HEADER CELL ADHESION 13-DEC-01 1ISN
TITLE CRYSTAL STRUCTURE OF MERLIN FERM DOMAIN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: MERLIN;
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 GENE: NEUROFIBROMATOSIS TYPE 2;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)RIL;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PGEX-4T-1
KEYWDS FERM DOMAIN, CELL ADHESION
EXPDTA X-RAY DIFFRACTION
AUTHOR T.SHIMIZU,A.SETO,N.MAITA,K.HAMADA,S.TSUKITA,S.TSUKITA,T.HAKOSHIMA
REVDAT 5 25-OCT-23 1ISN 1 REMARK
REVDAT 4 24-FEB-09 1ISN 1 VERSN
REVDAT 3 01-APR-03 1ISN 1 JRNL
REVDAT 2 07-JAN-03 1ISN 1 REMARK
REVDAT 1 03-APR-02 1ISN 0
JRNL AUTH T.SHIMIZU,A.SETO,N.MAITA,K.HAMADA,S.TSUKITA,S.TSUKITA,
JRNL AUTH 2 T.HAKOSHIMA
JRNL TITL STRUCTURAL BASIS FOR NEUROFIBROMATOSIS TYPE 2. CRYSTAL
JRNL TITL 2 STRUCTURE OF THE MERLIN FERM DOMAIN.
JRNL REF J.BIOL.CHEM. V. 277 10332 2002
JRNL REFN ISSN 0021-9258
JRNL PMID 11756419
JRNL DOI 10.1074/JBC.M109979200
REMARK 2
REMARK 2 RESOLUTION. 2.90 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) : 2.90
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 20.00
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 : 7821
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) : 0.229
REMARK 3 FREE R VALUE : 0.284
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 11.600
REMARK 3 FREE R VALUE TEST SET COUNT : 907
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) : 2.90
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 3.03
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : 0.3728
REMARK 3 BIN FREE R VALUE : 0.4065
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 83
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 : 2617
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) : 50.80
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) : 0.40
REMARK 3 ESD FROM SIGMAA (A) : 0.53
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) : 0.51
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.63
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.010
REMARK 3 BOND ANGLES (DEGREES) : 1.500
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 23.40
REMARK 3 IMPROPER ANGLES (DEGREES) : 1.240
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 1ISN COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 19-DEC-01.
REMARK 100 THE DEPOSITION ID IS D_1000005238.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 10-NOV-00
REMARK 200 TEMPERATURE (KELVIN) : 93
REMARK 200 PH : 7.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SPRING-8
REMARK 200 BEAMLINE : BL41XU
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9198
REMARK 200 MONOCHROMATOR : DOUBLE-CRYSTAL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DPS, MOSFLM
REMARK 200 DATA SCALING SOFTWARE : DPS, MOSFLM
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 8807
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.900
REMARK 200 RESOLUTION RANGE LOW (A) : 30.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 90.5
REMARK 200 DATA REDUNDANCY : 5.500
REMARK 200 R MERGE (I) : 0.06900
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 8.4000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.90
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.03
REMARK 200 COMPLETENESS FOR SHELL (%) : 75.8
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.31600
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.400
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: PDB ENTRY 1GC6
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 53.60
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.65
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG6000, LICL, PH 7.0, VAPOR
REMARK 280 DIFFUSION, HANGING DROP, TEMPERATURE 277K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 43 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+3/4
REMARK 290 4555 Y+1/2,-X+1/2,Z+1/4
REMARK 290 5555 -X+1/2,Y+1/2,-Z+3/4
REMARK 290 6555 X+1/2,-Y+1/2,-Z+1/4
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 89.56850
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 33.70400
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 33.70400
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 134.35275
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 33.70400
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 33.70400
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 44.78425
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 33.70400
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 33.70400
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 134.35275
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 33.70400
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 33.70400
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 44.78425
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 89.56850
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 GLN A 18 CG CD OE1 NE2
REMARK 470 LYS A 40 CG CD CE NZ
REMARK 470 LYS A 124 CG CD CE NZ
REMARK 470 ASN A 175 CG OD1 ND2
REMARK 470 GLN A 178 CG CD OE1 NE2
REMARK 470 MET A 183 CG SD CE
REMARK 470 ARG A 196 CG CD NE CZ NH1 NH2
REMARK 470 ARG A 262 CG CD NE CZ NH1 NH2
REMARK 470 ASN A 263 CG OD1 ND2
REMARK 470 ASP A 268 CG OD1 OD2
REMARK 470 LEU A 290 CG CD1 CD2
REMARK 470 LEU A 316 CG CD1 CD2
REMARK 470 GLU A 327 CG CD OE1 OE2
REMARK 470 LYS A 329 CG CD CE NZ
REMARK 470 ARG A 331 CG CD NE CZ NH1 NH2
REMARK 470 LYS A 332 CG CD CE NZ
REMARK 470 GLN A 333 CG CD OE1 NE2
REMARK 470 GLN A 337 CG CD OE1 NE2
REMARK 470 ARG A 338 CG CD NE CZ NH1 NH2
REMARK 470 LEU A 339 CG CD1 CD2
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 MET A 29 2.82 -66.13
REMARK 500 ASP A 30 -17.32 -151.79
REMARK 500 TRP A 60 -7.97 -51.54
REMARK 500 LYS A 69 -37.92 165.61
REMARK 500 ASP A 70 -94.44 -99.77
REMARK 500 ASP A 85 52.61 -69.98
REMARK 500 PRO A 135 -72.74 -43.24
REMARK 500 ALA A 164 -93.56 -59.76
REMARK 500 GLU A 166 -11.90 -149.29
REMARK 500 GLU A 167 75.88 57.53
REMARK 500 TYR A 177 -43.26 -21.98
REMARK 500 GLN A 178 -2.65 -56.79
REMARK 500 PRO A 181 -74.68 -28.88
REMARK 500 LYS A 227 -9.92 -54.96
REMARK 500 LEU A 232 -154.20 -120.14
REMARK 500 PRO A 246 -9.14 -48.86
REMARK 500 TYR A 266 101.34 -160.06
REMARK 500 ASP A 268 -91.22 63.74
REMARK 500 LYS A 269 34.36 -151.78
REMARK 500 ASP A 277 78.27 70.75
REMARK 500 ILE A 280 -73.94 -97.92
REMARK 500 ASP A 281 -164.68 -165.57
REMARK 500 VAL A 282 105.73 -166.23
REMARK 500 LYS A 289 90.11 176.28
REMARK 500 LEU A 290 -19.00 -41.02
REMARK 500 LEU A 339 23.93 -177.13
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1ISN A 18 340 UNP P46662 MERL_MOUSE 18 340
SEQRES 1 A 323 GLN PRO LYS THR PHE THR VAL ARG ILE VAL THR MET ASP
SEQRES 2 A 323 ALA GLU MET GLU PHE ASN CYS GLU MET LYS TRP LYS GLY
SEQRES 3 A 323 LYS ASP LEU PHE ASP LEU VAL CYS ARG THR LEU GLY LEU
SEQRES 4 A 323 ARG GLU THR TRP PHE PHE GLY LEU GLN TYR THR ILE LYS
SEQRES 5 A 323 ASP THR VAL ALA TRP LEU LYS MET ASP LYS LYS VAL LEU
SEQRES 6 A 323 ASP HIS ASP VAL SER LYS GLU GLU PRO VAL THR PHE HIS
SEQRES 7 A 323 PHE LEU ALA LYS PHE TYR PRO GLU ASN ALA GLU GLU GLU
SEQRES 8 A 323 LEU VAL GLN GLU ILE THR GLN HIS LEU PHE PHE LEU GLN
SEQRES 9 A 323 VAL LYS LYS GLN ILE LEU ASP GLU LYS VAL TYR CYS PRO
SEQRES 10 A 323 PRO GLU ALA SER VAL LEU LEU ALA SER TYR ALA VAL GLN
SEQRES 11 A 323 ALA LYS TYR GLY ASP TYR ASP PRO SER VAL HIS LYS ARG
SEQRES 12 A 323 GLY PHE LEU ALA GLN GLU GLU LEU LEU PRO LYS ARG VAL
SEQRES 13 A 323 ILE ASN LEU TYR GLN MET THR PRO GLU MET TRP GLU GLU
SEQRES 14 A 323 ARG ILE THR ALA TRP TYR ALA GLU HIS ARG GLY ARG ALA
SEQRES 15 A 323 ARG ASP GLU ALA GLU MET GLU TYR LEU LYS ILE ALA GLN
SEQRES 16 A 323 ASP LEU GLU MET TYR GLY VAL ASN TYR PHE THR ILE ARG
SEQRES 17 A 323 ASN LYS LYS GLY THR GLU LEU LEU LEU GLY VAL ASP ALA
SEQRES 18 A 323 LEU GLY LEU HIS ILE TYR ASP PRO GLU ASN ARG LEU THR
SEQRES 19 A 323 PRO LYS ILE SER PHE PRO TRP ASN GLU ILE ARG ASN ILE
SEQRES 20 A 323 SER TYR SER ASP LYS GLU PHE THR ILE LYS PRO LEU ASP
SEQRES 21 A 323 LYS LYS ILE ASP VAL PHE LYS PHE ASN SER SER LYS LEU
SEQRES 22 A 323 ARG VAL ASN LYS LEU ILE LEU GLN LEU CYS ILE GLY ASN
SEQRES 23 A 323 HIS ASP LEU PHE MET ARG ARG ARG LYS ALA ASP SER LEU
SEQRES 24 A 323 GLU VAL GLN GLN MET LYS ALA GLN ALA ARG GLU GLU LYS
SEQRES 25 A 323 ALA ARG LYS GLN MET GLU ARG GLN ARG LEU ALA
HELIX 1 1 LYS A 42 GLY A 55 1 14
HELIX 2 2 GLU A 58 TRP A 60 5 3
HELIX 3 3 ASN A 104 LEU A 109 1 6
HELIX 4 4 GLN A 111 ASP A 128 1 18
HELIX 5 5 PRO A 134 GLY A 151 1 18
HELIX 6 6 PRO A 170 ASN A 175 1 6
HELIX 7 7 THR A 180 HIS A 195 1 16
HELIX 8 8 ALA A 199 ASP A 213 1 15
HELIX 9 9 ARG A 291 LYS A 312 1 22
HELIX 10 10 SER A 315 ARG A 338 1 24
SHEET 1 A 5 GLU A 32 GLU A 38 0
SHEET 2 A 5 THR A 21 VAL A 27 -1 N VAL A 24 O PHE A 35
SHEET 3 A 5 VAL A 92 ALA A 98 1 O VAL A 92 N ARG A 25
SHEET 4 A 5 PHE A 62 THR A 67 -1 N GLN A 65 O HIS A 95
SHEET 5 A 5 VAL A 72 TRP A 74 -1 O ALA A 73 N TYR A 66
SHEET 1 B 4 ASN A 220 PHE A 222 0
SHEET 2 B 4 LEU A 233 VAL A 236 -1 O LEU A 234 N PHE A 222
SHEET 3 B 4 GLY A 240 TYR A 244 -1 O HIS A 242 N GLY A 235
SHEET 4 B 4 ILE A 254 PRO A 257 -1 O PHE A 256 N LEU A 241
SHEET 1 C 3 ILE A 261 SER A 267 0
SHEET 2 C 3 GLU A 270 PRO A 275 -1 O LYS A 274 N ASN A 263
SHEET 3 C 3 PHE A 285 ASN A 286 -1 O PHE A 285 N PHE A 271
CISPEP 1 GLU A 90 PRO A 91 0 -0.26
CRYST1 67.408 67.408 179.137 90.00 90.00 90.00 P 43 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 0.014835 0.000000 0.000000 0.00000
SCALE2 0.000000 0.014835 0.000000 0.00000
SCALE3 0.000000 0.000000 0.005582 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
