HEADER PROTEIN BINDING 23-AUG-07 2R1T
TITLE DOPAMINE QUINONE CONJUGATION TO DJ-1
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: DJ-1;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: ONCOGENE DJ1, PARKINSON DISEASE PROTEIN 7;
COMPND 5 ENGINEERED: YES;
COMPND 6 MUTATION: YES;
COMPND 7 MOL_ID: 2;
COMPND 8 MOLECULE: DJ-1;
COMPND 9 CHAIN: B;
COMPND 10 SYNONYM: ONCOGENE DJ1, PARKINSON DISEASE PROTEIN 7;
COMPND 11 ENGINEERED: YES;
COMPND 12 MUTATION: 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;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: B834;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: VECTOR;
SOURCE 10 EXPRESSION_SYSTEM_VECTOR: PET15B;
SOURCE 11 MOL_ID: 2;
SOURCE 12 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 13 ORGANISM_COMMON: HUMAN;
SOURCE 14 ORGANISM_TAXID: 9606;
SOURCE 15 GENE: PARK7;
SOURCE 16 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 17 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 18 EXPRESSION_SYSTEM_STRAIN: B834;
SOURCE 19 EXPRESSION_SYSTEM_VECTOR_TYPE: VECTOR;
SOURCE 20 EXPRESSION_SYSTEM_VECTOR: PET15B
KEYWDS DJ-1, DOPAMINE QUINONE CONJUGATION, ISOPEPTIDASE, SUMO-1, CHAPERONE,
KEYWDS 2 CYTOPLASM, DISEASE MUTATION, NUCLEUS, ONCOGENE, OXIDATION, PARKINSON
KEYWDS 3 DISEASE, PHOSPHORYLATION, POLYMORPHISM, UBL CONJUGATION, PROTEIN
KEYWDS 4 BINDING
EXPDTA X-RAY DIFFRACTION
AUTHOR Z.ZHONGTAO,F.YUE
REVDAT 4 20-OCT-21 2R1T 1 SEQADV SHEET LINK
REVDAT 3 25-OCT-17 2R1T 1 SOURCE REMARK
REVDAT 2 24-FEB-09 2R1T 1 VERSN
REVDAT 1 26-AUG-08 2R1T 0
JRNL AUTH Z.ZHONGTAO,F.YUE
JRNL TITL DJ-1 IS A PROISOPEPTIDASE
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 1.70 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) : 1.70
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 21.79
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) (%) : 70.0
REMARK 3 NUMBER OF REFLECTIONS : 37025
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) : 0.208
REMARK 3 FREE R VALUE : 0.236
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 7.100
REMARK 3 FREE R VALUE TEST SET COUNT : 3752
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : NULL
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : NULL
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : NULL
REMARK 3 BIN RESOLUTION RANGE LOW (A) : NULL
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : NULL
REMARK 3 BIN FREE R VALUE : NULL
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 BIN FREE R VALUE TEST SET COUNT : NULL
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2761
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 417
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 25.18
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -3.87100
REMARK 3 B22 (A**2) : -3.87100
REMARK 3 B33 (A**2) : 7.74200
REMARK 3 B12 (A**2) : -2.84700
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) : NULL
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) : 1.236 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 1.845 ; 2.000
REMARK 3 SIDE-CHAIN BOND (A**2) : 2.153 ; 2.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 3.201 ; 2.500
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : NULL
REMARK 3 KSOL : NULL
REMARK 3 BSOL : 61.98
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_DYS.PARAM
REMARK 3 PARAMETER FILE 2 : DNA-RNA_REP.PARAM
REMARK 3 PARAMETER FILE 3 : WATER_REP.PARAM
REMARK 3 PARAMETER FILE 4 : ION.PARAM
REMARK 3 PARAMETER FILE 5 : 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
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 2R1T COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 28-SEP-07.
REMARK 100 THE DEPOSITION ID IS D_1000044318.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 22-JUN-07
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 : APS
REMARK 200 BEAMLINE : 19-BM
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : NULL
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 52340
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.700
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 97.0
REMARK 200 DATA REDUNDANCY : 6.000
REMARK 200 R MERGE (I) : 0.08600
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 20.0000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
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: CNS
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 60.78
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.14
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 29% PEG4K, PH 6.5, VAPOR DIFFUSION,
REMARK 280 HANGING DROP, TEMPERATURE 290K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 31
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
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 25.16800
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 50.33600
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 2720 ANGSTROM**2
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 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 O HOH B 237 O HOH B 250 3454 2.15
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 106 -112.12 63.88
REMARK 500 ALA B 106 -110.91 63.84
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1J42 RELATED DB: PDB
REMARK 900 RELATED ID: 2R1U RELATED DB: PDB
REMARK 900 RELATED ID: 2R1V RELATED DB: PDB
DBREF 2R1T A 2 188 UNP Q99497 PARK7_HUMAN 2 188
DBREF 2R1T B 2 188 UNP Q99497 PARK7_HUMAN 2 188
SEQADV 2R1T ALA A 106 UNP Q99497 CYS 106 ENGINEERED MUTATION
SEQADV 2R1T ALA B 106 UNP Q99497 CYS 106 ENGINEERED MUTATION
SEQRES 1 A 187 ALA SER LYS ARG ALA LEU VAL ILE LEU ALA LYS GLY ALA
SEQRES 2 A 187 GLU GLU MET GLU THR VAL ILE PRO VAL ASP VAL MET ARG
SEQRES 3 A 187 ARG ALA GLY ILE LYS VAL THR VAL ALA GLY LEU ALA GLY
SEQRES 4 A 187 LYS ASP PRO VAL GLN CYS SER ARG ASP VAL VAL ILE CYS
SEQRES 5 A 187 PRO ASP ALA SER LEU GLU ASP ALA LYS LYS GLU GLY PRO
SEQRES 6 A 187 TYR ASP VAL VAL VAL LEU PRO GLY GLY ASN LEU GLY ALA
SEQRES 7 A 187 GLN ASN LEU SER GLU SER ALA ALA VAL LYS GLU ILE LEU
SEQRES 8 A 187 LYS GLU GLN GLU ASN ARG LYS GLY LEU ILE ALA ALA ILE
SEQRES 9 A 187 ALA ALA GLY PRO THR ALA LEU LEU ALA HIS GLU ILE GLY
SEQRES 10 A 187 PHE GLY SER LYS VAL THR THR HIS PRO LEU ALA LYS ASP
SEQRES 11 A 187 LYS MET MET ASN GLY GLY HIS TYR THR TYR SER GLU ASN
SEQRES 12 A 187 ARG VAL GLU LYS ASP GLY LEU ILE LEU THR SER ARG GLY
SEQRES 13 A 187 PRO GLY THR SER PHE GLU PHE ALA LEU ALA ILE VAL GLU
SEQRES 14 A 187 ALA LEU ASN GLY LYS GLU VAL ALA ALA GLN VAL LYS ALA
SEQRES 15 A 187 PRO LEU VAL LEU LYS
SEQRES 1 B 187 ALA SER LYS ARG ALA LEU VAL ILE LEU ALA LYS GLY ALA
SEQRES 2 B 187 GLU GLU MET GLU THR VAL ILE PRO VAL ASP VAL MET ARG
SEQRES 3 B 187 ARG ALA GLY ILE LYS VAL THR VAL ALA GLY LEU ALA GLY
SEQRES 4 B 187 LYS ASP PRO VAL GLN CYS SER ARG ASP VAL VAL ILE DYS
SEQRES 5 B 187 PRO ASP ALA SER LEU GLU ASP ALA LYS LYS GLU GLY PRO
SEQRES 6 B 187 TYR ASP VAL VAL VAL LEU PRO GLY GLY ASN LEU GLY ALA
SEQRES 7 B 187 GLN ASN LEU SER GLU SER ALA ALA VAL LYS GLU ILE LEU
SEQRES 8 B 187 LYS GLU GLN GLU ASN ARG LYS GLY LEU ILE ALA ALA ILE
SEQRES 9 B 187 ALA ALA GLY PRO THR ALA LEU LEU ALA HIS GLU ILE GLY
SEQRES 10 B 187 PHE GLY SER LYS VAL THR THR HIS PRO LEU ALA LYS ASP
SEQRES 11 B 187 LYS MET MET ASN GLY GLY HIS TYR THR TYR SER GLU ASN
SEQRES 12 B 187 ARG VAL GLU LYS ASP GLY LEU ILE LEU THR SER ARG GLY
SEQRES 13 B 187 PRO GLY THR SER PHE GLU PHE ALA LEU ALA ILE VAL GLU
SEQRES 14 B 187 ALA LEU ASN GLY LYS GLU VAL ALA ALA GLN VAL LYS ALA
SEQRES 15 B 187 PRO LEU VAL LEU LYS
MODRES 2R1T DYS B 53 CYS
HET DYS B 53 17
HETNAM DYS S-[5-(2-AMINOETHYL)-2,3-DIHYDROXYPHENYL]-L-CYSTEINE
FORMUL 2 DYS C11 H16 N2 O4 S
FORMUL 3 HOH *417(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 LYS A 63 GLY A 65 5 3
HELIX 4 4 GLY A 75 GLU A 84 1 10
HELIX 5 5 SER A 85 ARG A 98 1 14
HELIX 6 6 PRO A 109 HIS A 115 1 7
HELIX 7 7 HIS A 126 LEU A 128 5 3
HELIX 8 8 ALA A 129 ASN A 135 1 7
HELIX 9 9 GLY A 157 GLY A 159 5 3
HELIX 10 10 THR A 160 GLY A 174 1 15
HELIX 11 11 GLY A 174 ALA A 183 1 10
HELIX 12 12 PRO A 184 VAL A 186 5 3
HELIX 13 13 GLU B 15 ALA B 29 1 15
HELIX 14 14 LEU B 58 LYS B 62 1 5
HELIX 15 15 LYS B 63 GLY B 65 5 3
HELIX 16 16 GLY B 75 GLU B 84 1 10
HELIX 17 17 SER B 85 ARG B 98 1 14
HELIX 18 18 PRO B 109 HIS B 115 1 7
HELIX 19 19 HIS B 126 LEU B 128 5 3
HELIX 20 20 ALA B 129 MET B 134 1 6
HELIX 21 21 GLY B 157 GLY B 159 5 3
HELIX 22 22 THR B 160 GLY B 174 1 15
HELIX 23 23 GLY B 174 ALA B 183 1 10
HELIX 24 24 PRO B 184 VAL B 186 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 LEU A 10 O ALA A 36
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 LEU A 72
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 3 VAL A 44 GLN A 45 0
SHEET 2 B 3 VAL B 51 DYS B 53 -1 O DYS B 53 N VAL A 51
SHEET 3 B 3 VAL B 44 GLN B 45 -1 N VAL B 44 O ILE B 52
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 56 SER B 57 0
SHEET 2 D 7 LYS B 32 GLY B 37 1 N GLY B 37 O ALA B 56
SHEET 3 D 7 ARG B 5 LEU B 10 1 N LEU B 10 O ALA B 36
SHEET 4 D 7 VAL B 69 LEU B 72 1 O VAL B 71 N LEU B 7
SHEET 5 D 7 LEU B 101 ILE B 105 1 O ALA B 103 N LEU B 72
SHEET 6 D 7 ILE B 152 SER B 155 1 O LEU B 153 N ILE B 102
SHEET 7 D 7 VAL B 146 ASP B 149 -1 N GLU B 147 O THR B 154
SHEET 1 E 2 LYS B 122 VAL B 123 0
SHEET 2 E 2 THR B 140 TYR B 141 1 O THR B 140 N VAL B 123
LINK C ILE B 52 N DYS B 53 1555 1555 1.33
LINK C DYS B 53 N PRO B 54 1555 1555 1.34
CISPEP 1 GLY A 65 PRO A 66 0 -0.01
CISPEP 2 GLY B 65 PRO B 66 0 0.13
CRYST1 75.468 75.468 75.504 90.00 90.00 120.00 P 31 3
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 0.013251 0.007650 0.000000 0.00000
SCALE2 0.000000 0.015301 0.000000 0.00000
SCALE3 0.000000 0.000000 0.013244 0.00000
(ATOM LINES ARE NOT SHOWN.)
END