HEADER HELICASE 28-AUG-96 1CUK
TITLE ESCHERICHIA COLI RUVA PROTEIN AT PH 4.9 AND ROOM TEMPERATURE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: RUVA PROTEIN;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 3 ORGANISM_TAXID: 562;
SOURCE 4 STRAIN: 12 BL21 (DE3);
SOURCE 5 CELL_LINE: BL21;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PAM159
KEYWDS DNA REPAIR, SOS RESPONSE, DNA-BINDING, DNA RECOMBINATION, HELICASE
EXPDTA X-RAY DIFFRACTION
AUTHOR J.B.RAFFERTY,D.W.RICE
REVDAT 4 07-FEB-24 1CUK 1 REMARK
REVDAT 3 13-JUL-11 1CUK 1 VERSN
REVDAT 2 24-FEB-09 1CUK 1 VERSN
REVDAT 1 22-OCT-97 1CUK 0
JRNL AUTH J.B.RAFFERTY,S.E.SEDELNIKOVA,D.HARGREAVES,P.J.ARTYMIUK,
JRNL AUTH 2 P.J.BAKER,G.J.SHARPLES,A.A.MAHDI,R.G.LLOYD,D.W.RICE
JRNL TITL CRYSTAL STRUCTURE OF DNA RECOMBINATION PROTEIN RUVA AND A
JRNL TITL 2 MODEL FOR ITS BINDING TO THE HOLLIDAY JUNCTION.
JRNL REF SCIENCE V. 274 415 1996
JRNL REFN ISSN 0036-8075
JRNL PMID 8832889
JRNL DOI 10.1126/SCIENCE.274.5286.415
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH S.E.SEDELNIKOVA,J.B.RAFFERTY,D.HARGREAVES,A.A.MAHDI,
REMARK 1 AUTH 2 R.G.LLOYD,D.W.RICE
REMARK 1 TITL CRYSTALLIZATION OF E.COLI RUVA GIVES INSIGHTS INTO THE
REMARK 1 TITL 2 SYMMETRY OF A HOLLIDAY JUNCTION/PROTEIN COMPLEX
REMARK 1 REF TO BE PUBLISHED
REMARK 1 REFN
REMARK 2
REMARK 2 RESOLUTION. 1.90 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : TNT
REMARK 3 AUTHORS : TRONRUD,TEN EYCK,MATTHEWS
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.90
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 15.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : NULL
REMARK 3 NUMBER OF REFLECTIONS : 17090
REMARK 3
REMARK 3 USING DATA ABOVE SIGMA CUTOFF.
REMARK 3 CROSS-VALIDATION METHOD : NULL
REMARK 3 FREE R VALUE TEST SET SELECTION : NULL
REMARK 3 R VALUE (WORKING + TEST SET) : NULL
REMARK 3 R VALUE (WORKING SET) : 0.209
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
REMARK 3 USING ALL DATA, NO SIGMA CUTOFF.
REMARK 3 R VALUE (WORKING + TEST SET, NO CUTOFF) : NULL
REMARK 3 R VALUE (WORKING SET, NO CUTOFF) : 0.2090
REMARK 3 FREE R VALUE (NO CUTOFF) : NULL
REMARK 3 FREE R VALUE TEST SET SIZE (%, NO CUTOFF) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT (NO CUTOFF) : NULL
REMARK 3 TOTAL NUMBER OF REFLECTIONS (NO CUTOFF) : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 1377
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 51
REMARK 3
REMARK 3 WILSON B VALUE (FROM FCALC, A**2) : NULL
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES. RMS WEIGHT COUNT
REMARK 3 BOND LENGTHS (A) : 0.016 ; 0.300 ; NULL
REMARK 3 BOND ANGLES (DEGREES) : 1.900 ; 1.000 ; NULL
REMARK 3 TORSION ANGLES (DEGREES) : NULL ; NULL ; NULL
REMARK 3 PSEUDOROTATION ANGLES (DEGREES) : NULL ; NULL ; NULL
REMARK 3 TRIGONAL CARBON PLANES (A) : NULL ; NULL ; NULL
REMARK 3 GENERAL PLANES (A) : 0.008 ; 5.000 ; NULL
REMARK 3 ISOTROPIC THERMAL FACTORS (A**2) : NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS (A) : NULL ; NULL ; NULL
REMARK 3
REMARK 3 INCORRECT CHIRAL-CENTERS (COUNT) : 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 RESTRAINT LIBRARIES.
REMARK 3 STEREOCHEMISTRY : NULL
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS:
REMARK 3 THE B-FACTORS FOR THE C-TERMINAL SEGMENT OF THE PROTEIN
REMARK 3 (RESIDUES 107 - 203) ARE HIGH WITH AN AVERAGE VALUE OF
REMARK 3 73.6 A**2 OVER ALL ATOMS (71.0A**2 FOR MAIN CHAIN) AND THUS
REMARK 3 REPRESENT POSITIONAL UNCERTAINTY OF APPROXIMATELY 1A IN
REMARK 3 SOME REGIONS.
REMARK 4
REMARK 4 1CUK 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_1000172544.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 26-OCT-95
REMARK 200 TEMPERATURE (KELVIN) : NULL
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : NULL
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
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) : 1.5418
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : AREA DETECTOR
REMARK 200 DETECTOR MANUFACTURER : XUONG-HAMLIN MULTIWIRE
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : SDMS
REMARK 200 DATA SCALING SOFTWARE : NULL
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 16391
REMARK 200 RESOLUTION RANGE HIGH (A) : NULL
REMARK 200 RESOLUTION RANGE LOW (A) : NULL
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 89.0
REMARK 200 DATA REDUNDANCY : 2.700
REMARK 200 R MERGE (I) : 0.07300
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: NULL
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 53.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.61
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 4
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 -Y,X,Z
REMARK 290 4555 Y,-X,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 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 0.00000
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA,PQS
REMARK 350 TOTAL BURIED SURFACE AREA: 9540 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 33420 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -53.0 KCAL/MOL
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 BIOMT1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT1 3 0.000000 -1.000000 0.000000 0.00000
REMARK 350 BIOMT2 3 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT3 3 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT1 4 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT2 4 -1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT3 4 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 143
REMARK 465 ALA A 144
REMARK 465 ASP A 145
REMARK 465 LEU A 146
REMARK 465 VAL A 147
REMARK 465 LEU A 148
REMARK 465 THR A 149
REMARK 465 SER A 150
REMARK 465 PRO A 151
REMARK 465 ALA A 152
REMARK 465 SER A 153
REMARK 465 PRO A 154
REMARK 465 ALA A 155
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 LYS A 119 CG CD CE NZ
REMARK 470 ARG A 123 CG CD NE CZ NH1 NH2
REMARK 470 ARG A 131 CG CD NE CZ NH1 NH2
REMARK 470 LYS A 133 CG CD CE NZ
REMARK 470 HIS A 136 CG ND1 CD2 CE1 NE2
REMARK 470 THR A 141 OG1 CG2
REMARK 470 PRO A 142 CG CD
REMARK 470 THR A 156 OG1 CG2
REMARK 470 ASP A 157 CG OD1 OD2
REMARK 470 ASP A 158 CG OD1 OD2
REMARK 470 GLU A 160 CG CD OE1 OE2
REMARK 470 GLN A 161 CG CD OE1 NE2
REMARK 470 GLU A 162 CG CD OE1 OE2
REMARK 470 ARG A 166 CG CD NE CZ NH1 NH2
REMARK 470 LYS A 173 CG CD CE NZ
REMARK 470 GLN A 175 CG CD OE1 NE2
REMARK 470 GLU A 176 CG CD OE1 OE2
REMARK 470 ARG A 179 CG CD NE CZ NH1 NH2
REMARK 470 LYS A 183 CG CD CE NZ
REMARK 470 ARG A 186 CG CD NE CZ NH1 NH2
REMARK 470 ASP A 188 CG OD1 OD2
REMARK 470 GLU A 197 CG CD OE1 OE2
REMARK 470 ARG A 200 CG CD NE CZ NH1 NH2
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 O SER A 190 N THR A 193 1.79
REMARK 500 O SER A 178 OG SER A 182 1.92
REMARK 500 O VAL A 181 O ILE A 184 2.04
REMARK 500 O THR A 78 O HOH A 254 2.16
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 NH1 ARG A 54 O HOH A 233 1554 2.10
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 GLU A 11 CD GLU A 11 OE1 0.096
REMARK 500 GLU A 20 CD GLU A 20 OE1 -0.074
REMARK 500 GLU A 27 CD GLU A 27 OE1 0.083
REMARK 500 GLU A 74 CD GLU A 74 OE2 0.077
REMARK 500 GLN A 96 C GLN A 97 N -0.164
REMARK 500 GLU A 122 CD GLU A 122 OE2 0.070
REMARK 500 GLU A 127 CD GLU A 127 OE1 0.084
REMARK 500 ALA A 189 C SER A 190 N -0.225
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 54 NE - CZ - NH2 ANGL. DEV. = 3.1 DEGREES
REMARK 500 ARG A 104 NE - CZ - NH1 ANGL. DEV. = 3.2 DEGREES
REMARK 500 ILE A 116 C - N - CA ANGL. DEV. = -16.0 DEGREES
REMARK 500 MET A 180 CG - SD - CE ANGL. DEV. = 9.8 DEGREES
REMARK 500 ARG A 186 CB - CA - C ANGL. DEV. = 18.0 DEGREES
REMARK 500 PRO A 187 CA - C - N ANGL. DEV. = -17.2 DEGREES
REMARK 500 PRO A 187 O - C - N ANGL. DEV. = 14.6 DEGREES
REMARK 500 ASP A 188 CA - C - N ANGL. DEV. = -13.8 DEGREES
REMARK 500 ASP A 188 O - C - N ANGL. DEV. = 12.3 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 105 71.18 43.03
REMARK 500 LYS A 112 8.52 -55.10
REMARK 500 ALA A 185 162.26 171.69
REMARK 500 ARG A 186 174.47 141.49
REMARK 500 SER A 191 -38.18 -24.27
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1CUK A 1 203 UNP P0A809 RUVA_ECOLI 1 203
SEQRES 1 A 203 MET ILE GLY ARG LEU ARG GLY ILE ILE ILE GLU LYS GLN
SEQRES 2 A 203 PRO PRO LEU VAL LEU ILE GLU VAL GLY GLY VAL GLY TYR
SEQRES 3 A 203 GLU VAL HIS MET PRO MET THR CYS PHE TYR GLU LEU PRO
SEQRES 4 A 203 GLU ALA GLY GLN GLU ALA ILE VAL PHE THR HIS PHE VAL
SEQRES 5 A 203 VAL ARG GLU ASP ALA GLN LEU LEU TYR GLY PHE ASN ASN
SEQRES 6 A 203 LYS GLN GLU ARG THR LEU PHE LYS GLU LEU ILE LYS THR
SEQRES 7 A 203 ASN GLY VAL GLY PRO LYS LEU ALA LEU ALA ILE LEU SER
SEQRES 8 A 203 GLY MET SER ALA GLN GLN PHE VAL ASN ALA VAL GLU ARG
SEQRES 9 A 203 GLU GLU VAL GLY ALA LEU VAL LYS LEU PRO GLY ILE GLY
SEQRES 10 A 203 LYS LYS THR ALA GLU ARG LEU ILE VAL GLU MET LYS ASP
SEQRES 11 A 203 ARG PHE LYS GLY LEU HIS GLY ASP LEU PHE THR PRO ALA
SEQRES 12 A 203 ALA ASP LEU VAL LEU THR SER PRO ALA SER PRO ALA THR
SEQRES 13 A 203 ASP ASP ALA GLU GLN GLU ALA VAL ALA ARG LEU VAL ALA
SEQRES 14 A 203 LEU GLY TYR LYS PRO GLN GLU ALA SER ARG MET VAL SER
SEQRES 15 A 203 LYS ILE ALA ARG PRO ASP ALA SER SER GLU THR LEU ILE
SEQRES 16 A 203 ARG GLU ALA LEU ARG ALA ALA LEU
FORMUL 2 HOH *51(H2 O)
HELIX 1 1 MET A 32 GLU A 37 1 6
HELIX 2 2 LYS A 66 LYS A 77 1 12
HELIX 3 3 PRO A 83 GLY A 92 1 10
HELIX 4 4 ALA A 95 GLU A 103 1 9
HELIX 5 5 VAL A 107 LYS A 112 1 6
HELIX 6 6 LYS A 118 GLY A 134 1 17
HELIX 7 7 ASP A 158 LEU A 170 1 13
HELIX 8 8 PRO A 174 SER A 182 1 9
HELIX 9 9 SER A 191 ARG A 200 1 10
SHEET 1 A 5 ALA A 57 PHE A 63 0
SHEET 2 A 5 GLU A 44 ARG A 54 -1 N ARG A 54 O ALA A 57
SHEET 3 A 5 ARG A 4 GLN A 13 -1 N GLY A 7 O ALA A 45
SHEET 4 A 5 LEU A 16 VAL A 21 -1 N GLU A 20 O ILE A 8
SHEET 5 A 5 VAL A 24 HIS A 29 -1 N VAL A 28 O VAL A 17
CISPEP 1 PRO A 14 PRO A 15 0 2.74
CRYST1 83.700 83.700 33.100 90.00 90.00 90.00 P 4 4
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 0.011947 0.000000 0.000000 0.00000
SCALE2 0.000000 0.011947 0.000000 0.00000
SCALE3 0.000000 0.000000 0.030211 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
