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HEADER HYDROLASE 12-FEB-14 4OSE
TITLE X-RAY CRYSTAL STRUCTURE OF A PUTATIVE HYDROLASE FROM RICKETTSIA TYPHI
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PUTATIVE HYDROLASE;
COMPND 3 CHAIN: A, B;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: RICKETTSIA TYPHI;
SOURCE 3 ORGANISM_TAXID: 257363;
SOURCE 4 STRAIN: ATCC VR-144 / WILMINGTON;
SOURCE 5 GENE: RT0431;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS STRUCTURAL GENOMICS, NIAID, NATIONAL INSTITUTE OF ALLERGY AND
KEYWDS 2 INFECTIOUS DISEASES, SEATTLE STRUCTURAL GENOMICS CENTER FOR
KEYWDS 3 INFECTIOUS DISEASE, SSGCID, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR SEATTLE STRUCTURAL GENOMICS CENTER FOR INFECTIOUS DISEASE (SSGCID)
REVDAT 1 19-MAR-14 4OSE 0
JRNL AUTH J.W.FAIRMAN,J.ABENDROTH,T.E.EDWARDS,D.LORIMER
JRNL TITL X-RAY CRYSTAL STRUCTURE OF A PUTATIVE HYDROLASE FROM
JRNL TITL 2 RICKETTSIA TYPHI
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.40 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE: DEV_1615)
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VICENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-
REMARK 3 : KUNSTLEVE,LI-WEI HUNG,ROBERT IMMORMINO,
REMARK 3 : TOM IOERGER,AIRLIE MCCOY,ERIK MCKEE,NIGEL
REMARK 3 : MORIARTY,REETAL PAI,RANDY READ,JANE
REMARK 3 : RICHARDSON,DAVID RICHARDSON,TOD ROMO,JIM
REMARK 3 : SACCHETTINI,NICHOLAS SAUTER,JACOB SMITH,
REMARK 3 : LAURENT STORONI,TOM TERWILLIGER,PETER
REMARK 3 : ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.40
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 43.49
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.360
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.7
REMARK 3 NUMBER OF REFLECTIONS : 25907
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.203
REMARK 3 R VALUE (WORKING SET) : 0.201
REMARK 3 FREE R VALUE : 0.235
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.070
REMARK 3 FREE R VALUE TEST SET COUNT : 1314
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 43.4940 - 4.9902 0.99 2817 163 0.1682 0.1957
REMARK 3 2 4.9902 - 3.9617 1.00 2738 160 0.1562 0.1968
REMARK 3 3 3.9617 - 3.4612 1.00 2742 133 0.1876 0.2147
REMARK 3 4 3.4612 - 3.1448 1.00 2740 148 0.2260 0.2521
REMARK 3 5 3.1448 - 2.9195 1.00 2704 154 0.2528 0.2943
REMARK 3 6 2.9195 - 2.7474 1.00 2724 142 0.2543 0.2938
REMARK 3 7 2.7474 - 2.6098 1.00 2723 140 0.2648 0.3348
REMARK 3 8 2.6098 - 2.4962 1.00 2692 144 0.2699 0.3165
REMARK 3 9 2.4962 - 2.4000 0.99 2713 130 0.2763 0.3019
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) : 0.290
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 27.610
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 43.25
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 58.19
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 : 0.002 4494
REMARK 3 ANGLE : 0.656 6117
REMARK 3 CHIRALITY : 0.024 694
REMARK 3 PLANARITY : 0.003 771
REMARK 3 DIHEDRAL : 12.596 1586
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 13
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: chain 'A' and (resid 1 through 48 )
REMARK 3 ORIGIN FOR THE GROUP (A): 8.9221 59.1723 28.4562
REMARK 3 T TENSOR
REMARK 3 T11: 0.3813 T22: 0.4896
REMARK 3 T33: 0.5262 T12: 0.0630
REMARK 3 T13: -0.0162 T23: -0.1793
REMARK 3 L TENSOR
REMARK 3 L11: 5.9873 L22: 1.7515
REMARK 3 L33: 2.9198 L12: -2.2156
REMARK 3 L13: 0.1991 L23: -0.0149
REMARK 3 S TENSOR
REMARK 3 S11: -0.2289 S12: -0.9414 S13: 1.0970
REMARK 3 S21: -0.0354 S22: 0.3141 S23: -0.2007
REMARK 3 S31: -0.1461 S32: -0.0608 S33: -0.0605
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: chain 'A' and (resid 49 through 100 )
REMARK 3 ORIGIN FOR THE GROUP (A): 11.4463 56.0711 28.6697
REMARK 3 T TENSOR
REMARK 3 T11: 0.4087 T22: 0.5485
REMARK 3 T33: 0.4725 T12: 0.0752
REMARK 3 T13: -0.0245 T23: -0.1175
REMARK 3 L TENSOR
REMARK 3 L11: 7.5197 L22: 2.5949
REMARK 3 L33: 0.6982 L12: -0.1895
REMARK 3 L13: 0.8050 L23: 0.0873
REMARK 3 S TENSOR
REMARK 3 S11: -0.0032 S12: -0.9463 S13: 0.7301
REMARK 3 S21: 0.0307 S22: 0.0632 S23: -0.0225
REMARK 3 S31: -0.1623 S32: -0.0967 S33: -0.0558
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: chain 'A' and (resid 101 through 122 )
REMARK 3 ORIGIN FOR THE GROUP (A): 12.4246 52.5491 20.3314
REMARK 3 T TENSOR
REMARK 3 T11: 0.3312 T22: 0.4930
REMARK 3 T33: 0.3956 T12: 0.0080
REMARK 3 T13: -0.0341 T23: -0.0529
REMARK 3 L TENSOR
REMARK 3 L11: 3.5941 L22: 3.5132
REMARK 3 L33: 2.0357 L12: -0.8007
REMARK 3 L13: -0.3234 L23: -0.2662
REMARK 3 S TENSOR
REMARK 3 S11: 0.1257 S12: 0.3959 S13: -0.0945
REMARK 3 S21: -0.0984 S22: 0.0603 S23: -0.0996
REMARK 3 S31: 0.0251 S32: -0.2032 S33: -0.1607
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: chain 'A' and (resid 123 through 154 )
REMARK 3 ORIGIN FOR THE GROUP (A): 10.2877 42.1187 23.1920
REMARK 3 T TENSOR
REMARK 3 T11: 0.3561 T22: 0.5776
REMARK 3 T33: 0.4352 T12: 0.0070
REMARK 3 T13: 0.0324 T23: -0.1154
REMARK 3 L TENSOR
REMARK 3 L11: 6.8018 L22: 6.3518
REMARK 3 L33: 0.6073 L12: -0.3543
REMARK 3 L13: 0.7400 L23: 1.6821
REMARK 3 S TENSOR
REMARK 3 S11: 0.1416 S12: -0.0952 S13: -0.7793
REMARK 3 S21: 0.3492 S22: -0.4369 S23: 0.3447
REMARK 3 S31: 0.3218 S32: -0.3396 S33: 0.3183
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: chain 'A' and (resid 155 through 172 )
REMARK 3 ORIGIN FOR THE GROUP (A): 16.4939 42.7263 48.2879
REMARK 3 T TENSOR
REMARK 3 T11: 0.8195 T22: 1.4466
REMARK 3 T33: 0.6111 T12: 0.1706
REMARK 3 T13: 0.0010 T23: 0.1242
REMARK 3 L TENSOR
REMARK 3 L11: 6.2093 L22: 6.1909
REMARK 3 L33: 3.9146 L12: 0.4709
REMARK 3 L13: -3.6113 L23: 0.7952
REMARK 3 S TENSOR
REMARK 3 S11: -0.3691 S12: -2.2426 S13: -0.3849
REMARK 3 S21: 0.8752 S22: -0.2005 S23: -0.1618
REMARK 3 S31: 0.5277 S32: -0.7381 S33: 0.6471
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: chain 'A' and (resid 173 through 194 )
REMARK 3 ORIGIN FOR THE GROUP (A): 22.8169 46.2804 40.7047
REMARK 3 T TENSOR
REMARK 3 T11: 0.5010 T22: 1.0960
REMARK 3 T33: 0.4214 T12: 0.1315
REMARK 3 T13: -0.0607 T23: 0.0090
REMARK 3 L TENSOR
REMARK 3 L11: 4.3478 L22: 6.0077
REMARK 3 L33: 3.5512 L12: -2.6282
REMARK 3 L13: -2.2482 L23: 0.7966
REMARK 3 S TENSOR
REMARK 3 S11: -0.6838 S12: -1.3344 S13: 0.1305
REMARK 3 S21: 0.5544 S22: 0.5631 S23: -0.2389
REMARK 3 S31: 0.2230 S32: 0.2553 S33: 0.0678
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: chain 'A' and (resid 195 through 209 )
REMARK 3 ORIGIN FOR THE GROUP (A): 7.9221 50.0253 46.0911
REMARK 3 T TENSOR
REMARK 3 T11: 0.5345 T22: 0.9565
REMARK 3 T33: 0.3748 T12: 0.1101
REMARK 3 T13: -0.0000 T23: -0.0257
REMARK 3 L TENSOR
REMARK 3 L11: 8.1480 L22: 8.0006
REMARK 3 L33: 4.2961 L12: -4.9301
REMARK 3 L13: -4.6949 L23: 0.5089
REMARK 3 S TENSOR
REMARK 3 S11: -0.0932 S12: -0.1825 S13: -0.0163
REMARK 3 S21: 0.6498 S22: 0.0109 S23: -0.3424
REMARK 3 S31: 0.6963 S32: -0.1071 S33: 0.0062
REMARK 3 TLS GROUP : 8
REMARK 3 SELECTION: chain 'A' and (resid 210 through 264 )
REMARK 3 ORIGIN FOR THE GROUP (A): 14.6358 37.3508 17.9585
REMARK 3 T TENSOR
REMARK 3 T11: 0.4680 T22: 0.3690
REMARK 3 T33: 0.5946 T12: -0.0100
REMARK 3 T13: 0.0193 T23: -0.1455
REMARK 3 L TENSOR
REMARK 3 L11: 7.7151 L22: 4.3268
REMARK 3 L33: 4.5392 L12: 0.1880
REMARK 3 L13: -0.7081 L23: -0.1888
REMARK 3 S TENSOR
REMARK 3 S11: -0.0949 S12: 0.5672 S13: -1.4473
REMARK 3 S21: -0.1702 S22: -0.2636 S23: 0.3036
REMARK 3 S31: 0.7739 S32: -0.2179 S33: 0.3255
REMARK 3 TLS GROUP : 9
REMARK 3 SELECTION: chain 'A' and (resid 265 through 290 )
REMARK 3 ORIGIN FOR THE GROUP (A): 27.4114 45.1643 24.2206
REMARK 3 T TENSOR
REMARK 3 T11: 0.2747 T22: 0.4996
REMARK 3 T33: 0.4034 T12: 0.1165
REMARK 3 T13: -0.0108 T23: 0.0146
REMARK 3 L TENSOR
REMARK 3 L11: 8.5241 L22: 5.2401
REMARK 3 L33: 6.1920 L12: 3.2699
REMARK 3 L13: -3.1168 L23: -0.6103
REMARK 3 S TENSOR
REMARK 3 S11: -0.0584 S12: -0.6623 S13: -0.2284
REMARK 3 S21: 0.2664 S22: -0.2464 S23: -0.0765
REMARK 3 S31: -0.1258 S32: -0.3860 S33: 0.1871
REMARK 3 TLS GROUP : 10
REMARK 3 SELECTION: chain 'B' and (resid 0 through 112 )
REMARK 3 ORIGIN FOR THE GROUP (A): 59.7679 46.1202 20.2762
REMARK 3 T TENSOR
REMARK 3 T11: 0.3897 T22: 0.3293
REMARK 3 T33: 0.4720 T12: -0.0051
REMARK 3 T13: -0.0139 T23: -0.0291
REMARK 3 L TENSOR
REMARK 3 L11: 8.9675 L22: 2.4006
REMARK 3 L33: 4.6521 L12: -2.8262
REMARK 3 L13: -1.0882 L23: 0.9322
REMARK 3 S TENSOR
REMARK 3 S11: 0.0269 S12: -0.5919 S13: 0.8895
REMARK 3 S21: 0.0963 S22: 0.1428 S23: -0.5196
REMARK 3 S31: -0.2843 S32: 0.5042 S33: -0.1854
REMARK 3 TLS GROUP : 11
REMARK 3 SELECTION: chain 'B' and (resid 113 through 180 )
REMARK 3 ORIGIN FOR THE GROUP (A): 51.5222 44.2048 7.6611
REMARK 3 T TENSOR
REMARK 3 T11: 0.4486 T22: 0.2826
REMARK 3 T33: 0.3269 T12: 0.0726
REMARK 3 T13: 0.0609 T23: -0.0142
REMARK 3 L TENSOR
REMARK 3 L11: 4.7139 L22: 2.4164
REMARK 3 L33: 1.5139 L12: -0.4539
REMARK 3 L13: 0.1595 L23: 0.6014
REMARK 3 S TENSOR
REMARK 3 S11: 0.0389 S12: 0.4268 S13: 0.1843
REMARK 3 S21: -0.5625 S22: 0.1122 S23: -0.2140
REMARK 3 S31: -0.0783 S32: -0.0220 S33: -0.1738
REMARK 3 TLS GROUP : 12
REMARK 3 SELECTION: chain 'B' and (resid 181 through 209 )
REMARK 3 ORIGIN FOR THE GROUP (A): 55.7747 58.3785 6.2945
REMARK 3 T TENSOR
REMARK 3 T11: 0.6873 T22: 0.4212
REMARK 3 T33: 0.9306 T12: 0.0419
REMARK 3 T13: 0.1310 T23: 0.2303
REMARK 3 L TENSOR
REMARK 3 L11: 2.6491 L22: 0.8575
REMARK 3 L33: 3.0495 L12: 1.3538
REMARK 3 L13: -0.2643 L23: 0.0175
REMARK 3 S TENSOR
REMARK 3 S11: 0.0778 S12: 0.4290 S13: 1.2903
REMARK 3 S21: -0.0451 S22: 0.0077 S23: -0.1366
REMARK 3 S31: -0.6001 S32: -0.0008 S33: -0.0871
REMARK 3 TLS GROUP : 13
REMARK 3 SELECTION: chain 'B' and (resid 210 through 290 )
REMARK 3 ORIGIN FOR THE GROUP (A): 42.5393 36.6067 13.0487
REMARK 3 T TENSOR
REMARK 3 T11: 0.3663 T22: 0.2387
REMARK 3 T33: 0.3524 T12: -0.0144
REMARK 3 T13: -0.0345 T23: 0.0044
REMARK 3 L TENSOR
REMARK 3 L11: 6.4426 L22: 4.3706
REMARK 3 L33: 4.7791 L12: -1.0560
REMARK 3 L13: -0.8996 L23: 0.4459
REMARK 3 S TENSOR
REMARK 3 S11: 0.0977 S12: 0.1139 S13: -0.6496
REMARK 3 S21: -0.4709 S22: -0.0959 S23: -0.0211
REMARK 3 S31: 0.3998 S32: -0.3518 S33: -0.0234
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : 1
REMARK 3 NCS GROUP : 1
REMARK 3 NCS OPERATOR : 1
REMARK 3 REFERENCE SELECTION: chain A
REMARK 3 SELECTION : chain B
REMARK 3 ATOM PAIRS NUMBER : 2548
REMARK 3 RMSD : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 4OSE COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 14-FEB-14.
REMARK 100 THE RCSB ID CODE IS RCSB084891.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 28-MAR-13
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.50
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 21-ID-F
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9787
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MAR SCANNER 300 MM PLATE
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 25945
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.400
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : 0.06100
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 16.7400
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.40
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.46
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.7
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.51800
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 2.530
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: BALBES
REMARK 200 STARTING MODEL: PDB ENTRY 3BWX
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 48.56
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.39
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: MCSG1 CONDITION E3: 30% PEG 550 MME,
REMARK 280 0.05 M MAGNESIUM CHLORIDE, 0.1 M HEPES PH 7.50, VAPOR DIFFUSION,
REMARK 280 SITTING DROP, TEMPERATURE 289K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,Y,-Z
REMARK 290 3555 X+1/2,Y+1/2,Z
REMARK 290 4555 -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 0.00000
REMARK 290 SMTRY1 3 1.000000 0.000000 0.000000 77.46000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 24.53000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 77.46000
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 24.53000
REMARK 290 SMTRY3 4 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 300 REMARK: AS PER THE AUTHORS THE BIOLOGICAL ASSEMBLY IS UNKNOWN
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 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 350
REMARK 350 BIOMOLECULE: 2
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 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 MET A -7
REMARK 465 ALA A -6
REMARK 465 HIS A -5
REMARK 465 HIS A -4
REMARK 465 HIS A -3
REMARK 465 HIS A -2
REMARK 465 HIS A -1
REMARK 465 HIS A 0
REMARK 465 GLY A 211
REMARK 465 MET A 212
REMARK 465 GLN A 213
REMARK 465 SER A 214
REMARK 465 ASP A 215
REMARK 465 ASN A 216
REMARK 465 ASN A 217
REMARK 465 MET B -7
REMARK 465 ALA B -6
REMARK 465 HIS B -5
REMARK 465 HIS B -4
REMARK 465 HIS B -3
REMARK 465 HIS B -2
REMARK 465 HIS B -1
REMARK 465 GLY B 211
REMARK 465 MET B 212
REMARK 465 GLN B 213
REMARK 465 SER B 214
REMARK 465 ASP B 215
REMARK 465 ASN B 216
REMARK 465 ASN B 217
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 ASN A 4 CG OD1 ND2
REMARK 470 SER A 5 OG
REMARK 470 LYS A 7 CG CD CE NZ
REMARK 470 LEU A 15 CG CD1 CD2
REMARK 470 LEU A 17 CG CD1 CD2
REMARK 470 LYS A 34 CG CD CE NZ
REMARK 470 LYS A 36 CG CD CE NZ
REMARK 470 LYS A 80 CG CD CE NZ
REMARK 470 LYS A 81 CG CD CE NZ
REMARK 470 TYR A 83 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 LYS A 126 CG CD CE NZ
REMARK 470 ILE A 147 CG1 CG2 CD1
REMARK 470 LYS A 148 CG CD CE NZ
REMARK 470 TYR A 152 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 LYS A 154 CG CD CE NZ
REMARK 470 LYS A 155 CG CD CE NZ
REMARK 470 THR A 156 OG1 CG2
REMARK 470 LEU A 158 CG CD1 CD2
REMARK 470 GLU A 167 CG CD OE1 OE2
REMARK 470 LYS A 199 CG CD CE NZ
REMARK 470 LYS A 201 CG CD CE NZ
REMARK 470 LYS A 210 CG CD CE NZ
REMARK 470 GLN A 218 CG CD OE1 NE2
REMARK 470 GLU A 219 CG CD OE1 OE2
REMARK 470 LYS A 222 CG CD CE NZ
REMARK 470 LYS A 231 CG CD CE NZ
REMARK 470 LYS A 247 CG CD CE NZ
REMARK 470 GLN A 251 CG CD OE1 NE2
REMARK 470 LYS A 252 CG CD CE NZ
REMARK 470 LYS A 254 CG CD CE NZ
REMARK 470 LYS A 255 CG CD CE NZ
REMARK 470 LYS A 265 CG CD CE NZ
REMARK 470 LYS A 289 CG CD CE NZ
REMARK 470 HIS B 0 CG ND1 CD2 CE1 NE2
REMARK 470 SER B 5 OG
REMARK 470 LEU B 15 CG CD1 CD2
REMARK 470 LYS B 34 CG CD CE NZ
REMARK 470 LYS B 36 CG CD CE NZ
REMARK 470 LYS B 80 CG CD CE NZ
REMARK 470 LYS B 81 CG CD CE NZ
REMARK 470 TYR B 83 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 LYS B 104 CG CD CE NZ
REMARK 470 LYS B 126 CG CD CE NZ
REMARK 470 ILE B 147 CG1 CG2 CD1
REMARK 470 LYS B 148 CG CD CE NZ
REMARK 470 ILE B 149 CG1 CG2 CD1
REMARK 470 TYR B 152 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 LYS B 154 CG CD CE NZ
REMARK 470 LYS B 155 CG CD CE NZ
REMARK 470 THR B 156 OG1 CG2
REMARK 470 LEU B 171 CG CD1 CD2
REMARK 470 PHE B 196 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 LYS B 201 CG CD CE NZ
REMARK 470 THR B 209 OG1 CG2
REMARK 470 LYS B 210 CG CD CE NZ
REMARK 470 GLN B 218 CG CD OE1 NE2
REMARK 470 GLU B 219 CG CD OE1 OE2
REMARK 470 LYS B 222 CG CD CE NZ
REMARK 470 LYS B 229 CG CD CE NZ
REMARK 470 LYS B 231 CG CD CE NZ
REMARK 470 LYS B 247 CG CD CE NZ
REMARK 470 LYS B 254 CG CD CE NZ
REMARK 470 LYS B 289 CG CD CE NZ
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 NZ LYS B 130 O SER B 290 2.18
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 LEU A 15 86.82 52.79
REMARK 500 SER A 74 -121.65 55.36
REMARK 500 SER A 112 -113.22 55.34
REMARK 500 SER B 74 -121.03 55.23
REMARK 500 SER B 112 -113.66 55.39
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: RITYA.17523.A RELATED DB: TARGETTRACK
DBREF 4OSE A 1 290 UNP Q68WT4 Q68WT4_RICTY 1 290
DBREF 4OSE B 1 290 UNP Q68WT4 Q68WT4_RICTY 1 290
SEQADV 4OSE MET A -7 UNP Q68WT4 EXPRESSION TAG
SEQADV 4OSE ALA A -6 UNP Q68WT4 EXPRESSION TAG
SEQADV 4OSE HIS A -5 UNP Q68WT4 EXPRESSION TAG
SEQADV 4OSE HIS A -4 UNP Q68WT4 EXPRESSION TAG
SEQADV 4OSE HIS A -3 UNP Q68WT4 EXPRESSION TAG
SEQADV 4OSE HIS A -2 UNP Q68WT4 EXPRESSION TAG
SEQADV 4OSE HIS A -1 UNP Q68WT4 EXPRESSION TAG
SEQADV 4OSE HIS A 0 UNP Q68WT4 EXPRESSION TAG
SEQADV 4OSE MET B -7 UNP Q68WT4 EXPRESSION TAG
SEQADV 4OSE ALA B -6 UNP Q68WT4 EXPRESSION TAG
SEQADV 4OSE HIS B -5 UNP Q68WT4 EXPRESSION TAG
SEQADV 4OSE HIS B -4 UNP Q68WT4 EXPRESSION TAG
SEQADV 4OSE HIS B -3 UNP Q68WT4 EXPRESSION TAG
SEQADV 4OSE HIS B -2 UNP Q68WT4 EXPRESSION TAG
SEQADV 4OSE HIS B -1 UNP Q68WT4 EXPRESSION TAG
SEQADV 4OSE HIS B 0 UNP Q68WT4 EXPRESSION TAG
SEQRES 1 A 298 MET ALA HIS HIS HIS HIS HIS HIS MET GLN ILE ASN SER
SEQRES 2 A 298 ILE LYS ILE GLY PRO TYR ILE ASN LEU LEU PRO LEU GLN
SEQRES 3 A 298 TYR ILE PRO GLN HIS LYS ILE SER TYR VAL GLU PHE GLY
SEQRES 4 A 298 ASP PRO LYS ASN LYS ASN ILE ILE LEU CYS ALA HIS GLY
SEQRES 5 A 298 LEU THR ARG ASN ALA HIS ASP PHE ASP LYS ILE ALA LYS
SEQRES 6 A 298 GLU LEU CYS LYS ASN TYR ARG ILE ILE SER ILE ASN TYR
SEQRES 7 A 298 PRO GLY ARG SER ASP SER GLU ASN LEU LYS LYS PRO TYR
SEQRES 8 A 298 HIS TYR ASN TYR THR THR TYR ILE LYS ASP THR LEU LEU
SEQRES 9 A 298 PHE PHE LYS ARG LEU ASN ILE LYS ASN PRO ILE TRP LEU
SEQRES 10 A 298 GLY THR SER MET GLY GLY ILE ILE GLY MET VAL LEU ALA
SEQRES 11 A 298 SER LYS TYR LYS ASN ILE PHE LYS ALA LEU ILE LEU ASN
SEQRES 12 A 298 ASP ILE GLY ALA PHE ILE ASP ALA ALA PRO LEU ILE LYS
SEQRES 13 A 298 ILE GLY ASP TYR ALA LYS LYS THR VAL LEU LEU ASP ASP
SEQRES 14 A 298 LEU ALA SER ALA LYS GLU HIS LEU LYS LEU ILE TYR ALA
SEQRES 15 A 298 GLN ILE GLY ILE LYS ASN GLU GLU ASP TRP ASP TYR LEU
SEQRES 16 A 298 THR LYS TYR SER VAL ILE SER THR PHE GLY GLY LYS TYR
SEQRES 17 A 298 LYS MET ASN TYR ASP PRO ALA ILE THR LYS GLY MET GLN
SEQRES 18 A 298 SER ASP ASN ASN GLN GLU ASP VAL LYS LEU TRP SER VAL
SEQRES 19 A 298 TRP ASN LYS ILE LYS CYS ARG ILE LEU VAL ILE HIS GLY
SEQRES 20 A 298 MET LYS SER GLN ILE LEU THR LYS SER THR ILE GLN LYS
SEQRES 21 A 298 MET LYS LYS THR ASN THR PHE ASP LEU TYR GLU ILE LYS
SEQRES 22 A 298 TYR ALA GLY HIS ALA PRO SER LEU MET ASN ASP GLU GLU
SEQRES 23 A 298 ILE TYR TYR ILE GLU SER TRP LEU LYS GLN LYS SER
SEQRES 1 B 298 MET ALA HIS HIS HIS HIS HIS HIS MET GLN ILE ASN SER
SEQRES 2 B 298 ILE LYS ILE GLY PRO TYR ILE ASN LEU LEU PRO LEU GLN
SEQRES 3 B 298 TYR ILE PRO GLN HIS LYS ILE SER TYR VAL GLU PHE GLY
SEQRES 4 B 298 ASP PRO LYS ASN LYS ASN ILE ILE LEU CYS ALA HIS GLY
SEQRES 5 B 298 LEU THR ARG ASN ALA HIS ASP PHE ASP LYS ILE ALA LYS
SEQRES 6 B 298 GLU LEU CYS LYS ASN TYR ARG ILE ILE SER ILE ASN TYR
SEQRES 7 B 298 PRO GLY ARG SER ASP SER GLU ASN LEU LYS LYS PRO TYR
SEQRES 8 B 298 HIS TYR ASN TYR THR THR TYR ILE LYS ASP THR LEU LEU
SEQRES 9 B 298 PHE PHE LYS ARG LEU ASN ILE LYS ASN PRO ILE TRP LEU
SEQRES 10 B 298 GLY THR SER MET GLY GLY ILE ILE GLY MET VAL LEU ALA
SEQRES 11 B 298 SER LYS TYR LYS ASN ILE PHE LYS ALA LEU ILE LEU ASN
SEQRES 12 B 298 ASP ILE GLY ALA PHE ILE ASP ALA ALA PRO LEU ILE LYS
SEQRES 13 B 298 ILE GLY ASP TYR ALA LYS LYS THR VAL LEU LEU ASP ASP
SEQRES 14 B 298 LEU ALA SER ALA LYS GLU HIS LEU LYS LEU ILE TYR ALA
SEQRES 15 B 298 GLN ILE GLY ILE LYS ASN GLU GLU ASP TRP ASP TYR LEU
SEQRES 16 B 298 THR LYS TYR SER VAL ILE SER THR PHE GLY GLY LYS TYR
SEQRES 17 B 298 LYS MET ASN TYR ASP PRO ALA ILE THR LYS GLY MET GLN
SEQRES 18 B 298 SER ASP ASN ASN GLN GLU ASP VAL LYS LEU TRP SER VAL
SEQRES 19 B 298 TRP ASN LYS ILE LYS CYS ARG ILE LEU VAL ILE HIS GLY
SEQRES 20 B 298 MET LYS SER GLN ILE LEU THR LYS SER THR ILE GLN LYS
SEQRES 21 B 298 MET LYS LYS THR ASN THR PHE ASP LEU TYR GLU ILE LYS
SEQRES 22 B 298 TYR ALA GLY HIS ALA PRO SER LEU MET ASN ASP GLU GLU
SEQRES 23 B 298 ILE TYR TYR ILE GLU SER TRP LEU LYS GLN LYS SER
FORMUL 3 HOH *71(H2 O)
HELIX 1 1 ASN A 48 ASP A 51 5 4
HELIX 2 2 PHE A 52 CYS A 60 1 9
HELIX 3 3 LYS A 81 TYR A 85 5 5
HELIX 4 4 ASN A 86 LEU A 101 1 16
HELIX 5 5 SER A 112 TYR A 125 1 14
HELIX 6 6 ASP A 142 LYS A 155 1 14
HELIX 7 7 ASP A 161 TYR A 173 1 13
HELIX 8 8 ASN A 180 SER A 191 1 12
HELIX 9 9 ASP A 205 LYS A 210 5 6
HELIX 10 10 LEU A 223 ASN A 228 1 6
HELIX 11 11 THR A 246 LYS A 254 1 9
HELIX 12 12 ASN A 275 LYS A 289 1 15
HELIX 13 13 ASN B 48 ASP B 51 5 4
HELIX 14 14 PHE B 52 CYS B 60 1 9
HELIX 15 15 LYS B 81 TYR B 85 5 5
HELIX 16 16 ASN B 86 LEU B 101 1 16
HELIX 17 17 SER B 112 TYR B 125 1 14
HELIX 18 18 ASP B 142 LYS B 155 1 14
HELIX 19 19 ASP B 161 TYR B 173 1 13
HELIX 20 20 ASN B 180 SER B 191 1 12
HELIX 21 21 ASP B 205 LYS B 210 5 6
HELIX 22 22 LEU B 223 ASN B 228 1 6
HELIX 23 23 THR B 246 LYS B 255 1 10
HELIX 24 24 ASN B 275 LYS B 289 1 15
SHEET 1 A 8 GLN A 2 ILE A 8 0
SHEET 2 A 8 HIS A 23 PHE A 30 -1 O ILE A 25 N ILE A 6
SHEET 3 A 8 ARG A 64 ILE A 68 -1 O SER A 67 N VAL A 28
SHEET 4 A 8 ILE A 38 ALA A 42 1 N ILE A 39 O ARG A 64
SHEET 5 A 8 ILE A 107 THR A 111 1 O ILE A 107 N ILE A 38
SHEET 6 A 8 ALA A 131 ASN A 135 1 O ILE A 133 N TRP A 108
SHEET 7 A 8 ARG A 233 GLY A 239 1 O ARG A 233 N LEU A 132
SHEET 8 A 8 ASP A 260 ILE A 264 1 O TYR A 262 N HIS A 238
SHEET 1 B 2 TYR A 11 ASN A 13 0
SHEET 2 B 2 GLN A 18 ILE A 20 -1 O ILE A 20 N TYR A 11
SHEET 1 C 2 PHE A 140 ILE A 141 0
SHEET 2 C 2 VAL A 221 LYS A 222 -1 O VAL A 221 N ILE A 141
SHEET 1 D 2 VAL A 192 SER A 194 0
SHEET 2 D 2 TYR A 200 MET A 202 -1 O LYS A 201 N ILE A 193
SHEET 1 E 8 GLN B 2 ILE B 8 0
SHEET 2 E 8 HIS B 23 PHE B 30 -1 O ILE B 25 N ILE B 6
SHEET 3 E 8 ARG B 64 ILE B 68 -1 O SER B 67 N VAL B 28
SHEET 4 E 8 ILE B 38 ALA B 42 1 N ILE B 39 O ARG B 64
SHEET 5 E 8 ILE B 107 THR B 111 1 O ILE B 107 N LEU B 40
SHEET 6 E 8 ALA B 131 ASN B 135 1 O ILE B 133 N TRP B 108
SHEET 7 E 8 ARG B 233 GLY B 239 1 O ARG B 233 N LEU B 132
SHEET 8 E 8 ASP B 260 ILE B 264 1 O TYR B 262 N HIS B 238
SHEET 1 F 2 TYR B 11 ASN B 13 0
SHEET 2 F 2 GLN B 18 ILE B 20 -1 O ILE B 20 N TYR B 11
SHEET 1 G 2 PHE B 140 ILE B 141 0
SHEET 2 G 2 VAL B 221 LYS B 222 -1 O VAL B 221 N ILE B 141
SHEET 1 H 2 VAL B 192 SER B 194 0
SHEET 2 H 2 TYR B 200 MET B 202 -1 O LYS B 201 N ILE B 193
CISPEP 1 GLY A 9 PRO A 10 0 0.34
CISPEP 2 LEU A 15 PRO A 16 0 -3.62
CISPEP 3 HIS A 269 ALA A 270 0 -4.94
CISPEP 4 GLY B 9 PRO B 10 0 0.75
CISPEP 5 LEU B 15 PRO B 16 0 -2.49
CISPEP 6 HIS B 269 ALA B 270 0 -5.02
CRYST1 154.920 49.060 87.290 90.00 94.77 90.00 C 1 2 1 8
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.006455 0.000000 0.000539 0.00000
SCALE2 0.000000 0.020383 0.000000 0.00000
SCALE3 0.000000 0.000000 0.011496 0.00000
TER 2191 SER A 290
TER 4394 SER B 290
MASTER 548 0 0 24 28 0 0 6 4455 2 0 46
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