HEADER LIGASE 22-DEC-16 5UCM
TITLE CRYSTAL STRUCTURE OF PROLYL-TRNA SYNTHETASE FROM PSEUDOMONAS
TITLE 2 AERUGINOSA
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PROLINE--TRNA LIGASE;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: PROLYL-TRNA SYNTHETASE,PRORS;
COMPND 5 EC: 6.1.1.15;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: PSEUDOMONAS AERUGINOSA;
SOURCE 3 ORGANISM_TAXID: 208964;
SOURCE 4 STRAIN: ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228
SOURCE 5 / 1C / PRS 101 / PAO1;
SOURCE 6 GENE: PROS, PA0956;
SOURCE 7 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 9 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 10 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 11 EXPRESSION_SYSTEM_PLASMID: PSAEA.17981.A.B1
KEYWDS SSGCID, PRORS, PROLINE-TRNA LIGASE, STRUCTURAL GENOMICS, SEATTLE
KEYWDS 2 STRUCTURAL GENOMICS CENTER FOR INFECTIOUS DISEASE, LIGASE
EXPDTA X-RAY DIFFRACTION
AUTHOR SEATTLE STRUCTURAL GENOMICS CENTER FOR INFECTIOUS DISEASE,SEATTLE
AUTHOR 2 STRUCTURAL GENOMICS CENTER FOR INFECTIOUS DISEASE (SSGCID)
REVDAT 3 04-OCT-23 5UCM 1 LINK
REVDAT 2 20-FEB-19 5UCM 1 JRNL
REVDAT 1 22-FEB-17 5UCM 0
JRNL AUTH N.PENA,D.M.DRANOW,Y.HU,Y.ESCAMILLA,J.M.BULLARD
JRNL TITL CHARACTERIZATION AND STRUCTURE DETERMINATION OF PROLYL-TRNA
JRNL TITL 2 SYNTHETASE FROM PSEUDOMONAS AERUGINOSA AND DEVELOPMENT AS A
JRNL TITL 3 SCREENING PLATFORM.
JRNL REF PROTEIN SCI. 2019
JRNL REFN ESSN 1469-896X
JRNL PMID 30666738
JRNL DOI 10.1002/PRO.3579
REMARK 2
REMARK 2 RESOLUTION. 2.60 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,
REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,
REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,
REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON,
REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,
REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT
REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.60
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 49.00
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 92.4
REMARK 3 NUMBER OF REFLECTIONS : 47231
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.171
REMARK 3 R VALUE (WORKING SET) : 0.169
REMARK 3 FREE R VALUE : 0.232
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 3.970
REMARK 3 FREE R VALUE TEST SET COUNT : 1877
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS).
REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE
REMARK 3 1 49.0093 - 6.1098 0.93 3722 157 0.1653 0.1926
REMARK 3 2 6.1098 - 4.8509 0.95 3640 146 0.1416 0.1798
REMARK 3 3 4.8509 - 4.2381 0.96 3654 153 0.1200 0.1723
REMARK 3 4 4.2381 - 3.8508 0.95 3605 148 0.1343 0.1985
REMARK 3 5 3.8508 - 3.5749 0.96 3585 148 0.1558 0.2265
REMARK 3 6 3.5749 - 3.3642 0.95 3591 152 0.1780 0.2483
REMARK 3 7 3.3642 - 3.1957 0.94 3542 147 0.1989 0.2742
REMARK 3 8 3.1957 - 3.0566 0.92 3425 143 0.1918 0.3083
REMARK 3 9 3.0566 - 2.9390 0.93 3467 145 0.2000 0.2879
REMARK 3 10 2.9390 - 2.8376 0.90 3361 142 0.2000 0.2331
REMARK 3 11 2.8376 - 2.7489 0.89 3320 129 0.2136 0.3145
REMARK 3 12 2.7489 - 2.6703 0.87 3231 134 0.2181 0.3098
REMARK 3 13 2.6703 - 2.6000 0.86 3211 133 0.2290 0.3225
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : NULL
REMARK 3 SOLVENT RADIUS : 1.11
REMARK 3 SHRINKAGE RADIUS : 0.90
REMARK 3 K_SOL : NULL
REMARK 3 B_SOL : NULL
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.320
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 22.900
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 28.32
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 35.63
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
REMARK 3
REMARK 3 TWINNING INFORMATION.
REMARK 3 FRACTION: NULL
REMARK 3 OPERATOR: NULL
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : 0.007 8814
REMARK 3 ANGLE : 0.884 11970
REMARK 3 CHIRALITY : 0.050 1352
REMARK 3 PLANARITY : 0.006 1579
REMARK 3 DIHEDRAL : 15.088 5342
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 13
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 2 THROUGH 63 )
REMARK 3 ORIGIN FOR THE GROUP (A): 42.2137 43.4999 80.7658
REMARK 3 T TENSOR
REMARK 3 T11: 0.2254 T22: 0.2773
REMARK 3 T33: 0.1966 T12: -0.0024
REMARK 3 T13: -0.0863 T23: -0.0088
REMARK 3 L TENSOR
REMARK 3 L11: 1.9840 L22: 2.2050
REMARK 3 L33: 2.0463 L12: 0.4297
REMARK 3 L13: 0.1879 L23: 0.3787
REMARK 3 S TENSOR
REMARK 3 S11: 0.1528 S12: -0.2855 S13: -0.1796
REMARK 3 S21: 0.2599 S22: -0.0179 S23: -0.1782
REMARK 3 S31: 0.2041 S32: 0.3148 S33: -0.0709
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 64 THROUGH 139 )
REMARK 3 ORIGIN FOR THE GROUP (A): 29.4693 56.5681 60.5715
REMARK 3 T TENSOR
REMARK 3 T11: 0.1941 T22: 0.1979
REMARK 3 T33: 0.1927 T12: 0.0414
REMARK 3 T13: -0.0090 T23: 0.0429
REMARK 3 L TENSOR
REMARK 3 L11: 1.2565 L22: 1.5365
REMARK 3 L33: 1.2001 L12: -0.1229
REMARK 3 L13: -0.3015 L23: 0.8345
REMARK 3 S TENSOR
REMARK 3 S11: 0.0465 S12: 0.0942 S13: 0.1794
REMARK 3 S21: -0.1426 S22: -0.0588 S23: 0.0429
REMARK 3 S31: -0.2003 S32: -0.0858 S33: 0.0234
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 140 THROUGH 166 )
REMARK 3 ORIGIN FOR THE GROUP (A): 40.4188 56.3740 69.2270
REMARK 3 T TENSOR
REMARK 3 T11: 0.2071 T22: 0.2493
REMARK 3 T33: 0.2910 T12: 0.0081
REMARK 3 T13: -0.0357 T23: 0.0130
REMARK 3 L TENSOR
REMARK 3 L11: 2.1212 L22: 0.2383
REMARK 3 L33: 0.5215 L12: -0.5777
REMARK 3 L13: -0.6762 L23: 0.3422
REMARK 3 S TENSOR
REMARK 3 S11: -0.0396 S12: 0.0577 S13: 0.1036
REMARK 3 S21: 0.0834 S22: -0.0040 S23: -0.0176
REMARK 3 S31: -0.1149 S32: 0.1537 S33: 0.0281
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 167 THROUGH 213 )
REMARK 3 ORIGIN FOR THE GROUP (A): 36.1471 68.6435 79.8415
REMARK 3 T TENSOR
REMARK 3 T11: 0.3292 T22: 0.2400
REMARK 3 T33: 0.2400 T12: -0.0158
REMARK 3 T13: -0.0015 T23: -0.1194
REMARK 3 L TENSOR
REMARK 3 L11: 2.3654 L22: 2.7683
REMARK 3 L33: 1.5428 L12: 0.5552
REMARK 3 L13: -0.4702 L23: -0.9086
REMARK 3 S TENSOR
REMARK 3 S11: 0.1851 S12: -0.3997 S13: 0.4132
REMARK 3 S21: 0.3867 S22: -0.1128 S23: 0.1411
REMARK 3 S31: -0.2291 S32: 0.0119 S33: -0.0385
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 214 THROUGH 400 )
REMARK 3 ORIGIN FOR THE GROUP (A): 61.2446 83.3232 66.8452
REMARK 3 T TENSOR
REMARK 3 T11: 0.2866 T22: 0.3223
REMARK 3 T33: 0.2717 T12: -0.0771
REMARK 3 T13: -0.0407 T23: -0.0550
REMARK 3 L TENSOR
REMARK 3 L11: 1.3103 L22: 1.2752
REMARK 3 L33: 1.6359 L12: 0.3902
REMARK 3 L13: -0.5034 L23: -0.3895
REMARK 3 S TENSOR
REMARK 3 S11: 0.2021 S12: -0.2607 S13: 0.2238
REMARK 3 S21: 0.2983 S22: -0.2016 S23: -0.0911
REMARK 3 S31: -0.3199 S32: 0.4585 S33: -0.0025
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 401 THROUGH 437 )
REMARK 3 ORIGIN FOR THE GROUP (A): 30.7079 70.5663 67.2332
REMARK 3 T TENSOR
REMARK 3 T11: 0.3477 T22: 0.1669
REMARK 3 T33: 0.3789 T12: 0.0165
REMARK 3 T13: 0.0092 T23: 0.0595
REMARK 3 L TENSOR
REMARK 3 L11: 2.9806 L22: 0.2591
REMARK 3 L33: 2.3437 L12: -0.0225
REMARK 3 L13: 2.2044 L23: 0.0961
REMARK 3 S TENSOR
REMARK 3 S11: 0.0501 S12: 0.1519 S13: 0.4507
REMARK 3 S21: -0.0540 S22: -0.1157 S23: 0.1353
REMARK 3 S31: -0.1873 S32: 0.0518 S33: 0.0976
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 438 THROUGH 483 )
REMARK 3 ORIGIN FOR THE GROUP (A): 42.0620 48.2093 87.6289
REMARK 3 T TENSOR
REMARK 3 T11: 0.3630 T22: 0.4468
REMARK 3 T33: 0.2426 T12: -0.0347
REMARK 3 T13: -0.1148 T23: -0.0033
REMARK 3 L TENSOR
REMARK 3 L11: 1.4485 L22: 2.9974
REMARK 3 L33: 1.3453 L12: -0.2580
REMARK 3 L13: -0.1607 L23: -1.0026
REMARK 3 S TENSOR
REMARK 3 S11: 0.3117 S12: -0.3955 S13: -0.0633
REMARK 3 S21: 0.2022 S22: -0.2110 S23: -0.2076
REMARK 3 S31: 0.4398 S32: 0.2422 S33: -0.0633
REMARK 3 TLS GROUP : 8
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 484 THROUGH 570 )
REMARK 3 ORIGIN FOR THE GROUP (A): 41.6970 35.8390 102.7576
REMARK 3 T TENSOR
REMARK 3 T11: 0.6260 T22: 0.5477
REMARK 3 T33: 0.3423 T12: -0.1544
REMARK 3 T13: -0.1722 T23: 0.0791
REMARK 3 L TENSOR
REMARK 3 L11: 1.4418 L22: 0.8843
REMARK 3 L33: 3.0862 L12: -0.1515
REMARK 3 L13: 0.4679 L23: -1.4724
REMARK 3 S TENSOR
REMARK 3 S11: 0.4592 S12: -0.3070 S13: -0.3187
REMARK 3 S21: 0.2702 S22: -0.0995 S23: 0.1633
REMARK 3 S31: 0.5869 S32: -0.3684 S33: -0.3140
REMARK 3 TLS GROUP : 9
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 1 THROUGH 43 )
REMARK 3 ORIGIN FOR THE GROUP (A): 14.3664 50.6110 63.0452
REMARK 3 T TENSOR
REMARK 3 T11: 0.1792 T22: 0.2787
REMARK 3 T33: 0.2096 T12: 0.0561
REMARK 3 T13: -0.0449 T23: 0.0666
REMARK 3 L TENSOR
REMARK 3 L11: 3.9189 L22: 4.2374
REMARK 3 L33: 1.3752 L12: 0.0220
REMARK 3 L13: -0.8098 L23: -0.2461
REMARK 3 S TENSOR
REMARK 3 S11: -0.1317 S12: 0.0158 S13: 0.2721
REMARK 3 S21: -0.1222 S22: 0.1000 S23: 0.2509
REMARK 3 S31: -0.1997 S32: -0.2177 S33: 0.0771
REMARK 3 TLS GROUP : 10
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 44 THROUGH 213 )
REMARK 3 ORIGIN FOR THE GROUP (A): 30.7979 31.6395 68.4218
REMARK 3 T TENSOR
REMARK 3 T11: 0.1823 T22: 0.2337
REMARK 3 T33: 0.2074 T12: 0.0506
REMARK 3 T13: -0.0241 T23: 0.0130
REMARK 3 L TENSOR
REMARK 3 L11: 0.4824 L22: 1.1560
REMARK 3 L33: 0.6646 L12: 0.6592
REMARK 3 L13: 0.0001 L23: -0.1797
REMARK 3 S TENSOR
REMARK 3 S11: 0.0095 S12: -0.0783 S13: -0.1335
REMARK 3 S21: 0.0195 S22: -0.0545 S23: -0.1695
REMARK 3 S31: 0.1479 S32: 0.0294 S33: 0.0347
REMARK 3 TLS GROUP : 11
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 214 THROUGH 400 )
REMARK 3 ORIGIN FOR THE GROUP (A): 15.5033 7.3564 44.8177
REMARK 3 T TENSOR
REMARK 3 T11: 0.1769 T22: 0.1770
REMARK 3 T33: 0.2253 T12: -0.0473
REMARK 3 T13: 0.0014 T23: 0.0310
REMARK 3 L TENSOR
REMARK 3 L11: 0.5253 L22: 0.6039
REMARK 3 L33: 2.1722 L12: -0.1275
REMARK 3 L13: 0.0037 L23: 0.3962
REMARK 3 S TENSOR
REMARK 3 S11: 0.0492 S12: 0.0075 S13: -0.1356
REMARK 3 S21: 0.1048 S22: -0.0741 S23: 0.0412
REMARK 3 S31: 0.2288 S32: -0.1672 S33: 0.0373
REMARK 3 TLS GROUP : 12
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 401 THROUGH 466 )
REMARK 3 ORIGIN FOR THE GROUP (A): 25.2363 27.2921 68.8767
REMARK 3 T TENSOR
REMARK 3 T11: 0.2375 T22: 0.1986
REMARK 3 T33: 0.1928 T12: 0.0201
REMARK 3 T13: -0.0198 T23: -0.0136
REMARK 3 L TENSOR
REMARK 3 L11: 0.5663 L22: 0.6597
REMARK 3 L33: 0.9233 L12: 0.4151
REMARK 3 L13: 0.0167 L23: -0.1193
REMARK 3 S TENSOR
REMARK 3 S11: -0.0233 S12: 0.0145 S13: -0.2324
REMARK 3 S21: 0.0971 S22: -0.0265 S23: 0.0202
REMARK 3 S31: 0.2135 S32: -0.0268 S33: 0.0258
REMARK 3 TLS GROUP : 13
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 467 THROUGH 570 )
REMARK 3 ORIGIN FOR THE GROUP (A): 0.4934 55.0403 81.3689
REMARK 3 T TENSOR
REMARK 3 T11: 0.3688 T22: 0.6143
REMARK 3 T33: 0.3748 T12: 0.1367
REMARK 3 T13: 0.0776 T23: -0.0760
REMARK 3 L TENSOR
REMARK 3 L11: 1.3255 L22: 0.7221
REMARK 3 L33: 1.4576 L12: -0.2311
REMARK 3 L13: -0.1393 L23: 0.0272
REMARK 3 S TENSOR
REMARK 3 S11: -0.3683 S12: -0.7727 S13: 0.1816
REMARK 3 S21: 0.6114 S22: 0.2333 S23: 0.4270
REMARK 3 S31: -0.1385 S32: -0.2904 S33: 0.0656
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 5UCM COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 03-JAN-17.
REMARK 100 THE DEPOSITION ID IS D_1000225656.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 12-MAR-16
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8.5
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 : DIAMOND [111]
REMARK 200 OPTICS : BERYLLIUM LENSES
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 300 MM CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 49894
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.600
REMARK 200 RESOLUTION RANGE LOW (A) : 49.001
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 97.5
REMARK 200 DATA REDUNDANCY : 4.459
REMARK 200 R MERGE (I) : 0.13000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 9.7500
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.60
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.67
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.1
REMARK 200 DATA REDUNDANCY IN SHELL : 4.45
REMARK 200 R MERGE FOR SHELL (I) : 0.58500
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.670
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MR-ROSETTA
REMARK 200 STARTING MODEL: 2J3L
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 61.28
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.18
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PSAEA.17981.A.B1.PW37621 AT 9.5 MG/ML,
REMARK 280 INCUBATED WITH 1 MM PROLINE, AMPPNP, MGCL2 AND MIXED 1:1 WITH AN
REMARK 280 EQUAL VOLUME MCSG1(B11): 20% (W/V) PEG-8000, 0.2 M MGCL2, 0.1 M
REMARK 280 TRIS:HCL, PH=8.5, CRYOPROTECTED WITH 20% ETHYLENE GLYCOL, PH 8.5,
REMARK 280 VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 290K
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 42.91500
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 93.62000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 50.77000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 93.62000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 42.91500
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 50.77000
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: 5260 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 45120 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -34.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, 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 MET A -7
REMARK 465 ALA A -6
REMARK 465 HIS A -5
REMARK 465 HIS A -4
REMARK 465 HIS A -3
REMARK 465 HIS A -2
REMARK 465 HIS A -1
REMARK 465 HIS A 0
REMARK 465 MET A 1
REMARK 465 THR A 10
REMARK 465 LEU A 11
REMARK 465 LYS A 12
REMARK 465 GLU A 13
REMARK 465 THR A 14
REMARK 465 ARG A 571
REMARK 465 MET B -7
REMARK 465 ALA B -6
REMARK 465 HIS B -5
REMARK 465 HIS B -4
REMARK 465 HIS B -3
REMARK 465 HIS B -2
REMARK 465 HIS B -1
REMARK 465 HIS B 0
REMARK 465 THR B 10
REMARK 465 LEU B 11
REMARK 465 LYS B 12
REMARK 465 GLU B 13
REMARK 465 THR B 14
REMARK 465 ARG B 571
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 ASP A 17 CG OD1 OD2
REMARK 470 GLN A 88 CG CD OE1 NE2
REMARK 470 ASP A 228 CG OD1 OD2
REMARK 470 GLN A 271 CG CD OE1 NE2
REMARK 470 GLU A 374 CG CD OE1 OE2
REMARK 470 LYS A 398 CG CD CE NZ
REMARK 470 ARG A 405 CG CD NE CZ NH1 NH2
REMARK 470 LYS A 424 CG CD CE NZ
REMARK 470 LYS A 433 CG CD CE NZ
REMARK 470 GLU A 460 CG CD OE1 OE2
REMARK 470 LEU A 479 CG CD1 CD2
REMARK 470 LYS A 480 CG CD CE NZ
REMARK 470 GLU A 482 CG CD OE1 OE2
REMARK 470 THR A 483 OG1 CG2
REMARK 470 GLU A 484 CG CD OE1 OE2
REMARK 470 VAL A 486 CG1 CG2
REMARK 470 LYS A 487 CG CD CE NZ
REMARK 470 GLN A 488 CG CD OE1 NE2
REMARK 470 LYS A 492 CG CD CE NZ
REMARK 470 LYS A 511 CG CD CE NZ
REMARK 470 LYS A 512 CG CD CE NZ
REMARK 470 ASP A 535 CG OD1 OD2
REMARK 470 LEU A 538 CG CD1 CD2
REMARK 470 LYS A 546 CG CD CE NZ
REMARK 470 GLU A 552 CG CD OE1 OE2
REMARK 470 GLU A 560 CG CD OE1 OE2
REMARK 470 LEU A 561 CG CD1 CD2
REMARK 470 SER A 570 OG
REMARK 470 MET B 1 CG SD CE
REMARK 470 LYS B 126 CG CD CE NZ
REMARK 470 LYS B 424 CG CD CE NZ
REMARK 470 LYS B 433 CG CD CE NZ
REMARK 470 LYS B 480 CG CD CE NZ
REMARK 470 GLU B 482 CG CD OE1 OE2
REMARK 470 GLU B 484 CG CD OE1 OE2
REMARK 470 LYS B 487 CG CD CE NZ
REMARK 470 LYS B 492 CG CD CE NZ
REMARK 470 LYS B 512 CG CD CE NZ
REMARK 470 ASP B 535 CG OD1 OD2
REMARK 470 ARG B 536 CG CD NE CZ NH1 NH2
REMARK 470 GLU B 540 CG CD OE1 OE2
REMARK 470 GLU B 552 CG CD OE1 OE2
REMARK 470 LEU B 556 CG CD1 CD2
REMARK 470 GLU B 560 CG CD OE1 OE2
REMARK 470 LEU B 561 CG CD1 CD2
REMARK 470 SER B 563 OG
REMARK 470 ILE B 565 CG1 CG2 CD1
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 O HOH B 719 O HOH B 924 2.17
REMARK 500 O GLN A 310 O HOH A 701 2.19
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 LEU A 8 -140.85 58.51
REMARK 500 ALA A 16 -73.76 -133.25
REMARK 500 ARG A 151 49.96 -141.35
REMARK 500 LEU A 188 1.90 -67.85
REMARK 500 SER A 205 -150.04 -110.43
REMARK 500 SER A 226 -18.76 -153.52
REMARK 500 GLU A 374 -48.40 68.13
REMARK 500 PRO A 380 -166.09 -73.56
REMARK 500 LYS A 512 -70.28 -61.65
REMARK 500 SER B 4 1.67 -63.03
REMARK 500 LEU B 8 -128.47 56.57
REMARK 500 ALA B 16 -3.24 80.46
REMARK 500 ASP B 17 -25.11 -159.06
REMARK 500 SER B 205 -153.53 -150.78
REMARK 500 SER B 226 -34.47 -146.69
REMARK 500 GLU B 374 -50.25 75.96
REMARK 500 LEU B 479 75.45 72.99
REMARK 500
REMARK 500 REMARK: NULL
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG A 600 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH A 841 O
REMARK 620 2 HOH A 843 O 71.0
REMARK 620 3 HOH A 915 O 98.2 66.2
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG B 600 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH B 830 O
REMARK 620 2 HOH B 872 O 90.3
REMARK 620 3 HOH B 922 O 147.9 71.3
REMARK 620 4 HOH B 930 O 105.5 130.8 71.3
REMARK 620 N 1 2 3
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG A 600
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG B 600
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: SSGCID-PSAEA.17981.A.B1 RELATED DB: TARGETTRACK
DBREF 5UCM A 1 571 UNP Q9I502 SYP_PSEAE 1 571
DBREF 5UCM B 1 571 UNP Q9I502 SYP_PSEAE 1 571
SEQADV 5UCM MET A -7 UNP Q9I502 INITIATING METHIONINE
SEQADV 5UCM ALA A -6 UNP Q9I502 EXPRESSION TAG
SEQADV 5UCM HIS A -5 UNP Q9I502 EXPRESSION TAG
SEQADV 5UCM HIS A -4 UNP Q9I502 EXPRESSION TAG
SEQADV 5UCM HIS A -3 UNP Q9I502 EXPRESSION TAG
SEQADV 5UCM HIS A -2 UNP Q9I502 EXPRESSION TAG
SEQADV 5UCM HIS A -1 UNP Q9I502 EXPRESSION TAG
SEQADV 5UCM HIS A 0 UNP Q9I502 EXPRESSION TAG
SEQADV 5UCM MET B -7 UNP Q9I502 INITIATING METHIONINE
SEQADV 5UCM ALA B -6 UNP Q9I502 EXPRESSION TAG
SEQADV 5UCM HIS B -5 UNP Q9I502 EXPRESSION TAG
SEQADV 5UCM HIS B -4 UNP Q9I502 EXPRESSION TAG
SEQADV 5UCM HIS B -3 UNP Q9I502 EXPRESSION TAG
SEQADV 5UCM HIS B -2 UNP Q9I502 EXPRESSION TAG
SEQADV 5UCM HIS B -1 UNP Q9I502 EXPRESSION TAG
SEQADV 5UCM HIS B 0 UNP Q9I502 EXPRESSION TAG
SEQRES 1 A 579 MET ALA HIS HIS HIS HIS HIS HIS MET ARG THR SER GLN
SEQRES 2 A 579 TYR LEU LEU SER THR LEU LYS GLU THR PRO ALA ASP ALA
SEQRES 3 A 579 VAL VAL ILE SER HIS GLN LEU LEU LEU ARG ALA GLY MET
SEQRES 4 A 579 ILE ARG ARG LEU ALA SER GLY LEU TYR THR TRP LEU PRO
SEQRES 5 A 579 MET GLY LEU ARG VAL LEU ARG LYS VAL GLU THR ILE VAL
SEQRES 6 A 579 ARG GLU GLU MET ASN ALA ALA GLY ALA LEU GLU VAL LEU
SEQRES 7 A 579 MET PRO ALA VAL GLN PRO ALA GLU LEU TRP GLN GLU SER
SEQRES 8 A 579 GLY ARG TRP GLU GLN TYR GLY PRO GLU LEU LEU ARG LEU
SEQRES 9 A 579 LYS ASP ARG HIS GLU ARG GLU PHE CYS VAL GLY PRO THR
SEQRES 10 A 579 HIS GLU GLU VAL ILE THR ASP LEU ALA ARG ASN GLU LEU
SEQRES 11 A 579 ASN SER TYR LYS GLN LEU PRO ILE ASN PHE TYR GLN ILE
SEQRES 12 A 579 GLN THR LYS PHE ARG ASP GLU ILE ARG PRO ARG PHE GLY
SEQRES 13 A 579 LEU MET ARG GLY ARG GLU PHE ILE MET LYS ASP ALA TYR
SEQRES 14 A 579 SER PHE HIS LEU SER GLN ASP SER LEU GLN GLN THR TYR
SEQRES 15 A 579 ASP GLY MET TYR GLN ALA TYR SER LYS ILE PHE SER ARG
SEQRES 16 A 579 LEU GLY LEU ASP PHE ARG PRO VAL GLN ALA ASP ASN GLY
SEQRES 17 A 579 SER ILE GLY GLY SER GLY SER HIS GLU PHE HIS VAL LEU
SEQRES 18 A 579 ALA ASN SER GLY GLU ASP ASP ILE VAL PHE SER ASP SER
SEQRES 19 A 579 SER ASP TYR ALA ALA ASN ILE GLU LYS ALA GLU ALA VAL
SEQRES 20 A 579 PRO ARG GLU SER ALA ARG GLY SER ALA THR GLU ASP MET
SEQRES 21 A 579 ARG LEU VAL ASP THR PRO ASN THR LYS THR ILE ALA ALA
SEQRES 22 A 579 LEU VAL ASP GLY PHE GLN LEU PRO ILE GLU LYS THR ILE
SEQRES 23 A 579 LYS THR LEU VAL VAL HIS GLY ALA GLU GLU GLY THR LEU
SEQRES 24 A 579 VAL ALA LEU ILE VAL ARG GLY ASP HIS GLU LEU ASN GLU
SEQRES 25 A 579 ILE LYS ALA ALA ASN GLN PRO LEU VAL ALA SER PRO LEU
SEQRES 26 A 579 VAL PHE ALA SER GLU ALA GLU ILE ARG ALA ALA ILE GLY
SEQRES 27 A 579 ALA GLY PRO GLY SER LEU GLY PRO VAL ASN LEU PRO ILE
SEQRES 28 A 579 ALA CYS ILE VAL ASP ARG SER VAL ALA LEU MET SER ASP
SEQRES 29 A 579 PHE ALA ALA GLY ALA ASN ILE GLU ASP LYS HIS TYR PHE
SEQRES 30 A 579 GLY VAL ASN TRP GLU ARG ASP LEU PRO LEU PRO GLU VAL
SEQRES 31 A 579 ALA ASP LEU ARG ASN VAL VAL GLU GLY ASP PRO SER PRO
SEQRES 32 A 579 ASP GLY LYS GLY THR LEU VAL ILE LYS ARG GLY ILE GLU
SEQRES 33 A 579 VAL GLY HIS ILE PHE GLN LEU GLY THR LYS TYR SER GLU
SEQRES 34 A 579 ALA MET LYS LEU SER VAL LEU SER GLU GLN GLY LYS PRO
SEQRES 35 A 579 VAL ASN LEU ILE MET GLY CYS TYR GLY ILE GLY VAL SER
SEQRES 36 A 579 ARG VAL VAL ALA ALA ALA ILE GLU GLN ASN HIS ASP GLU
SEQRES 37 A 579 ARG GLY ILE LEU TRP PRO SER ALA LEU ALA PRO PHE GLN
SEQRES 38 A 579 ILE ALA LEU VAL PRO LEU LYS TYR GLU THR GLU SER VAL
SEQRES 39 A 579 LYS GLN ALA THR ASP LYS LEU TYR ALA GLU LEU THR ALA
SEQRES 40 A 579 ALA GLY PHE GLU VAL LEU LEU ASP ASP ARG ASP LYS LYS
SEQRES 41 A 579 THR SER PRO GLY VAL LYS PHE ALA ASP MET GLU LEU ILE
SEQRES 42 A 579 GLY ILE PRO HIS ARG ILE VAL ILE SER ASP ARG GLY LEU
SEQRES 43 A 579 SER GLU GLY VAL LEU GLU TYR LYS GLY ARG ARG ASP SER
SEQRES 44 A 579 GLU SER GLN ASN LEU PRO ILE GLY GLU LEU MET SER PHE
SEQRES 45 A 579 ILE THR GLU LYS LEU SER ARG
SEQRES 1 B 579 MET ALA HIS HIS HIS HIS HIS HIS MET ARG THR SER GLN
SEQRES 2 B 579 TYR LEU LEU SER THR LEU LYS GLU THR PRO ALA ASP ALA
SEQRES 3 B 579 VAL VAL ILE SER HIS GLN LEU LEU LEU ARG ALA GLY MET
SEQRES 4 B 579 ILE ARG ARG LEU ALA SER GLY LEU TYR THR TRP LEU PRO
SEQRES 5 B 579 MET GLY LEU ARG VAL LEU ARG LYS VAL GLU THR ILE VAL
SEQRES 6 B 579 ARG GLU GLU MET ASN ALA ALA GLY ALA LEU GLU VAL LEU
SEQRES 7 B 579 MET PRO ALA VAL GLN PRO ALA GLU LEU TRP GLN GLU SER
SEQRES 8 B 579 GLY ARG TRP GLU GLN TYR GLY PRO GLU LEU LEU ARG LEU
SEQRES 9 B 579 LYS ASP ARG HIS GLU ARG GLU PHE CYS VAL GLY PRO THR
SEQRES 10 B 579 HIS GLU GLU VAL ILE THR ASP LEU ALA ARG ASN GLU LEU
SEQRES 11 B 579 ASN SER TYR LYS GLN LEU PRO ILE ASN PHE TYR GLN ILE
SEQRES 12 B 579 GLN THR LYS PHE ARG ASP GLU ILE ARG PRO ARG PHE GLY
SEQRES 13 B 579 LEU MET ARG GLY ARG GLU PHE ILE MET LYS ASP ALA TYR
SEQRES 14 B 579 SER PHE HIS LEU SER GLN ASP SER LEU GLN GLN THR TYR
SEQRES 15 B 579 ASP GLY MET TYR GLN ALA TYR SER LYS ILE PHE SER ARG
SEQRES 16 B 579 LEU GLY LEU ASP PHE ARG PRO VAL GLN ALA ASP ASN GLY
SEQRES 17 B 579 SER ILE GLY GLY SER GLY SER HIS GLU PHE HIS VAL LEU
SEQRES 18 B 579 ALA ASN SER GLY GLU ASP ASP ILE VAL PHE SER ASP SER
SEQRES 19 B 579 SER ASP TYR ALA ALA ASN ILE GLU LYS ALA GLU ALA VAL
SEQRES 20 B 579 PRO ARG GLU SER ALA ARG GLY SER ALA THR GLU ASP MET
SEQRES 21 B 579 ARG LEU VAL ASP THR PRO ASN THR LYS THR ILE ALA ALA
SEQRES 22 B 579 LEU VAL ASP GLY PHE GLN LEU PRO ILE GLU LYS THR ILE
SEQRES 23 B 579 LYS THR LEU VAL VAL HIS GLY ALA GLU GLU GLY THR LEU
SEQRES 24 B 579 VAL ALA LEU ILE VAL ARG GLY ASP HIS GLU LEU ASN GLU
SEQRES 25 B 579 ILE LYS ALA ALA ASN GLN PRO LEU VAL ALA SER PRO LEU
SEQRES 26 B 579 VAL PHE ALA SER GLU ALA GLU ILE ARG ALA ALA ILE GLY
SEQRES 27 B 579 ALA GLY PRO GLY SER LEU GLY PRO VAL ASN LEU PRO ILE
SEQRES 28 B 579 ALA CYS ILE VAL ASP ARG SER VAL ALA LEU MET SER ASP
SEQRES 29 B 579 PHE ALA ALA GLY ALA ASN ILE GLU ASP LYS HIS TYR PHE
SEQRES 30 B 579 GLY VAL ASN TRP GLU ARG ASP LEU PRO LEU PRO GLU VAL
SEQRES 31 B 579 ALA ASP LEU ARG ASN VAL VAL GLU GLY ASP PRO SER PRO
SEQRES 32 B 579 ASP GLY LYS GLY THR LEU VAL ILE LYS ARG GLY ILE GLU
SEQRES 33 B 579 VAL GLY HIS ILE PHE GLN LEU GLY THR LYS TYR SER GLU
SEQRES 34 B 579 ALA MET LYS LEU SER VAL LEU SER GLU GLN GLY LYS PRO
SEQRES 35 B 579 VAL ASN LEU ILE MET GLY CYS TYR GLY ILE GLY VAL SER
SEQRES 36 B 579 ARG VAL VAL ALA ALA ALA ILE GLU GLN ASN HIS ASP GLU
SEQRES 37 B 579 ARG GLY ILE LEU TRP PRO SER ALA LEU ALA PRO PHE GLN
SEQRES 38 B 579 ILE ALA LEU VAL PRO LEU LYS TYR GLU THR GLU SER VAL
SEQRES 39 B 579 LYS GLN ALA THR ASP LYS LEU TYR ALA GLU LEU THR ALA
SEQRES 40 B 579 ALA GLY PHE GLU VAL LEU LEU ASP ASP ARG ASP LYS LYS
SEQRES 41 B 579 THR SER PRO GLY VAL LYS PHE ALA ASP MET GLU LEU ILE
SEQRES 42 B 579 GLY ILE PRO HIS ARG ILE VAL ILE SER ASP ARG GLY LEU
SEQRES 43 B 579 SER GLU GLY VAL LEU GLU TYR LYS GLY ARG ARG ASP SER
SEQRES 44 B 579 GLU SER GLN ASN LEU PRO ILE GLY GLU LEU MET SER PHE
SEQRES 45 B 579 ILE THR GLU LYS LEU SER ARG
HET MG A 600 1
HET MG B 600 1
HETNAM MG MAGNESIUM ION
FORMUL 3 MG 2(MG 2+)
FORMUL 5 HOH *488(H2 O)
HELIX 1 AA1 ARG A 2 LEU A 7 1 6
HELIX 2 AA2 VAL A 20 ALA A 29 1 10
HELIX 3 AA3 LEU A 43 ALA A 64 1 22
HELIX 4 AA4 ALA A 77 SER A 83 1 7
HELIX 5 AA5 GLY A 84 TYR A 89 1 6
HELIX 6 AA6 HIS A 110 LEU A 122 1 13
HELIX 7 AA7 SER A 124 LEU A 128 5 5
HELIX 8 AA8 PHE A 147 GLY A 152 5 6
HELIX 9 AA9 SER A 166 LEU A 188 1 23
HELIX 10 AB1 THR A 262 GLN A 271 1 10
HELIX 11 AB2 PRO A 273 LYS A 276 5 4
HELIX 12 AB3 ASN A 303 GLN A 310 1 8
HELIX 13 AB4 SER A 321 GLY A 330 1 10
HELIX 14 AB5 ARG A 349 LEU A 353 1 5
HELIX 15 AB6 THR A 417 MET A 423 1 7
HELIX 16 AB7 VAL A 446 ASN A 457 1 12
HELIX 17 AB8 PRO A 466 ALA A 470 5 5
HELIX 18 AB9 SER A 485 ALA A 500 1 16
HELIX 19 AC1 SER A 514 ILE A 525 1 12
HELIX 20 AC2 SER A 534 GLU A 540 1 7
HELIX 21 AC3 ILE A 558 LEU A 569 1 12
HELIX 22 AC4 ARG B 2 LEU B 7 1 6
HELIX 23 AC5 VAL B 20 ALA B 29 1 10
HELIX 24 AC6 LEU B 43 ALA B 64 1 22
HELIX 25 AC7 ALA B 77 SER B 83 1 7
HELIX 26 AC8 GLY B 84 TYR B 89 1 6
HELIX 27 AC9 HIS B 110 LEU B 122 1 13
HELIX 28 AD1 SER B 124 LEU B 128 5 5
HELIX 29 AD2 PHE B 147 ARG B 151 5 5
HELIX 30 AD3 SER B 166 LEU B 188 1 23
HELIX 31 AD4 THR B 262 PHE B 270 1 9
HELIX 32 AD5 PRO B 273 LYS B 276 5 4
HELIX 33 AD6 ASN B 303 GLN B 310 1 8
HELIX 34 AD7 SER B 321 GLY B 330 1 10
HELIX 35 AD8 ARG B 349 LEU B 353 1 5
HELIX 36 AD9 THR B 417 MET B 423 1 7
HELIX 37 AE1 GLY B 445 ASN B 457 1 13
HELIX 38 AE2 THR B 483 ALA B 500 1 18
HELIX 39 AE3 SER B 514 ILE B 525 1 12
HELIX 40 AE4 SER B 534 GLU B 540 1 7
HELIX 41 AE5 ILE B 558 SER B 570 1 13
SHEET 1 AA1 2 ILE A 32 ALA A 36 0
SHEET 2 AA1 2 LEU A 39 TRP A 42 -1 O THR A 41 N ARG A 33
SHEET 1 AA210 LEU A 67 GLU A 68 0
SHEET 2 AA210 ILE A 130 PHE A 139 1 O ASN A 131 N LEU A 67
SHEET 3 AA210 GLU A 154 HIS A 164 -1 O PHE A 155 N LYS A 138
SHEET 4 AA210 ILE A 438 GLY A 445 -1 O TYR A 442 N ALA A 160
SHEET 5 AA210 LEU A 401 GLY A 416 -1 N PHE A 413 O CYS A 441
SHEET 6 AA210 ASP A 219 SER A 224 -1 N PHE A 223 O VAL A 402
SHEET 7 AA210 ALA A 230 ASN A 232 -1 O ALA A 231 N VAL A 222
SHEET 8 AA210 PHE A 192 GLN A 196 1 N GLN A 196 O ALA A 230
SHEET 9 AA210 SER A 207 LEU A 213 -1 O GLU A 209 N VAL A 195
SHEET 10 AA210 LEU A 401 GLY A 416 -1 O GLY A 410 N PHE A 210
SHEET 1 AA3 3 VAL A 74 PRO A 76 0
SHEET 2 AA3 3 GLU A 103 VAL A 106 -1 O CYS A 105 N GLN A 75
SHEET 3 AA3 3 LEU A 94 LYS A 97 -1 N LEU A 96 O PHE A 104
SHEET 1 AA4 3 ARG A 253 ASP A 256 0
SHEET 2 AA4 3 LYS A 366 VAL A 371 -1 O HIS A 367 N VAL A 255
SHEET 3 AA4 3 PHE A 357 GLY A 360 -1 N ALA A 359 O TYR A 368
SHEET 1 AA5 4 ILE A 278 HIS A 284 0
SHEET 2 AA5 4 LEU A 291 ARG A 297 -1 O VAL A 292 N VAL A 283
SHEET 3 AA5 4 ALA A 344 ASP A 348 1 O ALA A 344 N ALA A 293
SHEET 4 AA5 4 GLU A 381 ALA A 383 1 O GLU A 381 N VAL A 347
SHEET 1 AA6 2 SER A 426 LEU A 428 0
SHEET 2 AA6 2 PRO A 434 ASN A 436 -1 O VAL A 435 N VAL A 427
SHEET 1 AA7 2 HIS A 458 ASP A 459 0
SHEET 2 AA7 2 GLY A 462 ILE A 463 -1 O GLY A 462 N ASP A 459
SHEET 1 AA8 5 VAL A 504 LEU A 506 0
SHEET 2 AA8 5 ILE A 474 PRO A 478 1 N ILE A 474 O LEU A 505
SHEET 3 AA8 5 HIS A 529 ILE A 533 1 O ILE A 531 N VAL A 477
SHEET 4 AA8 5 VAL A 542 GLY A 547 -1 O GLU A 544 N VAL A 532
SHEET 5 AA8 5 GLN A 554 PRO A 557 -1 O GLN A 554 N TYR A 545
SHEET 1 AA9 2 ILE B 32 ALA B 36 0
SHEET 2 AA9 2 LEU B 39 TRP B 42 -1 O LEU B 39 N LEU B 35
SHEET 1 AB110 LEU B 67 GLU B 68 0
SHEET 2 AB110 ILE B 130 PHE B 139 1 O ASN B 131 N LEU B 67
SHEET 3 AB110 GLU B 154 HIS B 164 -1 O TYR B 161 N PHE B 132
SHEET 4 AB110 ILE B 438 ILE B 444 -1 O ILE B 438 N HIS B 164
SHEET 5 AB110 LEU B 401 GLY B 416 -1 N HIS B 411 O GLY B 443
SHEET 6 AB110 ASP B 219 SER B 224 -1 N PHE B 223 O VAL B 402
SHEET 7 AB110 ALA B 230 ASN B 232 -1 O ALA B 231 N VAL B 222
SHEET 8 AB110 PHE B 192 GLN B 196 1 N GLN B 196 O ASN B 232
SHEET 9 AB110 SER B 207 LEU B 213 -1 O GLU B 209 N VAL B 195
SHEET 10 AB110 LEU B 401 GLY B 416 -1 O VAL B 409 N PHE B 210
SHEET 1 AB2 3 VAL B 74 PRO B 76 0
SHEET 2 AB2 3 GLU B 103 VAL B 106 -1 O CYS B 105 N GLN B 75
SHEET 3 AB2 3 LEU B 94 LYS B 97 -1 N LEU B 96 O PHE B 104
SHEET 1 AB3 3 ARG B 253 ASP B 256 0
SHEET 2 AB3 3 LYS B 366 VAL B 371 -1 O HIS B 367 N VAL B 255
SHEET 3 AB3 3 PHE B 357 GLY B 360 -1 N PHE B 357 O VAL B 371
SHEET 1 AB4 4 ILE B 278 HIS B 284 0
SHEET 2 AB4 4 LEU B 291 ARG B 297 -1 O VAL B 296 N LYS B 279
SHEET 3 AB4 4 ALA B 344 ASP B 348 1 O ALA B 344 N ALA B 293
SHEET 4 AB4 4 GLU B 381 ALA B 383 1 O GLU B 381 N VAL B 347
SHEET 1 AB5 2 SER B 426 LEU B 428 0
SHEET 2 AB5 2 PRO B 434 ASN B 436 -1 O VAL B 435 N VAL B 427
SHEET 1 AB6 2 HIS B 458 ASP B 459 0
SHEET 2 AB6 2 GLY B 462 ILE B 463 -1 O GLY B 462 N ASP B 459
SHEET 1 AB7 5 VAL B 504 LEU B 506 0
SHEET 2 AB7 5 ILE B 474 VAL B 477 1 N ILE B 474 O LEU B 505
SHEET 3 AB7 5 HIS B 529 VAL B 532 1 O ILE B 531 N VAL B 477
SHEET 4 AB7 5 VAL B 542 GLY B 547 -1 O GLU B 544 N VAL B 532
SHEET 5 AB7 5 GLN B 554 PRO B 557 -1 O LEU B 556 N LEU B 543
LINK MG MG A 600 O HOH A 841 1555 1555 1.98
LINK MG MG A 600 O HOH A 843 1555 1555 2.32
LINK MG MG A 600 O HOH A 915 1555 1555 2.11
LINK MG MG B 600 O HOH B 830 1555 1555 2.22
LINK MG MG B 600 O HOH B 872 1555 1555 2.14
LINK MG MG B 600 O HOH B 922 1555 1555 2.21
LINK MG MG B 600 O HOH B 930 1555 1555 2.10
CISPEP 1 LEU A 128 PRO A 129 0 -0.72
CISPEP 2 SER A 315 PRO A 316 0 -1.98
CISPEP 3 LEU B 128 PRO B 129 0 -0.24
CISPEP 4 SER B 315 PRO B 316 0 4.85
CISPEP 5 PRO B 478 LEU B 479 0 19.28
SITE 1 AC1 6 GLU A 209 GLU A 234 GLU A 408 HOH A 841
SITE 2 AC1 6 HOH A 843 HOH A 915
SITE 1 AC2 6 GLU B 209 GLU B 408 HOH B 830 HOH B 872
SITE 2 AC2 6 HOH B 922 HOH B 930
CRYST1 85.830 101.540 187.240 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 0.011651 0.000000 0.000000 0.00000
SCALE2 0.000000 0.009848 0.000000 0.00000
SCALE3 0.000000 0.000000 0.005341 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
