HEADER ISOMERASE 08-JUL-06 2IXH
TITLE RMLC P AERUGINOSA WITH DTDP-RHAMNOSE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: DTDP-4-DEHYDRORHAMNOSE 3,5-EPIMERASE;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: DTDP-4-KETO-6-DEOXYGLUCOSE 3,5-EPIMERASE;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: PSEUDOMONAS AERUGINOSA;
SOURCE 3 ORGANISM_TAXID: 287;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS ISOMERASE, LIPOPOLYSACCHARIDE BIOSYNTHESIS, EPIMERISE, EPIMERASE,
KEYWDS 2 EPIMERIZE
EXPDTA X-RAY DIFFRACTION
AUTHOR C.DONG,J.H.NAISMITH
REVDAT 5 06-JUN-18 2IXH 1 JRNL REMARK
REVDAT 4 13-JUL-11 2IXH 1 VERSN
REVDAT 3 24-FEB-09 2IXH 1 VERSN
REVDAT 2 06-DEC-06 2IXH 1 JRNL
REVDAT 1 26-OCT-06 2IXH 0
JRNL AUTH C.DONG,L.L.MAJOR,V.SRIKANNATHASAN,J.C.ERREY,M.F.GIRAUD,
JRNL AUTH 2 J.S.LAM,M.GRANINGER,P.MESSNER,M.R.MCNEIL,R.A.FIELD,
JRNL AUTH 3 C.WHITFIELD,J.H.NAISMITH
JRNL TITL RMLC, A C3' AND C5' CARBOHYDRATE EPIMERASE, APPEARS TO
JRNL TITL 2 OPERATE VIA AN INTERMEDIATE WITH AN UNUSUAL TWIST BOAT
JRNL TITL 3 CONFORMATION.
JRNL REF J. MOL. BIOL. V. 365 146 2007
JRNL REFN ISSN 0022-2836
JRNL PMID 17046787
JRNL DOI 10.1016/J.JMB.2006.09.063
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) : 63.25
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 3 NUMBER OF REFLECTIONS : 29011
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) : 0.193
REMARK 3 R VALUE (WORKING SET) : 0.190
REMARK 3 FREE R VALUE : 0.256
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 1544
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) : 2128
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : 0.2450
REMARK 3 BIN FREE R VALUE SET COUNT : 92
REMARK 3 BIN FREE R VALUE : 0.2920
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2980
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 70
REMARK 3 SOLVENT ATOMS : 590
REMARK 3
REMARK 3 B VALUES.
REMARK 3 B VALUE TYPE : LIKELY RESIDUAL
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 28.35
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 4.03000
REMARK 3 B22 (A**2) : -0.92000
REMARK 3 B33 (A**2) : -3.11000
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): 0.194
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.184
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.152
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 9.215
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.953
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.909
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 3140 ; 0.008 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): 2180 ; 0.001 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 4266 ; 1.116 ; 1.959
REMARK 3 BOND ANGLES OTHERS (DEGREES): 5226 ; 0.808 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 366 ; 6.580 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 166 ;30.566 ;22.892
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 484 ;13.206 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 30 ;17.692 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 438 ; 0.078 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 3506 ; 0.003 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 722 ; 0.001 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 482 ; 0.182 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): 2121 ; 0.181 ; 0.200
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 1422 ; 0.176 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): 1597 ; 0.077 ; 0.200
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 297 ; 0.119 ; 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): 39 ; 0.158 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): 125 ; 0.259 ; 0.200
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 88 ; 0.178 ; 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): 2390 ; 0.548 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 2936 ; 0.609 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1577 ; 0.917 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1330 ; 1.329 ; 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 : 2
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 3 A 184
REMARK 3 ORIGIN FOR THE GROUP (A): 9.5611 19.8578 16.7919
REMARK 3 T TENSOR
REMARK 3 T11: -0.1030 T22: 0.0005
REMARK 3 T33: 0.0124 T12: -0.0546
REMARK 3 T13: 0.0122 T23: 0.0044
REMARK 3 L TENSOR
REMARK 3 L11: 1.2551 L22: 1.5895
REMARK 3 L33: 2.8857 L12: 0.2110
REMARK 3 L13: 0.6157 L23: -0.4548
REMARK 3 S TENSOR
REMARK 3 S11: -0.1087 S12: 0.2886 S13: 0.0679
REMARK 3 S21: -0.1902 S22: 0.0732 S23: -0.1256
REMARK 3 S31: -0.1095 S32: 0.5403 S33: 0.0354
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 1 B 184
REMARK 3 ORIGIN FOR THE GROUP (A): 45.7860 9.6419 98.9419
REMARK 3 T TENSOR
REMARK 3 T11: -0.0704 T22: -0.1567
REMARK 3 T33: -0.1242 T12: 0.1734
REMARK 3 T13: -0.0545 T23: -0.0284
REMARK 3 L TENSOR
REMARK 3 L11: 0.9441 L22: 1.2157
REMARK 3 L33: 5.3856 L12: -0.3826
REMARK 3 L13: 0.5685 L23: 0.0169
REMARK 3 S TENSOR
REMARK 3 S11: 0.0298 S12: 0.0772 S13: 0.0382
REMARK 3 S21: -0.2430 S22: -0.1883 S23: 0.1577
REMARK 3 S31: -0.9936 S32: -0.6868 S33: 0.1585
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 2IXH COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 08-JUL-06.
REMARK 100 THE DEPOSITION ID IS D_1290029315.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : NULL
REMARK 200 TEMPERATURE (KELVIN) : 100.0
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SRS
REMARK 200 BEAMLINE : PX9.6
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.87
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 30581
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.000
REMARK 200 RESOLUTION RANGE LOW (A) : 40.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 4.000
REMARK 200 R MERGE (I) : 0.08000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 6.3000
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) : 2.10
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 4.00
REMARK 200 R MERGE FOR SHELL (I) : 0.36000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.100
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: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 43.30
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.19
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z+1/2
REMARK 290 3555 -X,Y,-Z+1/2
REMARK 290 4555 X,-Y,-Z
REMARK 290 5555 X+1/2,Y+1/2,Z
REMARK 290 6555 -X+1/2,-Y+1/2,Z+1/2
REMARK 290 7555 -X+1/2,Y+1/2,-Z+1/2
REMARK 290 8555 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 54.68300
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 54.68300
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 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 32.45750
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 62.76850
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 32.45750
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 62.76850
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 54.68300
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 32.45750
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 62.76850
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 54.68300
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 32.45750
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 62.76850
REMARK 290 SMTRY3 8 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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 5590 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 16210 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -20.0 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 -1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 2 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 54.68300
REMARK 350
REMARK 350 BIOMOLECULE: 2
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: 5300 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 16310 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -19.0 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 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 218.73200
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 A2042 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A2128 LIES ON A SPECIAL POSITION.
REMARK 375 HOH B2045 LIES ON A SPECIAL POSITION.
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 O HOH B 2151 O HOH B 2265 2.16
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 O HOH A 2169 O HOH A 2169 3555 1.76
REMARK 500 O HOH A 2080 O HOH B 2206 3656 2.15
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 ALA A 3 -115.52 -160.44
REMARK 500 LYS A 110 16.57 59.16
REMARK 500 PRO B 160 58.90 -68.94
REMARK 500 GLN B 162 -73.67 -24.94
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 A2011 DISTANCE = 6.58 ANGSTROMS
REMARK 525 HOH A2014 DISTANCE = 5.91 ANGSTROMS
REMARK 525 HOH A2017 DISTANCE = 6.34 ANGSTROMS
REMARK 525 HOH A2018 DISTANCE = 7.69 ANGSTROMS
REMARK 525 HOH A2022 DISTANCE = 6.82 ANGSTROMS
REMARK 525 HOH A2030 DISTANCE = 7.80 ANGSTROMS
REMARK 525 HOH A2031 DISTANCE = 7.34 ANGSTROMS
REMARK 525 HOH A2041 DISTANCE = 6.97 ANGSTROMS
REMARK 525 HOH A2042 DISTANCE = 6.62 ANGSTROMS
REMARK 525 HOH A2049 DISTANCE = 5.84 ANGSTROMS
REMARK 525 HOH A2051 DISTANCE = 7.05 ANGSTROMS
REMARK 525 HOH A2064 DISTANCE = 8.39 ANGSTROMS
REMARK 525 HOH A2065 DISTANCE = 7.11 ANGSTROMS
REMARK 525 HOH A2073 DISTANCE = 7.08 ANGSTROMS
REMARK 525 HOH A2086 DISTANCE = 6.29 ANGSTROMS
REMARK 525 HOH A2107 DISTANCE = 6.04 ANGSTROMS
REMARK 525 HOH A2115 DISTANCE = 7.41 ANGSTROMS
REMARK 525 HOH A2131 DISTANCE = 6.29 ANGSTROMS
REMARK 525 HOH B2003 DISTANCE = 5.98 ANGSTROMS
REMARK 525 HOH B2007 DISTANCE = 6.10 ANGSTROMS
REMARK 525 HOH B2010 DISTANCE = 7.04 ANGSTROMS
REMARK 525 HOH B2011 DISTANCE = 9.25 ANGSTROMS
REMARK 525 HOH B2012 DISTANCE = 6.95 ANGSTROMS
REMARK 525 HOH B2022 DISTANCE = 6.91 ANGSTROMS
REMARK 525 HOH B2023 DISTANCE = 5.82 ANGSTROMS
REMARK 525 HOH B2024 DISTANCE = 7.00 ANGSTROMS
REMARK 525 HOH B2037 DISTANCE = 7.36 ANGSTROMS
REMARK 525 HOH B2039 DISTANCE = 6.43 ANGSTROMS
REMARK 525 HOH B2040 DISTANCE = 7.75 ANGSTROMS
REMARK 525 HOH B2044 DISTANCE = 5.85 ANGSTROMS
REMARK 525 HOH B2045 DISTANCE = 8.31 ANGSTROMS
REMARK 525 HOH B2056 DISTANCE = 6.37 ANGSTROMS
REMARK 525 HOH B2058 DISTANCE = 6.11 ANGSTROMS
REMARK 525 HOH B2060 DISTANCE = 6.09 ANGSTROMS
REMARK 525 HOH B2061 DISTANCE = 5.84 ANGSTROMS
REMARK 525 HOH B2065 DISTANCE = 6.92 ANGSTROMS
REMARK 525 HOH B2066 DISTANCE = 6.41 ANGSTROMS
REMARK 525 HOH B2067 DISTANCE = 7.95 ANGSTROMS
REMARK 525 HOH B2068 DISTANCE = 7.91 ANGSTROMS
REMARK 525 HOH B2083 DISTANCE = 6.34 ANGSTROMS
REMARK 525 HOH B2084 DISTANCE = 5.81 ANGSTROMS
REMARK 525 HOH B2112 DISTANCE = 5.85 ANGSTROMS
REMARK 525 HOH B2123 DISTANCE = 6.28 ANGSTROMS
REMARK 525 HOH B2135 DISTANCE = 7.37 ANGSTROMS
REMARK 525 HOH B2146 DISTANCE = 6.22 ANGSTROMS
REMARK 525 HOH B2158 DISTANCE = 6.01 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TRH A1185
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TRH B1185
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1RTV RELATED DB: PDB
REMARK 900 RMLC (DTDP-6-DEOXY-D-XYLO-4-HEXULOSE 3, 5-EPIMERASE)
REMARK 900 CRYSTALSTRUCTURE FROM PSEUDOMONAS AERUGINOSA, APO STRUCTURE
REMARK 900 RELATED ID: 2IXI RELATED DB: PDB
REMARK 900 RMLC P AUERGINOSA WITHG DTDP-XYLOSE
REMARK 900 RELATED ID: 2IXJ RELATED DB: PDB
REMARK 900 RMLC P AUERGINOSA NATIVE
REMARK 900 RELATED ID: 2IXK RELATED DB: PDB
REMARK 900 RMLC P AUERGINOSA WITHG DTDP-4-KETO RHAMNNOSE (THE PRODUCT OF THE
REMARK 900 REACTION)
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 EXTRA S AT N-TERMINUS CLONING ARTEFACT
DBREF 2IXH A 1 3 PDB 2IXH 2IXH 1 3
DBREF 2IXH A 4 184 UNP Q9HU21 Q9HU21_PSEAE 1 181
DBREF 2IXH B 1 3 PDB 2IXH 2IXH 1 3
DBREF 2IXH B 4 184 UNP Q9HU21 Q9HU21_PSEAE 1 181
SEQRES 1 A 184 SER MET ALA MET LYS ALA THR ARG LEU ALA ILE PRO ASP
SEQRES 2 A 184 VAL ILE LEU PHE GLU PRO ARG VAL PHE GLY ASP ASP ARG
SEQRES 3 A 184 GLY PHE PHE PHE GLU SER TYR ASN GLN ARG ALA PHE GLU
SEQRES 4 A 184 GLU ALA CYS GLY HIS PRO VAL SER PHE VAL GLN ASP ASN
SEQRES 5 A 184 HIS SER ARG SER ALA ARG GLY VAL LEU ARG GLY LEU HIS
SEQRES 6 A 184 TYR GLN ILE ARG GLN ALA GLN GLY LYS LEU VAL ARG ALA
SEQRES 7 A 184 THR LEU GLY GLU VAL PHE ASP VAL ALA VAL ASP LEU ARG
SEQRES 8 A 184 ARG GLY SER PRO THR PHE GLY GLN TRP VAL GLY GLU ARG
SEQRES 9 A 184 LEU SER ALA GLU ASN LYS ARG GLN MET TRP ILE PRO ALA
SEQRES 10 A 184 GLY PHE ALA HIS GLY PHE VAL VAL LEU SER GLU TYR ALA
SEQRES 11 A 184 GLU PHE LEU TYR LYS THR THR ASP PHE TRP ALA PRO GLU
SEQRES 12 A 184 HIS GLU ARG CYS ILE VAL TRP ASN ASP PRO GLU LEU LYS
SEQRES 13 A 184 ILE ASP TRP PRO LEU GLN ASP ALA PRO LEU LEU SER GLU
SEQRES 14 A 184 LYS ASP ARG GLN GLY LYS ALA PHE ALA ASP ALA ASP CYS
SEQRES 15 A 184 PHE PRO
SEQRES 1 B 184 SER MET ALA MET LYS ALA THR ARG LEU ALA ILE PRO ASP
SEQRES 2 B 184 VAL ILE LEU PHE GLU PRO ARG VAL PHE GLY ASP ASP ARG
SEQRES 3 B 184 GLY PHE PHE PHE GLU SER TYR ASN GLN ARG ALA PHE GLU
SEQRES 4 B 184 GLU ALA CYS GLY HIS PRO VAL SER PHE VAL GLN ASP ASN
SEQRES 5 B 184 HIS SER ARG SER ALA ARG GLY VAL LEU ARG GLY LEU HIS
SEQRES 6 B 184 TYR GLN ILE ARG GLN ALA GLN GLY LYS LEU VAL ARG ALA
SEQRES 7 B 184 THR LEU GLY GLU VAL PHE ASP VAL ALA VAL ASP LEU ARG
SEQRES 8 B 184 ARG GLY SER PRO THR PHE GLY GLN TRP VAL GLY GLU ARG
SEQRES 9 B 184 LEU SER ALA GLU ASN LYS ARG GLN MET TRP ILE PRO ALA
SEQRES 10 B 184 GLY PHE ALA HIS GLY PHE VAL VAL LEU SER GLU TYR ALA
SEQRES 11 B 184 GLU PHE LEU TYR LYS THR THR ASP PHE TRP ALA PRO GLU
SEQRES 12 B 184 HIS GLU ARG CYS ILE VAL TRP ASN ASP PRO GLU LEU LYS
SEQRES 13 B 184 ILE ASP TRP PRO LEU GLN ASP ALA PRO LEU LEU SER GLU
SEQRES 14 B 184 LYS ASP ARG GLN GLY LYS ALA PHE ALA ASP ALA ASP CYS
SEQRES 15 B 184 PHE PRO
HET TRH A1185 35
HET TRH B1185 35
HETNAM TRH 2'-DEOXY-THYMIDINE-BETA-L-RHAMNOSE
FORMUL 3 TRH 2(C16 H26 N2 O15 P2)
FORMUL 5 HOH *590(H2 O)
HELIX 1 1 ASN A 34 GLY A 43 1 10
HELIX 2 2 ALA A 141 GLU A 143 5 3
HELIX 3 3 SER A 168 GLN A 173 1 6
HELIX 4 4 ALA A 176 ALA A 180 5 5
HELIX 5 5 ASN B 34 GLY B 43 1 10
HELIX 6 6 ALA B 141 GLU B 143 5 3
HELIX 7 7 SER B 168 GLN B 173 1 6
HELIX 8 8 ALA B 176 ALA B 180 5 5
SHEET 1 AA 6 MET A 4 ARG A 8 0
SHEET 2 AA 6 ILE A 15 PRO A 19 -1 O LEU A 16 N THR A 7
SHEET 3 AA 6 GLN A 112 ILE A 115 -1 O GLN A 112 N PHE A 17
SHEET 4 AA 6 LYS A 74 LEU A 80 -1 O LYS A 74 N ILE A 115
SHEET 5 AA 6 TYR A 129 THR A 136 -1 O GLU A 131 N THR A 79
SHEET 6 AA 6 GLN A 50 ALA A 57 -1 O GLN A 50 N THR A 136
SHEET 1 AB 2 PHE A 22 ASP A 24 0
SHEET 2 AB 2 GLY A 27 PHE A 29 -1 O GLY A 27 N ASP A 24
SHEET 1 AC 5 TRP A 100 SER A 106 0
SHEET 2 AC 5 GLU A 82 ASP A 89 -1 O VAL A 83 N LEU A 105
SHEET 3 AC 5 PHE A 119 VAL A 125 -1 O ALA A 120 N VAL A 88
SHEET 4 AC 5 LEU A 61 GLN A 67 -1 O ARG A 62 N PHE A 123
SHEET 5 AC 5 GLU A 145 CYS A 147 -1 O ARG A 146 N TYR A 66
SHEET 1 BA 6 LYS B 5 ARG B 8 0
SHEET 2 BA 6 ILE B 15 GLU B 18 -1 O LEU B 16 N THR B 7
SHEET 3 BA 6 GLN B 112 ILE B 115 -1 O GLN B 112 N PHE B 17
SHEET 4 BA 6 LYS B 74 LEU B 80 -1 O LYS B 74 N ILE B 115
SHEET 5 BA 6 TYR B 129 THR B 136 -1 O GLU B 131 N THR B 79
SHEET 6 BA 6 GLN B 50 ALA B 57 -1 O GLN B 50 N THR B 136
SHEET 1 BB 2 PHE B 22 ASP B 24 0
SHEET 2 BB 2 GLY B 27 PHE B 29 -1 O GLY B 27 N ASP B 24
SHEET 1 BC 5 TRP B 100 SER B 106 0
SHEET 2 BC 5 GLU B 82 ASP B 89 -1 O VAL B 83 N LEU B 105
SHEET 3 BC 5 PHE B 119 VAL B 125 -1 O ALA B 120 N VAL B 88
SHEET 4 BC 5 LEU B 61 GLN B 67 -1 O ARG B 62 N PHE B 123
SHEET 5 BC 5 GLU B 145 CYS B 147 -1 O ARG B 146 N TYR B 66
CISPEP 1 GLY A 63 LEU A 64 0 -2.96
CISPEP 2 GLY B 63 LEU B 64 0 -3.67
SITE 1 AC1 22 PHE A 22 ARG A 26 PHE A 29 GLU A 31
SITE 2 AC1 22 GLN A 50 ARG A 62 HIS A 65 LYS A 74
SITE 3 AC1 22 HIS A 121 TYR A 134 TRP A 140 LYS A 170
SITE 4 AC1 22 HOH A2229 HOH A2253 HOH A2281 HOH A2282
SITE 5 AC1 22 HOH A2283 HOH A2284 HOH A2285 HOH A2286
SITE 6 AC1 22 HOH A2287 HOH A2288
SITE 1 AC2 22 PHE B 22 ARG B 26 PHE B 29 GLU B 31
SITE 2 AC2 22 GLN B 50 ARG B 62 HIS B 65 LYS B 74
SITE 3 AC2 22 HIS B 121 TYR B 134 TRP B 140 LYS B 170
SITE 4 AC2 22 HOH B2272 HOH B2293 HOH B2294 HOH B2295
SITE 5 AC2 22 HOH B2296 HOH B2297 HOH B2298 HOH B2299
SITE 6 AC2 22 HOH B2300 HOH B2301
CRYST1 64.915 125.537 109.366 90.00 90.00 90.00 C 2 2 21 16
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 0.015405 0.000000 0.000000 0.00000
SCALE2 0.000000 0.007966 0.000000 0.00000
SCALE3 0.000000 0.000000 0.009144 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
