HEADER TRANSFERASE 09-JUN-04 1WKV
TITLE CRYSTAL STRUCTURE OF O-PHOSPHOSERINE SULFHYDRYLASE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CYSTEINE SYNTHASE;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: O-PHOSPHOSERINE SULFHYDRYLASE;
COMPND 5 EC: 2.5.1.-;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: AEROPYRUM PERNIX;
SOURCE 3 ORGANISM_TAXID: 272557;
SOURCE 4 STRAIN: K1;
SOURCE 5 GENE: APE1586;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: ROSETTA(DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PAPE1586
KEYWDS HOMODIMER, OPEN ALPHA/BETA FOLDING, TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR Y.ODA,K.MINO,K.ISHIKAWA,M.ATAKA
REVDAT 4 13-JUL-11 1WKV 1 VERSN
REVDAT 3 24-FEB-09 1WKV 1 VERSN
REVDAT 2 02-AUG-05 1WKV 1 JRNL
REVDAT 1 28-JUN-05 1WKV 0
JRNL AUTH Y.ODA,K.MINO,K.ISHIKAWA,M.ATAKA
JRNL TITL THREE-DIMENSIONAL STRUCTURE OF A NEW ENZYME, O-PHOSPHOSERINE
JRNL TITL 2 SULFHYDRYLASE, INVOLVED IN L-CYSTEINE BIOSYNTHESIS BY A
JRNL TITL 3 HYPERTHERMOPHILIC ARCHAEON, AEROPYRUM PERNIX K1, AT 2.0A
JRNL TITL 4 RESOLUTION
JRNL REF J.MOL.BIOL. V. 351 334 2005
JRNL REFN ISSN 0022-2836
JRNL PMID 16005886
JRNL DOI 10.1016/J.JMB.2005.05.064
REMARK 2
REMARK 2 RESOLUTION. 2.00 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.1.24
REMARK 3 AUTHORS : MURSHUDOV,VAGIN,DODSON
REMARK 3
REMARK 3 REFINEMENT TARGET : CCP4 LIBRARY
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.00
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 33.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 93.1
REMARK 3 NUMBER OF REFLECTIONS : 50639
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) : 0.190
REMARK 3 R VALUE (WORKING SET) : 0.188
REMARK 3 FREE R VALUE : 0.231
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : 2163
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) : 2.00
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.08
REMARK 3 REFLECTION IN BIN (WORKING SET) : NULL
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : 0.2700
REMARK 3 BIN FREE R VALUE SET COUNT : 136
REMARK 3 BIN FREE R VALUE : 0.3200
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 5834
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 38
REMARK 3 SOLVENT ATOMS : 634
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 23.00
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 27.40
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 OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): NULL
REMARK 3 ESU BASED ON FREE R VALUE (A): NULL
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 : NULL
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : NULL
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): NULL ; 0.011 ; NULL
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; 0.002 ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): NULL ; 1.521 ; NULL
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; 1.240 ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): NULL ; 6.213 ; NULL
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): NULL ; NULL ; NULL
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): NULL ; NULL ; NULL
REMARK 3 GENERAL PLANES REFINED ATOMS (A): NULL ; NULL ; NULL
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): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED 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 : NULL
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : NULL
REMARK 3 ION PROBE RADIUS : NULL
REMARK 3 SHRINKAGE RADIUS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1WKV COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 14-JUN-04.
REMARK 100 THE RCSB ID CODE IS RCSB023687.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 26-NOV-03
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SPRING-8
REMARK 200 BEAMLINE : BL40B2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9797
REMARK 200 MONOCHROMATOR : DOUBLE CRYSTAL MONOCHROMATOR,
REMARK 200 BENT-CYLINDER MIRROR
REMARK 200 OPTICS : DOUBLE CRYSTAL MONOCHROMATOR,
REMARK 200 BENT-CYLINDER MIRROR
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 4
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 52917
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.000
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 97.3
REMARK 200 DATA REDUNDANCY : 6.400
REMARK 200 R MERGE (I) : 0.06300
REMARK 200 R SYM (I) : 0.06300
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 11.0000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.00
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.07
REMARK 200 COMPLETENESS FOR SHELL (%) : 82.4
REMARK 200 DATA REDUNDANCY IN SHELL : 3.70
REMARK 200 R MERGE FOR SHELL (I) : 0.27800
REMARK 200 R SYM FOR SHELL (I) : 0.27800
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: MAD
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MAD
REMARK 200 SOFTWARE USED: SOLVE
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 45.60
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.26
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PYRIDOXAL 5'-PHOSPHATE, 2-
REMARK 280 MERCAPTOETHANOL, CACODYLATE, SODIUM ACETATE, PEG 8000, PH 7.0,
REMARK 280 VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 298K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 43 21 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z+1/2
REMARK 290 3555 -Y+1/2,X+1/2,Z+3/4
REMARK 290 4555 Y+1/2,-X+1/2,Z+1/4
REMARK 290 5555 -X+1/2,Y+1/2,-Z+3/4
REMARK 290 6555 X+1/2,-Y+1/2,-Z+1/4
REMARK 290 7555 Y,X,-Z
REMARK 290 8555 -Y,-X,-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 137.95400
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 37.43700
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 37.43700
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 206.93100
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 37.43700
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 37.43700
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 68.97700
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 37.43700
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 37.43700
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 206.93100
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 37.43700
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 37.43700
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 68.97700
REMARK 290 SMTRY1 7 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 7 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 137.95400
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 6710 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 26110 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -48.0 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 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 GLY A 384
REMARK 465 ALA A 385
REMARK 465 GLY A 386
REMARK 465 ASP A 387
REMARK 465 SER A 388
REMARK 465 VAL A 389
REMARK 465 MET B 1
REMARK 465 ALA B 385
REMARK 465 GLY B 386
REMARK 465 ASP B 387
REMARK 465 SER B 388
REMARK 465 VAL B 389
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
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,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
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 ATM2 ATM3
REMARK 500 LEU A 138 CA - CB - CG ANGL. DEV. = 14.0 DEGREES
REMARK 500 ARG A 170 NE - CZ - NH1 ANGL. DEV. = 3.3 DEGREES
REMARK 500 ASP A 362 CB - CG - OD2 ANGL. DEV. = 5.7 DEGREES
REMARK 500 ASP B 14 CB - CG - OD2 ANGL. DEV. = 5.7 DEGREES
REMARK 500 ASP B 75 CB - CG - OD1 ANGL. DEV. = 6.2 DEGREES
REMARK 500 LEU B 138 CA - CB - CG ANGL. DEV. = 15.6 DEGREES
REMARK 500 ASP B 334 CB - CG - OD2 ANGL. DEV. = 5.9 DEGREES
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 223 73.52 41.68
REMARK 500 SER A 263 1.80 83.21
REMARK 500 ASP B 75 49.46 -82.57
REMARK 500 PHE B 122 -67.66 -96.79
REMARK 500 ASN B 223 74.32 37.44
REMARK 500 SER B 263 4.50 82.02
REMARK 500 LEU B 304 -73.98 -79.06
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH A1555 DISTANCE = 5.55 ANGSTROMS
REMARK 525 HOH A1657 DISTANCE = 5.13 ANGSTROMS
REMARK 525 HOH A1681 DISTANCE = 5.03 ANGSTROMS
REMARK 525 HOH B2723 DISTANCE = 5.88 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT A 1401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT B 2401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PLP A 400
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PLP B 400
DBREF 1WKV A 1 389 UNP Q9YBL2 CYSO_AERPE 1 389
DBREF 1WKV B 1 389 UNP Q9YBL2 CYSO_AERPE 1 389
SEQRES 1 A 389 MET ALA LEU ALA ASP ILE SER GLY TYR LEU ASP VAL LEU
SEQRES 2 A 389 ASP SER VAL ARG GLY PHE SER TYR LEU GLU ASN ALA ARG
SEQRES 3 A 389 GLU VAL LEU ARG SER GLY GLU ALA ARG CYS LEU GLY ASN
SEQRES 4 A 389 PRO ARG SER GLU PRO GLU TYR VAL LYS ALA LEU TYR VAL
SEQRES 5 A 389 ILE GLY ALA SER ARG ILE PRO VAL GLY ASP GLY CYS SER
SEQRES 6 A 389 HIS THR LEU GLU GLU LEU GLY VAL PHE ASP ILE SER VAL
SEQRES 7 A 389 PRO GLY GLU MET VAL PHE PRO SER PRO LEU ASP PHE PHE
SEQRES 8 A 389 GLU ARG GLY LYS PRO THR PRO LEU VAL ARG SER ARG LEU
SEQRES 9 A 389 GLN LEU PRO ASN GLY VAL ARG VAL TRP LEU LYS LEU GLU
SEQRES 10 A 389 TRP TYR ASN PRO PHE SER LEU SER VAL LYS ASP ARG PRO
SEQRES 11 A 389 ALA VAL GLU ILE ILE SER ARG LEU SER ARG ARG VAL GLU
SEQRES 12 A 389 LYS GLY SER LEU VAL ALA ASP ALA THR SER SER ASN PHE
SEQRES 13 A 389 GLY VAL ALA LEU SER ALA VAL ALA ARG LEU TYR GLY TYR
SEQRES 14 A 389 ARG ALA ARG VAL TYR LEU PRO GLY ALA ALA GLU GLU PHE
SEQRES 15 A 389 GLY LYS LEU LEU PRO ARG LEU LEU GLY ALA GLN VAL ILE
SEQRES 16 A 389 VAL ASP PRO GLU ALA PRO SER THR VAL HIS LEU LEU PRO
SEQRES 17 A 389 ARG VAL MET LYS ASP SER LYS ASN GLU GLY PHE VAL HIS
SEQRES 18 A 389 VAL ASN GLN PHE TYR ASN ASP ALA ASN PHE GLU ALA HIS
SEQRES 19 A 389 MET ARG GLY THR ALA ARG GLU ILE PHE VAL GLN SER ARG
SEQRES 20 A 389 ARG GLY GLY LEU ALA LEU ARG GLY VAL ALA GLY SER LEU
SEQRES 21 A 389 GLY THR SER GLY HIS MET SER ALA ALA ALA PHE TYR LEU
SEQRES 22 A 389 GLN SER VAL ASP PRO SER ILE ARG ALA VAL LEU VAL GLN
SEQRES 23 A 389 PRO ALA GLN GLY ASP SER ILE PRO GLY ILE ARG ARG VAL
SEQRES 24 A 389 GLU THR GLY MET LEU TRP ILE ASN MET LEU ASP ILE SER
SEQRES 25 A 389 TYR THR LEU ALA GLU VAL THR LEU GLU GLU ALA MET GLU
SEQRES 26 A 389 ALA VAL VAL GLU VAL ALA ARG SER ASP GLY LEU VAL ILE
SEQRES 27 A 389 GLY PRO SER GLY GLY ALA ALA VAL LYS ALA LEU ALA LYS
SEQRES 28 A 389 LYS ALA ALA GLU GLY ASP LEU GLU PRO GLY ASP TYR VAL
SEQRES 29 A 389 VAL VAL VAL PRO ASP THR GLY PHE LYS TYR LEU SER LEU
SEQRES 30 A 389 VAL GLN ASN ALA LEU GLU GLY ALA GLY ASP SER VAL
SEQRES 1 B 389 MET ALA LEU ALA ASP ILE SER GLY TYR LEU ASP VAL LEU
SEQRES 2 B 389 ASP SER VAL ARG GLY PHE SER TYR LEU GLU ASN ALA ARG
SEQRES 3 B 389 GLU VAL LEU ARG SER GLY GLU ALA ARG CYS LEU GLY ASN
SEQRES 4 B 389 PRO ARG SER GLU PRO GLU TYR VAL LYS ALA LEU TYR VAL
SEQRES 5 B 389 ILE GLY ALA SER ARG ILE PRO VAL GLY ASP GLY CYS SER
SEQRES 6 B 389 HIS THR LEU GLU GLU LEU GLY VAL PHE ASP ILE SER VAL
SEQRES 7 B 389 PRO GLY GLU MET VAL PHE PRO SER PRO LEU ASP PHE PHE
SEQRES 8 B 389 GLU ARG GLY LYS PRO THR PRO LEU VAL ARG SER ARG LEU
SEQRES 9 B 389 GLN LEU PRO ASN GLY VAL ARG VAL TRP LEU LYS LEU GLU
SEQRES 10 B 389 TRP TYR ASN PRO PHE SER LEU SER VAL LYS ASP ARG PRO
SEQRES 11 B 389 ALA VAL GLU ILE ILE SER ARG LEU SER ARG ARG VAL GLU
SEQRES 12 B 389 LYS GLY SER LEU VAL ALA ASP ALA THR SER SER ASN PHE
SEQRES 13 B 389 GLY VAL ALA LEU SER ALA VAL ALA ARG LEU TYR GLY TYR
SEQRES 14 B 389 ARG ALA ARG VAL TYR LEU PRO GLY ALA ALA GLU GLU PHE
SEQRES 15 B 389 GLY LYS LEU LEU PRO ARG LEU LEU GLY ALA GLN VAL ILE
SEQRES 16 B 389 VAL ASP PRO GLU ALA PRO SER THR VAL HIS LEU LEU PRO
SEQRES 17 B 389 ARG VAL MET LYS ASP SER LYS ASN GLU GLY PHE VAL HIS
SEQRES 18 B 389 VAL ASN GLN PHE TYR ASN ASP ALA ASN PHE GLU ALA HIS
SEQRES 19 B 389 MET ARG GLY THR ALA ARG GLU ILE PHE VAL GLN SER ARG
SEQRES 20 B 389 ARG GLY GLY LEU ALA LEU ARG GLY VAL ALA GLY SER LEU
SEQRES 21 B 389 GLY THR SER GLY HIS MET SER ALA ALA ALA PHE TYR LEU
SEQRES 22 B 389 GLN SER VAL ASP PRO SER ILE ARG ALA VAL LEU VAL GLN
SEQRES 23 B 389 PRO ALA GLN GLY ASP SER ILE PRO GLY ILE ARG ARG VAL
SEQRES 24 B 389 GLU THR GLY MET LEU TRP ILE ASN MET LEU ASP ILE SER
SEQRES 25 B 389 TYR THR LEU ALA GLU VAL THR LEU GLU GLU ALA MET GLU
SEQRES 26 B 389 ALA VAL VAL GLU VAL ALA ARG SER ASP GLY LEU VAL ILE
SEQRES 27 B 389 GLY PRO SER GLY GLY ALA ALA VAL LYS ALA LEU ALA LYS
SEQRES 28 B 389 LYS ALA ALA GLU GLY ASP LEU GLU PRO GLY ASP TYR VAL
SEQRES 29 B 389 VAL VAL VAL PRO ASP THR GLY PHE LYS TYR LEU SER LEU
SEQRES 30 B 389 VAL GLN ASN ALA LEU GLU GLY ALA GLY ASP SER VAL
HET ACT A1401 4
HET ACT B2401 4
HET PLP A 400 15
HET PLP B 400 15
HETNAM ACT ACETATE ION
HETNAM PLP PYRIDOXAL-5'-PHOSPHATE
HETSYN PLP VITAMIN B6 PHOSPHATE
FORMUL 3 ACT 2(C2 H3 O2 1-)
FORMUL 5 PLP 2(C8 H10 N O6 P)
FORMUL 7 HOH *634(H2 O)
HELIX 1 1 SER A 7 LEU A 10 5 4
HELIX 2 2 ASP A 11 VAL A 16 1 6
HELIX 3 3 TYR A 21 GLY A 32 1 12
HELIX 4 4 ASN A 39 SER A 42 5 4
HELIX 5 5 GLU A 43 GLY A 54 1 12
HELIX 6 6 SER A 86 GLY A 94 1 9
HELIX 7 7 TRP A 118 ASN A 120 5 3
HELIX 8 8 LYS A 127 SER A 139 1 13
HELIX 9 9 SER A 153 TYR A 167 1 15
HELIX 10 10 GLU A 180 LEU A 190 1 11
HELIX 11 11 THR A 203 HIS A 205 5 3
HELIX 12 12 LEU A 206 GLY A 218 1 13
HELIX 13 13 ASN A 227 GLY A 237 1 11
HELIX 14 14 GLY A 237 GLY A 249 1 13
HELIX 15 15 SER A 263 ASP A 277 1 15
HELIX 16 16 ARG A 298 GLY A 302 5 5
HELIX 17 17 LEU A 304 LEU A 309 1 6
HELIX 18 18 THR A 319 GLY A 335 1 17
HELIX 19 19 GLY A 339 GLU A 355 1 17
HELIX 20 20 THR A 370 LYS A 373 5 4
HELIX 21 21 TYR A 374 GLU A 383 1 10
HELIX 22 22 SER B 7 LEU B 10 5 4
HELIX 23 23 ASP B 11 VAL B 16 1 6
HELIX 24 24 TYR B 21 GLY B 32 1 12
HELIX 25 25 ASN B 39 SER B 42 5 4
HELIX 26 26 GLU B 43 GLY B 54 1 12
HELIX 27 27 SER B 86 GLY B 94 1 9
HELIX 28 28 TRP B 118 ASN B 120 5 3
HELIX 29 29 LYS B 127 ARG B 137 1 11
HELIX 30 30 SER B 153 TYR B 167 1 15
HELIX 31 31 GLU B 180 LEU B 190 1 11
HELIX 32 32 THR B 203 HIS B 205 5 3
HELIX 33 33 LEU B 206 GLY B 218 1 13
HELIX 34 34 ASN B 227 GLY B 237 1 11
HELIX 35 35 GLY B 237 GLY B 249 1 13
HELIX 36 36 SER B 263 ASP B 277 1 15
HELIX 37 37 ARG B 298 GLY B 302 5 5
HELIX 38 38 LEU B 304 LEU B 309 1 6
HELIX 39 39 THR B 319 GLY B 335 1 17
HELIX 40 40 GLY B 339 GLU B 355 1 17
HELIX 41 41 THR B 370 LYS B 373 5 4
HELIX 42 42 TYR B 374 GLU B 383 1 10
SHEET 1 A 2 LEU A 3 ASP A 5 0
SHEET 2 A 2 ARG A 57 PRO A 59 -1 O ILE A 58 N ALA A 4
SHEET 1 B 2 GLU A 33 ARG A 35 0
SHEET 2 B 2 SER A 65 THR A 67 -1 O HIS A 66 N ALA A 34
SHEET 1 C 7 VAL A 83 PHE A 84 0
SHEET 2 C 7 LEU B 99 ARG B 101 1 O ARG B 101 N PHE A 84
SHEET 3 C 7 VAL B 110 LEU B 116 -1 O LEU B 114 N VAL B 100
SHEET 4 C 7 GLY B 361 VAL B 367 1 O VAL B 365 N TRP B 113
SHEET 5 C 7 LEU B 253 GLY B 258 1 N ARG B 254 O ASP B 362
SHEET 6 C 7 ARG B 281 PRO B 287 1 O VAL B 283 N VAL B 256
SHEET 7 C 7 THR B 314 VAL B 318 1 O THR B 314 N LEU B 284
SHEET 1 D 7 THR A 314 VAL A 318 0
SHEET 2 D 7 ARG A 281 PRO A 287 1 N LEU A 284 O THR A 314
SHEET 3 D 7 LEU A 253 GLY A 258 1 N VAL A 256 O VAL A 283
SHEET 4 D 7 GLY A 361 VAL A 367 1 O VAL A 364 N ALA A 257
SHEET 5 D 7 VAL A 110 LEU A 116 1 N TRP A 113 O VAL A 365
SHEET 6 D 7 LEU A 99 ARG A 101 -1 N VAL A 100 O LEU A 114
SHEET 7 D 7 VAL B 83 PHE B 84 1 O PHE B 84 N LEU A 99
SHEET 1 E 4 GLN A 193 ASP A 197 0
SHEET 2 E 4 ARG A 170 PRO A 176 1 N VAL A 173 O ILE A 195
SHEET 3 E 4 LEU A 147 ALA A 151 1 N ASP A 150 O TYR A 174
SHEET 4 E 4 VAL A 220 HIS A 221 1 O VAL A 220 N ALA A 149
SHEET 1 F 2 LEU B 3 ASP B 5 0
SHEET 2 F 2 ARG B 57 PRO B 59 -1 O ILE B 58 N ALA B 4
SHEET 1 G 2 GLU B 33 ARG B 35 0
SHEET 2 G 2 SER B 65 THR B 67 -1 O HIS B 66 N ALA B 34
SHEET 1 H 4 GLN B 193 ASP B 197 0
SHEET 2 H 4 ARG B 170 PRO B 176 1 N VAL B 173 O ILE B 195
SHEET 3 H 4 LEU B 147 ALA B 151 1 N VAL B 148 O ARG B 170
SHEET 4 H 4 VAL B 220 HIS B 221 1 O VAL B 220 N LEU B 147
SSBOND 1 CYS A 36 CYS A 64 1555 1555 2.04
SSBOND 2 CYS B 36 CYS B 64 1555 1555 2.04
LINK NZ LYS A 127 C4A PLP A 400 1555 1555 1.27
LINK NZ LYS B 127 C4A PLP B 400 1555 1555 1.27
CISPEP 1 LYS A 95 PRO A 96 0 -1.02
CISPEP 2 LYS B 95 PRO B 96 0 1.22
SITE 1 AC1 7 THR A 152 SER A 153 THR A 203 GLN A 224
SITE 2 AC1 7 PHE A 225 HOH A1417 HOH A1470
SITE 1 AC2 6 LYS B 127 THR B 152 SER B 153 GLN B 224
SITE 2 AC2 6 HOH B2413 HOH B2519
SITE 1 AC3 16 LYS A 127 ASN A 155 SER A 259 GLY A 261
SITE 2 AC3 16 THR A 262 SER A 263 GLY A 264 HIS A 265
SITE 3 AC3 16 GLY A 295 ILE A 296 SER A 341 PRO A 368
SITE 4 AC3 16 ASP A 369 HOH A1402 HOH A1412 HOH A1415
SITE 1 AC4 16 LYS B 127 ASN B 155 SER B 259 LEU B 260
SITE 2 AC4 16 GLY B 261 THR B 262 SER B 263 GLY B 264
SITE 3 AC4 16 HIS B 265 ILE B 296 SER B 341 PRO B 368
SITE 4 AC4 16 ASP B 369 HOH B2402 HOH B2407 HOH B2409
CRYST1 74.874 74.874 275.908 90.00 90.00 90.00 P 43 21 2 16
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 0.013356 0.000000 0.000000 0.00000
SCALE2 0.000000 0.013356 0.000000 0.00000
SCALE3 0.000000 0.000000 0.003624 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
