FMO DATABASE

FMODB ID: 1NMGZ

Calculation Name: 1TZV-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 1TZV

Chain ID: A

ChEMBL ID:

UniProt ID: Q9X286

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	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	141
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-1459578.134007
FMO2-HF: Nuclear repulsion	1401090.880178
FMO2-HF: Total energy	-58487.253829
FMO2-MP2: Total energy	-58660.321797

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:1:MET)

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

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.
-1.132	0.218	0.006	-0.594	-0.763	0.003

Interaction energy analysis for fragmet #1(A:1:MET)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : -0.004 / q_NPA : -0.021

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	3	THR	0	0.024	-0.011	3.788	-1.238	0.112	0.006	-0.594	-0.763	0.003
4	A	4	PRO	0	-0.032	-0.009	5.580	0.478	0.478	0.000	0.000	0.000	0.000
5	A	5	ARG	1	0.938	0.927	8.203	-0.195	-0.195	0.000	0.000	0.000	0.000
6	A	6	ARG	1	0.845	0.882	11.774	-0.125	-0.125	0.000	0.000	0.000	0.000
7	A	7	ARG	1	0.846	0.919	8.168	0.671	0.671	0.000	0.000	0.000	0.000
8	A	8	MET	0	-0.010	0.019	11.318	-0.003	-0.003	0.000	0.000	0.000	0.000
9	A	9	ARG	1	0.821	0.851	12.762	0.044	0.044	0.000	0.000	0.000	0.000
10	A	10	LEU	0	-0.007	-0.008	14.119	0.016	0.016	0.000	0.000	0.000	0.000
11	A	11	ALA	0	-0.036	-0.012	13.999	0.016	0.016	0.000	0.000	0.000	0.000
12	A	12	VAL	0	0.040	0.030	16.071	0.018	0.018	0.000	0.000	0.000	0.000
13	A	13	PHE	0	-0.007	-0.008	19.021	0.016	0.016	0.000	0.000	0.000	0.000
14	A	14	LYS	1	0.894	0.953	14.430	0.210	0.210	0.000	0.000	0.000	0.000
15	A	15	ALA	0	0.052	0.034	20.197	0.011	0.011	0.000	0.000	0.000	0.000
16	A	16	LEU	0	-0.004	-0.003	21.811	0.011	0.011	0.000	0.000	0.000	0.000
17	A	17	PHE	0	-0.048	-0.026	23.607	0.009	0.009	0.000	0.000	0.000	0.000
18	A	18	GLN	0	0.019	-0.016	21.788	0.002	0.002	0.000	0.000	0.000	0.000
19	A	19	HIS	0	0.033	0.027	25.524	0.008	0.008	0.000	0.000	0.000	0.000
20	A	20	GLU	-1	-0.793	-0.866	27.710	-0.027	-0.027	0.000	0.000	0.000	0.000
21	A	21	PHE	0	-0.068	-0.037	28.430	0.006	0.006	0.000	0.000	0.000	0.000
22	A	22	ARG	1	0.704	0.791	24.041	0.069	0.069	0.000	0.000	0.000	0.000
23	A	23	ARG	1	0.852	0.909	30.359	0.028	0.028	0.000	0.000	0.000	0.000
24	A	24	ASP	-1	-0.921	-0.937	32.669	-0.039	-0.039	0.000	0.000	0.000	0.000
25	A	25	GLU	-1	-0.811	-0.865	28.143	-0.059	-0.059	0.000	0.000	0.000	0.000
26	A	26	ASP	-1	-0.819	-0.903	27.568	-0.072	-0.072	0.000	0.000	0.000	0.000
27	A	27	LEU	0	0.042	0.009	24.004	-0.006	-0.006	0.000	0.000	0.000	0.000
28	A	28	GLU	-1	-0.824	-0.905	23.091	-0.103	-0.103	0.000	0.000	0.000	0.000
29	A	29	GLN	0	-0.009	-0.008	22.180	-0.015	-0.015	0.000	0.000	0.000	0.000
30	A	30	ILE	0	0.029	0.027	22.272	-0.008	-0.008	0.000	0.000	0.000	0.000
31	A	31	LEU	0	-0.030	-0.019	17.012	-0.010	-0.010	0.000	0.000	0.000	0.000
32	A	32	GLU	-1	-0.804	-0.876	17.841	-0.228	-0.228	0.000	0.000	0.000	0.000
33	A	33	GLU	-1	-0.843	-0.861	17.853	-0.092	-0.092	0.000	0.000	0.000	0.000
34	A	34	ILE	0	-0.092	-0.042	15.301	-0.006	-0.006	0.000	0.000	0.000	0.000
35	A	35	LEU	0	-0.098	-0.041	12.877	-0.052	-0.052	0.000	0.000	0.000	0.000
36	A	36	ASP	-1	-0.669	-0.790	10.739	-0.349	-0.349	0.000	0.000	0.000	0.000
37	A	37	GLU	-1	-0.897	-0.955	9.219	-0.291	-0.291	0.000	0.000	0.000	0.000
38	A	38	THR	0	-0.085	-0.060	6.510	-0.185	-0.185	0.000	0.000	0.000	0.000
39	A	39	TYR	0	-0.060	-0.025	6.223	-0.470	-0.470	0.000	0.000	0.000	0.000
40	A	40	ASP	-1	-0.761	-0.865	5.635	-1.204	-1.204	0.000	0.000	0.000	0.000
41	A	41	LYS	1	0.932	0.942	7.522	0.509	0.509	0.000	0.000	0.000	0.000
42	A	42	LYS	1	0.867	0.924	10.220	0.255	0.255	0.000	0.000	0.000	0.000
43	A	43	ALA	0	0.025	0.008	9.537	0.097	0.097	0.000	0.000	0.000	0.000
44	A	44	LYS	1	0.843	0.905	10.194	0.613	0.613	0.000	0.000	0.000	0.000
45	A	45	GLU	-1	-0.922	-0.953	13.396	-0.154	-0.154	0.000	0.000	0.000	0.000
46	A	46	ASP	-1	-0.787	-0.878	14.092	-0.127	-0.127	0.000	0.000	0.000	0.000
47	A	47	ALA	0	0.028	0.002	15.038	0.035	0.035	0.000	0.000	0.000	0.000
48	A	48	ARG	1	0.821	0.859	16.476	0.246	0.246	0.000	0.000	0.000	0.000
49	A	49	ARG	1	0.759	0.855	17.631	0.122	0.122	0.000	0.000	0.000	0.000
50	A	50	TYR	0	-0.016	-0.050	18.571	0.013	0.013	0.000	0.000	0.000	0.000
51	A	51	ILE	0	-0.030	-0.001	20.462	0.014	0.014	0.000	0.000	0.000	0.000
52	A	52	ARG	1	0.858	0.914	22.830	0.102	0.102	0.000	0.000	0.000	0.000
53	A	53	GLY	0	0.030	0.025	24.480	0.009	0.009	0.000	0.000	0.000	0.000
54	A	54	ILE	0	-0.005	-0.017	23.594	0.009	0.009	0.000	0.000	0.000	0.000
55	A	55	LYS	1	0.769	0.857	26.926	0.077	0.077	0.000	0.000	0.000	0.000
56	A	56	GLU	-1	-0.952	-0.970	28.841	-0.040	-0.040	0.000	0.000	0.000	0.000
57	A	57	ASN	0	-0.041	-0.020	29.460	0.009	0.009	0.000	0.000	0.000	0.000
58	A	58	LEU	0	0.013	0.020	30.219	0.004	0.004	0.000	0.000	0.000	0.000
59	A	59	SER	0	0.009	-0.004	32.365	0.002	0.002	0.000	0.000	0.000	0.000
60	A	60	MET	0	-0.007	0.009	32.348	0.003	0.003	0.000	0.000	0.000	0.000
61	A	61	ILE	0	0.034	0.013	28.765	0.003	0.003	0.000	0.000	0.000	0.000
62	A	62	ASP	-1	-0.769	-0.872	32.826	-0.026	-0.026	0.000	0.000	0.000	0.000
63	A	63	ASP	-1	-0.870	-0.904	34.741	-0.010	-0.010	0.000	0.000	0.000	0.000
64	A	64	LEU	0	0.010	0.005	33.222	0.002	0.002	0.000	0.000	0.000	0.000
65	A	65	ILE	0	0.002	-0.010	30.700	0.003	0.003	0.000	0.000	0.000	0.000
66	A	66	SER	0	-0.061	-0.055	34.995	0.002	0.002	0.000	0.000	0.000	0.000
67	A	67	ARG	1	0.818	0.918	38.374	0.011	0.011	0.000	0.000	0.000	0.000
68	A	68	TYR	0	-0.090	-0.072	36.458	0.001	0.001	0.000	0.000	0.000	0.000
69	A	69	LEU	0	-0.102	-0.037	35.615	0.001	0.001	0.000	0.000	0.000	0.000
70	A	70	GLU	-1	-0.887	-0.944	39.469	0.001	0.001	0.000	0.000	0.000	0.000
71	A	71	LYS	1	0.993	1.003	41.823	-0.003	-0.003	0.000	0.000	0.000	0.000
72	A	72	TRP	0	-0.042	-0.019	38.282	-0.001	-0.001	0.000	0.000	0.000	0.000
73	A	73	SER	0	0.074	0.021	39.965	0.001	0.001	0.000	0.000	0.000	0.000
74	A	74	LEU	0	0.075	0.028	32.841	0.000	0.000	0.000	0.000	0.000	0.000
75	A	75	ASN	0	0.019	0.011	35.493	0.000	0.000	0.000	0.000	0.000	0.000
76	A	76	ARG	1	0.865	0.932	37.397	0.006	0.006	0.000	0.000	0.000	0.000
77	A	77	LEU	0	-0.023	0.019	33.350	0.001	0.001	0.000	0.000	0.000	0.000
78	A	78	SER	0	-0.007	-0.028	30.919	-0.003	-0.003	0.000	0.000	0.000	0.000
79	A	79	VAL	0	0.045	0.014	28.750	0.000	0.000	0.000	0.000	0.000	0.000
80	A	80	VAL	0	0.032	0.022	25.291	-0.005	-0.005	0.000	0.000	0.000	0.000
81	A	81	ASP	-1	-0.831	-0.900	27.138	-0.011	-0.011	0.000	0.000	0.000	0.000
82	A	82	ARG	1	0.768	0.869	29.356	0.025	0.025	0.000	0.000	0.000	0.000
83	A	83	ASN	0	-0.030	-0.038	25.976	-0.003	-0.003	0.000	0.000	0.000	0.000
84	A	84	VAL	0	0.011	0.021	23.528	-0.005	-0.005	0.000	0.000	0.000	0.000
85	A	85	LEU	0	-0.001	-0.002	25.529	0.001	0.001	0.000	0.000	0.000	0.000
86	A	86	ARG	1	0.794	0.866	27.687	0.035	0.035	0.000	0.000	0.000	0.000
87	A	87	LEU	0	-0.024	-0.008	20.220	-0.002	-0.002	0.000	0.000	0.000	0.000
88	A	88	ALA	0	0.019	0.005	23.933	-0.001	-0.001	0.000	0.000	0.000	0.000
89	A	89	THR	0	0.004	-0.007	24.891	0.006	0.006	0.000	0.000	0.000	0.000
90	A	90	TYR	0	-0.036	-0.031	22.349	0.002	0.002	0.000	0.000	0.000	0.000
91	A	91	GLU	-1	-0.719	-0.796	19.651	-0.025	-0.025	0.000	0.000	0.000	0.000
92	A	92	LEU	0	-0.024	-0.033	23.776	0.006	0.006	0.000	0.000	0.000	0.000
93	A	93	LEU	0	-0.038	-0.022	26.488	0.004	0.004	0.000	0.000	0.000	0.000
94	A	94	PHE	0	0.000	-0.007	25.952	0.002	0.002	0.000	0.000	0.000	0.000
95	A	95	GLU	-1	-0.795	-0.820	20.524	-0.073	-0.073	0.000	0.000	0.000	0.000
96	A	96	LYN	0	-0.045	-0.031	23.313	0.012	0.012	0.000	0.000	0.000	0.000
97	A	97	ASP	-1	-0.893	-0.951	18.976	0.020	0.020	0.000	0.000	0.000	0.000
98	A	98	ILE	0	-0.054	-0.016	17.886	0.018	0.018	0.000	0.000	0.000	0.000
99	A	99	PRO	0	0.020	0.006	20.348	-0.007	-0.007	0.000	0.000	0.000	0.000
100	A	100	ILE	0	0.063	0.014	23.103	-0.003	-0.003	0.000	0.000	0.000	0.000
101	A	101	GLU	-1	-0.913	-0.957	23.887	0.064	0.064	0.000	0.000	0.000	0.000
102	A	102	VAL	0	0.011	0.013	18.223	0.003	0.003	0.000	0.000	0.000	0.000
103	A	103	THR	0	-0.042	-0.037	20.762	-0.005	-0.005	0.000	0.000	0.000	0.000
104	A	104	ILE	0	-0.027	-0.023	22.314	-0.008	-0.008	0.000	0.000	0.000	0.000
105	A	105	ASP	-1	-0.865	-0.930	21.722	0.048	0.048	0.000	0.000	0.000	0.000
106	A	106	GLU	-1	-0.790	-0.869	16.164	0.049	0.049	0.000	0.000	0.000	0.000
107	A	107	ALA	0	0.014	0.018	20.007	-0.011	-0.011	0.000	0.000	0.000	0.000
108	A	108	ILE	0	-0.017	-0.010	22.685	-0.005	-0.005	0.000	0.000	0.000	0.000
109	A	109	GLU	-1	-0.816	-0.863	17.722	0.048	0.048	0.000	0.000	0.000	0.000
110	A	110	ILE	0	-0.057	-0.030	18.597	-0.006	-0.006	0.000	0.000	0.000	0.000
111	A	111	ALA	0	0.011	-0.002	21.464	-0.002	-0.002	0.000	0.000	0.000	0.000
112	A	112	LYS	1	0.804	0.891	23.994	-0.027	-0.027	0.000	0.000	0.000	0.000
113	A	113	ARG	1	0.866	0.957	16.140	0.044	0.044	0.000	0.000	0.000	0.000
114	A	114	TYR	0	-0.023	-0.020	19.206	-0.002	-0.002	0.000	0.000	0.000	0.000
115	A	115	GLY	0	0.047	0.043	25.017	-0.001	-0.001	0.000	0.000	0.000	0.000
116	A	116	THR	0	0.003	-0.002	28.192	0.004	0.004	0.000	0.000	0.000	0.000
117	A	117	GLU	-1	-0.754	-0.884	28.815	0.026	0.026	0.000	0.000	0.000	0.000
118	A	118	ASN	0	-0.018	-0.026	30.182	0.002	0.002	0.000	0.000	0.000	0.000
119	A	119	SER	0	0.030	0.031	29.032	0.000	0.000	0.000	0.000	0.000	0.000
120	A	120	GLY	0	0.046	0.024	27.801	-0.001	-0.001	0.000	0.000	0.000	0.000
121	A	121	LYS	1	0.904	0.951	28.537	-0.020	-0.020	0.000	0.000	0.000	0.000
122	A	122	PHE	0	-0.018	-0.008	31.660	0.000	0.000	0.000	0.000	0.000	0.000
123	A	123	VAL	0	0.029	0.007	26.826	-0.001	-0.001	0.000	0.000	0.000	0.000
124	A	124	ASN	0	0.022	0.011	29.157	-0.001	-0.001	0.000	0.000	0.000	0.000
125	A	125	GLY	0	0.017	0.017	30.008	0.001	0.001	0.000	0.000	0.000	0.000
126	A	126	ILE	0	-0.035	-0.024	32.483	0.000	0.000	0.000	0.000	0.000	0.000
127	A	127	LEU	0	0.034	0.004	26.555	-0.001	-0.001	0.000	0.000	0.000	0.000
128	A	128	ASP	-1	-0.810	-0.879	30.656	0.019	0.019	0.000	0.000	0.000	0.000
129	A	129	ARG	1	0.857	0.924	32.165	-0.003	-0.003	0.000	0.000	0.000	0.000
130	A	130	ILE	0	0.011	0.013	31.702	-0.001	-0.001	0.000	0.000	0.000	0.000
131	A	131	ALA	0	0.011	-0.005	29.871	-0.001	-0.001	0.000	0.000	0.000	0.000
132	A	132	LYS	1	0.802	0.892	31.758	-0.016	-0.016	0.000	0.000	0.000	0.000
133	A	133	GLU	-1	-0.850	-0.889	34.808	0.003	0.003	0.000	0.000	0.000	0.000
134	A	134	HIS	1	0.780	0.877	33.460	0.000	0.000	0.000	0.000	0.000	0.000
135	A	135	ALA	0	0.037	0.040	30.266	-0.002	-0.002	0.000	0.000	0.000	0.000
136	A	136	PRO	0	-0.028	0.001	28.838	0.001	0.001	0.000	0.000	0.000	0.000
137	A	137	LYS	1	1.003	0.995	31.009	0.001	0.001	0.000	0.000	0.000	0.000
138	A	138	GLU	-1	-0.901	-0.954	28.758	0.006	0.006	0.000	0.000	0.000	0.000
139	A	139	LYS	1	0.801	0.898	24.377	0.001	0.001	0.000	0.000	0.000	0.000
140	A	140	PHE	0	-0.060	-0.026	28.603	0.002	0.002	0.000	0.000	0.000	0.000
141	A	141	GLU	-1	-0.989	-0.970	27.891	0.041	0.041	0.000	0.000	0.000	0.000

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