HEADER HYDROLASE 30-NOV-09 3KVN
TITLE CRYSTAL STRUCTURE OF THE FULL-LENGTH AUTOTRANSPORTER ESTA FROM
TITLE 2 PSEUDOMONAS AERUGINOSA
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ESTERASE ESTA;
COMPND 3 CHAIN: X, A;
COMPND 4 EC: 3.1.1.1;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: PSEUDOMONAS AERUGINOSA;
SOURCE 3 ORGANISM_TAXID: 287;
SOURCE 4 GENE: ESTA, PAPA, PA5112;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS BETA BARREL, ALPHA-BETA-ALPHA MOTIF, CELL MEMBRANE, CELL OUTER
KEYWDS 2 MEMBRANE, HYDROLASE, MEMBRANE, TRANSMEMBRANE
EXPDTA X-RAY DIFFRACTION
AUTHOR B.VAN DEN BERG
REVDAT 2 11-AUG-10 3KVN 1 JRNL
REVDAT 1 26-JAN-10 3KVN 0
JRNL AUTH B.VAN DEN BERG
JRNL TITL CRYSTAL STRUCTURE OF A FULL-LENGTH AUTOTRANSPORTER.
JRNL REF J.MOL.BIOL. V. 396 627 2010
JRNL REFN ISSN 0022-2836
JRNL PMID 20060837
JRNL DOI 10.1016/J.JMB.2009.12.061
REMARK 2
REMARK 2 RESOLUTION. 2.50 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE)
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VICENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-
REMARK 3 : KUNSTLEVE,LI-WEI HUNG,ROBERT IMMORMINO,
REMARK 3 : TOM IOERGER,AIRLIE MCCOY,ERIK MCKEE,NIGEL
REMARK 3 : MORIARTY,REETAL PAI,RANDY READ,JANE
REMARK 3 : RICHARDSON,DAVID RICHARDSON,TOD ROMO,JIM
REMARK 3 : SACCHETTINI,NICHOLAS SAUTER,JACOB SMITH,
REMARK 3 : LAURENT STORONI,TOM TERWILLIGER,PETER
REMARK 3 : ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.50
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 39.18
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.330
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.5
REMARK 3 NUMBER OF REFLECTIONS : 67394
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.206
REMARK 3 R VALUE (WORKING SET) : 0.204
REMARK 3 FREE R VALUE : 0.255
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 2.930
REMARK 3 FREE R VALUE TEST SET COUNT : 1976
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 39.1832 - 6.0162 0.96 4875 150 0.1719 0.1862
REMARK 3 2 6.0162 - 4.7780 0.98 4744 143 0.1726 0.2071
REMARK 3 3 4.7780 - 4.1748 0.98 4695 140 0.1715 0.2274
REMARK 3 4 4.1748 - 3.7934 0.98 4664 139 0.1858 0.2396
REMARK 3 5 3.7934 - 3.5217 0.99 4676 142 0.1958 0.2457
REMARK 3 6 3.5217 - 3.3142 0.99 4672 141 0.2097 0.2607
REMARK 3 7 3.3142 - 3.1483 0.99 4643 140 0.2252 0.3102
REMARK 3 8 3.1483 - 3.0113 0.99 4646 141 0.2383 0.2797
REMARK 3 9 3.0113 - 2.8954 0.99 4645 139 0.2350 0.3195
REMARK 3 10 2.8954 - 2.7955 0.99 4631 141 0.2229 0.2662
REMARK 3 11 2.7955 - 2.7081 0.99 4607 139 0.2240 0.2939
REMARK 3 12 2.7081 - 2.6307 0.99 4651 140 0.2252 0.2947
REMARK 3 13 2.6307 - 2.5615 0.99 4647 140 0.2414 0.3412
REMARK 3 14 2.5615 - 2.4990 0.99 4622 141 0.2515 0.3122
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.11
REMARK 3 SHRINKAGE RADIUS : 0.90
REMARK 3 K_SOL : 0.35
REMARK 3 B_SOL : 55.35
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.690
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 26.370
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 49.62
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.00000
REMARK 3 B22 (A**2) : 0.00000
REMARK 3 B33 (A**2) : 0.00000
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 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 9874
REMARK 3 ANGLE : 1.090 13399
REMARK 3 CHIRALITY : 0.067 1389
REMARK 3 PLANARITY : 0.004 1805
REMARK 3 DIHEDRAL : 18.324 3475
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 12
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: (CHAIN A AND RESID -4:108)
REMARK 3 ORIGIN FOR THE GROUP (A): -11.1203 40.0153 78.0506
REMARK 3 T TENSOR
REMARK 3 T11: 0.3703 T22: 0.5823
REMARK 3 T33: 0.1065 T12: -0.1861
REMARK 3 T13: -0.0255 T23: -0.0049
REMARK 3 L TENSOR
REMARK 3 L11: 0.3411 L22: 0.4635
REMARK 3 L33: 0.8106 L12: -0.3247
REMARK 3 L13: -0.1809 L23: 0.1174
REMARK 3 S TENSOR
REMARK 3 S11: 0.0785 S12: -0.0461 S13: -0.0435
REMARK 3 S21: 0.0920 S22: -0.0231 S23: 0.0180
REMARK 3 S31: 0.5618 S32: -0.7510 S33: -0.0459
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: (CHAIN A AND RESID 109:141)
REMARK 3 ORIGIN FOR THE GROUP (A): -15.8320 28.2255 78.0351
REMARK 3 T TENSOR
REMARK 3 T11: 0.6873 T22: 0.8610
REMARK 3 T33: 0.1399 T12: -0.5773
REMARK 3 T13: -0.0412 T23: -0.0014
REMARK 3 L TENSOR
REMARK 3 L11: 0.4951 L22: 0.1196
REMARK 3 L33: 0.1589 L12: -0.3729
REMARK 3 L13: -0.4519 L23: -0.2677
REMARK 3 S TENSOR
REMARK 3 S11: -0.1434 S12: 0.1985 S13: -0.1866
REMARK 3 S21: 0.1053 S22: 0.0741 S23: 0.1114
REMARK 3 S31: 1.6894 S32: -1.5521 S33: 0.0086
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: (CHAIN A AND RESID 142:180)
REMARK 3 ORIGIN FOR THE GROUP (A): 1.6798 23.6689 78.5476
REMARK 3 T TENSOR
REMARK 3 T11: 0.6948 T22: 0.3799
REMARK 3 T33: 0.2083 T12: -0.1375
REMARK 3 T13: -0.0970 T23: -0.0164
REMARK 3 L TENSOR
REMARK 3 L11: 1.5214 L22: 0.1850
REMARK 3 L33: 0.6714 L12: -0.2000
REMARK 3 L13: 0.3013 L23: 0.3642
REMARK 3 S TENSOR
REMARK 3 S11: 0.1384 S12: -0.2638 S13: -0.4459
REMARK 3 S21: -0.0272 S22: 0.0683 S23: -0.0504
REMARK 3 S31: 0.9541 S32: -0.4238 S33: -0.1329
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: (CHAIN A AND RESID 181:375)
REMARK 3 ORIGIN FOR THE GROUP (A): 3.8020 42.4223 59.9413
REMARK 3 T TENSOR
REMARK 3 T11: 0.3368 T22: 0.4743
REMARK 3 T33: 0.1316 T12: -0.0608
REMARK 3 T13: 0.0201 T23: -0.0054
REMARK 3 L TENSOR
REMARK 3 L11: 0.1614 L22: 0.5671
REMARK 3 L33: 2.2519 L12: -0.1065
REMARK 3 L13: 0.0490 L23: 0.0029
REMARK 3 S TENSOR
REMARK 3 S11: 0.0365 S12: 0.2358 S13: 0.0049
REMARK 3 S21: -0.1900 S22: 0.0344 S23: -0.1291
REMARK 3 S31: 0.2836 S32: -0.0182 S33: -0.0655
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: (CHAIN A AND RESID 376:537)
REMARK 3 ORIGIN FOR THE GROUP (A): -1.5412 40.0415 30.4733
REMARK 3 T TENSOR
REMARK 3 T11: 0.5731 T22: 0.6210
REMARK 3 T33: 0.1241 T12: -0.0692
REMARK 3 T13: 0.0687 T23: -0.0204
REMARK 3 L TENSOR
REMARK 3 L11: 0.3023 L22: 0.7119
REMARK 3 L33: 2.0303 L12: -0.1203
REMARK 3 L13: -0.4554 L23: -0.3357
REMARK 3 S TENSOR
REMARK 3 S11: 0.0231 S12: 0.2716 S13: 0.0323
REMARK 3 S21: -0.3205 S22: 0.0083 S23: -0.0984
REMARK 3 S31: 0.3614 S32: 0.1680 S33: -0.0438
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: (CHAIN A AND RESID 538:622)
REMARK 3 ORIGIN FOR THE GROUP (A): -6.1909 43.1373 33.1396
REMARK 3 T TENSOR
REMARK 3 T11: 0.5837 T22: 0.7448
REMARK 3 T33: 0.1464 T12: -0.0950
REMARK 3 T13: -0.0016 T23: 0.0083
REMARK 3 L TENSOR
REMARK 3 L11: -0.2120 L22: -0.1876
REMARK 3 L33: 1.3625 L12: -0.1195
REMARK 3 L13: 0.2876 L23: 0.3987
REMARK 3 S TENSOR
REMARK 3 S11: 0.0148 S12: 0.0074 S13: -0.0117
REMARK 3 S21: -0.2928 S22: 0.0292 S23: 0.0276
REMARK 3 S31: 0.2823 S32: -0.4768 S33: -0.0150
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: (CHAIN X AND RESID -5:108)
REMARK 3 ORIGIN FOR THE GROUP (A): 49.9465 30.7480 74.1474
REMARK 3 T TENSOR
REMARK 3 T11: 0.5143 T22: 0.3588
REMARK 3 T33: 0.1275 T12: 0.0154
REMARK 3 T13: 0.0446 T23: 0.0318
REMARK 3 L TENSOR
REMARK 3 L11: 0.4936 L22: 0.9212
REMARK 3 L33: 0.5589 L12: -0.2771
REMARK 3 L13: 0.4408 L23: -0.3770
REMARK 3 S TENSOR
REMARK 3 S11: -0.0365 S12: 0.0196 S13: 0.0246
REMARK 3 S21: -0.0141 S22: -0.0227 S23: -0.1061
REMARK 3 S31: -0.4337 S32: 0.2141 S33: 0.0448
REMARK 3 TLS GROUP : 8
REMARK 3 SELECTION: (CHAIN X AND RESID 109:141)
REMARK 3 ORIGIN FOR THE GROUP (A): 40.4710 39.1397 74.1839
REMARK 3 T TENSOR
REMARK 3 T11: 0.7535 T22: 0.2424
REMARK 3 T33: 0.1603 T12: 0.1564
REMARK 3 T13: 0.0011 T23: 0.0500
REMARK 3 L TENSOR
REMARK 3 L11: 1.0153 L22: 0.3348
REMARK 3 L33: -1.4900 L12: -0.4183
REMARK 3 L13: -0.2244 L23: 0.3784
REMARK 3 S TENSOR
REMARK 3 S11: -0.1860 S12: 0.0339 S13: 0.1103
REMARK 3 S21: 0.1041 S22: 0.0548 S23: -0.0876
REMARK 3 S31: -0.5540 S32: 0.0405 S33: 0.1087
REMARK 3 TLS GROUP : 9
REMARK 3 SELECTION: (CHAIN X AND RESID 142:180)
REMARK 3 ORIGIN FOR THE GROUP (A): 30.3379 24.8578 77.9295
REMARK 3 T TENSOR
REMARK 3 T11: 0.3619 T22: 0.4798
REMARK 3 T33: 0.1467 T12: 0.1359
REMARK 3 T13: 0.0411 T23: 0.0539
REMARK 3 L TENSOR
REMARK 3 L11: 0.2237 L22: 1.0317
REMARK 3 L33: -0.2235 L12: 0.8371
REMARK 3 L13: 0.5031 L23: -0.1842
REMARK 3 S TENSOR
REMARK 3 S11: 0.1578 S12: 0.0249 S13: 0.0416
REMARK 3 S21: 0.1363 S22: -0.0173 S23: 0.3406
REMARK 3 S31: -0.5582 S32: -0.8329 S33: -0.0931
REMARK 3 TLS GROUP : 10
REMARK 3 SELECTION: (CHAIN X AND RESID 181:375)
REMARK 3 ORIGIN FOR THE GROUP (A): 45.0590 13.3422 59.3264
REMARK 3 T TENSOR
REMARK 3 T11: 0.4918 T22: 0.2951
REMARK 3 T33: 0.1090 T12: 0.0301
REMARK 3 T13: 0.0089 T23: -0.0064
REMARK 3 L TENSOR
REMARK 3 L11: 0.5540 L22: 0.2941
REMARK 3 L33: 1.9755 L12: -0.0748
REMARK 3 L13: -0.4165 L23: -0.0454
REMARK 3 S TENSOR
REMARK 3 S11: 0.0295 S12: 0.2335 S13: -0.0487
REMARK 3 S21: -0.2999 S22: -0.0770 S23: 0.0082
REMARK 3 S31: 0.2182 S32: -0.1112 S33: 0.0572
REMARK 3 TLS GROUP : 11
REMARK 3 SELECTION: (CHAIN X AND RESID 376:536)
REMARK 3 ORIGIN FOR THE GROUP (A): 41.3545 14.5750 29.5756
REMARK 3 T TENSOR
REMARK 3 T11: 0.7148 T22: 0.6233
REMARK 3 T33: 0.1067 T12: 0.0689
REMARK 3 T13: -0.0335 T23: -0.0661
REMARK 3 L TENSOR
REMARK 3 L11: 0.8799 L22: 0.4283
REMARK 3 L33: 1.6621 L12: 0.1004
REMARK 3 L13: -0.6922 L23: 0.6985
REMARK 3 S TENSOR
REMARK 3 S11: 0.0336 S12: 0.4220 S13: -0.0887
REMARK 3 S21: -0.3148 S22: -0.0691 S23: 0.0326
REMARK 3 S31: 0.3067 S32: -0.4461 S33: 0.0392
REMARK 3 TLS GROUP : 12
REMARK 3 SELECTION: (CHAIN X AND RESID 537:622)
REMARK 3 ORIGIN FOR THE GROUP (A): 46.3405 17.9911 30.6748
REMARK 3 T TENSOR
REMARK 3 T11: 0.8425 T22: 0.6756
REMARK 3 T33: 0.1660 T12: 0.1464
REMARK 3 T13: 0.0273 T23: 0.0008
REMARK 3 L TENSOR
REMARK 3 L11: 0.4886 L22: -0.2806
REMARK 3 L33: -0.1136 L12: 0.2383
REMARK 3 L13: 0.4681 L23: -0.2449
REMARK 3 S TENSOR
REMARK 3 S11: 0.1536 S12: 0.4169 S13: -0.0920
REMARK 3 S21: -0.2333 S22: -0.1832 S23: 0.0527
REMARK 3 S31: -0.0234 S32: -0.1044 S33: -0.0294
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : 1
REMARK 3 NCS GROUP : 1
REMARK 3 NCS OPERATOR : 1
REMARK 3 REFERENCE SELECTION: chain X and (resseq 1:77 or resseq 82:111
REMARK 3 or resseq 132:203 or resseq 208:395 or
REMARK 3 resseq 397:475 or resseq 485:622 )
REMARK 3 SELECTION : chain A and (resseq 1:77 or resseq 82:111
REMARK 3 or resseq 132:203 or resseq 208:395 or
REMARK 3 resseq 397:475 or resseq 485:622 )
REMARK 3 ATOM PAIRS NUMBER : 4437
REMARK 3 RMSD : 0.045
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 3KVN COMPLIES WITH FORMAT V. 3.20, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 02-DEC-09.
REMARK 100 THE RCSB ID CODE IS RCSB056504.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 26-JUN-09
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : NSLS
REMARK 200 BEAMLINE : X25
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97
REMARK 200 MONOCHROMATOR : SI-111 DOUBLE CRYSTAL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 210
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 67607
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.500
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.8
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.50
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.54
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.6
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
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: SAD
REMARK 200 SOFTWARE USED: SOLVE
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 65.10
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.52
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 45% PEG400, 0.8 M AMMONIUM FORMATE,
REMARK 280 0.1 M MES PH 6.5, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 295K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 4 21 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z
REMARK 290 3555 -Y+1/2,X+1/2,Z
REMARK 290 4555 Y+1/2,-X+1/2,Z
REMARK 290 5555 -X+1/2,Y+1/2,-Z
REMARK 290 6555 X+1/2,-Y+1/2,-Z
REMARK 290 7555 Y,X,-Z
REMARK 290 8555 -Y,-X,-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 0.00000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 71.91300
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 71.91300
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 71.91300
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 71.91300
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 71.91300
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 71.91300
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 71.91300
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 71.91300
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 7 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 7 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 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: X
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: 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 X -9
REMARK 465 HIS X -8
REMARK 465 HIS X -7
REMARK 465 HIS X -6
REMARK 465 MET A -9
REMARK 465 HIS A -8
REMARK 465 HIS A -7
REMARK 465 HIS A -6
REMARK 465 HIS A -5
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 HIS X -5 CG ND1 CD2 CE1 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 GLY X 345 C GLY X 345 O -0.104
REMARK 500 TRP X 347 CG TRP X 347 CD1 -0.087
REMARK 500 TRP X 347 C TRP X 347 O -0.131
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 X 3 77.96 -160.23
REMARK 500 ASP X 13 -156.83 -123.60
REMARK 500 TYR X 42 -2.27 67.29
REMARK 500 THR X 73 27.60 -142.66
REMARK 500 ARG X 129 23.36 -77.50
REMARK 500 GLN X 130 15.46 -143.34
REMARK 500 ASP X 278 101.76 -161.35
REMARK 500 ASP X 286 -146.54 -131.83
REMARK 500 ASN X 340 41.56 -176.65
REMARK 500 TRP X 347 128.02 -39.73
REMARK 500 ARG X 427 -8.20 80.38
REMARK 500 ALA X 507 42.14 -148.92
REMARK 500 SER X 508 170.45 -58.52
REMARK 500 PHE X 534 61.17 -104.54
REMARK 500 SER X 536 -6.68 53.99
REMARK 500 GLU X 594 -11.85 85.10
REMARK 500 SER A 3 77.81 -158.93
REMARK 500 ASP A 13 -157.16 -124.32
REMARK 500 THR A 73 27.90 -141.24
REMARK 500 ALA A 128 -5.80 -59.75
REMARK 500 GLN A 130 7.91 93.00
REMARK 500 ASP A 278 103.66 -161.88
REMARK 500 ASP A 286 -148.71 -134.27
REMARK 500 ASN A 340 42.62 -175.31
REMARK 500 ARG A 427 -8.41 81.36
REMARK 500 ALA A 507 39.41 -147.69
REMARK 500 SER A 508 170.04 -58.20
REMARK 500 PHE A 534 59.83 -104.28
REMARK 500 SER A 536 -6.77 53.25
REMARK 500 GLU A 594 -10.99 86.20
REMARK 500
REMARK 500 REMARK: NULL
REMARK 610
REMARK 610 MISSING HETEROATOM
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 610 I=INSERTION CODE):
REMARK 610 M RES C SSEQI
REMARK 610 C8E X 623
REMARK 610 C8E X 624
REMARK 610 C8E A 623
REMARK 610 C8E A 624
REMARK 610 C8E A 625
REMARK 610 C8E A 626
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE C8E X 623
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE C8E X 624
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE C8E A 623
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE C8E A 624
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE C8E A 625
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE C8E A 626
DBREF 3KVN X 1 622 UNP O33407 ESTA_PSEAE 25 646
DBREF 3KVN A 1 622 UNP O33407 ESTA_PSEAE 25 646
SEQADV 3KVN MET X -9 UNP O33407 EXPRESSION TAG
SEQADV 3KVN HIS X -8 UNP O33407 EXPRESSION TAG
SEQADV 3KVN HIS X -7 UNP O33407 EXPRESSION TAG
SEQADV 3KVN HIS X -6 UNP O33407 EXPRESSION TAG
SEQADV 3KVN HIS X -5 UNP O33407 EXPRESSION TAG
SEQADV 3KVN HIS X -4 UNP O33407 EXPRESSION TAG
SEQADV 3KVN HIS X -3 UNP O33407 EXPRESSION TAG
SEQADV 3KVN HIS X -2 UNP O33407 EXPRESSION TAG
SEQADV 3KVN LEU X -1 UNP O33407 EXPRESSION TAG
SEQADV 3KVN GLU X 0 UNP O33407 EXPRESSION TAG
SEQADV 3KVN MET A -9 UNP O33407 EXPRESSION TAG
SEQADV 3KVN HIS A -8 UNP O33407 EXPRESSION TAG
SEQADV 3KVN HIS A -7 UNP O33407 EXPRESSION TAG
SEQADV 3KVN HIS A -6 UNP O33407 EXPRESSION TAG
SEQADV 3KVN HIS A -5 UNP O33407 EXPRESSION TAG
SEQADV 3KVN HIS A -4 UNP O33407 EXPRESSION TAG
SEQADV 3KVN HIS A -3 UNP O33407 EXPRESSION TAG
SEQADV 3KVN HIS A -2 UNP O33407 EXPRESSION TAG
SEQADV 3KVN LEU A -1 UNP O33407 EXPRESSION TAG
SEQADV 3KVN GLU A 0 UNP O33407 EXPRESSION TAG
SEQRES 1 X 632 MET HIS HIS HIS HIS HIS HIS HIS LEU GLU ALA PRO SER
SEQRES 2 X 632 PRO TYR SER THR LEU VAL VAL PHE GLY ASP SER LEU SER
SEQRES 3 X 632 ASP ALA GLY GLN PHE PRO ASP PRO ALA GLY PRO ALA GLY
SEQRES 4 X 632 SER THR SER ARG PHE THR ASN ARG VAL GLY PRO THR TYR
SEQRES 5 X 632 GLN ASN GLY SER GLY GLU ILE PHE GLY PRO THR ALA PRO
SEQRES 6 X 632 MET LEU LEU GLY ASN GLN LEU GLY ILE ALA PRO GLY ASP
SEQRES 7 X 632 LEU ALA ALA SER THR SER PRO VAL ASN ALA GLN GLN GLY
SEQRES 8 X 632 ILE ALA ASP GLY ASN ASN TRP ALA VAL GLY GLY TYR ARG
SEQRES 9 X 632 THR ASP GLN ILE TYR ASP SER ILE THR ALA ALA ASN GLY
SEQRES 10 X 632 SER LEU ILE GLU ARG ASP ASN THR LEU LEU ARG SER ARG
SEQRES 11 X 632 ASP GLY TYR LEU VAL ASP ARG ALA ARG GLN GLY LEU GLY
SEQRES 12 X 632 ALA ASP PRO ASN ALA LEU TYR TYR ILE THR GLY GLY GLY
SEQRES 13 X 632 ASN ASP PHE LEU GLN GLY ARG ILE LEU ASN ASP VAL GLN
SEQRES 14 X 632 ALA GLN GLN ALA ALA GLY ARG LEU VAL ASP SER VAL GLN
SEQRES 15 X 632 ALA LEU GLN GLN ALA GLY ALA ARG TYR ILE VAL VAL TRP
SEQRES 16 X 632 LEU LEU PRO ASP LEU GLY LEU THR PRO ALA THR PHE GLY
SEQRES 17 X 632 GLY PRO LEU GLN PRO PHE ALA SER GLN LEU SER GLY THR
SEQRES 18 X 632 PHE ASN ALA GLU LEU THR ALA GLN LEU SER GLN ALA GLY
SEQRES 19 X 632 ALA ASN VAL ILE PRO LEU ASN ILE PRO LEU LEU LEU LYS
SEQRES 20 X 632 GLU GLY MET ALA ASN PRO ALA SER PHE GLY LEU ALA ALA
SEQRES 21 X 632 ASP GLN ASN LEU ILE GLY THR CYS PHE SER GLY ASN GLY
SEQRES 22 X 632 CYS THR MET ASN PRO THR TYR GLY ILE ASN GLY SER THR
SEQRES 23 X 632 PRO ASP PRO SER LYS LEU LEU PHE ASN ASP SER VAL HIS
SEQRES 24 X 632 PRO THR ILE THR GLY GLN ARG LEU ILE ALA ASP TYR THR
SEQRES 25 X 632 TYR SER LEU LEU SER ALA PRO TRP GLU LEU THR LEU LEU
SEQRES 26 X 632 PRO GLU MET ALA HIS GLY THR LEU ARG ALA TYR GLN ASP
SEQRES 27 X 632 GLU LEU ARG SER GLN TRP GLN ALA ASP TRP GLU ASN TRP
SEQRES 28 X 632 GLN ASN VAL GLY GLN TRP ARG GLY PHE VAL GLY GLY GLY
SEQRES 29 X 632 GLY GLN ARG LEU ASP PHE ASP SER GLN ASP SER ALA ALA
SEQRES 30 X 632 SER GLY ASP GLY ASN GLY TYR ASN LEU THR LEU GLY GLY
SEQRES 31 X 632 SER TYR ARG ILE ASP GLU ALA TRP ARG ALA GLY VAL ALA
SEQRES 32 X 632 ALA GLY PHE TYR ARG GLN LYS LEU GLU ALA GLY ALA LYS
SEQRES 33 X 632 ASP SER ASP TYR ARG MET ASN SER TYR MET ALA SER ALA
SEQRES 34 X 632 PHE VAL GLN TYR GLN GLU ASN ARG TRP TRP ALA ASP ALA
SEQRES 35 X 632 ALA LEU THR GLY GLY TYR LEU ASP TYR ASP ASP LEU LYS
SEQRES 36 X 632 ARG LYS PHE ALA LEU GLY GLY GLY GLU ARG SER GLU LYS
SEQRES 37 X 632 GLY ASP THR ASN GLY HIS LEU TRP ALA PHE SER ALA ARG
SEQRES 38 X 632 LEU GLY TYR ASP ILE ALA GLN GLN ALA ASP SER PRO TRP
SEQRES 39 X 632 HIS LEU SER PRO PHE VAL SER ALA ASP TYR ALA ARG VAL
SEQRES 40 X 632 GLU VAL ASP GLY TYR SER GLU LYS GLY ALA SER ALA THR
SEQRES 41 X 632 ALA LEU ASP TYR ASP ASP GLN LYS ARG SER SER LYS ARG
SEQRES 42 X 632 LEU GLY ALA GLY LEU GLN GLY LYS TYR ALA PHE GLY SER
SEQRES 43 X 632 ASP THR GLN LEU PHE ALA GLU TYR ALA HIS GLU ARG GLU
SEQRES 44 X 632 TYR GLU ASP ASP THR GLN ASP LEU THR MET SER LEU ASN
SEQRES 45 X 632 SER LEU PRO GLY ASN ARG PHE THR LEU GLU GLY TYR THR
SEQRES 46 X 632 PRO GLN ASP HIS LEU ASN ARG VAL SER LEU GLY PHE SER
SEQRES 47 X 632 GLN LYS LEU ALA PRO GLU LEU SER LEU ARG GLY GLY TYR
SEQRES 48 X 632 ASN TRP ARG LYS GLY GLU ASP ASP THR GLN GLN SER VAL
SEQRES 49 X 632 SER LEU ALA LEU SER LEU ASP PHE
SEQRES 1 A 632 MET HIS HIS HIS HIS HIS HIS HIS LEU GLU ALA PRO SER
SEQRES 2 A 632 PRO TYR SER THR LEU VAL VAL PHE GLY ASP SER LEU SER
SEQRES 3 A 632 ASP ALA GLY GLN PHE PRO ASP PRO ALA GLY PRO ALA GLY
SEQRES 4 A 632 SER THR SER ARG PHE THR ASN ARG VAL GLY PRO THR TYR
SEQRES 5 A 632 GLN ASN GLY SER GLY GLU ILE PHE GLY PRO THR ALA PRO
SEQRES 6 A 632 MET LEU LEU GLY ASN GLN LEU GLY ILE ALA PRO GLY ASP
SEQRES 7 A 632 LEU ALA ALA SER THR SER PRO VAL ASN ALA GLN GLN GLY
SEQRES 8 A 632 ILE ALA ASP GLY ASN ASN TRP ALA VAL GLY GLY TYR ARG
SEQRES 9 A 632 THR ASP GLN ILE TYR ASP SER ILE THR ALA ALA ASN GLY
SEQRES 10 A 632 SER LEU ILE GLU ARG ASP ASN THR LEU LEU ARG SER ARG
SEQRES 11 A 632 ASP GLY TYR LEU VAL ASP ARG ALA ARG GLN GLY LEU GLY
SEQRES 12 A 632 ALA ASP PRO ASN ALA LEU TYR TYR ILE THR GLY GLY GLY
SEQRES 13 A 632 ASN ASP PHE LEU GLN GLY ARG ILE LEU ASN ASP VAL GLN
SEQRES 14 A 632 ALA GLN GLN ALA ALA GLY ARG LEU VAL ASP SER VAL GLN
SEQRES 15 A 632 ALA LEU GLN GLN ALA GLY ALA ARG TYR ILE VAL VAL TRP
SEQRES 16 A 632 LEU LEU PRO ASP LEU GLY LEU THR PRO ALA THR PHE GLY
SEQRES 17 A 632 GLY PRO LEU GLN PRO PHE ALA SER GLN LEU SER GLY THR
SEQRES 18 A 632 PHE ASN ALA GLU LEU THR ALA GLN LEU SER GLN ALA GLY
SEQRES 19 A 632 ALA ASN VAL ILE PRO LEU ASN ILE PRO LEU LEU LEU LYS
SEQRES 20 A 632 GLU GLY MET ALA ASN PRO ALA SER PHE GLY LEU ALA ALA
SEQRES 21 A 632 ASP GLN ASN LEU ILE GLY THR CYS PHE SER GLY ASN GLY
SEQRES 22 A 632 CYS THR MET ASN PRO THR TYR GLY ILE ASN GLY SER THR
SEQRES 23 A 632 PRO ASP PRO SER LYS LEU LEU PHE ASN ASP SER VAL HIS
SEQRES 24 A 632 PRO THR ILE THR GLY GLN ARG LEU ILE ALA ASP TYR THR
SEQRES 25 A 632 TYR SER LEU LEU SER ALA PRO TRP GLU LEU THR LEU LEU
SEQRES 26 A 632 PRO GLU MET ALA HIS GLY THR LEU ARG ALA TYR GLN ASP
SEQRES 27 A 632 GLU LEU ARG SER GLN TRP GLN ALA ASP TRP GLU ASN TRP
SEQRES 28 A 632 GLN ASN VAL GLY GLN TRP ARG GLY PHE VAL GLY GLY GLY
SEQRES 29 A 632 GLY GLN ARG LEU ASP PHE ASP SER GLN ASP SER ALA ALA
SEQRES 30 A 632 SER GLY ASP GLY ASN GLY TYR ASN LEU THR LEU GLY GLY
SEQRES 31 A 632 SER TYR ARG ILE ASP GLU ALA TRP ARG ALA GLY VAL ALA
SEQRES 32 A 632 ALA GLY PHE TYR ARG GLN LYS LEU GLU ALA GLY ALA LYS
SEQRES 33 A 632 ASP SER ASP TYR ARG MET ASN SER TYR MET ALA SER ALA
SEQRES 34 A 632 PHE VAL GLN TYR GLN GLU ASN ARG TRP TRP ALA ASP ALA
SEQRES 35 A 632 ALA LEU THR GLY GLY TYR LEU ASP TYR ASP ASP LEU LYS
SEQRES 36 A 632 ARG LYS PHE ALA LEU GLY GLY GLY GLU ARG SER GLU LYS
SEQRES 37 A 632 GLY ASP THR ASN GLY HIS LEU TRP ALA PHE SER ALA ARG
SEQRES 38 A 632 LEU GLY TYR ASP ILE ALA GLN GLN ALA ASP SER PRO TRP
SEQRES 39 A 632 HIS LEU SER PRO PHE VAL SER ALA ASP TYR ALA ARG VAL
SEQRES 40 A 632 GLU VAL ASP GLY TYR SER GLU LYS GLY ALA SER ALA THR
SEQRES 41 A 632 ALA LEU ASP TYR ASP ASP GLN LYS ARG SER SER LYS ARG
SEQRES 42 A 632 LEU GLY ALA GLY LEU GLN GLY LYS TYR ALA PHE GLY SER
SEQRES 43 A 632 ASP THR GLN LEU PHE ALA GLU TYR ALA HIS GLU ARG GLU
SEQRES 44 A 632 TYR GLU ASP ASP THR GLN ASP LEU THR MET SER LEU ASN
SEQRES 45 A 632 SER LEU PRO GLY ASN ARG PHE THR LEU GLU GLY TYR THR
SEQRES 46 A 632 PRO GLN ASP HIS LEU ASN ARG VAL SER LEU GLY PHE SER
SEQRES 47 A 632 GLN LYS LEU ALA PRO GLU LEU SER LEU ARG GLY GLY TYR
SEQRES 48 A 632 ASN TRP ARG LYS GLY GLU ASP ASP THR GLN GLN SER VAL
SEQRES 49 A 632 SER LEU ALA LEU SER LEU ASP PHE
HET C8E X 623 18
HET C8E X 624 6
HET C8E A 623 20
HET C8E A 624 6
HET C8E A 625 6
HET C8E A 626 6
HETNAM C8E (HYDROXYETHYLOXY)TRI(ETHYLOXY)OCTANE
FORMUL 3 C8E 6(C16 H34 O5)
FORMUL 9 HOH *449(H2 O)
HELIX 1 1 THR X 53 LEU X 62 1 10
HELIX 2 2 ALA X 65 ALA X 70 5 6
HELIX 3 3 SER X 74 GLY X 81 1 8
HELIX 4 4 ARG X 94 ALA X 104 1 11
HELIX 5 5 GLY X 122 ARG X 129 1 8
HELIX 6 6 GLY X 145 GLN X 151 1 7
HELIX 7 7 ASN X 156 ALA X 177 1 22
HELIX 8 8 ASP X 189 THR X 193 5 5
HELIX 9 9 LEU X 201 GLY X 224 1 24
HELIX 10 10 ASN X 231 ASN X 242 1 12
HELIX 11 11 PRO X 243 GLY X 247 5 5
HELIX 12 12 ASP X 278 LEU X 282 5 5
HELIX 13 13 THR X 291 ALA X 308 1 18
HELIX 14 14 ALA X 308 THR X 313 1 6
HELIX 15 15 LEU X 314 TRP X 338 1 25
HELIX 16 16 THR A 53 LEU A 62 1 10
HELIX 17 17 ALA A 65 ALA A 70 5 6
HELIX 18 18 SER A 74 GLY A 81 1 8
HELIX 19 19 ARG A 94 ALA A 104 1 11
HELIX 20 20 GLY A 122 ALA A 128 1 7
HELIX 21 21 GLY A 145 GLN A 151 1 7
HELIX 22 22 ASN A 156 ALA A 177 1 22
HELIX 23 23 ASP A 189 THR A 193 5 5
HELIX 24 24 LEU A 201 GLY A 224 1 24
HELIX 25 25 ASN A 231 ASN A 242 1 12
HELIX 26 26 PRO A 243 GLY A 247 5 5
HELIX 27 27 ASP A 278 LEU A 282 5 5
HELIX 28 28 THR A 291 ALA A 308 1 18
HELIX 29 29 ALA A 308 THR A 313 1 6
HELIX 30 30 LEU A 314 TRP A 338 1 25
SHEET 1 A 4 LEU X 8 PHE X 11 0
SHEET 2 A 4 LEU X 139 ILE X 142 1 O TYR X 141 N PHE X 11
SHEET 3 A 4 ILE X 182 TRP X 185 1 O VAL X 183 N TYR X 140
SHEET 4 A 4 VAL X 227 LEU X 230 1 O LEU X 230 N VAL X 184
SHEET 1 B 2 SER X 108 ARG X 112 0
SHEET 2 B 2 THR X 115 ARG X 120 -1 O ARG X 118 N ILE X 110
SHEET 1 C13 ARG X 348 PHE X 360 0
SHEET 2 C13 GLY X 369 ARG X 383 -1 O GLY X 369 N PHE X 360
SHEET 3 C13 TRP X 388 ALA X 403 -1 O ALA X 390 N TYR X 382
SHEET 4 C13 SER X 408 GLU X 425 -1 O SER X 414 N TYR X 397
SHEET 5 C13 TRP X 428 LEU X 450 -1 O LYS X 445 N ASP X 409
SHEET 6 C13 GLY X 453 TYR X 474 -1 O ALA X 467 N THR X 435
SHEET 7 C13 TRP X 484 VAL X 499 -1 O ALA X 492 N ALA X 470
SHEET 8 C13 GLN X 517 ALA X 533 -1 O GLN X 529 N SER X 487
SHEET 9 C13 THR X 538 GLU X 549 -1 O LEU X 540 N TYR X 532
SHEET 10 C13 HIS X 579 ALA X 592 -1 O LEU X 580 N GLU X 547
SHEET 11 C13 LEU X 595 GLY X 606 -1 O LEU X 595 N LEU X 591
SHEET 12 C13 ASP X 609 ASP X 621 -1 O SER X 619 N SER X 596
SHEET 13 C13 ARG X 348 PHE X 360 -1 N VAL X 351 O LEU X 618
SHEET 1 D 3 LEU X 512 TYR X 514 0
SHEET 2 D 3 ASP X 556 LEU X 561 -1 O SER X 560 N ASP X 513
SHEET 3 D 3 PHE X 569 GLU X 572 -1 O PHE X 569 N MET X 559
SHEET 1 E 4 LEU A 8 PHE A 11 0
SHEET 2 E 4 LEU A 139 ILE A 142 1 O TYR A 141 N PHE A 11
SHEET 3 E 4 ILE A 182 TRP A 185 1 O VAL A 183 N TYR A 140
SHEET 4 E 4 VAL A 227 LEU A 230 1 O LEU A 230 N VAL A 184
SHEET 1 F 2 SER A 108 ARG A 112 0
SHEET 2 F 2 THR A 115 ARG A 120 -1 O ARG A 118 N ILE A 110
SHEET 1 G13 TRP A 347 PHE A 360 0
SHEET 2 G13 GLY A 369 ARG A 383 -1 O GLY A 369 N PHE A 360
SHEET 3 G13 TRP A 388 ALA A 403 -1 O ALA A 390 N TYR A 382
SHEET 4 G13 SER A 408 GLU A 425 -1 O GLN A 422 N ARG A 389
SHEET 5 G13 TRP A 428 LEU A 450 -1 O LYS A 445 N ASP A 409
SHEET 6 G13 GLY A 453 TYR A 474 -1 O ALA A 467 N THR A 435
SHEET 7 G13 TRP A 484 VAL A 499 -1 O ALA A 492 N ALA A 470
SHEET 8 G13 GLN A 517 ALA A 533 -1 O GLN A 529 N SER A 487
SHEET 9 G13 THR A 538 GLU A 549 -1 O LEU A 540 N TYR A 532
SHEET 10 G13 HIS A 579 ALA A 592 -1 O LEU A 580 N GLU A 547
SHEET 11 G13 LEU A 595 GLY A 606 -1 O LEU A 595 N LEU A 591
SHEET 12 G13 ASP A 609 ASP A 621 -1 O SER A 619 N SER A 596
SHEET 13 G13 TRP A 347 PHE A 360 -1 N GLY A 349 O LEU A 620
SHEET 1 H 3 LEU A 512 TYR A 514 0
SHEET 2 H 3 ASP A 556 LEU A 561 -1 O SER A 560 N ASP A 513
SHEET 3 H 3 LEU A 564 GLU A 572 -1 O PHE A 569 N MET A 559
SSBOND 1 CYS X 258 CYS X 264 1555 1555 2.03
SSBOND 2 CYS A 258 CYS A 264 1555 1555 2.04
CISPEP 1 GLY X 39 PRO X 40 0 1.22
CISPEP 2 GLY A 39 PRO A 40 0 2.93
SITE 1 AC1 9 SER X 14 LEU X 15 ASN X 147 LEU X 150
SITE 2 AC1 9 PRO X 188 LEU X 190 VAL X 288 HIS X 289
SITE 3 AC1 9 HOH X 767
SITE 1 AC2 2 SER X 32 PHE X 34
SITE 1 AC3 11 SER A 14 LEU A 15 GLY A 146 ASN A 147
SITE 2 AC3 11 LEU A 150 PRO A 188 LEU A 190 VAL A 288
SITE 3 AC3 11 HIS A 289 PRO A 290 HOH A 631
SITE 1 AC4 1 HOH X 791
SITE 1 AC5 4 PHE A 149 LEU X 201 PHE X 204 HOH X 770
SITE 1 AC6 1 ARG A 112
CRYST1 143.826 143.826 186.883 90.00 90.00 90.00 P 4 21 2 16
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 0.006953 0.000000 0.000000 0.00000
SCALE2 0.000000 0.006953 0.000000 0.00000
SCALE3 0.000000 0.000000 0.005351 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
