HEADER ISOMERASE 30-NOV-04 2BES
TITLE STRUCTURE OF MYCOBACTERIUM TUBERCULOSIS RIBOSE-5-PHOSPHATE ISOMERASE,
TITLE 2 RPIB, RV2465C, IN COMPLEX WITH 4-PHOSPHO-D-ERYTHRONOHYDROXAMIC ACID.
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CARBOHYDRATE-PHOSPHATE ISOMERASE;
COMPND 3 CHAIN: A, B, C, D, E;
COMPND 4 SYNONYM: RIBOSE-5-PHOSPHATE ISOMERASE B;
COMPND 5 EC: 5.3.1.6;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MYCOBACTERIUM TUBERCULOSIS;
SOURCE 3 ORGANISM_TAXID: 83332;
SOURCE 4 STRAIN: H37RV;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 511693;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21;
SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PCR T7
KEYWDS RIBOSE 5-PHOSPHATE EPIMERASE, PHOSPHOPENTOSISOMERASE, PENTOSE
KEYWDS 2 PHOSPHATE PATHWAY, HIGH-ENERGY ENEDIOLATE INTERMEDIATE, ISOMERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR A.K.ROOS,D.J.ERICSSON,S.L.MOWBRAY
REVDAT 6 13-DEC-23 2BES 1 REMARK
REVDAT 5 05-JUL-17 2BES 1 REMARK
REVDAT 4 19-FEB-14 2BES 1 REMARK VERSN FORMUL
REVDAT 3 24-FEB-09 2BES 1 VERSN
REVDAT 2 23-FEB-05 2BES 1 JRNL
REVDAT 1 03-DEC-04 2BES 0
JRNL AUTH A.K.ROOS,E.BURGOS,D.J.ERICSSON,L.SALMON,S.L.MOWBRAY
JRNL TITL COMPETITIVE INHIBITORS OF MYCOBACTERIUM TUBERCULOSIS
JRNL TITL 2 RIBOSE-5-PHOSPHATE ISOMERASE B REVEAL NEW INFORMATION ABOUT
JRNL TITL 3 THE REACTION MECHANISM.
JRNL REF J.BIOL.CHEM. V. 280 6416 2005
JRNL REFN ISSN 0021-9258
JRNL PMID 15590681
JRNL DOI 10.1074/JBC.M412018200
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH A.K.ROOS,C.E.ANDERSSON,T.BERGFORS,M.JACOBSSON,A.KARLEN,
REMARK 1 AUTH 2 T.UNGE,T.A.JONES,S.L.MOWBRAY
REMARK 1 TITL MYCOBACTERIUM TUBERCULOSIS RIBOSE-5-PHOSPHATE ISOMERASE HAS
REMARK 1 TITL 2 A KNOWN FOLD, BUT A NOVEL ACTIVE SITE
REMARK 1 REF J.MOL.BIOL. V. 355 799 2004
REMARK 1 REFN ISSN 0022-2836
REMARK 1 PMID 14687575
REMARK 1 DOI 10.1016/J.JMB.2003.11.021
REMARK 2
REMARK 2 RESOLUTION. 2.10 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.1.24
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) : 81.65
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 3 NUMBER OF REFLECTIONS : 52926
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) : 0.203
REMARK 3 R VALUE (WORKING SET) : 0.202
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 : 2830
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) : 2.15
REMARK 3 REFLECTION IN BIN (WORKING SET) : 3900
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : 0.2550
REMARK 3 BIN FREE R VALUE SET COUNT : 210
REMARK 3 BIN FREE R VALUE : 0.2640
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 5929
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 70
REMARK 3 SOLVENT ATOMS : 390
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 19.65
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.51000
REMARK 3 B22 (A**2) : -0.53000
REMARK 3 B33 (A**2) : 0.83000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : -1.10000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.208
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.164
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 : 0.934
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.922
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 6119 ; 0.006 ; 0.021
REMARK 3 BOND LENGTHS OTHERS (A): 5512 ; 0.000 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 8320 ; 1.441 ; 1.945
REMARK 3 BOND ANGLES OTHERS (DEGREES): 12748 ; 3.794 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 782 ; 3.786 ; 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): 914 ; 0.058 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 6974 ; 0.002 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 1232 ; 0.002 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 1326 ; 0.162 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): 5840 ; 0.243 ; 0.200
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): 2863 ; 0.106 ; 0.200
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 385 ; 0.093 ; 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): 26 ; 0.112 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): 72 ; 0.263 ; 0.200
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 38 ; 0.098 ; 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): 3892 ; 0.204 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 6180 ; 0.385 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 2227 ; 0.434 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 2140 ; 0.800 ; 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 : 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 RIDING
REMARK 3 POSITIONS
REMARK 4
REMARK 4 2BES COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 30-NOV-04.
REMARK 100 THE DEPOSITION ID IS D_1290021567.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 08-NOV-03
REMARK 200 TEMPERATURE (KELVIN) : 110.0
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : BM14
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.009
REMARK 200 MONOCHROMATOR : S1(111)
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 55757
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.100
REMARK 200 RESOLUTION RANGE LOW (A) : 81.650
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.500
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 200 DATA REDUNDANCY : 3.200
REMARK 200 R MERGE (I) : 0.12000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 5.3000
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) : 2.20
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.9
REMARK 200 DATA REDUNDANCY IN SHELL : 3.10
REMARK 200 R MERGE FOR SHELL (I) : 0.36000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.500
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 1USL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 55.90
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.80
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.55 M AMMONIUM PHOSPHATE, 0.1 M
REMARK 280 HEPES, PH 7.5
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,Y,-Z
REMARK 290 3555 X+1/2,Y+1/2,Z
REMARK 290 4555 -X+1/2,Y+1/2,-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 0.00000
REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 3 1.000000 0.000000 0.000000 68.23950
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 51.42750
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 68.23950
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 51.42750
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, 3
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: PQS
REMARK 350 TOTAL BURIED SURFACE AREA: 5020 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 14960 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -35.7 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 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PQS
REMARK 350 TOTAL BURIED SURFACE AREA: 4920 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 14870 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -33.2 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D
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
REMARK 350 BIOMOLECULE: 3
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PQS
REMARK 350 TOTAL BURIED SURFACE AREA: 5260 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 14860 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -38.1 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: E
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 -1.000000 0.000000 0.000000 129.97049
REMARK 350 BIOMT2 2 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 69.23977
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 A2022 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 -9
REMARK 465 ALA A -8
REMARK 465 HIS A -7
REMARK 465 HIS A -6
REMARK 465 HIS A -5
REMARK 465 HIS A -4
REMARK 465 HIS A -3
REMARK 465 HIS A -2
REMARK 465 SER A -1
REMARK 465 GLY A 0
REMARK 465 MET A 1
REMARK 465 SER A 2
REMARK 465 ALA A 160
REMARK 465 PRO A 161
REMARK 465 ALA A 162
REMARK 465 MET B -9
REMARK 465 ALA B -8
REMARK 465 HIS B -7
REMARK 465 HIS B -6
REMARK 465 HIS B -5
REMARK 465 HIS B -4
REMARK 465 HIS B -3
REMARK 465 HIS B -2
REMARK 465 SER B -1
REMARK 465 GLY B 0
REMARK 465 MET B 1
REMARK 465 GLY B 159
REMARK 465 ALA B 160
REMARK 465 PRO B 161
REMARK 465 ALA B 162
REMARK 465 MET C -9
REMARK 465 ALA C -8
REMARK 465 HIS C -7
REMARK 465 HIS C -6
REMARK 465 HIS C -5
REMARK 465 HIS C -4
REMARK 465 HIS C -3
REMARK 465 HIS C -2
REMARK 465 SER C -1
REMARK 465 GLY C 0
REMARK 465 MET C 1
REMARK 465 SER C 2
REMARK 465 PRO C 161
REMARK 465 ALA C 162
REMARK 465 MET D -9
REMARK 465 ALA D -8
REMARK 465 HIS D -7
REMARK 465 HIS D -6
REMARK 465 HIS D -5
REMARK 465 HIS D -4
REMARK 465 HIS D -3
REMARK 465 HIS D -2
REMARK 465 SER D -1
REMARK 465 GLY D 0
REMARK 465 MET D 1
REMARK 465 GLY D 159
REMARK 465 ALA D 160
REMARK 465 PRO D 161
REMARK 465 ALA D 162
REMARK 465 MET E -9
REMARK 465 ALA E -8
REMARK 465 HIS E -7
REMARK 465 HIS E -6
REMARK 465 HIS E -5
REMARK 465 HIS E -4
REMARK 465 HIS E -3
REMARK 465 HIS E -2
REMARK 465 SER E -1
REMARK 465 GLY E 0
REMARK 465 MET E 1
REMARK 465 SER E 2
REMARK 465 PRO E 161
REMARK 465 ALA E 162
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 C 34 CB - CG - OD2 ANGL. DEV. = 5.5 DEGREES
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH C2008 DISTANCE = 6.62 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE RES A 200
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE RES B 200
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE RES C 200
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE RES D 200
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE RES E 200
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2BET RELATED DB: PDB
REMARK 900 STRUCTURE OF MYCOBACTERIUM TUBERCULOSIS RIBOSE-5-PHOSPHATE
REMARK 900 ISOMERASE, RPIB, RV2465C, IN COMPLEX WITH 4-PHOSPHO-D- ERYTHRONATE.
DBREF 2BES A -9 3 PDB 2BES 2BES -9 3
DBREF 2BES A 4 162 UNP Q7D737 Q7D737 1 159
DBREF 2BES B -9 3 PDB 2BES 2BES -9 3
DBREF 2BES B 4 162 UNP Q7D737 Q7D737 1 159
DBREF 2BES C -9 3 PDB 2BES 2BES -9 3
DBREF 2BES C 4 162 UNP Q7D737 Q7D737 1 159
DBREF 2BES D -9 3 PDB 2BES 2BES -9 3
DBREF 2BES D 4 162 UNP Q7D737 Q7D737 1 159
DBREF 2BES E -9 3 PDB 2BES 2BES -9 3
DBREF 2BES E 4 162 UNP Q7D737 Q7D737 1 159
SEQRES 1 A 172 MET ALA HIS HIS HIS HIS HIS HIS SER GLY MET SER GLY
SEQRES 2 A 172 MET ARG VAL TYR LEU GLY ALA ASP HIS ALA GLY TYR GLU
SEQRES 3 A 172 LEU LYS GLN ARG ILE ILE GLU HIS LEU LYS GLN THR GLY
SEQRES 4 A 172 HIS GLU PRO ILE ASP CYS GLY ALA LEU ARG TYR ASP ALA
SEQRES 5 A 172 ASP ASP ASP TYR PRO ALA PHE CYS ILE ALA ALA ALA THR
SEQRES 6 A 172 ARG THR VAL ALA ASP PRO GLY SER LEU GLY ILE VAL LEU
SEQRES 7 A 172 GLY GLY SER GLY ASN GLY GLU GLN ILE ALA ALA ASN LYS
SEQRES 8 A 172 VAL PRO GLY ALA ARG CYS ALA LEU ALA TRP SER VAL GLN
SEQRES 9 A 172 THR ALA ALA LEU ALA ARG GLU HIS ASN ASN ALA GLN LEU
SEQRES 10 A 172 ILE GLY ILE GLY GLY ARG MET HIS THR VAL ALA GLU ALA
SEQRES 11 A 172 LEU ALA ILE VAL ASP ALA PHE VAL THR THR PRO TRP SER
SEQRES 12 A 172 LYS ALA GLN ARG HIS GLN ARG ARG ILE ASP ILE LEU ALA
SEQRES 13 A 172 GLU TYR GLU ARG THR HIS GLU ALA PRO PRO VAL PRO GLY
SEQRES 14 A 172 ALA PRO ALA
SEQRES 1 B 172 MET ALA HIS HIS HIS HIS HIS HIS SER GLY MET SER GLY
SEQRES 2 B 172 MET ARG VAL TYR LEU GLY ALA ASP HIS ALA GLY TYR GLU
SEQRES 3 B 172 LEU LYS GLN ARG ILE ILE GLU HIS LEU LYS GLN THR GLY
SEQRES 4 B 172 HIS GLU PRO ILE ASP CYS GLY ALA LEU ARG TYR ASP ALA
SEQRES 5 B 172 ASP ASP ASP TYR PRO ALA PHE CYS ILE ALA ALA ALA THR
SEQRES 6 B 172 ARG THR VAL ALA ASP PRO GLY SER LEU GLY ILE VAL LEU
SEQRES 7 B 172 GLY GLY SER GLY ASN GLY GLU GLN ILE ALA ALA ASN LYS
SEQRES 8 B 172 VAL PRO GLY ALA ARG CYS ALA LEU ALA TRP SER VAL GLN
SEQRES 9 B 172 THR ALA ALA LEU ALA ARG GLU HIS ASN ASN ALA GLN LEU
SEQRES 10 B 172 ILE GLY ILE GLY GLY ARG MET HIS THR VAL ALA GLU ALA
SEQRES 11 B 172 LEU ALA ILE VAL ASP ALA PHE VAL THR THR PRO TRP SER
SEQRES 12 B 172 LYS ALA GLN ARG HIS GLN ARG ARG ILE ASP ILE LEU ALA
SEQRES 13 B 172 GLU TYR GLU ARG THR HIS GLU ALA PRO PRO VAL PRO GLY
SEQRES 14 B 172 ALA PRO ALA
SEQRES 1 C 172 MET ALA HIS HIS HIS HIS HIS HIS SER GLY MET SER GLY
SEQRES 2 C 172 MET ARG VAL TYR LEU GLY ALA ASP HIS ALA GLY TYR GLU
SEQRES 3 C 172 LEU LYS GLN ARG ILE ILE GLU HIS LEU LYS GLN THR GLY
SEQRES 4 C 172 HIS GLU PRO ILE ASP CYS GLY ALA LEU ARG TYR ASP ALA
SEQRES 5 C 172 ASP ASP ASP TYR PRO ALA PHE CYS ILE ALA ALA ALA THR
SEQRES 6 C 172 ARG THR VAL ALA ASP PRO GLY SER LEU GLY ILE VAL LEU
SEQRES 7 C 172 GLY GLY SER GLY ASN GLY GLU GLN ILE ALA ALA ASN LYS
SEQRES 8 C 172 VAL PRO GLY ALA ARG CYS ALA LEU ALA TRP SER VAL GLN
SEQRES 9 C 172 THR ALA ALA LEU ALA ARG GLU HIS ASN ASN ALA GLN LEU
SEQRES 10 C 172 ILE GLY ILE GLY GLY ARG MET HIS THR VAL ALA GLU ALA
SEQRES 11 C 172 LEU ALA ILE VAL ASP ALA PHE VAL THR THR PRO TRP SER
SEQRES 12 C 172 LYS ALA GLN ARG HIS GLN ARG ARG ILE ASP ILE LEU ALA
SEQRES 13 C 172 GLU TYR GLU ARG THR HIS GLU ALA PRO PRO VAL PRO GLY
SEQRES 14 C 172 ALA PRO ALA
SEQRES 1 D 172 MET ALA HIS HIS HIS HIS HIS HIS SER GLY MET SER GLY
SEQRES 2 D 172 MET ARG VAL TYR LEU GLY ALA ASP HIS ALA GLY TYR GLU
SEQRES 3 D 172 LEU LYS GLN ARG ILE ILE GLU HIS LEU LYS GLN THR GLY
SEQRES 4 D 172 HIS GLU PRO ILE ASP CYS GLY ALA LEU ARG TYR ASP ALA
SEQRES 5 D 172 ASP ASP ASP TYR PRO ALA PHE CYS ILE ALA ALA ALA THR
SEQRES 6 D 172 ARG THR VAL ALA ASP PRO GLY SER LEU GLY ILE VAL LEU
SEQRES 7 D 172 GLY GLY SER GLY ASN GLY GLU GLN ILE ALA ALA ASN LYS
SEQRES 8 D 172 VAL PRO GLY ALA ARG CYS ALA LEU ALA TRP SER VAL GLN
SEQRES 9 D 172 THR ALA ALA LEU ALA ARG GLU HIS ASN ASN ALA GLN LEU
SEQRES 10 D 172 ILE GLY ILE GLY GLY ARG MET HIS THR VAL ALA GLU ALA
SEQRES 11 D 172 LEU ALA ILE VAL ASP ALA PHE VAL THR THR PRO TRP SER
SEQRES 12 D 172 LYS ALA GLN ARG HIS GLN ARG ARG ILE ASP ILE LEU ALA
SEQRES 13 D 172 GLU TYR GLU ARG THR HIS GLU ALA PRO PRO VAL PRO GLY
SEQRES 14 D 172 ALA PRO ALA
SEQRES 1 E 172 MET ALA HIS HIS HIS HIS HIS HIS SER GLY MET SER GLY
SEQRES 2 E 172 MET ARG VAL TYR LEU GLY ALA ASP HIS ALA GLY TYR GLU
SEQRES 3 E 172 LEU LYS GLN ARG ILE ILE GLU HIS LEU LYS GLN THR GLY
SEQRES 4 E 172 HIS GLU PRO ILE ASP CYS GLY ALA LEU ARG TYR ASP ALA
SEQRES 5 E 172 ASP ASP ASP TYR PRO ALA PHE CYS ILE ALA ALA ALA THR
SEQRES 6 E 172 ARG THR VAL ALA ASP PRO GLY SER LEU GLY ILE VAL LEU
SEQRES 7 E 172 GLY GLY SER GLY ASN GLY GLU GLN ILE ALA ALA ASN LYS
SEQRES 8 E 172 VAL PRO GLY ALA ARG CYS ALA LEU ALA TRP SER VAL GLN
SEQRES 9 E 172 THR ALA ALA LEU ALA ARG GLU HIS ASN ASN ALA GLN LEU
SEQRES 10 E 172 ILE GLY ILE GLY GLY ARG MET HIS THR VAL ALA GLU ALA
SEQRES 11 E 172 LEU ALA ILE VAL ASP ALA PHE VAL THR THR PRO TRP SER
SEQRES 12 E 172 LYS ALA GLN ARG HIS GLN ARG ARG ILE ASP ILE LEU ALA
SEQRES 13 E 172 GLU TYR GLU ARG THR HIS GLU ALA PRO PRO VAL PRO GLY
SEQRES 14 E 172 ALA PRO ALA
HET RES A 200 14
HET RES B 200 14
HET RES C 200 14
HET RES D 200 14
HET RES E 200 14
HETNAM RES 4-PHOSPHO-D-ERYTHRONOHYDROXAMIC ACID
FORMUL 6 RES 5(C4 H10 N O8 P)
FORMUL 11 HOH *390(H2 O)
HELIX 1 1 GLY A 14 THR A 28 1 15
HELIX 2 2 TYR A 46 ALA A 59 1 14
HELIX 3 3 GLY A 72 LYS A 81 1 10
HELIX 4 4 SER A 92 HIS A 102 1 11
HELIX 5 5 THR A 116 THR A 130 1 15
HELIX 6 6 ALA A 135 HIS A 152 1 18
HELIX 7 7 GLY B 14 THR B 28 1 15
HELIX 8 8 TYR B 46 ALA B 59 1 14
HELIX 9 9 GLY B 72 LYS B 81 1 10
HELIX 10 10 SER B 92 HIS B 102 1 11
HELIX 11 11 THR B 116 THR B 130 1 15
HELIX 12 12 ALA B 135 HIS B 152 1 18
HELIX 13 13 GLY C 14 THR C 28 1 15
HELIX 14 14 TYR C 46 ALA C 59 1 14
HELIX 15 15 GLY C 72 LYS C 81 1 10
HELIX 16 16 SER C 92 HIS C 102 1 11
HELIX 17 17 THR C 116 THR C 130 1 15
HELIX 18 18 ALA C 135 HIS C 152 1 18
HELIX 19 19 ASP D 11 THR D 28 1 18
HELIX 20 20 ASP D 45 ALA D 59 1 15
HELIX 21 21 GLY D 72 LYS D 81 1 10
HELIX 22 22 SER D 92 HIS D 102 1 11
HELIX 23 23 THR D 116 THR D 130 1 15
HELIX 24 24 ALA D 135 HIS D 152 1 18
HELIX 25 25 GLY E 14 THR E 28 1 15
HELIX 26 26 TYR E 46 ALA E 59 1 14
HELIX 27 27 GLY E 72 LYS E 81 1 10
HELIX 28 28 SER E 92 HIS E 102 1 11
HELIX 29 29 THR E 116 THR E 130 1 15
HELIX 30 30 ALA E 135 HIS E 152 1 18
SHEET 1 AA 5 GLU A 31 GLY A 36 0
SHEET 2 AA 5 ARG A 5 ALA A 10 1 O VAL A 6 N ILE A 33
SHEET 3 AA 5 LEU A 64 GLY A 69 1 O LEU A 64 N TYR A 7
SHEET 4 AA 5 LEU A 107 GLY A 111 1 O ILE A 108 N VAL A 67
SHEET 5 AA 5 ALA A 85 ALA A 90 1 O ALA A 88 N GLY A 109
SHEET 1 BA 5 GLU B 31 ASP B 34 0
SHEET 2 BA 5 ARG B 5 ALA B 10 1 O VAL B 6 N ILE B 33
SHEET 3 BA 5 LEU B 64 GLY B 69 1 O LEU B 64 N TYR B 7
SHEET 4 BA 5 LEU B 107 GLY B 111 1 O ILE B 108 N VAL B 67
SHEET 5 BA 5 ALA B 85 ALA B 90 1 O ALA B 88 N GLY B 109
SHEET 1 CA 5 GLU C 31 ASP C 34 0
SHEET 2 CA 5 ARG C 5 ALA C 10 1 O VAL C 6 N ILE C 33
SHEET 3 CA 5 LEU C 64 GLY C 69 1 O LEU C 64 N TYR C 7
SHEET 4 CA 5 LEU C 107 GLY C 111 1 O ILE C 108 N VAL C 67
SHEET 5 CA 5 ALA C 85 ALA C 90 1 O ALA C 88 N GLY C 109
SHEET 1 DA 5 GLU D 31 ASP D 34 0
SHEET 2 DA 5 ARG D 5 ALA D 10 1 O VAL D 6 N ILE D 33
SHEET 3 DA 5 LEU D 64 GLY D 69 1 O LEU D 64 N TYR D 7
SHEET 4 DA 5 LEU D 107 GLY D 111 1 O ILE D 108 N VAL D 67
SHEET 5 DA 5 ALA D 85 ALA D 90 1 O ALA D 88 N GLY D 109
SHEET 1 EA 5 GLU E 31 ASP E 34 0
SHEET 2 EA 5 ARG E 5 ALA E 10 1 O VAL E 6 N ILE E 33
SHEET 3 EA 5 LEU E 64 GLY E 69 1 O LEU E 64 N TYR E 7
SHEET 4 EA 5 LEU E 107 GLY E 111 1 O ILE E 108 N VAL E 67
SHEET 5 EA 5 ALA E 85 ALA E 90 1 O ALA E 88 N GLY E 109
CISPEP 1 GLY A 36 ALA A 37 0 2.83
CISPEP 2 GLY B 36 ALA B 37 0 3.59
CISPEP 3 GLY C 36 ALA C 37 0 4.41
CISPEP 4 GLY D 36 ALA D 37 0 4.94
CISPEP 5 GLY E 36 ALA E 37 0 5.64
SITE 1 AC1 19 ASP A 11 HIS A 12 ALA A 13 GLY A 70
SITE 2 AC1 19 SER A 71 ASN A 73 GLY A 74 GLU A 75
SITE 3 AC1 19 ARG A 113 HOH A2063 HOH A2064 HOH A2065
SITE 4 AC1 19 HOH A2066 HIS B 102 ASN B 103 ARG B 137
SITE 5 AC1 19 HIS B 138 ARG B 141 HOH B2062
SITE 1 AC2 18 HIS A 102 ASN A 103 ARG A 137 ARG A 141
SITE 2 AC2 18 HOH A2050 ASP B 11 HIS B 12 ALA B 13
SITE 3 AC2 18 GLY B 70 SER B 71 ASN B 73 GLY B 74
SITE 4 AC2 18 GLU B 75 ARG B 113 HOH B2019 HOH B2079
SITE 5 AC2 18 HOH B2080 HOH B2081
SITE 1 AC3 17 ASP C 11 HIS C 12 GLY C 70 SER C 71
SITE 2 AC3 17 ASN C 73 GLY C 74 GLU C 75 ARG C 113
SITE 3 AC3 17 HOH C2084 HOH C2085 HOH C2086 HIS D 102
SITE 4 AC3 17 ASN D 103 ARG D 137 HIS D 138 ARG D 141
SITE 5 AC3 17 HOH D2072
SITE 1 AC4 18 HIS C 102 ASN C 103 ARG C 137 HIS C 138
SITE 2 AC4 18 ARG C 141 ASP D 11 HIS D 12 GLY D 70
SITE 3 AC4 18 SER D 71 ASN D 73 GLY D 74 GLU D 75
SITE 4 AC4 18 ARG D 113 HOH D2020 HOH D2094 HOH D2095
SITE 5 AC4 18 HOH D2096 HOH D2097
SITE 1 AC5 16 ASP E 11 HIS E 12 GLY E 70 SER E 71
SITE 2 AC5 16 ASN E 73 GLY E 74 GLU E 75 HIS E 102
SITE 3 AC5 16 ASN E 103 ARG E 113 ARG E 137 ARG E 141
SITE 4 AC5 16 HOH E2057 HOH E2058 HOH E2059 HOH E2060
CRYST1 136.479 102.855 69.545 90.00 95.37 90.00 C 1 2 1 20
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 0.007327 0.000000 0.000689 0.00000
SCALE2 0.000000 0.009722 0.000000 0.00000
SCALE3 0.000000 0.000000 0.014443 0.00000
MTRIX1 1 -0.401300 0.911400 0.090700 22.76060 1
MTRIX2 1 0.911400 0.387500 0.138300 16.98350 1
MTRIX3 1 0.090900 0.138200 -0.986200 20.02760 1
MTRIX1 2 -0.348200 -0.925900 0.146600 38.75420 1
MTRIX2 2 -0.926500 0.316100 -0.204100 35.28520 1
MTRIX3 2 0.142600 -0.206900 -0.967900 50.50350 1
MTRIX1 3 -0.690700 0.642900 -0.331100 43.79240 1
MTRIX2 3 -0.658400 -0.748400 -0.079900 39.09920 1
MTRIX3 3 -0.299100 0.162800 0.940200 -21.43080 1
MTRIX1 4 -0.767800 -0.547400 -0.332800 75.66250 1
MTRIX2 4 0.539800 -0.832600 0.124200 -43.42820 1
MTRIX3 4 -0.345100 -0.084300 0.934800 0.55810 1
(ATOM LINES ARE NOT SHOWN.)
END
