HEADER LIGASE 02-DEC-10 3PTF
TITLE X-RAY STRUCTURE OF THE NON-COVALENT COMPLEX BETWEEN UBCH5A AND
TITLE 2 UBIQUITIN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: UBIQUITIN-CONJUGATING ENZYME E2 D1;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: E2;
COMPND 5 SYNONYM: STIMULATOR OF FE TRANSPORT, SFT, UBC4/5 HOMOLOG, UBCH5,
COMPND 6 UBIQUITIN CARRIER PROTEIN D1, UBIQUITIN-CONJUGATING ENZYME E2(17)KB
COMPND 7 1, UBIQUITIN-CONJUGATING ENZYME E2-17 KDA 1, UBIQUITIN-PROTEIN LIGASE
COMPND 8 D1;
COMPND 9 EC: 6.3.2.19;
COMPND 10 ENGINEERED: YES;
COMPND 11 MOL_ID: 2;
COMPND 12 MOLECULE: POLYUBIQUITIN-B;
COMPND 13 CHAIN: C, D;
COMPND 14 FRAGMENT: UBIQUITIN;
COMPND 15 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: SFT, UBC5A, UBCH5, UBCH5A, UBE2D1;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21-CODONPLUS(DE3)-RIL;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET-15B;
SOURCE 11 MOL_ID: 2;
SOURCE 12 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 13 ORGANISM_COMMON: HUMAN;
SOURCE 14 ORGANISM_TAXID: 9606;
SOURCE 15 GENE: UBIQUITIN;
SOURCE 16 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 17 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 18 EXPRESSION_SYSTEM_STRAIN: BL21-CODONPLUS(DE3)-RIL;
SOURCE 19 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 20 EXPRESSION_SYSTEM_PLASMID: PET-15B
KEYWDS PROTEIN-PROTEIN COMPLEX, E2, UBIQUITIN, UBIQUITIN CONJUGATING ENZYME,
KEYWDS 2 ALPHA/BETA, LIGASE
EXPDTA X-RAY DIFFRACTION
AUTHOR I.BOSANAC,S.G.HYMOWITZ
REVDAT 2 06-SEP-23 3PTF 1 SEQADV
REVDAT 1 11-MAY-11 3PTF 0
JRNL AUTH I.BOSANAC,L.PHU,B.PAN,I.ZILBERLEYB,B.MAURER,V.M.DIXIT,
JRNL AUTH 2 S.G.HYMOWITZ,D.S.KIRKPATRICK
JRNL TITL MODULATION OF K11-LINKAGE FORMATION BY VARIABLE LOOP
JRNL TITL 2 RESIDUES WITHIN UBCH5A.
JRNL REF J.MOL.BIOL. V. 408 420 2011
JRNL REFN ISSN 0022-2836
JRNL PMID 21396940
JRNL DOI 10.1016/J.JMB.2011.03.011
REMARK 2
REMARK 2 RESOLUTION. 2.70 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) : 2.70
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 50.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 97.5
REMARK 3 NUMBER OF REFLECTIONS : 13133
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) : 0.212
REMARK 3 R VALUE (WORKING SET) : 0.209
REMARK 3 FREE R VALUE : 0.275
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.800
REMARK 3 FREE R VALUE TEST SET COUNT : 622
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 25
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.70
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.76
REMARK 3 REFLECTION IN BIN (WORKING SET) : 717
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 98.58
REMARK 3 BIN R VALUE (WORKING SET) : 0.3070
REMARK 3 BIN FREE R VALUE SET COUNT : 47
REMARK 3 BIN FREE R VALUE : 0.5100
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 3600
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 40
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 59.00
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 43.34
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.97000
REMARK 3 B22 (A**2) : -1.82000
REMARK 3 B33 (A**2) : 0.85000
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): NULL
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.415
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.285
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 30.479
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.937
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.894
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 3698 ; 0.009 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): 2549 ; 0.001 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 5023 ; 1.095 ; 1.975
REMARK 3 BOND ANGLES OTHERS (DEGREES): 6270 ; 0.808 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 450 ; 5.649 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 162 ;33.352 ;24.753
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 654 ;15.719 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 17 ;13.739 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 560 ; 0.060 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 4022 ; 0.004 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 677 ; 0.001 ; 0.020
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): 2276 ; 2.619 ; 2.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 886 ; 0.505 ; 2.500
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 3717 ; 4.661 ; 5.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1422 ; 3.513 ; 2.500
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1305 ; 5.951 ; 5.000
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 : 2
REMARK 3
REMARK 3 NCS GROUP NUMBER : 1
REMARK 3 CHAIN NAMES : A B
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 1
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 A 4 A 61 1
REMARK 3 1 B 4 B 61 1
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 TIGHT POSITIONAL 1 A (A): 778 ; 0.02 ; 0.05
REMARK 3 TIGHT THERMAL 1 A (A**2): 778 ; 0.45 ; 0.50
REMARK 3
REMARK 3 NCS GROUP NUMBER : 2
REMARK 3 CHAIN NAMES : C D
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 1
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 C 1 C 73 4
REMARK 3 1 D 1 D 73 4
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 MEDIUM POSITIONAL 2 C (A): 990 ; 0.25 ; 0.50
REMARK 3 MEDIUM THERMAL 2 C (A**2): 990 ; 0.49 ; 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 : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 1 A 147
REMARK 3 ORIGIN FOR THE GROUP (A): 2.2863 19.0461 33.6864
REMARK 3 T TENSOR
REMARK 3 T11: 0.1293 T22: 0.0899
REMARK 3 T33: 0.0848 T12: -0.0039
REMARK 3 T13: 0.0144 T23: 0.0268
REMARK 3 L TENSOR
REMARK 3 L11: 0.5165 L22: 1.4066
REMARK 3 L33: 3.2141 L12: 0.0598
REMARK 3 L13: 0.6924 L23: 1.2531
REMARK 3 S TENSOR
REMARK 3 S11: 0.0264 S12: 0.0290 S13: -0.0219
REMARK 3 S21: 0.0688 S22: -0.0369 S23: -0.0557
REMARK 3 S31: 0.2012 S32: -0.0078 S33: 0.0105
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 147
REMARK 3 ORIGIN FOR THE GROUP (A): 12.0049 50.2918 10.5067
REMARK 3 T TENSOR
REMARK 3 T11: 0.0966 T22: 0.1149
REMARK 3 T33: 0.0781 T12: 0.0155
REMARK 3 T13: 0.0260 T23: -0.0037
REMARK 3 L TENSOR
REMARK 3 L11: 1.0249 L22: 3.1262
REMARK 3 L33: 1.6981 L12: 0.1941
REMARK 3 L13: -0.0838 L23: 0.0599
REMARK 3 S TENSOR
REMARK 3 S11: -0.2224 S12: -0.0511 S13: -0.0381
REMARK 3 S21: -0.1340 S22: 0.2316 S23: -0.0582
REMARK 3 S31: -0.0331 S32: 0.1883 S33: -0.0092
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 73
REMARK 3 ORIGIN FOR THE GROUP (A): -0.6131 42.4372 33.0572
REMARK 3 T TENSOR
REMARK 3 T11: 0.0175 T22: 0.0461
REMARK 3 T33: 0.1027 T12: -0.0127
REMARK 3 T13: 0.0233 T23: -0.0072
REMARK 3 L TENSOR
REMARK 3 L11: 1.9410 L22: 3.5983
REMARK 3 L33: 4.8786 L12: 0.0594
REMARK 3 L13: 0.8408 L23: 0.1209
REMARK 3 S TENSOR
REMARK 3 S11: 0.0811 S12: 0.0728 S13: -0.0202
REMARK 3 S21: 0.0780 S22: -0.0698 S23: 0.0397
REMARK 3 S31: -0.0654 S32: -0.0299 S33: -0.0112
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 73
REMARK 3 ORIGIN FOR THE GROUP (A): 10.3371 61.8829 -10.3491
REMARK 3 T TENSOR
REMARK 3 T11: 0.1126 T22: 0.0710
REMARK 3 T33: 0.0705 T12: -0.0322
REMARK 3 T13: 0.0359 T23: 0.0149
REMARK 3 L TENSOR
REMARK 3 L11: 5.3677 L22: 5.2689
REMARK 3 L33: 4.9335 L12: -0.9046
REMARK 3 L13: -0.0959 L23: -0.9290
REMARK 3 S TENSOR
REMARK 3 S11: 0.0906 S12: 0.1105 S13: 0.1599
REMARK 3 S21: -0.0783 S22: -0.1136 S23: -0.1075
REMARK 3 S31: -0.1206 S32: -0.1498 S33: 0.0230
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 3PTF COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 07-DEC-10.
REMARK 100 THE DEPOSITION ID IS D_1000062791.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 01-JUN-06
REMARK 200 TEMPERATURE (KELVIN) : 93
REMARK 200 PH : 8.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SSRL
REMARK 200 BEAMLINE : BL9-2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97918
REMARK 200 MONOCHROMATOR : DOUBLE CRYSTAL SI(111)
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 325 MM CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 13156
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.700
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 97.4
REMARK 200 DATA REDUNDANCY : 5.300
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.12800
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 17.4000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.70
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.80
REMARK 200 COMPLETENESS FOR SHELL (%) : 98.3
REMARK 200 DATA REDUNDANCY IN SHELL : 5.30
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.45800
REMARK 200 <I/SIGMA(I)> FOR SHELL : 3.200
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: 1UBQ, 1X23
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 43.05
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.16
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: CRYSTALS OF THE COMPLEX WERE GROWN BY
REMARK 280 HANGING-DROP VAPOR DIFFUSION AT 19 C BY COMBINING 1.5 UL OF
REMARK 280 PROTEIN SOLUTION (20 MM MES PH 6.0, 150 MM NACL AND 0.5 MM TCEP)
REMARK 280 AT 20 MG/ML WITH 1.5 UL OF RESERVOIR SOLUTION (0.1 M TRIS PH 8.5
REMARK 280 AND 24% PEG 10,000), VAPOR DIFFUSION, HANGING DROP, TEMPERATURE
REMARK 280 292K
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 13.73100
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 79.90300
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 51.45150
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 79.90300
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 13.73100
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 51.45150
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 1300 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 11730 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -9.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, 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
REMARK 350 BIOMOLECULE: 2
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 1220 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 11910 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -7.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, 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 B -5
REMARK 465 GLY C -2
REMARK 465 SER C -1
REMARK 465 HIS C 0
REMARK 465 ARG C 74
REMARK 465 GLY C 75
REMARK 465 GLY C 76
REMARK 465 GLY D -2
REMARK 465 SER D -1
REMARK 465 ARG D 74
REMARK 465 GLY D 75
REMARK 465 GLY D 76
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 SER A -4 -66.64 -20.35
REMARK 500 ILE A 88 -7.44 -59.14
REMARK 500 ARG A 90 -106.08 -134.95
REMARK 500 ASP A 130 79.07 -160.06
REMARK 500 ARG B 90 -111.59 -138.01
REMARK 500 ALA C 46 54.95 28.43
REMARK 500 LYS C 63 125.30 -38.68
REMARK 500
REMARK 500 REMARK: NULL
DBREF 3PTF A 1 147 UNP P51668 UB2D1_HUMAN 1 147
DBREF 3PTF B 1 147 UNP P51668 UB2D1_HUMAN 1 147
DBREF 3PTF C 1 76 UNP P0CG47 UBB_HUMAN 1 76
DBREF 3PTF D 1 76 UNP P0CG47 UBB_HUMAN 1 76
SEQADV 3PTF GLY A -5 UNP P51668 EXPRESSION TAG
SEQADV 3PTF SER A -4 UNP P51668 EXPRESSION TAG
SEQADV 3PTF HIS A -3 UNP P51668 EXPRESSION TAG
SEQADV 3PTF MET A -2 UNP P51668 EXPRESSION TAG
SEQADV 3PTF LEU A -1 UNP P51668 EXPRESSION TAG
SEQADV 3PTF GLU A 0 UNP P51668 EXPRESSION TAG
SEQADV 3PTF GLY B -5 UNP P51668 EXPRESSION TAG
SEQADV 3PTF SER B -4 UNP P51668 EXPRESSION TAG
SEQADV 3PTF HIS B -3 UNP P51668 EXPRESSION TAG
SEQADV 3PTF MET B -2 UNP P51668 EXPRESSION TAG
SEQADV 3PTF LEU B -1 UNP P51668 EXPRESSION TAG
SEQADV 3PTF GLU B 0 UNP P51668 EXPRESSION TAG
SEQADV 3PTF GLY C -2 UNP P0CG47 EXPRESSION TAG
SEQADV 3PTF SER C -1 UNP P0CG47 EXPRESSION TAG
SEQADV 3PTF HIS C 0 UNP P0CG47 EXPRESSION TAG
SEQADV 3PTF GLY D -2 UNP P0CG47 EXPRESSION TAG
SEQADV 3PTF SER D -1 UNP P0CG47 EXPRESSION TAG
SEQADV 3PTF HIS D 0 UNP P0CG47 EXPRESSION TAG
SEQRES 1 A 153 GLY SER HIS MET LEU GLU MET ALA LEU LYS ARG ILE GLN
SEQRES 2 A 153 LYS GLU LEU SER ASP LEU GLN ARG ASP PRO PRO ALA HIS
SEQRES 3 A 153 CYS SER ALA GLY PRO VAL GLY ASP ASP LEU PHE HIS TRP
SEQRES 4 A 153 GLN ALA THR ILE MET GLY PRO PRO ASP SER ALA TYR GLN
SEQRES 5 A 153 GLY GLY VAL PHE PHE LEU THR VAL HIS PHE PRO THR ASP
SEQRES 6 A 153 TYR PRO PHE LYS PRO PRO LYS ILE ALA PHE THR THR LYS
SEQRES 7 A 153 ILE TYR HIS PRO ASN ILE ASN SER ASN GLY SER ILE CYS
SEQRES 8 A 153 LEU ASP ILE LEU ARG SER GLN TRP SER PRO ALA LEU THR
SEQRES 9 A 153 VAL SER LYS VAL LEU LEU SER ILE CYS SER LEU LEU CYS
SEQRES 10 A 153 ASP PRO ASN PRO ASP ASP PRO LEU VAL PRO ASP ILE ALA
SEQRES 11 A 153 GLN ILE TYR LYS SER ASP LYS GLU LYS TYR ASN ARG HIS
SEQRES 12 A 153 ALA ARG GLU TRP THR GLN LYS TYR ALA MET
SEQRES 1 B 153 GLY SER HIS MET LEU GLU MET ALA LEU LYS ARG ILE GLN
SEQRES 2 B 153 LYS GLU LEU SER ASP LEU GLN ARG ASP PRO PRO ALA HIS
SEQRES 3 B 153 CYS SER ALA GLY PRO VAL GLY ASP ASP LEU PHE HIS TRP
SEQRES 4 B 153 GLN ALA THR ILE MET GLY PRO PRO ASP SER ALA TYR GLN
SEQRES 5 B 153 GLY GLY VAL PHE PHE LEU THR VAL HIS PHE PRO THR ASP
SEQRES 6 B 153 TYR PRO PHE LYS PRO PRO LYS ILE ALA PHE THR THR LYS
SEQRES 7 B 153 ILE TYR HIS PRO ASN ILE ASN SER ASN GLY SER ILE CYS
SEQRES 8 B 153 LEU ASP ILE LEU ARG SER GLN TRP SER PRO ALA LEU THR
SEQRES 9 B 153 VAL SER LYS VAL LEU LEU SER ILE CYS SER LEU LEU CYS
SEQRES 10 B 153 ASP PRO ASN PRO ASP ASP PRO LEU VAL PRO ASP ILE ALA
SEQRES 11 B 153 GLN ILE TYR LYS SER ASP LYS GLU LYS TYR ASN ARG HIS
SEQRES 12 B 153 ALA ARG GLU TRP THR GLN LYS TYR ALA MET
SEQRES 1 C 79 GLY SER HIS MET GLN ILE PHE VAL LYS THR LEU THR GLY
SEQRES 2 C 79 LYS THR ILE THR LEU GLU VAL GLU PRO SER ASP THR ILE
SEQRES 3 C 79 GLU ASN VAL LYS ALA LYS ILE GLN ASP LYS GLU GLY ILE
SEQRES 4 C 79 PRO PRO ASP GLN GLN ARG LEU ILE PHE ALA GLY LYS GLN
SEQRES 5 C 79 LEU GLU ASP GLY ARG THR LEU SER ASP TYR ASN ILE GLN
SEQRES 6 C 79 LYS GLU SER THR LEU HIS LEU VAL LEU ARG LEU ARG GLY
SEQRES 7 C 79 GLY
SEQRES 1 D 79 GLY SER HIS MET GLN ILE PHE VAL LYS THR LEU THR GLY
SEQRES 2 D 79 LYS THR ILE THR LEU GLU VAL GLU PRO SER ASP THR ILE
SEQRES 3 D 79 GLU ASN VAL LYS ALA LYS ILE GLN ASP LYS GLU GLY ILE
SEQRES 4 D 79 PRO PRO ASP GLN GLN ARG LEU ILE PHE ALA GLY LYS GLN
SEQRES 5 D 79 LEU GLU ASP GLY ARG THR LEU SER ASP TYR ASN ILE GLN
SEQRES 6 D 79 LYS GLU SER THR LEU HIS LEU VAL LEU ARG LEU ARG GLY
SEQRES 7 D 79 GLY
FORMUL 5 HOH *40(H2 O)
HELIX 1 1 GLY A -5 ASP A 16 1 22
HELIX 2 2 LEU A 86 ARG A 90 5 5
HELIX 3 3 THR A 98 ASP A 112 1 15
HELIX 4 4 VAL A 120 ASP A 130 1 11
HELIX 5 5 ASP A 130 ALA A 146 1 17
HELIX 6 6 SER B -4 ASP B 16 1 21
HELIX 7 7 LEU B 86 ARG B 90 5 5
HELIX 8 8 THR B 98 ASP B 112 1 15
HELIX 9 9 VAL B 120 ASP B 130 1 11
HELIX 10 10 ASP B 130 ALA B 146 1 17
HELIX 11 11 THR C 22 GLY C 35 1 14
HELIX 12 12 PRO C 37 ASP C 39 5 3
HELIX 13 13 LEU C 56 ASN C 60 5 5
HELIX 14 14 THR D 22 GLY D 35 1 14
HELIX 15 15 PRO D 37 ASP D 39 5 3
SHEET 1 A 4 CYS A 21 PRO A 25 0
SHEET 2 A 4 HIS A 32 MET A 38 -1 O THR A 36 N SER A 22
SHEET 3 A 4 VAL A 49 HIS A 55 -1 O PHE A 50 N ILE A 37
SHEET 4 A 4 LYS A 66 PHE A 69 -1 O LYS A 66 N HIS A 55
SHEET 1 B 4 CYS B 21 PRO B 25 0
SHEET 2 B 4 HIS B 32 MET B 38 -1 O THR B 36 N SER B 22
SHEET 3 B 4 VAL B 49 HIS B 55 -1 O PHE B 50 N ILE B 37
SHEET 4 B 4 LYS B 66 PHE B 69 -1 O ALA B 68 N THR B 53
SHEET 1 C 5 THR C 12 GLU C 16 0
SHEET 2 C 5 GLN C 2 LYS C 6 -1 N VAL C 5 O ILE C 13
SHEET 3 C 5 THR C 66 LEU C 71 1 O LEU C 67 N LYS C 6
SHEET 4 C 5 GLN C 41 PHE C 45 -1 N ARG C 42 O VAL C 70
SHEET 5 C 5 LYS C 48 GLN C 49 -1 O LYS C 48 N PHE C 45
SHEET 1 D 5 THR D 12 VAL D 17 0
SHEET 2 D 5 MET D 1 LYS D 6 -1 N VAL D 5 O ILE D 13
SHEET 3 D 5 THR D 66 LEU D 71 1 O LEU D 69 N LYS D 6
SHEET 4 D 5 GLN D 41 PHE D 45 -1 N ILE D 44 O HIS D 68
SHEET 5 D 5 LYS D 48 GLN D 49 -1 O LYS D 48 N PHE D 45
CISPEP 1 TYR A 60 PRO A 61 0 10.01
CISPEP 2 TYR B 60 PRO B 61 0 8.97
CRYST1 27.462 102.903 159.806 90.00 90.00 90.00 P 21 21 21 8
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 0.036414 0.000000 0.000000 0.00000
SCALE2 0.000000 0.009718 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006258 0.00000
(ATOM LINES ARE NOT SHOWN.)
END