HEADER CELL ADHESION 15-SEP-05 2D2Q
TITLE CRYSTAL STRUCTURE OF THE DIMERIZED RADIXIN FERM DOMAIN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: RADIXIN;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: FERM DOMAIN (RESIDUES 1-310);
COMPND 5 SYNONYM: ESP10;
COMPND 6 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_STRAIN: BL21(DE3)RIL;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PGEX4T-3
KEYWDS HOMO DIMER, MASKING, CELL ADHESION
EXPDTA X-RAY DIFFRACTION
AUTHOR K.KITANO,F.YUSA,T.HAKOSHIMA
REVDAT 3 13-MAR-24 2D2Q 1 REMARK
REVDAT 2 24-FEB-09 2D2Q 1 VERSN
REVDAT 1 18-APR-06 2D2Q 0
JRNL AUTH K.KITANO,F.YUSA,T.HAKOSHIMA
JRNL TITL STRUCTURE OF DIMERIZED RADIXIN FERM DOMAIN SUGGESTS A NOVEL
JRNL TITL 2 MASKING MOTIF IN C-TERMINAL RESIDUES 295-304
JRNL REF ACTA CRYSTALLOGR.,SECT.F V. 62 340 2006
JRNL REFN ESSN 1744-3091
JRNL PMID 16582480
JRNL DOI 10.1107/S1744309106010062
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 : MAXIMUM LIKELIHOOD
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)) : NULL
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 : 19703
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) : 0.222
REMARK 3 FREE R VALUE : 0.269
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : 899
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 : 5016
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) : NULL
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) : NULL
REMARK 3 BOND ANGLES (DEGREES) : NULL
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 2D2Q COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 15-SEP-05.
REMARK 100 THE DEPOSITION ID IS D_1000024914.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 07-DEC-04
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SPRING-8
REMARK 200 BEAMLINE : BL44XU
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.90
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : BRUKER DIP-6040
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 19703
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 (%) : 96.4
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) : 2.80
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.90
REMARK 200 COMPLETENESS FOR SHELL (%) : 76.9
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
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: CNS
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 58.70
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.98
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 3350, HEPES-NA, PH 7.5, VAPOR
REMARK 280 DIFFUSION, TEMPERATURE 293K
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 35.10900
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
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 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
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 MET A 1
REMARK 465 PRO A 2
REMARK 465 ILE A 300
REMARK 465 GLU A 301
REMARK 465 VAL A 302
REMARK 465 GLN A 303
REMARK 465 GLN A 304
REMARK 465 MET A 305
REMARK 465 LYS A 306
REMARK 465 ALA A 307
REMARK 465 GLN A 308
REMARK 465 ALA A 309
REMARK 465 ARG A 310
REMARK 465 MET B 1
REMARK 465 PRO B 2
REMARK 465 MET B 305
REMARK 465 LYS B 306
REMARK 465 ALA B 307
REMARK 465 GLN B 308
REMARK 465 ALA B 309
REMARK 465 ARG B 310
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 PRO A 4 176.87 -56.33
REMARK 500 ASP A 13 3.44 -153.31
REMARK 500 PRO A 22 -7.68 -55.99
REMARK 500 VAL A 65 7.15 -57.00
REMARK 500 ASN A 74 -79.05 -44.62
REMARK 500 LYS A 133 -77.74 -82.65
REMARK 500 PRO A 144 91.08 -47.81
REMARK 500 ASN A 149 63.23 -115.37
REMARK 500 GLU A 159 41.72 -78.51
REMARK 500 HIS A 161 46.39 -15.66
REMARK 500 GLU A 178 30.16 -86.70
REMARK 500 ASP A 252 -120.96 77.27
REMARK 500 ASP A 261 13.11 -61.36
REMARK 500 LYS A 262 -75.00 48.25
REMARK 500 ALA A 264 154.90 -44.51
REMARK 500 ARG A 295 -62.23 -91.15
REMARK 500 PRO A 297 -164.43 -37.08
REMARK 500 ASP A 298 38.28 -56.62
REMARK 500 PRO B 4 122.59 -39.89
REMARK 500 THR B 11 -158.15 -100.52
REMARK 500 ALA B 19 40.36 -142.42
REMARK 500 ILE B 20 154.31 -49.65
REMARK 500 TRP B 43 -16.82 -47.41
REMARK 500 SER B 52 -39.84 -36.49
REMARK 500 LYS B 63 135.84 162.57
REMARK 500 GLN B 68 16.69 -147.64
REMARK 500 LYS B 72 99.98 -64.63
REMARK 500 LEU B 76 94.95 59.71
REMARK 500 CYS B 117 116.16 -165.07
REMARK 500 PRO B 144 147.03 -38.98
REMARK 500 ALA B 148 -9.36 -49.98
REMARK 500 GLN B 160 11.13 176.48
REMARK 500 HIS B 161 -159.32 50.76
REMARK 500 LYS B 162 -20.50 82.81
REMARK 500 LYS B 212 1.54 -65.40
REMARK 500 HIS B 230 -37.64 -31.82
REMARK 500 PHE B 240 87.18 -150.61
REMARK 500 ASP B 252 -61.83 74.12
REMARK 500 ASP B 261 47.53 -76.37
REMARK 500 LYS B 262 -80.99 19.26
REMARK 500 TYR B 291 -77.62 -39.00
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1GC7 RELATED DB: PDB
REMARK 900 THE RADIXIN FERM DOMAIN
REMARK 900 RELATED ID: 1GC6 RELATED DB: PDB
REMARK 900 THE RADIXIN FERM DOMAIN COMPLEXED WITH INOSITOL-(1,4,5)-TRIPHOSPHATE
REMARK 900 RELATED ID: 1J19 RELATED DB: PDB
REMARK 900 THE RADXIN FERM DOMAIN COMPLEXED WITH THE ICAM-2 CYTOPLASMIC PEPTIDE
DBREF 2D2Q A 1 310 UNP P26043 RADI_MOUSE 1 310
DBREF 2D2Q B 1 310 UNP P26043 RADI_MOUSE 1 310
SEQRES 1 A 310 MET PRO LYS PRO ILE ASN VAL ARG VAL THR THR MET ASP
SEQRES 2 A 310 ALA GLU LEU GLU PHE ALA ILE GLN PRO ASN THR THR GLY
SEQRES 3 A 310 LYS GLN LEU PHE ASP GLN VAL VAL LYS THR VAL GLY LEU
SEQRES 4 A 310 ARG GLU VAL TRP PHE PHE GLY LEU GLN TYR VAL ASP SER
SEQRES 5 A 310 LYS GLY TYR SER THR TRP LEU LYS LEU ASN LYS LYS VAL
SEQRES 6 A 310 THR GLN GLN ASP VAL LYS LYS GLU ASN PRO LEU GLN PHE
SEQRES 7 A 310 LYS PHE ARG ALA LYS PHE PHE PRO GLU ASP VAL SER GLU
SEQRES 8 A 310 GLU LEU ILE GLN GLU ILE THR GLN ARG LEU PHE PHE LEU
SEQRES 9 A 310 GLN VAL LYS GLU ALA ILE LEU ASN ASP GLU ILE TYR CYS
SEQRES 10 A 310 PRO PRO GLU THR ALA VAL LEU LEU ALA SER TYR ALA VAL
SEQRES 11 A 310 GLN ALA LYS TYR GLY ASP TYR ASN LYS GLU ILE HIS LYS
SEQRES 12 A 310 PRO GLY TYR LEU ALA ASN ASP ARG LEU LEU PRO GLN ARG
SEQRES 13 A 310 VAL LEU GLU GLN HIS LYS LEU THR LYS GLU GLN TRP GLU
SEQRES 14 A 310 GLU ARG ILE GLN ASN TRP HIS GLU GLU HIS ARG GLY MET
SEQRES 15 A 310 LEU ARG GLU ASP SER MET MET GLU TYR LEU LYS ILE ALA
SEQRES 16 A 310 GLN ASP LEU GLU MET TYR GLY VAL ASN TYR PHE GLU ILE
SEQRES 17 A 310 LYS ASN LYS LYS GLY THR GLU LEU TRP LEU GLY VAL ASP
SEQRES 18 A 310 ALA LEU GLY LEU ASN ILE TYR GLU HIS ASP ASP LYS LEU
SEQRES 19 A 310 THR PRO LYS ILE GLY PHE PRO TRP SER GLU ILE ARG ASN
SEQRES 20 A 310 ILE SER PHE ASN ASP LYS LYS PHE VAL ILE LYS PRO ILE
SEQRES 21 A 310 ASP LYS LYS ALA PRO ASP PHE VAL PHE TYR ALA PRO ARG
SEQRES 22 A 310 LEU ARG ILE ASN LYS ARG ILE LEU ALA LEU CYS MET GLY
SEQRES 23 A 310 ASN HIS GLU LEU TYR MET ARG ARG ARG LYS PRO ASP THR
SEQRES 24 A 310 ILE GLU VAL GLN GLN MET LYS ALA GLN ALA ARG
SEQRES 1 B 310 MET PRO LYS PRO ILE ASN VAL ARG VAL THR THR MET ASP
SEQRES 2 B 310 ALA GLU LEU GLU PHE ALA ILE GLN PRO ASN THR THR GLY
SEQRES 3 B 310 LYS GLN LEU PHE ASP GLN VAL VAL LYS THR VAL GLY LEU
SEQRES 4 B 310 ARG GLU VAL TRP PHE PHE GLY LEU GLN TYR VAL ASP SER
SEQRES 5 B 310 LYS GLY TYR SER THR TRP LEU LYS LEU ASN LYS LYS VAL
SEQRES 6 B 310 THR GLN GLN ASP VAL LYS LYS GLU ASN PRO LEU GLN PHE
SEQRES 7 B 310 LYS PHE ARG ALA LYS PHE PHE PRO GLU ASP VAL SER GLU
SEQRES 8 B 310 GLU LEU ILE GLN GLU ILE THR GLN ARG LEU PHE PHE LEU
SEQRES 9 B 310 GLN VAL LYS GLU ALA ILE LEU ASN ASP GLU ILE TYR CYS
SEQRES 10 B 310 PRO PRO GLU THR ALA VAL LEU LEU ALA SER TYR ALA VAL
SEQRES 11 B 310 GLN ALA LYS TYR GLY ASP TYR ASN LYS GLU ILE HIS LYS
SEQRES 12 B 310 PRO GLY TYR LEU ALA ASN ASP ARG LEU LEU PRO GLN ARG
SEQRES 13 B 310 VAL LEU GLU GLN HIS LYS LEU THR LYS GLU GLN TRP GLU
SEQRES 14 B 310 GLU ARG ILE GLN ASN TRP HIS GLU GLU HIS ARG GLY MET
SEQRES 15 B 310 LEU ARG GLU ASP SER MET MET GLU TYR LEU LYS ILE ALA
SEQRES 16 B 310 GLN ASP LEU GLU MET TYR GLY VAL ASN TYR PHE GLU ILE
SEQRES 17 B 310 LYS ASN LYS LYS GLY THR GLU LEU TRP LEU GLY VAL ASP
SEQRES 18 B 310 ALA LEU GLY LEU ASN ILE TYR GLU HIS ASP ASP LYS LEU
SEQRES 19 B 310 THR PRO LYS ILE GLY PHE PRO TRP SER GLU ILE ARG ASN
SEQRES 20 B 310 ILE SER PHE ASN ASP LYS LYS PHE VAL ILE LYS PRO ILE
SEQRES 21 B 310 ASP LYS LYS ALA PRO ASP PHE VAL PHE TYR ALA PRO ARG
SEQRES 22 B 310 LEU ARG ILE ASN LYS ARG ILE LEU ALA LEU CYS MET GLY
SEQRES 23 B 310 ASN HIS GLU LEU TYR MET ARG ARG ARG LYS PRO ASP THR
SEQRES 24 B 310 ILE GLU VAL GLN GLN MET LYS ALA GLN ALA ARG
HELIX 1 1 THR A 25 GLY A 38 1 14
HELIX 2 2 ASP A 88 LEU A 93 1 6
HELIX 3 3 GLN A 95 ASN A 112 1 18
HELIX 4 4 PRO A 118 GLY A 135 1 18
HELIX 5 5 PRO A 154 GLU A 159 1 6
HELIX 6 6 THR A 164 GLU A 178 1 15
HELIX 7 7 LEU A 183 GLN A 196 1 14
HELIX 8 8 ARG A 273 LYS A 296 1 24
HELIX 9 9 THR B 25 GLY B 38 1 14
HELIX 10 10 GLU B 41 TRP B 43 5 3
HELIX 11 11 ASP B 88 LEU B 93 1 6
HELIX 12 12 GLN B 95 ASN B 112 1 18
HELIX 13 13 PRO B 118 GLY B 135 1 18
HELIX 14 14 PRO B 154 GLU B 159 1 6
HELIX 15 15 THR B 164 GLU B 177 1 14
HELIX 16 16 GLU B 178 ARG B 180 5 3
HELIX 17 17 LEU B 183 GLN B 196 1 14
HELIX 18 18 ARG B 273 ARG B 295 1 23
SHEET 1 A 5 GLU A 15 ILE A 20 0
SHEET 2 A 5 ILE A 5 THR A 10 -1 N VAL A 9 O LEU A 16
SHEET 3 A 5 LEU A 76 ALA A 82 1 O PHE A 80 N THR A 10
SHEET 4 A 5 PHE A 45 VAL A 50 -1 N GLN A 48 O LYS A 79
SHEET 5 A 5 SER A 56 TRP A 58 -1 O THR A 57 N TYR A 49
SHEET 1 B 4 ASN A 204 LYS A 209 0
SHEET 2 B 4 GLU A 215 ASP A 221 -1 O LEU A 216 N ILE A 208
SHEET 3 B 4 GLY A 224 GLU A 229 -1 O TYR A 228 N TRP A 217
SHEET 4 B 4 ILE A 238 PRO A 241 -1 O PHE A 240 N LEU A 225
SHEET 1 C 4 PHE A 267 TYR A 270 0
SHEET 2 C 4 LYS A 254 PRO A 259 -1 N ILE A 257 O PHE A 267
SHEET 3 C 4 ILE A 245 ASN A 251 -1 N ARG A 246 O LYS A 258
SHEET 4 C 4 ASP B 298 GLU B 301 -1 O ILE B 300 N ILE A 248
SHEET 1 D 4 ARG B 8 THR B 10 0
SHEET 2 D 4 GLN B 77 ALA B 82 1 O PHE B 80 N THR B 10
SHEET 3 D 4 PHE B 45 VAL B 50 -1 N GLN B 48 O LYS B 79
SHEET 4 D 4 SER B 56 TRP B 58 -1 O THR B 57 N TYR B 49
SHEET 1 E 7 ILE B 238 PRO B 241 0
SHEET 2 E 7 GLY B 224 GLU B 229 -1 N ILE B 227 O ILE B 238
SHEET 3 E 7 GLU B 215 ASP B 221 -1 N GLY B 219 O ASN B 226
SHEET 4 E 7 VAL B 203 ASN B 210 -1 N ILE B 208 O LEU B 216
SHEET 5 E 7 PHE B 267 TYR B 270 -1 O TYR B 270 N LYS B 209
SHEET 6 E 7 LYS B 254 PRO B 259 -1 N ILE B 257 O PHE B 267
SHEET 7 E 7 ILE B 245 ASN B 251 -1 N SER B 249 O VAL B 256
CRYST1 57.218 70.218 110.810 90.00 98.97 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 0.017477 0.000000 0.002759 0.00000
SCALE2 0.000000 0.014241 0.000000 0.00000
SCALE3 0.000000 0.000000 0.009136 0.00000
(ATOM LINES ARE NOT SHOWN.)
END