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HEADER HYDROLASE 22-SEP-11 4A23
TITLE MUS MUSCULUS ACETYLCHOLINESTERASE IN COMPLEX WITH RACEMIC
TITLE 2 C5685
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ACETYLCHOLINESTERASE;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: CATALYTIC DOMAIN, RESIDUES 32-574;
COMPND 5 SYNONYM: ACHE;
COMPND 6 EC: 3.1.1.7;
COMPND 7 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MUS MUSCULUS;
SOURCE 3 ORGANISM_COMMON: HOUSE MOUSE;
SOURCE 4 ORGANISM_TAXID: 10090;
SOURCE 5 EXPRESSION_SYSTEM: HOMO SAPIENS;
SOURCE 6 EXPRESSION_SYSTEM_COMMON: HUMAN;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 9606
KEYWDS HYDROLASE, CHOLINESTERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR L.BERG,C.D.ANDERSSON,E.ARTRURSSON,A.HORNBERG,A.K.TUNEMALM,A.LINUSSON,
AUTHOR 2 F.EKSTROM
REVDAT 1 07-DEC-11 4A23 0
JRNL AUTH L.BERG,C.D.ANDERSSON,E.ARTRURSSON,A.HORNBERG,A.K.TUNEMALM,
JRNL AUTH 2 A.LINUSSON,F.EKSTROM
JRNL TITL TARGETING ACETYLCHOLINESTERASE IDENTIFICATION OF CHEMICAL
JRNL TITL 2 LEADS BY HIGH THROUGHPUT SCREENING, STRUCTURE DETERMINATION
JRNL TITL 3 AND MOLECULAR MODELLING
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.40 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE)
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VICENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,
REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,
REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,
REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON,
REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,
REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT
REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.400
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 28.809
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.39
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.32
REMARK 3 NUMBER OF REFLECTIONS : 78783
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.1750
REMARK 3 R VALUE (WORKING SET) : 0.1743
REMARK 3 FREE R VALUE : 0.2089
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 2.0
REMARK 3 FREE R VALUE TEST SET COUNT : 1557
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS).
REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE
REMARK 3 1 28.8114 - 5.3273 0.96 7152 144 0.1774 0.2153
REMARK 3 2 5.3273 - 4.2328 1.00 7159 140 0.1308 0.1358
REMARK 3 3 4.2328 - 3.6990 1.00 7073 138 0.1365 0.1760
REMARK 3 4 3.6990 - 3.3613 1.00 7057 140 0.1613 0.1807
REMARK 3 5 3.3613 - 3.1207 1.00 6997 135 0.1742 0.2074
REMARK 3 6 3.1207 - 2.9369 1.00 7004 156 0.1875 0.2101
REMARK 3 7 2.9369 - 2.7899 1.00 6989 139 0.1881 0.2625
REMARK 3 8 2.7899 - 2.6686 1.00 6974 145 0.1933 0.2512
REMARK 3 9 2.6686 - 2.5659 1.00 6961 153 0.1909 0.2553
REMARK 3 10 2.5659 - 2.4774 0.99 6928 140 0.2004 0.2207
REMARK 3 11 2.4774 - 2.4000 0.99 6932 127 0.2341 0.3111
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.11
REMARK 3 SHRINKAGE RADIUS : 0.90
REMARK 3 K_SOL : 0.349
REMARK 3 B_SOL : 72.489
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.12
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 20.08
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 48.24
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.7570
REMARK 3 B22 (A**2) : 1.7098
REMARK 3 B33 (A**2) : -2.4668
REMARK 3 B12 (A**2) : 0.0000
REMARK 3 B13 (A**2) : 0.0000
REMARK 3 B23 (A**2) : 0.0000
REMARK 3
REMARK 3 TWINNING INFORMATION.
REMARK 3 FRACTION: NULL
REMARK 3 OPERATOR: NULL
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : 0.008 8726
REMARK 3 ANGLE : 1.135 11900
REMARK 3 CHIRALITY : 0.077 1269
REMARK 3 PLANARITY : 0.006 1567
REMARK 3 DIHEDRAL : 17.609 3116
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 4A23 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 22-SEP-11.
REMARK 100 THE PDBE ID CODE IS EBI-49730.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 15-FEB-08
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : MAX II
REMARK 200 BEAMLINE : I911-3
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.03790
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 79324
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.40
REMARK 200 RESOLUTION RANGE LOW (A) : 19.64
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 3.0
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.6
REMARK 200 DATA REDUNDANCY : 7.4
REMARK 200 R MERGE (I) : 0.05
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 25.80
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) : 2.53
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.8
REMARK 200 DATA REDUNDANCY IN SHELL : 7.5
REMARK 200 R MERGE FOR SHELL (I) : 0.04
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 7.50
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: ISOMORPHOUS REPLACEMENT
REMARK 200 SOFTWARE USED: REFMAC
REMARK 200 STARTING MODEL: PDB ENTRY 1J06
REMARK 200
REMARK 200 REMARK: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 68
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.87
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
REMARK 290 4555 X+1/2,-Y+1/2,-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 -1.000000 0.000000 0.000000 39.46150
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 113.49950
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 55.91400
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 113.49950
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 39.46150
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 55.91400
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
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 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 3430 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 37490 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -3.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 PRO A 258
REMARK 465 PRO A 259
REMARK 465 GLY A 260
REMARK 465 GLY A 261
REMARK 465 ALA A 262
REMARK 465 GLY A 263
REMARK 465 GLY A 264
REMARK 465 THR A 543
REMARK 465 ALA A 544
REMARK 465 THR A 545
REMARK 465 GLU A 546
REMARK 465 ALA A 547
REMARK 465 PRO A 548
REMARK 465 GLU B 1
REMARK 465 GLY B 2
REMARK 465 ARG B 3
REMARK 465 PRO B 258
REMARK 465 PRO B 259
REMARK 465 GLY B 260
REMARK 465 GLY B 261
REMARK 465 ALA B 262
REMARK 465 GLY B 263
REMARK 465 GLY B 264
REMARK 465 THR B 545
REMARK 465 GLU B 546
REMARK 465 ALA B 547
REMARK 465 PRO B 548
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 LYS A 23 CD CE NZ
REMARK 470 LYS A 496 CG CD CE NZ
REMARK 470 ARG B 493 CG CD NE CZ NH1 NH2
REMARK 470 ALA B 544 CA C O CB
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 PHE A 47 -5.46 75.93
REMARK 500 PHE A 158 -5.15 -141.31
REMARK 500 ALA A 167 67.44 -157.38
REMARK 500 ASN A 170 18.22 54.08
REMARK 500 SER A 203 -120.03 57.20
REMARK 500 ASP A 306 -88.69 -122.81
REMARK 500 HIS A 387 57.84 -147.27
REMARK 500 VAL A 407 -63.92 -128.15
REMARK 500 ARG A 525 55.25 39.28
REMARK 500 PHE B 47 -1.99 71.89
REMARK 500 ALA B 62 53.04 -116.54
REMARK 500 SER B 93 147.51 -173.70
REMARK 500 ALA B 167 70.67 -154.58
REMARK 500 SER B 203 -121.59 57.41
REMARK 500 ASP B 306 -83.75 -121.09
REMARK 500 VAL B 407 -61.39 -128.23
REMARK 500 LYS B 496 134.41 60.39
REMARK 500 SER B 497 -58.10 -167.12
REMARK 500 ALA B 506 -75.52 -62.52
REMARK 500 ASN B 514 -168.63 -164.05
REMARK 500 SER B 541 44.14 -75.57
REMARK 500 ALA B 542 -88.70 177.88
REMARK 500
REMARK 500 REMARK: NULL
REMARK 600
REMARK 600 HETEROGEN
REMARK 600 C5685 INHIBITOR RECEMIC MIXTURE REPRESENTED AS RESIDUES C56 AND C57.
REMARK 600 4-(DIMETHYLAMINO)-N-[(1-ETHYL-2-PYRROLIDINYL)METHYL]-2-METHOXY-5-
REMARK 600 NITROBENZAMIDE
REMARK 610
REMARK 610 MISSING HETEROATOM
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 610 I=INSERTION CODE):
REMARK 610 M RES C SSEQI
REMARK 610 C56 A 1542
REMARK 610 C56 B 1544
REMARK 610 C57 A 1543
REMARK 610 C57 B 1545
REMARK 610 PE4 B 1547
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE C56 A1542
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE C57 A1543
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG A1544
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG A1545
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG A1546
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE C56 B1544
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE C57 B1545
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG B1546
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PE4 B1547
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG B1548
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2JGH RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF MOUSE ACETYLCHOLINESTERASE INHIBITED
REMARK 900 BY NON-AGED VX
REMARK 900 RELATED ID: 2WHQ RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF ACETYLCHOLINESTERASE, PHOSPHONYLATED BY
REMARK 900 SARIN (AGED) IN COMPLEX WITH HI-6
REMARK 900 RELATED ID: 1MAH RELATED DB: PDB
REMARK 900 FASCICULIN2 - MOUSE ACETYLCHOLINESTERASE COMPLEX
REMARK 900 RELATED ID: 1MAA RELATED DB: PDB
REMARK 900 MOUSE ACETYLCHOLINESTERASE CATALYTIC DOMAIN,
REMARK 900 GLYCOSYLATEDPROTEIN
REMARK 900 RELATED ID: 2HA6 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF MUTANT S203A OF
REMARK 900 MOUSEACETYLCHOLINESTERASE COMPLEXED WITH SUCCINYLCHOLINE
REMARK 900 RELATED ID: 2C0Q RELATED DB: PDB
REMARK 900 NON-AGED FORM OF MOUSE ACETYLCHOLINESTERASE INHIBITED BY
REMARK 900 TABUN
REMARK 900 RELATED ID: 2JGG RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF MOUSE ACETYLCHOLINESTERASE INHIBITED
REMARK 900 BY NON-AGED SARIN
REMARK 900 RELATED ID: 2JGL RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF MOUSE ACETYLCHOLINESTERASE INHIBITED
REMARK 900 BY AGED VX AND SARIN
REMARK 900 RELATED ID: 2XUG RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF MACHE-Y337A-TZ2PA6 ANTI COMPLEX (
REMARK 900 1 WK)
REMARK 900 RELATED ID: 1Q84 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE MOUSE ACETYLCHOLINESTERASE-
REMARK 900 TZ2PA6ANTI COMPLEX
REMARK 900 RELATED ID: 2XUD RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE Y337A MUTANT OF MOUSE
REMARK 900 ACETYLCHOLINESTERASE
REMARK 900 RELATED ID: 2JGM RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF MOUSE ACETYLCHOLINESTERASE INHIBITED
REMARK 900 BY AGED DIISOPROPYL FLUOROPHOSPHATE (DFP)
REMARK 900 RELATED ID: 2XUJ RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF MACHE-Y337A-TZ2PA6 SYN COMPLEX (1
REMARK 900 MTH)
REMARK 900 RELATED ID: 2JGE RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF MOUSE ACETYLCHOLINESTERASE INHIBITED
REMARK 900 BY NON-AGED METHAMIDOPHOS
REMARK 900 RELATED ID: 1Q83 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE MOUSE ACETYLCHOLINESTERASE-
REMARK 900 TZ2PA6SYN COMPLEX
REMARK 900 RELATED ID: 2WLS RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF MUS MUSCULUS ACETYLCHOLINESTERASE IN
REMARK 900 COMPLEX WITH AMTS13
REMARK 900 RELATED ID: 2XUP RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE MACHE-Y337A MUTANT IN COMPLEX
REMARK 900 WITH SOAKED TZ2PA6 SYN INHIBITOR
REMARK 900 RELATED ID: 2XUK RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF MACHE-Y337A-TZ2PA6 SYN COMPLEX (
REMARK 900 10 MTH)
REMARK 900 RELATED ID: 1C2B RELATED DB: PDB
REMARK 900 ELECTROPHORUS ELECTRICUS ACETYLCHOLINESTERASE
REMARK 900 RELATED ID: 2Y2U RELATED DB: PDB
REMARK 900 NONAGED FORM OF MOUSE ACETYLCHOLINESTERASE INHIBITED BY
REMARK 900 VX-UPDATE
REMARK 900 RELATED ID: 2HA3 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF MOUSE ACETYLCHOLINESTERASE
REMARK 900 COMPLEXEDWITH CHOLINE
REMARK 900 RELATED ID: 2HA0 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF MOUSE ACETYLCHOLINESTERASE
REMARK 900 COMPLEXEDWITH 4-KETOAMYLTRIMETHYLAMMONIUM
REMARK 900 RELATED ID: 2WU3 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF MOUSE ACETYLCHOLINESTERASE IN COMPLEX
REMARK 900 WITH FENAMIPHOS AND HI-6
REMARK 900 RELATED ID: 2XUF RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF MACHE-Y337A-TZ2PA6 ANTI COMPLEX (
REMARK 900 1 MTH)
REMARK 900 RELATED ID: 2JEY RELATED DB: PDB
REMARK 900 MUS MUSCULUS ACETYLCHOLINESTERASE IN COMPLEX WITH HLO-7
REMARK 900 RELATED ID: 2JGI RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF MOUSE ACETYLCHOLINESTERASE INHIBITED
REMARK 900 BY NON-AGED DIISOPROPYL FLUOROPHOSPHATE (DFP)
REMARK 900 RELATED ID: 1N5R RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE MOUSE ACETYLCHOLINESTERASE-
REMARK 900 PROPIDIUM COMPLEX
REMARK 900 RELATED ID: 2XUH RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF MACHE-Y337A-TZ2PA6 ANTI COMPLEX (
REMARK 900 10 MTH)
REMARK 900 RELATED ID: 2JGJ RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF MOUSE ACETYLCHOLINESTERASE INHIBITED
REMARK 900 BY AGED METHAMIDOPHOS
REMARK 900 RELATED ID: 1J06 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF MOUSE ACETYLCHOLINESTERASE IN THE
REMARK 900 APOFORM
REMARK 900 RELATED ID: 2C0P RELATED DB: PDB
REMARK 900 AGED FORM OF MOUSE ACETYLCHOLINESTERASE INHIBITED BY
REMARK 900 TABUN
REMARK 900 RELATED ID: 2JF0 RELATED DB: PDB
REMARK 900 MUS MUSCULUS ACETYLCHOLINESTERASE IN COMPLEX WITH TABUN
REMARK 900 AND ORTHO-7
REMARK 900 RELATED ID: 2XUO RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF MACHE-Y337A MUTANT IN COMPLEX
REMARK 900 WITH SOAKED TZ2PA6 ANTI INHIBITOR
REMARK 900 RELATED ID: 2H9Y RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF MOUSE ACETYLCHOLINESTERASE
REMARK 900 COMPLEXEDWITH M-(N,N,N-TRIMETHYLAMMONIO)
REMARK 900 TRIFLUOROACETOPHENONE
REMARK 900 RELATED ID: 2WHR RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF ACETYLCHOLINESTERASE IN COMPLEX WITH
REMARK 900 K027
REMARK 900 RELATED ID: 2XUI RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF MACHE-Y337A-TZ2PA6 SYN COMPLEX (1
REMARK 900 WK)
REMARK 900 RELATED ID: 1N5M RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE MOUSE ACETYLCHOLINESTERASE-
REMARK 900 GALLAMINE COMPLEX
REMARK 900 RELATED ID: 2HA5 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF MUTANT S203A OF
REMARK 900 ACETYLCHOLINESTERASECOMPLEXED WITH ACETYLTHIOCHOLINE
REMARK 900 RELATED ID: 2HA2 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF MOUSE ACETYLCHOLINESTERASE
REMARK 900 COMPLEXEDWITH SUCCINYLCHOLINE
REMARK 900 RELATED ID: 2XUQ RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE MACHE-Y337A MUTANT IN COMPLEX
REMARK 900 WITH SOAKED TZ2PA6 ANTI-SYN INHIBITORS
REMARK 900 RELATED ID: 2WHP RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF ACETYLCHOLINESTERASE, PHOSPHONYLATED BY
REMARK 900 SARIN AND IN COMPLEX WITH HI-6
REMARK 900 RELATED ID: 2JEZ RELATED DB: PDB
REMARK 900 MUS MUSCULUS ACETYLCHOLINESTERASE IN COMPLEX WITH TABUN
REMARK 900 AND HLO-7
REMARK 900 RELATED ID: 2JGK RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF MOUSE ACETYLCHOLINESTERASE INHIBITED
REMARK 900 BY AGED FENAMIPHOS
REMARK 900 RELATED ID: 1KU6 RELATED DB: PDB
REMARK 900 FASCICULIN 2-MOUSE ACETYLCHOLINESTERASE COMPLEX
REMARK 900 RELATED ID: 2HA4 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF MUTANT S203A OF
REMARK 900 MOUSEACETYLCHOLINESTERASE COMPLEXED WITH ACETYLCHOLINE
REMARK 900 RELATED ID: 1J07 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE MOUSE ACETYLCHOLINESTERASE-
REMARK 900 DECIDIUM COMPLEX
REMARK 900 RELATED ID: 2HA7 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF MUTANT S203A OF
REMARK 900 MOUSEACETYLCHOLINESTERASE COMPLEXED WITH BUTYRYLTHIOCHOLINE
REMARK 900 RELATED ID: 2JGF RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF MOUSE ACETYLCHOLINESTERASE INHIBITED
REMARK 900 BY NON-AGED FENAMIPHOS
REMARK 900 RELATED ID: 2Y2V RELATED DB: PDB
REMARK 900 NONAGED FORM OF MOUSE ACETYLCHOLINESTERASE INHIBITED BY
REMARK 900 SARIN-UPDATE
REMARK 900 RELATED ID: 2WU4 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF MOUSE ACETYLCHOLINESTERASE IN COMPLEX
REMARK 900 WITH FENAMIPHOS AND ORTHO-7
REMARK 900 RELATED ID: 1C2O RELATED DB: PDB
REMARK 900 ELECTROPHORUS ELECTRICUS ACETYLCHOLINESTERASE
REMARK 900 RELATED ID: 4A16 RELATED DB: PDB
REMARK 900 STRUCTURE OF MOUSE ACETYLCHOLINESTERASE COMPLEX WITH
REMARK 900 HUPRINE DERIVATIVE
DBREF 4A23 A 1 543 UNP P21836 ACES_MOUSE 32 574
DBREF 4A23 B 1 543 UNP P21836 ACES_MOUSE 32 574
SEQADV 4A23 ALA A 544 UNP P21836 EXPRESSION TAG
SEQADV 4A23 THR A 545 UNP P21836 EXPRESSION TAG
SEQADV 4A23 GLU A 546 UNP P21836 EXPRESSION TAG
SEQADV 4A23 ALA A 547 UNP P21836 EXPRESSION TAG
SEQADV 4A23 PRO A 548 UNP P21836 EXPRESSION TAG
SEQADV 4A23 ALA B 544 UNP P21836 EXPRESSION TAG
SEQADV 4A23 THR B 545 UNP P21836 EXPRESSION TAG
SEQADV 4A23 GLU B 546 UNP P21836 EXPRESSION TAG
SEQADV 4A23 ALA B 547 UNP P21836 EXPRESSION TAG
SEQADV 4A23 PRO B 548 UNP P21836 EXPRESSION TAG
SEQRES 1 A 548 GLU GLY ARG GLU ASP PRO GLN LEU LEU VAL ARG VAL ARG
SEQRES 2 A 548 GLY GLY GLN LEU ARG GLY ILE ARG LEU LYS ALA PRO GLY
SEQRES 3 A 548 GLY PRO VAL SER ALA PHE LEU GLY ILE PRO PHE ALA GLU
SEQRES 4 A 548 PRO PRO VAL GLY SER ARG ARG PHE MET PRO PRO GLU PRO
SEQRES 5 A 548 LYS ARG PRO TRP SER GLY VAL LEU ASP ALA THR THR PHE
SEQRES 6 A 548 GLN ASN VAL CYS TYR GLN TYR VAL ASP THR LEU TYR PRO
SEQRES 7 A 548 GLY PHE GLU GLY THR GLU MET TRP ASN PRO ASN ARG GLU
SEQRES 8 A 548 LEU SER GLU ASP CYS LEU TYR LEU ASN VAL TRP THR PRO
SEQRES 9 A 548 TYR PRO ARG PRO ALA SER PRO THR PRO VAL LEU ILE TRP
SEQRES 10 A 548 ILE TYR GLY GLY GLY PHE TYR SER GLY ALA ALA SER LEU
SEQRES 11 A 548 ASP VAL TYR ASP GLY ARG PHE LEU ALA GLN VAL GLU GLY
SEQRES 12 A 548 ALA VAL LEU VAL SER MET ASN TYR ARG VAL GLY THR PHE
SEQRES 13 A 548 GLY PHE LEU ALA LEU PRO GLY SER ARG GLU ALA PRO GLY
SEQRES 14 A 548 ASN VAL GLY LEU LEU ASP GLN ARG LEU ALA LEU GLN TRP
SEQRES 15 A 548 VAL GLN GLU ASN ILE ALA ALA PHE GLY GLY ASP PRO MET
SEQRES 16 A 548 SER VAL THR LEU PHE GLY GLU SER ALA GLY ALA ALA SER
SEQRES 17 A 548 VAL GLY MET HIS ILE LEU SER LEU PRO SER ARG SER LEU
SEQRES 18 A 548 PHE HIS ARG ALA VAL LEU GLN SER GLY THR PRO ASN GLY
SEQRES 19 A 548 PRO TRP ALA THR VAL SER ALA GLY GLU ALA ARG ARG ARG
SEQRES 20 A 548 ALA THR LEU LEU ALA ARG LEU VAL GLY CYS PRO PRO GLY
SEQRES 21 A 548 GLY ALA GLY GLY ASN ASP THR GLU LEU ILE ALA CYS LEU
SEQRES 22 A 548 ARG THR ARG PRO ALA GLN ASP LEU VAL ASP HIS GLU TRP
SEQRES 23 A 548 HIS VAL LEU PRO GLN GLU SER ILE PHE ARG PHE SER PHE
SEQRES 24 A 548 VAL PRO VAL VAL ASP GLY ASP PHE LEU SER ASP THR PRO
SEQRES 25 A 548 GLU ALA LEU ILE ASN THR GLY ASP PHE GLN ASP LEU GLN
SEQRES 26 A 548 VAL LEU VAL GLY VAL VAL LYS ASP GLU GLY SER TYR PHE
SEQRES 27 A 548 LEU VAL TYR GLY VAL PRO GLY PHE SER LYS ASP ASN GLU
SEQRES 28 A 548 SER LEU ILE SER ARG ALA GLN PHE LEU ALA GLY VAL ARG
SEQRES 29 A 548 ILE GLY VAL PRO GLN ALA SER ASP LEU ALA ALA GLU ALA
SEQRES 30 A 548 VAL VAL LEU HIS TYR THR ASP TRP LEU HIS PRO GLU ASP
SEQRES 31 A 548 PRO THR HIS LEU ARG ASP ALA MET SER ALA VAL VAL GLY
SEQRES 32 A 548 ASP HIS ASN VAL VAL CYS PRO VAL ALA GLN LEU ALA GLY
SEQRES 33 A 548 ARG LEU ALA ALA GLN GLY ALA ARG VAL TYR ALA TYR ILE
SEQRES 34 A 548 PHE GLU HIS ARG ALA SER THR LEU THR TRP PRO LEU TRP
SEQRES 35 A 548 MET GLY VAL PRO HIS GLY TYR GLU ILE GLU PHE ILE PHE
SEQRES 36 A 548 GLY LEU PRO LEU ASP PRO SER LEU ASN TYR THR THR GLU
SEQRES 37 A 548 GLU ARG ILE PHE ALA GLN ARG LEU MET LYS TYR TRP THR
SEQRES 38 A 548 ASN PHE ALA ARG THR GLY ASP PRO ASN ASP PRO ARG ASP
SEQRES 39 A 548 SER LYS SER PRO GLN TRP PRO PRO TYR THR THR ALA ALA
SEQRES 40 A 548 GLN GLN TYR VAL SER LEU ASN LEU LYS PRO LEU GLU VAL
SEQRES 41 A 548 ARG ARG GLY LEU ARG ALA GLN THR CYS ALA PHE TRP ASN
SEQRES 42 A 548 ARG PHE LEU PRO LYS LEU LEU SER ALA THR ALA THR GLU
SEQRES 43 A 548 ALA PRO
SEQRES 1 B 548 GLU GLY ARG GLU ASP PRO GLN LEU LEU VAL ARG VAL ARG
SEQRES 2 B 548 GLY GLY GLN LEU ARG GLY ILE ARG LEU LYS ALA PRO GLY
SEQRES 3 B 548 GLY PRO VAL SER ALA PHE LEU GLY ILE PRO PHE ALA GLU
SEQRES 4 B 548 PRO PRO VAL GLY SER ARG ARG PHE MET PRO PRO GLU PRO
SEQRES 5 B 548 LYS ARG PRO TRP SER GLY VAL LEU ASP ALA THR THR PHE
SEQRES 6 B 548 GLN ASN VAL CYS TYR GLN TYR VAL ASP THR LEU TYR PRO
SEQRES 7 B 548 GLY PHE GLU GLY THR GLU MET TRP ASN PRO ASN ARG GLU
SEQRES 8 B 548 LEU SER GLU ASP CYS LEU TYR LEU ASN VAL TRP THR PRO
SEQRES 9 B 548 TYR PRO ARG PRO ALA SER PRO THR PRO VAL LEU ILE TRP
SEQRES 10 B 548 ILE TYR GLY GLY GLY PHE TYR SER GLY ALA ALA SER LEU
SEQRES 11 B 548 ASP VAL TYR ASP GLY ARG PHE LEU ALA GLN VAL GLU GLY
SEQRES 12 B 548 ALA VAL LEU VAL SER MET ASN TYR ARG VAL GLY THR PHE
SEQRES 13 B 548 GLY PHE LEU ALA LEU PRO GLY SER ARG GLU ALA PRO GLY
SEQRES 14 B 548 ASN VAL GLY LEU LEU ASP GLN ARG LEU ALA LEU GLN TRP
SEQRES 15 B 548 VAL GLN GLU ASN ILE ALA ALA PHE GLY GLY ASP PRO MET
SEQRES 16 B 548 SER VAL THR LEU PHE GLY GLU SER ALA GLY ALA ALA SER
SEQRES 17 B 548 VAL GLY MET HIS ILE LEU SER LEU PRO SER ARG SER LEU
SEQRES 18 B 548 PHE HIS ARG ALA VAL LEU GLN SER GLY THR PRO ASN GLY
SEQRES 19 B 548 PRO TRP ALA THR VAL SER ALA GLY GLU ALA ARG ARG ARG
SEQRES 20 B 548 ALA THR LEU LEU ALA ARG LEU VAL GLY CYS PRO PRO GLY
SEQRES 21 B 548 GLY ALA GLY GLY ASN ASP THR GLU LEU ILE ALA CYS LEU
SEQRES 22 B 548 ARG THR ARG PRO ALA GLN ASP LEU VAL ASP HIS GLU TRP
SEQRES 23 B 548 HIS VAL LEU PRO GLN GLU SER ILE PHE ARG PHE SER PHE
SEQRES 24 B 548 VAL PRO VAL VAL ASP GLY ASP PHE LEU SER ASP THR PRO
SEQRES 25 B 548 GLU ALA LEU ILE ASN THR GLY ASP PHE GLN ASP LEU GLN
SEQRES 26 B 548 VAL LEU VAL GLY VAL VAL LYS ASP GLU GLY SER TYR PHE
SEQRES 27 B 548 LEU VAL TYR GLY VAL PRO GLY PHE SER LYS ASP ASN GLU
SEQRES 28 B 548 SER LEU ILE SER ARG ALA GLN PHE LEU ALA GLY VAL ARG
SEQRES 29 B 548 ILE GLY VAL PRO GLN ALA SER ASP LEU ALA ALA GLU ALA
SEQRES 30 B 548 VAL VAL LEU HIS TYR THR ASP TRP LEU HIS PRO GLU ASP
SEQRES 31 B 548 PRO THR HIS LEU ARG ASP ALA MET SER ALA VAL VAL GLY
SEQRES 32 B 548 ASP HIS ASN VAL VAL CYS PRO VAL ALA GLN LEU ALA GLY
SEQRES 33 B 548 ARG LEU ALA ALA GLN GLY ALA ARG VAL TYR ALA TYR ILE
SEQRES 34 B 548 PHE GLU HIS ARG ALA SER THR LEU THR TRP PRO LEU TRP
SEQRES 35 B 548 MET GLY VAL PRO HIS GLY TYR GLU ILE GLU PHE ILE PHE
SEQRES 36 B 548 GLY LEU PRO LEU ASP PRO SER LEU ASN TYR THR THR GLU
SEQRES 37 B 548 GLU ARG ILE PHE ALA GLN ARG LEU MET LYS TYR TRP THR
SEQRES 38 B 548 ASN PHE ALA ARG THR GLY ASP PRO ASN ASP PRO ARG ASP
SEQRES 39 B 548 SER LYS SER PRO GLN TRP PRO PRO TYR THR THR ALA ALA
SEQRES 40 B 548 GLN GLN TYR VAL SER LEU ASN LEU LYS PRO LEU GLU VAL
SEQRES 41 B 548 ARG ARG GLY LEU ARG ALA GLN THR CYS ALA PHE TRP ASN
SEQRES 42 B 548 ARG PHE LEU PRO LYS LEU LEU SER ALA THR ALA THR GLU
SEQRES 43 B 548 ALA PRO
HET C56 A1542 18
HET C57 A1543 18
HET PEG A1544 7
HET PEG A1545 7
HET PEG A1546 7
HET C56 B1544 19
HET C57 B1545 19
HET PEG B1546 7
HET PE4 B1547 23
HET PEG B1548 7
HETNAM C56 4-(DIMETHYLAMINO)-N-{[(2R)-1-ETHYLPYRROLIDIN-
HETNAM 2 C56 2-YL]METHYL}-2-METHOXY-5-NITROBENZAMIDE
HETNAM C57 4-(DIMETHYLAMINO)-N-{[(2S)-1-ETHYLPYRROLIDIN-
HETNAM 2 C57 2-YL]METHYL}-2-METHOXY-5-NITROBENZAMIDE
HETNAM PEG DI(HYDROXYETHYL)ETHER
HETNAM PE4 2-{2-[2-(2-{2-[2-(2-ETHOXY-ETHOXY)-ETHOXY]-
HETNAM 2 PE4 ETHOXY}-ETHOXY)-ETHOXY]-ETHOXY}-ETHANOL
HETSYN PE4 POLYETHYLENE GLYCOL PEG4000
FORMUL 3 C56 2(C17 H26 N4 O4)
FORMUL 4 C57 2(C17 H26 N4 O4)
FORMUL 5 PEG 5(C4 H10 O3)
FORMUL 6 PE4 C16 H34 O8
FORMUL 7 HOH *871(H2 O)
HELIX 1 1 ASP A 5 GLN A 7 5 3
HELIX 2 2 VAL A 42 ARG A 46 5 5
HELIX 3 3 PHE A 80 MET A 85 1 6
HELIX 4 4 LEU A 130 ASP A 134 5 5
HELIX 5 5 GLY A 135 GLY A 143 1 9
HELIX 6 6 VAL A 153 LEU A 159 1 7
HELIX 7 7 ASN A 170 ILE A 187 1 18
HELIX 8 8 ALA A 188 PHE A 190 5 3
HELIX 9 9 SER A 203 LEU A 214 1 12
HELIX 10 10 SER A 215 SER A 220 1 6
HELIX 11 11 SER A 240 VAL A 255 1 16
HELIX 12 12 ASN A 265 ARG A 274 1 10
HELIX 13 13 PRO A 277 GLU A 285 1 9
HELIX 14 14 TRP A 286 LEU A 289 5 4
HELIX 15 15 THR A 311 GLY A 319 1 9
HELIX 16 16 GLY A 335 VAL A 340 1 6
HELIX 17 17 SER A 355 VAL A 367 1 13
HELIX 18 18 SER A 371 THR A 383 1 13
HELIX 19 19 ASP A 390 VAL A 407 1 18
HELIX 20 20 VAL A 407 GLN A 421 1 15
HELIX 21 21 PRO A 440 GLY A 444 5 5
HELIX 22 22 GLU A 450 PHE A 455 1 6
HELIX 23 23 GLY A 456 ASP A 460 5 5
HELIX 24 24 ASP A 460 ASN A 464 5 5
HELIX 25 25 THR A 466 GLY A 487 1 22
HELIX 26 26 ARG A 525 ARG A 534 1 10
HELIX 27 27 ARG A 534 LEU A 539 1 6
HELIX 28 28 ASP B 5 GLN B 7 5 3
HELIX 29 29 VAL B 42 ARG B 46 5 5
HELIX 30 30 PHE B 80 MET B 85 1 6
HELIX 31 31 LEU B 130 ASP B 134 5 5
HELIX 32 32 GLY B 135 GLY B 143 1 9
HELIX 33 33 VAL B 153 LEU B 159 1 7
HELIX 34 34 ASN B 170 ILE B 187 1 18
HELIX 35 35 ALA B 188 PHE B 190 5 3
HELIX 36 36 SER B 203 LEU B 214 1 12
HELIX 37 37 SER B 215 PHE B 222 5 8
HELIX 38 38 ALA B 241 VAL B 255 1 15
HELIX 39 39 ASN B 265 THR B 275 1 11
HELIX 40 40 PRO B 277 TRP B 286 1 10
HELIX 41 41 HIS B 287 LEU B 289 5 3
HELIX 42 42 THR B 311 GLY B 319 1 9
HELIX 43 43 GLY B 335 VAL B 340 1 6
HELIX 44 44 SER B 355 VAL B 367 1 13
HELIX 45 45 SER B 371 THR B 383 1 13
HELIX 46 46 ASP B 390 VAL B 407 1 18
HELIX 47 47 VAL B 407 GLN B 421 1 15
HELIX 48 48 PRO B 440 GLY B 444 5 5
HELIX 49 49 GLU B 450 PHE B 455 1 6
HELIX 50 50 GLY B 456 ASP B 460 5 5
HELIX 51 51 ASP B 460 ASN B 464 5 5
HELIX 52 52 THR B 466 GLY B 487 1 22
HELIX 53 53 ARG B 525 ARG B 534 1 10
HELIX 54 54 ARG B 534 SER B 541 1 8
SHEET 1 AA 3 LEU A 9 VAL A 12 0
SHEET 2 AA 3 GLY A 15 ARG A 18 -1 O GLY A 15 N VAL A 12
SHEET 3 AA 3 VAL A 59 ASP A 61 1 O LEU A 60 N ARG A 18
SHEET 1 AB11 ILE A 20 ALA A 24 0
SHEET 2 AB11 GLY A 27 PRO A 36 -1 O GLY A 27 N ALA A 24
SHEET 3 AB11 TYR A 98 PRO A 104 -1 O LEU A 99 N ILE A 35
SHEET 4 AB11 VAL A 145 MET A 149 -1 O LEU A 146 N TRP A 102
SHEET 5 AB11 THR A 112 ILE A 118 1 O PRO A 113 N VAL A 145
SHEET 6 AB11 GLY A 192 GLU A 202 1 N ASP A 193 O THR A 112
SHEET 7 AB11 ARG A 224 GLN A 228 1 O ARG A 224 N LEU A 199
SHEET 8 AB11 GLN A 325 VAL A 331 1 O GLN A 325 N ALA A 225
SHEET 9 AB11 ARG A 424 PHE A 430 1 O ARG A 424 N VAL A 326
SHEET 10 AB11 GLN A 509 LEU A 513 1 O VAL A 511 N ILE A 429
SHEET 11 AB11 GLU A 519 ARG A 522 -1 O GLU A 519 N SER A 512
SHEET 1 AC 2 VAL A 68 CYS A 69 0
SHEET 2 AC 2 LEU A 92 SER A 93 1 N SER A 93 O VAL A 68
SHEET 1 BA 3 LEU B 9 VAL B 12 0
SHEET 2 BA 3 GLY B 15 ARG B 18 -1 O GLY B 15 N VAL B 12
SHEET 3 BA 3 VAL B 59 ASP B 61 1 O LEU B 60 N ARG B 18
SHEET 1 BB11 ILE B 20 ALA B 24 0
SHEET 2 BB11 GLY B 27 PRO B 36 -1 O GLY B 27 N ALA B 24
SHEET 3 BB11 TYR B 98 PRO B 104 -1 O LEU B 99 N ILE B 35
SHEET 4 BB11 VAL B 145 MET B 149 -1 O LEU B 146 N TRP B 102
SHEET 5 BB11 THR B 112 ILE B 118 1 O PRO B 113 N VAL B 145
SHEET 6 BB11 GLY B 192 GLU B 202 1 N ASP B 193 O THR B 112
SHEET 7 BB11 ARG B 224 GLN B 228 1 O ARG B 224 N LEU B 199
SHEET 8 BB11 GLN B 325 VAL B 331 1 O GLN B 325 N ALA B 225
SHEET 9 BB11 ARG B 424 PHE B 430 1 O ARG B 424 N VAL B 326
SHEET 10 BB11 GLN B 509 LEU B 513 1 O VAL B 511 N ILE B 429
SHEET 11 BB11 GLU B 519 ARG B 522 -1 O GLU B 519 N SER B 512
SHEET 1 BC 2 VAL B 68 CYS B 69 0
SHEET 2 BC 2 LEU B 92 SER B 93 1 N SER B 93 O VAL B 68
SHEET 1 BD 2 VAL B 239 SER B 240 0
SHEET 2 BD 2 VAL B 302 VAL B 303 1 N VAL B 303 O VAL B 239
SSBOND 1 CYS A 69 CYS A 96 1555 1555 2.07
SSBOND 2 CYS A 257 CYS A 272 1555 1555 2.09
SSBOND 3 CYS A 409 CYS A 529 1555 1555 2.04
SSBOND 4 CYS B 69 CYS B 96 1555 1555 2.07
SSBOND 5 CYS B 257 CYS B 272 1555 1555 2.08
SSBOND 6 CYS B 409 CYS B 529 1555 1555 2.05
CISPEP 1 TYR A 105 PRO A 106 0 2.92
CISPEP 2 TYR B 105 PRO B 106 0 4.79
CISPEP 3 SER B 497 PRO B 498 0 -4.97
SITE 1 AC1 12 TYR A 72 ASP A 74 TYR A 124 TRP A 286
SITE 2 AC1 12 SER A 293 ILE A 294 PHE A 295 ARG A 296
SITE 3 AC1 12 PHE A 297 TYR A 337 TYR A 341 HOH A2115
SITE 1 AC2 13 TYR A 72 ASP A 74 TYR A 124 TRP A 286
SITE 2 AC2 13 SER A 293 ILE A 294 PHE A 295 ARG A 296
SITE 3 AC2 13 PHE A 297 TYR A 337 TYR A 341 HOH A2115
SITE 4 AC2 13 HOH A2365
SITE 1 AC3 4 HIS A 381 THR A 528 HOH A2398 HOH A2414
SITE 1 AC4 4 VAL A 303 ASP A 304 GLY A 305 SER A 309
SITE 1 AC5 4 ASP A 333 ASP A 396 TRP A 442 HOH A2498
SITE 1 AC6 12 TYR B 72 ASP B 74 TYR B 124 TRP B 286
SITE 2 AC6 12 SER B 293 ILE B 294 PHE B 295 ARG B 296
SITE 3 AC6 12 TYR B 337 PHE B 338 TYR B 341 HOH B2241
SITE 1 AC7 12 TYR B 72 ASP B 74 TYR B 124 TRP B 286
SITE 2 AC7 12 SER B 293 ILE B 294 PHE B 295 ARG B 296
SITE 3 AC7 12 TYR B 337 PHE B 338 TYR B 341 HOH B2241
SITE 1 AC8 2 ASP B 304 SER B 309
SITE 1 AC9 12 LEU A 380 HIS A 381 GLN A 527 PHE A 531
SITE 2 AC9 12 PHE A 535 HOH A2396 HOH A2397 ALA B 377
SITE 3 AC9 12 LEU B 380 HIS B 381 GLN B 527 PHE B 535
SITE 1 BC1 4 GLN A 527 TYR B 382 HOH B2363 HOH B2364
CRYST1 78.923 111.828 226.999 90.00 90.00 90.00 P 21 21 21 8
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 0.012671 0.000000 0.000000 0.00000
SCALE2 0.000000 0.008942 0.000000 0.00000
SCALE3 0.000000 0.000000 0.004405 0.00000
TER 4204 ALA A 542
TER 8380 ALA B 544
MASTER 495 0 10 54 34 0 21 6 9381 2 144 86
END |