HEADER TRANSFERASE 17-SEP-15 5DSY
TITLE CRYSTAL STRUCTURE OF CONSTITUTIVELY ACTIVE PARP-2
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: POLY [ADP-RIBOSE] POLYMERASE 2;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 FRAGMENT: UNP RESIDUES 348-583;
COMPND 5 SYNONYM: HPARP-2,ADP-RIBOSYLTRANSFERASE DIPHTHERIA TOXIN-LIKE 2,
COMPND 6 ARTD2,NAD(+) ADP-RIBOSYLTRANSFERASE 2,ADPRT-2,POLY[ADP-RIBOSE]
COMPND 7 SYNTHASE 2,PADPRT-2;
COMPND 8 EC: 2.4.2.30;
COMPND 9 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: PARP2, ADPRT2, ADPRTL2;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS ADP-RIBOSYL TRANSFERASE, PARP, PARP-2, TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR A.A.RICCIO,J.M.PASCAL
REVDAT 2 20-SEP-17 5DSY 1 JRNL REMARK
REVDAT 1 27-JUL-16 5DSY 0
JRNL AUTH J.M.DAWICKI-MCKENNA,M.F.LANGELIER,J.E.DENIZIO,A.A.RICCIO,
JRNL AUTH 2 C.D.CAO,K.R.KARCH,M.MCCAULEY,J.D.STEFFEN,B.E.BLACK,
JRNL AUTH 3 J.M.PASCAL
JRNL TITL PARP-1 ACTIVATION REQUIRES LOCAL UNFOLDING OF AN
JRNL TITL 2 AUTOINHIBITORY DOMAIN.
JRNL REF MOL.CELL V. 60 755 2015
JRNL REFN ISSN 1097-2765
JRNL PMID 26626480
JRNL DOI 10.1016/J.MOLCEL.2015.10.013
REMARK 2
REMARK 2 RESOLUTION. 2.70 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.8.2_1309
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 : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.70
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 46.54
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.320
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.1
REMARK 3 NUMBER OF REFLECTIONS : 70646
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.195
REMARK 3 R VALUE (WORKING SET) : 0.193
REMARK 3 FREE R VALUE : 0.248
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.990
REMARK 3 FREE R VALUE TEST SET COUNT : 3524
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 46.5473 - 7.8701 1.00 2713 139 0.1642 0.1979
REMARK 3 2 7.8701 - 6.2515 1.00 2685 164 0.1840 0.2279
REMARK 3 3 6.2515 - 5.4627 1.00 2712 136 0.1766 0.2427
REMARK 3 4 5.4627 - 4.9638 1.00 2709 152 0.1512 0.2231
REMARK 3 5 4.9638 - 4.6084 1.00 2713 121 0.1313 0.1747
REMARK 3 6 4.6084 - 4.3369 1.00 2705 169 0.1482 0.2293
REMARK 3 7 4.3369 - 4.1198 1.00 2706 142 0.1488 0.1705
REMARK 3 8 4.1198 - 3.9406 1.00 2733 142 0.1686 0.2079
REMARK 3 9 3.9406 - 3.7890 1.00 2656 146 0.1756 0.2550
REMARK 3 10 3.7890 - 3.6583 1.00 2744 137 0.1737 0.2002
REMARK 3 11 3.6583 - 3.5439 1.00 2686 139 0.1864 0.2469
REMARK 3 12 3.5439 - 3.4427 1.00 2730 127 0.1932 0.3279
REMARK 3 13 3.4427 - 3.3521 1.00 2723 147 0.2187 0.3045
REMARK 3 14 3.3521 - 3.2703 1.00 2739 114 0.2219 0.2871
REMARK 3 15 3.2703 - 3.1960 1.00 2720 148 0.2348 0.3114
REMARK 3 16 3.1960 - 3.1280 1.00 2718 134 0.2334 0.2719
REMARK 3 17 3.1280 - 3.0654 1.00 2682 139 0.2313 0.2906
REMARK 3 18 3.0654 - 3.0076 1.00 2759 152 0.2458 0.2784
REMARK 3 19 3.0076 - 2.9539 1.00 2706 121 0.2751 0.3149
REMARK 3 20 2.9539 - 2.9038 1.00 2706 131 0.2842 0.3489
REMARK 3 21 2.9038 - 2.8570 1.00 2646 189 0.3019 0.3152
REMARK 3 22 2.8570 - 2.8130 1.00 2704 143 0.3045 0.3975
REMARK 3 23 2.8130 - 2.7717 1.00 2749 140 0.3046 0.3190
REMARK 3 24 2.7717 - 2.7326 1.00 2681 154 0.3132 0.3379
REMARK 3 25 2.7326 - 2.6957 0.77 2097 98 0.3345 0.3733
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
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) : 0.380
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 26.130
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 : 0.010 8248
REMARK 3 ANGLE : 1.349 11193
REMARK 3 CHIRALITY : 0.055 1204
REMARK 3 PLANARITY : 0.007 1541
REMARK 3 DIHEDRAL : 13.668 3147
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
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 5DSY COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 17-SEP-15.
REMARK 100 THE DEPOSITION ID IS D_1000213726.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 29-AUG-14
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.5-8.5
REMARK 200 NUMBER OF CRYSTALS USED : NULL
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ALS
REMARK 200 BEAMLINE : 12.3.1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.12
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315R
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XDS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 70646
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.700
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.4
REMARK 200 DATA REDUNDANCY : 12.00
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 11.0000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.68
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.80
REMARK 200 COMPLETENESS FOR SHELL (%) : 87.2
REMARK 200 DATA REDUNDANCY IN SHELL : 11.50
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.300
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: 3KJD
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 53.28
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.63
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 2.55-2.65 M NACL AND 0.1 M TRIS, PH
REMARK 280 8.0, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 298K
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 46.08150
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 60.36950
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 59.95000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 60.36950
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 46.08150
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 59.95000
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, 3, 4
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: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 3
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 4
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: D
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 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 197
REMARK 465 GLY A 198
REMARK 465 SER A 199
REMARK 465 SER A 200
REMARK 465 HIS A 201
REMARK 465 HIS A 202
REMARK 465 HIS A 203
REMARK 465 HIS A 204
REMARK 465 HIS A 205
REMARK 465 HIS A 206
REMARK 465 SER A 207
REMARK 465 SER A 208
REMARK 465 GLY A 209
REMARK 465 LEU A 210
REMARK 465 VAL A 211
REMARK 465 PRO A 212
REMARK 465 ARG A 213
REMARK 465 GLY A 214
REMARK 465 SER A 215
REMARK 465 HIS A 216
REMARK 465 VAL A 329
REMARK 465 GLN A 330
REMARK 465 ALA A 331
REMARK 465 MET A 332
REMARK 465 GLU A 333
REMARK 465 GLU A 334
REMARK 465 LYS A 335
REMARK 465 THR A 336
REMARK 465 GLU A 337
REMARK 465 LEU A 338
REMARK 465 LEU A 569
REMARK 465 TRP A 570
REMARK 465 MET B 197
REMARK 465 GLY B 198
REMARK 465 SER B 199
REMARK 465 SER B 200
REMARK 465 HIS B 201
REMARK 465 HIS B 202
REMARK 465 HIS B 203
REMARK 465 HIS B 204
REMARK 465 HIS B 205
REMARK 465 HIS B 206
REMARK 465 SER B 207
REMARK 465 SER B 208
REMARK 465 GLY B 209
REMARK 465 LEU B 210
REMARK 465 VAL B 211
REMARK 465 PRO B 212
REMARK 465 ARG B 213
REMARK 465 GLY B 214
REMARK 465 SER B 215
REMARK 465 HIS B 216
REMARK 465 VAL B 329
REMARK 465 GLN B 330
REMARK 465 ALA B 331
REMARK 465 MET B 332
REMARK 465 GLU B 333
REMARK 465 GLU B 334
REMARK 465 LYS B 335
REMARK 465 THR B 336
REMARK 465 GLU B 337
REMARK 465 MET C 197
REMARK 465 GLY C 198
REMARK 465 SER C 199
REMARK 465 SER C 200
REMARK 465 HIS C 201
REMARK 465 HIS C 202
REMARK 465 HIS C 203
REMARK 465 HIS C 204
REMARK 465 HIS C 205
REMARK 465 HIS C 206
REMARK 465 SER C 207
REMARK 465 SER C 208
REMARK 465 GLY C 209
REMARK 465 LEU C 210
REMARK 465 VAL C 211
REMARK 465 PRO C 212
REMARK 465 ARG C 213
REMARK 465 GLY C 214
REMARK 465 SER C 215
REMARK 465 HIS C 216
REMARK 465 VAL C 329
REMARK 465 GLN C 330
REMARK 465 ALA C 331
REMARK 465 MET C 332
REMARK 465 GLU C 333
REMARK 465 GLU C 334
REMARK 465 LYS C 335
REMARK 465 THR C 336
REMARK 465 GLU C 337
REMARK 465 LEU C 338
REMARK 465 LEU C 569
REMARK 465 TRP C 570
REMARK 465 MET D 197
REMARK 465 GLY D 198
REMARK 465 SER D 199
REMARK 465 SER D 200
REMARK 465 HIS D 201
REMARK 465 HIS D 202
REMARK 465 HIS D 203
REMARK 465 HIS D 204
REMARK 465 HIS D 205
REMARK 465 HIS D 206
REMARK 465 SER D 207
REMARK 465 SER D 208
REMARK 465 GLY D 209
REMARK 465 LEU D 210
REMARK 465 VAL D 211
REMARK 465 PRO D 212
REMARK 465 ARG D 213
REMARK 465 GLY D 214
REMARK 465 SER D 215
REMARK 465 HIS D 216
REMARK 465 VAL D 329
REMARK 465 GLN D 330
REMARK 465 ALA D 331
REMARK 465 MET D 332
REMARK 465 GLU D 333
REMARK 465 GLU D 334
REMARK 465 LYS D 335
REMARK 465 THR D 336
REMARK 465 GLU D 337
REMARK 465 LEU D 338
REMARK 465 GLN D 339
REMARK 465 LEU D 569
REMARK 465 TRP D 570
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 GLN A 568 CG CD OE1 NE2
REMARK 470 GLN B 568 CG CD OE1 NE2
REMARK 470 TRP B 570 CG CD1 CD2 NE1 CE2 CE3 CZ2
REMARK 470 TRP B 570 CZ3 CH2
REMARK 470 GLU C 218 CG CD OE1 OE2
REMARK 470 GLN D 568 CG CD OE1 NE2
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 PRO C 434 C - N - CA ANGL. DEV. = 10.8 DEGREES
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 HIS A 381 52.36 -106.30
REMARK 500 ASN A 489 105.99 -160.70
REMARK 500 ASP A 537 -67.35 -106.36
REMARK 500 ARG A 557 -42.65 -134.15
REMARK 500 HIS B 361 -4.72 -58.66
REMARK 500 HIS B 381 55.44 -106.95
REMARK 500 ASN B 489 102.32 -161.53
REMARK 500 ASP B 537 -67.59 -109.01
REMARK 500 ARG B 557 -43.03 -132.00
REMARK 500 CYS C 233 -53.55 -121.83
REMARK 500 HIS C 361 -6.16 -58.59
REMARK 500 HIS C 381 53.65 -107.82
REMARK 500 PHE C 444 38.21 -140.33
REMARK 500 ASN C 489 106.59 -165.28
REMARK 500 ARG C 557 -44.14 -133.41
REMARK 500 CYS D 233 -94.03 -117.05
REMARK 500 HIS D 361 -4.79 -57.23
REMARK 500 HIS D 381 57.90 -104.83
REMARK 500 ASP D 537 -60.39 -106.51
REMARK 500 ARG D 557 -43.83 -130.40
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue UHB A 1001
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue UHB B 1001
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue UHB C 1001
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue UHB D 1001
DBREF 5DSY A 335 570 UNP Q9UGN5 PARP2_HUMAN 348 583
DBREF 5DSY B 335 570 UNP Q9UGN5 PARP2_HUMAN 348 583
DBREF 5DSY C 335 570 UNP Q9UGN5 PARP2_HUMAN 348 583
DBREF 5DSY D 335 570 UNP Q9UGN5 PARP2_HUMAN 348 583
SEQADV 5DSY MET A 197 UNP Q9UGN5 INITIATING METHIONINE
SEQADV 5DSY GLY A 198 UNP Q9UGN5 EXPRESSION TAG
SEQADV 5DSY SER A 199 UNP Q9UGN5 EXPRESSION TAG
SEQADV 5DSY SER A 200 UNP Q9UGN5 EXPRESSION TAG
SEQADV 5DSY HIS A 201 UNP Q9UGN5 EXPRESSION TAG
SEQADV 5DSY HIS A 202 UNP Q9UGN5 EXPRESSION TAG
SEQADV 5DSY HIS A 203 UNP Q9UGN5 EXPRESSION TAG
SEQADV 5DSY HIS A 204 UNP Q9UGN5 EXPRESSION TAG
SEQADV 5DSY HIS A 205 UNP Q9UGN5 EXPRESSION TAG
SEQADV 5DSY HIS A 206 UNP Q9UGN5 EXPRESSION TAG
SEQADV 5DSY SER A 207 UNP Q9UGN5 EXPRESSION TAG
SEQADV 5DSY SER A 208 UNP Q9UGN5 EXPRESSION TAG
SEQADV 5DSY GLY A 209 UNP Q9UGN5 EXPRESSION TAG
SEQADV 5DSY LEU A 210 UNP Q9UGN5 EXPRESSION TAG
SEQADV 5DSY VAL A 211 UNP Q9UGN5 EXPRESSION TAG
SEQADV 5DSY PRO A 212 UNP Q9UGN5 EXPRESSION TAG
SEQADV 5DSY ARG A 213 UNP Q9UGN5 EXPRESSION TAG
SEQADV 5DSY GLY A 214 UNP Q9UGN5 EXPRESSION TAG
SEQADV 5DSY SER A 215 UNP Q9UGN5 EXPRESSION TAG
SEQADV 5DSY HIS A 216 UNP Q9UGN5 EXPRESSION TAG
SEQADV 5DSY PRO A 217 UNP Q9UGN5 EXPRESSION TAG
SEQADV 5DSY GLU A 218 UNP Q9UGN5 EXPRESSION TAG
SEQADV 5DSY SER A 219 UNP Q9UGN5 EXPRESSION TAG
SEQADV 5DSY GLN A 220 UNP Q9UGN5 EXPRESSION TAG
SEQADV 5DSY LEU A 221 UNP Q9UGN5 EXPRESSION TAG
SEQADV 5DSY ASP A 222 UNP Q9UGN5 EXPRESSION TAG
SEQADV 5DSY LEU A 223 UNP Q9UGN5 EXPRESSION TAG
SEQADV 5DSY ARG A 224 UNP Q9UGN5 EXPRESSION TAG
SEQADV 5DSY VAL A 225 UNP Q9UGN5 EXPRESSION TAG
SEQADV 5DSY GLN A 226 UNP Q9UGN5 EXPRESSION TAG
SEQADV 5DSY GLU A 227 UNP Q9UGN5 EXPRESSION TAG
SEQADV 5DSY LEU A 228 UNP Q9UGN5 EXPRESSION TAG
SEQADV 5DSY ILE A 229 UNP Q9UGN5 EXPRESSION TAG
SEQADV 5DSY LYS A 230 UNP Q9UGN5 EXPRESSION TAG
SEQADV 5DSY LEU A 231 UNP Q9UGN5 EXPRESSION TAG
SEQADV 5DSY ILE A 232 UNP Q9UGN5 EXPRESSION TAG
SEQADV 5DSY CYS A 233 UNP Q9UGN5 EXPRESSION TAG
SEQADV 5DSY ASN A 234 UNP Q9UGN5 EXPRESSION TAG
SEQADV 5DSY VAL A 329 UNP Q9UGN5 EXPRESSION TAG
SEQADV 5DSY GLN A 330 UNP Q9UGN5 EXPRESSION TAG
SEQADV 5DSY ALA A 331 UNP Q9UGN5 EXPRESSION TAG
SEQADV 5DSY MET A 332 UNP Q9UGN5 EXPRESSION TAG
SEQADV 5DSY GLU A 333 UNP Q9UGN5 EXPRESSION TAG
SEQADV 5DSY GLU A 334 UNP Q9UGN5 EXPRESSION TAG
SEQADV 5DSY MET B 197 UNP Q9UGN5 INITIATING METHIONINE
SEQADV 5DSY GLY B 198 UNP Q9UGN5 EXPRESSION TAG
SEQADV 5DSY SER B 199 UNP Q9UGN5 EXPRESSION TAG
SEQADV 5DSY SER B 200 UNP Q9UGN5 EXPRESSION TAG
SEQADV 5DSY HIS B 201 UNP Q9UGN5 EXPRESSION TAG
SEQADV 5DSY HIS B 202 UNP Q9UGN5 EXPRESSION TAG
SEQADV 5DSY HIS B 203 UNP Q9UGN5 EXPRESSION TAG
SEQADV 5DSY HIS B 204 UNP Q9UGN5 EXPRESSION TAG
SEQADV 5DSY HIS B 205 UNP Q9UGN5 EXPRESSION TAG
SEQADV 5DSY HIS B 206 UNP Q9UGN5 EXPRESSION TAG
SEQADV 5DSY SER B 207 UNP Q9UGN5 EXPRESSION TAG
SEQADV 5DSY SER B 208 UNP Q9UGN5 EXPRESSION TAG
SEQADV 5DSY GLY B 209 UNP Q9UGN5 EXPRESSION TAG
SEQADV 5DSY LEU B 210 UNP Q9UGN5 EXPRESSION TAG
SEQADV 5DSY VAL B 211 UNP Q9UGN5 EXPRESSION TAG
SEQADV 5DSY PRO B 212 UNP Q9UGN5 EXPRESSION TAG
SEQADV 5DSY ARG B 213 UNP Q9UGN5 EXPRESSION TAG
SEQADV 5DSY GLY B 214 UNP Q9UGN5 EXPRESSION TAG
SEQADV 5DSY SER B 215 UNP Q9UGN5 EXPRESSION TAG
SEQADV 5DSY HIS B 216 UNP Q9UGN5 EXPRESSION TAG
SEQADV 5DSY PRO B 217 UNP Q9UGN5 EXPRESSION TAG
SEQADV 5DSY GLU B 218 UNP Q9UGN5 EXPRESSION TAG
SEQADV 5DSY SER B 219 UNP Q9UGN5 EXPRESSION TAG
SEQADV 5DSY GLN B 220 UNP Q9UGN5 EXPRESSION TAG
SEQADV 5DSY LEU B 221 UNP Q9UGN5 EXPRESSION TAG
SEQADV 5DSY ASP B 222 UNP Q9UGN5 EXPRESSION TAG
SEQADV 5DSY LEU B 223 UNP Q9UGN5 EXPRESSION TAG
SEQADV 5DSY ARG B 224 UNP Q9UGN5 EXPRESSION TAG
SEQADV 5DSY VAL B 225 UNP Q9UGN5 EXPRESSION TAG
SEQADV 5DSY GLN B 226 UNP Q9UGN5 EXPRESSION TAG
SEQADV 5DSY GLU B 227 UNP Q9UGN5 EXPRESSION TAG
SEQADV 5DSY LEU B 228 UNP Q9UGN5 EXPRESSION TAG
SEQADV 5DSY ILE B 229 UNP Q9UGN5 EXPRESSION TAG
SEQADV 5DSY LYS B 230 UNP Q9UGN5 EXPRESSION TAG
SEQADV 5DSY LEU B 231 UNP Q9UGN5 EXPRESSION TAG
SEQADV 5DSY ILE B 232 UNP Q9UGN5 EXPRESSION TAG
SEQADV 5DSY CYS B 233 UNP Q9UGN5 EXPRESSION TAG
SEQADV 5DSY ASN B 234 UNP Q9UGN5 EXPRESSION TAG
SEQADV 5DSY VAL B 329 UNP Q9UGN5 EXPRESSION TAG
SEQADV 5DSY GLN B 330 UNP Q9UGN5 EXPRESSION TAG
SEQADV 5DSY ALA B 331 UNP Q9UGN5 EXPRESSION TAG
SEQADV 5DSY MET B 332 UNP Q9UGN5 EXPRESSION TAG
SEQADV 5DSY GLU B 333 UNP Q9UGN5 EXPRESSION TAG
SEQADV 5DSY GLU B 334 UNP Q9UGN5 EXPRESSION TAG
SEQADV 5DSY MET C 197 UNP Q9UGN5 INITIATING METHIONINE
SEQADV 5DSY GLY C 198 UNP Q9UGN5 EXPRESSION TAG
SEQADV 5DSY SER C 199 UNP Q9UGN5 EXPRESSION TAG
SEQADV 5DSY SER C 200 UNP Q9UGN5 EXPRESSION TAG
SEQADV 5DSY HIS C 201 UNP Q9UGN5 EXPRESSION TAG
SEQADV 5DSY HIS C 202 UNP Q9UGN5 EXPRESSION TAG
SEQADV 5DSY HIS C 203 UNP Q9UGN5 EXPRESSION TAG
SEQADV 5DSY HIS C 204 UNP Q9UGN5 EXPRESSION TAG
SEQADV 5DSY HIS C 205 UNP Q9UGN5 EXPRESSION TAG
SEQADV 5DSY HIS C 206 UNP Q9UGN5 EXPRESSION TAG
SEQADV 5DSY SER C 207 UNP Q9UGN5 EXPRESSION TAG
SEQADV 5DSY SER C 208 UNP Q9UGN5 EXPRESSION TAG
SEQADV 5DSY GLY C 209 UNP Q9UGN5 EXPRESSION TAG
SEQADV 5DSY LEU C 210 UNP Q9UGN5 EXPRESSION TAG
SEQADV 5DSY VAL C 211 UNP Q9UGN5 EXPRESSION TAG
SEQADV 5DSY PRO C 212 UNP Q9UGN5 EXPRESSION TAG
SEQADV 5DSY ARG C 213 UNP Q9UGN5 EXPRESSION TAG
SEQADV 5DSY GLY C 214 UNP Q9UGN5 EXPRESSION TAG
SEQADV 5DSY SER C 215 UNP Q9UGN5 EXPRESSION TAG
SEQADV 5DSY HIS C 216 UNP Q9UGN5 EXPRESSION TAG
SEQADV 5DSY PRO C 217 UNP Q9UGN5 EXPRESSION TAG
SEQADV 5DSY GLU C 218 UNP Q9UGN5 EXPRESSION TAG
SEQADV 5DSY SER C 219 UNP Q9UGN5 EXPRESSION TAG
SEQADV 5DSY GLN C 220 UNP Q9UGN5 EXPRESSION TAG
SEQADV 5DSY LEU C 221 UNP Q9UGN5 EXPRESSION TAG
SEQADV 5DSY ASP C 222 UNP Q9UGN5 EXPRESSION TAG
SEQADV 5DSY LEU C 223 UNP Q9UGN5 EXPRESSION TAG
SEQADV 5DSY ARG C 224 UNP Q9UGN5 EXPRESSION TAG
SEQADV 5DSY VAL C 225 UNP Q9UGN5 EXPRESSION TAG
SEQADV 5DSY GLN C 226 UNP Q9UGN5 EXPRESSION TAG
SEQADV 5DSY GLU C 227 UNP Q9UGN5 EXPRESSION TAG
SEQADV 5DSY LEU C 228 UNP Q9UGN5 EXPRESSION TAG
SEQADV 5DSY ILE C 229 UNP Q9UGN5 EXPRESSION TAG
SEQADV 5DSY LYS C 230 UNP Q9UGN5 EXPRESSION TAG
SEQADV 5DSY LEU C 231 UNP Q9UGN5 EXPRESSION TAG
SEQADV 5DSY ILE C 232 UNP Q9UGN5 EXPRESSION TAG
SEQADV 5DSY CYS C 233 UNP Q9UGN5 EXPRESSION TAG
SEQADV 5DSY ASN C 234 UNP Q9UGN5 EXPRESSION TAG
SEQADV 5DSY VAL C 329 UNP Q9UGN5 EXPRESSION TAG
SEQADV 5DSY GLN C 330 UNP Q9UGN5 EXPRESSION TAG
SEQADV 5DSY ALA C 331 UNP Q9UGN5 EXPRESSION TAG
SEQADV 5DSY MET C 332 UNP Q9UGN5 EXPRESSION TAG
SEQADV 5DSY GLU C 333 UNP Q9UGN5 EXPRESSION TAG
SEQADV 5DSY GLU C 334 UNP Q9UGN5 EXPRESSION TAG
SEQADV 5DSY MET D 197 UNP Q9UGN5 INITIATING METHIONINE
SEQADV 5DSY GLY D 198 UNP Q9UGN5 EXPRESSION TAG
SEQADV 5DSY SER D 199 UNP Q9UGN5 EXPRESSION TAG
SEQADV 5DSY SER D 200 UNP Q9UGN5 EXPRESSION TAG
SEQADV 5DSY HIS D 201 UNP Q9UGN5 EXPRESSION TAG
SEQADV 5DSY HIS D 202 UNP Q9UGN5 EXPRESSION TAG
SEQADV 5DSY HIS D 203 UNP Q9UGN5 EXPRESSION TAG
SEQADV 5DSY HIS D 204 UNP Q9UGN5 EXPRESSION TAG
SEQADV 5DSY HIS D 205 UNP Q9UGN5 EXPRESSION TAG
SEQADV 5DSY HIS D 206 UNP Q9UGN5 EXPRESSION TAG
SEQADV 5DSY SER D 207 UNP Q9UGN5 EXPRESSION TAG
SEQADV 5DSY SER D 208 UNP Q9UGN5 EXPRESSION TAG
SEQADV 5DSY GLY D 209 UNP Q9UGN5 EXPRESSION TAG
SEQADV 5DSY LEU D 210 UNP Q9UGN5 EXPRESSION TAG
SEQADV 5DSY VAL D 211 UNP Q9UGN5 EXPRESSION TAG
SEQADV 5DSY PRO D 212 UNP Q9UGN5 EXPRESSION TAG
SEQADV 5DSY ARG D 213 UNP Q9UGN5 EXPRESSION TAG
SEQADV 5DSY GLY D 214 UNP Q9UGN5 EXPRESSION TAG
SEQADV 5DSY SER D 215 UNP Q9UGN5 EXPRESSION TAG
SEQADV 5DSY HIS D 216 UNP Q9UGN5 EXPRESSION TAG
SEQADV 5DSY PRO D 217 UNP Q9UGN5 EXPRESSION TAG
SEQADV 5DSY GLU D 218 UNP Q9UGN5 EXPRESSION TAG
SEQADV 5DSY SER D 219 UNP Q9UGN5 EXPRESSION TAG
SEQADV 5DSY GLN D 220 UNP Q9UGN5 EXPRESSION TAG
SEQADV 5DSY LEU D 221 UNP Q9UGN5 EXPRESSION TAG
SEQADV 5DSY ASP D 222 UNP Q9UGN5 EXPRESSION TAG
SEQADV 5DSY LEU D 223 UNP Q9UGN5 EXPRESSION TAG
SEQADV 5DSY ARG D 224 UNP Q9UGN5 EXPRESSION TAG
SEQADV 5DSY VAL D 225 UNP Q9UGN5 EXPRESSION TAG
SEQADV 5DSY GLN D 226 UNP Q9UGN5 EXPRESSION TAG
SEQADV 5DSY GLU D 227 UNP Q9UGN5 EXPRESSION TAG
SEQADV 5DSY LEU D 228 UNP Q9UGN5 EXPRESSION TAG
SEQADV 5DSY ILE D 229 UNP Q9UGN5 EXPRESSION TAG
SEQADV 5DSY LYS D 230 UNP Q9UGN5 EXPRESSION TAG
SEQADV 5DSY LEU D 231 UNP Q9UGN5 EXPRESSION TAG
SEQADV 5DSY ILE D 232 UNP Q9UGN5 EXPRESSION TAG
SEQADV 5DSY CYS D 233 UNP Q9UGN5 EXPRESSION TAG
SEQADV 5DSY ASN D 234 UNP Q9UGN5 EXPRESSION TAG
SEQADV 5DSY VAL D 329 UNP Q9UGN5 EXPRESSION TAG
SEQADV 5DSY GLN D 330 UNP Q9UGN5 EXPRESSION TAG
SEQADV 5DSY ALA D 331 UNP Q9UGN5 EXPRESSION TAG
SEQADV 5DSY MET D 332 UNP Q9UGN5 EXPRESSION TAG
SEQADV 5DSY GLU D 333 UNP Q9UGN5 EXPRESSION TAG
SEQADV 5DSY GLU D 334 UNP Q9UGN5 EXPRESSION TAG
SEQRES 1 A 280 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 A 280 LEU VAL PRO ARG GLY SER HIS PRO GLU SER GLN LEU ASP
SEQRES 3 A 280 LEU ARG VAL GLN GLU LEU ILE LYS LEU ILE CYS ASN VAL
SEQRES 4 A 280 GLN ALA MET GLU GLU LYS THR GLU LEU GLN SER PRO GLU
SEQRES 5 A 280 HIS PRO LEU ASP GLN HIS TYR ARG ASN LEU HIS CYS ALA
SEQRES 6 A 280 LEU ARG PRO LEU ASP HIS GLU SER TYR GLU PHE LYS VAL
SEQRES 7 A 280 ILE SER GLN TYR LEU GLN SER THR HIS ALA PRO THR HIS
SEQRES 8 A 280 SER ASP TYR THR MET THR LEU LEU ASP LEU PHE GLU VAL
SEQRES 9 A 280 GLU LYS ASP GLY GLU LYS GLU ALA PHE ARG GLU ASP LEU
SEQRES 10 A 280 HIS ASN ARG MET LEU LEU TRP HIS GLY SER ARG MET SER
SEQRES 11 A 280 ASN TRP VAL GLY ILE LEU SER HIS GLY LEU ARG ILE ALA
SEQRES 12 A 280 PRO PRO GLU ALA PRO ILE THR GLY TYR MET PHE GLY LYS
SEQRES 13 A 280 GLY ILE TYR PHE ALA ASP MET SER SER LYS SER ALA ASN
SEQRES 14 A 280 TYR CYS PHE ALA SER ARG LEU LYS ASN THR GLY LEU LEU
SEQRES 15 A 280 LEU LEU SER GLU VAL ALA LEU GLY GLN CYS ASN GLU LEU
SEQRES 16 A 280 LEU GLU ALA ASN PRO LYS ALA GLU GLY LEU LEU GLN GLY
SEQRES 17 A 280 LYS HIS SER THR LYS GLY LEU GLY LYS MET ALA PRO SER
SEQRES 18 A 280 SER ALA HIS PHE VAL THR LEU ASN GLY SER THR VAL PRO
SEQRES 19 A 280 LEU GLY PRO ALA SER ASP THR GLY ILE LEU ASN PRO ASP
SEQRES 20 A 280 GLY TYR THR LEU ASN TYR ASN GLU TYR ILE VAL TYR ASN
SEQRES 21 A 280 PRO ASN GLN VAL ARG MET ARG TYR LEU LEU LYS VAL GLN
SEQRES 22 A 280 PHE ASN PHE LEU GLN LEU TRP
SEQRES 1 B 280 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 B 280 LEU VAL PRO ARG GLY SER HIS PRO GLU SER GLN LEU ASP
SEQRES 3 B 280 LEU ARG VAL GLN GLU LEU ILE LYS LEU ILE CYS ASN VAL
SEQRES 4 B 280 GLN ALA MET GLU GLU LYS THR GLU LEU GLN SER PRO GLU
SEQRES 5 B 280 HIS PRO LEU ASP GLN HIS TYR ARG ASN LEU HIS CYS ALA
SEQRES 6 B 280 LEU ARG PRO LEU ASP HIS GLU SER TYR GLU PHE LYS VAL
SEQRES 7 B 280 ILE SER GLN TYR LEU GLN SER THR HIS ALA PRO THR HIS
SEQRES 8 B 280 SER ASP TYR THR MET THR LEU LEU ASP LEU PHE GLU VAL
SEQRES 9 B 280 GLU LYS ASP GLY GLU LYS GLU ALA PHE ARG GLU ASP LEU
SEQRES 10 B 280 HIS ASN ARG MET LEU LEU TRP HIS GLY SER ARG MET SER
SEQRES 11 B 280 ASN TRP VAL GLY ILE LEU SER HIS GLY LEU ARG ILE ALA
SEQRES 12 B 280 PRO PRO GLU ALA PRO ILE THR GLY TYR MET PHE GLY LYS
SEQRES 13 B 280 GLY ILE TYR PHE ALA ASP MET SER SER LYS SER ALA ASN
SEQRES 14 B 280 TYR CYS PHE ALA SER ARG LEU LYS ASN THR GLY LEU LEU
SEQRES 15 B 280 LEU LEU SER GLU VAL ALA LEU GLY GLN CYS ASN GLU LEU
SEQRES 16 B 280 LEU GLU ALA ASN PRO LYS ALA GLU GLY LEU LEU GLN GLY
SEQRES 17 B 280 LYS HIS SER THR LYS GLY LEU GLY LYS MET ALA PRO SER
SEQRES 18 B 280 SER ALA HIS PHE VAL THR LEU ASN GLY SER THR VAL PRO
SEQRES 19 B 280 LEU GLY PRO ALA SER ASP THR GLY ILE LEU ASN PRO ASP
SEQRES 20 B 280 GLY TYR THR LEU ASN TYR ASN GLU TYR ILE VAL TYR ASN
SEQRES 21 B 280 PRO ASN GLN VAL ARG MET ARG TYR LEU LEU LYS VAL GLN
SEQRES 22 B 280 PHE ASN PHE LEU GLN LEU TRP
SEQRES 1 C 280 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 C 280 LEU VAL PRO ARG GLY SER HIS PRO GLU SER GLN LEU ASP
SEQRES 3 C 280 LEU ARG VAL GLN GLU LEU ILE LYS LEU ILE CYS ASN VAL
SEQRES 4 C 280 GLN ALA MET GLU GLU LYS THR GLU LEU GLN SER PRO GLU
SEQRES 5 C 280 HIS PRO LEU ASP GLN HIS TYR ARG ASN LEU HIS CYS ALA
SEQRES 6 C 280 LEU ARG PRO LEU ASP HIS GLU SER TYR GLU PHE LYS VAL
SEQRES 7 C 280 ILE SER GLN TYR LEU GLN SER THR HIS ALA PRO THR HIS
SEQRES 8 C 280 SER ASP TYR THR MET THR LEU LEU ASP LEU PHE GLU VAL
SEQRES 9 C 280 GLU LYS ASP GLY GLU LYS GLU ALA PHE ARG GLU ASP LEU
SEQRES 10 C 280 HIS ASN ARG MET LEU LEU TRP HIS GLY SER ARG MET SER
SEQRES 11 C 280 ASN TRP VAL GLY ILE LEU SER HIS GLY LEU ARG ILE ALA
SEQRES 12 C 280 PRO PRO GLU ALA PRO ILE THR GLY TYR MET PHE GLY LYS
SEQRES 13 C 280 GLY ILE TYR PHE ALA ASP MET SER SER LYS SER ALA ASN
SEQRES 14 C 280 TYR CYS PHE ALA SER ARG LEU LYS ASN THR GLY LEU LEU
SEQRES 15 C 280 LEU LEU SER GLU VAL ALA LEU GLY GLN CYS ASN GLU LEU
SEQRES 16 C 280 LEU GLU ALA ASN PRO LYS ALA GLU GLY LEU LEU GLN GLY
SEQRES 17 C 280 LYS HIS SER THR LYS GLY LEU GLY LYS MET ALA PRO SER
SEQRES 18 C 280 SER ALA HIS PHE VAL THR LEU ASN GLY SER THR VAL PRO
SEQRES 19 C 280 LEU GLY PRO ALA SER ASP THR GLY ILE LEU ASN PRO ASP
SEQRES 20 C 280 GLY TYR THR LEU ASN TYR ASN GLU TYR ILE VAL TYR ASN
SEQRES 21 C 280 PRO ASN GLN VAL ARG MET ARG TYR LEU LEU LYS VAL GLN
SEQRES 22 C 280 PHE ASN PHE LEU GLN LEU TRP
SEQRES 1 D 280 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 D 280 LEU VAL PRO ARG GLY SER HIS PRO GLU SER GLN LEU ASP
SEQRES 3 D 280 LEU ARG VAL GLN GLU LEU ILE LYS LEU ILE CYS ASN VAL
SEQRES 4 D 280 GLN ALA MET GLU GLU LYS THR GLU LEU GLN SER PRO GLU
SEQRES 5 D 280 HIS PRO LEU ASP GLN HIS TYR ARG ASN LEU HIS CYS ALA
SEQRES 6 D 280 LEU ARG PRO LEU ASP HIS GLU SER TYR GLU PHE LYS VAL
SEQRES 7 D 280 ILE SER GLN TYR LEU GLN SER THR HIS ALA PRO THR HIS
SEQRES 8 D 280 SER ASP TYR THR MET THR LEU LEU ASP LEU PHE GLU VAL
SEQRES 9 D 280 GLU LYS ASP GLY GLU LYS GLU ALA PHE ARG GLU ASP LEU
SEQRES 10 D 280 HIS ASN ARG MET LEU LEU TRP HIS GLY SER ARG MET SER
SEQRES 11 D 280 ASN TRP VAL GLY ILE LEU SER HIS GLY LEU ARG ILE ALA
SEQRES 12 D 280 PRO PRO GLU ALA PRO ILE THR GLY TYR MET PHE GLY LYS
SEQRES 13 D 280 GLY ILE TYR PHE ALA ASP MET SER SER LYS SER ALA ASN
SEQRES 14 D 280 TYR CYS PHE ALA SER ARG LEU LYS ASN THR GLY LEU LEU
SEQRES 15 D 280 LEU LEU SER GLU VAL ALA LEU GLY GLN CYS ASN GLU LEU
SEQRES 16 D 280 LEU GLU ALA ASN PRO LYS ALA GLU GLY LEU LEU GLN GLY
SEQRES 17 D 280 LYS HIS SER THR LYS GLY LEU GLY LYS MET ALA PRO SER
SEQRES 18 D 280 SER ALA HIS PHE VAL THR LEU ASN GLY SER THR VAL PRO
SEQRES 19 D 280 LEU GLY PRO ALA SER ASP THR GLY ILE LEU ASN PRO ASP
SEQRES 20 D 280 GLY TYR THR LEU ASN TYR ASN GLU TYR ILE VAL TYR ASN
SEQRES 21 D 280 PRO ASN GLN VAL ARG MET ARG TYR LEU LEU LYS VAL GLN
SEQRES 22 D 280 PHE ASN PHE LEU GLN LEU TRP
HET UHB A1001 39
HET UHB B1001 39
HET UHB C1001 39
HET UHB D1001 39
HETNAM UHB 2-[4-[(2S,3S,4R,5R)-5-(6-AMINOPURIN-9-YL)-3,4-
HETNAM 2 UHB BIS(OXIDANYL)OXOLAN-2-YL]CARBONYLPIPERAZIN-1-YL]-N-(1-
HETNAM 3 UHB OXIDANYLIDENE-2,3-DIHYDROISOINDOL-4-YL)ETHANAMIDE
FORMUL 5 UHB 4(C24 H27 N9 O6)
FORMUL 9 HOH *51(H2 O)
HELIX 1 AA1 ASP A 222 CYS A 233 1 12
HELIX 2 AA2 HIS A 343 ASN A 351 1 9
HELIX 3 AA3 SER A 363 THR A 376 1 14
HELIX 4 AA4 GLY A 398 PHE A 403 1 6
HELIX 5 AA5 ARG A 418 SER A 420 5 3
HELIX 6 AA6 ASN A 421 GLY A 429 1 9
HELIX 7 AA7 MET A 453 ASN A 459 1 7
HELIX 8 AA8 GLU A 493 GLN A 497 5 5
HELIX 9 AA9 SER A 512 PHE A 515 5 4
HELIX 10 AB1 ASN A 550 ASN A 552 5 3
HELIX 11 AB2 ASP B 222 CYS B 233 1 12
HELIX 12 AB3 HIS B 343 ASN B 351 1 9
HELIX 13 AB4 SER B 363 THR B 376 1 14
HELIX 14 AB5 GLY B 398 PHE B 403 1 6
HELIX 15 AB6 ARG B 418 SER B 420 5 3
HELIX 16 AB7 ASN B 421 GLY B 429 1 9
HELIX 17 AB8 MET B 453 ASN B 459 1 7
HELIX 18 AB9 TYR B 460 PHE B 462 5 3
HELIX 19 AC1 GLU B 493 GLN B 497 5 5
HELIX 20 AC2 SER B 512 PHE B 515 5 4
HELIX 21 AC3 ASN B 550 ASN B 552 5 3
HELIX 22 AC4 ASP C 222 ASN C 234 1 13
HELIX 23 AC5 HIS C 343 ASN C 351 1 9
HELIX 24 AC6 SER C 363 THR C 376 1 14
HELIX 25 AC7 GLY C 398 PHE C 403 1 6
HELIX 26 AC8 ARG C 418 SER C 420 5 3
HELIX 27 AC9 ASN C 421 GLY C 429 1 9
HELIX 28 AD1 MET C 453 ASN C 459 1 7
HELIX 29 AD2 TYR C 460 PHE C 462 5 3
HELIX 30 AD3 ASN C 489 GLN C 497 5 9
HELIX 31 AD4 SER C 512 PHE C 515 5 4
HELIX 32 AD5 ASN C 550 ASN C 552 5 3
HELIX 33 AD6 ASP D 222 CYS D 233 1 12
HELIX 34 AD7 HIS D 343 ASN D 351 1 9
HELIX 35 AD8 SER D 363 THR D 376 1 14
HELIX 36 AD9 GLY D 398 PHE D 403 1 6
HELIX 37 AE1 ARG D 418 SER D 420 5 3
HELIX 38 AE2 ASN D 421 GLY D 429 1 9
HELIX 39 AE3 MET D 453 ASN D 459 1 7
HELIX 40 AE4 TYR D 460 PHE D 462 5 3
HELIX 41 AE5 GLU D 493 GLN D 497 5 5
HELIX 42 AE6 SER D 511 PHE D 515 5 5
HELIX 43 AE7 ASN D 550 ASN D 552 5 3
SHEET 1 AA1 5 CYS A 354 PRO A 358 0
SHEET 2 AA1 5 TYR A 384 LYS A 396 -1 O GLU A 393 N ARG A 357
SHEET 3 AA1 5 VAL A 554 PHE A 566 -1 O ARG A 557 N VAL A 394
SHEET 4 AA1 5 THR A 469 ALA A 478 -1 N LEU A 472 O LEU A 560
SHEET 5 AA1 5 ARG A 410 GLY A 416 -1 N MET A 411 O VAL A 477
SHEET 1 AA2 4 ILE A 448 PHE A 450 0
SHEET 2 AA2 4 GLU A 545 VAL A 548 -1 O VAL A 548 N ILE A 448
SHEET 3 AA2 4 SER A 501 GLY A 504 -1 N THR A 502 O ILE A 547
SHEET 4 AA2 4 CYS A 482 LEU A 485 1 N ASN A 483 O LYS A 503
SHEET 1 AA3 3 ALA A 528 ASP A 530 0
SHEET 2 AA3 3 GLY A 506 PRO A 510 -1 N ALA A 509 O SER A 529
SHEET 3 AA3 3 LEU A 541 TYR A 543 1 O LEU A 541 N LYS A 507
SHEET 1 AA4 2 VAL A 516 LEU A 518 0
SHEET 2 AA4 2 SER A 521 VAL A 523 -1 O VAL A 523 N VAL A 516
SHEET 1 AA5 5 CYS B 354 PRO B 358 0
SHEET 2 AA5 5 TYR B 384 LYS B 396 -1 O GLU B 393 N ARG B 357
SHEET 3 AA5 5 VAL B 554 PHE B 566 -1 O GLN B 563 N THR B 387
SHEET 4 AA5 5 THR B 469 ALA B 478 -1 N LEU B 472 O LEU B 560
SHEET 5 AA5 5 ARG B 410 GLY B 416 -1 N HIS B 415 O LEU B 473
SHEET 1 AA6 4 ILE B 448 PHE B 450 0
SHEET 2 AA6 4 GLU B 545 VAL B 548 -1 O TYR B 546 N PHE B 450
SHEET 3 AA6 4 SER B 501 GLY B 504 -1 N GLY B 504 O GLU B 545
SHEET 4 AA6 4 CYS B 482 LEU B 485 1 N ASN B 483 O SER B 501
SHEET 1 AA7 2 MET B 508 PRO B 510 0
SHEET 2 AA7 2 ALA B 528 ASP B 530 -1 O SER B 529 N ALA B 509
SHEET 1 AA8 2 VAL B 516 LEU B 518 0
SHEET 2 AA8 2 SER B 521 VAL B 523 -1 O VAL B 523 N VAL B 516
SHEET 1 AA9 5 CYS C 354 PRO C 358 0
SHEET 2 AA9 5 TYR C 384 LYS C 396 -1 O GLU C 393 N ARG C 357
SHEET 3 AA9 5 VAL C 554 PHE C 566 -1 O LYS C 561 N ASP C 390
SHEET 4 AA9 5 THR C 469 ALA C 478 -1 N GLY C 470 O VAL C 562
SHEET 5 AA9 5 ARG C 410 GLY C 416 -1 N MET C 411 O VAL C 477
SHEET 1 AB1 4 ILE C 448 PHE C 450 0
SHEET 2 AB1 4 GLU C 545 VAL C 548 -1 O VAL C 548 N ILE C 448
SHEET 3 AB1 4 SER C 501 GLY C 504 -1 N THR C 502 O ILE C 547
SHEET 4 AB1 4 CYS C 482 LEU C 485 1 N ASN C 483 O SER C 501
SHEET 1 AB2 3 ALA C 528 ASP C 530 0
SHEET 2 AB2 3 GLY C 506 PRO C 510 -1 N ALA C 509 O SER C 529
SHEET 3 AB2 3 LEU C 541 TYR C 543 1 O LEU C 541 N LYS C 507
SHEET 1 AB3 2 VAL C 516 LEU C 518 0
SHEET 2 AB3 2 SER C 521 VAL C 523 -1 O VAL C 523 N VAL C 516
SHEET 1 AB4 5 CYS D 354 LEU D 359 0
SHEET 2 AB4 5 TYR D 384 LYS D 396 -1 O GLU D 393 N ARG D 357
SHEET 3 AB4 5 VAL D 554 PHE D 566 -1 O ARG D 557 N VAL D 394
SHEET 4 AB4 5 THR D 469 ALA D 478 -1 N LEU D 472 O LEU D 560
SHEET 5 AB4 5 ARG D 410 GLY D 416 -1 N MET D 411 O VAL D 477
SHEET 1 AB5 4 ILE D 448 ALA D 451 0
SHEET 2 AB5 4 GLU D 545 VAL D 548 -1 O VAL D 548 N ILE D 448
SHEET 3 AB5 4 SER D 501 GLY D 504 -1 N GLY D 504 O GLU D 545
SHEET 4 AB5 4 CYS D 482 LEU D 485 1 N ASN D 483 O SER D 501
SHEET 1 AB6 3 SER D 529 ASP D 530 0
SHEET 2 AB6 3 GLY D 506 ALA D 509 -1 N ALA D 509 O SER D 529
SHEET 3 AB6 3 LEU D 541 TYR D 543 1 O LEU D 541 N LYS D 507
SHEET 1 AB7 2 VAL D 516 LEU D 518 0
SHEET 2 AB7 2 SER D 521 VAL D 523 -1 O VAL D 523 N VAL D 516
CISPEP 1 GLY A 526 PRO A 527 0 6.70
CISPEP 2 GLY B 526 PRO B 527 0 6.28
CISPEP 3 GLY C 526 PRO C 527 0 4.86
CISPEP 4 GLY D 526 PRO D 527 0 7.40
SITE 1 AC1 15 TRP A 414 HIS A 415 GLY A 416 SER A 417
SITE 2 AC1 15 ASN A 421 GLY A 424 ILE A 425 GLY A 429
SITE 3 AC1 15 ARG A 431 ALA A 433 TYR A 449 SER A 457
SITE 4 AC1 15 TYR A 460 GLU A 545 HOH A1112
SITE 1 AC2 15 TRP B 414 HIS B 415 GLY B 416 SER B 417
SITE 2 AC2 15 GLY B 424 ILE B 425 GLY B 429 LEU B 430
SITE 3 AC2 15 ARG B 431 ALA B 433 PRO B 434 TYR B 449
SITE 4 AC2 15 SER B 457 TYR B 460 GLU B 545
SITE 1 AC3 16 LEU A 466 HIS C 415 GLY C 416 SER C 417
SITE 2 AC3 16 ASN C 421 GLY C 424 ILE C 425 GLY C 429
SITE 3 AC3 16 ARG C 431 ALA C 433 TYR C 449 SER C 457
SITE 4 AC3 16 TYR C 460 GLU C 545 HOH C1106 HOH C1114
SITE 1 AC4 14 LEU B 466 HIS D 415 GLY D 416 SER D 417
SITE 2 AC4 14 ASN D 421 GLY D 424 ILE D 425 GLY D 429
SITE 3 AC4 14 ARG D 431 PRO D 434 TYR D 442 TYR D 449
SITE 4 AC4 14 SER D 457 TYR D 460
CRYST1 92.163 119.900 120.739 90.00 90.00 90.00 P 21 21 21 16
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.010850 0.000000 0.000000 0.00000
SCALE2 0.000000 0.008340 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008282 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
