HEADER LYASE 19-OCT-99 1D7R
TITLE CRYSTAL STRUCTURE OF THE COMPLEX OF 2,2-DIALKYLGLYCINE DECARBOXYLASE
TITLE 2 WITH 5PA
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PROTEIN (2,2-DIALKYLGLYCINE DECARBOXYLASE (PYRUVATE));
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: DGD;
COMPND 5 EC: 4.1.1.64;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: BURKHOLDERIA CEPACIA;
SOURCE 3 ORGANISM_TAXID: 292;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 6 EXPRESSION_SYSTEM_STRAIN: TY103;
SOURCE 7 EXPRESSION_SYSTEM_PLASMID: PKDHE19
KEYWDS ENZYME COMPLEXES, CATALYTIC MECHANISM, DECARBOXYLATION INHIBITOR,
KEYWDS 2 LYASE
EXPDTA X-RAY DIFFRACTION
AUTHOR V.N.MALASHKEVICH,M.D.TONEY,P.STROP,J.KELLER,J.N.JANSONIUS
REVDAT 5 09-AUG-23 1D7R 1 REMARK LINK
REVDAT 4 24-FEB-09 1D7R 1 VERSN
REVDAT 3 01-APR-03 1D7R 1 JRNL
REVDAT 2 27-DEC-00 1D7R 1 REMARK
REVDAT 1 19-NOV-99 1D7R 0
JRNL AUTH V.N.MALASHKEVICH,P.STROP,J.W.KELLER,J.N.JANSONIUS,M.D.TONEY
JRNL TITL CRYSTAL STRUCTURES OF DIALKYLGLYCINE DECARBOXYLASE INHIBITOR
JRNL TITL 2 COMPLEXES.
JRNL REF J.MOL.BIOL. V. 294 193 1999
JRNL REFN ISSN 0022-2836
JRNL PMID 10556038
JRNL DOI 10.1006/JMBI.1999.3254
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH M.D.TONEY,J.W.KELLER,R.A.PAUPTIT,J.JAEGER,M.K.WISE,U.SAUDER,
REMARK 1 AUTH 2 J.N.JANSONIUS
REMARK 1 TITL CRYSTALLIZATION AND PRELIMINARY X-RAY DIFFRACTION STUDIES OF
REMARK 1 TITL 2 DIALKYLGLYCINE DECARBOXYLASE, A DECARBOXYLATING TRANSAMINASE
REMARK 1 REF J.MOL.BIOL. V. 222 873 1991
REMARK 1 REFN ISSN 0022-2836
REMARK 1 REFERENCE 2
REMARK 1 AUTH J.W.KELLER,K.B.BAURICK,G.C.RUTT,M.V.O'MALLEY,N.L.SONAFRANK,
REMARK 1 AUTH 2 R.A.REYNOLDS,L.O.EBBESSON,F.F.VAJDOS
REMARK 1 TITL PSEUDOMONAS CEPACIA 2,2-DIALKYLGLYCINE DECARBOXYLASE.
REMARK 1 TITL 2 SEQUENCE AND EXPRESSION IN ESCHERICHIA COLI OF STRUCTURAL
REMARK 1 TITL 3 AND REPRESSOR GENES
REMARK 1 REF J.BIOL.CHEM. V. 265 5531 1990
REMARK 1 REFN ISSN 0021-9258
REMARK 2
REMARK 2 RESOLUTION. 2.00 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : TNT
REMARK 3 AUTHORS : TRONRUD,TEN EYCK,MATTHEWS
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.00
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 10.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 2.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 96.6
REMARK 3 NUMBER OF REFLECTIONS : 40564
REMARK 3
REMARK 3 USING DATA ABOVE SIGMA CUTOFF.
REMARK 3 CROSS-VALIDATION METHOD : NULL
REMARK 3 FREE R VALUE TEST SET SELECTION : NULL
REMARK 3 R VALUE (WORKING + TEST SET) : NULL
REMARK 3 R VALUE (WORKING SET) : 0.215
REMARK 3 FREE R VALUE : NULL
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : NULL
REMARK 3
REMARK 3 USING ALL DATA, NO SIGMA CUTOFF.
REMARK 3 R VALUE (WORKING + TEST SET, NO CUTOFF) : NULL
REMARK 3 R VALUE (WORKING SET, NO CUTOFF) : NULL
REMARK 3 FREE R VALUE (NO CUTOFF) : NULL
REMARK 3 FREE R VALUE TEST SET SIZE (%, NO CUTOFF) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT (NO CUTOFF) : NULL
REMARK 3 TOTAL NUMBER OF REFLECTIONS (NO CUTOFF) : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 3246
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 24
REMARK 3 SOLVENT ATOMS : 130
REMARK 3
REMARK 3 WILSON B VALUE (FROM FCALC, A**2) : 25.830
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES. RMS WEIGHT COUNT
REMARK 3 BOND LENGTHS (A) : 0.011 ; NULL ; NULL
REMARK 3 BOND ANGLES (DEGREES) : 1.540 ; NULL ; NULL
REMARK 3 TORSION ANGLES (DEGREES) : NULL ; NULL ; NULL
REMARK 3 PSEUDOROTATION ANGLES (DEGREES) : NULL ; NULL ; NULL
REMARK 3 TRIGONAL CARBON PLANES (A) : NULL ; NULL ; NULL
REMARK 3 GENERAL PLANES (A) : NULL ; NULL ; NULL
REMARK 3 ISOTROPIC THERMAL FACTORS (A**2) : NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS (A) : NULL ; NULL ; NULL
REMARK 3
REMARK 3 INCORRECT CHIRAL-CENTERS (COUNT) : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : FLAT MODEL
REMARK 3 KSOL : 0.67
REMARK 3 BSOL : 155.3
REMARK 3
REMARK 3 RESTRAINT LIBRARIES.
REMARK 3 STEREOCHEMISTRY : NULL
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS : RESTRAINED
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1D7R COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 18-NOV-99.
REMARK 100 THE DEPOSITION ID IS D_1000009869.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 26-JUN-96
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.50
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : MPG/DESY, HAMBURG
REMARK 200 BEAMLINE : BW6
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.1
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 42301
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.000
REMARK 200 RESOLUTION RANGE LOW (A) : 35.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 96.6
REMARK 200 DATA REDUNDANCY : 3.900
REMARK 200 R MERGE (I) : 0.04900
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 9.8000
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) : 2.05
REMARK 200 COMPLETENESS FOR SHELL (%) : 96.4
REMARK 200 DATA REDUNDANCY IN SHELL : 3.80
REMARK 200 R MERGE FOR SHELL (I) : 0.31800
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: AMORE
REMARK 200 STARTING MODEL: 2DKB
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 61.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.12
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 15% PEG 4000, 0.15 M SODIUM PYRUVATE,
REMARK 280 0.03 M MES-KOH, PH 7.50, VAPOR DIFFUSION, HANGING DROP,
REMARK 280 TEMPERATURE 298K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 64 2 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+1/3
REMARK 290 3555 -X+Y,-X,Z+2/3
REMARK 290 4555 -X,-Y,Z
REMARK 290 5555 Y,-X+Y,Z+1/3
REMARK 290 6555 X-Y,X,Z+2/3
REMARK 290 7555 Y,X,-Z+1/3
REMARK 290 8555 X-Y,-Y,-Z
REMARK 290 9555 -X,-X+Y,-Z+2/3
REMARK 290 10555 -Y,-X,-Z+1/3
REMARK 290 11555 -X+Y,Y,-Z
REMARK 290 12555 X,X-Y,-Z+2/3
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 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 28.74000
REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 57.48000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 5 0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 5 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 28.74000
REMARK 290 SMTRY1 6 0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 6 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 57.48000
REMARK 290 SMTRY1 7 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 7 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 28.74000
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 9 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 9 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 9 0.000000 0.000000 -1.000000 57.48000
REMARK 290 SMTRY1 10 0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 10 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 10 0.000000 0.000000 -1.000000 28.74000
REMARK 290 SMTRY1 11 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 11 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 11 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 12 0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 12 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 12 0.000000 0.000000 -1.000000 57.48000
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: TETRAMERIC
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 BIOMT1 2 -1.000000 0.000000 0.000000 76.32500
REMARK 350 BIOMT2 2 0.000000 -1.000000 0.000000 132.19878
REMARK 350 BIOMT3 2 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 350 BIOMT2 3 0.866025 0.500000 0.000000 0.00000
REMARK 350 BIOMT3 3 0.000000 0.000000 -1.000000 28.74000
REMARK 350 BIOMT1 4 0.500000 -0.866025 0.000000 76.32500
REMARK 350 BIOMT2 4 -0.866025 -0.500000 0.000000 132.19878
REMARK 350 BIOMT3 4 0.000000 0.000000 -1.000000 28.74000
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 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 6 106.74 -44.62
REMARK 500 LYS A 33 122.96 -171.56
REMARK 500 GLN A 52 46.92 -97.75
REMARK 500 ALA A 55 67.35 -65.36
REMARK 500 LYS A 74 -51.90 -123.04
REMARK 500 LEU A 108 -159.22 -117.08
REMARK 500 TYR A 129 -15.75 -146.29
REMARK 500 ALA A 152 177.01 178.73
REMARK 500 ARG A 174 78.28 -118.32
REMARK 500 SER A 271 -74.95 -167.68
REMARK 500 PHE A 300 65.57 -159.02
REMARK 500 ARG A 369 29.02 -70.32
REMARK 500 ARG A 370 -34.73 -140.28
REMARK 500 ALA A 408 80.61 -155.92
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 K A 436 K
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 LEU A 78 O
REMARK 620 2 SER A 80 OG 97.4
REMARK 620 3 THR A 303 O 103.6 76.3
REMARK 620 4 VAL A 305 O 152.7 82.2 102.8
REMARK 620 5 ASP A 307 OD1 81.6 169.8 94.0 103.4
REMARK 620 6 HOH A 529 O 75.1 103.9 178.6 78.6 85.7
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA A 435 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ALA A 95 O
REMARK 620 2 THR A 98 O 88.8
REMARK 620 3 THR A 98 OG1 72.7 71.3
REMARK 620 4 PRO A 99 O 155.4 69.6 88.6
REMARK 620 5 LEU A 102 O 97.9 146.3 79.3 94.1
REMARK 620 N 1 2 3 4
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA A 435
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K A 436
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 5PA A 500
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1D7S RELATED DB: PDB
REMARK 900 RELATED ID: 1D7U RELATED DB: PDB
REMARK 900 RELATED ID: 1D7V RELATED DB: PDB
DBREF 1D7R A 1 433 UNP P16932 DGDA_BURCE 1 433
SEQRES 1 A 433 MET SER LEU ASN ASP ASP ALA THR PHE TRP ARG ASN ALA
SEQRES 2 A 433 ARG GLN HIS LEU VAL ARG TYR GLY GLY THR PHE GLU PRO
SEQRES 3 A 433 MET ILE ILE GLU ARG ALA LYS GLY SER PHE VAL TYR ASP
SEQRES 4 A 433 ALA ASP GLY ARG ALA ILE LEU ASP PHE THR SER GLY GLN
SEQRES 5 A 433 MET SER ALA VAL LEU GLY HIS CYS HIS PRO GLU ILE VAL
SEQRES 6 A 433 SER VAL ILE GLY GLU TYR ALA GLY LYS LEU ASP HIS LEU
SEQRES 7 A 433 PHE SER GLY MET LEU SER ARG PRO VAL VAL ASP LEU ALA
SEQRES 8 A 433 THR ARG LEU ALA ASN ILE THR PRO PRO GLY LEU ASP ARG
SEQRES 9 A 433 ALA LEU LEU LEU SER THR GLY ALA GLU SER ASN GLU ALA
SEQRES 10 A 433 ALA ILE ARG MET ALA LYS LEU VAL THR GLY LYS TYR GLU
SEQRES 11 A 433 ILE VAL GLY PHE ALA GLN SER TRP HIS GLY MET THR GLY
SEQRES 12 A 433 ALA ALA ALA SER ALA THR TYR SER ALA GLY ARG LYS GLY
SEQRES 13 A 433 VAL GLY PRO ALA ALA VAL GLY SER PHE ALA ILE PRO ALA
SEQRES 14 A 433 PRO PHE THR TYR ARG PRO ARG PHE GLU ARG ASN GLY ALA
SEQRES 15 A 433 TYR ASP TYR LEU ALA GLU LEU ASP TYR ALA PHE ASP LEU
SEQRES 16 A 433 ILE ASP ARG GLN SER SER GLY ASN LEU ALA ALA PHE ILE
SEQRES 17 A 433 ALA GLU PRO ILE LEU SER SER GLY GLY ILE ILE GLU LEU
SEQRES 18 A 433 PRO ASP GLY TYR MET ALA ALA LEU LYS ARG LYS CYS GLU
SEQRES 19 A 433 ALA ARG GLY MET LEU LEU ILE LEU ASP GLU ALA GLN THR
SEQRES 20 A 433 GLY VAL GLY ARG THR GLY THR MET PHE ALA CYS GLN ARG
SEQRES 21 A 433 ASP GLY VAL THR PRO ASP ILE LEU THR LEU SER LYS THR
SEQRES 22 A 433 LEU GLY ALA GLY LEU PRO LEU ALA ALA ILE VAL THR SER
SEQRES 23 A 433 ALA ALA ILE GLU GLU ARG ALA HIS GLU LEU GLY TYR LEU
SEQRES 24 A 433 PHE TYR THR THR HIS VAL SER ASP PRO LEU PRO ALA ALA
SEQRES 25 A 433 VAL GLY LEU ARG VAL LEU ASP VAL VAL GLN ARG ASP GLY
SEQRES 26 A 433 LEU VAL ALA ARG ALA ASN VAL MET GLY ASP ARG LEU ARG
SEQRES 27 A 433 ARG GLY LEU LEU ASP LEU MET GLU ARG PHE ASP CYS ILE
SEQRES 28 A 433 GLY ASP VAL ARG GLY ARG GLY LEU LEU LEU GLY VAL GLU
SEQRES 29 A 433 ILE VAL LYS ASP ARG ARG THR LYS GLU PRO ALA ASP GLY
SEQRES 30 A 433 LEU GLY ALA LYS ILE THR ARG GLU CYS MET ASN LEU GLY
SEQRES 31 A 433 LEU SER MET ASN ILE VAL GLN LEU PRO GLY MET GLY GLY
SEQRES 32 A 433 VAL PHE ARG ILE ALA PRO PRO LEU THR VAL SER GLU ASP
SEQRES 33 A 433 GLU ILE ASP LEU GLY LEU SER LEU LEU GLY GLN ALA ILE
SEQRES 34 A 433 GLU ARG ALA LEU
HET NA A 435 1
HET K A 436 1
HET 5PA A 500 22
HETNAM NA SODIUM ION
HETNAM K POTASSIUM ION
HETNAM 5PA N-[3-HYDROXY-2-METHYL-5-PHOSPHONOOXYMETHYL-PYRIDIN-4-Y-
HETNAM 2 5PA LMETHYL]-1-AMINO-CYCLOPROPANECARBOXYLIC ACID
HETSYN 5PA N-PYRIDOXYL-1-AMINO-CYCLOPROPANECARBOXYLIC ACID-5-
HETSYN 2 5PA MONOPHOSPHATE
FORMUL 2 NA NA 1+
FORMUL 3 K K 1+
FORMUL 4 5PA C12 H17 N2 O7 P
FORMUL 5 HOH *130(H2 O)
HELIX 1 1 ASP A 6 LEU A 17 1 12
HELIX 2 2 THR A 49 SER A 54 1 6
HELIX 3 3 HIS A 61 GLY A 73 1 13
HELIX 4 4 SER A 84 THR A 98 1 15
HELIX 5 5 THR A 110 GLY A 127 1 18
HELIX 6 6 THR A 142 ALA A 148 1 7
HELIX 7 7 ASP A 184 SER A 200 1 17
HELIX 8 8 GLY A 224 ARG A 236 1 13
HELIX 9 9 PHE A 256 GLY A 262 1 7
HELIX 10 10 SER A 271 ALA A 276 1 6
HELIX 11 11 SER A 286 LEU A 296 1 11
HELIX 12 12 ASP A 307 ASP A 324 1 18
HELIX 13 13 GLY A 325 PHE A 348 1 24
HELIX 14 14 GLY A 377 GLY A 390 1 14
HELIX 15 15 SER A 414 LEU A 433 1 20
SHEET 1 A 4 ILE A 29 LYS A 33 0
SHEET 2 A 4 PHE A 36 ASP A 39 -1 O PHE A 36 N LYS A 33
SHEET 3 A 4 ALA A 44 ASP A 47 -1 N ILE A 45 O VAL A 37
SHEET 4 A 4 LEU A 391 SER A 392 1 N SER A 392 O LEU A 46
SHEET 1 B 7 ARG A 104 LEU A 108 0
SHEET 2 B 7 ALA A 281 THR A 285 -1 O ALA A 281 N LEU A 108
SHEET 3 B 7 ILE A 267 LEU A 270 -1 N LEU A 268 O VAL A 284
SHEET 4 B 7 LEU A 239 ASP A 243 1 O LEU A 240 N ILE A 267
SHEET 5 B 7 LEU A 204 ALA A 209 1 O ALA A 205 N LEU A 239
SHEET 6 B 7 GLU A 130 PHE A 134 1 O GLU A 130 N ALA A 205
SHEET 7 B 7 SER A 164 ILE A 167 1 N PHE A 165 O ILE A 131
SHEET 1 C 2 GLU A 178 ARG A 179 0
SHEET 2 C 2 ALA A 182 TYR A 183 -1 O ALA A 182 N ARG A 179
SHEET 1 D 2 ILE A 212 LEU A 213 0
SHEET 2 D 2 ILE A 219 GLU A 220 -1 O ILE A 219 N LEU A 213
SHEET 1 E 4 ILE A 351 ARG A 357 0
SHEET 2 E 4 LEU A 360 ILE A 365 -1 O LEU A 360 N ARG A 357
SHEET 3 E 4 GLY A 403 ILE A 407 -1 O GLY A 403 N ILE A 365
SHEET 4 E 4 ILE A 395 VAL A 396 -1 O VAL A 396 N VAL A 404
LINK O LEU A 78 K K A 436 1555 1555 2.65
LINK OG SER A 80 K K A 436 1555 1555 2.66
LINK O ALA A 95 NA NA A 435 1555 1555 2.48
LINK O THR A 98 NA NA A 435 1555 1555 2.55
LINK OG1 THR A 98 NA NA A 435 1555 1555 2.89
LINK O PRO A 99 NA NA A 435 1555 1555 2.68
LINK O LEU A 102 NA NA A 435 1555 1555 2.73
LINK O THR A 303 K K A 436 1555 1555 2.87
LINK O VAL A 305 K K A 436 1555 1555 2.81
LINK OD1 ASP A 307 K K A 436 1555 1555 2.54
LINK K K A 436 O HOH A 529 1555 1555 2.86
SITE 1 AC1 4 ALA A 95 THR A 98 PRO A 99 LEU A 102
SITE 1 AC2 6 LEU A 78 SER A 80 THR A 303 VAL A 305
SITE 2 AC2 6 ASP A 307 HOH A 529
SITE 1 AC3 20 GLN A 52 GLY A 111 ALA A 112 TRP A 138
SITE 2 AC3 20 HIS A 139 GLU A 210 SER A 215 ASP A 243
SITE 3 AC3 20 ALA A 245 GLN A 246 LYS A 272 TYR A 301
SITE 4 AC3 20 THR A 302 THR A 303 ARG A 406 HOH A 504
SITE 5 AC3 20 HOH A 511 HOH A 513 HOH A 602 HOH A 605
CRYST1 152.650 152.650 86.220 90.00 90.00 120.00 P 64 2 2 12
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 0.006551 0.003782 0.000000 0.00000
SCALE2 0.000000 0.007564 0.000000 0.00000
SCALE3 0.000000 0.000000 0.011598 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
