HEADER ISOMERASE 26-MAR-15 4Z0J
TITLE F96S/S73A DOUBLE MUTANT OF PLASMODIUM FALCIPARUM TRIOSEPHOSPHATE
TITLE 2 ISOMERASE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: TRIOSEPHOSPHATE ISOMERASE;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: TIM,TRIOSE-PHOSPHATE ISOMERASE;
COMPND 5 EC: 5.3.1.1;
COMPND 6 ENGINEERED: YES;
COMPND 7 MUTATION: YES;
COMPND 8 OTHER_DETAILS: MUTATION OF A163V PRESENT IN THE WILD TYPE TIM
COMPND 9 CONSIDERED AS TEMPLATE
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: PLASMODIUM FALCIPARUM;
SOURCE 3 ORGANISM_TAXID: 5833;
SOURCE 4 GENE: TPI;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: AA200;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PTRC99A
KEYWDS TIM BARRELS, BETA-ALPHA BARRELS, ISOMERASE, GLYCOLYSIS
EXPDTA X-RAY DIFFRACTION
AUTHOR V.PAREEK,P.BALARAM,M.R.N.MURTHY
REVDAT 3 08-NOV-23 4Z0J 1 REMARK
REVDAT 2 20-APR-16 4Z0J 1 JRNL
REVDAT 1 03-FEB-16 4Z0J 0
JRNL AUTH V.PAREEK,M.SAMANTA,N.V.JOSHI,H.BALARAM,M.R.N.MURTHY,
JRNL AUTH 2 P.BALARAM
JRNL TITL CONNECTING ACTIVE-SITE LOOP CONFORMATIONS AND CATALYSIS IN
JRNL TITL 2 TRIOSEPHOSPHATE ISOMERASE: INSIGHTS FROM A RARE VARIATION AT
JRNL TITL 3 RESIDUE 96 IN THE PLASMODIAL ENZYME
JRNL REF CHEMBIOCHEM V. 17 620 2016
JRNL REFN ESSN 1439-7633
JRNL PMID 26762569
JRNL DOI 10.1002/CBIC.201500532
REMARK 2
REMARK 2 RESOLUTION. 2.07 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0049
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) : 53.45
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 94.0
REMARK 3 NUMBER OF REFLECTIONS : 27919
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) : 0.219
REMARK 3 R VALUE (WORKING SET) : 0.217
REMARK 3 FREE R VALUE : 0.260
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 1471
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) : 2.20
REMARK 3 REFLECTION IN BIN (WORKING SET) : 478
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 21.98
REMARK 3 BIN R VALUE (WORKING SET) : 0.2610
REMARK 3 BIN FREE R VALUE SET COUNT : 30
REMARK 3 BIN FREE R VALUE : 0.2750
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 3840
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 63
REMARK 3 SOLVENT ATOMS : 301
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 9.44
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.00000
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): 0.280
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.212
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.149
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 5.291
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.887
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.843
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 3960 ; 0.006 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 3782 ; 0.001 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 5336 ; 1.078 ; 1.953
REMARK 3 BOND ANGLES OTHERS (DEGREES): 8690 ; 0.737 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 495 ; 5.970 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 185 ;37.413 ;25.514
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 706 ;12.288 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 16 ;10.964 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 614 ; 0.062 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 4482 ; 0.003 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 894 ; 0.001 ; 0.020
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): 1967 ; 0.281 ; 0.930
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 1966 ; 0.281 ; 0.930
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 2456 ; 0.507 ; 1.394
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): 2457 ; 0.507 ; 1.394
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1993 ; 0.234 ; 0.961
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): 1981 ; 0.235 ; 0.964
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): 2852 ; 0.400 ; 1.423
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): 4775 ; 2.055 ; 7.582
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): 4776 ; 2.055 ; 7.584
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 4Z0J COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 09-APR-15.
REMARK 100 THE DEPOSITION ID IS D_1000208253.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 29-SEP-09
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 4.5
REMARK 200 NUMBER OF CRYSTALS USED : NULL
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : ROTATING ANODE
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : BRUKER AXS MICROSTAR
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.54
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : MAR SCANNER 345 MM PLATE
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : IMOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 29180
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.070
REMARK 200 RESOLUTION RANGE LOW (A) : 53.450
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.9
REMARK 200 DATA REDUNDANCY : 3.300
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 7.0000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.07
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.20
REMARK 200 COMPLETENESS FOR SHELL (%) : 93.0
REMARK 200 DATA REDUNDANCY IN SHELL : 3.30
REMARK 200 R MERGE FOR SHELL (I) : 0.36000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.800
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: 2VFD
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 43.22
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.17
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: NAOAC, 10MM LI2SO4, 0.5MM DTT, 0.5MM
REMARK 280 NAN3, 0.5MM EDTA, 28% PEG 1450, PH 4.5, VAPOR DIFFUSION, HANGING
REMARK 280 DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,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 25.42000
REMARK 290 SMTRY3 2 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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 3770 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 19460 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -65.0 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 1
REMARK 465 GLY A 171
REMARK 465 THR A 172
REMARK 465 GLY A 173
REMARK 465 MET B 1
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 ALA A 2 CB
REMARK 470 LYS A 21 CD CE NZ
REMARK 470 HIS A 50 ND1 CE1 NE2
REMARK 470 LYS A 118 CE NZ
REMARK 470 GLU A 135 OE2
REMARK 470 ASN A 137 ND2
REMARK 470 GLU A 141 OE2
REMARK 470 ASP A 155 CG OD1 OD2
REMARK 470 ILE A 170 O
REMARK 470 LYS A 174 CE NZ
REMARK 470 THR A 175 CB OG1 CG2
REMARK 470 LYS A 193 NZ
REMARK 470 LYS A 199 NZ
REMARK 470 GLU A 215 OE1
REMARK 470 GLN A 222 CD OE1 NE2
REMARK 470 GLU A 224 CD OE1 OE2
REMARK 470 ASN A 233 OD1 ND2
REMARK 470 LYS A 237 CE NZ
REMARK 470 LYS A 245 NZ
REMARK 470 ALA B 2 N
REMARK 470 LYS B 21 CE NZ
REMARK 470 LYS B 36 CE NZ
REMARK 470 LYS B 53 CD CE NZ
REMARK 470 LYS B 100 NZ
REMARK 470 HIS B 103 NE2
REMARK 470 ASN B 120 OD1
REMARK 470 LYS B 138 NZ
REMARK 470 LYS B 145 CE NZ
REMARK 470 ILE B 170 CD1
REMARK 470 LYS B 174 NZ
REMARK 470 LYS B 199 CE NZ
REMARK 470 GLU B 224 CG CD OE1 OE2
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 LYS A 12 -140.19 43.38
REMARK 500 LYS B 12 -147.19 51.10
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 EDO A 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 303
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 304
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 305
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 306
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO B 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO B 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO B 303
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO B 304
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO B 305
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO B 306
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO B 307
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO B 308
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 B 309
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4YXG RELATED DB: PDB
REMARK 900 RELATED ID: 4YWI RELATED DB: PDB
REMARK 900 RELATED ID: 2VFD RELATED DB: PDB
REMARK 900 RELATED ID: 2VFE RELATED DB: PDB
REMARK 900 RELATED ID: 2VFF RELATED DB: PDB
REMARK 900 RELATED ID: 2VFG RELATED DB: PDB
REMARK 900 RELATED ID: 2VFH RELATED DB: PDB
REMARK 900 RELATED ID: 4Z0S RELATED DB: PDB
DBREF 4Z0J A 1 248 UNP Q07412 TPIS_PLAFA 1 248
DBREF 4Z0J B 1 248 UNP Q07412 TPIS_PLAFA 1 248
SEQADV 4Z0J ALA A 73 UNP Q07412 SER 73 ENGINEERED MUTATION
SEQADV 4Z0J SER A 96 UNP Q07412 PHE 96 ENGINEERED MUTATION
SEQADV 4Z0J VAL A 163 UNP Q07412 ALA 163 ENGINEERED MUTATION
SEQADV 4Z0J ALA B 73 UNP Q07412 SER 73 ENGINEERED MUTATION
SEQADV 4Z0J SER B 96 UNP Q07412 PHE 96 ENGINEERED MUTATION
SEQADV 4Z0J VAL B 163 UNP Q07412 ALA 163 ENGINEERED MUTATION
SEQRES 1 A 248 MET ALA ARG LYS TYR PHE VAL ALA ALA ASN TRP LYS CYS
SEQRES 2 A 248 ASN GLY THR LEU GLU SER ILE LYS SER LEU THR ASN SER
SEQRES 3 A 248 PHE ASN ASN LEU ASP PHE ASP PRO SER LYS LEU ASP VAL
SEQRES 4 A 248 VAL VAL PHE PRO VAL SER VAL HIS TYR ASP HIS THR ARG
SEQRES 5 A 248 LYS LEU LEU GLN SER LYS PHE SER THR GLY ILE GLN ASN
SEQRES 6 A 248 VAL SER LYS PHE GLY ASN GLY ALA TYR THR GLY GLU VAL
SEQRES 7 A 248 SER ALA GLU ILE ALA LYS ASP LEU ASN ILE GLU TYR VAL
SEQRES 8 A 248 ILE ILE GLY HIS SER GLU ARG ARG LYS TYR PHE HIS GLU
SEQRES 9 A 248 THR ASP GLU ASP VAL ARG GLU LYS LEU GLN ALA SER LEU
SEQRES 10 A 248 LYS ASN ASN LEU LYS ALA VAL VAL CYS PHE GLY GLU SER
SEQRES 11 A 248 LEU GLU GLN ARG GLU GLN ASN LYS THR ILE GLU VAL ILE
SEQRES 12 A 248 THR LYS GLN VAL LYS ALA PHE VAL ASP LEU ILE ASP ASN
SEQRES 13 A 248 PHE ASP ASN VAL ILE LEU VAL TYR GLU PRO LEU TRP ALA
SEQRES 14 A 248 ILE GLY THR GLY LYS THR ALA THR PRO GLU GLN ALA GLN
SEQRES 15 A 248 LEU VAL HIS LYS GLU ILE ARG LYS ILE VAL LYS ASP THR
SEQRES 16 A 248 CYS GLY GLU LYS GLN ALA ASN GLN ILE ARG ILE LEU TYR
SEQRES 17 A 248 GLY GLY SER VAL ASN THR GLU ASN CYS SER SER LEU ILE
SEQRES 18 A 248 GLN GLN GLU ASP ILE ASP GLY PHE LEU VAL GLY ASN ALA
SEQRES 19 A 248 SER LEU LYS GLU SER PHE VAL ASP ILE ILE LYS SER ALA
SEQRES 20 A 248 MET
SEQRES 1 B 248 MET ALA ARG LYS TYR PHE VAL ALA ALA ASN TRP LYS CYS
SEQRES 2 B 248 ASN GLY THR LEU GLU SER ILE LYS SER LEU THR ASN SER
SEQRES 3 B 248 PHE ASN ASN LEU ASP PHE ASP PRO SER LYS LEU ASP VAL
SEQRES 4 B 248 VAL VAL PHE PRO VAL SER VAL HIS TYR ASP HIS THR ARG
SEQRES 5 B 248 LYS LEU LEU GLN SER LYS PHE SER THR GLY ILE GLN ASN
SEQRES 6 B 248 VAL SER LYS PHE GLY ASN GLY ALA TYR THR GLY GLU VAL
SEQRES 7 B 248 SER ALA GLU ILE ALA LYS ASP LEU ASN ILE GLU TYR VAL
SEQRES 8 B 248 ILE ILE GLY HIS SER GLU ARG ARG LYS TYR PHE HIS GLU
SEQRES 9 B 248 THR ASP GLU ASP VAL ARG GLU LYS LEU GLN ALA SER LEU
SEQRES 10 B 248 LYS ASN ASN LEU LYS ALA VAL VAL CYS PHE GLY GLU SER
SEQRES 11 B 248 LEU GLU GLN ARG GLU GLN ASN LYS THR ILE GLU VAL ILE
SEQRES 12 B 248 THR LYS GLN VAL LYS ALA PHE VAL ASP LEU ILE ASP ASN
SEQRES 13 B 248 PHE ASP ASN VAL ILE LEU VAL TYR GLU PRO LEU TRP ALA
SEQRES 14 B 248 ILE GLY THR GLY LYS THR ALA THR PRO GLU GLN ALA GLN
SEQRES 15 B 248 LEU VAL HIS LYS GLU ILE ARG LYS ILE VAL LYS ASP THR
SEQRES 16 B 248 CYS GLY GLU LYS GLN ALA ASN GLN ILE ARG ILE LEU TYR
SEQRES 17 B 248 GLY GLY SER VAL ASN THR GLU ASN CYS SER SER LEU ILE
SEQRES 18 B 248 GLN GLN GLU ASP ILE ASP GLY PHE LEU VAL GLY ASN ALA
SEQRES 19 B 248 SER LEU LYS GLU SER PHE VAL ASP ILE ILE LYS SER ALA
SEQRES 20 B 248 MET
HET EDO A 301 4
HET EDO A 302 4
HET EDO A 303 4
HET EDO A 304 4
HET SO4 A 305 5
HET SO4 A 306 5
HET EDO B 301 4
HET EDO B 302 4
HET EDO B 303 4
HET EDO B 304 4
HET EDO B 305 4
HET EDO B 306 4
HET EDO B 307 4
HET EDO B 308 4
HET SO4 B 309 5
HETNAM EDO 1,2-ETHANEDIOL
HETNAM SO4 SULFATE ION
HETSYN EDO ETHYLENE GLYCOL
FORMUL 3 EDO 12(C2 H6 O2)
FORMUL 7 SO4 3(O4 S 2-)
FORMUL 18 HOH *301(H2 O)
HELIX 1 AA1 THR A 16 ASN A 29 1 14
HELIX 2 AA2 VAL A 44 VAL A 46 5 3
HELIX 3 AA3 HIS A 47 LEU A 55 1 9
HELIX 4 AA4 SER A 79 LEU A 86 1 8
HELIX 5 AA5 HIS A 95 PHE A 102 1 8
HELIX 6 AA6 THR A 105 ASN A 119 1 15
HELIX 7 AA7 SER A 130 GLN A 136 1 7
HELIX 8 AA8 LYS A 138 ALA A 149 1 12
HELIX 9 AA9 PHE A 150 ILE A 154 5 5
HELIX 10 AB1 THR A 177 GLY A 197 1 21
HELIX 11 AB2 GLY A 197 ILE A 204 1 8
HELIX 12 AB3 ASN A 216 GLN A 222 1 7
HELIX 13 AB4 GLY A 232 GLU A 238 5 7
HELIX 14 AB5 SER A 239 ALA A 247 1 9
HELIX 15 AB6 THR B 16 ASN B 29 1 14
HELIX 16 AB7 VAL B 44 VAL B 46 5 3
HELIX 17 AB8 HIS B 47 LEU B 55 1 9
HELIX 18 AB9 SER B 79 LEU B 86 1 8
HELIX 19 AC1 HIS B 95 PHE B 102 1 8
HELIX 20 AC2 THR B 105 ASN B 119 1 15
HELIX 21 AC3 SER B 130 GLN B 136 1 7
HELIX 22 AC4 LYS B 138 ALA B 149 1 12
HELIX 23 AC5 PHE B 150 ILE B 154 5 5
HELIX 24 AC6 PRO B 166 ILE B 170 5 5
HELIX 25 AC7 THR B 177 CYS B 196 1 20
HELIX 26 AC8 GLY B 197 ILE B 204 1 8
HELIX 27 AC9 ASN B 216 GLN B 222 1 7
HELIX 28 AD1 GLY B 232 GLU B 238 5 7
HELIX 29 AD2 SER B 239 ALA B 247 1 9
SHEET 1 AA1 9 TYR A 5 ASN A 10 0
SHEET 2 AA1 9 LEU A 37 PHE A 42 1 O VAL A 40 N ALA A 9
SHEET 3 AA1 9 SER A 60 ILE A 63 1 O SER A 60 N VAL A 39
SHEET 4 AA1 9 TYR A 90 ILE A 93 1 O TYR A 90 N ILE A 63
SHEET 5 AA1 9 LYS A 122 PHE A 127 1 O CYS A 126 N ILE A 93
SHEET 6 AA1 9 VAL A 160 TYR A 164 1 O ILE A 161 N ALA A 123
SHEET 7 AA1 9 ARG A 205 TYR A 208 1 O LEU A 207 N LEU A 162
SHEET 8 AA1 9 GLY A 228 VAL A 231 1 O GLY A 228 N TYR A 208
SHEET 9 AA1 9 TYR A 5 ASN A 10 1 N ALA A 8 O VAL A 231
SHEET 1 AA2 9 PHE B 6 ASN B 10 0
SHEET 2 AA2 9 ASP B 38 PHE B 42 1 O VAL B 40 N ALA B 9
SHEET 3 AA2 9 SER B 60 ILE B 63 1 O SER B 60 N VAL B 39
SHEET 4 AA2 9 TYR B 90 ILE B 93 1 O ILE B 92 N ILE B 63
SHEET 5 AA2 9 LYS B 122 PHE B 127 1 O VAL B 124 N VAL B 91
SHEET 6 AA2 9 VAL B 160 TYR B 164 1 O ILE B 161 N VAL B 125
SHEET 7 AA2 9 ILE B 206 TYR B 208 1 O LEU B 207 N LEU B 162
SHEET 8 AA2 9 GLY B 228 VAL B 231 1 O GLY B 228 N TYR B 208
SHEET 9 AA2 9 PHE B 6 ASN B 10 1 N ALA B 8 O VAL B 231
SITE 1 AC1 8 SER A 45 VAL A 46 TYR A 48 ASP A 49
SITE 2 AC1 8 LEU A 86 HOH A 484 VAL B 46 HOH B 404
SITE 1 AC2 4 LEU A 117 ASN A 120 ASN A 159 HOH A 412
SITE 1 AC3 7 CYS A 196 GLY A 197 HOH A 404 HOH A 433
SITE 2 AC3 7 ARG B 52 LYS B 53 LEU B 55
SITE 1 AC4 5 ASN A 71 GLU A 81 HOH A 420 GLY B 15
SITE 2 AC4 5 THR B 16
SITE 1 AC5 6 ASN A 65 ARG A 98 GLU A 104 LYS A 112
SITE 2 AC5 6 HOH A 466 HOH A 507
SITE 1 AC6 7 SER A 211 GLY A 232 ASN A 233 HOH A 424
SITE 2 AC6 7 HOH A 432 HOH A 446 HOH A 451
SITE 1 AC7 3 ASN B 137 ILE B 140 EDO B 303
SITE 1 AC8 3 HIS A 50 ASP B 49 HOH B 448
SITE 1 AC9 5 ASN B 137 LYS B 138 ILE B 140 GLU B 141
SITE 2 AC9 5 EDO B 301
SITE 1 AD1 4 SER B 19 SER B 22 LEU B 23 GLU B 238
SITE 1 AD2 4 LYS B 186 LYS B 190 HOH B 417 HOH B 460
SITE 1 AD3 6 LEU B 117 ASN B 120 LEU B 121 ASP B 155
SITE 2 AD3 6 ASN B 156 ASN B 159
SITE 1 AD4 5 LYS A 148 HOH A 428 SER B 60 GLU B 89
SITE 2 AD4 5 HOH B 429
SITE 1 AD5 4 SER B 211 GLY B 232 ASN B 233 HOH B 437
SITE 1 AD6 4 ASN B 65 ARG B 98 GLU B 104 LYS B 112
CRYST1 53.480 50.840 88.260 90.00 91.74 90.00 P 1 21 1 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 0.018699 0.000000 0.000568 0.00000
SCALE2 0.000000 0.019670 0.000000 0.00000
SCALE3 0.000000 0.000000 0.011335 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
