HEADER SUGAR BINDING PROTEIN 12-OCT-05 2C3W
TITLE STRUCTURE OF CBM25 FROM BACILLUS HALODURANS AMYLASE IN COMPLEX WITH
TITLE 2 MALTOTETRAOSE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ALPHA-AMYLASE G-6;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 FRAGMENT: CARBOHYDRATE-BINDING MODULE, RESIDUES 863-958;
COMPND 5 SYNONYM: FAMILY 25 CARBOHYDRATE-BINDING MODULE;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: BACILLUS HALODURANS;
SOURCE 3 ORGANISM_TAXID: 272558;
SOURCE 4 STRAIN: C-125;
SOURCE 5 ATCC: BAA-125;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR: PET 28A;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET-BHCBM6
KEYWDS SUGAR-BINDING PROTEIN, CARBOHYDRATE-BINDING MODULE, STARCH BINDING,
KEYWDS 2 CARBOHYDRATE BINDING, GLYCOSIDE HYDROLASE, AMYLOSE, AMYLOPECTIN,
KEYWDS 3 MALTO-OLIGOSACCHARIDE, SUGAR BINDING PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR A.B.BORASTON,M.HEALEY,J.KLASSEN,E.FICKO-BLEAN,A.LAMMERTS VAN BUEREN,
AUTHOR 2 V.LAW
REVDAT 4 29-JUL-20 2C3W 1 COMPND REMARK HETNAM LINK
REVDAT 4 2 1 SITE ATOM
REVDAT 3 24-FEB-09 2C3W 1 VERSN
REVDAT 2 18-JAN-06 2C3W 1 JRNL
REVDAT 1 17-OCT-05 2C3W 0
JRNL AUTH A.B.BORASTON,M.HEALEY,J.KLASSEN,E.FICKO-BLEAN,
JRNL AUTH 2 A.LAMMERTS VAN BUEREN,V.LAW
JRNL TITL A STRUCTURAL AND FUNCTIONAL ANALYSIS OF ALPHA-GLUCAN
JRNL TITL 2 RECOGNITION BY FAMILY 25 AND 26 CARBOHYDRATE-BINDING MODULES
JRNL TITL 3 REVEALS A CONSERVED MODE OF STARCH RECOGNITION
JRNL REF J.BIOL.CHEM. V. 281 587 2006
JRNL REFN ISSN 0021-9258
JRNL PMID 16230347
JRNL DOI 10.1074/JBC.M509958200
REMARK 2
REMARK 2 RESOLUTION. 1.81 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) : 1.81
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 63.25
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.2
REMARK 3 NUMBER OF REFLECTIONS : 47599
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) : 0.161
REMARK 3 R VALUE (WORKING SET) : 0.158
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 : 2544
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) : 1.81
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.86
REMARK 3 REFLECTION IN BIN (WORKING SET) : 3517
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : 0.2260
REMARK 3 BIN FREE R VALUE SET COUNT : 182
REMARK 3 BIN FREE R VALUE : 0.2790
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2959
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 414
REMARK 3 SOLVENT ATOMS : 783
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 18.84
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.29000
REMARK 3 B22 (A**2) : -1.24000
REMARK 3 B33 (A**2) : 1.10000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : -0.86000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.107
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.110
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.073
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 2.368
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.966
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.948
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 3486 ; 0.020 ; 0.021
REMARK 3 BOND LENGTHS OTHERS (A): 2764 ; 0.003 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 4806 ; 1.975 ; 2.056
REMARK 3 BOND ANGLES OTHERS (DEGREES): 6412 ; 1.375 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 376 ; 7.036 ; 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): 610 ; 0.149 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 3485 ; 0.009 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 635 ; 0.006 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 578 ; 0.220 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): 3358 ; 0.273 ; 0.200
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): 1865 ; 0.095 ; 0.200
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 532 ; 0.170 ; 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): 7 ; 0.228 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): 35 ; 0.358 ; 0.200
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 52 ; 0.161 ; 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): 1861 ; 1.184 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 2986 ; 2.105 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1625 ; 3.200 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1819 ; 5.072 ; 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): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : 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 2C3W COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 12-OCT-05.
REMARK 100 THE DEPOSITION ID IS D_1290025973.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : NULL
REMARK 200 TEMPERATURE (KELVIN) : 113.0
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : NULL
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : ROTATING ANODE
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : NULL
REMARK 200 DETECTOR MANUFACTURER : NULL
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : NULL
REMARK 200 DATA SCALING SOFTWARE : NULL
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 47599
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.810
REMARK 200 RESOLUTION RANGE LOW (A) : 20.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.0
REMARK 200 DATA REDUNDANCY : 4.200
REMARK 200 R MERGE (I) : 0.05000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 17.3000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
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: OTHER
REMARK 200 SOFTWARE USED: NULL
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 48.78
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.42
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL
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 47.27650
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, 3, 4
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, E, F, G
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, H, I
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: 3
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: C, J
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: 4
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: D, K, L, M
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 GLY A 1
REMARK 465 SER A 2
REMARK 465 HIS A 3
REMARK 465 MET A 4
REMARK 465 ALA A 5
REMARK 465 SER A 6
REMARK 465 GLY A 7
REMARK 465 GLY B 1
REMARK 465 SER B 2
REMARK 465 HIS B 3
REMARK 465 MET B 4
REMARK 465 ALA B 5
REMARK 465 SER B 6
REMARK 465 GLY B 7
REMARK 465 GLY C 1
REMARK 465 SER C 2
REMARK 465 HIS C 3
REMARK 465 MET C 4
REMARK 465 ALA C 5
REMARK 465 SER C 6
REMARK 465 GLY C 7
REMARK 465 GLY D 1
REMARK 465 SER D 2
REMARK 465 HIS D 3
REMARK 465 MET D 4
REMARK 465 ALA D 5
REMARK 465 SER D 6
REMARK 465 GLY D 7
REMARK 465 ASP D 8
REMARK 465 LYS D 102
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 O HOH B 2151 O HOH C 2056 2645 2.18
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 8 CB - CG - OD2 ANGL. DEV. = 6.8 DEGREES
REMARK 500 ASP A 11 CB - CG - OD2 ANGL. DEV. = 5.7 DEGREES
REMARK 500 ASP B 11 CB - CG - OD2 ANGL. DEV. = 6.1 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 THR A 10 -78.78 -121.60
REMARK 500 ASP A 81 166.60 69.55
REMARK 500 THR B 10 -70.97 -116.14
REMARK 500 ASP B 81 162.60 64.59
REMARK 500 THR C 10 -74.94 -118.86
REMARK 500 GLN C 31 18.97 59.61
REMARK 500 ASP C 81 168.62 64.54
REMARK 500 THR D 10 -63.94 -123.00
REMARK 500 GLN D 31 19.72 59.76
REMARK 500 ASP D 81 165.41 65.87
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 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH A2021 DISTANCE = 6.36 ANGSTROMS
REMARK 525 HOH A2029 DISTANCE = 6.30 ANGSTROMS
REMARK 525 HOH A2173 DISTANCE = 5.93 ANGSTROMS
REMARK 525 HOH B2007 DISTANCE = 5.89 ANGSTROMS
REMARK 525 HOH C2016 DISTANCE = 7.11 ANGSTROMS
REMARK 525 HOH C2026 DISTANCE = 6.04 ANGSTROMS
REMARK 700
REMARK 700 SHEET
REMARK 700 THE SHEET STRUCTURE OF THIS MOLECULE IS BIFURCATED. IN
REMARK 700 ORDER TO REPRESENT THIS FEATURE IN THE SHEET RECORDS BELOW,
REMARK 700 TWO SHEETS ARE DEFINED.
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2C3G RELATED DB: PDB
REMARK 900 STRUCTURE OF CBM26 FROM BACILLUS HALODURANS AMYLASE
REMARK 900 RELATED ID: 2C3H RELATED DB: PDB
REMARK 900 STRUCTURE OF CBM26 FROM BACILLUS HALODURANS AMYLASE IN COMPLEX WITH
REMARK 900 MALTOSE
REMARK 900 RELATED ID: 2C3V RELATED DB: PDB
REMARK 900 STRUCTURE OF IODINATED CBM25 FROM BACILLUS HALODURANS AMYLASE
REMARK 900 RELATED ID: 2C3X RELATED DB: PDB
REMARK 900 STRUCTURE OF IODINATED CBM25 FROM BACILLUS HALODURANS AMYLASE IN
REMARK 900 COMPLEX WITH MALTOTETRAOSE
DBREF 2C3W A 1 6 PDB 2C3W 2C3W 1 6
DBREF 2C3W A 7 102 UNP Q9KFR4 Q9KFR4_BACHD 863 958
DBREF 2C3W B 1 6 PDB 2C3W 2C3W 1 6
DBREF 2C3W B 7 102 UNP Q9KFR4 Q9KFR4_BACHD 863 958
DBREF 2C3W C 1 6 PDB 2C3W 2C3W 1 6
DBREF 2C3W C 7 102 UNP Q9KFR4 Q9KFR4_BACHD 863 958
DBREF 2C3W D 1 6 PDB 2C3W 2C3W 1 6
DBREF 2C3W D 7 102 UNP Q9KFR4 Q9KFR4_BACHD 863 958
SEQRES 1 A 102 GLY SER HIS MET ALA SER GLY ASP ALA THR ASP ILE THR
SEQRES 2 A 102 ILE TYR TYR LYS THR GLY TRP THR HIS PRO HIS ILE HIS
SEQRES 3 A 102 TYR SER LEU ASN GLN GLY ALA TRP THR THR LEU PRO GLY
SEQRES 4 A 102 VAL PRO LEU THR LYS SER GLU TYR GLU GLY TYR VAL LYS
SEQRES 5 A 102 VAL THR ILE GLU ALA GLU GLU GLY SER GLN LEU ARG ALA
SEQRES 6 A 102 ALA PHE ASN ASN GLY SER GLY GLN TRP ASP ASN ASN GLN
SEQRES 7 A 102 GLY ARG ASP TYR ASP PHE SER SER GLY VAL HIS THR LEU
SEQRES 8 A 102 ALA ASP GLY ARG ILE LEU SER GLY THR PRO LYS
SEQRES 1 B 102 GLY SER HIS MET ALA SER GLY ASP ALA THR ASP ILE THR
SEQRES 2 B 102 ILE TYR TYR LYS THR GLY TRP THR HIS PRO HIS ILE HIS
SEQRES 3 B 102 TYR SER LEU ASN GLN GLY ALA TRP THR THR LEU PRO GLY
SEQRES 4 B 102 VAL PRO LEU THR LYS SER GLU TYR GLU GLY TYR VAL LYS
SEQRES 5 B 102 VAL THR ILE GLU ALA GLU GLU GLY SER GLN LEU ARG ALA
SEQRES 6 B 102 ALA PHE ASN ASN GLY SER GLY GLN TRP ASP ASN ASN GLN
SEQRES 7 B 102 GLY ARG ASP TYR ASP PHE SER SER GLY VAL HIS THR LEU
SEQRES 8 B 102 ALA ASP GLY ARG ILE LEU SER GLY THR PRO LYS
SEQRES 1 C 102 GLY SER HIS MET ALA SER GLY ASP ALA THR ASP ILE THR
SEQRES 2 C 102 ILE TYR TYR LYS THR GLY TRP THR HIS PRO HIS ILE HIS
SEQRES 3 C 102 TYR SER LEU ASN GLN GLY ALA TRP THR THR LEU PRO GLY
SEQRES 4 C 102 VAL PRO LEU THR LYS SER GLU TYR GLU GLY TYR VAL LYS
SEQRES 5 C 102 VAL THR ILE GLU ALA GLU GLU GLY SER GLN LEU ARG ALA
SEQRES 6 C 102 ALA PHE ASN ASN GLY SER GLY GLN TRP ASP ASN ASN GLN
SEQRES 7 C 102 GLY ARG ASP TYR ASP PHE SER SER GLY VAL HIS THR LEU
SEQRES 8 C 102 ALA ASP GLY ARG ILE LEU SER GLY THR PRO LYS
SEQRES 1 D 102 GLY SER HIS MET ALA SER GLY ASP ALA THR ASP ILE THR
SEQRES 2 D 102 ILE TYR TYR LYS THR GLY TRP THR HIS PRO HIS ILE HIS
SEQRES 3 D 102 TYR SER LEU ASN GLN GLY ALA TRP THR THR LEU PRO GLY
SEQRES 4 D 102 VAL PRO LEU THR LYS SER GLU TYR GLU GLY TYR VAL LYS
SEQRES 5 D 102 VAL THR ILE GLU ALA GLU GLU GLY SER GLN LEU ARG ALA
SEQRES 6 D 102 ALA PHE ASN ASN GLY SER GLY GLN TRP ASP ASN ASN GLN
SEQRES 7 D 102 GLY ARG ASP TYR ASP PHE SER SER GLY VAL HIS THR LEU
SEQRES 8 D 102 ALA ASP GLY ARG ILE LEU SER GLY THR PRO LYS
HET GLC E 1 12
HET GLC E 2 11
HET GLC E 3 11
HET GLC E 4 11
HET GLC F 1 12
HET GLC F 2 11
HET GLC F 3 11
HET GLC F 4 11
HET GLC G 1 12
HET GLC G 2 11
HET GLC G 3 11
HET GLC H 1 12
HET GLC H 2 11
HET GLC H 3 11
HET GLC H 4 11
HET GLC I 1 12
HET GLC I 2 11
HET GLC I 3 11
HET GLC I 4 11
HET GLC J 1 12
HET GLC J 2 11
HET GLC J 3 11
HET GLC J 4 11
HET GLC K 1 12
HET GLC K 2 11
HET GLC K 3 11
HET GLC K 4 11
HET GLC L 1 12
HET GLC L 2 11
HET GLC L 3 11
HET GLC L 4 11
HET GLC M 1 12
HET GLC M 2 11
HET GLC M 3 11
HET GLC M 4 11
HET SO4 A1112 5
HET SO4 B1110 5
HET SO4 C1110 5
HET SO4 D1114 5
HETNAM GLC ALPHA-D-GLUCOPYRANOSE
HETNAM SO4 SULFATE ION
FORMUL 5 GLC 35(C6 H12 O6)
FORMUL 14 SO4 4(O4 S 2-)
FORMUL 18 HOH *783(H2 O)
SHEET 1 AA 5 THR A 43 LYS A 44 0
SHEET 2 AA 5 TYR A 50 ILE A 55 -1 O LYS A 52 N THR A 43
SHEET 3 AA 5 ILE A 12 LYS A 17 -1 O ILE A 12 N ILE A 55
SHEET 4 AA 5 GLY A 87 ALA A 92 1 O GLY A 87 N THR A 13
SHEET 5 AA 5 ARG A 95 SER A 98 -1 O ARG A 95 N ALA A 92
SHEET 1 AB 4 VAL A 40 PRO A 41 0
SHEET 2 AB 4 HIS A 24 LEU A 29 -1 O ILE A 25 N VAL A 40
SHEET 3 AB 4 GLN A 62 ASN A 68 -1 O ARG A 64 N SER A 28
SHEET 4 AB 4 TYR A 82 SER A 85 -1 O TYR A 82 N ALA A 65
SHEET 1 AC 4 VAL A 40 PRO A 41 0
SHEET 2 AC 4 HIS A 24 LEU A 29 -1 O ILE A 25 N VAL A 40
SHEET 3 AC 4 GLN A 62 ASN A 68 -1 O ARG A 64 N SER A 28
SHEET 4 AC 4 TRP A 74 ASP A 75 -1 O ASP A 75 N PHE A 67
SHEET 1 BA 5 THR B 43 LYS B 44 0
SHEET 2 BA 5 TYR B 50 ILE B 55 -1 O LYS B 52 N THR B 43
SHEET 3 BA 5 ILE B 12 LYS B 17 -1 O ILE B 12 N ILE B 55
SHEET 4 BA 5 GLY B 87 ALA B 92 1 O GLY B 87 N THR B 13
SHEET 5 BA 5 ARG B 95 SER B 98 -1 O ARG B 95 N ALA B 92
SHEET 1 BB 4 VAL B 40 PRO B 41 0
SHEET 2 BB 4 HIS B 24 LEU B 29 -1 O ILE B 25 N VAL B 40
SHEET 3 BB 4 GLN B 62 ASN B 68 -1 O ARG B 64 N SER B 28
SHEET 4 BB 4 TYR B 82 SER B 85 -1 O TYR B 82 N ALA B 65
SHEET 1 BC 4 VAL B 40 PRO B 41 0
SHEET 2 BC 4 HIS B 24 LEU B 29 -1 O ILE B 25 N VAL B 40
SHEET 3 BC 4 GLN B 62 ASN B 68 -1 O ARG B 64 N SER B 28
SHEET 4 BC 4 TRP B 74 ASP B 75 -1 O ASP B 75 N PHE B 67
SHEET 1 CA 5 THR C 43 LYS C 44 0
SHEET 2 CA 5 TYR C 50 ILE C 55 -1 O LYS C 52 N THR C 43
SHEET 3 CA 5 ILE C 12 LYS C 17 -1 O ILE C 12 N ILE C 55
SHEET 4 CA 5 GLY C 87 ALA C 92 1 O GLY C 87 N THR C 13
SHEET 5 CA 5 ARG C 95 SER C 98 -1 O ARG C 95 N ALA C 92
SHEET 1 CB 4 VAL C 40 PRO C 41 0
SHEET 2 CB 4 HIS C 24 LEU C 29 -1 O ILE C 25 N VAL C 40
SHEET 3 CB 4 GLN C 62 ASN C 68 -1 O ARG C 64 N SER C 28
SHEET 4 CB 4 TYR C 82 SER C 85 -1 O TYR C 82 N ALA C 65
SHEET 1 CC 4 VAL C 40 PRO C 41 0
SHEET 2 CC 4 HIS C 24 LEU C 29 -1 O ILE C 25 N VAL C 40
SHEET 3 CC 4 GLN C 62 ASN C 68 -1 O ARG C 64 N SER C 28
SHEET 4 CC 4 TRP C 74 ASP C 75 -1 O ASP C 75 N PHE C 67
SHEET 1 DA 5 THR D 43 LYS D 44 0
SHEET 2 DA 5 TYR D 50 ILE D 55 -1 O LYS D 52 N THR D 43
SHEET 3 DA 5 ILE D 12 LYS D 17 -1 O ILE D 12 N ILE D 55
SHEET 4 DA 5 GLY D 87 ALA D 92 1 O GLY D 87 N THR D 13
SHEET 5 DA 5 ARG D 95 SER D 98 -1 O ARG D 95 N ALA D 92
SHEET 1 DB 7 VAL D 40 PRO D 41 0
SHEET 2 DB 7 HIS D 24 LEU D 29 -1 O ILE D 25 N VAL D 40
SHEET 3 DB 7 GLN D 62 ASN D 68 -1 O ARG D 64 N SER D 28
SHEET 4 DB 7 TRP D 74 ASP D 75 -1 O ASP D 75 N PHE D 67
SHEET 5 DB 7 GLN D 62 ASN D 68 -1 O PHE D 67 N ASP D 75
SHEET 6 DB 7 TYR D 82 SER D 85 -1 O TYR D 82 N ALA D 65
SHEET 7 DB 7 GLN D 62 ASN D 68 -1 O LEU D 63 N PHE D 84
LINK O4 GLC E 1 C1 GLC E 2 1555 1555 1.44
LINK O4 GLC E 2 C1 GLC E 3 1555 1555 1.44
LINK O4 GLC E 3 C1 GLC E 4 1555 1555 1.45
LINK O4 GLC F 1 C1 GLC F 2 1555 1555 1.47
LINK O4 GLC F 2 C1 GLC F 3 1555 1555 1.43
LINK O4 GLC F 3 C1 GLC F 4 1555 1555 1.46
LINK O4 GLC G 1 C1 GLC G 2 1555 1555 1.46
LINK O4 GLC G 2 C1 GLC G 3 1555 1555 1.45
LINK O4 GLC H 1 C1 GLC H 2 1555 1555 1.45
LINK O4 GLC H 2 C1 GLC H 3 1555 1555 1.45
LINK O4 GLC H 3 C1 GLC H 4 1555 1555 1.46
LINK O4 GLC I 1 C1 GLC I 2 1555 1555 1.47
LINK O4 GLC I 2 C1 GLC I 3 1555 1555 1.42
LINK O4 GLC I 3 C1 GLC I 4 1555 1555 1.48
LINK O4 GLC J 1 C1 GLC J 2 1555 1555 1.43
LINK O4 GLC J 2 C1 GLC J 3 1555 1555 1.44
LINK O4 GLC J 3 C1 GLC J 4 1555 1555 1.47
LINK O4 GLC K 1 C1 GLC K 2 1555 1555 1.43
LINK O4 GLC K 2 C1 GLC K 3 1555 1555 1.43
LINK O4 GLC K 3 C1 GLC K 4 1555 1555 1.42
LINK O4 GLC L 1 C1 GLC L 2 1555 1555 1.44
LINK O4 GLC L 2 C1 GLC L 3 1555 1555 1.43
LINK O4 GLC L 3 C1 GLC L 4 1555 1555 1.46
LINK O4 GLC M 1 C1 GLC M 2 1555 1555 1.43
LINK O4 GLC M 2 C1 GLC M 3 1555 1555 1.43
LINK O4 GLC M 3 C1 GLC M 4 1555 1555 1.47
CISPEP 1 LEU A 37 PRO A 38 0 10.49
CISPEP 2 LEU B 37 PRO B 38 0 -0.88
CISPEP 3 LEU C 37 PRO C 38 0 1.61
CISPEP 4 LEU D 37 PRO D 38 0 -0.98
CRYST1 47.533 94.553 64.868 90.00 104.65 90.00 P 1 21 1 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 0.021038 0.000000 0.005500 0.00000
SCALE2 0.000000 0.010576 0.000000 0.00000
SCALE3 0.000000 0.000000 0.015934 0.00000
(ATOM LINES ARE NOT SHOWN.)
END