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HEADER TRANSFERASE 27-APR-20 6YUO
TITLE CAPSULE O-ACETYLTRANSFERASE OF NEISSERIA MENINGITIDIS SEROGROUP A IN
TITLE 2 COMPLEX WITH CAGED GADOLINIUM
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: SACC;
COMPND 3 CHAIN: A, B;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: NEISSERIA MENINGITIDIS SEROGROUP A;
SOURCE 3 ORGANISM_TAXID: 65699;
SOURCE 4 GENE: SACC;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008
KEYWDS O-ACETYLTRANSFERASE, A/B HYDROLASE FOLD, SERINE TRANSFERASE,
KEYWDS 2 CATALYTIC TRIAD, TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR J.T.CRAMER,T.FIEBIG,R.FEDOROV,M.MUEHLENHOFF
REVDAT 1 19-AUG-20 6YUO 0
JRNL AUTH T.FIEBIG,J.T.CRAMER,A.BETHE,P.BARUCH,U.CURTH,J.I.FUEHRING,
JRNL AUTH 2 F.F.R.BUETTNER,U.VOGEL,M.SCHUBERT,R.FEDOROV,M.MUEHLENHOFF
JRNL TITL CAPSULE O-ACETYLTRANSFERASE OF NEISSERIA MENINGITIDIS
JRNL TITL 2 SEROGROUP A IN COMPLEX WITH POLYSACCHARIDE
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.20 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.18
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 : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.20
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 19.87
REMARK 3 MIN(FOBS/SIGMA_FOBS) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 89.3
REMARK 3 NUMBER OF REFLECTIONS : 28548
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.184
REMARK 3 R VALUE (WORKING SET) : 0.182
REMARK 3 FREE R VALUE : 0.219
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 1427
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 19.8700 - 4.7200 0.91 2925 154 0.1792 0.2015
REMARK 3 2 4.7200 - 3.7600 0.90 2780 147 0.1524 0.1806
REMARK 3 3 3.7500 - 3.2800 0.88 2684 141 0.1777 0.2124
REMARK 3 4 3.2800 - 2.9800 0.92 2763 145 0.1934 0.2313
REMARK 3 5 2.9800 - 2.7700 0.90 2701 143 0.2030 0.2994
REMARK 3 6 2.7700 - 2.6100 0.88 2655 139 0.2094 0.2432
REMARK 3 7 2.6100 - 2.4800 0.91 2720 142 0.2013 0.2525
REMARK 3 8 2.4800 - 2.3700 0.88 2639 139 0.2064 0.2449
REMARK 3 9 2.3700 - 2.2800 0.87 2604 137 0.2238 0.2941
REMARK 3 10 2.2800 - 2.2000 0.89 2650 140 0.2316 0.2908
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : NULL
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) : 0.200
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 22.334
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 52.00
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 55.05
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 : 0.003 3946
REMARK 3 ANGLE : 0.606 5337
REMARK 3 CHIRALITY : 0.044 607
REMARK 3 PLANARITY : 0.003 666
REMARK 3 DIHEDRAL : 15.556 1433
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 1 THROUGH 15 )
REMARK 3 ORIGIN FOR THE GROUP (A): 52.6908 38.4805 10.6976
REMARK 3 T TENSOR
REMARK 3 T11: 0.4849 T22: 0.7964
REMARK 3 T33: 0.6627 T12: 0.1424
REMARK 3 T13: 0.0648 T23: 0.0636
REMARK 3 L TENSOR
REMARK 3 L11: 7.9288 L22: 8.1461
REMARK 3 L33: 2.0085 L12: 0.4692
REMARK 3 L13: 0.4012 L23: -0.3496
REMARK 3 S TENSOR
REMARK 3 S11: 0.0122 S12: 1.2505 S13: 0.4316
REMARK 3 S21: 0.2380 S22: -0.3684 S23: 0.9201
REMARK 3 S31: -1.1121 S32: -2.3686 S33: 0.3470
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 16 THROUGH 51 )
REMARK 3 ORIGIN FOR THE GROUP (A): 61.9450 33.5556 5.8519
REMARK 3 T TENSOR
REMARK 3 T11: 0.3142 T22: 0.3375
REMARK 3 T33: 0.2573 T12: 0.0413
REMARK 3 T13: -0.0576 T23: -0.0107
REMARK 3 L TENSOR
REMARK 3 L11: 4.0026 L22: 9.3894
REMARK 3 L33: 7.2686 L12: 0.9747
REMARK 3 L13: -2.1856 L23: -2.3375
REMARK 3 S TENSOR
REMARK 3 S11: -0.0049 S12: 0.1428 S13: 0.3982
REMARK 3 S21: -0.1867 S22: 0.0388 S23: 0.1699
REMARK 3 S31: -0.6607 S32: -0.3922 S33: -0.0594
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 52 THROUGH 65 )
REMARK 3 ORIGIN FOR THE GROUP (A): 55.9737 26.1281 2.7574
REMARK 3 T TENSOR
REMARK 3 T11: 0.3967 T22: 0.8129
REMARK 3 T33: 0.5443 T12: 0.0013
REMARK 3 T13: -0.0546 T23: -0.0028
REMARK 3 L TENSOR
REMARK 3 L11: 5.0458 L22: 2.0500
REMARK 3 L33: 8.7088 L12: 4.0387
REMARK 3 L13: -0.6031 L23: -2.2224
REMARK 3 S TENSOR
REMARK 3 S11: -0.0164 S12: 1.4339 S13: 0.5053
REMARK 3 S21: -0.3720 S22: 0.2740 S23: 1.0362
REMARK 3 S31: 0.0146 S32: -1.6859 S33: -0.4215
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 66 THROUGH 87 )
REMARK 3 ORIGIN FOR THE GROUP (A): 73.8542 40.1481 9.4355
REMARK 3 T TENSOR
REMARK 3 T11: 0.6119 T22: 0.3965
REMARK 3 T33: 0.4621 T12: -0.0579
REMARK 3 T13: -0.0428 T23: -0.0512
REMARK 3 L TENSOR
REMARK 3 L11: 7.5874 L22: 2.0916
REMARK 3 L33: 2.1108 L12: -2.6121
REMARK 3 L13: 0.8441 L23: -7.1750
REMARK 3 S TENSOR
REMARK 3 S11: -0.0290 S12: -0.5562 S13: 0.9478
REMARK 3 S21: 0.8784 S22: -0.0441 S23: -0.0129
REMARK 3 S31: -1.1573 S32: 0.5867 S33: 0.0573
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 88 THROUGH 148 )
REMARK 3 ORIGIN FOR THE GROUP (A): 70.5126 26.3090 8.6625
REMARK 3 T TENSOR
REMARK 3 T11: 0.3206 T22: 0.2548
REMARK 3 T33: 0.2184 T12: 0.0119
REMARK 3 T13: -0.0288 T23: -0.0170
REMARK 3 L TENSOR
REMARK 3 L11: 5.6583 L22: 2.2049
REMARK 3 L33: 5.0623 L12: 1.5996
REMARK 3 L13: -3.0454 L23: -1.1277
REMARK 3 S TENSOR
REMARK 3 S11: 0.0160 S12: -0.1202 S13: -0.0490
REMARK 3 S21: 0.0390 S22: -0.0140 S23: -0.0113
REMARK 3 S31: -0.0716 S32: -0.1144 S33: 0.0067
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 149 THROUGH 172 )
REMARK 3 ORIGIN FOR THE GROUP (A): 84.7077 40.4933 7.7465
REMARK 3 T TENSOR
REMARK 3 T11: 0.6680 T22: 0.4193
REMARK 3 T33: 0.5570 T12: -0.1833
REMARK 3 T13: -0.0444 T23: -0.0081
REMARK 3 L TENSOR
REMARK 3 L11: 7.3911 L22: 2.0210
REMARK 3 L33: 3.8649 L12: -2.7258
REMARK 3 L13: -0.7145 L23: -3.9709
REMARK 3 S TENSOR
REMARK 3 S11: -0.0237 S12: -0.4337 S13: 0.9741
REMARK 3 S21: -0.2271 S22: -0.4478 S23: -0.8526
REMARK 3 S31: -0.4685 S32: 0.3755 S33: 0.2984
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 173 THROUGH 214 )
REMARK 3 ORIGIN FOR THE GROUP (A): 80.6443 20.6686 3.5259
REMARK 3 T TENSOR
REMARK 3 T11: 0.3227 T22: 0.3273
REMARK 3 T33: 0.3575 T12: 0.0653
REMARK 3 T13: 0.0313 T23: -0.0017
REMARK 3 L TENSOR
REMARK 3 L11: 3.5141 L22: 5.0283
REMARK 3 L33: 7.6059 L12: 1.4145
REMARK 3 L13: -0.4315 L23: -0.2296
REMARK 3 S TENSOR
REMARK 3 S11: -0.0439 S12: 0.0888 S13: -0.2589
REMARK 3 S21: 0.0884 S22: -0.0494 S23: -0.2978
REMARK 3 S31: 0.0518 S32: 0.4184 S33: 0.0698
REMARK 3 TLS GROUP : 8
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 215 THROUGH 229 )
REMARK 3 ORIGIN FOR THE GROUP (A): 76.3531 18.3453 -3.2293
REMARK 3 T TENSOR
REMARK 3 T11: 0.5074 T22: 0.3757
REMARK 3 T33: 0.3235 T12: 0.1212
REMARK 3 T13: 0.0195 T23: -0.0886
REMARK 3 L TENSOR
REMARK 3 L11: 9.3619 L22: 3.5405
REMARK 3 L33: 6.0289 L12: -2.1391
REMARK 3 L13: 5.6479 L23: -4.1211
REMARK 3 S TENSOR
REMARK 3 S11: 0.0949 S12: 0.4502 S13: -0.4740
REMARK 3 S21: -0.0928 S22: 0.4926 S23: -0.1449
REMARK 3 S31: -0.2143 S32: -0.2884 S33: -0.4826
REMARK 3 TLS GROUP : 9
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 230 THROUGH 246 )
REMARK 3 ORIGIN FOR THE GROUP (A): 64.4867 20.2891 -5.8205
REMARK 3 T TENSOR
REMARK 3 T11: 0.4247 T22: 0.5565
REMARK 3 T33: 0.4253 T12: -0.0312
REMARK 3 T13: -0.0503 T23: -0.0795
REMARK 3 L TENSOR
REMARK 3 L11: 7.3484 L22: 2.0528
REMARK 3 L33: 7.1727 L12: 0.0579
REMARK 3 L13: -1.8677 L23: -2.5897
REMARK 3 S TENSOR
REMARK 3 S11: 0.2543 S12: 0.5745 S13: -0.5202
REMARK 3 S21: -0.8057 S22: 0.0568 S23: 0.7046
REMARK 3 S31: 0.1857 S32: -1.0804 S33: -0.1709
REMARK 3 TLS GROUP : 10
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 1 THROUGH 47 )
REMARK 3 ORIGIN FOR THE GROUP (A): 61.0832 24.5438 33.9867
REMARK 3 T TENSOR
REMARK 3 T11: 0.3037 T22: 0.3234
REMARK 3 T33: 0.2860 T12: -0.0237
REMARK 3 T13: 0.0209 T23: 0.0298
REMARK 3 L TENSOR
REMARK 3 L11: 1.2117 L22: 4.7069
REMARK 3 L33: 5.0493 L12: 1.1381
REMARK 3 L13: 0.8245 L23: 2.3173
REMARK 3 S TENSOR
REMARK 3 S11: 0.0601 S12: -0.0913 S13: -0.1328
REMARK 3 S21: 0.0094 S22: 0.0320 S23: 0.0288
REMARK 3 S31: 0.1438 S32: 0.0067 S33: -0.1057
REMARK 3 TLS GROUP : 11
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 48 THROUGH 87 )
REMARK 3 ORIGIN FOR THE GROUP (A): 65.4023 29.7160 37.0020
REMARK 3 T TENSOR
REMARK 3 T11: 0.4028 T22: 0.3497
REMARK 3 T33: 0.2465 T12: -0.0284
REMARK 3 T13: -0.0088 T23: -0.0431
REMARK 3 L TENSOR
REMARK 3 L11: 7.2294 L22: 3.8271
REMARK 3 L33: 3.1615 L12: -0.3080
REMARK 3 L13: 2.5815 L23: -1.3185
REMARK 3 S TENSOR
REMARK 3 S11: 0.1623 S12: -0.7901 S13: -0.1893
REMARK 3 S21: 0.1803 S22: -0.1249 S23: 0.0534
REMARK 3 S31: 0.0197 S32: -0.1607 S33: 0.0115
REMARK 3 TLS GROUP : 12
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 88 THROUGH 114 )
REMARK 3 ORIGIN FOR THE GROUP (A): 58.6847 36.4385 29.4912
REMARK 3 T TENSOR
REMARK 3 T11: 0.4389 T22: 0.3453
REMARK 3 T33: 0.3898 T12: 0.0463
REMARK 3 T13: 0.0506 T23: -0.0064
REMARK 3 L TENSOR
REMARK 3 L11: 5.8892 L22: 4.1907
REMARK 3 L33: 7.2744 L12: 1.8662
REMARK 3 L13: 0.6750 L23: 3.6854
REMARK 3 S TENSOR
REMARK 3 S11: -0.0052 S12: -0.0351 S13: 0.5054
REMARK 3 S21: -0.0808 S22: -0.0459 S23: 0.3757
REMARK 3 S31: -0.4163 S32: -0.6528 S33: 0.0481
REMARK 3 TLS GROUP : 13
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 115 THROUGH 214 )
REMARK 3 ORIGIN FOR THE GROUP (A): 71.9583 43.4373 39.8650
REMARK 3 T TENSOR
REMARK 3 T11: 0.4173 T22: 0.3692
REMARK 3 T33: 0.3959 T12: -0.0811
REMARK 3 T13: 0.0067 T23: -0.0747
REMARK 3 L TENSOR
REMARK 3 L11: 6.1543 L22: 2.4936
REMARK 3 L33: 2.8555 L12: -1.3164
REMARK 3 L13: 0.3882 L23: -0.3865
REMARK 3 S TENSOR
REMARK 3 S11: 0.0392 S12: -0.5852 S13: 0.7468
REMARK 3 S21: 0.3083 S22: -0.1131 S23: -0.3314
REMARK 3 S31: -0.4884 S32: 0.1697 S33: 0.0704
REMARK 3 TLS GROUP : 14
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 215 THROUGH 244 )
REMARK 3 ORIGIN FOR THE GROUP (A): 58.1179 42.3774 47.8861
REMARK 3 T TENSOR
REMARK 3 T11: 0.5189 T22: 0.6248
REMARK 3 T33: 0.5485 T12: 0.0679
REMARK 3 T13: 0.0514 T23: -0.1931
REMARK 3 L TENSOR
REMARK 3 L11: 5.0964 L22: 2.4568
REMARK 3 L33: 4.7279 L12: 0.6443
REMARK 3 L13: 0.1298 L23: -1.4568
REMARK 3 S TENSOR
REMARK 3 S11: -0.1192 S12: -0.8532 S13: 0.5857
REMARK 3 S21: 0.5740 S22: 0.0600 S23: 0.1651
REMARK 3 S31: -0.6031 S32: -0.6585 S33: -0.0256
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 6YUO COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 27-APR-20.
REMARK 100 THE DEPOSITION ID IS D_1292108326.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 16-APR-16
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : ID30B
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.71177
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 6M-F
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 28553
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.200
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 89.3
REMARK 200 DATA REDUNDANCY : 24.50
REMARK 200 R MERGE (I) : 0.08600
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 26.5000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.20
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.28
REMARK 200 COMPLETENESS FOR SHELL (%) : 89.6
REMARK 200 DATA REDUNDANCY IN SHELL : 25.50
REMARK 200 R MERGE FOR SHELL (I) : 0.95200
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 3.900
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD
REMARK 200 SOFTWARE USED: CRANK2
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 52.77
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.60
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: NATIVE WILD TYPE CSAC CRYSTALLIZED IN
REMARK 280 SITTING DROP SETUPS AT CONCENTRATIONS OF 18 MG/ML. FINE SCREENS
REMARK 280 AROUND INITIAL SCREENING CONDITIONS RESULTED IN MANY ISOMORPHOUS
REMARK 280 CRYSTALS. MOTHER LIQUOR CONTAINED 50 MM HEPES PH 7.0, 100 MM
REMARK 280 HEPES PH 7.6, 100 MM NACL, 5 MM MGCL2, 1 MM EDTA, AND 31-42%
REMARK 280 PEG200., VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 291.15K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 41 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+1/4
REMARK 290 4555 Y+1/2,-X+1/2,Z+3/4
REMARK 290 5555 -X+1/2,Y+1/2,-Z+1/4
REMARK 290 6555 X+1/2,-Y+1/2,-Z+3/4
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 34.63500
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 66.46500
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 66.46500
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 17.31750
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 66.46500
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 66.46500
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 51.95250
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 66.46500
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 66.46500
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 17.31750
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 66.46500
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 66.46500
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 51.95250
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 34.63500
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: TETRAMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, 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 APPLY THE FOLLOWING TO CHAINS: A, B
REMARK 350 BIOMT1 2 0.000000 -1.000000 0.000000 132.93000
REMARK 350 BIOMT2 2 -1.000000 0.000000 0.000000 132.93000
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 34.63500
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 THR A 159
REMARK 465 SER A 160
REMARK 465 LYS A 161
REMARK 465 ARG A 162
REMARK 465 PHE A 163
REMARK 465 ILE A 247
REMARK 465 LEU A 248
REMARK 465 GLU A 249
REMARK 465 HIS A 250
REMARK 465 HIS A 251
REMARK 465 HIS A 252
REMARK 465 HIS A 253
REMARK 465 HIS A 254
REMARK 465 HIS A 255
REMARK 465 GLN B 245
REMARK 465 ASN B 246
REMARK 465 ILE B 247
REMARK 465 LEU B 248
REMARK 465 GLU B 249
REMARK 465 HIS B 250
REMARK 465 HIS B 251
REMARK 465 HIS B 252
REMARK 465 HIS B 253
REMARK 465 HIS B 254
REMARK 465 HIS B 255
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 A 31 CD OE1 OE2
REMARK 470 GLU A 72 CG CD OE1 OE2
REMARK 470 GLU A 84 CD OE1 OE2
REMARK 470 GLN A 164 CG CD OE1 NE2
REMARK 470 ASP A 165 CG OD1 OD2
REMARK 470 ILE A 166 CG1 CG2 CD1
REMARK 470 LYS A 187 CG CD CE NZ
REMARK 470 GLU A 231 CG CD OE1 OE2
REMARK 470 GLU A 238 CG CD OE1 OE2
REMARK 470 ASN A 246 CG OD1 ND2
REMARK 470 GLU B 31 CG CD OE1 OE2
REMARK 470 GLU B 72 CG CD OE1 OE2
REMARK 470 GLU B 84 OE1 OE2
REMARK 470 LYS B 196 CG CD CE NZ
REMARK 470 LYS B 220 CD CE NZ
REMARK 470 GLU B 238 CG CD OE1 OE2
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 31 -62.62 71.12
REMARK 500 ASP A 74 77.32 -151.48
REMARK 500 SER A 114 -122.57 54.33
REMARK 500 SER A 149 107.77 -162.55
REMARK 500 GLU B 31 -57.68 72.63
REMARK 500 ASP B 74 73.77 -156.41
REMARK 500 SER B 114 -114.70 55.12
REMARK 500 ASP B 198 79.54 -107.13
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL A 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL B 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PEG B 303
DBREF 6YUO A 1 247 UNP O68216 O68216_NEIMD 1 247
DBREF 6YUO B 1 247 UNP O68216 O68216_NEIMD 1 247
SEQADV 6YUO LEU A 248 UNP O68216 EXPRESSION TAG
SEQADV 6YUO GLU A 249 UNP O68216 EXPRESSION TAG
SEQADV 6YUO HIS A 250 UNP O68216 EXPRESSION TAG
SEQADV 6YUO HIS A 251 UNP O68216 EXPRESSION TAG
SEQADV 6YUO HIS A 252 UNP O68216 EXPRESSION TAG
SEQADV 6YUO HIS A 253 UNP O68216 EXPRESSION TAG
SEQADV 6YUO HIS A 254 UNP O68216 EXPRESSION TAG
SEQADV 6YUO HIS A 255 UNP O68216 EXPRESSION TAG
SEQADV 6YUO LEU B 248 UNP O68216 EXPRESSION TAG
SEQADV 6YUO GLU B 249 UNP O68216 EXPRESSION TAG
SEQADV 6YUO HIS B 250 UNP O68216 EXPRESSION TAG
SEQADV 6YUO HIS B 251 UNP O68216 EXPRESSION TAG
SEQADV 6YUO HIS B 252 UNP O68216 EXPRESSION TAG
SEQADV 6YUO HIS B 253 UNP O68216 EXPRESSION TAG
SEQADV 6YUO HIS B 254 UNP O68216 EXPRESSION TAG
SEQADV 6YUO HIS B 255 UNP O68216 EXPRESSION TAG
SEQRES 1 A 255 MET LEU SER ASN LEU LYS THR GLY ASN ASN ILE LEU GLY
SEQRES 2 A 255 LEU PRO GLU PHE GLU LEU ASN GLY CYS ARG PHE LEU TYR
SEQRES 3 A 255 LYS LYS GLY ILE GLU LYS THR ILE ILE THR PHE SER ALA
SEQRES 4 A 255 PHE PRO PRO LYS ASP ILE ALA GLN LYS TYR ASN TYR ILE
SEQRES 5 A 255 LYS ASP PHE LEU SER SER ASN TYR THR PHE LEU ALA PHE
SEQRES 6 A 255 LEU ASP THR LYS TYR PRO GLU ASP ASP ALA ARG GLY THR
SEQRES 7 A 255 TYR TYR ILE THR ASN GLU LEU ASP ASN GLY TYR LEU GLN
SEQRES 8 A 255 THR ILE HIS CYS ILE ILE GLN LEU LEU SER ASN THR ASN
SEQRES 9 A 255 GLN GLU ASP THR TYR LEU LEU GLY SER SER LYS GLY GLY
SEQRES 10 A 255 VAL GLY ALA LEU LEU LEU GLY LEU THR TYR ASN TYR PRO
SEQRES 11 A 255 ASN ILE ILE ILE ASN ALA PRO GLN ALA LYS LEU ALA ASP
SEQRES 12 A 255 TYR ILE LYS THR ARG SER LYS THR ILE LEU SER TYR MET
SEQRES 13 A 255 LEU GLY THR SER LYS ARG PHE GLN ASP ILE ASN TYR ASP
SEQRES 14 A 255 TYR ILE ASN ASP PHE LEU LEU SER LYS ILE LYS THR CYS
SEQRES 15 A 255 ASP SER SER LEU LYS TRP ASN ILE HIS ILE THR CYS GLY
SEQRES 16 A 255 LYS ASP ASP SER TYR HIS LEU ASN GLU LEU GLU ILE LEU
SEQRES 17 A 255 LYS ASN GLU PHE ASN ILE LYS ALA ILE THR ILE LYS THR
SEQRES 18 A 255 LYS LEU ILE SER GLY GLY HIS ASP ASN GLU ALA ILE ALA
SEQRES 19 A 255 HIS TYR ARG GLU TYR PHE LYS THR ILE ILE GLN ASN ILE
SEQRES 20 A 255 LEU GLU HIS HIS HIS HIS HIS HIS
SEQRES 1 B 255 MET LEU SER ASN LEU LYS THR GLY ASN ASN ILE LEU GLY
SEQRES 2 B 255 LEU PRO GLU PHE GLU LEU ASN GLY CYS ARG PHE LEU TYR
SEQRES 3 B 255 LYS LYS GLY ILE GLU LYS THR ILE ILE THR PHE SER ALA
SEQRES 4 B 255 PHE PRO PRO LYS ASP ILE ALA GLN LYS TYR ASN TYR ILE
SEQRES 5 B 255 LYS ASP PHE LEU SER SER ASN TYR THR PHE LEU ALA PHE
SEQRES 6 B 255 LEU ASP THR LYS TYR PRO GLU ASP ASP ALA ARG GLY THR
SEQRES 7 B 255 TYR TYR ILE THR ASN GLU LEU ASP ASN GLY TYR LEU GLN
SEQRES 8 B 255 THR ILE HIS CYS ILE ILE GLN LEU LEU SER ASN THR ASN
SEQRES 9 B 255 GLN GLU ASP THR TYR LEU LEU GLY SER SER LYS GLY GLY
SEQRES 10 B 255 VAL GLY ALA LEU LEU LEU GLY LEU THR TYR ASN TYR PRO
SEQRES 11 B 255 ASN ILE ILE ILE ASN ALA PRO GLN ALA LYS LEU ALA ASP
SEQRES 12 B 255 TYR ILE LYS THR ARG SER LYS THR ILE LEU SER TYR MET
SEQRES 13 B 255 LEU GLY THR SER LYS ARG PHE GLN ASP ILE ASN TYR ASP
SEQRES 14 B 255 TYR ILE ASN ASP PHE LEU LEU SER LYS ILE LYS THR CYS
SEQRES 15 B 255 ASP SER SER LEU LYS TRP ASN ILE HIS ILE THR CYS GLY
SEQRES 16 B 255 LYS ASP ASP SER TYR HIS LEU ASN GLU LEU GLU ILE LEU
SEQRES 17 B 255 LYS ASN GLU PHE ASN ILE LYS ALA ILE THR ILE LYS THR
SEQRES 18 B 255 LYS LEU ILE SER GLY GLY HIS ASP ASN GLU ALA ILE ALA
SEQRES 19 B 255 HIS TYR ARG GLU TYR PHE LYS THR ILE ILE GLN ASN ILE
SEQRES 20 B 255 LEU GLU HIS HIS HIS HIS HIS HIS
HET CL A 301 1
HET EDO A 302 4
HET GD3 B 301 1
HET CL B 302 1
HET PEG B 303 7
HET GD3 B 304 1
HETNAM CL CHLORIDE ION
HETNAM EDO 1,2-ETHANEDIOL
HETNAM GD3 GADOLINIUM ION
HETNAM PEG DI(HYDROXYETHYL)ETHER
HETSYN EDO ETHYLENE GLYCOL
FORMUL 3 CL 2(CL 1-)
FORMUL 4 EDO C2 H6 O2
FORMUL 5 GD3 2(GD 3+)
FORMUL 7 PEG C4 H10 O3
FORMUL 9 HOH *80(H2 O)
HELIX 1 AA1 MET A 1 ASN A 4 5 4
HELIX 2 AA2 TYR A 51 LEU A 56 1 6
HELIX 3 AA3 PRO A 71 ALA A 75 5 5
HELIX 4 AA4 ASN A 87 SER A 101 1 15
HELIX 5 AA5 ASN A 104 GLU A 106 5 3
HELIX 6 AA6 SER A 114 ASN A 128 1 15
HELIX 7 AA7 LYS A 140 SER A 149 1 10
HELIX 8 AA8 SER A 149 GLY A 158 1 10
HELIX 9 AA9 ASP A 165 ASP A 173 1 9
HELIX 10 AB1 ASP A 173 CYS A 182 1 10
HELIX 11 AB2 ASP A 198 LYS A 215 1 18
HELIX 12 AB3 ASP A 229 ASN A 246 1 18
HELIX 13 AB4 MET B 1 ASN B 4 5 4
HELIX 14 AB5 ILE B 52 SER B 57 1 6
HELIX 15 AB6 PRO B 71 ALA B 75 5 5
HELIX 16 AB7 ASN B 87 SER B 101 1 15
HELIX 17 AB8 ASN B 104 GLU B 106 5 3
HELIX 18 AB9 SER B 114 ASN B 128 1 15
HELIX 19 AC1 LYS B 140 SER B 149 1 10
HELIX 20 AC2 SER B 149 GLY B 158 1 10
HELIX 21 AC3 PHE B 163 ASP B 173 1 11
HELIX 22 AC4 ASP B 173 CYS B 182 1 10
HELIX 23 AC5 ASP B 198 LYS B 215 1 18
HELIX 24 AC6 ASP B 229 ILE B 244 1 16
SHEET 1 AA1 9 LYS A 6 ILE A 11 0
SHEET 2 AA1 9 LEU A 14 LEU A 19 -1 O LEU A 14 N ILE A 11
SHEET 3 AA1 9 CYS A 22 LYS A 27 -1 O PHE A 24 N PHE A 17
SHEET 4 AA1 9 TYR A 60 PHE A 65 -1 O PHE A 62 N LYS A 27
SHEET 5 AA1 9 ILE A 30 PHE A 37 1 N ILE A 34 O THR A 61
SHEET 6 AA1 9 THR A 108 SER A 113 1 O LEU A 111 N ILE A 35
SHEET 7 AA1 9 ASN A 131 ASN A 135 1 O ILE A 133 N LEU A 110
SHEET 8 AA1 9 ASN A 189 GLY A 195 1 O HIS A 191 N ILE A 132
SHEET 9 AA1 9 LYS A 220 ILE A 224 1 O LYS A 220 N ILE A 190
SHEET 1 AA2 9 LYS B 6 ILE B 11 0
SHEET 2 AA2 9 LEU B 14 LEU B 19 -1 O LEU B 14 N ILE B 11
SHEET 3 AA2 9 CYS B 22 LYS B 27 -1 O PHE B 24 N PHE B 17
SHEET 4 AA2 9 THR B 61 PHE B 65 -1 O PHE B 62 N LYS B 27
SHEET 5 AA2 9 THR B 33 PHE B 37 1 N ILE B 34 O THR B 61
SHEET 6 AA2 9 THR B 108 SER B 113 1 O LEU B 111 N ILE B 35
SHEET 7 AA2 9 ASN B 131 ASN B 135 1 O ILE B 133 N LEU B 110
SHEET 8 AA2 9 ASN B 189 GLY B 195 1 O HIS B 191 N ILE B 132
SHEET 9 AA2 9 LYS B 220 ILE B 224 1 O ILE B 224 N CYS B 194
CISPEP 1 TYR A 70 PRO A 71 0 -0.32
CISPEP 2 TYR B 70 PRO B 71 0 -0.35
SITE 1 AC1 4 PHE A 40 SER A 114 LYS A 115 ARG A 148
SITE 1 AC2 2 LYS A 222 TYR A 239
SITE 1 AC3 4 PHE B 40 SER B 114 LYS B 115 ARG B 148
SITE 1 AC4 4 ASN B 83 TYR B 155 MET B 156 GLY B 158
CRYST1 132.930 132.930 69.270 90.00 90.00 90.00 P 41 21 2 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 0.007523 0.000000 0.000000 0.00000
SCALE2 0.000000 0.007523 0.000000 0.00000
SCALE3 0.000000 0.000000 0.014436 0.00000
TER 1909 ASN A 246
TER 3859 ILE B 244
MASTER 526 0 6 24 18 0 4 6 3952 2 11 40
END |