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HEADER HYDROLASE 12-JAN-23 8FTP
TITLE FPHH, STAPHYLOCOCCUS AUREUS FLUOROPHOSPHONATE-BINDING SERINE
TITLE 2 HYDROLASES H, APO FORM
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ALPHA/BETA FOLD HYDROLASE;
COMPND 3 CHAIN: A, B;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: STAPHYLOCOCCUS AUREUS USA300-CA-263;
SOURCE 3 ORGANISM_TAXID: 1385529;
SOURCE 4 STRAIN: USA300;
SOURCE 5 GENE: EST_2;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET28A-LIC
KEYWDS FPHH, STAPHYLOCOCCUS AUREUS, S. AUREUS, FLUOROPHOSPHONATE-BINDING,
KEYWDS 2 SERINE HYDROLASES, LIPASE, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR M.FELLNER
REVDAT 1 11-OCT-23 8FTP 0
JRNL AUTH M.FELLNER
JRNL TITL FPHH, STAPHYLOCOCCUS AUREUS FLUOROPHOSPHONATE-BINDING SERINE
JRNL TITL 2 HYDROLASES H, APO FORM
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 1.37 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.20.1-4487
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) : 1.37
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 40.85
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 3 NUMBER OF REFLECTIONS : 129253
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.154
REMARK 3 R VALUE (WORKING SET) : 0.153
REMARK 3 FREE R VALUE : 0.164
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.030
REMARK 3 FREE R VALUE TEST SET COUNT : 6495
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 40.8500 - 4.2500 0.99 4309 223 0.1599 0.1534
REMARK 3 2 4.2500 - 3.3800 1.00 4199 199 0.1343 0.1551
REMARK 3 3 3.3800 - 2.9500 1.00 4179 220 0.1511 0.1705
REMARK 3 4 2.9500 - 2.6800 1.00 4129 239 0.1514 0.1538
REMARK 3 5 2.6800 - 2.4900 1.00 4135 233 0.1501 0.1650
REMARK 3 6 2.4900 - 2.3400 1.00 4059 242 0.1465 0.1642
REMARK 3 7 2.3400 - 2.2200 1.00 4126 220 0.1460 0.1326
REMARK 3 8 2.2200 - 2.1300 1.00 4132 185 0.1440 0.1636
REMARK 3 9 2.1300 - 2.0400 1.00 4101 202 0.1467 0.1501
REMARK 3 10 2.0400 - 1.9700 1.00 4068 221 0.1505 0.1756
REMARK 3 11 1.9700 - 1.9100 1.00 4091 239 0.1507 0.1755
REMARK 3 12 1.9100 - 1.8600 1.00 4107 202 0.1487 0.1607
REMARK 3 13 1.8600 - 1.8100 1.00 4087 230 0.1499 0.1698
REMARK 3 14 1.8100 - 1.7600 1.00 4131 197 0.1481 0.1563
REMARK 3 15 1.7600 - 1.7200 1.00 4054 225 0.1498 0.1771
REMARK 3 16 1.7200 - 1.6900 1.00 4024 253 0.1498 0.1425
REMARK 3 17 1.6900 - 1.6500 1.00 4037 231 0.1542 0.1608
REMARK 3 18 1.6500 - 1.6200 1.00 4112 224 0.1555 0.1902
REMARK 3 19 1.6200 - 1.5900 1.00 4103 186 0.1630 0.1965
REMARK 3 20 1.5900 - 1.5700 1.00 4004 245 0.1648 0.1814
REMARK 3 21 1.5700 - 1.5400 1.00 4104 205 0.1724 0.1916
REMARK 3 22 1.5400 - 1.5200 1.00 4100 189 0.1728 0.1867
REMARK 3 23 1.5200 - 1.5000 1.00 4073 200 0.1751 0.1669
REMARK 3 24 1.5000 - 1.4700 1.00 4100 204 0.1784 0.2178
REMARK 3 25 1.4700 - 1.4500 1.00 4059 190 0.1922 0.2341
REMARK 3 26 1.4500 - 1.4400 1.00 4076 226 0.2047 0.2088
REMARK 3 27 1.4400 - 1.4200 1.00 4032 215 0.2168 0.2369
REMARK 3 28 1.4200 - 1.4000 1.00 4107 218 0.2356 0.2479
REMARK 3 29 1.4000 - 1.3800 1.00 4006 232 0.2371 0.2340
REMARK 3 30 1.3800 - 1.3700 0.96 3914 200 0.2859 0.3159
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.10
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) : 0.130
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 15.620
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 : 0.009 NULL
REMARK 3 ANGLE : 1.028 NULL
REMARK 3 CHIRALITY : 0.080 575
REMARK 3 PLANARITY : 0.007 733
REMARK 3 DIHEDRAL : 15.566 1524
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 14
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 4 THROUGH 16 )
REMARK 3 ORIGIN FOR THE GROUP (A): -8.4727 -13.4607 17.6619
REMARK 3 T TENSOR
REMARK 3 T11: 0.1728 T22: 0.1490
REMARK 3 T33: 0.1469 T12: 0.0644
REMARK 3 T13: -0.0002 T23: 0.0153
REMARK 3 L TENSOR
REMARK 3 L11: 4.5021 L22: 4.6883
REMARK 3 L33: 4.5759 L12: 1.2185
REMARK 3 L13: 1.7092 L23: 0.7830
REMARK 3 S TENSOR
REMARK 3 S11: -0.2273 S12: 0.3849 S13: 0.4375
REMARK 3 S21: -0.3301 S22: 0.0189 S23: 0.2125
REMARK 3 S31: -0.3581 S32: -0.1021 S33: 0.2053
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 17 THROUGH 124 )
REMARK 3 ORIGIN FOR THE GROUP (A): -7.4177 -25.3155 19.5287
REMARK 3 T TENSOR
REMARK 3 T11: 0.1443 T22: 0.1531
REMARK 3 T33: 0.1371 T12: 0.0190
REMARK 3 T13: -0.0124 T23: -0.0105
REMARK 3 L TENSOR
REMARK 3 L11: 1.6831 L22: 1.3517
REMARK 3 L33: 1.7552 L12: -0.4538
REMARK 3 L13: 0.3419 L23: -0.1031
REMARK 3 S TENSOR
REMARK 3 S11: 0.0524 S12: 0.1406 S13: -0.1125
REMARK 3 S21: -0.1122 S22: -0.0306 S23: 0.0690
REMARK 3 S31: 0.0931 S32: -0.1289 S33: -0.0185
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 125 THROUGH 177 )
REMARK 3 ORIGIN FOR THE GROUP (A): -21.8827 -36.7275 13.9159
REMARK 3 T TENSOR
REMARK 3 T11: 0.2403 T22: 0.2841
REMARK 3 T33: 0.3229 T12: -0.0452
REMARK 3 T13: -0.0254 T23: -0.0327
REMARK 3 L TENSOR
REMARK 3 L11: 5.0415 L22: 0.5951
REMARK 3 L33: 2.7186 L12: -0.0577
REMARK 3 L13: 2.7125 L23: -0.0430
REMARK 3 S TENSOR
REMARK 3 S11: 0.1527 S12: 0.2613 S13: -0.4041
REMARK 3 S21: -0.0568 S22: 0.0154 S23: 0.2573
REMARK 3 S31: 0.1926 S32: -0.2329 S33: -0.2357
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 178 THROUGH 246 )
REMARK 3 ORIGIN FOR THE GROUP (A): -9.1949 -26.6990 34.5143
REMARK 3 T TENSOR
REMARK 3 T11: 0.1393 T22: 0.1965
REMARK 3 T33: 0.1023 T12: 0.0139
REMARK 3 T13: 0.0133 T23: 0.0040
REMARK 3 L TENSOR
REMARK 3 L11: 2.8990 L22: 3.0805
REMARK 3 L33: 2.5006 L12: -0.6631
REMARK 3 L13: 0.6929 L23: -0.3872
REMARK 3 S TENSOR
REMARK 3 S11: -0.0312 S12: -0.1155 S13: -0.0520
REMARK 3 S21: 0.1315 S22: 0.0887 S23: 0.1997
REMARK 3 S31: 0.0026 S32: -0.3224 S33: -0.0524
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 4 THROUGH 16 )
REMARK 3 ORIGIN FOR THE GROUP (A): -29.6963 8.6612 23.4956
REMARK 3 T TENSOR
REMARK 3 T11: 0.1909 T22: 0.1956
REMARK 3 T33: 0.1899 T12: 0.0577
REMARK 3 T13: 0.0065 T23: -0.0264
REMARK 3 L TENSOR
REMARK 3 L11: 3.9838 L22: 4.4379
REMARK 3 L33: 3.6599 L12: 0.5453
REMARK 3 L13: 0.3800 L23: 1.6198
REMARK 3 S TENSOR
REMARK 3 S11: -0.0336 S12: -0.4340 S13: 0.1300
REMARK 3 S21: 0.4442 S22: -0.0427 S23: 0.2912
REMARK 3 S31: -0.0333 S32: -0.2871 S33: 0.0781
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 17 THROUGH 64 )
REMARK 3 ORIGIN FOR THE GROUP (A): -20.8827 12.3154 23.2337
REMARK 3 T TENSOR
REMARK 3 T11: 0.2010 T22: 0.1708
REMARK 3 T33: 0.1561 T12: 0.0402
REMARK 3 T13: -0.0239 T23: -0.0663
REMARK 3 L TENSOR
REMARK 3 L11: 2.6283 L22: 2.2978
REMARK 3 L33: 1.7854 L12: 0.0799
REMARK 3 L13: -0.0120 L23: 0.5057
REMARK 3 S TENSOR
REMARK 3 S11: -0.0652 S12: -0.2943 S13: 0.2422
REMARK 3 S21: 0.2969 S22: 0.1369 S23: -0.1731
REMARK 3 S31: -0.1605 S32: 0.1544 S33: 0.0096
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 65 THROUGH 86 )
REMARK 3 ORIGIN FOR THE GROUP (A): -19.9731 0.1171 25.8720
REMARK 3 T TENSOR
REMARK 3 T11: 0.2363 T22: 0.1930
REMARK 3 T33: 0.1426 T12: 0.0839
REMARK 3 T13: 0.0004 T23: 0.0108
REMARK 3 L TENSOR
REMARK 3 L11: 4.2144 L22: 2.9816
REMARK 3 L33: 2.1546 L12: 0.3771
REMARK 3 L13: -0.0375 L23: 0.3737
REMARK 3 S TENSOR
REMARK 3 S11: -0.1373 S12: -0.5091 S13: -0.1112
REMARK 3 S21: 0.4035 S22: 0.1476 S23: 0.0390
REMARK 3 S31: 0.1476 S32: 0.0697 S33: -0.0128
REMARK 3 TLS GROUP : 8
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 87 THROUGH 124 )
REMARK 3 ORIGIN FOR THE GROUP (A): -11.9335 5.4637 16.5440
REMARK 3 T TENSOR
REMARK 3 T11: 0.1500 T22: 0.1537
REMARK 3 T33: 0.1665 T12: 0.0218
REMARK 3 T13: -0.0224 T23: -0.0337
REMARK 3 L TENSOR
REMARK 3 L11: 2.2649 L22: 2.7930
REMARK 3 L33: 2.8234 L12: -0.4428
REMARK 3 L13: -0.4546 L23: -0.2693
REMARK 3 S TENSOR
REMARK 3 S11: -0.0416 S12: -0.1672 S13: 0.2029
REMARK 3 S21: 0.0988 S22: 0.0402 S23: -0.2786
REMARK 3 S31: -0.1500 S32: 0.2657 S33: -0.0257
REMARK 3 TLS GROUP : 9
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 125 THROUGH 140 )
REMARK 3 ORIGIN FOR THE GROUP (A): -9.9222 26.4659 26.8589
REMARK 3 T TENSOR
REMARK 3 T11: 0.4521 T22: 0.3906
REMARK 3 T33: 0.7407 T12: -0.0940
REMARK 3 T13: -0.0339 T23: -0.2721
REMARK 3 L TENSOR
REMARK 3 L11: 2.4265 L22: 1.4196
REMARK 3 L33: 2.2991 L12: 0.2728
REMARK 3 L13: -1.3624 L23: 0.6720
REMARK 3 S TENSOR
REMARK 3 S11: 0.1835 S12: -0.3404 S13: 0.8471
REMARK 3 S21: 0.0483 S22: 0.1030 S23: -0.1618
REMARK 3 S31: -0.5820 S32: 0.2569 S33: 0.0895
REMARK 3 TLS GROUP : 10
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 141 THROUGH 157 )
REMARK 3 ORIGIN FOR THE GROUP (A): -7.3761 31.1838 35.5227
REMARK 3 T TENSOR
REMARK 3 T11: 0.6137 T22: 0.6850
REMARK 3 T33: 1.0278 T12: -0.0817
REMARK 3 T13: -0.1162 T23: -0.5186
REMARK 3 L TENSOR
REMARK 3 L11: 0.7079 L22: 1.1316
REMARK 3 L33: 0.4122 L12: -0.5982
REMARK 3 L13: -0.5254 L23: 0.5632
REMARK 3 S TENSOR
REMARK 3 S11: 0.1059 S12: -0.5219 S13: 0.6478
REMARK 3 S21: 0.3294 S22: 0.2869 S23: -0.6306
REMARK 3 S31: -0.2357 S32: 0.4331 S33: 0.1800
REMARK 3 TLS GROUP : 11
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 158 THROUGH 177 )
REMARK 3 ORIGIN FOR THE GROUP (A): -1.3459 7.0907 21.1780
REMARK 3 T TENSOR
REMARK 3 T11: 0.2074 T22: 0.4120
REMARK 3 T33: 0.3742 T12: 0.0200
REMARK 3 T13: -0.0819 T23: -0.1324
REMARK 3 L TENSOR
REMARK 3 L11: 1.5023 L22: 3.8734
REMARK 3 L33: 3.6286 L12: 0.8059
REMARK 3 L13: 0.6535 L23: 2.2560
REMARK 3 S TENSOR
REMARK 3 S11: -0.0771 S12: -0.5378 S13: 0.3593
REMARK 3 S21: 0.3282 S22: 0.2757 S23: -0.6185
REMARK 3 S31: -0.0024 S32: 0.6043 S33: -0.2587
REMARK 3 TLS GROUP : 12
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 178 THROUGH 215 )
REMARK 3 ORIGIN FOR THE GROUP (A): -10.3742 7.9450 5.9405
REMARK 3 T TENSOR
REMARK 3 T11: 0.1665 T22: 0.1389
REMARK 3 T33: 0.1693 T12: -0.0055
REMARK 3 T13: 0.0113 T23: -0.0025
REMARK 3 L TENSOR
REMARK 3 L11: 2.9069 L22: 3.0618
REMARK 3 L33: 2.6377 L12: -0.7946
REMARK 3 L13: -0.3448 L23: 0.6030
REMARK 3 S TENSOR
REMARK 3 S11: 0.0467 S12: 0.0466 S13: 0.3054
REMARK 3 S21: -0.1327 S22: 0.0247 S23: -0.2764
REMARK 3 S31: -0.2532 S32: 0.2115 S33: -0.0830
REMARK 3 TLS GROUP : 13
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 216 THROUGH 227 )
REMARK 3 ORIGIN FOR THE GROUP (A): -18.0199 20.8276 8.9018
REMARK 3 T TENSOR
REMARK 3 T11: 0.4067 T22: 0.2008
REMARK 3 T33: 0.3644 T12: 0.0195
REMARK 3 T13: 0.0335 T23: 0.0293
REMARK 3 L TENSOR
REMARK 3 L11: 3.8626 L22: 1.6319
REMARK 3 L33: 2.4200 L12: -0.3059
REMARK 3 L13: -1.2277 L23: 1.2398
REMARK 3 S TENSOR
REMARK 3 S11: 0.1419 S12: 0.1931 S13: 0.8204
REMARK 3 S21: -0.2578 S22: 0.0272 S23: -0.2375
REMARK 3 S31: -0.6940 S32: -0.0371 S33: -0.1281
REMARK 3 TLS GROUP : 14
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 228 THROUGH 246 )
REMARK 3 ORIGIN FOR THE GROUP (A): -26.3650 5.5107 6.7125
REMARK 3 T TENSOR
REMARK 3 T11: 0.1592 T22: 0.1603
REMARK 3 T33: 0.1495 T12: 0.0406
REMARK 3 T13: -0.0276 T23: -0.0292
REMARK 3 L TENSOR
REMARK 3 L11: 3.9676 L22: 5.7001
REMARK 3 L33: 3.5846 L12: -0.5753
REMARK 3 L13: -0.4560 L23: 0.7044
REMARK 3 S TENSOR
REMARK 3 S11: 0.0205 S12: 0.2475 S13: -0.0663
REMARK 3 S21: -0.3205 S22: -0.0650 S23: 0.2701
REMARK 3 S31: -0.0426 S32: -0.2758 S33: 0.1004
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 8FTP COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 17-JAN-23.
REMARK 100 THE DEPOSITION ID IS D_1000271400.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 27-APR-22
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 : AUSTRALIAN SYNCHROTRON
REMARK 200 BEAMLINE : MX2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9537
REMARK 200 MONOCHROMATOR : C(111)
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS EIGER X 16M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : AIMLESS 0.7.8
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 129324
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.370
REMARK 200 RESOLUTION RANGE LOW (A) : 49.090
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 200 DATA REDUNDANCY : 13.30
REMARK 200 R MERGE (I) : 0.06300
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 18.9000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.37
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.39
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : 13.20
REMARK 200 R MERGE FOR SHELL (I) : 1.53900
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 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: PHASER 2.8.3
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 54.73
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.72
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.15 UL 9.1 MG/ML FPHH (10MM HEPES PH
REMARK 280 7.6, 100MM NACL) WERE MIXED WITH 0.3 UL OF RESERVOIR SOLUTION.
REMARK 280 SITTING DROP RESERVOIR CONTAINED 200MM CALCIUM ACETATE HYDRATE,
REMARK 280 100MM TRIS PH 7.5, 10% W/V PEG 8000 AND 10% W/V PEG 1000.
REMARK 280 CRYSTAL APPEARED WITHIN A DAY AT 16C AND GREW UNTIL DAY 12.5
REMARK 280 WHEN IT WAS FROZEN IN A SOLUTION OF ~25% GLYCEROL, 75%
REMARK 280 RESERVOIR., VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 289.15K
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 82.34800
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 82.34800
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 42.57450
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 43.91850
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 42.57450
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 43.91850
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 82.34800
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 42.57450
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 43.91850
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 82.34800
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 42.57450
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 43.91850
REMARK 290 SMTRY3 8 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: MONOMERIC
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 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
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 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 553 LIES ON A SPECIAL POSITION.
REMARK 375 HOH B 475 LIES ON A SPECIAL POSITION.
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 GLY A -2
REMARK 465 PRO A -1
REMARK 465 GLY A 0
REMARK 465 MET A 1
REMARK 465 GLN A 2
REMARK 465 ILE A 3
REMARK 465 GLY B -2
REMARK 465 PRO B -1
REMARK 465 GLY B 0
REMARK 465 MET B 1
REMARK 465 GLN B 2
REMARK 465 ILE B 3
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 HZ1 LYS B 70 O HOH B 406 1.57
REMARK 500 O HOH A 574 O HOH A 587 2.11
REMARK 500 O HOH B 472 O HOH B 616 2.17
REMARK 500 O HOH B 504 O HOH B 599 2.18
REMARK 500 O HOH B 467 O HOH B 599 2.18
REMARK 500 O HOH A 446 O HOH A 657 2.19
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 GLU A 13 -111.48 -132.00
REMARK 500 THR A 25 -5.07 69.89
REMARK 500 SER A 63 -160.05 -109.18
REMARK 500 SER A 93 -126.96 61.46
REMARK 500 ASN A 189 60.26 -106.97
REMARK 500 GLU B 13 -115.56 -131.28
REMARK 500 THR B 25 -4.70 72.25
REMARK 500 SER B 63 -161.24 -108.29
REMARK 500 SER B 93 -128.17 64.84
REMARK 500 ASN B 189 60.52 -106.75
REMARK 500
REMARK 500 REMARK: NULL
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 302 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLN A 82 OE1
REMARK 620 2 HOH A 410 O 90.7
REMARK 620 3 HOH A 499 O 85.3 77.1
REMARK 620 4 HOH A 631 O 88.1 152.0 74.9
REMARK 620 5 HOH A 635 O 94.6 136.3 146.5 71.6
REMARK 620 6 HOH A 636 O 90.0 60.3 137.2 147.6 76.3
REMARK 620 7 HOH B 629 O 171.5 84.0 87.1 93.5 93.8 93.1
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 303 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU A 173 O
REMARK 620 2 ASP A 176 OD1 89.1
REMARK 620 3 ASP A 176 OD2 120.0 47.1
REMARK 620 4 HOH A 403 O 90.8 88.6 120.1
REMARK 620 5 HOH A 559 O 75.2 162.0 149.8 83.0
REMARK 620 6 HOH A 586 O 74.1 97.0 73.9 163.7 87.3
REMARK 620 7 HOH A 662 O 148.5 120.0 90.5 79.0 74.0 110.8
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 301 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 206 OD1
REMARK 620 2 HOH A 406 O 151.6
REMARK 620 3 HOH A 428 O 79.4 78.0
REMARK 620 4 HOH A 447 O 142.0 66.5 127.6
REMARK 620 5 HOH A 473 O 82.8 110.9 82.2 76.4
REMARK 620 6 HOH A 529 O 70.2 131.2 149.6 79.0 92.2
REMARK 620 7 HOH A 627 O 82.4 79.8 88.1 120.0 163.5 89.5
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 304 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 209 OD1
REMARK 620 2 HOH A 421 O 80.1
REMARK 620 3 HOH A 553 O 73.6 152.7
REMARK 620 4 HOH A 553 O 73.6 152.7 0.0
REMARK 620 5 HOH A 571 O 85.9 94.4 91.1 91.1
REMARK 620 6 HOH A 614 O 84.0 90.7 79.4 79.4 167.7
REMARK 620 7 HOH A 614 O 139.2 129.2 71.2 71.2 114.4 70.0
REMARK 620 8 HOH A 638 O 156.0 76.3 130.4 130.4 91.4 100.7 62.9
REMARK 620 N 1 2 3 4 5 6 7
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA B 303 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH A 663 O
REMARK 620 2 GLN B 82 OE1 170.8
REMARK 620 3 HOH B 431 O 92.4 94.5
REMARK 620 4 HOH B 449 O 93.3 81.9 79.2
REMARK 620 5 HOH B 589 O 86.9 84.3 155.4 76.3
REMARK 620 6 HOH B 602 O 83.0 97.0 131.1 149.5 73.3
REMARK 620 7 HOH B 608 O 86.7 102.1 59.4 138.6 144.9 71.7
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA B 304 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU B 173 O
REMARK 620 2 ASP B 176 OD1 86.9
REMARK 620 3 ASP B 176 OD2 119.7 51.4
REMARK 620 4 HOH B 467 O 92.1 74.4 111.0
REMARK 620 5 HOH B 504 O 148.8 115.5 68.1 113.9
REMARK 620 6 HOH B 525 O 77.3 153.8 154.6 85.3 87.7
REMARK 620 7 HOH B 532 O 79.1 101.0 70.9 170.4 75.6 96.4
REMARK 620 8 HOH B 599 O 147.8 98.1 86.8 59.3 54.7 85.2 130.2
REMARK 620 N 1 2 3 4 5 6 7
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA B 301 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP B 206 OD1
REMARK 620 2 HOH B 433 O 141.9
REMARK 620 3 HOH B 465 O 73.4 75.7
REMARK 620 4 HOH B 483 O 145.5 72.3 136.0
REMARK 620 5 HOH B 488 O 88.8 110.3 85.5 78.3
REMARK 620 6 HOH B 550 O 73.2 85.3 90.2 116.1 162.1
REMARK 620 7 HOH B 560 O 74.4 133.2 147.8 74.8 94.4 80.1
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA B 302 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP B 209 OD2
REMARK 620 2 HOH B 428 O 80.4
REMARK 620 3 HOH B 475 O 71.9 150.1
REMARK 620 4 HOH B 475 O 73.0 151.0 1.1
REMARK 620 5 HOH B 535 O 81.7 94.8 92.4 92.8
REMARK 620 6 HOH B 549 O 151.6 71.4 136.3 135.2 97.2
REMARK 620 7 HOH B 576 O 83.4 91.4 74.5 74.3 162.7 100.1
REMARK 620 8 HOH B 576 O 139.1 128.3 71.8 70.7 118.0 66.1 69.2
REMARK 620 N 1 2 3 4 5 6 7
DBREF1 8FTP A 1 246 UNP A0A0D6HZA6_STAAU
DBREF2 8FTP A A0A0D6HZA6 1 246
DBREF1 8FTP B 1 246 UNP A0A0D6HZA6_STAAU
DBREF2 8FTP B A0A0D6HZA6 1 246
SEQADV 8FTP GLY A -2 UNP A0A0D6HZA EXPRESSION TAG
SEQADV 8FTP PRO A -1 UNP A0A0D6HZA EXPRESSION TAG
SEQADV 8FTP GLY A 0 UNP A0A0D6HZA EXPRESSION TAG
SEQADV 8FTP GLY B -2 UNP A0A0D6HZA EXPRESSION TAG
SEQADV 8FTP PRO B -1 UNP A0A0D6HZA EXPRESSION TAG
SEQADV 8FTP GLY B 0 UNP A0A0D6HZA EXPRESSION TAG
SEQRES 1 A 249 GLY PRO GLY MET GLN ILE LYS LEU PRO LYS PRO PHE PHE
SEQRES 2 A 249 PHE GLU GLU GLY LYS ARG ALA VAL LEU LEU LEU HIS GLY
SEQRES 3 A 249 PHE THR GLY ASN SER SER ASP VAL ARG GLN LEU GLY ARG
SEQRES 4 A 249 PHE LEU GLN LYS LYS GLY TYR THR SER TYR ALA PRO GLN
SEQRES 5 A 249 TYR GLU GLY HIS ALA ALA PRO PRO ASP GLU ILE LEU LYS
SEQRES 6 A 249 SER SER PRO PHE VAL TRP PHE LYS ASP ALA LEU ASP GLY
SEQRES 7 A 249 TYR ASP TYR LEU VAL GLU GLN GLY TYR ASP GLU ILE VAL
SEQRES 8 A 249 VAL ALA GLY LEU SER LEU GLY GLY ASP PHE ALA LEU LYS
SEQRES 9 A 249 LEU SER LEU ASN ARG ASP VAL LYS GLY ILE VAL THR MET
SEQRES 10 A 249 CYS ALA PRO MET GLY GLY LYS THR GLU GLY ALA ILE TYR
SEQRES 11 A 249 GLU GLY PHE LEU GLU TYR ALA ARG ASN PHE LYS LYS TYR
SEQRES 12 A 249 GLU GLY LYS ASP GLN GLU THR ILE ASP ASN GLU MET ASP
SEQRES 13 A 249 HIS PHE LYS PRO THR GLU THR LEU LYS GLU LEU SER GLU
SEQRES 14 A 249 ALA LEU ASP THR ILE LYS GLU GLN VAL ASP GLU VAL LEU
SEQRES 15 A 249 ASP PRO ILE LEU VAL ILE GLN ALA GLU ASN ASP ASN MET
SEQRES 16 A 249 ILE ASP PRO GLN SER ALA ASN TYR ILE TYR ASP HIS VAL
SEQRES 17 A 249 ASP SER ASP ASP LYS ASN ILE LYS TRP TYR SER GLU SER
SEQRES 18 A 249 GLY HIS VAL ILE THR ILE ASP LYS GLU LYS GLU GLN VAL
SEQRES 19 A 249 PHE GLU ASP ILE TYR GLN PHE LEU GLU SER LEU ASP TRP
SEQRES 20 A 249 SER GLU
SEQRES 1 B 249 GLY PRO GLY MET GLN ILE LYS LEU PRO LYS PRO PHE PHE
SEQRES 2 B 249 PHE GLU GLU GLY LYS ARG ALA VAL LEU LEU LEU HIS GLY
SEQRES 3 B 249 PHE THR GLY ASN SER SER ASP VAL ARG GLN LEU GLY ARG
SEQRES 4 B 249 PHE LEU GLN LYS LYS GLY TYR THR SER TYR ALA PRO GLN
SEQRES 5 B 249 TYR GLU GLY HIS ALA ALA PRO PRO ASP GLU ILE LEU LYS
SEQRES 6 B 249 SER SER PRO PHE VAL TRP PHE LYS ASP ALA LEU ASP GLY
SEQRES 7 B 249 TYR ASP TYR LEU VAL GLU GLN GLY TYR ASP GLU ILE VAL
SEQRES 8 B 249 VAL ALA GLY LEU SER LEU GLY GLY ASP PHE ALA LEU LYS
SEQRES 9 B 249 LEU SER LEU ASN ARG ASP VAL LYS GLY ILE VAL THR MET
SEQRES 10 B 249 CYS ALA PRO MET GLY GLY LYS THR GLU GLY ALA ILE TYR
SEQRES 11 B 249 GLU GLY PHE LEU GLU TYR ALA ARG ASN PHE LYS LYS TYR
SEQRES 12 B 249 GLU GLY LYS ASP GLN GLU THR ILE ASP ASN GLU MET ASP
SEQRES 13 B 249 HIS PHE LYS PRO THR GLU THR LEU LYS GLU LEU SER GLU
SEQRES 14 B 249 ALA LEU ASP THR ILE LYS GLU GLN VAL ASP GLU VAL LEU
SEQRES 15 B 249 ASP PRO ILE LEU VAL ILE GLN ALA GLU ASN ASP ASN MET
SEQRES 16 B 249 ILE ASP PRO GLN SER ALA ASN TYR ILE TYR ASP HIS VAL
SEQRES 17 B 249 ASP SER ASP ASP LYS ASN ILE LYS TRP TYR SER GLU SER
SEQRES 18 B 249 GLY HIS VAL ILE THR ILE ASP LYS GLU LYS GLU GLN VAL
SEQRES 19 B 249 PHE GLU ASP ILE TYR GLN PHE LEU GLU SER LEU ASP TRP
SEQRES 20 B 249 SER GLU
HET CA A 301 1
HET CA A 302 1
HET CA A 303 1
HET CA A 304 1
HET CA B 301 1
HET CA B 302 1
HET CA B 303 1
HET CA B 304 1
HETNAM CA CALCIUM ION
FORMUL 3 CA 8(CA 2+)
FORMUL 11 HOH *541(H2 O)
HELIX 1 AA1 ASN A 27 ASP A 30 5 4
HELIX 2 AA2 VAL A 31 LYS A 41 1 11
HELIX 3 AA3 PRO A 57 LYS A 62 1 6
HELIX 4 AA4 SER A 64 GLN A 82 1 19
HELIX 5 AA5 SER A 93 LEU A 104 1 12
HELIX 6 AA6 GLY A 124 GLU A 141 1 18
HELIX 7 AA7 ASP A 144 HIS A 154 1 11
HELIX 8 AA8 PRO A 157 VAL A 175 1 19
HELIX 9 AA9 ASP A 176 VAL A 178 5 3
HELIX 10 AB1 GLN A 196 VAL A 205 1 10
HELIX 11 AB2 GLU A 227 SER A 241 1 15
HELIX 12 AB3 ASN B 27 ASP B 30 5 4
HELIX 13 AB4 VAL B 31 LYS B 41 1 11
HELIX 14 AB5 PRO B 57 LYS B 62 1 6
HELIX 15 AB6 SER B 64 GLN B 82 1 19
HELIX 16 AB7 SER B 93 LEU B 104 1 12
HELIX 17 AB8 GLY B 124 GLU B 141 1 18
HELIX 18 AB9 ASP B 144 HIS B 154 1 11
HELIX 19 AC1 PRO B 157 VAL B 175 1 19
HELIX 20 AC2 ASP B 176 VAL B 178 5 3
HELIX 21 AC3 GLN B 196 VAL B 205 1 10
HELIX 22 AC4 VAL B 221 ASP B 225 5 5
HELIX 23 AC5 GLU B 227 SER B 241 1 15
SHEET 1 AA1 7 PHE A 9 PHE A 11 0
SHEET 2 AA1 7 THR A 44 ALA A 47 -1 O SER A 45 N PHE A 11
SHEET 3 AA1 7 ALA A 17 LEU A 21 1 N LEU A 20 O TYR A 46
SHEET 4 AA1 7 ILE A 87 LEU A 92 1 O ALA A 90 N LEU A 19
SHEET 5 AA1 7 GLY A 110 MET A 114 1 O VAL A 112 N GLY A 91
SHEET 6 AA1 7 ILE A 182 ALA A 187 1 O ILE A 185 N THR A 113
SHEET 7 AA1 7 LYS A 210 TYR A 215 1 O ASN A 211 N VAL A 184
SHEET 1 AA2 7 PHE B 9 PHE B 11 0
SHEET 2 AA2 7 THR B 44 ALA B 47 -1 O ALA B 47 N PHE B 9
SHEET 3 AA2 7 ALA B 17 LEU B 21 1 N LEU B 20 O TYR B 46
SHEET 4 AA2 7 ILE B 87 LEU B 92 1 O ALA B 90 N LEU B 19
SHEET 5 AA2 7 GLY B 110 MET B 114 1 O VAL B 112 N GLY B 91
SHEET 6 AA2 7 ILE B 182 ALA B 187 1 O ILE B 185 N THR B 113
SHEET 7 AA2 7 LYS B 210 TYR B 215 1 O ASN B 211 N VAL B 184
LINK OE1 GLN A 82 CA CA A 302 1555 1555 2.31
LINK O GLU A 173 CA CA A 303 1555 1555 2.44
LINK OD1 ASP A 176 CA CA A 303 1555 1555 2.50
LINK OD2 ASP A 176 CA CA A 303 1555 1555 2.89
LINK OD1 ASP A 206 CA CA A 301 1555 1555 2.52
LINK OD1 ASP A 209 CA CA A 304 1555 1555 2.26
LINK CA CA A 301 O HOH A 406 1555 3555 2.47
LINK CA CA A 301 O HOH A 428 1555 1555 2.38
LINK CA CA A 301 O HOH A 447 1555 3555 2.33
LINK CA CA A 301 O HOH A 473 1555 3555 2.41
LINK CA CA A 301 O HOH A 529 1555 1555 2.38
LINK CA CA A 301 O HOH A 627 1555 1555 2.36
LINK CA CA A 302 O HOH A 410 1555 1555 2.40
LINK CA CA A 302 O HOH A 499 1555 1555 2.39
LINK CA CA A 302 O HOH A 631 1555 1555 2.45
LINK CA CA A 302 O HOH A 635 1555 1555 2.31
LINK CA CA A 302 O HOH A 636 1555 1555 2.49
LINK CA CA A 302 O HOH B 629 1555 1555 2.37
LINK CA CA A 303 O HOH A 403 1555 1555 2.29
LINK CA CA A 303 O HOH A 559 1555 1555 2.27
LINK CA CA A 303 O HOH A 586 1555 1555 2.42
LINK CA CA A 303 O HOH A 662 1555 1555 2.62
LINK CA CA A 304 O HOH A 421 1555 1555 2.35
LINK CA CA A 304 O HOH A 553 1555 1555 2.51
LINK CA CA A 304 O HOH A 553 1555 3555 2.51
LINK CA CA A 304 O HOH A 571 1555 1555 2.32
LINK CA CA A 304 O HOH A 614 1555 1555 2.33
LINK CA CA A 304 O HOH A 614 1555 3555 2.79
LINK CA CA A 304 O HOH A 638 1555 1555 2.14
LINK O HOH A 663 CA CA B 303 5455 1555 2.36
LINK OE1 GLN B 82 CA CA B 303 1555 1555 2.20
LINK O GLU B 173 CA CA B 304 1555 1555 2.37
LINK OD1 ASP B 176 CA CA B 304 1555 1555 2.51
LINK OD2 ASP B 176 CA CA B 304 1555 1555 2.53
LINK OD1 ASP B 206 CA CA B 301 1555 1555 2.48
LINK OD2 ASP B 209 CA CA B 302 1555 1555 2.29
LINK CA CA B 301 O HOH B 433 1555 4555 2.33
LINK CA CA B 301 O HOH B 465 1555 1555 2.35
LINK CA CA B 301 O HOH B 483 1555 4555 2.42
LINK CA CA B 301 O HOH B 488 1555 4555 2.41
LINK CA CA B 301 O HOH B 550 1555 1555 2.41
LINK CA CA B 301 O HOH B 560 1555 1555 2.40
LINK CA CA B 302 O HOH B 428 1555 1555 2.23
LINK CA CA B 302 O HOH B 475 1555 1555 2.40
LINK CA CA B 302 O HOH B 475 1555 4555 2.43
LINK CA CA B 302 O HOH B 535 1555 1555 2.37
LINK CA CA B 302 O HOH B 549 1555 1555 2.35
LINK CA CA B 302 O HOH B 576 1555 1555 2.26
LINK CA CA B 302 O HOH B 576 1555 4555 2.45
LINK CA CA B 303 O HOH B 431 1555 1555 2.41
LINK CA CA B 303 O HOH B 449 1555 1555 2.40
LINK CA CA B 303 O HOH B 589 1555 1555 2.44
LINK CA CA B 303 O HOH B 602 1555 1555 2.37
LINK CA CA B 303 O HOH B 608 1555 1555 2.48
LINK CA CA B 304 O HOH B 467 1555 1555 2.18
LINK CA CA B 304 O HOH B 504 1555 1555 2.49
LINK CA CA B 304 O HOH B 525 1555 1555 2.19
LINK CA CA B 304 O HOH B 532 1555 1555 2.42
LINK CA CA B 304 O HOH B 599 1555 1555 2.22
CRYST1 85.149 87.837 164.696 90.00 90.00 90.00 C 2 2 21 16
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 0.011744 0.000000 0.000000 0.00000
SCALE2 0.000000 0.011385 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006072 0.00000
TER 3884 GLU A 246
TER 7789 GLU B 246
MASTER 627 0 8 23 14 0 0 6 4467 2 62 40
END |