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HEADER HYDROLASE 15-AUG-01 1GKK
TITLE FERULOYL ESTERASE DOMAIN OF XYNY FROM CLOSTRIDIUM
TITLE 2 THERMOCELLUM
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, B;
COMPND 6 FRAGMENT: FERULOYL ESTERASE DOMAIN RESIDUES 792-1077;
COMPND 7 EC: 3.2.1.8;
COMPND 8 ENGINEERED: 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: PET21A
KEYWDS FERULIC ACID, ESTERASE FAMILY 1, X-RAY 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 1GKK 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. 1.6 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) : 1.60
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 20.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : NONE
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.03
REMARK 3 NUMBER OF REFLECTIONS : 101173
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) : 0.15499
REMARK 3 R VALUE (WORKING SET) : 0.15404
REMARK 3 FREE R VALUE : 0.17298
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.0
REMARK 3 FREE R VALUE TEST SET COUNT : 5323
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH : 1.600
REMARK 3 BIN RESOLUTION RANGE LOW : 1.641
REMARK 3 REFLECTION IN BIN (WORKING SET) : 6890
REMARK 3 BIN R VALUE (WORKING SET) : 0.195
REMARK 3 BIN FREE R VALUE SET COUNT : 362
REMARK 3 BIN FREE R VALUE : 0.210
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 4507
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 164
REMARK 3 SOLVENT ATOMS : 752
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 12.923
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.24
REMARK 3 B22 (A**2) : -0.01
REMARK 3 B33 (A**2) : -0.23
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): 0.066
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.065
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.089
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 2.489
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.967
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.960
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED (A): 4823 ; 0.016 ; 0.021
REMARK 3 BOND LENGTHS OTHERS (A): 4001 ; 0.003 ; 0.020
REMARK 3 BOND ANGLES OTHERS (DEGREES): 6568 ; 1.576 ; 1.917
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 9375 ; 2.801 ; 3.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 574 ; 4.918 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 784 ;15.925 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 654 ; 0.108 ; 0.200
REMARK 3 GENERAL PLANES REFINED (A): 5453 ; 0.009 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 1076 ; 0.006 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED (A): 1041 ; 0.224 ; 0.300
REMARK 3 NON-BONDED CONTACTS OTHERS (A): 3975 ; 0.197 ; 0.300
REMARK 3 NON-BONDED TORSION OTHERS (A): 16 ; 0.323 ; 0.500
REMARK 3 H-BOND (X...Y) REFINED (A): 601 ; 0.136 ; 0.500
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): 11 ; 0.173 ; 0.
REMARK 3 SYMMETRY VDW REFINED (A): 17 ; 0.288 ; 0.300
REMARK 3 SYMMETRY VDW OTHERS (A): 35 ; 0.236 ; 0.300
REMARK 3 SYMMETRY H-BOND REFINED (A): 34 ; 0.179 ; 0.500
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED (A**2): 2831 ; 0.919 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE REFINED (A**2): 4589 ; 1.511 ; 2.000
REMARK 3 SIDE-CHAIN BOND REFINED (A**2): 1992 ; 2.337 ; 3.000
REMARK 3 SIDE-CHAIN ANGLE REFINED (A**2): 1978 ; 3.476 ; 4.500
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 : 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:
REMARK 3 HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS
REMARK 4
REMARK 4 1GKK 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-8253.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 15-DEC-2000
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 : ESRF BEAMLINE ID29
REMARK 200 BEAMLINE : ID29
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9754,0.9796
REMARK 200 MONOCHROMATOR : SI
REMARK 200 OPTICS : CYLINDRICAL GRAZING
REMARK 200 INCIDENCE MIRROR
REMARK 200
REMARK 200 DETECTOR TYPE : QUANTUM 4
REMARK 200 DETECTOR MANUFACTURER : ADSC
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA-TRUNCATE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 106584
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.6
REMARK 200 RESOLUTION RANGE LOW (A) : 30
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NONE
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.1
REMARK 200 DATA REDUNDANCY : 3.9
REMARK 200 R MERGE (I) : 0.055
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 15
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.6
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.69
REMARK 200 COMPLETENESS FOR SHELL (%) : 95.1
REMARK 200 DATA REDUNDANCY IN SHELL : 2.9
REMARK 200 R MERGE FOR SHELL (I) : 0.224
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 3
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: MAD
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MAD
REMARK 200 SOFTWARE USED: SOLVE
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 100MM,
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 32.69050
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 56.93850
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 54.39650
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 56.93850
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 32.69050
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 54.39650
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 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 MSE 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 MSE 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 2.14
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 A2086 THE COORDINATION ANGLES ARE:
REMARK 600 1 CYS 823A SG
REMARK 600 2 GLU 1017B OE1 108.1
REMARK 600 3 HIS 886A ND1 94.0 90.6
REMARK 600 4 GLU 1017B OE2 154.8 53.9 103.0
REMARK 600 5 HOH 164Z O 125.6 126.1 89.0 73.8
REMARK 600 1 2 3 4
REMARK 600
REMARK 600 FOR METAL ATOM CD CD A2087 THE COORDINATION ANGLES ARE:
REMARK 600 1 GLU 1079A OE1
REMARK 600 2 GLU 1079A OE2 53.7
REMARK 600 3 GLU 894A OE2 128.6 171.0
REMARK 600 4 HIS 1076A ND1 96.4 99.1 89.4
REMARK 600 5 HIS 1083A ND1 85.2 83.9 87.6 177.0
REMARK 600 6 HIS 1085A NE2 139.2 85.7 92.1 85.4 95.0
REMARK 600 1 2 3 4 5
REMARK 600
REMARK 600 FOR METAL ATOM CD CD A2088 THE COORDINATION ANGLES ARE:
REMARK 600 1 HIS 1082B NE2
REMARK 600 2 HIS 1084B NE2 98.1
REMARK 600 3 HOH 272Z O 100.4 106.8
REMARK 600 4 GLU 1007A OE1 156.8 93.5 95.3
REMARK 600 5 GLU 1007A OE2 102.3 119.4 124.1 54.6
REMARK 600 1 2 3 4
REMARK 600
REMARK 600 FOR METAL ATOM CD CD A2089 THE COORDINATION ANGLES ARE:
REMARK 600 1 HIS 947A NE2
REMARK 600 2 HOH 231Z O 96.6
REMARK 600 3 HOH 232Z O 89.3 72.8
REMARK 600 4 HOH 346Z O 170.4 75.0 83.8
REMARK 600 5 HIS 1080A NE2 102.9 156.2 120.6 86.4
REMARK 600 6 HOH 343Z O 83.7 89.6 160.1 100.6 79.2
REMARK 600 1 2 3 4 5
REMARK 600
REMARK 600 FOR METAL ATOM CD CD A2090 THE COORDINATION ANGLES ARE:
REMARK 600 1 HIS 1081A ND1
REMARK 600 2 HOH 349Z O 113.5
REMARK 600 1
REMARK 600
REMARK 600 FOR METAL ATOM CD CD B2086 THE COORDINATION ANGLES ARE:
REMARK 600 1 GLU 1017A OE2
REMARK 600 2 CYS 823B SG 152.3
REMARK 600 3 HIS 886B ND1 104.7 93.7
REMARK 600 4 HOH 193Y O 75.9 124.8 91.3
REMARK 600 5 GLU 1017A OE1 53.7 106.0 92.4 128.6
REMARK 600 1 2 3 4
REMARK 600
REMARK 600 FOR METAL ATOM CD CD B2087 THE COORDINATION ANGLES ARE:
REMARK 600 1 GLU 1079B OE1
REMARK 600 2 GLU 1079B OE2 54.1
REMARK 600 3 GLU 894B OE2 129.4 167.5
REMARK 600 4 HIS 1076B ND1 95.7 101.6 90.2
REMARK 600 5 HIS 1083B ND1 87.8 83.4 84.7 174.9
REMARK 600 6 HIS 1085B NE2 139.6 85.9 90.9 85.7 94.1
REMARK 600 1 2 3 4 5
REMARK 600
REMARK 600 FOR METAL ATOM CD CD B2088 THE COORDINATION ANGLES ARE:
REMARK 600 1 HIS 1082A NE2
REMARK 600 2 HIS 1084A NE2 100.5
REMARK 600 3 HOH 297Y O 91.6 144.5
REMARK 600 4 GLU 1007B OE1 156.1 91.8 90.0
REMARK 600 5 GLU 1007B OE2 101.2 112.3 97.5 54.9
REMARK 600 1 2 3 4
REMARK 600
REMARK 600 FOR METAL ATOM CD CD B2089 THE COORDINATION ANGLES ARE:
REMARK 600 1 HOH 365Y O
REMARK 600 2 HIS 947B NE2 173.6
REMARK 600 3 HIS 1080B NE2 90.8 92.5
REMARK 600 4 HOH 253Y O 79.3 99.3 158.5
REMARK 600 5 HOH 254Y O 87.2 86.5 108.9 89.9
REMARK 600 6 HOH 361Y O 109.5 76.8 73.9 91.3 163.2
REMARK 600 1 2 3 4 5
REMARK 600
REMARK 600 FOR METAL ATOM CD CD B2090 THE COORDINATION ANGLES ARE:
REMARK 600 1 HOH 366Y O
REMARK 600 2 HOH 371Y O 75.8
REMARK 600 3 HIS 1081B ND1 113.5 120.7
REMARK 600 1 2
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: 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
REMARK 900 RELATED ID: 1GKL RELATED DB: PDB
REMARK 900 S954A MUTANT OF THE FERULOYL ESTERASE MODULE
REMARK 900 FROM CLOSTRIDIUM THERMOCELLUM COMPLEXED WITH
REMARK 900 FERULIC ACID
DBREF 1GKK A 789 791 PDB 1GKK 1GKK 789 791
DBREF 1GKK A 792 1077 SWS P51584 XYNY_CLOTM 792 1077
DBREF 1GKK A 1078 1085 PDB 1GKK 1GKK 1078 1085
DBREF 1GKK B 789 791 PDB 1GKK 1GKK 789 791
DBREF 1GKK B 792 1077 SWS P51584 XYNY_CLOTM 792 1077
DBREF 1GKK B 1078 1085 PDB 1GKK 1GKK 1078 1085
SEQADV 1GKK MSE A 863 SWS P51584 MET 863 MODIFIED RESIDUE
SEQADV 1GKK MSE A 889 SWS P51584 MET 889 MODIFIED RESIDUE
SEQADV 1GKK MSE A 946 SWS P51584 MET 946 MODIFIED RESIDUE
SEQADV 1GKK SEP A 954 SWS P51584 SER 954 MODIFIED RESIDUE
SEQADV 1GKK MSE A 955 SWS P51584 MET 955 MODIFIED RESIDUE
SEQADV 1GKK MSE A 964 SWS P51584 MET 964 MODIFIED RESIDUE
SEQADV 1GKK MSE A 975 SWS P51584 MET 975 MODIFIED RESIDUE
SEQADV 1GKK MSE A 1024 SWS P51584 MET 1024 MODIFIED RESIDUE
SEQADV 1GKK MSE A 1031 SWS P51584 MET 1031 MODIFIED RESIDUE
SEQADV 1GKK MSE B 863 SWS P51584 MET 863 MODIFIED RESIDUE
SEQADV 1GKK MSE B 889 SWS P51584 MET 889 MODIFIED RESIDUE
SEQADV 1GKK MSE B 946 SWS P51584 MET 946 MODIFIED RESIDUE
SEQADV 1GKK SEP B 954 SWS P51584 SER 954 MODIFIED RESIDUE
SEQADV 1GKK MSE B 955 SWS P51584 MET 955 MODIFIED RESIDUE
SEQADV 1GKK MSE B 964 SWS P51584 MET 964 MODIFIED RESIDUE
SEQADV 1GKK MSE B 975 SWS P51584 MET 975 MODIFIED RESIDUE
SEQADV 1GKK MSE B 1024 SWS P51584 MET 1024 MODIFIED RESIDUE
SEQADV 1GKK MSE B 1031 SWS P51584 MET 1031 MODIFIED RESIDUE
SEQADV 1GKK GLU A 1017 SWS P51584 ASP 1017 CONFLICT
SEQADV 1GKK ASP A 1018 SWS P51584 HIS 1018 CONFLICT
SEQADV 1GKK GLU B 1017 SWS P51584 ASP 1017 CONFLICT
SEQADV 1GKK ASP B 1018 SWS P51584 HIS 1018 CONFLICT
SEQRES 1 A 297 MSE 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 MSE 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 MSE 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 MSE HIS ARG GLY PHE GLY GLY PHE SEP MSE GLY GLY
SEQRES 14 A 297 LEU THR THR TRP TYR VAL MSE VAL ASN CYS LEU ASP TYR
SEQRES 15 A 297 VAL ALA TYR PHE MSE 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 MSE ASN PRO GLN ILE GLU ALA MSE 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 MSE 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 MSE 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 MSE 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 MSE HIS ARG GLY PHE GLY GLY PHE SEP MSE GLY GLY
SEQRES 14 B 297 LEU THR THR TRP TYR VAL MSE VAL ASN CYS LEU ASP TYR
SEQRES 15 B 297 VAL ALA TYR PHE MSE 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 MSE ASN PRO GLN ILE GLU ALA MSE 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
MODRES 1GKK MSE A 863 MET SELENOMETHIONINE
MODRES 1GKK MSE A 889 MET SELENOMETHIONINE
MODRES 1GKK MSE A 946 MET SELENOMETHIONINE
MODRES 1GKK SEP A 954 SER PHOSPHOSERINE
MODRES 1GKK MSE A 955 MET SELENOMETHIONINE
MODRES 1GKK MSE A 964 MET SELENOMETHIONINE
MODRES 1GKK MSE A 975 MET SELENOMETHIONINE
MODRES 1GKK MSE A 1024 MET SELENOMETHIONINE
MODRES 1GKK MSE A 1031 MET SELENOMETHIONINE
MODRES 1GKK MSE B 863 MET SELENOMETHIONINE
MODRES 1GKK MSE B 889 MET SELENOMETHIONINE
MODRES 1GKK MSE B 946 MET SELENOMETHIONINE
MODRES 1GKK SEP B 954 SER PHOSPHOSERINE
MODRES 1GKK MSE B 955 MET SELENOMETHIONINE
MODRES 1GKK MSE B 964 MET SELENOMETHIONINE
MODRES 1GKK MSE B 975 MET SELENOMETHIONINE
MODRES 1GKK MSE B 1024 MET SELENOMETHIONINE
MODRES 1GKK MSE B 1031 MET SELENOMETHIONINE
HET MSE A 863 8
HET MSE A 889 8
HET MSE A 946 8
HET SEP A 954 7
HET MSE A 955 11
HET MSE A 964 8
HET MSE A 975 8
HET MSE A1024 8
HET MSE A1031 8
HET MSE B 863 8
HET MSE B 889 8
HET MSE B 946 8
HET SEP B 954 7
HET MSE B 955 11
HET MSE B 964 8
HET MSE B 975 8
HET MSE B1024 8
HET MSE B1031 8
HET CD B2086 1
HET CD B2087 1
HET CD B2088 1
HET CD B2089 1
HET CD A2086 1
HET CD A2087 1
HET CD A2088 1
HET CD A2089 1
HET CD A2090 1
HET CD B2090 1
HET GOL B2091 6
HETNAM MSE SELENOMETHIONINE
HETNAM SEP PHOSPHOSERINE
HETNAM CD CADMIUM ION
HETNAM GOL GLYCEROL
FORMUL 3 MSE 16(C5 H11 N1 O2 SE1)
FORMUL 4 SEP 2(C3 H8 N1 O6 P1)
FORMUL 5 CD 10(CD1 2+)
FORMUL 6 GOL C3 H8 O3
FORMUL 7 HOH *752(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 SER A 944 1 8
HELIX 6 6 SEP A 954 LEU A 968 1 15
HELIX 7 7 SER A 986 GLY A 1002 1 17
HELIX 8 8 ALA A 1020 ALA A 1033 1 14
HELIX 9 9 TRP A 1059 LEU A 1071 1 13
HELIX 10 10 PRO A 1072 PHE A 1074 5 3
HELIX 11 11 PRO B 816 ASN B 821 5 6
HELIX 12 12 LYS B 879 ASN B 890 1 12
HELIX 13 13 ASN B 912 ASN B 920 1 9
HELIX 14 14 ASN B 920 TYR B 929 1 10
HELIX 15 15 THR B 937 SER B 944 1 8
HELIX 16 16 SEP B 954 LEU B 968 1 15
HELIX 17 17 SER B 986 GLY B 1002 1 17
HELIX 18 18 ILE B 1019 ALA B 1033 1 15
HELIX 19 19 TRP B 1059 LEU B 1071 1 13
HELIX 20 20 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 MSE 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 ILE B 897 THR B 900 -1 O VAL B 898 N TYR B 846
SHEET 4 BA 8 ILE B 859 MSE B 863 1 O PHE B 860 N VAL B 899
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 GLY B1015 1 O PHE B1009 N PHE B 974
SHEET 8 BA 8 PHE B1048 ALA B1053 1 O TYR B1049 N ALA B1012
LINK C LEU A 862 N MSE A 863 1555 1555 1.33
LINK C MSE A 863 N HIS A 864 1555 1555 1.32
LINK C ILE A 888 N MSE A 889 1555 1555 1.31
LINK C MSE A 889 N ASN A 890 1555 1555 1.32
LINK C ARG A 945 N MSE A 946 1555 1555 1.32
LINK C MSE A 946 N HIS A 947 1555 1555 1.32
LINK C PHE A 953 N SEP A 954 1555 1555 1.33
LINK C SEP A 954 N MSE A 955 1555 1555 1.34
LINK C MSE A 955 N GLY A 956 1555 1555 1.33
LINK C VAL A 963 N MSE A 964 1555 1555 1.32
LINK C MSE A 964 N VAL A 965 1555 1555 1.31
LINK C PHE A 974 N MSE A 975 1555 1555 1.33
LINK C MSE A 975 N PRO A 976 1555 1555 1.33
LINK C ASN A1023 N MSE A1024 1555 1555 1.32
LINK C MSE A1024 N ASN A1025 1555 1555 1.33
LINK C ALA A1030 N MSE A1031 1555 1555 1.34
LINK C MSE A1031 N LYS A1032 1555 1555 1.31
LINK CD CD A2086 SG CYS A 823 1555 1555 2.54
LINK CD CD A2086 OE1 GLU B1017 1555 2574 2.37
LINK CD CD A2086 ND1 HIS A 886 1555 1555 2.37
LINK CD CD A2086 OE2 GLU B1017 1555 2574 2.43
LINK CD CD A2086 O HOH Z 164 1555 1555 2.41
LINK CD CD A2087 OE1 GLU A1079 1555 1555 2.32
LINK CD CD A2087 OE2 GLU A1079 1555 1555 2.56
LINK CD CD A2087 OE2 GLU A 894 1555 1555 2.40
LINK CD CD A2087 ND1 HIS A1076 1555 1555 2.31
LINK CD CD A2087 ND1 HIS A1083 1555 1555 2.32
LINK CD CD A2087 NE2 HIS A1085 1555 1555 2.30
LINK CD CD A2088 NE2 HIS B1082 1555 1655 2.27
LINK CD CD A2088 NE2 HIS B1084 1555 1655 2.26
LINK CD CD A2088 O HOH Z 272 1555 1555 2.32
LINK CD CD A2088 OE1 GLU A1007 1555 1555 2.31
LINK CD CD A2088 OE2 GLU A1007 1555 1555 2.40
LINK CD CD A2089 NE2 HIS A 947 1555 1555 2.21
LINK CD CD A2089 O HOH Z 231 1555 1555 2.15
LINK CD CD A2089 O HOH Z 232 1555 1555 2.25
LINK CD CD A2089 O HOH Z 346 1555 1555 2.14
LINK CD CD A2089 O HOH Z 343 1555 1555 2.32
LINK CD CD A2089 NE2 HIS A1080 1555 1555 2.03
LINK CD A CD A2090 O HOH Z 349 1555 1555 2.02
LINK CD A CD A2090 ND1 HIS A1081 1555 1555 1.90
LINK C LEU B 862 N MSE B 863 1555 1555 1.35
LINK C MSE B 863 N HIS B 864 1555 1555 1.33
LINK C ILE B 888 N MSE B 889 1555 1555 1.30
LINK C MSE B 889 N ASN B 890 1555 1555 1.33
LINK C ARG B 945 N MSE B 946 1555 1555 1.34
LINK C MSE B 946 N HIS B 947 1555 1555 1.33
LINK C PHE B 953 N SEP B 954 1555 1555 1.33
LINK C SEP B 954 N MSE B 955 1555 1555 1.33
LINK C MSE B 955 N GLY B 956 1555 1555 1.34
LINK C VAL B 963 N MSE B 964 1555 1555 1.33
LINK C MSE B 964 N VAL B 965 1555 1555 1.31
LINK C PHE B 974 N MSE B 975 1555 1555 1.34
LINK C MSE B 975 N PRO B 976 1555 1555 1.35
LINK C ASN B1023 N MSE B1024 1555 1555 1.33
LINK C MSE B1024 N ASN B1025 1555 1555 1.32
LINK C ALA B1030 N MSE B1031 1555 1555 1.34
LINK C MSE B1031 N LYS B1032 1555 1555 1.33
LINK CD CD B2086 SG CYS B 823 1555 1555 2.53
LINK CD CD B2086 ND1 HIS B 886 1555 1555 2.35
LINK CD CD B2086 O HOH Y 193 1555 1555 2.39
LINK CD CD B2086 OE1 GLU A1017 1555 3545 2.37
LINK CD CD B2086 OE2 GLU A1017 1555 3545 2.42
LINK CD CD B2087 OE2 GLU B1079 1555 1555 2.53
LINK CD CD B2087 OE2 GLU B 894 1555 1555 2.39
LINK CD CD B2087 ND1 HIS B1076 1555 1555 2.33
LINK CD CD B2087 ND1 HIS B1083 1555 1555 2.27
LINK CD CD B2087 NE2 HIS B1085 1555 1555 2.35
LINK CD CD B2087 OE1 GLU B1079 1555 1555 2.40
LINK CD CD B2088 NE2 HIS A1084 1555 1455 2.27
LINK CD CD B2088 O HOH Y 297 1555 1555 2.31
LINK CD CD B2088 OE1 GLU B1007 1555 1555 2.36
LINK CD CD B2088 OE2 GLU B1007 1555 1555 2.32
LINK CD CD B2088 NE2 HIS A1082 1555 1455 2.34
LINK CD CD B2089 NE2 HIS B 947 1555 1555 2.25
LINK CD CD B2089 NE2 HIS B1080 1555 1555 2.21
LINK CD CD B2089 O HOH Y 253 1555 1555 1.96
LINK CD CD B2089 O HOH Y 254 1555 1555 2.38
LINK CD CD B2089 O HOH Y 361 1555 1555 2.14
LINK CD CD B2089 O HOH Y 365 1555 1555 2.26
LINK CD A CD B2090 O HOH Y 371 1555 1555 2.59
LINK CD A CD B2090 ND1 HIS B1081 1555 1555 2.21
LINK CD A CD B2090 O HOH Y 366 1555 1555 1.93
CRYST1 65.381 108.793 113.877 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 0.015295 0.000000 0.000000 0.00000
SCALE2 0.000000 0.009192 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008781 0.00000
END |