HEADER IMMUNE SYSTEM/DNA 16-MAR-93 1CBV
TITLE AN AUTOANTIBODY TO SINGLE-STRANDED DNA: COMPARISON OF THE THREE-
TITLE 2 DIMENSIONAL STRUCTURES OF THE UNLIGANDED FAB AND A DEOXYNUCLEOTIDE-
TITLE 3 FAB COMPLEX
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: DNA (5'-D(*TP*TP*T)-3');
COMPND 3 CHAIN: D;
COMPND 4 ENGINEERED: YES;
COMPND 5 MOL_ID: 2;
COMPND 6 MOLECULE: PROTEIN (FAB (BV04-01) AUTOANTIBODY-LIGHT CHAIN);
COMPND 7 CHAIN: L;
COMPND 8 ENGINEERED: YES;
COMPND 9 MOL_ID: 3;
COMPND 10 MOLECULE: PROTEIN (FAB (BV04-01) AUTOANTIBODY-HEAVY CHAIN);
COMPND 11 CHAIN: H;
COMPND 12 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 SYNTHETIC: YES;
SOURCE 3 MOL_ID: 2;
SOURCE 4 ORGANISM_SCIENTIFIC: MUS MUSCULUS;
SOURCE 5 ORGANISM_COMMON: HOUSE MOUSE;
SOURCE 6 ORGANISM_TAXID: 10090;
SOURCE 7 MOL_ID: 3;
SOURCE 8 ORGANISM_SCIENTIFIC: MUS MUSCULUS;
SOURCE 9 ORGANISM_COMMON: HOUSE MOUSE;
SOURCE 10 ORGANISM_TAXID: 10090
KEYWDS PROTEIN-DNA COMPLEX, SINGLE STRAND, IMMUNE SYSTEM-DNA COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR J.N.HERRON,X.M.HE,D.W.BALLARD,P.R.BLIER,P.E.PACE,A.L.M.BOTHWELL,
AUTHOR 2 E.W.VOSS JUNIOR,A.B.EDMUNDSON
REVDAT 5 29-NOV-17 1CBV 1 HELIX
REVDAT 4 05-FEB-14 1CBV 1 SOURCE VERSN
REVDAT 3 24-FEB-09 1CBV 1 VERSN
REVDAT 2 01-APR-03 1CBV 1 JRNL
REVDAT 1 31-JAN-94 1CBV 0
JRNL AUTH J.N.HERRON,X.M.HE,D.W.BALLARD,P.R.BLIER,P.E.PACE,
JRNL AUTH 2 A.L.BOTHWELL,E.W.VOSS JR.,A.B.EDMUNDSON
JRNL TITL AN AUTOANTIBODY TO SINGLE-STRANDED DNA: COMPARISON OF THE
JRNL TITL 2 THREE-DIMENSIONAL STRUCTURES OF THE UNLIGANDED FAB AND A
JRNL TITL 3 DEOXYNUCLEOTIDE-FAB COMPLEX.
JRNL REF PROTEINS V. 11 159 1991
JRNL REFN ISSN 0887-3585
JRNL PMID 1749770
JRNL DOI 10.1002/PROT.340110302
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH A.L.GIBSON,J.N.HERRON,D.W.BALLARD,E.W.VOSS,X.M.HE,
REMARK 1 AUTH 2 V.A.PATRICK,A.B.EDMUNDSON
REMARK 1 TITL CRYSTALLOGRAPHIC CHARACTERIZATION OF THE FAB FRAGMENT OF A
REMARK 1 TITL 2 MONOCLONAL ANTI-SS- DNA ANTIBODY
REMARK 1 REF MOL.IMMUNOL. V. 22 499 1985
REMARK 1 REFN ISSN 0161-5890
REMARK 2
REMARK 2 RESOLUTION. 2.66 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.66
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 6.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 NUMBER OF REFLECTIONS : 7759
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : NULL
REMARK 3 FREE R VALUE TEST SET SELECTION : NULL
REMARK 3 R VALUE (WORKING SET) : 0.191
REMARK 3 FREE R VALUE : NULL
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : NULL
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 : 3347
REMARK 3 NUCLEIC ACID ATOMS : 61
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 0
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
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) : 0.018
REMARK 3 BOND ANGLES (DEGREES) : NULL
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 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 1CBV COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY NDB.
REMARK 100 THE DEPOSITION ID IS D_1000172217.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : NULL
REMARK 200 TEMPERATURE (KELVIN) : NULL
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : NULL
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : NULL
REMARK 200 RADIATION SOURCE : NULL
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : NULL
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : NULL
REMARK 200 DETECTOR MANUFACTURER : NULL
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : NULL
REMARK 200 DATA SCALING SOFTWARE : NULL
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : NULL
REMARK 200 RESOLUTION RANGE HIGH (A) : NULL
REMARK 200 RESOLUTION RANGE LOW (A) : NULL
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
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: NULL
REMARK 200 SOFTWARE USED: NULL
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 47.97
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.36
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL
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 49.60000
REMARK 290 SMTRY3 2 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: TRIMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: D, L, H
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 400
REMARK 400 COMPOUND
REMARK 400 TURNS L2, L4, AND L10 CONTAIN ONLY 3 RESIDUES.
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 DT D 1 P DT D 1 OP3 0.122
REMARK 500 DT D 1 C4' DT D 1 C3' 0.069
REMARK 500 DT D 1 C2' DT D 1 C1' -0.171
REMARK 500 DT D 1 O3' DT D 1 C3' -0.145
REMARK 500 DT D 1 N3 DT D 1 C4 -0.061
REMARK 500 DT D 1 C4 DT D 1 C5 -0.080
REMARK 500 DT D 1 C5 DT D 1 C6 0.133
REMARK 500 DT D 1 C6 DT D 1 N1 -0.236
REMARK 500 DT D 1 C2 DT D 1 O2 0.132
REMARK 500 DT D 1 C5 DT D 1 C7 -0.049
REMARK 500 DT D 1 O3' DT D 2 P 0.090
REMARK 500 DT D 2 C4' DT D 2 C3' 0.098
REMARK 500 DT D 2 C3' DT D 2 C2' 0.074
REMARK 500 DT D 2 C2' DT D 2 C1' -0.067
REMARK 500 DT D 2 O4' DT D 2 C4' 0.078
REMARK 500 DT D 2 O3' DT D 2 C3' -0.125
REMARK 500 DT D 2 N1 DT D 2 C2 0.068
REMARK 500 DT D 2 N3 DT D 2 C4 -0.074
REMARK 500 DT D 2 C4 DT D 2 C5 -0.079
REMARK 500 DT D 2 C5 DT D 2 C6 0.128
REMARK 500 DT D 2 C6 DT D 2 N1 -0.229
REMARK 500 DT D 2 C2 DT D 2 O2 0.150
REMARK 500 DT D 2 C5 DT D 2 C7 -0.036
REMARK 500 DT D 3 C4' DT D 3 C3' 0.118
REMARK 500 DT D 3 C3' DT D 3 C2' 0.076
REMARK 500 DT D 3 C2' DT D 3 C1' -0.131
REMARK 500 DT D 3 O4' DT D 3 C1' 0.084
REMARK 500 DT D 3 O3' DT D 3 C3' -0.094
REMARK 500 DT D 3 N1 DT D 3 C2 0.082
REMARK 500 DT D 3 N3 DT D 3 C4 -0.062
REMARK 500 DT D 3 C4 DT D 3 C5 -0.080
REMARK 500 DT D 3 C5 DT D 3 C6 0.123
REMARK 500 DT D 3 C6 DT D 3 N1 -0.223
REMARK 500 DT D 3 C2 DT D 3 O2 0.142
REMARK 500 DT D 3 C4 DT D 3 O4 0.058
REMARK 500 DT D 3 C5 DT D 3 C7 -0.042
REMARK 500 GLU L 86 CD GLU L 86 OE2 0.109
REMARK 500 GLU L 110 CD GLU L 110 OE1 0.096
REMARK 500 GLU L 190 CD GLU L 190 OE2 0.076
REMARK 500 GLU L 200 CD GLU L 200 OE2 0.080
REMARK 500 GLU L 218 CD GLU L 218 OE2 0.079
REMARK 500 GLU H 1 CD GLU H 1 OE2 0.072
REMARK 500 PRO H 4 CD PRO H 4 N 0.100
REMARK 500 GLU H 6 CD GLU H 6 OE1 0.077
REMARK 500 GLU H 91 CD GLU H 91 OE2 0.068
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 DT D 1 C5' - C4' - C3' ANGL. DEV. = 12.5 DEGREES
REMARK 500 DT D 1 C1' - O4' - C4' ANGL. DEV. = 4.7 DEGREES
REMARK 500 DT D 1 C4' - C3' - C2' ANGL. DEV. = -4.9 DEGREES
REMARK 500 DT D 1 C3' - C2' - C1' ANGL. DEV. = 11.6 DEGREES
REMARK 500 DT D 1 O4' - C1' - N1 ANGL. DEV. = -4.5 DEGREES
REMARK 500 DT D 1 C6 - N1 - C2 ANGL. DEV. = -8.0 DEGREES
REMARK 500 DT D 1 C4 - C5 - C6 ANGL. DEV. = -5.9 DEGREES
REMARK 500 DT D 1 C5 - C6 - N1 ANGL. DEV. = 11.3 DEGREES
REMARK 500 DT D 1 N3 - C2 - O2 ANGL. DEV. = -4.2 DEGREES
REMARK 500 DT D 1 C6 - C5 - C7 ANGL. DEV. = 6.3 DEGREES
REMARK 500 DT D 1 C6 - N1 - C1' ANGL. DEV. = 10.6 DEGREES
REMARK 500 DT D 1 C3' - O3' - P ANGL. DEV. = 12.4 DEGREES
REMARK 500 DT D 2 O3' - P - O5' ANGL. DEV. = -11.4 DEGREES
REMARK 500 DT D 2 C5' - C4' - C3' ANGL. DEV. = 16.9 DEGREES
REMARK 500 DT D 2 C1' - O4' - C4' ANGL. DEV. = -7.5 DEGREES
REMARK 500 DT D 2 C4' - C3' - C2' ANGL. DEV. = -10.9 DEGREES
REMARK 500 DT D 2 O4' - C1' - C2' ANGL. DEV. = -8.9 DEGREES
REMARK 500 DT D 2 O4' - C1' - N1 ANGL. DEV. = 4.5 DEGREES
REMARK 500 DT D 2 C6 - N1 - C2 ANGL. DEV. = -7.1 DEGREES
REMARK 500 DT D 2 C4 - C5 - C6 ANGL. DEV. = -5.6 DEGREES
REMARK 500 DT D 2 C5 - C6 - N1 ANGL. DEV. = 10.3 DEGREES
REMARK 500 DT D 2 N3 - C4 - O4 ANGL. DEV. = -4.2 DEGREES
REMARK 500 DT D 2 C6 - C5 - C7 ANGL. DEV. = 4.4 DEGREES
REMARK 500 DT D 2 C6 - N1 - C1' ANGL. DEV. = 11.6 DEGREES
REMARK 500 DT D 2 C3' - O3' - P ANGL. DEV. = 8.0 DEGREES
REMARK 500 DT D 3 O4' - C4' - C3' ANGL. DEV. = -17.4 DEGREES
REMARK 500 DT D 3 C5' - C4' - C3' ANGL. DEV. = 29.7 DEGREES
REMARK 500 DT D 3 C4' - C3' - C2' ANGL. DEV. = -9.7 DEGREES
REMARK 500 DT D 3 O4' - C1' - C2' ANGL. DEV. = -4.9 DEGREES
REMARK 500 DT D 3 O4' - C1' - N1 ANGL. DEV. = -9.2 DEGREES
REMARK 500 DT D 3 C6 - N1 - C2 ANGL. DEV. = -6.1 DEGREES
REMARK 500 DT D 3 C4 - C5 - C6 ANGL. DEV. = -5.5 DEGREES
REMARK 500 DT D 3 C5 - C6 - N1 ANGL. DEV. = 9.3 DEGREES
REMARK 500 DT D 3 C6 - N1 - C1' ANGL. DEV. = 10.2 DEGREES
REMARK 500 ARG L 24 NE - CZ - NH2 ANGL. DEV. = 3.4 DEGREES
REMARK 500 ARG L 59 NE - CZ - NH2 ANGL. DEV. = 3.8 DEGREES
REMARK 500 ASP L 65 CB - CG - OD1 ANGL. DEV. = 7.5 DEGREES
REMARK 500 ARG L 82 CD - NE - CZ ANGL. DEV. = 14.4 DEGREES
REMARK 500 ARG L 82 NE - CZ - NH1 ANGL. DEV. = 3.3 DEGREES
REMARK 500 GLU L 86 CA - CB - CG ANGL. DEV. = 13.8 DEGREES
REMARK 500 GLU L 86 CG - CD - OE1 ANGL. DEV. = 12.2 DEGREES
REMARK 500 LEU L 88 CA - CB - CG ANGL. DEV. = 15.0 DEGREES
REMARK 500 ARG L 113 NE - CZ - NH1 ANGL. DEV. = 4.4 DEGREES
REMARK 500 ASP L 148 CB - CG - OD2 ANGL. DEV. = 6.5 DEGREES
REMARK 500 LYS L 152 CA - CB - CG ANGL. DEV. = 15.3 DEGREES
REMARK 500 ASP L 170 CB - CA - C ANGL. DEV. = 12.9 DEGREES
REMARK 500 ASP L 172 CB - CG - OD2 ANGL. DEV. = 6.4 DEGREES
REMARK 500 ASP L 175 CB - CG - OD1 ANGL. DEV. = 5.5 DEGREES
REMARK 500 LEU L 186 CA - CB - CG ANGL. DEV. = 23.4 DEGREES
REMARK 500 GLU L 190 CA - CB - CG ANGL. DEV. = 15.1 DEGREES
REMARK 500
REMARK 500 THIS ENTRY HAS 70 ANGLE DEVIATIONS.
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 LEU L 15 39.43 -83.05
REMARK 500 VAL L 30 90.69 -64.74
REMARK 500 HIS L 31 161.53 -49.11
REMARK 500 ASN L 33 102.15 170.70
REMARK 500 ASN L 35 100.53 98.10
REMARK 500 THR L 36 74.78 63.51
REMARK 500 LEU L 52 -68.65 -101.04
REMARK 500 VAL L 56 -49.96 67.39
REMARK 500 SER L 61 85.17 -65.68
REMARK 500 PRO L 64 155.74 -47.96
REMARK 500 ASP L 65 13.31 -61.66
REMARK 500 VAL L 83 93.80 -69.55
REMARK 500 SER L 96 45.01 -140.93
REMARK 500 GLU L 128 -32.88 -39.31
REMARK 500 TYR L 145 134.57 -173.98
REMARK 500 ARG L 160 -169.52 48.32
REMARK 500 ASN L 162 26.86 -161.99
REMARK 500 LYS L 174 -106.50 131.47
REMARK 500 SER L 176 10.33 80.77
REMARK 500 THR L 205 30.99 -88.91
REMARK 500 GLU L 218 -111.69 -164.32
REMARK 500 GLN H 3 130.52 60.30
REMARK 500 PHE H 27 -52.53 -1.69
REMARK 500 SER H 28 69.45 -153.14
REMARK 500 ASN H 30 -36.51 -25.44
REMARK 500 PRO H 41 -5.71 -56.96
REMARK 500 LYS H 43 -102.12 -170.26
REMARK 500 ARG H 52 -153.44 -77.92
REMARK 500 SER H 53 -168.69 -122.88
REMARK 500 ASN H 56 43.46 -83.52
REMARK 500 ASN H 57 34.05 39.91
REMARK 500 ASP H 68 -22.91 65.85
REMARK 500 SER H 77 -51.70 -28.04
REMARK 500 ASN H 87 57.80 28.47
REMARK 500 THR H 93 108.80 -44.43
REMARK 500 GLN H 102 78.64 -106.95
REMARK 500 THR H 103 104.43 -57.78
REMARK 500 THR H 105 -58.12 -144.64
REMARK 500 PHE H 108 37.84 73.13
REMARK 500 SER H 120 148.11 -174.84
REMARK 500 PRO H 134 -49.25 -25.78
REMARK 500 CYS H 136 -136.75 -94.35
REMARK 500 ASP H 138 -131.72 73.32
REMARK 500 GLU H 156 -61.22 -1.62
REMARK 500 SER H 164 70.95 -150.85
REMARK 500 SER H 166 -26.86 68.95
REMARK 500 SER H 168 46.45 -44.12
REMARK 500 THR H 195 -11.65 -152.11
REMARK 500 PRO H 208 -77.37 -52.94
REMARK 500 ALA H 209 107.92 -54.83
REMARK 500
REMARK 500 THIS ENTRY HAS 52 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: LD1
REMARK 800 EVIDENCE_CODE: UNKNOWN
REMARK 800 SITE_DESCRIPTION: NULL
REMARK 800
REMARK 800 SITE_IDENTIFIER: LD3
REMARK 800 EVIDENCE_CODE: UNKNOWN
REMARK 800 SITE_DESCRIPTION: NULL
REMARK 800
REMARK 800 SITE_IDENTIFIER: HD1
REMARK 800 EVIDENCE_CODE: UNKNOWN
REMARK 800 SITE_DESCRIPTION: NULL
REMARK 800
REMARK 800 SITE_IDENTIFIER: HD2
REMARK 800 EVIDENCE_CODE: UNKNOWN
REMARK 800 SITE_DESCRIPTION: NULL
REMARK 800
REMARK 800 SITE_IDENTIFIER: HD3
REMARK 800 EVIDENCE_CODE: UNKNOWN
REMARK 800 SITE_DESCRIPTION: NULL
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 THE PROTEIN WAS SEQUENCED BY D. W. BALLARD, P. R. BLIER,
REMARK 999 P. E. PACE, AND A. L. M. BOTHWELL. SEE REFERENCE 1 ABOVE.
DBREF 1CBV D 1 3 PDB 1CBV 1CBV 1 3
DBREF 1CBV L 1 219 PDB 1CBV 1CBV 1 219
DBREF 1CBV H 1 219 PDB 1CBV 1CBV 1 219
SEQRES 1 D 3 DT DT DT
SEQRES 1 L 219 ASP VAL VAL MET THR GLN THR PRO LEU SER LEU PRO VAL
SEQRES 2 L 219 SER LEU GLY ASP GLN ALA SER ILE SER CYS ARG SER SER
SEQRES 3 L 219 GLN SER LEU VAL HIS SER ASN GLY ASN THR TYR LEU HIS
SEQRES 4 L 219 TRP TYR LEU GLN LYS PRO GLY GLN SER PRO LYS LEU LEU
SEQRES 5 L 219 ILE TYR LYS VAL SER ASN ARG PHE SER GLY VAL PRO ASP
SEQRES 6 L 219 ARG PHE SER GLY SER GLY SER GLY THR ASP PHE THR LEU
SEQRES 7 L 219 LYS ILE SER ARG VAL GLU ALA GLU ASP LEU GLY VAL TYR
SEQRES 8 L 219 PHE CYS SER GLN SER THR HIS VAL PRO LEU THR PHE GLY
SEQRES 9 L 219 ALA GLY THR LYS LEU GLU LEU LYS ARG ALA ASP ALA ALA
SEQRES 10 L 219 PRO THR VAL SER ILE PHE PRO PRO SER SER GLU GLN LEU
SEQRES 11 L 219 THR SER GLY GLY ALA SER VAL VAL CYS PHE LEU ASN ASN
SEQRES 12 L 219 PHE TYR PRO LYS ASP ILE ASN VAL LYS TRP LYS ILE ASP
SEQRES 13 L 219 GLY SER GLU ARG GLN ASN GLY VAL LEU ASN SER TRP THR
SEQRES 14 L 219 ASP GLN ASP SER LYS ASP SER THR TYR SER MET SER SER
SEQRES 15 L 219 THR LEU THR LEU THR LYS ASP GLU TYR GLU ARG HIS ASN
SEQRES 16 L 219 SER TYR THR CYS GLU ALA THR HIS LYS THR SER THR SER
SEQRES 17 L 219 PRO ILE VAL LYS SER PHE ASN ARG ASN GLU CYS
SEQRES 1 H 219 GLU VAL GLN PRO VAL GLU THR GLY GLY GLY LEU VAL GLN
SEQRES 2 H 219 PRO LYS GLY SER LEU LYS LEU SER CYS ALA ALA SER GLY
SEQRES 3 H 219 PHE SER PHE ASN THR ASN ALA MET ASN TRP VAL ARG GLN
SEQRES 4 H 219 ALA PRO GLY LYS GLY LEU GLU TRP VAL ALA ARG ILE ARG
SEQRES 5 H 219 SER LYS SER ASN ASN TYR ALA THR TYR TYR ALA ASP SER
SEQRES 6 H 219 VAL LYS ASP ARG PHE THR ILE SER ARG ASP ASP SER GLN
SEQRES 7 H 219 ASN MET LEU TYR LEU GLN MET ASN ASN LEU LYS THR GLU
SEQRES 8 H 219 ASP THR ALA MET TYR TYR CYS VAL ARG ASP GLN THR GLY
SEQRES 9 H 219 THR ALA TRP PHE ALA TYR TRP GLY GLN GLY THR LEU VAL
SEQRES 10 H 219 THR VAL SER ALA ALA LYS THR THR PRO PRO SER VAL TYR
SEQRES 11 H 219 PRO LEU ALA PRO GLY CYS GLY ASP THR THR GLY SER SER
SEQRES 12 H 219 VAL THR LEU GLY CYS LEU VAL LYS GLY TYR PHE PRO GLU
SEQRES 13 H 219 SER VAL THR VAL THR TRP ASN SER GLY SER LEU SER SER
SEQRES 14 H 219 SER VAL HIS THR PHE PRO ALA LEU LEU GLN SER GLY LEU
SEQRES 15 H 219 TYR THR MET SER SER SER VAL THR VAL PRO SER SER THR
SEQRES 16 H 219 TRP PRO SER GLN THR VAL THR CYS SER VAL ALA HIS PRO
SEQRES 17 H 219 ALA SER SER THR THR VAL ASP LYS LYS LEU GLU
HELIX 1 L1 SER L 126 SER L 132 1 7
HELIX 2 L2 THR L 187 ARG L 193 1 7
HELIX 3 H1 ASP H 75 ASN H 79 1 5
HELIX 4 H2 PRO H 192 GLN H 199 1 8
SHEET 1 L1 4 VAL L 3 THR L 7 0
SHEET 2 L1 4 ALA L 19 SER L 26 -1 O ARG L 24 N THR L 5
SHEET 3 L1 4 ASP L 75 ILE L 80 -1 O PHE L 76 N CYS L 23
SHEET 4 L1 4 SER L 68 SER L 72 -1 O SER L 68 N LYS L 79
SHEET 1 L2 6 LEU L 9 VAL L 13 0
SHEET 2 L2 6 LEU L 101 LYS L 112 1 O LYS L 108 N LEU L 11
SHEET 3 L2 6 GLY L 89 SER L 96 -1 N GLN L 95 O THR L 102
SHEET 4 L2 6 TYR L 37 LYS L 44 -1 O HIS L 39 N SER L 94
SHEET 5 L2 6 GLN L 47 LYS L 55 -1 O ILE L 53 N TRP L 40
SHEET 6 L2 6 ASN L 58 PHE L 60 -1 O ASN L 58 N TYR L 54
SHEET 1 L3 4 THR L 119 PHE L 123 0
SHEET 2 L3 4 ALA L 135 PHE L 144 -1 O ASN L 142 N THR L 119
SHEET 3 L3 4 THR L 177 LEU L 186 -1 O LEU L 186 N ALA L 135
SHEET 4 L3 4 GLY L 163 ASP L 172 -1 N LEU L 165 O THR L 183
SHEET 1 L4 3 ASN L 150 ASP L 156 0
SHEET 2 L4 3 SER L 196 THR L 202 -1 O THR L 202 N ASN L 150
SHEET 3 L4 3 THR L 207 PHE L 214 -1 O ILE L 210 N ALA L 201
SHEET 1 H1 4 GLN H 3 THR H 7 0
SHEET 2 H1 4 LEU H 18 SER H 25 -1 O ALA H 23 N VAL H 5
SHEET 3 H1 4 MET H 80 ASN H 86 -1 O LEU H 81 N CYS H 22
SHEET 4 H1 4 ARG H 69 ASP H 75 -1 O SER H 73 N TYR H 82
SHEET 1 H2 6 GLY H 10 VAL H 12 0
SHEET 2 H2 6 TYR H 110 SER H 120 1 O LEU H 116 N GLY H 10
SHEET 3 H2 6 ALA H 94 VAL H 99 -1 O TYR H 96 N THR H 115
SHEET 4 H2 6 ALA H 33 ALA H 40 -1 N ASN H 35 O VAL H 99
SHEET 5 H2 6 LYS H 43 ARG H 52 -1 O ILE H 51 N MET H 34
SHEET 6 H2 6 ALA H 59 ALA H 63 -1 O TYR H 61 N ARG H 50
SHEET 1 H3 4 SER H 128 LEU H 132 0
SHEET 2 H3 4 VAL H 144 TYR H 153 -1 O LEU H 149 N TYR H 130
SHEET 3 H3 4 LEU H 182 VAL H 191 -1 O VAL H 191 N VAL H 144
SHEET 4 H3 4 SER H 170 GLN H 179 -1 O HIS H 172 N SER H 188
SHEET 1 H4 3 PHE H 154 ASN H 163 0
SHEET 2 H4 3 THR H 195 HIS H 207 -1 O SER H 204 N THR H 161
SHEET 3 H4 3 THR H 212 LEU H 218 -1 O LYS H 216 N CYS H 203
SSBOND 1 CYS L 23 CYS L 93 1555 1555 2.02
SSBOND 2 CYS L 139 CYS L 199 1555 1555 1.98
SSBOND 3 CYS L 219 CYS H 136 1555 1555 2.02
SSBOND 4 CYS H 22 CYS H 98 1555 1555 2.02
SSBOND 5 CYS H 148 CYS H 203 1555 1555 1.99
CISPEP 1 THR L 7 PRO L 8 0 -1.52
CISPEP 2 VAL L 99 PRO L 100 0 7.17
CISPEP 3 TYR L 145 PRO L 146 0 1.89
CISPEP 4 PHE H 154 PRO H 155 0 1.26
CISPEP 5 TRP H 196 PRO H 197 0 -1.45
SITE 1 LD1 4 HIS L 31 SER L 32 TYR L 37 HIS L 39
SITE 1 LD3 4 SER L 96 THR L 97 HIS L 98 VAL L 99
SITE 1 HD1 3 THR H 31 ASN H 32 ALA H 33
SITE 1 HD2 3 ARG H 52 SER H 53 ASN H 56
SITE 1 HD3 7 ASP H 101 GLN H 102 THR H 103 GLY H 104
SITE 2 HD3 7 THR H 105 ALA H 106 TRP H 107
CRYST1 63.500 99.200 36.600 90.00 95.30 90.00 P 1 21 1 2
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 0.015748 0.000000 0.001461 0.00000
SCALE2 0.000000 0.010081 0.000000 0.00000
SCALE3 0.000000 0.000000 0.027440 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
