FMO DATABASE

FMODB ID: J4QK9

Calculation Name: 4J4F-A-Xray540

Preferred Name:

Target Type:

Ligand Name:

Ligand 3-letter code:

Ligand of Interest (LOI):

PDB ID: 4J4F

Chain ID: A

ChEMBL ID:

UniProt ID: P81180

Base Structure: X-ray

Registration Date: 2025-07-14

Reference: C. Watanabe, N. Tani, K. Kamisaka, T. Honma et al., Interaction energy analysis of Apo structure dataset on FMODB, To be published.

DOI:

Apendix: None

IFIE MAP

IFIE Diagram

Modeling method

Optimization	MOE:Amber10:EHT
Restraint	OptAll
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	192
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-567392.623175
FMO2-HF: Nuclear repulsion	528188.108361
FMO2-HF: Total energy	-39204.514814
FMO2-MP2: Total energy	-39316.112589

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:LEU)

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

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.
-23.935	-24.687	8.488	-4.073	-3.662	0.046

Interaction energy analysis for fragmet #1(A:1:LEU)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : 0.103 / q_NPA : -0.008

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].
4	A	3	LYS	0	0.014	0.011	3.885	-0.249	0.821	-0.011	-0.524	-0.534	0.001
5	A	3	LYS	1	0.828	1.021	2.142	-25.131	-26.953	8.499	-3.549	-3.128	0.045
6	A	4	PHE	0	0.201	-0.039	6.373	0.215	0.215	0.000	0.000	0.000	0.000
7	A	4	PHE	0	-0.047	0.077	8.589	-0.037	-0.037	0.000	0.000	0.000	0.000
8	A	5	SER	0	0.031	-0.060	9.050	0.011	0.011	0.000	0.000	0.000	0.000
9	A	5	SER	0	-0.034	0.060	10.828	0.034	0.034	0.000	0.000	0.000	0.000
10	A	6	GLN	0	0.041	-0.093	9.766	-0.084	-0.084	0.000	0.000	0.000	0.000
11	A	6	GLN	0	-0.067	0.070	7.451	0.519	0.519	0.000	0.000	0.000	0.000
12	A	7	THR	0	-0.021	-0.075	10.972	0.001	0.001	0.000	0.000	0.000	0.000
13	A	7	THR	0	-0.034	0.070	10.135	0.038	0.038	0.000	0.000	0.000	0.000
14	A	8	CYS	0	0.033	-0.114	12.439	-0.060	-0.060	0.000	0.000	0.000	0.000
15	A	8	CYS	0	-0.198	0.209	12.762	-0.041	-0.041	0.000	0.000	0.000	0.000
16	A	9	TYR	0	0.131	-0.028	14.803	0.040	0.040	0.000	0.000	0.000	0.000
17	A	9	TYR	0	-0.069	0.077	18.407	-0.008	-0.008	0.000	0.000	0.000	0.000
18	A	10	ASN	0	0.054	-0.062	18.169	-0.022	-0.022	0.000	0.000	0.000	0.000
19	A	10	ASN	0	-0.083	0.057	21.113	0.010	0.010	0.000	0.000	0.000	0.000
20	A	11	SER	0	0.070	-0.088	16.685	-0.023	-0.023	0.000	0.000	0.000	0.000
21	A	11	SER	0	-0.045	0.046	15.871	0.017	0.017	0.000	0.000	0.000	0.000
22	A	12	ALA	0	0.081	-0.084	18.012	0.021	0.021	0.000	0.000	0.000	0.000
23	A	12	ALA	0	-0.067	0.107	21.327	0.002	0.002	0.000	0.000	0.000	0.000
24	A	13	ILE	0	0.048	-0.114	18.695	-0.021	-0.021	0.000	0.000	0.000	0.000
25	A	13	ILE	0	-0.052	0.108	16.396	-0.003	-0.003	0.000	0.000	0.000	0.000
26	A	14	GLN	0	0.093	-0.085	20.145	0.022	0.022	0.000	0.000	0.000	0.000
27	A	14	GLN	0	-0.091	0.103	23.642	-0.001	-0.001	0.000	0.000	0.000	0.000
28	A	15	GLY	0	-0.014	-0.114	22.626	-0.015	-0.015	0.000	0.000	0.000	0.000
29	A	16	SER	0	0.030	0.002	19.906	0.006	0.006	0.000	0.000	0.000	0.000
30	A	16	SER	0	-0.028	0.063	19.368	0.012	0.012	0.000	0.000	0.000	0.000
31	A	17	VAL	0	0.066	-0.099	18.257	-0.062	-0.062	0.000	0.000	0.000	0.000
32	A	17	VAL	0	-0.107	0.108	19.189	0.004	0.004	0.000	0.000	0.000	0.000
33	A	18	LEU	0	0.166	-0.073	15.489	0.057	0.057	0.000	0.000	0.000	0.000
34	A	18	LEU	0	-0.119	0.096	12.643	-0.016	-0.016	0.000	0.000	0.000	0.000
35	A	19	THR	0	0.022	-0.106	16.974	-0.026	-0.026	0.000	0.000	0.000	0.000
36	A	19	THR	0	-0.024	0.095	19.570	0.004	0.004	0.000	0.000	0.000	0.000
37	A	20	SER	0	0.063	-0.069	15.468	0.016	0.016	0.000	0.000	0.000	0.000
38	A	20	SER	0	-0.001	0.079	14.405	0.012	0.012	0.000	0.000	0.000	0.000
39	A	21	THR	0	-0.025	-0.075	16.955	-0.027	-0.027	0.000	0.000	0.000	0.000
40	A	21	THR	0	-0.067	0.066	19.580	-0.001	-0.001	0.000	0.000	0.000	0.000
41	A	22	CYS	0	0.083	-0.125	14.140	0.040	0.040	0.000	0.000	0.000	0.000
42	A	23	GLU	0	0.170	-0.085	14.660	-0.048	-0.048	0.000	0.000	0.000	0.000
43	A	23	GLU	-1	-0.941	-0.795	14.332	0.297	0.297	0.000	0.000	0.000	0.000
44	A	24	ARG	0	0.023	-0.112	14.446	-0.004	-0.004	0.000	0.000	0.000	0.000
45	A	24	ARG	1	0.806	1.035	17.328	-0.024	-0.024	0.000	0.000	0.000	0.000
46	A	25	THR	0	0.034	-0.105	14.952	0.028	0.028	0.000	0.000	0.000	0.000
47	A	25	THR	0	-0.049	0.065	13.317	-0.013	-0.013	0.000	0.000	0.000	0.000
48	A	26	ASN	0	0.022	-0.050	15.734	0.026	0.026	0.000	0.000	0.000	0.000
49	A	26	ASN	0	-0.089	0.071	18.822	-0.002	-0.002	0.000	0.000	0.000	0.000
50	A	27	GLY	0	0.075	-0.067	18.589	-0.009	-0.009	0.000	0.000	0.000	0.000
51	A	28	GLY	0	-0.003	-0.011	20.293	-0.022	-0.022	0.000	0.000	0.000	0.000
52	A	29	TYR	0	0.054	-0.002	18.647	0.020	0.020	0.000	0.000	0.000	0.000
53	A	29	TYR	0	-0.104	0.055	17.325	-0.017	-0.017	0.000	0.000	0.000	0.000
54	A	30	ASN	0	0.139	-0.094	18.179	-0.008	-0.008	0.000	0.000	0.000	0.000
55	A	30	ASN	0	-0.142	0.072	17.352	0.007	0.007	0.000	0.000	0.000	0.000
56	A	31	THR	0	0.026	-0.066	17.678	0.001	0.001	0.000	0.000	0.000	0.000
57	A	31	THR	0	-0.011	0.085	20.399	0.008	0.008	0.000	0.000	0.000	0.000
58	A	32	SER	0	-0.042	-0.078	16.507	0.005	0.005	0.000	0.000	0.000	0.000
59	A	32	SER	0	-0.007	0.076	15.469	-0.017	-0.017	0.000	0.000	0.000	0.000
60	A	33	SER	0	0.041	-0.108	17.012	0.012	0.012	0.000	0.000	0.000	0.000
61	A	33	SER	0	-0.012	0.073	18.828	0.012	0.012	0.000	0.000	0.000	0.000
62	A	34	ILE	0	0.066	-0.075	14.177	0.015	0.015	0.000	0.000	0.000	0.000
63	A	34	ILE	0	-0.084	0.096	11.672	-0.015	-0.015	0.000	0.000	0.000	0.000
64	A	35	ASP	0	0.098	-0.105	15.726	0.007	0.007	0.000	0.000	0.000	0.000
65	A	35	ASP	-1	-0.868	-0.768	18.399	-0.345	-0.345	0.000	0.000	0.000	0.000
66	A	36	LEU	0	0.080	-0.123	14.669	-0.067	-0.067	0.000	0.000	0.000	0.000
67	A	36	LEU	0	-0.090	0.105	12.850	-0.009	-0.009	0.000	0.000	0.000	0.000
68	A	37	ASN	0	0.145	-0.056	15.636	-0.064	-0.064	0.000	0.000	0.000	0.000
69	A	37	ASN	0	-0.109	0.059	19.925	0.014	0.014	0.000	0.000	0.000	0.000
70	A	38	SER	0	-0.030	-0.095	17.035	0.024	0.024	0.000	0.000	0.000	0.000
71	A	38	SER	0	-0.041	0.079	16.144	-0.025	-0.025	0.000	0.000	0.000	0.000
72	A	39	VAL	0	0.011	-0.105	12.462	0.013	0.013	0.000	0.000	0.000	0.000
73	A	39	VAL	0	-0.099	0.082	11.486	-0.046	-0.046	0.000	0.000	0.000	0.000
74	A	40	ILE	0	0.110	-0.079	12.555	-0.176	-0.176	0.000	0.000	0.000	0.000
75	A	40	ILE	0	-0.095	0.072	11.991	0.008	0.008	0.000	0.000	0.000	0.000
76	A	41	GLU	0	0.071	-0.091	14.717	0.052	0.052	0.000	0.000	0.000	0.000
77	A	41	GLU	-1	-0.917	-0.823	16.393	-0.496	-0.496	0.000	0.000	0.000	0.000
78	A	42	ASN	0	0.087	-0.089	17.765	-0.015	-0.015	0.000	0.000	0.000	0.000
79	A	42	ASN	0	-0.114	0.057	21.277	0.006	0.006	0.000	0.000	0.000	0.000
80	A	43	VAL	0	0.081	-0.092	20.152	0.013	0.013	0.000	0.000	0.000	0.000
81	A	43	VAL	0	-0.072	0.105	18.783	-0.006	-0.006	0.000	0.000	0.000	0.000
82	A	44	ASP	0	0.023	-0.108	21.324	0.002	0.002	0.000	0.000	0.000	0.000
83	A	44	ASP	-1	-0.976	-0.838	24.053	-0.201	-0.201	0.000	0.000	0.000	0.000
84	A	45	GLY	0	0.035	-0.114	23.855	0.020	0.020	0.000	0.000	0.000	0.000
85	A	46	SER	0	0.071	0.015	20.627	0.017	0.017	0.000	0.000	0.000	0.000
86	A	46	SER	0	-0.074	0.078	19.825	-0.010	-0.010	0.000	0.000	0.000	0.000
87	A	47	LEU	0	0.099	-0.091	17.407	-0.020	-0.020	0.000	0.000	0.000	0.000
88	A	47	LEU	0	-0.065	0.107	16.541	0.002	0.002	0.000	0.000	0.000	0.000
89	A	48	LYS	0	-0.051	-0.148	14.303	0.023	0.023	0.000	0.000	0.000	0.000
90	A	48	LYS	1	0.863	1.053	14.892	0.340	0.340	0.000	0.000	0.000	0.000
91	A	49	TRP	0	0.113	-0.065	10.520	0.072	0.072	0.000	0.000	0.000	0.000
92	A	49	TRP	0	-0.143	0.054	8.774	-0.231	-0.231	0.000	0.000	0.000	0.000
93	A	50	GLN	0	0.118	-0.078	11.994	0.031	0.031	0.000	0.000	0.000	0.000
94	A	50	GLN	0	-0.118	0.099	13.612	0.000	0.000	0.000	0.000	0.000	0.000
95	A	51	GLY	0	-0.055	-0.130	12.481	-0.174	-0.174	0.000	0.000	0.000	0.000
96	A	52	SER	0	0.017	0.010	14.592	-0.062	-0.062	0.000	0.000	0.000	0.000
97	A	52	SER	0	0.008	0.071	15.045	-0.015	-0.015	0.000	0.000	0.000	0.000
98	A	53	ASN	0	0.097	-0.069	16.714	0.021	0.021	0.000	0.000	0.000	0.000
99	A	53	ASN	0	-0.131	0.064	20.715	-0.001	-0.001	0.000	0.000	0.000	0.000
100	A	54	PHE	0	0.152	-0.060	20.451	-0.014	-0.014	0.000	0.000	0.000	0.000
101	A	54	PHE	0	-0.043	0.082	21.905	0.004	0.004	0.000	0.000	0.000	0.000
102	A	55	ILE	0	0.038	-0.119	21.708	0.004	0.004	0.000	0.000	0.000	0.000
103	A	55	ILE	0	-0.072	0.117	23.983	0.001	0.001	0.000	0.000	0.000	0.000
104	A	56	GLU	0	0.051	-0.132	20.853	0.031	0.031	0.000	0.000	0.000	0.000
105	A	56	GLU	-1	-0.917	-0.808	20.081	-0.402	-0.402	0.000	0.000	0.000	0.000
106	A	57	THR	0	-0.045	-0.080	17.989	0.004	0.004	0.000	0.000	0.000	0.000
107	A	57	THR	0	-0.072	0.039	16.312	0.009	0.009	0.000	0.000	0.000	0.000
108	A	58	CYS	0	0.038	-0.106	19.308	-0.023	-0.023	0.000	0.000	0.000	0.000
109	A	58	CYS	0	-0.185	0.227	18.934	-0.004	-0.004	0.000	0.000	0.000	0.000
110	A	59	ARG	0	0.097	-0.047	22.047	0.004	0.004	0.000	0.000	0.000	0.000
111	A	59	ARG	1	0.770	0.983	24.150	0.206	0.206	0.000	0.000	0.000	0.000
112	A	60	ASN	0	0.062	-0.067	25.464	-0.006	-0.006	0.000	0.000	0.000	0.000
113	A	60	ASN	0	-0.135	0.036	28.012	0.001	0.001	0.000	0.000	0.000	0.000
114	A	61	THR	0	0.110	-0.080	28.165	0.009	0.009	0.000	0.000	0.000	0.000
115	A	61	THR	0	-0.054	0.064	26.252	-0.006	-0.006	0.000	0.000	0.000	0.000
116	A	62	GLN	0	0.023	-0.068	28.707	0.004	0.004	0.000	0.000	0.000	0.000
117	A	62	GLN	0	-0.113	0.052	30.644	0.011	0.011	0.000	0.000	0.000	0.000
118	A	63	LEU	0	0.159	-0.088	31.278	-0.011	-0.011	0.000	0.000	0.000	0.000
119	A	63	LEU	0	-0.085	0.114	33.859	0.000	0.000	0.000	0.000	0.000	0.000
120	A	64	ALA	0	0.027	-0.108	33.420	0.005	0.005	0.000	0.000	0.000	0.000
121	A	64	ALA	0	-0.083	0.094	32.644	-0.001	-0.001	0.000	0.000	0.000	0.000
122	A	65	GLY	0	-0.006	-0.114	34.552	-0.001	-0.001	0.000	0.000	0.000	0.000
123	A	66	SER	0	0.035	-0.006	37.401	-0.001	-0.001	0.000	0.000	0.000	0.000
124	A	66	SER	0	-0.023	0.084	38.132	0.003	0.003	0.000	0.000	0.000	0.000
125	A	67	SER	0	-0.034	-0.103	35.501	0.000	0.000	0.000	0.000	0.000	0.000
126	A	67	SER	0	-0.013	0.076	35.207	0.002	0.002	0.000	0.000	0.000	0.000
127	A	68	GLU	0	0.104	-0.088	31.598	-0.007	-0.007	0.000	0.000	0.000	0.000
128	A	68	GLU	-1	-0.905	-0.798	30.964	-0.120	-0.120	0.000	0.000	0.000	0.000
129	A	69	LEU	0	0.160	-0.054	29.192	0.009	0.009	0.000	0.000	0.000	0.000
130	A	69	LEU	0	-0.113	0.090	27.065	-0.002	-0.002	0.000	0.000	0.000	0.000
131	A	70	ALA	0	0.072	-0.104	27.853	-0.012	-0.012	0.000	0.000	0.000	0.000
132	A	70	ALA	0	-0.078	0.089	29.359	0.003	0.003	0.000	0.000	0.000	0.000
133	A	71	ALA	0	0.096	-0.074	25.368	0.010	0.010	0.000	0.000	0.000	0.000
134	A	71	ALA	0	-0.053	0.079	24.555	-0.005	-0.005	0.000	0.000	0.000	0.000
135	A	72	GLU	0	0.043	-0.100	23.559	0.006	0.006	0.000	0.000	0.000	0.000
136	A	72	GLU	-1	-0.891	-0.786	23.744	-0.176	-0.176	0.000	0.000	0.000	0.000
137	A	73	CYS	0	0.085	-0.144	19.893	0.007	0.007	0.000	0.000	0.000	0.000
138	A	74	LYS	0	0.126	-0.084	17.215	0.025	0.025	0.000	0.000	0.000	0.000
139	A	74	LYS	1	0.739	1.017	15.145	0.451	0.451	0.000	0.000	0.000	0.000
140	A	75	THR	0	0.039	-0.098	14.376	-0.068	-0.068	0.000	0.000	0.000	0.000
141	A	75	THR	0	-0.093	0.050	13.715	-0.011	-0.011	0.000	0.000	0.000	0.000
142	A	76	ARG	0	0.119	-0.053	9.520	0.066	0.066	0.000	0.000	0.000	0.000
143	A	76	ARG	1	0.881	1.064	7.118	1.808	1.808	0.000	0.000	0.000	0.000
144	A	77	ALA	0	0.084	-0.102	10.527	-0.140	-0.140	0.000	0.000	0.000	0.000
145	A	77	ALA	0	-0.060	0.112	11.885	0.022	0.022	0.000	0.000	0.000	0.000
146	A	78	GLN	0	-0.009	-0.117	12.116	0.096	0.096	0.000	0.000	0.000	0.000
147	A	78	GLN	0	-0.024	0.121	11.533	0.107	0.107	0.000	0.000	0.000	0.000
148	A	79	GLN	0	0.133	-0.075	14.714	0.023	0.023	0.000	0.000	0.000	0.000
149	A	79	GLN	0	-0.026	0.116	17.192	0.005	0.005	0.000	0.000	0.000	0.000
150	A	80	PHE	0	0.060	-0.085	17.236	-0.060	-0.060	0.000	0.000	0.000	0.000
151	A	80	PHE	0	-0.056	0.087	20.876	0.001	0.001	0.000	0.000	0.000	0.000
152	A	81	VAL	0	0.027	-0.117	19.986	0.033	0.033	0.000	0.000	0.000	0.000
153	A	81	VAL	0	-0.050	0.114	18.588	0.000	0.000	0.000	0.000	0.000	0.000
154	A	82	SER	0	0.088	-0.079	21.087	-0.025	-0.025	0.000	0.000	0.000	0.000
155	A	82	SER	0	-0.020	0.083	25.324	0.008	0.008	0.000	0.000	0.000	0.000
156	A	83	THR	0	-0.028	-0.055	22.469	0.005	0.005	0.000	0.000	0.000	0.000
157	A	83	THR	0	-0.054	0.043	21.351	0.004	0.004	0.000	0.000	0.000	0.000
158	A	84	LYS	0	0.081	-0.112	23.851	0.004	0.004	0.000	0.000	0.000	0.000
159	A	84	LYS	1	0.750	0.995	27.009	0.128	0.128	0.000	0.000	0.000	0.000
160	A	85	ILE	0	0.063	-0.079	25.204	-0.007	-0.007	0.000	0.000	0.000	0.000
161	A	85	ILE	0	-0.069	0.106	24.260	-0.004	-0.004	0.000	0.000	0.000	0.000
162	A	86	ASN	0	0.106	-0.097	27.024	0.003	0.003	0.000	0.000	0.000	0.000
163	A	86	ASN	0	-0.110	0.072	30.522	0.003	0.003	0.000	0.000	0.000	0.000
164	A	87	LEU	0	0.069	-0.096	30.116	-0.010	-0.010	0.000	0.000	0.000	0.000
165	A	87	LEU	0	-0.082	0.094	30.086	-0.001	-0.001	0.000	0.000	0.000	0.000
166	A	88	ASP	0	0.132	-0.072	32.033	-0.005	-0.005	0.000	0.000	0.000	0.000
167	A	88	ASP	-1	-0.916	-0.827	35.128	-0.106	-0.106	0.000	0.000	0.000	0.000
168	A	89	ASP	0	0.072	-0.111	30.594	0.009	0.009	0.000	0.000	0.000	0.000
169	A	89	ASP	-1	-0.957	-0.826	29.248	-0.147	-0.147	0.000	0.000	0.000	0.000
170	A	90	HIS	0	-0.043	-0.093	30.592	0.002	0.002	0.000	0.000	0.000	0.000
171	A	90	HIS	1	0.801	1.010	28.089	0.164	0.164	0.000	0.000	0.000	0.000
172	A	91	ILE	0	0.084	-0.086	32.069	-0.002	-0.002	0.000	0.000	0.000	0.000
173	A	91	ILE	0	-0.071	0.103	31.261	-0.001	-0.001	0.000	0.000	0.000	0.000
174	A	92	ALA	0	0.146	-0.066	34.447	0.004	0.004	0.000	0.000	0.000	0.000
175	A	92	ALA	0	-0.059	0.101	37.683	0.001	0.001	0.000	0.000	0.000	0.000
176	A	93	ASN	0	0.135	-0.069	38.160	-0.004	-0.004	0.000	0.000	0.000	0.000
177	A	93	ASN	0	-0.125	0.064	41.891	0.000	0.000	0.000	0.000	0.000	0.000
178	A	94	ILE	0	0.032	-0.118	41.566	0.005	0.005	0.000	0.000	0.000	0.000
179	A	94	ILE	0	-0.127	0.097	40.196	0.000	0.000	0.000	0.000	0.000	0.000
180	A	95	ASP	0	0.085	-0.110	43.093	-0.002	-0.002	0.000	0.000	0.000	0.000
181	A	95	ASP	-1	-0.982	-0.840	47.156	-0.068	-0.068	0.000	0.000	0.000	0.000
182	A	96	GLY	0	0.003	-0.114	45.461	0.002	0.002	0.000	0.000	0.000	0.000
183	A	97	THR	0	0.010	-0.009	42.698	-0.002	-0.002	0.000	0.000	0.000	0.000
184	A	97	THR	0	-0.042	0.080	40.678	0.000	0.000	0.000	0.000	0.000	0.000
185	A	98	LEU	0	0.050	-0.092	38.606	0.002	0.002	0.000	0.000	0.000	0.000
186	A	98	LEU	0	-0.069	0.103	37.574	-0.001	-0.001	0.000	0.000	0.000	0.000
187	A	99	LYS	0	0.078	-0.099	36.664	-0.004	-0.004	0.000	0.000	0.000	0.000
188	A	99	LYS	1	0.740	0.986	36.238	0.121	0.121	0.000	0.000	0.000	0.000
189	A	100	TYR	0	0.125	-0.103	32.458	0.004	0.004	0.000	0.000	0.000	0.000
190	A	100	TYR	0	-0.091	0.106	28.523	-0.004	-0.004	0.000	0.000	0.000	0.000
191	A	101	GLU	0	-0.170	-0.162	32.362	-0.005	-0.005	0.000	0.000	0.000	0.000
192	A	101	GLU	-1	-0.737	-0.852	35.370	-0.114	-0.114	0.000	0.000	0.000	0.000

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