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HEADER TRANSFERASE 27-APR-20 6YUS
TITLE CAPSULE O-ACETYLTRANSFERASE OF NEISSERIA MENINGITIDIS SEROGROUP A
TITLE 2 H228A MUTANT IN COMPLEX WITH COA
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 6YUS 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. 2.00 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 : GEOSTD + MONOMER LIBRARY + CDL V1.2
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.00
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 49.16
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.330
REMARK 3 COMPLETENESS FOR RANGE (%) : 97.7
REMARK 3 NUMBER OF REFLECTIONS : 44759
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.199
REMARK 3 R VALUE (WORKING SET) : 0.198
REMARK 3 FREE R VALUE : 0.240
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 2239
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 49.1600 - 5.0400 1.00 2930 155 0.1748 0.2357
REMARK 3 2 5.0400 - 4.0000 1.00 2807 148 0.1628 0.1790
REMARK 3 3 4.0000 - 3.4900 1.00 2748 143 0.1822 0.2516
REMARK 3 4 3.4900 - 3.1700 1.00 2725 144 0.2136 0.2420
REMARK 3 5 3.1700 - 2.9500 1.00 2732 144 0.2266 0.2628
REMARK 3 6 2.9500 - 2.7700 1.00 2710 142 0.2226 0.2805
REMARK 3 7 2.7700 - 2.6300 1.00 2699 143 0.2226 0.2627
REMARK 3 8 2.6300 - 2.5200 1.00 2702 142 0.2246 0.2853
REMARK 3 9 2.5200 - 2.4200 1.00 2711 143 0.2333 0.2524
REMARK 3 10 2.4200 - 2.3400 1.00 2673 140 0.2392 0.2667
REMARK 3 11 2.3400 - 2.2700 1.00 2696 142 0.2516 0.3131
REMARK 3 12 2.2700 - 2.2000 1.00 2663 140 0.2798 0.2737
REMARK 3 13 2.2000 - 2.1400 1.00 2665 141 0.3086 0.3352
REMARK 3 14 2.1400 - 2.0900 1.00 2701 141 0.3365 0.3270
REMARK 3 15 2.0900 - 2.0400 0.96 2575 137 0.3875 0.4026
REMARK 3 16 2.0400 - 2.0000 0.67 1783 94 0.4323 0.4361
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.11
REMARK 3 SHRINKAGE RADIUS : 0.90
REMARK 3 K_SOL : NULL
REMARK 3 B_SOL : NULL
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.324
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 28.646
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 64.03
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 77.54
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 : 0.010 4062
REMARK 3 ANGLE : 1.140 5519
REMARK 3 CHIRALITY : 0.062 623
REMARK 3 PLANARITY : 0.006 682
REMARK 3 DIHEDRAL : 17.663 1441
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 12
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 1 THROUGH 11 )
REMARK 3 ORIGIN FOR THE GROUP (A): 11.4078 28.2896 -22.2268
REMARK 3 T TENSOR
REMARK 3 T11: 0.7249 T22: 1.2838
REMARK 3 T33: 1.0398 T12: 0.3315
REMARK 3 T13: -0.1260 T23: -0.4386
REMARK 3 L TENSOR
REMARK 3 L11: 5.8983 L22: 5.1465
REMARK 3 L33: 2.2839 L12: -0.7588
REMARK 3 L13: -3.2704 L23: 0.4993
REMARK 3 S TENSOR
REMARK 3 S11: 0.3836 S12: 1.3951 S13: -1.4011
REMARK 3 S21: -0.3835 S22: 0.6501 S23: -0.8445
REMARK 3 S31: 1.7779 S32: 3.1516 S33: -1.0822
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 12 THROUGH 52 )
REMARK 3 ORIGIN FOR THE GROUP (A): 3.6527 34.7544 -29.5663
REMARK 3 T TENSOR
REMARK 3 T11: 0.6395 T22: 1.0952
REMARK 3 T33: 0.6759 T12: 0.0077
REMARK 3 T13: -0.0689 T23: -0.3956
REMARK 3 L TENSOR
REMARK 3 L11: 1.9016 L22: 3.1293
REMARK 3 L33: 4.2736 L12: -1.3459
REMARK 3 L13: 0.1298 L23: 0.1177
REMARK 3 S TENSOR
REMARK 3 S11: 0.1015 S12: 0.9819 S13: -0.5879
REMARK 3 S21: -0.5277 S22: 0.3309 S23: -0.2267
REMARK 3 S31: 0.4917 S32: 0.9760 S33: -0.4709
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 53 THROUGH 70 )
REMARK 3 ORIGIN FOR THE GROUP (A): 4.7716 38.0871 -30.4224
REMARK 3 T TENSOR
REMARK 3 T11: 0.6717 T22: 1.2989
REMARK 3 T33: 0.6562 T12: -0.0027
REMARK 3 T13: -0.0474 T23: -0.4061
REMARK 3 L TENSOR
REMARK 3 L11: 3.2870 L22: 1.9170
REMARK 3 L33: 7.6244 L12: -1.8243
REMARK 3 L13: 0.8909 L23: 2.1326
REMARK 3 S TENSOR
REMARK 3 S11: -0.1229 S12: 1.5818 S13: -0.9120
REMARK 3 S21: -0.6514 S22: 0.5415 S23: -0.6761
REMARK 3 S31: -0.0617 S32: 1.6307 S33: -0.3731
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 71 THROUGH 149 )
REMARK 3 ORIGIN FOR THE GROUP (A): -7.1791 38.5120 -26.4576
REMARK 3 T TENSOR
REMARK 3 T11: 0.4427 T22: 0.5374
REMARK 3 T33: 0.4093 T12: -0.0010
REMARK 3 T13: -0.0836 T23: -0.1196
REMARK 3 L TENSOR
REMARK 3 L11: 5.4870 L22: 4.3581
REMARK 3 L33: 6.1130 L12: 1.3621
REMARK 3 L13: 0.8193 L23: 0.1590
REMARK 3 S TENSOR
REMARK 3 S11: -0.0293 S12: 0.7373 S13: -0.4109
REMARK 3 S21: -0.2127 S22: 0.5144 S23: -0.1364
REMARK 3 S31: 0.3690 S32: 0.6658 S33: -0.4500
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 150 THROUGH 172 )
REMARK 3 ORIGIN FOR THE GROUP (A): -22.3323 27.6752 -25.7743
REMARK 3 T TENSOR
REMARK 3 T11: 0.8680 T22: 0.5819
REMARK 3 T33: 0.8727 T12: -0.1963
REMARK 3 T13: -0.2053 T23: 0.0333
REMARK 3 L TENSOR
REMARK 3 L11: 7.3094 L22: 4.4304
REMARK 3 L33: 9.8681 L12: -3.7602
REMARK 3 L13: -0.4645 L23: 3.6211
REMARK 3 S TENSOR
REMARK 3 S11: -0.1431 S12: 0.2360 S13: -1.7303
REMARK 3 S21: 0.2469 S22: -0.0169 S23: 0.8953
REMARK 3 S31: 1.1861 S32: -0.6210 S33: -0.0192
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 173 THROUGH 229 )
REMARK 3 ORIGIN FOR THE GROUP (A): -14.6742 48.7124 -33.2823
REMARK 3 T TENSOR
REMARK 3 T11: 0.5772 T22: 0.6753
REMARK 3 T33: 0.4722 T12: -0.2030
REMARK 3 T13: -0.1310 T23: 0.0746
REMARK 3 L TENSOR
REMARK 3 L11: 3.6874 L22: 3.5815
REMARK 3 L33: 5.2966 L12: -0.2549
REMARK 3 L13: 0.3927 L23: -0.9244
REMARK 3 S TENSOR
REMARK 3 S11: -0.3848 S12: 1.1101 S13: 0.0131
REMARK 3 S21: -0.6539 S22: 0.4505 S23: 0.2218
REMARK 3 S31: -0.3099 S32: 0.0804 S33: -0.0992
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 230 THROUGH 245 )
REMARK 3 ORIGIN FOR THE GROUP (A): -0.0097 47.4797 -41.2967
REMARK 3 T TENSOR
REMARK 3 T11: 0.7879 T22: 1.3434
REMARK 3 T33: 0.4794 T12: -0.4050
REMARK 3 T13: 0.0743 T23: -0.0836
REMARK 3 L TENSOR
REMARK 3 L11: 8.0889 L22: 9.8147
REMARK 3 L33: 9.4170 L12: -4.2122
REMARK 3 L13: 2.5377 L23: 0.7013
REMARK 3 S TENSOR
REMARK 3 S11: -0.3211 S12: 1.2319 S13: 0.0212
REMARK 3 S21: -1.1785 S22: 0.5790 S23: -0.5437
REMARK 3 S31: -0.4254 S32: 1.6637 S33: -0.3259
REMARK 3 TLS GROUP : 8
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 1 THROUGH 52 )
REMARK 3 ORIGIN FOR THE GROUP (A): 4.5012 42.5927 -0.1229
REMARK 3 T TENSOR
REMARK 3 T11: 0.4480 T22: 0.5771
REMARK 3 T33: 0.5441 T12: 0.0625
REMARK 3 T13: -0.1822 T23: -0.1584
REMARK 3 L TENSOR
REMARK 3 L11: 1.9045 L22: 2.4497
REMARK 3 L33: 5.2397 L12: 0.7166
REMARK 3 L13: -3.1376 L23: -0.3815
REMARK 3 S TENSOR
REMARK 3 S11: 0.2129 S12: 0.0324 S13: -0.2262
REMARK 3 S21: 0.2847 S22: -0.1369 S23: -0.2390
REMARK 3 S31: -0.0798 S32: 0.1161 S33: -0.0900
REMARK 3 TLS GROUP : 9
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 53 THROUGH 65 )
REMARK 3 ORIGIN FOR THE GROUP (A): 13.2537 37.7361 2.9294
REMARK 3 T TENSOR
REMARK 3 T11: 0.6205 T22: 0.8218
REMARK 3 T33: 0.7205 T12: 0.0270
REMARK 3 T13: -0.2204 T23: -0.0381
REMARK 3 L TENSOR
REMARK 3 L11: 7.6923 L22: 4.9482
REMARK 3 L33: 2.0422 L12: -4.0846
REMARK 3 L13: -8.6949 L23: 3.0470
REMARK 3 S TENSOR
REMARK 3 S11: 0.3850 S12: -0.5346 S13: 0.4397
REMARK 3 S21: 0.6463 S22: 0.0046 S23: -0.8149
REMARK 3 S31: 0.0895 S32: 1.2648 S33: -0.4338
REMARK 3 TLS GROUP : 10
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 66 THROUGH 172 )
REMARK 3 ORIGIN FOR THE GROUP (A): -6.8405 31.6686 0.2651
REMARK 3 T TENSOR
REMARK 3 T11: 0.6156 T22: 0.5403
REMARK 3 T33: 0.6094 T12: 0.0217
REMARK 3 T13: -0.0985 T23: -0.1931
REMARK 3 L TENSOR
REMARK 3 L11: 4.1362 L22: 2.0535
REMARK 3 L33: 2.8901 L12: 1.3737
REMARK 3 L13: -1.1038 L23: -0.2337
REMARK 3 S TENSOR
REMARK 3 S11: -0.0525 S12: 0.2746 S13: -0.4732
REMARK 3 S21: 0.1729 S22: -0.1550 S23: 0.1195
REMARK 3 S31: 0.4820 S32: -0.2408 S33: 0.2077
REMARK 3 TLS GROUP : 11
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 173 THROUGH 188 )
REMARK 3 ORIGIN FOR THE GROUP (A): -3.7778 18.3154 -2.5550
REMARK 3 T TENSOR
REMARK 3 T11: 0.9716 T22: 0.5418
REMARK 3 T33: 0.8611 T12: 0.0032
REMARK 3 T13: -0.0416 T23: -0.1753
REMARK 3 L TENSOR
REMARK 3 L11: 9.0862 L22: 8.3862
REMARK 3 L33: 5.5862 L12: -6.8565
REMARK 3 L13: -4.8493 L23: 3.5544
REMARK 3 S TENSOR
REMARK 3 S11: 0.0365 S12: 1.0925 S13: -1.4682
REMARK 3 S21: -0.4107 S22: -0.7356 S23: 0.2522
REMARK 3 S31: 0.9522 S32: -0.7323 S33: 0.8728
REMARK 3 TLS GROUP : 12
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 189 THROUGH 244 )
REMARK 3 ORIGIN FOR THE GROUP (A): 2.1102 22.0890 12.5097
REMARK 3 T TENSOR
REMARK 3 T11: 0.8212 T22: 0.5468
REMARK 3 T33: 0.6426 T12: 0.1238
REMARK 3 T13: -0.0120 T23: 0.0971
REMARK 3 L TENSOR
REMARK 3 L11: 6.0076 L22: 6.0580
REMARK 3 L33: 6.9140 L12: 0.1730
REMARK 3 L13: -2.5215 L23: -0.9894
REMARK 3 S TENSOR
REMARK 3 S11: -0.4308 S12: -0.5013 S13: -0.8691
REMARK 3 S21: 0.7676 S22: 0.0522 S23: -0.3112
REMARK 3 S31: 1.3362 S32: 0.4323 S33: 0.3331
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 6YUS 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_1292108329.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 19-OCT-18
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 : PETRA III, EMBL C/O DESY
REMARK 200 BEAMLINE : P13 (MX1)
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.976247
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, XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 45806
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.000
REMARK 200 RESOLUTION RANGE LOW (A) : 49.190
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 23.50
REMARK 200 R MERGE (I) : 0.08000
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 20.8000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.00
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.13
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.9
REMARK 200 DATA REDUNDANCY IN SHELL : 14.80
REMARK 200 R MERGE FOR SHELL (I) : 4.50100
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 0.500
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: 6YUQ
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 56.34
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.82
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: NATIVE H228A MUTANT CSAC CRYSTALLIZED
REMARK 280 IN SITTING DROP SETUPS AT CONCENTRATIONS OF 18 MG/ML. FINE
REMARK 280 SCREENS AROUND INITIAL SCREENING CONDITIONS RESULTED IN MANY
REMARK 280 ISOMORPHOUS CRYSTALS. MOTHER LIQUOR CONTAINED 50 MM HEPES PH 7.0,
REMARK 280 100 MM HEPES PH 7.6, 100 MM NACL, 5 MM MGCL2, 1 MM EDTA, AND 31-
REMARK 280 42% 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 35.38000
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 68.37000
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 68.37000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 17.69000
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 68.37000
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 68.37000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 53.07000
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 68.37000
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 68.37000
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 17.69000
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 68.37000
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 68.37000
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 53.07000
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 35.38000
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 0.00000
REMARK 350 BIOMT2 2 -1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 -35.38000
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 ASN A 246
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 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 LYS A 43 CG CD CE NZ
REMARK 470 GLU A 106 CG CD OE1 OE2
REMARK 470 LYS A 161 CG CD CE NZ
REMARK 470 ARG A 162 CG CD NE CZ NH1 NH2
REMARK 470 PHE A 163 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 LYS A 187 CG CD CE NZ
REMARK 470 LYS A 196 CG CD CE NZ
REMARK 470 GLU A 231 CG CD OE1 OE2
REMARK 470 GLU A 238 CG CD OE1 OE2
REMARK 470 LYS A 241 CG CD CE NZ
REMARK 470 ASN B 59 CG OD1 ND2
REMARK 470 LYS B 150 CG CD CE NZ
REMARK 470 LYS B 161 CG CD CE NZ
REMARK 470 LYS B 187 CG CD CE NZ
REMARK 470 LYS B 196 CG CD CE NZ
REMARK 470 LYS B 220 CG CD CE NZ
REMARK 470 LYS B 222 CG CD CE NZ
REMARK 470 GLU B 238 CG CD OE1 OE2
REMARK 470 LYS B 241 CG CD CE NZ
REMARK 470 ILE B 244 CG1 CG2 CD1
REMARK 470 GLN B 245 CG CD OE1 NE2
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 LEU A 12 -137.58 50.32
REMARK 500 GLU A 31 -50.61 75.80
REMARK 500 TYR A 51 36.63 72.93
REMARK 500 ALA A 75 46.31 -86.90
REMARK 500 OAS A 114 -129.46 63.06
REMARK 500 ALA A 136 65.21 39.16
REMARK 500 SER A 149 108.64 -167.03
REMARK 500 GLU B 31 -49.35 74.81
REMARK 500 ASP B 74 67.97 -155.85
REMARK 500 OAS B 114 -105.20 -149.21
REMARK 500 SER B 149 110.46 -164.98
REMARK 500 SER B 184 -37.93 64.38
REMARK 500 CYS B 194 140.13 -171.51
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 COA A 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PEG A 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue COA B 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO B 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PEG B 303
DBREF 6YUS A 1 247 UNP O68216 O68216_NEIMD 1 247
DBREF 6YUS B 1 247 UNP O68216 O68216_NEIMD 1 247
SEQADV 6YUS ALA A 228 UNP O68216 HIS 228 ENGINEERED MUTATION
SEQADV 6YUS LEU A 248 UNP O68216 EXPRESSION TAG
SEQADV 6YUS GLU A 249 UNP O68216 EXPRESSION TAG
SEQADV 6YUS HIS A 250 UNP O68216 EXPRESSION TAG
SEQADV 6YUS HIS A 251 UNP O68216 EXPRESSION TAG
SEQADV 6YUS HIS A 252 UNP O68216 EXPRESSION TAG
SEQADV 6YUS HIS A 253 UNP O68216 EXPRESSION TAG
SEQADV 6YUS HIS A 254 UNP O68216 EXPRESSION TAG
SEQADV 6YUS HIS A 255 UNP O68216 EXPRESSION TAG
SEQADV 6YUS ALA B 228 UNP O68216 HIS 228 ENGINEERED MUTATION
SEQADV 6YUS LEU B 248 UNP O68216 EXPRESSION TAG
SEQADV 6YUS GLU B 249 UNP O68216 EXPRESSION TAG
SEQADV 6YUS HIS B 250 UNP O68216 EXPRESSION TAG
SEQADV 6YUS HIS B 251 UNP O68216 EXPRESSION TAG
SEQADV 6YUS HIS B 252 UNP O68216 EXPRESSION TAG
SEQADV 6YUS HIS B 253 UNP O68216 EXPRESSION TAG
SEQADV 6YUS HIS B 254 UNP O68216 EXPRESSION TAG
SEQADV 6YUS 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 OAS 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 ALA 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 OAS 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 ALA 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
MODRES 6YUS OAS A 114 SER MODIFIED RESIDUE
MODRES 6YUS OAS B 114 SER MODIFIED RESIDUE
HET OAS A 114 9
HET OAS B 114 9
HET COA A 301 48
HET PEG A 302 7
HET COA B 301 48
HET EDO B 302 4
HET PEG B 303 7
HETNAM OAS O-ACETYLSERINE
HETNAM COA COENZYME A
HETNAM PEG DI(HYDROXYETHYL)ETHER
HETNAM EDO 1,2-ETHANEDIOL
HETSYN EDO ETHYLENE GLYCOL
FORMUL 1 OAS 2(C5 H9 N O4)
FORMUL 3 COA 2(C21 H36 N7 O16 P3 S)
FORMUL 4 PEG 2(C4 H10 O3)
FORMUL 6 EDO C2 H6 O2
FORMUL 8 HOH *40(H2 O)
HELIX 1 AA1 MET A 1 ASN A 4 5 4
HELIX 2 AA2 ILE A 52 LEU A 56 5 5
HELIX 3 AA3 ASN A 87 SER A 101 1 15
HELIX 4 AA4 ASN A 104 GLU A 106 5 3
HELIX 5 AA5 OAS A 114 ASN A 128 1 15
HELIX 6 AA6 LYS A 140 LYS A 146 1 7
HELIX 7 AA7 SER A 149 GLY A 158 1 10
HELIX 8 AA8 SER A 160 ARG A 162 5 3
HELIX 9 AA9 PHE A 163 ASP A 173 1 11
HELIX 10 AB1 ASP A 173 THR A 181 1 9
HELIX 11 AB2 ASP A 198 LYS A 215 1 18
HELIX 12 AB3 ASP A 229 GLN A 245 1 17
HELIX 13 AB4 MET B 1 ASN B 4 5 4
HELIX 14 AB5 ILE B 52 LEU B 56 5 5
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 OAS 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 SER B 160 ASP B 173 1 14
HELIX 22 AC4 ASP B 173 THR B 181 1 9
HELIX 23 AC5 ASP B 198 LYS B 215 1 18
HELIX 24 AC6 ASP B 229 GLN B 245 1 17
SHEET 1 AA1 9 LYS A 6 ILE A 11 0
SHEET 2 AA1 9 LEU A 14 LEU A 19 -1 O GLU A 16 N ASN A 9
SHEET 3 AA1 9 CYS A 22 LYS A 27 -1 O PHE A 24 N PHE A 17
SHEET 4 AA1 9 THR A 61 PHE A 65 -1 O ALA A 64 N LEU A 25
SHEET 5 AA1 9 THR A 33 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 THR B 36 O PHE B 65
SHEET 6 AA2 9 THR B 108 GLY B 112 1 O TYR B 109 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 LYS B 220 N ILE B 190
LINK C SER A 113 N OAS A 114 1555 1555 1.33
LINK C OAS A 114 N LYS A 115 1555 1555 1.34
LINK C SER B 113 N OAS B 114 1555 1555 1.31
LINK C OAS B 114 N LYS B 115 1555 1555 1.33
CISPEP 1 TYR A 70 PRO A 71 0 -5.81
CISPEP 2 TYR B 70 PRO B 71 0 5.63
SITE 1 AC1 12 ILE A 11 GLN A 47 LYS A 48 TYR A 49
SITE 2 AC1 12 ASN A 50 TYR A 51 ILE A 52 LYS A 53
SITE 3 AC1 12 SER A 113 OAS A 114 ILE A 233 ARG A 237
SITE 1 AC2 3 LYS A 28 ASN A 210 EDO B 302
SITE 1 AC3 14 ILE B 11 PHE B 40 GLN B 47 LYS B 48
SITE 2 AC3 14 TYR B 49 ASN B 50 TYR B 51 ILE B 52
SITE 3 AC3 14 LYS B 53 SER B 113 OAS B 114 ILE B 233
SITE 4 AC3 14 ARG B 237 HOH B 411
SITE 1 AC4 5 ASN A 210 PEG A 302 TYR B 26 LYS B 28
SITE 2 AC4 5 LEU B 100
SITE 1 AC5 5 ASN B 83 GLU B 84 LEU B 85 TYR B 155
SITE 2 AC5 5 MET B 156
CRYST1 136.740 136.740 70.760 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 0.007313 0.000000 0.000000 0.00000
SCALE2 0.000000 0.007313 0.000000 0.00000
SCALE3 0.000000 0.000000 0.014132 0.00000
TER 1934 GLN A 245
TER 3870 GLN B 245
MASTER 511 0 7 24 18 0 12 6 4022 2 136 40
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