FMO DATABASE

FMODB ID: NZN6Q

Calculation Name: 4J4F-A-Xray540

Preferred Name:

Target Type:

Ligand Name:

Ligand 3-letter code:

Ligand of Interest (LOI):

Structure Source: PDB

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	OptHSide
Protonation	MOE:Protonate 3D
Complement	MOE:Structure Preparation
Water	No
Procedure	Auto-FMO protocol ver. 2.20220422
Remarks

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	-568148.216561
FMO2-HF: Nuclear repulsion	528943.908416
FMO2-HF: Total energy	-39204.308145
FMO2-MP2: Total energy	-39315.929759

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: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.
-10.508	-7.557	0.689	-1.782	-1.858	0.01

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 : 0.084 / q_NPA : 0.004

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	0.038	0.005	3.814	0.148	1.547	-0.017	-0.707	-0.675	0.002
5	A	3	LYS	1	0.847	1.053	2.633	-12.490	-10.938	0.706	-1.075	-1.183	0.008
6	A	4	PHE	0	0.189	-0.047	6.417	0.322	0.322	0.000	0.000	0.000	0.000
7	A	4	PHE	0	-0.054	0.084	8.697	-0.052	-0.052	0.000	0.000	0.000	0.000
8	A	5	SER	0	0.051	-0.077	9.062	0.062	0.062	0.000	0.000	0.000	0.000
9	A	5	SER	0	-0.027	0.077	11.129	-0.020	-0.020	0.000	0.000	0.000	0.000
10	A	6	GLN	0	0.011	-0.092	10.289	-0.149	-0.149	0.000	0.000	0.000	0.000
11	A	6	GLN	0	-0.077	0.065	8.563	0.345	0.345	0.000	0.000	0.000	0.000
12	A	7	THR	0	0.008	-0.064	11.746	-0.046	-0.046	0.000	0.000	0.000	0.000
13	A	7	THR	0	-0.034	0.076	11.411	0.096	0.096	0.000	0.000	0.000	0.000
14	A	8	CYS	0	0.041	-0.112	13.279	-0.040	-0.040	0.000	0.000	0.000	0.000
15	A	8	CYS	0	-0.211	0.192	12.804	-0.025	-0.025	0.000	0.000	0.000	0.000
16	A	9	TYR	0	0.117	-0.041	14.859	0.020	0.020	0.000	0.000	0.000	0.000
17	A	9	TYR	0	-0.056	0.077	18.510	-0.015	-0.015	0.000	0.000	0.000	0.000
18	A	10	ASN	0	0.088	-0.055	18.123	-0.020	-0.020	0.000	0.000	0.000	0.000
19	A	10	ASN	0	-0.106	0.052	21.264	0.006	0.006	0.000	0.000	0.000	0.000
20	A	11	SER	0	0.078	-0.084	17.073	-0.014	-0.014	0.000	0.000	0.000	0.000
21	A	11	SER	0	-0.044	0.037	16.184	0.008	0.008	0.000	0.000	0.000	0.000
22	A	12	ALA	0	0.060	-0.092	18.320	0.009	0.009	0.000	0.000	0.000	0.000
23	A	12	ALA	0	-0.069	0.111	21.602	0.002	0.002	0.000	0.000	0.000	0.000
24	A	13	ILE	0	0.072	-0.105	19.117	-0.010	-0.010	0.000	0.000	0.000	0.000
25	A	13	ILE	0	-0.071	0.112	16.400	-0.006	-0.006	0.000	0.000	0.000	0.000
26	A	14	GLN	0	0.087	-0.099	20.377	0.019	0.019	0.000	0.000	0.000	0.000
27	A	14	GLN	0	-0.097	0.107	23.755	0.005	0.005	0.000	0.000	0.000	0.000
28	A	15	GLY	0	-0.023	-0.115	22.539	-0.009	-0.009	0.000	0.000	0.000	0.000
29	A	16	SER	0	0.029	0.006	19.956	-0.005	-0.005	0.000	0.000	0.000	0.000
30	A	16	SER	0	-0.017	0.066	19.424	0.015	0.015	0.000	0.000	0.000	0.000
31	A	17	VAL	0	0.051	-0.101	18.280	-0.072	-0.072	0.000	0.000	0.000	0.000
32	A	17	VAL	0	-0.101	0.105	19.331	0.007	0.007	0.000	0.000	0.000	0.000
33	A	18	LEU	0	0.160	-0.085	15.734	0.050	0.050	0.000	0.000	0.000	0.000
34	A	18	LEU	0	-0.139	0.096	12.957	-0.017	-0.017	0.000	0.000	0.000	0.000
35	A	19	THR	0	0.040	-0.074	17.137	-0.012	-0.012	0.000	0.000	0.000	0.000
36	A	19	THR	0	-0.031	0.083	19.966	-0.004	-0.004	0.000	0.000	0.000	0.000
37	A	20	SER	0	0.090	-0.059	15.729	-0.003	-0.003	0.000	0.000	0.000	0.000
38	A	20	SER	0	0.002	0.084	14.744	0.012	0.012	0.000	0.000	0.000	0.000
39	A	21	THR	0	0.030	-0.076	17.172	-0.015	-0.015	0.000	0.000	0.000	0.000
40	A	21	THR	0	-0.049	0.099	19.650	-0.006	-0.006	0.000	0.000	0.000	0.000
41	A	22	CYS	0	0.059	-0.148	14.467	0.027	0.027	0.000	0.000	0.000	0.000
42	A	23	GLU	0	0.171	-0.087	15.087	-0.078	-0.078	0.000	0.000	0.000	0.000
43	A	23	GLU	-1	-0.938	-0.779	14.901	0.571	0.571	0.000	0.000	0.000	0.000
44	A	24	ARG	0	0.025	-0.116	14.497	0.069	0.069	0.000	0.000	0.000	0.000
45	A	24	ARG	1	0.843	1.059	17.679	-0.231	-0.231	0.000	0.000	0.000	0.000
46	A	25	THR	0	0.080	-0.080	15.304	0.026	0.026	0.000	0.000	0.000	0.000
47	A	25	THR	0	-0.055	0.055	13.369	-0.014	-0.014	0.000	0.000	0.000	0.000
48	A	26	ASN	0	0.005	-0.049	15.918	0.028	0.028	0.000	0.000	0.000	0.000
49	A	26	ASN	0	-0.122	0.059	18.908	0.032	0.032	0.000	0.000	0.000	0.000
50	A	27	GLY	0	0.089	-0.068	18.786	-0.036	-0.036	0.000	0.000	0.000	0.000
51	A	28	GLY	0	0.003	-0.006	20.503	-0.033	-0.033	0.000	0.000	0.000	0.000
52	A	29	TYR	0	0.056	-0.003	18.894	0.047	0.047	0.000	0.000	0.000	0.000
53	A	29	TYR	0	-0.122	0.050	17.569	-0.033	-0.033	0.000	0.000	0.000	0.000
54	A	30	ASN	0	0.129	-0.072	18.301	-0.027	-0.027	0.000	0.000	0.000	0.000
55	A	30	ASN	0	-0.145	0.054	17.677	-0.001	-0.001	0.000	0.000	0.000	0.000
56	A	31	THR	0	0.032	-0.092	17.919	0.025	0.025	0.000	0.000	0.000	0.000
57	A	31	THR	0	-0.029	0.088	20.291	0.003	0.003	0.000	0.000	0.000	0.000
58	A	32	SER	0	-0.076	-0.082	16.914	-0.002	-0.002	0.000	0.000	0.000	0.000
59	A	32	SER	0	-0.023	0.061	15.753	-0.005	-0.005	0.000	0.000	0.000	0.000
60	A	33	SER	0	0.064	-0.109	17.529	0.011	0.011	0.000	0.000	0.000	0.000
61	A	33	SER	0	-0.034	0.073	19.290	0.011	0.011	0.000	0.000	0.000	0.000
62	A	34	ILE	0	0.069	-0.078	14.313	0.030	0.030	0.000	0.000	0.000	0.000
63	A	34	ILE	0	-0.102	0.090	11.681	-0.015	-0.015	0.000	0.000	0.000	0.000
64	A	35	ASP	0	0.105	-0.108	15.861	0.000	0.000	0.000	0.000	0.000	0.000
65	A	35	ASP	-1	-0.873	-0.778	18.219	-0.385	-0.385	0.000	0.000	0.000	0.000
66	A	36	LEU	0	0.030	-0.132	14.499	-0.067	-0.067	0.000	0.000	0.000	0.000
67	A	36	LEU	0	-0.089	0.103	12.637	-0.016	-0.016	0.000	0.000	0.000	0.000
68	A	37	ASN	0	0.128	-0.058	15.446	-0.088	-0.088	0.000	0.000	0.000	0.000
69	A	37	ASN	0	-0.120	0.057	19.594	0.007	0.007	0.000	0.000	0.000	0.000
70	A	38	SER	0	0.046	-0.071	16.931	0.012	0.012	0.000	0.000	0.000	0.000
71	A	38	SER	0	-0.059	0.056	16.131	-0.022	-0.022	0.000	0.000	0.000	0.000
72	A	39	VAL	0	0.035	-0.082	12.251	0.026	0.026	0.000	0.000	0.000	0.000
73	A	39	VAL	0	-0.103	0.081	11.322	-0.051	-0.051	0.000	0.000	0.000	0.000
74	A	40	ILE	0	0.133	-0.065	12.599	-0.217	-0.217	0.000	0.000	0.000	0.000
75	A	40	ILE	0	-0.093	0.069	12.266	0.006	0.006	0.000	0.000	0.000	0.000
76	A	41	GLU	0	0.059	-0.113	14.737	0.074	0.074	0.000	0.000	0.000	0.000
77	A	41	GLU	-1	-0.901	-0.805	16.361	-0.648	-0.648	0.000	0.000	0.000	0.000
78	A	42	ASN	0	0.110	-0.081	17.839	-0.041	-0.041	0.000	0.000	0.000	0.000
79	A	42	ASN	0	-0.137	0.063	21.672	-0.001	-0.001	0.000	0.000	0.000	0.000
80	A	43	VAL	0	0.074	-0.098	19.926	0.031	0.031	0.000	0.000	0.000	0.000
81	A	43	VAL	0	-0.083	0.098	18.407	-0.010	-0.010	0.000	0.000	0.000	0.000
82	A	44	ASP	0	0.047	-0.106	21.057	-0.010	-0.010	0.000	0.000	0.000	0.000
83	A	44	ASP	-1	-0.985	-0.833	23.516	-0.338	-0.338	0.000	0.000	0.000	0.000
84	A	45	GLY	0	0.026	-0.124	23.499	0.024	0.024	0.000	0.000	0.000	0.000
85	A	46	SER	0	-0.016	-0.016	19.767	0.022	0.022	0.000	0.000	0.000	0.000
86	A	46	SER	0	-0.027	0.045	18.722	-0.009	-0.009	0.000	0.000	0.000	0.000
87	A	47	LEU	0	0.089	-0.062	17.234	-0.011	-0.011	0.000	0.000	0.000	0.000
88	A	47	LEU	0	-0.077	0.106	16.408	-0.002	-0.002	0.000	0.000	0.000	0.000
89	A	48	LYS	0	-0.028	-0.158	14.240	-0.029	-0.029	0.000	0.000	0.000	0.000
90	A	48	LYS	1	0.913	1.098	14.884	0.589	0.589	0.000	0.000	0.000	0.000
91	A	49	TRP	0	0.104	-0.049	10.592	0.105	0.105	0.000	0.000	0.000	0.000
92	A	49	TRP	0	-0.171	0.042	8.811	-0.246	-0.246	0.000	0.000	0.000	0.000
93	A	50	GLN	0	0.143	-0.090	12.042	0.016	0.016	0.000	0.000	0.000	0.000
94	A	50	GLN	0	-0.157	0.094	13.714	0.002	0.002	0.000	0.000	0.000	0.000
95	A	51	GLY	0	-0.056	-0.123	12.608	-0.204	-0.204	0.000	0.000	0.000	0.000
96	A	52	SER	0	0.057	0.039	14.576	0.006	0.006	0.000	0.000	0.000	0.000
97	A	52	SER	0	-0.062	0.027	14.605	-0.033	-0.033	0.000	0.000	0.000	0.000
98	A	53	ASN	0	0.144	-0.076	16.164	0.022	0.022	0.000	0.000	0.000	0.000
99	A	53	ASN	0	-0.155	0.066	20.041	-0.001	-0.001	0.000	0.000	0.000	0.000
100	A	54	PHE	0	0.127	-0.071	19.806	-0.019	-0.019	0.000	0.000	0.000	0.000
101	A	54	PHE	0	-0.023	0.090	21.532	0.004	0.004	0.000	0.000	0.000	0.000
102	A	55	ILE	0	0.066	-0.120	21.372	0.002	0.002	0.000	0.000	0.000	0.000
103	A	55	ILE	0	-0.069	0.127	23.735	0.001	0.001	0.000	0.000	0.000	0.000
104	A	56	GLU	0	0.063	-0.136	20.709	0.035	0.035	0.000	0.000	0.000	0.000
105	A	56	GLU	-1	-0.928	-0.811	19.650	-0.473	-0.473	0.000	0.000	0.000	0.000
106	A	57	THR	0	-0.067	-0.068	17.804	0.025	0.025	0.000	0.000	0.000	0.000
107	A	57	THR	0	-0.075	0.052	16.158	-0.038	-0.038	0.000	0.000	0.000	0.000
108	A	58	CYS	0	0.072	-0.102	19.140	-0.041	-0.041	0.000	0.000	0.000	0.000
109	A	58	CYS	0	-0.196	0.224	18.767	-0.009	-0.009	0.000	0.000	0.000	0.000
110	A	59	ARG	0	0.074	-0.060	21.826	0.011	0.011	0.000	0.000	0.000	0.000
111	A	59	ARG	1	0.772	0.978	23.906	0.269	0.269	0.000	0.000	0.000	0.000
112	A	60	ASN	0	0.026	-0.066	25.165	-0.010	-0.010	0.000	0.000	0.000	0.000
113	A	60	ASN	0	-0.144	0.029	27.754	0.006	0.006	0.000	0.000	0.000	0.000
114	A	61	THR	0	0.158	-0.072	28.142	0.004	0.004	0.000	0.000	0.000	0.000
115	A	61	THR	0	-0.036	0.069	26.376	-0.005	-0.005	0.000	0.000	0.000	0.000
116	A	62	GLN	0	0.003	-0.082	28.707	0.011	0.011	0.000	0.000	0.000	0.000
117	A	62	GLN	0	-0.099	0.060	30.412	0.014	0.014	0.000	0.000	0.000	0.000
118	A	63	LEU	0	0.145	-0.089	31.190	-0.017	-0.017	0.000	0.000	0.000	0.000
119	A	63	LEU	0	-0.083	0.124	33.684	0.001	0.001	0.000	0.000	0.000	0.000
120	A	64	ALA	0	0.032	-0.107	33.020	0.011	0.011	0.000	0.000	0.000	0.000
121	A	64	ALA	0	-0.093	0.091	32.318	-0.002	-0.002	0.000	0.000	0.000	0.000
122	A	65	GLY	0	-0.022	-0.121	34.202	-0.002	-0.002	0.000	0.000	0.000	0.000
123	A	66	SER	0	0.063	0.005	37.263	-0.001	-0.001	0.000	0.000	0.000	0.000
124	A	66	SER	0	-0.012	0.085	38.564	0.003	0.003	0.000	0.000	0.000	0.000
125	A	67	SER	0	-0.069	-0.103	35.410	0.002	0.002	0.000	0.000	0.000	0.000
126	A	67	SER	0	-0.033	0.090	35.005	0.001	0.001	0.000	0.000	0.000	0.000
127	A	68	GLU	0	0.149	-0.104	31.524	-0.010	-0.010	0.000	0.000	0.000	0.000
128	A	68	GLU	-1	-0.900	-0.784	30.762	-0.206	-0.206	0.000	0.000	0.000	0.000
129	A	69	LEU	0	0.132	-0.056	29.030	0.016	0.016	0.000	0.000	0.000	0.000
130	A	69	LEU	0	-0.125	0.083	26.916	-0.002	-0.002	0.000	0.000	0.000	0.000
131	A	70	ALA	0	0.088	-0.098	27.840	-0.020	-0.020	0.000	0.000	0.000	0.000
132	A	70	ALA	0	-0.086	0.085	29.250	0.004	0.004	0.000	0.000	0.000	0.000
133	A	71	ALA	0	0.083	-0.076	25.206	0.016	0.016	0.000	0.000	0.000	0.000
134	A	71	ALA	0	-0.060	0.071	24.366	-0.006	-0.006	0.000	0.000	0.000	0.000
135	A	72	GLU	0	0.071	-0.091	23.389	-0.002	-0.002	0.000	0.000	0.000	0.000
136	A	72	GLU	-1	-0.903	-0.786	23.513	-0.245	-0.245	0.000	0.000	0.000	0.000
137	A	73	CYS	0	0.090	-0.148	19.733	0.019	0.019	0.000	0.000	0.000	0.000
138	A	74	LYS	0	0.158	-0.073	17.088	0.014	0.014	0.000	0.000	0.000	0.000
139	A	74	LYS	1	0.757	1.043	15.198	0.509	0.509	0.000	0.000	0.000	0.000
140	A	75	THR	0	0.029	-0.094	14.121	-0.077	-0.077	0.000	0.000	0.000	0.000
141	A	75	THR	0	-0.060	0.069	13.674	-0.017	-0.017	0.000	0.000	0.000	0.000
142	A	76	ARG	0	0.104	-0.059	9.340	0.119	0.119	0.000	0.000	0.000	0.000
143	A	76	ARG	1	0.896	1.070	6.629	2.496	2.496	0.000	0.000	0.000	0.000
144	A	77	ALA	0	0.087	-0.103	10.122	-0.153	-0.153	0.000	0.000	0.000	0.000
145	A	77	ALA	0	-0.064	0.107	12.275	0.020	0.020	0.000	0.000	0.000	0.000
146	A	78	GLN	0	-0.050	-0.121	12.278	0.107	0.107	0.000	0.000	0.000	0.000
147	A	78	GLN	0	-0.011	0.114	11.546	0.118	0.118	0.000	0.000	0.000	0.000
148	A	79	GLN	0	0.110	-0.096	14.780	0.070	0.070	0.000	0.000	0.000	0.000
149	A	79	GLN	0	-0.039	0.118	17.003	0.011	0.011	0.000	0.000	0.000	0.000
150	A	80	PHE	0	0.088	-0.090	17.452	-0.074	-0.074	0.000	0.000	0.000	0.000
151	A	80	PHE	0	-0.076	0.086	20.986	0.005	0.005	0.000	0.000	0.000	0.000
152	A	81	VAL	0	0.030	-0.123	19.993	0.042	0.042	0.000	0.000	0.000	0.000
153	A	81	VAL	0	-0.056	0.111	18.562	-0.005	-0.005	0.000	0.000	0.000	0.000
154	A	82	SER	0	0.098	-0.074	21.048	-0.022	-0.022	0.000	0.000	0.000	0.000
155	A	82	SER	0	-0.021	0.083	25.184	0.009	0.009	0.000	0.000	0.000	0.000
156	A	83	THR	0	-0.003	-0.056	22.550	-0.006	-0.006	0.000	0.000	0.000	0.000
157	A	83	THR	0	-0.061	0.054	21.567	0.003	0.003	0.000	0.000	0.000	0.000
158	A	84	LYS	0	0.069	-0.123	23.882	0.010	0.010	0.000	0.000	0.000	0.000
159	A	84	LYS	1	0.769	1.005	27.602	0.207	0.207	0.000	0.000	0.000	0.000
160	A	85	ILE	0	0.077	-0.072	25.502	-0.015	-0.015	0.000	0.000	0.000	0.000
161	A	85	ILE	0	-0.066	0.111	24.311	-0.004	-0.004	0.000	0.000	0.000	0.000
162	A	86	ASN	0	0.122	-0.092	27.103	0.011	0.011	0.000	0.000	0.000	0.000
163	A	86	ASN	0	-0.105	0.080	30.356	0.008	0.008	0.000	0.000	0.000	0.000
164	A	87	LEU	0	0.081	-0.106	30.379	-0.011	-0.011	0.000	0.000	0.000	0.000
165	A	87	LEU	0	-0.085	0.087	29.655	-0.001	-0.001	0.000	0.000	0.000	0.000
166	A	88	ASP	0	0.110	-0.073	31.746	-0.003	-0.003	0.000	0.000	0.000	0.000
167	A	88	ASP	-1	-0.934	-0.840	34.671	-0.167	-0.167	0.000	0.000	0.000	0.000
168	A	89	ASP	0	0.078	-0.091	30.359	0.013	0.013	0.000	0.000	0.000	0.000
169	A	89	ASP	-1	-1.003	-0.849	28.898	-0.249	-0.249	0.000	0.000	0.000	0.000
170	A	90	HIS	0	-0.028	-0.104	30.675	0.006	0.006	0.000	0.000	0.000	0.000
171	A	90	HIS	1	0.810	1.006	28.167	0.252	0.252	0.000	0.000	0.000	0.000
172	A	91	ILE	0	0.090	-0.088	32.063	0.000	0.000	0.000	0.000	0.000	0.000
173	A	91	ILE	0	-0.088	0.101	30.987	-0.001	-0.001	0.000	0.000	0.000	0.000
174	A	92	ALA	0	0.174	-0.061	34.207	0.004	0.004	0.000	0.000	0.000	0.000
175	A	92	ALA	0	-0.059	0.102	37.203	0.001	0.001	0.000	0.000	0.000	0.000
176	A	93	ASN	0	0.130	-0.073	37.728	-0.004	-0.004	0.000	0.000	0.000	0.000
177	A	93	ASN	0	-0.133	0.062	41.512	0.001	0.001	0.000	0.000	0.000	0.000
178	A	94	ILE	0	0.051	-0.119	41.137	0.005	0.005	0.000	0.000	0.000	0.000
179	A	94	ILE	0	-0.126	0.101	39.958	0.000	0.000	0.000	0.000	0.000	0.000
180	A	95	ASP	0	0.084	-0.119	42.718	-0.001	-0.001	0.000	0.000	0.000	0.000
181	A	95	ASP	-1	-0.994	-0.835	46.555	-0.099	-0.099	0.000	0.000	0.000	0.000
182	A	96	GLY	0	-0.011	-0.122	45.094	0.003	0.003	0.000	0.000	0.000	0.000
183	A	97	THR	0	0.018	0.000	42.371	0.000	0.000	0.000	0.000	0.000	0.000
184	A	97	THR	0	-0.040	0.073	40.483	0.000	0.000	0.000	0.000	0.000	0.000
185	A	98	LEU	0	0.048	-0.086	38.073	0.001	0.001	0.000	0.000	0.000	0.000
186	A	98	LEU	0	-0.080	0.097	37.055	-0.001	-0.001	0.000	0.000	0.000	0.000
187	A	99	LYS	0	0.077	-0.106	36.443	-0.003	-0.003	0.000	0.000	0.000	0.000
188	A	99	LYS	1	0.751	1.009	36.500	0.169	0.169	0.000	0.000	0.000	0.000
189	A	100	TYR	0	0.143	-0.094	32.228	0.004	0.004	0.000	0.000	0.000	0.000
190	A	100	TYR	0	-0.103	0.102	28.085	-0.006	-0.006	0.000	0.000	0.000	0.000
191	A	101	GLU	0	-0.167	-0.156	32.588	-0.004	-0.004	0.000	0.000	0.000	0.000
192	A	101	GLU	-1	-0.747	-0.860	35.485	-0.164	-0.164	0.000	0.000	0.000	0.000

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