FMO DATABASE

FMODB ID: NL1RQ

Calculation Name: 1SRV-A-Xray547

Preferred Name:

Target Type:

Ligand Name:

Ligand 3-letter code:

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 1SRV

Chain ID: A

ChEMBL ID:

UniProt ID: P61491

Base Structure: X-ray

Registration Date: 2025-10-05

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	OptAll
Protonation	MOE:Protonate 3D
Complement	MOE:Homology Modeling
Water	No
Procedure	Manual calculation
Remarks	ac.sh, 23 2024 Oct; Missing atoms/residues were imported from a 100% homology model, which was constructed by MOE.

FMO calculation

FMO method	FMO2-MP2/6-31G(d)
Fragmentation	Auto
Number of fragment	145
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230922

Total energy (hartree)

FMO2-HF: Electronic energy	-1317723.861611
FMO2-HF: Nuclear repulsion	1263117.902488
FMO2-HF: Total energy	-54605.959122
FMO2-MP2: Total energy	-54766.915426

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:192:GLY)

Summations of interaction energy for fragment #1(A:192:GLY)

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.
-117.123	-114.486	4.327	-3.794	-3.17	-0.032

Interaction energy analysis for fragmet #1(A:192:GLY)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 1 / q_Mulliken : 0.834 / q_NPA : 0.903

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	194	GLN	0	-0.060	-0.045	3.827	-1.793	-1.018	-0.003	-0.242	-0.530	-0.001
140	A	331	THR	0	-0.021	-0.008	3.449	-4.583	-4.474	0.008	-0.052	-0.065	0.000
141	A	332	ILE	0	-0.001	0.003	3.954	4.946	5.094	-0.001	-0.056	-0.091	0.000
142	A	333	VAL	0	-0.035	-0.044	2.299	-27.148	-25.487	4.319	-3.414	-2.565	-0.031
143	A	334	GLY	0	0.063	0.034	3.927	6.662	6.606	0.004	-0.030	0.081	0.000
4	A	195	PHE	0	0.074	0.026	6.287	3.196	3.196	0.000	0.000	0.000	0.000
5	A	196	ASP	-1	-0.840	-0.901	10.039	-24.685	-24.685	0.000	0.000	0.000	0.000
6	A	197	LYS	1	0.827	0.899	12.647	20.666	20.666	0.000	0.000	0.000	0.000
7	A	198	GLY	0	0.062	0.061	12.984	-1.613	-1.613	0.000	0.000	0.000	0.000
8	A	199	TYR	0	-0.077	-0.063	14.879	0.744	0.744	0.000	0.000	0.000	0.000
9	A	200	ILE	0	-0.040	-0.014	16.971	0.555	0.555	0.000	0.000	0.000	0.000
10	A	201	SER	0	0.004	-0.001	20.323	0.820	0.820	0.000	0.000	0.000	0.000
11	A	202	PRO	0	0.037	0.020	20.758	-0.580	-0.580	0.000	0.000	0.000	0.000
12	A	203	TYR	0	0.008	0.001	21.987	-0.109	-0.109	0.000	0.000	0.000	0.000
13	A	204	PHE	0	0.012	-0.002	18.426	0.115	0.115	0.000	0.000	0.000	0.000
14	A	205	VAL	0	-0.049	-0.002	18.245	-0.629	-0.629	0.000	0.000	0.000	0.000
15	A	206	THR	0	-0.032	-0.024	16.307	1.089	1.089	0.000	0.000	0.000	0.000
16	A	207	ASN	0	-0.008	-0.012	17.753	1.212	1.212	0.000	0.000	0.000	0.000
17	A	208	PRO	0	0.001	-0.022	19.425	-0.368	-0.368	0.000	0.000	0.000	0.000
18	A	209	GLU	-1	-0.915	-0.926	20.676	-14.111	-14.111	0.000	0.000	0.000	0.000
19	A	210	THR	0	-0.045	-0.046	16.068	0.456	0.456	0.000	0.000	0.000	0.000
20	A	211	MET	0	-0.027	0.002	17.728	-0.350	-0.350	0.000	0.000	0.000	0.000
21	A	212	GLU	-1	-0.778	-0.842	12.940	-23.498	-23.498	0.000	0.000	0.000	0.000
22	A	213	ALA	0	-0.016	-0.007	14.329	1.316	1.316	0.000	0.000	0.000	0.000
23	A	214	VAL	0	-0.019	-0.010	11.154	-1.825	-1.825	0.000	0.000	0.000	0.000
24	A	215	LEU	0	-0.017	0.000	11.668	1.667	1.667	0.000	0.000	0.000	0.000
25	A	216	GLU	-1	-0.914	-0.974	11.189	-24.973	-24.973	0.000	0.000	0.000	0.000
26	A	217	ASP	-1	-0.841	-0.920	12.355	-17.563	-17.563	0.000	0.000	0.000	0.000
27	A	218	ALA	0	-0.007	0.020	11.843	1.426	1.426	0.000	0.000	0.000	0.000
28	A	219	PHE	0	0.043	0.004	12.994	-0.900	-0.900	0.000	0.000	0.000	0.000
29	A	220	ILE	0	-0.035	-0.017	10.334	-0.530	-0.530	0.000	0.000	0.000	0.000
30	A	221	LEU	0	0.003	0.012	14.203	0.636	0.636	0.000	0.000	0.000	0.000
31	A	222	ILE	0	-0.004	0.006	13.108	-0.391	-0.391	0.000	0.000	0.000	0.000
32	A	223	VAL	0	-0.018	-0.012	16.963	0.858	0.858	0.000	0.000	0.000	0.000
33	A	224	GLU	-1	-0.842	-0.915	19.706	-14.556	-14.556	0.000	0.000	0.000	0.000
34	A	225	LYS	1	0.780	0.881	21.686	11.106	11.106	0.000	0.000	0.000	0.000
35	A	226	LYS	1	0.845	0.903	23.296	11.252	11.252	0.000	0.000	0.000	0.000
36	A	227	VAL	0	0.008	0.000	23.193	0.383	0.383	0.000	0.000	0.000	0.000
37	A	228	SER	0	-0.002	-0.031	25.816	-0.028	-0.028	0.000	0.000	0.000	0.000
38	A	229	ASN	0	0.002	-0.004	28.950	0.190	0.190	0.000	0.000	0.000	0.000
39	A	230	VAL	0	0.075	0.035	29.505	-0.315	-0.315	0.000	0.000	0.000	0.000
40	A	231	ARG	1	0.924	0.955	30.085	8.464	8.464	0.000	0.000	0.000	0.000
41	A	232	GLU	-1	-0.832	-0.901	28.103	-10.791	-10.791	0.000	0.000	0.000	0.000
42	A	233	LEU	0	0.019	0.004	23.524	-0.352	-0.352	0.000	0.000	0.000	0.000
43	A	234	LEU	0	-0.025	-0.009	26.685	-0.248	-0.248	0.000	0.000	0.000	0.000
44	A	235	PRO	0	0.084	0.045	28.525	-0.153	-0.153	0.000	0.000	0.000	0.000
45	A	236	ILE	0	-0.005	0.016	22.440	-0.111	-0.111	0.000	0.000	0.000	0.000
46	A	237	LEU	0	-0.016	-0.014	23.016	-0.400	-0.400	0.000	0.000	0.000	0.000
47	A	238	GLU	-1	-0.918	-0.968	25.216	-9.924	-9.924	0.000	0.000	0.000	0.000
48	A	239	GLN	0	-0.055	-0.044	25.156	-0.144	-0.144	0.000	0.000	0.000	0.000
49	A	240	VAL	0	0.026	0.010	20.345	-0.127	-0.127	0.000	0.000	0.000	0.000
50	A	241	ALA	0	0.023	0.032	23.087	-0.127	-0.127	0.000	0.000	0.000	0.000
51	A	242	GLN	0	-0.056	-0.022	25.586	0.095	0.095	0.000	0.000	0.000	0.000
52	A	243	THR	0	-0.074	-0.054	22.021	-0.172	-0.172	0.000	0.000	0.000	0.000
53	A	244	GLY	0	-0.011	-0.004	23.227	-0.192	-0.192	0.000	0.000	0.000	0.000
54	A	245	LYS	1	0.823	0.909	17.843	15.973	15.973	0.000	0.000	0.000	0.000
55	A	246	PRO	0	-0.028	-0.017	15.329	0.363	0.363	0.000	0.000	0.000	0.000
56	A	247	LEU	0	-0.029	-0.004	16.343	-0.366	-0.366	0.000	0.000	0.000	0.000
57	A	248	LEU	0	0.011	0.005	10.607	0.215	0.215	0.000	0.000	0.000	0.000
58	A	249	ILE	0	-0.012	-0.014	14.683	0.397	0.397	0.000	0.000	0.000	0.000
59	A	250	ILE	0	0.007	0.006	11.643	-0.302	-0.302	0.000	0.000	0.000	0.000
60	A	251	ALA	0	0.055	0.031	16.143	0.560	0.560	0.000	0.000	0.000	0.000
61	A	252	GLU	-1	-0.843	-0.892	19.288	-12.799	-12.799	0.000	0.000	0.000	0.000
62	A	253	ASP	-1	-0.814	-0.937	21.468	-13.071	-13.071	0.000	0.000	0.000	0.000
63	A	254	VAL	0	-0.007	0.009	20.819	0.042	0.042	0.000	0.000	0.000	0.000
64	A	255	GLU	-1	-0.858	-0.905	23.533	-10.801	-10.801	0.000	0.000	0.000	0.000
65	A	256	GLY	0	0.036	0.008	26.966	0.099	0.099	0.000	0.000	0.000	0.000
66	A	257	GLU	-1	-0.913	-0.962	29.896	-9.268	-9.268	0.000	0.000	0.000	0.000
67	A	258	ALA	0	0.006	0.019	26.328	-0.068	-0.068	0.000	0.000	0.000	0.000
68	A	259	LEU	0	-0.005	0.001	23.458	-0.270	-0.270	0.000	0.000	0.000	0.000
69	A	260	ALA	0	0.017	0.006	26.130	-0.185	-0.185	0.000	0.000	0.000	0.000
70	A	261	THR	0	-0.001	-0.009	28.015	0.117	0.117	0.000	0.000	0.000	0.000
71	A	262	LEU	0	-0.003	0.006	21.574	-0.052	-0.052	0.000	0.000	0.000	0.000
72	A	263	VAL	0	0.004	0.000	24.375	-0.201	-0.201	0.000	0.000	0.000	0.000
73	A	264	VAL	0	-0.003	0.001	25.682	0.011	0.011	0.000	0.000	0.000	0.000
74	A	265	ASN	0	-0.024	-0.029	26.250	0.262	0.262	0.000	0.000	0.000	0.000
75	A	266	LYS	1	0.833	0.931	20.668	14.014	14.014	0.000	0.000	0.000	0.000
76	A	267	LEU	0	-0.039	-0.028	24.427	0.043	0.043	0.000	0.000	0.000	0.000
77	A	268	ARG	1	0.885	0.945	27.097	9.876	9.876	0.000	0.000	0.000	0.000
78	A	269	GLY	0	-0.005	0.006	25.654	0.258	0.258	0.000	0.000	0.000	0.000
79	A	270	THR	0	-0.082	-0.036	26.602	0.142	0.142	0.000	0.000	0.000	0.000
80	A	271	LEU	0	0.039	0.011	22.615	-0.078	-0.078	0.000	0.000	0.000	0.000
81	A	272	SER	0	-0.004	0.014	18.413	-0.148	-0.148	0.000	0.000	0.000	0.000
82	A	273	VAL	0	0.007	0.000	18.521	-0.649	-0.649	0.000	0.000	0.000	0.000
83	A	274	ALA	0	0.008	-0.004	15.564	0.284	0.284	0.000	0.000	0.000	0.000
84	A	275	ALA	0	0.012	0.018	16.818	-0.487	-0.487	0.000	0.000	0.000	0.000
85	A	276	VAL	0	0.011	0.000	12.857	0.220	0.220	0.000	0.000	0.000	0.000
86	A	277	LYS	1	0.836	0.903	16.183	14.391	14.391	0.000	0.000	0.000	0.000
87	A	278	ALA	0	0.028	0.015	15.507	-1.398	-1.398	0.000	0.000	0.000	0.000
88	A	279	PRO	0	-0.012	-0.005	12.753	0.931	0.931	0.000	0.000	0.000	0.000
89	A	280	GLY	0	0.000	-0.008	15.752	0.523	0.523	0.000	0.000	0.000	0.000
90	A	281	PHE	0	-0.005	-0.003	18.575	0.473	0.473	0.000	0.000	0.000	0.000
91	A	282	GLY	0	0.021	0.007	21.838	-0.198	-0.198	0.000	0.000	0.000	0.000
92	A	283	ASP	-1	-0.859	-0.931	21.985	-13.345	-13.345	0.000	0.000	0.000	0.000
93	A	284	ARG	1	0.974	0.978	18.460	14.611	14.611	0.000	0.000	0.000	0.000
94	A	285	ARG	0	-0.019	0.001	17.233	-0.526	-0.526	0.000	0.000	0.000	0.000
95	A	286	LYS	1	0.861	0.917	17.287	11.858	11.858	0.000	0.000	0.000	0.000
96	A	287	GLU	-1	-0.901	-0.953	16.206	-16.293	-16.293	0.000	0.000	0.000	0.000
97	A	288	MET	0	0.022	0.016	11.568	-0.341	-0.341	0.000	0.000	0.000	0.000
98	A	289	LEU	0	-0.011	-0.004	12.819	-1.571	-1.571	0.000	0.000	0.000	0.000
99	A	290	LYS	1	0.861	0.923	14.463	15.938	15.938	0.000	0.000	0.000	0.000
100	A	291	ASP	-1	-0.858	-0.913	10.202	-26.313	-26.313	0.000	0.000	0.000	0.000
101	A	292	ILE	0	-0.026	-0.022	9.188	-1.773	-1.773	0.000	0.000	0.000	0.000
102	A	293	ALA	0	-0.009	0.005	10.455	-0.584	-0.584	0.000	0.000	0.000	0.000
103	A	294	ALA	0	-0.006	-0.004	11.888	-0.043	-0.043	0.000	0.000	0.000	0.000
104	A	295	VAL	0	-0.085	-0.039	5.576	-1.438	-1.438	0.000	0.000	0.000	0.000
105	A	296	THR	0	-0.063	-0.046	7.788	-1.612	-1.612	0.000	0.000	0.000	0.000
106	A	297	GLY	0	0.083	0.058	10.162	1.515	1.515	0.000	0.000	0.000	0.000
107	A	298	GLY	0	-0.009	0.004	13.245	1.379	1.379	0.000	0.000	0.000	0.000
108	A	299	THR	0	-0.054	-0.034	15.131	0.393	0.393	0.000	0.000	0.000	0.000
109	A	300	VAL	0	-0.015	-0.005	16.700	-0.140	-0.140	0.000	0.000	0.000	0.000
110	A	301	ILE	0	-0.019	-0.009	18.912	0.833	0.833	0.000	0.000	0.000	0.000
111	A	302	SER	0	0.001	-0.033	22.184	0.201	0.201	0.000	0.000	0.000	0.000
112	A	303	GLU	-1	-0.841	-0.913	24.213	-10.383	-10.383	0.000	0.000	0.000	0.000
113	A	304	GLU	-1	-0.849	-0.908	26.650	-11.430	-11.430	0.000	0.000	0.000	0.000
114	A	305	LEU	0	-0.043	-0.019	24.261	0.299	0.299	0.000	0.000	0.000	0.000
115	A	306	GLY	0	-0.005	0.002	28.211	0.121	0.121	0.000	0.000	0.000	0.000
116	A	307	PHE	0	-0.055	-0.025	25.792	0.194	0.194	0.000	0.000	0.000	0.000
117	A	308	LYS	1	0.899	0.934	27.510	9.175	9.175	0.000	0.000	0.000	0.000
118	A	309	LEU	0	0.018	0.005	23.281	-0.136	-0.136	0.000	0.000	0.000	0.000
119	A	310	GLU	-1	-0.849	-0.923	26.820	-9.595	-9.595	0.000	0.000	0.000	0.000
120	A	311	ASN	0	-0.040	-0.012	29.065	0.319	0.319	0.000	0.000	0.000	0.000
121	A	312	ALA	0	0.015	0.013	23.629	-0.139	-0.139	0.000	0.000	0.000	0.000
122	A	313	THR	0	0.013	-0.005	24.274	0.163	0.163	0.000	0.000	0.000	0.000
123	A	314	LEU	0	0.037	0.005	21.628	-0.575	-0.575	0.000	0.000	0.000	0.000
124	A	315	SER	0	-0.047	-0.022	20.557	-0.466	-0.466	0.000	0.000	0.000	0.000
125	A	316	MET	0	-0.043	-0.002	20.118	-0.095	-0.095	0.000	0.000	0.000	0.000
126	A	317	LEU	0	-0.056	-0.010	17.366	-0.641	-0.641	0.000	0.000	0.000	0.000
127	A	318	GLY	0	0.090	0.053	13.288	0.075	0.075	0.000	0.000	0.000	0.000
128	A	319	ARG	1	0.873	0.919	12.494	19.384	19.384	0.000	0.000	0.000	0.000
129	A	320	ALA	0	0.036	0.009	7.535	-2.007	-2.007	0.000	0.000	0.000	0.000
130	A	321	GLU	-1	-0.975	-0.981	8.761	-25.653	-25.653	0.000	0.000	0.000	0.000
131	A	322	ARG	1	0.925	0.968	7.433	30.488	30.488	0.000	0.000	0.000	0.000
132	A	323	VAL	0	0.007	0.012	6.550	-5.191	-5.191	0.000	0.000	0.000	0.000
133	A	324	ARG	1	0.800	0.888	7.418	32.277	32.277	0.000	0.000	0.000	0.000
134	A	325	ILE	0	-0.004	0.003	8.787	-1.987	-1.987	0.000	0.000	0.000	0.000
135	A	326	THR	0	0.023	0.010	11.585	1.743	1.743	0.000	0.000	0.000	0.000
136	A	327	LYS	1	0.878	0.937	13.825	16.238	16.238	0.000	0.000	0.000	0.000
137	A	328	ASP	-1	-0.878	-0.943	15.254	-16.651	-16.651	0.000	0.000	0.000	0.000
138	A	329	GLU	-1	-0.851	-0.915	9.498	-32.944	-32.944	0.000	0.000	0.000	0.000
139	A	330	THR	0	0.018	-0.007	8.416	1.489	1.489	0.000	0.000	0.000	0.000
144	A	335	GLY	0	-0.034	-0.007	5.336	4.037	4.037	0.000	0.000	0.000	0.000
145	A	336	LYS	0	-0.030	-0.004	7.190	-1.399	-1.399	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:192:GLY)