HEADER LIGASE/LIGASE INHIBITOR 24-SEP-13 4MWB
TITLE TRYPANOSOMA BRUCEI METHIONYL-TRNA SYNTHETASE IN COMPLEX WITH INHIBITOR
TITLE 2 1-(3-{[(2,5-DICHLOROTHIOPHEN-3-YL)METHYL]AMINO}PROPYL)-3-THIOPHEN-3-
TITLE 3 YLUREA (CHEM 1509)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: METHIONYL-TRNA SYNTHETASE;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: UNP RESIDUES 237-773;
COMPND 5 EC: 6.1.1.10;
COMPND 6 ENGINEERED: YES;
COMPND 7 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: TRYPANOSOMA BRUCEI;
SOURCE 3 ORGANISM_TAXID: 5691;
SOURCE 4 GENE: TB10.70.6470;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: AVA0421
KEYWDS AMINOACYL-TRNA SYNTHETASE, AARS, METRS, PARASITE, PROTEIN-INHIBITOR
KEYWDS 2 COMPLEX, ROSSMANN FOLD, TRANSLATION, NUCLEOTIDE BINDING, LIGASE-
KEYWDS 3 LIGASE INHIBITOR COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR C.Y.KOH,J.E.KIM,A.B.WETZEL,W.J.DE VAN DER SCHUEREN,S.SHIBATA,J.LIU,
AUTHOR 2 Z.ZHANG,E.FAN,C.L.M.J.VERLINDE,W.G.J.HOL
REVDAT 2 20-SEP-23 4MWB 1 REMARK SEQADV LINK
REVDAT 1 30-APR-14 4MWB 0
JRNL AUTH C.Y.KOH,J.E.KIM,A.B.WETZEL,W.J.DE VAN DER SCHUEREN,
JRNL AUTH 2 S.SHIBATA,R.M.RANADE,J.LIU,Z.ZHANG,J.R.GILLESPIE,
JRNL AUTH 3 F.S.BUCKNER,C.L.VERLINDE,E.FAN,W.G.HOL
JRNL TITL STRUCTURES OF TRYPANOSOMA BRUCEI METHIONYL-TRNA SYNTHETASE
JRNL TITL 2 WITH UREA-BASED INHIBITORS PROVIDE GUIDANCE FOR DRUG DESIGN
JRNL TITL 3 AGAINST SLEEPING SICKNESS.
JRNL REF PLOS NEGL TROP DIS V. 8 E2775 2014
JRNL REFN ISSN 1935-2727
JRNL PMID 24743796
JRNL DOI 10.1371/JOURNAL.PNTD.0002775
REMARK 2
REMARK 2 RESOLUTION. 2.31 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC REFMAC_5.7.0032
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) : 2.31
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 30.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 3 NUMBER OF REFLECTIONS : 85417
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) : 0.181
REMARK 3 R VALUE (WORKING SET) : 0.181
REMARK 3 FREE R VALUE : 0.198
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 4273
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) : 2.31
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.37
REMARK 3 REFLECTION IN BIN (WORKING SET) : 5893
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.73
REMARK 3 BIN R VALUE (WORKING SET) : 0.2640
REMARK 3 BIN FREE R VALUE SET COUNT : 307
REMARK 3 BIN FREE R VALUE : 0.2680
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 8516
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 105
REMARK 3 SOLVENT ATOMS : 428
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 37.71
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 1.64000
REMARK 3 B22 (A**2) : -0.97000
REMARK 3 B33 (A**2) : -0.67000
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): 0.191
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.156
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.111
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 9.118
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.955
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.948
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 8845 ; 0.007 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 8437 ; 0.001 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 11999 ; 1.149 ; 1.965
REMARK 3 BOND ANGLES OTHERS (DEGREES): 19410 ; 0.732 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 1065 ; 5.398 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 401 ;36.116 ;23.441
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1460 ;13.404 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 59 ;13.961 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1326 ; 0.066 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 9877 ; 0.004 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 2028 ; 0.001 ; 0.020
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): 4260 ; 0.922 ; 2.336
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 4259 ; 0.922 ; 2.336
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 5319 ; 1.599 ; 3.499
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
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 : 10
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 238 A 380
REMARK 3 ORIGIN FOR THE GROUP (A): 6.4970 -11.7650 56.1920
REMARK 3 T TENSOR
REMARK 3 T11: 0.1403 T22: 0.0503
REMARK 3 T33: 0.0355 T12: 0.0053
REMARK 3 T13: 0.0342 T23: 0.0088
REMARK 3 L TENSOR
REMARK 3 L11: 0.8389 L22: 1.1363
REMARK 3 L33: 0.5924 L12: 0.6206
REMARK 3 L13: -0.4707 L23: -0.5030
REMARK 3 S TENSOR
REMARK 3 S11: 0.0111 S12: -0.1157 S13: -0.0490
REMARK 3 S21: 0.0708 S22: -0.0539 S23: -0.0569
REMARK 3 S31: -0.0222 S32: 0.0881 S33: 0.0428
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 381 A 546
REMARK 3 ORIGIN FOR THE GROUP (A): -1.4790 -14.6040 50.8660
REMARK 3 T TENSOR
REMARK 3 T11: 0.1444 T22: 0.0656
REMARK 3 T33: 0.0960 T12: 0.0023
REMARK 3 T13: 0.0328 T23: 0.0059
REMARK 3 L TENSOR
REMARK 3 L11: 1.2166 L22: 1.1953
REMARK 3 L33: 1.1359 L12: 0.5307
REMARK 3 L13: -0.3862 L23: -0.4500
REMARK 3 S TENSOR
REMARK 3 S11: -0.0370 S12: 0.0082 S13: -0.0075
REMARK 3 S21: -0.0106 S22: 0.0451 S23: 0.0023
REMARK 3 S31: 0.0264 S32: 0.0263 S33: -0.0080
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 547 A 617
REMARK 3 ORIGIN FOR THE GROUP (A): 28.4070 -8.6980 42.3060
REMARK 3 T TENSOR
REMARK 3 T11: 0.1805 T22: 0.0836
REMARK 3 T33: 0.1430 T12: 0.0747
REMARK 3 T13: 0.0411 T23: 0.0776
REMARK 3 L TENSOR
REMARK 3 L11: 1.9929 L22: 4.2779
REMARK 3 L33: 1.8867 L12: 0.9447
REMARK 3 L13: -0.4093 L23: 0.1975
REMARK 3 S TENSOR
REMARK 3 S11: -0.1278 S12: -0.1813 S13: -0.4840
REMARK 3 S21: 0.2720 S22: 0.0026 S23: -0.3142
REMARK 3 S31: 0.5584 S32: 0.2009 S33: 0.1252
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 618 A 755
REMARK 3 ORIGIN FOR THE GROUP (A): 26.3780 14.5600 32.0900
REMARK 3 T TENSOR
REMARK 3 T11: 0.0956 T22: 0.0721
REMARK 3 T33: 0.0515 T12: -0.0297
REMARK 3 T13: 0.0237 T23: 0.0038
REMARK 3 L TENSOR
REMARK 3 L11: 1.2426 L22: 1.2128
REMARK 3 L33: 1.4806 L12: 0.4331
REMARK 3 L13: -0.4487 L23: -0.2040
REMARK 3 S TENSOR
REMARK 3 S11: 0.0136 S12: 0.0079 S13: 0.0293
REMARK 3 S21: -0.0144 S22: 0.0131 S23: -0.0926
REMARK 3 S31: -0.2081 S32: 0.2468 S33: -0.0268
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 756 A 768
REMARK 3 ORIGIN FOR THE GROUP (A): 39.7450 1.4860 43.0150
REMARK 3 T TENSOR
REMARK 3 T11: 0.3505 T22: 0.7495
REMARK 3 T33: 0.9492 T12: -0.1650
REMARK 3 T13: 0.2186 T23: -0.0280
REMARK 3 L TENSOR
REMARK 3 L11: 3.0774 L22: 1.9977
REMARK 3 L33: 21.9180 L12: -0.0535
REMARK 3 L13: 7.6960 L23: 1.9585
REMARK 3 S TENSOR
REMARK 3 S11: -0.3791 S12: 0.1711 S13: 0.6101
REMARK 3 S21: -0.3790 S22: 0.1409 S23: -1.2855
REMARK 3 S31: -1.2508 S32: 1.1194 S33: 0.2382
REMARK 3
REMARK 3 TLS GROUP : 6
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 237 B 351
REMARK 3 ORIGIN FOR THE GROUP (A): 31.0670 12.3570 -10.8500
REMARK 3 T TENSOR
REMARK 3 T11: 0.1010 T22: 0.0776
REMARK 3 T33: 0.0401 T12: -0.0138
REMARK 3 T13: 0.0043 T23: -0.0027
REMARK 3 L TENSOR
REMARK 3 L11: 1.2003 L22: 0.3902
REMARK 3 L33: 1.0893 L12: 0.2396
REMARK 3 L13: -0.6045 L23: -0.3870
REMARK 3 S TENSOR
REMARK 3 S11: -0.0908 S12: 0.1047 S13: -0.0736
REMARK 3 S21: -0.1089 S22: 0.0360 S23: -0.0241
REMARK 3 S31: 0.1296 S32: -0.0418 S33: 0.0549
REMARK 3
REMARK 3 TLS GROUP : 7
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 352 B 406
REMARK 3 ORIGIN FOR THE GROUP (A): 60.5030 19.6710 -10.6350
REMARK 3 T TENSOR
REMARK 3 T11: 0.1568 T22: 0.2531
REMARK 3 T33: 0.3463 T12: 0.0782
REMARK 3 T13: -0.0740 T23: 0.0265
REMARK 3 L TENSOR
REMARK 3 L11: 2.4064 L22: 7.2663
REMARK 3 L33: 2.6089 L12: -1.5125
REMARK 3 L13: 1.0324 L23: -0.0651
REMARK 3 S TENSOR
REMARK 3 S11: 0.1556 S12: 0.0010 S13: -0.3495
REMARK 3 S21: 0.2765 S22: 0.1278 S23: -0.9331
REMARK 3 S31: 0.4038 S32: 0.6307 S33: -0.2834
REMARK 3
REMARK 3 TLS GROUP : 8
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 407 B 539
REMARK 3 ORIGIN FOR THE GROUP (A): 37.8090 22.8750 -4.7620
REMARK 3 T TENSOR
REMARK 3 T11: 0.0788 T22: 0.0798
REMARK 3 T33: 0.0777 T12: 0.0003
REMARK 3 T13: 0.0150 T23: 0.0012
REMARK 3 L TENSOR
REMARK 3 L11: 1.1239 L22: 0.8154
REMARK 3 L33: 1.4625 L12: 0.4115
REMARK 3 L13: -0.6157 L23: -0.1416
REMARK 3 S TENSOR
REMARK 3 S11: 0.0083 S12: -0.0385 S13: 0.0193
REMARK 3 S21: -0.0258 S22: -0.0269 S23: 0.0352
REMARK 3 S31: -0.0297 S32: 0.0433 S33: 0.0186
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 : B 540 B 731
REMARK 3 ORIGIN FOR THE GROUP (A): 17.7720 -4.0360 10.4670
REMARK 3 T TENSOR
REMARK 3 T11: 0.1282 T22: 0.0469
REMARK 3 T33: 0.0738 T12: -0.0121
REMARK 3 T13: 0.0232 T23: 0.0176
REMARK 3 L TENSOR
REMARK 3 L11: 1.5937 L22: 0.8861
REMARK 3 L33: 1.2669 L12: 0.4471
REMARK 3 L13: -0.6082 L23: -0.3695
REMARK 3 S TENSOR
REMARK 3 S11: -0.1102 S12: 0.0135 S13: -0.2090
REMARK 3 S21: -0.0753 S22: -0.0000 S23: -0.0797
REMARK 3 S31: 0.2627 S32: -0.0341 S33: 0.1102
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 : B 732 B 767
REMARK 3 ORIGIN FOR THE GROUP (A): 6.9910 -3.4700 5.6690
REMARK 3 T TENSOR
REMARK 3 T11: 0.1224 T22: 0.0970
REMARK 3 T33: 0.0920 T12: -0.0325
REMARK 3 T13: -0.0390 T23: -0.0482
REMARK 3 L TENSOR
REMARK 3 L11: 2.1292 L22: 2.0769
REMARK 3 L33: 1.5344 L12: -0.4321
REMARK 3 L13: -0.1219 L23: 0.1147
REMARK 3 S TENSOR
REMARK 3 S11: 0.1329 S12: 0.3667 S13: -0.3439
REMARK 3 S21: -0.2502 S22: 0.0030 S23: -0.0588
REMARK 3 S31: 0.3402 S32: -0.1849 S33: -0.1359
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.20
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS
REMARK 4
REMARK 4 4MWB COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 27-SEP-13.
REMARK 100 THE DEPOSITION ID IS D_1000082446.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 12-DEC-11
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.0-6.8
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SSRL
REMARK 200 BEAMLINE : BL12-2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : NULL
REMARK 200 WAVELENGTH OR RANGE (A) : 0.98
REMARK 200 MONOCHROMATOR : LIQUID NITROGEN-COOLED DOUBLE
REMARK 200 CRYSTAL SI(111)
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : SCALA 3.3.16, XDS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 85493
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.313
REMARK 200 RESOLUTION RANGE LOW (A) : 38.567
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 200 DATA REDUNDANCY : 8.200
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.16100
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 12.9000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.31
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.44
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.9
REMARK 200 DATA REDUNDANCY IN SHELL : 7.90
REMARK 200 R MERGE FOR SHELL (I) : 0.01100
REMARK 200 R SYM FOR SHELL (I) : 1.10900
REMARK 200 <I/SIGMA(I)> FOR SHELL : 0.700
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER 2.3.0
REMARK 200 STARTING MODEL: PDB ENTRY 4EG8
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 68.73
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.93
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 2.0-2.3 M AMMONIUM SULFATE, 0.2 M
REMARK 280 SODIUM CHLORIDE, 0.1 M SODIUM CACODYLATE, PH 6.0-6.8, VAPOR
REMARK 280 DIFFUSION, SITTING 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 44.06900
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 103.48750
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 53.08550
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 103.48750
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 44.06900
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 53.08550
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 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 -4
REMARK 465 PRO A -3
REMARK 465 GLY A -2
REMARK 465 SER A -1
REMARK 465 MET A 0
REMARK 465 LYS A 237
REMARK 465 ASN A 769
REMARK 465 THR A 770
REMARK 465 LYS A 771
REMARK 465 SER A 772
REMARK 465 THR A 773
REMARK 465 LYS B 382
REMARK 465 ASP B 383
REMARK 465 GLY B 384
REMARK 465 GLU B 768
REMARK 465 ASN B 769
REMARK 465 THR B 770
REMARK 465 LYS B 771
REMARK 465 SER B 772
REMARK 465 THR B 773
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 GLU A 757 CG CD OE1 OE2
REMARK 470 GLU B 491 CG CD OE1 OE2
REMARK 470 GLU B 757 CG CD OE1 OE2
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 TRP A 459 79.46 -118.95
REMARK 500 ALA A 460 176.63 179.14
REMARK 500 SER A 497 137.53 -174.23
REMARK 500 SER A 556 138.59 -172.06
REMARK 500 THR A 609 -65.61 -93.64
REMARK 500 THR A 767 82.07 -66.18
REMARK 500 SER B 497 140.26 -170.90
REMARK 500 ASP B 691 82.31 -154.89
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 GOL A 801
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 802
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 803
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 804
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 805
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 806
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DMS A 807
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DMS A 808
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MET A 809
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 801
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 802
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 803
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DMS B 804
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 806
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 2EK B 807
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4EG1 RELATED DB: PDB
REMARK 900 METHIONYL-TRNA SYNTHETASE IN COMPLEX WITH SUBSTRATE METHIONINE
REMARK 900 RELATED ID: 4EG3 RELATED DB: PDB
REMARK 900 METHIONYL-TRNA SYNTHETASE IN COMPLEX WITH INTERMEDIATE PRODUCT
REMARK 900 METHIONYL-ADENYLATE
REMARK 900 RELATED ID: 4EG5 RELATED DB: PDB
REMARK 900 METHIONYL-TRNA SYNTHETASE IN COMPLEX WITH INHIBITOR CHEM 1312
REMARK 900 RELATED ID: 4MVW RELATED DB: PDB
REMARK 900 RELATED ID: 4MVX RELATED DB: PDB
REMARK 900 RELATED ID: 4MVY RELATED DB: PDB
REMARK 900 RELATED ID: 4MW0 RELATED DB: PDB
REMARK 900 RELATED ID: 4MW1 RELATED DB: PDB
REMARK 900 RELATED ID: 4MW2 RELATED DB: PDB
REMARK 900 RELATED ID: 4MW4 RELATED DB: PDB
REMARK 900 RELATED ID: 4MW5 RELATED DB: PDB
REMARK 900 RELATED ID: 4MW6 RELATED DB: PDB
REMARK 900 RELATED ID: 4MW7 RELATED DB: PDB
REMARK 900 RELATED ID: 4MW9 RELATED DB: PDB
REMARK 900 RELATED ID: 4MWC RELATED DB: PDB
REMARK 900 RELATED ID: 4MWD RELATED DB: PDB
REMARK 900 RELATED ID: 4MWE RELATED DB: PDB
DBREF 4MWB A 237 773 UNP Q38C91 Q38C91_9TRYP 237 773
DBREF 4MWB B 237 773 UNP Q38C91 Q38C91_9TRYP 237 773
SEQADV 4MWB GLY A -4 UNP Q38C91 EXPRESSION TAG
SEQADV 4MWB PRO A -3 UNP Q38C91 EXPRESSION TAG
SEQADV 4MWB GLY A -2 UNP Q38C91 EXPRESSION TAG
SEQADV 4MWB SER A -1 UNP Q38C91 EXPRESSION TAG
SEQADV 4MWB MET A 0 UNP Q38C91 EXPRESSION TAG
SEQADV 4MWB THR A 309 UNP Q38C91 ALA 309 CONFLICT
SEQADV 4MWB ALA A 452 UNP Q38C91 LYS 452 ENGINEERED MUTATION
SEQADV 4MWB ARG A 453 UNP Q38C91 LYS 453 ENGINEERED MUTATION
SEQADV 4MWB ALA A 454 UNP Q38C91 GLU 454 ENGINEERED MUTATION
SEQADV 4MWB VAL A 499 UNP Q38C91 ALA 499 CONFLICT
SEQADV 4MWB ASN A 503 UNP Q38C91 SER 503 CONFLICT
SEQADV 4MWB GLY B -4 UNP Q38C91 EXPRESSION TAG
SEQADV 4MWB PRO B -3 UNP Q38C91 EXPRESSION TAG
SEQADV 4MWB GLY B -2 UNP Q38C91 EXPRESSION TAG
SEQADV 4MWB SER B -1 UNP Q38C91 EXPRESSION TAG
SEQADV 4MWB MET B 0 UNP Q38C91 EXPRESSION TAG
SEQADV 4MWB THR B 309 UNP Q38C91 ALA 309 CONFLICT
SEQADV 4MWB ALA B 452 UNP Q38C91 LYS 452 ENGINEERED MUTATION
SEQADV 4MWB ARG B 453 UNP Q38C91 LYS 453 ENGINEERED MUTATION
SEQADV 4MWB ALA B 454 UNP Q38C91 GLU 454 ENGINEERED MUTATION
SEQADV 4MWB VAL B 499 UNP Q38C91 ALA 499 CONFLICT
SEQADV 4MWB ASN B 503 UNP Q38C91 SER 503 CONFLICT
SEQRES 1 A 542 GLY PRO GLY SER MET LYS VAL GLU LYS VAL PHE PHE VAL
SEQRES 2 A 542 THR SER PRO ILE TYR TYR VAL ASN ALA ALA PRO HIS ILE
SEQRES 3 A 542 GLY HIS VAL TYR SER THR LEU ILE THR ASP VAL ILE GLY
SEQRES 4 A 542 ARG TYR HIS ARG VAL LYS GLY GLU ARG VAL PHE ALA LEU
SEQRES 5 A 542 THR GLY THR ASP GLU HIS GLY GLN LYS VAL ALA GLU ALA
SEQRES 6 A 542 ALA LYS GLN LYS GLN VAL SER PRO TYR ASP PHE THR THR
SEQRES 7 A 542 ALA VAL ALA GLY GLU PHE LYS LYS CAS PHE GLU GLN MET
SEQRES 8 A 542 ASP TYR SER ILE ASP TYR PHE ILE ARG THR THR ASN GLU
SEQRES 9 A 542 GLN HIS LYS ALA VAL VAL LYS GLU LEU TRP THR LYS LEU
SEQRES 10 A 542 GLU GLN LYS GLY ASP ILE TYR LEU GLY ARG TYR GLU GLY
SEQRES 11 A 542 TRP TYR SER ILE SER ASP GLU SER PHE LEU THR PRO GLN
SEQRES 12 A 542 ASN ILE THR ASP GLY VAL ASP LYS ASP GLY ASN PRO CYS
SEQRES 13 A 542 LYS VAL SER LEU GLU SER GLY HIS VAL VAL THR TRP VAL
SEQRES 14 A 542 SER GLU GLU ASN TYR MET PHE ARG LEU SER ALA PHE ARG
SEQRES 15 A 542 GLU ARG LEU LEU GLU TRP TYR HIS ALA ASN PRO GLY CYS
SEQRES 16 A 542 ILE VAL PRO GLU PHE ARG ARG ARG GLU VAL ILE ARG ALA
SEQRES 17 A 542 VAL GLU LYS GLY LEU PRO ASP LEU SER VAL SER ARG ALA
SEQRES 18 A 542 ARG ALA THR LEU HIS ASN TRP ALA ILE PRO VAL PRO GLY
SEQRES 19 A 542 ASN PRO ASP HIS CAS VAL TYR VAL TRP LEU ASP ALA LEU
SEQRES 20 A 542 THR ASN TYR LEU THR GLY SER ARG LEU ARG VAL ASP GLU
SEQRES 21 A 542 SER GLY LYS GLU VAL SER LEU VAL ASP ASP PHE ASN GLU
SEQRES 22 A 542 LEU GLU ARG PHE PRO ALA ASP VAL HIS VAL ILE GLY LYS
SEQRES 23 A 542 ASP ILE LEU LYS PHE HIS ALA ILE TYR TRP PRO ALA PHE
SEQRES 24 A 542 LEU LEU SER ALA GLY LEU PRO LEU PRO LYS LYS ILE VAL
SEQRES 25 A 542 ALA HIS GLY TRP TRP THR LYS ASP ARG LYS LYS ILE SER
SEQRES 26 A 542 LYS SER LEU GLY ASN VAL PHE ASP PRO VAL GLU LYS ALA
SEQRES 27 A 542 GLU GLU PHE GLY TYR ASP ALA LEU LYS TYR PHE LEU LEU
SEQRES 28 A 542 ARG GLU SER GLY PHE SER ASP ASP GLY ASP TYR SER ASP
SEQRES 29 A 542 LYS ASN MET ILE ALA ARG LEU ASN GLY GLU LEU ALA ASP
SEQRES 30 A 542 THR LEU GLY ASN LEU VAL MET ARG CYS THR SER ALA LYS
SEQRES 31 A 542 ILE ASN VAL ASN GLY GLU TRP PRO SER PRO ALA ALA TYR
SEQRES 32 A 542 THR GLU GLU ASP GLU SER LEU ILE GLN LEU ILE LYS ASP
SEQRES 33 A 542 LEU PRO GLY THR ALA ASP HIS TYR TYR LEU ILE PRO ASP
SEQRES 34 A 542 ILE GLN LYS ALA ILE ILE ALA VAL PHE ASP VAL LEU ARG
SEQRES 35 A 542 ALA ILE ASN ALA TYR VAL THR ASP MET ALA PRO TRP LYS
SEQRES 36 A 542 LEU VAL LYS THR ASP PRO GLU ARG LEU ARG THR VAL LEU
SEQRES 37 A 542 TYR ILE THR LEU GLU GLY VAL ARG VAL THR THR LEU LEU
SEQRES 38 A 542 LEU SER PRO ILE LEU PRO ARG LYS SER VAL VAL ILE PHE
SEQRES 39 A 542 ASP MET LEU GLY VAL PRO GLU VAL HIS ARG LYS GLY ILE
SEQRES 40 A 542 GLU ASN PHE GLU PHE GLY ALA VAL PRO PRO GLY THR ARG
SEQRES 41 A 542 LEU GLY PRO ALA VAL GLU GLY GLU VAL LEU PHE SER LYS
SEQRES 42 A 542 ARG SER THR GLU ASN THR LYS SER THR
SEQRES 1 B 542 GLY PRO GLY SER MET LYS VAL GLU LYS VAL PHE PHE VAL
SEQRES 2 B 542 THR SER PRO ILE TYR TYR VAL ASN ALA ALA PRO HIS ILE
SEQRES 3 B 542 GLY HIS VAL TYR SER THR LEU ILE THR ASP VAL ILE GLY
SEQRES 4 B 542 ARG TYR HIS ARG VAL LYS GLY GLU ARG VAL PHE ALA LEU
SEQRES 5 B 542 THR GLY THR ASP GLU HIS GLY GLN LYS VAL ALA GLU ALA
SEQRES 6 B 542 ALA LYS GLN LYS GLN VAL SER PRO TYR ASP PHE THR THR
SEQRES 7 B 542 ALA VAL ALA GLY GLU PHE LYS LYS CAS PHE GLU GLN MET
SEQRES 8 B 542 ASP TYR SER ILE ASP TYR PHE ILE ARG THR THR ASN GLU
SEQRES 9 B 542 GLN HIS LYS ALA VAL VAL LYS GLU LEU TRP THR LYS LEU
SEQRES 10 B 542 GLU GLN LYS GLY ASP ILE TYR LEU GLY ARG TYR GLU GLY
SEQRES 11 B 542 TRP TYR SER ILE SER ASP GLU SER PHE LEU THR PRO GLN
SEQRES 12 B 542 ASN ILE THR ASP GLY VAL ASP LYS ASP GLY ASN PRO CYS
SEQRES 13 B 542 LYS VAL SER LEU GLU SER GLY HIS VAL VAL THR TRP VAL
SEQRES 14 B 542 SER GLU GLU ASN TYR MET PHE ARG LEU SER ALA PHE ARG
SEQRES 15 B 542 GLU ARG LEU LEU GLU TRP TYR HIS ALA ASN PRO GLY CYS
SEQRES 16 B 542 ILE VAL PRO GLU PHE ARG ARG ARG GLU VAL ILE ARG ALA
SEQRES 17 B 542 VAL GLU LYS GLY LEU PRO ASP LEU SER VAL SER ARG ALA
SEQRES 18 B 542 ARG ALA THR LEU HIS ASN TRP ALA ILE PRO VAL PRO GLY
SEQRES 19 B 542 ASN PRO ASP HIS CAS VAL TYR VAL TRP LEU ASP ALA LEU
SEQRES 20 B 542 THR ASN TYR LEU THR GLY SER ARG LEU ARG VAL ASP GLU
SEQRES 21 B 542 SER GLY LYS GLU VAL SER LEU VAL ASP ASP PHE ASN GLU
SEQRES 22 B 542 LEU GLU ARG PHE PRO ALA ASP VAL HIS VAL ILE GLY LYS
SEQRES 23 B 542 ASP ILE LEU LYS PHE HIS ALA ILE TYR TRP PRO ALA PHE
SEQRES 24 B 542 LEU LEU SER ALA GLY LEU PRO LEU PRO LYS LYS ILE VAL
SEQRES 25 B 542 ALA HIS GLY TRP TRP THR LYS ASP ARG LYS LYS ILE SER
SEQRES 26 B 542 LYS SER LEU GLY ASN VAL PHE ASP PRO VAL GLU LYS ALA
SEQRES 27 B 542 GLU GLU PHE GLY TYR ASP ALA LEU LYS TYR PHE LEU LEU
SEQRES 28 B 542 ARG GLU SER GLY PHE SER ASP ASP GLY ASP TYR SER ASP
SEQRES 29 B 542 LYS ASN MET ILE ALA ARG LEU ASN GLY GLU LEU ALA ASP
SEQRES 30 B 542 THR LEU GLY ASN LEU VAL MET ARG CYS THR SER ALA LYS
SEQRES 31 B 542 ILE ASN VAL ASN GLY GLU TRP PRO SER PRO ALA ALA TYR
SEQRES 32 B 542 THR GLU GLU ASP GLU SER LEU ILE GLN LEU ILE LYS ASP
SEQRES 33 B 542 LEU PRO GLY THR ALA ASP HIS TYR TYR LEU ILE PRO ASP
SEQRES 34 B 542 ILE GLN LYS ALA ILE ILE ALA VAL PHE ASP VAL LEU ARG
SEQRES 35 B 542 ALA ILE ASN ALA TYR VAL THR ASP MET ALA PRO TRP LYS
SEQRES 36 B 542 LEU VAL LYS THR ASP PRO GLU ARG LEU ARG THR VAL LEU
SEQRES 37 B 542 TYR ILE THR LEU GLU GLY VAL ARG VAL THR THR LEU LEU
SEQRES 38 B 542 LEU SER PRO ILE LEU PRO ARG LYS SER VAL VAL ILE PHE
SEQRES 39 B 542 ASP MET LEU GLY VAL PRO GLU VAL HIS ARG LYS GLY ILE
SEQRES 40 B 542 GLU ASN PHE GLU PHE GLY ALA VAL PRO PRO GLY THR ARG
SEQRES 41 B 542 LEU GLY PRO ALA VAL GLU GLY GLU VAL LEU PHE SER LYS
SEQRES 42 B 542 ARG SER THR GLU ASN THR LYS SER THR
MODRES 4MWB CAS A 318 CYS S-(DIMETHYLARSENIC)CYSTEINE
MODRES 4MWB CAS A 470 CYS S-(DIMETHYLARSENIC)CYSTEINE
MODRES 4MWB CAS B 318 CYS S-(DIMETHYLARSENIC)CYSTEINE
MODRES 4MWB CAS B 470 CYS S-(DIMETHYLARSENIC)CYSTEINE
HET CAS A 318 9
HET CAS A 470 9
HET CAS B 318 9
HET CAS B 470 9
HET GOL A 801 6
HET GOL A 802 6
HET GOL A 803 6
HET GOL A 804 6
HET GOL A 805 6
HET GOL A 806 6
HET DMS A 807 4
HET DMS A 808 4
HET MET A 809 9
HET GOL B 801 6
HET GOL B 802 6
HET GOL B 803 6
HET DMS B 804 4
HET DMS B 805 4
HET SO4 B 806 5
HET 2EK B 807 21
HETNAM CAS S-(DIMETHYLARSENIC)CYSTEINE
HETNAM GOL GLYCEROL
HETNAM DMS DIMETHYL SULFOXIDE
HETNAM MET METHIONINE
HETNAM SO4 SULFATE ION
HETNAM 2EK 1-(3-{[(2,5-DICHLOROTHIOPHEN-3-YL)METHYL]AMINO}PROPYL)-
HETNAM 2 2EK 3-THIOPHEN-3-YLUREA
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 1 CAS 4(C5 H12 AS N O2 S)
FORMUL 3 GOL 9(C3 H8 O3)
FORMUL 9 DMS 4(C2 H6 O S)
FORMUL 11 MET C5 H11 N O2 S
FORMUL 17 SO4 O4 S 2-
FORMUL 18 2EK C13 H15 CL2 N3 O S2
FORMUL 19 HOH *428(H2 O)
HELIX 1 1 HIS A 256 LYS A 276 1 21
HELIX 2 2 GLY A 290 LYS A 300 1 11
HELIX 3 3 SER A 303 MET A 322 1 20
HELIX 4 4 ASN A 334 LYS A 351 1 18
HELIX 5 5 THR A 372 GLN A 374 5 3
HELIX 6 6 LEU A 409 ALA A 411 5 3
HELIX 7 7 PHE A 412 ASN A 423 1 12
HELIX 8 8 PRO A 429 LYS A 442 1 14
HELIX 9 9 TYR A 472 THR A 479 1 8
HELIX 10 10 THR A 479 ARG A 486 1 8
HELIX 11 11 ASP A 501 LEU A 505 5 5
HELIX 12 12 ILE A 519 ILE A 525 1 7
HELIX 13 13 ILE A 525 GLY A 535 1 11
HELIX 14 14 ASP A 564 GLY A 573 1 10
HELIX 15 15 GLY A 573 SER A 585 1 13
HELIX 16 16 SER A 594 GLU A 605 1 12
HELIX 17 17 THR A 609 SER A 619 1 11
HELIX 18 18 THR A 635 ILE A 658 1 24
HELIX 19 19 ASP A 660 ALA A 683 1 24
HELIX 20 20 ALA A 683 ASP A 691 1 9
HELIX 21 21 ASP A 691 SER A 714 1 24
HELIX 22 22 LEU A 717 GLY A 729 1 13
HELIX 23 23 PRO A 731 LYS A 736 5 6
HELIX 24 24 GLY A 737 GLU A 742 5 6
HELIX 25 25 HIS B 256 GLY B 277 1 22
HELIX 26 26 GLY B 290 LYS B 300 1 11
HELIX 27 27 SER B 303 MET B 322 1 20
HELIX 28 28 ASN B 334 LYS B 351 1 18
HELIX 29 29 THR B 372 GLN B 374 5 3
HELIX 30 30 LEU B 409 ALA B 411 5 3
HELIX 31 31 PHE B 412 ASN B 423 1 12
HELIX 32 32 PRO B 429 LYS B 442 1 14
HELIX 33 33 TYR B 472 LEU B 478 1 7
HELIX 34 34 THR B 479 ARG B 486 1 8
HELIX 35 35 ASP B 501 LEU B 505 5 5
HELIX 36 36 ILE B 519 ILE B 525 1 7
HELIX 37 37 ILE B 525 GLY B 535 1 11
HELIX 38 38 ASP B 564 GLY B 573 1 10
HELIX 39 39 GLY B 573 GLU B 584 1 12
HELIX 40 40 SER B 594 GLU B 605 1 12
HELIX 41 41 THR B 609 SER B 619 1 11
HELIX 42 42 THR B 635 ILE B 658 1 24
HELIX 43 43 ASP B 660 ALA B 683 1 24
HELIX 44 44 ALA B 683 ASP B 691 1 9
HELIX 45 45 ASP B 691 SER B 714 1 24
HELIX 46 46 LEU B 717 GLY B 729 1 13
HELIX 47 47 PRO B 731 ARG B 735 5 5
HELIX 48 48 GLY B 737 GLU B 742 5 6
SHEET 1 A 6 TYR A 328 ARG A 331 0
SHEET 2 A 6 VAL A 280 ASP A 287 1 N THR A 284 O ILE A 330
SHEET 3 A 6 PHE A 242 TYR A 250 1 N TYR A 249 O ASP A 287
SHEET 4 A 6 VAL A 512 GLY A 516 1 O VAL A 514 N THR A 245
SHEET 5 A 6 LYS A 541 HIS A 545 1 O VAL A 543 N HIS A 513
SHEET 6 A 6 ILE A 427 VAL A 428 1 N VAL A 428 O ALA A 544
SHEET 1 B 4 SER A 369 LEU A 371 0
SHEET 2 B 4 ILE A 354 SER A 364 -1 N SER A 364 O SER A 369
SHEET 3 B 4 VAL A 397 PHE A 407 -1 O MET A 406 N TYR A 355
SHEET 4 B 4 LEU A 447 SER A 448 -1 O LEU A 447 N PHE A 407
SHEET 1 C 2 ILE A 376 VAL A 380 0
SHEET 2 C 2 PRO A 386 SER A 390 -1 O VAL A 389 N THR A 377
SHEET 1 D 3 SER A 450 ALA A 452 0
SHEET 2 D 3 ASN A 466 VAL A 471 -1 O CAS A 470 N ARG A 451
SHEET 3 D 3 PRO A 462 VAL A 463 -1 N VAL A 463 O ASN A 466
SHEET 1 E 2 LEU A 487 VAL A 489 0
SHEET 2 E 2 GLU A 495 LEU A 498 -1 O VAL A 496 N ARG A 488
SHEET 1 F 3 LYS A 553 LYS A 554 0
SHEET 2 F 3 THR A 549 LYS A 550 -1 N LYS A 550 O LYS A 553
SHEET 3 F 3 ASP A 592 TYR A 593 1 O TYR A 593 N THR A 549
SHEET 1 G 6 TYR B 328 ARG B 331 0
SHEET 2 G 6 VAL B 280 ASP B 287 1 N THR B 284 O ILE B 330
SHEET 3 G 6 PHE B 242 TYR B 250 1 N TYR B 249 O GLY B 285
SHEET 4 G 6 VAL B 512 GLY B 516 1 O VAL B 514 N THR B 245
SHEET 5 G 6 ILE B 542 HIS B 545 1 O VAL B 543 N HIS B 513
SHEET 6 G 6 ILE B 427 VAL B 428 1 N VAL B 428 O ALA B 544
SHEET 1 H 4 SER B 369 LEU B 371 0
SHEET 2 H 4 ILE B 354 SER B 364 -1 N SER B 364 O SER B 369
SHEET 3 H 4 VAL B 397 PHE B 407 -1 O GLU B 402 N TYR B 359
SHEET 4 H 4 LEU B 447 SER B 448 -1 O LEU B 447 N PHE B 407
SHEET 1 I 2 ILE B 376 GLY B 379 0
SHEET 2 I 2 CYS B 387 SER B 390 -1 O VAL B 389 N THR B 377
SHEET 1 J 3 SER B 450 ALA B 452 0
SHEET 2 J 3 ASN B 466 VAL B 471 -1 O CAS B 470 N ARG B 451
SHEET 3 J 3 PRO B 462 VAL B 463 -1 N VAL B 463 O HIS B 469
SHEET 1 K 2 LEU B 487 VAL B 489 0
SHEET 2 K 2 GLU B 495 LEU B 498 -1 O VAL B 496 N ARG B 488
SHEET 1 L 3 LYS B 553 LYS B 554 0
SHEET 2 L 3 THR B 549 LYS B 550 -1 N LYS B 550 O LYS B 553
SHEET 3 L 3 ASP B 592 TYR B 593 1 O TYR B 593 N THR B 549
LINK C LYS A 317 N CAS A 318 1555 1555 1.33
LINK C CAS A 318 N PHE A 319 1555 1555 1.33
LINK C HIS A 469 N CAS A 470 1555 1555 1.33
LINK C CAS A 470 N VAL A 471 1555 1555 1.33
LINK C LYS B 317 N CAS B 318 1555 1555 1.33
LINK C CAS B 318 N PHE B 319 1555 1555 1.33
LINK C HIS B 469 N CAS B 470 1555 1555 1.33
LINK C CAS B 470 N VAL B 471 1555 1555 1.33
CISPEP 1 VAL A 428 PRO A 429 0 -2.83
CISPEP 2 PHE A 508 PRO A 509 0 -1.60
CISPEP 3 ILE A 658 PRO A 659 0 -6.44
CISPEP 4 VAL B 428 PRO B 429 0 -1.00
CISPEP 5 PHE B 508 PRO B 509 0 -1.36
CISPEP 6 ILE B 658 PRO B 659 0 -8.29
SITE 1 AC1 2 ARG A 583 ARG A 601
SITE 1 AC2 6 TRP A 345 GLU A 349 TYR A 405 PRO A 464
SITE 2 AC2 6 GLY A 465 ASN A 466
SITE 1 AC3 5 HIS A 289 LYS A 338 ASN A 458 TRP A 459
SITE 2 AC3 5 ALA A 460
SITE 1 AC4 1 ARG A 719
SITE 1 AC5 3 PRO A 731 GLU A 732 VAL A 733
SITE 1 AC6 7 ARG A 271 SER A 714 PRO A 718 SER A 721
SITE 2 AC6 7 VAL A 722 HOH A1051 HOH A1053
SITE 1 AC7 3 PHE A 370 LYS A 521 TYR A 526
SITE 1 AC8 1 HOH A1082
SITE 1 AC9 10 ILE A 248 TYR A 250 ASP A 287 TRP A 474
SITE 2 AC9 10 ALA A 477 TYR A 481 ILE A 519 HIS A 523
SITE 3 AC9 10 HOH A1034 HOH A1103
SITE 1 BC1 3 GLU B 343 ARG B 486 HOH B1043
SITE 1 BC2 3 ARG B 583 ARG B 601 HOH B1060
SITE 1 BC3 8 TYR A 305 HIS B 289 THR B 333 LYS B 338
SITE 2 BC3 8 ASN B 458 TRP B 459 ALA B 460 CAS B 470
SITE 1 BC4 4 GLU B 320 TYR B 324 ILE B 326 HOH B1057
SITE 1 BC5 5 ARG B 271 VAL B 275 SER B 714 PRO B 718
SITE 2 BC5 5 HOH B 939
SITE 1 BC6 14 TYR B 250 ASP B 287 HIS B 289 GLY B 290
SITE 2 BC6 14 TYR B 472 VAL B 473 TRP B 474 ASP B 476
SITE 3 BC6 14 LEU B 478 TYR B 481 ILE B 519 PHE B 522
SITE 4 BC6 14 HIS B 523 HOH B 981
CRYST1 88.138 106.171 206.975 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 0.011346 0.000000 0.000000 0.00000
SCALE2 0.000000 0.009419 0.000000 0.00000
SCALE3 0.000000 0.000000 0.004832 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
