HEADER TRANSCRIPTION 15-AUG-17 5OR9
TITLE CRYSTAL STRUCTURE OF BAZ2B BROMODOMAIN IN COMPLEX WITH 1-METHYL-
TITLE 2 CYCLOPENTAPYRAZOLE COMPOUND 13
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: BROMODOMAIN ADJACENT TO ZINC FINGER DOMAIN PROTEIN 2B;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: BROMODOMAIN, UNP RESIDUES 1954-2068;
COMPND 5 SYNONYM: HWALP4;
COMPND 6 ENGINEERED: YES;
COMPND 7 MUTATION: YES;
COMPND 8 OTHER_DETAILS: FIRST TWO RESIDUES SM DERIVE FROM THE EXPRESSION TAG
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: BAZ2B, KIAA1476;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS FOUR HELICAL BUNDLE, TRANSCRIPTION
EXPDTA X-RAY DIFFRACTION
AUTHOR G.LOLLI,A.D.VEDOVE,J.-R.MARCHAND,A.CAFLISCH
REVDAT 3 17-JAN-24 5OR9 1 REMARK
REVDAT 2 01-NOV-17 5OR9 1 JRNL
REVDAT 1 13-SEP-17 5OR9 0
JRNL AUTH J.R.MARCHAND,A.DALLE VEDOVE,G.LOLLI,A.CAFLISCH
JRNL TITL DISCOVERY OF INHIBITORS OF FOUR BROMODOMAINS BY
JRNL TITL 2 FRAGMENT-ANCHORED LIGAND DOCKING.
JRNL REF J CHEM INF MODEL V. 57 2584 2017
JRNL REFN ESSN 1549-960X
JRNL PMID 28862840
JRNL DOI 10.1021/ACS.JCIM.7B00336
REMARK 2
REMARK 2 RESOLUTION. 2.00 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (1.11.1_2575: ???)
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) : 2.00
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 40.72
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.2
REMARK 3 NUMBER OF REFLECTIONS : 15606
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.189
REMARK 3 R VALUE (WORKING SET) : 0.187
REMARK 3 FREE R VALUE : 0.208
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.180
REMARK 3 FREE R VALUE TEST SET COUNT : 808
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 40.7304 - 3.6336 1.00 2612 131 0.1665 0.1804
REMARK 3 2 3.6336 - 2.8843 1.00 2461 149 0.1885 0.2226
REMARK 3 3 2.8843 - 2.5198 1.00 2450 134 0.1782 0.1899
REMARK 3 4 2.5198 - 2.2894 0.99 2456 139 0.2020 0.2220
REMARK 3 5 2.2894 - 2.1254 0.98 2394 129 0.2311 0.2567
REMARK 3 6 2.1254 - 2.0001 0.98 2425 126 0.2730 0.2909
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) : 0.210
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 27.410
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 : 0.006 1014
REMARK 3 ANGLE : 0.800 1369
REMARK 3 CHIRALITY : 0.044 144
REMARK 3 PLANARITY : 0.004 171
REMARK 3 DIHEDRAL : 16.123 622
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 4
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 1856 THROUGH 1868 )
REMARK 3 ORIGIN FOR THE GROUP (A): -1.4641 34.3934 -9.7388
REMARK 3 T TENSOR
REMARK 3 T11: 0.3343 T22: 0.5552
REMARK 3 T33: 0.5146 T12: 0.0164
REMARK 3 T13: -0.0433 T23: -0.0331
REMARK 3 L TENSOR
REMARK 3 L11: 0.0354 L22: -0.0022
REMARK 3 L33: -0.0348 L12: 0.0318
REMARK 3 L13: 0.0883 L23: -0.0943
REMARK 3 S TENSOR
REMARK 3 S11: -0.2543 S12: -0.3333 S13: 0.2519
REMARK 3 S21: -0.1489 S22: 0.0264 S23: -0.1470
REMARK 3 S31: 0.2949 S32: -0.1700 S33: -0.0005
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 1869 THROUGH 1882 )
REMARK 3 ORIGIN FOR THE GROUP (A): 20.4355 29.9085 -2.0626
REMARK 3 T TENSOR
REMARK 3 T11: 0.2643 T22: 0.3375
REMARK 3 T33: 0.3893 T12: -0.0016
REMARK 3 T13: 0.0116 T23: -0.0187
REMARK 3 L TENSOR
REMARK 3 L11: 0.0351 L22: 0.0053
REMARK 3 L33: -0.0060 L12: -0.0315
REMARK 3 L13: -0.0351 L23: -0.0287
REMARK 3 S TENSOR
REMARK 3 S11: -0.1023 S12: 0.0913 S13: 0.1052
REMARK 3 S21: 0.0572 S22: -0.0379 S23: -0.1378
REMARK 3 S31: -0.2614 S32: 0.1410 S33: 0.0000
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 1883 THROUGH 1943 )
REMARK 3 ORIGIN FOR THE GROUP (A): 20.3456 15.1946 -4.3357
REMARK 3 T TENSOR
REMARK 3 T11: 0.3015 T22: 0.2644
REMARK 3 T33: 0.2853 T12: -0.0080
REMARK 3 T13: 0.0022 T23: 0.0015
REMARK 3 L TENSOR
REMARK 3 L11: 0.7758 L22: 0.2535
REMARK 3 L33: 0.6815 L12: -0.2474
REMARK 3 L13: -0.2053 L23: 0.0576
REMARK 3 S TENSOR
REMARK 3 S11: 0.0726 S12: 0.0699 S13: -0.0899
REMARK 3 S21: -0.1693 S22: -0.0814 S23: 0.0195
REMARK 3 S31: 0.3812 S32: -0.0185 S33: 0.0001
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 1944 THROUGH 1971 )
REMARK 3 ORIGIN FOR THE GROUP (A): 17.6107 20.2646 7.2938
REMARK 3 T TENSOR
REMARK 3 T11: 0.4964 T22: 0.3910
REMARK 3 T33: 0.3374 T12: 0.0675
REMARK 3 T13: 0.0302 T23: -0.0240
REMARK 3 L TENSOR
REMARK 3 L11: 0.1014 L22: 0.0779
REMARK 3 L33: 0.5124 L12: 0.0181
REMARK 3 L13: -0.1542 L23: 0.0637
REMARK 3 S TENSOR
REMARK 3 S11: -0.2152 S12: -0.3492 S13: 0.0521
REMARK 3 S21: 0.5119 S22: 0.1984 S23: 0.0050
REMARK 3 S31: -0.0723 S32: -0.2058 S33: 0.0001
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 5OR9 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 16-AUG-17.
REMARK 100 THE DEPOSITION ID IS D_1200006205.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 05-JUL-17
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ELETTRA
REMARK 200 BEAMLINE : 5.2R
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.00
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 2M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : AIMLESS 0.5.32
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 15678
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.000
REMARK 200 RESOLUTION RANGE LOW (A) : 48.320
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.7
REMARK 200 DATA REDUNDANCY : 7.200
REMARK 200 R MERGE (I) : 0.07800
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 14.5000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.00
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.05
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.3
REMARK 200 DATA REDUNDANCY IN SHELL : 7.50
REMARK 200 R MERGE FOR SHELL (I) : 0.66800
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
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: 5DYU
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 70.62
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.19
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 20% PEG500MME, 2% PEG1000, 2% PEG3350,
REMARK 280 10% PEG20000, 2% MPD, PH 7.5, VAPOR DIFFUSION, SITTING DROP,
REMARK 280 TEMPERATURE 277K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z+1/2
REMARK 290 3555 -X,Y,-Z+1/2
REMARK 290 4555 X,-Y,-Z
REMARK 290 5555 X+1/2,Y+1/2,Z
REMARK 290 6555 -X+1/2,-Y+1/2,Z+1/2
REMARK 290 7555 -X+1/2,Y+1/2,-Z+1/2
REMARK 290 8555 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 0.00000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 28.79200
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 28.79200
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 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 40.72200
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 48.32300
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 40.72200
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 48.32300
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 28.79200
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 40.72200
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 48.32300
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 28.79200
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 40.72200
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 48.32300
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 0.00000
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: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 160 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 7870 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 2.0 KCAL/MOL
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 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 SER A 1972
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue JR5 A 2001
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 2002
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 5OR8 RELATED DB: PDB
REMARK 900 5OR8 CONTAINS THE SIMILAR BROMODOMAIN BAZ2A COMPLEXED WITH A
REMARK 900 SIMILAR COMPOUND
DBREF 5OR9 A 1858 1972 UNP Q9UIF8 BAZ2B_HUMAN 1954 2068
SEQADV 5OR9 SER A 1856 UNP Q9UIF8 EXPRESSION TAG
SEQADV 5OR9 MET A 1857 UNP Q9UIF8 EXPRESSION TAG
SEQRES 1 A 117 SER MET SER VAL LYS LYS PRO LYS ARG ASP ASP SER LYS
SEQRES 2 A 117 ASP LEU ALA LEU CYS SER MET ILE LEU THR GLU MET GLU
SEQRES 3 A 117 THR HIS GLU ASP ALA TRP PRO PHE LEU LEU PRO VAL ASN
SEQRES 4 A 117 LEU LYS LEU VAL PRO GLY TYR LYS LYS VAL ILE LYS LYS
SEQRES 5 A 117 PRO MET ASP PHE SER THR ILE ARG GLU LYS LEU SER SER
SEQRES 6 A 117 GLY GLN TYR PRO ASN LEU GLU THR PHE ALA LEU ASP VAL
SEQRES 7 A 117 ARG LEU VAL PHE ASP ASN CYS GLU THR PHE ASN GLU ASP
SEQRES 8 A 117 ASP SER ASP ILE GLY ARG ALA GLY HIS ASN MET ARG LYS
SEQRES 9 A 117 TYR PHE GLU LYS LYS TRP THR ASP THR PHE LYS VAL SER
HET JR5 A2001 27
HET EDO A2002 4
HETNAM JR5 (2~{S})-1-(4-FLUOROPHENYL)SULFONYL-~{N}-(2-METHYL-5,6-
HETNAM 2 JR5 DIHYDRO-4~{H}-CYCLOPENTA[C]PYRAZOL-3-YL)PYRROLIDINE-2-
HETNAM 3 JR5 CARBOXAMIDE
HETNAM EDO 1,2-ETHANEDIOL
HETSYN EDO ETHYLENE GLYCOL
FORMUL 2 JR5 C18 H21 F N4 O3 S
FORMUL 3 EDO C2 H6 O2
FORMUL 4 HOH *93(H2 O)
HELIX 1 AA1 LYS A 1868 HIS A 1883 1 16
HELIX 2 AA2 GLU A 1884 LEU A 1890 5 7
HELIX 3 AA3 GLY A 1900 ILE A 1905 1 6
HELIX 4 AA4 ASP A 1910 SER A 1920 1 11
HELIX 5 AA5 ASN A 1925 ASN A 1944 1 20
HELIX 6 AA6 SER A 1948 LYS A 1970 1 23
SITE 1 AC1 12 LYS A1861 TRP A1887 PRO A1888 PHE A1889
SITE 2 AC1 12 LEU A1891 PRO A1892 VAL A1893 PHE A1943
SITE 3 AC1 12 ASN A1944 ILE A1950 HOH A2110 HOH A2138
SITE 1 AC2 1 LYS A1896
CRYST1 81.444 96.646 57.584 90.00 90.00 90.00 C 2 2 21 8
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.012278 0.000000 0.000000 0.00000
SCALE2 0.000000 0.010347 0.000000 0.00000
SCALE3 0.000000 0.000000 0.017366 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
