HEADER TRANSFERASE 09-JUL-14 4QTU
TITLE STRUCTURE OF S. CEREVISIAE BUD23-TRM112 COMPLEX INVOLVED IN FORMATION
TITLE 2 OF M7G1575 ON 18S RRNA (SAM BOUND FORM)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: MULTIFUNCTIONAL METHYLTRANSFERASE SUBUNIT TRM112;
COMPND 3 CHAIN: A, C;
COMPND 4 SYNONYM: RRNA MTASE ACTIVATOR SUBUNIT, ERF1 METHYLTRANSFERASE SUBUNIT
COMPND 5 TRM112, ERF1 MTASE SUBUNIT TRM112, TRNA METHYLTRANSFERASE 112;
COMPND 6 ENGINEERED: YES;
COMPND 7 MOL_ID: 2;
COMPND 8 MOLECULE: PUTATIVE METHYLTRANSFERASE BUD23;
COMPND 9 CHAIN: B, D;
COMPND 10 FRAGMENT: FRAGMENT RESIDUES 1-202;
COMPND 11 SYNONYM: RRNA MTASE CATALYTIC SUBUNIT, BUD SITE SELECTION PROTEIN 23;
COMPND 12 EC: 2.1.1.-;
COMPND 13 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE S288C;
SOURCE 3 ORGANISM_COMMON: YEAST;
SOURCE 4 ORGANISM_TAXID: 559292;
SOURCE 5 GENE: N3445, TRM112, YNR046W;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 MOL_ID: 2;
SOURCE 9 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE S288C;
SOURCE 10 ORGANISM_COMMON: YEAST;
SOURCE 11 ORGANISM_TAXID: 559292;
SOURCE 12 GENE: BUD23, YCR047C, YCR47C;
SOURCE 13 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 14 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS CLASS I, METHYLTRANSFERASE, TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR J.LETOQUART,E.HUVELLE,L.WACHEUL,G.BOURGEOIS,C.ZORBAS,M.GRAILLE,
AUTHOR 2 V.HEURGUE-HAMARD,D.L.J.LAFONTAINE
REVDAT 5 06-DEC-23 4QTU 1 REMARK
REVDAT 4 08-NOV-23 4QTU 1 REMARK
REVDAT 3 24-AUG-22 4QTU 1 JRNL REMARK SEQADV LINK
REVDAT 2 03-JAN-18 4QTU 1 TITLE
REVDAT 1 24-DEC-14 4QTU 0
JRNL AUTH J.LETOQUART,E.HUVELLE,L.WACHEUL,G.BOURGEOIS,C.ZORBAS,
JRNL AUTH 2 M.GRAILLE,V.HEURGUE-HAMARD,D.L.LAFONTAINE
JRNL TITL STRUCTURAL AND FUNCTIONAL STUDIES OF BUD23-TRM112 REVEAL 18S
JRNL TITL 2 RRNA N7-G1575 METHYLATION OCCURS ON LATE 40S PRECURSOR
JRNL TITL 3 RIBOSOMES.
JRNL REF PROC.NATL.ACAD.SCI.USA V. 111 E5518 2014
JRNL REFN ESSN 1091-6490
JRNL PMID 25489090
JRNL DOI 10.1073/PNAS.1413089111
REMARK 2
REMARK 2 RESOLUTION. 2.12 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE: 1.8.4_1496)
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,
REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,
REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,
REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON,
REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,
REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT
REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.12
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 38.31
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.990
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.9
REMARK 3 NUMBER OF REFLECTIONS : 38373
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.181
REMARK 3 R VALUE (WORKING SET) : 0.178
REMARK 3 FREE R VALUE : 0.229
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 1917
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS).
REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE
REMARK 3 1 38.3136 - 5.1142 0.99 2712 142 0.1578 0.1971
REMARK 3 2 5.1142 - 4.0608 1.00 2658 140 0.1415 0.1990
REMARK 3 3 4.0608 - 3.5479 0.99 2624 139 0.1577 0.2019
REMARK 3 4 3.5479 - 3.2237 0.99 2640 138 0.1818 0.1954
REMARK 3 5 3.2237 - 2.9927 1.00 2613 138 0.1954 0.2225
REMARK 3 6 2.9927 - 2.8163 1.00 2612 137 0.1907 0.2906
REMARK 3 7 2.8163 - 2.6753 1.00 2646 140 0.1938 0.2714
REMARK 3 8 2.6753 - 2.5589 1.00 2594 136 0.1935 0.2300
REMARK 3 9 2.5589 - 2.4604 1.00 2624 138 0.1986 0.2623
REMARK 3 10 2.4604 - 2.3755 1.00 2597 137 0.1977 0.2915
REMARK 3 11 2.3755 - 2.3012 1.00 2637 139 0.2123 0.2764
REMARK 3 12 2.3012 - 2.2355 0.98 2526 131 0.2613 0.3125
REMARK 3 13 2.2355 - 2.1766 1.00 2635 139 0.2518 0.3302
REMARK 3 14 2.1766 - 2.1235 0.90 2338 123 0.2606 0.3334
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.11
REMARK 3 SHRINKAGE RADIUS : 0.90
REMARK 3 K_SOL : NULL
REMARK 3 B_SOL : NULL
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.270
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 24.880
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 37.10
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 44.88
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
REMARK 3
REMARK 3 TWINNING INFORMATION.
REMARK 3 FRACTION: NULL
REMARK 3 OPERATOR: NULL
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : 0.008 5165
REMARK 3 ANGLE : 1.110 6963
REMARK 3 CHIRALITY : 0.046 783
REMARK 3 PLANARITY : 0.005 893
REMARK 3 DIHEDRAL : 15.530 1913
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 4QTU COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 24-JUL-14.
REMARK 100 THE DEPOSITION ID IS D_1000086505.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 16-DEC-12
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 : SOLEIL
REMARK 200 BEAMLINE : PROXIMA 1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9801
REMARK 200 MONOCHROMATOR : CHANNEL CUT CRYOGENICALLY COOLED
REMARK 200 MONOCHROMATOR CRYSTAL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : PSI PILATUS 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XDS, XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 38373
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.124
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 94.7
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) : 2.20
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.33
REMARK 200 COMPLETENESS FOR SHELL (%) : 94.7
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: SHARP
REMARK 200 STARTING MODEL: 4QTT
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 45.54
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.26
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PH 7.5, VAPOR DIFFUSION, HANGING DROP,
REMARK 280 TEMPERATURE 291K
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 26.86650
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 2470 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 15270 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -13.0 KCAL/MOL
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
REMARK 350 BIOMOLECULE: 2
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: 2450 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 14480 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -13.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D
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 VAL A 135
REMARK 465 MET B 1
REMARK 465 SER B 2
REMARK 465 ARG B 3
REMARK 465 PRO B 4
REMARK 465 GLU B 5
REMARK 465 GLU B 6
REMARK 465 LEU B 7
REMARK 465 ALA B 8
REMARK 465 PRO B 9
REMARK 465 PRO B 10
REMARK 465 GLU B 11
REMARK 465 HIS B 203
REMARK 465 HIS B 204
REMARK 465 HIS B 205
REMARK 465 HIS B 206
REMARK 465 HIS B 207
REMARK 465 HIS B 208
REMARK 465 MET D 1
REMARK 465 SER D 2
REMARK 465 ARG D 3
REMARK 465 PRO D 4
REMARK 465 GLU D 5
REMARK 465 GLU D 6
REMARK 465 LEU D 7
REMARK 465 ALA D 8
REMARK 465 PRO D 9
REMARK 465 PRO D 10
REMARK 465 GLU D 11
REMARK 465 ILE D 12
REMARK 465 PHE D 13
REMARK 465 TYR D 14
REMARK 465 ASN D 15
REMARK 465 ASP D 16
REMARK 465 SER D 17
REMARK 465 ALA D 126
REMARK 465 ASP D 127
REMARK 465 THR D 128
REMARK 465 SER D 129
REMARK 465 TYR D 130
REMARK 465 ASN D 131
REMARK 465 HIS D 203
REMARK 465 HIS D 204
REMARK 465 HIS D 205
REMARK 465 HIS D 206
REMARK 465 HIS D 207
REMARK 465 HIS D 208
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 OD2 ASP C 37 OG SER C 39 2.15
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 PRO A 132 -38.57 -37.38
REMARK 500 PHE B 13 -46.74 -134.00
REMARK 500 CSO D 124 63.77 -111.62
REMARK 500 LYS D 161 -76.49 -94.59
REMARK 500 ASP D 186 53.27 35.67
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 201 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 11 SG
REMARK 620 2 CYS A 16 SG 111.4
REMARK 620 3 CYS A 112 SG 105.0 116.6
REMARK 620 4 CYS A 115 SG 111.8 105.0 107.1
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN C 201 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS C 11 SG
REMARK 620 2 CYS C 16 SG 115.8
REMARK 620 3 CYS C 112 SG 104.4 119.0
REMARK 620 4 CYS C 115 SG 104.9 102.9 109.0
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 201
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 202
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 203
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 204
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 205
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 206
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 207
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SAM B 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 303
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 304
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 305
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 306
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 307
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 308
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 309
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 310
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 311
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN C 201
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO C 202
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO C 203
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SAM D 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO D 302
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4QTM RELATED DB: PDB
REMARK 900 RELATED ID: 4QTT RELATED DB: PDB
DBREF 4QTU A 1 135 UNP P53738 TR112_YEAST 1 135
DBREF 4QTU B 1 202 UNP P25627 BUD23_YEAST 1 202
DBREF 4QTU C 1 135 UNP P53738 TR112_YEAST 1 135
DBREF 4QTU D 1 202 UNP P25627 BUD23_YEAST 1 202
SEQADV 4QTU HIS B 203 UNP P25627 EXPRESSION TAG
SEQADV 4QTU HIS B 204 UNP P25627 EXPRESSION TAG
SEQADV 4QTU HIS B 205 UNP P25627 EXPRESSION TAG
SEQADV 4QTU HIS B 206 UNP P25627 EXPRESSION TAG
SEQADV 4QTU HIS B 207 UNP P25627 EXPRESSION TAG
SEQADV 4QTU HIS B 208 UNP P25627 EXPRESSION TAG
SEQADV 4QTU HIS D 203 UNP P25627 EXPRESSION TAG
SEQADV 4QTU HIS D 204 UNP P25627 EXPRESSION TAG
SEQADV 4QTU HIS D 205 UNP P25627 EXPRESSION TAG
SEQADV 4QTU HIS D 206 UNP P25627 EXPRESSION TAG
SEQADV 4QTU HIS D 207 UNP P25627 EXPRESSION TAG
SEQADV 4QTU HIS D 208 UNP P25627 EXPRESSION TAG
SEQRES 1 A 135 MET LYS PHE LEU THR THR ASN PHE LEU LYS CYS SER VAL
SEQRES 2 A 135 LYS ALA CYS ASP THR SER ASN ASP ASN PHE PRO LEU GLN
SEQRES 3 A 135 TYR ASP GLY SER LYS CYS GLN LEU VAL GLN ASP GLU SER
SEQRES 4 A 135 ILE GLU PHE ASN PRO GLU PHE LEU LEU ASN ILE VAL ASP
SEQRES 5 A 135 ARG VAL ASP TRP PRO ALA VAL LEU THR VAL ALA ALA GLU
SEQRES 6 A 135 LEU GLY ASN ASN ALA LEU PRO PRO THR LYS PRO SER PHE
SEQRES 7 A 135 PRO SER SER ILE GLN GLU LEU THR ASP ASP ASP MET ALA
SEQRES 8 A 135 ILE LEU ASN ASP LEU HIS THR LEU LEU LEU GLN THR SER
SEQRES 9 A 135 ILE ALA GLU GLY GLU MET LYS CYS ARG ASN CYS GLY HIS
SEQRES 10 A 135 ILE TYR TYR ILE LYS ASN GLY ILE PRO ASN LEU LEU LEU
SEQRES 11 A 135 PRO PRO HIS LEU VAL
SEQRES 1 B 208 MET SER ARG PRO GLU GLU LEU ALA PRO PRO GLU ILE PHE
SEQRES 2 B 208 TYR ASN ASP SER GLU ALA HIS LYS TYR THR GLY SER THR
SEQRES 3 B 208 ARG VAL GLN HIS ILE GLN ALA LYS MET THR LEU ARG ALA
SEQRES 4 B 208 LEU GLU LEU LEU ASN LEU GLN PRO CYS SER PHE ILE LEU
SEQRES 5 B 208 ASP ILE GLY CYS GLY SER GLY LEU SER GLY GLU ILE LEU
SEQRES 6 B 208 THR GLN GLU GLY ASP HIS VAL TRP CYS GLY LEU ASP ILE
SEQRES 7 B 208 SER PRO SER MET LEU ALA THR GLY LEU SER ARG GLU LEU
SEQRES 8 B 208 GLU GLY ASP LEU MET LEU GLN ASP MET GLY THR GLY ILE
SEQRES 9 B 208 PRO PHE ARG ALA GLY SER PHE ASP ALA ALA ILE SER ILE
SEQRES 10 B 208 SER ALA ILE GLN TRP LEU CSO ASN ALA ASP THR SER TYR
SEQRES 11 B 208 ASN ASP PRO LYS GLN ARG LEU MET ARG PHE PHE ASN THR
SEQRES 12 B 208 LEU TYR ALA ALA LEU LYS LYS GLY GLY LYS PHE VAL ALA
SEQRES 13 B 208 GLN PHE TYR PRO LYS ASN ASP ASP GLN VAL ASP ASP ILE
SEQRES 14 B 208 LEU GLN SER ALA LYS VAL ALA GLY PHE SER GLY GLY LEU
SEQRES 15 B 208 VAL VAL ASP ASP PRO GLU SER LYS LYS ASN LYS LYS TYR
SEQRES 16 B 208 TYR LEU VAL LEU SER SER GLY HIS HIS HIS HIS HIS HIS
SEQRES 1 C 135 MET LYS PHE LEU THR THR ASN PHE LEU LYS CYS SER VAL
SEQRES 2 C 135 LYS ALA CYS ASP THR SER ASN ASP ASN PHE PRO LEU GLN
SEQRES 3 C 135 TYR ASP GLY SER LYS CYS GLN LEU VAL GLN ASP GLU SER
SEQRES 4 C 135 ILE GLU PHE ASN PRO GLU PHE LEU LEU ASN ILE VAL ASP
SEQRES 5 C 135 ARG VAL ASP TRP PRO ALA VAL LEU THR VAL ALA ALA GLU
SEQRES 6 C 135 LEU GLY ASN ASN ALA LEU PRO PRO THR LYS PRO SER PHE
SEQRES 7 C 135 PRO SER SER ILE GLN GLU LEU THR ASP ASP ASP MET ALA
SEQRES 8 C 135 ILE LEU ASN ASP LEU HIS THR LEU LEU LEU GLN THR SER
SEQRES 9 C 135 ILE ALA GLU GLY GLU MET LYS CYS ARG ASN CYS GLY HIS
SEQRES 10 C 135 ILE TYR TYR ILE LYS ASN GLY ILE PRO ASN LEU LEU LEU
SEQRES 11 C 135 PRO PRO HIS LEU VAL
SEQRES 1 D 208 MET SER ARG PRO GLU GLU LEU ALA PRO PRO GLU ILE PHE
SEQRES 2 D 208 TYR ASN ASP SER GLU ALA HIS LYS TYR THR GLY SER THR
SEQRES 3 D 208 ARG VAL GLN HIS ILE GLN ALA LYS MET THR LEU ARG ALA
SEQRES 4 D 208 LEU GLU LEU LEU ASN LEU GLN PRO CYS SER PHE ILE LEU
SEQRES 5 D 208 ASP ILE GLY CYS GLY SER GLY LEU SER GLY GLU ILE LEU
SEQRES 6 D 208 THR GLN GLU GLY ASP HIS VAL TRP CYS GLY LEU ASP ILE
SEQRES 7 D 208 SER PRO SER MET LEU ALA THR GLY LEU SER ARG GLU LEU
SEQRES 8 D 208 GLU GLY ASP LEU MET LEU GLN ASP MET GLY THR GLY ILE
SEQRES 9 D 208 PRO PHE ARG ALA GLY SER PHE ASP ALA ALA ILE SER ILE
SEQRES 10 D 208 SER ALA ILE GLN TRP LEU CSO ASN ALA ASP THR SER TYR
SEQRES 11 D 208 ASN ASP PRO LYS GLN ARG LEU MET ARG PHE PHE ASN THR
SEQRES 12 D 208 LEU TYR ALA ALA LEU LYS LYS GLY GLY LYS PHE VAL ALA
SEQRES 13 D 208 GLN PHE TYR PRO LYS ASN ASP ASP GLN VAL ASP ASP ILE
SEQRES 14 D 208 LEU GLN SER ALA LYS VAL ALA GLY PHE SER GLY GLY LEU
SEQRES 15 D 208 VAL VAL ASP ASP PRO GLU SER LYS LYS ASN LYS LYS TYR
SEQRES 16 D 208 TYR LEU VAL LEU SER SER GLY HIS HIS HIS HIS HIS HIS
MODRES 4QTU CSO B 124 CYS S-HYDROXYCYSTEINE
MODRES 4QTU CSO D 124 CYS S-HYDROXYCYSTEINE
HET CSO B 124 7
HET CSO D 124 7
HET ZN A 201 1
HET EDO A 202 4
HET EDO A 203 4
HET EDO A 204 4
HET EDO A 205 4
HET EDO A 206 4
HET EDO A 207 4
HET SAM B 301 27
HET EDO B 302 4
HET EDO B 303 4
HET EDO B 304 4
HET EDO B 305 4
HET EDO B 306 4
HET EDO B 307 4
HET EDO B 308 4
HET EDO B 309 4
HET EDO B 310 4
HET EDO B 311 4
HET ZN C 201 1
HET EDO C 202 4
HET EDO C 203 4
HET SAM D 301 27
HET EDO D 302 4
HETNAM CSO S-HYDROXYCYSTEINE
HETNAM ZN ZINC ION
HETNAM EDO 1,2-ETHANEDIOL
HETNAM SAM S-ADENOSYLMETHIONINE
HETSYN EDO ETHYLENE GLYCOL
FORMUL 2 CSO 2(C3 H7 N O3 S)
FORMUL 5 ZN 2(ZN 2+)
FORMUL 6 EDO 19(C2 H6 O2)
FORMUL 12 SAM 2(C15 H22 N6 O5 S)
FORMUL 28 HOH *173(H2 O)
HELIX 1 1 LYS A 2 ASN A 7 1 6
HELIX 2 2 VAL A 13 SER A 19 5 7
HELIX 3 3 ASN A 43 VAL A 51 1 9
HELIX 4 4 ASP A 52 VAL A 54 5 3
HELIX 5 5 ASP A 55 LEU A 66 1 12
HELIX 6 6 SER A 81 LEU A 85 5 5
HELIX 7 7 THR A 86 LEU A 101 1 16
HELIX 8 8 ASN B 15 SER B 25 1 11
HELIX 9 9 SER B 25 ASN B 44 1 20
HELIX 10 10 GLY B 59 ASP B 70 1 12
HELIX 11 11 SER B 79 LEU B 87 1 9
HELIX 12 12 ASP B 99 GLY B 103 5 5
HELIX 13 13 ALA B 119 ASN B 125 5 7
HELIX 14 14 ASP B 132 ALA B 147 1 16
HELIX 15 15 ASN B 162 GLY B 177 1 16
HELIX 16 16 LYS C 2 ASN C 7 1 6
HELIX 17 17 VAL C 13 ASP C 17 5 5
HELIX 18 18 ASN C 43 VAL C 51 1 9
HELIX 19 19 ASP C 55 LEU C 66 1 12
HELIX 20 20 SER C 81 LEU C 85 5 5
HELIX 21 21 THR C 86 LEU C 101 1 16
HELIX 22 22 ALA D 19 GLY D 24 1 6
HELIX 23 23 SER D 25 ASN D 44 1 20
HELIX 24 24 GLY D 59 ASP D 70 1 12
HELIX 25 25 SER D 79 SER D 88 1 10
HELIX 26 26 ASP D 99 GLY D 103 5 5
HELIX 27 27 ALA D 119 CSO D 124 5 6
HELIX 28 28 PRO D 133 ALA D 147 1 15
HELIX 29 29 ASN D 162 GLY D 177 1 16
SHEET 1 A 3 GLN A 26 TYR A 27 0
SHEET 2 A 3 THR A 103 LYS A 111 -1 O LYS A 111 N GLN A 26
SHEET 3 A 3 GLN A 33 GLN A 36 -1 N GLN A 33 O GLU A 107
SHEET 1 B 4 GLN A 26 TYR A 27 0
SHEET 2 B 4 THR A 103 LYS A 111 -1 O LYS A 111 N GLN A 26
SHEET 3 B 4 ILE A 118 LYS A 122 -1 O TYR A 119 N MET A 110
SHEET 4 B 4 ILE A 125 PRO A 126 -1 O ILE A 125 N LYS A 122
SHEET 1 C14 ASP B 94 LEU B 97 0
SHEET 2 C14 VAL B 72 ASP B 77 1 N GLY B 75 O ASP B 94
SHEET 3 C14 PHE B 50 ILE B 54 1 N ASP B 53 O CYS B 74
SHEET 4 C14 PHE B 111 ILE B 117 1 O ILE B 115 N ILE B 54
SHEET 5 C14 LEU B 148 PHE B 158 1 O LYS B 149 N PHE B 111
SHEET 6 C14 LYS B 194 SER B 200 -1 O LEU B 197 N ALA B 156
SHEET 7 C14 SER B 179 ASP B 185 -1 N VAL B 183 O TYR B 196
SHEET 8 C14 SER D 179 ASP D 185 -1 O LEU D 182 N VAL B 184
SHEET 9 C14 LYS D 194 SER D 200 -1 O VAL D 198 N GLY D 181
SHEET 10 C14 LEU D 148 PHE D 158 -1 N ALA D 156 O LEU D 197
SHEET 11 C14 PHE D 111 ILE D 117 1 N PHE D 111 O LYS D 149
SHEET 12 C14 PHE D 50 ILE D 54 1 N LEU D 52 O ILE D 115
SHEET 13 C14 VAL D 72 ASP D 77 1 O CYS D 74 N ASP D 53
SHEET 14 C14 ASP D 94 LEU D 97 1 O ASP D 94 N GLY D 75
SHEET 1 D 3 GLN C 26 TYR C 27 0
SHEET 2 D 3 THR C 103 LYS C 111 -1 O LYS C 111 N GLN C 26
SHEET 3 D 3 GLN C 33 GLN C 36 -1 N GLN C 33 O GLU C 107
SHEET 1 E 4 GLN C 26 TYR C 27 0
SHEET 2 E 4 THR C 103 LYS C 111 -1 O LYS C 111 N GLN C 26
SHEET 3 E 4 ILE C 118 LYS C 122 -1 O TYR C 119 N MET C 110
SHEET 4 E 4 ILE C 125 ASN C 127 -1 O ASN C 127 N TYR C 120
LINK C LEU B 123 N CSO B 124 1555 1555 1.33
LINK C CSO B 124 N ASN B 125 1555 1555 1.33
LINK C LEU D 123 N CSO D 124 1555 1555 1.33
LINK C CSO D 124 N ASN D 125 1555 1555 1.33
LINK SG CYS A 11 ZN ZN A 201 1555 1555 2.43
LINK SG CYS A 16 ZN ZN A 201 1555 1555 2.27
LINK SG CYS A 112 ZN ZN A 201 1555 1555 2.26
LINK SG CYS A 115 ZN ZN A 201 1555 1555 2.35
LINK SG CYS C 11 ZN ZN C 201 1555 1555 2.35
LINK SG CYS C 16 ZN ZN C 201 1555 1555 2.28
LINK SG CYS C 112 ZN ZN C 201 1555 1555 2.41
LINK SG CYS C 115 ZN ZN C 201 1555 1555 2.42
CISPEP 1 PHE A 23 PRO A 24 0 -4.37
CISPEP 2 PHE C 23 PRO C 24 0 -6.30
SITE 1 AC1 4 CYS A 11 CYS A 16 CYS A 112 CYS A 115
SITE 1 AC2 4 LYS A 14 LEU A 134 HOH A 309 ARG B 139
SITE 1 AC3 1 GLN A 36
SITE 1 AC4 6 HIS A 117 ILE A 118 TYR A 119 TYR A 120
SITE 2 AC4 6 ASN A 127 LEU A 129
SITE 1 AC5 4 LEU A 48 ASP A 52 PHE A 78 PRO A 79
SITE 1 AC6 2 ASP A 87 TYR B 159
SITE 1 AC7 6 HOH A 315 HOH A 317 HOH A 338 GLN B 121
SITE 2 AC7 6 TRP B 122 LYS B 161
SITE 1 AC8 22 TYR B 22 GLN B 32 GLY B 55 CYS B 56
SITE 2 AC8 22 GLY B 57 LEU B 60 SER B 61 ASP B 77
SITE 3 AC8 22 ILE B 78 SER B 79 MET B 82 GLN B 98
SITE 4 AC8 22 ASP B 99 MET B 100 ILE B 117 SER B 118
SITE 5 AC8 22 ALA B 119 TRP B 122 EDO B 302 HOH B 401
SITE 6 AC8 22 HOH B 406 HOH B 438
SITE 1 AC9 4 THR A 86 ASP A 87 ASP A 88 SAM B 301
SITE 1 BC1 2 ARG B 139 ASN B 142
SITE 1 BC2 7 LEU B 170 LYS B 174 PHE B 178 SER B 179
SITE 2 BC2 7 GLY B 180 ASP D 186 GLU D 188
SITE 1 BC3 3 GLU B 188 LEU D 170 GLY D 180
SITE 1 BC4 3 SER B 25 THR B 26 ARG B 27
SITE 1 BC5 2 GLN B 67 GLU B 68
SITE 1 BC6 6 ASN A 43 ASP B 70 HIS B 71 VAL B 72
SITE 2 BC6 6 GLU B 92 HOH B 422
SITE 1 BC7 4 LEU B 45 GLU B 68 HIS B 71 HOH B 408
SITE 1 BC8 6 ILE B 12 TYR B 14 SER B 79 PRO B 80
SITE 2 BC8 6 SER B 81 HOH B 458
SITE 1 BC9 3 ARG B 38 VAL D 198 EDO D 302
SITE 1 CC1 4 CYS C 11 CYS C 16 CYS C 112 CYS C 115
SITE 1 CC2 7 THR A 18 SER A 19 ASN A 20 ASP A 21
SITE 2 CC2 7 HOH A 332 LYS C 75 SER C 77
SITE 1 CC3 4 ILE C 118 TYR C 119 TYR C 120 ASN C 127
SITE 1 CC4 18 TYR D 22 GLN D 32 GLY D 55 CYS D 56
SITE 2 CC4 18 GLY D 57 LEU D 60 SER D 61 ASP D 77
SITE 3 CC4 18 ILE D 78 SER D 79 MET D 82 GLN D 98
SITE 4 CC4 18 ASP D 99 MET D 100 ILE D 117 SER D 118
SITE 5 CC4 18 TRP D 122 HOH D 401
SITE 1 CC5 4 VAL B 183 VAL B 198 EDO B 311 ARG D 38
CRYST1 75.472 53.733 85.205 90.00 94.55 90.00 P 1 21 1 4
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 0.013250 0.000000 0.001055 0.00000
SCALE2 0.000000 0.018611 0.000000 0.00000
SCALE3 0.000000 0.000000 0.011774 0.00000
(ATOM LINES ARE NOT SHOWN.)
END