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HEADER HYDROLASE 20-FEB-24 8W2C
TITLE THIOESTERASE DOMAIN STRUCTURE FROM SULFAZECIN BIOSYNTHETIC
TITLE 2 NONRIBOSOMAL PEPTIDE SYNTHETASE SULM
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: NON-RIBOSOMAL PEPTIDE SYNTHETASE;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: THIOESTERASE DOMAIN;
COMPND 5 SYNONYM: SULM;
COMPND 6 ENGINEERED: YES;
COMPND 7 OTHER_DETAILS: THE PROTEIN WAS EXPRESSED AND CRYSTALLIZED WITH HIS-
COMPND 8 TAG FROM EXPRESSION VECTOR.
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: PARABURKHOLDERIA ACIDICOLA;
SOURCE 3 ORGANISM_TAXID: 1912599;
SOURCE 4 STRAIN: ATCC 31363;
SOURCE 5 GENE: SULM, BWP39_23695;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008
KEYWDS THIOESTERASE DOMAIN, NRPS, NONRIBOSOMAL PEPTIDE SYNTHETASE,
KEYWDS 2 SULFAZECIN, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR K.D.PATEL,A.M.GULICK
REVDAT 1 07-AUG-24 8W2C 0
JRNL AUTH K.D.PATEL,R.A.OLIVER,M.S.LICHSTRAHL,R.LI,C.A.TOWNSEND,
JRNL AUTH 2 A.M.GULICK
JRNL TITL THE STRUCTURE OF THE MONOBACTAM-PRODUCING THIOESTERASE
JRNL TITL 2 DOMAIN OF SULM FORMS A UNIQUE COMPLEX WITH THE UPSTREAM
JRNL TITL 3 CARRIER PROTEIN DOMAIN.
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 1.90 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.13_2998
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
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.90
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 42.27
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.360
REMARK 3 COMPLETENESS FOR RANGE (%) : 95.5
REMARK 3 NUMBER OF REFLECTIONS : 39525
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.177
REMARK 3 R VALUE (WORKING SET) : 0.175
REMARK 3 FREE R VALUE : 0.215
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.050
REMARK 3 FREE R VALUE TEST SET COUNT : 1995
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 42.2700 - 4.5800 0.95 2723 145 0.1636 0.1733
REMARK 3 2 4.5800 - 3.6300 0.97 2726 145 0.1426 0.1628
REMARK 3 3 3.6300 - 3.1700 0.95 2698 144 0.1676 0.2109
REMARK 3 4 3.1700 - 2.8800 0.96 2707 144 0.1697 0.2148
REMARK 3 5 2.8800 - 2.6800 0.98 2747 146 0.1775 0.2353
REMARK 3 6 2.6800 - 2.5200 0.97 2727 146 0.1671 0.2146
REMARK 3 7 2.5200 - 2.3900 0.92 2562 136 0.1730 0.2686
REMARK 3 8 2.3900 - 2.2900 0.96 2712 143 0.1689 0.1930
REMARK 3 9 2.2900 - 2.2000 0.97 2708 145 0.1804 0.2504
REMARK 3 10 2.2000 - 2.1200 0.97 2688 143 0.1950 0.2714
REMARK 3 11 2.1200 - 2.0600 0.95 2674 142 0.2254 0.2529
REMARK 3 12 2.0600 - 2.0000 0.91 2563 135 0.2415 0.3092
REMARK 3 13 2.0000 - 1.9500 0.95 2658 142 0.2638 0.2980
REMARK 3 14 1.9500 - 1.9000 0.95 2637 139 0.3108 0.3877
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) : 0.257
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 24.567
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 28.71
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 40.93
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 3926
REMARK 3 ANGLE : 0.915 5344
REMARK 3 CHIRALITY : 0.056 618
REMARK 3 PLANARITY : 0.006 700
REMARK 3 DIHEDRAL : 10.028 2343
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 2727 THROUGH 2833 )
REMARK 3 ORIGIN FOR THE GROUP (A): 18.3976 -13.7597 5.1480
REMARK 3 T TENSOR
REMARK 3 T11: 0.2675 T22: 0.3198
REMARK 3 T33: 0.2737 T12: -0.0793
REMARK 3 T13: -0.0210 T23: -0.0551
REMARK 3 L TENSOR
REMARK 3 L11: 1.9341 L22: 2.4234
REMARK 3 L33: 3.0099 L12: -0.1886
REMARK 3 L13: -0.3480 L23: 0.4579
REMARK 3 S TENSOR
REMARK 3 S11: 0.0039 S12: -0.0204 S13: 0.2253
REMARK 3 S21: 0.1499 S22: 0.1713 S23: -0.3290
REMARK 3 S31: -0.3760 S32: 0.6640 S33: -0.1559
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 2834 THROUGH 2859 )
REMARK 3 ORIGIN FOR THE GROUP (A): 4.7490 -15.0966 5.8742
REMARK 3 T TENSOR
REMARK 3 T11: 0.3118 T22: 0.1909
REMARK 3 T33: 0.2425 T12: 0.0424
REMARK 3 T13: 0.0186 T23: -0.0354
REMARK 3 L TENSOR
REMARK 3 L11: 0.3261 L22: 1.0557
REMARK 3 L33: 2.9801 L12: -0.5436
REMARK 3 L13: 0.1694 L23: -0.1825
REMARK 3 S TENSOR
REMARK 3 S11: 0.0019 S12: -0.0280 S13: 0.1279
REMARK 3 S21: 0.1451 S22: 0.0725 S23: -0.0028
REMARK 3 S31: -0.3810 S32: -0.0296 S33: -0.1067
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 2860 THROUGH 2877 )
REMARK 3 ORIGIN FOR THE GROUP (A): 6.4859 -35.8097 10.5535
REMARK 3 T TENSOR
REMARK 3 T11: 0.5803 T22: 0.2763
REMARK 3 T33: 0.2980 T12: 0.0815
REMARK 3 T13: 0.0582 T23: 0.0004
REMARK 3 L TENSOR
REMARK 3 L11: 3.3568 L22: 3.8322
REMARK 3 L33: 9.4097 L12: 0.5812
REMARK 3 L13: -2.3149 L23: 1.1594
REMARK 3 S TENSOR
REMARK 3 S11: -0.2343 S12: -0.0412 S13: -0.4097
REMARK 3 S21: -0.1302 S22: 0.2197 S23: 0.0196
REMARK 3 S31: 1.1282 S32: 0.5413 S33: -0.0489
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 2878 THROUGH 2962 )
REMARK 3 ORIGIN FOR THE GROUP (A): 4.4711 -18.4302 2.9264
REMARK 3 T TENSOR
REMARK 3 T11: 0.2124 T22: 0.1869
REMARK 3 T33: 0.1853 T12: 0.0058
REMARK 3 T13: -0.0019 T23: -0.0130
REMARK 3 L TENSOR
REMARK 3 L11: 1.3228 L22: 1.3970
REMARK 3 L33: 4.3435 L12: -0.0036
REMARK 3 L13: -0.2862 L23: 0.3472
REMARK 3 S TENSOR
REMARK 3 S11: -0.0485 S12: 0.0172 S13: 0.0514
REMARK 3 S21: 0.0838 S22: -0.0474 S23: 0.0899
REMARK 3 S31: -0.2339 S32: -0.0829 S33: 0.0861
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 2963 THROUGH 2979 )
REMARK 3 ORIGIN FOR THE GROUP (A): 16.7199 -15.0521 -11.3586
REMARK 3 T TENSOR
REMARK 3 T11: 0.3068 T22: 0.4102
REMARK 3 T33: 0.2497 T12: -0.0766
REMARK 3 T13: 0.0527 T23: -0.0302
REMARK 3 L TENSOR
REMARK 3 L11: 5.1091 L22: 9.5952
REMARK 3 L33: 7.1173 L12: -1.1315
REMARK 3 L13: 0.4881 L23: -0.6650
REMARK 3 S TENSOR
REMARK 3 S11: 0.1599 S12: 0.6492 S13: 0.2594
REMARK 3 S21: -1.0366 S22: -0.0092 S23: -0.3884
REMARK 3 S31: -0.5742 S32: 0.4363 S33: -0.0856
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 2726 THROUGH 2785 )
REMARK 3 ORIGIN FOR THE GROUP (A): -5.2150 -35.9899 -29.9818
REMARK 3 T TENSOR
REMARK 3 T11: 0.2854 T22: 0.2256
REMARK 3 T33: 0.3092 T12: -0.0804
REMARK 3 T13: 0.0026 T23: -0.0191
REMARK 3 L TENSOR
REMARK 3 L11: 1.9577 L22: 1.6612
REMARK 3 L33: 3.3712 L12: -0.2754
REMARK 3 L13: -0.7838 L23: -0.4694
REMARK 3 S TENSOR
REMARK 3 S11: -0.1693 S12: 0.0398 S13: -0.4210
REMARK 3 S21: -0.0235 S22: -0.0029 S23: 0.2686
REMARK 3 S31: 0.5803 S32: -0.4286 S33: 0.1616
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 2786 THROUGH 2810 )
REMARK 3 ORIGIN FOR THE GROUP (A): -9.0982 -25.8673 -39.6338
REMARK 3 T TENSOR
REMARK 3 T11: 0.2067 T22: 0.3096
REMARK 3 T33: 0.2810 T12: -0.0106
REMARK 3 T13: -0.0555 T23: 0.0055
REMARK 3 L TENSOR
REMARK 3 L11: 6.3539 L22: 2.3063
REMARK 3 L33: 7.2241 L12: 2.1976
REMARK 3 L13: -4.6378 L23: -2.0063
REMARK 3 S TENSOR
REMARK 3 S11: 0.0215 S12: 0.6366 S13: -0.0876
REMARK 3 S21: -0.0325 S22: 0.1346 S23: 0.2068
REMARK 3 S31: 0.0572 S32: -0.8514 S33: -0.1747
REMARK 3 TLS GROUP : 8
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 2811 THROUGH 2833 )
REMARK 3 ORIGIN FOR THE GROUP (A): -4.3626 -23.7250 -31.2273
REMARK 3 T TENSOR
REMARK 3 T11: 0.1964 T22: 0.1738
REMARK 3 T33: 0.2398 T12: -0.0166
REMARK 3 T13: -0.0060 T23: 0.0123
REMARK 3 L TENSOR
REMARK 3 L11: 5.3218 L22: 2.2241
REMARK 3 L33: 3.6993 L12: -1.6446
REMARK 3 L13: -0.3692 L23: 0.5253
REMARK 3 S TENSOR
REMARK 3 S11: 0.0750 S12: -0.0193 S13: 0.2626
REMARK 3 S21: -0.1537 S22: -0.0063 S23: 0.2083
REMARK 3 S31: 0.0572 S32: -0.1830 S33: -0.0687
REMARK 3 TLS GROUP : 9
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 2834 THROUGH 2859 )
REMARK 3 ORIGIN FOR THE GROUP (A): 3.7035 -21.0505 -33.0487
REMARK 3 T TENSOR
REMARK 3 T11: 0.2748 T22: 0.1648
REMARK 3 T33: 0.2402 T12: -0.0175
REMARK 3 T13: 0.0026 T23: 0.0084
REMARK 3 L TENSOR
REMARK 3 L11: 0.2555 L22: 1.3489
REMARK 3 L33: 2.6514 L12: -0.5246
REMARK 3 L13: -0.4197 L23: 0.2447
REMARK 3 S TENSOR
REMARK 3 S11: 0.1563 S12: -0.0854 S13: 0.2583
REMARK 3 S21: -0.1150 S22: -0.0388 S23: -0.0310
REMARK 3 S31: -0.3626 S32: 0.1056 S33: -0.1461
REMARK 3 TLS GROUP : 10
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 2860 THROUGH 2877 )
REMARK 3 ORIGIN FOR THE GROUP (A): 18.6758 -35.8481 -36.2231
REMARK 3 T TENSOR
REMARK 3 T11: 0.2718 T22: 0.3103
REMARK 3 T33: 0.2687 T12: 0.0550
REMARK 3 T13: 0.0407 T23: 0.0492
REMARK 3 L TENSOR
REMARK 3 L11: 4.5524 L22: 4.2705
REMARK 3 L33: 8.6814 L12: -1.1791
REMARK 3 L13: -1.9286 L23: -1.3593
REMARK 3 S TENSOR
REMARK 3 S11: -0.0045 S12: 0.0309 S13: 0.1425
REMARK 3 S21: -0.3530 S22: -0.2310 S23: -0.3689
REMARK 3 S31: 0.6457 S32: 0.6360 S33: 0.1474
REMARK 3 TLS GROUP : 11
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 2878 THROUGH 2962 )
REMARK 3 ORIGIN FOR THE GROUP (A): 6.3040 -22.9654 -29.9314
REMARK 3 T TENSOR
REMARK 3 T11: 0.1737 T22: 0.1455
REMARK 3 T33: 0.1730 T12: -0.0472
REMARK 3 T13: -0.0058 T23: -0.0169
REMARK 3 L TENSOR
REMARK 3 L11: 1.7212 L22: 1.4143
REMARK 3 L33: 3.5373 L12: -0.4979
REMARK 3 L13: -0.7605 L23: 0.0007
REMARK 3 S TENSOR
REMARK 3 S11: 0.0132 S12: -0.0875 S13: 0.1398
REMARK 3 S21: -0.0136 S22: -0.0005 S23: -0.0088
REMARK 3 S31: -0.1560 S32: 0.1756 S33: -0.0252
REMARK 3 TLS GROUP : 12
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 2963 THROUGH 2981 )
REMARK 3 ORIGIN FOR THE GROUP (A): -6.1629 -29.3547 -15.4437
REMARK 3 T TENSOR
REMARK 3 T11: 0.2849 T22: 0.2840
REMARK 3 T33: 0.2736 T12: -0.0342
REMARK 3 T13: 0.0652 T23: 0.0470
REMARK 3 L TENSOR
REMARK 3 L11: 5.0075 L22: 5.4101
REMARK 3 L33: 5.9010 L12: -2.8106
REMARK 3 L13: -2.0763 L23: 2.7790
REMARK 3 S TENSOR
REMARK 3 S11: -0.5228 S12: -0.8687 S13: -0.5381
REMARK 3 S21: 0.5850 S22: 0.2562 S23: 0.6395
REMARK 3 S31: 0.2637 S32: 0.0126 S33: 0.2494
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' AND (RESID 2727 THROUGH 2817
REMARK 3 OR RESID 2819 THROUGH 2979))
REMARK 3 SELECTION : (CHAIN 'B' AND (RESID 2727 THROUGH 2740
REMARK 3 OR (RESID 2741 THROUGH 2742 AND (NAME N
REMARK 3 OR NAME CA OR NAME C OR NAME O OR NAME CB
REMARK 3 )) OR RESID 2743 THROUGH 2817 OR RESID
REMARK 3 2819 THROUGH 2876 OR (RESID 2877 THROUGH
REMARK 3 2878 AND (NAME N OR NAME CA OR NAME C OR
REMARK 3 NAME O OR NAME CB )) OR RESID 2879 OR
REMARK 3 (RESID 2880 AND (NAME N OR NAME CA OR
REMARK 3 NAME C OR NAME O OR NAME CB )) OR RESID
REMARK 3 2881 THROUGH 2979))
REMARK 3 ATOM PAIRS NUMBER : NULL
REMARK 3 RMSD : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 8W2C COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 23-FEB-24.
REMARK 100 THE DEPOSITION ID IS D_1000281604.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 14-JUL-17
REMARK 200 TEMPERATURE (KELVIN) : 80
REMARK 200 PH : 7.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SSRL
REMARK 200 BEAMLINE : BL9-2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.979
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : NULL
REMARK 200 DATA SCALING SOFTWARE : NULL
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 39586
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.900
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 (%) : 94.3
REMARK 200 DATA REDUNDANCY : 6.200
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 11.4000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.90
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.00
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
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
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 43.86
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.19
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 100 MM AMMONIUM BROMIDE, AND 40% PEG
REMARK 280 20,000, PH 7.0, VAPOR DIFFUSION, TEMPERATURE 293.7K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,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 41.59500
REMARK 290 SMTRY3 2 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 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 2703
REMARK 465 SER A 2704
REMARK 465 SER A 2705
REMARK 465 HIS A 2706
REMARK 465 HIS A 2707
REMARK 465 HIS A 2708
REMARK 465 HIS A 2709
REMARK 465 HIS A 2710
REMARK 465 HIS A 2711
REMARK 465 SER A 2712
REMARK 465 SER A 2713
REMARK 465 GLY A 2714
REMARK 465 LEU A 2715
REMARK 465 VAL A 2716
REMARK 465 PRO A 2717
REMARK 465 ARG A 2718
REMARK 465 GLY A 2719
REMARK 465 SER A 2720
REMARK 465 HIS A 2721
REMARK 465 MET A 2722
REMARK 465 ALA A 2723
REMARK 465 SER A 2724
REMARK 465 GLU A 2725
REMARK 465 GLU A 2726
REMARK 465 LYS A 2980
REMARK 465 GLY A 2981
REMARK 465 VAL A 2982
REMARK 465 THR A 2983
REMARK 465 ALA A 2984
REMARK 465 GLY B 2703
REMARK 465 SER B 2704
REMARK 465 SER B 2705
REMARK 465 HIS B 2706
REMARK 465 HIS B 2707
REMARK 465 HIS B 2708
REMARK 465 HIS B 2709
REMARK 465 HIS B 2710
REMARK 465 HIS B 2711
REMARK 465 SER B 2712
REMARK 465 SER B 2713
REMARK 465 GLY B 2714
REMARK 465 LEU B 2715
REMARK 465 VAL B 2716
REMARK 465 PRO B 2717
REMARK 465 ARG B 2718
REMARK 465 GLY B 2719
REMARK 465 SER B 2720
REMARK 465 HIS B 2721
REMARK 465 MET B 2722
REMARK 465 ALA B 2723
REMARK 465 SER B 2724
REMARK 465 GLU B 2725
REMARK 465 VAL B 2982
REMARK 465 THR B 2983
REMARK 465 ALA B 2984
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 A2741 CG CD CE NZ
REMARK 470 GLN A2877 CG CD OE1 NE2
REMARK 470 PRO A2878 CG CD
REMARK 470 GLU A2880 CG CD OE1 OE2
REMARK 470 ARG A2944 CG CD NE CZ NH1 NH2
REMARK 470 GLU B2726 CG CD OE1 OE2
REMARK 470 ARG B2944 CG CD NE CZ NH1 NH2
REMARK 470 LYS B2980 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 OD2 ASP A 2837 O HOH A 3101 2.19
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 CYS B2818 CA - CB - SG ANGL. DEV. = 8.0 DEGREES
REMARK 500 CYS B2818 CA - CB - SG ANGL. DEV. = 8.5 DEGREES
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 ALA A2768 61.75 -151.21
REMARK 500 CYS A2818 -124.25 47.87
REMARK 500 CYS A2818 -119.57 40.00
REMARK 500 CYS A2962 57.92 -145.26
REMARK 500 ALA B2768 61.97 -153.41
REMARK 500 CYS B2818 -126.42 45.67
REMARK 500 CYS B2818 -121.59 37.48
REMARK 500 TYR B2957 72.46 -101.34
REMARK 500 CYS B2962 56.07 -145.34
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 NA A3007 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH A3207 O
REMARK 620 2 HOH A3211 O 128.5
REMARK 620 N 1
DBREF1 8W2C A 2723 2984 UNP A0A1I9RH13_9BURK
DBREF2 8W2C A A0A1I9RH13 2723 2984
DBREF1 8W2C B 2723 2984 UNP A0A1I9RH13_9BURK
DBREF2 8W2C B A0A1I9RH13 2723 2984
SEQADV 8W2C GLY A 2703 UNP A0A1I9RH1 EXPRESSION TAG
SEQADV 8W2C SER A 2704 UNP A0A1I9RH1 EXPRESSION TAG
SEQADV 8W2C SER A 2705 UNP A0A1I9RH1 EXPRESSION TAG
SEQADV 8W2C HIS A 2706 UNP A0A1I9RH1 EXPRESSION TAG
SEQADV 8W2C HIS A 2707 UNP A0A1I9RH1 EXPRESSION TAG
SEQADV 8W2C HIS A 2708 UNP A0A1I9RH1 EXPRESSION TAG
SEQADV 8W2C HIS A 2709 UNP A0A1I9RH1 EXPRESSION TAG
SEQADV 8W2C HIS A 2710 UNP A0A1I9RH1 EXPRESSION TAG
SEQADV 8W2C HIS A 2711 UNP A0A1I9RH1 EXPRESSION TAG
SEQADV 8W2C SER A 2712 UNP A0A1I9RH1 EXPRESSION TAG
SEQADV 8W2C SER A 2713 UNP A0A1I9RH1 EXPRESSION TAG
SEQADV 8W2C GLY A 2714 UNP A0A1I9RH1 EXPRESSION TAG
SEQADV 8W2C LEU A 2715 UNP A0A1I9RH1 EXPRESSION TAG
SEQADV 8W2C VAL A 2716 UNP A0A1I9RH1 EXPRESSION TAG
SEQADV 8W2C PRO A 2717 UNP A0A1I9RH1 EXPRESSION TAG
SEQADV 8W2C ARG A 2718 UNP A0A1I9RH1 EXPRESSION TAG
SEQADV 8W2C GLY A 2719 UNP A0A1I9RH1 EXPRESSION TAG
SEQADV 8W2C SER A 2720 UNP A0A1I9RH1 EXPRESSION TAG
SEQADV 8W2C HIS A 2721 UNP A0A1I9RH1 EXPRESSION TAG
SEQADV 8W2C MET A 2722 UNP A0A1I9RH1 EXPRESSION TAG
SEQADV 8W2C GLY B 2703 UNP A0A1I9RH1 EXPRESSION TAG
SEQADV 8W2C SER B 2704 UNP A0A1I9RH1 EXPRESSION TAG
SEQADV 8W2C SER B 2705 UNP A0A1I9RH1 EXPRESSION TAG
SEQADV 8W2C HIS B 2706 UNP A0A1I9RH1 EXPRESSION TAG
SEQADV 8W2C HIS B 2707 UNP A0A1I9RH1 EXPRESSION TAG
SEQADV 8W2C HIS B 2708 UNP A0A1I9RH1 EXPRESSION TAG
SEQADV 8W2C HIS B 2709 UNP A0A1I9RH1 EXPRESSION TAG
SEQADV 8W2C HIS B 2710 UNP A0A1I9RH1 EXPRESSION TAG
SEQADV 8W2C HIS B 2711 UNP A0A1I9RH1 EXPRESSION TAG
SEQADV 8W2C SER B 2712 UNP A0A1I9RH1 EXPRESSION TAG
SEQADV 8W2C SER B 2713 UNP A0A1I9RH1 EXPRESSION TAG
SEQADV 8W2C GLY B 2714 UNP A0A1I9RH1 EXPRESSION TAG
SEQADV 8W2C LEU B 2715 UNP A0A1I9RH1 EXPRESSION TAG
SEQADV 8W2C VAL B 2716 UNP A0A1I9RH1 EXPRESSION TAG
SEQADV 8W2C PRO B 2717 UNP A0A1I9RH1 EXPRESSION TAG
SEQADV 8W2C ARG B 2718 UNP A0A1I9RH1 EXPRESSION TAG
SEQADV 8W2C GLY B 2719 UNP A0A1I9RH1 EXPRESSION TAG
SEQADV 8W2C SER B 2720 UNP A0A1I9RH1 EXPRESSION TAG
SEQADV 8W2C HIS B 2721 UNP A0A1I9RH1 EXPRESSION TAG
SEQADV 8W2C MET B 2722 UNP A0A1I9RH1 EXPRESSION TAG
SEQRES 1 A 282 GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY LEU
SEQRES 2 A 282 VAL PRO ARG GLY SER HIS MET ALA SER GLU GLU SER SER
SEQRES 3 A 282 SER ILE VAL LEU MET ALA GLY ASP PRO ALA THR ALA LYS
SEQRES 4 A 282 ALA VAL VAL VAL CYS VAL ALA ASN ALA ALA GLY GLY PRO
SEQRES 5 A 282 VAL ASN PHE VAL ASP MET SER ARG ALA MET PRO GLU GLN
SEQRES 6 A 282 ALA SER ASP VAL ALA MET PHE GLY VAL LYS LEU PRO ARG
SEQRES 7 A 282 THR GLU VAL ASP SER ASP GLY ALA MET LEU GLU GLU VAL
SEQRES 8 A 282 ARG ARG LEU SER ASN ALA VAL CYS ASP ASP LEU LEU ALA
SEQRES 9 A 282 ALA THR ASP LEU PRO ALA ILE VAL PHE ALA GLN CYS ASN
SEQRES 10 A 282 GLY SER ALA LEU ALA LEU ALA ILE THR ARG GLU LEU VAL
SEQRES 11 A 282 ARG ARG SER ALA ASP VAL ARG ALA LEU CYS ILE GLY GLY
SEQRES 12 A 282 ALA LEU MET ARG THR VAL THR GLY LYS ARG ASP THR ARG
SEQRES 13 A 282 THR ASP ASP GLU ILE LEU ALA PHE LEU GLY LYS ALA GLY
SEQRES 14 A 282 SER THR LEU PRO ALA GLN PRO ASP GLU GLN ALA PHE PHE
SEQRES 15 A 282 LEU HIS ASP PHE ARG TYR ASP GLY TRP LEU ALA ASP VAL
SEQRES 16 A 282 TYR TYR ASN HIS LEU VAL ASP LEU MET SER ARG GLY ALA
SEQRES 17 A 282 LEU GLU VAL VAL ASP ILE PRO VAL TRP CYS LEU VAL GLY
SEQRES 18 A 282 SER GLU ASP PRO LEU VAL PRO ASN TYR PRO VAL ARG PHE
SEQRES 19 A 282 GLN ASP TRP SER HIS ILE GLY ARG PRO VAL GLN LEU VAL
SEQRES 20 A 282 GLU TYR ALA GLY ILE GLY HIS TYR LEU LEU ARG ASP CYS
SEQRES 21 A 282 PRO GLU ALA ILE ALA ARG ALA VAL GLY SER VAL TRP GLU
SEQRES 22 A 282 HIS VAL SER CYS LYS GLY VAL THR ALA
SEQRES 1 B 282 GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY LEU
SEQRES 2 B 282 VAL PRO ARG GLY SER HIS MET ALA SER GLU GLU SER SER
SEQRES 3 B 282 SER ILE VAL LEU MET ALA GLY ASP PRO ALA THR ALA LYS
SEQRES 4 B 282 ALA VAL VAL VAL CYS VAL ALA ASN ALA ALA GLY GLY PRO
SEQRES 5 B 282 VAL ASN PHE VAL ASP MET SER ARG ALA MET PRO GLU GLN
SEQRES 6 B 282 ALA SER ASP VAL ALA MET PHE GLY VAL LYS LEU PRO ARG
SEQRES 7 B 282 THR GLU VAL ASP SER ASP GLY ALA MET LEU GLU GLU VAL
SEQRES 8 B 282 ARG ARG LEU SER ASN ALA VAL CYS ASP ASP LEU LEU ALA
SEQRES 9 B 282 ALA THR ASP LEU PRO ALA ILE VAL PHE ALA GLN CYS ASN
SEQRES 10 B 282 GLY SER ALA LEU ALA LEU ALA ILE THR ARG GLU LEU VAL
SEQRES 11 B 282 ARG ARG SER ALA ASP VAL ARG ALA LEU CYS ILE GLY GLY
SEQRES 12 B 282 ALA LEU MET ARG THR VAL THR GLY LYS ARG ASP THR ARG
SEQRES 13 B 282 THR ASP ASP GLU ILE LEU ALA PHE LEU GLY LYS ALA GLY
SEQRES 14 B 282 SER THR LEU PRO ALA GLN PRO ASP GLU GLN ALA PHE PHE
SEQRES 15 B 282 LEU HIS ASP PHE ARG TYR ASP GLY TRP LEU ALA ASP VAL
SEQRES 16 B 282 TYR TYR ASN HIS LEU VAL ASP LEU MET SER ARG GLY ALA
SEQRES 17 B 282 LEU GLU VAL VAL ASP ILE PRO VAL TRP CYS LEU VAL GLY
SEQRES 18 B 282 SER GLU ASP PRO LEU VAL PRO ASN TYR PRO VAL ARG PHE
SEQRES 19 B 282 GLN ASP TRP SER HIS ILE GLY ARG PRO VAL GLN LEU VAL
SEQRES 20 B 282 GLU TYR ALA GLY ILE GLY HIS TYR LEU LEU ARG ASP CYS
SEQRES 21 B 282 PRO GLU ALA ILE ALA ARG ALA VAL GLY SER VAL TRP GLU
SEQRES 22 B 282 HIS VAL SER CYS LYS GLY VAL THR ALA
HET EDO A3001 10
HET EDO A3002 10
HET EDO A3003 10
HET EDO A3004 10
HET EDO A3005 10
HET EDO A3006 10
HET NA A3007 1
HET EDO B3001 10
HETNAM EDO 1,2-ETHANEDIOL
HETNAM NA SODIUM ION
HETSYN EDO ETHYLENE GLYCOL
FORMUL 3 EDO 7(C2 H6 O2)
FORMUL 9 NA NA 1+
FORMUL 11 HOH *283(H2 O)
HELIX 1 AA1 GLY A 2753 ASN A 2756 5 4
HELIX 2 AA2 PHE A 2757 ALA A 2768 1 12
HELIX 3 AA3 SER A 2785 THR A 2808 1 24
HELIX 4 AA4 GLY A 2820 ARG A 2834 1 15
HELIX 5 AA5 THR A 2859 GLY A 2871 1 13
HELIX 6 AA6 GLN A 2877 ARG A 2908 1 32
HELIX 7 AA7 ASN A 2931 PHE A 2936 1 6
HELIX 8 AA8 GLN A 2937 ILE A 2942 5 6
HELIX 9 AA9 TYR A 2957 CYS A 2962 1 6
HELIX 10 AB1 CYS A 2962 SER A 2978 1 17
HELIX 11 AB2 GLY B 2753 ASN B 2756 5 4
HELIX 12 AB3 PHE B 2757 ALA B 2768 1 12
HELIX 13 AB4 SER B 2785 THR B 2808 1 24
HELIX 14 AB5 GLY B 2820 ARG B 2834 1 15
HELIX 15 AB6 THR B 2859 ALA B 2870 1 12
HELIX 16 AB7 GLN B 2877 ARG B 2908 1 32
HELIX 17 AB8 ASN B 2931 PHE B 2936 1 6
HELIX 18 AB9 GLN B 2937 ILE B 2942 5 6
HELIX 19 AC1 TYR B 2957 CYS B 2962 1 6
HELIX 20 AC2 CYS B 2962 SER B 2978 1 17
SHEET 1 AA114 ILE A2730 ALA A2734 0
SHEET 2 AA114 VAL A2771 VAL A2776 -1 O MET A2773 N MET A2733
SHEET 3 AA114 ALA A2742 VAL A2747 1 N VAL A2744 O PHE A2774
SHEET 4 AA114 ALA A2812 GLN A2817 1 O PHE A2815 N VAL A2745
SHEET 5 AA114 VAL A2838 GLY A2844 1 O CYS A2842 N VAL A2814
SHEET 6 AA114 VAL A2918 GLY A2923 1 O TRP A2919 N ILE A2843
SHEET 7 AA114 VAL A2946 TYR A2951 1 O GLN A2947 N VAL A2918
SHEET 8 AA114 VAL B2946 TYR B2951 1 O GLU B2950 N GLU A2950
SHEET 9 AA114 VAL B2918 GLY B2923 1 N VAL B2922 O TYR B2951
SHEET 10 AA114 VAL B2838 GLY B2844 1 N ILE B2843 O TRP B2919
SHEET 11 AA114 ALA B2812 GLN B2817 1 N ALA B2812 O ARG B2839
SHEET 12 AA114 ALA B2742 VAL B2747 1 N VAL B2745 O PHE B2815
SHEET 13 AA114 VAL B2771 VAL B2776 1 O VAL B2776 N CYS B2746
SHEET 14 AA114 ILE B2730 ALA B2734 -1 N MET B2733 O MET B2773
LINK NA NA A3007 O HOH A3207 1555 1555 3.06
LINK NA NA A3007 O HOH A3211 1555 1555 3.00
CISPEP 1 ARG A 2944 PRO A 2945 0 -8.22
CISPEP 2 ARG B 2944 PRO B 2945 0 -9.67
CRYST1 47.096 83.190 69.380 90.00 101.36 90.00 P 1 21 1 4
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 0.021233 0.000000 0.004266 0.00000
SCALE2 0.000000 0.012021 0.000000 0.00000
SCALE3 0.000000 0.000000 0.014701 0.00000
TER 3757 CYS A2979
TER 7575 GLY B2981
MASTER 538 0 8 20 14 0 0 6 4132 2 73 44
END |