FMO DATABASE

FMODB ID: 9R3Y2

Calculation Name: 4Z3G-A-Xray547

Preferred Name:

Target Type:

Ligand Name: 2-(n-morpholino)-ethanesulfonic acid | beta-d-galactopyranose | alpha-d-galactopyranose | 4-methoxyphenol

Ligand 3-letter code: MES | GAL | GLA | 4KS

Ligand of Interest (LOI):

PDB ID: 4Z3G

Chain ID: A

ChEMBL ID:

UniProt ID: A0A182

Base Structure: X-ray

Registration Date: 2025-10-05

Reference: Sci Data 11, 1164 (2024).

DOI: https://doi.org/10.1038/s41597-024-03999-2

Apendix: None

IFIE MAP

IFIE Diagram

Modeling method

Optimization	MOE:Amber10:EHT
Restraint	OptAll
Protonation	MOE:Protonate 3D
Complement	MOE:Homology Modeling
Water	No
Procedure	Manual calculation

FMO calculation

FMO method	FMO2-MP2/6-31G(d)
Fragmentation	Auto
Number of fragment	197
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230922

Total energy (hartree)

FMO2-HF: Electronic energy	-2242931.865285
FMO2-HF: Nuclear repulsion	2163897.470682
FMO2-HF: Total energy	-79034.394603
FMO2-MP2: Total energy	-79267.588577

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:MET)

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

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.
-5.399	-2.239	0.259	-1.633	-1.786	-0.01

Interaction energy analysis for fragmet #1(A:-1:MET)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 1 / q_Mulliken : 0.853 / q_NPA : 0.921

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	1	TRP	0	-0.001	0.010	3.082	-5.129	-2.063	0.260	-1.628	-1.698	-0.010
4	A	2	ASN	0	0.023	0.007	5.342	5.232	5.326	-0.001	-0.005	-0.088	0.000
5	A	3	ASN	0	0.033	0.023	8.945	-2.065	-2.065	0.000	0.000	0.000	0.000
6	A	4	ILE	0	-0.030	-0.015	11.717	0.996	0.996	0.000	0.000	0.000	0.000
7	A	5	VAL	0	0.040	0.018	15.193	0.051	0.051	0.000	0.000	0.000	0.000
8	A	6	PHE	0	-0.040	-0.011	18.440	0.229	0.229	0.000	0.000	0.000	0.000
9	A	7	TYR	0	-0.056	-0.060	20.832	0.007	0.007	0.000	0.000	0.000	0.000
10	A	8	SER	0	-0.026	-0.038	24.875	0.222	0.222	0.000	0.000	0.000	0.000
11	A	9	LEU	0	-0.006	-0.015	28.112	0.023	0.023	0.000	0.000	0.000	0.000
12	A	10	GLY	0	0.033	0.028	31.569	0.093	0.093	0.000	0.000	0.000	0.000
13	A	11	ASP	-1	-0.885	-0.932	34.419	-7.897	-7.897	0.000	0.000	0.000	0.000
14	A	12	VAL	0	0.057	0.033	37.317	-0.013	-0.013	0.000	0.000	0.000	0.000
15	A	13	ASN	0	-0.002	-0.010	40.674	0.230	0.230	0.000	0.000	0.000	0.000
16	A	14	SER	0	-0.008	-0.001	43.086	0.088	0.088	0.000	0.000	0.000	0.000
17	A	15	TYR	0	0.032	0.006	46.310	-0.004	-0.004	0.000	0.000	0.000	0.000
18	A	16	GLN	0	-0.006	-0.005	48.321	0.121	0.121	0.000	0.000	0.000	0.000
19	A	17	GLY	0	0.017	0.014	51.969	0.005	0.005	0.000	0.000	0.000	0.000
20	A	18	GLY	0	-0.010	0.003	53.253	0.089	0.089	0.000	0.000	0.000	0.000
21	A	19	ASN	0	-0.022	-0.022	56.788	-0.041	-0.041	0.000	0.000	0.000	0.000
22	A	20	VAL	0	-0.010	-0.002	55.157	-0.007	-0.007	0.000	0.000	0.000	0.000
23	A	21	VAL	0	0.050	0.023	58.464	0.036	0.036	0.000	0.000	0.000	0.000
24	A	22	ILE	0	-0.012	-0.015	56.561	-0.112	-0.112	0.000	0.000	0.000	0.000
25	A	23	THR	0	-0.008	-0.004	56.577	-0.100	-0.100	0.000	0.000	0.000	0.000
26	A	24	GLN	0	-0.014	0.007	55.396	-0.019	-0.019	0.000	0.000	0.000	0.000
27	A	25	ARG	1	0.870	0.929	49.574	6.092	6.092	0.000	0.000	0.000	0.000
28	A	26	PRO	0	0.004	0.020	51.351	-0.044	-0.044	0.000	0.000	0.000	0.000
29	A	27	GLN	0	0.025	-0.011	47.858	-0.060	-0.060	0.000	0.000	0.000	0.000
30	A	28	PHE	0	-0.004	-0.007	41.980	0.074	0.074	0.000	0.000	0.000	0.000
31	A	29	ILE	0	-0.033	-0.008	43.055	-0.112	-0.112	0.000	0.000	0.000	0.000
32	A	30	THR	0	-0.040	-0.025	39.084	-0.036	-0.036	0.000	0.000	0.000	0.000
33	A	31	SER	0	0.002	-0.020	39.565	-0.072	-0.072	0.000	0.000	0.000	0.000
34	A	32	TRP	0	-0.034	-0.009	29.265	-0.030	-0.030	0.000	0.000	0.000	0.000
35	A	33	ARG	1	0.873	0.911	36.112	7.909	7.909	0.000	0.000	0.000	0.000
36	A	34	PRO	0	-0.025	-0.005	33.505	-0.187	-0.187	0.000	0.000	0.000	0.000
37	A	35	GLY	0	0.005	-0.002	32.858	0.336	0.336	0.000	0.000	0.000	0.000
38	A	36	ILE	0	-0.049	-0.021	30.975	-0.299	-0.299	0.000	0.000	0.000	0.000
39	A	37	ALA	0	0.019	0.013	27.883	0.198	0.198	0.000	0.000	0.000	0.000
40	A	38	THR	0	0.036	0.011	27.381	-0.263	-0.263	0.000	0.000	0.000	0.000
41	A	39	VAL	0	-0.050	-0.007	20.942	-0.058	-0.058	0.000	0.000	0.000	0.000
42	A	40	THR	0	0.027	0.004	24.163	-0.018	-0.018	0.000	0.000	0.000	0.000
43	A	41	TRP	0	0.009	-0.001	16.674	-0.083	-0.083	0.000	0.000	0.000	0.000
44	A	42	ASN	0	-0.047	-0.031	16.922	-0.071	-0.071	0.000	0.000	0.000	0.000
45	A	43	GLN	0	0.022	0.021	12.750	1.113	1.113	0.000	0.000	0.000	0.000
46	A	44	CYS	0	-0.097	-0.065	10.976	-1.021	-1.021	0.000	0.000	0.000	0.000
47	A	45	ASN	0	0.026	0.017	5.851	-0.189	-0.189	0.000	0.000	0.000	0.000
48	A	46	GLY	0	0.026	0.013	5.805	-6.552	-6.552	0.000	0.000	0.000	0.000
49	A	47	PRO	0	-0.032	-0.016	7.188	2.444	2.444	0.000	0.000	0.000	0.000
50	A	48	GLU	-1	-0.905	-0.950	9.969	-18.924	-18.924	0.000	0.000	0.000	0.000
51	A	49	PHE	0	-0.022	-0.019	13.513	1.297	1.297	0.000	0.000	0.000	0.000
52	A	50	ALA	0	0.018	0.025	13.465	-1.600	-1.600	0.000	0.000	0.000	0.000
53	A	51	ASP	-1	-0.800	-0.901	14.959	-17.682	-17.682	0.000	0.000	0.000	0.000
54	A	52	GLY	0	0.011	0.017	17.408	1.104	1.104	0.000	0.000	0.000	0.000
55	A	53	SER	0	-0.080	-0.050	16.433	0.182	0.182	0.000	0.000	0.000	0.000
56	A	54	TRP	0	-0.022	-0.018	10.732	-1.374	-1.374	0.000	0.000	0.000	0.000
57	A	55	ALA	0	-0.033	-0.016	13.268	0.404	0.404	0.000	0.000	0.000	0.000
58	A	56	TYR	0	-0.035	-0.019	11.769	-2.332	-2.332	0.000	0.000	0.000	0.000
59	A	57	TYR	0	-0.005	-0.010	12.091	1.958	1.958	0.000	0.000	0.000	0.000
60	A	58	ARG	1	0.884	0.946	14.566	15.255	15.255	0.000	0.000	0.000	0.000
61	A	59	GLU	-1	-0.801	-0.898	16.650	-16.997	-16.997	0.000	0.000	0.000	0.000
62	A	60	TYR	0	-0.050	-0.033	18.447	-0.338	-0.338	0.000	0.000	0.000	0.000
63	A	61	ILE	0	0.011	-0.004	20.241	0.547	0.547	0.000	0.000	0.000	0.000
64	A	62	ALA	0	0.009	0.017	23.466	-0.114	-0.114	0.000	0.000	0.000	0.000
65	A	63	TRP	0	-0.003	-0.018	22.557	0.252	0.252	0.000	0.000	0.000	0.000
66	A	64	VAL	0	0.015	-0.004	28.040	0.151	0.151	0.000	0.000	0.000	0.000
67	A	65	VAL	0	-0.028	-0.004	28.586	-0.013	-0.013	0.000	0.000	0.000	0.000
68	A	66	PHE	0	0.034	0.016	31.830	0.109	0.109	0.000	0.000	0.000	0.000
69	A	67	PRO	0	-0.010	0.008	35.587	-0.063	-0.063	0.000	0.000	0.000	0.000
70	A	68	LYS	1	0.843	0.910	36.025	8.559	8.559	0.000	0.000	0.000	0.000
71	A	69	LYS	1	0.904	0.959	39.815	7.287	7.287	0.000	0.000	0.000	0.000
72	A	70	VAL	0	0.009	0.006	41.614	-0.189	-0.189	0.000	0.000	0.000	0.000
73	A	71	MET	0	-0.010	0.017	44.065	0.107	0.107	0.000	0.000	0.000	0.000
74	A	72	THR	0	0.005	-0.011	46.831	-0.076	-0.076	0.000	0.000	0.000	0.000
75	A	73	LYS	1	0.974	0.971	48.253	6.475	6.475	0.000	0.000	0.000	0.000
76	A	74	ASN	0	0.008	0.013	50.821	-0.072	-0.072	0.000	0.000	0.000	0.000
77	A	75	GLY	0	0.029	0.019	50.802	0.088	0.088	0.000	0.000	0.000	0.000
78	A	76	TYR	0	0.009	0.013	51.314	-0.029	-0.029	0.000	0.000	0.000	0.000
79	A	77	PRO	0	-0.030	-0.021	48.034	-0.131	-0.131	0.000	0.000	0.000	0.000
80	A	78	LEU	0	0.036	0.016	47.245	0.114	0.114	0.000	0.000	0.000	0.000
81	A	79	PHE	0	-0.003	-0.015	45.193	-0.220	-0.220	0.000	0.000	0.000	0.000
82	A	80	ILE	0	-0.003	0.010	41.150	0.123	0.123	0.000	0.000	0.000	0.000
83	A	81	GLU	-1	-0.784	-0.868	42.375	-6.741	-6.741	0.000	0.000	0.000	0.000
84	A	82	VAL	0	0.039	0.011	38.597	0.017	0.017	0.000	0.000	0.000	0.000
85	A	83	HIS	0	-0.036	-0.019	41.923	0.116	0.116	0.000	0.000	0.000	0.000
86	A	84	ASN	0	0.006	-0.009	41.960	-0.107	-0.107	0.000	0.000	0.000	0.000
87	A	85	LYS	1	0.937	0.988	35.355	8.607	8.607	0.000	0.000	0.000	0.000
88	A	86	GLY	0	0.055	0.035	37.060	-0.254	-0.254	0.000	0.000	0.000	0.000
89	A	87	SER	0	-0.057	-0.035	34.558	-0.174	-0.174	0.000	0.000	0.000	0.000
90	A	88	TRP	0	-0.069	-0.028	29.683	-0.525	-0.525	0.000	0.000	0.000	0.000
91	A	89	SER	0	-0.064	-0.031	28.490	0.366	0.366	0.000	0.000	0.000	0.000
92	A	90	GLU	-1	-0.858	-0.950	31.097	-8.582	-8.582	0.000	0.000	0.000	0.000
93	A	91	GLU	-1	-0.773	-0.837	26.252	-11.690	-11.690	0.000	0.000	0.000	0.000
94	A	92	ASN	0	-0.020	-0.019	28.318	0.151	0.151	0.000	0.000	0.000	0.000
95	A	93	THR	0	0.039	0.016	30.267	0.107	0.107	0.000	0.000	0.000	0.000
96	A	94	GLY	0	0.015	0.007	33.373	0.266	0.266	0.000	0.000	0.000	0.000
97	A	95	ASP	-1	-0.806	-0.867	32.003	-9.288	-9.288	0.000	0.000	0.000	0.000
98	A	96	ASN	0	0.023	0.006	34.184	0.242	0.242	0.000	0.000	0.000	0.000
99	A	97	ASP	-1	-0.860	-0.922	35.125	-8.340	-8.340	0.000	0.000	0.000	0.000
100	A	98	SER	0	-0.070	-0.050	32.932	0.030	0.030	0.000	0.000	0.000	0.000
101	A	99	TYR	0	-0.020	-0.016	34.078	-0.080	-0.080	0.000	0.000	0.000	0.000
102	A	100	PHE	0	0.028	-0.008	28.498	-0.215	-0.215	0.000	0.000	0.000	0.000
103	A	101	PHE	0	0.003	0.010	30.971	0.042	0.042	0.000	0.000	0.000	0.000
104	A	102	LEU	0	-0.003	-0.004	24.430	-0.284	-0.284	0.000	0.000	0.000	0.000
105	A	103	LYS	1	0.865	0.918	27.495	10.456	10.456	0.000	0.000	0.000	0.000
106	A	104	GLY	0	0.047	0.033	24.275	-0.332	-0.332	0.000	0.000	0.000	0.000
107	A	105	TYR	0	-0.077	-0.074	24.716	0.257	0.257	0.000	0.000	0.000	0.000
108	A	106	LYS	1	0.831	0.921	21.203	13.827	13.827	0.000	0.000	0.000	0.000
109	A	107	TRP	0	0.047	0.029	19.247	-0.272	-0.272	0.000	0.000	0.000	0.000
110	A	108	ASP	-1	-0.757	-0.850	16.923	-17.072	-17.072	0.000	0.000	0.000	0.000
111	A	109	GLN	0	0.056	0.039	18.254	-0.034	-0.034	0.000	0.000	0.000	0.000
112	A	110	ARG	1	0.954	0.977	13.686	19.558	19.558	0.000	0.000	0.000	0.000
113	A	111	ALA	0	-0.055	-0.023	16.868	1.279	1.279	0.000	0.000	0.000	0.000
114	A	112	PHE	0	0.028	0.007	16.487	-1.324	-1.324	0.000	0.000	0.000	0.000
115	A	113	ASP	-1	-0.899	-0.943	17.661	-14.767	-14.767	0.000	0.000	0.000	0.000
116	A	114	THR	0	-0.016	-0.004	18.944	-0.538	-0.538	0.000	0.000	0.000	0.000
117	A	115	ALA	0	-0.013	0.000	17.965	0.803	0.803	0.000	0.000	0.000	0.000
118	A	116	ASN	0	0.034	0.016	17.128	-1.874	-1.874	0.000	0.000	0.000	0.000
119	A	117	LEU	0	-0.036	-0.014	12.220	0.290	0.290	0.000	0.000	0.000	0.000
120	A	119	GLN	0	-0.004	0.024	15.622	0.393	0.393	0.000	0.000	0.000	0.000
121	A	120	LYS	1	0.983	0.982	17.738	16.367	16.367	0.000	0.000	0.000	0.000
122	A	121	PRO	0	0.014	-0.011	19.889	0.506	0.506	0.000	0.000	0.000	0.000
123	A	122	GLY	0	-0.002	0.013	23.047	0.159	0.159	0.000	0.000	0.000	0.000
124	A	123	GLU	-1	-0.836	-0.893	21.299	-14.263	-14.263	0.000	0.000	0.000	0.000
125	A	124	THR	0	-0.010	-0.012	25.246	0.147	0.147	0.000	0.000	0.000	0.000
126	A	125	THR	0	0.003	0.011	24.750	-0.254	-0.254	0.000	0.000	0.000	0.000
127	A	126	ARG	1	0.947	0.977	26.979	9.874	9.874	0.000	0.000	0.000	0.000
128	A	127	LEU	0	-0.020	0.001	25.982	-0.417	-0.417	0.000	0.000	0.000	0.000
129	A	128	THR	0	-0.004	-0.021	29.398	0.321	0.321	0.000	0.000	0.000	0.000
130	A	129	GLU	-1	-0.779	-0.848	26.596	-11.560	-11.560	0.000	0.000	0.000	0.000
131	A	130	LYS	1	0.824	0.929	31.251	8.495	8.495	0.000	0.000	0.000	0.000
132	A	131	PHE	0	-0.020	-0.011	28.348	-0.109	-0.109	0.000	0.000	0.000	0.000
133	A	132	ASP	-1	-0.788	-0.916	34.241	-8.054	-8.054	0.000	0.000	0.000	0.000
134	A	133	ASP	-1	-0.812	-0.889	36.536	-8.035	-8.035	0.000	0.000	0.000	0.000
135	A	134	ILE	0	-0.039	-0.006	34.609	-0.006	-0.006	0.000	0.000	0.000	0.000
136	A	135	ILE	0	-0.032	-0.002	39.293	0.120	0.120	0.000	0.000	0.000	0.000
137	A	136	PHE	0	0.043	0.016	37.526	-0.067	-0.067	0.000	0.000	0.000	0.000
138	A	137	LYS	1	0.848	0.912	43.556	6.888	6.888	0.000	0.000	0.000	0.000
139	A	138	VAL	0	-0.003	0.007	46.107	-0.121	-0.121	0.000	0.000	0.000	0.000
140	A	139	ALA	0	-0.021	-0.004	48.143	0.155	0.155	0.000	0.000	0.000	0.000
141	A	140	LEU	0	0.013	0.002	49.950	-0.099	-0.099	0.000	0.000	0.000	0.000
142	A	141	PRO	0	-0.025	0.001	51.705	0.033	0.033	0.000	0.000	0.000	0.000
143	A	142	ALA	0	0.029	-0.011	53.926	0.058	0.058	0.000	0.000	0.000	0.000
144	A	143	ASP	-1	-0.877	-0.940	56.063	-5.599	-5.599	0.000	0.000	0.000	0.000
145	A	144	LEU	0	-0.059	-0.011	53.813	-0.004	-0.004	0.000	0.000	0.000	0.000
146	A	145	PRO	0	0.000	0.004	56.887	0.094	0.094	0.000	0.000	0.000	0.000
147	A	146	LEU	0	0.038	0.040	58.947	-0.083	-0.083	0.000	0.000	0.000	0.000
148	A	147	GLY	0	-0.008	0.005	60.708	0.016	0.016	0.000	0.000	0.000	0.000
149	A	148	ASP	-1	-0.885	-0.934	57.655	-5.392	-5.392	0.000	0.000	0.000	0.000
150	A	149	TYR	0	-0.020	-0.019	52.744	-0.092	-0.092	0.000	0.000	0.000	0.000
151	A	150	SER	0	-0.019	-0.016	51.017	-0.062	-0.062	0.000	0.000	0.000	0.000
152	A	151	VAL	0	-0.012	-0.019	46.090	-0.018	-0.018	0.000	0.000	0.000	0.000
153	A	152	THR	0	0.018	0.014	42.307	0.028	0.028	0.000	0.000	0.000	0.000
154	A	153	ILE	0	-0.036	-0.011	40.186	-0.010	-0.010	0.000	0.000	0.000	0.000
155	A	154	PRO	0	0.036	0.018	37.686	-0.105	-0.105	0.000	0.000	0.000	0.000
156	A	155	TYR	0	-0.033	-0.030	34.588	0.022	0.022	0.000	0.000	0.000	0.000
157	A	156	THR	0	0.036	0.012	28.567	-0.003	-0.003	0.000	0.000	0.000	0.000
158	A	157	SER	0	-0.050	-0.041	30.742	0.031	0.031	0.000	0.000	0.000	0.000
159	A	158	GLY	0	0.066	0.027	27.696	-0.003	-0.003	0.000	0.000	0.000	0.000
160	A	159	ILE	0	-0.054	-0.033	23.306	0.030	0.030	0.000	0.000	0.000	0.000
161	A	160	GLN	0	0.039	0.027	18.414	0.201	0.201	0.000	0.000	0.000	0.000
162	A	161	ARG	1	0.832	0.898	19.445	13.380	13.380	0.000	0.000	0.000	0.000
163	A	162	HIS	0	-0.031	-0.033	12.325	-1.953	-1.953	0.000	0.000	0.000	0.000
164	A	163	PHE	0	0.019	0.004	13.271	0.811	0.811	0.000	0.000	0.000	0.000
165	A	164	ALA	0	0.027	0.014	9.986	-1.629	-1.629	0.000	0.000	0.000	0.000
166	A	165	SER	0	0.024	0.004	6.616	-0.223	-0.223	0.000	0.000	0.000	0.000
167	A	166	TYR	0	-0.098	-0.059	8.053	-0.285	-0.285	0.000	0.000	0.000	0.000
168	A	167	LEU	0	0.021	0.011	10.585	1.382	1.382	0.000	0.000	0.000	0.000
169	A	168	GLY	0	0.012	0.003	13.010	-0.803	-0.803	0.000	0.000	0.000	0.000
170	A	169	ALA	0	-0.027	0.000	11.546	0.155	0.155	0.000	0.000	0.000	0.000
171	A	170	ARG	1	0.780	0.848	12.845	18.762	18.762	0.000	0.000	0.000	0.000
172	A	171	PHE	0	0.007	0.001	13.713	-0.990	-0.990	0.000	0.000	0.000	0.000
173	A	172	LYS	1	0.857	0.918	15.813	13.687	13.687	0.000	0.000	0.000	0.000
174	A	173	ILE	0	0.024	0.027	18.734	-0.401	-0.401	0.000	0.000	0.000	0.000
175	A	174	PRO	0	0.015	0.005	18.968	0.622	0.622	0.000	0.000	0.000	0.000
176	A	175	TYR	0	-0.001	-0.033	21.896	0.110	0.110	0.000	0.000	0.000	0.000
177	A	176	ASN	0	0.012	-0.005	25.439	0.483	0.483	0.000	0.000	0.000	0.000
178	A	177	VAL	0	0.029	0.027	21.255	0.206	0.206	0.000	0.000	0.000	0.000
179	A	178	ALA	0	0.024	0.014	24.611	0.282	0.282	0.000	0.000	0.000	0.000
180	A	179	LYS	1	0.790	0.885	26.116	9.797	9.797	0.000	0.000	0.000	0.000
181	A	180	THR	0	-0.056	-0.034	26.748	0.329	0.329	0.000	0.000	0.000	0.000
182	A	181	LEU	0	-0.002	0.016	23.874	-0.166	-0.166	0.000	0.000	0.000	0.000
183	A	182	PRO	0	0.015	0.001	27.510	0.373	0.373	0.000	0.000	0.000	0.000
184	A	183	ARG	1	0.800	0.915	30.437	9.145	9.145	0.000	0.000	0.000	0.000
185	A	184	GLU	-1	-0.837	-0.902	30.397	-10.067	-10.067	0.000	0.000	0.000	0.000
186	A	185	ASN	0	-0.017	0.041	33.824	-0.095	-0.095	0.000	0.000	0.000	0.000
187	A	186	GLU	-1	-0.901	-0.961	36.251	-7.578	-7.578	0.000	0.000	0.000	0.000
188	A	187	MET	0	-0.063	-0.011	39.901	0.115	0.115	0.000	0.000	0.000	0.000
189	A	188	LEU	0	-0.007	-0.009	42.307	0.071	0.071	0.000	0.000	0.000	0.000
190	A	189	PHE	0	0.031	0.001	45.806	0.091	0.091	0.000	0.000	0.000	0.000
191	A	190	LEU	0	-0.034	-0.009	48.030	0.071	0.071	0.000	0.000	0.000	0.000
192	A	191	PHE	0	-0.002	-0.009	50.817	0.011	0.011	0.000	0.000	0.000	0.000
193	A	192	LYS	1	0.895	0.933	54.661	5.222	5.222	0.000	0.000	0.000	0.000
194	A	193	ASN	0	-0.017	-0.011	57.324	0.037	0.037	0.000	0.000	0.000	0.000
195	A	194	ILE	0	-0.042	-0.034	58.914	0.077	0.077	0.000	0.000	0.000	0.000
196	A	195	GLY	0	0.038	0.020	61.072	0.095	0.095	0.000	0.000	0.000	0.000
197	A	196	GLY	-1	-0.932	-0.953	61.810	-4.990	-4.990	0.000	0.000	0.000	0.000

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