HEADER LIGASE/LIGASE INHIBITOR 19-JUN-14 4QOC
TITLE CRYSTAL STRUCTURE OF COMPOUND 16 BOUND TO MDM2(17-111), {(3R,5R,6S)-5-
TITLE 2 (3-CHLOROPHENYL)-6-(4-CHLOROPHENYL)-1-[(1S)-1-CYCLOPROPYL-2-
TITLE 3 (PYRROLIDIN-1-YLSULFONYL)ETHYL]-3-METHYL-2-OXOPIPERIDIN-3-YL}ACETIC
TITLE 4 ACID
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: E3 UBIQUITIN-PROTEIN LIGASE MDM2;
COMPND 3 CHAIN: A, C, E, G, I, K;
COMPND 4 SYNONYM: DOUBLE MINUTE 2 PROTEIN, HDM2, ONCOPROTEIN MDM2, P53-BINDING
COMPND 5 PROTEIN MDM2;
COMPND 6 EC: 6.3.2.-;
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: MDM2;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS MDM2, P53, PROTEIN-PROTEIN INTERACTION, INHIBITOR, LIGASE-LIGASE
KEYWDS 2 INHIBITOR COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR X.HUANG
REVDAT 2 28-FEB-24 4QOC 1 REMARK SEQADV
REVDAT 1 06-MAY-15 4QOC 0
JRNL AUTH Y.WANG,J.ZHU,J.J.LIU,X.CHEN,J.MIHALIC,J.DEIGNAN,M.YU,D.SUN,
JRNL AUTH 2 F.KAYSER,L.R.MCGEE,M.C.LO,A.CHEN,J.ZHOU,Q.YE,X.HUANG,
JRNL AUTH 3 A.M.LONG,P.YAKOWEC,J.D.OLINER,S.H.OLSON,J.C.MEDINA
JRNL TITL OPTIMIZATION BEYOND AMG 232: DISCOVERY AND SAR OF
JRNL TITL 2 SULFONAMIDES ON A PIPERIDINONE SCAFFOLD AS POTENT INHIBITORS
JRNL TITL 3 OF THE MDM2-P53 PROTEIN-PROTEIN INTERACTION.
JRNL REF BIOORG.MED.CHEM.LETT. V. 24 3782 2014
JRNL REFN ISSN 0960-894X
JRNL PMID 25042256
JRNL DOI 10.1016/J.BMCL.2014.06.073
REMARK 2
REMARK 2 RESOLUTION. 1.70 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 REFINEMENT TARGET : ENGH & HUBER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.70
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 50.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 NUMBER OF REFLECTIONS : 62432
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : NULL
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING SET) : 0.238
REMARK 3 FREE R VALUE : 0.253
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : 3159
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 : NULL
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : NULL
REMARK 3 BIN RESOLUTION RANGE LOW (A) : NULL
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : NULL
REMARK 3 BIN FREE R VALUE : NULL
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 BIN FREE R VALUE TEST SET COUNT : NULL
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 : 4566
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 234
REMARK 3 SOLVENT ATOMS : 603
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 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM SIGMAA (A) : NULL
REMARK 3 LOW RESOLUTION CUTOFF (A) : NULL
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM C-V SIGMAA (A) : NULL
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : NULL
REMARK 3 BOND ANGLES (DEGREES) : NULL
REMARK 3 DIHEDRAL ANGLES (DEGREES) : NULL
REMARK 3 IMPROPER ANGLES (DEGREES) : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : NULL
REMARK 3 KSOL : NULL
REMARK 3 BSOL : NULL
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 : NULL
REMARK 3 TOPOLOGY FILE 1 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 4QOC COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 20-JUN-14.
REMARK 100 THE DEPOSITION ID IS D_1000086307.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : NULL
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 5.0
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-F
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0000
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 225 MM CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 63269
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.700
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 96.8
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : 0.07600
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) : 1.70
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.76
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.0
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.85500
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: AMORE
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 43.38
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.17
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 100 MM CITRATE, 1.9-2.4 M AMMONIUM
REMARK 280 SULFATE, PH 5.0, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 277K
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 28.28800
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 51.96050
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 49.46250
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 51.96050
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 28.28800
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 49.46250
REMARK 290 SMTRY3 4 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
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: 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: 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: 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: 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: 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: 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: 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: 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: 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 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 16
REMARK 465 SER A 17
REMARK 465 GLN A 18
REMARK 465 ASN A 111
REMARK 465 GLY C 16
REMARK 465 SER C 17
REMARK 465 GLN C 18
REMARK 465 ASN C 111
REMARK 465 GLY E 16
REMARK 465 ARG E 65
REMARK 465 GLY G 16
REMARK 465 SER G 17
REMARK 465 GLY I 16
REMARK 465 ASN I 111
REMARK 465 GLY K 16
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 70 CG CD CE NZ
REMARK 470 GLN A 71 CG CD OE1 NE2
REMARK 470 GLU C 69 CG CD OE1 OE2
REMARK 470 GLN E 18 CG CD OE1 NE2
REMARK 470 GLU E 69 CG CD OE1 OE2
REMARK 470 LYS E 70 CG CD CE NZ
REMARK 470 GLN G 18 CG CD OE1 NE2
REMARK 470 GLU G 69 CG CD OE1 OE2
REMARK 470 LYS G 70 CG CD CE NZ
REMARK 470 GLU I 69 CG CD OE1 OE2
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 OE2 GLU I 25 O HOH I 381 1.63
REMARK 500 O GLN E 71 O HOH E 305 1.71
REMARK 500 O HOH K 301 O HOH K 376 1.73
REMARK 500 O HOH A 301 O HOH A 311 1.74
REMARK 500 O HOH C 310 O HOH C 409 1.75
REMARK 500 O HOH G 324 O HOH G 334 1.77
REMARK 500 O HOH C 345 O HOH C 392 1.78
REMARK 500 N ILE A 19 O HOH A 389 1.78
REMARK 500 O HOH C 309 O HOH K 320 1.78
REMARK 500 O HOH C 302 O HOH C 317 1.79
REMARK 500 O HOH A 346 O HOH A 415 1.79
REMARK 500 O HOH I 354 O HOH I 359 1.79
REMARK 500 O HOH C 328 O HOH E 332 1.80
REMARK 500 O HOH E 350 O HOH E 379 1.80
REMARK 500 O HOH G 308 O HOH G 311 1.81
REMARK 500 NH1 ARG G 97 O HOH G 333 1.83
REMARK 500 NE ARG C 105 O HOH C 389 1.83
REMARK 500 NH1 ARG C 105 O HOH C 393 1.84
REMARK 500 O HOH A 321 O HOH A 333 1.85
REMARK 500 OD1 ASN G 79 O HOH G 319 1.85
REMARK 500 O HOH G 361 O HOH I 360 1.87
REMARK 500 CE2 TYR C 48 O HOH C 398 1.87
REMARK 500 NZ LYS K 64 O HOH K 380 1.88
REMARK 500 O HOH A 349 O HOH A 359 1.88
REMARK 500 O HOH K 392 O HOH K 396 1.89
REMARK 500 OD1 ASP A 84 O HOH A 372 1.90
REMARK 500 O HOH C 379 O HOH C 397 1.91
REMARK 500 O HOH A 329 O HOH C 375 1.92
REMARK 500 O HOH C 360 O HOH G 329 1.92
REMARK 500 O HOH K 319 O HOH K 349 1.93
REMARK 500 CA GLN G 71 O HOH G 363 1.93
REMARK 500 O HOH A 341 O HOH A 405 1.93
REMARK 500 O HOH K 374 O HOH K 398 1.95
REMARK 500 O HOH C 320 O HOH C 346 1.95
REMARK 500 O HOH G 353 O HOH G 378 1.96
REMARK 500 O HOH C 356 O HOH C 398 1.96
REMARK 500 CB ASN E 111 O HOH E 319 1.96
REMARK 500 NZ LYS K 36 O HOH K 374 1.97
REMARK 500 CG GLN G 72 O HOH G 370 1.97
REMARK 500 NZ LYS G 51 O HOH G 368 1.98
REMARK 500 NE2 GLN C 71 O HOH C 344 1.98
REMARK 500 O HOH K 310 O HOH K 376 1.98
REMARK 500 O HOH C 317 O HOH C 337 1.98
REMARK 500 O HOH A 311 O HOH A 410 1.99
REMARK 500 O HOH E 332 O HOH K 383 1.99
REMARK 500 O HOH C 401 O HOH C 411 2.00
REMARK 500 O HOH A 339 O HOH C 410 2.00
REMARK 500 O HOH A 322 O HOH A 405 2.00
REMARK 500 O HOH A 308 O HOH A 362 2.01
REMARK 500 OE2 GLU G 52 O HOH G 365 2.02
REMARK 500
REMARK 500 THIS ENTRY HAS 90 CLOSE CONTACTS
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 O HOH A 348 O HOH I 301 1655 1.70
REMARK 500 O HOH A 309 O HOH C 309 1655 1.77
REMARK 500 O HOH E 370 O HOH I 360 2454 1.80
REMARK 500 O HOH A 342 O HOH K 381 1655 1.85
REMARK 500 O HOH E 344 O HOH E 382 4544 1.90
REMARK 500 O HOH E 333 O HOH E 344 4444 1.93
REMARK 500 O HOH E 385 O HOH I 372 2454 1.98
REMARK 500 O SER E 17 O HOH G 353 2454 2.11
REMARK 500 O HOH E 357 O HOH G 327 2454 2.11
REMARK 500 O HOH E 367 O HOH G 380 3544 2.14
REMARK 500 O HOH I 336 O HOH K 352 2455 2.19
REMARK 500
REMARK 500 REMARK: NULL
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 A 46 CB - CG - OD1 ANGL. DEV. = 12.5 DEGREES
REMARK 500 ASP A 46 CB - CG - OD2 ANGL. DEV. = -10.6 DEGREES
REMARK 500 ARG A 105 NE - CZ - NH1 ANGL. DEV. = 3.9 DEGREES
REMARK 500 ARG A 105 NE - CZ - NH2 ANGL. DEV. = -4.5 DEGREES
REMARK 500 ARG C 29 NE - CZ - NH1 ANGL. DEV. = 8.7 DEGREES
REMARK 500 ARG C 29 NE - CZ - NH2 ANGL. DEV. = -9.1 DEGREES
REMARK 500 LEU C 37 CB - CG - CD1 ANGL. DEV. = 10.3 DEGREES
REMARK 500 LEU C 37 CB - CG - CD2 ANGL. DEV. = -11.1 DEGREES
REMARK 500 LYS C 51 CB - CG - CD ANGL. DEV. = -16.1 DEGREES
REMARK 500 LEU C 85 CB - CG - CD1 ANGL. DEV. = -12.7 DEGREES
REMARK 500 LEU C 85 CB - CG - CD2 ANGL. DEV. = 12.3 DEGREES
REMARK 500 ARG C 105 NE - CZ - NH1 ANGL. DEV. = 6.7 DEGREES
REMARK 500 ARG C 105 NE - CZ - NH2 ANGL. DEV. = -6.7 DEGREES
REMARK 500 LEU G 33 CB - CG - CD2 ANGL. DEV. = -12.3 DEGREES
REMARK 500 LYS G 39 CD - CE - NZ ANGL. DEV. = -16.1 DEGREES
REMARK 500 LEU G 57 CB - CG - CD1 ANGL. DEV. = -11.0 DEGREES
REMARK 500 MET G 62 CG - SD - CE ANGL. DEV. = -16.8 DEGREES
REMARK 500 LEU G 66 CB - CG - CD1 ANGL. DEV. = 11.7 DEGREES
REMARK 500 LEU G 66 CB - CG - CD2 ANGL. DEV. = -12.4 DEGREES
REMARK 500 ASN G 79 CB - CA - C ANGL. DEV. = -13.7 DEGREES
REMARK 500 LEU G 81 CB - CG - CD1 ANGL. DEV. = -12.2 DEGREES
REMARK 500 ARG G 105 CD - NE - CZ ANGL. DEV. = -15.8 DEGREES
REMARK 500 ARG G 105 NE - CZ - NH1 ANGL. DEV. = -12.4 DEGREES
REMARK 500 ARG G 105 NE - CZ - NH2 ANGL. DEV. = 8.5 DEGREES
REMARK 500 ARG K 65 CG - CD - NE ANGL. DEV. = 13.6 DEGREES
REMARK 500 ARG K 65 CD - NE - CZ ANGL. DEV. = -16.5 DEGREES
REMARK 500 ARG K 65 NE - CZ - NH1 ANGL. DEV. = -14.0 DEGREES
REMARK 500 ARG K 65 NE - CZ - NH2 ANGL. DEV. = 12.7 DEGREES
REMARK 500 LYS K 70 CB - CA - C ANGL. DEV. = 14.8 DEGREES
REMARK 500 LYS K 70 N - CA - CB ANGL. DEV. = -11.2 DEGREES
REMARK 500 GLN K 71 CB - CG - CD ANGL. DEV. = -15.9 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 GLN A 71 41.15 -104.34
REMARK 500 GLN C 71 69.41 -118.51
REMARK 500 GLN C 72 45.07 32.83
REMARK 500 HIS E 73 19.26 54.49
REMARK 500 GLU G 69 10.60 -57.05
REMARK 500 HIS G 73 4.16 58.21
REMARK 500 CYS G 77 31.74 -142.64
REMARK 500 PRO I 32 -66.83 -29.50
REMARK 500 GLU I 69 -15.89 -49.88
REMARK 500 GLU K 69 36.01 -65.38
REMARK 500 LYS K 70 39.82 -164.42
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: PLANAR GROUPS
REMARK 500
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS
REMARK 500 AN RMSD GREATER THAN THIS VALUE
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI RMS TYPE
REMARK 500 ARG C 29 0.10 SIDE CHAIN
REMARK 500 ARG G 105 0.14 SIDE CHAIN
REMARK 500 ARG K 105 0.12 SIDE CHAIN
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 35T A 201
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 35T C 201
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 35T E 201
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 35T G 201
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 35T I 201
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 35T K 201
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4QO4 RELATED DB: PDB
DBREF 4QOC A 17 111 UNP Q00987 MDM2_HUMAN 17 111
DBREF 4QOC C 17 111 UNP Q00987 MDM2_HUMAN 17 111
DBREF 4QOC E 17 111 UNP Q00987 MDM2_HUMAN 17 111
DBREF 4QOC G 17 111 UNP Q00987 MDM2_HUMAN 17 111
DBREF 4QOC I 17 111 UNP Q00987 MDM2_HUMAN 17 111
DBREF 4QOC K 17 111 UNP Q00987 MDM2_HUMAN 17 111
SEQADV 4QOC GLY A 16 UNP Q00987 EXPRESSION TAG
SEQADV 4QOC GLY C 16 UNP Q00987 EXPRESSION TAG
SEQADV 4QOC GLY E 16 UNP Q00987 EXPRESSION TAG
SEQADV 4QOC GLY G 16 UNP Q00987 EXPRESSION TAG
SEQADV 4QOC GLY I 16 UNP Q00987 EXPRESSION TAG
SEQADV 4QOC GLY K 16 UNP Q00987 EXPRESSION TAG
SEQRES 1 A 96 GLY SER GLN ILE PRO ALA SER GLU GLN GLU THR LEU VAL
SEQRES 2 A 96 ARG PRO LYS PRO LEU LEU LEU LYS LEU LEU LYS SER VAL
SEQRES 3 A 96 GLY ALA GLN LYS ASP THR TYR THR MET LYS GLU VAL LEU
SEQRES 4 A 96 PHE TYR LEU GLY GLN TYR ILE MET THR LYS ARG LEU TYR
SEQRES 5 A 96 ASP GLU LYS GLN GLN HIS ILE VAL TYR CYS SER ASN ASP
SEQRES 6 A 96 LEU LEU GLY ASP LEU PHE GLY VAL PRO SER PHE SER VAL
SEQRES 7 A 96 LYS GLU HIS ARG LYS ILE TYR THR MET ILE TYR ARG ASN
SEQRES 8 A 96 LEU VAL VAL VAL ASN
SEQRES 1 C 96 GLY SER GLN ILE PRO ALA SER GLU GLN GLU THR LEU VAL
SEQRES 2 C 96 ARG PRO LYS PRO LEU LEU LEU LYS LEU LEU LYS SER VAL
SEQRES 3 C 96 GLY ALA GLN LYS ASP THR TYR THR MET LYS GLU VAL LEU
SEQRES 4 C 96 PHE TYR LEU GLY GLN TYR ILE MET THR LYS ARG LEU TYR
SEQRES 5 C 96 ASP GLU LYS GLN GLN HIS ILE VAL TYR CYS SER ASN ASP
SEQRES 6 C 96 LEU LEU GLY ASP LEU PHE GLY VAL PRO SER PHE SER VAL
SEQRES 7 C 96 LYS GLU HIS ARG LYS ILE TYR THR MET ILE TYR ARG ASN
SEQRES 8 C 96 LEU VAL VAL VAL ASN
SEQRES 1 E 96 GLY SER GLN ILE PRO ALA SER GLU GLN GLU THR LEU VAL
SEQRES 2 E 96 ARG PRO LYS PRO LEU LEU LEU LYS LEU LEU LYS SER VAL
SEQRES 3 E 96 GLY ALA GLN LYS ASP THR TYR THR MET LYS GLU VAL LEU
SEQRES 4 E 96 PHE TYR LEU GLY GLN TYR ILE MET THR LYS ARG LEU TYR
SEQRES 5 E 96 ASP GLU LYS GLN GLN HIS ILE VAL TYR CYS SER ASN ASP
SEQRES 6 E 96 LEU LEU GLY ASP LEU PHE GLY VAL PRO SER PHE SER VAL
SEQRES 7 E 96 LYS GLU HIS ARG LYS ILE TYR THR MET ILE TYR ARG ASN
SEQRES 8 E 96 LEU VAL VAL VAL ASN
SEQRES 1 G 96 GLY SER GLN ILE PRO ALA SER GLU GLN GLU THR LEU VAL
SEQRES 2 G 96 ARG PRO LYS PRO LEU LEU LEU LYS LEU LEU LYS SER VAL
SEQRES 3 G 96 GLY ALA GLN LYS ASP THR TYR THR MET LYS GLU VAL LEU
SEQRES 4 G 96 PHE TYR LEU GLY GLN TYR ILE MET THR LYS ARG LEU TYR
SEQRES 5 G 96 ASP GLU LYS GLN GLN HIS ILE VAL TYR CYS SER ASN ASP
SEQRES 6 G 96 LEU LEU GLY ASP LEU PHE GLY VAL PRO SER PHE SER VAL
SEQRES 7 G 96 LYS GLU HIS ARG LYS ILE TYR THR MET ILE TYR ARG ASN
SEQRES 8 G 96 LEU VAL VAL VAL ASN
SEQRES 1 I 96 GLY SER GLN ILE PRO ALA SER GLU GLN GLU THR LEU VAL
SEQRES 2 I 96 ARG PRO LYS PRO LEU LEU LEU LYS LEU LEU LYS SER VAL
SEQRES 3 I 96 GLY ALA GLN LYS ASP THR TYR THR MET LYS GLU VAL LEU
SEQRES 4 I 96 PHE TYR LEU GLY GLN TYR ILE MET THR LYS ARG LEU TYR
SEQRES 5 I 96 ASP GLU LYS GLN GLN HIS ILE VAL TYR CYS SER ASN ASP
SEQRES 6 I 96 LEU LEU GLY ASP LEU PHE GLY VAL PRO SER PHE SER VAL
SEQRES 7 I 96 LYS GLU HIS ARG LYS ILE TYR THR MET ILE TYR ARG ASN
SEQRES 8 I 96 LEU VAL VAL VAL ASN
SEQRES 1 K 96 GLY SER GLN ILE PRO ALA SER GLU GLN GLU THR LEU VAL
SEQRES 2 K 96 ARG PRO LYS PRO LEU LEU LEU LYS LEU LEU LYS SER VAL
SEQRES 3 K 96 GLY ALA GLN LYS ASP THR TYR THR MET LYS GLU VAL LEU
SEQRES 4 K 96 PHE TYR LEU GLY GLN TYR ILE MET THR LYS ARG LEU TYR
SEQRES 5 K 96 ASP GLU LYS GLN GLN HIS ILE VAL TYR CYS SER ASN ASP
SEQRES 6 K 96 LEU LEU GLY ASP LEU PHE GLY VAL PRO SER PHE SER VAL
SEQRES 7 K 96 LYS GLU HIS ARG LYS ILE TYR THR MET ILE TYR ARG ASN
SEQRES 8 K 96 LEU VAL VAL VAL ASN
HET 35T A 201 39
HET 35T C 201 39
HET 35T E 201 39
HET 35T G 201 39
HET 35T I 201 39
HET 35T K 201 39
HETNAM 35T {(3R,5R,6S)-5-(3-CHLOROPHENYL)-6-(4-CHLOROPHENYL)-1-
HETNAM 2 35T [(1S)-1-CYCLOPROPYL-2-(PYRROLIDIN-1-YLSULFONYL)ETHYL]-
HETNAM 3 35T 3-METHYL-2-OXOPIPERIDIN-3-YL}ACETIC ACID
FORMUL 7 35T 6(C29 H34 CL2 N2 O5 S)
FORMUL 13 HOH *603(H2 O)
HELIX 1 1 PRO A 20 GLU A 25 5 6
HELIX 2 2 LYS A 31 LYS A 39 1 9
HELIX 3 3 MET A 50 LYS A 64 1 15
HELIX 4 4 ASP A 68 GLN A 72 5 5
HELIX 5 5 ASP A 80 GLY A 87 1 8
HELIX 6 6 GLU A 95 ARG A 105 1 11
HELIX 7 7 PRO C 20 GLU C 25 5 6
HELIX 8 8 LYS C 31 LYS C 39 1 9
HELIX 9 9 MET C 50 LYS C 64 1 15
HELIX 10 10 ASP C 80 GLY C 87 1 8
HELIX 11 11 GLU C 95 ARG C 105 1 11
HELIX 12 12 PRO E 20 GLU E 25 5 6
HELIX 13 13 LYS E 31 SER E 40 1 10
HELIX 14 14 MET E 50 LYS E 64 1 15
HELIX 15 15 ASP E 80 GLY E 87 1 8
HELIX 16 16 GLU E 95 ARG E 105 1 11
HELIX 17 17 PRO G 20 GLU G 25 5 6
HELIX 18 18 LYS G 31 LYS G 39 1 9
HELIX 19 19 MET G 50 LYS G 64 1 15
HELIX 20 20 ASP G 80 GLY G 87 1 8
HELIX 21 21 GLU G 95 ARG G 105 1 11
HELIX 22 22 PRO I 20 GLU I 25 1 6
HELIX 23 23 LYS I 31 SER I 40 1 10
HELIX 24 24 MET I 50 LYS I 64 1 15
HELIX 25 25 ASP I 80 GLY I 87 1 8
HELIX 26 26 GLU I 95 ARG I 105 1 11
HELIX 27 27 PRO K 20 GLU K 25 5 6
HELIX 28 28 LYS K 31 SER K 40 1 10
HELIX 29 29 MET K 50 LYS K 64 1 15
HELIX 30 30 ASP K 80 GLY K 87 1 8
HELIX 31 31 GLU K 95 ARG K 105 1 11
SHEET 1 A 3 TYR A 48 THR A 49 0
SHEET 2 A 3 LEU A 27 PRO A 30 -1 N VAL A 28 O TYR A 48
SHEET 3 A 3 LEU A 107 VAL A 109 -1 O VAL A 108 N ARG A 29
SHEET 1 B 2 ILE A 74 TYR A 76 0
SHEET 2 B 2 SER A 90 SER A 92 -1 O PHE A 91 N VAL A 75
SHEET 1 C 3 TYR C 48 THR C 49 0
SHEET 2 C 3 LEU C 27 PRO C 30 -1 N VAL C 28 O TYR C 48
SHEET 3 C 3 LEU C 107 VAL C 109 -1 O VAL C 108 N ARG C 29
SHEET 1 D 2 ILE C 74 TYR C 76 0
SHEET 2 D 2 SER C 90 SER C 92 -1 O PHE C 91 N VAL C 75
SHEET 1 E 3 TYR E 48 THR E 49 0
SHEET 2 E 3 LEU E 27 PRO E 30 -1 N VAL E 28 O TYR E 48
SHEET 3 E 3 LEU E 107 VAL E 109 -1 O VAL E 108 N ARG E 29
SHEET 1 F 2 ILE E 74 TYR E 76 0
SHEET 2 F 2 SER E 90 SER E 92 -1 O PHE E 91 N VAL E 75
SHEET 1 G 3 TYR G 48 THR G 49 0
SHEET 2 G 3 LEU G 27 PRO G 30 -1 N VAL G 28 O TYR G 48
SHEET 3 G 3 LEU G 107 VAL G 109 -1 O VAL G 108 N ARG G 29
SHEET 1 H 2 ILE G 74 TYR G 76 0
SHEET 2 H 2 SER G 90 SER G 92 -1 O PHE G 91 N VAL G 75
SHEET 1 I 3 TYR I 48 THR I 49 0
SHEET 2 I 3 LEU I 27 PRO I 30 -1 N VAL I 28 O TYR I 48
SHEET 3 I 3 LEU I 107 VAL I 109 -1 O VAL I 108 N ARG I 29
SHEET 1 J 2 ILE I 74 TYR I 76 0
SHEET 2 J 2 SER I 90 SER I 92 -1 O PHE I 91 N VAL I 75
SHEET 1 K 3 TYR K 48 THR K 49 0
SHEET 2 K 3 LEU K 27 PRO K 30 -1 N VAL K 28 O TYR K 48
SHEET 3 K 3 LEU K 107 VAL K 109 -1 O VAL K 108 N ARG K 29
SHEET 1 L 2 ILE K 74 TYR K 76 0
SHEET 2 L 2 SER K 90 SER K 92 -1 O PHE K 91 N VAL K 75
SITE 1 AC1 18 LEU A 54 GLY A 58 ILE A 61 MET A 62
SITE 2 AC1 18 TYR A 67 VAL A 93 LYS A 94 HIS A 96
SITE 3 AC1 18 ILE A 99 TYR A 100 HOH A 306 HOH A 324
SITE 4 AC1 18 HOH A 337 HOH A 344 HOH A 357 GLN K 18
SITE 5 AC1 18 ARG K 97 LYS K 98
SITE 1 AC2 14 LEU C 54 GLY C 58 ILE C 61 TYR C 67
SITE 2 AC2 14 VAL C 93 LYS C 94 HIS C 96 ILE C 99
SITE 3 AC2 14 TYR C 100 HOH C 314 HOH C 324 HOH C 391
SITE 4 AC2 14 ARG G 97 LYS G 98
SITE 1 AC3 16 ARG C 97 LYS C 98 THR C 101 LEU E 54
SITE 2 AC3 16 LEU E 57 GLY E 58 GLN E 59 ILE E 61
SITE 3 AC3 16 TYR E 67 VAL E 93 LYS E 94 HIS E 96
SITE 4 AC3 16 ILE E 99 TYR E 100 HOH E 311 HOH E 342
SITE 1 AC4 10 GLY G 58 ILE G 61 TYR G 67 VAL G 93
SITE 2 AC4 10 LYS G 94 HIS G 96 ILE G 99 HOH G 312
SITE 3 AC4 10 HOH G 379 HOH G 387
SITE 1 AC5 13 ARG A 97 LYS A 98 THR A 101 LEU I 54
SITE 2 AC5 13 GLY I 58 ILE I 61 TYR I 67 VAL I 93
SITE 3 AC5 13 LYS I 94 HIS I 96 ILE I 99 HOH I 302
SITE 4 AC5 13 HOH I 373
SITE 1 AC6 13 LEU K 54 PHE K 55 GLY K 58 GLN K 59
SITE 2 AC6 13 ILE K 61 PHE K 86 VAL K 93 LYS K 94
SITE 3 AC6 13 HIS K 96 ILE K 99 TYR K 100 HOH K 332
SITE 4 AC6 13 HOH K 363
CRYST1 56.576 98.925 103.921 90.00 90.00 90.00 P 21 21 21 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 0.017675 0.000000 0.000000 0.00000
SCALE2 0.000000 0.010109 0.000000 0.00000
SCALE3 0.000000 0.000000 0.009623 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
