HEADER HYDROLASE/HYDROLASE INHIBITOR 22-MAR-13 4JSR
TITLE CRYSTAL STRUCTURE OF HUMAN SIRT3 WITH ELT INHIBITOR 11C [N-{2-[1-(6-
TITLE 2 CARBAMOYLTHIENO[3,2-D]PYRIMIDIN-4-YL)PIPERIDIN-4-YL]ETHYL}-N'-
TITLE 3 ETHYLTHIOPHENE-2,5-DICARBOXAMIDE]
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: NAD-DEPENDENT PROTEIN DEACETYLASE SIRTUIN-3, MITOCHONDRIAL;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: UNP RESIDUES 118-399;
COMPND 5 SYNONYM: HSIRT3, REGULATORY PROTEIN SIR2 HOMOLOG 3, SIR2-LIKE PROTEIN
COMPND 6 3;
COMPND 7 EC: 3.5.1.-;
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: SIRT3, SIR2L3;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS DEACETYLASE, HYDROLASE-HYDROLASE INHIBITOR COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR H.DAI
REVDAT 3 28-FEB-24 4JSR 1 REMARK SEQADV LINK
REVDAT 2 03-JUL-13 4JSR 1 JRNL
REVDAT 1 24-APR-13 4JSR 0
JRNL AUTH J.S.DISCH,G.EVINDAR,C.H.CHIU,C.A.BLUM,H.DAI,L.JIN,E.SCHUMAN,
JRNL AUTH 2 K.E.LIND,S.L.BELYANSKAYA,J.DENG,F.COPPO,L.AQUILANI,
JRNL AUTH 3 T.L.GRAYBILL,J.W.CUOZZO,S.LAVU,C.MAO,G.P.VLASUK,R.B.PERNI
JRNL TITL DISCOVERY OF THIENO[3,2-D]PYRIMIDINE-6-CARBOXAMIDES AS
JRNL TITL 2 POTENT INHIBITORS OF SIRT1, SIRT2, AND SIRT3.
JRNL REF J.MED.CHEM. V. 56 3666 2013
JRNL REFN ISSN 0022-2623
JRNL PMID 23570514
JRNL DOI 10.1021/JM400204K
REMARK 2
REMARK 2 RESOLUTION. 1.70 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.5.0066
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) : 1.70
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 40.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 3 NUMBER OF REFLECTIONS : 38011
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) : 0.200
REMARK 3 R VALUE (WORKING SET) : 0.198
REMARK 3 FREE R VALUE : 0.228
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 2006
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) : 1.70
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.75
REMARK 3 REFLECTION IN BIN (WORKING SET) : 2777
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.28
REMARK 3 BIN R VALUE (WORKING SET) : 0.3140
REMARK 3 BIN FREE R VALUE SET COUNT : 136
REMARK 3 BIN FREE R VALUE : 0.3500
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2148
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 34
REMARK 3 SOLVENT ATOMS : 306
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 27.59
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.18000
REMARK 3 B22 (A**2) : 0.18000
REMARK 3 B33 (A**2) : -0.27000
REMARK 3 B12 (A**2) : 0.09000
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): 0.102
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.101
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): NULL
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): NULL
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.956
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.945
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 2245 ; 0.030 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 3059 ; 2.465 ; 2.000
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 273 ; 6.253 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 97 ;34.212 ;22.887
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 359 ;15.451 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 19 ;16.930 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 342 ; 0.191 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 1726 ; 0.014 ; 0.022
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): 1373 ; 1.567 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 2233 ; 2.468 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 872 ; 3.609 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 825 ; 5.392 ; 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 : 1.40
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 4JSR COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 05-APR-13.
REMARK 100 THE DEPOSITION ID IS D_1000078457.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : NULL
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8.0
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) : NULL
REMARK 200 MONOCHROMATOR : SI(111)
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 : 38011
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.700
REMARK 200 RESOLUTION RANGE LOW (A) : 40.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : NULL
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) : 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: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 57.51
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.89
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M TRIS PH 8.0, 20% PEG 4000 OR 20%
REMARK 280 PEG 6000, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 291.15K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 65
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+2/3
REMARK 290 3555 -X+Y,-X,Z+1/3
REMARK 290 4555 -X,-Y,Z+1/2
REMARK 290 5555 Y,-X+Y,Z+1/6
REMARK 290 6555 X-Y,X,Z+5/6
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 29.68667
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 14.84333
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 22.26500
REMARK 290 SMTRY1 5 0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 5 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 7.42167
REMARK 290 SMTRY1 6 0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 6 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 37.10833
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 SER A 115
REMARK 465 ASN A 116
REMARK 465 ALA A 117
REMARK 465 SER A 118
REMARK 465 ASP A 119
REMARK 465 LYS A 120
REMARK 465 ASP A 395
REMARK 465 GLY A 396
REMARK 465 PRO A 397
REMARK 465 ASP A 398
REMARK 465 LYS A 399
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 O HOH A 695 O HOH A 802 4665 2.07
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 RES CSSEQI ATM2 DEVIATION
REMARK 500 PHE A 185 CE1 PHE A 185 CZ 0.134
REMARK 500 PHE A 251 CZ PHE A 251 CE2 0.128
REMARK 500 CYS A 259 CB CYS A 259 SG -0.134
REMARK 500 TRP A 379 CG TRP A 379 CD1 0.088
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 PRO A 160 C - N - CA ANGL. DEV. = -9.3 DEGREES
REMARK 500 ARG A 269 NE - CZ - NH1 ANGL. DEV. = 3.7 DEGREES
REMARK 500 ARG A 269 NE - CZ - NH2 ANGL. DEV. = -4.7 DEGREES
REMARK 500 ARG A 340 NE - CZ - NH1 ANGL. DEV. = -4.0 DEGREES
REMARK 500 LEU A 347 CB - CG - CD2 ANGL. DEV. = 12.8 DEGREES
REMARK 500 LEU A 351 CB - CG - CD2 ANGL. DEV. = 11.5 DEGREES
REMARK 500
REMARK 500 REMARK: NULL
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 207 -169.61 -113.42
REMARK 500 ASP A 290 46.59 -81.03
REMARK 500 LEU A 304 -16.48 -49.99
REMARK 500
REMARK 500 REMARK: NULL
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A 401 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 256 SG
REMARK 620 2 CYS A 259 SG 109.3
REMARK 620 3 CYS A 280 SG 107.2 108.0
REMARK 620 4 CYS A 283 SG 96.7 117.5 116.9
REMARK 620 N 1 2 3
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 1NQ A 402
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4JT8 RELATED DB: PDB
REMARK 900 RELATED ID: 4JT9 RELATED DB: PDB
DBREF 4JSR A 118 399 UNP Q9NTG7 SIR3_HUMAN 118 399
SEQADV 4JSR SER A 115 UNP Q9NTG7 EXPRESSION TAG
SEQADV 4JSR ASN A 116 UNP Q9NTG7 EXPRESSION TAG
SEQADV 4JSR ALA A 117 UNP Q9NTG7 EXPRESSION TAG
SEQRES 1 A 285 SER ASN ALA SER ASP LYS GLY LYS LEU SER LEU GLN ASP
SEQRES 2 A 285 VAL ALA GLU LEU ILE ARG ALA ARG ALA CYS GLN ARG VAL
SEQRES 3 A 285 VAL VAL MET VAL GLY ALA GLY ILE SER THR PRO SER GLY
SEQRES 4 A 285 ILE PRO ASP PHE ARG SER PRO GLY SER GLY LEU TYR SER
SEQRES 5 A 285 ASN LEU GLN GLN TYR ASP LEU PRO TYR PRO GLU ALA ILE
SEQRES 6 A 285 PHE GLU LEU PRO PHE PHE PHE HIS ASN PRO LYS PRO PHE
SEQRES 7 A 285 PHE THR LEU ALA LYS GLU LEU TYR PRO GLY ASN TYR LYS
SEQRES 8 A 285 PRO ASN VAL THR HIS TYR PHE LEU ARG LEU LEU HIS ASP
SEQRES 9 A 285 LYS GLY LEU LEU LEU ARG LEU TYR THR GLN ASN ILE ASP
SEQRES 10 A 285 GLY LEU GLU ARG VAL SER GLY ILE PRO ALA SER LYS LEU
SEQRES 11 A 285 VAL GLU ALA HIS GLY THR PHE ALA SER ALA THR CYS THR
SEQRES 12 A 285 VAL CYS GLN ARG PRO PHE PRO GLY GLU ASP ILE ARG ALA
SEQRES 13 A 285 ASP VAL MET ALA ASP ARG VAL PRO ARG CYS PRO VAL CYS
SEQRES 14 A 285 THR GLY VAL VAL LYS PRO ASP ILE VAL PHE PHE GLY GLU
SEQRES 15 A 285 PRO LEU PRO GLN ARG PHE LEU LEU HIS VAL VAL ASP PHE
SEQRES 16 A 285 PRO MET ALA ASP LEU LEU LEU ILE LEU GLY THR SER LEU
SEQRES 17 A 285 GLU VAL GLU PRO PHE ALA SER LEU THR GLU ALA VAL ARG
SEQRES 18 A 285 SER SER VAL PRO ARG LEU LEU ILE ASN ARG ASP LEU VAL
SEQRES 19 A 285 GLY PRO LEU ALA TRP HIS PRO ARG SER ARG ASP VAL ALA
SEQRES 20 A 285 GLN LEU GLY ASP VAL VAL HIS GLY VAL GLU SER LEU VAL
SEQRES 21 A 285 GLU LEU LEU GLY TRP THR GLU GLU MET ARG ASP LEU VAL
SEQRES 22 A 285 GLN ARG GLU THR GLY LYS LEU ASP GLY PRO ASP LYS
HET ZN A 401 1
HET 1NQ A 402 33
HETNAM ZN ZINC ION
HETNAM 1NQ N-{2-[1-(6-CARBAMOYLTHIENO[3,2-D]PYRIMIDIN-4-YL)
HETNAM 2 1NQ PIPERIDIN-4-YL]ETHYL}-N'-ETHYLTHIOPHENE-2,5-
HETNAM 3 1NQ DICARBOXAMIDE
FORMUL 2 ZN ZN 2+
FORMUL 3 1NQ C22 H26 N6 O3 S2
FORMUL 4 HOH *306(H2 O)
HELIX 1 1 SER A 124 ALA A 134 1 11
HELIX 2 2 ALA A 146 GLY A 153 5 8
HELIX 3 3 GLY A 163 SER A 166 5 4
HELIX 4 4 ASN A 167 ASP A 172 1 6
HELIX 5 5 TYR A 175 PHE A 180 5 6
HELIX 6 6 GLU A 181 ASN A 188 1 8
HELIX 7 7 PRO A 189 TYR A 200 1 12
HELIX 8 8 ASN A 207 LYS A 219 1 13
HELIX 9 9 GLY A 232 SER A 237 1 6
HELIX 10 10 PRO A 240 SER A 242 5 3
HELIX 11 11 ILE A 268 ALA A 274 1 7
HELIX 12 12 PRO A 299 LEU A 303 5 5
HELIX 13 13 LEU A 304 PHE A 309 1 6
HELIX 14 14 PRO A 326 THR A 331 1 6
HELIX 15 15 GLY A 349 HIS A 354 1 6
HELIX 16 16 ASP A 365 GLY A 378 1 14
HELIX 17 17 TRP A 379 LEU A 394 1 16
SHEET 1 A 6 LEU A 244 GLU A 246 0
SHEET 2 A 6 LEU A 222 THR A 227 1 N THR A 227 O VAL A 245
SHEET 3 A 6 VAL A 140 VAL A 144 1 N VAL A 142 O TYR A 226
SHEET 4 A 6 LEU A 314 LEU A 318 1 O LEU A 316 N VAL A 141
SHEET 5 A 6 ARG A 340 ASN A 344 1 O ILE A 343 N ILE A 317
SHEET 6 A 6 ASP A 359 LEU A 363 1 O GLN A 362 N LEU A 342
SHEET 1 B 3 PRO A 262 PRO A 264 0
SHEET 2 B 3 GLY A 249 CYS A 256 -1 N ALA A 254 O PHE A 263
SHEET 3 B 3 VAL A 287 ILE A 291 -1 O ASP A 290 N SER A 253
LINK SG CYS A 256 ZN ZN A 401 1555 1555 2.32
LINK SG CYS A 259 ZN ZN A 401 1555 1555 2.32
LINK SG CYS A 280 ZN ZN A 401 1555 1555 2.26
LINK SG CYS A 283 ZN ZN A 401 1555 1555 2.34
CISPEP 1 GLY A 121 LYS A 122 0 10.22
CISPEP 2 GLU A 325 PRO A 326 0 8.01
SITE 1 AC1 4 CYS A 256 CYS A 259 CYS A 280 CYS A 283
SITE 1 AC2 18 ALA A 146 ILE A 154 ASP A 156 PHE A 157
SITE 2 AC2 18 PHE A 180 GLN A 228 ASN A 229 ILE A 230
SITE 3 AC2 18 ASP A 231 HIS A 248 VAL A 292 PHE A 293
SITE 4 AC2 18 PHE A 294 GLU A 296 HOH A 531 HOH A 621
SITE 5 AC2 18 HOH A 632 HOH A 640
CRYST1 119.320 119.320 44.530 90.00 90.00 120.00 P 65 6
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 0.008381 0.004839 0.000000 0.00000
SCALE2 0.000000 0.009677 0.000000 0.00000
SCALE3 0.000000 0.000000 0.022457 0.00000
(ATOM LINES ARE NOT SHOWN.)
END