FMO DATABASE

FMODB ID: K81Z3

Calculation Name: 1CXV-A-Xray547

Preferred Name: Collagenase 3

Target Type: SINGLE PROTEIN

Ligand Name: 2-{4-[4-(4-chloro-phenoxy)-benzenesulfonyl]-tetrahydro-pyran-4-yl}-n-hydroxy-acetamide | calcium ion | zinc ion

Ligand 3-letter code: CBP | CA | ZN

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 1CXV

Chain ID: A

ChEMBL ID: CHEMBL3638350

UniProt ID: P33435

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	164
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230922

Total energy (hartree)

FMO2-HF: Electronic energy	-1704187.414446
FMO2-HF: Nuclear repulsion	1639623.42278
FMO2-HF: Total energy	-64563.991666
FMO2-MP2: Total energy	-64754.158835

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:83:TYR)

Summations of interaction energy for fragment #1(A:83:TYR)

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.
-259.464	-250.797	37.856	-17.779	-28.743	-0.191

Interaction energy analysis for fragmet #1(A:83:TYR)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 1 / q_Mulliken : 0.763 / q_NPA : 0.884

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	85	VAL	0	0.060	0.038	2.475	-2.435	0.817	0.745	-1.353	-2.644	-0.007
4	A	86	PHE	0	0.038	0.037	4.599	1.706	1.770	-0.001	-0.013	-0.050	0.000
127	A	209	LEU	0	-0.052	-0.017	2.813	-3.930	-3.089	0.122	-0.174	-0.790	-0.001
129	A	211	HIS	0	-0.017	-0.022	4.643	-5.766	-5.518	-0.001	-0.013	-0.234	0.000
130	A	212	SER	0	-0.048	-0.046	2.481	-10.849	-8.649	2.344	-2.370	-2.175	-0.015
131	A	213	LYS	1	0.918	0.943	3.357	48.597	48.763	0.029	0.078	-0.273	-0.001
132	A	214	ASP	-1	-0.857	-0.914	4.389	-36.288	-36.172	-0.001	-0.013	-0.101	0.000
137	A	219	MET	0	-0.038	0.005	4.445	3.399	3.521	-0.001	-0.022	-0.098	0.000
154	A	236	ASP	-1	-0.732	-0.823	1.773	-145.434	-149.030	23.886	-12.087	-8.203	-0.129
155	A	237	ASP	-1	-0.725	-0.877	2.581	-59.733	-56.421	1.321	-1.981	-2.652	-0.026
156	A	238	VAL	0	-0.004	0.002	4.335	3.031	3.094	-0.001	-0.013	-0.050	0.000
157	A	239	GLN	0	0.022	0.008	2.665	2.600	3.462	0.331	-0.248	-0.945	0.000
158	A	240	GLY	0	0.002	-0.010	2.750	0.415	2.026	6.381	-3.269	-4.722	0.004
159	A	241	ILE	0	-0.028	-0.026	3.340	7.664	3.146	0.261	5.695	-1.438	-0.001
161	A	243	PHE	0	-0.035	-0.007	2.665	-6.381	-2.664	2.442	-1.986	-4.173	-0.015
162	A	244	LEU	0	-0.044	-0.010	4.675	1.512	1.719	-0.001	-0.010	-0.195	0.000
5	A	87	PRO	0	0.016	-0.007	8.418	0.338	0.338	0.000	0.000	0.000	0.000
6	A	88	ARG	1	0.885	0.927	10.679	19.192	19.192	0.000	0.000	0.000	0.000
7	A	89	THR	0	0.002	0.015	5.868	0.393	0.393	0.000	0.000	0.000	0.000
8	A	90	LEU	0	-0.033	-0.006	8.280	1.249	1.249	0.000	0.000	0.000	0.000
9	A	91	LYS	1	0.917	0.957	9.260	19.354	19.354	0.000	0.000	0.000	0.000
10	A	92	TRP	0	0.025	-0.007	11.090	1.635	1.635	0.000	0.000	0.000	0.000
11	A	93	SER	0	-0.022	-0.024	14.136	-0.231	-0.231	0.000	0.000	0.000	0.000
12	A	94	GLN	0	-0.039	-0.017	16.672	0.671	0.671	0.000	0.000	0.000	0.000
13	A	95	THR	0	0.057	0.025	16.342	-0.467	-0.467	0.000	0.000	0.000	0.000
14	A	96	ASN	0	-0.033	-0.005	18.093	-0.318	-0.318	0.000	0.000	0.000	0.000
15	A	97	LEU	0	0.033	0.029	15.853	0.113	0.113	0.000	0.000	0.000	0.000
16	A	98	THR	0	-0.034	-0.050	20.319	0.333	0.333	0.000	0.000	0.000	0.000
17	A	99	TYR	0	0.011	-0.005	20.182	-0.282	-0.282	0.000	0.000	0.000	0.000
18	A	100	ARG	1	0.877	0.925	22.154	10.574	10.574	0.000	0.000	0.000	0.000
19	A	101	ILE	0	-0.033	-0.004	23.811	-0.312	-0.312	0.000	0.000	0.000	0.000
20	A	102	VAL	0	-0.009	-0.003	25.646	0.459	0.459	0.000	0.000	0.000	0.000
21	A	103	ASN	0	-0.047	-0.032	27.361	0.134	0.134	0.000	0.000	0.000	0.000
22	A	104	TYR	0	-0.077	-0.069	27.366	-0.355	-0.355	0.000	0.000	0.000	0.000
23	A	105	THR	0	0.039	0.020	27.116	0.314	0.314	0.000	0.000	0.000	0.000
24	A	106	PRO	0	-0.014	-0.010	29.201	0.188	0.188	0.000	0.000	0.000	0.000
25	A	107	ASP	-1	-0.835	-0.886	29.141	-10.488	-10.488	0.000	0.000	0.000	0.000
26	A	108	MET	0	-0.071	-0.019	25.258	-0.255	-0.255	0.000	0.000	0.000	0.000
27	A	109	SER	0	-0.004	-0.003	30.212	0.127	0.127	0.000	0.000	0.000	0.000
28	A	110	HIS	0	0.089	0.033	30.075	-0.392	-0.392	0.000	0.000	0.000	0.000
29	A	111	SER	0	0.031	0.005	29.224	-0.265	-0.265	0.000	0.000	0.000	0.000
30	A	112	GLU	-1	-0.885	-0.960	27.788	-10.592	-10.592	0.000	0.000	0.000	0.000
31	A	113	VAL	0	0.101	0.061	25.088	-0.522	-0.522	0.000	0.000	0.000	0.000
32	A	114	GLU	-1	-0.783	-0.852	24.258	-10.771	-10.771	0.000	0.000	0.000	0.000
33	A	115	LYS	1	0.755	0.894	24.576	10.573	10.573	0.000	0.000	0.000	0.000
34	A	116	ALA	0	-0.016	0.000	21.644	-0.394	-0.394	0.000	0.000	0.000	0.000
35	A	117	PHE	0	0.109	0.040	18.935	-0.619	-0.619	0.000	0.000	0.000	0.000
36	A	118	ARG	1	0.925	0.973	19.629	10.978	10.978	0.000	0.000	0.000	0.000
37	A	119	LYS	1	0.860	0.929	19.551	12.816	12.816	0.000	0.000	0.000	0.000
38	A	120	ALA	0	0.034	0.017	16.068	-0.611	-0.611	0.000	0.000	0.000	0.000
39	A	121	PHE	0	0.045	0.015	15.031	-0.976	-0.976	0.000	0.000	0.000	0.000
40	A	122	LYS	1	0.793	0.885	15.878	14.130	14.130	0.000	0.000	0.000	0.000
41	A	123	VAL	0	-0.035	-0.021	11.720	-0.154	-0.154	0.000	0.000	0.000	0.000
42	A	124	TRP	0	0.019	0.005	6.870	-1.936	-1.936	0.000	0.000	0.000	0.000
43	A	125	SER	0	0.027	0.022	12.653	-0.269	-0.269	0.000	0.000	0.000	0.000
44	A	126	ASP	-1	-0.881	-0.908	15.568	-15.456	-15.456	0.000	0.000	0.000	0.000
45	A	127	VAL	0	-0.035	-0.006	10.169	0.137	0.137	0.000	0.000	0.000	0.000
46	A	128	THR	0	0.013	-0.007	11.234	-1.079	-1.079	0.000	0.000	0.000	0.000
47	A	129	PRO	0	-0.011	0.006	13.422	1.039	1.039	0.000	0.000	0.000	0.000
48	A	130	LEU	0	-0.039	-0.011	12.642	0.806	0.806	0.000	0.000	0.000	0.000
49	A	131	ASN	0	-0.047	-0.028	16.889	0.060	0.060	0.000	0.000	0.000	0.000
50	A	132	PHE	0	0.032	0.010	14.316	0.250	0.250	0.000	0.000	0.000	0.000
51	A	133	THR	0	-0.037	-0.020	20.396	0.580	0.580	0.000	0.000	0.000	0.000
52	A	134	ARG	1	0.788	0.886	23.829	10.629	10.629	0.000	0.000	0.000	0.000
53	A	135	ILE	0	-0.005	-0.003	25.455	0.428	0.428	0.000	0.000	0.000	0.000
54	A	136	TYR	0	0.022	-0.008	27.837	-0.244	-0.244	0.000	0.000	0.000	0.000
55	A	137	ASP	-1	-0.903	-0.939	30.638	-8.705	-8.705	0.000	0.000	0.000	0.000
56	A	138	GLY	0	-0.013	-0.012	30.231	-0.220	-0.220	0.000	0.000	0.000	0.000
57	A	139	THR	0	-0.010	-0.025	25.429	-0.050	-0.050	0.000	0.000	0.000	0.000
58	A	140	ALA	0	-0.032	-0.020	23.336	0.179	0.179	0.000	0.000	0.000	0.000
59	A	141	ASP	-1	-0.822	-0.879	19.289	-13.264	-13.264	0.000	0.000	0.000	0.000
60	A	142	ILE	0	0.009	0.003	15.829	-0.628	-0.628	0.000	0.000	0.000	0.000
61	A	143	MET	0	-0.026	0.012	19.817	0.604	0.604	0.000	0.000	0.000	0.000
62	A	144	ILE	0	-0.013	-0.003	19.579	-0.383	-0.383	0.000	0.000	0.000	0.000
63	A	145	SER	0	-0.028	-0.012	21.978	0.633	0.633	0.000	0.000	0.000	0.000
64	A	146	PHE	0	0.015	0.000	23.140	-0.607	-0.607	0.000	0.000	0.000	0.000
65	A	147	GLY	0	0.026	0.007	25.628	0.405	0.405	0.000	0.000	0.000	0.000
66	A	148	THR	0	0.024	0.031	26.405	-0.358	-0.358	0.000	0.000	0.000	0.000
67	A	149	LYS	1	0.870	0.925	28.097	10.328	10.328	0.000	0.000	0.000	0.000
68	A	150	GLU	-1	-0.947	-0.960	27.117	-10.152	-10.152	0.000	0.000	0.000	0.000
69	A	151	HIS	1	0.816	0.913	23.292	12.612	12.612	0.000	0.000	0.000	0.000
70	A	152	GLY	0	0.016	0.007	27.458	-0.148	-0.148	0.000	0.000	0.000	0.000
71	A	153	ASP	-1	-0.823	-0.916	23.206	-13.060	-13.060	0.000	0.000	0.000	0.000
72	A	154	PHE	0	-0.036	-0.024	19.664	0.244	0.244	0.000	0.000	0.000	0.000
73	A	155	TYR	0	-0.030	-0.005	16.600	-0.732	-0.732	0.000	0.000	0.000	0.000
74	A	156	PRO	0	-0.025	-0.011	22.531	-0.028	-0.028	0.000	0.000	0.000	0.000
75	A	157	PHE	0	-0.014	-0.005	20.560	-0.381	-0.381	0.000	0.000	0.000	0.000
76	A	158	ASP	-1	-0.816	-0.916	23.817	-12.422	-12.422	0.000	0.000	0.000	0.000
77	A	159	GLY	0	-0.024	-0.007	26.134	0.582	0.582	0.000	0.000	0.000	0.000
78	A	160	PRO	0	-0.054	-0.009	26.075	-0.296	-0.296	0.000	0.000	0.000	0.000
79	A	161	SER	0	-0.064	-0.041	24.012	0.160	0.160	0.000	0.000	0.000	0.000
80	A	162	GLY	0	0.014	0.025	21.946	0.246	0.246	0.000	0.000	0.000	0.000
81	A	163	LEU	0	-0.088	-0.054	19.060	-1.044	-1.044	0.000	0.000	0.000	0.000
82	A	164	LEU	0	0.010	0.006	17.530	0.131	0.131	0.000	0.000	0.000	0.000
83	A	165	ALA	0	-0.027	-0.031	16.997	0.584	0.584	0.000	0.000	0.000	0.000
84	A	166	HIS	0	-0.014	0.007	15.660	-0.035	-0.035	0.000	0.000	0.000	0.000
85	A	167	ALA	0	0.019	0.023	13.799	1.010	1.010	0.000	0.000	0.000	0.000
86	A	168	PHE	0	-0.048	-0.013	14.160	-1.060	-1.060	0.000	0.000	0.000	0.000
87	A	169	PRO	0	-0.016	0.000	11.423	-0.286	-0.286	0.000	0.000	0.000	0.000
88	A	170	PRO	0	-0.014	-0.002	11.130	1.274	1.274	0.000	0.000	0.000	0.000
89	A	171	GLY	0	-0.005	-0.005	14.032	-0.179	-0.179	0.000	0.000	0.000	0.000
90	A	172	PRO	0	-0.006	-0.001	17.302	0.309	0.309	0.000	0.000	0.000	0.000
91	A	173	ASN	0	-0.055	-0.040	20.840	0.081	0.081	0.000	0.000	0.000	0.000
92	A	174	TYR	0	0.069	0.047	19.773	0.371	0.371	0.000	0.000	0.000	0.000
93	A	175	GLY	0	-0.032	-0.011	17.466	-0.565	-0.565	0.000	0.000	0.000	0.000
94	A	176	GLY	0	0.043	0.021	15.507	0.342	0.342	0.000	0.000	0.000	0.000
95	A	177	ASP	-1	-0.893	-0.926	16.573	-13.732	-13.732	0.000	0.000	0.000	0.000
96	A	178	ALA	0	-0.001	-0.010	16.920	-0.761	-0.761	0.000	0.000	0.000	0.000
97	A	179	HIS	1	0.793	0.899	18.392	14.251	14.251	0.000	0.000	0.000	0.000
98	A	180	PHE	0	0.018	-0.001	17.435	-0.870	-0.870	0.000	0.000	0.000	0.000
99	A	181	ASP	-1	-0.701	-0.875	21.720	-11.169	-11.169	0.000	0.000	0.000	0.000
100	A	182	ASP	-1	-0.915	-0.983	24.314	-10.484	-10.484	0.000	0.000	0.000	0.000
101	A	183	ASP	-1	-0.882	-0.948	27.582	-9.772	-9.772	0.000	0.000	0.000	0.000
102	A	184	GLU	-1	-0.872	-0.929	23.271	-12.417	-12.417	0.000	0.000	0.000	0.000
103	A	185	THR	0	-0.063	-0.025	26.510	0.268	0.268	0.000	0.000	0.000	0.000
104	A	186	TRP	0	-0.010	-0.009	20.155	-0.861	-0.861	0.000	0.000	0.000	0.000
105	A	187	THR	0	-0.073	-0.058	24.681	0.554	0.554	0.000	0.000	0.000	0.000
106	A	188	SER	0	-0.032	-0.030	24.341	-0.513	-0.513	0.000	0.000	0.000	0.000
107	A	189	SER	0	-0.048	-0.034	25.286	-0.155	-0.155	0.000	0.000	0.000	0.000
108	A	190	SER	0	0.045	0.010	23.672	-0.298	-0.298	0.000	0.000	0.000	0.000
109	A	191	LYS	1	0.918	0.972	24.723	9.959	9.959	0.000	0.000	0.000	0.000
110	A	192	GLY	0	0.064	0.041	25.716	0.326	0.326	0.000	0.000	0.000	0.000
111	A	193	TYR	0	0.041	0.035	20.427	-0.523	-0.523	0.000	0.000	0.000	0.000
112	A	194	ASN	0	-0.061	-0.049	19.888	-0.270	-0.270	0.000	0.000	0.000	0.000
113	A	195	LEU	0	0.092	0.035	19.622	-0.718	-0.718	0.000	0.000	0.000	0.000
114	A	196	PHE	0	-0.083	-0.035	16.563	-0.434	-0.434	0.000	0.000	0.000	0.000
115	A	197	ILE	0	0.014	0.001	14.109	-0.526	-0.526	0.000	0.000	0.000	0.000
116	A	198	VAL	0	0.040	0.025	14.479	-1.382	-1.382	0.000	0.000	0.000	0.000
117	A	199	ALA	0	0.022	0.013	14.881	-0.796	-0.796	0.000	0.000	0.000	0.000
118	A	200	ALA	0	-0.017	-0.011	13.099	-0.453	-0.453	0.000	0.000	0.000	0.000
119	A	201	HIS	0	-0.002	-0.004	8.922	-1.190	-1.190	0.000	0.000	0.000	0.000
120	A	202	GLU	-1	-0.804	-0.931	10.425	-22.080	-22.080	0.000	0.000	0.000	0.000
121	A	203	LEU	0	-0.028	-0.014	12.449	-0.183	-0.183	0.000	0.000	0.000	0.000
122	A	204	GLY	0	0.056	0.021	8.353	-0.296	-0.296	0.000	0.000	0.000	0.000
123	A	205	HIS	1	0.764	0.880	8.333	26.397	26.397	0.000	0.000	0.000	0.000
124	A	206	SER	0	0.002	-0.013	9.972	-0.119	-0.119	0.000	0.000	0.000	0.000
125	A	207	LEU	0	-0.026	-0.001	9.735	1.156	1.156	0.000	0.000	0.000	0.000
126	A	208	GLY	0	0.049	0.028	8.357	-0.178	-0.178	0.000	0.000	0.000	0.000
128	A	210	ASP	-1	-0.848	-0.919	5.005	-26.407	-26.407	0.000	0.000	0.000	0.000
133	A	215	PRO	0	-0.015	-0.034	6.059	0.359	0.359	0.000	0.000	0.000	0.000
134	A	216	GLY	0	-0.031	-0.005	8.521	2.911	2.911	0.000	0.000	0.000	0.000
135	A	217	ALA	0	-0.042	-0.012	5.038	1.161	1.161	0.000	0.000	0.000	0.000
136	A	218	LEU	0	-0.045	-0.030	7.091	3.512	3.512	0.000	0.000	0.000	0.000
138	A	220	PHE	0	-0.003	0.014	6.158	-1.130	-1.130	0.000	0.000	0.000	0.000
139	A	221	PRO	0	-0.014	-0.003	7.481	2.622	2.622	0.000	0.000	0.000	0.000
140	A	222	ILE	0	-0.044	-0.026	10.221	2.357	2.357	0.000	0.000	0.000	0.000
141	A	223	TYR	0	0.029	0.036	13.023	-0.593	-0.593	0.000	0.000	0.000	0.000
142	A	224	THR	0	0.017	0.001	14.320	0.872	0.872	0.000	0.000	0.000	0.000
143	A	225	TYR	0	-0.027	-0.018	16.810	-0.063	-0.063	0.000	0.000	0.000	0.000
144	A	226	THR	0	0.051	0.011	15.835	0.572	0.572	0.000	0.000	0.000	0.000
145	A	227	GLY	0	0.026	0.042	18.115	-0.066	-0.066	0.000	0.000	0.000	0.000
146	A	228	LYS	1	0.887	0.945	18.996	16.309	16.309	0.000	0.000	0.000	0.000
147	A	229	SER	0	-0.002	-0.016	19.846	-0.451	-0.451	0.000	0.000	0.000	0.000
148	A	230	HIS	0	0.032	0.008	20.981	-0.165	-0.165	0.000	0.000	0.000	0.000
149	A	231	PHE	0	-0.017	0.001	11.719	0.254	0.254	0.000	0.000	0.000	0.000
150	A	232	MET	0	-0.010	-0.006	14.548	0.635	0.635	0.000	0.000	0.000	0.000
151	A	233	LEU	0	0.001	0.012	8.094	-0.204	-0.204	0.000	0.000	0.000	0.000
152	A	234	PRO	0	0.003	0.007	7.556	0.913	0.913	0.000	0.000	0.000	0.000
153	A	235	ASP	-1	-0.873	-0.939	7.206	-36.884	-36.884	0.000	0.000	0.000	0.000
160	A	242	GLN	0	-0.035	-0.031	6.878	2.536	2.536	0.000	0.000	0.000	0.000
163	A	245	TYR	0	-0.116	-0.088	6.936	3.544	3.544	0.000	0.000	0.000	0.000
164	A	246	GLY	-1	-0.907	-0.933	9.001	-18.901	-18.901	0.000	0.000	0.000	0.000

Top

Graph

Overview

Highlights

Data Search

Manual

Support

Interactive mode: IFIE and PIEDA for fragment #1(A:83:TYR)