HEADER SIGNALING PROTEIN 21-MAY-04 1WDZ
TITLE CRYSTAL STRUCTURE OF RCB DOMAIN OF IRSP53
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: INSULIN RECEPTOR SUBSTRATE P53;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: N-TERMINAL DOMAIN;
COMPND 5 SYNONYM: IRSP53;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PGEX-4T-1
KEYWDS CELLULAR SIGNALING PROTEIN, RIKEN STRUCTURAL GENOMICS/PROTEOMICS
KEYWDS 2 INITIATIVE, RSGI, STRUCTURAL GENOMICS, SIGNALING PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR K.MURAYAMA,S.SUETSUGU,A.SETO,M.SHIROUZU,T.TAKENAWA,S.YOKOYAMA,RIKEN
AUTHOR 2 STRUCTURAL GENOMICS/PROTEOMICS INITIATIVE (RSGI)
REVDAT 3 13-MAR-24 1WDZ 1 SEQADV
REVDAT 2 24-FEB-09 1WDZ 1 VERSN
REVDAT 1 07-JUN-05 1WDZ 0
JRNL AUTH K.MURAYAMA,S.SUETSUGU,A.SETO,M.SHIROUZU,T.TAKENAWA,
JRNL AUTH 2 S.YOKOYAMA
JRNL TITL CRYSTAL STRUCTURE OF RCB DOMAIN OF IRSP53
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.63 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 1.1
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 : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.63
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 41.94
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 576339.670
REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0000
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 98.4
REMARK 3 NUMBER OF REFLECTIONS : 15846
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) : 0.235
REMARK 3 FREE R VALUE : 0.297
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 10.100
REMARK 3 FREE R VALUE TEST SET COUNT : 1593
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.007
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) : 2.63
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.79
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 97.40
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 2314
REMARK 3 BIN R VALUE (WORKING SET) : 0.3200
REMARK 3 BIN FREE R VALUE : 0.4220
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 10.70
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 276
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.025
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 3642
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 70
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 38.40
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 51.00
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -12.78000
REMARK 3 B22 (A**2) : 1.24000
REMARK 3 B33 (A**2) : 11.54000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 12.93000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.35
REMARK 3 ESD FROM SIGMAA (A) : 0.34
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) : 0.50
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.47
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.007
REMARK 3 BOND ANGLES (DEGREES) : 1.100
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 15.70
REMARK 3 IMPROPER ANGLES (DEGREES) : 0.760
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 : 0.29
REMARK 3 BSOL : 25.47
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 1WDZ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 21-MAY-04.
REMARK 100 THE DEPOSITION ID IS D_1000023476.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 22-OCT-02
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SPRING-8
REMARK 200 BEAMLINE : BL44B2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.00
REMARK 200 MONOCHROMATOR : SI 111 CHANNEL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 15858
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.630
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.6
REMARK 200 DATA REDUNDANCY : 4.200
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.05900
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 26.1000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.63
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.75
REMARK 200 COMPLETENESS FOR SHELL (%) : 98.2
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.30300
REMARK 200 <I/SIGMA(I)> FOR SHELL : 5.500
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SIRAS
REMARK 200 SOFTWARE USED: SOLVE
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 47.40
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.34
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 27% PEG4000, 0.09M TRIS PH8.5, 0.19M
REMARK 280 SODIUM ACETATE, 3.5% MPD, VAPOR DIFFUSION, HANGING DROP,
REMARK 280 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 34.62900
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: 5510 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 24840 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -58.0 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 GLY A -2
REMARK 465 SER A -1
REMARK 465 THR A 0
REMARK 465 MET A 1
REMARK 465 SER A 233
REMARK 465 GLY A 234
REMARK 465 ARG A 235
REMARK 465 ILE A 236
REMARK 465 VAL A 237
REMARK 465 THR A 238
REMARK 465 ASP A 239
REMARK 465 GLY B -2
REMARK 465 SER B -1
REMARK 465 THR B 0
REMARK 465 MET B 1
REMARK 465 GLY B 150
REMARK 465 SER B 151
REMARK 465 LYS B 152
REMARK 465 ASN B 153
REMARK 465 PRO B 154
REMARK 465 GLN B 155
REMARK 465 LYS B 156
REMARK 465 TYR B 157
REMARK 465 SER B 158
REMARK 465 SER B 233
REMARK 465 GLY B 234
REMARK 465 ARG B 235
REMARK 465 ILE B 236
REMARK 465 VAL B 237
REMARK 465 THR B 238
REMARK 465 ASP B 239
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 4 177.41 64.01
REMARK 500 GLN A 23 -54.63 -133.60
REMARK 500 LEU A 101 -68.59 -108.78
REMARK 500 LYS A 146 5.07 -67.53
REMARK 500 LEU B 3 -147.59 -92.08
REMARK 500 LEU B 101 -67.57 -109.03
REMARK 500 ALA B 139 4.23 -68.47
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: SRZ001000130.1 RELATED DB: TARGETDB
DBREF 1WDZ A 1 228 UNP Q9UQB8 BAIP2_HUMAN 1 228
DBREF 1WDZ B 1 228 UNP Q9UQB8 BAIP2_HUMAN 1 228
SEQADV 1WDZ GLY A -2 UNP Q9UQB8 CLONING ARTIFACT
SEQADV 1WDZ SER A -1 UNP Q9UQB8 CLONING ARTIFACT
SEQADV 1WDZ THR A 0 UNP Q9UQB8 CLONING ARTIFACT
SEQADV 1WDZ GLY A 229 UNP Q9UQB8 CLONING ARTIFACT
SEQADV 1WDZ VAL A 230 UNP Q9UQB8 CLONING ARTIFACT
SEQADV 1WDZ ASP A 231 UNP Q9UQB8 CLONING ARTIFACT
SEQADV 1WDZ SER A 232 UNP Q9UQB8 CLONING ARTIFACT
SEQADV 1WDZ SER A 233 UNP Q9UQB8 CLONING ARTIFACT
SEQADV 1WDZ GLY A 234 UNP Q9UQB8 CLONING ARTIFACT
SEQADV 1WDZ ARG A 235 UNP Q9UQB8 CLONING ARTIFACT
SEQADV 1WDZ ILE A 236 UNP Q9UQB8 CLONING ARTIFACT
SEQADV 1WDZ VAL A 237 UNP Q9UQB8 CLONING ARTIFACT
SEQADV 1WDZ THR A 238 UNP Q9UQB8 CLONING ARTIFACT
SEQADV 1WDZ ASP A 239 UNP Q9UQB8 CLONING ARTIFACT
SEQADV 1WDZ GLY B -2 UNP Q9UQB8 CLONING ARTIFACT
SEQADV 1WDZ SER B -1 UNP Q9UQB8 CLONING ARTIFACT
SEQADV 1WDZ THR B 0 UNP Q9UQB8 CLONING ARTIFACT
SEQADV 1WDZ GLY B 229 UNP Q9UQB8 CLONING ARTIFACT
SEQADV 1WDZ VAL B 230 UNP Q9UQB8 CLONING ARTIFACT
SEQADV 1WDZ ASP B 231 UNP Q9UQB8 CLONING ARTIFACT
SEQADV 1WDZ SER B 232 UNP Q9UQB8 CLONING ARTIFACT
SEQADV 1WDZ SER B 233 UNP Q9UQB8 CLONING ARTIFACT
SEQADV 1WDZ GLY B 234 UNP Q9UQB8 CLONING ARTIFACT
SEQADV 1WDZ ARG B 235 UNP Q9UQB8 CLONING ARTIFACT
SEQADV 1WDZ ILE B 236 UNP Q9UQB8 CLONING ARTIFACT
SEQADV 1WDZ VAL B 237 UNP Q9UQB8 CLONING ARTIFACT
SEQADV 1WDZ THR B 238 UNP Q9UQB8 CLONING ARTIFACT
SEQADV 1WDZ ASP B 239 UNP Q9UQB8 CLONING ARTIFACT
SEQRES 1 A 242 GLY SER THR MET SER LEU SER ARG SER GLU GLU MET HIS
SEQRES 2 A 242 ARG LEU THR GLU ASN VAL TYR LYS THR ILE MET GLU GLN
SEQRES 3 A 242 PHE ASN PRO SER LEU ARG ASN PHE ILE ALA MET GLY LYS
SEQRES 4 A 242 ASN TYR GLU LYS ALA LEU ALA GLY VAL THR TYR ALA ALA
SEQRES 5 A 242 LYS GLY TYR PHE ASP ALA LEU VAL LYS MET GLY GLU LEU
SEQRES 6 A 242 ALA SER GLU SER GLN GLY SER LYS GLU LEU GLY ASP VAL
SEQRES 7 A 242 LEU PHE GLN MET ALA GLU VAL HIS ARG GLN ILE GLN ASN
SEQRES 8 A 242 GLN LEU GLU GLU MET LEU LYS SER PHE HIS ASN GLU LEU
SEQRES 9 A 242 LEU THR GLN LEU GLU GLN LYS VAL GLU LEU ASP SER ARG
SEQRES 10 A 242 TYR LEU SER ALA ALA LEU LYS LYS TYR GLN THR GLU GLN
SEQRES 11 A 242 ARG SER LYS GLY ASP ALA LEU ASP LYS CYS GLN ALA GLU
SEQRES 12 A 242 LEU LYS LYS LEU ARG LYS LYS SER GLN GLY SER LYS ASN
SEQRES 13 A 242 PRO GLN LYS TYR SER ASP LYS GLU LEU GLN TYR ILE ASP
SEQRES 14 A 242 ALA ILE SER ASN LYS GLN GLY GLU LEU GLU ASN TYR VAL
SEQRES 15 A 242 SER ASP GLY TYR LYS THR ALA LEU THR GLU GLU ARG ARG
SEQRES 16 A 242 ARG PHE CYS PHE LEU VAL GLU LYS GLN CYS ALA VAL ALA
SEQRES 17 A 242 LYS ASN SER ALA ALA TYR HIS SER LYS GLY LYS GLU LEU
SEQRES 18 A 242 LEU ALA GLN LYS LEU PRO LEU TRP GLN GLN GLY VAL ASP
SEQRES 19 A 242 SER SER GLY ARG ILE VAL THR ASP
SEQRES 1 B 242 GLY SER THR MET SER LEU SER ARG SER GLU GLU MET HIS
SEQRES 2 B 242 ARG LEU THR GLU ASN VAL TYR LYS THR ILE MET GLU GLN
SEQRES 3 B 242 PHE ASN PRO SER LEU ARG ASN PHE ILE ALA MET GLY LYS
SEQRES 4 B 242 ASN TYR GLU LYS ALA LEU ALA GLY VAL THR TYR ALA ALA
SEQRES 5 B 242 LYS GLY TYR PHE ASP ALA LEU VAL LYS MET GLY GLU LEU
SEQRES 6 B 242 ALA SER GLU SER GLN GLY SER LYS GLU LEU GLY ASP VAL
SEQRES 7 B 242 LEU PHE GLN MET ALA GLU VAL HIS ARG GLN ILE GLN ASN
SEQRES 8 B 242 GLN LEU GLU GLU MET LEU LYS SER PHE HIS ASN GLU LEU
SEQRES 9 B 242 LEU THR GLN LEU GLU GLN LYS VAL GLU LEU ASP SER ARG
SEQRES 10 B 242 TYR LEU SER ALA ALA LEU LYS LYS TYR GLN THR GLU GLN
SEQRES 11 B 242 ARG SER LYS GLY ASP ALA LEU ASP LYS CYS GLN ALA GLU
SEQRES 12 B 242 LEU LYS LYS LEU ARG LYS LYS SER GLN GLY SER LYS ASN
SEQRES 13 B 242 PRO GLN LYS TYR SER ASP LYS GLU LEU GLN TYR ILE ASP
SEQRES 14 B 242 ALA ILE SER ASN LYS GLN GLY GLU LEU GLU ASN TYR VAL
SEQRES 15 B 242 SER ASP GLY TYR LYS THR ALA LEU THR GLU GLU ARG ARG
SEQRES 16 B 242 ARG PHE CYS PHE LEU VAL GLU LYS GLN CYS ALA VAL ALA
SEQRES 17 B 242 LYS ASN SER ALA ALA TYR HIS SER LYS GLY LYS GLU LEU
SEQRES 18 B 242 LEU ALA GLN LYS LEU PRO LEU TRP GLN GLN GLY VAL ASP
SEQRES 19 B 242 SER SER GLY ARG ILE VAL THR ASP
FORMUL 3 HOH *70(H2 O)
HELIX 1 1 LEU A 3 GLN A 23 1 21
HELIX 2 2 GLN A 23 GLU A 65 1 43
HELIX 3 3 SER A 69 GLU A 100 1 32
HELIX 4 4 LEU A 101 LEU A 111 1 11
HELIX 5 5 LEU A 111 LYS A 146 1 36
HELIX 6 6 LYS A 147 SER A 148 5 2
HELIX 7 7 GLN A 149 ASN A 153 5 5
HELIX 8 8 PRO A 154 SER A 232 1 79
HELIX 9 9 ARG B 5 GLN B 23 1 19
HELIX 10 10 GLN B 23 SER B 66 1 44
HELIX 11 11 SER B 69 LEU B 101 1 33
HELIX 12 12 LEU B 101 GLU B 110 1 10
HELIX 13 13 LEU B 111 LYS B 146 1 36
HELIX 14 14 GLU B 161 SER B 232 1 72
CRYST1 60.833 69.258 68.715 90.00 110.12 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 0.016438 0.000000 0.006023 0.00000
SCALE2 0.000000 0.014439 0.000000 0.00000
SCALE3 0.000000 0.000000 0.015499 0.00000
(ATOM LINES ARE NOT SHOWN.)
END