HEADER PROTEIN BINDING 26-FEB-12 4AKN
TITLE N-TERMINAL BROMODOMAIN OF HUMAN BRD2 WITH TBUTYL-PHENYL-AMINO-
TITLE 2 DIMETHYL-OXAZOLYL-QUINOLINE-CARBOXYLIC ACID
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: BROMODOMAIN-CONTAINING PROTEIN 2;
COMPND 3 CHAIN: A, B, C;
COMPND 4 FRAGMENT: RESIDUES 67-200;
COMPND 5 SYNONYM: O27.1.1, REALLY INTERESTING NEW GENE 3 PROTEIN HUMAN BRD2;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_TAXID: 9606;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS PROTEIN BINDING, INHIBITOR, HISTONE, EPIGENETIC READER
EXPDTA X-RAY DIFFRACTION
AUTHOR C.CHUNG,Y.LAMOTTE,F.DONCHE,A.BOUILLOT,O.MIRGUET
REVDAT 3 15-MAY-19 4AKN 1 REMARK
REVDAT 2 14-NOV-12 4AKN 1 SEQADV
REVDAT 1 04-JUL-12 4AKN 0
JRNL AUTH J.SEAL,Y.LAMOTTE,F.DONCHE,A.BOUILLOT,O.MIRGUET,F.GELLIBERT,
JRNL AUTH 2 E.NICODEME,G.KRYSA,J.KIRILOVSKY,S.BEINKE,S.MCCLEARY,I.RIOJA,
JRNL AUTH 3 P.BAMBOROUGH,C.CHUNG,L.GORDON,T.LEWIS,A.L.WALKER,L.CUTLER,
JRNL AUTH 4 D.LUGO,D.M.WILSON,J.WITHERINGTON,K.LEE,R.K.PRINJHA
JRNL TITL IDENTIFICATION OF A NOVEL SERIES OF BET FAMILY BROMODOMAIN
JRNL TITL 2 INHIBITORS: BINDING MODE AND PROFILE OF I-BET151
JRNL TITL 3 (GSK1210151A).
JRNL REF BIOORG.MED.CHEM.LETT. V. 22 2968 2012
JRNL REFN ISSN 0960-894X
JRNL PMID 22437115
JRNL DOI 10.1016/J.BMCL.2012.02.041
REMARK 2
REMARK 2 RESOLUTION. 1.82 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.6.0117
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : 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) : 1.82
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 67.73
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.0
REMARK 3 NUMBER OF REFLECTIONS : 36320
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) : 0.170
REMARK 3 R VALUE (WORKING SET) : 0.168
REMARK 3 FREE R VALUE : 0.197
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.000
REMARK 3 FREE R VALUE TEST SET COUNT : 1517
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) : 1.82
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.87
REMARK 3 REFLECTION IN BIN (WORKING SET) : 2485
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 93.98
REMARK 3 BIN R VALUE (WORKING SET) : 0.2100
REMARK 3 BIN FREE R VALUE SET COUNT : 105
REMARK 3 BIN FREE R VALUE : 0.2370
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2755
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 85
REMARK 3 SOLVENT ATOMS : 333
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 31.55
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.91000
REMARK 3 B22 (A**2) : -0.48000
REMARK 3 B33 (A**2) : -0.55000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : -0.81000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.117
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.110
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.070
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 4.360
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.966
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.948
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 3037 ; 0.005 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 2038 ; 0.001 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 4138 ; 0.870 ; 1.941
REMARK 3 BOND ANGLES OTHERS (DEGREES): 4991 ; 0.769 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 353 ; 3.832 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 145 ;35.605 ;25.103
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 548 ;11.428 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 10 ;22.839 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 425 ; 0.049 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 3329 ; 0.003 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 607 ; 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 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER 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 : 3
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 75 A 186
REMARK 3 ORIGIN FOR THE GROUP (A): 16.2839 6.7543 2.0946
REMARK 3 T TENSOR
REMARK 3 T11: 0.0320 T22: 0.0430
REMARK 3 T33: 0.0769 T12: 0.0126
REMARK 3 T13: 0.0209 T23: 0.0053
REMARK 3 L TENSOR
REMARK 3 L11: 0.9135 L22: 0.7779
REMARK 3 L33: 1.5245 L12: -0.5039
REMARK 3 L13: -0.2541 L23: 0.1117
REMARK 3 S TENSOR
REMARK 3 S11: -0.0489 S12: -0.0319 S13: -0.0811
REMARK 3 S21: 0.0399 S22: 0.0047 S23: 0.0866
REMARK 3 S31: -0.0098 S32: -0.1170 S33: 0.0442
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 73 B 182
REMARK 3 ORIGIN FOR THE GROUP (A): 34.7250 8.9388 10.8964
REMARK 3 T TENSOR
REMARK 3 T11: 0.0551 T22: 0.0235
REMARK 3 T33: 0.0725 T12: 0.0146
REMARK 3 T13: -0.0226 T23: -0.0038
REMARK 3 L TENSOR
REMARK 3 L11: 0.4800 L22: 1.2893
REMARK 3 L33: 1.5419 L12: -0.3330
REMARK 3 L13: -0.1206 L23: 0.1452
REMARK 3 S TENSOR
REMARK 3 S11: -0.0220 S12: -0.0465 S13: 0.0024
REMARK 3 S21: 0.1110 S22: 0.0738 S23: -0.0662
REMARK 3 S31: -0.0231 S32: 0.0527 S33: -0.0518
REMARK 3
REMARK 3 TLS GROUP : 3
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : C 76 C 182
REMARK 3 ORIGIN FOR THE GROUP (A): -1.5885 18.8862 23.5680
REMARK 3 T TENSOR
REMARK 3 T11: 0.0176 T22: 0.1231
REMARK 3 T33: 0.0260 T12: 0.0065
REMARK 3 T13: 0.0040 T23: 0.0118
REMARK 3 L TENSOR
REMARK 3 L11: 0.3108 L22: 1.7737
REMARK 3 L33: 2.7301 L12: 0.0185
REMARK 3 L13: 0.7932 L23: -0.3688
REMARK 3 S TENSOR
REMARK 3 S11: -0.0246 S12: 0.0462 S13: 0.0122
REMARK 3 S21: -0.1469 S22: 0.1175 S23: 0.0021
REMARK 3 S31: -0.0410 S32: 0.0908 S33: -0.0929
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 RIDING
REMARK 3 POSITIONS. U VALUES WITH TLS ADDED
REMARK 4
REMARK 4 4AKN COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 26-FEB-12.
REMARK 100 THE DEPOSITION ID IS D_1290051483.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 04-NOV-08
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : ID23-1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9762
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 : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 37838
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.820
REMARK 200 RESOLUTION RANGE LOW (A) : 40.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.5
REMARK 200 DATA REDUNDANCY : 3.700
REMARK 200 R MERGE (I) : 0.07000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 21.9000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.82
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.86
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 3.70
REMARK 200 R MERGE FOR SHELL (I) : 0.38000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.700
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: NONE
REMARK 200
REMARK 200 REMARK: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 39.24
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.02
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 20-26 % PEG3350, 0.2 M (NH4)2SO4, 100
REMARK 280 MM HEPES PH 7.0. AT 20C, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,Y,-Z
REMARK 290 3555 X+1/2,Y+1/2,Z
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 0.00000
REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 3 1.000000 0.000000 0.000000 57.15700
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 27.86500
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 57.15700
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 27.86500
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
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 2650 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 11610 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -28.4 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 3010 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 11400 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -34.6 KCAL/MOL
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 BIOMT1 2 -1.000000 0.000000 0.000000 -5.14521
REMARK 350 BIOMT2 2 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 67.79604
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 GLY A 47
REMARK 465 SER A 48
REMARK 465 SER A 49
REMARK 465 HIS A 50
REMARK 465 HIS A 51
REMARK 465 HIS A 52
REMARK 465 HIS A 53
REMARK 465 HIS A 54
REMARK 465 HIS A 55
REMARK 465 SER A 56
REMARK 465 SER A 57
REMARK 465 GLY A 58
REMARK 465 LEU A 59
REMARK 465 VAL A 60
REMARK 465 PRO A 61
REMARK 465 ARG A 62
REMARK 465 GLY A 63
REMARK 465 SER A 64
REMARK 465 HIS A 65
REMARK 465 MET A 66
REMARK 465 SER A 67
REMARK 465 ASN A 68
REMARK 465 PRO A 69
REMARK 465 LYS A 70
REMARK 465 LYS A 71
REMARK 465 PRO A 72
REMARK 465 GLY A 73
REMARK 465 ARG A 74
REMARK 465 LEU A 187
REMARK 465 VAL A 188
REMARK 465 VAL A 189
REMARK 465 THR A 190
REMARK 465 ILE A 191
REMARK 465 PRO A 192
REMARK 465 ASN A 193
REMARK 465 SER A 194
REMARK 465 HIS A 195
REMARK 465 LYS A 196
REMARK 465 LYS A 197
REMARK 465 GLY A 198
REMARK 465 ALA A 199
REMARK 465 GLY B 47
REMARK 465 SER B 48
REMARK 465 SER B 49
REMARK 465 HIS B 50
REMARK 465 HIS B 51
REMARK 465 HIS B 52
REMARK 465 HIS B 53
REMARK 465 HIS B 54
REMARK 465 HIS B 55
REMARK 465 SER B 56
REMARK 465 SER B 57
REMARK 465 GLY B 58
REMARK 465 LEU B 59
REMARK 465 VAL B 60
REMARK 465 PRO B 61
REMARK 465 ARG B 62
REMARK 465 GLY B 63
REMARK 465 SER B 64
REMARK 465 HIS B 65
REMARK 465 MET B 66
REMARK 465 SER B 67
REMARK 465 ASN B 68
REMARK 465 PRO B 69
REMARK 465 LYS B 70
REMARK 465 LYS B 71
REMARK 465 PRO B 72
REMARK 465 GLU B 184
REMARK 465 GLN B 185
REMARK 465 GLU B 186
REMARK 465 LEU B 187
REMARK 465 VAL B 188
REMARK 465 VAL B 189
REMARK 465 THR B 190
REMARK 465 ILE B 191
REMARK 465 PRO B 192
REMARK 465 ASN B 193
REMARK 465 SER B 194
REMARK 465 HIS B 195
REMARK 465 LYS B 196
REMARK 465 LYS B 197
REMARK 465 GLY B 198
REMARK 465 ALA B 199
REMARK 465 GLY C 47
REMARK 465 SER C 48
REMARK 465 SER C 49
REMARK 465 HIS C 50
REMARK 465 HIS C 51
REMARK 465 HIS C 52
REMARK 465 HIS C 53
REMARK 465 HIS C 54
REMARK 465 HIS C 55
REMARK 465 SER C 56
REMARK 465 SER C 57
REMARK 465 GLY C 58
REMARK 465 LEU C 59
REMARK 465 VAL C 60
REMARK 465 PRO C 61
REMARK 465 ARG C 62
REMARK 465 GLY C 63
REMARK 465 SER C 64
REMARK 465 HIS C 65
REMARK 465 MET C 66
REMARK 465 SER C 67
REMARK 465 ASN C 68
REMARK 465 PRO C 69
REMARK 465 LYS C 70
REMARK 465 LYS C 71
REMARK 465 PRO C 72
REMARK 465 GLY C 73
REMARK 465 ARG C 74
REMARK 465 VAL C 75
REMARK 465 GLU C 183
REMARK 465 GLU C 184
REMARK 465 GLN C 185
REMARK 465 GLU C 186
REMARK 465 LEU C 187
REMARK 465 VAL C 188
REMARK 465 VAL C 189
REMARK 465 THR C 190
REMARK 465 ILE C 191
REMARK 465 PRO C 192
REMARK 465 ASN C 193
REMARK 465 SER C 194
REMARK 465 HIS C 195
REMARK 465 LYS C 196
REMARK 465 LYS C 197
REMARK 465 GLY C 198
REMARK 465 ALA C 199
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 C 182 CG CD OE1 NE2
REMARK 480
REMARK 480 ZERO OCCUPANCY ATOM
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 480 M RES C SSEQI ATOMS
REMARK 480 MET A 123 CE
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 MET A 123 CG - SD - CE ANGL. DEV. = -11.1 DEGREES
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH C2080 DISTANCE = 6.66 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 1187
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE S5B A 1188
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 1189
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 1190
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE S5B B 1184
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DMS C 1183
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 C 1184
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1X0J RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE ANALYSIS OF THE N-TERMINAL BROMODOMAIN OFHUMAN
REMARK 900 BRD2
REMARK 900 RELATED ID: 2YDW RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE FIRST BROMODOMAIN OF HUMAN BRD2 WITH THE
REMARK 900 INHIBITOR GW841819X
REMARK 900 RELATED ID: 2YEK RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE FIRST BROMODOMAIN OF HUMAN BRD2 WITH THE
REMARK 900 INHIBITOR GSK525762 (IBET)
REMARK 900 RELATED ID: 4A9E RELATED DB: PDB
REMARK 900 N-TERMINAL BROMODOMAIN OF HUMAN BRD2 WITH 3-METHYL-1 ,2,3,4-
REMARK 900 TETRAHYDROQUINAZOLIN-2-ONE
REMARK 900 RELATED ID: 4A9F RELATED DB: PDB
REMARK 900 N-TERMINAL BROMODOMAIN OF HUMAN BRD2 WITH 1- METHYLPYRROLIDIN-2-ONE
REMARK 900 RELATED ID: 4A9H RELATED DB: PDB
REMARK 900 N-TERMINAL BROMODOMAIN OF HUMAN BRD2 WITH 1-(2- METHYL-1,2,3,4-
REMARK 900 TETRAHYDROQUINOLIN-1-YL)ETHAN-1-ONE
REMARK 900 RELATED ID: 4A9I RELATED DB: PDB
REMARK 900 N-TERMINAL BROMODOMAIN OF HUMAN BRD2 WITH 3-METHYL-1 ,2,3,4-
REMARK 900 TETRAHYDROQUINAZOLIN-2-ONE
REMARK 900 RELATED ID: 4A9J RELATED DB: PDB
REMARK 900 N-TERMINAL BROMODOMAIN OF HUMAN BRD2 WITH N-(4- HYDROXYPHENYL)
REMARK 900 ACETAMIDE
REMARK 900 RELATED ID: 4A9M RELATED DB: PDB
REMARK 900 N-TERMINAL BROMODOMAIN OF HUMAN BRD2 WITH N- CYCLOPENTYL-5-(3,5-
REMARK 900 DIMETHYL-1,2-OXAZOL-4-YL)-2- METHYLBENZENE-1-SULFONAMIDE
REMARK 900 RELATED ID: 4A9N RELATED DB: PDB
REMARK 900 N-TERMINAL BROMODOMAIN OF HUMAN BRD2 WITH N- CYCLOPROPYL-5-(3,5-
REMARK 900 DIMETHYL-1,2-OXAZOL-4-YL)-2- METHYLBENZENE-1-SULFONAMIDE
REMARK 900 RELATED ID: 4A9O RELATED DB: PDB
REMARK 900 N-TERMINAL BROMODOMAIN OF HUMAN BRD2 WITH 5 ETHYL-3 -METHYL-4-
REMARK 900 PHENYL-1,2-OXAZOLE
REMARK 900 RELATED ID: 4A9P RELATED DB: PDB
REMARK 900 N-TERMINAL BROMODOMAIN OF HUMAN BRD2 WITH 3,5 DIMETHYL-4-PHENYL-1,2-
REMARK 900 OXAZOLE
REMARK 900 RELATED ID: 4ALG RELATED DB: PDB
REMARK 900 N-TERMINAL BROMODOMAIN OF HUMAN BRD2 WITH IBET-151
DBREF 4AKN A 67 199 UNP P25440 BRD2_HUMAN 67 200
DBREF 4AKN B 67 199 UNP P25440 BRD2_HUMAN 67 200
DBREF 4AKN C 67 199 UNP P25440 BRD2_HUMAN 67 200
SEQADV 4AKN GLY A 47 UNP P25440 EXPRESSION TAG
SEQADV 4AKN SER A 48 UNP P25440 EXPRESSION TAG
SEQADV 4AKN SER A 49 UNP P25440 EXPRESSION TAG
SEQADV 4AKN HIS A 50 UNP P25440 EXPRESSION TAG
SEQADV 4AKN HIS A 51 UNP P25440 EXPRESSION TAG
SEQADV 4AKN HIS A 52 UNP P25440 EXPRESSION TAG
SEQADV 4AKN HIS A 53 UNP P25440 EXPRESSION TAG
SEQADV 4AKN HIS A 54 UNP P25440 EXPRESSION TAG
SEQADV 4AKN HIS A 55 UNP P25440 EXPRESSION TAG
SEQADV 4AKN SER A 56 UNP P25440 EXPRESSION TAG
SEQADV 4AKN SER A 57 UNP P25440 EXPRESSION TAG
SEQADV 4AKN GLY A 58 UNP P25440 EXPRESSION TAG
SEQADV 4AKN LEU A 59 UNP P25440 EXPRESSION TAG
SEQADV 4AKN VAL A 60 UNP P25440 EXPRESSION TAG
SEQADV 4AKN PRO A 61 UNP P25440 EXPRESSION TAG
SEQADV 4AKN ARG A 62 UNP P25440 EXPRESSION TAG
SEQADV 4AKN GLY A 63 UNP P25440 EXPRESSION TAG
SEQADV 4AKN SER A 64 UNP P25440 EXPRESSION TAG
SEQADV 4AKN HIS A 65 UNP P25440 EXPRESSION TAG
SEQADV 4AKN MET A 66 UNP P25440 EXPRESSION TAG
SEQADV 4AKN A UNP P25440 LYS 193 DELETION
SEQADV 4AKN GLY B 47 UNP P25440 EXPRESSION TAG
SEQADV 4AKN SER B 48 UNP P25440 EXPRESSION TAG
SEQADV 4AKN SER B 49 UNP P25440 EXPRESSION TAG
SEQADV 4AKN HIS B 50 UNP P25440 EXPRESSION TAG
SEQADV 4AKN HIS B 51 UNP P25440 EXPRESSION TAG
SEQADV 4AKN HIS B 52 UNP P25440 EXPRESSION TAG
SEQADV 4AKN HIS B 53 UNP P25440 EXPRESSION TAG
SEQADV 4AKN HIS B 54 UNP P25440 EXPRESSION TAG
SEQADV 4AKN HIS B 55 UNP P25440 EXPRESSION TAG
SEQADV 4AKN SER B 56 UNP P25440 EXPRESSION TAG
SEQADV 4AKN SER B 57 UNP P25440 EXPRESSION TAG
SEQADV 4AKN GLY B 58 UNP P25440 EXPRESSION TAG
SEQADV 4AKN LEU B 59 UNP P25440 EXPRESSION TAG
SEQADV 4AKN VAL B 60 UNP P25440 EXPRESSION TAG
SEQADV 4AKN PRO B 61 UNP P25440 EXPRESSION TAG
SEQADV 4AKN ARG B 62 UNP P25440 EXPRESSION TAG
SEQADV 4AKN GLY B 63 UNP P25440 EXPRESSION TAG
SEQADV 4AKN SER B 64 UNP P25440 EXPRESSION TAG
SEQADV 4AKN HIS B 65 UNP P25440 EXPRESSION TAG
SEQADV 4AKN MET B 66 UNP P25440 EXPRESSION TAG
SEQADV 4AKN B UNP P25440 LYS 193 DELETION
SEQADV 4AKN GLY C 47 UNP P25440 EXPRESSION TAG
SEQADV 4AKN SER C 48 UNP P25440 EXPRESSION TAG
SEQADV 4AKN SER C 49 UNP P25440 EXPRESSION TAG
SEQADV 4AKN HIS C 50 UNP P25440 EXPRESSION TAG
SEQADV 4AKN HIS C 51 UNP P25440 EXPRESSION TAG
SEQADV 4AKN HIS C 52 UNP P25440 EXPRESSION TAG
SEQADV 4AKN HIS C 53 UNP P25440 EXPRESSION TAG
SEQADV 4AKN HIS C 54 UNP P25440 EXPRESSION TAG
SEQADV 4AKN HIS C 55 UNP P25440 EXPRESSION TAG
SEQADV 4AKN SER C 56 UNP P25440 EXPRESSION TAG
SEQADV 4AKN SER C 57 UNP P25440 EXPRESSION TAG
SEQADV 4AKN GLY C 58 UNP P25440 EXPRESSION TAG
SEQADV 4AKN LEU C 59 UNP P25440 EXPRESSION TAG
SEQADV 4AKN VAL C 60 UNP P25440 EXPRESSION TAG
SEQADV 4AKN PRO C 61 UNP P25440 EXPRESSION TAG
SEQADV 4AKN ARG C 62 UNP P25440 EXPRESSION TAG
SEQADV 4AKN GLY C 63 UNP P25440 EXPRESSION TAG
SEQADV 4AKN SER C 64 UNP P25440 EXPRESSION TAG
SEQADV 4AKN HIS C 65 UNP P25440 EXPRESSION TAG
SEQADV 4AKN MET C 66 UNP P25440 EXPRESSION TAG
SEQADV 4AKN C UNP P25440 LYS 193 DELETION
SEQRES 1 A 153 GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY LEU
SEQRES 2 A 153 VAL PRO ARG GLY SER HIS MET SER ASN PRO LYS LYS PRO
SEQRES 3 A 153 GLY ARG VAL THR ASN GLN LEU GLN TYR LEU HIS LYS VAL
SEQRES 4 A 153 VAL MET LYS ALA LEU TRP LYS HIS GLN PHE ALA TRP PRO
SEQRES 5 A 153 PHE ARG GLN PRO VAL ASP ALA VAL LYS LEU GLY LEU PRO
SEQRES 6 A 153 ASP TYR HIS LYS ILE ILE LYS GLN PRO MET ASP MET GLY
SEQRES 7 A 153 THR ILE LYS ARG ARG LEU GLU ASN ASN TYR TYR TRP ALA
SEQRES 8 A 153 ALA SER GLU CYS MET GLN ASP PHE ASN THR MET PHE THR
SEQRES 9 A 153 ASN CYS TYR ILE TYR ASN LYS PRO THR ASP ASP ILE VAL
SEQRES 10 A 153 LEU MET ALA GLN THR LEU GLU LYS ILE PHE LEU GLN LYS
SEQRES 11 A 153 VAL ALA SER MET PRO GLN GLU GLU GLN GLU LEU VAL VAL
SEQRES 12 A 153 THR ILE PRO ASN SER HIS LYS LYS GLY ALA
SEQRES 1 B 153 GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY LEU
SEQRES 2 B 153 VAL PRO ARG GLY SER HIS MET SER ASN PRO LYS LYS PRO
SEQRES 3 B 153 GLY ARG VAL THR ASN GLN LEU GLN TYR LEU HIS LYS VAL
SEQRES 4 B 153 VAL MET LYS ALA LEU TRP LYS HIS GLN PHE ALA TRP PRO
SEQRES 5 B 153 PHE ARG GLN PRO VAL ASP ALA VAL LYS LEU GLY LEU PRO
SEQRES 6 B 153 ASP TYR HIS LYS ILE ILE LYS GLN PRO MET ASP MET GLY
SEQRES 7 B 153 THR ILE LYS ARG ARG LEU GLU ASN ASN TYR TYR TRP ALA
SEQRES 8 B 153 ALA SER GLU CYS MET GLN ASP PHE ASN THR MET PHE THR
SEQRES 9 B 153 ASN CYS TYR ILE TYR ASN LYS PRO THR ASP ASP ILE VAL
SEQRES 10 B 153 LEU MET ALA GLN THR LEU GLU LYS ILE PHE LEU GLN LYS
SEQRES 11 B 153 VAL ALA SER MET PRO GLN GLU GLU GLN GLU LEU VAL VAL
SEQRES 12 B 153 THR ILE PRO ASN SER HIS LYS LYS GLY ALA
SEQRES 1 C 153 GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY LEU
SEQRES 2 C 153 VAL PRO ARG GLY SER HIS MET SER ASN PRO LYS LYS PRO
SEQRES 3 C 153 GLY ARG VAL THR ASN GLN LEU GLN TYR LEU HIS LYS VAL
SEQRES 4 C 153 VAL MET LYS ALA LEU TRP LYS HIS GLN PHE ALA TRP PRO
SEQRES 5 C 153 PHE ARG GLN PRO VAL ASP ALA VAL LYS LEU GLY LEU PRO
SEQRES 6 C 153 ASP TYR HIS LYS ILE ILE LYS GLN PRO MET ASP MET GLY
SEQRES 7 C 153 THR ILE LYS ARG ARG LEU GLU ASN ASN TYR TYR TRP ALA
SEQRES 8 C 153 ALA SER GLU CYS MET GLN ASP PHE ASN THR MET PHE THR
SEQRES 9 C 153 ASN CYS TYR ILE TYR ASN LYS PRO THR ASP ASP ILE VAL
SEQRES 10 C 153 LEU MET ALA GLN THR LEU GLU LYS ILE PHE LEU GLN LYS
SEQRES 11 C 153 VAL ALA SER MET PRO GLN GLU GLU GLN GLU LEU VAL VAL
SEQRES 12 C 153 THR ILE PRO ASN SER HIS LYS LYS GLY ALA
HET EDO A1187 4
HET S5B A1188 31
HET SO4 A1189 5
HET SO4 A1190 5
HET S5B B1184 31
HET DMS C1183 4
HET SO4 C1184 5
HETNAM EDO 1,2-ETHANEDIOL
HETNAM S5B 4-[(2-TERT-BUTYLPHENYL)AMINO]-7-(3,5-DIMETHYL-1,2-
HETNAM 2 S5B OXAZOL-4-YL)QUINOLINE-3-CARBOXYLIC ACID
HETNAM SO4 SULFATE ION
HETNAM DMS DIMETHYL SULFOXIDE
HETSYN EDO ETHYLENE GLYCOL
FORMUL 4 EDO C2 H6 O2
FORMUL 5 S5B 2(C25 H25 N3 O3)
FORMUL 6 SO4 3(O4 S 2-)
FORMUL 9 DMS C2 H6 O S
FORMUL 11 HOH *333(H2 O)
HELIX 1 1 THR A 76 VAL A 85 1 10
HELIX 2 2 VAL A 85 LYS A 92 1 8
HELIX 3 3 ALA A 96 ARG A 100 5 5
HELIX 4 4 ASP A 104 GLY A 109 1 6
HELIX 5 5 ASP A 112 ILE A 117 1 6
HELIX 6 6 ASP A 122 ASN A 132 1 11
HELIX 7 7 ALA A 137 ASN A 156 1 20
HELIX 8 8 ASP A 160 ALA A 178 1 19
HELIX 9 9 THR B 76 VAL B 85 1 10
HELIX 10 10 VAL B 85 LYS B 92 1 8
HELIX 11 11 ALA B 96 ARG B 100 5 5
HELIX 12 12 ASP B 104 GLY B 109 1 6
HELIX 13 13 ASP B 112 ILE B 117 1 6
HELIX 14 14 ASP B 122 ASN B 132 1 11
HELIX 15 15 ALA B 137 ASN B 156 1 20
HELIX 16 16 ASP B 160 ALA B 178 1 19
HELIX 17 17 THR C 76 VAL C 85 1 10
HELIX 18 18 VAL C 85 LYS C 92 1 8
HELIX 19 19 ALA C 96 ARG C 100 5 5
HELIX 20 20 ASP C 112 ILE C 117 1 6
HELIX 21 21 ASP C 122 ASN C 132 1 11
HELIX 22 22 ALA C 137 ASN C 156 1 20
HELIX 23 23 ASP C 160 SER C 179 1 20
SITE 1 AC1 9 ASN A 146 THR A 150 TYR A 153 GLU A 170
SITE 2 AC1 9 HOH A2140 ASN B 146 THR B 150 TYR B 153
SITE 3 AC1 9 GLU B 170
SITE 1 AC2 10 TRP A 97 PRO A 98 PHE A 99 LEU A 108
SITE 2 AC2 10 LEU A 110 ASN A 156 HOH A2029 HOH A2034
SITE 3 AC2 10 HOH A2063 GLN B 94
SITE 1 AC3 4 ARG A 100 HOH A2020 HOH A2022 HOH A2141
SITE 1 AC4 4 THR A 125 ARG A 128 ARG A 129 HOH A2144
SITE 1 AC5 8 GLN A 94 TRP B 97 PHE B 99 LYS B 107
SITE 2 AC5 8 LEU B 108 ASN B 156 HOH B2022 HOH B2040
SITE 1 AC6 5 VAL C 103 ASN C 156 ILE C 162 HOH C2024
SITE 2 AC6 5 HOH C2067
SITE 1 AC7 8 ARG B 100 HOH B2014 HOH B2015 ARG C 128
SITE 2 AC7 8 ASN C 132 TYR C 134 HOH C2047 HOH C2079
CRYST1 114.314 55.730 67.991 90.00 94.34 90.00 C 1 2 1 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 0.008748 0.000000 0.000664 0.00000
SCALE2 0.000000 0.017944 0.000000 0.00000
SCALE3 0.000000 0.000000 0.014750 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
