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HEADER HYDROLASE 23-JUN-09 3HYS
TITLE STRUCTURE OF RV0554 FROM MYCOBACTERIUM TUBERCULOSIS COMPLEXED WITH
TITLE 2 MALONIC ACID
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PROTEIN RV0554, PUTATIVE BROMOPEROXIDASE;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: POSSIBLE PEROXIDASE BPOC (NON-HAEM PEROXIDASE);
COMPND 5 EC: 1.11.1.-;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MYCOBACTERIUM TUBERCULOSIS;
SOURCE 3 ORGANISM_TAXID: 1773;
SOURCE 4 GENE: BPOC, MT0580, RV0554;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS HYDROLASE, OXIDOREDUCTASE, PEROXIDASE
EXPDTA X-RAY DIFFRACTION
AUTHOR J.M.JOHNSTON,E.N.BAKER
REVDAT 1 02-JUN-10 3HYS 0
JRNL AUTH J.M.JOHNSTON,E.N.BAKER
JRNL TITL STRUCTURAL AND FUNCTIONAL ANALYSIS OF RV0554 FROM
JRNL TITL 2 MYCOBACTERIUM TUBERCULOSIS, TESTING A PUTATIVE ROLE IN
JRNL TITL 3 MENAQUINONE BIOSYNTHESIS
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.30 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.5.0072
REMARK 3 AUTHORS : MURSHUDOV,VAGIN,DODSON
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.30
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 50.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 3 NUMBER OF REFLECTIONS : 31347
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) : 0.169
REMARK 3 R VALUE (WORKING SET) : 0.166
REMARK 3 FREE R VALUE : 0.223
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 1579
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) : 2.30
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.36
REMARK 3 REFLECTION IN BIN (WORKING SET) : 2158
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 100.00
REMARK 3 BIN R VALUE (WORKING SET) : 0.1840
REMARK 3 BIN FREE R VALUE SET COUNT : 105
REMARK 3 BIN FREE R VALUE : 0.2390
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 4100
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 52
REMARK 3 SOLVENT ATOMS : 388
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 27.22
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.04000
REMARK 3 B22 (A**2) : -0.04000
REMARK 3 B33 (A**2) : 0.08000
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): 0.244
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.204
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): NULL
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): NULL
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.955
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.926
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 4255 ; 0.026 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 5785 ; 1.940 ; 1.963
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 540 ; 5.707 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 195 ;33.705 ;23.179
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 633 ;15.177 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 38 ;18.678 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 640 ; 0.139 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 3322 ; 0.011 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 2683 ; 1.120 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 4307 ; 1.951 ; 2.000
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1572 ; 3.379 ; 3.000
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1475 ; 5.052 ; 4.500
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 -13 A 43
REMARK 3 ORIGIN FOR THE GROUP (A): -0.3771 -48.1864 -11.8476
REMARK 3 T TENSOR
REMARK 3 T11: 0.0919 T22: 0.0746
REMARK 3 T33: 0.0646 T12: 0.0095
REMARK 3 T13: 0.0017 T23: -0.0131
REMARK 3 L TENSOR
REMARK 3 L11: 1.9454 L22: 0.7216
REMARK 3 L33: 0.3700 L12: 0.8072
REMARK 3 L13: -0.1846 L23: -0.3031
REMARK 3 S TENSOR
REMARK 3 S11: -0.0587 S12: 0.1241 S13: -0.2597
REMARK 3 S21: -0.1315 S22: 0.0287 S23: -0.0613
REMARK 3 S31: 0.1856 S32: -0.0351 S33: 0.0301
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 44 A 127
REMARK 3 ORIGIN FOR THE GROUP (A): -9.0478 -41.5078 -7.1605
REMARK 3 T TENSOR
REMARK 3 T11: 0.0357 T22: 0.0419
REMARK 3 T33: 0.0316 T12: -0.0126
REMARK 3 T13: 0.0128 T23: 0.0016
REMARK 3 L TENSOR
REMARK 3 L11: 0.8770 L22: 1.4015
REMARK 3 L33: 1.1004 L12: 0.0865
REMARK 3 L13: -0.2045 L23: 0.2978
REMARK 3 S TENSOR
REMARK 3 S11: 0.0007 S12: -0.0121 S13: 0.0108
REMARK 3 S21: -0.0080 S22: 0.0066 S23: 0.0629
REMARK 3 S31: -0.0358 S32: -0.0703 S33: -0.0072
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 128 A 187
REMARK 3 ORIGIN FOR THE GROUP (A): -11.4835 -34.2247 -26.0976
REMARK 3 T TENSOR
REMARK 3 T11: 0.0874 T22: 0.0825
REMARK 3 T33: 0.0916 T12: 0.0116
REMARK 3 T13: -0.0077 T23: -0.0134
REMARK 3 L TENSOR
REMARK 3 L11: 0.8539 L22: 0.8854
REMARK 3 L33: 1.3474 L12: 0.7522
REMARK 3 L13: -0.9970 L23: -1.0803
REMARK 3 S TENSOR
REMARK 3 S11: -0.0228 S12: 0.0605 S13: -0.0095
REMARK 3 S21: -0.0597 S22: 0.0136 S23: 0.0611
REMARK 3 S31: 0.0679 S32: -0.0563 S33: 0.0092
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 188 A 261
REMARK 3 ORIGIN FOR THE GROUP (A): -2.7473 -29.0427 -6.3596
REMARK 3 T TENSOR
REMARK 3 T11: 0.0831 T22: 0.0559
REMARK 3 T33: 0.0854 T12: -0.0057
REMARK 3 T13: -0.0067 T23: -0.0099
REMARK 3 L TENSOR
REMARK 3 L11: 1.1984 L22: 0.8367
REMARK 3 L33: 1.3807 L12: -0.0763
REMARK 3 L13: -0.3783 L23: -0.1874
REMARK 3 S TENSOR
REMARK 3 S11: 0.0025 S12: -0.0901 S13: 0.0118
REMARK 3 S21: 0.0901 S22: -0.0021 S23: -0.0344
REMARK 3 S31: -0.0300 S32: 0.0469 S33: -0.0005
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 2 B 8
REMARK 3 ORIGIN FOR THE GROUP (A): 14.4443 -46.9831 6.6995
REMARK 3 T TENSOR
REMARK 3 T11: 0.1416 T22: 0.1552
REMARK 3 T33: 0.1700 T12: 0.0022
REMARK 3 T13: -0.0022 T23: 0.0237
REMARK 3 L TENSOR
REMARK 3 L11: 5.1125 L22: 6.0666
REMARK 3 L33: 0.2956 L12: 0.3835
REMARK 3 L13: 0.2194 L23: -0.4575
REMARK 3 S TENSOR
REMARK 3 S11: -0.0213 S12: -0.4037 S13: 0.2846
REMARK 3 S21: 0.5133 S22: -0.1066 S23: 0.2186
REMARK 3 S31: 0.0650 S32: -0.1536 S33: 0.1279
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 9 B 122
REMARK 3 ORIGIN FOR THE GROUP (A): 26.5092 -45.5566 4.4353
REMARK 3 T TENSOR
REMARK 3 T11: 0.0909 T22: 0.0991
REMARK 3 T33: 0.0887 T12: 0.0071
REMARK 3 T13: 0.0039 T23: 0.0023
REMARK 3 L TENSOR
REMARK 3 L11: 0.7222 L22: 0.8732
REMARK 3 L33: 0.5778 L12: 0.2429
REMARK 3 L13: 0.1070 L23: 0.0242
REMARK 3 S TENSOR
REMARK 3 S11: 0.0209 S12: -0.1471 S13: -0.0573
REMARK 3 S21: 0.1745 S22: -0.0150 S23: -0.0094
REMARK 3 S31: 0.0527 S32: -0.0142 S33: -0.0058
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 123 B 169
REMARK 3 ORIGIN FOR THE GROUP (A): 28.1724 -26.8869 -9.0230
REMARK 3 T TENSOR
REMARK 3 T11: 0.0916 T22: 0.0964
REMARK 3 T33: 0.1242 T12: -0.0102
REMARK 3 T13: 0.0046 T23: 0.0129
REMARK 3 L TENSOR
REMARK 3 L11: 0.8626 L22: 0.8212
REMARK 3 L33: 2.3425 L12: 0.0490
REMARK 3 L13: 0.4356 L23: 0.0758
REMARK 3 S TENSOR
REMARK 3 S11: 0.0070 S12: 0.0856 S13: -0.0582
REMARK 3 S21: -0.0920 S22: -0.0385 S23: 0.0724
REMARK 3 S31: 0.0224 S32: -0.1138 S33: 0.0314
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 170 B 262
REMARK 3 ORIGIN FOR THE GROUP (A): 35.2823 -43.1363 -1.0628
REMARK 3 T TENSOR
REMARK 3 T11: 0.0859 T22: 0.0978
REMARK 3 T33: 0.0889 T12: -0.0060
REMARK 3 T13: 0.0017 T23: 0.0059
REMARK 3 L TENSOR
REMARK 3 L11: 0.3122 L22: 0.8663
REMARK 3 L33: 0.3515 L12: -0.0454
REMARK 3 L13: -0.2261 L23: 0.3473
REMARK 3 S TENSOR
REMARK 3 S11: 0.0008 S12: -0.0226 S13: 0.0213
REMARK 3 S21: 0.0348 S22: 0.0095 S23: -0.1272
REMARK 3 S31: -0.0147 S32: 0.0882 S33: -0.0103
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 3HYS COMPLIES WITH FORMAT V. 3.20, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 25-JUN-09.
REMARK 100 THE RCSB ID CODE IS RCSB053748.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 20-NOV-08
REMARK 200 TEMPERATURE (KELVIN) : 110
REMARK 200 PH : 4.92
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : AUSTRALIAN SYNCHROTRON
REMARK 200 BEAMLINE : MX1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : NULL
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 210
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL
REMARK 200 DATA SCALING SOFTWARE : HKL
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 31386
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.300
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 (%) : 99.8
REMARK 200 DATA REDUNDANCY : 8.100
REMARK 200 R MERGE (I) : 0.05900
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 35.6030
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.30
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.38
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 7.70
REMARK 200 R MERGE FOR SHELL (I) : 0.26700
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 7.600
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 53.41
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.64
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 95% (0.1M NAACETATE PH 4.92, 2% MPD,
REMARK 280 15% ETHYLENE GLYCOL) AND 5% MALONIC ACID 1.65M, VAPOR DIFFUSION,
REMARK 280 HANGING DROP, TEMPERATURE 291K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 41 21 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z+1/2
REMARK 290 3555 -Y+1/2,X+1/2,Z+1/4
REMARK 290 4555 Y+1/2,-X+1/2,Z+3/4
REMARK 290 5555 -X+1/2,Y+1/2,-Z+1/4
REMARK 290 6555 X+1/2,-Y+1/2,-Z+3/4
REMARK 290 7555 Y,X,-Z
REMARK 290 8555 -Y,-X,-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 67.53200
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 50.21750
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 50.21750
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 33.76600
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 50.21750
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 50.21750
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 101.29800
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 50.21750
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 50.21750
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 33.76600
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 50.21750
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 50.21750
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 101.29800
REMARK 290 SMTRY1 7 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 7 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 67.53200
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 5090 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 21940 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -34.0 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 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 -30
REMARK 465 SER A -29
REMARK 465 TYR A -28
REMARK 465 TYR A -27
REMARK 465 HIS A -26
REMARK 465 HIS A -25
REMARK 465 HIS A -24
REMARK 465 HIS A -23
REMARK 465 HIS A -22
REMARK 465 HIS A -21
REMARK 465 ASP A -20
REMARK 465 TYR A -19
REMARK 465 ASP A -18
REMARK 465 ILE A -17
REMARK 465 PRO A -16
REMARK 465 THR A -15
REMARK 465 THR A -14
REMARK 465 ALA A 262
REMARK 465 MET B -30
REMARK 465 SER B -29
REMARK 465 TYR B -28
REMARK 465 TYR B -27
REMARK 465 HIS B -26
REMARK 465 HIS B -25
REMARK 465 HIS B -24
REMARK 465 HIS B -23
REMARK 465 HIS B -22
REMARK 465 HIS B -21
REMARK 465 ASP B -20
REMARK 465 TYR B -19
REMARK 465 ASP B -18
REMARK 465 ILE B -17
REMARK 465 PRO B -16
REMARK 465 THR B -15
REMARK 465 THR B -14
REMARK 465 GLU B -13
REMARK 465 ASN B -12
REMARK 465 LEU B -11
REMARK 465 TYR B -10
REMARK 465 PHE B -9
REMARK 465 GLN B -8
REMARK 465 GLY B -7
REMARK 465 ALA B -6
REMARK 465 MET B -5
REMARK 465 ASP B -4
REMARK 465 PRO B -3
REMARK 465 GLU B -2
REMARK 465 PHE B -1
REMARK 465 ARG B 0
REMARK 465 VAL B 1
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 O HOH B 363 O HOH B 364 2.18
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 ASP B 8 CB - CG - OD1 ANGL. DEV. = 5.5 DEGREES
REMARK 500 ASP B 159 CB - CG - OD1 ANGL. DEV. = 6.6 DEGREES
REMARK 500 PRO B 216 C - N - CA ANGL. DEV. = 9.5 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 SER A 87 -118.72 51.08
REMARK 500 ALA A 100 56.35 -141.57
REMARK 500 ASP A 117 -174.98 -66.02
REMARK 500 LEU A 240 44.42 -93.18
REMARK 500 ASN B 48 154.91 -48.04
REMARK 500 SER B 87 -119.92 48.30
REMARK 500 LEU B 240 43.86 -95.34
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 NA A 267 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ALA A 223 O
REMARK 620 2 LEU A 226 O 78.6
REMARK 620 3 GLY A 229 O 90.1 99.7
REMARK 620 4 HOH A 308 O 87.6 165.6 84.2
REMARK 620 5 HOH A 309 O 161.3 94.0 74.1 100.4
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA B 267 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ALA B 223 O
REMARK 620 2 LEU B 226 O 83.9
REMARK 620 3 HOH B 282 O 95.7 178.3
REMARK 620 4 GLY B 229 O 88.2 97.2 81.1
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 MLA A 5188
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TRS A 263
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 264
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 265
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 266
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA A 267
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MLA B 5188
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 263
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 264
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 265
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 266
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA B 267
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: RCSB053538 RELATED DB: PDB
REMARK 900 RELATED ID: 3E3A RCSB048820 RELATED DB: PDB
DBREF 3HYS A 2 262 UNP O06420 O06420_MYCTU 2 262
DBREF 3HYS B 2 262 UNP O06420 O06420_MYCTU 2 262
SEQADV 3HYS MET A -30 UNP O06420 EXPRESSION TAG
SEQADV 3HYS SER A -29 UNP O06420 EXPRESSION TAG
SEQADV 3HYS TYR A -28 UNP O06420 EXPRESSION TAG
SEQADV 3HYS TYR A -27 UNP O06420 EXPRESSION TAG
SEQADV 3HYS HIS A -26 UNP O06420 EXPRESSION TAG
SEQADV 3HYS HIS A -25 UNP O06420 EXPRESSION TAG
SEQADV 3HYS HIS A -24 UNP O06420 EXPRESSION TAG
SEQADV 3HYS HIS A -23 UNP O06420 EXPRESSION TAG
SEQADV 3HYS HIS A -22 UNP O06420 EXPRESSION TAG
SEQADV 3HYS HIS A -21 UNP O06420 EXPRESSION TAG
SEQADV 3HYS ASP A -20 UNP O06420 EXPRESSION TAG
SEQADV 3HYS TYR A -19 UNP O06420 EXPRESSION TAG
SEQADV 3HYS ASP A -18 UNP O06420 EXPRESSION TAG
SEQADV 3HYS ILE A -17 UNP O06420 EXPRESSION TAG
SEQADV 3HYS PRO A -16 UNP O06420 EXPRESSION TAG
SEQADV 3HYS THR A -15 UNP O06420 EXPRESSION TAG
SEQADV 3HYS THR A -14 UNP O06420 EXPRESSION TAG
SEQADV 3HYS GLU A -13 UNP O06420 EXPRESSION TAG
SEQADV 3HYS ASN A -12 UNP O06420 EXPRESSION TAG
SEQADV 3HYS LEU A -11 UNP O06420 EXPRESSION TAG
SEQADV 3HYS TYR A -10 UNP O06420 EXPRESSION TAG
SEQADV 3HYS PHE A -9 UNP O06420 EXPRESSION TAG
SEQADV 3HYS GLN A -8 UNP O06420 EXPRESSION TAG
SEQADV 3HYS GLY A -7 UNP O06420 EXPRESSION TAG
SEQADV 3HYS ALA A -6 UNP O06420 EXPRESSION TAG
SEQADV 3HYS MET A -5 UNP O06420 EXPRESSION TAG
SEQADV 3HYS ASP A -4 UNP O06420 EXPRESSION TAG
SEQADV 3HYS PRO A -3 UNP O06420 EXPRESSION TAG
SEQADV 3HYS GLU A -2 UNP O06420 EXPRESSION TAG
SEQADV 3HYS PHE A -1 UNP O06420 EXPRESSION TAG
SEQADV 3HYS ARG A 0 UNP O06420 EXPRESSION TAG
SEQADV 3HYS VAL A 1 UNP O06420 EXPRESSION TAG
SEQADV 3HYS MET B -30 UNP O06420 EXPRESSION TAG
SEQADV 3HYS SER B -29 UNP O06420 EXPRESSION TAG
SEQADV 3HYS TYR B -28 UNP O06420 EXPRESSION TAG
SEQADV 3HYS TYR B -27 UNP O06420 EXPRESSION TAG
SEQADV 3HYS HIS B -26 UNP O06420 EXPRESSION TAG
SEQADV 3HYS HIS B -25 UNP O06420 EXPRESSION TAG
SEQADV 3HYS HIS B -24 UNP O06420 EXPRESSION TAG
SEQADV 3HYS HIS B -23 UNP O06420 EXPRESSION TAG
SEQADV 3HYS HIS B -22 UNP O06420 EXPRESSION TAG
SEQADV 3HYS HIS B -21 UNP O06420 EXPRESSION TAG
SEQADV 3HYS ASP B -20 UNP O06420 EXPRESSION TAG
SEQADV 3HYS TYR B -19 UNP O06420 EXPRESSION TAG
SEQADV 3HYS ASP B -18 UNP O06420 EXPRESSION TAG
SEQADV 3HYS ILE B -17 UNP O06420 EXPRESSION TAG
SEQADV 3HYS PRO B -16 UNP O06420 EXPRESSION TAG
SEQADV 3HYS THR B -15 UNP O06420 EXPRESSION TAG
SEQADV 3HYS THR B -14 UNP O06420 EXPRESSION TAG
SEQADV 3HYS GLU B -13 UNP O06420 EXPRESSION TAG
SEQADV 3HYS ASN B -12 UNP O06420 EXPRESSION TAG
SEQADV 3HYS LEU B -11 UNP O06420 EXPRESSION TAG
SEQADV 3HYS TYR B -10 UNP O06420 EXPRESSION TAG
SEQADV 3HYS PHE B -9 UNP O06420 EXPRESSION TAG
SEQADV 3HYS GLN B -8 UNP O06420 EXPRESSION TAG
SEQADV 3HYS GLY B -7 UNP O06420 EXPRESSION TAG
SEQADV 3HYS ALA B -6 UNP O06420 EXPRESSION TAG
SEQADV 3HYS MET B -5 UNP O06420 EXPRESSION TAG
SEQADV 3HYS ASP B -4 UNP O06420 EXPRESSION TAG
SEQADV 3HYS PRO B -3 UNP O06420 EXPRESSION TAG
SEQADV 3HYS GLU B -2 UNP O06420 EXPRESSION TAG
SEQADV 3HYS PHE B -1 UNP O06420 EXPRESSION TAG
SEQADV 3HYS ARG B 0 UNP O06420 EXPRESSION TAG
SEQADV 3HYS VAL B 1 UNP O06420 EXPRESSION TAG
SEQRES 1 A 293 MET SER TYR TYR HIS HIS HIS HIS HIS HIS ASP TYR ASP
SEQRES 2 A 293 ILE PRO THR THR GLU ASN LEU TYR PHE GLN GLY ALA MET
SEQRES 3 A 293 ASP PRO GLU PHE ARG VAL ILE ASN LEU ALA TYR ASP ASP
SEQRES 4 A 293 ASN GLY THR GLY ASP PRO VAL VAL PHE ILE ALA GLY ARG
SEQRES 5 A 293 GLY GLY ALA GLY ARG THR TRP HIS PRO HIS GLN VAL PRO
SEQRES 6 A 293 ALA PHE LEU ALA ALA GLY TYR ARG CYS ILE THR PHE ASP
SEQRES 7 A 293 ASN ARG GLY ILE GLY ALA THR GLU ASN ALA GLU GLY PHE
SEQRES 8 A 293 THR THR GLN THR MET VAL ALA ASP THR ALA ALA LEU ILE
SEQRES 9 A 293 GLU THR LEU ASP ILE ALA PRO ALA ARG VAL VAL GLY VAL
SEQRES 10 A 293 SER MET GLY ALA PHE ILE ALA GLN GLU LEU MET VAL VAL
SEQRES 11 A 293 ALA PRO GLU LEU VAL SER SER ALA VAL LEU MET ALA THR
SEQRES 12 A 293 ARG GLY ARG LEU ASP ARG ALA ARG GLN PHE PHE ASN LYS
SEQRES 13 A 293 ALA GLU ALA GLU LEU TYR ASP SER GLY VAL GLN LEU PRO
SEQRES 14 A 293 PRO THR TYR ASP ALA ARG ALA ARG LEU LEU GLU ASN PHE
SEQRES 15 A 293 SER ARG LYS THR LEU ASN ASP ASP VAL ALA VAL GLY ASP
SEQRES 16 A 293 TRP ILE ALA MET PHE SER MET TRP PRO ILE LYS SER THR
SEQRES 17 A 293 PRO GLY LEU ARG CYS GLN LEU ASP CYS ALA PRO GLN THR
SEQRES 18 A 293 ASN ARG LEU PRO ALA TYR ARG ASN ILE ALA ALA PRO VAL
SEQRES 19 A 293 LEU VAL ILE GLY PHE ALA ASP ASP VAL VAL THR PRO PRO
SEQRES 20 A 293 TYR LEU GLY ARG GLU VAL ALA ASP ALA LEU PRO ASN GLY
SEQRES 21 A 293 ARG TYR LEU GLN ILE PRO ASP ALA GLY HIS LEU GLY PHE
SEQRES 22 A 293 PHE GLU ARG PRO GLU ALA VAL ASN THR ALA MET LEU LYS
SEQRES 23 A 293 PHE PHE ALA SER VAL LYS ALA
SEQRES 1 B 293 MET SER TYR TYR HIS HIS HIS HIS HIS HIS ASP TYR ASP
SEQRES 2 B 293 ILE PRO THR THR GLU ASN LEU TYR PHE GLN GLY ALA MET
SEQRES 3 B 293 ASP PRO GLU PHE ARG VAL ILE ASN LEU ALA TYR ASP ASP
SEQRES 4 B 293 ASN GLY THR GLY ASP PRO VAL VAL PHE ILE ALA GLY ARG
SEQRES 5 B 293 GLY GLY ALA GLY ARG THR TRP HIS PRO HIS GLN VAL PRO
SEQRES 6 B 293 ALA PHE LEU ALA ALA GLY TYR ARG CYS ILE THR PHE ASP
SEQRES 7 B 293 ASN ARG GLY ILE GLY ALA THR GLU ASN ALA GLU GLY PHE
SEQRES 8 B 293 THR THR GLN THR MET VAL ALA ASP THR ALA ALA LEU ILE
SEQRES 9 B 293 GLU THR LEU ASP ILE ALA PRO ALA ARG VAL VAL GLY VAL
SEQRES 10 B 293 SER MET GLY ALA PHE ILE ALA GLN GLU LEU MET VAL VAL
SEQRES 11 B 293 ALA PRO GLU LEU VAL SER SER ALA VAL LEU MET ALA THR
SEQRES 12 B 293 ARG GLY ARG LEU ASP ARG ALA ARG GLN PHE PHE ASN LYS
SEQRES 13 B 293 ALA GLU ALA GLU LEU TYR ASP SER GLY VAL GLN LEU PRO
SEQRES 14 B 293 PRO THR TYR ASP ALA ARG ALA ARG LEU LEU GLU ASN PHE
SEQRES 15 B 293 SER ARG LYS THR LEU ASN ASP ASP VAL ALA VAL GLY ASP
SEQRES 16 B 293 TRP ILE ALA MET PHE SER MET TRP PRO ILE LYS SER THR
SEQRES 17 B 293 PRO GLY LEU ARG CYS GLN LEU ASP CYS ALA PRO GLN THR
SEQRES 18 B 293 ASN ARG LEU PRO ALA TYR ARG ASN ILE ALA ALA PRO VAL
SEQRES 19 B 293 LEU VAL ILE GLY PHE ALA ASP ASP VAL VAL THR PRO PRO
SEQRES 20 B 293 TYR LEU GLY ARG GLU VAL ALA ASP ALA LEU PRO ASN GLY
SEQRES 21 B 293 ARG TYR LEU GLN ILE PRO ASP ALA GLY HIS LEU GLY PHE
SEQRES 22 B 293 PHE GLU ARG PRO GLU ALA VAL ASN THR ALA MET LEU LYS
SEQRES 23 B 293 PHE PHE ALA SER VAL LYS ALA
HET MLA A5188 7
HET TRS A 263 8
HET EDO A 264 4
HET EDO A 265 4
HET EDO A 266 4
HET NA A 267 1
HET MLA B5188 7
HET EDO B 263 4
HET EDO B 264 4
HET EDO B 265 4
HET EDO B 266 4
HET NA B 267 1
HETNAM MLA MALONIC ACID
HETNAM TRS 2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL
HETNAM EDO 1,2-ETHANEDIOL
HETNAM NA SODIUM ION
HETSYN MLA DICARBOXYLIC ACID C3; PROPANEDIOLIC ACID;
HETSYN 2 MLA METAHNEDICARBOXYLIC ACID
HETSYN TRS TRIS BUFFER
HETSYN EDO ETHYLENE GLYCOL
FORMUL 3 MLA 2(C3 H4 O4)
FORMUL 4 TRS C4 H12 N O3 1+
FORMUL 5 EDO 7(C2 H6 O2)
FORMUL 8 NA 2(NA 1+)
FORMUL 15 HOH *388(H2 O)
HELIX 1 1 ALA A 24 HIS A 29 5 6
HELIX 2 2 GLN A 32 ALA A 39 1 8
HELIX 3 3 ILE A 51 GLU A 55 5 5
HELIX 4 4 THR A 61 ASP A 77 1 17
HELIX 5 5 SER A 87 ALA A 100 1 14
HELIX 6 6 ASP A 117 SER A 133 1 17
HELIX 7 7 PRO A 138 PHE A 151 1 14
HELIX 8 8 SER A 152 ASN A 157 1 6
HELIX 9 9 ASP A 158 TRP A 172 1 15
HELIX 10 10 THR A 177 LEU A 184 1 8
HELIX 11 11 ARG A 192 ARG A 197 1 6
HELIX 12 12 PRO A 215 LEU A 226 1 12
HELIX 13 13 LEU A 240 ARG A 245 1 6
HELIX 14 14 ARG A 245 VAL A 260 1 16
HELIX 15 15 ALA B 24 HIS B 29 5 6
HELIX 16 16 GLN B 32 ALA B 39 1 8
HELIX 17 17 ILE B 51 GLU B 55 5 5
HELIX 18 18 THR B 61 LEU B 76 1 16
HELIX 19 19 SER B 87 ALA B 100 1 14
HELIX 20 20 ASP B 117 SER B 133 1 17
HELIX 21 21 PRO B 138 PHE B 151 1 14
HELIX 22 22 SER B 152 ASN B 157 1 6
HELIX 23 23 ASP B 158 TRP B 172 1 15
HELIX 24 24 THR B 177 LEU B 184 1 8
HELIX 25 25 ARG B 192 ARG B 197 1 6
HELIX 26 26 PRO B 215 LEU B 226 1 12
HELIX 27 27 LEU B 240 ARG B 245 1 6
HELIX 28 28 ARG B 245 VAL B 260 1 16
SHEET 1 A 8 LEU A -11 MET A -5 0
SHEET 2 A 8 VAL A 1 ASN A 9 -1 O ILE A 2 N GLY A -7
SHEET 3 A 8 TYR A 41 PHE A 46 -1 O THR A 45 N ASP A 7
SHEET 4 A 8 ASP A 13 ILE A 18 1 N VAL A 15 O ARG A 42
SHEET 5 A 8 ALA A 81 VAL A 86 1 O ARG A 82 N VAL A 16
SHEET 6 A 8 VAL A 104 MET A 110 1 O MET A 110 N GLY A 85
SHEET 7 A 8 VAL A 203 PHE A 208 1 O ILE A 206 N LEU A 109
SHEET 8 A 8 GLY A 229 ILE A 234 1 O ARG A 230 N VAL A 205
SHEET 1 B 7 TYR B 6 ASN B 9 0
SHEET 2 B 7 ARG B 42 PHE B 46 -1 O THR B 45 N ASP B 7
SHEET 3 B 7 PRO B 14 ILE B 18 1 N VAL B 15 O ARG B 42
SHEET 4 B 7 ALA B 81 VAL B 86 1 O VAL B 84 N ILE B 18
SHEET 5 B 7 VAL B 104 MET B 110 1 O MET B 110 N GLY B 85
SHEET 6 B 7 VAL B 203 PHE B 208 1 O ILE B 206 N LEU B 109
SHEET 7 B 7 GLY B 229 ILE B 234 1 O ILE B 234 N GLY B 207
LINK O ALA A 223 NA NA A 267 1555 1555 2.43
LINK O LEU A 226 NA NA A 267 1555 1555 2.42
LINK O GLY A 229 NA NA A 267 1555 1555 2.77
LINK O ALA B 223 NA NA B 267 1555 1555 2.44
LINK O LEU B 226 NA NA B 267 1555 1555 2.34
LINK NA NA A 267 O HOH A 308 1555 1555 2.71
LINK NA NA A 267 O HOH A 309 1555 1555 2.22
LINK NA NA B 267 O HOH B 282 1555 1555 2.39
LINK O GLY B 229 NA NA B 267 1555 1555 3.04
CISPEP 1 ALA A 79 PRO A 80 0 -3.77
CISPEP 2 ALA B 79 PRO B 80 0 -7.75
SITE 1 AC1 6 THR A 27 ARG A 146 TRP A 172 LEU A 240
SITE 2 AC1 6 EDO A 264 HOH A 405
SITE 1 AC2 8 GLY A 20 ARG A 21 SER A 87 MET A 88
SITE 2 AC2 8 ARG A 113 GLN A 183 LEU A 184 HOH A 476
SITE 1 AC3 4 ARG A 21 GLY A 23 HOH A 400 MLA A5188
SITE 1 AC4 3 ALA A 161 ASP A 164 TRP A 165
SITE 1 AC5 6 PHE A 46 ASN A 48 ARG A 49 MET A 65
SITE 2 AC5 6 ASP A 68 THR A 69
SITE 1 AC6 5 ALA A 223 LEU A 226 GLY A 229 HOH A 308
SITE 2 AC6 5 HOH A 309
SITE 1 AC7 10 GLY B 20 ARG B 21 SER B 87 MET B 88
SITE 2 AC7 10 ARG B 120 PHE B 123 HIS B 239 HOH B 300
SITE 3 AC7 10 HOH B 301 HOH B 302
SITE 1 AC8 3 ARG B 146 HOH B 307 HOH B 417
SITE 1 AC9 7 GLY B 22 ALA B 24 ARG B 26 TRP B 172
SITE 2 AC9 7 PRO B 173 HOH B 417 HOH B 418
SITE 1 BC1 3 ALA B 119 HOH B 295 HOH B 296
SITE 1 BC2 3 GLY B 12 ASP B 13 GLY B 40
SITE 1 BC3 5 ALA B 223 ASP B 224 LEU B 226 GLY B 229
SITE 2 BC3 5 HOH B 282
CRYST1 100.435 100.435 135.064 90.00 90.00 90.00 P 41 21 2 16
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 0.009957 0.000000 0.000000 0.00000
SCALE2 0.000000 0.009957 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007404 0.00000
END |