FMO DATABASE

FMODB ID: LN1M9

Calculation Name: 1VSC-A-Xray372

Preferred Name: Vascular cell adhesion protein 1

Target Type: SINGLE PROTEIN

Ligand Name:

Ligand 3-letter code:

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 1VSC

Chain ID: A

ChEMBL ID: CHEMBL3735

UniProt ID: P19320

Base Structure: X-ray

Registration Date: 2023-09-24

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
Remarks

FMO calculation

FMO method	FMO2-MP2/6-31G(d)
Fragmentation	Auto
Number of fragment	193
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-1918331.098179
FMO2-HF: Nuclear repulsion	1840730.533185
FMO2-HF: Total energy	-77600.564994
FMO2-MP2: Total energy	-77823.422377

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:PHE)

Summations of interaction energy for fragment #1(A:1: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.
-46.855	-33.838	36.783	-17.323	-32.477	-0.033

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

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : -0.026 / q_NPA : 0.017

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	3	ILE	0	0.020	0.002	2.524	-5.315	-1.567	1.538	-2.260	-3.026	-0.009
4	A	4	GLU	-1	-0.843	-0.895	4.949	-1.992	-1.913	-0.001	-0.011	-0.067	0.000
5	A	5	THR	0	0.005	-0.014	8.395	-0.099	-0.099	0.000	0.000	0.000	0.000
6	A	6	THR	0	-0.052	0.004	11.049	0.110	0.110	0.000	0.000	0.000	0.000
7	A	7	PRO	0	0.078	0.023	14.688	0.009	0.009	0.000	0.000	0.000	0.000
8	A	8	GLU	-1	-0.808	-0.905	13.032	-1.010	-1.010	0.000	0.000	0.000	0.000
9	A	9	SER	0	-0.015	-0.012	14.118	-0.058	-0.058	0.000	0.000	0.000	0.000
10	A	10	ARG	1	0.866	0.906	16.506	0.330	0.330	0.000	0.000	0.000	0.000
11	A	11	TYR	0	0.007	-0.010	19.357	-0.024	-0.024	0.000	0.000	0.000	0.000
12	A	12	LEU	0	0.005	0.021	21.496	0.006	0.006	0.000	0.000	0.000	0.000
13	A	13	ALA	0	-0.041	-0.018	24.997	-0.002	-0.002	0.000	0.000	0.000	0.000
14	A	14	GLN	0	-0.012	-0.004	26.931	0.017	0.017	0.000	0.000	0.000	0.000
15	A	15	ILE	0	-0.040	-0.029	29.381	-0.007	-0.007	0.000	0.000	0.000	0.000
16	A	16	GLY	0	-0.013	-0.005	29.770	0.012	0.012	0.000	0.000	0.000	0.000
17	A	17	ASP	-1	-0.834	-0.899	27.260	-0.216	-0.216	0.000	0.000	0.000	0.000
18	A	18	SER	0	-0.020	-0.031	24.743	-0.003	-0.003	0.000	0.000	0.000	0.000
19	A	19	VAL	0	-0.005	0.018	20.692	-0.013	-0.013	0.000	0.000	0.000	0.000
20	A	20	SER	0	0.014	-0.002	18.516	0.009	0.009	0.000	0.000	0.000	0.000
21	A	21	LEU	0	-0.012	0.022	14.721	-0.013	-0.013	0.000	0.000	0.000	0.000
22	A	22	THR	0	-0.012	-0.006	12.877	-0.004	-0.004	0.000	0.000	0.000	0.000
23	A	23	CYS	0	-0.026	0.001	7.258	-0.194	-0.194	0.000	0.000	0.000	0.000
24	A	24	SER	0	0.033	0.008	7.428	0.178	0.178	0.000	0.000	0.000	0.000
25	A	25	THR	0	-0.014	-0.023	2.260	-1.279	-0.747	2.348	-0.844	-2.035	-0.003
26	A	26	THR	0	-0.042	-0.030	4.176	0.463	0.685	-0.001	-0.016	-0.205	0.000
27	A	27	GLY	0	-0.036	-0.032	2.988	-4.337	-2.347	0.237	-1.095	-1.133	-0.010
28	A	28	CYS	0	-0.020	-0.010	2.590	-3.681	1.406	6.733	-3.041	-8.779	0.001
29	A	29	GLU	-1	-0.924	-0.945	4.070	0.405	0.457	0.005	-0.032	-0.025	0.000
30	A	30	SER	0	-0.015	-0.023	7.329	-0.345	-0.345	0.000	0.000	0.000	0.000
31	A	31	PRO	0	-0.015	0.004	4.554	0.206	0.407	-0.001	-0.015	-0.185	0.000
32	A	32	PHE	0	-0.023	-0.005	5.778	-0.212	-0.212	0.000	0.000	0.000	0.000
33	A	33	PHE	0	0.011	-0.006	5.437	-0.492	-0.492	0.000	0.000	0.000	0.000
34	A	34	SER	0	-0.034	-0.012	7.745	0.290	0.290	0.000	0.000	0.000	0.000
35	A	35	TRP	0	0.016	-0.009	9.653	-0.191	-0.191	0.000	0.000	0.000	0.000
36	A	36	ARG	1	0.807	0.888	11.254	0.629	0.629	0.000	0.000	0.000	0.000
37	A	37	THR	0	0.008	-0.012	14.640	-0.031	-0.031	0.000	0.000	0.000	0.000
38	A	38	GLN	0	0.078	0.025	16.818	-0.020	-0.020	0.000	0.000	0.000	0.000
39	A	39	ILE	0	-0.055	-0.025	18.074	0.024	0.024	0.000	0.000	0.000	0.000
40	A	40	ASP	-1	-0.856	-0.916	15.709	-0.345	-0.345	0.000	0.000	0.000	0.000
41	A	41	SER	0	0.004	0.026	18.538	0.022	0.022	0.000	0.000	0.000	0.000
42	A	42	PRO	0	-0.011	-0.019	19.896	-0.024	-0.024	0.000	0.000	0.000	0.000
43	A	43	LEU	0	0.029	0.017	15.903	-0.002	-0.002	0.000	0.000	0.000	0.000
44	A	44	ASN	0	-0.077	-0.022	19.943	0.002	0.002	0.000	0.000	0.000	0.000
45	A	45	GLY	0	0.091	0.053	20.780	0.001	0.001	0.000	0.000	0.000	0.000
46	A	46	LYS	1	0.885	0.951	19.964	0.222	0.222	0.000	0.000	0.000	0.000
47	A	47	VAL	0	0.030	0.019	13.506	-0.019	-0.019	0.000	0.000	0.000	0.000
48	A	48	THR	0	-0.063	-0.036	15.226	0.072	0.072	0.000	0.000	0.000	0.000
49	A	49	ASN	0	-0.015	0.004	11.069	-0.133	-0.133	0.000	0.000	0.000	0.000
50	A	50	GLU	-1	-0.910	-0.966	12.276	-0.223	-0.223	0.000	0.000	0.000	0.000
51	A	51	GLY	0	0.069	0.047	11.987	-0.102	-0.102	0.000	0.000	0.000	0.000
52	A	52	THR	0	-0.056	-0.022	7.044	0.082	0.082	0.000	0.000	0.000	0.000
53	A	53	THR	0	0.024	0.008	7.614	-0.495	-0.495	0.000	0.000	0.000	0.000
54	A	54	SER	0	-0.012	-0.002	9.480	0.176	0.176	0.000	0.000	0.000	0.000
55	A	55	THR	0	0.019	-0.002	10.935	-0.059	-0.059	0.000	0.000	0.000	0.000
56	A	56	LEU	0	-0.010	0.000	14.118	0.039	0.039	0.000	0.000	0.000	0.000
57	A	57	THR	0	0.001	-0.004	16.164	-0.005	-0.005	0.000	0.000	0.000	0.000
58	A	58	MET	0	-0.073	-0.041	18.945	0.019	0.019	0.000	0.000	0.000	0.000
59	A	59	ASN	0	0.006	0.025	22.556	0.008	0.008	0.000	0.000	0.000	0.000
60	A	60	PRO	0	-0.010	0.003	25.895	0.009	0.009	0.000	0.000	0.000	0.000
61	A	61	VAL	0	-0.018	-0.003	24.109	-0.004	-0.004	0.000	0.000	0.000	0.000
62	A	62	SER	0	0.060	0.003	26.444	0.019	0.019	0.000	0.000	0.000	0.000
63	A	63	PHE	0	0.079	0.024	26.863	-0.019	-0.019	0.000	0.000	0.000	0.000
64	A	64	GLY	0	-0.047	-0.016	26.068	-0.005	-0.005	0.000	0.000	0.000	0.000
65	A	65	ASN	0	-0.006	-0.032	22.087	0.001	0.001	0.000	0.000	0.000	0.000
66	A	66	GLU	-1	-0.756	-0.813	22.642	-0.229	-0.229	0.000	0.000	0.000	0.000
67	A	67	HIS	1	0.836	0.922	19.696	0.307	0.307	0.000	0.000	0.000	0.000
68	A	68	SER	0	0.038	0.021	17.288	-0.021	-0.021	0.000	0.000	0.000	0.000
69	A	69	TYR	0	-0.034	-0.031	15.077	0.014	0.014	0.000	0.000	0.000	0.000
70	A	70	LEU	0	-0.009	-0.012	11.831	-0.045	-0.045	0.000	0.000	0.000	0.000
71	A	72	THR	0	-0.014	-0.019	6.422	-0.057	-0.057	0.000	0.000	0.000	0.000
72	A	73	ALA	0	0.047	0.024	2.658	-0.435	0.206	0.318	-0.264	-0.695	-0.001
73	A	74	THR	0	-0.030	-0.029	2.557	-5.147	-2.937	1.566	-1.571	-2.205	-0.019
74	A	76	GLU	-1	-0.778	-0.885	4.135	4.917	5.387	0.004	0.050	-0.523	0.001
75	A	77	SER	0	-0.059	-0.037	5.656	-0.706	-0.706	0.000	0.000	0.000	0.000
76	A	78	ARG	1	0.815	0.896	1.895	-23.252	-29.660	18.092	-5.899	-5.785	0.006
77	A	79	LYS	1	0.894	0.928	2.475	-0.777	0.448	1.768	-0.940	-2.054	-0.009
78	A	80	LEU	0	-0.051	-0.016	2.617	-2.581	0.221	4.176	-1.411	-5.567	0.010
79	A	81	GLU	-1	-0.774	-0.872	3.866	-1.448	-1.282	0.001	0.026	-0.193	0.000
80	A	82	LYS	1	0.798	0.896	7.075	1.154	1.154	0.000	0.000	0.000	0.000
81	A	83	GLY	0	0.007	0.008	9.442	0.017	0.017	0.000	0.000	0.000	0.000
82	A	84	ILE	0	-0.027	-0.013	12.994	-0.007	-0.007	0.000	0.000	0.000	0.000
83	A	85	GLN	0	0.044	0.034	15.752	0.010	0.010	0.000	0.000	0.000	0.000
84	A	86	VAL	0	-0.030	-0.018	18.801	0.002	0.002	0.000	0.000	0.000	0.000
85	A	87	GLU	-1	-0.828	-0.888	21.313	-0.275	-0.275	0.000	0.000	0.000	0.000
86	A	88	ILE	0	-0.029	-0.024	24.966	-0.005	-0.005	0.000	0.000	0.000	0.000
87	A	89	TYR	0	0.035	0.024	27.805	0.008	0.008	0.000	0.000	0.000	0.000
88	A	90	SER	0	-0.037	-0.042	31.519	-0.005	-0.005	0.000	0.000	0.000	0.000
89	A	91	PHE	0	0.060	0.017	34.388	0.006	0.006	0.000	0.000	0.000	0.000
90	A	92	PRO	0	0.027	0.026	36.775	0.002	0.002	0.000	0.000	0.000	0.000
91	A	93	LYS	1	0.813	0.888	38.601	0.111	0.111	0.000	0.000	0.000	0.000
92	A	94	ASP	-1	-0.853	-0.911	42.397	-0.109	-0.109	0.000	0.000	0.000	0.000
93	A	95	PRO	0	-0.010	-0.012	45.145	0.001	0.001	0.000	0.000	0.000	0.000
94	A	96	GLU	-1	-0.951	-0.966	47.510	-0.078	-0.078	0.000	0.000	0.000	0.000
95	A	97	ILE	0	-0.030	-0.034	50.805	0.000	0.000	0.000	0.000	0.000	0.000
96	A	98	HIS	0	0.014	0.017	54.311	0.001	0.001	0.000	0.000	0.000	0.000
97	A	99	LEU	0	-0.001	-0.011	56.951	0.000	0.000	0.000	0.000	0.000	0.000
98	A	100	SER	0	-0.036	-0.035	60.518	0.001	0.001	0.000	0.000	0.000	0.000
99	A	101	GLY	0	-0.016	-0.008	62.429	0.002	0.002	0.000	0.000	0.000	0.000
100	A	102	PRO	0	-0.033	-0.006	65.485	-0.001	-0.001	0.000	0.000	0.000	0.000
101	A	103	LEU	0	0.000	0.018	65.347	0.000	0.000	0.000	0.000	0.000	0.000
102	A	104	GLU	-1	-0.770	-0.881	68.104	-0.041	-0.041	0.000	0.000	0.000	0.000
103	A	105	ALA	0	0.009	0.000	70.802	-0.001	-0.001	0.000	0.000	0.000	0.000
104	A	106	GLY	0	-0.004	0.000	71.472	0.001	0.001	0.000	0.000	0.000	0.000
105	A	107	LYS	1	0.793	0.884	69.232	0.043	0.043	0.000	0.000	0.000	0.000
106	A	108	PRO	0	-0.035	-0.022	67.780	-0.001	-0.001	0.000	0.000	0.000	0.000
107	A	109	ILE	0	-0.017	-0.008	63.455	0.000	0.000	0.000	0.000	0.000	0.000
108	A	110	THR	0	0.012	0.008	59.275	-0.001	-0.001	0.000	0.000	0.000	0.000
109	A	111	VAL	0	-0.008	0.012	56.674	0.001	0.001	0.000	0.000	0.000	0.000
110	A	112	LYS	1	0.835	0.904	52.259	0.071	0.071	0.000	0.000	0.000	0.000
111	A	113	CYS	0	-0.049	-0.005	50.538	-0.001	-0.001	0.000	0.000	0.000	0.000
112	A	114	SER	0	0.026	0.009	48.609	0.001	0.001	0.000	0.000	0.000	0.000
113	A	115	VAL	0	0.040	0.013	43.134	-0.001	-0.001	0.000	0.000	0.000	0.000
114	A	116	ALA	0	0.017	0.016	43.158	0.001	0.001	0.000	0.000	0.000	0.000
115	A	117	ASP	-1	-0.806	-0.879	38.242	-0.118	-0.118	0.000	0.000	0.000	0.000
116	A	118	VAL	0	0.003	0.013	37.544	-0.008	-0.008	0.000	0.000	0.000	0.000
117	A	119	TYR	0	-0.087	-0.064	30.078	0.005	0.005	0.000	0.000	0.000	0.000
118	A	120	PRO	0	0.031	0.008	32.799	-0.006	-0.006	0.000	0.000	0.000	0.000
119	A	121	PHE	0	0.054	0.003	35.156	0.003	0.003	0.000	0.000	0.000	0.000
120	A	122	ASP	-1	-0.798	-0.885	35.289	-0.146	-0.146	0.000	0.000	0.000	0.000
121	A	123	ARG	1	0.733	0.828	33.176	0.168	0.168	0.000	0.000	0.000	0.000
122	A	124	LEU	0	-0.042	-0.009	37.973	0.000	0.000	0.000	0.000	0.000	0.000
123	A	125	GLU	-1	-0.788	-0.877	41.048	-0.094	-0.094	0.000	0.000	0.000	0.000
124	A	126	ILE	0	-0.036	-0.016	44.495	-0.001	-0.001	0.000	0.000	0.000	0.000
125	A	127	ASP	-1	-0.784	-0.890	47.244	-0.090	-0.090	0.000	0.000	0.000	0.000
126	A	128	LEU	0	-0.010	-0.026	50.302	0.000	0.000	0.000	0.000	0.000	0.000
127	A	129	LEU	0	-0.014	-0.002	51.959	0.001	0.001	0.000	0.000	0.000	0.000
128	A	130	LYS	1	0.834	0.907	56.197	0.056	0.056	0.000	0.000	0.000	0.000
129	A	131	GLY	0	0.003	0.003	57.929	0.003	0.003	0.000	0.000	0.000	0.000
130	A	132	ASP	-1	-0.909	-0.953	56.121	-0.068	-0.068	0.000	0.000	0.000	0.000
131	A	133	HIS	0	-0.019	-0.012	56.594	-0.001	-0.001	0.000	0.000	0.000	0.000
132	A	134	LEU	0	0.028	0.014	51.844	0.000	0.000	0.000	0.000	0.000	0.000
133	A	135	MET	0	-0.084	-0.033	56.094	0.002	0.002	0.000	0.000	0.000	0.000
134	A	136	LYS	1	0.872	0.928	53.243	0.073	0.073	0.000	0.000	0.000	0.000
135	A	137	SER	0	-0.024	-0.011	49.415	0.000	0.000	0.000	0.000	0.000	0.000
136	A	138	GLN	0	-0.078	-0.051	47.896	0.007	0.007	0.000	0.000	0.000	0.000
137	A	139	GLU	-1	-0.872	-0.922	44.197	-0.104	-0.104	0.000	0.000	0.000	0.000
138	A	140	PHE	0	-0.022	-0.030	42.388	0.005	0.005	0.000	0.000	0.000	0.000
139	A	141	LEU	0	0.007	0.005	40.470	-0.005	-0.005	0.000	0.000	0.000	0.000
140	A	142	GLU	-1	-0.954	-0.954	40.925	-0.098	-0.098	0.000	0.000	0.000	0.000
141	A	143	ASP	-1	-0.830	-0.930	39.929	-0.106	-0.106	0.000	0.000	0.000	0.000
142	A	144	ALA	0	-0.037	-0.019	41.027	0.000	0.000	0.000	0.000	0.000	0.000
143	A	145	ASP	-1	-0.844	-0.909	37.541	-0.117	-0.117	0.000	0.000	0.000	0.000
144	A	146	ARG	1	0.850	0.891	31.549	0.158	0.158	0.000	0.000	0.000	0.000
145	A	147	LYS	1	0.781	0.876	28.856	0.178	0.178	0.000	0.000	0.000	0.000
146	A	148	SER	0	-0.008	0.007	34.877	0.000	0.000	0.000	0.000	0.000	0.000
147	A	149	LEU	0	-0.086	-0.037	34.803	0.001	0.001	0.000	0.000	0.000	0.000
148	A	150	GLU	-1	-0.879	-0.934	38.548	-0.091	-0.091	0.000	0.000	0.000	0.000
149	A	151	THR	0	-0.035	-0.029	42.294	-0.004	-0.004	0.000	0.000	0.000	0.000
150	A	152	LYS	1	0.815	0.932	42.016	0.108	0.108	0.000	0.000	0.000	0.000
151	A	153	SER	0	-0.026	-0.044	45.920	0.001	0.001	0.000	0.000	0.000	0.000
152	A	154	LEU	0	-0.036	-0.009	49.421	0.000	0.000	0.000	0.000	0.000	0.000
153	A	155	GLU	-1	-0.749	-0.867	51.759	-0.068	-0.068	0.000	0.000	0.000	0.000
154	A	156	VAL	0	-0.040	-0.014	55.406	-0.001	-0.001	0.000	0.000	0.000	0.000
155	A	157	THR	0	-0.005	-0.020	58.289	0.000	0.000	0.000	0.000	0.000	0.000
156	A	158	PHE	0	-0.025	-0.009	62.102	0.000	0.000	0.000	0.000	0.000	0.000
157	A	159	THR	0	0.025	0.022	64.619	0.001	0.001	0.000	0.000	0.000	0.000
158	A	160	PRO	0	-0.008	0.017	66.526	-0.001	-0.001	0.000	0.000	0.000	0.000
159	A	161	VAL	0	0.012	0.000	67.967	0.002	0.002	0.000	0.000	0.000	0.000
160	A	162	ILE	0	0.030	0.011	70.297	-0.001	-0.001	0.000	0.000	0.000	0.000
161	A	163	GLU	-1	-0.855	-0.948	70.027	-0.045	-0.045	0.000	0.000	0.000	0.000
162	A	164	ASP	-1	-0.811	-0.905	66.129	-0.054	-0.054	0.000	0.000	0.000	0.000
163	A	165	ILE	0	-0.021	0.003	66.352	-0.002	-0.002	0.000	0.000	0.000	0.000
164	A	166	GLY	0	0.018	0.026	66.113	0.001	0.001	0.000	0.000	0.000	0.000
165	A	167	LYS	1	0.798	0.903	62.849	0.051	0.051	0.000	0.000	0.000	0.000
166	A	168	VAL	0	-0.006	-0.018	57.446	0.000	0.000	0.000	0.000	0.000	0.000
167	A	169	LEU	0	-0.005	0.005	57.763	-0.001	-0.001	0.000	0.000	0.000	0.000
168	A	170	VAL	0	-0.012	-0.006	52.462	-0.001	-0.001	0.000	0.000	0.000	0.000
169	A	172	ARG	1	0.911	0.945	47.453	0.086	0.086	0.000	0.000	0.000	0.000
170	A	173	ALA	0	0.023	0.018	43.598	0.002	0.002	0.000	0.000	0.000	0.000
171	A	174	LYS	1	0.780	0.870	42.510	0.095	0.095	0.000	0.000	0.000	0.000
172	A	175	LEU	0	0.039	0.010	35.582	0.001	0.001	0.000	0.000	0.000	0.000
173	A	176	HIS	0	0.004	-0.001	36.528	-0.007	-0.007	0.000	0.000	0.000	0.000
174	A	177	ILE	0	0.007	-0.002	32.285	-0.002	-0.002	0.000	0.000	0.000	0.000
175	A	178	ASP	-1	-0.852	-0.924	31.069	-0.231	-0.231	0.000	0.000	0.000	0.000
176	A	179	GLU	-1	-0.823	-0.875	30.471	-0.176	-0.176	0.000	0.000	0.000	0.000
177	A	180	MET	0	-0.127	-0.062	27.696	-0.006	-0.006	0.000	0.000	0.000	0.000
178	A	181	ASP	-1	-0.832	-0.904	32.847	-0.147	-0.147	0.000	0.000	0.000	0.000
179	A	182	SER	0	-0.102	-0.049	36.190	0.005	0.005	0.000	0.000	0.000	0.000
180	A	183	VAL	0	-0.068	-0.038	39.415	0.007	0.007	0.000	0.000	0.000	0.000
181	A	184	PRO	0	0.004	0.004	38.654	-0.006	-0.006	0.000	0.000	0.000	0.000
182	A	185	THR	0	0.020	0.021	36.605	0.001	0.001	0.000	0.000	0.000	0.000
183	A	186	VAL	0	-0.045	-0.028	38.998	0.005	0.005	0.000	0.000	0.000	0.000
184	A	187	ARG	1	0.828	0.924	39.244	0.122	0.122	0.000	0.000	0.000	0.000
185	A	188	GLN	0	0.019	-0.002	44.422	0.002	0.002	0.000	0.000	0.000	0.000
186	A	189	ALA	0	0.014	0.031	48.213	0.000	0.000	0.000	0.000	0.000	0.000
187	A	190	VAL	0	0.006	-0.018	51.183	0.001	0.001	0.000	0.000	0.000	0.000
188	A	191	LYS	1	0.905	0.955	54.936	0.058	0.058	0.000	0.000	0.000	0.000
189	A	192	GLU	-1	-0.826	-0.900	58.356	-0.055	-0.055	0.000	0.000	0.000	0.000
190	A	193	LEU	0	-0.043	-0.028	61.668	0.001	0.001	0.000	0.000	0.000	0.000
191	A	194	GLN	0	-0.042	-0.035	64.590	0.003	0.003	0.000	0.000	0.000	0.000
192	A	195	VAL	0	0.024	0.003	67.075	0.000	0.000	0.000	0.000	0.000	0.000
193	A	196	ASP	-1	-1.010	-0.992	70.540	-0.041	-0.041	0.000	0.000	0.000	0.000

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