HEADER OXIDOREDUCTASE 29-AUG-11 3TL3
TITLE STRUCTURE OF A SHORT-CHAIN TYPE DEHYDROGENASE/REDUCTASE FROM
TITLE 2 MYCOBACTERIUM ULCERANS
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: SHORT-CHAIN TYPE DEHYDROGENASE/REDUCTASE;
COMPND 3 CHAIN: A, B;
COMPND 4 EC: 1.-.-.-;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MYCOBACTERIUM ULCERANS;
SOURCE 3 ORGANISM_TAXID: 362242;
SOURCE 4 STRAIN: AGY99;
SOURCE 5 GENE: MUL_0987;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS SSGCID, SEATTLE STRUCTURAL GENOMICS CENTER FOR INFECTIOUS DISEASE,
KEYWDS 2 OXIDOREDUCTASE
EXPDTA X-RAY DIFFRACTION
AUTHOR SEATTLE STRUCTURAL GENOMICS CENTER FOR INFECTIOUS DISEASE (SSGCID)
REVDAT 4 13-SEP-23 3TL3 1 REMARK SEQADV
REVDAT 3 08-NOV-17 3TL3 1 REMARK
REVDAT 2 22-APR-15 3TL3 1 JRNL
REVDAT 1 07-SEP-11 3TL3 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. 1.85 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC
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) : 1.85
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 50.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.9
REMARK 3 NUMBER OF REFLECTIONS : 38188
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) : 0.179
REMARK 3 R VALUE (WORKING SET) : 0.177
REMARK 3 FREE R VALUE : 0.205
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 1914
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) : 1.85
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.90
REMARK 3 REFLECTION IN BIN (WORKING SET) : 2390
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 96.34
REMARK 3 BIN R VALUE (WORKING SET) : 0.2080
REMARK 3 BIN FREE R VALUE SET COUNT : 140
REMARK 3 BIN FREE R VALUE : 0.2780
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 3310
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 1
REMARK 3 SOLVENT ATOMS : 280
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 21.81
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.18000
REMARK 3 B22 (A**2) : -0.25000
REMARK 3 B33 (A**2) : 0.07000
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): 0.137
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.122
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.077
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 4.988
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.953
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.939
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 3389 ; 0.009 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 2159 ; 0.001 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 4624 ; 1.342 ; 1.975
REMARK 3 BOND ANGLES OTHERS (DEGREES): 5301 ; 0.914 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 479 ; 5.818 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 121 ;34.675 ;23.719
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 511 ;11.895 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 28 ;19.962 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 581 ; 0.073 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 3898 ; 0.006 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 646 ; 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 : 8
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 6 A 93
REMARK 3 ORIGIN FOR THE GROUP (A): -14.0987 -19.9726 -24.5804
REMARK 3 T TENSOR
REMARK 3 T11: 0.0688 T22: 0.0407
REMARK 3 T33: 0.0202 T12: 0.0090
REMARK 3 T13: 0.0095 T23: -0.0075
REMARK 3 L TENSOR
REMARK 3 L11: 1.4565 L22: 1.6732
REMARK 3 L33: 1.5234 L12: -0.0675
REMARK 3 L13: -0.0287 L23: 0.0029
REMARK 3 S TENSOR
REMARK 3 S11: 0.0297 S12: 0.0086 S13: 0.0214
REMARK 3 S21: -0.1840 S22: -0.0125 S23: -0.0732
REMARK 3 S31: 0.0442 S32: 0.0859 S33: -0.0171
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 94 A 135
REMARK 3 ORIGIN FOR THE GROUP (A): -16.8097 -6.9950 -21.9015
REMARK 3 T TENSOR
REMARK 3 T11: 0.1016 T22: 0.0774
REMARK 3 T33: 0.0636 T12: 0.0161
REMARK 3 T13: -0.0018 T23: 0.0212
REMARK 3 L TENSOR
REMARK 3 L11: 3.2388 L22: 1.5012
REMARK 3 L33: 0.8077 L12: 1.3973
REMARK 3 L13: -0.1681 L23: 0.4376
REMARK 3 S TENSOR
REMARK 3 S11: 0.1246 S12: 0.0849 S13: 0.0383
REMARK 3 S21: -0.0869 S22: -0.0382 S23: -0.0124
REMARK 3 S31: -0.0360 S32: 0.0047 S33: -0.0865
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 136 A 176
REMARK 3 ORIGIN FOR THE GROUP (A): -16.0406 -6.2607 -12.6614
REMARK 3 T TENSOR
REMARK 3 T11: 0.0811 T22: 0.0712
REMARK 3 T33: 0.0537 T12: 0.0023
REMARK 3 T13: 0.0021 T23: -0.0001
REMARK 3 L TENSOR
REMARK 3 L11: 3.2152 L22: 3.1830
REMARK 3 L33: 0.7572 L12: 2.5112
REMARK 3 L13: -0.5187 L23: -0.3580
REMARK 3 S TENSOR
REMARK 3 S11: 0.0381 S12: -0.0075 S13: 0.0755
REMARK 3 S21: -0.0083 S22: 0.0201 S23: -0.0975
REMARK 3 S31: -0.0869 S32: -0.0036 S33: -0.0582
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 177 A 248
REMARK 3 ORIGIN FOR THE GROUP (A): -8.5248 -14.7573 -8.4096
REMARK 3 T TENSOR
REMARK 3 T11: 0.0687 T22: 0.0917
REMARK 3 T33: 0.0526 T12: -0.0024
REMARK 3 T13: 0.0054 T23: 0.0109
REMARK 3 L TENSOR
REMARK 3 L11: 1.3681 L22: 0.9243
REMARK 3 L33: 1.4853 L12: 0.1520
REMARK 3 L13: 0.6139 L23: -0.0650
REMARK 3 S TENSOR
REMARK 3 S11: -0.0244 S12: 0.1307 S13: -0.0163
REMARK 3 S21: -0.0348 S22: -0.0159 S23: -0.1342
REMARK 3 S31: -0.0218 S32: 0.2464 S33: 0.0403
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 : B 5 B 90
REMARK 3 ORIGIN FOR THE GROUP (A): -14.0486 25.0517 -17.9617
REMARK 3 T TENSOR
REMARK 3 T11: 0.0864 T22: 0.0457
REMARK 3 T33: 0.0357 T12: -0.0067
REMARK 3 T13: -0.0126 T23: 0.0298
REMARK 3 L TENSOR
REMARK 3 L11: 1.4430 L22: 1.4668
REMARK 3 L33: 1.0962 L12: -0.0109
REMARK 3 L13: -0.0075 L23: -0.0927
REMARK 3 S TENSOR
REMARK 3 S11: -0.0340 S12: 0.0494 S13: 0.0613
REMARK 3 S21: -0.1488 S22: -0.0147 S23: 0.0258
REMARK 3 S31: -0.0750 S32: -0.0545 S33: 0.0487
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 : B 99 B 135
REMARK 3 ORIGIN FOR THE GROUP (A): -7.5853 13.3127 -18.3534
REMARK 3 T TENSOR
REMARK 3 T11: 0.0947 T22: 0.0749
REMARK 3 T33: 0.0485 T12: 0.0096
REMARK 3 T13: 0.0232 T23: 0.0090
REMARK 3 L TENSOR
REMARK 3 L11: 4.0930 L22: 3.8193
REMARK 3 L33: 1.6194 L12: 2.8707
REMARK 3 L13: 1.0688 L23: 1.0375
REMARK 3 S TENSOR
REMARK 3 S11: 0.0403 S12: 0.1391 S13: -0.1140
REMARK 3 S21: -0.1030 S22: 0.0263 S23: -0.1233
REMARK 3 S31: -0.0427 S32: 0.0652 S33: -0.0666
REMARK 3
REMARK 3 TLS GROUP : 7
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 136 B 174
REMARK 3 ORIGIN FOR THE GROUP (A): -14.5419 9.3794 -10.5983
REMARK 3 T TENSOR
REMARK 3 T11: 0.0622 T22: 0.0471
REMARK 3 T33: 0.0605 T12: -0.0016
REMARK 3 T13: 0.0066 T23: 0.0127
REMARK 3 L TENSOR
REMARK 3 L11: 1.2616 L22: 1.8205
REMARK 3 L33: 1.5427 L12: 0.6692
REMARK 3 L13: 0.7828 L23: 0.8038
REMARK 3 S TENSOR
REMARK 3 S11: 0.0291 S12: -0.0487 S13: -0.0279
REMARK 3 S21: -0.0798 S22: -0.0736 S23: 0.2250
REMARK 3 S31: 0.0928 S32: -0.0881 S33: 0.0445
REMARK 3
REMARK 3 TLS GROUP : 8
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 175 B 248
REMARK 3 ORIGIN FOR THE GROUP (A): -19.8288 15.7781 -4.5852
REMARK 3 T TENSOR
REMARK 3 T11: 0.0724 T22: 0.0713
REMARK 3 T33: 0.0447 T12: -0.0031
REMARK 3 T13: -0.0006 T23: 0.0004
REMARK 3 L TENSOR
REMARK 3 L11: 1.7176 L22: 0.6268
REMARK 3 L33: 1.1285 L12: 0.0149
REMARK 3 L13: -0.2936 L23: -0.0921
REMARK 3 S TENSOR
REMARK 3 S11: -0.0063 S12: 0.0834 S13: -0.0399
REMARK 3 S21: -0.0622 S22: -0.0057 S23: 0.0565
REMARK 3 S31: -0.0017 S32: -0.1516 S33: 0.0119
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : BABINET MODEL WITH 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:
REMARK 3 HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS
REMARK 3 U VALUES : WITH TLS ADDED
REMARK 4
REMARK 4 3TL3 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 30-AUG-11.
REMARK 100 THE DEPOSITION ID IS D_1000067611.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 11-JUN-11
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ALS
REMARK 200 BEAMLINE : 5.0.1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97
REMARK 200 MONOCHROMATOR : ASYMMETRIC CURVED CRYSTAL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 210
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO, HKL-2000
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK, HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 38385
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.850
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.5
REMARK 200 DATA REDUNDANCY : 4.800
REMARK 200 R MERGE (I) : 0.08200
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 11.7000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.85
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.88
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.0
REMARK 200 DATA REDUNDANCY IN SHELL : 4.90
REMARK 200 R MERGE FOR SHELL (I) : 0.43500
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 2.1.4
REMARK 200 STARTING MODEL: PDB ENTRY 1UAY
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 40.62
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.07
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 25.7 MG/ML MYULA.00554.A.A1 PS00974.
REMARK 280 0.1 M MMT BUFFER, PH 8.0, 25% PEG1500, CRYOPROTECTION 20%
REMARK 280 ETHYLENE GLYCOL , VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 289K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 2 21 21
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+1/2,-Z+1/2
REMARK 290 4555 -X,-Y+1/2,Z+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 36.62250
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 54.77650
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 36.62250
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 54.77650
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TETRAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 9770 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 33580 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -95.0 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 BIOMT1 2 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 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 -3
REMARK 465 PRO A -2
REMARK 465 GLY A -1
REMARK 465 SER A 0
REMARK 465 MET A 1
REMARK 465 GLU A 2
REMARK 465 ILE A 3
REMARK 465 ARG A 4
REMARK 465 ASP A 5
REMARK 465 GLY A 132
REMARK 465 PRO A 133
REMARK 465 ALA A 149
REMARK 465 PHE A 150
REMARK 465 ALA A 198
REMARK 465 SER A 199
REMARK 465 LEU A 200
REMARK 465 ARG A 249
REMARK 465 MET A 250
REMARK 465 ALA A 251
REMARK 465 PRO A 252
REMARK 465 ARG A 253
REMARK 465 GLY B -3
REMARK 465 PRO B -2
REMARK 465 GLY B -1
REMARK 465 SER B 0
REMARK 465 MET B 1
REMARK 465 GLU B 2
REMARK 465 ILE B 3
REMARK 465 ARG B 4
REMARK 465 VAL B 91
REMARK 465 LEU B 92
REMARK 465 SER B 93
REMARK 465 ARG B 94
REMARK 465 ASP B 95
REMARK 465 GLY B 96
REMARK 465 VAL B 97
REMARK 465 PHE B 98
REMARK 465 GLY B 132
REMARK 465 PRO B 133
REMARK 465 ARG B 249
REMARK 465 MET B 250
REMARK 465 ALA B 251
REMARK 465 PRO B 252
REMARK 465 ARG B 253
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 40 CG CD OE1 OE2
REMARK 470 ARG A 90 CG CD NE CZ NH1 NH2
REMARK 470 LEU A 92 CG CD1 CD2
REMARK 470 SER A 93 OG
REMARK 470 LEU A 100 CG CD1 CD2
REMARK 470 ASN A 134 CG OD1 ND2
REMARK 470 VAL A 147 CG1 CG2
REMARK 470 ASP A 151 CG OD1 OD2
REMARK 470 GLN A 156 CG CD OE1 NE2
REMARK 470 GLU A 202 CG CD OE1 OE2
REMARK 470 GLU A 203 CG CD OE1 OE2
REMARK 470 ARG A 205 CG CD NE CZ NH1 NH2
REMARK 470 SER A 207 OG
REMARK 470 LYS A 210 CG CD CE NZ
REMARK 470 ARG A 243 CG CD NE CZ NH1 NH2
REMARK 470 ASP B 5 CG OD1 OD2
REMARK 470 GLU B 40 CG CD OE1 OE2
REMARK 470 ARG B 90 CG CD NE CZ NH1 NH2
REMARK 470 LYS B 105 CG CD CE NZ
REMARK 470 ARG B 119 CG CD NE CZ NH1 NH2
REMARK 470 LYS B 127 CG CD CE NZ
REMARK 470 ASN B 134 CG OD1 ND2
REMARK 470 VAL B 147 CG1 CG2
REMARK 470 ASP B 151 CG OD1 OD2
REMARK 470 GLN B 211 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 OD1 ASP B 56 OG1 THR B 58 1.97
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 RES CSSEQI ATM2 DEVIATION
REMARK 500 HIS A 214 CG HIS A 214 CD2 0.058
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 SER A 146 130.79 26.01
REMARK 500 HIS A 214 122.02 -174.36
REMARK 500 ASP A 245 14.08 -154.94
REMARK 500 ASP B 245 17.05 -152.92
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 ASP B 5 ALA B 6 -36.26
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 NA B 254
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: MYULA.00554.A RELATED DB: TARGETDB
DBREF 3TL3 A 1 253 UNP A0PMN1 A0PMN1_MYCUA 1 253
DBREF 3TL3 B 1 253 UNP A0PMN1 A0PMN1_MYCUA 1 253
SEQADV 3TL3 GLY A -3 UNP A0PMN1 EXPRESSION TAG
SEQADV 3TL3 PRO A -2 UNP A0PMN1 EXPRESSION TAG
SEQADV 3TL3 GLY A -1 UNP A0PMN1 EXPRESSION TAG
SEQADV 3TL3 SER A 0 UNP A0PMN1 EXPRESSION TAG
SEQADV 3TL3 GLY B -3 UNP A0PMN1 EXPRESSION TAG
SEQADV 3TL3 PRO B -2 UNP A0PMN1 EXPRESSION TAG
SEQADV 3TL3 GLY B -1 UNP A0PMN1 EXPRESSION TAG
SEQADV 3TL3 SER B 0 UNP A0PMN1 EXPRESSION TAG
SEQRES 1 A 257 GLY PRO GLY SER MET GLU ILE ARG ASP ALA VAL ALA VAL
SEQRES 2 A 257 VAL THR GLY GLY ALA SER GLY LEU GLY LEU ALA THR THR
SEQRES 3 A 257 LYS ARG LEU LEU ASP ALA GLY ALA GLN VAL VAL VAL LEU
SEQRES 4 A 257 ASP ILE ARG GLY GLU ASP VAL VAL ALA ASP LEU GLY ASP
SEQRES 5 A 257 ARG ALA ARG PHE ALA ALA ALA ASP VAL THR ASP GLU ALA
SEQRES 6 A 257 ALA VAL ALA SER ALA LEU ASP LEU ALA GLU THR MET GLY
SEQRES 7 A 257 THR LEU ARG ILE VAL VAL ASN CYS ALA GLY THR GLY ASN
SEQRES 8 A 257 ALA ILE ARG VAL LEU SER ARG ASP GLY VAL PHE SER LEU
SEQRES 9 A 257 ALA ALA PHE ARG LYS ILE VAL ASP ILE ASN LEU VAL GLY
SEQRES 10 A 257 SER PHE ASN VAL LEU ARG LEU ALA ALA GLU ARG ILE ALA
SEQRES 11 A 257 LYS THR GLU PRO VAL GLY PRO ASN ALA GLU GLU ARG GLY
SEQRES 12 A 257 VAL ILE ILE ASN THR ALA SER VAL ALA ALA PHE ASP GLY
SEQRES 13 A 257 GLN ILE GLY GLN ALA ALA TYR SER ALA SER LYS GLY GLY
SEQRES 14 A 257 VAL VAL GLY MET THR LEU PRO ILE ALA ARG ASP LEU ALA
SEQRES 15 A 257 SER HIS ARG ILE ARG VAL MET THR ILE ALA PRO GLY LEU
SEQRES 16 A 257 PHE ASP THR PRO LEU LEU ALA SER LEU PRO GLU GLU ALA
SEQRES 17 A 257 ARG ALA SER LEU GLY LYS GLN VAL PRO HIS PRO SER ARG
SEQRES 18 A 257 LEU GLY ASN PRO ASP GLU TYR GLY ALA LEU ALA VAL HIS
SEQRES 19 A 257 ILE ILE GLU ASN PRO MET LEU ASN GLY GLU VAL ILE ARG
SEQRES 20 A 257 LEU ASP GLY ALA ILE ARG MET ALA PRO ARG
SEQRES 1 B 257 GLY PRO GLY SER MET GLU ILE ARG ASP ALA VAL ALA VAL
SEQRES 2 B 257 VAL THR GLY GLY ALA SER GLY LEU GLY LEU ALA THR THR
SEQRES 3 B 257 LYS ARG LEU LEU ASP ALA GLY ALA GLN VAL VAL VAL LEU
SEQRES 4 B 257 ASP ILE ARG GLY GLU ASP VAL VAL ALA ASP LEU GLY ASP
SEQRES 5 B 257 ARG ALA ARG PHE ALA ALA ALA ASP VAL THR ASP GLU ALA
SEQRES 6 B 257 ALA VAL ALA SER ALA LEU ASP LEU ALA GLU THR MET GLY
SEQRES 7 B 257 THR LEU ARG ILE VAL VAL ASN CYS ALA GLY THR GLY ASN
SEQRES 8 B 257 ALA ILE ARG VAL LEU SER ARG ASP GLY VAL PHE SER LEU
SEQRES 9 B 257 ALA ALA PHE ARG LYS ILE VAL ASP ILE ASN LEU VAL GLY
SEQRES 10 B 257 SER PHE ASN VAL LEU ARG LEU ALA ALA GLU ARG ILE ALA
SEQRES 11 B 257 LYS THR GLU PRO VAL GLY PRO ASN ALA GLU GLU ARG GLY
SEQRES 12 B 257 VAL ILE ILE ASN THR ALA SER VAL ALA ALA PHE ASP GLY
SEQRES 13 B 257 GLN ILE GLY GLN ALA ALA TYR SER ALA SER LYS GLY GLY
SEQRES 14 B 257 VAL VAL GLY MET THR LEU PRO ILE ALA ARG ASP LEU ALA
SEQRES 15 B 257 SER HIS ARG ILE ARG VAL MET THR ILE ALA PRO GLY LEU
SEQRES 16 B 257 PHE ASP THR PRO LEU LEU ALA SER LEU PRO GLU GLU ALA
SEQRES 17 B 257 ARG ALA SER LEU GLY LYS GLN VAL PRO HIS PRO SER ARG
SEQRES 18 B 257 LEU GLY ASN PRO ASP GLU TYR GLY ALA LEU ALA VAL HIS
SEQRES 19 B 257 ILE ILE GLU ASN PRO MET LEU ASN GLY GLU VAL ILE ARG
SEQRES 20 B 257 LEU ASP GLY ALA ILE ARG MET ALA PRO ARG
HET NA B 254 1
HETNAM NA SODIUM ION
FORMUL 3 NA NA 1+
FORMUL 4 HOH *280(H2 O)
HELIX 1 1 SER A 15 GLY A 29 1 15
HELIX 2 2 GLY A 39 LEU A 46 1 8
HELIX 3 3 ASP A 59 GLY A 74 1 16
HELIX 4 4 ALA A 83 THR A 85 5 3
HELIX 5 5 GLY A 86 ASP A 95 1 10
HELIX 6 6 SER A 99 ALA A 126 1 28
HELIX 7 7 GLY A 152 ALA A 178 1 27
HELIX 8 8 GLU A 202 GLN A 211 1 10
HELIX 9 9 ASN A 220 ASN A 234 1 15
HELIX 10 10 SER B 15 ALA B 28 1 14
HELIX 11 11 GLY B 39 LEU B 46 1 8
HELIX 12 12 ASP B 59 GLY B 74 1 16
HELIX 13 13 LEU B 100 LEU B 111 1 12
HELIX 14 14 LEU B 111 ALA B 126 1 16
HELIX 15 15 GLY B 155 ALA B 178 1 24
HELIX 16 16 THR B 194 ALA B 198 5 5
HELIX 17 17 PRO B 201 GLN B 211 1 11
HELIX 18 18 ASN B 220 ASN B 234 1 15
SHEET 1 A 7 ALA A 50 ALA A 54 0
SHEET 2 A 7 GLN A 31 ASP A 36 1 N VAL A 34 O ARG A 51
SHEET 3 A 7 VAL A 7 THR A 11 1 N ALA A 8 O VAL A 33
SHEET 4 A 7 LEU A 76 ASN A 81 1 O VAL A 80 N VAL A 9
SHEET 5 A 7 GLY A 139 THR A 144 1 O ILE A 142 N VAL A 79
SHEET 6 A 7 ILE A 182 PRO A 189 1 O ILE A 187 N ASN A 143
SHEET 7 A 7 VAL A 241 LEU A 244 1 O ILE A 242 N THR A 186
SHEET 1 B 7 ALA B 50 ALA B 54 0
SHEET 2 B 7 GLN B 31 ASP B 36 1 N VAL B 34 O ARG B 51
SHEET 3 B 7 VAL B 7 THR B 11 1 N ALA B 8 O VAL B 33
SHEET 4 B 7 LEU B 76 ASN B 81 1 O VAL B 80 N VAL B 9
SHEET 5 B 7 GLY B 139 THR B 144 1 O ILE B 142 N ASN B 81
SHEET 6 B 7 ILE B 182 PRO B 189 1 O MET B 185 N ASN B 143
SHEET 7 B 7 VAL B 241 LEU B 244 1 O ILE B 242 N THR B 186
CISPEP 1 HIS A 214 PRO A 215 0 -0.34
CISPEP 2 HIS B 214 PRO B 215 0 -0.18
SITE 1 AC1 6 GLU A 240 VAL A 241 GLU B 240 VAL B 241
SITE 2 AC1 6 HOH B 356 HOH B 358
CRYST1 54.946 73.245 109.553 90.00 90.00 90.00 P 2 21 21 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 0.018200 0.000000 0.000000 0.00000
SCALE2 0.000000 0.013653 0.000000 0.00000
SCALE3 0.000000 0.000000 0.009128 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
