HEADER SIGNALING PROTEIN 09-FEB-12 4DON
TITLE BRD4 BROMODOMAIN 1 COMPLEX WITH A FRAGMENT 3,4-DIHYDRO-3-METHYL-2(1H)-
TITLE 2 QUINAZOLINON
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: BROMODOMAIN-CONTAINING PROTEIN 4;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: BROMO 1 DOMAIN, UNP RESIDUES 44-166;
COMPND 5 SYNONYM: 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 GENE: BRD4, HUNK1;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)CODON PLUS;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET28A
KEYWDS BRD4, BROMODOMAIN, FOUR ALPHA HELICES, SIGNALING PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR B.XIONG,D.Y.CAO,W.Y.CHEN,T.T.CHEN,Y.C.XU,J.K.SHEN
REVDAT 2 25-DEC-19 4DON 1 REMARK SEQADV
REVDAT 1 13-FEB-13 4DON 0
JRNL AUTH B.XIONG,D.Y.CAO,W.Y.CHEN,T.T.CHEN,Y.C.XU,J.K.SHEN
JRNL TITL BRD4 BROMODOMAIN 1 COMPLEX WITH A FRAGMENT
JRNL TITL 2 3,4-DIHYDRO-3-METHYL-2(1H)-QUINAZOLINON
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 1.52 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.7_650
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) : 1.52
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 30.31
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.990
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.4
REMARK 3 NUMBER OF REFLECTIONS : 19328
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.202
REMARK 3 R VALUE (WORKING SET) : 0.201
REMARK 3 FREE R VALUE : 0.218
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 3.000
REMARK 3 FREE R VALUE TEST SET COUNT : 580
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 30.3150 - 2.4125 0.99 4833 149 0.1839 0.1886
REMARK 3 2 2.4125 - 1.9149 1.00 4663 144 0.1853 0.2137
REMARK 3 3 1.9149 - 1.6729 1.00 4642 144 0.2281 0.2724
REMARK 3 4 1.6729 - 1.5200 1.00 4610 143 0.2986 0.3172
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.00
REMARK 3 SHRINKAGE RADIUS : 0.72
REMARK 3 K_SOL : 0.40
REMARK 3 B_SOL : 54.34
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.190
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 26.820
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 21.41
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 25.11
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 17.67760
REMARK 3 B22 (A**2) : -10.42250
REMARK 3 B33 (A**2) : -7.25510
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 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 : 0.005 1091
REMARK 3 ANGLE : 0.952 1489
REMARK 3 CHIRALITY : 0.064 158
REMARK 3 PLANARITY : 0.005 191
REMARK 3 DIHEDRAL : 11.665 420
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 7
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN 'A' AND (RESSEQ 43:60)
REMARK 3 ORIGIN FOR THE GROUP (A): 11.0578 0.9450 21.3228
REMARK 3 T TENSOR
REMARK 3 T11: 0.1769 T22: 0.1244
REMARK 3 T33: 0.1280 T12: -0.0025
REMARK 3 T13: -0.0210 T23: 0.0026
REMARK 3 L TENSOR
REMARK 3 L11: 0.1615 L22: 0.2812
REMARK 3 L33: 0.6393 L12: 0.2126
REMARK 3 L13: 0.2462 L23: 0.3266
REMARK 3 S TENSOR
REMARK 3 S11: 0.0260 S12: -0.0347 S13: -0.0273
REMARK 3 S21: 0.1697 S22: -0.0803 S23: -0.0749
REMARK 3 S31: 0.1290 S32: -0.0676 S33: 0.0076
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN 'A' AND (RESSEQ 61:76)
REMARK 3 ORIGIN FOR THE GROUP (A): 2.1904 12.1613 10.2796
REMARK 3 T TENSOR
REMARK 3 T11: 0.1044 T22: 0.0806
REMARK 3 T33: 0.1559 T12: 0.0744
REMARK 3 T13: -0.0924 T23: -0.0048
REMARK 3 L TENSOR
REMARK 3 L11: 0.4751 L22: 1.0808
REMARK 3 L33: 0.0231 L12: 0.3933
REMARK 3 L13: 0.0942 L23: 0.0221
REMARK 3 S TENSOR
REMARK 3 S11: -0.0844 S12: -0.1127 S13: 0.0250
REMARK 3 S21: -0.1491 S22: 0.0578 S23: 0.2233
REMARK 3 S31: -0.0711 S32: -0.0914 S33: 0.0473
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN 'A' AND (RESSEQ 77:106)
REMARK 3 ORIGIN FOR THE GROUP (A): 10.8327 -6.3361 4.3397
REMARK 3 T TENSOR
REMARK 3 T11: 0.0504 T22: -0.0002
REMARK 3 T33: 0.0651 T12: 0.0552
REMARK 3 T13: -0.1088 T23: 0.0488
REMARK 3 L TENSOR
REMARK 3 L11: 1.1475 L22: 0.5187
REMARK 3 L33: 0.3361 L12: -0.7633
REMARK 3 L13: 0.5714 L23: -0.4075
REMARK 3 S TENSOR
REMARK 3 S11: 0.1495 S12: -0.1563 S13: -0.0905
REMARK 3 S21: -0.2638 S22: 0.0593 S23: 0.0512
REMARK 3 S31: 0.1280 S32: 0.0226 S33: -0.1030
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN 'A' AND (RESSEQ 107:115)
REMARK 3 ORIGIN FOR THE GROUP (A): 5.1729 3.3414 14.5429
REMARK 3 T TENSOR
REMARK 3 T11: 0.0067 T22: 0.1098
REMARK 3 T33: 0.0910 T12: -0.0054
REMARK 3 T13: -0.0062 T23: 0.0317
REMARK 3 L TENSOR
REMARK 3 L11: 0.6146 L22: 0.4547
REMARK 3 L33: 0.3915 L12: 0.5144
REMARK 3 L13: 0.2255 L23: 0.1025
REMARK 3 S TENSOR
REMARK 3 S11: 0.0405 S12: -0.1975 S13: 0.1821
REMARK 3 S21: 0.0244 S22: -0.0187 S23: 0.1536
REMARK 3 S31: 0.0137 S32: -0.2464 S33: -0.0225
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: CHAIN 'A' AND (RESSEQ 116:144)
REMARK 3 ORIGIN FOR THE GROUP (A): 14.1665 4.5506 8.6043
REMARK 3 T TENSOR
REMARK 3 T11: 0.1359 T22: 0.0968
REMARK 3 T33: 0.0948 T12: -0.0150
REMARK 3 T13: 0.0001 T23: 0.0023
REMARK 3 L TENSOR
REMARK 3 L11: 0.2697 L22: 0.5037
REMARK 3 L33: 0.4544 L12: 0.0485
REMARK 3 L13: 0.1084 L23: 0.2058
REMARK 3 S TENSOR
REMARK 3 S11: -0.0505 S12: 0.0297 S13: 0.0413
REMARK 3 S21: -0.0509 S22: 0.0374 S23: -0.0738
REMARK 3 S31: 0.0260 S32: -0.0923 S33: 0.0023
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: CHAIN 'A' AND (RESSEQ 145:161)
REMARK 3 ORIGIN FOR THE GROUP (A): 9.8506 7.7950 -1.8403
REMARK 3 T TENSOR
REMARK 3 T11: 0.2495 T22: 0.0854
REMARK 3 T33: 0.0753 T12: -0.0433
REMARK 3 T13: -0.0384 T23: 0.0124
REMARK 3 L TENSOR
REMARK 3 L11: 0.1473 L22: 0.3742
REMARK 3 L33: 0.0300 L12: 0.1944
REMARK 3 L13: 0.0667 L23: 0.0725
REMARK 3 S TENSOR
REMARK 3 S11: -0.1010 S12: 0.0932 S13: -0.0126
REMARK 3 S21: -0.3127 S22: 0.1251 S23: 0.0268
REMARK 3 S31: 0.0421 S32: -0.0070 S33: -0.0091
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: CHAIN 'A' AND (RESSEQ 162:166)
REMARK 3 ORIGIN FOR THE GROUP (A): 8.3069 22.4586 9.1225
REMARK 3 T TENSOR
REMARK 3 T11: 0.2845 T22: 0.1055
REMARK 3 T33: 0.2336 T12: 0.0687
REMARK 3 T13: -0.0188 T23: -0.0184
REMARK 3 L TENSOR
REMARK 3 L11: 0.8644 L22: 0.0599
REMARK 3 L33: 0.7289 L12: 0.1149
REMARK 3 L13: -0.1976 L23: -0.2001
REMARK 3 S TENSOR
REMARK 3 S11: 0.0548 S12: -0.0141 S13: 0.3908
REMARK 3 S21: -0.2239 S22: 0.0367 S23: -0.2024
REMARK 3 S31: -0.2834 S32: -0.0571 S33: -0.0925
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 4DON COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 22-FEB-12.
REMARK 100 THE DEPOSITION ID IS D_1000070590.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 20-DEC-11
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SSRF
REMARK 200 BEAMLINE : BL17U
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.979
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 19456
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.520
REMARK 200 RESOLUTION RANGE LOW (A) : 30.310
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 97.8
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : 0.18600
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 3.8000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.34
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.42
REMARK 200 COMPLETENESS FOR SHELL (%) : 87.9
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 0.870
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER 2.1.4
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 30.26
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.76
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 3.6M NAFORMATE, 10% GLYCEROL, VAPOR
REMARK 280 DIFFUSION, HANGING DROP, TEMPERATURE 293K
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 16.42000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 39.36500
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 23.50000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 39.36500
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 16.42000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 23.50000
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 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 22
REMARK 465 HIS A 23
REMARK 465 HIS A 24
REMARK 465 HIS A 25
REMARK 465 HIS A 26
REMARK 465 HIS A 27
REMARK 465 HIS A 28
REMARK 465 SER A 29
REMARK 465 SER A 30
REMARK 465 GLY A 31
REMARK 465 VAL A 32
REMARK 465 ASP A 33
REMARK 465 LEU A 34
REMARK 465 GLY A 35
REMARK 465 THR A 36
REMARK 465 GLU A 37
REMARK 465 ASN A 38
REMARK 465 LEU A 39
REMARK 465 TYR A 40
REMARK 465 PHE A 41
REMARK 465 GLN A 42
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 LEU A 94 66.37 -118.60
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 3PF A 201
DBREF 4DON A 44 166 UNP O60885 BRD4_HUMAN 44 166
SEQADV 4DON MET A 22 UNP O60885 EXPRESSION TAG
SEQADV 4DON HIS A 23 UNP O60885 EXPRESSION TAG
SEQADV 4DON HIS A 24 UNP O60885 EXPRESSION TAG
SEQADV 4DON HIS A 25 UNP O60885 EXPRESSION TAG
SEQADV 4DON HIS A 26 UNP O60885 EXPRESSION TAG
SEQADV 4DON HIS A 27 UNP O60885 EXPRESSION TAG
SEQADV 4DON HIS A 28 UNP O60885 EXPRESSION TAG
SEQADV 4DON SER A 29 UNP O60885 EXPRESSION TAG
SEQADV 4DON SER A 30 UNP O60885 EXPRESSION TAG
SEQADV 4DON GLY A 31 UNP O60885 EXPRESSION TAG
SEQADV 4DON VAL A 32 UNP O60885 EXPRESSION TAG
SEQADV 4DON ASP A 33 UNP O60885 EXPRESSION TAG
SEQADV 4DON LEU A 34 UNP O60885 EXPRESSION TAG
SEQADV 4DON GLY A 35 UNP O60885 EXPRESSION TAG
SEQADV 4DON THR A 36 UNP O60885 EXPRESSION TAG
SEQADV 4DON GLU A 37 UNP O60885 EXPRESSION TAG
SEQADV 4DON ASN A 38 UNP O60885 EXPRESSION TAG
SEQADV 4DON LEU A 39 UNP O60885 EXPRESSION TAG
SEQADV 4DON TYR A 40 UNP O60885 EXPRESSION TAG
SEQADV 4DON PHE A 41 UNP O60885 EXPRESSION TAG
SEQADV 4DON GLN A 42 UNP O60885 EXPRESSION TAG
SEQADV 4DON MET A 43 UNP O60885 EXPRESSION TAG
SEQRES 1 A 145 MET HIS HIS HIS HIS HIS HIS SER SER GLY VAL ASP LEU
SEQRES 2 A 145 GLY THR GLU ASN LEU TYR PHE GLN MET ASN PRO PRO PRO
SEQRES 3 A 145 PRO GLU THR SER ASN PRO ASN LYS PRO LYS ARG GLN THR
SEQRES 4 A 145 ASN GLN LEU GLN TYR LEU LEU ARG VAL VAL LEU LYS THR
SEQRES 5 A 145 LEU TRP LYS HIS GLN PHE ALA TRP PRO PHE GLN GLN PRO
SEQRES 6 A 145 VAL ASP ALA VAL LYS LEU ASN LEU PRO ASP TYR TYR LYS
SEQRES 7 A 145 ILE ILE LYS THR PRO MET ASP MET GLY THR ILE LYS LYS
SEQRES 8 A 145 ARG LEU GLU ASN ASN TYR TYR TRP ASN ALA GLN GLU CYS
SEQRES 9 A 145 ILE GLN ASP PHE ASN THR MET PHE THR ASN CYS TYR ILE
SEQRES 10 A 145 TYR ASN LYS PRO GLY ASP ASP ILE VAL LEU MET ALA GLU
SEQRES 11 A 145 ALA LEU GLU LYS LEU PHE LEU GLN LYS ILE ASN GLU LEU
SEQRES 12 A 145 PRO THR
HET 3PF A 201 12
HETNAM 3PF 3-METHYL-3,4-DIHYDROQUINAZOLIN-2(1H)-ONE
FORMUL 2 3PF C9 H10 N2 O
FORMUL 3 HOH *129(H2 O)
HELIX 1 1 THR A 60 VAL A 69 1 10
HELIX 2 2 VAL A 69 TRP A 75 1 7
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 ASN A 162 1 19
SITE 1 AC1 7 PRO A 82 VAL A 87 LEU A 92 ASN A 140
SITE 2 AC1 7 ILE A 146 HOH A 308 HOH A 314
CRYST1 32.840 47.000 78.730 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 0.030451 0.000000 0.000000 0.00000
SCALE2 0.000000 0.021277 0.000000 0.00000
SCALE3 0.000000 0.000000 0.012702 0.00000
(ATOM LINES ARE NOT SHOWN.)
END