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HEADER HYDROLASE 29-OCT-97 2ACK
TITLE ACETYLCHOLINESTERASE COMPLEXED WITH EDROPHONIUM,
TITLE 2 MONOCHROMATIC DATA
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ACETYLCHOLINESTERASE;
COMPND 3 CHAIN: NULL;
COMPND 4 EC: 3.1.1.7
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: TORPEDO CALIFORNICA;
SOURCE 3 ORGANISM_COMMON: PACIFIC ELECTRIC RAY;
SOURCE 4 ORGAN: ELECTRIC ORGAN
KEYWDS HYDROLASE, CARBOXYLIC ESTERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR M.L.RAVES,J.L.SUSSMAN,M.HAREL,I.SILMAN
REVDAT 1 11-FEB-98 2ACK 0
SPRSDE 11-FEB-98 2ACK 1ACK
JRNL AUTH R.B.G.RAVELLI,M.L.RAVES,Z.REN,D.BOURGEOIS,M.ROTH,
JRNL AUTH 2 J.KROON,I.SILMAN,J.L.SUSSMAN
JRNL TITL STATIC LAUE DIFFRACTION STUDIES ON
JRNL TITL 2 ACETYLCHOLINESTERASE
JRNL REF TO BE PUBLISHED
JRNL REFN 0353
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH M.HAREL,I.SCHALK,L.EHRET-SABATIER,F.BOUET,
REMARK 1 AUTH 2 M.GOELDNER,C.HIRTH,P.H.AXELSEN,I.SILMAN,J.L.SUSSMAN
REMARK 1 TITL QUATERNARY LIGAND BINDING TO AROMATIC RESIDUES IN
REMARK 1 TITL 2 THE ACTIVE-SITE GORGE OF ACETYLCHOLINESTERASE
REMARK 1 REF PROC.NAT.ACAD.SCI.USA V. 90 9031 1993
REMARK 1 REFN ASTM PNASA6 US ISSN 0027-8424 0040
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 1 REFERENCE 3
REMARK 1 AUTH J.L.SUSSMAN,M.HAREL,F.FROLOW,L.VARON,L.TOKER,
REMARK 1 AUTH 2 A.H.FUTERMAN,I.SILMAN
REMARK 1 TITL PURIFICATION AND CRYSTALLIZATION OF A DIMERIC FORM
REMARK 1 TITL 2 OF ACETYLCHOLINESTERASE FROM TORPEDO CALIFORNICA
REMARK 1 TITL 3 SUBSEQUENT TO SOLUBILIZATION WITH
REMARK 1 TITL 4 PHOSPHATIDYLINOSITOL-SPECIFIC PHOSPHOLIPASE C
REMARK 1 REF J.MOL.BIOL. V. 203 821 1988
REMARK 1 REFN ASTM JMOBAK UK ISSN 0022-2836 0070
REMARK 2
REMARK 2 RESOLUTION. 2.4 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC
REMARK 3 AUTHORS : MURSHUDOV,VAGIN,DODSON
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.4
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 20.0
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.0
REMARK 3 COMPLETENESS FOR RANGE (%) : 97.7
REMARK 3 NUMBER OF REFLECTIONS : 38560
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 + TEST SET) : 0.213
REMARK 3 R VALUE (WORKING SET) : NULL
REMARK 3 FREE R VALUE : 0.257
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.9
REMARK 3 FREE R VALUE TEST SET COUNT : 1890
REMARK 3
REMARK 3 FIT/AGREEMENT OF MODEL WITH ALL DATA.
REMARK 3 R VALUE (WORKING + TEST SET, NO CUTOFF) : 0.213
REMARK 3 R VALUE (WORKING SET, NO CUTOFF) : NULL
REMARK 3 FREE R VALUE (NO CUTOFF) : 0.257
REMARK 3 FREE R VALUE TEST SET SIZE (%, NO CUTOFF) : 4.9
REMARK 3 FREE R VALUE TEST SET COUNT (NO CUTOFF) : 1890
REMARK 3 TOTAL NUMBER OF REFLECTIONS (NO CUTOFF) : 38560
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 4146
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 12
REMARK 3 SOLVENT ATOMS : 254
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 37.3
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM SIGMAA (A) : NULL
REMARK 3 LOW RESOLUTION CUTOFF (A) : NULL
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 DISTANCE RESTRAINTS. RMS SIGMA
REMARK 3 BOND LENGTH (A) : NULL ; NULL
REMARK 3 ANGLE DISTANCE (A) : NULL ; NULL
REMARK 3 INTRAPLANAR 1-4 DISTANCE (A) : NULL ; NULL
REMARK 3 H-BOND OR METAL COORDINATION (A) : NULL ; NULL
REMARK 3
REMARK 3 PLANE RESTRAINT (A) : NULL ; NULL
REMARK 3 CHIRAL-CENTER RESTRAINT (A**3) : NULL ; NULL
REMARK 3
REMARK 3 NON-BONDED CONTACT RESTRAINTS.
REMARK 3 SINGLE TORSION (A) : NULL ; NULL
REMARK 3 MULTIPLE TORSION (A) : NULL ; NULL
REMARK 3 H-BOND (X...Y) (A) : NULL ; NULL
REMARK 3 H-BOND (X-H...Y) (A) : NULL ; NULL
REMARK 3
REMARK 3 CONFORMATIONAL TORSION ANGLE RESTRAINTS.
REMARK 3 SPECIFIED (DEGREES) : NULL ; NULL
REMARK 3 PLANAR (DEGREES) : NULL ; NULL
REMARK 3 STAGGERED (DEGREES) : NULL ; NULL
REMARK 3 TRANSVERSE (DEGREES) : NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 2ACK COMPLIES WITH FORMAT V. 2.2, 16-DEC-1996
REMARK 6
REMARK 6 TORPEDO CALIFONICA 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.
REMARK 7
REMARK 7 SEVERAL RESIDUES ARE NOT SEEN IN THE CRYSTAL STRUCTURE,
REMARK 7 DUE TO DISORDER. THESE INCLUDE THREE N-TERMINAL RESIDUES
REMARK 7 (ASP 1, ASP 2, HIS 3), THE LOOP FROM PRO 485 TO GLU 489
REMARK 7 AND THE C-TERMINAL RESIDUES AFTER THR 535.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : OCT-1993
REMARK 200 TEMPERATURE (KELVIN) : 273
REMARK 200 PH : 5.8
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : DESY-EMBL,HAMBURG
REMARK 200 BEAMLINE : X11
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.92
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 38611
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.4
REMARK 200 RESOLUTION RANGE LOW (A) : 33.3
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 97.7
REMARK 200 DATA REDUNDANCY : 3.1
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.089
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 14.0
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.40
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.46
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.6
REMARK 200 DATA REDUNDANCY IN SHELL : 3.1
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.42
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.1
REMARK 200
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR
REMARK 200 REPLACEMENT
REMARK 200 SOFTWARE USED: REFMAC
REMARK 200 STARTING MODEL: PDB ENTRY 2ACE
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 65.
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.6
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PROTEIN WAS CRYSTALLISED FROM
REMARK 280 40 % PEG200, 100 MM MES, PH 5.8 AT 4 DEGREES C.
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 -0.500000 -0.866007 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866044 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 45.51869
REMARK 290 SMTRY1 3 -0.500000 0.866007 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.866044 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 91.03737
REMARK 290 SMTRY1 4 -0.500000 0.866007 0.000000 0.00000
REMARK 290 SMTRY2 4 0.866044 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 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 91.03737
REMARK 290 SMTRY1 6 -0.500000 -0.866007 0.000000 0.00000
REMARK 290 SMTRY2 6 -0.866044 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 45.51869
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE
REMARK 300 THE ENZYME IS A GPI-ANCHORED DIMER. THE TWO MONOMERS IN
REMARK 300 THE DIMER ARE RELATED BY CRYSTALLOGRAPHIC TWO-FOLD
REMARK 300 SYMMETRY.
REMARK 350
REMARK 350 GENERATING THE BIOMOLECULE
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 APPLY THE FOLLOWING TO CHAINS: NULL
REMARK 350 BIOMT1 3 -0.500000 0.866007 0.000000 0.00000
REMARK 350 BIOMT2 3 0.866044 0.500000 0.000000 0.00000
REMARK 350 BIOMT3 3 0.000000 0.000000 -1.000000 136.55606
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 ASN 42 OD1 ND2
REMARK 470 ARG 46 CZ NH1 NH2
REMARK 470 GLU 49 OE1 OE2
REMARK 470 GLN 162 OE1 NE2
REMARK 470 ARG 250 CZ NH1 NH2
REMARK 470 ASN 257 CG OD1 ND2
REMARK 470 GLU 268 OE1 OE2
REMARK 470 LYS 270 CE NZ
REMARK 470 GLU 299 CD OE1 OE2
REMARK 470 GLU 344 OE1 OE2
REMARK 470 GLU 350 OE1 OE2
REMARK 470 LYS 413 CD CE NZ
REMARK 470 GLU 434 CD OE1 OE2
REMARK 470 LYS 454 CD CE NZ
REMARK 470 LYS 491 CD CE NZ
REMARK 470 LYS 498 CG CD CE NZ
REMARK 470 GLU 499 OE1 OE2
REMARK 470 GLU 508 CD OE1 OE2
REMARK 470 LYS 511 CD CE NZ
REMARK 470 ARG 515 CZ NH1 NH2
REMARK 470 GLN 526 OE1 NE2
REMARK 470 ASN 533 OD1 ND2
REMARK 650
REMARK 650 HELIX
REMARK 650 DETERMINATION METHOD: TAKEN FROM RELEASED PDB ENTRY 2ACE
REMARK 700
REMARK 700 SHEET
REMARK 700 DETERMINATION METHOD: TAKEN FROM RELEASED PDB ENTRY 2ACE
REMARK 700 STRAND: A3 1; SMALL BETA SHEET.
REMARK 700 STRAND: B11 1; LARGE BETA SHEET.
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: CAT
REMARK 800 SITE_DESCRIPTION: CATALYTIC TRIAD.
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 THIS ENTRY IS RELATED TO PDB ENTRY 1AX9.
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 2ACK SWS P04058 1 - 24 NOT IN ATOMS LIST
REMARK 999 2ACK SWS P04058 557 - 586 NOT IN ATOMS LIST
DBREF 2ACK 4 484 SWS P04058 ACES_TORCA 25 505
DBREF 2ACK 490 535 SWS P04058 ACES_TORCA 511 556
SEQADV 2ACK SWS P04058 PRO 506 GAP IN PDB ENTRY
SEQADV 2ACK SWS P04058 HIS 507 GAP IN PDB ENTRY
SEQADV 2ACK SWS P04058 SER 508 GAP IN PDB ENTRY
SEQADV 2ACK SWS P04058 GLN 509 GAP IN PDB ENTRY
SEQADV 2ACK SWS P04058 GLU 510 GAP IN PDB ENTRY
SEQRES 1 537 ASP ASP HIS SER GLU LEU LEU VAL ASN THR LYS SER GLY
SEQRES 2 537 LYS VAL MET GLY THR ARG VAL PRO VAL LEU SER SER HIS
SEQRES 3 537 ILE SER ALA PHE LEU GLY ILE PRO PHE ALA GLU PRO PRO
SEQRES 4 537 VAL GLY ASN MET ARG PHE ARG ARG PRO GLU PRO LYS LYS
SEQRES 5 537 PRO TRP SER GLY VAL TRP ASN ALA SER THR TYR PRO ASN
SEQRES 6 537 ASN CYS GLN GLN TYR VAL ASP GLU GLN PHE PRO GLY PHE
SEQRES 7 537 SER GLY SER GLU MET TRP ASN PRO ASN ARG GLU MET SER
SEQRES 8 537 GLU ASP CYS LEU TYR LEU ASN ILE TRP VAL PRO SER PRO
SEQRES 9 537 ARG PRO LYS SER THR THR VAL MET VAL TRP ILE TYR GLY
SEQRES 10 537 GLY GLY PHE TYR SER GLY SER SER THR LEU ASP VAL TYR
SEQRES 11 537 ASN GLY LYS TYR LEU ALA TYR THR GLU GLU VAL VAL LEU
SEQRES 12 537 VAL SER LEU SER TYR ARG VAL GLY ALA PHE GLY PHE LEU
SEQRES 13 537 ALA LEU HIS GLY SER GLN GLU ALA PRO GLY ASN VAL GLY
SEQRES 14 537 LEU LEU ASP GLN ARG MET ALA LEU GLN TRP VAL HIS ASP
SEQRES 15 537 ASN ILE GLN PHE PHE GLY GLY ASP PRO LYS THR VAL THR
SEQRES 16 537 ILE PHE GLY GLU SER ALA GLY GLY ALA SER VAL GLY MET
SEQRES 17 537 HIS ILE LEU SER PRO GLY SER ARG ASP LEU PHE ARG ARG
SEQRES 18 537 ALA ILE LEU GLN SER GLY SER PRO ASN CYS PRO TRP ALA
SEQRES 19 537 SER VAL SER VAL ALA GLU GLY ARG ARG ARG ALA VAL GLU
SEQRES 20 537 LEU GLY ARG ASN LEU ASN CYS ASN LEU ASN SER ASP GLU
SEQRES 21 537 GLU LEU ILE HIS CYS LEU ARG GLU LYS LYS PRO GLN GLU
SEQRES 22 537 LEU ILE ASP VAL GLU TRP ASN VAL LEU PRO PHE ASP SER
SEQRES 23 537 ILE PHE ARG PHE SER PHE VAL PRO VAL ILE ASP GLY GLU
SEQRES 24 537 PHE PHE PRO THR SER LEU GLU SER MET LEU ASN SER GLY
SEQRES 25 537 ASN PHE LYS LYS THR GLN ILE LEU LEU GLY VAL ASN LYS
SEQRES 26 537 ASP GLU GLY SER PHE PHE LEU LEU TYR GLY ALA PRO GLY
SEQRES 27 537 PHE SER LYS ASP SER GLU SER LYS ILE SER ARG GLU ASP
SEQRES 28 537 PHE MET SER GLY VAL LYS LEU SER VAL PRO HIS ALA ASN
SEQRES 29 537 ASP LEU GLY LEU ASP ALA VAL THR LEU GLN TYR THR ASP
SEQRES 30 537 TRP MET ASP ASP ASN ASN GLY ILE LYS ASN ARG ASP GLY
SEQRES 31 537 LEU ASP ASP ILE VAL GLY ASP HIS ASN VAL ILE CYS PRO
SEQRES 32 537 LEU MET HIS PHE VAL ASN LYS TYR THR LYS PHE GLY ASN
SEQRES 33 537 GLY THR TYR LEU TYR PHE PHE ASN HIS ARG ALA SER ASN
SEQRES 34 537 LEU VAL TRP PRO GLU TRP MET GLY VAL ILE HIS GLY TYR
SEQRES 35 537 GLU ILE GLU PHE VAL PHE GLY LEU PRO LEU VAL LYS GLU
SEQRES 36 537 LEU ASN TYR THR ALA GLU GLU GLU ALA LEU SER ARG ARG
SEQRES 37 537 ILE MET HIS TYR TRP ALA THR PHE ALA LYS THR GLY ASN
SEQRES 38 537 PRO ASN GLU PRO HIS SER GLN GLU SER LYS TRP PRO LEU
SEQRES 39 537 PHE THR THR LYS GLU GLN LYS PHE ILE ASP LEU ASN THR
SEQRES 40 537 GLU PRO MET LYS VAL HIS GLN ARG LEU ARG VAL GLN MET
SEQRES 41 537 CYS VAL PHE TRP ASN GLN PHE LEU PRO LYS LEU LEU ASN
SEQRES 42 537 ALA THR ALA CYS
HET EDR 999 12
HETNAM EDR EDROPHONIUM ION
FORMUL 2 EDR C10 H16 N1 O1 1+
FORMUL 3 HOH *252(H2 O1)
HELIX 1 H1 SER 79 ASN 85 1 7
HELIX 2 H2 GLY 132 GLU 139 1 8
HELIX 3 H3 VAL 168 ASN 183 1 16
HELIX 4 H4 SER 200 LEU 211 1 12
HELIX 5 H5 VAL 238 LEU 252 1 15
HELIX 6 H6 ASP 259 GLU 268 1 10
HELIX 7 H7 PRO 271 GLU 278 1 8
HELIX 8 H8 LEU 305 SER 311 1 7
HELIX 9 H9 SER 329 GLY 335 1 7
HELIX 10 H10 ARG 349 VAL 360 1 12
HELIX 11 H11 ASP 365 THR 376 1 12
HELIX 12 H12 GLY 384 VAL 400 1 17
HELIX 13 H13 VAL 400 TYR 411 1 12
HELIX 14 H14 GLU 443 PHE 448 1 6
HELIX 15 H15 ALA 460 THR 479 1 20
HELIX 16 H16 VAL 518 ALA 534 1 17
SHEET 1 A3 2 LEU 6 THR 10 0
SHEET 2 A3 2 GLY 13 MET 16 -1
SHEET 1 B12 2 MET 16 PRO 21 0
SHEET 2 B12 2 HIS 26 PRO 34 -1
SHEET 1 A4 1 VAL 57 ALA 60 0
SHEET 1 B11 9 TYR 96 PRO 102 0
SHEET 2 B11 9 VAL 142 SER 147 -1
SHEET 3 B11 9 THR 109 TYR 116 1
SHEET 4 B11 9 THR 193 GLU 199 1
SHEET 5 B11 9 ARG 220 SER 226 1
SHEET 6 B11 9 GLN 318 ASN 324 1
SHEET 7 B11 9 GLY 417 PHE 423 1
SHEET 8 B11 9 PHE 502 LEU 505 1
SHEET 9 B11 9 MET 510 GLN 514 -1
SSBOND 1 CYS 67 CYS 94
SSBOND 2 CYS 254 CYS 265
SSBOND 3 CYS 402 CYS 521
CISPEP 1 SER 103 PRO 104 0 7.69
SITE 1 CAT 3 SER 200 HIS 440 GLU 327
CRYST1 112.409 112.409 136.550 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 0.008896 0.005136 0.000000 0.00000
SCALE2 0.000000 0.010272 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007323 0.00000 |