FMO DATABASE

FMODB ID: QVG8Y

Calculation Name: 1WHI-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 1WHI

Chain ID: A

ChEMBL ID:

UniProt ID: P04450

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	OptH
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	122
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-991269.688197
FMO2-HF: Nuclear repulsion	944890.265315
FMO2-HF: Total energy	-46379.422882
FMO2-MP2: Total energy	-46515.780745

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.
-5.997	-1.157	10.021	-4.159	-10.701	8.673617379884E-19

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 : 0.008 / q_NPA : -0.013

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

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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	GLN	0	0.016	-0.004	2.936	0.490	3.338	0.069	-1.150	-1.767	0.002
4	A	4	GLN	0	0.010	0.000	5.495	0.385	0.385	0.000	0.000	0.000	0.000
5	A	5	GLU	-1	-0.898	-0.969	8.515	-1.257	-1.257	0.000	0.000	0.000	0.000
6	A	6	SER	0	-0.027	0.004	5.487	-0.635	-0.635	0.000	0.000	0.000	0.000
7	A	7	ARG	1	0.947	0.970	7.733	0.897	0.897	0.000	0.000	0.000	0.000
8	A	8	LEU	0	-0.047	-0.024	7.833	-0.040	-0.040	0.000	0.000	0.000	0.000
9	A	9	LYS	1	1.022	1.013	11.241	0.164	0.164	0.000	0.000	0.000	0.000
10	A	10	VAL	0	-0.003	-0.004	13.866	-0.037	-0.037	0.000	0.000	0.000	0.000
11	A	11	ALA	0	-0.028	0.000	16.127	0.039	0.039	0.000	0.000	0.000	0.000
12	A	12	ASP	-1	-0.744	-0.858	17.860	-0.179	-0.179	0.000	0.000	0.000	0.000
13	A	13	ASN	0	0.025	0.008	21.174	-0.011	-0.011	0.000	0.000	0.000	0.000
14	A	14	SER	0	-0.041	-0.049	21.567	-0.002	-0.002	0.000	0.000	0.000	0.000
15	A	15	GLY	0	0.044	0.024	23.667	0.001	0.001	0.000	0.000	0.000	0.000
16	A	16	ALA	0	-0.057	-0.025	19.720	-0.003	-0.003	0.000	0.000	0.000	0.000
17	A	17	ARG	1	0.872	0.932	19.859	0.170	0.170	0.000	0.000	0.000	0.000
18	A	18	GLU	-1	-0.919	-0.969	14.219	-0.358	-0.358	0.000	0.000	0.000	0.000
19	A	19	VAL	0	-0.020	-0.001	13.222	0.023	0.023	0.000	0.000	0.000	0.000
20	A	20	LEU	0	0.009	0.009	11.555	-0.073	-0.073	0.000	0.000	0.000	0.000
21	A	21	VAL	0	-0.010	-0.012	8.542	0.134	0.134	0.000	0.000	0.000	0.000
22	A	22	ILE	0	0.016	0.029	11.457	-0.047	-0.047	0.000	0.000	0.000	0.000
23	A	23	LYS	1	0.975	0.973	11.107	0.538	0.538	0.000	0.000	0.000	0.000
24	A	24	VAL	0	0.000	0.012	6.793	0.029	0.029	0.000	0.000	0.000	0.000
25	A	25	LEU	0	-0.049	-0.026	10.271	0.108	0.108	0.000	0.000	0.000	0.000
26	A	26	GLY	0	0.037	-0.003	11.887	-0.047	-0.047	0.000	0.000	0.000	0.000
27	A	27	GLY	0	0.021	0.022	13.690	0.040	0.040	0.000	0.000	0.000	0.000
28	A	28	SER	0	-0.001	-0.006	13.148	-0.100	-0.100	0.000	0.000	0.000	0.000
29	A	29	GLY	0	0.069	0.035	11.655	0.040	0.040	0.000	0.000	0.000	0.000
30	A	30	ARG	1	0.774	0.902	6.317	0.883	0.883	0.000	0.000	0.000	0.000
31	A	31	ARG	1	0.972	0.981	6.356	0.862	0.862	0.000	0.000	0.000	0.000
32	A	32	TYR	0	-0.022	-0.017	2.328	-3.081	-0.090	2.893	-1.398	-4.485	-0.009
33	A	33	ALA	0	-0.015	0.004	4.102	0.401	0.633	-0.001	-0.016	-0.215	0.000
34	A	34	ASN	0	-0.024	-0.018	4.714	-0.253	-0.121	-0.001	-0.009	-0.122	0.000
35	A	35	ILE	0	0.026	-0.010	6.770	-0.109	-0.109	0.000	0.000	0.000	0.000
36	A	36	GLY	0	-0.034	-0.008	10.307	0.009	0.009	0.000	0.000	0.000	0.000
37	A	37	ASP	-1	-0.801	-0.883	7.672	-0.842	-0.842	0.000	0.000	0.000	0.000
38	A	38	VAL	0	-0.002	-0.008	11.018	0.025	0.025	0.000	0.000	0.000	0.000
39	A	39	VAL	0	-0.022	-0.009	9.217	-0.109	-0.109	0.000	0.000	0.000	0.000
40	A	40	VAL	0	0.003	0.003	12.277	0.133	0.133	0.000	0.000	0.000	0.000
41	A	41	ALA	0	0.016	-0.003	13.599	-0.127	-0.127	0.000	0.000	0.000	0.000
42	A	42	THR	0	0.036	0.027	15.290	0.094	0.094	0.000	0.000	0.000	0.000
43	A	43	VAL	0	0.005	-0.003	16.950	-0.043	-0.043	0.000	0.000	0.000	0.000
44	A	44	LYS	1	0.926	0.971	15.191	0.392	0.392	0.000	0.000	0.000	0.000
45	A	45	ASP	-1	-0.862	-0.942	18.586	-0.159	-0.159	0.000	0.000	0.000	0.000
46	A	46	ALA	0	0.020	-0.003	20.780	-0.015	-0.015	0.000	0.000	0.000	0.000
47	A	47	THR	0	-0.018	0.001	23.551	0.012	0.012	0.000	0.000	0.000	0.000
48	A	48	PRO	0	-0.013	-0.017	26.818	-0.008	-0.008	0.000	0.000	0.000	0.000
49	A	49	GLY	0	0.007	-0.007	29.688	0.007	0.007	0.000	0.000	0.000	0.000
50	A	50	GLY	0	0.022	0.034	28.978	0.007	0.007	0.000	0.000	0.000	0.000
51	A	51	VAL	0	0.000	-0.005	27.180	-0.006	-0.006	0.000	0.000	0.000	0.000
52	A	52	VAL	0	-0.039	-0.003	22.482	-0.012	-0.012	0.000	0.000	0.000	0.000
53	A	53	LYS	1	0.987	0.984	25.625	0.167	0.167	0.000	0.000	0.000	0.000
54	A	54	LYS	1	0.929	0.962	22.690	0.179	0.179	0.000	0.000	0.000	0.000
55	A	55	GLY	0	0.016	0.009	21.863	0.018	0.018	0.000	0.000	0.000	0.000
56	A	56	GLN	0	0.025	0.018	22.916	-0.016	-0.016	0.000	0.000	0.000	0.000
57	A	57	VAL	0	0.017	0.009	18.699	-0.035	-0.035	0.000	0.000	0.000	0.000
58	A	58	VAL	0	-0.037	-0.012	17.702	0.045	0.045	0.000	0.000	0.000	0.000
59	A	59	LYS	1	0.986	0.993	16.822	0.298	0.298	0.000	0.000	0.000	0.000
60	A	60	ALA	0	0.015	-0.002	14.488	0.054	0.054	0.000	0.000	0.000	0.000
61	A	61	VAL	0	0.004	0.021	13.829	-0.092	-0.092	0.000	0.000	0.000	0.000
62	A	62	VAL	0	-0.002	-0.005	8.030	0.039	0.039	0.000	0.000	0.000	0.000
63	A	63	VAL	0	0.008	-0.009	11.400	0.070	0.070	0.000	0.000	0.000	0.000
64	A	64	ARG	1	0.783	0.893	11.112	-0.008	-0.008	0.000	0.000	0.000	0.000
65	A	65	THR	0	0.006	-0.004	5.615	-0.027	-0.027	0.000	0.000	0.000	0.000
66	A	66	LYS	1	0.983	0.992	5.982	-0.997	-0.997	0.000	0.000	0.000	0.000
67	A	67	ARG	1	0.888	0.949	1.837	-3.632	-4.995	7.061	-1.586	-4.112	0.007
68	A	68	GLY	0	0.045	0.017	5.601	-0.218	-0.218	0.000	0.000	0.000	0.000
69	A	69	VAL	0	-0.039	-0.006	7.369	0.102	0.102	0.000	0.000	0.000	0.000
70	A	70	ARG	1	0.956	0.978	9.744	-0.467	-0.467	0.000	0.000	0.000	0.000
71	A	71	ARG	1	0.802	0.870	11.573	-0.364	-0.364	0.000	0.000	0.000	0.000
72	A	72	PRO	0	0.007	-0.014	14.860	0.021	0.021	0.000	0.000	0.000	0.000
73	A	73	ASP	-1	-0.823	-0.887	17.476	0.266	0.266	0.000	0.000	0.000	0.000
74	A	74	GLY	0	-0.020	0.001	17.489	-0.002	-0.002	0.000	0.000	0.000	0.000
75	A	75	SER	0	-0.056	-0.027	17.276	0.050	0.050	0.000	0.000	0.000	0.000
76	A	76	TYR	0	0.032	-0.002	11.284	0.047	0.047	0.000	0.000	0.000	0.000
77	A	77	ILE	0	-0.002	0.012	12.982	-0.028	-0.028	0.000	0.000	0.000	0.000
78	A	78	ARG	1	0.936	0.966	9.671	-1.090	-1.090	0.000	0.000	0.000	0.000
79	A	79	PHE	0	0.012	-0.002	10.195	-0.149	-0.149	0.000	0.000	0.000	0.000
80	A	80	ASP	-1	-0.881	-0.939	10.567	0.621	0.621	0.000	0.000	0.000	0.000
81	A	81	GLU	-1	-0.861	-0.932	10.398	0.070	0.070	0.000	0.000	0.000	0.000
82	A	82	ASN	0	-0.010	-0.014	5.234	0.419	0.419	0.000	0.000	0.000	0.000
83	A	83	ALA	0	-0.005	0.006	8.716	-0.133	-0.133	0.000	0.000	0.000	0.000
84	A	84	CYS	0	-0.053	-0.023	11.422	-0.048	-0.048	0.000	0.000	0.000	0.000
85	A	85	VAL	0	0.047	0.034	13.528	0.053	0.053	0.000	0.000	0.000	0.000
86	A	86	ILE	0	0.011	-0.002	17.162	-0.045	-0.045	0.000	0.000	0.000	0.000
87	A	87	ILE	0	-0.056	-0.026	17.867	0.037	0.037	0.000	0.000	0.000	0.000
88	A	88	ARG	1	0.934	0.962	20.855	0.120	0.120	0.000	0.000	0.000	0.000
89	A	89	ASP	-1	-0.896	-0.963	22.236	-0.266	-0.266	0.000	0.000	0.000	0.000
90	A	90	ASP	-1	-0.869	-0.934	23.254	-0.158	-0.158	0.000	0.000	0.000	0.000
91	A	91	LYS	1	0.885	0.947	18.175	0.219	0.219	0.000	0.000	0.000	0.000
92	A	92	SER	0	-0.035	0.004	21.913	0.012	0.012	0.000	0.000	0.000	0.000
93	A	93	PRO	0	-0.021	-0.013	22.041	-0.021	-0.021	0.000	0.000	0.000	0.000
94	A	94	ARG	1	0.926	0.959	22.895	0.228	0.228	0.000	0.000	0.000	0.000
95	A	95	GLY	0	0.016	0.026	23.787	0.009	0.009	0.000	0.000	0.000	0.000
96	A	96	THR	0	-0.011	-0.017	25.311	0.005	0.005	0.000	0.000	0.000	0.000
97	A	97	ARG	1	0.895	0.945	25.546	0.052	0.052	0.000	0.000	0.000	0.000
98	A	98	ILE	0	0.038	0.025	19.609	-0.021	-0.021	0.000	0.000	0.000	0.000
99	A	99	PHE	0	0.007	-0.002	20.365	0.017	0.017	0.000	0.000	0.000	0.000
100	A	100	GLY	0	0.059	0.023	18.793	-0.003	-0.003	0.000	0.000	0.000	0.000
101	A	101	PRO	0	0.035	0.025	17.053	-0.021	-0.021	0.000	0.000	0.000	0.000
102	A	102	VAL	0	0.008	0.013	15.990	0.000	0.000	0.000	0.000	0.000	0.000
103	A	103	ALA	0	0.033	0.012	14.033	0.025	0.025	0.000	0.000	0.000	0.000
104	A	104	ARG	1	0.987	0.977	15.959	-0.172	-0.172	0.000	0.000	0.000	0.000
105	A	105	GLU	-1	-0.728	-0.853	12.959	0.211	0.211	0.000	0.000	0.000	0.000
106	A	106	LEU	0	-0.034	-0.017	14.497	-0.048	-0.048	0.000	0.000	0.000	0.000
107	A	107	ARG	1	0.943	0.966	16.955	-0.017	-0.017	0.000	0.000	0.000	0.000
108	A	108	ASP	-1	-0.890	-0.938	16.887	0.011	0.011	0.000	0.000	0.000	0.000
109	A	109	LYS	1	0.836	0.924	12.746	0.132	0.132	0.000	0.000	0.000	0.000
110	A	110	ASP	-1	-0.868	-0.946	17.739	-0.131	-0.131	0.000	0.000	0.000	0.000
111	A	111	PHE	0	0.001	0.013	15.922	-0.017	-0.017	0.000	0.000	0.000	0.000
112	A	112	MET	0	0.031	-0.001	20.760	0.019	0.019	0.000	0.000	0.000	0.000
113	A	113	LYS	1	0.992	1.006	24.112	0.073	0.073	0.000	0.000	0.000	0.000
114	A	114	ILE	0	0.040	0.011	18.631	0.009	0.009	0.000	0.000	0.000	0.000
115	A	115	ILE	0	-0.014	-0.002	19.779	0.016	0.016	0.000	0.000	0.000	0.000
116	A	116	SER	0	-0.086	-0.047	22.576	0.012	0.012	0.000	0.000	0.000	0.000
117	A	117	LEU	0	-0.033	-0.027	24.165	0.004	0.004	0.000	0.000	0.000	0.000
118	A	118	ALA	0	-0.051	-0.012	21.188	0.002	0.002	0.000	0.000	0.000	0.000
119	A	119	PRO	0	-0.024	-0.001	21.725	0.006	0.006	0.000	0.000	0.000	0.000
120	A	120	GLU	-1	-0.892	-0.945	22.329	0.144	0.144	0.000	0.000	0.000	0.000
121	A	121	VAL	0	-0.034	-0.008	20.047	-0.002	-0.002	0.000	0.000	0.000	0.000
122	A	122	ILE	0	0.020	0.014	17.753	0.019	0.019	0.000	0.000	0.000	0.000

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