HEADER HYDROLASE 29-NOV-05 2F6D
TITLE STRUCTURE OF THE COMPLEX OF A GLUCOAMYLASE FROM SACCHAROMYCOPSIS
TITLE 2 FIBULIGERA WITH ACARBOSE
CAVEAT 2F6D GLC B 1 HAS WRONG CHIRALITY AT ATOM C1 GLC C 1 HAS WRONG
CAVEAT 2 2F6D CHIRALITY AT ATOM C1
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: GLUCOAMYLASE GLU1;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: GLUCAN 1,4-ALPHA-GLUCOSIDASE, 1,4-ALPHA-D-GLUCAN
COMPND 5 GLUCOHYDROLASE;
COMPND 6 EC: 3.2.1.3;
COMPND 7 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: SACCHAROMYCOPSIS FIBULIGERA;
SOURCE 3 ORGANISM_TAXID: 4944;
SOURCE 4 STRAIN: HUT 7212;
SOURCE 5 GENE: GLU1;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET3D
KEYWDS (ALPHA-ALPHA)6 BARREL, PROTEIN-ACARBOSE COMPLEX, SUGAR TONGS,
KEYWDS 2 HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR J.SEVCIK,E.HOSTINOVA,A.SOLOVICOVA,J.GASPERIK,Z.DAUTER,K.S.WILSON
REVDAT 5 23-AUG-23 2F6D 1 HETSYN
REVDAT 4 29-JUL-20 2F6D 1 CAVEAT COMPND REMARK HET
REVDAT 4 2 1 HETNAM HETSYN FORMUL LINK
REVDAT 4 3 1 SITE ATOM
REVDAT 3 13-JUL-11 2F6D 1 VERSN
REVDAT 2 24-FEB-09 2F6D 1 VERSN
REVDAT 1 23-MAY-06 2F6D 0
JRNL AUTH J.SEVCIK,E.HOSTINOVA,A.SOLOVICOVA,J.GASPERIK,Z.DAUTER,
JRNL AUTH 2 K.S.WILSON
JRNL TITL STRUCTURE OF THE COMPLEX OF A YEAST GLUCOAMYLASE WITH
JRNL TITL 2 ACARBOSE REVEALS THE PRESENCE OF A RAW STARCH BINDING SITE
JRNL TITL 3 ON THE CATALYTIC DOMAIN.
JRNL REF FEBS J. V. 273 2161 2006
JRNL REFN ISSN 1742-464X
JRNL PMID 16649993
JRNL DOI 10.1111/J.1742-4658.2006.05230.X
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH J.SEVCIK,A.SOLOVICOVA,E.HOSTINOVA,J.GASPERIK,K.S.WILSON,
REMARK 1 AUTH 2 Z.DAUTER
REMARK 1 TITL STRUCTURE OF GLUCOAMYLASE FROM SACCHAROMYCOPSIS FIBULIGERA
REMARK 1 TITL 2 AT 1.7 A RESOLUTION.
REMARK 1 REF ACTA CRYSTALLOGR.,SECT.D V. D54 854 1998
REMARK 1 REFN ISSN 0907-4449
REMARK 2
REMARK 2 RESOLUTION. 1.60 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.1.24
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.60
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 10.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 2.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 94.0
REMARK 3 NUMBER OF REFLECTIONS : 56255
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) : 0.120
REMARK 3 R VALUE (WORKING SET) : 0.118
REMARK 3 FREE R VALUE : 0.160
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 3010
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) : 1.60
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.64
REMARK 3 REFLECTION IN BIN (WORKING SET) : 3705
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : 0.1460
REMARK 3 BIN FREE R VALUE SET COUNT : 199
REMARK 3 BIN FREE R VALUE : 0.1930
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 3870
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 95
REMARK 3 SOLVENT ATOMS : 810
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 15.60
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 12.66
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.21000
REMARK 3 B22 (A**2) : 0.48000
REMARK 3 B33 (A**2) : -0.27000
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): 0.117
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.077
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.046
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 1.314
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.979
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.965
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 4058 ; 0.011 ; 0.021
REMARK 3 BOND LENGTHS OTHERS (A): 3365 ; 0.002 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 5545 ; 1.609 ; 1.965
REMARK 3 BOND ANGLES OTHERS (DEGREES): 7887 ; 1.047 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 491 ; 5.733 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): NULL ; NULL ; NULL
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 624 ; 0.159 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 4611 ; 0.015 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 824 ; 0.015 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 984 ; 0.217 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): 4155 ; 0.248 ; 0.200
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): 2129 ; 0.085 ; 0.200
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 611 ; 0.193 ; 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): 29 ; 0.210 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): 76 ; 0.274 ; 0.200
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 99 ; 0.218 ; 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): 2443 ; 0.938 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 3928 ; 1.535 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1615 ; 2.237 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1617 ; 3.318 ; 4.500
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): 4058 ; 1.184 ; 2.000
REMARK 3 SPHERICITY; FREE ATOMS (A**2): 812 ; 2.593 ; 2.000
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): 3963 ; 1.820 ; 2.000
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 : BABINET MODEL WITH 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 2F6D COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 16-DEC-05.
REMARK 100 THE DEPOSITION ID IS D_1000035506.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 09-JUL-02
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 5.4
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : EMBL/DESY, HAMBURG
REMARK 200 BEAMLINE : X11
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9096
REMARK 200 MONOCHROMATOR : SI 111 CHANNEL
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : AREA DETECTOR
REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 59266
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.600
REMARK 200 RESOLUTION RANGE LOW (A) : 10.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 1.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 94.5
REMARK 200 DATA REDUNDANCY : 3.490
REMARK 200 R MERGE (I) : 0.04300
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 17.5000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.60
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.62
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.14400
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 4.200
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: PDB ENTRY 1AYX
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 42.87
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.15
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 50 MM ACETATE BUFFER, 15% PEG 8K, PH
REMARK 280 5.4, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 295K
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 28.29000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 48.75500
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 42.67500
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 48.75500
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 28.29000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 42.67500
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 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 O HOH A 1348 O HOH A 1807 1.98
REMARK 500 O HOH A 1613 O HOH A 1804 2.07
REMARK 500 O HOH A 1751 O HOH A 1799 2.16
REMARK 500 O HOH A 1146 O HOH A 1806 2.17
REMARK 500 O HOH A 1565 O HOH A 1802 2.19
REMARK 500 O4 GLC C 2 O5 AC1 C 3 2.19
REMARK 500 O4 GLC C 1 O5 GLC C 2 2.19
REMARK 500 O HOH A 1252 O HOH A 1783 2.19
REMARK 500 O4 GLC B 1 O5 GLC B 2 2.19
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 ASP A 160 CB - CG - OD2 ANGL. DEV. = 6.1 DEGREES
REMARK 500 ASP A 241 CB - CG - OD2 ANGL. DEV. = 6.3 DEGREES
REMARK 500 ASP A 268 CB - CG - OD2 ANGL. DEV. = 5.5 DEGREES
REMARK 500 ASP A 300 CB - CG - OD2 ANGL. DEV. = 6.8 DEGREES
REMARK 500 ASP A 310 CB - CG - OD2 ANGL. DEV. = 6.3 DEGREES
REMARK 500 ASP A 312 CB - CG - OD2 ANGL. DEV. = 6.5 DEGREES
REMARK 500 ASP A 329 CB - CG - OD2 ANGL. DEV. = 5.9 DEGREES
REMARK 500 ASP A 386 CB - CG - OD2 ANGL. DEV. = 5.9 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 PHE A 87 75.47 69.10
REMARK 500 ASN A 178 39.41 -91.65
REMARK 500 ILE A 189 -54.33 -123.42
REMARK 500 ASP A 202 34.77 -99.18
REMARK 500 ASP A 239 58.45 -112.82
REMARK 500 ALA A 339 -117.08 -119.40
REMARK 500 ASP A 354 38.82 -162.45
REMARK 500 SER A 357 -81.90 -160.31
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 ASP A 176 ILE A 177 -145.81
REMARK 500
REMARK 500 REMARK: NULL
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 NA A 998 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ILE A 177 O
REMARK 620 2 HOH A 999 O 86.2
REMARK 620 3 HOH A1000 O 91.5 167.5
REMARK 620 4 HOH A1350 O 169.4 88.9 91.2
REMARK 620 5 HOH A1600 O 83.1 85.4 82.2 87.1
REMARK 620 6 HOH A1613 O 100.9 103.4 89.0 89.3 170.4
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA A 997 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 310 OD1
REMARK 620 2 HOH A1620 O 97.4
REMARK 620 3 HOH A1627 O 90.9 169.3
REMARK 620 4 HOH A1646 O 90.6 95.2 91.4
REMARK 620 5 HOH A1764 O 175.5 84.7 87.5 85.2
REMARK 620 N 1 2 3 4
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1AYX RELATED DB: PDB
REMARK 900 GLUCOAMYLASE FROM SACCHAROMYCOPSIS FIBULIGERA
DBREF 2F6D A 1 492 UNP P08017 AMYG_SACFI 28 519
SEQRES 1 A 492 ALA TYR PRO SER PHE GLU ALA TYR SER ASN TYR LYS VAL
SEQRES 2 A 492 ASP ARG THR ASP LEU GLU THR PHE LEU ASP LYS GLN LYS
SEQRES 3 A 492 GLU VAL SER LEU TYR TYR LEU LEU GLN ASN ILE ALA TYR
SEQRES 4 A 492 PRO GLU GLY GLN PHE ASN ASN GLY VAL PRO GLY THR VAL
SEQRES 5 A 492 ILE ALA SER PRO SER THR SER ASN PRO ASP TYR TYR TYR
SEQRES 6 A 492 GLN TRP THR ARG ASP SER ALA ILE THR PHE LEU THR VAL
SEQRES 7 A 492 LEU SER GLU LEU GLU ASP ASN ASN PHE ASN THR THR LEU
SEQRES 8 A 492 ALA LYS ALA VAL GLU TYR TYR ILE ASN THR SER TYR ASN
SEQRES 9 A 492 LEU GLN ARG THR SER ASN PRO SER GLY SER PHE ASP ASP
SEQRES 10 A 492 GLU ASN HIS LYS GLY LEU GLY GLU PRO LYS PHE ASN THR
SEQRES 11 A 492 ASP GLY SER ALA TYR THR GLY ALA TRP GLY ARG PRO GLN
SEQRES 12 A 492 ASN ASP GLY PRO ALA LEU ARG ALA TYR ALA ILE SER ARG
SEQRES 13 A 492 TYR LEU ASN ASP VAL ASN SER LEU ASN GLU GLY LYS LEU
SEQRES 14 A 492 VAL LEU THR ASP SER GLY ASP ILE ASN PHE SER SER THR
SEQRES 15 A 492 GLU ASP ILE TYR LYS ASN ILE ILE LYS PRO ASP LEU GLU
SEQRES 16 A 492 TYR VAL ILE GLY TYR TRP ASP SER THR GLY PHE ASP LEU
SEQRES 17 A 492 TRP GLU GLU ASN GLN GLY ARG HIS PHE PHE THR SER LEU
SEQRES 18 A 492 VAL GLN GLN LYS ALA LEU ALA TYR ALA VAL ASP ILE ALA
SEQRES 19 A 492 LYS SER PHE ASP ASP GLY ASP PHE ALA ASN THR LEU SER
SEQRES 20 A 492 SER THR ALA SER THR LEU GLU SER TYR LEU SER GLY SER
SEQRES 21 A 492 ASP GLY GLY PHE VAL ASN THR ASP VAL ASN HIS ILE VAL
SEQRES 22 A 492 GLU ASN PRO ASP LEU LEU GLN GLN ASN SER ARG GLN GLY
SEQRES 23 A 492 LEU ASP SER ALA THR TYR ILE GLY PRO LEU LEU THR HIS
SEQRES 24 A 492 ASP ILE GLY GLU SER SER SER THR PRO PHE ASP VAL ASP
SEQRES 25 A 492 ASN GLU TYR VAL LEU GLN SER TYR TYR LEU LEU LEU GLU
SEQRES 26 A 492 ASP ASN LYS ASP ARG TYR SER VAL ASN SER ALA TYR SER
SEQRES 27 A 492 ALA GLY ALA ALA ILE GLY ARG TYR PRO GLU ASP VAL TYR
SEQRES 28 A 492 ASN GLY ASP GLY SER SER GLU GLY ASN PRO TRP PHE LEU
SEQRES 29 A 492 ALA THR ALA TYR ALA ALA GLN VAL PRO TYR LYS LEU ALA
SEQRES 30 A 492 TYR ASP ALA LYS SER ALA SER ASN ASP ILE THR ILE ASN
SEQRES 31 A 492 LYS ILE ASN TYR ASP PHE PHE ASN LYS TYR ILE VAL ASP
SEQRES 32 A 492 LEU SER THR ILE ASN SER ALA TYR GLN SER SER ASP SER
SEQRES 33 A 492 VAL THR ILE LYS SER GLY SER ASP GLU PHE ASN THR VAL
SEQRES 34 A 492 ALA ASP ASN LEU VAL THR PHE GLY ASP SER PHE LEU GLN
SEQRES 35 A 492 VAL ILE LEU ASP HIS ILE ASN ASP ASP GLY SER LEU ASN
SEQRES 36 A 492 GLU GLN LEU ASN ARG TYR THR GLY TYR SER THR GLY ALA
SEQRES 37 A 492 TYR SER LEU THR TRP SER SER GLY ALA LEU LEU GLU ALA
SEQRES 38 A 492 ILE ARG LEU ARG ASN LYS VAL LYS ALA LEU ALA
HET GLC B 1 12
HET GLC B 2 11
HET AC1 B 3 21
HET GLC C 1 12
HET GLC C 2 11
HET AC1 C 3 21
HET PO4 A 900 5
HET NA A 997 1
HET NA A 998 1
HETNAM GLC ALPHA-D-GLUCOPYRANOSE
HETNAM AC1 4,6-DIDEOXY-4-{[(1S,4R,5S,6S)-4,5,6-TRIHYDROXY-3-
HETNAM 2 AC1 (HYDROXYMETHYL)CYCLOHEX-2-EN-1-YL]AMINO}-ALPHA-D-
HETNAM 3 AC1 GLUCOPYRANOSE
HETNAM PO4 PHOSPHATE ION
HETNAM NA SODIUM ION
HETSYN GLC ALPHA-D-GLUCOSE; D-GLUCOSE; GLUCOSE
HETSYN AC1 6-METHYL-5-(4,5,6-TRIHYDROXY-3-HYDROXYMETHYL-CYCLOHEX-
HETSYN 2 AC1 2-ENYLAMINO)-TETRAHYDRO-PYRAN-2,3,4-TRIOL; 4,6-
HETSYN 3 AC1 DIDEOXY-4-{[(1S,4R,5S,6S)-4,5,6-TRIHYDROXY-3-
HETSYN 4 AC1 (HYDROXYMETHYL)CYCLOHEX-2-EN-1-YL]AMINO}-ALPHA-D-
HETSYN 5 AC1 GLUCOSE; 4,6-DIDEOXY-4-{[(1S,4R,5S,6S)-4,5,6-
HETSYN 6 AC1 TRIHYDROXY-3-(HYDROXYMETHYL)CYCLOHEX-2-EN-1-YL]AMINO}-
HETSYN 7 AC1 D-GLUCOSE; 4,6-DIDEOXY-4-{[(1S,4R,5S,6S)-4,5,6-
HETSYN 8 AC1 TRIHYDROXY-3-(HYDROXYMETHYL)CYCLOHEX-2-EN-1-YL]AMINO}-
HETSYN 9 AC1 GLUCOSE
FORMUL 2 GLC 4(C6 H12 O6)
FORMUL 2 AC1 2(C13 H23 N O8)
FORMUL 4 PO4 O4 P 3-
FORMUL 5 NA 2(NA 1+)
FORMUL 7 HOH *810(H2 O)
HELIX 1 1 ASP A 17 ASN A 36 1 20
HELIX 2 2 THR A 68 ASN A 85 1 18
HELIX 3 3 ASN A 88 ARG A 107 1 20
HELIX 4 4 ASP A 117 GLU A 125 5 9
HELIX 5 5 ASN A 144 ASN A 165 1 22
HELIX 6 6 SER A 181 ILE A 189 1 9
HELIX 7 7 ILE A 189 TRP A 201 1 13
HELIX 8 8 HIS A 216 PHE A 237 1 22
HELIX 9 9 ASP A 239 GLY A 259 1 21
HELIX 10 10 ASN A 275 GLN A 281 1 7
HELIX 11 11 SER A 289 HIS A 299 1 11
HELIX 12 12 ASN A 313 TYR A 331 1 19
HELIX 13 13 SER A 332 SER A 335 5 4
HELIX 14 14 TRP A 362 SER A 384 1 23
HELIX 15 15 ASN A 393 ILE A 401 1 9
HELIX 16 16 ASP A 403 ASN A 408 1 6
HELIX 17 17 ALA A 410 SER A 414 5 5
HELIX 18 18 SER A 423 ILE A 448 1 26
HELIX 19 19 LEU A 471 LEU A 491 1 21
SHEET 1 A 2 GLN A 66 TRP A 67 0
SHEET 2 A 2 LYS A 127 PHE A 128 -1 O PHE A 128 N GLN A 66
SHEET 1 B 2 VAL A 265 ASN A 266 0
SHEET 2 B 2 HIS A 271 ILE A 272 -1 O HIS A 271 N ASN A 266
SHEET 1 C 2 ILE A 387 ASN A 390 0
SHEET 2 C 2 SER A 416 ILE A 419 -1 O VAL A 417 N ILE A 389
SHEET 1 D 2 GLN A 457 LEU A 458 0
SHEET 2 D 2 SER A 465 THR A 466 -1 O THR A 466 N GLN A 457
LINK O4 GLC B 1 C1 GLC B 2 1555 1555 1.45
LINK O4 GLC B 2 C1 AC1 B 3 1555 1555 1.46
LINK O4 GLC C 1 C1 GLC C 2 1555 1555 1.45
LINK O4 GLC C 2 C1 AC1 C 3 1555 1555 1.45
LINK O ILE A 177 NA NA A 998 1555 1555 2.44
LINK OD1 ASP A 310 NA NA A 997 1555 1555 2.15
LINK NA NA A 997 O HOH A1620 1555 1555 2.20
LINK NA NA A 997 O HOH A1627 1555 1555 2.24
LINK NA NA A 997 O HOH A1646 1555 1555 2.04
LINK NA NA A 997 O HOH A1764 1555 1555 2.30
LINK NA NA A 998 O HOH A 999 1555 1555 2.52
LINK NA NA A 998 O HOH A1000 1555 1555 2.43
LINK NA NA A 998 O HOH A1350 1555 1455 2.37
LINK NA NA A 998 O HOH A1600 1555 1455 2.43
LINK NA NA A 998 O HOH A1613 1555 1555 2.33
CISPEP 1 ASN A 60 PRO A 61 0 -3.20
CISPEP 2 ARG A 141 PRO A 142 0 -6.52
CRYST1 56.580 85.350 97.510 90.00 90.00 90.00 P 21 21 21 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 0.017674 0.000000 0.000000 0.00000
SCALE2 0.000000 0.011716 0.000000 0.00000
SCALE3 0.000000 0.000000 0.010255 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
