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HEADER HYDROLASE 30-OCT-04 1WB4
TITLE S954A MUTANT OF THE FERULOYL ESTERASE MODULE FROM
TITLE 2 CLOSTRIDIUM THERMOCELLUM COMPLEXED WITH SINAPINATE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ENDO-1,4-BETA-XYLANASE Y;
COMPND 3 SYNONYM: XYLANASE Y, XYLY, 1,4-BETA-D-XYLAN
COMPND 4 XYLANOHYDROLASE Y, XYLANASE XYN10B;
COMPND 5 CHAIN: A, B;
COMPND 6 FRAGMENT: FERULOYL ESTERASE DOMAIN, RESIDUES 792-1077;
COMPND 7 EC: 3.2.1.8;
COMPND 8 MUTATION: YES;
COMPND 9 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 3 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 4 EXPRESSION_SYSTEM_PLASMID: PET22B;
SOURCE 5 ORGANISM_SCIENTIFIC: CLOSTRIDIUM THERMOCELLUM
KEYWDS ESTERASE FAMILY 1, FERULIC ACID, GLYCOSIDASE, HYDROLASE,
KEYWDS 2 REPEAT, XYLAN DEGRADATION, XYLANASE
EXPDTA X-RAY DIFFRACTION
AUTHOR N.TARBOURIECH,J.A.PRATES,C.FONTES,G.J.DAVIES
REVDAT 1 02-FEB-05 1WB4 0
JRNL AUTH N.TARBOURIECH,J.A.PRATES,C.FONTES,G.J.DAVIES
JRNL TITL MOLECULAR DETERMINANTS OF SUBSTRATE SPECIFICITY IN
JRNL TITL 2 THE FERULOYL ESTERASE MODULE OF XYLANASE 10B FROM
JRNL TITL 3 CLOSTRIDIUM THERMOCELLUM
JRNL REF ACTA CRYSTALLOGR.,SECT.D V. 61 194 2005
JRNL REFN ASTM ABCRE6 DK ISSN 0907-4449
REMARK 2
REMARK 2 RESOLUTION. 1.4 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC REFMAC 5.1.24
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) : 79.06
REMARK 3 DATA CUTOFF (SIGMA(F)) : NONE
REMARK 3 COMPLETENESS FOR RANGE (%) : 97.81
REMARK 3 NUMBER OF REFLECTIONS : 146352
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) : 0.11250
REMARK 3 R VALUE (WORKING SET) : 0.11139
REMARK 3 FREE R VALUE : 0.13357
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.0
REMARK 3 FREE R VALUE TEST SET COUNT : 7700
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) : 1.400
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.437
REMARK 3 REFLECTION IN BIN (WORKING SET) : 9869
REMARK 3 BIN R VALUE (WORKING SET) : 0.138
REMARK 3 BIN FREE R VALUE SET COUNT : 533
REMARK 3 BIN FREE R VALUE : 0.160
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 4767
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 94
REMARK 3 SOLVENT ATOMS : 750
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 11.732
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.38
REMARK 3 B22 (A**2) : -0.17
REMARK 3 B33 (A**2) : -0.20
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): 0.039
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.038
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.019
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 0.477
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.981
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.974
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED (A): 5006 ; 0.020 ; 0.021
REMARK 3 BOND LENGTHS OTHERS (A): 4123 ; 0.044 ; 0.020
REMARK 3 BOND ANGLES REFINED (DEGREES): 6799 ; 1.835 ; 1.927
REMARK 3 BOND ANGLES OTHERS (DEGREES): 9685 ; 3.244 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 582 ; 5.906 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): NULL ; NULL ; NULL
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 657 ; 0.141 ; 0.200
REMARK 3 GENERAL PLANES REFINED (A): 5682 ; 0.042 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 1122 ; 0.058 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED (A): 1054 ; 0.275 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): 5210 ; 0.287 ; 0.200
REMARK 3 NON-BONDED TORSION REFINED (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): 2650 ; 0.146 ; 0.200
REMARK 3 H-BOND (X...Y) REFINED (A): 449 ; 0.196 ; 0.200
REMARK 3 SYMMETRY VDW REFINED (A): 17 ; 0.259 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): 31 ; 0.211 ; 0.200
REMARK 3 SYMMETRY H-BOND REFINED (A): 26 ; 0.131 ; 0.200
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED (A**2): 2875 ; 1.823 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE REFINED (A**2): 4659 ; 2.495 ; 2.000
REMARK 3 SIDE-CHAIN BOND REFINED (A**2): 2131 ; 3.215 ; 3.000
REMARK 3 SIDE-CHAIN ANGLE REFINED (A**2): 2138 ; 4.355 ; 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: HYDROGENS HAVE BEEN ADDED IN THE
REMARK 3 RIDING POSITIONS.
REMARK 4
REMARK 4 1WB4 COMPLIES WITH FORMAT V. 2.3, 09-JULY-1998
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY EBI ON 1-NOV-2004.
REMARK 100 THE EBI ID CODE IS EBI-21467.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 13-OCT-2001
REMARK 200 TEMPERATURE (KELVIN) : 100
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 ID14-EH2
REMARK 200 BEAMLINE : ID14-EH2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.934
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : QUANTUM 4
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 : 157644
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.40
REMARK 200 RESOLUTION RANGE LOW (A) : 20.00
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.0
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.0
REMARK 200 DATA REDUNDANCY : 5.4
REMARK 200 R MERGE (I) : 0.04
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 35.00
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 (%) : 93.3
REMARK 200 DATA REDUNDANCY IN SHELL : 4.2
REMARK 200 R MERGE FOR SHELL (I) : 0.23
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 7.20
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: NULL
REMARK 200 STARTING MODEL: PDB ENTRY 1GKL
REMARK 200
REMARK 200 REMARK: NONE
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: NA ACETATE 1M CD ACETATE 50 MM
REMARK 280 GLYCEROL 5% HEPES PH 7.5 100 MM
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 32.53300
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 56.59000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 54.20250
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 56.59000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 32.53300
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 54.20250
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 ENGINEERED MUTATION IN CHAIN A, SER 954 TO ALA
REMARK 400 ENGINEERED MUTATION IN CHAIN B, SER 954 TO ALA
REMARK 400 CATALYTIC ACTIVITY: ENDOHYDROLYSIS OF 1,4-BETA-D-XYLOSIDIC
REMARK 400 LINKAGES IN XYLANS.
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: 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: ENGH AND HUBER, 1991
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 HIS B1076 CB - CG - CD2 ANGL. DEV. = -11.7 DEGREES
REMARK 500 HIS B1076 CB - CG - ND1 ANGL. DEV. = 10.3 DEGREES
REMARK 500
REMARK 500 REMARK: NULL
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 OH TYR A 819 OE2 GLU A 892 1.84
REMARK 500 OE2 GLU A 892 OH TYR A 819 1.84
REMARK 500 OH TYR B 819 OE2 GLU B 892 2.01
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 ALA A 954 -116.71 65.96
REMARK 500 ALA B 954 -117.45 67.22
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 96.5
REMARK 600 3 GLU 1017B OE1 109.0 90.9
REMARK 600 4 GLU 1017B OE2 155.2 100.1 52.8
REMARK 600 5 HOH 168Z O 128.3 89.8 122.2 70.3
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 54.2
REMARK 600 3 GLU 894A OE2 117.5 170.3
REMARK 600 4 HIS 1076A ND1 97.4 97.5 88.3
REMARK 600 5 HIS 1083A ND1 89.2 89.5 85.2 172.3
REMARK 600 6 HIS 1085A NE2 141.5 87.5 101.0 82.8 94.5
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 103.4
REMARK 600 3 HOH 358Y O 90.2 138.9
REMARK 600 4 HOH 269Z O 100.6 102.3 36.6
REMARK 600 5 GLU 1007A OE1 154.6 92.0 91.2 95.5
REMARK 600 6 GLU 1007A OE2 100.8 118.9 95.6 126.8 53.9
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 229Z O 91.1
REMARK 600 3 HOH 348Z O 177.3 90.5
REMARK 600 4 HIS 1080A NE2 89.3 104.1 88.3
REMARK 600 5 HOH 340Z O 93.3 159.1 85.9 96.3
REMARK 600 1 2 3 4
REMARK 600
REMARK 600 FOR METAL ATOM CD CD A2094 THE COORDINATION ANGLES ARE:
REMARK 600 1 HOH 353Z O
REMARK 600 2 HIS 1081A ND1 101.1
REMARK 600 1
REMARK 600
REMARK 600 FOR METAL ATOM CD CD A2095 THE COORDINATION ANGLES ARE:
REMARK 600 1 ACY 2089A O
REMARK 600 2 ACY 2089A OXT 52.2
REMARK 600 3 HOH 373Z O 132.9 81.0
REMARK 600 1 2
REMARK 600
REMARK 600 FOR METAL ATOM CD CD A2096 THE COORDINATION ANGLES ARE:
REMARK 600 1 HIS 1076A O
REMARK 600 2 HOH 339Z O 101.7
REMARK 600 3 HOH 345Z O 87.9 169.3
REMARK 600 4 HOH 335Z O 98.4 97.1 85.9
REMARK 600 5 HOH 341Z O 84.7 78.3 98.2 174.9
REMARK 600 1 2 3 4
REMARK 600
REMARK 600 FOR METAL ATOM CD CD A2097 THE COORDINATION ANGLES ARE:
REMARK 600 1 HOH 213Z O
REMARK 600 2 GLU 926A O 86.8
REMARK 600 3 TYR 929A O 171.3 85.0
REMARK 600 4 HOH 204Z O 93.9 110.0 91.5
REMARK 600 5 HOH 208Z O 79.3 164.7 108.5 77.5
REMARK 600 6 HOH 214Z O 88.3 89.8 88.8 160.2 83.6
REMARK 600 1 2 3 4 5
REMARK 600
REMARK 600 FOR METAL ATOM CD CD A2098 THE COORDINATION ANGLES ARE:
REMARK 600 1 ASN 985A O
REMARK 600 2 HOH 233Y O 78.0
REMARK 600 3 HOH 96Y O 176.4 99.3
REMARK 600 4 HOH 240Z O 92.5 102.2 85.8
REMARK 600 1 2 3
REMARK 600
REMARK 600 FOR METAL ATOM CD CD A2099 THE COORDINATION ANGLES ARE:
REMARK 600 1 HOH 372Y O
REMARK 600 2 HOH 211Y O 88.7
REMARK 600 3 HOH 204Z O 78.7 101.4
REMARK 600 4 HOH 208Z O 152.3 89.1 74.7
REMARK 600 5 HOH 213Z O 106.6 162.3 90.4 81.3
REMARK 600 6 HOH 217Z O 103.8 81.4 176.4 103.2 86.3
REMARK 600 1 2 3 4 5
REMARK 600
REMARK 600 FOR METAL ATOM CD CD B2092 THE COORDINATION ANGLES ARE:
REMARK 600 1 GLU 1017A OE1
REMARK 600 2 GLU 1017A OE2 53.5
REMARK 600 3 CYS 823B SG 106.9 153.4
REMARK 600 4 HIS 886B ND1 90.6 102.1 95.3
REMARK 600 5 HOH 160Y O 125.9 73.6 126.9 90.2
REMARK 600 1 2 3 4
REMARK 600
REMARK 600 FOR METAL ATOM CD CD B2093 THE COORDINATION ANGLES ARE:
REMARK 600 1 GLU 1079B OE1
REMARK 600 2 GLU 1079B OE2 55.6
REMARK 600 3 GLU 894B OE2 122.0 172.1
REMARK 600 4 HIS 1076B ND1 99.4 103.3 84.4
REMARK 600 5 HIS 1083B ND1 88.5 86.7 85.7 169.7
REMARK 600 6 HIS 1085B NE2 140.3 85.0 97.7 83.5 94.8
REMARK 600 1 2 3 4 5
REMARK 600
REMARK 600 FOR METAL ATOM CD CD B2094 THE COORDINATION ANGLES ARE:
REMARK 600 1 HIS 1082A NE2
REMARK 600 2 HIS 1084A NE2 100.1
REMARK 600 3 GLU 1007B OE1 157.6 91.0
REMARK 600 4 GLU 1007B OE2 103.4 113.9 54.2
REMARK 600 5 HOH 266Y O 103.8 98.5 93.6 132.6
REMARK 600 6 HOH 357Z O 91.6 142.3 91.3 97.7 43.8
REMARK 600 1 2 3 4 5
REMARK 600
REMARK 600 FOR METAL ATOM CD CD B2095 THE COORDINATION ANGLES ARE:
REMARK 600 1 HOH 348Y O
REMARK 600 2 HIS 947B NE2 179.1
REMARK 600 3 HIS 1080B NE2 89.0 90.1
REMARK 600 4 HOH 219Y O 88.7 91.7 104.4
REMARK 600 5 HOH 220Y O 65.7 115.1 152.2 87.3
REMARK 600 6 HOH 339Y O 86.3 93.7 100.3 154.8 68.1
REMARK 600 1 2 3 4 5
REMARK 600
REMARK 600 FOR METAL ATOM CD CD B2096 THE COORDINATION ANGLES ARE:
REMARK 600 1 HOH 360Y O
REMARK 600 2 HIS 1081B ND1 120.5
REMARK 600 3 HOH 352Y O 120.4 113.3
REMARK 600 4 HOH 354Y O 63.4 103.4 81.5
REMARK 600 1 2 3
REMARK 600
REMARK 600 FOR METAL ATOM CD CD B2097 THE COORDINATION ANGLES ARE:
REMARK 600 1 HOH 375Y O
REMARK 600 2 ACY 2091B C 96.5
REMARK 600 3 ACY 2091B O 108.5 27.3
REMARK 600 4 ACY 2091B OXT 82.8 27.3 54.6
REMARK 600 5 HOH 352Y O 85.2 178.0 152.9 152.4
REMARK 600 1 2 3 4
REMARK 600
REMARK 600 FOR METAL ATOM CD CD B2098 THE COORDINATION ANGLES ARE:
REMARK 600 1 HOH 205Z O
REMARK 600 2 GOL 2088B O2 94.8
REMARK 600 3 GOL 2088B O3 87.2 70.3
REMARK 600 4 ALA 933B O 91.6 173.2 112.2
REMARK 600 5 HOH 200Y O 88.9 79.9 149.4 98.2
REMARK 600 6 HOH 201Y O 168.7 83.8 81.8 90.3 101.9
REMARK 600 1 2 3 4 5
REMARK 600
REMARK 600 FOR METAL ATOM CD CD B2099 THE COORDINATION ANGLES ARE:
REMARK 600 1 HIS 1076B O
REMARK 600 2 HOH 336Y O 97.1
REMARK 600 3 HOH 340Y O 101.0 98.3
REMARK 600 4 HOH 341Y O 90.1 86.8 167.1
REMARK 600 5 HOH 343Y O 86.2 174.4 85.4 88.8
REMARK 600 1 2 3 4
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 SITE_DESCRIPTION: SXX BINDING SITE FOR CHAIN A
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 SITE_DESCRIPTION: SXX BINDING SITE FOR CHAIN B
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 SITE_DESCRIPTION: GOL BINDING SITE FOR CHAIN B
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 SITE_DESCRIPTION: GOL BINDING SITE FOR CHAIN A
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 SITE_DESCRIPTION: GOL BINDING SITE FOR CHAIN B
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 SITE_DESCRIPTION: GOL BINDING SITE FOR CHAIN A
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 SITE_DESCRIPTION: GOL BINDING SITE FOR CHAIN B
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 SITE_DESCRIPTION: GOL BINDING SITE FOR CHAIN B
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 SITE_DESCRIPTION: ACY BINDING SITE FOR CHAIN B
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 SITE_DESCRIPTION: ACY BINDING SITE FOR CHAIN A
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 SITE_DESCRIPTION: CD BINDING SITE FOR CHAIN B
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 SITE_DESCRIPTION: CD BINDING SITE FOR CHAIN B
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 SITE_DESCRIPTION: CD BINDING SITE FOR CHAIN B
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC5
REMARK 800 SITE_DESCRIPTION: CD BINDING SITE FOR CHAIN B
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC6
REMARK 800 SITE_DESCRIPTION: CD BINDING SITE FOR CHAIN A
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC7
REMARK 800 SITE_DESCRIPTION: CD BINDING SITE FOR CHAIN A
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC8
REMARK 800 SITE_DESCRIPTION: CD BINDING SITE FOR CHAIN A
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC9
REMARK 800 SITE_DESCRIPTION: CD BINDING SITE FOR CHAIN A
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC1
REMARK 800 SITE_DESCRIPTION: CD BINDING SITE FOR CHAIN A
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC2
REMARK 800 SITE_DESCRIPTION: CD BINDING SITE FOR CHAIN B
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC3
REMARK 800 SITE_DESCRIPTION: CD BINDING SITE FOR CHAIN A
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC4
REMARK 800 SITE_DESCRIPTION: CD BINDING SITE FOR CHAIN B
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC5
REMARK 800 SITE_DESCRIPTION: CD BINDING SITE FOR CHAIN B
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC6
REMARK 800 SITE_DESCRIPTION: CD BINDING SITE FOR CHAIN B
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC7
REMARK 800 SITE_DESCRIPTION: CD BINDING SITE FOR CHAIN A
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC8
REMARK 800 SITE_DESCRIPTION: CD BINDING SITE FOR CHAIN A
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC9
REMARK 800 SITE_DESCRIPTION: CD BINDING SITE FOR CHAIN A
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC1
REMARK 800 SITE_DESCRIPTION: CD BINDING SITE FOR CHAIN A
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: 1GKL RELATED DB: PDB
REMARK 900 S954A MUTANT OF THE FERULOYL ESTERASE MODULE
REMARK 900 FROM CLOSTRIDIUM THERMOCELLUM COMPLEXED WITH
REMARK 900 FERULIC ACID
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: 1OHZ RELATED DB: PDB
REMARK 900 COHESIN-DOCKERIN COMPLEX FROM THE CELLULOSOME
REMARK 900 OF CLOSTRIDIUM THERMOCELLUM
REMARK 900 RELATED ID: 1WB5 RELATED DB: PDB
REMARK 900 S954A MUTANT OF THE FERULOYL ESTERASE MODULE FROM
REMARK 900 CLOSTRIDIUM THERMOCELLUM COMPLEXED WITH SYRINGATE
REMARK 900 RELATED ID: 1WB6 RELATED DB: PDB
REMARK 900 S954A MUTANT OF THE FERULOYL ESTERASE MODULE FROM
REMARK 900 CLOSTRIDIUM THERMOCELLUM COMPLEXED WITH VANILLATE
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 ONLY THE FERULOYL ESTERASE DOMAIN WAS SUBCLONED. S954A
REMARK 999 MUTANT. THE SEQUENCE CONFLICTS (RESIDUES 1017 AND 1018) ARE
REMARK 999 DUE TO ERRORS IN THE UNIPROT ENTRY FROM THE ORIGINAL
REMARK 999 SEQUENCING OF THE PROTEIN.
DBREF 1WB4 A 789 791 PDB 1WB4 1WB4 789 791
DBREF 1WB4 A 792 1077 UNP P51584 XYNY_CLOTM 792 1077
DBREF 1WB4 A 1078 1085 PDB 1WB4 1WB4 1078 1085
DBREF 1WB4 B 789 791 PDB 1WB4 1WB4 789 791
DBREF 1WB4 B 792 1077 UNP P51584 XYNY_CLOTM 792 1077
DBREF 1WB4 B 1078 1085 PDB 1WB4 1WB4 1078 1085
SEQADV 1WB4 ALA A 954 UNP P51584 SER 954 ENGINEERED MUTATION
SEQADV 1WB4 GLU A 1017 UNP P51584 ASP 1017 CONFLICT SEE REMARK 999
SEQADV 1WB4 ASP A 1018 UNP P51584 HIS 1018 CONFLICT SEE REMARK 999
SEQADV 1WB4 ALA B 954 UNP P51584 SER 954 ENGINEERED MUTATION
SEQADV 1WB4 GLU B 1017 UNP P51584 ASP 1017 CONFLICT SEE REMARK 999
SEQADV 1WB4 ASP B 1018 UNP P51584 HIS 1018 CONFLICT SEE REMARK 999
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 SXX A2086 16
HET SXX B2086 16
HET GOL B2087 6
HET GOL A2087 6
HET GOL B2088 6
HET GOL A2088 6
HET GOL B2089 6
HET GOL B2090 6
HET ACY B2091 4
HET ACY A2089 4
HET CD B2092 1
HET CD B2093 1
HET CD B2094 1
HET CD B2095 1
HET CD A2090 1
HET CD A2091 1
HET CD A2092 1
HET CD A2093 1
HET CD A2094 1
HET CD B2096 1
HET CD A2095 1
HET CD B2097 1
HET CD B2098 1
HET CD B2099 1
HET CD A2096 1
HET CD A2097 1
HET CD A2099 1
HET CD A2098 1
HETNAM CD CADMIUM ION
HETNAM ACY ACETIC ACID
HETNAM GOL GLYCEROL
HETNAM SXX SINAPINATE
FORMUL 3 CD 18(CD1 2+)
FORMUL 4 ACY 2(C2 H4 O2)
FORMUL 5 GOL 6(C3 H8 O3)
FORMUL 6 SXX 2(C11 H12 O5)
FORMUL 7 HOH *750(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 SER B 944 1 8
HELIX 17 17 ALA B 954 LEU B 968 1 15
HELIX 18 18 SER B 986 GLY B 1002 1 17
HELIX 19 19 ALA B 1020 ALA B 1033 1 14
HELIX 20 20 TRP B 1059 LEU B 1071 1 13
HELIX 21 21 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 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 CD CD A2090 SG CYS A 823 1555 1555
LINK CD CD A2090 ND1 HIS A 886 1555 1555
LINK CD CD A2090 OE1 GLU B1017 1555 2574
LINK CD CD A2090 OE2 GLU B1017 1555 2574
LINK CD CD A2090 O HOH Z 168 1555 1555
LINK CD CD A2091 OE1 GLU A1079 1555 1555
LINK CD CD A2091 OE2 GLU A1079 1555 1555
LINK CD CD A2091 OE2 GLU A 894 1555 1555
LINK CD CD A2091 ND1 HIS A1076 1555 1555
LINK CD CD A2091 ND1 HIS A1083 1555 1555
LINK CD CD A2091 NE2 HIS A1085 1555 1555
LINK CD CD A2092 NE2 HIS B1082 1555 1655
LINK CD CD A2092 NE2 HIS B1084 1555 1655
LINK CD CD A2092 O HOH Y 358 1555 1555
LINK CD CD A2092 O HOH Z 269 1555 1555
LINK CD CD A2092 OE1 GLU A1007 1555 1555
LINK CD CD A2092 OE2 GLU A1007 1555 1555
LINK CD CD A2093 NE2 HIS A 947 1555 1555
LINK CD CD A2093 O HOH Z 229 1555 1555
LINK CD CD A2093 O HOH Z 348 1555 1555
LINK CD CD A2093 NE2 HIS A1080 1555 1555
LINK CD CD A2093 O HOH Z 340 1555 1555
LINK CD CD A2094 O HOH Z 353 1555 1555
LINK CD CD A2094 ND1 HIS A1081 1555 1555
LINK CD CD A2095 O ACY A2089 1555 1555
LINK CD CD A2095 OXT ACY A2089 1555 1555
LINK CD CD A2095 O HOH Z 373 1555 1555
LINK CD CD A2096 O HIS A1076 1555 1555
LINK CD CD A2096 O HOH Z 339 1555 1555
LINK CD CD A2096 O HOH Z 345 1555 1555
LINK CD CD A2096 O HOH Z 335 1555 1555
LINK CD CD A2096 O HOH Z 341 1555 1555
LINK CD CD A2097 O HOH Z 213 1555 1555
LINK CD CD A2097 O GLU A 926 1555 1555
LINK CD CD A2097 O TYR A 929 1555 1555
LINK CD CD A2097 O HOH Z 204 1555 1555
LINK CD CD A2097 O HOH Z 208 1555 1555
LINK CD CD A2097 O HOH Z 214 1555 1555
LINK CD CD A2098 O ASN A 985 1555 1555
LINK CD CD A2098 O HOH Y 233 1555 1555
LINK CD CD A2098 O HOH Y 96 1555 1555
LINK CD CD A2098 O HOH Z 240 1555 1555
LINK CD CD A2099 O HOH Y 372 1555 1555
LINK CD CD A2099 O HOH Y 211 1555 1555
LINK CD CD A2099 O HOH Z 204 1555 4465
LINK CD CD A2099 O HOH Z 208 1555 4465
LINK CD CD A2099 O HOH Z 213 1555 4465
LINK CD CD A2099 O HOH Z 217 1555 4465
LINK CD CD B2092 OE2 GLU A1017 1555 3545
LINK CD CD B2092 SG CYS B 823 1555 1555
LINK CD CD B2092 ND1 HIS B 886 1555 1555
LINK CD CD B2092 O HOH Y 160 1555 1555
LINK CD CD B2092 OE1 GLU A1017 1555 3545
LINK CD CD B2093 OE2 GLU B1079 1555 1555
LINK CD CD B2093 OE2 GLU B 894 1555 1555
LINK CD CD B2093 ND1 HIS B1076 1555 1555
LINK CD CD B2093 ND1 HIS B1083 1555 1555
LINK CD CD B2093 NE2 HIS B1085 1555 1555
LINK CD CD B2093 OE1 GLU B1079 1555 1555
LINK CD CD B2094 NE2 HIS A1084 1555 1455
LINK CD CD B2094 OE1 GLU B1007 1555 1555
LINK CD CD B2094 OE2 GLU B1007 1555 1555
LINK CD CD B2094 O HOH Y 266 1555 1555
LINK CD CD B2094 O HOH Z 357 1555 1555
LINK CD CD B2094 NE2 HIS A1082 1555 1455
LINK CD CD B2095 NE2 HIS B 947 1555 1555
LINK CD CD B2095 NE2 HIS B1080 1555 1555
LINK CD CD B2095 O HOH Y 219 1555 1555
LINK CD CD B2095 O HOH Y 220 1555 1555
LINK CD CD B2095 O HOH Y 339 1555 1555
LINK CD CD B2095 O HOH Y 348 1555 1555
LINK CD CD B2096 ND1 HIS B1081 1555 1555
LINK CD CD B2096 O HOH Y 352 1555 1555
LINK CD CD B2096 O HOH Y 354 1555 1555
LINK CD CD B2096 O HOH Y 360 1555 1555
LINK CD CD B2097 C ACY B2091 1555 1555
LINK CD CD B2097 O ACY B2091 1555 1555
LINK CD CD B2097 OXT ACY B2091 1555 1555
LINK CD CD B2097 O HOH Y 352 1555 1555
LINK CD CD B2097 O HOH Y 375 1555 1555
LINK CD CD B2098 O2 GOL B2088 1555 1555
LINK CD CD B2098 O3 GOL B2088 1555 1555
LINK CD CD B2098 O ALA B 933 1555 1555
LINK CD CD B2098 O HOH Y 200 1555 1555
LINK CD CD B2098 O HOH Y 201 1555 1555
LINK CD CD B2098 O HOH Z 205 1555 4465
LINK CD CD B2099 O HOH Y 336 1555 1555
LINK CD CD B2099 O HOH Y 340 1555 1555
LINK CD CD B2099 O HOH Y 341 1555 1555
LINK CD CD B2099 O HOH Y 343 1555 1555
LINK CD CD B2099 O HIS B1076 1555 1555
SITE 1 AC1 11 ALA A 954 MET A 955 LEU A 958 GLY A 979
SITE 2 AC1 11 ASP A 980 TRP A 982 ALA A1020 ASN A1023
SITE 3 AC1 11 HOH Z 283 HOH Z 369 HOH Z 370
SITE 1 AC2 9 MET B 955 LEU B 958 GLY B 979 ASP B 980
SITE 2 AC2 9 TRP B 982 ALA B1020 ASN B1023 HOH Y 369
SITE 3 AC2 9 HOH Y 370
SITE 1 AC3 8 GLY B 865 GLY B 866 GLU B 868 PHE B 953
SITE 2 AC3 8 ALA B 954 HIS B1058 HOH Y 370 HOH Y 371
SITE 1 AC4 8 GLY A 865 GLY A 866 GLU A 868 PHE A 953
SITE 2 AC4 8 ALA A 954 HIS A1058 HOH Z 370 HOH Z 371
SITE 1 AC5 10 SER A 927 LYS A 928 GLU B 926 SER B 927
SITE 2 AC5 10 LYS B 928 TYR B 929 SER B 930 HOH Y 198
SITE 3 AC5 10 HOH Y 199 HOH Y 372
SITE 1 AC6 8 LYS A 856 TYR A 857 ASN A 858 GLU A 894
SITE 2 AC6 8 PRO A 895 TYR A 932 HIS A1081 HOH Z 372
SITE 1 AC7 8 ILE A 837 ASN A 838 ASN A 907 ASN A 912
SITE 2 AC7 8 GLN B 915 ASN B 966 HOH Y 186 HOH Y 373
SITE 1 AC8 7 LYS B 856 TYR B 857 ASN B 858 GLU B 894
SITE 2 AC8 7 PRO B 895 TYR B 932 HIS B1081
SITE 1 AC9 6 LYS B 856 TYR B 857 HIS B1081 HOH Y 112
SITE 2 AC9 6 HOH Y 374 HOH Y 375
SITE 1 BC1 5 LYS A 856 TYR A 857 HIS A1081 HOH Z 374
SITE 2 BC1 5 HOH Z 375
SITE 1 BC2 5 GLU A1017 CYS B 823 HIS B 886 MET B 889
SITE 2 BC2 5 HOH Y 160
SITE 1 BC3 5 GLU B 894 HIS B1076 GLU B1079 HIS B1083
SITE 2 BC3 5 HIS B1085
SITE 1 BC4 5 HIS A1082 HIS A1084 GLU B1007 HOH Y 266
SITE 2 BC4 5 HOH Z 357
SITE 1 BC5 6 HIS B 947 HIS B1080 HOH Y 219 HOH Y 220
SITE 2 BC5 6 HOH Y 339 HOH Y 348
SITE 1 BC6 5 CYS A 823 HIS A 886 MET A 889 GLU B1017
SITE 2 BC6 5 HOH Z 168
SITE 1 BC7 5 GLU A 894 HIS A1076 GLU A1079 HIS A1083
SITE 2 BC7 5 HIS A1085
SITE 1 BC8 5 GLU A1007 HIS B1082 HIS B1084 HOH Y 358
SITE 2 BC8 5 HOH Z 269
SITE 1 BC9 5 HIS A 947 HIS A1080 HOH Z 229 HOH Z 340
SITE 2 BC9 5 HOH Z 348
SITE 1 CC1 3 HIS A1081 HOH Z 353 HOH Z 358
SITE 1 CC2 4 HIS B1081 HOH Y 352 HOH Y 354 HOH Y 360
SITE 1 CC3 2 HIS A1081 HOH Z 373
SITE 1 CC4 3 HIS B1081 HOH Y 352 HOH Y 375
SITE 1 CC5 4 ALA B 933 HOH Y 200 HOH Y 201 HOH Z 205
SITE 1 CC6 5 HIS B1076 HOH Y 336 HOH Y 340 HOH Y 341
SITE 2 CC6 5 HOH Y 343
SITE 1 CC7 5 HIS A1076 HOH Z 335 HOH Z 339 HOH Z 341
SITE 2 CC7 5 HOH Z 345
SITE 1 CC8 6 GLU A 926 TYR A 929 HOH Z 204 HOH Z 208
SITE 2 CC8 6 HOH Z 213 HOH Z 214
SITE 1 CC9 6 HOH Y 211 HOH Y 372 HOH Z 204 HOH Z 208
SITE 2 CC9 6 HOH Z 213 HOH Z 217
SITE 1 DC1 4 ASN A 985 HOH Y 96 HOH Y 233 HOH Z 240
CRYST1 65.066 108.405 113.180 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 0.015369 0.000000 0.000000 0.00000
SCALE2 0.000000 0.009225 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008835 0.00000
MASTER 582 0 28 21 16 0 53 6 5611 2 173 46
END |