HEADER HYDROLASE 02-FEB-11 3QL2
TITLE CRYSTAL STRUCTURE OF RIBONUCLEASE A VARIANT A4C/D83E/V118C
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;
COMPND 6 ENGINEERED: YES;
COMPND 7 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: BOS TAURUS;
SOURCE 3 ORGANISM_COMMON: BOVINE;
SOURCE 4 ORGANISM_TAXID: 9913;
SOURCE 5 GENE: RNASE1, RNS1;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS RIBONUCLEASE A, DISULFIDE BOND, SALT BRIDGE, STABILITY, FOLDING,
KEYWDS 2 PROTEOLYSIS, SITE-DIRECTED MUTAGENESIS, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR U.ARNOLD,M.SCHOEPFEL
REVDAT 4 01-NOV-23 3QL2 1 REMARK SEQADV
REVDAT 3 07-MAY-14 3QL2 1 JRNL
REVDAT 2 13-JUN-12 3QL2 1 JRNL
REVDAT 1 29-FEB-12 3QL2 0
JRNL AUTH U.ARNOLD,M.SCHOPFEL
JRNL TITL SIGNIFICANT STABILIZATION OF RIBONUCLEASE A BY ADDITIVE
JRNL TITL 2 EFFECTS
JRNL REF FEBS J. V. 279 2508 2012
JRNL REFN ISSN 1742-464X
JRNL PMID 22594773
JRNL DOI 10.1111/J.1742-4658.2012.08632.X
REMARK 2
REMARK 2 RESOLUTION. 1.49 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC
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) : 1.49
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 31.01
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 3 NUMBER OF REFLECTIONS : 34661
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) : 0.169
REMARK 3 R VALUE (WORKING SET) : 0.167
REMARK 3 FREE R VALUE : 0.209
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 1825
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) : 1.49
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.53
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1790
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 100.0
REMARK 3 BIN R VALUE (WORKING SET) : 0.2490
REMARK 3 BIN FREE R VALUE SET COUNT : 95
REMARK 3 BIN FREE R VALUE : 0.3050
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 1904
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 10
REMARK 3 SOLVENT ATOMS : 249
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 22.69
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 19.55
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.28000
REMARK 3 B22 (A**2) : 0.99000
REMARK 3 B33 (A**2) : -1.35000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : -0.72000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.074
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.080
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.053
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 3.166
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.965
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.946
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 1995 ; 0.025 ; 0.021
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 2715 ; 2.244 ; 1.935
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 264 ; 6.639 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 88 ;38.360 ;25.227
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 349 ;11.500 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 8 ;14.671 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 298 ; 0.148 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 1502 ; 0.015 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL
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): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL
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): 1269 ; 1.293 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 2063 ; 2.027 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 726 ; 3.284 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 643 ; 5.229 ; 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 : 2
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 124
REMARK 3 ORIGIN FOR THE GROUP (A): 10.6660 12.4890 4.1750
REMARK 3 T TENSOR
REMARK 3 T11: 0.0611 T22: 0.0344
REMARK 3 T33: 0.1959 T12: -0.0015
REMARK 3 T13: 0.0286 T23: -0.0026
REMARK 3 L TENSOR
REMARK 3 L11: 1.7033 L22: 0.6097
REMARK 3 L33: 2.3346 L12: 0.0403
REMARK 3 L13: -0.1081 L23: 0.3525
REMARK 3 S TENSOR
REMARK 3 S11: 0.0401 S12: -0.2010 S13: -0.0013
REMARK 3 S21: 0.0870 S22: -0.0064 S23: 0.0390
REMARK 3 S31: 0.0491 S32: 0.0474 S33: -0.0337
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 : B 1 B 124
REMARK 3 ORIGIN FOR THE GROUP (A): 30.9000 9.7490 26.7080
REMARK 3 T TENSOR
REMARK 3 T11: 0.0167 T22: 0.0771
REMARK 3 T33: 0.1627 T12: -0.0032
REMARK 3 T13: 0.0359 T23: -0.0136
REMARK 3 L TENSOR
REMARK 3 L11: 1.6956 L22: 0.5209
REMARK 3 L33: 1.6151 L12: 0.0584
REMARK 3 L13: 0.2431 L23: 0.1927
REMARK 3 S TENSOR
REMARK 3 S11: 0.0173 S12: -0.3098 S13: 0.0873
REMARK 3 S21: -0.0337 S22: 0.0203 S23: -0.0558
REMARK 3 S31: 0.0653 S32: -0.0826 S33: -0.0376
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 3QL2 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 18-FEB-11.
REMARK 100 THE DEPOSITION ID IS D_1000063779.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 08-OCT-10
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 4.8
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : BESSY
REMARK 200 BEAMLINE : 14.1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.91841
REMARK 200 MONOCHROMATOR : SI 111 CHANNEL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 225 MM CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 36486
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.490
REMARK 200 RESOLUTION RANGE LOW (A) : 35.080
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 94.4
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : 0.04000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 15.2300
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.49
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.53
REMARK 200 COMPLETENESS FOR SHELL (%) : 66.4
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.50200
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.890
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER 2.1.4
REMARK 200 STARTING MODEL: 7RSA
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 42.56
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.14
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M SODIUM ACETATE, 0.2M AMMONIUM
REMARK 280 SULFATE, 25% (W/V) PEG 4000, 10MM CALCIUM CHLORIDE, PH 4.8,
REMARK 280 VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K
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 51.44400
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 15.34700
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 51.44400
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 15.34700
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 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 480
REMARK 480 ZERO OCCUPANCY ATOM
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 480 M RES C SSEQI ATOMS
REMARK 480 LYS B 1 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 O HOH A 358 O HOH A 380 2.14
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
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 RES CSSEQI ATM2 DEVIATION
REMARK 500 SER A 59 CB SER A 59 OG 0.081
REMARK 500 TYR B 73 CZ TYR B 73 CE2 -0.091
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 ARG A 85 NE - CZ - NH2 ANGL. DEV. = -3.0 DEGREES
REMARK 500 ASP B 53 CB - CG - OD2 ANGL. DEV. = -6.9 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 ASN A 34 30.82 71.27
REMARK 500 HIS A 48 71.47 -105.68
REMARK 500 GLN A 60 -134.44 -104.69
REMARK 500 ASN A 94 71.05 -105.39
REMARK 500 GLN B 60 -131.61 -107.07
REMARK 500 ASN B 94 66.73 -114.23
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 125
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 125
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3QL1 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF RIBONUCLEASE A VARIANT A4C/D83E/V118C
DBREF 3QL2 A 1 124 UNP P61823 RNAS1_BOVIN 27 150
DBREF 3QL2 B 1 124 UNP P61823 RNAS1_BOVIN 27 150
SEQADV 3QL2 CYS A 4 UNP P61823 ALA 30 ENGINEERED MUTATION
SEQADV 3QL2 GLU A 83 UNP P61823 ASP 109 ENGINEERED MUTATION
SEQADV 3QL2 CYS A 118 UNP P61823 VAL 144 ENGINEERED MUTATION
SEQADV 3QL2 CYS B 4 UNP P61823 ALA 30 ENGINEERED MUTATION
SEQADV 3QL2 GLU B 83 UNP P61823 ASP 109 ENGINEERED MUTATION
SEQADV 3QL2 CYS B 118 UNP P61823 VAL 144 ENGINEERED MUTATION
SEQRES 1 A 124 LYS GLU THR CYS 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 GLU 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 CYS HIS PHE ASP ALA SER VAL
SEQRES 1 B 124 LYS GLU THR CYS 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 GLU 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 CYS HIS PHE ASP ALA SER VAL
HET SO4 A 125 10
HET SO4 B 125 5
HETNAM SO4 SULFATE ION
FORMUL 3 SO4 2(O4 S 2-)
FORMUL 5 HOH *249(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 ALA B 56 1 7
HELIX 8 8 VAL B 57 GLN B 60 5 4
SHEET 1 A 3 VAL A 43 VAL A 47 0
SHEET 2 A 3 MET A 79 GLU A 86 -1 O THR A 82 N PHE A 46
SHEET 3 A 3 TYR A 97 LYS A 104 -1 O THR A 100 N GLU A 83
SHEET 1 B 4 LYS A 61 VAL A 63 0
SHEET 2 B 4 CYS A 72 GLN A 74 -1 O GLN A 74 N LYS A 61
SHEET 3 B 4 ILE A 106 GLU A 111 -1 O VAL A 108 N TYR A 73
SHEET 4 B 4 VAL A 116 SER A 123 -1 O CYS A 118 N ALA A 109
SHEET 1 C 3 VAL B 43 VAL B 47 0
SHEET 2 C 3 MET B 79 GLU B 86 -1 O CYS B 84 N ASN B 44
SHEET 3 C 3 TYR B 97 LYS B 104 -1 O LYS B 98 N ARG B 85
SHEET 1 D 4 LYS B 61 VAL B 63 0
SHEET 2 D 4 CYS B 72 GLN B 74 -1 O GLN B 74 N LYS B 61
SHEET 3 D 4 ILE B 106 GLU B 111 -1 O VAL B 108 N TYR B 73
SHEET 4 D 4 VAL B 116 SER B 123 -1 O CYS B 118 N ALA B 109
SSBOND 1 CYS A 4 CYS A 118 1555 1555 2.04
SSBOND 2 CYS A 26 CYS A 84 1555 1555 2.10
SSBOND 3 CYS A 40 CYS A 95 1555 1555 2.03
SSBOND 4 CYS A 58 CYS A 110 1555 1555 2.07
SSBOND 5 CYS A 65 CYS A 72 1555 1555 2.07
SSBOND 6 CYS B 4 CYS B 118 1555 1555 2.09
SSBOND 7 CYS B 26 CYS B 84 1555 1555 2.08
SSBOND 8 CYS B 40 CYS B 95 1555 1555 2.05
SSBOND 9 CYS B 58 CYS B 110 1555 1555 2.07
SSBOND 10 CYS B 65 CYS B 72 1555 1555 2.04
CISPEP 1 TYR A 92 PRO A 93 0 3.38
CISPEP 2 ASN A 113 PRO A 114 0 3.98
CISPEP 3 TYR B 92 PRO B 93 0 6.88
CISPEP 4 ASN B 113 PRO B 114 0 3.91
SITE 1 AC1 9 GLN A 11 HIS A 12 LYS A 41 CYS A 118
SITE 2 AC1 9 HIS A 119 PHE A 120 HOH A 138 HOH A 191
SITE 3 AC1 9 HOH A 208
SITE 1 AC2 8 GLN B 11 HIS B 12 LYS B 41 HIS B 119
SITE 2 AC2 8 PHE B 120 HOH B 133 HOH B 211 HOH B 223
CRYST1 102.888 30.694 74.752 90.00 93.15 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 0.009719 0.000000 0.000535 0.00000
SCALE2 0.000000 0.032580 0.000000 0.00000
SCALE3 0.000000 0.000000 0.013398 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
