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PDBsum entry 2cbu

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Top Page protein ligands metals Protein-protein interface(s) links
Hydrolase PDB id
2cbu
Jmol
Contents
Protein chains
440 a.a.
Ligands
CTS ×2
ACT ×2
Metals
_CA
Waters ×824
HEADER    HYDROLASE                               09-JAN-06   2CBU
TITLE     BETA-GLUCOSIDASE FROM THERMOTOGA MARITIMA IN COMPLEX WITH
TITLE    2 CASTANOSPERMINE
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: BETA-GLUCOSIDASE A;
COMPND   3 CHAIN: A, B;
COMPND   4 SYNONYM: GENTIOBIASE, CELLOBIASE, BETA-D-GLUCOSIDE
COMPND   5  GLUCOHYDROLASE;
COMPND   6 EC: 3.2.1.21;
COMPND   7 ENGINEERED: YES
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: THERMOTOGA MARITIMA;
SOURCE   3 ORGANISM_TAXID: 2336;
SOURCE   4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE   5 EXPRESSION_SYSTEM_TAXID: 511693;
SOURCE   6 EXPRESSION_SYSTEM_STRAIN: BL21
KEYWDS    GLYCOSIDE HYDROLASE, INHIBITOR, TRANSITION STATE MIMIC,
KEYWDS   2 FAMILY 1, CARBOHYDRATE METABOLISM, CELLULOSE DEGRADATION,
KEYWDS   3 GLYCOSIDASE, HYDROLASE, POLYSACCHARIDE DEGRADATION
EXPDTA    X-RAY DIFFRACTION
AUTHOR    T.M.GLOSTER,G.J.DAVIES,R.MADSEN
REVDAT   5   24-FEB-09 2CBU    1       VERSN
REVDAT   4   06-MAR-07 2CBU    1       REMARK
REVDAT   3   20-FEB-07 2CBU    1       REMARK MASTER
REVDAT   2   20-DEC-06 2CBU    1       JRNL
REVDAT   1   03-FEB-06 2CBU    0
JRNL        AUTH   T.M.GLOSTER,R.MADSEN,G.J.DAVIES
JRNL        TITL   DISSECTION OF CONFORMATIONALLY RESTRICTED
JRNL        TITL 2 INHIBITORS BINDING TO A BETA-GLUCOSIDASE.
JRNL        REF    CHEMBIOCHEM                   V.   7   738 2006
JRNL        REFN                   ISSN 1439-4227
JRNL        PMID   16628756
JRNL        DOI    10.1002/CBIC.200600005
REMARK   1
REMARK   1 REFERENCE 1
REMARK   1  AUTH   T.M.GLOSTER,P.MELONCELLI,R.V.STICK,D.ZECHEL,
REMARK   1  AUTH 2 A.VASELLA,G.J.DAVIES
REMARK   1  TITL   GLYCOSIDASE INHIBITION: AN ASSESSMENT OF THE
REMARK   1  TITL 2 BINDING OF 18 PUTATIVE TRANSITION-STATE MIMICS.
REMARK   1  REF    J.AM.CHEM.SOC.                V. 129  2345 2007
REMARK   1  REFN                   ISSN 0002-7863
REMARK   1  PMID   17279749
REMARK   1  DOI    10.1021/JA066961G
REMARK   2
REMARK   2 RESOLUTION.    1.85 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) : 1.85
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 72.55
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.8
REMARK   3   NUMBER OF REFLECTIONS             : 82290
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) : 0.186
REMARK   3   R VALUE            (WORKING SET) : 0.183
REMARK   3   FREE R VALUE                     : 0.237
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100
REMARK   3   FREE R VALUE TEST SET COUNT      : 4397
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) : 1.85
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.90
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 5943
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2230
REMARK   3   BIN FREE R VALUE SET COUNT          : 319
REMARK   3   BIN FREE R VALUE                    : 0.2740
REMARK   3
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK   3   PROTEIN ATOMS            : 7366
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 35
REMARK   3   SOLVENT ATOMS            : 824
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : NULL
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 28.43
REMARK   3   OVERALL ANISOTROPIC B VALUE.
REMARK   3    B11 (A**2) : -0.33000
REMARK   3    B22 (A**2) : -0.02000
REMARK   3    B33 (A**2) : 0.36000
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): 0.141
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.141
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.094
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 3.020
REMARK   3
REMARK   3 CORRELATION COEFFICIENTS.
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.962
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.937
REMARK   3
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  7651 ; 0.014 ; 0.022
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 10439 ; 1.421 ; 1.933
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   937 ; 6.425 ; 5.000
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   404 ;35.530 ;23.663
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  1222 ;14.345 ;15.000
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    50 ;20.210 ;15.000
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  1069 ; 0.102 ; 0.200
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  6060 ; 0.007 ; 0.020
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  3870 ; 0.204 ; 0.200
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  5192 ; 0.313 ; 0.200
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   634 ; 0.146 ; 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):    83 ; 0.197 ; 0.200
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    46 ; 0.158 ; 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):  4603 ; 0.822 ; 1.500
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  7227 ; 1.274 ; 2.000
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  3609 ; 1.964 ; 3.000
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  3183 ; 2.898 ; 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 : 1
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE
REMARK   3           1     A      3       A     444      5
REMARK   3           1     B      3       B     444      5
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT
REMARK   3   MEDIUM POSITIONAL  1    A    (A):   1719 ;  0.15 ;  0.50
REMARK   3   LOOSE POSITIONAL   1    A    (A):   1699 ;  0.34 ;  5.00
REMARK   3   MEDIUM THERMAL     1    A (A**2):   1719 ;  3.52 ;  2.00
REMARK   3   LOOSE THERMAL      1    A (A**2):   1699 ;  4.12 ; 10.00
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.
REMARK   4
REMARK   4 2CBU COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 18-JAN-06.
REMARK 100 THE PDBE ID CODE IS EBI-24870.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 17-APR-04
REMARK 200  TEMPERATURE           (KELVIN) : 100.0
REMARK 200  PH                             : 7.00
REMARK 200  NUMBER OF CRYSTALS USED        : 1
REMARK 200
REMARK 200  SYNCHROTRON              (Y/N) : Y
REMARK 200  RADIATION SOURCE               : ESRF
REMARK 200  BEAMLINE                       : ID14-1
REMARK 200  X-RAY GENERATOR MODEL          : NULL
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.934
REMARK 200  MONOCHROMATOR                  : DIAMOND (111), GE(220)
REMARK 200  OPTICS                         : SAGITALLY FOCUSING GE(220)
REMARK 200                                   AND A MULTILAYER
REMARK 200
REMARK 200  DETECTOR TYPE                  : CCD
REMARK 200  DETECTOR MANUFACTURER          : ADSC
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 86774
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.850
REMARK 200  RESOLUTION RANGE LOW       (A) : 40.000
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.9
REMARK 200  DATA REDUNDANCY                : 5.600
REMARK 200  R MERGE                    (I) : 0.07000
REMARK 200  R SYM                      (I) : NULL
REMARK 200   FOR THE DATA SET  : 21.7200
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.85
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.92
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0
REMARK 200  DATA REDUNDANCY IN SHELL       : 5.60
REMARK 200  R MERGE FOR SHELL          (I) : 0.43000
REMARK 200  R SYM FOR SHELL            (I) : NULL
REMARK 200   FOR SHELL         : 3.970
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: PDB ENTRY 1OD0
REMARK 200
REMARK 200 REMARK: STRUCTURE ISOMORPHOUS WITH STARTING MODEL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 47
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.3
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 10 MG/ML PROTEIN, 15% PEG 4K,
REMARK 280  0.1 M IMIDAZOLE, 0.2 M CALCIUM ACETATE, 25% ETHYLENE GLYCOL
REMARK 280  AS CRYOPROTECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290      SYMOP   SYMMETRY
REMARK 290     NNNMMM   OPERATOR
REMARK 290       1555   X,Y,Z
REMARK 290       2555   -X+1/2,-Y,Z+1/2
REMARK 290       3555   -X,Y+1/2,-Z+1/2
REMARK 290       4555   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       47.03800
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       56.64000
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       47.26050
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       56.64000
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       47.03800
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       47.26050
REMARK 290   SMTRY3   4  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 GENERATING THE BIOMOLECULE
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE:  1
REMARK 350 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 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     MET A   -21
REMARK 465     GLY A   -20
REMARK 465     SER A   -19
REMARK 465     SER A   -18
REMARK 465     HIS A   -17
REMARK 465     HIS A   -16
REMARK 465     HIS A   -15
REMARK 465     HIS A   -14
REMARK 465     HIS A   -13
REMARK 465     HIS A   -12
REMARK 465     SER A   -11
REMARK 465     SER A   -10
REMARK 465     GLY A    -9
REMARK 465     LEU A    -8
REMARK 465     VAL A    -7
REMARK 465     PRO A    -6
REMARK 465     ARG A    -5
REMARK 465     GLY A    -4
REMARK 465     SER A    -3
REMARK 465     HIS A    -2
REMARK 465     MET A    -1
REMARK 465     ALA A     0
REMARK 465     SER A     1
REMARK 465     ASN A     2
REMARK 465     GLU A   233
REMARK 465     GLU A   234
REMARK 465     ALA A   306
REMARK 465     PRO A   307
REMARK 465     MET B   -21
REMARK 465     GLY B   -20
REMARK 465     SER B   -19
REMARK 465     SER B   -18
REMARK 465     HIS B   -17
REMARK 465     HIS B   -16
REMARK 465     HIS B   -15
REMARK 465     HIS B   -14
REMARK 465     HIS B   -13
REMARK 465     HIS B   -12
REMARK 465     SER B   -11
REMARK 465     SER B   -10
REMARK 465     GLY B    -9
REMARK 465     LEU B    -8
REMARK 465     VAL B    -7
REMARK 465     PRO B    -6
REMARK 465     ARG B    -5
REMARK 465     GLY B    -4
REMARK 465     SER B    -3
REMARK 465     HIS B    -2
REMARK 465     MET B    -1
REMARK 465     ALA B     0
REMARK 465     SER B     1
REMARK 465     PRO B   307
REMARK 465     ALA B   308
REMARK 465     GLU B   445
REMARK 465     ASP B   446
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   8    CG   CD   OE1  OE2
REMARK 470     LYS A 232    CD   CE   NZ
REMARK 470     LYS A 301    CB   CG   CD   CE   NZ
REMARK 470     LYS A 309    CB   CG   CD   CE   NZ
REMARK 470     LYS A 440    CD   CE   NZ
REMARK 470     GLU B   8    CD   OE1  OE2
REMARK 470     LYS B  70    CG   CD   CE   NZ
REMARK 470     LYS B  74    CD   CE   NZ
REMARK 470     ARG B  92    CD   NE   CZ   NH1  NH2
REMARK 470     LYS B 213    CG   CD   CE   NZ
REMARK 470     LYS B 216    CG   CD   CE   NZ
REMARK 470     GLU B 231    CB   CG   CD   OE1  OE2
REMARK 470     LYS B 232    CG   CD   CE   NZ
REMARK 470     ASP B 316    CB   CG   OD1  OD2
REMARK 470     LYS B 425    CD   CE   NZ
REMARK 470     LYS B 440    CG   CD   CE   NZ
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 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  54     -128.36     54.91
REMARK 500    TRP A 122      -10.94     96.00
REMARK 500    SER A 230      177.98    172.31
REMARK 500    TYR A 295      -37.44   -136.63
REMARK 500    TRP A 406     -131.37     53.08
REMARK 500    VAL B  53      -53.67   -122.07
REMARK 500    ALA B  54     -122.09     54.96
REMARK 500    TRP B 122       -9.30     96.29
REMARK 500    TYR B 295      -45.04   -138.75
REMARK 500    ASP B 316     -103.41    -58.13
REMARK 500    LEU B 317      140.83     45.33
REMARK 500    TRP B 406     -128.81     52.87
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 SER A  230     GLU A  231                  147.56
REMARK 500 GLU A  231     LYS A  232                  -67.82
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620  (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620   SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              CA B1446  CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP B 278   O
REMARK 620 2 SER B 281   OG   89.4
REMARK 620 3 GLU B 282   OE1 126.7  81.5
REMARK 620 4 GLU B 282   OE2  80.5  56.3  51.1
REMARK 620 5 HOH A2185   O   151.8 108.7  78.5 127.5
REMARK 620 6 HOH A2186   O    76.8 156.2  91.3 101.8  91.8
REMARK 620 7 HOH B2267   O    70.5  51.6 131.6 100.6 103.5 136.2
REMARK 620 8 HOH B2268   O    83.1 131.7 138.9 161.7  68.7  66.5  81.2
REMARK 620 N                    1     2     3     4     5     6     7
REMARK 700
REMARK 700 SHEET
REMARK 700 DETERMINATION METHOD: DSSP
REMARK 700 THE SHEETS PRESENTED AS "AB" 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 700
REMARK 700 THE SHEETS PRESENTED AS "BA" 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 ACT A1448
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT A1449
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  CA B1446
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CTS A1447
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CTS B1445
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1OD0   RELATED DB: PDB
REMARK 900  FAMILY 1 B-GLUCOSIDASE FROM THERMOTOGA
REMARK 900  MARITIMA
REMARK 900 RELATED ID: 1OIF   RELATED DB: PDB
REMARK 900  FAMILY 1 B-GLUCOSIDASE FROM THERMOTOGA
REMARK 900  MARITIMA
REMARK 900 RELATED ID: 1OIM   RELATED DB: PDB
REMARK 900  FAMILY 1 B-GLUCOSIDASE FROM THERMOTOGA
REMARK 900  MARITIMA
REMARK 900 RELATED ID: 1OIN   RELATED DB: PDB
REMARK 900  FAMILY 1 B-GLUCOSIDASE FROM THERMOTOGA
REMARK 900  MARITIMA
REMARK 900 RELATED ID: 1UZ1   RELATED DB: PDB
REMARK 900  FAMILY 1 B-GLUCOSIDASE FROM THERMOTOGA
REMARK 900  MARITIMA IN COMPLEX WITH GLUCO-ISOFAGOMINE
REMARK 900  LACTAM
REMARK 900 RELATED ID: 1W3J   RELATED DB: PDB
REMARK 900  FAMILY 1 B-GLUCOSIDASE FROM THERMOTOGA
REMARK 900  MARITIMA IN COMPLEX WITH TETRAHYDROOXAZINE
REMARK 900 RELATED ID: 2CBV   RELATED DB: PDB
REMARK 900  BETA-GLUCOSIDASE FROM THERMOTOGA MARITIMA IN
REMARK 900  COMPLEX WITH CALYSTEGINE B2
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 SEQUENCE CRYSTALLIZED CONTAINS A HIS TAG FROM THE
REMARK 999 EXPRESSION VECTOR. THE CO-ORDINATES ARE NUMBERED
REMARK 999 ACCORDING TO THE UNIPROT ENTRY AND IGNORE THE HIS TAG.
DBREF  2CBU A  -21     1  PDB    2CBU     2CBU           -21      1
DBREF  2CBU A    2   446  UNP    Q08638   BGLA_THEMA       2    446
DBREF  2CBU B  -21     1  PDB    2CBU     2CBU           -21      1
DBREF  2CBU B    2   446  UNP    Q08638   BGLA_THEMA       2    446
SEQRES   1 A  468  MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES   2 A  468  LEU VAL PRO ARG GLY SER HIS MET ALA SER ASN VAL LYS
SEQRES   3 A  468  LYS PHE PRO GLU GLY PHE LEU TRP GLY VAL ALA THR ALA
SEQRES   4 A  468  SER TYR GLN ILE GLU GLY SER PRO LEU ALA ASP GLY ALA
SEQRES   5 A  468  GLY MET SER ILE TRP HIS THR PHE SER HIS THR PRO GLY
SEQRES   6 A  468  ASN VAL LYS ASN GLY ASP THR GLY ASP VAL ALA CYS ASP
SEQRES   7 A  468  HIS TYR ASN ARG TRP LYS GLU ASP ILE GLU ILE ILE GLU
SEQRES   8 A  468  LYS LEU GLY VAL LYS ALA TYR ARG PHE SER ILE SER TRP
SEQRES   9 A  468  PRO ARG ILE LEU PRO GLU GLY THR GLY ARG VAL ASN GLN
SEQRES  10 A  468  LYS GLY LEU ASP PHE TYR ASN ARG ILE ILE ASP THR LEU
SEQRES  11 A  468  LEU GLU LYS GLY ILE THR PRO PHE VAL THR ILE TYR HIS
SEQRES  12 A  468  TRP ASP LEU PRO PHE ALA LEU GLN LEU LYS GLY GLY TRP
SEQRES  13 A  468  ALA ASN ARG GLU ILE ALA ASP TRP PHE ALA GLU TYR SER
SEQRES  14 A  468  ARG VAL LEU PHE GLU ASN PHE GLY ASP ARG VAL LYS ASN
SEQRES  15 A  468  TRP ILE THR LEU ASN GLU PRO TRP VAL VAL ALA ILE VAL
SEQRES  16 A  468  GLY HIS LEU TYR GLY VAL HIS ALA PRO GLY MET ARG ASP
SEQRES  17 A  468  ILE TYR VAL ALA PHE ARG ALA VAL HIS ASN LEU LEU ARG
SEQRES  18 A  468  ALA HIS ALA ARG ALA VAL LYS VAL PHE ARG GLU THR VAL
SEQRES  19 A  468  LYS ASP GLY LYS ILE GLY ILE VAL PHE ASN ASN GLY TYR
SEQRES  20 A  468  PHE GLU PRO ALA SER GLU LYS GLU GLU ASP ILE ARG ALA
SEQRES  21 A  468  VAL ARG PHE MET HIS GLN PHE ASN ASN TYR PRO LEU PHE
SEQRES  22 A  468  LEU ASN PRO ILE TYR ARG GLY ASP TYR PRO GLU LEU VAL
SEQRES  23 A  468  LEU GLU PHE ALA ARG GLU TYR LEU PRO GLU ASN TYR LYS
SEQRES  24 A  468  ASP ASP MET SER GLU ILE GLN GLU LYS ILE ASP PHE VAL
SEQRES  25 A  468  GLY LEU ASN TYR TYR SER GLY HIS LEU VAL LYS PHE ASP
SEQRES  26 A  468  PRO ASP ALA PRO ALA LYS VAL SER PHE VAL GLU ARG ASP
SEQRES  27 A  468  LEU PRO LYS THR ALA MET GLY TRP GLU ILE VAL PRO GLU
SEQRES  28 A  468  GLY ILE TYR TRP ILE LEU LYS LYS VAL LYS GLU GLU TYR
SEQRES  29 A  468  ASN PRO PRO GLU VAL TYR ILE THR GLU ASN GLY ALA ALA
SEQRES  30 A  468  PHE ASP ASP VAL VAL SER GLU ASP GLY ARG VAL HIS ASP
SEQRES  31 A  468  GLN ASN ARG ILE ASP TYR LEU LYS ALA HIS ILE GLY GLN
SEQRES  32 A  468  ALA TRP LYS ALA ILE GLN GLU GLY VAL PRO LEU LYS GLY
SEQRES  33 A  468  TYR PHE VAL TRP SER LEU LEU ASP ASN PHE GLU TRP ALA
SEQRES  34 A  468  GLU GLY TYR SER LYS ARG PHE GLY ILE VAL TYR VAL ASP
SEQRES  35 A  468  TYR SER THR GLN LYS ARG ILE VAL LYS ASP SER GLY TYR
SEQRES  36 A  468  TRP TYR SER ASN VAL VAL LYS ASN ASN GLY LEU GLU ASP
SEQRES   1 B  468  MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES   2 B  468  LEU VAL PRO ARG GLY SER HIS MET ALA SER ASN VAL LYS
SEQRES   3 B  468  LYS PHE PRO GLU GLY PHE LEU TRP GLY VAL ALA THR ALA
SEQRES   4 B  468  SER TYR GLN ILE GLU GLY SER PRO LEU ALA ASP GLY ALA
SEQRES   5 B  468  GLY MET SER ILE TRP HIS THR PHE SER HIS THR PRO GLY
SEQRES   6 B  468  ASN VAL LYS ASN GLY ASP THR GLY ASP VAL ALA CYS ASP
SEQRES   7 B  468  HIS TYR ASN ARG TRP LYS GLU ASP ILE GLU ILE ILE GLU
SEQRES   8 B  468  LYS LEU GLY VAL LYS ALA TYR ARG PHE SER ILE SER TRP
SEQRES   9 B  468  PRO ARG ILE LEU PRO GLU GLY THR GLY ARG VAL ASN GLN
SEQRES  10 B  468  LYS GLY LEU ASP PHE TYR ASN ARG ILE ILE ASP THR LEU
SEQRES  11 B  468  LEU GLU LYS GLY ILE THR PRO PHE VAL THR ILE TYR HIS
SEQRES  12 B  468  TRP ASP LEU PRO PHE ALA LEU GLN LEU LYS GLY GLY TRP
SEQRES  13 B  468  ALA ASN ARG GLU ILE ALA ASP TRP PHE ALA GLU TYR SER
SEQRES  14 B  468  ARG VAL LEU PHE GLU ASN PHE GLY ASP ARG VAL LYS ASN
SEQRES  15 B  468  TRP ILE THR LEU ASN GLU PRO TRP VAL VAL ALA ILE VAL
SEQRES  16 B  468  GLY HIS LEU TYR GLY VAL HIS ALA PRO GLY MET ARG ASP
SEQRES  17 B  468  ILE TYR VAL ALA PHE ARG ALA VAL HIS ASN LEU LEU ARG
SEQRES  18 B  468  ALA HIS ALA ARG ALA VAL LYS VAL PHE ARG GLU THR VAL
SEQRES  19 B  468  LYS ASP GLY LYS ILE GLY ILE VAL PHE ASN ASN GLY TYR
SEQRES  20 B  468  PHE GLU PRO ALA SER GLU LYS GLU GLU ASP ILE ARG ALA
SEQRES  21 B  468  VAL ARG PHE MET HIS GLN PHE ASN ASN TYR PRO LEU PHE
SEQRES  22 B  468  LEU ASN PRO ILE TYR ARG GLY ASP TYR PRO GLU LEU VAL
SEQRES  23 B  468  LEU GLU PHE ALA ARG GLU TYR LEU PRO GLU ASN TYR LYS
SEQRES  24 B  468  ASP ASP MET SER GLU ILE GLN GLU LYS ILE ASP PHE VAL
SEQRES  25 B  468  GLY LEU ASN TYR TYR SER GLY HIS LEU VAL LYS PHE ASP
SEQRES  26 B  468  PRO ASP ALA PRO ALA LYS VAL SER PHE VAL GLU ARG ASP
SEQRES  27 B  468  LEU PRO LYS THR ALA MET GLY TRP GLU ILE VAL PRO GLU
SEQRES  28 B  468  GLY ILE TYR TRP ILE LEU LYS LYS VAL LYS GLU GLU TYR
SEQRES  29 B  468  ASN PRO PRO GLU VAL TYR ILE THR GLU ASN GLY ALA ALA
SEQRES  30 B  468  PHE ASP ASP VAL VAL SER GLU ASP GLY ARG VAL HIS ASP
SEQRES  31 B  468  GLN ASN ARG ILE ASP TYR LEU LYS ALA HIS ILE GLY GLN
SEQRES  32 B  468  ALA TRP LYS ALA ILE GLN GLU GLY VAL PRO LEU LYS GLY
SEQRES  33 B  468  TYR PHE VAL TRP SER LEU LEU ASP ASN PHE GLU TRP ALA
SEQRES  34 B  468  GLU GLY TYR SER LYS ARG PHE GLY ILE VAL TYR VAL ASP
SEQRES  35 B  468  TYR SER THR GLN LYS ARG ILE VAL LYS ASP SER GLY TYR
SEQRES  36 B  468  TRP TYR SER ASN VAL VAL LYS ASN ASN GLY LEU GLU ASP
HET    ACT  A1448       4
HET    ACT  A1449       4
HET     CA  B1446       1
HET    CTS  A1447      13
HET    CTS  B1445      13
HETNAM     ACT ACETATE ION
HETNAM      CA CALCIUM ION
HETNAM     CTS CASTANOSPERMINE
HETSYN     CTS (1S,6S,7R,8R,8AR)-1,6,7,8-
HETSYN   2 CTS  TETRAHYDROXYINDOLIZIDINE
FORMUL   3  ACT    2(C2 H3 O2 1-)
FORMUL   5   CA    CA 2+
FORMUL   6  CTS    2(C8 H15 N O4)
FORMUL   8  HOH   *824(H2 O1)
HELIX    1   1 ALA A   17  GLU A   22  1                                   6
HELIX    2   2 LEU A   26  ALA A   30  5                                   5
HELIX    3   3 SER A   33  HIS A   40  1                                   8
HELIX    4   4 VAL A   45  ASP A   49  5                                   5
HELIX    5   5 ASP A   56  LEU A   71  1                                  16
HELIX    6   6 SER A   81  LEU A   86  1                                   6
HELIX    7   7 ASN A   94  LYS A  111  1                                  18
HELIX    8   8 PRO A  125  LEU A  130  1                                   6
HELIX    9   9 LYS A  131  ARG A  137  5                                   7
HELIX   10  10 GLU A  138  GLY A  155  1                                  18
HELIX   11  11 GLU A  166  LEU A  176  1                                  11
HELIX   12  12 ASP A  186  VAL A  212  1                                  27
HELIX   13  13 ASP A  235  ASN A  247  1                                  13
HELIX   14  14 TYR A  248  GLY A  258  1                                  11
HELIX   15  15 PRO A  261  ARG A  269  1                                   9
HELIX   16  16 GLU A  270  LEU A  272  5                                   3
HELIX   17  17 ASN A  275  ASP A  278  5                                   4
HELIX   18  18 ASP A  279  GLN A  284  1                                   6
HELIX   19  19 PRO A  328  ASN A  343  1                                  16
HELIX   20  20 ASP A  368  GLU A  388  1                                  21
HELIX   21  21 GLU A  405  LYS A  412  5                                   8
HELIX   22  22 LYS A  429  ASN A  441  1                                  13
HELIX   23  23 ALA B   17  GLU B   22  1                                   6
HELIX   24  24 LEU B   26  ALA B   30  5                                   5
HELIX   25  25 SER B   33  HIS B   40  1                                   8
HELIX   26  26 VAL B   45  ASP B   49  5                                   5
HELIX   27  27 ASP B   56  GLY B   72  1                                  17
HELIX   28  28 SER B   81  LEU B   86  1                                   6
HELIX   29  29 ASN B   94  LYS B  111  1                                  18
HELIX   30  30 PRO B  125  LEU B  130  1                                   6
HELIX   31  31 LYS B  131  ARG B  137  5                                   7
HELIX   32  32 GLU B  138  GLY B  155  1                                  18
HELIX   33  33 GLU B  166  LEU B  176  1                                  11
HELIX   34  34 ASP B  186  VAL B  212  1                                  27
HELIX   35  35 LYS B  232  ASN B  247  1                                  16
HELIX   36  36 TYR B  248  GLY B  258  1                                  11
HELIX   37  37 PRO B  261  ARG B  269  1                                   9
HELIX   38  38 GLU B  270  LEU B  272  5                                   3
HELIX   39  39 ASN B  275  ASP B  278  5                                   4
HELIX   40  40 ASP B  279  GLN B  284  1                                   6
HELIX   41  41 PRO B  328  TYR B  342  1                                  15
HELIX   42  42 ASP B  368  GLU B  388  1                                  21
HELIX   43  43 GLU B  405  LYS B  412  5                                   8
HELIX   44  44 LYS B  429  ASN B  442  1                                  14
SHEET    1  AA 2 LYS A   4  LYS A   5  0
SHEET    2  AA 2 GLY A 443  LEU A 444 -1  O  LEU A 444   N  LYS A   4
SHEET    1  AB 9 LEU A  11  ALA A  15  0
SHEET    2  AB 9 LEU A 392  TRP A 398  1  O  LYS A 393   N  LEU A  11
SHEET    3  AB 9 VAL A 347  ASN A 352  1  O  VAL A 347   N  LYS A 393
SHEET    4  AB 9 PHE A 289  ASN A 293  1  O  VAL A 290   N  TYR A 348
SHEET    5  AB 9 LYS A 216  PHE A 221  1  O  ILE A 219   N  GLY A 291
SHEET    6  AB 9 ASN A 160  ASN A 165  1  O  TRP A 161   N  GLY A 218
SHEET    7  AB 9 THR A 114  TYR A 120  1  O  VAL A 117   N  ILE A 162
SHEET    8  AB 9 ALA A  75  SER A  79  1  O  TYR A  76   N  PHE A 116
SHEET    9  AB 9 LEU A  11  ALA A  15  1  O  TRP A  12   N  ALA A  75
SHEET    1  AC 3 TYR A 225  PRO A 228  0
SHEET    2  AC 3 GLY A 297  PHE A 302  1  O  HIS A 298   N  GLU A 227
SHEET    3  AC 3 VAL A 310  VAL A 313 -1  O  SER A 311   N  LYS A 301
SHEET    1  AD 2 VAL A 417  VAL A 419  0
SHEET    2  AD 2 ARG A 426  VAL A 428 -1  O  ILE A 427   N  TYR A 418
SHEET    1  BA 9 LEU B  11  ALA B  15  0
SHEET    2  BA 9 LEU B 392  TRP B 398  1  O  LYS B 393   N  LEU B  11
SHEET    3  BA 9 VAL B 347  ASN B 352  1  O  VAL B 347   N  LYS B 393
SHEET    4  BA 9 PHE B 289  ASN B 293  1  O  VAL B 290   N  TYR B 348
SHEET    5  BA 9 LYS B 216  PHE B 221  1  O  ILE B 219   N  GLY B 291
SHEET    6  BA 9 ASN B 160  ASN B 165  1  O  TRP B 161   N  GLY B 218
SHEET    7  BA 9 THR B 114  TYR B 120  1  O  VAL B 117   N  ILE B 162
SHEET    8  BA 9 ALA B  75  SER B  79  1  O  TYR B  76   N  PHE B 116
SHEET    9  BA 9 LEU B  11  ALA B  15  1  O  TRP B  12   N  ALA B  75
SHEET    1  BB 3 TYR B 225  PRO B 228  0
SHEET    2  BB 3 GLY B 297  PHE B 302  1  O  HIS B 298   N  GLU B 227
SHEET    3  BB 3 VAL B 310  VAL B 313 -1  O  SER B 311   N  LYS B 301
SHEET    1  BC 2 VAL B 417  ASP B 420  0
SHEET    2  BC 2 LYS B 425  VAL B 428 -1  O  LYS B 425   N  ASP B 420
LINK        CA    CA B1446                 O   ASP B 278     1555   1555  2.38
LINK        CA    CA B1446                 OG  SER B 281     1555   1555  3.37
LINK        CA    CA B1446                 OE1 GLU B 282     1555   1555  2.47
LINK        CA    CA B1446                 OE2 GLU B 282     1555   1555  2.60
LINK        CA    CA B1446                 O   HOH A2185     1555   1545  2.46
LINK        CA    CA B1446                 O   HOH A2186     1555   1545  2.73
LINK        CA    CA B1446                 O   HOH B2267     1555   1555  1.93
LINK        CA    CA B1446                 O   HOH B2268     1555   1555  2.49
CISPEP   1 ALA A  181    PRO A  182          0         2.29
CISPEP   2 TRP A  398    SER A  399          0         3.78
CISPEP   3 ALA B  181    PRO B  182          0         2.60
CISPEP   4 TRP B  398    SER B  399          0         2.17
SITE     1 AC1  4 VAL A  53  ALA A  54  TYR A 421  HOH A2036
SITE     1 AC2  3 GLY A 364  VAL A 428  TYR A 433
SITE     1 AC3  7 HOH A2185  HOH A2186  ASP B 278  SER B 281
SITE     2 AC3  7 GLU B 282  HOH B2267  HOH B2268
SITE     1 AC4 11 GLN A  20  HIS A 121  ASN A 165  GLU A 166
SITE     2 AC4 11 TYR A 295  TRP A 324  GLU A 351  TRP A 398
SITE     3 AC4 11 GLU A 405  TRP A 406  HOH A2470
SITE     1 AC5 10 GLN B  20  HIS B 121  ASN B 165  GLU B 166
SITE     2 AC5 10 TYR B 295  TRP B 324  GLU B 351  TRP B 398
SITE     3 AC5 10 GLU B 405  TRP B 406
CRYST1   94.076   94.521  113.280  90.00  90.00  90.00 P 21 21 21    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      0.010630  0.000000  0.000000        0.00000
SCALE2      0.000000  0.010580  0.000000        0.00000
SCALE3      0.000000  0.000000  0.008828        0.00000
MTRIX1   1 -0.014000 -0.991000 -0.134000      -31.53593    1
MTRIX2   1  0.990000  0.005000 -0.137000       29.03707    1
MTRIX3   1  0.137000 -0.135000  0.981000       13.31038    1
      
PROCHECK
Go to PROCHECK summary
 References