HEADER TRANSFERASE(PHOSPHOTRANSFERASE) 25-JAN-88 1PFK
TITLE CRYSTAL STRUCTURE OF THE COMPLEX OF PHOSPHOFRUCTOKINASE FROM
TITLE 2 ESCHERICHIA COLI WITH ITS REACTION PRODUCTS
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PHOSPHOFRUCTOKINASE;
COMPND 3 CHAIN: A, B;
COMPND 4 EC: 2.7.1.11;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 3 ORGANISM_TAXID: 562;
SOURCE 4 CELL_LINE: 293;
SOURCE 5 EXPRESSION_SYSTEM_STRAIN: 293
KEYWDS TRANSFERASE(PHOSPHOTRANSFERASE)
EXPDTA X-RAY DIFFRACTION
AUTHOR Y.SHIRAKIHARA,P.R.EVANS
REVDAT 6 13-JUL-11 1PFK 1 VERSN
REVDAT 5 24-FEB-09 1PFK 1 VERSN
REVDAT 4 15-OCT-92 1PFK 1 SEQRES
REVDAT 3 15-JUL-90 1PFK 1 REMARK
REVDAT 2 19-APR-89 1PFK 1 JRNL
REVDAT 1 09-JAN-89 1PFK 0
JRNL AUTH Y.SHIRAKIHARA,P.R.EVANS
JRNL TITL CRYSTAL STRUCTURE OF THE COMPLEX OF PHOSPHOFRUCTOKINASE FROM
JRNL TITL 2 ESCHERICHIA COLI WITH ITS REACTION PRODUCTS.
JRNL REF J.MOL.BIOL. V. 204 973 1988
JRNL REFN ISSN 0022-2836
JRNL PMID 2975709
JRNL DOI 10.1016/0022-2836(88)90056-3
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH W.R.RYPNIEWSKI,P.R.EVANS
REMARK 1 TITL CRYSTAL STRUCTURE OF UNLIGANDED PHOSPHOFRUCTOKINASE FROM
REMARK 1 TITL 2 ESCHERICHIA COLI
REMARK 1 REF J.MOL.BIOL. V. 207 805 1989
REMARK 1 REFN ISSN 0022-2836
REMARK 1 REFERENCE 2
REMARK 1 AUTH P.R.EVANS,G.W.FARRANTS,M.C.LAWRENCE
REMARK 1 TITL CRYSTALLOGRAPHIC STRUCTURE OF ALLOSTERICALLY INHIBITED
REMARK 1 TITL 2 PHOSPHOFRUCTOKINASE AT 7 ANGSTROMS RESOLUTION
REMARK 1 REF J.MOL.BIOL. V. 191 713 1986
REMARK 1 REFN ISSN 0022-2836
REMARK 1 REFERENCE 3
REMARK 1 AUTH H.W.HELLINGA,P.R.EVANS
REMARK 1 TITL NUCLEOTIDE SEQUENCE AND HIGH-LEVEL EXPRESSION OF THE MAJOR
REMARK 1 TITL 2 ESCHERICHIA COLI PHOSPHOFRUCTOKINASE
REMARK 1 REF EUR.J.BIOCHEM. V. 149 363 1985
REMARK 1 REFN ISSN 0014-2956
REMARK 1 REFERENCE 4
REMARK 1 AUTH P.R.EVANS,G.W.FARRANTS,P.J.HUDSON
REMARK 1 TITL PHOSPHOFRUCTOKINASE. STRUCTURE AND CONTROL
REMARK 1 REF PHILOS.TRANS.R.SOC.LONDON, V. 293 53 1981
REMARK 1 REF 2 SER.B
REMARK 1 REFN ISSN 0080-4622
REMARK 1 REFERENCE 5
REMARK 1 AUTH P.R.EVANS,P.J.HUDSON
REMARK 1 TITL STRUCTURE AND CONTROL OF PHOSPHOFRUCTOKINASE FROM BACILLUS
REMARK 1 TITL 2 STEAROTHERMOPHILUS
REMARK 1 REF NATURE V. 279 500 1979
REMARK 1 REFN ISSN 0028-0836
REMARK 1 REFERENCE 6
REMARK 1 AUTH P.R.EVANS,P.J.HUDSON
REMARK 1 TITL THE THREE-DIMENSIONAL STRUCTURE OF PHOSPHOFRUCTOKINASE FROM
REMARK 1 TITL 2 BACILLUS STEAROTHERMOPHILUS
REMARK 1 REF PROC.FEBS MEET. V. 52 349 1978
REMARK 1 REFN ISSN 0071-4402
REMARK 2
REMARK 2 RESOLUTION. 2.40 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PROLSQ
REMARK 3 AUTHORS : KONNERT,HENDRICKSON
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.40
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 100.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : NULL
REMARK 3 NUMBER OF REFLECTIONS : NULL
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : NULL
REMARK 3 FREE R VALUE TEST SET SELECTION : NULL
REMARK 3 R VALUE (WORKING + TEST SET) : 0.165
REMARK 3 R VALUE (WORKING SET) : NULL
REMARK 3 FREE R VALUE : NULL
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : NULL
REMARK 3
REMARK 3 FIT/AGREEMENT OF MODEL WITH ALL DATA.
REMARK 3 R VALUE (WORKING + TEST SET, NO CUTOFF) : NULL
REMARK 3 R VALUE (WORKING SET, NO CUTOFF) : NULL
REMARK 3 FREE R VALUE (NO CUTOFF) : NULL
REMARK 3 FREE R VALUE TEST SET SIZE (%, NO CUTOFF) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT (NO CUTOFF) : NULL
REMARK 3 TOTAL NUMBER OF REFLECTIONS (NO CUTOFF) : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 4866
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 152
REMARK 3 SOLVENT ATOMS : 277
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM SIGMAA (A) : NULL
REMARK 3 LOW RESOLUTION CUTOFF (A) : NULL
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 DISTANCE RESTRAINTS. RMS SIGMA
REMARK 3 BOND LENGTH (A) : 0.008 ; NULL
REMARK 3 ANGLE DISTANCE (A) : 0.030 ; NULL
REMARK 3 INTRAPLANAR 1-4 DISTANCE (A) : NULL ; NULL
REMARK 3 H-BOND OR METAL COORDINATION (A) : NULL ; NULL
REMARK 3
REMARK 3 PLANE RESTRAINT (A) : NULL ; NULL
REMARK 3 CHIRAL-CENTER RESTRAINT (A**3) : NULL ; NULL
REMARK 3
REMARK 3 NON-BONDED CONTACT RESTRAINTS.
REMARK 3 SINGLE TORSION (A) : NULL ; NULL
REMARK 3 MULTIPLE TORSION (A) : NULL ; NULL
REMARK 3 H-BOND (X...Y) (A) : NULL ; NULL
REMARK 3 H-BOND (X-H...Y) (A) : NULL ; NULL
REMARK 3
REMARK 3 CONFORMATIONAL TORSION ANGLE RESTRAINTS.
REMARK 3 SPECIFIED (DEGREES) : NULL ; NULL
REMARK 3 PLANAR (DEGREES) : NULL ; NULL
REMARK 3 STAGGERED (DEGREES) : NULL ; NULL
REMARK 3 TRANSVERSE (DEGREES) : NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1PFK COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : NULL
REMARK 200 TEMPERATURE (KELVIN) : NULL
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : NULL
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : NULL
REMARK 200 RADIATION SOURCE : NULL
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : NULL
REMARK 200 WAVELENGTH OR RANGE (A) : NULL
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : NULL
REMARK 200 DETECTOR MANUFACTURER : NULL
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : NULL
REMARK 200 DATA SCALING SOFTWARE : NULL
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : NULL
REMARK 200 RESOLUTION RANGE HIGH (A) : NULL
REMARK 200 RESOLUTION RANGE LOW (A) : NULL
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : NULL
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: NULL
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL
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 (%): 53.56
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.65
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL
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 56.15000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 42.70000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 56.15000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 42.70000
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 300 REMARK: THE CRYSTALLOGRAPHIC ASYMMETRIC UNIT CONTAINS TWO SUBUNITS
REMARK 300 OF THE TETRAMER. THESE SUBUNITS HAVE BEEN ASSIGNED CHAIN
REMARK 300 IDENTIFIERS *A* AND *B* AND HAVE DIFFERENT CONFORMATIONS.
REMARK 300 CHAIN A IS A *CLOSED* SUBUNIT WITH THE MG++ ION BRIDGING
REMARK 300 THE TWO PRODUCTS. CHAIN B IS AN *OPEN* SUBUNIT WITH THE
REMARK 300 MG++ BOUND TO ADP ONLY. THERE ARE TWO WATER CHAINS, ONE
REMARK 300 CORRESPONDING TO EACH SUBUNIT, AND EQUIVALENT WATER
REMARK 300 MOLECULES IN EACH CHAIN HAVE BEEN ASSIGNED THE SAME RESIDUE
REMARK 300 NUMBER. THE TETRAMER CAN BE COMPLETED FROM THE DIMER IN
REMARK 300 THIS ENTRY BY ROTATING 180 DEGREES ABOUT Z
REMARK 300 (I.E. -X, -Y, Z). THE STORED ORTHOGONAL CRYSTALLOGRAPHIC
REMARK 300 COORDINATES IN THIS ENTRY MAY BE CONVERTED TO THE MOLECULAR
REMARK 300 PQR FRAME (WITH THE MOLECULAR DIADS ALONG P,Q,R) BY THE
REMARK 300 TRANSFORMATION
REMARK 300 0.87831 0.47808 0.00000 0.00000
REMARK 300 0.00000 0.00000 -1.00000 -2.71300
REMARK 300 -0.47808 0.87831 0.00000 0.00000
REMARK 300
REMARK 300 THE TRANSFORMATION SPECIFIED ON THE *MTRIX* RECORDS BELOW
REMARK 300 WILL YIELD APPROXIMATE COORDINATES FOR THE B CHAIN WHEN
REMARK 300 APPLIED TO THE A CHAIN. IT WILL ALSO YIELD APPROXIMATE
REMARK 300 COORDINATES FOR THE A CHAIN WHEN APPLIED TO THE B CHAIN.
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,PQS
REMARK 350 TOTAL BURIED SURFACE AREA: 23490 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 41100 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -194.0 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 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 0.00000
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 LYS A 214 CD CE NZ
REMARK 470 LYS A 236 CG CD CE NZ
REMARK 470 LYS B 236 CD CE NZ
REMARK 470 LYS B 304 CG CD CE NZ
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 NZ LYS A 316 O HOH A 427 2.12
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 48 NE - CZ - NH2 ANGL. DEV. = -4.3 DEGREES
REMARK 500 ASP A 59 CB - CG - OD1 ANGL. DEV. = 10.5 DEGREES
REMARK 500 ASP A 59 CB - CG - OD2 ANGL. DEV. = -7.2 DEGREES
REMARK 500 ARG A 63 CD - NE - CZ ANGL. DEV. = 12.3 DEGREES
REMARK 500 ARG A 63 NE - CZ - NH1 ANGL. DEV. = 6.5 DEGREES
REMARK 500 ARG A 63 NE - CZ - NH2 ANGL. DEV. = -3.6 DEGREES
REMARK 500 ARG A 72 CD - NE - CZ ANGL. DEV. = 12.1 DEGREES
REMARK 500 ARG A 72 NE - CZ - NH1 ANGL. DEV. = 3.3 DEGREES
REMARK 500 ARG A 77 NE - CZ - NH1 ANGL. DEV. = 4.4 DEGREES
REMARK 500 ARG A 77 NE - CZ - NH2 ANGL. DEV. = -3.5 DEGREES
REMARK 500 ASP A 78 CB - CG - OD1 ANGL. DEV. = 5.7 DEGREES
REMARK 500 ARG A 82 NE - CZ - NH1 ANGL. DEV. = 3.7 DEGREES
REMARK 500 ARG A 82 NE - CZ - NH2 ANGL. DEV. = -3.7 DEGREES
REMARK 500 ARG A 92 NE - CZ - NH2 ANGL. DEV. = -4.2 DEGREES
REMARK 500 ASP A 127 CB - CG - OD1 ANGL. DEV. = 5.8 DEGREES
REMARK 500 ARG A 152 NE - CZ - NH1 ANGL. DEV. = 5.8 DEGREES
REMARK 500 ARG A 154 NE - CZ - NH2 ANGL. DEV. = -3.3 DEGREES
REMARK 500 ARG A 198 NE - CZ - NH1 ANGL. DEV. = 5.0 DEGREES
REMARK 500 ARG A 198 NE - CZ - NH2 ANGL. DEV. = -5.8 DEGREES
REMARK 500 GLU A 241 CA - CB - CG ANGL. DEV. = 13.4 DEGREES
REMARK 500 ARG A 243 NE - CZ - NH1 ANGL. DEV. = 3.4 DEGREES
REMARK 500 ARG A 243 NE - CZ - NH2 ANGL. DEV. = -3.1 DEGREES
REMARK 500 ARG A 252 NE - CZ - NH1 ANGL. DEV. = 3.3 DEGREES
REMARK 500 ARG A 261 NE - CZ - NH1 ANGL. DEV. = 3.2 DEGREES
REMARK 500 ARG A 282 NE - CZ - NH1 ANGL. DEV. = 5.6 DEGREES
REMARK 500 ASP B 12 CB - CG - OD1 ANGL. DEV. = 5.8 DEGREES
REMARK 500 ASP B 53 CB - CG - OD1 ANGL. DEV. = 5.5 DEGREES
REMARK 500 ARG B 54 NE - CZ - NH1 ANGL. DEV. = 4.7 DEGREES
REMARK 500 ARG B 54 NE - CZ - NH2 ANGL. DEV. = -5.0 DEGREES
REMARK 500 ARG B 63 NE - CZ - NH2 ANGL. DEV. = -3.0 DEGREES
REMARK 500 ARG B 72 NE - CZ - NH2 ANGL. DEV. = -3.3 DEGREES
REMARK 500 ARG B 77 NE - CZ - NH2 ANGL. DEV. = -3.8 DEGREES
REMARK 500 ARG B 162 NE - CZ - NH1 ANGL. DEV. = 4.0 DEGREES
REMARK 500 ARG B 162 NE - CZ - NH2 ANGL. DEV. = -3.2 DEGREES
REMARK 500 ARG B 171 NE - CZ - NH1 ANGL. DEV. = 3.5 DEGREES
REMARK 500 ARG B 243 NE - CZ - NH1 ANGL. DEV. = 4.6 DEGREES
REMARK 500 ASP B 260 CB - CG - OD2 ANGL. DEV. = -5.6 DEGREES
REMARK 500 TRP B 311 CA - CB - CG ANGL. DEV. = 12.1 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 ILE A 1 98.33 74.16
REMARK 500 THR A 125 140.42 -170.08
REMARK 500 ARG A 171 -95.60 75.73
REMARK 500 CYS A 225 -172.30 -176.98
REMARK 500 LYS A 308 47.61 -92.64
REMARK 500 ILE B 1 108.89 77.75
REMARK 500 PHE B 76 -19.96 -46.97
REMARK 500 THR B 125 138.20 175.14
REMARK 500 ARG B 171 -92.84 59.72
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 B 407 DISTANCE = 5.24 ANGSTROMS
REMARK 525 HOH B 414 DISTANCE = 5.17 ANGSTROMS
REMARK 600
REMARK 600 HETEROGEN
REMARK 600 ADP A 324 AND ADP B 324 ARE THE PRODUCTS OF THE CATALYTIC
REMARK 600 REACTION ATP + F6P --> ADP + F-1,6-DP. ADP A 326 AND
REMARK 600 ADP B 326 ARE THE ALLOSTERIC ACTIVATORS.
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 MG A 325 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 FBP A 323 O2P
REMARK 620 2 HOH A 417 O 72.3
REMARK 620 3 ASP A 103 OD2 146.2 102.4
REMARK 620 4 ADP A 324 O2B 91.3 159.9 84.8
REMARK 620 5 HOH A 386 O 111.0 95.3 102.6 101.5
REMARK 620 6 HOH A 402 O 73.5 78.9 72.8 85.4 171.4
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG A 327 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLY A 185 O
REMARK 620 2 ADP A 326 O2B 90.6
REMARK 620 3 ADP A 326 O1A 173.5 86.5
REMARK 620 4 HOH A 368 O 86.9 81.7 98.4
REMARK 620 5 GLU A 187 OE1 103.4 159.7 81.0 84.4
REMARK 620 6 HOH A 369 O 80.7 97.0 94.0 167.5 99.8
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG B 325 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ADP B 324 O2B
REMARK 620 2 HOH B 419 O 106.9
REMARK 620 3 ADP B 324 O1A 81.4 91.5
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG B 327 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU B 187 OE1
REMARK 620 2 GLU B 187 OE2 44.6
REMARK 620 3 ADP B 326 O2B 177.4 132.9
REMARK 620 4 ADP B 326 O1A 88.6 102.5 92.1
REMARK 620 5 HOH B 369 O 99.8 55.7 77.7 101.2
REMARK 620 6 HOH B 370 O 80.0 121.0 102.4 92.8 166.0
REMARK 620 7 GLY B 185 O 88.9 82.6 90.8 169.8 88.9 77.1
REMARK 620 N 1 2 3 4 5 6
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FBP A 323
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FBP B 323
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 325
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 327
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG B 325
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG B 327
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ADP A 324
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ADP A 326
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ADP B 324
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ADP B 326
DBREF 1PFK A 0 319 UNP P0A796 K6PF1_ECOLI 1 320
DBREF 1PFK B 0 319 UNP P0A796 K6PF1_ECOLI 1 320
SEQRES 1 A 320 MET ILE LYS LYS ILE GLY VAL LEU THR SER GLY GLY ASP
SEQRES 2 A 320 ALA PRO GLY MET ASN ALA ALA ILE ARG GLY VAL VAL ARG
SEQRES 3 A 320 SER ALA LEU THR GLU GLY LEU GLU VAL MET GLY ILE TYR
SEQRES 4 A 320 ASP GLY TYR LEU GLY LEU TYR GLU ASP ARG MET VAL GLN
SEQRES 5 A 320 LEU ASP ARG TYR SER VAL SER ASP MET ILE ASN ARG GLY
SEQRES 6 A 320 GLY THR PHE LEU GLY SER ALA ARG PHE PRO GLU PHE ARG
SEQRES 7 A 320 ASP GLU ASN ILE ARG ALA VAL ALA ILE GLU ASN LEU LYS
SEQRES 8 A 320 LYS ARG GLY ILE ASP ALA LEU VAL VAL ILE GLY GLY ASP
SEQRES 9 A 320 GLY SER TYR MET GLY ALA MET ARG LEU THR GLU MET GLY
SEQRES 10 A 320 PHE PRO CYS ILE GLY LEU PRO GLY THR ILE ASP ASN ASP
SEQRES 11 A 320 ILE LYS GLY THR ASP TYR THR ILE GLY PHE PHE THR ALA
SEQRES 12 A 320 LEU SER THR VAL VAL GLU ALA ILE ASP ARG LEU ARG ASP
SEQRES 13 A 320 THR SER SER SER HIS GLN ARG ILE SER VAL VAL GLU VAL
SEQRES 14 A 320 MET GLY ARG TYR CYS GLY ASP LEU THR LEU ALA ALA ALA
SEQRES 15 A 320 ILE ALA GLY GLY CYS GLU PHE VAL VAL VAL PRO GLU VAL
SEQRES 16 A 320 GLU PHE SER ARG GLU ASP LEU VAL ASN GLU ILE LYS ALA
SEQRES 17 A 320 GLY ILE ALA LYS GLY LYS LYS HIS ALA ILE VAL ALA ILE
SEQRES 18 A 320 THR GLU HIS MET CYS ASP VAL ASP GLU LEU ALA HIS PHE
SEQRES 19 A 320 ILE GLU LYS GLU THR GLY ARG GLU THR ARG ALA THR VAL
SEQRES 20 A 320 LEU GLY HIS ILE GLN ARG GLY GLY SER PRO VAL PRO TYR
SEQRES 21 A 320 ASP ARG ILE LEU ALA SER ARG MET GLY ALA TYR ALA ILE
SEQRES 22 A 320 ASP LEU LEU LEU ALA GLY TYR GLY GLY ARG CYS VAL GLY
SEQRES 23 A 320 ILE GLN ASN GLU GLN LEU VAL HIS HIS ASP ILE ILE ASP
SEQRES 24 A 320 ALA ILE GLU ASN MET LYS ARG PRO PHE LYS GLY ASP TRP
SEQRES 25 A 320 LEU ASP CYS ALA LYS LYS LEU TYR
SEQRES 1 B 320 MET ILE LYS LYS ILE GLY VAL LEU THR SER GLY GLY ASP
SEQRES 2 B 320 ALA PRO GLY MET ASN ALA ALA ILE ARG GLY VAL VAL ARG
SEQRES 3 B 320 SER ALA LEU THR GLU GLY LEU GLU VAL MET GLY ILE TYR
SEQRES 4 B 320 ASP GLY TYR LEU GLY LEU TYR GLU ASP ARG MET VAL GLN
SEQRES 5 B 320 LEU ASP ARG TYR SER VAL SER ASP MET ILE ASN ARG GLY
SEQRES 6 B 320 GLY THR PHE LEU GLY SER ALA ARG PHE PRO GLU PHE ARG
SEQRES 7 B 320 ASP GLU ASN ILE ARG ALA VAL ALA ILE GLU ASN LEU LYS
SEQRES 8 B 320 LYS ARG GLY ILE ASP ALA LEU VAL VAL ILE GLY GLY ASP
SEQRES 9 B 320 GLY SER TYR MET GLY ALA MET ARG LEU THR GLU MET GLY
SEQRES 10 B 320 PHE PRO CYS ILE GLY LEU PRO GLY THR ILE ASP ASN ASP
SEQRES 11 B 320 ILE LYS GLY THR ASP TYR THR ILE GLY PHE PHE THR ALA
SEQRES 12 B 320 LEU SER THR VAL VAL GLU ALA ILE ASP ARG LEU ARG ASP
SEQRES 13 B 320 THR SER SER SER HIS GLN ARG ILE SER VAL VAL GLU VAL
SEQRES 14 B 320 MET GLY ARG TYR CYS GLY ASP LEU THR LEU ALA ALA ALA
SEQRES 15 B 320 ILE ALA GLY GLY CYS GLU PHE VAL VAL VAL PRO GLU VAL
SEQRES 16 B 320 GLU PHE SER ARG GLU ASP LEU VAL ASN GLU ILE LYS ALA
SEQRES 17 B 320 GLY ILE ALA LYS GLY LYS LYS HIS ALA ILE VAL ALA ILE
SEQRES 18 B 320 THR GLU HIS MET CYS ASP VAL ASP GLU LEU ALA HIS PHE
SEQRES 19 B 320 ILE GLU LYS GLU THR GLY ARG GLU THR ARG ALA THR VAL
SEQRES 20 B 320 LEU GLY HIS ILE GLN ARG GLY GLY SER PRO VAL PRO TYR
SEQRES 21 B 320 ASP ARG ILE LEU ALA SER ARG MET GLY ALA TYR ALA ILE
SEQRES 22 B 320 ASP LEU LEU LEU ALA GLY TYR GLY GLY ARG CYS VAL GLY
SEQRES 23 B 320 ILE GLN ASN GLU GLN LEU VAL HIS HIS ASP ILE ILE ASP
SEQRES 24 B 320 ALA ILE GLU ASN MET LYS ARG PRO PHE LYS GLY ASP TRP
SEQRES 25 B 320 LEU ASP CYS ALA LYS LYS LEU TYR
HET FBP A 323 20
HET FBP B 323 20
HET MG A 325 1
HET MG A 327 1
HET MG B 325 1
HET MG B 327 1
HET ADP A 324 27
HET ADP A 326 27
HET ADP B 324 27
HET ADP B 326 27
HETNAM FBP BETA-FRUCTOSE-1,6-DIPHOSPHATE
HETNAM MG MAGNESIUM ION
HETNAM ADP ADENOSINE-5'-DIPHOSPHATE
HETSYN FBP FRUCTOSE-1,6-BISPHOSPHATE
FORMUL 3 FBP 2(C6 H14 O12 P2)
FORMUL 5 MG 4(MG 2+)
FORMUL 9 ADP 4(C10 H15 N5 O10 P2)
FORMUL 13 HOH *277(H2 O)
HELIX 1 1A GLY A 15 GLU A 30 13/10 END 16
HELIX 2 2A GLY A 40 ASP A 47 13/10 BEGINNING AND END 8
HELIX 3 4AA PHE A 73 ASP A 78 5 6
HELIX 4 4A ASP A 78 GLY A 93 13/10 END 16
HELIX 5 5A GLY A 102 GLY A 116 1 15
HELIX 6 6A GLY A 138 HIS A 160 1 23
HELIX 7 7A THR A 177 GLY A 185 1 9
HELIX 8 8A SER A 197 GLY A 212 13/10 BEGINNING AND END 16
HELIX 9 9A ASP A 226 GLY A 239 1 14
HELIX 10 10A GLY A 248 ARG A 252 5 5
HELIX 11 11A VAL A 257 GLY A 278 13/10 END 22
HELIX 12 12A ASP A 295 ASN A 302 1 8
HELIX 13 13A LYS A 308 TYR A 319 1 12
HELIX 14 1B GLY B 15 GLU B 30 13/10 END 16
HELIX 15 2B GLY B 40 ASP B 47 13/10 BEGINNING AND END 8
HELIX 16 4AB PHE B 73 ASP B 78 5 6
HELIX 17 4B ASP B 78 GLY B 93 13/10 END 16
HELIX 18 5B GLY B 102 GLY B 116 1 15
HELIX 19 6B GLY B 138 HIS B 160 1 23
HELIX 20 7B THR B 177 GLY B 185 1 9
HELIX 21 8B SER B 197 GLY B 212 13/10 BEGINNING AND END 16
HELIX 22 9B ASP B 226 GLY B 239 1 14
HELIX 23 10B GLY B 248 ARG B 252 5 5
HELIX 24 11B VAL B 257 GLY B 278 13/10 END 22
HELIX 25 12B ASP B 295 ASN B 302 1 8
HELIX 26 13B LYS B 308 TYR B 319 1 12
SHEET 1 S1A 7 ARG A 48 LEU A 52 0
SHEET 2 S1A 7 GLU A 33 TYR A 38 -1 O GLY A 36 N VAL A 50
SHEET 3 S1A 7 LYS A 2 SER A 9 1 O VAL A 6 N ILE A 37
SHEET 4 S1A 7 ALA A 96 GLY A 101 1 O VAL A 98 N LEU A 7
SHEET 5 S1A 7 PRO A 118 LEU A 122 1 O ILE A 120 N VAL A 99
SHEET 6 S1A 7 GLY A 281 GLN A 287 1 O ARG A 282 N GLY A 121
SHEET 7 S1A 7 GLN A 290 ASP A 295 -1 O HIS A 294 N CYS A 283
SHEET 1 S2A 4 PHE A 188 VAL A 190 0
SHEET 2 S2A 4 ALA A 216 THR A 221 1 O ALA A 219 N VAL A 190
SHEET 3 S2A 4 ARG A 162 VAL A 168 1 O VAL A 166 N ILE A 220
SHEET 4 S2A 4 GLU A 241 LEU A 247 1 O THR A 245 N GLU A 167
SHEET 1 S1B 7 ARG B 48 LEU B 52 0
SHEET 2 S1B 7 GLU B 33 TYR B 38 -1 O GLY B 36 N VAL B 50
SHEET 3 S1B 7 LYS B 2 SER B 9 1 O VAL B 6 N ILE B 37
SHEET 4 S1B 7 ALA B 96 GLY B 101 1 O VAL B 98 N LEU B 7
SHEET 5 S1B 7 PRO B 118 LEU B 122 1 O ILE B 120 N VAL B 99
SHEET 6 S1B 7 GLY B 281 GLN B 287 1 O ARG B 282 N GLY B 121
SHEET 7 S1B 7 GLN B 290 ASP B 295 -1 O HIS B 294 N CYS B 283
SHEET 1 S2B 4 PHE B 188 VAL B 190 0
SHEET 2 S2B 4 ALA B 216 THR B 221 1 O ALA B 219 N VAL B 190
SHEET 3 S2B 4 ARG B 162 VAL B 168 1 O VAL B 166 N ILE B 220
SHEET 4 S2B 4 GLU B 241 LEU B 247 1 O THR B 245 N GLU B 167
LINK O2P FBP A 323 MG MG A 325 1555 1555 2.04
LINK MG MG A 325 O HOH A 417 1555 1555 2.38
LINK MG MG A 325 OD2 ASP A 103 1555 1555 1.95
LINK MG MG A 325 O2B ADP A 324 1555 1555 2.19
LINK MG MG A 325 O HOH A 386 1555 1555 2.25
LINK MG MG A 325 O HOH A 402 1555 1555 2.43
LINK MG MG A 327 O GLY A 185 1555 1555 2.25
LINK MG MG A 327 O2B ADP A 326 1555 1555 2.17
LINK MG MG A 327 O1A ADP A 326 1555 1555 2.42
LINK MG MG A 327 O HOH A 368 1555 1555 1.96
LINK MG MG A 327 OE1 GLU A 187 1555 1555 2.14
LINK MG MG A 327 O HOH A 369 1555 1555 1.91
LINK MG MG B 325 O2B ADP B 324 1555 1555 2.72
LINK MG MG B 325 O HOH B 419 1555 1555 2.37
LINK MG MG B 325 O1A ADP B 324 1555 1555 2.26
LINK MG MG B 327 OE1 GLU B 187 1555 1555 2.21
LINK MG MG B 327 OE2 GLU B 187 1555 1555 3.08
LINK MG MG B 327 O2B ADP B 326 1555 1555 2.23
LINK MG MG B 327 O1A ADP B 326 1555 1555 2.15
LINK MG MG B 327 O HOH B 369 1555 1555 2.17
LINK MG MG B 327 O HOH B 370 1555 1555 2.05
LINK MG MG B 327 O GLY B 185 1555 1555 2.30
SITE 1 AC1 20 GLY A 11 ARG A 72 THR A 125 ASP A 127
SITE 2 AC1 20 MET A 169 GLY A 170 ARG A 171 GLU A 222
SITE 3 AC1 20 HIS A 249 ARG A 252 ADP A 324 MG A 325
SITE 4 AC1 20 HOH A 330 HOH A 351 HOH A 402 HOH A 417
SITE 5 AC1 20 HOH A 430 HOH A 447 ARG B 162 ARG B 243
SITE 1 AC2 18 ARG A 162 ARG A 243 GLY B 11 THR B 125
SITE 2 AC2 18 ASP B 127 MET B 169 GLY B 170 ARG B 171
SITE 3 AC2 18 GLU B 222 HIS B 249 ARG B 252 ADP B 324
SITE 4 AC2 18 HOH B 331 HOH B 352 HOH B 387 HOH B 403
SITE 5 AC2 18 HOH B 447 HOH B 448
SITE 1 AC3 6 ASP A 103 FBP A 323 ADP A 324 HOH A 386
SITE 2 AC3 6 HOH A 402 HOH A 417
SITE 1 AC4 5 GLY A 185 GLU A 187 ADP A 326 HOH A 368
SITE 2 AC4 5 HOH A 369
SITE 1 AC5 3 ASP B 103 ADP B 324 HOH B 419
SITE 1 AC6 5 GLY B 185 GLU B 187 ADP B 326 HOH B 369
SITE 2 AC6 5 HOH B 370
SITE 1 AC7 19 GLY A 10 GLY A 11 TYR A 41 ARG A 72
SITE 2 AC7 19 PHE A 73 PHE A 76 ARG A 77 GLY A 102
SITE 3 AC7 19 ASP A 103 GLY A 104 SER A 105 MET A 107
SITE 4 AC7 19 GLY A 108 FBP A 323 MG A 325 HOH A 351
SITE 5 AC7 19 HOH A 365 HOH A 386 HOH A 465
SITE 1 AC8 19 ARG A 154 SER A 158 GLY A 185 GLU A 187
SITE 2 AC8 19 GLY A 212 LYS A 213 LYS A 214 HIS A 215
SITE 3 AC8 19 MG A 327 HOH A 368 HOH A 369 HOH A 467
SITE 4 AC8 19 ARG B 21 ARG B 25 ARG B 54 TYR B 55
SITE 5 AC8 19 SER B 58 ASP B 59 HOH B 420
SITE 1 AC9 16 SER B 9 TYR B 41 ARG B 72 PHE B 73
SITE 2 AC9 16 PRO B 74 PHE B 76 ARG B 77 GLY B 102
SITE 3 AC9 16 ASP B 103 GLY B 104 SER B 105 MET B 107
SITE 4 AC9 16 GLY B 108 FBP B 323 MG B 325 HOH B 366
SITE 1 BC1 19 ARG A 21 ARG A 25 ARG A 54 TYR A 55
SITE 2 BC1 19 SER A 58 ASP A 59 HOH A 419 ARG B 154
SITE 3 BC1 19 SER B 158 GLY B 185 GLU B 187 GLY B 212
SITE 4 BC1 19 LYS B 213 LYS B 214 HIS B 215 MG B 327
SITE 5 BC1 19 HOH B 328 HOH B 369 HOH B 370
CRYST1 112.300 85.400 77.100 90.00 90.00 90.00 P 21 21 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 0.008905 0.000000 0.000000 0.00000
SCALE2 0.000000 0.011710 0.000000 0.00000
SCALE3 0.000000 0.000000 0.012970 0.00000
MTRIX1 1 0.542870 0.839820 0.000000 0.00000 1
MTRIX2 1 0.839820 -0.542870 0.000000 0.00000 1
MTRIX3 1 0.000000 0.000000 -1.000000 -5.42690 1
(ATOM LINES ARE NOT SHOWN.)
END
