HEADER CHAPERONE 09-JAN-08 3BWE
TITLE CRYSTAL STRUCTURE OF AGGREGATED FORM OF DJ1
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PROTEIN DJ-1;
COMPND 3 CHAIN: A, B, C, D, E, F, G;
COMPND 4 SYNONYM: ONCOGENE DJ1, PARKINSON DISEASE PROTEIN 7;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: PARK7;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS DJ-1, FILAMENTOUS AGGREGATES, CHAPERONE, CYTOPLASM, DISEASE MUTATION,
KEYWDS 2 NUCLEUS, ONCOGENE, OXIDATION, PARKINSON DISEASE, PHOSPHOPROTEIN,
KEYWDS 3 POLYMORPHISM, UBL CONJUGATION
EXPDTA X-RAY DIFFRACTION
AUTHOR S.S.CHA
REVDAT 5 15-NOV-23 3BWE 1 REMARK
REVDAT 4 01-NOV-23 3BWE 1 REMARK LINK
REVDAT 3 14-APR-09 3BWE 1 JRNL
REVDAT 2 24-FEB-09 3BWE 1 VERSN
REVDAT 1 14-OCT-08 3BWE 0
JRNL AUTH S.S.CHA,H.I.JUNG,H.JEON,Y.J.AN,I.K.KIM,S.YUN,H.J.AHN,
JRNL AUTH 2 K.C.CHUNG,S.H.LEE,P.G.SUH,S.O.KANG
JRNL TITL CRYSTAL STRUCTURE OF FILAMENTOUS AGGREGATES OF HUMAN DJ-1
JRNL TITL 2 FORMED IN AN INORGANIC PHOSPHATE-DEPENDENT MANNER.
JRNL REF J.BIOL.CHEM. V. 283 34069 2008
JRNL REFN ISSN 0021-9258
JRNL PMID 18922803
JRNL DOI 10.1074/JBC.M804243200
REMARK 2
REMARK 2 RESOLUTION. 2.40 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 1.1
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) : 2.40
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 19.99
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 58196.920
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 94.5
REMARK 3 NUMBER OF REFLECTIONS : 56652
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) : 0.232
REMARK 3 FREE R VALUE : 0.282
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 10.200
REMARK 3 FREE R VALUE TEST SET COUNT : 5760
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) : 2.40
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.55
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 93.30
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 8338
REMARK 3 BIN R VALUE (WORKING SET) : 0.3300
REMARK 3 BIN FREE R VALUE : 0.3560
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 10.20
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 951
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.012
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 9490
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 35
REMARK 3 SOLVENT ATOMS : 283
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) : -3.78000
REMARK 3 B22 (A**2) : 0.00000
REMARK 3 B33 (A**2) : 0.00000
REMARK 3 B12 (A**2) : 1.71000
REMARK 3 B13 (A**2) : 2.06000
REMARK 3 B23 (A**2) : 3.36000
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.32
REMARK 3 ESD FROM SIGMAA (A) : 0.41
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) : NULL
REMARK 3 ESD FROM C-V SIGMAA (A) : NULL
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.012
REMARK 3 BOND ANGLES (DEGREES) : 1.700
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 3BWE COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 11-JAN-08.
REMARK 100 THE DEPOSITION ID IS D_1000046039.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 04-NOV-04
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
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-5A
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.12714
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 56724
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.400
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.6
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.40
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.40
REMARK 200 COMPLETENESS FOR SHELL (%) : 97.8
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: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: AMORE
REMARK 200 STARTING MODEL: PDB ENTRY 1J42
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 55.39
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.76
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: EVAPORATION
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,Y,-Z
REMARK 290 3555 X+1/2,Y+1/2,Z
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 0.00000
REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 3 1.000000 0.000000 0.000000 96.80800
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 51.29100
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 96.80800
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 51.29100
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3, 4
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: 3120 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 14650 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -32.0 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 350
REMARK 350 BIOMOLECULE: 2
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: 3090 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 14690 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -33.4 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D
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
REMARK 350 BIOMOLECULE: 3
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: 3040 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 14240 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -33.5 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: E, F
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
REMARK 350 BIOMOLECULE: 4
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: 3090 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 13930 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -34.9 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: G
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 193.61600
REMARK 350 BIOMT2 2 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 2 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 ASP A 189
REMARK 465 MSE B 201
REMARK 465 ASP B 389
REMARK 465 ASP C 589
REMARK 465 MSE D 601
REMARK 465 ALA D 602
REMARK 465 ASP D 789
REMARK 465 MSE E 801
REMARK 465 MSE F 1001
REMARK 465 ALA F 1002
REMARK 465 ASP F 1189
REMARK 465 MSE G 1201
REMARK 465 ALA G 1202
REMARK 465 ASP G 1389
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 MSE A 1 CG SE CE
REMARK 470 LYS A 41 CG CD CE NZ
REMARK 470 LYS A 63 CG CD CE NZ
REMARK 470 LYS A 99 CG CD CE NZ
REMARK 470 LYS B 241 CG CD CE NZ
REMARK 470 GLU B 259 CG CD OE1 OE2
REMARK 470 LYS B 263 CG CD CE NZ
REMARK 470 MSE C 401 CG SE CE
REMARK 470 LYS C 441 CG CD CE NZ
REMARK 470 LYS C 532 CG CD CE NZ
REMARK 470 LYS C 588 CG CD CE NZ
REMARK 470 LYS D 663 CG CD CE NZ
REMARK 470 GLU D 694 CG CD OE1 OE2
REMARK 470 LYS D 788 CG CD CE NZ
REMARK 470 GLU E 859 CG CD OE1 OE2
REMARK 470 LYS E 863 CG CD CE NZ
REMARK 470 GLU E 894 CG CD OE1 OE2
REMARK 470 LYS E 899 CG CD CE NZ
REMARK 470 GLU E 916 CG CD OE1 OE2
REMARK 470 VAL E 923 CG1 CG2
REMARK 470 GLU E 976 CG CD OE1 OE2
REMARK 470 LYS E 988 CG CD CE NZ
REMARK 470 ASP E 989 CG OD1 OD2
REMARK 470 LYS F1041 CG CD CE NZ
REMARK 470 GLU F1059 CG CD OE1 OE2
REMARK 470 LYS F1063 CG CD CE NZ
REMARK 470 GLU F1090 CG CD OE1 OE2
REMARK 470 LYS F1188 CG CD CE NZ
REMARK 470 LYS G1241 CG CD CE NZ
REMARK 470 GLU G1259 CG CD OE1 OE2
REMARK 470 LYS G1263 CG CD CE NZ
REMARK 470 GLU G1290 CG CD OE1 OE2
REMARK 470 GLU G1294 CG CD OE1 OE2
REMARK 470 ARG G1298 CG CD NE CZ NH1 NH2
REMARK 470 LYS G1299 CG CD CE NZ
REMARK 470 LYS G1332 CG CD CE NZ
REMARK 470 LYS G1388 CG CD CE NZ
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 PRO C 454 C - N - CA ANGL. DEV. = 9.5 DEGREES
REMARK 500 CYS D 653 CA - CB - SG ANGL. DEV. = 8.6 DEGREES
REMARK 500 PRO D 654 C - N - CA ANGL. DEV. = 15.7 DEGREES
REMARK 500 PRO D 654 C - N - CD ANGL. DEV. = -13.1 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 ALA A 2 -152.83 82.34
REMARK 500 CYS A 106 -105.60 70.46
REMARK 500 THR A 110 0.41 -67.40
REMARK 500 PRO B 273 170.03 -59.42
REMARK 500 ASN B 276 -76.44 -49.15
REMARK 500 CYS B 306 -106.55 69.83
REMARK 500 ALA C 402 -163.45 -66.08
REMARK 500 ALA C 456 175.33 176.67
REMARK 500 CYS C 506 -108.18 65.08
REMARK 500 PHE C 519 120.08 -38.28
REMARK 500 ASP C 531 -77.70 -47.67
REMARK 500 HIS C 538 -3.34 -48.77
REMARK 500 PRO D 654 155.30 -49.57
REMARK 500 CYS D 706 -114.54 63.13
REMARK 500 PRO D 709 -7.54 -59.94
REMARK 500 GLU E 864 63.11 -44.48
REMARK 500 LEU E 892 6.95 -68.72
REMARK 500 GLU E 896 -32.26 96.67
REMARK 500 CYS E 906 -107.64 73.34
REMARK 500 PRO E 909 1.58 -64.17
REMARK 500 GLU E 916 70.54 42.64
REMARK 500 MSE E 934 14.18 -69.50
REMARK 500 CYS F1106 -89.88 65.72
REMARK 500 VAL F1186 62.31 66.23
REMARK 500 ASP G1249 -6.98 74.11
REMARK 500 GLU G1264 97.47 -52.80
REMARK 500 PRO G1266 -161.53 -67.15
REMARK 500 VAL G1269 136.38 176.24
REMARK 500 ASN G1276 -65.79 77.09
REMARK 500 CYS G1306 -110.47 62.15
REMARK 500 GLU G1316 59.69 33.36
REMARK 500 THR G1325 -167.76 -119.07
REMARK 500 LYS G1330 -71.09 -48.76
REMARK 500 ASP G1331 -71.34 -28.81
REMARK 500 MSE G1334 9.72 -65.53
REMARK 500 ARG G1356 -136.83 -71.31
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 PO4 A 190
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 A 191
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 C 3
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 D 1
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 E 6
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 F 4
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 F 5
DBREF 3BWE A 1 189 UNP Q99497 PARK7_HUMAN 1 189
DBREF 3BWE B 201 389 UNP Q99497 PARK7_HUMAN 1 189
DBREF 3BWE C 401 589 UNP Q99497 PARK7_HUMAN 1 189
DBREF 3BWE D 601 789 UNP Q99497 PARK7_HUMAN 1 189
DBREF 3BWE E 801 989 UNP Q99497 PARK7_HUMAN 1 189
DBREF 3BWE F 1001 1189 UNP Q99497 PARK7_HUMAN 1 189
DBREF 3BWE G 1201 1389 UNP Q99497 PARK7_HUMAN 1 189
SEQRES 1 A 189 MSE ALA SER LYS ARG ALA LEU VAL ILE LEU ALA LYS GLY
SEQRES 2 A 189 ALA GLU GLU MSE GLU THR VAL ILE PRO VAL ASP VAL MSE
SEQRES 3 A 189 ARG ARG ALA GLY ILE LYS VAL THR VAL ALA GLY LEU ALA
SEQRES 4 A 189 GLY LYS ASP PRO VAL GLN CYS SER ARG ASP VAL VAL ILE
SEQRES 5 A 189 CYS PRO ASP ALA SER LEU GLU ASP ALA LYS LYS GLU GLY
SEQRES 6 A 189 PRO TYR ASP VAL VAL VAL LEU PRO GLY GLY ASN LEU GLY
SEQRES 7 A 189 ALA GLN ASN LEU SER GLU SER ALA ALA VAL LYS GLU ILE
SEQRES 8 A 189 LEU LYS GLU GLN GLU ASN ARG LYS GLY LEU ILE ALA ALA
SEQRES 9 A 189 ILE CYS ALA GLY PRO THR ALA LEU LEU ALA HIS GLU ILE
SEQRES 10 A 189 GLY PHE GLY SER LYS VAL THR THR HIS PRO LEU ALA LYS
SEQRES 11 A 189 ASP LYS MSE MSE ASN GLY GLY HIS TYR THR TYR SER GLU
SEQRES 12 A 189 ASN ARG VAL GLU LYS ASP GLY LEU ILE LEU THR SER ARG
SEQRES 13 A 189 GLY PRO GLY THR SER PHE GLU PHE ALA LEU ALA ILE VAL
SEQRES 14 A 189 GLU ALA LEU ASN GLY LYS GLU VAL ALA ALA GLN VAL LYS
SEQRES 15 A 189 ALA PRO LEU VAL LEU LYS ASP
SEQRES 1 B 189 MSE ALA SER LYS ARG ALA LEU VAL ILE LEU ALA LYS GLY
SEQRES 2 B 189 ALA GLU GLU MSE GLU THR VAL ILE PRO VAL ASP VAL MSE
SEQRES 3 B 189 ARG ARG ALA GLY ILE LYS VAL THR VAL ALA GLY LEU ALA
SEQRES 4 B 189 GLY LYS ASP PRO VAL GLN CYS SER ARG ASP VAL VAL ILE
SEQRES 5 B 189 CYS PRO ASP ALA SER LEU GLU ASP ALA LYS LYS GLU GLY
SEQRES 6 B 189 PRO TYR ASP VAL VAL VAL LEU PRO GLY GLY ASN LEU GLY
SEQRES 7 B 189 ALA GLN ASN LEU SER GLU SER ALA ALA VAL LYS GLU ILE
SEQRES 8 B 189 LEU LYS GLU GLN GLU ASN ARG LYS GLY LEU ILE ALA ALA
SEQRES 9 B 189 ILE CYS ALA GLY PRO THR ALA LEU LEU ALA HIS GLU ILE
SEQRES 10 B 189 GLY PHE GLY SER LYS VAL THR THR HIS PRO LEU ALA LYS
SEQRES 11 B 189 ASP LYS MSE MSE ASN GLY GLY HIS TYR THR TYR SER GLU
SEQRES 12 B 189 ASN ARG VAL GLU LYS ASP GLY LEU ILE LEU THR SER ARG
SEQRES 13 B 189 GLY PRO GLY THR SER PHE GLU PHE ALA LEU ALA ILE VAL
SEQRES 14 B 189 GLU ALA LEU ASN GLY LYS GLU VAL ALA ALA GLN VAL LYS
SEQRES 15 B 189 ALA PRO LEU VAL LEU LYS ASP
SEQRES 1 C 189 MSE ALA SER LYS ARG ALA LEU VAL ILE LEU ALA LYS GLY
SEQRES 2 C 189 ALA GLU GLU MSE GLU THR VAL ILE PRO VAL ASP VAL MSE
SEQRES 3 C 189 ARG ARG ALA GLY ILE LYS VAL THR VAL ALA GLY LEU ALA
SEQRES 4 C 189 GLY LYS ASP PRO VAL GLN CYS SER ARG ASP VAL VAL ILE
SEQRES 5 C 189 CYS PRO ASP ALA SER LEU GLU ASP ALA LYS LYS GLU GLY
SEQRES 6 C 189 PRO TYR ASP VAL VAL VAL LEU PRO GLY GLY ASN LEU GLY
SEQRES 7 C 189 ALA GLN ASN LEU SER GLU SER ALA ALA VAL LYS GLU ILE
SEQRES 8 C 189 LEU LYS GLU GLN GLU ASN ARG LYS GLY LEU ILE ALA ALA
SEQRES 9 C 189 ILE CYS ALA GLY PRO THR ALA LEU LEU ALA HIS GLU ILE
SEQRES 10 C 189 GLY PHE GLY SER LYS VAL THR THR HIS PRO LEU ALA LYS
SEQRES 11 C 189 ASP LYS MSE MSE ASN GLY GLY HIS TYR THR TYR SER GLU
SEQRES 12 C 189 ASN ARG VAL GLU LYS ASP GLY LEU ILE LEU THR SER ARG
SEQRES 13 C 189 GLY PRO GLY THR SER PHE GLU PHE ALA LEU ALA ILE VAL
SEQRES 14 C 189 GLU ALA LEU ASN GLY LYS GLU VAL ALA ALA GLN VAL LYS
SEQRES 15 C 189 ALA PRO LEU VAL LEU LYS ASP
SEQRES 1 D 189 MSE ALA SER LYS ARG ALA LEU VAL ILE LEU ALA LYS GLY
SEQRES 2 D 189 ALA GLU GLU MSE GLU THR VAL ILE PRO VAL ASP VAL MSE
SEQRES 3 D 189 ARG ARG ALA GLY ILE LYS VAL THR VAL ALA GLY LEU ALA
SEQRES 4 D 189 GLY LYS ASP PRO VAL GLN CYS SER ARG ASP VAL VAL ILE
SEQRES 5 D 189 CYS PRO ASP ALA SER LEU GLU ASP ALA LYS LYS GLU GLY
SEQRES 6 D 189 PRO TYR ASP VAL VAL VAL LEU PRO GLY GLY ASN LEU GLY
SEQRES 7 D 189 ALA GLN ASN LEU SER GLU SER ALA ALA VAL LYS GLU ILE
SEQRES 8 D 189 LEU LYS GLU GLN GLU ASN ARG LYS GLY LEU ILE ALA ALA
SEQRES 9 D 189 ILE CYS ALA GLY PRO THR ALA LEU LEU ALA HIS GLU ILE
SEQRES 10 D 189 GLY PHE GLY SER LYS VAL THR THR HIS PRO LEU ALA LYS
SEQRES 11 D 189 ASP LYS MSE MSE ASN GLY GLY HIS TYR THR TYR SER GLU
SEQRES 12 D 189 ASN ARG VAL GLU LYS ASP GLY LEU ILE LEU THR SER ARG
SEQRES 13 D 189 GLY PRO GLY THR SER PHE GLU PHE ALA LEU ALA ILE VAL
SEQRES 14 D 189 GLU ALA LEU ASN GLY LYS GLU VAL ALA ALA GLN VAL LYS
SEQRES 15 D 189 ALA PRO LEU VAL LEU LYS ASP
SEQRES 1 E 189 MSE ALA SER LYS ARG ALA LEU VAL ILE LEU ALA LYS GLY
SEQRES 2 E 189 ALA GLU GLU MSE GLU THR VAL ILE PRO VAL ASP VAL MSE
SEQRES 3 E 189 ARG ARG ALA GLY ILE LYS VAL THR VAL ALA GLY LEU ALA
SEQRES 4 E 189 GLY LYS ASP PRO VAL GLN CYS SER ARG ASP VAL VAL ILE
SEQRES 5 E 189 CYS PRO ASP ALA SER LEU GLU ASP ALA LYS LYS GLU GLY
SEQRES 6 E 189 PRO TYR ASP VAL VAL VAL LEU PRO GLY GLY ASN LEU GLY
SEQRES 7 E 189 ALA GLN ASN LEU SER GLU SER ALA ALA VAL LYS GLU ILE
SEQRES 8 E 189 LEU LYS GLU GLN GLU ASN ARG LYS GLY LEU ILE ALA ALA
SEQRES 9 E 189 ILE CYS ALA GLY PRO THR ALA LEU LEU ALA HIS GLU ILE
SEQRES 10 E 189 GLY PHE GLY SER LYS VAL THR THR HIS PRO LEU ALA LYS
SEQRES 11 E 189 ASP LYS MSE MSE ASN GLY GLY HIS TYR THR TYR SER GLU
SEQRES 12 E 189 ASN ARG VAL GLU LYS ASP GLY LEU ILE LEU THR SER ARG
SEQRES 13 E 189 GLY PRO GLY THR SER PHE GLU PHE ALA LEU ALA ILE VAL
SEQRES 14 E 189 GLU ALA LEU ASN GLY LYS GLU VAL ALA ALA GLN VAL LYS
SEQRES 15 E 189 ALA PRO LEU VAL LEU LYS ASP
SEQRES 1 F 189 MSE ALA SER LYS ARG ALA LEU VAL ILE LEU ALA LYS GLY
SEQRES 2 F 189 ALA GLU GLU MSE GLU THR VAL ILE PRO VAL ASP VAL MSE
SEQRES 3 F 189 ARG ARG ALA GLY ILE LYS VAL THR VAL ALA GLY LEU ALA
SEQRES 4 F 189 GLY LYS ASP PRO VAL GLN CYS SER ARG ASP VAL VAL ILE
SEQRES 5 F 189 CYS PRO ASP ALA SER LEU GLU ASP ALA LYS LYS GLU GLY
SEQRES 6 F 189 PRO TYR ASP VAL VAL VAL LEU PRO GLY GLY ASN LEU GLY
SEQRES 7 F 189 ALA GLN ASN LEU SER GLU SER ALA ALA VAL LYS GLU ILE
SEQRES 8 F 189 LEU LYS GLU GLN GLU ASN ARG LYS GLY LEU ILE ALA ALA
SEQRES 9 F 189 ILE CYS ALA GLY PRO THR ALA LEU LEU ALA HIS GLU ILE
SEQRES 10 F 189 GLY PHE GLY SER LYS VAL THR THR HIS PRO LEU ALA LYS
SEQRES 11 F 189 ASP LYS MSE MSE ASN GLY GLY HIS TYR THR TYR SER GLU
SEQRES 12 F 189 ASN ARG VAL GLU LYS ASP GLY LEU ILE LEU THR SER ARG
SEQRES 13 F 189 GLY PRO GLY THR SER PHE GLU PHE ALA LEU ALA ILE VAL
SEQRES 14 F 189 GLU ALA LEU ASN GLY LYS GLU VAL ALA ALA GLN VAL LYS
SEQRES 15 F 189 ALA PRO LEU VAL LEU LYS ASP
SEQRES 1 G 189 MSE ALA SER LYS ARG ALA LEU VAL ILE LEU ALA LYS GLY
SEQRES 2 G 189 ALA GLU GLU MSE GLU THR VAL ILE PRO VAL ASP VAL MSE
SEQRES 3 G 189 ARG ARG ALA GLY ILE LYS VAL THR VAL ALA GLY LEU ALA
SEQRES 4 G 189 GLY LYS ASP PRO VAL GLN CYS SER ARG ASP VAL VAL ILE
SEQRES 5 G 189 CYS PRO ASP ALA SER LEU GLU ASP ALA LYS LYS GLU GLY
SEQRES 6 G 189 PRO TYR ASP VAL VAL VAL LEU PRO GLY GLY ASN LEU GLY
SEQRES 7 G 189 ALA GLN ASN LEU SER GLU SER ALA ALA VAL LYS GLU ILE
SEQRES 8 G 189 LEU LYS GLU GLN GLU ASN ARG LYS GLY LEU ILE ALA ALA
SEQRES 9 G 189 ILE CYS ALA GLY PRO THR ALA LEU LEU ALA HIS GLU ILE
SEQRES 10 G 189 GLY PHE GLY SER LYS VAL THR THR HIS PRO LEU ALA LYS
SEQRES 11 G 189 ASP LYS MSE MSE ASN GLY GLY HIS TYR THR TYR SER GLU
SEQRES 12 G 189 ASN ARG VAL GLU LYS ASP GLY LEU ILE LEU THR SER ARG
SEQRES 13 G 189 GLY PRO GLY THR SER PHE GLU PHE ALA LEU ALA ILE VAL
SEQRES 14 G 189 GLU ALA LEU ASN GLY LYS GLU VAL ALA ALA GLN VAL LYS
SEQRES 15 G 189 ALA PRO LEU VAL LEU LYS ASP
MODRES 3BWE MSE A 1 MET SELENOMETHIONINE
MODRES 3BWE MSE A 17 MET SELENOMETHIONINE
MODRES 3BWE MSE A 26 MET SELENOMETHIONINE
MODRES 3BWE MSE A 133 MET SELENOMETHIONINE
MODRES 3BWE MSE A 134 MET SELENOMETHIONINE
MODRES 3BWE MSE B 217 MET SELENOMETHIONINE
MODRES 3BWE MSE B 226 MET SELENOMETHIONINE
MODRES 3BWE MSE B 333 MET SELENOMETHIONINE
MODRES 3BWE MSE B 334 MET SELENOMETHIONINE
MODRES 3BWE MSE C 401 MET SELENOMETHIONINE
MODRES 3BWE MSE C 417 MET SELENOMETHIONINE
MODRES 3BWE MSE C 426 MET SELENOMETHIONINE
MODRES 3BWE MSE C 533 MET SELENOMETHIONINE
MODRES 3BWE MSE C 534 MET SELENOMETHIONINE
MODRES 3BWE MSE D 617 MET SELENOMETHIONINE
MODRES 3BWE MSE D 626 MET SELENOMETHIONINE
MODRES 3BWE MSE D 733 MET SELENOMETHIONINE
MODRES 3BWE MSE D 734 MET SELENOMETHIONINE
MODRES 3BWE MSE E 817 MET SELENOMETHIONINE
MODRES 3BWE MSE E 826 MET SELENOMETHIONINE
MODRES 3BWE MSE E 933 MET SELENOMETHIONINE
MODRES 3BWE MSE E 934 MET SELENOMETHIONINE
MODRES 3BWE MSE F 1017 MET SELENOMETHIONINE
MODRES 3BWE MSE F 1026 MET SELENOMETHIONINE
MODRES 3BWE MSE F 1133 MET SELENOMETHIONINE
MODRES 3BWE MSE F 1134 MET SELENOMETHIONINE
MODRES 3BWE MSE G 1217 MET SELENOMETHIONINE
MODRES 3BWE MSE G 1226 MET SELENOMETHIONINE
MODRES 3BWE MSE G 1333 MET SELENOMETHIONINE
MODRES 3BWE MSE G 1334 MET SELENOMETHIONINE
HET MSE A 1 5
HET MSE A 17 8
HET MSE A 26 8
HET MSE A 133 8
HET MSE A 134 8
HET MSE B 217 8
HET MSE B 226 8
HET MSE B 333 8
HET MSE B 334 8
HET MSE C 401 5
HET MSE C 417 8
HET MSE C 426 8
HET MSE C 533 8
HET MSE C 534 8
HET MSE D 617 8
HET MSE D 626 8
HET MSE D 733 8
HET MSE D 734 8
HET MSE E 817 8
HET MSE E 826 8
HET MSE E 933 8
HET MSE E 934 8
HET MSE F1017 8
HET MSE F1026 8
HET MSE F1133 8
HET MSE F1134 8
HET MSE G1217 8
HET MSE G1226 8
HET MSE G1333 8
HET MSE G1334 8
HET PO4 A 190 5
HET PO4 A 191 5
HET PO4 C 3 5
HET PO4 D 1 5
HET PO4 E 6 5
HET PO4 F 4 5
HET PO4 F 5 5
HETNAM MSE SELENOMETHIONINE
HETNAM PO4 PHOSPHATE ION
FORMUL 1 MSE 30(C5 H11 N O2 SE)
FORMUL 8 PO4 7(O4 P 3-)
FORMUL 15 HOH *283(H2 O)
HELIX 1 1 GLU A 15 ALA A 29 1 15
HELIX 2 2 LEU A 58 LYS A 62 1 5
HELIX 3 3 GLY A 75 GLU A 84 1 10
HELIX 4 4 SER A 85 ARG A 98 1 14
HELIX 5 5 PRO A 109 HIS A 115 1 7
HELIX 6 6 HIS A 126 LEU A 128 5 3
HELIX 7 7 ALA A 129 MSE A 134 1 6
HELIX 8 8 GLY A 157 GLY A 159 5 3
HELIX 9 9 THR A 160 GLY A 174 1 15
HELIX 10 10 GLY A 174 ALA A 183 1 10
HELIX 11 11 PRO A 184 VAL A 186 5 3
HELIX 12 12 GLU B 215 ALA B 229 1 15
HELIX 13 13 LEU B 258 LYS B 262 1 5
HELIX 14 14 GLY B 275 GLU B 284 1 10
HELIX 15 15 SER B 285 ARG B 298 1 14
HELIX 16 16 GLY B 308 HIS B 315 1 8
HELIX 17 17 HIS B 326 LEU B 328 5 3
HELIX 18 18 ALA B 329 ASN B 335 1 7
HELIX 19 19 GLY B 357 GLY B 359 5 3
HELIX 20 20 THR B 360 GLY B 374 1 15
HELIX 21 21 GLY B 374 VAL B 386 1 13
HELIX 22 22 GLU C 415 ALA C 429 1 15
HELIX 23 23 LEU C 458 GLU C 464 1 7
HELIX 24 24 GLY C 475 GLU C 484 1 10
HELIX 25 25 SER C 485 ARG C 498 1 14
HELIX 26 26 GLY C 508 HIS C 515 1 8
HELIX 27 27 HIS C 526 LEU C 528 5 3
HELIX 28 28 ALA C 529 ASN C 535 1 7
HELIX 29 29 GLY C 557 GLY C 559 5 3
HELIX 30 30 THR C 560 GLY C 574 1 15
HELIX 31 31 GLY C 574 ALA C 583 1 10
HELIX 32 32 PRO C 584 VAL C 586 5 3
HELIX 33 33 GLU D 615 ALA D 629 1 15
HELIX 34 34 LEU D 658 LYS D 662 1 5
HELIX 35 35 GLY D 675 SER D 685 1 11
HELIX 36 36 SER D 685 ARG D 698 1 14
HELIX 37 37 GLY D 708 HIS D 715 1 8
HELIX 38 38 HIS D 726 LEU D 728 5 3
HELIX 39 39 ALA D 729 MSE D 734 1 6
HELIX 40 40 GLY D 757 GLY D 759 5 3
HELIX 41 41 THR D 760 ALA D 783 1 24
HELIX 42 42 PRO D 784 VAL D 786 5 3
HELIX 43 43 GLU E 815 ALA E 829 1 15
HELIX 44 44 LEU E 858 GLU E 864 1 7
HELIX 45 45 GLY E 875 SER E 885 1 11
HELIX 46 46 SER E 885 ARG E 898 1 14
HELIX 47 47 PRO E 909 HIS E 915 1 7
HELIX 48 48 HIS E 926 LEU E 928 5 3
HELIX 49 49 ALA E 929 MSE E 934 1 6
HELIX 50 50 GLY E 957 GLY E 959 5 3
HELIX 51 51 THR E 960 GLY E 974 1 15
HELIX 52 52 GLY E 974 ALA E 983 1 10
HELIX 53 53 PRO E 984 VAL E 986 5 3
HELIX 54 54 GLU F 1015 ALA F 1029 1 15
HELIX 55 55 LEU F 1058 GLU F 1064 1 7
HELIX 56 56 GLY F 1075 SER F 1085 1 11
HELIX 57 57 SER F 1085 ARG F 1098 1 14
HELIX 58 58 GLY F 1108 HIS F 1115 1 8
HELIX 59 59 HIS F 1126 LEU F 1128 5 3
HELIX 60 60 ALA F 1129 ASN F 1135 1 7
HELIX 61 61 GLY F 1157 GLY F 1159 5 3
HELIX 62 62 THR F 1160 GLY F 1174 1 15
HELIX 63 63 GLY F 1174 ALA F 1183 1 10
HELIX 64 64 PRO F 1184 VAL F 1186 5 3
HELIX 65 65 GLU G 1215 ALA G 1229 1 15
HELIX 66 66 LEU G 1258 GLU G 1264 1 7
HELIX 67 67 ASN G 1276 SER G 1285 1 10
HELIX 68 68 SER G 1285 ARG G 1298 1 14
HELIX 69 69 GLY G 1308 HIS G 1315 1 8
HELIX 70 70 HIS G 1326 LEU G 1328 5 3
HELIX 71 71 ALA G 1329 MSE G 1334 1 6
HELIX 72 72 ASN G 1335 HIS G 1338 5 4
HELIX 73 73 GLY G 1357 GLY G 1359 5 3
HELIX 74 74 THR G 1360 GLY G 1374 1 15
HELIX 75 75 GLY G 1374 ALA G 1383 1 10
HELIX 76 76 PRO G 1384 VAL G 1386 5 3
SHEET 1 A 7 ALA A 56 SER A 57 0
SHEET 2 A 7 LYS A 32 GLY A 37 1 N GLY A 37 O ALA A 56
SHEET 3 A 7 ARG A 5 LEU A 10 1 N ALA A 6 O LYS A 32
SHEET 4 A 7 VAL A 69 LEU A 72 1 O VAL A 71 N LEU A 7
SHEET 5 A 7 LEU A 101 ILE A 105 1 O ALA A 103 N VAL A 70
SHEET 6 A 7 ILE A 152 SER A 155 1 O LEU A 153 N ILE A 102
SHEET 7 A 7 VAL A 146 ASP A 149 -1 N GLU A 147 O THR A 154
SHEET 1 B 4 VAL A 44 GLN A 45 0
SHEET 2 B 4 VAL A 51 CYS A 53 -1 O ILE A 52 N VAL A 44
SHEET 3 B 4 VAL B 251 CYS B 253 -1 O CYS B 253 N VAL A 51
SHEET 4 B 4 VAL B 244 GLN B 245 -1 N VAL B 244 O ILE B 252
SHEET 1 C 2 LYS A 122 VAL A 123 0
SHEET 2 C 2 THR A 140 TYR A 141 1 O THR A 140 N VAL A 123
SHEET 1 D 7 ALA B 256 SER B 257 0
SHEET 2 D 7 LYS B 232 GLY B 237 1 N GLY B 237 O ALA B 256
SHEET 3 D 7 ARG B 205 LEU B 210 1 N LEU B 210 O ALA B 236
SHEET 4 D 7 VAL B 269 LEU B 272 1 O VAL B 271 N LEU B 207
SHEET 5 D 7 LEU B 301 ILE B 305 1 O ALA B 303 N LEU B 272
SHEET 6 D 7 ILE B 352 SER B 355 1 O LEU B 353 N ILE B 302
SHEET 7 D 7 VAL B 346 ASP B 349 -1 N GLU B 347 O THR B 354
SHEET 1 E 2 LYS B 322 VAL B 323 0
SHEET 2 E 2 THR B 340 TYR B 341 1 O THR B 340 N VAL B 323
SHEET 1 F 7 ALA C 456 SER C 457 0
SHEET 2 F 7 LYS C 432 GLY C 437 1 N GLY C 437 O ALA C 456
SHEET 3 F 7 ARG C 405 LEU C 410 1 N VAL C 408 O ALA C 436
SHEET 4 F 7 VAL C 469 LEU C 472 1 O VAL C 471 N LEU C 407
SHEET 5 F 7 LEU C 501 ILE C 505 1 O ALA C 503 N VAL C 470
SHEET 6 F 7 ILE C 552 SER C 555 1 O LEU C 553 N ILE C 502
SHEET 7 F 7 VAL C 546 ASP C 549 -1 N GLU C 547 O THR C 554
SHEET 1 G 4 VAL C 444 GLN C 445 0
SHEET 2 G 4 VAL C 451 CYS C 453 -1 O ILE C 452 N VAL C 444
SHEET 3 G 4 VAL D 651 ILE D 652 -1 O VAL D 651 N CYS C 453
SHEET 4 G 4 VAL D 644 GLN D 645 -1 N VAL D 644 O ILE D 652
SHEET 1 H 2 LYS C 522 VAL C 523 0
SHEET 2 H 2 THR C 540 TYR C 541 1 O THR C 540 N VAL C 523
SHEET 1 I 7 ALA D 656 SER D 657 0
SHEET 2 I 7 LYS D 632 GLY D 637 1 N GLY D 637 O ALA D 656
SHEET 3 I 7 ARG D 605 LEU D 610 1 N LEU D 610 O ALA D 636
SHEET 4 I 7 VAL D 669 LEU D 672 1 O VAL D 671 N LEU D 607
SHEET 5 I 7 LEU D 701 ILE D 705 1 O ALA D 703 N LEU D 672
SHEET 6 I 7 ILE D 752 SER D 755 1 O LEU D 753 N ILE D 702
SHEET 7 I 7 VAL D 746 ASP D 749 -1 N GLU D 747 O THR D 754
SHEET 1 J 2 LYS D 722 VAL D 723 0
SHEET 2 J 2 THR D 740 TYR D 741 1 O THR D 740 N VAL D 723
SHEET 1 K 7 ALA E 856 SER E 857 0
SHEET 2 K 7 LYS E 832 GLY E 837 1 N GLY E 837 O ALA E 856
SHEET 3 K 7 ARG E 805 LEU E 810 1 N VAL E 808 O ALA E 836
SHEET 4 K 7 VAL E 869 LEU E 872 1 O VAL E 869 N LEU E 807
SHEET 5 K 7 LEU E 901 ILE E 905 1 O ALA E 903 N LEU E 872
SHEET 6 K 7 ILE E 952 SER E 955 1 O LEU E 953 N ILE E 902
SHEET 7 K 7 VAL E 946 ASP E 949 -1 N GLU E 947 O THR E 954
SHEET 1 L 4 VAL E 844 GLN E 845 0
SHEET 2 L 4 VAL E 851 CYS E 853 -1 O ILE E 852 N VAL E 844
SHEET 3 L 4 VAL F1051 CYS F1053 -1 O VAL F1051 N CYS E 853
SHEET 4 L 4 VAL F1044 GLN F1045 -1 N VAL F1044 O ILE F1052
SHEET 1 M 2 LYS E 922 VAL E 923 0
SHEET 2 M 2 THR E 940 TYR E 941 1 O THR E 940 N VAL E 923
SHEET 1 N 7 ALA F1056 SER F1057 0
SHEET 2 N 7 LYS F1032 GLY F1037 1 N GLY F1037 O ALA F1056
SHEET 3 N 7 ARG F1005 LEU F1010 1 N VAL F1008 O THR F1034
SHEET 4 N 7 VAL F1069 LEU F1072 1 O VAL F1071 N LEU F1007
SHEET 5 N 7 LEU F1101 ILE F1105 1 O ALA F1103 N LEU F1072
SHEET 6 N 7 ILE F1152 SER F1155 1 O LEU F1153 N ALA F1104
SHEET 7 N 7 VAL F1146 ASP F1149 -1 N GLU F1147 O THR F1154
SHEET 1 O 2 LYS F1122 VAL F1123 0
SHEET 2 O 2 THR F1140 TYR F1141 1 O THR F1140 N VAL F1123
SHEET 1 P 7 ALA G1256 SER G1257 0
SHEET 2 P 7 LYS G1232 GLY G1237 1 N GLY G1237 O ALA G1256
SHEET 3 P 7 ARG G1205 LEU G1210 1 N LEU G1210 O ALA G1236
SHEET 4 P 7 VAL G1269 LEU G1272 1 O VAL G1269 N LEU G1207
SHEET 5 P 7 LEU G1301 ILE G1305 1 O ALA G1303 N LEU G1272
SHEET 6 P 7 ILE G1352 SER G1355 1 O LEU G1353 N ILE G1302
SHEET 7 P 7 VAL G1346 ASP G1349 -1 N ASP G1349 O ILE G1352
SHEET 1 Q 2 VAL G1244 GLN G1245 0
SHEET 2 Q 2 VAL G1251 ILE G1252 -1 O ILE G1252 N VAL G1244
SHEET 1 R 2 LYS G1322 VAL G1323 0
SHEET 2 R 2 THR G1340 TYR G1341 1 O THR G1340 N VAL G1323
SSBOND 1 CYS C 453 CYS D 653 1555 1555 2.07
SSBOND 2 CYS E 853 CYS F 1053 1555 1555 3.00
LINK C MSE A 1 N ALA A 2 1555 1555 1.34
LINK C GLU A 16 N MSE A 17 1555 1555 1.33
LINK C MSE A 17 N GLU A 18 1555 1555 1.32
LINK C VAL A 25 N MSE A 26 1555 1555 1.33
LINK C MSE A 26 N ARG A 27 1555 1555 1.33
LINK C LYS A 132 N MSE A 133 1555 1555 1.33
LINK C MSE A 133 N MSE A 134 1555 1555 1.33
LINK C MSE A 134 N ASN A 135 1555 1555 1.32
LINK C GLU B 216 N MSE B 217 1555 1555 1.33
LINK C MSE B 217 N GLU B 218 1555 1555 1.33
LINK C VAL B 225 N MSE B 226 1555 1555 1.33
LINK C MSE B 226 N ARG B 227 1555 1555 1.33
LINK C LYS B 332 N MSE B 333 1555 1555 1.32
LINK C MSE B 333 N MSE B 334 1555 1555 1.32
LINK C MSE B 334 N ASN B 335 1555 1555 1.32
LINK C MSE C 401 N ALA C 402 1555 1555 1.33
LINK C GLU C 416 N MSE C 417 1555 1555 1.33
LINK C MSE C 417 N GLU C 418 1555 1555 1.33
LINK C VAL C 425 N MSE C 426 1555 1555 1.33
LINK C MSE C 426 N ARG C 427 1555 1555 1.33
LINK C LYS C 532 N MSE C 533 1555 1555 1.32
LINK C MSE C 533 N MSE C 534 1555 1555 1.33
LINK C MSE C 534 N ASN C 535 1555 1555 1.32
LINK C GLU D 616 N MSE D 617 1555 1555 1.33
LINK C MSE D 617 N GLU D 618 1555 1555 1.33
LINK C VAL D 625 N MSE D 626 1555 1555 1.33
LINK C MSE D 626 N ARG D 627 1555 1555 1.33
LINK C LYS D 732 N MSE D 733 1555 1555 1.33
LINK C MSE D 733 N MSE D 734 1555 1555 1.33
LINK C MSE D 734 N ASN D 735 1555 1555 1.33
LINK C GLU E 816 N MSE E 817 1555 1555 1.32
LINK C MSE E 817 N GLU E 818 1555 1555 1.33
LINK C VAL E 825 N MSE E 826 1555 1555 1.33
LINK C MSE E 826 N ARG E 827 1555 1555 1.33
LINK C LYS E 932 N MSE E 933 1555 1555 1.33
LINK C MSE E 933 N MSE E 934 1555 1555 1.33
LINK C MSE E 934 N ASN E 935 1555 1555 1.33
LINK C GLU F1016 N MSE F1017 1555 1555 1.32
LINK C MSE F1017 N GLU F1018 1555 1555 1.33
LINK C VAL F1025 N MSE F1026 1555 1555 1.33
LINK C MSE F1026 N ARG F1027 1555 1555 1.33
LINK C LYS F1132 N MSE F1133 1555 1555 1.32
LINK C MSE F1133 N MSE F1134 1555 1555 1.33
LINK C MSE F1134 N ASN F1135 1555 1555 1.32
LINK C GLU G1216 N MSE G1217 1555 1555 1.33
LINK C MSE G1217 N GLU G1218 1555 1555 1.33
LINK C VAL G1225 N MSE G1226 1555 1555 1.33
LINK C MSE G1226 N ARG G1227 1555 1555 1.33
LINK C LYS G1332 N MSE G1333 1555 1555 1.33
LINK C MSE G1333 N MSE G1334 1555 1555 1.33
LINK C MSE G1334 N ASN G1335 1555 1555 1.33
SITE 1 AC1 4 ARG A 48 ASN A 76 HOH C 95 GLN C 580
SITE 1 AC2 6 GLN A 180 HOH A 228 SER B 247 ARG B 248
SITE 2 AC2 6 GLY B 275 ASN B 276
SITE 1 AC3 4 ARG C 448 ASN C 476 ARG D 628 GLN E 980
SITE 1 AC4 5 GLN B 380 ARG C 428 ARG D 648 GLY D 675
SITE 2 AC4 5 ASN D 676
SITE 1 AC5 4 ARG E 848 ASN E 876 HOH G 174 GLN G1380
SITE 1 AC6 4 HOH D 126 GLN D 780 ARG F1048 ASN F1076
SITE 1 AC7 6 GLN F1180 GLU G1215 ARG G1248 GLY G1275
SITE 2 AC7 6 ASN G1276 LEU G1277
CRYST1 193.616 102.582 85.535 90.00 113.69 90.00 C 1 2 1 28
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 0.005165 0.000000 0.002266 0.00000
SCALE2 0.000000 0.009748 0.000000 0.00000
SCALE3 0.000000 0.000000 0.012767 0.00000
HETATM 1 N MSE A 1 -19.082 17.673 46.909 1.00 43.63 N
HETATM 2 CA MSE A 1 -17.638 17.348 47.126 1.00 43.68 C
HETATM 3 C MSE A 1 -16.810 17.511 45.851 1.00 43.68 C
HETATM 4 O MSE A 1 -15.647 17.925 45.916 1.00 44.47 O
HETATM 5 CB MSE A 1 -17.494 15.922 47.661 1.00 43.55 C
(ATOM LINES ARE NOT SHOWN.)
END