HEADER OXIDOREDUCTASE 04-NOV-10 3PHI
TITLE SHIKIMATE 5-DEHYDROGENASE (AROE) FROM HELICOBACTER PYLORI IN COMPLEX
TITLE 2 WITH SHIKIMATE AND NADPH
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: SHIKIMATE DEHYDROGENASE;
COMPND 3 CHAIN: A, B;
COMPND 4 EC: 1.1.1.25;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HELICOBACTER PYLORI;
SOURCE 3 ORGANISM_COMMON: CAMPYLOBACTER PYLORI;
SOURCE 4 ORGANISM_TAXID: 85962;
SOURCE 5 STRAIN: 26695;
SOURCE 6 GENE: AROE, HP_1249;
SOURCE 7 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 9 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 10 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 11 EXPRESSION_SYSTEM_PLASMID: PET28A
KEYWDS SHIKIMATE DEHYDROGENASE, SHIKIMATE PATHWAY, HELICOBACTER PYLORI,
KEYWDS 2 OXIDOREDUCTASE, ALPHA/BETA DOMAIN, ROSSMANN FOLD
EXPDTA X-RAY DIFFRACTION
AUTHOR W.C.CHENG,S.C.LIN,W.C.WANG
REVDAT 2 01-NOV-23 3PHI 1 REMARK SEQADV
REVDAT 1 09-NOV-11 3PHI 0
JRNL AUTH W.C.CHENG,S.C.LIN,W.C.WANG
JRNL TITL SHIKIMATE 5-DEHYDROGENASE (AROE) FROM HELICOBACTER PYLORI IN
JRNL TITL 2 COMPLEX WITH SHIKIMATE AND NADPH
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.04 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.4.0077
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.04
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 28.23
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 96.2
REMARK 3 NUMBER OF REFLECTIONS : 30682
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 + TEST SET) : 0.209
REMARK 3 R VALUE (WORKING SET) : 0.208
REMARK 3 FREE R VALUE : 0.231
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 1646
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.04
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.10
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1873
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 80.35
REMARK 3 BIN R VALUE (WORKING SET) : 0.2080
REMARK 3 BIN FREE R VALUE SET COUNT : 102
REMARK 3 BIN FREE R VALUE : 0.2210
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 4054
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 120
REMARK 3 SOLVENT ATOMS : 165
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 34.25
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 4.15000
REMARK 3 B22 (A**2) : -2.18000
REMARK 3 B33 (A**2) : -2.21000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : -0.91000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): NULL
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.183
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): NULL
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): NULL
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.940
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.926
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 4273 ; 0.015 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 5773 ; 1.656 ; 2.017
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 514 ; 5.945 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 173 ;35.637 ;24.451
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 744 ;16.001 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 12 ;18.736 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 641 ; 0.112 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 3128 ; 0.018 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 2570 ; 1.931 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 4100 ; 3.156 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1703 ; 4.975 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1673 ; 7.306 ; 4.500
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.20
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS
REMARK 4
REMARK 4 3PHI COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 25-NOV-10.
REMARK 100 THE DEPOSITION ID IS D_1000062380.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 01-NOV-08
REMARK 200 TEMPERATURE (KELVIN) : 110
REMARK 200 PH : 6.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : NSRRC
REMARK 200 BEAMLINE : BL13C1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9762
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 210
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 32329
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.040
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 (%) : 96.9
REMARK 200 DATA REDUNDANCY : 4.400
REMARK 200 R MERGE (I) : 0.03700
REMARK 200 R SYM (I) : 0.03700
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 32.2000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.05
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.12
REMARK 200 COMPLETENESS FOR SHELL (%) : 90.9
REMARK 200 DATA REDUNDANCY IN SHELL : 4.20
REMARK 200 R MERGE FOR SHELL (I) : 0.13100
REMARK 200 R SYM FOR SHELL (I) : 0.13100
REMARK 200 <I/SIGMA(I)> FOR SHELL : 10.30
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 3PHG
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 44.13
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.20
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 25% PEG 8000, 0.1M BIS-TRIS, PH 6.0,
REMARK 280 VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,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 24.19550
REMARK 290 SMTRY3 2 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: 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 350
REMARK 350 BIOMOLECULE: 2
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: 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 GLN A 115
REMARK 465 LYS A 116
REMARK 465 ASN A 117
REMARK 465 PHE A 263
REMARK 465 HIS A 264
REMARK 465 HIS A 265
REMARK 465 HIS A 266
REMARK 465 HIS A 267
REMARK 465 HIS A 268
REMARK 465 HIS A 269
REMARK 465 GLN B 115
REMARK 465 LYS B 116
REMARK 465 ASN B 117
REMARK 465 PHE B 263
REMARK 465 HIS B 264
REMARK 465 HIS B 265
REMARK 465 HIS B 266
REMARK 465 HIS B 267
REMARK 465 HIS B 268
REMARK 465 HIS B 269
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 ILE B 50 -55.41 73.59
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 SKM A 500
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NDP A 1411
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SKM B 500
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NDP B 1411
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3PHG RELATED DB: PDB
REMARK 900 THE APO FORM OF THE SAME PROTEIN
REMARK 900 RELATED ID: 3PHH RELATED DB: PDB
REMARK 900 THE SAME PROTEIN COMPLEXED WITH SHIKIMATE
REMARK 900 RELATED ID: 3PHJ RELATED DB: PDB
REMARK 900 THE SAME PROTEIN COMPLEXED WITH 3-DEHYDROSHIKIMATE
DBREF 3PHI A 1 263 UNP P56119 AROE_HELPY 1 263
DBREF 3PHI B 1 263 UNP P56119 AROE_HELPY 1 263
SEQADV 3PHI HIS A 264 UNP P56119 EXPRESSION TAG
SEQADV 3PHI HIS A 265 UNP P56119 EXPRESSION TAG
SEQADV 3PHI HIS A 266 UNP P56119 EXPRESSION TAG
SEQADV 3PHI HIS A 267 UNP P56119 EXPRESSION TAG
SEQADV 3PHI HIS A 268 UNP P56119 EXPRESSION TAG
SEQADV 3PHI HIS A 269 UNP P56119 EXPRESSION TAG
SEQADV 3PHI HIS B 264 UNP P56119 EXPRESSION TAG
SEQADV 3PHI HIS B 265 UNP P56119 EXPRESSION TAG
SEQADV 3PHI HIS B 266 UNP P56119 EXPRESSION TAG
SEQADV 3PHI HIS B 267 UNP P56119 EXPRESSION TAG
SEQADV 3PHI HIS B 268 UNP P56119 EXPRESSION TAG
SEQADV 3PHI HIS B 269 UNP P56119 EXPRESSION TAG
SEQRES 1 A 269 MET LYS LEU LYS SER PHE GLY VAL PHE GLY ASN PRO ILE
SEQRES 2 A 269 LYS HIS SER LYS SER PRO LEU ILE HIS ASN ALA CYS PHE
SEQRES 3 A 269 LEU THR PHE GLN LYS GLU LEU ARG PHE LEU GLY HIS TYR
SEQRES 4 A 269 HIS PRO ILE LEU LEU PRO LEU GLU SER HIS ILE LYS SER
SEQRES 5 A 269 GLU PHE LEU HIS LEU GLY LEU SER GLY ALA ASN VAL THR
SEQRES 6 A 269 LEU PRO PHE LYS GLU ARG ALA PHE GLN VAL CYS ASP LYS
SEQRES 7 A 269 ILE LYS GLY ILE ALA LEU GLU CYS GLY ALA VAL ASN THR
SEQRES 8 A 269 LEU VAL LEU GLU ASN ASP GLU LEU VAL GLY TYR ASN THR
SEQRES 9 A 269 ASP ALA LEU GLY PHE TYR LEU SER LEU LYS GLN LYS ASN
SEQRES 10 A 269 TYR GLN ASN ALA LEU ILE LEU GLY ALA GLY GLY SER ALA
SEQRES 11 A 269 LYS ALA LEU ALA CYS GLU LEU LYS LYS GLN GLY LEU GLN
SEQRES 12 A 269 VAL SER VAL LEU ASN ARG SER SER ARG GLY LEU ASP PHE
SEQRES 13 A 269 PHE GLN ARG LEU GLY CYS ASP CYS PHE MET GLU PRO PRO
SEQRES 14 A 269 LYS SER ALA PHE ASP LEU ILE ILE ASN ALA THR SER ALA
SEQRES 15 A 269 SER LEU HIS ASN GLU LEU PRO LEU ASN LYS GLU VAL LEU
SEQRES 16 A 269 LYS GLY TYR PHE LYS GLU GLY LYS LEU ALA TYR ASP LEU
SEQRES 17 A 269 ALA TYR GLY PHE LEU THR PRO PHE LEU SER LEU ALA LYS
SEQRES 18 A 269 GLU LEU LYS THR PRO PHE GLN ASP GLY LYS ASP MET LEU
SEQRES 19 A 269 ILE TYR GLN ALA ALA LEU SER PHE GLU LYS PHE SER ALA
SEQRES 20 A 269 SER GLN ILE PRO TYR SER LYS ALA PHE GLU VAL MET ARG
SEQRES 21 A 269 SER VAL PHE HIS HIS HIS HIS HIS HIS
SEQRES 1 B 269 MET LYS LEU LYS SER PHE GLY VAL PHE GLY ASN PRO ILE
SEQRES 2 B 269 LYS HIS SER LYS SER PRO LEU ILE HIS ASN ALA CYS PHE
SEQRES 3 B 269 LEU THR PHE GLN LYS GLU LEU ARG PHE LEU GLY HIS TYR
SEQRES 4 B 269 HIS PRO ILE LEU LEU PRO LEU GLU SER HIS ILE LYS SER
SEQRES 5 B 269 GLU PHE LEU HIS LEU GLY LEU SER GLY ALA ASN VAL THR
SEQRES 6 B 269 LEU PRO PHE LYS GLU ARG ALA PHE GLN VAL CYS ASP LYS
SEQRES 7 B 269 ILE LYS GLY ILE ALA LEU GLU CYS GLY ALA VAL ASN THR
SEQRES 8 B 269 LEU VAL LEU GLU ASN ASP GLU LEU VAL GLY TYR ASN THR
SEQRES 9 B 269 ASP ALA LEU GLY PHE TYR LEU SER LEU LYS GLN LYS ASN
SEQRES 10 B 269 TYR GLN ASN ALA LEU ILE LEU GLY ALA GLY GLY SER ALA
SEQRES 11 B 269 LYS ALA LEU ALA CYS GLU LEU LYS LYS GLN GLY LEU GLN
SEQRES 12 B 269 VAL SER VAL LEU ASN ARG SER SER ARG GLY LEU ASP PHE
SEQRES 13 B 269 PHE GLN ARG LEU GLY CYS ASP CYS PHE MET GLU PRO PRO
SEQRES 14 B 269 LYS SER ALA PHE ASP LEU ILE ILE ASN ALA THR SER ALA
SEQRES 15 B 269 SER LEU HIS ASN GLU LEU PRO LEU ASN LYS GLU VAL LEU
SEQRES 16 B 269 LYS GLY TYR PHE LYS GLU GLY LYS LEU ALA TYR ASP LEU
SEQRES 17 B 269 ALA TYR GLY PHE LEU THR PRO PHE LEU SER LEU ALA LYS
SEQRES 18 B 269 GLU LEU LYS THR PRO PHE GLN ASP GLY LYS ASP MET LEU
SEQRES 19 B 269 ILE TYR GLN ALA ALA LEU SER PHE GLU LYS PHE SER ALA
SEQRES 20 B 269 SER GLN ILE PRO TYR SER LYS ALA PHE GLU VAL MET ARG
SEQRES 21 B 269 SER VAL PHE HIS HIS HIS HIS HIS HIS
HET SKM A 500 12
HET NDP A1411 48
HET SKM B 500 12
HET NDP B1411 48
HETNAM SKM (3R,4S,5R)-3,4,5-TRIHYDROXYCYCLOHEX-1-ENE-1-CARBOXYLIC
HETNAM 2 SKM ACID
HETNAM NDP NADPH DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE
HETNAM 2 NDP PHOSPHATE
HETSYN SKM SHIKIMATE
FORMUL 3 SKM 2(C7 H10 O5)
FORMUL 4 NDP 2(C21 H30 N7 O17 P3)
FORMUL 7 HOH *165(H2 O)
HELIX 1 1 LYS A 17 PHE A 29 1 13
HELIX 2 2 PHE A 29 ARG A 34 1 6
HELIX 3 3 HIS A 49 LEU A 57 1 9
HELIX 4 4 PHE A 68 CYS A 76 1 9
HELIX 5 5 ILE A 82 GLY A 87 1 6
HELIX 6 6 THR A 104 LEU A 113 1 10
HELIX 7 7 GLY A 127 GLN A 140 1 14
HELIX 8 8 LEU A 154 GLY A 161 1 8
HELIX 9 9 ASN A 191 GLY A 202 1 12
HELIX 10 10 THR A 214 LEU A 223 1 10
HELIX 11 11 GLY A 230 SER A 246 1 17
HELIX 12 12 PRO A 251 VAL A 262 1 12
HELIX 13 13 LYS B 17 PHE B 29 1 13
HELIX 14 14 PHE B 29 ARG B 34 1 6
HELIX 15 15 ILE B 50 GLY B 58 1 9
HELIX 16 16 PHE B 68 CYS B 76 1 9
HELIX 17 17 ILE B 82 GLY B 87 1 6
HELIX 18 18 THR B 104 LEU B 113 1 10
HELIX 19 19 GLY B 127 GLN B 140 1 14
HELIX 20 20 LEU B 154 LEU B 160 1 7
HELIX 21 21 SER B 181 HIS B 185 5 5
HELIX 22 22 ASN B 191 GLY B 202 1 12
HELIX 23 23 THR B 214 LEU B 223 1 10
HELIX 24 24 GLY B 230 SER B 246 1 17
HELIX 25 25 PRO B 251 VAL B 262 1 12
SHEET 1 A 6 LEU A 36 LEU A 43 0
SHEET 2 A 6 LEU A 3 GLY A 10 1 N PHE A 6 O HIS A 38
SHEET 3 A 6 GLY A 61 VAL A 64 1 O ASN A 63 N PHE A 9
SHEET 4 A 6 THR A 91 GLU A 95 -1 O LEU A 92 N ALA A 62
SHEET 5 A 6 GLU A 98 TYR A 102 -1 O VAL A 100 N VAL A 93
SHEET 6 A 6 LYS A 78 ILE A 79 1 N LYS A 78 O GLY A 101
SHEET 1 B 6 ASP A 163 PHE A 165 0
SHEET 2 B 6 GLN A 143 LEU A 147 1 N VAL A 146 O PHE A 165
SHEET 3 B 6 ASN A 120 LEU A 124 1 N ILE A 123 O LEU A 147
SHEET 4 B 6 LEU A 175 ASN A 178 1 O LEU A 175 N LEU A 122
SHEET 5 B 6 LEU A 204 ASP A 207 1 O TYR A 206 N ASN A 178
SHEET 6 B 6 PHE A 227 GLN A 228 1 O GLN A 228 N ASP A 207
SHEET 1 C 6 LEU B 36 LEU B 43 0
SHEET 2 C 6 LEU B 3 GLY B 10 1 N PHE B 6 O HIS B 38
SHEET 3 C 6 GLY B 61 VAL B 64 1 O ASN B 63 N GLY B 7
SHEET 4 C 6 THR B 91 GLU B 95 -1 O LEU B 92 N ALA B 62
SHEET 5 C 6 GLU B 98 TYR B 102 -1 O GLU B 98 N GLU B 95
SHEET 6 C 6 LYS B 78 ILE B 79 1 N LYS B 78 O GLY B 101
SHEET 1 D 6 ASP B 163 PHE B 165 0
SHEET 2 D 6 GLN B 143 LEU B 147 1 N VAL B 146 O PHE B 165
SHEET 3 D 6 ASN B 120 LEU B 124 1 N ILE B 123 O SER B 145
SHEET 4 D 6 LEU B 175 ASN B 178 1 O ILE B 177 N LEU B 124
SHEET 5 D 6 LEU B 204 ASP B 207 1 O TYR B 206 N ILE B 176
SHEET 6 D 6 PHE B 227 GLN B 228 1 O GLN B 228 N ASP B 207
CISPEP 1 ASN A 11 PRO A 12 0 6.38
CISPEP 2 LEU A 66 PRO A 67 0 7.07
CISPEP 3 ASN B 11 PRO B 12 0 5.38
CISPEP 4 LEU B 66 PRO B 67 0 -5.90
SITE 1 AC1 12 SER A 16 SER A 18 ASN A 63 VAL A 64
SITE 2 AC1 12 THR A 65 LYS A 69 ASN A 90 ASP A 105
SITE 3 AC1 12 TYR A 210 GLN A 237 HOH A 286 NDP A1411
SITE 1 AC2 28 LEU A 66 PRO A 67 LYS A 69 ALA A 126
SITE 2 AC2 28 GLY A 127 GLY A 128 SER A 129 ASN A 148
SITE 3 AC2 28 ARG A 149 SER A 150 ALA A 179 THR A 180
SITE 4 AC2 28 SER A 181 LEU A 184 PRO A 189 LEU A 208
SITE 5 AC2 28 TYR A 210 GLY A 230 MET A 233 LEU A 234
SITE 6 AC2 28 HOH A 273 HOH A 276 HOH A 286 HOH A 306
SITE 7 AC2 28 HOH A 309 HOH A 316 HOH A 347 SKM A 500
SITE 1 AC3 11 SER B 16 SER B 18 ASN B 63 THR B 65
SITE 2 AC3 11 LYS B 69 ASN B 90 ASP B 105 TYR B 210
SITE 3 AC3 11 GLN B 237 HOH B 293 NDP B1411
SITE 1 AC4 33 LEU B 66 PRO B 67 LYS B 69 ASP B 105
SITE 2 AC4 33 GLY B 125 ALA B 126 GLY B 127 GLY B 128
SITE 3 AC4 33 SER B 129 ASN B 148 ARG B 149 SER B 150
SITE 4 AC4 33 ALA B 179 THR B 180 SER B 181 ALA B 182
SITE 5 AC4 33 LEU B 184 GLU B 187 PRO B 189 LEU B 208
SITE 6 AC4 33 TYR B 210 GLY B 230 MET B 233 LEU B 234
SITE 7 AC4 33 HOH B 271 HOH B 279 HOH B 293 HOH B 297
SITE 8 AC4 33 HOH B 309 HOH B 336 HOH B 339 HOH B 342
SITE 9 AC4 33 SKM B 500
CRYST1 44.990 48.391 123.002 90.00 97.61 90.00 P 1 21 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 0.022227 0.000000 0.002970 0.00000
SCALE2 0.000000 0.020665 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008202 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
