HEADER ISOMERASE 08-MAY-09 3HEE
TITLE STRUCTURAL STUDY OF CLOSTRIDIUM THERMOCELLUM RIBOSE-5-PHOSPHATE
TITLE 2 ISOMERASE B AND RIBOSE-5-PHOSPHATE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: RIBOSE-5-PHOSPHATE ISOMERASE;
COMPND 3 CHAIN: A, B;
COMPND 4 EC: 5.3.1.6;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: CLOSTRIDIUM THERMOCELLUM;
SOURCE 3 ORGANISM_TAXID: 203119;
SOURCE 4 GENE: CTHE_2597;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PET 28A(+)
KEYWDS D-RIBOSE PHOSPHATE ISOMERASE, CTRPI B, ISOMERIZATION, RIBOSE-5-
KEYWDS 2 PHOSPHATE, ISOMERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR L.W.KANG,J.K.KIM,J.H.JUNG,M.K.HONG
REVDAT 3 01-NOV-23 3HEE 1 REMARK
REVDAT 2 13-APR-11 3HEE 1 JRNL
REVDAT 1 10-NOV-09 3HEE 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. 2.00 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.2.0019
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) : 2.00
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 33.84
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.2
REMARK 3 NUMBER OF REFLECTIONS : 27713
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) : 0.177
REMARK 3 R VALUE (WORKING SET) : 0.174
REMARK 3 FREE R VALUE : 0.221
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 1487
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) : 2.00
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.05
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1677
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 81.49
REMARK 3 BIN R VALUE (WORKING SET) : 0.2280
REMARK 3 BIN FREE R VALUE SET COUNT : 88
REMARK 3 BIN FREE R VALUE : 0.2460
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 : 28
REMARK 3 SOLVENT ATOMS : 165
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 25.10
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 25.08
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) : -0.01000
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): 0.131
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.134
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.087
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 3.083
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.960
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.934
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 2302 ; 0.032 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 3090 ; 2.192 ; 1.970
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 294 ; 6.036 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 100 ;35.281 ;23.600
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 408 ;13.511 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 18 ;18.438 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 340 ; 0.174 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 1702 ; 0.012 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 1170 ; 0.215 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 1592 ; 0.305 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 166 ; 0.140 ; 0.200
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): 28 ; 0.130 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 13 ; 0.435 ; 0.200
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): 1516 ; 1.620 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 2286 ; 2.241 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 926 ; 4.113 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 804 ; 5.877 ; 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 : 1.20
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 3HEE COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 12-MAY-09.
REMARK 100 THE DEPOSITION ID IS D_1000053031.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 18-DEC-08
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.0
REMARK 200 NUMBER OF CRYSTALS USED : 4
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) : 0.9999
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 210
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : NULL
REMARK 200 DATA SCALING SOFTWARE : NULL
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 29281
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.000
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 1.200
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.3
REMARK 200 DATA REDUNDANCY : 16.30
REMARK 200 R MERGE (I) : 0.09500
REMARK 200 R SYM (I) : 0.09500
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 31.6000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.00
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 50.00
REMARK 200 COMPLETENESS FOR SHELL (%) : 98.3
REMARK 200 DATA REDUNDANCY IN SHELL : 16.30
REMARK 200 R MERGE FOR SHELL (I) : 0.09500
REMARK 200 R SYM FOR SHELL (I) : 0.09500
REMARK 200 <I/SIGMA(I)> FOR SHELL : 31.60
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: SWISS-MODEL
REMARK 200 STARTING MODEL: PDB ENTRY 2VVR
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 62.76
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.30
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.05M TRIS, PH7.0, 10% PEG8000, 0.15M
REMARK 280 MAGNESIUM CHLORIDE, 0.2M POTASSIUM CHLORIDE, VAPOR DIFFUSION,
REMARK 280 HANGING DROP, TEMPERATURE 283K
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 102.37733
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 51.18867
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 51.18867
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 102.37733
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: 5000 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 10680 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 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 HOH A 200 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A 228 LIES ON A SPECIAL POSITION.
REMARK 375 HOH B 194 LIES ON A SPECIAL POSITION.
REMARK 375 HOH B 216 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 LYS A 149
REMARK 465 LYS B 149
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 ALA B 105 CA ALA B 105 CB 0.158
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 A 31 CB - CG - OD1 ANGL. DEV. = 5.7 DEGREES
REMARK 500 ASP A 59 CB - CG - OD1 ANGL. DEV. = -5.4 DEGREES
REMARK 500 ARG A 60 CG - CD - NE ANGL. DEV. = -13.0 DEGREES
REMARK 500 ARG A 96 NE - CZ - NH2 ANGL. DEV. = -3.5 DEGREES
REMARK 500 LYS B 23 CD - CE - NZ ANGL. DEV. = 14.3 DEGREES
REMARK 500 ARG B 25 NE - CZ - NH1 ANGL. DEV. = 3.5 DEGREES
REMARK 500 ARG B 25 NE - CZ - NH2 ANGL. DEV. = -3.9 DEGREES
REMARK 500 CYS B 58 CA - CB - SG ANGL. DEV. = -10.9 DEGREES
REMARK 500 ARG B 96 NE - CZ - NH2 ANGL. DEV. = -3.7 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 R5P A 651
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE R5P B 0
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2VVR RELATED DB: PDB
REMARK 900 USING FOR MOLECULAR REPLACEMENT
REMARK 900 RELATED ID: 3HE8 RELATED DB: PDB
DBREF 3HEE A 1 149 UNP A3DIL8 A3DIL8_CLOTH 1 149
DBREF 3HEE B 1 149 UNP A3DIL8 A3DIL8_CLOTH 1 149
SEQRES 1 A 149 MET LYS ILE GLY ILE GLY SER ASP HIS GLY GLY TYR ASN
SEQRES 2 A 149 LEU LYS ARG GLU ILE ALA ASP PHE LEU LYS LYS ARG GLY
SEQRES 3 A 149 TYR GLU VAL ILE ASP PHE GLY THR HIS GLY ASN GLU SER
SEQRES 4 A 149 VAL ASP TYR PRO ASP PHE GLY LEU LYS VAL ALA GLU ALA
SEQRES 5 A 149 VAL LYS SER GLY GLU CYS ASP ARG GLY ILE VAL ILE CYS
SEQRES 6 A 149 GLY THR GLY LEU GLY ILE SER ILE ALA ALA ASN LYS VAL
SEQRES 7 A 149 PRO GLY ILE ARG ALA ALA VAL CYS THR ASN SER TYR MET
SEQRES 8 A 149 ALA ARG MET SER ARG GLU HIS ASN ASP ALA ASN ILE LEU
SEQRES 9 A 149 ALA LEU GLY GLU ARG VAL VAL GLY LEU ASP LEU ALA LEU
SEQRES 10 A 149 ASP ILE VAL ASP THR TRP LEU LYS ALA GLU PHE GLN GLY
SEQRES 11 A 149 GLY ARG HIS ALA THR ARG VAL GLY LYS ILE GLY GLU ILE
SEQRES 12 A 149 GLU LYS LYS TYR SER LYS
SEQRES 1 B 149 MET LYS ILE GLY ILE GLY SER ASP HIS GLY GLY TYR ASN
SEQRES 2 B 149 LEU LYS ARG GLU ILE ALA ASP PHE LEU LYS LYS ARG GLY
SEQRES 3 B 149 TYR GLU VAL ILE ASP PHE GLY THR HIS GLY ASN GLU SER
SEQRES 4 B 149 VAL ASP TYR PRO ASP PHE GLY LEU LYS VAL ALA GLU ALA
SEQRES 5 B 149 VAL LYS SER GLY GLU CYS ASP ARG GLY ILE VAL ILE CYS
SEQRES 6 B 149 GLY THR GLY LEU GLY ILE SER ILE ALA ALA ASN LYS VAL
SEQRES 7 B 149 PRO GLY ILE ARG ALA ALA VAL CYS THR ASN SER TYR MET
SEQRES 8 B 149 ALA ARG MET SER ARG GLU HIS ASN ASP ALA ASN ILE LEU
SEQRES 9 B 149 ALA LEU GLY GLU ARG VAL VAL GLY LEU ASP LEU ALA LEU
SEQRES 10 B 149 ASP ILE VAL ASP THR TRP LEU LYS ALA GLU PHE GLN GLY
SEQRES 11 B 149 GLY ARG HIS ALA THR ARG VAL GLY LYS ILE GLY GLU ILE
SEQRES 12 B 149 GLU LYS LYS TYR SER LYS
HET R5P A 651 14
HET R5P B 0 14
HETNAM R5P RIBOSE-5-PHOSPHATE
FORMUL 3 R5P 2(C5 H11 O8 P)
FORMUL 5 HOH *165(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 LYS A 77 1 10
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 ARG B 25 1 15
HELIX 8 8 ASP B 41 SER B 55 1 15
HELIX 9 9 GLY B 68 LYS B 77 1 10
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 5 O ILE B 30
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 0.68
CISPEP 2 GLY B 33 THR B 34 0 1.33
SITE 1 AC1 16 ASP A 8 HIS A 9 TYR A 42 CYS A 65
SITE 2 AC1 16 GLY A 66 THR A 67 GLY A 70 ARG A 109
SITE 3 AC1 16 HOH A 156 HOH A 191 HOH A 202 HOH A 220
SITE 4 AC1 16 HIS B 98 ASN B 99 ARG B 132 ARG B 136
SITE 1 AC2 15 HIS A 98 ASN A 99 ARG A 132 ARG A 136
SITE 2 AC2 15 ASP B 8 HIS B 9 TYR B 42 CYS B 65
SITE 3 AC2 15 GLY B 66 THR B 67 GLY B 70 ARG B 109
SITE 4 AC2 15 HOH B 155 HOH B 180 HOH B 183
CRYST1 69.381 69.381 153.566 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 0.014413 0.008321 0.000000 0.00000
SCALE2 0.000000 0.016643 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006512 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
