HEADER BIOSYNTHETIC PROTEIN 19-DEC-08 3FM0
TITLE CRYSTAL STRUCTURE OF WD40 PROTEIN CIAO1
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PROTEIN CIAO1;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: WD REPEAT-CONTAINING PROTEIN 39;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_TAXID: 9606;
SOURCE 4 GENE: CIAO1, WDR39;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21 ROSETTA-R3;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PET28A
KEYWDS WDR39, SGC, WD40, CIAO1, NUCLEUS, WD REPEAT, BIOSYNTHETIC PROTEIN,
KEYWDS 2 STRUCTURAL GENOMICS, STRUCTURAL GENOMICS CONSORTIUM
EXPDTA X-RAY DIFFRACTION
AUTHOR A.DONG,M.RAVICHANDRAN,L.CROMBET,D.COSSAR,A.M.EDWARDS,C.H.ARROWSMITH,
AUTHOR 2 J.WEIGELT,C.BOUNTRA,A.BOCHKAREV,J.MIN,H.OUYANG,STRUCTURAL GENOMICS
AUTHOR 3 CONSORTIUM (SGC)
REVDAT 3 06-SEP-23 3FM0 1 SEQADV
REVDAT 2 20-APR-11 3FM0 1 JRNL
REVDAT 1 10-FEB-09 3FM0 0
JRNL AUTH C.XU,J.MIN
JRNL TITL STRUCTURE AND FUNCTION OF WD40 DOMAIN PROTEINS.
JRNL REF PROTEIN CELL V. 2 202 2011
JRNL REFN ISSN 1674-800X
JRNL PMID 21468892
JRNL DOI 10.1007/S13238-011-1018-1
REMARK 2
REMARK 2 RESOLUTION. 1.70 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.2.0019
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.70
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 47.78
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 95.6
REMARK 3 NUMBER OF REFLECTIONS : 29897
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 + TEST SET) : 0.161
REMARK 3 R VALUE (WORKING SET) : 0.160
REMARK 3 FREE R VALUE : 0.196
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 2.600
REMARK 3 FREE R VALUE TEST SET COUNT : 791
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 1.70
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.75
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1540
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 67.26
REMARK 3 BIN R VALUE (WORKING SET) : 0.2180
REMARK 3 BIN FREE R VALUE SET COUNT : 42
REMARK 3 BIN FREE R VALUE : 0.2840
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2538
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 5
REMARK 3 SOLVENT ATOMS : 392
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 17.90
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 18.73
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.36000
REMARK 3 B22 (A**2) : 0.23000
REMARK 3 B33 (A**2) : 0.25000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.22000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.112
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.107
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.070
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 2.057
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.966
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.952
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 2613 ; 0.009 ; 0.021
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 3569 ; 1.232 ; 1.911
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 325 ; 6.344 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 118 ;31.256 ;23.983
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 385 ;11.658 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 14 ;12.926 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 386 ; 0.083 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 2014 ; 0.005 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 1140 ; 0.195 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 1739 ; 0.298 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 302 ; 0.122 ; 0.200
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): 59 ; 0.193 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 39 ; 0.140 ; 0.200
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 1677 ; 0.763 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 2614 ; 1.229 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1132 ; 1.845 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 955 ; 2.825 ; 4.500
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.40
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS
REMARK 4
REMARK 4 3FM0 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 23-DEC-08.
REMARK 100 THE DEPOSITION ID IS D_1000050754.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 14-DEC-08
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 19-ID
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9792
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-3000
REMARK 200 DATA SCALING SOFTWARE : HKL-3000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 30710
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.700
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 (%) : 95.7
REMARK 200 DATA REDUNDANCY : 5.500
REMARK 200 R MERGE (I) : 0.06000
REMARK 200 R SYM (I) : 0.06000
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 12.5000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.70
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.76
REMARK 200 COMPLETENESS FOR SHELL (%) : 66.5
REMARK 200 DATA REDUNDANCY IN SHELL : 3.40
REMARK 200 R MERGE FOR SHELL (I) : 0.42100
REMARK 200 R SYM FOR SHELL (I) : 0.42100
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.620
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: PDB ENTRY 2HES
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 35.95
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.92
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 25% PEG 3350, 0.1M (NH4)2SO4, 0.1M BIS
REMARK 280 -TRIS, PH6.0, 8% 2,2,2-TRIFLURO ETHANOL, VAPOR DIFFUSION,
REMARK 280 SITTING DROP, TEMPERATURE 297K
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 37.32000
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: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
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 MET A 1
REMARK 465 LYS A 2
REMARK 465 ASP A 3
REMARK 465 ASP A 93
REMARK 465 GLY A 236
REMARK 465 SER A 237
REMARK 465 ASP A 238
REMARK 465 PRO A 336
REMARK 465 GLU A 337
REMARK 465 GLY A 338
REMARK 465 LEU A 339
REMARK 465 HIS A 340
REMARK 465 HIS A 341
REMARK 465 HIS A 342
REMARK 465 HIS A 343
REMARK 465 HIS A 344
REMARK 465 HIS A 345
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 ARG A 39 NE CZ NH1 NH2
REMARK 470 LYS A 53 CE NZ
REMARK 470 GLU A 58 CG CD OE1 OE2
REMARK 470 ASN A 91 CG OD1 ND2
REMARK 470 GLN A 92 CG CD OE1 NE2
REMARK 470 ASP A 94 CG OD1 OD2
REMARK 470 THR A 99 CG2
REMARK 470 ASP A 138 CG OD1 OD2
REMARK 470 GLU A 180 CD OE1 OE2
REMARK 470 GLU A 181 CB CG CD OE1 OE2
REMARK 470 ASP A 182 CG OD1 OD2
REMARK 470 ARG A 335 CG CD NE CZ NH1 NH2
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 NH2 ARG A 222 OE1 GLN A 288 2.12
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 THR A 63 131.18 -32.69
REMARK 500 ASP A 152 121.50 -27.98
REMARK 500 SER A 161 -30.40 -136.62
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 SO4 A2003
DBREF 3FM0 A 1 339 UNP O76071 CIAO1_HUMAN 1 339
SEQADV 3FM0 HIS A 340 UNP O76071 EXPRESSION TAG
SEQADV 3FM0 HIS A 341 UNP O76071 EXPRESSION TAG
SEQADV 3FM0 HIS A 342 UNP O76071 EXPRESSION TAG
SEQADV 3FM0 HIS A 343 UNP O76071 EXPRESSION TAG
SEQADV 3FM0 HIS A 344 UNP O76071 EXPRESSION TAG
SEQADV 3FM0 HIS A 345 UNP O76071 EXPRESSION TAG
SEQRES 1 A 345 MET LYS ASP SER LEU VAL LEU LEU GLY ARG VAL PRO ALA
SEQRES 2 A 345 HIS PRO ASP SER ARG CYS TRP PHE LEU ALA TRP ASN PRO
SEQRES 3 A 345 ALA GLY THR LEU LEU ALA SER CYS GLY GLY ASP ARG ARG
SEQRES 4 A 345 ILE ARG ILE TRP GLY THR GLU GLY ASP SER TRP ILE CYS
SEQRES 5 A 345 LYS SER VAL LEU SER GLU GLY HIS GLN ARG THR VAL ARG
SEQRES 6 A 345 LYS VAL ALA TRP SER PRO CYS GLY ASN TYR LEU ALA SER
SEQRES 7 A 345 ALA SER PHE ASP ALA THR THR CYS ILE TRP LYS LYS ASN
SEQRES 8 A 345 GLN ASP ASP PHE GLU CYS VAL THR THR LEU GLU GLY HIS
SEQRES 9 A 345 GLU ASN GLU VAL LYS SER VAL ALA TRP ALA PRO SER GLY
SEQRES 10 A 345 ASN LEU LEU ALA THR CYS SER ARG ASP LYS SER VAL TRP
SEQRES 11 A 345 VAL TRP GLU VAL ASP GLU GLU ASP GLU TYR GLU CYS VAL
SEQRES 12 A 345 SER VAL LEU ASN SER HIS THR GLN ASP VAL LYS HIS VAL
SEQRES 13 A 345 VAL TRP HIS PRO SER GLN GLU LEU LEU ALA SER ALA SER
SEQRES 14 A 345 TYR ASP ASP THR VAL LYS LEU TYR ARG GLU GLU GLU ASP
SEQRES 15 A 345 ASP TRP VAL CYS CYS ALA THR LEU GLU GLY HIS GLU SER
SEQRES 16 A 345 THR VAL TRP SER LEU ALA PHE ASP PRO SER GLY GLN ARG
SEQRES 17 A 345 LEU ALA SER CYS SER ASP ASP ARG THR VAL ARG ILE TRP
SEQRES 18 A 345 ARG GLN TYR LEU PRO GLY ASN GLU GLN GLY VAL ALA CYS
SEQRES 19 A 345 SER GLY SER ASP PRO SER TRP LYS CYS ILE CYS THR LEU
SEQRES 20 A 345 SER GLY PHE HIS SER ARG THR ILE TYR ASP ILE ALA TRP
SEQRES 21 A 345 CYS GLN LEU THR GLY ALA LEU ALA THR ALA CYS GLY ASP
SEQRES 22 A 345 ASP ALA ILE ARG VAL PHE GLN GLU ASP PRO ASN SER ASP
SEQRES 23 A 345 PRO GLN GLN PRO THR PHE SER LEU THR ALA HIS LEU HIS
SEQRES 24 A 345 GLN ALA HIS SER GLN ASP VAL ASN CYS VAL ALA TRP ASN
SEQRES 25 A 345 PRO LYS GLU PRO GLY LEU LEU ALA SER CYS SER ASP ASP
SEQRES 26 A 345 GLY GLU VAL ALA PHE TRP LYS TYR GLN ARG PRO GLU GLY
SEQRES 27 A 345 LEU HIS HIS HIS HIS HIS HIS
HET SO4 A2003 5
HETNAM SO4 SULFATE ION
FORMUL 2 SO4 O4 S 2-
FORMUL 3 HOH *392(H2 O)
SHEET 1 A 4 LEU A 5 VAL A 11 0
SHEET 2 A 4 VAL A 328 TYR A 333 -1 O PHE A 330 N LEU A 8
SHEET 3 A 4 LEU A 318 SER A 323 -1 N LEU A 319 O TRP A 331
SHEET 4 A 4 VAL A 306 TRP A 311 -1 N ALA A 310 O ALA A 320
SHEET 1 B 4 CYS A 19 TRP A 24 0
SHEET 2 B 4 LEU A 31 GLY A 35 -1 O ALA A 32 N ALA A 23
SHEET 3 B 4 ILE A 40 GLU A 46 -1 O TRP A 43 N LEU A 31
SHEET 4 B 4 SER A 49 LEU A 56 -1 O LEU A 56 N ILE A 40
SHEET 1 C 4 VAL A 64 TRP A 69 0
SHEET 2 C 4 TYR A 75 SER A 80 -1 O ALA A 77 N ALA A 68
SHEET 3 C 4 THR A 85 LYS A 90 -1 O TRP A 88 N LEU A 76
SHEET 4 C 4 PHE A 95 LEU A 101 -1 O LEU A 101 N THR A 85
SHEET 1 D 4 VAL A 108 TRP A 113 0
SHEET 2 D 4 LEU A 119 SER A 124 -1 O ALA A 121 N ALA A 112
SHEET 3 D 4 VAL A 129 VAL A 134 -1 O TRP A 132 N LEU A 120
SHEET 4 D 4 TYR A 140 LEU A 146 -1 O LEU A 146 N VAL A 129
SHEET 1 E 4 VAL A 153 TRP A 158 0
SHEET 2 E 4 LEU A 165 SER A 169 -1 O ALA A 166 N VAL A 157
SHEET 3 E 4 VAL A 174 GLU A 180 -1 O TYR A 177 N LEU A 165
SHEET 4 E 4 ASP A 183 LEU A 190 -1 O LEU A 190 N VAL A 174
SHEET 1 F 4 VAL A 197 PHE A 202 0
SHEET 2 F 4 ARG A 208 SER A 213 -1 O ALA A 210 N ALA A 201
SHEET 3 F 4 VAL A 218 TYR A 224 -1 O TRP A 221 N LEU A 209
SHEET 4 F 4 SER A 240 LEU A 247 -1 O SER A 240 N TYR A 224
SHEET 1 G 4 ILE A 255 TRP A 260 0
SHEET 2 G 4 LEU A 267 CYS A 271 -1 O ALA A 268 N ALA A 259
SHEET 3 G 4 ILE A 276 GLU A 281 -1 O PHE A 279 N LEU A 267
SHEET 4 G 4 PHE A 292 LEU A 298 -1 O THR A 295 N VAL A 278
SITE 1 AC1 6 ARG A 62 THR A 63 PHE A 81 HOH A 370
SITE 2 AC1 6 HOH A 597 HOH A 724
CRYST1 41.682 74.640 49.481 90.00 105.05 90.00 P 1 21 1 2
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 0.023991 0.000000 0.006450 0.00000
SCALE2 0.000000 0.013398 0.000000 0.00000
SCALE3 0.000000 0.000000 0.020927 0.00000
(ATOM LINES ARE NOT SHOWN.)
END