HEADER TRANSFERASE/TRANSFERASE INHIBITOR 27-NOV-12 4I4E
TITLE STRUCTURE OF FOCAL ADHESION KINASE CATALYTIC DOMAIN IN COMPLEX WITH
TITLE 2 HINGE BINDING PYRAZOLOBENZOTHIAZINE COMPOUND.
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: FOCAL ADHESION KINASE 1;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: KINASE DOMAIN: UNP RESIDUES 411-686;
COMPND 5 SYNONYM: FADK 1, FOCAL ADHESION KINASE-RELATED NONKINASE, FRNK,
COMPND 6 PROTEIN PHOSPHATASE 1 REGULATORY SUBUNIT 71, PPP1R71, PROTEIN-
COMPND 7 TYROSINE KINASE 2, P125FAK, PP125FAK;
COMPND 8 EC: 2.7.10.2;
COMPND 9 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: PTK2, FAK, FAK1;
SOURCE 6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 7108
KEYWDS PHOSPHORYLATED ON TYROSINES, TRANSFERASE, CYTOPLASMIC; LOCALIZED TO
KEYWDS 2 FOCAL ADHESIONS, TRANSFERASE-TRANSFERASE INHIBITOR COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR R.J.SKENE,D.J.HOSFIELD
REVDAT 3 20-SEP-23 4I4E 1 REMARK SEQADV
REVDAT 2 24-APR-13 4I4E 1 JRNL
REVDAT 1 06-MAR-13 4I4E 0
JRNL AUTH N.TOMITA,Y.HAYASHI,S.SUZUKI,Y.OOMORI,Y.ARAMAKI,Y.MATSUSHITA,
JRNL AUTH 2 M.IWATANI,H.IWATA,A.OKABE,Y.AWAZU,O.ISONO,R.J.SKENE,
JRNL AUTH 3 D.J.HOSFIELD,H.MIKI,T.KAWAMOTO,A.HORI,A.BABA
JRNL TITL STRUCTURE-BASED DISCOVERY OF CELLULAR-ACTIVE ALLOSTERIC
JRNL TITL 2 INHIBITORS OF FAK.
JRNL REF BIOORG.MED.CHEM.LETT. V. 23 1779 2013
JRNL REFN ISSN 0960-894X
JRNL PMID 23414845
JRNL DOI 10.1016/J.BMCL.2013.01.047
REMARK 2
REMARK 2 RESOLUTION. 1.55 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.7.0025
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) : 1.55
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 45.06
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 96.6
REMARK 3 NUMBER OF REFLECTIONS : 35403
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) : 0.166
REMARK 3 R VALUE (WORKING SET) : 0.165
REMARK 3 FREE R VALUE : 0.189
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 1852
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) : 1.55
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.59
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1873
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 68.80
REMARK 3 BIN R VALUE (WORKING SET) : 0.2320
REMARK 3 BIN FREE R VALUE SET COUNT : 85
REMARK 3 BIN FREE R VALUE : 0.2390
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2043
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 33
REMARK 3 SOLVENT ATOMS : 295
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 21.97
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.30000
REMARK 3 B22 (A**2) : -0.11000
REMARK 3 B33 (A**2) : 0.62000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.71000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.081
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.079
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.051
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 3.087
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.967
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.953
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 2173 ; 0.008 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 2097 ; 0.001 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 2945 ; 1.325 ; 1.983
REMARK 3 BOND ANGLES OTHERS (DEGREES): 4828 ; 0.781 ; 3.001
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 251 ; 5.128 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 99 ;31.587 ;23.232
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 398 ;11.054 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 19 ;16.305 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 327 ; 0.076 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 2369 ; 0.005 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 495 ; 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 : 1
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 NUMBER OF COMPONENTS GROUP : 3
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 414 A 686
REMARK 3 RESIDUE RANGE : A 1000 A 1000
REMARK 3 RESIDUE RANGE : A 1001 A 1395
REMARK 3 ORIGIN FOR THE GROUP (A): 9.7740 -0.0336 14.9842
REMARK 3 T TENSOR
REMARK 3 T11: 0.0079 T22: 0.0183
REMARK 3 T33: 0.0074 T12: -0.0053
REMARK 3 T13: -0.0066 T23: -0.0001
REMARK 3 L TENSOR
REMARK 3 L11: 0.2002 L22: 0.5551
REMARK 3 L33: 0.3954 L12: -0.1095
REMARK 3 L13: -0.1160 L23: 0.1886
REMARK 3 S TENSOR
REMARK 3 S11: 0.0078 S12: -0.0304 S13: -0.0053
REMARK 3 S21: 0.0532 S22: -0.0253 S23: -0.0440
REMARK 3 S31: 0.0059 S32: -0.0478 S33: 0.0176
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 : 1.40
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 4I4E COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 28-NOV-12.
REMARK 100 THE DEPOSITION ID IS D_1000076289.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 01-SEP-09
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ALS
REMARK 200 BEAMLINE : 5.0.1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0
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 : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 35403
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.550
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 96.7
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.55
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.58
REMARK 200 COMPLETENESS FOR SHELL (%) : 67.1
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 : NULL
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: 1MP8
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 40.86
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.08
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 20% PEG4000, 8% 2-PROPANOL, 12%
REMARK 280 GLYCEROL, 0.1M HEPES, PH 7.5, VAPOR DIFFUSION, SITTING DROP,
REMARK 280 TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,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 23.66950
REMARK 290 SMTRY3 2 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 GLY A 406
REMARK 465 ALA A 407
REMARK 465 MET A 408
REMARK 465 GLY A 409
REMARK 465 SER A 410
REMARK 465 SER A 411
REMARK 465 THR A 412
REMARK 465 ARG A 413
REMARK 465 GLU A 445
REMARK 465 GLY A 566
REMARK 465 LEU A 567
REMARK 465 SER A 568
REMARK 465 ARG A 569
REMARK 465 TYR A 570
REMARK 465 MET A 571
REMARK 465 GLU A 572
REMARK 465 ASP A 573
REMARK 465 SER A 574
REMARK 465 THR A 575
REMARK 465 TYR A 576
REMARK 465 TYR A 577
REMARK 465 LYS A 578
REMARK 465 ALA A 579
REMARK 465 SER A 580
REMARK 465 LYS A 581
REMARK 465 GLY A 582
REMARK 465 LYS A 583
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 ALA A 448 70.63 -151.05
REMARK 500 ARG A 545 -2.27 80.80
REMARK 500 ASP A 546 52.23 -152.15
REMARK 500 ASP A 564 -106.34 -1.10
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 1BQ A 1000
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4EBV RELATED DB: PDB
REMARK 900 RELATED ID: 4EBW RELATED DB: PDB
REMARK 900 RELATED ID: 4I4F RELATED DB: PDB
DBREF 4I4E A 411 686 UNP Q05397 FAK1_HUMAN 411 686
SEQADV 4I4E GLY A 406 UNP Q05397 EXPRESSION TAG
SEQADV 4I4E ALA A 407 UNP Q05397 EXPRESSION TAG
SEQADV 4I4E MET A 408 UNP Q05397 EXPRESSION TAG
SEQADV 4I4E GLY A 409 UNP Q05397 EXPRESSION TAG
SEQADV 4I4E SER A 410 UNP Q05397 EXPRESSION TAG
SEQRES 1 A 281 GLY ALA MET GLY SER SER THR ARG ASP TYR GLU ILE GLN
SEQRES 2 A 281 ARG GLU ARG ILE GLU LEU GLY ARG CYS ILE GLY GLU GLY
SEQRES 3 A 281 GLN PHE GLY ASP VAL HIS GLN GLY ILE TYR MET SER PRO
SEQRES 4 A 281 GLU ASN PRO ALA LEU ALA VAL ALA ILE LYS THR CYS LYS
SEQRES 5 A 281 ASN CYS THR SER ASP SER VAL ARG GLU LYS PHE LEU GLN
SEQRES 6 A 281 GLU ALA LEU THR MET ARG GLN PHE ASP HIS PRO HIS ILE
SEQRES 7 A 281 VAL LYS LEU ILE GLY VAL ILE THR GLU ASN PRO VAL TRP
SEQRES 8 A 281 ILE ILE MET GLU LEU CYS THR LEU GLY GLU LEU ARG SER
SEQRES 9 A 281 PHE LEU GLN VAL ARG LYS TYR SER LEU ASP LEU ALA SER
SEQRES 10 A 281 LEU ILE LEU TYR ALA TYR GLN LEU SER THR ALA LEU ALA
SEQRES 11 A 281 TYR LEU GLU SER LYS ARG PHE VAL HIS ARG ASP ILE ALA
SEQRES 12 A 281 ALA ARG ASN VAL LEU VAL SER SER ASN ASP CYS VAL LYS
SEQRES 13 A 281 LEU GLY ASP PHE GLY LEU SER ARG TYR MET GLU ASP SER
SEQRES 14 A 281 THR TYR TYR LYS ALA SER LYS GLY LYS LEU PRO ILE LYS
SEQRES 15 A 281 TRP MET ALA PRO GLU SER ILE ASN PHE ARG ARG PHE THR
SEQRES 16 A 281 SER ALA SER ASP VAL TRP MET PHE GLY VAL CYS MET TRP
SEQRES 17 A 281 GLU ILE LEU MET HIS GLY VAL LYS PRO PHE GLN GLY VAL
SEQRES 18 A 281 LYS ASN ASN ASP VAL ILE GLY ARG ILE GLU ASN GLY GLU
SEQRES 19 A 281 ARG LEU PRO MET PRO PRO ASN CYS PRO PRO THR LEU TYR
SEQRES 20 A 281 SER LEU MET THR LYS CYS TRP ALA TYR ASP PRO SER ARG
SEQRES 21 A 281 ARG PRO ARG PHE THR GLU LEU LYS ALA GLN LEU SER THR
SEQRES 22 A 281 ILE LEU GLU GLU GLU LYS ALA GLN
HET 1BQ A1000 33
HETNAM 1BQ [4-(2-HYDROXYETHYL)PIPERIDIN-1-YL][4-(5-METHYL-4,4-
HETNAM 2 1BQ DIOXIDO-1,5-DIHYDROPYRAZOLO[4,3-C][2,1]BENZOTHIAZIN-8-
HETNAM 3 1BQ YL)PHENYL]METHANONE
FORMUL 2 1BQ C24 H26 N4 O4 S
FORMUL 3 HOH *295(H2 O)
HELIX 1 1 GLN A 418 GLU A 420 5 3
HELIX 2 2 SER A 461 LEU A 469 1 9
HELIX 3 3 LEU A 469 GLN A 477 1 9
HELIX 4 4 GLU A 506 ARG A 514 1 9
HELIX 5 5 ASP A 519 LYS A 540 1 22
HELIX 6 6 ALA A 548 ARG A 550 5 3
HELIX 7 7 PRO A 585 MET A 589 5 5
HELIX 8 8 ALA A 590 ARG A 597 1 8
HELIX 9 9 THR A 600 MET A 617 1 18
HELIX 10 10 LYS A 627 ASN A 629 5 3
HELIX 11 11 ASP A 630 ASN A 637 1 8
HELIX 12 12 PRO A 648 TRP A 659 1 12
HELIX 13 13 ASP A 662 ARG A 666 5 5
HELIX 14 14 ARG A 668 ALA A 685 1 18
SHEET 1 A 5 ILE A 422 GLU A 430 0
SHEET 2 A 5 ASP A 435 TYR A 441 -1 O VAL A 436 N ILE A 428
SHEET 3 A 5 LEU A 449 THR A 455 -1 O ILE A 453 N HIS A 437
SHEET 4 A 5 TRP A 496 GLU A 500 -1 O MET A 499 N ALA A 452
SHEET 5 A 5 LEU A 486 ILE A 490 -1 N GLY A 488 O ILE A 498
SHEET 1 B 2 VAL A 552 SER A 556 0
SHEET 2 B 2 CYS A 559 LEU A 562 -1 O LYS A 561 N LEU A 553
SSBOND 1 CYS A 456 CYS A 459 1555 1555 2.03
CISPEP 1 ASN A 493 PRO A 494 0 -4.17
SITE 1 AC1 13 ARG A 426 ILE A 428 VAL A 436 ALA A 452
SITE 2 AC1 13 LYS A 454 GLU A 500 CYS A 502 THR A 503
SITE 3 AC1 13 LEU A 504 GLY A 505 ARG A 514 LEU A 553
SITE 4 AC1 13 HOH A1187
CRYST1 45.584 47.339 62.686 90.00 98.99 90.00 P 1 21 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 0.021938 0.000000 0.003472 0.00000
SCALE2 0.000000 0.021124 0.000000 0.00000
SCALE3 0.000000 0.000000 0.016151 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
