HEADER TRANSFERASE 27-JAN-06 2FUM
TITLE CATALYTIC DOMAIN OF PROTEIN KINASE PKNB FROM MYCOBACTERIUM
TITLE 2 TUBERCULOSIS IN COMPLEX WITH MITOXANTRONE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PROBABLE SERINE/THREONINE-PROTEIN KINASE PKNB;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 FRAGMENT: CATALYTIC DOMAIN;
COMPND 5 SYNONYM: PKNB SER/THR KINASE;
COMPND 6 EC: 2.7.1.37;
COMPND 7 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MYCOBACTERIUM TUBERCULOSIS H37RV;
SOURCE 3 ORGANISM_TAXID: 83332;
SOURCE 4 STRAIN: H37RV;
SOURCE 5 GENE: PKNB;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21 (DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET28
KEYWDS PROTEIN KINASE-INHIBITOR COMPLEX, TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR A.WEHENKEL,P.M.ALZARI
REVDAT 4 25-OCT-23 2FUM 1 REMARK SEQADV HETSYN
REVDAT 3 13-JUL-11 2FUM 1 VERSN
REVDAT 2 24-FEB-09 2FUM 1 VERSN
REVDAT 1 01-AUG-06 2FUM 0
JRNL AUTH A.WEHENKEL,P.FERNANDEZ,M.BELLINZONI,V.CATHERINOT,N.BARILONE,
JRNL AUTH 2 G.LABESSE,M.JACKSON,P.M.ALZARI
JRNL TITL THE STRUCTURE OF PKNB IN COMPLEX WITH MITOXANTRONE, AN
JRNL TITL 2 ATP-COMPETITIVE INHIBITOR, SUGGESTS A MODE OF PROTEIN KINASE
JRNL TITL 3 REGULATION IN MYCOBACTERIA
JRNL REF FEBS LETT. V. 580 3018 2006
JRNL REFN ISSN 0014-5793
JRNL PMID 16674948
JRNL DOI 10.1016/J.FEBSLET.2006.04.046
REMARK 2
REMARK 2 RESOLUTION. 2.89 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.2.0005
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) : 2.89
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 69.84
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 68.1
REMARK 3 NUMBER OF REFLECTIONS : 26685
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) : 0.221
REMARK 3 R VALUE (WORKING SET) : 0.218
REMARK 3 FREE R VALUE : 0.278
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 1426
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) : 2.89
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.97
REMARK 3 REFLECTION IN BIN (WORKING SET) : 217
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 7.81
REMARK 3 BIN R VALUE (WORKING SET) : 0.3410
REMARK 3 BIN FREE R VALUE SET COUNT : 17
REMARK 3 BIN FREE R VALUE : 0.5280
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 7870
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 128
REMARK 3 SOLVENT ATOMS : 0
REMARK 3
REMARK 3 B VALUES.
REMARK 3 B VALUE TYPE : LIKELY RESIDUAL
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 79.78
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 3.91000
REMARK 3 B22 (A**2) : 3.91000
REMARK 3 B33 (A**2) : -7.82000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): NULL
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.509
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.412
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 53.161
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.938
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.905
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 8171 ; 0.015 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 11143 ; 1.737 ; 1.980
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 1029 ; 7.212 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 366 ;39.069 ;23.579
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1223 ;24.322 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 66 ;20.695 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1256 ; 0.127 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 6315 ; 0.005 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 4512 ; 0.266 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 5666 ; 0.325 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 384 ; 0.182 ; 0.200
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): 49 ; 0.244 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 4 ; 0.181 ; 0.200
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): 5272 ; 0.319 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 8336 ; 0.566 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 3497 ; 1.140 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 2807 ; 2.074 ; 4.500
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 : 2
REMARK 3
REMARK 3 NCS GROUP NUMBER : 1
REMARK 3 CHAIN NAMES : A B
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 2
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 A 3 A 163 2
REMARK 3 1 B 3 B 163 2
REMARK 3 2 A 178 A 277 2
REMARK 3 2 B 178 B 277 2
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 TIGHT POSITIONAL 1 A (A): 1028 ; 0.09 ; 0.05
REMARK 3 MEDIUM POSITIONAL 1 A (A): 925 ; 0.68 ; 0.50
REMARK 3 TIGHT THERMAL 1 A (A**2): 1028 ; 0.10 ; 0.50
REMARK 3 MEDIUM THERMAL 1 A (A**2): 925 ; 0.62 ; 2.00
REMARK 3
REMARK 3 NCS GROUP NUMBER : 2
REMARK 3 CHAIN NAMES : C D
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 2
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 C 3 C 157 2
REMARK 3 1 D 3 D 157 2
REMARK 3 2 C 180 C 277 2
REMARK 3 2 D 180 D 277 2
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 TIGHT POSITIONAL 2 C (A): 1000 ; 0.07 ; 0.05
REMARK 3 MEDIUM POSITIONAL 2 C (A): 898 ; 0.63 ; 0.50
REMARK 3 TIGHT THERMAL 2 C (A**2): 1000 ; 0.08 ; 0.50
REMARK 3 MEDIUM THERMAL 2 C (A**2): 898 ; 0.50 ; 2.00
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 3 A 96
REMARK 3 ORIGIN FOR THE GROUP (A): 67.0125 -6.5450 -29.4674
REMARK 3 T TENSOR
REMARK 3 T11: 0.1344 T22: 0.1291
REMARK 3 T33: -0.4018 T12: 0.1484
REMARK 3 T13: 0.0184 T23: -0.0342
REMARK 3 L TENSOR
REMARK 3 L11: 4.4687 L22: 6.2814
REMARK 3 L33: 8.5972 L12: -1.6504
REMARK 3 L13: 0.1288 L23: -1.4013
REMARK 3 S TENSOR
REMARK 3 S11: -0.0472 S12: 0.0765 S13: -0.2787
REMARK 3 S21: 0.5686 S22: 0.1803 S23: -0.6401
REMARK 3 S31: 0.1763 S32: 1.1117 S33: -0.1330
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 97 A 277
REMARK 3 ORIGIN FOR THE GROUP (A): 44.7911 4.5138 -19.3964
REMARK 3 T TENSOR
REMARK 3 T11: -0.0275 T22: 0.0082
REMARK 3 T33: -0.2955 T12: 0.1858
REMARK 3 T13: 0.0849 T23: 0.0606
REMARK 3 L TENSOR
REMARK 3 L11: 5.8702 L22: 4.2298
REMARK 3 L33: 9.2680 L12: 0.9899
REMARK 3 L13: -0.7276 L23: 0.3096
REMARK 3 S TENSOR
REMARK 3 S11: 0.4650 S12: -0.2260 S13: 0.4728
REMARK 3 S21: -0.0149 S22: -0.3419 S23: 0.4071
REMARK 3 S31: -0.4227 S32: -1.0215 S33: -0.1232
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 : B 3 B 96
REMARK 3 ORIGIN FOR THE GROUP (A): 64.8508 -9.9255 -50.3222
REMARK 3 T TENSOR
REMARK 3 T11: 0.1330 T22: 0.1710
REMARK 3 T33: -0.4050 T12: 0.2421
REMARK 3 T13: -0.0633 T23: 0.0686
REMARK 3 L TENSOR
REMARK 3 L11: 3.4415 L22: 8.7188
REMARK 3 L33: 8.9766 L12: -0.6644
REMARK 3 L13: -2.5180 L23: 1.8398
REMARK 3 S TENSOR
REMARK 3 S11: 0.0886 S12: 0.3725 S13: -0.3847
REMARK 3 S21: -0.3879 S22: 0.2819 S23: -0.6441
REMARK 3 S31: 0.3904 S32: 1.0653 S33: -0.3704
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 : B 97 B 278
REMARK 3 ORIGIN FOR THE GROUP (A): 50.8413 10.5132 -61.1760
REMARK 3 T TENSOR
REMARK 3 T11: 0.2017 T22: -0.0042
REMARK 3 T33: -0.2790 T12: 0.3196
REMARK 3 T13: 0.0557 T23: 0.1167
REMARK 3 L TENSOR
REMARK 3 L11: 2.5792 L22: 7.0844
REMARK 3 L33: 9.0768 L12: 0.8157
REMARK 3 L13: 0.5078 L23: -0.9319
REMARK 3 S TENSOR
REMARK 3 S11: -0.0210 S12: -0.1885 S13: 0.2804
REMARK 3 S21: -0.0756 S22: 0.3042 S23: 0.4925
REMARK 3 S31: -1.4792 S32: -0.4772 S33: -0.2832
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 : C 3 C 96
REMARK 3 ORIGIN FOR THE GROUP (A): 82.2391 -52.4819 -16.0674
REMARK 3 T TENSOR
REMARK 3 T11: 0.5581 T22: -0.2236
REMARK 3 T33: 0.1414 T12: 0.2031
REMARK 3 T13: 0.0817 T23: 0.0867
REMARK 3 L TENSOR
REMARK 3 L11: 13.0911 L22: 5.6346
REMARK 3 L33: 8.1272 L12: -2.7748
REMARK 3 L13: 1.9719 L23: -1.5368
REMARK 3 S TENSOR
REMARK 3 S11: -0.2334 S12: -1.2927 S13: 0.4817
REMARK 3 S21: 0.9614 S22: 0.2270 S23: 0.1945
REMARK 3 S31: -0.9569 S32: -0.0804 S33: 0.0064
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 : C 97 C 278
REMARK 3 ORIGIN FOR THE GROUP (A): 67.1133 -39.6418 -35.1497
REMARK 3 T TENSOR
REMARK 3 T11: 0.4184 T22: 0.0340
REMARK 3 T33: 0.0570 T12: 0.2856
REMARK 3 T13: -0.0971 T23: 0.0270
REMARK 3 L TENSOR
REMARK 3 L11: 3.2682 L22: 8.4385
REMARK 3 L33: 3.8236 L12: -2.9604
REMARK 3 L13: -0.7250 L23: -0.9037
REMARK 3 S TENSOR
REMARK 3 S11: 0.3024 S12: 0.3950 S13: -0.3130
REMARK 3 S21: -0.5721 S22: -0.4089 S23: 0.3902
REMARK 3 S31: -0.1276 S32: -0.3518 S33: 0.1065
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 : D 3 D 96
REMARK 3 ORIGIN FOR THE GROUP (A): 78.8837 -73.5430 -17.9286
REMARK 3 T TENSOR
REMARK 3 T11: 0.4906 T22: 0.1293
REMARK 3 T33: 0.7230 T12: 0.0382
REMARK 3 T13: 0.1094 T23: 0.2388
REMARK 3 L TENSOR
REMARK 3 L11: 5.8330 L22: 8.2540
REMARK 3 L33: 10.7647 L12: -1.2247
REMARK 3 L13: -0.7978 L23: 3.0378
REMARK 3 S TENSOR
REMARK 3 S11: -0.2015 S12: -1.2362 S13: -1.6227
REMARK 3 S21: 0.7915 S22: 0.1289 S23: 0.6833
REMARK 3 S31: 1.3560 S32: 0.0420 S33: 0.0726
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 : D 97 D 277
REMARK 3 ORIGIN FOR THE GROUP (A): 78.5643 -79.9137 -44.4222
REMARK 3 T TENSOR
REMARK 3 T11: 0.7465 T22: -0.0030
REMARK 3 T33: 0.4742 T12: 0.0775
REMARK 3 T13: -0.3271 T23: -0.0892
REMARK 3 L TENSOR
REMARK 3 L11: 3.5649 L22: 4.9495
REMARK 3 L33: 7.3434 L12: 0.4624
REMARK 3 L13: -2.2931 L23: 1.2909
REMARK 3 S TENSOR
REMARK 3 S11: -0.1703 S12: 0.6221 S13: -0.4317
REMARK 3 S21: -0.8218 S22: -0.0993 S23: 0.8760
REMARK 3 S31: 0.1620 S32: -0.7398 S33: 0.2695
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: THE DATA IS HIGHLY ANISOTROPIC (2.89 A
REMARK 3 RESOLUTION LIMIT ALONG THE C* AXIS, BUT ONLY 3.5 A ALONG THE A*
REMARK 3 AND B* AXES), ACCOUNTING FOR THE POOR DATA COMPLETENESS AT THE
REMARK 3 HIGHER RESOLUTION SHELLS (DATA IS 99% COMPLETE AT 3.49 A, 45% IN
REMARK 3 THE 3.49-3.21 A SHELL, AND ONLY 16% IN THE 3.21-2.89 A SHELL.
REMARK 4
REMARK 4 2FUM COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 03-FEB-06.
REMARK 100 THE DEPOSITION ID IS D_1000036331.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 10-MAR-05
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 5.6
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : ID14-3
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.931
REMARK 200 MONOCHROMATOR : DIAMOND (111), GE(220)
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : CCP4 (SCALA)
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 28195
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.890
REMARK 200 RESOLUTION RANGE LOW (A) : 69.840
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 1.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 63.5
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.89
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.21
REMARK 200 COMPLETENESS FOR SHELL (%) : 16.0
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: PDB ENTRY 1O6Y
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 64.05
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.42
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.2M NAACETATE 50MM NACACODYLATE, PH
REMARK 280 5.6, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 291K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 43 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+3/4
REMARK 290 4555 Y+1/2,-X+1/2,Z+1/4
REMARK 290 5555 -X+1/2,Y+1/2,-Z+3/4
REMARK 290 6555 X+1/2,-Y+1/2,-Z+1/4
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 130.17350
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 58.43150
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 58.43150
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 195.26025
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 58.43150
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 58.43150
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 65.08675
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 58.43150
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 58.43150
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 195.26025
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 58.43150
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 58.43150
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 65.08675
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 130.17350
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3, 4
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: MONOMERIC
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
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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: 3
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C
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: 4
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 MET A -19
REMARK 465 GLY A -18
REMARK 465 SER A -17
REMARK 465 SER A -16
REMARK 465 HIS A -15
REMARK 465 HIS A -14
REMARK 465 HIS A -13
REMARK 465 HIS A -12
REMARK 465 HIS A -11
REMARK 465 HIS A -10
REMARK 465 SER A -9
REMARK 465 SER A -8
REMARK 465 GLY A -7
REMARK 465 LEU A -6
REMARK 465 VAL A -5
REMARK 465 PRO A -4
REMARK 465 ARG A -3
REMARK 465 GLY A -2
REMARK 465 SER A -1
REMARK 465 HIS A 0
REMARK 465 MET A 1
REMARK 465 THR A 2
REMARK 465 SER A 166
REMARK 465 GLY A 167
REMARK 465 ASN A 168
REMARK 465 SER A 169
REMARK 465 VAL A 170
REMARK 465 THR A 171
REMARK 465 GLN A 172
REMARK 465 THR A 173
REMARK 465 ALA A 174
REMARK 465 ALA A 175
REMARK 465 VAL A 176
REMARK 465 ILE A 177
REMARK 465 ASN A 278
REMARK 465 GLY A 279
REMARK 465 MET B -19
REMARK 465 GLY B -18
REMARK 465 SER B -17
REMARK 465 SER B -16
REMARK 465 HIS B -15
REMARK 465 HIS B -14
REMARK 465 HIS B -13
REMARK 465 HIS B -12
REMARK 465 HIS B -11
REMARK 465 HIS B -10
REMARK 465 SER B -9
REMARK 465 SER B -8
REMARK 465 GLY B -7
REMARK 465 LEU B -6
REMARK 465 VAL B -5
REMARK 465 PRO B -4
REMARK 465 ARG B -3
REMARK 465 GLY B -2
REMARK 465 SER B -1
REMARK 465 HIS B 0
REMARK 465 MET B 1
REMARK 465 THR B 2
REMARK 465 ALA B 164
REMARK 465 ASP B 165
REMARK 465 SER B 166
REMARK 465 GLY B 167
REMARK 465 ASN B 168
REMARK 465 SER B 169
REMARK 465 VAL B 170
REMARK 465 THR B 171
REMARK 465 GLN B 172
REMARK 465 THR B 173
REMARK 465 ALA B 174
REMARK 465 ALA B 175
REMARK 465 VAL B 176
REMARK 465 ILE B 177
REMARK 465 GLY B 279
REMARK 465 MET C -19
REMARK 465 GLY C -18
REMARK 465 SER C -17
REMARK 465 SER C -16
REMARK 465 HIS C -15
REMARK 465 HIS C -14
REMARK 465 HIS C -13
REMARK 465 HIS C -12
REMARK 465 HIS C -11
REMARK 465 HIS C -10
REMARK 465 SER C -9
REMARK 465 SER C -8
REMARK 465 GLY C -7
REMARK 465 LEU C -6
REMARK 465 VAL C -5
REMARK 465 PRO C -4
REMARK 465 ARG C -3
REMARK 465 GLY C -2
REMARK 465 SER C -1
REMARK 465 HIS C 0
REMARK 465 MET C 1
REMARK 465 THR C 2
REMARK 465 GLY C 158
REMARK 465 ILE C 159
REMARK 465 ALA C 160
REMARK 465 ARG C 161
REMARK 465 ALA C 162
REMARK 465 ILE C 163
REMARK 465 ALA C 164
REMARK 465 ASP C 165
REMARK 465 SER C 166
REMARK 465 GLY C 167
REMARK 465 ASN C 168
REMARK 465 SER C 169
REMARK 465 VAL C 170
REMARK 465 THR C 171
REMARK 465 GLN C 172
REMARK 465 THR C 173
REMARK 465 ALA C 174
REMARK 465 ALA C 175
REMARK 465 VAL C 176
REMARK 465 ILE C 177
REMARK 465 GLY C 178
REMARK 465 THR C 179
REMARK 465 GLY C 279
REMARK 465 MET D -19
REMARK 465 GLY D -18
REMARK 465 SER D -17
REMARK 465 SER D -16
REMARK 465 HIS D -15
REMARK 465 HIS D -14
REMARK 465 HIS D -13
REMARK 465 HIS D -12
REMARK 465 HIS D -11
REMARK 465 HIS D -10
REMARK 465 SER D -9
REMARK 465 SER D -8
REMARK 465 GLY D -7
REMARK 465 LEU D -6
REMARK 465 VAL D -5
REMARK 465 PRO D -4
REMARK 465 ARG D -3
REMARK 465 GLY D -2
REMARK 465 SER D -1
REMARK 465 HIS D 0
REMARK 465 MET D 1
REMARK 465 THR D 2
REMARK 465 ALA D 160
REMARK 465 ARG D 161
REMARK 465 ALA D 162
REMARK 465 ILE D 163
REMARK 465 ALA D 164
REMARK 465 ASP D 165
REMARK 465 SER D 166
REMARK 465 GLY D 167
REMARK 465 ASN D 168
REMARK 465 SER D 169
REMARK 465 VAL D 170
REMARK 465 THR D 171
REMARK 465 GLN D 172
REMARK 465 THR D 173
REMARK 465 ALA D 174
REMARK 465 ALA D 175
REMARK 465 VAL D 176
REMARK 465 ASN D 278
REMARK 465 GLY D 279
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 43 CG CD NE CZ NH1 NH2
REMARK 470 ARG A 55 CG CD NE CZ NH1 NH2
REMARK 470 GLU A 81 CG CD OE1 OE2
REMARK 470 LYS A 113 CG CD CE NZ
REMARK 470 ARG A 161 CG CD NE CZ NH1 NH2
REMARK 470 ARG B 43 CG CD NE CZ NH1 NH2
REMARK 470 LYS B 113 CG CD CE NZ
REMARK 470 ARG B 161 CG CD NE CZ NH1 NH2
REMARK 470 GLU B 231 CG CD OE1 OE2
REMARK 470 GLU B 241 CG CD OE1 OE2
REMARK 470 ARG C 43 CG CD NE CZ NH1 NH2
REMARK 470 ARG C 55 CG CD NE CZ NH1 NH2
REMARK 470 ARG C 57 CG CD NE CZ NH1 NH2
REMARK 470 ARG C 58 CG CD NE CZ NH1 NH2
REMARK 470 GLU C 81 CG CD OE1 OE2
REMARK 470 LYS C 113 CG CD CE NZ
REMARK 470 PHE D 19 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 ARG D 43 CG CD NE CZ NH1 NH2
REMARK 470 ARG D 55 CG CD NE CZ NH1 NH2
REMARK 470 ARG D 57 CG CD NE CZ NH1 NH2
REMARK 470 GLU D 81 CG CD OE1 OE2
REMARK 470 GLU D 241 CG CD OE1 OE2
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 NH2 ARG A 10 OD1 ASP B 76 2.05
REMARK 500 O GLU B 231 NZ LYS B 257 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 THR A 179 N - CA - C ANGL. DEV. = 20.6 DEGREES
REMARK 500 THR B 179 N - CA - C ANGL. DEV. = 17.9 DEGREES
REMARK 500 ALA B 180 N - CA - C ANGL. DEV. = 21.1 DEGREES
REMARK 500 LEU B 183 CB - CG - CD1 ANGL. DEV. = -10.7 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 8 4.40 57.57
REMARK 500 ASP A 9 -18.94 85.82
REMARK 500 MET A 22 40.84 -55.23
REMARK 500 HIS A 34 64.60 39.20
REMARK 500 ALA A 44 -60.78 124.92
REMARK 500 ALA A 65 4.52 -66.75
REMARK 500 ASP A 76 150.93 171.23
REMARK 500 ALA A 84 43.21 -85.31
REMARK 500 THR A 111 139.01 -39.63
REMARK 500 ASP A 138 38.44 -150.26
REMARK 500 ASP A 156 61.28 70.25
REMARK 500 PHE A 157 38.78 -74.95
REMARK 500 ALA A 162 -169.88 -67.49
REMARK 500 THR A 179 -74.56 79.05
REMARK 500 ALA A 180 -77.49 96.46
REMARK 500 SER A 192 135.72 -38.68
REMARK 500 HIS A 240 113.27 -176.80
REMARK 500 GLU A 241 177.93 -51.03
REMARK 500 SER B 8 11.77 54.18
REMARK 500 ASP B 9 -4.33 72.25
REMARK 500 MET B 22 -4.88 -2.00
REMARK 500 ALA B 44 -64.07 133.51
REMARK 500 SER B 51 -43.79 -26.17
REMARK 500 ASP B 76 149.78 173.83
REMARK 500 GLU B 93 133.40 -39.98
REMARK 500 LEU B 100 -38.13 -35.03
REMARK 500 ASP B 138 32.61 -158.43
REMARK 500 THR B 149 19.76 -69.10
REMARK 500 PHE B 157 46.36 -70.69
REMARK 500 ALA B 160 124.62 -28.68
REMARK 500 ALA B 162 -168.55 -64.42
REMARK 500 THR B 179 67.91 -109.44
REMARK 500 ALA B 180 -59.14 67.88
REMARK 500 SER B 192 129.60 -32.89
REMARK 500 HIS B 240 103.76 -177.90
REMARK 500 ASP C 9 22.45 26.18
REMARK 500 PHE C 19 58.14 -153.34
REMARK 500 MET C 22 -47.09 -141.16
REMARK 500 HIS C 34 72.02 37.41
REMARK 500 ALA C 44 -38.87 91.09
REMARK 500 ALA C 65 21.98 -71.97
REMARK 500 ARG C 137 -11.79 72.99
REMARK 500 THR C 149 10.49 -68.96
REMARK 500 ASP C 156 100.21 62.60
REMARK 500 GLN C 181 35.45 -167.24
REMARK 500 THR C 217 129.08 -35.40
REMARK 500 ASP C 219 -66.52 167.90
REMARK 500 ALA C 238 32.78 -91.52
REMARK 500 HIS C 277 17.26 -43.68
REMARK 500 SER D 5 -70.06 -109.37
REMARK 500
REMARK 500 THIS ENTRY HAS 63 RAMACHANDRAN OUTLIERS.
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 GLY A 178 THR A 179 145.80
REMARK 500 ALA A 180 GLN A 181 -149.01
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 MIX A 539
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MIX B 1539
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MIX C 2539
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MIX D 3539
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1O6Y RELATED DB: PDB
REMARK 900 THE CRYSTAL STRUCTURE OF THE SAME PROTEIN IN COMPLEX WITH AN ATP
REMARK 900 ANALOGUE, AMP-PCP.
DBREF 2FUM A 1 279 UNP P0A5S4 PKNB_MYCTU 1 279
DBREF 2FUM B 1 279 UNP P0A5S4 PKNB_MYCTU 1 279
DBREF 2FUM C 1 279 UNP P0A5S4 PKNB_MYCTU 1 279
DBREF 2FUM D 1 279 UNP P0A5S4 PKNB_MYCTU 1 279
SEQADV 2FUM MET A -19 UNP P0A5S4 CLONING ARTIFACT
SEQADV 2FUM GLY A -18 UNP P0A5S4 CLONING ARTIFACT
SEQADV 2FUM SER A -17 UNP P0A5S4 CLONING ARTIFACT
SEQADV 2FUM SER A -16 UNP P0A5S4 CLONING ARTIFACT
SEQADV 2FUM HIS A -15 UNP P0A5S4 CLONING ARTIFACT
SEQADV 2FUM HIS A -14 UNP P0A5S4 CLONING ARTIFACT
SEQADV 2FUM HIS A -13 UNP P0A5S4 CLONING ARTIFACT
SEQADV 2FUM HIS A -12 UNP P0A5S4 CLONING ARTIFACT
SEQADV 2FUM HIS A -11 UNP P0A5S4 CLONING ARTIFACT
SEQADV 2FUM HIS A -10 UNP P0A5S4 CLONING ARTIFACT
SEQADV 2FUM SER A -9 UNP P0A5S4 CLONING ARTIFACT
SEQADV 2FUM SER A -8 UNP P0A5S4 CLONING ARTIFACT
SEQADV 2FUM GLY A -7 UNP P0A5S4 CLONING ARTIFACT
SEQADV 2FUM LEU A -6 UNP P0A5S4 CLONING ARTIFACT
SEQADV 2FUM VAL A -5 UNP P0A5S4 CLONING ARTIFACT
SEQADV 2FUM PRO A -4 UNP P0A5S4 CLONING ARTIFACT
SEQADV 2FUM ARG A -3 UNP P0A5S4 CLONING ARTIFACT
SEQADV 2FUM GLY A -2 UNP P0A5S4 CLONING ARTIFACT
SEQADV 2FUM SER A -1 UNP P0A5S4 CLONING ARTIFACT
SEQADV 2FUM HIS A 0 UNP P0A5S4 CLONING ARTIFACT
SEQADV 2FUM MET B -19 UNP P0A5S4 CLONING ARTIFACT
SEQADV 2FUM GLY B -18 UNP P0A5S4 CLONING ARTIFACT
SEQADV 2FUM SER B -17 UNP P0A5S4 CLONING ARTIFACT
SEQADV 2FUM SER B -16 UNP P0A5S4 CLONING ARTIFACT
SEQADV 2FUM HIS B -15 UNP P0A5S4 CLONING ARTIFACT
SEQADV 2FUM HIS B -14 UNP P0A5S4 CLONING ARTIFACT
SEQADV 2FUM HIS B -13 UNP P0A5S4 CLONING ARTIFACT
SEQADV 2FUM HIS B -12 UNP P0A5S4 CLONING ARTIFACT
SEQADV 2FUM HIS B -11 UNP P0A5S4 CLONING ARTIFACT
SEQADV 2FUM HIS B -10 UNP P0A5S4 CLONING ARTIFACT
SEQADV 2FUM SER B -9 UNP P0A5S4 CLONING ARTIFACT
SEQADV 2FUM SER B -8 UNP P0A5S4 CLONING ARTIFACT
SEQADV 2FUM GLY B -7 UNP P0A5S4 CLONING ARTIFACT
SEQADV 2FUM LEU B -6 UNP P0A5S4 CLONING ARTIFACT
SEQADV 2FUM VAL B -5 UNP P0A5S4 CLONING ARTIFACT
SEQADV 2FUM PRO B -4 UNP P0A5S4 CLONING ARTIFACT
SEQADV 2FUM ARG B -3 UNP P0A5S4 CLONING ARTIFACT
SEQADV 2FUM GLY B -2 UNP P0A5S4 CLONING ARTIFACT
SEQADV 2FUM SER B -1 UNP P0A5S4 CLONING ARTIFACT
SEQADV 2FUM HIS B 0 UNP P0A5S4 CLONING ARTIFACT
SEQADV 2FUM MET C -19 UNP P0A5S4 CLONING ARTIFACT
SEQADV 2FUM GLY C -18 UNP P0A5S4 CLONING ARTIFACT
SEQADV 2FUM SER C -17 UNP P0A5S4 CLONING ARTIFACT
SEQADV 2FUM SER C -16 UNP P0A5S4 CLONING ARTIFACT
SEQADV 2FUM HIS C -15 UNP P0A5S4 CLONING ARTIFACT
SEQADV 2FUM HIS C -14 UNP P0A5S4 CLONING ARTIFACT
SEQADV 2FUM HIS C -13 UNP P0A5S4 CLONING ARTIFACT
SEQADV 2FUM HIS C -12 UNP P0A5S4 CLONING ARTIFACT
SEQADV 2FUM HIS C -11 UNP P0A5S4 CLONING ARTIFACT
SEQADV 2FUM HIS C -10 UNP P0A5S4 CLONING ARTIFACT
SEQADV 2FUM SER C -9 UNP P0A5S4 CLONING ARTIFACT
SEQADV 2FUM SER C -8 UNP P0A5S4 CLONING ARTIFACT
SEQADV 2FUM GLY C -7 UNP P0A5S4 CLONING ARTIFACT
SEQADV 2FUM LEU C -6 UNP P0A5S4 CLONING ARTIFACT
SEQADV 2FUM VAL C -5 UNP P0A5S4 CLONING ARTIFACT
SEQADV 2FUM PRO C -4 UNP P0A5S4 CLONING ARTIFACT
SEQADV 2FUM ARG C -3 UNP P0A5S4 CLONING ARTIFACT
SEQADV 2FUM GLY C -2 UNP P0A5S4 CLONING ARTIFACT
SEQADV 2FUM SER C -1 UNP P0A5S4 CLONING ARTIFACT
SEQADV 2FUM HIS C 0 UNP P0A5S4 CLONING ARTIFACT
SEQADV 2FUM MET D -19 UNP P0A5S4 CLONING ARTIFACT
SEQADV 2FUM GLY D -18 UNP P0A5S4 CLONING ARTIFACT
SEQADV 2FUM SER D -17 UNP P0A5S4 CLONING ARTIFACT
SEQADV 2FUM SER D -16 UNP P0A5S4 CLONING ARTIFACT
SEQADV 2FUM HIS D -15 UNP P0A5S4 CLONING ARTIFACT
SEQADV 2FUM HIS D -14 UNP P0A5S4 CLONING ARTIFACT
SEQADV 2FUM HIS D -13 UNP P0A5S4 CLONING ARTIFACT
SEQADV 2FUM HIS D -12 UNP P0A5S4 CLONING ARTIFACT
SEQADV 2FUM HIS D -11 UNP P0A5S4 CLONING ARTIFACT
SEQADV 2FUM HIS D -10 UNP P0A5S4 CLONING ARTIFACT
SEQADV 2FUM SER D -9 UNP P0A5S4 CLONING ARTIFACT
SEQADV 2FUM SER D -8 UNP P0A5S4 CLONING ARTIFACT
SEQADV 2FUM GLY D -7 UNP P0A5S4 CLONING ARTIFACT
SEQADV 2FUM LEU D -6 UNP P0A5S4 CLONING ARTIFACT
SEQADV 2FUM VAL D -5 UNP P0A5S4 CLONING ARTIFACT
SEQADV 2FUM PRO D -4 UNP P0A5S4 CLONING ARTIFACT
SEQADV 2FUM ARG D -3 UNP P0A5S4 CLONING ARTIFACT
SEQADV 2FUM GLY D -2 UNP P0A5S4 CLONING ARTIFACT
SEQADV 2FUM SER D -1 UNP P0A5S4 CLONING ARTIFACT
SEQADV 2FUM HIS D 0 UNP P0A5S4 CLONING ARTIFACT
SEQRES 1 A 299 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 A 299 LEU VAL PRO ARG GLY SER HIS MET THR THR PRO SER HIS
SEQRES 3 A 299 LEU SER ASP ARG TYR GLU LEU GLY GLU ILE LEU GLY PHE
SEQRES 4 A 299 GLY GLY MET SER GLU VAL HIS LEU ALA ARG ASP LEU ARG
SEQRES 5 A 299 LEU HIS ARG ASP VAL ALA VAL LYS VAL LEU ARG ALA ASP
SEQRES 6 A 299 LEU ALA ARG ASP PRO SER PHE TYR LEU ARG PHE ARG ARG
SEQRES 7 A 299 GLU ALA GLN ASN ALA ALA ALA LEU ASN HIS PRO ALA ILE
SEQRES 8 A 299 VAL ALA VAL TYR ASP THR GLY GLU ALA GLU THR PRO ALA
SEQRES 9 A 299 GLY PRO LEU PRO TYR ILE VAL MET GLU TYR VAL ASP GLY
SEQRES 10 A 299 VAL THR LEU ARG ASP ILE VAL HIS THR GLU GLY PRO MET
SEQRES 11 A 299 THR PRO LYS ARG ALA ILE GLU VAL ILE ALA ASP ALA CYS
SEQRES 12 A 299 GLN ALA LEU ASN PHE SER HIS GLN ASN GLY ILE ILE HIS
SEQRES 13 A 299 ARG ASP VAL LYS PRO ALA ASN ILE MET ILE SER ALA THR
SEQRES 14 A 299 ASN ALA VAL LYS VAL MET ASP PHE GLY ILE ALA ARG ALA
SEQRES 15 A 299 ILE ALA ASP SER GLY ASN SER VAL THR GLN THR ALA ALA
SEQRES 16 A 299 VAL ILE GLY THR ALA GLN TYR LEU SER PRO GLU GLN ALA
SEQRES 17 A 299 ARG GLY ASP SER VAL ASP ALA ARG SER ASP VAL TYR SER
SEQRES 18 A 299 LEU GLY CYS VAL LEU TYR GLU VAL LEU THR GLY GLU PRO
SEQRES 19 A 299 PRO PHE THR GLY ASP SER PRO VAL SER VAL ALA TYR GLN
SEQRES 20 A 299 HIS VAL ARG GLU ASP PRO ILE PRO PRO SER ALA ARG HIS
SEQRES 21 A 299 GLU GLY LEU SER ALA ASP LEU ASP ALA VAL VAL LEU LYS
SEQRES 22 A 299 ALA LEU ALA LYS ASN PRO GLU ASN ARG TYR GLN THR ALA
SEQRES 23 A 299 ALA GLU MET ARG ALA ASP LEU VAL ARG VAL HIS ASN GLY
SEQRES 1 B 299 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 B 299 LEU VAL PRO ARG GLY SER HIS MET THR THR PRO SER HIS
SEQRES 3 B 299 LEU SER ASP ARG TYR GLU LEU GLY GLU ILE LEU GLY PHE
SEQRES 4 B 299 GLY GLY MET SER GLU VAL HIS LEU ALA ARG ASP LEU ARG
SEQRES 5 B 299 LEU HIS ARG ASP VAL ALA VAL LYS VAL LEU ARG ALA ASP
SEQRES 6 B 299 LEU ALA ARG ASP PRO SER PHE TYR LEU ARG PHE ARG ARG
SEQRES 7 B 299 GLU ALA GLN ASN ALA ALA ALA LEU ASN HIS PRO ALA ILE
SEQRES 8 B 299 VAL ALA VAL TYR ASP THR GLY GLU ALA GLU THR PRO ALA
SEQRES 9 B 299 GLY PRO LEU PRO TYR ILE VAL MET GLU TYR VAL ASP GLY
SEQRES 10 B 299 VAL THR LEU ARG ASP ILE VAL HIS THR GLU GLY PRO MET
SEQRES 11 B 299 THR PRO LYS ARG ALA ILE GLU VAL ILE ALA ASP ALA CYS
SEQRES 12 B 299 GLN ALA LEU ASN PHE SER HIS GLN ASN GLY ILE ILE HIS
SEQRES 13 B 299 ARG ASP VAL LYS PRO ALA ASN ILE MET ILE SER ALA THR
SEQRES 14 B 299 ASN ALA VAL LYS VAL MET ASP PHE GLY ILE ALA ARG ALA
SEQRES 15 B 299 ILE ALA ASP SER GLY ASN SER VAL THR GLN THR ALA ALA
SEQRES 16 B 299 VAL ILE GLY THR ALA GLN TYR LEU SER PRO GLU GLN ALA
SEQRES 17 B 299 ARG GLY ASP SER VAL ASP ALA ARG SER ASP VAL TYR SER
SEQRES 18 B 299 LEU GLY CYS VAL LEU TYR GLU VAL LEU THR GLY GLU PRO
SEQRES 19 B 299 PRO PHE THR GLY ASP SER PRO VAL SER VAL ALA TYR GLN
SEQRES 20 B 299 HIS VAL ARG GLU ASP PRO ILE PRO PRO SER ALA ARG HIS
SEQRES 21 B 299 GLU GLY LEU SER ALA ASP LEU ASP ALA VAL VAL LEU LYS
SEQRES 22 B 299 ALA LEU ALA LYS ASN PRO GLU ASN ARG TYR GLN THR ALA
SEQRES 23 B 299 ALA GLU MET ARG ALA ASP LEU VAL ARG VAL HIS ASN GLY
SEQRES 1 C 299 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 C 299 LEU VAL PRO ARG GLY SER HIS MET THR THR PRO SER HIS
SEQRES 3 C 299 LEU SER ASP ARG TYR GLU LEU GLY GLU ILE LEU GLY PHE
SEQRES 4 C 299 GLY GLY MET SER GLU VAL HIS LEU ALA ARG ASP LEU ARG
SEQRES 5 C 299 LEU HIS ARG ASP VAL ALA VAL LYS VAL LEU ARG ALA ASP
SEQRES 6 C 299 LEU ALA ARG ASP PRO SER PHE TYR LEU ARG PHE ARG ARG
SEQRES 7 C 299 GLU ALA GLN ASN ALA ALA ALA LEU ASN HIS PRO ALA ILE
SEQRES 8 C 299 VAL ALA VAL TYR ASP THR GLY GLU ALA GLU THR PRO ALA
SEQRES 9 C 299 GLY PRO LEU PRO TYR ILE VAL MET GLU TYR VAL ASP GLY
SEQRES 10 C 299 VAL THR LEU ARG ASP ILE VAL HIS THR GLU GLY PRO MET
SEQRES 11 C 299 THR PRO LYS ARG ALA ILE GLU VAL ILE ALA ASP ALA CYS
SEQRES 12 C 299 GLN ALA LEU ASN PHE SER HIS GLN ASN GLY ILE ILE HIS
SEQRES 13 C 299 ARG ASP VAL LYS PRO ALA ASN ILE MET ILE SER ALA THR
SEQRES 14 C 299 ASN ALA VAL LYS VAL MET ASP PHE GLY ILE ALA ARG ALA
SEQRES 15 C 299 ILE ALA ASP SER GLY ASN SER VAL THR GLN THR ALA ALA
SEQRES 16 C 299 VAL ILE GLY THR ALA GLN TYR LEU SER PRO GLU GLN ALA
SEQRES 17 C 299 ARG GLY ASP SER VAL ASP ALA ARG SER ASP VAL TYR SER
SEQRES 18 C 299 LEU GLY CYS VAL LEU TYR GLU VAL LEU THR GLY GLU PRO
SEQRES 19 C 299 PRO PHE THR GLY ASP SER PRO VAL SER VAL ALA TYR GLN
SEQRES 20 C 299 HIS VAL ARG GLU ASP PRO ILE PRO PRO SER ALA ARG HIS
SEQRES 21 C 299 GLU GLY LEU SER ALA ASP LEU ASP ALA VAL VAL LEU LYS
SEQRES 22 C 299 ALA LEU ALA LYS ASN PRO GLU ASN ARG TYR GLN THR ALA
SEQRES 23 C 299 ALA GLU MET ARG ALA ASP LEU VAL ARG VAL HIS ASN GLY
SEQRES 1 D 299 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 D 299 LEU VAL PRO ARG GLY SER HIS MET THR THR PRO SER HIS
SEQRES 3 D 299 LEU SER ASP ARG TYR GLU LEU GLY GLU ILE LEU GLY PHE
SEQRES 4 D 299 GLY GLY MET SER GLU VAL HIS LEU ALA ARG ASP LEU ARG
SEQRES 5 D 299 LEU HIS ARG ASP VAL ALA VAL LYS VAL LEU ARG ALA ASP
SEQRES 6 D 299 LEU ALA ARG ASP PRO SER PHE TYR LEU ARG PHE ARG ARG
SEQRES 7 D 299 GLU ALA GLN ASN ALA ALA ALA LEU ASN HIS PRO ALA ILE
SEQRES 8 D 299 VAL ALA VAL TYR ASP THR GLY GLU ALA GLU THR PRO ALA
SEQRES 9 D 299 GLY PRO LEU PRO TYR ILE VAL MET GLU TYR VAL ASP GLY
SEQRES 10 D 299 VAL THR LEU ARG ASP ILE VAL HIS THR GLU GLY PRO MET
SEQRES 11 D 299 THR PRO LYS ARG ALA ILE GLU VAL ILE ALA ASP ALA CYS
SEQRES 12 D 299 GLN ALA LEU ASN PHE SER HIS GLN ASN GLY ILE ILE HIS
SEQRES 13 D 299 ARG ASP VAL LYS PRO ALA ASN ILE MET ILE SER ALA THR
SEQRES 14 D 299 ASN ALA VAL LYS VAL MET ASP PHE GLY ILE ALA ARG ALA
SEQRES 15 D 299 ILE ALA ASP SER GLY ASN SER VAL THR GLN THR ALA ALA
SEQRES 16 D 299 VAL ILE GLY THR ALA GLN TYR LEU SER PRO GLU GLN ALA
SEQRES 17 D 299 ARG GLY ASP SER VAL ASP ALA ARG SER ASP VAL TYR SER
SEQRES 18 D 299 LEU GLY CYS VAL LEU TYR GLU VAL LEU THR GLY GLU PRO
SEQRES 19 D 299 PRO PHE THR GLY ASP SER PRO VAL SER VAL ALA TYR GLN
SEQRES 20 D 299 HIS VAL ARG GLU ASP PRO ILE PRO PRO SER ALA ARG HIS
SEQRES 21 D 299 GLU GLY LEU SER ALA ASP LEU ASP ALA VAL VAL LEU LYS
SEQRES 22 D 299 ALA LEU ALA LYS ASN PRO GLU ASN ARG TYR GLN THR ALA
SEQRES 23 D 299 ALA GLU MET ARG ALA ASP LEU VAL ARG VAL HIS ASN GLY
HET MIX A 539 32
HET MIX B1539 32
HET MIX C2539 32
HET MIX D3539 32
HETNAM MIX 1,4-DIHYDROXY-5,8-BIS({2-[(2-HYDROXYETHYL)
HETNAM 2 MIX AMINO]ETHYL}AMINO)-9,10-ANTHRACENEDIONE
HETSYN MIX MITOXANTRONE; 1,4-DIHYDROXY-5,8-BIS({2-[(2-
HETSYN 2 MIX HYDROXYETHYL)AMINO]ETHYL}AMINO)ANTHRA-9,10-QUINONE
FORMUL 5 MIX 4(C22 H28 N4 O6)
HELIX 1 1 ASP A 45 ARG A 48 5 4
HELIX 2 2 ASP A 49 LEU A 54 1 6
HELIX 3 3 PHE A 56 ALA A 65 1 10
HELIX 4 4 LEU A 100 GLY A 108 1 9
HELIX 5 5 ARG A 114 ASN A 132 1 19
HELIX 6 6 LYS A 140 ALA A 142 5 3
HELIX 7 7 SER A 184 GLY A 190 1 7
HELIX 8 8 ASP A 194 GLY A 212 1 19
HELIX 9 9 SER A 220 GLU A 231 1 12
HELIX 10 10 PRO A 235 HIS A 240 1 6
HELIX 11 11 SER A 244 LEU A 255 1 12
HELIX 12 12 ASN A 258 ARG A 262 5 5
HELIX 13 13 THR A 265 HIS A 277 1 13
HELIX 14 14 ASP B 45 ARG B 48 5 4
HELIX 15 15 ASP B 49 ALA B 65 1 17
HELIX 16 16 LEU B 100 GLY B 108 1 9
HELIX 17 17 ARG B 114 ASN B 132 1 19
HELIX 18 18 LYS B 140 ALA B 142 5 3
HELIX 19 19 SER B 184 GLY B 190 1 7
HELIX 20 20 ASP B 194 GLY B 212 1 19
HELIX 21 21 SER B 220 ARG B 230 1 11
HELIX 22 22 PRO B 235 HIS B 240 1 6
HELIX 23 23 SER B 244 LEU B 255 1 12
HELIX 24 24 ASN B 258 ARG B 262 5 5
HELIX 25 25 THR B 265 ASN B 278 1 14
HELIX 26 26 ASP C 49 LEU C 54 1 6
HELIX 27 27 GLU C 59 ALA C 65 1 7
HELIX 28 28 LEU C 100 GLU C 107 1 8
HELIX 29 29 ARG C 114 ASN C 132 1 19
HELIX 30 30 LYS C 140 ALA C 142 5 3
HELIX 31 31 SER C 184 ARG C 189 1 6
HELIX 32 32 ASP C 194 GLY C 212 1 19
HELIX 33 33 SER C 220 GLU C 231 1 12
HELIX 34 34 PRO C 235 ARG C 239 5 5
HELIX 35 35 SER C 244 LEU C 255 1 12
HELIX 36 36 ASN C 258 ARG C 262 5 5
HELIX 37 37 THR C 265 ARG C 275 1 11
HELIX 38 38 ASP D 49 LEU D 54 1 6
HELIX 39 39 ARG D 58 ALA D 65 1 8
HELIX 40 40 LEU D 100 GLU D 107 1 8
HELIX 41 41 THR D 111 ASN D 132 1 22
HELIX 42 42 LYS D 140 ALA D 142 5 3
HELIX 43 43 SER D 184 GLY D 190 1 7
HELIX 44 44 ASP D 194 GLY D 212 1 19
HELIX 45 45 SER D 220 GLU D 231 1 12
HELIX 46 46 PRO D 235 ARG D 239 5 5
HELIX 47 47 SER D 244 LEU D 255 1 12
HELIX 48 48 ASN D 258 ARG D 262 5 5
HELIX 49 49 THR D 265 ARG D 275 1 11
SHEET 1 A 6 HIS A 6 LEU A 7 0
SHEET 2 A 6 TYR A 11 PHE A 19 -1 O TYR A 11 N LEU A 7
SHEET 3 A 6 SER A 23 ASP A 30 -1 O VAL A 25 N LEU A 17
SHEET 4 A 6 ARG A 35 LEU A 42 -1 O VAL A 39 N HIS A 26
SHEET 5 A 6 LEU A 87 MET A 92 -1 O MET A 92 N ALA A 38
SHEET 6 A 6 VAL A 74 ALA A 80 -1 N ASP A 76 O VAL A 91
SHEET 1 B 3 GLY A 97 THR A 99 0
SHEET 2 B 3 ILE A 144 SER A 147 -1 O ILE A 146 N VAL A 98
SHEET 3 B 3 VAL A 152 VAL A 154 -1 O LYS A 153 N MET A 145
SHEET 1 C 6 HIS B 6 LEU B 7 0
SHEET 2 C 6 TYR B 11 PHE B 19 -1 O TYR B 11 N LEU B 7
SHEET 3 C 6 SER B 23 ASP B 30 -1 O VAL B 25 N LEU B 17
SHEET 4 C 6 ARG B 35 LEU B 42 -1 O VAL B 37 N ALA B 28
SHEET 5 C 6 GLY B 85 MET B 92 -1 O MET B 92 N ALA B 38
SHEET 6 C 6 VAL B 74 THR B 82 -1 N ASP B 76 O VAL B 91
SHEET 1 D 3 GLY B 97 THR B 99 0
SHEET 2 D 3 ILE B 144 SER B 147 -1 O ILE B 146 N VAL B 98
SHEET 3 D 3 VAL B 152 VAL B 154 -1 O LYS B 153 N MET B 145
SHEET 1 E 6 HIS C 6 LEU C 7 0
SHEET 2 E 6 TYR C 11 GLY C 18 -1 O TYR C 11 N LEU C 7
SHEET 3 E 6 GLU C 24 ASP C 30 -1 O VAL C 25 N LEU C 17
SHEET 4 E 6 ARG C 35 VAL C 41 -1 O VAL C 37 N ALA C 28
SHEET 5 E 6 LEU C 87 GLU C 93 -1 O MET C 92 N ALA C 38
SHEET 6 E 6 VAL C 74 ALA C 80 -1 N ASP C 76 O VAL C 91
SHEET 1 F 3 GLY C 97 THR C 99 0
SHEET 2 F 3 ILE C 144 SER C 147 -1 O ILE C 146 N VAL C 98
SHEET 3 F 3 VAL C 152 VAL C 154 -1 O LYS C 153 N MET C 145
SHEET 1 G 6 HIS D 6 LEU D 7 0
SHEET 2 G 6 TYR D 11 GLY D 18 -1 O TYR D 11 N LEU D 7
SHEET 3 G 6 GLU D 24 ASP D 30 -1 O VAL D 25 N LEU D 17
SHEET 4 G 6 ARG D 35 VAL D 41 -1 O VAL D 39 N HIS D 26
SHEET 5 G 6 LEU D 87 GLU D 93 -1 O MET D 92 N ALA D 38
SHEET 6 G 6 VAL D 74 ALA D 80 -1 N ASP D 76 O VAL D 91
SHEET 1 H 3 GLY D 97 THR D 99 0
SHEET 2 H 3 ILE D 144 SER D 147 -1 O ILE D 146 N VAL D 98
SHEET 3 H 3 VAL D 152 VAL D 154 -1 O LYS D 153 N MET D 145
SITE 1 AC1 13 LEU A 17 PHE A 19 ALA A 38 GLU A 93
SITE 2 AC1 13 TYR A 94 VAL A 95 GLY A 97 ASP A 102
SITE 3 AC1 13 LYS A 140 ALA A 142 ASN A 143 MET A 145
SITE 4 AC1 13 ASP B 219
SITE 1 AC2 13 ASP A 219 LEU B 17 GLY B 18 PHE B 19
SITE 2 AC2 13 ALA B 38 GLU B 93 TYR B 94 VAL B 95
SITE 3 AC2 13 GLY B 97 LYS B 140 ASN B 143 MET B 145
SITE 4 AC2 13 ASP B 156
SITE 1 AC3 10 LEU C 17 PHE C 19 ALA C 38 MET C 92
SITE 2 AC3 10 GLU C 93 VAL C 95 GLY C 97 ASN C 143
SITE 3 AC3 10 MET C 155 ASP C 156
SITE 1 AC4 14 LEU D 17 GLY D 18 PHE D 19 VAL D 25
SITE 2 AC4 14 ALA D 38 MET D 92 VAL D 95 GLY D 97
SITE 3 AC4 14 VAL D 98 ASP D 138 ASN D 143 MET D 145
SITE 4 AC4 14 MET D 155 ASP D 156
CRYST1 116.863 116.863 260.347 90.00 90.00 90.00 P 43 21 2 32
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 0.008557 0.000000 0.000000 0.00000
SCALE2 0.000000 0.008557 0.000000 0.00000
SCALE3 0.000000 0.000000 0.003841 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
