HEADER OXIDOREDUCTASE 31-OCT-05 2D5C
TITLE CRYSTAL STRUCTURE OF SHIKIMATE 5-DEHYDROGENASE (AROE) FROM THERMUS
TITLE 2 THERMOPHILUS HB8 IN COMPLEX WITH SHIKIMATE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: SHIKIMATE 5-DEHYDROGENASE;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: AROE;
COMPND 5 EC: 1.1.1.25;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: THERMUS THERMOPHILUS;
SOURCE 3 ORGANISM_TAXID: 300852;
SOURCE 4 STRAIN: HB8;
SOURCE 5 GENE: AROE;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET 11A
KEYWDS SHIKIMATE, SUBSTRATE, DIMER, STRUCTURAL GENOMICS, NPPSFA, NATIONAL
KEYWDS 2 PROJECT ON PROTEIN STRUCTURAL AND FUNCTIONAL ANALYSES, RIKEN
KEYWDS 3 STRUCTURAL GENOMICS/PROTEOMICS INITIATIVE, RSGI, OXIDOREDUCTASE
EXPDTA X-RAY DIFFRACTION
AUTHOR B.BAGAUTDINOV,N.KUNISHIMA,RIKEN STRUCTURAL GENOMICS/PROTEOMICS
AUTHOR 2 INITIATIVE (RSGI)
REVDAT 5 25-OCT-23 2D5C 1 REMARK
REVDAT 4 13-JUL-11 2D5C 1 VERSN
REVDAT 3 24-FEB-09 2D5C 1 VERSN
REVDAT 2 13-NOV-07 2D5C 1 JRNL
REVDAT 1 01-MAY-06 2D5C 0
JRNL AUTH B.BAGAUTDINOV,N.KUNISHIMA
JRNL TITL CRYSTAL STRUCTURES OF SHIKIMATE DEHYDROGENASE AROE FROM
JRNL TITL 2 THERMUS THERMOPHILUS HB8 AND ITS COFACTOR AND SUBSTRATE
JRNL TITL 3 COMPLEXES: INSIGHTS INTO THE ENZYMATIC MECHANISM
JRNL REF J.MOL.BIOL. V. 373 424 2007
JRNL REFN ISSN 0022-2836
JRNL PMID 17825835
JRNL DOI 10.1016/J.JMB.2007.08.017
REMARK 2
REMARK 2 RESOLUTION. 1.65 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) : 1.65
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 35.13
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 93.5
REMARK 3 NUMBER OF REFLECTIONS : 52062
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) : 0.200
REMARK 3 FREE R VALUE : 0.235
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : 2583
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 : 3960
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 44
REMARK 3 SOLVENT ATOMS : 459
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 28.30
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 34.10
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -7.51000
REMARK 3 B22 (A**2) : 6.14000
REMARK 3 B33 (A**2) : 1.38000
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) : 0.21
REMARK 3 ESD FROM SIGMAA (A) : 0.24
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) : 0.27
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.27
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.007
REMARK 3 BOND ANGLES (DEGREES) : 1.400
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 23.30
REMARK 3 IMPROPER ANGLES (DEGREES) : 0.950
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : OVERALL
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 2D5C COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 08-NOV-05.
REMARK 100 THE DEPOSITION ID IS D_1000025005.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 22-JUL-05
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 4.6
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SPRING-8
REMARK 200 BEAMLINE : BL26B1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1
REMARK 200 MONOCHROMATOR : GRAPHITE
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 52062
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.650
REMARK 200 RESOLUTION RANGE LOW (A) : 40.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 93.7
REMARK 200 DATA REDUNDANCY : 2.400
REMARK 200 R MERGE (I) : 0.05000
REMARK 200 R SYM (I) : 0.04400
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 19.3000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.65
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.71
REMARK 200 COMPLETENESS FOR SHELL (%) : 71.6
REMARK 200 DATA REDUNDANCY IN SHELL : 2.90
REMARK 200 R MERGE FOR SHELL (I) : 0.39500
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 1.1
REMARK 200 STARTING MODEL: PDB ENTRY 1WXD
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 38.66
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.01
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: AMMONIUM SULFATE, SODIUM ACETATE
REMARK 280 TRIHYDRATE, PEG4000, PH 4.6, MICROBATCH, TEMPERATURE 295K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
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 31.40550
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 56.58650
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 31.97200
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 56.58650
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 31.40550
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 31.97200
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: DIMERIC
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 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 GLY A 262
REMARK 465 VAL A 263
REMARK 465 GLU B 184
REMARK 465 ASP B 185
REMARK 465 PRO B 186
REMARK 465 SER B 187
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 9 113.08 -167.22
REMARK 500 LEU A 161 -158.46 -110.10
REMARK 500 ASP A 185 87.69 -150.27
REMARK 500 PRO B 62 51.27 -112.42
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 1401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 1402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 1403
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 1404
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SKM A 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SKM B 302
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1WXD RELATED DB: PDB
REMARK 900 THE SAME PROTEIN IN APO FORM
REMARK 900 RELATED ID: 2CY0 RELATED DB: PDB
REMARK 900 THE SAME PROTEIN IN COMPLEX WITH NADP
REMARK 900 RELATED ID: 2EV9 RELATED DB: PDB
REMARK 900 THE SAME PROTEIN IN COMPLEX WITH NADP AND SHIKIMATE
REMARK 900 RELATED ID: TTK003000004.4 RELATED DB: TARGETDB
DBREF 2D5C A 1 263 UNP Q5SJF8 Q5SJF8_THET8 1 263
DBREF 2D5C B 1 263 UNP Q5SJF8 Q5SJF8_THET8 1 263
SEQRES 1 A 263 MET LEU ARG PHE ALA VAL LEU GLY HIS PRO VAL ALA HIS
SEQRES 2 A 263 SER LEU SER PRO ALA MET HIS ALA PHE ALA LEU GLU SER
SEQRES 3 A 263 LEU GLY LEU GLU GLY SER TYR GLU ALA TRP ASP THR PRO
SEQRES 4 A 263 LEU GLU ALA LEU PRO GLY ARG LEU LYS GLU VAL ARG ARG
SEQRES 5 A 263 ALA PHE ARG GLY VAL ASN LEU THR LEU PRO LEU LYS GLU
SEQRES 6 A 263 ALA ALA LEU ALA HIS LEU ASP TRP VAL SER PRO GLU ALA
SEQRES 7 A 263 GLN ARG ILE GLY ALA VAL ASN THR VAL LEU GLN VAL GLU
SEQRES 8 A 263 GLY ARG LEU PHE GLY PHE ASN THR ASP ALA PRO GLY PHE
SEQRES 9 A 263 LEU GLU ALA LEU LYS ALA GLY GLY ILE PRO LEU LYS GLY
SEQRES 10 A 263 PRO ALA LEU VAL LEU GLY ALA GLY GLY ALA GLY ARG ALA
SEQRES 11 A 263 VAL ALA PHE ALA LEU ARG GLU ALA GLY LEU GLU VAL TRP
SEQRES 12 A 263 VAL TRP ASN ARG THR PRO GLN ARG ALA LEU ALA LEU ALA
SEQRES 13 A 263 GLU GLU PHE GLY LEU ARG ALA VAL PRO LEU GLU LYS ALA
SEQRES 14 A 263 ARG GLU ALA ARG LEU LEU VAL ASN ALA THR ARG VAL GLY
SEQRES 15 A 263 LEU GLU ASP PRO SER ALA SER PRO LEU PRO ALA GLU LEU
SEQRES 16 A 263 PHE PRO GLU GLU GLY ALA ALA VAL ASP LEU VAL TYR ARG
SEQRES 17 A 263 PRO LEU TRP THR ARG PHE LEU ARG GLU ALA LYS ALA LYS
SEQRES 18 A 263 GLY LEU LYS VAL GLN THR GLY LEU PRO MET LEU ALA TRP
SEQRES 19 A 263 GLN GLY ALA LEU ALA PHE ARG LEU TRP THR GLY LEU LEU
SEQRES 20 A 263 PRO ASP PRO SER GLY MET GLU GLU ALA ALA ARG ARG ALA
SEQRES 21 A 263 LEU GLY VAL
SEQRES 1 B 263 MET LEU ARG PHE ALA VAL LEU GLY HIS PRO VAL ALA HIS
SEQRES 2 B 263 SER LEU SER PRO ALA MET HIS ALA PHE ALA LEU GLU SER
SEQRES 3 B 263 LEU GLY LEU GLU GLY SER TYR GLU ALA TRP ASP THR PRO
SEQRES 4 B 263 LEU GLU ALA LEU PRO GLY ARG LEU LYS GLU VAL ARG ARG
SEQRES 5 B 263 ALA PHE ARG GLY VAL ASN LEU THR LEU PRO LEU LYS GLU
SEQRES 6 B 263 ALA ALA LEU ALA HIS LEU ASP TRP VAL SER PRO GLU ALA
SEQRES 7 B 263 GLN ARG ILE GLY ALA VAL ASN THR VAL LEU GLN VAL GLU
SEQRES 8 B 263 GLY ARG LEU PHE GLY PHE ASN THR ASP ALA PRO GLY PHE
SEQRES 9 B 263 LEU GLU ALA LEU LYS ALA GLY GLY ILE PRO LEU LYS GLY
SEQRES 10 B 263 PRO ALA LEU VAL LEU GLY ALA GLY GLY ALA GLY ARG ALA
SEQRES 11 B 263 VAL ALA PHE ALA LEU ARG GLU ALA GLY LEU GLU VAL TRP
SEQRES 12 B 263 VAL TRP ASN ARG THR PRO GLN ARG ALA LEU ALA LEU ALA
SEQRES 13 B 263 GLU GLU PHE GLY LEU ARG ALA VAL PRO LEU GLU LYS ALA
SEQRES 14 B 263 ARG GLU ALA ARG LEU LEU VAL ASN ALA THR ARG VAL GLY
SEQRES 15 B 263 LEU GLU ASP PRO SER ALA SER PRO LEU PRO ALA GLU LEU
SEQRES 16 B 263 PHE PRO GLU GLU GLY ALA ALA VAL ASP LEU VAL TYR ARG
SEQRES 17 B 263 PRO LEU TRP THR ARG PHE LEU ARG GLU ALA LYS ALA LYS
SEQRES 18 B 263 GLY LEU LYS VAL GLN THR GLY LEU PRO MET LEU ALA TRP
SEQRES 19 B 263 GLN GLY ALA LEU ALA PHE ARG LEU TRP THR GLY LEU LEU
SEQRES 20 B 263 PRO ASP PRO SER GLY MET GLU GLU ALA ALA ARG ARG ALA
SEQRES 21 B 263 LEU GLY VAL
HET SO4 A1401 5
HET SO4 A1403 5
HET SKM A 301 12
HET SO4 B1402 5
HET SO4 B1404 5
HET SKM B 302 12
HETNAM SO4 SULFATE ION
HETNAM SKM (3R,4S,5R)-3,4,5-TRIHYDROXYCYCLOHEX-1-ENE-1-CARBOXYLIC
HETNAM 2 SKM ACID
HETSYN SKM SHIKIMATE
FORMUL 3 SO4 4(O4 S 2-)
FORMUL 5 SKM 2(C7 H10 O5)
FORMUL 9 HOH *459(H2 O)
HELIX 1 1 LEU A 15 LEU A 27 1 13
HELIX 2 2 PRO A 39 GLU A 41 5 3
HELIX 3 3 ALA A 42 PHE A 54 1 13
HELIX 4 4 GLU A 65 LEU A 71 5 7
HELIX 5 5 SER A 75 GLY A 82 1 8
HELIX 6 6 THR A 99 GLY A 111 1 13
HELIX 7 7 GLY A 125 ALA A 138 1 14
HELIX 8 8 THR A 148 GLY A 160 1 13
HELIX 9 9 PRO A 165 ALA A 172 5 8
HELIX 10 10 PRO A 192 PHE A 196 5 5
HELIX 11 11 THR A 212 LYS A 221 1 10
HELIX 12 12 GLY A 228 GLY A 245 1 18
HELIX 13 13 ASP A 249 LEU A 261 1 13
HELIX 14 14 LEU B 15 LEU B 27 1 13
HELIX 15 15 PRO B 39 GLU B 41 5 3
HELIX 16 16 ALA B 42 PHE B 54 1 13
HELIX 17 17 ALA B 67 LEU B 71 5 5
HELIX 18 18 SER B 75 GLY B 82 1 8
HELIX 19 19 THR B 99 GLY B 111 1 13
HELIX 20 20 GLY B 125 ALA B 138 1 14
HELIX 21 21 THR B 148 GLY B 160 1 13
HELIX 22 22 PRO B 165 ALA B 172 5 8
HELIX 23 23 PRO B 192 PHE B 196 5 5
HELIX 24 24 THR B 212 LYS B 221 1 10
HELIX 25 25 GLY B 228 GLY B 245 1 18
HELIX 26 26 ASP B 249 GLY B 262 1 14
SHEET 1 A 6 GLY A 31 ASP A 37 0
SHEET 2 A 6 LEU A 2 GLY A 8 1 N PHE A 4 O SER A 32
SHEET 3 A 6 GLY A 56 LEU A 59 1 O ASN A 58 N LEU A 7
SHEET 4 A 6 THR A 86 VAL A 90 -1 O VAL A 87 N VAL A 57
SHEET 5 A 6 ARG A 93 PHE A 97 -1 O PHE A 97 N THR A 86
SHEET 6 A 6 TRP A 73 VAL A 74 1 N TRP A 73 O GLY A 96
SHEET 1 B 6 ARG A 162 ALA A 163 0
SHEET 2 B 6 VAL A 142 TRP A 145 1 N VAL A 144 O ARG A 162
SHEET 3 B 6 ALA A 119 LEU A 122 1 N ALA A 119 O TRP A 143
SHEET 4 B 6 LEU A 174 ASN A 177 1 O LEU A 174 N LEU A 120
SHEET 5 B 6 ALA A 201 ASP A 204 1 O VAL A 203 N ASN A 177
SHEET 6 B 6 LYS A 224 GLN A 226 1 O LYS A 224 N ALA A 202
SHEET 1 C 6 GLY B 31 ASP B 37 0
SHEET 2 C 6 LEU B 2 GLY B 8 1 N PHE B 4 O SER B 32
SHEET 3 C 6 GLY B 56 LEU B 59 1 O ASN B 58 N LEU B 7
SHEET 4 C 6 THR B 86 VAL B 90 -1 O VAL B 87 N VAL B 57
SHEET 5 C 6 ARG B 93 PHE B 97 -1 O PHE B 97 N THR B 86
SHEET 6 C 6 TRP B 73 VAL B 74 1 N TRP B 73 O GLY B 96
SHEET 1 D 6 ARG B 162 ALA B 163 0
SHEET 2 D 6 VAL B 142 TRP B 145 1 N VAL B 144 O ARG B 162
SHEET 3 D 6 ALA B 119 LEU B 122 1 N ALA B 119 O TRP B 143
SHEET 4 D 6 LEU B 174 ASN B 177 1 O VAL B 176 N LEU B 122
SHEET 5 D 6 ALA B 201 ASP B 204 1 O VAL B 203 N LEU B 175
SHEET 6 D 6 LYS B 224 GLN B 226 1 O LYS B 224 N ALA B 202
CISPEP 1 HIS A 9 PRO A 10 0 -0.09
CISPEP 2 LEU A 61 PRO A 62 0 -0.43
CISPEP 3 GLY A 117 PRO A 118 0 -0.14
CISPEP 4 ARG A 208 PRO A 209 0 -0.27
CISPEP 5 HIS B 9 PRO B 10 0 -0.03
CISPEP 6 LEU B 61 PRO B 62 0 0.00
CISPEP 7 GLY B 117 PRO B 118 0 -0.16
SITE 1 AC1 11 LYS A 109 PRO A 192 ALA A 193 ARG A 213
SITE 2 AC1 11 HOH A1413 HOH A1429 HOH A1466 HOH A1550
SITE 3 AC1 11 HOH A1642 ARG B 162 HOH B1480
SITE 1 AC2 8 ARG A 241 LEU A 242 GLN B 89 VAL B 90
SITE 2 AC2 8 GLU B 91 HOH B1409 HOH B1413 HOH B1454
SITE 1 AC3 6 GLN A 226 THR A 227 ARG A 258 HOH A1572
SITE 2 AC3 6 HOH A1590 HOH A1635
SITE 1 AC4 7 GLU A 157 ARG B 180 ALA B 188 SER B 189
SITE 2 AC4 7 THR B 212 ARG B 213 PHE B 214
SITE 1 AC5 11 VAL A 6 SER A 14 SER A 16 ASN A 58
SITE 2 AC5 11 LEU A 59 THR A 60 LYS A 64 ASN A 85
SITE 3 AC5 11 ASP A 100 TYR A 207 GLN A 235
SITE 1 AC6 9 SER B 14 SER B 16 ASN B 58 THR B 60
SITE 2 AC6 9 LYS B 64 ASN B 85 ASP B 100 GLN B 235
SITE 3 AC6 9 HOH B1421
CRYST1 62.811 63.944 113.173 90.00 90.00 90.00 P 21 21 21 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 0.015921 0.000000 0.000000 0.00000
SCALE2 0.000000 0.015639 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008836 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
