HEADER HYDROLASE 16-SEP-12 4H45
TITLE PRODUCT COMPLEXES OF PORCINE LIVER FRUCTOSE-1,6-BISPHOSPHATASE WITH
TITLE 2 MUTATION E192Q
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: FRUCTOSE-1,6-BISPHOSPHATASE 1;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: FBPASE 1, D-FRUCTOSE-1,6-BISPHOSPHATE 1-PHOSPHOHYDROLASE 1;
COMPND 5 EC: 3.1.3.11;
COMPND 6 ENGINEERED: YES;
COMPND 7 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: SUS SCROFA;
SOURCE 3 ORGANISM_COMMON: PIG;
SOURCE 4 ORGANISM_TAXID: 9823;
SOURCE 5 GENE: FBP, FBP1;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: DF657;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET24B
KEYWDS ALLOSTERIC ENZYMES, COOPERATIVITY, OLIGOMERIZATION, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR Y.GAO,R.B.HONZATKO
REVDAT 3 20-SEP-23 4H45 1 HETSYN
REVDAT 2 29-JUL-20 4H45 1 COMPND REMARK SEQADV HETNAM
REVDAT 2 2 1 LINK SITE
REVDAT 1 18-SEP-13 4H45 0
JRNL AUTH Y.GAO,R.B.HONZATKO
JRNL TITL DIMER-DIMER INTERFACE IN PORCINE LIVER
JRNL TITL 2 FRUCTOSE-1,6-BISPHOSPHATASE IS ESSENTIAL IN COOPERATIVE
JRNL TITL 3 BINDING OF AMP
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 3.10 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC
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) : 3.10
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 32.42
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 96.9
REMARK 3 NUMBER OF REFLECTIONS : 6601
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) : 0.229
REMARK 3 R VALUE (WORKING SET) : 0.227
REMARK 3 FREE R VALUE : 0.283
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.800
REMARK 3 FREE R VALUE TEST SET COUNT : 330
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) : 3.10
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 3.18
REMARK 3 REFLECTION IN BIN (WORKING SET) : 482
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.21
REMARK 3 BIN R VALUE (WORKING SET) : 0.2850
REMARK 3 BIN FREE R VALUE SET COUNT : 23
REMARK 3 BIN FREE R VALUE : 0.4320
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2488
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 28
REMARK 3 SOLVENT ATOMS : 35
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 46.52
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.31000
REMARK 3 B22 (A**2) : -0.19000
REMARK 3 B33 (A**2) : -0.11000
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): NULL
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.560
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 : 0.911
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.864
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 2554 ; 0.022 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 3460 ; 1.855 ; 1.996
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 325 ; 7.361 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 98 ;37.574 ;24.490
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 452 ;21.333 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 13 ;17.119 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 401 ; 0.122 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 1860 ; 0.010 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
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): 1617 ; 5.125 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 2612 ; 7.743 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 937 ; 1.454 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 848 ; 2.591 ; 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 : 1.40
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 4H45 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 19-SEP-12.
REMARK 100 THE DEPOSITION ID IS D_1000074995.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 11-JAN-11
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : ROTATING ANODE
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : RIGAKU
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : GRAPHITE
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : RIGAKU RAXIS
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : D*TREK 9.7L
REMARK 200 DATA SCALING SOFTWARE : D*TREK 9.7L
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 7665
REMARK 200 RESOLUTION RANGE HIGH (A) : 3.000
REMARK 200 RESOLUTION RANGE LOW (A) : 32.420
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 97.3
REMARK 200 DATA REDUNDANCY : 3.490
REMARK 200 R MERGE (I) : 0.12900
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 6.9000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.00
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.11
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.9
REMARK 200 DATA REDUNDANCY IN SHELL : 3.53
REMARK 200 R MERGE FOR SHELL (I) : 0.42600
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.300
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 1CNQ
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 51.90
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.56
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG3350, T-BUTYL ALCOHOL, 1,2
REMARK 280 -ETHANEDIOL, PH 7.5, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE
REMARK 280 298K
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 26.99800
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 41.81050
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 83.11000
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 26.99800
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 41.81050
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 83.11000
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 26.99800
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 41.81050
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 83.11000
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 26.99800
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 41.81050
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 83.11000
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: TETRAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 15970 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 44480 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -444.0 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 53.99600
REMARK 350 BIOMT2 2 0.000000 -1.000000 0.000000 83.62100
REMARK 350 BIOMT3 2 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT1 3 -1.000000 0.000000 0.000000 53.99600
REMARK 350 BIOMT2 3 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 3 0.000000 0.000000 -1.000000 0.00000
REMARK 350 BIOMT1 4 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 4 0.000000 -1.000000 0.000000 83.62100
REMARK 350 BIOMT3 4 0.000000 0.000000 -1.000000 0.00000
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 A 528 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A 534 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 THR A 1
REMARK 465 ASP A 2
REMARK 465 GLN A 3
REMARK 465 ALA A 4
REMARK 465 ALA A 5
REMARK 465 PHE A 6
REMARK 465 ASP A 7
REMARK 465 THR A 8
REMARK 465 ASN A 9
REMARK 465 ALA A 336
REMARK 465 LYS A 337
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 THR A 66 43.95 -89.85
REMARK 500 PHE A 117 146.82 -171.37
REMARK 500 GLU A 280 -60.27 -126.97
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 ASN A 64 VAL A 65 -149.99
REMARK 500
REMARK 500 REMARK: NULL
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 ZN A 402 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 118 OD2
REMARK 620 2 LEU A 120 O 98.1
REMARK 620 3 PO4 A 404 O2 99.4 85.8
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A 403 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 118 OD1
REMARK 620 2 GLU A 280 OE1 81.6
REMARK 620 3 PO4 A 404 O2 87.9 144.6
REMARK 620 N 1 2
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4GX3 RELATED DB: PDB
REMARK 900 RELATED ID: 4GX4 RELATED DB: PDB
REMARK 900 RELATED ID: 4GX6 RELATED DB: PDB
DBREF 4H45 A 1 337 UNP P00636 F16P1_PIG 2 338
SEQADV 4H45 GLN A 192 UNP P00636 GLU 193 ENGINEERED MUTATION
SEQRES 1 A 337 THR ASP GLN ALA ALA PHE ASP THR ASN ILE VAL THR LEU
SEQRES 2 A 337 THR ARG PHE VAL MET GLU GLU GLY ARG LYS ALA ARG GLY
SEQRES 3 A 337 THR GLY GLU MET THR GLN LEU LEU ASN SER LEU CYS THR
SEQRES 4 A 337 ALA VAL LYS ALA ILE SER THR ALA VAL ARG LYS ALA GLY
SEQRES 5 A 337 ILE ALA HIS LEU TYR GLY ILE ALA GLY SER THR ASN VAL
SEQRES 6 A 337 THR GLY ASP GLN VAL LYS LYS LEU ASP VAL LEU SER ASN
SEQRES 7 A 337 ASP LEU VAL ILE ASN VAL LEU LYS SER SER PHE ALA THR
SEQRES 8 A 337 CYS VAL LEU VAL SER GLU GLU ASP LYS ASN ALA ILE ILE
SEQRES 9 A 337 VAL GLU PRO GLU LYS ARG GLY LYS TYR VAL VAL CYS PHE
SEQRES 10 A 337 ASP PRO LEU ASP GLY SER SER ASN ILE ASP CYS LEU VAL
SEQRES 11 A 337 SER ILE GLY THR ILE PHE GLY ILE TYR ARG LYS ASN SER
SEQRES 12 A 337 THR ASP GLU PRO SER GLU LYS ASP ALA LEU GLN PRO GLY
SEQRES 13 A 337 ARG ASN LEU VAL ALA ALA GLY TYR ALA LEU TYR GLY SER
SEQRES 14 A 337 ALA THR MET LEU VAL LEU ALA MET VAL ASN GLY VAL ASN
SEQRES 15 A 337 CYS PHE MET LEU ASP PRO ALA ILE GLY GLN PHE ILE LEU
SEQRES 16 A 337 VAL ASP ARG ASP VAL LYS ILE LYS LYS LYS GLY SER ILE
SEQRES 17 A 337 TYR SER ILE ASN GLU GLY TYR ALA LYS GLU PHE ASP PRO
SEQRES 18 A 337 ALA ILE THR GLU TYR ILE GLN ARG LYS LYS PHE PRO PRO
SEQRES 19 A 337 ASP ASN SER ALA PRO TYR GLY ALA ARG TYR VAL GLY SER
SEQRES 20 A 337 MET VAL ALA ASP VAL HIS ARG THR LEU VAL TYR GLY GLY
SEQRES 21 A 337 ILE PHE MET TYR PRO ALA ASN LYS LYS SER PRO LYS GLY
SEQRES 22 A 337 LYS LEU ARG LEU LEU TYR GLU CYS ASN PRO MET ALA TYR
SEQRES 23 A 337 VAL MET GLU LYS ALA GLY GLY LEU ALA THR THR GLY LYS
SEQRES 24 A 337 GLU ALA VAL LEU ASP ILE VAL PRO THR ASP ILE HIS GLN
SEQRES 25 A 337 ARG ALA PRO ILE ILE LEU GLY SER PRO GLU ASP VAL THR
SEQRES 26 A 337 GLU LEU LEU GLU ILE TYR GLN LYS HIS ALA ALA LYS
HET F6P A 401 16
HET ZN A 402 1
HET ZN A 403 1
HET PO4 A 404 5
HET PO4 A 405 5
HETNAM F6P 6-O-PHOSPHONO-BETA-D-FRUCTOFURANOSE
HETNAM ZN ZINC ION
HETNAM PO4 PHOSPHATE ION
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 F6P C6 H13 O9 P
FORMUL 3 ZN 2(ZN 2+)
FORMUL 5 PO4 2(O4 P 3-)
FORMUL 7 HOH *35(H2 O)
HELIX 1 1 THR A 12 ALA A 24 1 13
HELIX 2 2 GLY A 28 LYS A 50 1 23
HELIX 3 3 LYS A 71 SER A 88 1 18
HELIX 4 4 GLU A 106 ARG A 110 5 5
HELIX 5 5 GLY A 122 LEU A 129 5 8
HELIX 6 6 SER A 148 LEU A 153 5 6
HELIX 7 7 PRO A 155 ARG A 157 5 3
HELIX 8 8 ASN A 212 PHE A 219 5 8
HELIX 9 9 ASP A 220 PHE A 232 1 13
HELIX 10 10 SER A 247 GLY A 259 1 13
HELIX 11 11 GLU A 280 ALA A 291 1 12
HELIX 12 12 SER A 320 HIS A 334 1 15
SHEET 1 A 8 ILE A 103 ILE A 104 0
SHEET 2 A 8 THR A 91 SER A 96 -1 N LEU A 94 O ILE A 103
SHEET 3 A 8 TYR A 113 ASP A 121 1 O PHE A 117 N VAL A 95
SHEET 4 A 8 ILE A 132 ARG A 140 -1 O GLY A 133 N ASP A 121
SHEET 5 A 8 LEU A 159 TYR A 167 -1 O VAL A 160 N ILE A 138
SHEET 6 A 8 THR A 171 MET A 177 -1 O VAL A 174 N TYR A 164
SHEET 7 A 8 GLY A 180 ASP A 187 -1 O PHE A 184 N LEU A 173
SHEET 8 A 8 GLN A 192 ARG A 198 -1 O ILE A 194 N MET A 185
SHEET 1 B 5 GLY A 241 ALA A 242 0
SHEET 2 B 5 ILE A 208 SER A 210 1 N TYR A 209 O GLY A 241
SHEET 3 B 5 ILE A 261 TYR A 264 1 O MET A 263 N SER A 210
SHEET 4 B 5 ILE A 316 GLY A 319 -1 O ILE A 316 N TYR A 264
SHEET 5 B 5 LEU A 294 THR A 296 -1 N THR A 296 O ILE A 317
SHEET 1 C 2 LEU A 275 ARG A 276 0
SHEET 2 C 2 ARG A 313 ALA A 314 -1 O ALA A 314 N LEU A 275
LINK OD2 ASP A 118 ZN ZN A 402 1555 1555 2.10
LINK OD1 ASP A 118 ZN ZN A 403 1555 1555 2.23
LINK O LEU A 120 ZN ZN A 402 1555 1555 2.15
LINK OE1 GLU A 280 ZN ZN A 403 1555 1555 2.37
LINK ZN ZN A 402 O2 PO4 A 404 1555 1555 2.60
LINK ZN ZN A 403 O2 PO4 A 404 1555 1555 1.98
CISPEP 1 ARG A 198 ASP A 199 0 -26.06
CRYST1 53.996 83.621 166.220 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 0.018520 0.000000 0.000000 0.00000
SCALE2 0.000000 0.011959 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006016 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
