HEADER LYASE 28-JAN-02 1KW1
TITLE CRYSTAL STRUCTURE OF 3-KETO-L-GULONATE 6-PHOSPHATE DECARBOXYLASE WITH
TITLE 2 BOUND L-GULONATE 6-PHOSPHATE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: 3-KETO-L-GULONATE 6-PHOSPHATE DECARBOXYLASE;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: HEXULOSE-6-PHOSPHATE SYNTHASE; HUMPS; D-ARABINO 3-HEXULOSE
COMPND 5 6-PHOSPHATE FORMALDEHYDE LYASE;
COMPND 6 EC: 4.1.2.-;
COMPND 7 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 3 ORGANISM_TAXID: 562;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 6 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)
KEYWDS BETA/ALPHA-BARREL, LYASE
EXPDTA X-RAY DIFFRACTION
AUTHOR E.WISE,W.S.YEW,P.C.BABBITT,J.A.GERLT,I.RAYMENT
REVDAT 3 16-AUG-23 1KW1 1 REMARK LINK
REVDAT 2 24-FEB-09 1KW1 1 VERSN
REVDAT 1 15-APR-02 1KW1 0
JRNL AUTH E.WISE,W.S.YEW,P.C.BABBITT,J.A.GERLT,I.RAYMENT
JRNL TITL HOMOLOGOUS (BETA/ALPHA)8-BARREL ENZYMES THAT CATALYZE
JRNL TITL 2 UNRELATED REACTIONS: OROTIDINE 5'-MONOPHOSPHATE
JRNL TITL 3 DECARBOXYLASE AND 3-KETO-L-GULONATE 6-PHOSPHATE
JRNL TITL 4 DECARBOXYLASE.
JRNL REF BIOCHEMISTRY V. 41 3861 2002
JRNL REFN ISSN 0006-2960
JRNL PMID 11900527
JRNL DOI 10.1021/BI012174E
REMARK 2
REMARK 2 RESOLUTION. 2.20 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 : ENGH & HUBER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.20
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 30.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 1.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 88.5
REMARK 3 NUMBER OF REFLECTIONS : 21499
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : NULL
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING SET) : 0.180
REMARK 3 FREE R VALUE : 0.212
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.900
REMARK 3 FREE R VALUE TEST SET COUNT : 1053
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 : 3278
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 36
REMARK 3 SOLVENT ATOMS : 193
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 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) : 0.006
REMARK 3 BOND ANGLES (DEGREES) : 1.200
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 : 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: NULL
REMARK 4
REMARK 4 1KW1 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 06-FEB-02.
REMARK 100 THE DEPOSITION ID IS D_1000015392.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 01-MAY-01
REMARK 200 TEMPERATURE (KELVIN) : 274
REMARK 200 PH : 7.0
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 : GOBEL MIRRORS
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : AREA DETECTOR
REMARK 200 DETECTOR MANUFACTURER : SIEMENS HI-STAR
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : FRMABO
REMARK 200 DATA SCALING SOFTWARE : XDS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 32215
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.200
REMARK 200 RESOLUTION RANGE LOW (A) : 30.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 1.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 91.2
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : 0.03000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 15.7000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.20
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.28
REMARK 200 COMPLETENESS FOR SHELL (%) : 80.0
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.09000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 3.400
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: 1KV8
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 51.14
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.52
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 18% MEPEG 5000, 50 MM BIS-TRIS
REMARK 280 PROPANE, PH 7.0, 25 MM L-GULONATE 6-PHOSPHATE. MICRO-BATCH AT
REMARK 280 298K, MICROBATCH
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 61.98900
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 21.03550
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 61.98900
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 21.03550
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 4480 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 16150 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -64.0 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
REMARK 350 BIOMOLECULE: 2
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 11290 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 29960 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -135.0 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 123.97800
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 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 SER A 2
REMARK 465 GLY A 216
REMARK 465 MET B 1
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 SER B 2 OG
REMARK 470 GLU B 120 CG CD OE1 OE2
REMARK 470 GLU B 150 CG CD OE1 OE2
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 HOH A 667 O HOH A 667 2655 2.16
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 11 52.59 -99.41
REMARK 500 ASP B 11 56.26 -90.56
REMARK 500 ASN B 80 25.06 80.54
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 602 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU A 33 OE2
REMARK 620 2 ASP A 62 OD2 103.0
REMARK 620 3 LG6 A 502 O3 148.0 100.6
REMARK 620 4 LG6 A 502 O4 88.8 163.0 64.2
REMARK 620 5 HOH A 681 O 96.8 106.8 96.9 83.5
REMARK 620 6 HOH A 682 O 76.1 93.2 81.2 77.6 159.9
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG B 601 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU B 33 OE2
REMARK 620 2 ASP B 62 OD2 99.7
REMARK 620 3 LG6 B 501 O3 156.4 102.2
REMARK 620 4 LG6 B 501 O4 94.0 166.2 64.0
REMARK 620 5 HOH B 710 O 92.3 91.7 95.7 89.6
REMARK 620 6 HOH B 711 O 83.9 100.2 83.7 79.3 167.9
REMARK 620 N 1 2 3 4 5
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG B 601
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 602
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE LG6 B 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE LG6 A 502
DBREF 1KW1 A 1 216 UNP P39304 SGAH_ECOLI 1 216
DBREF 1KW1 B 1 216 UNP P39304 SGAH_ECOLI 1 216
SEQRES 1 A 216 MET SER LEU PRO MET LEU GLN VAL ALA LEU ASP ASN GLN
SEQRES 2 A 216 THR MET ASP SER ALA TYR GLU THR THR ARG LEU ILE ALA
SEQRES 3 A 216 GLU GLU VAL ASP ILE ILE GLU VAL GLY THR ILE LEU CYS
SEQRES 4 A 216 VAL GLY GLU GLY VAL ARG ALA VAL ARG ASP LEU LYS ALA
SEQRES 5 A 216 LEU TYR PRO HIS LYS ILE VAL LEU ALA ASP ALA LYS ILE
SEQRES 6 A 216 ALA ASP ALA GLY LYS ILE LEU SER ARG MET CYS PHE GLU
SEQRES 7 A 216 ALA ASN ALA ASP TRP VAL THR VAL ILE CYS CYS ALA ASP
SEQRES 8 A 216 ILE ASN THR ALA LYS GLY ALA LEU ASP VAL ALA LYS GLU
SEQRES 9 A 216 PHE ASN GLY ASP VAL GLN ILE GLU LEU THR GLY TYR TRP
SEQRES 10 A 216 THR TRP GLU GLN ALA GLN GLN TRP ARG ASP ALA GLY ILE
SEQRES 11 A 216 GLY GLN VAL VAL TYR HIS ARG SER ARG ASP ALA GLN ALA
SEQRES 12 A 216 ALA GLY VAL ALA TRP GLY GLU ALA ASP ILE THR ALA ILE
SEQRES 13 A 216 LYS ARG LEU SER ASP MET GLY PHE LYS VAL THR VAL THR
SEQRES 14 A 216 GLY GLY LEU ALA LEU GLU ASP LEU PRO LEU PHE LYS GLY
SEQRES 15 A 216 ILE PRO ILE HIS VAL PHE ILE ALA GLY ARG SER ILE ARG
SEQRES 16 A 216 ASP ALA ALA SER PRO VAL GLU ALA ALA ARG GLN PHE LYS
SEQRES 17 A 216 ARG SER ILE ALA GLU LEU TRP GLY
SEQRES 1 B 216 MET SER LEU PRO MET LEU GLN VAL ALA LEU ASP ASN GLN
SEQRES 2 B 216 THR MET ASP SER ALA TYR GLU THR THR ARG LEU ILE ALA
SEQRES 3 B 216 GLU GLU VAL ASP ILE ILE GLU VAL GLY THR ILE LEU CYS
SEQRES 4 B 216 VAL GLY GLU GLY VAL ARG ALA VAL ARG ASP LEU LYS ALA
SEQRES 5 B 216 LEU TYR PRO HIS LYS ILE VAL LEU ALA ASP ALA LYS ILE
SEQRES 6 B 216 ALA ASP ALA GLY LYS ILE LEU SER ARG MET CYS PHE GLU
SEQRES 7 B 216 ALA ASN ALA ASP TRP VAL THR VAL ILE CYS CYS ALA ASP
SEQRES 8 B 216 ILE ASN THR ALA LYS GLY ALA LEU ASP VAL ALA LYS GLU
SEQRES 9 B 216 PHE ASN GLY ASP VAL GLN ILE GLU LEU THR GLY TYR TRP
SEQRES 10 B 216 THR TRP GLU GLN ALA GLN GLN TRP ARG ASP ALA GLY ILE
SEQRES 11 B 216 GLY GLN VAL VAL TYR HIS ARG SER ARG ASP ALA GLN ALA
SEQRES 12 B 216 ALA GLY VAL ALA TRP GLY GLU ALA ASP ILE THR ALA ILE
SEQRES 13 B 216 LYS ARG LEU SER ASP MET GLY PHE LYS VAL THR VAL THR
SEQRES 14 B 216 GLY GLY LEU ALA LEU GLU ASP LEU PRO LEU PHE LYS GLY
SEQRES 15 B 216 ILE PRO ILE HIS VAL PHE ILE ALA GLY ARG SER ILE ARG
SEQRES 16 B 216 ASP ALA ALA SER PRO VAL GLU ALA ALA ARG GLN PHE LYS
SEQRES 17 B 216 ARG SER ILE ALA GLU LEU TRP GLY
HET MG A 602 1
HET LG6 A 502 17
HET MG B 601 1
HET LG6 B 501 17
HETNAM MG MAGNESIUM ION
HETNAM LG6 L-GULURONIC ACID 6-PHOSPHATE
FORMUL 3 MG 2(MG 2+)
FORMUL 4 LG6 2(C6 H13 O10 P)
FORMUL 7 HOH *193(H2 O)
HELIX 1 1 THR A 14 ALA A 26 1 13
HELIX 2 2 GLU A 27 VAL A 29 5 3
HELIX 3 3 GLY A 35 GLY A 43 1 9
HELIX 4 4 VAL A 44 TYR A 54 1 11
HELIX 5 5 ALA A 68 ALA A 79 1 12
HELIX 6 6 ASP A 91 PHE A 105 1 15
HELIX 7 7 THR A 118 GLY A 129 1 12
HELIX 8 8 SER A 138 ALA A 144 1 7
HELIX 9 9 GLY A 149 MET A 162 1 14
HELIX 10 10 ALA A 173 LYS A 181 5 9
HELIX 11 11 GLY A 191 ASP A 196 1 6
HELIX 12 12 SER A 199 TRP A 215 1 17
HELIX 13 13 THR B 14 ALA B 26 1 13
HELIX 14 14 GLY B 35 GLY B 43 1 9
HELIX 15 15 VAL B 44 TYR B 54 1 11
HELIX 16 16 ALA B 68 ALA B 79 1 12
HELIX 17 17 ASP B 91 PHE B 105 1 15
HELIX 18 18 THR B 118 GLY B 129 1 12
HELIX 19 19 SER B 138 ALA B 144 1 7
HELIX 20 20 GLY B 149 MET B 162 1 14
HELIX 21 21 ALA B 173 LYS B 181 5 9
HELIX 22 22 GLY B 191 ASP B 196 1 6
HELIX 23 23 SER B 199 GLY B 216 1 18
SHEET 1 A 9 MET A 5 LEU A 10 0
SHEET 2 A 9 ILE A 31 VAL A 34 1 O ILE A 31 N VAL A 8
SHEET 3 A 9 ILE A 58 ILE A 65 1 O LEU A 60 N VAL A 34
SHEET 4 A 9 TRP A 83 ILE A 87 1 O TRP A 83 N ALA A 61
SHEET 5 A 9 ASP A 108 LEU A 113 1 O GLU A 112 N VAL A 86
SHEET 6 A 9 GLN A 132 HIS A 136 1 O VAL A 134 N ILE A 111
SHEET 7 A 9 LYS A 165 THR A 169 1 O THR A 167 N TYR A 135
SHEET 8 A 9 VAL A 187 ALA A 190 1 O VAL A 187 N VAL A 168
SHEET 9 A 9 MET A 5 LEU A 10 1 N GLN A 7 O PHE A 188
SHEET 1 B 9 MET B 5 LEU B 10 0
SHEET 2 B 9 ILE B 31 VAL B 34 1 O GLU B 33 N VAL B 8
SHEET 3 B 9 ILE B 58 ILE B 65 1 O LEU B 60 N VAL B 34
SHEET 4 B 9 TRP B 83 ILE B 87 1 O TRP B 83 N ALA B 61
SHEET 5 B 9 ASP B 108 LEU B 113 1 O GLU B 112 N VAL B 86
SHEET 6 B 9 GLN B 132 HIS B 136 1 O GLN B 132 N ILE B 111
SHEET 7 B 9 LYS B 165 THR B 169 1 O THR B 167 N TYR B 135
SHEET 8 B 9 VAL B 187 ALA B 190 1 O VAL B 187 N VAL B 168
SHEET 9 B 9 MET B 5 LEU B 10 1 N MET B 5 O PHE B 188
LINK OE2 GLU A 33 MG MG A 602 1555 1555 2.41
LINK OD2 ASP A 62 MG MG A 602 1555 1555 2.15
LINK O3 LG6 A 502 MG MG A 602 1555 1555 2.56
LINK O4 LG6 A 502 MG MG A 602 1555 1555 2.56
LINK MG MG A 602 O HOH A 681 1555 1555 2.36
LINK MG MG A 602 O HOH A 682 1555 1555 2.55
LINK OE2 GLU B 33 MG MG B 601 1555 1555 2.42
LINK OD2 ASP B 62 MG MG B 601 1555 1555 2.23
LINK O3 LG6 B 501 MG MG B 601 1555 1555 2.50
LINK O4 LG6 B 501 MG MG B 601 1555 1555 2.52
LINK MG MG B 601 O HOH B 710 1555 1555 2.36
LINK MG MG B 601 O HOH B 711 1555 1555 2.41
SITE 1 AC1 5 GLU B 33 ASP B 62 LG6 B 501 HOH B 710
SITE 2 AC1 5 HOH B 711
SITE 1 AC2 5 GLU A 33 ASP A 62 LG6 A 502 HOH A 681
SITE 2 AC2 5 HOH A 682
SITE 1 AC3 20 ASP A 67 ALA B 9 ASP B 11 GLU B 33
SITE 2 AC3 20 THR B 36 ASP B 62 LYS B 64 HIS B 136
SITE 3 AC3 20 THR B 169 GLY B 171 GLY B 191 ARG B 192
SITE 4 AC3 20 MG B 601 HOH B 603 HOH B 614 HOH B 616
SITE 5 AC3 20 HOH B 693 HOH B 710 HOH B 711 HOH B 712
SITE 1 AC4 20 ALA A 9 ASP A 11 GLU A 33 THR A 36
SITE 2 AC4 20 ASP A 62 LYS A 64 HIS A 136 THR A 169
SITE 3 AC4 20 GLY A 171 GLY A 191 ARG A 192 MG A 602
SITE 4 AC4 20 HOH A 604 HOH A 609 HOH A 613 HOH A 627
SITE 5 AC4 20 HOH A 630 HOH A 681 HOH A 682 ASP B 67
CRYST1 123.978 42.071 91.837 90.00 97.00 90.00 C 1 2 1 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 0.008066 0.000000 0.000990 0.00000
SCALE2 0.000000 0.023769 0.000000 0.00000
SCALE3 0.000000 0.000000 0.010971 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
