HEADER HYDROLASE 21-NOV-16 5MGN
TITLE HUMAN SIRT6 IN COMPLEX WITH ACTIVATOR UBCS38
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: NAD-DEPENDENT PROTEIN DEACETYLASE SIRTUIN-6;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: REGULATORY PROTEIN SIR2 HOMOLOG 6,SIR2-LIKE PROTEIN 6;
COMPND 5 EC: 3.5.1.-;
COMPND 6 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: SIRT6, SIR2L6;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_VARIANT: ROSETTA2 (DE3) PLYSS;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET151-D-TOPO
KEYWDS 4-(PYRIDIN-3-YL)-5-((3-(TRIFLUOROMETHYL)PHENYL)SULFONYL)-4, 5-
KEYWDS 2 DIHYDROPYRROLO[1, 2-A]QUINOXALINE, DRUG, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR C.STEEGBORN,W.YOU,C.KAMBACH
REVDAT 3 17-JAN-24 5MGN 1 HETSYN
REVDAT 2 25-JAN-17 5MGN 1 JRNL
REVDAT 1 28-DEC-16 5MGN 0
JRNL AUTH W.YOU,D.ROTILI,T.M.LI,C.KAMBACH,M.MELESHIN,M.SCHUTKOWSKI,
JRNL AUTH 2 K.F.CHUA,A.MAI,C.STEEGBORN
JRNL TITL STRUCTURAL BASIS OF SIRTUIN 6 ACTIVATION BY SYNTHETIC SMALL
JRNL TITL 2 MOLECULES.
JRNL REF ANGEW. CHEM. INT. ED. ENGL. V. 56 1007 2017
JRNL REFN ESSN 1521-3773
JRNL PMID 27990725
JRNL DOI 10.1002/ANIE.201610082
REMARK 2
REMARK 2 RESOLUTION. 2.07 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0155
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.07
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 45.93
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 3 NUMBER OF REFLECTIONS : 40233
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) : 0.146
REMARK 3 R VALUE (WORKING SET) : 0.144
REMARK 3 FREE R VALUE : 0.192
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 2121
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) : 2.07
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.12
REMARK 3 REFLECTION IN BIN (WORKING SET) : 2918
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 98.09
REMARK 3 BIN R VALUE (WORKING SET) : 0.1820
REMARK 3 BIN FREE R VALUE SET COUNT : 161
REMARK 3 BIN FREE R VALUE : 0.2800
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 4309
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 159
REMARK 3 SOLVENT ATOMS : 88
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 31.89
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -9.79000
REMARK 3 B22 (A**2) : -9.79000
REMARK 3 B33 (A**2) : 19.58000
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): 0.029
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.029
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 : 0.963
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.942
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 4569 ; 0.024 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 4343 ; 0.000 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 6220 ; 2.410 ; 1.999
REMARK 3 BOND ANGLES OTHERS (DEGREES): 9979 ; 3.741 ; 3.002
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 553 ; 6.659 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 186 ;37.910 ;22.419
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 741 ;16.285 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 46 ;21.320 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 703 ; 0.227 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 4960 ; 0.012 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 1005 ; 0.020 ; 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): 2224 ; 3.326 ; 2.998
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 2223 ; 3.325 ; 2.998
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 2773 ; 4.451 ; 4.477
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): 2774 ; 4.451 ; 4.477
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 2345 ; 4.101 ; 3.397
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): 2343 ; 4.073 ; 3.393
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): 3444 ; 5.689 ; 4.951
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): 4738 ; 7.407 ;35.399
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): 4739 ; 7.407 ;35.406
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 TWIN DETAILS
REMARK 3 NUMBER OF TWIN DOMAINS : 2
REMARK 3 TWIN DOMAIN : 1
REMARK 3 TWIN OPERATOR : H, K, L
REMARK 3 TWIN FRACTION : 0.564
REMARK 3 TWIN DOMAIN : 2
REMARK 3 TWIN OPERATOR : K, H, -L
REMARK 3 TWIN FRACTION : 0.436
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : NULL
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 5MGN COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 22-NOV-16.
REMARK 100 THE DEPOSITION ID IS D_1200002417.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 28-JUN-16
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 5.7-6.2
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : BESSY
REMARK 200 BEAMLINE : 14.1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9184
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XDS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 42356
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.070
REMARK 200 RESOLUTION RANGE LOW (A) : 48.450
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.300
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 200 DATA REDUNDANCY : 11.30
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 8.7300
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.07
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.19
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.0
REMARK 200 DATA REDUNDANCY IN SHELL : 11.50
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: 5MF6
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 53.38
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.64
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.6 M (NH4)2SO4, 10% PEG 400, AND BIS
REMARK 280 -TRIS BUFFER PH 5.7, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE
REMARK 280 293.0K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 63
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,-Y,Z+1/2
REMARK 290 5555 Y,-X+Y,Z+1/2
REMARK 290 6555 X-Y,X,Z+1/2
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 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 72.67650
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 72.67650
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 72.67650
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 GLY A 7
REMARK 465 ILE A 8
REMARK 465 ASP A 9
REMARK 465 LYS A 170
REMARK 465 ALA A 171
REMARK 465 ARG A 172
REMARK 465 GLY A 173
REMARK 465 LEU A 174
REMARK 465 ARG A 175
REMARK 465 ALA A 176
REMARK 465 PRO A 299
REMARK 465 LYS A 300
REMARK 465 GLU A 301
REMARK 465 GLU A 302
REMARK 465 SER A 303
REMARK 465 PRO A 304
REMARK 465 THR A 305
REMARK 465 ARG A 306
REMARK 465 ILE A 307
REMARK 465 ASN A 308
REMARK 465 GLY B 7
REMARK 465 ILE B 8
REMARK 465 ASP B 9
REMARK 465 PRO B 10
REMARK 465 PHE B 11
REMARK 465 THR B 12
REMARK 465 ALA B 13
REMARK 465 ASP B 14
REMARK 465 LYS B 170
REMARK 465 ALA B 171
REMARK 465 ARG B 172
REMARK 465 GLY B 173
REMARK 465 LEU B 174
REMARK 465 ARG B 175
REMARK 465 ALA B 176
REMARK 465 LEU B 297
REMARK 465 GLU B 298
REMARK 465 PRO B 299
REMARK 465 LYS B 300
REMARK 465 GLU B 301
REMARK 465 GLU B 302
REMARK 465 SER B 303
REMARK 465 PRO B 304
REMARK 465 THR B 305
REMARK 465 ARG B 306
REMARK 465 ILE B 307
REMARK 465 ASN B 308
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 GLU A 180 CG CD OE1 OE2
REMARK 470 GLU A 189 CG CD OE1 OE2
REMARK 470 ARG A 231 CG CD NE CZ NH1 NH2
REMARK 470 GLU A 298 CG CD OE1 OE2
REMARK 470 LYS B 143 CG CD CE NZ
REMARK 470 ARG B 178 CG CD NE CZ NH1 NH2
REMARK 470 GLU B 180 CG CD OE1 OE2
REMARK 470 GLU B 189 CG CD OE1 OE2
REMARK 470 ARG B 231 CG CD NE CZ NH1 NH2
REMARK 470 ARG B 232 CG CD NE CZ NH1 NH2
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 ARG A 65 NE - CZ - NH2 ANGL. DEV. = 3.2 DEGREES
REMARK 500 ASP A 83 CB - CG - OD1 ANGL. DEV. = -6.2 DEGREES
REMARK 500 ASP A 83 CB - CG - OD2 ANGL. DEV. = 6.6 DEGREES
REMARK 500 ASP A 190 CB - CG - OD2 ANGL. DEV. = 5.8 DEGREES
REMARK 500 ARG A 291 NE - CZ - NH1 ANGL. DEV. = -3.7 DEGREES
REMARK 500 ARG B 126 NE - CZ - NH1 ANGL. DEV. = 3.6 DEGREES
REMARK 500 ARG B 280 NE - CZ - NH1 ANGL. DEV. = -3.0 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 ALA A 13 120.92 -33.68
REMARK 500 ARG B 178 23.94 42.16
REMARK 500 TRP B 188 -39.28 -37.14
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 402 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 141 SG
REMARK 620 2 CYS A 144 SG 110.0
REMARK 620 3 CYS A 166 SG 108.2 107.7
REMARK 620 4 CYS A 177 SG 106.4 123.6 99.9
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN B 402 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS B 141 SG
REMARK 620 2 CYS B 144 SG 120.8
REMARK 620 3 CYS B 166 SG 108.4 107.6
REMARK 620 4 CYS B 177 SG 104.5 115.1 98.2
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 AR6 A 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN A 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 403
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 404
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 405
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 406
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 407
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 408
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue 7N2 A 409
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue AR6 B 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN B 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 B 403
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 B 404
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 B 405
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 B 406
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO B 407
DBREF 5MGN A 8 308 UNP Q8N6T7 SIR6_HUMAN 8 308
DBREF 5MGN B 8 308 UNP Q8N6T7 SIR6_HUMAN 8 308
SEQADV 5MGN GLY A 7 UNP Q8N6T7 EXPRESSION TAG
SEQADV 5MGN ILE A 8 UNP Q8N6T7 GLY 8 EXPRESSION TAG
SEQADV 5MGN ASP A 9 UNP Q8N6T7 LEU 9 EXPRESSION TAG
SEQADV 5MGN PRO A 10 UNP Q8N6T7 SER 10 EXPRESSION TAG
SEQADV 5MGN PHE A 11 UNP Q8N6T7 PRO 11 EXPRESSION TAG
SEQADV 5MGN THR A 12 UNP Q8N6T7 TYR 12 EXPRESSION TAG
SEQADV 5MGN GLY B 7 UNP Q8N6T7 EXPRESSION TAG
SEQADV 5MGN ILE B 8 UNP Q8N6T7 GLY 8 EXPRESSION TAG
SEQADV 5MGN ASP B 9 UNP Q8N6T7 LEU 9 EXPRESSION TAG
SEQADV 5MGN PRO B 10 UNP Q8N6T7 SER 10 EXPRESSION TAG
SEQADV 5MGN PHE B 11 UNP Q8N6T7 PRO 11 EXPRESSION TAG
SEQADV 5MGN THR B 12 UNP Q8N6T7 TYR 12 EXPRESSION TAG
SEQRES 1 A 302 GLY ILE ASP PRO PHE THR ALA ASP LYS GLY LYS CYS GLY
SEQRES 2 A 302 LEU PRO GLU ILE PHE ASP PRO PRO GLU GLU LEU GLU ARG
SEQRES 3 A 302 LYS VAL TRP GLU LEU ALA ARG LEU VAL TRP GLN SER SER
SEQRES 4 A 302 SER VAL VAL PHE HIS THR GLY ALA GLY ILE SER THR ALA
SEQRES 5 A 302 SER GLY ILE PRO ASP PHE ARG GLY PRO HIS GLY VAL TRP
SEQRES 6 A 302 THR MET GLU GLU ARG GLY LEU ALA PRO LYS PHE ASP THR
SEQRES 7 A 302 THR PHE GLU SER ALA ARG PRO THR GLN THR HIS MET ALA
SEQRES 8 A 302 LEU VAL GLN LEU GLU ARG VAL GLY LEU LEU ARG PHE LEU
SEQRES 9 A 302 VAL SER GLN ASN VAL ASP GLY LEU HIS VAL ARG SER GLY
SEQRES 10 A 302 PHE PRO ARG ASP LYS LEU ALA GLU LEU HIS GLY ASN MET
SEQRES 11 A 302 PHE VAL GLU GLU CYS ALA LYS CYS LYS THR GLN TYR VAL
SEQRES 12 A 302 ARG ASP THR VAL VAL GLY THR MET GLY LEU LYS ALA THR
SEQRES 13 A 302 GLY ARG LEU CYS THR VAL ALA LYS ALA ARG GLY LEU ARG
SEQRES 14 A 302 ALA CYS ARG GLY GLU LEU ARG ASP THR ILE LEU ASP TRP
SEQRES 15 A 302 GLU ASP SER LEU PRO ASP ARG ASP LEU ALA LEU ALA ASP
SEQRES 16 A 302 GLU ALA SER ARG ASN ALA ASP LEU SER ILE THR LEU GLY
SEQRES 17 A 302 THR SER LEU GLN ILE ARG PRO SER GLY ASN LEU PRO LEU
SEQRES 18 A 302 ALA THR LYS ARG ARG GLY GLY ARG LEU VAL ILE VAL ASN
SEQRES 19 A 302 LEU GLN PRO THR LYS HIS ASP ARG HIS ALA ASP LEU ARG
SEQRES 20 A 302 ILE HIS GLY TYR VAL ASP GLU VAL MET THR ARG LEU MET
SEQRES 21 A 302 LYS HIS LEU GLY LEU GLU ILE PRO ALA TRP ASP GLY PRO
SEQRES 22 A 302 ARG VAL LEU GLU ARG ALA LEU PRO PRO LEU PRO ARG PRO
SEQRES 23 A 302 PRO THR PRO LYS LEU GLU PRO LYS GLU GLU SER PRO THR
SEQRES 24 A 302 ARG ILE ASN
SEQRES 1 B 302 GLY ILE ASP PRO PHE THR ALA ASP LYS GLY LYS CYS GLY
SEQRES 2 B 302 LEU PRO GLU ILE PHE ASP PRO PRO GLU GLU LEU GLU ARG
SEQRES 3 B 302 LYS VAL TRP GLU LEU ALA ARG LEU VAL TRP GLN SER SER
SEQRES 4 B 302 SER VAL VAL PHE HIS THR GLY ALA GLY ILE SER THR ALA
SEQRES 5 B 302 SER GLY ILE PRO ASP PHE ARG GLY PRO HIS GLY VAL TRP
SEQRES 6 B 302 THR MET GLU GLU ARG GLY LEU ALA PRO LYS PHE ASP THR
SEQRES 7 B 302 THR PHE GLU SER ALA ARG PRO THR GLN THR HIS MET ALA
SEQRES 8 B 302 LEU VAL GLN LEU GLU ARG VAL GLY LEU LEU ARG PHE LEU
SEQRES 9 B 302 VAL SER GLN ASN VAL ASP GLY LEU HIS VAL ARG SER GLY
SEQRES 10 B 302 PHE PRO ARG ASP LYS LEU ALA GLU LEU HIS GLY ASN MET
SEQRES 11 B 302 PHE VAL GLU GLU CYS ALA LYS CYS LYS THR GLN TYR VAL
SEQRES 12 B 302 ARG ASP THR VAL VAL GLY THR MET GLY LEU LYS ALA THR
SEQRES 13 B 302 GLY ARG LEU CYS THR VAL ALA LYS ALA ARG GLY LEU ARG
SEQRES 14 B 302 ALA CYS ARG GLY GLU LEU ARG ASP THR ILE LEU ASP TRP
SEQRES 15 B 302 GLU ASP SER LEU PRO ASP ARG ASP LEU ALA LEU ALA ASP
SEQRES 16 B 302 GLU ALA SER ARG ASN ALA ASP LEU SER ILE THR LEU GLY
SEQRES 17 B 302 THR SER LEU GLN ILE ARG PRO SER GLY ASN LEU PRO LEU
SEQRES 18 B 302 ALA THR LYS ARG ARG GLY GLY ARG LEU VAL ILE VAL ASN
SEQRES 19 B 302 LEU GLN PRO THR LYS HIS ASP ARG HIS ALA ASP LEU ARG
SEQRES 20 B 302 ILE HIS GLY TYR VAL ASP GLU VAL MET THR ARG LEU MET
SEQRES 21 B 302 LYS HIS LEU GLY LEU GLU ILE PRO ALA TRP ASP GLY PRO
SEQRES 22 B 302 ARG VAL LEU GLU ARG ALA LEU PRO PRO LEU PRO ARG PRO
SEQRES 23 B 302 PRO THR PRO LYS LEU GLU PRO LYS GLU GLU SER PRO THR
SEQRES 24 B 302 ARG ILE ASN
HET AR6 A 401 36
HET ZN A 402 1
HET SO4 A 403 5
HET SO4 A 404 5
HET SO4 A 405 5
HET SO4 A 406 5
HET SO4 A 407 5
HET EDO A 408 4
HET 7N2 A 409 32
HET AR6 B 401 36
HET ZN B 402 1
HET SO4 B 403 5
HET SO4 B 404 5
HET SO4 B 405 5
HET SO4 B 406 5
HET EDO B 407 4
HETNAM AR6 [(2R,3S,4R,5R)-5-(6-AMINOPURIN-9-YL)-3,4-DIHYDROXY-
HETNAM 2 AR6 OXOLAN-2-YL]METHYL [HYDROXY-[[(2R,3S,4R,5S)-3,4,5-
HETNAM 3 AR6 TRIHYDROXYOXOLAN-2-YL]METHOXY]PHOSPHORYL] HYDROGEN
HETNAM 4 AR6 PHOSPHATE
HETNAM ZN ZINC ION
HETNAM SO4 SULFATE ION
HETNAM EDO 1,2-ETHANEDIOL
HETNAM 7N2 (4~{R})-4-PYRIDIN-3-YL-5-[3-(TRIFLUOROMETHYL)
HETNAM 2 7N2 PHENYL]SULFONYL-4~{H}-PYRROLO[1,2-A]QUINOXALINE
HETSYN AR6 ADENOSINE-5-DIPHOSPHORIBOSE
HETSYN EDO ETHYLENE GLYCOL
FORMUL 3 AR6 2(C15 H23 N5 O14 P2)
FORMUL 4 ZN 2(ZN 2+)
FORMUL 5 SO4 9(O4 S 2-)
FORMUL 10 EDO 2(C2 H6 O2)
FORMUL 11 7N2 C23 H16 F3 N3 O2 S
FORMUL 19 HOH *88(H2 O)
HELIX 1 AA1 PRO A 26 SER A 44 1 19
HELIX 2 AA2 ALA A 53 GLY A 60 5 8
HELIX 3 AA3 GLY A 69 ARG A 76 1 8
HELIX 4 AA4 THR A 92 VAL A 104 1 13
HELIX 5 AA5 GLY A 117 SER A 122 1 6
HELIX 6 AA6 PRO A 125 ASP A 127 5 3
HELIX 7 AA7 PRO A 193 ALA A 207 1 15
HELIX 8 AA8 PRO A 221 GLY A 223 5 3
HELIX 9 AA9 ASN A 224 ARG A 231 1 8
HELIX 10 AB1 ARG A 232 GLY A 234 5 3
HELIX 11 AB2 HIS A 246 ALA A 250 5 5
HELIX 12 AB3 TYR A 257 GLY A 270 1 14
HELIX 13 AB4 PRO B 26 SER B 44 1 19
HELIX 14 AB5 ALA B 53 GLY B 60 5 8
HELIX 15 AB6 GLY B 69 ARG B 76 1 8
HELIX 16 AB7 THR B 92 VAL B 104 1 13
HELIX 17 AB8 GLY B 117 ARG B 121 1 5
HELIX 18 AB9 PRO B 193 ALA B 207 1 15
HELIX 19 AC1 PRO B 221 GLY B 223 5 3
HELIX 20 AC2 ASN B 224 ARG B 231 1 8
HELIX 21 AC3 HIS B 246 ALA B 250 5 5
HELIX 22 AC4 TYR B 257 GLY B 270 1 14
SHEET 1 AA1 6 LEU A 129 GLU A 131 0
SHEET 2 AA1 6 PHE A 109 SER A 112 1 N LEU A 110 O ALA A 130
SHEET 3 AA1 6 VAL A 47 THR A 51 1 N PHE A 49 O VAL A 111
SHEET 4 AA1 6 LEU A 209 LEU A 213 1 O LEU A 213 N HIS A 50
SHEET 5 AA1 6 ARG A 235 VAL A 239 1 O VAL A 237 N THR A 212
SHEET 6 AA1 6 LEU A 252 ILE A 254 1 O LEU A 252 N ILE A 238
SHEET 1 AA2 4 GLN A 147 VAL A 149 0
SHEET 2 AA2 4 VAL A 138 CYS A 141 -1 N GLU A 139 O TYR A 148
SHEET 3 AA2 4 GLU A 180 ASP A 183 -1 O ARG A 182 N GLU A 140
SHEET 4 AA2 4 ALA A 161 LEU A 165 -1 N THR A 162 O LEU A 181
SHEET 1 AA3 6 LEU B 129 GLU B 131 0
SHEET 2 AA3 6 PHE B 109 SER B 112 1 N SER B 112 O ALA B 130
SHEET 3 AA3 6 VAL B 47 THR B 51 1 N PHE B 49 O VAL B 111
SHEET 4 AA3 6 LEU B 209 LEU B 213 1 O LEU B 209 N VAL B 48
SHEET 5 AA3 6 ARG B 235 VAL B 239 1 O VAL B 237 N THR B 212
SHEET 6 AA3 6 LEU B 252 ILE B 254 1 O LEU B 252 N ILE B 238
SHEET 1 AA4 2 SER B 122 PRO B 125 0
SHEET 2 AA4 2 ARG B 280 LEU B 282 1 N ARG B 280 O GLY B 123
SHEET 1 AA5 4 GLN B 147 VAL B 149 0
SHEET 2 AA5 4 VAL B 138 CYS B 141 -1 N GLU B 139 O TYR B 148
SHEET 3 AA5 4 GLU B 180 ASP B 183 -1 O ARG B 182 N GLU B 140
SHEET 4 AA5 4 ALA B 161 LEU B 165 -1 N ARG B 164 O LEU B 181
LINK SG CYS A 141 ZN ZN A 402 1555 1555 2.25
LINK SG CYS A 144 ZN ZN A 402 1555 1555 2.24
LINK SG CYS A 166 ZN ZN A 402 1555 1555 2.33
LINK SG CYS A 177 ZN ZN A 402 1555 1555 2.35
LINK SG CYS B 141 ZN ZN B 402 1555 1555 2.26
LINK SG CYS B 144 ZN ZN B 402 1555 1555 2.29
LINK SG CYS B 166 ZN ZN B 402 1555 1555 2.37
LINK SG CYS B 177 ZN ZN B 402 1555 1555 2.40
CISPEP 1 ARG A 220 PRO A 221 0 7.22
CISPEP 2 ARG B 220 PRO B 221 0 5.70
SITE 1 AC1 25 GLY A 52 ALA A 53 GLY A 54 THR A 57
SITE 2 AC1 25 ASP A 63 PHE A 64 ARG A 65 TRP A 71
SITE 3 AC1 25 GLN A 113 HIS A 133 GLY A 214 THR A 215
SITE 4 AC1 25 SER A 216 ILE A 219 ASN A 240 LEU A 241
SITE 5 AC1 25 GLN A 242 GLY A 256 TYR A 257 VAL A 258
SITE 6 AC1 25 HOH A 507 HOH A 510 HOH A 525 HOH A 538
SITE 7 AC1 25 ASP B 83
SITE 1 AC2 4 CYS A 141 CYS A 144 CYS A 166 CYS A 177
SITE 1 AC3 7 ARG A 90 ALA A 275 TRP A 276 HOH A 505
SITE 2 AC3 7 ARG B 90 ALA B 275 TRP B 276
SITE 1 AC4 4 VAL A 154 GLY A 155 ARG A 164 LYS A 296
SITE 1 AC5 3 LYS A 33 ARG A 253 HIS A 255
SITE 1 AC6 3 ARG A 220 PRO A 221 ASN A 224
SITE 1 AC7 3 ARG A 205 ARG A 232 ARG B 205
SITE 1 AC8 1 ASP A 187
SITE 1 AC9 10 LYS A 15 ILE A 61 PRO A 62 PHE A 64
SITE 2 AC9 10 VAL A 70 TRP A 71 PHE A 86 MET A 136
SITE 3 AC9 10 MET A 157 TRP A 188
SITE 1 AD1 25 ASP A 83 GLY B 52 ALA B 53 GLY B 54
SITE 2 AD1 25 THR B 57 ASP B 63 PHE B 64 ARG B 65
SITE 3 AD1 25 GLN B 113 HIS B 133 TRP B 188 GLY B 214
SITE 4 AD1 25 THR B 215 SER B 216 ILE B 219 ASN B 240
SITE 5 AD1 25 LEU B 241 GLN B 242 GLY B 256 TYR B 257
SITE 6 AD1 25 VAL B 258 HOH B 504 HOH B 506 HOH B 516
SITE 7 AD1 25 HOH B 530
SITE 1 AD2 4 CYS B 141 CYS B 144 CYS B 166 CYS B 177
SITE 1 AD3 4 HIS A 68 LYS A 81 HIS B 68 LYS B 81
SITE 1 AD4 3 LYS B 33 ARG B 253 HIS B 255
SITE 1 AD5 5 VAL B 154 GLY B 155 THR B 162 ARG B 164
SITE 2 AD5 5 LYS B 296
SITE 1 AD6 3 ARG B 220 PRO B 221 ASN B 224
SITE 1 AD7 3 PHE A 82 TYR B 257 HOH B 509
CRYST1 91.868 91.868 145.353 90.00 90.00 120.00 P 63 12
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 0.010885 0.006285 0.000000 0.00000
SCALE2 0.000000 0.012569 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006880 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
