FMO DATABASE

FMODB ID: M2M2Z

Calculation Name: 2QJ2-A-Xray549

Preferred Name: Hepatocyte growth factor

Target Type: SINGLE PROTEIN

Ligand Name: sulfate ion

Ligand 3-letter code: SO4

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 2QJ2

Chain ID: A

ChEMBL ID: CHEMBL5479

UniProt ID: P14210

Base Structure: X-ray

Registration Date: 2025-10-12

Reference: Sci Data 11, 1164 (2024).

DOI: https://doi.org/10.1038/s41597-024-03999-2

Apendix: None

IFIE MAP

IFIE Diagram

Modeling method

Optimization	MOE:Amber10:EHT
Restraint	OptH
Protonation	MOE:Protonate 3D
Complement	ac.sh, 23 2024 Oct
Water	No
Procedure	Manual calculation
Remarks

FMO calculation

FMO method	FMO2-MP2/6-31G(d)
Fragmentation	Auto
Number of fragment	169
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230922

Total energy (hartree)

FMO2-HF: Electronic energy	-1826897.67632
FMO2-HF: Nuclear repulsion	1755072.648994
FMO2-HF: Total energy	-71825.027326
FMO2-MP2: Total energy	-72028.461302

3D Structure Molmil

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:36:ARG)

Summations of interaction energy for fragment #1(A:36:ARG)

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.
147.748	146.534	33.25	-16.809	-15.226	-0.185

Interaction energy analysis for fragmet #1(A:36:ARG)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 2 / q_Mulliken : 1.688 / q_NPA : 1.805

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	38	THR	0	0.033	0.000	2.589	-9.697	-5.700	3.315	-2.671	-4.640	-0.014
4	A	39	ILE	0	0.012	0.009	4.310	4.771	5.014	0.000	-0.045	-0.198	0.000
6	A	41	GLU	-1	-0.770	-0.839	1.746	-188.776	-195.715	29.744	-13.612	-9.194	-0.171
37	A	72	ASN	0	-0.004	-0.009	4.787	-11.730	-11.706	-0.001	-0.021	-0.001	0.000
40	A	75	THR	0	0.031	-0.002	2.961	4.596	5.181	0.160	-0.194	-0.551	0.001
41	A	76	ARG	1	0.901	0.957	2.877	96.187	97.063	0.032	-0.266	-0.642	-0.001
5	A	40	HIS	0	0.005	-0.002	7.117	5.397	5.397	0.000	0.000	0.000	0.000
7	A	42	PHE	0	-0.032	-0.030	6.024	5.905	5.905	0.000	0.000	0.000	0.000
8	A	43	LYS	1	0.820	0.906	8.898	32.312	32.312	0.000	0.000	0.000	0.000
9	A	44	LYS	1	0.866	0.939	12.590	36.608	36.608	0.000	0.000	0.000	0.000
10	A	45	SER	0	0.027	0.020	14.652	2.088	2.088	0.000	0.000	0.000	0.000
11	A	46	ALA	0	0.051	0.014	18.309	-0.439	-0.439	0.000	0.000	0.000	0.000
12	A	47	LYS	1	0.934	0.990	20.138	23.959	23.959	0.000	0.000	0.000	0.000
13	A	48	THR	0	-0.026	-0.015	20.466	1.362	1.362	0.000	0.000	0.000	0.000
14	A	49	THR	0	0.008	-0.004	20.782	-1.797	-1.797	0.000	0.000	0.000	0.000
15	A	50	LEU	0	-0.053	-0.028	18.705	0.398	0.398	0.000	0.000	0.000	0.000
16	A	51	ILE	0	0.013	0.020	22.469	-0.328	-0.328	0.000	0.000	0.000	0.000
17	A	52	LYS	1	0.795	0.884	25.024	22.243	22.243	0.000	0.000	0.000	0.000
18	A	53	ILE	0	-0.013	-0.012	26.487	0.508	0.508	0.000	0.000	0.000	0.000
19	A	54	ASP	-1	-0.815	-0.903	27.917	-20.050	-20.050	0.000	0.000	0.000	0.000
20	A	55	PRO	0	0.016	-0.008	28.487	-0.838	-0.838	0.000	0.000	0.000	0.000
21	A	56	ALA	0	0.037	0.031	28.532	-0.451	-0.451	0.000	0.000	0.000	0.000
22	A	57	LEU	0	-0.046	0.000	23.214	-0.963	-0.963	0.000	0.000	0.000	0.000
23	A	58	LYS	1	0.967	0.987	21.376	25.941	25.941	0.000	0.000	0.000	0.000
24	A	59	ILE	0	0.023	0.006	20.528	-0.827	-0.827	0.000	0.000	0.000	0.000
25	A	60	LYS	1	0.895	0.970	18.228	32.406	32.406	0.000	0.000	0.000	0.000
26	A	61	THR	0	0.028	0.017	19.365	-1.173	-1.173	0.000	0.000	0.000	0.000
27	A	62	LYS	1	0.948	0.966	16.269	32.626	32.626	0.000	0.000	0.000	0.000
28	A	63	LYS	1	0.978	1.015	18.654	24.546	24.546	0.000	0.000	0.000	0.000
29	A	64	VAL	0	-0.046	-0.034	14.265	-1.035	-1.035	0.000	0.000	0.000	0.000
30	A	65	ASN	0	0.047	0.026	14.495	2.661	2.661	0.000	0.000	0.000	0.000
31	A	66	THR	0	0.004	-0.008	12.112	0.237	0.237	0.000	0.000	0.000	0.000
32	A	67	ALA	0	0.081	0.034	13.038	-1.015	-1.015	0.000	0.000	0.000	0.000
33	A	68	ASP	-1	-0.847	-0.927	8.069	-62.294	-62.294	0.000	0.000	0.000	0.000
34	A	69	GLN	0	0.016	0.004	8.260	-4.147	-4.147	0.000	0.000	0.000	0.000
35	A	70	CYS	0	-0.060	0.010	10.261	-0.477	-0.477	0.000	0.000	0.000	0.000
36	A	71	ALA	0	0.060	0.045	7.477	0.220	0.220	0.000	0.000	0.000	0.000
38	A	73	ARG	1	0.862	0.948	6.909	39.543	39.543	0.000	0.000	0.000	0.000
39	A	74	CYS	0	-0.104	-0.041	9.218	5.344	5.344	0.000	0.000	0.000	0.000
42	A	77	ASN	0	0.052	0.036	7.839	3.566	3.566	0.000	0.000	0.000	0.000
43	A	78	LYS	0	0.079	0.046	9.159	1.798	1.798	0.000	0.000	0.000	0.000
44	A	79	GLY	0	0.037	0.015	12.438	1.545	1.545	0.000	0.000	0.000	0.000
45	A	80	LEU	0	-0.074	-0.035	12.716	2.098	2.098	0.000	0.000	0.000	0.000
46	A	81	PRO	0	0.011	0.015	16.259	-0.469	-0.469	0.000	0.000	0.000	0.000
47	A	82	PHE	0	-0.029	-0.037	15.692	2.010	2.010	0.000	0.000	0.000	0.000
48	A	83	THR	0	0.016	0.021	11.747	-1.979	-1.979	0.000	0.000	0.000	0.000
49	A	85	LYS	1	0.917	0.976	11.236	29.544	29.544	0.000	0.000	0.000	0.000
50	A	86	ALA	0	0.021	0.016	12.874	-0.621	-0.621	0.000	0.000	0.000	0.000
51	A	87	PHE	0	-0.025	-0.008	9.691	0.631	0.631	0.000	0.000	0.000	0.000
52	A	88	VAL	0	0.020	0.020	14.509	0.091	0.091	0.000	0.000	0.000	0.000
53	A	89	PHE	0	-0.020	-0.024	15.381	-0.962	-0.962	0.000	0.000	0.000	0.000
54	A	90	ASP	-1	-0.765	-0.859	17.436	-24.968	-24.968	0.000	0.000	0.000	0.000
55	A	91	LYS	1	0.843	0.906	19.102	28.468	28.468	0.000	0.000	0.000	0.000
56	A	92	ALA	0	0.006	0.015	21.153	0.298	0.298	0.000	0.000	0.000	0.000
57	A	93	ARG	1	0.788	0.854	24.167	24.096	24.096	0.000	0.000	0.000	0.000
58	A	94	LYS	1	0.877	0.949	18.407	30.927	30.927	0.000	0.000	0.000	0.000
59	A	95	GLN	0	0.011	-0.002	19.614	-0.436	-0.436	0.000	0.000	0.000	0.000
60	A	97	LEU	0	0.015	-0.003	17.447	1.751	1.751	0.000	0.000	0.000	0.000
61	A	98	TRP	0	-0.045	-0.041	12.530	-0.097	-0.097	0.000	0.000	0.000	0.000
62	A	99	PHE	0	0.072	0.018	15.720	1.951	1.951	0.000	0.000	0.000	0.000
63	A	100	PRO	0	0.012	0.022	15.508	-2.255	-2.255	0.000	0.000	0.000	0.000
64	A	101	PHE	0	0.008	-0.007	17.227	0.472	0.472	0.000	0.000	0.000	0.000
65	A	102	ASN	0	0.017	-0.009	15.814	-0.242	-0.242	0.000	0.000	0.000	0.000
66	A	103	SER	0	-0.042	-0.061	17.988	1.852	1.852	0.000	0.000	0.000	0.000
67	A	104	MET	0	-0.072	-0.027	17.806	1.063	1.063	0.000	0.000	0.000	0.000
68	A	105	SER	0	-0.015	0.004	20.290	0.336	0.336	0.000	0.000	0.000	0.000
69	A	106	SER	0	0.056	0.023	22.742	0.464	0.464	0.000	0.000	0.000	0.000
70	A	107	GLY	0	0.055	0.024	25.700	-0.365	-0.365	0.000	0.000	0.000	0.000
71	A	108	VAL	0	-0.019	-0.005	22.127	-0.088	-0.088	0.000	0.000	0.000	0.000
72	A	109	LYS	1	0.864	0.920	25.488	20.861	20.861	0.000	0.000	0.000	0.000
73	A	110	LYS	1	0.932	0.972	20.679	26.382	26.382	0.000	0.000	0.000	0.000
74	A	111	GLU	-1	-0.858	-0.916	24.482	-19.398	-19.398	0.000	0.000	0.000	0.000
75	A	112	PHE	0	0.028	0.012	24.825	-1.124	-1.124	0.000	0.000	0.000	0.000
76	A	113	GLY	0	0.074	0.009	25.551	0.660	0.660	0.000	0.000	0.000	0.000
77	A	114	HIS	0	-0.024	0.001	24.638	-1.359	-1.359	0.000	0.000	0.000	0.000
78	A	115	GLU	-1	-0.788	-0.893	24.488	-23.762	-23.762	0.000	0.000	0.000	0.000
79	A	116	PHE	0	-0.038	-0.021	21.357	-1.438	-1.438	0.000	0.000	0.000	0.000
80	A	117	ASP	-1	-0.825	-0.900	17.096	-31.638	-31.638	0.000	0.000	0.000	0.000
81	A	118	LEU	0	0.017	0.005	16.309	-1.119	-1.119	0.000	0.000	0.000	0.000
82	A	119	TYR	0	0.008	-0.006	11.286	-0.277	-0.277	0.000	0.000	0.000	0.000
83	A	120	GLU	-1	-0.780	-0.886	12.730	-32.449	-32.449	0.000	0.000	0.000	0.000
84	A	121	ASN	0	0.000	-0.006	8.088	-2.922	-2.922	0.000	0.000	0.000	0.000
85	A	122	LYS	1	0.920	0.948	8.893	52.253	52.253	0.000	0.000	0.000	0.000
86	A	123	ASP	-1	-0.840	-0.899	8.029	-52.493	-52.493	0.000	0.000	0.000	0.000
87	A	124	TYR	0	-0.022	-0.030	11.011	4.285	4.285	0.000	0.000	0.000	0.000
88	A	125	ILE	0	-0.097	-0.048	13.670	2.520	2.520	0.000	0.000	0.000	0.000
89	A	126	ARG	1	0.860	0.925	15.132	24.158	24.158	0.000	0.000	0.000	0.000
90	A	127	ASN	0	0.011	-0.004	14.245	2.044	2.044	0.000	0.000	0.000	0.000
91	A	128	CYS	0	-0.062	-0.028	17.141	-0.456	-0.456	0.000	0.000	0.000	0.000
92	A	129	ILE	0	-0.050	-0.027	20.688	0.223	0.223	0.000	0.000	0.000	0.000
93	A	130	ILE	0	0.042	0.027	24.399	-0.023	-0.023	0.000	0.000	0.000	0.000
94	A	131	GLY	0	0.068	0.048	27.488	0.594	0.594	0.000	0.000	0.000	0.000
95	A	132	LYS	1	0.949	0.972	29.099	15.889	15.889	0.000	0.000	0.000	0.000
96	A	133	GLY	0	0.035	0.006	26.329	-0.196	-0.196	0.000	0.000	0.000	0.000
97	A	134	ARG	1	0.924	0.979	26.526	16.947	16.947	0.000	0.000	0.000	0.000
98	A	135	SER	0	-0.013	-0.016	26.303	-0.095	-0.095	0.000	0.000	0.000	0.000
99	A	136	TYR	0	0.029	0.024	18.296	-0.739	-0.739	0.000	0.000	0.000	0.000
100	A	137	LYS	1	0.932	0.963	19.744	24.413	24.413	0.000	0.000	0.000	0.000
101	A	138	GLY	0	0.088	0.059	16.479	-1.316	-1.316	0.000	0.000	0.000	0.000
102	A	139	THR	0	-0.012	-0.021	13.368	-0.186	-0.186	0.000	0.000	0.000	0.000
103	A	140	VAL	0	0.033	0.038	15.814	-0.941	-0.941	0.000	0.000	0.000	0.000
104	A	141	SER	0	0.026	0.005	17.602	1.036	1.036	0.000	0.000	0.000	0.000
105	A	142	ILE	0	-0.015	0.003	18.701	0.227	0.227	0.000	0.000	0.000	0.000
106	A	143	THR	0	0.009	-0.035	21.460	-0.365	-0.365	0.000	0.000	0.000	0.000
107	A	144	LYS	1	0.838	0.902	24.280	21.207	21.207	0.000	0.000	0.000	0.000
108	A	145	SER	0	-0.026	-0.035	26.119	-0.224	-0.224	0.000	0.000	0.000	0.000
109	A	146	GLY	0	0.010	0.006	23.424	-0.004	-0.004	0.000	0.000	0.000	0.000
110	A	147	ILE	0	-0.013	0.004	23.701	-0.700	-0.700	0.000	0.000	0.000	0.000
111	A	148	LYS	1	0.953	0.984	19.971	27.794	27.794	0.000	0.000	0.000	0.000
112	A	149	CYS	0	0.002	0.009	22.744	0.306	0.306	0.000	0.000	0.000	0.000
113	A	150	GLN	0	-0.003	-0.012	24.026	-0.706	-0.706	0.000	0.000	0.000	0.000
114	A	151	PRO	0	-0.034	-0.043	23.909	-0.243	-0.243	0.000	0.000	0.000	0.000
115	A	152	TRP	0	-0.008	-0.006	24.218	1.456	1.456	0.000	0.000	0.000	0.000
116	A	153	SER	0	-0.045	-0.034	27.192	0.810	0.810	0.000	0.000	0.000	0.000
117	A	154	SER	0	-0.051	-0.013	28.288	0.411	0.411	0.000	0.000	0.000	0.000
118	A	155	MET	0	-0.002	0.011	30.086	-0.029	-0.029	0.000	0.000	0.000	0.000
119	A	156	ILE	0	0.031	0.046	30.709	0.454	0.454	0.000	0.000	0.000	0.000
120	A	157	PRO	0	-0.018	-0.029	29.902	-0.793	-0.793	0.000	0.000	0.000	0.000
121	A	158	HIS	0	-0.025	0.000	31.943	1.054	1.054	0.000	0.000	0.000	0.000
122	A	159	GLU	-1	-0.840	-0.913	33.999	-16.023	-16.023	0.000	0.000	0.000	0.000
123	A	160	HIS	0	-0.033	-0.014	31.315	0.515	0.515	0.000	0.000	0.000	0.000
124	A	161	SER	0	0.060	0.027	35.923	0.029	0.029	0.000	0.000	0.000	0.000
125	A	162	PHE	0	-0.034	-0.026	31.277	0.068	0.068	0.000	0.000	0.000	0.000
126	A	163	LEU	0	0.071	0.033	30.988	-0.788	-0.788	0.000	0.000	0.000	0.000
127	A	164	PRO	0	0.032	-0.004	28.018	0.304	0.304	0.000	0.000	0.000	0.000
128	A	165	SER	0	-0.025	-0.017	30.062	-0.151	-0.151	0.000	0.000	0.000	0.000
129	A	166	SER	0	-0.015	0.006	33.033	0.561	0.561	0.000	0.000	0.000	0.000
130	A	167	TYR	0	-0.009	0.004	30.702	0.174	0.174	0.000	0.000	0.000	0.000
131	A	168	ARG	1	1.026	1.009	29.780	16.459	16.459	0.000	0.000	0.000	0.000
132	A	169	GLY	0	-0.018	-0.020	27.407	0.282	0.282	0.000	0.000	0.000	0.000
133	A	170	LYS	1	0.828	0.928	26.978	19.440	19.440	0.000	0.000	0.000	0.000
134	A	171	ASP	-1	-0.799	-0.864	20.658	-27.969	-27.969	0.000	0.000	0.000	0.000
135	A	172	LEU	0	0.012	0.033	23.137	-0.830	-0.830	0.000	0.000	0.000	0.000
136	A	173	GLN	0	-0.070	-0.064	19.436	-0.167	-0.167	0.000	0.000	0.000	0.000
137	A	174	GLU	-1	-0.899	-0.961	18.258	-29.594	-29.594	0.000	0.000	0.000	0.000
138	A	175	ASN	0	-0.055	-0.038	20.058	0.183	0.183	0.000	0.000	0.000	0.000
139	A	176	TYR	0	0.006	0.008	16.121	-0.925	-0.925	0.000	0.000	0.000	0.000
140	A	177	CYS	0	0.012	0.023	20.854	0.704	0.704	0.000	0.000	0.000	0.000
141	A	178	ARG	1	0.726	0.841	19.185	26.174	26.174	0.000	0.000	0.000	0.000
142	A	179	ASN	0	0.053	0.020	25.276	0.823	0.823	0.000	0.000	0.000	0.000
143	A	180	PRO	0	-0.056	-0.028	28.661	0.200	0.200	0.000	0.000	0.000	0.000
144	A	181	ARG	1	0.888	0.927	30.625	16.514	16.514	0.000	0.000	0.000	0.000
145	A	182	GLY	0	-0.083	-0.045	32.045	0.337	0.337	0.000	0.000	0.000	0.000
146	A	183	GLU	-1	-0.793	-0.891	33.042	-16.632	-16.632	0.000	0.000	0.000	0.000
147	A	184	GLU	-1	-0.787	-0.908	32.776	-16.865	-16.865	0.000	0.000	0.000	0.000
148	A	185	GLY	0	0.000	0.011	32.058	-0.278	-0.278	0.000	0.000	0.000	0.000
149	A	186	GLY	0	0.043	0.032	28.271	-0.520	-0.520	0.000	0.000	0.000	0.000
150	A	187	PRO	0	-0.106	-0.063	23.885	0.352	0.352	0.000	0.000	0.000	0.000
151	A	188	TRP	0	0.037	0.036	26.289	-0.367	-0.367	0.000	0.000	0.000	0.000
152	A	190	PHE	0	0.061	0.025	27.375	0.601	0.601	0.000	0.000	0.000	0.000
153	A	191	THR	0	-0.011	-0.009	27.626	-1.052	-1.052	0.000	0.000	0.000	0.000
154	A	192	SER	0	-0.042	-0.054	25.824	0.454	0.454	0.000	0.000	0.000	0.000
155	A	193	ASN	0	0.051	0.037	28.195	0.475	0.475	0.000	0.000	0.000	0.000
156	A	194	PRO	0	0.013	-0.009	31.113	0.160	0.160	0.000	0.000	0.000	0.000
157	A	195	GLU	-1	-0.893	-0.936	34.586	-16.319	-16.319	0.000	0.000	0.000	0.000
158	A	196	VAL	0	-0.031	-0.003	31.612	0.292	0.292	0.000	0.000	0.000	0.000
159	A	197	ARG	1	0.884	0.940	32.389	16.098	16.098	0.000	0.000	0.000	0.000
160	A	198	TYR	0	-0.032	-0.036	31.001	-0.502	-0.502	0.000	0.000	0.000	0.000
161	A	199	GLU	-1	-0.780	-0.836	28.795	-20.293	-20.293	0.000	0.000	0.000	0.000
162	A	200	VAL	0	0.010	0.007	27.698	-0.525	-0.525	0.000	0.000	0.000	0.000
163	A	202	ASP	-1	-0.803	-0.885	22.727	-22.673	-22.673	0.000	0.000	0.000	0.000
164	A	203	ILE	0	-0.098	-0.048	20.141	-1.343	-1.343	0.000	0.000	0.000	0.000
165	A	204	PRO	0	0.092	0.051	20.072	0.868	0.868	0.000	0.000	0.000	0.000
166	A	205	GLN	0	-0.009	-0.026	22.777	-0.484	-0.484	0.000	0.000	0.000	0.000
167	A	207	SER	0	0.008	0.003	23.464	-0.172	-0.172	0.000	0.000	0.000	0.000
168	A	208	GLU	-1	-0.917	-0.942	24.393	-21.677	-21.677	0.000	0.000	0.000	0.000
169	A	209	VAL	-1	-0.936	-0.951	22.185	-23.459	-23.459	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:36:ARG)