longtext: 4B0O-pdb

content
HEADER    HYDROLASE                               04-JUL-12   4B0O
TITLE     CRYSTAL STRUCTURE OF SOMAN-AGED HUMAN BUTYRYLCHOLINESTERASE IN
TITLE    2 COMPLEX WITH BENZYL PYRIDINIUM-4-METHYLTRICHLOROACETIMIDATE
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: CHOLINESTERASE;
COMPND   3 CHAIN: A;
COMPND   4 FRAGMENT: RESIDUES 29-557;
COMPND   5 SYNONYM: ACYLCHOLINE ACYLHYDROLASE, BUTYRYLCHOLINE ESTERASE,
COMPND   6  CHOLINE ESTERASE II, PSEUDOCHOLINESTERASE;
COMPND   7 EC: 3.1.1.8;
COMPND   8 ENGINEERED: YES
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE   3 ORGANISM_COMMON: HUMAN;
SOURCE   4 ORGANISM_TAXID: 9606;
SOURCE   5 EXPRESSION_SYSTEM: CRICETULUS GRISEUS;
SOURCE   6 EXPRESSION_SYSTEM_COMMON: CHINESE HAMSTER;
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 10029;
SOURCE   8 EXPRESSION_SYSTEM_CELL_LINE: CHO-K1;
SOURCE   9 EXPRESSION_SYSTEM_ORGAN: OVARY;
SOURCE  10 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE  11 EXPRESSION_SYSTEM_PLASMID: PGS
KEYWDS    HYDROLASE, AGING
EXPDTA    X-RAY DIFFRACTION
AUTHOR    M.WANDHAMMER,M.DE KONING,M.VAN GROL,D.NOORT,M.GOELDNER,F.NACHON
REVDAT   1   29-AUG-12 4B0O    0
JRNL        AUTH   M.WANDHAMMER,M.DE KONING,M.VAN GROL,M.LOIODICE,L.SAUREL,
JRNL        AUTH 2 D.NOORT,M.GOELDNER,F.NACHON
JRNL        TITL   A STEP TOWARD THE REACTIVATION OF AGED CHOLINESTERASES -
JRNL        TITL 2 CRYSTAL STRUCTURE OF LIGANDS BINDING TO AGED HUMAN
JRNL        TITL 3 BUTYRYLCHOLINESTERASE
JRNL        REF    CHEM.BIOL.INTERACT                         2012
JRNL        REFN                   ESSN 1872-7786
JRNL        DOI    10.1016/J.CBI.2012.08.005
REMARK   2
REMARK   2 RESOLUTION.    2.36 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : PHENIX (PHENIX.REFINE: 1.7.3_928)
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) : 2.35
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 30.827
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.36
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.64
REMARK   3   NUMBER OF REFLECTIONS             : 32524
REMARK   3
REMARK   3  FIT TO DATA USED IN REFINEMENT.
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.1698
REMARK   3   R VALUE            (WORKING SET) : 0.1685
REMARK   3   FREE R VALUE                     : 0.2044
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 3.5
REMARK   3   FREE R VALUE TEST SET COUNT      : 1138
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 30.8298 -  4.6952    0.96     4000   145  0.1694 0.1756
REMARK   3     2  4.6952 -  3.7288    0.98     3913   142  0.1333 0.1540
REMARK   3     3  3.7288 -  3.2580    0.98     3907   141  0.1579 0.2068
REMARK   3     4  3.2580 -  2.9604    0.99     3917   142  0.1754 0.2271
REMARK   3     5  2.9604 -  2.7483    1.00     3941   143  0.1892 0.2392
REMARK   3     6  2.7483 -  2.5864    1.00     3896   142  0.1976 0.2825
REMARK   3     7  2.5864 -  2.4569    1.00     3918   142  0.2094 0.2513
REMARK   3     8  2.4569 -  2.3500    1.00     3894   141  0.2195 0.2969
REMARK   3
REMARK   3  BULK SOLVENT MODELLING.
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL
REMARK   3   SOLVENT RADIUS     : 1.10
REMARK   3   SHRINKAGE RADIUS   : 0.86
REMARK   3   K_SOL              : 0.342
REMARK   3   B_SOL              : 56.478
REMARK   3
REMARK   3  ERROR ESTIMATES.
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.25
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 20.32
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : 37.48
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL
REMARK   3   OVERALL ANISOTROPIC B VALUE.
REMARK   3    B11 (A**2) : -2.0181
REMARK   3    B22 (A**2) : -2.0181
REMARK   3    B33 (A**2) : 4.0363
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      :  0.007           4586
REMARK   3   ANGLE     :  1.079           6254
REMARK   3   CHIRALITY :  0.077            680
REMARK   3   PLANARITY :  0.005            795
REMARK   3   DIHEDRAL  : 19.448           1712
REMARK   3
REMARK   3  TLS DETAILS
REMARK   3   NUMBER OF TLS GROUPS  : 4
REMARK   3   TLS GROUP : 1
REMARK   3    SELECTION: CHAIN A AND (RESSEQ 3:242)
REMARK   3    ORIGIN FOR THE GROUP (A): -18.1647 -29.3336 -36.4063
REMARK   3    T TENSOR
REMARK   3      T11:   0.1657 T22:   0.0922
REMARK   3      T33:   0.1678 T12:  -0.0984
REMARK   3      T13:  -0.1158 T23:  -0.0463
REMARK   3    L TENSOR
REMARK   3      L11:   2.1967 L22:   2.3228
REMARK   3      L33:   2.8968 L12:   0.0911
REMARK   3      L13:   0.1375 L23:   0.3554
REMARK   3    S TENSOR
REMARK   3      S11:  -0.0381 S12:   0.3484 S13:  -0.0584
REMARK   3      S21:  -0.5255 S22:   0.0954 S23:   0.1014
REMARK   3      S31:   0.0050 S32:  -0.0882 S33:  -0.0046
REMARK   3   TLS GROUP : 2
REMARK   3    SELECTION: CHAIN A AND (RESSEQ 243:322)
REMARK   3    ORIGIN FOR THE GROUP (A):  -4.3056 -40.6940 -31.7023
REMARK   3    T TENSOR
REMARK   3      T11:   0.2951 T22:   0.2458
REMARK   3      T33:   0.3894 T12:   0.0273
REMARK   3      T13:  -0.0231 T23:  -0.0842
REMARK   3    L TENSOR
REMARK   3      L11:   2.1516 L22:   2.6118
REMARK   3      L33:   3.0845 L12:  -0.0633
REMARK   3      L13:  -0.2054 L23:   1.2089
REMARK   3    S TENSOR
REMARK   3      S11:  -0.0904 S12:   0.3000 S13:  -0.5434
REMARK   3      S21:  -0.2252 S22:   0.1973 S23:  -0.2620
REMARK   3      S31:   0.5470 S32:   0.4161 S33:  -0.1383
REMARK   3   TLS GROUP : 3
REMARK   3    SELECTION: CHAIN A AND (RESSEQ 323:402)
REMARK   3    ORIGIN FOR THE GROUP (A): -15.4612 -45.3489  -6.2040
REMARK   3    T TENSOR
REMARK   3      T11:   0.3326 T22:   0.2022
REMARK   3      T33:   0.3074 T12:  -0.0627
REMARK   3      T13:  -0.1146 T23:   0.0264
REMARK   3    L TENSOR
REMARK   3      L11:   6.7603 L22:   4.0038
REMARK   3      L33:   2.9541 L12:   1.7351
REMARK   3      L13:   1.7740 L23:  -1.2520
REMARK   3    S TENSOR
REMARK   3      S11:   0.3308 S12:  -0.6254 S13:  -0.6115
REMARK   3      S21:   0.3080 S22:   0.0164 S23:   0.1399
REMARK   3      S31:   0.5427 S32:  -0.3127 S33:  -0.3022
REMARK   3   TLS GROUP : 4
REMARK   3    SELECTION: CHAIN A AND (RESSEQ 403:1296)
REMARK   3    ORIGIN FOR THE GROUP (A): -20.3681 -28.1070 -17.2882
REMARK   3    T TENSOR
REMARK   3      T11:   0.1011 T22:   0.1243
REMARK   3      T33:   0.2124 T12:  -0.0150
REMARK   3      T13:  -0.0585 T23:  -0.0344
REMARK   3    L TENSOR
REMARK   3      L11:   1.1601 L22:   1.5058
REMARK   3      L33:   1.8960 L12:   0.2813
REMARK   3      L13:   0.2233 L23:   0.2441
REMARK   3    S TENSOR
REMARK   3      S11:  -0.0024 S12:  -0.0394 S13:  -0.0517
REMARK   3      S21:   0.0661 S22:   0.0412 S23:   0.0096
REMARK   3      S31:   0.0219 S32:  -0.1263 S33:   0.0148
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 4B0O COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 03-AUG-12.
REMARK 100 THE PDBE ID CODE IS EBI-53191.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 26-SEP-11
REMARK 200  TEMPERATURE           (KELVIN) : 77
REMARK 200  PH                             : 6.5
REMARK 200  NUMBER OF CRYSTALS USED        : 1
REMARK 200
REMARK 200  SYNCHROTRON              (Y/N) : Y
REMARK 200  RADIATION SOURCE               : ESRF
REMARK 200  BEAMLINE                       : ID23-1
REMARK 200  X-RAY GENERATOR MODEL          : NULL
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.00407
REMARK 200  MONOCHROMATOR                  : NULL
REMARK 200  OPTICS                         : NULL
REMARK 200
REMARK 200  DETECTOR TYPE                  : CCD (QUANTUM 315R)
REMARK 200  DETECTOR MANUFACTURER          : ADSC
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200  DATA SCALING SOFTWARE          : XSALE
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 32534
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.35
REMARK 200  RESOLUTION RANGE LOW       (A) : 48.10
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.0
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.6
REMARK 200  DATA REDUNDANCY                : 5.6
REMARK 200  R MERGE                    (I) : 0.09
REMARK 200  R SYM                      (I) : NULL
REMARK 200   FOR THE DATA SET  : 21.70
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.35
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.45
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.8
REMARK 200  DATA REDUNDANCY IN SHELL       : 5.7
REMARK 200  R MERGE FOR SHELL          (I) : 0.38
REMARK 200  R SYM FOR SHELL            (I) : NULL
REMARK 200   FOR SHELL         : 5.10
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: NULL
REMARK 200 STARTING MODEL: PDB ENTRY 1P0I
REMARK 200
REMARK 200 REMARK: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 61
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.16
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 2.1 M AMMONIUM SULFATE, 0.1 M
REMARK 280  MES BUFFER PH 6.5
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 4 2 2
REMARK 290
REMARK 290      SYMOP   SYMMETRY
REMARK 290     NNNMMM   OPERATOR
REMARK 290       1555   X,Y,Z
REMARK 290       2555   -X,-Y,Z
REMARK 290       3555   -Y,X,Z
REMARK 290       4555   Y,-X,Z
REMARK 290       5555   -X,Y,-Z
REMARK 290       6555   X,-Y,-Z
REMARK 290       7555   Y,X,-Z
REMARK 290       8555   -Y,-X,-Z
REMARK 290       9555   X+1/2,Y+1/2,Z+1/2
REMARK 290      10555   -X+1/2,-Y+1/2,Z+1/2
REMARK 290      11555   -Y+1/2,X+1/2,Z+1/2
REMARK 290      12555   Y+1/2,-X+1/2,Z+1/2
REMARK 290      13555   -X+1/2,Y+1/2,-Z+1/2
REMARK 290      14555   X+1/2,-Y+1/2,-Z+1/2
REMARK 290      15555   Y+1/2,X+1/2,-Z+1/2
REMARK 290      16555   -Y+1/2,-X+1/2,-Z+1/2
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        0.00000
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000        0.00000
REMARK 290   SMTRY1   3  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY2   3  1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000
REMARK 290   SMTRY1   4  0.000000  1.000000  0.000000        0.00000
REMARK 290   SMTRY2   4 -1.000000  0.000000  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        0.00000
REMARK 290   SMTRY1   6  1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000        0.00000
REMARK 290   SMTRY1   7  0.000000  1.000000  0.000000        0.00000
REMARK 290   SMTRY2   7  1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000        0.00000
REMARK 290   SMTRY1   8  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY2   8 -1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000        0.00000
REMARK 290   SMTRY1   9  1.000000  0.000000  0.000000       77.75500
REMARK 290   SMTRY2   9  0.000000  1.000000  0.000000       77.75500
REMARK 290   SMTRY3   9  0.000000  0.000000  1.000000       64.23000
REMARK 290   SMTRY1  10 -1.000000  0.000000  0.000000       77.75500
REMARK 290   SMTRY2  10  0.000000 -1.000000  0.000000       77.75500
REMARK 290   SMTRY3  10  0.000000  0.000000  1.000000       64.23000
REMARK 290   SMTRY1  11  0.000000 -1.000000  0.000000       77.75500
REMARK 290   SMTRY2  11  1.000000  0.000000  0.000000       77.75500
REMARK 290   SMTRY3  11  0.000000  0.000000  1.000000       64.23000
REMARK 290   SMTRY1  12  0.000000  1.000000  0.000000       77.75500
REMARK 290   SMTRY2  12 -1.000000  0.000000  0.000000       77.75500
REMARK 290   SMTRY3  12  0.000000  0.000000  1.000000       64.23000
REMARK 290   SMTRY1  13 -1.000000  0.000000  0.000000       77.75500
REMARK 290   SMTRY2  13  0.000000  1.000000  0.000000       77.75500
REMARK 290   SMTRY3  13  0.000000  0.000000 -1.000000       64.23000
REMARK 290   SMTRY1  14  1.000000  0.000000  0.000000       77.75500
REMARK 290   SMTRY2  14  0.000000 -1.000000  0.000000       77.75500
REMARK 290   SMTRY3  14  0.000000  0.000000 -1.000000       64.23000
REMARK 290   SMTRY1  15  0.000000  1.000000  0.000000       77.75500
REMARK 290   SMTRY2  15  1.000000  0.000000  0.000000       77.75500
REMARK 290   SMTRY3  15  0.000000  0.000000 -1.000000       64.23000
REMARK 290   SMTRY1  16  0.000000 -1.000000  0.000000       77.75500
REMARK 290   SMTRY2  16 -1.000000  0.000000  0.000000       77.75500
REMARK 290   SMTRY3  16  0.000000  0.000000 -1.000000       64.23000
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: OCTAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: OCTAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 48940 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 156390 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -348.9 KCAL/MOL
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   BIOMT1   2  1.000000  0.000000  0.000000        0.00000
REMARK 350   BIOMT2   2  0.000000 -1.000000  0.000000        0.00000
REMARK 350   BIOMT3   2  0.000000  0.000000 -1.000000        0.00000
REMARK 350   BIOMT1   3 -1.000000  0.000000  0.000000        0.00000
REMARK 350   BIOMT2   3  0.000000 -1.000000  0.000000        0.00000
REMARK 350   BIOMT3   3  0.000000  0.000000  1.000000        0.00000
REMARK 350   BIOMT1   4 -1.000000  0.000000  0.000000        0.00000
REMARK 350   BIOMT2   4  0.000000  1.000000  0.000000        0.00000
REMARK 350   BIOMT3   4  0.000000  0.000000 -1.000000        0.00000
REMARK 350   BIOMT1   5  0.000000 -1.000000  0.000000        0.00000
REMARK 350   BIOMT2   5  1.000000  0.000000  0.000000        0.00000
REMARK 350   BIOMT3   5  0.000000  0.000000  1.000000        0.00000
REMARK 350   BIOMT1   6  0.000000  1.000000  0.000000        0.00000
REMARK 350   BIOMT2   6 -1.000000  0.000000  0.000000        0.00000
REMARK 350   BIOMT3   6  0.000000  0.000000  1.000000        0.00000
REMARK 350   BIOMT1   7  0.000000  1.000000  0.000000        0.00000
REMARK 350   BIOMT2   7  1.000000  0.000000  0.000000        0.00000
REMARK 350   BIOMT3   7  0.000000  0.000000 -1.000000        0.00000
REMARK 350   BIOMT1   8  0.000000 -1.000000  0.000000        0.00000
REMARK 350   BIOMT2   8 -1.000000  0.000000  0.000000        0.00000
REMARK 350   BIOMT3   8  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     GLU A     1
REMARK 465     ASP A     2
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     ARG A 138    NE
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE
REMARK 500   O4   NAG A   571     O    HOH A  2285              2.17
REMARK 500   O    HOH A  2056     O    HOH A  2067              2.19
REMARK 500   O    HOH A  2197     O    HOH A  2275              2.18
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE
REMARK 500   O    HOH A  2265     O    HOH A  2269     7555     2.11
REMARK 500
REMARK 500 REMARK: NULL
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  43       -6.45     74.82
REMARK 500    LYS A  51      141.99     94.54
REMARK 500    ASP A  54     -179.22     56.74
REMARK 500    CYS A  92       13.00   -141.41
REMARK 500    ASN A 106       56.54   -158.49
REMARK 500    ALA A 162       73.11   -158.92
REMARK 500    ASP A 297      -81.33   -126.13
REMARK 500    ASP A 324       57.85   -119.91
REMARK 500    ASP A 378      -11.46   -140.58
REMARK 500    PHE A 398      -56.59   -132.64
REMARK 500    PRO A 480       49.79    -82.89
REMARK 500    THR A 496      -78.84    178.11
REMARK 500    GLU A 506      -93.34   -113.97
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GLY A1296
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  CL A1297
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  CL A1298
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  CL A1300
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  CL A1301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  CA A1303
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  CA A1304
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  NA A1305
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  NA A1306
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 15F A1307
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR MONO-SACCHARIDE
REMARK 800   NAG A 540 BOUND TO ASN A  57
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR MONO-SACCHARIDE
REMARK 800   NAG A 550 BOUND TO ASN A 106
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR CHAIN A OF SUGAR BOUND TO
REMARK 800   ASN A 241 RESIDUES  560 TO  562
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR MONO-SACCHARIDE
REMARK 800   NAG A 590 BOUND TO ASN A 256
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR CHAIN A OF SUGAR BOUND TO
REMARK 800   ASN A 341 RESIDUES  570 TO  572
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR MONO-SACCHARIDE
REMARK 800   NAG A 580 BOUND TO ASN A 485
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1EHO   RELATED DB: PDB
REMARK 900  MODEL OF (-)-COCAINE-BOUND BCHE COMPLEX.
REMARK 900 RELATED ID: 1EHQ   RELATED DB: PDB
REMARK 900  MODEL OF (+)-COCAINE-BOUND BCHE COMPLEX
REMARK 900 RELATED ID: 1KCJ   RELATED DB: PDB
REMARK 900  MODEL OF (-)-COCAINE-BOUND (-)-COCAINE HYDROLASE COMPLEX
REMARK 900 RELATED ID: 1P0I   RELATED DB: PDB
REMARK 900  CRYSTAL STRUCTURE OF HUMAN BUTYRYL CHOLINESTERASE
REMARK 900 RELATED ID: 1P0M   RELATED DB: PDB
REMARK 900  CRYSTAL STRUCTURE OF HUMAN BUTYRYL CHOLINESTERASE
REMARK 900  INCOMPLEX WITH A CHOLINE MOLECULE
REMARK 900 RELATED ID: 1P0P   RELATED DB: PDB
REMARK 900  CRYSTAL STRUCTURE OF SOMAN-AGED HUMAN
REMARK 900  BUTYRYLCHOLINESTERASE IN COMPLEX WITH THE SUBSTRATE
REMARK 900  ANALOGBUTYRYLTHIOCHOLINE
REMARK 900 RELATED ID: 1P0Q   RELATED DB: PDB
REMARK 900  CRYSTAL STRUCTURE OF SOMAN-AGED HUMAN BUTYRYL
REMARK 900  CHOLINESTERASE
REMARK 900 RELATED ID: 1XLU   RELATED DB: PDB
REMARK 900  X-RAY STRUCTURE OF DI-ISOPROPYL-PHOSPHORO-FLUORIDATE (
REMARK 900  DFP)INHIBITED BUTYRYLCHOLINESTERASE AFTER AGING
REMARK 900 RELATED ID: 1XLV   RELATED DB: PDB
REMARK 900  ETHYLPHOSPHORYLATED BUTYRYLCHOLINESTERASE (AGED) OBTAINEDBY
REMARK 900  REACTION WITH ECHOTHIOPHATE
REMARK 900 RELATED ID: 1XLW   RELATED DB: PDB
REMARK 900  DIETHYLPHOSPHORYLATED BUTYRYLCHOLINESTERASE (NONAGED)OBTAINED
REMARK 900  BY REACTION WITH ECHOTHIOPHATE
REMARK 900 RELATED ID: 2J4C   RELATED DB: PDB
REMARK 900  STRUCTURE OF HUMAN BUTYRYLCHOLINESTERASE IN COMPLEX WITH
REMARK 900  10MM HGCL2
REMARK 900 RELATED ID: 2WID   RELATED DB: PDB
REMARK 900  AGED FORM OF HUMAN BUTYRYLCHOLINESTERASE INHIBITED BY
REMARK 900  TABUN ANALOGUE TA1
REMARK 900 RELATED ID: 2WIF   RELATED DB: PDB
REMARK 900  AGED FORM OF HUMAN BUTYRYLCHOLINESTERASE INHIBITED BY
REMARK 900  TABUN ANALOGUE TA1
REMARK 900 RELATED ID: 2WIG   RELATED DB: PDB
REMARK 900  NONAGED FORM OF HUMAN BUTYRYLCHOLINESTERASE INHIBITED BY
REMARK 900  TABUN ANALOGUE TA4
REMARK 900 RELATED ID: 2WIJ   RELATED DB: PDB
REMARK 900  NONAGED FORM OF HUMAN BUTYRYLCHOLINESTERASE INHIBITED BY
REMARK 900  TABUN ANALOGUE TA5
REMARK 900 RELATED ID: 2WIK   RELATED DB: PDB
REMARK 900  NONAGED FORM OF HUMAN BUTYRYLCHOLINESTERASE INHIBITED BY
REMARK 900  TABUN ANALOGUE TA6
REMARK 900 RELATED ID: 2WIL   RELATED DB: PDB
REMARK 900  AGED FORM OF HUMAN BUTYRYLCHOLINESTERASE INHIBITED BY
REMARK 900  TABUN ANALOGUE TA5
REMARK 900 RELATED ID: 2WSL   RELATED DB: PDB
REMARK 900  AGED FORM OF HUMAN BUTYRYLCHOLINESTERASE INHIBITED BY
REMARK 900  TABUN ANALOGUE TA4
REMARK 900 RELATED ID: 2XMB   RELATED DB: PDB
REMARK 900  G117H MUTANT OF HUMAN BUTYRYLCHOLINESTERASE IN COMPLEX
REMARK 900  WITH SULFATE
REMARK 900 RELATED ID: 2XMC   RELATED DB: PDB
REMARK 900  G117H MUTANT OF HUMAN BUTYRYLCHOLINESTERASE IN COMPLEX
REMARK 900  WITH FLUORIDE ANION
REMARK 900 RELATED ID: 2XMD   RELATED DB: PDB
REMARK 900  G117H MUTANT OF HUMAN BUTYRYLCHOLINESTERASE IN COMPLEX
REMARK 900  WITH ECHOTHIOPHATE
REMARK 900 RELATED ID: 2XMG   RELATED DB: PDB
REMARK 900  G117H MUTANT OF HUMAN BUTYRYLCHOLINESTERASE IN COMPLEX
REMARK 900  WITH VX
REMARK 900 RELATED ID: 2XQF   RELATED DB: PDB
REMARK 900  X-RAY STRUCTURE OF HUMAN BUTYRYLCHOLINESTERASE INHIBITED
REMARK 900  BY RACEMIC VX
REMARK 900 RELATED ID: 2XQG   RELATED DB: PDB
REMARK 900  X-RAY STRUCTURE OF HUMAN BUTYRYLCHOLINESTERASE INHIBITED
REMARK 900  BY RACEMIC VR
REMARK 900 RELATED ID: 2XQI   RELATED DB: PDB
REMARK 900  X-RAY STRUCTURE OF HUMAN BUTYRYLCHOLINESTERASE INHIBITED
REMARK 900  BY RACEMIC CVX
REMARK 900 RELATED ID: 2XQJ   RELATED DB: PDB
REMARK 900  X-RAY STRUCTURE OF HUMAN BUTYRYLCHOLINESTERASE INHIBITED
REMARK 900  BY PURE ENANTIOMER VX-(R)
REMARK 900 RELATED ID: 2XQK   RELATED DB: PDB
REMARK 900  X-RAY STRUCTURE OF HUMAN BUTYRYLCHOLINESTERASE INHIBITED
REMARK 900  BY PURE ENANTIOMER VX-(S)
REMARK 900 RELATED ID: 2Y1K   RELATED DB: PDB
REMARK 900  STRUCTURE OF HUMAN BUTYRYLCHOLINESTERASE INHIBITED BY CBDP
REMARK 900   (12H SOAK): PHOSPHOSERINE ADDUCT
REMARK 900 RELATED ID: 4AQD   RELATED DB: PDB
REMARK 900  CRYSTAL STRUCTURE OF FULLY GLYCOSYLATED HUMAN
REMARK 900  BUTYRYLCHOLINESTERASE
REMARK 900 RELATED ID: 4AXB   RELATED DB: PDB
REMARK 900  CRYSTAL STRUCTURE OF SOMAN-AGED HUMAN
REMARK 900  BUTYRYLCHOLINESTERASE IN COMPLEX WITH 2-PAM
REMARK 900 RELATED ID: 4B0P   RELATED DB: PDB
REMARK 900  CRYSTAL STRUCTURE OF SOMAN-AGED HUMAN
REMARK 900  BUTYRYLCHOLINESTERASE IN COMPLEX WITH METHYL 2-(
REMARK 900  PENTAFLUOROBENZYLOXYIMINO)PYRIDINIUM
DBREF  4B0O A    1   529  UNP    P06276   CHLE_HUMAN      29    557
SEQADV 4B0O GLN A   17  UNP  P06276    ASN    45 CONFLICT
SEQADV 4B0O GLN A  384  UNP  P06276    ASN   412 CONFLICT
SEQADV 4B0O GLN A  455  UNP  P06276    ASN   483 CONFLICT
SEQADV 4B0O GLN A  481  UNP  P06276    ASN   509 CONFLICT
SEQRES   1 A  529  GLU ASP ASP ILE ILE ILE ALA THR LYS ASN GLY LYS VAL
SEQRES   2 A  529  ARG GLY MET GLN LEU THR VAL PHE GLY GLY THR VAL THR
SEQRES   3 A  529  ALA PHE LEU GLY ILE PRO TYR ALA GLN PRO PRO LEU GLY
SEQRES   4 A  529  ARG LEU ARG PHE LYS LYS PRO GLN SER LEU THR LYS TRP
SEQRES   5 A  529  SER ASP ILE TRP ASN ALA THR LYS TYR ALA ASN SER CYS
SEQRES   6 A  529  CYS GLN ASN ILE ASP GLN SER PHE PRO GLY PHE HIS GLY
SEQRES   7 A  529  SER GLU MET TRP ASN PRO ASN THR ASP LEU SER GLU ASP
SEQRES   8 A  529  CYS LEU TYR LEU ASN VAL TRP ILE PRO ALA PRO LYS PRO
SEQRES   9 A  529  LYS ASN ALA THR VAL LEU ILE TRP ILE TYR GLY GLY GLY
SEQRES  10 A  529  PHE GLN THR GLY THR SER SER LEU HIS VAL TYR ASP GLY
SEQRES  11 A  529  LYS PHE LEU ALA ARG VAL GLU ARG VAL ILE VAL VAL SER
SEQRES  12 A  529  MET ASN TYR ARG VAL GLY ALA LEU GLY PHE LEU ALA LEU
SEQRES  13 A  529  PRO GLY ASN PRO GLU ALA PRO GLY ASN MET GLY LEU PHE
SEQRES  14 A  529  ASP GLN GLN LEU ALA LEU GLN TRP VAL GLN LYS ASN ILE
SEQRES  15 A  529  ALA ALA PHE GLY GLY ASN PRO LYS SER VAL THR LEU PHE
SEQRES  16 A  529  GLY GLU SBG ALA GLY ALA ALA SER VAL SER LEU HIS LEU
SEQRES  17 A  529  LEU SER PRO GLY SER HIS SER LEU PHE THR ARG ALA ILE
SEQRES  18 A  529  LEU GLN SER GLY SER PHE ASN ALA PRO TRP ALA VAL THR
SEQRES  19 A  529  SER LEU TYR GLU ALA ARG ASN ARG THR LEU ASN LEU ALA
SEQRES  20 A  529  LYS LEU THR GLY CYS SER ARG GLU ASN GLU THR GLU ILE
SEQRES  21 A  529  ILE LYS CYS LEU ARG ASN LYS ASP PRO GLN GLU ILE LEU
SEQRES  22 A  529  LEU ASN GLU ALA PHE VAL VAL PRO TYR GLY THR PRO LEU
SEQRES  23 A  529  SER VAL ASN PHE GLY PRO THR VAL ASP GLY ASP PHE LEU
SEQRES  24 A  529  THR ASP MET PRO ASP ILE LEU LEU GLU LEU GLY GLN PHE
SEQRES  25 A  529  LYS LYS THR GLN ILE LEU VAL GLY VAL ASN LYS ASP GLU
SEQRES  26 A  529  GLY THR ALA PHE LEU VAL TYR GLY ALA PRO GLY PHE SER
SEQRES  27 A  529  LYS ASP ASN ASN SER ILE ILE THR ARG LYS GLU PHE GLN
SEQRES  28 A  529  GLU GLY LEU LYS ILE PHE PHE PRO GLY VAL SER GLU PHE
SEQRES  29 A  529  GLY LYS GLU SER ILE LEU PHE HIS TYR THR ASP TRP VAL
SEQRES  30 A  529  ASP ASP GLN ARG PRO GLU GLN TYR ARG GLU ALA LEU GLY
SEQRES  31 A  529  ASP VAL VAL GLY ASP TYR ASN PHE ILE CYS PRO ALA LEU
SEQRES  32 A  529  GLU PHE THR LYS LYS PHE SER GLU TRP GLY ASN ASN ALA
SEQRES  33 A  529  PHE PHE TYR TYR PHE GLU HIS ARG SER SER LYS LEU PRO
SEQRES  34 A  529  TRP PRO GLU TRP MET GLY VAL MET HIS GLY TYR GLU ILE
SEQRES  35 A  529  GLU PHE VAL PHE GLY LEU PRO LEU GLU ARG ARG ASP GLN
SEQRES  36 A  529  TYR THR LYS ALA GLU GLU ILE LEU SER ARG SER ILE VAL
SEQRES  37 A  529  LYS ARG TRP ALA ASN PHE ALA LYS TYR GLY ASN PRO GLN
SEQRES  38 A  529  GLU THR GLN ASN ASN SER THR SER TRP PRO VAL PHE LYS
SEQRES  39 A  529  SER THR GLU GLN LYS TYR LEU THR LEU ASN THR GLU SER
SEQRES  40 A  529  THR ARG ILE MET THR LYS LEU ARG ALA GLN GLN CYS ARG
SEQRES  41 A  529  PHE TRP THR SER PHE PHE PRO LYS VAL
MODRES 4B0O SBG A  198  SER  O-[(S)-HYDROXY(METHYL)PHOSPHORYL]-L-SERINE
HET    SBG  A 198      10
HET    NAG  A 540      14
HET    NAG  A 550      14
HET    NAG  A 560      14
HET    NAG  A 561      14
HET    FUL  A 562      10
HET    NAG  A 570      14
HET    NAG  A 571      14
HET    FUL  A 572      10
HET    NAG  A 580      14
HET    NAG  A 590      14
HET    GLY  A1296       5
HET     CL  A1297       1
HET     CL  A1298       1
HET     CL  A1299       1
HET     CL  A1300       1
HET     CL  A1301       1
HET     BR  A1302       1
HET     CA  A1303       1
HET     CA  A1304       1
HET     NA  A1305       1
HET     NA  A1306       1
HET    15F  A1307      29
HETNAM     SBG O-[(S)-HYDROXY(METHYL)PHOSPHORYL]-L-SERINE
HETNAM     NAG N-ACETYL-D-GLUCOSAMINE
HETNAM     FUL BETA-L-FUCOSE
HETNAM     GLY GLYCINE
HETNAM      CL CHLORIDE ION
HETNAM      BR BROMIDE ION
HETNAM      CA CALCIUM ION
HETNAM      NA SODIUM ION
HETNAM     15F 1-BENZYL-4-({[(1E)-2,2,2-
HETNAM   2 15F  TRICHLOROETHANIMIDOYL]OXY}METHYL)PYRIDINIUM
HETSYN     FUL 6-DEOXY-BETA-L-GALACTOSE
FORMUL   2  SBG    C4 H10 N O5 P
FORMUL   3  NAG    8(C8 H15 N O6)
FORMUL   4  FUL    2(C6 H12 O5)
FORMUL   5  GLY    C2 H5 N O2
FORMUL   6   CL    5(CL 1-)
FORMUL   7   BR    BR 1-
FORMUL   8   CA    2(CA 2+)
FORMUL   9   NA    2(NA 1+)
FORMUL   9  15F    C15 H14 CL3 N2 O 1+
FORMUL  10  HOH   *295(H2 O)
HELIX    1   1 LEU A   38  ARG A   42  5                                   5
HELIX    2   2 PHE A   76  MET A   81  1                                   6
HELIX    3   3 LEU A  125  ASP A  129  5                                   5
HELIX    4   4 GLY A  130  ARG A  138  1                                   9
HELIX    5   5 VAL A  148  LEU A  154  1                                   7
HELIX    6   6 ASN A  165  ILE A  182  1                                  18
HELIX    7   7 ALA A  183  PHE A  185  5                                   3
HELIX    8   8 ALA A  199  SER A  210  1                                  12
HELIX    9   9 PRO A  211  PHE A  217  5                                   7
HELIX   10  10 SER A  235  THR A  250  1                                  16
HELIX   11  11 ASN A  256  ARG A  265  1                                  10
HELIX   12  12 ASP A  268  GLU A  276  1                                   9
HELIX   13  13 ALA A  277  VAL A  280  5                                   4
HELIX   14  14 MET A  302  LEU A  309  1                                   8
HELIX   15  15 GLY A  326  VAL A  331  1                                   6
HELIX   16  16 THR A  346  PHE A  358  1                                  13
HELIX   17  17 SER A  362  THR A  374  1                                  13
HELIX   18  18 GLU A  383  PHE A  398  1                                  16
HELIX   19  19 PHE A  398  GLU A  411  1                                  14
HELIX   20  20 PRO A  431  GLY A  435  5                                   5
HELIX   21  21 GLU A  441  PHE A  446  1                                   6
HELIX   22  22 GLY A  447  GLU A  451  5                                   5
HELIX   23  23 GLU A  451  GLN A  455  5                                   5
HELIX   24  24 THR A  457  GLY A  478  1                                  22
HELIX   25  25 ARG A  515  SER A  524  1                                  10
SHEET    1  AA 3 ILE A   5  THR A   8  0
SHEET    2  AA 3 GLY A  11  ARG A  14 -1  O  GLY A  11   N  THR A   8
SHEET    3  AA 3 ILE A  55  ASN A  57  1  O  TRP A  56   N  ARG A  14
SHEET    1  AB11 MET A  16  VAL A  20  0
SHEET    2  AB11 GLY A  23  PRO A  32 -1  O  GLY A  23   N  VAL A  20
SHEET    3  AB11 TYR A  94  ALA A 101 -1  O  LEU A  95   N  ILE A  31
SHEET    4  AB11 ILE A 140  MET A 144 -1  O  VAL A 141   N  TRP A  98
SHEET    5  AB11 ALA A 107  ILE A 113  1  O  THR A 108   N  ILE A 140
SHEET    6  AB11 GLY A 187  GLY A 196  1  N  ASN A 188   O  ALA A 107
SHEET    7  AB11 ARG A 219  GLN A 223  1  O  ARG A 219   N  LEU A 194
SHEET    8  AB11 ILE A 317  ASN A 322  1  O  LEU A 318   N  LEU A 222
SHEET    9  AB11 ALA A 416  PHE A 421  1  O  PHE A 417   N  VAL A 319
SHEET   10  AB11 LYS A 499  LEU A 503  1  O  LEU A 501   N  TYR A 420
SHEET   11  AB11 ILE A 510  THR A 512 -1  O  MET A 511   N  TYR A 500
SHEET    1  AC 2 SER A  64  CYS A  65  0
SHEET    2  AC 2 LEU A  88  SER A  89  1  N  SER A  89   O  SER A  64
SSBOND   1 CYS A   65    CYS A   92                          1555   1555  2.04
SSBOND   2 CYS A  252    CYS A  263                          1555   1555  2.04
SSBOND   3 CYS A  400    CYS A  519                          1555   1555  2.05
LINK         ND2 ASN A  57                 C1  NAG A 540     1555   1555  1.44
LINK         ND2 ASN A 106                 C1  NAG A 550     1555   1555  1.45
LINK         N   SBG A 198                 C   GLU A 197     1555   1555  1.34
LINK         C   SBG A 198                 N   ALA A 199     1555   1555  1.34
LINK         ND2 ASN A 241                 C1  NAG A 560     1555   1555  1.45
LINK         ND2 ASN A 256                 C1  NAG A 590     1555   1555  1.44
LINK         ND2 ASN A 341                 C1  NAG A 570     1555   1555  1.45
LINK         ND2 ASN A 485                 C1  NAG A 580     1555   1555  1.45
LINK         O4  NAG A 560                 C1  NAG A 561     1555   1555  1.45
LINK         O6  NAG A 560                 C1  FUL A 562     1555   1555  1.44
LINK         O6  NAG A 570                 C1  FUL A 572     1555   1555  1.45
LINK         O4  NAG A 570                 C1  NAG A 571     1555   1555  1.43
LINK        CA    CA A1303                 O   HOH A2271     1555   1555  3.13
CISPEP   1 ALA A  101    PRO A  102          0         2.57
CISPEP   2 VAL A  377    ASP A  378          0       -13.42
SITE     1 AC1  5 LEU A  18  TYR A  61  TRP A  98  ASP A 129
SITE     2 AC1  5 LYS A 131
SITE     1 AC2  2 ARG A 347  HOH A2191
SITE     1 AC3  1 THR A 512
SITE     1 AC4  2 PHE A 217  THR A 218
SITE     1 AC5  1 GLN A 316
SITE     1 AC6  1 TYR A 420
SITE     1 AC7  1 THR A 488
SITE     1 AC8  1 ARG A 242
SITE     1 AC9  2 CYS A  66  GLN A 270
SITE     1 BC1 17 ASP A  70  SER A  72  TRP A  82  GLY A 116
SITE     2 BC1 17 GLY A 117  PRO A 285  SER A 287  ALA A 328
SITE     3 BC1 17 PHE A 329  TYR A 332  TRP A 430  MET A 437
SITE     4 BC1 17 HIS A 438  TYR A 440  HOH A2011  HOH A2012
SITE     5 BC1 17 HOH A2291
SITE     1 BC2  3 ASN A  57  HOH A2279  HOH A2280
SITE     1 BC3  4 ASN A 106  ASN A 188  HOH A2281  HOH A2282
SITE     1 BC4  8 ASN A 241  ASN A 245  LYS A 248  LEU A 249
SITE     2 BC4  8 PHE A 278  PRO A 281  HOH A2150  HOH A2284
SITE     1 BC5  3 ASN A 256  HOH A2289  HOH A2290
SITE     1 BC6  6 PRO A 335  GLY A 336  SER A 338  ASN A 341
SITE     2 BC6  6 ASN A 342  HOH A2285
SITE     1 BC7  3 ARG A 465  ASN A 485  HOH A2288
CRYST1  155.510  155.510  128.460  90.00  90.00  90.00 I 4 2 2      16
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      0.006430  0.000000  0.000000        0.00000
SCALE2      0.000000  0.006430  0.000000        0.00000
SCALE3      0.000000  0.000000  0.007785        0.00000
TER    4275      VAL A 529
MASTER      569    0   23   25   16    0   23    6 4745    1  192   41
END