HEADER HYDROLASE 16-OCT-08 3EXD
TITLE SULFUR-SAD PHASED HEWL CRYSTAL
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: LYSOZYME C;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: 1,4-BETA-N-ACETYLMURAMIDASE C, ALLERGEN GAL D IV;
COMPND 5 EC: 3.2.1.17
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: GALLUS GALLUS;
SOURCE 3 ORGANISM_COMMON: BANTAM,CHICKENS;
SOURCE 4 ORGANISM_TAXID: 9031
KEYWDS HEWL, SULFUR, SAD PHASING, ALLERGEN, ANTIMICROBIAL, BACTERIOLYTIC
KEYWDS 2 ENZYME, GLYCOSIDASE, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR A.S.NASCIMENTO,M.V.LIBERATO,I.POLIKARPOV
REVDAT 5 27-DEC-23 3EXD 1 REMARK
REVDAT 4 25-OCT-17 3EXD 1 REMARK
REVDAT 3 14-APR-09 3EXD 1 JRNL
REVDAT 2 24-FEB-09 3EXD 1 VERSN
REVDAT 1 28-OCT-08 3EXD 0
JRNL AUTH B.G.GUIMARAES,L.SANFELICI,R.T.NEUENSCHWANDER,F.RODRIGUES,
JRNL AUTH 2 W.C.GRIZOLLI,M.A.RAULIK,J.R.PITON,B.C.MEYER,A.S.NASCIMENTO,
JRNL AUTH 3 I.POLIKARPOV
JRNL TITL THE MX2 MACROMOLECULAR CRYSTALLOGRAPHY BEAMLINE: A WIGGLER
JRNL TITL 2 X-RAY SOURCE AT THE LNLS.
JRNL REF J.SYNCHROTRON RADIAT. V. 16 69 2009
JRNL REFN ISSN 0909-0495
JRNL PMID 19096177
JRNL DOI 10.1107/S0909049508034870
REMARK 2
REMARK 2 RESOLUTION. 1.49 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE)
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) : 1.49
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 7.99
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 0.190
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.5
REMARK 3 NUMBER OF REFLECTIONS : 19252
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.165
REMARK 3 R VALUE (WORKING SET) : 0.163
REMARK 3 FREE R VALUE : 0.184
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 10.000
REMARK 3 FREE R VALUE TEST SET COUNT : 1926
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 7.9890 - 3.4957 1.00 1345 150 0.1646 0.1739
REMARK 3 2 3.4957 - 2.8144 1.00 1276 142 0.1568 0.1641
REMARK 3 3 2.8144 - 2.4707 1.00 1252 139 0.1689 0.1826
REMARK 3 4 2.4707 - 2.2503 1.00 1258 140 0.1566 0.1822
REMARK 3 5 2.2503 - 2.0921 1.00 1242 138 0.1553 0.1835
REMARK 3 6 2.0921 - 1.9707 1.00 1241 137 0.1534 0.1973
REMARK 3 7 1.9707 - 1.8734 1.00 1235 138 0.1498 0.1764
REMARK 3 8 1.8734 - 1.7928 1.00 1223 136 0.1525 0.1934
REMARK 3 9 1.7928 - 1.7245 1.00 1224 136 0.1530 0.1920
REMARK 3 10 1.7245 - 1.6655 0.99 1208 135 0.1525 0.1987
REMARK 3 11 1.6655 - 1.6139 0.99 1205 134 0.1455 0.1628
REMARK 3 12 1.6139 - 1.5681 0.99 1220 135 0.1534 0.1911
REMARK 3 13 1.5681 - 1.5271 0.99 1194 133 0.1615 0.1725
REMARK 3 14 1.5271 - 1.4900 0.98 1203 133 0.1609 0.2023
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 : 0.53
REMARK 3 B_SOL : 99.11
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.160
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : NULL
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 16.20
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 : 0.006 NULL
REMARK 3 ANGLE : NULL NULL
REMARK 3 CHIRALITY : NULL NULL
REMARK 3 PLANARITY : NULL NULL
REMARK 3 DIHEDRAL : 16.308 NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 10
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN A AND RESID 1:13)
REMARK 3 ORIGIN FOR THE GROUP (A): 45.3675 22.3753 8.6845
REMARK 3 T TENSOR
REMARK 3 T11: 0.1330 T22: 0.1954
REMARK 3 T33: 0.1824 T12: -0.0075
REMARK 3 T13: 0.0302 T23: 0.0133
REMARK 3 L TENSOR
REMARK 3 L11: 0.2536 L22: 0.3002
REMARK 3 L33: 0.6670 L12: 0.3988
REMARK 3 L13: -0.2940 L23: -0.2643
REMARK 3 S TENSOR
REMARK 3 S11: 0.0063 S12: 0.1562 S13: 0.0032
REMARK 3 S21: -0.0578 S22: -0.0450 S23: -0.2666
REMARK 3 S31: -0.0455 S32: 0.0979 S33: 0.0001
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN A AND RESID 14:21)
REMARK 3 ORIGIN FOR THE GROUP (A): 51.6242 19.2364 19.8682
REMARK 3 T TENSOR
REMARK 3 T11: 0.1286 T22: 0.2091
REMARK 3 T33: 0.2068 T12: -0.0095
REMARK 3 T13: -0.0173 T23: 0.0237
REMARK 3 L TENSOR
REMARK 3 L11: 0.5738 L22: 0.4370
REMARK 3 L33: 0.4039 L12: -0.1014
REMARK 3 L13: -0.1098 L23: 0.5222
REMARK 3 S TENSOR
REMARK 3 S11: -0.1812 S12: 0.3213 S13: 0.1430
REMARK 3 S21: 0.2607 S22: 0.2129 S23: -0.6516
REMARK 3 S31: -0.4128 S32: 0.3969 S33: 0.0018
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN A AND RESID 22:40)
REMARK 3 ORIGIN FOR THE GROUP (A): 41.2366 15.6269 13.6212
REMARK 3 T TENSOR
REMARK 3 T11: 0.0948 T22: 0.1088
REMARK 3 T33: 0.1267 T12: 0.0063
REMARK 3 T13: 0.0142 T23: -0.0051
REMARK 3 L TENSOR
REMARK 3 L11: 0.5846 L22: 0.6247
REMARK 3 L33: 0.6294 L12: 0.2004
REMARK 3 L13: -0.3861 L23: 0.1767
REMARK 3 S TENSOR
REMARK 3 S11: 0.0532 S12: 0.0279 S13: -0.0284
REMARK 3 S21: -0.0194 S22: -0.0463 S23: -0.0413
REMARK 3 S31: 0.0266 S32: 0.0621 S33: -0.0002
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN A AND RESID 41:58)
REMARK 3 ORIGIN FOR THE GROUP (A): 29.5860 21.2967 20.7247
REMARK 3 T TENSOR
REMARK 3 T11: 0.1272 T22: 0.1246
REMARK 3 T33: 0.1183 T12: 0.0037
REMARK 3 T13: 0.0319 T23: 0.0223
REMARK 3 L TENSOR
REMARK 3 L11: 0.5753 L22: 1.1435
REMARK 3 L33: 0.7359 L12: -0.2909
REMARK 3 L13: 0.3162 L23: 0.6731
REMARK 3 S TENSOR
REMARK 3 S11: -0.0037 S12: -0.0243 S13: 0.0128
REMARK 3 S21: 0.2039 S22: 0.0515 S23: 0.0980
REMARK 3 S31: 0.2855 S32: -0.0206 S33: 0.0000
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: CHAIN A AND RESID 59:68)
REMARK 3 ORIGIN FOR THE GROUP (A): 31.3830 23.4237 29.4998
REMARK 3 T TENSOR
REMARK 3 T11: 0.2151 T22: 0.2052
REMARK 3 T33: 0.1684 T12: 0.0389
REMARK 3 T13: 0.0248 T23: 0.0174
REMARK 3 L TENSOR
REMARK 3 L11: 0.4158 L22: 0.4602
REMARK 3 L33: 0.3588 L12: -0.0938
REMARK 3 L13: -0.0195 L23: 0.3060
REMARK 3 S TENSOR
REMARK 3 S11: -0.3096 S12: -0.5729 S13: -0.0341
REMARK 3 S21: 0.3995 S22: 0.2848 S23: 0.2840
REMARK 3 S31: 0.3196 S32: -0.0911 S33: 0.0013
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: CHAIN A AND RESID 69:96)
REMARK 3 ORIGIN FOR THE GROUP (A): 38.4804 26.5628 25.2082
REMARK 3 T TENSOR
REMARK 3 T11: 0.1384 T22: 0.1376
REMARK 3 T33: 0.1578 T12: 0.0071
REMARK 3 T13: -0.0062 T23: -0.0011
REMARK 3 L TENSOR
REMARK 3 L11: 1.5680 L22: 1.4607
REMARK 3 L33: 0.5817 L12: -0.7346
REMARK 3 L13: 0.8019 L23: 0.6106
REMARK 3 S TENSOR
REMARK 3 S11: -0.1105 S12: -0.2092 S13: 0.1970
REMARK 3 S21: 0.1578 S22: 0.1008 S23: -0.1616
REMARK 3 S31: -0.0730 S32: -0.0195 S33: 0.0001
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: CHAIN A AND RESID 97:108)
REMARK 3 ORIGIN FOR THE GROUP (A): 42.0888 13.3561 26.5502
REMARK 3 T TENSOR
REMARK 3 T11: 0.1659 T22: 0.1530
REMARK 3 T33: 0.1665 T12: 0.0130
REMARK 3 T13: 0.0002 T23: -0.0030
REMARK 3 L TENSOR
REMARK 3 L11: 0.6570 L22: 0.3325
REMARK 3 L33: 0.2960 L12: -0.2768
REMARK 3 L13: -0.0318 L23: -0.0317
REMARK 3 S TENSOR
REMARK 3 S11: -0.0638 S12: -0.2758 S13: 0.1060
REMARK 3 S21: 0.2849 S22: 0.0510 S23: -0.0244
REMARK 3 S31: -0.0222 S32: -0.0740 S33: -0.0002
REMARK 3 TLS GROUP : 8
REMARK 3 SELECTION: CHAIN A AND RESID 109:119)
REMARK 3 ORIGIN FOR THE GROUP (A): 39.1203 6.2798 16.2047
REMARK 3 T TENSOR
REMARK 3 T11: 0.1166 T22: 0.1454
REMARK 3 T33: 0.1423 T12: -0.0101
REMARK 3 T13: 0.0006 T23: -0.0148
REMARK 3 L TENSOR
REMARK 3 L11: 0.5822 L22: 0.9200
REMARK 3 L33: 0.4242 L12: 0.2479
REMARK 3 L13: 1.2306 L23: -0.0648
REMARK 3 S TENSOR
REMARK 3 S11: 0.0391 S12: -0.1403 S13: 0.1109
REMARK 3 S21: -0.1582 S22: -0.0632 S23: -0.0150
REMARK 3 S31: 0.2710 S32: -0.0804 S33: 0.0001
REMARK 3 TLS GROUP : 9
REMARK 3 SELECTION: CHAIN A AND RESID 120:124)
REMARK 3 ORIGIN FOR THE GROUP (A): 46.9589 10.1871 7.9697
REMARK 3 T TENSOR
REMARK 3 T11: 0.1390 T22: 0.1739
REMARK 3 T33: 0.1736 T12: 0.0334
REMARK 3 T13: 0.0163 T23: -0.0348
REMARK 3 L TENSOR
REMARK 3 L11: 0.0267 L22: 0.0920
REMARK 3 L33: 0.1317 L12: 0.2074
REMARK 3 L13: -0.0533 L23: -0.0540
REMARK 3 S TENSOR
REMARK 3 S11: -0.0553 S12: 0.3915 S13: -0.1357
REMARK 3 S21: -0.0458 S22: -0.0234 S23: -0.5491
REMARK 3 S31: 0.6537 S32: 0.4658 S33: -0.0001
REMARK 3 TLS GROUP : 10
REMARK 3 SELECTION: CHAIN A AND RESID 125:129)
REMARK 3 ORIGIN FOR THE GROUP (A): 52.8793 16.3339 3.1387
REMARK 3 T TENSOR
REMARK 3 T11: 0.1955 T22: 0.4152
REMARK 3 T33: 0.3444 T12: -0.0306
REMARK 3 T13: 0.1073 T23: -0.0809
REMARK 3 L TENSOR
REMARK 3 L11: 0.1236 L22: 0.1215
REMARK 3 L33: -0.0813 L12: -0.2219
REMARK 3 L13: -0.0933 L23: -0.3061
REMARK 3 S TENSOR
REMARK 3 S11: -0.0816 S12: 0.7942 S13: -0.4653
REMARK 3 S21: -0.1339 S22: 0.1691 S23: -1.1432
REMARK 3 S31: 0.3798 S32: 0.3783 S33: 0.0070
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 3EXD COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 17-OCT-08.
REMARK 100 THE DEPOSITION ID IS D_1000049885.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 01-AUG-08
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 5.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : LNLS
REMARK 200 BEAMLINE : W01B-MX2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.46
REMARK 200 MONOCHROMATOR : SI
REMARK 200 OPTICS : SI MONOCHROMATOR
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 225 MM CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 25761
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.350
REMARK 200 RESOLUTION RANGE LOW (A) : 30.760
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.8
REMARK 200 DATA REDUNDANCY : 24.50
REMARK 200 R MERGE (I) : 0.07800
REMARK 200 R SYM (I) : 0.07800
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 31.1000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.35
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.42
REMARK 200 COMPLETENESS FOR SHELL (%) : 92.3
REMARK 200 DATA REDUNDANCY IN SHELL : 10.50
REMARK 200 R MERGE FOR SHELL (I) : 0.71900
REMARK 200 R SYM FOR SHELL (I) : 0.71900
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.700
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD
REMARK 200 SOFTWARE USED: SHELXS
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 38.30
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.99
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 100MM SODIUM CITRATE, PH 5.5, VAPOR
REMARK 280 DIFFUSION, HANGING DROP, TEMPERATURE 291K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 43 21 2
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 -Y+1/2,X+1/2,Z+3/4
REMARK 290 4555 Y+1/2,-X+1/2,Z+1/4
REMARK 290 5555 -X+1/2,Y+1/2,-Z+3/4
REMARK 290 6555 X+1/2,-Y+1/2,-Z+1/4
REMARK 290 7555 Y,X,-Z
REMARK 290 8555 -Y,-X,-Z+1/2
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 18.46000
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 39.34100
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 39.34100
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 27.69000
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 39.34100
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 39.34100
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 9.23000
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 39.34100
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 39.34100
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 27.69000
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 39.34100
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 39.34100
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 9.23000
REMARK 290 SMTRY1 7 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 7 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 18.46000
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 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 152 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A 230 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A 251 LIES ON A SPECIAL POSITION.
DBREF 3EXD A 1 129 UNP P00698 LYSC_CHICK 19 147
SEQRES 1 A 129 LYS VAL PHE GLY ARG CYS GLU LEU ALA ALA ALA MET LYS
SEQRES 2 A 129 ARG HIS GLY LEU ASP ASN TYR ARG GLY TYR SER LEU GLY
SEQRES 3 A 129 ASN TRP VAL CYS ALA ALA LYS PHE GLU SER ASN PHE ASN
SEQRES 4 A 129 THR GLN ALA THR ASN ARG ASN THR ASP GLY SER THR ASP
SEQRES 5 A 129 TYR GLY ILE LEU GLN ILE ASN SER ARG TRP TRP CYS ASN
SEQRES 6 A 129 ASP GLY ARG THR PRO GLY SER ARG ASN LEU CYS ASN ILE
SEQRES 7 A 129 PRO CYS SER ALA LEU LEU SER SER ASP ILE THR ALA SER
SEQRES 8 A 129 VAL ASN CYS ALA LYS LYS ILE VAL SER ASP GLY ASN GLY
SEQRES 9 A 129 MET ASN ALA TRP VAL ALA TRP ARG ASN ARG CYS LYS GLY
SEQRES 10 A 129 THR ASP VAL GLN ALA TRP ILE ARG GLY CYS ARG LEU
FORMUL 2 HOH *233(H2 O)
HELIX 1 1 GLY A 4 HIS A 15 1 12
HELIX 2 2 ASN A 19 TYR A 23 5 5
HELIX 3 3 SER A 24 ASN A 37 1 14
HELIX 4 4 PRO A 79 SER A 85 5 7
HELIX 5 5 ILE A 88 SER A 100 1 13
HELIX 6 6 ASN A 103 ALA A 107 5 5
HELIX 7 7 TRP A 108 CYS A 115 1 8
HELIX 8 8 ASP A 119 ARG A 125 5 7
SHEET 1 A 3 THR A 43 ARG A 45 0
SHEET 2 A 3 THR A 51 TYR A 53 -1 O ASP A 52 N ASN A 44
SHEET 3 A 3 ILE A 58 ASN A 59 -1 O ILE A 58 N TYR A 53
SSBOND 1 CYS A 6 CYS A 127 1555 1555 2.11
SSBOND 2 CYS A 30 CYS A 115 1555 1555 2.04
SSBOND 3 CYS A 64 CYS A 80 1555 1555 2.04
SSBOND 4 CYS A 76 CYS A 94 1555 1555 2.03
CRYST1 78.682 78.682 36.920 90.00 90.00 90.00 P 43 21 2 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 0.012709 0.000000 0.000000 0.00000
SCALE2 0.000000 0.012709 0.000000 0.00000
SCALE3 0.000000 0.000000 0.027086 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
