HEADER TRANSPORT PROTEIN/INHIBITOR 03-SEP-15 5AYT
TITLE CRYSTAL STRUCTURE OF TRANSTHYRETIN IN COMPLEX WITH L6
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: TRANSTHYRETIN;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: ATTR,PREALBUMIN,TBPA;
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: TTR, PALB;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS AMYLOIDOGENIC PROTEIN, INHIBITOR, STABILIZER, DRUG DISCOVERY,
KEYWDS 2 TRANSPORT PROTEIN-INHIBITOR COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR T.YOKOYAMA,M.MIZUGUCHI,H.KAI
REVDAT 3 20-MAR-24 5AYT 1 REMARK
REVDAT 2 26-FEB-20 5AYT 1 REMARK
REVDAT 1 20-JAN-16 5AYT 0
JRNL AUTH T.YOKOYAMA,S.TAKAKI,K.CHOSA,T.SATO,M.A.SUICO,Y.TERANISHI,
JRNL AUTH 2 T.SHUTO,M.MIZUGUCHI,H.KAI
JRNL TITL STRUCTURAL STABILIZATION OF TRANSTHYRETIN BY A NEW COMPOUND,
JRNL TITL 2 6-BENZOYL-2-HYDROXY-1H-BENZO[DE]ISOQUINOLINE-1,3(2H)-DIONE
JRNL REF J. PHARMACOL. SCI. V. 129 240 2015
JRNL REFN ISSN 1347-8648
JRNL PMID 26639444
JRNL DOI 10.1016/J.JPHS.2015.09.006
REMARK 2
REMARK 2 RESOLUTION. 1.40 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.7.0029
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) : 1.40
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 36.25
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 96.1
REMARK 3 NUMBER OF REFLECTIONS : 44414
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) : 0.190
REMARK 3 R VALUE (WORKING SET) : 0.189
REMARK 3 FREE R VALUE : 0.209
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 2364
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) : 1.40
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.43
REMARK 3 REFLECTION IN BIN (WORKING SET) : 3026
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 89.45
REMARK 3 BIN R VALUE (WORKING SET) : 0.3240
REMARK 3 BIN FREE R VALUE SET COUNT : 135
REMARK 3 BIN FREE R VALUE : 0.3530
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 1778
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 48
REMARK 3 SOLVENT ATOMS : 244
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 20.65
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.01000
REMARK 3 B22 (A**2) : -0.31000
REMARK 3 B33 (A**2) : 0.33000
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): 0.066
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.066
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.045
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 1.163
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.966
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.964
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 1918 ; 0.014 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 2633 ; 1.667 ; 1.977
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 240 ; 6.260 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 77 ;30.733 ;23.636
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 289 ;12.975 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 8 ;16.108 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 295 ; 0.123 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 1473 ; 0.010 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
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 : NULL
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 : 1.20
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 5AYT COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 08-SEP-15.
REMARK 100 THE DEPOSITION ID IS D_1300000216.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 18-MAY-14
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.0
REMARK 200 NUMBER OF CRYSTALS USED : NULL
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : PHOTON FACTORY
REMARK 200 BEAMLINE : AR-NW12A
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 210
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 46782
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.400
REMARK 200 RESOLUTION RANGE LOW (A) : 36.250
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 96.2
REMARK 200 DATA REDUNDANCY : 4.400
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 27.4000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
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: NULL
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 29.41
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.74
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 18% POLYETHYLENE GLYCOL 400, 0.1 M
REMARK 280 HEPES-NAOH, 0.2 M CACL2, 1 MM L6, PH 7.0, VAPOR DIFFUSION,
REMARK 280 HANGING DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z
REMARK 290 3555 -X+1/2,Y+1/2,-Z
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 0.00000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 21.78900
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 42.40700
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 21.78900
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 42.40700
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: TETRAMERIC
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 350 APPLY THE FOLLOWING TO CHAINS: A, B
REMARK 350 BIOMT1 2 -1.000000 0.000000 0.000000 -43.57800
REMARK 350 BIOMT2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 1.000000 0.00000
REMARK 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375 OAX L6Y B 201 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A 375 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A 435 LIES ON A SPECIAL POSITION.
REMARK 375 HOH B 369 LIES ON A SPECIAL POSITION.
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 -31
REMARK 465 ARG A -30
REMARK 465 GLY A -29
REMARK 465 SER A -28
REMARK 465 HIS A -27
REMARK 465 HIS A -26
REMARK 465 HIS A -25
REMARK 465 HIS A -24
REMARK 465 HIS A -23
REMARK 465 HIS A -22
REMARK 465 GLY A -21
REMARK 465 SER A -20
REMARK 465 MET A -19
REMARK 465 ALA A -18
REMARK 465 SER A -17
REMARK 465 HIS A -16
REMARK 465 ARG A -15
REMARK 465 LEU A -14
REMARK 465 LEU A -13
REMARK 465 LEU A -12
REMARK 465 LEU A -11
REMARK 465 CYS A -10
REMARK 465 LEU A -9
REMARK 465 ALA A -8
REMARK 465 GLY A -7
REMARK 465 LEU A -6
REMARK 465 VAL A -5
REMARK 465 PHE A -4
REMARK 465 VAL A -3
REMARK 465 SER A -2
REMARK 465 GLU A -1
REMARK 465 ALA A 0
REMARK 465 GLY A 1
REMARK 465 PRO A 2
REMARK 465 THR A 3
REMARK 465 GLY A 4
REMARK 465 THR A 5
REMARK 465 GLY A 6
REMARK 465 GLU A 7
REMARK 465 SER A 8
REMARK 465 LYS A 9
REMARK 465 PRO A 125
REMARK 465 LYS A 126
REMARK 465 GLU A 127
REMARK 465 MET B -31
REMARK 465 ARG B -30
REMARK 465 GLY B -29
REMARK 465 SER B -28
REMARK 465 HIS B -27
REMARK 465 HIS B -26
REMARK 465 HIS B -25
REMARK 465 HIS B -24
REMARK 465 HIS B -23
REMARK 465 HIS B -22
REMARK 465 GLY B -21
REMARK 465 SER B -20
REMARK 465 MET B -19
REMARK 465 ALA B -18
REMARK 465 SER B -17
REMARK 465 HIS B -16
REMARK 465 ARG B -15
REMARK 465 LEU B -14
REMARK 465 LEU B -13
REMARK 465 LEU B -12
REMARK 465 LEU B -11
REMARK 465 CYS B -10
REMARK 465 LEU B -9
REMARK 465 ALA B -8
REMARK 465 GLY B -7
REMARK 465 LEU B -6
REMARK 465 VAL B -5
REMARK 465 PHE B -4
REMARK 465 VAL B -3
REMARK 465 SER B -2
REMARK 465 GLU B -1
REMARK 465 ALA B 0
REMARK 465 GLY B 1
REMARK 465 PRO B 2
REMARK 465 THR B 3
REMARK 465 GLY B 4
REMARK 465 THR B 5
REMARK 465 GLY B 6
REMARK 465 GLU B 7
REMARK 465 SER B 8
REMARK 465 LYS B 9
REMARK 465 PRO B 125
REMARK 465 LYS B 126
REMARK 465 GLU B 127
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 PHE B 44 -50.45 -132.88
REMARK 500 PHE B 44 -6.13 -154.24
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 A 435 DISTANCE = 6.72 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue L6Y A 201
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue L6Y B 201
DBREF 5AYT A -19 127 UNP P02766 TTHY_HUMAN 1 147
DBREF 5AYT B -19 127 UNP P02766 TTHY_HUMAN 1 147
SEQADV 5AYT MET A -31 UNP P02766 EXPRESSION TAG
SEQADV 5AYT ARG A -30 UNP P02766 EXPRESSION TAG
SEQADV 5AYT GLY A -29 UNP P02766 EXPRESSION TAG
SEQADV 5AYT SER A -28 UNP P02766 EXPRESSION TAG
SEQADV 5AYT HIS A -27 UNP P02766 EXPRESSION TAG
SEQADV 5AYT HIS A -26 UNP P02766 EXPRESSION TAG
SEQADV 5AYT HIS A -25 UNP P02766 EXPRESSION TAG
SEQADV 5AYT HIS A -24 UNP P02766 EXPRESSION TAG
SEQADV 5AYT HIS A -23 UNP P02766 EXPRESSION TAG
SEQADV 5AYT HIS A -22 UNP P02766 EXPRESSION TAG
SEQADV 5AYT GLY A -21 UNP P02766 EXPRESSION TAG
SEQADV 5AYT SER A -20 UNP P02766 EXPRESSION TAG
SEQADV 5AYT MET B -31 UNP P02766 EXPRESSION TAG
SEQADV 5AYT ARG B -30 UNP P02766 EXPRESSION TAG
SEQADV 5AYT GLY B -29 UNP P02766 EXPRESSION TAG
SEQADV 5AYT SER B -28 UNP P02766 EXPRESSION TAG
SEQADV 5AYT HIS B -27 UNP P02766 EXPRESSION TAG
SEQADV 5AYT HIS B -26 UNP P02766 EXPRESSION TAG
SEQADV 5AYT HIS B -25 UNP P02766 EXPRESSION TAG
SEQADV 5AYT HIS B -24 UNP P02766 EXPRESSION TAG
SEQADV 5AYT HIS B -23 UNP P02766 EXPRESSION TAG
SEQADV 5AYT HIS B -22 UNP P02766 EXPRESSION TAG
SEQADV 5AYT GLY B -21 UNP P02766 EXPRESSION TAG
SEQADV 5AYT SER B -20 UNP P02766 EXPRESSION TAG
SEQRES 1 A 159 MET ARG GLY SER HIS HIS HIS HIS HIS HIS GLY SER MET
SEQRES 2 A 159 ALA SER HIS ARG LEU LEU LEU LEU CYS LEU ALA GLY LEU
SEQRES 3 A 159 VAL PHE VAL SER GLU ALA GLY PRO THR GLY THR GLY GLU
SEQRES 4 A 159 SER LYS CYS PRO LEU MET VAL LYS VAL LEU ASP ALA VAL
SEQRES 5 A 159 ARG GLY SER PRO ALA ILE ASN VAL ALA VAL HIS VAL PHE
SEQRES 6 A 159 ARG LYS ALA ALA ASP ASP THR TRP GLU PRO PHE ALA SER
SEQRES 7 A 159 GLY LYS THR SER GLU SER GLY GLU LEU HIS GLY LEU THR
SEQRES 8 A 159 THR GLU GLU GLU PHE VAL GLU GLY ILE TYR LYS VAL GLU
SEQRES 9 A 159 ILE ASP THR LYS SER TYR TRP LYS ALA LEU GLY ILE SER
SEQRES 10 A 159 PRO PHE HIS GLU HIS ALA GLU VAL VAL PHE THR ALA ASN
SEQRES 11 A 159 ASP SER GLY PRO ARG ARG TYR THR ILE ALA ALA LEU LEU
SEQRES 12 A 159 SER PRO TYR SER TYR SER THR THR ALA VAL VAL THR ASN
SEQRES 13 A 159 PRO LYS GLU
SEQRES 1 B 159 MET ARG GLY SER HIS HIS HIS HIS HIS HIS GLY SER MET
SEQRES 2 B 159 ALA SER HIS ARG LEU LEU LEU LEU CYS LEU ALA GLY LEU
SEQRES 3 B 159 VAL PHE VAL SER GLU ALA GLY PRO THR GLY THR GLY GLU
SEQRES 4 B 159 SER LYS CYS PRO LEU MET VAL LYS VAL LEU ASP ALA VAL
SEQRES 5 B 159 ARG GLY SER PRO ALA ILE ASN VAL ALA VAL HIS VAL PHE
SEQRES 6 B 159 ARG LYS ALA ALA ASP ASP THR TRP GLU PRO PHE ALA SER
SEQRES 7 B 159 GLY LYS THR SER GLU SER GLY GLU LEU HIS GLY LEU THR
SEQRES 8 B 159 THR GLU GLU GLU PHE VAL GLU GLY ILE TYR LYS VAL GLU
SEQRES 9 B 159 ILE ASP THR LYS SER TYR TRP LYS ALA LEU GLY ILE SER
SEQRES 10 B 159 PRO PHE HIS GLU HIS ALA GLU VAL VAL PHE THR ALA ASN
SEQRES 11 B 159 ASP SER GLY PRO ARG ARG TYR THR ILE ALA ALA LEU LEU
SEQRES 12 B 159 SER PRO TYR SER TYR SER THR THR ALA VAL VAL THR ASN
SEQRES 13 B 159 PRO LYS GLU
HET L6Y A 201 24
HET L6Y B 201 24
HETNAM L6Y 2-OXIDANYL-6-(PHENYLCARBONYL)BENZO[DE]ISOQUINOLINE-1,3-
HETNAM 2 L6Y DIONE
FORMUL 3 L6Y 2(C19 H11 N O4)
FORMUL 5 HOH *244(H2 O)
HELIX 1 AA1 ASP A 74 LEU A 82 1 9
HELIX 2 AA2 ASP B 74 LEU B 82 1 9
SHEET 1 AA1 8 SER A 23 PRO A 24 0
SHEET 2 AA1 8 LEU A 12 ASP A 18 -1 N ASP A 18 O SER A 23
SHEET 3 AA1 8 ARG A 104 SER A 112 1 O LEU A 111 N LEU A 17
SHEET 4 AA1 8 SER A 115 THR A 123 -1 O THR A 123 N ARG A 104
SHEET 5 AA1 8 SER B 115 THR B 123 -1 O TYR B 116 N THR A 118
SHEET 6 AA1 8 ARG B 104 SER B 112 -1 N THR B 106 O VAL B 121
SHEET 7 AA1 8 LEU B 12 ASP B 18 1 N LEU B 17 O LEU B 111
SHEET 8 AA1 8 SER B 23 PRO B 24 -1 O SER B 23 N ASP B 18
SHEET 1 AA2 8 GLU A 54 LEU A 55 0
SHEET 2 AA2 8 LEU A 12 ASP A 18 -1 N VAL A 14 O LEU A 55
SHEET 3 AA2 8 ARG A 104 SER A 112 1 O LEU A 111 N LEU A 17
SHEET 4 AA2 8 SER A 115 THR A 123 -1 O THR A 123 N ARG A 104
SHEET 5 AA2 8 SER B 115 THR B 123 -1 O TYR B 116 N THR A 118
SHEET 6 AA2 8 ARG B 104 SER B 112 -1 N THR B 106 O VAL B 121
SHEET 7 AA2 8 LEU B 12 ASP B 18 1 N LEU B 17 O LEU B 111
SHEET 8 AA2 8 GLU B 54 LEU B 55 -1 O LEU B 55 N VAL B 14
SHEET 1 AA3 4 TRP A 41 LYS A 48 0
SHEET 2 AA3 4 ALA A 29 LYS A 35 -1 N VAL A 32 O ALA A 45
SHEET 3 AA3 4 GLY A 67 ILE A 73 -1 O GLU A 72 N HIS A 31
SHEET 4 AA3 4 ALA A 91 ALA A 97 -1 O ALA A 91 N ILE A 73
SHEET 1 AA4 4 TRP B 41 LYS B 48 0
SHEET 2 AA4 4 ALA B 29 LYS B 35 -1 N VAL B 32 O ALA B 45
SHEET 3 AA4 4 GLY B 67 ILE B 73 -1 O GLU B 72 N HIS B 31
SHEET 4 AA4 4 ALA B 91 ALA B 97 -1 O ALA B 91 N ILE B 73
SITE 1 AC1 10 LYS A 15 LEU A 17 ALA A 108 LEU A 110
SITE 2 AC1 10 SER A 117 THR A 119 VAL A 121 HOH A 301
SITE 3 AC1 10 HOH A 315 HOH A 382
SITE 1 AC2 9 LYS B 15 LEU B 17 ALA B 108 LEU B 110
SITE 2 AC2 9 SER B 117 THR B 119 VAL B 121 HOH B 307
SITE 3 AC2 9 HOH B 349
CRYST1 43.578 84.814 65.291 90.00 90.00 90.00 P 21 21 2 8
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 0.022947 0.000000 0.000000 0.00000
SCALE2 0.000000 0.011791 0.000000 0.00000
SCALE3 0.000000 0.000000 0.015316 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
