HEADER HYDROLASE 06-MAY-10 3MWR
TITLE CRYSTAL STRUCTURE OF RIBONUCLEASE A TANDEM ENZYMES AND THEIR
TITLE 2 INTERACTION WITH THE CYTOSOLIC RIBONUCLEASE INHIBITOR
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: RIBONUCLEASE PANCREATIC, LINKER, RIBONUCLEASE PANCREATIC;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: RNASE 1, RNASE A;
COMPND 5 EC: 3.1.27.5;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: BOS TAURUS;
SOURCE 3 ORGANISM_TAXID: 9913;
SOURCE 4 GENE: RNS1;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PET26B(+)
KEYWDS RIBONUCLEASE A TANDEM ENZYME, SGSGSG-LINKER, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR P.NEUMANN,F.LEICH
REVDAT 4 01-NOV-23 3MWR 1 REMARK
REVDAT 3 28-JUN-17 3MWR 1 SOURCE
REVDAT 2 12-FEB-14 3MWR 1 REMARK VERSN
REVDAT 1 09-FEB-11 3MWR 0
JRNL AUTH U.ARNOLD,F.LEICH,P.NEUMANN,H.LILIE,R.ULBRICH-HOFMANN
JRNL TITL CRYSTAL STRUCTURE OF RNASE A TANDEM ENZYMES AND THEIR
JRNL TITL 2 INTERACTION WITH THE CYTOSOLIC RIBONUCLEASE INHIBITOR
JRNL REF FEBS J. V. 278 331 2011
JRNL REFN ISSN 1742-464X
JRNL PMID 21134128
JRNL DOI 10.1111/J.1742-4658.2010.07957.X
REMARK 2
REMARK 2 RESOLUTION. 1.85 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,
REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,
REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,
REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON,
REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,
REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT
REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.85
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 24.03
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.380
REMARK 3 COMPLETENESS FOR RANGE (%) : 93.4
REMARK 3 NUMBER OF REFLECTIONS : 21141
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 : 0.207
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.110
REMARK 3 FREE R VALUE TEST SET COUNT : 1963
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 24.0350 - 4.4500 0.92 2546 152 0.1790 0.1850
REMARK 3 2 4.4500 - 3.5360 0.95 2647 141 0.1340 0.1270
REMARK 3 3 3.5360 - 3.0900 0.96 2686 132 0.1510 0.2290
REMARK 3 4 3.0900 - 2.8080 0.96 2650 180 0.1820 0.2150
REMARK 3 5 2.8080 - 2.6070 0.95 2698 122 0.1770 0.2480
REMARK 3 6 2.6070 - 2.4530 0.94 2612 143 0.1750 0.1850
REMARK 3 7 2.4530 - 2.3300 0.94 2616 127 0.1750 0.2470
REMARK 3 8 2.3300 - 2.2290 0.94 2630 149 0.1880 0.2420
REMARK 3 9 2.2290 - 2.1430 0.93 2613 124 0.1760 0.2710
REMARK 3 10 2.1430 - 2.0690 0.94 2560 161 0.1870 0.2080
REMARK 3 11 2.0690 - 2.0050 0.90 2583 152 0.1930 0.2270
REMARK 3 12 2.0050 - 1.9470 0.93 2530 139 0.2240 0.2850
REMARK 3 13 1.9470 - 1.8960 0.90 2538 131 0.2390 0.2790
REMARK 3 14 1.8960 - 1.8500 0.92 2559 110 0.2460 0.2900
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3 K_SOL : 0.40
REMARK 3 B_SOL : 86.85
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.220
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : NULL
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 27.23
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 42.40
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -7.56600
REMARK 3 B22 (A**2) : 2.01800
REMARK 3 B33 (A**2) : 5.54700
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 2.59900
REMARK 3 B23 (A**2) : 0.00000
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 2014
REMARK 3 ANGLE : 0.808 2714
REMARK 3 CHIRALITY : 0.054 296
REMARK 3 PLANARITY : 0.003 356
REMARK 3 DIHEDRAL : 14.164 726
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 11
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN A AND (RESSEQ 1:15)
REMARK 3 ORIGIN FOR THE GROUP (A): 32.5088 9.0118 11.1553
REMARK 3 T TENSOR
REMARK 3 T11: 0.3587 T22: 0.4372
REMARK 3 T33: 0.2001 T12: 0.1574
REMARK 3 T13: 0.0955 T23: 0.1708
REMARK 3 L TENSOR
REMARK 3 L11: 4.1672 L22: 1.7807
REMARK 3 L33: 3.0705 L12: -0.3484
REMARK 3 L13: -2.7240 L23: -1.6729
REMARK 3 S TENSOR
REMARK 3 S11: 0.3834 S12: 1.3270 S13: 0.5270
REMARK 3 S21: -0.3415 S22: -0.1567 S23: 0.0711
REMARK 3 S31: -0.5960 S32: -0.7580 S33: -0.3040
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN A AND (RESSEQ 16:24)
REMARK 3 ORIGIN FOR THE GROUP (A): 26.5776 -2.1472 -2.1326
REMARK 3 T TENSOR
REMARK 3 T11: 0.4200 T22: 2.0322
REMARK 3 T33: 0.3934 T12: 0.1022
REMARK 3 T13: -0.0070 T23: -0.3814
REMARK 3 L TENSOR
REMARK 3 L11: 0.9139 L22: 6.3089
REMARK 3 L33: 1.9159 L12: -1.1798
REMARK 3 L13: 0.0312 L23: 1.9071
REMARK 3 S TENSOR
REMARK 3 S11: -0.2346 S12: 0.0673 S13: -0.0903
REMARK 3 S21: -0.5999 S22: 0.4703 S23: 0.4012
REMARK 3 S31: -0.3926 S32: -0.0100 S33: -0.0432
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN A AND (RESSEQ 25:42)
REMARK 3 ORIGIN FOR THE GROUP (A): 39.0065 3.3315 1.6508
REMARK 3 T TENSOR
REMARK 3 T11: 0.3686 T22: 0.9211
REMARK 3 T33: 0.1550 T12: 0.0601
REMARK 3 T13: 0.1081 T23: -0.0321
REMARK 3 L TENSOR
REMARK 3 L11: 3.4252 L22: 1.6389
REMARK 3 L33: -1.1210 L12: -0.4848
REMARK 3 L13: -1.2194 L23: 0.9805
REMARK 3 S TENSOR
REMARK 3 S11: 0.2582 S12: 1.8031 S13: -0.0560
REMARK 3 S21: -0.6274 S22: -0.1789 S23: -0.2312
REMARK 3 S31: -0.7385 S32: -1.2078 S33: -0.0686
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN A AND (RESSEQ 43:86 OR RESSEQ 98:124)
REMARK 3 ORIGIN FOR THE GROUP (A): 28.7090 -1.4700 16.2111
REMARK 3 T TENSOR
REMARK 3 T11: 0.1221 T22: 0.3054
REMARK 3 T33: 0.1909 T12: -0.0077
REMARK 3 T13: 0.0140 T23: -0.0906
REMARK 3 L TENSOR
REMARK 3 L11: 4.0950 L22: 1.6204
REMARK 3 L33: 2.4411 L12: -0.3387
REMARK 3 L13: -2.9999 L23: 0.0256
REMARK 3 S TENSOR
REMARK 3 S11: -0.1861 S12: 0.9617 S13: -0.4834
REMARK 3 S21: 0.0249 S22: -0.0744 S23: 0.0112
REMARK 3 S31: 0.0321 S32: -0.7364 S33: 0.2199
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: CHAIN A AND (RESSEQ 87:97)
REMARK 3 ORIGIN FOR THE GROUP (A): 45.4648 -2.2957 -2.7276
REMARK 3 T TENSOR
REMARK 3 T11: 0.4237 T22: 0.9345
REMARK 3 T33: 0.2859 T12: 0.0770
REMARK 3 T13: 0.2065 T23: -0.1420
REMARK 3 L TENSOR
REMARK 3 L11: 0.7584 L22: 0.6453
REMARK 3 L33: 0.0591 L12: -0.4988
REMARK 3 L13: -0.0369 L23: -0.1524
REMARK 3 S TENSOR
REMARK 3 S11: 0.2545 S12: 0.9371 S13: -0.1348
REMARK 3 S21: -0.8705 S22: -0.4611 S23: -0.0115
REMARK 3 S31: -0.2616 S32: -0.0100 S33: 0.0436
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: CHAIN A AND (RESSEQ 125:134)
REMARK 3 ORIGIN FOR THE GROUP (A): 21.8334 -15.7136 24.4504
REMARK 3 T TENSOR
REMARK 3 T11: 0.4195 T22: 0.7366
REMARK 3 T33: 0.6573 T12: 0.0864
REMARK 3 T13: -0.0674 T23: -0.3123
REMARK 3 L TENSOR
REMARK 3 L11: 0.5963 L22: 1.1152
REMARK 3 L33: 1.9675 L12: -0.1583
REMARK 3 L13: -0.4689 L23: -0.9480
REMARK 3 S TENSOR
REMARK 3 S11: -0.3119 S12: -0.3433 S13: 0.0826
REMARK 3 S21: -0.1286 S22: -0.2728 S23: -0.2354
REMARK 3 S31: -0.0271 S32: -0.2457 S33: 0.3939
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: CHAIN A AND (RESSEQ 135:146)
REMARK 3 ORIGIN FOR THE GROUP (A): 15.508 -2.652 29.488
REMARK 3 T TENSOR
REMARK 3 T11: 0.1726 T22: 0.2907
REMARK 3 T33: 0.1798 T12: 0.0008
REMARK 3 T13: -0.0228 T23: -0.0991
REMARK 3 L TENSOR
REMARK 3 L11: 4.2365 L22: 1.9102
REMARK 3 L33: -0.1372 L12: 0.6779
REMARK 3 L13: -0.3866 L23: 0.2245
REMARK 3 S TENSOR
REMARK 3 S11: -0.2262 S12: 1.0719 S13: -0.1157
REMARK 3 S21: 0.1079 S22: 0.2765 S23: -0.1631
REMARK 3 S31: -0.0336 S32: 0.2964 S33: -0.0822
REMARK 3 TLS GROUP : 8
REMARK 3 SELECTION: CHAIN A AND (RESSEQ 147:155)
REMARK 3 ORIGIN FOR THE GROUP (A): 8.153 8.329 21.377
REMARK 3 T TENSOR
REMARK 3 T11: 0.1960 T22: 0.5102
REMARK 3 T33: 0.5030 T12: -0.1393
REMARK 3 T13: -0.1263 T23: 0.2139
REMARK 3 L TENSOR
REMARK 3 L11: 1.1061 L22: 0.0866
REMARK 3 L33: 1.5042 L12: -1.5474
REMARK 3 L13: 0.2127 L23: 0.3751
REMARK 3 S TENSOR
REMARK 3 S11: -0.3005 S12: 0.2695 S13: 0.3957
REMARK 3 S21: -0.3350 S22: 0.3811 S23: 0.0369
REMARK 3 S31: 0.0057 S32: 0.0518 S33: -0.1698
REMARK 3 TLS GROUP : 9
REMARK 3 SELECTION: CHAIN A AND (RESSEQ 156:172)
REMARK 3 ORIGIN FOR THE GROUP (A): 8.1213 -4.5741 19.8844
REMARK 3 T TENSOR
REMARK 3 T11: 0.2277 T22: 0.6342
REMARK 3 T33: 0.1617 T12: -0.0238
REMARK 3 T13: 0.0044 T23: -0.0497
REMARK 3 L TENSOR
REMARK 3 L11: 3.7563 L22: 3.2927
REMARK 3 L33: -0.5281 L12: -0.3057
REMARK 3 L13: 1.6109 L23: 0.9860
REMARK 3 S TENSOR
REMARK 3 S11: -0.0703 S12: 1.6410 S13: 0.0119
REMARK 3 S21: -0.6276 S22: 0.0600 S23: -0.2295
REMARK 3 S31: -0.0811 S32: 0.6236 S33: -0.0263
REMARK 3 TLS GROUP : 10
REMARK 3 SELECTION: CHAIN A AND (RESSEQ 173:220 OR RESSEQ 228:254)
REMARK 3 ORIGIN FOR THE GROUP (A): 9.2656 0.1641 37.1570
REMARK 3 T TENSOR
REMARK 3 T11: 0.1486 T22: 0.0985
REMARK 3 T33: 0.2285 T12: -0.0133
REMARK 3 T13: -0.0065 T23: -0.0129
REMARK 3 L TENSOR
REMARK 3 L11: 2.9157 L22: -0.0094
REMARK 3 L33: 1.2798 L12: 0.2886
REMARK 3 L13: 0.5652 L23: 0.5639
REMARK 3 S TENSOR
REMARK 3 S11: -0.0814 S12: 0.1109 S13: 0.0179
REMARK 3 S21: -0.0192 S22: 0.0468 S23: 0.1388
REMARK 3 S31: -0.0502 S32: 0.0452 S33: 0.0383
REMARK 3 TLS GROUP : 11
REMARK 3 SELECTION: CHAIN A AND (RESSEQ 221:227)
REMARK 3 ORIGIN FOR THE GROUP (A): -1.0358 -9.0560 15.4420
REMARK 3 T TENSOR
REMARK 3 T11: 0.3207 T22: 0.8726
REMARK 3 T33: 0.4186 T12: -0.0133
REMARK 3 T13: -0.0666 T23: -0.2537
REMARK 3 L TENSOR
REMARK 3 L11: 2.4519 L22: -0.1286
REMARK 3 L33: 1.5210 L12: -1.8695
REMARK 3 L13: -1.2350 L23: 0.2647
REMARK 3 S TENSOR
REMARK 3 S11: 0.6952 S12: 0.3673 S13: -0.9357
REMARK 3 S21: -0.2610 S22: -0.3195 S23: 0.1782
REMARK 3 S31: 0.2149 S32: 0.2885 S33: -0.2598
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 3MWR COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 31-MAY-10.
REMARK 100 THE DEPOSITION ID IS D_1000059090.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 07-JUL-07
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 5.9
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : ROTATING ANODE
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : RIGAKU MICROMAX-007
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : GRAPHITE
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : RIGAKU RAXIS IV++
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA 3.2.21
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 21141
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.850
REMARK 200 RESOLUTION RANGE LOW (A) : 73.922
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.6
REMARK 200 DATA REDUNDANCY : 5.000
REMARK 200 R MERGE (I) : 0.08000
REMARK 200 R SYM (I) : 0.08000
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 5.8040
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.85
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.95
REMARK 200 COMPLETENESS FOR SHELL (%) : 97.3
REMARK 200 DATA REDUNDANCY IN SHELL : 5.00
REMARK 200 R MERGE FOR SHELL (I) : 0.55800
REMARK 200 R SYM FOR SHELL (I) : 0.55800
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.300
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHENIX
REMARK 200 STARTING MODEL: 3MWQ
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 44.99
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.24
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 30% PEG 8000, 0.2M AMMONIUM SULFATE,
REMARK 280 PH 5.9, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 286K
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 50.95150
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 16.53350
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 50.95150
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 16.53350
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
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: MONOMERIC
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 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375 HOH A 315 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A 514 LIES ON A SPECIAL POSITION.
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 SER A 127
REMARK 465 GLY A 128
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 SER A 15 35.00 -83.62
REMARK 500 HIS A 48 64.84 -100.29
REMARK 500 GLN A 60 -138.98 -106.72
REMARK 500 GLN A 60 -138.98 -98.04
REMARK 500 ASN A 71 38.57 -95.75
REMARK 500 HIS A 178 69.37 -101.38
REMARK 500 GLN A 190 -134.75 -103.70
REMARK 500 GLN A 190 -134.44 -103.70
REMARK 500 PRO A 223 30.49 -88.83
REMARK 500 ASN A 224 70.53 -111.76
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 SO4 A 255
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 256
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 257
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 258
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 259
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1R3M RELATED DB: PDB
REMARK 900 X-RAY STRUCTURE OF UNSWAPPED DIMER OF BOVINE SEMINAL RIBONUCLEASE
REMARK 900 RELATED ID: 1BSR RELATED DB: PDB
REMARK 900 SWAPPED FORM OF BS-RNASE
REMARK 900 RELATED ID: 1A2W RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF A 3D DOMAIN-SWAPPED DIMER OF RNASE A
REMARK 900 RELATED ID: 7RSA RELATED DB: PDB
REMARK 900 STRUCTURE OF PHOSPHATE-FREE RIBONUCLEASE A
REMARK 900 RELATED ID: 1SRN RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF A FULLY ACTIVE SEMISYNTHETIC RIBONUCLEASE
REMARK 900 RELATED ID: 3MWQ RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF RIBONUCLEASE A TANDEM ENZYME (SGRSGRSG LINKER)
REMARK 900 RELATED ID: 3MX8 RELATED DB: PDB
DBREF 3MWR A 1 124 UNP P61823 RNAS1_BOVIN 27 150
DBREF 3MWR A 125 130 PDB 3MWR 3MWR 125 130
DBREF 3MWR A 131 254 UNP P61823 RNAS1_BOVIN 27 150
SEQRES 1 A 254 LYS GLU THR ALA ALA ALA LYS PHE GLU ARG GLN HIS MET
SEQRES 2 A 254 ASP SER SER THR SER ALA ALA SER SER SER ASN TYR CYS
SEQRES 3 A 254 ASN GLN MET MET LYS SER ARG ASN LEU THR LYS ASP ARG
SEQRES 4 A 254 CYS LYS PRO VAL ASN THR PHE VAL HIS GLU SER LEU ALA
SEQRES 5 A 254 ASP VAL GLN ALA VAL CYS SER GLN LYS ASN VAL ALA CYS
SEQRES 6 A 254 LYS ASN GLY GLN THR ASN CYS TYR GLN SER TYR SER THR
SEQRES 7 A 254 MET SER ILE THR ASP CYS ARG GLU THR GLY SER SER LYS
SEQRES 8 A 254 TYR PRO ASN CYS ALA TYR LYS THR THR GLN ALA ASN LYS
SEQRES 9 A 254 HIS ILE ILE VAL ALA CYS GLU GLY ASN PRO TYR VAL PRO
SEQRES 10 A 254 VAL HIS PHE ASP ALA SER VAL SER GLY SER GLY SER GLY
SEQRES 11 A 254 LYS GLU THR ALA ALA ALA LYS PHE GLU ARG GLN HIS MET
SEQRES 12 A 254 ASP SER SER THR SER ALA ALA SER SER SER ASN TYR CYS
SEQRES 13 A 254 ASN GLN MET MET LYS SER ARG ASN LEU THR LYS ASP ARG
SEQRES 14 A 254 CYS LYS PRO VAL ASN THR PHE VAL HIS GLU SER LEU ALA
SEQRES 15 A 254 ASP VAL GLN ALA VAL CYS SER GLN LYS ASN VAL ALA CYS
SEQRES 16 A 254 LYS ASN GLY GLN THR ASN CYS TYR GLN SER TYR SER THR
SEQRES 17 A 254 MET SER ILE THR ASP CYS ARG GLU THR GLY SER SER LYS
SEQRES 18 A 254 TYR PRO ASN CYS ALA TYR LYS THR THR GLN ALA ASN LYS
SEQRES 19 A 254 HIS ILE ILE VAL ALA CYS GLU GLY ASN PRO TYR VAL PRO
SEQRES 20 A 254 VAL HIS PHE ASP ALA SER VAL
HET SO4 A 255 5
HET SO4 A 256 5
HET SO4 A 257 5
HET SO4 A 258 5
HET GOL A 259 6
HETNAM SO4 SULFATE ION
HETNAM GOL GLYCEROL
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 2 SO4 4(O4 S 2-)
FORMUL 6 GOL C3 H8 O3
FORMUL 7 HOH *318(H2 O)
HELIX 1 1 THR A 3 MET A 13 1 11
HELIX 2 2 ASN A 24 ARG A 33 1 10
HELIX 3 3 SER A 50 VAL A 57 1 8
HELIX 4 4 CYS A 58 GLN A 60 5 3
HELIX 5 5 THR A 133 MET A 143 1 11
HELIX 6 6 ASN A 154 ARG A 163 1 10
HELIX 7 7 SER A 180 ALA A 186 1 7
HELIX 8 8 VAL A 187 GLN A 190 5 4
SHEET 1 A 5 VAL A 43 VAL A 47 0
SHEET 2 A 5 MET A 79 GLU A 86 -1 O CYS A 84 N ASN A 44
SHEET 3 A 5 TYR A 97 GLU A 111 -1 O LYS A 98 N ARG A 85
SHEET 4 A 5 CYS A 72 GLN A 74 -1 N TYR A 73 O VAL A 108
SHEET 5 A 5 LYS A 61 VAL A 63 -1 N LYS A 61 O GLN A 74
SHEET 1 B 4 VAL A 43 VAL A 47 0
SHEET 2 B 4 MET A 79 GLU A 86 -1 O CYS A 84 N ASN A 44
SHEET 3 B 4 TYR A 97 GLU A 111 -1 O LYS A 98 N ARG A 85
SHEET 4 B 4 VAL A 116 VAL A 124 -1 O VAL A 124 N HIS A 105
SHEET 1 C 5 VAL A 173 VAL A 177 0
SHEET 2 C 5 MET A 209 GLU A 216 -1 O CYS A 214 N ASN A 174
SHEET 3 C 5 TYR A 227 GLU A 241 -1 O THR A 230 N ASP A 213
SHEET 4 C 5 CYS A 202 GLN A 204 -1 N TYR A 203 O VAL A 238
SHEET 5 C 5 LYS A 191 VAL A 193 -1 N LYS A 191 O GLN A 204
SHEET 1 D 4 VAL A 173 VAL A 177 0
SHEET 2 D 4 MET A 209 GLU A 216 -1 O CYS A 214 N ASN A 174
SHEET 3 D 4 TYR A 227 GLU A 241 -1 O THR A 230 N ASP A 213
SHEET 4 D 4 VAL A 246 VAL A 254 -1 O VAL A 248 N ALA A 239
SSBOND 1 CYS A 26 CYS A 84 1555 1555 2.04
SSBOND 2 CYS A 40 CYS A 95 1555 1555 2.03
SSBOND 3 CYS A 58 CYS A 110 1555 1555 2.03
SSBOND 4 CYS A 65 CYS A 72 1555 1555 2.03
SSBOND 5 CYS A 156 CYS A 214 1555 1555 2.03
SSBOND 6 CYS A 170 CYS A 225 1555 1555 2.03
SSBOND 7 CYS A 188 CYS A 240 1555 1555 2.02
SSBOND 8 CYS A 195 CYS A 202 1555 1555 2.03
CISPEP 1 TYR A 92 PRO A 93 0 3.16
CISPEP 2 ASN A 113 PRO A 114 0 9.55
CISPEP 3 TYR A 222 PRO A 223 0 0.51
CISPEP 4 ASN A 243 PRO A 244 0 5.86
SITE 1 AC1 8 THR A 3 ALA A 4 ASN A 192 HOH A 357
SITE 2 AC1 8 HOH A 373 HOH A 402 HOH A 421 HOH A 467
SITE 1 AC2 8 GLN A 11 HIS A 12 VAL A 118 HIS A 119
SITE 2 AC2 8 PHE A 120 HOH A 374 HOH A 449 HOH A 480
SITE 1 AC3 9 GLN A 141 HIS A 142 LYS A 171 VAL A 248
SITE 2 AC3 9 HIS A 249 PHE A 250 HOH A 365 HOH A 403
SITE 3 AC3 9 HOH A 451
SITE 1 AC4 5 ALA A 252 SER A 253 HOH A 289 HOH A 345
SITE 2 AC4 5 HOH A 543
SITE 1 AC5 5 SER A 153 THR A 229 THR A 230 GLN A 231
SITE 2 AC5 5 HOH A 576
CRYST1 101.903 33.067 73.869 90.00 90.39 90.00 C 1 2 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 0.009813 0.000000 0.000067 0.00000
SCALE2 0.000000 0.030242 0.000000 0.00000
SCALE3 0.000000 0.000000 0.013538 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
