HEADER LIGASE 30-OCT-10 3PG6
TITLE THE CARBOXYL TERMINAL DOMAIN OF HUMAN DELTEX 3-LIKE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: E3 UBIQUITIN-PROTEIN LIGASE DTX3L;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 FRAGMENT: CARBOXYL TERMINAL DOMAIN (UNP RESIDUES 601-740);
COMPND 5 SYNONYM: B-LYMPHOMA- AND BAL-ASSOCIATED PROTEIN, PROTEIN DELTEX-3-
COMPND 6 LIKE, RHYSIN-2, RHYSIN2;
COMPND 7 EC: 6.3.2.-;
COMPND 8 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: BBAP, DTX3L;
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: PET28A-LIC
KEYWDS DNA-DAMAGE, LIGASE, METAL-BINDING, NUCLEUS, PHOSPHORYLATION,
KEYWDS 2 CHROMATIN REGULATOR, UBL CONJUGATION PATHWAY, ZINC-FINGER,
KEYWDS 3 STRUCTURAL GENOMICS CONSORTIUM, SGC
EXPDTA X-RAY DIFFRACTION
AUTHOR J.R.WALKER,J.OBIERO,J.KANIA,H.SCHULER,C.BOUNTRA,J.WEIGELT,
AUTHOR 2 A.M.EDWARDS,C.H.ARROWSMITH,S.DHE-PAGANON,STRUCTURAL GENOMICS
AUTHOR 3 CONSORTIUM (SGC)
REVDAT 3 21-FEB-24 3PG6 1 REMARK SEQADV
REVDAT 2 28-NOV-12 3PG6 1 JRNL VERSN
REVDAT 1 01-DEC-10 3PG6 0
JRNL AUTH J.OBIERO,J.R.WALKER,S.DHE-PAGANON
JRNL TITL FOLD OF THE CONSERVED DTC DOMAIN IN DELTEX PROTEINS.
JRNL REF PROTEINS V. 80 1495 2012
JRNL REFN ISSN 0887-3585
JRNL PMID 22411408
JRNL DOI 10.1002/PROT.24054
REMARK 2
REMARK 2 RESOLUTION. 1.70 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.5.0109
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) : 1.70
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 30.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 3 NUMBER OF REFLECTIONS : 86249
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) : 0.166
REMARK 3 R VALUE (WORKING SET) : 0.165
REMARK 3 FREE R VALUE : 0.186
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 2.300
REMARK 3 FREE R VALUE TEST SET COUNT : 2043
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) : 1.70
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.74
REMARK 3 REFLECTION IN BIN (WORKING SET) : 6368
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.55
REMARK 3 BIN R VALUE (WORKING SET) : 0.2140
REMARK 3 BIN FREE R VALUE SET COUNT : 0
REMARK 3 BIN FREE R VALUE : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 4259
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 72
REMARK 3 SOLVENT ATOMS : 607
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 22.97
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.46000
REMARK 3 B22 (A**2) : -0.28000
REMARK 3 B33 (A**2) : -0.18000
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): 0.079
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.078
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.052
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 3.427
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.965
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.954
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 4607 ; 0.015 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 6251 ; 1.546 ; 1.983
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 578 ; 5.861 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 200 ;31.466 ;23.200
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 784 ;12.500 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 32 ;18.449 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 647 ; 0.107 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 3568 ; 0.008 ; 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): 2787 ; 0.843 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 4545 ; 1.577 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1820 ; 2.679 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1701 ; 4.518 ; 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 : 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 606 A 740
REMARK 3 ORIGIN FOR THE GROUP (A): 1.1200 38.0010 -26.9990
REMARK 3 T TENSOR
REMARK 3 T11: 0.0565 T22: 0.0313
REMARK 3 T33: 0.0376 T12: 0.0055
REMARK 3 T13: -0.0288 T23: -0.0130
REMARK 3 L TENSOR
REMARK 3 L11: 0.7395 L22: 1.3839
REMARK 3 L33: 0.8290 L12: 0.2029
REMARK 3 L13: 0.1431 L23: 0.0347
REMARK 3 S TENSOR
REMARK 3 S11: 0.0404 S12: -0.0990 S13: -0.0238
REMARK 3 S21: 0.0550 S22: -0.0294 S23: -0.0158
REMARK 3 S31: 0.1007 S32: -0.0415 S33: -0.0110
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 607 B 740
REMARK 3 ORIGIN FOR THE GROUP (A): 24.4980 61.7850 -11.1140
REMARK 3 T TENSOR
REMARK 3 T11: 0.0705 T22: 0.1001
REMARK 3 T33: 0.0782 T12: -0.0388
REMARK 3 T13: -0.0274 T23: 0.0281
REMARK 3 L TENSOR
REMARK 3 L11: 1.9944 L22: 0.7058
REMARK 3 L33: 1.0754 L12: -0.3566
REMARK 3 L13: 0.8153 L23: 0.4158
REMARK 3 S TENSOR
REMARK 3 S11: -0.1242 S12: 0.1807 S13: 0.1640
REMARK 3 S21: -0.1614 S22: 0.0355 S23: -0.0304
REMARK 3 S31: -0.2187 S32: 0.1952 S33: 0.0886
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 606 C 740
REMARK 3 ORIGIN FOR THE GROUP (A): 13.3560 50.3280 1.1620
REMARK 3 T TENSOR
REMARK 3 T11: 0.0740 T22: 0.1259
REMARK 3 T33: 0.0691 T12: -0.0289
REMARK 3 T13: -0.0283 T23: 0.0103
REMARK 3 L TENSOR
REMARK 3 L11: 0.9194 L22: 0.9148
REMARK 3 L33: 2.0711 L12: 0.3553
REMARK 3 L13: 1.1003 L23: 0.9055
REMARK 3 S TENSOR
REMARK 3 S11: 0.0862 S12: -0.2070 S13: -0.0639
REMARK 3 S21: 0.1274 S22: -0.0785 S23: 0.0119
REMARK 3 S31: 0.2607 S32: -0.2236 S33: -0.0077
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 607 D 740
REMARK 3 ORIGIN FOR THE GROUP (A): 9.0210 49.2450 -42.0930
REMARK 3 T TENSOR
REMARK 3 T11: 0.1186 T22: 0.0434
REMARK 3 T33: 0.0568 T12: -0.0025
REMARK 3 T13: 0.0116 T23: -0.0059
REMARK 3 L TENSOR
REMARK 3 L11: 0.4675 L22: 2.5029
REMARK 3 L33: 0.5183 L12: 0.0454
REMARK 3 L13: 0.2570 L23: 0.3781
REMARK 3 S TENSOR
REMARK 3 S11: -0.0406 S12: 0.1224 S13: 0.0389
REMARK 3 S21: -0.3161 S22: 0.0488 S23: -0.1617
REMARK 3 S31: -0.0430 S32: 0.0718 S33: -0.0082
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 3PG6 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 03-NOV-10.
REMARK 100 THE DEPOSITION ID IS D_1000062337.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 22-OCT-10
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 23-ID-D
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97949, 0.97946
REMARK 200 MONOCHROMATOR : DOUBLE CRYSTAL CRYO-COOLED
REMARK 200 SI(111)
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 300 MM CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 88378
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.700
REMARK 200 RESOLUTION RANGE LOW (A) : 30.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 7.400
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.07400
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 31.6279
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.70
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.73
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 2.73
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.64300
REMARK 200 <I/SIGMA(I)> FOR SHELL : 7.400
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD
REMARK 200 SOFTWARE USED: SHELX C/D/E
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: THE SE-MET DATA SET USED FOR PHASING WAS COLLECTED AT A
REMARK 200 WAVELENGTH OF 0.97946
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 59.65
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.05
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 22% PEG3350, 0.2 M TRI-LITHIUM CITRATE
REMARK 280 PH 6.0, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
REMARK 290 4555 X+1/2,-Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 37.66150
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 69.37650
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 38.07300
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 69.37650
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 37.66150
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 38.07300
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
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: 2330 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 13100 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -10.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, 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: 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: 3120 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 12580 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -7.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, C
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 MET A 582
REMARK 465 GLY A 583
REMARK 465 SER A 584
REMARK 465 SER A 585
REMARK 465 HIS A 586
REMARK 465 HIS A 587
REMARK 465 HIS A 588
REMARK 465 HIS A 589
REMARK 465 HIS A 590
REMARK 465 HIS A 591
REMARK 465 SER A 592
REMARK 465 SER A 593
REMARK 465 GLY A 594
REMARK 465 LEU A 595
REMARK 465 VAL A 596
REMARK 465 PRO A 597
REMARK 465 ARG A 598
REMARK 465 GLY A 599
REMARK 465 SER A 600
REMARK 465 THR A 601
REMARK 465 SER A 602
REMARK 465 TYR A 603
REMARK 465 GLY A 604
REMARK 465 ILE A 605
REMARK 465 MET B 582
REMARK 465 GLY B 583
REMARK 465 SER B 584
REMARK 465 SER B 585
REMARK 465 HIS B 586
REMARK 465 HIS B 587
REMARK 465 HIS B 588
REMARK 465 HIS B 589
REMARK 465 HIS B 590
REMARK 465 HIS B 591
REMARK 465 SER B 592
REMARK 465 SER B 593
REMARK 465 GLY B 594
REMARK 465 LEU B 595
REMARK 465 VAL B 596
REMARK 465 PRO B 597
REMARK 465 ARG B 598
REMARK 465 GLY B 599
REMARK 465 SER B 600
REMARK 465 THR B 601
REMARK 465 SER B 602
REMARK 465 TYR B 603
REMARK 465 GLY B 604
REMARK 465 ILE B 605
REMARK 465 GLN B 606
REMARK 465 MET C 582
REMARK 465 GLY C 583
REMARK 465 SER C 584
REMARK 465 SER C 585
REMARK 465 HIS C 586
REMARK 465 HIS C 587
REMARK 465 HIS C 588
REMARK 465 HIS C 589
REMARK 465 HIS C 590
REMARK 465 HIS C 591
REMARK 465 SER C 592
REMARK 465 SER C 593
REMARK 465 GLY C 594
REMARK 465 LEU C 595
REMARK 465 VAL C 596
REMARK 465 PRO C 597
REMARK 465 ARG C 598
REMARK 465 GLY C 599
REMARK 465 SER C 600
REMARK 465 THR C 601
REMARK 465 SER C 602
REMARK 465 TYR C 603
REMARK 465 GLY C 604
REMARK 465 ILE C 605
REMARK 465 MET D 582
REMARK 465 GLY D 583
REMARK 465 SER D 584
REMARK 465 SER D 585
REMARK 465 HIS D 586
REMARK 465 HIS D 587
REMARK 465 HIS D 588
REMARK 465 HIS D 589
REMARK 465 HIS D 590
REMARK 465 HIS D 591
REMARK 465 SER D 592
REMARK 465 SER D 593
REMARK 465 GLY D 594
REMARK 465 LEU D 595
REMARK 465 VAL D 596
REMARK 465 PRO D 597
REMARK 465 ARG D 598
REMARK 465 GLY D 599
REMARK 465 SER D 600
REMARK 465 THR D 601
REMARK 465 SER D 602
REMARK 465 TYR D 603
REMARK 465 GLY D 604
REMARK 465 ILE D 605
REMARK 465 GLN D 606
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 ARG A 621 NE CZ NH1 NH2
REMARK 470 LYS A 653 CD CE NZ
REMARK 470 ARG A 654 CZ NH1 NH2
REMARK 470 LYS B 675 CD CE NZ
REMARK 470 LYS B 728 CG CD CE NZ
REMARK 470 LYS B 735 CE NZ
REMARK 470 GLU C 647 OE1 OE2
REMARK 470 LYS C 675 CE NZ
REMARK 470 ARG C 693 CZ NH1 NH2
REMARK 470 LEU C 695 CG CD1 CD2
REMARK 470 LYS C 728 CE NZ
REMARK 470 LYS C 735 CE NZ
REMARK 470 LYS D 607 CE NZ
REMARK 470 ARG D 621 CG CD NE CZ NH1 NH2
REMARK 470 LYS D 672 CE NZ
REMARK 470 LYS D 675 CE NZ
REMARK 470 LYS D 728 CG CD CE NZ
REMARK 470 LYS D 735 CE NZ
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 OG SER D 638 O HOH D 1150 2.16
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 723 87.63 -156.37
REMARK 500 SER B 698 -169.11 -109.38
REMARK 500 SER B 698 -162.69 -108.56
REMARK 500 SER D 698 -161.34 -107.04
REMARK 500
REMARK 500 REMARK: NULL
REMARK 610
REMARK 610 MISSING HETEROATOM
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 610 I=INSERTION CODE):
REMARK 610 M RES C SSEQI
REMARK 610 CIT A 1000
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CIT A 1000
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG A 1001
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG B 1002
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CIT B 1000
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG B 1001
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG B 741
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CIT C 1001
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL D 1000
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: DTX3L RELATED DB: TARGETDB
DBREF 3PG6 A 601 740 UNP Q8TDB6 DTX3L_HUMAN 601 740
DBREF 3PG6 B 601 740 UNP Q8TDB6 DTX3L_HUMAN 601 740
DBREF 3PG6 C 601 740 UNP Q8TDB6 DTX3L_HUMAN 601 740
DBREF 3PG6 D 601 740 UNP Q8TDB6 DTX3L_HUMAN 601 740
SEQADV 3PG6 MET A 582 UNP Q8TDB6 EXPRESSION TAG
SEQADV 3PG6 GLY A 583 UNP Q8TDB6 EXPRESSION TAG
SEQADV 3PG6 SER A 584 UNP Q8TDB6 EXPRESSION TAG
SEQADV 3PG6 SER A 585 UNP Q8TDB6 EXPRESSION TAG
SEQADV 3PG6 HIS A 586 UNP Q8TDB6 EXPRESSION TAG
SEQADV 3PG6 HIS A 587 UNP Q8TDB6 EXPRESSION TAG
SEQADV 3PG6 HIS A 588 UNP Q8TDB6 EXPRESSION TAG
SEQADV 3PG6 HIS A 589 UNP Q8TDB6 EXPRESSION TAG
SEQADV 3PG6 HIS A 590 UNP Q8TDB6 EXPRESSION TAG
SEQADV 3PG6 HIS A 591 UNP Q8TDB6 EXPRESSION TAG
SEQADV 3PG6 SER A 592 UNP Q8TDB6 EXPRESSION TAG
SEQADV 3PG6 SER A 593 UNP Q8TDB6 EXPRESSION TAG
SEQADV 3PG6 GLY A 594 UNP Q8TDB6 EXPRESSION TAG
SEQADV 3PG6 LEU A 595 UNP Q8TDB6 EXPRESSION TAG
SEQADV 3PG6 VAL A 596 UNP Q8TDB6 EXPRESSION TAG
SEQADV 3PG6 PRO A 597 UNP Q8TDB6 EXPRESSION TAG
SEQADV 3PG6 ARG A 598 UNP Q8TDB6 EXPRESSION TAG
SEQADV 3PG6 GLY A 599 UNP Q8TDB6 EXPRESSION TAG
SEQADV 3PG6 SER A 600 UNP Q8TDB6 EXPRESSION TAG
SEQADV 3PG6 MET B 582 UNP Q8TDB6 EXPRESSION TAG
SEQADV 3PG6 GLY B 583 UNP Q8TDB6 EXPRESSION TAG
SEQADV 3PG6 SER B 584 UNP Q8TDB6 EXPRESSION TAG
SEQADV 3PG6 SER B 585 UNP Q8TDB6 EXPRESSION TAG
SEQADV 3PG6 HIS B 586 UNP Q8TDB6 EXPRESSION TAG
SEQADV 3PG6 HIS B 587 UNP Q8TDB6 EXPRESSION TAG
SEQADV 3PG6 HIS B 588 UNP Q8TDB6 EXPRESSION TAG
SEQADV 3PG6 HIS B 589 UNP Q8TDB6 EXPRESSION TAG
SEQADV 3PG6 HIS B 590 UNP Q8TDB6 EXPRESSION TAG
SEQADV 3PG6 HIS B 591 UNP Q8TDB6 EXPRESSION TAG
SEQADV 3PG6 SER B 592 UNP Q8TDB6 EXPRESSION TAG
SEQADV 3PG6 SER B 593 UNP Q8TDB6 EXPRESSION TAG
SEQADV 3PG6 GLY B 594 UNP Q8TDB6 EXPRESSION TAG
SEQADV 3PG6 LEU B 595 UNP Q8TDB6 EXPRESSION TAG
SEQADV 3PG6 VAL B 596 UNP Q8TDB6 EXPRESSION TAG
SEQADV 3PG6 PRO B 597 UNP Q8TDB6 EXPRESSION TAG
SEQADV 3PG6 ARG B 598 UNP Q8TDB6 EXPRESSION TAG
SEQADV 3PG6 GLY B 599 UNP Q8TDB6 EXPRESSION TAG
SEQADV 3PG6 SER B 600 UNP Q8TDB6 EXPRESSION TAG
SEQADV 3PG6 MET C 582 UNP Q8TDB6 EXPRESSION TAG
SEQADV 3PG6 GLY C 583 UNP Q8TDB6 EXPRESSION TAG
SEQADV 3PG6 SER C 584 UNP Q8TDB6 EXPRESSION TAG
SEQADV 3PG6 SER C 585 UNP Q8TDB6 EXPRESSION TAG
SEQADV 3PG6 HIS C 586 UNP Q8TDB6 EXPRESSION TAG
SEQADV 3PG6 HIS C 587 UNP Q8TDB6 EXPRESSION TAG
SEQADV 3PG6 HIS C 588 UNP Q8TDB6 EXPRESSION TAG
SEQADV 3PG6 HIS C 589 UNP Q8TDB6 EXPRESSION TAG
SEQADV 3PG6 HIS C 590 UNP Q8TDB6 EXPRESSION TAG
SEQADV 3PG6 HIS C 591 UNP Q8TDB6 EXPRESSION TAG
SEQADV 3PG6 SER C 592 UNP Q8TDB6 EXPRESSION TAG
SEQADV 3PG6 SER C 593 UNP Q8TDB6 EXPRESSION TAG
SEQADV 3PG6 GLY C 594 UNP Q8TDB6 EXPRESSION TAG
SEQADV 3PG6 LEU C 595 UNP Q8TDB6 EXPRESSION TAG
SEQADV 3PG6 VAL C 596 UNP Q8TDB6 EXPRESSION TAG
SEQADV 3PG6 PRO C 597 UNP Q8TDB6 EXPRESSION TAG
SEQADV 3PG6 ARG C 598 UNP Q8TDB6 EXPRESSION TAG
SEQADV 3PG6 GLY C 599 UNP Q8TDB6 EXPRESSION TAG
SEQADV 3PG6 SER C 600 UNP Q8TDB6 EXPRESSION TAG
SEQADV 3PG6 MET D 582 UNP Q8TDB6 EXPRESSION TAG
SEQADV 3PG6 GLY D 583 UNP Q8TDB6 EXPRESSION TAG
SEQADV 3PG6 SER D 584 UNP Q8TDB6 EXPRESSION TAG
SEQADV 3PG6 SER D 585 UNP Q8TDB6 EXPRESSION TAG
SEQADV 3PG6 HIS D 586 UNP Q8TDB6 EXPRESSION TAG
SEQADV 3PG6 HIS D 587 UNP Q8TDB6 EXPRESSION TAG
SEQADV 3PG6 HIS D 588 UNP Q8TDB6 EXPRESSION TAG
SEQADV 3PG6 HIS D 589 UNP Q8TDB6 EXPRESSION TAG
SEQADV 3PG6 HIS D 590 UNP Q8TDB6 EXPRESSION TAG
SEQADV 3PG6 HIS D 591 UNP Q8TDB6 EXPRESSION TAG
SEQADV 3PG6 SER D 592 UNP Q8TDB6 EXPRESSION TAG
SEQADV 3PG6 SER D 593 UNP Q8TDB6 EXPRESSION TAG
SEQADV 3PG6 GLY D 594 UNP Q8TDB6 EXPRESSION TAG
SEQADV 3PG6 LEU D 595 UNP Q8TDB6 EXPRESSION TAG
SEQADV 3PG6 VAL D 596 UNP Q8TDB6 EXPRESSION TAG
SEQADV 3PG6 PRO D 597 UNP Q8TDB6 EXPRESSION TAG
SEQADV 3PG6 ARG D 598 UNP Q8TDB6 EXPRESSION TAG
SEQADV 3PG6 GLY D 599 UNP Q8TDB6 EXPRESSION TAG
SEQADV 3PG6 SER D 600 UNP Q8TDB6 EXPRESSION TAG
SEQRES 1 A 159 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 A 159 LEU VAL PRO ARG GLY SER THR SER TYR GLY ILE GLN LYS
SEQRES 3 A 159 GLY ASN GLN PRO GLU GLY SER MET VAL PHE THR VAL SER
SEQRES 4 A 159 ARG ASP SER LEU PRO GLY TYR GLU SER PHE GLY THR ILE
SEQRES 5 A 159 VAL ILE THR TYR SER MET LYS ALA GLY ILE GLN THR GLU
SEQRES 6 A 159 GLU HIS PRO ASN PRO GLY LYS ARG TYR PRO GLY ILE GLN
SEQRES 7 A 159 ARG THR ALA TYR LEU PRO ASP ASN LYS GLU GLY ARG LYS
SEQRES 8 A 159 VAL LEU LYS LEU LEU TYR ARG ALA PHE ASP GLN LYS LEU
SEQRES 9 A 159 ILE PHE THR VAL GLY TYR SER ARG VAL LEU GLY VAL SER
SEQRES 10 A 159 ASP VAL ILE THR TRP ASN ASP ILE HIS HIS LYS THR SER
SEQRES 11 A 159 ARG PHE GLY GLY PRO GLU MET TYR GLY TYR PRO ASP PRO
SEQRES 12 A 159 SER TYR LEU LYS ARG VAL LYS GLU GLU LEU LYS ALA LYS
SEQRES 13 A 159 GLY ILE GLU
SEQRES 1 B 159 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 B 159 LEU VAL PRO ARG GLY SER THR SER TYR GLY ILE GLN LYS
SEQRES 3 B 159 GLY ASN GLN PRO GLU GLY SER MET VAL PHE THR VAL SER
SEQRES 4 B 159 ARG ASP SER LEU PRO GLY TYR GLU SER PHE GLY THR ILE
SEQRES 5 B 159 VAL ILE THR TYR SER MET LYS ALA GLY ILE GLN THR GLU
SEQRES 6 B 159 GLU HIS PRO ASN PRO GLY LYS ARG TYR PRO GLY ILE GLN
SEQRES 7 B 159 ARG THR ALA TYR LEU PRO ASP ASN LYS GLU GLY ARG LYS
SEQRES 8 B 159 VAL LEU LYS LEU LEU TYR ARG ALA PHE ASP GLN LYS LEU
SEQRES 9 B 159 ILE PHE THR VAL GLY TYR SER ARG VAL LEU GLY VAL SER
SEQRES 10 B 159 ASP VAL ILE THR TRP ASN ASP ILE HIS HIS LYS THR SER
SEQRES 11 B 159 ARG PHE GLY GLY PRO GLU MET TYR GLY TYR PRO ASP PRO
SEQRES 12 B 159 SER TYR LEU LYS ARG VAL LYS GLU GLU LEU LYS ALA LYS
SEQRES 13 B 159 GLY ILE GLU
SEQRES 1 C 159 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 C 159 LEU VAL PRO ARG GLY SER THR SER TYR GLY ILE GLN LYS
SEQRES 3 C 159 GLY ASN GLN PRO GLU GLY SER MET VAL PHE THR VAL SER
SEQRES 4 C 159 ARG ASP SER LEU PRO GLY TYR GLU SER PHE GLY THR ILE
SEQRES 5 C 159 VAL ILE THR TYR SER MET LYS ALA GLY ILE GLN THR GLU
SEQRES 6 C 159 GLU HIS PRO ASN PRO GLY LYS ARG TYR PRO GLY ILE GLN
SEQRES 7 C 159 ARG THR ALA TYR LEU PRO ASP ASN LYS GLU GLY ARG LYS
SEQRES 8 C 159 VAL LEU LYS LEU LEU TYR ARG ALA PHE ASP GLN LYS LEU
SEQRES 9 C 159 ILE PHE THR VAL GLY TYR SER ARG VAL LEU GLY VAL SER
SEQRES 10 C 159 ASP VAL ILE THR TRP ASN ASP ILE HIS HIS LYS THR SER
SEQRES 11 C 159 ARG PHE GLY GLY PRO GLU MET TYR GLY TYR PRO ASP PRO
SEQRES 12 C 159 SER TYR LEU LYS ARG VAL LYS GLU GLU LEU LYS ALA LYS
SEQRES 13 C 159 GLY ILE GLU
SEQRES 1 D 159 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 D 159 LEU VAL PRO ARG GLY SER THR SER TYR GLY ILE GLN LYS
SEQRES 3 D 159 GLY ASN GLN PRO GLU GLY SER MET VAL PHE THR VAL SER
SEQRES 4 D 159 ARG ASP SER LEU PRO GLY TYR GLU SER PHE GLY THR ILE
SEQRES 5 D 159 VAL ILE THR TYR SER MET LYS ALA GLY ILE GLN THR GLU
SEQRES 6 D 159 GLU HIS PRO ASN PRO GLY LYS ARG TYR PRO GLY ILE GLN
SEQRES 7 D 159 ARG THR ALA TYR LEU PRO ASP ASN LYS GLU GLY ARG LYS
SEQRES 8 D 159 VAL LEU LYS LEU LEU TYR ARG ALA PHE ASP GLN LYS LEU
SEQRES 9 D 159 ILE PHE THR VAL GLY TYR SER ARG VAL LEU GLY VAL SER
SEQRES 10 D 159 ASP VAL ILE THR TRP ASN ASP ILE HIS HIS LYS THR SER
SEQRES 11 D 159 ARG PHE GLY GLY PRO GLU MET TYR GLY TYR PRO ASP PRO
SEQRES 12 D 159 SER TYR LEU LYS ARG VAL LYS GLU GLU LEU LYS ALA LYS
SEQRES 13 D 159 GLY ILE GLU
HET CIT A1000 12
HET PEG A1001 7
HET PEG B1002 7
HET CIT B1000 13
HET PEG B1001 7
HET PEG B 741 7
HET CIT C1001 13
HET GOL D1000 6
HETNAM CIT CITRIC ACID
HETNAM PEG DI(HYDROXYETHYL)ETHER
HETNAM GOL GLYCEROL
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 5 CIT 3(C6 H8 O7)
FORMUL 6 PEG 4(C4 H10 O3)
FORMUL 12 GOL C3 H8 O3
FORMUL 13 HOH *607(H2 O)
HELIX 1 1 ASN A 667 GLN A 683 1 17
HELIX 2 2 GLY A 715 TYR A 719 5 5
HELIX 3 3 SER A 725 LYS A 737 1 13
HELIX 4 4 ASN B 667 GLN B 683 1 17
HELIX 5 5 GLY B 715 TYR B 719 5 5
HELIX 6 6 SER B 725 LYS B 737 1 13
HELIX 7 7 ASN C 667 GLN C 683 1 17
HELIX 8 8 GLY C 715 TYR C 719 5 5
HELIX 9 9 SER C 725 LYS C 737 1 13
HELIX 10 10 ASN D 667 GLN D 683 1 17
HELIX 11 11 GLY D 715 TYR D 719 5 5
HELIX 12 12 SER D 725 ALA D 736 1 12
SHEET 1 A 3 GLY A 613 SER A 620 0
SHEET 2 A 3 GLY A 631 MET A 639 -1 O VAL A 634 N THR A 618
SHEET 3 A 3 ILE A 658 ASP A 666 -1 O LEU A 664 N ILE A 633
SHEET 1 B 2 GLY A 642 ILE A 643 0
SHEET 2 B 2 ARG A 654 TYR A 655 -1 O TYR A 655 N GLY A 642
SHEET 1 C 2 PHE A 687 SER A 692 0
SHEET 2 C 2 VAL A 697 TRP A 703 -1 O VAL A 697 N SER A 692
SHEET 1 D 3 GLY B 613 SER B 620 0
SHEET 2 D 3 THR B 632 MET B 639 -1 O THR B 632 N SER B 620
SHEET 3 D 3 ILE B 658 PRO B 665 -1 O ARG B 660 N TYR B 637
SHEET 1 E 2 GLY B 642 ILE B 643 0
SHEET 2 E 2 ARG B 654 TYR B 655 -1 O TYR B 655 N GLY B 642
SHEET 1 F 2 PHE B 687 SER B 692 0
SHEET 2 F 2 VAL B 697 TRP B 703 -1 O VAL B 697 N SER B 692
SHEET 1 G 3 GLY C 613 SER C 620 0
SHEET 2 G 3 THR C 632 MET C 639 -1 O VAL C 634 N THR C 618
SHEET 3 G 3 ILE C 658 PRO C 665 -1 O ARG C 660 N TYR C 637
SHEET 1 H 2 GLY C 642 ILE C 643 0
SHEET 2 H 2 ARG C 654 TYR C 655 -1 O TYR C 655 N GLY C 642
SHEET 1 I 2 PHE C 687 SER C 692 0
SHEET 2 I 2 VAL C 697 TRP C 703 -1 O VAL C 697 N SER C 692
SHEET 1 J 3 GLY D 613 SER D 620 0
SHEET 2 J 3 GLY D 631 MET D 639 -1 O VAL D 634 N THR D 618
SHEET 3 J 3 ILE D 658 ASP D 666 -1 O ARG D 660 N TYR D 637
SHEET 1 K 2 GLY D 642 ILE D 643 0
SHEET 2 K 2 ARG D 654 TYR D 655 -1 O TYR D 655 N GLY D 642
SHEET 1 L 2 PHE D 687 SER D 692 0
SHEET 2 L 2 VAL D 697 TRP D 703 -1 O VAL D 697 N SER D 692
CISPEP 1 TYR A 721 PRO A 722 0 6.66
CISPEP 2 TYR B 721 PRO B 722 0 3.79
CISPEP 3 TYR C 721 PRO C 722 0 1.25
CISPEP 4 TYR D 721 PRO D 722 0 3.23
SITE 1 AC1 7 ARG A 660 SER A 692 THR A 702 TRP A 703
SITE 2 AC1 7 HOH A1129 HOH A1168 HOH D1007
SITE 1 AC2 6 ALA A 641 GLY A 642 ARG A 654 TYR A 655
SITE 2 AC2 6 HOH A1124 HOH A1157
SITE 1 AC3 5 GLY B 715 PRO B 716 PEG B 741 HOH B1028
SITE 2 AC3 5 HOH B1064
SITE 1 AC4 8 SER B 692 ARG B 693 VAL B 694 THR B 702
SITE 2 AC4 8 TRP B 703 HOH B1068 HOH B1071 HOH B1130
SITE 1 AC5 8 PHE B 630 HOH B1026 HOH B1050 HOH B1108
SITE 2 AC5 8 HOH B1119 GLY D 714 GLY D 715 HOH D1096
SITE 1 AC6 9 PHE B 713 GLY B 714 GLU B 717 MET B 718
SITE 2 AC6 9 PEG B1002 SER C 614 SER C 638 LYS C 640
SITE 3 AC6 9 HOH C1131
SITE 1 AC7 10 HOH B1088 ARG C 660 SER C 692 ILE C 701
SITE 2 AC7 10 THR C 702 TRP C 703 HOH C1097 HOH C1121
SITE 3 AC7 10 HOH C1147 HOH C1148
SITE 1 AC8 4 LYS A 675 ARG D 693 TRP D 703 HOH D1154
CRYST1 75.323 76.146 138.753 90.00 90.00 90.00 P 21 21 21 16
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 0.013276 0.000000 0.000000 0.00000
SCALE2 0.000000 0.013133 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007207 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
