HEADER LYASE 16-AUG-01 1JS3
TITLE CRYSTAL STRUCTURE OF DOPA DECARBOXYLASE IN COMPLEX WITH THE INHIBITOR
TITLE 2 CARBIDOPA
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: DOPA DECARBOXYLASE;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: AROMATIC-L-AMINO-ACID DECARBOXYLASE; DDC;
COMPND 5 EC: 4.1.1.28;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: SUS SCROFA;
SOURCE 3 ORGANISM_COMMON: PIG;
SOURCE 4 ORGANISM_TAXID: 9823;
SOURCE 5 ORGAN: KIDNEY;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: JM109;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PKKDDC(DELTA)4
KEYWDS DOPA DECARBOXYLASE, CARBIDOPA, PARKINSON'S DISEASE, VITAMIN B6, LYASE
EXPDTA X-RAY DIFFRACTION
AUTHOR P.BURKHARD,P.DOMINICI,C.BORRI-VOLTATTORNI,J.N.JANSONIUS,
AUTHOR 2 V.N.MALASHKEVICH
REVDAT 5 07-FEB-24 1JS3 1 REMARK HETSYN LINK
REVDAT 4 13-JUL-11 1JS3 1 VERSN
REVDAT 3 24-FEB-09 1JS3 1 VERSN
REVDAT 2 30-SEP-03 1JS3 1 JRNL DBREF
REVDAT 1 26-OCT-01 1JS3 0
JRNL AUTH P.BURKHARD,P.DOMINICI,C.BORRI-VOLTATTORNI,J.N.JANSONIUS,
JRNL AUTH 2 V.N.MALASHKEVICH
JRNL TITL STRUCTURAL INSIGHT INTO PARKINSON'S DISEASE TREATMENT FROM
JRNL TITL 2 DRUG-INHIBITED DOPA DECARBOXYLASE.
JRNL REF NAT.STRUCT.BIOL. V. 8 963 2001
JRNL REFN ISSN 1072-8368
JRNL PMID 11685243
JRNL DOI 10.1038/NSB1101-963
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH V.N.MALASHKEVICH,P.BURKHARD,P.DOMINICI,P.S.MOORE,
REMARK 1 AUTH 2 C.BORRI-VOLTATTORNI,J.N.JANSONIUS
REMARK 1 TITL PRELIMINARY X-RAY ANALYSIS OF A NEW CRYSTAL FORM OF PIG
REMARK 1 TITL 2 KIDNEY DOPA DECARBOXYLASE
REMARK 1 REF ACTA CRYSTALLOGR.,SECT.D V. 55 568 1999
REMARK 1 REFN ISSN 0907-4449
REMARK 1 DOI 10.1107/S0907444998006283
REMARK 1 REFERENCE 2
REMARK 1 AUTH V.N.MALASHKEVICH,P.FILIPPONI,U.SAUDER,P.DOMINICI,
REMARK 1 AUTH 2 J.N.JANSONIUS,C.BORRI-VOLTATTORNI
REMARK 1 TITL CRYSTALLIZATION AND PRELIMINARY X-RAY ANALYSIS OF PIG KIDNEY
REMARK 1 TITL 2 DOPA DECARBOXYLASE
REMARK 1 REF J.MOL.BIOL. V. 224 1167 1992
REMARK 1 REFN ISSN 0022-2836
REMARK 2
REMARK 2 RESOLUTION. 2.25 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 1.0
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) : 2.25
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 19.61
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 2350530.700
REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0000
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 95.8
REMARK 3 NUMBER OF REFLECTIONS : 53582
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) : 0.144
REMARK 3 FREE R VALUE : 0.187
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 2722
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.004
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 6
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.25
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.39
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 84.40
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 7404
REMARK 3 BIN R VALUE (WORKING SET) : 0.1800
REMARK 3 BIN FREE R VALUE : 0.2150
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 5.30
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 418
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.011
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 7250
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 82
REMARK 3 SOLVENT ATOMS : 455
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 15.00
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 23.40
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.34000
REMARK 3 B22 (A**2) : -0.34000
REMARK 3 B33 (A**2) : 0.67000
REMARK 3 B12 (A**2) : 2.14000
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) : 0.18
REMARK 3 ESD FROM SIGMAA (A) : 0.17
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) : 0.24
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.22
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.009
REMARK 3 BOND ANGLES (DEGREES) : 1.500
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 22.20
REMARK 3 IMPROPER ANGLES (DEGREES) : 0.970
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : RESTRAINED
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 : FLAT MODEL
REMARK 3 KSOL : 0.33
REMARK 3 BSOL : 30.50
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 : PROTEIN_REP.PARAM
REMARK 3 PARAMETER FILE 2 : WATER_REP.PARAM
REMARK 3 PARAMETER FILE 3 : PARAM
REMARK 3 PARAMETER FILE 4 : PARAM
REMARK 3 PARAMETER FILE 5 : ION.PARAM
REMARK 3 PARAMETER FILE 6 : NULL
REMARK 3 TOPOLOGY FILE 1 : PROTEIN.TOP
REMARK 3 TOPOLOGY FILE 2 : NULL
REMARK 3 TOPOLOGY FILE 3 : NULL
REMARK 3 TOPOLOGY FILE 4 : NULL
REMARK 3 TOPOLOGY FILE 5 : NULL
REMARK 3 TOPOLOGY FILE 6 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1JS3 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 23-AUG-01.
REMARK 100 THE DEPOSITION ID IS D_1000014124.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 10-APR-93
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : LURE
REMARK 200 BEAMLINE : D41A
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9500
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 : 53582
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.250
REMARK 200 RESOLUTION RANGE LOW (A) : 19.610
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 95.8
REMARK 200 DATA REDUNDANCY : 2.900
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.05600
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 9.5000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.25
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.30
REMARK 200 COMPLETENESS FOR SHELL (%) : 70.7
REMARK 200 DATA REDUNDANCY IN SHELL : 1.70
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.19000
REMARK 200 <I/SIGMA(I)> FOR SHELL : 4.700
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MAD
REMARK 200 SOFTWARE USED: SHARP, DM
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 55.47
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.76
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG MME 5000, MES, AMMONIUM SULFATE AT
REMARK 280 PH 6.5, VAPOR DIFFUSION, HANGING DROP AT 298K, TEMPERATURE 298.0K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 62
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+2/3
REMARK 290 3555 -X+Y,-X,Z+1/3
REMARK 290 4555 -X,-Y,Z
REMARK 290 5555 Y,-X+Y,Z+2/3
REMARK 290 6555 X-Y,X,Z+1/3
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 57.85333
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 28.92667
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 57.85333
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 28.92667
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 300 REMARK: THE ASYMMETRIC UNIT CONTAINS ONE DIMER WHICH IS THE
REMARK 300 BIOLOGICALLY ACTIVE OLIGOMER
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: 14480 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 28730 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -146.0 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 LEU A 328
REMARK 465 ASP A 329
REMARK 465 PRO A 330
REMARK 465 VAL A 331
REMARK 465 TYR A 332
REMARK 465 LEU A 333
REMARK 465 LYS A 334
REMARK 465 HIS A 335
REMARK 465 SER A 336
REMARK 465 HIS A 337
REMARK 465 GLN A 338
REMARK 465 GLY A 339
REMARK 465 ALA A 477
REMARK 465 GLU A 478
REMARK 465 GLU A 479
REMARK 465 GLY A 480
REMARK 465 LYS A 481
REMARK 465 ALA A 482
REMARK 465 GLU A 483
REMARK 465 ILE A 484
REMARK 465 LYS A 485
REMARK 465 SER A 486
REMARK 465 LEU B 328
REMARK 465 ASP B 329
REMARK 465 PRO B 330
REMARK 465 VAL B 331
REMARK 465 TYR B 332
REMARK 465 LEU B 333
REMARK 465 LYS B 334
REMARK 465 HIS B 335
REMARK 465 SER B 336
REMARK 465 HIS B 337
REMARK 465 GLN B 338
REMARK 465 GLY B 339
REMARK 465 ALA B 477
REMARK 465 GLU B 478
REMARK 465 GLU B 479
REMARK 465 GLY B 480
REMARK 465 LYS B 481
REMARK 465 ALA B 482
REMARK 465 GLU B 483
REMARK 465 ILE B 484
REMARK 465 LYS B 485
REMARK 465 SER B 486
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 ARG A 431 CD - NE - CZ ANGL. DEV. = 9.0 DEGREES
REMARK 500 ARG A 431 NE - CZ - NH1 ANGL. DEV. = -6.5 DEGREES
REMARK 500 ARG A 431 NE - CZ - NH2 ANGL. DEV. = 5.9 DEGREES
REMARK 500 ARG B 431 CD - NE - CZ ANGL. DEV. = 11.1 DEGREES
REMARK 500 ARG B 431 NE - CZ - NH1 ANGL. DEV. = 7.7 DEGREES
REMARK 500 ARG B 431 NE - CZ - NH2 ANGL. DEV. = -7.9 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 TYR A 79 -116.30 49.39
REMARK 500 SER A 108 89.61 159.86
REMARK 500 LYS A 303 -70.75 -104.07
REMARK 500 ASN A 308 138.71 -36.19
REMARK 500 ASP A 310 55.59 111.12
REMARK 500 CYS A 311 89.42 -165.90
REMARK 500 ARG A 355 149.52 -172.61
REMARK 500 LEU A 406 -143.15 -121.27
REMARK 500 TYR B 79 -117.48 50.48
REMARK 500 SER B 108 90.63 160.19
REMARK 500 LYS B 303 -71.31 -105.47
REMARK 500 ASN B 308 137.69 -37.36
REMARK 500 ASP B 310 55.92 111.21
REMARK 500 CYS B 311 89.23 -165.33
REMARK 500 ARG B 355 149.03 -175.60
REMARK 500 LEU B 406 -140.96 -119.69
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 B 801
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 802
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 803
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 804
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PLP A 601
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PLP B 602
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 142 A 701
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 142 B 702
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1JS6 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF DOPA DECARBOXYLASE
DBREF 1JS3 A 1 486 UNP P80041 DDC_PIG 1 486
DBREF 1JS3 B 1 486 UNP P80041 DDC_PIG 1 486
SEQRES 1 A 486 MET ASN ALA SER ASP PHE ARG ARG ARG GLY LYS GLU MET
SEQRES 2 A 486 VAL ASP TYR MET ALA ASP TYR LEU GLU GLY ILE GLU GLY
SEQRES 3 A 486 ARG GLN VAL TYR PRO ASP VAL GLN PRO GLY TYR LEU ARG
SEQRES 4 A 486 PRO LEU ILE PRO ALA THR ALA PRO GLN GLU PRO ASP THR
SEQRES 5 A 486 PHE GLU ASP ILE LEU GLN ASP VAL GLU LYS ILE ILE MET
SEQRES 6 A 486 PRO GLY VAL THR HIS TRP HIS SER PRO TYR PHE PHE ALA
SEQRES 7 A 486 TYR PHE PRO THR ALA SER SER TYR PRO ALA MET LEU ALA
SEQRES 8 A 486 ASP MET LEU CYS GLY ALA ILE GLY CYS ILE GLY PHE SER
SEQRES 9 A 486 TRP ALA ALA SER PRO ALA CYS THR GLU LEU GLU THR VAL
SEQRES 10 A 486 MET MET ASP TRP LEU GLY LYS MET LEU GLN LEU PRO GLU
SEQRES 11 A 486 ALA PHE LEU ALA GLY GLU ALA GLY GLU GLY GLY GLY VAL
SEQRES 12 A 486 ILE GLN GLY SER ALA SER GLU ALA THR LEU VAL ALA LEU
SEQRES 13 A 486 LEU ALA ALA ARG THR LYS VAL VAL ARG ARG LEU GLN ALA
SEQRES 14 A 486 ALA SER PRO GLY LEU THR GLN GLY ALA VAL LEU GLU LYS
SEQRES 15 A 486 LEU VAL ALA TYR ALA SER ASP GLN ALA HIS SER SER VAL
SEQRES 16 A 486 GLU ARG ALA GLY LEU ILE GLY GLY VAL LYS LEU LYS ALA
SEQRES 17 A 486 ILE PRO SER ASP GLY LYS PHE ALA MET ARG ALA SER ALA
SEQRES 18 A 486 LEU GLN GLU ALA LEU GLU ARG ASP LYS ALA ALA GLY LEU
SEQRES 19 A 486 ILE PRO PHE PHE VAL VAL ALA THR LEU GLY THR THR SER
SEQRES 20 A 486 CYS CYS SER PHE ASP ASN LEU LEU GLU VAL GLY PRO ILE
SEQRES 21 A 486 CYS HIS GLU GLU ASP ILE TRP LEU HIS VAL ASP ALA ALA
SEQRES 22 A 486 TYR ALA GLY SER ALA PHE ILE CYS PRO GLU PHE ARG HIS
SEQRES 23 A 486 LEU LEU ASN GLY VAL GLU PHE ALA ASP SER PHE ASN PHE
SEQRES 24 A 486 ASN PRO HIS LYS TRP LEU LEU VAL ASN PHE ASP CYS SER
SEQRES 25 A 486 ALA MET TRP VAL LYS ARG ARG THR ASP LEU THR GLY ALA
SEQRES 26 A 486 PHE LYS LEU ASP PRO VAL TYR LEU LYS HIS SER HIS GLN
SEQRES 27 A 486 GLY SER GLY LEU ILE THR ASP TYR ARG HIS TRP GLN LEU
SEQRES 28 A 486 PRO LEU GLY ARG ARG PHE ARG SER LEU LYS MET TRP PHE
SEQRES 29 A 486 VAL PHE ARG MET TYR GLY VAL LYS GLY LEU GLN ALA TYR
SEQRES 30 A 486 ILE ARG LYS HIS VAL GLN LEU SER HIS GLU PHE GLU ALA
SEQRES 31 A 486 PHE VAL LEU GLN ASP PRO ARG PHE GLU VAL CYS ALA GLU
SEQRES 32 A 486 VAL THR LEU GLY LEU VAL CYS PHE ARG LEU LYS GLY SER
SEQRES 33 A 486 ASP GLY LEU ASN GLU ALA LEU LEU GLU ARG ILE ASN SER
SEQRES 34 A 486 ALA ARG LYS ILE HIS LEU VAL PRO CYS ARG LEU ARG GLY
SEQRES 35 A 486 GLN PHE VAL LEU ARG PHE ALA ILE CYS SER ARG LYS VAL
SEQRES 36 A 486 GLU SER GLY HIS VAL ARG LEU ALA TRP GLU HIS ILE ARG
SEQRES 37 A 486 GLY LEU ALA ALA GLU LEU LEU ALA ALA GLU GLU GLY LYS
SEQRES 38 A 486 ALA GLU ILE LYS SER
SEQRES 1 B 486 MET ASN ALA SER ASP PHE ARG ARG ARG GLY LYS GLU MET
SEQRES 2 B 486 VAL ASP TYR MET ALA ASP TYR LEU GLU GLY ILE GLU GLY
SEQRES 3 B 486 ARG GLN VAL TYR PRO ASP VAL GLN PRO GLY TYR LEU ARG
SEQRES 4 B 486 PRO LEU ILE PRO ALA THR ALA PRO GLN GLU PRO ASP THR
SEQRES 5 B 486 PHE GLU ASP ILE LEU GLN ASP VAL GLU LYS ILE ILE MET
SEQRES 6 B 486 PRO GLY VAL THR HIS TRP HIS SER PRO TYR PHE PHE ALA
SEQRES 7 B 486 TYR PHE PRO THR ALA SER SER TYR PRO ALA MET LEU ALA
SEQRES 8 B 486 ASP MET LEU CYS GLY ALA ILE GLY CYS ILE GLY PHE SER
SEQRES 9 B 486 TRP ALA ALA SER PRO ALA CYS THR GLU LEU GLU THR VAL
SEQRES 10 B 486 MET MET ASP TRP LEU GLY LYS MET LEU GLN LEU PRO GLU
SEQRES 11 B 486 ALA PHE LEU ALA GLY GLU ALA GLY GLU GLY GLY GLY VAL
SEQRES 12 B 486 ILE GLN GLY SER ALA SER GLU ALA THR LEU VAL ALA LEU
SEQRES 13 B 486 LEU ALA ALA ARG THR LYS VAL VAL ARG ARG LEU GLN ALA
SEQRES 14 B 486 ALA SER PRO GLY LEU THR GLN GLY ALA VAL LEU GLU LYS
SEQRES 15 B 486 LEU VAL ALA TYR ALA SER ASP GLN ALA HIS SER SER VAL
SEQRES 16 B 486 GLU ARG ALA GLY LEU ILE GLY GLY VAL LYS LEU LYS ALA
SEQRES 17 B 486 ILE PRO SER ASP GLY LYS PHE ALA MET ARG ALA SER ALA
SEQRES 18 B 486 LEU GLN GLU ALA LEU GLU ARG ASP LYS ALA ALA GLY LEU
SEQRES 19 B 486 ILE PRO PHE PHE VAL VAL ALA THR LEU GLY THR THR SER
SEQRES 20 B 486 CYS CYS SER PHE ASP ASN LEU LEU GLU VAL GLY PRO ILE
SEQRES 21 B 486 CYS HIS GLU GLU ASP ILE TRP LEU HIS VAL ASP ALA ALA
SEQRES 22 B 486 TYR ALA GLY SER ALA PHE ILE CYS PRO GLU PHE ARG HIS
SEQRES 23 B 486 LEU LEU ASN GLY VAL GLU PHE ALA ASP SER PHE ASN PHE
SEQRES 24 B 486 ASN PRO HIS LYS TRP LEU LEU VAL ASN PHE ASP CYS SER
SEQRES 25 B 486 ALA MET TRP VAL LYS ARG ARG THR ASP LEU THR GLY ALA
SEQRES 26 B 486 PHE LYS LEU ASP PRO VAL TYR LEU LYS HIS SER HIS GLN
SEQRES 27 B 486 GLY SER GLY LEU ILE THR ASP TYR ARG HIS TRP GLN LEU
SEQRES 28 B 486 PRO LEU GLY ARG ARG PHE ARG SER LEU LYS MET TRP PHE
SEQRES 29 B 486 VAL PHE ARG MET TYR GLY VAL LYS GLY LEU GLN ALA TYR
SEQRES 30 B 486 ILE ARG LYS HIS VAL GLN LEU SER HIS GLU PHE GLU ALA
SEQRES 31 B 486 PHE VAL LEU GLN ASP PRO ARG PHE GLU VAL CYS ALA GLU
SEQRES 32 B 486 VAL THR LEU GLY LEU VAL CYS PHE ARG LEU LYS GLY SER
SEQRES 33 B 486 ASP GLY LEU ASN GLU ALA LEU LEU GLU ARG ILE ASN SER
SEQRES 34 B 486 ALA ARG LYS ILE HIS LEU VAL PRO CYS ARG LEU ARG GLY
SEQRES 35 B 486 GLN PHE VAL LEU ARG PHE ALA ILE CYS SER ARG LYS VAL
SEQRES 36 B 486 GLU SER GLY HIS VAL ARG LEU ALA TRP GLU HIS ILE ARG
SEQRES 37 B 486 GLY LEU ALA ALA GLU LEU LEU ALA ALA GLU GLU GLY LYS
SEQRES 38 B 486 ALA GLU ILE LYS SER
HET SO4 A 802 5
HET SO4 A 803 5
HET PLP A 601 15
HET 142 A 701 16
HET SO4 B 801 5
HET SO4 B 804 5
HET PLP B 602 15
HET 142 B 702 16
HETNAM SO4 SULFATE ION
HETNAM PLP PYRIDOXAL-5'-PHOSPHATE
HETNAM 142 CARBIDOPA
HETSYN PLP VITAMIN B6 PHOSPHATE
HETSYN 142 KINSON; 3-(3,4-DIHYDROXY-PHENYL)-2-HYDRAZINO-2-METHYL-
HETSYN 2 142 PROPIONIC ACID
FORMUL 3 SO4 4(O4 S 2-)
FORMUL 5 PLP 2(C8 H10 N O6 P)
FORMUL 6 142 2(C10 H14 N2 O4)
FORMUL 11 HOH *455(H2 O)
HELIX 1 1 ASN A 2 GLY A 23 1 22
HELIX 2 2 ILE A 24 ARG A 27 5 4
HELIX 3 3 LEU A 38 ILE A 42 5 5
HELIX 4 4 THR A 52 ILE A 63 1 12
HELIX 5 5 ILE A 64 VAL A 68 5 5
HELIX 6 6 SER A 85 GLY A 99 1 15
HELIX 7 7 SER A 104 ALA A 107 5 4
HELIX 8 8 SER A 108 LEU A 126 1 19
HELIX 9 9 PRO A 129 LEU A 133 5 5
HELIX 10 10 SER A 147 SER A 171 1 25
HELIX 11 11 THR A 175 LYS A 182 1 8
HELIX 12 12 HIS A 192 GLY A 203 1 12
HELIX 13 13 ARG A 218 ALA A 232 1 15
HELIX 14 14 ASN A 253 GLU A 264 1 12
HELIX 15 15 TYR A 274 CYS A 281 5 8
HELIX 16 16 PHE A 284 ASN A 289 5 6
HELIX 17 17 GLY A 290 ALA A 294 5 5
HELIX 18 18 ASN A 300 LEU A 305 1 6
HELIX 19 19 ARG A 318 GLY A 324 1 7
HELIX 20 20 ALA A 325 LYS A 327 5 3
HELIX 21 21 ASP A 345 TRP A 349 5 5
HELIX 22 22 ARG A 358 ASP A 395 1 38
HELIX 23 23 SER A 416 ARG A 431 1 16
HELIX 24 24 GLU A 456 ALA A 476 1 21
HELIX 25 25 ASN B 2 GLY B 23 1 22
HELIX 26 26 ILE B 24 ARG B 27 5 4
HELIX 27 27 LEU B 38 ILE B 42 5 5
HELIX 28 28 THR B 52 ILE B 63 1 12
HELIX 29 29 ILE B 64 VAL B 68 5 5
HELIX 30 30 SER B 85 GLY B 99 1 15
HELIX 31 31 SER B 104 ALA B 107 5 4
HELIX 32 32 SER B 108 LEU B 126 1 19
HELIX 33 33 PRO B 129 LEU B 133 5 5
HELIX 34 34 SER B 147 SER B 171 1 25
HELIX 35 35 THR B 175 LYS B 182 1 8
HELIX 36 36 HIS B 192 GLY B 203 1 12
HELIX 37 37 ARG B 218 ALA B 232 1 15
HELIX 38 38 ASN B 253 GLU B 264 1 12
HELIX 39 39 TYR B 274 CYS B 281 5 8
HELIX 40 40 PHE B 284 ASN B 289 5 6
HELIX 41 41 GLY B 290 ALA B 294 5 5
HELIX 42 42 ASN B 300 LEU B 305 1 6
HELIX 43 43 ARG B 318 GLY B 324 1 7
HELIX 44 44 ALA B 325 LYS B 327 5 3
HELIX 45 45 ASP B 345 TRP B 349 5 5
HELIX 46 46 ARG B 358 ASP B 395 1 38
HELIX 47 47 SER B 416 ARG B 431 1 16
HELIX 48 48 GLU B 456 ALA B 476 1 21
SHEET 1 A 7 GLY A 141 GLN A 145 0
SHEET 2 A 7 SER A 312 VAL A 316 -1 O SER A 312 N GLN A 145
SHEET 3 A 7 SER A 296 PHE A 299 -1 N PHE A 299 O ALA A 313
SHEET 4 A 7 TRP A 267 ASP A 271 1 N VAL A 270 O SER A 296
SHEET 5 A 7 ILE A 235 THR A 242 1 N ALA A 241 O ASP A 271
SHEET 6 A 7 LEU A 183 SER A 188 1 N TYR A 186 O PHE A 238
SHEET 7 A 7 LYS A 205 ILE A 209 1 O LYS A 205 N ALA A 185
SHEET 1 B 4 PHE A 398 VAL A 400 0
SHEET 2 B 4 LEU A 408 LEU A 413 -1 O ARG A 412 N GLU A 399
SHEET 3 B 4 GLN A 443 ALA A 449 -1 O LEU A 446 N PHE A 411
SHEET 4 B 4 VAL A 436 LEU A 440 -1 N CYS A 438 O VAL A 445
SHEET 1 C 7 GLY B 141 GLN B 145 0
SHEET 2 C 7 SER B 312 VAL B 316 -1 O SER B 312 N GLN B 145
SHEET 3 C 7 SER B 296 PHE B 299 -1 N PHE B 299 O ALA B 313
SHEET 4 C 7 TRP B 267 ASP B 271 1 N VAL B 270 O SER B 296
SHEET 5 C 7 ILE B 235 THR B 242 1 N ALA B 241 O ASP B 271
SHEET 6 C 7 LEU B 183 SER B 188 1 N TYR B 186 O PHE B 238
SHEET 7 C 7 LYS B 205 ILE B 209 1 O LYS B 205 N ALA B 185
SHEET 1 D 4 PHE B 398 VAL B 400 0
SHEET 2 D 4 LEU B 408 LEU B 413 -1 O ARG B 412 N GLU B 399
SHEET 3 D 4 GLN B 443 ALA B 449 -1 O LEU B 446 N PHE B 411
SHEET 4 D 4 VAL B 436 LEU B 440 -1 N CYS B 438 O VAL B 445
LINK C4A PLP A 601 N 142 A 701 1555 1555 1.34
LINK C4A PLP B 602 N 142 B 702 1555 1555 1.34
SITE 1 AC1 5 ASN A 2 ALA A 3 TYR B 86 ARG B 453
SITE 2 AC1 5 LYS B 454
SITE 1 AC2 5 TYR A 86 ARG A 453 LYS A 454 ASN B 2
SITE 2 AC2 5 ALA B 3
SITE 1 AC3 3 ARG A 347 HIS A 348 HOH B 941
SITE 1 AC4 2 ARG B 347 HIS B 348
SITE 1 AC5 14 SER A 147 ALA A 148 SER A 149 HIS A 192
SITE 2 AC5 14 SER A 194 THR A 246 ASP A 271 ALA A 273
SITE 3 AC5 14 ASN A 300 HIS A 302 LYS A 303 142 A 701
SITE 4 AC5 14 HOH A 805 HOH A 908
SITE 1 AC6 14 SER B 147 ALA B 148 SER B 149 HIS B 192
SITE 2 AC6 14 SER B 194 THR B 246 ASP B 271 ALA B 273
SITE 3 AC6 14 ASN B 300 HIS B 302 LYS B 303 142 B 702
SITE 4 AC6 14 HOH B 959 HOH B 987
SITE 1 AC7 10 TYR A 79 PHE A 80 PRO A 81 THR A 82
SITE 2 AC7 10 HIS A 192 HIS A 302 LYS A 303 PLP A 601
SITE 3 AC7 10 HOH A1001 HOH A1003
SITE 1 AC8 10 TYR B 79 PHE B 80 PRO B 81 THR B 82
SITE 2 AC8 10 HIS B 192 THR B 246 HIS B 302 LYS B 303
SITE 3 AC8 10 PLP B 602 HOH B1022
CRYST1 154.360 154.360 86.780 90.00 90.00 120.00 P 62 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 0.006478 0.003740 0.000000 0.00000
SCALE2 0.000000 0.007481 0.000000 0.00000
SCALE3 0.000000 0.000000 0.011523 0.00000
(ATOM LINES ARE NOT SHOWN.)
END