HEADER ISOMERASE 31-AUG-99 1CY0
TITLE COMPLEX OF E.COLI DNA TOPOISOMERASE I WITH 3'-5'-ADENOSINE DIPHOSPHATE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: DNA TOPOISOMERASE I;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: 67 KDA N-TERMINAL FRAGMENT OF E.COLI TOPOISOMERASE I;
COMPND 5 EC: 5.99.1.2;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 3 ORGANISM_TAXID: 83333;
SOURCE 4 STRAIN: K12;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PGEX-2T
KEYWDS DNA TOPOISOMERASE, RELAXING ENZYME, ISOMERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR H.FEINBERG,A.CHANGELA,A.MONDRAGON
REVDAT 6 21-DEC-22 1CY0 1 REMARK SEQADV
REVDAT 5 14-AUG-19 1CY0 1 REMARK
REVDAT 4 24-JUL-19 1CY0 1 REMARK
REVDAT 3 13-JUL-11 1CY0 1 VERSN
REVDAT 2 24-FEB-09 1CY0 1 VERSN
REVDAT 1 08-MAR-00 1CY0 0
JRNL AUTH H.FEINBERG,A.CHANGELA,A.MONDRAGON
JRNL TITL PROTEIN-NUCLEOTIDE INTERACTIONS IN E. COLI DNA TOPOISOMERASE
JRNL TITL 2 I.
JRNL REF NAT.STRUCT.BIOL. V. 6 961 1999
JRNL REFN ISSN 1072-8368
JRNL PMID 10504732
JRNL DOI 10.1038/13333
REMARK 2
REMARK 2 RESOLUTION. 2.45 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 0.9
REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-
REMARK 3 : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,
REMARK 3 : READ,RICE,SIMONSON,WARREN
REMARK 3
REMARK 3 REFINEMENT TARGET : R. A. ENGH AND R. HUBER, ACTA CRYST. SECT.
REMARK 3 A., 1991
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.45
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 19.98
REMARK 3 DATA CUTOFF (SIGMA(F)) : 2.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 15292774.300
REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0000
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 95.2
REMARK 3 NUMBER OF REFLECTIONS : 22433
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 SET) : 0.220
REMARK 3 FREE R VALUE : 0.274
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.200
REMARK 3 FREE R VALUE TEST SET COUNT : 1160
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.008
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 6
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.45
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.60
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 86.00
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 3149
REMARK 3 BIN R VALUE (WORKING SET) : 0.2740
REMARK 3 BIN FREE R VALUE : 0.3540
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 5.00
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 166
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.027
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 4260
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 27
REMARK 3 SOLVENT ATOMS : 123
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 37.00
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 37.20
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.68000
REMARK 3 B22 (A**2) : -2.11000
REMARK 3 B33 (A**2) : 1.43000
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 COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.31
REMARK 3 ESD FROM SIGMAA (A) : 0.21
REMARK 3 LOW RESOLUTION CUTOFF (A) : 20.0
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : 0.41
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.33
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.007
REMARK 3 BOND ANGLES (DEGREES) : 1.200
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 22.10
REMARK 3 IMPROPER ANGLES (DEGREES) : 0.820
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : RESTRAINED
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : 0.810 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 1.430 ; 2.000
REMARK 3 SIDE-CHAIN BOND (A**2) : 1.190 ; 2.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 1.900 ; 2.500
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : FLAT MODEL
REMARK 3 KSOL : 0.37
REMARK 3 BSOL : 30.38
REMARK 3
REMARK 3 NCS MODEL : NULL
REMARK 3
REMARK 3 NCS RESTRAINTS. RMS SIGMA/WEIGHT
REMARK 3 GROUP 1 POSITIONAL (A) : NULL ; NULL
REMARK 3 GROUP 1 B-FACTOR (A**2) : NULL ; NULL
REMARK 3
REMARK 3 PARAMETER FILE 1 : PROTEIN_REP.PA
REMARK 3 PARAMETER FILE 2 : A3P_XPLOR_PAR.TXT
REMARK 3 PARAMETER FILE 3 : WATER_REP.PARA
REMARK 3 PARAMETER FILE 4 : NULL
REMARK 3 TOPOLOGY FILE 1 : PROTEIN.TOP
REMARK 3 TOPOLOGY FILE 2 : A3P_XPLOR_TOP.TXT
REMARK 3 TOPOLOGY FILE 3 : WATER.TOP
REMARK 3 TOPOLOGY FILE 4 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS:
REMARK 3 REFINEMENT DONE WITH REFMAC. THE SOLVENT CORRECTION WAS CALCULATED
REMARK 3 WITH XPLOR
REMARK 3 AND APPLIED IN REFMAC.
REMARK 3 FINAL PARAMETERS OBTAINED WITH CNS 0.9
REMARK 4
REMARK 4 1CY0 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 03-SEP-99.
REMARK 100 THE DEPOSITION ID IS D_1000009618.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 01-JUL-97
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 5.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SSRL
REMARK 200 BEAMLINE : BL9-1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.98
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 24161
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.450
REMARK 200 RESOLUTION RANGE LOW (A) : 999.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 96.3
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : 0.06900
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) : 2.45
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.52
REMARK 200 COMPLETENESS FOR SHELL (%) : 66.8
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.23800
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: AMORE
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 46.50
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.30
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 2.14M AMMONIUM SULFATE, PH 5.0,
REMARK 280 MICRODIALYSIS, TEMPERATURE 287K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
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 31.52000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 67.23000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 36.65500
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 67.23000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 31.52000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 36.65500
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: 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 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 -1
REMARK 465 SER A 0
REMARK 465 MET A 1
REMARK 465 THR A 39
REMARK 465 SER A 40
REMARK 465 GLY A 41
REMARK 465 SER A 42
REMARK 465 ALA A 43
REMARK 465 ALA A 44
REMARK 465 LYS A 45
REMARK 465 LYS A 46
REMARK 465 SER A 47
REMARK 465 ALA A 48
REMARK 465 ASP A 49
REMARK 465 SER A 50
REMARK 465 THR A 51
REMARK 465 SER A 52
REMARK 465 THR A 53
REMARK 465 LYS A 54
REMARK 465 THR A 55
REMARK 465 ALA A 56
REMARK 465 LYS A 57
REMARK 465 LYS A 58
REMARK 465 PRO A 59
REMARK 465 LYS A 60
REMARK 465 LYS A 61
REMARK 465 ASP A 62
REMARK 465 GLU A 63
REMARK 465 ARG A 64
REMARK 465 GLY A 65
REMARK 465 PRO A 439
REMARK 465 ALA A 440
REMARK 465 LEU A 441
REMARK 465 ARG A 442
REMARK 465 LYS A 443
REMARK 465 GLY A 444
REMARK 465 ASP A 445
REMARK 465 GLU A 446
REMARK 465 ASP A 447
REMARK 465 ARG A 448
REMARK 465 GLN A 573
REMARK 465 GLN A 574
REMARK 465 LEU A 575
REMARK 465 ASP A 576
REMARK 465 LYS A 577
REMARK 465 ALA A 578
REMARK 465 GLU A 579
REMARK 465 LYS A 580
REMARK 465 ASP A 581
REMARK 465 PRO A 582
REMARK 465 GLU A 583
REMARK 465 GLU A 584
REMARK 465 GLY A 585
REMARK 465 GLY A 586
REMARK 465 MET A 587
REMARK 465 ARG A 588
REMARK 465 PRO A 589
REMARK 465 ASN A 590
REMARK 465 GLN A 591
REMARK 465 MET A 592
REMARK 465 VAL A 593
REMARK 465 LEU A 594
REMARK 465 THR A 595
REMARK 465 SER A 596
REMARK 465 ILE A 597
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 LYS A 3 -108.43 -94.99
REMARK 500 ASP A 24 20.96 -76.13
REMARK 500 VAL A 31 105.97 -48.02
REMARK 500 ALA A 109 43.72 -106.15
REMARK 500 ILE A 142 78.19 -101.48
REMARK 500 LYS A 153 67.84 -113.93
REMARK 500 ILE A 187 -64.57 -132.71
REMARK 500 PHE A 343 -30.95 -131.33
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 A3P A 605
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1CY1 RELATED DB: PDB
REMARK 900 COMPLEX OF E.COLI DNA TOPOISOMERASE I WITH 5'PTPTPT
REMARK 900 RELATED ID: 1CY2 RELATED DB: PDB
REMARK 900 COMPLEX OF E.COLI DNA TOPOISOMERASE I WITH TPTPTP3'
REMARK 900 RELATED ID: 1CY4 RELATED DB: PDB
REMARK 900 COMPLEX OF E.COLI DNA TOPOISOMERASE I WITH 5'PTPTPTP3'
REMARK 900 RELATED ID: 1CY6 RELATED DB: PDB
REMARK 900 COMPLEX OF E.COLI DNA TOPOISOMERASE I WITH 3'-THYMIDINE
REMARK 900 MONOPHOSPHATE
REMARK 900 RELATED ID: 1CY7 RELATED DB: PDB
REMARK 900 COMPLEX OF E.COLI DNA TOPOISOMERASE I WITH 5'-THYMIDINE
REMARK 900 MONOPHOSPHATE
REMARK 900 RELATED ID: 1CY8 RELATED DB: PDB
REMARK 900 COMPLEX OF E.COLI DNA TOPOISOMERASE I WITH 5'-THYMIDINE
REMARK 900 MONOPHOSPHATE AND 3'-THYMIDINE MONOPHOSPHATE
REMARK 900 RELATED ID: 1CY9 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE 30 KDA FRAGMENT OF E. COLI DNA
REMARK 900 TOPOISOMERASE I. MONOCLINIC FORM
REMARK 900 RELATED ID: 1CYY RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE 30 KDA FRAGMENT OF E. COLI DNA
REMARK 900 TOPOISOMERASE I. HEXAGONAL FORM
DBREF 1CY0 A 1 597 UNP P06612 TOP1_ECOLI 1 597
SEQADV 1CY0 GLY A -1 UNP P06612 CLONING ARTIFACT
SEQADV 1CY0 SER A 0 UNP P06612 CLONING ARTIFACT
SEQRES 1 A 599 GLY SER MET GLY LYS ALA LEU VAL ILE VAL GLU SER PRO
SEQRES 2 A 599 ALA LYS ALA LYS THR ILE ASN LYS TYR LEU GLY SER ASP
SEQRES 3 A 599 TYR VAL VAL LYS SER SER VAL GLY HIS ILE ARG ASP LEU
SEQRES 4 A 599 PRO THR SER GLY SER ALA ALA LYS LYS SER ALA ASP SER
SEQRES 5 A 599 THR SER THR LYS THR ALA LYS LYS PRO LYS LYS ASP GLU
SEQRES 6 A 599 ARG GLY ALA LEU VAL ASN ARG MET GLY VAL ASP PRO TRP
SEQRES 7 A 599 HIS ASN TRP GLU ALA HIS TYR GLU VAL LEU PRO GLY LYS
SEQRES 8 A 599 GLU LYS VAL VAL SER GLU LEU LYS GLN LEU ALA GLU LYS
SEQRES 9 A 599 ALA ASP HIS ILE TYR LEU ALA THR ASP LEU ASP ARG GLU
SEQRES 10 A 599 GLY GLU ALA ILE ALA TRP HIS LEU ARG GLU VAL ILE GLY
SEQRES 11 A 599 GLY ASP ASP ALA ARG TYR SER ARG VAL VAL PHE ASN GLU
SEQRES 12 A 599 ILE THR LYS ASN ALA ILE ARG GLN ALA PHE ASN LYS PRO
SEQRES 13 A 599 GLY GLU LEU ASN ILE ASP ARG VAL ASN ALA GLN GLN ALA
SEQRES 14 A 599 ARG ARG PHE MET ASP ARG VAL VAL GLY TYR MET VAL SER
SEQRES 15 A 599 PRO LEU LEU TRP LYS LYS ILE ALA ARG GLY LEU SER ALA
SEQRES 16 A 599 GLY ARG VAL GLN SER VAL ALA VAL ARG LEU VAL VAL GLU
SEQRES 17 A 599 ARG GLU ARG GLU ILE LYS ALA PHE VAL PRO GLU GLU PHE
SEQRES 18 A 599 TRP GLU VAL ASP ALA SER THR THR THR PRO SER GLY GLU
SEQRES 19 A 599 ALA LEU ALA LEU GLN VAL THR HIS GLN ASN ASP LYS PRO
SEQRES 20 A 599 PHE ARG PRO VAL ASN LYS GLU GLN THR GLN ALA ALA VAL
SEQRES 21 A 599 SER LEU LEU GLU LYS ALA ARG TYR SER VAL LEU GLU ARG
SEQRES 22 A 599 GLU ASP LYS PRO THR THR SER LYS PRO GLY ALA PRO PHE
SEQRES 23 A 599 ILE THR SER THR LEU GLN GLN ALA ALA SER THR ARG LEU
SEQRES 24 A 599 GLY PHE GLY VAL LYS LYS THR MET MET MET ALA GLN ARG
SEQRES 25 A 599 LEU TYR GLU ALA GLY TYR ILE THR TYR MET ARG THR ASP
SEQRES 26 A 599 SER THR ASN LEU SER GLN ASP ALA VAL ASN MET VAL ARG
SEQRES 27 A 599 GLY TYR ILE SER ASP ASN PHE GLY LYS LYS TYR LEU PRO
SEQRES 28 A 599 GLU SER PRO ASN GLN TYR ALA SER LYS GLU ASN SER GLN
SEQRES 29 A 599 GLU ALA HIS GLU ALA ILE ARG PRO SER ASP VAL ASN VAL
SEQRES 30 A 599 MET ALA GLU SER LEU LYS ASP MET GLU ALA ASP ALA GLN
SEQRES 31 A 599 LYS LEU TYR GLN LEU ILE TRP ARG GLN PHE VAL ALA CYS
SEQRES 32 A 599 GLN MET THR PRO ALA LYS TYR ASP SER THR THR LEU THR
SEQRES 33 A 599 VAL GLY ALA GLY ASP PHE ARG LEU LYS ALA ARG GLY ARG
SEQRES 34 A 599 ILE LEU ARG PHE ASP GLY TRP THR LYS VAL MET PRO ALA
SEQRES 35 A 599 LEU ARG LYS GLY ASP GLU ASP ARG ILE LEU PRO ALA VAL
SEQRES 36 A 599 ASN LYS GLY ASP ALA LEU THR LEU VAL GLU LEU THR PRO
SEQRES 37 A 599 ALA GLN HIS PHE THR LYS PRO PRO ALA ARG PHE SER GLU
SEQRES 38 A 599 ALA SER LEU VAL LYS GLU LEU GLU LYS ARG GLY ILE GLY
SEQRES 39 A 599 ARG PRO SER THR TYR ALA SER ILE ILE SER THR ILE GLN
SEQRES 40 A 599 ASP ARG GLY TYR VAL ARG VAL GLU ASN ARG ARG PHE TYR
SEQRES 41 A 599 ALA GLU LYS MET GLY GLU ILE VAL THR ASP ARG LEU GLU
SEQRES 42 A 599 GLU ASN PHE ARG GLU LEU MET ASN TYR ASP PHE THR ALA
SEQRES 43 A 599 GLN MET GLU ASN SER LEU ASP GLN VAL ALA ASN HIS GLU
SEQRES 44 A 599 ALA GLU TRP LYS ALA VAL LEU ASP HIS PHE PHE SER ASP
SEQRES 45 A 599 PHE THR GLN GLN LEU ASP LYS ALA GLU LYS ASP PRO GLU
SEQRES 46 A 599 GLU GLY GLY MET ARG PRO ASN GLN MET VAL LEU THR SER
SEQRES 47 A 599 ILE
HET A3P A 605 27
HETNAM A3P ADENOSINE-3'-5'-DIPHOSPHATE
FORMUL 2 A3P C10 H15 N5 O10 P2
FORMUL 3 HOH *123(H2 O)
HELIX 1 1 SER A 10 ASN A 18 1 9
HELIX 2 2 LYS A 19 LEU A 21 5 3
HELIX 3 3 ALA A 66 GLY A 72 1 7
HELIX 4 4 LYS A 89 GLU A 101 1 13
HELIX 5 5 ASP A 113 GLY A 128 1 16
HELIX 6 6 ASP A 130 ALA A 132 5 3
HELIX 7 7 THR A 143 LYS A 153 1 11
HELIX 8 8 ASN A 158 ILE A 187 1 30
HELIX 9 9 VAL A 196 PHE A 214 1 19
HELIX 10 10 ASN A 250 ALA A 264 1 15
HELIX 11 11 ILE A 285 GLY A 298 1 14
HELIX 12 12 GLY A 300 ALA A 314 1 15
HELIX 13 13 SER A 328 PHE A 343 1 16
HELIX 14 14 GLY A 344 LEU A 348 5 5
HELIX 15 15 MET A 376 LEU A 380 5 5
HELIX 16 16 GLU A 384 CYS A 401 1 18
HELIX 17 17 ASP A 432 MET A 438 5 7
HELIX 18 18 SER A 478 ARG A 489 1 12
HELIX 19 19 THR A 496 ARG A 507 1 12
HELIX 20 20 GLU A 520 PHE A 534 1 15
HELIX 21 21 ASN A 539 ASN A 555 1 17
HELIX 22 22 GLU A 559 THR A 572 1 14
SHEET 1 A 4 TYR A 25 SER A 29 0
SHEET 2 A 4 ALA A 4 VAL A 8 1 O ALA A 4 N VAL A 26
SHEET 3 A 4 ILE A 106 LEU A 108 1 N TYR A 107 O LEU A 5
SHEET 4 A 4 TYR A 134 ARG A 136 1 O SER A 135 N LEU A 108
SHEET 1 B 2 ARG A 35 ASP A 36 0
SHEET 2 B 2 GLU A 84 VAL A 85 -1 N GLU A 84 O ASP A 36
SHEET 1 C 8 LYS A 244 PRO A 245 0
SHEET 2 C 8 ALA A 233 GLN A 241 -1 N GLN A 241 O LYS A 244
SHEET 3 C 8 GLU A 218 THR A 227 -1 O VAL A 222 N VAL A 238
SHEET 4 C 8 ALA A 458 PHE A 470 -1 N THR A 460 O THR A 227
SHEET 5 C 8 TYR A 266 SER A 278 -1 O TYR A 266 N LEU A 459
SHEET 6 C 8 ALA A 406 ALA A 417 -1 N ALA A 406 O SER A 278
SHEET 7 C 8 PHE A 420 PHE A 431 -1 N PHE A 420 O ALA A 417
SHEET 8 C 8 ALA A 233 GLN A 241 -1 N GLN A 237 O LYS A 423
SHEET 1 D 2 VAL A 510 GLU A 513 0
SHEET 2 D 2 ARG A 516 ALA A 519 -1 O ARG A 516 N GLU A 513
SITE 1 AC1 11 SER A 340 ASP A 341 LEU A 348 GLU A 520
SITE 2 AC1 11 LYS A 521 MET A 522 ILE A 525 HIS A 566
SITE 3 AC1 11 SER A 569 HOH A 606 HOH A 728
CRYST1 63.040 73.310 134.460 90.00 90.00 90.00 P 21 21 21 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 0.015863 0.000000 0.000000 0.00000
SCALE2 0.000000 0.013641 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007437 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
