HEADER HYDROLASE 31-OCT-18 5QJQ
TITLE PANDDA ANALYSIS GROUP DEPOSITION OF MODELS WITH MODELLED EVENTS (E.G.
TITLE 2 BOUND LIGANDS) -- CRYSTAL STRUCTURE OF NUDT5 IN COMPLEX WITH
TITLE 3 Z56791867
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ADP-SUGAR PYROPHOSPHATASE;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 SYNONYM: 8-OXO-DGDP PHOSPHATASE,NUCLEAR ATP-SYNTHESIS PROTEIN NUDIX5,
COMPND 5 NUCLEOSIDE DIPHOSPHATE-LINKED MOIETY X MOTIF 5,HNUDT5,YSA1H;
COMPND 6 EC: 3.6.1.13,3.6.1.58,2.7.7.96;
COMPND 7 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: NUDT5, NUDIX5, HSPC115;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS SGC - DIAMOND I04-1 FRAGMENT SCREENING, PANDDA, XCHEMEXPLORER, NUDT5,
KEYWDS 2 HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR Y.DUBIANOK,P.COLLINS,T.KROJER,N.WRIGHT,C.STRAIN-DAMERELL,N.BURGESS-
AUTHOR 2 BROWN,C.BOUNTRA,C.H.ARROWSMITH,A.EDWARDS,K.HUBER,F.VON DELFT
REVDAT 2 06-MAR-24 5QJQ 1 LINK
REVDAT 1 19-DEC-18 5QJQ 0
JRNL AUTH Y.DUBIANOK,P.COLLINS,T.KROJER,N.WRIGHT,C.STRAIN-DAMERELL,
JRNL AUTH 2 N.BURGESS-BROWN,C.BOUNTRA,C.H.ARROWSMITH,A.EDWARDS,K.HUBER,
JRNL AUTH 3 F.VON DELFT
JRNL TITL PANDDA ANALYSIS GROUP DEPOSITION OF MODELS WITH MODELLED
JRNL TITL 2 EVENTS (E.G. BOUND LIGANDS)
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 1.55 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0189
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.55
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 78.14
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 95.4
REMARK 3 NUMBER OF REFLECTIONS : 113070
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) : 0.213
REMARK 3 R VALUE (WORKING SET) : 0.211
REMARK 3 FREE R VALUE : 0.240
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 6010
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) : 1.55
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.59
REMARK 3 REFLECTION IN BIN (WORKING SET) : 8116
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 92.18
REMARK 3 BIN R VALUE (WORKING SET) : 0.3550
REMARK 3 BIN FREE R VALUE SET COUNT : 461
REMARK 3 BIN FREE R VALUE : 0.3710
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 5789
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 89
REMARK 3 SOLVENT ATOMS : 288
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 32.34
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 2.67000
REMARK 3 B22 (A**2) : -0.70000
REMARK 3 B33 (A**2) : -1.08000
REMARK 3 B12 (A**2) : 0.82000
REMARK 3 B13 (A**2) : 0.31000
REMARK 3 B23 (A**2) : 0.90000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.098
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.096
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.096
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 2.878
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.964
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.953
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 7896 ; 0.016 ; 0.020
REMARK 3 BOND LENGTHS OTHERS (A): 6322 ; 0.002 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 9490 ; 1.834 ; 1.991
REMARK 3 BOND ANGLES OTHERS (DEGREES): 14609 ; 0.999 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 934 ; 6.866 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 257 ;35.288 ;24.475
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1049 ;14.128 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 36 ;12.676 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1072 ; 0.107 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 8445 ; 0.009 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 1335 ; 0.002 ; 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): 4187 ; 2.498 ; 3.280
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 4188 ; 2.498 ; 3.280
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 4572 ; 3.649 ; 4.840
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
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 : 1.20
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 U VALUES : REFINED INDIVIDUALLY
REMARK 4
REMARK 4 5QJQ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 02-NOV-18.
REMARK 100 THE DEPOSITION ID IS D_1001402035.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 29-JUL-18
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : PH
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : DIAMOND
REMARK 200 BEAMLINE : I04-1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : NULL
REMARK 200 WAVELENGTH OR RANGE (A) : 0.91587
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : AIMLESS 0.7.1
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 119114
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.550
REMARK 200 RESOLUTION RANGE LOW (A) : 78.170
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 95.5
REMARK 200 DATA REDUNDANCY : 1.700
REMARK 200 R MERGE (I) : 0.02500
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 11.2000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.55
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.59
REMARK 200 COMPLETENESS FOR SHELL (%) : 93.6
REMARK 200 DATA REDUNDANCY IN SHELL : 1.40
REMARK 200 R MERGE FOR SHELL (I) : 0.38900
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: FOURIER SYNTHESIS
REMARK 200 SOFTWARE USED: REFMAC
REMARK 200 STARTING MODEL: 6GRU
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 48.60
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.39
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 33 % PEG4K, 0.2 MGCL2 AND 0.1 M TRIS,
REMARK 280 VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 293.15K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,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
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
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: 7530 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 15760 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -90.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B
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
REMARK 350 BIOMOLECULE: 2
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: 7660 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 15730 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -75.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 SER A 0
REMARK 465 MET A 1
REMARK 465 GLU A 2
REMARK 465 SER A 3
REMARK 465 GLN A 4
REMARK 465 GLU A 5
REMARK 465 PRO A 6
REMARK 465 THR A 7
REMARK 465 GLU A 8
REMARK 465 SER A 9
REMARK 465 SER A 10
REMARK 465 GLN A 11
REMARK 465 ASN A 12
REMARK 465 GLY A 13
REMARK 465 ASN A 208
REMARK 465 SER B 0
REMARK 465 MET B 1
REMARK 465 GLU B 2
REMARK 465 SER B 3
REMARK 465 GLN B 4
REMARK 465 GLU B 5
REMARK 465 PRO B 6
REMARK 465 THR B 7
REMARK 465 GLU B 8
REMARK 465 SER B 9
REMARK 465 SER B 10
REMARK 465 GLN B 11
REMARK 465 ASN B 12
REMARK 465 GLY B 13
REMARK 465 GLU B 56
REMARK 465 SER C 0
REMARK 465 MET C 1
REMARK 465 GLU C 2
REMARK 465 SER C 3
REMARK 465 GLN C 4
REMARK 465 GLU C 5
REMARK 465 PRO C 6
REMARK 465 THR C 7
REMARK 465 GLU C 8
REMARK 465 SER C 9
REMARK 465 SER C 10
REMARK 465 GLN C 11
REMARK 465 ASN C 12
REMARK 465 GLY C 13
REMARK 465 LYS C 14
REMARK 465 GLU C 56
REMARK 465 ASN C 208
REMARK 465 SER D 0
REMARK 465 MET D 1
REMARK 465 GLU D 2
REMARK 465 SER D 3
REMARK 465 GLN D 4
REMARK 465 GLU D 5
REMARK 465 PRO D 6
REMARK 465 THR D 7
REMARK 465 GLU D 8
REMARK 465 SER D 9
REMARK 465 SER D 10
REMARK 465 GLN D 11
REMARK 465 ASN D 12
REMARK 465 GLY D 13
REMARK 465 ARG D 54
REMARK 465 LYS D 55
REMARK 465 GLU D 56
REMARK 465 GLN D 57
REMARK 465 THR D 58
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 A 21 CG CD OE1 OE2
REMARK 470 LYS A 55 CG CD CE NZ
REMARK 470 GLU A 56 CG CD OE1 OE2
REMARK 470 GLU A 154 CG CD OE1 OE2
REMARK 470 ARG A 157 CG CD NE CZ NH1 NH2
REMARK 470 LYS A 159 CG CD CE NZ
REMARK 470 LYS A 161 CG CD CE NZ
REMARK 470 GLU A 188 CG CD OE1 OE2
REMARK 470 GLU A 189 CG CD OE1 OE2
REMARK 470 HIS A 190 CG ND1 CD2 CE1 NE2
REMARK 470 LYS B 27 CG CD CE NZ
REMARK 470 LYS B 55 CG CD CE NZ
REMARK 470 GLN B 57 CG CD OE1 NE2
REMARK 470 THR B 58 OG1 CG2
REMARK 470 ASP B 101 CG OD1 OD2
REMARK 470 LYS B 120 CG CD CE NZ
REMARK 470 ARG B 157 CG CD NE CZ NH1 NH2
REMARK 470 LYS B 159 CG CD CE NZ
REMARK 470 LYS B 161 CG CD CE NZ
REMARK 470 GLU B 169 CG CD OE1 OE2
REMARK 470 GLN B 180 CG CD OE1 NE2
REMARK 470 ILE C 17 CG1 CG2 CD1
REMARK 470 GLU C 20 CG CD OE1 OE2
REMARK 470 GLU C 21 CG CD OE1 OE2
REMARK 470 LYS C 33 CG CD CE NZ
REMARK 470 MET C 37 CG SD CE
REMARK 470 PRO C 39 CG CD
REMARK 470 LYS C 55 CG CD CE NZ
REMARK 470 GLN C 57 CG CD OE1 NE2
REMARK 470 THR C 58 OG1 CG2
REMARK 470 ARG C 157 CG CD NE CZ NH1 NH2
REMARK 470 LYS C 159 CG CD CE NZ
REMARK 470 LYS C 161 CG CD CE NZ
REMARK 470 GLN C 180 CG CD OE1 NE2
REMARK 470 GLU C 188 CG CD OE1 OE2
REMARK 470 GLU D 20 CG CD OE1 OE2
REMARK 470 GLU D 25 CG CD OE1 OE2
REMARK 470 THR D 53 OG1 CG2
REMARK 470 LYS D 81 CG CD CE NZ
REMARK 470 ASP D 101 CG OD1 OD2
REMARK 470 GLU D 114 CG CD OE1 OE2
REMARK 470 LYS D 120 CG CD CE NZ
REMARK 470 ASP D 122 CG OD1 OD2
REMARK 470 ARG D 157 CG CD NE CZ NH1 NH2
REMARK 470 LYS D 159 CG CD CE NZ
REMARK 470 ASP D 164 CG OD1 OD2
REMARK 470 GLU D 169 CG CD OE1 OE2
REMARK 470 GLN D 180 CG CD OE1 NE2
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 MG MG B 303 O HOH B 415 1.65
REMARK 500 OE1 GLU C 125 O HOH C 401 2.05
REMARK 500 O HOH A 405 O HOH A 417 2.08
REMARK 500 O HOH C 402 O HOH C 432 2.17
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. = -3.2 DEGREES
REMARK 500 ARG A 70 NE - CZ - NH2 ANGL. DEV. = -4.2 DEGREES
REMARK 500 ASP A 183 CB - CG - OD1 ANGL. DEV. = 5.8 DEGREES
REMARK 500 ARG B 196 NE - CZ - NH1 ANGL. DEV. = 4.3 DEGREES
REMARK 500 ARG C 196 NE - CZ - NH1 ANGL. DEV. = 3.8 DEGREES
REMARK 500 THR D 53 N - CA - CB ANGL. DEV. = 12.8 DEGREES
REMARK 500 ARG D 196 NE - CZ - NH1 ANGL. DEV. = 4.6 DEGREES
REMARK 500 ARG D 196 NE - CZ - NH2 ANGL. DEV. = -4.9 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 LYS A 55 -95.92 -120.18
REMARK 500 ASP A 133 74.02 -161.83
REMARK 500 ASP B 133 78.88 -161.10
REMARK 500 LYS B 161 73.89 -103.67
REMARK 500 ASP C 133 70.11 -167.29
REMARK 500 ASP C 177 31.82 -144.42
REMARK 500 ASP D 133 82.10 -163.48
REMARK 500 ARG D 157 56.77 -148.92
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 301 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ALA A 96 O
REMARK 620 2 GLU A 116 OE2 92.1
REMARK 620 3 HOH A 418 O 92.6 86.7
REMARK 620 4 HOH A 445 O 175.0 92.2 90.4
REMARK 620 5 HOH A 453 O 90.6 86.2 172.4 87.0
REMARK 620 6 HOH A 459 O 88.3 179.1 94.1 87.5 92.9
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG A 302 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU A 112 OE2
REMARK 620 2 GLU A 116 OE2 91.9
REMARK 620 3 GLU A 166 OE2 153.3 72.0
REMARK 620 4 HOH A 407 O 88.9 165.9 111.9
REMARK 620 5 HOH A 412 O 80.0 113.4 86.9 80.5
REMARK 620 6 HOH A 453 O 99.3 78.2 98.1 87.9 168.4
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG B 302 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ALA B 96 O
REMARK 620 2 GLU B 116 OE2 89.2
REMARK 620 3 HOH B 419 O 92.4 87.1
REMARK 620 4 HOH B 422 O 174.9 95.6 89.6
REMARK 620 5 HOH B 437 O 85.9 174.3 96.0 89.2
REMARK 620 6 HOH B 445 O 87.2 85.9 173.0 91.4 91.0
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG B 303 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU B 166 OE1
REMARK 620 2 HOH B 413 O 81.1
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG C 302 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ALA C 96 O
REMARK 620 2 GLU C 116 OE2 59.6
REMARK 620 3 HOH C 402 O 97.2 55.4
REMARK 620 4 HOH C 418 O 123.3 131.6 77.7
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG C 303 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ALA C 96 O
REMARK 620 2 GLU C 116 OE2 87.2
REMARK 620 3 HOH C 413 O 176.1 92.4
REMARK 620 4 HOH C 415 O 93.0 84.8 90.8
REMARK 620 5 HOH C 457 O 90.9 177.7 89.4 96.5
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG D 301 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ALA D 96 O
REMARK 620 2 GLU D 116 OE2 92.5
REMARK 620 3 HOH D 414 O 89.6 84.9
REMARK 620 4 HOH D 425 O 175.4 87.8 95.0
REMARK 620 5 HOH D 426 O 82.7 174.9 96.8 96.8
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG D 302 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU D 116 OE2
REMARK 620 2 HOH D 425 O 60.5
REMARK 620 3 HOH D 426 O 90.9 65.1
REMARK 620 4 HOH D 445 O 140.0 79.9 65.8
REMARK 620 N 1 2 3
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG A 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG A 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue K1S A 304
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 305
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO B 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG B 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG B 303
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue K1S B 304
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO C 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG C 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG C 303
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue K1S C 304
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue K1S C 305
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG D 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG D 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO D 303
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO D 304
DBREF 5QJQ A 1 208 UNP Q9UKK9 NUDT5_HUMAN 1 208
DBREF 5QJQ B 1 208 UNP Q9UKK9 NUDT5_HUMAN 1 208
DBREF 5QJQ C 1 208 UNP Q9UKK9 NUDT5_HUMAN 1 208
DBREF 5QJQ D 1 208 UNP Q9UKK9 NUDT5_HUMAN 1 208
SEQADV 5QJQ SER A 0 UNP Q9UKK9 EXPRESSION TAG
SEQADV 5QJQ SER B 0 UNP Q9UKK9 EXPRESSION TAG
SEQADV 5QJQ SER C 0 UNP Q9UKK9 EXPRESSION TAG
SEQADV 5QJQ SER D 0 UNP Q9UKK9 EXPRESSION TAG
SEQRES 1 A 209 SER MET GLU SER GLN GLU PRO THR GLU SER SER GLN ASN
SEQRES 2 A 209 GLY LYS GLN TYR ILE ILE SER GLU GLU LEU ILE SER GLU
SEQRES 3 A 209 GLY LYS TRP VAL LYS LEU GLU LYS THR THR TYR MET ASP
SEQRES 4 A 209 PRO THR GLY LYS THR ARG THR TRP GLU SER VAL LYS ARG
SEQRES 5 A 209 THR THR ARG LYS GLU GLN THR ALA ASP GLY VAL ALA VAL
SEQRES 6 A 209 ILE PRO VAL LEU GLN ARG THR LEU HIS TYR GLU CYS ILE
SEQRES 7 A 209 VAL LEU VAL LYS GLN PHE ARG PRO PRO MET GLY GLY TYR
SEQRES 8 A 209 CYS ILE GLU PHE PRO ALA GLY LEU ILE ASP ASP GLY GLU
SEQRES 9 A 209 THR PRO GLU ALA ALA ALA LEU ARG GLU LEU GLU GLU GLU
SEQRES 10 A 209 THR GLY TYR LYS GLY ASP ILE ALA GLU CYS SER PRO ALA
SEQRES 11 A 209 VAL CYS MET ASP PRO GLY LEU SER ASN CYS THR ILE HIS
SEQRES 12 A 209 ILE VAL THR VAL THR ILE ASN GLY ASP ASP ALA GLU ASN
SEQRES 13 A 209 ALA ARG PRO LYS PRO LYS PRO GLY ASP GLY GLU PHE VAL
SEQRES 14 A 209 GLU VAL ILE SER LEU PRO LYS ASN ASP LEU LEU GLN ARG
SEQRES 15 A 209 LEU ASP ALA LEU VAL ALA GLU GLU HIS LEU THR VAL ASP
SEQRES 16 A 209 ALA ARG VAL TYR SER TYR ALA LEU ALA LEU LYS HIS ALA
SEQRES 17 A 209 ASN
SEQRES 1 B 209 SER MET GLU SER GLN GLU PRO THR GLU SER SER GLN ASN
SEQRES 2 B 209 GLY LYS GLN TYR ILE ILE SER GLU GLU LEU ILE SER GLU
SEQRES 3 B 209 GLY LYS TRP VAL LYS LEU GLU LYS THR THR TYR MET ASP
SEQRES 4 B 209 PRO THR GLY LYS THR ARG THR TRP GLU SER VAL LYS ARG
SEQRES 5 B 209 THR THR ARG LYS GLU GLN THR ALA ASP GLY VAL ALA VAL
SEQRES 6 B 209 ILE PRO VAL LEU GLN ARG THR LEU HIS TYR GLU CYS ILE
SEQRES 7 B 209 VAL LEU VAL LYS GLN PHE ARG PRO PRO MET GLY GLY TYR
SEQRES 8 B 209 CYS ILE GLU PHE PRO ALA GLY LEU ILE ASP ASP GLY GLU
SEQRES 9 B 209 THR PRO GLU ALA ALA ALA LEU ARG GLU LEU GLU GLU GLU
SEQRES 10 B 209 THR GLY TYR LYS GLY ASP ILE ALA GLU CYS SER PRO ALA
SEQRES 11 B 209 VAL CYS MET ASP PRO GLY LEU SER ASN CYS THR ILE HIS
SEQRES 12 B 209 ILE VAL THR VAL THR ILE ASN GLY ASP ASP ALA GLU ASN
SEQRES 13 B 209 ALA ARG PRO LYS PRO LYS PRO GLY ASP GLY GLU PHE VAL
SEQRES 14 B 209 GLU VAL ILE SER LEU PRO LYS ASN ASP LEU LEU GLN ARG
SEQRES 15 B 209 LEU ASP ALA LEU VAL ALA GLU GLU HIS LEU THR VAL ASP
SEQRES 16 B 209 ALA ARG VAL TYR SER TYR ALA LEU ALA LEU LYS HIS ALA
SEQRES 17 B 209 ASN
SEQRES 1 C 209 SER MET GLU SER GLN GLU PRO THR GLU SER SER GLN ASN
SEQRES 2 C 209 GLY LYS GLN TYR ILE ILE SER GLU GLU LEU ILE SER GLU
SEQRES 3 C 209 GLY LYS TRP VAL LYS LEU GLU LYS THR THR TYR MET ASP
SEQRES 4 C 209 PRO THR GLY LYS THR ARG THR TRP GLU SER VAL LYS ARG
SEQRES 5 C 209 THR THR ARG LYS GLU GLN THR ALA ASP GLY VAL ALA VAL
SEQRES 6 C 209 ILE PRO VAL LEU GLN ARG THR LEU HIS TYR GLU CYS ILE
SEQRES 7 C 209 VAL LEU VAL LYS GLN PHE ARG PRO PRO MET GLY GLY TYR
SEQRES 8 C 209 CYS ILE GLU PHE PRO ALA GLY LEU ILE ASP ASP GLY GLU
SEQRES 9 C 209 THR PRO GLU ALA ALA ALA LEU ARG GLU LEU GLU GLU GLU
SEQRES 10 C 209 THR GLY TYR LYS GLY ASP ILE ALA GLU CYS SER PRO ALA
SEQRES 11 C 209 VAL CYS MET ASP PRO GLY LEU SER ASN CYS THR ILE HIS
SEQRES 12 C 209 ILE VAL THR VAL THR ILE ASN GLY ASP ASP ALA GLU ASN
SEQRES 13 C 209 ALA ARG PRO LYS PRO LYS PRO GLY ASP GLY GLU PHE VAL
SEQRES 14 C 209 GLU VAL ILE SER LEU PRO LYS ASN ASP LEU LEU GLN ARG
SEQRES 15 C 209 LEU ASP ALA LEU VAL ALA GLU GLU HIS LEU THR VAL ASP
SEQRES 16 C 209 ALA ARG VAL TYR SER TYR ALA LEU ALA LEU LYS HIS ALA
SEQRES 17 C 209 ASN
SEQRES 1 D 209 SER MET GLU SER GLN GLU PRO THR GLU SER SER GLN ASN
SEQRES 2 D 209 GLY LYS GLN TYR ILE ILE SER GLU GLU LEU ILE SER GLU
SEQRES 3 D 209 GLY LYS TRP VAL LYS LEU GLU LYS THR THR TYR MET ASP
SEQRES 4 D 209 PRO THR GLY LYS THR ARG THR TRP GLU SER VAL LYS ARG
SEQRES 5 D 209 THR THR ARG LYS GLU GLN THR ALA ASP GLY VAL ALA VAL
SEQRES 6 D 209 ILE PRO VAL LEU GLN ARG THR LEU HIS TYR GLU CYS ILE
SEQRES 7 D 209 VAL LEU VAL LYS GLN PHE ARG PRO PRO MET GLY GLY TYR
SEQRES 8 D 209 CYS ILE GLU PHE PRO ALA GLY LEU ILE ASP ASP GLY GLU
SEQRES 9 D 209 THR PRO GLU ALA ALA ALA LEU ARG GLU LEU GLU GLU GLU
SEQRES 10 D 209 THR GLY TYR LYS GLY ASP ILE ALA GLU CYS SER PRO ALA
SEQRES 11 D 209 VAL CYS MET ASP PRO GLY LEU SER ASN CYS THR ILE HIS
SEQRES 12 D 209 ILE VAL THR VAL THR ILE ASN GLY ASP ASP ALA GLU ASN
SEQRES 13 D 209 ALA ARG PRO LYS PRO LYS PRO GLY ASP GLY GLU PHE VAL
SEQRES 14 D 209 GLU VAL ILE SER LEU PRO LYS ASN ASP LEU LEU GLN ARG
SEQRES 15 D 209 LEU ASP ALA LEU VAL ALA GLU GLU HIS LEU THR VAL ASP
SEQRES 16 D 209 ALA ARG VAL TYR SER TYR ALA LEU ALA LEU LYS HIS ALA
SEQRES 17 D 209 ASN
HET MG A 301 1
HET MG A 302 1
HET CL A 303 1
HET K1S A 304 15
HET EDO A 305 4
HET EDO B 301 4
HET MG B 302 1
HET MG B 303 1
HET K1S B 304 15
HET EDO C 301 4
HET MG C 302 1
HET MG C 303 1
HET K1S C 304 15
HET K1S C 305 15
HET MG D 301 1
HET MG D 302 1
HET EDO D 303 4
HET EDO D 304 4
HETNAM MG MAGNESIUM ION
HETNAM CL CHLORIDE ION
HETNAM K1S N,N-DIETHYL-5-METHYL[1,2,4]TRIAZOLO[1,5-A]PYRIMIDIN-7-
HETNAM 2 K1S AMINE
HETNAM EDO 1,2-ETHANEDIOL
HETSYN EDO ETHYLENE GLYCOL
FORMUL 5 MG 8(MG 2+)
FORMUL 7 CL CL 1-
FORMUL 8 K1S 4(C10 H15 N5)
FORMUL 9 EDO 5(C2 H6 O2)
FORMUL 23 HOH *288(H2 O)
HELIX 1 AA1 THR A 104 GLY A 118 1 15
HELIX 2 AA2 ASP A 152 ALA A 156 5 5
HELIX 3 AA3 ASP A 177 GLU A 189 1 13
HELIX 4 AA4 ALA A 195 ALA A 207 1 13
HELIX 5 AA5 THR B 104 GLY B 118 1 15
HELIX 6 AA6 ASP B 152 ALA B 156 5 5
HELIX 7 AA7 ASP B 177 HIS B 190 1 14
HELIX 8 AA8 ASP B 194 ALA B 207 1 14
HELIX 9 AA9 THR C 104 GLY C 118 1 15
HELIX 10 AB1 ASP C 152 ALA C 156 5 5
HELIX 11 AB2 ASP C 177 GLU C 189 1 13
HELIX 12 AB3 ASP C 194 ALA C 207 1 14
HELIX 13 AB4 PRO D 85 GLY D 88 5 4
HELIX 14 AB5 THR D 104 GLY D 118 1 15
HELIX 15 AB6 ASP D 152 ALA D 156 5 5
HELIX 16 AB7 ASP D 177 GLU D 189 1 13
HELIX 17 AB8 ASP D 194 ALA D 207 1 14
SHEET 1 AA1 3 TYR A 16 GLU A 25 0
SHEET 2 AA1 3 VAL A 29 MET A 37 -1 O MET A 37 N TYR A 16
SHEET 3 AA1 3 THR A 43 ARG A 51 -1 O ARG A 44 N TYR A 36
SHEET 1 AA212 ASP A 122 CYS A 126 0
SHEET 2 AA212 THR A 140 ASN A 149 -1 O THR A 145 N ALA A 124
SHEET 3 AA212 GLY A 61 GLN A 69 1 N ALA A 63 O VAL A 144
SHEET 4 AA212 CYS A 76 ARG A 84 -1 O CYS A 76 N LEU A 68
SHEET 5 AA212 GLY A 89 GLU A 93 -1 O GLU A 93 N VAL A 80
SHEET 6 AA212 LEU A 191 ASP A 194 1 O ASP A 194 N ILE A 92
SHEET 7 AA212 VAL B 130 CYS B 131 1 O CYS B 131 N VAL A 193
SHEET 8 AA212 THR B 140 ASN B 149 -1 O ILE B 141 N VAL B 130
SHEET 9 AA212 GLY B 61 GLN B 69 1 N VAL B 67 O VAL B 146
SHEET 10 AA212 CYS B 76 ARG B 84 -1 O VAL B 78 N PRO B 66
SHEET 11 AA212 GLY B 89 GLU B 93 -1 O GLU B 93 N VAL B 80
SHEET 12 AA212 THR B 192 VAL B 193 1 O THR B 192 N ILE B 92
SHEET 1 AA3 4 VAL A 130 CYS A 131 0
SHEET 2 AA3 4 THR A 140 ASN A 149 -1 O ILE A 141 N VAL A 130
SHEET 3 AA3 4 GLY A 61 GLN A 69 1 N ALA A 63 O VAL A 144
SHEET 4 AA3 4 ALA A 96 LEU A 98 -1 O GLY A 97 N VAL A 62
SHEET 1 AA4 5 VAL A 130 CYS A 131 0
SHEET 2 AA4 5 THR A 140 ASN A 149 -1 O ILE A 141 N VAL A 130
SHEET 3 AA4 5 GLY A 61 GLN A 69 1 N ALA A 63 O VAL A 144
SHEET 4 AA4 5 CYS A 76 ARG A 84 -1 O CYS A 76 N LEU A 68
SHEET 5 AA4 5 GLU A 169 PRO A 174 -1 O LEU A 173 N ILE A 77
SHEET 1 AA5 4 ASP B 122 CYS B 126 0
SHEET 2 AA5 4 THR B 140 ASN B 149 -1 O THR B 147 N ASP B 122
SHEET 3 AA5 4 GLY B 61 GLN B 69 1 N VAL B 67 O VAL B 146
SHEET 4 AA5 4 ALA B 96 LEU B 98 -1 O GLY B 97 N VAL B 62
SHEET 1 AA6 4 ALA B 96 LEU B 98 0
SHEET 2 AA6 4 GLY B 61 GLN B 69 -1 N VAL B 62 O GLY B 97
SHEET 3 AA6 4 CYS B 76 ARG B 84 -1 O VAL B 78 N PRO B 66
SHEET 4 AA6 4 GLU B 169 PRO B 174 -1 O ILE B 171 N LEU B 79
SHEET 1 AA7 3 TYR B 16 GLU B 25 0
SHEET 2 AA7 3 VAL B 29 MET B 37 -1 O LYS B 33 N GLU B 21
SHEET 3 AA7 3 THR B 43 ARG B 51 -1 O TRP B 46 N THR B 34
SHEET 1 AA8 3 TYR C 16 GLU C 25 0
SHEET 2 AA8 3 VAL C 29 MET C 37 -1 O LYS C 33 N GLU C 21
SHEET 3 AA8 3 THR C 43 ARG C 51 -1 O ARG C 44 N TYR C 36
SHEET 1 AA9 6 ASP C 122 CYS C 126 0
SHEET 2 AA9 6 THR C 140 ASN C 149 -1 O THR C 145 N ALA C 124
SHEET 3 AA9 6 GLY C 61 GLN C 69 1 N ALA C 63 O VAL C 144
SHEET 4 AA9 6 CYS C 76 ARG C 84 -1 O CYS C 76 N LEU C 68
SHEET 5 AA9 6 GLY C 89 GLU C 93 -1 O GLU C 93 N VAL C 80
SHEET 6 AA9 6 LEU C 191 VAL C 193 1 O THR C 192 N ILE C 92
SHEET 1 AB1 4 VAL C 130 CYS C 131 0
SHEET 2 AB1 4 THR C 140 ASN C 149 -1 O ILE C 141 N VAL C 130
SHEET 3 AB1 4 GLY C 61 GLN C 69 1 N ALA C 63 O VAL C 144
SHEET 4 AB1 4 ALA C 96 LEU C 98 -1 O GLY C 97 N VAL C 62
SHEET 1 AB2 5 VAL C 130 CYS C 131 0
SHEET 2 AB2 5 THR C 140 ASN C 149 -1 O ILE C 141 N VAL C 130
SHEET 3 AB2 5 GLY C 61 GLN C 69 1 N ALA C 63 O VAL C 144
SHEET 4 AB2 5 CYS C 76 ARG C 84 -1 O CYS C 76 N LEU C 68
SHEET 5 AB2 5 GLU C 169 PRO C 174 -1 O LEU C 173 N ILE C 77
SHEET 1 AB3 3 TYR D 16 GLU D 25 0
SHEET 2 AB3 3 VAL D 29 MET D 37 -1 O THR D 35 N ILE D 18
SHEET 3 AB3 3 THR D 43 ARG D 51 -1 O TRP D 46 N THR D 34
SHEET 1 AB4 6 ASP D 122 CYS D 126 0
SHEET 2 AB4 6 THR D 140 ASN D 149 -1 O THR D 145 N ALA D 124
SHEET 3 AB4 6 GLY D 61 GLN D 69 1 N ALA D 63 O VAL D 144
SHEET 4 AB4 6 CYS D 76 PHE D 83 -1 O CYS D 76 N LEU D 68
SHEET 5 AB4 6 TYR D 90 GLU D 93 -1 O GLU D 93 N VAL D 80
SHEET 6 AB4 6 THR D 192 VAL D 193 1 O THR D 192 N ILE D 92
SHEET 1 AB5 4 VAL D 130 CYS D 131 0
SHEET 2 AB5 4 THR D 140 ASN D 149 -1 O ILE D 141 N VAL D 130
SHEET 3 AB5 4 GLY D 61 GLN D 69 1 N ALA D 63 O VAL D 144
SHEET 4 AB5 4 ALA D 96 LEU D 98 -1 O GLY D 97 N VAL D 62
SHEET 1 AB6 5 VAL D 130 CYS D 131 0
SHEET 2 AB6 5 THR D 140 ASN D 149 -1 O ILE D 141 N VAL D 130
SHEET 3 AB6 5 GLY D 61 GLN D 69 1 N ALA D 63 O VAL D 144
SHEET 4 AB6 5 CYS D 76 PHE D 83 -1 O CYS D 76 N LEU D 68
SHEET 5 AB6 5 GLU D 169 PRO D 174 -1 O LEU D 173 N ILE D 77
LINK O ALA A 96 MG MG A 301 1555 1555 2.04
LINK OE2 GLU A 112 MG MG A 302 1555 1555 2.12
LINK OE2 GLU A 116 MG MG A 301 1555 1555 2.07
LINK OE2 GLU A 116 MG MG A 302 1555 1555 2.46
LINK OE2 GLU A 166 MG MG A 302 1555 1555 2.43
LINK MG MG A 301 O HOH A 418 1555 1555 2.09
LINK MG MG A 301 O HOH A 445 1555 1555 2.14
LINK MG MG A 301 O HOH A 453 1555 1555 2.13
LINK MG MG A 301 O HOH A 459 1555 1555 2.14
LINK MG MG A 302 O HOH A 407 1555 1555 2.46
LINK MG MG A 302 O HOH A 412 1555 1555 1.96
LINK MG MG A 302 O HOH A 453 1555 1555 2.06
LINK O ALA B 96 MG MG B 302 1555 1555 2.00
LINK OE2 GLU B 116 MG MG B 302 1555 1555 2.08
LINK OE1 GLU B 166 MG MG B 303 1555 1555 2.35
LINK MG MG B 302 O HOH B 419 1555 1555 2.09
LINK MG MG B 302 O HOH B 422 1555 1555 2.17
LINK MG MG B 302 O HOH B 437 1555 1555 2.11
LINK MG MG B 302 O HOH B 445 1555 1555 2.16
LINK MG MG B 303 O HOH B 413 1555 1555 2.22
LINK O ALA C 96 MG MG C 302 1555 1555 2.95
LINK O ALA C 96 MG MG C 303 1555 1555 2.12
LINK OE2 GLU C 116 MG MG C 302 1555 1555 2.81
LINK OE2 GLU C 116 MG MG C 303 1555 1555 2.03
LINK MG MG C 302 O HOH C 402 1555 1555 2.76
LINK MG MG C 302 O HOH C 418 1555 1555 2.84
LINK MG MG C 303 O HOH C 413 1555 1555 2.21
LINK MG MG C 303 O HOH C 415 1555 1555 2.12
LINK MG MG C 303 O HOH C 457 1555 1555 2.03
LINK O ALA D 96 MG MG D 301 1555 1555 2.08
LINK OE2 GLU D 116 MG MG D 301 1555 1555 2.04
LINK OE2 GLU D 116 MG MG D 302 1555 1555 2.84
LINK MG MG D 301 O HOH D 414 1555 1555 2.11
LINK MG MG D 301 O HOH D 425 1555 1555 1.90
LINK MG MG D 301 O HOH D 426 1555 1555 2.06
LINK MG MG D 302 O HOH D 425 1555 1555 2.57
LINK MG MG D 302 O HOH D 426 1555 1555 2.91
LINK MG MG D 302 O HOH D 445 1555 1555 2.24
SITE 1 AC1 7 ALA A 96 GLU A 116 MG A 302 HOH A 418
SITE 2 AC1 7 HOH A 445 HOH A 453 HOH A 459
SITE 1 AC2 7 GLU A 112 GLU A 116 GLU A 166 MG A 301
SITE 2 AC2 7 HOH A 407 HOH A 412 HOH A 453
SITE 1 AC3 8 THR A 45 TRP A 46 GLU A 47 HOH A 413
SITE 2 AC3 8 HOH A 437 TRP B 28 VAL B 29 LEU B 98
SITE 1 AC4 5 ARG A 51 MET A 132 CYS A 139 HOH A 406
SITE 2 AC4 5 ASP B 133
SITE 1 AC5 5 GLN B 69 ASN B 149 ASP B 151 HOH B 404
SITE 2 AC5 5 HOH B 410
SITE 1 AC6 6 ALA B 96 GLU B 116 HOH B 419 HOH B 422
SITE 2 AC6 6 HOH B 437 HOH B 445
SITE 1 AC7 6 GLU B 112 GLU B 115 GLU B 166 HOH B 413
SITE 2 AC7 6 HOH B 415 HOH B 445
SITE 1 AC8 8 TRP A 28 VAL A 29 LEU A 98 THR B 45
SITE 2 AC8 8 TRP B 46 GLU B 47 HOH B 409 HOH B 455
SITE 1 AC9 3 ASP C 122 GLU C 154 HOH C 427
SITE 1 AD1 10 ALA C 96 GLY C 97 GLU C 112 GLU C 116
SITE 2 AD1 10 GLU C 166 MG C 303 HOH C 402 HOH C 413
SITE 3 AD1 10 HOH C 418 HOH C 457
SITE 1 AD2 6 ALA C 96 GLU C 116 MG C 302 HOH C 413
SITE 2 AD2 6 HOH C 415 HOH C 457
SITE 1 AD3 6 TRP C 28 HOH C 410 HOH C 461 THR D 45
SITE 2 AD3 6 TRP D 46 GLU D 47
SITE 1 AD4 7 THR C 45 TRP C 46 GLU C 47 HOH C 428
SITE 2 AD4 7 TRP D 28 VAL D 29 LEU D 98
SITE 1 AD5 6 ALA D 96 GLU D 116 MG D 302 HOH D 414
SITE 2 AD5 6 HOH D 425 HOH D 426
SITE 1 AD6 9 ALA D 96 GLY D 97 GLU D 112 GLU D 116
SITE 2 AD6 9 GLU D 166 MG D 301 HOH D 425 HOH D 426
SITE 3 AD6 9 HOH D 445
SITE 1 AD7 5 ARG C 51 MET C 132 CYS C 139 ASP D 133
SITE 2 AD7 5 HOH D 420
SITE 1 AD8 4 ASP C 133 ARG D 51 CYS D 139 HOH D 411
CRYST1 48.923 59.630 79.839 79.67 82.01 76.26 P 1 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 0.020440 -0.005000 -0.002133 0.00000
SCALE2 0.000000 0.017264 -0.002658 0.00000
SCALE3 0.000000 0.000000 0.012797 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
