HEADER LIGASE 21-NOV-17 6BOY
TITLE CRYSTAL STRUCTURE OF DDB1-CRBN-BRD4(BD1) COMPLEX BOUND TO DBET6
TITLE 2 PROTAC.
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,DAMAGE-
COMPND 5 SPECIFIC DNA-BINDING PROTEIN 1,HBV X-ASSOCIATED PROTEIN 1,XAP-1,UV-
COMPND 6 DAMAGED DNA-BINDING FACTOR,UV-DAMAGED DNA-BINDING PROTEIN 1,UV-DDB 1,
COMPND 7 XPE-BINDING FACTOR,XPE-BF,XERODERMA PIGMENTOSUM GROUP E-COMPLEMENTING
COMPND 8 PROTEIN,XPCE,DDB P127 SUBUNIT,DNA DAMAGE-BINDING PROTEIN A,DDBA,
COMPND 9 DAMAGE-SPECIFIC DNA-BINDING PROTEIN 1,HBV X-ASSOCIATED PROTEIN 1,XAP-
COMPND 10 1,UV-DAMAGED DNA-BINDING FACTOR,UV-DAMAGED DNA-BINDING PROTEIN 1,UV-
COMPND 11 DDB 1,XPE-BINDING FACTOR,XPE-BF,XERODERMA PIGMENTOSUM GROUP E-
COMPND 12 COMPLEMENTING PROTEIN,XPCE;
COMPND 13 ENGINEERED: YES;
COMPND 14 MOL_ID: 2;
COMPND 15 MOLECULE: PROTEIN CEREBLON;
COMPND 16 CHAIN: B;
COMPND 17 ENGINEERED: YES;
COMPND 18 MOL_ID: 3;
COMPND 19 MOLECULE: BROMODOMAIN-CONTAINING PROTEIN 4;
COMPND 20 CHAIN: C;
COMPND 21 FRAGMENT: RESIDUES 42-168;
COMPND 22 SYNONYM: PROTEIN HUNK1;
COMPND 23 ENGINEERED: YES;
COMPND 24 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: DDB1, XAP1;
SOURCE 6 EXPRESSION_SYSTEM: TRICHOPLUSIA NI;
SOURCE 7 EXPRESSION_SYSTEM_COMMON: CABBAGE LOOPER;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 7111;
SOURCE 9 MOL_ID: 2;
SOURCE 10 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 11 ORGANISM_COMMON: HUMAN;
SOURCE 12 ORGANISM_TAXID: 9606;
SOURCE 13 GENE: CRBN, AD-006;
SOURCE 14 EXPRESSION_SYSTEM: TRICHOPLUSIA NI;
SOURCE 15 EXPRESSION_SYSTEM_COMMON: CABBAGE LOOPER;
SOURCE 16 EXPRESSION_SYSTEM_TAXID: 7111;
SOURCE 17 MOL_ID: 3;
SOURCE 18 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 19 ORGANISM_COMMON: HUMAN;
SOURCE 20 ORGANISM_TAXID: 9606;
SOURCE 21 GENE: BRD4, HUNK1;
SOURCE 22 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 23 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS PROTAC, DEGRADER, E3 LIGASE, CRBN, LIGASE
EXPDTA X-RAY DIFFRACTION
AUTHOR R.P.NOWAK,S.L.DEANGELO,D.BUCKLEY,J.E.BRADNER,E.S.FISCHER
REVDAT 6 04-OCT-23 6BOY 1 REMARK
REVDAT 5 04-DEC-19 6BOY 1 REMARK
REVDAT 4 20-FEB-19 6BOY 1 REMARK
REVDAT 3 07-NOV-18 6BOY 1 JRNL
REVDAT 2 01-AUG-18 6BOY 1 JRNL
REVDAT 1 30-MAY-18 6BOY 0
JRNL AUTH R.P.NOWAK,S.L.DEANGELO,D.BUCKLEY,Z.HE,K.A.DONOVAN,J.AN,
JRNL AUTH 2 N.SAFAEE,M.P.JEDRYCHOWSKI,C.M.PONTHIER,M.ISHOEY,T.ZHANG,
JRNL AUTH 3 J.D.MANCIAS,N.S.GRAY,J.E.BRADNER,E.S.FISCHER
JRNL TITL PLASTICITY IN BINDING CONFERS SELECTIVITY IN LIGAND-INDUCED
JRNL TITL 2 PROTEIN DEGRADATION.
JRNL REF NAT. CHEM. BIOL. V. 14 706 2018
JRNL REFN ESSN 1552-4469
JRNL PMID 29892083
JRNL DOI 10.1038/S41589-018-0055-Y
REMARK 2
REMARK 2 RESOLUTION. 3.33 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (1.12_2829)
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,
REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,
REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,
REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON,
REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,
REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT
REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 3.33
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 49.79
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.5
REMARK 3 NUMBER OF REFLECTIONS : 35242
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.201
REMARK 3 R VALUE (WORKING SET) : 0.199
REMARK 3 FREE R VALUE : 0.234
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.220
REMARK 3 FREE R VALUE TEST SET COUNT : 1839
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS).
REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE
REMARK 3 1 49.7984 - 7.8207 1.00 2864 182 0.1916 0.2078
REMARK 3 2 7.8207 - 6.2113 1.00 2667 156 0.2162 0.2484
REMARK 3 3 6.2113 - 5.4272 1.00 2627 139 0.2072 0.2305
REMARK 3 4 5.4272 - 4.9315 1.00 2600 139 0.1729 0.2485
REMARK 3 5 4.9315 - 4.5783 1.00 2555 149 0.1548 0.2088
REMARK 3 6 4.5783 - 4.3085 1.00 2558 140 0.1588 0.1910
REMARK 3 7 4.3085 - 4.0928 1.00 2518 155 0.1811 0.2159
REMARK 3 8 4.0928 - 3.9148 1.00 2553 133 0.2175 0.2803
REMARK 3 9 3.9148 - 3.7641 1.00 2549 121 0.2332 0.2872
REMARK 3 10 3.7641 - 3.6343 1.00 2500 132 0.2471 0.2866
REMARK 3 11 3.6343 - 3.5207 1.00 2546 133 0.2691 0.3218
REMARK 3 12 3.5207 - 3.4200 1.00 2495 138 0.3068 0.4036
REMARK 3 13 3.4200 - 3.3300 0.94 2371 122 0.3859 0.4343
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : NULL
REMARK 3 SOLVENT RADIUS : 1.11
REMARK 3 SHRINKAGE RADIUS : 0.90
REMARK 3 K_SOL : NULL
REMARK 3 B_SOL : NULL
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.470
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 25.350
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
REMARK 3
REMARK 3 TWINNING INFORMATION.
REMARK 3 FRACTION: NULL
REMARK 3 OPERATOR: NULL
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : 0.002 10593
REMARK 3 ANGLE : 0.500 14379
REMARK 3 CHIRALITY : 0.043 1622
REMARK 3 PLANARITY : 0.004 1892
REMARK 3 DIHEDRAL : 3.267 6401
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 1
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: ALL
REMARK 3 ORIGIN FOR THE GROUP (A): 70.8418 53.7786 8.2940
REMARK 3 T TENSOR
REMARK 3 T11: 0.5978 T22: 1.5331
REMARK 3 T33: 1.3177 T12: 0.0451
REMARK 3 T13: -0.0224 T23: 0.3916
REMARK 3 L TENSOR
REMARK 3 L11: 1.3109 L22: 0.9934
REMARK 3 L33: 1.8784 L12: 0.5581
REMARK 3 L13: -0.4725 L23: -0.4121
REMARK 3 S TENSOR
REMARK 3 S11: -0.1250 S12: 0.4168 S13: 0.2096
REMARK 3 S21: 0.0411 S22: 0.0525 S23: 0.0312
REMARK 3 S31: -0.2016 S32: 0.2958 S33: 0.0706
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 6BOY COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 22-NOV-17.
REMARK 100 THE DEPOSITION ID IS D_1000231151.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 14-JUL-17
REMARK 200 TEMPERATURE (KELVIN) : 100.0
REMARK 200 PH : 8.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 24-ID-E
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 : SI(220)
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS EIGER X 16M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : AIMLESS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 35541
REMARK 200 RESOLUTION RANGE HIGH (A) : 3.330
REMARK 200 RESOLUTION RANGE LOW (A) : 49.793
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 32.20
REMARK 200 R MERGE (I) : 0.17900
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 16.4000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.33
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.49
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 33.20
REMARK 200 R MERGE FOR SHELL (I) : 5.47100
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 0.900
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: 6BN7
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 67.63
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.80
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 9% (W/V) PEG20K, 18% (V/V) PEG MME
REMARK 280 550, 0.09M BICINE PH8.5, 9% (V/V) SILVER BULLET D11 (0.25% W/V 2,
REMARK 280 6-NAPHTHALENEDISULFONIC ACID DISODIUM SALT, 0.25% W/V 4-
REMARK 280 AMINOBENZOIC ACID, 0.25% W/V 5-SULFOSALICYLIC ACID DIHYDRATE,
REMARK 280 0.25% W/V NAPHTHALENE-1,3,6-TRISULFONIC ACID TRISODIUM SALT
REMARK 280 HYDRATE, 0.02 M HEPES SODIUM PH 6.8), VAPOR DIFFUSION, SITTING
REMARK 280 DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 65 2 2
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 -X,-Y,Z+1/2
REMARK 290 5555 Y,-X+Y,Z+1/6
REMARK 290 6555 X-Y,X,Z+5/6
REMARK 290 7555 Y,X,-Z+2/3
REMARK 290 8555 X-Y,-Y,-Z
REMARK 290 9555 -X,-X+Y,-Z+1/3
REMARK 290 10555 -Y,-X,-Z+1/6
REMARK 290 11555 -X+Y,Y,-Z+1/2
REMARK 290 12555 X,X-Y,-Z+5/6
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 392.09533
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 196.04767
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 294.07150
REMARK 290 SMTRY1 5 0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 5 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 98.02383
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 490.11917
REMARK 290 SMTRY1 7 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 7 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 392.09533
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 9 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 9 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 9 0.000000 0.000000 -1.000000 196.04767
REMARK 290 SMTRY1 10 0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 10 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 10 0.000000 0.000000 -1.000000 98.02383
REMARK 290 SMTRY1 11 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 11 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 11 0.000000 0.000000 -1.000000 294.07150
REMARK 290 SMTRY1 12 0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 12 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 12 0.000000 0.000000 -1.000000 490.11917
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: TRIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 6380 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 55700 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -39.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, 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 -27
REMARK 465 GLY A -26
REMARK 465 SER A -25
REMARK 465 SER A -24
REMARK 465 HIS A -23
REMARK 465 HIS A -22
REMARK 465 HIS A -21
REMARK 465 HIS A -20
REMARK 465 HIS A -19
REMARK 465 HIS A -18
REMARK 465 SER A -17
REMARK 465 ALA A -16
REMARK 465 ALA A -15
REMARK 465 HIS A -14
REMARK 465 ILE A -13
REMARK 465 VAL A -12
REMARK 465 MET A -11
REMARK 465 VAL A -10
REMARK 465 ASP A -9
REMARK 465 ALA A -8
REMARK 465 TYR A -7
REMARK 465 LYS A -6
REMARK 465 PRO A -5
REMARK 465 THR A -4
REMARK 465 LYS A -3
REMARK 465 GLY A -2
REMARK 465 GLY A -1
REMARK 465 ARG A 0
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 ILE A 698
REMARK 465 GLY A 699
REMARK 465 GLY A 700
REMARK 465 ASN A 701
REMARK 465 GLY A 702
REMARK 465 ASN A 703
REMARK 465 SER A 704
REMARK 465 GLY A 705
REMARK 465 GLU A 706
REMARK 465 ILE A 707
REMARK 465 GLN A 708
REMARK 465 PHE A 771
REMARK 465 SER A 772
REMARK 465 SER A 773
REMARK 465 SER A 774
REMARK 465 THR A 775
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 MET B -20
REMARK 465 GLY B -19
REMARK 465 SER B -18
REMARK 465 SER B -17
REMARK 465 HIS B -16
REMARK 465 HIS B -15
REMARK 465 HIS B -14
REMARK 465 HIS B -13
REMARK 465 HIS B -12
REMARK 465 HIS B -11
REMARK 465 SER B -10
REMARK 465 ALA B -9
REMARK 465 VAL B -8
REMARK 465 ASP B -7
REMARK 465 GLU B -6
REMARK 465 ASN B -5
REMARK 465 LEU B -4
REMARK 465 TYR B -3
REMARK 465 PHE B -2
REMARK 465 GLN B -1
REMARK 465 GLY B 0
REMARK 465 GLY B 1
REMARK 465 MET B 2
REMARK 465 ALA B 3
REMARK 465 GLY B 4
REMARK 465 GLU B 5
REMARK 465 GLY B 6
REMARK 465 ASP B 7
REMARK 465 GLN B 8
REMARK 465 GLN B 9
REMARK 465 ASP B 10
REMARK 465 ALA B 11
REMARK 465 ALA B 12
REMARK 465 HIS B 13
REMARK 465 ASN B 14
REMARK 465 MET B 15
REMARK 465 GLY B 16
REMARK 465 ASN B 17
REMARK 465 HIS B 18
REMARK 465 LEU B 19
REMARK 465 PRO B 20
REMARK 465 LEU B 21
REMARK 465 LEU B 22
REMARK 465 PRO B 23
REMARK 465 GLU B 24
REMARK 465 SER B 25
REMARK 465 GLU B 26
REMARK 465 GLU B 27
REMARK 465 GLU B 28
REMARK 465 ASP B 29
REMARK 465 GLU B 30
REMARK 465 MET B 31
REMARK 465 GLU B 32
REMARK 465 VAL B 33
REMARK 465 GLU B 34
REMARK 465 ASP B 35
REMARK 465 GLN B 36
REMARK 465 ASP B 37
REMARK 465 SER B 38
REMARK 465 LYS B 39
REMARK 465 GLU B 40
REMARK 465 ALA B 41
REMARK 465 LYS B 42
REMARK 465 LYS B 43
REMARK 465 SER B 210
REMARK 465 LYS B 211
REMARK 465 PRO B 212
REMARK 465 VAL B 213
REMARK 465 SER B 214
REMARK 465 ARG B 215
REMARK 465 GLU B 216
REMARK 465 ASP B 217
REMARK 465 GLN B 218
REMARK 465 ASP B 428
REMARK 465 THR B 429
REMARK 465 GLU B 430
REMARK 465 ASP B 431
REMARK 465 GLU B 432
REMARK 465 ILE B 433
REMARK 465 SER B 434
REMARK 465 PRO B 435
REMARK 465 ASP B 436
REMARK 465 LYS B 437
REMARK 465 VAL B 438
REMARK 465 ILE B 439
REMARK 465 LEU B 440
REMARK 465 CYS B 441
REMARK 465 LEU B 442
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 ASP A 99 CG OD1 OD2
REMARK 470 ARG A 111 CG CD NE CZ NH1 NH2
REMARK 470 ARG A 114 CG CD NE CZ NH1 NH2
REMARK 470 ARG A 129 CG CD NE CZ NH1 NH2
REMARK 470 ARG A 147 CG CD NE CZ NH1 NH2
REMARK 470 LYS A 153 CG CD CE NZ
REMARK 470 GLN A 186 CG CD OE1 NE2
REMARK 470 LYS A 204 CG CD CE NZ
REMARK 470 LYS A 208 CG CD CE NZ
REMARK 470 GLN A 209 CG CD OE1 NE2
REMARK 470 ILE A 237 CG1 CG2 CD1
REMARK 470 LYS A 287 CG CD CE NZ
REMARK 470 LYS A 298 CG CD CE NZ
REMARK 470 VAL A 338 CG1 CG2
REMARK 470 ARG A 369 CG CD NE CZ NH1 NH2
REMARK 470 LYS A 709 CG CD CE NZ
REMARK 470 LYS A 769 CG CD CE NZ
REMARK 470 LYS A 823 CG CD CE NZ
REMARK 470 LYS A 867 CG CD CE NZ
REMARK 470 SER A 981 OG
REMARK 470 GLN A1113 CG CD OE1 NE2
REMARK 470 LYS A1121 CG CD CE NZ
REMARK 470 LYS A1131 CG CD CE NZ
REMARK 470 ASN B 45 CG OD1 ND2
REMARK 470 ARG B 70 CG CD NE CZ NH1 NH2
REMARK 470 LYS B 269 CG CD CE NZ
REMARK 470 TYR B 363 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 LYS C 141 CD CE NZ
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 TYR A 3 71.45 58.06
REMARK 500 ASN A 36 -89.16 55.08
REMARK 500 LEU A 145 52.70 -90.48
REMARK 500 VAL A 212 -169.29 -112.91
REMARK 500 ASN A 241 85.89 -165.70
REMARK 500 VAL A 264 -70.58 -92.32
REMARK 500 ILE A 310 97.63 -57.19
REMARK 500 LEU A 317 -89.19 -89.18
REMARK 500 ASN A 341 -156.89 -78.75
REMARK 500 LEU A 367 -76.54 -66.27
REMARK 500 GLU A 368 -97.18 -71.25
REMARK 500 PHE A 382 -137.85 61.84
REMARK 500 SER A 746 -99.28 -78.00
REMARK 500 SER A 755 -168.53 -116.09
REMARK 500 THR A 780 -174.59 57.53
REMARK 500 ASN A 885 -117.54 52.27
REMARK 500 LYS A 917 111.98 -161.85
REMARK 500 MET A 927 42.24 -101.56
REMARK 500 ASN A 952 145.68 -170.45
REMARK 500 SER A 955 -31.71 -153.35
REMARK 500 GLU A 969 -156.24 -138.92
REMARK 500 ALA A 983 -154.89 56.21
REMARK 500 THR A 984 -31.05 -137.11
REMARK 500 SER A1027 114.22 -164.16
REMARK 500 PHE A1076 103.54 -56.27
REMARK 500 GLU A1079 0.32 -69.15
REMARK 500 LEU A1112 -103.88 -74.51
REMARK 500 ASP A1116 59.17 -119.43
REMARK 500 MET A1120 -129.54 -108.45
REMARK 500 ARG A1138 11.74 -68.88
REMARK 500 ASN B 45 -167.78 59.13
REMARK 500 ASP B 50 96.11 66.25
REMARK 500 ASP B 76 -4.28 64.65
REMARK 500 LYS B 116 -130.07 -115.74
REMARK 500 ARG B 145 113.31 -160.14
REMARK 500 GLN B 148 -155.28 -87.78
REMARK 500 ASP B 149 38.49 28.30
REMARK 500 ARG B 162 -71.08 -118.49
REMARK 500 CYS B 234 -3.86 -59.53
REMARK 500 ASP B 271 -40.36 -138.75
REMARK 500 GLN B 327 -9.82 66.29
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 B 501 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS B 323 SG
REMARK 620 2 CYS B 326 SG 116.1
REMARK 620 3 CYS B 391 SG 136.8 95.4
REMARK 620 4 CYS B 394 SG 101.5 94.7 104.8
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 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue RN6 B 502
DBREF 6BOY A 1 699 UNP Q16531 DDB1_HUMAN 1 395
DBREF 6BOY A 706 1140 UNP Q16531 DDB1_HUMAN 706 1140
DBREF 6BOY B 2 442 UNP Q96SW2 CRBN_HUMAN 1 441
DBREF 6BOY C 42 168 UNP O60885 BRD4_HUMAN 42 168
SEQADV 6BOY MET A -27 UNP Q16531 INITIATING METHIONINE
SEQADV 6BOY GLY A -26 UNP Q16531 EXPRESSION TAG
SEQADV 6BOY SER A -25 UNP Q16531 EXPRESSION TAG
SEQADV 6BOY SER A -24 UNP Q16531 EXPRESSION TAG
SEQADV 6BOY HIS A -23 UNP Q16531 EXPRESSION TAG
SEQADV 6BOY HIS A -22 UNP Q16531 EXPRESSION TAG
SEQADV 6BOY HIS A -21 UNP Q16531 EXPRESSION TAG
SEQADV 6BOY HIS A -20 UNP Q16531 EXPRESSION TAG
SEQADV 6BOY HIS A -19 UNP Q16531 EXPRESSION TAG
SEQADV 6BOY HIS A -18 UNP Q16531 EXPRESSION TAG
SEQADV 6BOY SER A -17 UNP Q16531 EXPRESSION TAG
SEQADV 6BOY ALA A -16 UNP Q16531 EXPRESSION TAG
SEQADV 6BOY ALA A -15 UNP Q16531 EXPRESSION TAG
SEQADV 6BOY HIS A -14 UNP Q16531 EXPRESSION TAG
SEQADV 6BOY ILE A -13 UNP Q16531 EXPRESSION TAG
SEQADV 6BOY VAL A -12 UNP Q16531 EXPRESSION TAG
SEQADV 6BOY MET A -11 UNP Q16531 EXPRESSION TAG
SEQADV 6BOY VAL A -10 UNP Q16531 EXPRESSION TAG
SEQADV 6BOY ASP A -9 UNP Q16531 EXPRESSION TAG
SEQADV 6BOY ALA A -8 UNP Q16531 EXPRESSION TAG
SEQADV 6BOY TYR A -7 UNP Q16531 EXPRESSION TAG
SEQADV 6BOY LYS A -6 UNP Q16531 EXPRESSION TAG
SEQADV 6BOY PRO A -5 UNP Q16531 EXPRESSION TAG
SEQADV 6BOY THR A -4 UNP Q16531 EXPRESSION TAG
SEQADV 6BOY LYS A -3 UNP Q16531 EXPRESSION TAG
SEQADV 6BOY GLY A -2 UNP Q16531 EXPRESSION TAG
SEQADV 6BOY GLY A -1 UNP Q16531 EXPRESSION TAG
SEQADV 6BOY ARG A 0 UNP Q16531 EXPRESSION TAG
SEQADV 6BOY GLY A 700 UNP Q16531 LINKER
SEQADV 6BOY ASN A 701 UNP Q16531 LINKER
SEQADV 6BOY GLY A 702 UNP Q16531 LINKER
SEQADV 6BOY ASN A 703 UNP Q16531 LINKER
SEQADV 6BOY SER A 704 UNP Q16531 LINKER
SEQADV 6BOY GLY A 705 UNP Q16531 LINKER
SEQADV 6BOY MET B -20 UNP Q96SW2 INITIATING METHIONINE
SEQADV 6BOY GLY B -19 UNP Q96SW2 EXPRESSION TAG
SEQADV 6BOY SER B -18 UNP Q96SW2 EXPRESSION TAG
SEQADV 6BOY SER B -17 UNP Q96SW2 EXPRESSION TAG
SEQADV 6BOY HIS B -16 UNP Q96SW2 EXPRESSION TAG
SEQADV 6BOY HIS B -15 UNP Q96SW2 EXPRESSION TAG
SEQADV 6BOY HIS B -14 UNP Q96SW2 EXPRESSION TAG
SEQADV 6BOY HIS B -13 UNP Q96SW2 EXPRESSION TAG
SEQADV 6BOY HIS B -12 UNP Q96SW2 EXPRESSION TAG
SEQADV 6BOY HIS B -11 UNP Q96SW2 EXPRESSION TAG
SEQADV 6BOY SER B -10 UNP Q96SW2 EXPRESSION TAG
SEQADV 6BOY ALA B -9 UNP Q96SW2 EXPRESSION TAG
SEQADV 6BOY VAL B -8 UNP Q96SW2 EXPRESSION TAG
SEQADV 6BOY ASP B -7 UNP Q96SW2 EXPRESSION TAG
SEQADV 6BOY GLU B -6 UNP Q96SW2 EXPRESSION TAG
SEQADV 6BOY ASN B -5 UNP Q96SW2 EXPRESSION TAG
SEQADV 6BOY LEU B -4 UNP Q96SW2 EXPRESSION TAG
SEQADV 6BOY TYR B -3 UNP Q96SW2 EXPRESSION TAG
SEQADV 6BOY PHE B -2 UNP Q96SW2 EXPRESSION TAG
SEQADV 6BOY GLN B -1 UNP Q96SW2 EXPRESSION TAG
SEQADV 6BOY GLY B 0 UNP Q96SW2 EXPRESSION TAG
SEQADV 6BOY GLY B 1 UNP Q96SW2 EXPRESSION TAG
SEQADV 6BOY MET C 43 UNP O60885 THR 43 ENGINEERED MUTATION
SEQRES 1 A 864 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER ALA ALA
SEQRES 2 A 864 HIS ILE VAL MET VAL ASP ALA TYR LYS PRO THR LYS GLY
SEQRES 3 A 864 GLY ARG MET SER TYR ASN TYR VAL VAL THR ALA GLN LYS
SEQRES 4 A 864 PRO THR ALA VAL ASN GLY CYS VAL THR GLY HIS PHE THR
SEQRES 5 A 864 SER ALA GLU ASP LEU ASN LEU LEU ILE ALA LYS ASN THR
SEQRES 6 A 864 ARG LEU GLU ILE TYR VAL VAL THR ALA GLU GLY LEU ARG
SEQRES 7 A 864 PRO VAL LYS GLU VAL GLY MET TYR GLY LYS ILE ALA VAL
SEQRES 8 A 864 MET GLU LEU PHE ARG PRO LYS GLY GLU SER LYS ASP LEU
SEQRES 9 A 864 LEU PHE ILE LEU THR ALA LYS TYR ASN ALA CYS ILE LEU
SEQRES 10 A 864 GLU TYR LYS GLN SER GLY GLU SER ILE ASP ILE ILE THR
SEQRES 11 A 864 ARG ALA HIS GLY ASN VAL GLN ASP ARG ILE GLY ARG PRO
SEQRES 12 A 864 SER GLU THR GLY ILE ILE GLY ILE ILE ASP PRO GLU CYS
SEQRES 13 A 864 ARG MET ILE GLY LEU ARG LEU TYR ASP GLY LEU PHE LYS
SEQRES 14 A 864 VAL ILE PRO LEU ASP ARG ASP ASN LYS GLU LEU LYS ALA
SEQRES 15 A 864 PHE ASN ILE ARG LEU GLU GLU LEU HIS VAL ILE ASP VAL
SEQRES 16 A 864 LYS PHE LEU TYR GLY CYS GLN ALA PRO THR ILE CYS PHE
SEQRES 17 A 864 VAL TYR GLN ASP PRO GLN GLY ARG HIS VAL LYS THR TYR
SEQRES 18 A 864 GLU VAL SER LEU ARG GLU LYS GLU PHE ASN LYS GLY PRO
SEQRES 19 A 864 TRP LYS GLN GLU ASN VAL GLU ALA GLU ALA SER MET VAL
SEQRES 20 A 864 ILE ALA VAL PRO GLU PRO PHE GLY GLY ALA ILE ILE ILE
SEQRES 21 A 864 GLY GLN GLU SER ILE THR TYR HIS ASN GLY ASP LYS TYR
SEQRES 22 A 864 LEU ALA ILE ALA PRO PRO ILE ILE LYS GLN SER THR ILE
SEQRES 23 A 864 VAL CYS HIS ASN ARG VAL ASP PRO ASN GLY SER ARG TYR
SEQRES 24 A 864 LEU LEU GLY ASP MET GLU GLY ARG LEU PHE MET LEU LEU
SEQRES 25 A 864 LEU GLU LYS GLU GLU GLN MET ASP GLY THR VAL THR LEU
SEQRES 26 A 864 LYS ASP LEU ARG VAL GLU LEU LEU GLY GLU THR SER ILE
SEQRES 27 A 864 ALA GLU CYS LEU THR TYR LEU ASP ASN GLY VAL VAL PHE
SEQRES 28 A 864 VAL GLY SER ARG LEU GLY ASP SER GLN LEU VAL LYS LEU
SEQRES 29 A 864 ASN VAL ASP SER ASN GLU GLN GLY SER TYR VAL VAL ALA
SEQRES 30 A 864 MET GLU THR PHE THR ASN LEU GLY PRO ILE VAL ASP MET
SEQRES 31 A 864 CYS VAL VAL ASP LEU GLU ARG GLN GLY GLN GLY GLN LEU
SEQRES 32 A 864 VAL THR CYS SER GLY ALA PHE LYS GLU GLY SER LEU ARG
SEQRES 33 A 864 ILE ILE ARG ASN GLY ILE GLY GLY ASN GLY ASN SER GLY
SEQRES 34 A 864 GLU ILE GLN LYS LEU HIS ILE ARG THR VAL PRO LEU TYR
SEQRES 35 A 864 GLU SER PRO ARG LYS ILE CYS TYR GLN GLU VAL SER GLN
SEQRES 36 A 864 CYS PHE GLY VAL LEU SER SER ARG ILE GLU VAL GLN ASP
SEQRES 37 A 864 THR SER GLY GLY THR THR ALA LEU ARG PRO SER ALA SER
SEQRES 38 A 864 THR GLN ALA LEU SER SER SER VAL SER SER SER LYS LEU
SEQRES 39 A 864 PHE SER SER SER THR ALA PRO HIS GLU THR SER PHE GLY
SEQRES 40 A 864 GLU GLU VAL GLU VAL HIS ASN LEU LEU ILE ILE ASP GLN
SEQRES 41 A 864 HIS THR PHE GLU VAL LEU HIS ALA HIS GLN PHE LEU GLN
SEQRES 42 A 864 ASN GLU TYR ALA LEU SER LEU VAL SER CYS LYS LEU GLY
SEQRES 43 A 864 LYS ASP PRO ASN THR TYR PHE ILE VAL GLY THR ALA MET
SEQRES 44 A 864 VAL TYR PRO GLU GLU ALA GLU PRO LYS GLN GLY ARG ILE
SEQRES 45 A 864 VAL VAL PHE GLN TYR SER ASP GLY LYS LEU GLN THR VAL
SEQRES 46 A 864 ALA GLU LYS GLU VAL LYS GLY ALA VAL TYR SER MET VAL
SEQRES 47 A 864 GLU PHE ASN GLY LYS LEU LEU ALA SER ILE ASN SER THR
SEQRES 48 A 864 VAL ARG LEU TYR GLU TRP THR THR GLU LYS GLU LEU ARG
SEQRES 49 A 864 THR GLU CYS ASN HIS TYR ASN ASN ILE MET ALA LEU TYR
SEQRES 50 A 864 LEU LYS THR LYS GLY ASP PHE ILE LEU VAL GLY ASP LEU
SEQRES 51 A 864 MET ARG SER VAL LEU LEU LEU ALA TYR LYS PRO MET GLU
SEQRES 52 A 864 GLY ASN PHE GLU GLU ILE ALA ARG ASP PHE ASN PRO ASN
SEQRES 53 A 864 TRP MET SER ALA VAL GLU ILE LEU ASP ASP ASP ASN PHE
SEQRES 54 A 864 LEU GLY ALA GLU ASN ALA PHE ASN LEU PHE VAL CYS GLN
SEQRES 55 A 864 LYS ASP SER ALA ALA THR THR ASP GLU GLU ARG GLN HIS
SEQRES 56 A 864 LEU GLN GLU VAL GLY LEU PHE HIS LEU GLY GLU PHE VAL
SEQRES 57 A 864 ASN VAL PHE CYS HIS GLY SER LEU VAL MET GLN ASN LEU
SEQRES 58 A 864 GLY GLU THR SER THR PRO THR GLN GLY SER VAL LEU PHE
SEQRES 59 A 864 GLY THR VAL ASN GLY MET ILE GLY LEU VAL THR SER LEU
SEQRES 60 A 864 SER GLU SER TRP TYR ASN LEU LEU LEU ASP MET GLN ASN
SEQRES 61 A 864 ARG LEU ASN LYS VAL ILE LYS SER VAL GLY LYS ILE GLU
SEQRES 62 A 864 HIS SER PHE TRP ARG SER PHE HIS THR GLU ARG LYS THR
SEQRES 63 A 864 GLU PRO ALA THR GLY PHE ILE ASP GLY ASP LEU ILE GLU
SEQRES 64 A 864 SER PHE LEU ASP ILE SER ARG PRO LYS MET GLN GLU VAL
SEQRES 65 A 864 VAL ALA ASN LEU GLN TYR ASP ASP GLY SER GLY MET LYS
SEQRES 66 A 864 ARG GLU ALA THR ALA ASP ASP LEU ILE LYS VAL VAL GLU
SEQRES 67 A 864 GLU LEU THR ARG ILE HIS
SEQRES 1 B 463 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER ALA VAL
SEQRES 2 B 463 ASP GLU ASN LEU TYR PHE GLN GLY GLY MET ALA GLY GLU
SEQRES 3 B 463 GLY ASP GLN GLN ASP ALA ALA HIS ASN MET GLY ASN HIS
SEQRES 4 B 463 LEU PRO LEU LEU PRO GLU SER GLU GLU GLU ASP GLU MET
SEQRES 5 B 463 GLU VAL GLU ASP GLN ASP SER LYS GLU ALA LYS LYS PRO
SEQRES 6 B 463 ASN ILE ILE ASN PHE ASP THR SER LEU PRO THR SER HIS
SEQRES 7 B 463 THR TYR LEU GLY ALA ASP MET GLU GLU PHE HIS GLY ARG
SEQRES 8 B 463 THR LEU HIS ASP ASP ASP SER CYS GLN VAL ILE PRO VAL
SEQRES 9 B 463 LEU PRO GLN VAL MET MET ILE LEU ILE PRO GLY GLN THR
SEQRES 10 B 463 LEU PRO LEU GLN LEU PHE HIS PRO GLN GLU VAL SER MET
SEQRES 11 B 463 VAL ARG ASN LEU ILE GLN LYS ASP ARG THR PHE ALA VAL
SEQRES 12 B 463 LEU ALA TYR SER ASN VAL GLN GLU ARG GLU ALA GLN PHE
SEQRES 13 B 463 GLY THR THR ALA GLU ILE TYR ALA TYR ARG GLU GLU GLN
SEQRES 14 B 463 ASP PHE GLY ILE GLU ILE VAL LYS VAL LYS ALA ILE GLY
SEQRES 15 B 463 ARG GLN ARG PHE LYS VAL LEU GLU LEU ARG THR GLN SER
SEQRES 16 B 463 ASP GLY ILE GLN GLN ALA LYS VAL GLN ILE LEU PRO GLU
SEQRES 17 B 463 CYS VAL LEU PRO SER THR MET SER ALA VAL GLN LEU GLU
SEQRES 18 B 463 SER LEU ASN LYS CYS GLN ILE PHE PRO SER LYS PRO VAL
SEQRES 19 B 463 SER ARG GLU ASP GLN CYS SER TYR LYS TRP TRP GLN LYS
SEQRES 20 B 463 TYR GLN LYS ARG LYS PHE HIS CYS ALA ASN LEU THR SER
SEQRES 21 B 463 TRP PRO ARG TRP LEU TYR SER LEU TYR ASP ALA GLU THR
SEQRES 22 B 463 LEU MET ASP ARG ILE LYS LYS GLN LEU ARG GLU TRP ASP
SEQRES 23 B 463 GLU ASN LEU LYS ASP ASP SER LEU PRO SER ASN PRO ILE
SEQRES 24 B 463 ASP PHE SER TYR ARG VAL ALA ALA CYS LEU PRO ILE ASP
SEQRES 25 B 463 ASP VAL LEU ARG ILE GLN LEU LEU LYS ILE GLY SER ALA
SEQRES 26 B 463 ILE GLN ARG LEU ARG CYS GLU LEU ASP ILE MET ASN LYS
SEQRES 27 B 463 CYS THR SER LEU CYS CYS LYS GLN CYS GLN GLU THR GLU
SEQRES 28 B 463 ILE THR THR LYS ASN GLU ILE PHE SER LEU SER LEU CYS
SEQRES 29 B 463 GLY PRO MET ALA ALA TYR VAL ASN PRO HIS GLY TYR VAL
SEQRES 30 B 463 HIS GLU THR LEU THR VAL TYR LYS ALA CYS ASN LEU ASN
SEQRES 31 B 463 LEU ILE GLY ARG PRO SER THR GLU HIS SER TRP PHE PRO
SEQRES 32 B 463 GLY TYR ALA TRP THR VAL ALA GLN CYS LYS ILE CYS ALA
SEQRES 33 B 463 SER HIS ILE GLY TRP LYS PHE THR ALA THR LYS LYS ASP
SEQRES 34 B 463 MET SER PRO GLN LYS PHE TRP GLY LEU THR ARG SER ALA
SEQRES 35 B 463 LEU LEU PRO THR ILE PRO ASP THR GLU ASP GLU ILE SER
SEQRES 36 B 463 PRO ASP LYS VAL ILE LEU CYS LEU
SEQRES 1 C 127 SER MET ASN PRO PRO PRO PRO GLU THR SER ASN PRO ASN
SEQRES 2 C 127 LYS PRO LYS ARG GLN THR ASN GLN LEU GLN TYR LEU LEU
SEQRES 3 C 127 ARG VAL VAL LEU LYS THR LEU TRP LYS HIS GLN PHE ALA
SEQRES 4 C 127 TRP PRO PHE GLN GLN PRO VAL ASP ALA VAL LYS LEU ASN
SEQRES 5 C 127 LEU PRO ASP TYR TYR LYS ILE ILE LYS THR PRO MET ASP
SEQRES 6 C 127 MET GLY THR ILE LYS LYS ARG LEU GLU ASN ASN TYR TYR
SEQRES 7 C 127 TRP ASN ALA GLN GLU CYS ILE GLN ASP PHE ASN THR MET
SEQRES 8 C 127 PHE THR ASN CYS TYR ILE TYR ASN LYS PRO GLY ASP ASP
SEQRES 9 C 127 ILE VAL LEU MET ALA GLU ALA LEU GLU LYS LEU PHE LEU
SEQRES 10 C 127 GLN LYS ILE ASN GLU LEU PRO THR GLU GLU
HET ZN B 501 1
HET RN6 B 502 59
HETNAM ZN ZINC ION
HETNAM RN6 2-[(6S)-4-(4-CHLOROPHENYL)-2,3,9-TRIMETHYL-6H-THIENO[3,
HETNAM 2 RN6 2-F][1,2,4]TRIAZOLO[4,3-A][1,4]DIAZEPIN-6-YL]-N-(8-
HETNAM 3 RN6 {[({2-[(3S)-2,6-DIOXOPIPERIDIN-3-YL]-1,3-DIOXO-2,3-
HETNAM 4 RN6 DIHYDRO-1H-ISOINDOL-4-YL}OXY)ACETYL]AMINO}OCTYL)
HETNAM 5 RN6 ACETAMIDE
FORMUL 4 ZN ZN 2+
FORMUL 5 RN6 C42 H45 CL N8 O7 S
HELIX 1 AA1 PRO A 250 GLN A 255 5 6
HELIX 2 AA2 ALA A 381 GLU A 384 5 4
HELIX 3 AA3 GLU A 728 SER A 730 5 3
HELIX 4 AA4 SER A 755 GLN A 759 5 5
HELIX 5 AA5 THR A 985 GLN A 990 1 6
HELIX 6 AA6 SER A 1044 LYS A 1060 1 17
HELIX 7 AA7 GLU A 1069 SER A 1075 1 7
HELIX 8 AA8 GLY A 1091 SER A 1096 1 6
HELIX 9 AA9 PHE A 1097 ILE A 1100 5 4
HELIX 10 AB1 SER A 1101 ALA A 1110 1 10
HELIX 11 AB2 THR A 1125 ARG A 1138 1 14
HELIX 12 AB3 THR B 51 HIS B 57 1 7
HELIX 13 AB4 THR B 58 GLY B 61 5 4
HELIX 14 AB5 HIS B 103 LYS B 116 1 14
HELIX 15 AB6 LEU B 202 GLN B 206 5 5
HELIX 16 AB7 SER B 220 PHE B 232 1 13
HELIX 17 AB8 HIS B 233 THR B 238 5 6
HELIX 18 AB9 PRO B 241 LEU B 247 1 7
HELIX 19 AC1 ASP B 249 GLU B 263 1 15
HELIX 20 AC2 ASN B 276 CYS B 287 1 12
HELIX 21 AC3 ASP B 291 ILE B 301 1 11
HELIX 22 AC4 SER B 303 CYS B 318 1 16
HELIX 23 AC5 ASN B 335 ILE B 337 5 3
HELIX 24 AC6 THR C 60 VAL C 69 1 10
HELIX 25 AC7 VAL C 69 LYS C 76 1 8
HELIX 26 AC8 ALA C 80 GLN C 84 5 5
HELIX 27 AC9 ASP C 96 ILE C 101 1 6
HELIX 28 AD1 ASP C 106 ASN C 116 1 11
HELIX 29 AD2 ASN C 121 ASN C 140 1 20
HELIX 30 AD3 ASP C 144 ASN C 162 1 19
SHEET 1 AA1 5 VAL A1004 HIS A1009 0
SHEET 2 AA1 5 GLN A1025 THR A1032 -1 O GLY A1031 N ASN A1005
SHEET 3 AA1 5 ILE A1037 SER A1042 -1 O GLY A1038 N PHE A1030
SHEET 4 AA1 5 ASN A 4 GLN A 10 -1 N VAL A 7 O LEU A1039
SHEET 5 AA1 5 PHE A1088 ASP A1090 1 O ILE A1089 N VAL A 6
SHEET 1 AA2 4 GLY A 17 GLY A 21 0
SHEET 2 AA2 4 ASN A 30 ALA A 34 -1 O LEU A 32 N VAL A 19
SHEET 3 AA2 4 ARG A 38 VAL A 44 -1 O GLU A 40 N ILE A 33
SHEET 4 AA2 4 LEU A 49 GLY A 56 -1 O VAL A 52 N ILE A 41
SHEET 1 AA3 4 ILE A 61 PHE A 67 0
SHEET 2 AA3 4 LEU A 76 THR A 81 -1 O LEU A 76 N PHE A 67
SHEET 3 AA3 4 ASN A 85 SER A 94 -1 O LEU A 89 N LEU A 77
SHEET 4 AA3 4 SER A 97 ASN A 107 -1 O GLY A 106 N ALA A 86
SHEET 1 AA4 4 ILE A 121 ILE A 124 0
SHEET 2 AA4 4 MET A 130 TYR A 136 -1 O GLY A 132 N ILE A 123
SHEET 3 AA4 4 LEU A 139 PRO A 144 -1 O LYS A 141 N LEU A 133
SHEET 4 AA4 4 PHE A 155 ARG A 158 -1 O ILE A 157 N PHE A 140
SHEET 1 AA5 4 VAL A 164 PHE A 169 0
SHEET 2 AA5 4 THR A 177 ASP A 184 -1 O VAL A 181 N ILE A 165
SHEET 3 AA5 4 GLY A 187 SER A 196 -1 O LYS A 191 N PHE A 180
SHEET 4 AA5 4 GLU A 201 LYS A 204 -1 O GLU A 201 N SER A 196
SHEET 1 AA6 4 VAL A 164 PHE A 169 0
SHEET 2 AA6 4 THR A 177 ASP A 184 -1 O VAL A 181 N ILE A 165
SHEET 3 AA6 4 GLY A 187 SER A 196 -1 O LYS A 191 N PHE A 180
SHEET 4 AA6 4 GLU A 210 ASN A 211 -1 O GLU A 210 N VAL A 190
SHEET 1 AA7 4 MET A 218 ALA A 221 0
SHEET 2 AA7 4 ALA A 229 ILE A 232 -1 O ILE A 232 N MET A 218
SHEET 3 AA7 4 ILE A 237 ASN A 241 -1 O THR A 238 N ILE A 231
SHEET 4 AA7 4 LYS A 244 ILE A 248 -1 O LEU A 246 N TYR A 239
SHEET 1 AA8 4 ILE A 258 ARG A 263 0
SHEET 2 AA8 4 ARG A 270 ASP A 275 -1 O GLY A 274 N VAL A 259
SHEET 3 AA8 4 ARG A 279 GLU A 286 -1 O PHE A 281 N LEU A 273
SHEET 4 AA8 4 ASP A 299 GLU A 307 -1 O GLU A 303 N MET A 282
SHEET 1 AA9 4 CYS A 313 TYR A 316 0
SHEET 2 AA9 4 VAL A 321 GLY A 325 -1 O PHE A 323 N THR A 315
SHEET 3 AA9 4 SER A 331 LEU A 336 -1 O VAL A 334 N VAL A 322
SHEET 4 AA9 4 VAL A 347 PHE A 353 -1 O VAL A 348 N LYS A 335
SHEET 1 AB1 4 ASP A 361 VAL A 365 0
SHEET 2 AB1 4 GLN A 374 SER A 379 -1 O CYS A 378 N ASP A 361
SHEET 3 AB1 4 SER A 386 ARG A 391 -1 O SER A 386 N SER A 379
SHEET 4 AB1 4 HIS A 711 PRO A 716 -1 O VAL A 715 N LEU A 387
SHEET 1 AB2 3 SER A 720 GLN A 727 0
SHEET 2 AB2 3 CYS A 732 GLN A 743 -1 O LEU A 736 N ARG A 722
SHEET 3 AB2 3 THR A 749 ALA A 751 -1 O THR A 750 N VAL A 742
SHEET 1 AB3 5 SER A 720 GLN A 727 0
SHEET 2 AB3 5 CYS A 732 GLN A 743 -1 O LEU A 736 N ARG A 722
SHEET 3 AB3 5 GLU A 785 ASP A 795 -1 O LEU A 792 N VAL A 735
SHEET 4 AB3 5 VAL A 801 GLN A 806 -1 O HIS A 805 N LEU A 791
SHEET 5 AB3 5 SER A 762 VAL A 765 1 N SER A 764 O GLN A 806
SHEET 1 AB4 4 GLU A 811 CYS A 819 0
SHEET 2 AB4 4 TYR A 828 MET A 835 -1 O ILE A 830 N VAL A 817
SHEET 3 AB4 4 GLY A 846 SER A 854 -1 O PHE A 851 N PHE A 829
SHEET 4 AB4 4 LYS A 857 VAL A 866 -1 O ALA A 862 N VAL A 850
SHEET 1 AB5 4 VAL A 870 PHE A 876 0
SHEET 2 AB5 4 LYS A 879 ILE A 884 -1 O LEU A 881 N VAL A 874
SHEET 3 AB5 4 THR A 887 TRP A 893 -1 O ARG A 889 N ALA A 882
SHEET 4 AB5 4 LEU A 899 TYR A 906 -1 O GLU A 902 N LEU A 890
SHEET 1 AB6 4 TYR A 913 LYS A 917 0
SHEET 2 AB6 4 PHE A 920 GLY A 924 -1 O LEU A 922 N LYS A 915
SHEET 3 AB6 4 SER A 929 LYS A 936 -1 O LEU A 931 N VAL A 923
SHEET 4 AB6 4 ASN A 941 PHE A 949 -1 O ALA A 946 N LEU A 932
SHEET 1 AB7 4 ALA A 956 ILE A 959 0
SHEET 2 AB7 4 ASN A 964 GLU A 969 -1 O ALA A 968 N ALA A 956
SHEET 3 AB7 4 ASN A 973 GLN A 978 -1 O PHE A 975 N GLY A 967
SHEET 4 AB7 4 GLN A 993 HIS A 999 -1 O PHE A 998 N LEU A 974
SHEET 1 AB8 2 PHE A1076 THR A1078 0
SHEET 2 AB8 2 LYS A1081 GLU A1083 -1 O LYS A1081 N THR A1078
SHEET 1 AB9 7 GLU B 65 GLU B 66 0
SHEET 2 AB9 7 GLU B 132 GLU B 147 -1 O TYR B 144 N GLU B 65
SHEET 3 AB9 7 THR B 119 ASN B 127 -1 N ALA B 124 O PHE B 135
SHEET 4 AB9 7 CYS B 78 VAL B 83 1 N PRO B 82 O ALA B 121
SHEET 5 AB9 7 GLN B 178 ILE B 184 -1 O ALA B 180 N ILE B 81
SHEET 6 AB9 7 ILE B 154 THR B 172 -1 N ARG B 171 O GLN B 179
SHEET 7 AB9 7 THR B 96 LEU B 101 -1 N LEU B 101 O VAL B 155
SHEET 1 AC1 4 GLU B 65 GLU B 66 0
SHEET 2 AC1 4 GLU B 132 GLU B 147 -1 O TYR B 144 N GLU B 65
SHEET 3 AC1 4 ILE B 154 THR B 172 -1 O ARG B 162 N THR B 138
SHEET 4 AC1 4 THR B 96 LEU B 101 -1 N LEU B 101 O VAL B 155
SHEET 1 AC2 3 GLU B 330 THR B 333 0
SHEET 2 AC2 3 SER B 320 CYS B 323 -1 N LEU B 321 O THR B 332
SHEET 3 AC2 3 LEU B 422 THR B 425 -1 O LEU B 423 N CYS B 322
SHEET 1 AC3 6 MET B 346 VAL B 350 0
SHEET 2 AC3 6 VAL B 356 VAL B 362 -1 O HIS B 357 N TYR B 349
SHEET 3 AC3 6 LYS B 413 THR B 418 -1 O TRP B 415 N VAL B 362
SHEET 4 AC3 6 HIS B 397 ALA B 404 -1 N TRP B 400 O GLY B 416
SHEET 5 AC3 6 TYR B 384 CYS B 391 -1 N ALA B 385 O THR B 403
SHEET 6 AC3 6 LEU B 368 SER B 375 -1 N ILE B 371 O VAL B 388
LINK SG CYS B 323 ZN ZN B 501 1555 1555 2.31
LINK SG CYS B 326 ZN ZN B 501 1555 1555 2.35
LINK SG CYS B 391 ZN ZN B 501 1555 1555 2.40
LINK SG CYS B 394 ZN ZN B 501 1555 1555 2.27
CISPEP 1 GLU A 224 PRO A 225 0 3.71
CISPEP 2 GLY A 357 PRO A 358 0 -4.49
CISPEP 3 SER B 410 PRO B 411 0 0.96
SITE 1 AC1 4 CYS B 323 CYS B 326 CYS B 391 CYS B 394
SITE 1 AC2 16 ASN B 351 PRO B 352 HIS B 353 TYR B 355
SITE 2 AC2 16 HIS B 378 SER B 379 TRP B 380 TRP B 386
SITE 3 AC2 16 TRP B 400 PHE B 402 TRP C 81 PRO C 82
SITE 4 AC2 16 PHE C 83 LEU C 94 ASN C 140 ILE C 146
CRYST1 115.406 115.406 588.143 90.00 90.00 120.00 P 65 2 2 12
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 0.008665 0.005003 0.000000 0.00000
SCALE2 0.000000 0.010006 0.000000 0.00000
SCALE3 0.000000 0.000000 0.001700 0.00000
(ATOM LINES ARE NOT SHOWN.)
END