HEADER HYDROLASE 05-NOV-14 4WVC
TITLE CRYSTAL STRUCTURE OF GH63 MANNOSYLGLYCERATE HYDROLASE FROM THERMUS
TITLE 2 THERMOPHILUS HB8 IN COMPLEX WITH TRIS AND D-GLYCERATE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: UNCHARACTERIZED PROTEIN;
COMPND 3 CHAIN: A, B;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: THERMUS THERMOPHILUS HB8;
SOURCE 3 ORGANISM_TAXID: 300852;
SOURCE 4 GENE: TTHA0978;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PET-11A
KEYWDS HYDROLASE, GH63, (ALPHA/ALPHA)6-BARREL
EXPDTA X-RAY DIFFRACTION
AUTHOR T.MIYAZAKI,M.ICHIKAWA,A.NISHIKAWA,T.TONOZUKA
REVDAT 4 20-MAR-24 4WVC 1 REMARK
REVDAT 3 05-FEB-20 4WVC 1 SOURCE JRNL REMARK
REVDAT 2 22-APR-15 4WVC 1 JRNL
REVDAT 1 11-MAR-15 4WVC 0
JRNL AUTH T.MIYAZAKI,M.ICHIKAWA,H.IINO,A.NISHIKAWA,T.TONOZUKA
JRNL TITL CRYSTAL STRUCTURE AND SUBSTRATE-BINDING MODE OF GH63
JRNL TITL 2 MANNOSYLGLYCERATE HYDROLASE FROM THERMUS THERMOPHILUS HB8.
JRNL REF J.STRUCT.BIOL. V. 190 21 2015
JRNL REFN ESSN 1095-8657
JRNL PMID 25712767
JRNL DOI 10.1016/J.JSB.2015.02.006
REMARK 2
REMARK 2 RESOLUTION. 2.10 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0049
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.10
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 45.15
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 97.5
REMARK 3 NUMBER OF REFLECTIONS : 52252
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) : 0.247
REMARK 3 R VALUE (WORKING SET) : 0.245
REMARK 3 FREE R VALUE : 0.280
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 2809
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.10
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.16
REMARK 3 REFLECTION IN BIN (WORKING SET) : 3662
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 93.60
REMARK 3 BIN R VALUE (WORKING SET) : 0.2960
REMARK 3 BIN FREE R VALUE SET COUNT : 199
REMARK 3 BIN FREE R VALUE : 0.3340
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 6796
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 32
REMARK 3 SOLVENT ATOMS : 265
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 30.16
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.00000
REMARK 3 B22 (A**2) : 0.00000
REMARK 3 B33 (A**2) : 0.00000
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): 0.287
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.222
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): NULL
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): NULL
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.879
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.825
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 7058 ; 0.010 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 6467 ; 0.000 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 9620 ; 1.394 ; 1.947
REMARK 3 BOND ANGLES OTHERS (DEGREES): 14801 ; 3.556 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 818 ; 5.671 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 372 ;33.787 ;22.016
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1049 ;14.946 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 79 ;15.827 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 954 ; 0.128 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 8007 ; 0.006 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 1824 ; 0.008 ; 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): 3286 ; 1.609 ; 2.923
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 3284 ; 1.609 ; 2.922
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 4098 ; 2.515 ; 4.378
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): 4099 ; 2.515 ; 4.378
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 3772 ; 1.678 ; 3.111
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): 3772 ; 1.677 ; 3.111
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): 5522 ; 2.731 ; 4.600
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): 8688 ; 4.909 ;24.088
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): 8628 ; 4.883 ;24.086
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 : BABINET MODEL WITH MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.20
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS
REMARK 4
REMARK 4 4WVC COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 13-NOV-14.
REMARK 100 THE DEPOSITION ID IS D_1000204572.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 14-JUN-13
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 : PHOTON FACTORY
REMARK 200 BEAMLINE : AR-NE3A
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 270
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : SCALEPACK
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 55067
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.100
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 97.6
REMARK 200 DATA REDUNDANCY : 4.600
REMARK 200 R MERGE (I) : 0.11000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 9.3000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.10
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.21
REMARK 200 COMPLETENESS FOR SHELL (%) : 93.6
REMARK 200 DATA REDUNDANCY IN SHELL : 4.20
REMARK 200 R MERGE FOR SHELL (I) : 0.19000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 5.500
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 49.48
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.43
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.4M POTASSIUM SODIUM TARTRATE, 0.1M
REMARK 280 HEPES-NAOH (PH 7.5), 50MM CALCIUM CHLORIDE, 10MM D-GLYCERATE,
REMARK 280 VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 3 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z
REMARK 290 3555 -X+Y,-X,Z
REMARK 290 4555 Y,X,-Z
REMARK 290 5555 X-Y,-Y,-Z
REMARK 290 6555 -X,-X+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 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 4 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 5 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 6 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 6 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
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: TRIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 9200 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 39090 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -7.0 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 350 BIOMT1 2 -0.500000 -0.866025 0.000000 92.94000
REMARK 350 BIOMT2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT1 3 -0.500000 0.866025 0.000000 46.47000
REMARK 350 BIOMT2 3 -0.866025 -0.500000 0.000000 80.48840
REMARK 350 BIOMT3 3 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TRIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 9580 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 39210 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -7.0 KCAL/MOL
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 350 BIOMT1 2 -0.500000 -0.866025 0.000000 92.94000
REMARK 350 BIOMT2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT1 3 -0.500000 0.866025 0.000000 46.47000
REMARK 350 BIOMT2 3 -0.866025 -0.500000 0.000000 80.48840
REMARK 350 BIOMT3 3 0.000000 0.000000 1.000000 0.00000
REMARK 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375 CL CL A 500 LIES ON A SPECIAL POSITION.
REMARK 375 CL CL B 500 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A 621 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A 633 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A 640 LIES ON A SPECIAL POSITION.
REMARK 375 HOH B 638 LIES ON A SPECIAL POSITION.
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 1
REMARK 465 ALA A 2
REMARK 465 GLU A 91
REMARK 465 ALA A 92
REMARK 465 ARG A 93
REMARK 465 ALA A 94
REMARK 465 GLN A 95
REMARK 465 MET B 1
REMARK 465 ALA B 2
REMARK 465 VAL B 87
REMARK 465 TRP B 88
REMARK 465 GLY B 89
REMARK 465 ARG B 90
REMARK 465 GLU B 91
REMARK 465 ALA B 92
REMARK 465 ARG B 93
REMARK 465 ALA B 94
REMARK 465 GLN B 95
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 OE1 GLU A 257 NE ARG B 222 1.97
REMARK 500 OG SER B 336 O PRO B 353 2.14
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 B 633 O HOH B 633 2655 0.70
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 ASP B 278 CB - CG - OD1 ANGL. DEV. = 6.2 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 PRO A 29 32.49 -84.46
REMARK 500 ASP A 47 112.27 -165.55
REMARK 500 ASP A 147 59.36 -141.43
REMARK 500 TYR A 260 -125.01 44.65
REMARK 500 ASP A 338 116.75 -36.70
REMARK 500 TYR A 349 -102.75 71.67
REMARK 500 PRO B 29 32.31 -85.78
REMARK 500 ASP B 47 114.88 -166.56
REMARK 500 TYR B 260 -125.43 48.04
REMARK 500 ASP B 338 115.94 -37.11
REMARK 500 TYR B 349 -102.21 72.75
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL A 500
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue TRS A 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue DGY A 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL B 500
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue TRS B 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue DGY B 502
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2Z07 RELATED DB: PDB
REMARK 900 THE SAME PROTEIN WITHOUT LIGAND AT 2.1-A RESOLUTION
REMARK 900 RELATED ID: 4WVA RELATED DB: PDB
REMARK 900 THE SAME PROTEIN IN COMPLEX WITH TRIS
REMARK 900 RELATED ID: 4WVB RELATED DB: PDB
REMARK 900 THE SAME PROTEIN IN COMPLEX WITH GLUCOSE
DBREF 4WVC A 1 420 UNP Q5SJN0 Q5SJN0_THET8 1 420
DBREF 4WVC B 1 420 UNP Q5SJN0 Q5SJN0_THET8 1 420
SEQRES 1 A 420 MET ALA PRO LEU ARG THR LYS ALA VAL GLU VAL LEU GLN
SEQRES 2 A 420 ARG ASN SER ARG GLY ALA PHE THR VAL PRO ALA HIS GLY
SEQRES 3 A 420 LEU TYR PRO TYR GLN TRP LEU TRP ASP SER ALA PHE ILE
SEQRES 4 A 420 ALA LEU GLY TRP THR GLN VAL ASP TRP GLU ARG ALA TRP
SEQRES 5 A 420 GLN GLU LEU LEU CYS LEU PHE ASP TYR GLY GLN GLY PRO
SEQRES 6 A 420 ASP GLY MET LEU PRO HIS ILE VAL PHE HIS GLU GLN SER
SEQRES 7 A 420 ARG ASP TYR PHE PRO GLY PRO ASP VAL TRP GLY ARG GLU
SEQRES 8 A 420 ALA ARG ALA GLN PRO ALA THR SER GLY ILE THR GLN PRO
SEQRES 9 A 420 PRO VAL VAL ALA THR VAL VAL ARG TYR LEU TYR GLU LYS
SEQRES 10 A 420 ASP PRO ASP ARG ASP ARG ALA ARG GLU ARG ALA ARG TYR
SEQRES 11 A 420 LEU PHE PRO LYS LEU LEU ALA PHE HIS ARG TRP LEU TYR
SEQRES 12 A 420 HIS ALA ARG ASP PRO TYR ARG THR GLY LEU VAL VAL ILE
SEQRES 13 A 420 VAL HIS PRO TRP GLU SER GLY MET ASP ASN SER PRO ALA
SEQRES 14 A 420 TRP ASP LYS PRO LEU SER ARG VAL PRO VAL GLU ASN LEU
SEQRES 15 A 420 PRO PRO TYR GLU ARG ARG ASP VAL LYS HIS VAL ASN PRO
SEQRES 16 A 420 GLU GLU ARG PRO ARG LYS GLU ASP TYR ASP ARG TYR LEU
SEQRES 17 A 420 SER LEU LEU TYR LEU PHE ARG ARG LEU GLU TYR ASP PRO
SEQRES 18 A 420 ARG GLU ILE TYR ARG GLN SER PRO PHE LYS VAL VAL ASP
SEQRES 19 A 420 VAL GLY PHE ASN ALA ILE LEU GLN ARG ALA ASN ARG ASP
SEQRES 20 A 420 LEU TYR ALA LEU ALA VAL LEU LEU GLN GLU ASP PRO TYR
SEQRES 21 A 420 GLU ILE GLU GLU TRP ILE VAL ARG GLY GLU VAL GLY LEU
SEQRES 22 A 420 GLU ALA LEU TRP ASP ARG GLU ALA GLY PHE TYR PHE SER
SEQRES 23 A 420 TRP ASP LEU VAL ALA GLY GLU PRO ILE ALA VAL LYS THR
SEQRES 24 A 420 SER ALA GLY PHE LEU PRO LEU PHE ALA GLY THR PRO HIS
SEQRES 25 A 420 GLN GLY ARG ALA SER LEU LEU ALA GLN GLU ALA GLU ARG
SEQRES 26 A 420 TRP GLY GLU LYS ALA ARG TYR LEU LEU PRO SER VAL ASP
SEQRES 27 A 420 PRO THR SER PRO PHE PHE GLU PRO GLY ARG TYR TRP ARG
SEQRES 28 A 420 GLY PRO VAL TRP ILE ASN VAL ASN TRP MET VAL ALA GLU
SEQRES 29 A 420 GLY PHE ARG ASP TYR GLY PHE ALA ALA LEU ALA ALA ARG
SEQRES 30 A 420 LEU LYS ALA ASP ALA LEU ALA LEU MET GLU ARG GLU GLY
SEQRES 31 A 420 PHE ARG GLU TYR TYR ASP PRO LEU THR GLY GLN GLY ARG
SEQRES 32 A 420 GLY GLY GLU GLY PHE SER TRP SER ALA ALA LEU ALA LEU
SEQRES 33 A 420 PHE TRP THR ARG
SEQRES 1 B 420 MET ALA PRO LEU ARG THR LYS ALA VAL GLU VAL LEU GLN
SEQRES 2 B 420 ARG ASN SER ARG GLY ALA PHE THR VAL PRO ALA HIS GLY
SEQRES 3 B 420 LEU TYR PRO TYR GLN TRP LEU TRP ASP SER ALA PHE ILE
SEQRES 4 B 420 ALA LEU GLY TRP THR GLN VAL ASP TRP GLU ARG ALA TRP
SEQRES 5 B 420 GLN GLU LEU LEU CYS LEU PHE ASP TYR GLY GLN GLY PRO
SEQRES 6 B 420 ASP GLY MET LEU PRO HIS ILE VAL PHE HIS GLU GLN SER
SEQRES 7 B 420 ARG ASP TYR PHE PRO GLY PRO ASP VAL TRP GLY ARG GLU
SEQRES 8 B 420 ALA ARG ALA GLN PRO ALA THR SER GLY ILE THR GLN PRO
SEQRES 9 B 420 PRO VAL VAL ALA THR VAL VAL ARG TYR LEU TYR GLU LYS
SEQRES 10 B 420 ASP PRO ASP ARG ASP ARG ALA ARG GLU ARG ALA ARG TYR
SEQRES 11 B 420 LEU PHE PRO LYS LEU LEU ALA PHE HIS ARG TRP LEU TYR
SEQRES 12 B 420 HIS ALA ARG ASP PRO TYR ARG THR GLY LEU VAL VAL ILE
SEQRES 13 B 420 VAL HIS PRO TRP GLU SER GLY MET ASP ASN SER PRO ALA
SEQRES 14 B 420 TRP ASP LYS PRO LEU SER ARG VAL PRO VAL GLU ASN LEU
SEQRES 15 B 420 PRO PRO TYR GLU ARG ARG ASP VAL LYS HIS VAL ASN PRO
SEQRES 16 B 420 GLU GLU ARG PRO ARG LYS GLU ASP TYR ASP ARG TYR LEU
SEQRES 17 B 420 SER LEU LEU TYR LEU PHE ARG ARG LEU GLU TYR ASP PRO
SEQRES 18 B 420 ARG GLU ILE TYR ARG GLN SER PRO PHE LYS VAL VAL ASP
SEQRES 19 B 420 VAL GLY PHE ASN ALA ILE LEU GLN ARG ALA ASN ARG ASP
SEQRES 20 B 420 LEU TYR ALA LEU ALA VAL LEU LEU GLN GLU ASP PRO TYR
SEQRES 21 B 420 GLU ILE GLU GLU TRP ILE VAL ARG GLY GLU VAL GLY LEU
SEQRES 22 B 420 GLU ALA LEU TRP ASP ARG GLU ALA GLY PHE TYR PHE SER
SEQRES 23 B 420 TRP ASP LEU VAL ALA GLY GLU PRO ILE ALA VAL LYS THR
SEQRES 24 B 420 SER ALA GLY PHE LEU PRO LEU PHE ALA GLY THR PRO HIS
SEQRES 25 B 420 GLN GLY ARG ALA SER LEU LEU ALA GLN GLU ALA GLU ARG
SEQRES 26 B 420 TRP GLY GLU LYS ALA ARG TYR LEU LEU PRO SER VAL ASP
SEQRES 27 B 420 PRO THR SER PRO PHE PHE GLU PRO GLY ARG TYR TRP ARG
SEQRES 28 B 420 GLY PRO VAL TRP ILE ASN VAL ASN TRP MET VAL ALA GLU
SEQRES 29 B 420 GLY PHE ARG ASP TYR GLY PHE ALA ALA LEU ALA ALA ARG
SEQRES 30 B 420 LEU LYS ALA ASP ALA LEU ALA LEU MET GLU ARG GLU GLY
SEQRES 31 B 420 PHE ARG GLU TYR TYR ASP PRO LEU THR GLY GLN GLY ARG
SEQRES 32 B 420 GLY GLY GLU GLY PHE SER TRP SER ALA ALA LEU ALA LEU
SEQRES 33 B 420 PHE TRP THR ARG
HET CL A 500 1
HET TRS A 501 8
HET DGY A 502 7
HET CL B 500 1
HET TRS B 501 8
HET DGY B 502 7
HETNAM CL CHLORIDE ION
HETNAM TRS 2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL
HETNAM DGY (2R)-2,3-DIHYDROXYPROPANOIC ACID
HETSYN TRS TRIS BUFFER
FORMUL 3 CL 2(CL 1-)
FORMUL 4 TRS 2(C4 H12 N O3 1+)
FORMUL 5 DGY 2(C3 H6 O4)
FORMUL 9 HOH *265(H2 O)
HELIX 1 AA1 PRO A 3 SER A 16 1 14
HELIX 2 AA2 LEU A 33 THR A 44 1 12
HELIX 3 AA3 ASP A 47 GLN A 63 1 17
HELIX 4 AA4 GLY A 84 GLY A 89 1 6
HELIX 5 AA5 VAL A 106 ASP A 118 1 13
HELIX 6 AA6 ASP A 120 ASP A 147 1 28
HELIX 7 AA7 HIS A 158 GLY A 163 5 6
HELIX 8 AA8 SER A 167 ALA A 169 5 3
HELIX 9 AA9 TRP A 170 ARG A 176 1 7
HELIX 10 AB1 ARG A 188 VAL A 193 1 6
HELIX 11 AB2 ASN A 194 ARG A 198 5 5
HELIX 12 AB3 ARG A 200 LEU A 217 1 18
HELIX 13 AB4 ASP A 220 SER A 228 1 9
HELIX 14 AB5 ASP A 234 GLN A 256 1 23
HELIX 15 AB6 GLU A 261 LEU A 276 1 16
HELIX 16 AB7 THR A 299 PHE A 303 5 5
HELIX 17 AB8 LEU A 304 GLY A 309 1 6
HELIX 18 AB9 HIS A 312 ALA A 330 1 19
HELIX 19 AC1 TRP A 355 TYR A 369 1 15
HELIX 20 AC2 PHE A 371 GLY A 390 1 20
HELIX 21 AC3 PHE A 408 THR A 419 1 12
HELIX 22 AC4 LEU B 4 SER B 16 1 13
HELIX 23 AC5 LEU B 33 THR B 44 1 12
HELIX 24 AC6 ASP B 47 GLN B 63 1 17
HELIX 25 AC7 VAL B 106 ASP B 118 1 13
HELIX 26 AC8 ASP B 120 ASP B 147 1 28
HELIX 27 AC9 HIS B 158 SER B 162 5 5
HELIX 28 AD1 SER B 167 ALA B 169 5 3
HELIX 29 AD2 TRP B 170 ARG B 176 1 7
HELIX 30 AD3 ARG B 188 VAL B 193 1 6
HELIX 31 AD4 ASN B 194 ARG B 198 5 5
HELIX 32 AD5 ARG B 200 LEU B 217 1 18
HELIX 33 AD6 ASP B 220 SER B 228 1 9
HELIX 34 AD7 ASP B 234 GLN B 256 1 23
HELIX 35 AD8 GLU B 261 LEU B 276 1 16
HELIX 36 AD9 THR B 299 PHE B 303 5 5
HELIX 37 AE1 LEU B 304 GLY B 309 1 6
HELIX 38 AE2 HIS B 312 GLY B 327 1 16
HELIX 39 AE3 TRP B 355 TYR B 369 1 15
HELIX 40 AE4 PHE B 371 GLY B 390 1 20
HELIX 41 AE5 PHE B 408 THR B 419 1 12
SHEET 1 AA1 2 GLN A 31 TRP A 32 0
SHEET 2 AA1 2 ILE A 72 VAL A 73 -1 O VAL A 73 N GLN A 31
SHEET 1 AA2 3 VAL A 232 VAL A 233 0
SHEET 2 AA2 3 TRP A 287 ASP A 288 -1 O TRP A 287 N VAL A 233
SHEET 3 AA2 3 GLU A 293 PRO A 294 -1 O GLU A 293 N ASP A 288
SHEET 1 AA3 2 TRP A 277 ASP A 278 0
SHEET 2 AA3 2 PHE A 283 TYR A 284 -1 O PHE A 283 N ASP A 278
SHEET 1 AA4 2 TYR A 394 TYR A 395 0
SHEET 2 AA4 2 GLY A 402 ARG A 403 -1 O ARG A 403 N TYR A 394
SHEET 1 AA5 2 GLN B 31 TRP B 32 0
SHEET 2 AA5 2 ILE B 72 VAL B 73 -1 O VAL B 73 N GLN B 31
SHEET 1 AA6 3 VAL B 232 VAL B 233 0
SHEET 2 AA6 3 TRP B 287 ASP B 288 -1 O TRP B 287 N VAL B 233
SHEET 3 AA6 3 GLU B 293 PRO B 294 -1 O GLU B 293 N ASP B 288
SHEET 1 AA7 2 TRP B 277 ASP B 278 0
SHEET 2 AA7 2 PHE B 283 TYR B 284 -1 O PHE B 283 N ASP B 278
SHEET 1 AA8 2 TYR B 394 TYR B 395 0
SHEET 2 AA8 2 GLY B 402 ARG B 403 -1 O ARG B 403 N TYR B 394
CISPEP 1 PHE A 82 PRO A 83 0 7.33
CISPEP 2 LEU A 333 LEU A 334 0 12.50
CISPEP 3 PHE B 82 PRO B 83 0 4.76
CISPEP 4 LEU B 333 LEU B 334 0 11.68
SITE 1 AC1 3 HIS A 312 GLN A 313 HOH A 640
SITE 1 AC2 11 TYR A 28 TRP A 32 TRP A 34 ASP A 35
SITE 2 AC2 11 GLN A 103 GLY A 163 TYR A 349 GLU A 393
SITE 3 AC2 11 PHE A 408 TRP A 410 DGY A 502
SITE 1 AC3 9 TRP A 32 HIS A 71 TYR A 81 ASP A 165
SITE 2 AC3 9 ARG A 198 TYR A 349 TRS A 501 HOH A 658
SITE 3 AC3 9 HOH A 692
SITE 1 AC4 3 HIS B 312 GLN B 313 HOH B 638
SITE 1 AC5 11 TYR B 28 TRP B 32 TRP B 34 ASP B 35
SITE 2 AC5 11 GLN B 103 GLY B 163 TYR B 349 TRP B 350
SITE 3 AC5 11 GLU B 393 PHE B 408 DGY B 502
SITE 1 AC6 10 TRP B 32 HIS B 71 TYR B 81 TRP B 160
SITE 2 AC6 10 ASP B 165 ARG B 198 TYR B 204 TYR B 349
SITE 3 AC6 10 TRS B 501 HOH B 664
CRYST1 92.940 92.940 190.401 90.00 90.00 120.00 P 3 2 1 12
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 0.010760 0.006212 0.000000 0.00000
SCALE2 0.000000 0.012424 0.000000 0.00000
SCALE3 0.000000 0.000000 0.005252 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
