HEADER TRANSCRIPTION 29-JUN-13 4BW3
TITLE THE FIRST BROMODOMAIN OF HUMAN BRD4 IN COMPLEX WITH 3,5
TITLE 2 DIMETHYLISOXAXOLE LIGAND
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: BROMODOMAIN-CONTAINING PROTEIN 4;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: N-TERMINAL BROMODOMAIN, RESIDUES 44-168;
COMPND 5 SYNONYM: BRD4, PROTEIN HUNK1;
COMPND 6 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: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS TRANSCRIPTION, INHIBITOR, HISTONE, EPIGENETIC READER, ANTAGONIST
EXPDTA X-RAY DIFFRACTION
AUTHOR C.CHUNG,O.MIRGUET,Y.LAMOTTE,P.BAMBOROUGH,D.DELANNEE,A.BOUILLOT,
AUTHOR 2 F.GELLIBERT,G.KRYSA,A.LEWIS,J.WITHERINGTON,P.HUET,Y.DUDIT,L.TROTTET,
AUTHOR 3 E.NICODEME
REVDAT 2 19-MAR-14 4BW3 1 JRNL
REVDAT 1 11-SEP-13 4BW3 0
JRNL AUTH O.MIRGUET,Y.LAMOTTE,C.CHUNG,P.BAMBOROUGH,D.DELANNEE,
JRNL AUTH 2 A.BOUILLOT,F.GELLIBERT,G.KRYSA,A.LEWIS,J.WITHERINGTON,
JRNL AUTH 3 P.HUET,Y.DUDIT,L.TROTTET,E.NICODEME
JRNL TITL NAPHTHYRIDINES AS NOVEL BET FAMILY BROMODOMAIN INHIBITORS.
JRNL REF CHEMMEDCHEM V. 9 589 2014
JRNL REFN ISSN 1860-7179
JRNL PMID 24000170
JRNL DOI 10.1002/CMDC.201300259
REMARK 2
REMARK 2 RESOLUTION. 1.50 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.7.0029
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,
REMARK 3 STEINER,NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.50
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 38.14
REMARK 3 DATA CUTOFF (SIGMA(F)) : NONE
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.69
REMARK 3 NUMBER OF REFLECTIONS : 20307
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) : 0.20460
REMARK 3 R VALUE (WORKING SET) : 0.20323
REMARK 3 FREE R VALUE : 0.23067
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.1
REMARK 3 FREE R VALUE TEST SET COUNT : 1098
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 1.500
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.539
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1460
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.48
REMARK 3 BIN R VALUE (WORKING SET) : 0.315
REMARK 3 BIN FREE R VALUE SET COUNT : 84
REMARK 3 BIN FREE R VALUE : 0.343
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 1076
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 45
REMARK 3 SOLVENT ATOMS : 190
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 24.755
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.40
REMARK 3 B22 (A**2) : -0.40
REMARK 3 B33 (A**2) : 0.80
REMARK 3 B12 (A**2) : 0.00
REMARK 3 B13 (A**2) : 0.00
REMARK 3 B23 (A**2) : 0.00
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.092
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.090
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.060
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 3.169
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.959
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.950
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 1154 ; 0.005 ; 0.020
REMARK 3 BOND LENGTHS OTHERS (A): 1101 ; 0.001 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 1573 ; 1.043 ; 1.971
REMARK 3 BOND ANGLES OTHERS (DEGREES): 2543 ; 0.721 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 132 ; 4.741 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 55 ;33.910 ;26.000
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 203 ;10.934 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 3 ;18.470 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 162 ; 0.057 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 1279 ; 0.003 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 254 ; 0.001 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 1
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 42 A 168
REMARK 3 ORIGIN FOR THE GROUP (A): 3.9829 5.2841 19.7549
REMARK 3 T TENSOR
REMARK 3 T11: 0.1124 T22: 0.0933
REMARK 3 T33: 0.0159 T12: 0.0091
REMARK 3 T13: -0.0105 T23: -0.0249
REMARK 3 L TENSOR
REMARK 3 L11: 0.9123 L22: 0.8895
REMARK 3 L33: 0.8984 L12: -0.2498
REMARK 3 L13: -0.3956 L23: 0.8797
REMARK 3 S TENSOR
REMARK 3 S11: -0.0373 S12: 0.0396 S13: -0.0790
REMARK 3 S21: -0.0296 S22: -0.0497 S23: 0.0817
REMARK 3 S31: -0.0222 S32: -0.0386 S33: 0.0869
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : BABINET MODEL WITH MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.20
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE
REMARK 3 RIDING POSITIONS.
REMARK 4
REMARK 4 4BW3 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 01-JUL-13.
REMARK 100 THE PDBE ID CODE IS EBI-57535.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 28-JAN-13
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : ID29
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97630
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : NULL
REMARK 200 DETECTOR MANUFACTURER : NULL
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 21405
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.50
REMARK 200 RESOLUTION RANGE LOW (A) : 38.14
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.0
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 15.5
REMARK 200 DATA REDUNDANCY : 6.4
REMARK 200 R MERGE (I) : 0.06
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 15.50
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.50
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.58
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.7
REMARK 200 DATA REDUNDANCY IN SHELL : 6.5
REMARK 200 R MERGE FOR SHELL (I) : 0.60
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 3.10
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: NULL
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 42.80
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.15
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 20% PEG3350, 0.2M NANO3, 0.1M
REMARK 280 BIS-TRIS-PROPANE PH8.5
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 21.78500
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 30.51000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 24.42500
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 30.51000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 21.78500
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 24.42500
REMARK 290 SMTRY3 4 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 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 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 O2 EDO A 1171 O HOH A 2085 2.18
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 EDO A1169
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A1170
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A1171
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 9BM A1172
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4BW1 RELATED DB: PDB
REMARK 900 THE FIRST BROMODOMAIN OF HUMAN BRD4 IN COMPLEX WITH
REMARK 900 3,5 DIMETHYLISOXAXOLE LIGAND
REMARK 900 RELATED ID: 4BW2 RELATED DB: PDB
REMARK 900 THE FIRST BROMODOMAIN OF HUMAN BRD4 IN COMPLEX WITH
REMARK 900 3,5 DIMETHYLISOXAXOLE LIGAND
REMARK 900 RELATED ID: 4BW4 RELATED DB: PDB
REMARK 900 THE FIRST BROMODOMAIN OF HUMAN BRD4 IN COMPLEX WITH
REMARK 900 3,5 DIMETHYLISOXAXOLE LIGAND
DBREF 4BW3 A 44 168 UNP O60885 BRD4_HUMAN 44 168
SEQADV 4BW3 SER A 42 UNP O60885 EXPRESSION TAG
SEQADV 4BW3 MET A 43 UNP O60885 EXPRESSION TAG
SEQRES 1 A 127 SER MET ASN PRO PRO PRO PRO GLU THR SER ASN PRO ASN
SEQRES 2 A 127 LYS PRO LYS ARG GLN THR ASN GLN LEU GLN TYR LEU LEU
SEQRES 3 A 127 ARG VAL VAL LEU LYS THR LEU TRP LYS HIS GLN PHE ALA
SEQRES 4 A 127 TRP PRO PHE GLN GLN PRO VAL ASP ALA VAL LYS LEU ASN
SEQRES 5 A 127 LEU PRO ASP TYR TYR LYS ILE ILE LYS THR PRO MET ASP
SEQRES 6 A 127 MET GLY THR ILE LYS LYS ARG LEU GLU ASN ASN TYR TYR
SEQRES 7 A 127 TRP ASN ALA GLN GLU CYS ILE GLN ASP PHE ASN THR MET
SEQRES 8 A 127 PHE THR ASN CYS TYR ILE TYR ASN LYS PRO GLY ASP ASP
SEQRES 9 A 127 ILE VAL LEU MET ALA GLU ALA LEU GLU LYS LEU PHE LEU
SEQRES 10 A 127 GLN LYS ILE ASN GLU LEU PRO THR GLU GLU
HET EDO A1169 4
HET EDO A1170 4
HET EDO A1171 4
HET 9BM A1172 33
HETNAM EDO 1,2-ETHANEDIOL
HETNAM 9BM 4-((2-(TERT-BUTYL)PHENYL)AMINO)-7-(3,5-
HETNAM 2 9BM DIMETHYLISOXAZOL-4-YL)-6-METHOXY-1,5-NAPHTHYRIDINE-
HETNAM 3 9BM 3-CARBOXYLIC ACID
HETSYN EDO ETHYLENE GLYCOL
FORMUL 2 EDO 3(C2 H6 O2)
FORMUL 3 9BM C25 H26 N4 O4
FORMUL 4 HOH *190(H2 O)
HELIX 1 1 THR A 60 VAL A 69 1 10
HELIX 2 2 VAL A 69 LYS A 76 1 8
HELIX 3 3 ALA A 80 GLN A 84 5 5
HELIX 4 4 ASP A 96 ILE A 101 1 6
HELIX 5 5 ASP A 106 ASN A 116 1 11
HELIX 6 6 ASN A 121 ASN A 140 1 20
HELIX 7 7 ASP A 144 GLU A 163 1 20
SITE 1 AC1 2 EDO A1171 HOH A2085
SITE 1 AC2 3 GLN A 64 LYS A 155 GLN A 159
SITE 1 AC3 6 PRO A 86 GLY A 108 THR A 109 LYS A 112
SITE 2 AC3 6 EDO A1169 HOH A2085
SITE 1 AC4 13 SER A 51 LYS A 57 TRP A 81 PRO A 82
SITE 2 AC4 13 PHE A 83 LEU A 92 ASN A 116 ASN A 140
SITE 3 AC4 13 ILE A 146 HOH A2081 HOH A2110 HOH A2188
SITE 4 AC4 13 HOH A2189
CRYST1 43.570 48.850 61.020 90.00 90.00 90.00 P 21 21 21 4
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 0.022952 0.000000 0.000000 0.00000
SCALE2 0.000000 0.020471 0.000000 0.00000
SCALE3 0.000000 0.000000 0.016388 0.00000
(ATOM LINES ARE NOT SHOWN.)
END