HEADER PHOSPHOTRANSFERASE 25-AUG-95 1CKJ
TITLE CASEIN KINASE I DELTA TRUNCATION MUTANT CONTAINING RESIDUES
TITLE 2 1-317 COMPLEX WITH BOUND TUNGSTATE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: RECOMBINANT CASEIN KINASE I DELTA;
COMPND 3 CHAIN: A, B;
COMPND 4 EC: 2.7.1.-;
COMPND 5 ENGINEERED: YES;
COMPND 6 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: RATTUS NORVEGICUS;
SOURCE 3 ORGANISM_COMMON: NORWAY RAT;
SOURCE 4 ORGANISM_TAXID: 10116;
SOURCE 5 CELL_LINE: 293;
SOURCE 6 ORGAN: TESTES;
SOURCE 7 GENE: T7;
SOURCE 8 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 9 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 10 EXPRESSION_SYSTEM_STRAIN: 293;
SOURCE 11 EXPRESSION_SYSTEM_VECTOR_TYPE: T7;
SOURCE 12 EXPRESSION_SYSTEM_PLASMID: PET-8C;
SOURCE 13 EXPRESSION_SYSTEM_GENE: T7;
SOURCE 14 OTHER_DETAILS: HOST BL21(DE3)
KEYWDS PROTEIN KINASE, PHOSPHOTRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR K.L.LONGENECKER,P.J.ROACH,T.D.HURLEY
REVDAT 2 24-FEB-09 1CKJ 1 VERSN
REVDAT 1 07-DEC-95 1CKJ 0
JRNL AUTH K.L.LONGENECKER,P.J.ROACH,T.D.HURLEY
JRNL TITL THREE-DIMENSIONAL STRUCTURE OF MAMMALIAN CASEIN
JRNL TITL 2 KINASE I: MOLECULAR BASIS FOR PHOSPHATE
JRNL TITL 3 RECOGNITION.
JRNL REF J.MOL.BIOL. V. 257 618 1996
JRNL REFN ISSN 0022-2836
JRNL PMID 8648628
JRNL DOI 10.1006/JMBI.1996.0189
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH R.XU,G.CARMEL,R.M.SWEET,J.KURET,X.CHENG
REMARK 1 TITL CRYSTAL STRUCTURE OF CASEIN KINASE-1, A
REMARK 1 TITL 2 PHOSPHATE-DIRECTED PROTEIN KINASE
REMARK 1 REF EMBO J. V. 14 1015 1995
REMARK 1 REFN ISSN 0261-4189
REMARK 1 REFERENCE 2
REMARK 1 AUTH P.R.GRAVES,D.W.HAAS,C.H.HAGEDORN,A.A.DEPAOLI-ROACH,
REMARK 1 AUTH 2 P.J.ROACH
REMARK 1 TITL MOLECULAR CLONING, EXPRESSION, AND
REMARK 1 TITL 2 CHARACTERIZATION OF A 49-KILODALTON CASEIN KINASE
REMARK 1 TITL 3 I ISOFORM FROM RAT TESTIS
REMARK 1 REF J.BIOL.CHEM. V. 268 6394 1993
REMARK 1 REFN ISSN 0021-9258
REMARK 2
REMARK 2 RESOLUTION. 2.46 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR 3.1
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.46
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 8.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 1.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 85.0
REMARK 3 NUMBER OF REFLECTIONS : 22955
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : NULL
REMARK 3 FREE R VALUE TEST SET SELECTION : NULL
REMARK 3 R VALUE (WORKING SET) : 0.192
REMARK 3 FREE R VALUE : 0.271
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 7.000
REMARK 3 FREE R VALUE TEST SET COUNT : NULL
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 : 4816
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 25
REMARK 3 SOLVENT ATOMS : 32
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 38.10
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) : 0.25
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) : 0.007
REMARK 3 BOND ANGLES (DEGREES) : 1.53
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 21.55
REMARK 3 IMPROPER ANGLES (DEGREES) : 1.12
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 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 1CKJ COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 01-AUG-94
REMARK 200 TEMPERATURE (KELVIN) : NULL
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : NULL
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : NULL
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : RIGAKU RAXIS II
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : R-AXIS
REMARK 200 DATA SCALING SOFTWARE : NULL
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 23846
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.460
REMARK 200 RESOLUTION RANGE LOW (A) : 53.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 85.0
REMARK 200 DATA REDUNDANCY : 2.900
REMARK 200 R MERGE (I) : 0.06600
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) : NULL
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
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: NULL
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL
REMARK 200 SOFTWARE USED: X-PLOR 3.1
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 51.25
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.52
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: MOLECULE: RECOMBINANT CASEIN
REMARK 280 KINASE I DELTA. CRYSTALS WERE GROWN BY THE SITTING DROP
REMARK 280 TECHNIQUE, MIXING 3 MICROLITER OF PROTEIN SOLUTION WITH 3
REMARK 280 MICROLITER OF RESERVOIR SOLUTION. THE PROTEIN SOLUTION
REMARK 280 CONSISTED OF 14 MG/ML PROTEIN IN 50 MM TRIS-HCL (PH=7.5), 1 MM
REMARK 280 EDTA, 5 MM DTT, 0.2 M NACL, 2.5 MM BETA-OCTYL GLUCOSIDE. THE
REMARK 280 RESERVOIR SOLUTION CONTAINED 15% PEG 3400, 50 MM SODIUM
REMARK 280 CITRATE, 50 MM DIBASIC POTASSIUM PHOSPHATE, (PH=6.8). DATA WAS
REMARK 280 COLLECTED ON A CRYSTAL SOAKED FOR 6 DAYS IN 15% PEG 3400, 50
REMARK 280 MM SODIUM CITRATE, 17.5 MM SODIUM TUNGSTATE, (PH=6.8). ROOM
REMARK 280 TEMPERATURE.
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
REMARK 290 4555 X+1/2,-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 53.37000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 30.30000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 57.73500
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 30.30000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 53.37000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 57.73500
REMARK 290 SMTRY3 4 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 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 ALA A 302
REMARK 465 SER A 303
REMARK 465 ARG A 304
REMARK 465 ALA A 305
REMARK 465 ALA A 306
REMARK 465 ASP A 307
REMARK 465 ASP A 308
REMARK 465 ALA A 309
REMARK 465 GLU A 310
REMARK 465 ARG A 311
REMARK 465 GLU A 312
REMARK 465 ARG A 313
REMARK 465 ARG A 314
REMARK 465 ASP A 315
REMARK 465 ARG A 316
REMARK 465 GLU A 317
REMARK 465 GLU A 318
REMARK 465 ARG A 319
REMARK 465 LEU A 320
REMARK 465 ARG A 321
REMARK 465 HIS A 322
REMARK 465 LYS B 299
REMARK 465 PHE B 300
REMARK 465 GLY B 301
REMARK 465 ALA B 302
REMARK 465 SER B 303
REMARK 465 ARG B 304
REMARK 465 ALA B 305
REMARK 465 ALA B 306
REMARK 465 ASP B 307
REMARK 465 ASP B 308
REMARK 465 ALA B 309
REMARK 465 GLU B 310
REMARK 465 ARG B 311
REMARK 465 GLU B 312
REMARK 465 ARG B 313
REMARK 465 ARG B 314
REMARK 465 ASP B 315
REMARK 465 ARG B 316
REMARK 465 GLU B 317
REMARK 465 GLU B 318
REMARK 465 ARG B 319
REMARK 465 LEU B 320
REMARK 465 ARG B 321
REMARK 465 HIS B 322
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 ASN A 10 -51.64 -167.17
REMARK 500 ALA A 34 -9.65 -149.30
REMARK 500 CYS A 44 102.91 -59.78
REMARK 500 VAL A 45 -72.19 -12.77
REMARK 500 THR A 47 -75.33 -88.98
REMARK 500 LYS A 48 -42.72 -168.93
REMARK 500 PRO A 50 76.96 -65.81
REMARK 500 ARG A 130 -5.40 72.86
REMARK 500 ASP A 154 86.60 71.65
REMARK 500 LYS A 222 83.62 50.41
REMARK 500 TYR A 291 44.24 -98.59
REMARK 500 ILE B 18 42.62 -98.34
REMARK 500 PHE B 23 31.16 -152.16
REMARK 500 LYS B 46 56.33 -90.95
REMARK 500 CYS B 99 43.35 -88.77
REMARK 500 SER B 100 28.21 45.55
REMARK 500 ASN B 126 32.96 74.54
REMARK 500 ASP B 131 46.80 -156.55
REMARK 500 ASP B 154 89.89 62.79
REMARK 500 SER B 251 -31.97 -36.08
REMARK 500 TYR B 291 48.88 -97.56
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE WO4 A 400
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE WO4 A 401
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE WO4 B 400
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE WO4 B 402
DBREF 1CKJ A 1 322 UNP Q06486 KC1D_RAT 1 317
DBREF 1CKJ B 1 322 UNP Q06486 KC1D_RAT 1 317
SEQRES 1 A 317 MET GLU LEU ARG VAL GLY ASN ARG TYR ARG LEU GLY ARG
SEQRES 2 A 317 LYS ILE GLY SER GLY SER PHE GLY ASP ILE TYR LEU GLY
SEQRES 3 A 317 THR ASP ILE ALA ALA GLY GLU GLU VAL ALA ILE LYS LEU
SEQRES 4 A 317 GLU CYS VAL LYS THR LYS HIS PRO GLN LEU HIS ILE GLU
SEQRES 5 A 317 SER LYS ILE TYR LYS MET MET GLN GLY GLY VAL GLY ILE
SEQRES 6 A 317 PRO THR ILE ARG TRP CYS GLY ALA GLU GLY ASP TYR ASN
SEQRES 7 A 317 VAL MET VAL MET GLU LEU LEU GLY PRO SER LEU GLU ASP
SEQRES 8 A 317 LEU PHE ASN PHE CYS SER ARG LYS PHE SER LEU LYS THR
SEQRES 9 A 317 VAL LEU LEU LEU ALA ASP GLN MET ILE SER ARG ILE GLU
SEQRES 10 A 317 TYR ILE HIS SER LYS ASN PHE ILE HIS ARG ASP VAL LYS
SEQRES 11 A 317 PRO ASP ASN PHE LEU MET GLY LEU GLY LYS LYS GLY ASN
SEQRES 12 A 317 LEU VAL TYR ILE ILE ASP PHE GLY LEU ALA LYS LYS TYR
SEQRES 13 A 317 ARG ASP ALA ARG THR HIS GLN HIS ILE PRO TYR ARG GLU
SEQRES 14 A 317 ASN LYS ASN LEU THR GLY THR ALA ARG TYR ALA SER ILE
SEQRES 15 A 317 ASN THR HIS LEU GLY ILE GLU GLN SER ARG ARG ASP ASP
SEQRES 16 A 317 LEU GLU SER LEU GLY TYR VAL LEU MET TYR PHE ASN LEU
SEQRES 17 A 317 GLY SER LEU PRO TRP GLN GLY LEU LYS ALA ALA THR LYS
SEQRES 18 A 317 ARG GLN LYS TYR GLU ARG ILE SER GLU LYS LYS MET SER
SEQRES 19 A 317 THR PRO ILE GLU VAL LEU CYS LYS GLY TYR PRO SER GLU
SEQRES 20 A 317 PHE ALA THR TYR LEU ASN PHE CYS ARG SER LEU ARG PHE
SEQRES 21 A 317 ASP ASP LYS PRO ASP TYR SER TYR LEU ARG GLN LEU PHE
SEQRES 22 A 317 ARG ASN LEU PHE HIS ARG GLN GLY PHE SER TYR ASP TYR
SEQRES 23 A 317 VAL PHE ASP TRP ASN MET LEU LYS PHE GLY ALA SER ARG
SEQRES 24 A 317 ALA ALA ASP ASP ALA GLU ARG GLU ARG ARG ASP ARG GLU
SEQRES 25 A 317 GLU ARG LEU ARG HIS
SEQRES 1 B 317 MET GLU LEU ARG VAL GLY ASN ARG TYR ARG LEU GLY ARG
SEQRES 2 B 317 LYS ILE GLY SER GLY SER PHE GLY ASP ILE TYR LEU GLY
SEQRES 3 B 317 THR ASP ILE ALA ALA GLY GLU GLU VAL ALA ILE LYS LEU
SEQRES 4 B 317 GLU CYS VAL LYS THR LYS HIS PRO GLN LEU HIS ILE GLU
SEQRES 5 B 317 SER LYS ILE TYR LYS MET MET GLN GLY GLY VAL GLY ILE
SEQRES 6 B 317 PRO THR ILE ARG TRP CYS GLY ALA GLU GLY ASP TYR ASN
SEQRES 7 B 317 VAL MET VAL MET GLU LEU LEU GLY PRO SER LEU GLU ASP
SEQRES 8 B 317 LEU PHE ASN PHE CYS SER ARG LYS PHE SER LEU LYS THR
SEQRES 9 B 317 VAL LEU LEU LEU ALA ASP GLN MET ILE SER ARG ILE GLU
SEQRES 10 B 317 TYR ILE HIS SER LYS ASN PHE ILE HIS ARG ASP VAL LYS
SEQRES 11 B 317 PRO ASP ASN PHE LEU MET GLY LEU GLY LYS LYS GLY ASN
SEQRES 12 B 317 LEU VAL TYR ILE ILE ASP PHE GLY LEU ALA LYS LYS TYR
SEQRES 13 B 317 ARG ASP ALA ARG THR HIS GLN HIS ILE PRO TYR ARG GLU
SEQRES 14 B 317 ASN LYS ASN LEU THR GLY THR ALA ARG TYR ALA SER ILE
SEQRES 15 B 317 ASN THR HIS LEU GLY ILE GLU GLN SER ARG ARG ASP ASP
SEQRES 16 B 317 LEU GLU SER LEU GLY TYR VAL LEU MET TYR PHE ASN LEU
SEQRES 17 B 317 GLY SER LEU PRO TRP GLN GLY LEU LYS ALA ALA THR LYS
SEQRES 18 B 317 ARG GLN LYS TYR GLU ARG ILE SER GLU LYS LYS MET SER
SEQRES 19 B 317 THR PRO ILE GLU VAL LEU CYS LYS GLY TYR PRO SER GLU
SEQRES 20 B 317 PHE ALA THR TYR LEU ASN PHE CYS ARG SER LEU ARG PHE
SEQRES 21 B 317 ASP ASP LYS PRO ASP TYR SER TYR LEU ARG GLN LEU PHE
SEQRES 22 B 317 ARG ASN LEU PHE HIS ARG GLN GLY PHE SER TYR ASP TYR
SEQRES 23 B 317 VAL PHE ASP TRP ASN MET LEU LYS PHE GLY ALA SER ARG
SEQRES 24 B 317 ALA ALA ASP ASP ALA GLU ARG GLU ARG ARG ASP ARG GLU
SEQRES 25 B 317 GLU ARG LEU ARG HIS
HET WO4 A 400 5
HET WO4 A 401 5
HET WO4 B 400 5
HET WO4 B 401 5
HET WO4 B 402 5
HETNAM WO4 TUNGSTATE(VI)ION
FORMUL 3 WO4 5(O4 W 2-)
FORMUL 8 HOH *32(H2 O)
HELIX 1 1 GLN A 51 MET A 62 5 12
HELIX 2 2 LEU A 92 PHE A 98 1 7
HELIX 3 3 LEU A 105 LYS A 125 1 21
HELIX 4 4 PRO A 134 ASN A 136 5 3
HELIX 5 5 GLY A 144 LYS A 146 5 3
HELIX 6 6 ILE A 187 LEU A 191 1 5
HELIX 7 7 ARG A 197 LEU A 213 1 17
HELIX 8 8 TYR A 230 SER A 239 1 10
HELIX 9 9 ILE A 242 LEU A 245 1 4
HELIX 10 10 GLU A 252 SER A 262 1 11
HELIX 11 11 TYR A 271 ARG A 284 1 14
HELIX 12 12 ASP A 294 PHE A 300 1 7
HELIX 13 13 VAL B 8 ASN B 10 5 3
HELIX 14 14 LEU B 52 MET B 61 1 10
HELIX 15 15 ASP B 94 PHE B 98 1 5
HELIX 16 16 LEU B 105 LYS B 125 1 21
HELIX 17 17 PRO B 134 ASN B 136 5 3
HELIX 18 18 GLY B 144 LYS B 146 5 3
HELIX 19 19 ILE B 187 HIS B 190 1 4
HELIX 20 20 ARG B 197 LEU B 213 1 17
HELIX 21 21 LYS B 226 SER B 239 1 14
HELIX 22 22 ILE B 242 LEU B 245 1 4
HELIX 23 23 GLU B 252 SER B 262 1 11
HELIX 24 24 TYR B 271 ARG B 284 1 14
HELIX 25 25 ASP B 294 ASN B 296 5 3
SHEET 1 A 5 TYR A 12 LEU A 14 0
SHEET 2 A 5 ASP A 25 ASP A 31 -1 N THR A 30 O ARG A 13
SHEET 3 A 5 GLU A 36 CYS A 44 -1 N LEU A 42 O ASP A 25
SHEET 4 A 5 TYR A 80 GLU A 86 -1 N MET A 85 O ALA A 39
SHEET 5 A 5 ILE A 71 GLU A 77 -1 N GLU A 77 O TYR A 80
SHEET 1 B 2 PHE A 137 MET A 139 0
SHEET 2 B 2 VAL A 150 ILE A 152 -1 N TYR A 151 O LEU A 138
SHEET 1 C 5 TYR B 12 LEU B 14 0
SHEET 2 C 5 ASP B 25 ASP B 31 -1 N THR B 30 O ARG B 13
SHEET 3 C 5 GLU B 37 CYS B 44 -1 N LEU B 42 O ASP B 25
SHEET 4 C 5 TYR B 80 GLU B 86 -1 N MET B 85 O ALA B 39
SHEET 5 C 5 ILE B 71 ALA B 76 -1 N GLY B 75 O VAL B 82
SHEET 1 D 2 PHE B 137 MET B 139 0
SHEET 2 D 2 VAL B 150 ILE B 152 -1 N TYR B 151 O LEU B 138
SHEET 1 E 2 LYS A 17 GLY A 21 0
SHEET 2 E 2 GLY A 24 TYR A 27 -1 N ILE A 26 O ILE A 18
SITE 1 AC1 3 ARG A 183 GLY A 220 LYS A 229
SITE 1 AC2 3 HIS A 167 LYS A 268 HOH A 419
SITE 1 AC3 4 ARG B 183 GLN B 219 GLY B 220 LYS B 229
SITE 1 AC4 2 ARG B 130 LYS B 159
CRYST1 106.740 115.470 60.600 90.00 90.00 90.00 P 21 21 21 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 0.009369 0.000000 0.000000 0.00000
SCALE2 0.000000 0.008660 0.000000 0.00000
SCALE3 0.000000 0.000000 0.016502 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
