HEADER CELL ADHESION 21-JUL-00 1GC7
TITLE CRYSTAL STRUCTURE OF THE RADIXIN FERM DOMAIN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: RADIXIN;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: FERM DOMAIN;
COMPND 5 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 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PGEX4T-3
KEYWDS 3 SUBDOMAINS, CYTOSKELETON, CELL ADHESION
EXPDTA X-RAY DIFFRACTION
AUTHOR K.HAMADA,T.SHIMIZU,T.MATSUI,S.TSUKITA,S.TSUKITA,T.HAKOSHIMA
REVDAT 5 27-DEC-23 1GC7 1 REMARK
REVDAT 4 24-FEB-09 1GC7 1 VERSN
REVDAT 3 01-APR-03 1GC7 1 JRNL
REVDAT 2 28-JAN-03 1GC7 1 REMARK
REVDAT 1 20-SEP-00 1GC7 0
JRNL AUTH K.HAMADA,T.SHIMIZU,T.MATSUI,S.TSUKITA,T.HAKOSHIMA
JRNL TITL STRUCTURAL BASIS OF THE MEMBRANE-TARGETING AND UNMASKING
JRNL TITL 2 MECHANISMS OF THE RADIXIN FERM DOMAIN.
JRNL REF EMBO J. V. 19 4449 2000
JRNL REFN ISSN 0261-4189
JRNL PMID 10970839
JRNL DOI 10.1093/EMBOJ/19.17.4449
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH K.HAMADA,T.SHIMIZU,T.MATSUI,S.TSUKITA,S.TSUKITA,T.HAKOSHIMA
REMARK 1 TITL CRYSTALLOGRAPHIC CHARACTERIZATION OF THE MEMBRANE-BINDING
REMARK 1 TITL 2 DOMAIN OF RADIXIN
REMARK 1 REF ACTA CRYSTALLOGR.,SECT.D V. 56 922 2000
REMARK 1 REFN ISSN 0907-4449
REMARK 1 DOI 10.1107/S0907444900006363
REMARK 2
REMARK 2 RESOLUTION. 2.80 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 : PROTEIN.PARAM
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.80
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 30.00
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) (%) : NULL
REMARK 3 NUMBER OF REFLECTIONS : 15929
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : NULL
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING SET) : 0.215
REMARK 3 FREE R VALUE : 0.255
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : 765
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 : 2482
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 0
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 64.20
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
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) : 1.442
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) : 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 : NULL
REMARK 3 KSOL : NULL
REMARK 3 BSOL : NULL
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 : NULL
REMARK 3 TOPOLOGY FILE 1 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1GC7 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 28-JUL-00.
REMARK 100 THE DEPOSITION ID IS D_1000005029.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 02-MAR-00
REMARK 200 TEMPERATURE (KELVIN) : 288.0
REMARK 200 PH : 6.0
REMARK 200 NUMBER OF CRYSTALS USED : 3
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : PHOTON FACTORY
REMARK 200 BEAMLINE : BL-6A
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0000
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUAMTUM 4R
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : CCP4 (SCALA)
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 23751
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.800
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 (%) : 99.8
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : 0.04600
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 11.8000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.80
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.90
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.9
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.39300
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: NULL
REMARK 200 SOFTWARE USED: MLPHARE
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 71.87
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.37
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 6000, MES, PH 6.0, VAPOR
REMARK 280 DIFFUSION, HANGING DROP, TEMPERATURE 277K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 41 21 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z+1/2
REMARK 290 3555 -Y+1/2,X+1/2,Z+1/4
REMARK 290 4555 Y+1/2,-X+1/2,Z+3/4
REMARK 290 5555 -X+1/2,Y+1/2,-Z+1/4
REMARK 290 6555 X+1/2,-Y+1/2,-Z+3/4
REMARK 290 7555 Y,X,-Z
REMARK 290 8555 -Y,-X,-Z+1/2
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 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 66.52000
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 48.16500
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 48.16500
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 33.26000
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 48.16500
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 48.16500
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 99.78000
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 48.16500
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 48.16500
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 33.26000
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 48.16500
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 48.16500
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 99.78000
REMARK 290 SMTRY1 7 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 7 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 66.52000
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 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 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 LYS A 296 CG CD CE NZ
REMARK 470 PRO A 297 CG CD
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 PRO A 75 C - N - CA ANGL. DEV. = -9.1 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 GLU A 41 43.44 -78.43
REMARK 500 ASN A 74 -87.57 -60.83
REMARK 500 LYS A 139 -4.66 -58.20
REMARK 500 ASP A 221 -164.61 -126.75
REMARK 500 ASP A 252 -29.85 -31.82
REMARK 500 ASP A 261 94.60 -57.26
REMARK 500 LYS A 263 46.13 -96.13
REMARK 500 PRO A 272 -87.49 -45.58
REMARK 500 ARG A 295 -79.51 -99.21
REMARK 500 LYS A 296 56.34 -68.03
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1EF1 RELATED DB: PDB
REMARK 900 STRUCTURE OF THE ERM PROTEIN MOESIN
REMARK 900 RELATED ID: 1GC6 RELATED DB: PDB
REMARK 900 STRUCTURE OF THE RADIXIN FERM DOMAIN COMPLEXED WITH INOSITOL-(1,4,5)
REMARK 900 -TRIPHOSPHATE
DBREF 1GC7 A 1 297 UNP P26043 RADI_MOUSE 1 297
SEQRES 1 A 297 MET PRO LYS PRO ILE ASN VAL ARG VAL THR THR MET ASP
SEQRES 2 A 297 ALA GLU LEU GLU PHE ALA ILE GLN PRO ASN THR THR GLY
SEQRES 3 A 297 LYS GLN LEU PHE ASP GLN VAL VAL LYS THR VAL GLY LEU
SEQRES 4 A 297 ARG GLU VAL TRP PHE PHE GLY LEU GLN TYR VAL ASP SER
SEQRES 5 A 297 LYS GLY TYR SER THR TRP LEU LYS LEU ASN LYS LYS VAL
SEQRES 6 A 297 THR GLN GLN ASP VAL LYS LYS GLU ASN PRO LEU GLN PHE
SEQRES 7 A 297 LYS PHE ARG ALA LYS PHE PHE PRO GLU ASP VAL SER GLU
SEQRES 8 A 297 GLU LEU ILE GLN GLU ILE THR GLN ARG LEU PHE PHE LEU
SEQRES 9 A 297 GLN VAL LYS GLU ALA ILE LEU ASN ASP GLU ILE TYR CYS
SEQRES 10 A 297 PRO PRO GLU THR ALA VAL LEU LEU ALA SER TYR ALA VAL
SEQRES 11 A 297 GLN ALA LYS TYR GLY ASP TYR ASN LYS GLU ILE HIS LYS
SEQRES 12 A 297 PRO GLY TYR LEU ALA ASN ASP ARG LEU LEU PRO GLN ARG
SEQRES 13 A 297 VAL LEU GLU GLN HIS LYS LEU THR LYS GLU GLN TRP GLU
SEQRES 14 A 297 GLU ARG ILE GLN ASN TRP HIS GLU GLU HIS ARG GLY MET
SEQRES 15 A 297 LEU ARG GLU ASP SER MET MET GLU TYR LEU LYS ILE ALA
SEQRES 16 A 297 GLN ASP LEU GLU MET TYR GLY VAL ASN TYR PHE GLU ILE
SEQRES 17 A 297 LYS ASN LYS LYS GLY THR GLU LEU TRP LEU GLY VAL ASP
SEQRES 18 A 297 ALA LEU GLY LEU ASN ILE TYR GLU HIS ASP ASP LYS LEU
SEQRES 19 A 297 THR PRO LYS ILE GLY PHE PRO TRP SER GLU ILE ARG ASN
SEQRES 20 A 297 ILE SER PHE ASN ASP LYS LYS PHE VAL ILE LYS PRO ILE
SEQRES 21 A 297 ASP LYS LYS ALA PRO ASP PHE VAL PHE TYR ALA PRO ARG
SEQRES 22 A 297 LEU ARG ILE ASN LYS ARG ILE LEU ALA LEU CYS MET GLY
SEQRES 23 A 297 ASN HIS GLU LEU TYR MET ARG ARG ARG LYS PRO
HELIX 1 1 THR A 25 GLY A 38 1 14
HELIX 2 2 GLU A 41 TRP A 43 5 3
HELIX 3 3 VAL A 65 GLN A 68 5 4
HELIX 4 4 ASP A 88 LEU A 93 1 6
HELIX 5 5 GLN A 95 ASN A 112 1 18
HELIX 6 6 PRO A 118 GLY A 135 1 18
HELIX 7 7 PRO A 154 GLU A 159 1 6
HELIX 8 8 THR A 164 HIS A 179 1 16
HELIX 9 9 LEU A 183 GLN A 196 1 14
HELIX 10 10 ARG A 273 LYS A 296 1 24
SHEET 1 A 5 GLU A 15 ILE A 20 0
SHEET 2 A 5 ILE A 5 THR A 10 -1 N ILE A 5 O ILE A 20
SHEET 3 A 5 LEU A 76 ALA A 82 1 O LEU A 76 N ARG A 8
SHEET 4 A 5 PHE A 45 VAL A 50 -1 N GLY A 46 O ARG A 81
SHEET 5 A 5 SER A 56 TRP A 58 -1 N THR A 57 O TYR A 49
SHEET 1 B 7 ILE A 238 PRO A 241 0
SHEET 2 B 7 GLY A 224 GLU A 229 -1 O LEU A 225 N PHE A 240
SHEET 3 B 7 GLU A 215 VAL A 220 -1 O TRP A 217 N TYR A 228
SHEET 4 B 7 ASN A 204 ASN A 210 -1 O ASN A 204 N VAL A 220
SHEET 5 B 7 PHE A 267 TYR A 270 -1 N TYR A 270 O LYS A 209
SHEET 6 B 7 LYS A 254 PRO A 259 -1 N PHE A 255 O PHE A 269
SHEET 7 B 7 ILE A 245 ASN A 251 -1 N ARG A 246 O LYS A 258
CRYST1 96.330 96.330 133.040 90.00 90.00 90.00 P 41 21 2 8
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 0.010381 0.000000 0.000000 0.00000
SCALE2 0.000000 0.010381 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007517 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
