HEADER HYDROLASE 24-AUG-96 1FSA
TITLE THE T-STATE STRUCTURE OF LYS 42 TO ALA MUTANT OF THE PIG KIDNEY
TITLE 2 FRUCTOSE 1,6-BISPHOSPHATASE EXPRESSED IN E. COLI
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: FRUCTOSE 1,6-BISPHOSPHATASE;
COMPND 3 CHAIN: A, B;
COMPND 4 EC: 3.1.3.11;
COMPND 5 ENGINEERED: YES;
COMPND 6 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: SUS SCROFA;
SOURCE 3 ORGANISM_COMMON: PIG;
SOURCE 4 ORGANISM_TAXID: 9823;
SOURCE 5 ORGAN: KIDNEY;
SOURCE 6 GENE: FBP;
SOURCE 7 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 9 EXPRESSION_SYSTEM_STRAIN: EK1601;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PEK292;
SOURCE 11 EXPRESSION_SYSTEM_GENE: FBP
KEYWDS LYASE, FRUCTOSE 1, 6-BISPHOSPHATASE, HYDROLASE, CARBOHYDRATE
KEYWDS 2 METABOLISM, GLUCONEOGENESIS, ACETYLATION PHOSPHORYLATION
EXPDTA X-RAY DIFFRACTION
AUTHOR G.LU,B.STEC,E.GIROUX,E.R.KANTROWITZ
REVDAT 7 07-FEB-24 1FSA 1 REMARK
REVDAT 6 03-NOV-21 1FSA 1 SEQADV HETSYN
REVDAT 5 29-JUL-20 1FSA 1 COMPND REMARK SEQADV HETNAM
REVDAT 5 2 1 LINK SITE
REVDAT 4 16-NOV-11 1FSA 1 HETATM
REVDAT 3 13-JUL-11 1FSA 1 VERSN
REVDAT 2 24-FEB-09 1FSA 1 VERSN
REVDAT 1 04-SEP-97 1FSA 0
JRNL AUTH G.LU,B.STEC,E.L.GIROUX,E.R.KANTROWITZ
JRNL TITL EVIDENCE FOR AN ACTIVE T-STATE PIG KIDNEY FRUCTOSE
JRNL TITL 2 1,6-BISPHOSPHATASE: INTERFACE RESIDUE LYS-42 IS IMPORTANT
JRNL TITL 3 FOR ALLOSTERIC INHIBITION AND AMP COOPERATIVITY.
JRNL REF PROTEIN SCI. V. 5 2333 1996
JRNL REFN ISSN 0961-8368
JRNL PMID 8931152
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH B.STEC,R.ABRAHAM,E.GIROUX,E.R.KANTROWITZ
REMARK 1 TITL CRYSTAL STRUCTURES OF THE ACTIVE SITE MUTANT (ARG-243-->ALA)
REMARK 1 TITL 2 IN THE T AND R ALLOSTERIC STATES OF PIG KIDNEY
REMARK 1 TITL 3 FRUCTOSE-1,6-BISPHOSPHATASE EXPRESSED IN ESCHERICHIA COLI
REMARK 1 REF PROTEIN SCI. V. 5 1541 1996
REMARK 1 REFN ISSN 0961-8368
REMARK 1 REFERENCE 2
REMARK 1 AUTH Y.XUE,S.HUANG,J.Y.LIANG,Y.ZHANG,W.N.LIPSCOMB
REMARK 1 TITL CRYSTAL STRUCTURE OF FRUCTOSE-1,6-BISPHOSPHATASE COMPLEXED
REMARK 1 TITL 2 WITH FRUCTOSE 2,6-BISPHOSPHATE, AMP, AND ZN2+ AT 2.0-A
REMARK 1 TITL 3 RESOLUTION: ASPECTS OF SYNERGISM BETWEEN INHIBITORS
REMARK 1 REF PROC.NATL.ACAD.SCI.USA V. 91 12482 1994
REMARK 1 REFN ISSN 0027-8424
REMARK 1 REFERENCE 3
REMARK 1 AUTH H.KE,Y.ZHANG,J.Y.LIANG,W.N.LIPSCOMB
REMARK 1 TITL CRYSTAL STRUCTURE OF THE NEUTRAL FORM OF
REMARK 1 TITL 2 FRUCTOSE-1,6-BISPHOSPHATASE COMPLEXED WITH THE PRODUCT
REMARK 1 TITL 3 FRUCTOSE 6-PHOSPHATE AT 2.1-A RESOLUTION
REMARK 1 REF PROC.NATL.ACAD.SCI.USA V. 88 2989 1991
REMARK 1 REFN ISSN 0027-8424
REMARK 2
REMARK 2 RESOLUTION. 2.30 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR 3.1
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.30
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 10.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 2.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 65.0
REMARK 3 NUMBER OF REFLECTIONS : 19578
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 SET) : 0.184
REMARK 3 FREE R VALUE : 0.232
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 10.000
REMARK 3 FREE R VALUE TEST SET COUNT : NULL
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : NULL
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : NULL
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : NULL
REMARK 3 BIN RESOLUTION RANGE LOW (A) : NULL
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : NULL
REMARK 3 BIN FREE R VALUE : NULL
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 BIN FREE R VALUE TEST SET COUNT : NULL
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 5136
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 80
REMARK 3 SOLVENT ATOMS : 131
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 30.90
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 24.31
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) : 0.24
REMARK 3 ESD FROM SIGMAA (A) : NULL
REMARK 3 LOW RESOLUTION CUTOFF (A) : 10.0
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM C-V SIGMAA (A) : NULL
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.012
REMARK 3 BOND ANGLES (DEGREES) : 1.870
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 24.87
REMARK 3 IMPROPER ANGLES (DEGREES) : 1.540
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : 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 NCS MODEL : NULL
REMARK 3
REMARK 3 NCS RESTRAINTS. RMS SIGMA/WEIGHT
REMARK 3 GROUP 1 POSITIONAL (A) : NULL ; NULL
REMARK 3 GROUP 1 B-FACTOR (A**2) : NULL ; NULL
REMARK 3
REMARK 3 PARAMETER FILE 1 : NULL
REMARK 3 TOPOLOGY FILE 1 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS:
REMARK 3 REGIONS WITH WEAK ELECTRON DENSITY AND HIGH TEMPERATURE
REMARK 3 FACTORS WHICH ARE MOST LIKELY DISORDERED: 1 - 8 AND 64 - 69
REMARK 3 IN A AND B SUBUNITS.
REMARK 4
REMARK 4 1FSA COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.
REMARK 100 THE DEPOSITION ID IS D_1000173399.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : FEB-96
REMARK 200 TEMPERATURE (KELVIN) : 295
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 RUH2R
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : GRAPHITE(002)
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : AREA DETECTOR
REMARK 200 DETECTOR MANUFACTURER : XUONG-HAMLIN MULTIWIRE
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : SDMS
REMARK 200 DATA SCALING SOFTWARE : NULL
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 27660
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.200
REMARK 200 RESOLUTION RANGE LOW (A) : 80.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.500
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 81.0
REMARK 200 DATA REDUNDANCY : 2.300
REMARK 200 R MERGE (I) : 0.09000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 3.5000
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: X-PLOR 3.1
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 55.69
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.78
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PH 7.5
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 30.52500
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 83.36000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 30.52500
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 83.36000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TETRAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA,PQS
REMARK 350 TOTAL BURIED SURFACE AREA: 21800 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 49010 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -146.0 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 61.05000
REMARK 350 BIOMT2 2 0.000000 -1.000000 0.000000 166.72000
REMARK 350 BIOMT3 2 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 380 LIES ON A SPECIAL POSITION.
REMARK 375 HOH B 377 LIES ON A SPECIAL POSITION.
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 ALA B 4 O ALA B 4 2765 1.96
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 PRO B 265 C - N - CA ANGL. DEV. = 9.2 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 ASP A 2 -50.67 -150.37
REMARK 500 GLN A 3 112.54 -170.13
REMARK 500 ALA A 4 99.35 -173.79
REMARK 500 ALA A 5 -157.58 -66.20
REMARK 500 PHE A 6 93.17 -61.37
REMARK 500 THR A 8 128.52 -179.39
REMARK 500 ARG A 25 64.63 14.46
REMARK 500 SER A 62 87.16 -61.54
REMARK 500 ASN A 64 37.69 -148.99
REMARK 500 VAL A 65 151.11 79.47
REMARK 500 THR A 66 -154.19 -139.07
REMARK 500 ASP A 68 36.47 -95.60
REMARK 500 GLN A 69 98.55 70.59
REMARK 500 LYS A 71 -116.53 -103.70
REMARK 500 SER A 87 8.53 -64.52
REMARK 500 ALA A 90 9.93 -153.40
REMARK 500 GLU A 106 150.26 -47.48
REMARK 500 ARG A 110 108.26 -54.09
REMARK 500 LYS A 112 -19.63 -141.55
REMARK 500 LEU A 120 90.16 -160.96
REMARK 500 SER A 123 -30.80 -37.96
REMARK 500 SER A 131 135.48 -29.73
REMARK 500 SER A 143 -167.63 177.76
REMARK 500 ASP A 145 -174.57 -65.05
REMARK 500 VAL A 178 -55.25 -5.66
REMARK 500 GLU A 213 -4.69 -56.69
REMARK 500 ASN A 236 37.72 39.83
REMARK 500 GLU A 280 -51.38 -133.56
REMARK 500 HIS A 334 43.40 -107.01
REMARK 500 ALA A 335 136.83 -38.19
REMARK 500 ASP B 2 -97.09 -70.99
REMARK 500 ALA B 4 -139.10 -170.81
REMARK 500 ALA B 5 -104.48 -132.79
REMARK 500 THR B 31 -39.15 -36.94
REMARK 500 TYR B 57 51.12 -106.72
REMARK 500 THR B 63 -89.66 -28.98
REMARK 500 ASP B 68 -90.23 -179.41
REMARK 500 GLN B 69 57.75 -113.38
REMARK 500 VAL B 70 -111.56 -129.84
REMARK 500 LYS B 112 41.23 -87.16
REMARK 500 ASN B 125 37.49 -79.72
REMARK 500 LEU B 129 17.13 54.03
REMARK 500 THR B 144 -23.56 -144.97
REMARK 500 PRO B 147 96.23 -47.00
REMARK 500 LEU B 153 68.30 -58.63
REMARK 500 ALA B 161 144.44 -172.49
REMARK 500 TYR B 167 51.07 -106.47
REMARK 500 VAL B 178 -59.98 -20.22
REMARK 500 SER B 207 36.64 -149.96
REMARK 500 ASP B 235 6.58 -65.40
REMARK 500
REMARK 500 THIS ENTRY HAS 58 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: PLANAR GROUPS
REMARK 500
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS
REMARK 500 AN RMSD GREATER THAN THIS VALUE
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI RMS TYPE
REMARK 500 TYR B 139 0.06 SIDE CHAIN
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 MN A 339 MN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 118 OD2
REMARK 620 2 ASP A 121 OD2 92.4
REMARK 620 3 GLU A 280 OE2 83.4 109.2
REMARK 620 4 F6P A 338 O1 170.3 79.8 93.8
REMARK 620 5 HOH A 342 O 114.3 119.2 126.5 74.8
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MN B 339 MN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP B 118 OD2
REMARK 620 2 ASP B 121 OD1 79.5
REMARK 620 3 GLU B 280 OE2 108.0 111.6
REMARK 620 4 HOH B 342 O 106.3 94.3 140.0
REMARK 620 N 1 2 3
DBREF 1FSA A 1 337 UNP P00636 F16P_PIG 1 337
DBREF 1FSA B 1 337 UNP P00636 F16P_PIG 1 337
SEQADV 1FSA GLN A 20 UNP P00636 GLU 20 CONFLICT
SEQADV 1FSA ALA A 42 UNP P00636 LYS 42 ENGINEERED MUTATION
SEQADV 1FSA THR A 96 UNP P00636 SER 96 CONFLICT
SEQADV 1FSA ASN A 199 UNP P00636 ASP 199 CONFLICT
SEQADV 1FSA GLN B 20 UNP P00636 GLU 20 CONFLICT
SEQADV 1FSA ALA B 42 UNP P00636 LYS 42 ENGINEERED MUTATION
SEQADV 1FSA THR B 96 UNP P00636 SER 96 CONFLICT
SEQADV 1FSA ASN B 199 UNP P00636 ASP 199 CONFLICT
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 GLN 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 ALA 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 THR 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 GLU PHE ILE LEU
SEQRES 16 A 337 VAL ASP ARG ASN 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
SEQRES 1 B 337 THR ASP GLN ALA ALA PHE ASP THR ASN ILE VAL THR LEU
SEQRES 2 B 337 THR ARG PHE VAL MET GLU GLN GLY ARG LYS ALA ARG GLY
SEQRES 3 B 337 THR GLY GLU MET THR GLN LEU LEU ASN SER LEU CYS THR
SEQRES 4 B 337 ALA VAL ALA ALA ILE SER THR ALA VAL ARG LYS ALA GLY
SEQRES 5 B 337 ILE ALA HIS LEU TYR GLY ILE ALA GLY SER THR ASN VAL
SEQRES 6 B 337 THR GLY ASP GLN VAL LYS LYS LEU ASP VAL LEU SER ASN
SEQRES 7 B 337 ASP LEU VAL ILE ASN VAL LEU LYS SER SER PHE ALA THR
SEQRES 8 B 337 CYS VAL LEU VAL THR GLU GLU ASP LYS ASN ALA ILE ILE
SEQRES 9 B 337 VAL GLU PRO GLU LYS ARG GLY LYS TYR VAL VAL CYS PHE
SEQRES 10 B 337 ASP PRO LEU ASP GLY SER SER ASN ILE ASP CYS LEU VAL
SEQRES 11 B 337 SER ILE GLY THR ILE PHE GLY ILE TYR ARG LYS ASN SER
SEQRES 12 B 337 THR ASP GLU PRO SER GLU LYS ASP ALA LEU GLN PRO GLY
SEQRES 13 B 337 ARG ASN LEU VAL ALA ALA GLY TYR ALA LEU TYR GLY SER
SEQRES 14 B 337 ALA THR MET LEU VAL LEU ALA MET VAL ASN GLY VAL ASN
SEQRES 15 B 337 CYS PHE MET LEU ASP PRO ALA ILE GLY GLU PHE ILE LEU
SEQRES 16 B 337 VAL ASP ARG ASN VAL LYS ILE LYS LYS LYS GLY SER ILE
SEQRES 17 B 337 TYR SER ILE ASN GLU GLY TYR ALA LYS GLU PHE ASP PRO
SEQRES 18 B 337 ALA ILE THR GLU TYR ILE GLN ARG LYS LYS PHE PRO PRO
SEQRES 19 B 337 ASP ASN SER ALA PRO TYR GLY ALA ARG TYR VAL GLY SER
SEQRES 20 B 337 MET VAL ALA ASP VAL HIS ARG THR LEU VAL TYR GLY GLY
SEQRES 21 B 337 ILE PHE MET TYR PRO ALA ASN LYS LYS SER PRO LYS GLY
SEQRES 22 B 337 LYS LEU ARG LEU LEU TYR GLU CYS ASN PRO MET ALA TYR
SEQRES 23 B 337 VAL MET GLU LYS ALA GLY GLY LEU ALA THR THR GLY LYS
SEQRES 24 B 337 GLU ALA VAL LEU ASP ILE VAL PRO THR ASP ILE HIS GLN
SEQRES 25 B 337 ARG ALA PRO ILE ILE LEU GLY SER PRO GLU ASP VAL THR
SEQRES 26 B 337 GLU LEU LEU GLU ILE TYR GLN LYS HIS ALA ALA LYS
HET F6P A 338 16
HET MN A 339 1
HET AMP A 340 23
HET F6P B 338 16
HET MN B 339 1
HET AMP B 340 23
HETNAM F6P 6-O-PHOSPHONO-BETA-D-FRUCTOFURANOSE
HETNAM MN MANGANESE (II) ION
HETNAM AMP ADENOSINE MONOPHOSPHATE
HETSYN F6P FRUCTOSE-6-PHOSPHATE; 6-O-PHOSPHONO-BETA-D-FRUCTOSE; 6-
HETSYN 2 F6P O-PHOSPHONO-D-FRUCTOSE; 6-O-PHOSPHONO-FRUCTOSE
FORMUL 3 F6P 2(C6 H13 O9 P)
FORMUL 4 MN 2(MN 2+)
FORMUL 5 AMP 2(C10 H14 N5 O7 P)
FORMUL 9 HOH *131(H2 O)
HELIX 1 1 LEU A 13 LYS A 23 1 11
HELIX 2 2 THR A 31 VAL A 48 1 18
HELIX 3 3 ILE A 53 TYR A 57 1 5
HELIX 4 4 LEU A 73 SER A 88 1 16
HELIX 5 5 ASN A 125 CYS A 128 5 4
HELIX 6 6 GLU A 149 ASP A 151 5 3
HELIX 7 7 GLY A 156 ASN A 158 5 3
HELIX 8 8 GLU A 213 GLU A 218 5 6
HELIX 9 9 PRO A 221 LYS A 231 1 11
HELIX 10 10 MET A 248 TYR A 258 1 11
HELIX 11 11 CYS A 281 ALA A 291 1 11
HELIX 12 12 VAL A 302 ASP A 304 5 3
HELIX 13 13 PRO A 321 LYS A 333 1 13
HELIX 14 14 LEU B 13 ALA B 24 1 12
HELIX 15 15 GLU B 29 VAL B 48 1 20
HELIX 16 16 ILE B 53 LEU B 56 1 4
HELIX 17 17 LEU B 73 SER B 88 1 16
HELIX 18 18 PRO B 107 LYS B 109 5 3
HELIX 19 19 SER B 123 ILE B 126 5 4
HELIX 20 20 GLU B 149 ALA B 152 5 4
HELIX 21 21 GLY B 156 ASN B 158 5 3
HELIX 22 22 GLU B 213 GLU B 218 5 6
HELIX 23 23 PRO B 221 LYS B 231 1 11
HELIX 24 24 MET B 248 TYR B 258 1 11
HELIX 25 25 CYS B 281 LYS B 290 1 10
HELIX 26 26 VAL B 302 ASP B 304 5 3
HELIX 27 27 PRO B 321 HIS B 334 1 14
SHEET 1 A 8 ALA A 102 ILE A 104 0
SHEET 2 A 8 VAL A 93 THR A 96 -1 N LEU A 94 O ILE A 103
SHEET 3 A 8 TYR A 113 ASP A 118 1 N VAL A 115 O VAL A 93
SHEET 4 A 8 ILE A 132 ARG A 140 -1 N TYR A 139 O VAL A 114
SHEET 5 A 8 LEU A 159 TYR A 167 -1 N TYR A 167 O ILE A 132
SHEET 6 A 8 THR A 171 MET A 177 -1 N ALA A 176 O ALA A 162
SHEET 7 A 8 GLY A 180 ASP A 187 -1 N PHE A 184 O LEU A 173
SHEET 8 A 8 GLU A 192 ASP A 197 -1 N ASP A 197 O CYS A 183
SHEET 1 B 3 ILE A 261 TYR A 264 0
SHEET 2 B 3 ILE A 316 GLY A 319 -1 N LEU A 318 O PHE A 262
SHEET 3 B 3 LEU A 294 THR A 296 -1 N THR A 296 O ILE A 317
SHEET 1 C 7 GLU B 192 ASP B 197 0
SHEET 2 C 7 GLY B 180 ASP B 187 -1 N ASP B 187 O GLU B 192
SHEET 3 C 7 THR B 171 MET B 177 -1 N MET B 177 O GLY B 180
SHEET 4 C 7 ALA B 161 TYR B 167 -1 N LEU B 166 O MET B 172
SHEET 5 C 7 ILE B 132 ARG B 140 -1 N ILE B 138 O ALA B 161
SHEET 6 C 7 TYR B 113 ASP B 118 -1 N ASP B 118 O ILE B 135
SHEET 7 C 7 THR B 91 THR B 96 1 N CYS B 92 O TYR B 113
SHEET 1 D 2 ILE B 208 SER B 210 0
SHEET 2 D 2 GLY B 241 ARG B 243 1 N GLY B 241 O TYR B 209
SHEET 1 E 3 ILE B 261 TYR B 264 0
SHEET 2 E 3 ILE B 316 GLY B 319 -1 N LEU B 318 O PHE B 262
SHEET 3 E 3 LEU B 294 THR B 296 -1 N THR B 296 O ILE B 317
LINK OD2 ASP A 118 MN MN A 339 1555 1555 2.08
LINK OD2 ASP A 121 MN MN A 339 1555 1555 2.15
LINK OE2 GLU A 280 MN MN A 339 1555 1555 2.05
LINK O1 F6P A 338 MN MN A 339 1555 1555 1.95
LINK MN MN A 339 O HOH A 342 1555 1555 2.24
LINK OD2 ASP B 118 MN MN B 339 1555 1555 2.40
LINK OD1 ASP B 121 MN MN B 339 1555 1555 2.43
LINK OE2 GLU B 280 MN MN B 339 1555 1555 2.09
LINK MN MN B 339 O HOH B 342 1555 1555 1.90
CRYST1 61.050 166.720 79.980 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 0.016380 0.000000 0.000000 0.00000
SCALE2 0.000000 0.005998 0.000000 0.00000
SCALE3 0.000000 0.000000 0.012503 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
