HEADER HYDROLASE 05-MAY-09 2WHL
TITLE UNDERSTANDING HOW DIVERSE MANNANASES RECOGNISE HETEROGENEOUS
TITLE 2 SUBSTRATES
CAVEAT 2WHL ASP A 231 HAS WRONG CHIRALITY AT ATOM CA THR A 299 HAS WRONG
CAVEAT 2 2WHL CHIRALITY AT ATOM CA
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: BETA-MANNANASE;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: RESIDUES 35-330;
COMPND 5 SYNONYM: BAMAN5;
COMPND 6 EC: 3.2.1.78;
COMPND 7 ENGINEERED: YES;
COMPND 8 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: BACILLUS AGARADHAERENS;
SOURCE 3 ORGANISM_TAXID: 76935;
SOURCE 4 STRAIN: NCIMB 40482;
SOURCE 5 EXPRESSION_SYSTEM: BACILLUS SUBTILIS;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 1423;
SOURCE 7 EXPRESSION_SYSTEM_VECTOR: PMOL944
KEYWDS MANNANASE, GLYCOSIDE HYDROLASE, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR L.E.TAILFORD,V.M.A.DUCROS,J.E.FLINT,S.M.ROBERTS,C.MORLAND,D.L.ZECHEL,
AUTHOR 2 N.SMITH,M.E.BJORNVAD,T.V.BORCHERT,K.S.WILSON,G.J.DAVIES,H.J.GILBERT
REVDAT 5 13-DEC-23 2WHL 1 REMARK HETSYN
REVDAT 4 29-JUL-20 2WHL 1 CAVEAT COMPND REMARK HETNAM
REVDAT 4 2 1 LINK SITE ATOM
REVDAT 3 28-NOV-12 2WHL 1 REMARK VERSN SEQADV
REVDAT 2 06-JUL-11 2WHL 1 JRNL REMARK FORMUL
REVDAT 1 26-MAY-09 2WHL 0
JRNL AUTH L.E.TAILFORD,V.M.A.DUCROS,J.E.FLINT,S.M.ROBERTS,C.MORLAND,
JRNL AUTH 2 D.L.ZECHEL,N.SMITH,M.E.BJORNVAD,T.V.BORCHERT,K.S.WILSON,
JRNL AUTH 3 G.J.DAVIES,H.J.GILBERT
JRNL TITL UNDERSTANDING HOW DIVERSE -MANNANASES RECOGNISE
JRNL TITL 2 HETEROGENEOUS SUBSTRATES.
JRNL REF BIOCHEMISTRY V. 48 7009 2009
JRNL REFN ISSN 0006-2960
JRNL PMID 19441796
JRNL DOI 10.1021/BI900515D
REMARK 2
REMARK 2 RESOLUTION. 1.40 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.4.0062
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) : 1.40
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 50.64
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 94.2
REMARK 3 NUMBER OF REFLECTIONS : 55790
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) : 0.152
REMARK 3 R VALUE (WORKING SET) : 0.150
REMARK 3 FREE R VALUE : 0.188
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 2980
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) : 1.40
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.43
REMARK 3 REFLECTION IN BIN (WORKING SET) : 2503
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 58.35
REMARK 3 BIN R VALUE (WORKING SET) : 0.2610
REMARK 3 BIN FREE R VALUE SET COUNT : 146
REMARK 3 BIN FREE R VALUE : 0.2890
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2312
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 38
REMARK 3 SOLVENT ATOMS : 273
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 16.22
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 4.52000
REMARK 3 B22 (A**2) : -2.32000
REMARK 3 B33 (A**2) : -2.20000
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): 0.063
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.060
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.056
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 3.442
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.976
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.964
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 2474 ; 0.021 ; 0.021
REMARK 3 BOND LENGTHS OTHERS (A): 1575 ; 0.002 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 3384 ; 1.960 ; 1.922
REMARK 3 BOND ANGLES OTHERS (DEGREES): 3826 ; 1.618 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 306 ; 6.722 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 130 ;33.176 ;24.923
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 377 ;11.340 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 13 ;10.432 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 368 ; 0.304 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 2824 ; 0.010 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 508 ; 0.001 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 1483 ; 2.167 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 620 ; 1.261 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 2385 ; 2.939 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 991 ; 4.289 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 996 ; 5.783 ; 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): 4049 ; 2.360 ; 3.000
REMARK 3 SPHERICITY; FREE ATOMS (A**2): 273 ;12.157 ; 3.000
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): 3984 ; 7.546 ; 3.000
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 : 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 2WHL COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 05-MAY-09.
REMARK 100 THE DEPOSITION ID IS D_1290039705.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : NULL
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : NULL
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : ID14-4
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9392
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 62370
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.400
REMARK 200 RESOLUTION RANGE LOW (A) : 19.730
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 95.0
REMARK 200 DATA REDUNDANCY : 3.700
REMARK 200 R MERGE (I) : 0.05000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 27.0000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.40
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.45
REMARK 200 COMPLETENESS FOR SHELL (%) : 68.0
REMARK 200 DATA REDUNDANCY IN SHELL : 2.30
REMARK 200 R MERGE FOR SHELL (I) : 0.20000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 3.500
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: AMORE
REMARK 200 STARTING MODEL: PDB ENTRY 2WHJ
REMARK 200
REMARK 200 REMARK: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 46.09
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.28
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.6M NA/K PO4, 0.1M HEPES PH 7.5
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 29.12750
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 41.78850
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 31.84500
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 41.78850
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 29.12750
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 31.84500
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
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 400
REMARK 400 COMPOUND
REMARK 400 ENGINEERED RESIDUE IN CHAIN A, TYR 37 TO SER
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 2242 O HOH A 2248 2.14
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 RES CSSEQI ATM2 DEVIATION
REMARK 500 ALA A 83 CA ALA A 83 CB 0.129
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 34 CB - CG - OD1 ANGL. DEV. = 5.7 DEGREES
REMARK 500 ARG A 52 NE - CZ - NH1 ANGL. DEV. = 3.0 DEGREES
REMARK 500 ALA A 83 N - CA - CB ANGL. DEV. = 9.1 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 TYR A 32 57.27 -144.61
REMARK 500 TYR A 129 84.48 74.64
REMARK 500 ALA A 161 153.79 -45.14
REMARK 500 ASN A 186 58.12 -144.41
REMARK 500 TYR A 194 -139.05 -119.73
REMARK 500 HIS A 227 -76.75 -116.27
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 A2039 DISTANCE = 5.84 ANGSTROMS
REMARK 615
REMARK 615 ZERO OCCUPANCY ATOM
REMARK 615 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO
REMARK 615 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS
REMARK 615 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 615 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 615 M RES C SSEQI
REMARK 615 MAN B 1
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 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2WHM RELATED DB: PDB
REMARK 900 CELLVIBRIO JAPONICUS MAN26A E121A AND E320G DOUBLE MUTANT IN
REMARK 900 COMPLEX WITH MANNOBIOSE
REMARK 900 RELATED ID: 2WHJ RELATED DB: PDB
REMARK 900 UNDERSTANDING HOW DIVERSE MANNANASES RECOGNISE HETEROGENEOUS
REMARK 900 SUBSTRATES
REMARK 900 RELATED ID: 2WHK RELATED DB: PDB
REMARK 900 STRUCTURE OF BACILLUS SUBTILIS MANNANASE MAN26
DBREF 2WHL A 4 299 UNP Q5YEX6 Q5YEX6_9BACI 35 330
SEQADV 2WHL SER A 6 UNP Q5YEX6 TYR 37 ENGINEERED MUTATION
SEQADV 2WHL ARG A 23 UNP Q5YEX6 LYS 54 CONFLICT
SEQADV 2WHL ILE A 69 UNP Q5YEX6 VAL 100 CONFLICT
SEQADV 2WHL ASN A 100 UNP Q5YEX6 ASP 131 CONFLICT
SEQADV 2WHL SER A 135 UNP Q5YEX6 ALA 166 CONFLICT
SEQADV 2WHL MET A 188 UNP Q5YEX6 ILE 219 CONFLICT
SEQADV 2WHL A UNP Q5YEX6 GLY 261 DELETION
SEQADV 2WHL A UNP Q5YEX6 ASP 262 DELETION
SEQADV 2WHL THR A 258 UNP Q5YEX6 ALA 289 CONFLICT
SEQADV 2WHL SER A 259 UNP Q5YEX6 GLU 290 CONFLICT
SEQADV 2WHL GLN A 272 UNP Q5YEX6 ASN 303 CONFLICT
SEQADV 2WHL ASP A 286 UNP Q5YEX6 ASN 317 CONFLICT
SEQRES 1 A 294 GLY PHE SER VAL ASP GLY ASN THR LEU TYR ASP ALA ASN
SEQRES 2 A 294 GLY GLN PRO PHE VAL MET ARG GLY ILE ASN HIS GLY HIS
SEQRES 3 A 294 ALA TRP TYR LYS ASP THR ALA SER THR ALA ILE PRO ALA
SEQRES 4 A 294 ILE ALA GLU GLN GLY ALA ASN THR ILE ARG ILE VAL LEU
SEQRES 5 A 294 SER ASP GLY GLY GLN TRP GLU LYS ASP ASP ILE ASP THR
SEQRES 6 A 294 ILE ARG GLU VAL ILE GLU LEU ALA GLU GLN ASN LYS MET
SEQRES 7 A 294 VAL ALA VAL VAL GLU VAL HIS ASP ALA THR GLY ARG ASP
SEQRES 8 A 294 SER ARG SER ASP LEU ASN ARG ALA VAL ASP TYR TRP ILE
SEQRES 9 A 294 GLU MET LYS ASP ALA LEU ILE GLY LYS GLU ASP THR VAL
SEQRES 10 A 294 ILE ILE ASN ILE ALA ASN GLU TRP TYR GLY SER TRP ASP
SEQRES 11 A 294 GLY SER ALA TRP ALA ASP GLY TYR ILE ASP VAL ILE PRO
SEQRES 12 A 294 LYS LEU ARG ASP ALA GLY LEU THR HIS THR LEU MET VAL
SEQRES 13 A 294 ASP ALA ALA GLY TRP GLY GLN TYR PRO GLN SER ILE HIS
SEQRES 14 A 294 ASP TYR GLY GLN ASP VAL PHE ASN ALA ASP PRO LEU LYS
SEQRES 15 A 294 ASN THR MET PHE SER ILE HIS MET TYR GLU TYR ALA GLY
SEQRES 16 A 294 GLY ASP ALA ASN THR VAL ARG SER ASN ILE ASP ARG VAL
SEQRES 17 A 294 ILE ASP GLN ASP LEU ALA LEU VAL ILE GLY GLU PHE GLY
SEQRES 18 A 294 HIS ARG HIS THR ASP VAL ASP GLU ASP THR ILE LEU SER
SEQRES 19 A 294 TYR SER GLU GLU THR GLY THR GLY TRP LEU ALA TRP SER
SEQRES 20 A 294 TRP LYS GLY ASN SER THR SER TRP ASP TYR LEU ASP LEU
SEQRES 21 A 294 SER GLU ASP TRP ALA GLY GLN HIS LEU THR ASP TRP GLY
SEQRES 22 A 294 ASN ARG ILE VAL HIS GLY ALA ASP GLY LEU GLN GLU THR
SEQRES 23 A 294 SER LYS PRO SER THR VAL PHE THR
HET MAN B 1 13
HET BMA B 2 11
HET BMA B 3 11
HET ACT A1300 4
HETNAM MAN ALPHA-D-MANNOPYRANOSE
HETNAM BMA BETA-D-MANNOPYRANOSE
HETNAM ACT ACETATE ION
HETSYN MAN ALPHA-D-MANNOSE; D-MANNOSE; MANNOSE
HETSYN BMA BETA-D-MANNOSE; D-MANNOSE; MANNOSE
FORMUL 2 MAN C6 H12 O6
FORMUL 2 BMA 2(C6 H12 O6)
FORMUL 3 ACT C2 H3 O2 1-
FORMUL 4 HOH *273(H2 O)
HELIX 1 1 GLY A 28 TYR A 32 5 5
HELIX 2 2 TYR A 32 ASP A 34 5 3
HELIX 3 3 THR A 35 GLN A 46 1 12
HELIX 4 4 ASP A 65 GLN A 78 1 14
HELIX 5 5 SER A 95 MET A 109 1 15
HELIX 6 6 MET A 109 ILE A 114 1 6
HELIX 7 7 ASP A 133 ALA A 151 1 19
HELIX 8 8 PRO A 168 ALA A 181 1 14
HELIX 9 9 ASP A 200 ASP A 213 1 14
HELIX 10 10 ASP A 233 GLY A 245 1 13
HELIX 11 11 SER A 257 ASP A 264 5 8
HELIX 12 12 THR A 275 GLY A 284 1 10
HELIX 13 13 GLY A 287 SER A 292 1 6
HELIX 14 14 SER A 295 THR A 299 5 5
SHEET 1 AA 2 SER A 6 ASP A 8 0
SHEET 2 AA 2 THR A 11 TYR A 13 -1 O THR A 11 N ASP A 8
SHEET 1 AB 9 ARG A 23 HIS A 27 0
SHEET 2 AB 9 GLY A 247 ALA A 250 1 O TRP A 248 N GLY A 24
SHEET 3 AB 9 LEU A 218 PHE A 223 1 O LEU A 218 N GLY A 247
SHEET 4 AB 9 THR A 187 MET A 193 1 O PHE A 189 N VAL A 219
SHEET 5 AB 9 LEU A 157 ASP A 160 1 O LEU A 157 N MET A 188
SHEET 6 AB 9 VAL A 120 ASN A 123 1 O ILE A 122 N MET A 158
SHEET 7 AB 9 VAL A 82 VAL A 87 1 O ALA A 83 N ILE A 121
SHEET 8 AB 9 THR A 50 LEU A 55 1 O ILE A 51 N VAL A 84
SHEET 9 AB 9 ARG A 23 HIS A 27 1 O ILE A 25 N ARG A 52
LINK O4 MAN B 1 C1 BMA B 2 1555 1555 1.43
LINK O4 BMA B 2 C1 BMA B 3 1555 1555 1.45
CISPEP 1 TRP A 251 SER A 252 0 -11.95
CRYST1 58.255 63.690 83.577 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 0.017166 0.000000 0.000000 0.00000
SCALE2 0.000000 0.015701 0.000000 0.00000
SCALE3 0.000000 0.000000 0.011965 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
