HEADER PEPTIDE BINDING PROTEIN 18-MAR-13 4JOR
TITLE CFTR ASSOCIATED LIGAND (CAL) PDZ DOMAIN BOUND TO HPV18 E6 ONCOPROTEIN
TITLE 2 C-TERMINAL PEPTIDE (RLQRRRETQV)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: GOLGI-ASSOCIATED PDZ AND COILED-COIL MOTIF-CONTAINING
COMPND 3 PROTEIN;
COMPND 4 CHAIN: A, B;
COMPND 5 FRAGMENT: CAL PDZ DOMAIN;
COMPND 6 ENGINEERED: YES;
COMPND 7 MOL_ID: 2;
COMPND 8 MOLECULE: PROTEIN E6;
COMPND 9 CHAIN: C, D;
COMPND 10 FRAGMENT: HPV18 E6 PEPTIDE;
COMPND 11 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: GOPC, CAL, FIG;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3) RIL;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET16B;
SOURCE 11 MOL_ID: 2;
SOURCE 12 SYNTHETIC: YES;
SOURCE 13 ORGANISM_SCIENTIFIC: HUMAN PAPILLOMAVIRUS TYPE 18;
SOURCE 14 ORGANISM_TAXID: 333761
KEYWDS PDZ, CFTR ASSOCIATED LIGAND, CAL, PIST, FIG, HUMAN PAPILLOMAVIRUS
KEYWDS 2 TYPE 18, HPV18, E6 ONCOPROTEIN, PEPTIDE BINDING PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR J.F.AMACHER,D.R.MADDEN
REVDAT 3 20-SEP-23 4JOR 1 REMARK
REVDAT 2 21-OCT-20 4JOR 1 REMARK
REVDAT 1 22-JAN-14 4JOR 0
JRNL AUTH J.F.AMACHER,P.R.CUSHING,L.BROOKS,P.BOISGUERIN,D.R.MADDEN
JRNL TITL STEREOCHEMICAL PREFERENCES MODULATE AFFINITY AND SELECTIVITY
JRNL TITL 2 AMONG FIVE PDZ DOMAINS THAT BIND CFTR: COMPARATIVE
JRNL TITL 3 STRUCTURAL AND SEQUENCE ANALYSES.
JRNL REF STRUCTURE V. 22 82 2014
JRNL REFN ISSN 0969-2126
JRNL PMID 24210758
JRNL DOI 10.1016/J.STR.2013.09.019
REMARK 2
REMARK 2 RESOLUTION. 1.34 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE: 1.7_650)
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 : MLHL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.34
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 19.29
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 2.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 95.2
REMARK 3 NUMBER OF REFLECTIONS : 34482
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.172
REMARK 3 R VALUE (WORKING SET) : 0.171
REMARK 3 FREE R VALUE : 0.181
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.010
REMARK 3 FREE R VALUE TEST SET COUNT : 1729
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 19.2941 - 3.0737 1.00 2894 180 0.1630 0.1577
REMARK 3 2 3.0737 - 2.4413 0.99 2939 90 0.1775 0.1868
REMARK 3 3 2.4413 - 2.1331 0.99 2819 180 0.1635 0.1795
REMARK 3 4 2.1331 - 1.9383 0.98 2774 177 0.1676 0.1659
REMARK 3 5 1.9383 - 1.7995 0.98 2894 89 0.1650 0.1575
REMARK 3 6 1.7995 - 1.6935 0.98 2767 178 0.1659 0.2053
REMARK 3 7 1.6935 - 1.6087 0.97 2724 176 0.1665 0.1977
REMARK 3 8 1.6087 - 1.5387 0.97 2835 89 0.1592 0.1865
REMARK 3 9 1.5387 - 1.4795 0.96 2728 176 0.1650 0.1919
REMARK 3 10 1.4795 - 1.4284 0.96 2680 176 0.1924 0.2139
REMARK 3 11 1.4284 - 1.3838 0.93 2690 84 0.1965 0.2439
REMARK 3 12 1.3838 - 1.3400 0.71 2009 134 0.2397 0.2566
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 0.90
REMARK 3 SHRINKAGE RADIUS : 0.61
REMARK 3 K_SOL : 0.45
REMARK 3 B_SOL : 39.62
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.160
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 17.360
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) : 1.17910
REMARK 3 B22 (A**2) : -1.51590
REMARK 3 B33 (A**2) : 0.33680
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : -1.39670
REMARK 3 B23 (A**2) : 0.00000
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 : 0.007 1541
REMARK 3 ANGLE : 1.166 2084
REMARK 3 CHIRALITY : 0.064 239
REMARK 3 PLANARITY : 0.006 278
REMARK 3 DIHEDRAL : 14.567 594
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 2
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN A AND RESID 284:370
REMARK 3 ORIGIN FOR THE GROUP (A): 30.9115 24.5358 16.0734
REMARK 3 T TENSOR
REMARK 3 T11: 0.0277 T22: 0.0369
REMARK 3 T33: 0.0326 T12: 0.0065
REMARK 3 T13: -0.0031 T23: -0.0031
REMARK 3 L TENSOR
REMARK 3 L11: 0.1502 L22: 0.1843
REMARK 3 L33: 0.2739 L12: -0.0993
REMARK 3 L13: -0.0685 L23: -0.0046
REMARK 3 S TENSOR
REMARK 3 S11: -0.0354 S12: -0.0261 S13: 0.0177
REMARK 3 S21: 0.0129 S22: 0.0095 S23: 0.0032
REMARK 3 S31: -0.0005 S32: -0.0055 S33: 0.0133
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN B AND RESID 284:370
REMARK 3 ORIGIN FOR THE GROUP (A): 26.4675 26.1783 -8.3825
REMARK 3 T TENSOR
REMARK 3 T11: 0.0372 T22: 0.0280
REMARK 3 T33: 0.0357 T12: -0.0139
REMARK 3 T13: -0.0065 T23: -0.0047
REMARK 3 L TENSOR
REMARK 3 L11: 0.1087 L22: 0.2191
REMARK 3 L33: 0.1546 L12: 0.0532
REMARK 3 L13: -0.0351 L23: -0.0294
REMARK 3 S TENSOR
REMARK 3 S11: 0.0399 S12: -0.0141 S13: 0.0000
REMARK 3 S21: 0.0126 S22: -0.0195 S23: 0.0451
REMARK 3 S31: 0.0306 S32: -0.0000 S33: -0.0010
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 4JOR COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 22-MAR-13.
REMARK 100 THE DEPOSITION ID IS D_1000078313.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 29-SEP-12
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : NSLS
REMARK 200 BEAMLINE : X6A
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 : S1 111 CHANNEL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 270
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 34483
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.340
REMARK 200 RESOLUTION RANGE LOW (A) : 19.290
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 7.530
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 94.2
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : 0.05000
REMARK 200 R SYM (I) : 0.03800
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 36.6900
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.34
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.42
REMARK 200 COMPLETENESS FOR SHELL (%) : 77.8
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.24700
REMARK 200 R SYM FOR SHELL (I) : 0.26500
REMARK 200 <I/SIGMA(I)> FOR SHELL : 7.530
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHENIX
REMARK 200 STARTING MODEL: PDB ENTRY 4E34 (CAL PDZ DOMAIN BOUND TO ICAL36
REMARK 200 PEPTIDE)
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 36.06
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.92
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 29% (W/V) POLYETHYLENE GLYCOL (PEG),
REMARK 280 0.075 M SODIUM CHLORIDE, 0.1 M TRIS(HYDROXYMETHYL)AMINOMETHANE
REMARK 280 (TRIS), PH 7.5, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 291K
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 23.98000
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
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, 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: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 720 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 5200 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -3.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, 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 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 ARG D 1
REMARK 465 LEU D 2
REMARK 465 GLN D 3
REMARK 465 ARG D 4
REMARK 465 ARG D 5
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 CYS B 327 CA - CB - SG ANGL. DEV. = 7.9 DEGREES
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 GOL A 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 402
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4JOE RELATED DB: PDB
REMARK 900 RELATED ID: 4JOF RELATED DB: PDB
REMARK 900 RELATED ID: 4JOG RELATED DB: PDB
REMARK 900 RELATED ID: 4JOH RELATED DB: PDB
REMARK 900 RELATED ID: 4JOJ RELATED DB: PDB
REMARK 900 RELATED ID: 4JOK RELATED DB: PDB
REMARK 900 RELATED ID: 4JOP RELATED DB: PDB
DBREF 4JOR A 284 370 UNP Q9HD26 GOPC_HUMAN 284 370
DBREF 4JOR B 284 370 UNP Q9HD26 GOPC_HUMAN 284 370
DBREF 4JOR C 1 10 UNP P06463 VE6_HPV18 149 158
DBREF 4JOR D 1 10 UNP P06463 VE6_HPV18 149 158
SEQRES 1 A 87 GLY PRO ILE ARG LYS VAL LEU LEU LEU LYS GLU ASP HIS
SEQRES 2 A 87 GLU GLY LEU GLY ILE SER ILE THR GLY GLY LYS GLU HIS
SEQRES 3 A 87 GLY VAL PRO ILE LEU ILE SER GLU ILE HIS PRO GLY GLN
SEQRES 4 A 87 PRO ALA ASP ARG CYS GLY GLY LEU HIS VAL GLY ASP ALA
SEQRES 5 A 87 ILE LEU ALA VAL ASN GLY VAL ASN LEU ARG ASP THR LYS
SEQRES 6 A 87 HIS LYS GLU ALA VAL THR ILE LEU SER GLN GLN ARG GLY
SEQRES 7 A 87 GLU ILE GLU PHE GLU VAL VAL TYR VAL
SEQRES 1 B 87 GLY PRO ILE ARG LYS VAL LEU LEU LEU LYS GLU ASP HIS
SEQRES 2 B 87 GLU GLY LEU GLY ILE SER ILE THR GLY GLY LYS GLU HIS
SEQRES 3 B 87 GLY VAL PRO ILE LEU ILE SER GLU ILE HIS PRO GLY GLN
SEQRES 4 B 87 PRO ALA ASP ARG CYS GLY GLY LEU HIS VAL GLY ASP ALA
SEQRES 5 B 87 ILE LEU ALA VAL ASN GLY VAL ASN LEU ARG ASP THR LYS
SEQRES 6 B 87 HIS LYS GLU ALA VAL THR ILE LEU SER GLN GLN ARG GLY
SEQRES 7 B 87 GLU ILE GLU PHE GLU VAL VAL TYR VAL
SEQRES 1 C 10 ARG LEU GLN ARG ARG ARG GLU THR GLN VAL
SEQRES 1 D 10 ARG LEU GLN ARG ARG ARG GLU THR GLN VAL
HET GOL A 401 6
HET GOL A 402 6
HETNAM GOL GLYCEROL
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 5 GOL 2(C3 H8 O3)
FORMUL 7 HOH *258(H2 O)
HELIX 1 1 LYS A 307 GLY A 310 5 4
HELIX 2 2 GLN A 322 GLY A 328 1 7
HELIX 3 3 LYS A 348 GLN A 359 1 12
HELIX 4 4 LYS B 307 GLY B 310 5 4
HELIX 5 5 GLN B 322 GLY B 328 1 7
HELIX 6 6 LYS B 348 GLN B 359 1 12
SHEET 1 A 4 ARG A 287 LYS A 293 0
SHEET 2 A 4 GLY A 361 TYR A 369 -1 O ILE A 363 N LEU A 291
SHEET 3 A 4 ASP A 334 VAL A 339 -1 N ALA A 335 O VAL A 368
SHEET 4 A 4 VAL A 342 ASN A 343 -1 O VAL A 342 N VAL A 339
SHEET 1 B 3 VAL A 311 ILE A 318 0
SHEET 2 B 3 ILE A 301 GLY A 306 -1 N SER A 302 O SER A 316
SHEET 3 B 3 GLU C 7 VAL C 10 -1 O VAL C 10 N ILE A 301
SHEET 1 C 4 ARG B 287 LEU B 292 0
SHEET 2 C 4 GLU B 362 VAL B 368 -1 O PHE B 365 N VAL B 289
SHEET 3 C 4 ALA B 335 VAL B 339 -1 N ALA B 335 O VAL B 368
SHEET 4 C 4 VAL B 342 ASN B 343 -1 O VAL B 342 N VAL B 339
SHEET 1 D 3 VAL B 311 ILE B 318 0
SHEET 2 D 3 ILE B 301 GLY B 306 -1 N SER B 302 O SER B 316
SHEET 3 D 3 GLU D 7 GLN D 9 -1 O THR D 8 N ILE B 303
SITE 1 AC1 4 LYS A 288 LEU A 290 GLU A 364 ASP B 295
SITE 1 AC2 8 GLU A 294 ASP A 295 THR A 304 GLY A 305
SITE 2 AC2 8 HIS A 309 HOH A 544 ARG C 5 ARG C 6
CRYST1 33.205 47.960 52.852 90.00 101.98 90.00 P 1 21 1 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 0.030116 0.000000 0.006390 0.00000
SCALE2 0.000000 0.020851 0.000000 0.00000
SCALE3 0.000000 0.000000 0.019342 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
