HEADER PROTEIN BINDING 22-APR-11 3RNJ
TITLE CRYSTAL STRUCTURE OF THE SH3 DOMAIN FROM IRSP53 (BAIAP2)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: BRAIN-SPECIFIC ANGIOGENESIS INHIBITOR 1-ASSOCIATED PROTEIN
COMPND 3 2;
COMPND 4 CHAIN: A;
COMPND 5 FRAGMENT: SH3 DOMAIN, UNP RESIDUES 375-436;
COMPND 6 SYNONYM: BAI-ASSOCIATED PROTEIN 2, BAI1-ASSOCIATED PROTEIN 2, PROTEIN
COMPND 7 BAP2, FAS LIGAND-ASSOCIATED FACTOR 3, FLAF3, INSULIN RECEPTOR
COMPND 8 SUBSTRATE P53/P58, IRS-58, IRSP53/58, INSULIN RECEPTOR SUBSTRATE
COMPND 9 PROTEIN OF 53 KDA, IRSP53, INSULIN RECEPTOR SUBSTRATE P53;
COMPND 10 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: BAIAP2;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21 (DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PGEX-6P1
KEYWDS STRUCTURAL GENOMICS, STRUCTURAL GENOMICS CONSORTIUM, SGC, BETA
KEYWDS 2 BARREL, PROTEIN INTERACTION DOMAIN, PROLINE-RICH MOTIFS, PROTEIN
KEYWDS 3 BINDING
EXPDTA X-RAY DIFFRACTION
AUTHOR P.C.SIMISTER,M.BARILARI,J.R.C.MUNIZ,L.DENTE,S.KNAPP,F.VON DELFT,
AUTHOR 2 P.FILIPPAKOPOULOS,M.VOLLMAR,A.CHAIKUAD,J.RAYNOR,A.TREGUBOVA,
AUTHOR 3 C.H.ARROWSMITH,A.M.EDWARDS,J.WEIGELT,C.BOUNTRA,S.M.FELLER,STRUCTURAL
AUTHOR 4 GENOMICS CONSORTIUM (SGC)
REVDAT 4 13-SEP-23 3RNJ 1 REMARK SEQADV
REVDAT 3 24-JAN-18 3RNJ 1 AUTHOR
REVDAT 2 05-DEC-12 3RNJ 1 AUTHOR JRNL VERSN
REVDAT 1 04-MAY-11 3RNJ 0
JRNL AUTH P.C.SIMISTER,M.BARILARI,J.R.C.MUNIZ,L.DENTE,S.KNAPP,
JRNL AUTH 2 F.VON DELFT,P.FILIPPAKOPOULOS,M.VOLLMAR,A.CHAIKUAD,J.RAYNOR,
JRNL AUTH 3 A.TREGUBOVA,C.H.ARROWSMITH,A.M EDWARDS,J.WEIGELT,C.BOUNTRA,
JRNL AUTH 4 S.M.FELLER,STRUCTURAL GENOMICS CONSORTIUM (SGC)
JRNL TITL CRYSTAL STRUCTURE OF THE SH3 DOMAIN FROM IRSP53 (BAIAP2)
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 1.50 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 : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.50
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 23.20
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.7
REMARK 3 NUMBER OF REFLECTIONS : 10700
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.198
REMARK 3 R VALUE (WORKING SET) : 0.197
REMARK 3 FREE R VALUE : 0.219
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.010
REMARK 3 FREE R VALUE TEST SET COUNT : 536
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 23.1962 - 2.3805 1.00 2658 140 0.1652 0.1745
REMARK 3 2 2.3805 - 1.8898 1.00 2528 133 0.1813 0.2141
REMARK 3 3 1.8898 - 1.6510 1.00 2506 132 0.2246 0.2424
REMARK 3 4 1.6510 - 1.5000 1.00 2472 131 0.3311 0.3854
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.65
REMARK 3 K_SOL : 0.40
REMARK 3 B_SOL : 40.01
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.230
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 25.130
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 17.60
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -4.16560
REMARK 3 B22 (A**2) : -7.88720
REMARK 3 B33 (A**2) : 12.05280
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 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 : 0.004 604
REMARK 3 ANGLE : 0.944 813
REMARK 3 CHIRALITY : 0.054 80
REMARK 3 PLANARITY : 0.004 106
REMARK 3 DIHEDRAL : 18.548 243
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 5
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN 'A' AND (RESSEQ 370:376)
REMARK 3 ORIGIN FOR THE GROUP (A): 22.0209 -4.5968 17.0634
REMARK 3 T TENSOR
REMARK 3 T11: 0.1268 T22: 0.1445
REMARK 3 T33: -0.0042 T12: -0.0676
REMARK 3 T13: 0.0020 T23: 0.0583
REMARK 3 L TENSOR
REMARK 3 L11: 0.0545 L22: 0.1106
REMARK 3 L33: 0.0550 L12: 0.0774
REMARK 3 L13: -0.0546 L23: -0.0778
REMARK 3 S TENSOR
REMARK 3 S11: 0.0581 S12: 0.0293 S13: 0.0149
REMARK 3 S21: -0.0601 S22: -0.0528 S23: -0.0296
REMARK 3 S31: 0.0054 S32: -0.0044 S33: -0.0104
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN 'A' AND (RESSEQ 377:396)
REMARK 3 ORIGIN FOR THE GROUP (A): 10.6820 1.9543 -1.3668
REMARK 3 T TENSOR
REMARK 3 T11: 0.0785 T22: 0.0710
REMARK 3 T33: 0.0701 T12: -0.0087
REMARK 3 T13: -0.0052 T23: -0.0041
REMARK 3 L TENSOR
REMARK 3 L11: 0.1794 L22: 0.3360
REMARK 3 L33: 0.1893 L12: -0.0599
REMARK 3 L13: 0.0409 L23: -0.0005
REMARK 3 S TENSOR
REMARK 3 S11: -0.0538 S12: -0.0056 S13: -0.0092
REMARK 3 S21: 0.0078 S22: 0.0201 S23: 0.0382
REMARK 3 S31: -0.0109 S32: -0.0385 S33: 0.0093
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN 'A' AND (RESSEQ 397:409)
REMARK 3 ORIGIN FOR THE GROUP (A): 12.5152 -1.1787 4.2267
REMARK 3 T TENSOR
REMARK 3 T11: 0.0169 T22: 0.0206
REMARK 3 T33: 0.0423 T12: -0.0163
REMARK 3 T13: -0.0052 T23: -0.0037
REMARK 3 L TENSOR
REMARK 3 L11: 0.0642 L22: 0.0279
REMARK 3 L33: 0.0605 L12: 0.0307
REMARK 3 L13: -0.0140 L23: 0.0085
REMARK 3 S TENSOR
REMARK 3 S11: 0.0359 S12: -0.0360 S13: -0.0054
REMARK 3 S21: 0.0385 S22: -0.0120 S23: 0.0004
REMARK 3 S31: 0.0107 S32: -0.0372 S33: -0.0072
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN 'A' AND (RESSEQ 410:422)
REMARK 3 ORIGIN FOR THE GROUP (A): 13.2834 2.9080 3.5960
REMARK 3 T TENSOR
REMARK 3 T11: 0.0270 T22: 0.0059
REMARK 3 T33: 0.0364 T12: 0.0087
REMARK 3 T13: 0.0040 T23: 0.0014
REMARK 3 L TENSOR
REMARK 3 L11: 0.3341 L22: 0.4016
REMARK 3 L33: 0.2573 L12: 0.0347
REMARK 3 L13: 0.0668 L23: 0.0180
REMARK 3 S TENSOR
REMARK 3 S11: -0.0129 S12: -0.0399 S13: -0.0210
REMARK 3 S21: 0.0235 S22: 0.0044 S23: -0.0342
REMARK 3 S31: 0.0221 S32: -0.0651 S33: 0.0043
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: CHAIN 'A' AND (RESSEQ 423:436)
REMARK 3 ORIGIN FOR THE GROUP (A): 9.3937 -1.0022 3.7239
REMARK 3 T TENSOR
REMARK 3 T11: 0.0236 T22: 0.0168
REMARK 3 T33: 0.0616 T12: 0.0068
REMARK 3 T13: -0.0033 T23: 0.0105
REMARK 3 L TENSOR
REMARK 3 L11: 0.1897 L22: 0.3775
REMARK 3 L33: 0.1264 L12: -0.0008
REMARK 3 L13: 0.0159 L23: -0.0065
REMARK 3 S TENSOR
REMARK 3 S11: -0.0182 S12: -0.0162 S13: -0.0348
REMARK 3 S21: -0.0127 S22: 0.0320 S23: -0.0879
REMARK 3 S31: -0.0001 S32: -0.0247 S33: -0.0030
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 3RNJ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 25-APR-11.
REMARK 100 THE DEPOSITION ID IS D_1000065150.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 27-OCT-10
REMARK 200 TEMPERATURE (KELVIN) : 100.0
REMARK 200 PH : 8.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : DIAMOND
REMARK 200 BEAMLINE : I02
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9795
REMARK 200 MONOCHROMATOR : DOUBLE CRYSTAL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 10716
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.500
REMARK 200 RESOLUTION RANGE LOW (A) : 31.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 200 DATA REDUNDANCY : 4.600
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 9.7000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.50
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.52
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 4.50
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.430
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: 1BG5, 1Y6E, 1GNE, 1DUG AND 3QMZ
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 42.06
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.12
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2M AMMONIUM ACETATE, 0.1M TRIS-HCL
REMARK 280 PH 8.5, 30% ISOPROPANOL, VAPOR DIFFUSION, SITTING DROP,
REMARK 280 TEMPERATURE 298K
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 14.98000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 29.05500
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 18.32000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 29.05500
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 14.98000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 18.32000
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 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 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDT A 1
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 437
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 2
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 3
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IPA A 438
DBREF 3RNJ A 375 436 UNP Q9UQB8 BAIP2_HUMAN 375 436
SEQADV 3RNJ GLY A 370 UNP Q9UQB8 EXPRESSION TAG
SEQADV 3RNJ PRO A 371 UNP Q9UQB8 EXPRESSION TAG
SEQADV 3RNJ LEU A 372 UNP Q9UQB8 EXPRESSION TAG
SEQADV 3RNJ GLY A 373 UNP Q9UQB8 EXPRESSION TAG
SEQADV 3RNJ SER A 374 UNP Q9UQB8 EXPRESSION TAG
SEQRES 1 A 67 GLY PRO LEU GLY SER GLY ARG MET ARG VAL LYS ALA ILE
SEQRES 2 A 67 PHE SER HIS ALA ALA GLY ASP ASN SER THR LEU LEU SER
SEQRES 3 A 67 PHE LYS GLU GLY ASP LEU ILE THR LEU LEU VAL PRO GLU
SEQRES 4 A 67 ALA ARG ASP GLY TRP HIS TYR GLY GLU SER GLU LYS THR
SEQRES 5 A 67 LYS MET ARG GLY TRP PHE PRO PHE SER TYR THR ARG VAL
SEQRES 6 A 67 LEU ASP
HET EDT A 1 20
HET EDO A 437 4
HET EDO A 2 4
HET EDO A 3 4
HET IPA A 438 4
HETNAM EDT {[-(BIS-CARBOXYMETHYL-AMINO)-ETHYL]-CARBOXYMETHYL-
HETNAM 2 EDT AMINO}-ACETIC ACID
HETNAM EDO 1,2-ETHANEDIOL
HETNAM IPA ISOPROPYL ALCOHOL
HETSYN EDO ETHYLENE GLYCOL
HETSYN IPA 2-PROPANOL
FORMUL 2 EDT C10 H16 N2 O8
FORMUL 3 EDO 3(C2 H6 O2)
FORMUL 6 IPA C3 H8 O
FORMUL 7 HOH *86(H2 O)
SHEET 1 A 5 ARG A 424 PRO A 428 0
SHEET 2 A 5 TRP A 413 SER A 418 -1 N HIS A 414 O PHE A 427
SHEET 3 A 5 LEU A 401 LEU A 404 -1 N THR A 403 O GLU A 417
SHEET 4 A 5 ARG A 378 ALA A 381 -1 N VAL A 379 O ILE A 402
SHEET 5 A 5 THR A 432 VAL A 434 -1 O ARG A 433 N LYS A 380
SITE 1 AC1 17 EDO A 3 HOH A 25 HOH A 26 HOH A 34
SITE 2 AC1 17 HOH A 35 HOH A 63 HOH A 74 LYS A 380
SITE 3 AC1 17 PHE A 383 LYS A 420 LYS A 422 SER A 430
SITE 4 AC1 17 TYR A 431 ARG A 433 LEU A 435 ASP A 436
SITE 5 AC1 17 EDO A 437
SITE 1 AC2 6 EDT A 1 HOH A 25 HOH A 74 SER A 391
SITE 2 AC2 6 THR A 392 TYR A 431
SITE 1 AC3 3 HOH A 13 PHE A 429 THR A 432
SITE 1 AC4 4 EDT A 1 GLY A 399 LEU A 401 SER A 430
SITE 1 AC5 3 HOH A 29 HOH A 49 TRP A 426
CRYST1 29.960 36.640 58.110 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 0.033378 0.000000 0.000000 0.00000
SCALE2 0.000000 0.027293 0.000000 0.00000
SCALE3 0.000000 0.000000 0.017209 0.00000
(ATOM LINES ARE NOT SHOWN.)
END