HEADER CONTRACTILE PROTEIN 08-JUN-04 1WKU
TITLE HIGH RESOLUTION STRUCTURE OF THE HUMAN ALPHA-ACTININ
TITLE 2 ISOFORM 3
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ALPHA-ACTININ 3;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: ACTIN BINDING DOMAIN (ABD);
COMPND 5 SYNONYM: ALPHA ACTININ SKELETAL MUSCLE ISOFORM 3, F-ACTIN
COMPND 6 CROSS LINKING PROTEIN;
COMPND 7 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: ACTN3;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21[DE3];
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET
KEYWDS CALPONIN HOMOLOGY DOMAIN, ACTIN BINDING DOMAIN, CONTRACTILE
KEYWDS 2 PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR G.FRANZOT,B.SJOBLOM,M.GAUTEL,K.DJINOVIC CARUGO
REVDAT 2 24-FEB-09 1WKU 1 VERSN
REVDAT 1 17-MAY-05 1WKU 0
JRNL AUTH G.FRANZOT,B.SJOBLOM,M.GAUTEL,K.DJINOVIC CARUGO
JRNL TITL THE CRYSTAL STRUCTURE OF THE ACTIN BINDING DOMAIN
JRNL TITL 2 FROM ALPHA-ACTININ IN ITS CLOSED CONFORMATION:
JRNL TITL 3 STRUCTURAL INSIGHT INTO PHOSPHOLIPID REGULATION OF
JRNL TITL 4 ALPHA-ACTININ
JRNL REF J.MOL.BIOL. V. 348 151 2005
JRNL REFN ISSN 0022-2836
JRNL PMID 15808860
JRNL DOI 10.1016/J.JMB.2005.01.002
REMARK 1
REMARK 2
REMARK 2 RESOLUTION. 1.60 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) : 1.60
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 33.42
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 197138.000
REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0000
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 94.0
REMARK 3 NUMBER OF REFLECTIONS : 56760
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) : 0.182
REMARK 3 FREE R VALUE : 0.208
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 7.100
REMARK 3 FREE R VALUE TEST SET COUNT : 4024
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.003
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) : 1.60
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.70
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 87.90
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 8218
REMARK 3 BIN R VALUE (WORKING SET) : 0.2050
REMARK 3 BIN FREE R VALUE : 0.2340
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 7.10
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 626
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.009
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 3626
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 459
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 18.50
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 19.80
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 3.00000
REMARK 3 B22 (A**2) : 0.69000
REMARK 3 B33 (A**2) : -3.69000
REMARK 3 B12 (A**2) : 0.73000
REMARK 3 B13 (A**2) : 1.39000
REMARK 3 B23 (A**2) : 3.71000
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.16
REMARK 3 ESD FROM SIGMAA (A) : 0.07
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) : 0.19
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.09
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.004
REMARK 3 BOND ANGLES (DEGREES) : 1.10
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 19.90
REMARK 3 IMPROPER ANGLES (DEGREES) : 0.77
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 : 0.37
REMARK 3 BSOL : 46.76
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 : NULL
REMARK 3 TOPOLOGY FILE 1 : PROTEIN.TOP
REMARK 3 TOPOLOGY FILE 2 : NULL
REMARK 3 TOPOLOGY FILE 3 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1WKU COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 22-JUN-04.
REMARK 100 THE RCSB ID CODE IS RCSB023686.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : NULL
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 5.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ELETTRA
REMARK 200 BEAMLINE : 5.2R
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 : SI111
REMARK 200 OPTICS : GRAPHITE MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 56760
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.600
REMARK 200 RESOLUTION RANGE LOW (A) : 33.420
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 94.0
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) : 1.60
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.70
REMARK 200 COMPLETENESS FOR SHELL (%) : 87.9
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: AMORE
REMARK 200 STARTING MODEL: LOW RESOLUTION MODEL OF DIFFERENT SPACE GROUP
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 39.04
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.02
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 20000, SODIUM ACETATE, PH 5.0,
REMARK 280 VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 298.0K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,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
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 HIS A 20
REMARK 465 HIS A 21
REMARK 465 HIS A 22
REMARK 465 HIS A 23
REMARK 465 HIS A 24
REMARK 465 HIS A 25
REMARK 465 TYR A 26
REMARK 465 MET A 27
REMARK 465 GLU A 28
REMARK 465 GLN A 29
REMARK 465 GLU A 30
REMARK 465 GLU A 31
REMARK 465 ASP A 32
REMARK 465 TRP A 33
REMARK 465 ASP A 34
REMARK 465 ARG A 35
REMARK 465 ASP A 36
REMARK 465 LEU A 37
REMARK 465 LEU A 38
REMARK 465 LEU A 39
REMARK 465 ASP A 40
REMARK 465 PRO A 41
REMARK 465 GLU A 267
REMARK 465 GLN A 268
REMARK 465 ALA A 269
REMARK 465 GLU A 270
REMARK 465 THR A 271
REMARK 465 ALA A 272
REMARK 465 ALA A 273
REMARK 465 HIS B 20
REMARK 465 HIS B 21
REMARK 465 HIS B 22
REMARK 465 HIS B 23
REMARK 465 HIS B 24
REMARK 465 HIS B 25
REMARK 465 TYR B 26
REMARK 465 MET B 27
REMARK 465 GLU B 28
REMARK 465 GLN B 29
REMARK 465 GLU B 30
REMARK 465 GLU B 31
REMARK 465 ASP B 32
REMARK 465 TRP B 33
REMARK 465 ASP B 34
REMARK 465 ARG B 35
REMARK 465 ASP B 36
REMARK 465 LEU B 37
REMARK 465 LEU B 38
REMARK 465 LEU B 39
REMARK 465 ASP B 40
REMARK 465 PRO B 41
REMARK 465 ALA B 269
REMARK 465 GLU B 270
REMARK 465 THR B 271
REMARK 465 ALA B 272
REMARK 465 ALA B 273
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 123 -26.70 70.03
REMARK 500 ASN A 133 98.10 -165.92
REMARK 500 ALA A 160 -136.07 51.42
REMARK 500 ASN A 179 85.25 -154.52
REMARK 500 HIS A 184 -93.44 -141.13
REMARK 500 ALA B 160 -136.48 51.21
REMARK 500 ASN B 179 84.84 -152.12
REMARK 500 HIS B 184 -92.38 -144.07
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH B 448 DISTANCE = 5.39 ANGSTROMS
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1AOA RELATED DB: PDB
REMARK 900 FIMBRIN
REMARK 900 RELATED ID: 1DXX RELATED DB: PDB
REMARK 900 DYSTROPHIN
REMARK 900 RELATED ID: 1MB8 RELATED DB: PDB
REMARK 900 PLECTIN
REMARK 900 RELATED ID: 1QAG RELATED DB: PDB
REMARK 900 UTROPHIN
REMARK 900 RELATED ID: 1TJT RELATED DB: PDB
REMARK 900 THE SAME PROTEIN AT 2.2 ANGSTROM
DBREF 1WKU A 26 273 UNP Q08043 ACTN3_HUMAN 26 273
DBREF 1WKU B 26 273 UNP Q08043 ACTN3_HUMAN 26 273
SEQADV 1WKU HIS A 20 UNP Q08043 EXPRESSION TAG
SEQADV 1WKU HIS A 21 UNP Q08043 EXPRESSION TAG
SEQADV 1WKU HIS A 22 UNP Q08043 EXPRESSION TAG
SEQADV 1WKU HIS A 23 UNP Q08043 EXPRESSION TAG
SEQADV 1WKU HIS A 24 UNP Q08043 EXPRESSION TAG
SEQADV 1WKU HIS A 25 UNP Q08043 EXPRESSION TAG
SEQADV 1WKU HIS B 20 UNP Q08043 EXPRESSION TAG
SEQADV 1WKU HIS B 21 UNP Q08043 EXPRESSION TAG
SEQADV 1WKU HIS B 22 UNP Q08043 EXPRESSION TAG
SEQADV 1WKU HIS B 23 UNP Q08043 EXPRESSION TAG
SEQADV 1WKU HIS B 24 UNP Q08043 EXPRESSION TAG
SEQADV 1WKU HIS B 25 UNP Q08043 EXPRESSION TAG
SEQRES 1 A 254 HIS HIS HIS HIS HIS HIS TYR MET GLU GLN GLU GLU ASP
SEQRES 2 A 254 TRP ASP ARG ASP LEU LEU LEU ASP PRO ALA TRP GLU LYS
SEQRES 3 A 254 GLN GLN ARG LYS THR PHE THR ALA TRP CYS ASN SER HIS
SEQRES 4 A 254 LEU ARG LYS ALA GLY THR GLN ILE GLU ASN ILE GLU GLU
SEQRES 5 A 254 ASP PHE ARG ASN GLY LEU LYS LEU MET LEU LEU LEU GLU
SEQRES 6 A 254 VAL ILE SER GLY GLU ARG LEU PRO ARG PRO ASP LYS GLY
SEQRES 7 A 254 LYS MET ARG PHE HIS LYS ILE ALA ASN VAL ASN LYS ALA
SEQRES 8 A 254 LEU ASP PHE ILE ALA SER LYS GLY VAL LYS LEU VAL SER
SEQRES 9 A 254 ILE GLY ALA GLU GLU ILE VAL ASP GLY ASN LEU LYS MET
SEQRES 10 A 254 THR LEU GLY MET ILE TRP THR ILE ILE LEU ARG PHE ALA
SEQRES 11 A 254 ILE GLN ASP ILE SER VAL GLU GLU THR SER ALA LYS GLU
SEQRES 12 A 254 GLY LEU LEU LEU TRP CYS GLN ARG LYS THR ALA PRO TYR
SEQRES 13 A 254 ARG ASN VAL ASN VAL GLN ASN PHE HIS THR SER TRP LYS
SEQRES 14 A 254 ASP GLY LEU ALA LEU CYS ALA LEU ILE HIS ARG HIS ARG
SEQRES 15 A 254 PRO ASP LEU ILE ASP TYR ALA LYS LEU ARG LYS ASP ASP
SEQRES 16 A 254 PRO ILE GLY ASN LEU ASN THR ALA PHE GLU VAL ALA GLU
SEQRES 17 A 254 LYS TYR LEU ASP ILE PRO LYS MET LEU ASP ALA GLU ASP
SEQRES 18 A 254 ILE VAL ASN THR PRO LYS PRO ASP GLU LYS ALA ILE MET
SEQRES 19 A 254 THR TYR VAL SER CYS PHE TYR HIS ALA PHE ALA GLY ALA
SEQRES 20 A 254 GLU GLN ALA GLU THR ALA ALA
SEQRES 1 B 254 HIS HIS HIS HIS HIS HIS TYR MET GLU GLN GLU GLU ASP
SEQRES 2 B 254 TRP ASP ARG ASP LEU LEU LEU ASP PRO ALA TRP GLU LYS
SEQRES 3 B 254 GLN GLN ARG LYS THR PHE THR ALA TRP CYS ASN SER HIS
SEQRES 4 B 254 LEU ARG LYS ALA GLY THR GLN ILE GLU ASN ILE GLU GLU
SEQRES 5 B 254 ASP PHE ARG ASN GLY LEU LYS LEU MET LEU LEU LEU GLU
SEQRES 6 B 254 VAL ILE SER GLY GLU ARG LEU PRO ARG PRO ASP LYS GLY
SEQRES 7 B 254 LYS MET ARG PHE HIS LYS ILE ALA ASN VAL ASN LYS ALA
SEQRES 8 B 254 LEU ASP PHE ILE ALA SER LYS GLY VAL LYS LEU VAL SER
SEQRES 9 B 254 ILE GLY ALA GLU GLU ILE VAL ASP GLY ASN LEU LYS MET
SEQRES 10 B 254 THR LEU GLY MET ILE TRP THR ILE ILE LEU ARG PHE ALA
SEQRES 11 B 254 ILE GLN ASP ILE SER VAL GLU GLU THR SER ALA LYS GLU
SEQRES 12 B 254 GLY LEU LEU LEU TRP CYS GLN ARG LYS THR ALA PRO TYR
SEQRES 13 B 254 ARG ASN VAL ASN VAL GLN ASN PHE HIS THR SER TRP LYS
SEQRES 14 B 254 ASP GLY LEU ALA LEU CYS ALA LEU ILE HIS ARG HIS ARG
SEQRES 15 B 254 PRO ASP LEU ILE ASP TYR ALA LYS LEU ARG LYS ASP ASP
SEQRES 16 B 254 PRO ILE GLY ASN LEU ASN THR ALA PHE GLU VAL ALA GLU
SEQRES 17 B 254 LYS TYR LEU ASP ILE PRO LYS MET LEU ASP ALA GLU ASP
SEQRES 18 B 254 ILE VAL ASN THR PRO LYS PRO ASP GLU LYS ALA ILE MET
SEQRES 19 B 254 THR TYR VAL SER CYS PHE TYR HIS ALA PHE ALA GLY ALA
SEQRES 20 B 254 GLU GLN ALA GLU THR ALA ALA
FORMUL 3 HOH *459(H2 O)
HELIX 1 1 ALA A 42 ARG A 60 1 19
HELIX 2 2 LYS A 61 GLY A 63 5 3
HELIX 3 3 GLY A 76 GLY A 88 1 13
HELIX 4 4 MET A 99 SER A 116 1 18
HELIX 5 5 GLY A 125 GLY A 132 1 8
HELIX 6 6 ASN A 133 ILE A 150 1 18
HELIX 7 7 ALA A 160 ALA A 173 1 14
HELIX 8 8 HIS A 184 LYS A 188 5 5
HELIX 9 9 GLY A 190 ARG A 201 1 12
HELIX 10 10 ASP A 206 LEU A 210 5 5
HELIX 11 11 ASP A 214 LEU A 230 1 17
HELIX 12 12 ASP A 237 THR A 244 1 8
HELIX 13 13 ASP A 248 ALA A 266 1 19
HELIX 14 14 ALA B 42 ARG B 60 1 19
HELIX 15 15 LYS B 61 GLY B 63 5 3
HELIX 16 16 GLY B 76 GLY B 88 1 13
HELIX 17 17 MET B 99 SER B 116 1 18
HELIX 18 18 GLY B 125 ASP B 131 1 7
HELIX 19 19 ASN B 133 ILE B 150 1 18
HELIX 20 20 ALA B 160 ALA B 173 1 14
HELIX 21 21 HIS B 184 LYS B 188 5 5
HELIX 22 22 GLY B 190 ARG B 201 1 12
HELIX 23 23 PRO B 202 ILE B 205 5 4
HELIX 24 24 ASP B 206 LEU B 210 5 5
HELIX 25 25 ASP B 214 LEU B 230 1 17
HELIX 26 26 ASP B 237 THR B 244 1 8
HELIX 27 27 ASP B 248 ALA B 266 1 19
SHEET 1 A 2 SER A 154 VAL A 155 0
SHEET 2 A 2 THR A 158 SER A 159 -1 O THR A 158 N VAL A 155
SHEET 1 B 2 SER B 154 VAL B 155 0
SHEET 2 B 2 THR B 158 SER B 159 -1 O THR B 158 N VAL B 155
CRYST1 38.499 45.960 66.998 86.67 87.80 87.33 P 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 0.025975 -0.001211 -0.000931 0.00000
SCALE2 0.000000 0.021782 -0.001230 0.00000
SCALE3 0.000000 0.000000 0.014961 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
