HEADER ISOMERASE 03-NOV-10 3PH4
TITLE CLOSTRIDIUM THERMOCELLUM RIBOSE-5-PHOSPHATE ISOMERASE B WITH D-ALLOSE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: RIBOSE-5-PHOSPHATE ISOMERASE;
COMPND 3 CHAIN: A, B;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: CLOSTRIDIUM THERMOCELLUM;
SOURCE 3 ORGANISM_TAXID: 203119;
SOURCE 4 STRAIN: ATCC 27405;
SOURCE 5 GENE: CTHE_2597;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS ALPHA-BETA-ALPHA SANDWICH FOLD, ISOMERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR J.JUNG,J.-K.KIM,S.-J.YEOM,Y.-J.AHN,D.-K.OH,L.-W.KANG
REVDAT 2 01-NOV-23 3PH4 1 REMARK SEQADV
REVDAT 1 13-APR-11 3PH4 0
JRNL AUTH J.JUNG,J.K.KIM,S.J.YEOM,Y.J.AHN,D.K.OH,L.W.KANG
JRNL TITL CRYSTAL STRUCTURE OF CLOSTRIDIUM THERMOCELLUM
JRNL TITL 2 RIBOSE-5-PHOSPHATE ISOMERASE B REVEALS PROPERTIES CRITICAL
JRNL TITL 3 FOR FAST ENZYME KINETICS.
JRNL REF APPL.MICROBIOL.BIOTECHNOL. V. 90 517 2011
JRNL REFN ISSN 0175-7598
JRNL PMID 21253719
JRNL DOI 10.1007/S00253-011-3095-8
REMARK 2
REMARK 2 RESOLUTION. 2.07 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.5.0102
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) : 2.07
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 39.01
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.7
REMARK 3 NUMBER OF REFLECTIONS : 25106
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) : 0.186
REMARK 3 R VALUE (WORKING SET) : 0.184
REMARK 3 FREE R VALUE : 0.220
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 1333
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) : 2.07
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.12
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1839
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 100.0
REMARK 3 BIN R VALUE (WORKING SET) : 0.2510
REMARK 3 BIN FREE R VALUE SET COUNT : 99
REMARK 3 BIN FREE R VALUE : 0.3470
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2244
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 24
REMARK 3 SOLVENT ATOMS : 176
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 33.19
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.01000
REMARK 3 B22 (A**2) : 0.01000
REMARK 3 B33 (A**2) : -0.01000
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): NULL
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.145
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.096
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 3.585
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.959
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.945
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 2298 ; 0.026 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 3082 ; 2.018 ; 1.965
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 294 ; 6.069 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 100 ;36.660 ;23.600
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 408 ;13.749 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 18 ;17.851 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 342 ; 0.160 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 1702 ; 0.009 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
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): 1442 ; 1.194 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 2286 ; 2.082 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 856 ; 3.697 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 796 ; 5.662 ; 4.500
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL
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 : 1.40
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 RIDING
REMARK 3 POSITIONS
REMARK 4
REMARK 4 3PH4 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 14-NOV-10.
REMARK 100 THE DEPOSITION ID IS D_1000062366.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 17-OCT-09
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 : PAL/PLS
REMARK 200 BEAMLINE : 6C1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.24
REMARK 200 MONOCHROMATOR : DOUBLE CRYSTAL MONOCHROMATOR
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 210
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 25673
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.070
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 95.7
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : NULL
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) : 2.20
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.3
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: 3HE8
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 57.65
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.90
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.05M TRIS PH 7.0, 10% PEG 8000, 0.15M
REMARK 280 MAGNESIUM CHLORIDE, 0.2M POTASSIUM CHLORIDE , VAPOR DIFFUSION,
REMARK 280 SITTING DROP, TEMPERATURE 285K, PH 7.5
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 32 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+2/3
REMARK 290 3555 -X+Y,-X,Z+1/3
REMARK 290 4555 Y,X,-Z
REMARK 290 5555 X-Y,-Y,-Z+1/3
REMARK 290 6555 -X,-X+Y,-Z+2/3
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 102.85600
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 51.42800
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 51.42800
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 102.85600
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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 3860 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 11100 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -19.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, 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 MET A -19
REMARK 465 GLY A -18
REMARK 465 SER A -17
REMARK 465 SER A -16
REMARK 465 HIS A -15
REMARK 465 HIS A -14
REMARK 465 HIS A -13
REMARK 465 HIS A -12
REMARK 465 HIS A -11
REMARK 465 HIS A -10
REMARK 465 SER A -9
REMARK 465 SER A -8
REMARK 465 GLY A -7
REMARK 465 LEU A -6
REMARK 465 VAL A -5
REMARK 465 PRO A -4
REMARK 465 ARG A -3
REMARK 465 GLY A -2
REMARK 465 SER A -1
REMARK 465 HIS A 0
REMARK 465 LYS A 149
REMARK 465 MET B -19
REMARK 465 GLY B -18
REMARK 465 SER B -17
REMARK 465 SER B -16
REMARK 465 HIS B -15
REMARK 465 HIS B -14
REMARK 465 HIS B -13
REMARK 465 HIS B -12
REMARK 465 HIS B -11
REMARK 465 HIS B -10
REMARK 465 SER B -9
REMARK 465 SER B -8
REMARK 465 GLY B -7
REMARK 465 LEU B -6
REMARK 465 VAL B -5
REMARK 465 PRO B -4
REMARK 465 ARG B -3
REMARK 465 GLY B -2
REMARK 465 SER B -1
REMARK 465 HIS B 0
REMARK 465 LYS B 149
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 OG SER B 55 O HOH B 233 2.18
REMARK 500 OG SER A 55 O HOH A 218 2.19
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 CYS A 58 CB CYS A 58 SG -0.097
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 CYS A 65 CA - CB - SG ANGL. DEV. = 7.2 DEGREES
REMARK 500 MET A 94 CG - SD - CE ANGL. DEV. = -11.6 DEGREES
REMARK 500 CYS B 65 CA - CB - SG ANGL. DEV. = 7.4 DEGREES
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 AOS A 1655
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE AOS B 1655
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3HE8 RELATED DB: PDB
REMARK 900 APO-STRUCTURE
REMARK 900 RELATED ID: 3HEE RELATED DB: PDB
REMARK 900 COMPLEX STRUCTURE WITH RIBOSE-5-PHOSPHATE
REMARK 900 RELATED ID: 3PH3 RELATED DB: PDB
REMARK 900 COMPLEX STRUCTURE WITH D-RIBOSE
DBREF 3PH4 A 1 149 UNP A3DIL8 A3DIL8_CLOTH 1 149
DBREF 3PH4 B 1 149 UNP A3DIL8 A3DIL8_CLOTH 1 149
SEQADV 3PH4 MET A -19 UNP A3DIL8 EXPRESSION TAG
SEQADV 3PH4 GLY A -18 UNP A3DIL8 EXPRESSION TAG
SEQADV 3PH4 SER A -17 UNP A3DIL8 EXPRESSION TAG
SEQADV 3PH4 SER A -16 UNP A3DIL8 EXPRESSION TAG
SEQADV 3PH4 HIS A -15 UNP A3DIL8 EXPRESSION TAG
SEQADV 3PH4 HIS A -14 UNP A3DIL8 EXPRESSION TAG
SEQADV 3PH4 HIS A -13 UNP A3DIL8 EXPRESSION TAG
SEQADV 3PH4 HIS A -12 UNP A3DIL8 EXPRESSION TAG
SEQADV 3PH4 HIS A -11 UNP A3DIL8 EXPRESSION TAG
SEQADV 3PH4 HIS A -10 UNP A3DIL8 EXPRESSION TAG
SEQADV 3PH4 SER A -9 UNP A3DIL8 EXPRESSION TAG
SEQADV 3PH4 SER A -8 UNP A3DIL8 EXPRESSION TAG
SEQADV 3PH4 GLY A -7 UNP A3DIL8 EXPRESSION TAG
SEQADV 3PH4 LEU A -6 UNP A3DIL8 EXPRESSION TAG
SEQADV 3PH4 VAL A -5 UNP A3DIL8 EXPRESSION TAG
SEQADV 3PH4 PRO A -4 UNP A3DIL8 EXPRESSION TAG
SEQADV 3PH4 ARG A -3 UNP A3DIL8 EXPRESSION TAG
SEQADV 3PH4 GLY A -2 UNP A3DIL8 EXPRESSION TAG
SEQADV 3PH4 SER A -1 UNP A3DIL8 EXPRESSION TAG
SEQADV 3PH4 HIS A 0 UNP A3DIL8 EXPRESSION TAG
SEQADV 3PH4 MET B -19 UNP A3DIL8 EXPRESSION TAG
SEQADV 3PH4 GLY B -18 UNP A3DIL8 EXPRESSION TAG
SEQADV 3PH4 SER B -17 UNP A3DIL8 EXPRESSION TAG
SEQADV 3PH4 SER B -16 UNP A3DIL8 EXPRESSION TAG
SEQADV 3PH4 HIS B -15 UNP A3DIL8 EXPRESSION TAG
SEQADV 3PH4 HIS B -14 UNP A3DIL8 EXPRESSION TAG
SEQADV 3PH4 HIS B -13 UNP A3DIL8 EXPRESSION TAG
SEQADV 3PH4 HIS B -12 UNP A3DIL8 EXPRESSION TAG
SEQADV 3PH4 HIS B -11 UNP A3DIL8 EXPRESSION TAG
SEQADV 3PH4 HIS B -10 UNP A3DIL8 EXPRESSION TAG
SEQADV 3PH4 SER B -9 UNP A3DIL8 EXPRESSION TAG
SEQADV 3PH4 SER B -8 UNP A3DIL8 EXPRESSION TAG
SEQADV 3PH4 GLY B -7 UNP A3DIL8 EXPRESSION TAG
SEQADV 3PH4 LEU B -6 UNP A3DIL8 EXPRESSION TAG
SEQADV 3PH4 VAL B -5 UNP A3DIL8 EXPRESSION TAG
SEQADV 3PH4 PRO B -4 UNP A3DIL8 EXPRESSION TAG
SEQADV 3PH4 ARG B -3 UNP A3DIL8 EXPRESSION TAG
SEQADV 3PH4 GLY B -2 UNP A3DIL8 EXPRESSION TAG
SEQADV 3PH4 SER B -1 UNP A3DIL8 EXPRESSION TAG
SEQADV 3PH4 HIS B 0 UNP A3DIL8 EXPRESSION TAG
SEQRES 1 A 169 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 A 169 LEU VAL PRO ARG GLY SER HIS MET LYS ILE GLY ILE GLY
SEQRES 3 A 169 SER ASP HIS GLY GLY TYR ASN LEU LYS ARG GLU ILE ALA
SEQRES 4 A 169 ASP PHE LEU LYS LYS ARG GLY TYR GLU VAL ILE ASP PHE
SEQRES 5 A 169 GLY THR HIS GLY ASN GLU SER VAL ASP TYR PRO ASP PHE
SEQRES 6 A 169 GLY LEU LYS VAL ALA GLU ALA VAL LYS SER GLY GLU CYS
SEQRES 7 A 169 ASP ARG GLY ILE VAL ILE CYS GLY THR GLY LEU GLY ILE
SEQRES 8 A 169 SER ILE ALA ALA ASN LYS VAL PRO GLY ILE ARG ALA ALA
SEQRES 9 A 169 VAL CYS THR ASN SER TYR MET ALA ARG MET SER ARG GLU
SEQRES 10 A 169 HIS ASN ASP ALA ASN ILE LEU ALA LEU GLY GLU ARG VAL
SEQRES 11 A 169 VAL GLY LEU ASP LEU ALA LEU ASP ILE VAL ASP THR TRP
SEQRES 12 A 169 LEU LYS ALA GLU PHE GLN GLY GLY ARG HIS ALA THR ARG
SEQRES 13 A 169 VAL GLY LYS ILE GLY GLU ILE GLU LYS LYS TYR SER LYS
SEQRES 1 B 169 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 B 169 LEU VAL PRO ARG GLY SER HIS MET LYS ILE GLY ILE GLY
SEQRES 3 B 169 SER ASP HIS GLY GLY TYR ASN LEU LYS ARG GLU ILE ALA
SEQRES 4 B 169 ASP PHE LEU LYS LYS ARG GLY TYR GLU VAL ILE ASP PHE
SEQRES 5 B 169 GLY THR HIS GLY ASN GLU SER VAL ASP TYR PRO ASP PHE
SEQRES 6 B 169 GLY LEU LYS VAL ALA GLU ALA VAL LYS SER GLY GLU CYS
SEQRES 7 B 169 ASP ARG GLY ILE VAL ILE CYS GLY THR GLY LEU GLY ILE
SEQRES 8 B 169 SER ILE ALA ALA ASN LYS VAL PRO GLY ILE ARG ALA ALA
SEQRES 9 B 169 VAL CYS THR ASN SER TYR MET ALA ARG MET SER ARG GLU
SEQRES 10 B 169 HIS ASN ASP ALA ASN ILE LEU ALA LEU GLY GLU ARG VAL
SEQRES 11 B 169 VAL GLY LEU ASP LEU ALA LEU ASP ILE VAL ASP THR TRP
SEQRES 12 B 169 LEU LYS ALA GLU PHE GLN GLY GLY ARG HIS ALA THR ARG
SEQRES 13 B 169 VAL GLY LYS ILE GLY GLU ILE GLU LYS LYS TYR SER LYS
HET AOS A1655 12
HET AOS B1655 12
HETNAM AOS D-ALLOSE
FORMUL 3 AOS 2(C6 H12 O6)
FORMUL 5 HOH *176(H2 O)
HELIX 1 1 GLY A 11 ARG A 25 1 15
HELIX 2 2 ASP A 41 SER A 55 1 15
HELIX 3 3 GLY A 68 ASN A 76 1 9
HELIX 4 4 ASN A 88 HIS A 98 1 11
HELIX 5 5 GLY A 112 ALA A 126 1 15
HELIX 6 6 GLY A 131 SER A 148 1 18
HELIX 7 7 GLY B 11 LYS B 24 1 14
HELIX 8 8 ASP B 41 SER B 55 1 15
HELIX 9 9 GLY B 68 ASN B 76 1 9
HELIX 10 10 ASN B 88 HIS B 98 1 11
HELIX 11 11 GLY B 112 ALA B 126 1 15
HELIX 12 12 GLY B 131 SER B 148 1 18
SHEET 1 A 5 GLU A 28 ASP A 31 0
SHEET 2 A 5 LYS A 2 SER A 7 1 N ILE A 3 O GLU A 28
SHEET 3 A 5 ARG A 60 CYS A 65 1 O ARG A 60 N GLY A 4
SHEET 4 A 5 ILE A 103 GLY A 107 1 O LEU A 104 N VAL A 63
SHEET 5 A 5 ALA A 83 VAL A 85 1 N ALA A 84 O ALA A 105
SHEET 1 B 5 GLU B 28 ASP B 31 0
SHEET 2 B 5 LYS B 2 SER B 7 1 N ILE B 3 O GLU B 28
SHEET 3 B 5 ARG B 60 CYS B 65 1 O ARG B 60 N GLY B 4
SHEET 4 B 5 ILE B 103 GLY B 107 1 O LEU B 104 N VAL B 63
SHEET 5 B 5 ALA B 83 VAL B 85 1 N ALA B 84 O ALA B 105
CISPEP 1 GLY A 33 THR A 34 0 6.99
CISPEP 2 GLY B 33 THR B 34 0 3.39
SITE 1 AC1 13 ASP A 8 HIS A 9 GLY A 10 TYR A 42
SITE 2 AC1 13 GLY A 66 ARG A 109 HOH A 189 HOH A 227
SITE 3 AC1 13 HIS B 98 ARG B 132 ARG B 136 HOH B 178
SITE 4 AC1 13 HOH B 187
SITE 1 AC2 13 HIS A 98 ASN A 99 ARG A 132 ARG A 136
SITE 2 AC2 13 ASP B 8 HIS B 9 GLY B 10 TYR B 42
SITE 3 AC2 13 GLY B 66 THR B 67 ARG B 109 HOH B 175
SITE 4 AC2 13 HOH B 237
CRYST1 69.134 69.134 154.284 90.00 90.00 120.00 P 32 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 0.014465 0.008351 0.000000 0.00000
SCALE2 0.000000 0.016702 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006482 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
