longtext: 2WU4-pdb

content
HEADER    HYDROLASE                               28-SEP-09   2WU4
TITLE     CRYSTAL STRUCTURE OF MOUSE ACETYLCHOLINESTERASE IN COMPLEX
TITLE    2 WITH FENAMIPHOS AND ORTHO-7
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: ACETYLCHOLINESTERASE;
COMPND   3 CHAIN: A, B;
COMPND   4 FRAGMENT: CATALYTIC DOMAIN, RESIDUES 32-574;
COMPND   5 EC: 3.1.1.7;
COMPND   6 ENGINEERED: YES;
COMPND   7 OTHER_DETAILS: FENAMIPHOS COVALENTLY BOUND TO SER203
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: MUS MUSCULUS;
SOURCE   3 ORGANISM_COMMON: MOUSE;
SOURCE   4 ORGANISM_TAXID: 10090;
SOURCE   5 EXPRESSION_SYSTEM: HOMO SAPIENS;
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 9606;
SOURCE   7 EXPRESSION_SYSTEM_CELL_LINE: HEK293F;
SOURCE   8 EXPRESSION_SYSTEM_VECTOR: PCDNA3.1
KEYWDS    GLYCOPROTEIN, SERINE ESTERASE, ACETYLCHOLINESTERASE,
KEYWDS   2 ALTERNATIVE SPLICING, NEUROTRANSMITTER DEGRADATION,
KEYWDS   3 SYNAPSE, MEMBRANE, HYDROLASE, FENAMIPHOS
EXPDTA    X-RAY DIFFRACTION
AUTHOR    A.HORNBERG,E.ARTURSSON,R.WARME,Y.-P.PANG,F.EKSTROM
REVDAT   1   20-OCT-09 2WU4    0
JRNL        AUTH   A.HORNBERG,E.ARTURSSON,R.WARME,Y.-P.PANG,F.EKSTROM
JRNL        TITL   CRYSTAL STRUCTURES OF OXIME-BOUND FENAMIPHOS-
JRNL        TITL 2 ACETYLCHOLINESTERASES: REACTIVATION INVOLVING
JRNL        TITL 3 FLIPPING OF THE HIS447 RING TO FORM A REACTIVE
JRNL        TITL 4 GLU334-HIS447-OXIME TRIAD.
JRNL        REF    BIOCHEM.PHARM.                             2009
JRNL        REFN                   ESSN 1873-2968
JRNL        PMID   19732756
JRNL        DOI    10.1016/J.BCP.2009.08.027
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-
REMARK   3               : KUNSTLEVE,LI-WEI HUNG,ROBERT IMMORMINO,
REMARK   3               : TOM IOERGER,AIRLIE MCCOY,ERIK MCKEE,NIGEL
REMARK   3               : MORIARTY,REETAL PAI,RANDY READ,JANE
REMARK   3               : RICHARDSON,DAVID RICHARDSON,TOD ROMO,JIM
REMARK   3               : SACCHETTINI,NICHOLAS SAUTER,JACOB SMITH,
REMARK   3               : LAURENT STORONI,TOM TERWILLIGER,PETER
REMARK   3               : 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) : 29.146
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.35
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.94
REMARK   3   NUMBER OF REFLECTIONS             : 80602
REMARK   3
REMARK   3  FIT TO DATA USED IN REFINEMENT.
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.1866
REMARK   3   R VALUE            (WORKING SET) : 0.1859
REMARK   3   FREE R VALUE                     : 0.2232
REMARK   3   FREE R VALUE TEST SET SIZE   (%) :  2.0
REMARK   3   FREE R VALUE TEST SET COUNT      : 1595
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 29.1477 -  5.3277    0.99     7486   149  0.1839 0.2191
REMARK   3     2  5.3277 -  4.2329    1.00     7312   144  0.1388 0.1623
REMARK   3     3  4.2329 -  3.6991    1.00     7218   141  0.1552 0.1785
REMARK   3     4  3.6991 -  3.3614    1.00     7180   138  0.1744 0.2247
REMARK   3     5  3.3614 -  3.1208    1.00     7169   145  0.1868 0.2147
REMARK   3     6  3.1208 -  2.9370    1.00     7106   156  0.1859 0.2303
REMARK   3     7  2.9370 -  2.7900    1.00     7132   143  0.1887 0.2372
REMARK   3     8  2.7900 -  2.6686    1.00     7113   145  0.1896 0.2365
REMARK   3     9  2.6686 -  2.5660    1.00     7078   163  0.2045 0.2107
REMARK   3    10  2.5660 -  2.4775    1.00     7105   138  0.2269 0.3044
REMARK   3    11  2.4775 -  2.4000    1.00     7108   133  0.2735 0.3393
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              : 0.364
REMARK   3   B_SOL              : 66.695
REMARK   3
REMARK   3  ERROR ESTIMATES.
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.35
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 20.23
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : 50.39
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 51.59
REMARK   3   OVERALL ANISOTROPIC B VALUE.
REMARK   3    B11 (A**2) : -0.4565
REMARK   3    B22 (A**2) : -0.1888
REMARK   3    B33 (A**2) : 0.6453
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      :  0.012           8631
REMARK   3   ANGLE     :  1.395          11775
REMARK   3   CHIRALITY :  0.089           1258
REMARK   3   PLANARITY :  0.007           1547
REMARK   3   DIHEDRAL  : 18.649           3058
REMARK   3
REMARK   3  TLS DETAILS
REMARK   3   NUMBER OF TLS GROUPS  : 2
REMARK   3   TLS GROUP : 1
REMARK   3    SELECTION: CHAIN A
REMARK   3    ORIGIN FOR THE GROUP (A):  28.1707  12.7397  16.6323
REMARK   3    T TENSOR
REMARK   3      T11:   0.2266 T22:   0.1890
REMARK   3      T33:   0.2614 T12:   0.0039
REMARK   3      T13:   0.0112 T23:   0.0229
REMARK   3    L TENSOR
REMARK   3      L11:   0.8141 L22:   0.6818
REMARK   3      L33:   1.6728 L12:  -0.0913
REMARK   3      L13:   0.1756 L23:  -0.2661
REMARK   3    S TENSOR
REMARK   3      S11:  -0.0808 S12:   0.0047 S13:  -0.0022
REMARK   3      S21:  -0.0120 S22:   0.0271 S23:   0.0014
REMARK   3      S31:   0.1600 S32:  -0.0102 S33:   0.0506
REMARK   3   TLS GROUP : 2
REMARK   3    SELECTION: CHAIN B
REMARK   3    ORIGIN FOR THE GROUP (A):   7.8848   4.2385 -40.4488
REMARK   3    T TENSOR
REMARK   3      T11:   0.2775 T22:   0.2856
REMARK   3      T33:   0.3021 T12:  -0.0199
REMARK   3      T13:  -0.0262 T23:  -0.0744
REMARK   3    L TENSOR
REMARK   3      L11:   0.6684 L22:   0.9373
REMARK   3      L33:   1.8831 L12:  -0.0243
REMARK   3      L13:   0.2334 L23:   0.5108
REMARK   3    S TENSOR
REMARK   3      S11:   0.1435 S12:   0.0767 S13:  -0.0462
REMARK   3      S21:   0.1425 S22:  -0.1347 S23:   0.1078
REMARK   3      S31:   0.1986 S32:   0.0107 S33:  -0.0029
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 2WU4 COMPLIES WITH FORMAT V. 3.20, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 28-SEP-09
REMARK 100 THE PDBE ID CODE IS EBI-41274
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 21-FEB-07
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) : 1.04123
REMARK 200  MONOCHROMATOR                  : NULL
REMARK 200  OPTICS                         : NULL
REMARK 200
REMARK 200  DETECTOR TYPE                  : CCD (MX-225)
REMARK 200  DETECTOR MANUFACTURER          : RAYONIX
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200  DATA SCALING SOFTWARE          : SCALA
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 80714
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.40
REMARK 200  RESOLUTION RANGE LOW       (A) : 29.22
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.0
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.9
REMARK 200  DATA REDUNDANCY                : 7.4
REMARK 200  R MERGE                    (I) : 0.06
REMARK 200  R SYM                      (I) : NULL
REMARK 200   FOR THE DATA SET  : NULL
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     (%) : 100.0
REMARK 200  DATA REDUNDANCY IN SHELL       : 7.4
REMARK 200  R MERGE FOR SHELL          (I) : 0.40
REMARK 200  R SYM FOR SHELL            (I) : NULL
REMARK 200   FOR SHELL         : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: CCP4
REMARK 200 STARTING MODEL: PDB ENTRY 1J06
REMARK 200
REMARK 200 REMARK: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 70
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.8
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 28% PEG750MME, 0.1M HEPES PH7.0
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       39.87000
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000      113.34500
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       56.35000
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000      113.34500
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       39.87000
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       56.35000
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
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 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 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
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 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS:  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     ARG A   493
REMARK 465     ASP A   494
REMARK 465     SER A   495
REMARK 465     LYS A   496
REMARK 465     SER A   497
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     ARG B   493
REMARK 465     ASP B   494
REMARK 465     SER B   495
REMARK 465     LYS B   496
REMARK 465     SER B   497
REMARK 465     LEU B   540
REMARK 465     SER B   541
REMARK 465     ALA B   542
REMARK 465     THR B   543
REMARK 465     ALA B   544
REMARK 465     THR B   545
REMARK 465     GLU B   546
REMARK 465     ALA B   547
REMARK 465     PRO B   548
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3
REMARK 500    PRO A 458   C   -  N   -  CA  ANGL. DEV. =  -9.2 DEGREES
REMARK 500    PRO B 108   C   -  N   -  CA  ANGL. DEV. =  10.0 DEGREES
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       -8.07     72.69
REMARK 500    PRO A  49      150.05    -45.37
REMARK 500    ALA A  62       51.78   -119.30
REMARK 500    ASN A  67      150.43    -46.68
REMARK 500    PHE A 158       -7.11   -141.83
REMARK 500    ALA A 167       69.19   -153.20
REMARK 500    PRO A 290      124.24    -39.52
REMARK 500    ILE A 294       31.35    -77.09
REMARK 500    ASP A 306      -90.13   -129.99
REMARK 500    TYR A 341       53.43    -98.12
REMARK 500    SER A 371     -178.90    -66.18
REMARK 500    VAL A 407      -60.62   -129.09
REMARK 500    PHE B  47       -3.54     73.62
REMARK 500    ALA B  62       55.85   -119.25
REMARK 500    SER B  93      142.34   -176.02
REMARK 500    CYS B  96       10.75   -144.12
REMARK 500    PRO B 108      140.07    -21.78
REMARK 500    ALA B 127      144.85   -174.55
REMARK 500    ALA B 167       66.36   -150.25
REMARK 500    SER B 293     -143.37   -124.91
REMARK 500    ASP B 306      -82.00   -115.80
REMARK 500    TYR B 341       57.90   -101.32
REMARK 500    VAL B 407      -64.31   -123.16
REMARK 500    ASN B 514     -167.58   -166.08
REMARK 500    LEU B 518      127.68    -39.09
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 600
REMARK 600 HETEROGEN
REMARK 600 O-{(S)-ETHOXY[(1-METHYLETHYL)AMINO] PHOSPHORYL}-L-SERINE
REMARK 600  (SXE): MODIFIED SER203
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HBP A1544
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HBP B1545
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE P6G A1545
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A1543
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2JGH   RELATED DB: PDB
REMARK 900  CRYSTAL STRUCTURE OF MOUSE ACETYLCHOLINESTERASE
REMARK 900   INHIBITED BY NON-AGED VX
REMARK 900 RELATED ID: 2WHQ   RELATED DB: PDB
REMARK 900  CRYSTAL STRUCTURE OF ACETYLCHOLINESTERASE,
REMARK 900  PHOSPHONYLATED BY SARIN (AGED) IN COMPLEX
REMARK 900  WITH HI-6
REMARK 900 RELATED ID: 1MAH   RELATED DB: PDB
REMARK 900  FASCICULIN2 - MOUSE ACETYLCHOLINESTERASE COMPLEX
REMARK 900 RELATED ID: 2HA6   RELATED DB: PDB
REMARK 900  CRYSTAL STRUCTURE OF MUTANT S203A OF
REMARK 900  MOUSEACETYLCHOLINESTERASE COMPLEXED WITH
REMARK 900  SUCCINYLCHOLINE
REMARK 900 RELATED ID: 1MAA   RELATED DB: PDB
REMARK 900  MOUSE ACETYLCHOLINESTERASE CATALYTIC DOMAIN,
REMARK 900  GLYCOSYLATEDPROTEIN
REMARK 900 RELATED ID: 2C0Q   RELATED DB: PDB
REMARK 900  NON-AGED FORM OF MOUSE ACETYLCHOLINESTERASE
REMARK 900  INHIBITED BY TABUN
REMARK 900 RELATED ID: 2JGG   RELATED DB: PDB
REMARK 900  CRYSTAL STRUCTURE OF MOUSE ACETYLCHOLINESTERASE
REMARK 900   INHIBITED BY NON-AGED SARIN
REMARK 900 RELATED ID: 2JGL   RELATED DB: PDB
REMARK 900  CRYSTAL STRUCTURE OF MOUSE ACETYLCHOLINESTERASE
REMARK 900   INHIBITED BY AGED VX AND SARIN
REMARK 900 RELATED ID: 1Q84   RELATED DB: PDB
REMARK 900  CRYSTAL STRUCTURE OF THE MOUSE
REMARK 900  ACETYLCHOLINESTERASE-TZ2PA6ANTI COMPLEX
REMARK 900 RELATED ID: 2JGM   RELATED DB: PDB
REMARK 900  CRYSTAL STRUCTURE OF MOUSE ACETYLCHOLINESTERASE
REMARK 900   INHIBITED BY AGED DIISOPROPYL FLUOROPHOSPHATE
REMARK 900   (DFP)
REMARK 900 RELATED ID: 2JGE   RELATED DB: PDB
REMARK 900  CRYSTAL STRUCTURE OF MOUSE ACETYLCHOLINESTERASE
REMARK 900   INHIBITED BY NON-AGED METHAMIDOPHOS
REMARK 900 RELATED ID: 1Q83   RELATED DB: PDB
REMARK 900  CRYSTAL STRUCTURE OF THE MOUSE
REMARK 900  ACETYLCHOLINESTERASE-TZ2PA6SYN COMPLEX
REMARK 900 RELATED ID: 2WLS   RELATED DB: PDB
REMARK 900  CRYSTAL STRUCTURE OF MUS MUSCULUS
REMARK 900  ACETYLCHOLINESTERASE IN COMPLEX WITH AMTS13
REMARK 900 RELATED ID: 1C2B   RELATED DB: PDB
REMARK 900  ELECTROPHORUS ELECTRICUS ACETYLCHOLINESTERASE
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: 2JEY   RELATED DB: PDB
REMARK 900  MUS MUSCULUS ACETYLCHOLINESTERASE IN COMPLEX
REMARK 900  WITH HLO-7
REMARK 900 RELATED ID: 2JGI   RELATED DB: PDB
REMARK 900  CRYSTAL STRUCTURE OF MOUSE ACETYLCHOLINESTERASE
REMARK 900   INHIBITED BY NON-AGED DIISOPROPYL
REMARK 900  FLUOROPHOSPHATE (DFP)
REMARK 900 RELATED ID: 1N5R   RELATED DB: PDB
REMARK 900  CRYSTAL STRUCTURE OF THE MOUSE
REMARK 900  ACETYLCHOLINESTERASE-PROPIDIUM COMPLEX
REMARK 900 RELATED ID: 2JGJ   RELATED DB: PDB
REMARK 900  CRYSTAL STRUCTURE OF MOUSE ACETYLCHOLINESTERASE
REMARK 900   INHIBITED BY AGED METHAMIDOPHOS
REMARK 900 RELATED ID: 1J06   RELATED DB: PDB
REMARK 900  CRYSTAL STRUCTURE OF MOUSE ACETYLCHOLINESTERASE
REMARK 900   IN THE APOFORM
REMARK 900 RELATED ID: 2JF0   RELATED DB: PDB
REMARK 900  MUS MUSCULUS ACETYLCHOLINESTERASE IN COMPLEX
REMARK 900  WITH TABUN AND ORTHO-7
REMARK 900 RELATED ID: 2C0P   RELATED DB: PDB
REMARK 900  AGED FORM OF MOUSE ACETYLCHOLINESTERASE
REMARK 900  INHIBITED BY TABUN
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
REMARK 900  COMPLEX WITH K027
REMARK 900 RELATED ID: 1N5M   RELATED DB: PDB
REMARK 900  CRYSTAL STRUCTURE OF THE MOUSE
REMARK 900  ACETYLCHOLINESTERASE-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: 2WHP   RELATED DB: PDB
REMARK 900  CRYSTAL STRUCTURE OF ACETYLCHOLINESTERASE,
REMARK 900  PHOSPHONYLATED BY SARIN AND IN COMPLEX WITH
REMARK 900   HI-6
REMARK 900 RELATED ID: 2JEZ   RELATED DB: PDB
REMARK 900  MUS MUSCULUS ACETYLCHOLINESTERASE IN COMPLEX
REMARK 900  WITH TABUN AND HLO-7
REMARK 900 RELATED ID: 2JGK   RELATED DB: PDB
REMARK 900  CRYSTAL STRUCTURE OF MOUSE ACETYLCHOLINESTERASE
REMARK 900   INHIBITED 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
REMARK 900  ACETYLCHOLINE
REMARK 900 RELATED ID: 1J07   RELATED DB: PDB
REMARK 900  CRYSTAL STRUCTURE OF THE MOUSE
REMARK 900  ACETYLCHOLINESTERASE-DECIDIUM COMPLEX
REMARK 900 RELATED ID: 2JGF   RELATED DB: PDB
REMARK 900  CRYSTAL STRUCTURE OF MOUSE ACETYLCHOLINESTERASE
REMARK 900   INHIBITED BY NON-AGED FENAMIPHOS
REMARK 900 RELATED ID: 2HA7   RELATED DB: PDB
REMARK 900  CRYSTAL STRUCTURE OF MUTANT S203A OF
REMARK 900  MOUSEACETYLCHOLINESTERASE COMPLEXED WITH
REMARK 900  BUTYRYLTHIOCHOLINE
REMARK 900 RELATED ID: 1C2O   RELATED DB: PDB
REMARK 900  ELECTROPHORUS ELECTRICUS ACETYLCHOLINESTERASE
REMARK 900 RELATED ID: 2WU3   RELATED DB: PDB
REMARK 900  CRYSTAL STRUCTURE OF MOUSE ACETYLCHOLINESTERASE
REMARK 900   IN COMPLEX WITH FENAMIPHOS AND HI-6
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 STRUCTURE STARTS AT RESIDUE 32 AND ENDS AT RESIDUE 574
DBREF  2WU4 A    1   543  UNP    P21836   ACES_MOUSE      32    574
DBREF  2WU4 A  544   548  PDB    2WU4     2WU4           544    548
DBREF  2WU4 B    1   543  UNP    P21836   ACES_MOUSE      32    574
DBREF  2WU4 B  544   548  PDB    2WU4     2WU4           544    548
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 SXE 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 SXE 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
MODRES 2WU4 SXE A  203  SER  MODIFIED SERINE
MODRES 2WU4 SXE B  203  SER  MODIFIED SERINE
HET    SXE  A 203      30
HET    SXE  B 203      20
HET    HBP  A1544      25
HET    HBP  B1545      25
HET    P6G  A1545      19
HET    NAG  A1543      14
HETNAM     P6G HEXAETHYLENE GLYCOL
HETNAM     HBP 1,7-HEPTYLENE-BIS-N,N'-SYN-2-
HETNAM   2 HBP  PYRIDINIUMALDOXIME
HETNAM     SXE O-{(S)-ETHOXY[(1-METHYLETHYL)AMINO]
HETNAM   2 SXE  PHOSPHORYL}-L-SERINE
HETNAM     NAG N-ACETYL-D-GLUCOSAMINE
HETSYN     P6G POLYETHYLENE GLYCOL PEG400
HETSYN     NAG NAG
FORMUL   3  P6G    C12 H26 O7
FORMUL   4  HBP    2(C19 H26 N4 O2 2+)
FORMUL   5  SXE    2(C8 H19 N2 O5 P)
FORMUL   6  NAG    C8 H15 N O6
FORMUL   7  HOH   *325(H2 O)
HELIX    1   1 ASP A    5  LEU A    9  5                                   5
HELIX    2   2 THR A   83  ASN A   87  5                                   5
HELIX    3   3 LEU A  130  ASP A  134  5                                   5
HELIX    4   4 ARG A  136  GLU A  142  1                                   7
HELIX    5   5 LEU A  173  ILE A  187  1                                  15
HELIX    6   6 ALA A  188  PHE A  190  5                                   3
HELIX    7   7 SER A  215  SER A  220  1                                   6
HELIX    8   8 GLU A  243  VAL A  255  1                                  13
HELIX    9   9 ASN A  265  THR A  275  1                                  11
HELIX   10  10 PRO A  277  TRP A  286  1                                  10
HELIX   11  11 HIS A  287  LEU A  289  5                                   3
HELIX   12  12 THR A  311  THR A  318  1                                   8
HELIX   13  13 SER A  336  TYR A  341  5                                   6
HELIX   14  14 SER A  355  ALA A  361  1                                   7
HELIX   15  15 SER A  371  THR A  383  1                                  13
HELIX   16  16 ASP A  390  VAL A  402  1                                  13
HELIX   17  17 VAL A  407  ALA A  415  1                                   9
HELIX   18  18 GLU A  450  PHE A  455  1                                   6
HELIX   19  19 ASP A  460  ASN A  464  5                                   5
HELIX   20  20 THR A  466  THR A  486  1                                  21
HELIX   21  21 ARG A  525  ARG A  534  1                                  10
HELIX   22  22 ARG A  534  ALA A  542  1                                   9
HELIX   23  23 ASP B    5  LEU B    9  5                                   5
HELIX   24  24 THR B   83  ASN B   87  5                                   5
HELIX   25  25 LEU B  130  ASP B  134  5                                   5
HELIX   26  26 ARG B  136  GLU B  142  1                                   7
HELIX   27  27 LEU B  173  ILE B  187  1                                  15
HELIX   28  28 ALA B  188  PHE B  190  5                                   3
HELIX   29  29 SER B  215  SER B  220  1                                   6
HELIX   30  30 GLU B  243  VAL B  255  1                                  13
HELIX   31  31 ASN B  265  THR B  275  1                                  11
HELIX   32  32 PRO B  277  TRP B  286  1                                  10
HELIX   33  33 HIS B  287  LEU B  289  5                                   3
HELIX   34  34 THR B  311  THR B  318  1                                   8
HELIX   35  35 SER B  355  ALA B  361  1                                   7
HELIX   36  36 SER B  371  THR B  383  1                                  13
HELIX   37  37 ASP B  390  VAL B  402  1                                  13
HELIX   38  38 VAL B  407  ALA B  415  1                                   9
HELIX   39  39 GLU B  450  PHE B  455  1                                   6
HELIX   40  40 ASP B  460  ASN B  464  5                                   5
HELIX   41  41 THR B  466  THR B  486  1                                  21
HELIX   42  42 ARG B  525  ARG B  534  1                                  10
HELIX   43  43 ARG B  534  LEU B  539  1                                   6
SHEET    1  AA 2 LEU A  17  ARG A  18  0
SHEET    2  AA 2 LEU A  60  ASP A  61  1  O  LEU A  60   N  ARG A  18
SHEET    1  AB11 ARG A  21  LEU A  22  0
SHEET    2  AB11 VAL A  29  PHE A  32 -1  O  VAL A  29   N  LEU A  22
SHEET    3  AB11 LEU A  99  PRO A 104 -1  O  VAL A 101   N  PHE A  32
SHEET    4  AB11 VAL A 145  MET A 149 -1  O  LEU A 146   N  TRP A 102
SHEET    5  AB11 VAL A 114  TRP A 117  1  O  LEU A 115   N  VAL A 147
SHEET    6  AB11 VAL A 197  PHE A 200  1  O  THR A 198   N  ILE A 116
SHEET    7  AB11 ARG A 224  VAL A 226  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 TYR A 510  LEU A 513  1  O  VAL A 511   N  ILE A 429
SHEET   11  AB11 GLU A 519  ARG A 521 -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  AD 2 VAL A 239  SER A 240  0
SHEET    2  AD 2 VAL A 302  VAL A 303  1  N  VAL A 303   O  VAL A 239
SHEET    1  BA 2 LEU B  17  ARG B  18  0
SHEET    2  BA 2 LEU B  60  ASP B  61  1  O  LEU B  60   N  ARG B  18
SHEET    1  BB11 ARG B  21  LEU B  22  0
SHEET    2  BB11 VAL B  29  PHE B  32 -1  O  VAL B  29   N  LEU B  22
SHEET    3  BB11 LEU B  99  PRO B 104 -1  O  VAL B 101   N  PHE B  32
SHEET    4  BB11 VAL B 145  MET B 149 -1  O  LEU B 146   N  TRP B 102
SHEET    5  BB11 VAL B 114  TRP B 117  1  O  LEU B 115   N  VAL B 147
SHEET    6  BB11 VAL B 197  PHE B 200  1  O  THR B 198   N  ILE B 116
SHEET    7  BB11 ARG B 224  VAL B 226  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 TYR B 510  LEU B 513  1  O  VAL B 511   N  ILE B 429
SHEET   11  BB11 GLU B 519  ARG B 521 -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  2.08
SSBOND   2 CYS A  257    CYS A  272                          1555   1555  2.08
SSBOND   3 CYS A  409    CYS A  529                          1555   1555  2.07
SSBOND   4 CYS B   69    CYS B   96                          1555   1555  2.06
SSBOND   5 CYS B  257    CYS B  272                          1555   1555  2.11
SSBOND   6 CYS B  409    CYS B  529                          1555   1555  2.05
LINK         C   GLU A 202                 N  ASXE A 203     1555   1555  1.34
LINK         C   GLU A 202                 N  BSXE A 203     1555   1555  1.34
LINK         C  ASXE A 203                 N   ALA A 204     1555   1555  1.34
LINK         C  BSXE A 203                 N   ALA A 204     1555   1555  1.34
LINK         ND2 ASN A 350                 C1  NAG A1543     1555   1555  1.48
LINK         C   GLU B 202                 N  BSXE B 203     1555   1555  1.34
LINK         C   GLU B 202                 N  ASXE B 203     1555   1555  1.34
LINK         C  BSXE B 203                 N   ALA B 204     1555   1555  1.34
LINK         C  ASXE B 203                 N   ALA B 204     1555   1555  1.34
CISPEP   1 TYR A  105    PRO A  106          0        -6.62
CISPEP   2 TYR B  105    PRO B  106          0         2.90
SITE     1 AC1 13 TYR A  72  TRP A  86  TYR A 124  SXE A 203
SITE     2 AC1 13 GLU A 285  TRP A 286  ILE A 294  PHE A 297
SITE     3 AC1 13 TYR A 337  PHE A 338  TYR A 341  HIS A 447
SITE     4 AC1 13 HOH A2140
SITE     1 AC2 10 TYR B  72  TRP B  86  TYR B 124  GLU B 285
SITE     2 AC2 10 TRP B 286  ILE B 294  TYR B 337  PHE B 338
SITE     3 AC2 10 TYR B 341  HIS B 447
SITE     1 AC3  7 LEU A 380  HIS A 381  GLN A 527  PHE A 535
SITE     2 AC3  7 ALA B 377  LEU B 380  HIS B 381
SITE     1 AC4  4 SER A 347  ASN A 350  LEU A 353  HOH A2192
CRYST1   79.740  112.700  226.690  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      0.012541  0.000000  0.000000        0.00000
SCALE2      0.000000  0.008873  0.000000        0.00000
SCALE3      0.000000  0.000000  0.004411        0.00000
END