spacer
spacer

PDBsum entry 3gxf

Go to PDB code: 
Top Page protein ligands Protein-protein interface(s) links
Hydrolase PDB id
3gxf
Jmol
Contents
Protein chain
497 a.a.
Ligands
PO4 ×64
NAG ×4
GOL ×5
IFM ×2
Waters ×905
HEADER    HYDROLASE                               02-APR-09   3GXF
TITLE     CRYSTAL STRUCTURE OF ACID-BETA-GLUCOSIDASE WITH ISOFAGOMINE AT NEUTRAL
TITLE    2 PH
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: GLUCOSYLCERAMIDASE;
COMPND   3 CHAIN: A, B, C, D;
COMPND   4 SYNONYM: BETA-GLUCOCEREBROSIDASE, ACID BETA-GLUCOSIDASE, D-GLUCOSYL-
COMPND   5 N-ACYLSPHINGOSINE GLUCOHYDROLASE, ALGLUCERASE, IMIGLUCERASE;
COMPND   6 EC: 3.2.1.45;
COMPND   7 ENGINEERED: YES
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE   3 ORGANISM_COMMON: HUMAN;
SOURCE   4 ORGANISM_TAXID: 9606;
SOURCE   5 GENE: GBA, GC, GLUC;
SOURCE   6 EXPRESSION_SYSTEM: CRICETULUS GRISEUS;
SOURCE   7 EXPRESSION_SYSTEM_COMMON: CHINESE HAMSTER
KEYWDS    HYDROLASE, ALTERNATIVE INITIATION, DISEASE MUTATION, DISULFIDE BOND,
KEYWDS   2 GAUCHER DISEASE, GLYCOPROTEIN, GLYCOSIDASE, ICHTHYOSIS, LIPID
KEYWDS   3 METABOLISM, LYSOSOME, MEMBRANE, SPHINGOLIPID METABOLISM
EXPDTA    X-RAY DIFFRACTION
AUTHOR    R.L.LIEBERMAN
REVDAT   3   13-JUL-11 3GXF    1       VERSN
REVDAT   2   16-JUN-09 3GXF    1       JRNL
REVDAT   1   05-MAY-09 3GXF    0
JRNL        AUTH   R.L.LIEBERMAN,J.A.D'AQUINO,D.RINGE,G.A.PETSKO
JRNL        TITL   EFFECTS OF PH AND IMINOSUGAR PHARMACOLOGICAL CHAPERONES ON
JRNL        TITL 2 LYSOSOMAL GLYCOSIDASE STRUCTURE AND STABILITY.
JRNL        REF    BIOCHEMISTRY                  V.  48  4816 2009
JRNL        REFN                   ISSN 0006-2960
JRNL        PMID   19374450
JRNL        DOI    10.1021/BI9002265
REMARK   2
REMARK   2 RESOLUTION.    2.40 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : REFMAC 5.2.0005
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON
REMARK   3
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK   3
REMARK   3  DATA USED IN REFINEMENT.
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.40
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 32.12
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000
REMARK   3   COMPLETENESS FOR RANGE        (%) : 93.2
REMARK   3   NUMBER OF REFLECTIONS             : 103572
REMARK   3
REMARK   3  FIT TO DATA USED IN REFINEMENT.
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.182
REMARK   3   R VALUE            (WORKING SET) : 0.178
REMARK   3   FREE R VALUE                     : 0.245
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000
REMARK   3   FREE R VALUE TEST SET COUNT      : 5209
REMARK   3
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.
REMARK   3   TOTAL NUMBER OF BINS USED           : 20
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.40
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.46
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 5942
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 76.90
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2380
REMARK   3   BIN FREE R VALUE SET COUNT          : 327
REMARK   3   BIN FREE R VALUE                    : 0.3060
REMARK   3
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK   3   PROTEIN ATOMS            : 15720
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 426
REMARK   3   SOLVENT ATOMS            : 905
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : NULL
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 27.27
REMARK   3   OVERALL ANISOTROPIC B VALUE.
REMARK   3    B11 (A**2) : 0.20000
REMARK   3    B22 (A**2) : -0.18000
REMARK   3    B33 (A**2) : -0.14000
REMARK   3    B12 (A**2) : 0.00000
REMARK   3    B13 (A**2) : -0.17000
REMARK   3    B23 (A**2) : 0.00000
REMARK   3
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.
REMARK   3   ESU BASED ON R VALUE                            (A): 0.336
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.255
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.178
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 7.687
REMARK   3
REMARK   3 CORRELATION COEFFICIENTS.
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.947
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.902
REMARK   3
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT
REMARK   3   BOND LENGTHS REFINED ATOMS        (A): 16573 ; 0.020 ; 0.022
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 22635 ; 1.957 ; 1.970
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):  1984 ; 8.265 ; 5.000
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   720 ;37.898 ;23.444
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  2516 ;17.889 ;15.000
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    84 ;20.705 ;15.000
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  2418 ; 0.134 ; 0.200
REMARK   3   GENERAL PLANES REFINED ATOMS      (A): 12532 ; 0.008 ; 0.020
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  8179 ; 0.229 ; 0.200
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A): 10812 ; 0.313 ; 0.200
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  1107 ; 0.335 ; 0.200
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):    67 ; 0.198 ; 0.200
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    16 ; 0.184 ; 0.200
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL
REMARK   3
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2): 10183 ; 0.978 ; 1.500
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 16072 ; 1.659 ; 2.000
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  7325 ; 2.398 ; 3.000
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  6563 ; 3.684 ; 4.500
REMARK   3
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL
REMARK   3
REMARK   3  NCS RESTRAINTS STATISTICS
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : 2
REMARK   3
REMARK   3  NCS GROUP NUMBER               : 1
REMARK   3     CHAIN NAMES                    : A C
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 1
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE
REMARK   3           1     A      1       A     497      4
REMARK   3           1     C      1       C     497      4
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT
REMARK   3   MEDIUM POSITIONAL  1    A    (A):   3930 ; 0.270 ; 0.500
REMARK   3   MEDIUM THERMAL     1    A (A**2):   3930 ; 0.750 ; 2.000
REMARK   3
REMARK   3  NCS GROUP NUMBER               : 2
REMARK   3     CHAIN NAMES                    : B D
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 1
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE
REMARK   3           1     B      1       B     497      4
REMARK   3           1     D      1       D     497      4
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT
REMARK   3   MEDIUM POSITIONAL  2    B    (A):   3930 ; 0.250 ; 0.500
REMARK   3   MEDIUM THERMAL     2    B (A**2):   3930 ; 0.770 ; 2.000
REMARK   3
REMARK   3  TLS DETAILS
REMARK   3   NUMBER OF TLS GROUPS  : NULL
REMARK   3
REMARK   3  BULK SOLVENT MODELLING.
REMARK   3   METHOD USED : MASK
REMARK   3   PARAMETERS FOR MASK CALCULATION
REMARK   3   VDW PROBE RADIUS   : 1.20
REMARK   3   ION PROBE RADIUS   : 0.80
REMARK   3   SHRINKAGE RADIUS   : 0.80
REMARK   3
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK   3  POSITIONS
REMARK   4
REMARK   4 3GXF COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 20-APR-09.
REMARK 100 THE RCSB ID CODE IS RCSB052426.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : NULL
REMARK 200  TEMPERATURE           (KELVIN) : NULL
REMARK 200  PH                             : 7.5
REMARK 200  NUMBER OF CRYSTALS USED        : 1
REMARK 200
REMARK 200  SYNCHROTRON              (Y/N) : Y
REMARK 200  RADIATION SOURCE               : APS
REMARK 200  BEAMLINE                       : 23-ID-D
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                  : NULL
REMARK 200  DETECTOR MANUFACTURER          : NULL
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL
REMARK 200  DATA SCALING SOFTWARE          : HKL
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 103572
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.400
REMARK 200  RESOLUTION RANGE LOW       (A) : 32.120
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : NULL
REMARK 200  DATA REDUNDANCY                : NULL
REMARK 200  R MERGE                    (I) : NULL
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) : NULL
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : NULL
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL
REMARK 200  R MERGE FOR SHELL          (I) : NULL
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: NULL
REMARK 200 SOFTWARE USED: NULL
REMARK 200 STARTING MODEL: PDB ENTRY '2NSX
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 62.02
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.24
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.8 M NAH2PO4, 0.8 M KH2PO4, 0.1 M
REMARK 280  HEPES PH 7.5, SOAK WITH 500UM ISOFAGOMINE FOR 10 MIN, GLYCEROL IN
REMARK 280  CRYO, VAPOR DIFFUSION, TEMPERATURE 298K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290      SYMOP   SYMMETRY
REMARK 290     NNNMMM   OPERATOR
REMARK 290       1555   X,Y,Z
REMARK 290       2555   -X,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        0.00000
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000       46.00650
REMARK 290   SMTRY3   2  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 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: TETRAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 20880 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 67580 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -349.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 19010 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 69450 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -341.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D
REMARK 350   BIOMT1   2  1.000000  0.000000  0.000000        0.00000
REMARK 350   BIOMT2   2  0.000000  1.000000  0.000000       92.01300
REMARK 350   BIOMT3   2  0.000000  0.000000  1.000000        0.00000
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   OE1  GLN D   226     O1   PO4 D   501              1.98
REMARK 500   NE2  GLN B   207     OD1  ASP B   263              2.03
REMARK 500   NE2  GLN A   207     OD1  ASP A   263              2.05
REMARK 500   O4   PO4 B   499     O    HOH B   522              2.06
REMARK 500   OG   SER B    12     O1   PO4 B   498              2.09
REMARK 500   CD   ARG A    44     O2   PO4 A   501              2.13
REMARK 500   O    PHE C    31     O    HOH C   592              2.14
REMARK 500   N    ASN B   333     O2   PO4 B   506              2.19
REMARK 500
REMARK 500 REMARK: NULL
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 PROTEIN: 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    GLY A 243   N   -  CA  -  C   ANGL. DEV. = -18.2 DEGREES
REMARK 500    LEU A 317   CA  -  CB  -  CG  ANGL. DEV. =  17.4 DEGREES
REMARK 500    GLY B  62   N   -  CA  -  C   ANGL. DEV. = -17.8 DEGREES
REMARK 500    LEU B 286   CA  -  CB  -  CG  ANGL. DEV. =  17.7 DEGREES
REMARK 500    LEU B 317   CA  -  CB  -  CG  ANGL. DEV. =  15.1 DEGREES
REMARK 500    ARG C   2   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.9 DEGREES
REMARK 500    LEU C 286   CA  -  CB  -  CG  ANGL. DEV. =  17.2 DEGREES
REMARK 500    ARG D  39   NE  -  CZ  -  NH1 ANGL. DEV. =   4.6 DEGREES
REMARK 500    ARG D  39   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.8 DEGREES
REMARK 500    ARG D  47   NE  -  CZ  -  NH1 ANGL. DEV. =   3.5 DEGREES
REMARK 500    VAL D 343   N   -  CA  -  C   ANGL. DEV. =  19.0 DEGREES
REMARK 500    GLY D 344   N   -  CA  -  C   ANGL. DEV. = -15.7 DEGREES
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    ASN A  19     -159.49   -148.66
REMARK 500    ALA A  33      161.99    -49.93
REMARK 500    MET A  49       55.24     31.77
REMARK 500    PHE A  75     -138.66   -117.87
REMARK 500    ALA A 124     -162.17     65.56
REMARK 500    ALA A 136       63.95   -152.69
REMARK 500    PRO A 150     -157.27    -73.63
REMARK 500    LEU A 156      -67.12    -99.87
REMARK 500    ASN A 192     -161.31   -117.92
REMARK 500    ASP A 203     -172.52    -69.74
REMARK 500    GLU A 233      132.16    151.29
REMARK 500    SER A 242     -113.30     60.00
REMARK 500    ASP A 263      -60.95   -125.04
REMARK 500    LEU A 281      -89.47     63.67
REMARK 500    TRP A 312      -62.70   -105.56
REMARK 500    TYR A 313       60.88     31.97
REMARK 500    LEU A 314      -13.02    136.67
REMARK 500    PHE A 316     -133.10    154.62
REMARK 500    LEU A 317      162.98    -36.33
REMARK 500    ALA A 318      159.86    -39.55
REMARK 500    THR A 323      -72.43   -102.45
REMARK 500    LYS A 346       63.05    144.65
REMARK 500    TRP A 381     -139.27    -83.15
REMARK 500    ARG A 395      140.95   -179.47
REMARK 500    PHE A 397       -2.80   -145.97
REMARK 500    VAL A 477      -46.33   -133.85
REMARK 500    SER B  12      -13.85    -49.76
REMARK 500    MET B  49       60.72     30.54
REMARK 500    THR B  63      -33.62     94.90
REMARK 500    GLN B  70       78.09   -118.09
REMARK 500    PHE B  75     -138.53   -124.89
REMARK 500    ALA B 124     -149.98     67.37
REMARK 500    CYS B 126     -156.52   -132.64
REMARK 500    TYR B 133      148.50    177.51
REMARK 500    LEU B 156      -71.80   -107.65
REMARK 500    ASN B 192     -167.93   -116.87
REMARK 500    PRO B 201      134.53    -38.81
REMARK 500    GLU B 233      133.84    166.86
REMARK 500    GLU B 235       67.06     39.02
REMARK 500    PHE B 246     -167.74   -125.44
REMARK 500    LEU B 281      -89.54     70.31
REMARK 500    LEU B 287       -4.31    -56.96
REMARK 500    THR B 323      -73.71   -102.84
REMARK 500    TRP B 348      -80.35     76.65
REMARK 500    SER B 351      -67.67    -93.48
REMARK 500    HIS B 374       -3.38     87.89
REMARK 500    TRP B 381     -139.97    -84.93
REMARK 500    ASP B 409       38.26     39.83
REMARK 500    PHE B 423      -60.33   -107.69
REMARK 500    LEU B 436       97.49   -162.76
REMARK 500
REMARK 500 THIS ENTRY HAS      98 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION.  CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS.  TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500                                 MODEL     OMEGA
REMARK 500 LEU A  241     SER A  242                  149.15
REMARK 500 ASP A  315     PHE A  316                  -42.76
REMARK 500 TYR C  313     LEU C  314                  -34.91
REMARK 500 LEU C  314     ASP C  315                  147.63
REMARK 500 PHE C  316     LEU C  317                  -45.40
REMARK 500 GLY C  344     SER C  345                  147.51
REMARK 500 CYS D  342     VAL D  343                  101.75
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CHIRAL CENTERS
REMARK 500
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY
REMARK 500 FOR AMINO ACIDS AND C1'--O4'--N1(N9)--C2' FOR
REMARK 500 NUCLEIC ACIDS OR EQUIVALENT ANGLE
REMARK 500 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,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)
REMARK 500
REMARK 500  M RES CSSEQI    IMPROPER   EXPECTED   FOUND DETAILS
REMARK 500    PHE A 246        24.3      L          L   OUTSIDE RANGE
REMARK 500    ASP A 315        20.3      L          L   OUTSIDE RANGE
REMARK 500    PHE A 316        19.6      L          L   OUTSIDE RANGE
REMARK 500    LEU A 317        19.1      L          L   OUTSIDE RANGE
REMARK 500    VAL A 398        24.2      L          L   OUTSIDE RANGE
REMARK 500    THR A 410        24.6      L          L   OUTSIDE RANGE
REMARK 500    THR B  63        21.6      L          L   OUTSIDE RANGE
REMARK 500    PHE B 347        20.8      L          L   OUTSIDE RANGE
REMARK 500    ILE D  93        22.0      L          L   OUTSIDE RANGE
REMARK 500    TYR D 313        24.6      L          L   OUTSIDE RANGE
REMARK 500    VAL D 343        21.0      L          L   OUTSIDE RANGE
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 PO4 A 498
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 A 499
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 A 500
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 A 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 A 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 A 503
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 A 504
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 A 505
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 A 506
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 A 507
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 A 508
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 A 509
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 A 510
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 A 511
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 A 512
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 A 513
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 A 514
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 A 515
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 516
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 517
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 518
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 B 498
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 B 499
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 B 500
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 B 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 B 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 B 503
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 B 504
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 B 505
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 B 506
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 B 507
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 B 508
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 B 509
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 B 510
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 B 511
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 B 512
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 B 513
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 B 514
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 B 515
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 516
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IFM B 517
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 518
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 519
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 C 498
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 C 499
REMARK 800
REMARK 800 SITE_IDENTIFIER: FC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 C 500
REMARK 800
REMARK 800 SITE_IDENTIFIER: FC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 C 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: FC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 C 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: FC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 C 503
REMARK 800
REMARK 800 SITE_IDENTIFIER: FC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 C 504
REMARK 800
REMARK 800 SITE_IDENTIFIER: FC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 C 505
REMARK 800
REMARK 800 SITE_IDENTIFIER: FC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 C 506
REMARK 800
REMARK 800 SITE_IDENTIFIER: FC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 C 507
REMARK 800
REMARK 800 SITE_IDENTIFIER: FC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 C 508
REMARK 800
REMARK 800 SITE_IDENTIFIER: GC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 C 509
REMARK 800
REMARK 800 SITE_IDENTIFIER: GC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 C 510
REMARK 800
REMARK 800 SITE_IDENTIFIER: GC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 C 511
REMARK 800
REMARK 800 SITE_IDENTIFIER: GC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 C 512
REMARK 800
REMARK 800 SITE_IDENTIFIER: GC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG C 513
REMARK 800
REMARK 800 SITE_IDENTIFIER: GC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL C 514
REMARK 800
REMARK 800 SITE_IDENTIFIER: GC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 D 498
REMARK 800
REMARK 800 SITE_IDENTIFIER: GC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 D 499
REMARK 800
REMARK 800 SITE_IDENTIFIER: GC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 D 500
REMARK 800
REMARK 800 SITE_IDENTIFIER: HC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 D 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: HC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 D 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: HC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 D 503
REMARK 800
REMARK 800 SITE_IDENTIFIER: HC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 D 504
REMARK 800
REMARK 800 SITE_IDENTIFIER: HC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 D 505
REMARK 800
REMARK 800 SITE_IDENTIFIER: HC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 D 506
REMARK 800
REMARK 800 SITE_IDENTIFIER: HC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 D 507
REMARK 800
REMARK 800 SITE_IDENTIFIER: HC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 D 508
REMARK 800
REMARK 800 SITE_IDENTIFIER: HC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 D 509
REMARK 800
REMARK 800 SITE_IDENTIFIER: IC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 D 510
REMARK 800
REMARK 800 SITE_IDENTIFIER: IC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG D 511
REMARK 800
REMARK 800 SITE_IDENTIFIER: IC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IFM D 512
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3GXM   RELATED DB: PDB
REMARK 900 STRUCTURE OF ACID-BETA-GLUCOSIDASE AT PH 4.5
REMARK 900 RELATED ID: 3GXI   RELATED DB: PDB
REMARK 900 STRUCTURE OF ACID-BETA-GLUCOSIDASE AT PH 5.5
DBREF  3GXF A    1   497  UNP    P04062   GLCM_HUMAN      40    536
DBREF  3GXF B    1   497  UNP    P04062   GLCM_HUMAN      40    536
DBREF  3GXF C    1   497  UNP    P04062   GLCM_HUMAN      40    536
DBREF  3GXF D    1   497  UNP    P04062   GLCM_HUMAN      40    536
SEQADV 3GXF HIS A  495  UNP  P04062    ARG   534 VARIANT
SEQADV 3GXF HIS B  495  UNP  P04062    ARG   534 VARIANT
SEQADV 3GXF HIS C  495  UNP  P04062    ARG   534 VARIANT
SEQADV 3GXF HIS D  495  UNP  P04062    ARG   534 VARIANT
SEQRES   1 A  497  ALA ARG PRO CYS ILE PRO LYS SER PHE GLY TYR SER SER
SEQRES   2 A  497  VAL VAL CYS VAL CYS ASN ALA THR TYR CYS ASP SER PHE
SEQRES   3 A  497  ASP PRO PRO THR PHE PRO ALA LEU GLY THR PHE SER ARG
SEQRES   4 A  497  TYR GLU SER THR ARG SER GLY ARG ARG MET GLU LEU SER
SEQRES   5 A  497  MET GLY PRO ILE GLN ALA ASN HIS THR GLY THR GLY LEU
SEQRES   6 A  497  LEU LEU THR LEU GLN PRO GLU GLN LYS PHE GLN LYS VAL
SEQRES   7 A  497  LYS GLY PHE GLY GLY ALA MET THR ASP ALA ALA ALA LEU
SEQRES   8 A  497  ASN ILE LEU ALA LEU SER PRO PRO ALA GLN ASN LEU LEU
SEQRES   9 A  497  LEU LYS SER TYR PHE SER GLU GLU GLY ILE GLY TYR ASN
SEQRES  10 A  497  ILE ILE ARG VAL PRO MET ALA SER CYS ASP PHE SER ILE
SEQRES  11 A  497  ARG THR TYR THR TYR ALA ASP THR PRO ASP ASP PHE GLN
SEQRES  12 A  497  LEU HIS ASN PHE SER LEU PRO GLU GLU ASP THR LYS LEU
SEQRES  13 A  497  LYS ILE PRO LEU ILE HIS ARG ALA LEU GLN LEU ALA GLN
SEQRES  14 A  497  ARG PRO VAL SER LEU LEU ALA SER PRO TRP THR SER PRO
SEQRES  15 A  497  THR TRP LEU LYS THR ASN GLY ALA VAL ASN GLY LYS GLY
SEQRES  16 A  497  SER LEU LYS GLY GLN PRO GLY ASP ILE TYR HIS GLN THR
SEQRES  17 A  497  TRP ALA ARG TYR PHE VAL LYS PHE LEU ASP ALA TYR ALA
SEQRES  18 A  497  GLU HIS LYS LEU GLN PHE TRP ALA VAL THR ALA GLU ASN
SEQRES  19 A  497  GLU PRO SER ALA GLY LEU LEU SER GLY TYR PRO PHE GLN
SEQRES  20 A  497  CYS LEU GLY PHE THR PRO GLU HIS GLN ARG ASP PHE ILE
SEQRES  21 A  497  ALA ARG ASP LEU GLY PRO THR LEU ALA ASN SER THR HIS
SEQRES  22 A  497  HIS ASN VAL ARG LEU LEU MET LEU ASP ASP GLN ARG LEU
SEQRES  23 A  497  LEU LEU PRO HIS TRP ALA LYS VAL VAL LEU THR ASP PRO
SEQRES  24 A  497  GLU ALA ALA LYS TYR VAL HIS GLY ILE ALA VAL HIS TRP
SEQRES  25 A  497  TYR LEU ASP PHE LEU ALA PRO ALA LYS ALA THR LEU GLY
SEQRES  26 A  497  GLU THR HIS ARG LEU PHE PRO ASN THR MET LEU PHE ALA
SEQRES  27 A  497  SER GLU ALA CYS VAL GLY SER LYS PHE TRP GLU GLN SER
SEQRES  28 A  497  VAL ARG LEU GLY SER TRP ASP ARG GLY MET GLN TYR SER
SEQRES  29 A  497  HIS SER ILE ILE THR ASN LEU LEU TYR HIS VAL VAL GLY
SEQRES  30 A  497  TRP THR ASP TRP ASN LEU ALA LEU ASN PRO GLU GLY GLY
SEQRES  31 A  497  PRO ASN TRP VAL ARG ASN PHE VAL ASP SER PRO ILE ILE
SEQRES  32 A  497  VAL ASP ILE THR LYS ASP THR PHE TYR LYS GLN PRO MET
SEQRES  33 A  497  PHE TYR HIS LEU GLY HIS PHE SER LYS PHE ILE PRO GLU
SEQRES  34 A  497  GLY SER GLN ARG VAL GLY LEU VAL ALA SER GLN LYS ASN
SEQRES  35 A  497  ASP LEU ASP ALA VAL ALA LEU MET HIS PRO ASP GLY SER
SEQRES  36 A  497  ALA VAL VAL VAL VAL LEU ASN ARG SER SER LYS ASP VAL
SEQRES  37 A  497  PRO LEU THR ILE LYS ASP PRO ALA VAL GLY PHE LEU GLU
SEQRES  38 A  497  THR ILE SER PRO GLY TYR SER ILE HIS THR TYR LEU TRP
SEQRES  39 A  497  HIS ARG GLN
SEQRES   1 B  497  ALA ARG PRO CYS ILE PRO LYS SER PHE GLY TYR SER SER
SEQRES   2 B  497  VAL VAL CYS VAL CYS ASN ALA THR TYR CYS ASP SER PHE
SEQRES   3 B  497  ASP PRO PRO THR PHE PRO ALA LEU GLY THR PHE SER ARG
SEQRES   4 B  497  TYR GLU SER THR ARG SER GLY ARG ARG MET GLU LEU SER
SEQRES   5 B  497  MET GLY PRO ILE GLN ALA ASN HIS THR GLY THR GLY LEU
SEQRES   6 B  497  LEU LEU THR LEU GLN PRO GLU GLN LYS PHE GLN LYS VAL
SEQRES   7 B  497  LYS GLY PHE GLY GLY ALA MET THR ASP ALA ALA ALA LEU
SEQRES   8 B  497  ASN ILE LEU ALA LEU SER PRO PRO ALA GLN ASN LEU LEU
SEQRES   9 B  497  LEU LYS SER TYR PHE SER GLU GLU GLY ILE GLY TYR ASN
SEQRES  10 B  497  ILE ILE ARG VAL PRO MET ALA SER CYS ASP PHE SER ILE
SEQRES  11 B  497  ARG THR TYR THR TYR ALA ASP THR PRO ASP ASP PHE GLN
SEQRES  12 B  497  LEU HIS ASN PHE SER LEU PRO GLU GLU ASP THR LYS LEU
SEQRES  13 B  497  LYS ILE PRO LEU ILE HIS ARG ALA LEU GLN LEU ALA GLN
SEQRES  14 B  497  ARG PRO VAL SER LEU LEU ALA SER PRO TRP THR SER PRO
SEQRES  15 B  497  THR TRP LEU LYS THR ASN GLY ALA VAL ASN GLY LYS GLY
SEQRES  16 B  497  SER LEU LYS GLY GLN PRO GLY ASP ILE TYR HIS GLN THR
SEQRES  17 B  497  TRP ALA ARG TYR PHE VAL LYS PHE LEU ASP ALA TYR ALA
SEQRES  18 B  497  GLU HIS LYS LEU GLN PHE TRP ALA VAL THR ALA GLU ASN
SEQRES  19 B  497  GLU PRO SER ALA GLY LEU LEU SER GLY TYR PRO PHE GLN
SEQRES  20 B  497  CYS LEU GLY PHE THR PRO GLU HIS GLN ARG ASP PHE ILE
SEQRES  21 B  497  ALA ARG ASP LEU GLY PRO THR LEU ALA ASN SER THR HIS
SEQRES  22 B  497  HIS ASN VAL ARG LEU LEU MET LEU ASP ASP GLN ARG LEU
SEQRES  23 B  497  LEU LEU PRO HIS TRP ALA LYS VAL VAL LEU THR ASP PRO
SEQRES  24 B  497  GLU ALA ALA LYS TYR VAL HIS GLY ILE ALA VAL HIS TRP
SEQRES  25 B  497  TYR LEU ASP PHE LEU ALA PRO ALA LYS ALA THR LEU GLY
SEQRES  26 B  497  GLU THR HIS ARG LEU PHE PRO ASN THR MET LEU PHE ALA
SEQRES  27 B  497  SER GLU ALA CYS VAL GLY SER LYS PHE TRP GLU GLN SER
SEQRES  28 B  497  VAL ARG LEU GLY SER TRP ASP ARG GLY MET GLN TYR SER
SEQRES  29 B  497  HIS SER ILE ILE THR ASN LEU LEU TYR HIS VAL VAL GLY
SEQRES  30 B  497  TRP THR ASP TRP ASN LEU ALA LEU ASN PRO GLU GLY GLY
SEQRES  31 B  497  PRO ASN TRP VAL ARG ASN PHE VAL ASP SER PRO ILE ILE
SEQRES  32 B  497  VAL ASP ILE THR LYS ASP THR PHE TYR LYS GLN PRO MET
SEQRES  33 B  497  PHE TYR HIS LEU GLY HIS PHE SER LYS PHE ILE PRO GLU
SEQRES  34 B  497  GLY SER GLN ARG VAL GLY LEU VAL ALA SER GLN LYS ASN
SEQRES  35 B  497  ASP LEU ASP ALA VAL ALA LEU MET HIS PRO ASP GLY SER
SEQRES  36 B  497  ALA VAL VAL VAL VAL LEU ASN ARG SER SER LYS ASP VAL
SEQRES  37 B  497  PRO LEU THR ILE LYS ASP PRO ALA VAL GLY PHE LEU GLU
SEQRES  38 B  497  THR ILE SER PRO GLY TYR SER ILE HIS THR TYR LEU TRP
SEQRES  39 B  497  HIS ARG GLN
SEQRES   1 C  497  ALA ARG PRO CYS ILE PRO LYS SER PHE GLY TYR SER SER
SEQRES   2 C  497  VAL VAL CYS VAL CYS ASN ALA THR TYR CYS ASP SER PHE
SEQRES   3 C  497  ASP PRO PRO THR PHE PRO ALA LEU GLY THR PHE SER ARG
SEQRES   4 C  497  TYR GLU SER THR ARG SER GLY ARG ARG MET GLU LEU SER
SEQRES   5 C  497  MET GLY PRO ILE GLN ALA ASN HIS THR GLY THR GLY LEU
SEQRES   6 C  497  LEU LEU THR LEU GLN PRO GLU GLN LYS PHE GLN LYS VAL
SEQRES   7 C  497  LYS GLY PHE GLY GLY ALA MET THR ASP ALA ALA ALA LEU
SEQRES   8 C  497  ASN ILE LEU ALA LEU SER PRO PRO ALA GLN ASN LEU LEU
SEQRES   9 C  497  LEU LYS SER TYR PHE SER GLU GLU GLY ILE GLY TYR ASN
SEQRES  10 C  497  ILE ILE ARG VAL PRO MET ALA SER CYS ASP PHE SER ILE
SEQRES  11 C  497  ARG THR TYR THR TYR ALA ASP THR PRO ASP ASP PHE GLN
SEQRES  12 C  497  LEU HIS ASN PHE SER LEU PRO GLU GLU ASP THR LYS LEU
SEQRES  13 C  497  LYS ILE PRO LEU ILE HIS ARG ALA LEU GLN LEU ALA GLN
SEQRES  14 C  497  ARG PRO VAL SER LEU LEU ALA SER PRO TRP THR SER PRO
SEQRES  15 C  497  THR TRP LEU LYS THR ASN GLY ALA VAL ASN GLY LYS GLY
SEQRES  16 C  497  SER LEU LYS GLY GLN PRO GLY ASP ILE TYR HIS GLN THR
SEQRES  17 C  497  TRP ALA ARG TYR PHE VAL LYS PHE LEU ASP ALA TYR ALA
SEQRES  18 C  497  GLU HIS LYS LEU GLN PHE TRP ALA VAL THR ALA GLU ASN
SEQRES  19 C  497  GLU PRO SER ALA GLY LEU LEU SER GLY TYR PRO PHE GLN
SEQRES  20 C  497  CYS LEU GLY PHE THR PRO GLU HIS GLN ARG ASP PHE ILE
SEQRES  21 C  497  ALA ARG ASP LEU GLY PRO THR LEU ALA ASN SER THR HIS
SEQRES  22 C  497  HIS ASN VAL ARG LEU LEU MET LEU ASP ASP GLN ARG LEU
SEQRES  23 C  497  LEU LEU PRO HIS TRP ALA LYS VAL VAL LEU THR ASP PRO
SEQRES  24 C  497  GLU ALA ALA LYS TYR VAL HIS GLY ILE ALA VAL HIS TRP
SEQRES  25 C  497  TYR LEU ASP PHE LEU ALA PRO ALA LYS ALA THR LEU GLY
SEQRES  26 C  497  GLU THR HIS ARG LEU PHE PRO ASN THR MET LEU PHE ALA
SEQRES  27 C  497  SER GLU ALA CYS VAL GLY SER LYS PHE TRP GLU GLN SER
SEQRES  28 C  497  VAL ARG LEU GLY SER TRP ASP ARG GLY MET GLN TYR SER
SEQRES  29 C  497  HIS SER ILE ILE THR ASN LEU LEU TYR HIS VAL VAL GLY
SEQRES  30 C  497  TRP THR ASP TRP ASN LEU ALA LEU ASN PRO GLU GLY GLY
SEQRES  31 C  497  PRO ASN TRP VAL ARG ASN PHE VAL ASP SER PRO ILE ILE
SEQRES  32 C  497  VAL ASP ILE THR LYS ASP THR PHE TYR LYS GLN PRO MET
SEQRES  33 C  497  PHE TYR HIS LEU GLY HIS PHE SER LYS PHE ILE PRO GLU
SEQRES  34 C  497  GLY SER GLN ARG VAL GLY LEU VAL ALA SER GLN LYS ASN
SEQRES  35 C  497  ASP LEU ASP ALA VAL ALA LEU MET HIS PRO ASP GLY SER
SEQRES  36 C  497  ALA VAL VAL VAL VAL LEU ASN ARG SER SER LYS ASP VAL
SEQRES  37 C  497  PRO LEU THR ILE LYS ASP PRO ALA VAL GLY PHE LEU GLU
SEQRES  38 C  497  THR ILE SER PRO GLY TYR SER ILE HIS THR TYR LEU TRP
SEQRES  39 C  497  HIS ARG GLN
SEQRES   1 D  497  ALA ARG PRO CYS ILE PRO LYS SER PHE GLY TYR SER SER
SEQRES   2 D  497  VAL VAL CYS VAL CYS ASN ALA THR TYR CYS ASP SER PHE
SEQRES   3 D  497  ASP PRO PRO THR PHE PRO ALA LEU GLY THR PHE SER ARG
SEQRES   4 D  497  TYR GLU SER THR ARG SER GLY ARG ARG MET GLU LEU SER
SEQRES   5 D  497  MET GLY PRO ILE GLN ALA ASN HIS THR GLY THR GLY LEU
SEQRES   6 D  497  LEU LEU THR LEU GLN PRO GLU GLN LYS PHE GLN LYS VAL
SEQRES   7 D  497  LYS GLY PHE GLY GLY ALA MET THR ASP ALA ALA ALA LEU
SEQRES   8 D  497  ASN ILE LEU ALA LEU SER PRO PRO ALA GLN ASN LEU LEU
SEQRES   9 D  497  LEU LYS SER TYR PHE SER GLU GLU GLY ILE GLY TYR ASN
SEQRES  10 D  497  ILE ILE ARG VAL PRO MET ALA SER CYS ASP PHE SER ILE
SEQRES  11 D  497  ARG THR TYR THR TYR ALA ASP THR PRO ASP ASP PHE GLN
SEQRES  12 D  497  LEU HIS ASN PHE SER LEU PRO GLU GLU ASP THR LYS LEU
SEQRES  13 D  497  LYS ILE PRO LEU ILE HIS ARG ALA LEU GLN LEU ALA GLN
SEQRES  14 D  497  ARG PRO VAL SER LEU LEU ALA SER PRO TRP THR SER PRO
SEQRES  15 D  497  THR TRP LEU LYS THR ASN GLY ALA VAL ASN GLY LYS GLY
SEQRES  16 D  497  SER LEU LYS GLY GLN PRO GLY ASP ILE TYR HIS GLN THR
SEQRES  17 D  497  TRP ALA ARG TYR PHE VAL LYS PHE LEU ASP ALA TYR ALA
SEQRES  18 D  497  GLU HIS LYS LEU GLN PHE TRP ALA VAL THR ALA GLU ASN
SEQRES  19 D  497  GLU PRO SER ALA GLY LEU LEU SER GLY TYR PRO PHE GLN
SEQRES  20 D  497  CYS LEU GLY PHE THR PRO GLU HIS GLN ARG ASP PHE ILE
SEQRES  21 D  497  ALA ARG ASP LEU GLY PRO THR LEU ALA ASN SER THR HIS
SEQRES  22 D  497  HIS ASN VAL ARG LEU LEU MET LEU ASP ASP GLN ARG LEU
SEQRES  23 D  497  LEU LEU PRO HIS TRP ALA LYS VAL VAL LEU THR ASP PRO
SEQRES  24 D  497  GLU ALA ALA LYS TYR VAL HIS GLY ILE ALA VAL HIS TRP
SEQRES  25 D  497  TYR LEU ASP PHE LEU ALA PRO ALA LYS ALA THR LEU GLY
SEQRES  26 D  497  GLU THR HIS ARG LEU PHE PRO ASN THR MET LEU PHE ALA
SEQRES  27 D  497  SER GLU ALA CYS VAL GLY SER LYS PHE TRP GLU GLN SER
SEQRES  28 D  497  VAL ARG LEU GLY SER TRP ASP ARG GLY MET GLN TYR SER
SEQRES  29 D  497  HIS SER ILE ILE THR ASN LEU LEU TYR HIS VAL VAL GLY
SEQRES  30 D  497  TRP THR ASP TRP ASN LEU ALA LEU ASN PRO GLU GLY GLY
SEQRES  31 D  497  PRO ASN TRP VAL ARG ASN PHE VAL ASP SER PRO ILE ILE
SEQRES  32 D  497  VAL ASP ILE THR LYS ASP THR PHE TYR LYS GLN PRO MET
SEQRES  33 D  497  PHE TYR HIS LEU GLY HIS PHE SER LYS PHE ILE PRO GLU
SEQRES  34 D  497  GLY SER GLN ARG VAL GLY LEU VAL ALA SER GLN LYS ASN
SEQRES  35 D  497  ASP LEU ASP ALA VAL ALA LEU MET HIS PRO ASP GLY SER
SEQRES  36 D  497  ALA VAL VAL VAL VAL LEU ASN ARG SER SER LYS ASP VAL
SEQRES  37 D  497  PRO LEU THR ILE LYS ASP PRO ALA VAL GLY PHE LEU GLU
SEQRES  38 D  497  THR ILE SER PRO GLY TYR SER ILE HIS THR TYR LEU TRP
SEQRES  39 D  497  HIS ARG GLN
MODRES 3GXF ASN A   19  ASN  GLYCOSYLATION SITE
MODRES 3GXF ASN B   19  ASN  GLYCOSYLATION SITE
MODRES 3GXF ASN C   19  ASN  GLYCOSYLATION SITE
MODRES 3GXF ASN D   19  ASN  GLYCOSYLATION SITE
HET    PO4  A 498       5
HET    PO4  A 499       5
HET    PO4  A 500       5
HET    PO4  A 501       5
HET    PO4  A 502       5
HET    PO4  A 503       5
HET    PO4  A 504       5
HET    PO4  A 505       5
HET    PO4  A 506       5
HET    PO4  A 507       5
HET    PO4  A 508       5
HET    PO4  A 509       5
HET    PO4  A 510       5
HET    PO4  A 511       5
HET    PO4  A 512       5
HET    PO4  A 513       5
HET    PO4  A 514       5
HET    PO4  A 515       5
HET    NAG  A 516      14
HET    GOL  A 517       6
HET    GOL  A 518       6
HET    PO4  B 498       5
HET    PO4  B 499       5
HET    PO4  B 500       5
HET    PO4  B 501       5
HET    PO4  B 502       5
HET    PO4  B 503       5
HET    PO4  B 504       5
HET    PO4  B 505       5
HET    PO4  B 506       5
HET    PO4  B 507       5
HET    PO4  B 508       5
HET    PO4  B 509       5
HET    PO4  B 510       5
HET    PO4  B 511       5
HET    PO4  B 512       5
HET    PO4  B 513       5
HET    PO4  B 514       5
HET    PO4  B 515       5
HET    NAG  B 516      14
HET    IFM  B 517      10
HET    GOL  B 518       6
HET    GOL  B 519       6
HET    PO4  C 498       5
HET    PO4  C 499       5
HET    PO4  C 500       5
HET    PO4  C 501       5
HET    PO4  C 502       5
HET    PO4  C 503       5
HET    PO4  C 504       5
HET    PO4  C 505       5
HET    PO4  C 506       5
HET    PO4  C 507       5
HET    PO4  C 508       5
HET    PO4  C 509       5
HET    PO4  C 510       5
HET    PO4  C 511       5
HET    PO4  C 512       5
HET    NAG  C 513      14
HET    GOL  C 514       6
HET    PO4  D 498       5
HET    PO4  D 499       5
HET    PO4  D 500       5
HET    PO4  D 501       5
HET    PO4  D 502       5
HET    PO4  D 503       5
HET    PO4  D 504       5
HET    PO4  D 505       5
HET    PO4  D 506       5
HET    PO4  D 507       5
HET    PO4  D 508       5
HET    PO4  D 509       5
HET    PO4  D 510       5
HET    NAG  D 511      14
HET    IFM  D 512      10
HETNAM     PO4 PHOSPHATE ION
HETNAM     NAG N-ACETYL-D-GLUCOSAMINE
HETNAM     GOL GLYCEROL
HETNAM     IFM 5-HYDROXYMETHYL-3,4-DIHYDROXYPIPERIDINE
HETSYN     GOL GLYCERIN; PROPANE-1,2,3-TRIOL
HETSYN     IFM (3R,4R,5R)-5-(HYDROXYMETHYL)PIPERIDINE-3,4-DIOL
FORMUL   5  PO4    64(O4 P 3-)
FORMUL  23  NAG    4(C8 H15 N O6)
FORMUL  24  GOL    5(C3 H8 O3)
FORMUL  45  IFM    2(C6 H13 N O3)
FORMUL  80  HOH   *905(H2 O)
HELIX    1   1 THR A   86  LEU A   94  1                                   9
HELIX    2   2 SER A   97  SER A  110  1                                  14
HELIX    3   3 PRO A  150  LEU A  156  1                                   7
HELIX    4   4 LEU A  156  ALA A  168  1                                  13
HELIX    5   5 PRO A  182  LYS A  186  5                                   5
HELIX    6   6 ASP A  203  HIS A  223  1                                  21
HELIX    7   7 GLU A  235  LEU A  241  5                                   7
HELIX    8   8 THR A  252  ASP A  263  1                                  12
HELIX    9   9 ASP A  263  ASN A  270  1                                   8
HELIX   10  10 SER A  271  VAL A  276  5                                   6
HELIX   11  11 LEU A  286  LEU A  288  5                                   3
HELIX   12  12 PRO A  289  THR A  297  1                                   9
HELIX   13  13 ASP A  298  LYS A  303  1                                   6
HELIX   14  14 PRO A  319  PHE A  331  1                                  13
HELIX   15  15 SER A  356  TYR A  373  1                                  18
HELIX   16  16 ILE A  406  ASP A  409  5                                   4
HELIX   17  17 GLN A  414  LYS A  425  1                                  12
HELIX   18  18 THR B   86  LEU B   94  1                                   9
HELIX   19  19 SER B   97  SER B  110  1                                  14
HELIX   20  20 PRO B  150  LYS B  155  1                                   6
HELIX   21  21 LEU B  156  ALA B  168  1                                  13
HELIX   22  22 PRO B  182  LYS B  186  5                                   5
HELIX   23  23 ASP B  203  HIS B  223  1                                  21
HELIX   24  24 GLU B  235  LEU B  241  5                                   7
HELIX   25  25 THR B  252  ASP B  263  1                                  12
HELIX   26  26 ASP B  263  ASN B  270  1                                   8
HELIX   27  27 LEU B  286  LEU B  288  5                                   3
HELIX   28  28 PRO B  289  THR B  297  1                                   9
HELIX   29  29 ASP B  298  LYS B  303  1                                   6
HELIX   30  30 LEU B  314  ALA B  318  5                                   5
HELIX   31  31 PRO B  319  PHE B  331  1                                  13
HELIX   32  32 SER B  356  TYR B  373  1                                  18
HELIX   33  33 ILE B  406  ASP B  409  5                                   4
HELIX   34  34 GLN B  414  LYS B  425  1                                  12
HELIX   35  35 THR C   86  ALA C   95  1                                  10
HELIX   36  36 SER C   97  SER C  110  1                                  14
HELIX   37  37 PRO C  150  LYS C  155  1                                   6
HELIX   38  38 LEU C  156  ALA C  168  1                                  13
HELIX   39  39 PRO C  182  LYS C  186  5                                   5
HELIX   40  40 ASP C  203  HIS C  223  1                                  21
HELIX   41  41 GLU C  235  LEU C  241  5                                   7
HELIX   42  42 THR C  252  ASP C  263  1                                  12
HELIX   43  43 ASP C  263  ASN C  270  1                                   8
HELIX   44  44 LEU C  286  LEU C  288  5                                   3
HELIX   45  45 PRO C  289  THR C  297  1                                   9
HELIX   46  46 ASP C  298  LYS C  303  1                                   6
HELIX   47  47 PRO C  319  PHE C  331  1                                  13
HELIX   48  48 SER C  356  TYR C  373  1                                  18
HELIX   49  49 ILE C  406  ASP C  409  5                                   4
HELIX   50  50 GLN C  414  LYS C  425  1                                  12
HELIX   51  51 THR D   86  ALA D   95  1                                  10
HELIX   52  52 SER D   97  SER D  110  1                                  14
HELIX   53  53 PRO D  150  LYS D  155  1                                   6
HELIX   54  54 LEU D  156  ALA D  168  1                                  13
HELIX   55  55 PRO D  182  LYS D  186  5                                   5
HELIX   56  56 ASP D  203  HIS D  223  1                                  21
HELIX   57  57 GLU D  235  LEU D  241  5                                   7
HELIX   58  58 THR D  252  ASP D  263  1                                  12
HELIX   59  59 ASP D  263  ASN D  270  1                                   8
HELIX   60  60 LEU D  286  LEU D  288  5                                   3
HELIX   61  61 PRO D  289  THR D  297  1                                   9
HELIX   62  62 ASP D  298  LYS D  303  1                                   6
HELIX   63  63 LEU D  314  ALA D  318  5                                   5
HELIX   64  64 THR D  323  PHE D  331  1                                   9
HELIX   65  65 SER D  356  TYR D  373  1                                  18
HELIX   66  66 ILE D  406  ASP D  409  5                                   4
HELIX   67  67 GLN D  414  LYS D  425  1                                  12
SHEET    1   A 4 PRO A   6  LYS A   7  0
SHEET    2   A 4 VAL A  15  CYS A  18 -1  O  VAL A  15   N  LYS A   7
SHEET    3   A 4 THR A 410  LYS A 413 -1  O  PHE A 411   N  CYS A  18
SHEET    4   A 4 ILE A 402  ASP A 405 -1  N  ILE A 403   O  TYR A 412
SHEET    1   B 9 GLU A  50  PRO A  55  0
SHEET    2   B 9 THR A  36  THR A  43 -1  N  ARG A  39   O  SER A  52
SHEET    3   B 9 SER A 488  TRP A 494 -1  O  LEU A 493   N  SER A  38
SHEET    4   B 9 ALA A 456  ASN A 462 -1  N  ALA A 456   O  TRP A 494
SHEET    5   B 9 ASP A 445  MET A 450 -1  N  LEU A 449   O  VAL A 457
SHEET    6   B 9 GLN A 432  ALA A 438 -1  N  GLN A 432   O  MET A 450
SHEET    7   B 9 LEU A  65  LYS A  77 -1  N  PHE A  75   O  ARG A 433
SHEET    8   B 9 VAL A 468  ASP A 474  1  O  LYS A 473   N  LEU A  69
SHEET    9   B 9 GLY A 478  SER A 484 -1  O  SER A 484   N  VAL A 468
SHEET    1   C 9 GLY A  80  ALA A  84  0
SHEET    2   C 9 ILE A 118  MET A 123  1  O  ARG A 120   N  GLY A  83
SHEET    3   C 9 SER A 173  PRO A 178  1  O  LEU A 175   N  VAL A 121
SHEET    4   C 9 ALA A 229  THR A 231  1  O  THR A 231   N  ALA A 176
SHEET    5   C 9 ARG A 277  GLN A 284  1  O  ARG A 277   N  VAL A 230
SHEET    6   C 9 GLY A 307  HIS A 311  1  O  ALA A 309   N  MET A 280
SHEET    7   C 9 MET A 335  ALA A 341  1  O  PHE A 337   N  VAL A 310
SHEET    8   C 9 VAL A 375  ASN A 382  1  O  VAL A 376   N  LEU A 336
SHEET    9   C 9 GLY A  80  ALA A  84  1  N  GLY A  82   O  ASP A 380
SHEET    1   D 4 PRO B   6  LYS B   7  0
SHEET    2   D 4 VAL B  15  CYS B  18 -1  O  VAL B  15   N  LYS B   7
SHEET    3   D 4 THR B 410  LYS B 413 -1  O  PHE B 411   N  CYS B  18
SHEET    4   D 4 ILE B 402  ASP B 405 -1  N  ASP B 405   O  THR B 410
SHEET    1   E 9 GLU B  50  PRO B  55  0
SHEET    2   E 9 THR B  36  THR B  43 -1  N  ARG B  39   O  SER B  52
SHEET    3   E 9 SER B 488  TRP B 494 -1  O  LEU B 493   N  SER B  38
SHEET    4   E 9 ALA B 456  ASN B 462 -1  N  ASN B 462   O  SER B 488
SHEET    5   E 9 LEU B 444  MET B 450 -1  N  ASP B 445   O  LEU B 461
SHEET    6   E 9 GLN B 432  ALA B 438 -1  N  GLN B 432   O  MET B 450
SHEET    7   E 9 LEU B  65  LYS B  77 -1  N  THR B  68   O  VAL B 437
SHEET    8   E 9 VAL B 468  ASP B 474  1  O  LYS B 473   N  LEU B  69
SHEET    9   E 9 GLY B 478  SER B 484 -1  O  SER B 484   N  VAL B 468
SHEET    1   F 9 GLY B  80  ALA B  84  0
SHEET    2   F 9 ILE B 118  MET B 123  1  O  ARG B 120   N  GLY B  83
SHEET    3   F 9 SER B 173  PRO B 178  1  O  LEU B 175   N  VAL B 121
SHEET    4   F 9 ALA B 229  THR B 231  1  O  THR B 231   N  ALA B 176
SHEET    5   F 9 ARG B 277  GLN B 284  1  O  ARG B 277   N  VAL B 230
SHEET    6   F 9 GLY B 307  HIS B 311  1  O  ALA B 309   N  MET B 280
SHEET    7   F 9 MET B 335  GLU B 340  1  O  MET B 335   N  ILE B 308
SHEET    8   F 9 VAL B 375  ASN B 382  1  O  VAL B 376   N  LEU B 336
SHEET    9   F 9 GLY B  80  ALA B  84  1  N  GLY B  82   O  ASP B 380
SHEET    1   G 5 PRO C   6  LYS C   7  0
SHEET    2   G 5 VAL C  15  CYS C  18 -1  O  VAL C  15   N  LYS C   7
SHEET    3   G 5 THR C 410  LYS C 413 -1  O  PHE C 411   N  CYS C  18
SHEET    4   G 5 ILE C 402  ASP C 405 -1  N  ASP C 405   O  THR C 410
SHEET    5   G 5 ALA C 384  LEU C 385  1  N  LEU C 385   O  VAL C 404
SHEET    1   H 9 GLU C  50  PRO C  55  0
SHEET    2   H 9 THR C  36  THR C  43 -1  N  ARG C  39   O  SER C  52
SHEET    3   H 9 SER C 488  TRP C 494 -1  O  LEU C 493   N  SER C  38
SHEET    4   H 9 ALA C 456  ASN C 462 -1  N  ALA C 456   O  TRP C 494
SHEET    5   H 9 ASP C 445  MET C 450 -1  N  ASP C 445   O  LEU C 461
SHEET    6   H 9 GLN C 432  ALA C 438 -1  N  GLN C 432   O  MET C 450
SHEET    7   H 9 LEU C  65  LYS C  77 -1  N  PHE C  75   O  ARG C 433
SHEET    8   H 9 VAL C 468  ASP C 474  1  O  LYS C 473   N  LEU C  69
SHEET    9   H 9 GLY C 478  SER C 484 -1  O  SER C 484   N  VAL C 468
SHEET    1   I 9 GLY C  80  ALA C  84  0
SHEET    2   I 9 ILE C 118  MET C 123  1  O  ARG C 120   N  GLY C  83
SHEET    3   I 9 SER C 173  PRO C 178  1  O  LEU C 175   N  VAL C 121
SHEET    4   I 9 ALA C 229  THR C 231  1  O  THR C 231   N  ALA C 176
SHEET    5   I 9 ARG C 277  GLN C 284  1  O  LEU C 279   N  VAL C 230
SHEET    6   I 9 GLY C 307  TRP C 312  1  O  ALA C 309   N  MET C 280
SHEET    7   I 9 MET C 335  ALA C 341  1  O  PHE C 337   N  VAL C 310
SHEET    8   I 9 VAL C 375  ASN C 382  1  O  VAL C 376   N  LEU C 336
SHEET    9   I 9 GLY C  80  ALA C  84  1  N  GLY C  82   O  ASP C 380
SHEET    1   J 5 PRO D   6  LYS D   7  0
SHEET    2   J 5 VAL D  15  CYS D  18 -1  O  VAL D  15   N  LYS D   7
SHEET    3   J 5 THR D 410  LYS D 413 -1  O  PHE D 411   N  CYS D  18
SHEET    4   J 5 ILE D 402  ASP D 405 -1  N  ILE D 403   O  TYR D 412
SHEET    5   J 5 ALA D 384  LEU D 385  1  N  LEU D 385   O  VAL D 404
SHEET    1   K 9 GLU D  50  PRO D  55  0
SHEET    2   K 9 THR D  36  THR D  43 -1  N  ARG D  39   O  SER D  52
SHEET    3   K 9 SER D 488  TRP D 494 -1  O  LEU D 493   N  SER D  38
SHEET    4   K 9 ALA D 456  ASN D 462 -1  N  ASN D 462   O  SER D 488
SHEET    5   K 9 LEU D 444  MET D 450 -1  N  ASP D 445   O  LEU D 461
SHEET    6   K 9 GLN D 432  ALA D 438 -1  N  GLN D 432   O  MET D 450
SHEET    7   K 9 LEU D  65  LYS D  77 -1  N  THR D  68   O  VAL D 437
SHEET    8   K 9 VAL D 468  ASP D 474  1  O  LYS D 473   N  LEU D  69
SHEET    9   K 9 GLY D 478  SER D 484 -1  O  SER D 484   N  VAL D 468
SHEET    1   L 9 GLY D  80  ALA D  84  0
SHEET    2   L 9 ILE D 118  MET D 123  1  O  ARG D 120   N  GLY D  83
SHEET    3   L 9 SER D 173  PRO D 178  1  O  LEU D 175   N  VAL D 121
SHEET    4   L 9 ALA D 229  THR D 231  1  O  THR D 231   N  ALA D 176
SHEET    5   L 9 ARG D 277  GLN D 284  1  O  LEU D 279   N  VAL D 230
SHEET    6   L 9 GLY D 307  HIS D 311  1  O  ALA D 309   N  MET D 280
SHEET    7   L 9 MET D 335  GLU D 340  1  O  MET D 335   N  ILE D 308
SHEET    8   L 9 VAL D 375  ASN D 382  1  O  VAL D 376   N  LEU D 336
SHEET    9   L 9 GLY D  80  ALA D  84  1  N  GLY D  82   O  ASP D 380
SSBOND   1 CYS A    4    CYS A   16                          1555   1555  2.05
SSBOND   2 CYS A   18    CYS A   23                          1555   1555  2.06
SSBOND   3 CYS B    4    CYS B   16                          1555   1555  2.11
SSBOND   4 CYS B   18    CYS B   23                          1555   1555  2.11
SSBOND   5 CYS C    4    CYS C   16                          1555   1555  2.08
SSBOND   6 CYS C   18    CYS C   23                          1555   1555  2.10
SSBOND   7 CYS D    4    CYS D   16                          1555   1555  2.13
SSBOND   8 CYS D   18    CYS D   23                          1555   1555  2.14
LINK         ND2 ASN A  19                 C1  NAG A 516     1555   1555  1.43
LINK         ND2 ASN B  19                 C1  NAG B 516     1555   1555  1.46
LINK         ND2 ASN C  19                 C1  NAG C 513     1555   1555  1.45
LINK         ND2 ASN D  19                 C1  NAG D 511     1555   1555  1.46
CISPEP   1 LEU A  288    PRO A  289          0        -3.42
CISPEP   2 TYR A  313    LEU A  314          0         7.06
CISPEP   3 VAL A  343    GLY A  344          0        -1.16
CISPEP   4 GLY A  344    SER A  345          0       -26.41
CISPEP   5 SER A  345    LYS A  346          0       -13.23
CISPEP   6 GLY A  390    PRO A  391          0         3.98
CISPEP   7 GLY B   62    THR B   63          0        -6.88
CISPEP   8 LEU B  288    PRO B  289          0        -0.88
CISPEP   9 PHE B  347    TRP B  348          0        26.73
CISPEP  10 GLY B  390    PRO B  391          0         8.60
CISPEP  11 LEU C  288    PRO C  289          0         3.54
CISPEP  12 VAL C  343    GLY C  344          0       -21.27
CISPEP  13 SER C  345    LYS C  346          0        11.32
CISPEP  14 GLY C  390    PRO C  391          0         1.44
CISPEP  15 LEU D  288    PRO D  289          0         0.44
CISPEP  16 VAL D  343    GLY D  344          0       -27.35
CISPEP  17 GLY D  344    SER D  345          0        17.13
CISPEP  18 GLY D  390    PRO D  391          0         6.57
SITE     1 AC1  6 TYR A  11  SER A  12  ARG A 353  SER A 356
SITE     2 AC1  6 ASP A 358  HOH A 530
SITE     1 AC2  4 THR A  63  GLN A 440  HOH A 878  LYS C 473
SITE     1 AC3  5 LYS A  79  TRP A 228  ARG A 277  HIS A 306
SITE     2 AC3  5 HOH A 696
SITE     1 AC4  4 ARG A  44  SER A  45  HOH A 669  HOH A 886
SITE     1 AC5  2 ARG A  44  TYR A 487
SITE     1 AC6  4 GLN A 226  HIS A 273  VAL A 276  HOH A 688
SITE     1 AC7  4 PHE A  75  HIS A 328  HIS A 374  HOH A 879
SITE     1 AC8  6 LEU A 165  ARG A 170  PRO A 171  VAL A 172
SITE     2 AC8  6 HOH A 596  HOH A 948
SITE     1 AC9  3 HIS A 290  LYS A 293  HOH A 567
SITE     1 BC1  2 GLU D 254  ARG D 257
SITE     1 BC2  3 GLY A  54  PRO A  55  HOH A 584
SITE     1 BC3  3 GLU A 111  ARG A 170  PO4 A 515
SITE     1 BC4  5 ARG A 277  VAL A 305  HIS A 306  HOH A 693
SITE     2 BC4  5 HOH A 713
SITE     1 BC5  4 GLU A 254  ARG A 257  HOH A 638  HOH A 689
SITE     1 BC6  4 ARG A 329  LEU A 330  LYS D 321  ARG D 329
SITE     1 BC7  4 THR A 187  LYS A 198  GLY A 199  HOH A 686
SITE     1 BC8  5 TYR A  11  TRP A 348  GLU A 349  GLN A 350
SITE     2 BC8  5 ARG A 353
SITE     1 BC9  5 ARG A 170  PRO A 428  PO4 A 509  HOH A 665
SITE     2 BC9  5 HOH A 802
SITE     1 CC1  5 ASN A  19  HOH A 526  HOH A 538  HOH A 645
SITE     2 CC1  5 HOH A 761
SITE     1 CC2  8 ASP A 127  PHE A 128  TRP A 179  ASN A 234
SITE     2 CC2  8 GLU A 235  GLU A 340  TRP A 381  PHE A 397
SITE     1 CC3  7 ASP A  24  SER A  25  PHE A  26  ARG A  48
SITE     2 CC3  7 HOH A 587  HOH A 663  HOH A 667
SITE     1 CC4  6 TYR B  11  SER B  12  ARG B 353  SER B 356
SITE     2 CC4  6 TRP B 357  ASP B 358
SITE     1 CC5  6 GLY B 193  LYS B 194  SER B 242  GLY B 243
SITE     2 CC5  6 HOH B 522  HOH B 562
SITE     1 CC6  4 LYS B  79  TRP B 228  ARG B 277  HIS B 306
SITE     1 CC7  4 ARG B  44  SER B  45  HOH B 656  HOH B 939
SITE     1 CC8  8 GLN B 226  THR B 272  HIS B 273  VAL B 276
SITE     2 CC8  8 HOH B 541  HOH B 574  HOH B 699  HOH B 711
SITE     1 CC9  6 THR B 187  LYS B 194  GLY B 195  SER B 196
SITE     2 CC9  6 HOH B 617  HOH B 620
SITE     1 DC1  3 THR B 187  LYS B 198  GLY B 199
SITE     1 DC2  2 HIS B 290  LYS B 293
SITE     1 DC3  5 LEU B 330  PHE B 331  PRO B 332  ASN B 333
SITE     2 DC3  5 THR B 334
SITE     1 DC4  4 ARG B 277  VAL B 305  HIS B 306  HOH B 944
SITE     1 DC5  2 ARG B 262  HOH B 611
SITE     1 DC6  4 PRO B 171  VAL B 172  HOH B 596  HOH B 616
SITE     1 DC7  2 GLN B 207  ARG B 211
SITE     1 DC8  4 GLN B 143  HIS B 145  HOH B 595  HOH B 627
SITE     1 DC9  5 VAL B 214  ASP B 218  SER B 271  THR B 272
SITE     2 DC9  5 HIS B 273
SITE     1 EC1  4 LYS B 321  ARG B 329  ARG C 329  LEU C 330
SITE     1 EC2  3 ARG B  44  SER B 465  TYR B 487
SITE     1 EC3  5 PRO B 159  HIS B 162  HOH B 546  HOH B 599
SITE     2 EC3  5 HOH B 601
SITE     1 EC4  5 ILE B   5  ASN B  19  THR B  21  TYR B  22
SITE     2 EC4  5 HOH B 670
SITE     1 EC5 10 ASP B 127  PHE B 128  TRP B 179  GLU B 235
SITE     2 EC5 10 PHE B 246  TYR B 313  GLU B 340  SER B 345
SITE     3 EC5 10 TRP B 381  ASN B 396
SITE     1 EC6  7 CYS B   4  ASP B  24  ARG B  48  MET B  49
SITE     2 EC6  7 GOL B 519  HOH B 563  HOH B 817
SITE     1 EC7  9 PHE B  26  MET B  49  GLU B  50  LEU B  51
SITE     2 EC7  9 GOL B 518  HOH B 635  HOH B 659  HOH B 664
SITE     3 EC7  9 HOH B 684
SITE     1 EC8  7 TYR C  11  SER C  12  ARG C 353  SER C 356
SITE     2 EC8  7 TRP C 357  ASP C 358  HOH C 619
SITE     1 EC9  5 LYS A 473  THR C  63  GLY C  64  GLN C 440
SITE     2 EC9  5 HOH C 653
SITE     1 FC1  3 ARG C  44  SER C  45  HOH C 601
SITE     1 FC2  4 LYS C  79  TRP C 228  ARG C 277  HIS C 306
SITE     1 FC3  7 GLN C 226  PHE C 227  THR C 272  HIS C 273
SITE     2 FC3  7 HIS C 274  ASN C 275  VAL C 276
SITE     1 FC4  5 TYR C  11  TRP C 348  GLU C 349  GLN C 350
SITE     2 FC4  5 ARG C 353
SITE     1 FC5  2 ARG C 170  PRO C 428
SITE     1 FC6  3 LYS C 466  ASP C 467  HOH C 937
SITE     1 FC7  7 THR C 154  ILE C 158  PRO C 159  HIS C 162
SITE     2 FC7  7 HIS C 223  HOH C 607  HOH C 720
SITE     1 FC8  2 GLU C 254  ARG C 257
SITE     1 FC9  6 ARG C 277  VAL C 305  HIS C 306  HOH C 565
SITE     2 FC9  6 HOH C 623  HOH C 641
SITE     1 GC1  2 ARG C  44  TYR C 487
SITE     1 GC2  6 PHE C  75  HIS C 328  HIS C 374  HOH C 522
SITE     2 GC2  6 HOH C 608  HOH C 783
SITE     1 GC3  5 LEU C 165  ARG C 170  PRO C 171  VAL C 172
SITE     2 GC3  5 HOH C 768
SITE     1 GC4  4 HIS C 290  LYS C 293  HOH C 602  HOH C 622
SITE     1 GC5  5 ASN C  19  TYR C  22  HOH C 524  HOH C 559
SITE     2 GC5  5 HOH C 629
SITE     1 GC6  7 ASP C 127  PHE C 128  TRP C 179  GLU C 235
SITE     2 GC6  7 GLU C 340  TRP C 381  PHE C 397
SITE     1 GC7  7 SER C 242  TYR D  11  SER D  12  ARG D 353
SITE     2 GC7  7 SER D 356  TRP D 357  ASP D 358
SITE     1 GC8  6 GLY D 193  LYS D 194  SER D 242  GLY D 243
SITE     2 GC8  6 HOH D 612  HOH D 626
SITE     1 GC9  6 LYS D  79  TRP D 228  ARG D 277  HIS D 306
SITE     2 GC9  6 HOH D 516  HOH D 910
SITE     1 HC1  6 GLN D 226  THR D 272  HIS D 273  VAL D 276
SITE     2 HC1  6 HOH D 530  HOH D 628
SITE     1 HC2  2 ARG D  44  SER D  45
SITE     1 HC3  5 THR D 154  ILE D 158  PRO D 159  HIS D 162
SITE     2 HC3  5 HOH D 537
SITE     1 HC4  3 HIS D 290  LYS D 293  HOH D 581
SITE     1 HC5  3 LYS D 198  GLY D 199  HOH D 577
SITE     1 HC6  3 GLN D 207  ARG D 211  HOH D 562
SITE     1 HC7  2 ARG D  44  TYR D 487
SITE     1 HC8  4 LEU D 165  PRO D 171  VAL D 172  HOH D 661
SITE     1 HC9  5 ARG D 277  VAL D 305  HIS D 306  HOH D 594
SITE     2 HC9  5 HOH D 900
SITE     1 IC1  4 ALA D 438  ASN D 442  LEU D 444  HOH D 532
SITE     1 IC2  3 ASN D  19  THR D  21  TYR D  22
SITE     1 IC3  9 ASP D 127  PHE D 128  TRP D 179  GLU D 235
SITE     2 IC3  9 PHE D 246  TYR D 313  GLU D 340  TRP D 381
SITE     3 IC3  9 ASN D 396
CRYST1  110.311   92.013  152.362  90.00 111.21  90.00 P 1 21 1      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      0.009065  0.000000  0.003518        0.00000
SCALE2      0.000000  0.010868  0.000000        0.00000
SCALE3      0.000000  0.000000  0.007040        0.00000
      
PROCHECK
Go to PROCHECK summary
 References