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HEADER SERINE HYDROLASE 04-MAR-98 1EVE
TITLE THREE DIMENSIONAL STRUCTURE OF THE ANTI-ALZHEIMER DRUG,
TITLE 2 E2020 (ARICEPT), COMPLEXED WITH ITS TARGET
TITLE 3 ACETYLCHOLINESTERASE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ACETYLCHOLINESTERASE;
COMPND 3 CHAIN: NULL;
COMPND 4 EC: 3.1.1.7;
COMPND 5 BIOLOGICAL_UNIT: HOMODIMER
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: TORPEDO CALIFORNICA;
SOURCE 3 ORGANISM_COMMON: PACIFIC ELECTRIC RAY;
SOURCE 4 VARIANT: G2 FORM;
SOURCE 5 ORGAN: ELECTRIC ORGAN;
SOURCE 6 TISSUE: ELECTROPLAQUE
KEYWDS ALZHEIMER'S DISEASE, DRUG, SERINE HYDROLASE, ALPHA/BETA
KEYWDS 2 HYDROLASE, NEUROTRANSMITTER CLEAVAGE, CATALYTIC TRIAD,
KEYWDS 3 GLYCOSYLATED PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR G.KRYGER,I.SILMAN,J.L.SUSSMAN
REVDAT 1 20-JAN-99 1EVE 0
JRNL AUTH G.KRYGER,I.SILMAN,J.L.SUSSMAN
JRNL TITL THREE DIMENSIONAL STRUCTURE OF ANTI-ALZHEIMER DRUG,
JRNL TITL 2 E2020 (ARICEPT), COMPLEXED WITH ITS TARGET,
JRNL TITL 3 ACETYLCHOLINESTERASE
JRNL REF TO BE PUBLISHED
JRNL REFN 0353
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH Y.KAWAKAMI,A.INOUE,T.KAWAI,M.WAKITA,H.SUGIMOTO,
REMARK 1 AUTH 2 A.J.HOPFINGER
REMARK 1 TITL THE RATIONALE FOR E2020 AS A POTENT
REMARK 1 TITL 2 ACETYLCHOLINESTERASE INHIBITOR
REMARK 1 REF BIOORG.MED.CHEM. V. 4 1429 1996
REMARK 1 REFN ASTM BMECEP UK ISSN 0968-0896 1200
REMARK 1 REFERENCE 2
REMARK 1 AUTH J.L.SUSSMAN,M.HAREL,F.FROLOW,C.OEFNER,A.GOLDMAN,
REMARK 1 AUTH 2 L.TOKER,I.SILMAN
REMARK 1 TITL ATOMIC STRUCTURE OF ACETYLCHOLINESTERASE FROM
REMARK 1 TITL 2 TORPEDO CALIFORNICA: A PROTOTYPIC
REMARK 1 TITL 3 ACETYLCHOLINE-BINDING PROTEIN
REMARK 1 REF SCIENCE V. 253 872 1991
REMARK 1 REFN ASTM SCIEAS US ISSN 0036-8075 0038
REMARK 2
REMARK 2 RESOLUTION. 2.5 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR 3.851
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.50
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 30.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.0
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 10000000.00
REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.001000
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 98.3
REMARK 3 NUMBER OF REFLECTIONS : 34240
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING SET) : 0.188
REMARK 3 FREE R VALUE : 0.228
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.8
REMARK 3 FREE R VALUE TEST SET COUNT : 1976
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.005
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 6
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.50
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.66
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 97.7
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 5288
REMARK 3 BIN R VALUE (WORKING SET) : 0.286
REMARK 3 BIN FREE R VALUE : 0.367
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 5.3
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 295
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.021
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 5174
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 98
REMARK 3 SOLVENT ATOMS : 396
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 39.1
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 29.3
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 1.06
REMARK 3 B22 (A**2) : 1.06
REMARK 3 B33 (A**2) : -2.13
REMARK 3 B12 (A**2) : -0.48
REMARK 3 B13 (A**2) : 0.00
REMARK 3 B23 (A**2) : 0.00
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.25
REMARK 3 ESD FROM SIGMAA (A) : 0.30
REMARK 3 LOW RESOLUTION CUTOFF (A) : 30.00
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : 0.30
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.39
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.005
REMARK 3 BOND ANGLES (DEGREES) : 1.2
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 23.1
REMARK 3 IMPROPER ANGLES (DEGREES) : 0.97
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : RESTRAINED
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : 3.10 ; 1.50
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 4.59 ; 2.00
REMARK 3 SIDE-CHAIN BOND (A**2) : 5.13 ; 2.00
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 6.88 ; 2.50
REMARK 3
REMARK 3 NCS MODEL : NONE
REMARK 3
REMARK 3 NCS RESTRAINTS. RMS SIGMA/WEIGHT
REMARK 3 GROUP 1 POSITIONAL (A) : NULL ; NULL
REMARK 3 GROUP 1 B-FACTOR (A**2) : NULL ; NULL
REMARK 3
REMARK 3 PARAMETER FILE 1 : PARHCSDX.PRO
REMARK 3 PARAMETER FILE 2 : PARAM19.SOL
REMARK 3 PARAMETER FILE 3 : CBH3.PARAM
REMARK 3 PARAMETER FILE 4 : LEARN.E2020
REMARK 3 TOPOLOGY FILE 1 : TOPHCSDX.PRO
REMARK 3 TOPOLOGY FILE 2 : TOPH11.WAT
REMARK 3 TOPOLOGY FILE 3 : E2020.TOP
REMARK 3 TOPOLOGY FILE 4 : CBH3-P.CHO
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: BULK SOLVENT MODEL USED
REMARK 4
REMARK 4 1EVE COMPLIES WITH FORMAT V. 2.2, 16-DEC-1996
REMARK 6
REMARK 6 TORPEDO CALIFORNICA ACETYLCHOLINESTERASE IS A G2 DIMER IN
REMARK 6 SOLUTION (SEE SUSSMAN 1988). THE ASYMMETRIC UNIT CONTAINS
REMARK 6 A MONOMER, WITH THE CRYSTALLOGRAPHIC TWO-FOLD AXIS RELATING
REMARK 6 THE TWO MONOMERS IN A DIMER. THIS STRUCTURE IS MORE
REMARK 6 COMPLETE THAN THE STARTING MODEL OF THE NATIVE STRUCTURE
REMARK 6 (PDB ID 2ACE). RESIDUES THAT ARE NOT SEEN IN THE CRYSTAL
REMARK 6 STRUCTURE DUE TO DISORDER INCLUDE THE N-TERMINAL RESIDUE
REMARK 6 ASP 1 AND THE C-TERMINAL RESIDUES AFTER THR 535. THR 535
REMARK 6 IS THE LAST RESIDUE OBSERVED AT THE C-TERMINUS. THE LIGAND
REMARK 6 SEEN IN THE STRUCTURE, E2020 (DONEPEZIL, ARICEPT), IS A
REMARK 6 POTENT REVERSIBLE ACHE INHIBITOR WHICH IS AN FDA APPROVED
REMARK 6 DRUG FOR THE SYMPTOMATIC TREATMENT OF ALZHEIMER'S DISEASE
REMARK 6 (SEE KAWAKAMI 1996). THE CHIRAL INHIBITOR WAS SOAKED AS A
REMARK 6 RACEMATE BUT ONLY THE R FORM SEEMS TO BIND TO THE ENZYME
REMARK 6 ACCORDING TO THE X-RAY DIFFRACTION EXPERIMENT.
REMARK 7
REMARK 7 THE ENZYME IS A GPI-ANCHORED DIMER, THE TWO MONOMERS IN THE
REMARK 7 DIMER ARE RELATED BY CRYSTALLOGRAPHIC TWO-FOLD SYMMETRY AND
REMARK 7 GENERATE A FOUR HELIX BUNDLE A365-A375 AND A518-A535.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : MAY-1997
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 5.8
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : NULL
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : RIGAKU FR300
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.54
REMARK 200 MONOCHROMATOR : NI FILTER
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : R-AXIS-II
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 34266
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.5
REMARK 200 RESOLUTION RANGE LOW (A) : 30.0
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.0
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.1
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.050
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.5
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.59
REMARK 200 COMPLETENESS FOR SHELL (%) : 95.0
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.252
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.8
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: NULL
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR
REMARK 200 REPLACEMENT
REMARK 200 SOFTWARE USED: X-PLOR 3.851
REMARK 200 STARTING MODEL: PDB ENTRY 2ACE
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 68.
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.8
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PROTEIN WAS CRYSTALLIZED FROM
REMARK 280 35% PEG 200, 100 MM MES, PH 5.8, AT 4 DEG.
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 31 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+1/3
REMARK 290 3555 Y-X,-X,Z+2/3
REMARK 290 4555 Y,X,-Z
REMARK 290 5555 X-Y,-Y,2/3-Z
REMARK 290 6555 -X,Y-X,1/3-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -0.499952 -0.866004 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866046 -0.500048 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 45.63085
REMARK 290 SMTRY1 3 -0.500048 0.866004 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.866046 -0.499952 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 91.26169
REMARK 290 SMTRY1 4 -0.499952 0.866060 0.000000 0.00000
REMARK 290 SMTRY2 4 0.866046 0.499952 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 1.000000 -0.000112 0.000000 0.00000
REMARK 290 SMTRY2 5 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 91.26169
REMARK 290 SMTRY1 6 -0.500048 -0.865949 0.000000 0.00000
REMARK 290 SMTRY2 6 -0.866046 0.500048 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 45.63085
REMARK 290
REMARK 290 REMARK: NULL
REMARK 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375 O HOH 1381
REMARK 375 O HOH 1382
REMARK 375
REMARK 375 REMARK: NULL
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 ASP 2 CG OD1 OD2
REMARK 470 HIS 3 CG ND1 CE1 NE2 CD2
REMARK 600
REMARK 600 HETEROGEN
REMARK 600 NAG: THERE ARE 5 NAG GROUPS NUMBERED 3001 - 3005 IN THIS
REMARK 600 STRUCTURE.
REMARK 650
REMARK 650 HELIX
REMARK 650 DETERMINATION METHOD: AUTHOR-DETERMINED
REMARK 700
REMARK 700 SHEET
REMARK 700 DETERMINATION METHOD: AUTHOR-DETERMINED. TAKEN FROM PDB
REMARK 700 ENTRY 2ACE.
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: CAT
REMARK 800 SITE_DESCRIPTION: CATALYTIC TRIAD.
REMARK 800
REMARK 800 SITE_IDENTIFIER: IHB
REMARK 800 SITE_DESCRIPTION: INHIBITOR BINDING SITE.
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 1EVE SWS P04058 1 - 22 NOT IN ATOMS LIST
REMARK 999 1EVE SWS P04058 557 - 586 NOT IN ATOMS LIST
DBREF 1EVE 2 535 SWS P04058 ACES_TORCA 23 556
SEQRES 1 543 ASP ASP HIS SER GLU LEU LEU VAL ASN THR LYS SER GLY
SEQRES 2 543 LYS VAL MET GLY THR ARG VAL PRO VAL LEU SER SER HIS
SEQRES 3 543 ILE SER ALA PHE LEU GLY ILE PRO PHE ALA GLU PRO PRO
SEQRES 4 543 VAL GLY ASN MET ARG PHE ARG ARG PRO GLU PRO LYS LYS
SEQRES 5 543 PRO TRP SER GLY VAL TRP ASN ALA SER THR TYR PRO ASN
SEQRES 6 543 ASN CYS GLN GLN TYR VAL ASP GLU GLN PHE PRO GLY PHE
SEQRES 7 543 SER GLY SER GLU MET TRP ASN PRO ASN ARG GLU MET SER
SEQRES 8 543 GLU ASP CYS LEU TYR LEU ASN ILE TRP VAL PRO SER PRO
SEQRES 9 543 ARG PRO LYS SER THR THR VAL MET VAL TRP ILE TYR GLY
SEQRES 10 543 GLY GLY PHE TYR SER GLY SER SER THR LEU ASP VAL TYR
SEQRES 11 543 ASN GLY LYS TYR LEU ALA TYR THR GLU GLU VAL VAL LEU
SEQRES 12 543 VAL SER LEU SER TYR ARG VAL GLY ALA PHE GLY PHE LEU
SEQRES 13 543 ALA LEU HIS GLY SER GLN GLU ALA PRO GLY ASN VAL GLY
SEQRES 14 543 LEU LEU ASP GLN ARG MET ALA LEU GLN TRP VAL HIS ASP
SEQRES 15 543 ASN ILE GLN PHE PHE GLY GLY ASP PRO LYS THR VAL THR
SEQRES 16 543 ILE PHE GLY GLU SER ALA GLY GLY ALA SER VAL GLY MET
SEQRES 17 543 HIS ILE LEU SER PRO GLY SER ARG ASP LEU PHE ARG ARG
SEQRES 18 543 ALA ILE LEU GLN SER GLY SER PRO ASN CYS PRO TRP ALA
SEQRES 19 543 SER VAL SER VAL ALA GLU GLY ARG ARG ARG ALA VAL GLU
SEQRES 20 543 LEU GLY ARG ASN LEU ASN CYS ASN LEU ASN SER ASP GLU
SEQRES 21 543 GLU LEU ILE HIS CYS LEU ARG GLU LYS LYS PRO GLN GLU
SEQRES 22 543 LEU ILE ASP VAL GLU TRP ASN VAL LEU PRO PHE ASP SER
SEQRES 23 543 ILE PHE ARG PHE SER PHE VAL PRO VAL ILE ASP GLY GLU
SEQRES 24 543 PHE PHE PRO THR SER LEU GLU SER MET LEU ASN SER GLY
SEQRES 25 543 ASN PHE LYS LYS THR GLN ILE LEU LEU GLY VAL ASN LYS
SEQRES 26 543 ASP GLU GLY SER PHE PHE LEU LEU TYR GLY ALA PRO GLY
SEQRES 27 543 PHE SER LYS ASP SER GLU SER LYS ILE SER ARG GLU ASP
SEQRES 28 543 PHE MET SER GLY VAL LYS LEU SER VAL PRO HIS ALA ASN
SEQRES 29 543 ASP LEU GLY LEU ASP ALA VAL THR LEU GLN TYR THR ASP
SEQRES 30 543 TRP MET ASP ASP ASN ASN GLY ILE LYS ASN ARG ASP GLY
SEQRES 31 543 LEU ASP ASP ILE VAL GLY ASP HIS ASN VAL ILE CYS PRO
SEQRES 32 543 LEU MET HIS PHE VAL ASN LYS TYR THR LYS PHE GLY ASN
SEQRES 33 543 GLY THR TYR LEU TYR PHE PHE ASN HIS ARG ALA SER ASN
SEQRES 34 543 LEU VAL TRP PRO GLU TRP MET GLY VAL ILE HIS GLY TYR
SEQRES 35 543 GLU ILE GLU PHE VAL PHE GLY LEU PRO LEU VAL LYS GLU
SEQRES 36 543 LEU ASN TYR THR ALA GLU GLU GLU ALA LEU SER ARG ARG
SEQRES 37 543 ILE MET HIS TYR TRP ALA THR PHE ALA LYS THR GLY ASN
SEQRES 38 543 PRO ASN GLU PRO HIS SER GLN GLU SER LYS TRP PRO LEU
SEQRES 39 543 PHE THR THR LYS GLU GLN LYS PHE ILE ASP LEU ASN THR
SEQRES 40 543 GLU PRO MET LYS VAL HIS GLN ARG LEU ARG VAL GLN MET
SEQRES 41 543 CYS VAL PHE TRP ASN GLN PHE LEU PRO LYS LEU LEU ASN
SEQRES 42 543 ALA THR ALA CYS ASP GLY GLU LEU SER SER
MODRES 1EVE ASN 59 ASN N-GLYCOSYLATION SITE
MODRES 1EVE ASN 416 ASN N-GLYCOSYLATION SITE
MODRES 1EVE ASN 457 ASN N-GLYCOSYLATION SITE
MODRES 1EVE ASN 533 ASN N-GLYCOSYLATION SITE
HET E20 2001 28
HET NAG 3001 14
HET NAG 3002 14
HET NAG 3003 14
HET NAG 3004 14
HET NAG 3005 14
HETNAM E20 1-BENZYL-4-[(5,6-DIMETHOXY-1-INDANON-2-YL)METHYL]
HETNAM 2 E20 PIPERIDINE
HETNAM NAG N-ACETYL-D-GLUCOSAMINE
HETSYN E20 E2020
FORMUL 2 E20 C24 H29 N1 O3
FORMUL 3 NAG 5(C8 H15 N1 O6)
FORMUL 4 HOH *396(H2 O1)
HELIX 1 1 GLY 41 MET 43 5 3
HELIX 2 2 SER 79 TRP 84 1 6
HELIX 3 3 ASP 128 TYR 130 5 3
HELIX 4 4 LYS 133 GLU 139 1 7
HELIX 5 5 GLY 151 PHE 155 1 5
HELIX 6 6 VAL 168 PHE 187 1 20
HELIX 7 7 ALA 201 LEU 211 1 11
HELIX 8 8 PRO 213 LEU 218 1 6
HELIX 9 9 VAL 238 LEU 252 1 15
HELIX 10 10 ASP 259 GLU 268 1 10
HELIX 11 11 PRO 271 VAL 281 1 11
HELIX 12 12 LEU 305 SER 311 1 7
HELIX 13 13 SER 329 GLY 335 1 7
HELIX 14 14 ARG 349 SER 359 1 11
HELIX 15 15 ASP 365 GLN 374 1 10
HELIX 16 16 GLY 384 ASN 399 1 16
HELIX 17 17 ILE 401 PHE 414 1 14
HELIX 18 18 GLU 434 MET 436 5 3
HELIX 19 19 ILE 444 VAL 447 1 4
HELIX 20 20 LEU 450 LEU 452 5 3
HELIX 21 21 LYS 454 LEU 456 5 3
HELIX 22 22 ALA 460 THR 479 1 20
HELIX 23 23 VAL 518 ASN 525 1 8
HELIX 24 24 PHE 527 ASN 533 1 7
SHEET 1 A 3 LEU 6 THR 10 0
SHEET 2 A 3 GLY 13 MET 16 -1 N VAL 15 O VAL 8
SHEET 3 A 3 VAL 57 ALA 60 1 N TRP 58 O LYS 14
SHEET 1 B11 MET 16 PRO 21 0
SHEET 2 B11 HIS 26 PRO 34 -1 O ALA 29 N THR 18
SHEET 3 B11 TYR 96 PRO 102 -1 N ILE 99 O PHE 30
SHEET 4 B11 VAL 142 SER 147 -1 N LEU 143 O TRP 100
SHEET 5 B11 THR 109 TYR 116 1 N MET 112 O VAL 142
SHEET 6 B11 THR 193 GLU 199 1 O THR 195 N VAL 113
SHEET 7 B11 ARG 220 SER 226 1 N ILE 223 O ILE 196
SHEET 8 B11 GLN 318 ASN 324 1 N GLY 322 O LEU 224
SHEET 9 B11 GLY 417 PHE 423 1 N TYR 421 O LEU 321
SHEET 10 B11 PHE 502 LEU 505 1 N ILE 503 O LEU 420
SHEET 11 B11 MET 510 GLN 514 -1 N HIS 513 O PHE 502
SSBOND 1 CYS 67 CYS 94
SSBOND 2 CYS 254 CYS 265
SSBOND 3 CYS 402 CYS 521
LINK C1 NAG 3001 ND2 ASN 59
LINK C1 NAG 3002 ND2 ASN 416
LINK O4 NAG 3002 C1 NAG 3003
LINK C1 NAG 3004 ND2 ASN 533
LINK C1 NAG 3005 ND2 ASN 457
CISPEP 1 SER 103 PRO 104 0 -0.32
SITE 1 CAT 3 SER 200 GLU 327 HIS 440
SITE 1 IHB 3 TRP 84 PHE 330 TRP 279
CRYST1 111.925 111.925 136.896 90.00 90.00 120.00 P 31 2 1 6
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.008935 0.005158 0.000000 0.00000
SCALE2 0.000000 0.010317 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007305 0.00000 |