HEADER TRANSFERASE/TRANSFERASE INHIBITOR 27-JUN-12 4FSN
TITLE CRYSTAL STRUCTURE OF THE CHK1
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: SERINE/THREONINE-PROTEIN KINASE CHK1;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: CHK1 CHECKPOINT HOMOLOG, CELL CYCLE CHECKPOINT KINASE,
COMPND 5 CHECKPOINT KINASE-1;
COMPND 6 EC: 2.7.11.1;
COMPND 7 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: CHEK1, CHK1;
SOURCE 6 EXPRESSION_SYSTEM: HOMO SAPIENS;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 9606
KEYWDS TRANSFERASE, TRANSFERASE-TRANSFERASE INHIBITOR COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR Y.N.KANG,J.A.STUCKEY,P.CHANG,A.J.RUSSELL
REVDAT 3 29-NOV-23 4FSN 1 REMARK SEQADV
REVDAT 2 29-MAY-13 4FSN 1 SOURCE
REVDAT 1 22-AUG-12 4FSN 0
JRNL AUTH Y.N.KANG,J.A.STUCKEY,P.CHANG,A.J.RUSSELL
JRNL TITL CRYSTAL STRUCTURE OF THE CHK1
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.10 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : BUSTER-TNT BUSTER 2.11.1
REMARK 3 AUTHORS : BRICOGNE,BLANC,BRANDL,FLENSBURG,KELLER,
REMARK 3 : PACIOREK,ROVERSI,SHARFF,SMART,VONRHEIN,
REMARK 3 : WOMACK,MATTHEWS,TEN EYCK,TRONRUD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.10
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 19.68
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 97.9
REMARK 3 NUMBER OF REFLECTIONS : 19248
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) : 0.178
REMARK 3 R VALUE (WORKING SET) : 0.176
REMARK 3 FREE R VALUE : 0.218
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.120
REMARK 3 FREE R VALUE TEST SET COUNT : 985
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 : 10
REMARK 3 BIN RESOLUTION RANGE HIGH (ANGSTROMS) : 2.10
REMARK 3 BIN RESOLUTION RANGE LOW (ANGSTROMS) : 2.21
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 97.87
REMARK 3 REFLECTIONS IN BIN (WORKING + TEST SET) : 2778
REMARK 3 BIN R VALUE (WORKING + TEST SET) : 0.1733
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 2635
REMARK 3 BIN R VALUE (WORKING SET) : 0.1713
REMARK 3 BIN FREE R VALUE : 0.2084
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 5.15
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 143
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 : 2137
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 39
REMARK 3 SOLVENT ATOMS : 190
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 28.15
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 4.53240
REMARK 3 B22 (A**2) : -3.84620
REMARK 3 B33 (A**2) : -0.68630
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : -1.48870
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.234
REMARK 3 DPI (BLOW EQ-10) BASED ON R VALUE (A) : NULL
REMARK 3 DPI (BLOW EQ-9) BASED ON FREE R VALUE (A) : NULL
REMARK 3 DPI (CRUICKSHANK) BASED ON R VALUE (A) : 0.184
REMARK 3 DPI (CRUICKSHANK) BASED ON FREE R VALUE (A) : NULL
REMARK 3
REMARK 3 REFERENCES: BLOW, D. (2002) ACTA CRYST D58, 792-797
REMARK 3 CRUICKSHANK, D.W.J. (1999) ACTA CRYST D55, 583-601
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.942
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.918
REMARK 3
REMARK 3 NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15
REMARK 3 TERM COUNT WEIGHT FUNCTION.
REMARK 3 BOND LENGTHS : 2261 ; 2.000 ; HARMONIC
REMARK 3 BOND ANGLES : 3097 ; 2.000 ; HARMONIC
REMARK 3 TORSION ANGLES : 1029 ; 2.000 ; SINUSOIDAL
REMARK 3 TRIGONAL CARBON PLANES : 58 ; 2.000 ; HARMONIC
REMARK 3 GENERAL PLANES : 350 ; 5.000 ; HARMONIC
REMARK 3 ISOTROPIC THERMAL FACTORS : 2261 ; 20.000 ; HARMONIC
REMARK 3 BAD NON-BONDED CONTACTS : NULL ; NULL ; NULL
REMARK 3 IMPROPER TORSIONS : NULL ; NULL ; NULL
REMARK 3 PSEUDOROTATION ANGLES : NULL ; NULL ; NULL
REMARK 3 CHIRAL IMPROPER TORSION : 278 ; 5.000 ; SEMIHARMONIC
REMARK 3 SUM OF OCCUPANCIES : NULL ; NULL ; NULL
REMARK 3 UTILITY DISTANCES : NULL ; NULL ; NULL
REMARK 3 UTILITY ANGLES : NULL ; NULL ; NULL
REMARK 3 UTILITY TORSION : NULL ; NULL ; NULL
REMARK 3 IDEAL-DIST CONTACT TERM : 2732 ; 4.000 ; SEMIHARMONIC
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.010
REMARK 3 BOND ANGLES (DEGREES) : 0.98
REMARK 3 PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 3.36
REMARK 3 OTHER TORSION ANGLES (DEGREES) : 2.74
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 3
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: {A|3 - 55}
REMARK 3 ORIGIN FOR THE GROUP (A): 9.8965 -6.0792 1.8674
REMARK 3 T TENSOR
REMARK 3 T11: 0.0583 T22: 0.0186
REMARK 3 T33: -0.1019 T12: -0.0774
REMARK 3 T13: -0.0007 T23: -0.0068
REMARK 3 L TENSOR
REMARK 3 L11: 0.2401 L22: 0.0000
REMARK 3 L33: 4.1464 L12: -0.8269
REMARK 3 L13: -0.1775 L23: 0.6849
REMARK 3 S TENSOR
REMARK 3 S11: 0.1173 S12: -0.0300 S13: -0.0561
REMARK 3 S21: 0.1457 S22: -0.1003 S23: 0.1185
REMARK 3 S31: 0.2930 S32: -0.1656 S33: -0.0170
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: {A|56 - 257}
REMARK 3 ORIGIN FOR THE GROUP (A): 15.5142 -0.4741 26.4849
REMARK 3 T TENSOR
REMARK 3 T11: -0.0527 T22: -0.0899
REMARK 3 T33: -0.0566 T12: 0.0193
REMARK 3 T13: 0.0056 T23: -0.0017
REMARK 3 L TENSOR
REMARK 3 L11: 1.8769 L22: 1.2505
REMARK 3 L33: 1.3518 L12: 0.6539
REMARK 3 L13: -0.4538 L23: -0.0667
REMARK 3 S TENSOR
REMARK 3 S11: -0.0828 S12: 0.0452 S13: -0.0603
REMARK 3 S21: -0.1058 S22: 0.0121 S23: -0.0150
REMARK 3 S31: 0.0972 S32: -0.0314 S33: 0.0707
REMARK 3
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: {A|258 - 280}
REMARK 3 ORIGIN FOR THE GROUP (A): 27.0946 16.9005 23.0804
REMARK 3 T TENSOR
REMARK 3 T11: -0.0573 T22: -0.0269
REMARK 3 T33: 0.0240 T12: 0.0374
REMARK 3 T13: 0.0028 T23: 0.0043
REMARK 3 L TENSOR
REMARK 3 L11: 0.0147 L22: 3.2471
REMARK 3 L33: 0.7934 L12: 1.9474
REMARK 3 L13: -0.1290 L23: -2.7710
REMARK 3 S TENSOR
REMARK 3 S11: 0.0619 S12: 0.1693 S13: 0.0512
REMARK 3 S21: -0.0531 S22: -0.1043 S23: 0.0454
REMARK 3 S31: -0.0525 S32: 0.0737 S33: 0.0424
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 4FSN COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 03-JUL-12.
REMARK 100 THE DEPOSITION ID IS D_1000073305.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : NULL
REMARK 200 TEMPERATURE (KELVIN) : 110
REMARK 200 PH : 7.5
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 RU200
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.54
REMARK 200 MONOCHROMATOR : OSMIC SI
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : NULL
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 19279
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.100
REMARK 200 RESOLUTION RANGE LOW (A) : 20.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.0
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : 0.08600
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 12.3000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.10
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.17
REMARK 200 COMPLETENESS FOR SHELL (%) : 98.4
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.22900
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: NULL
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 53.65
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.65
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 8000, ISOPROPANOL, HEPES, PH 7.5,
REMARK 280 VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 298.0K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,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 0.00000
REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 32.85550
REMARK 290 SMTRY3 2 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 TYR A 20
REMARK 465 LYS A 43
REMARK 465 ARG A 44
REMARK 465 ALA A 45
REMARK 465 VAL A 46
REMARK 465 ASP A 47
REMARK 465 CYS A 48
REMARK 465 PRO A 49
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 7 CG CD OE1 OE2
REMARK 470 ALA A 19 C O CB
REMARK 470 MET A 42 C O CB CG SD CE
REMARK 470 GLU A 50 CG CD OE1 OE2
REMARK 470 LYS A 53 CG CD CE NZ
REMARK 470 ARG A 75 CG CD NE CZ NH1 NH2
REMARK 470 GLU A 76 CG CD OE1 OE2
REMARK 470 LYS A 180 CG CD CE NZ
REMARK 470 LYS A 274 CG CD CE NZ
REMARK 470 ARG A 275 CG CD NE CZ NH1 NH2
REMARK 470 ARG A 277 CG CD NE CZ NH1 NH2
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 63 90.34 -160.37
REMARK 500 GLU A 76 74.25 -109.80
REMARK 500 ARG A 129 -1.49 74.33
REMARK 500 ASP A 130 46.41 -147.00
REMARK 500 ASP A 148 97.56 70.43
REMARK 500 ASN A 165 -9.97 -141.97
REMARK 500 LEU A 269 -37.67 -136.62
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 A58 A 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IPA A 303
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4FSM RELATED DB: PDB
REMARK 900 RELATED ID: 4FSQ RELATED DB: PDB
REMARK 900 RELATED ID: 4FSR RELATED DB: PDB
REMARK 900 RELATED ID: 4FST RELATED DB: PDB
REMARK 900 RELATED ID: 4FSU RELATED DB: PDB
REMARK 900 RELATED ID: 4FSW RELATED DB: PDB
REMARK 900 RELATED ID: 4FSY RELATED DB: PDB
REMARK 900 RELATED ID: 4FSZ RELATED DB: PDB
REMARK 900 RELATED ID: 4FT0 RELATED DB: PDB
REMARK 900 RELATED ID: 4FT1 RELATED DB: PDB
REMARK 900 RELATED ID: 4FT3 RELATED DB: PDB
REMARK 900 RELATED ID: 4FT5 RELATED DB: PDB
REMARK 900 RELATED ID: 4FT7 RELATED DB: PDB
REMARK 900 RELATED ID: 4FT9 RELATED DB: PDB
REMARK 900 RELATED ID: 4FTA RELATED DB: PDB
REMARK 900 RELATED ID: 4FTC RELATED DB: PDB
REMARK 900 RELATED ID: 4FTI RELATED DB: PDB
REMARK 900 RELATED ID: 4FTJ RELATED DB: PDB
REMARK 900 RELATED ID: 4FTK RELATED DB: PDB
REMARK 900 RELATED ID: 4FTL RELATED DB: PDB
REMARK 900 RELATED ID: 4FTM RELATED DB: PDB
REMARK 900 RELATED ID: 4FTN RELATED DB: PDB
REMARK 900 RELATED ID: 4FTO RELATED DB: PDB
REMARK 900 RELATED ID: 4FTQ RELATED DB: PDB
REMARK 900 RELATED ID: 4FTR RELATED DB: PDB
REMARK 900 RELATED ID: 4FTT RELATED DB: PDB
REMARK 900 RELATED ID: 4FTU RELATED DB: PDB
DBREF 4FSN A 3 280 UNP O14757 CHK1_HUMAN 4 282
SEQADV 4FSN A UNP O14757 VAL 5 DELETION
SEQRES 1 A 278 ALA PRO PHE VAL GLU ASP TRP ASP LEU VAL GLN THR LEU
SEQRES 2 A 278 GLY GLU GLY ALA TYR GLY GLU VAL GLN LEU ALA VAL ASN
SEQRES 3 A 278 ARG VAL THR GLU GLU ALA VAL ALA VAL LYS ILE VAL ASP
SEQRES 4 A 278 MET LYS ARG ALA VAL ASP CYS PRO GLU ASN ILE LYS LYS
SEQRES 5 A 278 GLU ILE CYS ILE ASN LYS MET LEU ASN HIS GLU ASN VAL
SEQRES 6 A 278 VAL LYS PHE TYR GLY HIS ARG ARG GLU GLY ASN ILE GLN
SEQRES 7 A 278 TYR LEU PHE LEU GLU TYR CYS SER GLY GLY GLU LEU PHE
SEQRES 8 A 278 ASP ARG ILE GLU PRO ASP ILE GLY MET PRO GLU PRO ASP
SEQRES 9 A 278 ALA GLN ARG PHE PHE HIS GLN LEU MET ALA GLY VAL VAL
SEQRES 10 A 278 TYR LEU HIS GLY ILE GLY ILE THR HIS ARG ASP ILE LYS
SEQRES 11 A 278 PRO GLU ASN LEU LEU LEU ASP GLU ARG ASP ASN LEU LYS
SEQRES 12 A 278 ILE SER ASP PHE GLY LEU ALA THR VAL PHE ARG TYR ASN
SEQRES 13 A 278 ASN ARG GLU ARG LEU LEU ASN LYS MET CYS GLY THR LEU
SEQRES 14 A 278 PRO TYR VAL ALA PRO GLU LEU LEU LYS ARG ARG GLU PHE
SEQRES 15 A 278 HIS ALA GLU PRO VAL ASP VAL TRP SER CYS GLY ILE VAL
SEQRES 16 A 278 LEU THR ALA MET LEU ALA GLY GLU LEU PRO TRP ASP GLN
SEQRES 17 A 278 PRO SER ASP SER CYS GLN GLU TYR SER ASP TRP LYS GLU
SEQRES 18 A 278 LYS LYS THR TYR LEU ASN PRO TRP LYS LYS ILE ASP SER
SEQRES 19 A 278 ALA PRO LEU ALA LEU LEU HIS LYS ILE LEU VAL GLU ASN
SEQRES 20 A 278 PRO SER ALA ARG ILE THR ILE PRO ASP ILE LYS LYS ASP
SEQRES 21 A 278 ARG TRP TYR ASN LYS PRO LEU LYS LYS GLY ALA LYS ARG
SEQRES 22 A 278 PRO ARG VAL THR SER
HET A58 A 301 56
HET SO4 A 302 5
HET IPA A 303 4
HETNAM A58 4-(6-{[(4-METHYLCYCLOHEXYL)AMINO]METHYL}-1,4-
HETNAM 2 A58 DIHYDROINDENO[1,2-C]PYRAZOL-3-YL)BENZOIC ACID
HETNAM SO4 SULFATE ION
HETNAM IPA ISOPROPYL ALCOHOL
HETSYN IPA 2-PROPANOL
FORMUL 2 A58 C25 H27 N3 O2
FORMUL 3 SO4 O4 S 2-
FORMUL 4 IPA C3 H8 O
FORMUL 5 HOH *190(H2 O)
HELIX 1 1 ASN A 51 LYS A 60 1 10
HELIX 2 2 PHE A 93 ILE A 96 5 4
HELIX 3 3 PRO A 103 ILE A 124 1 22
HELIX 4 4 LYS A 132 GLU A 134 5 3
HELIX 5 5 THR A 170 VAL A 174 5 5
HELIX 6 6 ALA A 175 ARG A 181 1 7
HELIX 7 7 HIS A 185 GLY A 204 1 20
HELIX 8 8 CYS A 215 GLU A 223 1 9
HELIX 9 9 PRO A 230 ILE A 234 5 5
HELIX 10 10 ASP A 235 LEU A 246 1 12
HELIX 11 11 THR A 255 LYS A 260 1 6
SHEET 1 A 5 TRP A 9 GLU A 17 0
SHEET 2 A 5 GLU A 22 ASN A 28 -1 O LEU A 25 N GLN A 13
SHEET 3 A 5 ALA A 34 ASP A 41 -1 O VAL A 37 N GLN A 24
SHEET 4 A 5 ILE A 79 GLU A 85 -1 O LEU A 84 N ALA A 36
SHEET 5 A 5 PHE A 70 GLU A 76 -1 N GLY A 72 O PHE A 83
SHEET 1 B 3 GLY A 90 GLU A 91 0
SHEET 2 B 3 LEU A 136 LEU A 138 -1 O LEU A 138 N GLY A 90
SHEET 3 B 3 LEU A 144 ILE A 146 -1 O LYS A 145 N LEU A 137
SHEET 1 C 2 ILE A 126 THR A 127 0
SHEET 2 C 2 THR A 153 VAL A 154 -1 O THR A 153 N THR A 127
SHEET 1 D 2 ARG A 156 TYR A 157 0
SHEET 2 D 2 ARG A 160 GLU A 161 -1 O ARG A 160 N TYR A 157
CISPEP 1 ASN A 229 PRO A 230 0 2.96
SITE 1 AC1 13 GLN A 13 LEU A 15 ALA A 36 LYS A 38
SITE 2 AC1 13 LEU A 84 GLU A 85 TYR A 86 CYS A 87
SITE 3 AC1 13 GLY A 90 LEU A 137 ASP A 148 HOH A 570
SITE 4 AC1 13 HOH A 571
SITE 1 AC2 6 LYS A 54 ARG A 129 THR A 153 LYS A 166
SITE 2 AC2 6 HOH A 427 HOH A 442
SITE 1 AC3 4 ILE A 96 TYR A 173 GLY A 204 GLU A 205
CRYST1 44.940 65.711 57.773 90.00 94.20 90.00 P 1 21 1 2
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 0.022252 0.000000 0.001634 0.00000
SCALE2 0.000000 0.015218 0.000000 0.00000
SCALE3 0.000000 0.000000 0.017356 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
