HEADER HYDROLASE 13-MAR-14 4PUD
TITLE EXTRACELLULR XYLANASE FROM GEOBACILLUS STEAROTHERMOPHILUS: E159Q
TITLE 2 MUTANT, WITH XYLOPENTAOSE IN ACTIVE SITE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ENDO-1,4-BETA-XYLANASE;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: XYLANASE, 1,4-BETA-D-XYLAN XYLANOHYDROLASE;
COMPND 5 EC: 3.2.1.8;
COMPND 6 ENGINEERED: YES;
COMPND 7 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: GEOBACILLUS STEAROTHERMOPHILUS;
SOURCE 3 ORGANISM_TAXID: 1422;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS TIM BARREL, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR R.D.DANN,H.V.SOLOMON,S.LANSKY,A.BEN-DAVID,N.LAVID,R.SALAMA,Y.SHOHAM,
AUTHOR 2 G.SHOHAM
REVDAT 1 18-MAR-15 4PUD 0
JRNL AUTH R.D.DANN,H.V.SOLOMON,S.LANSKY,A.BEN-DAVID,N.LAVID,R.SALAMA,
JRNL AUTH 2 Y.SHOHAM,G.SHOHAM
JRNL TITL EXTRACELLULR XYLANASE FROM GEOBACILLUS STEAROTHERMOPHILUS:
JRNL TITL 2 E159Q MUTANT, WITH XYLOPENTAOSE IN ACTIVE SITE.
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.01 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.7.0029
REMARK 3 AUTHORS : MURSHUDOV,VAGIN,DODSON
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.01
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 50.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.0
REMARK 3 NUMBER OF REFLECTIONS : 36157
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) : 0.148
REMARK 3 R VALUE (WORKING SET) : 0.146
REMARK 3 FREE R VALUE : 0.183
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 1901
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) : 2.01
REMARK 3 BIN RESOLUTION RANGE LOW (A) : NULL
REMARK 3 REFLECTION IN BIN (WORKING SET) : 2546
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 94.54
REMARK 3 BIN R VALUE (WORKING SET) : 0.2140
REMARK 3 BIN FREE R VALUE SET COUNT : 136
REMARK 3 BIN FREE R VALUE : 0.2450
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 3036
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 58
REMARK 3 SOLVENT ATOMS : 354
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 31.83
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.98000
REMARK 3 B22 (A**2) : 1.37000
REMARK 3 B33 (A**2) : -1.25000
REMARK 3 B12 (A**2) : -0.00000
REMARK 3 B13 (A**2) : -0.54000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.121
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.118
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.071
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 2.518
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.974
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.959
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 3282 ; 0.020 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 3073 ; 0.001 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 4472 ; 2.029 ; 1.959
REMARK 3 BOND ANGLES OTHERS (DEGREES): 7098 ; 0.928 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 391 ; 6.551 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 169 ;34.061 ;25.207
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 559 ;15.210 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 14 ;15.574 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 475 ; 0.129 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 3748 ; 0.011 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 768 ; 0.003 ; 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): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
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 : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.20
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS
REMARK 4
REMARK 4 4PUD COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 03-APR-14.
REMARK 100 THE RCSB ID CODE IS RCSB085229.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 10-SEP-13
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.7
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : ROTATING ANODE
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : RIGAKU
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.54
REMARK 200 MONOCHROMATOR : A HOME SOURCE WAS USED
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : RIGAKU RAXIS HTC
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-3000
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 36157
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.010
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.0
REMARK 200 DATA REDUNDANCY : 5.700
REMARK 200 R MERGE (I) : 0.09800
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) : 2.01
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL
REMARK 200 COMPLETENESS FOR SHELL (%) : 94.5
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: REFMAC 5.7.0032
REMARK 200 STARTING MODEL: 1R86
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 63.70
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.39
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 16% PEG 4000, 0.1M MES, 10MM ZINC
REMARK 280 CHLORIDE, PH 6.7, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 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 60.69700
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 30.83200
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 60.69700
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 30.83200
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375 HOH A 515 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A 742 LIES ON A SPECIAL POSITION.
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 LYS A 114 CG CD CE NZ
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 NZ LYS A 182 OE1 GLU A 224 2.13
REMARK 500
REMARK 500 REMARK: NULL
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 CE1 HIS A 378 CL CL A 409 4445 2.13
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 PRO A 104 C - N - CA ANGL. DEV. = -9.4 DEGREES
REMARK 500 LEU A 214 CA - CB - CG ANGL. DEV. = 14.0 DEGREES
REMARK 500 ASP A 377 CB - CG - OD1 ANGL. DEV. = 8.3 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 ASN A 59 -31.28 -136.29
REMARK 500 GLN A 102 74.46 19.95
REMARK 500 ASN A 169 56.61 -94.99
REMARK 500 GLU A 265 45.56 -141.96
REMARK 500 TRP A 316 57.08 -90.14
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 ZN A 417 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 365 OD1
REMARK 620 2 HIS A 11 NE2 120.4
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A 410 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 322 NE2
REMARK 620 2 HOH A 843 O 113.6
REMARK 620 3 GLU A 58 OE1 97.1 109.2
REMARK 620 4 GLU A 58 OE2 120.9 124.0 54.0
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A 413 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 282 OD2
REMARK 620 2 HOH A 844 O 112.6
REMARK 620 3 HOH A 760 O 92.1 89.6
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A 406 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH A 746 O
REMARK 620 2 ASP A 21 OD2 177.3
REMARK 620 3 HOH A 795 O 90.4 91.9
REMARK 620 4 HOH A 745 O 85.3 93.3 90.3
REMARK 620 5 HOH A 772 O 90.0 91.2 91.1 175.2
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A 411 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 297 OD1
REMARK 620 2 ALA A 374 O 97.5
REMARK 620 3 ASP A 377 OD1 150.4 82.2
REMARK 620 4 LYS A 379 O 92.2 167.1 85.2
REMARK 620 5 HOH A 532 O 140.0 88.4 69.6 89.7
REMARK 620 6 HOH A 531 O 73.9 91.9 76.5 82.5 145.7
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A 412 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU A 27 O
REMARK 620 2 ILE A 310 O 96.2
REMARK 620 3 SER A 307 O 100.8 83.1
REMARK 620 4 HOH A 533 O 89.2 107.0 165.0
REMARK 620 5 HOH A 624 O 169.1 84.7 90.1 80.1
REMARK 620 6 HOH A 588 O 80.6 166.6 84.7 86.0 100.9
REMARK 620 N 1 2 3 4 5
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 406
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 407
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 408
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 409
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 410
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 411
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 412
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 413
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 414
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 415
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 416
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 417
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR CHAIN A OF POLYSACCHARIDE
REMARK 800 RESIDUES 401 TO 405
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1R86 RELATED DB: PDB
REMARK 900 RELATED ID: 1HIZ RELATED DB: PDB
REMARK 900 RELATED ID: 3MMD RELATED DB: PDB
REMARK 900 RELATED ID: 1R85 RELATED DB: PDB
REMARK 900 RELATED ID: 1R87 RELATED DB: PDB
REMARK 900 RELATED ID: 4PRW RELATED DB: PDB
REMARK 900 RELATED ID: 4PUE RELATED DB: PDB
DBREF 4PUD A 9 379 UNP P40943 XYN1_GEOSE 37 407
SEQADV 4PUD GLN A 159 UNP P40943 GLU 187 ENGINEERED MUTATION
SEQRES 1 A 371 LYS PRO HIS ILE SER ALA LEU ASN ALA PRO GLN LEU ASP
SEQRES 2 A 371 GLN ARG TYR LYS ASN GLU PHE THR ILE GLY ALA ALA VAL
SEQRES 3 A 371 GLU PRO TYR GLN LEU GLN ASN GLU LYS ASP VAL GLN MET
SEQRES 4 A 371 LEU LYS ARG HIS PHE ASN SER ILE VAL ALA GLU ASN VAL
SEQRES 5 A 371 MET LYS PRO ILE SER ILE GLN PRO GLU GLU GLY LYS PHE
SEQRES 6 A 371 ASN PHE GLU GLN ALA ASP ARG ILE VAL LYS PHE ALA LYS
SEQRES 7 A 371 ALA ASN GLY MET ASP ILE ARG PHE HIS THR LEU VAL TRP
SEQRES 8 A 371 HIS SER GLN VAL PRO GLN TRP PHE PHE LEU ASP LYS GLU
SEQRES 9 A 371 GLY LYS PRO MET VAL ASN GLU THR ASP PRO VAL LYS ARG
SEQRES 10 A 371 GLU GLN ASN LYS GLN LEU LEU LEU LYS ARG LEU GLU THR
SEQRES 11 A 371 HIS ILE LYS THR ILE VAL GLU ARG TYR LYS ASP ASP ILE
SEQRES 12 A 371 LYS TYR TRP ASP VAL VAL ASN GLN VAL VAL GLY ASP ASP
SEQRES 13 A 371 GLY LYS LEU ARG ASN SER PRO TRP TYR GLN ILE ALA GLY
SEQRES 14 A 371 ILE ASP TYR ILE LYS VAL ALA PHE GLN ALA ALA ARG LYS
SEQRES 15 A 371 TYR GLY GLY ASP ASN ILE LYS LEU TYR MET ASN ASP TYR
SEQRES 16 A 371 ASN THR GLU VAL GLU PRO LYS ARG THR ALA LEU TYR ASN
SEQRES 17 A 371 LEU VAL LYS GLN LEU LYS GLU GLU GLY VAL PRO ILE ASP
SEQRES 18 A 371 GLY ILE GLY HIS GLN SER HIS ILE GLN ILE GLY TRP PRO
SEQRES 19 A 371 SER GLU ALA GLU ILE GLU LYS THR ILE ASN MET PHE ALA
SEQRES 20 A 371 ALA LEU GLY LEU ASP ASN GLN ILE THR GLU LEU ASP VAL
SEQRES 21 A 371 SER MET TYR GLY TRP PRO PRO ARG ALA TYR PRO THR TYR
SEQRES 22 A 371 ASP ALA ILE PRO LYS GLN LYS PHE LEU ASP GLN ALA ALA
SEQRES 23 A 371 ARG TYR ASP ARG LEU PHE LYS LEU TYR GLU LYS LEU SER
SEQRES 24 A 371 ASP LYS ILE SER ASN VAL THR PHE TRP GLY ILE ALA ASP
SEQRES 25 A 371 ASN HIS THR TRP LEU ASP SER ARG ALA ASP VAL TYR TYR
SEQRES 26 A 371 ASP ALA ASN GLY ASN VAL VAL VAL ASP PRO ASN ALA PRO
SEQRES 27 A 371 TYR ALA LYS VAL GLU LYS GLY LYS GLY LYS ASP ALA PRO
SEQRES 28 A 371 PHE VAL PHE GLY PRO ASP TYR LYS VAL LYS PRO ALA TYR
SEQRES 29 A 371 TRP ALA ILE ILE ASP HIS LYS
HET XYP A 401 9
HET XYP A 402 9
HET XYP A 403 9
HET XYP A 404 9
HET XYP A 405 10
HET ZN A 406 1
HET ZN A 407 1
HET CL A 408 1
HET CL A 409 1
HET ZN A 410 1
HET ZN A 411 1
HET ZN A 412 1
HET ZN A 413 1
HET CL A 414 1
HET ZN A 415 1
HET ZN A 416 1
HET ZN A 417 1
HETNAM XYP BETA-D-XYLOPYRANOSE
HETNAM ZN ZINC ION
HETNAM CL CHLORIDE ION
FORMUL 2 XYP 5(C5 H10 O5)
FORMUL 3 ZN 9(ZN 2+)
FORMUL 5 CL 3(CL 1-)
FORMUL 15 HOH *354(H2 O)
HELIX 1 1 SER A 13 ALA A 17 5 5
HELIX 2 2 GLN A 19 TYR A 24 1 6
HELIX 3 3 GLU A 35 GLN A 40 5 6
HELIX 4 4 ASN A 41 PHE A 52 1 12
HELIX 5 5 LYS A 62 GLN A 67 1 6
HELIX 6 6 PHE A 75 ASN A 88 1 14
HELIX 7 7 PRO A 104 LEU A 109 5 6
HELIX 8 8 PRO A 115 GLU A 119 5 5
HELIX 9 9 ASP A 121 LYS A 148 1 28
HELIX 10 10 SER A 170 GLY A 177 1 8
HELIX 11 11 ILE A 178 GLY A 193 1 16
HELIX 12 12 PRO A 209 GLU A 224 1 16
HELIX 13 13 SER A 243 LEU A 257 1 15
HELIX 14 14 THR A 280 ILE A 284 5 5
HELIX 15 15 PRO A 285 LEU A 306 1 22
HELIX 16 16 THR A 323 ALA A 329 5 7
HELIX 17 17 LYS A 369 ASP A 377 1 9
SHEET 1 A10 HIS A 236 GLN A 238 0
SHEET 2 A10 ASP A 260 SER A 269 1 O SER A 269 N ILE A 237
SHEET 3 A10 ILE A 310 PHE A 315 1 O THR A 314 N ILE A 263
SHEET 4 A10 THR A 29 VAL A 34 1 N GLY A 31 O PHE A 315
SHEET 5 A10 SER A 54 ALA A 57 1 O VAL A 56 N VAL A 34
SHEET 6 A10 ASP A 91 VAL A 98 1 O ARG A 93 N ILE A 55
SHEET 7 A10 TYR A 153 ASN A 158 1 O ASP A 155 N PHE A 94
SHEET 8 A10 LYS A 197 ASP A 202 1 O TYR A 199 N TRP A 154
SHEET 9 A10 GLY A 230 HIS A 233 1 O GLY A 232 N MET A 200
SHEET 10 A10 ASP A 260 SER A 269 1 O GLN A 262 N HIS A 233
SHEET 1 B 3 VAL A 339 VAL A 340 0
SHEET 2 B 3 VAL A 331 TYR A 333 -1 N TYR A 332 O VAL A 340
SHEET 3 B 3 LYS A 349 GLU A 351 -1 O GLU A 351 N VAL A 331
LINK C1B XYP A 401 O4B XYP A 402 1555 1555 1.40
LINK C1B XYP A 404 O4B XYP A 405 1555 1555 1.43
LINK C1B XYP A 403 O4B XYP A 404 1555 1555 1.44
LINK C1B XYP A 402 O4B XYP A 403 1555 1555 1.47
LINK OD1 ASP A 365 ZN ZN A 417 1555 1555 1.89
LINK NE2 HIS A 322 ZN ZN A 410 1555 1555 1.96
LINK ZN ZN A 410 O HOH A 843 1555 1555 1.99
LINK OD2 ASP A 282 ZN ZN A 413 1555 1555 1.99
LINK NE2 HIS A 11 ZN ZN A 417 1555 1555 2.02
LINK ZN ZN A 406 O HOH A 746 1555 1555 2.03
LINK OD2 ASP A 21 ZN ZN A 406 1555 1555 2.05
LINK ZN ZN A 406 O HOH A 795 1555 1555 2.11
LINK ZN ZN A 406 O HOH A 745 1555 1555 2.12
LINK ZN ZN A 406 O HOH A 772 1555 1555 2.14
LINK OD1 ASP A 282 ZN ZN A 416 1555 1555 2.21
LINK OD1 ASP A 297 ZN ZN A 411 1555 1555 2.21
LINK ZN ZN A 413 O HOH A 844 1555 1555 2.21
LINK OE1 GLU A 58 ZN ZN A 410 1555 1555 2.25
LINK O GLU A 27 ZN ZN A 412 1555 1555 2.29
LINK O ALA A 374 ZN ZN A 411 1555 1555 2.30
LINK O ILE A 310 ZN ZN A 412 1555 1555 2.30
LINK O SER A 307 ZN ZN A 412 1555 1555 2.31
LINK OD1 ASP A 377 ZN ZN A 411 1555 1555 2.32
LINK O LYS A 379 ZN ZN A 411 1555 1555 2.34
LINK ZN ZN A 411 O HOH A 532 1555 1555 2.36
LINK ZN ZN A 411 O HOH A 531 1555 1555 2.38
LINK ZN ZN A 412 O HOH A 533 1555 1555 2.38
LINK ZN ZN A 413 O HOH A 760 1555 1555 2.45
LINK OE2 GLU A 58 ZN ZN A 410 1555 1555 2.52
LINK ZN ZN A 412 O HOH A 624 1555 1555 2.53
LINK ZN ZN A 412 O HOH A 588 1555 1555 2.65
CISPEP 1 HIS A 95 THR A 96 0 0.39
CISPEP 2 GLU A 208 PRO A 209 0 2.02
CISPEP 3 TRP A 241 PRO A 242 0 -3.66
CISPEP 4 TRP A 273 PRO A 274 0 -6.82
SITE 1 AC1 6 ASP A 21 ZN A 415 HOH A 745 HOH A 746
SITE 2 AC1 6 HOH A 772 HOH A 795
SITE 1 AC2 5 HIS A 11 ASN A 26 GLU A 27 ASP A 365
SITE 2 AC2 5 ZN A 417
SITE 1 AC3 6 GLU A 58 HIS A 322 TRP A 324 XYP A 401
SITE 2 AC3 6 ZN A 410 HOH A 843
SITE 1 AC4 5 ASP A 282 HIS A 378 ZN A 416 HOH A 719
SITE 2 AC4 5 HOH A 845
SITE 1 AC5 5 GLU A 58 HIS A 322 XYP A 401 CL A 408
SITE 2 AC5 5 HOH A 843
SITE 1 AC6 7 ASP A 297 ALA A 374 ASP A 377 LYS A 379
SITE 2 AC6 7 CL A 414 HOH A 531 HOH A 532
SITE 1 AC7 6 GLU A 27 SER A 307 ILE A 310 HOH A 533
SITE 2 AC7 6 HOH A 588 HOH A 624
SITE 1 AC8 5 ASP A 282 HIS A 378 HOH A 577 HOH A 760
SITE 2 AC8 5 HOH A 844
SITE 1 AC9 7 ASP A 297 LYS A 301 ALA A 374 LYS A 379
SITE 2 AC9 7 ZN A 411 HOH A 532 HOH A 583
SITE 1 BC1 7 ASP A 21 LYS A 49 PHE A 52 ZN A 406
SITE 2 BC1 7 HOH A 745 HOH A 746 HOH A 772
SITE 1 BC2 4 ARG A 23 ASP A 282 CL A 409 HOH A 824
SITE 1 BC3 4 HIS A 11 GLU A 27 ASP A 365 ZN A 407
SITE 1 BC4 25 GLU A 58 ASN A 59 LYS A 62 HIS A 95
SITE 2 BC4 25 GLN A 102 ASN A 158 GLN A 159 ASN A 204
SITE 3 BC4 25 GLN A 234 HIS A 236 GLN A 238 TRP A 241
SITE 4 BC4 25 GLU A 265 TRP A 273 TRP A 316 TRP A 324
SITE 5 BC4 25 ARG A 328 CL A 408 ZN A 410 HOH A 550
SITE 6 BC4 25 HOH A 574 HOH A 697 HOH A 737 HOH A 793
SITE 7 BC4 25 HOH A 838
CRYST1 121.394 61.664 89.321 90.00 119.37 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 0.008238 0.000000 0.004637 0.00000
SCALE2 0.000000 0.016217 0.000000 0.00000
SCALE3 0.000000 0.000000 0.012847 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
