HEADER TRANSFERASE 26-JAN-11 3QHP
TITLE CRYSTAL STRUCTURE OF THE CATALYTIC DOMAIN OF CHOLESTEROL-ALPHA-
TITLE 2 GLUCOSYLTRANSFERASE FROM HELICOBACTER PYLORI
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: TYPE 1 CAPSULAR POLYSACCHARIDE BIOSYNTHESIS PROTEIN J
COMPND 3 (CAPJ);
COMPND 4 CHAIN: A, B;
COMPND 5 FRAGMENT: CATALYTIC DOMAIN, RESIDUES 201-366;
COMPND 6 SYNONYM: CHOLESTEROL-ALPHA-GLUCOSYLTRANSFERASE;
COMPND 7 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HELICOBACTER PYLORI;
SOURCE 3 ORGANISM_COMMON: CAMPYLOBACTER PYLORI;
SOURCE 4 ORGANISM_TAXID: 85962;
SOURCE 5 STRAIN: ATCC 26695;
SOURCE 6 GENE: HP0421;
SOURCE 7 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 9 EXPRESSION_SYSTEM_STRAIN: ROSETTA2(DE3)PLYSS;
SOURCE 10 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 11 EXPRESSION_SYSTEM_PLASMID: PET-21A(+)
KEYWDS ROSSMANN FOLD, GLYCOSYLTRANSFERASE, TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR S.J.LEE,B.I.LEE,S.W.SUH
REVDAT 2 20-MAR-24 3QHP 1 REMARK
REVDAT 1 29-JUN-11 3QHP 0
JRNL AUTH S.J.LEE,B.I.LEE,S.W.SUH
JRNL TITL CRYSTAL STRUCTURE OF THE CATALYTIC DOMAIN OF
JRNL TITL 2 CHOLESTEROL-ALPHA-GLUCOSYLTRANSFERASE FROM HELICOBACTER
JRNL TITL 3 PYLORI
JRNL REF PROTEINS V. 79 2321 2011
JRNL REFN ISSN 0887-3585
JRNL PMID 21557320
JRNL DOI 10.1002/PROT.23038
REMARK 2
REMARK 2 RESOLUTION. 1.50 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.5.0102
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) : 1.50
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 19.94
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 96.0
REMARK 3 NUMBER OF REFLECTIONS : 43082
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) : 0.198
REMARK 3 R VALUE (WORKING SET) : 0.196
REMARK 3 FREE R VALUE : 0.227
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 2306
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) : 1.50
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.54
REMARK 3 REFLECTION IN BIN (WORKING SET) : 3076
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 93.50
REMARK 3 BIN R VALUE (WORKING SET) : 0.2310
REMARK 3 BIN FREE R VALUE SET COUNT : 158
REMARK 3 BIN FREE R VALUE : 0.2670
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2440
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 280
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 17.49
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.10000
REMARK 3 B22 (A**2) : -0.11000
REMARK 3 B33 (A**2) : -0.28000
REMARK 3 B12 (A**2) : 0.12000
REMARK 3 B13 (A**2) : -0.27000
REMARK 3 B23 (A**2) : -0.62000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.090
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.089
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.053
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 1.368
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.953
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.933
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 2552 ; 0.010 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 3454 ; 1.315 ; 1.982
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 328 ; 6.577 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 103 ;38.658 ;25.437
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 499 ;12.615 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 10 ;16.810 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 402 ; 0.086 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 1847 ; 0.006 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL
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): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL
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): 1592 ; 0.766 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 2571 ; 1.413 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 960 ; 2.012 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 877 ; 3.408 ; 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 3QHP COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 31-JAN-11.
REMARK 100 THE DEPOSITION ID IS D_1000063658.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 23-NOV-08; 28-NOV-08
REMARK 200 TEMPERATURE (KELVIN) : 100; 100
REMARK 200 PH : 7.5
REMARK 200 NUMBER OF CRYSTALS USED : 2
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y; Y
REMARK 200 RADIATION SOURCE : PHOTON FACTORY; PHOTON FACTORY
REMARK 200 BEAMLINE : BL-5A; BL-5A
REMARK 200 X-RAY GENERATOR MODEL : NULL; NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M; M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0000; 0.9194, 0.9196, 0.9062
REMARK 200 MONOCHROMATOR : NULL; NULL
REMARK 200 OPTICS : NULL; NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD; CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315; ADSC QUANTUM
REMARK 200 315
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 45557
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.500
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 (%) : 96.0
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) : 1.50
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.53
REMARK 200 COMPLETENESS FOR SHELL (%) : 94.3
REMARK 200 DATA REDUNDANCY IN SHELL : 3.10
REMARK 200 R MERGE FOR SHELL (I) : 0.14100
REMARK 200 R SYM FOR SHELL (I) : 0.13800
REMARK 200 <I/SIGMA(I)> FOR SHELL : 8.600
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH; MAD
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MAD
REMARK 200 SOFTWARE USED: SOLVE
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 40.21
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.06
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M HEPES (PH 7.5), 25% (W/V) PEG
REMARK 280 3350, 0.1M GLYCINE, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE
REMARK 280 297K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,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
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
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 350
REMARK 350 BIOMOLECULE: 2
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: 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 LEU A 360
REMARK 465 GLU A 361
REMARK 465 ASN A 362
REMARK 465 SER A 363
REMARK 465 VAL A 364
REMARK 465 ILE A 365
REMARK 465 GLN A 366
REMARK 465 THR B 201
REMARK 465 ASN B 264
REMARK 465 SER B 265
REMARK 465 ASN B 266
REMARK 465 GLU B 267
REMARK 465 SER B 286
REMARK 465 GLU B 287
REMARK 465 THR B 359
REMARK 465 LEU B 360
REMARK 465 GLU B 361
REMARK 465 ASN B 362
REMARK 465 SER B 363
REMARK 465 VAL B 364
REMARK 465 ILE B 365
REMARK 465 GLN B 366
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 GLU A 285 N - CA - C ANGL. DEV. = -24.8 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 PHE A 260 -153.28 -99.18
REMARK 500 ASN B 340 67.63 -115.85
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 VAL A 284 GLU A 285 -43.89
REMARK 500 GLU A 285 SER A 286 -135.14
REMARK 500
REMARK 500 REMARK: NULL
DBREF 3QHP A 201 366 UNP O25175 O25175_HELPY 201 366
DBREF 3QHP B 201 366 UNP O25175 O25175_HELPY 201 366
SEQRES 1 A 166 THR PRO PHE LYS ILE ALA MET VAL GLY ARG TYR SER ASN
SEQRES 2 A 166 GLU LYS ASN GLN SER VAL LEU ILE LYS ALA VAL ALA LEU
SEQRES 3 A 166 SER LYS TYR LYS GLN ASP ILE VAL LEU LEU LEU LYS GLY
SEQRES 4 A 166 LYS GLY PRO ASP GLU LYS LYS ILE LYS LEU LEU ALA GLN
SEQRES 5 A 166 LYS LEU GLY VAL LYS ALA GLU PHE GLY PHE VAL ASN SER
SEQRES 6 A 166 ASN GLU LEU LEU GLU ILE LEU LYS THR CYS THR LEU TYR
SEQRES 7 A 166 VAL HIS ALA ALA ASN VAL GLU SER GLU ALA ILE ALA CYS
SEQRES 8 A 166 LEU GLU ALA ILE SER VAL GLY ILE VAL PRO VAL ILE ALA
SEQRES 9 A 166 ASN SER PRO LEU SER ALA THR ARG GLN PHE ALA LEU ASP
SEQRES 10 A 166 GLU ARG SER LEU PHE GLU PRO ASN ASN ALA LYS ASP LEU
SEQRES 11 A 166 SER ALA LYS ILE ASP TRP TRP LEU GLU ASN LYS LEU GLU
SEQRES 12 A 166 ARG GLU ARG MET GLN ASN GLU TYR ALA LYS SER ALA LEU
SEQRES 13 A 166 ASN TYR THR LEU GLU ASN SER VAL ILE GLN
SEQRES 1 B 166 THR PRO PHE LYS ILE ALA MET VAL GLY ARG TYR SER ASN
SEQRES 2 B 166 GLU LYS ASN GLN SER VAL LEU ILE LYS ALA VAL ALA LEU
SEQRES 3 B 166 SER LYS TYR LYS GLN ASP ILE VAL LEU LEU LEU LYS GLY
SEQRES 4 B 166 LYS GLY PRO ASP GLU LYS LYS ILE LYS LEU LEU ALA GLN
SEQRES 5 B 166 LYS LEU GLY VAL LYS ALA GLU PHE GLY PHE VAL ASN SER
SEQRES 6 B 166 ASN GLU LEU LEU GLU ILE LEU LYS THR CYS THR LEU TYR
SEQRES 7 B 166 VAL HIS ALA ALA ASN VAL GLU SER GLU ALA ILE ALA CYS
SEQRES 8 B 166 LEU GLU ALA ILE SER VAL GLY ILE VAL PRO VAL ILE ALA
SEQRES 9 B 166 ASN SER PRO LEU SER ALA THR ARG GLN PHE ALA LEU ASP
SEQRES 10 B 166 GLU ARG SER LEU PHE GLU PRO ASN ASN ALA LYS ASP LEU
SEQRES 11 B 166 SER ALA LYS ILE ASP TRP TRP LEU GLU ASN LYS LEU GLU
SEQRES 12 B 166 ARG GLU ARG MET GLN ASN GLU TYR ALA LYS SER ALA LEU
SEQRES 13 B 166 ASN TYR THR LEU GLU ASN SER VAL ILE GLN
FORMUL 3 HOH *280(H2 O)
HELIX 1 1 ASN A 216 LEU A 226 1 11
HELIX 2 2 TYR A 229 GLN A 231 5 3
HELIX 3 3 ASP A 243 GLY A 255 1 13
HELIX 4 4 ASN A 264 LYS A 273 1 10
HELIX 5 5 ALA A 288 VAL A 297 1 10
HELIX 6 6 SER A 309 ALA A 315 5 7
HELIX 7 7 ASP A 317 ARG A 319 5 3
HELIX 8 8 ASN A 326 ASN A 340 1 15
HELIX 9 9 ASN A 340 THR A 359 1 20
HELIX 10 10 ASN B 216 SER B 227 1 12
HELIX 11 11 TYR B 229 GLN B 231 5 3
HELIX 12 12 ASP B 243 GLY B 255 1 13
HELIX 13 13 LEU B 268 LYS B 273 1 6
HELIX 14 14 ALA B 288 VAL B 297 1 10
HELIX 15 15 THR B 311 ALA B 315 5 5
HELIX 16 16 ASP B 317 ARG B 319 5 3
HELIX 17 17 ASN B 326 ASN B 340 1 15
HELIX 18 18 ASN B 340 ALA B 355 1 16
HELIX 19 19 LEU B 356 TYR B 358 5 3
SHEET 1 A 6 LYS A 257 GLU A 259 0
SHEET 2 A 6 ILE A 233 LYS A 238 1 N LEU A 235 O GLU A 259
SHEET 3 A 6 PHE A 203 VAL A 208 1 N ILE A 205 O LEU A 236
SHEET 4 A 6 LEU A 277 HIS A 280 1 O VAL A 279 N ALA A 206
SHEET 5 A 6 PRO A 301 ALA A 304 1 O ALA A 304 N HIS A 280
SHEET 6 A 6 LEU A 321 PHE A 322 1 O PHE A 322 N ILE A 303
SHEET 1 B 6 LYS B 257 GLU B 259 0
SHEET 2 B 6 ILE B 233 LYS B 238 1 N LEU B 235 O GLU B 259
SHEET 3 B 6 PHE B 203 VAL B 208 1 N ILE B 205 O LEU B 236
SHEET 4 B 6 CYS B 275 HIS B 280 1 O VAL B 279 N ALA B 206
SHEET 5 B 6 PRO B 301 ALA B 304 1 O ALA B 304 N HIS B 280
SHEET 6 B 6 LEU B 321 PHE B 322 1 O PHE B 322 N ILE B 303
CRYST1 35.786 40.714 53.738 101.44 94.87 90.58 P 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 0.027944 0.000283 0.002488 0.00000
SCALE2 0.000000 0.024563 0.005012 0.00000
SCALE3 0.000000 0.000000 0.019061 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
