HEADER PROTEIN BINDING 01-SEP-06 2J4O
TITLE STRUCTURE OF TAB1
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: MITOGEN-ACTIVATED PROTEIN KINASE KINASE KINASE 7-
COMPND 3 INTERACTING PROTEIN 1;
COMPND 4 CHAIN: A;
COMPND 5 FRAGMENT: N-TERMINAL PP2C-LIKE DOMAIN, RESIDUES 1-401;
COMPND 6 SYNONYM: TGF-BETA-ACTIVATED KINASE 1-BINDING PROTEIN 1, TAK1-BINDING
COMPND 7 PROTEIN 1, TAB1;
COMPND 8 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
KEYWDS TGF-BETA, PSEUDO-PHOSPHATASE, TAK1 BINDING PROTEIN, PROTEIN BINDING
EXPDTA X-RAY DIFFRACTION
AUTHOR D.VAN AALTEN
REVDAT 3 06-MAR-19 2J4O 1 REMARK
REVDAT 2 24-FEB-09 2J4O 1 VERSN
REVDAT 1 04-SEP-06 2J4O 0
JRNL AUTH S.H.CONNER,G.KULAR,M.PEGGIE,S.SHEPHERD,A.W.SCHUTTELKOPF,
JRNL AUTH 2 P.COHEN,D.M.F.VAN AALTEN
JRNL TITL TAK1-BINDING PROTEIN 1 IS A PSEUDOPHOSPHATASE.
JRNL REF BIOCHEM.J. V. 399 427 2006
JRNL REFN ISSN 0264-6021
JRNL PMID 16879102
JRNL DOI 10.1042/BJ20061077
REMARK 2
REMARK 2 RESOLUTION. 2.25 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 : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.25
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 20.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 10000.000
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 93.3
REMARK 3 NUMBER OF REFLECTIONS : 34008
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) : 0.228
REMARK 3 FREE R VALUE : 0.236
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 1.400
REMARK 3 FREE R VALUE TEST SET COUNT : 519
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 : 2736
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 83
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) : -8.25000
REMARK 3 B22 (A**2) : -8.25000
REMARK 3 B33 (A**2) : 16.50000
REMARK 3 B12 (A**2) : -4.94300
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
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) : 0.011
REMARK 3 BOND ANGLES (DEGREES) : 1.815
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 : 0.33
REMARK 3 BSOL : 43.87
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 : DNA-RNA_REP.PARAM
REMARK 3 PARAMETER FILE 3 : WATER_REP.PARAM
REMARK 3 PARAMETER FILE 4 : ION.PARAM
REMARK 3 PARAMETER FILE 5 : NULL
REMARK 3 TOPOLOGY FILE 1 : PROTEIN.TOP
REMARK 3 TOPOLOGY FILE 2 : DNA-RNA.TOP
REMARK 3 TOPOLOGY FILE 3 : WATER.TOP
REMARK 3 TOPOLOGY FILE 4 : ION.TOP
REMARK 3 TOPOLOGY FILE 5 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 2J4O COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 01-SEP-06.
REMARK 100 THE DEPOSITION ID IS D_1290029883.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 01-SEP-05
REMARK 200 TEMPERATURE (KELVIN) : 100.0
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : BM14
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.03962
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
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 : 151048
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.250
REMARK 200 RESOLUTION RANGE LOW (A) : 20.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.0
REMARK 200 DATA REDUNDANCY : 4.200
REMARK 200 R MERGE (I) : 0.07000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 13.6000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.25
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.33
REMARK 200 COMPLETENESS FOR SHELL (%) : 82.4
REMARK 200 DATA REDUNDANCY IN SHELL : 3.30
REMARK 200 R MERGE FOR SHELL (I) : 0.47000
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: SAD
REMARK 200 SOFTWARE USED: SHELX
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 72.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.40
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: TAB1, WAS CONCENTRATED TO 14.1 MG/ML,
REMARK 280 AND CRYSTALLISED BY VAPOUR DIFFUSION. 1 MICROL OF PROTEIN WAS
REMARK 280 MIXED WITH 1 MICROL OF MOTHER LIQUOR (100 MM HEPES PH 7.5, 1.5 M
REMARK 280 LI2SO4) AND 0.25 MICROL 100 MM BACL2. HEXAGONALLY-SHAPED
REMARK 280 CRYSTALS APPEARED WITHIN THREE DAYS., VAPOR DIFFUSION
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 3 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z
REMARK 290 3555 -X+Y,-X,Z
REMARK 290 4555 Y,X,-Z
REMARK 290 5555 X-Y,-Y,-Z
REMARK 290 6555 -X,-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 SMTRY1 2 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 4 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 5 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 6 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 6 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 6 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: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PQS
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 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 ALA A 2
REMARK 465 ALA A 3
REMARK 465 GLN A 4
REMARK 465 ARG A 5
REMARK 465 ARG A 6
REMARK 465 SER A 7
REMARK 465 LEU A 8
REMARK 465 LEU A 9
REMARK 465 GLN A 10
REMARK 465 SER A 11
REMARK 465 GLU A 12
REMARK 465 GLN A 13
REMARK 465 GLN A 14
REMARK 465 PRO A 15
REMARK 465 MET A 372
REMARK 465 SER A 373
REMARK 465 GLN A 374
REMARK 465 PRO A 375
REMARK 465 THR A 376
REMARK 465 PRO A 377
REMARK 465 SER A 378
REMARK 465 PRO A 379
REMARK 465 ALA A 380
REMARK 465 PRO A 381
REMARK 465 ALA A 382
REMARK 465 ALA A 383
REMARK 465 GLY A 384
REMARK 465 GLY A 385
REMARK 465 ARG A 386
REMARK 465 VAL A 387
REMARK 465 TYR A 388
REMARK 465 PRO A 389
REMARK 465 VAL A 390
REMARK 465 SER A 391
REMARK 465 VAL A 392
REMARK 465 PRO A 393
REMARK 465 TYR A 394
REMARK 465 SER A 395
REMARK 465 SER A 396
REMARK 465 ALA A 397
REMARK 465 GLN A 398
REMARK 465 SER A 399
REMARK 465 THR A 400
REMARK 465 SER A 401
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 GLU A 371 CA C O CB CG CD OE1
REMARK 470 GLU A 371 OE2
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 O TRP A 17 OD2 ASP A 20 2.17
REMARK 500
REMARK 500 REMARK: NULL
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 22 C - N - CA ANGL. DEV. = 13.7 DEGREES
REMARK 500 PRO A 140 C - N - CA ANGL. DEV. = 10.5 DEGREES
REMARK 500 PRO A 302 C - N - CA ANGL. DEV. = 9.0 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 PRO A 22 110.54 -6.91
REMARK 500 LYS A 42 81.96 164.43
REMARK 500 GLU A 59 158.56 -29.94
REMARK 500 ASN A 60 43.51 35.97
REMARK 500 ASN A 61 77.32 38.78
REMARK 500 ASN A 94 134.65 -177.50
REMARK 500 GLU A 96 -25.73 -172.21
REMARK 500 ALA A 98 137.63 77.38
REMARK 500 GLU A 99 -73.37 -11.46
REMARK 500 PRO A 140 146.06 -14.97
REMARK 500 HIS A 142 -159.08 -87.67
REMARK 500 GLN A 143 42.30 38.37
REMARK 500 PRO A 145 138.36 -31.96
REMARK 500 ASN A 175 78.77 25.53
REMARK 500 ASN A 176 19.37 48.37
REMARK 500 THR A 194 -139.46 -115.09
REMARK 500 ASP A 196 -3.09 147.60
REMARK 500 ASP A 245 88.63 61.05
REMARK 500 ASP A 256 -62.51 -15.66
REMARK 500 ALA A 275 106.24 152.90
REMARK 500 SER A 344 -120.03 -66.31
REMARK 500 GLU A 347 -90.67 57.98
REMARK 500 ARG A 348 -21.53 -34.45
REMARK 500
REMARK 500 REMARK: NULL
REMARK 700
REMARK 700 SHEET
REMARK 700 THE SHEET STRUCTURE OF THIS MOLECULE IS BIFURCATED. IN
REMARK 700 ORDER TO REPRESENT THIS FEATURE IN THE SHEET RECORDS BELOW,
REMARK 700 TWO SHEETS ARE DEFINED.
DBREF 2J4O A 1 401 UNP Q15750 TAB1_HUMAN 1 401
SEQRES 1 A 401 MET ALA ALA GLN ARG ARG SER LEU LEU GLN SER GLU GLN
SEQRES 2 A 401 GLN PRO SER TRP THR ASP ASP LEU PRO LEU CYS HIS LEU
SEQRES 3 A 401 SER GLY VAL GLY SER ALA SER ASN ARG SER TYR SER ALA
SEQRES 4 A 401 ASP GLY LYS GLY THR GLU SER HIS PRO PRO GLU ASP SER
SEQRES 5 A 401 TRP LEU LYS PHE ARG SER GLU ASN ASN CYS PHE LEU TYR
SEQRES 6 A 401 GLY VAL PHE ASN GLY TYR ASP GLY ASN ARG VAL THR ASN
SEQRES 7 A 401 PHE VAL ALA GLN ARG LEU SER ALA GLU LEU LEU LEU GLY
SEQRES 8 A 401 GLN LEU ASN ALA GLU HIS ALA GLU ALA ASP VAL ARG ARG
SEQRES 9 A 401 VAL LEU LEU GLN ALA PHE ASP VAL VAL GLU ARG SER PHE
SEQRES 10 A 401 LEU GLU SER ILE ASP ASP ALA LEU ALA GLU LYS ALA SER
SEQRES 11 A 401 LEU GLN SER GLN LEU PRO GLU GLY VAL PRO GLN HIS GLN
SEQRES 12 A 401 LEU PRO PRO GLN TYR GLN LYS ILE LEU GLU ARG LEU LYS
SEQRES 13 A 401 THR LEU GLU ARG GLU ILE SER GLY GLY ALA MET ALA VAL
SEQRES 14 A 401 VAL ALA VAL LEU LEU ASN ASN LYS LEU TYR VAL ALA ASN
SEQRES 15 A 401 VAL GLY THR ASN ARG ALA LEU LEU CYS LYS SER THR VAL
SEQRES 16 A 401 ASP GLY LEU GLN VAL THR GLN LEU ASN VAL ASP HIS THR
SEQRES 17 A 401 THR GLU ASN GLU ASP GLU LEU PHE ARG LEU SER GLN LEU
SEQRES 18 A 401 GLY LEU ASP ALA GLY LYS ILE LYS GLN VAL GLY ILE ILE
SEQRES 19 A 401 CYS GLY GLN GLU SER THR ARG ARG ILE GLY ASP TYR LYS
SEQRES 20 A 401 VAL LYS TYR GLY TYR THR ASP ILE ASP LEU LEU SER ALA
SEQRES 21 A 401 ALA LYS SER LYS PRO ILE ILE ALA GLU PRO GLU ILE HIS
SEQRES 22 A 401 GLY ALA GLN PRO LEU ASP GLY VAL THR GLY PHE LEU VAL
SEQRES 23 A 401 LEU MET SER GLU GLY LEU TYR LYS ALA LEU GLU ALA ALA
SEQRES 24 A 401 HIS GLY PRO GLY GLN ALA ASN GLN GLU ILE ALA ALA MET
SEQRES 25 A 401 ILE ASP THR GLU PHE ALA LYS GLN THR SER LEU ASP ALA
SEQRES 26 A 401 VAL ALA GLN ALA VAL VAL ASP ARG VAL LYS ARG ILE HIS
SEQRES 27 A 401 SER ASP THR PHE ALA SER GLY GLY GLU ARG ALA ARG PHE
SEQRES 28 A 401 CYS PRO ARG HIS GLU ASP MET THR LEU LEU VAL ARG ASN
SEQRES 29 A 401 PHE GLY TYR PRO LEU GLY GLU MET SER GLN PRO THR PRO
SEQRES 30 A 401 SER PRO ALA PRO ALA ALA GLY GLY ARG VAL TYR PRO VAL
SEQRES 31 A 401 SER VAL PRO TYR SER SER ALA GLN SER THR SER
FORMUL 2 HOH *83(H2 O)
HELIX 1 1 ASN A 74 GLU A 87 1 14
HELIX 2 2 ALA A 98 GLN A 134 1 37
HELIX 3 3 PRO A 145 GLN A 147 5 3
HELIX 4 4 TYR A 148 SER A 163 1 16
HELIX 5 5 ASN A 211 GLN A 220 1 10
HELIX 6 6 ASP A 224 GLY A 232 1 9
HELIX 7 7 ASP A 245 GLY A 251 1 7
HELIX 8 8 TYR A 252 ILE A 255 5 4
HELIX 9 9 SER A 289 GLY A 301 1 13
HELIX 10 10 GLN A 304 GLN A 320 1 17
HELIX 11 11 SER A 322 SER A 344 1 23
HELIX 12 12 GLU A 347 CYS A 352 5 6
SHEET 1 AA 5 SER A 27 ALA A 32 0
SHEET 2 AA 5 MET A 358 ASN A 364 -1 O MET A 358 N ALA A 32
SHEET 3 AA 5 GLY A 283 MET A 288 -1 O LEU A 285 N ARG A 363
SHEET 4 AA 5 ARG A 187 SER A 193 -1 O ARG A 187 N MET A 288
SHEET 5 AA 5 LEU A 198 GLN A 202 -1 O GLN A 199 N LYS A 192
SHEET 1 AB 3 THR A 44 GLU A 45 0
SHEET 2 AB 3 ARG A 35 TYR A 37 -1 O SER A 36 N GLU A 45
SHEET 3 AB 3 ARG A 354 HIS A 355 -1 O HIS A 355 N ARG A 35
SHEET 1 AC 4 ASP A 51 SER A 58 0
SHEET 2 AC 4 CYS A 62 TYR A 71 -1 O CYS A 62 N SER A 58
SHEET 3 AC 4 GLY A 165 LEU A 174 -1 O GLY A 165 N TYR A 71
SHEET 4 AC 4 ILE A 243 GLY A 244 -1 O ILE A 243 N ALA A 166
SHEET 1 AD 5 ASP A 51 SER A 58 0
SHEET 2 AD 5 CYS A 62 TYR A 71 -1 O CYS A 62 N SER A 58
SHEET 3 AD 5 GLY A 165 LEU A 174 -1 O GLY A 165 N TYR A 71
SHEET 4 AD 5 LYS A 177 VAL A 183 -1 O LYS A 177 N LEU A 174
SHEET 5 AD 5 GLU A 271 PRO A 277 -1 O GLU A 271 N ASN A 182
CRYST1 141.961 141.961 65.905 90.00 90.00 120.00 P 3 2 1 6
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 0.007044 0.004067 0.000000 0.00000
SCALE2 0.000000 0.008134 0.000000 0.00000
SCALE3 0.000000 0.000000 0.015173 0.00000
(ATOM LINES ARE NOT SHOWN.)
END