longtext: 2DQZ-pdb

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HEADER    HYDROLASE                               02-JUN-06   2DQZ
TITLE     CRYSTAL STRUCTURE OF HUMAN CARBOXYLESTERASE IN COMPLEX WITH
TITLE    2 HOMATROPINE, COENZYME A, AND PALMITATE
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: LIVER CARBOXYLESTERASE 1;
COMPND   3 CHAIN: A, B, C;
COMPND   4 FRAGMENT: RESIDUES 19-561;
COMPND   5 SYNONYM: ACYL COENZYME A:CHOLESTEROL ACYLTRANSFERASE, ACAT,
COMPND   6 MONOCYTE/MACROPHAGE SERINE ESTERASE, HMSE, SERINE ESTERASE
COMPND   7 1, BRAIN CARBOXYLESTERASE HBR1, TRIACYLGLYCEROL HYDROLASE,
COMPND   8 TGH, EGASYN;
COMPND   9 EC: 3.1.1.1;
COMPND  10 ENGINEERED: YES
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE   3 ORGANISM_COMMON: HUMAN;
SOURCE   4 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;
SOURCE   5 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM;
SOURCE   6 EXPRESSION_SYSTEM_CELL_LINE: SF9;
SOURCE   7 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS
KEYWDS    CHOLESTEROL, ESTERASE
EXPDTA    X-RAY DIFFRACTION
AUTHOR    S.BENCHARIT,M.R.REDINBO
REVDAT   1   29-AUG-06 2DQZ    0
JRNL        AUTH   S.BENCHARIT,C.C.EDWARDS,C.L.MORTON,
JRNL        AUTH 2 E.L.HOWARD-WILLIAMS,P.KUHN,P.M.POTTER,M.R.REDINBO
JRNL        TITL   MULTISITE PROMISCUITY ENABLES HUMAN
JRNL        TITL 2 CARBOXYLESTERASE 1 TO METABOLIZE A VARIETY OF
JRNL        TITL 3 ENDOGENOUS SUBSTRATES
JRNL        REF    TO BE PUBLISHED
JRNL        REFN
REMARK   1
REMARK   2
REMARK   2 RESOLUTION. 2.80 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : CNS 1.1
REMARK   3   AUTHORS     : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-
REMARK   3               : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES, PANNU,
REMARK   3               : READ,RICE,SIMONSON,WARREN
REMARK   3
REMARK   3  REFINEMENT TARGET : ENGH & HUBER
REMARK   3
REMARK   3  DATA USED IN REFINEMENT.
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.80
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 22.60
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 1.000
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : 2112319.150
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : 0.0000
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 97.9
REMARK   3   NUMBER OF REFLECTIONS             : 50237
REMARK   3
REMARK   3  FIT TO DATA USED IN REFINEMENT.
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM
REMARK   3   R VALUE            (WORKING SET) : 0.193
REMARK   3   FREE R VALUE                     : 0.244
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 7.100
REMARK   3   FREE R VALUE TEST SET COUNT      : 3546
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : 0.004
REMARK   3
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.
REMARK   3   TOTAL NUMBER OF BINS USED           : 6
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.80
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.98
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 91.70
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 7106
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2890
REMARK   3   BIN FREE R VALUE                    : 0.3550
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 7.60
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 583
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : 0.015
REMARK   3
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK   3   PROTEIN ATOMS            : 12390
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 263
REMARK   3   SOLVENT ATOMS            : 508
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : 47.20
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 39.50
REMARK   3   OVERALL ANISOTROPIC B VALUE.
REMARK   3    B11 (A**2) : -4.36000
REMARK   3    B22 (A**2) : 6.57000
REMARK   3    B33 (A**2) : -2.21000
REMARK   3    B12 (A**2) : 0.00000
REMARK   3    B13 (A**2) : 0.00000
REMARK   3    B23 (A**2) : 0.00000
REMARK   3
REMARK   3  ESTIMATED COORDINATE ERROR.
REMARK   3   ESD FROM LUZZATI PLOT        (A) : 0.30
REMARK   3   ESD FROM SIGMAA              (A) : 0.34
REMARK   3   LOW RESOLUTION CUTOFF        (A) : 5.00
REMARK   3
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : 0.39
REMARK   3   ESD FROM C-V SIGMAA          (A) : 0.45
REMARK   3
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.
REMARK   3   BOND LENGTHS                 (A) : 0.007
REMARK   3   BOND ANGLES            (DEGREES) : 1.20
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 22.90
REMARK   3   IMPROPER ANGLES        (DEGREES) : 0.84
REMARK   3
REMARK   3  ISOTROPIC THERMAL MODEL : RESTRAINED
REMARK   3
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA
REMARK   3   MAIN-CHAIN BOND              (A**2) : 1.380 ; 1.500
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : 2.400 ; 2.000
REMARK   3   SIDE-CHAIN BOND              (A**2) : 1.860 ; 2.000
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : 2.900 ; 2.500
REMARK   3
REMARK   3  BULK SOLVENT MODELING.
REMARK   3   METHOD USED : FLAT MODEL
REMARK   3   KSOL        : 0.37
REMARK   3   BSOL        : 47.35
REMARK   3
REMARK   3  NCS MODEL : NULL
REMARK   3
REMARK   3  NCS RESTRAINTS.                         RMS   SIGMA/WEIGHT
REMARK   3   GROUP  1  POSITIONAL            (A) : NULL  ; NULL
REMARK   3   GROUP  1  B-FACTOR           (A**2) : NULL  ; NULL
REMARK   3
REMARK   3  PARAMETER FILE  1  : PROTEIN_REP.PARAM
REMARK   3  PARAMETER FILE  2  : CARBOHYDRATE.PARAM
REMARK   3  PARAMETER FILE  3  : WATER_REP.PARAM
REMARK   3  PARAMETER FILE  4  : ION.PARAM
REMARK   3  PARAMETER FILE  5  : HTO.PARAM
REMARK   3  PARAMETER FILE  6  : NULL
REMARK   3  TOPOLOGY FILE  1   : PROTEIN.TOP
REMARK   3  TOPOLOGY FILE  2   : CARBOHYDRATE.TOP
REMARK   3  TOPOLOGY FILE  3   : WATER.TOP
REMARK   3  TOPOLOGY FILE  4   : ION.TOP
REMARK   3  TOPOLOGY FILE  5   : HTO.TOP
REMARK   3  TOPOLOGY FILE  6   : NULL
REMARK   3
REMARK   3  OTHER REFINEMENT REMARKS: NULL
REMARK   4
REMARK   4 2DQZ COMPLIES WITH FORMAT V. 2.3, 09-JULY-1998
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 06-JUN-2006.
REMARK 100 THE RCSB ID CODE IS RCSB025740.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 14-APR-2001
REMARK 200  TEMPERATURE           (KELVIN) : NULL
REMARK 200  PH                             : 5.60
REMARK 200  NUMBER OF CRYSTALS USED        : 1
REMARK 200
REMARK 200  SYNCHROTRON              (Y/N) : Y
REMARK 200  RADIATION SOURCE               : SSRL
REMARK 200  BEAMLINE                       : BL9-3
REMARK 200  X-RAY GENERATOR MODEL          : NULL
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : NULL
REMARK 200  MONOCHROMATOR                  : NULL
REMARK 200  OPTICS                         : NULL
REMARK 200
REMARK 200  DETECTOR TYPE                  : CCD
REMARK 200  DETECTOR MANUFACTURER          : MAR CCD 165MM
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : ADSC
REMARK 200  DATA SCALING SOFTWARE          : MOSFLM
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 50837
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.800
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.1
REMARK 200  DATA REDUNDANCY                : 4.700
REMARK 200  R MERGE                    (I) : NULL
REMARK 200  R SYM                      (I) : 0.12300
REMARK 200   FOR THE DATA SET  : 8.5000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.80
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 3.00
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.7
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL
REMARK 200  R MERGE FOR SHELL          (I) : NULL
REMARK 200  R SYM FOR SHELL            (I) : 0.34100
REMARK 200   FOR SHELL         : 2.800
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: AMORE
REMARK 200 STARTING MODEL: 1MX5
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 56.66
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.84
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 8% PEG 3350, 0.4M LI2SO4, 0.1M
REMARK 280  NACL, 0.1M LICL, 0.1M CITRATE (PH 5.5), 5% GLYCEROL , PH 5.6,
REMARK 280  VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 298K
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   1/2-X,-Y,1/2+Z
REMARK 290       3555   -X,1/2+Y,1/2-Z
REMARK 290       4555   1/2+X,1/2-Y,-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       27.78200
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000      101.28000
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       90.50850
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000      101.28000
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       27.78200
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       90.50850
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 THIS ENTRY CONTAINS THE CRYSTALLOGRAPHIC ASYMMETRIC UNIT
REMARK 300 WHICH CONSISTS OF 3 CHAIN(S). SEE REMARK 350 FOR
REMARK 300 INFORMATION ON GENERATING THE BIOLOGICAL MOLECULE(S).
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 APPLY THE FOLLOWING TO CHAINS: A, B, C
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     HIS A  1019
REMARK 465     PRO A  1020
REMARK 465     LYS A  1554
REMARK 465     ALA A  1555
REMARK 465     VAL A  1556
REMARK 465     GLU A  1557
REMARK 465     LYS A  1558
REMARK 465     PRO A  1559
REMARK 465     PRO A  1560
REMARK 465     GLN A  1561
REMARK 465     HIS B  2019
REMARK 465     PRO B  2020
REMARK 465     LYS B  2554
REMARK 465     ALA B  2555
REMARK 465     VAL B  2556
REMARK 465     GLU B  2557
REMARK 465     LYS B  2558
REMARK 465     PRO B  2559
REMARK 465     PRO B  2560
REMARK 465     GLN B  2561
REMARK 465     HIS C  3019
REMARK 465     PRO C  3020
REMARK 465     LYS C  3554
REMARK 465     ALA C  3555
REMARK 465     VAL C  3556
REMARK 465     GLU C  3557
REMARK 465     LYS C  3558
REMARK 465     PRO C  3559
REMARK 465     PRO C  3560
REMARK 465     GLN C  3561
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
REMARK 500   O9   SIA     382     O    HOH    7347              2.06
REMARK 500   O7   SIA     382     O    HOH    7034              2.18
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
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,2(A3,1X,A1,I4,A1,1X,A4,3X),F6.3)
REMARK 500
REMARK 500 EXPECTED VALUES: ENGH AND HUBER, 1991
REMARK 500
REMARK 500  M RES CSSEQI ATM1   RES CSSEQI ATM2   DEVIATION
REMARK 500    MET A1425   SD    MET A1425   CE    -0.048
REMARK 500    THR B2151   CA    THR B2151   CB     0.048
REMARK 500    MET B2282   CG    MET B2282   SD     0.048
REMARK 500    MET B2459   SD    MET B2459   CE     0.046
REMARK 500    MET C3136   SD    MET C3136   CE    -0.072
REMARK 500    MET C3145   SD    MET C3145   CE     0.073
REMARK 500    MET C3425   SD    MET C3425   CE    -0.073
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, 1991
REMARK 500
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3
REMARK 500    GLY A1052   N   -  CA  -  C   ANGL. DEV. =  6.9 DEGREES
REMARK 500    SER A1075   N   -  CA  -  C   ANGL. DEV. =  7.5 DEGREES
REMARK 500    ASP A1115   N   -  CA  -  C   ANGL. DEV. = -7.9 DEGREES
REMARK 500    PHE A1177   N   -  CA  -  C   ANGL. DEV. =  9.0 DEGREES
REMARK 500    GLY A1320   N   -  CA  -  C   ANGL. DEV. =  7.7 DEGREES
REMARK 500    LEU A1358   N   -  CA  -  C   ANGL. DEV. =  7.2 DEGREES
REMARK 500    LEU B2034   CA  -  CB  -  CG  ANGL. DEV. =  9.3 DEGREES
REMARK 500    SER B2075   N   -  CA  -  C   ANGL. DEV. =  8.2 DEGREES
REMARK 500    ASP B2090   N   -  CA  -  C   ANGL. DEV. = -7.8 DEGREES
REMARK 500    LEU B2119   CA  -  CB  -  CG  ANGL. DEV. =  7.6 DEGREES
REMARK 500    PHE B2177   N   -  CA  -  C   ANGL. DEV. =  7.2 DEGREES
REMARK 500    PHE B2303   N   -  CA  -  C   ANGL. DEV. =  8.2 DEGREES
REMARK 500    LEU C3034   CA  -  CB  -  CG  ANGL. DEV. =  8.1 DEGREES
REMARK 500    MET C3086   N   -  CA  -  C   ANGL. DEV. = -7.0 DEGREES
REMARK 500    ASP C3090   N   -  CA  -  C   ANGL. DEV. = -7.9 DEGREES
REMARK 500    PHE C3177   N   -  CA  -  C   ANGL. DEV. =  7.0 DEGREES
REMARK 500    THR C3252   N   -  CA  -  C   ANGL. DEV. = -7.0 DEGREES
REMARK 500    SER C3253   N   -  CA  -  C   ANGL. DEV. =  7.9 DEGREES
REMARK 500    PHE C3303   N   -  CA  -  C   ANGL. DEV. =  8.1 DEGREES
REMARK 500    LEU C3319   N   -  CA  -  C   ANGL. DEV. = -8.1 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  M RES CSSEQI        PSI       PHI
REMARK 500    SER A1221     -116.19     62.02
REMARK 500    SER C3221     -115.22     58.96
REMARK 525
REMARK 525 SOLVENT
REMARK 525 THE FOLLOWING SOLVENT MOLECULES LIE FARTHER THAN EXPECTED
REMARK 525 FROM THE PROTEIN OR NUCLEIC ACID MOLECULE AND MAY BE
REMARK 525 ASSOCIATED WITH A SYMMETRY RELATED MOLECULE (M=MODEL
REMARK 525 NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525  M RES CSSEQI
REMARK 525    HOH  7050        DISTANCE =  7.24 ANGSTROMS
REMARK 525    HOH  7093        DISTANCE =  6.48 ANGSTROMS
REMARK 525    HOH  7269        DISTANCE =  5.24 ANGSTROMS
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2H7C   RELATED DB: PDB
REMARK 900 SAME PROTEIN IN COMPLEX WITH COENZYME A
REMARK 900 RELATED ID: 2DQY   RELATED DB: PDB
REMARK 900 SAME PROTEIN IN COMPLEX WITH CHOLATE AND PALMITATE
REMARK 900 RELATED ID: 2DR0   RELATED DB: PDB
REMARK 900 SAME PROTEIN IN COMPLEX WITH TAUROCHOLATE
DBREF  2DQZ A 1019  1561  UNP    P23141   EST1_HUMAN      19    561
DBREF  2DQZ B 2019  2561  UNP    P23141   EST1_HUMAN      19    561
DBREF  2DQZ C 3019  3561  UNP    P23141   EST1_HUMAN      19    561
SEQADV 2DQZ     A       UNP  P23141    GLN   362 DELETION
SEQADV 2DQZ     B       UNP  P23141    GLN   362 DELETION
SEQADV 2DQZ     C       UNP  P23141    GLN   362 DELETION
SEQRES   1 A  542  HIS PRO SER SER PRO PRO VAL VAL ASP THR VAL HIS GLY
SEQRES   2 A  542  LYS VAL LEU GLY LYS PHE VAL SER LEU GLU GLY PHE ALA
SEQRES   3 A  542  GLN PRO VAL ALA ILE PHE LEU GLY ILE PRO PHE ALA LYS
SEQRES   4 A  542  PRO PRO LEU GLY PRO LEU ARG PHE THR PRO PRO GLN PRO
SEQRES   5 A  542  ALA GLU PRO TRP SER PHE VAL LYS ASN ALA THR SER TYR
SEQRES   6 A  542  PRO PRO MET CYS THR GLN ASP PRO LYS ALA GLY GLN LEU
SEQRES   7 A  542  LEU SER GLU LEU PHE THR ASN ARG LYS GLU ASN ILE PRO
SEQRES   8 A  542  LEU LYS LEU SER GLU ASP CYS LEU TYR LEU ASN ILE TYR
SEQRES   9 A  542  THR PRO ALA ASP LEU THR LYS LYS ASN ARG LEU PRO VAL
SEQRES  10 A  542  MET VAL TRP ILE HIS GLY GLY GLY LEU MET VAL GLY ALA
SEQRES  11 A  542  ALA SER THR TYR ASP GLY LEU ALA LEU ALA ALA HIS GLU
SEQRES  12 A  542  ASN VAL VAL VAL VAL THR ILE GLN TYR ARG LEU GLY ILE
SEQRES  13 A  542  TRP GLY PHE PHE SER THR GLY ASP GLU HIS SER ARG GLY
SEQRES  14 A  542  ASN TRP GLY HIS LEU ASP GLN VAL ALA ALA LEU ARG TRP
SEQRES  15 A  542  VAL GLN ASP ASN ILE ALA SER PHE GLY GLY ASN PRO GLY
SEQRES  16 A  542  SER VAL THR ILE PHE GLY GLU SER ALA GLY GLY GLU SER
SEQRES  17 A  542  VAL SER VAL LEU VAL LEU SER PRO LEU ALA LYS ASN LEU
SEQRES  18 A  542  PHE HIS ARG ALA ILE SER GLU SER GLY VAL ALA LEU THR
SEQRES  19 A  542  SER VAL LEU VAL LYS LYS GLY ASP VAL LYS PRO LEU ALA
SEQRES  20 A  542  GLU GLN ILE ALA ILE THR ALA GLY CYS LYS THR THR THR
SEQRES  21 A  542  SER ALA VAL MET VAL HIS CYS LEU ARG GLN LYS THR GLU
SEQRES  22 A  542  GLU GLU LEU LEU GLU THR THR LEU LYS MET LYS PHE LEU
SEQRES  23 A  542  SER LEU ASP LEU GLN GLY ASP PRO ARG GLU SER GLN PRO
SEQRES  24 A  542  LEU LEU GLY THR VAL ILE ASP GLY MET LEU LEU LEU LYS
SEQRES  25 A  542  THR PRO GLU GLU LEU GLN ALA GLU ARG ASN PHE HIS THR
SEQRES  26 A  542  VAL PRO TYR MET VAL GLY ILE ASN LYS GLN GLU PHE GLY
SEQRES  27 A  542  TRP LEU ILE PRO MET LEU MET SER TYR PRO LEU SER GLU
SEQRES  28 A  542  GLY GLN LEU ASP GLN LYS THR ALA MET SER LEU LEU TRP
SEQRES  29 A  542  LYS SER TYR PRO LEU VAL CYS ILE ALA LYS GLU LEU ILE
SEQRES  30 A  542  PRO GLU ALA THR GLU LYS TYR LEU GLY GLY THR ASP ASP
SEQRES  31 A  542  THR VAL LYS LYS LYS ASP LEU PHE LEU ASP LEU ILE ALA
SEQRES  32 A  542  ASP VAL MET PHE GLY VAL PRO SER VAL ILE VAL ALA ARG
SEQRES  33 A  542  ASN HIS ARG ASP ALA GLY ALA PRO THR TYR MET TYR GLU
SEQRES  34 A  542  PHE GLN TYR ARG PRO SER PHE SER SER ASP MET LYS PRO
SEQRES  35 A  542  LYS THR VAL ILE GLY ASP HIS GLY ASP GLU LEU PHE SER
SEQRES  36 A  542  VAL PHE GLY ALA PRO PHE LEU LYS GLU GLY ALA SER GLU
SEQRES  37 A  542  GLU GLU ILE ARG LEU SER LYS MET VAL MET LYS PHE TRP
SEQRES  38 A  542  ALA ASN PHE ALA ARG ASN GLY ASN PRO ASN GLY GLU GLY
SEQRES  39 A  542  LEU PRO HIS TRP PRO GLU TYR ASN GLN LYS GLU GLY TYR
SEQRES  40 A  542  LEU GLN ILE GLY ALA ASN THR GLN ALA ALA GLN LYS LEU
SEQRES  41 A  542  LYS ASP LYS GLU VAL ALA PHE TRP THR ASN LEU PHE ALA
SEQRES  42 A  542  LYS LYS ALA VAL GLU LYS PRO PRO GLN
SEQRES   1 B  542  HIS PRO SER SER PRO PRO VAL VAL ASP THR VAL HIS GLY
SEQRES   2 B  542  LYS VAL LEU GLY LYS PHE VAL SER LEU GLU GLY PHE ALA
SEQRES   3 B  542  GLN PRO VAL ALA ILE PHE LEU GLY ILE PRO PHE ALA LYS
SEQRES   4 B  542  PRO PRO LEU GLY PRO LEU ARG PHE THR PRO PRO GLN PRO
SEQRES   5 B  542  ALA GLU PRO TRP SER PHE VAL LYS ASN ALA THR SER TYR
SEQRES   6 B  542  PRO PRO MET CYS THR GLN ASP PRO LYS ALA GLY GLN LEU
SEQRES   7 B  542  LEU SER GLU LEU PHE THR ASN ARG LYS GLU ASN ILE PRO
SEQRES   8 B  542  LEU LYS LEU SER GLU ASP CYS LEU TYR LEU ASN ILE TYR
SEQRES   9 B  542  THR PRO ALA ASP LEU THR LYS LYS ASN ARG LEU PRO VAL
SEQRES  10 B  542  MET VAL TRP ILE HIS GLY GLY GLY LEU MET VAL GLY ALA
SEQRES  11 B  542  ALA SER THR TYR ASP GLY LEU ALA LEU ALA ALA HIS GLU
SEQRES  12 B  542  ASN VAL VAL VAL VAL THR ILE GLN TYR ARG LEU GLY ILE
SEQRES  13 B  542  TRP GLY PHE PHE SER THR GLY ASP GLU HIS SER ARG GLY
SEQRES  14 B  542  ASN TRP GLY HIS LEU ASP GLN VAL ALA ALA LEU ARG TRP
SEQRES  15 B  542  VAL GLN ASP ASN ILE ALA SER PHE GLY GLY ASN PRO GLY
SEQRES  16 B  542  SER VAL THR ILE PHE GLY GLU SER ALA GLY GLY GLU SER
SEQRES  17 B  542  VAL SER VAL LEU VAL LEU SER PRO LEU ALA LYS ASN LEU
SEQRES  18 B  542  PHE HIS ARG ALA ILE SER GLU SER GLY VAL ALA LEU THR
SEQRES  19 B  542  SER VAL LEU VAL LYS LYS GLY ASP VAL LYS PRO LEU ALA
SEQRES  20 B  542  GLU GLN ILE ALA ILE THR ALA GLY CYS LYS THR THR THR
SEQRES  21 B  542  SER ALA VAL MET VAL HIS CYS LEU ARG GLN LYS THR GLU
SEQRES  22 B  542  GLU GLU LEU LEU GLU THR THR LEU LYS MET LYS PHE LEU
SEQRES  23 B  542  SER LEU ASP LEU GLN GLY ASP PRO ARG GLU SER GLN PRO
SEQRES  24 B  542  LEU LEU GLY THR VAL ILE ASP GLY MET LEU LEU LEU LYS
SEQRES  25 B  542  THR PRO GLU GLU LEU GLN ALA GLU ARG ASN PHE HIS THR
SEQRES  26 B  542  VAL PRO TYR MET VAL GLY ILE ASN LYS GLN GLU PHE GLY
SEQRES  27 B  542  TRP LEU ILE PRO MET LEU MET SER TYR PRO LEU SER GLU
SEQRES  28 B  542  GLY GLN LEU ASP GLN LYS THR ALA MET SER LEU LEU TRP
SEQRES  29 B  542  LYS SER TYR PRO LEU VAL CYS ILE ALA LYS GLU LEU ILE
SEQRES  30 B  542  PRO GLU ALA THR GLU LYS TYR LEU GLY GLY THR ASP ASP
SEQRES  31 B  542  THR VAL LYS LYS LYS ASP LEU PHE LEU ASP LEU ILE ALA
SEQRES  32 B  542  ASP VAL MET PHE GLY VAL PRO SER VAL ILE VAL ALA ARG
SEQRES  33 B  542  ASN HIS ARG ASP ALA GLY ALA PRO THR TYR MET TYR GLU
SEQRES  34 B  542  PHE GLN TYR ARG PRO SER PHE SER SER ASP MET LYS PRO
SEQRES  35 B  542  LYS THR VAL ILE GLY ASP HIS GLY ASP GLU LEU PHE SER
SEQRES  36 B  542  VAL PHE GLY ALA PRO PHE LEU LYS GLU GLY ALA SER GLU
SEQRES  37 B  542  GLU GLU ILE ARG LEU SER LYS MET VAL MET LYS PHE TRP
SEQRES  38 B  542  ALA ASN PHE ALA ARG ASN GLY ASN PRO ASN GLY GLU GLY
SEQRES  39 B  542  LEU PRO HIS TRP PRO GLU TYR ASN GLN LYS GLU GLY TYR
SEQRES  40 B  542  LEU GLN ILE GLY ALA ASN THR GLN ALA ALA GLN LYS LEU
SEQRES  41 B  542  LYS ASP LYS GLU VAL ALA PHE TRP THR ASN LEU PHE ALA
SEQRES  42 B  542  LYS LYS ALA VAL GLU LYS PRO PRO GLN
SEQRES   1 C  542  HIS PRO SER SER PRO PRO VAL VAL ASP THR VAL HIS GLY
SEQRES   2 C  542  LYS VAL LEU GLY LYS PHE VAL SER LEU GLU GLY PHE ALA
SEQRES   3 C  542  GLN PRO VAL ALA ILE PHE LEU GLY ILE PRO PHE ALA LYS
SEQRES   4 C  542  PRO PRO LEU GLY PRO LEU ARG PHE THR PRO PRO GLN PRO
SEQRES   5 C  542  ALA GLU PRO TRP SER PHE VAL LYS ASN ALA THR SER TYR
SEQRES   6 C  542  PRO PRO MET CYS THR GLN ASP PRO LYS ALA GLY GLN LEU
SEQRES   7 C  542  LEU SER GLU LEU PHE THR ASN ARG LYS GLU ASN ILE PRO
SEQRES   8 C  542  LEU LYS LEU SER GLU ASP CYS LEU TYR LEU ASN ILE TYR
SEQRES   9 C  542  THR PRO ALA ASP LEU THR LYS LYS ASN ARG LEU PRO VAL
SEQRES  10 C  542  MET VAL TRP ILE HIS GLY GLY GLY LEU MET VAL GLY ALA
SEQRES  11 C  542  ALA SER THR TYR ASP GLY LEU ALA LEU ALA ALA HIS GLU
SEQRES  12 C  542  ASN VAL VAL VAL VAL THR ILE GLN TYR ARG LEU GLY ILE
SEQRES  13 C  542  TRP GLY PHE PHE SER THR GLY ASP GLU HIS SER ARG GLY
SEQRES  14 C  542  ASN TRP GLY HIS LEU ASP GLN VAL ALA ALA LEU ARG TRP
SEQRES  15 C  542  VAL GLN ASP ASN ILE ALA SER PHE GLY GLY ASN PRO GLY
SEQRES  16 C  542  SER VAL THR ILE PHE GLY GLU SER ALA GLY GLY GLU SER
SEQRES  17 C  542  VAL SER VAL LEU VAL LEU SER PRO LEU ALA LYS ASN LEU
SEQRES  18 C  542  PHE HIS ARG ALA ILE SER GLU SER GLY VAL ALA LEU THR
SEQRES  19 C  542  SER VAL LEU VAL LYS LYS GLY ASP VAL LYS PRO LEU ALA
SEQRES  20 C  542  GLU GLN ILE ALA ILE THR ALA GLY CYS LYS THR THR THR
SEQRES  21 C  542  SER ALA VAL MET VAL HIS CYS LEU ARG GLN LYS THR GLU
SEQRES  22 C  542  GLU GLU LEU LEU GLU THR THR LEU LYS MET LYS PHE LEU
SEQRES  23 C  542  SER LEU ASP LEU GLN GLY ASP PRO ARG GLU SER GLN PRO
SEQRES  24 C  542  LEU LEU GLY THR VAL ILE ASP GLY MET LEU LEU LEU LYS
SEQRES  25 C  542  THR PRO GLU GLU LEU GLN ALA GLU ARG ASN PHE HIS THR
SEQRES  26 C  542  VAL PRO TYR MET VAL GLY ILE ASN LYS GLN GLU PHE GLY
SEQRES  27 C  542  TRP LEU ILE PRO MET LEU MET SER TYR PRO LEU SER GLU
SEQRES  28 C  542  GLY GLN LEU ASP GLN LYS THR ALA MET SER LEU LEU TRP
SEQRES  29 C  542  LYS SER TYR PRO LEU VAL CYS ILE ALA LYS GLU LEU ILE
SEQRES  30 C  542  PRO GLU ALA THR GLU LYS TYR LEU GLY GLY THR ASP ASP
SEQRES  31 C  542  THR VAL LYS LYS LYS ASP LEU PHE LEU ASP LEU ILE ALA
SEQRES  32 C  542  ASP VAL MET PHE GLY VAL PRO SER VAL ILE VAL ALA ARG
SEQRES  33 C  542  ASN HIS ARG ASP ALA GLY ALA PRO THR TYR MET TYR GLU
SEQRES  34 C  542  PHE GLN TYR ARG PRO SER PHE SER SER ASP MET LYS PRO
SEQRES  35 C  542  LYS THR VAL ILE GLY ASP HIS GLY ASP GLU LEU PHE SER
SEQRES  36 C  542  VAL PHE GLY ALA PRO PHE LEU LYS GLU GLY ALA SER GLU
SEQRES  37 C  542  GLU GLU ILE ARG LEU SER LYS MET VAL MET LYS PHE TRP
SEQRES  38 C  542  ALA ASN PHE ALA ARG ASN GLY ASN PRO ASN GLY GLU GLY
SEQRES  39 C  542  LEU PRO HIS TRP PRO GLU TYR ASN GLN LYS GLU GLY TYR
SEQRES  40 C  542  LEU GLN ILE GLY ALA ASN THR GLN ALA ALA GLN LYS LEU
SEQRES  41 C  542  LYS ASP LYS GLU VAL ALA PHE TRP THR ASN LEU PHE ALA
SEQRES  42 C  542  LYS LYS ALA VAL GLU LYS PRO PRO GLN
MODRES 2DQZ ASN A 1079  ASN  GLYCOSYLATION SITE
MODRES 2DQZ ASN B 2079  ASN  GLYCOSYLATION SITE
MODRES 2DQZ ASN C 3079  ASN  GLYCOSYLATION SITE
HET    NAG  A 179      14
HET    SIA    182      21
HET    NAG  B 279      14
HET    SIA    282      21
HET    NAG  C 379      14
HET    SIA    382      21
HET    SO4    184       5
HET    SO4    185       5
HET    SO4    284       5
HET    SO4    285       5
HET    SO4    384       5
HET    SO4    385       5
HET    SO4    286       5
HET      F   4001       1
HET      F   4002       1
HET      F   4003       1
HET    COA      1       7
HET    PLM    111      11
HET    PLM    112      11
HET    PLM    113      11
HET    HTQ     11      20
HET    HTQ     21      20
HET    HTQ     31      40
HETNAM     NAG N-ACETYL-D-GLUCOSAMINE
HETNAM     SIA O-SIALIC ACID
HETNAM     SO4 SULFATE ION
HETNAM       F FLUORIDE ION
HETNAM     COA COENZYME A
HETNAM     PLM PALMITIC ACID
HETNAM     HTQ HOMOTROPINE
HETSYN     NAG NAG
HETSYN     HTQ HYDROXY-PHENYL-ACETIC ACID 8-METHYL-8-AZA-
HETSYN   2 HTQ  BICYCLO[3.2.1]OCT-3-YL ESTER
FORMUL   4  NAG    3(C8 H15 N1 O6)
FORMUL   5  SIA    3(C11 H19 N1 O9)
FORMUL  10  SO4    7(O4 S1 2-)
FORMUL  17    F    3(F1 1-)
FORMUL  20  COA    C21 H36 N7 O16 P3 S1
FORMUL  21  PLM    3(C16 H32 O2)
FORMUL  24  HTQ    3(C16 H21 N1 O3)
FORMUL  27  HOH   *508(H2 O1)
HELIX    1   1 LEU A 1060  ARG A 1064  5                                   5
HELIX    2   2 ASP A 1090  THR A 1102  1                                  13
HELIX    3   3 GLY A 1154  ASN A 1162  1                                   9
HELIX    4   4 LEU A 1172  PHE A 1178  1                                   7
HELIX    5   5 ASN A 1188  ILE A 1205  1                                  18
HELIX    6   6 ALA A 1206  PHE A 1208  5                                   3
HELIX    7   7 SER A 1221  SER A 1233  1                                  13
HELIX    8   8 PRO A 1234  LYS A 1237  5                                   4
HELIX    9   9 THR A 1252  VAL A 1256  5                                   5
HELIX   10  10 VAL A 1261  GLY A 1273  1                                  13
HELIX   11  11 THR A 1278  LYS A 1289  1                                  12
HELIX   12  12 THR A 1290  LYS A 1302  1                                  13
HELIX   13  13 ASP A 1311  SER A 1315  5                                   5
HELIX   14  14 THR A 1331  GLN A 1336  1                                   6
HELIX   15  15 TRP A 1357  SER A 1365  1                                   8
HELIX   16  16 ASP A 1374  SER A 1385  1                                  12
HELIX   17  17 SER A 1385  CYS A 1390  1                                   6
HELIX   18  18 LEU A 1395  GLY A 1405  1                                  11
HELIX   19  19 ASP A 1409  PHE A 1426  1                                  18
HELIX   20  20 PHE A 1426  ALA A 1440  1                                  15
HELIX   21  21 GLU A 1471  PHE A 1476  1                                   6
HELIX   22  22 GLY A 1477  LEU A 1481  5                                   5
HELIX   23  23 SER A 1486  GLY A 1507  1                                  22
HELIX   24  24 LYS A 1540  ALA A 1552  1                                  13
HELIX   25  25 LEU B 2060  ARG B 2064  5                                   5
HELIX   26  26 ASP B 2090  THR B 2102  1                                  13
HELIX   27  27 GLY B 2154  GLU B 2161  1                                   8
HELIX   28  28 LEU B 2172  PHE B 2178  1                                   7
HELIX   29  29 ASN B 2188  ILE B 2205  1                                  18
HELIX   30  30 ALA B 2206  PHE B 2208  5                                   3
HELIX   31  31 SER B 2221  SER B 2233  1                                  13
HELIX   32  32 THR B 2252  VAL B 2256  5                                   5
HELIX   33  33 VAL B 2261  GLY B 2273  1                                  13
HELIX   34  34 THR B 2278  LYS B 2289  1                                  12
HELIX   35  35 THR B 2290  LYS B 2302  1                                  13
HELIX   36  36 ASP B 2311  SER B 2315  5                                   5
HELIX   37  37 THR B 2331  GLU B 2338  1                                   8
HELIX   38  38 TRP B 2357  MET B 2364  1                                   7
HELIX   39  39 ASP B 2374  SER B 2385  1                                  12
HELIX   40  40 SER B 2385  CYS B 2390  1                                   6
HELIX   41  41 LEU B 2395  GLY B 2405  1                                  11
HELIX   42  42 ASP B 2409  PHE B 2426  1                                  18
HELIX   43  43 PHE B 2426  ALA B 2440  1                                  15
HELIX   44  44 GLU B 2471  PHE B 2476  1                                   6
HELIX   45  45 GLY B 2477  LEU B 2481  5                                   5
HELIX   46  46 SER B 2486  GLY B 2507  1                                  22
HELIX   47  47 LYS B 2540  PHE B 2551  1                                  12
HELIX   48  48 LEU C 3060  ARG C 3064  5                                   5
HELIX   49  49 ASP C 3090  THR C 3102  1                                  13
HELIX   50  50 GLY C 3154  ASN C 3162  1                                   9
HELIX   51  51 LEU C 3172  PHE C 3178  1                                   7
HELIX   52  52 ASN C 3188  ILE C 3205  1                                  18
HELIX   53  53 ALA C 3206  PHE C 3208  5                                   3
HELIX   54  54 SER C 3221  SER C 3233  1                                  13
HELIX   55  55 THR C 3252  VAL C 3256  5                                   5
HELIX   56  56 VAL C 3261  ALA C 3272  1                                  12
HELIX   57  57 THR C 3278  LYS C 3289  1                                  12
HELIX   58  58 THR C 3290  LYS C 3302  1                                  13
HELIX   59  59 THR C 3331  GLN C 3336  1                                   6
HELIX   60  60 TRP C 3357  SER C 3365  1                                   8
HELIX   61  61 ASP C 3374  SER C 3385  1                                  12
HELIX   62  62 SER C 3385  CYS C 3390  1                                   6
HELIX   63  63 LEU C 3395  GLY C 3405  1                                  11
HELIX   64  64 ASP C 3409  PHE C 3426  1                                  18
HELIX   65  65 PHE C 3426  ALA C 3440  1                                  15
HELIX   66  66 GLU C 3471  PHE C 3476  1                                   6
HELIX   67  67 GLY C 3477  LEU C 3481  5                                   5
HELIX   68  68 SER C 3486  GLY C 3507  1                                  22
HELIX   69  69 LYS C 3540  LYS C 3553  1                                  14
SHEET    1   A 3 VAL A1025  THR A1028  0
SHEET    2   A 3 GLY A1031  LEU A1034 -1  O  VAL A1033   N  VAL A1026
SHEET    3   A 3 VAL A1077  ASN A1079  1  O  LYS A1078   N  LYS A1032
SHEET    1   B11 LYS A1036  VAL A1038  0
SHEET    2   B11 VAL A1047  PRO A1054 -1  O  ILE A1049   N  LYS A1036
SHEET    3   B11 TYR A1118  THR A1123 -1  O  THR A1123   N  ALA A1048
SHEET    4   B11 VAL A1164  ILE A1168 -1  O  THR A1167   N  ASN A1120
SHEET    5   B11 LEU A1133  ILE A1139  1  N  TRP A1138   O  VAL A1166
SHEET    6   B11 GLY A1210  GLU A1220  1  O  THR A1216   N  VAL A1135
SHEET    7   B11 ARG A1242  GLU A1246  1  O  GLU A1246   N  GLY A1219
SHEET    8   B11 TYR A1346  ASN A1351  1  O  MET A1347   N  ALA A1243
SHEET    9   B11 THR A1444  GLN A1450  1  O  PHE A1449   N  ILE A1350
SHEET   10   B11 GLY A1525  GLY A1530  1  O  ILE A1529   N  GLN A1450
SHEET   11   B11 GLN A1534  GLN A1537 -1  O  GLN A1534   N  GLN A1528
SHEET    1   C 3 VAL B2025  ASP B2027  0
SHEET    2   C 3 LYS B2032  LEU B2034 -1  O  VAL B2033   N  VAL B2026
SHEET    3   C 3 VAL B2077  ASN B2079  1  O  LYS B2078   N  LEU B2034
SHEET    1   D11 LYS B2036  VAL B2038  0
SHEET    2   D11 VAL B2047  PRO B2054 -1  O  VAL B2047   N  VAL B2038
SHEET    3   D11 TYR B2118  THR B2123 -1  O  THR B2123   N  ALA B2048
SHEET    4   D11 VAL B2164  ILE B2168 -1  O  THR B2167   N  ASN B2120
SHEET    5   D11 LEU B2133  ILE B2139  1  N  TRP B2138   O  VAL B2166
SHEET    6   D11 GLY B2210  GLU B2220  1  O  ASN B2211   N  LEU B2133
SHEET    7   D11 ARG B2242  GLU B2246  1  O  ARG B2242   N  ILE B2217
SHEET    8   D11 TYR B2346  ASN B2351  1  O  MET B2347   N  SER B2245
SHEET    9   D11 THR B2444  PHE B2449  1  O  TYR B2445   N  VAL B2348
SHEET   10   D11 GLY B2525  ILE B2529  1  O  LEU B2527   N  GLU B2448
SHEET   11   D11 GLN B2534  GLN B2537 -1  O  ALA B2536   N  TYR B2526
SHEET    1   E 2 MET B2086  CYS B2087  0
SHEET    2   E 2 LEU B2112  SER B2113  1  O  SER B2113   N  MET B2086
SHEET    1   F 3 VAL C3025  THR C3028  0
SHEET    2   F 3 GLY C3031  LEU C3034 -1  O  VAL C3033   N  VAL C3026
SHEET    3   F 3 VAL C3077  ASN C3079  1  O  LYS C3078   N  LEU C3034
SHEET    1   G11 LYS C3036  VAL C3038  0
SHEET    2   G11 VAL C3047  PRO C3054 -1  O  VAL C3047   N  VAL C3038
SHEET    3   G11 TYR C3118  THR C3123 -1  O  THR C3123   N  ALA C3048
SHEET    4   G11 VAL C3164  ILE C3168 -1  O  VAL C3165   N  TYR C3122
SHEET    5   G11 LEU C3133  ILE C3139  1  N  TRP C3138   O  VAL C3166
SHEET    6   G11 GLY C3210  GLU C3220  1  O  THR C3216   N  VAL C3135
SHEET    7   G11 ARG C3242  GLU C3246  1  O  ARG C3242   N  ILE C3217
SHEET    8   G11 TYR C3346  ASN C3351  1  O  MET C3347   N  SER C3245
SHEET    9   G11 THR C3444  PHE C3449  1  O  TYR C3445   N  VAL C3348
SHEET   10   G11 GLY C3525  ILE C3529  1  O  LEU C3527   N  GLU C3448
SHEET   11   G11 GLN C3534  GLN C3537 -1  O  GLN C3534   N  GLN C3528
SHEET    1   H 2 MET C3086  CYS C3087  0
SHEET    2   H 2 LEU C3112  SER C3113  1  O  SER C3113   N  MET C3086
SSBOND   1 CYS A 1087    CYS A 1116
SSBOND   2 CYS A 1274    CYS A 1285
SSBOND   3 CYS B 2087    CYS B 2116
SSBOND   4 CYS B 2274    CYS B 2285
SSBOND   5 CYS C 3087    CYS C 3116
SSBOND   6 CYS C 3274    CYS C 3285
LINK         ND2 ASN A1079                 C1  NAG A 179
LINK         ND2 ASN B2079                 C1  NAG B 279
LINK         ND2 ASN C3079                 C1  NAG C 379
CRYST1   55.564  181.017  202.560  90.00  90.00  90.00 P 21 21 21   12
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      0.017997  0.000000  0.000000        0.00000
SCALE2      0.000000  0.005524  0.000000        0.00000
SCALE3      0.000000  0.000000  0.004937        0.00000
TER    4131      LYS A1553
TER    8262      LYS B2553
TER   12393      LYS C3553
MASTER      355    0   23   69   46    0    0    613161    3  275  126
END