HEADER TRANSFERASE/TRANSFERASE INHIBITOR 14-APR-11 3RIN
TITLE P38 KINASE CRYSTAL STRUCTURE IN COMPLEX WITH SMALL MOLECULE INHIBITOR
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: MITOGEN-ACTIVATED PROTEIN KINASE 14;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: MITOGEN-ACTIVATED PROTEIN KINASE P38 ALPHA, MAP KINASE P38
COMPND 5 ALPHA, MAP KINASE 14, MAPK 14, CYTOKINE SUPPRESSIVE ANTI-INFLAMMATORY
COMPND 6 DRUG-BINDING PROTEIN, CSAID-BINDING PROTEIN, CSBP, MAP KINASE MXI2,
COMPND 7 MAX-INTERACTING PROTEIN 2, SAPK2A;
COMPND 8 EC: 2.7.11.24;
COMPND 9 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 STRAIN: DH10B-R;
SOURCE 6 GENE: CSBP, CSBP1, CSBP2, CSPB1, MAPK14, MXI2;
SOURCE 7 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: SAREUM PROPRIETARY PT7-NH2 VECTOR
KEYWDS P38 MAP KINASE, TRANSFERASE-TRANSFERASE INHIBITOR COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR V.SEGARRA,P.EASTWOOD,R.ROCA,M.FISHER,M.LAMERS
REVDAT 2 13-SEP-23 3RIN 1 REMARK
REVDAT 1 29-FEB-12 3RIN 0
JRNL AUTH P.EASTWOOD,J.GONZALEZ,E.GOMEZ,B.VIDAL,F.CATURLA,R.ROCA,
JRNL AUTH 2 C.BALAGUE,A.ORELLANA,M.DOMINGUEZ
JRNL TITL INDOLIN-2-ONE P38(ALPHA) INHIBITORS I: DESIGN, PROFILING AND
JRNL TITL 2 CRYSTALLOGRAPHIC BINDING MODE.
JRNL REF BIOORG.MED.CHEM.LETT. V. 21 4130 2011
JRNL REFN ISSN 0960-894X
JRNL PMID 21696951
JRNL DOI 10.1016/J.BMCL.2011.05.114
REMARK 2
REMARK 2 RESOLUTION. 2.20 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.2.0019
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.20
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 19.78
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 82.7
REMARK 3 NUMBER OF REFLECTIONS : 20902
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 + TEST SET) : 0.265
REMARK 3 R VALUE (WORKING SET) : 0.261
REMARK 3 FREE R VALUE : 0.308
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.200
REMARK 3 FREE R VALUE TEST SET COUNT : 1081
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.20
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.26
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1497
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 86.42
REMARK 3 BIN R VALUE (WORKING SET) : 0.2960
REMARK 3 BIN FREE R VALUE SET COUNT : 88
REMARK 3 BIN FREE R VALUE : 0.3790
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2807
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 27
REMARK 3 SOLVENT ATOMS : 105
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 39.65
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.15000
REMARK 3 B22 (A**2) : -0.19000
REMARK 3 B33 (A**2) : 0.04000
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 OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.377
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.302
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.210
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 8.139
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.931
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.893
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 2904 ; 0.020 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 3951 ; 1.910 ; 1.973
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 348 ; 7.199 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 136 ;39.368 ;24.044
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 495 ;17.111 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 18 ;25.979 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 441 ; 0.116 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 2203 ; 0.008 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 1209 ; 0.229 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 1956 ; 0.309 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 121 ; 0.162 ; 0.200
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): 26 ; 0.206 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 2 ; 0.164 ; 0.200
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 1806 ; 1.006 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 2831 ; 1.661 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1273 ; 2.488 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1117 ; 3.735 ; 4.500
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.40
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS
REMARK 4
REMARK 4 3RIN COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 15-APR-11.
REMARK 100 THE DEPOSITION ID IS D_1000064977.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 18-AUG-06
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : ROTATING ANODE
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : RIGAKU MICROMAX-007 HF
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.54
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : RIGAKU RAXIS IV++
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : CRYSTALCLEAR 1.3 SP5
REMARK 200 DATA SCALING SOFTWARE : CRYSTALCLEAR 1.3 SP5
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 20902
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.200
REMARK 200 RESOLUTION RANGE LOW (A) : 19.790
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 93.3
REMARK 200 DATA REDUNDANCY : 2.970
REMARK 200 R MERGE (I) : 0.08000
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) : 2.20
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.28
REMARK 200 COMPLETENESS FOR SHELL (%) : 96.1
REMARK 200 DATA REDUNDANCY IN SHELL : 3.03
REMARK 200 R MERGE FOR SHELL (I) : 0.41000
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: MOLREP
REMARK 200 STARTING MODEL: PDB ENTRY 1OVE
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 59.18
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.01
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 22% PEG3350, 0.2 M SODIUM CHLORIDE, 1
REMARK 280 MM THP, 0.1 M BIS-TRIS, PH 6.5, VAPOR DIFFUSION, HANGING DROP,
REMARK 280 TEMPERATURE 298K
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 22.55500
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 61.74000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 43.31000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 61.74000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 22.55500
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 43.31000
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
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 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 LYS A 15 CG CD CE NZ
REMARK 470 ARG A 173 CG CD NE CZ NH1 NH2
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 27 CA - CB - CG ANGL. DEV. = 15.0 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 21 145.70 -39.97
REMARK 500 SER A 32 12.18 -69.23
REMARK 500 ARG A 57 65.69 36.27
REMARK 500 ASN A 100 12.16 -147.81
REMARK 500 ASN A 114 -70.31 -30.42
REMARK 500 ARG A 149 -19.05 73.84
REMARK 500 ALA A 172 110.41 -15.53
REMARK 500 ARG A 173 61.90 -152.11
REMARK 500 ASN A 201 -144.40 -124.83
REMARK 500 VAL A 273 -60.09 -90.85
REMARK 500 ASN A 278 126.81 -39.55
REMARK 500 LEU A 289 62.49 -100.94
REMARK 500 PRO A 350 154.35 -48.91
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 I2O A 401
DBREF 3RIN A 1 360 UNP Q16539 MK14_HUMAN 1 360
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 LEU 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 THR GLY TYR
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 I2O A 401 27
HETNAM I2O N-CYCLOPROPYL-4-METHYL-3-(2'-OXO-1',2'-
HETNAM 2 I2O DIHYDROSPIRO[CYCLOPENTANE-1,3'-INDOL]-6'-YL)BENZAMIDE
FORMUL 2 I2O C23 H24 N2 O2
FORMUL 3 HOH *105(H2 O)
HELIX 1 1 SER A 61 MET A 78 1 18
HELIX 2 2 LEU A 113 LYS A 118 1 6
HELIX 3 3 THR A 123 ALA A 144 1 22
HELIX 4 4 LYS A 152 SER A 154 5 3
HELIX 5 5 THR A 175 THR A 180 5 6
HELIX 6 6 ALA A 190 LEU A 195 1 6
HELIX 7 7 THR A 203 GLY A 219 1 17
HELIX 8 8 ASP A 227 GLY A 240 1 14
HELIX 9 9 GLY A 243 ILE A 250 1 8
HELIX 10 10 SER A 252 GLN A 260 1 9
HELIX 11 11 ASN A 269 PHE A 274 1 6
HELIX 12 12 ASN A 278 LEU A 289 1 12
HELIX 13 13 ASP A 292 ARG A 296 5 5
HELIX 14 14 THR A 298 ALA A 304 1 7
HELIX 15 15 HIS A 305 ALA A 309 5 5
HELIX 16 16 GLN A 325 ARG A 330 5 6
HELIX 17 17 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 TRP A 18 N GLN A 11
SHEET 1 B 5 TYR A 24 PRO A 29 0
SHEET 2 B 5 VAL A 38 ASP A 43 -1 O PHE A 42 N GLN A 25
SHEET 3 B 5 ARG A 49 SER A 56 -1 O VAL A 52 N CYS A 39
SHEET 4 B 5 ASP A 101 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 15 TYR A 35 ALA A 51 GLU A 71 LEU A 75
SITE 2 AC1 15 ILE A 84 THR A 106 HIS A 107 LEU A 108
SITE 3 AC1 15 MET A 109 GLY A 110 ALA A 111 LEU A 167
SITE 4 AC1 15 ASP A 168 PHE A 169 LEU A 171
CRYST1 45.110 86.620 123.480 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 0.022168 0.000000 0.000000 0.00000
SCALE2 0.000000 0.011545 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008098 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
