HEADER RECOMBINATION 23-DEC-13 4O6P
TITLE STRUCTURAL AND FUNCTIONAL STUDIES THE CHARACTERIZATION OF C58G/C70G
TITLE 2 MUTANT IN CYS4 ZINC-FINGER MOTIF IN THE RECOMBINATION MEDIATOR
TITLE 3 PROTEIN RECR
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: RECOMBINATION PROTEIN RECR;
COMPND 3 CHAIN: B, C;
COMPND 4 SYNONYM: RECR RECOMBINATIONAL DNA REPAIR PROTEIN;
COMPND 5 ENGINEERED: YES;
COMPND 6 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: THERMOANAEROBACTER TENGCONGENSIS;
SOURCE 3 ORGANISM_TAXID: 273068;
SOURCE 4 STRAIN: MB4;
SOURCE 5 GENE: RECR;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS ZINC FINGER, DNA REPAIR, DNA BINDING, RECOMBINATION
EXPDTA X-RAY DIFFRACTION
AUTHOR Q.TANG,Y.P.LIU,X.X.YAN,D.C.LIANG
REVDAT 3 08-NOV-23 4O6P 1 REMARK LINK
REVDAT 2 01-JAN-20 4O6P 1 JRNL SEQADV
REVDAT 1 10-DEC-14 4O6P 0
JRNL AUTH Q.TANG,Y.P.LIU,X.X.YAN,D.C.LIANG
JRNL TITL STRUCTURAL AND FUNCTIONAL CHARACTERIZATION OF CYS4 ZINC
JRNL TITL 2 FINGER MOTIF IN THE RECOMBINATION MEDIATOR PROTEIN RECR.
JRNL REF DNA REPAIR (AMST.) V. 24 10 2014
JRNL REFN ISSN 1568-7856
JRNL PMID 25460918
JRNL DOI 10.1016/J.DNAREP.2014.09.012
REMARK 2
REMARK 2 RESOLUTION. 3.00 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.5.0109
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD WITH PHASES
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 3.00
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 19.84
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.5
REMARK 3 NUMBER OF REFLECTIONS : 10641
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) : 0.236
REMARK 3 R VALUE (WORKING SET) : 0.235
REMARK 3 FREE R VALUE : 0.253
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 568
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) : 3.00
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 3.08
REMARK 3 REFLECTION IN BIN (WORKING SET) : 749
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.75
REMARK 3 BIN R VALUE (WORKING SET) : 0.3160
REMARK 3 BIN FREE R VALUE SET COUNT : 39
REMARK 3 BIN FREE R VALUE : 0.3570
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 3047
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 2
REMARK 3 SOLVENT ATOMS : 71
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 72.20
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.13000
REMARK 3 B22 (A**2) : 0.08000
REMARK 3 B33 (A**2) : 0.07000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.08000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): NULL
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.418
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.365
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 19.968
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.925
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.912
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 3088 ; 0.017 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 4175 ; 1.858 ; 1.993
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 391 ; 7.454 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 123 ;38.319 ;24.228
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 576 ;24.108 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 20 ;22.261 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 492 ; 0.121 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 2253 ; 0.007 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL
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): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL
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): 1953 ; 0.682 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 3175 ; 1.295 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1135 ; 1.677 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1000 ; 2.912 ; 4.500
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL
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 : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : 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 4O6P COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 08-JAN-14.
REMARK 100 THE DEPOSITION ID IS D_1000084110.
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 : 5.15
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SSRF
REMARK 200 BEAMLINE : BL17U
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.005
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : MAR SCANNER 345 MM PLATE
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 10641
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.700
REMARK 200 RESOLUTION RANGE LOW (A) : 20.000
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: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASES
REMARK 200 STARTING MODEL: 3VDP
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 58.91
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.99
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 12%(W/V) PEG33500, 100MM SODIUM
REMARK 280 ACETATE, 2%(W/V) TACSIMATE, PH 5.15, VAPOR DIFFUSION, HANGING
REMARK 280 DROP, TEMPERATURE 293K
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 46.93100
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 32.87700
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 46.93100
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 32.87700
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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 4310 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 23710 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -103.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, 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 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375 HOH C 324 LIES ON A SPECIAL POSITION.
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 GLY B -15
REMARK 465 SER B -14
REMARK 465 SER B -13
REMARK 465 HIS B -12
REMARK 465 HIS B -11
REMARK 465 HIS B -10
REMARK 465 HIS B -9
REMARK 465 HIS B -8
REMARK 465 HIS B -7
REMARK 465 SER B -6
REMARK 465 GLN B -5
REMARK 465 ASP B -4
REMARK 465 PRO B -3
REMARK 465 MET B -2
REMARK 465 SER B -1
REMARK 465 GLY C -15
REMARK 465 SER C -14
REMARK 465 SER C -13
REMARK 465 HIS C -12
REMARK 465 HIS C -11
REMARK 465 HIS C -10
REMARK 465 HIS C -9
REMARK 465 HIS C -8
REMARK 465 HIS C -7
REMARK 465 SER C -6
REMARK 465 GLN C -5
REMARK 465 ASP C -4
REMARK 465 PRO C -3
REMARK 465 MET C -2
REMARK 465 SER C -1
REMARK 465 VAL C 196
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 GLU B 93 OE1
REMARK 470 PHE C 59 CG CD1 CD2 CE1 CE2 CZ
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 TYR C 102 CE1 TYR C 102 CZ -0.085
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 PRO C 86 C - N - CA ANGL. DEV. = 11.1 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 THR B 3 -35.35 -35.38
REMARK 500 ILE B 30 -72.06 -71.91
REMARK 500 ILE B 31 -48.71 -25.47
REMARK 500 LYS B 56 6.88 -45.75
REMARK 500 PHE B 59 -2.57 73.98
REMARK 500 THR B 62 -141.08 -149.55
REMARK 500 SER B 71 29.97 -69.91
REMARK 500 ASN B 74 47.51 -100.59
REMARK 500 ASP B 76 87.12 -68.23
REMARK 500 GLU B 97 -36.78 -141.73
REMARK 500 TYR B 98 178.06 -55.65
REMARK 500 LYS B 99 -7.24 -157.04
REMARK 500 HIS B 106 38.46 88.32
REMARK 500 ARG B 121 51.73 -93.75
REMARK 500 ASP B 144 158.19 -28.82
REMARK 500 SER B 187 -67.08 -24.19
REMARK 500 LEU B 190 -87.21 -92.98
REMARK 500 GLU B 191 -53.23 -19.79
REMARK 500 ILE C 57 -76.26 -83.21
REMARK 500 VAL C 66 -130.44 -62.12
REMARK 500 CYS C 67 -128.27 -130.68
REMARK 500 ASP C 68 -36.96 -148.86
REMARK 500 ASN C 74 39.19 -68.01
REMARK 500 HIS C 77 35.82 -86.21
REMARK 500 PRO C 86 -37.67 -23.34
REMARK 500 MET C 92 -75.57 -54.47
REMARK 500 GLU C 93 -21.97 -37.24
REMARK 500 LYS C 96 -9.04 63.55
REMARK 500 TYR C 98 102.18 65.20
REMARK 500 LYS C 99 50.08 -115.61
REMARK 500 HIS C 103 75.35 -171.08
REMARK 500 VAL C 104 175.07 -56.93
REMARK 500 LEU C 105 -17.27 -154.19
REMARK 500 HIS C 106 10.86 56.63
REMARK 500 VAL C 115 140.43 -34.25
REMARK 500 ASP C 119 -0.90 -57.86
REMARK 500 ARG C 121 65.86 -100.11
REMARK 500 ILE C 122 -78.22 -85.09
REMARK 500 GLU C 127 48.07 -108.98
REMARK 500 ARG C 128 -46.01 -145.05
REMARK 500 ASP C 131 -135.36 -54.61
REMARK 500 LYS C 135 -75.60 -56.76
REMARK 500 ASP C 144 -167.74 -69.98
REMARK 500 THR C 150 -74.21 -89.62
REMARK 500 PRO C 160 -74.10 -52.82
REMARK 500 ILE C 168 -121.25 -76.66
REMARK 500 GLU C 179 -70.87 -62.43
REMARK 500 ARG C 194 -21.07 -172.32
REMARK 500
REMARK 500 REMARK: NULL
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN B 201 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS B 55 SG
REMARK 620 2 CYS B 67 SG 111.0
REMARK 620 3 HOH B 308 O 125.8 71.6
REMARK 620 4 HOH B 312 O 120.0 111.6 106.6
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN C 201 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS C 55 SG
REMARK 620 2 HOH C 330 O 101.7
REMARK 620 3 HOH C 349 O 128.4 73.6
REMARK 620 N 1 2
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN B 201
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN C 201
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4O6O RELATED DB: PDB
REMARK 900 THE DOUBLE POINTS MUTANT TTERECR C58G/C70G
DBREF 4O6P B -2 196 UNP Q8RDI4 RECR_THETN 1 199
DBREF 4O6P C -2 196 UNP Q8RDI4 RECR_THETN 1 199
SEQADV 4O6P GLY B -15 UNP Q8RDI4 EXPRESSION TAG
SEQADV 4O6P SER B -14 UNP Q8RDI4 EXPRESSION TAG
SEQADV 4O6P SER B -13 UNP Q8RDI4 EXPRESSION TAG
SEQADV 4O6P HIS B -12 UNP Q8RDI4 EXPRESSION TAG
SEQADV 4O6P HIS B -11 UNP Q8RDI4 EXPRESSION TAG
SEQADV 4O6P HIS B -10 UNP Q8RDI4 EXPRESSION TAG
SEQADV 4O6P HIS B -9 UNP Q8RDI4 EXPRESSION TAG
SEQADV 4O6P HIS B -8 UNP Q8RDI4 EXPRESSION TAG
SEQADV 4O6P HIS B -7 UNP Q8RDI4 EXPRESSION TAG
SEQADV 4O6P SER B -6 UNP Q8RDI4 EXPRESSION TAG
SEQADV 4O6P GLN B -5 UNP Q8RDI4 EXPRESSION TAG
SEQADV 4O6P ASP B -4 UNP Q8RDI4 EXPRESSION TAG
SEQADV 4O6P PRO B -3 UNP Q8RDI4 EXPRESSION TAG
SEQADV 4O6P GLY B 58 UNP Q8RDI4 CYS 61 ENGINEERED MUTATION
SEQADV 4O6P GLY B 70 UNP Q8RDI4 CYS 73 ENGINEERED MUTATION
SEQADV 4O6P GLY C -15 UNP Q8RDI4 EXPRESSION TAG
SEQADV 4O6P SER C -14 UNP Q8RDI4 EXPRESSION TAG
SEQADV 4O6P SER C -13 UNP Q8RDI4 EXPRESSION TAG
SEQADV 4O6P HIS C -12 UNP Q8RDI4 EXPRESSION TAG
SEQADV 4O6P HIS C -11 UNP Q8RDI4 EXPRESSION TAG
SEQADV 4O6P HIS C -10 UNP Q8RDI4 EXPRESSION TAG
SEQADV 4O6P HIS C -9 UNP Q8RDI4 EXPRESSION TAG
SEQADV 4O6P HIS C -8 UNP Q8RDI4 EXPRESSION TAG
SEQADV 4O6P HIS C -7 UNP Q8RDI4 EXPRESSION TAG
SEQADV 4O6P SER C -6 UNP Q8RDI4 EXPRESSION TAG
SEQADV 4O6P GLN C -5 UNP Q8RDI4 EXPRESSION TAG
SEQADV 4O6P ASP C -4 UNP Q8RDI4 EXPRESSION TAG
SEQADV 4O6P PRO C -3 UNP Q8RDI4 EXPRESSION TAG
SEQADV 4O6P GLY C 58 UNP Q8RDI4 CYS 61 ENGINEERED MUTATION
SEQADV 4O6P GLY C 70 UNP Q8RDI4 CYS 73 ENGINEERED MUTATION
SEQRES 1 B 212 GLY SER SER HIS HIS HIS HIS HIS HIS SER GLN ASP PRO
SEQRES 2 B 212 MET SER TYR TYR SER THR SER VAL ALA LYS LEU ILE GLU
SEQRES 3 B 212 GLU LEU SER LYS LEU PRO GLY ILE GLY PRO LYS THR ALA
SEQRES 4 B 212 GLN ARG LEU ALA PHE PHE ILE ILE ASN MET PRO LEU ASP
SEQRES 5 B 212 GLU VAL ARG SER LEU SER GLN ALA ILE ILE GLU ALA LYS
SEQRES 6 B 212 GLU LYS LEU ARG TYR CYS LYS ILE GLY PHE ASN ILE THR
SEQRES 7 B 212 ASP LYS GLU VAL CYS ASP ILE GLY SER ASP GLU ASN ARG
SEQRES 8 B 212 ASP HIS SER THR ILE CYS VAL VAL SER HIS PRO MET ASP
SEQRES 9 B 212 VAL VAL ALA MET GLU LYS VAL LYS GLU TYR LYS GLY VAL
SEQRES 10 B 212 TYR HIS VAL LEU HIS GLY VAL ILE SER PRO ILE GLU GLY
SEQRES 11 B 212 VAL GLY PRO GLU ASP ILE ARG ILE LYS GLU LEU LEU GLU
SEQRES 12 B 212 ARG VAL ARG ASP GLY SER VAL LYS GLU VAL ILE LEU ALA
SEQRES 13 B 212 THR ASN PRO ASP ILE GLU GLY GLU ALA THR ALA MET TYR
SEQRES 14 B 212 ILE ALA LYS LEU LEU LYS PRO PHE GLY VAL LYS VAL THR
SEQRES 15 B 212 ARG ILE ALA HIS GLY ILE PRO VAL GLY GLY ASP LEU GLU
SEQRES 16 B 212 TYR THR ASP VAL VAL THR LEU SER LYS ALA LEU GLU GLY
SEQRES 17 B 212 ARG ARG GLU VAL
SEQRES 1 C 212 GLY SER SER HIS HIS HIS HIS HIS HIS SER GLN ASP PRO
SEQRES 2 C 212 MET SER TYR TYR SER THR SER VAL ALA LYS LEU ILE GLU
SEQRES 3 C 212 GLU LEU SER LYS LEU PRO GLY ILE GLY PRO LYS THR ALA
SEQRES 4 C 212 GLN ARG LEU ALA PHE PHE ILE ILE ASN MET PRO LEU ASP
SEQRES 5 C 212 GLU VAL ARG SER LEU SER GLN ALA ILE ILE GLU ALA LYS
SEQRES 6 C 212 GLU LYS LEU ARG TYR CYS LYS ILE GLY PHE ASN ILE THR
SEQRES 7 C 212 ASP LYS GLU VAL CYS ASP ILE GLY SER ASP GLU ASN ARG
SEQRES 8 C 212 ASP HIS SER THR ILE CYS VAL VAL SER HIS PRO MET ASP
SEQRES 9 C 212 VAL VAL ALA MET GLU LYS VAL LYS GLU TYR LYS GLY VAL
SEQRES 10 C 212 TYR HIS VAL LEU HIS GLY VAL ILE SER PRO ILE GLU GLY
SEQRES 11 C 212 VAL GLY PRO GLU ASP ILE ARG ILE LYS GLU LEU LEU GLU
SEQRES 12 C 212 ARG VAL ARG ASP GLY SER VAL LYS GLU VAL ILE LEU ALA
SEQRES 13 C 212 THR ASN PRO ASP ILE GLU GLY GLU ALA THR ALA MET TYR
SEQRES 14 C 212 ILE ALA LYS LEU LEU LYS PRO PHE GLY VAL LYS VAL THR
SEQRES 15 C 212 ARG ILE ALA HIS GLY ILE PRO VAL GLY GLY ASP LEU GLU
SEQRES 16 C 212 TYR THR ASP VAL VAL THR LEU SER LYS ALA LEU GLU GLY
SEQRES 17 C 212 ARG ARG GLU VAL
HET ZN B 201 1
HET ZN C 201 1
HETNAM ZN ZINC ION
FORMUL 3 ZN 2(ZN 2+)
FORMUL 5 HOH *71(H2 O)
HELIX 1 1 SER B 2 LEU B 15 1 14
HELIX 2 2 GLY B 19 MET B 33 1 15
HELIX 3 3 PRO B 34 LEU B 52 1 19
HELIX 4 4 HIS B 85 VAL B 95 1 11
HELIX 5 5 ARG B 121 GLY B 132 1 12
HELIX 6 6 ASP B 144 LYS B 159 1 16
HELIX 7 7 ASP B 182 GLU B 191 1 10
HELIX 8 8 SER C 2 LYS C 14 1 13
HELIX 9 9 GLY C 19 MET C 33 1 15
HELIX 10 10 PRO C 34 LEU C 52 1 19
HELIX 11 11 PRO C 86 LYS C 94 1 9
HELIX 12 12 ASP C 144 LYS C 156 1 13
HELIX 13 13 LEU C 157 LYS C 159 5 3
HELIX 14 14 ASP C 182 GLY C 192 1 11
SHEET 1 A 2 ARG B 53 TYR B 54 0
SHEET 2 A 2 ILE B 61 THR B 62 -1 O THR B 62 N ARG B 53
SHEET 1 B 4 GLY B 100 VAL B 104 0
SHEET 2 B 4 ASP B 76 VAL B 83 1 N THR B 79 O VAL B 101
SHEET 3 B 4 GLU B 136 ALA B 140 1 O ILE B 138 N VAL B 82
SHEET 4 B 4 LYS B 164 ARG B 167 1 O THR B 166 N LEU B 139
SHEET 1 C 2 ARG C 53 TYR C 54 0
SHEET 2 C 2 ILE C 61 THR C 62 -1 O THR C 62 N ARG C 53
SHEET 1 D 3 THR C 79 VAL C 83 0
SHEET 2 D 3 GLU C 136 ALA C 140 1 O GLU C 136 N ILE C 80
SHEET 3 D 3 LYS C 164 ARG C 167 1 O LYS C 164 N VAL C 137
LINK SG CYS B 55 ZN ZN B 201 1555 1555 1.99
LINK SG CYS B 67 ZN ZN B 201 1555 1555 2.19
LINK ZN ZN B 201 O HOH B 308 1555 1555 2.04
LINK ZN ZN B 201 O HOH B 312 1555 1555 2.50
LINK SG CYS C 55 ZN ZN C 201 1555 1555 2.63
LINK ZN ZN C 201 O HOH C 330 1555 1555 2.25
LINK ZN ZN C 201 O HOH C 349 1555 1555 2.50
SITE 1 AC1 4 CYS B 55 CYS B 67 HOH B 308 HOH B 312
SITE 1 AC2 5 CYS C 55 GLY C 58 CYS C 67 HOH C 330
SITE 2 AC2 5 HOH C 349
CRYST1 93.862 65.754 91.755 90.00 95.41 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 0.010654 0.000000 0.001010 0.00000
SCALE2 0.000000 0.015208 0.000000 0.00000
SCALE3 0.000000 0.000000 0.010947 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
