2:PRO)

Summations of interaction energy for fragment #1(A:2:PRO)

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.
-6.954	-4.276	-0.018	-1.19	-1.47	0

Interaction energy analysis for fragmet #1(A:2:PRO)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : -0.015 / q_NPA : -0.035

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].
3	A	4	THR	0	-0.027	-0.015	3.746	-0.916	1.296	-0.022	-1.055	-1.135
4	A	5	ILE	0	-0.017	0.009	5.473	0.186	0.186	0.000	0.000	0.000
5	A	6	ARG	1	0.810	0.894	8.310	-1.286	-1.286	0.000	0.000	0.000
6	A	7	LEU	0	0.011	0.017	11.209	-0.025	-0.025	0.000	0.000	0.000
7	A	8	HIS	0	0.010	-0.001	14.499	0.058	0.058	0.000	0.000	0.000
8	A	9	ARG	1	0.883	0.932	17.561	-0.172	-0.172	0.000	0.000	0.000
9	A	10	VAL	0	0.054	0.039	21.401	0.000	0.000	0.000	0.000	0.000
10	A	11	LEU	0	-0.025	-0.013	24.476	-0.010	-0.010	0.000	0.000	0.000
11	A	12	SER	0	-0.015	-0.026	27.414	0.005	0.005	0.000	0.000	0.000
12	A	13	ALA	0	0.002	-0.007	29.812	-0.009	-0.009	0.000	0.000	0.000
13	A	14	PRO	0	-0.007	0.002	30.466	0.008	0.008	0.000	0.000	0.000
14	A	15	PRO	0	0.046	0.017	28.402	-0.006	-0.006	0.000	0.000	0.000
15	A	16	GLU	-1	-0.798	-0.910	28.905	0.045	0.045	0.000	0.000	0.000
16	A	17	ARG	1	0.765	0.871	31.047	-0.044	-0.044	0.000	0.000	0.000
17	A	18	VAL	0	0.032	0.015	25.040	-0.008	-0.008	0.000	0.000	0.000
18	A	19	TYR	0	0.010	0.010	26.460	-0.005	-0.005	0.000	0.000	0.000
19	A	20	ARG	1	0.918	0.945	27.352	-0.036	-0.036	0.000	0.000	0.000
20	A	21	ALA	0	0.015	0.022	27.107	-0.010	-0.010	0.000	0.000	0.000
21	A	22	PHE	0	0.015	0.007	19.913	-0.009	-0.009	0.000	0.000	0.000
22	A	23	LEU	0	-0.060	-0.025	25.014	-0.007	-0.007	0.000	0.000	0.000
23	A	24	ASP	-1	-0.868	-0.930	27.810	-0.015	-0.015	0.000	0.000	0.000
24	A	25	PRO	0	0.023	0.005	29.384	-0.003	-0.003	0.000	0.000	0.000
25	A	26	LEU	0	-0.010	-0.009	30.326	-0.008	-0.008	0.000	0.000	0.000
26	A	27	ALA	0	-0.024	-0.011	29.342	-0.002	-0.002	0.000	0.000	0.000
27	A	28	LEU	0	-0.005	0.004	24.074	-0.005	-0.005	0.000	0.000	0.000
28	A	29	ALA	0	-0.011	-0.020	26.305	-0.010	-0.010	0.000	0.000	0.000
29	A	30	LYS	1	0.913	0.970	28.585	0.008	0.008	0.000	0.000	0.000
30	A	31	TRP	0	-0.049	-0.043	20.677	-0.001	-0.001	0.000	0.000	0.000
31	A	32	LEU	0	0.040	0.022	19.743	-0.003	-0.003	0.000	0.000	0.000
32	A	33	PRO	0	-0.026	0.019	21.525	-0.017	-0.017	0.000	0.000	0.000
33	A	34	PRO	0	0.043	0.029	19.267	0.016	0.016	0.000	0.000	0.000
34	A	35	GLU	-1	-0.756	-0.876	21.924	-0.049	-0.049	0.000	0.000	0.000
35	A	36	GLY	0	-0.016	-0.002	23.713	-0.012	-0.012	0.000	0.000	0.000
36	A	37	PHE	0	-0.063	-0.028	20.786	-0.013	-0.013	0.000	0.000	0.000
37	A	38	VAL	0	-0.007	0.010	25.540	0.015	0.015	0.000	0.000	0.000
38	A	39	CYS	0	-0.019	-0.008	25.638	-0.018	-0.018	0.000	0.000	0.000
39	A	40	LYS	1	0.858	0.944	27.324	0.115	0.115	0.000	0.000	0.000
40	A	41	VAL	0	0.034	0.006	27.865	-0.011	-0.011	0.000	0.000	0.000
41	A	42	LEU	0	-0.109	-0.044	27.848	0.004	0.004	0.000	0.000	0.000
42	A	43	GLU	-1	-0.927	-0.964	28.046	-0.084	-0.084	0.000	0.000	0.000
43	A	44	HIS	0	0.038	-0.003	28.114	-0.007	-0.007	0.000	0.000	0.000
44	A	45	ASP	-1	-0.835	-0.867	29.316	-0.012	-0.012	0.000	0.000	0.000
45	A	46	ALA	0	0.022	0.019	28.335	0.002	0.002	0.000	0.000	0.000
46	A	47	ARG	1	0.820	0.854	29.159	0.020	0.020	0.000	0.000	0.000
47	A	48	VAL	0	0.025	0.017	26.266	-0.006	-0.006	0.000	0.000	0.000
48	A	49	GLY	0	0.012	0.012	26.217	-0.002	-0.002	0.000	0.000	0.000
49	A	50	GLY	0	-0.003	0.013	27.354	-0.012	-0.012	0.000	0.000	0.000
50	A	51	ALA	0	-0.023	-0.022	25.583	-0.001	-0.001	0.000	0.000	0.000
51	A	52	TYR	0	-0.043	-0.043	19.178	0.006	0.006	0.000	0.000	0.000
52	A	53	LYS	1	0.845	0.898	24.215	0.155	0.155	0.000	0.000	0.000
53	A	54	MET	0	0.012	0.007	22.791	0.020	0.020	0.000	0.000	0.000
54	A	55	GLU	-1	-0.789	-0.891	24.408	-0.144	-0.144	0.000	0.000	0.000
55	A	56	PHE	0	0.072	0.024	19.655	0.018	0.018	0.000	0.000	0.000
56	A	57	LEU	0	-0.046	-0.033	24.377	-0.012	-0.012	0.000	0.000	0.000
57	A	58	ALA	0	0.047	0.034	23.833	0.012	0.012	0.000	0.000	0.000
58	A	59	PHE	0	-0.010	-0.015	25.611	0.005	0.005	0.000	0.000	0.000
59	A	60	ALA	0	-0.017	-0.010	28.107	0.005	0.005	0.000	0.000	0.000
60	A	61	SER	0	-0.026	-0.021	26.159	0.002	0.002	0.000	0.000	0.000
61	A	62	GLY	0	0.011	0.017	29.166	-0.001	-0.001	0.000	0.000	0.000
62	A	63	GLN	0	-0.013	0.000	22.059	-0.009	-0.009	0.000	0.000	0.000
63	A	64	LYS	1	0.873	0.933	24.783	0.145	0.145	0.000	0.000	0.000
64	A	65	HIS	0	0.016	0.004	19.104	-0.030	-0.030	0.000	0.000	0.000
65	A	66	ALA	0	-0.010	-0.001	22.038	0.018	0.018	0.000	0.000	0.000
66	A	67	PHE	0	0.036	0.019	19.272	-0.029	-0.029	0.000	0.000	0.000
67	A	68	GLY	0	0.017	0.000	20.254	0.032	0.032	0.000	0.000	0.000
68	A	69	GLY	0	0.021	0.032	19.836	-0.029	-0.029	0.000	0.000	0.000
69	A	70	ARG	1	0.853	0.912	20.891	0.069	0.069	0.000	0.000	0.000
70	A	71	TYR	0	0.047	0.029	21.401	0.005	0.005	0.000	0.000	0.000
71	A	72	LEU	0	-0.061	-0.033	18.924	-0.001	-0.001	0.000	0.000	0.000
72	A	73	GLU	-1	-0.812	-0.890	21.229	0.185	0.185	0.000	0.000	0.000
73	A	74	LEU	0	-0.036	-0.016	24.276	-0.004	-0.004	0.000	0.000	0.000
74	A	75	VAL	0	0.005	0.013	26.982	-0.004	-0.004	0.000	0.000	0.000
75	A	76	PRO	0	0.017	-0.008	28.185	0.007	0.007	0.000	0.000	0.000
76	A	77	GLY	0	0.015	0.009	29.080	0.002	0.002	0.000	0.000	0.000
77	A	78	GLU	-1	-0.957	-0.965	26.702	0.126	0.126	0.000	0.000	0.000
78	A	79	ARG	1	0.840	0.895	20.674	-0.191	-0.191	0.000	0.000	0.000
79	A	80	ILE	0	-0.004	0.011	22.044	-0.021	-0.021	0.000	0.000	0.000
80	A	81	ARG	1	0.875	0.924	15.642	-0.216	-0.216	0.000	0.000	0.000
81	A	82	TYR	0	0.017	0.004	18.313	0.000	0.000	0.000	0.000	0.000
82	A	83	THR	0	0.006	0.015	16.547	0.023	0.023	0.000	0.000	0.000
83	A	84	ASP	-1	-0.851	-0.929	15.229	-0.220	-0.220	0.000	0.000	0.000
84	A	85	ARG	1	0.902	0.941	15.026	0.191	0.191	0.000	0.000	0.000
85	A	86	PHE	0	0.046	0.017	14.665	0.045	0.045	0.000	0.000	0.000
86	A	87	ASP	-1	-0.901	-0.927	18.203	-0.219	-0.219	0.000	0.000	0.000
87	A	88	ASP	-1	-0.896	-0.948	18.002	-0.386	-0.386	0.000	0.000	0.000
88	A	89	ALA	0	-0.033	-0.028	17.223	-0.030	-0.030	0.000	0.000	0.000
89	A	90	GLY	0	-0.008	0.008	15.267	-0.061	-0.061	0.000	0.000	0.000
90	A	91	LEU	0	-0.058	-0.008	10.452	-0.046	-0.046	0.000	0.000	0.000
91	A	92	PRO	0	-0.011	-0.015	14.092	0.069	0.069	0.000	0.000	0.000
92	A	93	GLY	0	0.013	-0.018	12.282	-0.041	-0.041	0.000	0.000	0.000
93	A	94	ASP	-1	-0.862	-0.904	13.350	-0.224	-0.224	0.000	0.000	0.000
94	A	95	MET	0	-0.010	0.016	10.379	-0.076	-0.076	0.000	0.000	0.000
95	A	96	ILE	0	-0.037	-0.037	11.870	0.060	0.060	0.000	0.000	0.000
96	A	97	THR	0	-0.041	-0.007	12.767	0.071	0.071	0.000	0.000	0.000
97	A	98	THR	0	-0.036	-0.036	15.189	-0.007	-0.007	0.000	0.000	0.000
98	A	99	ILE	0	0.032	0.028	16.818	0.038	0.038	0.000	0.000	0.000
99	A	100	THR	0	-0.057	-0.053	19.266	0.013	0.013	0.000	0.000	0.000
100	A	101	LEU	0	-0.027	-0.007	21.349	-0.002	-0.002	0.000	0.000	0.000
101	A	102	ALA	0	0.051	0.029	24.467	0.003	0.003	0.000	0.000	0.000
102	A	103	PRO	0	0.002	0.000	26.978	-0.005	-0.005	0.000	0.000	0.000
103	A	104	LEU	0	-0.007	-0.004	26.715	0.008	0.008	0.000	0.000	0.000
104	A	105	SER	0	-0.031	-0.026	31.080	-0.008	-0.008	0.000	0.000	0.000
105	A	106	CYS	0	-0.029	-0.010	30.299	-0.003	-0.003	0.000	0.000	0.000
106	A	107	GLY	0	0.019	0.011	31.322	-0.007	-0.007	0.000	0.000	0.000
107	A	108	ALA	0	-0.012	-0.010	27.238	0.002	0.002	0.000	0.000	0.000
108	A	109	ASP	-1	-0.870	-0.911	22.020	0.221	0.221	0.000	0.000	0.000
109	A	110	LEU	0	0.005	-0.001	20.562	-0.010	-0.010	0.000	0.000	0.000
110	A	111	SER	0	0.010	-0.001	18.048	0.026	0.026	0.000	0.000	0.000
111	A	112	ILE	0	-0.023	-0.008	15.202	-0.018	-0.018	0.000	0.000	0.000
112	A	113	VAL	0	-0.018	-0.006	11.154	0.082	0.082	0.000	0.000	0.000
113	A	114	GLN	0	0.002	0.012	10.993	-0.088	-0.088	0.000	0.000	0.000
114	A	115	GLU	-1	-0.795	-0.901	8.176	1.205	1.205	0.000	0.000	0.000
115	A	116	GLY	0	0.050	0.020	6.969	-0.098	-0.098	0.000	0.000	0.000
116	A	117	ILE	0	-0.031	-0.018	6.539	-0.081	-0.081	0.000	0.000	0.000
117	A	118	PRO	0	0.036	0.008	6.224	-0.950	-0.950	0.000	0.000	0.000
118	A	119	ASP	-1	-0.844	-0.922	3.966	-5.128	-4.903	0.000	-0.080	-0.146
119	A	120	ALA	0	-0.050	-0.015	5.812	0.317	0.317	0.000	0.000	0.000
120	A	121	ILE	0	-0.028	-0.011	8.255	0.286	0.286	0.000	0.000	0.000
121	A	122	PRO	0	0.048	0.028	6.506	-0.304	-0.304	0.000	0.000	0.000
122	A	123	PRO	0	0.076	0.024	3.653	0.173	0.414	0.004	-0.055	-0.189
123	A	124	GLU	-1	-0.935	-0.955	6.919	-0.142	-0.142	0.000	0.000	0.000
124	A	125	ASN	0	0.014	-0.006	9.642	0.042	0.042	0.000	0.000	0.000
125	A	126	CYS	0	-0.002	0.015	9.409	0.057	0.057	0.000	0.000	0.000
126	A	127	TYR	0	0.008	-0.016	7.731	0.157	0.157	0.000	0.000	0.000
127	A	128	LEU	0	-0.054	-0.012	12.233	0.056	0.056	0.000	0.000	0.000
128	A	129	GLY	0	0.056	0.030	14.889	0.029	0.029	0.000	0.000	0.000
129	A	130	TRP	0	0.019	-0.011	12.845	0.067	0.067	0.000	0.000	0.000
130	A	131	GLN	0	-0.084	-0.054	14.862	0.052	0.052	0.000	0.000	0.000
131	A	132	GLN	0	-0.097	-0.050	18.211	-0.006	-0.006	0.000	0.000	0.000
132	A	133	SER	0	0.021	-0.001	19.598	0.010	0.010	0.000	0.000	0.000
133	A	134	LEU	0	-0.002	-0.017	17.473	0.014	0.014	0.000	0.000	0.000
134	A	135	LYS	1	0.797	0.905	21.447	0.024	0.024	0.000	0.000	0.000
135	A	136	GLN	0	-0.059	-0.039	24.024	0.003	0.003	0.000	0.000	0.000
136	A	137	LEU	0	-0.010	-0.001	22.862	0.003	0.003	0.000	0.000	0.000
137	A	138	ALA	0	0.012	0.005	25.412	0.003	0.003	0.000	0.000	0.000
138	A	139	ALA	0	0.017	0.002	27.163	0.000	0.000	0.000	0.000	0.000
139	A	140	LEU	0	-0.063	-0.018	28.865	-0.005	-0.005	0.000	0.000	0.000
140	A	141	VAL	0	-0.031	-0.019	27.586	0.000	0.000	0.000	0.000	0.000
141	A	142	GLU	-1	-0.806	-0.880	29.533	0.066	0.066	0.000	0.000	0.000
142	A	143	PRO	0	-0.018	0.002	32.255	0.001	0.001	0.000	0.000	0.000
143	A	144	ASP	-1	-0.963	-0.952	35.590	0.025	0.025	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:2:PRO)