FMO DATABASE

FMODB ID: Z73JN

Calculation Name: 2DLI-A-Xray547

Preferred Name: Killer cell immunoglobulin-like receptor 2DL2

Target Type: SINGLE PROTEIN

Ligand Name:

Ligand 3-letter code:

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 2DLI

Chain ID: A

ChEMBL ID: CHEMBL3833441

UniProt ID: P43627

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	194
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230922

Total energy (hartree)

FMO2-HF: Electronic energy	-1980335.188056
FMO2-HF: Nuclear repulsion	1903850.658947
FMO2-HF: Total energy	-76484.529109
FMO2-MP2: Total energy	-76705.53053

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:5:HIS)

Summations of interaction energy for fragment #1(A:5:HIS)

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.
-85.064	-78.432	2.904	-3.566	-5.971	-0.021

Interaction energy analysis for fragmet #1(A:5:HIS)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 1 / q_Mulliken : 0.851 / q_NPA : 0.919

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	7	LYS	1	0.885	0.943	3.858	22.174	23.330	0.000	-0.558	-0.599	-0.001
28	A	32	VAL	0	-0.050	-0.015	2.943	-0.479	-0.009	0.024	-0.174	-0.321	-0.001
30	A	34	PHE	0	-0.026	-0.013	3.016	-2.792	-2.252	0.019	-0.164	-0.395	-0.001
84	A	89	GLN	0	-0.009	0.004	2.834	0.362	0.791	0.083	-0.109	-0.403	-0.001
85	A	90	LEU	0	0.017	0.012	4.062	2.564	2.771	-0.001	-0.031	-0.175	0.000
86	A	91	SER	0	-0.071	-0.049	2.198	-17.687	-15.227	2.535	-2.300	-2.696	-0.014
87	A	92	ALA	0	-0.024	-0.003	2.871	3.732	5.016	0.242	-0.196	-1.329	-0.003
88	A	93	PRO	0	0.041	0.022	4.147	-0.024	0.062	0.002	-0.034	-0.053	0.000
4	A	8	PRO	0	-0.005	0.009	5.914	1.675	1.675	0.000	0.000	0.000	0.000
5	A	9	SER	0	0.008	0.008	8.396	1.133	1.133	0.000	0.000	0.000	0.000
6	A	10	LEU	0	-0.017	-0.011	12.168	-0.173	-0.173	0.000	0.000	0.000	0.000
7	A	11	LEU	0	-0.021	-0.014	14.473	0.658	0.658	0.000	0.000	0.000	0.000
8	A	12	ALA	0	0.045	0.013	18.234	-0.209	-0.209	0.000	0.000	0.000	0.000
9	A	13	HIS	0	-0.040	-0.015	20.122	0.323	0.323	0.000	0.000	0.000	0.000
10	A	14	PRO	0	-0.007	0.004	23.769	0.271	0.271	0.000	0.000	0.000	0.000
11	A	15	GLY	0	0.072	0.039	25.328	0.319	0.319	0.000	0.000	0.000	0.000
12	A	16	ARG	1	0.858	0.920	22.661	12.207	12.207	0.000	0.000	0.000	0.000
13	A	17	LEU	0	-0.051	-0.015	25.097	-0.009	-0.009	0.000	0.000	0.000	0.000
14	A	18	VAL	0	0.041	0.028	26.958	0.060	0.060	0.000	0.000	0.000	0.000
15	A	19	LYS	1	0.838	0.930	30.004	9.218	9.218	0.000	0.000	0.000	0.000
16	A	20	SER	0	0.045	0.012	32.792	-0.259	-0.259	0.000	0.000	0.000	0.000
17	A	21	GLU	-1	-0.987	-0.993	33.579	-8.279	-8.279	0.000	0.000	0.000	0.000
18	A	22	GLU	-1	-0.855	-0.905	31.897	-9.377	-9.377	0.000	0.000	0.000	0.000
19	A	23	THR	0	-0.026	-0.019	28.087	-0.235	-0.235	0.000	0.000	0.000	0.000
20	A	24	VAL	0	0.010	0.002	23.932	0.076	0.076	0.000	0.000	0.000	0.000
21	A	25	ILE	0	-0.024	0.000	20.993	-0.302	-0.302	0.000	0.000	0.000	0.000
22	A	26	LEU	0	-0.002	-0.005	18.010	-0.031	-0.031	0.000	0.000	0.000	0.000
23	A	27	GLN	0	-0.013	-0.022	16.544	-0.771	-0.771	0.000	0.000	0.000	0.000
24	A	28	CYS	0	-0.043	0.003	11.260	-0.054	-0.054	0.000	0.000	0.000	0.000
25	A	29	TRP	0	0.020	0.006	12.128	-0.097	-0.097	0.000	0.000	0.000	0.000
26	A	30	SER	0	0.010	-0.007	6.255	-0.745	-0.745	0.000	0.000	0.000	0.000
27	A	31	ASP	-1	-0.791	-0.854	8.680	-31.791	-31.791	0.000	0.000	0.000	0.000
29	A	33	ARG	1	0.923	0.961	6.415	22.651	22.651	0.000	0.000	0.000	0.000
31	A	35	GLU	-1	-0.797	-0.884	7.812	-22.326	-22.326	0.000	0.000	0.000	0.000
32	A	36	HIS	0	-0.017	0.004	9.860	3.490	3.490	0.000	0.000	0.000	0.000
33	A	37	PHE	0	0.017	-0.014	9.535	-4.039	-4.039	0.000	0.000	0.000	0.000
34	A	38	LEU	0	-0.034	-0.006	10.663	1.966	1.966	0.000	0.000	0.000	0.000
35	A	39	LEU	0	0.009	-0.006	11.735	-1.543	-1.543	0.000	0.000	0.000	0.000
36	A	40	HIS	0	-0.054	-0.027	14.103	1.006	1.006	0.000	0.000	0.000	0.000
37	A	41	ARG	1	0.863	0.944	15.985	13.547	13.547	0.000	0.000	0.000	0.000
38	A	42	GLU	-1	-0.806	-0.900	16.994	-17.120	-17.120	0.000	0.000	0.000	0.000
39	A	43	GLY	0	0.031	0.018	20.665	0.440	0.440	0.000	0.000	0.000	0.000
40	A	44	LYS	1	0.865	0.921	24.500	10.171	10.171	0.000	0.000	0.000	0.000
41	A	45	PHE	0	0.034	0.013	24.139	-0.171	-0.171	0.000	0.000	0.000	0.000
42	A	46	LYS	1	0.884	0.948	19.824	12.421	12.421	0.000	0.000	0.000	0.000
43	A	47	ASP	-1	-0.850	-0.921	19.816	-13.977	-13.977	0.000	0.000	0.000	0.000
44	A	48	THR	0	-0.053	-0.036	14.376	-0.863	-0.863	0.000	0.000	0.000	0.000
45	A	49	LEU	0	0.029	0.039	17.240	0.568	0.568	0.000	0.000	0.000	0.000
46	A	50	HIS	0	0.021	-0.012	15.084	-1.255	-1.255	0.000	0.000	0.000	0.000
47	A	51	LEU	0	-0.012	0.002	15.234	1.161	1.161	0.000	0.000	0.000	0.000
48	A	52	ILE	0	0.012	0.007	14.446	-1.591	-1.591	0.000	0.000	0.000	0.000
49	A	53	GLY	0	-0.030	-0.020	12.368	0.461	0.461	0.000	0.000	0.000	0.000
50	A	54	GLU	-1	-0.862	-0.910	13.453	-15.929	-15.929	0.000	0.000	0.000	0.000
51	A	55	HIS	0	-0.032	-0.041	12.216	-0.275	-0.275	0.000	0.000	0.000	0.000
52	A	56	HIS	0	-0.101	-0.055	15.589	1.128	1.128	0.000	0.000	0.000	0.000
53	A	57	ASP	-1	-0.856	-0.933	18.418	-14.939	-14.939	0.000	0.000	0.000	0.000
54	A	58	GLY	0	-0.012	0.008	15.810	-0.670	-0.670	0.000	0.000	0.000	0.000
55	A	59	VAL	0	-0.056	-0.035	12.230	-1.590	-1.590	0.000	0.000	0.000	0.000
56	A	60	SER	0	-0.036	-0.005	9.765	0.590	0.590	0.000	0.000	0.000	0.000
57	A	61	LYS	1	0.911	0.938	11.670	16.170	16.170	0.000	0.000	0.000	0.000
58	A	62	ALA	0	0.031	0.031	13.482	0.526	0.526	0.000	0.000	0.000	0.000
59	A	63	ASN	0	0.012	0.000	15.136	-0.349	-0.349	0.000	0.000	0.000	0.000
60	A	64	PHE	0	0.065	0.028	14.200	0.750	0.750	0.000	0.000	0.000	0.000
61	A	65	SER	0	-0.013	-0.006	19.596	0.269	0.269	0.000	0.000	0.000	0.000
62	A	66	ILE	0	-0.018	0.003	20.739	0.014	0.014	0.000	0.000	0.000	0.000
63	A	67	GLY	0	0.052	0.008	24.487	0.355	0.355	0.000	0.000	0.000	0.000
64	A	68	PRO	0	0.009	-0.002	28.040	-0.071	-0.071	0.000	0.000	0.000	0.000
65	A	69	MET	0	-0.033	0.014	26.141	-0.135	-0.135	0.000	0.000	0.000	0.000
66	A	70	MET	0	0.056	0.013	29.687	0.409	0.409	0.000	0.000	0.000	0.000
67	A	71	GLN	0	-0.048	-0.054	29.539	-0.262	-0.262	0.000	0.000	0.000	0.000
68	A	72	ASP	-1	-0.931	-0.963	27.920	-10.808	-10.808	0.000	0.000	0.000	0.000
69	A	73	LEU	0	-0.020	-0.001	25.429	-0.560	-0.560	0.000	0.000	0.000	0.000
70	A	74	ALA	0	-0.001	0.016	24.575	-0.588	-0.588	0.000	0.000	0.000	0.000
71	A	75	GLY	0	0.002	-0.013	23.653	0.087	0.087	0.000	0.000	0.000	0.000
72	A	76	THR	0	-0.064	-0.047	17.902	-0.053	-0.053	0.000	0.000	0.000	0.000
73	A	77	TYR	0	0.000	-0.014	17.169	-0.393	-0.393	0.000	0.000	0.000	0.000
74	A	78	ARG	1	0.838	0.895	12.439	18.424	18.424	0.000	0.000	0.000	0.000
75	A	80	TYR	0	0.001	-0.007	7.304	-2.465	-2.465	0.000	0.000	0.000	0.000
76	A	81	GLY	0	0.059	0.027	6.150	3.456	3.456	0.000	0.000	0.000	0.000
77	A	82	SER	0	-0.042	-0.030	5.347	-7.571	-7.571	0.000	0.000	0.000	0.000
78	A	83	VAL	0	0.051	0.019	6.273	2.371	2.371	0.000	0.000	0.000	0.000
79	A	84	THR	0	-0.013	-0.031	8.318	-0.129	-0.129	0.000	0.000	0.000	0.000
80	A	85	HIS	0	-0.047	-0.015	7.302	2.234	2.234	0.000	0.000	0.000	0.000
81	A	86	SER	0	-0.030	-0.016	6.702	0.252	0.252	0.000	0.000	0.000	0.000
82	A	87	PRO	0	0.023	0.011	7.713	-2.850	-2.850	0.000	0.000	0.000	0.000
83	A	88	TYR	0	-0.001	-0.004	8.346	-0.133	-0.133	0.000	0.000	0.000	0.000
89	A	94	SER	0	-0.004	-0.006	7.970	0.068	0.068	0.000	0.000	0.000	0.000
90	A	95	ASP	-1	-0.870	-0.910	9.998	-20.609	-20.609	0.000	0.000	0.000	0.000
91	A	96	PRO	0	-0.042	-0.014	13.459	-0.260	-0.260	0.000	0.000	0.000	0.000
92	A	97	LEU	0	0.009	0.011	16.234	0.644	0.644	0.000	0.000	0.000	0.000
93	A	98	ASP	-1	-0.834	-0.897	18.868	-13.977	-13.977	0.000	0.000	0.000	0.000
94	A	99	ILE	0	-0.004	0.007	21.130	0.430	0.430	0.000	0.000	0.000	0.000
95	A	100	VAL	0	-0.017	-0.015	24.118	0.151	0.151	0.000	0.000	0.000	0.000
96	A	101	ILE	0	0.032	0.038	27.878	0.045	0.045	0.000	0.000	0.000	0.000
97	A	102	THR	0	-0.054	-0.051	30.948	0.299	0.299	0.000	0.000	0.000	0.000
98	A	103	GLY	0	-0.006	-0.024	33.812	0.017	0.017	0.000	0.000	0.000	0.000
99	A	104	LEU	0	0.029	0.013	34.375	-0.020	-0.020	0.000	0.000	0.000	0.000
100	A	105	TYR	0	-0.017	-0.004	36.990	0.111	0.111	0.000	0.000	0.000	0.000
101	A	106	GLU	-1	-0.878	-0.940	41.143	-6.836	-6.836	0.000	0.000	0.000	0.000
102	A	107	LYS	1	0.878	0.940	42.183	6.852	6.852	0.000	0.000	0.000	0.000
103	A	108	PRO	0	-0.031	-0.010	40.193	0.162	0.162	0.000	0.000	0.000	0.000
104	A	109	SER	0	-0.036	-0.019	43.489	0.078	0.078	0.000	0.000	0.000	0.000
105	A	110	LEU	0	-0.029	-0.005	40.816	-0.002	-0.002	0.000	0.000	0.000	0.000
106	A	111	SER	0	-0.031	-0.007	44.487	0.173	0.173	0.000	0.000	0.000	0.000
107	A	112	ALA	0	0.066	0.016	45.617	-0.163	-0.163	0.000	0.000	0.000	0.000
108	A	113	GLN	0	-0.002	0.008	47.232	0.184	0.184	0.000	0.000	0.000	0.000
109	A	114	PRO	0	-0.032	-0.008	48.224	0.118	0.118	0.000	0.000	0.000	0.000
110	A	115	GLY	0	0.054	0.037	50.634	0.106	0.106	0.000	0.000	0.000	0.000
111	A	116	PRO	0	-0.029	-0.026	47.594	-0.116	-0.116	0.000	0.000	0.000	0.000
112	A	117	THR	0	-0.060	-0.041	47.812	-0.092	-0.092	0.000	0.000	0.000	0.000
113	A	118	VAL	0	0.001	0.023	47.375	0.108	0.108	0.000	0.000	0.000	0.000
114	A	119	LEU	0	0.034	0.008	49.568	-0.057	-0.057	0.000	0.000	0.000	0.000
115	A	120	ALA	0	0.048	0.009	47.352	-0.131	-0.131	0.000	0.000	0.000	0.000
116	A	121	GLY	0	-0.080	-0.040	46.568	0.117	0.117	0.000	0.000	0.000	0.000
117	A	122	GLU	-1	-0.888	-0.934	47.541	-6.135	-6.135	0.000	0.000	0.000	0.000
118	A	123	SER	0	-0.079	-0.039	45.773	-0.128	-0.128	0.000	0.000	0.000	0.000
119	A	124	VAL	0	0.046	0.025	43.268	0.118	0.118	0.000	0.000	0.000	0.000
120	A	125	THR	0	-0.016	-0.016	43.351	-0.248	-0.248	0.000	0.000	0.000	0.000
121	A	126	LEU	0	0.026	0.008	40.302	0.168	0.168	0.000	0.000	0.000	0.000
122	A	127	SER	0	-0.033	-0.024	42.700	-0.145	-0.145	0.000	0.000	0.000	0.000
123	A	128	CYS	0	-0.078	-0.022	37.274	-0.193	-0.193	0.000	0.000	0.000	0.000
124	A	129	SER	0	0.053	0.024	43.622	-0.057	-0.057	0.000	0.000	0.000	0.000
125	A	130	SER	0	0.064	0.024	44.520	-0.016	-0.016	0.000	0.000	0.000	0.000
126	A	131	ARG	1	0.924	0.963	46.587	6.146	6.146	0.000	0.000	0.000	0.000
127	A	132	SER	0	0.013	0.023	43.616	0.094	0.094	0.000	0.000	0.000	0.000
128	A	133	SER	0	-0.006	-0.006	42.994	0.004	0.004	0.000	0.000	0.000	0.000
129	A	134	TYR	0	-0.044	-0.036	39.719	-0.171	-0.171	0.000	0.000	0.000	0.000
130	A	135	ASP	-1	-0.835	-0.909	37.121	-8.059	-8.059	0.000	0.000	0.000	0.000
131	A	136	MET	0	-0.106	-0.048	32.386	-0.038	-0.038	0.000	0.000	0.000	0.000
132	A	137	TYR	0	0.015	0.002	37.192	0.018	0.018	0.000	0.000	0.000	0.000
133	A	138	HIS	1	0.805	0.887	31.381	9.438	9.438	0.000	0.000	0.000	0.000
134	A	139	LEU	0	0.014	0.011	34.375	0.207	0.207	0.000	0.000	0.000	0.000
135	A	140	SER	0	-0.027	-0.007	33.031	-0.371	-0.371	0.000	0.000	0.000	0.000
136	A	141	ARG	1	0.891	0.934	33.083	9.194	9.194	0.000	0.000	0.000	0.000
137	A	142	GLU	-1	-0.881	-0.928	32.596	-8.482	-8.482	0.000	0.000	0.000	0.000
138	A	143	GLY	0	0.042	0.020	29.599	0.131	0.131	0.000	0.000	0.000	0.000
139	A	144	GLU	-1	-0.935	-0.956	28.037	-10.305	-10.305	0.000	0.000	0.000	0.000
140	A	145	ALA	0	-0.017	-0.011	22.809	-0.097	-0.097	0.000	0.000	0.000	0.000
141	A	146	HIS	0	-0.052	-0.041	20.738	0.132	0.132	0.000	0.000	0.000	0.000
142	A	147	GLU	-1	-0.793	-0.886	26.035	-9.979	-9.979	0.000	0.000	0.000	0.000
143	A	148	CYS	0	0.018	0.016	29.352	-0.121	-0.121	0.000	0.000	0.000	0.000
144	A	149	ARG	1	0.908	0.945	31.149	9.710	9.710	0.000	0.000	0.000	0.000
145	A	150	PHE	0	0.002	0.015	33.245	-0.150	-0.150	0.000	0.000	0.000	0.000
146	A	151	SER	0	0.001	-0.019	35.779	-0.072	-0.072	0.000	0.000	0.000	0.000
147	A	152	ALA	0	-0.034	-0.009	37.582	0.095	0.095	0.000	0.000	0.000	0.000
148	A	153	GLY	0	0.004	0.008	41.248	0.005	0.005	0.000	0.000	0.000	0.000
149	A	154	PRO	0	-0.030	-0.041	44.468	0.025	0.025	0.000	0.000	0.000	0.000
150	A	155	LYS	1	0.902	0.963	46.574	6.266	6.266	0.000	0.000	0.000	0.000
151	A	156	VAL	0	0.053	0.035	49.512	0.107	0.107	0.000	0.000	0.000	0.000
152	A	157	ASN	0	0.022	0.001	51.991	0.035	0.035	0.000	0.000	0.000	0.000
153	A	158	GLY	0	-0.046	-0.028	53.187	0.062	0.062	0.000	0.000	0.000	0.000
154	A	159	THR	0	0.005	0.003	48.545	-0.081	-0.081	0.000	0.000	0.000	0.000
155	A	160	PHE	0	0.045	0.025	44.505	0.085	0.085	0.000	0.000	0.000	0.000
156	A	161	GLN	0	-0.024	-0.026	44.232	0.072	0.072	0.000	0.000	0.000	0.000
157	A	162	ALA	0	0.003	0.013	40.012	-0.025	-0.025	0.000	0.000	0.000	0.000
158	A	163	ASP	-1	-0.806	-0.881	42.032	-6.975	-6.975	0.000	0.000	0.000	0.000
159	A	164	PHE	0	-0.033	-0.028	35.901	-0.230	-0.230	0.000	0.000	0.000	0.000
160	A	165	PRO	0	0.014	-0.001	39.942	0.088	0.088	0.000	0.000	0.000	0.000
161	A	166	LEU	0	-0.016	-0.007	38.123	-0.206	-0.206	0.000	0.000	0.000	0.000
162	A	167	GLY	0	0.006	0.017	39.699	-0.118	-0.118	0.000	0.000	0.000	0.000
163	A	168	PRO	0	-0.024	-0.027	41.942	0.090	0.090	0.000	0.000	0.000	0.000
164	A	169	ALA	0	0.025	0.030	42.658	-0.198	-0.198	0.000	0.000	0.000	0.000
165	A	170	THR	0	0.004	-0.008	40.692	0.026	0.026	0.000	0.000	0.000	0.000
166	A	171	HIS	0	0.013	0.009	38.001	0.192	0.192	0.000	0.000	0.000	0.000
167	A	172	GLY	0	0.039	0.032	39.324	-0.209	-0.209	0.000	0.000	0.000	0.000
168	A	173	GLY	0	-0.010	-0.008	39.185	-0.188	-0.188	0.000	0.000	0.000	0.000
169	A	174	THR	0	-0.027	-0.011	38.944	0.279	0.279	0.000	0.000	0.000	0.000
170	A	175	TYR	0	0.039	0.020	37.281	-0.195	-0.195	0.000	0.000	0.000	0.000
171	A	176	ARG	1	0.865	0.916	36.942	8.429	8.429	0.000	0.000	0.000	0.000
172	A	178	PHE	0	0.040	0.018	34.357	0.075	0.075	0.000	0.000	0.000	0.000
173	A	179	GLY	0	0.061	0.020	37.297	-0.024	-0.024	0.000	0.000	0.000	0.000
174	A	180	SER	0	-0.019	-0.008	34.051	-0.218	-0.218	0.000	0.000	0.000	0.000
175	A	181	PHE	0	0.026	0.007	35.631	0.207	0.207	0.000	0.000	0.000	0.000
176	A	182	ARG	1	0.925	0.940	33.669	8.041	8.041	0.000	0.000	0.000	0.000
177	A	183	ASP	-1	-0.900	-0.934	32.202	-9.002	-9.002	0.000	0.000	0.000	0.000
178	A	184	SER	0	-0.017	-0.005	31.130	-0.235	-0.235	0.000	0.000	0.000	0.000
179	A	185	PRO	0	0.021	0.013	27.674	0.099	0.099	0.000	0.000	0.000	0.000
180	A	186	TYR	0	-0.032	-0.007	22.892	0.070	0.070	0.000	0.000	0.000	0.000
181	A	187	GLU	-1	-0.793	-0.887	28.971	-9.811	-9.811	0.000	0.000	0.000	0.000
182	A	188	TRP	0	-0.026	-0.033	29.312	0.215	0.215	0.000	0.000	0.000	0.000
183	A	189	SER	0	0.004	-0.004	34.617	0.044	0.044	0.000	0.000	0.000	0.000
184	A	190	ASN	0	-0.037	-0.015	36.981	-0.323	-0.323	0.000	0.000	0.000	0.000
185	A	191	SER	0	0.005	0.009	36.970	0.046	0.046	0.000	0.000	0.000	0.000
186	A	192	SER	0	-0.016	0.004	38.888	0.114	0.114	0.000	0.000	0.000	0.000
187	A	193	ASP	-1	-0.867	-0.929	41.395	-7.105	-7.105	0.000	0.000	0.000	0.000
188	A	194	PRO	0	-0.036	-0.014	41.093	-0.061	-0.061	0.000	0.000	0.000	0.000
189	A	195	LEU	0	0.015	0.007	42.196	0.209	0.209	0.000	0.000	0.000	0.000
190	A	196	LEU	0	-0.004	0.000	42.601	-0.191	-0.191	0.000	0.000	0.000	0.000
191	A	197	VAL	0	-0.025	-0.012	42.746	0.181	0.181	0.000	0.000	0.000	0.000
192	A	198	SER	0	-0.025	-0.022	43.800	-0.157	-0.157	0.000	0.000	0.000	0.000
193	A	199	VAL	0	-0.029	-0.026	44.242	0.033	0.033	0.000	0.000	0.000	0.000
194	A	200	ILE	-1	-0.905	-0.933	47.152	-6.415	-6.415	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:5:HIS)