HEADER APOPTOSIS/INHIBITOR 07-NOV-12 4HW3
TITLE DISCOVERY OF POTENT MCL-1 INHIBITORS USING FRAGMENT-BASED METHODS AND
TITLE 2 STRUCTURE-BASED DESIGN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: INDUCED MYELOID LEUKEMIA CELL DIFFERENTIATION PROTEIN MCL-
COMPND 3 1;
COMPND 4 CHAIN: A, B, C, D, E, F, G, H, I, J, K, L;
COMPND 5 SYNONYM: BCL-2-LIKE PROTEIN 3, BCL2-L-3, BCL-2-RELATED PROTEIN
COMPND 6 EAT/MCL1, MCL1/EAT;
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: MCL1, BCL2L3;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21-CODONPLUS (DE3)-RIL;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PDEST-HISMBP
KEYWDS REGULATION OF APOPTOSIS, MAINTENANCE OF VIABILITY, APOPTOSIS,
KEYWDS 2 APOPTOSIS-INHIBITOR COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR B.ZHAO
REVDAT 2 06-MAR-13 4HW3 1 JRNL
REVDAT 1 09-JAN-13 4HW3 0
JRNL AUTH A.FRIBERG,D.VIGIL,B.ZHAO,R.N.DANIELS,J.P.BURKE,
JRNL AUTH 2 P.M.GARCIA-BARRANTES,D.CAMPER,B.A.CHAUDER,T.LEE,
JRNL AUTH 3 E.T.OLEJNICZAK,S.W.FESIK
JRNL TITL DISCOVERY OF POTENT MYELOID CELL LEUKEMIA 1 (MCL-1)
JRNL TITL 2 INHIBITORS USING FRAGMENT-BASED METHODS AND STRUCTURE-BASED
JRNL TITL 3 DESIGN.
JRNL REF J.MED.CHEM. V. 56 15 2013
JRNL REFN ISSN 0022-2623
JRNL PMID 23244564
JRNL DOI 10.1021/JM301448P
REMARK 2
REMARK 2 RESOLUTION. 2.40 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE: 1.8_1069)
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VICENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-
REMARK 3 : KUNSTLEVE,LI-WEI HUNG,ROBERT IMMORMINO,
REMARK 3 : TOM IOERGER,AIRLIE MCCOY,ERIK MCKEE,NIGEL
REMARK 3 : MORIARTY,REETAL PAI,RANDY READ,JANE
REMARK 3 : RICHARDSON,DAVID RICHARDSON,TOD ROMO,JIM
REMARK 3 : SACCHETTINI,NICHOLAS SAUTER,JACOB SMITH,
REMARK 3 : LAURENT STORONI,TOM TERWILLIGER,PETER
REMARK 3 : ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.40
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 29.98
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.460
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.2
REMARK 3 NUMBER OF REFLECTIONS : 88346
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.216
REMARK 3 R VALUE (WORKING SET) : 0.215
REMARK 3 FREE R VALUE : 0.263
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 2.260
REMARK 3 FREE R VALUE TEST SET COUNT : 2001
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS).
REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE
REMARK 3 1 29.9826 - 5.7717 0.99 6505 151 0.1779 0.2156
REMARK 3 2 5.7717 - 4.5864 1.00 6319 148 0.1989 0.2356
REMARK 3 3 4.5864 - 4.0082 1.00 6304 146 0.1882 0.2237
REMARK 3 4 4.0082 - 3.6424 0.99 6223 141 0.1975 0.2369
REMARK 3 5 3.6424 - 3.3817 0.99 6239 148 0.2271 0.2724
REMARK 3 6 3.3817 - 3.1826 0.99 6232 140 0.2404 0.3160
REMARK 3 7 3.1826 - 3.0234 0.99 6190 141 0.2427 0.3010
REMARK 3 8 3.0234 - 2.8919 0.98 6115 143 0.2461 0.3070
REMARK 3 9 2.8919 - 2.7806 0.98 6113 147 0.2446 0.3096
REMARK 3 10 2.7806 - 2.6847 0.98 6057 143 0.2467 0.3174
REMARK 3 11 2.6847 - 2.6008 0.97 6088 137 0.2488 0.2773
REMARK 3 12 2.6008 - 2.5265 0.97 5983 145 0.2597 0.3373
REMARK 3 13 2.5265 - 2.4600 0.96 5978 130 0.2685 0.3500
REMARK 3 14 2.4600 - 2.4000 0.96 5999 141 0.2715 0.3131
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.11
REMARK 3 SHRINKAGE RADIUS : 0.90
REMARK 3 K_SOL : NULL
REMARK 3 B_SOL : NULL
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.330
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 26.320
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
REMARK 3
REMARK 3 TWINNING INFORMATION.
REMARK 3 FRACTION: NULL
REMARK 3 OPERATOR: NULL
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : 0.010 14919
REMARK 3 ANGLE : 1.411 20092
REMARK 3 CHIRALITY : 0.080 2193
REMARK 3 PLANARITY : 0.008 2551
REMARK 3 DIHEDRAL : 19.612 5550
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 4HW3 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 08-NOV-12.
REMARK 100 THE RCSB ID CODE IS RCSB075992.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 19-JUN-12
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 : 21-ID-G
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97856
REMARK 200 MONOCHROMATOR : SAGITALLY FOCUSED SI(111)
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MAR SCANNER 300 MM PLATE
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : NULL
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.400
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 1.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.2
REMARK 200 DATA REDUNDANCY : 3.500
REMARK 200 R MERGE (I) : 0.05300
REMARK 200 R SYM (I) : 0.04500
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 23.7000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.40
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.44
REMARK 200 COMPLETENESS FOR SHELL (%) : 96.3
REMARK 200 DATA REDUNDANCY IN SHELL : 2.70
REMARK 200 R MERGE FOR SHELL (I) : 0.29900
REMARK 200 R SYM FOR SHELL (I) : 0.36400
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.550
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 55.19
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.75
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 30% PEG3350, 0.2M MGCL2, PH 6.5, VAPOR
REMARK 280 DIFFUSION, HANGING DROP, TEMPERATURE 298K
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 29.38000
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12
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 350
REMARK 350 BIOMOLECULE: 2
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: 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 350
REMARK 350 BIOMOLECULE: 3
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: C
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 350
REMARK 350 BIOMOLECULE: 4
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: D
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 350
REMARK 350 BIOMOLECULE: 5
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: E
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 350
REMARK 350 BIOMOLECULE: 6
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: F
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 350
REMARK 350 BIOMOLECULE: 7
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: G
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 350
REMARK 350 BIOMOLECULE: 8
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: H
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 350
REMARK 350 BIOMOLECULE: 9
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: I
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 350
REMARK 350 BIOMOLECULE: 10
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: J
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 350
REMARK 350 BIOMOLECULE: 11
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: K
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 350
REMARK 350 BIOMOLECULE: 12
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: L
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 VAL A 321
REMARK 465 GLU A 322
REMARK 465 ASP A 323
REMARK 465 GLU B 322
REMARK 465 ASP B 323
REMARK 465 VAL C 321
REMARK 465 GLU C 322
REMARK 465 ASP C 323
REMARK 465 GLU E 322
REMARK 465 ASP E 323
REMARK 465 GLU F 322
REMARK 465 ASP F 323
REMARK 465 GLU G 322
REMARK 465 ASP G 323
REMARK 465 VAL H 321
REMARK 465 GLU H 322
REMARK 465 ASP H 323
REMARK 465 MET I 199
REMARK 465 GLY I 200
REMARK 465 ARG I 201
REMARK 465 VAL I 321
REMARK 465 GLU I 322
REMARK 465 ASP I 323
REMARK 465 GLY J 171
REMARK 465 GLU J 322
REMARK 465 ASP J 323
REMARK 465 GLU K 322
REMARK 465 ASP K 323
REMARK 465 ALA L 193
REMARK 465 LYS L 194
REMARK 465 ASP L 195
REMARK 465 THR L 196
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 197 CG CD CE NZ
REMARK 470 PRO A 198 CG CD
REMARK 470 ARG A 201 CG CD NE CZ NH1 NH2
REMARK 470 ARG C 201 CG CD NE CZ NH1 NH2
REMARK 470 THR D 196 OG1 CG2
REMARK 470 LYS D 197 CG CD CE NZ
REMARK 470 ARG D 201 CG CD NE CZ NH1 NH2
REMARK 470 GLU D 322 CG CD OE1 OE2
REMARK 470 ASP D 323 CG OD1 OD2
REMARK 470 LYS E 194 CG CD CE NZ
REMARK 470 THR G 196 OG1 CG2
REMARK 470 LYS G 197 CG CD CE NZ
REMARK 470 LYS H 194 CG CD CE NZ
REMARK 470 THR H 196 OG1 CG2
REMARK 470 LYS H 197 CG CD CE NZ
REMARK 470 PRO H 198 CG CD
REMARK 470 MET H 199 CG SD CE
REMARK 470 ARG H 201 CG CD NE CZ NH1 NH2
REMARK 470 LYS I 194 CG CD CE NZ
REMARK 470 ASP I 195 CG OD1 OD2
REMARK 470 THR I 196 OG1 CG2
REMARK 470 LYS I 197 CG CD CE NZ
REMARK 470 PRO I 198 CG CD
REMARK 470 LYS J 194 CG CD CE NZ
REMARK 470 THR J 196 OG1 CG2
REMARK 470 LYS J 197 CG CD CE NZ
REMARK 470 ARG J 201 CG CD NE CZ NH1 NH2
REMARK 470 LYS K 197 CG CD CE NZ
REMARK 470 LYS L 197 CG CD CE NZ
REMARK 470 ARG L 201 CG CD NE CZ NH1 NH2
REMARK 470 SER L 202 OG
REMARK 470 LEU L 278 CG CD1 CD2
REMARK 470 LYS L 279 CG CD CE NZ
REMARK 470 ASN L 282 CG OD1 ND2
REMARK 470 GLN L 283 CG CD OE1 NE2
REMARK 470 GLU L 284 CG CD OE1 OE2
REMARK 470 SER L 285 OG
REMARK 470 ASP L 323 CG OD1 OD2
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 ASP B 172 CB - CG - OD1 ANGL. DEV. = 5.6 DEGREES
REMARK 500 GLY L 200 N - CA - C ANGL. DEV. = 22.1 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 ASP A 172 -128.17 47.76
REMARK 500 ALA A 193 -179.90 179.92
REMARK 500 ARG A 201 -124.55 -109.61
REMARK 500 ILE A 281 20.81 -75.69
REMARK 500 ASP B 172 -126.93 46.19
REMARK 500 MET B 199 -106.84 -90.68
REMARK 500 ARG B 201 -35.07 -38.24
REMARK 500 ILE B 281 6.64 -65.76
REMARK 500 ASP C 172 -128.70 46.24
REMARK 500 MET C 199 172.32 73.38
REMARK 500 ARG C 201 -59.90 71.25
REMARK 500 ASP D 172 -128.53 48.47
REMARK 500 ALA D 193 158.57 -31.37
REMARK 500 THR D 280 -72.75 -74.71
REMARK 500 ILE D 281 22.36 -59.90
REMARK 500 ASP E 172 -131.41 47.69
REMARK 500 ALA E 193 89.34 -154.53
REMARK 500 LYS E 194 153.87 94.39
REMARK 500 THR E 280 -71.82 -77.78
REMARK 500 ILE E 281 0.68 -56.58
REMARK 500 HIS E 320 -125.01 53.07
REMARK 500 ASP F 172 -131.31 47.85
REMARK 500 LYS F 194 138.08 17.72
REMARK 500 SER F 255 31.38 -92.84
REMARK 500 ILE F 281 3.37 -54.55
REMARK 500 ASP G 172 -127.74 52.70
REMARK 500 LYS G 194 149.20 68.98
REMARK 500 THR G 280 -71.57 -75.86
REMARK 500 ILE G 281 3.73 -58.52
REMARK 500 ASP H 172 -131.53 47.02
REMARK 500 LYS H 194 140.77 82.06
REMARK 500 MET H 199 177.69 77.11
REMARK 500 THR H 280 -71.11 -78.34
REMARK 500 ILE H 281 5.26 -57.97
REMARK 500 ASP I 172 -123.06 54.49
REMARK 500 LYS I 194 128.14 51.82
REMARK 500 THR I 196 -130.98 54.17
REMARK 500 LYS I 197 59.00 -155.15
REMARK 500 ILE I 281 3.12 -55.62
REMARK 500 LYS J 194 144.51 85.83
REMARK 500 THR J 196 -55.70 69.12
REMARK 500 SER J 202 74.11 -101.81
REMARK 500 ASN J 282 49.97 76.27
REMARK 500 ASP K 172 -129.11 49.15
REMARK 500 THR K 196 -130.60 53.80
REMARK 500 LYS K 197 -52.29 -129.66
REMARK 500 PRO K 198 178.20 -59.56
REMARK 500 MET K 199 -169.55 -172.51
REMARK 500 ASP K 256 128.56 91.11
REMARK 500 ASP L 172 -127.15 50.40
REMARK 500
REMARK 500 THIS ENTRY HAS 57 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 LYS A 197 PRO A 198 -148.08
REMARK 500 PRO A 198 MET A 199 -139.43
REMARK 500 ASP E 195 THR E 196 -141.22
REMARK 500 ALA F 193 LYS F 194 121.43
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CHIRAL CENTERS
REMARK 500
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY
REMARK 500 FOR AMINO ACIDS AND C1'--O4'--N1(N9)--C2' FOR
REMARK 500 NUCLEIC ACIDS OR EQUIVALENT ANGLE
REMARK 500 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,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)
REMARK 500
REMARK 500 M RES CSSEQI IMPROPER EXPECTED FOUND DETAILS
REMARK 500 SER C 255 22.3 L L OUTSIDE RANGE
REMARK 500 ASN D 282 24.0 L L OUTSIDE RANGE
REMARK 500 THR E 196 23.5 L L OUTSIDE RANGE
REMARK 500 LYS F 194 23.3 L L OUTSIDE RANGE
REMARK 500 ASN L 282 23.1 L L OUTSIDE RANGE
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 19G A 400
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 19G B 400
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 19G C 400
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 19G D 400
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 19G E 400
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 19G F 400
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 19G G 400
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 19G H 400
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 19G I 400
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 19G J 400
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 19G K 400
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 19G L 400
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4HW2 RELATED DB: PDB
REMARK 900 RELATED ID: 4HW4 RELATED DB: PDB
DBREF 4HW3 A 172 323 UNP Q07820 MCL1_HUMAN 172 323
DBREF 4HW3 B 172 323 UNP Q07820 MCL1_HUMAN 172 323
DBREF 4HW3 C 172 323 UNP Q07820 MCL1_HUMAN 172 323
DBREF 4HW3 D 172 323 UNP Q07820 MCL1_HUMAN 172 323
DBREF 4HW3 E 172 323 UNP Q07820 MCL1_HUMAN 172 323
DBREF 4HW3 F 172 323 UNP Q07820 MCL1_HUMAN 172 323
DBREF 4HW3 G 172 323 UNP Q07820 MCL1_HUMAN 172 323
DBREF 4HW3 H 172 323 UNP Q07820 MCL1_HUMAN 172 323
DBREF 4HW3 I 172 323 UNP Q07820 MCL1_HUMAN 172 323
DBREF 4HW3 J 172 323 UNP Q07820 MCL1_HUMAN 172 323
DBREF 4HW3 K 172 323 UNP Q07820 MCL1_HUMAN 172 323
DBREF 4HW3 L 172 323 UNP Q07820 MCL1_HUMAN 172 323
SEQADV 4HW3 GLY A 171 UNP Q07820 EXPRESSION TAG
SEQADV 4HW3 GLY B 171 UNP Q07820 EXPRESSION TAG
SEQADV 4HW3 GLY C 171 UNP Q07820 EXPRESSION TAG
SEQADV 4HW3 GLY D 171 UNP Q07820 EXPRESSION TAG
SEQADV 4HW3 GLY E 171 UNP Q07820 EXPRESSION TAG
SEQADV 4HW3 GLY F 171 UNP Q07820 EXPRESSION TAG
SEQADV 4HW3 GLY G 171 UNP Q07820 EXPRESSION TAG
SEQADV 4HW3 GLY H 171 UNP Q07820 EXPRESSION TAG
SEQADV 4HW3 GLY I 171 UNP Q07820 EXPRESSION TAG
SEQADV 4HW3 GLY J 171 UNP Q07820 EXPRESSION TAG
SEQADV 4HW3 GLY K 171 UNP Q07820 EXPRESSION TAG
SEQADV 4HW3 GLY L 171 UNP Q07820 EXPRESSION TAG
SEQRES 1 A 153 GLY ASP GLU LEU TYR ARG GLN SER LEU GLU ILE ILE SER
SEQRES 2 A 153 ARG TYR LEU ARG GLU GLN ALA THR GLY ALA LYS ASP THR
SEQRES 3 A 153 LYS PRO MET GLY ARG SER GLY ALA THR SER ARG LYS ALA
SEQRES 4 A 153 LEU GLU THR LEU ARG ARG VAL GLY ASP GLY VAL GLN ARG
SEQRES 5 A 153 ASN HIS GLU THR ALA PHE GLN GLY MET LEU ARG LYS LEU
SEQRES 6 A 153 ASP ILE LYS ASN GLU ASP ASP VAL LYS SER LEU SER ARG
SEQRES 7 A 153 VAL MET ILE HIS VAL PHE SER ASP GLY VAL THR ASN TRP
SEQRES 8 A 153 GLY ARG ILE VAL THR LEU ILE SER PHE GLY ALA PHE VAL
SEQRES 9 A 153 ALA LYS HIS LEU LYS THR ILE ASN GLN GLU SER CYS ILE
SEQRES 10 A 153 GLU PRO LEU ALA GLU SER ILE THR ASP VAL LEU VAL ARG
SEQRES 11 A 153 THR LYS ARG ASP TRP LEU VAL LYS GLN ARG GLY TRP ASP
SEQRES 12 A 153 GLY PHE VAL GLU PHE PHE HIS VAL GLU ASP
SEQRES 1 B 153 GLY ASP GLU LEU TYR ARG GLN SER LEU GLU ILE ILE SER
SEQRES 2 B 153 ARG TYR LEU ARG GLU GLN ALA THR GLY ALA LYS ASP THR
SEQRES 3 B 153 LYS PRO MET GLY ARG SER GLY ALA THR SER ARG LYS ALA
SEQRES 4 B 153 LEU GLU THR LEU ARG ARG VAL GLY ASP GLY VAL GLN ARG
SEQRES 5 B 153 ASN HIS GLU THR ALA PHE GLN GLY MET LEU ARG LYS LEU
SEQRES 6 B 153 ASP ILE LYS ASN GLU ASP ASP VAL LYS SER LEU SER ARG
SEQRES 7 B 153 VAL MET ILE HIS VAL PHE SER ASP GLY VAL THR ASN TRP
SEQRES 8 B 153 GLY ARG ILE VAL THR LEU ILE SER PHE GLY ALA PHE VAL
SEQRES 9 B 153 ALA LYS HIS LEU LYS THR ILE ASN GLN GLU SER CYS ILE
SEQRES 10 B 153 GLU PRO LEU ALA GLU SER ILE THR ASP VAL LEU VAL ARG
SEQRES 11 B 153 THR LYS ARG ASP TRP LEU VAL LYS GLN ARG GLY TRP ASP
SEQRES 12 B 153 GLY PHE VAL GLU PHE PHE HIS VAL GLU ASP
SEQRES 1 C 153 GLY ASP GLU LEU TYR ARG GLN SER LEU GLU ILE ILE SER
SEQRES 2 C 153 ARG TYR LEU ARG GLU GLN ALA THR GLY ALA LYS ASP THR
SEQRES 3 C 153 LYS PRO MET GLY ARG SER GLY ALA THR SER ARG LYS ALA
SEQRES 4 C 153 LEU GLU THR LEU ARG ARG VAL GLY ASP GLY VAL GLN ARG
SEQRES 5 C 153 ASN HIS GLU THR ALA PHE GLN GLY MET LEU ARG LYS LEU
SEQRES 6 C 153 ASP ILE LYS ASN GLU ASP ASP VAL LYS SER LEU SER ARG
SEQRES 7 C 153 VAL MET ILE HIS VAL PHE SER ASP GLY VAL THR ASN TRP
SEQRES 8 C 153 GLY ARG ILE VAL THR LEU ILE SER PHE GLY ALA PHE VAL
SEQRES 9 C 153 ALA LYS HIS LEU LYS THR ILE ASN GLN GLU SER CYS ILE
SEQRES 10 C 153 GLU PRO LEU ALA GLU SER ILE THR ASP VAL LEU VAL ARG
SEQRES 11 C 153 THR LYS ARG ASP TRP LEU VAL LYS GLN ARG GLY TRP ASP
SEQRES 12 C 153 GLY PHE VAL GLU PHE PHE HIS VAL GLU ASP
SEQRES 1 D 153 GLY ASP GLU LEU TYR ARG GLN SER LEU GLU ILE ILE SER
SEQRES 2 D 153 ARG TYR LEU ARG GLU GLN ALA THR GLY ALA LYS ASP THR
SEQRES 3 D 153 LYS PRO MET GLY ARG SER GLY ALA THR SER ARG LYS ALA
SEQRES 4 D 153 LEU GLU THR LEU ARG ARG VAL GLY ASP GLY VAL GLN ARG
SEQRES 5 D 153 ASN HIS GLU THR ALA PHE GLN GLY MET LEU ARG LYS LEU
SEQRES 6 D 153 ASP ILE LYS ASN GLU ASP ASP VAL LYS SER LEU SER ARG
SEQRES 7 D 153 VAL MET ILE HIS VAL PHE SER ASP GLY VAL THR ASN TRP
SEQRES 8 D 153 GLY ARG ILE VAL THR LEU ILE SER PHE GLY ALA PHE VAL
SEQRES 9 D 153 ALA LYS HIS LEU LYS THR ILE ASN GLN GLU SER CYS ILE
SEQRES 10 D 153 GLU PRO LEU ALA GLU SER ILE THR ASP VAL LEU VAL ARG
SEQRES 11 D 153 THR LYS ARG ASP TRP LEU VAL LYS GLN ARG GLY TRP ASP
SEQRES 12 D 153 GLY PHE VAL GLU PHE PHE HIS VAL GLU ASP
SEQRES 1 E 153 GLY ASP GLU LEU TYR ARG GLN SER LEU GLU ILE ILE SER
SEQRES 2 E 153 ARG TYR LEU ARG GLU GLN ALA THR GLY ALA LYS ASP THR
SEQRES 3 E 153 LYS PRO MET GLY ARG SER GLY ALA THR SER ARG LYS ALA
SEQRES 4 E 153 LEU GLU THR LEU ARG ARG VAL GLY ASP GLY VAL GLN ARG
SEQRES 5 E 153 ASN HIS GLU THR ALA PHE GLN GLY MET LEU ARG LYS LEU
SEQRES 6 E 153 ASP ILE LYS ASN GLU ASP ASP VAL LYS SER LEU SER ARG
SEQRES 7 E 153 VAL MET ILE HIS VAL PHE SER ASP GLY VAL THR ASN TRP
SEQRES 8 E 153 GLY ARG ILE VAL THR LEU ILE SER PHE GLY ALA PHE VAL
SEQRES 9 E 153 ALA LYS HIS LEU LYS THR ILE ASN GLN GLU SER CYS ILE
SEQRES 10 E 153 GLU PRO LEU ALA GLU SER ILE THR ASP VAL LEU VAL ARG
SEQRES 11 E 153 THR LYS ARG ASP TRP LEU VAL LYS GLN ARG GLY TRP ASP
SEQRES 12 E 153 GLY PHE VAL GLU PHE PHE HIS VAL GLU ASP
SEQRES 1 F 153 GLY ASP GLU LEU TYR ARG GLN SER LEU GLU ILE ILE SER
SEQRES 2 F 153 ARG TYR LEU ARG GLU GLN ALA THR GLY ALA LYS ASP THR
SEQRES 3 F 153 LYS PRO MET GLY ARG SER GLY ALA THR SER ARG LYS ALA
SEQRES 4 F 153 LEU GLU THR LEU ARG ARG VAL GLY ASP GLY VAL GLN ARG
SEQRES 5 F 153 ASN HIS GLU THR ALA PHE GLN GLY MET LEU ARG LYS LEU
SEQRES 6 F 153 ASP ILE LYS ASN GLU ASP ASP VAL LYS SER LEU SER ARG
SEQRES 7 F 153 VAL MET ILE HIS VAL PHE SER ASP GLY VAL THR ASN TRP
SEQRES 8 F 153 GLY ARG ILE VAL THR LEU ILE SER PHE GLY ALA PHE VAL
SEQRES 9 F 153 ALA LYS HIS LEU LYS THR ILE ASN GLN GLU SER CYS ILE
SEQRES 10 F 153 GLU PRO LEU ALA GLU SER ILE THR ASP VAL LEU VAL ARG
SEQRES 11 F 153 THR LYS ARG ASP TRP LEU VAL LYS GLN ARG GLY TRP ASP
SEQRES 12 F 153 GLY PHE VAL GLU PHE PHE HIS VAL GLU ASP
SEQRES 1 G 153 GLY ASP GLU LEU TYR ARG GLN SER LEU GLU ILE ILE SER
SEQRES 2 G 153 ARG TYR LEU ARG GLU GLN ALA THR GLY ALA LYS ASP THR
SEQRES 3 G 153 LYS PRO MET GLY ARG SER GLY ALA THR SER ARG LYS ALA
SEQRES 4 G 153 LEU GLU THR LEU ARG ARG VAL GLY ASP GLY VAL GLN ARG
SEQRES 5 G 153 ASN HIS GLU THR ALA PHE GLN GLY MET LEU ARG LYS LEU
SEQRES 6 G 153 ASP ILE LYS ASN GLU ASP ASP VAL LYS SER LEU SER ARG
SEQRES 7 G 153 VAL MET ILE HIS VAL PHE SER ASP GLY VAL THR ASN TRP
SEQRES 8 G 153 GLY ARG ILE VAL THR LEU ILE SER PHE GLY ALA PHE VAL
SEQRES 9 G 153 ALA LYS HIS LEU LYS THR ILE ASN GLN GLU SER CYS ILE
SEQRES 10 G 153 GLU PRO LEU ALA GLU SER ILE THR ASP VAL LEU VAL ARG
SEQRES 11 G 153 THR LYS ARG ASP TRP LEU VAL LYS GLN ARG GLY TRP ASP
SEQRES 12 G 153 GLY PHE VAL GLU PHE PHE HIS VAL GLU ASP
SEQRES 1 H 153 GLY ASP GLU LEU TYR ARG GLN SER LEU GLU ILE ILE SER
SEQRES 2 H 153 ARG TYR LEU ARG GLU GLN ALA THR GLY ALA LYS ASP THR
SEQRES 3 H 153 LYS PRO MET GLY ARG SER GLY ALA THR SER ARG LYS ALA
SEQRES 4 H 153 LEU GLU THR LEU ARG ARG VAL GLY ASP GLY VAL GLN ARG
SEQRES 5 H 153 ASN HIS GLU THR ALA PHE GLN GLY MET LEU ARG LYS LEU
SEQRES 6 H 153 ASP ILE LYS ASN GLU ASP ASP VAL LYS SER LEU SER ARG
SEQRES 7 H 153 VAL MET ILE HIS VAL PHE SER ASP GLY VAL THR ASN TRP
SEQRES 8 H 153 GLY ARG ILE VAL THR LEU ILE SER PHE GLY ALA PHE VAL
SEQRES 9 H 153 ALA LYS HIS LEU LYS THR ILE ASN GLN GLU SER CYS ILE
SEQRES 10 H 153 GLU PRO LEU ALA GLU SER ILE THR ASP VAL LEU VAL ARG
SEQRES 11 H 153 THR LYS ARG ASP TRP LEU VAL LYS GLN ARG GLY TRP ASP
SEQRES 12 H 153 GLY PHE VAL GLU PHE PHE HIS VAL GLU ASP
SEQRES 1 I 153 GLY ASP GLU LEU TYR ARG GLN SER LEU GLU ILE ILE SER
SEQRES 2 I 153 ARG TYR LEU ARG GLU GLN ALA THR GLY ALA LYS ASP THR
SEQRES 3 I 153 LYS PRO MET GLY ARG SER GLY ALA THR SER ARG LYS ALA
SEQRES 4 I 153 LEU GLU THR LEU ARG ARG VAL GLY ASP GLY VAL GLN ARG
SEQRES 5 I 153 ASN HIS GLU THR ALA PHE GLN GLY MET LEU ARG LYS LEU
SEQRES 6 I 153 ASP ILE LYS ASN GLU ASP ASP VAL LYS SER LEU SER ARG
SEQRES 7 I 153 VAL MET ILE HIS VAL PHE SER ASP GLY VAL THR ASN TRP
SEQRES 8 I 153 GLY ARG ILE VAL THR LEU ILE SER PHE GLY ALA PHE VAL
SEQRES 9 I 153 ALA LYS HIS LEU LYS THR ILE ASN GLN GLU SER CYS ILE
SEQRES 10 I 153 GLU PRO LEU ALA GLU SER ILE THR ASP VAL LEU VAL ARG
SEQRES 11 I 153 THR LYS ARG ASP TRP LEU VAL LYS GLN ARG GLY TRP ASP
SEQRES 12 I 153 GLY PHE VAL GLU PHE PHE HIS VAL GLU ASP
SEQRES 1 J 153 GLY ASP GLU LEU TYR ARG GLN SER LEU GLU ILE ILE SER
SEQRES 2 J 153 ARG TYR LEU ARG GLU GLN ALA THR GLY ALA LYS ASP THR
SEQRES 3 J 153 LYS PRO MET GLY ARG SER GLY ALA THR SER ARG LYS ALA
SEQRES 4 J 153 LEU GLU THR LEU ARG ARG VAL GLY ASP GLY VAL GLN ARG
SEQRES 5 J 153 ASN HIS GLU THR ALA PHE GLN GLY MET LEU ARG LYS LEU
SEQRES 6 J 153 ASP ILE LYS ASN GLU ASP ASP VAL LYS SER LEU SER ARG
SEQRES 7 J 153 VAL MET ILE HIS VAL PHE SER ASP GLY VAL THR ASN TRP
SEQRES 8 J 153 GLY ARG ILE VAL THR LEU ILE SER PHE GLY ALA PHE VAL
SEQRES 9 J 153 ALA LYS HIS LEU LYS THR ILE ASN GLN GLU SER CYS ILE
SEQRES 10 J 153 GLU PRO LEU ALA GLU SER ILE THR ASP VAL LEU VAL ARG
SEQRES 11 J 153 THR LYS ARG ASP TRP LEU VAL LYS GLN ARG GLY TRP ASP
SEQRES 12 J 153 GLY PHE VAL GLU PHE PHE HIS VAL GLU ASP
SEQRES 1 K 153 GLY ASP GLU LEU TYR ARG GLN SER LEU GLU ILE ILE SER
SEQRES 2 K 153 ARG TYR LEU ARG GLU GLN ALA THR GLY ALA LYS ASP THR
SEQRES 3 K 153 LYS PRO MET GLY ARG SER GLY ALA THR SER ARG LYS ALA
SEQRES 4 K 153 LEU GLU THR LEU ARG ARG VAL GLY ASP GLY VAL GLN ARG
SEQRES 5 K 153 ASN HIS GLU THR ALA PHE GLN GLY MET LEU ARG LYS LEU
SEQRES 6 K 153 ASP ILE LYS ASN GLU ASP ASP VAL LYS SER LEU SER ARG
SEQRES 7 K 153 VAL MET ILE HIS VAL PHE SER ASP GLY VAL THR ASN TRP
SEQRES 8 K 153 GLY ARG ILE VAL THR LEU ILE SER PHE GLY ALA PHE VAL
SEQRES 9 K 153 ALA LYS HIS LEU LYS THR ILE ASN GLN GLU SER CYS ILE
SEQRES 10 K 153 GLU PRO LEU ALA GLU SER ILE THR ASP VAL LEU VAL ARG
SEQRES 11 K 153 THR LYS ARG ASP TRP LEU VAL LYS GLN ARG GLY TRP ASP
SEQRES 12 K 153 GLY PHE VAL GLU PHE PHE HIS VAL GLU ASP
SEQRES 1 L 153 GLY ASP GLU LEU TYR ARG GLN SER LEU GLU ILE ILE SER
SEQRES 2 L 153 ARG TYR LEU ARG GLU GLN ALA THR GLY ALA LYS ASP THR
SEQRES 3 L 153 LYS PRO MET GLY ARG SER GLY ALA THR SER ARG LYS ALA
SEQRES 4 L 153 LEU GLU THR LEU ARG ARG VAL GLY ASP GLY VAL GLN ARG
SEQRES 5 L 153 ASN HIS GLU THR ALA PHE GLN GLY MET LEU ARG LYS LEU
SEQRES 6 L 153 ASP ILE LYS ASN GLU ASP ASP VAL LYS SER LEU SER ARG
SEQRES 7 L 153 VAL MET ILE HIS VAL PHE SER ASP GLY VAL THR ASN TRP
SEQRES 8 L 153 GLY ARG ILE VAL THR LEU ILE SER PHE GLY ALA PHE VAL
SEQRES 9 L 153 ALA LYS HIS LEU LYS THR ILE ASN GLN GLU SER CYS ILE
SEQRES 10 L 153 GLU PRO LEU ALA GLU SER ILE THR ASP VAL LEU VAL ARG
SEQRES 11 L 153 THR LYS ARG ASP TRP LEU VAL LYS GLN ARG GLY TRP ASP
SEQRES 12 L 153 GLY PHE VAL GLU PHE PHE HIS VAL GLU ASP
HET 19G A 400 25
HET 19G B 400 25
HET 19G C 400 25
HET 19G D 400 25
HET 19G E 400 25
HET 19G F 400 25
HET 19G G 400 25
HET 19G H 400 25
HET 19G I 400 25
HET 19G J 400 25
HET 19G K 400 25
HET 19G L 400 25
HETNAM 19G 3-[3-(4-CHLORO-3,5-DIMETHYLPHENOXY)PROPYL]-1-
HETNAM 2 19G BENZOTHIOPHENE-2-CARBOXYLIC ACID
FORMUL 13 19G 12(C20 H19 CL O3 S)
FORMUL 25 HOH *251(H2 O)
HELIX 1 1 GLY A 171 THR A 191 1 21
HELIX 2 2 SER A 202 HIS A 224 1 23
HELIX 3 3 HIS A 224 ASP A 236 1 13
HELIX 4 4 ASN A 239 LYS A 244 1 6
HELIX 5 5 LEU A 246 SER A 255 1 10
HELIX 6 6 ASN A 260 ILE A 281 1 22
HELIX 7 7 GLN A 283 SER A 285 5 3
HELIX 8 8 CYS A 286 GLN A 309 1 24
HELIX 9 9 ARG A 310 PHE A 319 1 10
HELIX 10 10 ASP B 172 THR B 191 1 20
HELIX 11 11 SER B 202 HIS B 224 1 23
HELIX 12 12 HIS B 224 ASP B 236 1 13
HELIX 13 13 ASN B 239 SER B 245 1 7
HELIX 14 14 LEU B 246 SER B 255 1 10
HELIX 15 15 ASN B 260 ILE B 281 1 22
HELIX 16 16 GLN B 283 SER B 285 5 3
HELIX 17 17 CYS B 286 GLN B 309 1 24
HELIX 18 18 ARG B 310 PHE B 319 1 10
HELIX 19 19 ASP C 172 GLY C 192 1 21
HELIX 20 20 SER C 202 HIS C 224 1 23
HELIX 21 21 HIS C 224 ASP C 236 1 13
HELIX 22 22 ASN C 239 LYS C 244 1 6
HELIX 23 23 LEU C 246 ASP C 256 1 11
HELIX 24 24 ASN C 260 ILE C 281 1 22
HELIX 25 25 GLN C 283 SER C 285 5 3
HELIX 26 26 CYS C 286 GLN C 309 1 24
HELIX 27 27 ARG C 310 PHE C 319 1 10
HELIX 28 28 ASP D 172 THR D 191 1 20
HELIX 29 29 GLY D 203 HIS D 224 1 22
HELIX 30 30 HIS D 224 ASP D 236 1 13
HELIX 31 31 ASN D 239 LYS D 244 1 6
HELIX 32 32 LEU D 246 SER D 255 1 10
HELIX 33 33 ASN D 260 ILE D 281 1 22
HELIX 34 34 GLN D 283 SER D 285 5 3
HELIX 35 35 CYS D 286 GLN D 309 1 24
HELIX 36 36 ARG D 310 PHE D 319 1 10
HELIX 37 37 ASP E 172 THR E 191 1 20
HELIX 38 38 SER E 202 HIS E 224 1 23
HELIX 39 39 HIS E 224 ASP E 236 1 13
HELIX 40 40 ASN E 239 LYS E 244 1 6
HELIX 41 41 LEU E 246 SER E 255 1 10
HELIX 42 42 ASN E 260 ILE E 281 1 22
HELIX 43 43 GLN E 283 SER E 285 5 3
HELIX 44 44 CYS E 286 GLN E 309 1 24
HELIX 45 45 ARG E 310 PHE E 319 1 10
HELIX 46 46 ASP F 172 THR F 191 1 20
HELIX 47 47 SER F 202 HIS F 224 1 23
HELIX 48 48 HIS F 224 ASP F 236 1 13
HELIX 49 49 ASN F 239 LYS F 244 1 6
HELIX 50 50 LEU F 246 SER F 255 1 10
HELIX 51 51 ASN F 260 ILE F 281 1 22
HELIX 52 52 GLN F 283 SER F 285 5 3
HELIX 53 53 CYS F 286 GLN F 309 1 24
HELIX 54 54 GLY F 311 PHE F 319 1 9
HELIX 55 55 ASP G 172 GLY G 192 1 21
HELIX 56 56 GLY G 203 HIS G 224 1 22
HELIX 57 57 HIS G 224 ASP G 236 1 13
HELIX 58 58 ASN G 239 SER G 245 1 7
HELIX 59 59 LEU G 246 SER G 255 1 10
HELIX 60 60 ASN G 260 ILE G 281 1 22
HELIX 61 61 GLN G 283 SER G 285 5 3
HELIX 62 62 CYS G 286 GLN G 309 1 24
HELIX 63 63 ARG G 310 PHE G 319 1 10
HELIX 64 64 ASP H 172 THR H 191 1 20
HELIX 65 65 GLY H 203 HIS H 224 1 22
HELIX 66 66 HIS H 224 ASP H 236 1 13
HELIX 67 67 ASN H 239 SER H 245 1 7
HELIX 68 68 SER H 245 SER H 255 1 11
HELIX 69 69 ASN H 260 ASN H 282 1 23
HELIX 70 70 GLN H 283 SER H 285 5 3
HELIX 71 71 CYS H 286 LYS H 302 1 17
HELIX 72 72 LYS H 302 GLN H 309 1 8
HELIX 73 73 ARG H 310 PHE H 319 1 10
HELIX 74 74 ASP I 172 THR I 191 1 20
HELIX 75 75 GLY I 203 HIS I 224 1 22
HELIX 76 76 HIS I 224 ASP I 236 1 13
HELIX 77 77 ASN I 239 LYS I 244 1 6
HELIX 78 78 LEU I 246 SER I 255 1 10
HELIX 79 79 ASN I 260 ILE I 281 1 22
HELIX 80 80 GLN I 283 SER I 285 5 3
HELIX 81 81 CYS I 286 GLN I 309 1 24
HELIX 82 82 ARG I 310 PHE I 319 1 10
HELIX 83 83 GLU J 173 THR J 191 1 19
HELIX 84 84 SER J 202 HIS J 224 1 23
HELIX 85 85 HIS J 224 ASP J 236 1 13
HELIX 86 86 ASP J 242 LYS J 244 5 3
HELIX 87 87 SER J 245 ASP J 256 1 12
HELIX 88 88 ASN J 260 ASN J 282 1 23
HELIX 89 89 GLN J 283 SER J 285 5 3
HELIX 90 90 CYS J 286 GLN J 309 1 24
HELIX 91 91 ARG J 310 PHE J 319 1 10
HELIX 92 92 ASP K 172 THR K 191 1 20
HELIX 93 93 GLY K 203 HIS K 224 1 22
HELIX 94 94 HIS K 224 ASP K 236 1 13
HELIX 95 95 ASN K 239 LYS K 244 1 6
HELIX 96 96 LEU K 246 SER K 255 1 10
HELIX 97 97 ASN K 260 ILE K 281 1 22
HELIX 98 98 GLN K 283 SER K 285 5 3
HELIX 99 99 CYS K 286 GLN K 309 1 24
HELIX 100 100 ARG K 310 PHE K 319 1 10
HELIX 101 101 ASP L 172 GLY L 192 1 21
HELIX 102 102 SER L 202 HIS L 224 1 23
HELIX 103 103 HIS L 224 ASP L 236 1 13
HELIX 104 104 ASN L 239 SER L 245 1 7
HELIX 105 105 LEU L 246 SER L 255 1 10
HELIX 106 106 ASN L 260 THR L 280 1 21
HELIX 107 107 CYS L 286 GLN L 309 1 24
HELIX 108 108 ARG L 310 PHE L 319 1 10
CISPEP 1 GLY A 192 ALA A 193 0 7.08
CISPEP 2 MET A 199 GLY A 200 0 -14.97
CISPEP 3 PRO D 198 MET D 199 0 -22.48
CISPEP 4 ARG D 201 SER D 202 0 -0.22
CISPEP 5 SER D 202 GLY D 203 0 10.03
CISPEP 6 THR E 196 LYS E 197 0 -9.45
CISPEP 7 GLY F 257 VAL F 258 0 3.78
CISPEP 8 MET G 199 GLY G 200 0 -13.05
CISPEP 9 ARG H 201 SER H 202 0 6.84
CISPEP 10 SER H 255 ASP H 256 0 -1.84
CISPEP 11 LYS J 197 PRO J 198 0 -15.85
CISPEP 12 LYS L 197 PRO L 198 0 -15.42
CISPEP 13 GLY L 257 VAL L 258 0 8.58
SITE 1 AC1 7 PHE A 228 LEU A 246 VAL A 253 ARG A 263
SITE 2 AC1 7 THR A 266 LEU A 267 PHE A 270
SITE 1 AC2 10 MET B 231 LEU B 246 MET B 250 VAL B 253
SITE 2 AC2 10 ARG B 263 THR B 266 LEU B 267 PHE B 270
SITE 3 AC2 10 ILE B 294 LYS D 308
SITE 1 AC3 7 LYS A 308 PHE C 228 VAL C 253 ARG C 263
SITE 2 AC3 7 THR C 266 LEU C 267 PHE C 270
SITE 1 AC4 6 MET D 231 VAL D 253 ARG D 263 LEU D 267
SITE 2 AC4 6 PHE D 270 ILE D 294
SITE 1 AC5 7 VAL A 258 MET E 231 LEU E 246 ARG E 263
SITE 2 AC5 7 THR E 266 LEU E 267 PHE E 270
SITE 1 AC6 9 VAL D 258 PHE F 228 LEU F 246 MET F 250
SITE 2 AC6 9 ARG F 263 THR F 266 LEU F 267 PHE F 270
SITE 3 AC6 9 ILE F 294
SITE 1 AC7 7 MET G 231 LEU G 246 VAL G 253 ARG G 263
SITE 2 AC7 7 THR G 266 LEU G 267 PHE G 270
SITE 1 AC8 8 PHE H 228 MET H 250 VAL H 253 ARG H 263
SITE 2 AC8 8 THR H 266 LEU H 267 PHE H 270 GLY H 271
SITE 1 AC9 8 LEU I 246 MET I 250 VAL I 253 PHE I 254
SITE 2 AC9 8 ARG I 263 LEU I 267 PHE I 270 HIS K 320
SITE 1 BC1 11 PHE J 228 MET J 231 LEU J 235 LEU J 246
SITE 2 BC1 11 MET J 250 VAL J 253 ARG J 263 THR J 266
SITE 3 BC1 11 LEU J 267 PHE J 270 GLY J 271
SITE 1 BC2 7 PHE K 228 VAL K 253 PHE K 254 ARG K 263
SITE 2 BC2 7 LEU K 267 PHE K 270 ILE K 294
SITE 1 BC3 8 LEU L 246 MET L 250 VAL L 253 ARG L 263
SITE 2 BC3 8 THR L 266 LEU L 267 PHE L 270 GLY L 271
CRYST1 139.446 58.760 140.675 90.00 90.71 90.00 P 1 21 1 24
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 0.007171 0.000000 0.000088 0.00000
SCALE2 0.000000 0.017018 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007109 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
