HEADER TRANSCRIPTION 15-JAN-16 5HLS
TITLE CRYSTAL STRUCTURE OF THE FIRST BROMODOMAIN OF HUMAN BRD4 BOUND TO CPI-
TITLE 2 0610
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: BROMODOMAIN-CONTAINING PROTEIN 4;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: PROTEIN HUNK1;
COMPND 5 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: BRD4, HUNK1;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS BROMODOMAIN, TRANSCRIPTION
EXPDTA X-RAY DIFFRACTION
AUTHOR H.JAYARAM,F.POY,J.W.SETSER,S.F.BELLON
REVDAT 3 27-SEP-23 5HLS 1 JRNL REMARK
REVDAT 2 09-MAR-16 5HLS 1 JRNL
REVDAT 1 10-FEB-16 5HLS 0
JRNL AUTH B.K.ALBRECHT,V.S.GEHLING,M.C.HEWITT,R.G.VASWANI,A.COTE,
JRNL AUTH 2 Y.LEBLANC,C.G.NASVESCHUK,S.BELLON,L.BERGERON,R.CAMPBELL,
JRNL AUTH 3 N.CANTONE,M.R.COOPER,R.T.CUMMINGS,H.JAYARAM,S.JOSHI,
JRNL AUTH 4 J.A.MERTZ,A.NEISS,E.NORMANT,M.O'MEARA,E.PARDO,F.POY,P.SANDY,
JRNL AUTH 5 J.SUPKO,R.J.SIMS,J.C.HARMANGE,A.M.TAYLOR,J.E.AUDIA
JRNL TITL IDENTIFICATION OF A BENZOISOXAZOLOAZEPINE INHIBITOR
JRNL TITL 2 (CPI-0610) OF THE BROMODOMAIN AND EXTRA-TERMINAL (BET)
JRNL TITL 3 FAMILY AS A CANDIDATE FOR HUMAN CLINICAL TRIALS.
JRNL REF J.MED.CHEM. V. 59 1330 2016
JRNL REFN ISSN 0022-2623
JRNL PMID 26815195
JRNL DOI 10.1021/ACS.JMEDCHEM.5B01882
REMARK 2
REMARK 2 RESOLUTION. 2.18 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0069
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.18
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 40.62
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 90.1
REMARK 3 NUMBER OF REFLECTIONS : 5826
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) : 0.192
REMARK 3 R VALUE (WORKING SET) : 0.186
REMARK 3 FREE R VALUE : 0.277
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 6.900
REMARK 3 FREE R VALUE TEST SET COUNT : 435
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) : 2.18
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.24
REMARK 3 REFLECTION IN BIN (WORKING SET) : 330
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 70.02
REMARK 3 BIN R VALUE (WORKING SET) : 0.2680
REMARK 3 BIN FREE R VALUE SET COUNT : 25
REMARK 3 BIN FREE R VALUE : 0.3760
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 1061
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 26
REMARK 3 SOLVENT ATOMS : 153
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 23.79
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 3.78000
REMARK 3 B22 (A**2) : -2.66000
REMARK 3 B33 (A**2) : -1.12000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.521
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.296
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.204
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 13.940
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.940
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.865
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 1125 ; 0.010 ; 0.020
REMARK 3 BOND LENGTHS OTHERS (A): 1043 ; 0.000 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 1537 ; 1.416 ; 1.999
REMARK 3 BOND ANGLES OTHERS (DEGREES): 2416 ; 0.693 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 128 ; 6.306 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 54 ;35.198 ;25.926
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 196 ;17.774 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 3 ;21.354 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 162 ; 0.084 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 1299 ; 0.014 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 244 ; 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): 509 ; 2.024 ; 1.706
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 508 ; 2.020 ; 1.702
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 635 ; 2.811 ; 2.550
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): 636 ; 2.811 ; 2.554
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 616 ; 2.334 ; 1.843
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): 584 ; 2.307 ; 1.859
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): 858 ; 3.455 ; 2.711
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): 2617 ; 5.164 ;15.538
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): 2505 ; 5.011 ;15.310
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): 10.7307 3.4475 8.1170
REMARK 3 T TENSOR
REMARK 3 T11: 0.0049 T22: 0.1197
REMARK 3 T33: 0.0044 T12: 0.0029
REMARK 3 T13: -0.0038 T23: 0.0055
REMARK 3 L TENSOR
REMARK 3 L11: 0.3515 L22: 1.3889
REMARK 3 L33: 0.3496 L12: 0.0979
REMARK 3 L13: 0.2522 L23: 0.2552
REMARK 3 S TENSOR
REMARK 3 S11: 0.0007 S12: -0.0200 S13: -0.0045
REMARK 3 S21: -0.0584 S22: -0.0126 S23: 0.0705
REMARK 3 S31: -0.0259 S32: -0.0358 S33: 0.0120
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : NULL
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
REMARK 4
REMARK 4 5HLS COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 15-JAN-16.
REMARK 100 THE DEPOSITION ID IS D_1000217278.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 15-NOV-13
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.8
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : ROTATING ANODE
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : RIGAKU
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.54
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : RIGAKU RAXIS IV
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 6289
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.180
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 (%) : 90.0
REMARK 200 DATA REDUNDANCY : 4.300
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.10800
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 16.4000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.18
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.26
REMARK 200 COMPLETENESS FOR SHELL (%) : 70.2
REMARK 200 DATA REDUNDANCY IN SHELL : 3.20
REMARK 200 R MERGE FOR SHELL (I) : 0.25000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 8.500
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: 2OSS
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 40.55
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.07
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 3.4-3.8 M SODIUM FORMATE, 0.1 M TRIS
REMARK 280 PH 7.8, AND 10% GLYCEROL, VAPOR DIFFUSION, SITTING DROP,
REMARK 280 TEMPERATURE 277K
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 16.89400
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 38.88750
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 23.81700
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 38.88750
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 16.89400
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 23.81700
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 TOTAL BURIED SURFACE AREA: 0 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 7460 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 0.0 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 GLY A 41
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 O HOH A 357 O HOH A 401 1.81
REMARK 500 O HOH A 379 O HOH A 411 1.87
REMARK 500 O HOH A 384 O HOH A 426 1.94
REMARK 500 O HOH A 353 O HOH A 417 2.11
REMARK 500 OE1 GLU A 163 O HOH A 301 2.17
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 ASN A 52 105.50 -167.70
REMARK 500 LEU A 94 68.08 -115.52
REMARK 500 THR A 166 122.12 -33.79
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 62G A 201
DBREF 5HLS A 42 168 UNP O60885 BRD4_HUMAN 42 168
SEQADV 5HLS GLY A 41 UNP O60885 EXPRESSION TAG
SEQRES 1 A 128 GLY SER THR ASN PRO PRO PRO PRO GLU THR SER ASN PRO
SEQRES 2 A 128 ASN LYS PRO LYS ARG GLN THR ASN GLN LEU GLN TYR LEU
SEQRES 3 A 128 LEU ARG VAL VAL LEU LYS THR LEU TRP LYS HIS GLN PHE
SEQRES 4 A 128 ALA TRP PRO PHE GLN GLN PRO VAL ASP ALA VAL LYS LEU
SEQRES 5 A 128 ASN LEU PRO ASP TYR TYR LYS ILE ILE LYS THR PRO MET
SEQRES 6 A 128 ASP MET GLY THR ILE LYS LYS ARG LEU GLU ASN ASN TYR
SEQRES 7 A 128 TYR TRP ASN ALA GLN GLU CYS ILE GLN ASP PHE ASN THR
SEQRES 8 A 128 MET PHE THR ASN CYS TYR ILE TYR ASN LYS PRO GLY ASP
SEQRES 9 A 128 ASP ILE VAL LEU MET ALA GLU ALA LEU GLU LYS LEU PHE
SEQRES 10 A 128 LEU GLN LYS ILE ASN GLU LEU PRO THR GLU GLU
HET 62G A 201 26
HETNAM 62G CPI-0610
HETSYN 62G 2-[(4S)-6-(4-CHLOROPHENYL)-1-METHYL-4H-[1,2]OXAZOLO[5,
HETSYN 2 62G 4-D][2]BENZAZEPIN-4-YL]ACETAMIDE
FORMUL 2 62G C20 H16 CL N3 O2
FORMUL 3 HOH *153(H2 O)
HELIX 1 AA1 THR A 60 VAL A 69 1 10
HELIX 2 AA2 VAL A 69 HIS A 77 1 9
HELIX 3 AA3 ALA A 80 GLN A 84 5 5
HELIX 4 AA4 ASP A 96 ILE A 101 1 6
HELIX 5 AA5 ASP A 106 ASN A 116 1 11
HELIX 6 AA6 ASN A 121 ASN A 140 1 20
HELIX 7 AA7 ASP A 144 ASN A 162 1 19
SITE 1 AC1 11 PRO A 53 TRP A 81 PRO A 82 LEU A 92
SITE 2 AC1 11 LEU A 94 LYS A 99 TYR A 139 ASN A 140
SITE 3 AC1 11 MET A 149 HOH A 330 HOH A 337
CRYST1 33.788 47.634 77.775 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 0.029596 0.000000 0.000000 0.00000
SCALE2 0.000000 0.020993 0.000000 0.00000
SCALE3 0.000000 0.000000 0.012858 0.00000
(ATOM LINES ARE NOT SHOWN.)
END