HEADER DNA BINDING PROTEIN 06-DEC-96 1KAW
TITLE STRUCTURE OF SINGLE STRANDED DNA BINDING PROTEIN (SSB)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: SINGLE-STRANDED DNA BINDING PROTEIN;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 FRAGMENT: CHYMOTRYPTIC FRAGMENT, RESIDUES 1 - 135;
COMPND 5 SYNONYM: SSB
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 3 ORGANISM_TAXID: 562
KEYWDS DNA-BINDING PROTEIN, SINGLE STRANDED DNA BINDING PROTEIN, SSB, DNA
KEYWDS 2 BINDING PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR S.RAGHUNATHAN,G.WAKSMAN
REVDAT 3 07-FEB-24 1KAW 1 KEYWDS
REVDAT 2 24-FEB-09 1KAW 1 VERSN
REVDAT 1 31-DEC-97 1KAW 0
JRNL AUTH S.RAGHUNATHAN,C.S.RICARD,T.M.LOHMAN,G.WAKSMAN
JRNL TITL CRYSTAL STRUCTURE OF THE HOMO-TETRAMERIC DNA BINDING DOMAIN
JRNL TITL 2 OF ESCHERICHIA COLI SINGLE-STRANDED DNA-BINDING PROTEIN
JRNL TITL 3 DETERMINED BY MULTIWAVELENGTH X-RAY DIFFRACTION ON THE
JRNL TITL 4 SELENOMETHIONYL PROTEIN AT 2.9-A RESOLUTION.
JRNL REF PROC.NATL.ACAD.SCI.USA V. 94 6652 1997
JRNL REFN ISSN 0027-8424
JRNL PMID 9192620
JRNL DOI 10.1073/PNAS.94.13.6652
REMARK 2
REMARK 2 RESOLUTION. 2.90 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR 3.85
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.90
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 8.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 1.000
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 : 10473
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) : 0.221
REMARK 3 FREE R VALUE : 0.289
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 : 3032
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 35
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 21.90
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) : 0.016
REMARK 3 BOND ANGLES (DEGREES) : 1.900
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: MOLECULAR DYNAMICS RESTRAINED
REMARK 3 REFINEMENT FOLLOWED BY LEAST-SQUARES OPTIMIZATION
REMARK 4
REMARK 4 1KAW COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.
REMARK 100 THE DEPOSITION ID IS D_1000174392.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 11-NOV-95
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 : SSRL
REMARK 200 BEAMLINE : BL7-1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0800
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 14346
REMARK 200 RESOLUTION RANGE HIGH (A) : NULL
REMARK 200 RESOLUTION RANGE LOW (A) : NULL
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 1.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 89.7
REMARK 200 DATA REDUNDANCY : 2.600
REMARK 200 R MERGE (I) : 0.05300
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: NULL
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL
REMARK 200 SOFTWARE USED: X-PLOR 3.85
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 52.00
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: 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 29.04000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 52.92500
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 29.04000
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 52.92500
REMARK 290 SMTRY3 4 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: TETRAMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, 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 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 ALA A 1
REMARK 465 SER A 2
REMARK 465 PRO A 24
REMARK 465 ASN A 25
REMARK 465 GLY A 26
REMARK 465 GLY A 27
REMARK 465 TRP A 40
REMARK 465 ARG A 41
REMARK 465 ASP A 42
REMARK 465 LYS A 43
REMARK 465 ALA A 44
REMARK 465 THR A 45
REMARK 465 GLY A 46
REMARK 465 GLU A 47
REMARK 465 MET A 48
REMARK 465 LYS A 49
REMARK 465 GLY A 113
REMARK 465 GLY A 114
REMARK 465 ARG A 115
REMARK 465 GLN A 116
REMARK 465 GLY A 117
REMARK 465 GLY A 118
REMARK 465 GLY A 119
REMARK 465 ALA A 120
REMARK 465 PRO A 121
REMARK 465 ALA A 122
REMARK 465 GLY A 123
REMARK 465 GLY A 124
REMARK 465 ASN A 125
REMARK 465 ILE A 126
REMARK 465 GLY A 127
REMARK 465 GLY A 128
REMARK 465 GLY A 129
REMARK 465 GLN A 130
REMARK 465 PRO A 131
REMARK 465 GLN A 132
REMARK 465 GLY A 133
REMARK 465 GLY A 134
REMARK 465 TRP A 135
REMARK 465 ALA B 1
REMARK 465 SER B 2
REMARK 465 PRO B 24
REMARK 465 ASN B 25
REMARK 465 GLY B 26
REMARK 465 GLY B 27
REMARK 465 TRP B 40
REMARK 465 ARG B 41
REMARK 465 ASP B 42
REMARK 465 LYS B 43
REMARK 465 ALA B 44
REMARK 465 THR B 45
REMARK 465 GLY B 46
REMARK 465 GLU B 47
REMARK 465 MET B 48
REMARK 465 LYS B 49
REMARK 465 GLY B 113
REMARK 465 GLY B 114
REMARK 465 ARG B 115
REMARK 465 GLN B 116
REMARK 465 GLY B 117
REMARK 465 GLY B 118
REMARK 465 GLY B 119
REMARK 465 ALA B 120
REMARK 465 PRO B 121
REMARK 465 ALA B 122
REMARK 465 GLY B 123
REMARK 465 GLY B 124
REMARK 465 ASN B 125
REMARK 465 ILE B 126
REMARK 465 GLY B 127
REMARK 465 GLY B 128
REMARK 465 GLY B 129
REMARK 465 GLN B 130
REMARK 465 PRO B 131
REMARK 465 GLN B 132
REMARK 465 GLY B 133
REMARK 465 GLY B 134
REMARK 465 TRP B 135
REMARK 465 ALA C 1
REMARK 465 SER C 2
REMARK 465 PRO C 24
REMARK 465 ASN C 25
REMARK 465 GLY C 26
REMARK 465 GLY C 27
REMARK 465 TRP C 40
REMARK 465 ARG C 41
REMARK 465 ASP C 42
REMARK 465 LYS C 43
REMARK 465 ALA C 44
REMARK 465 THR C 45
REMARK 465 GLY C 46
REMARK 465 GLU C 47
REMARK 465 MET C 48
REMARK 465 LYS C 49
REMARK 465 GLY C 113
REMARK 465 GLY C 114
REMARK 465 ARG C 115
REMARK 465 GLN C 116
REMARK 465 GLY C 117
REMARK 465 GLY C 118
REMARK 465 GLY C 119
REMARK 465 ALA C 120
REMARK 465 PRO C 121
REMARK 465 ALA C 122
REMARK 465 GLY C 123
REMARK 465 GLY C 124
REMARK 465 ASN C 125
REMARK 465 ILE C 126
REMARK 465 GLY C 127
REMARK 465 GLY C 128
REMARK 465 GLY C 129
REMARK 465 GLN C 130
REMARK 465 PRO C 131
REMARK 465 GLN C 132
REMARK 465 GLY C 133
REMARK 465 GLY C 134
REMARK 465 TRP C 135
REMARK 465 ALA D 1
REMARK 465 SER D 2
REMARK 465 PRO D 24
REMARK 465 ASN D 25
REMARK 465 GLY D 26
REMARK 465 GLY D 27
REMARK 465 TRP D 40
REMARK 465 ARG D 41
REMARK 465 ASP D 42
REMARK 465 LYS D 43
REMARK 465 ALA D 44
REMARK 465 THR D 45
REMARK 465 GLY D 46
REMARK 465 GLU D 47
REMARK 465 MET D 48
REMARK 465 LYS D 49
REMARK 465 GLY D 113
REMARK 465 GLY D 114
REMARK 465 ARG D 115
REMARK 465 GLN D 116
REMARK 465 GLY D 117
REMARK 465 GLY D 118
REMARK 465 GLY D 119
REMARK 465 ALA D 120
REMARK 465 PRO D 121
REMARK 465 ALA D 122
REMARK 465 GLY D 123
REMARK 465 GLY D 124
REMARK 465 ASN D 125
REMARK 465 ILE D 126
REMARK 465 GLY D 127
REMARK 465 GLY D 128
REMARK 465 GLY D 129
REMARK 465 GLN D 130
REMARK 465 PRO D 131
REMARK 465 GLN D 132
REMARK 465 GLY D 133
REMARK 465 GLY D 134
REMARK 465 TRP D 135
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 NH2 ARG C 96 CD ARG D 96 0.96
REMARK 500 NH2 ARG A 96 CD ARG B 96 0.96
REMARK 500 NE ARG A 96 CZ ARG B 96 0.97
REMARK 500 NE ARG C 96 CZ ARG D 96 0.97
REMARK 500 CZ ARG A 96 NE ARG B 96 1.04
REMARK 500 CZ ARG C 96 NE ARG D 96 1.04
REMARK 500 NH2 ARG A 96 NE ARG B 96 1.07
REMARK 500 NH2 ARG C 96 NE ARG D 96 1.07
REMARK 500 NH2 ARG C 3 O HOH C 148 1.20
REMARK 500 NE ARG A 96 NH2 ARG B 96 1.32
REMARK 500 NE ARG C 96 NH2 ARG D 96 1.32
REMARK 500 NE ARG A 96 NE ARG B 96 1.35
REMARK 500 NE ARG C 96 NE ARG D 96 1.35
REMARK 500 CD ARG A 96 NH2 ARG B 96 1.49
REMARK 500 CD ARG C 96 NH2 ARG D 96 1.49
REMARK 500 OE2 GLU C 50 O HOH C 142 1.60
REMARK 500 OG1 THR D 98 O HOH D 138 1.69
REMARK 500 O SER D 92 O HOH D 140 1.86
REMARK 500 CZ ARG A 96 CZ ARG B 96 1.94
REMARK 500 CZ ARG C 96 CZ ARG D 96 1.94
REMARK 500 CZ ARG C 96 CD ARG D 96 2.00
REMARK 500 CZ ARG A 96 CD ARG B 96 2.00
REMARK 500 NH2 ARG A 84 O GLN C 91 2.01
REMARK 500 NE2 GLN C 94 NE2 GLN D 94 2.03
REMARK 500 NE2 GLN A 94 NE2 GLN B 94 2.03
REMARK 500 CD ARG A 96 CZ ARG B 96 2.14
REMARK 500 CD ARG C 96 CZ ARG D 96 2.14
REMARK 500 NH1 ARG C 84 OE2 GLU C 100 2.15
REMARK 500 NH1 ARG B 84 OE2 GLU B 100 2.15
REMARK 500 NH1 ARG A 84 OE2 GLU A 100 2.15
REMARK 500 NH1 ARG D 84 OE2 GLU D 100 2.15
REMARK 500 NE ARG A 96 NH1 ARG B 96 2.15
REMARK 500 NE ARG C 96 NH1 ARG D 96 2.15
REMARK 500
REMARK 500 REMARK: NULL
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 CE LYS B 7 OE2 GLU B 80 2556 1.78
REMARK 500 CG2 VAL B 5 OE1 GLN B 110 2556 1.95
REMARK 500 OE1 GLU B 65 O LYS D 87 3445 2.05
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 LEU A 10 CA - CB - CG ANGL. DEV. = 22.7 DEGREES
REMARK 500 ARG A 72 NE - CZ - NH2 ANGL. DEV. = 3.4 DEGREES
REMARK 500 LEU B 10 CA - CB - CG ANGL. DEV. = 22.8 DEGREES
REMARK 500 ARG B 72 NE - CZ - NH2 ANGL. DEV. = 3.4 DEGREES
REMARK 500 LEU C 10 CA - CB - CG ANGL. DEV. = 22.8 DEGREES
REMARK 500 ARG C 72 NE - CZ - NH2 ANGL. DEV. = 3.5 DEGREES
REMARK 500 LEU D 10 CA - CB - CG ANGL. DEV. = 22.8 DEGREES
REMARK 500 ARG D 72 NE - CZ - NH2 ANGL. DEV. = 3.4 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 ASP A 17 153.10 -41.62
REMARK 500 GLU A 19 70.91 -105.20
REMARK 500 GLN A 51 46.52 20.01
REMARK 500 PHE A 60 -142.96 -66.40
REMARK 500 LEU A 63 -17.60 -44.68
REMARK 500 TYR A 70 11.82 -141.86
REMARK 500 LEU A 71 -91.18 -70.92
REMARK 500 ARG A 72 112.30 73.25
REMARK 500 LYS A 73 131.39 2.51
REMARK 500 SER A 92 9.45 -65.90
REMARK 500 VAL A 103 73.33 -118.43
REMARK 500 ASN A 104 -101.77 -86.85
REMARK 500 ASP B 17 153.11 -41.60
REMARK 500 GLU B 19 70.93 -105.23
REMARK 500 GLN B 51 46.49 20.04
REMARK 500 PHE B 60 -142.93 -66.40
REMARK 500 LEU B 63 -17.64 -44.62
REMARK 500 TYR B 70 11.77 -141.81
REMARK 500 LEU B 71 -91.14 -70.93
REMARK 500 ARG B 72 112.30 73.22
REMARK 500 LYS B 73 131.35 2.55
REMARK 500 SER B 92 9.39 -65.85
REMARK 500 VAL B 103 73.31 -118.43
REMARK 500 ASN B 104 -101.79 -86.80
REMARK 500 ASP C 17 153.10 -41.61
REMARK 500 GLU C 19 70.91 -105.25
REMARK 500 GLN C 51 46.57 19.98
REMARK 500 PHE C 60 -142.96 -66.41
REMARK 500 LEU C 63 -17.55 -44.74
REMARK 500 TYR C 70 11.80 -141.79
REMARK 500 LEU C 71 -91.17 -70.96
REMARK 500 ARG C 72 112.28 73.28
REMARK 500 LYS C 73 131.41 2.50
REMARK 500 SER C 92 9.50 -65.93
REMARK 500 VAL C 103 73.39 -118.43
REMARK 500 ASN C 104 -101.81 -86.89
REMARK 500 ASP D 17 153.14 -41.68
REMARK 500 GLU D 19 70.98 -105.23
REMARK 500 GLN D 51 46.46 20.06
REMARK 500 PHE D 60 -142.92 -66.40
REMARK 500 LEU D 63 -17.66 -44.64
REMARK 500 TYR D 70 11.81 -141.79
REMARK 500 LEU D 71 -91.08 -70.98
REMARK 500 ARG D 72 112.31 73.15
REMARK 500 LYS D 73 131.39 2.56
REMARK 500 SER D 92 9.42 -65.85
REMARK 500 VAL D 103 73.28 -118.41
REMARK 500 ASN D 104 -101.73 -86.80
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1KAW A 1 135 UNP P02339 SSB_ECOLI 1 135
DBREF 1KAW B 1 135 UNP P02339 SSB_ECOLI 1 135
DBREF 1KAW C 1 135 UNP P02339 SSB_ECOLI 1 135
DBREF 1KAW D 1 135 UNP P02339 SSB_ECOLI 1 135
SEQRES 1 A 135 ALA SER ARG GLY VAL ASN LYS VAL ILE LEU VAL GLY ASN
SEQRES 2 A 135 LEU GLY GLN ASP PRO GLU VAL ARG TYR MET PRO ASN GLY
SEQRES 3 A 135 GLY ALA VAL ALA ASN ILE THR LEU ALA THR SER GLU SER
SEQRES 4 A 135 TRP ARG ASP LYS ALA THR GLY GLU MET LYS GLU GLN THR
SEQRES 5 A 135 GLU TRP HIS ARG VAL VAL LEU PHE GLY LYS LEU ALA GLU
SEQRES 6 A 135 VAL ALA SER GLU TYR LEU ARG LYS GLY SER GLN VAL TYR
SEQRES 7 A 135 ILE GLU GLY GLN LEU ARG THR ARG LYS TRP THR ASP GLN
SEQRES 8 A 135 SER GLY GLN ASP ARG TYR THR THR GLU VAL VAL VAL ASN
SEQRES 9 A 135 VAL GLY GLY THR MET GLN MET LEU GLY GLY ARG GLN GLY
SEQRES 10 A 135 GLY GLY ALA PRO ALA GLY GLY ASN ILE GLY GLY GLY GLN
SEQRES 11 A 135 PRO GLN GLY GLY TRP
SEQRES 1 B 135 ALA SER ARG GLY VAL ASN LYS VAL ILE LEU VAL GLY ASN
SEQRES 2 B 135 LEU GLY GLN ASP PRO GLU VAL ARG TYR MET PRO ASN GLY
SEQRES 3 B 135 GLY ALA VAL ALA ASN ILE THR LEU ALA THR SER GLU SER
SEQRES 4 B 135 TRP ARG ASP LYS ALA THR GLY GLU MET LYS GLU GLN THR
SEQRES 5 B 135 GLU TRP HIS ARG VAL VAL LEU PHE GLY LYS LEU ALA GLU
SEQRES 6 B 135 VAL ALA SER GLU TYR LEU ARG LYS GLY SER GLN VAL TYR
SEQRES 7 B 135 ILE GLU GLY GLN LEU ARG THR ARG LYS TRP THR ASP GLN
SEQRES 8 B 135 SER GLY GLN ASP ARG TYR THR THR GLU VAL VAL VAL ASN
SEQRES 9 B 135 VAL GLY GLY THR MET GLN MET LEU GLY GLY ARG GLN GLY
SEQRES 10 B 135 GLY GLY ALA PRO ALA GLY GLY ASN ILE GLY GLY GLY GLN
SEQRES 11 B 135 PRO GLN GLY GLY TRP
SEQRES 1 C 135 ALA SER ARG GLY VAL ASN LYS VAL ILE LEU VAL GLY ASN
SEQRES 2 C 135 LEU GLY GLN ASP PRO GLU VAL ARG TYR MET PRO ASN GLY
SEQRES 3 C 135 GLY ALA VAL ALA ASN ILE THR LEU ALA THR SER GLU SER
SEQRES 4 C 135 TRP ARG ASP LYS ALA THR GLY GLU MET LYS GLU GLN THR
SEQRES 5 C 135 GLU TRP HIS ARG VAL VAL LEU PHE GLY LYS LEU ALA GLU
SEQRES 6 C 135 VAL ALA SER GLU TYR LEU ARG LYS GLY SER GLN VAL TYR
SEQRES 7 C 135 ILE GLU GLY GLN LEU ARG THR ARG LYS TRP THR ASP GLN
SEQRES 8 C 135 SER GLY GLN ASP ARG TYR THR THR GLU VAL VAL VAL ASN
SEQRES 9 C 135 VAL GLY GLY THR MET GLN MET LEU GLY GLY ARG GLN GLY
SEQRES 10 C 135 GLY GLY ALA PRO ALA GLY GLY ASN ILE GLY GLY GLY GLN
SEQRES 11 C 135 PRO GLN GLY GLY TRP
SEQRES 1 D 135 ALA SER ARG GLY VAL ASN LYS VAL ILE LEU VAL GLY ASN
SEQRES 2 D 135 LEU GLY GLN ASP PRO GLU VAL ARG TYR MET PRO ASN GLY
SEQRES 3 D 135 GLY ALA VAL ALA ASN ILE THR LEU ALA THR SER GLU SER
SEQRES 4 D 135 TRP ARG ASP LYS ALA THR GLY GLU MET LYS GLU GLN THR
SEQRES 5 D 135 GLU TRP HIS ARG VAL VAL LEU PHE GLY LYS LEU ALA GLU
SEQRES 6 D 135 VAL ALA SER GLU TYR LEU ARG LYS GLY SER GLN VAL TYR
SEQRES 7 D 135 ILE GLU GLY GLN LEU ARG THR ARG LYS TRP THR ASP GLN
SEQRES 8 D 135 SER GLY GLN ASP ARG TYR THR THR GLU VAL VAL VAL ASN
SEQRES 9 D 135 VAL GLY GLY THR MET GLN MET LEU GLY GLY ARG GLN GLY
SEQRES 10 D 135 GLY GLY ALA PRO ALA GLY GLY ASN ILE GLY GLY GLY GLN
SEQRES 11 D 135 PRO GLN GLY GLY TRP
FORMUL 5 HOH *35(H2 O)
HELIX 1 1 GLY A 61 TYR A 70 1 10
HELIX 2 2 GLY B 61 TYR B 70 1 10
HELIX 3 3 GLY C 61 TYR C 70 1 10
HELIX 4 4 GLY D 61 TYR D 70 1 10
SHEET 1 A 6 THR A 108 MET A 111 0
SHEET 2 A 6 GLN A 76 GLY A 81 -1 N GLU A 80 O THR A 108
SHEET 3 A 6 VAL A 5 ASN A 13 -1 N GLY A 12 O VAL A 77
SHEET 4 A 6 VAL B 5 ASN B 13 -1 N VAL B 11 O VAL A 5
SHEET 5 A 6 GLN B 76 GLY B 81 -1 N GLY B 81 O VAL B 8
SHEET 6 A 6 THR B 108 MET B 111 -1 N GLN B 110 O TYR B 78
SHEET 1 B 4 ALA A 30 THR A 36 0
SHEET 2 B 4 GLU A 53 LEU A 59 -1 N LEU A 59 O ALA A 30
SHEET 3 B 4 TYR A 97 VAL A 103 1 N VAL A 101 O VAL A 58
SHEET 4 B 4 GLN A 82 LYS A 87 -1 N ARG A 86 O THR A 98
SHEET 1 C 4 ALA B 30 THR B 36 0
SHEET 2 C 4 GLU B 53 LEU B 59 -1 N LEU B 59 O ALA B 30
SHEET 3 C 4 TYR B 97 VAL B 103 1 N VAL B 101 O VAL B 58
SHEET 4 C 4 GLN B 82 LYS B 87 -1 N ARG B 86 O THR B 98
SHEET 1 D 6 THR C 108 MET C 111 0
SHEET 2 D 6 GLN C 76 GLY C 81 -1 N GLU C 80 O THR C 108
SHEET 3 D 6 VAL C 5 ASN C 13 -1 N GLY C 12 O VAL C 77
SHEET 4 D 6 VAL D 5 ASN D 13 -1 N VAL D 11 O VAL C 5
SHEET 5 D 6 GLN D 76 GLY D 81 -1 N GLY D 81 O VAL D 8
SHEET 6 D 6 THR D 108 MET D 111 -1 N GLN D 110 O TYR D 78
SHEET 1 E 4 ALA C 30 THR C 36 0
SHEET 2 E 4 GLU C 53 LEU C 59 -1 N LEU C 59 O ALA C 30
SHEET 3 E 4 TYR C 97 VAL C 103 1 N VAL C 101 O VAL C 58
SHEET 4 E 4 GLN C 82 LYS C 87 -1 N ARG C 86 O THR C 98
SHEET 1 F 4 ALA D 30 THR D 36 0
SHEET 2 F 4 GLU D 53 LEU D 59 -1 N LEU D 59 O ALA D 30
SHEET 3 F 4 TYR D 97 VAL D 103 1 N VAL D 101 O VAL D 58
SHEET 4 F 4 GLN D 82 LYS D 87 -1 N ARG D 86 O THR D 98
CRYST1 58.080 105.850 90.240 90.00 99.00 90.00 C 1 2 1 16
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 0.017218 0.000000 0.002727 0.00000
SCALE2 0.000000 0.009447 0.000000 0.00000
SCALE3 0.000000 0.000000 0.011220 0.00000
MTRIX1 1 0.030100 -0.036800 -0.998900 40.56470 1
MTRIX2 1 -0.029800 -0.998900 0.035900 79.58260 1
MTRIX3 1 -0.999100 0.028700 -0.031200 38.55650 1
MTRIX1 2 0.231800 -0.004400 0.972700 -13.00480 1
MTRIX2 2 -0.025700 -0.999700 0.001600 101.95840 1
MTRIX3 2 0.972400 -0.025300 -0.231900 18.32200 1
(ATOM LINES ARE NOT SHOWN.)
END