HEADER HYDROLASE/HYDROLASE INHIBITOR 03-OCT-14 4WKS
TITLE N-ALKYLBORONIC ACID INHIBITORS REVEAL DETERMINANTS OF LIGAND
TITLE 2 SPECIFICITY IN THE QUORUM-QUENCHING AND SIDEROPHORE BIOSYNTHETIC
TITLE 3 ENZYME PVDQ
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ACYL-HOMOSERINE LACTONE ACYLASE PVDQ;
COMPND 3 CHAIN: C;
COMPND 4 FRAGMENT: UNP RESIDUES 217-762;
COMPND 5 SYNONYM: ACYL-HSL ACYLASE PVDQ;
COMPND 6 EC: 3.5.1.97;
COMPND 7 ENGINEERED: YES;
COMPND 8 MOL_ID: 2;
COMPND 9 MOLECULE: ACYL-HOMOSERINE LACTONE ACYLASE PVDQ;
COMPND 10 CHAIN: A;
COMPND 11 FRAGMENT: UNP RESIDUES 28-192;
COMPND 12 SYNONYM: ACYL-HSL ACYLASE PVDQ;
COMPND 13 EC: 3.5.1.97;
COMPND 14 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: PSEUDOMONAS AERUGINOSA;
SOURCE 3 ORGANISM_TAXID: 208964;
SOURCE 4 STRAIN: ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228;
SOURCE 5 GENE: PVDQ, QSC112, PA2385;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 MOL_ID: 2;
SOURCE 9 ORGANISM_SCIENTIFIC: PSEUDOMONAS AERUGINOSA;
SOURCE 10 ORGANISM_TAXID: 208964;
SOURCE 11 STRAIN: ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228;
SOURCE 12 GENE: PVDQ, QSC112, PA2385;
SOURCE 13 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 14 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS PVDQ, N-ALKYLBORONIC ACID, HYDROLASE-HYDROLASE INHIBITOR COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR R.WU,D.K.CLEVENGER,W.FAST,D.LIU
REVDAT 2 27-SEP-23 4WKS 1 SOURCE KEYWDS JRNL REMARK
REVDAT 1 12-NOV-14 4WKS 0
JRNL AUTH K.D.CLEVENGER,R.WU,D.LIU,W.FAST
JRNL TITL N-ALKYLBORONIC ACID INHIBITORS REVEAL DETERMINANTS OF LIGAND
JRNL TITL 2 SPECIFICITY IN THE QUORUM-QUENCHING AND SIDEROPHORE
JRNL TITL 3 BIOSYNTHETIC ENZYME PVDQ.
JRNL REF BIOCHEMISTRY V. 53 6679 2014
JRNL REFN ISSN 0006-2960
JRNL PMID 25290020
JRNL DOI 10.1021/BI501086S
REMARK 2
REMARK 2 RESOLUTION. 1.63 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE: 1.9_1678)
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) : 1.63
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 42.59
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.4
REMARK 3 NUMBER OF REFLECTIONS : 119501
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.159
REMARK 3 R VALUE (WORKING SET) : 0.158
REMARK 3 FREE R VALUE : 0.190
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.010
REMARK 3 FREE R VALUE TEST SET COUNT : 5988
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 42.6011 - 5.0602 0.94 3819 186 0.1495 0.1886
REMARK 3 2 5.0602 - 4.0174 0.97 3780 197 0.1264 0.1497
REMARK 3 3 4.0174 - 3.5098 0.98 3805 179 0.1360 0.1678
REMARK 3 4 3.5098 - 3.1891 0.98 3801 211 0.1452 0.1758
REMARK 3 5 3.1891 - 2.9605 0.99 3756 209 0.1493 0.1967
REMARK 3 6 2.9605 - 2.7860 0.99 3793 209 0.1530 0.1793
REMARK 3 7 2.7860 - 2.6465 0.99 3772 206 0.1526 0.1878
REMARK 3 8 2.6465 - 2.5313 1.00 3804 214 0.1524 0.1817
REMARK 3 9 2.5313 - 2.4339 1.00 3805 219 0.1531 0.1837
REMARK 3 10 2.4339 - 2.3499 1.00 3783 205 0.1463 0.1651
REMARK 3 11 2.3499 - 2.2764 1.00 3859 157 0.1445 0.1875
REMARK 3 12 2.2764 - 2.2114 1.00 3766 205 0.1424 0.1742
REMARK 3 13 2.2114 - 2.1532 1.00 3758 226 0.1522 0.1800
REMARK 3 14 2.1532 - 2.1006 1.00 3801 192 0.1557 0.1943
REMARK 3 15 2.1006 - 2.0529 1.00 3799 174 0.1577 0.1842
REMARK 3 16 2.0529 - 2.0092 1.00 3789 207 0.1591 0.2004
REMARK 3 17 2.0092 - 1.9690 1.00 3802 188 0.1614 0.1683
REMARK 3 18 1.9690 - 1.9318 1.00 3760 235 0.1621 0.2249
REMARK 3 19 1.9318 - 1.8973 1.00 3766 193 0.1764 0.1943
REMARK 3 20 1.8973 - 1.8652 1.00 3785 215 0.1800 0.2487
REMARK 3 21 1.8652 - 1.8351 1.00 3810 181 0.1952 0.2255
REMARK 3 22 1.8351 - 1.8069 1.00 3761 208 0.2011 0.2397
REMARK 3 23 1.8069 - 1.7803 1.00 3738 188 0.2092 0.2391
REMARK 3 24 1.7803 - 1.7552 1.00 3792 185 0.2241 0.2602
REMARK 3 25 1.7552 - 1.7315 1.00 3789 193 0.2289 0.2720
REMARK 3 26 1.7315 - 1.7090 1.00 3765 207 0.2260 0.2440
REMARK 3 27 1.7090 - 1.6876 1.00 3783 201 0.2428 0.2596
REMARK 3 28 1.6876 - 1.6673 1.00 3780 184 0.2595 0.2992
REMARK 3 29 1.6673 - 1.6479 1.00 3722 222 0.2692 0.2841
REMARK 3 30 1.6479 - 1.6290 0.99 3770 192 0.2818 0.3135
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) : 0.180
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 18.820
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 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 : 0.019 5738
REMARK 3 ANGLE : 1.707 7819
REMARK 3 CHIRALITY : 0.108 836
REMARK 3 PLANARITY : 0.010 1049
REMARK 3 DIHEDRAL : 14.338 2146
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 7
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN 'C' AND (RESID 218 THROUGH 528 )
REMARK 3 ORIGIN FOR THE GROUP (A): 16.3103 32.9626 6.9336
REMARK 3 T TENSOR
REMARK 3 T11: 0.1199 T22: 0.1323
REMARK 3 T33: 0.1463 T12: -0.0222
REMARK 3 T13: 0.0067 T23: 0.0064
REMARK 3 L TENSOR
REMARK 3 L11: 0.8105 L22: 0.4630
REMARK 3 L33: 0.7025 L12: -0.2871
REMARK 3 L13: 0.2832 L23: 0.0586
REMARK 3 S TENSOR
REMARK 3 S11: -0.0050 S12: -0.0815 S13: -0.0480
REMARK 3 S21: -0.0063 S22: 0.0031 S23: 0.1012
REMARK 3 S31: 0.0998 S32: -0.1193 S33: -0.0070
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN 'C' AND (RESID 529 THROUGH 764 )
REMARK 3 ORIGIN FOR THE GROUP (A): 33.0867 17.5983 -6.0098
REMARK 3 T TENSOR
REMARK 3 T11: 0.2951 T22: 0.1629
REMARK 3 T33: 0.1959 T12: 0.0432
REMARK 3 T13: -0.0043 T23: -0.0042
REMARK 3 L TENSOR
REMARK 3 L11: 1.1968 L22: 1.5467
REMARK 3 L33: 2.0013 L12: 0.4739
REMARK 3 L13: 0.8011 L23: 0.6187
REMARK 3 S TENSOR
REMARK 3 S11: -0.0357 S12: 0.1866 S13: -0.1059
REMARK 3 S21: -0.2956 S22: 0.1094 S23: 0.1114
REMARK 3 S31: 0.3031 S32: 0.2304 S33: -0.0775
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 30 THROUGH 49 )
REMARK 3 ORIGIN FOR THE GROUP (A): 43.6711 33.0530 22.5919
REMARK 3 T TENSOR
REMARK 3 T11: 0.1593 T22: 0.2261
REMARK 3 T33: 0.1410 T12: 0.0444
REMARK 3 T13: -0.0228 T23: 0.0045
REMARK 3 L TENSOR
REMARK 3 L11: 3.2502 L22: 4.1274
REMARK 3 L33: 6.6318 L12: -2.5976
REMARK 3 L13: -2.2831 L23: 3.7419
REMARK 3 S TENSOR
REMARK 3 S11: -0.2027 S12: -0.2264 S13: 0.0592
REMARK 3 S21: 0.2914 S22: 0.2190 S23: -0.1575
REMARK 3 S31: 0.3001 S32: 0.4386 S33: -0.0361
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 50 THROUGH 106 )
REMARK 3 ORIGIN FOR THE GROUP (A): 34.6634 46.1571 4.1609
REMARK 3 T TENSOR
REMARK 3 T11: 0.0939 T22: 0.0997
REMARK 3 T33: 0.1285 T12: -0.0309
REMARK 3 T13: 0.0025 T23: -0.0215
REMARK 3 L TENSOR
REMARK 3 L11: 1.9937 L22: 1.5162
REMARK 3 L33: 3.7539 L12: -1.0677
REMARK 3 L13: 1.7927 L23: -1.7469
REMARK 3 S TENSOR
REMARK 3 S11: -0.0101 S12: 0.0934 S13: 0.1059
REMARK 3 S21: -0.0817 S22: -0.0484 S23: -0.0863
REMARK 3 S31: -0.0121 S32: 0.1677 S33: 0.0424
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 107 THROUGH 120 )
REMARK 3 ORIGIN FOR THE GROUP (A): 22.1878 51.3447 15.5804
REMARK 3 T TENSOR
REMARK 3 T11: 0.1955 T22: 0.1888
REMARK 3 T33: 0.2280 T12: 0.0419
REMARK 3 T13: -0.0037 T23: -0.0582
REMARK 3 L TENSOR
REMARK 3 L11: 1.5193 L22: 7.9529
REMARK 3 L33: 3.5387 L12: 0.7504
REMARK 3 L13: -0.4114 L23: -5.2982
REMARK 3 S TENSOR
REMARK 3 S11: -0.0553 S12: -0.1991 S13: 0.0871
REMARK 3 S21: 0.5213 S22: 0.1493 S23: 0.3111
REMARK 3 S31: -0.8164 S32: -0.4220 S33: -0.1056
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 121 THROUGH 158 )
REMARK 3 ORIGIN FOR THE GROUP (A): 42.2581 46.6196 13.5963
REMARK 3 T TENSOR
REMARK 3 T11: 0.1277 T22: 0.1676
REMARK 3 T33: 0.1624 T12: -0.0118
REMARK 3 T13: -0.0279 T23: -0.0426
REMARK 3 L TENSOR
REMARK 3 L11: 3.9898 L22: 0.9084
REMARK 3 L33: 3.0302 L12: 0.5000
REMARK 3 L13: -2.5747 L23: -0.4822
REMARK 3 S TENSOR
REMARK 3 S11: -0.0603 S12: -0.1399 S13: 0.2467
REMARK 3 S21: 0.0521 S22: 0.1348 S23: -0.0818
REMARK 3 S31: -0.0673 S32: 0.1251 S33: -0.0829
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 159 THROUGH 192 )
REMARK 3 ORIGIN FOR THE GROUP (A): 20.6987 46.6597 -0.0604
REMARK 3 T TENSOR
REMARK 3 T11: 0.0849 T22: 0.0905
REMARK 3 T33: 0.1276 T12: 0.0135
REMARK 3 T13: 0.0331 T23: 0.0008
REMARK 3 L TENSOR
REMARK 3 L11: 3.5938 L22: 1.7486
REMARK 3 L33: 5.4230 L12: -0.4462
REMARK 3 L13: 2.6013 L23: -0.4747
REMARK 3 S TENSOR
REMARK 3 S11: 0.0381 S12: 0.0858 S13: -0.0192
REMARK 3 S21: -0.0846 S22: 0.0117 S23: 0.0827
REMARK 3 S31: 0.0409 S32: -0.0378 S33: -0.0910
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 4WKS COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 07-OCT-14.
REMARK 100 THE DEPOSITION ID IS D_1000203933.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 08-JUN-13
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 : APS
REMARK 200 BEAMLINE : 23-ID-B
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.99
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 300 MM CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : NULL
REMARK 200 DATA SCALING SOFTWARE : NULL
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 119528
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.600
REMARK 200 RESOLUTION RANGE LOW (A) : 42.600
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.5
REMARK 200 DATA REDUNDANCY : 3.800
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 12.7000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
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: NULL
REMARK 200 STARTING MODEL: 4M1J
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 59.84
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.06
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: HEPES (50 MM) AT PH 7.5; RBCL (80 MM);
REMARK 280 PEG-4000 10% (W/V), EVAPORATION, TEMPERATURE 298K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z+1/2
REMARK 290 3555 -X,Y,-Z+1/2
REMARK 290 4555 X,-Y,-Z
REMARK 290 5555 X+1/2,Y+1/2,Z
REMARK 290 6555 -X+1/2,-Y+1/2,Z+1/2
REMARK 290 7555 -X+1/2,Y+1/2,-Z+1/2
REMARK 290 8555 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 0.00000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 47.22500
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 47.22500
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 60.93100
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 83.73550
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 60.93100
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 83.73550
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 47.22500
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 60.93100
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 83.73550
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 47.22500
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 60.93100
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 83.73550
REMARK 290 SMTRY3 8 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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 7790 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 28240 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -51.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, 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 PRO A 28
REMARK 465 THR A 29
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 GLU C 561 CG CD OE1 OE2
REMARK 470 LYS C 562 CG CD CE NZ
REMARK 470 ASP C 648 CB CG OD1 OD2
REMARK 470 LYS A 192 CG CD CE NZ
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 NE2 GLN C 376 O HOH C 1393 1.81
REMARK 500 O HOH C 1395 O HOH C 1412 1.82
REMARK 500 O HOH C 1357 O HOH C 1366 1.84
REMARK 500 O HOH A 404 O HOH A 409 1.88
REMARK 500 O HOH A 399 O HOH A 407 1.88
REMARK 500 OE1 GLU C 370 O HOH C 1294 1.92
REMARK 500 O HOH C 1421 O HOH C 1430 1.93
REMARK 500 O HOH C 918 O HOH C 1435 1.98
REMARK 500 O HOH C 1374 O HOH C 1389 1.98
REMARK 500 O HOH C 1277 O HOH C 1278 2.00
REMARK 500 NE2 GLN C 341 O HOH C 1199 2.01
REMARK 500 O HOH A 411 O HOH A 416 2.01
REMARK 500 O HOH A 383 O HOH A 410 2.02
REMARK 500 OE2 GLU A 71 O HOH A 414 2.03
REMARK 500 OD1 ASP C 750 O HOH C 901 2.03
REMARK 500 O HOH A 390 O HOH A 413 2.05
REMARK 500 O HOH C 1226 O HOH C 1231 2.05
REMARK 500 O HOH C 979 O HOH C 996 2.07
REMARK 500 O HOH C 982 O HOH C 1283 2.07
REMARK 500 O HOH C 1457 O HOH C 1459 2.08
REMARK 500 O HOH C 1391 O HOH C 1455 2.08
REMARK 500 O HOH C 960 O HOH C 1415 2.08
REMARK 500 O HOH C 984 O HOH C 1103 2.10
REMARK 500 N GLY A 30 O HOH A 397 2.10
REMARK 500 OE2 GLU A 71 O HOH A 414 2.10
REMARK 500 O HOH C 1262 O HOH C 1266 2.12
REMARK 500 O HOH C 1091 O HOH C 1393 2.12
REMARK 500 O HOH C 1364 O HOH C 1408 2.12
REMARK 500 O HOH C 1451 O HOH C 1454 2.13
REMARK 500 O HOH C 1403 O HOH C 1416 2.14
REMARK 500 O HOH C 936 O HOH C 979 2.14
REMARK 500 O HOH C 1257 O HOH C 1416 2.14
REMARK 500 O HOH C 932 O HOH C 981 2.14
REMARK 500 O HOH C 1264 O HOH A 344 2.14
REMARK 500 O HOH C 1257 O HOH C 1325 2.14
REMARK 500 O HOH C 1216 O HOH C 1256 2.16
REMARK 500 O HOH C 1417 O HOH C 1428 2.16
REMARK 500 O HOH C 1314 O HOH A 364 2.17
REMARK 500 O HOH A 345 O HOH A 385 2.18
REMARK 500 O HOH C 1338 O HOH C 1458 2.18
REMARK 500 O HOH A 318 O HOH A 346 2.18
REMARK 500 O HOH C 968 O HOH C 1381 2.18
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 C 966 O HOH C 970 6554 1.77
REMARK 500 O HOH A 256 O HOH A 261 6555 2.04
REMARK 500 O HOH A 203 O HOH A 247 6554 2.08
REMARK 500 O HOH C 901 O HOH A 205 6555 2.09
REMARK 500 O HOH A 255 O HOH A 257 6555 2.16
REMARK 500 O HOH C 971 O HOH A 204 6555 2.17
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 ARG C 258 -4.52 -145.71
REMARK 500 PRO C 270 42.49 -88.40
REMARK 500 ASP C 303 106.93 -169.85
REMARK 500 LYS C 353 -56.42 -141.01
REMARK 500 ASN C 357 -154.67 -115.98
REMARK 500 TRP C 402 26.16 -156.27
REMARK 500 ASN C 418 60.07 -102.42
REMARK 500 ASP C 479 -74.92 -100.48
REMARK 500 SER C 696 -95.90 -143.52
REMARK 500 SER C 717 159.80 79.91
REMARK 500 ASN A 65 30.37 -146.92
REMARK 500 ASN A 107 42.14 -105.78
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH C1327 DISTANCE = 5.90 ANGSTROMS
REMARK 525 HOH C1391 DISTANCE = 7.78 ANGSTROMS
REMARK 525 HOH C1418 DISTANCE = 5.84 ANGSTROMS
REMARK 525 HOH C1452 DISTANCE = 5.89 ANGSTROMS
REMARK 525 HOH C1455 DISTANCE = 7.70 ANGSTROMS
REMARK 525 HOH A 400 DISTANCE = 8.32 ANGSTROMS
REMARK 525 HOH A 402 DISTANCE = 6.78 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue 3QD C 801
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4WKT RELATED DB: PDB
REMARK 900 RELATED ID: 4WKU RELATED DB: PDB
REMARK 900 RELATED ID: 4WKV RELATED DB: PDB
DBREF 4WKS C 217 762 UNP Q9I194 PVDQ_PSEAE 217 762
DBREF 4WKS A 28 192 UNP Q9I194 PVDQ_PSEAE 28 192
SEQADV 4WKS ALA C 763 UNP Q9I194 EXPRESSION TAG
SEQADV 4WKS ALA C 764 UNP Q9I194 EXPRESSION TAG
SEQRES 1 C 548 SER ASN ALA ILE ALA VAL GLY SER GLU ARG SER ALA ASP
SEQRES 2 C 548 GLY LYS GLY MET LEU LEU ALA ASN PRO HIS PHE PRO TRP
SEQRES 3 C 548 ASN GLY ALA MET ARG PHE TYR GLN MET HIS LEU THR ILE
SEQRES 4 C 548 PRO GLY ARG LEU ASP VAL MET GLY ALA SER LEU PRO GLY
SEQRES 5 C 548 LEU PRO VAL VAL ASN ILE GLY PHE SER ARG HIS LEU ALA
SEQRES 6 C 548 TRP THR HIS THR VAL ASP THR SER SER HIS PHE THR LEU
SEQRES 7 C 548 TYR ARG LEU ALA LEU ASP PRO LYS ASP PRO ARG ARG TYR
SEQRES 8 C 548 LEU VAL ASP GLY ARG SER LEU PRO LEU GLU GLU LYS SER
SEQRES 9 C 548 VAL ALA ILE GLU VAL ARG GLY ALA ASP GLY LYS LEU SER
SEQRES 10 C 548 ARG VAL GLU HIS LYS VAL TYR GLN SER ILE TYR GLY PRO
SEQRES 11 C 548 LEU VAL VAL TRP PRO GLY LYS LEU ASP TRP ASN ARG SER
SEQRES 12 C 548 GLU ALA TYR ALA LEU ARG ASP ALA ASN LEU GLU ASN THR
SEQRES 13 C 548 ARG VAL LEU GLN GLN TRP TYR SER ILE ASN GLN ALA SER
SEQRES 14 C 548 ASP VAL ALA ASP LEU ARG ARG ARG VAL GLU ALA LEU GLN
SEQRES 15 C 548 GLY ILE PRO TRP VAL ASN THR LEU ALA ALA ASP GLU GLN
SEQRES 16 C 548 GLY ASN ALA LEU TYR MET ASN GLN SER VAL VAL PRO TYR
SEQRES 17 C 548 LEU LYS PRO GLU LEU ILE PRO ALA CYS ALA ILE PRO GLN
SEQRES 18 C 548 LEU VAL ALA GLU GLY LEU PRO ALA LEU GLN GLY GLN ASP
SEQRES 19 C 548 SER ARG CYS ALA TRP SER ARG ASP PRO ALA ALA ALA GLN
SEQRES 20 C 548 ALA GLY ILE THR PRO ALA ALA GLN LEU PRO VAL LEU LEU
SEQRES 21 C 548 ARG ARG ASP PHE VAL GLN ASN SER ASN ASP SER ALA TRP
SEQRES 22 C 548 LEU THR ASN PRO ALA SER PRO LEU GLN GLY PHE SER PRO
SEQRES 23 C 548 LEU VAL SER GLN GLU LYS PRO ILE GLY PRO ARG ALA ARG
SEQRES 24 C 548 TYR ALA LEU SER ARG LEU GLN GLY LYS GLN PRO LEU GLU
SEQRES 25 C 548 ALA LYS THR LEU GLU GLU MET VAL THR ALA ASN HIS VAL
SEQRES 26 C 548 PHE SER ALA ASP GLN VAL LEU PRO ASP LEU LEU ARG LEU
SEQRES 27 C 548 CYS ARG ASP ASN GLN GLY GLU LYS SER LEU ALA ARG ALA
SEQRES 28 C 548 CYS ALA ALA LEU ALA GLN TRP ASP ARG GLY ALA ASN LEU
SEQRES 29 C 548 ASP SER GLY SER GLY PHE VAL TYR PHE GLN ARG PHE MET
SEQRES 30 C 548 GLN ARG PHE ALA GLU LEU ASP GLY ALA TRP LYS GLU PRO
SEQRES 31 C 548 PHE ASP ALA GLN ARG PRO LEU ASP THR PRO GLN GLY ILE
SEQRES 32 C 548 ALA LEU ASP ARG PRO GLN VAL ALA THR GLN VAL ARG GLN
SEQRES 33 C 548 ALA LEU ALA ASP ALA ALA ALA GLU VAL GLU LYS SER GLY
SEQRES 34 C 548 ILE PRO ASP GLY ALA ARG TRP GLY ASP LEU GLN VAL SER
SEQRES 35 C 548 THR ARG GLY GLN GLU ARG ILE ALA ILE PRO GLY GLY ASP
SEQRES 36 C 548 GLY HIS PHE GLY VAL TYR ASN ALA ILE GLN SER VAL ARG
SEQRES 37 C 548 LYS GLY ASP HIS LEU GLU VAL VAL GLY GLY THR SER TYR
SEQRES 38 C 548 ILE GLN LEU VAL THR PHE PRO GLU GLU GLY PRO LYS ALA
SEQRES 39 C 548 ARG GLY LEU LEU ALA PHE SER GLN SER SER ASP PRO ARG
SEQRES 40 C 548 SER PRO HIS TYR ARG ASP GLN THR GLU LEU PHE SER ARG
SEQRES 41 C 548 GLN GLN TRP GLN THR LEU PRO PHE SER ASP ARG GLN ILE
SEQRES 42 C 548 ASP ALA ASP PRO GLN LEU GLN ARG LEU SER ILE ARG GLU
SEQRES 43 C 548 ALA ALA
SEQRES 1 A 165 PRO THR GLY LEU ALA ALA ASP ILE ARG TRP THR ALA TYR
SEQRES 2 A 165 GLY VAL PRO HIS ILE ARG ALA LYS ASP GLU ARG GLY LEU
SEQRES 3 A 165 GLY TYR GLY ILE GLY TYR ALA TYR ALA ARG ASP ASN ALA
SEQRES 4 A 165 CYS LEU LEU ALA GLU GLU ILE VAL THR ALA ARG GLY GLU
SEQRES 5 A 165 ARG ALA ARG TYR PHE GLY SER GLU GLY LYS SER SER ALA
SEQRES 6 A 165 GLU LEU ASP ASN LEU PRO SER ASP ILE PHE TYR ALA TRP
SEQRES 7 A 165 LEU ASN GLN PRO GLU ALA LEU GLN ALA PHE TRP GLN ALA
SEQRES 8 A 165 GLN THR PRO ALA VAL ARG GLN LEU LEU GLU GLY TYR ALA
SEQRES 9 A 165 ALA GLY PHE ASN ARG PHE LEU ARG GLU ALA ASP GLY LYS
SEQRES 10 A 165 THR THR SER CYS LEU GLY GLN PRO TRP LEU ARG ALA ILE
SEQRES 11 A 165 ALA THR ASP ASP LEU LEU ARG LEU THR ARG ARG LEU LEU
SEQRES 12 A 165 VAL GLU GLY GLY VAL GLY GLN PHE ALA ASP ALA LEU VAL
SEQRES 13 A 165 ALA ALA ALA PRO PRO GLY ALA GLU LYS
HET 3QD C 801 4
HETNAM 3QD ETHYLBORONIC ACID
FORMUL 3 3QD C2 H7 B O2
FORMUL 4 HOH *781(H2 O)
HELIX 1 AA1 ASN C 243 ARG C 247 5 5
HELIX 2 AA2 ASN C 368 ASN C 371 5 4
HELIX 3 AA3 ARG C 373 GLN C 383 1 11
HELIX 4 AA4 ASP C 386 GLN C 398 1 13
HELIX 5 AA5 GLU C 428 ALA C 434 1 7
HELIX 6 AA6 ILE C 435 GLU C 441 1 7
HELIX 7 AA7 ASP C 450 ALA C 454 5 5
HELIX 8 AA8 PRO C 468 LEU C 472 5 5
HELIX 9 AA9 GLY C 511 GLN C 522 1 12
HELIX 10 AB1 GLU C 528 ALA C 538 1 11
HELIX 11 AB2 PHE C 542 ASP C 557 1 16
HELIX 12 AB3 GLU C 561 SER C 563 5 3
HELIX 13 AB4 LEU C 564 TRP C 574 1 11
HELIX 14 AB5 SER C 584 ALA C 597 1 14
HELIX 15 AB6 ARG C 623 SER C 644 1 22
HELIX 16 AB7 ARG C 651 LEU C 655 1 5
HELIX 17 AB8 ASP C 671 GLY C 675 5 5
HELIX 18 AB9 ARG C 728 ARG C 736 1 9
HELIX 19 AC1 SER C 745 ALA C 751 1 7
HELIX 20 AC2 ALA A 39 GLY A 41 5 3
HELIX 21 AC3 ASP A 49 ARG A 77 1 29
HELIX 22 AC4 GLU A 79 GLY A 85 1 7
HELIX 23 AC5 ASP A 95 ASN A 107 1 13
HELIX 24 AC6 GLN A 108 ALA A 118 1 11
HELIX 25 AC7 THR A 120 ALA A 141 1 22
HELIX 26 AC8 ALA A 158 VAL A 171 1 14
HELIX 27 AC9 GLU A 172 GLN A 177 5 6
HELIX 28 AD1 PHE A 178 ALA A 185 1 8
SHEET 1 AA1 6 PHE C 480 ASN C 483 0
SHEET 2 AA1 6 ASN C 218 VAL C 222 -1 N ALA C 221 O VAL C 481
SHEET 3 AA1 6 MET C 233 ASN C 237 -1 O LEU C 235 N ILE C 220
SHEET 4 AA1 6 TYR C 697 THR C 702 -1 O GLN C 699 N ALA C 236
SHEET 5 AA1 6 LYS C 709 LEU C 714 -1 O LEU C 713 N ILE C 698
SHEET 6 AA1 6 GLN C 740 THR C 741 -1 O GLN C 740 N GLY C 712
SHEET 1 AA2 4 HIS C 239 PRO C 241 0
SHEET 2 AA2 4 HIS C 688 THR C 695 -1 O GLY C 694 N PHE C 240
SHEET 3 AA2 4 GLN C 656 ARG C 660 1 N VAL C 657 O LEU C 689
SHEET 4 AA2 4 GLU C 663 ALA C 666 -1 O GLU C 663 N ARG C 660
SHEET 1 AA3 3 HIS C 239 PRO C 241 0
SHEET 2 AA3 3 HIS C 688 THR C 695 -1 O GLY C 694 N PHE C 240
SHEET 3 AA3 3 ILE C 680 LYS C 685 -1 N GLN C 681 O VAL C 692
SHEET 1 AA410 VAL C 474 ARG C 477 0
SHEET 2 AA410 ALA C 414 MET C 417 -1 N ALA C 414 O ARG C 477
SHEET 3 AA410 VAL C 403 ASP C 409 -1 N ALA C 407 O LEU C 415
SHEET 4 AA410 LEU C 280 VAL C 286 -1 N THR C 285 O ASN C 404
SHEET 5 AA410 ILE C 274 PHE C 276 -1 N GLY C 275 O TRP C 282
SHEET 6 AA410 LEU C 259 SER C 265 -1 N MET C 262 O PHE C 276
SHEET 7 AA410 TYR C 249 ILE C 255 -1 N LEU C 253 O VAL C 261
SHEET 8 AA410 VAL A 42 ARG A 46 1 O ILE A 45 N HIS C 252
SHEET 9 AA410 ALA A 32 THR A 38 -1 N ARG A 36 O HIS A 44
SHEET 10 AA410 GLN C 756 ARG C 761 -1 N LEU C 758 O ILE A 35
SHEET 1 AA5 7 ARG C 312 PRO C 315 0
SHEET 2 AA5 7 ASP C 303 VAL C 309 -1 N TYR C 307 O LEU C 314
SHEET 3 AA5 7 PHE C 292 ASP C 300 -1 N ALA C 298 O LEU C 308
SHEET 4 AA5 7 GLU C 360 ASP C 366 -1 O ALA C 361 N LEU C 297
SHEET 5 AA5 7 GLY C 345 VAL C 348 -1 N VAL C 348 O TYR C 362
SHEET 6 AA5 7 LEU C 332 SER C 342 -1 N SER C 342 O GLY C 345
SHEET 7 AA5 7 GLU C 317 ARG C 326 -1 N ILE C 323 O VAL C 335
SHEET 1 AA6 4 ARG C 312 PRO C 315 0
SHEET 2 AA6 4 ASP C 303 VAL C 309 -1 N TYR C 307 O LEU C 314
SHEET 3 AA6 4 PHE C 292 ASP C 300 -1 N ALA C 298 O LEU C 308
SHEET 4 AA6 4 ALA C 445 GLN C 447 1 O LEU C 446 N ARG C 296
SHEET 1 AA7 2 TRP C 603 GLU C 605 0
SHEET 2 AA7 2 GLN C 617 ILE C 619 -1 O GLN C 617 N GLU C 605
SSBOND 1 CYS C 433 CYS C 453 1555 1555 2.17
SSBOND 2 CYS C 555 CYS C 568 1555 1555 2.07
SSBOND 3 CYS A 67 CYS A 148 1555 1555 2.13
LINK OG SER C 217 B1 3QD C 801 1555 1555 1.42
CISPEP 1 THR C 615 PRO C 616 0 -0.66
SITE 1 AC1 5 SER C 217 HIS C 239 PHE C 240 ASN C 485
SITE 2 AC1 5 HOH C1395
CRYST1 121.862 167.471 94.450 90.00 90.00 90.00 C 2 2 21 8
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 0.008206 0.000000 0.000000 0.00000
SCALE2 0.000000 0.005971 0.000000 0.00000
SCALE3 0.000000 0.000000 0.010588 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
