FMO DATABASE

FMODB ID: 82GVY

Calculation Name: 1DUS-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 1DUS

Chain ID: A

ChEMBL ID:

UniProt ID: Q58292

Base Structure: X-ray

Registration Date: 2023-03-13

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

DOI:

IFIE MAP

IFIE Diagram

Modeling method

Optimization	MOE:Amber10:EHT
Restraint	OptH
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	194
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-2219135.056998
FMO2-HF: Nuclear repulsion	2143825.539578
FMO2-HF: Total energy	-75309.51742
FMO2-MP2: Total energy	-75533.310933

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:4:PHE)

Summations of interaction energy for fragment #1(A:4:PHE)

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.
-7.045	-1.122	0.728	-3.063	-3.587	-0.007

Interaction energy analysis for fragmet #1(A:4:PHE)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : 0.060 / q_NPA : 0.036

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	6	GLU	-1	-0.876	-0.946	2.713	-11.845	-6.010	0.728	-3.040	-3.523	-0.007
4	A	7	LYS	1	0.876	0.934	4.269	1.434	1.522	0.000	-0.023	-0.064	0.000
5	A	8	PRO	0	0.025	0.015	7.868	0.056	0.056	0.000	0.000	0.000	0.000
6	A	9	THR	0	0.030	0.016	8.889	0.187	0.187	0.000	0.000	0.000	0.000
7	A	10	THR	0	-0.003	0.001	11.151	0.157	0.157	0.000	0.000	0.000	0.000
8	A	11	LYS	1	0.956	0.984	13.570	0.427	0.427	0.000	0.000	0.000	0.000
9	A	12	SER	0	0.022	0.008	15.764	-0.065	-0.065	0.000	0.000	0.000	0.000
10	A	13	ASP	-1	-0.859	-0.889	17.756	-0.390	-0.390	0.000	0.000	0.000	0.000
11	A	14	VAL	0	-0.023	-0.032	21.261	0.000	0.000	0.000	0.000	0.000	0.000
12	A	15	LYS	1	0.901	0.964	23.391	0.247	0.247	0.000	0.000	0.000	0.000
13	A	16	ILE	0	0.023	0.016	26.820	-0.005	-0.005	0.000	0.000	0.000	0.000
14	A	17	VAL	0	-0.052	-0.013	28.727	0.004	0.004	0.000	0.000	0.000	0.000
15	A	18	GLU	-1	-0.889	-0.940	31.213	-0.111	-0.111	0.000	0.000	0.000	0.000
16	A	19	ASP	-1	-0.867	-0.943	33.969	-0.102	-0.102	0.000	0.000	0.000	0.000
17	A	20	ILE	0	-0.050	-0.024	35.780	0.003	0.003	0.000	0.000	0.000	0.000
18	A	21	LEU	0	-0.042	-0.023	32.340	-0.002	-0.002	0.000	0.000	0.000	0.000
19	A	22	ARG	1	0.784	0.855	35.604	0.028	0.028	0.000	0.000	0.000	0.000
20	A	23	GLY	0	0.003	0.007	38.893	0.003	0.003	0.000	0.000	0.000	0.000
21	A	24	LYS	1	0.747	0.829	35.732	0.037	0.037	0.000	0.000	0.000	0.000
22	A	25	LYS	1	0.894	0.948	37.753	0.053	0.053	0.000	0.000	0.000	0.000
23	A	26	LEU	0	0.039	0.027	32.605	0.000	0.000	0.000	0.000	0.000	0.000
24	A	27	LYS	1	0.966	0.979	31.407	0.116	0.116	0.000	0.000	0.000	0.000
25	A	28	PHE	0	0.000	-0.005	27.256	-0.001	-0.001	0.000	0.000	0.000	0.000
26	A	29	LYS	1	0.853	0.926	22.301	0.278	0.278	0.000	0.000	0.000	0.000
27	A	30	THR	0	-0.044	-0.021	23.739	-0.008	-0.008	0.000	0.000	0.000	0.000
28	A	31	ASP	-1	-0.740	-0.895	18.183	-0.512	-0.512	0.000	0.000	0.000	0.000
29	A	32	SER	0	-0.039	-0.041	19.531	0.004	0.004	0.000	0.000	0.000	0.000
30	A	33	GLY	0	-0.008	0.009	16.253	-0.008	-0.008	0.000	0.000	0.000	0.000
31	A	34	VAL	0	-0.077	-0.048	16.594	-0.020	-0.020	0.000	0.000	0.000	0.000
32	A	35	PHE	0	0.012	0.003	19.180	0.010	0.010	0.000	0.000	0.000	0.000
33	A	36	SER	0	-0.041	-0.042	21.603	0.012	0.012	0.000	0.000	0.000	0.000
34	A	37	TYR	0	0.090	0.036	22.789	0.015	0.015	0.000	0.000	0.000	0.000
35	A	38	GLY	0	-0.031	-0.029	24.771	0.011	0.011	0.000	0.000	0.000	0.000
36	A	39	LYS	1	0.956	0.976	28.046	0.172	0.172	0.000	0.000	0.000	0.000
37	A	40	VAL	0	0.073	0.067	28.830	-0.008	-0.008	0.000	0.000	0.000	0.000
38	A	41	ASP	-1	-0.826	-0.916	27.789	-0.109	-0.109	0.000	0.000	0.000	0.000
39	A	42	LYS	1	0.975	0.970	29.901	0.106	0.106	0.000	0.000	0.000	0.000
40	A	43	GLY	0	0.053	0.032	30.979	0.009	0.009	0.000	0.000	0.000	0.000
41	A	44	THR	0	0.019	-0.014	27.916	0.010	0.010	0.000	0.000	0.000	0.000
42	A	45	LYS	1	0.848	0.934	30.186	0.105	0.105	0.000	0.000	0.000	0.000
43	A	46	ILE	0	-0.052	-0.010	33.555	0.007	0.007	0.000	0.000	0.000	0.000
44	A	47	LEU	0	0.001	-0.001	29.279	0.006	0.006	0.000	0.000	0.000	0.000
45	A	48	VAL	0	0.014	0.003	31.176	0.006	0.006	0.000	0.000	0.000	0.000
46	A	49	GLU	-1	-0.863	-0.912	33.647	-0.047	-0.047	0.000	0.000	0.000	0.000
47	A	50	ASN	0	-0.099	-0.067	36.610	0.007	0.007	0.000	0.000	0.000	0.000
48	A	51	VAL	0	-0.010	0.021	33.174	0.005	0.005	0.000	0.000	0.000	0.000
49	A	52	VAL	0	-0.002	0.007	36.088	-0.003	-0.003	0.000	0.000	0.000	0.000
50	A	53	VAL	0	-0.043	-0.032	34.090	0.005	0.005	0.000	0.000	0.000	0.000
51	A	54	ASP	-1	-0.825	-0.917	37.287	0.017	0.017	0.000	0.000	0.000	0.000
52	A	55	LYS	1	0.918	0.961	37.469	-0.016	-0.016	0.000	0.000	0.000	0.000
53	A	56	ASP	-1	-0.923	-0.962	37.883	0.028	0.028	0.000	0.000	0.000	0.000
54	A	57	ASP	-1	-0.882	-0.947	33.836	0.032	0.032	0.000	0.000	0.000	0.000
55	A	58	ASP	-1	-0.781	-0.850	30.069	0.055	0.055	0.000	0.000	0.000	0.000
56	A	59	ILE	0	-0.027	-0.035	28.601	0.006	0.006	0.000	0.000	0.000	0.000
57	A	60	LEU	0	-0.015	-0.009	21.811	0.001	0.001	0.000	0.000	0.000	0.000
58	A	61	ASP	-1	-0.835	-0.925	24.391	-0.062	-0.062	0.000	0.000	0.000	0.000
59	A	62	LEU	0	0.000	-0.017	19.624	-0.003	-0.003	0.000	0.000	0.000	0.000
60	A	63	GLY	0	-0.034	-0.007	18.812	-0.008	-0.008	0.000	0.000	0.000	0.000
61	A	64	CYS	0	-0.005	0.006	19.874	-0.015	-0.015	0.000	0.000	0.000	0.000
62	A	65	GLY	0	0.021	0.015	19.590	-0.012	-0.012	0.000	0.000	0.000	0.000
63	A	66	TYR	0	-0.090	-0.070	20.476	0.001	0.001	0.000	0.000	0.000	0.000
64	A	67	GLY	0	0.048	0.005	22.426	0.005	0.005	0.000	0.000	0.000	0.000
65	A	68	VAL	0	-0.044	-0.003	24.481	0.012	0.012	0.000	0.000	0.000	0.000
66	A	69	ILE	0	0.038	0.012	26.174	0.006	0.006	0.000	0.000	0.000	0.000
67	A	70	GLY	0	0.036	0.006	26.643	0.008	0.008	0.000	0.000	0.000	0.000
68	A	71	ILE	0	-0.034	-0.023	26.405	0.005	0.005	0.000	0.000	0.000	0.000
69	A	72	ALA	0	-0.022	-0.012	29.541	0.004	0.004	0.000	0.000	0.000	0.000
70	A	73	LEU	0	-0.001	-0.008	30.761	0.005	0.005	0.000	0.000	0.000	0.000
71	A	74	ALA	0	0.021	0.017	30.314	0.007	0.007	0.000	0.000	0.000	0.000
72	A	75	ASP	-1	-0.856	-0.895	32.215	-0.028	-0.028	0.000	0.000	0.000	0.000
73	A	76	GLU	-1	-0.803	-0.871	35.412	-0.022	-0.022	0.000	0.000	0.000	0.000
74	A	77	VAL	0	-0.085	-0.028	32.113	0.005	0.005	0.000	0.000	0.000	0.000
75	A	78	LYS	1	0.907	0.984	34.015	-0.050	-0.050	0.000	0.000	0.000	0.000
76	A	79	SER	0	-0.036	-0.047	29.648	0.002	0.002	0.000	0.000	0.000	0.000
77	A	80	THR	0	0.010	0.010	26.551	-0.002	-0.002	0.000	0.000	0.000	0.000
78	A	81	THR	0	-0.023	0.007	22.109	0.007	0.007	0.000	0.000	0.000	0.000
79	A	82	MET	0	-0.032	0.003	21.802	-0.010	-0.010	0.000	0.000	0.000	0.000
80	A	83	ALA	0	0.035	0.017	17.890	0.010	0.010	0.000	0.000	0.000	0.000
81	A	84	ASP	-1	-0.796	-0.901	15.816	-0.221	-0.221	0.000	0.000	0.000	0.000
82	A	85	ILE	0	0.101	0.060	9.903	0.000	0.000	0.000	0.000	0.000	0.000
83	A	86	ASN	0	-0.029	-0.014	11.016	-0.178	-0.178	0.000	0.000	0.000	0.000
84	A	87	ARG	1	1.032	0.990	6.513	0.859	0.859	0.000	0.000	0.000	0.000
85	A	88	ARG	1	0.836	0.924	12.577	0.542	0.542	0.000	0.000	0.000	0.000
86	A	89	ALA	0	0.021	0.006	15.315	0.048	0.048	0.000	0.000	0.000	0.000
87	A	90	ILE	0	0.023	0.026	14.592	0.034	0.034	0.000	0.000	0.000	0.000
88	A	91	LYS	1	0.907	0.947	15.910	0.489	0.489	0.000	0.000	0.000	0.000
89	A	92	LEU	0	0.008	-0.006	18.375	0.027	0.027	0.000	0.000	0.000	0.000
90	A	93	ALA	0	0.061	0.043	20.532	0.023	0.023	0.000	0.000	0.000	0.000
91	A	94	LYS	1	0.945	0.962	17.216	0.145	0.145	0.000	0.000	0.000	0.000
92	A	95	GLU	-1	-0.928	-0.955	21.781	-0.259	-0.259	0.000	0.000	0.000	0.000
93	A	96	ASN	0	0.019	0.000	24.504	0.010	0.010	0.000	0.000	0.000	0.000
94	A	97	ILE	0	0.041	0.041	24.775	0.009	0.009	0.000	0.000	0.000	0.000
95	A	98	LYS	1	0.957	0.982	24.871	0.129	0.129	0.000	0.000	0.000	0.000
96	A	99	LEU	0	-0.097	-0.045	27.912	0.004	0.004	0.000	0.000	0.000	0.000
97	A	100	ASN	0	-0.032	-0.028	29.932	0.006	0.006	0.000	0.000	0.000	0.000
98	A	101	ASN	0	-0.011	0.011	32.812	0.004	0.004	0.000	0.000	0.000	0.000
99	A	102	LEU	0	0.019	0.004	30.486	0.007	0.007	0.000	0.000	0.000	0.000
100	A	103	ASP	-1	-0.914	-0.978	29.918	-0.062	-0.062	0.000	0.000	0.000	0.000
101	A	104	ASN	0	-0.048	-0.009	31.788	0.003	0.003	0.000	0.000	0.000	0.000
102	A	105	TYR	0	0.007	0.016	32.094	0.006	0.006	0.000	0.000	0.000	0.000
103	A	106	ASP	-1	-0.908	-0.940	29.147	0.035	0.035	0.000	0.000	0.000	0.000
104	A	107	ILE	0	0.018	0.003	25.701	0.001	0.001	0.000	0.000	0.000	0.000
105	A	108	ARG	1	0.765	0.865	22.286	-0.112	-0.112	0.000	0.000	0.000	0.000
106	A	109	VAL	0	-0.029	-0.018	18.718	-0.006	-0.006	0.000	0.000	0.000	0.000
107	A	110	VAL	0	-0.044	-0.029	16.667	-0.003	-0.003	0.000	0.000	0.000	0.000
108	A	111	HIS	0	-0.095	-0.045	8.437	0.040	0.040	0.000	0.000	0.000	0.000
109	A	112	SER	0	0.013	-0.031	13.612	0.106	0.106	0.000	0.000	0.000	0.000
110	A	113	ASP	-1	-0.876	-0.907	11.195	0.249	0.249	0.000	0.000	0.000	0.000
111	A	114	LEU	0	0.035	-0.012	13.187	0.033	0.033	0.000	0.000	0.000	0.000
112	A	115	TYR	0	-0.058	-0.055	16.902	-0.024	-0.024	0.000	0.000	0.000	0.000
113	A	116	GLU	-1	-0.932	-0.970	12.761	0.592	0.592	0.000	0.000	0.000	0.000
114	A	117	ASN	0	-0.044	-0.017	14.487	0.066	0.066	0.000	0.000	0.000	0.000
115	A	118	VAL	0	-0.020	0.001	16.592	-0.033	-0.033	0.000	0.000	0.000	0.000
116	A	119	LYS	1	0.961	0.983	19.590	-0.320	-0.320	0.000	0.000	0.000	0.000
117	A	120	ASP	-1	-0.787	-0.867	22.096	0.177	0.177	0.000	0.000	0.000	0.000
118	A	121	ARG	1	0.929	0.966	23.700	-0.105	-0.105	0.000	0.000	0.000	0.000
119	A	122	LYS	1	0.964	0.993	26.140	-0.123	-0.123	0.000	0.000	0.000	0.000
120	A	123	TYR	0	-0.007	-0.023	23.361	-0.015	-0.015	0.000	0.000	0.000	0.000
121	A	124	ASN	0	0.024	0.024	29.725	0.005	0.005	0.000	0.000	0.000	0.000
122	A	125	LYS	1	0.909	0.963	31.098	-0.027	-0.027	0.000	0.000	0.000	0.000
123	A	126	ILE	0	0.007	0.027	25.481	0.002	0.002	0.000	0.000	0.000	0.000
124	A	127	ILE	0	0.002	-0.006	27.203	-0.003	-0.003	0.000	0.000	0.000	0.000
125	A	128	THR	0	0.001	-0.012	23.406	-0.004	-0.004	0.000	0.000	0.000	0.000
126	A	129	ASN	0	-0.002	-0.007	25.108	0.009	0.009	0.000	0.000	0.000	0.000
127	A	130	PRO	0	-0.028	-0.001	23.055	-0.012	-0.012	0.000	0.000	0.000	0.000
128	A	131	PRO	0	0.038	0.017	19.151	-0.014	-0.014	0.000	0.000	0.000	0.000
129	A	132	ILE	0	0.031	-0.005	22.028	0.017	0.017	0.000	0.000	0.000	0.000
130	A	133	ARG	1	0.937	0.948	20.696	0.241	0.241	0.000	0.000	0.000	0.000
131	A	134	ALA	0	0.007	0.021	18.738	-0.004	-0.004	0.000	0.000	0.000	0.000
132	A	135	GLY	0	0.067	0.048	20.115	0.022	0.022	0.000	0.000	0.000	0.000
133	A	136	LYS	1	0.919	0.926	23.087	0.002	0.002	0.000	0.000	0.000	0.000
134	A	137	GLU	-1	-0.847	-0.916	21.762	0.057	0.057	0.000	0.000	0.000	0.000
135	A	138	VAL	0	0.038	0.021	18.489	0.018	0.018	0.000	0.000	0.000	0.000
136	A	139	LEU	0	-0.023	-0.011	21.114	0.004	0.004	0.000	0.000	0.000	0.000
137	A	140	HIS	1	0.868	0.916	24.345	-0.055	-0.055	0.000	0.000	0.000	0.000
138	A	141	ARG	1	1.003	1.034	15.840	-0.307	-0.307	0.000	0.000	0.000	0.000
139	A	142	ILE	0	0.004	0.010	21.187	0.007	0.007	0.000	0.000	0.000	0.000
140	A	143	ILE	0	-0.042	-0.004	23.559	0.000	0.000	0.000	0.000	0.000	0.000
141	A	144	GLU	-1	-0.940	-0.979	25.980	0.142	0.142	0.000	0.000	0.000	0.000
142	A	145	GLU	-1	-0.840	-0.929	20.520	0.257	0.257	0.000	0.000	0.000	0.000
143	A	146	GLY	0	0.026	0.012	24.755	0.001	0.001	0.000	0.000	0.000	0.000
144	A	147	LYS	1	0.892	0.947	26.334	-0.093	-0.093	0.000	0.000	0.000	0.000
145	A	148	GLU	-1	-0.946	-0.971	25.396	0.189	0.189	0.000	0.000	0.000	0.000
146	A	149	LEU	0	-0.027	-0.005	22.735	0.005	0.005	0.000	0.000	0.000	0.000
147	A	150	LEU	0	-0.051	-0.009	27.380	-0.009	-0.009	0.000	0.000	0.000	0.000
148	A	151	LYS	1	0.796	0.882	30.653	-0.061	-0.061	0.000	0.000	0.000	0.000
149	A	152	ASP	-1	-0.850	-0.928	33.614	0.078	0.078	0.000	0.000	0.000	0.000
150	A	153	ASN	0	-0.071	-0.046	36.915	-0.005	-0.005	0.000	0.000	0.000	0.000
151	A	154	GLY	0	0.014	0.019	33.885	-0.006	-0.006	0.000	0.000	0.000	0.000
152	A	155	GLU	-1	-0.839	-0.948	33.594	0.021	0.021	0.000	0.000	0.000	0.000
153	A	156	ILE	0	-0.010	0.009	27.042	0.000	0.000	0.000	0.000	0.000	0.000
154	A	157	TRP	0	-0.007	-0.015	30.396	-0.007	-0.007	0.000	0.000	0.000	0.000
155	A	158	VAL	0	0.023	0.005	28.324	-0.003	-0.003	0.000	0.000	0.000	0.000
156	A	159	VAL	0	-0.038	-0.001	29.201	-0.001	-0.001	0.000	0.000	0.000	0.000
157	A	160	ILE	0	0.022	0.004	29.047	-0.004	-0.004	0.000	0.000	0.000	0.000
158	A	161	GLN	0	-0.027	-0.010	30.430	-0.003	-0.003	0.000	0.000	0.000	0.000
159	A	162	THR	0	-0.113	-0.121	32.983	0.006	0.006	0.000	0.000	0.000	0.000
160	A	163	LYS	1	0.975	0.985	35.596	0.047	0.047	0.000	0.000	0.000	0.000
161	A	164	GLN	0	0.077	0.001	36.340	0.007	0.007	0.000	0.000	0.000	0.000
162	A	165	GLY	0	0.031	0.041	32.708	0.006	0.006	0.000	0.000	0.000	0.000
163	A	166	ALA	0	0.062	0.025	32.707	0.007	0.007	0.000	0.000	0.000	0.000
164	A	167	LYS	1	0.937	0.976	34.320	0.019	0.019	0.000	0.000	0.000	0.000
165	A	168	SER	0	-0.049	-0.020	32.809	0.006	0.006	0.000	0.000	0.000	0.000
166	A	169	LEU	0	0.038	0.022	28.881	0.007	0.007	0.000	0.000	0.000	0.000
167	A	170	ALA	0	0.049	0.021	32.173	0.006	0.006	0.000	0.000	0.000	0.000
168	A	171	LYS	1	0.899	0.940	35.285	-0.009	-0.009	0.000	0.000	0.000	0.000
169	A	172	TYR	0	0.066	0.047	28.010	0.000	0.000	0.000	0.000	0.000	0.000
170	A	173	MET	0	0.003	-0.002	31.357	0.004	0.004	0.000	0.000	0.000	0.000
171	A	174	LYS	1	0.927	0.969	33.321	-0.026	-0.026	0.000	0.000	0.000	0.000
172	A	175	ASP	-1	-0.898	-0.949	34.106	0.053	0.053	0.000	0.000	0.000	0.000
173	A	176	VAL	0	-0.012	0.007	30.201	0.004	0.004	0.000	0.000	0.000	0.000
174	A	177	PHE	0	-0.031	-0.039	30.423	0.006	0.006	0.000	0.000	0.000	0.000
175	A	178	GLY	0	0.013	0.028	35.438	-0.001	-0.001	0.000	0.000	0.000	0.000
176	A	179	ASN	0	-0.062	-0.044	37.856	-0.009	-0.009	0.000	0.000	0.000	0.000
177	A	180	VAL	0	-0.017	0.009	35.872	0.002	0.002	0.000	0.000	0.000	0.000
178	A	181	GLU	-1	-0.891	-0.930	37.940	0.007	0.007	0.000	0.000	0.000	0.000
179	A	182	THR	0	-0.084	-0.054	38.086	-0.003	-0.003	0.000	0.000	0.000	0.000
180	A	183	VAL	0	0.035	0.022	37.964	-0.001	-0.001	0.000	0.000	0.000	0.000
181	A	184	THR	0	0.031	0.013	38.090	-0.003	-0.003	0.000	0.000	0.000	0.000
182	A	185	ILE	0	-0.025	-0.024	38.700	-0.001	-0.001	0.000	0.000	0.000	0.000
183	A	186	LYS	1	1.000	1.005	38.842	0.047	0.047	0.000	0.000	0.000	0.000
184	A	187	GLY	0	0.047	0.021	38.244	-0.004	-0.004	0.000	0.000	0.000	0.000
185	A	188	GLY	0	0.059	0.037	37.611	-0.005	-0.005	0.000	0.000	0.000	0.000
186	A	189	TYR	0	-0.009	0.059	31.297	0.000	0.000	0.000	0.000	0.000	0.000
187	A	190	ARG	1	0.928	0.946	34.690	0.025	0.025	0.000	0.000	0.000	0.000
188	A	191	VAL	0	0.046	0.037	34.037	-0.003	-0.003	0.000	0.000	0.000	0.000
189	A	192	LEU	0	-0.067	-0.030	32.871	0.002	0.002	0.000	0.000	0.000	0.000
190	A	193	LYS	1	0.969	0.995	33.654	-0.015	-0.015	0.000	0.000	0.000	0.000
191	A	194	SER	0	0.000	-0.022	33.623	-0.002	-0.002	0.000	0.000	0.000	0.000
192	A	195	LYS	1	0.897	0.962	34.627	-0.034	-0.034	0.000	0.000	0.000	0.000
193	A	196	LYS	1	0.850	0.938	31.486	-0.103	-0.103	0.000	0.000	0.000	0.000
194	A	197	LEU	0	0.010	0.009	35.834	-0.001	-0.001	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:4:PHE)