HEADER HYDROLASE 08-AUG-07 2QVR
TITLE E. COLI FRUCTOSE-1,6-BISPHOSPHATASE: CITRATE, FRU-2,6-P2, AND MG2+
TITLE 2 BOUND
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: FRUCTOSE-1,6-BISPHOSPHATASE;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: D-FRUCTOSE-1,6-BISPHOSPHATE 1-PHOSPHOHYDROLASE, FBPASE;
COMPND 5 EC: 3.1.3.11;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 3 ORGANISM_TAXID: 562;
SOURCE 4 STRAIN: XL1-BLUE;
SOURCE 5 GENE: FBP, FDP;
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: PET-24B
KEYWDS TETRAMER, SUGAR PHOSPHATASE FOLD, CARBOHYDRATE METABOLISM, CYTOPLASM,
KEYWDS 2 HYDROLASE, MAGNESIUM
EXPDTA X-RAY DIFFRACTION
AUTHOR J.K.HINES,H.J.FROMM,R.B.HONZATKO
REVDAT 7 15-NOV-23 2QVR 1 REMARK
REVDAT 6 30-AUG-23 2QVR 1 HETSYN
REVDAT 5 29-JUL-20 2QVR 1 COMPND REMARK HETNAM LINK
REVDAT 5 2 1 SITE
REVDAT 4 24-FEB-09 2QVR 1 VERSN
REVDAT 3 18-DEC-07 2QVR 1 JRNL
REVDAT 2 30-OCT-07 2QVR 1 JRNL
REVDAT 1 23-OCT-07 2QVR 0
JRNL AUTH J.K.HINES,X.CHEN,J.C.NIX,H.J.FROMM,R.B.HONZATKO
JRNL TITL STRUCTURES OF MAMMALIAN AND BACTERIAL
JRNL TITL 2 FRUCTOSE-1,6-BISPHOSPHATASE REVEAL THE BASIS FOR SYNERGISM
JRNL TITL 3 IN AMP/FRUCTOSE 2,6-BISPHOSPHATE INHIBITION.
JRNL REF J.BIOL.CHEM. V. 282 36121 2007
JRNL REFN ISSN 0021-9258
JRNL PMID 17933867
JRNL DOI 10.1074/JBC.M707302200
REMARK 2
REMARK 2 RESOLUTION. 2.18 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 1.1
REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-
REMARK 3 : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,
REMARK 3 : READ,RICE,SIMONSON,WARREN
REMARK 3
REMARK 3 REFINEMENT TARGET : ENGH & HUBER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.18
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 47.44
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 2972981.750
REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0000
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 99.3
REMARK 3 NUMBER OF REFLECTIONS : 16881
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 SET) : 0.196
REMARK 3 FREE R VALUE : 0.242
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 10.100
REMARK 3 FREE R VALUE TEST SET COUNT : 1699
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.006
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 6
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.18
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.32
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 95.90
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 2391
REMARK 3 BIN R VALUE (WORKING SET) : 0.2380
REMARK 3 BIN FREE R VALUE : 0.3010
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 10.10
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 269
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.018
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2593
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 34
REMARK 3 SOLVENT ATOMS : 128
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 36.30
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -2.34000
REMARK 3 B22 (A**2) : 7.41000
REMARK 3 B33 (A**2) : -5.07000
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 COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.24
REMARK 3 ESD FROM SIGMAA (A) : 0.21
REMARK 3 LOW RESOLUTION CUTOFF (A) : 5.00
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : 0.31
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.29
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.006
REMARK 3 BOND ANGLES (DEGREES) : 1.300
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 22.60
REMARK 3 IMPROPER ANGLES (DEGREES) : 1.020
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : RESTRAINED
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : 1.380 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 2.190 ; 2.000
REMARK 3 SIDE-CHAIN BOND (A**2) : 2.190 ; 2.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 2.970 ; 2.500
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : FLAT MODEL
REMARK 3 KSOL : 0.38
REMARK 3 BSOL : 46.42
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 : PROTEIN_REP.PARAM
REMARK 3 PARAMETER FILE 2 : WATER.PARAM
REMARK 3 PARAMETER FILE 3 : ION.PARAM
REMARK 3 PARAMETER FILE 4 : CITRATE.PARAM
REMARK 3 PARAMETER FILE 5 : LIG.PARAM
REMARK 3 PARAMETER FILE 6 : NULL
REMARK 3 TOPOLOGY FILE 1 : PROTEIN.TOP
REMARK 3 TOPOLOGY FILE 2 : WATER.TOP
REMARK 3 TOPOLOGY FILE 3 : ION.TOP
REMARK 3 TOPOLOGY FILE 4 : CITRATE.TOP
REMARK 3 TOPOLOGY FILE 5 : LIG.TOP
REMARK 3 TOPOLOGY FILE 6 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 2QVR COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 09-AUG-07.
REMARK 100 THE DEPOSITION ID IS D_1000044116.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 22-MAR-05
REMARK 200 TEMPERATURE (KELVIN) : 110
REMARK 200 PH : 6.3
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) : 1.54
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : RIGAKU RAXIS IV++
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : D*TREK
REMARK 200 DATA SCALING SOFTWARE : D*TREK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 16881
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.840
REMARK 200 RESOLUTION RANGE LOW (A) : 47.440
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 75.5
REMARK 200 DATA REDUNDANCY : 6.800
REMARK 200 R MERGE (I) : 0.04500
REMARK 200 R SYM (I) : 0.04500
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 16.0000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.84
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: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: AMORE
REMARK 200 STARTING MODEL: PDB ENTRY 2GQ1
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 42.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.12
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: SEE CITATION, PH 6.3, VAPOR DIFFUSION,
REMARK 280 HANGING DROP, TEMPERATURE 298.0K
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 22.00100
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 41.12550
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 87.09700
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 22.00100
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 41.12550
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 87.09700
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 22.00100
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 41.12550
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 87.09700
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 22.00100
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 41.12550
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 87.09700
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: 42070 ANGSTROM**2
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 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 350 BIOMT1 3 -1.000000 0.000000 0.000000 0.00000
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 0.00000
REMARK 350 BIOMT3 4 0.000000 0.000000 -1.000000 0.00000
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 HIS A 17 90.06 54.99
REMARK 500 ALA A 18 32.37 -160.82
REMARK 500 GLN A 191 111.25 -165.16
REMARK 500 ASP A 228 92.29 -168.26
REMARK 500 GLU A 275 -51.95 -123.00
REMARK 500 LYS A 294 -52.24 -138.41
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: MAIN CHAIN PLANARITY
REMARK 500
REMARK 500 THE FOLLOWING RESIDUES HAVE A PSEUDO PLANARITY
REMARK 500 TORSION ANGLE, C(I) - CA(I) - N(I+1) - O(I), GREATER
REMARK 500 10.0 DEGREES. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 500 I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI ANGLE
REMARK 500 ALA A 18 11.31
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 MG A 334 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 110 OD1
REMARK 620 2 ASP A 113 OD1 105.1
REMARK 620 3 GLU A 275 OE1 88.7 119.4
REMARK 620 4 FDP A 333 O1 167.0 84.3 78.7
REMARK 620 N 1 2 3
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2GQ1 RELATED DB: PDB
REMARK 900 RELATED ID: 2OWZ RELATED DB: PDB
REMARK 900 RELATED ID: 2OX3 RELATED DB: PDB
REMARK 900 RELATED ID: 2Q8M RELATED DB: PDB
REMARK 900 RELATED ID: 2QVU RELATED DB: PDB
REMARK 900 RELATED ID: 2QVV RELATED DB: PDB
DBREF 2QVR A 1 332 UNP P0A993 F16P_ECOLI 1 332
SEQRES 1 A 332 MSE LYS THR LEU GLY GLU PHE ILE VAL GLU LYS GLN HIS
SEQRES 2 A 332 GLU PHE SER HIS ALA THR GLY GLU LEU THR ALA LEU LEU
SEQRES 3 A 332 SER ALA ILE LYS LEU GLY ALA LYS ILE ILE HIS ARG ASP
SEQRES 4 A 332 ILE ASN LYS ALA GLY LEU VAL ASP ILE LEU GLY ALA SER
SEQRES 5 A 332 GLY ALA GLU ASN VAL GLN GLY GLU VAL GLN GLN LYS LEU
SEQRES 6 A 332 ASP LEU PHE ALA ASN GLU LYS LEU LYS ALA ALA LEU LYS
SEQRES 7 A 332 ALA ARG ASP ILE VAL ALA GLY ILE ALA SER GLU GLU GLU
SEQRES 8 A 332 ASP GLU ILE VAL VAL PHE GLU GLY CYS GLU HIS ALA LYS
SEQRES 9 A 332 TYR VAL VAL LEU MSE ASP PRO LEU ASP GLY SER SER ASN
SEQRES 10 A 332 ILE ASP VAL ASN VAL SER VAL GLY THR ILE PHE SER ILE
SEQRES 11 A 332 TYR ARG ARG VAL THR PRO VAL GLY THR PRO VAL THR GLU
SEQRES 12 A 332 GLU ASP PHE LEU GLN PRO GLY ASN LYS GLN VAL ALA ALA
SEQRES 13 A 332 GLY TYR VAL VAL TYR GLY SER SER THR MSE LEU VAL TYR
SEQRES 14 A 332 THR THR GLY CYS GLY VAL HIS ALA PHE THR TYR ASP PRO
SEQRES 15 A 332 SER LEU GLY VAL PHE CYS LEU CYS GLN GLU ARG MSE ARG
SEQRES 16 A 332 PHE PRO GLU LYS GLY LYS THR TYR SER ILE ASN GLU GLY
SEQRES 17 A 332 ASN TYR ILE LYS PHE PRO ASN GLY VAL LYS LYS TYR ILE
SEQRES 18 A 332 LYS PHE CYS GLN GLU GLU ASP LYS SER THR ASN ARG PRO
SEQRES 19 A 332 TYR THR SER ARG TYR ILE GLY SER LEU VAL ALA ASP PHE
SEQRES 20 A 332 HIS ARG ASN LEU LEU LYS GLY GLY ILE TYR LEU TYR PRO
SEQRES 21 A 332 SER THR ALA SER HIS PRO ASP GLY LYS LEU ARG LEU LEU
SEQRES 22 A 332 TYR GLU CYS ASN PRO MSE ALA PHE LEU ALA GLU GLN ALA
SEQRES 23 A 332 GLY GLY LYS ALA SER ASP GLY LYS GLU ARG ILE LEU ASP
SEQRES 24 A 332 ILE ILE PRO GLU THR LEU HIS GLN ARG ARG SER PHE PHE
SEQRES 25 A 332 VAL GLY ASN ASP HIS MSE VAL GLU ASP VAL GLU ARG PHE
SEQRES 26 A 332 ILE ARG GLU PHE PRO ASP ALA
MODRES 2QVR MSE A 1 MET SELENOMETHIONINE
MODRES 2QVR MSE A 109 MET SELENOMETHIONINE
MODRES 2QVR MSE A 166 MET SELENOMETHIONINE
MODRES 2QVR MSE A 194 MET SELENOMETHIONINE
MODRES 2QVR MSE A 279 MET SELENOMETHIONINE
MODRES 2QVR MSE A 318 MET SELENOMETHIONINE
HET MSE A 1 8
HET MSE A 109 8
HET MSE A 166 8
HET MSE A 194 8
HET MSE A 279 8
HET MSE A 318 8
HET FDP A 333 20
HET MG A 334 1
HET CIT A 335 13
HETNAM MSE SELENOMETHIONINE
HETNAM FDP 2,6-DI-O-PHOSPHONO-BETA-D-FRUCTOFURANOSE
HETNAM MG MAGNESIUM ION
HETNAM CIT CITRIC ACID
HETSYN FDP FRUCTOSE-2,6-DIPHOSPHATE; 2,6-DI-O-PHOSPHONO-BETA-D-
HETSYN 2 FDP FRUCTOSE; 2,6-DI-O-PHOSPHONO-D-FRUCTOSE; 2,6-DI-O-
HETSYN 3 FDP PHOSPHONO-FRUCTOSE
FORMUL 1 MSE 6(C5 H11 N O2 SE)
FORMUL 2 FDP C6 H14 O12 P2
FORMUL 3 MG MG 2+
FORMUL 4 CIT C6 H8 O7
FORMUL 5 HOH *128(H2 O)
HELIX 1 1 THR A 3 LYS A 11 1 9
HELIX 2 2 ALA A 18 ASN A 41 1 24
HELIX 3 3 LYS A 64 ARG A 80 1 17
HELIX 4 4 GLY A 114 ILE A 118 5 5
HELIX 5 5 THR A 142 PHE A 146 5 5
HELIX 6 6 PRO A 149 GLN A 153 5 5
HELIX 7 7 ASN A 206 PHE A 213 5 8
HELIX 8 8 PRO A 214 GLU A 226 1 13
HELIX 9 9 ASP A 228 ASN A 232 5 5
HELIX 10 10 SER A 242 GLY A 254 1 13
HELIX 11 11 GLU A 275 ALA A 286 1 12
HELIX 12 12 ARG A 296 ILE A 300 5 5
HELIX 13 13 ASN A 315 PHE A 329 1 15
SHEET 1 A 2 ALA A 51 GLU A 55 0
SHEET 2 A 2 VAL A 61 GLN A 63 -1 O GLN A 62 N SER A 52
SHEET 1 B 8 VAL A 95 VAL A 96 0
SHEET 2 B 8 VAL A 83 SER A 88 -1 N ILE A 86 O VAL A 95
SHEET 3 B 8 TYR A 105 ASP A 113 1 O TYR A 105 N ALA A 84
SHEET 4 B 8 VAL A 124 ARG A 132 -1 O SER A 129 N LEU A 108
SHEET 5 B 8 ALA A 155 TYR A 161 -1 O ALA A 155 N ILE A 130
SHEET 6 B 8 THR A 165 THR A 170 -1 O VAL A 168 N TYR A 158
SHEET 7 B 8 VAL A 175 TYR A 180 -1 O TYR A 180 N THR A 165
SHEET 8 B 8 PHE A 187 MSE A 194 -1 O GLN A 191 N ALA A 177
SHEET 1 C 5 THR A 236 SER A 237 0
SHEET 2 C 5 THR A 202 SER A 204 1 N TYR A 203 O THR A 236
SHEET 3 C 5 ILE A 256 TYR A 259 1 O LEU A 258 N SER A 204
SHEET 4 C 5 PHE A 311 GLY A 314 -1 O VAL A 313 N TYR A 257
SHEET 5 C 5 LYS A 289 SER A 291 -1 N LYS A 289 O GLY A 314
LINK C MSE A 1 N LYS A 2 1555 1555 1.33
LINK C LEU A 108 N MSE A 109 1555 1555 1.32
LINK C MSE A 109 N ASP A 110 1555 1555 1.32
LINK C THR A 165 N MSE A 166 1555 1555 1.33
LINK C MSE A 166 N LEU A 167 1555 1555 1.32
LINK C ARG A 193 N MSE A 194 1555 1555 1.33
LINK C MSE A 194 N ARG A 195 1555 1555 1.33
LINK C PRO A 278 N MSE A 279 1555 1555 1.33
LINK C MSE A 279 N ALA A 280 1555 1555 1.33
LINK C HIS A 317 N MSE A 318 1555 1555 1.33
LINK C MSE A 318 N VAL A 319 1555 1555 1.33
LINK OD1 ASP A 110 MG MG A 334 1555 1555 2.06
LINK OD1 ASP A 113 MG MG A 334 1555 1555 2.19
LINK OE1 GLU A 275 MG MG A 334 1555 1555 2.31
LINK O1 FDP A 333 MG MG A 334 1555 1555 2.37
CISPEP 1 ARG A 233 PRO A 234 0 0.20
CRYST1 44.002 82.251 174.194 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 0.022726 0.000000 0.000000 0.00000
SCALE2 0.000000 0.012158 0.000000 0.00000
SCALE3 0.000000 0.000000 0.005741 0.00000
HETATM 1 N MSE A 1 -15.928 12.423 2.173 1.00 38.97 N
HETATM 2 CA MSE A 1 -14.503 12.413 2.612 1.00 39.98 C
HETATM 3 C MSE A 1 -13.897 13.797 2.442 1.00 38.35 C
HETATM 4 O MSE A 1 -14.183 14.497 1.471 1.00 38.15 O
HETATM 5 CB MSE A 1 -13.707 11.390 1.796 1.00 42.11 C
HETATM 6 CG MSE A 1 -12.275 11.164 2.274 1.00 46.56 C
HETATM 7 SE MSE A 1 -10.959 12.418 1.585 1.00 51.92 SE
HETATM 8 CE MSE A 1 -10.454 11.435 -0.016 1.00 46.94 C
(ATOM LINES ARE NOT SHOWN.)
END
