HEADER TRANSFERASE 30-MAY-07 2Q3D
TITLE 2.2 A RESOLUTION CRYSTAL STRUCTURE OF O-ACETYLSERINE SULFHYDRYLASE
TITLE 2 (OASS) FROM MYCOBACTERIUM TUBERCULOSIS IN COMPLEX WITH THE REACTION
TITLE 3 INTERMEDIATE ALPHA-AMINOACRYLATE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CYSTEINE SYNTHASE A;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: O-ACETYLSERINE SULFHYDRYLASE A, O-ACETYLSERINE THIOL, LYASE
COMPND 5 A, CSASE A;
COMPND 6 EC: 2.5.1.47;
COMPND 7 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MYCOBACTERIUM TUBERCULOSIS;
SOURCE 3 ORGANISM_TAXID: 1773;
SOURCE 4 STRAIN: RV2334;
SOURCE 5 GENE: CYSK;
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: PET28A
KEYWDS MYCOBACTERIUM TUBERCULOSIS, PYRIDOXAL-5'-PHOSPHATE, SULPHUR
KEYWDS 2 METABOLISM, CYSTEINE BIOSYNTHESIS, ALPHA-AMINOACRYLATE INTERMEDIATE,
KEYWDS 3 TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR G.SCHNEIDER,R.SCHNELL
REVDAT 6 30-AUG-23 2Q3D 1 REMARK SEQADV
REVDAT 5 07-MAR-18 2Q3D 1 REMARK
REVDAT 4 13-JUL-11 2Q3D 1 VERSN
REVDAT 3 24-FEB-09 2Q3D 1 VERSN
REVDAT 2 21-AUG-07 2Q3D 1 JRNL
REVDAT 1 12-JUN-07 2Q3D 0
JRNL AUTH R.SCHNELL,W.OEHLMANN,M.SINGH,G.SCHNEIDER
JRNL TITL STRUCTURAL INSIGHTS INTO CATALYSIS AND INHIBITION OF
JRNL TITL 2 O-ACETYLSERINE SULFHYDRYLASE FROM MYCOBACTERIUM
JRNL TITL 3 TUBERCULOSIS: CRYSTAL STRUCTURES OF THE ENZYME
JRNL TITL 4 {ALPHA}-AMINOACRYLATE INTERMEDIATE AND AN ENZYME-INHIBITOR
JRNL TITL 5 COMPLEX.
JRNL REF J.BIOL.CHEM. V. 282 23473 2007
JRNL REFN ISSN 0021-9258
JRNL PMID 17567578
JRNL DOI 10.1074/JBC.M703518200
REMARK 2
REMARK 2 RESOLUTION. 2.20 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) : 2.20
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 28.35
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.5
REMARK 3 NUMBER OF REFLECTIONS : 23287
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) : 0.196
REMARK 3 R VALUE (WORKING SET) : 0.194
REMARK 3 FREE R VALUE : 0.249
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 1245
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) : 2.20
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.26
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1684
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.61
REMARK 3 BIN R VALUE (WORKING SET) : 0.3020
REMARK 3 BIN FREE R VALUE SET COUNT : 103
REMARK 3 BIN FREE R VALUE : 0.3180
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2271
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 29
REMARK 3 SOLVENT ATOMS : 42
REMARK 3
REMARK 3 B VALUES.
REMARK 3 B VALUE TYPE : LIKELY RESIDUAL
REMARK 3 FROM WILSON PLOT (A**2) : 43.00
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 30.42
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 3.56000
REMARK 3 B22 (A**2) : 3.56000
REMARK 3 B33 (A**2) : -7.12000
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): 0.181
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.179
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.158
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 13.344
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.962
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.937
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 2363 ; 0.012 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 3221 ; 1.419 ; 1.999
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 313 ; 5.487 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 93 ;28.280 ;23.441
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 391 ;16.682 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 23 ;14.801 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 382 ; 0.092 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 1778 ; 0.005 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 1158 ; 0.211 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 1623 ; 0.310 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 125 ; 0.508 ; 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): 46 ; 0.233 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 11 ; 0.221 ; 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): 1564 ; 0.581 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 2473 ; 0.970 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 870 ; 1.739 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 744 ; 2.668 ; 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 : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 20
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 1 A 9
REMARK 3 ORIGIN FOR THE GROUP (A): 58.2310 14.6070 32.4690
REMARK 3 T TENSOR
REMARK 3 T11: 0.2803 T22: 0.1557
REMARK 3 T33: 0.2486 T12: 0.1373
REMARK 3 T13: 0.0297 T23: -0.0343
REMARK 3 L TENSOR
REMARK 3 L11: 19.8513 L22: 7.2998
REMARK 3 L33: 17.7702 L12: 10.4344
REMARK 3 L13: 8.5097 L23: 1.6284
REMARK 3 S TENSOR
REMARK 3 S11: 0.1209 S12: 1.5252 S13: -0.3784
REMARK 3 S21: 0.5415 S22: 0.4199 S23: -0.5056
REMARK 3 S31: 0.5381 S32: 0.2559 S33: -0.5408
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 10 A 20
REMARK 3 ORIGIN FOR THE GROUP (A): 52.4540 12.1281 50.9402
REMARK 3 T TENSOR
REMARK 3 T11: 0.1685 T22: 0.2749
REMARK 3 T33: 0.4407 T12: 0.2117
REMARK 3 T13: 0.0091 T23: -0.0084
REMARK 3 L TENSOR
REMARK 3 L11: 2.4137 L22: 5.6058
REMARK 3 L33: 36.4197 L12: 1.5807
REMARK 3 L13: -2.6971 L23: 1.3633
REMARK 3 S TENSOR
REMARK 3 S11: -0.0411 S12: -0.0416 S13: -0.3756
REMARK 3 S21: 0.1316 S22: -0.0178 S23: -0.1037
REMARK 3 S31: -0.2941 S32: 0.9382 S33: 0.0588
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 21 A 32
REMARK 3 ORIGIN FOR THE GROUP (A): 46.2830 12.0956 66.0708
REMARK 3 T TENSOR
REMARK 3 T11: 0.2490 T22: 0.1564
REMARK 3 T33: 0.1586 T12: 0.0625
REMARK 3 T13: 0.0049 T23: 0.0121
REMARK 3 L TENSOR
REMARK 3 L11: 0.4956 L22: 5.5624
REMARK 3 L33: 4.8136 L12: -0.9001
REMARK 3 L13: 1.4495 L23: -4.1342
REMARK 3 S TENSOR
REMARK 3 S11: -0.0397 S12: -0.1391 S13: -0.3574
REMARK 3 S21: 0.6327 S22: 0.0429 S23: -0.1482
REMARK 3 S31: 0.1278 S32: 0.2299 S33: -0.0032
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 33 A 55
REMARK 3 ORIGIN FOR THE GROUP (A): 45.5410 12.9055 40.0606
REMARK 3 T TENSOR
REMARK 3 T11: 0.1541 T22: 0.2429
REMARK 3 T33: 0.3200 T12: 0.0918
REMARK 3 T13: -0.0234 T23: -0.0243
REMARK 3 L TENSOR
REMARK 3 L11: 2.7153 L22: 0.1250
REMARK 3 L33: 0.3863 L12: -0.5827
REMARK 3 L13: -1.0241 L23: 0.2198
REMARK 3 S TENSOR
REMARK 3 S11: 0.0043 S12: 0.3695 S13: 0.1826
REMARK 3 S21: -0.1499 S22: 0.0887 S23: -0.2296
REMARK 3 S31: -0.0647 S32: -0.0497 S33: -0.0930
REMARK 3
REMARK 3 TLS GROUP : 5
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 56 A 69
REMARK 3 ORIGIN FOR THE GROUP (A): 38.5804 10.7399 22.6538
REMARK 3 T TENSOR
REMARK 3 T11: 0.1731 T22: 0.3311
REMARK 3 T33: 0.1211 T12: 0.0022
REMARK 3 T13: -0.0246 T23: -0.0423
REMARK 3 L TENSOR
REMARK 3 L11: 3.7740 L22: 11.6089
REMARK 3 L33: 6.7379 L12: -4.8055
REMARK 3 L13: -4.8260 L23: 6.6200
REMARK 3 S TENSOR
REMARK 3 S11: -0.2880 S12: 0.1172 S13: -0.0618
REMARK 3 S21: -0.2029 S22: 0.3795 S23: -0.0197
REMARK 3 S31: -0.4263 S32: 0.1315 S33: -0.0915
REMARK 3
REMARK 3 TLS GROUP : 6
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 70 A 85
REMARK 3 ORIGIN FOR THE GROUP (A): 39.6614 17.7894 34.7048
REMARK 3 T TENSOR
REMARK 3 T11: 0.1502 T22: 0.2284
REMARK 3 T33: 0.2765 T12: 0.0416
REMARK 3 T13: 0.0150 T23: -0.0106
REMARK 3 L TENSOR
REMARK 3 L11: 1.5295 L22: 2.9976
REMARK 3 L33: 4.4626 L12: -0.1213
REMARK 3 L13: 2.4556 L23: 1.0519
REMARK 3 S TENSOR
REMARK 3 S11: -0.3480 S12: 0.6019 S13: -0.0092
REMARK 3 S21: -0.2128 S22: 0.3548 S23: -0.1863
REMARK 3 S31: 0.1064 S32: -0.1678 S33: -0.0068
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 : A 86 A 105
REMARK 3 ORIGIN FOR THE GROUP (A): 34.7538 22.7374 35.2097
REMARK 3 T TENSOR
REMARK 3 T11: 0.1022 T22: 0.3737
REMARK 3 T33: 0.3986 T12: 0.1544
REMARK 3 T13: -0.0376 T23: 0.0241
REMARK 3 L TENSOR
REMARK 3 L11: 4.5192 L22: 2.8452
REMARK 3 L33: 7.9895 L12: -0.5856
REMARK 3 L13: -1.6354 L23: 2.6384
REMARK 3 S TENSOR
REMARK 3 S11: -0.0792 S12: 0.0188 S13: 0.0298
REMARK 3 S21: -0.6420 S22: -0.0100 S23: 0.4290
REMARK 3 S31: -0.5877 S32: -0.3638 S33: 0.0892
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 : A 106 A 122
REMARK 3 ORIGIN FOR THE GROUP (A): 30.6834 23.1481 34.9140
REMARK 3 T TENSOR
REMARK 3 T11: 0.1283 T22: 0.4283
REMARK 3 T33: 0.3555 T12: 0.1620
REMARK 3 T13: -0.0485 T23: 0.0143
REMARK 3 L TENSOR
REMARK 3 L11: 15.1958 L22: 5.9197
REMARK 3 L33: 2.5805 L12: 3.2065
REMARK 3 L13: -1.9130 L23: 0.3882
REMARK 3 S TENSOR
REMARK 3 S11: -0.1717 S12: 0.2324 S13: 0.4225
REMARK 3 S21: -0.3298 S22: 0.0634 S23: 0.6692
REMARK 3 S31: -0.1564 S32: -0.9369 S33: 0.1082
REMARK 3
REMARK 3 TLS GROUP : 9
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 123 A 130
REMARK 3 ORIGIN FOR THE GROUP (A): 24.0483 13.9755 33.2245
REMARK 3 T TENSOR
REMARK 3 T11: 0.0849 T22: 0.5366
REMARK 3 T33: 0.5299 T12: -0.0479
REMARK 3 T13: -0.0917 T23: -0.0382
REMARK 3 L TENSOR
REMARK 3 L11: 25.4607 L22: 2.6173
REMARK 3 L33: 67.3821 L12: -7.7222
REMARK 3 L13: 8.4637 L23: -6.7820
REMARK 3 S TENSOR
REMARK 3 S11: 0.2140 S12: 0.2338 S13: -0.3852
REMARK 3 S21: -0.0522 S22: -0.2830 S23: 1.3741
REMARK 3 S31: 0.4183 S32: -2.6388 S33: 0.0690
REMARK 3
REMARK 3 TLS GROUP : 10
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 131 A 158
REMARK 3 ORIGIN FOR THE GROUP (A): 34.6856 8.2368 31.5755
REMARK 3 T TENSOR
REMARK 3 T11: 0.0908 T22: 0.3246
REMARK 3 T33: 0.1648 T12: 0.0175
REMARK 3 T13: 0.0130 T23: -0.0599
REMARK 3 L TENSOR
REMARK 3 L11: 5.8014 L22: 4.8327
REMARK 3 L33: 8.7764 L12: -2.2846
REMARK 3 L13: 4.2299 L23: -1.6637
REMARK 3 S TENSOR
REMARK 3 S11: 0.1026 S12: 0.7386 S13: -0.1136
REMARK 3 S21: -0.4330 S22: -0.1017 S23: 0.4348
REMARK 3 S31: 0.1853 S32: -0.3530 S33: -0.0009
REMARK 3
REMARK 3 TLS GROUP : 11
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 159 A 163
REMARK 3 ORIGIN FOR THE GROUP (A): 51.2713 0.8620 48.5392
REMARK 3 T TENSOR
REMARK 3 T11: 0.3373 T22: 0.1095
REMARK 3 T33: 0.4200 T12: 0.2491
REMARK 3 T13: -0.0327 T23: -0.0720
REMARK 3 L TENSOR
REMARK 3 L11: 8.1599 L22: 15.0603
REMARK 3 L33: 31.3361 L12: -1.7967
REMARK 3 L13: -0.9813 L23: -21.1803
REMARK 3 S TENSOR
REMARK 3 S11: 0.2076 S12: 0.3161 S13: -0.4782
REMARK 3 S21: 0.2406 S22: -0.0255 S23: -1.2104
REMARK 3 S31: 0.7262 S32: 0.7929 S33: -0.1821
REMARK 3
REMARK 3 TLS GROUP : 12
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 164 A 172
REMARK 3 ORIGIN FOR THE GROUP (A): 51.9994 0.3817 55.3418
REMARK 3 T TENSOR
REMARK 3 T11: 0.3551 T22: 0.3452
REMARK 3 T33: 0.2904 T12: 0.2433
REMARK 3 T13: -0.0828 T23: -0.0022
REMARK 3 L TENSOR
REMARK 3 L11: 26.6951 L22: 19.9725
REMARK 3 L33: 3.8999 L12: 9.3276
REMARK 3 L13: -9.9147 L23: -5.3710
REMARK 3 S TENSOR
REMARK 3 S11: 0.4166 S12: -0.0302 S13: -0.5888
REMARK 3 S21: 0.5915 S22: -0.4066 S23: -0.8137
REMARK 3 S31: 1.2040 S32: 0.9182 S33: -0.0099
REMARK 3
REMARK 3 TLS GROUP : 13
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 173 A 191
REMARK 3 ORIGIN FOR THE GROUP (A): 39.7829 1.8474 48.2921
REMARK 3 T TENSOR
REMARK 3 T11: 0.2169 T22: 0.1975
REMARK 3 T33: 0.2759 T12: 0.1149
REMARK 3 T13: 0.0513 T23: -0.0134
REMARK 3 L TENSOR
REMARK 3 L11: 4.7605 L22: 0.8021
REMARK 3 L33: 2.4392 L12: -0.4932
REMARK 3 L13: -1.2235 L23: 1.3900
REMARK 3 S TENSOR
REMARK 3 S11: -0.0202 S12: -0.3103 S13: -0.2544
REMARK 3 S21: -0.3731 S22: 0.2451 S23: -0.0544
REMARK 3 S31: 0.9781 S32: -0.4461 S33: -0.2249
REMARK 3
REMARK 3 TLS GROUP : 14
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 192 A 203
REMARK 3 ORIGIN FOR THE GROUP (A): 40.9159 -2.6265 53.9198
REMARK 3 T TENSOR
REMARK 3 T11: 0.3160 T22: 0.0910
REMARK 3 T33: 0.2467 T12: 0.0368
REMARK 3 T13: -0.0007 T23: -0.0397
REMARK 3 L TENSOR
REMARK 3 L11: 13.3616 L22: 10.5845
REMARK 3 L33: 2.9421 L12: -8.1024
REMARK 3 L13: -4.7098 L23: 3.0531
REMARK 3 S TENSOR
REMARK 3 S11: 0.3592 S12: 0.3808 S13: -0.9485
REMARK 3 S21: -0.1857 S22: -0.5398 S23: 0.1460
REMARK 3 S31: 0.8852 S32: -0.3396 S33: 0.1806
REMARK 3
REMARK 3 TLS GROUP : 15
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 204 A 233
REMARK 3 ORIGIN FOR THE GROUP (A): 26.3063 9.6763 48.7351
REMARK 3 T TENSOR
REMARK 3 T11: 0.0694 T22: 0.4052
REMARK 3 T33: 0.2759 T12: -0.0049
REMARK 3 T13: 0.0513 T23: -0.0410
REMARK 3 L TENSOR
REMARK 3 L11: 1.7404 L22: 6.9684
REMARK 3 L33: 4.7666 L12: -0.0523
REMARK 3 L13: 0.6441 L23: 0.6841
REMARK 3 S TENSOR
REMARK 3 S11: -0.0453 S12: 0.0855 S13: 0.0316
REMARK 3 S21: 0.1622 S22: -0.1653 S23: 0.4344
REMARK 3 S31: 0.4366 S32: -1.2377 S33: 0.2106
REMARK 3
REMARK 3 TLS GROUP : 16
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 234 A 244
REMARK 3 ORIGIN FOR THE GROUP (A): 31.9117 1.2052 54.4186
REMARK 3 T TENSOR
REMARK 3 T11: 0.1889 T22: 0.1314
REMARK 3 T33: 0.2412 T12: 0.0278
REMARK 3 T13: 0.0542 T23: -0.0266
REMARK 3 L TENSOR
REMARK 3 L11: 1.5415 L22: 8.6741
REMARK 3 L33: 6.7566 L12: -2.0805
REMARK 3 L13: -1.4793 L23: 1.6208
REMARK 3 S TENSOR
REMARK 3 S11: 0.1902 S12: 0.0435 S13: -0.2901
REMARK 3 S21: 0.3438 S22: -0.2123 S23: 0.0672
REMARK 3 S31: 1.2819 S32: -0.8247 S33: 0.0221
REMARK 3
REMARK 3 TLS GROUP : 17
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 245 A 257
REMARK 3 ORIGIN FOR THE GROUP (A): 36.9664 21.7461 61.0242
REMARK 3 T TENSOR
REMARK 3 T11: 0.3721 T22: 0.2428
REMARK 3 T33: 0.3653 T12: 0.1606
REMARK 3 T13: 0.1185 T23: -0.0534
REMARK 3 L TENSOR
REMARK 3 L11: 34.3385 L22: 1.8011
REMARK 3 L33: 7.9184 L12: 7.5609
REMARK 3 L13: 2.9345 L23: -0.3762
REMARK 3 S TENSOR
REMARK 3 S11: 0.4788 S12: -0.5975 S13: 1.9258
REMARK 3 S21: 0.6566 S22: -0.4080 S23: 0.7301
REMARK 3 S31: -0.5187 S32: -0.6609 S33: -0.0708
REMARK 3
REMARK 3 TLS GROUP : 18
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 258 A 275
REMARK 3 ORIGIN FOR THE GROUP (A): 41.0989 16.9404 58.1638
REMARK 3 T TENSOR
REMARK 3 T11: 0.2306 T22: 0.2132
REMARK 3 T33: 0.3071 T12: 0.1457
REMARK 3 T13: 0.0376 T23: 0.0253
REMARK 3 L TENSOR
REMARK 3 L11: 3.7417 L22: 2.4307
REMARK 3 L33: 4.1105 L12: 1.1310
REMARK 3 L13: -2.7634 L23: 1.1555
REMARK 3 S TENSOR
REMARK 3 S11: 0.0721 S12: 0.0064 S13: 0.1034
REMARK 3 S21: 0.3982 S22: -0.0560 S23: 0.2348
REMARK 3 S31: -0.0897 S32: -0.0374 S33: -0.0161
REMARK 3
REMARK 3 TLS GROUP : 19
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 276 A 300
REMARK 3 ORIGIN FOR THE GROUP (A): 41.6921 11.1132 58.2472
REMARK 3 T TENSOR
REMARK 3 T11: 0.2799 T22: 0.2008
REMARK 3 T33: 0.3416 T12: 0.1477
REMARK 3 T13: 0.0487 T23: -0.0503
REMARK 3 L TENSOR
REMARK 3 L11: 2.3878 L22: 0.2603
REMARK 3 L33: 4.1992 L12: -0.1063
REMARK 3 L13: 1.3431 L23: 0.8783
REMARK 3 S TENSOR
REMARK 3 S11: 0.2176 S12: -0.1386 S13: -0.0791
REMARK 3 S21: 0.3766 S22: -0.2500 S23: 0.1978
REMARK 3 S31: 0.3917 S32: 0.2890 S33: 0.0324
REMARK 3
REMARK 3 TLS GROUP : 20
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 301 A 306
REMARK 3 ORIGIN FOR THE GROUP (A): 34.6274 28.8728 53.4579
REMARK 3 T TENSOR
REMARK 3 T11: 0.1785 T22: 0.2545
REMARK 3 T33: 0.3502 T12: 0.1347
REMARK 3 T13: 0.1112 T23: -0.0496
REMARK 3 L TENSOR
REMARK 3 L11: 30.5569 L22: 34.0180
REMARK 3 L33: 55.3639 L12: -32.1898
REMARK 3 L13: 7.4806 L23: -5.4771
REMARK 3 S TENSOR
REMARK 3 S11: -0.8026 S12: -2.3003 S13: 0.7415
REMARK 3 S21: 0.9565 S22: 1.2654 S23: -0.0952
REMARK 3 S31: -2.0814 S32: -1.1126 S33: -0.4628
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: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS
REMARK 4
REMARK 4 2Q3D COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 31-MAY-07.
REMARK 100 THE DEPOSITION ID IS D_1000043097.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 19-OCT-06
REMARK 200 TEMPERATURE (KELVIN) : 110
REMARK 200 PH : 8.2
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : MAX II
REMARK 200 BEAMLINE : I911-3
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.000
REMARK 200 MONOCHROMATOR : DOUBLE CRYSTAL MONOCHROMATOR,
REMARK 200 SI(111). THE FIRST CRYSTAL IS
REMARK 200 WATER COOLED.
REMARK 200 OPTICS : FIRST MIRROR: WATER-COOLED
REMARK 200 VERTICALLY COLLIMATING
REMARK 200 CYLINDRICAL MIRROR (R = 7300 M).
REMARK 200 SECOND MIRROR: TOROID MIRROR FOR
REMARK 200 HORIZONTAL AND VERTICAL FOCUSING
REMARK 200 (R=3300M, R=27MM).
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MAR CCD 165 MM
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 24607
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.200
REMARK 200 RESOLUTION RANGE LOW (A) : 71.800
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.9
REMARK 200 DATA REDUNDANCY : 5.400
REMARK 200 R MERGE (I) : 0.09100
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 14.2000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.20
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.32
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.8
REMARK 200 DATA REDUNDANCY IN SHELL : 5.30
REMARK 200 R MERGE FOR SHELL (I) : 0.49900
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.400
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: PDB ENTRY 2Q3B, HOLOENZYME
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 65.85
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.60
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M HEPES, 80% MPD. SOAKED WITH 1 MM
REMARK 280 O-ACETYL-SERINE FOR 30 MINUTES BEFORE FREEZING., PH 8.2, VAPOR
REMARK 280 DIFFUSION, SITTING DROP, TEMPERATURE 293K
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 90.58950
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 35.89250
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 35.89250
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 45.29475
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 35.89250
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 35.89250
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 135.88425
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 35.89250
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 35.89250
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 45.29475
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 35.89250
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 35.89250
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 135.88425
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 90.58950
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 300 REMARK: THE OASS FORMS A DIMER, THE SECOND PART OF THE BIOLOGICAL
REMARK 300 ASSEMBLY IS GENERATED BY THE TWO FOLD AXIS: -Y+1, -X+1, -Z+1/2.
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,PQS
REMARK 350 TOTAL BURIED SURFACE AREA: 5010 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 20470 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -42.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT1 2 0.000000 -1.000000 0.000000 71.78500
REMARK 350 BIOMT2 2 -1.000000 0.000000 0.000000 71.78500
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 90.58950
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 -2
REMARK 465 SER A -1
REMARK 465 HIS A 0
REMARK 465 ASP A 307
REMARK 465 VAL A 308
REMARK 465 ALA A 309
REMARK 465 ASP A 310
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 THR A 23 22.37 -141.88
REMARK 500 PHE A 37 34.13 -80.56
REMARK 500 GLN A 143 71.63 65.03
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 PDA A 311
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MPD A 312
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2Q3B RELATED DB: PDB
REMARK 900 RELATED ID: 2Q3C RELATED DB: PDB
DBREF 2Q3D A 1 310 UNP P0A534 CYSK_MYCTU 1 310
SEQADV 2Q3D GLY A -2 UNP P0A534 CLONING ARTIFACT
SEQADV 2Q3D SER A -1 UNP P0A534 CLONING ARTIFACT
SEQADV 2Q3D HIS A 0 UNP P0A534 CLONING ARTIFACT
SEQRES 1 A 313 GLY SER HIS MET SER ILE ALA GLU ASP ILE THR GLN LEU
SEQRES 2 A 313 ILE GLY ARG THR PRO LEU VAL ARG LEU ARG ARG VAL THR
SEQRES 3 A 313 ASP GLY ALA VAL ALA ASP ILE VAL ALA LYS LEU GLU PHE
SEQRES 4 A 313 PHE ASN PRO ALA ASN SER VAL LYS ASP ARG ILE GLY VAL
SEQRES 5 A 313 ALA MET LEU GLN ALA ALA GLU GLN ALA GLY LEU ILE LYS
SEQRES 6 A 313 PRO ASP THR ILE ILE LEU GLU PRO THR SER GLY ASN THR
SEQRES 7 A 313 GLY ILE ALA LEU ALA MET VAL CYS ALA ALA ARG GLY TYR
SEQRES 8 A 313 ARG CYS VAL LEU THR MET PRO GLU THR MET SER LEU GLU
SEQRES 9 A 313 ARG ARG MET LEU LEU ARG ALA TYR GLY ALA GLU LEU ILE
SEQRES 10 A 313 LEU THR PRO GLY ALA ASP GLY MET SER GLY ALA ILE ALA
SEQRES 11 A 313 LYS ALA GLU GLU LEU ALA LYS THR ASP GLN ARG TYR PHE
SEQRES 12 A 313 VAL PRO GLN GLN PHE GLU ASN PRO ALA ASN PRO ALA ILE
SEQRES 13 A 313 HIS ARG VAL THR THR ALA GLU GLU VAL TRP ARG ASP THR
SEQRES 14 A 313 ASP GLY LYS VAL ASP ILE VAL VAL ALA GLY VAL GLY THR
SEQRES 15 A 313 GLY GLY THR ILE THR GLY VAL ALA GLN VAL ILE LYS GLU
SEQRES 16 A 313 ARG LYS PRO SER ALA ARG PHE VAL ALA VAL GLU PRO ALA
SEQRES 17 A 313 ALA SER PRO VAL LEU SER GLY GLY GLN LYS GLY PRO HIS
SEQRES 18 A 313 PRO ILE GLN GLY ILE GLY ALA GLY PHE VAL PRO PRO VAL
SEQRES 19 A 313 LEU ASP GLN ASP LEU VAL ASP GLU ILE ILE THR VAL GLY
SEQRES 20 A 313 ASN GLU ASP ALA LEU ASN VAL ALA ARG ARG LEU ALA ARG
SEQRES 21 A 313 GLU GLU GLY LEU LEU VAL GLY ILE SER SER GLY ALA ALA
SEQRES 22 A 313 THR VAL ALA ALA LEU GLN VAL ALA ARG ARG PRO GLU ASN
SEQRES 23 A 313 ALA GLY LYS LEU ILE VAL VAL VAL LEU PRO ASP PHE GLY
SEQRES 24 A 313 GLU ARG TYR LEU SER THR PRO LEU PHE ALA ASP VAL ALA
SEQRES 25 A 313 ASP
HET PDA A 311 21
HET MPD A 312 8
HETNAM PDA 2-[(3-HYDROXY-2-METHYL-5-PHOSPHONOOXYMETHYL-PYRIDIN-4-
HETNAM 2 PDA YLMETHYL)-AMINO]-PROPIONIC ACID
HETNAM MPD (4S)-2-METHYL-2,4-PENTANEDIOL
HETSYN PDA PYRIDOXYL-ALANINE-5-PHOSPHATE
FORMUL 2 PDA C11 H17 N2 O7 P
FORMUL 3 MPD C6 H14 O2
FORMUL 4 HOH *42(H2 O)
HELIX 1 1 ASP A 6 ILE A 11 5 6
HELIX 2 2 LYS A 44 ALA A 58 1 15
HELIX 3 3 GLY A 73 GLY A 87 1 15
HELIX 4 4 SER A 99 TYR A 109 1 11
HELIX 5 5 ASP A 120 LYS A 134 1 15
HELIX 6 6 PRO A 148 THR A 157 1 10
HELIX 7 7 THR A 157 THR A 166 1 10
HELIX 8 8 GLY A 180 LYS A 194 1 15
HELIX 9 9 GLY A 244 GLY A 260 1 17
HELIX 10 10 GLY A 264 ALA A 278 1 15
HELIX 11 11 ARG A 279 ALA A 284 5 6
HELIX 12 12 PHE A 295 LEU A 300 5 6
SHEET 1 A 6 LEU A 16 ARG A 18 0
SHEET 2 A 6 ASP A 29 LEU A 34 -1 O ALA A 32 N VAL A 17
SHEET 3 A 6 LEU A 287 LEU A 292 1 O ILE A 288 N ASP A 29
SHEET 4 A 6 ILE A 172 GLY A 176 1 N VAL A 174 O VAL A 289
SHEET 5 A 6 ARG A 198 PRO A 204 1 O VAL A 200 N VAL A 173
SHEET 6 A 6 GLU A 239 VAL A 243 1 O GLU A 239 N ALA A 201
SHEET 1 B 4 GLU A 112 THR A 116 0
SHEET 2 B 4 ARG A 89 PRO A 95 1 N LEU A 92 O ILE A 114
SHEET 3 B 4 ILE A 66 PRO A 70 1 N ILE A 67 O VAL A 91
SHEET 4 B 4 TYR A 139 PHE A 140 1 O PHE A 140 N LEU A 68
SITE 1 AC1 23 LYS A 44 THR A 71 SER A 72 GLY A 73
SITE 2 AC1 23 ASN A 74 THR A 75 GLN A 144 VAL A 177
SITE 3 AC1 23 GLY A 178 THR A 179 GLY A 180 GLY A 181
SITE 4 AC1 23 THR A 182 GLY A 222 ILE A 223 SER A 266
SITE 5 AC1 23 PRO A 293 ASP A 294 TYR A 299 HOH A 322
SITE 6 AC1 23 HOH A 338 HOH A 346 HOH A 351
SITE 1 AC2 4 GLN A 57 ASP A 247 GLN A 276 ARG A 279
CRYST1 71.785 71.785 181.179 90.00 90.00 90.00 P 41 21 2 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 0.013930 0.000000 0.000000 0.00000
SCALE2 0.000000 0.013930 0.000000 0.00000
SCALE3 0.000000 0.000000 0.005519 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
