HEADER TRANSFERASE 05-JAN-19 6J3O
TITLE CRYSTAL STRUCTURE OF THE HUMAN PCAF BROMODOMAIN IN COMPLEX WITH
TITLE 2 COMPOUND 12
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: HISTONE ACETYLTRANSFERASE KAT2B;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: HISTONE ACETYLTRANSFERASE PCAF,HISTONE ACETYLASE PCAF,LYSINE
COMPND 5 ACETYLTRANSFERASE 2B,P300/CBP-ASSOCIATED FACTOR,P/CAF,SPERMIDINE
COMPND 6 ACETYLTRANSFERASE KAT2B;
COMPND 7 EC: 2.3.1.48,2.3.1.57;
COMPND 8 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: KAT2B, PCAF;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS CRYSTAL STRUCTURE OF THE HUMAN PCAF BROMODOMAIN IN COMPLEX WITH
KEYWDS 2 COMPOUND 12, TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR L.Y.HUANG,H.LI,L.L.LI,L.NIU,R.SEUPEL,C.Y.WU,G.B.LI,Y.M.YU,
AUTHOR 2 P.E.BRENNAN,S.Y.YANG
REVDAT 3 22-NOV-23 6J3O 1 REMARK
REVDAT 2 22-MAY-19 6J3O 1 COMPND JRNL REMARK HETNAM
REVDAT 2 2 1 ATOM
REVDAT 1 01-MAY-19 6J3O 0
JRNL AUTH L.HUANG,H.LI,L.LI,L.NIU,R.SEUPEL,C.WU,W.CHENG,C.CHEN,B.DING,
JRNL AUTH 2 P.E.BRENNAN,S.YANG
JRNL TITL DISCOVERY OF PYRROLO[3,2- D]PYRIMIDIN-4-ONE DERIVATIVES AS A
JRNL TITL 2 NEW CLASS OF POTENT AND CELL-ACTIVE INHIBITORS OF
JRNL TITL 3 P300/CBP-ASSOCIATED FACTOR BROMODOMAIN.
JRNL REF J.MED.CHEM. V. 62 4526 2019
JRNL REFN ISSN 0022-2623
JRNL PMID 30998845
JRNL DOI 10.1021/ACS.JMEDCHEM.9B00096
REMARK 2
REMARK 2 RESOLUTION. 2.11 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (1.14RC3_3199: ???)
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 : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.11
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 50.76
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.960
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.3
REMARK 3 NUMBER OF REFLECTIONS : 21873
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.233
REMARK 3 R VALUE (WORKING SET) : 0.230
REMARK 3 FREE R VALUE : 0.257
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 9.130
REMARK 3 FREE R VALUE TEST SET COUNT : 1996
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 50.7747 - 5.0848 0.99 1418 143 0.1886 0.1925
REMARK 3 2 5.0848 - 4.0365 1.00 1430 141 0.1838 0.2129
REMARK 3 3 4.0365 - 3.5264 1.00 1422 146 0.1936 0.2140
REMARK 3 4 3.5264 - 3.2040 1.00 1428 146 0.2236 0.2376
REMARK 3 5 3.2040 - 2.9744 1.00 1432 145 0.2472 0.2764
REMARK 3 6 2.9744 - 2.7991 1.00 1413 142 0.2579 0.3216
REMARK 3 7 2.7991 - 2.6589 1.00 1450 150 0.2809 0.3373
REMARK 3 8 2.6589 - 2.5431 1.00 1398 139 0.2869 0.3659
REMARK 3 9 2.5431 - 2.4452 1.00 1449 147 0.2868 0.3233
REMARK 3 10 2.4452 - 2.3609 1.00 1436 146 0.2842 0.3636
REMARK 3 11 2.3609 - 2.2870 1.00 1436 141 0.3380 0.3780
REMARK 3 12 2.2870 - 2.2217 0.94 1333 125 0.5393 0.6288
REMARK 3 13 2.2217 - 2.1632 0.99 1418 145 0.3786 0.3925
REMARK 3 14 2.1632 - 2.1104 0.99 1414 140 0.3617 0.3983
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : NULL
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) : 0.400
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 33.820
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 : 0.002 1851
REMARK 3 ANGLE : 0.505 2501
REMARK 3 CHIRALITY : 0.035 257
REMARK 3 PLANARITY : 0.003 311
REMARK 3 DIHEDRAL : 16.830 1119
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
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 6J3O COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 22-JAN-19.
REMARK 100 THE DEPOSITION ID IS D_1300010411.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 15-MAR-18
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 : BL17U1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.978897
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 225 MM CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XDS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 21934
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.110
REMARK 200 RESOLUTION RANGE LOW (A) : 50.760
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.6
REMARK 200 DATA REDUNDANCY : 5.300
REMARK 200 R MERGE (I) : 0.12900
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 10.5000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.11
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.17
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 1.55300
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: 5MKX
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 58.58
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.97
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 100 MM HEPES PH 8.2, 26% PEG10000
REMARK 280 (V/V), 4% GLYCOL, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 277K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: H 3
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z
REMARK 290 3555 -X+Y,-X,Z
REMARK 290 4555 X+2/3,Y+1/3,Z+1/3
REMARK 290 5555 -Y+2/3,X-Y+1/3,Z+1/3
REMARK 290 6555 -X+Y+2/3,-X+1/3,Z+1/3
REMARK 290 7555 X+1/3,Y+2/3,Z+2/3
REMARK 290 8555 -Y+1/3,X-Y+2/3,Z+2/3
REMARK 290 9555 -X+Y+1/3,-X+2/3,Z+2/3
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 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 50.76000
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 29.30630
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 33.22667
REMARK 290 SMTRY1 5 -0.500000 -0.866025 0.000000 50.76000
REMARK 290 SMTRY2 5 0.866025 -0.500000 0.000000 29.30630
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 33.22667
REMARK 290 SMTRY1 6 -0.500000 0.866025 0.000000 50.76000
REMARK 290 SMTRY2 6 -0.866025 -0.500000 0.000000 29.30630
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 33.22667
REMARK 290 SMTRY1 7 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 58.61260
REMARK 290 SMTRY3 7 0.000000 0.000000 1.000000 66.45333
REMARK 290 SMTRY1 8 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 8 0.866025 -0.500000 0.000000 58.61260
REMARK 290 SMTRY3 8 0.000000 0.000000 1.000000 66.45333
REMARK 290 SMTRY1 9 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 9 -0.866025 -0.500000 0.000000 58.61260
REMARK 290 SMTRY3 9 0.000000 0.000000 1.000000 66.45333
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 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
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 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 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 692
REMARK 465 HIS A 693
REMARK 465 HIS A 694
REMARK 465 HIS A 695
REMARK 465 HIS A 696
REMARK 465 HIS A 697
REMARK 465 HIS A 698
REMARK 465 SER A 699
REMARK 465 SER A 700
REMARK 465 GLY A 701
REMARK 465 VAL A 702
REMARK 465 ASP A 703
REMARK 465 LEU A 704
REMARK 465 GLY A 705
REMARK 465 THR A 706
REMARK 465 GLU A 707
REMARK 465 ASN A 708
REMARK 465 LEU A 709
REMARK 465 TYR A 710
REMARK 465 PHE A 711
REMARK 465 GLN A 712
REMARK 465 SER A 713
REMARK 465 MET A 714
REMARK 465 GLY A 715
REMARK 465 LYS A 716
REMARK 465 GLU A 717
REMARK 465 LYS A 718
REMARK 465 SER A 719
REMARK 465 LYS A 720
REMARK 465 GLU A 721
REMARK 465 PRO A 722
REMARK 465 ARG A 723
REMARK 465 ASP A 724
REMARK 465 PRO A 725
REMARK 465 MET B 692
REMARK 465 HIS B 693
REMARK 465 HIS B 694
REMARK 465 HIS B 695
REMARK 465 HIS B 696
REMARK 465 HIS B 697
REMARK 465 HIS B 698
REMARK 465 SER B 699
REMARK 465 SER B 700
REMARK 465 GLY B 701
REMARK 465 VAL B 702
REMARK 465 ASP B 703
REMARK 465 LEU B 704
REMARK 465 GLY B 705
REMARK 465 THR B 706
REMARK 465 GLU B 707
REMARK 465 ASN B 708
REMARK 465 LEU B 709
REMARK 465 TYR B 710
REMARK 465 PHE B 711
REMARK 465 GLN B 712
REMARK 465 SER B 713
REMARK 465 MET B 714
REMARK 465 GLY B 715
REMARK 465 LYS B 716
REMARK 465 GLU B 717
REMARK 465 LYS B 718
REMARK 465 SER B 719
REMARK 465 LYS B 720
REMARK 465 GLU B 721
REMARK 465 PRO B 722
REMARK 465 ARG B 723
REMARK 465 ASP B 724
REMARK 465 PRO B 725
REMARK 465 ASP B 831
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 ARG A 765 CG CD NE CZ NH1 NH2
REMARK 470 LYS A 778 CG CD CE NZ
REMARK 470 LYS A 786 CD CE NZ
REMARK 470 LYS B 785 CG CD CE NZ
REMARK 470 LYS B 786 CD CE NZ
REMARK 470 GLU B 808 CG CD OE1 OE2
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 ARG A 780 32.83 73.41
REMARK 500 LYS A 786 87.48 -64.05
REMARK 500 LEU A 787 -65.87 163.10
REMARK 500 ILE B 764 92.86 62.57
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 B1020 DISTANCE = 5.89 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue B4L A 900
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue B4L B 900
DBREF 6J3O A 715 831 UNP Q92831 KAT2B_HUMAN 715 831
DBREF 6J3O B 715 831 UNP Q92831 KAT2B_HUMAN 715 831
SEQADV 6J3O MET A 692 UNP Q92831 INITIATING METHIONINE
SEQADV 6J3O HIS A 693 UNP Q92831 EXPRESSION TAG
SEQADV 6J3O HIS A 694 UNP Q92831 EXPRESSION TAG
SEQADV 6J3O HIS A 695 UNP Q92831 EXPRESSION TAG
SEQADV 6J3O HIS A 696 UNP Q92831 EXPRESSION TAG
SEQADV 6J3O HIS A 697 UNP Q92831 EXPRESSION TAG
SEQADV 6J3O HIS A 698 UNP Q92831 EXPRESSION TAG
SEQADV 6J3O SER A 699 UNP Q92831 EXPRESSION TAG
SEQADV 6J3O SER A 700 UNP Q92831 EXPRESSION TAG
SEQADV 6J3O GLY A 701 UNP Q92831 EXPRESSION TAG
SEQADV 6J3O VAL A 702 UNP Q92831 EXPRESSION TAG
SEQADV 6J3O ASP A 703 UNP Q92831 EXPRESSION TAG
SEQADV 6J3O LEU A 704 UNP Q92831 EXPRESSION TAG
SEQADV 6J3O GLY A 705 UNP Q92831 EXPRESSION TAG
SEQADV 6J3O THR A 706 UNP Q92831 EXPRESSION TAG
SEQADV 6J3O GLU A 707 UNP Q92831 EXPRESSION TAG
SEQADV 6J3O ASN A 708 UNP Q92831 EXPRESSION TAG
SEQADV 6J3O LEU A 709 UNP Q92831 EXPRESSION TAG
SEQADV 6J3O TYR A 710 UNP Q92831 EXPRESSION TAG
SEQADV 6J3O PHE A 711 UNP Q92831 EXPRESSION TAG
SEQADV 6J3O GLN A 712 UNP Q92831 EXPRESSION TAG
SEQADV 6J3O SER A 713 UNP Q92831 EXPRESSION TAG
SEQADV 6J3O MET A 714 UNP Q92831 EXPRESSION TAG
SEQADV 6J3O MET B 692 UNP Q92831 INITIATING METHIONINE
SEQADV 6J3O HIS B 693 UNP Q92831 EXPRESSION TAG
SEQADV 6J3O HIS B 694 UNP Q92831 EXPRESSION TAG
SEQADV 6J3O HIS B 695 UNP Q92831 EXPRESSION TAG
SEQADV 6J3O HIS B 696 UNP Q92831 EXPRESSION TAG
SEQADV 6J3O HIS B 697 UNP Q92831 EXPRESSION TAG
SEQADV 6J3O HIS B 698 UNP Q92831 EXPRESSION TAG
SEQADV 6J3O SER B 699 UNP Q92831 EXPRESSION TAG
SEQADV 6J3O SER B 700 UNP Q92831 EXPRESSION TAG
SEQADV 6J3O GLY B 701 UNP Q92831 EXPRESSION TAG
SEQADV 6J3O VAL B 702 UNP Q92831 EXPRESSION TAG
SEQADV 6J3O ASP B 703 UNP Q92831 EXPRESSION TAG
SEQADV 6J3O LEU B 704 UNP Q92831 EXPRESSION TAG
SEQADV 6J3O GLY B 705 UNP Q92831 EXPRESSION TAG
SEQADV 6J3O THR B 706 UNP Q92831 EXPRESSION TAG
SEQADV 6J3O GLU B 707 UNP Q92831 EXPRESSION TAG
SEQADV 6J3O ASN B 708 UNP Q92831 EXPRESSION TAG
SEQADV 6J3O LEU B 709 UNP Q92831 EXPRESSION TAG
SEQADV 6J3O TYR B 710 UNP Q92831 EXPRESSION TAG
SEQADV 6J3O PHE B 711 UNP Q92831 EXPRESSION TAG
SEQADV 6J3O GLN B 712 UNP Q92831 EXPRESSION TAG
SEQADV 6J3O SER B 713 UNP Q92831 EXPRESSION TAG
SEQADV 6J3O MET B 714 UNP Q92831 EXPRESSION TAG
SEQRES 1 A 140 MET HIS HIS HIS HIS HIS HIS SER SER GLY VAL ASP LEU
SEQRES 2 A 140 GLY THR GLU ASN LEU TYR PHE GLN SER MET GLY LYS GLU
SEQRES 3 A 140 LYS SER LYS GLU PRO ARG ASP PRO ASP GLN LEU TYR SER
SEQRES 4 A 140 THR LEU LYS SER ILE LEU GLN GLN VAL LYS SER HIS GLN
SEQRES 5 A 140 SER ALA TRP PRO PHE MET GLU PRO VAL LYS ARG THR GLU
SEQRES 6 A 140 ALA PRO GLY TYR TYR GLU VAL ILE ARG PHE PRO MET ASP
SEQRES 7 A 140 LEU LYS THR MET SER GLU ARG LEU LYS ASN ARG TYR TYR
SEQRES 8 A 140 VAL SER LYS LYS LEU PHE MET ALA ASP LEU GLN ARG VAL
SEQRES 9 A 140 PHE THR ASN CYS LYS GLU TYR ASN PRO PRO GLU SER GLU
SEQRES 10 A 140 TYR TYR LYS CYS ALA ASN ILE LEU GLU LYS PHE PHE PHE
SEQRES 11 A 140 SER LYS ILE LYS GLU ALA GLY LEU ILE ASP
SEQRES 1 B 140 MET HIS HIS HIS HIS HIS HIS SER SER GLY VAL ASP LEU
SEQRES 2 B 140 GLY THR GLU ASN LEU TYR PHE GLN SER MET GLY LYS GLU
SEQRES 3 B 140 LYS SER LYS GLU PRO ARG ASP PRO ASP GLN LEU TYR SER
SEQRES 4 B 140 THR LEU LYS SER ILE LEU GLN GLN VAL LYS SER HIS GLN
SEQRES 5 B 140 SER ALA TRP PRO PHE MET GLU PRO VAL LYS ARG THR GLU
SEQRES 6 B 140 ALA PRO GLY TYR TYR GLU VAL ILE ARG PHE PRO MET ASP
SEQRES 7 B 140 LEU LYS THR MET SER GLU ARG LEU LYS ASN ARG TYR TYR
SEQRES 8 B 140 VAL SER LYS LYS LEU PHE MET ALA ASP LEU GLN ARG VAL
SEQRES 9 B 140 PHE THR ASN CYS LYS GLU TYR ASN PRO PRO GLU SER GLU
SEQRES 10 B 140 TYR TYR LYS CYS ALA ASN ILE LEU GLU LYS PHE PHE PHE
SEQRES 11 B 140 SER LYS ILE LYS GLU ALA GLY LEU ILE ASP
HET B4L A 900 19
HET B4L B 900 19
HETNAM B4L 3-METHYL-2-[[(3~{R})-1-METHYLPIPERIDIN-3-YL]AMINO]-
HETNAM 2 B4L 5~{H}-PYRROLO[3,2-D]PYRIMIDIN-4-ONE
FORMUL 3 B4L 2(C13 H19 N5 O)
FORMUL 5 HOH *44(H2 O)
HELIX 1 AA1 ASP A 726 HIS A 742 1 17
HELIX 2 AA2 GLN A 743 MET A 749 5 7
HELIX 3 AA3 GLY A 759 VAL A 763 5 5
HELIX 4 AA4 ASP A 769 ASN A 779 1 11
HELIX 5 AA5 SER A 784 ASN A 803 1 20
HELIX 6 AA6 SER A 807 ALA A 827 1 21
HELIX 7 AA7 GLN B 727 SER B 741 1 15
HELIX 8 AA8 HIS B 742 MET B 749 5 8
HELIX 9 AA9 ASP B 769 ASN B 779 1 11
HELIX 10 AB1 SER B 784 ASN B 803 1 20
HELIX 11 AB2 SER B 807 ALA B 827 1 21
SITE 1 AC1 6 PRO A 747 PRO A 751 GLU A 756 ASN A 803
SITE 2 AC1 6 TYR A 809 HOH A1018
SITE 1 AC2 6 PRO B 747 PRO B 751 GLU B 756 ALA B 757
SITE 2 AC2 6 ASN B 803 TYR B 809
CRYST1 101.520 101.520 99.680 90.00 90.00 120.00 H 3 18
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 0.009850 0.005687 0.000000 0.00000
SCALE2 0.000000 0.011374 0.000000 0.00000
SCALE3 0.000000 0.000000 0.010032 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
