HEADER LYASE 16-JAN-14 4OGG
TITLE CRYSTAL STRUCTURE OF ARABIDOPSIS THALIANA DJ-1D WITH GLYOXYLATE AS
TITLE 2 SUBSTRATE ANALOG
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PROTEIN DJ-1 HOMOLOG D;
COMPND 3 CHAIN: A, B, C;
COMPND 4 SYNONYM: ATDJ1D, LACTOYLGLUTATHIONE LYASE DJ1D;
COMPND 5 EC: 4.2.1.130;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ARABIDOPSIS THALIANA;
SOURCE 3 ORGANISM_COMMON: MOUSE-EAR CRESS;
SOURCE 4 ORGANISM_TAXID: 3702;
SOURCE 5 GENE: DJ1D, AT3G02720, F13E7.34;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS GLYOXALASE, LYASE
EXPDTA X-RAY DIFFRACTION
AUTHOR D.CHOI,J.KIM,K.-S.RYU,C.PARK
REVDAT 4 20-SEP-23 4OGG 1 SEQADV LINK
REVDAT 3 24-DEC-14 4OGG 1 JRNL
REVDAT 2 22-OCT-14 4OGG 1 JRNL
REVDAT 1 15-OCT-14 4OGG 0
JRNL AUTH D.CHOI,J.KIM,S.HA,K.KWON,E.H.KIM,H.Y.LEE,K.S.RYU,C.PARK
JRNL TITL STEREOSPECIFIC MECHANISM OF DJ-1 GLYOXALASES INFERRED FROM
JRNL TITL 2 THEIR HEMITHIOACETAL-CONTAINING CRYSTAL STRUCTURES.
JRNL REF FEBS J. V. 281 5447 2014
JRNL REFN ISSN 1742-464X
JRNL PMID 25283443
JRNL DOI 10.1111/FEBS.13085
REMARK 2
REMARK 2 RESOLUTION. 1.60 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 : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.60
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 50.00
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) (%) : 95.9
REMARK 3 NUMBER OF REFLECTIONS : 136449
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : NULL
REMARK 3 FREE R VALUE TEST SET SELECTION : NULL
REMARK 3 R VALUE (WORKING SET) : 0.185
REMARK 3 FREE R VALUE : 0.212
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 9.600
REMARK 3 FREE R VALUE TEST SET COUNT : 13617
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 : 10
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 1.60
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.66
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 82.40
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 10438
REMARK 3 BIN R VALUE (WORKING SET) : 0.3026
REMARK 3 BIN FREE R VALUE : 0.3171
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 1149
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 : 8797
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 969
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 20.01
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 4.77100
REMARK 3 B22 (A**2) : 1.17400
REMARK 3 B33 (A**2) : -5.94500
REMARK 3 B12 (A**2) : 0.00000
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) : NULL
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) : 0.005
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) : 1.106 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 1.652 ; 2.000
REMARK 3 SIDE-CHAIN BOND (A**2) : 1.779 ; 2.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 2.573 ; 2.500
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 : CNS_TOPPAR:PROTEIN_REP.PARAM
REMARK 3 PARAMETER FILE 2 : CNS_TOPPAR:DNA -RNA_REP.PARAM
REMARK 3 PARAMETER FILE 3 : CNS_TOPPAR:WATER_REP.PARAM
REMARK 3 PARAMETER FILE 4 : CNS_TOPPAR:ION.PARAM
REMARK 3 PARAMETER FILE 5 : CNS_TOPPAR:CARBOHYDRATE.PARAM
REMARK 3 PARAMETER FILE 6 : NULL
REMARK 3 TOPOLOGY FILE 1 : NULL
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 4OGG COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 22-JAN-14.
REMARK 100 THE DEPOSITION ID IS D_1000084461.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 19-DEC-11
REMARK 200 TEMPERATURE (KELVIN) : NULL
REMARK 200 PH : 6.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : PHOTON FACTORY
REMARK 200 BEAMLINE : BL-17A
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : NULL
REMARK 200 MONOCHROMATOR : DOUBLE CRYSTAL SI(111)
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315R
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 139052
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.600
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 97.7
REMARK 200 DATA REDUNDANCY : 9.500
REMARK 200 R MERGE (I) : 0.08800
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 10.8000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.60
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.66
REMARK 200 COMPLETENESS FOR SHELL (%) : 93.2
REMARK 200 DATA REDUNDANCY IN SHELL : 6.50
REMARK 200 R MERGE FOR SHELL (I) : 0.40000
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: COOT
REMARK 200 STARTING MODEL: PDB ENTRY 1PDV
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 42.46
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.14
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M MES, 0.1 M SODIUM CHLORIDE, 16%
REMARK 280 PEG4000, PH 6.0, VAPOR DIFFUSION, HANGING DROP
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 41.84250
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 69.12100
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 46.46100
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 69.12100
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 41.84250
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 46.46100
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: TRIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 7220 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 37490 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -22.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C
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 HIS A 389
REMARK 465 HIS A 390
REMARK 465 HIS B 390
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 SER A 4 -37.18 71.85
REMARK 500 CYS A 55 37.19 -83.76
REMARK 500 CGV A 120 -107.38 58.97
REMARK 500 ALA A 139 -179.57 -179.20
REMARK 500 CGV A 313 -109.63 61.02
REMARK 500 ALA A 332 -174.87 -177.63
REMARK 500 SER B 4 -53.92 71.43
REMARK 500 CGV B 120 -109.23 58.74
REMARK 500 ALA B 139 -177.99 178.81
REMARK 500 CGV B 313 -111.78 61.40
REMARK 500 ALA B 332 -177.43 -175.22
REMARK 500 PHE C 54 75.91 -103.37
REMARK 500 CYS C 55 -79.77 -71.48
REMARK 500 CGV C 120 -108.70 58.38
REMARK 500 ALA C 139 -177.46 -179.67
REMARK 500 GLU C 233 -2.64 65.39
REMARK 500 CGV C 313 -112.27 61.60
REMARK 500 ALA C 332 -178.51 -177.22
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4OFW RELATED DB: PDB
REMARK 900 RELATED ID: 4OGF RELATED DB: PDB
DBREF 4OGG A 3 388 UNP Q9M8R4 DJ1D_ARATH 3 388
DBREF 4OGG B 3 388 UNP Q9M8R4 DJ1D_ARATH 3 388
DBREF 4OGG C 3 388 UNP Q9M8R4 DJ1D_ARATH 3 388
SEQADV 4OGG HIS A 389 UNP Q9M8R4 EXPRESSION TAG
SEQADV 4OGG HIS A 390 UNP Q9M8R4 EXPRESSION TAG
SEQADV 4OGG HIS B 389 UNP Q9M8R4 EXPRESSION TAG
SEQADV 4OGG HIS B 390 UNP Q9M8R4 EXPRESSION TAG
SEQADV 4OGG HIS C 389 UNP Q9M8R4 EXPRESSION TAG
SEQADV 4OGG HIS C 390 UNP Q9M8R4 EXPRESSION TAG
SEQRES 1 A 388 ASN SER ARG THR VAL LEU ILE LEU CYS GLY ASP TYR MET
SEQRES 2 A 388 GLU ASP TYR GLU VAL MET VAL PRO PHE GLN ALA LEU GLN
SEQRES 3 A 388 ALA PHE GLY ILE THR VAL HIS THR VAL CYS PRO GLY LYS
SEQRES 4 A 388 LYS ALA GLY ASP SER CYS PRO THR ALA VAL HIS ASP PHE
SEQRES 5 A 388 CYS GLY HIS GLN THR TYR PHE GLU SER ARG GLY HIS ASN
SEQRES 6 A 388 PHE THR LEU ASN ALA THR PHE ASP GLU VAL ASP LEU SER
SEQRES 7 A 388 LYS TYR ASP GLY LEU VAL ILE PRO GLY GLY ARG ALA PRO
SEQRES 8 A 388 GLU TYR LEU ALA LEU THR ALA SER VAL VAL GLU LEU VAL
SEQRES 9 A 388 LYS GLU PHE SER ARG SER GLY LYS PRO ILE ALA SER ILE
SEQRES 10 A 388 CGV HIS GLY GLN LEU ILE LEU ALA ALA ALA ASP THR VAL
SEQRES 11 A 388 ASN GLY ARG LYS CYS THR ALA TYR ALA THR VAL GLY PRO
SEQRES 12 A 388 SER LEU VAL ALA ALA GLY ALA LYS TRP VAL GLU PRO ILE
SEQRES 13 A 388 THR PRO ASP VAL CYS VAL VAL ASP GLY SER LEU ILE THR
SEQRES 14 A 388 ALA ALA THR TYR GLU GLY HIS PRO GLU PHE ILE GLN LEU
SEQRES 15 A 388 PHE VAL LYS ALA LEU GLY GLY LYS ILE THR GLY ALA ASN
SEQRES 16 A 388 LYS ARG ILE LEU PHE LEU CYS GLY ASP TYR MET GLU ASP
SEQRES 17 A 388 TYR GLU VAL LYS VAL PRO PHE GLN SER LEU GLN ALA LEU
SEQRES 18 A 388 GLY CYS GLN VAL ASP ALA VAL CYS PRO GLU LYS LYS ALA
SEQRES 19 A 388 GLY ASP ARG CYS PRO THR ALA ILE HIS ASP PHE GLU GLY
SEQRES 20 A 388 ASP GLN THR TYR SER GLU LYS PRO GLY HIS THR PHE ALA
SEQRES 21 A 388 LEU THR THR ASN PHE ASP ASP LEU VAL SER SER SER TYR
SEQRES 22 A 388 ASP ALA LEU VAL ILE PRO GLY GLY ARG ALA PRO GLU TYR
SEQRES 23 A 388 LEU ALA LEU ASN GLU HIS VAL LEU ASN ILE VAL LYS GLU
SEQRES 24 A 388 PHE MET ASN SER GLU LYS PRO VAL ALA SER ILE CGV HIS
SEQRES 25 A 388 GLY GLN GLN ILE LEU ALA ALA ALA GLY VAL LEU LYS GLY
SEQRES 26 A 388 ARG LYS CYS THR ALA TYR PRO ALA VAL LYS LEU ASN VAL
SEQRES 27 A 388 VAL LEU GLY GLY GLY THR TRP LEU GLU PRO ASP PRO ILE
SEQRES 28 A 388 ASP ARG CYS PHE THR ASP GLY ASN LEU VAL THR GLY ALA
SEQRES 29 A 388 ALA TRP PRO GLY HIS PRO GLU PHE VAL SER GLN LEU MET
SEQRES 30 A 388 ALA LEU LEU GLY ILE GLN VAL SER PHE HIS HIS
SEQRES 1 B 388 ASN SER ARG THR VAL LEU ILE LEU CYS GLY ASP TYR MET
SEQRES 2 B 388 GLU ASP TYR GLU VAL MET VAL PRO PHE GLN ALA LEU GLN
SEQRES 3 B 388 ALA PHE GLY ILE THR VAL HIS THR VAL CYS PRO GLY LYS
SEQRES 4 B 388 LYS ALA GLY ASP SER CYS PRO THR ALA VAL HIS ASP PHE
SEQRES 5 B 388 CYS GLY HIS GLN THR TYR PHE GLU SER ARG GLY HIS ASN
SEQRES 6 B 388 PHE THR LEU ASN ALA THR PHE ASP GLU VAL ASP LEU SER
SEQRES 7 B 388 LYS TYR ASP GLY LEU VAL ILE PRO GLY GLY ARG ALA PRO
SEQRES 8 B 388 GLU TYR LEU ALA LEU THR ALA SER VAL VAL GLU LEU VAL
SEQRES 9 B 388 LYS GLU PHE SER ARG SER GLY LYS PRO ILE ALA SER ILE
SEQRES 10 B 388 CGV HIS GLY GLN LEU ILE LEU ALA ALA ALA ASP THR VAL
SEQRES 11 B 388 ASN GLY ARG LYS CYS THR ALA TYR ALA THR VAL GLY PRO
SEQRES 12 B 388 SER LEU VAL ALA ALA GLY ALA LYS TRP VAL GLU PRO ILE
SEQRES 13 B 388 THR PRO ASP VAL CYS VAL VAL ASP GLY SER LEU ILE THR
SEQRES 14 B 388 ALA ALA THR TYR GLU GLY HIS PRO GLU PHE ILE GLN LEU
SEQRES 15 B 388 PHE VAL LYS ALA LEU GLY GLY LYS ILE THR GLY ALA ASN
SEQRES 16 B 388 LYS ARG ILE LEU PHE LEU CYS GLY ASP TYR MET GLU ASP
SEQRES 17 B 388 TYR GLU VAL LYS VAL PRO PHE GLN SER LEU GLN ALA LEU
SEQRES 18 B 388 GLY CYS GLN VAL ASP ALA VAL CYS PRO GLU LYS LYS ALA
SEQRES 19 B 388 GLY ASP ARG CYS PRO THR ALA ILE HIS ASP PHE GLU GLY
SEQRES 20 B 388 ASP GLN THR TYR SER GLU LYS PRO GLY HIS THR PHE ALA
SEQRES 21 B 388 LEU THR THR ASN PHE ASP ASP LEU VAL SER SER SER TYR
SEQRES 22 B 388 ASP ALA LEU VAL ILE PRO GLY GLY ARG ALA PRO GLU TYR
SEQRES 23 B 388 LEU ALA LEU ASN GLU HIS VAL LEU ASN ILE VAL LYS GLU
SEQRES 24 B 388 PHE MET ASN SER GLU LYS PRO VAL ALA SER ILE CGV HIS
SEQRES 25 B 388 GLY GLN GLN ILE LEU ALA ALA ALA GLY VAL LEU LYS GLY
SEQRES 26 B 388 ARG LYS CYS THR ALA TYR PRO ALA VAL LYS LEU ASN VAL
SEQRES 27 B 388 VAL LEU GLY GLY GLY THR TRP LEU GLU PRO ASP PRO ILE
SEQRES 28 B 388 ASP ARG CYS PHE THR ASP GLY ASN LEU VAL THR GLY ALA
SEQRES 29 B 388 ALA TRP PRO GLY HIS PRO GLU PHE VAL SER GLN LEU MET
SEQRES 30 B 388 ALA LEU LEU GLY ILE GLN VAL SER PHE HIS HIS
SEQRES 1 C 388 ASN SER ARG THR VAL LEU ILE LEU CYS GLY ASP TYR MET
SEQRES 2 C 388 GLU ASP TYR GLU VAL MET VAL PRO PHE GLN ALA LEU GLN
SEQRES 3 C 388 ALA PHE GLY ILE THR VAL HIS THR VAL CYS PRO GLY LYS
SEQRES 4 C 388 LYS ALA GLY ASP SER CYS PRO THR ALA VAL HIS ASP PHE
SEQRES 5 C 388 CYS GLY HIS GLN THR TYR PHE GLU SER ARG GLY HIS ASN
SEQRES 6 C 388 PHE THR LEU ASN ALA THR PHE ASP GLU VAL ASP LEU SER
SEQRES 7 C 388 LYS TYR ASP GLY LEU VAL ILE PRO GLY GLY ARG ALA PRO
SEQRES 8 C 388 GLU TYR LEU ALA LEU THR ALA SER VAL VAL GLU LEU VAL
SEQRES 9 C 388 LYS GLU PHE SER ARG SER GLY LYS PRO ILE ALA SER ILE
SEQRES 10 C 388 CGV HIS GLY GLN LEU ILE LEU ALA ALA ALA ASP THR VAL
SEQRES 11 C 388 ASN GLY ARG LYS CYS THR ALA TYR ALA THR VAL GLY PRO
SEQRES 12 C 388 SER LEU VAL ALA ALA GLY ALA LYS TRP VAL GLU PRO ILE
SEQRES 13 C 388 THR PRO ASP VAL CYS VAL VAL ASP GLY SER LEU ILE THR
SEQRES 14 C 388 ALA ALA THR TYR GLU GLY HIS PRO GLU PHE ILE GLN LEU
SEQRES 15 C 388 PHE VAL LYS ALA LEU GLY GLY LYS ILE THR GLY ALA ASN
SEQRES 16 C 388 LYS ARG ILE LEU PHE LEU CYS GLY ASP TYR MET GLU ASP
SEQRES 17 C 388 TYR GLU VAL LYS VAL PRO PHE GLN SER LEU GLN ALA LEU
SEQRES 18 C 388 GLY CYS GLN VAL ASP ALA VAL CYS PRO GLU LYS LYS ALA
SEQRES 19 C 388 GLY ASP ARG CYS PRO THR ALA ILE HIS ASP PHE GLU GLY
SEQRES 20 C 388 ASP GLN THR TYR SER GLU LYS PRO GLY HIS THR PHE ALA
SEQRES 21 C 388 LEU THR THR ASN PHE ASP ASP LEU VAL SER SER SER TYR
SEQRES 22 C 388 ASP ALA LEU VAL ILE PRO GLY GLY ARG ALA PRO GLU TYR
SEQRES 23 C 388 LEU ALA LEU ASN GLU HIS VAL LEU ASN ILE VAL LYS GLU
SEQRES 24 C 388 PHE MET ASN SER GLU LYS PRO VAL ALA SER ILE CGV HIS
SEQRES 25 C 388 GLY GLN GLN ILE LEU ALA ALA ALA GLY VAL LEU LYS GLY
SEQRES 26 C 388 ARG LYS CYS THR ALA TYR PRO ALA VAL LYS LEU ASN VAL
SEQRES 27 C 388 VAL LEU GLY GLY GLY THR TRP LEU GLU PRO ASP PRO ILE
SEQRES 28 C 388 ASP ARG CYS PHE THR ASP GLY ASN LEU VAL THR GLY ALA
SEQRES 29 C 388 ALA TRP PRO GLY HIS PRO GLU PHE VAL SER GLN LEU MET
SEQRES 30 C 388 ALA LEU LEU GLY ILE GLN VAL SER PHE HIS HIS
MODRES 4OGG CGV A 120 CYS
MODRES 4OGG CGV A 313 CYS
MODRES 4OGG CGV B 120 CYS
MODRES 4OGG CGV B 313 CYS
MODRES 4OGG CGV C 120 CYS
MODRES 4OGG CGV C 313 CYS
HET CGV A 120 11
HET CGV A 313 11
HET CGV B 120 11
HET CGV B 313 11
HET CGV C 120 11
HET CGV C 313 11
HETNAM CGV S-[(R)-CARBOXY(HYDROXY)METHYL]-L-CYSTEINE
FORMUL 1 CGV 6(C5 H9 N O5 S)
FORMUL 4 HOH *969(H2 O)
HELIX 1 1 ASP A 17 PHE A 30 1 14
HELIX 2 2 THR A 73 VAL A 77 5 5
HELIX 3 3 ASP A 78 TYR A 82 5 5
HELIX 4 4 ARG A 91 ALA A 97 1 7
HELIX 5 5 THR A 99 SER A 112 1 14
HELIX 6 6 GLY A 122 ALA A 129 1 8
HELIX 7 7 TYR A 140 THR A 142 5 3
HELIX 8 8 VAL A 143 ALA A 150 1 8
HELIX 9 9 THR A 174 GLU A 176 5 3
HELIX 10 10 GLY A 177 LEU A 189 1 13
HELIX 11 11 ASP A 210 GLY A 224 1 15
HELIX 12 12 VAL A 271 TYR A 275 5 5
HELIX 13 13 ARG A 284 ALA A 290 1 7
HELIX 14 14 ASN A 292 SER A 305 1 14
HELIX 15 15 GLY A 315 GLY A 323 1 9
HELIX 16 16 TYR A 333 ALA A 335 5 3
HELIX 17 17 VAL A 336 GLY A 343 1 8
HELIX 18 18 ALA A 367 PRO A 369 5 3
HELIX 19 19 GLY A 370 GLY A 383 1 14
HELIX 20 20 ASP B 17 PHE B 30 1 14
HELIX 21 21 THR B 73 VAL B 77 5 5
HELIX 22 22 ASP B 78 TYR B 82 5 5
HELIX 23 23 ARG B 91 ALA B 97 1 7
HELIX 24 24 THR B 99 GLY B 113 1 15
HELIX 25 25 GLY B 122 ALA B 129 1 8
HELIX 26 26 TYR B 140 THR B 142 5 3
HELIX 27 27 VAL B 143 ALA B 150 1 8
HELIX 28 28 THR B 174 GLU B 176 5 3
HELIX 29 29 GLY B 177 LEU B 189 1 13
HELIX 30 30 ASP B 210 GLY B 224 1 15
HELIX 31 31 ASN B 266 LEU B 270 5 5
HELIX 32 32 VAL B 271 TYR B 275 5 5
HELIX 33 33 ARG B 284 ALA B 290 1 7
HELIX 34 34 ASN B 292 GLU B 306 1 15
HELIX 35 35 GLY B 315 ALA B 322 1 8
HELIX 36 36 TYR B 333 ALA B 335 5 3
HELIX 37 37 VAL B 336 GLY B 344 1 9
HELIX 38 38 ALA B 367 PRO B 369 5 3
HELIX 39 39 GLY B 370 GLY B 383 1 14
HELIX 40 40 ASP C 17 PHE C 30 1 14
HELIX 41 41 THR C 73 VAL C 77 5 5
HELIX 42 42 ASP C 78 TYR C 82 5 5
HELIX 43 43 ARG C 91 ALA C 97 1 7
HELIX 44 44 THR C 99 GLY C 113 1 15
HELIX 45 45 GLY C 122 ALA C 129 1 8
HELIX 46 46 TYR C 140 THR C 142 5 3
HELIX 47 47 VAL C 143 ALA C 150 1 8
HELIX 48 48 THR C 174 GLU C 176 5 3
HELIX 49 49 GLY C 177 LEU C 189 1 13
HELIX 50 50 ASP C 210 GLY C 224 1 15
HELIX 51 51 VAL C 271 TYR C 275 5 5
HELIX 52 52 ARG C 284 ALA C 290 1 7
HELIX 53 53 ASN C 292 SER C 305 1 14
HELIX 54 54 GLY C 315 GLY C 323 1 9
HELIX 55 55 TYR C 333 ALA C 335 5 3
HELIX 56 56 VAL C 336 GLY C 343 1 8
HELIX 57 57 ALA C 367 PRO C 369 5 3
HELIX 58 58 GLY C 370 GLY C 383 1 14
SHEET 1 A 6 THR A 33 VAL A 37 0
SHEET 2 A 6 THR A 6 LEU A 10 1 N VAL A 7 O THR A 33
SHEET 3 A 6 GLY A 84 ILE A 87 1 O VAL A 86 N LEU A 8
SHEET 4 A 6 ILE A 116 ILE A 119 1 O ALA A 117 N LEU A 85
SHEET 5 A 6 LEU A 169 ALA A 172 1 O ILE A 170 N ILE A 116
SHEET 6 A 6 CYS A 163 ASP A 166 -1 N VAL A 164 O THR A 171
SHEET 1 B 3 MET A 15 GLU A 16 0
SHEET 2 B 3 THR A 49 ASP A 53 1 O ALA A 50 N MET A 15
SHEET 3 B 3 PHE A 61 ARG A 64 -1 O SER A 63 N VAL A 51
SHEET 1 C 2 SER A 46 CYS A 47 0
SHEET 2 C 2 PHE A 68 THR A 69 -1 O PHE A 68 N CYS A 47
SHEET 1 D 2 LYS A 136 CYS A 137 0
SHEET 2 D 2 LYS A 153 TRP A 154 1 O LYS A 153 N CYS A 137
SHEET 1 E 2 LYS A 192 THR A 194 0
SHEET 2 E 2 GLN A 385 SER A 387 -1 O SER A 387 N LYS A 192
SHEET 1 F 6 GLN A 226 VAL A 230 0
SHEET 2 F 6 ARG A 199 LEU A 203 1 N ILE A 200 O ASP A 228
SHEET 3 F 6 ALA A 277 ILE A 280 1 O VAL A 279 N LEU A 201
SHEET 4 F 6 VAL A 309 ILE A 312 1 O ALA A 310 N LEU A 278
SHEET 5 F 6 LEU A 362 GLY A 365 1 O VAL A 363 N VAL A 309
SHEET 6 F 6 PHE A 357 ASP A 359 -1 N PHE A 357 O THR A 364
SHEET 1 G 3 MET A 208 GLU A 209 0
SHEET 2 G 3 THR A 242 ASP A 246 1 O ALA A 243 N MET A 208
SHEET 3 G 3 SER A 254 PRO A 257 -1 O SER A 254 N ASP A 246
SHEET 1 H 2 ARG A 239 CYS A 240 0
SHEET 2 H 2 PHE A 261 ALA A 262 -1 O PHE A 261 N CYS A 240
SHEET 1 I 2 LYS A 329 CYS A 330 0
SHEET 2 I 2 THR A 346 TRP A 347 1 O THR A 346 N CYS A 330
SHEET 1 J 6 THR B 33 VAL B 37 0
SHEET 2 J 6 THR B 6 LEU B 10 1 N VAL B 7 O THR B 33
SHEET 3 J 6 GLY B 84 ILE B 87 1 O VAL B 86 N LEU B 10
SHEET 4 J 6 ILE B 116 ILE B 119 1 O ALA B 117 N LEU B 85
SHEET 5 J 6 LEU B 169 ALA B 172 1 O ILE B 170 N ILE B 116
SHEET 6 J 6 CYS B 163 ASP B 166 -1 N VAL B 164 O THR B 171
SHEET 1 K 3 MET B 15 GLU B 16 0
SHEET 2 K 3 THR B 49 ASP B 53 1 O ALA B 50 N MET B 15
SHEET 3 K 3 PHE B 61 ARG B 64 -1 O SER B 63 N VAL B 51
SHEET 1 L 2 SER B 46 CYS B 47 0
SHEET 2 L 2 PHE B 68 THR B 69 -1 O PHE B 68 N CYS B 47
SHEET 1 M 2 LYS B 136 CYS B 137 0
SHEET 2 M 2 LYS B 153 TRP B 154 1 O LYS B 153 N CYS B 137
SHEET 1 N 2 GLY B 191 THR B 194 0
SHEET 2 N 2 GLN B 385 PHE B 388 -1 O SER B 387 N LYS B 192
SHEET 1 O 6 GLN B 226 VAL B 230 0
SHEET 2 O 6 ARG B 199 LEU B 203 1 N ILE B 200 O GLN B 226
SHEET 3 O 6 ALA B 277 ILE B 280 1 O VAL B 279 N LEU B 201
SHEET 4 O 6 VAL B 309 ILE B 312 1 O ALA B 310 N LEU B 278
SHEET 5 O 6 LEU B 362 GLY B 365 1 O VAL B 363 N VAL B 309
SHEET 6 O 6 PHE B 357 ASP B 359 -1 N ASP B 359 O LEU B 362
SHEET 1 P 3 MET B 208 GLU B 209 0
SHEET 2 P 3 THR B 242 ASP B 246 1 O ALA B 243 N MET B 208
SHEET 3 P 3 SER B 254 PRO B 257 -1 O SER B 254 N ASP B 246
SHEET 1 Q 2 ARG B 239 CYS B 240 0
SHEET 2 Q 2 PHE B 261 ALA B 262 -1 O PHE B 261 N CYS B 240
SHEET 1 R 2 LYS B 329 CYS B 330 0
SHEET 2 R 2 THR B 346 TRP B 347 1 O THR B 346 N CYS B 330
SHEET 1 S 6 ILE C 32 VAL C 37 0
SHEET 2 S 6 ARG C 5 LEU C 10 1 N VAL C 7 O THR C 33
SHEET 3 S 6 GLY C 84 ILE C 87 1 O VAL C 86 N LEU C 10
SHEET 4 S 6 ILE C 116 ILE C 119 1 O ALA C 117 N LEU C 85
SHEET 5 S 6 LEU C 169 ALA C 172 1 O ILE C 170 N ILE C 116
SHEET 6 S 6 CYS C 163 ASP C 166 -1 N VAL C 164 O THR C 171
SHEET 1 T 3 MET C 15 GLU C 16 0
SHEET 2 T 3 THR C 49 ASP C 53 1 O ALA C 50 N MET C 15
SHEET 3 T 3 PHE C 61 ARG C 64 -1 O SER C 63 N VAL C 51
SHEET 1 U 2 SER C 46 CYS C 47 0
SHEET 2 U 2 PHE C 68 THR C 69 -1 O PHE C 68 N CYS C 47
SHEET 1 V 2 LYS C 136 CYS C 137 0
SHEET 2 V 2 LYS C 153 TRP C 154 1 O LYS C 153 N CYS C 137
SHEET 1 W 2 GLY C 191 THR C 194 0
SHEET 2 W 2 GLN C 385 PHE C 388 -1 O SER C 387 N LYS C 192
SHEET 1 X 6 GLN C 226 VAL C 230 0
SHEET 2 X 6 ARG C 199 LEU C 203 1 N ILE C 200 O GLN C 226
SHEET 3 X 6 ALA C 277 ILE C 280 1 O VAL C 279 N LEU C 201
SHEET 4 X 6 VAL C 309 ILE C 312 1 O ALA C 310 N LEU C 278
SHEET 5 X 6 LEU C 362 GLY C 365 1 O VAL C 363 N VAL C 309
SHEET 6 X 6 PHE C 357 ASP C 359 -1 N ASP C 359 O LEU C 362
SHEET 1 Y 3 MET C 208 GLU C 209 0
SHEET 2 Y 3 THR C 242 ASP C 246 1 O ALA C 243 N MET C 208
SHEET 3 Y 3 SER C 254 PRO C 257 -1 O LYS C 256 N ILE C 244
SHEET 1 Z 2 ARG C 239 CYS C 240 0
SHEET 2 Z 2 PHE C 261 ALA C 262 -1 O PHE C 261 N CYS C 240
SHEET 1 AA 2 LYS C 329 CYS C 330 0
SHEET 2 AA 2 THR C 346 TRP C 347 1 O THR C 346 N CYS C 330
LINK C ILE A 119 N CGV A 120 1555 1555 1.33
LINK C CGV A 120 N HIS A 121 1555 1555 1.33
LINK C ILE A 312 N CGV A 313 1555 1555 1.33
LINK C CGV A 313 N HIS A 314 1555 1555 1.33
LINK C ILE B 119 N CGV B 120 1555 1555 1.33
LINK C CGV B 120 N HIS B 121 1555 1555 1.34
LINK C ILE B 312 N CGV B 313 1555 1555 1.33
LINK C CGV B 313 N HIS B 314 1555 1555 1.33
LINK C ILE C 119 N CGV C 120 1555 1555 1.33
LINK C CGV C 120 N HIS C 121 1555 1555 1.34
LINK C ILE C 312 N CGV C 313 1555 1555 1.33
LINK C CGV C 313 N HIS C 314 1555 1555 1.34
CISPEP 1 ASP A 351 PRO A 352 0 0.23
CISPEP 2 ASP B 351 PRO B 352 0 0.10
CISPEP 3 ASP C 351 PRO C 352 0 0.00
CRYST1 83.685 92.922 138.242 90.00 90.00 90.00 P 21 21 21 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 0.011950 0.000000 0.000000 0.00000
SCALE2 0.000000 0.010762 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007234 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
