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PDBsum entry 3keh

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Top Page protein ligands Protein-protein interface(s) links
Hydrolase PDB id
3keh
Jmol
Contents
Protein chain
497 a.a.
Ligands
NDG
SO4 ×8
GOL ×2
NAG ×2
NAG-NAG
Waters ×42
HEADER    HYDROLASE                               26-OCT-09   3KEH
TITLE     CRYSTAL STRUCTURE OF N370S GLUCOCEREBROSIDASE MUTANT AT PH 7.4
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: GLUCOCEREBROSIDASE;
COMPND   3 CHAIN: A, B;
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;
COMPND   8 MUTATION: 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: SPODOPTERA FRUGIPERDA;
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 7108
KEYWDS    GLUCOCEREBROSIDASE, ACID-BETA-GLUCOSIDASE, N370S, GLUCOSYCEREMIDASE,
KEYWDS   2 TIM BARREL, ALTERNATIVE INITIATION, DISEASE MUTATION, DISULFIDE
KEYWDS   3 BOND, GAUCHER DISEASE, GLYCOPROTEIN, GLYCOSIDASE, HYDROLASE,
KEYWDS   4 ICHTHYOSIS, LIPID METABOLISM, LYSOSOME, MEMBRANE, SPHINGOLIPID
KEYWDS   5 METABOLISM
EXPDTA    X-RAY DIFFRACTION
AUTHOR    R.R.WEI,S.BOUCHER,C.Q.PAN,T.EDMUNDS
REVDAT   1   27-OCT-10 3KEH    0
JRNL        AUTH   R.R.WEI,S.BOUCHER,H.HUGHES,N.GUZIEWICA,S.VANPATTEN,C.Q.PAN,
JRNL        AUTH 2 T.EDMUNDS
JRNL        TITL   CRYSTAL STRUCTURE OF GLUCOCEREBROSIDASE CONTAINING THE N370S
JRNL        TITL 2 MUTATION: IMPLICATION ON CHAPERON THERAPY
JRNL        REF    TO BE PUBLISHED
JRNL        REFN
REMARK   2
REMARK   2 RESOLUTION.    2.80 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : REFMAC 5.5.0088
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) : 2.80
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 50.00
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000
REMARK   3   COMPLETENESS FOR RANGE        (%) : 94.2
REMARK   3   NUMBER OF REFLECTIONS             : 31773
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) : 0.215
REMARK   3   R VALUE            (WORKING SET) : 0.212
REMARK   3   FREE R VALUE                     : 0.273
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100
REMARK   3   FREE R VALUE TEST SET COUNT      : 1698
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) : 2.80
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.87
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 2249
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 90.36
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3310
REMARK   3   BIN FREE R VALUE SET COUNT          : 104
REMARK   3   BIN FREE R VALUE                    : 0.4080
REMARK   3
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK   3   PROTEIN ATOMS            : 7857
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 109
REMARK   3   SOLVENT ATOMS            : 42
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : 39.50
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 28.11
REMARK   3   OVERALL ANISOTROPIC B VALUE.
REMARK   3    B11 (A**2) : 5.68000
REMARK   3    B22 (A**2) : -1.67000
REMARK   3    B33 (A**2) : -4.01000
REMARK   3    B12 (A**2) : 0.00000
REMARK   3    B13 (A**2) : 0.00000
REMARK   3    B23 (A**2) : 0.00000
REMARK   3
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.
REMARK   3   ESU BASED ON R VALUE                            (A): NULL
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.399
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.303
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 15.352
REMARK   3
REMARK   3 CORRELATION COEFFICIENTS.
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.914
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.853
REMARK   3
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  8202 ; 0.015 ; 0.022
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 11189 ; 1.605 ; 1.960
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   992 ; 7.050 ; 5.000
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   358 ;36.124 ;23.352
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  1262 ;18.394 ;15.000
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    44 ;19.315 ;15.000
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  1215 ; 0.103 ; 0.200
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  6274 ; 0.007 ; 0.021
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL
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):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL
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):  4971 ; 0.625 ; 1.500
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  8037 ; 1.195 ; 2.000
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  3231 ; 1.747 ; 3.000
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  3152 ; 2.915 ; 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   : 1.40
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 3KEH COMPLIES WITH FORMAT V. 3.20, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 29-OCT-09.
REMARK 100 THE RCSB ID CODE IS RCSB055890.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 28-FEB-09
REMARK 200  TEMPERATURE           (KELVIN) : 100
REMARK 200  PH                             : 7.4
REMARK 200  NUMBER OF CRYSTALS USED        : 1
REMARK 200
REMARK 200  SYNCHROTRON              (Y/N) : Y
REMARK 200  RADIATION SOURCE               : ALS
REMARK 200  BEAMLINE                       : 5.0.3
REMARK 200  X-RAY GENERATOR MODEL          : NULL
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9765
REMARK 200  MONOCHROMATOR                  : SINGLE CRYSTAL, CYLINDRICALLY
REMARK 200                                   BENT, SI(220)
REMARK 200  OPTICS                         : NULL
REMARK 200
REMARK 200  DETECTOR TYPE                  : CCD
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315R
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200  DATA SCALING SOFTWARE          : SCALA
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 31773
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.800
REMARK 200  RESOLUTION RANGE LOW       (A) : 85.000
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 94.7
REMARK 200  DATA REDUNDANCY                : 5.200
REMARK 200  R MERGE                    (I) : NULL
REMARK 200  R SYM                      (I) : 0.15800
REMARK 200   FOR THE DATA SET  : 8.4000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.80
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.88
REMARK 200  COMPLETENESS FOR SHELL     (%) : 91.1
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.40
REMARK 200  R MERGE FOR SHELL          (I) : NULL
REMARK 200  R SYM FOR SHELL            (I) : 0.35500
REMARK 200   FOR SHELL         : 2.300
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: !OGS
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 61.40
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.19
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.7M POTASSIUM PHOSPHATE/0.7M SODIUM
REMARK 280  PHOSPHATE/0.1M HEPES, PH7.4, VAPOR DIFFUSION, SITTING DROP,
REMARK 280  TEMPERATURE 294K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 21
REMARK 290
REMARK 290      SYMOP   SYMMETRY
REMARK 290     NNNMMM   OPERATOR
REMARK 290       1555   X,Y,Z
REMARK 290       2555   -X,-Y,Z+1/2
REMARK 290       3555   -X,Y,-Z+1/2
REMARK 290       4555   X,-Y,-Z
REMARK 290       5555   X+1/2,Y+1/2,Z
REMARK 290       6555   -X+1/2,-Y+1/2,Z+1/2
REMARK 290       7555   -X+1/2,Y+1/2,-Z+1/2
REMARK 290       8555   X+1/2,-Y+1/2,-Z
REMARK 290
REMARK 290     WHERE NNN -> OPERATOR NUMBER
REMARK 290           MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       46.00000
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000        0.00000
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       46.00000
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000
REMARK 290   SMTRY1   5  1.000000  0.000000  0.000000       53.91500
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000      142.96000
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000        0.00000
REMARK 290   SMTRY1   6 -1.000000  0.000000  0.000000       53.91500
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000      142.96000
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       46.00000
REMARK 290   SMTRY1   7 -1.000000  0.000000  0.000000       53.91500
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000      142.96000
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000       46.00000
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000       53.91500
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000      142.96000
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000        0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3
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: DIMERIC
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
REMARK 350 BIOMOLECULE: 2
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 4600 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 36450 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -109.0 KCAL/MOL
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 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350   BIOMT1   2  1.000000  0.000000  0.000000      -53.91500
REMARK 350   BIOMT2   2  0.000000 -1.000000  0.000000      142.96000
REMARK 350   BIOMT3   2  0.000000  0.000000 -1.000000        0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 3
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 13640 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 68460 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -239.0 KCAL/MOL
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   BIOMT1   2 -1.000000  0.000000  0.000000        0.00000
REMARK 350   BIOMT2   2  0.000000  1.000000  0.000000        0.00000
REMARK 350   BIOMT3   2  0.000000  0.000000 -1.000000       46.00000
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350   BIOMT1   3 -1.000000  0.000000  0.000000       53.91500
REMARK 350   BIOMT2   3  0.000000 -1.000000  0.000000      142.96000
REMARK 350   BIOMT3   3  0.000000  0.000000  1.000000       46.00000
REMARK 350   BIOMT1   4  1.000000  0.000000  0.000000      -53.91500
REMARK 350   BIOMT2   4  0.000000 -1.000000  0.000000      142.96000
REMARK 350   BIOMT3   4  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   OH   TYR A   363     OD1  ASP A   380              2.06
REMARK 500   O    LEU B   281     O    ALA B   309              2.08
REMARK 500   OH   TYR B   363     OD1  ASP B   380              2.15
REMARK 500   O    PRO B     3     OH   TYR B    22              2.18
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
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   RES CSSEQI ATM2   DEVIATION
REMARK 500    CYS A  23   CB    CYS A  23   SG      0.116
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 167   CA  -  CB  -  CG  ANGL. DEV. =  14.7 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     -157.66   -110.80
REMARK 500    ALA A  33      132.48    -32.38
REMARK 500    PHE A  75     -146.57   -120.53
REMARK 500    ALA A 124     -169.34     85.18
REMARK 500    PHE A 128       53.62    -92.32
REMARK 500    ALA A 136       83.15   -159.49
REMARK 500    LEU A 144       69.93     60.18
REMARK 500    LEU A 156      -62.76   -104.76
REMARK 500    LYS A 194       97.20    -54.12
REMARK 500    LYS A 224       60.44     68.92
REMARK 500    LEU A 281       59.75     38.81
REMARK 500    ALA A 318       98.15   -168.92
REMARK 500    THR A 323      -79.18    -98.24
REMARK 500    LYS A 346      119.27    -32.13
REMARK 500    TRP A 381     -100.85    -82.78
REMARK 500    ARG A 395      142.92   -175.09
REMARK 500    PHE A 397       -1.68   -141.38
REMARK 500    ASP A 399     -179.47    -69.36
REMARK 500    ASP A 409       23.32     41.61
REMARK 500    PHE A 423      -63.34   -102.25
REMARK 500    LEU A 436      108.74   -161.96
REMARK 500    HIS A 451      162.64    -49.06
REMARK 500    ASN B  19     -158.07   -137.81
REMARK 500    PHE B  75     -147.93   -122.64
REMARK 500    ALA B 124     -160.27     90.22
REMARK 500    CYS B 126     -163.76   -110.13
REMARK 500    PHE B 128       54.71    -93.02
REMARK 500    LEU B 156      -72.13   -118.08
REMARK 500    GLU B 233      146.34   -178.26
REMARK 500    GLU B 235       55.83     32.12
REMARK 500    LEU B 249      113.16   -175.94
REMARK 500    ASP B 263      -74.08   -120.81
REMARK 500    HIS B 274      -36.70    -38.92
REMARK 500    LEU B 281       71.97     37.84
REMARK 500    THR B 323      -82.48    -95.90
REMARK 500    TRP B 381     -119.42    -79.43
REMARK 500    ASN B 396       44.03    -91.55
REMARK 500    PHE B 423      -63.35   -105.88
REMARK 500    GLN B 440      154.23    178.37
REMARK 500    ASN B 442      154.22    175.72
REMARK 500    VAL B 477      -32.65   -130.43
REMARK 500
REMARK 500 REMARK: NULL
REMARK 610
REMARK 610 MISSING HETEROATOM
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 610 I=INSERTION CODE):
REMARK 610   M RES C SSEQI
REMARK 610     NDG A 1997
REMARK 610     NAG A 1998
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NDG A 1997
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 1501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 1502
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 1504
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 1506
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 1507
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 1509
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 1503
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 1504
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 1499
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 1500
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 1502
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 1505
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 498
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3KE0   RELATED DB: PDB
REMARK 900 THE SAME PROTEIN CRYSTALLIZED AT PH5.4
DBREF  3KEH A    1   497  UNP    P04062   GLCM_HUMAN      40    536
DBREF  3KEH B    1   497  UNP    P04062   GLCM_HUMAN      40    536
SEQADV 3KEH SER A  370  UNP  P04062    ASN   409 ENGINEERED
SEQADV 3KEH SER B  370  UNP  P04062    ASN   409 ENGINEERED
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 SER 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  ARG 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 SER 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  ARG ARG GLN
MODRES 3KEH ASN B   19  ASN  GLYCOSYLATION SITE
MODRES 3KEH ASN B  146  ASN  GLYCOSYLATION SITE
HET    NDG  A1997      14
HET    SO4  A1501       5
HET    SO4  A1502       5
HET    SO4  A1504       5
HET    SO4  A1506       5
HET    SO4  A1507       5
HET    GOL  A1509       6
HET    NAG  A1998       1
HET    NAG  B1503      14
HET    NAG  B1504      14
HET    SO4  B1499       5
HET    SO4  B1500       5
HET    SO4  B1502       5
HET    NAG  B1505      14
HET    GOL  B 498       6
HETNAM     NDG 2-(ACETYLAMINO)-2-DEOXY-A-D-GLUCOPYRANOSE
HETNAM     SO4 SULFATE ION
HETNAM     GOL GLYCEROL
HETNAM     NAG N-ACETYL-D-GLUCOSAMINE
HETSYN     GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL   3  NDG    C8 H15 N O6
FORMUL   4  SO4    8(O4 S 2-)
FORMUL   9  GOL    2(C3 H8 O3)
FORMUL  10  NAG    4(C8 H15 N O6)
FORMUL  17  HOH   *42(H2 O)
HELIX    1   1 THR A   86  LEU A   96  1                                  11
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 SER A  237  LEU A  241  5                                   5
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
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  ILE A 403   O  TYR A 412
SHEET    5   A 5 ALA A 384  LEU A 385  1  N  LEU A 385   O  VAL A 404
SHEET    1   B 9 ARG A  48  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 460   O  HIS A 490
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  THR A 471   N  LEU A  67
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  ILE A 118   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 VAL A 305  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 5 PRO B   6  LYS B   7  0
SHEET    2   D 5 VAL B  15  CYS B  18 -1  O  VAL B  15   N  LYS B   7
SHEET    3   D 5 THR B 410  LYS B 413 -1  O  PHE B 411   N  CYS B  18
SHEET    4   D 5 ILE B 402  ASP B 405 -1  N  ILE B 403   O  TYR B 412
SHEET    5   D 5 ALA B 384  LEU B 385  1  N  LEU B 385   O  VAL B 404
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  VAL B 460   O  HIS B 490
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  VAL B 437 -1  N  VAL B 434   O  ALA B 448
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  ILE B 118   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  PHE B 337   N  VAL B 310
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
SSBOND   1 CYS A    4    CYS A   16                          1555   1555  2.08
SSBOND   2 CYS A   18    CYS A   23                          1555   1555  2.09
SSBOND   3 CYS B    4    CYS B   16                          1555   1555  2.10
SSBOND   4 CYS B   18    CYS B   23                          1555   1555  2.13
LINK         ND2 ASN B  19                 C1  NAG B1503     1555   1555  1.46
LINK         ND2 ASN B 146                 C1  NAG B1505     1555   1555  1.47
LINK         O4  NAG B1503                 C1  NAG B1504     1555   1555  1.47
CISPEP   1 LEU A  288    PRO A  289          0        -4.27
CISPEP   2 GLY A  390    PRO A  391          0        11.30
CISPEP   3 LEU B  288    PRO B  289          0         2.97
CISPEP   4 GLY B  390    PRO B  391          0         4.63
SITE     1 AC1  2 ASN A  19  THR A  21
SITE     1 AC2  3 GLU A 254  ARG A 257  VAL A 294
SITE     1 AC3  3 GLN A 169  ARG A 170  PRO A 428
SITE     1 AC4  7 TYR A  11  SER A  12  ARG A 353  SER A 356
SITE     2 AC4  7 TRP A 357  ASP A 358  HOH A 509
SITE     1 AC5  4 LYS A  79  TRP A 228  ARG A 277  HIS A 306
SITE     1 AC6  4 ARG A 329  LEU A 330  LYS B 321  ARG B 329
SITE     1 AC7  6 ASP A  24  SER A  25  PHE A  26  ARG A  48
SITE     2 AC7  6 MET A  49  TYR A 418
SITE     1 AC8  2 ASN B  19  NAG B1504
SITE     1 AC9  1 NAG B1503
SITE     1 BC1  4 LYS B  79  TRP B 228  ARG B 277  HIS B 306
SITE     1 BC2  7 SER A 242  TYR B  11  SER B  12  ARG B 353
SITE     2 BC2  7 SER B 356  TRP B 357  ASP B 358
SITE     1 BC3  3 ARG B  44  SER B 465  TYR B 487
SITE     1 BC4  2 HOH A 506  ASN B 146
SITE     1 BC5  9 ASP B 127  PHE B 128  TRP B 179  ASN B 234
SITE     2 BC5  9 GLU B 235  PHE B 246  GLU B 340  TRP B 381
SITE     3 BC5  9 ASN B 396
CRYST1  107.830  285.920   92.000  90.00  90.00  90.00 C 2 2 21     16
ORIGX1      1.000000  0.000000  0.000000        0.00000
ORIGX2      0.000000  1.000000  0.000000        0.00000
ORIGX3      0.000000  0.000000  1.000000        0.00000
SCALE1      0.009274  0.000000  0.000000        0.00000
SCALE2      0.000000  0.003497  0.000000        0.00000
SCALE3      0.000000  0.000000  0.010870        0.00000
      
PROCHECK
Go to PROCHECK summary
 References