6fj4-pdb | HEADER HYDROLASE 19-JAN-18 6FJ4
TITLE STRUCTURE OF FAE SOLVED BY SAD FROM DATA COLLECTED AT THE PEAK OF THE
TITLE 2 SELENIUM ABSORPTION EDGE ON ID30B
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ENDO-1,4-BETA-XYLANASE Y;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: XYLANASE Y,1,4-BETA-D-XYLAN XYLANOHYDROLASE Y,XYLY;
COMPND 5 EC: 3.2.1.8;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: CLOSTRIDIUM THERMOCELLUM;
SOURCE 3 ORGANISM_COMMON: RUMINICLOSTRIDIUM THERMOCELLUM;
SOURCE 4 ORGANISM_TAXID: 1515;
SOURCE 5 GENE: XYNY;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 511693
KEYWDS HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR A.A.MCCARTHY,C.MUELLER-DIECKMANN
REVDAT 1 07-FEB-18 6FJ4 0
JRNL AUTH A.A.MCCARTHY,R.BARRETT,A.BETEVA,H.CASEROTTO,F.DOBIAS,
JRNL AUTH 2 F.FELISAZ,T.GIRAUD,M.GUIJARRO,A.KHADROUCHE,M.LENTINI,
JRNL AUTH 3 G.A.LEONARD,M.LOPEZ MARRERO,S.MALBET-MONACO,S.MCSWEENEY,
JRNL AUTH 4 D.NURIZZO,G.PAPP,C.ROSSI,J.SINOIR,C.SOREZ,J.SURR,O.SVENSSON,
JRNL AUTH 5 U.ZANDER,F.CIPRIANI,P.THEVENEAU,C.MUELLER-DIECKMANN
JRNL TITL ID30B - A VERSATILE BEAMLINE FOR MACROMOLECULAR
JRNL TITL 2 CRYSTALLOGRAPHY EXPERIMENTS AT THE ESRF.
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 1.70 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0189
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) : 1.70
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 79.21
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.7
REMARK 3 NUMBER OF REFLECTIONS : 43496
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) : 0.161
REMARK 3 R VALUE (WORKING SET) : 0.160
REMARK 3 FREE R VALUE : 0.178
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.400
REMARK 3 FREE R VALUE TEST SET COUNT : 2487
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) : 1.70
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.74
REMARK 3 REFLECTION IN BIN (WORKING SET) : 3195
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.71
REMARK 3 BIN R VALUE (WORKING SET) : 0.3680
REMARK 3 BIN FREE R VALUE SET COUNT : 192
REMARK 3 BIN FREE R VALUE : 0.3810
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2290
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 22
REMARK 3 SOLVENT ATOMS : 194
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 24.20
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 20.91
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.37000
REMARK 3 B22 (A**2) : 0.37000
REMARK 3 B33 (A**2) : -0.73000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.077
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.075
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.059
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 3.498
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.975
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.972
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 2440 ; 0.020 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 2040 ; 0.002 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 3292 ; 1.695 ; 1.940
REMARK 3 BOND ANGLES OTHERS (DEGREES): 4749 ; 1.026 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 292 ; 5.964 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 127 ;36.890 ;23.858
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 324 ;11.160 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 9 ;17.183 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 327 ; 0.109 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 2750 ; 0.009 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 554 ; 0.002 ; 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): 1141 ; 1.035 ; 1.905
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 1140 ; 1.034 ; 1.905
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 1427 ; 1.619 ; 2.851
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): 1428 ; 1.619 ; 2.851
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1291 ; 2.067 ; 2.160
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): 1287 ; 1.917 ; 2.145
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): 1855 ; 2.510 ; 3.120
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): 2657 ; 5.209 ;23.071
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): 2622 ; 5.160 ;22.599
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 : 1.30
REMARK 3 ION PROBE RADIUS : 0.70
REMARK 3 SHRINKAGE RADIUS : 0.70
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS
REMARK 4
REMARK 4 6FJ4 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 19-JAN-18.
REMARK 100 THE DEPOSITION ID IS D_1200008426.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 05-APR-17
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
REMARK 200 BEAMLINE : ID30B
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.979
REMARK 200 MONOCHROMATOR : SI111
REMARK 200 OPTICS : BE CRL (VERTICAL) AND RH
REMARK 200 ELLIPTICAL MIRROR (HORIZONTAL)
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS3 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : AIMLESS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 46013
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.700
REMARK 200 RESOLUTION RANGE LOW (A) : 79.210
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 96.3
REMARK 200 DATA REDUNDANCY : 2.400
REMARK 200 R MERGE (I) : 0.05700
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 11.2000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.70
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.73
REMARK 200 COMPLETENESS FOR SHELL (%) : 96.1
REMARK 200 DATA REDUNDANCY IN SHELL : 2.30
REMARK 200 R MERGE FOR SHELL (I) : 1.39000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 0.900
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD
REMARK 200 SOFTWARE USED: CRANK2
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 61.06
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.16
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M HEPES, 50 MM CDSO4, 5% (V/V)
REMARK 280 GLYCEROL, AND 1 M NA-ACETATE, PH 7.5, VAPOR DIFFUSION, HANGING
REMARK 280 DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 41 21 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z+1/2
REMARK 290 3555 -Y+1/2,X+1/2,Z+1/4
REMARK 290 4555 Y+1/2,-X+1/2,Z+3/4
REMARK 290 5555 -X+1/2,Y+1/2,-Z+1/4
REMARK 290 6555 X+1/2,-Y+1/2,-Z+3/4
REMARK 290 7555 Y,X,-Z
REMARK 290 8555 -Y,-X,-Z+1/2
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 32.93250
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 56.01150
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 56.01150
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 16.46625
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 56.01150
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 56.01150
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 49.39875
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 56.01150
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 56.01150
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 16.46625
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 56.01150
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 56.01150
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 49.39875
REMARK 290 SMTRY1 7 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 7 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 32.93250
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 TOTAL BURIED SURFACE AREA: 1010 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 11780 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -34.0 KCAL/MOL
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 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 2.18
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 O HOH A 1368 O HOH A 1374 8664 1.92
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 RES CSSEQI ATM2 DEVIATION
REMARK 500 GLU A 894 CG GLU A 894 CD 0.092
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 ARG A 828 NE - CZ - NH1 ANGL. DEV. = 3.6 DEGREES
REMARK 500 GLU A 894 OE1 - CD - OE2 ANGL. DEV. = -13.9 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 VAL A 878 -49.84 -130.45
REMARK 500 SEP A 954 -118.55 65.43
REMARK 500 TYR A 983 89.88 -163.26
REMARK 500 THR A1040 149.65 176.60
REMARK 500 ASN A1047 16.04 -151.85
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 CD A1101 CD
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 823 SG
REMARK 620 2 HIS A 886 ND1 93.2
REMARK 620 3 GLU A1017 OE1 102.3 20.8
REMARK 620 4 GLU A1017 OE2 105.8 21.3 3.7
REMARK 620 5 HOH A1206 O 130.5 88.3 68.1 67.0
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CD A1102 CD
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU A 894 OE1
REMARK 620 2 GLU A 894 OE2 51.9
REMARK 620 3 HIS A1076 ND1 90.3 89.1
REMARK 620 4 GLU A1079 OE1 78.3 129.9 97.3
REMARK 620 5 GLU A1079 OE2 135.7 167.2 100.4 57.8
REMARK 620 6 HIS A1083 ND1 86.5 83.4 172.2 89.0 86.7
REMARK 620 7 HIS A1085 NE2 135.9 84.5 81.7 145.6 88.4 95.6
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CD A1104 CD
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 947 NE2
REMARK 620 2 HIS A1080 NE2 95.0
REMARK 620 3 HOH A1372 O 93.1 117.9
REMARK 620 4 HOH A1214 O 86.7 85.2 156.8
REMARK 620 5 HOH A1375 O 99.8 153.8 82.9 74.3
REMARK 620 6 HOH A1377 O 169.2 95.8 80.8 95.4 70.7
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CD A1103 CD
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU A1007 OE1
REMARK 620 2 GLU A1007 OE2 54.3
REMARK 620 3 HOH A1374 O 93.0 130.8
REMARK 620 4 HIS A1082 NE2 83.8 31.6 152.4
REMARK 620 5 HIS A1084 NE2 76.7 26.9 155.0 8.4
REMARK 620 6 HOH A1368 O 89.2 88.6 51.5 101.0 105.0
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 CD A 1101
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CD A 1102
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CD A 1103
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CD A 1104
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CD A 1105
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 1106
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 1107
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 1108
DBREF 6FJ4 A 803 1077 UNP P51584 XYNY_CLOTM 803 1077
SEQADV 6FJ4 GLU A 1017 UNP P51584 ASP 1017 CONFLICT
SEQADV 6FJ4 ASP A 1018 UNP P51584 HIS 1018 CONFLICT
SEQADV 6FJ4 LEU A 1078 UNP P51584 EXPRESSION TAG
SEQADV 6FJ4 GLU A 1079 UNP P51584 EXPRESSION TAG
SEQADV 6FJ4 HIS A 1080 UNP P51584 EXPRESSION TAG
SEQADV 6FJ4 HIS A 1081 UNP P51584 EXPRESSION TAG
SEQADV 6FJ4 HIS A 1082 UNP P51584 EXPRESSION TAG
SEQADV 6FJ4 HIS A 1083 UNP P51584 EXPRESSION TAG
SEQADV 6FJ4 HIS A 1084 UNP P51584 EXPRESSION TAG
SEQADV 6FJ4 HIS A 1085 UNP P51584 EXPRESSION TAG
SEQRES 1 A 283 SER PHE LYS TYR GLU SER ALA VAL GLN TYR ARG PRO ALA
SEQRES 2 A 283 PRO ASP SER TYR LEU ASN PRO CYS PRO GLN ALA GLY ARG
SEQRES 3 A 283 ILE VAL LYS GLU THR TYR THR GLY ILE ASN GLY THR LYS
SEQRES 4 A 283 SER LEU ASN VAL TYR LEU PRO TYR GLY TYR ASP PRO ASN
SEQRES 5 A 283 LYS LYS TYR ASN ILE PHE TYR LEU MSE HIS GLY GLY GLY
SEQRES 6 A 283 GLU ASN GLU ASN THR ILE PHE SER ASN ASP VAL LYS LEU
SEQRES 7 A 283 GLN ASN ILE LEU ASP HIS ALA ILE MSE ASN GLY GLU LEU
SEQRES 8 A 283 GLU PRO LEU ILE VAL VAL THR PRO THR PHE ASN GLY GLY
SEQRES 9 A 283 ASN CYS THR ALA GLN ASN PHE TYR GLN GLU PHE ARG GLN
SEQRES 10 A 283 ASN VAL ILE PRO PHE VAL GLU SER LYS TYR SER THR TYR
SEQRES 11 A 283 ALA GLU SER THR THR PRO GLN GLY ILE ALA ALA SER ARG
SEQRES 12 A 283 MSE HIS ARG GLY PHE GLY GLY PHE SEP MSE GLY GLY LEU
SEQRES 13 A 283 THR THR TRP TYR VAL MSE VAL ASN CYS LEU ASP TYR VAL
SEQRES 14 A 283 ALA TYR PHE MSE PRO LEU SER GLY ASP TYR TRP TYR GLY
SEQRES 15 A 283 ASN SER PRO GLN ASP LYS ALA ASN SER ILE ALA GLU ALA
SEQRES 16 A 283 ILE ASN ARG SER GLY LEU SER LYS ARG GLU TYR PHE VAL
SEQRES 17 A 283 PHE ALA ALA THR GLY SER GLU ASP ILE ALA TYR ALA ASN
SEQRES 18 A 283 MSE ASN PRO GLN ILE GLU ALA MSE LYS ALA LEU PRO HIS
SEQRES 19 A 283 PHE ASP TYR THR SER ASP PHE SER LYS GLY ASN PHE TYR
SEQRES 20 A 283 PHE LEU VAL ALA PRO GLY ALA THR HIS TRP TRP GLY TYR
SEQRES 21 A 283 VAL ARG HIS TYR ILE TYR ASP ALA LEU PRO TYR PHE PHE
SEQRES 22 A 283 HIS GLU LEU GLU HIS HIS HIS HIS HIS HIS
MODRES 6FJ4 MSE A 863 MET MODIFIED RESIDUE
MODRES 6FJ4 MSE A 889 MET MODIFIED RESIDUE
MODRES 6FJ4 MSE A 946 MET MODIFIED RESIDUE
MODRES 6FJ4 SEP A 954 SER MODIFIED RESIDUE
MODRES 6FJ4 MSE A 955 MET MODIFIED RESIDUE
MODRES 6FJ4 MSE A 964 MET MODIFIED RESIDUE
MODRES 6FJ4 MSE A 975 MET MODIFIED RESIDUE
MODRES 6FJ4 MSE A 1024 MET MODIFIED RESIDUE
MODRES 6FJ4 MSE A 1031 MET MODIFIED RESIDUE
HET MSE A 863 8
HET MSE A 889 8
HET MSE A 946 8
HET SEP A 954 10
HET MSE A 955 13
HET MSE A 964 8
HET MSE A 975 8
HET MSE A1024 8
HET MSE A1031 8
HET CD A1101 1
HET CD A1102 1
HET CD A1103 1
HET CD A1104 1
HET CD A1105 1
HET GOL A1106 6
HET GOL A1107 6
HET SO4 A1108 5
HETNAM MSE SELENOMETHIONINE
HETNAM SEP PHOSPHOSERINE
HETNAM CD CADMIUM ION
HETNAM GOL GLYCEROL
HETNAM SO4 SULFATE ION
HETSYN SEP PHOSPHONOSERINE
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 1 MSE 8(C5 H11 N O2 SE)
FORMUL 1 SEP C3 H8 N O6 P
FORMUL 2 CD 5(CD 2+)
FORMUL 7 GOL 2(C3 H8 O3)
FORMUL 9 SO4 O4 S 2-
FORMUL 10 HOH *194(H2 O)
HELIX 1 AA1 PRO A 816 ASN A 821 5 6
HELIX 2 AA2 LYS A 879 ASN A 890 1 12
HELIX 3 AA3 ASN A 912 ASN A 920 1 9
HELIX 4 AA4 ASN A 920 TYR A 929 1 10
HELIX 5 AA5 THR A 937 SER A 944 1 8
HELIX 6 AA6 SEP A 954 LEU A 968 1 15
HELIX 7 AA7 SER A 986 GLY A 1002 1 17
HELIX 8 AA8 ALA A 1020 ALA A 1033 1 14
HELIX 9 AA9 TRP A 1059 LEU A 1071 1 13
HELIX 10 AB1 PRO A 1072 PHE A 1074 5 3
SHEET 1 AA1 8 ARG A 828 GLY A 836 0
SHEET 2 AA1 8 GLY A 839 LEU A 847 -1 O LEU A 847 N ARG A 828
SHEET 3 AA1 8 ILE A 897 THR A 900 -1 O VAL A 898 N TYR A 846
SHEET 4 AA1 8 ILE A 859 MSE A 863 1 N LEU A 862 O VAL A 899
SHEET 5 AA1 8 ARG A 948 PHE A 953 1 O GLY A 951 N TYR A 861
SHEET 6 AA1 8 TYR A 973 LEU A 977 1 O LEU A 977 N GLY A 952
SHEET 7 AA1 8 PHE A1009 GLY A1015 1 O PHE A1011 N PHE A 974
SHEET 8 AA1 8 PHE A1048 ALA A1053 1 O TYR A1049 N ALA A1012
LINK SG CYS A 823 CD CD A1101 1555 1555 2.64
LINK C LEU A 862 N MSE A 863 1555 1555 1.35
LINK C MSE A 863 N HIS A 864 1555 1555 1.34
LINK ND1 HIS A 886 CD CD A1101 1555 1555 2.37
LINK C ILE A 888 N MSE A 889 1555 1555 1.34
LINK C MSE A 889 N ASN A 890 1555 1555 1.33
LINK OE1 GLU A 894 CD CD A1102 1555 1555 2.39
LINK OE2 GLU A 894 CD CD A1102 1555 1555 2.25
LINK C ARG A 945 N MSE A 946 1555 1555 1.35
LINK C MSE A 946 N HIS A 947 1555 1555 1.33
LINK NE2 HIS A 947 CD CD A1104 1555 1555 2.30
LINK C PHE A 953 N SEP A 954 1555 1555 1.34
LINK C SEP A 954 N MSE A 955 1555 1555 1.34
LINK C MSE A 955 N GLY A 956 1555 1555 1.34
LINK C VAL A 963 N MSE A 964 1555 1555 1.33
LINK C MSE A 964 N VAL A 965 1555 1555 1.32
LINK C PHE A 974 N MSE A 975 1555 1555 1.33
LINK C MSE A 975 N PRO A 976 1555 1555 1.35
LINK OE1 GLU A1007 CD CD A1103 1555 1555 2.33
LINK OE2 GLU A1007 CD CD A1103 1555 1555 2.27
LINK C ASN A1023 N MSE A1024 1555 1555 1.33
LINK C MSE A1024 N ASN A1025 1555 1555 1.34
LINK C ALA A1030 N MSE A1031 1555 1555 1.34
LINK C MSE A1031 N LYS A1032 1555 1555 1.34
LINK ND1 HIS A1076 CD CD A1102 1555 1555 2.38
LINK OE1 GLU A1079 CD CD A1102 1555 1555 2.20
LINK OE2 GLU A1079 CD CD A1102 1555 1555 2.28
LINK NE2 HIS A1080 CD CD A1104 1555 1555 2.23
LINK ND1 HIS A1081 CD CD A1105 1555 1555 2.25
LINK ND1 HIS A1083 CD CD A1102 1555 1555 2.36
LINK NE2 HIS A1085 CD CD A1102 1555 1555 2.28
LINK CD CD A1103 O HOH A1374 1555 1555 2.19
LINK CD CD A1104 O HOH A1372 1555 1555 2.17
LINK CD CD A1104 O HOH A1214 1555 1555 2.16
LINK CD CD A1104 O HOH A1375 1555 1555 2.11
LINK CD CD A1104 O HOH A1377 1555 1555 2.48
LINK OE1 GLU A1017 CD CD A1101 1555 3545 2.28
LINK OE2 GLU A1017 CD CD A1101 1555 3545 2.30
LINK NE2 HIS A1082 CD CD A1103 1555 8664 2.26
LINK NE2 HIS A1084 CD CD A1103 1555 8664 2.26
LINK CD CD A1101 O HOH A1206 1555 4554 2.19
LINK CD CD A1103 O HOH A1368 1555 8664 2.23
SITE 1 AC1 5 CYS A 823 HIS A 886 MSE A 889 GLU A1017
SITE 2 AC1 5 HOH A1206
SITE 1 AC2 5 GLU A 894 HIS A1076 GLU A1079 HIS A1083
SITE 2 AC2 5 HIS A1085
SITE 1 AC3 5 GLU A1007 HIS A1082 HIS A1084 HOH A1368
SITE 2 AC3 5 HOH A1374
SITE 1 AC4 6 HIS A 947 HIS A1080 HOH A1214 HOH A1372
SITE 2 AC4 6 HOH A1375 HOH A1377
SITE 1 AC5 3 HIS A1081 SO4 A1108 HOH A1279
SITE 1 AC6 8 ILE A 837 ASN A 838 ASN A 907 ASN A 912
SITE 2 AC6 8 GLN A 915 ARG A 918 ASN A 966 HOH A1204
SITE 1 AC7 6 GLU A 926 SER A 927 LYS A 928 TYR A 929
SITE 2 AC7 6 SER A 930 HOH A1208
SITE 1 AC8 3 LYS A 855 HIS A1081 CD A1105
CRYST1 112.023 112.023 65.865 90.00 90.00 90.00 P 41 21 2 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 0.008927 0.000000 0.000000 0.00000
SCALE2 0.000000 0.008927 0.000000 0.00000
SCALE3 0.000000 0.000000 0.015183 0.00000
TER 2318 HIS A1085
MASTER 427 0 17 10 8 0 14 6 2506 1 138 22
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