HEADER UNKNOWN FUNCTION 01-AUG-12 4GE3
TITLE SCHIZOSACCHAROMYCES POMBE DJ-1 T114V MUTANT
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: UNCHARACTERIZED PROTEIN C22E12.03C;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 SYNONYM: DJ-1;
COMPND 5 ENGINEERED: YES;
COMPND 6 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: SCHIZOSACCHAROMYCES POMBE;
SOURCE 3 ORGANISM_COMMON: FISSION YEAST;
SOURCE 4 ORGANISM_TAXID: 4896;
SOURCE 5 GENE: SPAC22E12.03C;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET15B
KEYWDS DJ-1/PFPI FAMILY, UNKNOWN FUNCTION
EXPDTA X-RAY DIFFRACTION
AUTHOR P.MADZELAN,T.LABUNSKA,M.A.WILSON
REVDAT 6 13-SEP-23 4GE3 1 REMARK SEQADV LINK
REVDAT 5 15-NOV-17 4GE3 1 REMARK
REVDAT 4 19-NOV-14 4GE3 1 HET HETATM HETNAM HETSYN
REVDAT 3 19-DEC-12 4GE3 1 JRNL
REVDAT 2 26-SEP-12 4GE3 1 JRNL
REVDAT 1 15-AUG-12 4GE3 0
JRNL AUTH P.MADZELAN,T.LABUNSKA,M.A.WILSON
JRNL TITL INFLUENCE OF PEPTIDE DIPOLES AND HYDROGEN BONDS ON REACTIVE
JRNL TITL 2 CYSTEINE PK(A) VALUES IN FISSION YEAST DJ-1.
JRNL REF FEBS J. V. 279 4111 2012
JRNL REFN ISSN 1742-464X
JRNL PMID 22971103
JRNL DOI 10.1111/FEBS.12004
REMARK 2
REMARK 2 RESOLUTION. 1.50 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.6.0116
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.50
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 82.89
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 93.2
REMARK 3 NUMBER OF REFLECTIONS : 102117
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 + TEST SET) : 0.160
REMARK 3 R VALUE (WORKING SET) : 0.158
REMARK 3 FREE R VALUE : 0.189
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 5115
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 1.50
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.54
REMARK 3 REFLECTION IN BIN (WORKING SET) : 6687
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 86.59
REMARK 3 BIN R VALUE (WORKING SET) : 0.2720
REMARK 3 BIN FREE R VALUE SET COUNT : 386
REMARK 3 BIN FREE R VALUE : 0.3020
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 5936
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 14
REMARK 3 SOLVENT ATOMS : 875
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 16.40
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 19.17
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.05000
REMARK 3 B22 (A**2) : 0.42000
REMARK 3 B33 (A**2) : -0.66000
REMARK 3 B12 (A**2) : 0.24000
REMARK 3 B13 (A**2) : 0.34000
REMARK 3 B23 (A**2) : -0.16000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.080
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.080
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.046
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 2.448
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.972
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.960
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 6478 ; 0.014 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 8805 ; 1.504 ; 1.985
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 838 ; 6.155 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 253 ;37.304 ;25.020
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1180 ;12.536 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 23 ;16.594 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 957 ; 0.105 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 4899 ; 0.009 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 4
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 1 A 191
REMARK 3 ORIGIN FOR THE GROUP (A): 2.9024 12.5158 -1.6898
REMARK 3 T TENSOR
REMARK 3 T11: 0.0415 T22: 0.0274
REMARK 3 T33: 0.0646 T12: -0.0217
REMARK 3 T13: 0.0342 T23: -0.0165
REMARK 3 L TENSOR
REMARK 3 L11: 1.1204 L22: 1.4843
REMARK 3 L33: 2.7697 L12: -0.4586
REMARK 3 L13: -0.1362 L23: 1.0362
REMARK 3 S TENSOR
REMARK 3 S11: -0.1007 S12: 0.0691 S13: -0.1606
REMARK 3 S21: 0.1248 S22: -0.0277 S23: 0.1083
REMARK 3 S31: 0.2732 S32: -0.0448 S33: 0.1285
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 1 B 191
REMARK 3 ORIGIN FOR THE GROUP (A): 2.5278 32.5883 17.3821
REMARK 3 T TENSOR
REMARK 3 T11: 0.0768 T22: 0.0305
REMARK 3 T33: 0.0293 T12: 0.0073
REMARK 3 T13: -0.0048 T23: -0.0027
REMARK 3 L TENSOR
REMARK 3 L11: 0.9394 L22: 2.3087
REMARK 3 L33: 2.1893 L12: -0.3215
REMARK 3 L13: -0.5368 L23: 0.5599
REMARK 3 S TENSOR
REMARK 3 S11: -0.0724 S12: -0.1183 S13: 0.0861
REMARK 3 S21: 0.1796 S22: 0.0876 S23: -0.0765
REMARK 3 S31: -0.1622 S32: 0.0876 S33: -0.0152
REMARK 3
REMARK 3 TLS GROUP : 3
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : C 1 C 191
REMARK 3 ORIGIN FOR THE GROUP (A): 3.5030 42.7807 -23.5347
REMARK 3 T TENSOR
REMARK 3 T11: 0.0100 T22: 0.0404
REMARK 3 T33: 0.0205 T12: -0.0031
REMARK 3 T13: -0.0069 T23: 0.0241
REMARK 3 L TENSOR
REMARK 3 L11: 1.3133 L22: 0.9793
REMARK 3 L33: 1.5936 L12: -0.2585
REMARK 3 L13: 0.3822 L23: -0.2657
REMARK 3 S TENSOR
REMARK 3 S11: 0.0099 S12: -0.0860 S13: -0.0484
REMARK 3 S21: 0.0390 S22: -0.0082 S23: -0.0262
REMARK 3 S31: 0.0883 S32: 0.0750 S33: -0.0018
REMARK 3
REMARK 3 TLS GROUP : 4
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : D 1 D 191
REMARK 3 ORIGIN FOR THE GROUP (A): -12.5754 54.7130 -42.7032
REMARK 3 T TENSOR
REMARK 3 T11: 0.0299 T22: 0.0366
REMARK 3 T33: 0.0215 T12: 0.0024
REMARK 3 T13: -0.0133 T23: 0.0188
REMARK 3 L TENSOR
REMARK 3 L11: 1.2625 L22: 1.1556
REMARK 3 L33: 1.6723 L12: -0.4636
REMARK 3 L13: -0.2373 L23: 0.0982
REMARK 3 S TENSOR
REMARK 3 S11: 0.0347 S12: 0.0851 S13: 0.0375
REMARK 3 S21: -0.1570 S22: -0.0182 S23: 0.0624
REMARK 3 S31: -0.1099 S32: -0.1374 S33: -0.0165
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.20
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: TLS REFINEMENT WITH 4 GROUPS
REMARK 4
REMARK 4 4GE3 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 03-AUG-12.
REMARK 100 THE DEPOSITION ID IS D_1000074067.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 12-JUL-12
REMARK 200 TEMPERATURE (KELVIN) : 110
REMARK 200 PH : 7.4
REMARK 200 NUMBER OF CRYSTALS USED : 2
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : ROTATING ANODE
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : RIGAKU MICROMAX-007
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : OSMIC BLUE OPTIC
REMARK 200 OPTICS : OSMIC BLUE CONFOCAL
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : RIGAKU RAXIS IV
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 102613
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.500
REMARK 200 RESOLUTION RANGE LOW (A) : 83.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 93.4
REMARK 200 DATA REDUNDANCY : 5.400
REMARK 200 R MERGE (I) : 0.07200
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 16.6000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.50
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.55
REMARK 200 COMPLETENESS FOR SHELL (%) : 87.6
REMARK 200 DATA REDUNDANCY IN SHELL : 4.40
REMARK 200 R MERGE FOR SHELL (I) : 0.25300
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 5.900
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: RIGID BODY REFINEMENT OF 4GDH
REMARK 200 STARTING MODEL: 4GDH
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 40.32
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.06
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 26% PEG4000, 100 MM TRIS-HCL, 200 MM
REMARK 280 MAGNESIUM CHLORIDE, PH 7.4, VAPOR DIFFUSION, HANGING DROP,
REMARK 280 TEMPERATURE 298K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,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
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
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: 2770 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 14970 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -12.0 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: 3240 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 14960 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -12.0 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 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 GLY A -2
REMARK 465 SER A -1
REMARK 465 HIS A 0
REMARK 465 GLY B -2
REMARK 465 SER B -1
REMARK 465 HIS B 0
REMARK 465 GLY C -2
REMARK 465 SER C -1
REMARK 465 HIS C 0
REMARK 465 GLY D -2
REMARK 465 SER D -1
REMARK 465 HIS D 0
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 O HOH B 259 O HOH B 359 1.76
REMARK 500 NH1 ARG D 48 O HOH D 257 1.78
REMARK 500 O HOH A 341 O HOH A 511 1.83
REMARK 500 O HOH B 309 O HOH C 367 1.92
REMARK 500 O HOH B 336 O HOH B 366 1.98
REMARK 500 O HOH D 257 O HOH D 368 2.01
REMARK 500 NZ LYS C 170 O HOH C 556 2.01
REMARK 500 O HOH B 267 O HOH B 389 2.02
REMARK 500 CH2 TRP C 106 O HOH C 555 2.03
REMARK 500 O HOH A 473 O HOH A 506 2.04
REMARK 500 O HOH C 566 O HOH D 346 2.04
REMARK 500 O GLU A 138 O HOH A 475 2.04
REMARK 500 OD1 ASP B 179 O HOH B 306 2.08
REMARK 500 O HOH D 253 O HOH D 346 2.08
REMARK 500 O HOH D 304 O HOH D 381 2.10
REMARK 500 OG SER A 18 O HOH A 458 2.10
REMARK 500 O HOH D 339 O HOH D 380 2.11
REMARK 500 CB ASN B 124 O HOH B 378 2.11
REMARK 500 O HOH C 442 O HOH C 520 2.12
REMARK 500 O HOH B 386 O HOH B 395 2.12
REMARK 500 O HOH C 451 O HOH C 456 2.13
REMARK 500 O HOH C 479 O HOH D 268 2.13
REMARK 500 O HOH B 291 O HOH B 371 2.13
REMARK 500 O HOH B 389 O HOH C 358 2.13
REMARK 500 O GLU A 138 O HOH A 475 2.14
REMARK 500 O HOH D 338 O HOH D 352 2.14
REMARK 500 O HOH B 389 O HOH C 484 2.18
REMARK 500 O HOH C 347 O HOH D 253 2.18
REMARK 500
REMARK 500 REMARK: NULL
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 353 O HOH D 380 1656 2.12
REMARK 500 OE2 GLU C 38 O HOH A 507 1565 2.15
REMARK 500 O HOH B 388 O HOH D 380 1656 2.18
REMARK 500 O HOH B 374 O HOH D 380 1656 2.19
REMARK 500 N MET A 1 OD1 ASP C 41 1645 2.19
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 ASP A 49 2.65 85.35
REMARK 500 CSD A 111 -135.63 57.89
REMARK 500 GLU A 153 -117.64 50.34
REMARK 500 ASP B 49 5.71 86.40
REMARK 500 CSD B 111 -133.22 58.06
REMARK 500 GLU B 153 -119.28 52.14
REMARK 500 ASP C 49 5.86 83.40
REMARK 500 CSD C 111 -133.28 62.76
REMARK 500 GLU C 153 -119.76 49.95
REMARK 500 ASP D 49 4.46 85.71
REMARK 500 ASP D 49 4.46 85.32
REMARK 500 CSD D 111 -134.76 63.59
REMARK 500 GLU D 153 -121.91 50.55
REMARK 500
REMARK 500 REMARK: NULL
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG C 204 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH A 514 O
REMARK 620 2 HOH A 515 O 79.1
REMARK 620 3 HOH C 524 O 143.3 137.0
REMARK 620 4 HOH C 564 O 92.3 88.0 95.0
REMARK 620 5 HOH C 565 O 94.1 90.8 81.3 173.2
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG C 203 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH C 421 O
REMARK 620 2 HOH C 563 O 87.9
REMARK 620 3 HOH D 244 O 171.0 101.1
REMARK 620 4 HOH D 246 O 91.8 86.0 88.9
REMARK 620 N 1 2 3
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 201
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO C 201
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO C 202
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG C 203
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG C 204
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4GDN RELATED DB: PDB
REMARK 900 WILD-TYPE SCHIZOSACCHAROMYCES POMBE
REMARK 900 RELATED ID: 4GE0 RELATED DB: PDB
REMARK 900 SCHIZOSACCHAROMYCES POMBE DJ-1 T114P MUTANT
DBREF 4GE3 A 1 191 UNP Q10356 YDB3_SCHPO 1 191
DBREF 4GE3 B 1 191 UNP Q10356 YDB3_SCHPO 1 191
DBREF 4GE3 C 1 191 UNP Q10356 YDB3_SCHPO 1 191
DBREF 4GE3 D 1 191 UNP Q10356 YDB3_SCHPO 1 191
SEQADV 4GE3 GLY A -2 UNP Q10356 EXPRESSION TAG
SEQADV 4GE3 SER A -1 UNP Q10356 EXPRESSION TAG
SEQADV 4GE3 HIS A 0 UNP Q10356 EXPRESSION TAG
SEQADV 4GE3 VAL A 114 UNP Q10356 THR 114 ENGINEERED MUTATION
SEQADV 4GE3 GLY B -2 UNP Q10356 EXPRESSION TAG
SEQADV 4GE3 SER B -1 UNP Q10356 EXPRESSION TAG
SEQADV 4GE3 HIS B 0 UNP Q10356 EXPRESSION TAG
SEQADV 4GE3 VAL B 114 UNP Q10356 THR 114 ENGINEERED MUTATION
SEQADV 4GE3 GLY C -2 UNP Q10356 EXPRESSION TAG
SEQADV 4GE3 SER C -1 UNP Q10356 EXPRESSION TAG
SEQADV 4GE3 HIS C 0 UNP Q10356 EXPRESSION TAG
SEQADV 4GE3 VAL C 114 UNP Q10356 THR 114 ENGINEERED MUTATION
SEQADV 4GE3 GLY D -2 UNP Q10356 EXPRESSION TAG
SEQADV 4GE3 SER D -1 UNP Q10356 EXPRESSION TAG
SEQADV 4GE3 HIS D 0 UNP Q10356 EXPRESSION TAG
SEQADV 4GE3 VAL D 114 UNP Q10356 THR 114 ENGINEERED MUTATION
SEQRES 1 A 194 GLY SER HIS MET VAL LYS VAL CYS LEU PHE VAL ALA ASP
SEQRES 2 A 194 GLY THR ASP GLU ILE GLU PHE SER ALA PRO TRP GLY ILE
SEQRES 3 A 194 PHE LYS ARG ALA GLU ILE PRO ILE ASP SER VAL TYR VAL
SEQRES 4 A 194 GLY GLU ASN LYS ASP ARG LEU VAL LYS MET SER ARG ASP
SEQRES 5 A 194 VAL GLU MET TYR ALA ASN ARG SER TYR LYS GLU ILE PRO
SEQRES 6 A 194 SER ALA ASP ASP PHE ALA LYS GLN TYR ASP ILE ALA ILE
SEQRES 7 A 194 ILE PRO GLY GLY GLY LEU GLY ALA LYS THR LEU SER THR
SEQRES 8 A 194 THR PRO PHE VAL GLN GLN VAL VAL LYS GLU PHE TYR LYS
SEQRES 9 A 194 LYS PRO ASN LYS TRP ILE GLY MET ILE CSD ALA GLY VAL
SEQRES 10 A 194 LEU THR ALA LYS THR SER GLY LEU PRO ASN LYS GLN ILE
SEQRES 11 A 194 THR GLY HIS PRO SER VAL ARG GLY GLN LEU GLU GLU GLY
SEQRES 12 A 194 GLY TYR LYS TYR LEU ASP GLN PRO VAL VAL LEU GLU GLU
SEQRES 13 A 194 ASN LEU ILE THR SER GLN GLY PRO GLY THR ALA MET LEU
SEQRES 14 A 194 PHE GLY LEU LYS LEU LEU GLU GLN VAL ALA SER LYS ASP
SEQRES 15 A 194 LYS TYR ASN ALA VAL TYR LYS SER LEU SER MET PRO
SEQRES 1 B 194 GLY SER HIS MET VAL LYS VAL CYS LEU PHE VAL ALA ASP
SEQRES 2 B 194 GLY THR ASP GLU ILE GLU PHE SER ALA PRO TRP GLY ILE
SEQRES 3 B 194 PHE LYS ARG ALA GLU ILE PRO ILE ASP SER VAL TYR VAL
SEQRES 4 B 194 GLY GLU ASN LYS ASP ARG LEU VAL LYS MET SER ARG ASP
SEQRES 5 B 194 VAL GLU MET TYR ALA ASN ARG SER TYR LYS GLU ILE PRO
SEQRES 6 B 194 SER ALA ASP ASP PHE ALA LYS GLN TYR ASP ILE ALA ILE
SEQRES 7 B 194 ILE PRO GLY GLY GLY LEU GLY ALA LYS THR LEU SER THR
SEQRES 8 B 194 THR PRO PHE VAL GLN GLN VAL VAL LYS GLU PHE TYR LYS
SEQRES 9 B 194 LYS PRO ASN LYS TRP ILE GLY MET ILE CSD ALA GLY VAL
SEQRES 10 B 194 LEU THR ALA LYS THR SER GLY LEU PRO ASN LYS GLN ILE
SEQRES 11 B 194 THR GLY HIS PRO SER VAL ARG GLY GLN LEU GLU GLU GLY
SEQRES 12 B 194 GLY TYR LYS TYR LEU ASP GLN PRO VAL VAL LEU GLU GLU
SEQRES 13 B 194 ASN LEU ILE THR SER GLN GLY PRO GLY THR ALA MET LEU
SEQRES 14 B 194 PHE GLY LEU LYS LEU LEU GLU GLN VAL ALA SER LYS ASP
SEQRES 15 B 194 LYS TYR ASN ALA VAL TYR LYS SER LEU SER MET PRO
SEQRES 1 C 194 GLY SER HIS MET VAL LYS VAL CYS LEU PHE VAL ALA ASP
SEQRES 2 C 194 GLY THR ASP GLU ILE GLU PHE SER ALA PRO TRP GLY ILE
SEQRES 3 C 194 PHE LYS ARG ALA GLU ILE PRO ILE ASP SER VAL TYR VAL
SEQRES 4 C 194 GLY GLU ASN LYS ASP ARG LEU VAL LYS MET SER ARG ASP
SEQRES 5 C 194 VAL GLU MET TYR ALA ASN ARG SER TYR LYS GLU ILE PRO
SEQRES 6 C 194 SER ALA ASP ASP PHE ALA LYS GLN TYR ASP ILE ALA ILE
SEQRES 7 C 194 ILE PRO GLY GLY GLY LEU GLY ALA LYS THR LEU SER THR
SEQRES 8 C 194 THR PRO PHE VAL GLN GLN VAL VAL LYS GLU PHE TYR LYS
SEQRES 9 C 194 LYS PRO ASN LYS TRP ILE GLY MET ILE CSD ALA GLY VAL
SEQRES 10 C 194 LEU THR ALA LYS THR SER GLY LEU PRO ASN LYS GLN ILE
SEQRES 11 C 194 THR GLY HIS PRO SER VAL ARG GLY GLN LEU GLU GLU GLY
SEQRES 12 C 194 GLY TYR LYS TYR LEU ASP GLN PRO VAL VAL LEU GLU GLU
SEQRES 13 C 194 ASN LEU ILE THR SER GLN GLY PRO GLY THR ALA MET LEU
SEQRES 14 C 194 PHE GLY LEU LYS LEU LEU GLU GLN VAL ALA SER LYS ASP
SEQRES 15 C 194 LYS TYR ASN ALA VAL TYR LYS SER LEU SER MET PRO
SEQRES 1 D 194 GLY SER HIS MET VAL LYS VAL CYS LEU PHE VAL ALA ASP
SEQRES 2 D 194 GLY THR ASP GLU ILE GLU PHE SER ALA PRO TRP GLY ILE
SEQRES 3 D 194 PHE LYS ARG ALA GLU ILE PRO ILE ASP SER VAL TYR VAL
SEQRES 4 D 194 GLY GLU ASN LYS ASP ARG LEU VAL LYS MET SER ARG ASP
SEQRES 5 D 194 VAL GLU MET TYR ALA ASN ARG SER TYR LYS GLU ILE PRO
SEQRES 6 D 194 SER ALA ASP ASP PHE ALA LYS GLN TYR ASP ILE ALA ILE
SEQRES 7 D 194 ILE PRO GLY GLY GLY LEU GLY ALA LYS THR LEU SER THR
SEQRES 8 D 194 THR PRO PHE VAL GLN GLN VAL VAL LYS GLU PHE TYR LYS
SEQRES 9 D 194 LYS PRO ASN LYS TRP ILE GLY MET ILE CSD ALA GLY VAL
SEQRES 10 D 194 LEU THR ALA LYS THR SER GLY LEU PRO ASN LYS GLN ILE
SEQRES 11 D 194 THR GLY HIS PRO SER VAL ARG GLY GLN LEU GLU GLU GLY
SEQRES 12 D 194 GLY TYR LYS TYR LEU ASP GLN PRO VAL VAL LEU GLU GLU
SEQRES 13 D 194 ASN LEU ILE THR SER GLN GLY PRO GLY THR ALA MET LEU
SEQRES 14 D 194 PHE GLY LEU LYS LEU LEU GLU GLN VAL ALA SER LYS ASP
SEQRES 15 D 194 LYS TYR ASN ALA VAL TYR LYS SER LEU SER MET PRO
MODRES 4GE3 CSD A 111 CYS 3-SULFINOALANINE
MODRES 4GE3 CSD B 111 CYS 3-SULFINOALANINE
MODRES 4GE3 CSD C 111 CYS 3-SULFINOALANINE
MODRES 4GE3 CSD D 111 CYS 3-SULFINOALANINE
HET CSD A 111 8
HET CSD B 111 8
HET CSD C 111 8
HET CSD D 111 8
HET EDO A 201 4
HET EDO C 201 4
HET EDO C 202 4
HET MG C 203 1
HET MG C 204 1
HETNAM CSD 3-SULFINOALANINE
HETNAM EDO 1,2-ETHANEDIOL
HETNAM MG MAGNESIUM ION
HETSYN CSD S-CYSTEINESULFINIC ACID; S-SULFINOCYSTEINE
HETSYN EDO ETHYLENE GLYCOL
FORMUL 1 CSD 4(C3 H7 N O4 S)
FORMUL 5 EDO 3(C2 H6 O2)
FORMUL 8 MG 2(MG 2+)
FORMUL 10 HOH *875(H2 O)
HELIX 1 1 ASP A 13 ALA A 27 1 15
HELIX 2 2 LYS A 59 ILE A 61 5 3
HELIX 3 3 SER A 63 TYR A 71 1 9
HELIX 4 4 GLY A 79 THR A 88 1 10
HELIX 5 5 THR A 89 TYR A 100 1 12
HELIX 6 6 VAL A 114 GLY A 121 1 8
HELIX 7 7 HIS A 130 SER A 132 5 3
HELIX 8 8 VAL A 133 GLY A 140 1 8
HELIX 9 9 GLY A 160 GLY A 162 5 3
HELIX 10 10 THR A 163 ALA A 176 1 14
HELIX 11 11 SER A 177 LEU A 188 1 12
HELIX 12 12 ASP B 13 ALA B 27 1 15
HELIX 13 13 LYS B 59 ILE B 61 5 3
HELIX 14 14 SER B 63 TYR B 71 1 9
HELIX 15 15 GLY B 79 THR B 89 1 11
HELIX 16 16 THR B 89 TYR B 100 1 12
HELIX 17 17 VAL B 114 SER B 120 1 7
HELIX 18 18 HIS B 130 SER B 132 5 3
HELIX 19 19 VAL B 133 GLY B 140 1 8
HELIX 20 20 GLY B 160 GLY B 162 5 3
HELIX 21 21 THR B 163 GLN B 174 1 12
HELIX 22 22 SER B 177 LEU B 188 1 12
HELIX 23 23 ASP C 13 ALA C 27 1 15
HELIX 24 24 LYS C 59 ILE C 61 5 3
HELIX 25 25 SER C 63 TYR C 71 1 9
HELIX 26 26 GLY C 79 THR C 89 1 11
HELIX 27 27 THR C 89 TYR C 100 1 12
HELIX 28 28 VAL C 114 SER C 120 1 7
HELIX 29 29 HIS C 130 SER C 132 5 3
HELIX 30 30 VAL C 133 GLY C 140 1 8
HELIX 31 31 GLY C 160 GLY C 162 5 3
HELIX 32 32 THR C 163 ALA C 176 1 14
HELIX 33 33 SER C 177 LEU C 188 1 12
HELIX 34 34 ASP D 13 ALA D 27 1 15
HELIX 35 35 LYS D 59 ILE D 61 5 3
HELIX 36 36 SER D 63 TYR D 71 1 9
HELIX 37 37 GLY D 79 THR D 88 1 10
HELIX 38 38 THR D 89 TYR D 100 1 12
HELIX 39 39 VAL D 114 SER D 120 1 7
HELIX 40 40 HIS D 130 SER D 132 5 3
HELIX 41 41 VAL D 133 GLY D 140 1 8
HELIX 42 42 GLY D 160 GLY D 162 5 3
HELIX 43 43 THR D 163 GLN D 174 1 12
HELIX 44 44 SER D 177 LEU D 188 1 12
SHEET 1 A 7 ARG A 56 SER A 57 0
SHEET 2 A 7 ILE A 31 VAL A 36 1 N TYR A 35 O ARG A 56
SHEET 3 A 7 VAL A 4 ALA A 9 1 N LEU A 6 O ASP A 32
SHEET 4 A 7 ILE A 73 ILE A 76 1 O ILE A 73 N CYS A 5
SHEET 5 A 7 TRP A 106 ILE A 110 1 O GLY A 108 N ILE A 76
SHEET 6 A 7 LEU A 155 SER A 158 1 O ILE A 156 N ILE A 107
SHEET 7 A 7 VAL A 149 GLU A 152 -1 N GLU A 152 O LEU A 155
SHEET 1 B 4 LEU A 43 LYS A 45 0
SHEET 2 B 4 GLU A 51 TYR A 53 -1 O MET A 52 N VAL A 44
SHEET 3 B 4 GLU B 51 TYR B 53 -1 O GLU B 51 N TYR A 53
SHEET 4 B 4 LEU B 43 LYS B 45 -1 N VAL B 44 O MET B 52
SHEET 1 C 2 GLN A 126 ILE A 127 0
SHEET 2 C 2 LYS A 143 TYR A 144 1 O LYS A 143 N ILE A 127
SHEET 1 D 7 ARG B 56 SER B 57 0
SHEET 2 D 7 ILE B 31 VAL B 36 1 N TYR B 35 O ARG B 56
SHEET 3 D 7 VAL B 4 ALA B 9 1 N LEU B 6 O ASP B 32
SHEET 4 D 7 ILE B 73 ILE B 76 1 O ILE B 73 N CYS B 5
SHEET 5 D 7 TRP B 106 ILE B 110 1 O GLY B 108 N ILE B 76
SHEET 6 D 7 LEU B 155 SER B 158 1 O ILE B 156 N ILE B 107
SHEET 7 D 7 VAL B 149 GLU B 152 -1 N VAL B 150 O THR B 157
SHEET 1 E 2 GLN B 126 ILE B 127 0
SHEET 2 E 2 LYS B 143 TYR B 144 1 O LYS B 143 N ILE B 127
SHEET 1 F 7 ARG C 56 SER C 57 0
SHEET 2 F 7 ILE C 31 VAL C 36 1 N TYR C 35 O ARG C 56
SHEET 3 F 7 VAL C 4 ALA C 9 1 N LEU C 6 O ASP C 32
SHEET 4 F 7 ILE C 73 ILE C 76 1 O ILE C 73 N CYS C 5
SHEET 5 F 7 TRP C 106 ILE C 110 1 O GLY C 108 N ILE C 76
SHEET 6 F 7 LEU C 155 SER C 158 1 O ILE C 156 N ILE C 107
SHEET 7 F 7 VAL C 149 GLU C 152 -1 N VAL C 150 O THR C 157
SHEET 1 G 4 LEU C 43 LYS C 45 0
SHEET 2 G 4 GLU C 51 TYR C 53 -1 O MET C 52 N VAL C 44
SHEET 3 G 4 GLU D 51 TYR D 53 -1 O TYR D 53 N GLU C 51
SHEET 4 G 4 LEU D 43 LYS D 45 -1 N VAL D 44 O MET D 52
SHEET 1 H 2 GLN C 126 ILE C 127 0
SHEET 2 H 2 LYS C 143 TYR C 144 1 O LYS C 143 N ILE C 127
SHEET 1 I 7 ARG D 56 SER D 57 0
SHEET 2 I 7 ILE D 31 VAL D 36 1 N TYR D 35 O ARG D 56
SHEET 3 I 7 VAL D 4 ALA D 9 1 N LEU D 6 O ASP D 32
SHEET 4 I 7 ILE D 73 ILE D 76 1 O ILE D 73 N CYS D 5
SHEET 5 I 7 TRP D 106 ILE D 110 1 O GLY D 108 N ILE D 76
SHEET 6 I 7 LEU D 155 SER D 158 1 O ILE D 156 N ILE D 107
SHEET 7 I 7 VAL D 149 GLU D 152 -1 N VAL D 150 O THR D 157
SHEET 1 J 2 GLN D 126 ILE D 127 0
SHEET 2 J 2 LYS D 143 TYR D 144 1 O LYS D 143 N ILE D 127
LINK C ILE A 110 N CSD A 111 1555 1555 1.34
LINK C CSD A 111 N ALA A 112 1555 1555 1.33
LINK C ILE B 110 N CSD B 111 1555 1555 1.33
LINK C CSD B 111 N ALA B 112 1555 1555 1.34
LINK C ILE C 110 N CSD C 111 1555 1555 1.35
LINK C CSD C 111 N ALA C 112 1555 1555 1.33
LINK C ILE D 110 N CSD D 111 1555 1555 1.34
LINK C CSD D 111 N ALA D 112 1555 1555 1.33
LINK O HOH A 514 MG MG C 204 1555 1555 2.11
LINK O HOH A 515 MG MG C 204 1555 1555 2.06
LINK MG MG C 203 O HOH C 421 1555 1555 1.99
LINK MG MG C 203 O HOH C 563 1555 1555 2.27
LINK MG MG C 203 O HOH D 244 1555 1555 2.09
LINK MG MG C 203 O HOH D 246 1555 1555 2.23
LINK MG MG C 204 O HOH C 524 1555 1555 1.98
LINK MG MG C 204 O HOH C 564 1555 1555 2.15
LINK MG MG C 204 O HOH C 565 1555 1555 1.95
SITE 1 AC1 4 LYS A 84 ASP A 179 HOH A 311 HOH A 396
SITE 1 AC2 7 GLU C 14 PHE C 17 SER C 18 MET C 46
SITE 2 AC2 7 HOH C 502 SER D 18 HOH D 310
SITE 1 AC3 8 PHE C 17 TRP C 21 SER C 33 MET C 52
SITE 2 AC3 8 TYR C 53 ASN C 55 VAL D 50 GLU D 51
SITE 1 AC4 4 HOH C 421 HOH C 563 HOH D 244 HOH D 246
SITE 1 AC5 5 HOH A 514 HOH A 515 HOH C 524 HOH C 564
SITE 2 AC5 5 HOH C 565
CRYST1 44.579 52.075 82.912 89.01 88.98 66.55 P 1 4
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 0.022432 -0.009730 -0.000291 0.00000
SCALE2 0.000000 0.020932 -0.000233 0.00000
SCALE3 0.000000 0.000000 0.012064 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
