FMO DATABASE

FMODB ID: QVVRY

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

Total energy (hartree)

FMO2-HF: Electronic energy	-1292013.189803
FMO2-HF: Nuclear repulsion	1236834.381732
FMO2-HF: Total energy	-55178.808071
FMO2-MP2: Total energy	-55339.9337

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.
-7.835	-4.566	-0.016	-1.488	-1.764	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 : -0.019 / q_NPA : -0.034

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	-0.035	-0.017	3.371	-1.615	1.198	-0.025	-1.410	-1.378
4	A	5	ILE	0	-0.018	0.005	5.051	0.352	0.449	-0.001	-0.005	-0.091
5	A	6	ARG	1	0.875	0.932	7.740	-1.225	-1.225	0.000	0.000	0.000
6	A	7	LEU	0	-0.006	0.001	10.796	-0.018	-0.018	0.000	0.000	0.000
7	A	8	HIS	0	0.014	0.000	14.204	0.061	0.061	0.000	0.000	0.000
8	A	9	ARG	1	0.876	0.932	17.187	-0.167	-0.167	0.000	0.000	0.000
9	A	10	VAL	0	0.048	0.041	21.010	0.004	0.004	0.000	0.000	0.000
10	A	11	LEU	0	-0.025	-0.017	24.051	-0.011	-0.011	0.000	0.000	0.000
11	A	12	SER	0	-0.014	-0.019	26.900	0.007	0.007	0.000	0.000	0.000
12	A	13	ALA	0	0.005	-0.008	29.574	-0.009	-0.009	0.000	0.000	0.000
13	A	14	PRO	0	0.002	0.006	30.204	0.008	0.008	0.000	0.000	0.000
14	A	15	PRO	0	0.063	0.016	28.120	-0.007	-0.007	0.000	0.000	0.000
15	A	16	GLU	-1	-0.849	-0.938	28.698	0.036	0.036	0.000	0.000	0.000
16	A	17	ARG	1	0.785	0.886	30.906	-0.038	-0.038	0.000	0.000	0.000
17	A	18	VAL	0	0.033	0.013	24.835	-0.008	-0.008	0.000	0.000	0.000
18	A	19	TYR	0	0.021	0.021	26.220	-0.007	-0.007	0.000	0.000	0.000
19	A	20	ARG	1	0.957	0.973	27.153	-0.026	-0.026	0.000	0.000	0.000
20	A	21	ALA	0	0.009	0.019	26.935	-0.010	-0.010	0.000	0.000	0.000
21	A	22	PHE	0	0.014	0.000	19.787	-0.009	-0.009	0.000	0.000	0.000
22	A	23	LEU	0	-0.046	-0.016	24.797	-0.011	-0.011	0.000	0.000	0.000
23	A	24	ASP	-1	-0.880	-0.931	27.501	-0.028	-0.028	0.000	0.000	0.000
24	A	25	PRO	0	0.025	0.011	29.354	-0.004	-0.004	0.000	0.000	0.000
25	A	26	LEU	0	-0.017	-0.012	30.409	-0.007	-0.007	0.000	0.000	0.000
26	A	27	ALA	0	-0.036	-0.011	29.254	-0.001	-0.001	0.000	0.000	0.000
27	A	28	LEU	0	-0.012	-0.007	23.987	-0.005	-0.005	0.000	0.000	0.000
28	A	29	ALA	0	-0.002	-0.009	26.290	-0.009	-0.009	0.000	0.000	0.000
29	A	30	LYS	1	0.906	0.961	28.484	0.020	0.020	0.000	0.000	0.000
30	A	31	TRP	0	-0.038	-0.039	20.684	-0.002	-0.002	0.000	0.000	0.000
31	A	32	LEU	0	0.025	0.021	19.653	-0.002	-0.002	0.000	0.000	0.000
32	A	33	PRO	0	-0.028	0.013	21.598	-0.016	-0.016	0.000	0.000	0.000
33	A	34	PRO	0	0.028	0.029	19.258	0.017	0.017	0.000	0.000	0.000
34	A	35	GLU	-1	-0.809	-0.919	22.077	-0.058	-0.058	0.000	0.000	0.000
35	A	36	GLY	0	-0.038	-0.012	23.788	-0.015	-0.015	0.000	0.000	0.000
36	A	37	PHE	0	-0.041	-0.013	21.158	-0.017	-0.017	0.000	0.000	0.000
37	A	38	VAL	0	-0.004	0.015	25.712	0.016	0.016	0.000	0.000	0.000
38	A	39	CYS	0	-0.013	-0.014	25.506	-0.019	-0.019	0.000	0.000	0.000
39	A	40	LYS	1	0.923	0.988	27.379	0.127	0.127	0.000	0.000	0.000
40	A	41	VAL	0	0.041	-0.004	27.794	-0.011	-0.011	0.000	0.000	0.000
41	A	42	LEU	0	-0.108	-0.040	27.638	0.007	0.007	0.000	0.000	0.000
42	A	43	GLU	-1	-0.937	-0.968	28.186	-0.101	-0.101	0.000	0.000	0.000
43	A	44	HIS	0	0.019	-0.010	28.133	-0.007	-0.007	0.000	0.000	0.000
44	A	45	ASP	-1	-0.828	-0.860	29.335	-0.029	-0.029	0.000	0.000	0.000
45	A	46	ALA	0	0.017	0.008	28.443	-0.001	-0.001	0.000	0.000	0.000
46	A	47	ARG	1	0.829	0.865	29.079	0.038	0.038	0.000	0.000	0.000
47	A	48	VAL	0	0.030	0.023	26.047	-0.008	-0.008	0.000	0.000	0.000
48	A	49	GLY	0	0.012	0.011	26.114	0.000	0.000	0.000	0.000	0.000
49	A	50	GLY	0	-0.019	0.000	27.188	-0.012	-0.012	0.000	0.000	0.000
50	A	51	ALA	0	-0.020	-0.018	25.544	-0.003	-0.003	0.000	0.000	0.000
51	A	52	TYR	0	-0.022	-0.028	19.239	0.009	0.009	0.000	0.000	0.000
52	A	53	LYS	1	0.825	0.880	24.098	0.184	0.184	0.000	0.000	0.000
53	A	54	MET	0	0.005	0.010	22.709	0.023	0.023	0.000	0.000	0.000
54	A	55	GLU	-1	-0.860	-0.948	24.197	-0.173	-0.173	0.000	0.000	0.000
55	A	56	PHE	0	0.045	0.013	19.623	0.021	0.021	0.000	0.000	0.000
56	A	57	LEU	0	-0.035	-0.033	24.146	-0.014	-0.014	0.000	0.000	0.000
57	A	58	ALA	0	0.025	0.029	24.124	0.013	0.013	0.000	0.000	0.000
58	A	59	PHE	0	-0.030	-0.028	25.876	0.006	0.006	0.000	0.000	0.000
59	A	60	ALA	0	-0.021	-0.003	28.565	0.005	0.005	0.000	0.000	0.000
60	A	61	SER	0	0.003	-0.006	25.882	0.005	0.005	0.000	0.000	0.000
61	A	62	GLY	0	0.061	0.034	28.304	0.004	0.004	0.000	0.000	0.000
62	A	63	GLN	0	-0.060	-0.022	21.965	-0.009	-0.009	0.000	0.000	0.000
63	A	64	LYS	1	0.897	0.953	25.156	0.168	0.168	0.000	0.000	0.000
64	A	65	HIS	0	0.033	0.014	19.403	-0.033	-0.033	0.000	0.000	0.000
65	A	66	ALA	0	-0.004	0.003	22.357	0.019	0.019	0.000	0.000	0.000
66	A	67	PHE	0	0.029	0.015	18.991	-0.031	-0.031	0.000	0.000	0.000
67	A	68	GLY	0	0.024	0.000	20.150	0.038	0.038	0.000	0.000	0.000
68	A	69	GLY	0	-0.002	0.023	19.785	-0.034	-0.034	0.000	0.000	0.000
69	A	70	ARG	1	0.857	0.909	20.818	0.100	0.100	0.000	0.000	0.000
70	A	71	TYR	0	0.054	0.036	21.361	0.001	0.001	0.000	0.000	0.000
71	A	72	LEU	0	-0.045	-0.038	18.722	0.003	0.003	0.000	0.000	0.000
72	A	73	GLU	-1	-0.835	-0.898	21.222	0.154	0.154	0.000	0.000	0.000
73	A	74	LEU	0	-0.013	-0.011	24.117	-0.006	-0.006	0.000	0.000	0.000
74	A	75	VAL	0	-0.001	0.016	26.289	-0.005	-0.005	0.000	0.000	0.000
75	A	76	PRO	0	0.009	-0.013	27.659	0.007	0.007	0.000	0.000	0.000
76	A	77	GLY	0	0.031	0.011	28.598	0.004	0.004	0.000	0.000	0.000
77	A	78	GLU	-1	-0.969	-0.971	26.246	0.115	0.115	0.000	0.000	0.000
78	A	79	ARG	1	0.822	0.889	19.732	-0.169	-0.169	0.000	0.000	0.000
79	A	80	ILE	0	0.001	0.024	21.530	-0.019	-0.019	0.000	0.000	0.000
80	A	81	ARG	1	0.879	0.935	16.286	-0.171	-0.171	0.000	0.000	0.000
81	A	82	TYR	0	-0.001	0.004	17.858	0.010	0.010	0.000	0.000	0.000
82	A	83	THR	0	0.011	0.020	16.576	0.017	0.017	0.000	0.000	0.000
83	A	84	ASP	-1	-0.883	-0.946	15.313	-0.283	-0.283	0.000	0.000	0.000
84	A	85	ARG	1	0.905	0.953	15.096	0.226	0.226	0.000	0.000	0.000
85	A	86	PHE	0	0.069	0.029	14.550	0.047	0.047	0.000	0.000	0.000
86	A	87	ASP	-1	-0.910	-0.923	18.053	-0.257	-0.257	0.000	0.000	0.000
87	A	88	ASP	-1	-0.934	-0.990	18.189	-0.428	-0.428	0.000	0.000	0.000
88	A	89	ALA	0	-0.041	-0.010	17.033	-0.058	-0.058	0.000	0.000	0.000
89	A	90	GLY	0	0.019	0.015	16.611	-0.034	-0.034	0.000	0.000	0.000
90	A	91	LEU	0	-0.039	0.004	11.074	-0.054	-0.054	0.000	0.000	0.000
91	A	92	PRO	0	-0.013	-0.018	14.502	0.077	0.077	0.000	0.000	0.000
92	A	93	GLY	0	0.012	-0.018	11.769	-0.045	-0.045	0.000	0.000	0.000
93	A	94	ASP	-1	-0.874	-0.921	12.779	-0.260	-0.260	0.000	0.000	0.000
94	A	95	MET	0	-0.020	0.014	10.553	-0.082	-0.082	0.000	0.000	0.000
95	A	96	ILE	0	-0.010	-0.021	12.001	0.085	0.085	0.000	0.000	0.000
96	A	97	THR	0	-0.037	0.001	12.834	0.061	0.061	0.000	0.000	0.000
97	A	98	THR	0	-0.061	-0.047	14.760	-0.001	-0.001	0.000	0.000	0.000
98	A	99	ILE	0	0.043	0.021	16.370	0.039	0.039	0.000	0.000	0.000
99	A	100	THR	0	-0.031	-0.024	19.042	0.006	0.006	0.000	0.000	0.000
100	A	101	LEU	0	-0.033	-0.025	20.954	0.003	0.003	0.000	0.000	0.000
101	A	102	ALA	0	0.051	0.030	24.042	0.000	0.000	0.000	0.000	0.000
102	A	103	PRO	0	0.010	-0.003	26.531	-0.004	-0.004	0.000	0.000	0.000
103	A	104	LEU	0	-0.001	0.008	26.312	0.009	0.009	0.000	0.000	0.000
104	A	105	SER	0	-0.014	-0.012	30.584	-0.009	-0.009	0.000	0.000	0.000
105	A	106	CYS	0	-0.041	-0.025	29.727	-0.004	-0.004	0.000	0.000	0.000
106	A	107	GLY	0	0.018	0.011	30.871	-0.007	-0.007	0.000	0.000	0.000
107	A	108	ALA	0	-0.030	-0.018	26.864	0.002	0.002	0.000	0.000	0.000
108	A	109	ASP	-1	-0.908	-0.944	22.012	0.209	0.209	0.000	0.000	0.000
109	A	110	LEU	0	0.009	-0.002	19.928	-0.005	-0.005	0.000	0.000	0.000
110	A	111	SER	0	0.005	0.008	17.150	0.034	0.034	0.000	0.000	0.000
111	A	112	ILE	0	0.001	0.001	14.234	-0.028	-0.028	0.000	0.000	0.000
112	A	113	VAL	0	-0.013	0.003	10.367	0.084	0.084	0.000	0.000	0.000
113	A	114	GLN	0	0.030	0.020	10.244	-0.079	-0.079	0.000	0.000	0.000
114	A	115	GLU	-1	-0.826	-0.928	8.103	0.965	0.965	0.000	0.000	0.000
115	A	116	GLY	0	0.045	0.011	7.101	-0.088	-0.088	0.000	0.000	0.000
116	A	117	ILE	0	-0.028	-0.006	6.775	-0.007	-0.007	0.000	0.000	0.000
117	A	118	PRO	0	0.025	0.001	6.322	-0.943	-0.943	0.000	0.000	0.000
118	A	119	ASP	-1	-0.831	-0.913	4.597	-5.231	-5.145	-0.001	-0.015	-0.069
119	A	120	ALA	0	-0.057	-0.019	6.329	0.301	0.301	0.000	0.000	0.000
120	A	121	ILE	0	-0.027	-0.010	8.714	0.286	0.286	0.000	0.000	0.000
121	A	122	PRO	0	0.050	0.024	6.880	-0.347	-0.347	0.000	0.000	0.000
122	A	123	PRO	0	0.092	0.026	3.432	0.123	0.396	0.011	-0.058	-0.226
123	A	124	GLU	-1	-0.957	-0.968	6.770	-0.104	-0.104	0.000	0.000	0.000
124	A	125	ASN	0	0.019	-0.007	9.186	0.071	0.071	0.000	0.000	0.000
125	A	126	CYS	0	0.002	0.013	9.608	0.028	0.028	0.000	0.000	0.000
126	A	127	TYR	0	-0.031	-0.014	7.733	0.150	0.150	0.000	0.000	0.000
127	A	128	LEU	0	-0.016	-0.003	12.275	0.042	0.042	0.000	0.000	0.000
128	A	129	GLY	0	0.029	0.019	14.586	0.025	0.025	0.000	0.000	0.000
129	A	130	TRP	0	0.037	-0.008	12.739	0.065	0.065	0.000	0.000	0.000
130	A	131	GLN	0	-0.078	-0.042	14.390	0.017	0.017	0.000	0.000	0.000
131	A	132	GLN	0	-0.021	-0.010	18.106	0.007	0.007	0.000	0.000	0.000
132	A	133	SER	0	0.042	0.015	19.331	0.007	0.007	0.000	0.000	0.000
133	A	134	LEU	0	-0.016	-0.020	17.213	0.014	0.014	0.000	0.000	0.000
134	A	135	LYS	1	0.840	0.932	21.337	0.032	0.032	0.000	0.000	0.000
135	A	136	GLN	0	-0.069	-0.051	23.977	0.003	0.003	0.000	0.000	0.000
136	A	137	LEU	0	-0.022	-0.004	22.763	0.003	0.003	0.000	0.000	0.000
137	A	138	ALA	0	0.002	-0.002	25.398	0.002	0.002	0.000	0.000	0.000
138	A	139	ALA	0	0.019	0.007	27.151	0.001	0.001	0.000	0.000	0.000
139	A	140	LEU	0	-0.065	-0.024	29.043	-0.002	-0.002	0.000	0.000	0.000
140	A	141	VAL	0	-0.015	-0.020	27.536	0.001	0.001	0.000	0.000	0.000
141	A	142	GLU	-1	-0.823	-0.886	29.157	0.061	0.061	0.000	0.000	0.000
142	A	143	PRO	0	-0.033	-0.001	31.962	0.002	0.002	0.000	0.000	0.000
143	A	144	ASP	-1	-0.969	-0.966	35.425	0.018	0.018	0.000	0.000	0.000

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