HEADER OXIDOREDUCTASE 23-JUN-03 1PTM
TITLE CRYSTAL STRUCTURE OF E.COLI PDXA
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: 4-HYDROXYTHREONINE-4-PHOSPHATE DEHYDROGENASE;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: 4- PHOSPHOHYDROXY, -L-THREONINE DEHYDROGENASE;
COMPND 5 EC: 1.1.1.262;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 3 ORGANISM_TAXID: 562;
SOURCE 4 GENE: PDXA OR B0052;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: DL41;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PFO4
KEYWDS CRYSTAL STRUCRURE, PDXA, 4-HYDROXYTHREONINE-4-PHOSPHATE
KEYWDS 2 DEHYDROGENASE, PYRIDOXAL 5'-PHOSPHATE BIOSYNTHESIS, PLP, MONTREAL-
KEYWDS 3 KINGSTON BACTERIAL STRUCTURAL GENOMICS INITIATIVE, BSGI, STRUCTURAL
KEYWDS 4 GENOMICS, OXIDOREDUCTASE
EXPDTA X-RAY DIFFRACTION
AUTHOR J.SIVARAMAN,Y.LI,J.BANKS,D.E.CANE,A.MATTE,M.CYGLER,MONTREAL-KINGSTON
AUTHOR 2 BACTERIAL STRUCTURAL GENOMICS INITIATIVE (BSGI)
REVDAT 3 11-OCT-17 1PTM 1 REMARK
REVDAT 2 24-FEB-09 1PTM 1 VERSN
REVDAT 1 04-NOV-03 1PTM 0
JRNL AUTH J.SIVARAMAN,Y.LI,J.BANKS,D.E.CANE,A.MATTE,M.CYGLER
JRNL TITL CRYSTAL STRUCTURE OF ESCHERICHIA COLI PDXA, AN ENZYME
JRNL TITL 2 INVOLVED IN THE PYRIDOXAL PHOSPHATE BIOSYNTHESIS PATHWAY
JRNL REF J.BIOL.CHEM. V. 278 43682 2003
JRNL REFN ISSN 0021-9258
JRNL PMID 12896974
JRNL DOI 10.1074/JBC.M306344200
REMARK 2
REMARK 2 RESOLUTION. 1.96 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) : 1.96
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 45.00
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) (%) : NULL
REMARK 3 NUMBER OF REFLECTIONS : 91148
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : NULL
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDAM
REMARK 3 R VALUE (WORKING SET) : 0.217
REMARK 3 FREE R VALUE : 0.267
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : 2646
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 : 4859
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 7
REMARK 3 SOLVENT ATOMS : 263
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) : 0.30
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) : 0.008
REMARK 3 BOND ANGLES (DEGREES) : NULL
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 1PTM COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 01-JUL-03.
REMARK 100 THE DEPOSITION ID IS D_1000019559.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 17-AUG-02
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : NSLS
REMARK 200 BEAMLINE : X8C
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.979322, 0.979289, 0.964092
REMARK 200 MONOCHROMATOR : SILICON
REMARK 200 OPTICS : NULL
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 : 348771
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.960
REMARK 200 RESOLUTION RANGE LOW (A) : 99.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.5
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.10000
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 11.1000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.96
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.03
REMARK 200 COMPLETENESS FOR SHELL (%) : 97.7
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
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 (%): 47.80
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.38
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: TRI HCL, PEG8K, NAOAC, MGCL2, NAKPO4,
REMARK 280 VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K, PH 8
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 37.73900
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 57.07850
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 39.61400
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 57.07850
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 37.73900
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 39.61400
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 3470 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 24710 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -97.0 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 MSE 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 GLN A 88 CG CD OE1 NE2
REMARK 470 GLU A 157 CG CD OE1 OE2
REMARK 470 HIS A 217 CG ND1 CD2 CE1 NE2
REMARK 470 PHE A 278 CB CG CD1 CD2 CE1 CE2 CZ
REMARK 470 LYS A 308 CG CD CE NZ
REMARK 470 LEU B 25 CG CD1 CD2
REMARK 470 GLU B 156 CG CD OE1 OE2
REMARK 470 GLU B 157 CG CD OE1 OE2
REMARK 470 GLU B 200 CG CD OE1 OE2
REMARK 470 PHE B 278 CB CG CD1 CD2 CE1 CE2 CZ
REMARK 470 ARG B 280 CB CG CD NE CZ NH1 NH2
REMARK 470 GLU B 302 CG CD OE1 OE2
REMARK 470 ARG B 306 CB CG CD NE CZ NH1 NH2
REMARK 470 LYS B 308 CG CD CE NZ
REMARK 470 ALA B 309 CB
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 OD1 ASN A 319 OD1 ASN B 110 4555 2.08
REMARK 500
REMARK 500 REMARK: NULL
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 GLY A 279 N - CA - C ANGL. DEV. = -15.9 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 62 31.31 -97.95
REMARK 500 THR A 155 -156.83 -123.52
REMARK 500 GLU A 157 -26.80 80.66
REMARK 500 THR A 165 -104.20 -122.02
REMARK 500 GLU A 214 64.40 36.12
REMARK 500 THR A 225 -55.35 -122.68
REMARK 500 GLN A 276 -9.45 178.46
REMARK 500 PHE A 278 -74.39 -43.43
REMARK 500 ARG A 280 -14.34 55.41
REMARK 500 ALA A 300 58.48 37.96
REMARK 500 GLN B 27 0.91 -67.52
REMARK 500 PHE B 133 112.44 -167.75
REMARK 500 THR B 155 -152.53 -127.03
REMARK 500 THR B 165 -104.50 -115.14
REMARK 500 GLU B 214 74.78 36.89
REMARK 500 THR B 225 -59.69 -129.05
REMARK 500 TYR B 254 -65.23 -109.88
REMARK 500 PHE B 278 -116.21 102.16
REMARK 500 ALA B 300 57.84 35.35
REMARK 500 ALA B 309 -83.80 -44.30
REMARK 500 ASP B 310 87.69 103.86
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 ZN A 330 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 166 NE2
REMARK 620 2 HOH B 480 O 170.6
REMARK 620 3 HOH A 452 O 91.5 81.1
REMARK 620 4 HIS B 211 NE2 93.1 92.6 88.6
REMARK 620 5 HOH A 594 O 97.1 75.8 78.8 163.9
REMARK 620 6 HIS A 266 NE2 102.1 85.1 166.2 93.0 97.0
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN B 331 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS B 266 NE2
REMARK 620 2 HOH A 588 O 85.5
REMARK 620 3 HOH B 590 O 95.5 81.5
REMARK 620 4 HIS A 211 NE2 100.0 88.9 161.0
REMARK 620 5 HOH A 616 O 166.7 82.8 76.5 86.1
REMARK 620 6 HIS B 166 NE2 100.3 173.6 95.2 92.6 91.2
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 ZN A 330
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN B 331
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 A 332
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1PS6 RELATED DB: PDB
REMARK 900 PDXA COMPLEXED WITH HTP
REMARK 900 RELATED ID: 1PS7 RELATED DB: PDB
REMARK 900 PDXA SECOND CRYSTAL FORM
REMARK 900 RELATED ID: PDXA_ECOLI RELATED DB: TARGETDB
DBREF 1PTM A 1 329 UNP P19624 PDXA_ECOLI 1 329
DBREF 1PTM B 1 329 UNP P19624 PDXA_ECOLI 1 329
SEQADV 1PTM MSE A 1 UNP P19624 MET 1 MODIFIED RESIDUE
SEQADV 1PTM MSE A 49 UNP P19624 MET 49 MODIFIED RESIDUE
SEQADV 1PTM MSE A 151 UNP P19624 MET 151 MODIFIED RESIDUE
SEQADV 1PTM MSE A 152 UNP P19624 MET 152 MODIFIED RESIDUE
SEQADV 1PTM MSE A 218 UNP P19624 MET 218 MODIFIED RESIDUE
SEQADV 1PTM MSE A 238 UNP P19624 MET 238 MODIFIED RESIDUE
SEQADV 1PTM MSE A 264 UNP P19624 MET 264 MODIFIED RESIDUE
SEQADV 1PTM MSE A 324 UNP P19624 MET 324 MODIFIED RESIDUE
SEQADV 1PTM MSE B 1 UNP P19624 MET 1 MODIFIED RESIDUE
SEQADV 1PTM MSE B 49 UNP P19624 MET 49 MODIFIED RESIDUE
SEQADV 1PTM MSE B 151 UNP P19624 MET 151 MODIFIED RESIDUE
SEQADV 1PTM MSE B 152 UNP P19624 MET 152 MODIFIED RESIDUE
SEQADV 1PTM MSE B 218 UNP P19624 MET 218 MODIFIED RESIDUE
SEQADV 1PTM MSE B 238 UNP P19624 MET 238 MODIFIED RESIDUE
SEQADV 1PTM MSE B 264 UNP P19624 MET 264 MODIFIED RESIDUE
SEQADV 1PTM MSE B 324 UNP P19624 MET 324 MODIFIED RESIDUE
SEQRES 1 A 329 MSE VAL LYS THR GLN ARG VAL VAL ILE THR PRO GLY GLU
SEQRES 2 A 329 PRO ALA GLY ILE GLY PRO ASP LEU VAL VAL GLN LEU ALA
SEQRES 3 A 329 GLN ARG GLU TRP PRO VAL GLU LEU VAL VAL CYS ALA ASP
SEQRES 4 A 329 ALA THR LEU LEU THR ASN ARG ALA ALA MSE LEU GLY LEU
SEQRES 5 A 329 PRO LEU THR LEU ARG PRO TYR SER PRO ASN SER PRO ALA
SEQRES 6 A 329 GLN PRO GLN THR ALA GLY THR LEU THR LEU LEU PRO VAL
SEQRES 7 A 329 ALA LEU ARG ALA PRO VAL THR ALA GLY GLN LEU ALA VAL
SEQRES 8 A 329 GLU ASN GLY HIS TYR VAL VAL GLU THR LEU ALA ARG ALA
SEQRES 9 A 329 CYS ASP GLY CYS LEU ASN GLY GLU PHE ALA ALA LEU ILE
SEQRES 10 A 329 THR GLY PRO VAL HIS LYS GLY VAL ILE ASN ASP ALA GLY
SEQRES 11 A 329 ILE PRO PHE THR GLY HIS THR GLU PHE PHE GLU GLU ARG
SEQRES 12 A 329 SER GLN ALA LYS LYS VAL VAL MSE MSE LEU ALA THR GLU
SEQRES 13 A 329 GLU LEU ARG VAL ALA LEU ALA THR THR HIS LEU PRO LEU
SEQRES 14 A 329 ARG ASP ILE ALA ASP ALA ILE THR PRO ALA LEU LEU HIS
SEQRES 15 A 329 GLU VAL ILE ALA ILE LEU HIS HIS ASP LEU ARG THR LYS
SEQRES 16 A 329 PHE GLY ILE ALA GLU PRO ARG ILE LEU VAL CYS GLY LEU
SEQRES 17 A 329 ASN PRO HIS ALA GLY GLU GLY GLY HIS MSE GLY THR GLU
SEQRES 18 A 329 GLU ILE ASP THR ILE ILE PRO VAL LEU ASN GLU LEU ARG
SEQRES 19 A 329 ALA GLN GLY MSE LYS LEU ASN GLY PRO LEU PRO ALA ASP
SEQRES 20 A 329 THR LEU PHE GLN PRO LYS TYR LEU ASP ASN ALA ASP ALA
SEQRES 21 A 329 VAL LEU ALA MSE TYR HIS ASP GLN GLY LEU PRO VAL LEU
SEQRES 22 A 329 LYS TYR GLN GLY PHE GLY ARG GLY VAL ASN ILE THR LEU
SEQRES 23 A 329 GLY LEU PRO PHE ILE ARG THR SER VAL ASP HIS GLY THR
SEQRES 24 A 329 ALA LEU GLU LEU ALA GLY ARG GLY LYS ALA ASP VAL GLY
SEQRES 25 A 329 SER PHE ILE THR ALA LEU ASN LEU ALA ILE LYS MSE ILE
SEQRES 26 A 329 VAL ASN THR GLN
SEQRES 1 B 329 MSE VAL LYS THR GLN ARG VAL VAL ILE THR PRO GLY GLU
SEQRES 2 B 329 PRO ALA GLY ILE GLY PRO ASP LEU VAL VAL GLN LEU ALA
SEQRES 3 B 329 GLN ARG GLU TRP PRO VAL GLU LEU VAL VAL CYS ALA ASP
SEQRES 4 B 329 ALA THR LEU LEU THR ASN ARG ALA ALA MSE LEU GLY LEU
SEQRES 5 B 329 PRO LEU THR LEU ARG PRO TYR SER PRO ASN SER PRO ALA
SEQRES 6 B 329 GLN PRO GLN THR ALA GLY THR LEU THR LEU LEU PRO VAL
SEQRES 7 B 329 ALA LEU ARG ALA PRO VAL THR ALA GLY GLN LEU ALA VAL
SEQRES 8 B 329 GLU ASN GLY HIS TYR VAL VAL GLU THR LEU ALA ARG ALA
SEQRES 9 B 329 CYS ASP GLY CYS LEU ASN GLY GLU PHE ALA ALA LEU ILE
SEQRES 10 B 329 THR GLY PRO VAL HIS LYS GLY VAL ILE ASN ASP ALA GLY
SEQRES 11 B 329 ILE PRO PHE THR GLY HIS THR GLU PHE PHE GLU GLU ARG
SEQRES 12 B 329 SER GLN ALA LYS LYS VAL VAL MSE MSE LEU ALA THR GLU
SEQRES 13 B 329 GLU LEU ARG VAL ALA LEU ALA THR THR HIS LEU PRO LEU
SEQRES 14 B 329 ARG ASP ILE ALA ASP ALA ILE THR PRO ALA LEU LEU HIS
SEQRES 15 B 329 GLU VAL ILE ALA ILE LEU HIS HIS ASP LEU ARG THR LYS
SEQRES 16 B 329 PHE GLY ILE ALA GLU PRO ARG ILE LEU VAL CYS GLY LEU
SEQRES 17 B 329 ASN PRO HIS ALA GLY GLU GLY GLY HIS MSE GLY THR GLU
SEQRES 18 B 329 GLU ILE ASP THR ILE ILE PRO VAL LEU ASN GLU LEU ARG
SEQRES 19 B 329 ALA GLN GLY MSE LYS LEU ASN GLY PRO LEU PRO ALA ASP
SEQRES 20 B 329 THR LEU PHE GLN PRO LYS TYR LEU ASP ASN ALA ASP ALA
SEQRES 21 B 329 VAL LEU ALA MSE TYR HIS ASP GLN GLY LEU PRO VAL LEU
SEQRES 22 B 329 LYS TYR GLN GLY PHE GLY ARG GLY VAL ASN ILE THR LEU
SEQRES 23 B 329 GLY LEU PRO PHE ILE ARG THR SER VAL ASP HIS GLY THR
SEQRES 24 B 329 ALA LEU GLU LEU ALA GLY ARG GLY LYS ALA ASP VAL GLY
SEQRES 25 B 329 SER PHE ILE THR ALA LEU ASN LEU ALA ILE LYS MSE ILE
SEQRES 26 B 329 VAL ASN THR GLN
MODRES 1PTM MSE A 1 MET SELENOMETHIONINE
MODRES 1PTM MSE A 49 MET SELENOMETHIONINE
MODRES 1PTM MSE A 151 MET SELENOMETHIONINE
MODRES 1PTM MSE A 152 MET SELENOMETHIONINE
MODRES 1PTM MSE A 218 MET SELENOMETHIONINE
MODRES 1PTM MSE A 238 MET SELENOMETHIONINE
MODRES 1PTM MSE A 264 MET SELENOMETHIONINE
MODRES 1PTM MSE A 324 MET SELENOMETHIONINE
MODRES 1PTM MSE B 49 MET SELENOMETHIONINE
MODRES 1PTM MSE B 151 MET SELENOMETHIONINE
MODRES 1PTM MSE B 152 MET SELENOMETHIONINE
MODRES 1PTM MSE B 218 MET SELENOMETHIONINE
MODRES 1PTM MSE B 238 MET SELENOMETHIONINE
MODRES 1PTM MSE B 264 MET SELENOMETHIONINE
MODRES 1PTM MSE B 324 MET SELENOMETHIONINE
HET MSE A 1 8
HET MSE A 49 8
HET MSE A 151 8
HET MSE A 152 8
HET MSE A 218 8
HET MSE A 238 8
HET MSE A 264 8
HET MSE A 324 8
HET MSE B 49 8
HET MSE B 151 8
HET MSE B 152 8
HET MSE B 218 8
HET MSE B 238 8
HET MSE B 264 8
HET MSE B 324 8
HET ZN A 330 1
HET PO4 A 332 5
HET ZN B 331 1
HETNAM MSE SELENOMETHIONINE
HETNAM ZN ZINC ION
HETNAM PO4 PHOSPHATE ION
FORMUL 1 MSE 15(C5 H11 N O2 SE)
FORMUL 3 ZN 2(ZN 2+)
FORMUL 4 PO4 O4 P 3-
FORMUL 6 HOH *263(H2 O)
HELIX 1 1 ILE A 17 ALA A 26 1 10
HELIX 2 2 ASP A 39 LEU A 50 1 12
HELIX 3 3 GLU A 92 ASN A 110 1 19
HELIX 4 4 HIS A 122 ALA A 129 1 8
HELIX 5 5 GLY A 135 SER A 144 1 10
HELIX 6 6 PRO A 168 ARG A 170 5 3
HELIX 7 7 ASP A 171 ILE A 176 1 6
HELIX 8 8 THR A 177 LYS A 195 1 19
HELIX 9 9 ASN A 209 HIS A 217 5 9
HELIX 10 10 THR A 220 THR A 225 1 6
HELIX 11 11 THR A 225 GLN A 236 1 12
HELIX 12 12 PRO A 245 PHE A 250 1 6
HELIX 13 13 GLN A 251 ASP A 256 1 6
HELIX 14 14 TYR A 265 TYR A 275 1 11
HELIX 15 15 ALA A 300 ALA A 304 5 5
HELIX 16 16 VAL A 311 GLN A 329 1 19
HELIX 17 17 ILE B 17 ALA B 26 1 10
HELIX 18 18 ASP B 39 GLY B 51 1 13
HELIX 19 19 ALA B 90 GLU B 92 5 3
HELIX 20 20 ASN B 93 ASN B 110 1 18
HELIX 21 21 HIS B 122 ALA B 129 1 8
HELIX 22 22 GLY B 135 SER B 144 1 10
HELIX 23 23 PRO B 168 ARG B 170 5 3
HELIX 24 24 ASP B 171 ILE B 176 1 6
HELIX 25 25 THR B 177 LYS B 195 1 19
HELIX 26 26 ASN B 209 GLU B 214 5 6
HELIX 27 27 THR B 220 THR B 225 1 6
HELIX 28 28 THR B 225 ALA B 235 1 11
HELIX 29 29 PRO B 245 PHE B 250 1 6
HELIX 30 30 GLN B 251 ASP B 256 1 6
HELIX 31 31 TYR B 265 GLY B 277 1 13
HELIX 32 32 VAL B 311 ASN B 327 1 17
SHEET 1 A12 THR A 55 PRO A 58 0
SHEET 2 A12 THR A 72 PRO A 77 1 O LEU A 75 N ARG A 57
SHEET 3 A12 GLU A 33 ALA A 38 1 N VAL A 36 O THR A 74
SHEET 4 A12 ARG A 6 THR A 10 1 N ILE A 9 O VAL A 35
SHEET 5 A12 ALA A 115 THR A 118 1 O ALA A 115 N VAL A 8
SHEET 6 A12 ILE A 291 SER A 294 1 O ILE A 291 N LEU A 116
SHEET 7 A12 VAL A 282 LEU A 286 -1 N THR A 285 O ARG A 292
SHEET 8 A12 VAL A 150 ALA A 154 -1 N MSE A 152 O ILE A 284
SHEET 9 A12 ARG A 159 LEU A 162 -1 O VAL A 160 N LEU A 153
SHEET 10 A12 ALA A 260 ALA A 263 1 O VAL A 261 N ALA A 161
SHEET 11 A12 ARG A 202 CYS A 206 1 N LEU A 204 O LEU A 262
SHEET 12 A12 LYS A 239 LEU A 244 1 O LYS A 239 N ILE A 203
SHEET 1 B12 THR B 55 PRO B 58 0
SHEET 2 B12 THR B 72 PRO B 77 1 O LEU B 75 N ARG B 57
SHEET 3 B12 GLU B 33 ALA B 38 1 N VAL B 36 O THR B 74
SHEET 4 B12 ARG B 6 THR B 10 1 N VAL B 7 O VAL B 35
SHEET 5 B12 ALA B 115 THR B 118 1 O ALA B 115 N VAL B 8
SHEET 6 B12 ILE B 291 SER B 294 1 O ILE B 291 N LEU B 116
SHEET 7 B12 VAL B 282 LEU B 286 -1 N ASN B 283 O SER B 294
SHEET 8 B12 VAL B 150 ALA B 154 -1 N VAL B 150 O LEU B 286
SHEET 9 B12 ARG B 159 LEU B 162 -1 O VAL B 160 N LEU B 153
SHEET 10 B12 ALA B 260 ALA B 263 1 O VAL B 261 N ALA B 161
SHEET 11 B12 ARG B 202 CYS B 206 1 N LEU B 204 O LEU B 262
SHEET 12 B12 LYS B 239 LEU B 244 1 O ASN B 241 N ILE B 203
LINK C MSE A 1 N VAL A 2 1555 1555 1.33
LINK C ALA A 48 N MSE A 49 1555 1555 1.33
LINK C MSE A 49 N LEU A 50 1555 1555 1.33
LINK C VAL A 150 N MSE A 151 1555 1555 1.33
LINK C MSE A 151 N MSE A 152 1555 1555 1.32
LINK C MSE A 152 N LEU A 153 1555 1555 1.33
LINK C HIS A 217 N MSE A 218 1555 1555 1.33
LINK C MSE A 218 N GLY A 219 1555 1555 1.33
LINK C GLY A 237 N MSE A 238 1555 1555 1.33
LINK C MSE A 238 N LYS A 239 1555 1555 1.33
LINK C ALA A 263 N MSE A 264 1555 1555 1.33
LINK C MSE A 264 N TYR A 265 1555 1555 1.33
LINK C LYS A 323 N MSE A 324 1555 1555 1.33
LINK C MSE A 324 N ILE A 325 1555 1555 1.33
LINK ZN ZN A 330 NE2 HIS A 166 1555 1555 2.05
LINK ZN ZN A 330 O HOH B 480 1555 1555 2.04
LINK ZN ZN A 330 O HOH A 452 1555 1555 2.37
LINK ZN ZN A 330 NE2 HIS B 211 1555 1555 2.21
LINK ZN ZN A 330 O HOH A 594 1555 1555 2.24
LINK ZN ZN A 330 NE2 HIS A 266 1555 1555 2.27
LINK C ALA B 48 N MSE B 49 1555 1555 1.33
LINK C MSE B 49 N LEU B 50 1555 1555 1.33
LINK C VAL B 150 N MSE B 151 1555 1555 1.32
LINK C MSE B 151 N MSE B 152 1555 1555 1.32
LINK C MSE B 152 N LEU B 153 1555 1555 1.33
LINK C HIS B 217 N MSE B 218 1555 1555 1.33
LINK C MSE B 218 N GLY B 219 1555 1555 1.33
LINK C GLY B 237 N MSE B 238 1555 1555 1.33
LINK C MSE B 238 N LYS B 239 1555 1555 1.33
LINK C ALA B 263 N MSE B 264 1555 1555 1.33
LINK C MSE B 264 N TYR B 265 1555 1555 1.33
LINK C LYS B 323 N MSE B 324 1555 1555 1.33
LINK C MSE B 324 N ILE B 325 1555 1555 1.33
LINK ZN ZN B 331 NE2 HIS B 266 1555 1555 2.23
LINK ZN ZN B 331 O HOH A 588 1555 1555 2.11
LINK ZN ZN B 331 O HOH B 590 1555 1555 2.13
LINK ZN ZN B 331 NE2 HIS A 211 1555 1555 2.16
LINK ZN ZN B 331 O HOH A 616 1555 1555 2.31
LINK ZN ZN B 331 NE2 HIS B 166 1555 1555 2.14
CISPEP 1 GLY A 242 PRO A 243 0 0.50
SITE 1 AC1 6 HIS A 166 HIS A 266 HOH A 452 HOH A 594
SITE 2 AC1 6 HIS B 211 HOH B 480
SITE 1 AC2 6 HIS A 211 HOH A 588 HOH A 616 HIS B 166
SITE 2 AC2 6 HIS B 266 HOH B 590
SITE 1 AC3 6 GLY A 135 HIS A 136 THR A 137 ASN A 283
SITE 2 AC3 6 ARG A 292 HOH A 518
CRYST1 75.478 79.228 114.157 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 0.013249 0.000000 0.000000 0.00000
SCALE2 0.000000 0.012622 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008760 0.00000
HETATM 1 N MSE A 1 42.462 -22.467 -6.339 1.00 34.34 N
HETATM 2 CA MSE A 1 41.808 -21.424 -7.181 1.00 33.13 C
HETATM 3 C MSE A 1 40.300 -21.366 -6.970 1.00 32.51 C
HETATM 4 O MSE A 1 39.739 -22.068 -6.121 1.00 32.87 O
HETATM 5 CB MSE A 1 42.093 -21.674 -8.661 1.00 33.92 C
HETATM 6 CG MSE A 1 43.568 -21.705 -8.994 1.00 35.43 C
HETATM 7 SE MSE A 1 44.217 -23.390 -9.076 1.00 39.01 SE
HETATM 8 CE MSE A 1 44.088 -23.660 -10.843 1.00 38.74 C
(ATOM LINES ARE NOT SHOWN.)
END
