HEADER HYDROLASE/DNA 17-MAY-00 1F0V
TITLE CRYSTAL STRUCTURE OF AN RNASE A DIMER DISPLAYING A NEW TYPE OF 3D
TITLE 2 DOMAIN SWAPPING
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: 5'-D(*CP*G)-3';
COMPND 3 CHAIN: M, N, O, P;
COMPND 4 ENGINEERED: YES;
COMPND 5 MOL_ID: 2;
COMPND 6 MOLECULE: RIBONUCLEASE A;
COMPND 7 CHAIN: A, B, C, D;
COMPND 8 SYNONYM: RNASE 1, RNASE A;
COMPND 9 EC: 3.1.27.5
SOURCE MOL_ID: 1;
SOURCE 2 SYNTHETIC: YES;
SOURCE 3 MOL_ID: 2;
SOURCE 4 ORGANISM_SCIENTIFIC: BOS TAURUS;
SOURCE 5 ORGANISM_COMMON: CATTLE;
SOURCE 6 ORGANISM_TAXID: 9913;
SOURCE 7 ORGAN: PANCREAS
KEYWDS DOMAIN SWAPPING, CRYSTAL, RIBONUCLEASE, BOVINE PANCREAS, HYDROLASE-
KEYWDS 2 DNA COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR Y.S.LIU,G.GOTTE,M.LIBONATI,D.S.EISENBERG
REVDAT 6 13-JUL-11 1F0V 1 VERSN
REVDAT 5 24-FEB-09 1F0V 1 VERSN
REVDAT 4 01-AUG-06 1F0V 1 REMARK AUTHOR COMPND
REVDAT 3 01-APR-03 1F0V 1 JRNL
REVDAT 2 14-MAR-01 1F0V 1 REMARK
REVDAT 1 21-FEB-01 1F0V 0
JRNL AUTH Y.S.LIU,G.GOTTE,M.LIBONATI,D.S.EISENBERG
JRNL TITL A DOMAIN-SWAPPED RNASE A DIMER WITH IMPLICATIONS FOR AMYLOID
JRNL TITL 2 FORMATION
JRNL REF NAT.STRUCT.BIOL. V. 8 211 2001
JRNL REFN ISSN 1072-8368
JRNL PMID 11224563
JRNL DOI 10.1038/84941
REMARK 2
REMARK 2 RESOLUTION. 1.70 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS
REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-
REMARK 3 : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,
REMARK 3 : READ,RICE,SIMONSON,WARREN
REMARK 3
REMARK 3 REFINEMENT TARGET : ENGH & HUBER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.70
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 10.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 90.0
REMARK 3 NUMBER OF REFLECTIONS : 68191
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 SET) : 0.184
REMARK 3 FREE R VALUE : 0.213
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 11.200
REMARK 3 FREE R VALUE TEST SET COUNT : 7651
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : NULL
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : NULL
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : NULL
REMARK 3 BIN RESOLUTION RANGE LOW (A) : NULL
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : NULL
REMARK 3 BIN FREE R VALUE : NULL
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 BIN FREE R VALUE TEST SET COUNT : NULL
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 3804
REMARK 3 NUCLEIC ACID ATOMS : 152
REMARK 3 HETEROGEN ATOMS : 164
REMARK 3 SOLVENT ATOMS : 554
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 20.00
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
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 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM SIGMAA (A) : NULL
REMARK 3 LOW RESOLUTION CUTOFF (A) : NULL
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM C-V SIGMAA (A) : NULL
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.019
REMARK 3 BOND ANGLES (DEGREES) : 2.07
REMARK 3 DIHEDRAL ANGLES (DEGREES) : NULL
REMARK 3 IMPROPER ANGLES (DEGREES) : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : NULL
REMARK 3 KSOL : NULL
REMARK 3 BSOL : NULL
REMARK 3
REMARK 3 NCS MODEL : NULL
REMARK 3
REMARK 3 NCS RESTRAINTS. RMS SIGMA/WEIGHT
REMARK 3 GROUP 1 POSITIONAL (A) : NULL ; NULL
REMARK 3 GROUP 1 B-FACTOR (A**2) : NULL ; NULL
REMARK 3
REMARK 3 PARAMETER FILE 1 : NULL
REMARK 3 TOPOLOGY FILE 1 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1F0V COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 19-MAY-00.
REMARK 100 THE RCSB ID CODE IS RCSB011107.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : NULL
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : NSLS
REMARK 200 BEAMLINE : X12B
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.072
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : AREA DETECTOR
REMARK 200 DETECTOR MANUFACTURER : NULL
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 76047
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.700
REMARK 200 RESOLUTION RANGE LOW (A) : 100.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 95.0
REMARK 200 DATA REDUNDANCY : 10.000
REMARK 200 R MERGE (I) : 0.05200
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 14.0000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.70
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.76
REMARK 200 COMPLETENESS FOR SHELL (%) : 95.0
REMARK 200 DATA REDUNDANCY IN SHELL : 3.00
REMARK 200 R MERGE FOR SHELL (I) : 0.08000
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: NULL
REMARK 200 SOFTWARE USED: AMORE
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 61.96
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.23
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M PHOSPHATE BUFFER, 16 % PEG 4000,
REMARK 280 2 % DIOXANE, PH 6.5, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE
REMARK 280 293K
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 48.17050
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, 3, 4
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: DIMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: M, 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: DIMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: N, 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 350
REMARK 350 BIOMOLECULE: 3
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: O, C
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: 4
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: P, D
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 SER D 690 O3 GOL C 919 2555 1.96
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 - NH1 ANGL. DEV. = 3.8 DEGREES
REMARK 500 ARG A 85 NE - CZ - NH2 ANGL. DEV. = -3.1 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 HIS A 48 65.48 -100.16
REMARK 500 GLN A 60 -132.50 -108.22
REMARK 500 SER B 222 137.41 170.84
REMARK 500 HIS B 248 65.25 -104.29
REMARK 500 GLN B 260 -133.80 -103.37
REMARK 500 ASN B 271 36.08 -96.82
REMARK 500 ASN B 294 76.91 -114.83
REMARK 500 HIS C 448 63.86 -103.64
REMARK 500 GLN C 460 -133.77 -103.06
REMARK 500 ASN C 494 72.93 -104.18
REMARK 500 ASP D 614 72.19 -150.96
REMARK 500 HIS D 648 68.07 -106.57
REMARK 500 GLN D 660 -130.33 -103.67
REMARK 500 ASN D 671 35.67 -95.78
REMARK 500 LYS D 691 110.05 -165.16
REMARK 500 ASN D 694 69.21 -105.73
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH A1537 DISTANCE = 6.32 ANGSTROMS
REMARK 525 HOH A1538 DISTANCE = 5.67 ANGSTROMS
REMARK 525 HOH A1574 DISTANCE = 5.81 ANGSTROMS
REMARK 525 HOH B1536 DISTANCE = 5.63 ANGSTROMS
REMARK 525 HOH D1585 DISTANCE = 5.73 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 A 801
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 B 802
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 C 803
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 P 804
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL D 901
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 902
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL C 903
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 904
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 905
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 906
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 907
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 908
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL D 909
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 910
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 911
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL C 912
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL D 913
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 914
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 915
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL D 916
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL C 917
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 918
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL C 919
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 920
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 921
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 922
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 923
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL D 924
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1A2W RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF A 3D DOMAIN-SWAPPED DIMER OF RNASE A
REMARK 900 AT 2.1 A RESOLUTION
DBREF 1F0V A 1 124 UNP P61823 RNAS1_BOVIN 27 150
DBREF 1F0V B 201 324 UNP P61823 RNAS1_BOVIN 27 150
DBREF 1F0V C 401 524 UNP P61823 RNAS1_BOVIN 27 150
DBREF 1F0V D 601 724 UNP P61823 RNAS1_BOVIN 27 150
DBREF 1F0V M 751 752 PDB 1F0V 1F0V 751 752
DBREF 1F0V N 753 754 PDB 1F0V 1F0V 753 754
DBREF 1F0V O 755 756 PDB 1F0V 1F0V 755 756
DBREF 1F0V P 757 758 PDB 1F0V 1F0V 757 758
SEQRES 1 M 2 DC DG
SEQRES 1 N 2 DC DG
SEQRES 1 O 2 DC DG
SEQRES 1 P 2 DC DG
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
SEQRES 1 C 124 LYS GLU THR ALA ALA ALA LYS PHE GLU ARG GLN HIS MET
SEQRES 2 C 124 ASP SER SER THR SER ALA ALA SER SER SER ASN TYR CYS
SEQRES 3 C 124 ASN GLN MET MET LYS SER ARG ASN LEU THR LYS ASP ARG
SEQRES 4 C 124 CYS LYS PRO VAL ASN THR PHE VAL HIS GLU SER LEU ALA
SEQRES 5 C 124 ASP VAL GLN ALA VAL CYS SER GLN LYS ASN VAL ALA CYS
SEQRES 6 C 124 LYS ASN GLY GLN THR ASN CYS TYR GLN SER TYR SER THR
SEQRES 7 C 124 MET SER ILE THR ASP CYS ARG GLU THR GLY SER SER LYS
SEQRES 8 C 124 TYR PRO ASN CYS ALA TYR LYS THR THR GLN ALA ASN LYS
SEQRES 9 C 124 HIS ILE ILE VAL ALA CYS GLU GLY ASN PRO TYR VAL PRO
SEQRES 10 C 124 VAL HIS PHE ASP ALA SER VAL
SEQRES 1 D 124 LYS GLU THR ALA ALA ALA LYS PHE GLU ARG GLN HIS MET
SEQRES 2 D 124 ASP SER SER THR SER ALA ALA SER SER SER ASN TYR CYS
SEQRES 3 D 124 ASN GLN MET MET LYS SER ARG ASN LEU THR LYS ASP ARG
SEQRES 4 D 124 CYS LYS PRO VAL ASN THR PHE VAL HIS GLU SER LEU ALA
SEQRES 5 D 124 ASP VAL GLN ALA VAL CYS SER GLN LYS ASN VAL ALA CYS
SEQRES 6 D 124 LYS ASN GLY GLN THR ASN CYS TYR GLN SER TYR SER THR
SEQRES 7 D 124 MET SER ILE THR ASP CYS ARG GLU THR GLY SER SER LYS
SEQRES 8 D 124 TYR PRO ASN CYS ALA TYR LYS THR THR GLN ALA ASN LYS
SEQRES 9 D 124 HIS ILE ILE VAL ALA CYS GLU GLY ASN PRO TYR VAL PRO
SEQRES 10 D 124 VAL HIS PHE ASP ALA SER VAL
HET PO4 A 801 5
HET PO4 B 802 5
HET PO4 C 803 5
HET PO4 P 804 5
HET GOL D 901 6
HET GOL B 902 6
HET GOL C 903 6
HET GOL A 904 6
HET GOL B 905 6
HET GOL B 906 6
HET GOL B 907 6
HET GOL A 908 6
HET GOL D 909 6
HET GOL B 910 6
HET GOL A 911 6
HET GOL C 912 6
HET GOL D 913 6
HET GOL B 914 6
HET GOL A 915 6
HET GOL D 916 6
HET GOL C 917 6
HET GOL A 918 6
HET GOL C 919 6
HET GOL B 920 6
HET GOL B 921 6
HET GOL B 922 6
HET GOL A 923 6
HET GOL D 924 6
HETNAM PO4 PHOSPHATE ION
HETNAM GOL GLYCEROL
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 9 PO4 4(O4 P 3-)
FORMUL 13 GOL 24(C3 H8 O3)
FORMUL 37 HOH *554(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 203 MET B 213 1 11
HELIX 6 6 ASN B 224 ARG B 233 1 10
HELIX 7 7 SER B 250 VAL B 257 1 8
HELIX 8 8 CYS B 258 GLN B 260 5 3
HELIX 9 9 THR C 403 MET C 413 1 11
HELIX 10 10 ASN C 424 ARG C 433 1 10
HELIX 11 11 SER C 450 VAL C 457 1 8
HELIX 12 12 CYS C 458 GLN C 460 5 3
HELIX 13 13 THR D 603 MET D 613 1 11
HELIX 14 14 ASN D 624 ARG D 633 1 10
HELIX 15 15 SER D 650 ALA D 656 1 7
HELIX 16 16 VAL D 657 GLN D 660 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 N LYS A 98 O ARG A 85
SHEET 1 B 6 LYS A 61 VAL A 63 0
SHEET 2 B 6 CYS A 72 GLN A 74 -1 O CYS A 72 N VAL A 63
SHEET 3 B 6 ILE A 106 VAL A 124 -1 O VAL A 108 N TYR A 73
SHEET 4 B 6 TYR B 297 SER B 323 -1 N HIS B 305 O VAL A 124
SHEET 5 B 6 CYS B 272 GLN B 274 -1 N TYR B 273 O VAL B 308
SHEET 6 B 6 LYS B 261 VAL B 263 -1 O LYS B 261 N GLN B 274
SHEET 1 C 6 LYS A 61 VAL A 63 0
SHEET 2 C 6 CYS A 72 GLN A 74 -1 O CYS A 72 N VAL A 63
SHEET 3 C 6 ILE A 106 VAL A 124 -1 O VAL A 108 N TYR A 73
SHEET 4 C 6 TYR B 297 SER B 323 -1 N HIS B 305 O VAL A 124
SHEET 5 C 6 MET B 279 GLU B 286 -1 N MET B 279 O LYS B 304
SHEET 6 C 6 VAL B 243 VAL B 247 -1 O ASN B 244 N CYS B 284
SHEET 1 D 6 LYS D 661 VAL D 663 0
SHEET 2 D 6 CYS D 672 GLN D 674 -1 O CYS D 672 N VAL D 663
SHEET 3 D 6 ILE D 706 VAL D 724 -1 N VAL D 708 O TYR D 673
SHEET 4 D 6 TYR C 497 SER C 523 -1 N HIS C 505 O VAL D 724
SHEET 5 D 6 CYS C 472 GLN C 474 -1 N TYR C 473 O VAL C 508
SHEET 6 D 6 LYS C 461 VAL C 463 -1 O LYS C 461 N GLN C 474
SHEET 1 E 6 LYS D 661 VAL D 663 0
SHEET 2 E 6 CYS D 672 GLN D 674 -1 O CYS D 672 N VAL D 663
SHEET 3 E 6 ILE D 706 VAL D 724 -1 N VAL D 708 O TYR D 673
SHEET 4 E 6 TYR C 497 SER C 523 -1 N HIS C 505 O VAL D 724
SHEET 5 E 6 MET C 479 GLU C 486 -1 N MET C 479 O LYS C 504
SHEET 6 E 6 VAL C 443 VAL C 447 -1 N ASN C 444 O CYS C 484
SHEET 1 F 3 VAL D 643 VAL D 647 0
SHEET 2 F 3 MET D 679 GLU D 686 -1 N THR D 682 O PHE D 646
SHEET 3 F 3 TYR D 697 LYS D 704 -1 N LYS D 698 O ARG D 685
SSBOND 1 CYS A 26 CYS A 84 1555 1555 2.08
SSBOND 2 CYS A 40 CYS A 95 1555 1555 2.06
SSBOND 3 CYS A 58 CYS A 110 1555 1555 2.09
SSBOND 4 CYS A 65 CYS A 72 1555 1555 2.08
SSBOND 5 CYS B 226 CYS B 284 1555 1555 2.08
SSBOND 6 CYS B 240 CYS B 295 1555 1555 2.04
SSBOND 7 CYS B 258 CYS B 310 1555 1555 2.12
SSBOND 8 CYS B 265 CYS B 272 1555 1555 2.11
SSBOND 9 CYS C 426 CYS C 484 1555 1555 2.09
SSBOND 10 CYS C 440 CYS C 495 1555 1555 2.06
SSBOND 11 CYS C 458 CYS C 510 1555 1555 2.08
SSBOND 12 CYS C 465 CYS C 472 1555 1555 2.08
SSBOND 13 CYS D 626 CYS D 684 1555 1555 2.06
SSBOND 14 CYS D 640 CYS D 695 1555 1555 2.02
SSBOND 15 CYS D 658 CYS D 710 1555 1555 2.10
SSBOND 16 CYS D 665 CYS D 672 1555 1555 2.09
CISPEP 1 TYR A 92 PRO A 93 0 0.69
CISPEP 2 TYR B 292 PRO B 293 0 1.06
CISPEP 3 TYR C 492 PRO C 493 0 0.01
CISPEP 4 TYR D 692 PRO D 693 0 -0.53
SITE 1 AC1 9 GLN A 11 HIS A 12 LYS A 41 HOH A1004
SITE 2 AC1 9 HOH A1252 HOH A1553 HIS B 319 PHE B 320
SITE 3 AC1 9 DG M 752
SITE 1 AC2 10 HIS A 119 PHE A 120 GLN B 211 HIS B 212
SITE 2 AC2 10 LYS B 241 HOH B1074 HOH B1396 HOH B1554
SITE 3 AC2 10 HOH B1555 DG N 754
SITE 1 AC3 8 GLN C 411 HIS C 412 LYS C 441 HOH C1045
SITE 2 AC3 8 HOH C1571 HIS D 719 PHE D 720 DG O 756
SITE 1 AC4 8 HIS C 519 PHE C 520 GLN D 611 HIS D 612
SITE 2 AC4 8 LYS D 641 DG P 758 HOH P1029 HOH P1273
SITE 1 AC5 9 ALA C 405 GLU C 511 ASN D 713 PRO D 714
SITE 2 AC5 9 HOH D1051 HOH D1254 HOH D1355 HOH D1575
SITE 3 AC5 9 HOH D1576
SITE 1 AC6 4 GLN B 301 ALA B 302 ASN B 303 HOH B1442
SITE 1 AC7 2 PRO C 442 HOH C1179
SITE 1 AC8 2 GLN A 69 THR A 70
SITE 1 AC9 7 GLU B 202 ALA B 206 GLU B 209 ARG B 210
SITE 2 AC9 7 GOL B 922 HOH B1307 HOH B1514
SITE 1 BC1 4 SER B 223 THR B 299 THR B 300 GLN B 301
SITE 1 BC2 6 VAL A 124 VAL B 263 ALA B 264 GLN B 274
SITE 2 BC2 6 ILE B 307 HOH B1192
SITE 1 BC3 3 SER A 50 ALA A 52 ASP A 53
SITE 1 BC4 6 GLU D 711 GLY D 712 ASN D 713 HOH D1303
SITE 2 BC4 6 HOH D1581 HOH D1582
SITE 1 BC5 9 ASN A 113 PRO A 114 VAL A 116 GLU B 311
SITE 2 BC5 9 GLY B 312 ASN B 313 GOL B 920 HOH B1056
SITE 3 BC5 9 HOH B1123
SITE 1 BC6 2 ASN C 503 GOL C 912
SITE 1 BC7 5 THR A 78 GOL A 911 THR C 478 ASN C 503
SITE 2 BC7 5 HOH C1157
SITE 1 BC8 4 GLN D 701 ALA D 702 ASN D 703 HOH D1509
SITE 1 BC9 4 ARG B 239 CYS B 240 LYS B 241 PRO B 242
SITE 1 CC1 3 ARG A 39 PRO A 42 HOH A1330
SITE 1 CC2 5 SER D 623 THR D 699 THR D 700 GLN D 701
SITE 2 CC2 5 HOH D1281
SITE 1 CC3 4 SER C 422 THR C 499 THR C 500 GLN C 501
SITE 1 CC4 3 SER A 23 THR A 99 HOH A1062
SITE 1 CC5 3 SER C 450 ASP C 453 HOH C1437
SITE 1 CC6 6 ALA B 204 GLU B 311 ASN B 313 GOL B 910
SITE 2 CC6 6 HOH B1332 HOH B1494
SITE 1 CC7 6 ALA B 256 SER B 259 GLN B 260 HOH B1010
SITE 2 CC7 6 HOH B1348 HOH B1431
SITE 1 CC8 5 GLU B 202 ARG B 210 ASN B 234 GOL B 905
SITE 2 CC8 5 HOH B1269
SITE 1 CC9 5 SER A 77 HOH A1140 HOH A1579 THR C 478
SITE 2 CC9 5 HIS C 505
SITE 1 DC1 4 ASP D 653 ALA D 656 HOH D1021 HOH D1028
CRYST1 83.569 96.341 48.240 90.00 107.50 90.00 P 1 21 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 0.011966 0.000000 0.003773 0.00000
SCALE2 0.000000 0.010380 0.000000 0.00000
SCALE3 0.000000 0.000000 0.021736 0.00000
(ATOM LINES ARE NOT SHOWN.)
END