HEADER TRANSCRIPTION 21-APR-14 3WU0
TITLE CRYSTAL STRUCTURE OF PHOSPHORYLATED ETS-1 DNA BINDING AND
TITLE 2 AUTOINHIBITORY DOMAINS (276-441)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PROTEIN C-ETS-1;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: UNP RESIDUES 276-441;
COMPND 5 SYNONYM: P54;
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: ETS1, EWSR2;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET23A
KEYWDS PHOSPHORYLATION, TRANSCRIPTION, ETS-1, AUTOINHIBITION, ETS DOMAIN,
KEYWDS 2 DNA-BINDING, ISOPEPTIDE BOND, NUCLEUS, PHOSPHOPROTEIN, PROTO-
KEYWDS 3 ONCOGENE, TRANSCRIPTION REGULATION
EXPDTA X-RAY DIFFRACTION
AUTHOR M.SHIINA,K.HAMADA,K.OGATA
REVDAT 4 08-NOV-23 3WU0 1 REMARK
REVDAT 3 24-AUG-22 3WU0 1 JRNL
REVDAT 2 22-NOV-17 3WU0 1 REMARK
REVDAT 1 20-AUG-14 3WU0 0
JRNL AUTH M.SHIINA,K.HAMADA,T.INOUE-BUNGO,M.SHIMAMURA,A.UCHIYAMA,
JRNL AUTH 2 S.BABA,K.SATO,M.YAMAMOTO,K.OGATA
JRNL TITL A NOVEL ALLOSTERIC MECHANISM ON PROTEIN-DNA INTERACTIONS
JRNL TITL 2 UNDERLYING THE PHOSPHORYLATION-DEPENDENT REGULATION OF ETS1
JRNL TITL 3 TARGET GENE EXPRESSIONS.
JRNL REF J.MOL.BIOL. V. 427 1655 2015
JRNL REFN ESSN 1089-8638
JRNL PMID 25083921
JRNL DOI 10.1016/J.JMB.2014.07.020
REMARK 2
REMARK 2 RESOLUTION. 2.60 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS
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 : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.60
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 36.02
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 553586.000
REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0000
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 99.8
REMARK 3 NUMBER OF REFLECTIONS : 11718
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) : 0.222
REMARK 3 FREE R VALUE : 0.277
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 603
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.011
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) : 2.60
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.76
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 100.0
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 1843
REMARK 3 BIN R VALUE (WORKING SET) : 0.3360
REMARK 3 BIN FREE R VALUE : 0.3910
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 4.80
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 93
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.041
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2263
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 21
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 75.50
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 7.44000
REMARK 3 B22 (A**2) : 7.44000
REMARK 3 B33 (A**2) : -14.89000
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) : 0.35
REMARK 3 ESD FROM SIGMAA (A) : 0.33
REMARK 3 LOW RESOLUTION CUTOFF (A) : 5.00
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : 0.43
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.40
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.007
REMARK 3 BOND ANGLES (DEGREES) : 1.000
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 21.60
REMARK 3 IMPROPER ANGLES (DEGREES) : 0.740
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) : 1.670 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 2.990 ; 2.000
REMARK 3 SIDE-CHAIN BOND (A**2) : 1.980 ; 2.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 3.080 ; 2.500
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : FLAT MODEL
REMARK 3 KSOL : 0.35
REMARK 3 BSOL : 63.27
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.PARAM
REMARK 3 PARAMETER FILE 2 : WATER_REP.PARAM
REMARK 3 PARAMETER FILE 3 : NULL
REMARK 3 TOPOLOGY FILE 1 : PROTEIN.TOP
REMARK 3 TOPOLOGY FILE 2 : WATER.TOP
REMARK 3 TOPOLOGY FILE 3 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: BULK SOLVENT MODEL USED
REMARK 4
REMARK 4 3WU0 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 22-MAY-14.
REMARK 100 THE DEPOSITION ID IS D_1000096790.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 09-JUN-06
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 : PHOTON FACTORY
REMARK 200 BEAMLINE : AR-NW12A
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 210
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000, DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 11771
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.600
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 200 DATA REDUNDANCY : 5.600
REMARK 200 R MERGE (I) : 0.04400
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 19.0000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.60
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.69
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 5.30
REMARK 200 R MERGE FOR SHELL (I) : 0.43500
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: CNS
REMARK 200 STARTING MODEL: PDB ENTRY 1GVJ
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 51.95
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.56
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 5% PEG 3000, 25% MPD, 0.1M HEPES, PH
REMARK 280 7.5, VAPOR DIFFUSION, SITTING DROP
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 31
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+1/3
REMARK 290 3555 -X+Y,-X,Z+2/3
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 35.32800
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 70.65600
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: 1370 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 15660 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -12.0 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 SER A 276
REMARK 465 LEU A 277
REMARK 465 GLN A 278
REMARK 465 ARG A 279
REMARK 465 VAL A 280
REMARK 465 PRO A 281
REMARK 465 SER A 282
REMARK 465 TYR A 283
REMARK 465 ASP A 284
REMARK 465 SER A 285
REMARK 465 PHE A 286
REMARK 465 ASP A 287
REMARK 465 SER A 288
REMARK 465 GLU A 289
REMARK 465 ASP A 290
REMARK 465 TYR A 291
REMARK 465 PRO A 292
REMARK 465 ALA A 293
REMARK 465 ALA A 294
REMARK 465 LEU A 295
REMARK 465 PRO A 296
REMARK 465 ASN A 297
REMARK 465 HIS A 298
REMARK 465 LYS A 299
REMARK 465 PRO A 300
REMARK 465 GLU A 441
REMARK 465 SER B 276
REMARK 465 LEU B 277
REMARK 465 GLN B 278
REMARK 465 ARG B 279
REMARK 465 VAL B 280
REMARK 465 PRO B 281
REMARK 465 SER B 282
REMARK 465 TYR B 283
REMARK 465 ASP B 284
REMARK 465 SER B 285
REMARK 465 PHE B 286
REMARK 465 ASP B 287
REMARK 465 SER B 288
REMARK 465 GLU B 289
REMARK 465 ASP B 290
REMARK 465 TYR B 291
REMARK 465 PRO B 292
REMARK 465 ALA B 293
REMARK 465 ALA B 294
REMARK 465 LEU B 295
REMARK 465 PRO B 296
REMARK 465 ASN B 297
REMARK 465 HIS B 298
REMARK 465 LYS B 299
REMARK 465 PRO B 300
REMARK 465 PRO B 437
REMARK 465 ASP B 438
REMARK 465 ALA B 439
REMARK 465 ASP B 440
REMARK 465 GLU B 441
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 ASP A 440 CG OD1 OD2
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 316 179.88 -59.60
REMARK 500 ILE A 321 76.06 -111.81
REMARK 500 GLN A 351 -3.29 -59.58
REMARK 500 LEU B 314 -90.48 -100.65
REMARK 500 ASN B 315 99.16 -54.24
REMARK 500 ASP B 317 84.16 -157.32
REMARK 500 SER B 349 1.21 -55.98
REMARK 500 GLN B 351 3.98 -59.92
REMARK 500 ILE B 354 127.53 177.82
REMARK 500 LYS B 381 66.87 -118.44
REMARK 500 PRO B 382 -0.29 -58.63
REMARK 500 ASN B 385 -159.26 -107.84
REMARK 500 ARG B 409 -57.64 -134.22
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3WTS RELATED DB: PDB
REMARK 900 RELATED ID: 3WTT RELATED DB: PDB
REMARK 900 RELATED ID: 3WTU RELATED DB: PDB
REMARK 900 RELATED ID: 3WTV RELATED DB: PDB
REMARK 900 RELATED ID: 3WTW RELATED DB: PDB
REMARK 900 RELATED ID: 3WTX RELATED DB: PDB
REMARK 900 RELATED ID: 3WTY RELATED DB: PDB
REMARK 900 RELATED ID: 3WTZ RELATED DB: PDB
REMARK 900 RELATED ID: 3WU1 RELATED DB: PDB
DBREF 3WU0 A 276 441 UNP P14921 ETS1_HUMAN 276 441
DBREF 3WU0 B 276 441 UNP P14921 ETS1_HUMAN 276 441
SEQRES 1 A 166 SER LEU GLN ARG VAL PRO SER TYR ASP SER PHE ASP SER
SEQRES 2 A 166 GLU ASP TYR PRO ALA ALA LEU PRO ASN HIS LYS PRO LYS
SEQRES 3 A 166 GLY THR PHE LYS ASP TYR VAL ARG ASP ARG ALA ASP LEU
SEQRES 4 A 166 ASN LYS ASP LYS PRO VAL ILE PRO ALA ALA ALA LEU ALA
SEQRES 5 A 166 GLY TYR THR GLY SER GLY PRO ILE GLN LEU TRP GLN PHE
SEQRES 6 A 166 LEU LEU GLU LEU LEU THR ASP LYS SER CYS GLN SER PHE
SEQRES 7 A 166 ILE SER TRP THR GLY ASP GLY TRP GLU PHE LYS LEU SER
SEQRES 8 A 166 ASP PRO ASP GLU VAL ALA ARG ARG TRP GLY LYS ARG LYS
SEQRES 9 A 166 ASN LYS PRO LYS MET ASN TYR GLU LYS LEU SER ARG GLY
SEQRES 10 A 166 LEU ARG TYR TYR TYR ASP LYS ASN ILE ILE HIS LYS THR
SEQRES 11 A 166 ALA GLY LYS ARG TYR VAL TYR ARG PHE VAL CYS ASP LEU
SEQRES 12 A 166 GLN SER LEU LEU GLY TYR THR PRO GLU GLU LEU HIS ALA
SEQRES 13 A 166 MET LEU ASP VAL LYS PRO ASP ALA ASP GLU
SEQRES 1 B 166 SER LEU GLN ARG VAL PRO SER TYR ASP SER PHE ASP SER
SEQRES 2 B 166 GLU ASP TYR PRO ALA ALA LEU PRO ASN HIS LYS PRO LYS
SEQRES 3 B 166 GLY THR PHE LYS ASP TYR VAL ARG ASP ARG ALA ASP LEU
SEQRES 4 B 166 ASN LYS ASP LYS PRO VAL ILE PRO ALA ALA ALA LEU ALA
SEQRES 5 B 166 GLY TYR THR GLY SER GLY PRO ILE GLN LEU TRP GLN PHE
SEQRES 6 B 166 LEU LEU GLU LEU LEU THR ASP LYS SER CYS GLN SER PHE
SEQRES 7 B 166 ILE SER TRP THR GLY ASP GLY TRP GLU PHE LYS LEU SER
SEQRES 8 B 166 ASP PRO ASP GLU VAL ALA ARG ARG TRP GLY LYS ARG LYS
SEQRES 9 B 166 ASN LYS PRO LYS MET ASN TYR GLU LYS LEU SER ARG GLY
SEQRES 10 B 166 LEU ARG TYR TYR TYR ASP LYS ASN ILE ILE HIS LYS THR
SEQRES 11 B 166 ALA GLY LYS ARG TYR VAL TYR ARG PHE VAL CYS ASP LEU
SEQRES 12 B 166 GLN SER LEU LEU GLY TYR THR PRO GLU GLU LEU HIS ALA
SEQRES 13 B 166 MET LEU ASP VAL LYS PRO ASP ALA ASP GLU
FORMUL 3 HOH *21(H2 O)
HELIX 1 1 THR A 303 ASP A 310 1 8
HELIX 2 2 PRO A 322 GLY A 331 1 10
HELIX 3 3 GLN A 336 THR A 346 1 11
HELIX 4 4 ASP A 347 GLN A 351 5 5
HELIX 5 5 ASP A 367 LYS A 379 1 13
HELIX 6 6 ASN A 385 LYS A 399 1 15
HELIX 7 7 ASP A 417 GLY A 423 1 7
HELIX 8 8 THR A 425 LEU A 433 1 9
HELIX 9 9 THR B 303 LEU B 314 1 12
HELIX 10 10 PRO B 322 THR B 330 1 9
HELIX 11 11 GLN B 336 THR B 346 1 11
HELIX 12 12 ASP B 347 GLN B 351 5 5
HELIX 13 13 ASP B 367 LYS B 379 1 13
HELIX 14 14 TYR B 386 LYS B 399 1 14
HELIX 15 15 ASP B 417 GLY B 423 1 7
HELIX 16 16 THR B 425 LEU B 433 1 9
SHEET 1 A 4 ILE A 354 TRP A 356 0
SHEET 2 A 4 GLU A 362 LEU A 365 -1 O LYS A 364 N SER A 355
SHEET 3 A 4 VAL A 411 PHE A 414 -1 O TYR A 412 N PHE A 363
SHEET 4 A 4 ILE A 402 LYS A 404 -1 N HIS A 403 O ARG A 413
SHEET 1 B 4 SER B 355 TRP B 356 0
SHEET 2 B 4 GLU B 362 LYS B 364 -1 O LYS B 364 N SER B 355
SHEET 3 B 4 VAL B 411 PHE B 414 -1 O TYR B 412 N PHE B 363
SHEET 4 B 4 ILE B 402 LYS B 404 -1 N HIS B 403 O ARG B 413
CRYST1 56.710 56.710 105.984 90.00 90.00 120.00 P 31 6
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 0.017634 0.010181 0.000000 0.00000
SCALE2 0.000000 0.020361 0.000000 0.00000
SCALE3 0.000000 0.000000 0.009435 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
