HEADER ISOMERASE 24-MAR-06 2CIQ
TITLE STRUCTURE-BASED FUNCTIONAL ANNOTATION: YEAST YMR099C CODES FOR A D-
TITLE 2 HEXOSE-6-PHOSPHATE MUTAROTASE.
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: HEXOSE-6-PHOSPHATE MUTAROTASE;
COMPND 3 CHAIN: A;
COMPND 4 EC: 5.1.3.15;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;
SOURCE 3 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE 4 ORGANISM_TAXID: 559292;
SOURCE 5 STRAIN: S288C;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_VARIANT: ROSETTA PLYSS;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PET9
KEYWDS EPIMERASE, ISOMERASE, MANNOSE-6-PHOSPHATE-1-EPIMERASE, GALACTOSE-6-
KEYWDS 2 PHOSPHATE-1-EPIMERASE, D-HEXOSE-6-PHOSPHATE-1-MUTAROTASE
EXPDTA X-RAY DIFFRACTION
AUTHOR M.GRAILLE,J.-P.BALTAZE,N.LEULLIOT,D.LIGER,S.QUEVILLON-CHERUEL,H.VAN
AUTHOR 2 TILBEURGH
REVDAT 4 13-DEC-23 2CIQ 1 LINK
REVDAT 3 07-MAR-18 2CIQ 1 SOURCE AUTHOR JRNL
REVDAT 2 24-FEB-09 2CIQ 1 VERSN
REVDAT 1 11-JUL-06 2CIQ 0
JRNL AUTH M.GRAILLE,J.P.BALTAZE,N.LEULLIOT,D.LIGER,
JRNL AUTH 2 S.QUEVILLON-CHERUEL,H.VAN TILBEURGH
JRNL TITL STRUCTURE-BASED FUNCTIONAL ANNOTATION: YEAST YMR099C CODES
JRNL TITL 2 FOR A D-HEXOSE-6-PHOSPHATE MUTAROTASE.
JRNL REF J. BIOL. CHEM. V. 281 30175 2006
JRNL REFN ISSN 0021-9258
JRNL PMID 16857670
JRNL DOI 10.1074/JBC.M604443200
REMARK 2
REMARK 2 RESOLUTION. 1.70 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.2.0005
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) : 1.70
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 19.16
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 3 NUMBER OF REFLECTIONS : 37126
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) : 0.188
REMARK 3 R VALUE (WORKING SET) : 0.187
REMARK 3 FREE R VALUE : 0.219
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 1954
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) : 1.70
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.74
REMARK 3 REFLECTION IN BIN (WORKING SET) : 2668
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : 0.2310
REMARK 3 BIN FREE R VALUE SET COUNT : 140
REMARK 3 BIN FREE R VALUE : 0.2530
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2311
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 32
REMARK 3 SOLVENT ATOMS : 303
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 24.58
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.30000
REMARK 3 B22 (A**2) : 0.61000
REMARK 3 B33 (A**2) : -0.90000
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): 0.102
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.101
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.069
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 2.072
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.960
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.941
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 2401 ; 0.012 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 3264 ; 1.397 ; 1.967
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 286 ; 6.283 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 104 ;39.114 ;25.385
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 417 ;13.331 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 5 ;13.423 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 359 ; 0.095 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 1769 ; 0.006 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 1080 ; 0.203 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 1608 ; 0.315 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 229 ; 0.142 ; 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): 18 ; 0.326 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 14 ; 0.155 ; 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): 1435 ; 0.860 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 2340 ; 1.546 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1017 ; 2.477 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 924 ; 4.028 ; 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 2CIQ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 24-MAR-06.
REMARK 100 THE DEPOSITION ID IS D_1290028270.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 20-APR-05
REMARK 200 TEMPERATURE (KELVIN) : 100.0
REMARK 200 PH : 7.50
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : ID14-1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.978
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 : XDS
REMARK 200 DATA SCALING SOFTWARE : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 39082
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.700
REMARK 200 RESOLUTION RANGE LOW (A) : 20.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.4
REMARK 200 DATA REDUNDANCY : 3.500
REMARK 200 R MERGE (I) : 0.06000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 14.8000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.70
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.80
REMARK 200 COMPLETENESS FOR SHELL (%) : 98.2
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.41000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 4.900
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: PDB ENTRY 1JOV
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 50.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.80
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 25-30% POLYETHYLENE GLYCOL 3000, 0.2 M
REMARK 280 LITHIUM SULFATE, 0.1M HEPES PH 7.5, PH 7.50
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 2
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 53.09500
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 22.40000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 53.09500
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 22.40000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
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: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PQS
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 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 GLU A 289
REMARK 465 GLU A 290
REMARK 465 LEU A 291
REMARK 465 LYS A 292
REMARK 465 TYR A 293
REMARK 465 GLN A 294
REMARK 465 ALA A 295
REMARK 465 ILE A 296
REMARK 465 GLN A 297
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 A 2117 O HOH A 2173 2.09
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 ASP A 17 102.15 -162.24
REMARK 500 SER A 38 -15.16 88.67
REMARK 500 PRO A 121 49.67 -83.07
REMARK 500 ASP A 135 23.46 -140.26
REMARK 500 ASN A 174 16.54 87.52
REMARK 500 ASP A 203 86.65 -152.68
REMARK 500 TRP A 241 -161.21 61.93
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 A2007 DISTANCE = 6.56 ANGSTROMS
REMARK 525 HOH A2041 DISTANCE = 6.02 ANGSTROMS
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA A1290 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU A 74 OE2
REMARK 620 2 ALA A 249 O 126.3
REMARK 620 3 GLU A 252 OE2 93.2 106.9
REMARK 620 4 HOH A2099 O 72.7 85.8 165.2
REMARK 620 5 HOH A2265 O 155.7 71.3 96.9 94.3
REMARK 620 6 HOH A2268 O 86.0 144.6 82.4 91.6 73.6
REMARK 620 N 1 2 3 4 5
REMARK 700
REMARK 700 SHEET
REMARK 700 THE SHEET STRUCTURE OF THIS MOLECULE IS BIFURCATED. IN
REMARK 700 ORDER TO REPRESENT THIS FEATURE IN THE SHEET RECORDS BELOW,
REMARK 700 TWO SHEETS ARE DEFINED.
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA A1290
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A1292
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A1293
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EPE A1289
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A1291
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2CIR RELATED DB: PDB
REMARK 900 STRUCTURE-BASED FUNCTIONAL ANNOTATION: YEAST YMR099C CODES FOR A D-
REMARK 900 HEXOSE-6-PHOSPHATE MUTAROTASE. COMPLEX WITH GLUCOSE-6-PHOSPHATE
REMARK 900 RELATED ID: 2CIS RELATED DB: PDB
REMARK 900 STRUCTURE-BASED FUNCTIONAL ANNOTATION: YEAST YMR099C CODES FOR A D-
REMARK 900 HEXOSE-6-PHOSPHATE MUTAROTASE. COMPLEX WITH TAGATOSE-6-PHOSPHATE
DBREF 2CIQ A 1 297 UNP Q03161 YMY9_YEAST 1 297
SEQRES 1 A 297 MET PRO ILE LYS GLU THR ASP LYS GLU VAL VAL LEU THR
SEQRES 2 A 297 HIS PRO ALA ASP GLU THR THR SER VAL HIS ILE LEU LYS
SEQRES 3 A 297 TYR GLY ALA THR VAL TYR SER TRP LYS LEU LYS SER GLU
SEQRES 4 A 297 GLU GLN LEU TRP LEU SER THR ALA ALA LYS LEU ASP GLY
SEQRES 5 A 297 SER LYS PRO VAL ARG GLY GLY ILE PRO LEU VAL PHE PRO
SEQRES 6 A 297 VAL PHE GLY LYS ASN SER THR ASP GLU HIS LEU SER LYS
SEQRES 7 A 297 LEU PRO GLN HIS GLY LEU ALA ARG ASN SER THR TRP GLU
SEQRES 8 A 297 PHE LEU GLY GLN THR LYS GLU ASN PRO PRO THR VAL GLN
SEQRES 9 A 297 PHE GLY LEU LYS PRO GLU ILE ALA ASN PRO GLU LEU THR
SEQRES 10 A 297 LYS LEU TRP PRO MET ASP TYR LEU LEU ILE LEU THR VAL
SEQRES 11 A 297 GLU LEU GLY SER ASP TYR LEU LYS THR ALA ILE GLU VAL
SEQRES 12 A 297 GLU ASN THR SER SER SER LYS GLU LEU LYS PHE ASN TRP
SEQRES 13 A 297 LEU PHE HIS THR TYR PHE ARG ILE GLU ASP ILE GLU GLY
SEQRES 14 A 297 THR MET VAL SER ASN LEU ALA GLY MET LYS LEU TYR ASP
SEQRES 15 A 297 GLN LEU LEU LYS GLU SER TYR VAL ASP LYS HIS PRO VAL
SEQRES 16 A 297 VAL THR PHE ASN GLN GLU THR ASP VAL ILE TYR GLN ASN
SEQRES 17 A 297 VAL SER ALA GLU ARG ALA ILE GLN ILE VAL ASP LYS GLY
SEQRES 18 A 297 VAL GLN ILE HIS THR LEU LYS ARG TYR ASN LEU PRO ASP
SEQRES 19 A 297 THR VAL VAL TRP ASN PRO TRP ILE GLU LYS SER GLN GLY
SEQRES 20 A 297 MET ALA ASP PHE GLU PRO LYS THR GLY TYR GLN GLN MET
SEQRES 21 A 297 ILE CYS ILE GLU PRO GLY HIS VAL HIS ASP PHE ILE SER
SEQRES 22 A 297 LEU ALA PRO GLY LYS LYS TRP ASN ALA TYR GLN LEU LEU
SEQRES 23 A 297 CYS LYS GLU GLU LEU LYS TYR GLN ALA ILE GLN
HET EPE A1289 15
HET NA A1290 1
HET GOL A1291 6
HET SO4 A1292 5
HET SO4 A1293 5
HETNAM EPE 4-(2-HYDROXYETHYL)-1-PIPERAZINE ETHANESULFONIC ACID
HETNAM NA SODIUM ION
HETNAM GOL GLYCEROL
HETNAM SO4 SULFATE ION
HETSYN EPE HEPES
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 2 EPE C8 H18 N2 O4 S
FORMUL 3 NA NA 1+
FORMUL 4 GOL C3 H8 O3
FORMUL 5 SO4 2(O4 S 2-)
FORMUL 7 HOH *303(H2 O)
HELIX 1 1 HIS A 75 LEU A 79 5 5
HELIX 2 2 LEU A 84 SER A 88 5 5
HELIX 3 3 LYS A 108 ALA A 112 5 5
HELIX 4 4 ASN A 113 TRP A 120 1 8
HELIX 5 5 ASP A 166 GLU A 168 5 3
HELIX 6 6 PRO A 240 MET A 248 1 9
HELIX 7 7 THR A 255 GLN A 258 5 4
SHEET 1 AA 5 ILE A 3 GLU A 5 0
SHEET 2 AA 5 GLU A 9 HIS A 14 -1 O VAL A 11 N LYS A 4
SHEET 3 AA 5 ASP A 17 LEU A 25 -1 N ASP A 17 O HIS A 14
SHEET 4 AA 5 THR A 30 LEU A 36 -1 O THR A 30 N LEU A 25
SHEET 5 AA 5 GLU A 39 GLU A 40 -1 O GLU A 39 N LEU A 36
SHEET 1 AB 4 LEU A 62 VAL A 63 0
SHEET 2 AB 4 LEU A 152 PHE A 158 -1 O LEU A 157 N VAL A 63
SHEET 3 AB 4 MET A 260 LEU A 274 -1 O PRO A 265 N PHE A 158
SHEET 4 AB 4 TYR A 161 ARG A 163 -1 O PHE A 162 N ILE A 261
SHEET 1 AC 7 LEU A 62 VAL A 63 0
SHEET 2 AC 7 LEU A 152 PHE A 158 -1 O LEU A 157 N VAL A 63
SHEET 3 AC 7 MET A 260 LEU A 274 -1 O PRO A 265 N PHE A 158
SHEET 4 AC 7 ASP A 234 ASN A 239 -1 O ASP A 234 N GLY A 266
SHEET 5 AC 7 THR A 202 TYR A 206 -1 O THR A 202 N ASN A 239
SHEET 6 AC 7 LYS A 179 ASP A 182 -1 O TYR A 181 N ILE A 205
SHEET 7 AC 7 GLU A 187 VAL A 190 -1 O GLU A 187 N ASP A 182
SHEET 1 AD 9 GLU A 91 LYS A 97 0
SHEET 2 AD 9 THR A 102 LEU A 107 -1 O THR A 102 N THR A 96
SHEET 3 AD 9 LEU A 125 LEU A 132 -1 O LEU A 126 N LEU A 107
SHEET 4 AD 9 TYR A 136 GLU A 144 -1 O LYS A 138 N GLU A 131
SHEET 5 AD 9 LYS A 279 CYS A 287 -1 O TRP A 280 N VAL A 143
SHEET 6 AD 9 VAL A 222 TYR A 230 -1 O THR A 226 N CYS A 287
SHEET 7 AD 9 ILE A 215 ASP A 219 -1 O ILE A 215 N LEU A 227
SHEET 8 AD 9 THR A 170 SER A 173 -1 O MET A 171 N VAL A 218
SHEET 9 AD 9 VAL A 195 VAL A 196 -1 O VAL A 196 N VAL A 172
LINK OE2 GLU A 74 NA NA A1290 3555 1555 2.53
LINK O ALA A 249 NA NA A1290 1555 1555 2.40
LINK OE2 GLU A 252 NA NA A1290 1555 1555 2.38
LINK NA NA A1290 O HOH A2099 1555 3555 2.40
LINK NA NA A1290 O HOH A2265 1555 1555 2.31
LINK NA NA A1290 O HOH A2268 1555 1555 2.39
CISPEP 1 PHE A 64 PRO A 65 0 -0.36
CISPEP 2 ASN A 99 PRO A 100 0 1.37
CISPEP 3 GLU A 252 PRO A 253 0 -6.76
SITE 1 AC1 6 GLU A 74 ALA A 249 GLU A 252 HOH A2099
SITE 2 AC1 6 HOH A2265 HOH A2268
SITE 1 AC2 6 ARG A 57 GLN A 81 ARG A 86 HOH A2300
SITE 2 AC2 6 HOH A2301 HOH A2303
SITE 1 AC3 2 ASN A 199 GLN A 200
SITE 1 AC4 9 ASN A 99 SER A 210 ALA A 211 TYR A 230
SITE 2 AC4 9 ASN A 231 TRP A 280 HOH A2235 HOH A2296
SITE 3 AC4 9 HOH A2297
SITE 1 AC5 9 PHE A 67 HIS A 82 HIS A 159 GLN A 183
SITE 2 AC5 9 ASP A 203 GLU A 264 HOH A2110 HOH A2299
SITE 3 AC5 9 HOH A2300
CRYST1 106.190 44.800 73.990 90.00 90.00 90.00 P 21 21 2 4
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 0.009417 0.000000 0.000000 0.00000
SCALE2 0.000000 0.022321 0.000000 0.00000
SCALE3 0.000000 0.000000 0.013515 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
