HEADER TRANSFERASE 05-SEP-07 2R66
TITLE COMPLEX STRUCTURE OF SUCROSE PHOSPHATE SYNTHASE (SPS)-F6P OF
TITLE 2 HALOTHERMOTHRIX ORENII
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: GLYCOSYL TRANSFERASE, GROUP 1;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: SUCROSE PHOSPHATE SYNTHASE;
COMPND 5 EC: 2.4.1.14;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HALOTHERMOTHRIX ORENII;
SOURCE 3 ORGANISM_TAXID: 373903;
SOURCE 4 STRAIN: H 168;
SOURCE 5 GENE: SPS;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PTRCHISA
KEYWDS ROSSMANN-FOLD, TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR J.SIVARAMAN,T.K.CHUA
REVDAT 5 25-OCT-23 2R66 1 HETSYN
REVDAT 4 29-JUL-20 2R66 1 COMPND REMARK HETNAM SITE
REVDAT 3 25-OCT-17 2R66 1 REMARK
REVDAT 2 24-FEB-09 2R66 1 VERSN
REVDAT 1 10-JUN-08 2R66 0
JRNL AUTH T.K.CHUA,J.M.BUJNICKI,T.-C.TAN,F.HUYNH,B.K.PATEL,J.SIVARAMAN
JRNL TITL THE STRUCTURE OF SUCROSE PHOSPHATE SYNTHASE FROM
JRNL TITL 2 HALOTHERMOTHRIX ORENII REVEALS ITS MECHANISM OF ACTION AND
JRNL TITL 3 BINDING MODE
JRNL REF PLANT CELL V. 20 1059 2008
JRNL REFN ISSN 1040-4651
JRNL PMID 18424616
JRNL DOI 10.1105/TPC.107.051193
REMARK 2
REMARK 2 RESOLUTION. 2.80 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS
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 : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.80
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 20.00
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) (%) : 82.8
REMARK 3 NUMBER OF REFLECTIONS : 12600
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) : 0.210
REMARK 3 FREE R VALUE : 0.267
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 8.400
REMARK 3 FREE R VALUE TEST SET COUNT : 1282
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 : 3611
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 16
REMARK 3 SOLVENT ATOMS : 118
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 46.81
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 12.22600
REMARK 3 B22 (A**2) : -1.76400
REMARK 3 B33 (A**2) : -10.46200
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : -8.53900
REMARK 3 B23 (A**2) : 0.00000
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 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) : 0.005
REMARK 3 BOND ANGLES (DEGREES) : 1.062
REMARK 3 DIHEDRAL ANGLES (DEGREES) : NULL
REMARK 3 IMPROPER ANGLES (DEGREES) : NULL
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 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : NULL
REMARK 3 KSOL : NULL
REMARK 3 BSOL : 52.90
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_REP.PARAM
REMARK 3 PARAMETER FILE 3 : F6P.PARAM
REMARK 3 PARAMETER FILE 4 : NULL
REMARK 3 TOPOLOGY FILE 1 : NULL
REMARK 3 TOPOLOGY FILE 2 : NULL
REMARK 3 TOPOLOGY FILE 3 : NULL
REMARK 3 TOPOLOGY FILE 4 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 2R66 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 19-SEP-07.
REMARK 100 THE DEPOSITION ID IS D_1000044473.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 13-JUN-06
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.5
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 : 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 : DENZO, HKL-2000
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK, HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 13734
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.800
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 200 DATA REDUNDANCY : 3.700
REMARK 200 R MERGE (I) : 0.07500
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 14.6000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.80
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.90
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 3.60
REMARK 200 R MERGE FOR SHELL (I) : 0.28200
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: CNS
REMARK 200 STARTING MODEL: PDB ENTRY 2R60
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 49.23
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.42
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 20% PEG 4000, 0.6M NACL, 0.1M NA MES,
REMARK 280 PH 6.5, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 298K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1
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 77.11250
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 24.24950
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 77.11250
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 24.24950
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: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
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 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 MET A 1
REMARK 465 VAL A 2
REMARK 465 GLU A 3
REMARK 465 MET A 4
REMARK 465 THR A 5
REMARK 465 ARG A 6
REMARK 465 LYS A 463
REMARK 465 ASP A 464
REMARK 465 GLU A 465
REMARK 465 GLU A 466
REMARK 465 ASP A 467
REMARK 465 GLU A 468
REMARK 465 GLY A 469
REMARK 465 GLY A 470
REMARK 465 SER A 471
REMARK 465 LEU A 472
REMARK 465 ASN A 473
REMARK 465 ILE A 474
REMARK 465 PRO A 475
REMARK 465 ASP A 476
REMARK 465 TYR A 477
REMARK 465 PHE A 478
REMARK 465 THR A 479
REMARK 465 ASN A 480
REMARK 465 PRO A 481
REMARK 465 GLY A 482
REMARK 465 ALA A 483
REMARK 465 SER A 484
REMARK 465 ASN A 485
REMARK 465 ASP A 486
REMARK 465 GLU A 487
REMARK 465 LYS A 488
REMARK 465 LEU A 489
REMARK 465 LEU A 490
REMARK 465 ASP A 491
REMARK 465 THR A 492
REMARK 465 PHE A 493
REMARK 465 ASN A 494
REMARK 465 LYS A 495
REMARK 465 LEU A 496
REMARK 465 TRP A 497
REMARK 465 LYS A 498
REMARK 465 GLU A 499
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 THR A 27 OG1 CG2
REMARK 470 LEU A 161 CB CG CD1 CD2
REMARK 470 ASN A 162 CB CG OD1 ND2
REMARK 470 VAL A 163 CB CG1 CG2
REMARK 470 ASN A 164 CG OD1 ND2
REMARK 470 ASN A 167 CG OD1 ND2
REMARK 470 PHE A 168 CB CG CD1 CD2 CE1 CE2 CZ
REMARK 470 LYS A 169 CB CG CD CE NZ
REMARK 470 GLU A 170 CG CD OE1 OE2
REMARK 470 GLU A 173 CB CG CD OE1 OE2
REMARK 470 ARG A 174 CG CD NE CZ NH1 NH2
REMARK 470 ARG A 462 CG CD NE CZ NH1 NH2
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 GLN A 432 CG GLN A 432 CD -0.188
REMARK 500 GLN A 432 CD GLN A 432 OE1 -0.196
REMARK 500 GLN A 432 CD GLN A 432 NE2 -0.200
REMARK 500 GLN A 432 C GLN A 432 O -0.116
REMARK 500 GLU A 433 N GLU A 433 CA -0.128
REMARK 500 GLU A 433 CA GLU A 433 CB -0.138
REMARK 500 GLU A 433 CB GLU A 433 CG -0.265
REMARK 500 GLU A 433 CG GLU A 433 CD -0.154
REMARK 500 GLU A 433 CD GLU A 433 OE1 -0.090
REMARK 500 GLU A 433 C GLU A 433 O -0.136
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 ASN A 18 176.94 179.03
REMARK 500 ASP A 23 55.71 33.53
REMARK 500 PHE A 32 79.20 -118.84
REMARK 500 THR A 57 -161.52 -114.13
REMARK 500 PHE A 88 140.87 -179.27
REMARK 500 PHE A 93 152.04 -46.31
REMARK 500 TYR A 128 162.23 79.11
REMARK 500 HIS A 151 -34.54 69.65
REMARK 500 SER A 152 108.44 -177.23
REMARK 500 GLU A 159 -77.49 -52.73
REMARK 500 LEU A 161 41.78 88.96
REMARK 500 ASN A 162 150.78 -43.62
REMARK 500 VAL A 163 69.47 -100.07
REMARK 500 THR A 165 -25.28 61.66
REMARK 500 PHE A 175 -3.09 -143.75
REMARK 500 LYS A 193 125.98 -170.56
REMARK 500 LEU A 210 -7.51 -54.72
REMARK 500 LEU A 300 -164.33 -116.90
REMARK 500 TYR A 310 42.80 -146.91
REMARK 500 PRO A 370 17.83 -57.59
REMARK 500 PHE A 371 108.04 78.90
REMARK 500 ARG A 442 -14.77 -143.51
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2R68 RELATED DB: PDB
REMARK 900 THE SAME PROTEIN IN COMPLEX WITH S6P
REMARK 900 RELATED ID: 2R60 RELATED DB: PDB
REMARK 900 STRUCTURE OF APO SUCROSE PHOSPHATE SYNTHASE (SPS) OF
REMARK 900 HALOTHERMOTHRIX ORENII
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 THE FIRST THREE RESIDUES, MET 1, VAL 2, AND GLU 3 ARE PART
REMARK 999 OF THE GENE PRODUCT.
DBREF 2R66 A 4 499 UNP Q2ADF5 Q2ADF5_9FIRM 1 496
SEQADV 2R66 MET A 1 UNP Q2ADF5 SEE REMARK 999
SEQADV 2R66 VAL A 2 UNP Q2ADF5 SEE REMARK 999
SEQADV 2R66 GLU A 3 UNP Q2ADF5 SEE REMARK 999
SEQRES 1 A 499 MET VAL GLU MET THR ARG ILE LYS HIS VAL ALA PHE LEU
SEQRES 2 A 499 ASN PRO GLN GLY ASN PHE ASP PRO ALA ASP SER TYR TRP
SEQRES 3 A 499 THR GLU HIS PRO ASP PHE GLY GLY GLN LEU VAL TYR VAL
SEQRES 4 A 499 LYS GLU VAL SER LEU ALA LEU ALA GLU MET GLY VAL GLN
SEQRES 5 A 499 VAL ASP ILE ILE THR ARG ARG ILE LYS ASP GLU ASN TRP
SEQRES 6 A 499 PRO GLU PHE SER GLY GLU ILE ASP TYR TYR GLN GLU THR
SEQRES 7 A 499 ASN LYS VAL ARG ILE VAL ARG ILE PRO PHE GLY GLY ASP
SEQRES 8 A 499 LYS PHE LEU PRO LYS GLU GLU LEU TRP PRO TYR LEU HIS
SEQRES 9 A 499 GLU TYR VAL ASN LYS ILE ILE ASN PHE TYR ARG GLU GLU
SEQRES 10 A 499 GLY LYS PHE PRO GLN VAL VAL THR THR HIS TYR GLY ASP
SEQRES 11 A 499 GLY GLY LEU ALA GLY VAL LEU LEU LYS ASN ILE LYS GLY
SEQRES 12 A 499 LEU PRO PHE THR PHE THR GLY HIS SER LEU GLY ALA GLN
SEQRES 13 A 499 LYS MET GLU LYS LEU ASN VAL ASN THR SER ASN PHE LYS
SEQRES 14 A 499 GLU MET ASP GLU ARG PHE LYS PHE HIS ARG ARG ILE ILE
SEQRES 15 A 499 ALA GLU ARG LEU THR MET SER TYR ALA ASP LYS ILE ILE
SEQRES 16 A 499 VAL SER THR SER GLN GLU ARG PHE GLY GLN TYR SER HIS
SEQRES 17 A 499 ASP LEU TYR ARG GLY ALA VAL ASN VAL GLU ASP ASP ASP
SEQRES 18 A 499 LYS PHE SER VAL ILE PRO PRO GLY VAL ASN THR ARG VAL
SEQRES 19 A 499 PHE ASP GLY GLU TYR GLY ASP LYS ILE LYS ALA LYS ILE
SEQRES 20 A 499 THR LYS TYR LEU GLU ARG ASP LEU GLY SER GLU ARG MET
SEQRES 21 A 499 GLU LEU PRO ALA ILE ILE ALA SER SER ARG LEU ASP GLN
SEQRES 22 A 499 LYS LYS ASN HIS TYR GLY LEU VAL GLU ALA TYR VAL GLN
SEQRES 23 A 499 ASN LYS GLU LEU GLN ASP LYS ALA ASN LEU VAL LEU THR
SEQRES 24 A 499 LEU ARG GLY ILE GLU ASN PRO PHE GLU ASP TYR SER ARG
SEQRES 25 A 499 ALA GLY GLN GLU GLU LYS GLU ILE LEU GLY LYS ILE ILE
SEQRES 26 A 499 GLU LEU ILE ASP ASN ASN ASP CYS ARG GLY LYS VAL SER
SEQRES 27 A 499 MET PHE PRO LEU ASN SER GLN GLN GLU LEU ALA GLY CYS
SEQRES 28 A 499 TYR ALA TYR LEU ALA SER LYS GLY SER VAL PHE ALA LEU
SEQRES 29 A 499 THR SER PHE TYR GLU PRO PHE GLY LEU ALA PRO VAL GLU
SEQRES 30 A 499 ALA MET ALA SER GLY LEU PRO ALA VAL VAL THR ARG ASN
SEQRES 31 A 499 GLY GLY PRO ALA GLU ILE LEU ASP GLY GLY LYS TYR GLY
SEQRES 32 A 499 VAL LEU VAL ASP PRO GLU ASP PRO GLU ASP ILE ALA ARG
SEQRES 33 A 499 GLY LEU LEU LYS ALA PHE GLU SER GLU GLU THR TRP SER
SEQRES 34 A 499 ALA TYR GLN GLU LYS GLY LYS GLN ARG VAL GLU GLU ARG
SEQRES 35 A 499 TYR THR TRP GLN GLU THR ALA ARG GLY TYR LEU GLU VAL
SEQRES 36 A 499 ILE GLN GLU ILE ALA ASP ARG LYS ASP GLU GLU ASP GLU
SEQRES 37 A 499 GLY GLY SER LEU ASN ILE PRO ASP TYR PHE THR ASN PRO
SEQRES 38 A 499 GLY ALA SER ASN ASP GLU LYS LEU LEU ASP THR PHE ASN
SEQRES 39 A 499 LYS LEU TRP LYS GLU
HET F6P A 501 16
HETNAM F6P 6-O-PHOSPHONO-BETA-D-FRUCTOFURANOSE
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 HOH *118(H2 O)
HELIX 1 1 GLY A 33 MET A 49 1 17
HELIX 2 2 TRP A 65 SER A 69 5 5
HELIX 3 3 PRO A 95 PRO A 101 5 7
HELIX 4 4 TYR A 102 GLY A 118 1 17
HELIX 5 5 TYR A 128 GLY A 143 1 16
HELIX 6 6 LEU A 153 LYS A 160 1 8
HELIX 7 7 PHE A 168 LYS A 176 1 9
HELIX 8 8 LYS A 176 ALA A 191 1 16
HELIX 9 9 THR A 198 TYR A 206 1 9
HELIX 10 10 HIS A 208 ARG A 212 5 5
HELIX 11 11 ASP A 219 ASP A 221 5 3
HELIX 12 12 GLY A 240 LEU A 255 1 16
HELIX 13 13 ASP A 272 LYS A 275 5 4
HELIX 14 14 ASN A 276 GLN A 286 1 11
HELIX 15 15 ASN A 287 ALA A 294 1 8
HELIX 16 16 GLY A 314 ASN A 331 1 18
HELIX 17 17 SER A 344 SER A 357 1 14
HELIX 18 18 LEU A 373 SER A 381 1 9
HELIX 19 19 GLY A 391 LEU A 397 1 7
HELIX 20 20 ASP A 410 PHE A 422 1 13
HELIX 21 21 SER A 424 TYR A 443 1 20
HELIX 22 22 THR A 444 ARG A 462 1 19
SHEET 1 A 8 ILE A 72 TYR A 75 0
SHEET 2 A 8 THR A 78 ILE A 86 -1 O ILE A 83 N ASP A 73
SHEET 3 A 8 GLN A 52 ARG A 58 1 N VAL A 53 O LYS A 80
SHEET 4 A 8 HIS A 9 LEU A 13 1 N PHE A 12 O ASP A 54
SHEET 5 A 8 VAL A 123 HIS A 127 1 O THR A 125 N ALA A 11
SHEET 6 A 8 PHE A 146 THR A 149 1 O THR A 147 N THR A 126
SHEET 7 A 8 LYS A 193 VAL A 196 1 O ILE A 195 N PHE A 148
SHEET 8 A 8 PHE A 223 VAL A 225 1 O SER A 224 N VAL A 196
SHEET 1 B 6 VAL A 337 PRO A 341 0
SHEET 2 B 6 ASN A 295 LEU A 300 1 N LEU A 300 O PHE A 340
SHEET 3 B 6 ALA A 264 ALA A 267 1 N ILE A 265 O VAL A 297
SHEET 4 B 6 VAL A 361 LEU A 364 1 O VAL A 361 N ALA A 264
SHEET 5 B 6 ALA A 385 THR A 388 1 O VAL A 386 N PHE A 362
SHEET 6 B 6 VAL A 404 VAL A 406 1 O VAL A 404 N ALA A 385
CRYST1 154.225 48.499 75.051 90.00 100.92 90.00 C 1 2 1 4
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 0.006484 0.000000 0.001251 0.00000
SCALE2 0.000000 0.020619 0.000000 0.00000
SCALE3 0.000000 0.000000 0.013570 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
