HEADER TRANSFERASE 18-FEB-05 1YWR
TITLE CRYSTAL STRUCTURE ANALYSIS OF INACTIVE P38 KINASE DOMAIN IN COMPLEX
TITLE 2 WITH A MONOCYCLIC PYRAZOLONE INHIBITOR
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: MITOGEN-ACTIVATED PROTEIN KINASE 14;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: MITOGEN-ACTIVATED PROTEIN KINASE P38ALPHA, MAP KINASE
COMPND 5 P38ALPHA, CRK1;
COMPND 6 EC: 2.7.1.37;
COMPND 7 ENGINEERED: YES;
COMPND 8 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MUS MUSCULUS;
SOURCE 3 ORGANISM_COMMON: HOUSE MOUSE;
SOURCE 4 ORGANISM_TAXID: 10090;
SOURCE 5 GENE: MAPK14, CRK1, CSBP1, CSBP2;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS P38 KINASE, MONCYCLIC PYRAZOLONE, TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR A.GOLEBIOWSKI,J.A.TOWNES,M.J.LAUFERSWEILER,T.A.BRUGEL,M.P.CLARK,
AUTHOR 2 C.M.CLARK,J.F.DJUNG,S.K.LAUGHLIN,M.P.SABAT,R.G.BOOKLAND,J.C.VANRENS,
AUTHOR 3 B.DE,L.C.HSIEH,M.J.JANUSZ,R.L.WALTER,M.E.WEBSTER,M.J.MEKEL
REVDAT 5 14-FEB-24 1YWR 1 REMARK
REVDAT 4 20-OCT-21 1YWR 1 REMARK SEQADV
REVDAT 3 11-OCT-17 1YWR 1 REMARK
REVDAT 2 24-FEB-09 1YWR 1 VERSN
REVDAT 1 10-MAY-05 1YWR 0
JRNL AUTH A.GOLEBIOWSKI,J.A.TOWNES,M.J.LAUFERSWEILER,T.A.BRUGEL,
JRNL AUTH 2 M.P.CLARK,C.M.CLARK,J.F.DJUNG,S.K.LAUGHLIN,M.P.SABAT,
JRNL AUTH 3 R.G.BOOKLAND,J.C.VANRENS,B.DE,L.C.HSIEH,M.J.JANUSZ,
JRNL AUTH 4 R.L.WALTER,M.E.WEBSTER,M.J.MEKEL
JRNL TITL THE DEVELOPMENT OF MONOCYCLIC PYRAZOLONE BASED CYTOKINE
JRNL TITL 2 SYNTHESIS INHIBITORS.
JRNL REF BIOORG.MED.CHEM.LETT. V. 15 2285 2005
JRNL REFN ISSN 0960-894X
JRNL PMID 15837310
JRNL DOI 10.1016/J.BMCL.2005.03.007
REMARK 2
REMARK 2 RESOLUTION. 1.95 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : SHELXL-97
REMARK 3 AUTHORS : G.M.SHELDRICK
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.95
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 50.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 1.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.7
REMARK 3 CROSS-VALIDATION METHOD : FREE R
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (NO CUTOFF).
REMARK 3 R VALUE (WORKING + TEST SET, NO CUTOFF) : 0.221
REMARK 3 R VALUE (WORKING SET, NO CUTOFF) : NULL
REMARK 3 FREE R VALUE (NO CUTOFF) : NULL
REMARK 3 FREE R VALUE TEST SET SIZE (%, NO CUTOFF) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT (NO CUTOFF) : NULL
REMARK 3 TOTAL NUMBER OF REFLECTIONS (NO CUTOFF) : 28007
REMARK 3
REMARK 3 FIT/AGREEMENT OF MODEL FOR DATA WITH F>4SIG(F).
REMARK 3 R VALUE (WORKING + TEST SET, F>4SIG(F)) : 0.200
REMARK 3 R VALUE (WORKING SET, F>4SIG(F)) : NULL
REMARK 3 FREE R VALUE (F>4SIG(F)) : NULL
REMARK 3 FREE R VALUE TEST SET SIZE (%, F>4SIG(F)) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT (F>4SIG(F)) : NULL
REMARK 3 TOTAL NUMBER OF REFLECTIONS (F>4SIG(F)) : 21926
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2728
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 35
REMARK 3 SOLVENT ATOMS : 196
REMARK 3
REMARK 3 MODEL REFINEMENT.
REMARK 3 OCCUPANCY SUM OF NON-HYDROGEN ATOMS : 2959.0
REMARK 3 OCCUPANCY SUM OF HYDROGEN ATOMS : 0.00
REMARK 3 NUMBER OF DISCRETELY DISORDERED RESIDUES : 0
REMARK 3 NUMBER OF LEAST-SQUARES PARAMETERS : 11851
REMARK 3 NUMBER OF RESTRAINTS : 11507
REMARK 3
REMARK 3 RMS DEVIATIONS FROM RESTRAINT TARGET VALUES.
REMARK 3 BOND LENGTHS (A) : 0.006
REMARK 3 ANGLE DISTANCES (A) : 0.023
REMARK 3 SIMILAR DISTANCES (NO TARGET VALUES) (A) : 0.000
REMARK 3 DISTANCES FROM RESTRAINT PLANES (A) : 0.024
REMARK 3 ZERO CHIRAL VOLUMES (A**3) : 0.030
REMARK 3 NON-ZERO CHIRAL VOLUMES (A**3) : 0.037
REMARK 3 ANTI-BUMPING DISTANCE RESTRAINTS (A) : 0.007
REMARK 3 RIGID-BOND ADP COMPONENTS (A**2) : 0.000
REMARK 3 SIMILAR ADP COMPONENTS (A**2) : 0.096
REMARK 3 APPROXIMATELY ISOTROPIC ADPS (A**2) : 0.000
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED: NULL
REMARK 3
REMARK 3 STEREOCHEMISTRY TARGET VALUES : ENGH AND HUBER
REMARK 3 SPECIAL CASE: NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1YWR COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 14-MAR-05.
REMARK 100 THE DEPOSITION ID IS D_1000032009.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 23-JUN-03
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 22-ID
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.000
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 : MAR
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 30232
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.950
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.6
REMARK 200 DATA REDUNDANCY : 4.500
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.04000
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 28.6000
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: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
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 (%): 45.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.10
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 12-17% PEG 4000, 100MM MES (PH 6.0
REMARK 280 -7.0), PH 6.5, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 287K
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 32.86800
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 38.68850
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 37.28750
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 38.68850
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 32.86800
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 37.28750
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: 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 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 GLN A 3
REMARK 465 GLU A 4
REMARK 465 VAL A 117
REMARK 465 HIS A 174
REMARK 465 THR A 175
REMARK 465 ASP A 176
REMARK 465 ASP A 177
REMARK 465 GLU A 178
REMARK 465 MET A 179
REMARK 465 ALA A 180
REMARK 465 GLY A 181
REMARK 465 PHE A 182
REMARK 465 LEU A 353
REMARK 465 ASP A 354
REMARK 465 GLN A 355
REMARK 465 GLU A 356
REMARK 465 GLU A 357
REMARK 465 MET A 358
REMARK 465 GLU A 359
REMARK 465 SER A 360
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 VAL A 183 CG1 CG2
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 LEU A 74 CA - CB - CG ANGL. DEV. = 14.2 DEGREES
REMARK 500 TYR A 200 C - N - CA ANGL. DEV. = 17.2 DEGREES
REMARK 500 ARG A 296 CG - CD - NE ANGL. DEV. = 14.9 DEGREES
REMARK 500 ARG A 296 CD - NE - CZ ANGL. DEV. = 17.9 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 GLN A 11 149.70 -174.07
REMARK 500 SER A 56 -81.35 -66.13
REMARK 500 PHE A 99 116.74 -38.82
REMARK 500 ASN A 100 1.85 -154.09
REMARK 500 LEU A 122 -19.45 -48.32
REMARK 500 THR A 123 133.87 73.68
REMARK 500 ARG A 149 -15.96 83.18
REMARK 500 ASN A 196 112.84 -31.97
REMARK 500 PRO A 224 -100.93 -56.88
REMARK 500 ASP A 227 -177.13 -171.99
REMARK 500 SER A 254 -72.73 -39.37
REMARK 500 ILE A 275 -97.12 15.96
REMARK 500 LEU A 289 54.72 -92.68
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 LI9 A 361
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1YW2 RELATED DB: PDB
DBREF 1YWR A 1 360 UNP P47811 MK14_MOUSE 0 359
SEQADV 1YWR ALA A 180 UNP P47811 THR 179 ENGINEERED MUTATION
SEQADV 1YWR PHE A 182 UNP P47811 TYR 181 ENGINEERED MUTATION
SEQADV 1YWR THR A 263 UNP P47811 ALA 262 CONFLICT
SEQRES 1 A 360 MET SER GLN GLU ARG PRO THR PHE TYR ARG GLN GLU LEU
SEQRES 2 A 360 ASN LYS THR ILE TRP GLU VAL PRO GLU ARG TYR GLN ASN
SEQRES 3 A 360 LEU SER PRO VAL GLY SER GLY ALA TYR GLY SER VAL CYS
SEQRES 4 A 360 ALA ALA PHE ASP THR LYS THR GLY HIS ARG VAL ALA VAL
SEQRES 5 A 360 LYS LYS LEU SER ARG PRO PHE GLN SER ILE ILE HIS ALA
SEQRES 6 A 360 LYS ARG THR TYR ARG GLU LEU ARG LEU LEU LYS HIS MET
SEQRES 7 A 360 LYS HIS GLU ASN VAL ILE GLY LEU LEU ASP VAL PHE THR
SEQRES 8 A 360 PRO ALA ARG SER LEU GLU GLU PHE ASN ASP VAL TYR LEU
SEQRES 9 A 360 VAL THR HIS LEU MET GLY ALA ASP LEU ASN ASN ILE VAL
SEQRES 10 A 360 LYS CYS GLN LYS LEU THR ASP ASP HIS VAL GLN PHE LEU
SEQRES 11 A 360 ILE TYR GLN ILE LEU ARG GLY LEU LYS TYR ILE HIS SER
SEQRES 12 A 360 ALA ASP ILE ILE HIS ARG ASP LEU LYS PRO SER ASN LEU
SEQRES 13 A 360 ALA VAL ASN GLU ASP CYS GLU LEU LYS ILE LEU ASP PHE
SEQRES 14 A 360 GLY LEU ALA ARG HIS THR ASP ASP GLU MET ALA GLY PHE
SEQRES 15 A 360 VAL ALA THR ARG TRP TYR ARG ALA PRO GLU ILE MET LEU
SEQRES 16 A 360 ASN TRP MET HIS TYR ASN GLN THR VAL ASP ILE TRP SER
SEQRES 17 A 360 VAL GLY CYS ILE MET ALA GLU LEU LEU THR GLY ARG THR
SEQRES 18 A 360 LEU PHE PRO GLY THR ASP HIS ILE ASP GLN LEU LYS LEU
SEQRES 19 A 360 ILE LEU ARG LEU VAL GLY THR PRO GLY ALA GLU LEU LEU
SEQRES 20 A 360 LYS LYS ILE SER SER GLU SER ALA ARG ASN TYR ILE GLN
SEQRES 21 A 360 SER LEU THR GLN MET PRO LYS MET ASN PHE ALA ASN VAL
SEQRES 22 A 360 PHE ILE GLY ALA ASN PRO LEU ALA VAL ASP LEU LEU GLU
SEQRES 23 A 360 LYS MET LEU VAL LEU ASP SER ASP LYS ARG ILE THR ALA
SEQRES 24 A 360 ALA GLN ALA LEU ALA HIS ALA TYR PHE ALA GLN TYR HIS
SEQRES 25 A 360 ASP PRO ASP ASP GLU PRO VAL ALA ASP PRO TYR ASP GLN
SEQRES 26 A 360 SER PHE GLU SER ARG ASP LEU LEU ILE ASP GLU TRP LYS
SEQRES 27 A 360 SER LEU THR TYR ASP GLU VAL ILE SER PHE VAL PRO PRO
SEQRES 28 A 360 PRO LEU ASP GLN GLU GLU MET GLU SER
HET LI9 A 361 35
HETNAM LI9 4-(4-FLUOROPHENYL)-1-METHYL-5-(2-{[(1S)-1-
HETNAM 2 LI9 PHENYLETHYL]AMINO}PYRIMIDIN-4-YL)-2-PIPERIDIN-4-YL-1,
HETNAM 3 LI9 2-DIHYDRO-3H-PYRAZOL-3-ONE
FORMUL 2 LI9 C27 H29 F N6 O
FORMUL 3 HOH *196(H2 O)
HELIX 1 1 SER A 61 MET A 78 1 18
HELIX 2 2 THR A 123 ALA A 144 1 22
HELIX 3 3 LYS A 152 SER A 154 5 3
HELIX 4 4 ALA A 184 ARG A 189 5 6
HELIX 5 5 ALA A 190 LEU A 195 1 6
HELIX 6 6 THR A 203 GLY A 219 1 17
HELIX 7 7 ASP A 227 GLY A 240 1 14
HELIX 8 8 GLY A 243 LYS A 248 1 6
HELIX 9 9 SER A 252 LEU A 262 1 11
HELIX 10 10 ASN A 269 PHE A 274 1 6
HELIX 11 11 ASN A 278 LEU A 289 1 12
HELIX 12 12 THR A 298 LEU A 303 1 6
HELIX 13 13 ALA A 304 ALA A 309 5 6
HELIX 14 14 ASP A 313 GLU A 317 5 5
HELIX 15 15 GLN A 325 ARG A 330 5 6
HELIX 16 16 LEU A 333 SER A 347 1 15
SHEET 1 A 2 PHE A 8 LEU A 13 0
SHEET 2 A 2 THR A 16 PRO A 21 -1 O THR A 16 N LEU A 13
SHEET 1 B 5 TYR A 24 SER A 32 0
SHEET 2 B 5 GLY A 36 ASP A 43 -1 O PHE A 42 N GLN A 25
SHEET 3 B 5 ARG A 49 LEU A 55 -1 O VAL A 50 N ALA A 41
SHEET 4 B 5 TYR A 103 HIS A 107 -1 O LEU A 104 N LYS A 53
SHEET 5 B 5 ASP A 88 PHE A 90 -1 N ASP A 88 O VAL A 105
SHEET 1 C 3 ALA A 111 ASP A 112 0
SHEET 2 C 3 LEU A 156 VAL A 158 -1 O VAL A 158 N ALA A 111
SHEET 3 C 3 LEU A 164 ILE A 166 -1 O LYS A 165 N ALA A 157
SITE 1 AC1 13 VAL A 30 TYR A 35 ALA A 51 LYS A 53
SITE 2 AC1 13 LEU A 104 VAL A 105 THR A 106 HIS A 107
SITE 3 AC1 13 LEU A 108 MET A 109 ALA A 111 ASP A 112
SITE 4 AC1 13 ASP A 168
CRYST1 65.736 74.575 77.377 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 0.015212 0.000000 0.000000 0.00000
SCALE2 0.000000 0.013409 0.000000 0.00000
SCALE3 0.000000 0.000000 0.012924 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
