FMO DATABASE

FMODB ID: GNRL1

Calculation Name: 1TX9-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 1TX9

Chain ID: A

ChEMBL ID:

UniProt ID: P69486

Base Structure: X-ray

Registration Date: 2023-03-13

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	-1286074.525643
FMO2-HF: Nuclear repulsion	1231151.413634
FMO2-HF: Total energy	-54923.11201
FMO2-MP2: Total energy	-55084.13042

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:4:VAL)

Summations of interaction energy for fragment #1(A:4:VAL)

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.
-4.094	0.773	2.404	-2.568	-4.703	0

Interaction energy analysis for fragmet #1(A:4:VAL)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : 0.011 / q_NPA : -0.019

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	6	GLU	-1	-0.837	-0.912	3.002	-1.156	1.804	0.139	-0.944	-2.154	0.001
4	A	7	GLN	0	-0.016	-0.028	2.154	-2.855	-1.994	2.211	-1.303	-1.769	-0.001
5	A	8	SER	0	-0.005	0.009	2.987	-0.712	0.191	0.055	-0.304	-0.655	0.000
6	A	9	VAL	0	0.070	0.027	4.560	0.194	0.337	-0.001	-0.017	-0.125	0.000
7	A	10	ARG	1	0.790	0.898	7.088	-0.539	-0.539	0.000	0.000	0.000	0.000
8	A	11	PHE	0	0.024	0.008	7.225	0.007	0.007	0.000	0.000	0.000	0.000
9	A	12	GLN	0	0.014	0.022	8.715	0.008	0.008	0.000	0.000	0.000	0.000
10	A	13	THR	0	0.023	0.014	10.635	0.015	0.015	0.000	0.000	0.000	0.000
11	A	14	ALA	0	0.021	0.020	12.036	0.020	0.020	0.000	0.000	0.000	0.000
12	A	15	LEU	0	-0.020	-0.019	11.711	0.014	0.014	0.000	0.000	0.000	0.000
13	A	16	ALA	0	-0.088	-0.045	14.337	0.018	0.018	0.000	0.000	0.000	0.000
14	A	17	SER	0	-0.032	-0.023	16.379	0.027	0.027	0.000	0.000	0.000	0.000
15	A	18	ILE	0	0.022	0.029	16.827	0.009	0.009	0.000	0.000	0.000	0.000
16	A	19	LYS	1	0.844	0.920	19.338	0.107	0.107	0.000	0.000	0.000	0.000
17	A	20	LEU	0	-0.019	-0.001	21.071	0.007	0.007	0.000	0.000	0.000	0.000
18	A	21	ILE	0	-0.010	-0.017	20.401	0.005	0.005	0.000	0.000	0.000	0.000
19	A	22	GLN	0	0.037	0.014	22.777	-0.005	-0.005	0.000	0.000	0.000	0.000
20	A	23	ALA	0	-0.051	-0.008	25.248	0.003	0.003	0.000	0.000	0.000	0.000
21	A	24	SER	0	-0.060	-0.020	27.290	0.005	0.005	0.000	0.000	0.000	0.000
22	A	25	ALA	0	0.076	0.045	28.582	0.002	0.002	0.000	0.000	0.000	0.000
23	A	26	VAL	0	-0.074	-0.042	30.234	0.002	0.002	0.000	0.000	0.000	0.000
24	A	27	LEU	0	0.014	0.008	28.312	0.003	0.003	0.000	0.000	0.000	0.000
25	A	28	ASP	-1	-0.939	-0.973	32.335	0.004	0.004	0.000	0.000	0.000	0.000
26	A	29	LEU	0	-0.030	-0.025	30.790	0.002	0.002	0.000	0.000	0.000	0.000
27	A	30	THR	0	-0.035	-0.005	35.401	-0.002	-0.002	0.000	0.000	0.000	0.000
28	A	31	GLU	-1	-0.763	-0.884	36.572	-0.021	-0.021	0.000	0.000	0.000	0.000
29	A	32	ASP	-1	-0.839	-0.898	36.454	-0.011	-0.011	0.000	0.000	0.000	0.000
30	A	33	ASP	-1	-0.744	-0.861	34.586	-0.003	-0.003	0.000	0.000	0.000	0.000
31	A	34	PHE	0	-0.010	0.009	29.484	0.000	0.000	0.000	0.000	0.000	0.000
32	A	35	ASP	-1	-0.838	-0.911	31.834	-0.026	-0.026	0.000	0.000	0.000	0.000
33	A	36	PHE	0	-0.110	-0.074	32.163	-0.001	-0.001	0.000	0.000	0.000	0.000
34	A	37	LEU	0	-0.042	-0.027	27.318	0.000	0.000	0.000	0.000	0.000	0.000
35	A	38	THR	0	0.011	-0.002	27.568	-0.002	-0.002	0.000	0.000	0.000	0.000
36	A	39	SER	0	-0.020	0.016	28.839	-0.005	-0.005	0.000	0.000	0.000	0.000
37	A	40	ASN	0	-0.073	-0.042	28.788	0.001	0.001	0.000	0.000	0.000	0.000
38	A	41	LYS	1	0.908	0.967	29.845	0.013	0.013	0.000	0.000	0.000	0.000
39	A	42	VAL	0	0.000	-0.006	29.581	0.001	0.001	0.000	0.000	0.000	0.000
40	A	43	TRP	0	-0.023	-0.005	26.374	0.004	0.004	0.000	0.000	0.000	0.000
41	A	44	ILE	0	-0.044	-0.025	31.113	0.002	0.002	0.000	0.000	0.000	0.000
42	A	45	ALA	0	0.003	-0.013	33.144	0.002	0.002	0.000	0.000	0.000	0.000
43	A	46	THR	0	0.015	0.007	34.158	0.002	0.002	0.000	0.000	0.000	0.000
44	A	47	ASP	-1	-0.834	-0.931	33.392	-0.003	-0.003	0.000	0.000	0.000	0.000
45	A	48	ARG	1	0.963	0.998	29.440	-0.014	-0.014	0.000	0.000	0.000	0.000
46	A	49	SER	0	0.021	0.002	32.189	0.002	0.002	0.000	0.000	0.000	0.000
47	A	50	ARG	1	0.805	0.890	33.958	0.007	0.007	0.000	0.000	0.000	0.000
48	A	51	ALA	0	0.042	0.014	29.182	0.000	0.000	0.000	0.000	0.000	0.000
49	A	52	ARG	1	0.806	0.914	26.939	-0.038	-0.038	0.000	0.000	0.000	0.000
50	A	53	ARG	1	0.854	0.896	29.867	-0.001	-0.001	0.000	0.000	0.000	0.000
51	A	54	CYS	0	-0.023	-0.004	30.367	0.000	0.000	0.000	0.000	0.000	0.000
52	A	55	VAL	0	0.050	0.008	24.287	-0.002	-0.002	0.000	0.000	0.000	0.000
53	A	56	GLU	-1	-0.857	-0.929	26.190	0.035	0.035	0.000	0.000	0.000	0.000
54	A	57	ALA	0	0.010	0.018	28.113	0.002	0.002	0.000	0.000	0.000	0.000
55	A	58	CYS	0	-0.034	-0.010	25.580	-0.003	-0.003	0.000	0.000	0.000	0.000
56	A	59	VAL	0	-0.029	0.002	22.837	-0.001	-0.001	0.000	0.000	0.000	0.000
57	A	60	TYR	0	-0.057	-0.031	25.269	0.005	0.005	0.000	0.000	0.000	0.000
58	A	61	GLY	0	0.090	0.020	27.440	-0.001	-0.001	0.000	0.000	0.000	0.000
59	A	62	THR	0	0.015	0.001	29.165	0.000	0.000	0.000	0.000	0.000	0.000
60	A	63	LEU	0	-0.096	-0.055	28.882	0.001	0.001	0.000	0.000	0.000	0.000
61	A	64	ASP	-1	-0.717	-0.817	32.296	0.022	0.022	0.000	0.000	0.000	0.000
62	A	65	PHE	0	-0.047	-0.004	34.172	-0.002	-0.002	0.000	0.000	0.000	0.000
63	A	66	VAL	0	-0.053	-0.023	36.102	-0.001	-0.001	0.000	0.000	0.000	0.000
64	A	67	GLY	0	0.005	-0.006	37.404	0.001	0.001	0.000	0.000	0.000	0.000
65	A	68	TYR	0	-0.033	-0.027	34.798	0.001	0.001	0.000	0.000	0.000	0.000
66	A	69	PRO	0	0.009	0.017	33.969	0.000	0.000	0.000	0.000	0.000	0.000
67	A	70	ARG	1	0.783	0.858	29.896	-0.028	-0.028	0.000	0.000	0.000	0.000
68	A	71	PHE	0	-0.029	-0.028	25.341	0.003	0.003	0.000	0.000	0.000	0.000
69	A	72	PRO	0	-0.007	-0.006	23.733	-0.004	-0.004	0.000	0.000	0.000	0.000
70	A	73	ALA	0	0.039	0.036	21.932	0.001	0.001	0.000	0.000	0.000	0.000
71	A	74	PRO	0	0.053	0.014	17.233	0.009	0.009	0.000	0.000	0.000	0.000
72	A	75	VAL	0	0.026	0.006	13.798	-0.026	-0.026	0.000	0.000	0.000	0.000
73	A	76	GLU	-1	-0.845	-0.897	12.045	0.148	0.148	0.000	0.000	0.000	0.000
74	A	77	PHE	0	0.033	0.006	14.590	-0.033	-0.033	0.000	0.000	0.000	0.000
75	A	78	ILE	0	0.021	0.020	18.104	-0.013	-0.013	0.000	0.000	0.000	0.000
76	A	79	ALA	0	-0.042	-0.051	14.211	-0.014	-0.014	0.000	0.000	0.000	0.000
77	A	80	ALA	0	-0.010	0.000	16.239	-0.020	-0.020	0.000	0.000	0.000	0.000
78	A	81	VAL	0	0.058	0.026	17.099	-0.011	-0.011	0.000	0.000	0.000	0.000
79	A	82	ILE	0	-0.089	-0.048	18.608	-0.006	-0.006	0.000	0.000	0.000	0.000
80	A	83	ALA	0	-0.034	-0.016	16.096	-0.006	-0.006	0.000	0.000	0.000	0.000
81	A	84	TYR	0	-0.067	-0.023	18.217	-0.014	-0.014	0.000	0.000	0.000	0.000
82	A	85	TYR	0	-0.009	-0.029	21.015	0.000	0.000	0.000	0.000	0.000	0.000
83	A	86	VAL	0	-0.025	-0.003	22.362	0.001	0.001	0.000	0.000	0.000	0.000
84	A	87	HIS	0	0.105	0.064	22.657	-0.008	-0.008	0.000	0.000	0.000	0.000
85	A	88	PRO	0	-0.022	-0.041	20.797	0.005	0.005	0.000	0.000	0.000	0.000
86	A	89	VAL	0	-0.051	-0.015	22.261	0.004	0.004	0.000	0.000	0.000	0.000
87	A	90	ASN	0	0.043	0.019	25.205	0.007	0.007	0.000	0.000	0.000	0.000
88	A	91	ILE	0	0.026	0.016	18.456	0.008	0.008	0.000	0.000	0.000	0.000
89	A	92	GLN	0	0.007	0.013	20.539	0.015	0.015	0.000	0.000	0.000	0.000
90	A	93	THR	0	-0.031	-0.022	21.581	0.011	0.011	0.000	0.000	0.000	0.000
91	A	94	ALA	0	0.061	0.035	22.196	0.008	0.008	0.000	0.000	0.000	0.000
92	A	95	CYS	0	-0.044	0.002	18.686	0.005	0.005	0.000	0.000	0.000	0.000
93	A	96	LEU	0	-0.023	-0.022	20.736	0.012	0.012	0.000	0.000	0.000	0.000
94	A	97	ILE	0	-0.078	-0.040	23.399	0.008	0.008	0.000	0.000	0.000	0.000
95	A	98	MET	0	-0.037	-0.023	21.656	0.004	0.004	0.000	0.000	0.000	0.000
96	A	99	GLU	-1	-0.817	-0.882	20.342	0.097	0.097	0.000	0.000	0.000	0.000
97	A	100	GLY	0	-0.067	-0.040	20.081	-0.005	-0.005	0.000	0.000	0.000	0.000
98	A	101	ALA	0	0.037	0.037	18.808	0.008	0.008	0.000	0.000	0.000	0.000
99	A	102	GLU	-1	-0.798	-0.898	17.033	0.233	0.233	0.000	0.000	0.000	0.000
100	A	103	PHE	0	-0.021	-0.026	11.175	-0.010	-0.010	0.000	0.000	0.000	0.000
101	A	104	THR	0	0.024	-0.031	13.990	-0.003	-0.003	0.000	0.000	0.000	0.000
102	A	105	GLU	-1	-0.806	-0.885	10.472	0.603	0.603	0.000	0.000	0.000	0.000
103	A	106	ASN	0	-0.048	-0.032	14.220	0.018	0.018	0.000	0.000	0.000	0.000
104	A	107	ILE	0	0.009	0.016	16.661	-0.030	-0.030	0.000	0.000	0.000	0.000
105	A	108	ILE	0	-0.064	-0.023	16.865	-0.023	-0.023	0.000	0.000	0.000	0.000
106	A	109	ASN	0	-0.069	-0.049	15.858	-0.012	-0.012	0.000	0.000	0.000	0.000
107	A	110	GLY	0	0.016	0.033	20.105	-0.009	-0.009	0.000	0.000	0.000	0.000
108	A	111	VAL	0	-0.072	-0.034	17.660	0.000	0.000	0.000	0.000	0.000	0.000
109	A	112	GLU	-1	-0.881	-0.952	18.555	0.178	0.178	0.000	0.000	0.000	0.000
110	A	113	ARG	1	0.738	0.855	11.799	-0.402	-0.402	0.000	0.000	0.000	0.000
111	A	114	PRO	0	-0.010	-0.008	16.776	0.007	0.007	0.000	0.000	0.000	0.000
112	A	115	VAL	0	-0.043	-0.013	14.053	0.018	0.018	0.000	0.000	0.000	0.000
113	A	116	LYS	1	0.871	0.917	16.596	-0.136	-0.136	0.000	0.000	0.000	0.000
114	A	117	ALA	0	0.080	0.035	17.285	0.002	0.002	0.000	0.000	0.000	0.000
115	A	118	ALA	0	-0.042	0.001	16.868	-0.010	-0.010	0.000	0.000	0.000	0.000
116	A	119	GLU	-1	-0.777	-0.864	11.193	0.348	0.348	0.000	0.000	0.000	0.000
117	A	120	LEU	0	0.034	0.013	13.294	-0.022	-0.022	0.000	0.000	0.000	0.000
118	A	121	PHE	0	0.004	-0.025	14.495	-0.028	-0.028	0.000	0.000	0.000	0.000
119	A	122	ALA	0	-0.015	-0.008	11.576	-0.027	-0.027	0.000	0.000	0.000	0.000
120	A	123	PHE	0	-0.040	-0.026	8.068	-0.035	-0.035	0.000	0.000	0.000	0.000
121	A	124	THR	0	0.061	0.021	11.021	-0.052	-0.052	0.000	0.000	0.000	0.000
122	A	125	LEU	0	0.005	0.011	13.466	-0.021	-0.021	0.000	0.000	0.000	0.000
123	A	126	ARG	1	0.865	0.923	5.903	0.209	0.209	0.000	0.000	0.000	0.000
124	A	127	VAL	0	-0.002	-0.006	10.588	-0.045	-0.045	0.000	0.000	0.000	0.000
125	A	128	ARG	1	0.936	0.972	11.933	0.082	0.082	0.000	0.000	0.000	0.000
126	A	129	ALA	0	-0.088	-0.041	11.703	-0.005	-0.005	0.000	0.000	0.000	0.000
127	A	130	GLY	0	-0.036	-0.008	11.701	-0.014	-0.014	0.000	0.000	0.000	0.000
128	A	131	ASN	0	0.014	-0.027	12.728	0.001	0.001	0.000	0.000	0.000	0.000
129	A	132	THR	0	0.055	0.040	15.638	0.011	0.011	0.000	0.000	0.000	0.000
130	A	133	ASP	-1	-0.963	-0.944	18.777	-0.130	-0.130	0.000	0.000	0.000	0.000
131	A	134	VAL	0	-0.085	-0.058	17.873	0.011	0.011	0.000	0.000	0.000	0.000
132	A	135	LEU	0	0.046	0.001	20.538	-0.007	-0.007	0.000	0.000	0.000	0.000
133	A	136	THR	0	-0.018	0.006	23.091	0.002	0.002	0.000	0.000	0.000	0.000
134	A	137	ASP	-1	-0.914	-0.953	26.386	-0.068	-0.068	0.000	0.000	0.000	0.000
135	A	138	ALA	0	0.020	-0.006	29.846	0.003	0.003	0.000	0.000	0.000	0.000
136	A	139	GLU	-1	-0.975	-0.965	32.555	-0.027	-0.027	0.000	0.000	0.000	0.000
137	A	140	GLU	-1	-0.820	-0.911	28.438	-0.035	-0.035	0.000	0.000	0.000	0.000
138	A	141	ASN	0	-0.053	-0.015	32.655	0.002	0.002	0.000	0.000	0.000	0.000
139	A	142	VAL	0	-0.005	-0.016	35.250	0.001	0.001	0.000	0.000	0.000	0.000
140	A	143	ARG	1	0.840	0.919	34.488	0.013	0.013	0.000	0.000	0.000	0.000
141	A	144	GLN	0	0.007	0.019	37.275	0.000	0.000	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:4:VAL)