HEADER TRANSFERASE 11-JUL-17 5XZ7
TITLE CRYSTAL STRUCTURE OF PHOSPHOFRUCTOKINASE FROM STAPHYLOCOCCUS AUREUS IN
TITLE 2 COMPLEX WITH ADENYLYLIMIDODIPHOSPHATE, THE ATP ANALOGUE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ATP-DEPENDENT 6-PHOSPHOFRUCTOKINASE;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: PHOSPHOFRUCTOKINASE,PHOSPHOHEXOKINASE;
COMPND 5 EC: 2.7.1.11;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: STAPHYLOCOCCUS AUREUS (STRAIN NCTC 8325);
SOURCE 3 ORGANISM_TAXID: 93061;
SOURCE 4 STRAIN: NCTC 8325;
SOURCE 5 GENE: PFKA, SAOUHSC_01807;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS PHOSPHOFRUCTOKINASE, STAPHYLOCOCCUS AUREUS, TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR C.L.WANG,T.TIAN,J.Y.ZANG
REVDAT 4 22-NOV-23 5XZ7 1 REMARK HETSYN
REVDAT 3 29-JUL-20 5XZ7 1 COMPND REMARK HETNAM SITE
REVDAT 2 22-MAY-19 5XZ7 1 SOURCE DBREF SEQADV
REVDAT 1 13-MAR-19 5XZ7 0
JRNL AUTH T.TIAN,C.L.WANG,M.H.WU,X.ZHANG,J.Y.ZANG
JRNL TITL STRUCTURAL INSIGHTS INTO THE REGULATION OF STAPHYLOCOCCUS
JRNL TITL 2 AUREUS PHOSPHOFRUCTOKINASE BY TETRAMER-DIMER CONVERSION.
JRNL REF BIOCHEMISTRY V. 57 4252 2018
JRNL REFN ISSN 1520-4995
JRNL PMID 29940104
JRNL DOI 10.1021/ACS.BIOCHEM.8B00028
REMARK 2
REMARK 2 RESOLUTION. 1.60 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0103
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) : 1.60
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 66.90
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 3 NUMBER OF REFLECTIONS : 45110
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) : 0.155
REMARK 3 R VALUE (WORKING SET) : 0.154
REMARK 3 FREE R VALUE : 0.179
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 2404
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) : 1.60
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.64
REMARK 3 REFLECTION IN BIN (WORKING SET) : 3257
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 100.0
REMARK 3 BIN R VALUE (WORKING SET) : 0.2080
REMARK 3 BIN FREE R VALUE SET COUNT : 198
REMARK 3 BIN FREE R VALUE : 0.2090
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2446
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 59
REMARK 3 SOLVENT ATOMS : 283
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 12.60
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 15.54
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.56000
REMARK 3 B22 (A**2) : -0.23000
REMARK 3 B33 (A**2) : -0.33000
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): 0.071
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.072
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.044
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 1.255
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.965
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.955
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 2499 ; 0.026 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 2407 ; 0.004 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 3376 ; 2.217 ; 1.967
REMARK 3 BOND ANGLES OTHERS (DEGREES): 5507 ; 1.149 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 328 ; 5.028 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 106 ;35.488 ;24.245
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 416 ;12.535 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 17 ;14.811 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 391 ; 0.141 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 2873 ; 0.011 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 554 ; 0.002 ; 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): 1306 ; 1.653 ; 1.340
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 1305 ; 1.640 ; 1.337
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 1634 ; 2.336 ; 1.996
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): 1635 ; 2.341 ; 1.998
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1193 ; 3.070 ; 1.680
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): 1193 ; 3.070 ; 1.680
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): 1743 ; 4.496 ; 2.386
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): 3077 ; 6.053 ;12.422
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): 3077 ; 6.053 ;12.422
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 5XZ7 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 21-JUL-17.
REMARK 100 THE DEPOSITION ID IS D_1300003902.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 15-DEC-13
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SSRF
REMARK 200 BEAMLINE : BL17U1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9793
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315R
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : IMOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 47521
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.600
REMARK 200 RESOLUTION RANGE LOW (A) : 66.900
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 6.200
REMARK 200 R MERGE (I) : 0.10700
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 11.6000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.60
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.69
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 5.30
REMARK 200 R MERGE FOR SHELL (I) : 0.41700
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 4.300
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: 5XOE
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 51.95
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.56
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 15% PEG4000, 0.1M MES PH 6.0 ,
REMARK 280 0.15M(NH4)2SO4, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 283K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 2 2 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,Y,-Z
REMARK 290 4555 X,-Y,-Z
REMARK 290 5555 X+1/2,Y+1/2,Z+1/2
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+1/2
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 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000
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 36.78000
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 40.10000
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 60.65000
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 36.78000
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 40.10000
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 60.65000
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 36.78000
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 40.10000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 60.65000
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 36.78000
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 40.10000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 60.65000
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: 7540 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 24290 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -28.0 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 73.56000
REMARK 350 BIOMT2 2 0.000000 -1.000000 0.000000 80.20000
REMARK 350 BIOMT3 2 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 GLY A 304
REMARK 465 LYS A 305
REMARK 465 ASP A 306
REMARK 465 HIS A 307
REMARK 465 HIS A 327
REMARK 465 HIS A 328
REMARK 465 HIS A 329
REMARK 465 HIS A 330
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 GLU A 80 CG CD OE1 OE2
REMARK 470 MET A 278 CE
REMARK 480
REMARK 480 ZERO OCCUPANCY ATOM
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 480 M RES C SSEQI ATOMS
REMARK 480 LYS A 2 C NZ
REMARK 480 LYS A 83 CG CD CE NZ
REMARK 480 LYS A 201 C CE NZ
REMARK 480 ASP A 205 CG OD1 OD2
REMARK 480 LYS A 206 CG CD CE NZ
REMARK 480 GLN A 209 CG CD OE1 NE2
REMARK 480 LYS A 212 CG CD CE NZ
REMARK 480 ARG A 213 CG CD NE CZ NH1 NH2
REMARK 480 LYS A 216 CG CD CE NZ
REMARK 480 GLN A 230 C CD OE1 NE2
REMARK 480 LYS A 234 CD CE NZ
REMARK 480 LYS A 292 CD CE NZ
REMARK 480 ASP A 303 CG OD1 OD2
REMARK 480 GLU A 324 CG CD OE1 OE2
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 505 O HOH A 751 1.67
REMARK 500 O HOH A 755 O HOH A 774 1.78
REMARK 500 NH1 ARG A 213 O HIS A 326 1.90
REMARK 500 CZ ARG A 213 O HIS A 326 1.96
REMARK 500 NH1 ARG A 213 CA HIS A 326 1.99
REMARK 500 CD ARG A 156 O HOH A 525 2.00
REMARK 500 CD1 PHE A 67 O HOH A 659 2.02
REMARK 500 O HOH A 577 O HOH A 715 2.05
REMARK 500 CE1 PHE A 67 O HOH A 659 2.06
REMARK 500 OE2 GLU A 33 NZ LYS A 51 2.12
REMARK 500 NH1 ARG A 164 OD2 ASP A 243 2.13
REMARK 500 O HOH A 512 O HOH A 709 2.18
REMARK 500 NH1 ARG A 213 C HIS A 326 2.18
REMARK 500 O HOH A 509 O HOH A 548 2.19
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 626 O HOH A 747 4565 1.74
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 RES CSSEQI ATM2 DEVIATION
REMARK 500 GLU A 95 CD GLU A 95 OE1 -0.075
REMARK 500 LYS A 201 C LYS A 201 O -0.164
REMARK 500 GLN A 230 CG GLN A 230 CD 0.199
REMARK 500 TYR A 311 CE1 TYR A 311 CZ -0.092
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 ARG A 21 NE - CZ - NH2 ANGL. DEV. = -3.9 DEGREES
REMARK 500 ARG A 82 NE - CZ - NH1 ANGL. DEV. = 5.2 DEGREES
REMARK 500 ARG A 82 NE - CZ - NH2 ANGL. DEV. = -4.6 DEGREES
REMARK 500 ARG A 90 NE - CZ - NH1 ANGL. DEV. = 4.1 DEGREES
REMARK 500 LYS A 91 CB - CA - C ANGL. DEV. = -13.2 DEGREES
REMARK 500 ARG A 92 NE - CZ - NH2 ANGL. DEV. = -3.1 DEGREES
REMARK 500 ARG A 107 NE - CZ - NH1 ANGL. DEV. = 3.8 DEGREES
REMARK 500 ASP A 153 CB - CG - OD1 ANGL. DEV. = 6.5 DEGREES
REMARK 500 ARG A 156 NE - CZ - NH2 ANGL. DEV. = -3.5 DEGREES
REMARK 500 ASP A 303 CB - CG - OD2 ANGL. DEV. = 6.6 DEGREES
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 TYR A 69 166.20 68.93
REMARK 500 THR A 127 145.34 -173.15
REMARK 500 ARG A 173 -117.30 60.22
REMARK 500
REMARK 500 REMARK: NULL
DBREF 5XZ7 A 1 322 UNP Q2FXM8 PFKA_STAA8 1 322
SEQADV 5XZ7 LEU A 323 UNP Q2FXM8 EXPRESSION TAG
SEQADV 5XZ7 GLU A 324 UNP Q2FXM8 EXPRESSION TAG
SEQADV 5XZ7 HIS A 325 UNP Q2FXM8 EXPRESSION TAG
SEQADV 5XZ7 HIS A 326 UNP Q2FXM8 EXPRESSION TAG
SEQADV 5XZ7 HIS A 327 UNP Q2FXM8 EXPRESSION TAG
SEQADV 5XZ7 HIS A 328 UNP Q2FXM8 EXPRESSION TAG
SEQADV 5XZ7 HIS A 329 UNP Q2FXM8 EXPRESSION TAG
SEQADV 5XZ7 HIS A 330 UNP Q2FXM8 EXPRESSION TAG
SEQRES 1 A 330 MET LYS LYS ILE ALA VAL LEU THR SER GLY GLY ASP SER
SEQRES 2 A 330 PRO GLY MET ASN ALA ALA VAL ARG ALA VAL VAL ARG THR
SEQRES 3 A 330 ALA ILE TYR ASN GLU ILE GLU VAL TYR GLY VAL TYR HIS
SEQRES 4 A 330 GLY TYR GLN GLY LEU LEU ASN ASP ASP ILE HIS LYS LEU
SEQRES 5 A 330 GLU LEU GLY SER VAL GLY ASP THR ILE GLN ARG GLY GLY
SEQRES 6 A 330 THR PHE LEU TYR SER ALA ARG CYS PRO GLU PHE LYS GLU
SEQRES 7 A 330 GLN GLU VAL ARG LYS VAL ALA ILE GLU ASN LEU ARG LYS
SEQRES 8 A 330 ARG GLY ILE GLU GLY LEU VAL VAL ILE GLY GLY ASP GLY
SEQRES 9 A 330 SER TYR ARG GLY ALA GLN ARG ILE SER GLU GLU CYS LYS
SEQRES 10 A 330 GLU ILE GLN THR ILE GLY ILE PRO GLY THR ILE ASP ASN
SEQRES 11 A 330 ASP ILE ASN GLY THR ASP PHE THR ILE GLY PHE ASP THR
SEQRES 12 A 330 ALA LEU ASN THR ILE ILE GLY LEU VAL ASP LYS ILE ARG
SEQRES 13 A 330 ASP THR ALA SER SER HIS ALA ARG THR PHE ILE ILE GLU
SEQRES 14 A 330 ALA MET GLY ARG ASP CYS GLY ASP LEU ALA LEU TRP ALA
SEQRES 15 A 330 GLY LEU SER VAL GLY ALA GLU THR ILE VAL VAL PRO GLU
SEQRES 16 A 330 VAL LYS THR ASP ILE LYS GLU ILE ALA ASP LYS ILE GLU
SEQRES 17 A 330 GLN GLY ILE LYS ARG GLY LYS LYS HIS SER ILE VAL LEU
SEQRES 18 A 330 VAL ALA GLU GLY CYS MET THR ALA GLN ASP CYS GLN LYS
SEQRES 19 A 330 GLU LEU SER GLN TYR ILE ASN VAL ASP ASN ARG VAL SER
SEQRES 20 A 330 VAL LEU GLY HIS VAL GLN ARG GLY GLY SER PRO THR GLY
SEQRES 21 A 330 ALA ASP ARG VAL LEU ALA SER ARG LEU GLY GLY TYR ALA
SEQRES 22 A 330 VAL ASP LEU LEU MET GLN GLY GLU THR ALA LYS GLY VAL
SEQRES 23 A 330 GLY ILE LYS ASN ASN LYS ILE VAL ALA THR SER PHE ASP
SEQRES 24 A 330 GLU ILE PHE ASP GLY LYS ASP HIS LYS PHE ASP TYR SER
SEQRES 25 A 330 LEU TYR GLU LEU ALA ASN LYS LEU SER ILE LEU GLU HIS
SEQRES 26 A 330 HIS HIS HIS HIS HIS
HET GOL A 401 6
HET GOL A 402 6
HET GOL A 403 6
HET GOL A 404 6
HET GOL A 405 6
HET GOL A 406 6
HET F6P A 407 16
HET PEG A 408 7
HETNAM GOL GLYCEROL
HETNAM F6P 6-O-PHOSPHONO-BETA-D-FRUCTOFURANOSE
HETNAM PEG DI(HYDROXYETHYL)ETHER
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
HETSYN F6P FRUCTOSE-6-PHOSPHATE; 6-O-PHOSPHONO-BETA-D-FRUCTOSE; 6-
HETSYN 2 F6P O-PHOSPHONO-D-FRUCTOSE; 6-O-PHOSPHONO-FRUCTOSE
FORMUL 2 GOL 6(C3 H8 O3)
FORMUL 8 F6P C6 H13 O9 P
FORMUL 9 PEG C4 H10 O3
FORMUL 10 HOH *283(H2 O)
HELIX 1 AA1 GLY A 15 ASN A 30 1 16
HELIX 2 AA2 GLY A 40 ASP A 47 1 8
HELIX 3 AA3 GLU A 53 GLY A 58 5 6
HELIX 4 AA4 CYS A 73 LYS A 77 5 5
HELIX 5 AA5 GLU A 78 LYS A 91 1 14
HELIX 6 AA6 GLY A 102 CYS A 116 1 15
HELIX 7 AA7 GLY A 140 ALA A 163 1 24
HELIX 8 AA8 GLY A 176 VAL A 186 1 11
HELIX 9 AA9 ASP A 199 ARG A 213 1 15
HELIX 10 AB1 THR A 228 GLN A 238 1 11
HELIX 11 AB2 GLY A 250 GLY A 255 5 6
HELIX 12 AB3 THR A 259 GLN A 279 1 21
HELIX 13 AB4 PHE A 298 ASP A 303 1 6
HELIX 14 AB5 ASP A 310 SER A 321 1 12
HELIX 15 AB6 SER A 321 HIS A 326 1 6
SHEET 1 AA1 7 ILE A 49 LEU A 52 0
SHEET 2 AA1 7 GLU A 33 VAL A 37 -1 N GLY A 36 O HIS A 50
SHEET 3 AA1 7 LYS A 3 THR A 8 1 N VAL A 6 O VAL A 37
SHEET 4 AA1 7 GLY A 96 GLY A 101 1 O VAL A 98 N ALA A 5
SHEET 5 AA1 7 GLN A 120 PRO A 125 1 O ILE A 124 N VAL A 99
SHEET 6 AA1 7 LYS A 284 LYS A 289 1 O VAL A 286 N GLY A 123
SHEET 7 AA1 7 LYS A 292 SER A 297 -1 O THR A 296 N GLY A 285
SHEET 1 AA2 4 THR A 190 VAL A 192 0
SHEET 2 AA2 4 ILE A 219 ALA A 223 1 O ALA A 223 N VAL A 192
SHEET 3 AA2 4 THR A 165 ALA A 170 1 N ILE A 168 O VAL A 222
SHEET 4 AA2 4 ASN A 244 VAL A 248 1 O SER A 247 N GLU A 169
CRYST1 73.560 80.200 121.300 90.00 90.00 90.00 I 2 2 2 8
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 0.013594 0.000000 0.000000 0.00000
SCALE2 0.000000 0.012469 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008244 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
