HEADER HYDROLASE 21-MAY-08 3D7B
TITLE THE RIBONUCLEASE A- 5'-DEOXY-5'-N-PYRROLIDINOURIDINE COMPLEX
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: RIBONUCLEASE PANCREATIC;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: RNASE 1, RNASE A;
COMPND 5 EC: 3.1.27.5
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: BOS TAURUS;
SOURCE 3 ORGANISM_COMMON: BOVINE;
SOURCE 4 ORGANISM_TAXID: 9913
KEYWDS HYDROLASE, RIBONUCLEASE A, LIGAND, ENDONUCLEASE, GLYCATION,
KEYWDS 2 GLYCOPROTEIN, NUCLEASE, SECRETED
EXPDTA X-RAY DIFFRACTION
AUTHOR D.D.LEONIDAS,S.E.ZOGRAPHOS,N.G.OIKONOMAKOS
REVDAT 4 30-AUG-23 3D7B 1 REMARK
REVDAT 3 13-JUL-11 3D7B 1 VERSN
REVDAT 2 30-JUN-09 3D7B 1 JRNL
REVDAT 1 10-FEB-09 3D7B 0
JRNL AUTH A.SAMANTA,D.D.LEONIDAS,S.DASGUPTA,T.PATHAK,S.E.ZOGRAPHOS,
JRNL AUTH 2 N.G.OIKONOMAKOS
JRNL TITL MORPHOLINO, PIPERIDINO, AND PYRROLIDINO DERIVATIVES OF
JRNL TITL 2 PYRIMIDINE NUCLEOSIDES AS INHIBITORS OF RIBONUCLEASE A:
JRNL TITL 3 SYNTHESIS, BIOCHEMICAL, AND CRYSTALLOGRAPHIC EVALUATION.
JRNL REF J.MED.CHEM. V. 52 932 2009
JRNL REFN ISSN 0022-2623
JRNL PMID 19173562
JRNL DOI 10.1021/JM800724T
REMARK 2
REMARK 2 RESOLUTION. 1.60 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.3.0037
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.60
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 30.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 96.2
REMARK 3 NUMBER OF REFLECTIONS : 28676
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING + TEST SET) : 0.180
REMARK 3 R VALUE (WORKING SET) : 0.179
REMARK 3 FREE R VALUE : 0.213
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 1519
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 1.60
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.64
REMARK 3 REFLECTION IN BIN (WORKING SET) : 2062
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 93.85
REMARK 3 BIN R VALUE (WORKING SET) : 0.2130
REMARK 3 BIN FREE R VALUE SET COUNT : 105
REMARK 3 BIN FREE R VALUE : 0.2520
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 1902
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 47
REMARK 3 SOLVENT ATOMS : 346
REMARK 3
REMARK 3 B VALUES.
REMARK 3 B VALUE TYPE : LIKELY RESIDUAL
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 14.92
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.07000
REMARK 3 B22 (A**2) : 0.36000
REMARK 3 B33 (A**2) : -0.29000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.05000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.101
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.100
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.054
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 2.880
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.956
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.937
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 1998 ; 0.007 ; 0.021
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 2707 ; 1.429 ; 1.951
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 246 ; 5.757 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 89 ;35.003 ;25.169
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 339 ;10.903 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 8 ;11.107 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 298 ; 0.135 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 1505 ; 0.004 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 930 ; 0.182 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 1379 ; 0.292 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 282 ; 0.124 ; 0.200
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): 71 ; 0.162 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 44 ; 0.130 ; 0.200
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 1275 ; 0.479 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 2022 ; 0.808 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 800 ; 1.354 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 685 ; 2.214 ; 4.500
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 8
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 1 A 22
REMARK 3 ORIGIN FOR THE GROUP (A): 28.9442 5.8612 6.9621
REMARK 3 T TENSOR
REMARK 3 T11: 0.0885 T22: 0.0782
REMARK 3 T33: 0.0198 T12: 0.0148
REMARK 3 T13: 0.0275 T23: 0.0402
REMARK 3 L TENSOR
REMARK 3 L11: 3.2363 L22: 3.1131
REMARK 3 L33: 7.1260 L12: -0.2955
REMARK 3 L13: 0.2381 L23: 0.5183
REMARK 3 S TENSOR
REMARK 3 S11: 0.1832 S12: 0.2702 S13: -0.0779
REMARK 3 S21: -0.2240 S22: -0.0276 S23: -0.0835
REMARK 3 S31: -0.1554 S32: -0.1291 S33: -0.1556
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 23 A 78
REMARK 3 ORIGIN FOR THE GROUP (A): 30.5230 0.5017 11.4167
REMARK 3 T TENSOR
REMARK 3 T11: 0.0367 T22: 0.0464
REMARK 3 T33: 0.0417 T12: -0.0050
REMARK 3 T13: 0.0056 T23: 0.0060
REMARK 3 L TENSOR
REMARK 3 L11: 1.2456 L22: 0.6582
REMARK 3 L33: 1.9312 L12: -0.0224
REMARK 3 L13: -0.2646 L23: 0.0209
REMARK 3 S TENSOR
REMARK 3 S11: 0.0251 S12: 0.1990 S13: -0.0067
REMARK 3 S21: -0.0823 S22: 0.0516 S23: -0.1014
REMARK 3 S31: -0.0582 S32: -0.0748 S33: -0.0767
REMARK 3
REMARK 3 TLS GROUP : 3
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 79 A 99
REMARK 3 ORIGIN FOR THE GROUP (A): 38.8614 -4.7361 1.2183
REMARK 3 T TENSOR
REMARK 3 T11: 0.0399 T22: 0.0356
REMARK 3 T33: 0.0325 T12: -0.0146
REMARK 3 T13: 0.0344 T23: -0.0659
REMARK 3 L TENSOR
REMARK 3 L11: 9.1095 L22: 0.3529
REMARK 3 L33: 3.7750 L12: 1.0866
REMARK 3 L13: -4.5419 L23: -0.9585
REMARK 3 S TENSOR
REMARK 3 S11: -0.2360 S12: 0.1428 S13: -0.3859
REMARK 3 S21: -0.1360 S22: 0.0918 S23: -0.2320
REMARK 3 S31: 0.4232 S32: 0.1447 S33: 0.1441
REMARK 3
REMARK 3 TLS GROUP : 4
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 100 A 124
REMARK 3 ORIGIN FOR THE GROUP (A): 28.4799 0.2141 16.6040
REMARK 3 T TENSOR
REMARK 3 T11: 0.0449 T22: 0.0531
REMARK 3 T33: 0.0386 T12: -0.0085
REMARK 3 T13: -0.0055 T23: 0.0170
REMARK 3 L TENSOR
REMARK 3 L11: 1.8822 L22: 2.5170
REMARK 3 L33: 2.2527 L12: 0.5309
REMARK 3 L13: -0.1247 L23: 0.5860
REMARK 3 S TENSOR
REMARK 3 S11: -0.0309 S12: 0.1174 S13: -0.0446
REMARK 3 S21: -0.1138 S22: 0.0735 S23: -0.0405
REMARK 3 S31: 0.0409 S32: -0.2176 S33: -0.0425
REMARK 3
REMARK 3 TLS GROUP : 5
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 1 B 17
REMARK 3 ORIGIN FOR THE GROUP (A): 16.0988 -3.4937 29.6479
REMARK 3 T TENSOR
REMARK 3 T11: 0.0215 T22: 0.0756
REMARK 3 T33: 0.0244 T12: -0.0194
REMARK 3 T13: 0.0036 T23: -0.0159
REMARK 3 L TENSOR
REMARK 3 L11: 4.9020 L22: 1.9840
REMARK 3 L33: 5.0908 L12: 0.0224
REMARK 3 L13: 0.4451 L23: 0.5191
REMARK 3 S TENSOR
REMARK 3 S11: -0.0751 S12: 0.3302 S13: -0.0529
REMARK 3 S21: 0.0098 S22: 0.1946 S23: -0.0771
REMARK 3 S31: 0.0177 S32: 0.1842 S33: -0.1196
REMARK 3
REMARK 3 TLS GROUP : 6
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 18 B 39
REMARK 3 ORIGIN FOR THE GROUP (A): 8.8809 -0.2244 19.7025
REMARK 3 T TENSOR
REMARK 3 T11: 0.0913 T22: 0.1576
REMARK 3 T33: -0.0690 T12: -0.0828
REMARK 3 T13: -0.0287 T23: 0.0442
REMARK 3 L TENSOR
REMARK 3 L11: 7.1660 L22: 6.3901
REMARK 3 L33: 2.5041 L12: -1.6594
REMARK 3 L13: 1.2704 L23: 1.4569
REMARK 3 S TENSOR
REMARK 3 S11: -0.3056 S12: 0.7755 S13: 0.1635
REMARK 3 S21: -0.6253 S22: 0.1698 S23: 0.0946
REMARK 3 S31: -0.3298 S32: 0.1845 S33: 0.1358
REMARK 3
REMARK 3 TLS GROUP : 7
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 40 B 101
REMARK 3 ORIGIN FOR THE GROUP (A): 7.0671 1.0194 32.7640
REMARK 3 T TENSOR
REMARK 3 T11: 0.0398 T22: 0.0133
REMARK 3 T33: 0.0649 T12: -0.0133
REMARK 3 T13: -0.0137 T23: 0.0024
REMARK 3 L TENSOR
REMARK 3 L11: 1.2995 L22: 0.8021
REMARK 3 L33: 0.9996 L12: 0.2172
REMARK 3 L13: 0.5538 L23: 0.8198
REMARK 3 S TENSOR
REMARK 3 S11: -0.0897 S12: 0.1228 S13: -0.0172
REMARK 3 S21: -0.1339 S22: 0.0064 S23: 0.0989
REMARK 3 S31: -0.0777 S32: -0.0290 S33: 0.0833
REMARK 3
REMARK 3 TLS GROUP : 8
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 102 B 124
REMARK 3 ORIGIN FOR THE GROUP (A): 11.2267 -0.1423 39.4306
REMARK 3 T TENSOR
REMARK 3 T11: 0.0534 T22: 0.0219
REMARK 3 T33: 0.0564 T12: -0.0146
REMARK 3 T13: -0.0088 T23: 0.0000
REMARK 3 L TENSOR
REMARK 3 L11: 2.8182 L22: 2.2597
REMARK 3 L33: 2.2533 L12: -0.8513
REMARK 3 L13: 0.6019 L23: -0.2672
REMARK 3 S TENSOR
REMARK 3 S11: -0.0452 S12: 0.0684 S13: -0.0603
REMARK 3 S21: -0.0802 S22: -0.0101 S23: 0.1639
REMARK 3 S31: -0.0156 S32: -0.0246 S33: 0.0553
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.40
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS
REMARK 4
REMARK 4 3D7B COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 21-MAY-08.
REMARK 100 THE DEPOSITION ID IS D_1000047682.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 07-NOV-06
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 5.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SRS
REMARK 200 BEAMLINE : PX9.6
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.92
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 4
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 30196
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.600
REMARK 200 RESOLUTION RANGE LOW (A) : 30.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 96.4
REMARK 200 DATA REDUNDANCY : 3.200
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.05100
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 11.7000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.60
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.64
REMARK 200 COMPLETENESS FOR SHELL (%) : 95.9
REMARK 200 DATA REDUNDANCY IN SHELL : 3.30
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.17400
REMARK 200 <I/SIGMA(I)> FOR SHELL : 3.000
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: FOURIER SYNTHESIS
REMARK 200 SOFTWARE USED: REFMAC
REMARK 200 STARTING MODEL: PDB ENTRY: 2G8Q
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 42.75
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.15
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 4000, SODIUM CITRATE, PH 5.5,
REMARK 280 VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 298K
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 49.97950
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 16.27000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 49.97950
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 16.27000
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 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 350
REMARK 350 BIOMOLECULE: 2
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: 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 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 OG SER A 59 O HOH A 213 2.07
REMARK 500 O HOH A 217 O HOH B 386 2.17
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 HIS A 48 64.06 -102.09
REMARK 500 GLN A 60 -138.18 -98.05
REMARK 500 HIS B 48 62.89 -104.94
REMARK 500 GLN B 60 -130.80 -104.58
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 FLC A 125
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FLC A 126
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE U4S A 127
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3D6O RELATED DB: PDB
REMARK 900 RELATED ID: 3D6P RELATED DB: PDB
REMARK 900 RELATED ID: 3D6Q RELATED DB: PDB
DBREF 3D7B A 1 124 UNP P61823 RNAS1_BOVIN 27 150
DBREF 3D7B B 1 124 UNP P61823 RNAS1_BOVIN 27 150
SEQRES 1 A 124 LYS GLU THR ALA ALA ALA LYS PHE GLU ARG GLN HIS MET
SEQRES 2 A 124 ASP SER SER THR SER ALA ALA SER SER SER ASN TYR CYS
SEQRES 3 A 124 ASN GLN MET MET LYS SER ARG ASN LEU THR LYS ASP ARG
SEQRES 4 A 124 CYS LYS PRO VAL ASN THR PHE VAL HIS GLU SER LEU ALA
SEQRES 5 A 124 ASP VAL GLN ALA VAL CYS SER GLN LYS ASN VAL ALA CYS
SEQRES 6 A 124 LYS ASN GLY GLN THR ASN CYS TYR GLN SER TYR SER THR
SEQRES 7 A 124 MET SER ILE THR ASP CYS ARG GLU THR GLY SER SER LYS
SEQRES 8 A 124 TYR PRO ASN CYS ALA TYR LYS THR THR GLN ALA ASN LYS
SEQRES 9 A 124 HIS ILE ILE VAL ALA CYS GLU GLY ASN PRO TYR VAL PRO
SEQRES 10 A 124 VAL HIS PHE ASP ALA SER VAL
SEQRES 1 B 124 LYS GLU THR ALA ALA ALA LYS PHE GLU ARG GLN HIS MET
SEQRES 2 B 124 ASP SER SER THR SER ALA ALA SER SER SER ASN TYR CYS
SEQRES 3 B 124 ASN GLN MET MET LYS SER ARG ASN LEU THR LYS ASP ARG
SEQRES 4 B 124 CYS LYS PRO VAL ASN THR PHE VAL HIS GLU SER LEU ALA
SEQRES 5 B 124 ASP VAL GLN ALA VAL CYS SER GLN LYS ASN VAL ALA CYS
SEQRES 6 B 124 LYS ASN GLY GLN THR ASN CYS TYR GLN SER TYR SER THR
SEQRES 7 B 124 MET SER ILE THR ASP CYS ARG GLU THR GLY SER SER LYS
SEQRES 8 B 124 TYR PRO ASN CYS ALA TYR LYS THR THR GLN ALA ASN LYS
SEQRES 9 B 124 HIS ILE ILE VAL ALA CYS GLU GLY ASN PRO TYR VAL PRO
SEQRES 10 B 124 VAL HIS PHE ASP ALA SER VAL
HET FLC A 125 13
HET FLC A 126 13
HET U4S A 127 21
HETNAM FLC CITRATE ANION
HETNAM U4S 1-(5-DEOXY-5-PYRROLIDIN-1-YL-ALPHA-L-ARABINOFURANOSYL)
HETNAM 2 U4S PYRIMIDINE-2,4(1H,3H)-DIONE
FORMUL 3 FLC 2(C6 H5 O7 3-)
FORMUL 5 U4S C13 H19 N3 O5
FORMUL 6 HOH *346(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 B 3 MET B 13 1 11
HELIX 6 6 ASN B 24 ARG B 33 1 10
HELIX 7 7 SER B 50 VAL B 57 1 8
HELIX 8 8 CYS B 58 GLN B 60 5 3
SHEET 1 A 5 VAL A 43 VAL A 47 0
SHEET 2 A 5 MET A 79 GLU A 86 -1 O THR A 82 N PHE A 46
SHEET 3 A 5 TYR A 97 GLU A 111 -1 O THR A 100 N ASP A 83
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 THR A 82 N PHE A 46
SHEET 3 B 4 TYR A 97 GLU A 111 -1 O THR A 100 N ASP A 83
SHEET 4 B 4 VAL A 116 VAL A 124 -1 O VAL A 118 N ALA A 109
SHEET 1 C 5 VAL B 43 VAL B 47 0
SHEET 2 C 5 MET B 79 GLU B 86 -1 O CYS B 84 N ASN B 44
SHEET 3 C 5 TYR B 97 GLU B 111 -1 O THR B 100 N ASP B 83
SHEET 4 C 5 CYS B 72 GLN B 74 -1 N TYR B 73 O VAL B 108
SHEET 5 C 5 LYS B 61 VAL B 63 -1 N LYS B 61 O GLN B 74
SHEET 1 D 4 VAL B 43 VAL B 47 0
SHEET 2 D 4 MET B 79 GLU B 86 -1 O CYS B 84 N ASN B 44
SHEET 3 D 4 TYR B 97 GLU B 111 -1 O THR B 100 N ASP B 83
SHEET 4 D 4 VAL B 116 VAL B 124 -1 O VAL B 118 N ALA B 109
SSBOND 1 CYS A 26 CYS A 84 1555 1555 2.03
SSBOND 2 CYS A 40 CYS A 95 1555 1555 2.02
SSBOND 3 CYS A 58 CYS A 110 1555 1555 2.03
SSBOND 4 CYS A 65 CYS A 72 1555 1555 2.04
SSBOND 5 CYS B 26 CYS B 84 1555 1555 2.04
SSBOND 6 CYS B 40 CYS B 95 1555 1555 2.03
SSBOND 7 CYS B 58 CYS B 110 1555 1555 2.04
SSBOND 8 CYS B 65 CYS B 72 1555 1555 2.03
CISPEP 1 TYR A 92 PRO A 93 0 5.24
CISPEP 2 ASN A 113 PRO A 114 0 6.20
CISPEP 3 TYR B 92 PRO B 93 0 7.94
CISPEP 4 ASN B 113 PRO B 114 0 4.74
SITE 1 AC1 4 GLN A 11 LYS A 41 HIS A 119 LYS B 91
SITE 1 AC2 8 ARG A 10 GLN A 11 ASN A 34 LEU A 35
SITE 2 AC2 8 ASP A 38 ARG A 39 LYS A 41 LYS B 91
SITE 1 AC3 6 HIS A 12 LYS A 41 ASN A 44 THR A 45
SITE 2 AC3 6 HIS A 119 PHE A 120
CRYST1 99.959 32.540 72.439 90.00 90.62 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 0.010004 0.000000 0.000108 0.00000
SCALE2 0.000000 0.030731 0.000000 0.00000
SCALE3 0.000000 0.000000 0.013806 0.00000
(ATOM LINES ARE NOT SHOWN.)
END