HEADER HYDROLASE 12-MAY-17 5NZ2
TITLE TWIST AND INDUCE: DISSECTING THE LINK BETWEEN THE ENZYMATIC ACTIVITY
TITLE 2 AND THE SAPI INDUCING CAPACITY OF THE PHAGE 80 DUTPASE. D95E MUTANT
TITLE 3 FROM DUTPASE 80ALPHA PHAGE.
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: DUTPASE;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES;
COMPND 5 MUTATION: YES;
COMPND 6 OTHER_DETAILS: C-TERMINAL NOT PRESENT IN THE STRCUTRE ALTHOUGH
COMPND 7 NUCLEOTIDE IS PLACED IN THE ACTIVE CENTER. MAGNESIUM ATOM IS NOT
COMPND 8 COORDINATED BY E95.
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: STAPHYLOCOCCUS PHAGE 80ALPHA;
SOURCE 3 ORGANISM_TAXID: 53369;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 6 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 7 EXPRESSION_SYSTEM_PLASMID: PET28A
KEYWDS DUTPASE, 80 PHAGE, S.AUREUS, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR C.ALITE,S.HUMPHREY,J.DONDERIS,E.MAIQUES,J.R.CIGES-TOMAS,J.R.PENADES,
AUTHOR 2 A.MARINA
REVDAT 2 17-JAN-24 5NZ2 1 REMARK
REVDAT 1 20-SEP-17 5NZ2 0
JRNL AUTH C.ALITE,S.HUMPHREY,J.DONDERIS,E.MAIQUES,J.R.CIGES-TOMAS,
JRNL AUTH 2 J.R.PENADES,A.MARINA
JRNL TITL DISSECTING THE LINK BETWEEN THE ENZYMATIC ACTIVITY AND THE
JRNL TITL 2 SAPI INDUCING CAPACITY OF THE PHAGE 80 ALPHA DUTPASE.
JRNL REF SCI REP V. 7 11234 2017
JRNL REFN ESSN 2045-2322
JRNL PMID 28894239
JRNL DOI 10.1038/S41598-017-11234-9
REMARK 2
REMARK 2 RESOLUTION. 2.85 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0135
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.85
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 38.99
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 95.6
REMARK 3 NUMBER OF REFLECTIONS : 4894
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) : 0.231
REMARK 3 R VALUE (WORKING SET) : 0.228
REMARK 3 FREE R VALUE : 0.278
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.600
REMARK 3 FREE R VALUE TEST SET COUNT : 235
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) : 2.85
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.93
REMARK 3 REFLECTION IN BIN (WORKING SET) : 363
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 95.75
REMARK 3 BIN R VALUE (WORKING SET) : 0.2890
REMARK 3 BIN FREE R VALUE SET COUNT : 20
REMARK 3 BIN FREE R VALUE : 0.3050
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 1200
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 29
REMARK 3 SOLVENT ATOMS : 21
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 56.22
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.00000
REMARK 3 B22 (A**2) : 0.00000
REMARK 3 B33 (A**2) : 0.00000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.00000
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): 0.413
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.367
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 20.197
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.914
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.869
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 1249 ; 0.006 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 1194 ; 0.001 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 1698 ; 1.040 ; 1.986
REMARK 3 BOND ANGLES OTHERS (DEGREES): 2745 ; 0.779 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 154 ; 5.642 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 54 ;32.436 ;25.000
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 215 ;14.500 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 6 ;21.198 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 196 ; 0.062 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 1391 ; 0.003 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 269 ; 0.001 ; 0.020
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): 619 ; 1.005 ; 5.753
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 618 ; 1.005 ; 5.750
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 772 ; 1.831 ; 8.621
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): 773 ; 1.830 ; 8.625
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 630 ; 0.649 ; 5.824
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): 629 ; 0.649 ; 5.825
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): 927 ; 1.226 ; 8.709
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): 1251 ; 3.489 ;43.732
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): 1249 ; 3.375 ;43.750
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 : NULL
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.20
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 5NZ2 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 12-MAY-17.
REMARK 100 THE DEPOSITION ID IS D_1200004944.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 01-JUL-13
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 4.2
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : DIAMOND
REMARK 200 BEAMLINE : I04
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97949
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 6M-F
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 5130
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.850
REMARK 200 RESOLUTION RANGE LOW (A) : 38.990
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 96.1
REMARK 200 DATA REDUNDANCY : 2.200
REMARK 200 R MERGE (I) : 0.10200
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 5.2000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.85
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.00
REMARK 200 COMPLETENESS FOR SHELL (%) : 96.1
REMARK 200 DATA REDUNDANCY IN SHELL : 2.30
REMARK 200 R MERGE FOR SHELL (I) : 0.39400
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: PHASER
REMARK 200 STARTING MODEL: 3ZEZ
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 48.82
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.40
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 32% ETANOL, 2% PEG 1000, 0.1M
REMARK 280 PHOSPHATE CITRATE PH 4.2, VAPOR DIFFUSION, SITTING DROP,
REMARK 280 TEMPERATURE 296K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 3
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
REMARK 290 4555 X+1/2,-Y+1/2,-Z
REMARK 290 5555 Z,X,Y
REMARK 290 6555 Z+1/2,-X+1/2,-Y
REMARK 290 7555 -Z+1/2,-X,Y+1/2
REMARK 290 8555 -Z,X+1/2,-Y+1/2
REMARK 290 9555 Y,Z,X
REMARK 290 10555 -Y,Z+1/2,-X+1/2
REMARK 290 11555 Y+1/2,-Z+1/2,-X
REMARK 290 12555 -Y+1/2,-Z,X+1/2
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 43.59600
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 43.59600
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 43.59600
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 43.59600
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 43.59600
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 43.59600
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY2 5 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY1 6 0.000000 0.000000 1.000000 43.59600
REMARK 290 SMTRY2 6 -1.000000 0.000000 0.000000 43.59600
REMARK 290 SMTRY3 6 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY1 7 0.000000 0.000000 -1.000000 43.59600
REMARK 290 SMTRY2 7 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 1.000000 0.000000 43.59600
REMARK 290 SMTRY1 8 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY2 8 1.000000 0.000000 0.000000 43.59600
REMARK 290 SMTRY3 8 0.000000 -1.000000 0.000000 43.59600
REMARK 290 SMTRY1 9 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 9 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY3 9 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY1 10 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 10 0.000000 0.000000 1.000000 43.59600
REMARK 290 SMTRY3 10 -1.000000 0.000000 0.000000 43.59600
REMARK 290 SMTRY1 11 0.000000 1.000000 0.000000 43.59600
REMARK 290 SMTRY2 11 0.000000 0.000000 -1.000000 43.59600
REMARK 290 SMTRY3 11 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY1 12 0.000000 -1.000000 0.000000 43.59600
REMARK 290 SMTRY2 12 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY3 12 1.000000 0.000000 0.000000 43.59600
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 12290 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 19730 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -85.0 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 0.000000 0.000000 -1.000000 43.59600
REMARK 350 BIOMT2 2 -1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 1.000000 0.000000 43.59600
REMARK 350 BIOMT1 3 0.000000 -1.000000 0.000000 0.00000
REMARK 350 BIOMT2 3 0.000000 0.000000 1.000000 -43.59600
REMARK 350 BIOMT3 3 -1.000000 0.000000 0.000000 43.59600
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 A 313 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 MET A 1
REMARK 465 VAL A 157
REMARK 465 SER A 158
REMARK 465 GLU A 159
REMARK 465 ARG A 160
REMARK 465 GLY A 161
REMARK 465 GLU A 162
REMARK 465 LYS A 163
REMARK 465 GLY A 164
REMARK 465 PHE A 165
REMARK 465 GLY A 166
REMARK 465 SER A 167
REMARK 465 SER A 168
REMARK 465 GLY A 169
REMARK 465 VAL A 170
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 22 CG CD CE NZ
REMARK 470 THR A 23 OG1 CG2
REMARK 470 GLU A 55 CG CD OE1 OE2
REMARK 470 LYS A 117 CG CD CE NZ
REMARK 470 GLU A 118 CG CD OE1 OE2
REMARK 470 ARG A 119 CG CD NE CZ NH1 NH2
REMARK 470 LYS A 131 CE NZ
REMARK 470 GLU A 147 CG CD OE1 OE2
REMARK 470 LYS A 149 CG CD CE NZ
REMARK 470 GLU A 155 CG CD OE1 OE2
REMARK 470 SER A 156 OG
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 155 58.03 -91.38
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 MG A 202 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 DUP A 201 O2A
REMARK 620 2 DUP A 201 O2B 68.9
REMARK 620 3 DUP A 201 O1G 71.9 61.6
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 DUP A 201
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG A 202
DBREF 5NZ2 A 1 170 UNP A4ZF98 A4ZF98_9CAUD 1 170
SEQADV 5NZ2 GLU A 95 UNP A4ZF98 ASP 95 ENGINEERED MUTATION
SEQRES 1 A 170 MET THR ASN THR LEU GLN VAL LYS LEU LEU SER LYS ASN
SEQRES 2 A 170 ALA ARG MET PRO GLU ARG ASN HIS LYS THR ASP ALA GLY
SEQRES 3 A 170 TYR ASP ILE PHE SER ALA GLU THR VAL VAL LEU GLU PRO
SEQRES 4 A 170 GLN GLU LYS ALA VAL ILE LYS THR ASP VAL ALA VAL SER
SEQRES 5 A 170 ILE PRO GLU GLY TYR VAL GLY LEU LEU THR SER ARG SER
SEQRES 6 A 170 GLY VAL SER SER LYS THR HIS LEU VAL ILE GLU THR GLY
SEQRES 7 A 170 LYS ILE ASP ALA GLY TYR HIS GLY ASN LEU GLY ILE ASN
SEQRES 8 A 170 ILE LYS ASN GLU HIS GLU ASP ASP LYS MET GLN THR ILE
SEQRES 9 A 170 PHE LEU ARG ASN ILE ASP ASN GLU LYS ILE PHE GLU LYS
SEQRES 10 A 170 GLU ARG HIS LEU TYR LYS LEU GLY SER TYR ARG ILE GLU
SEQRES 11 A 170 LYS GLY GLU ARG ILE ALA GLN LEU VAL ILE VAL PRO ILE
SEQRES 12 A 170 TRP THR PRO GLU LEU LYS GLN VAL GLU GLU PHE GLU SER
SEQRES 13 A 170 VAL SER GLU ARG GLY GLU LYS GLY PHE GLY SER SER GLY
SEQRES 14 A 170 VAL
HET DUP A 201 28
HET MG A 202 1
HETNAM DUP 2'-DEOXYURIDINE 5'-ALPHA,BETA-IMIDO-TRIPHOSPHATE
HETNAM MG MAGNESIUM ION
FORMUL 2 DUP C9 H16 N3 O13 P3
FORMUL 3 MG MG 2+
FORMUL 4 HOH *21(H2 O)
HELIX 1 AA1 ARG A 64 THR A 71 1 8
SHEET 1 AA1 2 GLN A 6 LEU A 9 0
SHEET 2 AA1 2 VAL A 49 SER A 52 -1 O ALA A 50 N LYS A 8
SHEET 1 AA2 4 TYR A 27 PHE A 30 0
SHEET 2 AA2 4 ARG A 134 PRO A 142 -1 O LEU A 138 N TYR A 27
SHEET 3 AA2 4 TYR A 57 SER A 63 -1 N THR A 62 O GLN A 137
SHEET 4 AA2 4 GLY A 78 ILE A 80 -1 O GLY A 78 N LEU A 61
SHEET 1 AA3 2 VAL A 35 LEU A 37 0
SHEET 2 AA3 2 TYR A 127 ILE A 129 -1 O ILE A 129 N VAL A 35
SHEET 1 AA4 3 LYS A 42 LYS A 46 0
SHEET 2 AA4 3 GLY A 89 ASN A 94 -1 O ILE A 90 N ILE A 45
SHEET 3 AA4 3 LEU A 73 ILE A 75 -1 N VAL A 74 O LYS A 93
SHEET 1 AA5 2 GLN A 102 THR A 103 0
SHEET 2 AA5 2 TYR A 122 LYS A 123 -1 O TYR A 122 N THR A 103
SHEET 1 AA6 2 LEU A 106 ARG A 107 0
SHEET 2 AA6 2 LYS A 113 ILE A 114 -1 O ILE A 114 N LEU A 106
LINK O2A DUP A 201 MG MG A 202 1555 1555 2.19
LINK O2B DUP A 201 MG MG A 202 1555 1555 2.50
LINK O1G DUP A 201 MG MG A 202 1555 1555 2.51
SITE 1 AC1 11 ARG A 64 SER A 65 GLY A 66 GLY A 78
SITE 2 AC1 11 LYS A 79 ASP A 81 TYR A 84 GLY A 89
SITE 3 AC1 11 GLN A 137 MG A 202 HOH A 307
SITE 1 AC2 3 ASP A 28 GLN A 137 DUP A 201
CRYST1 87.192 87.192 87.192 90.00 90.00 90.00 P 21 3 12
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 0.011469 0.000000 0.000000 0.00000
SCALE2 0.000000 0.011469 0.000000 0.00000
SCALE3 0.000000 0.000000 0.011469 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
