HEADER TRANSCRIPTION 28-FEB-12 3VP9
TITLE CRYSTAL STRUCTURE OF THE N-TERMINAL DOMAIN OF THE YEAST GENERAL
TITLE 2 COREPRESSOR TUP1P MUTANT
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: GENERAL TRANSCRIPTIONAL COREPRESSOR TUP1;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: N-TERMINAL DOMAIN;
COMPND 5 SYNONYM: FLOCCULATION SUPPRESSOR PROTEIN, GLUCOSE REPRESSION
COMPND 6 REGULATORY PROTEIN TUP1, REPRESSOR AER2;
COMPND 7 ENGINEERED: YES;
COMPND 8 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;
SOURCE 3 ORGANISM_COMMON: YEAST;
SOURCE 4 ORGANISM_TAXID: 559292;
SOURCE 5 STRAIN: S288C;
SOURCE 6 GENE: TUP1;
SOURCE 7 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS FOUR HELIX BUNDLE, TRANSCRIPTION
EXPDTA X-RAY DIFFRACTION
AUTHOR H.MATSUMURA,N.KUSAKA,T.NAKAMURA,N.TANAKA,K.SAGEGAMI,K.UEGAKI,T.INOUE,
AUTHOR 2 Y.MUKAI
REVDAT 3 20-MAR-24 3VP9 1 REMARK SEQADV
REVDAT 2 17-JUL-13 3VP9 1 JRNL
REVDAT 1 13-JUN-12 3VP9 0
JRNL AUTH H.MATSUMURA,N.KUSAKA,T.NAKAMURA,N.TANAKA,K.SAGEGAMI,
JRNL AUTH 2 K.UEGAKI,T.INOUE,Y.MUKAI
JRNL TITL CRYSTAL STRUCTURE OF THE N-TERMINAL DOMAIN OF THE YEAST
JRNL TITL 2 GENERAL COREPRESSOR TUP1P AND ITS FUNCTIONAL IMPLICATIONS
JRNL REF J.BIOL.CHEM. V. 287 26528 2012
JRNL REFN ISSN 0021-9258
JRNL PMID 22707714
JRNL DOI 10.1074/JBC.M112.369652
REMARK 2
REMARK 2 RESOLUTION. 1.80 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE: 1.7_650)
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) : 1.80
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 33.29
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 87.0
REMARK 3 NUMBER OF REFLECTIONS : 19436
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.222
REMARK 3 R VALUE (WORKING SET) : 0.220
REMARK 3 FREE R VALUE : 0.258
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.840
REMARK 3 FREE R VALUE TEST SET COUNT : 941
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 33.2977 - 3.4408 0.85 2647 131 0.2423 0.2837
REMARK 3 2 3.4408 - 2.7315 0.90 2724 157 0.2133 0.2425
REMARK 3 3 2.7315 - 2.3863 0.90 2738 145 0.2079 0.2698
REMARK 3 4 2.3863 - 2.1682 0.90 2691 150 0.1874 0.2372
REMARK 3 5 2.1682 - 2.0128 0.90 2743 127 0.1997 0.2105
REMARK 3 6 2.0128 - 1.8941 0.85 2569 108 0.2255 0.2461
REMARK 3 7 1.8941 - 1.7993 0.79 2383 123 0.2377 0.2730
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.00
REMARK 3 SHRINKAGE RADIUS : 0.72
REMARK 3 K_SOL : 0.40
REMARK 3 B_SOL : 79.79
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.140
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 25.250
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 45.77
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -6.99890
REMARK 3 B22 (A**2) : -5.48130
REMARK 3 B33 (A**2) : 12.48020
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 9.96690
REMARK 3 B23 (A**2) : 0.00000
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 : 0.007 1308
REMARK 3 ANGLE : 1.071 1738
REMARK 3 CHIRALITY : 0.074 177
REMARK 3 PLANARITY : 0.004 230
REMARK 3 DIHEDRAL : 20.874 518
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 3VP9 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 01-MAR-12.
REMARK 100 THE DEPOSITION ID IS D_1000095329.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 04-OCT-10
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : PHOTON FACTORY
REMARK 200 BEAMLINE : BL-17A
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 20399
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.799
REMARK 200 RESOLUTION RANGE LOW (A) : 409.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 91.4
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.80
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.83
REMARK 200 COMPLETENESS FOR SHELL (%) : 91.1
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD
REMARK 200 SOFTWARE USED: SHELXS
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 54.66
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.71
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 14%(V/V) 1,4-DIOXANE, 0.1M MES
REMARK 280 MONOHYDRATE, 1.6M AMMONIUM SULFATE, PH 6.5, VAPOR DIFFUSION,
REMARK 280 TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1
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 28.05100
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 20.73050
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 28.05100
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 20.73050
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 9400 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 21340 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -45.0 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 BIOMT1 2 -1.000000 0.000000 0.000000 56.10200
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 HOH A 227 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A 231 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A 247 LIES ON A SPECIAL POSITION.
REMARK 375 HOH B 259 LIES ON A SPECIAL POSITION.
REMARK 375 HOH B 263 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 1
REMARK 465 THR A 2
REMARK 465 ALA A 3
REMARK 465 SER A 4
REMARK 465 VAL A 5
REMARK 465 SER A 6
REMARK 465 ASN A 7
REMARK 465 THR A 8
REMARK 465 GLN A 9
REMARK 465 ASN A 10
REMARK 465 LYS A 11
REMARK 465 LEU A 12
REMARK 465 ASN A 13
REMARK 465 GLU A 14
REMARK 465 LEU A 15
REMARK 465 LEU A 16
REMARK 465 ARG A 87
REMARK 465 ASP A 88
REMARK 465 HIS A 89
REMARK 465 GLN A 90
REMARK 465 ILE A 91
REMARK 465 ALA A 92
REMARK 465 MET B 1
REMARK 465 THR B 2
REMARK 465 ALA B 3
REMARK 465 SER B 4
REMARK 465 VAL B 5
REMARK 465 SER B 6
REMARK 465 ASN B 7
REMARK 465 THR B 8
REMARK 465 GLN B 9
REMARK 465 ASN B 10
REMARK 465 LYS B 11
REMARK 465 LEU B 12
REMARK 465 ASN B 13
REMARK 465 ILE B 91
REMARK 465 ALA B 92
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 O HOH A 249 O HOH A 256 1.82
REMARK 500 O HOH A 220 O HOH B 226 1.99
REMARK 500 O HOH A 266 O HOH A 269 2.02
REMARK 500 O HOH B 261 O HOH B 268 2.09
REMARK 500 O HOH A 219 O HOH A 237 2.11
REMARK 500 O HOH B 283 O HOH B 286 2.13
REMARK 500
REMARK 500 REMARK: NULL
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 B 262 O HOH B 262 2655 2.08
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 18 -3.28 170.82
REMARK 500 GLN A 25 40.69 -79.31
REMARK 500 VAL A 26 -29.67 -160.02
REMARK 500 ARG A 34 1.56 -68.31
REMARK 500 LEU A 35 -60.89 -107.18
REMARK 500 LEU B 16 52.01 -68.25
REMARK 500 ASP B 17 2.21 -166.25
REMARK 500 GLU B 22 -61.77 -96.14
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DIO A 101
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DIO B 101
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DIO B 102
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DIO B 103
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3VP8 RELATED DB: PDB
DBREF 3VP9 A 1 92 UNP P16649 TUP1_YEAST 1 92
DBREF 3VP9 B 1 92 UNP P16649 TUP1_YEAST 1 92
SEQADV 3VP9 ARG A 62 UNP P16649 LEU 62 ENGINEERED MUTATION
SEQADV 3VP9 ARG B 62 UNP P16649 LEU 62 ENGINEERED MUTATION
SEQRES 1 A 92 MET THR ALA SER VAL SER ASN THR GLN ASN LYS LEU ASN
SEQRES 2 A 92 GLU LEU LEU ASP ALA ILE ARG GLN GLU PHE LEU GLN VAL
SEQRES 3 A 92 SER GLN GLU ALA ASN THR TYR ARG LEU GLN ASN GLN LYS
SEQRES 4 A 92 ASP TYR ASP PHE LYS MET ASN GLN GLN LEU ALA GLU MET
SEQRES 5 A 92 GLN GLN ILE ARG ASN THR VAL TYR GLU ARG GLU LEU THR
SEQRES 6 A 92 HIS ARG LYS MET LYS ASP ALA TYR GLU GLU GLU ILE LYS
SEQRES 7 A 92 HIS LEU LYS LEU GLY LEU GLU GLN ARG ASP HIS GLN ILE
SEQRES 8 A 92 ALA
SEQRES 1 B 92 MET THR ALA SER VAL SER ASN THR GLN ASN LYS LEU ASN
SEQRES 2 B 92 GLU LEU LEU ASP ALA ILE ARG GLN GLU PHE LEU GLN VAL
SEQRES 3 B 92 SER GLN GLU ALA ASN THR TYR ARG LEU GLN ASN GLN LYS
SEQRES 4 B 92 ASP TYR ASP PHE LYS MET ASN GLN GLN LEU ALA GLU MET
SEQRES 5 B 92 GLN GLN ILE ARG ASN THR VAL TYR GLU ARG GLU LEU THR
SEQRES 6 B 92 HIS ARG LYS MET LYS ASP ALA TYR GLU GLU GLU ILE LYS
SEQRES 7 B 92 HIS LEU LYS LEU GLY LEU GLU GLN ARG ASP HIS GLN ILE
SEQRES 8 B 92 ALA
HET DIO A 101 6
HET DIO B 101 6
HET DIO B 102 6
HET DIO B 103 6
HETNAM DIO 1,4-DIETHYLENE DIOXIDE
FORMUL 3 DIO 4(C4 H8 O2)
FORMUL 7 HOH *174(H2 O)
HELIX 1 1 VAL A 26 GLU A 85 1 60
HELIX 2 2 ILE B 19 LEU B 24 1 6
HELIX 3 3 VAL B 26 ASP B 88 1 63
SITE 1 AC1 5 ARG A 56 VAL A 59 TYR A 60 ARG B 62
SITE 2 AC1 5 HOH B 274
SITE 1 AC2 5 ARG A 62 VAL B 59 TYR B 60 GLU B 63
SITE 2 AC2 5 ARG B 67
SITE 1 AC3 7 HIS A 66 TYR A 73 HIS B 66 MET B 69
SITE 2 AC3 7 LYS B 70 TYR B 73 HOH B 244
SITE 1 AC4 7 LEU A 64 LYS A 68 ASP A 71 HOH A 224
SITE 2 AC4 7 ASN B 57 TYR B 60 GLU B 61
CRYST1 56.102 41.461 103.889 90.00 95.35 90.00 C 1 2 1 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 0.017825 0.000000 0.001669 0.00000
SCALE2 0.000000 0.024119 0.000000 0.00000
SCALE3 0.000000 0.000000 0.009668 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
