HEADER HYDROLASE 10-DEC-07 3BLA
TITLE SYNTHETIC GENE ENCODED DCPS BOUND TO INHIBITOR DG153249
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: SCAVENGER MRNA-DECAPPING ENZYME DCPS;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: UNP RESIDUES 38-337;
COMPND 5 SYNONYM: DCS-1, HINT- RELATED 7MEGMP-DIRECTED HYDROLASE, HISTIDINE
COMPND 6 TRIAD PROTEIN MEMBER 5, HINT-5;
COMPND 7 EC: 3.-.-.-;
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: DCPS, DCS1, HINT5;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PBAD
KEYWDS MRNA DECAPPING ENZYME, DCPS, LIGAND COMPLEX, CYTOPLASM, HYDROLASE,
KEYWDS 2 NONSENSE-MEDIATED MRNA DECAY, NUCLEUS, POLYMORPHISM, STRUCTURAL
KEYWDS 3 GENOMICS, PSI-2, PROTEIN STRUCTURE INITIATIVE, ACCELERATED
KEYWDS 4 TECHNOLOGIES CENTER FOR GENE TO 3D STRUCTURE, ATCG3D
EXPDTA X-RAY DIFFRACTION
AUTHOR B.L.STAKER,J.CHRISTENSEN,L.STEWART,ACCELERATED TECHNOLOGIES CENTER
AUTHOR 2 FOR GENE TO 3D STRUCTURE (ATCG3D)
REVDAT 7 30-AUG-23 3BLA 1 REMARK SEQADV
REVDAT 6 06-OCT-09 3BLA 1 TITLE
REVDAT 5 08-SEP-09 3BLA 1 AUTHOR
REVDAT 4 09-JUN-09 3BLA 1 REVDAT
REVDAT 3 24-FEB-09 3BLA 1 VERSN
REVDAT 2 16-DEC-08 3BLA 1 JRNL
REVDAT 1 21-OCT-08 3BLA 0
JRNL AUTH J.SINGH,M.SALCIUS,S.W.LIU,B.L.STAKER,R.MISHRA,J.THURMOND,
JRNL AUTH 2 G.MICHAUD,D.R.MATTOON,J.PRINTEN,J.CHRISTENSEN,J.M.BJORNSSON,
JRNL AUTH 3 B.A.POLLOK,M.KILEDJIAN,L.STEWART,J.JARECKI,M.E.GURNEY
JRNL TITL DCPS AS A THERAPEUTIC TARGET FOR SPINAL MUSCULAR ATROPHY.
JRNL REF ACS CHEM.BIOL. V. 3 711 2008
JRNL REFN ISSN 1554-8929
JRNL PMID 18839960
JRNL DOI 10.1021/CB800120T
REMARK 2
REMARK 2 RESOLUTION. 2.60 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC REFMAC_5.2.0019
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) : 2.60
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 32.84
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 95.8
REMARK 3 NUMBER OF REFLECTIONS : 15958
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) : 0.213
REMARK 3 R VALUE (WORKING SET) : 0.210
REMARK 3 FREE R VALUE : 0.278
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 799
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) : 2.60
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.66
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1024
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 87.74
REMARK 3 BIN R VALUE (WORKING SET) : 0.2970
REMARK 3 BIN FREE R VALUE SET COUNT : 49
REMARK 3 BIN FREE R VALUE : 0.3740
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 4755
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 44
REMARK 3 SOLVENT ATOMS : 64
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 27.09
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.39000
REMARK 3 B22 (A**2) : -0.34000
REMARK 3 B33 (A**2) : 0.05000
REMARK 3 B12 (A**2) : 0.33000
REMARK 3 B13 (A**2) : 1.92000
REMARK 3 B23 (A**2) : -0.26000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): NULL
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.422
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.312
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 14.791
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.927
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.879
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 4915 ; 0.008 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): 3384 ; 0.001 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 6673 ; 1.121 ; 1.978
REMARK 3 BOND ANGLES OTHERS (DEGREES): 8199 ; 0.828 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 571 ; 6.113 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 257 ;35.881 ;23.541
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 852 ;16.919 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 43 ;20.378 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 734 ; 0.062 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 5400 ; 0.003 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 1031 ; 0.001 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 1102 ; 0.209 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): 3670 ; 0.188 ; 0.200
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 2315 ; 0.176 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): 2676 ; 0.082 ; 0.200
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 153 ; 0.147 ; 0.200
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): 20 ; 0.160 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): 78 ; 0.178 ; 0.200
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 4 ; 0.096 ; 0.200
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): 3762 ; 0.473 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 1138 ; 0.049 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 4676 ; 0.529 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 2379 ; 0.684 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1997 ; 1.082 ; 4.500
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 : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : 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
REMARK 4
REMARK 4 3BLA COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 12-DEC-07.
REMARK 100 THE DEPOSITION ID IS D_1000045660.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 27-SEP-07
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
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 RU300
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.54178
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : RIGAKU SATURN 944
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK, HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 15959
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.600
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 1.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 96.3
REMARK 200 DATA REDUNDANCY : 2.000
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.10400
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 9.7000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.60
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.69
REMARK 200 COMPLETENESS FOR SHELL (%) : 94.3
REMARK 200 DATA REDUNDANCY IN SHELL : 2.00
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.46700
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.000
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: PDB ENTRY 1ST0
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 40.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.10
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 3350, AMMONIUM FORMATE, VAPOR
REMARK 280 DIFFUSION, HANGING DROP, TEMPERATURE 289K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,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
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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 8790 ANGSTROM**2
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 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 SER A 37
REMARK 465 ALA A 38
REMARK 465 PRO A 39
REMARK 465 VAL A 40
REMARK 465 ARG A 41
REMARK 465 ALA A 71
REMARK 465 SER A 72
REMARK 465 GLY A 73
REMARK 465 ASP A 74
REMARK 465 GLY A 75
REMARK 465 ASP A 76
REMARK 465 GLY A 77
REMARK 465 GLN A 335
REMARK 465 GLN A 336
REMARK 465 SER A 337
REMARK 465 SER B 37
REMARK 465 ALA B 38
REMARK 465 PRO B 39
REMARK 465 GLU B 70
REMARK 465 ALA B 71
REMARK 465 SER B 72
REMARK 465 GLY B 73
REMARK 465 ASP B 74
REMARK 465 GLY B 75
REMARK 465 ASP B 76
REMARK 465 GLY B 77
REMARK 465 SER B 337
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 A 146 CG CD OE1 NE2
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 69 77.74 52.97
REMARK 500 ASP A 111 -110.61 50.22
REMARK 500 LEU A 144 123.80 -33.20
REMARK 500 TYR A 274 58.16 -96.85
REMARK 500 LEU A 276 134.71 -36.48
REMARK 500 GLU A 293 1.64 -67.99
REMARK 500 ARG A 294 -30.94 -146.90
REMARK 500 ASP A 308 88.08 -158.69
REMARK 500 PRO B 43 13.56 -65.71
REMARK 500 GLU B 103 84.58 -63.00
REMARK 500 ASN B 110 115.99 -161.97
REMARK 500 ASP B 111 -125.99 55.54
REMARK 500 LEU B 144 109.85 -45.32
REMARK 500 ILE B 161 -52.94 -124.75
REMARK 500 LYS B 182 34.47 74.45
REMARK 500 PRO B 194 2.21 -65.74
REMARK 500 ARG B 255 -70.14 -76.21
REMARK 500 TYR B 274 57.17 -94.53
REMARK 500 ARG B 294 -39.37 -132.50
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 DD3 A 1
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DD3 B 2
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1ST0 RELATED DB: PDB
REMARK 900 STRUCTURE OF DCPS BOUND TO M7GPPPG
REMARK 900 RELATED ID: 1ST4 RELATED DB: PDB
REMARK 900 STRUCTURE OF DCPS BOUND TO M7GPPPA
REMARK 900 RELATED ID: 3BL7 RELATED DB: PDB
REMARK 900 DCPS BOUND TO INHIBITOR DG156844
REMARK 900 RELATED ID: 3BL9 RELATED DB: PDB
REMARK 900 DCPS BOUND TO INHIBITOR DG157493
DBREF 3BLA A 38 337 UNP Q96C86 DCPS_HUMAN 38 337
DBREF 3BLA B 38 337 UNP Q96C86 DCPS_HUMAN 38 337
SEQADV 3BLA SER A 37 UNP Q96C86 EXPRESSION TAG
SEQADV 3BLA SER B 37 UNP Q96C86 EXPRESSION TAG
SEQRES 1 A 301 SER ALA PRO VAL ARG LEU PRO PHE SER GLY PHE ARG LEU
SEQRES 2 A 301 GLN LYS VAL LEU ARG GLU SER ALA ARG ASP LYS ILE ILE
SEQRES 3 A 301 PHE LEU HIS GLY LYS VAL ASN GLU ALA SER GLY ASP GLY
SEQRES 4 A 301 ASP GLY GLU ASP ALA VAL VAL ILE LEU GLU LYS THR PRO
SEQRES 5 A 301 PHE GLN VAL GLU GLN VAL ALA GLN LEU LEU THR GLY SER
SEQRES 6 A 301 PRO GLU LEU GLN LEU GLN PHE SER ASN ASP ILE TYR SER
SEQRES 7 A 301 THR TYR HIS LEU PHE PRO PRO ARG GLN LEU ASN ASP VAL
SEQRES 8 A 301 LYS THR THR VAL VAL TYR PRO ALA THR GLU LYS HIS LEU
SEQRES 9 A 301 GLN LYS TYR LEU ARG GLN ASP LEU ARG LEU ILE ARG GLU
SEQRES 10 A 301 THR GLY ASP ASP TYR ARG ASN ILE THR LEU PRO HIS LEU
SEQRES 11 A 301 GLU SER GLN SER LEU SER ILE GLN TRP VAL TYR ASN ILE
SEQRES 12 A 301 LEU ASP LYS LYS ALA GLU ALA ASP ARG ILE VAL PHE GLU
SEQRES 13 A 301 ASN PRO ASP PRO SER ASP GLY PHE VAL LEU ILE PRO ASP
SEQRES 14 A 301 LEU LYS TRP ASN GLN GLN GLN LEU ASP ASP LEU TYR LEU
SEQRES 15 A 301 ILE ALA ILE CYS HIS ARG ARG GLY ILE ARG SER LEU ARG
SEQRES 16 A 301 ASP LEU THR PRO GLU HIS LEU PRO LEU LEU ARG ASN ILE
SEQRES 17 A 301 LEU HIS GLN GLY GLN GLU ALA ILE LEU GLN ARG TYR ARG
SEQRES 18 A 301 MET LYS GLY ASP HIS LEU ARG VAL TYR LEU HIS TYR LEU
SEQRES 19 A 301 PRO SER TYR TYR HIS LEU HIS VAL HIS PHE THR ALA LEU
SEQRES 20 A 301 GLY PHE GLU ALA PRO GLY SER GLY VAL GLU ARG ALA HIS
SEQRES 21 A 301 LEU LEU ALA GLU VAL ILE GLU ASN LEU GLU CYS ASP PRO
SEQRES 22 A 301 ARG HIS TYR GLN GLN ARG THR LEU THR PHE ALA LEU ARG
SEQRES 23 A 301 ALA ASP ASP PRO LEU LEU LYS LEU LEU GLN GLU ALA GLN
SEQRES 24 A 301 GLN SER
SEQRES 1 B 301 SER ALA PRO VAL ARG LEU PRO PHE SER GLY PHE ARG LEU
SEQRES 2 B 301 GLN LYS VAL LEU ARG GLU SER ALA ARG ASP LYS ILE ILE
SEQRES 3 B 301 PHE LEU HIS GLY LYS VAL ASN GLU ALA SER GLY ASP GLY
SEQRES 4 B 301 ASP GLY GLU ASP ALA VAL VAL ILE LEU GLU LYS THR PRO
SEQRES 5 B 301 PHE GLN VAL GLU GLN VAL ALA GLN LEU LEU THR GLY SER
SEQRES 6 B 301 PRO GLU LEU GLN LEU GLN PHE SER ASN ASP ILE TYR SER
SEQRES 7 B 301 THR TYR HIS LEU PHE PRO PRO ARG GLN LEU ASN ASP VAL
SEQRES 8 B 301 LYS THR THR VAL VAL TYR PRO ALA THR GLU LYS HIS LEU
SEQRES 9 B 301 GLN LYS TYR LEU ARG GLN ASP LEU ARG LEU ILE ARG GLU
SEQRES 10 B 301 THR GLY ASP ASP TYR ARG ASN ILE THR LEU PRO HIS LEU
SEQRES 11 B 301 GLU SER GLN SER LEU SER ILE GLN TRP VAL TYR ASN ILE
SEQRES 12 B 301 LEU ASP LYS LYS ALA GLU ALA ASP ARG ILE VAL PHE GLU
SEQRES 13 B 301 ASN PRO ASP PRO SER ASP GLY PHE VAL LEU ILE PRO ASP
SEQRES 14 B 301 LEU LYS TRP ASN GLN GLN GLN LEU ASP ASP LEU TYR LEU
SEQRES 15 B 301 ILE ALA ILE CYS HIS ARG ARG GLY ILE ARG SER LEU ARG
SEQRES 16 B 301 ASP LEU THR PRO GLU HIS LEU PRO LEU LEU ARG ASN ILE
SEQRES 17 B 301 LEU HIS GLN GLY GLN GLU ALA ILE LEU GLN ARG TYR ARG
SEQRES 18 B 301 MET LYS GLY ASP HIS LEU ARG VAL TYR LEU HIS TYR LEU
SEQRES 19 B 301 PRO SER TYR TYR HIS LEU HIS VAL HIS PHE THR ALA LEU
SEQRES 20 B 301 GLY PHE GLU ALA PRO GLY SER GLY VAL GLU ARG ALA HIS
SEQRES 21 B 301 LEU LEU ALA GLU VAL ILE GLU ASN LEU GLU CYS ASP PRO
SEQRES 22 B 301 ARG HIS TYR GLN GLN ARG THR LEU THR PHE ALA LEU ARG
SEQRES 23 B 301 ALA ASP ASP PRO LEU LEU LYS LEU LEU GLN GLU ALA GLN
SEQRES 24 B 301 GLN SER
HET DD3 A 1 22
HET DD3 B 2 22
HETNAM DD3 5-[(1S)-1-(3-CHLOROPHENYL)ETHOXY]QUINAZOLINE-2,4-
HETNAM 2 DD3 DIAMINE
FORMUL 3 DD3 2(C16 H15 CL N4 O)
FORMUL 5 HOH *64(H2 O)
HELIX 1 1 GLN A 90 THR A 99 1 10
HELIX 2 2 PRO A 121 ASN A 125 5 5
HELIX 3 3 THR A 136 LEU A 144 1 9
HELIX 4 4 THR A 154 ILE A 161 1 8
HELIX 5 5 ILE A 161 SER A 168 1 8
HELIX 6 6 ILE A 173 ASP A 181 1 9
HELIX 7 7 GLU A 185 ILE A 189 5 5
HELIX 8 8 GLN A 212 ASP A 215 5 4
HELIX 9 9 SER A 229 LEU A 233 5 5
HELIX 10 10 THR A 234 GLU A 236 5 3
HELIX 11 11 HIS A 237 ARG A 257 1 21
HELIX 12 12 LYS A 259 ASP A 261 5 3
HELIX 13 13 LEU A 298 ASP A 308 1 11
HELIX 14 14 ARG A 310 ARG A 315 1 6
HELIX 15 15 PRO A 326 ALA A 334 1 9
HELIX 16 16 GLN B 90 LEU B 98 1 9
HELIX 17 17 PRO B 121 ASN B 125 5 5
HELIX 18 18 THR B 136 LEU B 144 1 9
HELIX 19 19 THR B 154 ILE B 161 1 8
HELIX 20 20 ILE B 161 SER B 168 1 8
HELIX 21 21 ILE B 173 ASP B 181 1 9
HELIX 22 22 GLU B 185 ILE B 189 5 5
HELIX 23 23 GLN B 212 ASP B 215 5 4
HELIX 24 24 SER B 229 LEU B 233 5 5
HELIX 25 25 THR B 234 GLU B 236 5 3
HELIX 26 26 HIS B 237 ARG B 257 1 21
HELIX 27 27 LYS B 259 ASP B 261 5 3
HELIX 28 28 LEU B 298 ASP B 308 1 11
HELIX 29 29 ARG B 310 ARG B 315 1 6
HELIX 30 30 ASP B 325 GLN B 335 1 11
SHEET 1 A 6 ARG A 48 SER A 56 0
SHEET 2 A 6 ILE A 61 LYS A 67 -1 O HIS A 65 N GLN A 50
SHEET 3 A 6 ASP A 79 LYS A 86 -1 O ALA A 80 N GLY A 66
SHEET 4 A 6 VAL A 127 VAL A 132 -1 O THR A 130 N ILE A 83
SHEET 5 A 6 TYR B 113 LEU B 118 -1 O TYR B 116 N THR A 129
SHEET 6 A 6 LEU B 104 ASN B 110 -1 N GLN B 107 O THR B 115
SHEET 1 B 6 LEU A 104 ASN A 110 0
SHEET 2 B 6 TYR A 113 LEU A 118 -1 O THR A 115 N PHE A 108
SHEET 3 B 6 VAL B 127 VAL B 132 -1 O THR B 129 N TYR A 116
SHEET 4 B 6 ASP B 79 LYS B 86 -1 N ILE B 83 O THR B 130
SHEET 5 B 6 ILE B 61 LYS B 67 -1 N LEU B 64 O VAL B 82
SHEET 6 B 6 ARG B 48 SER B 56 -1 N ARG B 54 O PHE B 63
SHEET 1 C 2 LEU A 148 GLU A 153 0
SHEET 2 C 2 LEU A 317 ARG A 322 -1 O LEU A 321 N ARG A 149
SHEET 1 D 6 PHE A 191 ASN A 193 0
SHEET 2 D 6 PHE A 200 PRO A 204 -1 O LEU A 202 N PHE A 191
SHEET 3 D 6 TYR A 217 CYS A 222 -1 O ILE A 219 N ILE A 203
SHEET 4 D 6 HIS A 277 ALA A 282 -1 O PHE A 280 N LEU A 218
SHEET 5 D 6 LEU A 263 HIS A 268 -1 N TYR A 266 O HIS A 279
SHEET 6 D 6 ALA A 295 LEU A 297 -1 O HIS A 296 N LEU A 267
SHEET 1 E 2 LEU B 148 GLU B 153 0
SHEET 2 E 2 LEU B 317 ARG B 322 -1 O LEU B 317 N GLU B 153
SHEET 1 F 6 PHE B 191 ASN B 193 0
SHEET 2 F 6 PHE B 200 PRO B 204 -1 O LEU B 202 N PHE B 191
SHEET 3 F 6 TYR B 217 CYS B 222 -1 O ILE B 219 N ILE B 203
SHEET 4 F 6 HIS B 277 ALA B 282 -1 O PHE B 280 N LEU B 218
SHEET 5 F 6 LEU B 263 HIS B 268 -1 N TYR B 266 O HIS B 279
SHEET 6 F 6 ALA B 295 LEU B 297 -1 O HIS B 296 N LEU B 267
CISPEP 1 TYR A 133 PRO A 134 0 -4.69
CISPEP 2 TYR A 269 LEU A 270 0 -0.13
CISPEP 3 TYR B 133 PRO B 134 0 -7.22
CISPEP 4 TYR B 269 LEU B 270 0 -4.92
SITE 1 AC1 11 ILE A 83 TYR A 143 TRP A 175 GLU A 185
SITE 2 AC1 11 ARG A 188 PRO A 204 ASP A 205 LEU A 206
SITE 3 AC1 11 ILE A 219 TYR A 273 TYR B 113
SITE 1 AC2 7 TRP B 175 GLU B 185 ARG B 188 PRO B 204
SITE 2 AC2 7 ASP B 205 LEU B 206 LYS B 207
CRYST1 48.730 55.812 59.400 117.68 93.35 99.72 P 1 2
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 0.020521 0.003517 0.003304 0.00000
SCALE2 0.000000 0.018179 0.010003 0.00000
SCALE3 0.000000 0.000000 0.019248 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
