HEADER APOPTOSIS 17-JUN-03 1PQ1
TITLE CRYSTAL STRUCTURE OF BCL-XL/BIM
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: APOPTOSIS REGULATOR BCL-X;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: BIM;
COMPND 5 SYNONYM: BCL2-LIKE 1 PROTEIN;
COMPND 6 ENGINEERED: YES;
COMPND 7 MOL_ID: 2;
COMPND 8 MOLECULE: BCL2-LIKE PROTEIN 11;
COMPND 9 CHAIN: B;
COMPND 10 SYNONYM: BCL2 INTERACTING MEDIATOR OF CELL DEATH;
COMPND 11 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MUS MUSCULUS;
SOURCE 3 ORGANISM_COMMON: HOUSE MOUSE;
SOURCE 4 ORGANISM_TAXID: 10090;
SOURCE 5 GENE: BCL2L1 OR BCL2L OR BCLX;
SOURCE 6 EXPRESSION_SYSTEM: TRICHOPLUSIA NI;
SOURCE 7 EXPRESSION_SYSTEM_COMMON: CABBAGE LOOPER;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 7111;
SOURCE 9 EXPRESSION_SYSTEM_STRAIN: HI-FIVE;
SOURCE 10 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS;
SOURCE 11 EXPRESSION_SYSTEM_VECTOR: BACVECTOR 3000 (NOVAGEN);
SOURCE 12 MOL_ID: 2;
SOURCE 13 ORGANISM_SCIENTIFIC: MUS MUSCULUS;
SOURCE 14 ORGANISM_COMMON: HOUSE MOUSE;
SOURCE 15 ORGANISM_TAXID: 10090;
SOURCE 16 GENE: BCL2L11 OR BIM;
SOURCE 17 EXPRESSION_SYSTEM: TRICHOPLUSIA NI;
SOURCE 18 EXPRESSION_SYSTEM_COMMON: CABBAGE LOOPER;
SOURCE 19 EXPRESSION_SYSTEM_TAXID: 7111;
SOURCE 20 EXPRESSION_SYSTEM_STRAIN: HI-FIVE;
SOURCE 21 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS;
SOURCE 22 EXPRESSION_SYSTEM_VECTOR: BACVECTOR 3000 (NOVAGEN)
KEYWDS BCL-XL/BIM, APOPTOSIS
EXPDTA X-RAY DIFFRACTION
AUTHOR X.LIU,S.DAI,Y.ZHU,P.MARRACK,J.W.KAPPLER
REVDAT 3 16-AUG-23 1PQ1 1 REMARK
REVDAT 2 24-FEB-09 1PQ1 1 VERSN
REVDAT 1 23-SEP-03 1PQ1 0
JRNL AUTH X.LIU,S.DAI,Y.ZHU,P.MARRACK,J.W.KAPPLER
JRNL TITL THE STRUCTURE OF A BCL-XL/BIM FRAGMENT COMPLEX: IMPLICATIONS
JRNL TITL 2 FOR BIM FUNCTION
JRNL REF IMMUNITY V. 19 341 2003
JRNL REFN ISSN 1074-7613
JRNL PMID 14499110
JRNL DOI 10.1016/S1074-7613(03)00234-6
REMARK 2
REMARK 2 RESOLUTION. 1.65 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 1.0
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 : ENGH & HUBER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.65
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 19.90
REMARK 3 DATA CUTOFF (SIGMA(F)) : 2.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 95.0
REMARK 3 NUMBER OF REFLECTIONS : 19462
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) : 0.219
REMARK 3 FREE R VALUE : 0.237
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.700
REMARK 3 FREE R VALUE TEST SET COUNT : 923
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.008
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) : 1.65
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.75
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 87.90
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 2856
REMARK 3 BIN R VALUE (WORKING SET) : 0.2710
REMARK 3 BIN FREE R VALUE : 0.3090
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 4.70
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 140
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.026
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 1458
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 169
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 25.10
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 23.90
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 3.17000
REMARK 3 B22 (A**2) : 0.49000
REMARK 3 B33 (A**2) : -3.67000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : -1.28000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.21
REMARK 3 ESD FROM SIGMAA (A) : 0.14
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) : 0.24
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.18
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.006
REMARK 3 BOND ANGLES (DEGREES) : 1.100
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 18.70
REMARK 3 IMPROPER ANGLES (DEGREES) : 0.680
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) : 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 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : FLAT MODEL
REMARK 3 KSOL : 0.39
REMARK 3 BSOL : 47.20
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 : &_1_PARAMETER_INFILE_3
REMARK 3 PARAMETER FILE 4 : NULL
REMARK 3 TOPOLOGY FILE 1 : PROTEIN.TOP
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 1PQ1 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 23-JUN-03.
REMARK 100 THE DEPOSITION ID IS D_1000019486.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 18-FEB-02
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 4.5
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 RU300
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : OSMIC MIRRORS
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : RIGAKU RAXIS IV
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 19877
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.650
REMARK 200 RESOLUTION RANGE LOW (A) : 20.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 97.2
REMARK 200 DATA REDUNDANCY : 4.800
REMARK 200 R MERGE (I) : 0.06200
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 8.6000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.65
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.75
REMARK 200 COMPLETENESS FOR SHELL (%) : 90.9
REMARK 200 DATA REDUNDANCY IN SHELL : 4.40
REMARK 200 R MERGE FOR SHELL (I) : 0.21800
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.700
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: AMORE
REMARK 200 STARTING MODEL: MOUSE BCL-XL, PDB ENTRY 1PQ0
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): NULL
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): NULL
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: NH4H2PO4, PH 4.5, VAPOR DIFFUSION,
REMARK 280 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 23.67000
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: 2110 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 9100 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -10.0 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 ASP A 29
REMARK 465 VAL A 30
REMARK 465 GLU A 31
REMARK 465 GLU A 32
REMARK 465 ASN A 33
REMARK 465 ARG A 34
REMARK 465 THR A 35
REMARK 465 GLU A 36
REMARK 465 ALA A 37
REMARK 465 PRO A 38
REMARK 465 GLU A 39
REMARK 465 GLU A 40
REMARK 465 THR A 41
REMARK 465 GLU A 42
REMARK 465 ALA A 43
REMARK 465 GLU A 44
REMARK 465 ARG A 45
REMARK 465 GLU A 46
REMARK 465 THR A 47
REMARK 465 PRO A 48
REMARK 465 SER A 49
REMARK 465 ALA A 50
REMARK 465 ILE A 51
REMARK 465 ASN A 52
REMARK 465 GLY A 53
REMARK 465 ASN A 54
REMARK 465 PRO A 55
REMARK 465 SER A 56
REMARK 465 TRP A 57
REMARK 465 HIS A 58
REMARK 465 LEU A 59
REMARK 465 ALA A 60
REMARK 465 ASP A 61
REMARK 465 SER A 62
REMARK 465 PRO A 63
REMARK 465 ALA A 64
REMARK 465 VAL A 65
REMARK 465 ASN A 66
REMARK 465 GLY A 67
REMARK 465 ALA A 68
REMARK 465 THR A 69
REMARK 465 GLY A 70
REMARK 465 HIS A 71
REMARK 465 SER A 72
REMARK 465 SER A 73
REMARK 465 SER A 74
REMARK 465 LEU A 75
REMARK 465 ASP A 76
REMARK 465 ALA A 77
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 GLN A 26 CG CD OE1 NE2
REMARK 470 PHE A 27 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 SER A 28 OG
REMARK 470 ARG A 78 CG CD NE CZ NH1 NH2
REMARK 470 ASP B 83 CB CG OD1 OD2
REMARK 470 ARG B 115 CB 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 O MET A 1 O HOH A 327 2.02
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 2 161.36 -12.96
REMARK 500 ASP B 113 48.90 -99.67
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1PQ0 RELATED DB: PDB
REMARK 900 MONOMER
DBREF 1PQ1 A 1 196 UNP Q64373 BCLX_MOUSE 1 196
DBREF 1PQ1 B 83 115 UNP O54918 BIM_MOUSE 83 115
SEQRES 1 A 196 MET SER GLN SER ASN ARG GLU LEU VAL VAL ASP PHE LEU
SEQRES 2 A 196 SER TYR LYS LEU SER GLN LYS GLY TYR SER TRP SER GLN
SEQRES 3 A 196 PHE SER ASP VAL GLU GLU ASN ARG THR GLU ALA PRO GLU
SEQRES 4 A 196 GLU THR GLU ALA GLU ARG GLU THR PRO SER ALA ILE ASN
SEQRES 5 A 196 GLY ASN PRO SER TRP HIS LEU ALA ASP SER PRO ALA VAL
SEQRES 6 A 196 ASN GLY ALA THR GLY HIS SER SER SER LEU ASP ALA ARG
SEQRES 7 A 196 GLU VAL ILE PRO MET ALA ALA VAL LYS GLN ALA LEU ARG
SEQRES 8 A 196 GLU ALA GLY ASP GLU PHE GLU LEU ARG TYR ARG ARG ALA
SEQRES 9 A 196 PHE SER ASP LEU THR SER GLN LEU HIS ILE THR PRO GLY
SEQRES 10 A 196 THR ALA TYR GLN SER PHE GLU GLN VAL VAL ASN GLU LEU
SEQRES 11 A 196 PHE ARG ASP GLY VAL ASN TRP GLY ARG ILE VAL ALA PHE
SEQRES 12 A 196 PHE SER PHE GLY GLY ALA LEU CYS VAL GLU SER VAL ASP
SEQRES 13 A 196 LYS GLU MET GLN VAL LEU VAL SER ARG ILE ALA SER TRP
SEQRES 14 A 196 MET ALA THR TYR LEU ASN ASP HIS LEU GLU PRO TRP ILE
SEQRES 15 A 196 GLN GLU ASN GLY GLY TRP ASP THR PHE VAL ASP LEU TYR
SEQRES 16 A 196 GLY
SEQRES 1 B 33 ASP LEU ARG PRO GLU ILE ARG ILE ALA GLN GLU LEU ARG
SEQRES 2 B 33 ARG ILE GLY ASP GLU PHE ASN GLU THR TYR THR ARG ARG
SEQRES 3 B 33 VAL PHE ALA ASN ASP TYR ARG
FORMUL 3 HOH *169(H2 O)
HELIX 1 1 GLN A 3 GLN A 19 1 17
HELIX 2 2 PRO A 82 ARG A 102 1 21
HELIX 3 3 ARG A 103 SER A 106 5 4
HELIX 4 4 ASP A 107 LEU A 112 1 6
HELIX 5 5 THR A 118 PHE A 131 1 14
HELIX 6 6 ASN A 136 LYS A 157 1 22
HELIX 7 7 GLU A 158 GLU A 158 5 1
HELIX 8 8 MET A 159 GLN A 160 5 2
HELIX 9 9 VAL A 161 LEU A 178 1 18
HELIX 10 10 LEU A 178 ASN A 185 1 8
HELIX 11 11 GLY A 186 GLY A 196 1 11
HELIX 12 12 ARG B 85 ASP B 113 1 29
CRYST1 39.100 47.340 49.280 90.00 110.10 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 0.025575 0.000000 0.009359 0.00000
SCALE2 0.000000 0.021124 0.000000 0.00000
SCALE3 0.000000 0.000000 0.021608 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
