HEADER HYDROLASE 10-AUG-12 4GK6
TITLE X-RAY CRYSTAL STRUCTURE OF A HYPOTHETICAL DEOXYURIDINE 5-TRIPHOSPHATE
TITLE 2 NUCLEOTIDOHYDROLASE FROM MYCOBACTERIUM ABSCESSUS
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: DEOXYURIDINE 5'-TRIPHOSPHATE NUCLEOTIDOHYDROLASE;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: DUTPASE, DUTP PYROPHOSPHATASE;
COMPND 5 EC: 3.6.1.23;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MYCOBACTERIUM ABSCESSUS;
SOURCE 3 ORGANISM_TAXID: 561007;
SOURCE 4 STRAIN: ATCC 19977 / DSM 44196;
SOURCE 5 GENE: DUT, MAB_3003C;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS STRUCTURAL GENOMICS, NIAID, NATIONAL INSTITUTE OF ALLERGY AND
KEYWDS 2 INFECTIOUS DISEASES, SEATTLE STRUCTURAL GENOMICS CENTER FOR
KEYWDS 3 INFECTIOUS DISEASE, SSGCID, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR SEATTLE STRUCTURAL GENOMICS CENTER FOR INFECTIOUS DISEASE (SSGCID)
REVDAT 3 13-SEP-23 4GK6 1 REMARK SEQADV
REVDAT 2 22-APR-15 4GK6 1 JRNL
REVDAT 1 19-DEC-12 4GK6 0
JRNL AUTH L.BAUGH,I.PHAN,D.W.BEGLEY,M.C.CLIFTON,B.ARMOUR,D.M.DRANOW,
JRNL AUTH 2 B.M.TAYLOR,M.M.MURUTHI,J.ABENDROTH,J.W.FAIRMAN,D.FOX,
JRNL AUTH 3 S.H.DIETERICH,B.L.STAKER,A.S.GARDBERG,R.CHOI,S.N.HEWITT,
JRNL AUTH 4 A.J.NAPULI,J.MYERS,L.K.BARRETT,Y.ZHANG,M.FERRELL,E.MUNDT,
JRNL AUTH 5 K.THOMPKINS,N.TRAN,S.LYONS-ABBOTT,A.ABRAMOV,A.SEKAR,
JRNL AUTH 6 D.SERBZHINSKIY,D.LORIMER,G.W.BUCHKO,R.STACY,L.J.STEWART,
JRNL AUTH 7 T.E.EDWARDS,W.C.VAN VOORHIS,P.J.MYLER
JRNL TITL INCREASING THE STRUCTURAL COVERAGE OF TUBERCULOSIS DRUG
JRNL TITL 2 TARGETS.
JRNL REF TUBERCULOSIS (EDINB) V. 95 142 2015
JRNL REFN ISSN 1472-9792
JRNL PMID 25613812
JRNL DOI 10.1016/J.TUBE.2014.12.003
REMARK 2
REMARK 2 RESOLUTION. 1.65 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.7.0029
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) : 1.65
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 40.15
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 3 NUMBER OF REFLECTIONS : 19154
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) : 0.160
REMARK 3 R VALUE (WORKING SET) : 0.159
REMARK 3 FREE R VALUE : 0.181
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 986
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) : 1.65
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.69
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1341
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 100.0
REMARK 3 BIN R VALUE (WORKING SET) : 0.2070
REMARK 3 BIN FREE R VALUE SET COUNT : 79
REMARK 3 BIN FREE R VALUE : 0.2310
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 992
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 1
REMARK 3 SOLVENT ATOMS : 158
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 21.71
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 15.77
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): 0.079
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.077
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.048
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 2.601
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.965
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.958
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 1044 ; 0.011 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 1040 ; 0.001 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 1437 ; 1.486 ; 2.000
REMARK 3 BOND ANGLES OTHERS (DEGREES): 2398 ; 0.744 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 151 ; 6.511 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 41 ;37.200 ;24.390
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 171 ;10.475 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 9 ; 8.397 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 179 ; 0.084 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 1211 ; 0.006 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 206 ; 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): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
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 : 6
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A -2 A 12
REMARK 3 ORIGIN FOR THE GROUP (A): 17.5243 80.7978 52.4528
REMARK 3 T TENSOR
REMARK 3 T11: 0.1651 T22: 0.1767
REMARK 3 T33: 0.0040 T12: -0.0941
REMARK 3 T13: 0.0094 T23: -0.0178
REMARK 3 L TENSOR
REMARK 3 L11: 0.8794 L22: 1.3531
REMARK 3 L33: 1.3078 L12: -0.7448
REMARK 3 L13: -0.9947 L23: 0.7699
REMARK 3 S TENSOR
REMARK 3 S11: -0.0619 S12: 0.1616 S13: -0.0359
REMARK 3 S21: -0.0459 S22: 0.0305 S23: -0.0122
REMARK 3 S31: -0.0801 S32: -0.0887 S33: 0.0314
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 13 A 37
REMARK 3 ORIGIN FOR THE GROUP (A): 18.5197 86.4728 64.7011
REMARK 3 T TENSOR
REMARK 3 T11: 0.0668 T22: 0.0502
REMARK 3 T33: 0.0520 T12: 0.0015
REMARK 3 T13: -0.0070 T23: 0.0076
REMARK 3 L TENSOR
REMARK 3 L11: 0.3060 L22: 0.4280
REMARK 3 L33: 0.8969 L12: -0.0776
REMARK 3 L13: 0.0852 L23: -0.1615
REMARK 3 S TENSOR
REMARK 3 S11: -0.0195 S12: 0.0954 S13: 0.0133
REMARK 3 S21: -0.0669 S22: -0.0497 S23: 0.0260
REMARK 3 S31: -0.1707 S32: 0.0058 S33: 0.0691
REMARK 3
REMARK 3 TLS GROUP : 3
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 38 A 76
REMARK 3 ORIGIN FOR THE GROUP (A): 18.1176 79.9622 68.1916
REMARK 3 T TENSOR
REMARK 3 T11: 0.0667 T22: 0.0548
REMARK 3 T33: 0.0562 T12: -0.0019
REMARK 3 T13: 0.0050 T23: -0.0084
REMARK 3 L TENSOR
REMARK 3 L11: 0.2059 L22: 0.1063
REMARK 3 L33: 0.4999 L12: -0.0695
REMARK 3 L13: 0.2153 L23: 0.0761
REMARK 3 S TENSOR
REMARK 3 S11: -0.0095 S12: 0.0037 S13: 0.0105
REMARK 3 S21: -0.0106 S22: -0.0051 S23: -0.0054
REMARK 3 S31: -0.0273 S32: -0.0229 S33: 0.0146
REMARK 3
REMARK 3 TLS GROUP : 4
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 77 A 87
REMARK 3 ORIGIN FOR THE GROUP (A): 13.3962 71.8565 61.3531
REMARK 3 T TENSOR
REMARK 3 T11: 0.0490 T22: 0.0653
REMARK 3 T33: 0.0621 T12: -0.0193
REMARK 3 T13: -0.0086 T23: -0.0073
REMARK 3 L TENSOR
REMARK 3 L11: 1.0221 L22: 3.5914
REMARK 3 L33: 0.8367 L12: 0.0781
REMARK 3 L13: 0.7322 L23: -0.8083
REMARK 3 S TENSOR
REMARK 3 S11: -0.0695 S12: -0.1012 S13: -0.0830
REMARK 3 S21: -0.1684 S22: 0.0904 S23: -0.0358
REMARK 3 S31: 0.0228 S32: -0.1677 S33: -0.0209
REMARK 3
REMARK 3 TLS GROUP : 5
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 88 A 120
REMARK 3 ORIGIN FOR THE GROUP (A): 17.6071 80.9058 70.0228
REMARK 3 T TENSOR
REMARK 3 T11: 0.0624 T22: 0.0474
REMARK 3 T33: 0.0450 T12: 0.0077
REMARK 3 T13: 0.0030 T23: -0.0024
REMARK 3 L TENSOR
REMARK 3 L11: 0.2736 L22: 0.6887
REMARK 3 L33: 0.2363 L12: -0.1969
REMARK 3 L13: 0.1369 L23: -0.0454
REMARK 3 S TENSOR
REMARK 3 S11: -0.0177 S12: 0.0139 S13: 0.0140
REMARK 3 S21: -0.0116 S22: 0.0110 S23: 0.0082
REMARK 3 S31: -0.0226 S32: -0.0406 S33: 0.0067
REMARK 3
REMARK 3 TLS GROUP : 6
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 121 A 133
REMARK 3 ORIGIN FOR THE GROUP (A): 27.1639 48.0474 81.3928
REMARK 3 T TENSOR
REMARK 3 T11: 0.0879 T22: 0.0185
REMARK 3 T33: 0.0714 T12: 0.0029
REMARK 3 T13: 0.0022 T23: 0.0041
REMARK 3 L TENSOR
REMARK 3 L11: 2.1563 L22: 1.5587
REMARK 3 L33: 1.0645 L12: -0.4206
REMARK 3 L13: 1.2101 L23: 0.5179
REMARK 3 S TENSOR
REMARK 3 S11: -0.0666 S12: 0.0268 S13: -0.0065
REMARK 3 S21: -0.0097 S22: 0.0784 S23: 0.0023
REMARK 3 S31: -0.0411 S32: 0.0602 S33: -0.0118
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 : RESIDUAL ONLY
REMARK 4
REMARK 4 4GK6 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 17-AUG-12.
REMARK 100 THE DEPOSITION ID IS D_1000074285.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 02-AUG-12
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.50
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ALS
REMARK 200 BEAMLINE : 5.0.2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9774
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315R
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XSCALE
REMARK 200 DATA SCALING SOFTWARE : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 19154
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.650
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : 0.08400
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 14.5900
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.65
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.69
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.54500
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 3.270
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: PDB ENTRY 1MQ7
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 55.17
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.74
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 1 M LITHIUM CHLORIDE, 0.1 M SODIUM
REMARK 280 ACETATE, 30% PEG 6000, PH 7.50, VAPOR DIFFUSION, SITTING DROP,
REMARK 280 TEMPERATURE 289K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 2 3
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,Y,-Z
REMARK 290 4555 X,-Y,-Z
REMARK 290 5555 Z,X,Y
REMARK 290 6555 Z,-X,-Y
REMARK 290 7555 -Z,-X,Y
REMARK 290 8555 -Z,X,-Y
REMARK 290 9555 Y,Z,X
REMARK 290 10555 -Y,Z,-X
REMARK 290 11555 Y,-Z,-X
REMARK 290 12555 -Y,-Z,X
REMARK 290 13555 X+1/2,Y+1/2,Z+1/2
REMARK 290 14555 -X+1/2,-Y+1/2,Z+1/2
REMARK 290 15555 -X+1/2,Y+1/2,-Z+1/2
REMARK 290 16555 X+1/2,-Y+1/2,-Z+1/2
REMARK 290 17555 Z+1/2,X+1/2,Y+1/2
REMARK 290 18555 Z+1/2,-X+1/2,-Y+1/2
REMARK 290 19555 -Z+1/2,-X+1/2,Y+1/2
REMARK 290 20555 -Z+1/2,X+1/2,-Y+1/2
REMARK 290 21555 Y+1/2,Z+1/2,X+1/2
REMARK 290 22555 -Y+1/2,Z+1/2,-X+1/2
REMARK 290 23555 Y+1/2,-Z+1/2,-X+1/2
REMARK 290 24555 -Y+1/2,-Z+1/2,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 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 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000
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 0.00000
REMARK 290 SMTRY2 6 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY1 7 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY2 7 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY1 8 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY2 8 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 -1.000000 0.000000 0.00000
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 0.00000
REMARK 290 SMTRY3 10 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY1 11 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 11 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY3 11 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY1 12 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 12 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY3 12 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY1 13 1.000000 0.000000 0.000000 49.13000
REMARK 290 SMTRY2 13 0.000000 1.000000 0.000000 49.13000
REMARK 290 SMTRY3 13 0.000000 0.000000 1.000000 49.13000
REMARK 290 SMTRY1 14 -1.000000 0.000000 0.000000 49.13000
REMARK 290 SMTRY2 14 0.000000 -1.000000 0.000000 49.13000
REMARK 290 SMTRY3 14 0.000000 0.000000 1.000000 49.13000
REMARK 290 SMTRY1 15 -1.000000 0.000000 0.000000 49.13000
REMARK 290 SMTRY2 15 0.000000 1.000000 0.000000 49.13000
REMARK 290 SMTRY3 15 0.000000 0.000000 -1.000000 49.13000
REMARK 290 SMTRY1 16 1.000000 0.000000 0.000000 49.13000
REMARK 290 SMTRY2 16 0.000000 -1.000000 0.000000 49.13000
REMARK 290 SMTRY3 16 0.000000 0.000000 -1.000000 49.13000
REMARK 290 SMTRY1 17 0.000000 0.000000 1.000000 49.13000
REMARK 290 SMTRY2 17 1.000000 0.000000 0.000000 49.13000
REMARK 290 SMTRY3 17 0.000000 1.000000 0.000000 49.13000
REMARK 290 SMTRY1 18 0.000000 0.000000 1.000000 49.13000
REMARK 290 SMTRY2 18 -1.000000 0.000000 0.000000 49.13000
REMARK 290 SMTRY3 18 0.000000 -1.000000 0.000000 49.13000
REMARK 290 SMTRY1 19 0.000000 0.000000 -1.000000 49.13000
REMARK 290 SMTRY2 19 -1.000000 0.000000 0.000000 49.13000
REMARK 290 SMTRY3 19 0.000000 1.000000 0.000000 49.13000
REMARK 290 SMTRY1 20 0.000000 0.000000 -1.000000 49.13000
REMARK 290 SMTRY2 20 1.000000 0.000000 0.000000 49.13000
REMARK 290 SMTRY3 20 0.000000 -1.000000 0.000000 49.13000
REMARK 290 SMTRY1 21 0.000000 1.000000 0.000000 49.13000
REMARK 290 SMTRY2 21 0.000000 0.000000 1.000000 49.13000
REMARK 290 SMTRY3 21 1.000000 0.000000 0.000000 49.13000
REMARK 290 SMTRY1 22 0.000000 -1.000000 0.000000 49.13000
REMARK 290 SMTRY2 22 0.000000 0.000000 1.000000 49.13000
REMARK 290 SMTRY3 22 -1.000000 0.000000 0.000000 49.13000
REMARK 290 SMTRY1 23 0.000000 1.000000 0.000000 49.13000
REMARK 290 SMTRY2 23 0.000000 0.000000 -1.000000 49.13000
REMARK 290 SMTRY3 23 -1.000000 0.000000 0.000000 49.13000
REMARK 290 SMTRY1 24 0.000000 -1.000000 0.000000 49.13000
REMARK 290 SMTRY2 24 0.000000 0.000000 -1.000000 49.13000
REMARK 290 SMTRY3 24 1.000000 0.000000 0.000000 49.13000
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: 10460 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 17140 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -72.0 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 98.26000
REMARK 350 BIOMT2 2 -1.000000 0.000000 0.000000 98.26000
REMARK 350 BIOMT3 2 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT1 3 0.000000 -1.000000 0.000000 98.26000
REMARK 350 BIOMT2 3 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT3 3 -1.000000 0.000000 0.000000 98.26000
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 362 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A 443 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A 444 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 A -4
REMARK 465 PRO A -3
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 ARG A 8 CG CD NE CZ NH1 NH2
REMARK 470 VAL A 133 CG1 CG2
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 ND2 ASN A 89 O HOH A 377 1.79
REMARK 500 OG SER A 125 OD1 ASP A 127 1.82
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 201
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: SSGCID-MYABA.10050.A RELATED DB: TARGETTRACK
DBREF 4GK6 A 2 133 UNP B1MCW0 B1MCW0_MYCA9 2 133
SEQADV 4GK6 GLY A -4 UNP B1MCW0 EXPRESSION TAG
SEQADV 4GK6 PRO A -3 UNP B1MCW0 EXPRESSION TAG
SEQADV 4GK6 GLY A -2 UNP B1MCW0 EXPRESSION TAG
SEQADV 4GK6 SER A -1 UNP B1MCW0 EXPRESSION TAG
SEQADV 4GK6 MET A 0 UNP B1MCW0 EXPRESSION TAG
SEQADV 4GK6 LEU A 1 UNP B1MCW0 EXPRESSION TAG
SEQRES 1 A 138 GLY PRO GLY SER MET LEU ALA ILE VAL ARG LEU ASP ARG
SEQRES 2 A 138 GLU LEU PRO LEU PRO SER ARG ALA HIS ALA ASP ASP ALA
SEQRES 3 A 138 GLY VAL ASP LEU TYR SER ALA GLU ASP VAL VAL ILE GLU
SEQRES 4 A 138 PRO GLY ARG ARG THR LEU VAL GLY THR GLY ILE ALA VAL
SEQRES 5 A 138 ALA ILE PRO SER GLY MET VAL GLY LEU VAL HIS PRO ARG
SEQRES 6 A 138 SER GLY LEU ALA ALA ARG VAL GLY LEU SER ILE VAL ASN
SEQRES 7 A 138 SER PRO GLY THR ILE ASP ALA GLY TYR ARG GLY GLU VAL
SEQRES 8 A 138 LYS VAL ASN LEU ILE ASN LEU ASP SER GLU VAL PRO ILE
SEQRES 9 A 138 VAL ILE ALA ARG GLY ASP ARG ILE ALA GLN LEU LEU VAL
SEQRES 10 A 138 GLN GLN VAL GLU LEU PRO GLU LEU VAL GLU VAL ASP SER
SEQRES 11 A 138 PHE ASP GLU ALA GLY LEU ALA VAL
HET CL A 201 1
HETNAM CL CHLORIDE ION
FORMUL 2 CL CL 1-
FORMUL 3 HOH *158(H2 O)
HELIX 1 1 GLY A 62 VAL A 67 1 6
SHEET 1 A 2 ILE A 3 ARG A 5 0
SHEET 2 A 2 ILE A 45 VAL A 47 -1 O ALA A 46 N VAL A 4
SHEET 1 B 4 VAL A 23 TYR A 26 0
SHEET 2 B 4 ARG A 106 GLN A 114 -1 O LEU A 110 N VAL A 23
SHEET 3 B 4 MET A 53 HIS A 58 -1 N LEU A 56 O LEU A 111
SHEET 4 B 4 GLY A 76 ASP A 79 -1 O GLY A 76 N VAL A 57
SHEET 1 C 2 VAL A 31 ILE A 33 0
SHEET 2 C 2 ILE A 99 ILE A 101 -1 O ILE A 101 N VAL A 31
SHEET 1 D 3 ARG A 38 GLY A 42 0
SHEET 2 D 3 LYS A 87 ASN A 92 -1 O VAL A 88 N VAL A 41
SHEET 3 D 3 LEU A 69 ILE A 71 -1 N SER A 70 O ILE A 91
CISPEP 1 SER A 74 PRO A 75 0 -6.14
SITE 1 AC1 3 SER A 14 ARG A 15 LEU A 120
CRYST1 98.260 98.260 98.260 90.00 90.00 90.00 I 2 3 24
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 0.010177 0.000000 0.000000 0.00000
SCALE2 0.000000 0.010177 0.000000 0.00000
SCALE3 0.000000 0.000000 0.010177 0.00000
(ATOM LINES ARE NOT SHOWN.)
END