HEADER ISOMERASE 01-OCT-99 1D3Y
TITLE STRUCTURE OF THE DNA TOPOISOMERASE VI A SUBUNIT
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: DNA TOPOISOMERASE VI A SUBUNIT;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: DNA BINDING CORE;
COMPND 5 EC: 5.99.1.3;
COMPND 6 ENGINEERED: YES;
COMPND 7 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: METHANOCALDOCOCCUS JANNASCHII;
SOURCE 3 ORGANISM_TAXID: 2190;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 6 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 7 EXPRESSION_SYSTEM_PLASMID: PET24B
KEYWDS TOPOISOMERASE VI, DNA BINDING PROTEIN, SPO11 HOMOLOG, ISOMERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR M.D.NICHOLS,K.A.DEANGELIS,J.L.KECK,J.M.BERGER
REVDAT 4 07-FEB-24 1D3Y 1 REMARK SHEET LINK
REVDAT 3 24-FEB-09 1D3Y 1 VERSN
REVDAT 2 01-APR-03 1D3Y 1 JRNL
REVDAT 1 05-NOV-99 1D3Y 0
JRNL AUTH M.D.NICHOLS,K.DEANGELIS,J.L.KECK,J.M.BERGER
JRNL TITL STRUCTURE AND FUNCTION OF AN ARCHAEAL TOPOISOMERASE VI
JRNL TITL 2 SUBUNIT WITH HOMOLOGY TO THE MEIOTIC RECOMBINATION FACTOR
JRNL TITL 3 SPO11.
JRNL REF EMBO J. V. 18 6177 1999
JRNL REFN ISSN 0261-4189
JRNL PMID 10545127
JRNL DOI 10.1093/EMBOJ/18.21.6177
REMARK 2
REMARK 2 RESOLUTION. 2.00 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.00
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 20.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : NULL
REMARK 3 NUMBER OF REFLECTIONS : 43761
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : NULL
REMARK 3 FREE R VALUE TEST SET SELECTION : NULL
REMARK 3 R VALUE (WORKING + TEST SET) : NULL
REMARK 3 R VALUE (WORKING SET) : 0.197
REMARK 3 FREE R VALUE : 0.242
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : 3653
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 4648
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 5
REMARK 3 SOLVENT ATOMS : 326
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 19.40
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
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 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): NULL
REMARK 3 ESU BASED ON FREE R VALUE (A): NULL
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 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 DISTANCE RESTRAINTS. RMS SIGMA
REMARK 3 BOND LENGTH (A) : NULL ; NULL
REMARK 3 ANGLE DISTANCE (A) : NULL ; NULL
REMARK 3 INTRAPLANAR 1-4 DISTANCE (A) : NULL ; NULL
REMARK 3 H-BOND OR METAL COORDINATION (A) : NULL ; NULL
REMARK 3
REMARK 3 PLANE RESTRAINT (A) : NULL ; NULL
REMARK 3 CHIRAL-CENTER RESTRAINT (A**3) : NULL ; NULL
REMARK 3
REMARK 3 NON-BONDED CONTACT RESTRAINTS.
REMARK 3 SINGLE TORSION (A) : NULL ; NULL
REMARK 3 MULTIPLE TORSION (A) : NULL ; NULL
REMARK 3 H-BOND (X...Y) (A) : NULL ; NULL
REMARK 3 H-BOND (X-H...Y) (A) : NULL ; NULL
REMARK 3
REMARK 3 CONFORMATIONAL TORSION ANGLE RESTRAINTS.
REMARK 3 SPECIFIED (DEGREES) : NULL ; NULL
REMARK 3 PLANAR (DEGREES) : NULL ; NULL
REMARK 3 STAGGERED (DEGREES) : NULL ; NULL
REMARK 3 TRANSVERSE (DEGREES) : NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1D3Y COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 05-OCT-99.
REMARK 100 THE DEPOSITION ID IS D_1000009772.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : NULL
REMARK 200 TEMPERATURE (KELVIN) : 110
REMARK 200 PH : 6.1
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : ROTATING ANODE
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : RIGAKU RU200
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.54
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : RIGAKU RAXIS IIC
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 43773
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.000
REMARK 200 RESOLUTION RANGE LOW (A) : 20.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 96.5
REMARK 200 DATA REDUNDANCY : 8.800
REMARK 200 R MERGE (I) : 0.03600
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 17.8000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.00
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.07
REMARK 200 COMPLETENESS FOR SHELL (%) : 93.6
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.13100
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: SHARP
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 50.90
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.50
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 8000, MPD, NA-CACODYLATE, MGCL2,
REMARK 280 NACL, PH 6.1, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K
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 29.52000
REMARK 290 SMTRY3 2 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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 4700 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 23920 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -53.0 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 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 THR A 69
REMARK 465 VAL A 70
REMARK 465 ASN A 71
REMARK 465 GLY A 265
REMARK 465 SER A 266
REMARK 465 GLY A 267
REMARK 465 LYS A 268
REMARK 465 ALA A 269
REMARK 465 ILE A 270
REMARK 465 HIS A 271
REMARK 465 LEU A 272
REMARK 465 ALA A 273
REMARK 465 THR B 69
REMARK 465 VAL B 70
REMARK 465 SER B 266
REMARK 465 GLY B 267
REMARK 465 LYS B 268
REMARK 465 ALA B 269
REMARK 465 ILE B 270
REMARK 465 HIS B 271
REMARK 465 LEU B 272
REMARK 465 ALA B 273
REMARK 465 ASP B 274
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 231 CD - NE - CZ ANGL. DEV. = 19.8 DEGREES
REMARK 500 ARG A 231 NE - CZ - NH1 ANGL. DEV. = -3.2 DEGREES
REMARK 500 ARG A 231 NE - CZ - NH2 ANGL. DEV. = 3.4 DEGREES
REMARK 500 GLY A 285 CA - C - N ANGL. DEV. = 21.2 DEGREES
REMARK 500 GLY A 285 O - C - N ANGL. DEV. = -20.6 DEGREES
REMARK 500 ARG B 230 CD - NE - CZ ANGL. DEV. = 8.4 DEGREES
REMARK 500 ARG B 231 NE - CZ - NH2 ANGL. DEV. = -3.1 DEGREES
REMARK 500 GLY B 285 CA - C - N ANGL. DEV. = 15.5 DEGREES
REMARK 500 GLY B 285 O - C - N ANGL. DEV. = -18.5 DEGREES
REMARK 500 PRO B 369 C - N - CD ANGL. DEV. = 13.3 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 SER A 146 -151.74 -90.54
REMARK 500 PRO A 151 85.53 -66.76
REMARK 500 ASN A 257 -53.44 -121.72
REMARK 500 THR A 355 -59.91 -122.52
REMARK 500 SER B 146 -152.63 -91.39
REMARK 500 PRO B 151 88.52 -69.44
REMARK 500 ASN B 257 -52.74 -123.45
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 MG A 371 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU A 197 OE2
REMARK 620 2 ASP A 249 OD2 89.1
REMARK 620 3 HOH A 381 O 89.6 98.1
REMARK 620 4 HOH A 399 O 95.7 169.3 91.5
REMARK 620 5 HOH A 463 O 93.0 83.2 177.2 87.0
REMARK 620 6 HOH A 511 O 172.5 91.7 83.0 84.7 94.5
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG A 372 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH A 394 O
REMARK 620 2 HOH A 426 O 84.0
REMARK 620 3 HOH A 490 O 91.4 92.3
REMARK 620 4 HOH B 376 O 91.3 175.3 87.7
REMARK 620 5 HOH B 379 O 95.9 91.8 172.0 88.8
REMARK 620 6 HOH B 451 O 172.7 89.8 85.1 94.9 88.0
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG B 374 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU B 197 OE2
REMARK 620 2 ASP B 249 OD2 92.1
REMARK 620 3 HOH B 413 O 169.9 92.5
REMARK 620 4 HOH B 417 O 87.6 98.4 82.8
REMARK 620 5 HOH B 426 O 96.0 82.8 93.6 176.2
REMARK 620 6 HOH B 501 O 93.7 168.1 83.6 92.2 86.2
REMARK 620 N 1 2 3 4 5
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA A 370
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 371
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 372
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA B 373
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG B 374
DBREF 1D3Y A 69 369 UNP Q57815 TOP6A_METJA 69 369
DBREF 1D3Y B 69 369 UNP Q57815 TOP6A_METJA 69 369
SEQRES 1 A 301 THR VAL ASN GLN ALA LYS ILE PHE ALA GLN THR THR LYS
SEQRES 2 A 301 MET LEU GLU PHE ALA LYS GLN LEU LEU GLU THR ASP ASP
SEQRES 3 A 301 PHE SER THR LEU ARG GLU ALA TYR TYR VAL SER LYS ASN
SEQRES 4 A 301 TRP GLY GLU ALA ARG PHE ASP ASP GLN GLN ALA SER ASN
SEQRES 5 A 301 ASN VAL ILE GLU ASP LEU GLU ALA ALA LEU GLY VAL LEU
SEQRES 6 A 301 ARG GLU HIS LEU GLY PHE ILE PRO GLU GLU ASP GLY SER
SEQRES 7 A 301 SER VAL VAL GLY PRO LEU LYS ILE ILE GLU GLU THR PRO
SEQRES 8 A 301 GLU GLY GLU LEU VAL VAL ASP CYS THR LYS LEU GLY THR
SEQRES 9 A 301 GLY ALA TYR ASN ILE PRO ASN ASP VAL THR LYS LEU ASN
SEQRES 10 A 301 LEU GLU THR ASP ALA ASP PHE ILE LEU ALA ILE GLU THR
SEQRES 11 A 301 SER GLY MET PHE ALA ARG LEU ASN ALA GLU ARG PHE TRP
SEQRES 12 A 301 ASP LYS HIS ASN CYS ILE LEU VAL SER LEU LYS GLY VAL
SEQRES 13 A 301 PRO ALA ARG ALA THR ARG ARG PHE ILE LYS ARG LEU HIS
SEQRES 14 A 301 GLU GLU HIS ASP LEU PRO VAL LEU VAL PHE THR ASP GLY
SEQRES 15 A 301 ASP PRO TYR GLY TYR LEU ASN ILE TYR ARG THR LEU LYS
SEQRES 16 A 301 VAL GLY SER GLY LYS ALA ILE HIS LEU ALA ASP LYS LEU
SEQRES 17 A 301 SER ILE PRO ALA ALA ARG LEU ILE GLY VAL THR PRO GLN
SEQRES 18 A 301 ASP ILE ILE ASP TYR ASP LEU PRO THR HIS PRO LEU LYS
SEQRES 19 A 301 GLU GLN ASP ILE LYS ARG ILE LYS ASP GLY LEU LYS ASN
SEQRES 20 A 301 ASP ASP PHE VAL ARG SER PHE PRO GLU TRP GLN LYS ALA
SEQRES 21 A 301 LEU LYS GLN MET LEU ASP MET GLY VAL ARG ALA GLU GLN
SEQRES 22 A 301 GLN SER LEU ALA LYS TYR GLY LEU LYS TYR VAL VAL ASN
SEQRES 23 A 301 THR TYR LEU PRO GLU LYS ILE LYS ASP GLU SER THR TRP
SEQRES 24 A 301 LEU PRO
SEQRES 1 B 301 THR VAL ASN GLN ALA LYS ILE PHE ALA GLN THR THR LYS
SEQRES 2 B 301 MET LEU GLU PHE ALA LYS GLN LEU LEU GLU THR ASP ASP
SEQRES 3 B 301 PHE SER THR LEU ARG GLU ALA TYR TYR VAL SER LYS ASN
SEQRES 4 B 301 TRP GLY GLU ALA ARG PHE ASP ASP GLN GLN ALA SER ASN
SEQRES 5 B 301 ASN VAL ILE GLU ASP LEU GLU ALA ALA LEU GLY VAL LEU
SEQRES 6 B 301 ARG GLU HIS LEU GLY PHE ILE PRO GLU GLU ASP GLY SER
SEQRES 7 B 301 SER VAL VAL GLY PRO LEU LYS ILE ILE GLU GLU THR PRO
SEQRES 8 B 301 GLU GLY GLU LEU VAL VAL ASP CYS THR LYS LEU GLY THR
SEQRES 9 B 301 GLY ALA TYR ASN ILE PRO ASN ASP VAL THR LYS LEU ASN
SEQRES 10 B 301 LEU GLU THR ASP ALA ASP PHE ILE LEU ALA ILE GLU THR
SEQRES 11 B 301 SER GLY MET PHE ALA ARG LEU ASN ALA GLU ARG PHE TRP
SEQRES 12 B 301 ASP LYS HIS ASN CYS ILE LEU VAL SER LEU LYS GLY VAL
SEQRES 13 B 301 PRO ALA ARG ALA THR ARG ARG PHE ILE LYS ARG LEU HIS
SEQRES 14 B 301 GLU GLU HIS ASP LEU PRO VAL LEU VAL PHE THR ASP GLY
SEQRES 15 B 301 ASP PRO TYR GLY TYR LEU ASN ILE TYR ARG THR LEU LYS
SEQRES 16 B 301 VAL GLY SER GLY LYS ALA ILE HIS LEU ALA ASP LYS LEU
SEQRES 17 B 301 SER ILE PRO ALA ALA ARG LEU ILE GLY VAL THR PRO GLN
SEQRES 18 B 301 ASP ILE ILE ASP TYR ASP LEU PRO THR HIS PRO LEU LYS
SEQRES 19 B 301 GLU GLN ASP ILE LYS ARG ILE LYS ASP GLY LEU LYS ASN
SEQRES 20 B 301 ASP ASP PHE VAL ARG SER PHE PRO GLU TRP GLN LYS ALA
SEQRES 21 B 301 LEU LYS GLN MET LEU ASP MET GLY VAL ARG ALA GLU GLN
SEQRES 22 B 301 GLN SER LEU ALA LYS TYR GLY LEU LYS TYR VAL VAL ASN
SEQRES 23 B 301 THR TYR LEU PRO GLU LYS ILE LYS ASP GLU SER THR TRP
SEQRES 24 B 301 LEU PRO
HET NA A 370 1
HET MG A 371 1
HET MG A 372 1
HET NA B 373 1
HET MG B 374 1
HETNAM NA SODIUM ION
HETNAM MG MAGNESIUM ION
FORMUL 3 NA 2(NA 1+)
FORMUL 4 MG 3(MG 2+)
FORMUL 8 HOH *326(H2 O)
HELIX 1 1 GLN A 72 THR A 92 1 21
HELIX 2 2 LEU A 98 SER A 105 1 8
HELIX 3 3 LYS A 106 ARG A 112 5 7
HELIX 4 4 ASP A 115 GLY A 131 1 17
HELIX 5 5 LEU A 133 LEU A 137 5 5
HELIX 6 6 THR A 198 GLU A 208 1 11
HELIX 7 7 ARG A 209 HIS A 214 1 6
HELIX 8 8 ALA A 226 ASP A 241 1 16
HELIX 9 9 ASP A 251 ASN A 257 1 7
HELIX 10 10 ASN A 257 VAL A 264 1 8
HELIX 11 11 THR A 287 TYR A 294 1 8
HELIX 12 12 LYS A 302 ASP A 316 1 15
HELIX 13 13 ASP A 316 SER A 321 1 6
HELIX 14 14 PHE A 322 GLY A 336 1 15
HELIX 15 15 GLU A 340 GLY A 348 5 9
HELIX 16 16 LYS A 350 THR A 355 1 6
HELIX 17 17 THR A 355 ASP A 363 1 9
HELIX 18 18 GLU A 364 TRP A 367 5 4
SHEET 1 A 2 SER A 96 THR A 97 0
SHEET 2 A 2 PHE A 139 ILE A 140 1 N ILE A 140 O SER A 96
SHEET 1 B 6 ARG A 282 GLY A 285 0
SHEET 2 B 6 VAL A 244 PHE A 247 1 O VAL A 244 N ARG A 282
SHEET 3 B 6 PHE A 192 ILE A 196 1 O ILE A 193 N LEU A 245
SHEET 4 B 6 CYS A 216 SER A 220 1 O ILE A 217 N LEU A 194
SHEET 5 B 6 SER A 147 VAL A 149 -1 O SER A 147 N SER A 220
SHEET 6 B 6 ALA A 174 ASN A 176 -1 N TYR A 175 O VAL A 148
SHEET 1 C 3 GLY A 161 ASP A 166 0
SHEET 2 C 3 LYS A 153 THR A 158 -1 N ILE A 154 O VAL A 165
SHEET 3 C 3 ASN A 185 GLU A 187 -1 O ASN A 185 N ILE A 155
SHEET 1 D 2 HIS A 299 PRO A 300 0
SHEET 2 D 2 VAL A 337 ARG A 338 -1 N ARG A 338 O HIS A 299
LINK OE2 GLU A 197 MG MG A 371 1555 1555 2.01
LINK OD2 ASP A 249 MG MG A 371 1555 1555 2.11
LINK MG MG A 371 O HOH A 381 1555 1555 2.21
LINK MG MG A 371 O HOH A 399 1555 1555 2.24
LINK MG MG A 371 O HOH A 463 1555 1555 2.23
LINK MG MG A 371 O HOH A 511 1555 1555 2.15
LINK MG MG A 372 O HOH A 394 1555 1555 2.13
LINK MG MG A 372 O HOH A 426 1555 1555 2.33
LINK MG MG A 372 O HOH A 490 1555 1555 2.17
LINK MG MG A 372 O HOH B 376 1555 1555 2.19
LINK MG MG A 372 O HOH B 379 1555 1555 2.10
LINK MG MG A 372 O HOH B 451 1555 1555 2.19
LINK OE2 GLU B 197 MG MG B 374 1555 1555 1.97
LINK OD2 ASP B 249 MG MG B 374 1555 1555 2.06
LINK MG MG B 374 O HOH B 413 1555 1555 2.20
LINK MG MG B 374 O HOH B 417 1555 1555 2.21
LINK MG MG B 374 O HOH B 426 1555 1555 2.08
LINK MG MG B 374 O HOH B 501 1555 1555 2.23
CISPEP 1 GLY A 285 VAL A 286 0 -9.24
CISPEP 2 GLY B 285 VAL B 286 0 -25.57
SITE 1 AC1 3 LYS A 74 GLN A 78 ASP A 114
SITE 1 AC2 6 GLU A 197 ASP A 249 HOH A 381 HOH A 399
SITE 2 AC2 6 HOH A 463 HOH A 511
SITE 1 AC3 6 HOH A 394 HOH A 426 HOH A 490 HOH B 376
SITE 2 AC3 6 HOH B 379 HOH B 451
SITE 1 AC4 3 LYS B 74 GLN B 78 ASP B 114
SITE 1 AC5 6 GLU B 197 ASP B 249 HOH B 413 HOH B 417
SITE 2 AC5 6 HOH B 426 HOH B 501
CRYST1 66.510 59.040 87.260 90.00 94.05 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 0.015035 0.000000 0.001065 0.00000
SCALE2 0.000000 0.016938 0.000000 0.00000
SCALE3 0.000000 0.000000 0.011489 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
