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PDBsum entry 2nt0

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Top Page protein ligands Protein-protein interface(s) links
Hydrolase PDB id
2nt0
Jmol
Contents
Protein chain
497 a.a.
Ligands
NAG ×5
SO4 ×20
GOL ×13
Waters ×1710
HEADER    HYDROLASE                               06-NOV-06   2NT0
TITLE     ACID-BETA-GLUCOSIDASE LOW PH, GLYCEROL BOUND
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;
SOURCE   6 EXPRESSION_SYSTEM: CRICETULUS GRISEUS;
SOURCE   7 EXPRESSION_SYSTEM_COMMON: CHINESE HAMSTER;
SOURCE   8 EXPRESSION_SYSTEM_TAXID: 10029;
SOURCE   9 EXPRESSION_SYSTEM_ORGAN: OVARY
KEYWDS    CEREZYME, GLUCOCEREBROSIDASE, GLUCOSYLCERAMIDE, HYDROLYSIS, GAUCHER
KEYWDS   2 DISEASE, HYDROLASE
EXPDTA    X-RAY DIFFRACTION
AUTHOR    R.L.LIEBERMAN,G.A.PETSKO,D.RINGE
REVDAT   3   13-JUL-11 2NT0    1       VERSN
REVDAT   2   24-FEB-09 2NT0    1       VERSN
REVDAT   1   26-DEC-06 2NT0    0
JRNL        AUTH   R.L.LIEBERMAN,B.A.WUSTMAN,P.HUERTAS,A.C.POWE,C.W.PINE,
JRNL        AUTH 2 R.KHANNA,M.G.SCHLOSSMACHER,D.RINGE,G.A.PETSKO
JRNL        TITL   STRUCTURE OF ACID BETA-GLUCOSIDASE WITH PHARMACOLOGICAL
JRNL        TITL 2 CHAPERONE PROVIDES INSIGHT INTO GAUCHER DISEASE.
JRNL        REF    NAT.CHEM.BIOL.                V.   3   101 2007
JRNL        REFN                   ISSN 1552-4450
JRNL        PMID   17187079
JRNL        DOI    10.1038/NCHEMBIO850
REMARK   1
REMARK   1 REFERENCE 1
REMARK   1  TITL   STRUCTURE OF ACID-BETA-GLUCOSIDASE WITH PHARMACOLOGICAL
REMARK   1  TITL 2 CHAPERONE PROVIDES INSIGHT INTO GAUCHER DISEASE
REMARK   1  REF    NAT.CHEM.BIOL.                             2006
REMARK   1  REFN                   ESSN 1552-4469
REMARK   1  DOI    10.1038/NCHEMBIO850
REMARK   2
REMARK   2 RESOLUTION.    1.79 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) : 1.79
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 50.00
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000
REMARK   3   COMPLETENESS FOR RANGE        (%) : 84.1
REMARK   3   NUMBER OF REFLECTIONS             : 220955
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) : 0.181
REMARK   3   R VALUE            (WORKING SET) : 0.179
REMARK   3   FREE R VALUE                     : 0.215
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000
REMARK   3   FREE R VALUE TEST SET COUNT      : 11117
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) : 1.79
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.83
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 11696
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 63.17
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2690
REMARK   3   BIN FREE R VALUE SET COUNT          : 588
REMARK   3   BIN FREE R VALUE                    : 0.3170
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          : 248
REMARK   3   SOLVENT ATOMS            : 1710
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : 24.35
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 24.35
REMARK   3   OVERALL ANISOTROPIC B VALUE.
REMARK   3    B11 (A**2) : 2.15000
REMARK   3    B22 (A**2) : -1.24000
REMARK   3    B33 (A**2) : -1.15000
REMARK   3    B12 (A**2) : 0.00000
REMARK   3    B13 (A**2) : -0.33000
REMARK   3    B23 (A**2) : 0.00000
REMARK   3
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.
REMARK   3   ESU BASED ON R VALUE                            (A): 0.123
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.121
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.076
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 2.437
REMARK   3
REMARK   3 CORRELATION COEFFICIENTS.
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.963
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.946
REMARK   3
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT
REMARK   3   BOND LENGTHS REFINED ATOMS        (A): 16525 ; 0.017 ; 0.022
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 22584 ; 1.585 ; 1.958
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):  1984 ; 6.833 ; 5.000
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   720 ;36.931 ;23.444
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  2516 ;14.367 ;15.000
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    84 ;18.413 ;15.000
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  2416 ; 0.115 ; 0.200
REMARK   3   GENERAL PLANES REFINED ATOMS      (A): 12536 ; 0.008 ; 0.020
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  8643 ; 0.219 ; 0.200
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A): 11086 ; 0.308 ; 0.200
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  1673 ; 0.197 ; 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 ; 0.200 ; 0.200
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    26 ; 0.165 ; 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): 10191 ; 1.011 ; 1.500
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 16072 ; 1.530 ; 2.000
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  7184 ; 2.485 ; 3.000
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  6328 ; 3.622 ; 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 : NULL
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: NULL
REMARK   4
REMARK   4 2NT0 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 10-NOV-06.
REMARK 100 THE RCSB ID CODE IS RCSB040264.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 30-SEP-05
REMARK 200  TEMPERATURE           (KELVIN) : 100
REMARK 200  PH                             : 4.5
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-B
REMARK 200  X-RAY GENERATOR MODEL          : NULL
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 1
REMARK 200  MONOCHROMATOR                  : NULL
REMARK 200  OPTICS                         : NULL
REMARK 200
REMARK 200  DETECTOR TYPE                  : CCD
REMARK 200  DETECTOR MANUFACTURER          : MARRESEARCH
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200  DATA SCALING SOFTWARE          : HKL
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 220956
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.800
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 84.8
REMARK 200  DATA REDUNDANCY                : 2.100
REMARK 200  R MERGE                    (I) : NULL
REMARK 200  R SYM                      (I) : 0.06200
REMARK 200   FOR THE DATA SET  : 7.6000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.80
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.86
REMARK 200  COMPLETENESS FOR SHELL     (%) : 71.8
REMARK 200  DATA REDUNDANCY IN SHELL       : 1.80
REMARK 200  R MERGE FOR SHELL          (I) : NULL
REMARK 200  R SYM FOR SHELL            (I) : 0.41700
REMARK 200   FOR SHELL         : 1.500
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: NULL
REMARK 200 STARTING MODEL: 1OGS MONOMER
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 61.24
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.17
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 1 M AMMONIUM SULFATE  0.17 M
REMARK 280  GUANIDINIUM HCL 0.02 M KCL 0.1 M ACETATE BUFFER PH 4.5
REMARK 280  CRYOPROTECTANT INCLUDES 20% GLYCEROL, VAPOR DIFFUSION, HANGING
REMARK 280  DROP, 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       45.87950
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, 3, 4
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: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 3
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 350
REMARK 350 BIOMOLECULE: 4
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 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  GLU C   151     O    HOH C  2005              1.32
REMARK 500   OE1  GLN A    73     O    HOH A   869              1.71
REMARK 500   O    PHE A   109     O    HOH A   903              1.72
REMARK 500   O    HOH C  1644     O    HOH C  1990              1.74
REMARK 500   O    HOH B   609     O    HOH B   913              1.79
REMARK 500   O7   NAG B   498     O    HOH B   602              1.80
REMARK 500   O    HOH D   584     O    HOH D   889              1.82
REMARK 500   O    HOH C  1615     O    HOH C  1929              1.88
REMARK 500   O3   GOL D   508     O    HOH D   798              1.93
REMARK 500   O    HOH D   564     O    HOH D   829              1.94
REMARK 500   O    HOH D   942     O    HOH D   944              1.97
REMARK 500   CB   SER C   196     O    HOH C  1949              1.97
REMARK 500   OD1  ASN D   102     O    HOH D   806              2.01
REMARK 500   CB   ILE D    93     O    HOH D   750              2.01
REMARK 500   O    HOH C  1627     O    HOH D   900              2.02
REMARK 500   O    HOH A   562     O    HOH A   804              2.03
REMARK 500   NH2  ARG C   211     O    HOH C  1872              2.03
REMARK 500   OE1  GLU C   388     O    HOH C  1776              2.04
REMARK 500   O    HOH B   757     O    HOH B   865              2.05
REMARK 500   OE2  GLU B   152     O    HOH B   842              2.05
REMARK 500   C    PHE A   109     O    HOH A   903              2.07
REMARK 500   OH   TYR D    11     OE1  GLN D   350              2.07
REMARK 500   O    HOH B   797     O    HOH B   897              2.07
REMARK 500   OE1  GLN C    57     O    HOH C  1870              2.08
REMARK 500   O    HOH C  1759     O    HOH C  1927              2.10
REMARK 500   ND2  ASN B    19     O5   NAG B   498              2.10
REMARK 500   CG   ASN B   146     C1   NAG B   499              2.11
REMARK 500   O    HOH B   926     O    HOH B   963              2.11
REMARK 500   ND2  ASN B    19     C5   NAG B   498              2.11
REMARK 500   O    HOH D   702     O    HOH D   916              2.13
REMARK 500   O    HOH B   757     O    HOH B   948              2.13
REMARK 500   O    HOH A   722     O    HOH A   814              2.13
REMARK 500   C1   NAG B   498     O    HOH B   964              2.13
REMARK 500   SG   CYS C    23     O    HOH C  1989              2.13
REMARK 500   O    HOH D   665     O    HOH D   875              2.13
REMARK 500   OD1  ASN C   102     O    HOH C  1813              2.14
REMARK 500   OD2  ASP A   405     O    HOH A   729              2.14
REMARK 500   O    HOH D   597     O    HOH D   844              2.14
REMARK 500   CB   CYS C    23     O    HOH C  1989              2.15
REMARK 500   OH   TYR B    11     OE1  GLN B   350              2.15
REMARK 500   OD1  ASN A   146     O    HOH A   835              2.16
REMARK 500   CA   ALA A   168     O    HOH A   903              2.18
REMARK 500   OG1  THR A   410     O    HOH A   824              2.18
REMARK 500   O    HOH B   842     O    HOH C  1685              2.18
REMARK 500   OD2  ASP B   405     O    HOH B   627              2.18
REMARK 500   O    HOH C  1895     O    HOH C  1984              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    LEU B 480   CA  -  CB  -  CG  ANGL. DEV. =  16.1 DEGREES
REMARK 500    ARG D  44   NE  -  CZ  -  NH2 ANGL. DEV. =  -4.0 DEGREES
REMARK 500    VAL D 394   CG1 -  CB  -  CG2 ANGL. DEV. =  10.6 DEGREES
REMARK 500    ARG D 433   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.0 DEGREES
REMARK 500    LEU D 480   CA  -  CB  -  CG  ANGL. DEV. =  18.0 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     -159.70   -146.80
REMARK 500    PHE A  75     -139.35   -122.88
REMARK 500    ALA A 124     -154.63     67.74
REMARK 500    ASP A 141       66.06   -106.64
REMARK 500    LEU A 156      -68.68   -103.44
REMARK 500    ASN A 192     -158.83   -125.79
REMARK 500    GLU A 233      136.79    167.72
REMARK 500    ASP A 263      -62.38   -123.57
REMARK 500    LEU A 281      -79.47     68.84
REMARK 500    THR A 323      -76.92   -108.50
REMARK 500    HIS A 374       -3.99     83.56
REMARK 500    TRP A 381     -139.85    -81.70
REMARK 500    VAL A 394      -64.81    -98.17
REMARK 500    PHE A 397      -11.99   -151.19
REMARK 500    VAL A 477      -39.18   -133.93
REMARK 500    THR B  61     -154.55    -80.91
REMARK 500    PHE B  75     -133.02   -116.00
REMARK 500    ALA B 124     -151.67     67.91
REMARK 500    LEU B 156      -70.48   -112.47
REMARK 500    ASN B 192     -166.70   -111.92
REMARK 500    GLU B 233      132.04    167.15
REMARK 500    LEU B 281      -82.27     71.15
REMARK 500    ALA B 318       84.98   -160.21
REMARK 500    PRO B 319      119.04    -35.96
REMARK 500    THR B 323      -76.60   -107.38
REMARK 500    SER B 356      108.59    -53.44
REMARK 500    HIS B 374       -1.06     77.82
REMARK 500    TRP B 381     -140.31    -85.67
REMARK 500    ASN B 396       57.56    -90.60
REMARK 500    ASN C  19     -158.57   -149.24
REMARK 500    PHE C  75     -137.99   -119.85
REMARK 500    ALA C 124     -152.30     72.01
REMARK 500    ASP C 141       59.90   -105.08
REMARK 500    LEU C 156      -64.46   -104.87
REMARK 500    ASN C 192     -157.80   -127.48
REMARK 500    GLU C 233      135.37    165.25
REMARK 500    LEU C 281      -82.75     72.27
REMARK 500    THR C 323      -73.29   -110.09
REMARK 500    LEU C 354      109.68    -54.03
REMARK 500    HIS C 374        0.23     80.68
REMARK 500    TRP C 381     -134.62    -87.70
REMARK 500    VAL C 394      -61.09   -105.07
REMARK 500    ARG C 395      139.11   -171.68
REMARK 500    PHE C 397      -10.90   -149.68
REMARK 500    VAL C 477      -43.39   -130.16
REMARK 500    PHE D  75     -135.27   -126.74
REMARK 500    ALA D 124     -153.31     68.14
REMARK 500    ASN D 192     -169.91   -115.14
REMARK 500    GLU D 233      135.60    170.05
REMARK 500    ASP D 263      -68.90   -123.31
REMARK 500
REMARK 500 THIS ENTRY HAS      54 RAMACHANDRAN OUTLIERS.
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    TRP B 312        24.9      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 NAG A 498
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 498
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 499
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG D 498
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG C 498
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 D 499
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 D 500
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 500
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 C 499
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 499
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 500
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 C 500
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 C 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 D 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 D 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 503
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 504
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 D 503
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 505
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 D 504
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 D 505
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL C 1591
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 506
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL C 1592
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL D 506
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 503
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 507
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL D 507
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL D 508
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 508
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 504
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL C 1593
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL C 1594
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL C 1595
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2NSX   RELATED DB: PDB
DBREF  2NT0 A    1   497  UNP    P04062   GLCM_HUMAN      40    536
DBREF  2NT0 B    1   497  UNP    P04062   GLCM_HUMAN      40    536
DBREF  2NT0 C    1   497  UNP    P04062   GLCM_HUMAN      40    536
DBREF  2NT0 D    1   497  UNP    P04062   GLCM_HUMAN      40    536
SEQADV 2NT0 HIS A  495  UNP  P04062    ARG   534 CONFLICT
SEQADV 2NT0 HIS B  495  UNP  P04062    ARG   534 CONFLICT
SEQADV 2NT0 HIS C  495  UNP  P04062    ARG   534 CONFLICT
SEQADV 2NT0 HIS D  495  UNP  P04062    ARG   534 CONFLICT
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 2NT0 ASN A   19  ASN  GLYCOSYLATION SITE
MODRES 2NT0 ASN B   19  ASN  GLYCOSYLATION SITE
MODRES 2NT0 ASN C   19  ASN  GLYCOSYLATION SITE
MODRES 2NT0 ASN D   19  ASN  GLYCOSYLATION SITE
MODRES 2NT0 ASN B  146  ASN  GLYCOSYLATION SITE
MODRES 2NT0 THR D   21  THR  GLYCOSYLATION SITE
HET    NAG  A 498      14
HET    NAG  B 498      14
HET    NAG  B 499      14
HET    NAG  D 498      14
HET    NAG  C 498      14
HET    SO4  D 499       5
HET    SO4  D 500       5
HET    SO4  B 500       5
HET    SO4  C 499       5
HET    SO4  A 499       5
HET    SO4  B 501       5
HET    SO4  A 500       5
HET    SO4  C 500       5
HET    SO4  A 501       5
HET    SO4  C 501       5
HET    SO4  D 501       5
HET    SO4  A 502       5
HET    SO4  D 502       5
HET    SO4  B 502       5
HET    SO4  B 503       5
HET    SO4  B 504       5
HET    SO4  D 503       5
HET    SO4  B 505       5
HET    SO4  D 504       5
HET    SO4  D 505       5
HET    GOL  C1591       6
HET    GOL  B 506       6
HET    GOL  C1592       6
HET    GOL  D 506       6
HET    GOL  A 503       6
HET    GOL  B 507       6
HET    GOL  D 507       6
HET    GOL  D 508       6
HET    GOL  B 508       6
HET    GOL  A 504       6
HET    GOL  C1593       6
HET    GOL  C1594       6
HET    GOL  C1595       6
HETNAM     NAG N-ACETYL-D-GLUCOSAMINE
HETNAM     SO4 SULFATE ION
HETNAM     GOL GLYCEROL
HETSYN     GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL   5  NAG    5(C8 H15 N O6)
FORMUL  10  SO4    20(O4 S 2-)
FORMUL  30  GOL    13(C3 H8 O3)
FORMUL  43  HOH   *1710(H2 O)
HELIX    1   1 THR A   86  ALA A   95  1                                  10
HELIX    2   2 SER A   97  SER A  110  1                                  14
HELIX    3   3 PRO A  150  LYS A  155  1                                   6
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 LEU A  286  LEU A  288  5                                   3
HELIX   11  11 PRO A  289  THR A  297  1                                   9
HELIX   12  12 ASP A  298  LYS A  303  1                                   6
HELIX   13  13 PRO A  319  PHE A  331  1                                  13
HELIX   14  14 SER A  356  TYR A  373  1                                  18
HELIX   15  15 ILE A  406  ASP A  409  5                                   4
HELIX   16  16 GLN A  414  LYS A  425  1                                  12
HELIX   17  17 THR B   86  ALA B   95  1                                  10
HELIX   18  18 SER B   97  SER B  110  1                                  14
HELIX   19  19 PRO B  150  LYS B  155  1                                   6
HELIX   20  20 LEU B  156  ALA B  168  1                                  13
HELIX   21  21 PRO B  182  LYS B  186  5                                   5
HELIX   22  22 ASP B  203  HIS B  223  1                                  21
HELIX   23  23 GLU B  235  LEU B  241  5                                   7
HELIX   24  24 THR B  252  ASP B  263  1                                  12
HELIX   25  25 ASP B  263  ASN B  270  1                                   8
HELIX   26  26 LEU B  286  LEU B  288  5                                   3
HELIX   27  27 PRO B  289  THR B  297  1                                   9
HELIX   28  28 ASP B  298  LYS B  303  1                                   6
HELIX   29  29 PRO B  319  PHE B  331  1                                  13
HELIX   30  30 SER B  356  TYR B  373  1                                  18
HELIX   31  31 ILE B  406  ASP B  409  5                                   4
HELIX   32  32 GLN B  414  LYS B  425  1                                  12
HELIX   33  33 THR C   86  ALA C   95  1                                  10
HELIX   34  34 SER C   97  SER C  110  1                                  14
HELIX   35  35 PRO C  150  LYS C  155  1                                   6
HELIX   36  36 LEU C  156  ALA C  168  1                                  13
HELIX   37  37 PRO C  182  LYS C  186  5                                   5
HELIX   38  38 ASP C  203  HIS C  223  1                                  21
HELIX   39  39 GLU C  235  LEU C  241  5                                   7
HELIX   40  40 THR C  252  ASP C  263  1                                  12
HELIX   41  41 ASP C  263  ASN C  270  1                                   8
HELIX   42  42 LEU C  286  LEU C  288  5                                   3
HELIX   43  43 PRO C  289  THR C  297  1                                   9
HELIX   44  44 ASP C  298  LYS C  303  1                                   6
HELIX   45  45 PRO C  319  PHE C  331  1                                  13
HELIX   46  46 SER C  356  TYR C  373  1                                  18
HELIX   47  47 ILE C  406  ASP C  409  5                                   4
HELIX   48  48 GLN C  414  LYS C  425  1                                  12
HELIX   49  49 THR D   86  ALA D   95  1                                  10
HELIX   50  50 SER D   97  SER D  110  1                                  14
HELIX   51  51 PRO D  150  LYS D  155  1                                   6
HELIX   52  52 LEU D  156  ALA D  168  1                                  13
HELIX   53  53 PRO D  182  LYS D  186  5                                   5
HELIX   54  54 ASP D  203  HIS D  223  1                                  21
HELIX   55  55 GLU D  235  LEU D  241  5                                   7
HELIX   56  56 THR D  252  ASP D  263  1                                  12
HELIX   57  57 ASP D  263  SER D  271  1                                   9
HELIX   58  58 LEU D  286  LEU D  288  5                                   3
HELIX   59  59 PRO D  289  THR D  297  1                                   9
HELIX   60  60 ASP D  298  LYS D  303  1                                   6
HELIX   61  61 PRO D  319  PHE D  331  1                                  13
HELIX   62  62 SER D  356  TYR D  373  1                                  18
HELIX   63  63 ILE D  406  ASP D  409  5                                   4
HELIX   64  64 GLN D  414  LYS D  425  1                                  12
SHEET    1   A 5 PRO A   6  LYS A   7  0
SHEET    2   A 5 VAL A  15  CYS A  18 -1  O  VAL A  15   N  LYS A   7
SHEET    3   A 5 THR A 410  LYS A 413 -1  O  PHE A 411   N  CYS A  18
SHEET    4   A 5 ILE A 402  ASP A 405 -1  N  ASP A 405   O  THR A 410
SHEET    5   A 5 ALA A 384  LEU A 385  1  N  LEU A 385   O  VAL A 404
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  VAL A 458   O  TYR A 492
SHEET    5   B 9 LEU A 444  MET A 450 -1  N  ASP A 445   O  LEU A 461
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  LEU A 480   N  ILE A 472
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  TYR A 313  1  O  ALA A 309   N  MET A 280
SHEET    7   C 9 MET A 335  CYS A 342  1  O  MET A 335   N  ILE A 308
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  GLU B  41   O  GLU B  50
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  VAL B 458   O  TYR B 492
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  VAL B 434   O  ALA B 448
SHEET    7   E 9 LEU B  65  LYS B  77 -1  N  PHE B  75   O  ARG B 433
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  GLY B 478   N  ASP B 474
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  LEU B 279   N  VAL B 230
SHEET    6   F 9 GLY B 307  TYR B 313  1  O  ALA B 309   N  MET B 280
SHEET    7   F 9 MET B 335  CYS B 342  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 4 PRO C   6  LYS C   7  0
SHEET    2   G 4 VAL C  15  CYS C  18 -1  O  VAL C  15   N  LYS C   7
SHEET    3   G 4 THR C 410  LYS C 413 -1  O  PHE C 411   N  CYS C  18
SHEET    4   G 4 ILE C 402  ASP C 405 -1  N  ASP C 405   O  THR C 410
SHEET    1   H 9 GLU C  50  PRO C  55  0
SHEET    2   H 9 THR C  36  THR C  43 -1  N  PHE C  37   O  GLY C  54
SHEET    3   H 9 SER C 488  TRP C 494 -1  O  THR C 491   N  TYR C  40
SHEET    4   H 9 ALA C 456  ASN C 462 -1  N  VAL C 458   O  TYR C 492
SHEET    5   H 9 LEU C 444  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  LEU C 480   N  ILE C 472
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  TYR C 313  1  O  ALA C 309   N  MET C 280
SHEET    7   I 9 MET C 335  CYS C 342  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 4 PRO D   6  LYS D   7  0
SHEET    2   J 4 VAL D  15  CYS D  18 -1  O  VAL D  15   N  LYS D   7
SHEET    3   J 4 THR D 410  LYS D 413 -1  O  PHE D 411   N  CYS D  18
SHEET    4   J 4 ILE D 402  ASP D 405 -1  N  ASP D 405   O  THR D 410
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  VAL D 458   O  TYR D 492
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  GLY D 478   N  ASP D 474
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  TYR D 313  1  O  ALA D 309   N  MET D 280
SHEET    7   L 9 MET D 335  CYS D 342  1  O  PHE D 337   N  VAL D 310
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  2.04
SSBOND   2 CYS A   18    CYS A   23                          1555   1555  2.04
SSBOND   3 CYS B    4    CYS B   16                          1555   1555  2.04
SSBOND   4 CYS B   18    CYS B   23                          1555   1555  2.05
SSBOND   5 CYS C    4    CYS C   16                          1555   1555  2.04
SSBOND   6 CYS C   18    CYS C   23                          1555   1555  2.04
SSBOND   7 CYS D    4    CYS D   16                          1555   1555  2.04
SSBOND   8 CYS D   18    CYS D   23                          1555   1555  2.05
LINK         ND2 ASN A  19                 C1  NAG A 498     1555   1555  1.45
LINK         ND2 ASN B  19                 C6  NAG B 498     1555   1555  1.33
LINK         ND2 ASN C  19                 C1  NAG C 498     1555   1555  2.25
LINK         ND2 ASN D  19                 C1  NAG D 498     1555   1555  1.46
LINK         OD1 ASN B 146                 C1  NAG B 499     1555   1555  1.35
LINK         OD1 ASN B 146                 O5  NAG B 499     1555   1555  1.15
LINK         OG1 THR D  21                 C8  NAG D 498     1555   1555  1.34
CISPEP   1 LEU A  288    PRO A  289          0         3.04
CISPEP   2 GLY A  390    PRO A  391          0         1.04
CISPEP   3 GLY B   62    THR B   63          0       -17.71
CISPEP   4 LEU B  288    PRO B  289          0         2.03
CISPEP   5 GLY B  390    PRO B  391          0         1.97
CISPEP   6 LEU C  288    PRO C  289          0         2.26
CISPEP   7 GLY C  390    PRO C  391          0         1.53
CISPEP   8 LEU D  288    PRO D  289          0         2.13
CISPEP   9 GLY D  390    PRO D  391          0         2.64
SITE     1 AC1  6 ILE A   5  ASN A  19  HOH A 546  HOH A 716
SITE     2 AC1  6 HOH A 744  HOH A 816
SITE     1 AC2  8 ASN B  19  TYR B  22  HOH B 602  HOH B 617
SITE     2 AC2  8 HOH B 720  HOH B 822  HOH B 937  HOH B 964
SITE     1 AC3  6 THR B 138  ASN B 146  HOH B 652  HOH B 934
SITE     2 AC3  6 SER C  97  PRO C  98
SITE     1 AC4  5 ASN D  19  THR D  21  HOH D 590  HOH D 687
SITE     2 AC4  5 HOH D 942
SITE     1 AC5 11 ILE C   5  ASN C  19  THR C  21  HOH C1611
SITE     2 AC5 11 HOH C1895  HOH C1896  HOH C1902  HOH C1934
SITE     3 AC5 11 HOH C1968  HOH C1982  HOH C1984
SITE     1 AC6 10 SER C 242  TYR D  11  SER D  12  ARG D 353
SITE     2 AC6 10 SER D 356  TRP D 357  ASP D 358  HOH D 550
SITE     3 AC6 10 HOH D 770  HOH D 830
SITE     1 AC7  7 LYS D  79  TRP D 228  ARG D 277  HIS D 306
SITE     2 AC7  7 HOH D 650  HOH D 749  HOH D 876
SITE     1 AC8  9 SER A 242  TYR B  11  SER B  12  ARG B 353
SITE     2 AC8  9 SER B 356  TRP B 357  ASP B 358  HOH B 848
SITE     3 AC8  9 HOH B 899
SITE     1 AC9  7 TYR C  11  SER C  12  ARG C 353  SER C 356
SITE     2 AC9  7 TRP C 357  ASP C 358  HOH C1863
SITE     1 BC1  7 TYR A  11  SER A  12  ARG A 353  SER A 356
SITE     2 BC1  7 TRP A 357  ASP A 358  HOH A 813
SITE     1 BC2  6 LYS B  79  TRP B 228  ARG B 277  HIS B 306
SITE     2 BC2  6 HOH B 669  HOH B 755
SITE     1 BC3  5 LYS A  79  TRP A 228  ARG A 277  HIS A 306
SITE     2 BC3  5 HOH A 735
SITE     1 BC4  5 LYS C  79  TRP C 228  ARG C 277  HIS C 306
SITE     2 BC4  5 HOH C1782
SITE     1 BC5  4 ARG A  44  SER A  45  HOH A 643  HOH A 908
SITE     1 BC6  3 ARG C  44  SER C  45  HOH C1762
SITE     1 BC7  6 PRO D  29  GLU D 111  GLN D 169  ARG D 170
SITE     2 BC7  6 HOH D 607  HOH D 790
SITE     1 BC8  2 ARG A  44  TYR A 487
SITE     1 BC9  7 GLY D 193  LYS D 194  SER D 242  GLY D 243
SITE     2 BC9  7 HOH D 689  HOH D 727  HOH D 925
SITE     1 CC1  4 LYS B 321  ARG B 329  ARG C 329  LEU C 330
SITE     1 CC2  4 ARG B  44  SER B 465  TYR B 487  HOH B 941
SITE     1 CC3  6 GLY B 193  LYS B 194  SER B 242  GLY B 243
SITE     2 CC3  6 HOH B 603  HOH B 655
SITE     1 CC4  3 ARG D  44  SER D  45  HOH D 539
SITE     1 CC5  3 ARG B  44  SER B  45  HOH B 597
SITE     1 CC6  3 ARG A 329  LYS D 321  ARG D 329
SITE     1 CC7  3 ARG D  44  TYR D 487  HOH D 939
SITE     1 CC8  4 PHE C  75  HIS C 328  HIS C 374  HOH C1622
SITE     1 CC9 11 ASP B 127  PHE B 128  TRP B 179  ASN B 234
SITE     2 CC9 11 GLU B 235  PHE B 246  TYR B 313  GLU B 340
SITE     3 CC9 11 TRP B 381  ASN B 396  HOH B 868
SITE     1 DC1  9 ASP C 127  PHE C 128  TRP C 179  ASN C 234
SITE     2 DC1  9 GLU C 235  TYR C 313  GLU C 340  TRP C 381
SITE     3 DC1  9 PHE C 397
SITE     1 DC2 11 ASP D 127  PHE D 128  TRP D 179  ASN D 234
SITE     2 DC2 11 GLU D 235  PHE D 246  TYR D 313  GLU D 340
SITE     3 DC2 11 TRP D 381  ASN D 396  HOH D 880
SITE     1 DC3 10 ASP A 127  PHE A 128  TRP A 179  ASN A 234
SITE     2 DC3 10 GLU A 235  TYR A 313  GLU A 340  TRP A 381
SITE     3 DC3 10 PHE A 397  HOH A 833
SITE     1 DC4  9 PRO B 391  ASN B 392  ARG B 395  PHE B 397
SITE     2 DC4  9 HOH B 577  HOH B 598  VAL C 394  ARG C 395
SITE     3 DC4  9 HOH C1742
SITE     1 DC5  7 ARG D   2  ASP D  24  SER D  25  PHE D  26
SITE     2 DC5  7 ARG D  48  GOL D 508  HOH D 583
SITE     1 DC6  9 PRO D   3  CYS D   4  ARG D  48  MET D  49
SITE     2 DC6  9 GLU D  50  GOL D 507  HOH D 555  HOH D 667
SITE     3 DC6  9 HOH D 798
SITE     1 DC7  7 ASP B  24  SER B  25  PHE B  26  ARG B  48
SITE     2 DC7  7 MET B  49  HOH B 574  HOH B 592
SITE     1 DC8  9 ASP A  24  SER A  25  PHE A  26  ARG A  48
SITE     2 DC8  9 MET A  49  TYR A 418  HOH A 644  HOH A 760
SITE     3 DC8  9 HOH A 842
SITE     1 DC9  8 ARG C   2  ASP C  24  SER C  25  PHE C  26
SITE     2 DC9  8 ARG C  48  MET C  49  HOH C1774  HOH C1866
SITE     1 EC1  6 PRO C 289  LYS C 293  GOL C1595  HOH C1801
SITE     2 EC1  6 HOH C1889  PRO D 319
SITE     1 EC2  3 HIS C 290  LYS C 293  GOL C1594
CRYST1  107.941   91.759  152.810  90.00 110.96  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      0.009264  0.000000  0.003549        0.00000
SCALE2      0.000000  0.010898  0.000000        0.00000
SCALE3      0.000000  0.000000  0.007008        0.00000
      
PROCHECK
Go to PROCHECK summary
 References