HEADER VIRAL PROTEIN/APOPTOSIS 10-DEC-07 3BL2
TITLE CRYSTAL STRUCTURE OF M11, THE BCL-2 HOMOLOG OF MURINE GAMMA-
TITLE 2 HERPESVIRUS 68, COMPLEXED WITH MOUSE BECLIN1 (RESIDUES 106-124)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: V-BCL-2;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: UNP RESIDUES 5-135;
COMPND 5 SYNONYM: BCL-2 HOMOLOG, GENE 16?, M11;
COMPND 6 ENGINEERED: YES;
COMPND 7 MOL_ID: 2;
COMPND 8 MOLECULE: BECLIN-1;
COMPND 9 CHAIN: C, D;
COMPND 10 FRAGMENT: BCL-2 BINDING REGION, BH3-LIKE DOMAIN, UNP RESIDUES 106-
COMPND 11 124;
COMPND 12 SYNONYM: COILED-COIL MYOSIN-LIKE BCL2-INTERACTING PROTEIN;
COMPND 13 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MURID HERPESVIRUS 4;
SOURCE 3 ORGANISM_COMMON: MURINE HERPESVIRUS 68;
SOURCE 4 ORGANISM_TAXID: 33708;
SOURCE 5 GENE: V-BCL-2, GAMMAHV.M11, M11;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET30;
SOURCE 11 MOL_ID: 2;
SOURCE 12 ORGANISM_SCIENTIFIC: MUS MUSCULUS;
SOURCE 13 ORGANISM_COMMON: HOUSE MOUSE;
SOURCE 14 ORGANISM_TAXID: 10090;
SOURCE 15 GENE: BECN1;
SOURCE 16 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 17 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 18 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 19 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 20 EXPRESSION_SYSTEM_PLASMID: PPROEX
KEYWDS PROTEIN-PROTEIN COMPLEX, VIRAL BCL-2, BECLIN1, APOPTOSIS, M11,
KEYWDS 2 AUTOPHAGY, ANTIVIRAL DEFENSE, COILED COIL, CYTOPLASM, GOLGI
KEYWDS 3 APPARATUS, MEMBRANE, VIRAL PROTEIN-APOPTOSIS COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR B.-H.OH,J.-S.WOO,B.KU
REVDAT 5 01-NOV-23 3BL2 1 REMARK
REVDAT 4 25-OCT-17 3BL2 1 REMARK
REVDAT 3 24-FEB-09 3BL2 1 VERSN
REVDAT 2 19-FEB-08 3BL2 1 JRNL
REVDAT 1 12-FEB-08 3BL2 0
JRNL AUTH B.KU,J.-S.WOO,C.LIANG,K.-H.LEE,H.-S.HONG,X.E,K.-S.KIM,
JRNL AUTH 2 J.U.JUNG,B.-H.OH
JRNL TITL STRUCTURAL AND BIOCHEMICAL BASES FOR THE INHIBITION OF
JRNL TITL 2 AUTOPHAGY AND APOPTOSIS BY VIRAL BCL-2 OF MURINE
JRNL TITL 3 GAMMA-HERPESVIRUS 68
JRNL REF PLOS PATHOG. V. 4 E25 2008
JRNL REFN ISSN 1553-7366
JRNL PMID 18248095
JRNL DOI 10.1371/JOURNAL.PPAT.0040025
REMARK 2
REMARK 2 RESOLUTION. 2.30 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) : 2.30
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 20.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 94.1
REMARK 3 NUMBER OF REFLECTIONS : 13447
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) : 0.204
REMARK 3 FREE R VALUE : 0.247
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.800
REMARK 3 FREE R VALUE TEST SET COUNT : 684
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : NULL
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : NULL
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : NULL
REMARK 3 BIN RESOLUTION RANGE LOW (A) : NULL
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : NULL
REMARK 3 BIN FREE R VALUE : NULL
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 BIN FREE R VALUE TEST SET COUNT : NULL
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2444
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 59
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 29.91
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -7.07600
REMARK 3 B22 (A**2) : 3.28300
REMARK 3 B33 (A**2) : 3.79300
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 11.09000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM SIGMAA (A) : NULL
REMARK 3 LOW RESOLUTION CUTOFF (A) : NULL
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM C-V SIGMAA (A) : NULL
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.007
REMARK 3 BOND ANGLES (DEGREES) : 1.063
REMARK 3 DIHEDRAL ANGLES (DEGREES) : NULL
REMARK 3 IMPROPER ANGLES (DEGREES) : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : 1.553 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 2.657 ; 2.000
REMARK 3 SIDE-CHAIN BOND (A**2) : 2.267 ; 2.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 3.366 ; 2.500
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : NULL
REMARK 3 KSOL : NULL
REMARK 3 BSOL : 32.02
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 : ION.PARAM
REMARK 3 PARAMETER FILE 4 : NULL
REMARK 3 TOPOLOGY FILE 1 : NULL
REMARK 3 TOPOLOGY FILE 2 : NULL
REMARK 3 TOPOLOGY FILE 3 : NULL
REMARK 3 TOPOLOGY FILE 4 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 3BL2 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 13-DEC-07.
REMARK 100 THE DEPOSITION ID IS D_1000045652.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 20-SEP-06
REMARK 200 TEMPERATURE (KELVIN) : 193
REMARK 200 PH : 7.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : PAL/PLS
REMARK 200 BEAMLINE : 4A
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.000
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 : DENZO, HKL-2000
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK, HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 13513
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.300
REMARK 200 RESOLUTION RANGE LOW (A) : 30.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 94.0
REMARK 200 DATA REDUNDANCY : 4.900
REMARK 200 R MERGE (I) : 0.06400
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 14.4000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.30
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.38
REMARK 200 COMPLETENESS FOR SHELL (%) : 80.5
REMARK 200 DATA REDUNDANCY IN SHELL : 3.30
REMARK 200 R MERGE FOR SHELL (I) : 0.16200
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: MOLREP
REMARK 200 STARTING MODEL: PDB ENTRY 2ABO
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 46.91
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.32
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 25% PEG 3350, 0.2M MGCL2, PH 7.0,
REMARK 280 VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 298K
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 26.80050
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3
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: 1860 ANGSTROM**2
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, C
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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 1810 ANGSTROM**2
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, D
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: 3
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 5130 ANGSTROM**2
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, C
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 APPLY THE FOLLOWING TO CHAINS: B, D
REMARK 350 BIOMT1 2 -1.000000 0.000000 0.000000 20.68627
REMARK 350 BIOMT2 2 0.000000 1.000000 0.000000 -26.80050
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 70.16475
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 CYS A 29 127.60 -37.53
REMARK 500 LEU B 134 30.40 -84.59
REMARK 500 ILE C 123 -93.08 -96.36
REMARK 500 ASP D 122 -72.84 -26.72
REMARK 500
REMARK 500 REMARK: NULL
DBREF 3BL2 A 5 135 UNP P89884 P89884_MHV68 5 135
DBREF 3BL2 B 5 135 UNP P89884 P89884_MHV68 5 135
DBREF 3BL2 C 106 124 UNP O88597 BECN1_MOUSE 106 124
DBREF 3BL2 D 106 124 UNP O88597 BECN1_MOUSE 106 124
SEQRES 1 A 131 LYS SER GLY THR TYR TRP ALA THR LEU ILE THR ALA PHE
SEQRES 2 A 131 LEU LYS THR VAL SER LYS VAL GLU GLU LEU ASP CYS VAL
SEQRES 3 A 131 ASP SER ALA VAL LEU VAL ASP VAL SER LYS ILE ILE THR
SEQRES 4 A 131 LEU THR GLN GLU PHE ARG ARG HIS TYR ASP SER VAL TYR
SEQRES 5 A 131 ARG ALA ASP TYR GLY PRO ALA LEU LYS ASN TRP LYS ARG
SEQRES 6 A 131 ASP LEU SER LYS LEU PHE THR SER LEU PHE VAL ASP VAL
SEQRES 7 A 131 ILE ASN SER GLY ARG ILE VAL GLY PHE PHE ASP VAL GLY
SEQRES 8 A 131 ARG TYR VAL CYS GLU GLU VAL LEU CYS PRO GLY SER TRP
SEQRES 9 A 131 THR GLU ASP HIS GLU LEU LEU ASN ASP CYS MET THR HIS
SEQRES 10 A 131 PHE PHE ILE GLU ASN ASN LEU MET ASN HIS PHE PRO LEU
SEQRES 11 A 131 GLU
SEQRES 1 B 131 LYS SER GLY THR TYR TRP ALA THR LEU ILE THR ALA PHE
SEQRES 2 B 131 LEU LYS THR VAL SER LYS VAL GLU GLU LEU ASP CYS VAL
SEQRES 3 B 131 ASP SER ALA VAL LEU VAL ASP VAL SER LYS ILE ILE THR
SEQRES 4 B 131 LEU THR GLN GLU PHE ARG ARG HIS TYR ASP SER VAL TYR
SEQRES 5 B 131 ARG ALA ASP TYR GLY PRO ALA LEU LYS ASN TRP LYS ARG
SEQRES 6 B 131 ASP LEU SER LYS LEU PHE THR SER LEU PHE VAL ASP VAL
SEQRES 7 B 131 ILE ASN SER GLY ARG ILE VAL GLY PHE PHE ASP VAL GLY
SEQRES 8 B 131 ARG TYR VAL CYS GLU GLU VAL LEU CYS PRO GLY SER TRP
SEQRES 9 B 131 THR GLU ASP HIS GLU LEU LEU ASN ASP CYS MET THR HIS
SEQRES 10 B 131 PHE PHE ILE GLU ASN ASN LEU MET ASN HIS PHE PRO LEU
SEQRES 11 B 131 GLU
SEQRES 1 C 19 THR MET GLU ASN LEU SER ARG ARG LEU LYS VAL THR GLY
SEQRES 2 C 19 ASP LEU PHE ASP ILE MET
SEQRES 1 D 19 THR MET GLU ASN LEU SER ARG ARG LEU LYS VAL THR GLY
SEQRES 2 D 19 ASP LEU PHE ASP ILE MET
FORMUL 5 HOH *59(H2 O)
HELIX 1 1 SER A 6 SER A 22 1 17
HELIX 2 2 ASP A 31 TYR A 56 1 26
HELIX 3 3 PRO A 62 LYS A 65 5 4
HELIX 4 4 ASN A 66 PHE A 79 1 14
HELIX 5 5 ASN A 84 GLU A 101 1 18
HELIX 6 6 THR A 109 ASN A 126 1 18
HELIX 7 7 ASN A 127 PHE A 132 5 6
HELIX 8 8 SER B 6 SER B 22 1 17
HELIX 9 9 VAL B 30 ALA B 33 5 4
HELIX 10 10 VAL B 34 TYR B 56 1 23
HELIX 11 11 TYR B 60 LYS B 65 5 6
HELIX 12 12 ASN B 66 PHE B 79 1 14
HELIX 13 13 ASN B 84 VAL B 102 1 19
HELIX 14 14 THR B 109 ASN B 126 1 18
HELIX 15 15 ASN B 127 PHE B 132 5 6
HELIX 16 16 THR C 106 ASP C 122 1 17
HELIX 17 17 THR D 106 ILE D 123 1 18
CRYST1 42.863 53.601 73.586 90.00 107.54 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 0.023330 0.000000 0.007374 0.00000
SCALE2 0.000000 0.018656 0.000000 0.00000
SCALE3 0.000000 0.000000 0.014252 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
