FMO DATABASE

FMODB ID: 46LQN

Calculation Name: 3MW4-A-Xray547

Preferred Name:

Target Type:

Ligand Name: 2-acetamido-2-deoxy-beta-d-glucopyranose | beta-d-mannopyranose | calcium ion

Ligand 3-letter code: NAG | BMA | CA

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 3MW4

Chain ID: A

ChEMBL ID:

UniProt ID: Q6P9K9

Base Structure: X-ray

Registration Date: 2025-10-04

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
Remarks	ac.sh, 23 2024 Oct; Missing atoms/residues were imported from a 100% homology model, which was constructed by MOE.

FMO calculation

FMO method	FMO2-MP2/6-31G(d)
Fragmentation	Auto
Number of fragment	178
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230922

Total energy (hartree)

FMO2-HF: Electronic energy	-1834058.902797
FMO2-HF: Nuclear repulsion	1767429.863341
FMO2-HF: Total energy	-66629.039457
FMO2-MP2: Total energy	-66828.296111

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:79:GLY)

Summations of interaction energy for fragment #1(A:79:GLY)

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.
68.813	70.782	5.293	-3.679	-3.584	-0.041

Interaction energy analysis for fragmet #1(A:79:GLY)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 1 / q_Mulliken : 0.834 / q_NPA : 0.905

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	81	GLY	0	0.066	0.049	3.653	5.167	6.297	0.001	-0.490	-0.641	-0.002
4	A	82	SER	0	-0.071	-0.031	2.027	-21.311	-20.757	5.290	-3.031	-2.814	-0.038
5	A	83	ALA	0	0.057	0.046	3.790	4.386	4.671	0.002	-0.158	-0.129	-0.001
6	A	84	THR	0	0.014	0.005	7.059	-2.038	-2.038	0.000	0.000	0.000	0.000
7	A	85	TYR	0	0.018	0.005	9.279	2.955	2.955	0.000	0.000	0.000	0.000
8	A	86	ILE	0	0.003	0.006	12.927	-0.227	-0.227	0.000	0.000	0.000	0.000
9	A	87	PHE	0	0.009	0.004	14.575	0.848	0.848	0.000	0.000	0.000	0.000
10	A	88	GLY	0	0.057	0.021	18.576	0.039	0.039	0.000	0.000	0.000	0.000
11	A	89	LYS	1	0.972	0.979	21.912	11.688	11.688	0.000	0.000	0.000	0.000
12	A	90	SER	0	-0.007	0.000	25.005	0.262	0.262	0.000	0.000	0.000	0.000
13	A	91	GLY	0	0.035	0.032	23.152	0.400	0.400	0.000	0.000	0.000	0.000
14	A	92	GLY	0	-0.016	-0.013	21.791	0.540	0.540	0.000	0.000	0.000	0.000
15	A	93	LEU	0	-0.039	-0.014	20.853	-0.171	-0.171	0.000	0.000	0.000	0.000
16	A	94	ILE	0	0.001	0.006	15.016	-0.031	-0.031	0.000	0.000	0.000	0.000
17	A	95	LEU	0	-0.003	-0.008	18.870	-0.141	-0.141	0.000	0.000	0.000	0.000
18	A	96	TYR	0	0.028	0.011	17.887	-0.166	-0.166	0.000	0.000	0.000	0.000
19	A	97	THR	0	-0.027	-0.016	20.001	0.593	0.593	0.000	0.000	0.000	0.000
20	A	98	TRP	0	0.025	0.003	19.824	-0.410	-0.410	0.000	0.000	0.000	0.000
21	A	99	PRO	0	0.025	0.014	23.314	0.588	0.588	0.000	0.000	0.000	0.000
22	A	100	ALA	0	-0.038	-0.025	26.482	-0.021	-0.021	0.000	0.000	0.000	0.000
23	A	101	ASN	0	-0.012	-0.010	29.163	0.423	0.423	0.000	0.000	0.000	0.000
24	A	102	ASP	-1	-0.873	-0.934	24.114	-12.349	-12.349	0.000	0.000	0.000	0.000
25	A	103	ARG	1	0.897	0.955	24.436	10.395	10.395	0.000	0.000	0.000	0.000
26	A	104	PRO	0	-0.006	0.022	21.936	0.409	0.409	0.000	0.000	0.000	0.000
27	A	105	SER	0	0.039	0.021	25.145	0.262	0.262	0.000	0.000	0.000	0.000
28	A	106	THR	0	-0.043	-0.038	22.262	0.269	0.269	0.000	0.000	0.000	0.000
29	A	107	ARG	1	0.978	0.995	25.485	10.706	10.706	0.000	0.000	0.000	0.000
30	A	108	SER	0	0.010	0.008	22.390	0.249	0.249	0.000	0.000	0.000	0.000
31	A	109	ASP	-1	-0.721	-0.783	19.708	-14.469	-14.469	0.000	0.000	0.000	0.000
32	A	110	ARG	1	0.921	0.958	11.592	22.546	22.546	0.000	0.000	0.000	0.000
33	A	111	LEU	0	0.020	0.019	14.105	-0.727	-0.727	0.000	0.000	0.000	0.000
34	A	112	ALA	0	-0.046	-0.025	10.266	0.209	0.209	0.000	0.000	0.000	0.000
35	A	113	VAL	0	0.014	0.010	9.113	-1.123	-1.123	0.000	0.000	0.000	0.000
36	A	114	GLY	0	0.030	0.035	7.373	1.330	1.330	0.000	0.000	0.000	0.000
37	A	115	PHE	0	-0.023	-0.034	8.360	0.850	0.850	0.000	0.000	0.000	0.000
38	A	116	SER	0	0.041	0.025	11.458	0.306	0.306	0.000	0.000	0.000	0.000
39	A	117	THR	0	0.024	-0.015	14.066	0.673	0.673	0.000	0.000	0.000	0.000
40	A	118	THR	0	0.041	0.021	17.796	0.039	0.039	0.000	0.000	0.000	0.000
41	A	119	VAL	0	-0.038	-0.003	20.754	0.848	0.848	0.000	0.000	0.000	0.000
42	A	120	LYS	1	0.978	0.970	22.962	11.127	11.127	0.000	0.000	0.000	0.000
43	A	121	ASP	-1	-0.796	-0.879	25.135	-11.770	-11.770	0.000	0.000	0.000	0.000
44	A	122	GLY	0	0.041	0.033	22.475	-0.161	-0.161	0.000	0.000	0.000	0.000
45	A	123	ILE	0	-0.043	-0.013	21.347	-0.373	-0.373	0.000	0.000	0.000	0.000
46	A	124	LEU	0	-0.030	-0.009	14.838	-0.265	-0.265	0.000	0.000	0.000	0.000
47	A	125	VAL	0	0.003	-0.018	14.992	-0.738	-0.738	0.000	0.000	0.000	0.000
48	A	126	ARG	1	0.757	0.855	18.308	12.475	12.475	0.000	0.000	0.000	0.000
49	A	127	ILE	0	-0.017	0.013	18.555	-0.152	-0.152	0.000	0.000	0.000	0.000
50	A	128	ASP	-1	-0.781	-0.869	22.342	-11.545	-11.545	0.000	0.000	0.000	0.000
51	A	129	SER	0	0.041	0.002	25.915	-0.454	-0.454	0.000	0.000	0.000	0.000
52	A	130	ALA	0	-0.033	-0.015	28.304	0.089	0.089	0.000	0.000	0.000	0.000
53	A	131	PRO	0	0.001	-0.015	30.902	0.159	0.159	0.000	0.000	0.000	0.000
54	A	132	GLY	0	0.015	0.016	33.739	0.179	0.179	0.000	0.000	0.000	0.000
55	A	133	LEU	0	-0.061	-0.018	31.568	0.174	0.174	0.000	0.000	0.000	0.000
56	A	134	GLY	0	0.013	0.004	33.036	-0.084	-0.084	0.000	0.000	0.000	0.000
57	A	135	ASP	-1	-0.858	-0.926	28.914	-10.538	-10.538	0.000	0.000	0.000	0.000
58	A	136	PHE	0	-0.056	-0.040	25.801	-0.258	-0.258	0.000	0.000	0.000	0.000
59	A	137	LEU	0	-0.013	0.002	20.059	-0.003	-0.003	0.000	0.000	0.000	0.000
60	A	138	GLN	0	0.022	0.017	22.002	-0.301	-0.301	0.000	0.000	0.000	0.000
61	A	139	LEU	0	-0.006	0.009	15.231	0.176	0.176	0.000	0.000	0.000	0.000
62	A	140	HIS	0	0.016	-0.001	19.731	-0.119	-0.119	0.000	0.000	0.000	0.000
63	A	141	ILE	0	0.001	0.006	18.267	-0.166	-0.166	0.000	0.000	0.000	0.000
64	A	142	GLU	-1	-0.824	-0.914	22.300	-11.149	-11.149	0.000	0.000	0.000	0.000
65	A	143	GLN	0	-0.010	-0.013	26.015	0.174	0.174	0.000	0.000	0.000	0.000
66	A	144	GLY	0	0.007	0.001	23.545	0.063	0.063	0.000	0.000	0.000	0.000
67	A	145	LYS	1	0.874	0.937	22.303	10.830	10.830	0.000	0.000	0.000	0.000
68	A	146	ILE	0	0.002	0.000	16.487	0.238	0.238	0.000	0.000	0.000	0.000
69	A	147	GLY	0	0.041	0.012	20.798	0.351	0.351	0.000	0.000	0.000	0.000
70	A	148	VAL	0	-0.069	-0.022	19.246	-0.608	-0.608	0.000	0.000	0.000	0.000
71	A	149	VAL	0	-0.001	0.009	22.127	0.469	0.469	0.000	0.000	0.000	0.000
72	A	150	PHE	0	0.008	-0.014	24.508	-0.490	-0.490	0.000	0.000	0.000	0.000
73	A	151	ASN	0	0.003	0.003	26.509	0.444	0.444	0.000	0.000	0.000	0.000
74	A	152	ILE	0	-0.013	-0.008	27.805	-0.349	-0.349	0.000	0.000	0.000	0.000
75	A	153	GLY	0	0.064	0.039	30.648	0.202	0.202	0.000	0.000	0.000	0.000
76	A	154	THR	0	-0.077	-0.039	33.913	0.223	0.223	0.000	0.000	0.000	0.000
77	A	155	VAL	0	-0.001	-0.006	34.143	0.259	0.259	0.000	0.000	0.000	0.000
78	A	156	ASP	-1	-0.848	-0.923	30.717	-10.449	-10.449	0.000	0.000	0.000	0.000
79	A	157	ILE	0	-0.034	-0.001	28.112	0.200	0.200	0.000	0.000	0.000	0.000
80	A	158	SER	0	-0.013	-0.017	26.765	-0.610	-0.610	0.000	0.000	0.000	0.000
81	A	159	ILE	0	-0.002	0.005	22.594	0.225	0.225	0.000	0.000	0.000	0.000
82	A	160	LYS	1	0.857	0.918	23.320	11.810	11.810	0.000	0.000	0.000	0.000
83	A	161	GLU	-1	-0.819	-0.894	20.421	-13.702	-13.702	0.000	0.000	0.000	0.000
84	A	162	GLU	-1	-0.881	-0.957	22.913	-10.877	-10.877	0.000	0.000	0.000	0.000
85	A	163	ARG	1	0.901	0.970	25.231	12.001	12.001	0.000	0.000	0.000	0.000
86	A	164	THR	0	-0.013	-0.010	21.785	0.525	0.525	0.000	0.000	0.000	0.000
87	A	165	PRO	0	-0.034	-0.022	22.148	-0.473	-0.473	0.000	0.000	0.000	0.000
88	A	166	VAL	0	0.020	0.005	17.277	-0.407	-0.407	0.000	0.000	0.000	0.000
89	A	167	ASN	0	-0.088	-0.023	18.080	-0.777	-0.777	0.000	0.000	0.000	0.000
90	A	168	ASP	-1	-0.801	-0.901	18.219	-16.460	-16.460	0.000	0.000	0.000	0.000
91	A	169	GLY	0	-0.009	-0.009	18.436	0.184	0.184	0.000	0.000	0.000	0.000
92	A	170	LYS	1	0.905	0.966	15.404	15.304	15.304	0.000	0.000	0.000	0.000
93	A	171	TYR	0	-0.028	-0.016	6.075	-1.604	-1.604	0.000	0.000	0.000	0.000
94	A	172	HIS	1	0.812	0.881	11.646	20.768	20.768	0.000	0.000	0.000	0.000
95	A	173	VAL	0	-0.047	-0.024	7.755	-2.913	-2.913	0.000	0.000	0.000	0.000
96	A	174	VAL	0	-0.005	0.019	10.488	2.147	2.147	0.000	0.000	0.000	0.000
97	A	175	ARG	1	0.920	0.948	8.217	27.410	27.410	0.000	0.000	0.000	0.000
98	A	176	PHE	0	0.063	0.030	14.108	1.127	1.127	0.000	0.000	0.000	0.000
99	A	177	THR	0	-0.070	-0.046	16.716	-0.766	-0.766	0.000	0.000	0.000	0.000
100	A	178	ARG	1	0.799	0.882	19.292	13.193	13.193	0.000	0.000	0.000	0.000
101	A	179	ASN	0	-0.017	-0.030	22.058	-0.194	-0.194	0.000	0.000	0.000	0.000
102	A	180	GLY	0	0.009	0.010	25.277	0.459	0.459	0.000	0.000	0.000	0.000
103	A	181	ALA	0	0.061	0.031	27.663	-0.299	-0.299	0.000	0.000	0.000	0.000
104	A	182	ASN	0	0.000	0.005	27.058	0.181	0.181	0.000	0.000	0.000	0.000
105	A	183	ALA	0	-0.016	-0.012	23.445	-0.410	-0.410	0.000	0.000	0.000	0.000
106	A	184	THR	0	0.010	0.014	20.260	0.141	0.141	0.000	0.000	0.000	0.000
107	A	185	LEU	0	-0.006	-0.002	18.012	-0.693	-0.693	0.000	0.000	0.000	0.000
108	A	186	GLN	0	-0.023	-0.016	15.627	-0.265	-0.265	0.000	0.000	0.000	0.000
109	A	187	VAL	0	0.027	0.009	14.930	-1.044	-1.044	0.000	0.000	0.000	0.000
110	A	188	ASP	-1	-0.799	-0.889	12.583	-22.250	-22.250	0.000	0.000	0.000	0.000
111	A	189	ASN	0	-0.039	-0.025	13.672	-0.577	-0.577	0.000	0.000	0.000	0.000
112	A	190	TRP	0	0.004	0.009	16.020	1.114	1.114	0.000	0.000	0.000	0.000
113	A	191	PRO	0	0.010	-0.008	19.183	-0.356	-0.356	0.000	0.000	0.000	0.000
114	A	192	VAL	0	-0.025	-0.001	19.060	-0.204	-0.204	0.000	0.000	0.000	0.000
115	A	193	ASN	0	-0.025	-0.006	21.453	1.230	1.230	0.000	0.000	0.000	0.000
116	A	194	GLU	-1	-0.872	-0.941	22.869	-12.351	-12.351	0.000	0.000	0.000	0.000
117	A	195	HIS	0	0.002	-0.002	25.444	0.398	0.398	0.000	0.000	0.000	0.000
118	A	196	TYR	0	-0.019	-0.028	26.820	-0.287	-0.287	0.000	0.000	0.000	0.000
119	A	197	PRO	0	-0.033	-0.002	29.933	0.392	0.392	0.000	0.000	0.000	0.000
120	A	198	THR	0	0.039	0.024	33.161	0.045	0.045	0.000	0.000	0.000	0.000
121	A	199	GLY	0	0.018	0.014	36.621	0.043	0.043	0.000	0.000	0.000	0.000
122	A	200	ARG	1	0.922	0.953	37.693	7.413	7.413	0.000	0.000	0.000	0.000
123	A	201	GLN	0	0.027	0.010	33.563	-0.162	-0.162	0.000	0.000	0.000	0.000
124	A	202	LEU	0	0.004	0.019	33.772	0.102	0.102	0.000	0.000	0.000	0.000
125	A	203	THR	0	-0.013	-0.028	30.253	-0.289	-0.289	0.000	0.000	0.000	0.000
126	A	204	ILE	0	-0.027	-0.020	28.727	-0.453	-0.453	0.000	0.000	0.000	0.000
127	A	205	PHE	0	0.021	0.035	22.825	0.236	0.236	0.000	0.000	0.000	0.000
128	A	206	ASN	0	0.035	0.009	27.256	-0.429	-0.429	0.000	0.000	0.000	0.000
129	A	207	THR	0	-0.006	-0.007	28.462	-0.018	-0.018	0.000	0.000	0.000	0.000
130	A	208	GLN	0	0.026	0.027	22.446	-0.523	-0.523	0.000	0.000	0.000	0.000
131	A	209	ALA	0	-0.012	-0.017	25.568	-0.036	-0.036	0.000	0.000	0.000	0.000
132	A	210	GLN	0	-0.015	-0.010	23.133	0.031	0.031	0.000	0.000	0.000	0.000
133	A	211	ILE	0	0.001	-0.003	16.945	-0.174	-0.174	0.000	0.000	0.000	0.000
134	A	212	ALA	0	0.028	0.031	19.816	-0.307	-0.307	0.000	0.000	0.000	0.000
135	A	213	ILE	0	-0.013	-0.016	14.556	-0.597	-0.597	0.000	0.000	0.000	0.000
136	A	214	GLY	0	0.055	0.014	18.305	0.249	0.249	0.000	0.000	0.000	0.000
137	A	215	GLY	0	0.054	0.027	19.496	0.537	0.537	0.000	0.000	0.000	0.000
138	A	216	LYS	1	0.845	0.913	22.787	12.474	12.474	0.000	0.000	0.000	0.000
139	A	217	ASP	-1	-0.894	-0.955	24.733	-12.374	-12.374	0.000	0.000	0.000	0.000
140	A	218	LYS	1	0.915	0.961	26.270	11.733	11.733	0.000	0.000	0.000	0.000
141	A	219	GLY	0	-0.003	0.007	28.035	0.233	0.233	0.000	0.000	0.000	0.000
142	A	220	ARG	1	0.792	0.871	25.623	12.156	12.156	0.000	0.000	0.000	0.000
143	A	221	LEU	0	-0.019	-0.007	23.644	-0.584	-0.584	0.000	0.000	0.000	0.000
144	A	222	PHE	0	0.008	0.007	15.380	0.119	0.119	0.000	0.000	0.000	0.000
145	A	223	GLN	0	-0.002	-0.015	19.988	0.366	0.366	0.000	0.000	0.000	0.000
146	A	224	GLY	0	-0.012	0.017	17.011	0.109	0.109	0.000	0.000	0.000	0.000
147	A	225	GLN	0	-0.009	-0.004	9.079	1.906	1.906	0.000	0.000	0.000	0.000
148	A	226	LEU	0	0.003	0.000	11.125	0.034	0.034	0.000	0.000	0.000	0.000
149	A	227	SER	0	-0.015	-0.028	5.746	-3.578	-3.578	0.000	0.000	0.000	0.000
150	A	228	GLY	0	-0.003	-0.004	5.299	-0.766	-0.766	0.000	0.000	0.000	0.000
151	A	229	LEU	0	-0.033	-0.005	6.129	0.409	0.409	0.000	0.000	0.000	0.000
152	A	230	TYR	0	-0.059	-0.020	9.104	-0.149	-0.149	0.000	0.000	0.000	0.000
153	A	231	TYR	0	0.038	-0.023	10.745	0.756	0.756	0.000	0.000	0.000	0.000
154	A	232	ASP	0	-0.030	-0.049	14.555	0.022	0.022	0.000	0.000	0.000	0.000
155	A	233	GLY	0	0.009	0.012	13.402	0.849	0.849	0.000	0.000	0.000	0.000
156	A	234	LEU	0	0.004	0.010	12.927	-1.341	-1.341	0.000	0.000	0.000	0.000
157	A	235	LYS	1	0.965	0.977	7.063	36.583	36.583	0.000	0.000	0.000	0.000
158	A	236	VAL	0	0.066	0.025	10.397	-0.484	-0.484	0.000	0.000	0.000	0.000
159	A	237	LEU	0	0.007	0.012	9.297	0.991	0.991	0.000	0.000	0.000	0.000
160	A	238	ASN	0	-0.006	-0.016	6.058	-2.327	-2.327	0.000	0.000	0.000	0.000
161	A	239	MET	0	0.040	0.026	9.816	1.317	1.317	0.000	0.000	0.000	0.000
162	A	240	ALA	0	-0.011	-0.001	13.262	1.505	1.505	0.000	0.000	0.000	0.000
163	A	241	ALA	0	-0.021	-0.006	11.188	0.996	0.996	0.000	0.000	0.000	0.000
164	A	242	GLU	-1	-0.965	-0.980	11.345	-24.898	-24.898	0.000	0.000	0.000	0.000
165	A	243	ASN	0	-0.059	-0.019	14.722	1.500	1.500	0.000	0.000	0.000	0.000
166	A	244	ASN	0	0.052	0.027	16.841	1.702	1.702	0.000	0.000	0.000	0.000
167	A	245	PRO	0	0.041	0.012	18.606	0.089	0.089	0.000	0.000	0.000	0.000
168	A	246	ASN	0	-0.051	-0.024	21.141	1.146	1.146	0.000	0.000	0.000	0.000
169	A	247	ILE	0	-0.043	-0.017	16.490	-0.129	-0.129	0.000	0.000	0.000	0.000
170	A	248	LYS	1	0.941	0.976	20.070	12.472	12.472	0.000	0.000	0.000	0.000
171	A	249	ILE	0	0.039	0.014	17.286	-0.552	-0.552	0.000	0.000	0.000	0.000
172	A	250	ASN	0	-0.028	-0.009	21.260	0.418	0.418	0.000	0.000	0.000	0.000
173	A	251	GLY	0	0.053	0.029	23.068	-0.331	-0.331	0.000	0.000	0.000	0.000
174	A	252	SER	0	-0.062	-0.037	23.237	-0.325	-0.325	0.000	0.000	0.000	0.000
175	A	253	VAL	0	-0.001	-0.005	17.190	-0.377	-0.377	0.000	0.000	0.000	0.000
176	A	254	ARG	1	0.925	0.972	17.471	17.062	17.062	0.000	0.000	0.000	0.000
177	A	255	LEU	0	0.018	0.017	11.372	-0.772	-0.772	0.000	0.000	0.000	0.000
178	A	256	VAL	-1	-0.921	-0.968	10.719	-27.561	-27.561	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:79:GLY)