HEADER TRANSFERASE/UNKNOWN FUNCTION 16-FEB-13 4J9C
TITLE CRYSTAL STRUCTURE OF THE ABL-SH3 DOMAIN H59Q-N96T MUTANT COMPLEXED
TITLE 2 WITH THE DESIGNED HIGH-AFFINITY PEPTIDE LIGAND P17
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: TYROSINE-PROTEIN KINASE ABL1;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: SH3 DOMAIN (UNP RESIDUES 60-121);
COMPND 5 SYNONYM: ABELSON MURINE LEUKEMIA VIRAL ONCOGENE HOMOLOG 1, ABELSON
COMPND 6 TYROSINE-PROTEIN KINASE 1, PROTO-ONCOGENE C-ABL, P150;
COMPND 7 EC: 2.7.10.2;
COMPND 8 ENGINEERED: YES;
COMPND 9 MUTATION: YES;
COMPND 10 MOL_ID: 2;
COMPND 11 MOLECULE: P17;
COMPND 12 CHAIN: B;
COMPND 13 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: ABL, ABL1, JTK7;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
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: PET15B;
SOURCE 11 MOL_ID: 2;
SOURCE 12 SYNTHETIC: YES
KEYWDS BETA SHANDWICH, SH3 DOMAIN, KINASE, POLY PROLINE RICH MOTIFS,
KEYWDS 2 TRANSFERASE-UNKNOWN FUNCTION COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR A.CAMARA-ARTIGAS
REVDAT 3 20-SEP-23 4J9C 1 REMARK SEQADV LINK
REVDAT 2 15-OCT-14 4J9C 1 AUTHOR
REVDAT 1 29-JAN-14 4J9C 0
JRNL AUTH A.CAMARA-ARTIGAS
JRNL TITL CRYSTAL STRUCTURE OF THE ABL-SH3 DOMAIN H59Q-N96T MUTANT
JRNL TITL 2 COMPLEXED WITH THE DESIGNED HIGH-AFFINITY PEPTIDE LIGAND P17
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH A.CAMARA-ARTIGAS,A.PALENCIA,J.C.MARTINEZ,I.LUQUE,J.A.GAVIRA,
REMARK 1 AUTH 2 J.M.GARCIA-RUIZ
REMARK 1 TITL CRYSTALLIZATION BY CAPILLARY COUNTER-DIFFUSION AND STRUCTURE
REMARK 1 TITL 2 DETERMINATION OF THE N114A MUTANT OF THE SH3 DOMAIN OF ABL
REMARK 1 TITL 3 TYROSINE KINASE COMPLEXED WITH A HIGH-AFFINITY PEPTIDE
REMARK 1 TITL 4 LIGAND.
REMARK 1 REF ACTA CRYSTALLOGR.,SECT.D V. 63 646 2007
REMARK 1 REFN ISSN 0907-4449
REMARK 1 PMID 17452790
REMARK 1 DOI 10.1107/S0907444907011109
REMARK 1 REFERENCE 2
REMARK 1 AUTH A.PALENCIA,A.CAMARA-ARTIGAS,M.T.PISABARRO,J.C.MARTINEZ,
REMARK 1 AUTH 2 I.LUQUE
REMARK 1 TITL ROLE OF INTERFACIAL WATER MOLECULES IN PROLINE-RICH LIGAND
REMARK 1 TITL 2 RECOGNITION BY THE SRC HOMOLOGY 3 DOMAIN OF ABL.
REMARK 1 REF J.BIOL.CHEM. V. 285 2823 2010
REMARK 1 REFN ISSN 0021-9258
REMARK 1 PMID 19906645
REMARK 1 DOI 10.1074/JBC.M109.048033
REMARK 2
REMARK 2 RESOLUTION. 1.05 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.8.1_1168
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,
REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,
REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,
REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON,
REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,
REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT
REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.05
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 16.75
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.6
REMARK 3 NUMBER OF REFLECTIONS : 29561
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.147
REMARK 3 R VALUE (WORKING SET) : 0.146
REMARK 3 FREE R VALUE : 0.162
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.080
REMARK 3 FREE R VALUE TEST SET COUNT : 1500
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 16.7558 - 2.8950 0.77 2074 66 0.1948 0.2325
REMARK 3 2 2.8950 - 2.2997 1.00 2647 128 0.1631 0.1569
REMARK 3 3 2.2997 - 2.0096 1.00 2643 136 0.1370 0.1246
REMARK 3 4 2.0096 - 1.8261 1.00 2611 136 0.1250 0.1367
REMARK 3 5 1.8261 - 1.6953 1.00 2680 123 0.1212 0.1741
REMARK 3 6 1.6953 - 1.5955 1.00 2592 154 0.1175 0.1232
REMARK 3 7 1.5955 - 1.5156 1.00 2621 180 0.1239 0.1704
REMARK 3 8 1.5156 - 1.4497 1.00 2655 133 0.1163 0.1416
REMARK 3 9 1.4497 - 1.3939 1.00 2624 158 0.1170 0.1460
REMARK 3 10 1.3939 - 1.3458 1.00 2584 133 0.1165 0.1421
REMARK 3 11 1.3458 - 1.3038 1.00 2693 134 0.1262 0.1526
REMARK 3 12 1.3038 - 1.2665 1.00 2601 152 0.1283 0.1899
REMARK 3 13 1.2665 - 1.2332 1.00 2635 170 0.1319 0.1904
REMARK 3 14 1.2332 - 1.2031 1.00 2606 127 0.1332 0.1545
REMARK 3 15 1.2031 - 1.1758 1.00 2623 147 0.1309 0.1337
REMARK 3 16 1.1758 - 1.1507 1.00 2616 176 0.1319 0.1849
REMARK 3 17 1.1507 - 1.1277 1.00 2633 119 0.1412 0.2199
REMARK 3 18 1.1277 - 1.1065 1.00 2614 140 0.1564 0.1502
REMARK 3 19 1.1065 - 1.0867 1.00 2632 152 0.1730 0.1802
REMARK 3 20 1.0867 - 1.0683 0.99 2612 130 0.1920 0.2439
REMARK 3 21 1.0683 - 1.0510 0.98 2575 125 0.2298 0.2666
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) : 0.080
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 13.520
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 8.30
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 14.95
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 : 0.008 569
REMARK 3 ANGLE : 1.237 772
REMARK 3 CHIRALITY : 0.070 83
REMARK 3 PLANARITY : 0.008 99
REMARK 3 DIHEDRAL : 14.422 209
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 4J9C COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 18-FEB-13.
REMARK 100 THE DEPOSITION ID IS D_1000077759.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 08-APR-11
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 5.6
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : ID14-4
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97
REMARK 200 MONOCHROMATOR : CHANNEL CUT ESRF MONOCHROMATOR
REMARK 200 AND TORODIAL FOCUSING MIRROR
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : NULL
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : SCALA 0.1.30
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 29561
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.051
REMARK 200 RESOLUTION RANGE LOW (A) : 42.995
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.8
REMARK 200 DATA REDUNDANCY : 8.300
REMARK 200 R MERGE (I) : 0.04000
REMARK 200 R SYM (I) : 0.04000
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 28.7000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.05
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.11
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.1
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.47200
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 4.610
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: 2O88
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 38.69
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.01
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.5 M AMS, 5% PEG 200, 20 MM LICL, 0.1
REMARK 280 M ACONA , PH 5.6, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 298K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 32 1 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+2/3
REMARK 290 3555 -X+Y,-X,Z+1/3
REMARK 290 4555 -Y,-X,-Z+1/3
REMARK 290 5555 -X+Y,Y,-Z+2/3
REMARK 290 6555 X,X-Y,-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 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 30.27333
REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 15.13667
REMARK 290 SMTRY1 4 0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 4 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 15.13667
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 30.27333
REMARK 290 SMTRY1 6 0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 6 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 6 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: DIMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, 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 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375 HOH A 303 LIES ON A SPECIAL POSITION.
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 MET A 59
REMARK 465 GLU A 60
REMARK 465 ASN A 61
REMARK 465 ASP A 62
REMARK 465 SER A 121
REMARK 480
REMARK 480 ZERO OCCUPANCY ATOM
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 480 M RES C SSEQI ATOMS
REMARK 480 ASN A 78 OD1
REMARK 480 ARG A 89 NH1
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PGE A 201
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG A 202
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR CHAIN B OF P17
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2O88 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE N114A MUTANT OF ABL-SH3 DOMAIN COMPLEXED
REMARK 900 WITH A DESIGNED HIGH-AFFINITY PEPTIDE LIGAND: IMPLICATIONS FOR SH3-
REMARK 900 LIGAND INTERACTIONS
REMARK 900 RELATED ID: 3EG0 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE N114T MUTANT OF ABL-SH3 DOMAIN
REMARK 900 RELATED ID: 3EG1 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE N114Q MUTANT OF ABL-SH3 DOMAIN COMPLEXED
REMARK 900 WITH A DESIGNED HIGH-AFFINITY PEPTIDE LIGAND: IMPLICATIONS FOR SH3-
REMARK 900 LIGAND INTERACTIONS
REMARK 900 RELATED ID: 3EG2 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE N114Q MUTANT OF ABL-SH3 DOMAIN
REMARK 900 RELATED ID: 3EG3 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE N114A MUTANT OF ABL-SH3 DOMAIN
REMARK 900 RELATED ID: 3EGU RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE N114A MUTANT OF ABL-SH3 DOMAIN
REMARK 900 RELATED ID: 4J9B RELATED DB: PDB
DBREF 4J9C A 60 121 UNP P00519 ABL1_HUMAN 60 121
DBREF 4J9C B 0 10 PDB 4J9C 4J9C 0 10
SEQADV 4J9C MET A 59 UNP P00519 INITIATING METHIONINE
SEQADV 4J9C GLN A 95 UNP P00519 HIS 95 ENGINEERED MUTATION
SEQADV 4J9C THR A 96 UNP P00519 ASN 96 ENGINEERED MUTATION
SEQRES 1 A 63 MET GLU ASN ASP PRO ASN LEU PHE VAL ALA LEU TYR ASP
SEQRES 2 A 63 PHE VAL ALA SER GLY ASP ASN THR LEU SER ILE THR LYS
SEQRES 3 A 63 GLY GLU LYS LEU ARG VAL LEU GLY TYR ASN GLN THR GLY
SEQRES 4 A 63 GLU TRP CYS GLU ALA GLN THR LYS ASN GLY GLN GLY TRP
SEQRES 5 A 63 VAL PRO SER ASN TYR ILE THR PRO VAL ASN SER
SEQRES 1 B 11 ACE ALA PRO THR TYR SER PRO PRO LEU PRO PRO
HET ACE B 0 3
HET PGE A 201 24
HET PEG A 202 17
HETNAM ACE ACETYL GROUP
HETNAM PGE TRIETHYLENE GLYCOL
HETNAM PEG DI(HYDROXYETHYL)ETHER
FORMUL 2 ACE C2 H4 O
FORMUL 3 PGE C6 H14 O4
FORMUL 4 PEG C4 H10 O3
FORMUL 5 HOH *80(H2 O)
SHEET 1 A 5 GLY A 107 PRO A 112 0
SHEET 2 A 5 TRP A 99 THR A 104 -1 N CYS A 100 O VAL A 111
SHEET 3 A 5 LYS A 87 TYR A 93 -1 N LEU A 91 O GLU A 101
SHEET 4 A 5 LEU A 65 ALA A 68 -1 N PHE A 66 O LEU A 88
SHEET 5 A 5 ILE A 116 PRO A 118 -1 O THR A 117 N VAL A 67
LINK C ACE B 0 N ALA B 1 1555 1555 1.33
SITE 1 AC1 7 TYR A 70 SER A 113 ASN A 114 ILE A 116
SITE 2 AC1 7 HOH A 330 PRO B 9 PRO B 10
SITE 1 AC2 4 LEU A 91 GLU A 101 ASN A 106 HOH A 332
SITE 1 AC3 32 TYR A 70 SER A 75 ASP A 77 LYS A 84
SITE 2 AC3 32 ASN A 94 GLU A 98 TRP A 99 LYS A 105
SITE 3 AC3 32 ASN A 106 TRP A 110 PRO A 112 ASN A 114
SITE 4 AC3 32 TYR A 115 PGE A 201 HOH A 308 HOH A 312
SITE 5 AC3 32 HOH A 316 HOH A 354 HOH A 364 HOH B 101
SITE 6 AC3 32 HOH B 102 HOH B 103 HOH B 104 HOH B 105
SITE 7 AC3 32 HOH B 106 HOH B 107 HOH B 108 HOH B 109
SITE 8 AC3 32 HOH B 111 HOH B 113 HOH B 115 HOH B 116
CRYST1 49.646 49.646 45.410 90.00 90.00 120.00 P 32 1 2 6
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 0.020143 0.011629 0.000000 0.00000
SCALE2 0.000000 0.023259 0.000000 0.00000
SCALE3 0.000000 0.000000 0.022022 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
