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HEADER HYDROLASE 15-AUG-01 1GKL
TITLE S954A MUTANT OF THE FERULOYL ESTERASE MODULE FROM
TITLE 2 CLOSTRIDIUM THERMOCELLUM COMPLEXED WITH FERULIC ACID
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ENDO-1,4-BETA-XYLANASE Y;
COMPND 3 SYNONYM: CBM22-2, XYLANASE Y, XYLY,
COMPND 4 1,4-BETA-D-XYLAN XYLANOHYDROLASE Y;
COMPND 5 CHAIN: A;
COMPND 6 FRAGMENT: FERULOYL ESTERASE DOMAIN;
COMPND 7 EC: 3.2.1.8;
COMPND 8 ENGINEERED: YES;
COMPND 9 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: CLOSTRIDIUM THERMOCELLUM;
SOURCE 3 STRAIN: YS;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 5 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 6 EXPRESSION_SYSTEM_PLASMID: PET-21A
KEYWDS ESTERASE FAMILY 1, FERULIC ACID, INACTIVE MUTANT, X-RAY
KEYWDS 2 CRYSTALLOGRAPHY
EXPDTA X-RAY DIFFRACTION
AUTHOR J.A.M.PRATES,N.TARBOURIECH,S.J.CHARNOCK,C.M.G.A.FONTES,
AUTHOR 2 L.M.A.FERREIRA,G.J.DAVIES
REVDAT 1 13-DEC-01 1GKL 0
JRNL AUTH J.A.M.PRATES,N.TARBOURIECH,S.J.CHARNOCK,
JRNL AUTH 2 C.M.G.A.FONTES,L.M.A.FERREIRA,G.J.DAVIES
JRNL TITL THE STRUCTURE OF THE FERULOYL ESTERASE MODULE OF
JRNL TITL 2 XYLANASE 10B FROM CLOSTRIDIUM THERMOCELLUM
JRNL TITL 3 PROVIDES INSIGHTS INTO SUBSTRATE RECOGNITION
JRNL REF STRUCTURE (LONDON) V. 9 1183 2001
JRNL REFN ASTM STRUE6 UK ISSN 0969-2126
REMARK 2
REMARK 2 RESOLUTION. 1.4 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.0
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) : 1.40
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 19.92
REMARK 3 DATA CUTOFF (SIGMA(F)) : NONE
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.57
REMARK 3 NUMBER OF REFLECTIONS : 148644
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) : 0.14376
REMARK 3 R VALUE (WORKING SET) : 0.14290
REMARK 3 FREE R VALUE : 0.16029
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.0
REMARK 3 FREE R VALUE TEST SET COUNT : 7782
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH : 1.400
REMARK 3 BIN RESOLUTION RANGE LOW : 1.436
REMARK 3 REFLECTION IN BIN (WORKING SET) : 10387
REMARK 3 BIN R VALUE (WORKING SET) : 0.163
REMARK 3 BIN FREE R VALUE SET COUNT : 564
REMARK 3 BIN FREE R VALUE : 0.191
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 4737
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 72
REMARK 3 SOLVENT ATOMS : 751
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 10.002
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.00
REMARK 3 B22 (A**2) : 0.00
REMARK 3 B33 (A**2) : 0.00
REMARK 3 B12 (A**2) : 0.00
REMARK 3 B13 (A**2) : 0.00
REMARK 3 B23 (A**2) : 0.00
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.048
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.044
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.019
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 0.904
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.969
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.962
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED (A): 4965 ; 0.010 ; 0.021
REMARK 3 BOND LENGTHS OTHERS (A): 4092 ; 0.006 ; 0.020
REMARK 3 BOND ANGLES OTHERS (DEGREES): 6800 ; 1.418 ; 1.923
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 9603 ; 3.692 ; 3.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 600 ; 4.846 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 782 ;15.530 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 681 ; 0.106 ; 0.200
REMARK 3 GENERAL PLANES REFINED (A): 5665 ; 0.007 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 1117 ; 0.006 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED (A): 1228 ; 0.613 ; 0.300
REMARK 3 NON-BONDED CONTACTS OTHERS (A): 4433 ; 0.334 ; 0.300
REMARK 3 NON-BONDED TORSION OTHERS (A): 35 ; 0.620 ; 0.500
REMARK 3 H-BOND (X...Y) REFINED (A): 595 ; 0.214 ; 0.500
REMARK 3 H-BOND (X...Y) OTHERS (A): 1 ; 0.002 ; 0.
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): 9 ; 0.329 ; 0.
REMARK 3 SYMMETRY VDW REFINED (A): 16 ; 0.255 ; 0.300
REMARK 3 SYMMETRY VDW OTHERS (A): 30 ; 0.221 ; 0.300
REMARK 3 SYMMETRY H-BOND REFINED (A): 34 ; 0.218 ; 0.500
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED (A**2): 2891 ; 0.847 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE REFINED (A**2): 4718 ; 1.352 ; 2.000
REMARK 3 SIDE-CHAIN BOND REFINED (A**2): 2074 ; 1.728 ; 3.000
REMARK 3 SIDE-CHAIN ANGLE REFINED (A**2): 2079 ; 2.655 ; 4.500
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): 4965 ; 1.183 ; 2.000
REMARK 3 SPHERICITY; FREE ATOMS (A**2): 763 ; 1.673 ; 2.000
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): 4797 ; 1.020 ; 2.000
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF 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:
REMARK 3 HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS
REMARK 4
REMARK 4 1GKL COMPLIES WITH FORMAT V. 2.3, 09-JULY-1998
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY EBI ON 15-AUG-2001.
REMARK 100 THE EBI ID CODE IS EBI-8241.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 15-JUN-2001
REMARK 200 TEMPERATURE (KELVIN) : 120
REMARK 200 PH : 7.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SRS BEAMLINE PX14.2
REMARK 200 BEAMLINE : PX14.2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.978
REMARK 200 MONOCHROMATOR : SILICON (111)
REMARK 200 OPTICS : MIRROR
REMARK 200
REMARK 200 DETECTOR TYPE : CCD Q4
REMARK 200 DETECTOR MANUFACTURER : ADSC
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 148644
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.40
REMARK 200 RESOLUTION RANGE LOW (A) : 20.0
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NONE
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.6
REMARK 200 DATA REDUNDANCY : 5.2
REMARK 200 R MERGE (I) : 0.048
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 33.5
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) : 1.42
REMARK 200 COMPLETENESS FOR SHELL (%) : 94.5
REMARK 200 DATA REDUNDANCY IN SHELL : 2.8
REMARK 200 R MERGE FOR SHELL (I) : 0.136
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 6.6
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: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 58
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.95
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: HEPES PH 7.5 100 MM,
REMARK 280 NA ACETATE 1M, CD ACETATE 50 MM, GLYCEROL 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 1/2-X,-Y,1/2+Z
REMARK 290 3555 -X,1/2+Y,1/2-Z
REMARK 290 4555 1/2+X,1/2-Y,-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 32.55050
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 56.48200
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 54.11650
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 56.48200
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 32.55050
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 54.11650
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
REMARK 300 THIS ENTRY CONTAINS THE CRYSTALLOGRAPHIC ASYMMETRIC UNIT
REMARK 300 WHICH CONSISTS OF 2 CHAIN(S). SEE REMARK 350 FOR
REMARK 300 INFORMATION ON GENERATING THE BIOLOGICAL MOLECULE(S).
REMARK 300
REMARK 300 QUATERNARY STRUCTURE FOR THIS ENTRY: MONOMERIC
REMARK 350
REMARK 350 GENERATING THE BIOMOLECULE
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 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 350 BIOMOLECULE: 2
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 CHAIN A, B ENGINEERED MUTATION SER954ALA
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 MET A 789
REMARK 465 ALA A 790
REMARK 465 SER A 791
REMARK 465 ASP A 792
REMARK 465 LYS A 793
REMARK 465 PHE A 794
REMARK 465 PRO A 795
REMARK 465 VAL A 796
REMARK 465 ALA A 797
REMARK 465 GLU A 798
REMARK 465 ASN A 799
REMARK 465 PRO A 800
REMARK 465 SER A 801
REMARK 465 SER A 802
REMARK 465 MET B 789
REMARK 465 ALA B 790
REMARK 465 SER B 791
REMARK 465 ASP B 792
REMARK 465 LYS B 793
REMARK 465 PHE B 794
REMARK 465 PRO B 795
REMARK 465 VAL B 796
REMARK 465 ALA B 797
REMARK 465 GLU B 798
REMARK 465 ASN B 799
REMARK 465 PRO B 800
REMARK 465 SER B 801
REMARK 465 SER B 802
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
REMARK 500 OH TYR A 819 OE2 GLU A 892 1.95
REMARK 500 ND2B ASN A 854 O HOH Z 108 1.88
REMARK 500 OH TYR B 819 OE2 GLU B 892 1.95
REMARK 500 NH2A ARG B 1000 O A HOH Y 259 1.89
REMARK 500 CG1B ILE B 1019 O HOH Y 276 2.09
REMARK 500 O HOH Y 58 O HOH Y 190 2.16
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 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500
REMARK 500 ALA A 954 66.81 -117.78
REMARK 500 ALA B 954 65.69 -117.29
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES ARE GIVEN CHAIN IDENTIFIERS TO
REMARK 525 INDICATE THE PROTEIN CHAIN TO WHICH THEY ARE MOST CLOSELY
REMARK 525 ASSOCIATED WITH:
REMARK 525 PROTEIN CHAIN SOLVENT CHAIN
REMARK 525 A Z
REMARK 525 B Y
REMARK 600
REMARK 600 HETEROGEN
REMARK 600
REMARK 600 FOR METAL ATOM CD CD A2090 THE COORDINATION ANGLES ARE:
REMARK 600 1 CYS 823A SG
REMARK 600 2 HIS 886A ND1 96.8
REMARK 600 3 GLU 1017B OE1 108.6 94.4
REMARK 600 4 GLU 1017B OE2 155.1 101.5 53.5
REMARK 600 5 HOH 171Z O 128.1 87.4 122.6 69.9
REMARK 600 1 2 3 4
REMARK 600
REMARK 600 FOR METAL ATOM CD CD A2091 THE COORDINATION ANGLES ARE:
REMARK 600 1 GLU 1079A OE1
REMARK 600 2 GLU 1079A OE2 54.3
REMARK 600 3 GLU 894A OE2 119.3 172.3
REMARK 600 4 HIS 1076A ND1 96.6 97.6 87.0
REMARK 600 5 HIS 1083A ND1 88.8 89.5 86.1 172.7
REMARK 600 6 HIS 1085A NE2 142.0 87.9 98.8 83.4 95.5
REMARK 600 1 2 3 4 5
REMARK 600
REMARK 600 FOR METAL ATOM CD CD A2092 THE COORDINATION ANGLES ARE:
REMARK 600 1 HIS 1082B NE2
REMARK 600 2 HIS 1084B NE2 102.1
REMARK 600 3 HOH 354Y O 86.6 152.6
REMARK 600 4 HOH 265Z O 102.6 101.6 51.0
REMARK 600 5 GLU 1007A OE1 155.0 91.4 91.1 95.1
REMARK 600 6 GLU 1007A OE2 99.8 118.0 85.3 128.6 55.1
REMARK 600 1 2 3 4 5
REMARK 600
REMARK 600 FOR METAL ATOM CD CD A2093 THE COORDINATION ANGLES ARE:
REMARK 600 1 HIS 947A NE2
REMARK 600 2 HOH 221Z O 107.7
REMARK 600 3 HOH 225Z O 89.8 86.0
REMARK 600 4 HOH 338Z O 177.7 71.7 92.3
REMARK 600 5 HIS 1080A NE2 94.0 150.0 115.2 85.8
REMARK 600 6 HOH 331Z O 92.0 73.4 158.8 85.7 85.8
REMARK 600 1 2 3 4 5
REMARK 600
REMARK 600 FOR METAL ATOM CD CD A2094 THE COORDINATION ANGLES ARE:
REMARK 600 1 HOH 344Z O
REMARK 600 2 HIS 1081A ND1 101.6
REMARK 600 3 HOH 349Z O 66.5 123.0
REMARK 600 1 2
REMARK 600
REMARK 600 FOR METAL ATOM CD CD A2095 THE COORDINATION ANGLES ARE:
REMARK 600 1 ACY 2089A C
REMARK 600 2 ACY 2089A O 27.1
REMARK 600 3 ACY 2089A OXT 27.1 54.1
REMARK 600 4 HOH 369Z O 108.3 133.2 82.3
REMARK 600 1 2 3
REMARK 600
REMARK 600 FOR METAL ATOM CD CD B2090 THE COORDINATION ANGLES ARE:
REMARK 600 1 GLU 1017A OE1
REMARK 600 2 GLU 1017A OE2 53.9
REMARK 600 3 CYS 823B SG 107.1 154.3
REMARK 600 4 HIS 886B ND1 89.6 100.6 96.1
REMARK 600 5 HOH 163Y O 126.4 73.9 126.3 88.5
REMARK 600 1 2 3 4
REMARK 600
REMARK 600 FOR METAL ATOM CD CD B2091 THE COORDINATION ANGLES ARE:
REMARK 600 1 GLU 1079B OE1
REMARK 600 2 GLU 1079B OE2 54.6
REMARK 600 3 GLU 894B OE2 120.9 172.9
REMARK 600 4 HIS 1076B ND1 97.5 98.1 87.9
REMARK 600 5 HIS 1083B ND1 86.9 87.8 86.4 174.0
REMARK 600 6 HIS 1085B NE2 140.3 85.9 98.8 83.5 95.7
REMARK 600 1 2 3 4 5
REMARK 600
REMARK 600 FOR METAL ATOM CD CD B2092 THE COORDINATION ANGLES ARE:
REMARK 600 1 HIS 1082A NE2
REMARK 600 2 HIS 1084A NE2 101.3
REMARK 600 3 GLU 1007B OE1 156.0 90.8
REMARK 600 4 GLU 1007B OE2 100.8 112.5 55.2
REMARK 600 5 HOH 348Z O 89.3 144.3 92.8 98.5
REMARK 600 6 HOH 355Z O 104.9 96.8 94.0 136.0 47.6
REMARK 600 1 2 3 4 5
REMARK 600
REMARK 600 FOR METAL ATOM CD CD B2093 THE COORDINATION ANGLES ARE:
REMARK 600 1 HOH 345Y O
REMARK 600 2 HIS 947B NE2 178.3
REMARK 600 3 HIS 1080B NE2 88.5 92.9
REMARK 600 4 HOH 228Y O 89.1 91.0 113.9
REMARK 600 5 HOH 229Y O 68.1 110.3 152.0 82.1
REMARK 600 6 HOH 337Y O 93.3 86.2 81.0 164.9 85.0
REMARK 600 1 2 3 4 5
REMARK 600
REMARK 600 FOR METAL ATOM CD CD B2094 THE COORDINATION ANGLES ARE:
REMARK 600 1 HOH 355Y O
REMARK 600 2 HIS 1081B ND1 118.4
REMARK 600 3 HOH 350Y O 74.4 108.7
REMARK 600 4 HOH 351Y O 136.7 104.7 97.3
REMARK 600 1 2 3
REMARK 600
REMARK 600 FOR METAL ATOM CD CD B2095 THE COORDINATION ANGLES ARE:
REMARK 600 1 HOH 378Y O
REMARK 600 2 ACY 2089B C 96.7
REMARK 600 3 ACY 2089B O 106.3 27.8
REMARK 600 4 ACY 2089B OXT 85.9 27.8 55.6
REMARK 600 5 HOH 351Y O 85.5 176.1 154.2 149.9
REMARK 600 1 2 3 4
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: FEA
REMARK 800 SITE_DESCRIPTION: FER BINDING SITE FOR CHAIN A
REMARK 800
REMARK 800 SITE_IDENTIFIER: FEB
REMARK 800 SITE_DESCRIPTION: FER BINDING SITE FOR CHAIN B
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1DYO RELATED DB: PDB
REMARK 900 XYLAN-BINDING DOMAIN FROM CBM 22, FORMALLY
REMARK 900 X6B DOMAIN
REMARK 900 RELATED ID: 1GKK RELATED DB: PDB
REMARK 900 FERULOYL ESTERASE DOMAIN OF XYNY FROM
REMARK 900 CLOSTRIDIUM THERMOCELLUM
REMARK 900 RELATED ID: 1H6X RELATED DB: PDB
REMARK 900 THE ROLE OF CONSERVED AMONI ACIDS IN THE
REMARK 900 CLEFT OF THE C-TERMINAL FAMILY 22
REMARK 900 CARBOHYDRATE BINDING MODULE OF CLOSTRIDIUM
REMARK 900 THERMOCELLUM XYN10B IN LIGAND BINDING
REMARK 900 RELATED ID: 1H6Y RELATED DB: PDB
REMARK 900 THE ROLE OF CONSERVED AMONI ACIDS IN THE
REMARK 900 CLEFT OF THE C-TERMINAL FAMILY 22
REMARK 900 CARBOHYDRATE BINDING MODULE OF CLOSTRIDIUM
REMARK 900 THERMOCELLUM XYN10B IN LIGAND BINDING
DBREF 1GKL A 789 791 PDB 1GKL 1GKL 789 791
DBREF 1GKL A 792 1077 SWS P51584 XYNY_CLOTM 792 1077
DBREF 1GKL A 1078 1085 PDB 1GKL 1GKL 1078 1085
DBREF 1GKL B 792 1077 SWS P51584 XYNY_CLOTM 792 1077
DBREF 1GKL B 1078 1085 PDB 1GKL 1GKL 1078 1085
SEQADV 1GKL GLU A 1017 SWS P51584 ASP 1017 CONFLICT
SEQADV 1GKL ASP A 1018 SWS P51584 HIS 1018 CONFLICT
SEQADV 1GKL ALA A 954 SWS P51584 SER 954 ENGINEERED MUTATION
SEQADV 1GKL GLU B 1017 SWS P51584 ASP 1017 CONFLICT
SEQADV 1GKL ASP B 1018 SWS P51584 HIS 1018 CONFLICT
SEQADV 1GKL ALA B 954 SWS P51584 SER 954 ENGINEERED MUTATION
SEQRES 1 A 297 MET ALA SER ASP LYS PHE PRO VAL ALA GLU ASN PRO SER
SEQRES 2 A 297 SER SER PHE LYS TYR GLU SER ALA VAL GLN TYR ARG PRO
SEQRES 3 A 297 ALA PRO ASP SER TYR LEU ASN PRO CYS PRO GLN ALA GLY
SEQRES 4 A 297 ARG ILE VAL LYS GLU THR TYR THR GLY ILE ASN GLY THR
SEQRES 5 A 297 LYS SER LEU ASN VAL TYR LEU PRO TYR GLY TYR ASP PRO
SEQRES 6 A 297 ASN LYS LYS TYR ASN ILE PHE TYR LEU MET HIS GLY GLY
SEQRES 7 A 297 GLY GLU ASN GLU ASN THR ILE PHE SER ASN ASP VAL LYS
SEQRES 8 A 297 LEU GLN ASN ILE LEU ASP HIS ALA ILE MET ASN GLY GLU
SEQRES 9 A 297 LEU GLU PRO LEU ILE VAL VAL THR PRO THR PHE ASN GLY
SEQRES 10 A 297 GLY ASN CYS THR ALA GLN ASN PHE TYR GLN GLU PHE ARG
SEQRES 11 A 297 GLN ASN VAL ILE PRO PHE VAL GLU SER LYS TYR SER THR
SEQRES 12 A 297 TYR ALA GLU SER THR THR PRO GLN GLY ILE ALA ALA SER
SEQRES 13 A 297 ARG MET HIS ARG GLY PHE GLY GLY PHE ALA MET GLY GLY
SEQRES 14 A 297 LEU THR THR TRP TYR VAL MET VAL ASN CYS LEU ASP TYR
SEQRES 15 A 297 VAL ALA TYR PHE MET PRO LEU SER GLY ASP TYR TRP TYR
SEQRES 16 A 297 GLY ASN SER PRO GLN ASP LYS ALA ASN SER ILE ALA GLU
SEQRES 17 A 297 ALA ILE ASN ARG SER GLY LEU SER LYS ARG GLU TYR PHE
SEQRES 18 A 297 VAL PHE ALA ALA THR GLY SER GLU ASP ILE ALA TYR ALA
SEQRES 19 A 297 ASN MET ASN PRO GLN ILE GLU ALA MET LYS ALA LEU PRO
SEQRES 20 A 297 HIS PHE ASP TYR THR SER ASP PHE SER LYS GLY ASN PHE
SEQRES 21 A 297 TYR PHE LEU VAL ALA PRO GLY ALA THR HIS TRP TRP GLY
SEQRES 22 A 297 TYR VAL ARG HIS TYR ILE TYR ASP ALA LEU PRO TYR PHE
SEQRES 23 A 297 PHE HIS GLU LEU GLU HIS HIS HIS HIS HIS HIS
SEQRES 1 B 297 MET ALA SER ASP LYS PHE PRO VAL ALA GLU ASN PRO SER
SEQRES 2 B 297 SER SER PHE LYS TYR GLU SER ALA VAL GLN TYR ARG PRO
SEQRES 3 B 297 ALA PRO ASP SER TYR LEU ASN PRO CYS PRO GLN ALA GLY
SEQRES 4 B 297 ARG ILE VAL LYS GLU THR TYR THR GLY ILE ASN GLY THR
SEQRES 5 B 297 LYS SER LEU ASN VAL TYR LEU PRO TYR GLY TYR ASP PRO
SEQRES 6 B 297 ASN LYS LYS TYR ASN ILE PHE TYR LEU MET HIS GLY GLY
SEQRES 7 B 297 GLY GLU ASN GLU ASN THR ILE PHE SER ASN ASP VAL LYS
SEQRES 8 B 297 LEU GLN ASN ILE LEU ASP HIS ALA ILE MET ASN GLY GLU
SEQRES 9 B 297 LEU GLU PRO LEU ILE VAL VAL THR PRO THR PHE ASN GLY
SEQRES 10 B 297 GLY ASN CYS THR ALA GLN ASN PHE TYR GLN GLU PHE ARG
SEQRES 11 B 297 GLN ASN VAL ILE PRO PHE VAL GLU SER LYS TYR SER THR
SEQRES 12 B 297 TYR ALA GLU SER THR THR PRO GLN GLY ILE ALA ALA SER
SEQRES 13 B 297 ARG MET HIS ARG GLY PHE GLY GLY PHE ALA MET GLY GLY
SEQRES 14 B 297 LEU THR THR TRP TYR VAL MET VAL ASN CYS LEU ASP TYR
SEQRES 15 B 297 VAL ALA TYR PHE MET PRO LEU SER GLY ASP TYR TRP TYR
SEQRES 16 B 297 GLY ASN SER PRO GLN ASP LYS ALA ASN SER ILE ALA GLU
SEQRES 17 B 297 ALA ILE ASN ARG SER GLY LEU SER LYS ARG GLU TYR PHE
SEQRES 18 B 297 VAL PHE ALA ALA THR GLY SER GLU ASP ILE ALA TYR ALA
SEQRES 19 B 297 ASN MET ASN PRO GLN ILE GLU ALA MET LYS ALA LEU PRO
SEQRES 20 B 297 HIS PHE ASP TYR THR SER ASP PHE SER LYS GLY ASN PHE
SEQRES 21 B 297 TYR PHE LEU VAL ALA PRO GLY ALA THR HIS TRP TRP GLY
SEQRES 22 B 297 TYR VAL ARG HIS TYR ILE TYR ASP ALA LEU PRO TYR PHE
SEQRES 23 B 297 PHE HIS GLU LEU GLU HIS HIS HIS HIS HIS HIS
HET FER A2086 14
HET FER B2086 14
HET GOL B2087 6
HET GOL A2087 6
HET GOL B2088 6
HET GOL A2088 6
HET ACY B2089 4
HET ACY A2089 4
HET CD B2090 1
HET CD B2091 1
HET CD B2092 1
HET CD B2093 1
HET CD A2090 1
HET CD A2091 1
HET CD A2092 1
HET CD A2093 1
HET CD A2094 1
HET CD B2094 1
HET CD A2095 1
HET CD B2095 1
HETNAM FER 3-(4-HYDROXY-3-METHOXYPHENYL)-2-PROPENOIC
HETNAM 2 FER ACID
HETNAM GOL GLYCEROL
HETNAM ACY ACETIC ACID
HETNAM CD CADMIUM ION
FORMUL 3 FER 2(C10 H10 O4)
FORMUL 4 GOL 4(C3 H8 O3)
FORMUL 5 ACY 2(C2 H4 O2)
FORMUL 6 CD 12(CD1 2+)
FORMUL 7 HOH *751(H2 O1)
HELIX 1 1 PRO A 816 ASN A 821 5 6
HELIX 2 2 LYS A 879 ASN A 890 1 12
HELIX 3 3 ASN A 912 ASN A 920 1 9
HELIX 4 4 ASN A 920 TYR A 929 1 10
HELIX 5 5 THR A 937 ALA A 943 1 7
HELIX 6 6 SER A 944 MET A 946 5 3
HELIX 7 7 ALA A 954 LEU A 968 1 15
HELIX 8 8 SER A 986 GLY A 1002 1 17
HELIX 9 9 ALA A 1020 ALA A 1033 1 14
HELIX 10 10 TRP A 1059 LEU A 1071 1 13
HELIX 11 11 PRO A 1072 PHE A 1074 5 3
HELIX 12 12 PRO B 816 ASN B 821 5 6
HELIX 13 13 LYS B 879 ASN B 890 1 12
HELIX 14 14 ASN B 912 ASN B 920 1 9
HELIX 15 15 ASN B 920 TYR B 929 1 10
HELIX 16 16 THR B 937 ALA B 943 1 7
HELIX 17 17 SER B 944 MET B 946 5 3
HELIX 18 18 ALA B 954 LEU B 968 1 15
HELIX 19 19 SER B 986 GLY B 1002 1 17
HELIX 20 20 ILE B 1019 ALA B 1033 1 15
HELIX 21 21 TRP B 1059 LEU B 1071 1 13
HELIX 22 22 PRO B 1072 PHE B 1074 5 3
SHEET 1 AA 8 ARG A 828 GLY A 836 0
SHEET 2 AA 8 GLY A 839 LEU A 847 -1 O GLY A 839 N GLY A 836
SHEET 3 AA 8 LEU A 896 THR A 900 -1 O VAL A 898 N TYR A 846
SHEET 4 AA 8 ASN A 858 MET A 863 1 O ASN A 858 N ILE A 897
SHEET 5 AA 8 ARG A 948 PHE A 953 1 O GLY A 949 N TYR A 861
SHEET 6 AA 8 TYR A 973 LEU A 977 1 O TYR A 973 N PHE A 950
SHEET 7 AA 8 PHE A1009 GLY A1015 1 O PHE A1009 N PHE A 974
SHEET 8 AA 8 PHE A1048 ALA A1053 1 O TYR A1049 N ALA A1012
SHEET 1 BA 8 ARG B 828 GLY B 836 0
SHEET 2 BA 8 GLY B 839 LEU B 847 -1 O GLY B 839 N GLY B 836
SHEET 3 BA 8 LEU B 896 THR B 900 -1 O VAL B 898 N TYR B 846
SHEET 4 BA 8 ASN B 858 MET B 863 1 O ASN B 858 N ILE B 897
SHEET 5 BA 8 ARG B 948 PHE B 953 1 O GLY B 949 N TYR B 861
SHEET 6 BA 8 TYR B 973 LEU B 977 1 O TYR B 973 N PHE B 950
SHEET 7 BA 8 PHE B1009 GLU B1017 1 O PHE B1009 N PHE B 974
SHEET 8 BA 8 PHE B1048 THR B1057 1 O TYR B1049 N ALA B1012
LINK CD CD A2090 SG CYS A 823 1555 1555 2.51
LINK CD CD A2090 ND1 HIS A 886 1555 1555 2.37
LINK CD CD A2090 OE1 GLU B1017 1555 2574 2.20
LINK CD CD A2090 OE2 GLU B1017 1555 2574 2.60
LINK CD CD A2090 O HOH Z 171 1555 1555 2.33
LINK CD CD A2091 OE1 GLU A1079 1555 1555 2.33
LINK CD CD A2091 OE2 GLU A1079 1555 1555 2.45
LINK CD CD A2091 OE2 GLU A 894 1555 1555 2.29
LINK CD CD A2091 ND1 HIS A1076 1555 1555 2.41
LINK CD CD A2091 ND1 HIS A1083 1555 1555 2.35
LINK CD CD A2091 NE2 HIS A1085 1555 1555 2.32
LINK CD CD A2092 NE2 HIS B1082 1555 1655 2.24
LINK CD CD A2092 NE2 HIS B1084 1555 1655 2.25
LINK CD CD A2092 O HOH Y 354 1555 1655 2.58
LINK CD CD A2092 O HOH Z 265 1555 1555 2.34
LINK CD CD A2092 OE1 GLU A1007 1555 1555 2.33
LINK CD CD A2092 OE2 GLU A1007 1555 1555 2.35
LINK CD CD A2093 NE2 HIS A 947 1555 1555 2.23
LINK CD CD A2093 O AHOH Z 221 1555 1555 2.43
LINK CD CD A2093 O HOH Z 225 1555 1555 2.28
LINK CD CD A2093 O HOH Z 338 1555 1555 2.20
LINK CD CD A2093 NE2 HIS A1080 1555 1555 2.25
LINK CD CD A2093 O HOH Z 331 1555 1555 2.43
LINK CD A CD A2094 O HOH Z 344 1555 1555 2.34
LINK CD A CD A2094 ND1 HIS A1081 1555 1555 1.46
LINK CD A CD A2094 O HOH Z 349 1555 1555 2.61
LINK CD A CD A2095 C ACY A2089 1555 1555 2.73
LINK CD A CD A2095 O ACY A2089 1555 1555 2.34
LINK CD A CD A2095 OXT ACY A2089 1555 1555 2.47
LINK CD A CD A2095 O HOH Z 369 1555 1555 2.45
LINK CD CD B2090 SG CYS B 823 1555 1555 2.52
LINK CD CD B2090 OE2 GLU A1017 1555 3545 2.49
LINK CD CD B2090 ND1 HIS B 886 1555 1555 2.37
LINK CD CD B2090 O HOH Y 163 1555 1555 2.34
LINK CD CD B2090 OE1 GLU A1017 1555 3545 2.29
LINK CD CD B2091 OE2 GLU B1079 1555 1555 2.47
LINK CD CD B2091 OE2 GLU B 894 1555 1555 2.29
LINK CD CD B2091 ND1 HIS B1076 1555 1555 2.38
LINK CD CD B2091 ND1 HIS B1083 1555 1555 2.35
LINK CD CD B2091 NE2 HIS B1085 1555 1555 2.32
LINK CD CD B2091 OE1 GLU B1079 1555 1555 2.34
LINK CD CD B2092 NE2 HIS A1084 1555 1455 2.26
LINK CD CD B2092 OE1 GLU B1007 1555 1555 2.39
LINK CD CD B2092 OE2 GLU B1007 1555 1555 2.29
LINK CD CD B2092 O AHOH Z 348 1555 1555 2.37
LINK CD CD B2092 O BHOH Z 355 1555 1555 2.36
LINK CD CD B2092 NE2 HIS A1082 1555 1455 2.26
LINK CD CD B2093 NE2 HIS B 947 1555 1555 2.21
LINK CD CD B2093 NE2 HIS B1080 1555 1555 2.22
LINK CD CD B2093 O HOH Y 228 1555 1555 2.26
LINK CD CD B2093 O AHOH Y 229 1555 1555 2.54
LINK CD CD B2093 O HOH Y 337 1555 1555 2.21
LINK CD CD B2093 O HOH Y 345 1555 1555 2.16
LINK CD A CD B2094 ND1 HIS B1081 1555 1555 1.67
LINK CD A CD B2094 O HOH Y 350 1555 1555 2.03
LINK CD A CD B2094 O HOH Y 351 1555 1555 2.39
LINK CD A CD B2094 O HOH Y 355 1555 1555 2.47
LINK CD A CD B2095 C ACY B2089 1555 1555 2.68
LINK CD A CD B2095 O ACY B2089 1555 1555 2.32
LINK CD A CD B2095 OXT ACY B2089 1555 1555 2.40
LINK CD A CD B2095 O HOH Y 351 1555 1555 2.32
LINK CD A CD B2095 O HOH Y 378 1555 1555 2.13
SITE 1 FEA 8 ALA A 954 LEU A 958 GLY A 979 ASP A 980
SITE 2 FEA 8 TRP A 982 ALA A1020 HOH Z 363 HOH Z 364
SITE 1 FEB 11 ALA B 954 LEU B 958 GLY B 979 ASP B 980
SITE 2 FEB 11 TRP B 982 ALA B1020 ASN B1023 HOH Y 369
SITE 3 FEB 11 HOH Y 370 HOH Y 371 HOH Y 372
CRYST1 65.101 108.233 112.964 90.00 90.00 90.00 P 21 21 21 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 0.015361 0.000000 0.000000 0.00000
SCALE2 0.000000 0.009239 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008852 0.00000
END |