HEADER PROTEIN BINDING 12-MAY-08 3D3K
TITLE CRYSTAL STRUCTURE OF HUMAN EDC3P
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ENHANCER OF MRNA-DECAPPING PROTEIN 3;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 FRAGMENT: C-TERMINAL, UNP RESIDUES 250-508;
COMPND 5 SYNONYM: YJEF DOMAIN-CONTAINING PROTEIN 1, LSM16 HOMOLOG;
COMPND 6 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: EDC3;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PGEX6P1
KEYWDS HEDC3, PHOSPHOPROTEIN, PROTEIN BINDING
EXPDTA X-RAY DIFFRACTION
AUTHOR S.H.M.LING
REVDAT 5 20-MAR-24 3D3K 1 REMARK
REVDAT 4 13-JUL-11 3D3K 1 VERSN
REVDAT 3 24-FEB-09 3D3K 1 VERSN
REVDAT 2 07-OCT-08 3D3K 1 JRNL
REVDAT 1 26-AUG-08 3D3K 0
JRNL AUTH S.H.M.LING,C.J.DECKER,M.A.WALSH,M.SHE,R.PARKER,H.SONG
JRNL TITL CRYSTAL STRUCTURE OF HUMAN EDC3 AND ITS FUNCTIONAL
JRNL TITL 2 IMPLICATIONS
JRNL REF MOL.CELL.BIOL. V. 28 5965 2008
JRNL REFN ISSN 0270-7306
JRNL PMID 18678652
JRNL DOI 10.1128/MCB.00761-08
REMARK 2
REMARK 2 RESOLUTION. 2.20 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.2.0019
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) : 2.20
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 20.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 3 NUMBER OF REFLECTIONS : 63120
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) : 0.229
REMARK 3 R VALUE (WORKING SET) : 0.228
REMARK 3 FREE R VALUE : 0.256
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 3376
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) : 2.20
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.26
REMARK 3 REFLECTION IN BIN (WORKING SET) : 4556
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 100.0
REMARK 3 BIN R VALUE (WORKING SET) : 0.2530
REMARK 3 BIN FREE R VALUE SET COUNT : 252
REMARK 3 BIN FREE R VALUE : 0.2970
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 7208
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 348
REMARK 3
REMARK 3 B VALUES.
REMARK 3 B VALUE TYPE : LIKELY RESIDUAL
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 28.36
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -1.78000
REMARK 3 B22 (A**2) : 0.79000
REMARK 3 B33 (A**2) : 0.99000
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 OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.244
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.198
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.135
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 10.267
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.942
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.930
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 7380 ; 0.008 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 10036 ; 1.102 ; 1.978
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 916 ; 5.734 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 292 ;32.509 ;24.110
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1236 ;14.739 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 36 ;12.068 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1160 ; 0.076 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 5492 ; 0.003 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 3263 ; 0.186 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 4957 ; 0.298 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 413 ; 0.119 ; 0.200
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): 67 ; 0.141 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 18 ; 0.175 ; 0.200
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): 4845 ; 0.557 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 7552 ; 0.970 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 2910 ; 1.223 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 2484 ; 1.961 ; 4.500
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 : 1
REMARK 3
REMARK 3 NCS GROUP NUMBER : 1
REMARK 3 CHAIN NAMES : A D
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 1
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 A 258 A 506 4
REMARK 3 1 D 258 D 506 4
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 MEDIUM POSITIONAL 1 A (A): 1796 ; 0.32 ; 0.50
REMARK 3 MEDIUM THERMAL 1 A (A**2): 1796 ; 0.44 ; 2.00
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 : 4
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 258 A 264
REMARK 3 RESIDUE RANGE : A 268 A 323
REMARK 3 RESIDUE RANGE : A 333 A 447
REMARK 3 RESIDUE RANGE : A 453 A 507
REMARK 3 ORIGIN FOR THE GROUP (A): 13.7756 39.4744 67.3719
REMARK 3 T TENSOR
REMARK 3 T11: -0.0691 T22: 0.0218
REMARK 3 T33: -0.0380 T12: -0.0039
REMARK 3 T13: 0.0075 T23: 0.0025
REMARK 3 L TENSOR
REMARK 3 L11: 1.4544 L22: 1.9480
REMARK 3 L33: 0.7524 L12: 1.1078
REMARK 3 L13: -0.3649 L23: -0.3860
REMARK 3 S TENSOR
REMARK 3 S11: -0.0407 S12: -0.1311 S13: -0.1706
REMARK 3 S21: -0.0150 S22: 0.0172 S23: -0.2043
REMARK 3 S31: 0.0537 S32: 0.2341 S33: 0.0235
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 NUMBER OF COMPONENTS GROUP : 4
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 258 B 264
REMARK 3 RESIDUE RANGE : B 268 B 323
REMARK 3 RESIDUE RANGE : B 333 B 447
REMARK 3 RESIDUE RANGE : B 453 B 507
REMARK 3 ORIGIN FOR THE GROUP (A): -13.7707 42.4031 67.3870
REMARK 3 T TENSOR
REMARK 3 T11: -0.0583 T22: -0.0281
REMARK 3 T33: -0.0272 T12: -0.0175
REMARK 3 T13: -0.0097 T23: 0.0117
REMARK 3 L TENSOR
REMARK 3 L11: 1.1876 L22: 1.4365
REMARK 3 L33: 0.6325 L12: 0.9203
REMARK 3 L13: 0.1480 L23: 0.3887
REMARK 3 S TENSOR
REMARK 3 S11: -0.0058 S12: -0.0278 S13: 0.1063
REMARK 3 S21: -0.0419 S22: -0.0176 S23: 0.1461
REMARK 3 S31: -0.0057 S32: -0.0828 S33: 0.0234
REMARK 3
REMARK 3 TLS GROUP : 3
REMARK 3 NUMBER OF COMPONENTS GROUP : 4
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : C 258 C 264
REMARK 3 RESIDUE RANGE : C 268 C 323
REMARK 3 RESIDUE RANGE : C 333 C 447
REMARK 3 RESIDUE RANGE : C 453 C 507
REMARK 3 ORIGIN FOR THE GROUP (A): 33.3496 68.9602 41.4316
REMARK 3 T TENSOR
REMARK 3 T11: -0.0857 T22: -0.0469
REMARK 3 T33: 0.0059 T12: -0.0147
REMARK 3 T13: 0.0117 T23: -0.0137
REMARK 3 L TENSOR
REMARK 3 L11: 0.9743 L22: 0.4759
REMARK 3 L33: 2.1458 L12: 0.1275
REMARK 3 L13: -0.8774 L23: -0.5655
REMARK 3 S TENSOR
REMARK 3 S11: -0.0438 S12: 0.0575 S13: 0.0274
REMARK 3 S21: -0.0279 S22: -0.0022 S23: 0.0665
REMARK 3 S31: 0.1203 S32: -0.0960 S33: 0.0461
REMARK 3
REMARK 3 TLS GROUP : 4
REMARK 3 NUMBER OF COMPONENTS GROUP : 4
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : D 258 D 264
REMARK 3 RESIDUE RANGE : D 268 D 323
REMARK 3 RESIDUE RANGE : D 333 D 447
REMARK 3 RESIDUE RANGE : D 453 D 507
REMARK 3 ORIGIN FOR THE GROUP (A): -33.3634 12.9482 41.4171
REMARK 3 T TENSOR
REMARK 3 T11: -0.0996 T22: -0.0559
REMARK 3 T33: 0.0006 T12: -0.0147
REMARK 3 T13: -0.0100 T23: 0.0080
REMARK 3 L TENSOR
REMARK 3 L11: 1.1813 L22: 0.6304
REMARK 3 L33: 2.2445 L12: 0.1703
REMARK 3 L13: 0.9319 L23: 0.5788
REMARK 3 S TENSOR
REMARK 3 S11: -0.0497 S12: 0.0801 S13: 0.0041
REMARK 3 S21: -0.0258 S22: 0.0154 S23: -0.0613
REMARK 3 S31: -0.1380 S32: 0.0928 S33: 0.0343
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.40
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS
REMARK 4
REMARK 4 3D3K COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 15-MAY-08.
REMARK 100 THE DEPOSITION ID IS D_1000047547.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : NULL
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 5.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : BM14
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9798
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 225 MM CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 63120
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.200
REMARK 200 RESOLUTION RANGE LOW (A) : NULL
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : NULL
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) : 2.20
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: SAD
REMARK 200 SOFTWARE USED: SNB
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 56.93
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.86
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 6000, SODIUM CITRATE, PH 5.0,
REMARK 280 VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z+1/2
REMARK 290 3555 -X,Y,-Z+1/2
REMARK 290 4555 X,-Y,-Z
REMARK 290 5555 X+1/2,Y+1/2,Z
REMARK 290 6555 -X+1/2,-Y+1/2,Z+1/2
REMARK 290 7555 -X+1/2,Y+1/2,-Z+1/2
REMARK 290 8555 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 81.80450
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 81.80450
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 47.18850
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 84.60200
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 47.18850
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 84.60200
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 81.80450
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 47.18850
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 84.60200
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 81.80450
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 47.18850
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 84.60200
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3
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: 3760 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 19780 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -7.0 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: 3750 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 19720 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -6.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 350 BIOMT1 2 -1.000000 0.000000 0.000000 94.37700
REMARK 350 BIOMT2 2 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 81.80450
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: 3720 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 19640 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -6.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 BIOMT1 2 -1.000000 0.000000 0.000000 -94.37700
REMARK 350 BIOMT2 2 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 81.80450
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 ILE A 250
REMARK 465 LEU A 251
REMARK 465 GLU A 252
REMARK 465 SER A 253
REMARK 465 GLU A 254
REMARK 465 PRO A 255
REMARK 465 ILE A 256
REMARK 465 VAL A 257
REMARK 465 HIS A 265
REMARK 465 ASN A 266
REMARK 465 VAL A 267
REMARK 465 ASN A 324
REMARK 465 ARG A 325
REMARK 465 LEU A 326
REMARK 465 ASN A 327
REMARK 465 PRO A 328
REMARK 465 LYS A 329
REMARK 465 ASN A 330
REMARK 465 VAL A 331
REMARK 465 HIS A 332
REMARK 465 GLU A 448
REMARK 465 VAL A 449
REMARK 465 GLU A 450
REMARK 465 GLN A 451
REMARK 465 GLY A 452
REMARK 465 ALA A 508
REMARK 465 ILE B 250
REMARK 465 LEU B 251
REMARK 465 GLU B 252
REMARK 465 SER B 253
REMARK 465 GLU B 254
REMARK 465 PRO B 255
REMARK 465 ILE B 256
REMARK 465 VAL B 257
REMARK 465 HIS B 265
REMARK 465 ASN B 266
REMARK 465 VAL B 267
REMARK 465 ASN B 324
REMARK 465 ARG B 325
REMARK 465 LEU B 326
REMARK 465 ASN B 327
REMARK 465 PRO B 328
REMARK 465 LYS B 329
REMARK 465 ASN B 330
REMARK 465 VAL B 331
REMARK 465 HIS B 332
REMARK 465 GLU B 448
REMARK 465 VAL B 449
REMARK 465 GLU B 450
REMARK 465 GLN B 451
REMARK 465 GLY B 452
REMARK 465 ALA B 508
REMARK 465 ILE C 250
REMARK 465 LEU C 251
REMARK 465 GLU C 252
REMARK 465 SER C 253
REMARK 465 GLU C 254
REMARK 465 PRO C 255
REMARK 465 ILE C 256
REMARK 465 VAL C 257
REMARK 465 HIS C 265
REMARK 465 ASN C 266
REMARK 465 VAL C 267
REMARK 465 ASN C 324
REMARK 465 ARG C 325
REMARK 465 LEU C 326
REMARK 465 ASN C 327
REMARK 465 PRO C 328
REMARK 465 LYS C 329
REMARK 465 ASN C 330
REMARK 465 VAL C 331
REMARK 465 HIS C 332
REMARK 465 GLU C 448
REMARK 465 VAL C 449
REMARK 465 GLU C 450
REMARK 465 GLN C 451
REMARK 465 GLY C 452
REMARK 465 ALA C 508
REMARK 465 ILE D 250
REMARK 465 LEU D 251
REMARK 465 GLU D 252
REMARK 465 SER D 253
REMARK 465 GLU D 254
REMARK 465 PRO D 255
REMARK 465 ILE D 256
REMARK 465 VAL D 257
REMARK 465 HIS D 265
REMARK 465 ASN D 266
REMARK 465 VAL D 267
REMARK 465 ASN D 324
REMARK 465 ARG D 325
REMARK 465 LEU D 326
REMARK 465 ASN D 327
REMARK 465 PRO D 328
REMARK 465 LYS D 329
REMARK 465 ASN D 330
REMARK 465 VAL D 331
REMARK 465 HIS D 332
REMARK 465 GLU D 448
REMARK 465 VAL D 449
REMARK 465 GLU D 450
REMARK 465 GLN D 451
REMARK 465 GLY D 452
REMARK 465 ALA D 508
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 ARG A 436 -11.68 92.42
REMARK 500 ARG B 436 -21.61 86.77
REMARK 500 ARG C 436 -14.70 87.81
REMARK 500 ARG D 436 59.07 28.05
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3D3J RELATED DB: PDB
REMARK 900 HEDC3_203C
DBREF 3D3K A 250 508 UNP Q96F86 EDC3_HUMAN 250 508
DBREF 3D3K B 250 508 UNP Q96F86 EDC3_HUMAN 250 508
DBREF 3D3K C 250 508 UNP Q96F86 EDC3_HUMAN 250 508
DBREF 3D3K D 250 508 UNP Q96F86 EDC3_HUMAN 250 508
SEQRES 1 A 259 ILE LEU GLU SER GLU PRO ILE VAL TYR ARG ARG ILE ILE
SEQRES 2 A 259 VAL PRO HIS ASN VAL SER LYS GLU PHE CYS THR ASP SER
SEQRES 3 A 259 GLY LEU VAL VAL PRO SER ILE SER TYR GLU LEU HIS LYS
SEQRES 4 A 259 LYS LEU LEU SER VAL ALA GLU LYS HIS GLY LEU THR LEU
SEQRES 5 A 259 GLU ARG ARG LEU GLU MET THR GLY VAL CYS ALA SER GLN
SEQRES 6 A 259 MET ALA LEU THR LEU LEU GLY GLY PRO ASN ARG LEU ASN
SEQRES 7 A 259 PRO LYS ASN VAL HIS GLN ARG PRO THR VAL ALA LEU LEU
SEQRES 8 A 259 CYS GLY PRO HIS VAL LYS GLY ALA GLN GLY ILE SER CYS
SEQRES 9 A 259 GLY ARG HIS LEU ALA ASN HIS ASP VAL GLN VAL ILE LEU
SEQRES 10 A 259 PHE LEU PRO ASN PHE VAL LYS MET LEU GLU SER ILE THR
SEQRES 11 A 259 ASN GLU LEU SER LEU PHE SER LYS THR GLN GLY GLN GLN
SEQRES 12 A 259 VAL SER SER LEU LYS ASP LEU PRO THR SER PRO VAL ASP
SEQRES 13 A 259 LEU VAL ILE ASN CYS LEU ASP CYS PRO GLU ASN VAL PHE
SEQRES 14 A 259 LEU ARG ASP GLN PRO TRP TYR LYS ALA ALA VAL ALA TRP
SEQRES 15 A 259 ALA ASN GLN ASN ARG ALA PRO VAL LEU SER ILE ASP PRO
SEQRES 16 A 259 PRO VAL HIS GLU VAL GLU GLN GLY ILE ASP ALA LYS TRP
SEQRES 17 A 259 SER LEU ALA LEU GLY LEU PRO LEU PRO LEU GLY GLU HIS
SEQRES 18 A 259 ALA GLY ARG ILE TYR LEU CYS ASP ILE GLY ILE PRO GLN
SEQRES 19 A 259 GLN VAL PHE GLN GLU VAL GLY ILE ASN TYR HIS SER PRO
SEQRES 20 A 259 PHE GLY CYS LYS PHE VAL ILE PRO LEU HIS SER ALA
SEQRES 1 B 259 ILE LEU GLU SER GLU PRO ILE VAL TYR ARG ARG ILE ILE
SEQRES 2 B 259 VAL PRO HIS ASN VAL SER LYS GLU PHE CYS THR ASP SER
SEQRES 3 B 259 GLY LEU VAL VAL PRO SER ILE SER TYR GLU LEU HIS LYS
SEQRES 4 B 259 LYS LEU LEU SER VAL ALA GLU LYS HIS GLY LEU THR LEU
SEQRES 5 B 259 GLU ARG ARG LEU GLU MET THR GLY VAL CYS ALA SER GLN
SEQRES 6 B 259 MET ALA LEU THR LEU LEU GLY GLY PRO ASN ARG LEU ASN
SEQRES 7 B 259 PRO LYS ASN VAL HIS GLN ARG PRO THR VAL ALA LEU LEU
SEQRES 8 B 259 CYS GLY PRO HIS VAL LYS GLY ALA GLN GLY ILE SER CYS
SEQRES 9 B 259 GLY ARG HIS LEU ALA ASN HIS ASP VAL GLN VAL ILE LEU
SEQRES 10 B 259 PHE LEU PRO ASN PHE VAL LYS MET LEU GLU SER ILE THR
SEQRES 11 B 259 ASN GLU LEU SER LEU PHE SER LYS THR GLN GLY GLN GLN
SEQRES 12 B 259 VAL SER SER LEU LYS ASP LEU PRO THR SER PRO VAL ASP
SEQRES 13 B 259 LEU VAL ILE ASN CYS LEU ASP CYS PRO GLU ASN VAL PHE
SEQRES 14 B 259 LEU ARG ASP GLN PRO TRP TYR LYS ALA ALA VAL ALA TRP
SEQRES 15 B 259 ALA ASN GLN ASN ARG ALA PRO VAL LEU SER ILE ASP PRO
SEQRES 16 B 259 PRO VAL HIS GLU VAL GLU GLN GLY ILE ASP ALA LYS TRP
SEQRES 17 B 259 SER LEU ALA LEU GLY LEU PRO LEU PRO LEU GLY GLU HIS
SEQRES 18 B 259 ALA GLY ARG ILE TYR LEU CYS ASP ILE GLY ILE PRO GLN
SEQRES 19 B 259 GLN VAL PHE GLN GLU VAL GLY ILE ASN TYR HIS SER PRO
SEQRES 20 B 259 PHE GLY CYS LYS PHE VAL ILE PRO LEU HIS SER ALA
SEQRES 1 C 259 ILE LEU GLU SER GLU PRO ILE VAL TYR ARG ARG ILE ILE
SEQRES 2 C 259 VAL PRO HIS ASN VAL SER LYS GLU PHE CYS THR ASP SER
SEQRES 3 C 259 GLY LEU VAL VAL PRO SER ILE SER TYR GLU LEU HIS LYS
SEQRES 4 C 259 LYS LEU LEU SER VAL ALA GLU LYS HIS GLY LEU THR LEU
SEQRES 5 C 259 GLU ARG ARG LEU GLU MET THR GLY VAL CYS ALA SER GLN
SEQRES 6 C 259 MET ALA LEU THR LEU LEU GLY GLY PRO ASN ARG LEU ASN
SEQRES 7 C 259 PRO LYS ASN VAL HIS GLN ARG PRO THR VAL ALA LEU LEU
SEQRES 8 C 259 CYS GLY PRO HIS VAL LYS GLY ALA GLN GLY ILE SER CYS
SEQRES 9 C 259 GLY ARG HIS LEU ALA ASN HIS ASP VAL GLN VAL ILE LEU
SEQRES 10 C 259 PHE LEU PRO ASN PHE VAL LYS MET LEU GLU SER ILE THR
SEQRES 11 C 259 ASN GLU LEU SER LEU PHE SER LYS THR GLN GLY GLN GLN
SEQRES 12 C 259 VAL SER SER LEU LYS ASP LEU PRO THR SER PRO VAL ASP
SEQRES 13 C 259 LEU VAL ILE ASN CYS LEU ASP CYS PRO GLU ASN VAL PHE
SEQRES 14 C 259 LEU ARG ASP GLN PRO TRP TYR LYS ALA ALA VAL ALA TRP
SEQRES 15 C 259 ALA ASN GLN ASN ARG ALA PRO VAL LEU SER ILE ASP PRO
SEQRES 16 C 259 PRO VAL HIS GLU VAL GLU GLN GLY ILE ASP ALA LYS TRP
SEQRES 17 C 259 SER LEU ALA LEU GLY LEU PRO LEU PRO LEU GLY GLU HIS
SEQRES 18 C 259 ALA GLY ARG ILE TYR LEU CYS ASP ILE GLY ILE PRO GLN
SEQRES 19 C 259 GLN VAL PHE GLN GLU VAL GLY ILE ASN TYR HIS SER PRO
SEQRES 20 C 259 PHE GLY CYS LYS PHE VAL ILE PRO LEU HIS SER ALA
SEQRES 1 D 259 ILE LEU GLU SER GLU PRO ILE VAL TYR ARG ARG ILE ILE
SEQRES 2 D 259 VAL PRO HIS ASN VAL SER LYS GLU PHE CYS THR ASP SER
SEQRES 3 D 259 GLY LEU VAL VAL PRO SER ILE SER TYR GLU LEU HIS LYS
SEQRES 4 D 259 LYS LEU LEU SER VAL ALA GLU LYS HIS GLY LEU THR LEU
SEQRES 5 D 259 GLU ARG ARG LEU GLU MET THR GLY VAL CYS ALA SER GLN
SEQRES 6 D 259 MET ALA LEU THR LEU LEU GLY GLY PRO ASN ARG LEU ASN
SEQRES 7 D 259 PRO LYS ASN VAL HIS GLN ARG PRO THR VAL ALA LEU LEU
SEQRES 8 D 259 CYS GLY PRO HIS VAL LYS GLY ALA GLN GLY ILE SER CYS
SEQRES 9 D 259 GLY ARG HIS LEU ALA ASN HIS ASP VAL GLN VAL ILE LEU
SEQRES 10 D 259 PHE LEU PRO ASN PHE VAL LYS MET LEU GLU SER ILE THR
SEQRES 11 D 259 ASN GLU LEU SER LEU PHE SER LYS THR GLN GLY GLN GLN
SEQRES 12 D 259 VAL SER SER LEU LYS ASP LEU PRO THR SER PRO VAL ASP
SEQRES 13 D 259 LEU VAL ILE ASN CYS LEU ASP CYS PRO GLU ASN VAL PHE
SEQRES 14 D 259 LEU ARG ASP GLN PRO TRP TYR LYS ALA ALA VAL ALA TRP
SEQRES 15 D 259 ALA ASN GLN ASN ARG ALA PRO VAL LEU SER ILE ASP PRO
SEQRES 16 D 259 PRO VAL HIS GLU VAL GLU GLN GLY ILE ASP ALA LYS TRP
SEQRES 17 D 259 SER LEU ALA LEU GLY LEU PRO LEU PRO LEU GLY GLU HIS
SEQRES 18 D 259 ALA GLY ARG ILE TYR LEU CYS ASP ILE GLY ILE PRO GLN
SEQRES 19 D 259 GLN VAL PHE GLN GLU VAL GLY ILE ASN TYR HIS SER PRO
SEQRES 20 D 259 PHE GLY CYS LYS PHE VAL ILE PRO LEU HIS SER ALA
FORMUL 5 HOH *348(H2 O)
HELIX 1 1 SER A 283 HIS A 297 1 15
HELIX 2 2 THR A 300 LEU A 320 1 21
HELIX 3 3 HIS A 344 HIS A 360 1 17
HELIX 4 4 LEU A 375 SER A 386 1 12
HELIX 5 5 SER A 395 LEU A 399 5 5
HELIX 6 6 PHE A 418 ASP A 421 5 4
HELIX 7 7 GLN A 422 ARG A 436 1 15
HELIX 8 8 GLY A 468 GLY A 472 5 5
HELIX 9 9 PRO A 482 VAL A 489 1 8
HELIX 10 10 SER B 283 HIS B 297 1 15
HELIX 11 11 THR B 300 LEU B 320 1 21
HELIX 12 12 HIS B 344 HIS B 360 1 17
HELIX 13 13 LEU B 375 SER B 386 1 12
HELIX 14 14 SER B 395 LEU B 399 5 5
HELIX 15 15 PHE B 418 ASP B 421 5 4
HELIX 16 16 GLN B 422 ARG B 436 1 15
HELIX 17 17 GLY B 468 GLY B 472 5 5
HELIX 18 18 PRO B 482 VAL B 489 1 8
HELIX 19 19 SER C 283 HIS C 297 1 15
HELIX 20 20 THR C 300 LEU C 320 1 21
HELIX 21 21 HIS C 344 HIS C 360 1 17
HELIX 22 22 LEU C 375 SER C 386 1 12
HELIX 23 23 SER C 395 LEU C 399 5 5
HELIX 24 24 ASN C 416 ASP C 421 5 6
HELIX 25 25 GLN C 422 ARG C 436 1 15
HELIX 26 26 GLY C 468 GLY C 472 5 5
HELIX 27 27 PRO C 482 VAL C 489 1 8
HELIX 28 28 SER D 283 HIS D 297 1 15
HELIX 29 29 THR D 300 LEU D 320 1 21
HELIX 30 30 HIS D 344 HIS D 360 1 17
HELIX 31 31 LEU D 375 SER D 386 1 12
HELIX 32 32 SER D 395 LEU D 399 5 5
HELIX 33 33 ASN D 416 ASP D 421 5 6
HELIX 34 34 GLN D 422 ARG D 436 1 15
HELIX 35 35 GLY D 468 GLY D 472 5 5
HELIX 36 36 PRO D 482 VAL D 489 1 8
SHEET 1 A 2 GLU A 270 CYS A 272 0
SHEET 2 A 2 VAL A 278 PRO A 280 -1 O VAL A 279 N PHE A 271
SHEET 1 B 8 GLN A 391 VAL A 393 0
SHEET 2 B 8 GLN A 363 PHE A 367 1 N LEU A 366 O GLN A 391
SHEET 3 B 8 THR A 336 CYS A 341 1 N LEU A 339 O PHE A 367
SHEET 4 B 8 LEU A 406 CYS A 410 1 O ILE A 408 N LEU A 340
SHEET 5 B 8 VAL A 439 ILE A 442 1 O LEU A 440 N VAL A 407
SHEET 6 B 8 TRP A 457 LEU A 461 1 O LEU A 459 N SER A 441
SHEET 7 B 8 ARG A 473 CYS A 477 1 O TYR A 475 N ALA A 460
SHEET 8 B 8 VAL A 502 LEU A 505 -1 O LEU A 505 N ILE A 474
SHEET 1 C 2 GLU B 270 CYS B 272 0
SHEET 2 C 2 VAL B 278 PRO B 280 -1 O VAL B 279 N PHE B 271
SHEET 1 D 8 GLN B 391 VAL B 393 0
SHEET 2 D 8 GLN B 363 PHE B 367 1 N LEU B 366 O GLN B 391
SHEET 3 D 8 THR B 336 CYS B 341 1 N LEU B 339 O PHE B 367
SHEET 4 D 8 LEU B 406 CYS B 410 1 O CYS B 410 N LEU B 340
SHEET 5 D 8 VAL B 439 ILE B 442 1 O LEU B 440 N ASN B 409
SHEET 6 D 8 TRP B 457 LEU B 461 1 O LEU B 459 N SER B 441
SHEET 7 D 8 ARG B 473 CYS B 477 1 O TYR B 475 N ALA B 460
SHEET 8 D 8 VAL B 502 LEU B 505 -1 O LEU B 505 N ILE B 474
SHEET 1 E 2 GLU C 270 CYS C 272 0
SHEET 2 E 2 VAL C 278 PRO C 280 -1 O VAL C 279 N PHE C 271
SHEET 1 F 8 GLN C 391 VAL C 393 0
SHEET 2 F 8 GLN C 363 PHE C 367 1 N LEU C 366 O GLN C 391
SHEET 3 F 8 THR C 336 CYS C 341 1 N LEU C 339 O PHE C 367
SHEET 4 F 8 LEU C 406 CYS C 410 1 O CYS C 410 N LEU C 340
SHEET 5 F 8 VAL C 439 ILE C 442 1 O LEU C 440 N ASN C 409
SHEET 6 F 8 TRP C 457 LEU C 461 1 O LEU C 459 N SER C 441
SHEET 7 F 8 ARG C 473 CYS C 477 1 O TYR C 475 N ALA C 460
SHEET 8 F 8 VAL C 502 LEU C 505 -1 O LEU C 505 N ILE C 474
SHEET 1 G 2 GLU D 270 CYS D 272 0
SHEET 2 G 2 VAL D 278 PRO D 280 -1 O VAL D 279 N PHE D 271
SHEET 1 H 8 GLN D 391 VAL D 393 0
SHEET 2 H 8 GLN D 363 PHE D 367 1 N LEU D 366 O GLN D 391
SHEET 3 H 8 THR D 336 CYS D 341 1 N LEU D 339 O PHE D 367
SHEET 4 H 8 LEU D 406 CYS D 410 1 O ILE D 408 N LEU D 340
SHEET 5 H 8 VAL D 439 ILE D 442 1 O LEU D 440 N VAL D 407
SHEET 6 H 8 TRP D 457 LEU D 461 1 O LEU D 459 N SER D 441
SHEET 7 H 8 ARG D 473 CYS D 477 1 O TYR D 475 N ALA D 460
SHEET 8 H 8 VAL D 502 PRO D 504 -1 O ILE D 503 N LEU D 476
CRYST1 94.377 169.204 163.609 90.00 90.00 90.00 C 2 2 21 32
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 0.010596 0.000000 0.000000 0.00000
SCALE2 0.000000 0.005910 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006112 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
