HEADER HYDROLASE 22-FEB-06 2G4W
TITLE ANOMALOUS SUBSTRUCTURE OF RIBONUCLEASE A (C2)
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: CATTLE;
SOURCE 4 ORGANISM_TAXID: 9913
KEYWDS ANOMALOUS SUBSTRUCTURE OF RIBONUCLEASE A, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR C.MUELLER-DIECKMANN,M.S.WEISS
REVDAT 4 13-JUL-11 2G4W 1 VERSN
REVDAT 3 24-FEB-09 2G4W 1 VERSN
REVDAT 2 20-MAR-07 2G4W 1 JRNL
REVDAT 1 20-FEB-07 2G4W 0
JRNL AUTH C.MUELLER-DIECKMANN,S.PANJIKAR,A.SCHMIDT,S.MUELLER,J.KUPER,
JRNL AUTH 2 A.GEERLOF,M.WILMANNS,R.K.SINGH,P.A.TUCKER,M.S.WEISS
JRNL TITL ON THE ROUTINE USE OF SOFT X-RAYS IN MACROMOLECULAR
JRNL TITL 2 CRYSTALLOGRAPHY. PART IV. EFFICIENT DETERMINATION OF
JRNL TITL 3 ANOMALOUS SUBSTRUCTURES IN BIOMACROMOLECULES USING LONGER
JRNL TITL 4 X-RAY WAVELENGTHS.
JRNL REF ACTA CRYSTALLOGR.,SECT.D V. 63 366 2007
JRNL REFN ISSN 0907-4449
JRNL PMID 17327674
JRNL DOI 10.1107/S0907444906055624
REMARK 2
REMARK 2 RESOLUTION. 1.84 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.2.0005
REMARK 3 AUTHORS : MURSHUDOV,VAGIN,DODSON
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.84
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 30.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.4
REMARK 3 NUMBER OF REFLECTIONS : 19941
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) : 0.214
REMARK 3 R VALUE (WORKING SET) : 0.213
REMARK 3 FREE R VALUE : 0.274
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 2.000
REMARK 3 FREE R VALUE TEST SET COUNT : 408
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) : 1.84
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.89
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1404
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 95.81
REMARK 3 BIN R VALUE (WORKING SET) : 0.3120
REMARK 3 BIN FREE R VALUE SET COUNT : 35
REMARK 3 BIN FREE R VALUE : 0.4460
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 : 6
REMARK 3 SOLVENT ATOMS : 87
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) : 28.03
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.01000
REMARK 3 B22 (A**2) : -0.47000
REMARK 3 B33 (A**2) : 0.48000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : -0.10000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.162
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.162
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.119
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 7.531
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.942
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.903
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 1946 ; 0.027 ; 0.021
REMARK 3 BOND LENGTHS OTHERS (A): 1612 ; 0.001 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 2634 ; 2.314 ; 1.927
REMARK 3 BOND ANGLES OTHERS (DEGREES): 3808 ; 1.044 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 246 ; 7.168 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 88 ;34.414 ;25.227
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 336 ;16.237 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 8 ;16.916 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 290 ; 0.136 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 2180 ; 0.012 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 364 ; 0.001 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 402 ; 0.231 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): 1640 ; 0.201 ; 0.200
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 940 ; 0.192 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): 1142 ; 0.097 ; 0.200
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 96 ; 0.163 ; 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): 20 ; 0.234 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): 55 ; 0.308 ; 0.200
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 17 ; 0.625 ; 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): 1549 ; 1.801 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 498 ; 0.463 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 2008 ; 2.275 ; 2.500
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 804 ; 5.021 ; 5.000
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 626 ; 6.663 ;10.000
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): 31.2729 0.6134 9.9420
REMARK 3 T TENSOR
REMARK 3 T11: -0.0361 T22: -0.0369
REMARK 3 T33: -0.0949 T12: 0.0186
REMARK 3 T13: 0.0414 T23: 0.0262
REMARK 3 L TENSOR
REMARK 3 L11: 3.0755 L22: 2.3655
REMARK 3 L33: 5.0606 L12: -0.5976
REMARK 3 L13: -0.8181 L23: 0.6204
REMARK 3 S TENSOR
REMARK 3 S11: 0.2052 S12: 0.7177 S13: 0.0962
REMARK 3 S21: -0.5124 S22: 0.0204 S23: -0.3331
REMARK 3 S31: -0.1955 S32: -0.3238 S33: -0.2256
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): 9.4495 -0.1000 31.2520
REMARK 3 T TENSOR
REMARK 3 T11: -0.0869 T22: -0.1075
REMARK 3 T33: -0.0544 T12: -0.0060
REMARK 3 T13: -0.0257 T23: 0.0149
REMARK 3 L TENSOR
REMARK 3 L11: 2.7467 L22: 1.6665
REMARK 3 L33: 3.5679 L12: -0.2584
REMARK 3 L13: 0.8341 L23: 1.2379
REMARK 3 S TENSOR
REMARK 3 S11: -0.0046 S12: 0.4271 S13: 0.0821
REMARK 3 S21: -0.2993 S22: -0.0817 S23: 0.0955
REMARK 3 S31: -0.0808 S32: -0.1259 S33: 0.0863
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : BABINET MODEL WITH 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 2G4W COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 22-MAR-06.
REMARK 100 THE RCSB ID CODE IS RCSB036691.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 01-JAN-05
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : EMBL/DESY, HAMBURG
REMARK 200 BEAMLINE : X12
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 2.00
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : CCP4 (SCALA)
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 20349
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.840
REMARK 200 RESOLUTION RANGE LOW (A) : 30.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : NULL
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL
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 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: FOURIER SYNTHESIS
REMARK 200 SOFTWARE USED: FFT
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 42.95
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.16
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL
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 50.06000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 16.30000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 50.06000
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 16.30000
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 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
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 O HOH A 161 O HOH B 169 4546 0.93
REMARK 500 O HOH A 163 O HOH B 173 4546 1.07
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 ARG B 85 CD ARG B 85 NE -0.106
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 B 39 NE - CZ - NH1 ANGL. DEV. = 3.2 DEGREES
REMARK 500 ASP B 83 CB - CG - OD1 ANGL. DEV. = -5.5 DEGREES
REMARK 500 ASP B 83 CB - CG - OD2 ANGL. DEV. = 5.4 DEGREES
REMARK 500 ARG B 85 CG - CD - NE ANGL. DEV. = -17.8 DEGREES
REMARK 500 ARG B 85 NE - CZ - NH1 ANGL. DEV. = 7.3 DEGREES
REMARK 500 ARG B 85 NE - CZ - NH2 ANGL. DEV. = -11.9 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 GLU A 2 129.35 148.08
REMARK 500 ALA A 20 109.07 -52.66
REMARK 500 SER A 21 -167.33 -66.23
REMARK 500 SER A 22 -177.67 -8.07
REMARK 500 HIS A 48 69.13 -102.47
REMARK 500 GLN A 60 -138.97 -102.24
REMARK 500 SER B 21 -77.96 -112.56
REMARK 500 GLN B 60 -126.76 -100.31
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 CL B 125
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2G4H RELATED DB: PDB
REMARK 900 RELATED ID: 2G4I RELATED DB: PDB
REMARK 900 RELATED ID: 2G4J RELATED DB: PDB
REMARK 900 RELATED ID: 2G4K RELATED DB: PDB
REMARK 900 RELATED ID: 2G4L RELATED DB: PDB
REMARK 900 RELATED ID: 2G4M RELATED DB: PDB
REMARK 900 RELATED ID: 2G4N RELATED DB: PDB
REMARK 900 RELATED ID: 2G4O RELATED DB: PDB
REMARK 900 RELATED ID: 2G4P RELATED DB: PDB
REMARK 900 RELATED ID: 2G4Q RELATED DB: PDB
REMARK 900 RELATED ID: 2G4R RELATED DB: PDB
REMARK 900 RELATED ID: 2G4S RELATED DB: PDB
REMARK 900 RELATED ID: 2G4T RELATED DB: PDB
REMARK 900 RELATED ID: 2G4U RELATED DB: PDB
REMARK 900 RELATED ID: 2G4V RELATED DB: PDB
REMARK 900 RELATED ID: 2G4X RELATED DB: PDB
REMARK 900 RELATED ID: 2G4Y RELATED DB: PDB
REMARK 900 RELATED ID: 2G4Z RELATED DB: PDB
REMARK 900 RELATED ID: 2G51 RELATED DB: PDB
REMARK 900 RELATED ID: 2G52 RELATED DB: PDB
REMARK 900 RELATED ID: 2G55 RELATED DB: PDB
DBREF 2G4W A 1 124 UNP P61823 RNAS1_BOVIN 27 150
DBREF 2G4W 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 SO4 A 125 5
HET CL B 125 1
HETNAM SO4 SULFATE ION
HETNAM CL CHLORIDE ION
FORMUL 3 SO4 O4 S 2-
FORMUL 4 CL CL 1-
FORMUL 5 HOH *87(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 ALA A 56 1 7
HELIX 4 4 VAL A 57 GLN A 60 5 4
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 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 B 43 VAL B 47 0
SHEET 2 C 5 MET B 79 GLU B 86 -1 O THR B 82 N PHE B 46
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 VAL B 63 O CYS B 72
SHEET 1 D 4 VAL B 43 VAL B 47 0
SHEET 2 D 4 MET B 79 GLU B 86 -1 O THR B 82 N PHE B 46
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 2.07
SSBOND 2 CYS A 40 CYS A 95 1555 1555 2.04
SSBOND 3 CYS A 58 CYS A 110 1555 1555 2.02
SSBOND 4 CYS A 65 CYS A 72 1555 1555 2.08
SSBOND 5 CYS B 26 CYS B 84 1555 1555 2.06
SSBOND 6 CYS B 40 CYS B 95 1555 1555 2.05
SSBOND 7 CYS B 58 CYS B 110 1555 1555 2.00
SSBOND 8 CYS B 65 CYS B 72 1555 1555 1.97
CISPEP 1 TYR A 92 PRO A 93 0 5.15
CISPEP 2 ASN A 113 PRO A 114 0 10.72
CISPEP 3 TYR B 92 PRO B 93 0 9.85
CISPEP 4 ASN B 113 PRO B 114 0 10.71
SITE 1 AC1 7 GLN A 11 HIS A 12 LYS A 41 VAL A 118
SITE 2 AC1 7 HIS A 119 PHE A 120 HOH A 154
SITE 1 AC2 4 HIS B 12 HIS B 119 PHE B 120 HOH B 137
CRYST1 100.120 32.600 72.470 90.00 90.56 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 0.009988 0.000000 0.000098 0.00000
SCALE2 0.000000 0.030675 0.000000 0.00000
SCALE3 0.000000 0.000000 0.013799 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
