HEADER DNA BINDING PROTEIN 05-DEC-13 4CI3
TITLE STRUCTURE OF THE DDB1-CRBN E3 UBIQUITIN LIGASE BOUND TO POMALIDOMIDE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: DNA DAMAGE-BINDING PROTEIN 1;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: DDB P127 SUBUNIT, DNA DAMAGE-BINDING PROTEIN A, DDBA,
COMPND 5 DAMAGE-SPECIFIC DNA-BINDING PROTEIN 1, HBV X-ASSOCIATED PROTEIN 1,
COMPND 6 XAP- 1, UV-DAMAGED DNA-BINDING FACTOR, UV-DAMAGED DNA-BINDING PROTEIN
COMPND 7 1, UV-DDB 1, XPE-BINDING FACTOR, XPE-BF, XERODERMA PIGMENTOSUM GROUP
COMPND 8 E-COMPLEMENTING PROTEIN, XPCE, DNA DAMAGE BINDING PROTEIN 1;
COMPND 9 ENGINEERED: YES;
COMPND 10 MOL_ID: 2;
COMPND 11 MOLECULE: PROTEIN CEREBLON;
COMPND 12 CHAIN: B;
COMPND 13 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 EXPRESSION_SYSTEM: TRICHOPLUSIA NI;
SOURCE 6 EXPRESSION_SYSTEM_COMMON: CABBAGE LOOPER;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 7111;
SOURCE 8 EXPRESSION_SYSTEM_CELL_LINE: HIGH FIVE;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PFASTBAC DUAL;
SOURCE 11 MOL_ID: 2;
SOURCE 12 ORGANISM_SCIENTIFIC: GALLUS GALLUS;
SOURCE 13 ORGANISM_COMMON: CHICKEN;
SOURCE 14 ORGANISM_TAXID: 9031;
SOURCE 15 EXPRESSION_SYSTEM: TRICHOPLUSIA NI;
SOURCE 16 EXPRESSION_SYSTEM_COMMON: CABBAGE LOOPER;
SOURCE 17 EXPRESSION_SYSTEM_TAXID: 7111;
SOURCE 18 EXPRESSION_SYSTEM_CELL_LINE: HIGH FIVE;
SOURCE 19 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS;
SOURCE 20 EXPRESSION_SYSTEM_PLASMID: PFASTBAC DUAL
KEYWDS DNA BINDING PROTEIN, DDB1, CRBN, CULLIN, E3 LIGASE, UBIQUITIN,
KEYWDS 2 THALIDOMIDE, CONTERGAN
EXPDTA X-RAY DIFFRACTION
AUTHOR E.S.FISCHER,K.BOEHM,N.H.THOMA
REVDAT 5 20-DEC-23 4CI3 1 REMARK LINK
REVDAT 4 27-MAR-19 4CI3 1 SOURCE
REVDAT 3 13-AUG-14 4CI3 1 JRNL
REVDAT 2 30-JUL-14 4CI3 1 JRNL
REVDAT 1 16-JUL-14 4CI3 0
JRNL AUTH E.S.FISCHER,K.BOHM,J.R.LYDEARD,H.YANG,M.B.STADLER,
JRNL AUTH 2 S.CAVADINI,J.NAGEL,F.SERLUCA,V.ACKER,G.M.LINGARAJU,
JRNL AUTH 3 R.B.TICHKULE,M.SCHEBESTA,W.C.FORRESTER,M.SCHIRLE,
JRNL AUTH 4 U.HASSIEPEN,J.OTTL,M.HILD,R.E.J.BECKWITH,J.W.HARPER,
JRNL AUTH 5 J.L.JENKINS,N.H.THOMA
JRNL TITL STRUCTURE OF THE DDB1-CRBN E3 UBIQUITIN LIGASE IN COMPLEX
JRNL TITL 2 WITH THALIDOMIDE.
JRNL REF NATURE V. 512 49 2014
JRNL REFN ISSN 0028-0836
JRNL PMID 25043012
JRNL DOI 10.1038/NATURE13527
REMARK 2
REMARK 2 RESOLUTION. 3.50 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : BUSTER 2.11.4
REMARK 3 AUTHORS : BRICOGNE,BLANC,BRANDL,FLENSBURG,KELLER,
REMARK 3 : PACIOREK,ROVERSI,SHARFF,SMART,VONRHEIN,
REMARK 3 : WOMACK,MATTHEWS,TEN EYCK,TRONRUD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 3.50
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 29.63
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 84.5
REMARK 3 NUMBER OF REFLECTIONS : 25108
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) : 0.211
REMARK 3 FREE R VALUE : 0.235
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 1256
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : NULL
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 13
REMARK 3 BIN RESOLUTION RANGE HIGH (ANGSTROMS) : 3.50
REMARK 3 BIN RESOLUTION RANGE LOW (ANGSTROMS) : 3.64
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 84.52
REMARK 3 REFLECTIONS IN BIN (WORKING + TEST SET) : 2778
REMARK 3 BIN R VALUE (WORKING + TEST SET) : 0.2403
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 2639
REMARK 3 BIN R VALUE (WORKING SET) : 0.2402
REMARK 3 BIN FREE R VALUE : 0.2423
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 5.00
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 139
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 11389
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 21
REMARK 3 SOLVENT ATOMS : 0
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 88.20
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 139.2
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 10.70410
REMARK 3 B22 (A**2) : 10.70410
REMARK 3 B33 (A**2) : -21.40820
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 COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.921
REMARK 3 DPI (BLOW EQ-10) BASED ON R VALUE (A) : NULL
REMARK 3 DPI (BLOW EQ-9) BASED ON FREE R VALUE (A) : 0.567
REMARK 3 DPI (CRUICKSHANK) BASED ON R VALUE (A) : NULL
REMARK 3 DPI (CRUICKSHANK) BASED ON FREE R VALUE (A) : NULL
REMARK 3
REMARK 3 REFERENCES: BLOW, D. (2002) ACTA CRYST D58, 792-797
REMARK 3 CRUICKSHANK, D.W.J. (1999) ACTA CRYST D55, 583-601
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.925
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.916
REMARK 3
REMARK 3 NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15
REMARK 3 TERM COUNT WEIGHT FUNCTION.
REMARK 3 BOND LENGTHS : 11640 ; 2.000 ; HARMONIC
REMARK 3 BOND ANGLES : 15803 ; 2.000 ; HARMONIC
REMARK 3 TORSION ANGLES : 4005 ; 4.000 ; SINUSOIDAL
REMARK 3 TRIGONAL CARBON PLANES : 289 ; 2.000 ; HARMONIC
REMARK 3 GENERAL PLANES : 1679 ; 5.000 ; HARMONIC
REMARK 3 ISOTROPIC THERMAL FACTORS : 11640 ; 20.000 ; HARMONIC
REMARK 3 BAD NON-BONDED CONTACTS : 2 ; 5.000 ; SEMIHARMONIC
REMARK 3 IMPROPER TORSIONS : NULL ; NULL ; NULL
REMARK 3 PSEUDOROTATION ANGLES : NULL ; NULL ; NULL
REMARK 3 CHIRAL IMPROPER TORSION : 1553 ; 5.000 ; SEMIHARMONIC
REMARK 3 SUM OF OCCUPANCIES : NULL ; NULL ; NULL
REMARK 3 UTILITY DISTANCES : NULL ; NULL ; NULL
REMARK 3 UTILITY ANGLES : NULL ; NULL ; NULL
REMARK 3 UTILITY TORSION : NULL ; NULL ; NULL
REMARK 3 IDEAL-DIST CONTACT TERM : 12762 ; 4.000 ; SEMIHARMONIC
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.008
REMARK 3 BOND ANGLES (DEGREES) : 1.16
REMARK 3 PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 2.69
REMARK 3 OTHER TORSION ANGLES (DEGREES) : 17.70
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 2
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: NULL
REMARK 3 ORIGIN FOR THE GROUP (A): -72.8209 -29.3981 -4.3369
REMARK 3 T TENSOR
REMARK 3 T11: -0.1836 T22: -0.0740
REMARK 3 T33: -0.3040 T12: 0.1177
REMARK 3 T13: -0.0316 T23: -0.1937
REMARK 3 L TENSOR
REMARK 3 L11: 1.2000 L22: 1.5445
REMARK 3 L33: 0.9342 L12: 0.9528
REMARK 3 L13: -0.0998 L23: 0.1407
REMARK 3 S TENSOR
REMARK 3 S11: 0.0646 S12: -0.3325 S13: -0.0915
REMARK 3 S21: 0.0651 S22: -0.0446 S23: 0.1756
REMARK 3 S31: -0.1405 S32: -0.3444 S33: -0.0200
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: NULL
REMARK 3 ORIGIN FOR THE GROUP (A): -24.6365 -5.2858 -9.7386
REMARK 3 T TENSOR
REMARK 3 T11: -0.0235 T22: 0.0333
REMARK 3 T33: -0.2944 T12: -0.0142
REMARK 3 T13: 0.0001 T23: -0.1266
REMARK 3 L TENSOR
REMARK 3 L11: 3.4794 L22: 1.6136
REMARK 3 L33: 0.5110 L12: 1.0780
REMARK 3 L13: -0.2246 L23: -0.5907
REMARK 3 S TENSOR
REMARK 3 S11: -0.1828 S12: 0.3799 S13: -0.0040
REMARK 3 S21: -0.0612 S22: -0.0382 S23: 0.3228
REMARK 3 S31: 0.0565 S32: -0.2342 S33: 0.2210
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 4CI3 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 05-DEC-13.
REMARK 100 THE DEPOSITION ID IS D_1290059151.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 14-NOV-12
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SLS
REMARK 200 BEAMLINE : X10SA
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.99997
REMARK 200 MONOCHROMATOR : SI(111) MONOCHROMATOR
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 25109
REMARK 200 RESOLUTION RANGE HIGH (A) : 3.500
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 (%) : 84.4
REMARK 200 DATA REDUNDANCY : 2.600
REMARK 200 R MERGE (I) : 0.14000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 7.0500
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.50
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.59
REMARK 200 COMPLETENESS FOR SHELL (%) : 83.4
REMARK 200 DATA REDUNDANCY IN SHELL : 2.50
REMARK 200 R MERGE FOR SHELL (I) : 1.31000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 0.910
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: PDB ENTRY 3EI3, CHAIN A
REMARK 200
REMARK 200 REMARK: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 65.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.51
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PROTEIN WAS CRYSTALLIZED FROM 100 MM
REMARK 280 NA-CACOCYLATE, 80 MM NAH2PO4, 120 MM K2HPO4, 700 MM TRI-NA
REMARK 280 CITRATE., PH 6.5
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 32 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+2/3
REMARK 290 3555 -X+Y,-X,Z+1/3
REMARK 290 4555 Y,X,-Z
REMARK 290 5555 X-Y,-Y,-Z+1/3
REMARK 290 6555 -X,-X+Y,-Z+2/3
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 91.95333
REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 45.97667
REMARK 290 SMTRY1 4 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 4 0.866025 0.500000 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 0.00000
REMARK 290 SMTRY2 5 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 45.97667
REMARK 290 SMTRY1 6 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 6 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 91.95333
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 4470 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 59880 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -19.1 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 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 -17
REMARK 465 HIS A -16
REMARK 465 HIS A -15
REMARK 465 HIS A -14
REMARK 465 HIS A -13
REMARK 465 HIS A -12
REMARK 465 HIS A -11
REMARK 465 ARG A -10
REMARK 465 ARG A -9
REMARK 465 LEU A -8
REMARK 465 VAL A -7
REMARK 465 PRO A -6
REMARK 465 ARG A -5
REMARK 465 GLY A -4
REMARK 465 SER A -3
REMARK 465 GLY A -2
REMARK 465 GLY A -1
REMARK 465 ARG A 0
REMARK 465 MET A 1
REMARK 465 ASP A 146
REMARK 465 ARG A 147
REMARK 465 ASP A 148
REMARK 465 ASN A 149
REMARK 465 GLU A 286
REMARK 465 LYS A 287
REMARK 465 GLU A 288
REMARK 465 GLU A 289
REMARK 465 GLN A 290
REMARK 465 MET A 291
REMARK 465 ASP A 292
REMARK 465 GLY A 293
REMARK 465 THR A 294
REMARK 465 VAL A 295
REMARK 465 THR A 296
REMARK 465 LEU A 297
REMARK 465 LYS A 298
REMARK 465 ASP A 299
REMARK 465 SER A 772
REMARK 465 SER A 773
REMARK 465 SER A 774
REMARK 465 THR A 775
REMARK 465 ALA A 776
REMARK 465 PRO A 777
REMARK 465 HIS A 778
REMARK 465 GLU A 779
REMARK 465 THR A 780
REMARK 465 SER A 781
REMARK 465 PHE A 782
REMARK 465 GLY A 783
REMARK 465 ASP A 980
REMARK 465 SER A 981
REMARK 465 ALA A 982
REMARK 465 ALA A 983
REMARK 465 GLN A 1015
REMARK 465 ASN A 1016
REMARK 465 LEU A 1017
REMARK 465 GLY A 1018
REMARK 465 GLU A 1019
REMARK 465 THR A 1020
REMARK 465 SER A 1021
REMARK 465 TYR A 1114
REMARK 465 ASP A 1115
REMARK 465 ASP A 1116
REMARK 465 GLY A 1117
REMARK 465 SER A 1118
REMARK 465 GLY A 1119
REMARK 465 MET A 1120
REMARK 465 MET B -23
REMARK 465 ASP B -22
REMARK 465 TRP B -21
REMARK 465 SER B -20
REMARK 465 HIS B -19
REMARK 465 PRO B -18
REMARK 465 GLN B -17
REMARK 465 PHE B -16
REMARK 465 GLU B -15
REMARK 465 LYS B -14
REMARK 465 SER B -13
REMARK 465 ALA B -12
REMARK 465 VAL B -11
REMARK 465 ASP B -10
REMARK 465 GLU B -9
REMARK 465 ASN B -8
REMARK 465 LEU B -7
REMARK 465 TYR B -6
REMARK 465 PHE B -5
REMARK 465 GLN B -4
REMARK 465 GLY B -3
REMARK 465 GLY B -2
REMARK 465 GLY B -1
REMARK 465 ARG B 0
REMARK 465 MET B 1
REMARK 465 ALA B 2
REMARK 465 ALA B 3
REMARK 465 GLU B 4
REMARK 465 GLU B 5
REMARK 465 GLY B 6
REMARK 465 GLY B 7
REMARK 465 ASP B 8
REMARK 465 GLY B 9
REMARK 465 ARG B 10
REMARK 465 ARG B 11
REMARK 465 ASN B 12
REMARK 465 MET B 13
REMARK 465 GLY B 14
REMARK 465 ASN B 15
REMARK 465 PRO B 16
REMARK 465 PRO B 17
REMARK 465 PRO B 18
REMARK 465 PRO B 19
REMARK 465 ALA B 20
REMARK 465 PRO B 21
REMARK 465 ALA B 22
REMARK 465 GLU B 23
REMARK 465 SER B 24
REMARK 465 GLU B 25
REMARK 465 GLU B 26
REMARK 465 GLU B 27
REMARK 465 ASP B 28
REMARK 465 ASP B 29
REMARK 465 ASN B 30
REMARK 465 GLU B 31
REMARK 465 MET B 32
REMARK 465 GLU B 33
REMARK 465 VAL B 34
REMARK 465 GLU B 35
REMARK 465 ASP B 36
REMARK 465 GLN B 37
REMARK 465 ASP B 38
REMARK 465 GLY B 39
REMARK 465 LYS B 40
REMARK 465 GLU B 41
REMARK 465 ALA B 42
REMARK 465 GLU B 43
REMARK 465 LYS B 44
REMARK 465 PRO B 45
REMARK 465 ASN B 46
REMARK 465 PHE B 209
REMARK 465 PRO B 210
REMARK 465 SER B 211
REMARK 465 SER B 212
REMARK 465 LYS B 213
REMARK 465 PRO B 214
REMARK 465 LYS B 215
REMARK 465 VAL B 216
REMARK 465 TRP B 217
REMARK 465 GLN B 218
REMARK 465 ASP B 219
REMARK 465 ILE B 428
REMARK 465 PRO B 429
REMARK 465 GLU B 430
REMARK 465 ALA B 431
REMARK 465 GLU B 432
REMARK 465 ASP B 433
REMARK 465 GLU B 434
REMARK 465 LEU B 435
REMARK 465 GLY B 436
REMARK 465 HIS B 437
REMARK 465 ASP B 438
REMARK 465 ARG B 439
REMARK 465 SER B 440
REMARK 465 PRO B 441
REMARK 465 LEU B 442
REMARK 465 LEU B 443
REMARK 465 CYS B 444
REMARK 465 LEU B 445
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 GLU A 27 CG CD OE1 OE2
REMARK 470 LYS A 70 CG CD CE NZ
REMARK 470 LYS A 74 CG CD CE NZ
REMARK 470 GLU A 96 CG CD OE1 OE2
REMARK 470 ARG A 114 CG CD NE CZ NH1 NH2
REMARK 470 GLU A 127 CG CD OE1 OE2
REMARK 470 ARG A 129 CG CD NE CZ NH1 NH2
REMARK 470 LEU A 145 CG CD1 CD2
REMARK 470 LYS A 150 CG CD CE NZ
REMARK 470 LYS A 153 CG CD CE NZ
REMARK 470 ARG A 158 CG CD NE CZ NH1 NH2
REMARK 470 GLN A 174 CG CD OE1 NE2
REMARK 470 VAL A 195 CG1 CG2
REMARK 470 ARG A 198 CG CD NE CZ NH1 NH2
REMARK 470 GLU A 199 CG CD OE1 OE2
REMARK 470 LYS A 200 CG CD CE NZ
REMARK 470 LYS A 208 CG CD CE NZ
REMARK 470 GLU A 224 CG CD OE1 OE2
REMARK 470 ASP A 243 CG OD1 OD2
REMARK 470 LYS A 254 CG CD CE NZ
REMARK 470 ASP A 318 CG OD1 OD2
REMARK 470 VAL A 338 CG1 CG2
REMARK 470 GLU A 420 CG CD OE1 OE2
REMARK 470 ARG A 589 CG CD NE CZ NH1 NH2
REMARK 470 LYS A 769 CG CD CE NZ
REMARK 470 GLU A 800 CG CD OE1 OE2
REMARK 470 GLN A 852 CG CD OE1 NE2
REMARK 470 ASP A 855 CG OD1 OD2
REMARK 470 LYS A 857 CG CD CE NZ
REMARK 470 GLN A 859 CG CD OE1 NE2
REMARK 470 GLU A 892 CG CD OE1 OE2
REMARK 470 LYS A 936 CG CD CE NZ
REMARK 470 MET A 938 CG SD CE
REMARK 470 GLU A 988 CG CD OE1 OE2
REMARK 470 ARG A1080 CG CD NE CZ NH1 NH2
REMARK 470 MET B 47 CG SD CE
REMARK 470 MET B 89 CG SD CE
REMARK 470 ARG B 172 CG CD NE CZ NH1 NH2
REMARK 470 LYS B 182 CG CD CE NZ
REMARK 470 ARG B 220 CG CD NE CZ NH1 NH2
REMARK 470 LYS B 271 CG CD CE NZ
REMARK 470 ARG B 427 CG CD NE CZ NH1 NH2
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 THR A 24 -74.68 -68.11
REMARK 500 LYS A 35 60.22 -114.79
REMARK 500 ASN A 36 -89.84 67.26
REMARK 500 ALA A 46 -30.69 72.53
REMARK 500 TYR A 58 54.19 -91.62
REMARK 500 LYS A 70 -129.52 54.43
REMARK 500 LYS A 74 -154.25 -154.70
REMARK 500 PRO A 144 99.72 -68.93
REMARK 500 ARG A 158 95.48 -66.86
REMARK 500 LYS A 204 126.93 -25.56
REMARK 500 ASN A 241 59.87 -152.97
REMARK 500 ASP A 318 -138.06 53.80
REMARK 500 MET A 350 -69.86 -97.68
REMARK 500 GLU A 368 -95.62 66.86
REMARK 500 PHE A 382 -132.56 56.50
REMARK 500 VAL A 430 108.52 -59.30
REMARK 500 ALA A 495 19.93 53.95
REMARK 500 ASN A 504 -130.10 -112.88
REMARK 500 THR A 562 -60.06 60.64
REMARK 500 SER A 653 -167.25 -163.81
REMARK 500 GLU A 675 146.85 -174.67
REMARK 500 ASN A 695 -151.92 -118.18
REMARK 500 ASP A 705 -162.32 -71.13
REMARK 500 THR A 745 49.90 -77.61
REMARK 500 GLN A 759 42.80 -94.56
REMARK 500 LYS A 769 -9.56 -141.60
REMARK 500 ASN A 810 -1.91 66.84
REMARK 500 LYS A 867 36.09 -87.90
REMARK 500 ASN A 877 66.32 39.18
REMARK 500 ASN A 885 -109.76 55.05
REMARK 500 GLU A 902 -83.99 -102.11
REMARK 500 ASN A 908 -12.03 70.32
REMARK 500 ALA A 911 58.82 -90.57
REMARK 500 LYS A 917 107.72 -163.20
REMARK 500 ALA A 971 49.58 80.20
REMARK 500 ARG A1080 -84.34 -83.71
REMARK 500 ASP B 77 -1.96 60.91
REMARK 500 LYS B 117 -122.62 -143.97
REMARK 500 ARG B 119 -0.51 64.95
REMARK 500 ARG B 163 -66.63 -124.16
REMARK 500 GLU B 170 134.02 -173.10
REMARK 500 ALA B 221 -28.81 76.37
REMARK 500 CYS B 236 3.72 -69.35
REMARK 500 THR B 321 -73.34 -138.16
REMARK 500 GLN B 329 -39.06 66.93
REMARK 500 CYS B 368 -74.39 -113.16
REMARK 500 PRO B 426 1.93 -67.67
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 ZN B1428 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS B 325 SG
REMARK 620 2 CYS B 328 SG 105.3
REMARK 620 3 CYS B 393 SG 103.3 107.3
REMARK 620 4 CYS B 396 SG 102.1 125.7 110.6
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 ZN B 1428
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE Y70 B 1429
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4CI1 RELATED DB: PDB
REMARK 900 RELATED ID: 4CI2 RELATED DB: PDB
REMARK 900 RELATED ID: 3EI1 RELATED DB: PDB
REMARK 900 RELATED ID: 3EI2 RELATED DB: PDB
REMARK 900 RELATED ID: 3EI3 RELATED DB: PDB
REMARK 900 RELATED ID: 3EI4 RELATED DB: PDB
REMARK 900 RELATED ID: 2B5M RELATED DB: PDB
REMARK 900 RELATED ID: 2B5L RELATED DB: PDB
REMARK 900 RELATED ID: 3E0C RELATED DB: PDB
REMARK 900 RELATED ID: 4A11 RELATED DB: PDB
DBREF 4CI3 A 1 1140 UNP Q16531 DDB1_HUMAN 1 1140
DBREF 4CI3 B 1 445 UNP P0CF65 CRBN_CHICK 1 445
SEQADV 4CI3 MET A -17 UNP Q16531 EXPRESSION TAG
SEQADV 4CI3 HIS A -16 UNP Q16531 EXPRESSION TAG
SEQADV 4CI3 HIS A -15 UNP Q16531 EXPRESSION TAG
SEQADV 4CI3 HIS A -14 UNP Q16531 EXPRESSION TAG
SEQADV 4CI3 HIS A -13 UNP Q16531 EXPRESSION TAG
SEQADV 4CI3 HIS A -12 UNP Q16531 EXPRESSION TAG
SEQADV 4CI3 HIS A -11 UNP Q16531 EXPRESSION TAG
SEQADV 4CI3 ARG A -10 UNP Q16531 EXPRESSION TAG
SEQADV 4CI3 ARG A -9 UNP Q16531 EXPRESSION TAG
SEQADV 4CI3 LEU A -8 UNP Q16531 EXPRESSION TAG
SEQADV 4CI3 VAL A -7 UNP Q16531 EXPRESSION TAG
SEQADV 4CI3 PRO A -6 UNP Q16531 EXPRESSION TAG
SEQADV 4CI3 ARG A -5 UNP Q16531 EXPRESSION TAG
SEQADV 4CI3 GLY A -4 UNP Q16531 EXPRESSION TAG
SEQADV 4CI3 SER A -3 UNP Q16531 EXPRESSION TAG
SEQADV 4CI3 GLY A -2 UNP Q16531 EXPRESSION TAG
SEQADV 4CI3 GLY A -1 UNP Q16531 EXPRESSION TAG
SEQADV 4CI3 ARG A 0 UNP Q16531 EXPRESSION TAG
SEQADV 4CI3 MET B -23 UNP P0CF65 EXPRESSION TAG
SEQADV 4CI3 ASP B -22 UNP P0CF65 EXPRESSION TAG
SEQADV 4CI3 TRP B -21 UNP P0CF65 EXPRESSION TAG
SEQADV 4CI3 SER B -20 UNP P0CF65 EXPRESSION TAG
SEQADV 4CI3 HIS B -19 UNP P0CF65 EXPRESSION TAG
SEQADV 4CI3 PRO B -18 UNP P0CF65 EXPRESSION TAG
SEQADV 4CI3 GLN B -17 UNP P0CF65 EXPRESSION TAG
SEQADV 4CI3 PHE B -16 UNP P0CF65 EXPRESSION TAG
SEQADV 4CI3 GLU B -15 UNP P0CF65 EXPRESSION TAG
SEQADV 4CI3 LYS B -14 UNP P0CF65 EXPRESSION TAG
SEQADV 4CI3 SER B -13 UNP P0CF65 EXPRESSION TAG
SEQADV 4CI3 ALA B -12 UNP P0CF65 EXPRESSION TAG
SEQADV 4CI3 VAL B -11 UNP P0CF65 EXPRESSION TAG
SEQADV 4CI3 ASP B -10 UNP P0CF65 EXPRESSION TAG
SEQADV 4CI3 GLU B -9 UNP P0CF65 EXPRESSION TAG
SEQADV 4CI3 ASN B -8 UNP P0CF65 EXPRESSION TAG
SEQADV 4CI3 LEU B -7 UNP P0CF65 EXPRESSION TAG
SEQADV 4CI3 TYR B -6 UNP P0CF65 EXPRESSION TAG
SEQADV 4CI3 PHE B -5 UNP P0CF65 EXPRESSION TAG
SEQADV 4CI3 GLN B -4 UNP P0CF65 EXPRESSION TAG
SEQADV 4CI3 GLY B -3 UNP P0CF65 EXPRESSION TAG
SEQADV 4CI3 GLY B -2 UNP P0CF65 EXPRESSION TAG
SEQADV 4CI3 GLY B -1 UNP P0CF65 EXPRESSION TAG
SEQADV 4CI3 ARG B 0 UNP P0CF65 EXPRESSION TAG
SEQRES 1 A 1158 MET HIS HIS HIS HIS HIS HIS ARG ARG LEU VAL PRO ARG
SEQRES 2 A 1158 GLY SER GLY GLY ARG MET SER TYR ASN TYR VAL VAL THR
SEQRES 3 A 1158 ALA GLN LYS PRO THR ALA VAL ASN GLY CYS VAL THR GLY
SEQRES 4 A 1158 HIS PHE THR SER ALA GLU ASP LEU ASN LEU LEU ILE ALA
SEQRES 5 A 1158 LYS ASN THR ARG LEU GLU ILE TYR VAL VAL THR ALA GLU
SEQRES 6 A 1158 GLY LEU ARG PRO VAL LYS GLU VAL GLY MET TYR GLY LYS
SEQRES 7 A 1158 ILE ALA VAL MET GLU LEU PHE ARG PRO LYS GLY GLU SER
SEQRES 8 A 1158 LYS ASP LEU LEU PHE ILE LEU THR ALA LYS TYR ASN ALA
SEQRES 9 A 1158 CYS ILE LEU GLU TYR LYS GLN SER GLY GLU SER ILE ASP
SEQRES 10 A 1158 ILE ILE THR ARG ALA HIS GLY ASN VAL GLN ASP ARG ILE
SEQRES 11 A 1158 GLY ARG PRO SER GLU THR GLY ILE ILE GLY ILE ILE ASP
SEQRES 12 A 1158 PRO GLU CYS ARG MET ILE GLY LEU ARG LEU TYR ASP GLY
SEQRES 13 A 1158 LEU PHE LYS VAL ILE PRO LEU ASP ARG ASP ASN LYS GLU
SEQRES 14 A 1158 LEU LYS ALA PHE ASN ILE ARG LEU GLU GLU LEU HIS VAL
SEQRES 15 A 1158 ILE ASP VAL LYS PHE LEU TYR GLY CYS GLN ALA PRO THR
SEQRES 16 A 1158 ILE CYS PHE VAL TYR GLN ASP PRO GLN GLY ARG HIS VAL
SEQRES 17 A 1158 LYS THR TYR GLU VAL SER LEU ARG GLU LYS GLU PHE ASN
SEQRES 18 A 1158 LYS GLY PRO TRP LYS GLN GLU ASN VAL GLU ALA GLU ALA
SEQRES 19 A 1158 SER MET VAL ILE ALA VAL PRO GLU PRO PHE GLY GLY ALA
SEQRES 20 A 1158 ILE ILE ILE GLY GLN GLU SER ILE THR TYR HIS ASN GLY
SEQRES 21 A 1158 ASP LYS TYR LEU ALA ILE ALA PRO PRO ILE ILE LYS GLN
SEQRES 22 A 1158 SER THR ILE VAL CYS HIS ASN ARG VAL ASP PRO ASN GLY
SEQRES 23 A 1158 SER ARG TYR LEU LEU GLY ASP MET GLU GLY ARG LEU PHE
SEQRES 24 A 1158 MET LEU LEU LEU GLU LYS GLU GLU GLN MET ASP GLY THR
SEQRES 25 A 1158 VAL THR LEU LYS ASP LEU ARG VAL GLU LEU LEU GLY GLU
SEQRES 26 A 1158 THR SER ILE ALA GLU CYS LEU THR TYR LEU ASP ASN GLY
SEQRES 27 A 1158 VAL VAL PHE VAL GLY SER ARG LEU GLY ASP SER GLN LEU
SEQRES 28 A 1158 VAL LYS LEU ASN VAL ASP SER ASN GLU GLN GLY SER TYR
SEQRES 29 A 1158 VAL VAL ALA MET GLU THR PHE THR ASN LEU GLY PRO ILE
SEQRES 30 A 1158 VAL ASP MET CYS VAL VAL ASP LEU GLU ARG GLN GLY GLN
SEQRES 31 A 1158 GLY GLN LEU VAL THR CYS SER GLY ALA PHE LYS GLU GLY
SEQRES 32 A 1158 SER LEU ARG ILE ILE ARG ASN GLY ILE GLY ILE HIS GLU
SEQRES 33 A 1158 HIS ALA SER ILE ASP LEU PRO GLY ILE LYS GLY LEU TRP
SEQRES 34 A 1158 PRO LEU ARG SER ASP PRO ASN ARG GLU THR ASP ASP THR
SEQRES 35 A 1158 LEU VAL LEU SER PHE VAL GLY GLN THR ARG VAL LEU MET
SEQRES 36 A 1158 LEU ASN GLY GLU GLU VAL GLU GLU THR GLU LEU MET GLY
SEQRES 37 A 1158 PHE VAL ASP ASP GLN GLN THR PHE PHE CYS GLY ASN VAL
SEQRES 38 A 1158 ALA HIS GLN GLN LEU ILE GLN ILE THR SER ALA SER VAL
SEQRES 39 A 1158 ARG LEU VAL SER GLN GLU PRO LYS ALA LEU VAL SER GLU
SEQRES 40 A 1158 TRP LYS GLU PRO GLN ALA LYS ASN ILE SER VAL ALA SER
SEQRES 41 A 1158 CYS ASN SER SER GLN VAL VAL VAL ALA VAL GLY ARG ALA
SEQRES 42 A 1158 LEU TYR TYR LEU GLN ILE HIS PRO GLN GLU LEU ARG GLN
SEQRES 43 A 1158 ILE SER HIS THR GLU MET GLU HIS GLU VAL ALA CYS LEU
SEQRES 44 A 1158 ASP ILE THR PRO LEU GLY ASP SER ASN GLY LEU SER PRO
SEQRES 45 A 1158 LEU CYS ALA ILE GLY LEU TRP THR ASP ILE SER ALA ARG
SEQRES 46 A 1158 ILE LEU LYS LEU PRO SER PHE GLU LEU LEU HIS LYS GLU
SEQRES 47 A 1158 MET LEU GLY GLY GLU ILE ILE PRO ARG SER ILE LEU MET
SEQRES 48 A 1158 THR THR PHE GLU SER SER HIS TYR LEU LEU CYS ALA LEU
SEQRES 49 A 1158 GLY ASP GLY ALA LEU PHE TYR PHE GLY LEU ASN ILE GLU
SEQRES 50 A 1158 THR GLY LEU LEU SER ASP ARG LYS LYS VAL THR LEU GLY
SEQRES 51 A 1158 THR GLN PRO THR VAL LEU ARG THR PHE ARG SER LEU SER
SEQRES 52 A 1158 THR THR ASN VAL PHE ALA CYS SER ASP ARG PRO THR VAL
SEQRES 53 A 1158 ILE TYR SER SER ASN HIS LYS LEU VAL PHE SER ASN VAL
SEQRES 54 A 1158 ASN LEU LYS GLU VAL ASN TYR MET CYS PRO LEU ASN SER
SEQRES 55 A 1158 ASP GLY TYR PRO ASP SER LEU ALA LEU ALA ASN ASN SER
SEQRES 56 A 1158 THR LEU THR ILE GLY THR ILE ASP GLU ILE GLN LYS LEU
SEQRES 57 A 1158 HIS ILE ARG THR VAL PRO LEU TYR GLU SER PRO ARG LYS
SEQRES 58 A 1158 ILE CYS TYR GLN GLU VAL SER GLN CYS PHE GLY VAL LEU
SEQRES 59 A 1158 SER SER ARG ILE GLU VAL GLN ASP THR SER GLY GLY THR
SEQRES 60 A 1158 THR ALA LEU ARG PRO SER ALA SER THR GLN ALA LEU SER
SEQRES 61 A 1158 SER SER VAL SER SER SER LYS LEU PHE SER SER SER THR
SEQRES 62 A 1158 ALA PRO HIS GLU THR SER PHE GLY GLU GLU VAL GLU VAL
SEQRES 63 A 1158 HIS ASN LEU LEU ILE ILE ASP GLN HIS THR PHE GLU VAL
SEQRES 64 A 1158 LEU HIS ALA HIS GLN PHE LEU GLN ASN GLU TYR ALA LEU
SEQRES 65 A 1158 SER LEU VAL SER CYS LYS LEU GLY LYS ASP PRO ASN THR
SEQRES 66 A 1158 TYR PHE ILE VAL GLY THR ALA MET VAL TYR PRO GLU GLU
SEQRES 67 A 1158 ALA GLU PRO LYS GLN GLY ARG ILE VAL VAL PHE GLN TYR
SEQRES 68 A 1158 SER ASP GLY LYS LEU GLN THR VAL ALA GLU LYS GLU VAL
SEQRES 69 A 1158 LYS GLY ALA VAL TYR SER MET VAL GLU PHE ASN GLY LYS
SEQRES 70 A 1158 LEU LEU ALA SER ILE ASN SER THR VAL ARG LEU TYR GLU
SEQRES 71 A 1158 TRP THR THR GLU LYS GLU LEU ARG THR GLU CYS ASN HIS
SEQRES 72 A 1158 TYR ASN ASN ILE MET ALA LEU TYR LEU LYS THR LYS GLY
SEQRES 73 A 1158 ASP PHE ILE LEU VAL GLY ASP LEU MET ARG SER VAL LEU
SEQRES 74 A 1158 LEU LEU ALA TYR LYS PRO MET GLU GLY ASN PHE GLU GLU
SEQRES 75 A 1158 ILE ALA ARG ASP PHE ASN PRO ASN TRP MET SER ALA VAL
SEQRES 76 A 1158 GLU ILE LEU ASP ASP ASP ASN PHE LEU GLY ALA GLU ASN
SEQRES 77 A 1158 ALA PHE ASN LEU PHE VAL CYS GLN LYS ASP SER ALA ALA
SEQRES 78 A 1158 THR THR ASP GLU GLU ARG GLN HIS LEU GLN GLU VAL GLY
SEQRES 79 A 1158 LEU PHE HIS LEU GLY GLU PHE VAL ASN VAL PHE CYS HIS
SEQRES 80 A 1158 GLY SER LEU VAL MET GLN ASN LEU GLY GLU THR SER THR
SEQRES 81 A 1158 PRO THR GLN GLY SER VAL LEU PHE GLY THR VAL ASN GLY
SEQRES 82 A 1158 MET ILE GLY LEU VAL THR SER LEU SER GLU SER TRP TYR
SEQRES 83 A 1158 ASN LEU LEU LEU ASP MET GLN ASN ARG LEU ASN LYS VAL
SEQRES 84 A 1158 ILE LYS SER VAL GLY LYS ILE GLU HIS SER PHE TRP ARG
SEQRES 85 A 1158 SER PHE HIS THR GLU ARG LYS THR GLU PRO ALA THR GLY
SEQRES 86 A 1158 PHE ILE ASP GLY ASP LEU ILE GLU SER PHE LEU ASP ILE
SEQRES 87 A 1158 SER ARG PRO LYS MET GLN GLU VAL VAL ALA ASN LEU GLN
SEQRES 88 A 1158 TYR ASP ASP GLY SER GLY MET LYS ARG GLU ALA THR ALA
SEQRES 89 A 1158 ASP ASP LEU ILE LYS VAL VAL GLU GLU LEU THR ARG ILE
SEQRES 90 A 1158 HIS
SEQRES 1 B 469 MET ASP TRP SER HIS PRO GLN PHE GLU LYS SER ALA VAL
SEQRES 2 B 469 ASP GLU ASN LEU TYR PHE GLN GLY GLY GLY ARG MET ALA
SEQRES 3 B 469 ALA GLU GLU GLY GLY ASP GLY ARG ARG ASN MET GLY ASN
SEQRES 4 B 469 PRO PRO PRO PRO ALA PRO ALA GLU SER GLU GLU GLU ASP
SEQRES 5 B 469 ASP ASN GLU MET GLU VAL GLU ASP GLN ASP GLY LYS GLU
SEQRES 6 B 469 ALA GLU LYS PRO ASN MET ILE ASN PHE ASP THR SER LEU
SEQRES 7 B 469 PRO THR SER HIS MET TYR LEU GLY SER ASP MET GLU GLU
SEQRES 8 B 469 PHE HIS GLY ARG THR LEU HIS ASP ASP ASP SER CYS GLN
SEQRES 9 B 469 VAL ILE PRO VAL LEU PRO HIS VAL MET VAL MET LEU ILE
SEQRES 10 B 469 PRO GLY GLN THR LEU PRO LEU GLN LEU PHE HIS PRO GLN
SEQRES 11 B 469 GLU VAL SER MET VAL ARG ASN LEU ILE GLN LYS ASP ARG
SEQRES 12 B 469 THR PHE ALA VAL LEU ALA TYR SER ASN VAL ARG GLU ARG
SEQRES 13 B 469 GLU ALA HIS PHE GLY THR THR ALA GLU ILE TYR ALA TYR
SEQRES 14 B 469 ARG GLU GLU GLN GLU TYR GLY ILE GLU THR VAL LYS VAL
SEQRES 15 B 469 LYS ALA ILE GLY ARG GLN ARG PHE LYS VAL LEU GLU ILE
SEQRES 16 B 469 ARG THR GLN SER ASP GLY ILE GLN GLN ALA LYS VAL GLN
SEQRES 17 B 469 ILE LEU PRO GLU ARG VAL LEU PRO SER THR MET SER ALA
SEQRES 18 B 469 VAL GLN LEU GLN SER LEU SER ARG ARG HIS ILE PHE PRO
SEQRES 19 B 469 SER SER LYS PRO LYS VAL TRP GLN ASP ARG ALA PHE ARG
SEQRES 20 B 469 GLN TRP TRP GLN LYS TYR GLN LYS ARG LYS PHE HIS CYS
SEQRES 21 B 469 ALA SER LEU THR SER TRP PRO PRO TRP LEU TYR SER LEU
SEQRES 22 B 469 TYR ASP ALA GLU THR LEU MET GLU ARG VAL LYS ARG GLN
SEQRES 23 B 469 LEU HIS GLU TRP ASP GLU ASN LEU LYS ASP GLU SER LEU
SEQRES 24 B 469 PRO THR ASN PRO ILE ASP PHE SER TYR ARG VAL ALA ALA
SEQRES 25 B 469 CYS LEU PRO ILE ASP ASP ALA LEU ARG ILE GLN LEU LEU
SEQRES 26 B 469 LYS ILE GLY SER ALA ILE GLN ARG LEU ARG CYS GLU LEU
SEQRES 27 B 469 ASP ILE MET ASN LYS CYS THR SER LEU CYS CYS LYS GLN
SEQRES 28 B 469 CYS GLN ASP THR GLU ILE THR THR LYS ASN GLU ILE PHE
SEQRES 29 B 469 SER LEU SER LEU CYS GLY PRO MET ALA ALA TYR VAL ASN
SEQRES 30 B 469 PRO HIS GLY TYR ILE HIS GLU THR LEU THR VAL TYR LYS
SEQRES 31 B 469 ALA CYS ASN LEU ASN LEU SER GLY ARG PRO SER THR GLU
SEQRES 32 B 469 HIS SER TRP PHE PRO GLY TYR ALA TRP THR ILE ALA GLN
SEQRES 33 B 469 CYS ARG ILE CYS GLY ASN HIS MET GLY TRP LYS PHE THR
SEQRES 34 B 469 ALA THR LYS LYS ASP MET SER PRO GLN LYS PHE TRP GLY
SEQRES 35 B 469 LEU THR ARG SER ALA LEU LEU PRO ARG ILE PRO GLU ALA
SEQRES 36 B 469 GLU ASP GLU LEU GLY HIS ASP ARG SER PRO LEU LEU CYS
SEQRES 37 B 469 LEU
HET ZN B1428 1
HET Y70 B1429 20
HETNAM ZN ZINC ION
HETNAM Y70 S-POMALIDOMIDE
FORMUL 3 ZN ZN 2+
FORMUL 4 Y70 C13 H11 N3 O4
HELIX 1 1 PRO A 250 LYS A 254 5 5
HELIX 2 2 ALA A 381 GLU A 384 5 4
HELIX 3 3 THR A 985 GLN A 990 1 6
HELIX 4 4 SER A 1044 ILE A 1062 1 19
HELIX 5 5 GLU A 1069 SER A 1075 1 7
HELIX 6 6 GLY A 1091 SER A 1096 1 6
HELIX 7 7 SER A 1101 ALA A 1110 1 10
HELIX 8 8 THR A 1125 ARG A 1138 1 14
HELIX 9 9 THR B 52 SER B 57 1 6
HELIX 10 10 HIS B 58 GLY B 62 5 5
HELIX 11 11 HIS B 104 GLN B 116 1 13
HELIX 12 12 GLN B 201 ARG B 205 5 5
HELIX 13 13 PHE B 222 PHE B 234 1 13
HELIX 14 14 HIS B 235 THR B 240 5 6
HELIX 15 15 PRO B 243 LEU B 249 1 7
HELIX 16 16 ASP B 251 ASP B 267 1 17
HELIX 17 17 LYS B 271 LEU B 275 5 5
HELIX 18 18 ASN B 278 ALA B 288 1 11
HELIX 19 19 ASP B 293 ILE B 303 1 11
HELIX 20 20 SER B 305 CYS B 320 1 16
SHEET 1 AA 5 VAL A1004 HIS A1009 0
SHEET 2 AA 5 GLN A1025 THR A1032 -1 O LEU A1029 N CYS A1008
SHEET 3 AA 5 ILE A1037 LEU A1043 -1 O GLY A1038 N PHE A1030
SHEET 4 AA 5 TYR A 3 GLN A 10 -1 O TYR A 3 N LEU A1043
SHEET 5 AA 5 PHE A1088 ASP A1090 1 O ILE A1089 N VAL A 6
SHEET 1 AB 4 GLY A 17 GLY A 21 0
SHEET 2 AB 4 ASN A 30 LYS A 35 -1 O ASN A 30 N GLY A 21
SHEET 3 AB 4 ARG A 38 VAL A 44 -1 O ARG A 38 N LYS A 35
SHEET 4 AB 4 LEU A 49 GLY A 56 -1 O ARG A 50 N VAL A 43
SHEET 1 AC 4 ILE A 61 PHE A 67 0
SHEET 2 AC 4 LEU A 76 THR A 81 -1 O LEU A 76 N PHE A 67
SHEET 3 AC 4 ASN A 85 SER A 94 -1 O ASN A 85 N THR A 81
SHEET 4 AC 4 SER A 97 ASN A 107 -1 O SER A 97 N SER A 94
SHEET 1 AD 3 ILE A 121 ILE A 124 0
SHEET 2 AD 3 ILE A 131 ARG A 134 -1 O GLY A 132 N ILE A 123
SHEET 3 AD 3 LYS A 141 ILE A 143 -1 O LYS A 141 N LEU A 133
SHEET 1 AE 4 HIS A 163 PHE A 169 0
SHEET 2 AE 4 THR A 177 GLN A 183 -1 O CYS A 179 N LYS A 168
SHEET 3 AE 4 ARG A 188 SER A 196 -1 O HIS A 189 N TYR A 182
SHEET 4 AE 4 GLU A 201 LYS A 204 -1 O GLU A 201 N SER A 196
SHEET 1 AF 4 MET A 218 ALA A 221 0
SHEET 2 AF 4 ALA A 229 ILE A 232 -1 O ILE A 230 N ILE A 220
SHEET 3 AF 4 ILE A 237 ASN A 241 -1 O THR A 238 N ILE A 231
SHEET 4 AF 4 LYS A 244 ILE A 248 -1 O LYS A 244 N ASN A 241
SHEET 1 AG 4 ILE A 258 ARG A 263 0
SHEET 2 AG 4 ARG A 270 ASP A 275 -1 O LEU A 272 N ASN A 262
SHEET 3 AG 4 ARG A 279 LEU A 284 -1 O ARG A 279 N ASP A 275
SHEET 4 AG 4 ARG A 301 GLU A 307 -1 O ARG A 301 N LEU A 284
SHEET 1 AH 4 ALA A 311 TYR A 316 0
SHEET 2 AH 4 VAL A 321 SER A 326 -1 O PHE A 323 N THR A 315
SHEET 3 AH 4 SER A 331 LEU A 336 -1 O GLN A 332 N VAL A 324
SHEET 4 AH 4 VAL A 347 PHE A 353 -1 O VAL A 348 N LYS A 335
SHEET 1 AI 4 ILE A 359 VAL A 365 0
SHEET 2 AI 4 GLN A 374 SER A 379 -1 O GLN A 374 N VAL A 365
SHEET 3 AI 4 SER A 386 ASN A 392 -1 O SER A 386 N SER A 379
SHEET 4 AI 4 LEU A 710 PRO A 716 -1 O HIS A 711 N ARG A 391
SHEET 1 AJ 4 ILE A 396 ASP A 403 0
SHEET 2 AJ 4 THR A 698 ILE A 704 -1 O LEU A 699 N ILE A 402
SHEET 3 AJ 4 SER A 690 ALA A 694 -1 O LEU A 691 N GLY A 702
SHEET 4 AJ 4 TYR A 678 LEU A 682 -1 O TYR A 678 N ALA A 694
SHEET 1 AK 4 GLY A 409 LEU A 413 0
SHEET 2 AK 4 THR A 424 PHE A 429 -1 O THR A 424 N LEU A 413
SHEET 3 AK 4 GLN A 432 ASN A 439 -1 O GLN A 432 N PHE A 429
SHEET 4 AK 4 GLU A 442 THR A 446 -1 O GLU A 442 N ASN A 439
SHEET 1 AL 4 THR A 457 VAL A 463 0
SHEET 2 AL 4 GLN A 467 THR A 472 -1 O GLN A 467 N VAL A 463
SHEET 3 AL 4 VAL A 476 SER A 480 -1 O ARG A 477 N GLN A 470
SHEET 4 AL 4 ALA A 485 TRP A 490 -1 O ALA A 485 N SER A 480
SHEET 1 AM 4 VAL A 500 CYS A 503 0
SHEET 2 AM 4 GLN A 507 VAL A 512 -1 O VAL A 509 N SER A 502
SHEET 3 AM 4 ALA A 515 HIS A 522 -1 O ALA A 515 N VAL A 512
SHEET 4 AM 4 GLU A 525 GLU A 533 -1 O GLU A 525 N HIS A 522
SHEET 1 AN 4 VAL A 538 ASP A 542 0
SHEET 2 AN 4 LEU A 555 LEU A 560 -1 O ALA A 557 N ASP A 542
SHEET 3 AN 4 SER A 565 LYS A 570 -1 O SER A 565 N LEU A 560
SHEET 4 AN 4 LEU A 576 MET A 581 -1 N LEU A 577 O ILE A 568
SHEET 1 AO 4 PRO A 588 PHE A 596 0
SHEET 2 AO 4 SER A 599 LEU A 606 -1 O SER A 599 N PHE A 596
SHEET 3 AO 4 ALA A 610 LEU A 616 -1 O ALA A 610 N LEU A 606
SHEET 4 AO 4 LEU A 623 THR A 630 -1 O SER A 624 N GLY A 615
SHEET 1 AP 4 VAL A 637 SER A 643 0
SHEET 2 AP 4 THR A 646 CYS A 652 -1 O THR A 646 N SER A 643
SHEET 3 AP 4 THR A 657 SER A 661 -1 O THR A 657 N ALA A 651
SHEET 4 AP 4 LEU A 666 ASN A 670 -1 O VAL A 667 N TYR A 660
SHEET 1 AQ 2 SER A 720 GLN A 727 0
SHEET 2 AQ 2 CYS A 732 GLN A 743 -1 O CYS A 732 N GLN A 727
SHEET 1 AR 2 THR A 749 ALA A 751 0
SHEET 2 AR 2 CYS A 732 GLN A 743 1 O VAL A 742 N THR A 750
SHEET 1 AS 5 SER A 762 VAL A 765 0
SHEET 2 AS 5 VAL A 801 GLN A 806 1 O LEU A 802 N SER A 762
SHEET 3 AS 5 GLU A 785 ASP A 795 -1 O LEU A 791 N HIS A 805
SHEET 4 AS 5 CYS A 732 GLN A 743 -1 O PHE A 733 N ILE A 794
SHEET 5 AS 5 THR A 749 ALA A 751 1 O THR A 750 N VAL A 742
SHEET 1 AT 5 SER A 762 VAL A 765 0
SHEET 2 AT 5 VAL A 801 GLN A 806 1 O LEU A 802 N SER A 762
SHEET 3 AT 5 GLU A 785 ASP A 795 -1 O LEU A 791 N HIS A 805
SHEET 4 AT 5 CYS A 732 GLN A 743 -1 O PHE A 733 N ILE A 794
SHEET 5 AT 5 SER A 720 GLN A 727 -1 O SER A 720 N SER A 738
SHEET 1 AU 4 GLU A 811 CYS A 819 0
SHEET 2 AU 4 TYR A 828 MET A 835 -1 O TYR A 828 N CYS A 819
SHEET 3 AU 4 GLY A 846 SER A 854 -1 O ARG A 847 N THR A 833
SHEET 4 AU 4 LYS A 857 VAL A 866 -1 O LYS A 857 N SER A 854
SHEET 1 AV 4 MET A 873 PHE A 876 0
SHEET 2 AV 4 LYS A 879 ILE A 884 -1 O LYS A 879 N PHE A 876
SHEET 3 AV 4 THR A 887 TRP A 893 -1 O THR A 887 N ILE A 884
SHEET 4 AV 4 LEU A 899 TYR A 906 -1 O ARG A 900 N GLU A 892
SHEET 1 AW 4 TYR A 913 LYS A 917 0
SHEET 2 AW 4 PHE A 920 GLY A 924 -1 O PHE A 920 N LYS A 917
SHEET 3 AW 4 VAL A 930 LYS A 936 -1 O LEU A 931 N VAL A 923
SHEET 4 AW 4 ASN A 941 ASP A 948 -1 O ASN A 941 N LYS A 936
SHEET 1 AX 4 MET A 954 ILE A 959 0
SHEET 2 AX 4 PHE A 965 GLU A 969 -1 O LEU A 966 N GLU A 958
SHEET 3 AX 4 ASN A 973 GLN A 978 -1 O ASN A 973 N GLU A 969
SHEET 4 AX 4 GLN A 993 HIS A 999 -1 O GLN A 993 N GLN A 978
SHEET 1 AY 2 PHE A1076 HIS A1077 0
SHEET 2 AY 2 THR A1082 GLU A1083 -1 O GLU A1083 N PHE A1076
SHEET 1 BA 2 GLU B 66 GLU B 67 0
SHEET 2 BA 2 GLU B 133 GLU B 150 -1 O TYR B 145 N GLU B 66
SHEET 1 BB 2 THR B 97 LEU B 102 0
SHEET 2 BB 2 ILE B 153 THR B 173 -1 O VAL B 156 N LEU B 102
SHEET 1 BC 3 GLU B 332 THR B 335 0
SHEET 2 BC 3 SER B 322 CYS B 325 -1 O LEU B 323 N ILE B 333
SHEET 3 BC 3 LEU B 424 LEU B 425 -1 O LEU B 425 N CYS B 324
SHEET 1 BD 6 MET B 348 VAL B 352 0
SHEET 2 BD 6 ILE B 358 VAL B 364 -1 O HIS B 359 N TYR B 351
SHEET 3 BD 6 LYS B 415 THR B 420 -1 O TRP B 417 N VAL B 364
SHEET 4 BD 6 HIS B 399 ALA B 406 -1 O MET B 400 N THR B 420
SHEET 5 BD 6 TYR B 386 CYS B 393 -1 O ALA B 387 N THR B 405
SHEET 6 BD 6 LEU B 370 SER B 377 -1 O ASN B 371 N GLN B 392
LINK SG CYS B 325 ZN ZN B1428 1555 1555 2.29
LINK SG CYS B 328 ZN ZN B1428 1555 1555 2.13
LINK SG CYS B 393 ZN ZN B1428 1555 1555 2.39
LINK SG CYS B 396 ZN ZN B1428 1555 1555 2.14
CISPEP 1 GLU A 224 PRO A 225 0 5.62
CISPEP 2 GLY A 357 PRO A 358 0 -2.03
CISPEP 3 GLU A 482 PRO A 483 0 -0.16
CISPEP 4 LEU A 571 PRO A 572 0 6.26
CISPEP 5 SER B 412 PRO B 413 0 1.41
SITE 1 AC1 4 CYS B 325 CYS B 328 CYS B 393 CYS B 396
SITE 1 AC2 12 GLN B 149 ASN B 353 PRO B 354 HIS B 355
SITE 2 AC2 12 GLU B 379 HIS B 380 SER B 381 TRP B 382
SITE 3 AC2 12 TRP B 388 ARG B 394 TRP B 402 PHE B 404
CRYST1 171.070 171.070 137.930 90.00 90.00 120.00 P 32 2 1 6
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 0.005846 0.003375 0.000000 0.00000
SCALE2 0.000000 0.006750 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007250 0.00000
(ATOM LINES ARE NOT SHOWN.)
END