HEADER HYDROLASE 16-SEP-03 1ULV
TITLE CRYSTAL STRUCTURE OF GLUCODEXTRANASE COMPLEXED WITH ACARBOSE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: GLUCODEXTRANASE;
COMPND 3 CHAIN: A;
COMPND 4 EC: 3.2.1.70
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ARTHROBACTER GLOBIFORMIS;
SOURCE 3 ORGANISM_TAXID: 1665;
SOURCE 4 STRAIN: I42
KEYWDS GH FAMILY 15, (ALPHA-ALPHA)6-BARREL, SLH DOMAIN, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR M.MIZUNO,T.TONOZUKA,S.SUZUKI,R.UOTSU-TOMITA,S.KAMITORI,A.NISHIKAWA,
AUTHOR 2 Y.SAKANO
REVDAT 6 27-DEC-23 1ULV 1 HETSYN
REVDAT 5 29-JUL-20 1ULV 1 COMPND REMARK HET HETNAM
REVDAT 5 2 1 HETSYN FORMUL LINK SITE
REVDAT 5 3 1 ATOM
REVDAT 4 13-JUL-11 1ULV 1 VERSN
REVDAT 3 24-FEB-09 1ULV 1 VERSN
REVDAT 2 30-MAR-04 1ULV 1 JRNL
REVDAT 1 09-DEC-03 1ULV 0
JRNL AUTH M.MIZUNO,T.TONOZUKA,S.SUZUKI,R.UOTSU-TOMITA,S.KAMITORI,
JRNL AUTH 2 A.NISHIKAWA,Y.SAKANO
JRNL TITL STRUCTURAL INSIGHTS INTO SUBSTRATE SPECIFICITY AND FUNCTION
JRNL TITL 2 OF GLUCODEXTRANASE
JRNL REF J.BIOL.CHEM. V. 279 10575 2004
JRNL REFN ISSN 0021-9258
JRNL PMID 14660574
JRNL DOI 10.1074/JBC.M310771200
REMARK 2
REMARK 2 RESOLUTION. 2.42 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 1.1
REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-
REMARK 3 : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,
REMARK 3 : READ,RICE,SIMONSON,WARREN
REMARK 3
REMARK 3 REFINEMENT TARGET : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.42
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 49.59
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 4504609.140
REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0000
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 98.0
REMARK 3 NUMBER OF REFLECTIONS : 48692
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 SET) : 0.196
REMARK 3 FREE R VALUE : 0.238
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 10.100
REMARK 3 FREE R VALUE TEST SET COUNT : 4919
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.003
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 6
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.42
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.55
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 79.80
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 5994
REMARK 3 BIN R VALUE (WORKING SET) : 0.2250
REMARK 3 BIN FREE R VALUE : 0.2860
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 10.30
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 689
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.011
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 7506
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 38
REMARK 3 SOLVENT ATOMS : 436
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 23.00
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 26.50
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -1.70000
REMARK 3 B22 (A**2) : -4.14000
REMARK 3 B33 (A**2) : 5.83000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 6.05000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.25
REMARK 3 ESD FROM SIGMAA (A) : 0.18
REMARK 3 LOW RESOLUTION CUTOFF (A) : 5.00
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : 0.32
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.27
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.006
REMARK 3 BOND ANGLES (DEGREES) : 1.300
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 24.80
REMARK 3 IMPROPER ANGLES (DEGREES) : 0.770
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : RESTRAINED
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : 1.170 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 1.870 ; 2.000
REMARK 3 SIDE-CHAIN BOND (A**2) : 1.950 ; 2.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 2.720 ; 2.500
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : FLAT MODEL
REMARK 3 KSOL : 0.37
REMARK 3 BSOL : 40.11
REMARK 3
REMARK 3 NCS MODEL : NULL
REMARK 3
REMARK 3 NCS RESTRAINTS. RMS SIGMA/WEIGHT
REMARK 3 GROUP 1 POSITIONAL (A) : NULL ; NULL
REMARK 3 GROUP 1 B-FACTOR (A**2) : NULL ; NULL
REMARK 3
REMARK 3 PARAMETER FILE 1 : PROTEIN_REP.PARAM
REMARK 3 PARAMETER FILE 2 : CARBOHYDRATE.PARAM
REMARK 3 PARAMETER FILE 3 : WATER_REP.PARAM
REMARK 3 PARAMETER FILE 4 : ION.PARAM
REMARK 3 PARAMETER FILE 5 : ACR.PARAM
REMARK 3 PARAMETER FILE 6 : NULL
REMARK 3 TOPOLOGY FILE 1 : PROTEIN.TOP
REMARK 3 TOPOLOGY FILE 2 : CARBOHYDRATE.TOP
REMARK 3 TOPOLOGY FILE 3 : WATER.TOP
REMARK 3 TOPOLOGY FILE 4 : ION.TOP
REMARK 3 TOPOLOGY FILE 5 : ACR.TOP
REMARK 3 TOPOLOGY FILE 6 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1ULV COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 19-SEP-03.
REMARK 100 THE DEPOSITION ID IS D_1000005969.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 28-JUN-03
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 5.1
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : PHOTON FACTORY
REMARK 200 BEAMLINE : AR-NW12A
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 4
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 48692
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.418
REMARK 200 RESOLUTION RANGE LOW (A) : 49.590
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.8
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.42
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.51
REMARK 200 COMPLETENESS FOR SHELL (%) : 95.3
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: CNS
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 57.78
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.94
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 8000, POTASSIUM DIHYDROGEN
REMARK 280 PHOSPHATE, PH 5.1, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE
REMARK 280 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,Y,-Z
REMARK 290 3555 X+1/2,Y+1/2,Z
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 0.00000
REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 3 1.000000 0.000000 0.000000 99.39750
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 44.12350
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 99.39750
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 44.12350
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
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 GLU A 1
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 546 CB - CG - OD1 ANGL. DEV. = 6.5 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 TRP A 15 -154.06 -95.30
REMARK 500 LYS A 32 40.80 -86.48
REMARK 500 SER A 43 -132.50 -92.96
REMARK 500 TYR A 47 143.87 177.08
REMARK 500 SER A 113 73.77 -68.66
REMARK 500 ASP A 125 -161.12 -107.81
REMARK 500 ASP A 128 73.07 73.77
REMARK 500 SER A 138 58.07 -155.17
REMARK 500 ASP A 159 95.59 -160.04
REMARK 500 THR A 187 -57.05 -147.31
REMARK 500 ASP A 197 28.30 -148.42
REMARK 500 SER A 308 135.73 -174.65
REMARK 500 PRO A 487 38.68 -74.09
REMARK 500 PRO A 503 -9.08 -58.95
REMARK 500 ARG A 589 -159.38 -104.47
REMARK 500 THR A 637 -164.07 -61.95
REMARK 500 SER A 651 115.20 -164.21
REMARK 500 THR A 687 127.88 -34.10
REMARK 500 SER A 740 119.89 -165.37
REMARK 500 ASP A 787 49.77 -73.31
REMARK 500 ALA A 800 -32.29 -39.80
REMARK 500 ALA A 816 57.67 -106.39
REMARK 500 ASN A 832 58.94 -158.55
REMARK 500 TRP A 834 17.65 -62.83
REMARK 500 ALA A 838 -54.61 70.02
REMARK 500 SER A 840 -42.70 -131.27
REMARK 500 PRO A 860 -89.24 -29.83
REMARK 500 LEU A 916 61.28 -101.40
REMARK 500 PRO A 957 -171.48 -69.50
REMARK 500 ARG A 979 3.40 59.86
REMARK 500 ASP A 990 150.34 173.64
REMARK 500 ASP A1004 88.00 -69.32
REMARK 500
REMARK 500 REMARK: NULL
REMARK 610
REMARK 610 MISSING HETEROATOM
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 610 I=INSERTION CODE):
REMARK 610 M RES C SSEQI
REMARK 610 GLC B 1
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 A2003 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 136 OD2
REMARK 620 2 PRO A 137 O 84.4
REMARK 620 3 ASN A 211 OD1 112.2 142.1
REMARK 620 4 ILE A 212 O 74.5 117.4 100.2
REMARK 620 5 HOH A3037 O 152.3 79.7 94.1 92.9
REMARK 620 6 HOH A3041 O 87.5 72.5 74.4 157.7 108.9
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A2001 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 LEU A 139 O
REMARK 620 2 THR A 142 O 84.3
REMARK 620 3 THR A 142 OG1 82.2 74.8
REMARK 620 4 GLY A 144 O 162.8 86.3 81.4
REMARK 620 5 ASP A 146 OD1 101.4 106.1 176.3 95.0
REMARK 620 6 ASP A 159 OD2 95.2 163.6 89.0 89.8 90.0
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A2002 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 PHE A 358 O
REMARK 620 2 GLN A 362 OE1 96.8
REMARK 620 3 GLU A 409 OE2 87.6 92.7
REMARK 620 4 HOH A3146 O 165.6 82.8 78.0
REMARK 620 5 HOH A3190 O 85.6 173.2 81.0 93.3
REMARK 620 6 HOH A3308 O 102.2 118.2 145.5 90.6 67.2
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A2005 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 782 OD1
REMARK 620 2 PRO A 783 O 91.1
REMARK 620 3 ASP A 807 OD2 174.8 93.4
REMARK 620 4 LEU A 808 O 91.9 99.5 84.9
REMARK 620 5 ASP A 990 OD2 80.6 162.9 95.7 95.7
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A2006 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 782 OD1
REMARK 620 2 ASP A 782 OD2 49.1
REMARK 620 3 VAL A 991 O 108.4 72.2
REMARK 620 4 GLN A 999 OE1 152.4 154.8 84.0
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A2004 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 VAL A 946 O
REMARK 620 2 ALA A 969 O 96.8
REMARK 620 3 ASP A 980 OD2 72.4 112.5
REMARK 620 4 ASP A 982 O 153.5 86.6 82.0
REMARK 620 5 ASP A 985 OD1 135.3 81.0 149.4 71.3
REMARK 620 6 ASP A 985 OD2 82.2 104.9 136.6 122.5 56.1
REMARK 620 N 1 2 3 4 5
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1UG9 RELATED DB: PDB
REMARK 900 UNLIGANDED STRUCTURE OF GLUCODEXTRANASE
DBREF 1ULV A 1 1020 UNP Q9LBQ9 Q9LBQ9_ARTGO 29 1048
SEQRES 1 A 1020 GLU THR ALA GLU PRO PRO GLY SER PRO GLY ALA ALA ALA
SEQRES 2 A 1020 THR TRP THR LYS GLY ASP LYS GLU GLY VAL GLY THR SER
SEQRES 3 A 1020 LEU ASN PRO ALA SER LYS VAL TRP TYR THR LEU THR GLU
SEQRES 4 A 1020 GLY THR MET SER GLU VAL TYR TYR PRO HIS ALA ASP THR
SEQRES 5 A 1020 PRO ASN THR ARG GLU LEU GLN PHE ALA VAL SER ASP GLY
SEQRES 6 A 1020 THR SER ALA GLN ARG GLU SER GLU GLN THR THR ARG THR
SEQRES 7 A 1020 VAL GLU LEU ALA ASP PRO LYS ALA LEU SER TYR ARG GLN
SEQRES 8 A 1020 THR THR THR ASP ASN ALA GLY ARG TRP ARG LEU THR LYS
SEQRES 9 A 1020 THR TYR VAL THR ASP PRO ARG ARG SER THR VAL MET LEU
SEQRES 10 A 1020 GLY VAL THR PHE GLU VAL LEU ASP GLY GLY ASP TYR GLN
SEQRES 11 A 1020 LEU PHE VAL LEU SER ASP PRO SER LEU ALA GLY THR SER
SEQRES 12 A 1020 GLY GLY ASP THR GLY SER VAL THR ASP GLY ALA LEU LEU
SEQRES 13 A 1020 ALA SER ASP LEU ALA ASP ALA ALA THR PRO VAL ALA THR
SEQRES 14 A 1020 ALA LEU VAL SER SER VAL GLY PHE GLY ALA VAL ALA ASN
SEQRES 15 A 1020 GLY TYR VAL GLY THR SER ASP GLY TRP THR ASP LEU ALA
SEQRES 16 A 1020 ALA ASP GLY ARG LEU ASP ASN ALA SER ALA THR ALA GLY
SEQRES 17 A 1020 PRO GLY ASN ILE SER GLN THR GLY GLN ILE PRO LEU ALA
SEQRES 18 A 1020 ALA GLY GLY LYS THR GLU PHE SER LEU ALA LEU GLY PHE
SEQRES 19 A 1020 GLY ALA ASP THR ALA GLU ALA LEU ALA THR ALA LYS ALA
SEQRES 20 A 1020 SER LEU GLY THR GLY TYR LYS LYS VAL SER LYS SER TYR
SEQRES 21 A 1020 THR GLY GLU TRP LYS LYS TYR LEU ASN SER LEU ASP ALA
SEQRES 22 A 1020 PRO ALA THR SER LEU THR GLY ALA LEU ARG THR GLN TYR
SEQRES 23 A 1020 ASP VAL SER LEU MET THR VAL LYS SER HIS GLU ASP LYS
SEQRES 24 A 1020 THR PHE PRO GLY ALA PHE ILE ALA SER LEU THR ILE PRO
SEQRES 25 A 1020 TRP GLY GLN ALA ALA SER ALA GLU THR HIS ARG GLU GLY
SEQRES 26 A 1020 TYR HIS ALA VAL TRP ALA ARG ASP MET TYR GLN SER VAL
SEQRES 27 A 1020 THR ALA LEU LEU ALA ALA GLY ASP GLU GLU ALA ALA ALA
SEQRES 28 A 1020 ARG GLY VAL GLU TRP LEU PHE THR TYR GLN GLN GLN PRO
SEQRES 29 A 1020 ASP GLY HIS PHE PRO GLN THR SER ARG VAL ASP GLY THR
SEQRES 30 A 1020 ILE GLY GLN ASN GLY ILE GLN LEU ASP GLU THR ALA PHE
SEQRES 31 A 1020 PRO ILE LEU LEU ALA ASN GLN ILE GLY ARG THR ASP ALA
SEQRES 32 A 1020 GLY PHE TYR ARG ASN GLU LEU LYS PRO ALA ALA ASP TYR
SEQRES 33 A 1020 LEU VAL ALA ALA GLY PRO LYS THR PRO GLN GLU ARG TRP
SEQRES 34 A 1020 GLU GLU THR GLY GLY TYR SER THR SER THR LEU ALA SER
SEQRES 35 A 1020 GLN ILE ALA ALA LEU ALA ALA ALA ALA ASP ILE ALA GLY
SEQRES 36 A 1020 LYS ASN GLY ASP ALA GLY SER ALA ALA VAL TYR ARG ALA
SEQRES 37 A 1020 THR ALA ASP GLU TRP GLN ARG SER THR GLU LYS TRP MET
SEQRES 38 A 1020 PHE THR THR ASN GLY PRO VAL GLY ASP GLY LYS TYR TYR
SEQRES 39 A 1020 LEU ARG ILE SER ALA THR GLY ASN PRO ASN ASP GLY ALA
SEQRES 40 A 1020 THR ARG ASP TRP GLY ASN GLY ALA GLY VAL HIS PRO GLU
SEQRES 41 A 1020 ASN ALA VAL LEU ASP GLY GLY PHE LEU GLU PHE VAL ARG
SEQRES 42 A 1020 LEU GLY VAL LYS ALA PRO ALA ASP PRO TYR VAL ALA ASP
SEQRES 43 A 1020 SER LEU ALA GLU THR ASP ALA SER ILE SER GLN GLU THR
SEQRES 44 A 1020 PRO GLY GLY ARG MET TRP HIS ARG TYR THR TYR ASP GLY
SEQRES 45 A 1020 TYR GLY GLU LYS ALA ASP GLY SER PRO TRP ASP GLY THR
SEQRES 46 A 1020 GLY ILE GLY ARG LEU TRP PRO LEU LEU SER GLY GLU ARG
SEQRES 47 A 1020 GLY GLU TYR ALA LEU ALA ASN GLY GLN ASP ALA LEU PRO
SEQRES 48 A 1020 TYR LEU GLU THR MET HIS SER ALA ALA ASN ALA GLY TYR
SEQRES 49 A 1020 MET ILE PRO GLU GLN VAL TRP ASP ARG ASP GLU PRO THR
SEQRES 50 A 1020 SER TYR GLY HIS GLU LEU GLY ARG SER THR GLY SER ALA
SEQRES 51 A 1020 SER PRO LEU SER TRP ALA MET ALA GLN TYR VAL ARG LEU
SEQRES 52 A 1020 ALA ALA GLY VAL LYS ALA GLY ALA PRO VAL GLU THR PRO
SEQRES 53 A 1020 GLN ASN VAL ALA ALA ARG TYR ALA ALA GLY THR PRO LEU
SEQRES 54 A 1020 SER SER PRO GLU LEU SER VAL THR ALA PRO GLU ALA LEU
SEQRES 55 A 1020 SER THR ALA ASP SER ALA THR ALA VAL VAL ARG GLY THR
SEQRES 56 A 1020 THR ASN ALA ALA LYS VAL TYR VAL SER VAL ASN GLY THR
SEQRES 57 A 1020 ALA THR GLU ALA PRO VAL THR ASP GLY THR PHE SER LEU
SEQRES 58 A 1020 ASP VAL ALA LEU THR GLY ALA LYS ASN LYS VAL THR VAL
SEQRES 59 A 1020 ALA ALA VAL ALA ALA ASP GLY GLY THR ALA VAL GLU ASP
SEQRES 60 A 1020 ARG THR VAL LEU TYR TYR GLY SER ARG ILE GLY ALA LEU
SEQRES 61 A 1020 SER ASP PRO ALA GLY ASP ASP ASN GLY PRO GLY THR TYR
SEQRES 62 A 1020 ARG TYR PRO THR ASN SER ALA TYR VAL PRO GLY ALA PHE
SEQRES 63 A 1020 ASP LEU THR GLY VAL ASP VAL TYR ASP ALA GLY ASP ASP
SEQRES 64 A 1020 TYR ALA PHE VAL ALA THR ILE ALA GLY GLU VAL THR ASN
SEQRES 65 A 1020 PRO TRP GLY GLY GLN ALA ILE SER HIS GLN ARG VAL ASN
SEQRES 66 A 1020 ILE TYR LEU GLY LYS GLY GLU GLY GLY ALA THR PRO GLY
SEQRES 67 A 1020 LEU PRO GLY THR ASN ILE ASN LEU GLU HIS ALA TRP ASP
SEQRES 68 A 1020 SER VAL ILE VAL THR ASP GLY ARG PHE ASP GLY ALA GLY
SEQRES 69 A 1020 VAL TYR ALA PRO ASP GLY THR ARG THR SER ALA VAL SER
SEQRES 70 A 1020 LEU LEU ALA VAL PRO GLU ALA ARG GLN ILE VAL THR ARG
SEQRES 71 A 1020 VAL PRO LYS ALA ALA LEU GLY GLY LEU ASP PRO ALA THR
SEQRES 72 A 1020 ALA ARG MET SER VAL ALA MET PHE GLY ASN ALA GLU SER
SEQRES 73 A 1020 GLY GLU GLY ILE GLY ASN VAL ARG PRO VAL TYR ASP GLY
SEQRES 74 A 1020 ALA TYR TRP GLU ALA GLY ASP PRO ALA TRP ILE LYS GLU
SEQRES 75 A 1020 TRP ARG PHE GLY GLY GLY ALA GLY VAL PHE ASP GLY THR
SEQRES 76 A 1020 ILE PRO SER ARG ASP THR ASP THR ASP ASP PRO ASN ALA
SEQRES 77 A 1020 LEU ASP VAL LEU VAL GLY GLU GLY GLN THR GLN ALA ALA
SEQRES 78 A 1020 VAL LEU ASP TRP ARG ALA GLY SER PRO VAL VAL VAL PRO
SEQRES 79 A 1020 MET LEU GLY LEU GLN PRO
HET GLC B 1 11
HET AC1 B 2 21
HET CA A2001 1
HET CA A2002 1
HET CA A2003 1
HET CA A2004 1
HET CA A2005 1
HET CA A2006 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 CA CALCIUM 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 C6 H12 O6
FORMUL 2 AC1 C13 H23 N O8
FORMUL 3 CA 6(CA 2+)
FORMUL 9 HOH *436(H2 O)
HELIX 1 1 SER A 72 GLN A 74 5 3
HELIX 2 2 LEU A 139 THR A 142 5 4
HELIX 3 3 ASP A 189 GLY A 198 1 10
HELIX 4 4 ASP A 237 GLY A 252 1 16
HELIX 5 5 GLY A 252 LEU A 271 1 20
HELIX 6 6 THR A 279 SER A 295 1 17
HELIX 7 7 TRP A 313 ALA A 317 5 5
HELIX 8 8 TRP A 330 GLY A 345 1 16
HELIX 9 9 ASP A 346 GLN A 361 1 16
HELIX 10 10 LEU A 385 GLY A 399 1 15
HELIX 11 11 ASP A 402 GLU A 409 1 8
HELIX 12 12 GLU A 409 GLY A 421 1 13
HELIX 13 13 THR A 437 ASN A 457 1 21
HELIX 14 14 ASP A 459 SER A 476 1 18
HELIX 15 15 SER A 476 MET A 481 1 6
HELIX 16 16 ASN A 521 VAL A 523 5 3
HELIX 17 17 ASP A 525 PHE A 528 5 4
HELIX 18 18 LEU A 529 LEU A 534 1 6
HELIX 19 19 ASP A 541 ILE A 555 1 15
HELIX 20 20 PRO A 592 ASN A 605 1 14
HELIX 21 21 ALA A 609 ALA A 619 1 11
HELIX 22 22 LEU A 653 GLY A 670 1 18
HELIX 23 23 PRO A 676 ALA A 684 1 9
HELIX 24 24 LEU A 859 ASN A 863 5 5
HELIX 25 25 ALA A 914 LEU A 916 5 3
HELIX 26 26 GLU A 935 VAL A 943 5 9
HELIX 27 27 GLY A 949 GLY A 955 1 7
HELIX 28 28 TRP A 959 ARG A 964 1 6
HELIX 29 29 THR A 998 LEU A 1003 1 6
HELIX 30 30 ASP A 1004 GLY A 1008 5 5
SHEET 1 A 3 GLY A 22 GLY A 24 0
SHEET 2 A 3 TRP A 34 THR A 38 -1 O TYR A 35 N GLY A 24
SHEET 3 A 3 THR A 41 TYR A 46 -1 O TYR A 46 N TRP A 34
SHEET 1 B 5 ALA A 68 ARG A 70 0
SHEET 2 B 5 THR A 55 SER A 63 -1 N VAL A 62 O GLN A 69
SHEET 3 B 5 GLN A 130 PRO A 137 -1 O GLN A 130 N SER A 63
SHEET 4 B 5 ILE A 212 ILE A 218 -1 O GLY A 216 N VAL A 133
SHEET 5 B 5 VAL A 180 TYR A 184 -1 N ALA A 181 O THR A 215
SHEET 1 C 9 ARG A 77 LEU A 81 0
SHEET 2 C 9 TYR A 89 THR A 94 -1 O ARG A 90 N GLU A 80
SHEET 3 C 9 TRP A 100 THR A 108 -1 O LYS A 104 N GLN A 91
SHEET 4 C 9 THR A 114 VAL A 123 -1 O MET A 116 N VAL A 107
SHEET 5 C 9 LYS A 225 GLY A 235 -1 O LEU A 232 N VAL A 115
SHEET 6 C 9 VAL A 167 SER A 173 -1 N VAL A 172 O ALA A 231
SHEET 7 C 9 ALA A 154 ASP A 159 -1 N LEU A 155 O LEU A 171
SHEET 8 C 9 ASP A 146 THR A 151 -1 N SER A 149 O LEU A 156
SHEET 9 C 9 ALA A 207 GLY A 210 -1 O ALA A 207 N GLY A 148
SHEET 1 D 2 TYR A 435 SER A 436 0
SHEET 2 D 2 ILE A 497 SER A 498 -1 O SER A 498 N TYR A 435
SHEET 1 E 2 PHE A 482 THR A 483 0
SHEET 2 E 2 TYR A 493 TYR A 494 -1 O TYR A 493 N THR A 483
SHEET 1 F 2 THR A 508 ASP A 510 0
SHEET 2 F 2 VAL A 517 PRO A 519 -1 O HIS A 518 N ARG A 509
SHEET 1 G 2 SER A 556 THR A 559 0
SHEET 2 G 2 GLY A 562 TRP A 565 -1 O MET A 564 N GLN A 557
SHEET 1 H 3 LEU A 694 ALA A 698 0
SHEET 2 H 3 THR A 709 THR A 716 -1 O THR A 715 N SER A 695
SHEET 3 H 3 THR A 738 ALA A 744 -1 O LEU A 741 N VAL A 712
SHEET 1 I 5 LEU A 702 THR A 704 0
SHEET 2 I 5 THR A 763 LEU A 771 1 O LEU A 771 N SER A 703
SHEET 3 I 5 LYS A 749 VAL A 757 -1 N VAL A 752 O ARG A 768
SHEET 4 I 5 LYS A 720 VAL A 725 -1 N SER A 724 O THR A 753
SHEET 5 I 5 THR A 728 ALA A 732 -1 O ALA A 732 N VAL A 721
SHEET 1 J 5 SER A 775 SER A 781 0
SHEET 2 J 5 LEU A 808 ALA A 816 -1 O ASP A 815 N SER A 775
SHEET 3 J 5 ASP A 819 ILE A 826 -1 O VAL A 823 N ASP A 812
SHEET 4 J 5 GLN A 906 PRO A 912 -1 O VAL A 911 N TYR A 820
SHEET 5 J 5 SER A 897 VAL A 901 -1 N LEU A 899 O VAL A 908
SHEET 1 K 6 ARG A 892 SER A 894 0
SHEET 2 K 6 GLY A 884 TYR A 886 -1 N VAL A 885 O SER A 894
SHEET 3 K 6 TRP A 870 THR A 876 -1 N VAL A 873 O TYR A 886
SHEET 4 K 6 GLN A 842 GLY A 849 -1 N LEU A 848 O SER A 872
SHEET 5 K 6 ARG A 925 GLY A 932 -1 O ARG A 925 N GLY A 849
SHEET 6 K 6 ASP A 990 VAL A 991 -1 O ASP A 990 N MET A 930
SHEET 1 L 6 ARG A 892 SER A 894 0
SHEET 2 L 6 GLY A 884 TYR A 886 -1 N VAL A 885 O SER A 894
SHEET 3 L 6 TRP A 870 THR A 876 -1 N VAL A 873 O TYR A 886
SHEET 4 L 6 GLN A 842 GLY A 849 -1 N LEU A 848 O SER A 872
SHEET 5 L 6 ARG A 925 GLY A 932 -1 O ARG A 925 N GLY A 849
SHEET 6 L 6 LEU A1016 GLY A1017 -1 O LEU A1016 N MET A 926
SHEET 1 M 3 THR A 856 PRO A 857 0
SHEET 2 M 3 ASN A 865 LEU A 866 -1 O LEU A 866 N THR A 856
SHEET 3 M 3 VAL A1012 VAL A1013 1 O VAL A1013 N ASN A 865
SHEET 1 N 2 VAL A 946 ASP A 948 0
SHEET 2 N 2 PHE A 965 GLY A 968 1 O GLY A 968 N TYR A 947
LINK O4 GLC B 1 C1 AC1 B 2 1555 1555 1.43
LINK OD2 ASP A 136 CA CA A2003 1555 1555 2.32
LINK O PRO A 137 CA CA A2003 1555 1555 2.46
LINK O LEU A 139 CA CA A2001 1555 1555 2.38
LINK O THR A 142 CA CA A2001 1555 1555 2.53
LINK OG1 THR A 142 CA CA A2001 1555 1555 2.48
LINK O GLY A 144 CA CA A2001 1555 1555 2.42
LINK OD1 ASP A 146 CA CA A2001 1555 1555 2.52
LINK OD2 ASP A 159 CA CA A2001 1555 1555 2.48
LINK OD1 ASN A 211 CA CA A2003 1555 1555 2.23
LINK O ILE A 212 CA CA A2003 1555 1555 2.44
LINK O PHE A 358 CA CA A2002 1555 1555 2.33
LINK OE1 GLN A 362 CA CA A2002 1555 1555 2.50
LINK OE2 GLU A 409 CA CA A2002 1555 1555 2.33
LINK OD1 ASP A 782 CA CA A2005 1555 1555 2.35
LINK OD1 ASP A 782 CA CA A2006 1555 1555 2.57
LINK OD2 ASP A 782 CA CA A2006 1555 1555 2.70
LINK O PRO A 783 CA CA A2005 1555 1555 2.35
LINK OD2 ASP A 807 CA CA A2005 1555 1555 2.44
LINK O LEU A 808 CA CA A2005 1555 1555 2.26
LINK O VAL A 946 CA CA A2004 1555 1555 2.46
LINK O ALA A 969 CA CA A2004 1555 1555 2.28
LINK OD2 ASP A 980 CA CA A2004 1555 1555 2.32
LINK O ASP A 982 CA CA A2004 1555 1555 2.47
LINK OD1 ASP A 985 CA CA A2004 1555 1555 2.36
LINK OD2 ASP A 985 CA CA A2004 1555 1555 2.29
LINK OD2 ASP A 990 CA CA A2005 1555 1555 2.95
LINK O VAL A 991 CA CA A2006 1555 1555 2.34
LINK OE1 GLN A 999 CA CA A2006 1555 1555 2.28
LINK CA CA A2002 O HOH A3146 1555 1555 2.43
LINK CA CA A2002 O HOH A3190 1555 1555 2.71
LINK CA CA A2002 O HOH A3308 1555 1555 2.59
LINK CA CA A2003 O HOH A3037 1555 1555 2.35
LINK CA CA A2003 O HOH A3041 1555 1555 2.40
CISPEP 1 SER A 8 PRO A 9 0 0.23
CISPEP 2 TYR A 47 PRO A 48 0 -0.11
CISPEP 3 GLY A 208 PRO A 209 0 0.26
CISPEP 4 SER A 651 PRO A 652 0 0.58
CISPEP 5 ALA A 698 PRO A 699 0 0.09
CISPEP 6 ASP A 956 PRO A 957 0 0.11
CISPEP 7 SER A 1009 PRO A 1010 0 -0.21
CRYST1 198.795 88.247 80.994 90.00 112.55 90.00 C 1 2 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 0.005030 0.000000 0.002089 0.00000
SCALE2 0.000000 0.011332 0.000000 0.00000
SCALE3 0.000000 0.000000 0.013369 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
