HEADER TRANSFERASE/TRANSFERASE INHIBITOR 15-JUN-11 3SH0
TITLE CRYSTAL STRUCTURE OF E. COLI UNDECAPRENYL PYROPHOSPHATE SYNTHASE IN
TITLE 2 COMPLEX WITH BPH-1065
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, B0174, JW0169;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS ALPHA/BETA, TRANSFERASE-TRANSFERASE INHIBITOR COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR R.CAO,Y.-L.LIU,E.OLDFIELD
REVDAT 3 13-SEP-23 3SH0 1 REMARK
REVDAT 2 16-JAN-13 3SH0 1 JRNL
REVDAT 1 19-DEC-12 3SH0 0
JRNL AUTH W.ZHU,Y.ZHANG,W.SINKO,M.E.HENSLER,J.OLSON,K.J.MOLOHON,
JRNL AUTH 2 S.LINDERT,R.CAO,K.LI,K.WANG,Y.WANG,Y.L.LIU,A.SANKOVSKY,
JRNL AUTH 3 C.A.DE OLIVEIRA,D.A.MITCHELL,V.NIZET,J.A.MCCAMMON,E.OLDFIELD
JRNL TITL ANTIBACTERIAL DRUG LEADS TARGETING ISOPRENOID BIOSYNTHESIS.
JRNL REF PROC.NATL.ACAD.SCI.USA V. 110 123 2013
JRNL REFN ISSN 0027-8424
JRNL PMID 23248302
JRNL DOI 10.1073/PNAS.1219899110
REMARK 2
REMARK 2 RESOLUTION. 1.84 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) : 1.84
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 35.71
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.0
REMARK 3 NUMBER OF REFLECTIONS : 42354
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) : 0.170
REMARK 3 R VALUE (WORKING SET) : 0.168
REMARK 3 FREE R VALUE : 0.211
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 2129
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) : 1.84
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.89
REMARK 3 REFLECTION IN BIN (WORKING SET) : 2706
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 91.56
REMARK 3 BIN R VALUE (WORKING SET) : 0.2660
REMARK 3 BIN FREE R VALUE SET COUNT : 125
REMARK 3 BIN FREE R VALUE : 0.3360
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 3397
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 69
REMARK 3 SOLVENT ATOMS : 315
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 30.23
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.01000
REMARK 3 B22 (A**2) : -0.07000
REMARK 3 B33 (A**2) : 0.05000
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): 0.123
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.076
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 5.469
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.961
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.940
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 3532 ; 0.024 ; 0.021
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 4755 ; 1.901 ; 1.939
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 424 ; 5.649 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 184 ;37.569 ;23.424
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 585 ;14.541 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 34 ;19.616 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 502 ; 0.160 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 2715 ; 0.010 ; 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): 2109 ; 1.231 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 3350 ; 2.049 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1423 ; 3.318 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1405 ; 5.185 ; 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): 21.1290 2.5810 18.0680
REMARK 3 T TENSOR
REMARK 3 T11: 0.1443 T22: 0.1566
REMARK 3 T33: 0.1686 T12: 0.0210
REMARK 3 T13: 0.0218 T23: -0.0011
REMARK 3 L TENSOR
REMARK 3 L11: 2.6969 L22: 2.3736
REMARK 3 L33: 1.7746 L12: -2.3902
REMARK 3 L13: -0.0426 L23: 0.5669
REMARK 3 S TENSOR
REMARK 3 S11: 0.1023 S12: 0.0606 S13: -0.0312
REMARK 3 S21: -0.1484 S22: -0.0485 S23: -0.0281
REMARK 3 S31: 0.1166 S32: 0.1636 S33: -0.0538
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 49
REMARK 3 ORIGIN FOR THE GROUP (A): 31.6540 -2.6620 23.3260
REMARK 3 T TENSOR
REMARK 3 T11: 0.1230 T22: 0.5175
REMARK 3 T33: 0.1835 T12: 0.1333
REMARK 3 T13: 0.0134 T23: 0.0733
REMARK 3 L TENSOR
REMARK 3 L11: 5.9461 L22: 15.1908
REMARK 3 L33: 1.4255 L12: -8.9647
REMARK 3 L13: -2.8033 L23: 3.8145
REMARK 3 S TENSOR
REMARK 3 S11: -0.3001 S12: -0.6852 S13: -0.1365
REMARK 3 S21: 0.2922 S22: 0.1818 S23: 0.0853
REMARK 3 S31: 0.1814 S32: 0.5326 S33: 0.1183
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 50 A 69
REMARK 3 ORIGIN FOR THE GROUP (A): 20.6610 12.8940 22.4030
REMARK 3 T TENSOR
REMARK 3 T11: 0.1422 T22: 0.1499
REMARK 3 T33: 0.1476 T12: -0.0175
REMARK 3 T13: 0.0190 T23: 0.0075
REMARK 3 L TENSOR
REMARK 3 L11: 2.2835 L22: 1.7694
REMARK 3 L33: 2.3169 L12: -0.4492
REMARK 3 L13: -0.5104 L23: 0.4500
REMARK 3 S TENSOR
REMARK 3 S11: 0.0867 S12: -0.1015 S13: 0.1335
REMARK 3 S21: -0.0452 S22: -0.0329 S23: -0.1502
REMARK 3 S31: -0.1056 S32: 0.1862 S33: -0.0538
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 70 A 95
REMARK 3 ORIGIN FOR THE GROUP (A): 22.3420 1.4660 33.0770
REMARK 3 T TENSOR
REMARK 3 T11: 0.6193 T22: 1.0621
REMARK 3 T33: 0.6965 T12: 0.1866
REMARK 3 T13: -0.3039 T23: -0.3542
REMARK 3 L TENSOR
REMARK 3 L11: 5.9487 L22: 2.5940
REMARK 3 L33: 0.2477 L12: -3.9152
REMARK 3 L13: 1.2097 L23: -0.7923
REMARK 3 S TENSOR
REMARK 3 S11: -0.0762 S12: -0.3632 S13: -0.8073
REMARK 3 S21: 0.0357 S22: 0.3206 S23: 0.4684
REMARK 3 S31: 0.0086 S32: -0.0483 S33: -0.2444
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 96 A 107
REMARK 3 ORIGIN FOR THE GROUP (A): 22.8780 16.9830 34.0090
REMARK 3 T TENSOR
REMARK 3 T11: 0.1181 T22: 0.2078
REMARK 3 T33: 0.1553 T12: -0.0344
REMARK 3 T13: -0.0211 T23: -0.0066
REMARK 3 L TENSOR
REMARK 3 L11: 2.2058 L22: 5.2422
REMARK 3 L33: 5.1193 L12: -1.4867
REMARK 3 L13: -1.3576 L23: -0.2568
REMARK 3 S TENSOR
REMARK 3 S11: -0.1150 S12: -0.3716 S13: 0.0717
REMARK 3 S21: 0.0430 S22: 0.0235 S23: -0.4394
REMARK 3 S31: -0.1743 S32: 0.4861 S33: 0.0916
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 108 A 122
REMARK 3 ORIGIN FOR THE GROUP (A): 13.6830 2.0110 39.9090
REMARK 3 T TENSOR
REMARK 3 T11: 0.1738 T22: 0.2146
REMARK 3 T33: 0.1407 T12: -0.0614
REMARK 3 T13: -0.0241 T23: 0.0589
REMARK 3 L TENSOR
REMARK 3 L11: 2.1596 L22: 0.9364
REMARK 3 L33: 6.2476 L12: -0.4973
REMARK 3 L13: 3.2388 L23: 0.2973
REMARK 3 S TENSOR
REMARK 3 S11: 0.0891 S12: -0.3367 S13: -0.1496
REMARK 3 S21: 0.1075 S22: 0.0817 S23: 0.0178
REMARK 3 S31: 0.2262 S32: -0.4505 S33: -0.1707
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 123 A 151
REMARK 3 ORIGIN FOR THE GROUP (A): 12.7240 8.7940 33.5130
REMARK 3 T TENSOR
REMARK 3 T11: 0.1534 T22: 0.1678
REMARK 3 T33: 0.1236 T12: 0.0009
REMARK 3 T13: 0.0013 T23: 0.0013
REMARK 3 L TENSOR
REMARK 3 L11: 0.9773 L22: 0.5931
REMARK 3 L33: 1.1014 L12: 0.5557
REMARK 3 L13: 0.6203 L23: 0.6275
REMARK 3 S TENSOR
REMARK 3 S11: 0.0538 S12: -0.1630 S13: -0.0293
REMARK 3 S21: 0.0909 S22: -0.0217 S23: -0.0571
REMARK 3 S31: 0.0231 S32: -0.1055 S33: -0.0321
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 152 A 178
REMARK 3 ORIGIN FOR THE GROUP (A): -9.5500 6.0360 33.3970
REMARK 3 T TENSOR
REMARK 3 T11: 0.1551 T22: 0.2361
REMARK 3 T33: 0.1242 T12: -0.0279
REMARK 3 T13: 0.0754 T23: -0.0715
REMARK 3 L TENSOR
REMARK 3 L11: 1.7619 L22: 2.4359
REMARK 3 L33: 3.7411 L12: -0.0054
REMARK 3 L13: -2.2207 L23: -0.3850
REMARK 3 S TENSOR
REMARK 3 S11: 0.1985 S12: -0.1681 S13: 0.2276
REMARK 3 S21: 0.4215 S22: -0.0889 S23: 0.1293
REMARK 3 S31: -0.3015 S32: -0.1632 S33: -0.1096
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 179 A 223
REMARK 3 ORIGIN FOR THE GROUP (A): 10.6000 5.3970 18.2240
REMARK 3 T TENSOR
REMARK 3 T11: 0.1417 T22: 0.1433
REMARK 3 T33: 0.1372 T12: 0.0058
REMARK 3 T13: 0.0146 T23: -0.0015
REMARK 3 L TENSOR
REMARK 3 L11: 1.0478 L22: 0.5641
REMARK 3 L33: 0.7809 L12: 0.3550
REMARK 3 L13: 0.1647 L23: 0.2313
REMARK 3 S TENSOR
REMARK 3 S11: -0.0027 S12: -0.0027 S13: 0.0113
REMARK 3 S21: -0.0026 S22: -0.0334 S23: 0.0131
REMARK 3 S31: -0.0116 S32: -0.0291 S33: 0.0361
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 224 A 239
REMARK 3 ORIGIN FOR THE GROUP (A): 19.6030 12.8520 10.2070
REMARK 3 T TENSOR
REMARK 3 T11: 0.4642 T22: 0.1163
REMARK 3 T33: 0.1376 T12: -0.0345
REMARK 3 T13: 0.1222 T23: 0.0096
REMARK 3 L TENSOR
REMARK 3 L11: 10.4244 L22: 5.8532
REMARK 3 L33: 3.0465 L12: -6.3958
REMARK 3 L13: 2.7281 L23: -1.9617
REMARK 3 S TENSOR
REMARK 3 S11: 0.3785 S12: 0.3417 S13: 0.0373
REMARK 3 S21: -0.9952 S22: -0.1388 S23: -0.2471
REMARK 3 S31: -0.3282 S32: 0.1909 S33: -0.2396
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): 0.4070 -7.6870 4.1510
REMARK 3 T TENSOR
REMARK 3 T11: 0.1755 T22: 0.1407
REMARK 3 T33: 0.1588 T12: -0.0002
REMARK 3 T13: 0.0182 T23: 0.0093
REMARK 3 L TENSOR
REMARK 3 L11: 0.9065 L22: 0.1408
REMARK 3 L33: 1.2436 L12: 0.2227
REMARK 3 L13: -0.4547 L23: 0.1762
REMARK 3 S TENSOR
REMARK 3 S11: -0.0426 S12: -0.0383 S13: -0.0819
REMARK 3 S21: 0.0415 S22: -0.0067 S23: -0.0027
REMARK 3 S31: 0.1281 S32: 0.0691 S33: 0.0493
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 48
REMARK 3 ORIGIN FOR THE GROUP (A): -5.1400 8.2770 -10.5120
REMARK 3 T TENSOR
REMARK 3 T11: 0.1535 T22: 0.1574
REMARK 3 T33: 0.1327 T12: -0.0001
REMARK 3 T13: -0.0364 T23: 0.0438
REMARK 3 L TENSOR
REMARK 3 L11: 2.0096 L22: 9.3749
REMARK 3 L33: 3.4671 L12: 1.1793
REMARK 3 L13: -1.3411 L23: -4.1937
REMARK 3 S TENSOR
REMARK 3 S11: 0.0149 S12: 0.1984 S13: 0.1971
REMARK 3 S21: -0.0678 S22: 0.0973 S23: 0.3092
REMARK 3 S31: -0.1295 S32: -0.0780 S33: -0.1123
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 49 B 72
REMARK 3 ORIGIN FOR THE GROUP (A): -4.6900 -6.5540 0.3820
REMARK 3 T TENSOR
REMARK 3 T11: 0.1532 T22: 0.1328
REMARK 3 T33: 0.1415 T12: -0.0044
REMARK 3 T13: 0.0056 T23: 0.0036
REMARK 3 L TENSOR
REMARK 3 L11: 0.9147 L22: 1.1117
REMARK 3 L33: 2.1618 L12: 0.7441
REMARK 3 L13: 0.0612 L23: -0.0270
REMARK 3 S TENSOR
REMARK 3 S11: -0.0387 S12: 0.0242 S13: -0.0051
REMARK 3 S21: -0.0394 S22: 0.0498 S23: 0.0607
REMARK 3 S31: 0.1207 S32: -0.0897 S33: -0.0111
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 80 B 94
REMARK 3 ORIGIN FOR THE GROUP (A): -17.2700 5.6230 0.6170
REMARK 3 T TENSOR
REMARK 3 T11: 0.2161 T22: 0.2024
REMARK 3 T33: 0.1732 T12: 0.0857
REMARK 3 T13: 0.0342 T23: 0.0623
REMARK 3 L TENSOR
REMARK 3 L11: 6.5164 L22: 18.6785
REMARK 3 L33: 2.9144 L12: 2.4315
REMARK 3 L13: 1.5940 L23: 5.9562
REMARK 3 S TENSOR
REMARK 3 S11: -0.1476 S12: 0.3413 S13: 0.1970
REMARK 3 S21: -0.9199 S22: 0.1099 S23: 0.1383
REMARK 3 S31: -0.4744 S32: -0.1933 S33: 0.0377
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 95 B 114
REMARK 3 ORIGIN FOR THE GROUP (A): -16.4020 -8.6140 3.0870
REMARK 3 T TENSOR
REMARK 3 T11: 0.1519 T22: 0.1956
REMARK 3 T33: 0.1929 T12: -0.0747
REMARK 3 T13: -0.0024 T23: 0.0324
REMARK 3 L TENSOR
REMARK 3 L11: 1.5651 L22: 4.5247
REMARK 3 L33: 1.2285 L12: 0.5607
REMARK 3 L13: 1.2659 L23: 1.3007
REMARK 3 S TENSOR
REMARK 3 S11: 0.0126 S12: -0.2455 S13: -0.0295
REMARK 3 S21: -0.0454 S22: 0.0005 S23: 0.2886
REMARK 3 S31: 0.0634 S32: -0.2323 S33: -0.0132
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 115 B 128
REMARK 3 ORIGIN FOR THE GROUP (A): -24.6860 -0.7830 8.3800
REMARK 3 T TENSOR
REMARK 3 T11: 0.0166 T22: 0.3957
REMARK 3 T33: 0.2741 T12: 0.0212
REMARK 3 T13: 0.0467 T23: 0.0021
REMARK 3 L TENSOR
REMARK 3 L11: 4.5267 L22: 22.6320
REMARK 3 L33: 3.8226 L12: -3.2409
REMARK 3 L13: -3.2253 L23: 3.7807
REMARK 3 S TENSOR
REMARK 3 S11: -0.0280 S12: 0.2253 S13: 0.0934
REMARK 3 S21: 0.3955 S22: 0.0554 S23: 0.9831
REMARK 3 S31: -0.0474 S32: -0.5804 S33: -0.0274
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 129 B 155
REMARK 3 ORIGIN FOR THE GROUP (A): -11.6710 -4.4920 12.3030
REMARK 3 T TENSOR
REMARK 3 T11: 0.1316 T22: 0.2071
REMARK 3 T33: 0.1740 T12: -0.0127
REMARK 3 T13: 0.0106 T23: 0.0172
REMARK 3 L TENSOR
REMARK 3 L11: 0.2612 L22: 0.3175
REMARK 3 L33: 1.2044 L12: 0.2204
REMARK 3 L13: 0.1559 L23: 0.4293
REMARK 3 S TENSOR
REMARK 3 S11: -0.0214 S12: -0.1269 S13: 0.0269
REMARK 3 S21: -0.0071 S22: -0.0566 S23: 0.0907
REMARK 3 S31: 0.0545 S32: -0.1839 S33: 0.0780
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 156 B 179
REMARK 3 ORIGIN FOR THE GROUP (A): -10.8040 -4.9530 32.2780
REMARK 3 T TENSOR
REMARK 3 T11: 0.1563 T22: 0.2203
REMARK 3 T33: 0.1156 T12: -0.0547
REMARK 3 T13: 0.0421 T23: 0.0103
REMARK 3 L TENSOR
REMARK 3 L11: 1.9579 L22: 3.0352
REMARK 3 L33: 2.8859 L12: 0.3791
REMARK 3 L13: -1.9508 L23: -1.3086
REMARK 3 S TENSOR
REMARK 3 S11: -0.0351 S12: -0.0730 S13: -0.1052
REMARK 3 S21: 0.2192 S22: -0.0023 S23: 0.2872
REMARK 3 S31: -0.0063 S32: -0.1291 S33: 0.0374
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 222
REMARK 3 ORIGIN FOR THE GROUP (A): 1.0010 -1.8530 9.5830
REMARK 3 T TENSOR
REMARK 3 T11: 0.1425 T22: 0.1405
REMARK 3 T33: 0.1411 T12: 0.0038
REMARK 3 T13: 0.0142 T23: 0.0085
REMARK 3 L TENSOR
REMARK 3 L11: 0.3831 L22: 0.1804
REMARK 3 L33: 1.4551 L12: 0.1820
REMARK 3 L13: 0.1861 L23: 0.0834
REMARK 3 S TENSOR
REMARK 3 S11: 0.0261 S12: -0.0507 S13: -0.0001
REMARK 3 S21: 0.0059 S22: -0.0334 S23: 0.0172
REMARK 3 S31: 0.0033 S32: 0.0252 S33: 0.0073
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 223 B 240
REMARK 3 ORIGIN FOR THE GROUP (A): 7.1900 -9.0920 -0.6480
REMARK 3 T TENSOR
REMARK 3 T11: 0.1646 T22: 0.1212
REMARK 3 T33: 0.1510 T12: 0.0366
REMARK 3 T13: 0.0176 T23: -0.0179
REMARK 3 L TENSOR
REMARK 3 L11: 3.4544 L22: 2.8468
REMARK 3 L33: 4.5680 L12: -1.8710
REMARK 3 L13: 2.8685 L23: -2.7201
REMARK 3 S TENSOR
REMARK 3 S11: 0.0780 S12: 0.1777 S13: -0.1862
REMARK 3 S21: -0.0583 S22: 0.0063 S23: -0.1112
REMARK 3 S31: 0.1763 S32: 0.2474 S33: -0.0842
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 : 1.40
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 U VALUES : RESIDUAL ONLY
REMARK 4
REMARK 4 3SH0 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 15-JUN-11.
REMARK 100 THE DEPOSITION ID IS D_1000066190.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 06-JUN-10
REMARK 200 TEMPERATURE (KELVIN) : 298
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-D
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9787
REMARK 200 MONOCHROMATOR : SI(111)
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 300 MM CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK, HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 42560
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.840
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 1.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.3
REMARK 200 DATA REDUNDANCY : 10.00
REMARK 200 R MERGE (I) : 0.06500
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 8.1000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.84
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.87
REMARK 200 COMPLETENESS FOR SHELL (%) : 89.2
REMARK 200 DATA REDUNDANCY IN SHELL : 5.30
REMARK 200 R MERGE FOR SHELL (I) : 0.64200
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 2E98
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 42.02
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.12
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 50MM HEPES, PH 7.5, 5% PEG 4,000,
REMARK 280 VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 298K
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 31.38250
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 56.02800
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 34.36200
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 56.02800
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 31.38250
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 34.36200
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 3680 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 20030 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -11.0 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 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 SER A 72
REMARK 465 GLU A 73
REMARK 465 ASN A 74
REMARK 465 TRP A 75
REMARK 465 ASN A 76
REMARK 465 ARG A 77
REMARK 465 PRO A 78
REMARK 465 ALA A 79
REMARK 465 GLN A 80
REMARK 465 GLU A 81
REMARK 465 VAL A 82
REMARK 465 SER A 83
REMARK 465 ALA A 84
REMARK 465 LEU A 85
REMARK 465 MET A 86
REMARK 465 GLU A 87
REMARK 465 LEU A 88
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 GLN B 80 CG CD OE1 NE2
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 -0.148
REMARK 500 ARG B 106 CD ARG B 106 NE -0.114
REMARK 500 VAL A 54 CB VAL A 54 CG2 0.128
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 ARG B 106 CB - CG - CD ANGL. DEV. = -18.1 DEGREES
REMARK 500 ARG B 106 NE - CZ - NH1 ANGL. DEV. = 6.2 DEGREES
REMARK 500 ARG B 106 NE - CZ - NH2 ANGL. DEV. = -7.8 DEGREES
REMARK 500 ARG B 239 NE - CZ - NH1 ANGL. DEV. = -4.4 DEGREES
REMARK 500 ARG B 239 NE - CZ - NH2 ANGL. DEV. = 3.3 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 B 71 -53.65 -127.30
REMARK 500 HIS B 199 68.61 -112.47
REMARK 500 PHE B 204 -147.25 -80.66
REMARK 500 LEU B 206 -63.38 -121.86
REMARK 500 ASP B 225 -164.62 -118.53
REMARK 500 ASP A 94 0.67 -65.52
REMARK 500 HIS A 199 60.36 -114.47
REMARK 500 PHE A 204 -146.19 -74.59
REMARK 500 LEU A 206 -63.73 -122.46
REMARK 500 ASP A 225 -166.54 -123.46
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 SAX B 1001
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SAX B 1002
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SAX A 2001
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3SGV RELATED DB: PDB
REMARK 900 RELATED ID: 3SGX RELATED DB: PDB
REMARK 900 RELATED ID: 3SGT RELATED DB: PDB
DBREF 3SH0 B 1 253 UNP P60472 UPPS_ECOLI 1 253
DBREF 3SH0 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
HET SAX B1001 23
HET SAX B1002 23
HET SAX A2001 23
HETNAM SAX 2-(DODECYLOXY)-6-HYDROXYBENZOIC ACID
FORMUL 3 SAX 3(C19 H30 O4)
FORMUL 6 HOH *315(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 ALA B 79 HIS B 103 1 25
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 PHE A 89 ASP A 94 1 6
HELIX 14 14 GLU A 96 HIS A 103 1 8
HELIX 15 15 ASN A 117 ALA A 132 1 16
HELIX 16 16 GLY A 146 GLN A 164 1 19
HELIX 17 17 GLN A 168 ILE A 172 5 5
HELIX 18 18 ASP A 173 GLN A 179 1 7
HELIX 19 19 LEU A 206 ALA A 210 5 5
HELIX 20 20 LEU A 220 PHE A 224 5 5
HELIX 21 21 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 LEU B 139 N ARG B 106
SHEET 3 A 6 ALA B 64 ALA B 69 1 N LEU B 67 O ASN B 140
SHEET 4 A 6 HIS B 20 MET B 25 1 N MET B 25 O TYR B 68
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 ALA A 69 1 N LEU A 67 O ALA A 142
SHEET 4 B 6 HIS A 20 MET A 25 1 N MET A 25 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
SITE 1 AC1 11 ALA B 47 LEU B 85 MET B 86 ILE B 141
SITE 2 AC1 11 ALA B 142 ALA B 143 ASN B 144 HOH B 299
SITE 3 AC1 11 HOH B 310 HOH B 357 HOH B 407
SITE 1 AC2 7 SER B 55 ALA B 58 ASN B 59 SER B 99
SITE 2 AC2 7 LEU B 100 HIS B 103 HOH B 272
SITE 1 AC3 9 VAL A 50 SER A 55 ALA A 58 ASN A 59
SITE 2 AC3 9 LEU A 93 GLU A 96 SER A 99 HIS A 103
SITE 3 AC3 9 LEU A 107
CRYST1 62.765 68.724 112.056 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 0.015932 0.000000 0.000000 0.00000
SCALE2 0.000000 0.014551 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008924 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
