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PDBsum entry 2vt0

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Top Page protein ligands Protein-protein interface(s) links
Hydrolase PDB id
2vt0
Jmol
Contents
Protein chain
495 a.a.
Ligands
CBU ×2
NAG-NAG-MAN
SO4 ×10
FUC ×2
NAG-NAG
Waters ×464
HEADER    HYDROLASE                               03-MAY-08   2VT0
TITLE     X-RAY STRUCTURE OF A CONJUGATE WITH CONDURITOL-BETA-EPOXIDE
TITLE    2 OF ACID-BETA-GLUCOSIDASE OVEREXPRESSED IN CULTURED PLANT
TITLE    3 CELLS
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: GLUCOSYLCERAMIDASE;
COMPND   3 CHAIN: A, B;
COMPND   4 FRAGMENT: TIM BARREL GLUCOSIDASE, RESIDUES 40-536;
COMPND   5 SYNONYM: BETA-GLUCOCEREBROSIDASE, ACID BETA-GLUCOSIDASE,
COMPND   6  D-GLUCOSYL-N-ACYLSPHINGOSINE GLUCOHYDROLASE, GLUCOSIDASE;
COMPND   7 EC: 3.2.1.45;
COMPND   8 ENGINEERED: YES;
COMPND   9 OTHER_DETAILS: THE ENZYME IS COVALENTLY INHIBITED BY CBE
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE   3 ORGANISM_COMMON: HUMAN;
SOURCE   4 ORGANISM_TAXID: 9606;
SOURCE   5 ORGAN: LYSOSOME;
SOURCE   6 EXPRESSION_SYSTEM: DAUCUS CAROTA;
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 4039
KEYWDS    HYDROLASE, ALTERNATIVE INITIATION, SPHINGOLIPID METABOLISM,
KEYWDS   2 ISRAEL STRUCTURAL PROTEOMICS CENTER, DISEASE MUTATION,
KEYWDS   3 GLUCOCEREBROSIDASE, PHARMACEUTICAL, GAUCHER DISEASE, LIPID
KEYWDS   4 METABOLISM, GLUCOSIDASE, GLYCOSIDASE, POLYMORPHISM,
KEYWDS   5 GLYCOPROTEIN, ISPC, MEMBRANE, CEREZYME, LYSOSOME,
KEYWDS   6 STRUCTURAL GENOMICS, ALTERNATIVE SPLICING
EXPDTA    X-RAY DIFFRACTION
AUTHOR    B.BRUMSHTEIN,H.M.GREENBLATT,Y.SHAALTIEL,D.AVIEZER,I.SILMAN,
AUTHOR   2 A.H.FUTERMAN,J.L.SUSSMAN
REVDAT   3   10-OCT-12 2VT0    1       JRNL   REMARK VERSN  FORMUL
REVDAT   3 2                           SITE
REVDAT   2   24-FEB-09 2VT0    1       VERSN
REVDAT   1   23-SEP-08 2VT0    0
JRNL        AUTH   Y.KACHER,B.BRUMSHTEIN,S.BOLDIN-ADAMSKY,L.TOKER,A.SHAINSKAYA,
JRNL        AUTH 2 I.SILMAN,J.L.SUSSMAN,A.H.FUTERMAN
JRNL        TITL   ACID BETA-GLUCOSIDASE: INSIGHTS FROM STRUCTURAL ANALYSIS
JRNL        TITL 2 AND RELEVANCE TO GAUCHER DISEASE THERAPY.
JRNL        REF    BIOL.CHEM.                    V. 389  1361 2008
JRNL        REFN                   ISSN 1431-6730
JRNL        PMID   18783340
JRNL        DOI    10.1515/BC.2008.163
REMARK   2
REMARK   2 RESOLUTION.    2.15 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : REFMAC 5.4.0067
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) : 2.15
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 19.77
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.2
REMARK   3   NUMBER OF REFLECTIONS             : 53238
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) : 0.154
REMARK   3   R VALUE            (WORKING SET) : 0.152
REMARK   3   FREE R VALUE                     : 0.201
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100
REMARK   3   FREE R VALUE TEST SET COUNT      : 2838
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) : 2.15
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.21
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 3474
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2000
REMARK   3   BIN FREE R VALUE SET COUNT          : 201
REMARK   3   BIN FREE R VALUE                    : 0.2560
REMARK   3
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK   3   PROTEIN ATOMS            : 7723
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 159
REMARK   3   SOLVENT ATOMS            : 464
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : NULL
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 22.18
REMARK   3   OVERALL ANISOTROPIC B VALUE.
REMARK   3    B11 (A**2) : 0.00000
REMARK   3    B22 (A**2) : 0.00000
REMARK   3    B33 (A**2) : 0.00000
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): 0.217
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.175
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.117
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 4.520
REMARK   3
REMARK   3 CORRELATION COEFFICIENTS.
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.964
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.939
REMARK   3
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  8119 ; 0.025 ; 0.022
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 11089 ; 1.993 ; 1.963
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   979 ; 7.228 ; 5.000
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   349 ;36.583 ;23.381
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  1218 ;14.264 ;15.000
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    40 ;23.574 ;15.000
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  1226 ; 0.140 ; 0.200
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  6145 ; 0.011 ; 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):  4907 ; 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):  7912 ; 1.765 ; 2.000
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  3212 ; 3.000 ; 3.000
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  3177 ; 4.543 ; 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 : 1
REMARK   3
REMARK   3  NCS GROUP NUMBER               : 1
REMARK   3     CHAIN NAMES                    : A B
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 3
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE
REMARK   3           1     A      1       A     162      2
REMARK   3           1     B      1       B     162      2
REMARK   3           2     A    167       A     450      2
REMARK   3           2     B    167       B     450      2
REMARK   3           3     A    452       A     496      2
REMARK   3           3     B    452       B     496      2
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT
REMARK   3   TIGHT POSITIONAL   1    A    (A):   1936 ;  0.06 ;  0.05
REMARK   3   TIGHT POSITIONAL   1    B    (A):   1936 ;  0.06 ;  0.05
REMARK   3   MEDIUM POSITIONAL  1    A    (A):   1848 ;  0.10 ;  0.50
REMARK   3   MEDIUM POSITIONAL  1    B    (A):   1848 ;  0.10 ;  0.50
REMARK   3   TIGHT THERMAL      1    A (A**2):   1936 ;  0.27 ;  0.50
REMARK   3   TIGHT THERMAL      1    B (A**2):   1936 ;  0.27 ;  0.50
REMARK   3   MEDIUM THERMAL     1    A (A**2):   1848 ;  0.32 ;  2.00
REMARK   3   MEDIUM THERMAL     1    B (A**2):   1848 ;  0.32 ;  2.00
REMARK   3
REMARK   3  TLS DETAILS
REMARK   3   NUMBER OF TLS GROUPS  : NULL
REMARK   3
REMARK   3  BULK SOLVENT MODELLING.
REMARK   3   METHOD USED : MASK
REMARK   3   PARAMETERS FOR MASK CALCULATION
REMARK   3   VDW PROBE RADIUS   : 1.20
REMARK   3   ION PROBE RADIUS   : 0.80
REMARK   3   SHRINKAGE RADIUS   : 0.80
REMARK   3
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE
REMARK   3  RIDING POSITIONS. RESIDUES 27-31 ON CHAIN A AND 27-33 ON CHAIN
REMARK   3  B ARE NOT VISIBLE IN ELECTRON DENSITY, HENCE ARE MISSING
REMARK   4
REMARK   4 2VT0 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON  07-MAY-08.
REMARK 100 THE PDBE ID CODE IS EBI-35997.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 03-FEB-08
REMARK 200  TEMPERATURE           (KELVIN) : 100
REMARK 200  PH                             : 6.5
REMARK 200  NUMBER OF CRYSTALS USED        : 1
REMARK 200
REMARK 200  SYNCHROTRON              (Y/N) : Y
REMARK 200  RADIATION SOURCE               : ESRF
REMARK 200  BEAMLINE                       : ID29
REMARK 200  X-RAY GENERATOR MODEL          : NULL
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.979
REMARK 200  MONOCHROMATOR                  : SI
REMARK 200  OPTICS                         : NULL
REMARK 200
REMARK 200  DETECTOR TYPE                  : CCD
REMARK 200  DETECTOR MANUFACTURER          : ADSC
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL2000ONE
REMARK 200  DATA SCALING SOFTWARE          : HKL2000
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 59355
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.10
REMARK 200  RESOLUTION RANGE LOW       (A) : 20.00
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.0
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 97.1
REMARK 200  DATA REDUNDANCY                : 3.6
REMARK 200  R MERGE                    (I) : 0.09
REMARK 200  R SYM                      (I) : NULL
REMARK 200   FOR THE DATA SET  : 10.40
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.10
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.17
REMARK 200  COMPLETENESS FOR SHELL     (%) : 82.7
REMARK 200  DATA REDUNDANCY IN SHELL       : 1.9
REMARK 200  R MERGE FOR SHELL          (I) : 0.41
REMARK 200  R SYM FOR SHELL            (I) : NULL
REMARK 200   FOR SHELL         : 1.73
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: PDB ENTRY 2V3F
REMARK 200
REMARK 200 REMARK: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 48
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.4
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2M AMMONIUM SULFATE; 0.1M
REMARK 280  TRIS PH 6.5; 25% W/V PEG 3350; CRYSTALLIZATION UNDER OIL
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       48.44200
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PQS
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PQS
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 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465   M RES C SSSEQI
REMARK 465     ASP A    27
REMARK 465     PRO A    28
REMARK 465     PRO A    29
REMARK 465     THR A    30
REMARK 465     PHE A    31
REMARK 465     LEU A   499
REMARK 465     VAL A   500
REMARK 465     ASP A   501
REMARK 465     THR A   502
REMARK 465     MET A   503
REMARK 465     GLU B    -1
REMARK 465     PHE B     0
REMARK 465     ASP B    27
REMARK 465     PRO B    28
REMARK 465     PRO B    29
REMARK 465     THR B    30
REMARK 465     PHE B    31
REMARK 465     PRO B    32
REMARK 465     ALA B    33
REMARK 465     GLN B   497
REMARK 465     LEU B   498
REMARK 465     LEU B   499
REMARK 465     VAL B   500
REMARK 465     ASP B   501
REMARK 465     THR B   502
REMARK 465     MET B   503
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470   M RES CSSEQI  ATOMS
REMARK 470     GLU A  -1    CG   CD   OE1  OE2
REMARK 470     LEU A  34    CG   CD1  CD2
REMARK 470     GLN A 169    CG   CD   OE1  NE2
REMARK 470     LYS A 224    CE   NZ
REMARK 470     GLU A 300    CD   OE1  OE2
REMARK 470     LYS A 441    CG   CD   CE   NZ
REMARK 470     LYS A 466    CG   CD   CE   NZ
REMARK 470     LEU A 498    CA   C    O    CB   CG   CD1  CD2
REMARK 470     ARG B   2    CZ   NH1  NH2
REMARK 470     LEU B  34    CG   CD1  CD2
REMARK 470     ASN B  59    CG   OD1  ND2
REMARK 470     GLU B 111    CG   CD   OE1  OE2
REMARK 470     GLU B 112    CG   CD   OE1  OE2
REMARK 470     ARG B 211    CG   CD   NE   CZ   NH1  NH2
REMARK 470     LYS B 303    NZ
REMARK 470     LYS B 441    CD   CE   NZ
REMARK 470     LYS B 466    CG   CD   CE   NZ
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   OD2  ASP A   298     O    HOH A  2128              2.16
REMARK 500   O    HOH A  2102     O    HOH A  2122              1.89
REMARK 500   O    HOH A  2153     O    HOH A  2159              1.98
REMARK 500   O    HOH B  2013     O    HOH B  2014              2.12
REMARK 500   O    HOH B  2021     O    HOH B  2221              2.09
REMARK 500   O    HOH B  2049     O    HOH B  2126              1.77
REMARK 500   O    HOH B  2076     O    HOH B  2206              2.19
REMARK 500   O    HOH B  2089     O    HOH B  2092              2.12
REMARK 500   O    HOH B  2164     O    HOH B  2165              2.10
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    TYR A 212   CD1   TYR A 212   CE1     0.096
REMARK 500    ARG A 353   CZ    ARG A 353   NH2    -0.080
REMARK 500    TYR A 487   C     TYR A 487   O       0.136
REMARK 500    TRP B 184   CB    TRP B 184   CG      0.117
REMARK 500    ALA B 384   CA    ALA B 384   CB      0.130
REMARK 500    VAL B 394   CB    VAL B 394   CG1    -0.132
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    ARG A 131   NE  -  CZ  -  NH1 ANGL. DEV. =  -3.1 DEGREES
REMARK 500    ARG A 163   NE  -  CZ  -  NH1 ANGL. DEV. =   3.0 DEGREES
REMARK 500    ARG A 353   NE  -  CZ  -  NH2 ANGL. DEV. =   4.4 DEGREES
REMARK 500    ARG A 433   NE  -  CZ  -  NH1 ANGL. DEV. =   8.6 DEGREES
REMARK 500    ARG A 433   NE  -  CZ  -  NH2 ANGL. DEV. =  -8.9 DEGREES
REMARK 500    ARG A 463   NE  -  CZ  -  NH1 ANGL. DEV. =   3.5 DEGREES
REMARK 500    ARG B  39   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.6 DEGREES
REMARK 500    LEU B 317   CA  -  CB  -  CG  ANGL. DEV. =  17.5 DEGREES
REMARK 500    ARG B 353   NE  -  CZ  -  NH1 ANGL. DEV. =   3.6 DEGREES
REMARK 500    VAL B 457   CG1 -  CB  -  CG2 ANGL. DEV. = -12.2 DEGREES
REMARK 500    ARG B 463   NE  -  CZ  -  NH1 ANGL. DEV. =  -3.4 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    ALA A  33      151.31    -48.94
REMARK 500    MET A  49       49.77     39.78
REMARK 500    PHE A  75     -129.33   -122.82
REMARK 500    ALA A 124     -152.54     68.60
REMARK 500    PHE A 128       48.15    -81.90
REMARK 500    LEU A 156      -69.20   -107.93
REMARK 500    ASN A 192     -169.83   -120.58
REMARK 500    GLU A 233      139.96    177.11
REMARK 500    LEU A 249      108.46   -162.35
REMARK 500    LEU A 281      -84.94     71.82
REMARK 500    THR A 323      -74.16   -109.08
REMARK 500    HIS A 374        1.14     84.55
REMARK 500    TRP A 381     -132.70    -90.95
REMARK 500    ASN A 392      115.89   -166.76
REMARK 500    PHE B  75     -124.34   -115.97
REMARK 500    ALA B 124     -156.08     76.37
REMARK 500    LEU B 156      -68.90   -100.19
REMARK 500    ASN B 192     -163.39   -124.69
REMARK 500    GLU B 233      134.52    171.05
REMARK 500    LEU B 281      -81.64     68.30
REMARK 500    THR B 323      -75.17   -116.62
REMARK 500    HIS B 374       -0.88     87.09
REMARK 500    TRP B 381     -138.13    -88.23
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION.  CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS.  TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500                                 MODEL     OMEGA
REMARK 500 LEU A   34     GLY A   35                  -47.38
REMARK 500 ALA A  476     VAL A  477                 -142.94
REMARK 500
REMARK 500 REMARK: NULL
REMARK 600
REMARK 600 HETEROGEN
REMARK 600 CBU IS THE COVALENTLY BOUND FORM OF CONDURITOL-BETA-EPOXIDE,
REMARK 600  ONLY STEREOISOMER WAS EXPERIMENTALLY OBSERVED IN THE STRUCTURE
REMARK 700
REMARK 700 SHEET
REMARK 700 DETERMINATION METHOD: DSSP
REMARK 700 THE SHEETS PRESENTED AS "AC", "BC" IN EACH CHAIN ON SHEET RECORDS
REMARK 700 BELOW IS ACTUALLY AN  8-STRANDED BARREL THIS IS REPRESENTED BY
REMARK 700 A  9-STRANDED SHEET IN WHICH THE FIRST AND LAST STRANDS
REMARK 700 ARE IDENTICAL.
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CBU A1499
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CBU B1497
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR CHAIN A OF SUGAR BOUND TO
REMARK 800   ASN A  19 RESIDUES 1500 TO 1509
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR CHAIN B OF SUGAR BOUND TO
REMARK 800   ASN B  19 RESIDUES 1498 TO 1504
DBREF  2VT0 A   -1     0  PDB    2VT0     2VT0            -1      0
DBREF  2VT0 A    1   497  UNP    Q9BDT0   GLCM_PANTR      40    536
DBREF  2VT0 A  498   503  PDB    2VT0     2VT0           498    503
DBREF  2VT0 B   -1     0  PDB    2VT0     2VT0            -1      0
DBREF  2VT0 B    1   497  UNP    Q9BDT0   GLCM_PANTR      40    536
DBREF  2VT0 B  498   503  PDB    2VT0     2VT0           498    503
SEQADV 2VT0 PRO A   55  UNP  Q9BDT0    THR    94 CONFLICT
SEQADV 2VT0 HIS A  495  UNP  Q9BDT0    ARG   534 CONFLICT
SEQADV 2VT0 PRO B   55  UNP  Q9BDT0    THR    94 CONFLICT
SEQADV 2VT0 HIS B  495  UNP  Q9BDT0    ARG   534 CONFLICT
SEQRES   1 A  505  GLU PHE ALA ARG PRO CYS ILE PRO LYS SER PHE GLY TYR
SEQRES   2 A  505  SER SER VAL VAL CYS VAL CYS ASN ALA THR TYR CYS ASP
SEQRES   3 A  505  SER PHE ASP PRO PRO THR PHE PRO ALA LEU GLY THR PHE
SEQRES   4 A  505  SER ARG TYR GLU SER THR ARG SER GLY ARG ARG MET GLU
SEQRES   5 A  505  LEU SER MET GLY PRO ILE GLN ALA ASN HIS THR GLY THR
SEQRES   6 A  505  GLY LEU LEU LEU THR LEU GLN PRO GLU GLN LYS PHE GLN
SEQRES   7 A  505  LYS VAL LYS GLY PHE GLY GLY ALA MET THR ASP ALA ALA
SEQRES   8 A  505  ALA LEU ASN ILE LEU ALA LEU SER PRO PRO ALA GLN ASN
SEQRES   9 A  505  LEU LEU LEU LYS SER TYR PHE SER GLU GLU GLY ILE GLY
SEQRES  10 A  505  TYR ASN ILE ILE ARG VAL PRO MET ALA SER CYS ASP PHE
SEQRES  11 A  505  SER ILE ARG THR TYR THR TYR ALA ASP THR PRO ASP ASP
SEQRES  12 A  505  PHE GLN LEU HIS ASN PHE SER LEU PRO GLU GLU ASP THR
SEQRES  13 A  505  LYS LEU LYS ILE PRO LEU ILE HIS ARG ALA LEU GLN LEU
SEQRES  14 A  505  ALA GLN ARG PRO VAL SER LEU LEU ALA SER PRO TRP THR
SEQRES  15 A  505  SER PRO THR TRP LEU LYS THR ASN GLY ALA VAL ASN GLY
SEQRES  16 A  505  LYS GLY SER LEU LYS GLY GLN PRO GLY ASP ILE TYR HIS
SEQRES  17 A  505  GLN THR TRP ALA ARG TYR PHE VAL LYS PHE LEU ASP ALA
SEQRES  18 A  505  TYR ALA GLU HIS LYS LEU GLN PHE TRP ALA VAL THR ALA
SEQRES  19 A  505  GLU ASN GLU PRO SER ALA GLY LEU LEU SER GLY TYR PRO
SEQRES  20 A  505  PHE GLN CYS LEU GLY PHE THR PRO GLU HIS GLN ARG ASP
SEQRES  21 A  505  PHE ILE ALA ARG ASP LEU GLY PRO THR LEU ALA ASN SER
SEQRES  22 A  505  THR HIS HIS ASN VAL ARG LEU LEU MET LEU ASP ASP GLN
SEQRES  23 A  505  ARG LEU LEU LEU PRO HIS TRP ALA LYS VAL VAL LEU THR
SEQRES  24 A  505  ASP PRO GLU ALA ALA LYS TYR VAL HIS GLY ILE ALA VAL
SEQRES  25 A  505  HIS TRP TYR LEU ASP PHE LEU ALA PRO ALA LYS ALA THR
SEQRES  26 A  505  LEU GLY GLU THR HIS ARG LEU PHE PRO ASN THR MET LEU
SEQRES  27 A  505  PHE ALA SER GLU ALA CYS VAL GLY SER LYS PHE TRP GLU
SEQRES  28 A  505  GLN SER VAL ARG LEU GLY SER TRP ASP ARG GLY MET GLN
SEQRES  29 A  505  TYR SER HIS SER ILE ILE THR ASN LEU LEU TYR HIS VAL
SEQRES  30 A  505  VAL GLY TRP THR ASP TRP ASN LEU ALA LEU ASN PRO GLU
SEQRES  31 A  505  GLY GLY PRO ASN TRP VAL ARG ASN PHE VAL ASP SER PRO
SEQRES  32 A  505  ILE ILE VAL ASP ILE THR LYS ASP THR PHE TYR LYS GLN
SEQRES  33 A  505  PRO MET PHE TYR HIS LEU GLY HIS PHE SER LYS PHE ILE
SEQRES  34 A  505  PRO GLU GLY SER GLN ARG VAL GLY LEU VAL ALA SER GLN
SEQRES  35 A  505  LYS ASN ASP LEU ASP ALA VAL ALA LEU MET HIS PRO ASP
SEQRES  36 A  505  GLY SER ALA VAL VAL VAL VAL LEU ASN ARG SER SER LYS
SEQRES  37 A  505  ASP VAL PRO LEU THR ILE LYS ASP PRO ALA VAL GLY PHE
SEQRES  38 A  505  LEU GLU THR ILE SER PRO GLY TYR SER ILE HIS THR TYR
SEQRES  39 A  505  LEU TRP HIS ARG GLN LEU LEU VAL ASP THR MET
SEQRES   1 B  505  GLU PHE ALA ARG PRO CYS ILE PRO LYS SER PHE GLY TYR
SEQRES   2 B  505  SER SER VAL VAL CYS VAL CYS ASN ALA THR TYR CYS ASP
SEQRES   3 B  505  SER PHE ASP PRO PRO THR PHE PRO ALA LEU GLY THR PHE
SEQRES   4 B  505  SER ARG TYR GLU SER THR ARG SER GLY ARG ARG MET GLU
SEQRES   5 B  505  LEU SER MET GLY PRO ILE GLN ALA ASN HIS THR GLY THR
SEQRES   6 B  505  GLY LEU LEU LEU THR LEU GLN PRO GLU GLN LYS PHE GLN
SEQRES   7 B  505  LYS VAL LYS GLY PHE GLY GLY ALA MET THR ASP ALA ALA
SEQRES   8 B  505  ALA LEU ASN ILE LEU ALA LEU SER PRO PRO ALA GLN ASN
SEQRES   9 B  505  LEU LEU LEU LYS SER TYR PHE SER GLU GLU GLY ILE GLY
SEQRES  10 B  505  TYR ASN ILE ILE ARG VAL PRO MET ALA SER CYS ASP PHE
SEQRES  11 B  505  SER ILE ARG THR TYR THR TYR ALA ASP THR PRO ASP ASP
SEQRES  12 B  505  PHE GLN LEU HIS ASN PHE SER LEU PRO GLU GLU ASP THR
SEQRES  13 B  505  LYS LEU LYS ILE PRO LEU ILE HIS ARG ALA LEU GLN LEU
SEQRES  14 B  505  ALA GLN ARG PRO VAL SER LEU LEU ALA SER PRO TRP THR
SEQRES  15 B  505  SER PRO THR TRP LEU LYS THR ASN GLY ALA VAL ASN GLY
SEQRES  16 B  505  LYS GLY SER LEU LYS GLY GLN PRO GLY ASP ILE TYR HIS
SEQRES  17 B  505  GLN THR TRP ALA ARG TYR PHE VAL LYS PHE LEU ASP ALA
SEQRES  18 B  505  TYR ALA GLU HIS LYS LEU GLN PHE TRP ALA VAL THR ALA
SEQRES  19 B  505  GLU ASN GLU PRO SER ALA GLY LEU LEU SER GLY TYR PRO
SEQRES  20 B  505  PHE GLN CYS LEU GLY PHE THR PRO GLU HIS GLN ARG ASP
SEQRES  21 B  505  PHE ILE ALA ARG ASP LEU GLY PRO THR LEU ALA ASN SER
SEQRES  22 B  505  THR HIS HIS ASN VAL ARG LEU LEU MET LEU ASP ASP GLN
SEQRES  23 B  505  ARG LEU LEU LEU PRO HIS TRP ALA LYS VAL VAL LEU THR
SEQRES  24 B  505  ASP PRO GLU ALA ALA LYS TYR VAL HIS GLY ILE ALA VAL
SEQRES  25 B  505  HIS TRP TYR LEU ASP PHE LEU ALA PRO ALA LYS ALA THR
SEQRES  26 B  505  LEU GLY GLU THR HIS ARG LEU PHE PRO ASN THR MET LEU
SEQRES  27 B  505  PHE ALA SER GLU ALA CYS VAL GLY SER LYS PHE TRP GLU
SEQRES  28 B  505  GLN SER VAL ARG LEU GLY SER TRP ASP ARG GLY MET GLN
SEQRES  29 B  505  TYR SER HIS SER ILE ILE THR ASN LEU LEU TYR HIS VAL
SEQRES  30 B  505  VAL GLY TRP THR ASP TRP ASN LEU ALA LEU ASN PRO GLU
SEQRES  31 B  505  GLY GLY PRO ASN TRP VAL ARG ASN PHE VAL ASP SER PRO
SEQRES  32 B  505  ILE ILE VAL ASP ILE THR LYS ASP THR PHE TYR LYS GLN
SEQRES  33 B  505  PRO MET PHE TYR HIS LEU GLY HIS PHE SER LYS PHE ILE
SEQRES  34 B  505  PRO GLU GLY SER GLN ARG VAL GLY LEU VAL ALA SER GLN
SEQRES  35 B  505  LYS ASN ASP LEU ASP ALA VAL ALA LEU MET HIS PRO ASP
SEQRES  36 B  505  GLY SER ALA VAL VAL VAL VAL LEU ASN ARG SER SER LYS
SEQRES  37 B  505  ASP VAL PRO LEU THR ILE LYS ASP PRO ALA VAL GLY PHE
SEQRES  38 B  505  LEU GLU THR ILE SER PRO GLY TYR SER ILE HIS THR TYR
SEQRES  39 B  505  LEU TRP HIS ARG GLN LEU LEU VAL ASP THR MET
HET    CBU  A1499      11
HET    CBU  B1497      11
HET    FUC  A1509      10
HET    NAG  A1500      14
HET    NAG  A1501      14
HET    MAN  A1502      11
HET    FUC  B1504      10
HET    NAG  B1498      14
HET    NAG  B1499      14
HET    SO4  A1503       5
HET    SO4  B1500       5
HET    SO4  B1501       5
HET    SO4  A1504       5
HET    SO4  A1505       5
HET    SO4  B1502       5
HET    SO4  A1506       5
HET    SO4  B1503       5
HET    SO4  A1507       5
HET    SO4  A1508       5
HETNAM     CBU (1R,2R,3S,4S,5S,6S)-CYCLOHEXANE-1,2,3,4,5,6-
HETNAM   2 CBU  HEXOL
HETNAM     SO4 SULFATE ION
HETNAM     MAN ALPHA-D-MANNOSE
HETNAM     FUC ALPHA-L-FUCOSE
HETNAM     NAG N-ACETYL-D-GLUCOSAMINE
FORMUL   3  CBU    2(C6 H12 O6)
FORMUL   4  SO4    10(O4 S 2-)
FORMUL   5  MAN    C6 H12 O6
FORMUL   6  FUC    2(C6 H12 O5)
FORMUL   7  NAG    4(C8 H15 N O6)
FORMUL   8  HOH   *464(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  LEU A  185  5                                   4
HELIX    6   6 ASP A  203  GLU A  222  1                                  20
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 LEU A  314  ALA A  318  5                                   5
HELIX   14  14 PRO A  319  PHE A  331  1                                  13
HELIX   15  15 SER A  356  TYR A  373  1                                  18
HELIX   16  16 ILE A  406  ASP A  409  5                                   4
HELIX   17  17 GLN A  414  LYS A  425  1                                  12
HELIX   18  18 THR B   86  ALA B   95  1                                  10
HELIX   19  19 SER B   97  SER B  110  1                                  14
HELIX   20  20 PRO B  150  LYS B  155  1                                   6
HELIX   21  21 LEU B  156  ALA B  168  1                                  13
HELIX   22  22 PRO B  182  LEU B  185  5                                   4
HELIX   23  23 ASP B  203  HIS B  223  1                                  21
HELIX   24  24 GLU B  235  LEU B  241  5                                   7
HELIX   25  25 THR B  252  ASP B  263  1                                  12
HELIX   26  26 ASP B  263  ASN B  270  1                                   8
HELIX   27  27 LEU B  286  LEU B  288  5                                   3
HELIX   28  28 PRO B  289  THR B  297  1                                   9
HELIX   29  29 ASP B  298  LYS B  303  1                                   6
HELIX   30  30 LEU B  314  ALA B  318  5                                   5
HELIX   31  31 THR B  323  PHE B  331  1                                   9
HELIX   32  32 SER B  356  TYR B  373  1                                  18
HELIX   33  33 ILE B  406  ASP B  409  5                                   4
HELIX   34  34 GLN B  414  LYS B  425  1                                  12
SHEET    1  AA 4 PRO A   6  LYS A   7  0
SHEET    2  AA 4 VAL A  15  CYS A  18 -1  O  VAL A  15   N  LYS A   7
SHEET    3  AA 4 THR A 410  LYS A 413 -1  O  PHE A 411   N  CYS A  18
SHEET    4  AA 4 ILE A 402  ASP A 405 -1  O  ILE A 403   N  TYR A 412
SHEET    1  AB 9 GLU A  50  PRO A  55  0
SHEET    2  AB 9 THR A  36  THR A  43 -1  O  PHE A  37   N  GLY A  54
SHEET    3  AB 9 SER A 488  TRP A 494 -1  O  ILE A 489   N  SER A  42
SHEET    4  AB 9 ALA A 456  ASN A 462 -1  O  ALA A 456   N  TRP A 494
SHEET    5  AB 9 LEU A 444  MET A 450 -1  O  ASP A 445   N  LEU A 461
SHEET    6  AB 9 GLN A 432  ALA A 438 -1  O  GLN A 432   N  MET A 450
SHEET    7  AB 9 LEU A  65  LYS A  77 -1  O  THR A  68   N  VAL A 437
SHEET    8  AB 9 VAL A 468  ASP A 474  1  O  PRO A 469   N  LEU A  65
SHEET    9  AB 9 GLY A 478  SER A 484 -1  O  GLY A 478   N  ASP A 474
SHEET    1  AC 9 GLY A  80  ALA A  84  0
SHEET    2  AC 9 GLY A 377  ASN A 382  1  O  TRP A 378   N  GLY A  82
SHEET    3  AC 9 MET A 335  GLU A 340  1  O  ALA A 338   N  THR A 379
SHEET    4  AC 9 GLY A 307  HIS A 311  1  O  ILE A 308   N  PHE A 337
SHEET    5  AC 9 ARG A 277  GLN A 284  1  O  MET A 280   N  ALA A 309
SHEET    6  AC 9 ALA A 229  THR A 231  1  O  VAL A 230   N  LEU A 279
SHEET    7  AC 9 SER A 173  PRO A 178  1  O  ALA A 176   N  THR A 231
SHEET    8  AC 9 ILE A 118  MET A 123  1  O  ILE A 119   N  LEU A 175
SHEET    9  AC 9 GLY A  80  ALA A  84  1  O  GLY A  83   N  ARG A 120
SHEET    1  BA 4 PRO B   6  LYS B   7  0
SHEET    2  BA 4 VAL B  15  CYS B  18 -1  O  VAL B  15   N  LYS B   7
SHEET    3  BA 4 THR B 410  LYS B 413 -1  O  PHE B 411   N  CYS B  18
SHEET    4  BA 4 ILE B 402  ASP B 405 -1  O  ILE B 403   N  TYR B 412
SHEET    1  BB 9 GLU B  50  PRO B  55  0
SHEET    2  BB 9 THR B  36  THR B  43 -1  O  PHE B  37   N  GLY B  54
SHEET    3  BB 9 SER B 488  TRP B 494 -1  O  ILE B 489   N  SER B  42
SHEET    4  BB 9 ALA B 456  ASN B 462 -1  O  ALA B 456   N  TRP B 494
SHEET    5  BB 9 LEU B 444  MET B 450 -1  O  ASP B 445   N  LEU B 461
SHEET    6  BB 9 GLN B 432  ALA B 438 -1  O  GLN B 432   N  MET B 450
SHEET    7  BB 9 LEU B  65  LYS B  77 -1  O  THR B  68   N  VAL B 437
SHEET    8  BB 9 VAL B 468  ASP B 474  1  O  PRO B 469   N  LEU B  65
SHEET    9  BB 9 GLY B 478  SER B 484 -1  O  GLY B 478   N  ASP B 474
SHEET    1  BC 9 GLY B  80  ALA B  84  0
SHEET    2  BC 9 VAL B 375  ASN B 382  1  O  TRP B 378   N  GLY B  82
SHEET    3  BC 9 MET B 335  GLU B 340  1  O  LEU B 336   N  VAL B 376
SHEET    4  BC 9 GLY B 307  HIS B 311  1  O  ILE B 308   N  PHE B 337
SHEET    5  BC 9 ARG B 277  GLN B 284  1  O  MET B 280   N  ALA B 309
SHEET    6  BC 9 ALA B 229  THR B 231  1  O  VAL B 230   N  LEU B 279
SHEET    7  BC 9 SER B 173  PRO B 178  1  O  ALA B 176   N  THR B 231
SHEET    8  BC 9 ILE B 118  MET B 123  1  O  ILE B 119   N  LEU B 175
SHEET    9  BC 9 GLY B  80  ALA B  84  1  O  GLY B  83   N  ARG B 120
SSBOND   1 CYS A    4    CYS A   16                          1555   1555  2.19
SSBOND   2 CYS A   18    CYS A   23                          1555   1555  2.21
SSBOND   3 CYS B    4    CYS B   16                          1555   1555  2.12
SSBOND   4 CYS B   18    CYS B   23                          1555   1555  2.23
LINK         ND2 ASN A  19                 C1  NAG A1500     1555   1555  1.47
LINK         OE2 GLU A 340                 C5  CBU A1499     1555   1555  1.47
LINK         O3  NAG A1500                 C1  FUC A1509     1555   1555  1.49
LINK         O4  NAG A1500                 C1  NAG A1501     1555   1555  1.43
LINK         O4  NAG A1501                 C1  MAN A1502     1555   1555  1.45
LINK         ND2 ASN B  19                 C1  NAG B1498     1555   1555  1.45
LINK         OE2 GLU B 340                 C5  CBU B1497     1555   1555  1.48
LINK         O3  NAG B1498                 C1  FUC B1504     1555   1555  1.47
LINK         O4  NAG B1498                 C1  NAG B1499     1555   1555  1.44
CISPEP   1 LEU A  288    PRO A  289          0         3.70
CISPEP   2 GLY A  390    PRO A  391          0         3.15
CISPEP   3 LEU B  288    PRO B  289          0         0.99
CISPEP   4 GLY B  390    PRO B  391          0         3.50
SITE     1 AC1 12 ASP A 127  PHE A 128  TRP A 179  ASN A 234
SITE     2 AC1 12 GLU A 235  PHE A 246  TYR A 313  GLU A 340
SITE     3 AC1 12 TRP A 381  ASN A 396  HOH A2224  HOH A2225
SITE     1 AC2 12 ASP B 127  PHE B 128  TRP B 179  ASN B 234
SITE     2 AC2 12 GLU B 235  PHE B 246  TYR B 313  GLU B 340
SITE     3 AC2 12 TRP B 381  ASN B 396  HOH B2226  HOH B2227
SITE     1 AC3 27 TYR A  11  SER A  12  ASN A  19  ARG A  44
SITE     2 AC3 27 SER A  45  LYS A  79  GLY A 193  LYS A 194
SITE     3 AC3 27 TRP A 228  SER A 242  GLY A 243  GLU A 254
SITE     4 AC3 27 ARG A 257  ARG A 277  HIS A 306  ARG A 353
SITE     5 AC3 27 SER A 356  TRP A 357  ASP A 358  TYR A 487
SITE     6 AC3 27 HOH A2012  HOH A2113  HOH A2226  HOH A2227
SITE     7 AC3 27 HOH A2228  HOH A2229  HOH A2230
SITE     1 AC4 26 TYR B  11  SER B  12  ASN B  19  TYR B  22
SITE     2 AC4 26 LYS B  79  GLY B 193  LYS B 194  TRP B 228
SITE     3 AC4 26 SER B 242  GLY B 243  GLU B 254  ARG B 257
SITE     4 AC4 26 ARG B 277  HIS B 306  ARG B 353  SER B 356
SITE     5 AC4 26 TRP B 357  ASP B 358  HOH B2009  HOH B2228
SITE     6 AC4 26 HOH B2229  HOH B2230  HOH B2231  HOH B2232
SITE     7 AC4 26 HOH B2233  HOH B2234
CRYST1   68.184   96.884   83.171  90.00 103.73  90.00 P 1 21 1      4
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      0.014666  0.000000  0.003583        0.00000
SCALE2      0.000000  0.010322  0.000000        0.00000
SCALE3      0.000000  0.000000  0.012377        0.00000
      
PROCHECK
Go to PROCHECK summary
 References