HEADER TRANSFERASE 11-JAN-11 3QAS
TITLE STRUCTURE OF UNDECAPRENYL DIPHOSPHATE SYNTHASE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: UNDECAPRENYL PYROPHOSPHATE SYNTHASE;
COMPND 3 CHAIN: B, A;
COMPND 4 SYNONYM: UPP SYNTHASE, DI-TRANS,POLY-CIS-DECAPRENYLCISTRANSFERASE,
COMPND 5 UNDECAPRENYL DIPHOSPHATE SYNTHASE, UDS;
COMPND 6 EC: 2.5.1.31;
COMPND 7 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 3 ORGANISM_TAXID: 83333;
SOURCE 4 STRAIN: K12;
SOURCE 5 GENE: UPPS, ISPU, RTH, YAES;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR: PET-32
KEYWDS ALPHA-HELIX, ISOPRENOID BIOSYNTHESIS, TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR R.CAO,E.OLDFIELD
REVDAT 3 13-SEP-23 3QAS 1 REMARK
REVDAT 2 01-JUN-11 3QAS 1 JRNL
REVDAT 1 09-MAR-11 3QAS 0
JRNL AUTH W.SINKO,C.DE OLIVEIRA,S.WILLIAMS,A.VAN WYNSBERGHE,
JRNL AUTH 2 J.D.DURRANT,R.CAO,E.OLDFIELD,J.A.MCCAMMON
JRNL TITL APPLYING MOLECULAR DYNAMICS SIMULATIONS TO IDENTIFY RARELY
JRNL TITL 2 SAMPLED LIGAND-BOUND CONFORMATIONAL STATES OF UNDECAPRENYL
JRNL TITL 3 PYROPHOSPHATE SYNTHASE, AN ANTIBACTERIAL TARGET.
JRNL REF CHEM.BIOL.DRUG DES. V. 77 412 2011
JRNL REFN ISSN 1747-0277
JRNL PMID 21294851
JRNL DOI 10.1111/J.1747-0285.2011.01101.X
REMARK 2
REMARK 2 RESOLUTION. 1.70 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.5.0109
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.70
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 27.95
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.5
REMARK 3 NUMBER OF REFLECTIONS : 50646
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) : 0.186
REMARK 3 R VALUE (WORKING SET) : 0.184
REMARK 3 FREE R VALUE : 0.224
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 2711
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 1.70
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.75
REMARK 3 REFLECTION IN BIN (WORKING SET) : 3532
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 95.59
REMARK 3 BIN R VALUE (WORKING SET) : 0.2920
REMARK 3 BIN FREE R VALUE SET COUNT : 197
REMARK 3 BIN FREE R VALUE : 0.3240
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 3451
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 344
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 28.99
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.07000
REMARK 3 B22 (A**2) : -0.13000
REMARK 3 B33 (A**2) : 0.06000
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): 0.105
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.107
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.065
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 4.325
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.959
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.942
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 3522 ; 0.026 ; 0.021
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 4757 ; 2.115 ; 1.920
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 431 ; 5.912 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 189 ;38.080 ;23.492
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 595 ;15.180 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 35 ;19.322 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 508 ; 0.180 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 2732 ; 0.012 ; 0.020
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): 2141 ; 1.517 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 3403 ; 2.592 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1381 ; 3.869 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1354 ; 6.198 ; 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 17 A 34
REMARK 3 ORIGIN FOR THE GROUP (A): 20.9670 2.5295 18.1606
REMARK 3 T TENSOR
REMARK 3 T11: 0.1428 T22: 0.1470
REMARK 3 T33: 0.1711 T12: 0.0161
REMARK 3 T13: 0.0092 T23: -0.0025
REMARK 3 L TENSOR
REMARK 3 L11: 0.9291 L22: 1.0415
REMARK 3 L33: 0.9356 L12: -1.0103
REMARK 3 L13: 0.3390 L23: 0.0417
REMARK 3 S TENSOR
REMARK 3 S11: 0.0986 S12: 0.0712 S13: 0.0011
REMARK 3 S21: -0.0650 S22: -0.0931 S23: -0.0149
REMARK 3 S31: 0.0716 S32: 0.0807 S33: -0.0055
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 35 A 56
REMARK 3 ORIGIN FOR THE GROUP (A): 29.5143 2.2639 23.2413
REMARK 3 T TENSOR
REMARK 3 T11: 0.0999 T22: 0.2380
REMARK 3 T33: 0.1635 T12: 0.0347
REMARK 3 T13: -0.0146 T23: -0.0042
REMARK 3 L TENSOR
REMARK 3 L11: 1.6122 L22: 5.6024
REMARK 3 L33: 0.7646 L12: -2.4004
REMARK 3 L13: -1.2958 L23: 0.3183
REMARK 3 S TENSOR
REMARK 3 S11: -0.0710 S12: -0.2733 S13: 0.0408
REMARK 3 S21: 0.0681 S22: 0.1048 S23: -0.1230
REMARK 3 S31: -0.0291 S32: 0.4084 S33: -0.0337
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 57 A 77
REMARK 3 ORIGIN FOR THE GROUP (A): 17.2885 3.0123 22.5481
REMARK 3 T TENSOR
REMARK 3 T11: 0.1578 T22: 0.1417
REMARK 3 T33: 0.1669 T12: -0.0077
REMARK 3 T13: 0.0055 T23: 0.0147
REMARK 3 L TENSOR
REMARK 3 L11: 1.0577 L22: 0.3257
REMARK 3 L33: 1.0133 L12: -0.1105
REMARK 3 L13: 0.1980 L23: 0.2676
REMARK 3 S TENSOR
REMARK 3 S11: 0.1046 S12: -0.0635 S13: -0.1019
REMARK 3 S21: 0.0331 S22: -0.0721 S23: -0.0593
REMARK 3 S31: 0.1329 S32: -0.0031 S33: -0.0325
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 78 A 107
REMARK 3 ORIGIN FOR THE GROUP (A): 21.2564 5.5311 34.2844
REMARK 3 T TENSOR
REMARK 3 T11: 0.1486 T22: 0.1758
REMARK 3 T33: 0.1350 T12: 0.0195
REMARK 3 T13: -0.0127 T23: -0.0083
REMARK 3 L TENSOR
REMARK 3 L11: 0.1820 L22: 2.1623
REMARK 3 L33: 1.8007 L12: -0.3105
REMARK 3 L13: 0.4432 L23: 0.0202
REMARK 3 S TENSOR
REMARK 3 S11: -0.0211 S12: -0.1411 S13: 0.0341
REMARK 3 S21: 0.0306 S22: 0.1637 S23: -0.0547
REMARK 3 S31: 0.2030 S32: 0.1325 S33: -0.1426
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 108 A 121
REMARK 3 ORIGIN FOR THE GROUP (A): 13.8370 1.5861 39.2418
REMARK 3 T TENSOR
REMARK 3 T11: 0.1617 T22: 0.1957
REMARK 3 T33: 0.1219 T12: -0.0368
REMARK 3 T13: 0.0045 T23: 0.0350
REMARK 3 L TENSOR
REMARK 3 L11: 1.7706 L22: 1.3964
REMARK 3 L33: 3.8889 L12: -1.0188
REMARK 3 L13: 2.5501 L23: -1.1108
REMARK 3 S TENSOR
REMARK 3 S11: 0.0855 S12: -0.3053 S13: -0.0696
REMARK 3 S21: -0.0091 S22: 0.1221 S23: 0.0543
REMARK 3 S31: 0.2115 S32: -0.4074 S33: -0.2076
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 122 A 128
REMARK 3 ORIGIN FOR THE GROUP (A): 17.1087 9.3187 42.5921
REMARK 3 T TENSOR
REMARK 3 T11: 0.1989 T22: 0.2364
REMARK 3 T33: 0.1056 T12: -0.0149
REMARK 3 T13: 0.0024 T23: -0.0294
REMARK 3 L TENSOR
REMARK 3 L11: 2.2900 L22: 2.2187
REMARK 3 L33: 1.5744 L12: -0.8948
REMARK 3 L13: 1.8434 L23: -0.5332
REMARK 3 S TENSOR
REMARK 3 S11: 0.0403 S12: -0.3358 S13: 0.0638
REMARK 3 S21: 0.4064 S22: -0.0186 S23: -0.0374
REMARK 3 S31: -0.0032 S32: -0.2859 S33: -0.0218
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 129 A 150
REMARK 3 ORIGIN FOR THE GROUP (A): 12.1224 9.0526 30.7653
REMARK 3 T TENSOR
REMARK 3 T11: 0.1533 T22: 0.1537
REMARK 3 T33: 0.1422 T12: -0.0043
REMARK 3 T13: 0.0022 T23: -0.0060
REMARK 3 L TENSOR
REMARK 3 L11: 0.5649 L22: 0.9460
REMARK 3 L33: 0.8356 L12: 0.6764
REMARK 3 L13: 0.5599 L23: 0.7248
REMARK 3 S TENSOR
REMARK 3 S11: 0.0597 S12: -0.0728 S13: 0.0102
REMARK 3 S21: 0.1005 S22: -0.0064 S23: -0.0342
REMARK 3 S31: 0.0273 S32: -0.1135 S33: -0.0532
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 151 A 175
REMARK 3 ORIGIN FOR THE GROUP (A): -9.7045 5.3922 33.7663
REMARK 3 T TENSOR
REMARK 3 T11: 0.2308 T22: 0.2228
REMARK 3 T33: 0.1223 T12: -0.0753
REMARK 3 T13: 0.0989 T23: -0.0707
REMARK 3 L TENSOR
REMARK 3 L11: 1.9594 L22: 1.6419
REMARK 3 L33: 4.6448 L12: -0.7988
REMARK 3 L13: -1.5225 L23: -0.1964
REMARK 3 S TENSOR
REMARK 3 S11: 0.2173 S12: -0.1420 S13: 0.1679
REMARK 3 S21: 0.4448 S22: -0.1454 S23: 0.0594
REMARK 3 S31: -0.4142 S32: -0.1131 S33: -0.0720
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 176 A 222
REMARK 3 ORIGIN FOR THE GROUP (A): 9.2349 5.6952 18.7859
REMARK 3 T TENSOR
REMARK 3 T11: 0.1395 T22: 0.1468
REMARK 3 T33: 0.1503 T12: 0.0068
REMARK 3 T13: 0.0133 T23: -0.0064
REMARK 3 L TENSOR
REMARK 3 L11: 0.8029 L22: 0.2764
REMARK 3 L33: 0.3634 L12: 0.3210
REMARK 3 L13: 0.2296 L23: 0.1967
REMARK 3 S TENSOR
REMARK 3 S11: 0.0205 S12: -0.0198 S13: 0.0355
REMARK 3 S21: 0.0090 S22: -0.0433 S23: 0.0273
REMARK 3 S31: 0.0015 S32: -0.0346 S33: 0.0228
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 223 A 239
REMARK 3 ORIGIN FOR THE GROUP (A): 20.1643 12.1251 10.3694
REMARK 3 T TENSOR
REMARK 3 T11: 0.2991 T22: 0.1220
REMARK 3 T33: 0.1371 T12: -0.0100
REMARK 3 T13: 0.0646 T23: 0.0129
REMARK 3 L TENSOR
REMARK 3 L11: 6.3818 L22: 2.6924
REMARK 3 L33: 1.4826 L12: -3.9780
REMARK 3 L13: 1.2706 L23: -0.6663
REMARK 3 S TENSOR
REMARK 3 S11: 0.3124 S12: 0.2355 S13: -0.0525
REMARK 3 S21: -0.5694 S22: -0.1238 S23: -0.1004
REMARK 3 S31: -0.2711 S32: 0.1601 S33: -0.1886
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 : B 13 B 29
REMARK 3 ORIGIN FOR THE GROUP (A): 0.2613 -7.7897 4.1306
REMARK 3 T TENSOR
REMARK 3 T11: 0.1641 T22: 0.1398
REMARK 3 T33: 0.1642 T12: -0.0036
REMARK 3 T13: -0.0011 T23: 0.0138
REMARK 3 L TENSOR
REMARK 3 L11: 0.5634 L22: -0.1228
REMARK 3 L33: 0.9424 L12: 0.0441
REMARK 3 L13: -0.4218 L23: -0.2696
REMARK 3 S TENSOR
REMARK 3 S11: -0.0520 S12: 0.0070 S13: -0.0841
REMARK 3 S21: -0.0122 S22: -0.0114 S23: 0.0746
REMARK 3 S31: 0.0649 S32: 0.0335 S33: 0.0634
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 : B 30 B 44
REMARK 3 ORIGIN FOR THE GROUP (A): -4.7619 9.7850 -10.4481
REMARK 3 T TENSOR
REMARK 3 T11: 0.1655 T22: 0.1295
REMARK 3 T33: 0.1319 T12: 0.0070
REMARK 3 T13: -0.0344 T23: 0.0544
REMARK 3 L TENSOR
REMARK 3 L11: 0.8007 L22: 9.6180
REMARK 3 L33: 2.8177 L12: -0.2170
REMARK 3 L13: 0.5344 L23: -5.0014
REMARK 3 S TENSOR
REMARK 3 S11: -0.0395 S12: 0.2966 S13: 0.1247
REMARK 3 S21: 0.1888 S22: 0.1129 S23: 0.0616
REMARK 3 S31: -0.1560 S32: 0.0083 S33: -0.0734
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 : B 45 B 67
REMARK 3 ORIGIN FOR THE GROUP (A): -5.3367 -9.0571 -2.0399
REMARK 3 T TENSOR
REMARK 3 T11: 0.1672 T22: 0.1301
REMARK 3 T33: 0.1549 T12: -0.0181
REMARK 3 T13: -0.0043 T23: 0.0008
REMARK 3 L TENSOR
REMARK 3 L11: 0.6880 L22: 1.5492
REMARK 3 L33: 1.9950 L12: 0.3969
REMARK 3 L13: 0.0074 L23: -0.9684
REMARK 3 S TENSOR
REMARK 3 S11: -0.0469 S12: 0.0684 S13: -0.0209
REMARK 3 S21: -0.1508 S22: 0.0403 S23: 0.0455
REMARK 3 S31: 0.2488 S32: -0.1276 S33: 0.0066
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 : B 68 B 98
REMARK 3 ORIGIN FOR THE GROUP (A): -14.7819 0.4531 0.4712
REMARK 3 T TENSOR
REMARK 3 T11: 0.2610 T22: 0.1427
REMARK 3 T33: 0.2554 T12: -0.0486
REMARK 3 T13: -0.1274 T23: 0.0919
REMARK 3 L TENSOR
REMARK 3 L11: 5.8925 L22: 3.9695
REMARK 3 L33: 3.0321 L12: 3.0361
REMARK 3 L13: 3.2711 L23: 4.2017
REMARK 3 S TENSOR
REMARK 3 S11: -0.3469 S12: -0.1950 S13: 0.7041
REMARK 3 S21: -0.6004 S22: -0.0657 S23: 0.4555
REMARK 3 S31: -0.4246 S32: -0.1885 S33: 0.4126
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 : B 99 B 110
REMARK 3 ORIGIN FOR THE GROUP (A): -15.3504 -11.6417 2.4540
REMARK 3 T TENSOR
REMARK 3 T11: 0.1820 T22: 0.2255
REMARK 3 T33: 0.1508 T12: -0.1362
REMARK 3 T13: -0.0433 T23: 0.0552
REMARK 3 L TENSOR
REMARK 3 L11: 2.7126 L22: 5.0450
REMARK 3 L33: -0.0582 L12: 2.7527
REMARK 3 L13: 0.6189 L23: 0.9999
REMARK 3 S TENSOR
REMARK 3 S11: -0.0359 S12: -0.0681 S13: 0.0709
REMARK 3 S21: -0.1189 S22: 0.1241 S23: 0.1026
REMARK 3 S31: 0.1713 S32: -0.2225 S33: -0.0882
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 : B 111 B 119
REMARK 3 ORIGIN FOR THE GROUP (A): -22.1235 4.5429 11.1243
REMARK 3 T TENSOR
REMARK 3 T11: 0.0752 T22: 0.4216
REMARK 3 T33: 0.3433 T12: 0.1722
REMARK 3 T13: 0.0071 T23: -0.1063
REMARK 3 L TENSOR
REMARK 3 L11: 20.6807 L22: 6.1709
REMARK 3 L33: -0.4553 L12: 3.2852
REMARK 3 L13: 6.9189 L23: -3.1056
REMARK 3 S TENSOR
REMARK 3 S11: -0.6534 S12: -0.1665 S13: 1.2167
REMARK 3 S21: 0.5784 S22: 0.7156 S23: 0.9193
REMARK 3 S31: -0.0236 S32: 0.0049 S33: -0.0622
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 : B 120 B 143
REMARK 3 ORIGIN FOR THE GROUP (A): -18.8211 -8.0242 6.3271
REMARK 3 T TENSOR
REMARK 3 T11: 0.1146 T22: 0.2001
REMARK 3 T33: 0.1719 T12: -0.0407
REMARK 3 T13: 0.0075 T23: 0.0437
REMARK 3 L TENSOR
REMARK 3 L11: 1.0310 L22: 2.7727
REMARK 3 L33: 1.2500 L12: 0.0800
REMARK 3 L13: 0.2211 L23: 0.9819
REMARK 3 S TENSOR
REMARK 3 S11: -0.0896 S12: -0.1143 S13: 0.0434
REMARK 3 S21: 0.0718 S22: 0.0762 S23: 0.2264
REMARK 3 S31: 0.0842 S32: -0.2636 S33: 0.0134
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 : B 144 B 179
REMARK 3 ORIGIN FOR THE GROUP (A): -10.2261 -2.3913 27.9613
REMARK 3 T TENSOR
REMARK 3 T11: 0.1277 T22: 0.2586
REMARK 3 T33: 0.1463 T12: -0.0698
REMARK 3 T13: 0.0249 T23: -0.0298
REMARK 3 L TENSOR
REMARK 3 L11: 0.3909 L22: 1.2841
REMARK 3 L33: 1.7523 L12: -0.2998
REMARK 3 L13: -0.7767 L23: -1.0273
REMARK 3 S TENSOR
REMARK 3 S11: 0.0267 S12: -0.0397 S13: -0.0090
REMARK 3 S21: 0.0510 S22: -0.0372 S23: 0.1543
REMARK 3 S31: 0.0342 S32: -0.1648 S33: 0.0105
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 : B 180 B 226
REMARK 3 ORIGIN FOR THE GROUP (A): 1.0193 -2.1546 7.9665
REMARK 3 T TENSOR
REMARK 3 T11: 0.1452 T22: 0.1408
REMARK 3 T33: 0.1430 T12: 0.0023
REMARK 3 T13: 0.0061 T23: 0.0054
REMARK 3 L TENSOR
REMARK 3 L11: 0.4831 L22: 0.1603
REMARK 3 L33: 0.9976 L12: 0.1889
REMARK 3 L13: 0.2318 L23: -0.0314
REMARK 3 S TENSOR
REMARK 3 S11: 0.0274 S12: -0.0358 S13: 0.0007
REMARK 3 S21: -0.0225 S22: -0.0403 S23: 0.0193
REMARK 3 S31: 0.0050 S32: 0.0274 S33: 0.0129
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 : B 227 B 240
REMARK 3 ORIGIN FOR THE GROUP (A): 8.7666 -10.7418 1.5022
REMARK 3 T TENSOR
REMARK 3 T11: 0.1809 T22: 0.1340
REMARK 3 T33: 0.1574 T12: 0.0453
REMARK 3 T13: 0.0074 T23: -0.0075
REMARK 3 L TENSOR
REMARK 3 L11: 2.7397 L22: 2.1299
REMARK 3 L33: 3.9257 L12: -1.5305
REMARK 3 L13: 3.4452 L23: -1.5887
REMARK 3 S TENSOR
REMARK 3 S11: 0.1118 S12: 0.1739 S13: -0.0579
REMARK 3 S21: -0.0603 S22: 0.0034 S23: -0.1331
REMARK 3 S31: 0.2670 S32: 0.1683 S33: -0.1152
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.40
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 3QAS COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 13-JAN-11.
REMARK 100 THE DEPOSITION ID IS D_1000063409.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 19-DEC-09
REMARK 200 TEMPERATURE (KELVIN) : 123
REMARK 200 PH : 7.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 21-ID-F
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97872
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 225 MM CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 50646
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.700
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 97.5
REMARK 200 DATA REDUNDANCY : 7.200
REMARK 200 R MERGE (I) : 0.05100
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 51.2000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.70
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.73
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.7
REMARK 200 DATA REDUNDANCY IN SHELL : 5.80
REMARK 200 R MERGE FOR SHELL (I) : 0.40000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 3.700
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASES
REMARK 200 STARTING MODEL: 2E99
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 41.80
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.11
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 5% PEG 4000, PH 7.5, VAPOR DIFFUSION,
REMARK 280 HANGING DROP, TEMPERATURE 298.15K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
REMARK 290 4555 X+1/2,-Y+1/2,-Z
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 31.31650
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 55.90800
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 34.38100
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 55.90800
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 31.31650
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 34.38100
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
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: 3710 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 20460 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -12.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, 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 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 B 1
REMARK 465 MET B 2
REMARK 465 LEU B 3
REMARK 465 SER B 4
REMARK 465 ALA B 5
REMARK 465 THR B 6
REMARK 465 GLN B 7
REMARK 465 PRO B 8
REMARK 465 LEU B 9
REMARK 465 SER B 10
REMARK 465 GLU B 11
REMARK 465 LYS B 12
REMARK 465 GLU B 73
REMARK 465 ASN B 74
REMARK 465 TRP B 75
REMARK 465 ASN B 76
REMARK 465 ARG B 77
REMARK 465 PRO B 78
REMARK 465 ALA B 79
REMARK 465 GLN B 80
REMARK 465 GLU B 81
REMARK 465 VAL B 82
REMARK 465 SER B 83
REMARK 465 ALA B 84
REMARK 465 LEU B 85
REMARK 465 MET B 86
REMARK 465 GLU B 87
REMARK 465 LEU B 88
REMARK 465 PHE B 89
REMARK 465 ARG B 241
REMARK 465 ARG B 242
REMARK 465 PHE B 243
REMARK 465 GLY B 244
REMARK 465 GLY B 245
REMARK 465 THR B 246
REMARK 465 GLU B 247
REMARK 465 PRO B 248
REMARK 465 GLY B 249
REMARK 465 ASP B 250
REMARK 465 GLU B 251
REMARK 465 THR B 252
REMARK 465 ALA B 253
REMARK 465 MET A 1
REMARK 465 MET A 2
REMARK 465 LEU A 3
REMARK 465 SER A 4
REMARK 465 ALA A 5
REMARK 465 THR A 6
REMARK 465 GLN A 7
REMARK 465 PRO A 8
REMARK 465 LEU A 9
REMARK 465 SER A 10
REMARK 465 GLU A 11
REMARK 465 LYS A 12
REMARK 465 LEU A 13
REMARK 465 PRO A 14
REMARK 465 ALA A 15
REMARK 465 HIS A 16
REMARK 465 GLU A 240
REMARK 465 ARG A 241
REMARK 465 ARG A 242
REMARK 465 PHE A 243
REMARK 465 GLY A 244
REMARK 465 GLY A 245
REMARK 465 THR A 246
REMARK 465 GLU A 247
REMARK 465 PRO A 248
REMARK 465 GLY A 249
REMARK 465 ASP A 250
REMARK 465 GLU A 251
REMARK 465 THR A 252
REMARK 465 ALA A 253
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 VAL B 90 CG1 CG2
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 NH1 ARG A 108 OE2 GLU A 185 2.05
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 RES CSSEQI ATM2 DEVIATION
REMARK 500 CYS B 18 CB CYS B 18 SG -0.160
REMARK 500 PHE B 224 CE2 PHE B 224 CD2 0.130
REMARK 500 CYS A 18 CB CYS A 18 SG -0.130
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 PRO B 14 C - N - CA ANGL. DEV. = -9.1 DEGREES
REMARK 500 PHE B 224 CB - CG - CD2 ANGL. DEV. = -4.3 DEGREES
REMARK 500 ARG B 239 NE - CZ - NH1 ANGL. DEV. = -5.2 DEGREES
REMARK 500 ARG B 239 NE - CZ - NH2 ANGL. DEV. = 3.9 DEGREES
REMARK 500 ARG A 123 NE - CZ - NH2 ANGL. DEV. = -3.8 DEGREES
REMARK 500 PHE A 204 CB - CG - CD2 ANGL. DEV. = -5.2 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 HIS B 199 68.99 -117.09
REMARK 500 PHE B 204 -147.91 -78.52
REMARK 500 LEU B 206 -61.17 -121.23
REMARK 500 ASP B 225 -163.05 -113.53
REMARK 500 ASN A 76 58.52 -104.34
REMARK 500 HIS A 199 63.83 -111.22
REMARK 500 PHE A 204 -150.42 -71.61
REMARK 500 LEU A 206 -62.67 -120.49
REMARK 500 ASP A 225 -162.42 -119.57
REMARK 500
REMARK 500 REMARK: NULL
DBREF 3QAS B 1 253 UNP P60472 UPPS_ECOLI 1 253
DBREF 3QAS A 1 253 UNP P60472 UPPS_ECOLI 1 253
SEQRES 1 B 253 MET MET LEU SER ALA THR GLN PRO LEU SER GLU LYS LEU
SEQRES 2 B 253 PRO ALA HIS GLY CYS ARG HIS VAL ALA ILE ILE MET ASP
SEQRES 3 B 253 GLY ASN GLY ARG TRP ALA LYS LYS GLN GLY LYS ILE ARG
SEQRES 4 B 253 ALA PHE GLY HIS LYS ALA GLY ALA LYS SER VAL ARG ARG
SEQRES 5 B 253 ALA VAL SER PHE ALA ALA ASN ASN GLY ILE GLU ALA LEU
SEQRES 6 B 253 THR LEU TYR ALA PHE SER SER GLU ASN TRP ASN ARG PRO
SEQRES 7 B 253 ALA GLN GLU VAL SER ALA LEU MET GLU LEU PHE VAL TRP
SEQRES 8 B 253 ALA LEU ASP SER GLU VAL LYS SER LEU HIS ARG HIS ASN
SEQRES 9 B 253 VAL ARG LEU ARG ILE ILE GLY ASP THR SER ARG PHE ASN
SEQRES 10 B 253 SER ARG LEU GLN GLU ARG ILE ARG LYS SER GLU ALA LEU
SEQRES 11 B 253 THR ALA GLY ASN THR GLY LEU THR LEU ASN ILE ALA ALA
SEQRES 12 B 253 ASN TYR GLY GLY ARG TRP ASP ILE VAL GLN GLY VAL ARG
SEQRES 13 B 253 GLN LEU ALA GLU LYS VAL GLN GLN GLY ASN LEU GLN PRO
SEQRES 14 B 253 ASP GLN ILE ASP GLU GLU MET LEU ASN GLN HIS VAL CYS
SEQRES 15 B 253 MET HIS GLU LEU ALA PRO VAL ASP LEU VAL ILE ARG THR
SEQRES 16 B 253 GLY GLY GLU HIS ARG ILE SER ASN PHE LEU LEU TRP GLN
SEQRES 17 B 253 ILE ALA TYR ALA GLU LEU TYR PHE THR ASP VAL LEU TRP
SEQRES 18 B 253 PRO ASP PHE ASP GLU GLN ASP PHE GLU GLY ALA LEU ASN
SEQRES 19 B 253 ALA PHE ALA ASN ARG GLU ARG ARG PHE GLY GLY THR GLU
SEQRES 20 B 253 PRO GLY ASP GLU THR ALA
SEQRES 1 A 253 MET MET LEU SER ALA THR GLN PRO LEU SER GLU LYS LEU
SEQRES 2 A 253 PRO ALA HIS GLY CYS ARG HIS VAL ALA ILE ILE MET ASP
SEQRES 3 A 253 GLY ASN GLY ARG TRP ALA LYS LYS GLN GLY LYS ILE ARG
SEQRES 4 A 253 ALA PHE GLY HIS LYS ALA GLY ALA LYS SER VAL ARG ARG
SEQRES 5 A 253 ALA VAL SER PHE ALA ALA ASN ASN GLY ILE GLU ALA LEU
SEQRES 6 A 253 THR LEU TYR ALA PHE SER SER GLU ASN TRP ASN ARG PRO
SEQRES 7 A 253 ALA GLN GLU VAL SER ALA LEU MET GLU LEU PHE VAL TRP
SEQRES 8 A 253 ALA LEU ASP SER GLU VAL LYS SER LEU HIS ARG HIS ASN
SEQRES 9 A 253 VAL ARG LEU ARG ILE ILE GLY ASP THR SER ARG PHE ASN
SEQRES 10 A 253 SER ARG LEU GLN GLU ARG ILE ARG LYS SER GLU ALA LEU
SEQRES 11 A 253 THR ALA GLY ASN THR GLY LEU THR LEU ASN ILE ALA ALA
SEQRES 12 A 253 ASN TYR GLY GLY ARG TRP ASP ILE VAL GLN GLY VAL ARG
SEQRES 13 A 253 GLN LEU ALA GLU LYS VAL GLN GLN GLY ASN LEU GLN PRO
SEQRES 14 A 253 ASP GLN ILE ASP GLU GLU MET LEU ASN GLN HIS VAL CYS
SEQRES 15 A 253 MET HIS GLU LEU ALA PRO VAL ASP LEU VAL ILE ARG THR
SEQRES 16 A 253 GLY GLY GLU HIS ARG ILE SER ASN PHE LEU LEU TRP GLN
SEQRES 17 A 253 ILE ALA TYR ALA GLU LEU TYR PHE THR ASP VAL LEU TRP
SEQRES 18 A 253 PRO ASP PHE ASP GLU GLN ASP PHE GLU GLY ALA LEU ASN
SEQRES 19 A 253 ALA PHE ALA ASN ARG GLU ARG ARG PHE GLY GLY THR GLU
SEQRES 20 A 253 PRO GLY ASP GLU THR ALA
FORMUL 3 HOH *344(H2 O)
HELIX 1 1 GLY B 27 GLN B 35 1 9
HELIX 2 2 ILE B 38 ASN B 60 1 23
HELIX 3 3 TRP B 91 HIS B 103 1 13
HELIX 4 4 ASN B 117 ALA B 132 1 16
HELIX 5 5 GLY B 146 GLN B 164 1 19
HELIX 6 6 GLN B 168 ILE B 172 5 5
HELIX 7 7 ASP B 173 GLN B 179 1 7
HELIX 8 8 LEU B 206 ALA B 210 5 5
HELIX 9 9 LEU B 220 PHE B 224 5 5
HELIX 10 10 ASP B 225 GLU B 240 1 16
HELIX 11 11 GLY A 27 GLY A 36 1 10
HELIX 12 12 ILE A 38 ASN A 60 1 23
HELIX 13 13 SER A 71 TRP A 75 5 5
HELIX 14 14 PRO A 78 SER A 95 1 18
HELIX 15 15 GLU A 96 HIS A 103 1 8
HELIX 16 16 ASN A 117 ALA A 132 1 16
HELIX 17 17 GLY A 146 GLN A 164 1 19
HELIX 18 18 GLN A 168 ILE A 172 5 5
HELIX 19 19 ASP A 173 GLN A 179 1 7
HELIX 20 20 LEU A 206 ALA A 210 5 5
HELIX 21 21 LEU A 220 PHE A 224 5 5
HELIX 22 22 ASP A 225 ARG A 239 1 15
SHEET 1 A 6 ARG B 106 ILE B 110 0
SHEET 2 A 6 THR B 138 ALA B 142 1 O ILE B 141 N ARG B 108
SHEET 3 A 6 ALA B 64 TYR B 68 1 N LEU B 67 O ALA B 142
SHEET 4 A 6 HIS B 20 ILE B 24 1 N ILE B 23 O THR B 66
SHEET 5 A 6 LEU B 191 ARG B 194 1 O ILE B 193 N ILE B 24
SHEET 6 A 6 GLU B 213 PHE B 216 1 O TYR B 215 N VAL B 192
SHEET 1 B 6 ARG A 106 ILE A 110 0
SHEET 2 B 6 THR A 138 ALA A 142 1 O LEU A 139 N ARG A 106
SHEET 3 B 6 ALA A 64 TYR A 68 1 N LEU A 67 O ALA A 142
SHEET 4 B 6 HIS A 20 ILE A 24 1 N ILE A 23 O TYR A 68
SHEET 5 B 6 LEU A 191 ARG A 194 1 O ILE A 193 N ILE A 24
SHEET 6 B 6 GLU A 213 PHE A 216 1 O TYR A 215 N VAL A 192
CRYST1 62.633 68.762 111.816 90.00 90.00 90.00 P 21 21 21 8
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.015966 0.000000 0.000000 0.00000
SCALE2 0.000000 0.014543 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008943 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
