HEADER OXIDOREDUCTASE 10-NOV-11 3UL3
TITLE STRUCTURAL INSIGHTS INTO THIOREDOXIN-2: A COMPONENT OF MALARIA
TITLE 2 PARASITE PROTEIN SECRETION MACHINERY
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: THIOREDOXIN;
COMPND 3 CHAIN: B, A;
COMPND 4 FRAGMENT: UNP RESIDUES 29-156;
COMPND 5 SYNONYM: THIOREDOXIN-2;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: PLASMODIUM FALCIPARUM;
SOURCE 3 ORGANISM_TAXID: 36329;
SOURCE 4 STRAIN: 3D7;
SOURCE 5 GENE: MAL13P1.225, TRX2;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: LEMO21 DE3;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PGEX4T1
KEYWDS THIOREDOXIN, PTEX, OXIDOREDUCTASE
EXPDTA X-RAY DIFFRACTION
AUTHOR A.SHARMA,A.SHARMA,S.DIXIT,A.SHARMA
REVDAT 4 20-MAR-24 3UL3 1 REMARK
REVDAT 3 25-DEC-19 3UL3 1 JRNL
REVDAT 2 08-NOV-17 3UL3 1 REMARK
REVDAT 1 14-DEC-11 3UL3 0
JRNL AUTH A.SHARMA,A.SHARMA,S.DIXIT,A.SHARMA
JRNL TITL STRUCTURAL INSIGHTS INTO THIOREDOXIN-2: A COMPONENT OF
JRNL TITL 2 MALARIA PARASITE PROTEIN SECRETION MACHINERY.
JRNL REF SCI REP V. 1 179 2011
JRNL REFN ESSN 2045-2322
JRNL PMID 22355694
JRNL DOI 10.1038/SREP00179
REMARK 2
REMARK 2 RESOLUTION. 2.91 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.7.1_743
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) : 2.91
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 39.26
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 0.140
REMARK 3 COMPLETENESS FOR RANGE (%) : 94.7
REMARK 3 NUMBER OF REFLECTIONS : 8635
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.261
REMARK 3 R VALUE (WORKING SET) : 0.257
REMARK 3 FREE R VALUE : 0.298
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 10.090
REMARK 3 FREE R VALUE TEST SET COUNT : 871
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 39.2592 - 5.2754 0.96 1391 160 0.2503 0.2860
REMARK 3 2 5.2754 - 4.1888 0.98 1317 152 0.2038 0.2440
REMARK 3 3 4.1888 - 3.6597 0.97 1346 144 0.2352 0.2930
REMARK 3 4 3.6597 - 3.3253 0.96 1292 141 0.3078 0.3585
REMARK 3 5 3.3253 - 3.0871 0.93 1243 143 0.3390 0.3764
REMARK 3 6 3.0871 - 2.9051 0.88 1175 131 0.3675 0.3640
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 0.50
REMARK 3 SHRINKAGE RADIUS : 0.16
REMARK 3 K_SOL : 0.36
REMARK 3 B_SOL : 110.7
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.800
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 30.690
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 90.25
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.39820
REMARK 3 B22 (A**2) : 0.39820
REMARK 3 B33 (A**2) : -0.79640
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 : 0.025 1624
REMARK 3 ANGLE : 1.688 2173
REMARK 3 CHIRALITY : 0.121 246
REMARK 3 PLANARITY : 0.007 266
REMARK 3 DIHEDRAL : 23.275 609
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 14
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN 'B' AND (RESSEQ 54:58)
REMARK 3 ORIGIN FOR THE GROUP (A): -28.7912 1.6050 -3.2648
REMARK 3 T TENSOR
REMARK 3 T11: 1.4824 T22: 1.7136
REMARK 3 T33: 1.5847 T12: -0.2964
REMARK 3 T13: -0.9593 T23: -0.8304
REMARK 3 L TENSOR
REMARK 3 L11: 6.7035 L22: 5.5050
REMARK 3 L33: 4.0334 L12: 4.7742
REMARK 3 L13: -4.5256 L23: -4.4215
REMARK 3 S TENSOR
REMARK 3 S11: 0.1057 S12: 0.0594 S13: -0.4221
REMARK 3 S21: -0.1729 S22: 0.0670 S23: 0.4264
REMARK 3 S31: 0.5199 S32: -0.7989 S33: 0.6659
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN 'B' AND (RESSEQ 59:71)
REMARK 3 ORIGIN FOR THE GROUP (A): -37.6128 -9.4057 -4.0906
REMARK 3 T TENSOR
REMARK 3 T11: 1.0151 T22: 0.5401
REMARK 3 T33: 0.4046 T12: 0.2186
REMARK 3 T13: -0.2400 T23: -0.0869
REMARK 3 L TENSOR
REMARK 3 L11: 9.9651 L22: 1.8336
REMARK 3 L33: 1.5445 L12: 4.2438
REMARK 3 L13: -3.8920 L23: -1.6859
REMARK 3 S TENSOR
REMARK 3 S11: -0.4098 S12: -1.5840 S13: 1.4922
REMARK 3 S21: 1.1977 S22: 0.1393 S23: -0.0056
REMARK 3 S31: -1.8563 S32: -0.2206 S33: 0.4351
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN 'B' AND (RESSEQ 72:82)
REMARK 3 ORIGIN FOR THE GROUP (A): -24.7017 -25.0226 -5.5665
REMARK 3 T TENSOR
REMARK 3 T11: 0.6675 T22: 0.7446
REMARK 3 T33: 0.2428 T12: 0.1941
REMARK 3 T13: -0.3608 T23: 0.0603
REMARK 3 L TENSOR
REMARK 3 L11: 0.0205 L22: 4.8839
REMARK 3 L33: 5.6843 L12: 0.0184
REMARK 3 L13: 0.4395 L23: -2.3942
REMARK 3 S TENSOR
REMARK 3 S11: -0.0699 S12: 1.4465 S13: 0.3630
REMARK 3 S21: -0.5876 S22: -1.2250 S23: -0.9218
REMARK 3 S31: 0.9716 S32: 1.6643 S33: -0.2741
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN 'B' AND (RESSEQ 83:112)
REMARK 3 ORIGIN FOR THE GROUP (A): -29.5143 -25.5386 -11.2663
REMARK 3 T TENSOR
REMARK 3 T11: 0.8337 T22: 0.5988
REMARK 3 T33: 0.5678 T12: 0.0859
REMARK 3 T13: -0.1409 T23: -0.0061
REMARK 3 L TENSOR
REMARK 3 L11: 5.8451 L22: 6.5934
REMARK 3 L33: 5.7983 L12: -1.5144
REMARK 3 L13: 3.7105 L23: 0.0051
REMARK 3 S TENSOR
REMARK 3 S11: 0.0703 S12: 1.0301 S13: -0.0351
REMARK 3 S21: -1.0253 S22: -0.1223 S23: 0.1082
REMARK 3 S31: 0.3991 S32: 0.4630 S33: -0.0211
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: CHAIN 'B' AND (RESSEQ 113:132)
REMARK 3 ORIGIN FOR THE GROUP (A): -26.8437 -22.8972 2.2458
REMARK 3 T TENSOR
REMARK 3 T11: 0.6052 T22: 0.9765
REMARK 3 T33: 0.5663 T12: 0.1153
REMARK 3 T13: -0.1677 T23: -0.0640
REMARK 3 L TENSOR
REMARK 3 L11: 6.8752 L22: 8.2059
REMARK 3 L33: 2.0975 L12: -1.8375
REMARK 3 L13: 2.8778 L23: -0.7157
REMARK 3 S TENSOR
REMARK 3 S11: -1.0964 S12: -1.1766 S13: -0.1323
REMARK 3 S21: 1.0953 S22: 0.7289 S23: 0.2533
REMARK 3 S31: -0.7135 S32: 0.4134 S33: 0.1741
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: CHAIN 'B' AND (RESSEQ 133:145)
REMARK 3 ORIGIN FOR THE GROUP (A): -34.8282 -27.2217 -0.5685
REMARK 3 T TENSOR
REMARK 3 T11: 0.9505 T22: 0.7352
REMARK 3 T33: 0.6710 T12: 0.4025
REMARK 3 T13: -0.0226 T23: 0.0138
REMARK 3 L TENSOR
REMARK 3 L11: 1.8747 L22: 5.4878
REMARK 3 L33: 2.3589 L12: 0.9629
REMARK 3 L13: 0.9824 L23: -1.4258
REMARK 3 S TENSOR
REMARK 3 S11: -0.7633 S12: -0.7901 S13: -0.1215
REMARK 3 S21: 0.1678 S22: 0.9773 S23: 1.4500
REMARK 3 S31: 0.3947 S32: 0.0952 S33: -0.0028
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: CHAIN 'B' AND (RESSEQ 146:156)
REMARK 3 ORIGIN FOR THE GROUP (A): -41.4048 -30.1204 -7.8448
REMARK 3 T TENSOR
REMARK 3 T11: 0.7917 T22: 1.0075
REMARK 3 T33: 1.2468 T12: -0.0349
REMARK 3 T13: -0.3119 T23: -0.4072
REMARK 3 L TENSOR
REMARK 3 L11: 7.8822 L22: 1.7995
REMARK 3 L33: 7.6834 L12: 0.9234
REMARK 3 L13: -1.7223 L23: -3.7296
REMARK 3 S TENSOR
REMARK 3 S11: -0.5112 S12: -0.5692 S13: -0.0685
REMARK 3 S21: -1.0146 S22: -0.9529 S23: 2.2456
REMARK 3 S31: 0.6297 S32: -1.5877 S33: 0.4806
REMARK 3 TLS GROUP : 8
REMARK 3 SELECTION: CHAIN 'A' AND (RESSEQ 54:63)
REMARK 3 ORIGIN FOR THE GROUP (A): -29.0747 -10.9930 3.2196
REMARK 3 T TENSOR
REMARK 3 T11: 1.3603 T22: 1.0525
REMARK 3 T33: 0.4764 T12: -0.1402
REMARK 3 T13: -0.3800 T23: -0.1570
REMARK 3 L TENSOR
REMARK 3 L11: 9.2925 L22: 8.3642
REMARK 3 L33: 2.0351 L12: 3.9345
REMARK 3 L13: -1.9449 L23: -8.0756
REMARK 3 S TENSOR
REMARK 3 S11: -1.6977 S12: 0.1123 S13: 2.3092
REMARK 3 S21: -1.2025 S22: -0.5413 S23: 0.0906
REMARK 3 S31: -2.4291 S32: 1.7156 S33: -2.1342
REMARK 3 TLS GROUP : 9
REMARK 3 SELECTION: CHAIN 'A' AND (RESSEQ 64:71)
REMARK 3 ORIGIN FOR THE GROUP (A): -23.1925 -10.1500 -4.3791
REMARK 3 T TENSOR
REMARK 3 T11: 1.1799 T22: 0.5002
REMARK 3 T33: 0.6432 T12: 0.2723
REMARK 3 T13: -0.5661 T23: -0.1242
REMARK 3 L TENSOR
REMARK 3 L11: 2.9862 L22: 4.2104
REMARK 3 L33: 6.8610 L12: 1.2329
REMARK 3 L13: 4.3472 L23: 0.3749
REMARK 3 S TENSOR
REMARK 3 S11: -0.6696 S12: -0.0475 S13: 0.7984
REMARK 3 S21: 0.3808 S22: -0.8811 S23: -0.0014
REMARK 3 S31: -1.8769 S32: -1.6423 S33: -2.4740
REMARK 3 TLS GROUP : 10
REMARK 3 SELECTION: CHAIN 'A' AND (RESSEQ 72:99)
REMARK 3 ORIGIN FOR THE GROUP (A): -29.4691 -9.1203 -23.0729
REMARK 3 T TENSOR
REMARK 3 T11: 0.8428 T22: 0.5643
REMARK 3 T33: 0.8644 T12: 0.1271
REMARK 3 T13: 0.0383 T23: 0.0537
REMARK 3 L TENSOR
REMARK 3 L11: 3.6291 L22: 2.5387
REMARK 3 L33: 6.9991 L12: -0.6283
REMARK 3 L13: 3.9442 L23: -0.3769
REMARK 3 S TENSOR
REMARK 3 S11: -0.2110 S12: 0.5626 S13: -0.2572
REMARK 3 S21: -0.2592 S22: -0.1979 S23: -0.4742
REMARK 3 S31: 0.6056 S32: 0.7651 S33: 0.3247
REMARK 3 TLS GROUP : 11
REMARK 3 SELECTION: CHAIN 'A' AND (RESSEQ 100:112)
REMARK 3 ORIGIN FOR THE GROUP (A): -30.1361 -9.9248 -15.0765
REMARK 3 T TENSOR
REMARK 3 T11: 0.7835 T22: 0.6764
REMARK 3 T33: 0.6650 T12: 0.1237
REMARK 3 T13: 0.1372 T23: -0.0163
REMARK 3 L TENSOR
REMARK 3 L11: 8.0151 L22: 7.0669
REMARK 3 L33: 5.4798 L12: -4.4911
REMARK 3 L13: 3.9569 L23: -0.7530
REMARK 3 S TENSOR
REMARK 3 S11: -0.1829 S12: -0.3339 S13: -1.1605
REMARK 3 S21: -0.7107 S22: 0.2665 S23: -0.7997
REMARK 3 S31: 0.2744 S32: 0.4635 S33: -0.0430
REMARK 3 TLS GROUP : 12
REMARK 3 SELECTION: CHAIN 'A' AND (RESSEQ 113:132)
REMARK 3 ORIGIN FOR THE GROUP (A): -33.2825 0.9877 -14.2062
REMARK 3 T TENSOR
REMARK 3 T11: 0.8343 T22: 0.6080
REMARK 3 T33: 0.5867 T12: 0.0808
REMARK 3 T13: -0.0978 T23: -0.1519
REMARK 3 L TENSOR
REMARK 3 L11: 4.3399 L22: 5.4148
REMARK 3 L33: 8.5799 L12: 0.0777
REMARK 3 L13: 0.1698 L23: -0.0201
REMARK 3 S TENSOR
REMARK 3 S11: -0.5856 S12: -0.7511 S13: 0.9870
REMARK 3 S21: 0.8942 S22: 0.1106 S23: 0.3746
REMARK 3 S31: -1.7243 S32: -0.8038 S33: 0.4733
REMARK 3 TLS GROUP : 13
REMARK 3 SELECTION: CHAIN 'A' AND (RESSEQ 133:145)
REMARK 3 ORIGIN FOR THE GROUP (A): -24.1953 0.2829 -17.7726
REMARK 3 T TENSOR
REMARK 3 T11: 0.8231 T22: 0.6449
REMARK 3 T33: 0.7826 T12: 0.0284
REMARK 3 T13: -0.2726 T23: 0.0959
REMARK 3 L TENSOR
REMARK 3 L11: 7.4858 L22: 3.6764
REMARK 3 L33: 6.2608 L12: -0.0717
REMARK 3 L13: -1.7640 L23: -2.2088
REMARK 3 S TENSOR
REMARK 3 S11: 0.0733 S12: -1.1939 S13: -0.4999
REMARK 3 S21: 1.9250 S22: 0.0385 S23: -0.9529
REMARK 3 S31: 0.0927 S32: 2.0206 S33: -0.0464
REMARK 3 TLS GROUP : 14
REMARK 3 SELECTION: CHAIN 'A' AND (RESSEQ 146:156)
REMARK 3 ORIGIN FOR THE GROUP (A): -16.7287 -5.1893 -22.4794
REMARK 3 T TENSOR
REMARK 3 T11: 0.6111 T22: 1.3466
REMARK 3 T33: 1.3017 T12: 0.0898
REMARK 3 T13: 0.0295 T23: 0.0807
REMARK 3 L TENSOR
REMARK 3 L11: 5.8755 L22: 7.9157
REMARK 3 L33: 5.0091 L12: 0.8457
REMARK 3 L13: -0.4246 L23: -1.4106
REMARK 3 S TENSOR
REMARK 3 S11: 0.6989 S12: 0.3241 S13: 0.0577
REMARK 3 S21: -0.2548 S22: -0.1999 S23: -1.8834
REMARK 3 S31: 0.5463 S32: 2.8379 S33: -0.5733
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 3UL3 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 24-NOV-11.
REMARK 100 THE DEPOSITION ID IS D_1000068889.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 13-DEC-10
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 5.5
REMARK 200 NUMBER OF CRYSTALS USED : 3
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : BM14
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.07
REMARK 200 MONOCHROMATOR : SI 111 CHANNEL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 8947
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.900
REMARK 200 RESOLUTION RANGE LOW (A) : 100.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.2
REMARK 200 DATA REDUNDANCY : 3.700
REMARK 200 R MERGE (I) : 0.04000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 15.1000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.90
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.00
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.1
REMARK 200 DATA REDUNDANCY IN SHELL : 3.70
REMARK 200 R MERGE FOR SHELL (I) : 0.36600
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: MIRAS
REMARK 200 SOFTWARE USED: SOLVE
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 62.80
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.31
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.125M BIS-TRIS PH 5.5, 2.2M AMMONIUM
REMARK 280 SULFATE, 5MM DTT, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 32 2 1
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
REMARK 290 5555 X-Y,-Y,-Z+1/3
REMARK 290 6555 -X,-X+Y,-Z+2/3
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 60.60267
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 30.30133
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 0.00000
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 30.30133
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 60.60267
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: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 350
REMARK 350 BIOMOLECULE: 2
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 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 SER B 29
REMARK 465 THR B 30
REMARK 465 ASN B 31
REMARK 465 ASP B 32
REMARK 465 ASP B 33
REMARK 465 PRO B 34
REMARK 465 LEU B 35
REMARK 465 THR B 36
REMARK 465 PRO B 37
REMARK 465 LEU B 38
REMARK 465 ASN B 39
REMARK 465 ARG B 40
REMARK 465 PHE B 41
REMARK 465 ASP B 42
REMARK 465 LYS B 43
REMARK 465 TYR B 44
REMARK 465 TYR B 45
REMARK 465 LEU B 46
REMARK 465 ARG B 47
REMARK 465 MET B 48
REMARK 465 PHE B 49
REMARK 465 LYS B 50
REMARK 465 LYS B 51
REMARK 465 VAL B 52
REMARK 465 PRO B 53
REMARK 465 SER A 29
REMARK 465 THR A 30
REMARK 465 ASN A 31
REMARK 465 ASP A 32
REMARK 465 ASP A 33
REMARK 465 PRO A 34
REMARK 465 LEU A 35
REMARK 465 THR A 36
REMARK 465 PRO A 37
REMARK 465 LEU A 38
REMARK 465 ASN A 39
REMARK 465 ARG A 40
REMARK 465 PHE A 41
REMARK 465 ASP A 42
REMARK 465 LYS A 43
REMARK 465 TYR A 44
REMARK 465 TYR A 45
REMARK 465 LEU A 46
REMARK 465 ARG A 47
REMARK 465 MET A 48
REMARK 465 PHE A 49
REMARK 465 LYS A 50
REMARK 465 LYS A 51
REMARK 465 VAL A 52
REMARK 465 PRO A 53
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 ARG B 54 CG CD NE CZ NH1 NH2
REMARK 470 LEU B 55 CB CG CD1 CD2
REMARK 470 GLN B 56 CG CD OE1 NE2
REMARK 470 GLN B 57 CG CD OE1 NE2
REMARK 470 ASN B 58 CG OD1 ND2
REMARK 470 ILE B 62 CB CG1 CG2 CD1
REMARK 470 ILE B 63 CG1 CG2 CD1
REMARK 470 ASN B 64 CG OD1 ND2
REMARK 470 ASN B 67 CB CG OD1 ND2
REMARK 470 MET B 68 CG SD CE
REMARK 470 ARG A 54 CG CD NE CZ NH1 NH2
REMARK 470 LEU A 55 CG CD1 CD2
REMARK 470 GLN A 56 CB CG CD OE1 NE2
REMARK 470 GLN A 57 CB CG CD OE1 NE2
REMARK 470 ASN A 58 CB CG OD1 ND2
REMARK 470 SER A 60 CB OG
REMARK 470 ASN A 61 CB CG OD1 ND2
REMARK 470 ILE A 62 CB CG1 CG2 CD1
REMARK 470 ILE A 63 CB CG1 CG2 CD1
REMARK 470 VAL A 66 CB CG1 CG2
REMARK 470 ASN A 67 CB CG OD1 ND2
REMARK 470 MET A 68 CG SD CE
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 OH TYR B 104 OH TYR A 104 1.54
REMARK 500 O ALA A 117 CG2 VAL A 122 1.97
REMARK 500 O HOH A 3 O HOH A 7 1.98
REMARK 500 OG SER A 145 OD1 ASP A 148 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 NE2 GLN B 83 OD1 ASP A 111 6444 2.14
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
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 RES CSSEQI ATM2 DEVIATION
REMARK 500 CYS B 82 CB CYS B 82 SG -0.114
REMARK 500 CYS B 85 CB CYS B 85 SG -0.107
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 ASN B 67 9.59 86.66
REMARK 500 MET B 68 -86.30 -118.61
REMARK 500 ASN A 61 -87.32 159.06
REMARK 500 VAL A 66 -124.97 47.99
REMARK 500 ASN A 67 157.80 110.13
REMARK 500 LYS A 134 2.98 81.80
REMARK 500
REMARK 500 REMARK: NULL
DBREF 3UL3 B 29 156 UNP Q8IDP4 Q8IDP4_PLAF7 29 156
DBREF 3UL3 A 29 156 UNP Q8IDP4 Q8IDP4_PLAF7 29 156
SEQRES 1 B 128 SER THR ASN ASP ASP PRO LEU THR PRO LEU ASN ARG PHE
SEQRES 2 B 128 ASP LYS TYR TYR LEU ARG MET PHE LYS LYS VAL PRO ARG
SEQRES 3 B 128 LEU GLN GLN ASN GLY SER ASN ILE ILE ASN GLY VAL ASN
SEQRES 4 B 128 MET LYS ASN THR VAL ILE VAL LEU TYR PHE PHE ALA LYS
SEQRES 5 B 128 TRP CYS GLN ALA CYS THR MET GLN SER THR GLU MET ASP
SEQRES 6 B 128 LYS LEU GLN LYS TYR TYR GLY LYS ARG ILE TYR LEU LEU
SEQRES 7 B 128 LYS VAL ASP LEU ASP LYS ASN GLU SER LEU ALA ARG LYS
SEQRES 8 B 128 PHE SER VAL LYS SER LEU PRO THR ILE ILE LEU LEU LYS
SEQRES 9 B 128 ASN LYS THR MET LEU ALA ARG LYS ASP HIS PHE VAL SER
SEQRES 10 B 128 SER ASN ASP LEU ILE ALA LEU ILE LYS LYS HIS
SEQRES 1 A 128 SER THR ASN ASP ASP PRO LEU THR PRO LEU ASN ARG PHE
SEQRES 2 A 128 ASP LYS TYR TYR LEU ARG MET PHE LYS LYS VAL PRO ARG
SEQRES 3 A 128 LEU GLN GLN ASN GLY SER ASN ILE ILE ASN GLY VAL ASN
SEQRES 4 A 128 MET LYS ASN THR VAL ILE VAL LEU TYR PHE PHE ALA LYS
SEQRES 5 A 128 TRP CYS GLN ALA CYS THR MET GLN SER THR GLU MET ASP
SEQRES 6 A 128 LYS LEU GLN LYS TYR TYR GLY LYS ARG ILE TYR LEU LEU
SEQRES 7 A 128 LYS VAL ASP LEU ASP LYS ASN GLU SER LEU ALA ARG LYS
SEQRES 8 A 128 PHE SER VAL LYS SER LEU PRO THR ILE ILE LEU LEU LYS
SEQRES 9 A 128 ASN LYS THR MET LEU ALA ARG LYS ASP HIS PHE VAL SER
SEQRES 10 A 128 SER ASN ASP LEU ILE ALA LEU ILE LYS LYS HIS
FORMUL 3 HOH *30(H2 O)
HELIX 1 1 CYS B 82 GLY B 100 1 19
HELIX 2 2 ASN B 113 PHE B 120 1 8
HELIX 3 3 SER B 145 LYS B 154 1 10
HELIX 4 4 CYS A 82 GLY A 100 1 19
HELIX 5 5 ASN A 113 PHE A 120 1 8
HELIX 6 6 SER A 145 HIS A 156 1 12
SHEET 1 A 4 ILE B 103 ASP B 109 0
SHEET 2 A 4 VAL B 72 PHE B 78 1 N VAL B 74 O TYR B 104
SHEET 3 A 4 THR B 127 LYS B 132 -1 O THR B 127 N PHE B 77
SHEET 4 A 4 THR B 135 LYS B 140 -1 O LEU B 137 N LEU B 130
SHEET 1 B 4 ILE A 103 ASP A 109 0
SHEET 2 B 4 VAL A 72 PHE A 78 1 N VAL A 74 O TYR A 104
SHEET 3 B 4 THR A 127 LYS A 132 -1 O ILE A 129 N LEU A 75
SHEET 4 B 4 THR A 135 LYS A 140 -1 O LYS A 140 N ILE A 128
CISPEP 1 LEU B 125 PRO B 126 0 -3.13
CISPEP 2 VAL A 66 ASN A 67 0 0.77
CISPEP 3 MET A 68 LYS A 69 0 3.50
CISPEP 4 LEU A 125 PRO A 126 0 -2.27
CRYST1 87.046 87.046 90.904 90.00 90.00 120.00 P 32 2 1 12
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 0.011488 0.006633 0.000000 0.00000
SCALE2 0.000000 0.013265 0.000000 0.00000
SCALE3 0.000000 0.000000 0.011001 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
