HEADER CELL ADHESION 12-SEP-06 2ICA
TITLE CD11A (LFA1) I-DOMAIN COMPLEXED WITH BMS-587101 AKA 5-[(5S, 9R)-9-(4-
TITLE 2 CYANOPHENYL)-3-(3,5-DICHLOROPHENYL)-1-METHYL-2,4-DIOXO-1,3,7-
TITLE 3 TRIAZASPIRO [4.4]NON-7-YL]METHYL]-3-THIOPHENECARBOXYLICACID
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: INTEGRIN ALPHA-L;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: VWFA DOMAIN, RESIDUES 154-332;
COMPND 5 SYNONYM: LEUKOCYTE ADHESION GLYCOPROTEIN LFA-1 ALPHA CHAIN, LFA-1A,
COMPND 6 LEUKOCYTE FUNCTION-ASSOCIATED MOLECULE 1 ALPHA CHAIN, CD11A ANTIGEN;
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: ITGAL, CD11A;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET28A;
SOURCE 11 OTHER_DETAILS: MINIMAL MEDIA
KEYWDS INHIBITOR, PROTEIN-LIGAND COMPLEX, CELL ADHESION
EXPDTA X-RAY DIFFRACTION
AUTHOR S.SHERIFF,H.EINSPAHR
REVDAT 4 30-AUG-23 2ICA 1 REMARK SEQADV
REVDAT 3 18-OCT-17 2ICA 1 REMARK
REVDAT 2 24-FEB-09 2ICA 1 VERSN
REVDAT 1 19-DEC-06 2ICA 0
JRNL AUTH D.POTIN,M.LAUNAY,F.MONATLIK,P.MALABRE,M.FABREGUETTES,
JRNL AUTH 2 A.FOUQUET,M.MAILLET,E.NICOLAI,L.DORGERET,F.CHEVALLIER,
JRNL AUTH 3 D.BESSE,M.DUFORT,F.CAUSSADE,S.Z.AHMAD,D.K.STETSKO,S.SKALA,
JRNL AUTH 4 P.M.DAVIS,P.BALIMANE,K.PATEL,Z.YANG,P.MARATHE,J.POSTELNECK,
JRNL AUTH 5 R.M.TOWNSEND,V.GOLDFARB,S.SHERIFF,H.EINSPAHR,K.KISH,
JRNL AUTH 6 M.F.MALLEY,J.D.DIMARCO,J.Z.GOUGOUTAS,P.KADIYALA,D.L.CHENEY,
JRNL AUTH 7 R.W.TEJWANI,D.K.MURPHY,K.W.MCINTYRE,X.YANG,S.CHAO,L.LEITH,
JRNL AUTH 8 Z.XIAO,A.MATHUR,B.C.CHEN,D.R.WU,S.C.TRAEGER,M.MCKINNON,
JRNL AUTH 9 J.C.BARRISH,J.A.ROBL,E.J.IWANOWICZ,S.J.SUCHARD,T.G.DHAR
JRNL TITL DISCOVERY AND DEVELOPMENT OF 5-[(5S,9R)-9-
JRNL TITL 2 (4-CYANOPHENYL)-3-(3,5-DICHLOROPHENYL)-1-
JRNL TITL 3 METHYL-2,4-DIOXO-1,3,7-TRIAZASPIRO[4.4]NON-
JRNL TITL 4 7-YL-METHYL]-3-THIOPHENECARBOXYLIC ACID (BMS-587101)-A SMALL
JRNL TITL 5 MOLECULE ANTAGONIST LEUKOCYTE FUNCTION ASSOCIATED ANTIGEN-1.
JRNL REF J.MED.CHEM. V. 49 6946 2006
JRNL REFN ISSN 0022-2623
JRNL PMID 17125246
JRNL DOI 10.1021/JM0610806
REMARK 2
REMARK 2 RESOLUTION. 1.56 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS
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 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.56
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 34.01
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 1021678.820
REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0000
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 98.2
REMARK 3 NUMBER OF REFLECTIONS : 23387
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) : 0.192
REMARK 3 R VALUE (WORKING SET) : 0.191
REMARK 3 FREE R VALUE : 0.223
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.800
REMARK 3 FREE R VALUE TEST SET COUNT : 1364
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.006
REMARK 3
REMARK 3 FIT/AGREEMENT OF MODEL WITH ALL DATA.
REMARK 3 R VALUE (WORKING + TEST SET, NO CUTOFF) : 0.1920
REMARK 3 R VALUE (WORKING SET, NO CUTOFF) : 0.1910
REMARK 3 FREE R VALUE (NO CUTOFF) : 0.223
REMARK 3 FREE R VALUE TEST SET SIZE (%, NO CUTOFF) : 5.800
REMARK 3 FREE R VALUE TEST SET COUNT (NO CUTOFF) : 1364
REMARK 3 ESTIMATED ERROR OF FREE R VALUE (NO CUTOFF) : 0.0060
REMARK 3 TOTAL NUMBER OF REFLECTIONS (NO CUTOFF) : 23387
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 8
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 1.56
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.63
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 87.40
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 2428
REMARK 3 BIN R VALUE (WORKING SET) : 0.3090
REMARK 3 BIN FREE R VALUE : 0.3380
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 5.60
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 143
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.028
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 1414
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 37
REMARK 3 SOLVENT ATOMS : 144
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 16.60
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 15.70
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -1.34000
REMARK 3 B22 (A**2) : 1.43000
REMARK 3 B33 (A**2) : -0.09000
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) : 0.17
REMARK 3 ESD FROM SIGMAA (A) : 0.06
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) : 0.20
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.03
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.004
REMARK 3 BOND ANGLES (DEGREES) : 1.200
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 24.00
REMARK 3 IMPROPER ANGLES (DEGREES) : 0.640
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) : 1.070 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 1.650 ; 2.000
REMARK 3 SIDE-CHAIN BOND (A**2) : 1.950 ; 2.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 2.840 ; 2.500
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : FLAT MODEL
REMARK 3 KSOL : 0.38
REMARK 3 BSOL : 48.33
REMARK 3
REMARK 3 NCS MODEL : NULL
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.PAR
REMARK 3 PARAMETER FILE 2 : WATER_REP.PAR
REMARK 3 PARAMETER FILE 3 : ION.PARAM
REMARK 3 PARAMETER FILE 4 : 2IC.PAR
REMARK 3 PARAMETER FILE 5 : NULL
REMARK 3 TOPOLOGY FILE 1 : PROTEIN.TOP
REMARK 3 TOPOLOGY FILE 2 : WATER.TOP
REMARK 3 TOPOLOGY FILE 3 : ION.TOP
REMARK 3 TOPOLOGY FILE 4 : 2IC.TOP
REMARK 3 TOPOLOGY FILE 5 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 2ICA COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 19-SEP-06.
REMARK 100 THE DEPOSITION ID IS D_1000039405.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 01-MAY-02
REMARK 200 TEMPERATURE (KELVIN) : 100.0
REMARK 200 PH : 8.9
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) : 1.5418
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : "BLUE" CONFOCAL
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : RIGAKU
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 23466
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.560
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.5
REMARK 200 DATA REDUNDANCY : 4.000
REMARK 200 R MERGE (I) : 0.04100
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 35.6000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.56
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.62
REMARK 200 COMPLETENESS FOR SHELL (%) : 86.3
REMARK 200 DATA REDUNDANCY IN SHELL : 2.50
REMARK 200 R MERGE FOR SHELL (I) : 0.23700
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 4.600
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: AMORE
REMARK 200 STARTING MODEL: PDB ENTRY 1LFA CHAIN A
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 38.94
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.01
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 80% (W/V) SODIUM CITRATE, 5% (V/V)
REMARK 280 GLYCEROL, MEASURED PH 8.9, VAPOR DIFFUSION, HANGING DROP,
REMARK 280 TEMPERATURE 293K
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 20.15000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 31.65000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 31.70000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 31.65000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 20.15000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 31.70000
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 GLY A 125
REMARK 465 SER A 126
REMARK 465 HIS A 127
REMARK 465 TYR A 307
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 MET A 128 CG SD CE
REMARK 470 ASN A 163 CG OD1 ND2
REMARK 470 ASP A 229 CG OD1 OD2
REMARK 470 LYS A 268 CG CD CE NZ
REMARK 470 GLU A 269 CG CD OE1 OE2
REMARK 470 ASP A 290 CG OD1 OD2
REMARK 470 GLU A 293 CG CD OE1 OE2
REMARK 470 GLU A 301 CG CD OE1 OE2
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 SER A 174 -102.64 -147.10
REMARK 500 LEU A 204 -131.37 -124.82
REMARK 500 ASP A 244 -159.29 -103.63
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 2IC A 1
DBREF 2ICA A 129 307 UNP P20701 ITAL_HUMAN 154 332
SEQADV 2ICA GLY A 125 UNP P20701 CLONING ARTIFACT
SEQADV 2ICA SER A 126 UNP P20701 CLONING ARTIFACT
SEQADV 2ICA HIS A 127 UNP P20701 CLONING ARTIFACT
SEQADV 2ICA MET A 128 UNP P20701 CLONING ARTIFACT
SEQRES 1 A 183 GLY SER HIS MET ASN VAL ASP LEU VAL PHE LEU PHE ASP
SEQRES 2 A 183 GLY SER MET SER LEU GLN PRO ASP GLU PHE GLN LYS ILE
SEQRES 3 A 183 LEU ASP PHE MET LYS ASP VAL MET LYS LYS LEU SER ASN
SEQRES 4 A 183 THR SER TYR GLN PHE ALA ALA VAL GLN PHE SER THR SER
SEQRES 5 A 183 TYR LYS THR GLU PHE ASP PHE SER ASP TYR VAL LYS ARG
SEQRES 6 A 183 LYS ASP PRO ASP ALA LEU LEU LYS HIS VAL LYS HIS MET
SEQRES 7 A 183 LEU LEU LEU THR ASN THR PHE GLY ALA ILE ASN TYR VAL
SEQRES 8 A 183 ALA THR GLU VAL PHE ARG GLU GLU LEU GLY ALA ARG PRO
SEQRES 9 A 183 ASP ALA THR LYS VAL LEU ILE ILE ILE THR ASP GLY GLU
SEQRES 10 A 183 ALA THR ASP SER GLY ASN ILE ASP ALA ALA LYS ASP ILE
SEQRES 11 A 183 ILE ARG TYR ILE ILE GLY ILE GLY LYS HIS PHE GLN THR
SEQRES 12 A 183 LYS GLU SER GLN GLU THR LEU HIS LYS PHE ALA SER LYS
SEQRES 13 A 183 PRO ALA SER GLU PHE VAL LYS ILE LEU ASP THR PHE GLU
SEQRES 14 A 183 LYS LEU LYS ASP LEU PHE THR GLU LEU GLN LYS LYS ILE
SEQRES 15 A 183 TYR
HET 2IC A 1 37
HETNAM 2IC 5-[(5S,9R)-9-(4-CYANOPHENYL)-3-(3,5-DICHLOROPHENYL)-1-
HETNAM 2 2IC METHYL-2,4-DIOXO-1,3,7-TRIAZASPIRO [4.4]NON-7-
HETNAM 3 2IC YL]METHYL]-3-THIOPHENECARBOXYLICACID
FORMUL 2 2IC C26 H20 CL2 N4 O4 S
FORMUL 3 HOH *144(H2 O)
HELIX 1 1 GLN A 143 LEU A 161 1 19
HELIX 2 2 ASP A 182 LYS A 190 1 9
HELIX 3 3 ASP A 191 LYS A 197 1 7
HELIX 4 4 ASN A 207 VAL A 219 1 13
HELIX 5 5 ARG A 221 GLY A 225 5 5
HELIX 6 6 ILE A 248 LYS A 252 5 5
HELIX 7 7 LYS A 263 GLN A 266 5 4
HELIX 8 8 THR A 267 THR A 273 1 7
HELIX 9 9 LEU A 274 ALA A 278 5 5
HELIX 10 10 PRO A 281 PHE A 285 1 5
SHEET 1 A 6 TYR A 177 PHE A 181 0
SHEET 2 A 6 TYR A 166 PHE A 173 -1 N GLN A 172 O LYS A 178
SHEET 3 A 6 VAL A 130 ASP A 137 1 N PHE A 134 O VAL A 171
SHEET 4 A 6 THR A 231 THR A 238 1 O ILE A 235 N VAL A 133
SHEET 5 A 6 ILE A 255 ILE A 261 1 O ILE A 259 N ILE A 236
SHEET 6 A 6 VAL A 286 LEU A 289 1 O LYS A 160 N GLY A 260
CISPEP 1 LYS A 280 PRO A 281 0 1.63
SITE 1 AC1 11 TYR A 166 VAL A 233 ILE A 235 ILE A 255
SITE 2 AC1 11 TYR A 257 ILE A 259 LYS A 287 LEU A 302
SITE 3 AC1 11 ILE A 306 HOH A 324 HOH A 381
CRYST1 40.300 63.400 63.300 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 0.024814 0.000000 0.000000 0.00000
SCALE2 0.000000 0.015773 0.000000 0.00000
SCALE3 0.000000 0.000000 0.015798 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
