FMO DATABASE

FMODB ID: Z6VZN

Calculation Name: 1LAY-A-Xray372

Preferred Name: Human herpes virus 5 capsid protein P40

Target Type: SINGLE PROTEIN

Ligand Name:

ligand 3-letter code:

PDB ID: 1LAY

Chain ID: A

ChEMBL ID: CHEMBL3771

UniProt ID: P16753

Base Structure: X-ray

Registration Date: 2023-06-22

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	206
LigandCharge	DGL=-1,DAR=1
Software	ABINIT-MP - Open Ver. 1 Rev. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-2359279.452865
FMO2-HF: Nuclear repulsion	2279651.867357
FMO2-HF: Total energy	-79627.585508
FMO2-MP2: Total energy	-79860.563912

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:9:GLN)

Summations of interaction energy for fragment #1(A:9:GLN)

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.
-6.981	-2.126	0.699	-2.304	-3.251	-0.005

Interaction energy analysis for fragmet #1(A:9:GLN)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : 0.034 / q_NPA : 0.011

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	11	VAL	0	0.015	0.020	2.974	-3.949	-1.373	0.165	-1.125	-1.617	0.008
4	A	12	ALA	0	-0.010	0.005	2.754	-3.258	-1.088	0.534	-1.151	-1.552	-0.013
5	A	13	PRO	0	0.030	0.000	4.042	0.003	0.112	0.000	-0.028	-0.082	0.000
6	A	14	VAL	0	0.003	0.013	7.812	-0.299	-0.299	0.000	0.000	0.000	0.000
7	A	15	TYR	0	0.003	0.001	10.214	0.181	0.181	0.000	0.000	0.000	0.000
8	A	16	VAL	0	0.023	0.006	13.526	-0.104	-0.104	0.000	0.000	0.000	0.000
9	A	17	GLY	0	0.016	0.008	16.645	0.052	0.052	0.000	0.000	0.000	0.000
10	A	18	GLY	0	0.051	0.017	19.883	-0.031	-0.031	0.000	0.000	0.000	0.000
11	A	19	PHE	0	-0.004	0.016	23.360	0.026	0.026	0.000	0.000	0.000	0.000
12	A	20	LEU	0	0.015	0.007	24.923	-0.001	-0.001	0.000	0.000	0.000	0.000
13	A	21	ALA	0	-0.082	-0.065	27.966	0.010	0.010	0.000	0.000	0.000	0.000
14	A	22	ARG	1	0.891	0.965	29.612	0.159	0.159	0.000	0.000	0.000	0.000
15	A	23	TYR	0	-0.044	-0.015	33.780	0.010	0.010	0.000	0.000	0.000	0.000
16	A	24	ASP	-1	-0.824	-0.895	35.497	-0.110	-0.110	0.000	0.000	0.000	0.000
17	A	56	ALA	0	0.030	0.012	21.975	0.000	0.000	0.000	0.000	0.000	0.000
18	A	57	LEU	0	-0.060	-0.031	22.778	0.010	0.010	0.000	0.000	0.000	0.000
19	A	58	PRO	0	0.038	0.042	20.808	-0.002	-0.002	0.000	0.000	0.000	0.000
20	A	59	LEU	0	0.015	-0.017	16.358	-0.024	-0.024	0.000	0.000	0.000	0.000
21	A	60	ASN	0	0.009	-0.004	19.133	0.013	0.013	0.000	0.000	0.000	0.000
22	A	61	ILE	0	0.027	0.019	17.038	-0.034	-0.034	0.000	0.000	0.000	0.000
23	A	62	ASN	0	-0.004	-0.019	20.844	0.001	0.001	0.000	0.000	0.000	0.000
24	A	63	HIS	0	-0.006	-0.009	24.197	-0.009	-0.009	0.000	0.000	0.000	0.000
25	A	64	ASP	-1	-0.804	-0.870	23.661	0.079	0.079	0.000	0.000	0.000	0.000
26	A	65	ASP	-1	-0.873	-0.963	23.665	0.062	0.062	0.000	0.000	0.000	0.000
27	A	66	THR	0	-0.111	-0.039	23.548	0.021	0.021	0.000	0.000	0.000	0.000
28	A	67	ALA	0	-0.019	-0.009	19.946	0.031	0.031	0.000	0.000	0.000	0.000
29	A	68	VAL	0	0.016	-0.006	18.335	-0.026	-0.026	0.000	0.000	0.000	0.000
30	A	69	VAL	0	-0.013	-0.020	14.427	0.035	0.035	0.000	0.000	0.000	0.000
31	A	70	GLY	0	0.020	0.011	13.933	0.016	0.016	0.000	0.000	0.000	0.000
32	A	71	HIS	0	-0.007	0.036	14.598	-0.028	-0.028	0.000	0.000	0.000	0.000
33	A	72	VAL	0	-0.011	-0.013	17.597	-0.031	-0.031	0.000	0.000	0.000	0.000
34	A	73	ALA	0	0.004	-0.010	17.463	0.020	0.020	0.000	0.000	0.000	0.000
35	A	74	ALA	0	0.026	0.003	19.579	0.012	0.012	0.000	0.000	0.000	0.000
36	A	75	MET	0	-0.033	-0.018	22.785	-0.017	-0.017	0.000	0.000	0.000	0.000
37	A	76	GLN	0	0.031	0.023	25.769	0.021	0.021	0.000	0.000	0.000	0.000
38	A	77	SER	0	-0.014	0.018	28.517	-0.009	-0.009	0.000	0.000	0.000	0.000
39	A	78	VAL	0	0.008	0.016	28.330	0.004	0.004	0.000	0.000	0.000	0.000
40	A	79	ARG	1	0.859	0.900	31.334	0.153	0.153	0.000	0.000	0.000	0.000
41	A	80	ASP	-1	-0.791	-0.897	32.082	-0.134	-0.134	0.000	0.000	0.000	0.000
42	A	81	GLY	0	-0.021	-0.017	31.937	-0.003	-0.003	0.000	0.000	0.000	0.000
43	A	82	LEU	0	-0.048	-0.002	28.720	0.003	0.003	0.000	0.000	0.000	0.000
44	A	83	PHE	0	0.001	-0.002	21.874	-0.004	-0.004	0.000	0.000	0.000	0.000
45	A	84	CYS	0	-0.034	-0.024	22.636	0.023	0.023	0.000	0.000	0.000	0.000
46	A	85	LEU	0	0.038	0.026	16.802	-0.033	-0.033	0.000	0.000	0.000	0.000
47	A	86	GLY	0	-0.028	-0.022	17.936	0.040	0.040	0.000	0.000	0.000	0.000
48	A	87	CYS	0	-0.045	-0.018	12.473	-0.029	-0.029	0.000	0.000	0.000	0.000
49	A	88	VAL	0	0.002	0.001	11.250	0.062	0.062	0.000	0.000	0.000	0.000
50	A	89	THR	0	0.006	-0.016	9.962	-0.051	-0.051	0.000	0.000	0.000	0.000
51	A	90	SER	0	-0.042	-0.019	10.144	0.095	0.095	0.000	0.000	0.000	0.000
52	A	91	PRO	0	0.047	0.021	8.376	-0.011	-0.011	0.000	0.000	0.000	0.000
53	A	92	ARG	1	0.829	0.924	9.457	-0.225	-0.225	0.000	0.000	0.000	0.000
54	A	93	PHE	0	0.031	0.022	12.360	-0.023	-0.023	0.000	0.000	0.000	0.000
55	A	94	LEU	0	0.013	-0.008	6.821	-0.033	-0.033	0.000	0.000	0.000	0.000
56	A	95	GLU	-1	-0.793	-0.892	8.870	1.521	1.521	0.000	0.000	0.000	0.000
57	A	96	ILE	0	-0.081	-0.025	10.059	-0.080	-0.080	0.000	0.000	0.000	0.000
58	A	97	VAL	0	0.005	-0.016	11.162	-0.053	-0.053	0.000	0.000	0.000	0.000
59	A	98	ARG	1	0.803	0.903	6.324	-1.348	-1.348	0.000	0.000	0.000	0.000
60	A	99	ARG	1	0.937	0.987	10.014	-0.795	-0.795	0.000	0.000	0.000	0.000
61	A	100	ALA	0	0.013	0.012	12.586	-0.083	-0.083	0.000	0.000	0.000	0.000
62	A	101	SER	0	-0.052	-0.034	11.360	-0.102	-0.102	0.000	0.000	0.000	0.000
63	A	102	GLU	-1	-0.896	-0.955	9.963	0.193	0.193	0.000	0.000	0.000	0.000
64	A	103	LYS	1	0.887	0.952	13.525	0.027	0.027	0.000	0.000	0.000	0.000
65	A	104	SER	0	0.013	0.015	16.042	-0.002	-0.002	0.000	0.000	0.000	0.000
66	A	105	GLU	-1	-0.869	-0.939	17.019	-0.331	-0.331	0.000	0.000	0.000	0.000
67	A	106	LEU	0	-0.020	-0.013	18.490	-0.051	-0.051	0.000	0.000	0.000	0.000
68	A	107	VAL	0	0.009	-0.006	12.522	-0.050	-0.050	0.000	0.000	0.000	0.000
69	A	108	SER	0	-0.057	-0.037	14.106	-0.143	-0.143	0.000	0.000	0.000	0.000
70	A	109	ARG	1	0.872	0.951	15.679	0.340	0.340	0.000	0.000	0.000	0.000
71	A	110	GLY	0	0.007	0.035	14.088	-0.027	-0.027	0.000	0.000	0.000	0.000
72	A	111	PRO	0	-0.039	-0.037	12.396	0.131	0.131	0.000	0.000	0.000	0.000
73	A	112	VAL	0	-0.001	0.021	15.550	0.027	0.027	0.000	0.000	0.000	0.000
74	A	113	SER	0	0.029	-0.044	17.247	0.061	0.061	0.000	0.000	0.000	0.000
75	A	114	PRO	0	-0.057	0.001	15.991	-0.017	-0.017	0.000	0.000	0.000	0.000
76	A	115	LEU	0	-0.012	0.017	12.854	-0.106	-0.106	0.000	0.000	0.000	0.000
77	A	116	GLN	0	0.047	0.028	7.197	-0.394	-0.394	0.000	0.000	0.000	0.000
78	A	117	PRO	0	0.021	0.036	9.163	0.002	0.002	0.000	0.000	0.000	0.000
79	A	118	ASP	-1	-0.760	-0.847	6.756	-3.664	-3.664	0.000	0.000	0.000	0.000
80	A	119	LYS	1	1.015	0.984	7.915	1.371	1.371	0.000	0.000	0.000	0.000
81	A	120	VAL	0	0.052	0.024	7.419	0.242	0.242	0.000	0.000	0.000	0.000
82	A	121	VAL	0	0.018	0.022	8.499	0.233	0.233	0.000	0.000	0.000	0.000
83	A	122	GLU	-1	-0.812	-0.889	10.671	-0.954	-0.954	0.000	0.000	0.000	0.000
84	A	123	PHE	0	0.013	0.008	12.402	0.121	0.121	0.000	0.000	0.000	0.000
85	A	124	LEU	0	-0.026	-0.007	11.768	0.090	0.090	0.000	0.000	0.000	0.000
86	A	125	SER	0	-0.020	-0.040	14.471	0.065	0.065	0.000	0.000	0.000	0.000
87	A	126	GLY	0	-0.021	-0.006	16.872	0.035	0.035	0.000	0.000	0.000	0.000
88	A	127	SER	0	-0.071	-0.019	17.842	0.060	0.060	0.000	0.000	0.000	0.000
89	A	128	TYR	0	-0.057	-0.045	16.830	0.039	0.039	0.000	0.000	0.000	0.000
90	A	129	ALA	0	0.052	0.025	20.179	-0.018	-0.018	0.000	0.000	0.000	0.000
91	A	130	GLY	0	0.034	0.016	21.820	-0.007	-0.007	0.000	0.000	0.000	0.000
92	A	131	LEU	0	-0.020	0.010	20.509	0.016	0.016	0.000	0.000	0.000	0.000
93	A	132	SER	0	-0.065	-0.046	24.399	0.010	0.010	0.000	0.000	0.000	0.000
94	A	133	LEU	0	0.039	0.029	26.114	0.006	0.006	0.000	0.000	0.000	0.000
95	A	134	SER	0	-0.040	-0.059	27.926	0.001	0.001	0.000	0.000	0.000	0.000
96	A	135	SER	0	0.010	0.004	29.814	0.004	0.004	0.000	0.000	0.000	0.000
97	A	136	ARG	1	0.873	0.913	32.012	-0.039	-0.039	0.000	0.000	0.000	0.000
98	A	137	ARG	1	0.873	0.926	34.532	-0.005	-0.005	0.000	0.000	0.000	0.000
99	A	138	CYS	0	-0.010	-0.018	37.767	0.003	0.003	0.000	0.000	0.000	0.000
100	A	139	ASP	-1	-0.946	-0.969	39.311	0.012	0.012	0.000	0.000	0.000	0.000
101	A	140	ASP	-1	-0.863	-0.927	34.453	0.015	0.015	0.000	0.000	0.000	0.000
102	A	141	VAL	0	0.039	0.025	35.043	0.001	0.001	0.000	0.000	0.000	0.000
103	A	142	GLU	-1	-0.866	-0.900	33.412	0.054	0.054	0.000	0.000	0.000	0.000
104	A	154	PRO	0	-0.014	-0.017	29.851	0.000	0.000	0.000	0.000	0.000	0.000
105	A	155	PHE	0	-0.028	-0.036	30.439	0.006	0.006	0.000	0.000	0.000	0.000
106	A	156	LYS	1	0.944	0.986	29.024	-0.005	-0.005	0.000	0.000	0.000	0.000
107	A	157	HIS	0	0.079	0.072	24.392	-0.002	-0.002	0.000	0.000	0.000	0.000
108	A	158	VAL	0	-0.028	-0.010	22.421	-0.014	-0.014	0.000	0.000	0.000	0.000
109	A	159	ALA	0	0.000	0.019	22.349	0.011	0.011	0.000	0.000	0.000	0.000
110	A	160	LEU	0	-0.018	-0.006	16.669	-0.021	-0.021	0.000	0.000	0.000	0.000
111	A	161	CYS	0	-0.005	-0.014	21.275	0.028	0.028	0.000	0.000	0.000	0.000
112	A	162	SER	0	-0.011	0.006	23.249	-0.027	-0.027	0.000	0.000	0.000	0.000
113	A	163	VAL	0	0.018	-0.010	24.825	-0.024	-0.024	0.000	0.000	0.000	0.000
114	A	164	GLY	0	0.042	0.050	26.925	0.017	0.017	0.000	0.000	0.000	0.000
115	A	165	ARG	1	0.879	0.915	28.278	0.056	0.056	0.000	0.000	0.000	0.000
116	A	166	ARG	1	0.943	0.980	30.862	0.074	0.074	0.000	0.000	0.000	0.000
117	A	167	ARG	1	0.816	0.885	31.099	0.099	0.099	0.000	0.000	0.000	0.000
118	A	168	GLY	0	0.047	0.008	29.336	0.007	0.007	0.000	0.000	0.000	0.000
119	A	169	THR	0	-0.086	-0.036	26.933	-0.012	-0.012	0.000	0.000	0.000	0.000
120	A	170	LEU	0	-0.001	0.014	22.493	0.005	0.005	0.000	0.000	0.000	0.000
121	A	171	ALA	0	-0.040	-0.009	19.538	0.002	0.002	0.000	0.000	0.000	0.000
122	A	172	VAL	0	-0.004	0.008	17.169	-0.039	-0.039	0.000	0.000	0.000	0.000
123	A	173	TYR	0	-0.012	-0.030	13.199	0.055	0.055	0.000	0.000	0.000	0.000
124	A	174	GLY	0	0.018	-0.006	11.882	-0.081	-0.081	0.000	0.000	0.000	0.000
125	A	175	ARG	1	0.720	0.838	5.571	2.092	2.092	0.000	0.000	0.000	0.000
126	A	176	ASP	-1	-0.833	-0.914	9.430	-0.304	-0.304	0.000	0.000	0.000	0.000
127	A	177	PRO	0	0.047	0.022	11.610	-0.031	-0.031	0.000	0.000	0.000	0.000
128	A	178	GLU	-1	-0.798	-0.899	14.880	-0.221	-0.221	0.000	0.000	0.000	0.000
129	A	179	TRP	0	-0.054	-0.019	13.248	-0.037	-0.037	0.000	0.000	0.000	0.000
130	A	180	VAL	0	0.018	0.011	14.403	0.001	0.001	0.000	0.000	0.000	0.000
131	A	181	THR	0	-0.042	-0.016	16.774	0.031	0.031	0.000	0.000	0.000	0.000
132	A	182	GLN	0	-0.073	-0.063	18.254	0.037	0.037	0.000	0.000	0.000	0.000
133	A	183	ARG	1	0.819	0.917	16.702	0.587	0.587	0.000	0.000	0.000	0.000
134	A	184	PHE	0	0.013	0.010	20.442	0.017	0.017	0.000	0.000	0.000	0.000
135	A	185	PRO	0	0.063	0.035	23.912	0.019	0.019	0.000	0.000	0.000	0.000
136	A	186	ASP	-1	-0.872	-0.928	26.870	-0.186	-0.186	0.000	0.000	0.000	0.000
137	A	187	LEU	0	-0.068	-0.028	23.409	0.022	0.022	0.000	0.000	0.000	0.000
138	A	188	THR	0	-0.013	0.025	26.518	-0.018	-0.018	0.000	0.000	0.000	0.000
139	A	189	ALA	0	0.005	-0.022	26.081	-0.004	-0.004	0.000	0.000	0.000	0.000
140	A	190	ALA	0	0.088	0.029	26.721	0.005	0.005	0.000	0.000	0.000	0.000
141	A	191	ASP	-1	-0.833	-0.923	27.226	-0.128	-0.128	0.000	0.000	0.000	0.000
142	A	192	ARG	1	0.883	0.925	21.775	0.250	0.250	0.000	0.000	0.000	0.000
143	A	193	ASP	-1	-0.886	-0.926	23.516	-0.108	-0.108	0.000	0.000	0.000	0.000
144	A	194	GLY	0	-0.028	-0.013	25.611	0.017	0.017	0.000	0.000	0.000	0.000
145	A	195	LEU	0	-0.017	-0.020	22.642	0.014	0.014	0.000	0.000	0.000	0.000
146	A	196	ARG	1	0.930	0.950	19.527	0.174	0.174	0.000	0.000	0.000	0.000
147	A	197	ALA	0	0.008	0.000	21.567	0.025	0.025	0.000	0.000	0.000	0.000
148	A	198	GLN	0	-0.065	-0.047	23.282	0.031	0.031	0.000	0.000	0.000	0.000
149	A	199	TRP	0	0.059	0.050	16.903	0.014	0.014	0.000	0.000	0.000	0.000
150	A	200	GLN	0	-0.050	-0.019	18.197	0.031	0.031	0.000	0.000	0.000	0.000
151	A	201	ARG	1	0.866	0.943	19.997	-0.012	-0.012	0.000	0.000	0.000	0.000
152	A	202	CYS	0	-0.052	0.006	18.569	0.015	0.015	0.000	0.000	0.000	0.000
153	A	203	GLY	0	0.042	0.010	14.605	-0.042	-0.042	0.000	0.000	0.000	0.000
154	A	204	SER	0	-0.044	-0.051	9.059	0.009	0.009	0.000	0.000	0.000	0.000
155	A	205	THR	0	-0.039	-0.026	11.073	-0.049	-0.049	0.000	0.000	0.000	0.000
156	A	206	ALA	0	0.052	0.049	13.441	0.042	0.042	0.000	0.000	0.000	0.000
157	A	207	VAL	0	-0.038	-0.026	15.436	0.048	0.048	0.000	0.000	0.000	0.000
158	A	208	ASP	-1	-0.886	-0.941	17.839	0.285	0.285	0.000	0.000	0.000	0.000
159	A	209	ALA	0	-0.008	0.005	18.146	-0.024	-0.024	0.000	0.000	0.000	0.000
160	A	210	SER	0	-0.009	-0.021	19.994	0.002	0.002	0.000	0.000	0.000	0.000
161	A	211	GLY	0	-0.005	0.014	16.688	-0.001	-0.001	0.000	0.000	0.000	0.000
162	A	212	ASP	-1	-0.762	-0.900	13.296	0.448	0.448	0.000	0.000	0.000	0.000
163	A	213	PRO	0	-0.025	-0.004	14.887	-0.021	-0.021	0.000	0.000	0.000	0.000
164	A	214	PHE	0	-0.023	-0.008	15.710	-0.035	-0.035	0.000	0.000	0.000	0.000
165	A	215	ARG	1	0.927	0.942	17.548	-0.143	-0.143	0.000	0.000	0.000	0.000
166	A	216	SER	0	0.080	0.088	19.754	-0.010	-0.010	0.000	0.000	0.000	0.000
167	A	217	ASP	-1	-0.861	-0.978	19.049	0.196	0.196	0.000	0.000	0.000	0.000
168	A	218	SER	0	-0.011	-0.021	18.846	-0.029	-0.029	0.000	0.000	0.000	0.000
169	A	219	TYR	0	0.014	0.003	19.664	-0.030	-0.030	0.000	0.000	0.000	0.000
170	A	220	GLY	0	0.041	0.045	22.674	-0.020	-0.020	0.000	0.000	0.000	0.000
171	A	221	LEU	0	-0.022	-0.010	17.252	-0.018	-0.018	0.000	0.000	0.000	0.000
172	A	222	LEU	0	-0.029	-0.014	21.443	-0.026	-0.026	0.000	0.000	0.000	0.000
173	A	223	GLY	0	0.028	0.024	23.473	-0.016	-0.016	0.000	0.000	0.000	0.000
174	A	224	ASN	0	0.028	0.013	22.973	0.002	0.002	0.000	0.000	0.000	0.000
175	A	225	SER	0	-0.103	-0.051	23.204	-0.021	-0.021	0.000	0.000	0.000	0.000
176	A	226	VAL	0	0.048	0.002	24.995	-0.018	-0.018	0.000	0.000	0.000	0.000
177	A	227	ASP	-1	-0.835	-0.910	28.566	-0.031	-0.031	0.000	0.000	0.000	0.000
178	A	228	ALA	0	-0.051	-0.026	26.414	-0.009	-0.009	0.000	0.000	0.000	0.000
179	A	229	LEU	0	-0.046	-0.017	27.249	-0.013	-0.013	0.000	0.000	0.000	0.000
180	A	230	TYR	0	-0.055	-0.031	30.004	-0.004	-0.004	0.000	0.000	0.000	0.000
181	A	231	ILE	0	-0.005	0.028	29.122	0.005	0.005	0.000	0.000	0.000	0.000
182	A	232	DAR	1	0.790	0.868	32.103	0.094	0.094	0.000	0.000	0.000	0.000
183	A	233	DGL	-1	-0.790	-0.902	32.213	-0.134	-0.134	0.000	0.000	0.000	0.000
184	A	234	ARG	1	0.954	1.006	22.992	0.194	0.194	0.000	0.000	0.000	0.000
185	A	235	LEU	0	0.031	0.001	27.157	-0.012	-0.012	0.000	0.000	0.000	0.000
186	A	236	PRO	0	-0.014	-0.012	29.177	-0.013	-0.013	0.000	0.000	0.000	0.000
187	A	237	LYS	1	0.877	0.972	30.201	0.136	0.136	0.000	0.000	0.000	0.000
188	A	238	LEU	0	0.020	-0.002	24.549	-0.006	-0.006	0.000	0.000	0.000	0.000
189	A	239	ARG	1	0.880	0.938	27.419	0.193	0.193	0.000	0.000	0.000	0.000
190	A	240	TYR	0	0.019	0.009	29.064	-0.004	-0.004	0.000	0.000	0.000	0.000
191	A	241	ASP	-1	-0.721	-0.864	27.584	-0.172	-0.172	0.000	0.000	0.000	0.000
192	A	242	LYS	1	0.839	0.928	24.400	0.350	0.350	0.000	0.000	0.000	0.000
193	A	243	GLN	0	-0.043	-0.025	26.664	0.001	0.001	0.000	0.000	0.000	0.000
194	A	244	LEU	0	-0.040	-0.006	29.707	0.003	0.003	0.000	0.000	0.000	0.000
195	A	245	VAL	0	-0.046	-0.038	25.338	0.006	0.006	0.000	0.000	0.000	0.000
196	A	246	GLY	0	0.025	0.024	27.073	-0.007	-0.007	0.000	0.000	0.000	0.000
197	A	247	VAL	0	-0.006	0.025	20.957	-0.017	-0.017	0.000	0.000	0.000	0.000
198	A	248	THR	0	0.007	-0.002	22.819	-0.002	-0.002	0.000	0.000	0.000	0.000
199	A	249	GLU	-1	-0.913	-0.959	20.153	-0.438	-0.438	0.000	0.000	0.000	0.000
200	A	250	ARG	1	0.945	0.952	18.879	0.520	0.520	0.000	0.000	0.000	0.000
201	A	251	GLU	-1	-0.880	-0.947	18.576	-0.512	-0.512	0.000	0.000	0.000	0.000
202	A	252	SER	0	0.006	-0.014	16.000	-0.027	-0.027	0.000	0.000	0.000	0.000
203	A	253	TYR	0	-0.020	-0.065	9.874	0.056	0.056	0.000	0.000	0.000	0.000
204	A	254	VAL	0	-0.001	0.012	15.913	0.036	0.036	0.000	0.000	0.000	0.000
205	A	255	LYS	1	0.871	0.922	15.643	0.724	0.724	0.000	0.000	0.000	0.000
206	A	256	ALA	0	-0.008	0.005	20.331	0.030	0.030	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:9:GLN)