HEADER TRANSFERASE 23-AUG-03 1UKH
TITLE STRUCTURAL BASIS FOR THE SELECTIVE INHIBITION OF JNK1 BY THE
TITLE 2 SCAFFOLDING PROTEIN JIP1 AND SP600125
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: MITOGEN-ACTIVATED PROTEIN KINASE 8 ISOFORM 4;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: RESIDUES 1-369;
COMPND 5 SYNONYM: JNK1;
COMPND 6 EC: 2.7.1.37;
COMPND 7 ENGINEERED: YES;
COMPND 8 MOL_ID: 2;
COMPND 9 MOLECULE: 11-MER PEPTIDE FROM C-JUN-AMINO-TERMINAL KINASE INTERACTING
COMPND 10 PROTEIN 1;
COMPND 11 CHAIN: B;
COMPND 12 SYNONYM: JIP1;
COMPND 13 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: PET21B;
SOURCE 9 MOL_ID: 2;
SOURCE 10 SYNTHETIC: YES;
SOURCE 11 OTHER_DETAILS: THIS SEQUENCE OCCURS PEPTIDE SYNTHESIS
KEYWDS TRANSFERASE, PHOSPHORYLATION
EXPDTA X-RAY DIFFRACTION
AUTHOR Y.-S.HEO,Y.K.KIM,B.-J.SUNG,H.S.LEE,J.I.LEE,C.I.SEO,S.-Y.PARK,J.H.KIM,
AUTHOR 2 Y.-L.HYUN,Y.H.JEON,S.RO,T.G.LEE,J.M.CHO,K.Y.HWANG,C.-H.YANG
REVDAT 4 27-DEC-23 1UKH 1 SEQADV
REVDAT 3 24-FEB-09 1UKH 1 VERSN
REVDAT 2 26-APR-05 1UKH 1 SEQADV SEQRES
REVDAT 1 30-AUG-04 1UKH 0
JRNL AUTH Y.-S.HEO,S.K.KIM,C.I.SEO,Y.K.KIM,B.-J.SUNG,H.S.LEE,J.I.LEE,
JRNL AUTH 2 S.-Y.PARK,J.H.KIM,K.Y.HWANG,Y.-L.HYUN,Y.H.JEON,S.RO,J.M.CHO,
JRNL AUTH 3 T.G.LEE,C.-H.YANG
JRNL TITL STRUCTURAL BASIS FOR THE SELECTIVE INHIBITION OF JNK1 BY THE
JRNL TITL 2 SCAFFOLDING PROTEIN JIP1 AND SP600125
JRNL REF EMBO J. V. 23 2185 2004
JRNL REFN ISSN 0261-4189
JRNL PMID 15141161
JRNL DOI 10.1038/SJ.EMBOJ.7600212
REMARK 2
REMARK 2 RESOLUTION. 2.35 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) : 2.35
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 19.82
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 479481.890
REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0000
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 NUMBER OF REFLECTIONS : 16729
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) : 0.226
REMARK 3 FREE R VALUE : 0.245
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.900
REMARK 3 FREE R VALUE TEST SET COUNT : 818
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.008
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) : 2.35
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.50
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 77.70
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 2203
REMARK 3 BIN R VALUE (WORKING SET) : 0.3760
REMARK 3 BIN FREE R VALUE : 0.3870
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 4.80
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 111
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.037
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2672
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 95
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 28.10
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 61.30
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 6.77000
REMARK 3 B22 (A**2) : 0.89000
REMARK 3 B33 (A**2) : -7.66000
REMARK 3 B12 (A**2) : 0.00000
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) : 0.38
REMARK 3 ESD FROM SIGMAA (A) : 0.75
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) : 0.39
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.49
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.008
REMARK 3 BOND ANGLES (DEGREES) : 1.200
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 22.80
REMARK 3 IMPROPER ANGLES (DEGREES) : 0.850
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : OVERALL
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 : 0.34
REMARK 3 BSOL : 59.77
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 4 : ION.PARAM
REMARK 3 PARAMETER FILE 5 : NULL
REMARK 3 TOPOLOGY FILE 1 : PROTEIN.TOP
REMARK 3 TOPOLOGY FILE 2 : 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 1UKH COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 27-AUG-03.
REMARK 100 THE DEPOSITION ID IS D_1000005927.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 11-MAR-03
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 5.5
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) : 1.0
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 : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 16980
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.350
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 (%) : 91.9
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) : 2.35
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.43
REMARK 200 COMPLETENESS FOR SHELL (%) : 72.6
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 (%): 54.51
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.73
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 20% PEG3000, 0.1M SODIUM CITRATE, PH
REMARK 280 5.5, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 277K
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 31.19900
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 41.87100
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 40.42050
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 41.87100
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 31.19900
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 40.42050
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 1130 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 16360 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -7.0 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 MET A 1
REMARK 465 SER A 2
REMARK 465 ARG A 3
REMARK 465 SER A 4
REMARK 465 LYS A 5
REMARK 465 ARG A 6
REMARK 465 ASP A 7
REMARK 465 ASN A 8
REMARK 465 ALA A 173
REMARK 465 ARG A 174
REMARK 465 THR A 175
REMARK 465 ALA A 176
REMARK 465 GLY A 177
REMARK 465 THR A 178
REMARK 465 SER A 179
REMARK 465 PHE A 180
REMARK 465 MET A 181
REMARK 465 MET A 182
REMARK 465 THR A 183
REMARK 465 PRO A 184
REMARK 465 TYR A 185
REMARK 465 VAL A 186
REMARK 465 VAL A 187
REMARK 465 THR A 188
REMARK 465 ARG A 189
REMARK 465 ALA A 282
REMARK 465 ASP A 283
REMARK 465 SER A 284
REMARK 465 GLU A 285
REMARK 465 HIS A 286
REMARK 465 ILE A 337
REMARK 465 PRO A 338
REMARK 465 ASP A 339
REMARK 465 LYS A 340
REMARK 465 GLN A 341
REMARK 465 LEU A 342
REMARK 465 ASP A 343
REMARK 465 GLU A 344
REMARK 465 ARG A 345
REMARK 465 GLU A 346
REMARK 465 HIS A 347
REMARK 465 THR A 348
REMARK 465 HIS A 364
REMARK 465 HIS A 365
REMARK 465 HIS A 366
REMARK 465 HIS A 367
REMARK 465 HIS A 368
REMARK 465 HIS A 369
REMARK 465 ARG B 153
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 34 88.02 178.63
REMARK 500 ASN A 63 138.06 175.92
REMARK 500 ASN A 84 31.94 -94.87
REMARK 500 ASN A 90 156.10 175.21
REMARK 500 GLN A 102 -35.03 -140.59
REMARK 500 ARG A 150 -11.73 74.83
REMARK 500 VAL A 278 0.87 -65.39
REMARK 500 GLU A 329 -62.33 -96.20
REMARK 500 PRO A 334 167.01 -45.30
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1UKI RELATED DB: PDB
REMARK 900 THE SAME PROTEIN COMPLEXED WITH SP6
DBREF 1UKH A 1 363 UNP P45983 MK08_HUMAN 1 363
DBREF 1UKH B 153 163 UNP Q9WVI9 JIP1_MOUSE 153 163
SEQADV 1UKH HIS A 364 UNP P45983 EXPRESSION TAG
SEQADV 1UKH HIS A 365 UNP P45983 EXPRESSION TAG
SEQADV 1UKH HIS A 366 UNP P45983 EXPRESSION TAG
SEQADV 1UKH HIS A 367 UNP P45983 EXPRESSION TAG
SEQADV 1UKH HIS A 368 UNP P45983 EXPRESSION TAG
SEQADV 1UKH HIS A 369 UNP P45983 EXPRESSION TAG
SEQRES 1 A 369 MET SER ARG SER LYS ARG ASP ASN ASN PHE TYR SER VAL
SEQRES 2 A 369 GLU ILE GLY ASP SER THR PHE THR VAL LEU LYS ARG TYR
SEQRES 3 A 369 GLN ASN LEU LYS PRO ILE GLY SER GLY ALA GLN GLY ILE
SEQRES 4 A 369 VAL CYS ALA ALA TYR ASP ALA ILE LEU GLU ARG ASN VAL
SEQRES 5 A 369 ALA ILE LYS LYS LEU SER ARG PRO PHE GLN ASN GLN THR
SEQRES 6 A 369 HIS ALA LYS ARG ALA TYR ARG GLU LEU VAL LEU MET LYS
SEQRES 7 A 369 CYS VAL ASN HIS LYS ASN ILE ILE GLY LEU LEU ASN VAL
SEQRES 8 A 369 PHE THR PRO GLN LYS SER LEU GLU GLU PHE GLN ASP VAL
SEQRES 9 A 369 TYR ILE VAL MET GLU LEU MET ASP ALA ASN LEU CYS GLN
SEQRES 10 A 369 VAL ILE GLN MET GLU LEU ASP HIS GLU ARG MET SER TYR
SEQRES 11 A 369 LEU LEU TYR GLN MET LEU CYS GLY ILE LYS HIS LEU HIS
SEQRES 12 A 369 SER ALA GLY ILE ILE HIS ARG ASP LEU LYS PRO SER ASN
SEQRES 13 A 369 ILE VAL VAL LYS SER ASP CYS THR LEU LYS ILE LEU ASP
SEQRES 14 A 369 PHE GLY LEU ALA ARG THR ALA GLY THR SER PHE MET MET
SEQRES 15 A 369 THR PRO TYR VAL VAL THR ARG TYR TYR ARG ALA PRO GLU
SEQRES 16 A 369 VAL ILE LEU GLY MET GLY TYR LYS GLU ASN VAL ASP ILE
SEQRES 17 A 369 TRP SER VAL GLY CYS ILE MET GLY GLU MET ILE LYS GLY
SEQRES 18 A 369 GLY VAL LEU PHE PRO GLY THR ASP HIS ILE ASP GLN TRP
SEQRES 19 A 369 ASN LYS VAL ILE GLU GLN LEU GLY THR PRO CYS PRO GLU
SEQRES 20 A 369 PHE MET LYS LYS LEU GLN PRO THR VAL ARG THR TYR VAL
SEQRES 21 A 369 GLU ASN ARG PRO LYS TYR ALA GLY TYR SER PHE GLU LYS
SEQRES 22 A 369 LEU PHE PRO ASP VAL LEU PHE PRO ALA ASP SER GLU HIS
SEQRES 23 A 369 ASN LYS LEU LYS ALA SER GLN ALA ARG ASP LEU LEU SER
SEQRES 24 A 369 LYS MET LEU VAL ILE ASP ALA SER LYS ARG ILE SER VAL
SEQRES 25 A 369 ASP GLU ALA LEU GLN HIS PRO TYR ILE ASN VAL TRP TYR
SEQRES 26 A 369 ASP PRO SER GLU ALA GLU ALA PRO PRO PRO LYS ILE PRO
SEQRES 27 A 369 ASP LYS GLN LEU ASP GLU ARG GLU HIS THR ILE GLU GLU
SEQRES 28 A 369 TRP LYS GLU LEU ILE TYR LYS GLU VAL MET ASP LEU HIS
SEQRES 29 A 369 HIS HIS HIS HIS HIS
SEQRES 1 B 11 ARG PRO LYS ARG PRO THR THR LEU ASN LEU PHE
FORMUL 3 HOH *95(H2 O)
HELIX 1 1 ASN A 63 VAL A 80 1 18
HELIX 2 2 LEU A 115 ILE A 119 1 5
HELIX 3 3 ASP A 124 SER A 144 1 21
HELIX 4 4 ALA A 193 LEU A 198 1 6
HELIX 5 5 ASN A 205 GLY A 221 1 17
HELIX 6 6 ASP A 229 GLY A 242 1 14
HELIX 7 7 CYS A 245 LYS A 251 1 7
HELIX 8 8 GLN A 253 GLU A 261 1 9
HELIX 9 9 SER A 270 PHE A 275 1 6
HELIX 10 10 PRO A 276 PHE A 280 5 5
HELIX 11 11 ASN A 287 LEU A 302 1 16
HELIX 12 12 ASP A 305 ARG A 309 5 5
HELIX 13 13 SER A 311 HIS A 318 1 8
HELIX 14 14 ILE A 321 TYR A 325 5 5
HELIX 15 15 ASP A 326 GLU A 331 1 6
HELIX 16 16 GLU A 350 ASP A 362 1 13
SHEET 1 A 2 PHE A 10 ILE A 15 0
SHEET 2 A 2 SER A 18 LEU A 23 -1 O PHE A 20 N VAL A 13
SHEET 1 B 5 TYR A 26 SER A 34 0
SHEET 2 B 5 GLY A 38 ASP A 45 -1 O ALA A 42 N LYS A 30
SHEET 3 B 5 ARG A 50 LEU A 57 -1 O ILE A 54 N CYS A 41
SHEET 4 B 5 TYR A 105 GLU A 109 -1 O ILE A 106 N LYS A 55
SHEET 5 B 5 LEU A 88 PHE A 92 -1 N ASN A 90 O VAL A 107
SHEET 1 C 3 ALA A 113 ASN A 114 0
SHEET 2 C 3 ILE A 157 VAL A 159 -1 O VAL A 159 N ALA A 113
SHEET 3 C 3 LEU A 165 ILE A 167 -1 O LYS A 166 N VAL A 158
CRYST1 62.398 80.841 83.742 90.00 90.00 90.00 P 21 21 21 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 0.016026 0.000000 0.000000 0.00000
SCALE2 0.000000 0.012370 0.000000 0.00000
SCALE3 0.000000 0.000000 0.011941 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
