HEADER TRANSFERASE/TRANSFERASE INHIBITOR 10-DEC-10 3PY1
TITLE CDK2 TERNARY COMPLEX WITH SU9516 AND ANS
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CELL DIVISION PROTEIN KINASE 2;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: CDK2, P33 PROTEIN KINASE;
COMPND 5 EC: 2.7.11.22;
COMPND 6 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: CDK2;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: TUNER(DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PGEX6P-1
KEYWDS PROTEIN KINASE, CDK2, ALLOSTERIC LIGAND, ANS, TRANSFERASE-TRANSFERASE
KEYWDS 2 INHIBITOR COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR S.BETZI,R.ALAM,E.SCHONBRUNN
REVDAT 3 13-SEP-23 3PY1 1 REMARK SEQADV
REVDAT 2 01-JUN-11 3PY1 1 JRNL
REVDAT 1 16-FEB-11 3PY1 0
JRNL AUTH S.BETZI,R.ALAM,M.MARTIN,D.J.LUBBERS,H.HAN,S.R.JAKKARAJ,
JRNL AUTH 2 G.I.GEORG,E.SCHONBRUNN
JRNL TITL DISCOVERY OF A POTENTIAL ALLOSTERIC LIGAND BINDING SITE IN
JRNL TITL 2 CDK2.
JRNL REF ACS CHEM.BIOL. V. 6 492 2011
JRNL REFN ISSN 1554-8929
JRNL PMID 21291269
JRNL DOI 10.1021/CB100410M
REMARK 2
REMARK 2 RESOLUTION. 2.05 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 1.2
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 : ENGH & HUBER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.05
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 19.58
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 1464924.090
REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0000
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 98.8
REMARK 3 NUMBER OF REFLECTIONS : 17189
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) : 0.199
REMARK 3 FREE R VALUE : 0.251
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 860
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.009
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) : 2.05
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.18
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.50
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 2692
REMARK 3 BIN R VALUE (WORKING SET) : 0.2130
REMARK 3 BIN FREE R VALUE : 0.2650
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 5.00
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 142
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.022
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2431
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 64
REMARK 3 SOLVENT ATOMS : 120
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 17.00
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 31.10
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -1.96000
REMARK 3 B22 (A**2) : 3.42000
REMARK 3 B33 (A**2) : -1.46000
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) : 0.23
REMARK 3 ESD FROM SIGMAA (A) : 0.12
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) : 0.30
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.15
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.010
REMARK 3 BOND ANGLES (DEGREES) : 1.400
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 21.90
REMARK 3 IMPROPER ANGLES (DEGREES) : 0.830
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : RESTRAINED
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : 1.300 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 2.190 ; 2.000
REMARK 3 SIDE-CHAIN BOND (A**2) : 1.670 ; 2.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 2.440 ; 2.500
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : FLAT MODEL
REMARK 3 KSOL : 0.40
REMARK 3 BSOL : 59.03
REMARK 3
REMARK 3 NCS MODEL : NONE
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 3 : EDO.PAR
REMARK 3 PARAMETER FILE 4 : INH.PAR
REMARK 3 PARAMETER FILE 5 : SU9.PAR
REMARK 3 PARAMETER FILE 6 : NULL
REMARK 3 TOPOLOGY FILE 1 : PROTEIN.TOP
REMARK 3 TOPOLOGY FILE 2 : WATER.TOP
REMARK 3 TOPOLOGY FILE 3 : EDO.TOP
REMARK 3 TOPOLOGY FILE 4 : INH.TOP
REMARK 3 TOPOLOGY FILE 5 : SU9.TOP
REMARK 3 TOPOLOGY FILE 6 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: BULK SOLVENT MODEL USED
REMARK 4
REMARK 4 3PY1 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 16-DEC-10.
REMARK 100 THE DEPOSITION ID IS D_1000062952.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 21-OCT-10
REMARK 200 TEMPERATURE (KELVIN) : 93
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 MICROMAX-007 HF
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.54178
REMARK 200 MONOCHROMATOR : MIRRORS
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : RIGAKU
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XDS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 17189
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.050
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 (%) : 98.7
REMARK 200 DATA REDUNDANCY : 4.300
REMARK 200 R MERGE (I) : 0.04400
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 23.0000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.05
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.10
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.5
REMARK 200 DATA REDUNDANCY IN SHELL : 4.20
REMARK 200 R MERGE FOR SHELL (I) : 0.04400
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 4.800
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: CNS 1.2
REMARK 200 STARTING MODEL: 1PW2
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 36.10
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.93
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 5 MG/ML CDK2, 1.5 MM SU9516, 15% (V/V)
REMARK 280 PEG3350, 50 MM HEPES/NAOH, SOAKED FOR 24 HRS IN 15 MM ANS, 2 MM
REMARK 280 SU9516, 50 MM HEPES, 50 MM NA/K PHOSPHATE, 7.5% (V/V) PEG3350,
REMARK 280 VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 291K, PH 7.5
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 26.67500
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 35.74000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 35.09500
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 35.74000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 26.67500
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 35.09500
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 GLY A -7
REMARK 465 PRO A -6
REMARK 465 LEU A -5
REMARK 465 GLY A -4
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 ASP A 38 76.16 -116.55
REMARK 500 GLU A 40 -103.07 -113.94
REMARK 500 THR A 41 -46.36 -27.96
REMARK 500 GLU A 42 -16.17 -157.58
REMARK 500 THR A 72 -142.78 -134.04
REMARK 500 GLU A 73 -85.70 -62.48
REMARK 500 ARG A 126 -23.11 78.87
REMARK 500 PHE A 152 -73.83 -104.59
REMARK 500 TYR A 179 117.36 54.19
REMARK 500 HIS A 295 76.84 -103.56
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 EDO A 299
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SU9 A 300
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 2AN A 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 2AN A 302
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3PXF RELATED DB: PDB
REMARK 900 CDK2/ANS/ANS COMPLEX
REMARK 900 RELATED ID: 3PXQ RELATED DB: PDB
REMARK 900 CDK2/ANS/ANS/ANS COMPLEX
REMARK 900 RELATED ID: 3PXR RELATED DB: PDB
REMARK 900 CDK2
REMARK 900 RELATED ID: 3PXY RELATED DB: PDB
REMARK 900 CDK2/JWS648 COMPLEX
REMARK 900 RELATED ID: 3PXZ RELATED DB: PDB
REMARK 900 CDK2/JWS648/ANS/ANS COMPLEX
REMARK 900 RELATED ID: 3PY0 RELATED DB: PDB
REMARK 900 CDK2/SU9516 COMPLEX
DBREF 3PY1 A 1 298 UNP P24941 CDK2_HUMAN 1 298
SEQADV 3PY1 GLY A -7 UNP P24941 EXPRESSION TAG
SEQADV 3PY1 PRO A -6 UNP P24941 EXPRESSION TAG
SEQADV 3PY1 LEU A -5 UNP P24941 EXPRESSION TAG
SEQADV 3PY1 GLY A -4 UNP P24941 EXPRESSION TAG
SEQADV 3PY1 SER A -3 UNP P24941 EXPRESSION TAG
SEQADV 3PY1 PRO A -2 UNP P24941 EXPRESSION TAG
SEQADV 3PY1 GLU A -1 UNP P24941 EXPRESSION TAG
SEQADV 3PY1 PHE A 0 UNP P24941 EXPRESSION TAG
SEQRES 1 A 306 GLY PRO LEU GLY SER PRO GLU PHE MET GLU ASN PHE GLN
SEQRES 2 A 306 LYS VAL GLU LYS ILE GLY GLU GLY THR TYR GLY VAL VAL
SEQRES 3 A 306 TYR LYS ALA ARG ASN LYS LEU THR GLY GLU VAL VAL ALA
SEQRES 4 A 306 LEU LYS LYS ILE ARG LEU ASP THR GLU THR GLU GLY VAL
SEQRES 5 A 306 PRO SER THR ALA ILE ARG GLU ILE SER LEU LEU LYS GLU
SEQRES 6 A 306 LEU ASN HIS PRO ASN ILE VAL LYS LEU LEU ASP VAL ILE
SEQRES 7 A 306 HIS THR GLU ASN LYS LEU TYR LEU VAL PHE GLU PHE LEU
SEQRES 8 A 306 HIS GLN ASP LEU LYS LYS PHE MET ASP ALA SER ALA LEU
SEQRES 9 A 306 THR GLY ILE PRO LEU PRO LEU ILE LYS SER TYR LEU PHE
SEQRES 10 A 306 GLN LEU LEU GLN GLY LEU ALA PHE CYS HIS SER HIS ARG
SEQRES 11 A 306 VAL LEU HIS ARG ASP LEU LYS PRO GLN ASN LEU LEU ILE
SEQRES 12 A 306 ASN THR GLU GLY ALA ILE LYS LEU ALA ASP PHE GLY LEU
SEQRES 13 A 306 ALA ARG ALA PHE GLY VAL PRO VAL ARG THR TYR THR HIS
SEQRES 14 A 306 GLU VAL VAL THR LEU TRP TYR ARG ALA PRO GLU ILE LEU
SEQRES 15 A 306 LEU GLY CYS LYS TYR TYR SER THR ALA VAL ASP ILE TRP
SEQRES 16 A 306 SER LEU GLY CYS ILE PHE ALA GLU MET VAL THR ARG ARG
SEQRES 17 A 306 ALA LEU PHE PRO GLY ASP SER GLU ILE ASP GLN LEU PHE
SEQRES 18 A 306 ARG ILE PHE ARG THR LEU GLY THR PRO ASP GLU VAL VAL
SEQRES 19 A 306 TRP PRO GLY VAL THR SER MET PRO ASP TYR LYS PRO SER
SEQRES 20 A 306 PHE PRO LYS TRP ALA ARG GLN ASP PHE SER LYS VAL VAL
SEQRES 21 A 306 PRO PRO LEU ASP GLU ASP GLY ARG SER LEU LEU SER GLN
SEQRES 22 A 306 MET LEU HIS TYR ASP PRO ASN LYS ARG ILE SER ALA LYS
SEQRES 23 A 306 ALA ALA LEU ALA HIS PRO PHE PHE GLN ASP VAL THR LYS
SEQRES 24 A 306 PRO VAL PRO HIS LEU ARG LEU
HET EDO A 299 4
HET SU9 A 300 18
HET 2AN A 301 21
HET 2AN A 302 21
HETNAM EDO 1,2-ETHANEDIOL
HETNAM SU9 (3Z)-3-(1H-IMIDAZOL-5-YLMETHYLENE)-5-METHOXY-1H-INDOL-
HETNAM 2 SU9 2(3H)-ONE
HETNAM 2AN 8-ANILINO-1-NAPHTHALENE SULFONATE
HETSYN EDO ETHYLENE GLYCOL
HETSYN SU9 SU9516
FORMUL 2 EDO C2 H6 O2
FORMUL 3 SU9 C13 H11 N3 O2
FORMUL 4 2AN 2(C16 H13 N O3 S)
FORMUL 6 HOH *120(H2 O)
HELIX 1 1 PHE A 0 GLU A 2 5 3
HELIX 2 2 PRO A 45 LEU A 58 1 14
HELIX 3 3 LEU A 87 ALA A 95 1 9
HELIX 4 4 PRO A 100 HIS A 121 1 22
HELIX 5 5 LYS A 129 GLN A 131 5 3
HELIX 6 6 THR A 158 VAL A 163 1 6
HELIX 7 7 VAL A 163 TYR A 168 1 6
HELIX 8 8 ALA A 170 LEU A 175 1 6
HELIX 9 9 THR A 182 ARG A 199 1 18
HELIX 10 10 SER A 207 GLY A 220 1 14
HELIX 11 11 GLY A 229 MET A 233 5 5
HELIX 12 12 ASP A 247 VAL A 252 1 6
HELIX 13 13 ASP A 256 LEU A 267 1 12
HELIX 14 14 SER A 276 ALA A 282 1 7
HELIX 15 15 HIS A 283 GLN A 287 5 5
SHEET 1 A 5 PHE A 4 GLY A 13 0
SHEET 2 A 5 GLY A 16 ASN A 23 -1 O GLY A 16 N GLY A 13
SHEET 3 A 5 VAL A 29 ARG A 36 -1 O LEU A 32 N TYR A 19
SHEET 4 A 5 LYS A 75 GLU A 81 -1 O LEU A 76 N ILE A 35
SHEET 5 A 5 LEU A 66 HIS A 71 -1 N ASP A 68 O VAL A 79
SHEET 1 B 3 GLN A 85 ASP A 86 0
SHEET 2 B 3 LEU A 133 ILE A 135 -1 O ILE A 135 N GLN A 85
SHEET 3 B 3 ILE A 141 LEU A 143 -1 O LYS A 142 N LEU A 134
SITE 1 AC1 2 LEU A 67 ASP A 68
SITE 1 AC2 11 ILE A 10 ALA A 31 PHE A 80 GLU A 81
SITE 2 AC2 11 PHE A 82 LEU A 83 HIS A 84 GLN A 85
SITE 3 AC2 11 LYS A 89 LEU A 134 ASP A 145
SITE 1 AC3 8 ILE A 49 ILE A 52 LYS A 56 LEU A 66
SITE 2 AC3 8 VAL A 69 HIS A 71 LEU A 76 PHE A 152
SITE 1 AC4 11 TYR A 15 LYS A 33 ILE A 35 LEU A 55
SITE 2 AC4 11 LYS A 56 VAL A 64 PHE A 80 ALA A 144
SITE 3 AC4 11 ASP A 145 PHE A 146 LEU A 148
CRYST1 53.350 70.190 71.480 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 0.018744 0.000000 0.000000 0.00000
SCALE2 0.000000 0.014247 0.000000 0.00000
SCALE3 0.000000 0.000000 0.013990 0.00000
(ATOM LINES ARE NOT SHOWN.)
END