HEADER LYASE 17-MAR-11 3R4I
TITLE CRYSTAL STRUCTURE OF A CITRATE LYASE (BXE_B2899) FROM BURKHOLDERIA
TITLE 2 XENOVORANS LB400 AT 2.24 A RESOLUTION
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CITRATE LYASE;
COMPND 3 CHAIN: A, B, C, D, E, F;
COMPND 4 EC: 4.1.3.6;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: BURKHOLDERIA XENOVORANS;
SOURCE 3 ORGANISM_TAXID: 266265;
SOURCE 4 STRAIN: LB400;
SOURCE 5 GENE: BXENO_B0128, BXE_B2899;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: HK100;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: SPEEDET
KEYWDS TIM BETA/ALPHA-BARREL, STRUCTURAL GENOMICS, JOINT CENTER FOR
KEYWDS 2 STRUCTURAL GENOMICS, JCSG, PROTEIN STRUCTURE INITIATIVE, PSI-
KEYWDS 3 BIOLOGY, LYASE
EXPDTA X-RAY DIFFRACTION
AUTHOR JOINT CENTER FOR STRUCTURAL GENOMICS (JCSG)
REVDAT 3 01-FEB-23 3R4I 1 REMARK SEQADV LINK
REVDAT 2 25-OCT-17 3R4I 1 REMARK
REVDAT 1 06-APR-11 3R4I 0
JRNL AUTH JOINT CENTER FOR STRUCTURAL GENOMICS (JCSG)
JRNL TITL CRYSTAL STRUCTURE OF A CITRATE LYASE (BXE_B2899) FROM
JRNL TITL 2 BURKHOLDERIA XENOVORANS LB400 AT 2.24 A RESOLUTION
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.24 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.6.4
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 : TWIN_LSQ_F
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.24
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 48.60
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.710
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.3
REMARK 3 NUMBER OF REFLECTIONS : 93681
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.153
REMARK 3 R VALUE (WORKING SET) : 0.151
REMARK 3 FREE R VALUE : 0.174
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.020
REMARK 3 FREE R VALUE TEST SET COUNT : 4707
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 33.6411 - 6.0699 0.94 4453 241 0.1405 0.1659
REMARK 3 2 6.0699 - 4.8224 0.95 4463 242 0.1231 0.1339
REMARK 3 3 4.8224 - 4.2142 0.95 4463 244 0.1080 0.1253
REMARK 3 4 4.2142 - 3.8294 0.95 4452 235 0.1125 0.1345
REMARK 3 5 3.8294 - 3.5553 0.94 4480 236 0.1328 0.1666
REMARK 3 6 3.5553 - 3.3459 0.94 4418 265 0.1429 0.1728
REMARK 3 7 3.3459 - 3.1784 0.94 4434 237 0.1575 0.1751
REMARK 3 8 3.1784 - 3.0402 0.94 4486 241 0.1701 0.1921
REMARK 3 9 3.0402 - 2.9232 0.95 4425 220 0.1783 0.2080
REMARK 3 10 2.9232 - 2.8224 0.94 4437 258 0.1776 0.2023
REMARK 3 11 2.8224 - 2.7342 0.95 4477 238 0.1735 0.2115
REMARK 3 12 2.7342 - 2.6561 0.95 4437 212 0.1791 0.1786
REMARK 3 13 2.6561 - 2.5862 0.94 4412 250 0.1888 0.2207
REMARK 3 14 2.5862 - 2.5231 0.95 4500 199 0.1897 0.2084
REMARK 3 15 2.5231 - 2.4657 0.94 4455 225 0.1909 0.2129
REMARK 3 16 2.4657 - 2.4133 0.95 4473 225 0.1946 0.2100
REMARK 3 17 2.4133 - 2.3650 0.93 4385 257 0.1977 0.2512
REMARK 3 18 2.3650 - 2.3204 0.94 4395 211 0.2025 0.2336
REMARK 3 19 2.3204 - 2.2790 0.94 4465 251 0.2155 0.2486
REMARK 3 20 2.2790 - 2.2404 0.93 4423 214 0.2240 0.2500
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.00
REMARK 3 SHRINKAGE RADIUS : 0.72
REMARK 3 K_SOL : 0.36
REMARK 3 B_SOL : 33.44
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : NULL
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : NULL
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 37.13
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 37.45
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 3.59240
REMARK 3 B22 (A**2) : 3.59240
REMARK 3 B33 (A**2) : -7.18470
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: 0.4760
REMARK 3 OPERATOR: H,-H-K,-L
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : 0.007 14875
REMARK 3 ANGLE : 0.956 20355
REMARK 3 CHIRALITY : 0.064 2323
REMARK 3 PLANARITY : 0.004 2687
REMARK 3 DIHEDRAL : 11.286 5190
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 3:266)
REMARK 3 ORIGIN FOR THE GROUP (A): 14.6352 -17.8845 -34.2697
REMARK 3 T TENSOR
REMARK 3 T11: 0.1085 T22: 0.1427
REMARK 3 T33: 0.1092 T12: 0.0425
REMARK 3 T13: 0.0288 T23: 0.0124
REMARK 3 L TENSOR
REMARK 3 L11: 0.3935 L22: 0.2801
REMARK 3 L33: 0.2044 L12: 0.0564
REMARK 3 L13: -0.0977 L23: 0.0671
REMARK 3 S TENSOR
REMARK 3 S11: 0.0169 S12: 0.0767 S13: -0.0004
REMARK 3 S21: -0.0427 S22: -0.0167 S23: -0.0489
REMARK 3 S31: 0.0216 S32: 0.0491 S33: 0.0000
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: (CHAIN A AND RESID 267:327)
REMARK 3 ORIGIN FOR THE GROUP (A): -16.4538 -26.0585 -24.5067
REMARK 3 T TENSOR
REMARK 3 T11: 0.1694 T22: 0.1299
REMARK 3 T33: 0.2387 T12: -0.0247
REMARK 3 T13: 0.0204 T23: -0.0343
REMARK 3 L TENSOR
REMARK 3 L11: 0.0479 L22: 0.0316
REMARK 3 L33: 0.0605 L12: -0.0158
REMARK 3 L13: 0.0445 L23: -0.0383
REMARK 3 S TENSOR
REMARK 3 S11: -0.0630 S12: 0.0552 S13: -0.2038
REMARK 3 S21: -0.0296 S22: 0.0669 S23: -0.0111
REMARK 3 S31: 0.2520 S32: -0.0803 S33: 0.0000
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: (CHAIN B AND RESID 3:266)
REMARK 3 ORIGIN FOR THE GROUP (A): -4.3929 -22.6202 9.9398
REMARK 3 T TENSOR
REMARK 3 T11: 0.1633 T22: 0.0639
REMARK 3 T33: 0.0819 T12: -0.0166
REMARK 3 T13: 0.0315 T23: 0.0140
REMARK 3 L TENSOR
REMARK 3 L11: 0.2838 L22: 0.1576
REMARK 3 L33: 0.3267 L12: -0.1337
REMARK 3 L13: 0.0380 L23: -0.1921
REMARK 3 S TENSOR
REMARK 3 S11: 0.0279 S12: -0.0760 S13: 0.0250
REMARK 3 S21: 0.0398 S22: -0.0008 S23: 0.0399
REMARK 3 S31: 0.1276 S32: -0.0325 S33: 0.0000
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: (CHAIN B AND RESID 267:327)
REMARK 3 ORIGIN FOR THE GROUP (A): 26.9988 -15.0405 0.1446
REMARK 3 T TENSOR
REMARK 3 T11: 0.1623 T22: 0.1686
REMARK 3 T33: 0.2061 T12: 0.0502
REMARK 3 T13: 0.0047 T23: 0.0640
REMARK 3 L TENSOR
REMARK 3 L11: 0.0384 L22: 0.0341
REMARK 3 L33: 0.0489 L12: -0.0147
REMARK 3 L13: 0.0001 L23: 0.0393
REMARK 3 S TENSOR
REMARK 3 S11: 0.0042 S12: -0.0552 S13: -0.0908
REMARK 3 S21: -0.0654 S22: 0.0251 S23: -0.1283
REMARK 3 S31: 0.0950 S32: 0.1515 S33: -0.0000
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: (CHAIN C AND RESID 4:266)
REMARK 3 ORIGIN FOR THE GROUP (A): 56.7195 -57.9726 17.7809
REMARK 3 T TENSOR
REMARK 3 T11: 0.1801 T22: 0.2229
REMARK 3 T33: 0.1261 T12: -0.0492
REMARK 3 T13: -0.0037 T23: -0.0214
REMARK 3 L TENSOR
REMARK 3 L11: 0.3274 L22: 0.2252
REMARK 3 L33: 0.3379 L12: -0.0557
REMARK 3 L13: 0.1796 L23: -0.1915
REMARK 3 S TENSOR
REMARK 3 S11: -0.0556 S12: 0.0670 S13: -0.0550
REMARK 3 S21: -0.0314 S22: 0.0778 S23: -0.0496
REMARK 3 S31: 0.1220 S32: -0.1890 S33: 0.0000
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: (CHAIN C AND RESID 267:327)
REMARK 3 ORIGIN FOR THE GROUP (A): 47.9587 -27.1729 27.7626
REMARK 3 T TENSOR
REMARK 3 T11: 0.2606 T22: 0.3025
REMARK 3 T33: 0.2392 T12: 0.1045
REMARK 3 T13: -0.0313 T23: 0.0393
REMARK 3 L TENSOR
REMARK 3 L11: 0.0403 L22: 0.0326
REMARK 3 L33: 0.0585 L12: -0.0279
REMARK 3 L13: -0.0112 L23: -0.0219
REMARK 3 S TENSOR
REMARK 3 S11: 0.1363 S12: 0.0617 S13: -0.0434
REMARK 3 S21: 0.0975 S22: -0.1957 S23: 0.1694
REMARK 3 S31: -0.2293 S32: -0.0032 S33: -0.0001
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: (CHAIN D AND RESID 4:266)
REMARK 3 ORIGIN FOR THE GROUP (A): 51.4073 -38.8984 -17.7805
REMARK 3 T TENSOR
REMARK 3 T11: 0.0570 T22: 0.1442
REMARK 3 T33: 0.1252 T12: 0.0088
REMARK 3 T13: 0.0196 T23: -0.0101
REMARK 3 L TENSOR
REMARK 3 L11: 0.2054 L22: 0.2830
REMARK 3 L33: 0.2401 L12: -0.0733
REMARK 3 L13: -0.0878 L23: -0.1187
REMARK 3 S TENSOR
REMARK 3 S11: -0.0316 S12: -0.0221 S13: -0.0201
REMARK 3 S21: -0.0129 S22: 0.0456 S23: -0.0097
REMARK 3 S31: -0.0722 S32: -0.0501 S33: 0.0000
REMARK 3 TLS GROUP : 8
REMARK 3 SELECTION: (CHAIN D AND RESID 267:327)
REMARK 3 ORIGIN FOR THE GROUP (A): 59.7418 -69.9110 -27.3859
REMARK 3 T TENSOR
REMARK 3 T11: 0.1578 T22: 0.1215
REMARK 3 T33: 0.1111 T12: -0.0694
REMARK 3 T13: 0.0251 T23: -0.0075
REMARK 3 L TENSOR
REMARK 3 L11: 0.0331 L22: 0.0450
REMARK 3 L33: 0.0814 L12: -0.0371
REMARK 3 L13: 0.0346 L23: -0.0295
REMARK 3 S TENSOR
REMARK 3 S11: 0.0475 S12: 0.1340 S13: -0.0683
REMARK 3 S21: -0.1778 S22: -0.0068 S23: 0.0031
REMARK 3 S31: -0.1505 S32: 0.0517 S33: -0.0000
REMARK 3 TLS GROUP : 9
REMARK 3 SELECTION: (CHAIN E AND RESID 2:266)
REMARK 3 ORIGIN FOR THE GROUP (A): 13.0723 -66.7917 25.2325
REMARK 3 T TENSOR
REMARK 3 T11: 0.1304 T22: 0.1440
REMARK 3 T33: 0.1403 T12: -0.0498
REMARK 3 T13: -0.0344 T23: 0.0501
REMARK 3 L TENSOR
REMARK 3 L11: 0.1382 L22: 0.1462
REMARK 3 L33: 0.2627 L12: -0.0617
REMARK 3 L13: 0.0084 L23: -0.0177
REMARK 3 S TENSOR
REMARK 3 S11: -0.0483 S12: 0.0856 S13: 0.0637
REMARK 3 S21: -0.0478 S22: 0.0036 S23: 0.0070
REMARK 3 S31: -0.0992 S32: 0.1944 S33: -0.0000
REMARK 3 TLS GROUP : 10
REMARK 3 SELECTION: (CHAIN E AND RESID 267:328)
REMARK 3 ORIGIN FOR THE GROUP (A): 29.7827 -93.9860 34.6508
REMARK 3 T TENSOR
REMARK 3 T11: 0.1676 T22: 0.2501
REMARK 3 T33: 0.2274 T12: 0.0413
REMARK 3 T13: 0.0250 T23: 0.0515
REMARK 3 L TENSOR
REMARK 3 L11: 0.0679 L22: 0.0151
REMARK 3 L33: 0.0177 L12: -0.0156
REMARK 3 L13: -0.0359 L23: 0.0084
REMARK 3 S TENSOR
REMARK 3 S11: -0.0419 S12: -0.0230 S13: 0.0588
REMARK 3 S21: 0.2088 S22: 0.1339 S23: -0.1411
REMARK 3 S31: 0.0654 S32: -0.0611 S33: 0.0000
REMARK 3 TLS GROUP : 11
REMARK 3 SELECTION: (CHAIN F AND RESID 4:266)
REMARK 3 ORIGIN FOR THE GROUP (A): 23.0360 -83.8572 -10.5191
REMARK 3 T TENSOR
REMARK 3 T11: 0.2122 T22: 0.3626
REMARK 3 T33: 0.1764 T12: 0.0066
REMARK 3 T13: -0.0604 T23: 0.0826
REMARK 3 L TENSOR
REMARK 3 L11: 0.2178 L22: 0.4338
REMARK 3 L33: 0.2080 L12: 0.2587
REMARK 3 L13: -0.0180 L23: 0.0496
REMARK 3 S TENSOR
REMARK 3 S11: -0.0008 S12: -0.1810 S13: -0.0815
REMARK 3 S21: 0.1016 S22: -0.0889 S23: -0.0623
REMARK 3 S31: -0.0503 S32: 0.1604 S33: -0.0000
REMARK 3 TLS GROUP : 12
REMARK 3 SELECTION: (CHAIN F AND RESID 267:327)
REMARK 3 ORIGIN FOR THE GROUP (A): 7.2535 -55.7763 -19.9840
REMARK 3 T TENSOR
REMARK 3 T11: 0.2651 T22: 0.1777
REMARK 3 T33: 0.1317 T12: 0.0024
REMARK 3 T13: -0.0980 T23: -0.0426
REMARK 3 L TENSOR
REMARK 3 L11: 0.0301 L22: 0.0224
REMARK 3 L33: 0.0345 L12: -0.0218
REMARK 3 L13: -0.0160 L23: 0.0279
REMARK 3 S TENSOR
REMARK 3 S11: -0.0934 S12: -0.0330 S13: 0.2839
REMARK 3 S21: 0.0173 S22: -0.0261 S23: -0.1561
REMARK 3 S31: -0.0810 S32: -0.1369 S33: -0.0000
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 A AND (RESSEQ 4:12 OR RESSEQ 17:327
REMARK 3 )
REMARK 3 SELECTION : CHAIN B AND (RESSEQ 4:12 OR RESSEQ 17:327
REMARK 3 )
REMARK 3 ATOM PAIRS NUMBER : 2374
REMARK 3 RMSD : 0.041
REMARK 3 NCS OPERATOR : 2
REMARK 3 REFERENCE SELECTION: CHAIN A AND (RESSEQ 4:12 OR RESSEQ 17:327
REMARK 3 )
REMARK 3 SELECTION : CHAIN C AND (RESSEQ 4:12 OR RESSEQ 17:327
REMARK 3 )
REMARK 3 ATOM PAIRS NUMBER : 2375
REMARK 3 RMSD : 0.040
REMARK 3 NCS OPERATOR : 3
REMARK 3 REFERENCE SELECTION: CHAIN A AND (RESSEQ 4:12 OR RESSEQ 17:327
REMARK 3 )
REMARK 3 SELECTION : CHAIN D AND (RESSEQ 4:12 OR RESSEQ 17:327
REMARK 3 )
REMARK 3 ATOM PAIRS NUMBER : 2375
REMARK 3 RMSD : 0.032
REMARK 3 NCS OPERATOR : 4
REMARK 3 REFERENCE SELECTION: CHAIN A AND (RESSEQ 4:12 OR RESSEQ 17:327
REMARK 3 )
REMARK 3 SELECTION : CHAIN E AND (RESSEQ 4:12 OR RESSEQ 17:327
REMARK 3 )
REMARK 3 ATOM PAIRS NUMBER : 2315
REMARK 3 RMSD : 0.040
REMARK 3 NCS OPERATOR : 5
REMARK 3 REFERENCE SELECTION: CHAIN A AND (RESSEQ 4:12 OR RESSEQ 17:327
REMARK 3 )
REMARK 3 SELECTION : CHAIN F AND (RESSEQ 4:12 OR RESSEQ 17:327
REMARK 3 )
REMARK 3 ATOM PAIRS NUMBER : 2327
REMARK 3 RMSD : 0.041
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: 1. A MET-INHIBITION PROTOCOL WAS USED
REMARK 3 FOR SELENOMETHIONINE INCORPORATION DURING PROTEIN EXPRESSION.
REMARK 3 THE OCCUPANCY OF THE SE ATOMS IN THE MSE RESIDUES WAS REDUCED TO
REMARK 3 0.75 FOR THE REDUCED SCATTERING POWER DUE TO PARTIAL S-MET
REMARK 3 INCORPORATION. 2. CALCIUM (CA) AND ACETATE (ACT) FROM THE
REMARK 3 CRYSTALLIZATION SOLUTION, AND CHLORIDE (CL) FROM THE
REMARK 3 PURIFICATION BUFFER WERE MODELED INTO THE STRUCTURE. 3. ATOM
REMARK 3 RECORD CONTAINS SUM OF TLS AND RESIDUAL B FACTORS. ANISOU RECORD
REMARK 3 CONTAINS SUM OF TLS AND RESIDUAL U FACTORS. 4. THE DIFFRACTION
REMARK 3 DATA SHOW MEROHEDERAL TWINNING WITH TWIN LAW "H, -H-K, -L". THE
REMARK 3 REFINED TWIN FRACTION WAS 0.48. THE R-FREE TEST SET REFLECTIONS
REMARK 3 WERE CHOSEN AT RANDOM WITH THE TWIN LAW INCLUDED.
REMARK 4
REMARK 4 3R4I COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 23-MAR-11.
REMARK 100 THE DEPOSITION ID IS D_1000064478.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 10-JUN-10
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.33
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SSRL
REMARK 200 BEAMLINE : BL11-1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97879
REMARK 200 MONOCHROMATOR : SINGLE CRYSTAL SI(111) BENT
REMARK 200 OPTICS : FLAT MIRROR (VERTICAL FOCUSING);
REMARK 200 SINGLE CRYSTAL SI(111) BENT
REMARK 200 MONOCHROMATOR (HO RIZONTAL
REMARK 200 FOCUSING)
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 325 MM CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XSCALE JANUARY 30, 2009
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 93682
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.240
REMARK 200 RESOLUTION RANGE LOW (A) : 48.598
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 96.8
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : 0.06200
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 12.3600
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.24
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.32
REMARK 200 COMPLETENESS FOR SHELL (%) : 96.0
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.52700
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.800
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD
REMARK 200 SOFTWARE USED: SHELX, SHARP, SHELXD
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: THE STRUCTURE WAS INITIALLY PHASED IN SPACE GROUP P321.
REMARK 200 HOWEVER, ANAYSIS OF THE SOLUTION USING XTRIAGE AND INITIAL
REMARK 200 REFINEMENT RESULTS SUGGESTED THAT THE CORRECT SPACE GROUP WAS P3
REMARK 200 WITH MEROHEDRAL TWINNING.
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 45.29
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.25
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 44.0% POLYETHYLENE GLYCOL 600, 0.15M
REMARK 280 CALCIUM ACETATE, 0.1M SODIUM CACODYLATE PH 6.33, NANODROP, VAPOR
REMARK 280 DIFFUSION, SITTING DROP, TEMPERATURE 277K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 3
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z
REMARK 290 3555 -X+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 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3, 4, 5, 6
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 300 REMARK: ANALYTICAL SIZE EXCLUSION CHROMATOGRAPHY SUPPORTS THE
REMARK 300 ASSIGNMENT OF A TRIMER AS A SIGNIFICANT OLIGOMERIZATION STATE IN
REMARK 300 SOLUTION.
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: TRIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 10320 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 35430 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -107.0 KCAL/MOL
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 BIOMT1 2 -0.500000 -0.866025 0.000000 0.00000
REMARK 350 BIOMT2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 350 BIOMT2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 350 BIOMT3 3 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TRIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 10780 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 35010 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -139.0 KCAL/MOL
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 350 BIOMT1 2 -0.500000 -0.866025 0.000000 0.00000
REMARK 350 BIOMT2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 350 BIOMT2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 350 BIOMT3 3 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 3
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TRIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 12060 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 34770 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -175.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C
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 BIOMT1 2 -0.500000 -0.866025 0.000000 74.23400
REMARK 350 BIOMT2 2 0.866025 -0.500000 0.000000 -128.57706
REMARK 350 BIOMT3 2 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT1 3 -0.500000 0.866025 0.000000 148.46800
REMARK 350 BIOMT2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 350 BIOMT3 3 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 4
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TRIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 11540 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 33480 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -145.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: D
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 BIOMT1 2 -0.500000 -0.866025 0.000000 74.23400
REMARK 350 BIOMT2 2 0.866025 -0.500000 0.000000 -128.57706
REMARK 350 BIOMT3 2 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT1 3 -0.500000 0.866025 0.000000 148.46800
REMARK 350 BIOMT2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 350 BIOMT3 3 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 5
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TRIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 10370 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 34190 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -148.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: E
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 BIOMT1 2 -0.500000 -0.866025 0.000000 -74.23400
REMARK 350 BIOMT2 2 0.866025 -0.500000 0.000000 -128.57706
REMARK 350 BIOMT3 2 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT1 3 -0.500000 0.866025 0.000000 74.23400
REMARK 350 BIOMT2 3 -0.866025 -0.500000 0.000000 -128.57706
REMARK 350 BIOMT3 3 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 6
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TRIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 10440 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 33890 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -149.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: F
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 BIOMT1 2 -0.500000 -0.866025 0.000000 -74.23400
REMARK 350 BIOMT2 2 0.866025 -0.500000 0.000000 -128.57706
REMARK 350 BIOMT3 2 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT1 3 -0.500000 0.866025 0.000000 74.23400
REMARK 350 BIOMT2 3 -0.866025 -0.500000 0.000000 -128.57706
REMARK 350 BIOMT3 3 0.000000 0.000000 1.000000 0.00000
REMARK 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375 HOH C 577 LIES ON A SPECIAL POSITION.
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 0
REMARK 465 MSE A 1
REMARK 465 ARG A 2
REMARK 465 GLY A 13
REMARK 465 GLU A 14
REMARK 465 VAL A 15
REMARK 465 PRO A 16
REMARK 465 THR A 328
REMARK 465 LYS A 329
REMARK 465 VAL A 330
REMARK 465 GLY A 331
REMARK 465 THR A 332
REMARK 465 ASN A 333
REMARK 465 VAL A 334
REMARK 465 GLN A 335
REMARK 465 ALA A 336
REMARK 465 ALA A 337
REMARK 465 SER A 338
REMARK 465 GLY B 0
REMARK 465 MSE B 1
REMARK 465 ARG B 2
REMARK 465 GLY B 13
REMARK 465 GLU B 14
REMARK 465 VAL B 15
REMARK 465 PRO B 16
REMARK 465 PRO B 17
REMARK 465 ALA B 18
REMARK 465 THR B 328
REMARK 465 LYS B 329
REMARK 465 VAL B 330
REMARK 465 GLY B 331
REMARK 465 THR B 332
REMARK 465 ASN B 333
REMARK 465 VAL B 334
REMARK 465 GLN B 335
REMARK 465 ALA B 336
REMARK 465 ALA B 337
REMARK 465 SER B 338
REMARK 465 GLY C 0
REMARK 465 MSE C 1
REMARK 465 ARG C 2
REMARK 465 ALA C 3
REMARK 465 GLY C 13
REMARK 465 GLU C 14
REMARK 465 VAL C 15
REMARK 465 PRO C 16
REMARK 465 THR C 328
REMARK 465 LYS C 329
REMARK 465 VAL C 330
REMARK 465 GLY C 331
REMARK 465 THR C 332
REMARK 465 ASN C 333
REMARK 465 VAL C 334
REMARK 465 GLN C 335
REMARK 465 ALA C 336
REMARK 465 ALA C 337
REMARK 465 SER C 338
REMARK 465 GLY D 0
REMARK 465 MSE D 1
REMARK 465 ARG D 2
REMARK 465 ALA D 3
REMARK 465 GLY D 13
REMARK 465 GLU D 14
REMARK 465 VAL D 15
REMARK 465 PRO D 16
REMARK 465 PRO D 17
REMARK 465 ALA D 18
REMARK 465 VAL D 19
REMARK 465 THR D 328
REMARK 465 LYS D 329
REMARK 465 VAL D 330
REMARK 465 GLY D 331
REMARK 465 THR D 332
REMARK 465 ASN D 333
REMARK 465 VAL D 334
REMARK 465 GLN D 335
REMARK 465 ALA D 336
REMARK 465 ALA D 337
REMARK 465 SER D 338
REMARK 465 GLY E 0
REMARK 465 MSE E 1
REMARK 465 GLY E 13
REMARK 465 GLU E 14
REMARK 465 VAL E 15
REMARK 465 PRO E 16
REMARK 465 PRO E 17
REMARK 465 ALA E 18
REMARK 465 VAL E 19
REMARK 465 LYS E 329
REMARK 465 VAL E 330
REMARK 465 GLY E 331
REMARK 465 THR E 332
REMARK 465 ASN E 333
REMARK 465 VAL E 334
REMARK 465 GLN E 335
REMARK 465 ALA E 336
REMARK 465 ALA E 337
REMARK 465 SER E 338
REMARK 465 GLY F 0
REMARK 465 MSE F 1
REMARK 465 ARG F 2
REMARK 465 ALA F 3
REMARK 465 GLY F 13
REMARK 465 GLU F 14
REMARK 465 VAL F 15
REMARK 465 PRO F 16
REMARK 465 PRO F 17
REMARK 465 ALA F 18
REMARK 465 VAL F 19
REMARK 465 THR F 328
REMARK 465 LYS F 329
REMARK 465 VAL F 330
REMARK 465 GLY F 331
REMARK 465 THR F 332
REMARK 465 ASN F 333
REMARK 465 VAL F 334
REMARK 465 GLN F 335
REMARK 465 ALA F 336
REMARK 465 ALA F 337
REMARK 465 SER F 338
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 ARG A 61 CG CD NE CZ NH1 NH2
REMARK 470 GLN A 64 CG CD OE1 NE2
REMARK 470 GLU A 76 CG CD OE1 OE2
REMARK 470 ARG A 79 CG CD NE CZ NH1 NH2
REMARK 470 LEU A 101 CG CD1 CD2
REMARK 470 LYS A 107 CG CD CE NZ
REMARK 470 ILE A 118 O
REMARK 470 ARG A 119 CZ NH1 NH2
REMARK 470 ARG A 158 NE CZ NH1 NH2
REMARK 470 ARG A 192 CD NE CZ NH1 NH2
REMARK 470 ARG A 268 CG CD NE CZ NH1 NH2
REMARK 470 ARG A 311 CD NE CZ NH1 NH2
REMARK 470 ARG A 317 CG CD NE CZ NH1 NH2
REMARK 470 GLN A 321 CG CD OE1 NE2
REMARK 470 LYS B 31 CG CD CE NZ
REMARK 470 ARG B 61 CG CD NE CZ NH1 NH2
REMARK 470 GLN B 64 CG CD OE1 NE2
REMARK 470 GLU B 76 CG CD OE1 OE2
REMARK 470 ARG B 79 CG CD NE CZ NH1 NH2
REMARK 470 ASP B 91 CG OD1 OD2
REMARK 470 ARG B 96 CG CD NE CZ NH1 NH2
REMARK 470 LEU B 101 CG CD1 CD2
REMARK 470 LYS B 107 CG CD CE NZ
REMARK 470 HIS B 122 CG ND1 CD2 CE1 NE2
REMARK 470 ARG B 158 NE CZ NH1 NH2
REMARK 470 ARG B 192 CD NE CZ NH1 NH2
REMARK 470 GLU B 259 CG CD OE1 OE2
REMARK 470 ARG B 268 CG CD NE CZ NH1 NH2
REMARK 470 ARG B 311 CG CD NE CZ NH1 NH2
REMARK 470 ARG B 317 CG CD NE CZ NH1 NH2
REMARK 470 VAL C 19 CG1 CG2
REMARK 470 LYS C 31 CG CD CE NZ
REMARK 470 LYS C 35 CE NZ
REMARK 470 ARG C 61 CG CD NE CZ NH1 NH2
REMARK 470 LEU C 68 CG CD1 CD2
REMARK 470 ARG C 79 CG CD NE CZ NH1 NH2
REMARK 470 ARG C 100 CG CD NE CZ NH1 NH2
REMARK 470 LEU C 101 CG CD1 CD2
REMARK 470 LEU C 103 CG CD1 CD2
REMARK 470 LYS C 107 CD CE NZ
REMARK 470 HIS C 122 CG ND1 CD2 CE1 NE2
REMARK 470 ARG C 158 NE CZ NH1 NH2
REMARK 470 ARG C 192 CD NE CZ NH1 NH2
REMARK 470 GLU C 259 CG CD OE1 OE2
REMARK 470 ARG C 310 CG CD NE CZ NH1 NH2
REMARK 470 ARG C 311 CD NE CZ NH1 NH2
REMARK 470 ASP C 322 CG OD1 OD2
REMARK 470 PHE C 327 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 ARG D 61 CG CD NE CZ NH1 NH2
REMARK 470 GLN D 64 CG CD OE1 NE2
REMARK 470 GLU D 76 CG CD OE1 OE2
REMARK 470 ARG D 79 CG CD NE CZ NH1 NH2
REMARK 470 ARG D 96 CG CD NE CZ NH1 NH2
REMARK 470 ARG D 100 CG CD NE CZ NH1 NH2
REMARK 470 ARG D 119 CZ NH1 NH2
REMARK 470 HIS D 122 CG ND1 CD2 CE1 NE2
REMARK 470 ARG D 136 CG CD NE CZ NH1 NH2
REMARK 470 GLN D 142 CG CD OE1 NE2
REMARK 470 ARG D 158 NE CZ NH1 NH2
REMARK 470 ARG D 192 CD NE CZ NH1 NH2
REMARK 470 GLU D 259 CG CD OE1 OE2
REMARK 470 ARG D 311 CG CD NE CZ NH1 NH2
REMARK 470 THR D 315 OG1 CG2
REMARK 470 GLN D 321 CG CD OE1 NE2
REMARK 470 ARG E 2 CG CD NE CZ NH1 NH2
REMARK 470 LYS E 31 CG CD CE NZ
REMARK 470 ARG E 61 CG CD NE CZ NH1 NH2
REMARK 470 GLN E 64 CG CD OE1 NE2
REMARK 470 LEU E 68 CG CD1 CD2
REMARK 470 GLU E 76 CG CD OE1 OE2
REMARK 470 ARG E 79 CG CD NE CZ NH1 NH2
REMARK 470 ARG E 96 CG CD NE CZ NH1 NH2
REMARK 470 LEU E 103 CG CD1 CD2
REMARK 470 LYS E 107 CG CD CE NZ
REMARK 470 ILE E 118 CG1 CG2 CD1
REMARK 470 ARG E 119 CD NE CZ NH1 NH2
REMARK 470 HIS E 122 CG ND1 CD2 CE1 NE2
REMARK 470 GLU E 126 CG CD OE1 OE2
REMARK 470 PHE E 130 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 ARG E 136 CG CD NE CZ NH1 NH2
REMARK 470 GLN E 142 CD OE1 NE2
REMARK 470 ARG E 158 NE CZ NH1 NH2
REMARK 470 ARG E 192 CD NE CZ NH1 NH2
REMARK 470 ARG E 229 CG CD NE CZ NH1 NH2
REMARK 470 ILE E 253 CG1 CG2 CD1
REMARK 470 GLU E 259 CG CD OE1 OE2
REMARK 470 ARG E 310 CG CD NE CZ NH1 NH2
REMARK 470 ARG E 311 CG CD NE CZ NH1 NH2
REMARK 470 THR E 315 OG1 CG2
REMARK 470 VAL E 319 CG1 CG2
REMARK 470 GLN E 321 CG CD OE1 NE2
REMARK 470 THR E 328 OG1 CG2
REMARK 470 LYS F 31 CG CD CE NZ
REMARK 470 ARG F 61 CG CD NE CZ NH1 NH2
REMARK 470 GLN F 64 CG CD OE1 NE2
REMARK 470 GLU F 76 CG CD OE1 OE2
REMARK 470 ARG F 79 CG CD NE CZ NH1 NH2
REMARK 470 ARG F 100 CG CD NE CZ NH1 NH2
REMARK 470 LEU F 101 CG CD1 CD2
REMARK 470 LEU F 103 CG CD1 CD2
REMARK 470 LYS F 107 CG CD CE NZ
REMARK 470 ARG F 119 CD NE CZ NH1 NH2
REMARK 470 HIS F 122 CG ND1 CD2 CE1 NE2
REMARK 470 PHE F 130 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 ARG F 136 CG CD NE CZ NH1 NH2
REMARK 470 GLN F 142 CG CD OE1 NE2
REMARK 470 ARG F 158 NE CZ NH1 NH2
REMARK 470 ARG F 192 CD NE CZ NH1 NH2
REMARK 470 LYS F 218 CG CD CE NZ
REMARK 470 ARG F 229 CG CD NE CZ NH1 NH2
REMARK 470 ARG F 310 CG CD NE CZ NH1 NH2
REMARK 470 ARG F 311 CG CD NE CZ NH1 NH2
REMARK 470 ARG F 317 CG CD NE CZ NH1 NH2
REMARK 470 GLN F 321 CG CD OE1 NE2
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 OD2 ASP B 198 O HOH B 362 2.18
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 OD2 ASP B 188 O HOH A 391 3555 2.17
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 GLU A 54 -121.97 -94.47
REMARK 500 ARG A 82 49.61 -107.77
REMARK 500 GLU A 151 18.81 -148.49
REMARK 500 ARG A 229 -61.57 -108.43
REMARK 500 HIS A 293 -112.85 57.98
REMARK 500 ASP A 294 8.91 58.66
REMARK 500 THR A 315 21.34 -72.91
REMARK 500 PRO A 325 3.77 -69.93
REMARK 500 GLU B 54 -120.89 -92.02
REMARK 500 ARG B 82 49.74 -109.16
REMARK 500 GLU B 151 21.60 -147.96
REMARK 500 HIS B 293 -113.18 57.31
REMARK 500 ASP B 294 7.37 58.87
REMARK 500 GLU C 54 -121.55 -92.42
REMARK 500 ARG C 82 51.39 -107.41
REMARK 500 GLU C 151 20.65 -148.26
REMARK 500 ARG C 229 -61.10 -109.32
REMARK 500 HIS C 293 -113.59 57.25
REMARK 500 ASP C 294 8.18 58.15
REMARK 500 THR C 315 20.43 -74.23
REMARK 500 GLU D 54 -122.36 -93.20
REMARK 500 ARG D 82 49.93 -107.46
REMARK 500 GLU D 151 18.59 -147.13
REMARK 500 TRP D 287 19.37 58.99
REMARK 500 HIS D 293 -113.19 58.50
REMARK 500 ASP D 294 6.45 59.17
REMARK 500 THR D 315 20.53 -72.05
REMARK 500 GLU E 54 -122.05 -92.95
REMARK 500 ARG E 82 50.15 -108.49
REMARK 500 GLU E 151 20.43 -147.72
REMARK 500 HIS E 293 -110.93 64.39
REMARK 500 THR E 315 22.33 -73.37
REMARK 500 PRO E 325 1.64 -69.23
REMARK 500 GLU F 54 -123.00 -95.03
REMARK 500 ARG F 82 49.22 -106.50
REMARK 500 GLU F 151 17.65 -145.82
REMARK 500 HIS F 293 -120.92 56.11
REMARK 500 THR F 315 20.70 -73.59
REMARK 500 PRO F 325 2.95 -68.99
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 CA A 341 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU A 151 OE1
REMARK 620 2 ASP A 177 OD2 85.6
REMARK 620 3 HOH A 372 O 81.6 82.7
REMARK 620 4 HOH A 381 O 100.6 92.3 174.4
REMARK 620 5 HOH A 427 O 160.5 77.0 87.6 88.8
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 346 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 230 OD1
REMARK 620 2 ASP A 230 OD2 50.0
REMARK 620 3 HOH A 390 O 131.1 83.2
REMARK 620 4 HOH A 391 O 165.0 144.1 63.9
REMARK 620 5 HOH A 550 O 101.7 93.1 93.3 75.9
REMARK 620 6 HOH B 408 O 74.7 123.8 152.9 90.3 88.0
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA B 340 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH A 385 O
REMARK 620 2 ASP B 230 OD1 62.3
REMARK 620 3 ASP B 230 OD2 111.1 49.0
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA B 339 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU B 151 OE1
REMARK 620 2 ASP B 177 OD2 91.9
REMARK 620 3 HOH B 395 O 156.8 100.4
REMARK 620 4 HOH B 397 O 93.5 93.0 66.5
REMARK 620 5 HOH B 432 O 90.4 175.7 78.8 90.5
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA C 343 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU C 151 OE1
REMARK 620 2 ASP C 177 OD2 77.9
REMARK 620 3 HOH C 407 O 71.1 92.6
REMARK 620 4 HOH C 442 O 155.5 77.7 108.6
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA C 344 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP C 230 OD1
REMARK 620 2 ASP C 230 OD2 47.7
REMARK 620 3 HOH C 402 O 84.9 73.9
REMARK 620 4 HOH C 426 O 78.2 85.2 158.8
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA D 342 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU D 151 OE1
REMARK 620 2 ASP D 177 OD2 89.8
REMARK 620 3 HOH D 364 O 93.4 169.3
REMARK 620 4 HOH D 430 O 160.4 99.7 80.4
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA D 345 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP D 230 OD1
REMARK 620 2 ASP D 230 OD2 45.4
REMARK 620 3 HOH D 549 O 82.0 65.4
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA E 348 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU E 151 OE1
REMARK 620 2 ASP E 177 OD2 84.1
REMARK 620 3 HOH E 463 O 177.8 97.1
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA E 347 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP E 230 OD1
REMARK 620 2 ASP E 230 OD2 44.3
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA F 349 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU F 151 OE1
REMARK 620 2 ASP F 177 OD2 79.1
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA F 351 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP F 230 OD1
REMARK 620 2 ASP F 230 OD2 47.2
REMARK 620 N 1
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 341
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 346
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA B 339
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA B 340
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL B 354
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA C 343
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA C 344
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL C 353
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT C 357
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA D 342
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA D 345
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA D 350
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL D 352
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT D 358
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA E 347
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA E 348
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL E 355
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA F 349
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA F 351
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL F 356
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 397760 RELATED DB: TARGETDB
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 THE CONSTRUCT WAS EXPRESSED WITH A PURIFICATION TAG
REMARK 999 MGSDKIHHHHHHENLYFQG. THE TAG WAS REMOVED WITH TEV PROTEASE LEAVING
REMARK 999 ONLY A GLYCINE (0) FOLLOWED BY THE TARGET SEQUENCE.
DBREF 3R4I A 1 338 UNP Q13S43 Q13S43_BURXL 1 338
DBREF 3R4I B 1 338 UNP Q13S43 Q13S43_BURXL 1 338
DBREF 3R4I C 1 338 UNP Q13S43 Q13S43_BURXL 1 338
DBREF 3R4I D 1 338 UNP Q13S43 Q13S43_BURXL 1 338
DBREF 3R4I E 1 338 UNP Q13S43 Q13S43_BURXL 1 338
DBREF 3R4I F 1 338 UNP Q13S43 Q13S43_BURXL 1 338
SEQADV 3R4I GLY A 0 UNP Q13S43 EXPRESSION TAG
SEQADV 3R4I GLY B 0 UNP Q13S43 EXPRESSION TAG
SEQADV 3R4I GLY C 0 UNP Q13S43 EXPRESSION TAG
SEQADV 3R4I GLY D 0 UNP Q13S43 EXPRESSION TAG
SEQADV 3R4I GLY E 0 UNP Q13S43 EXPRESSION TAG
SEQADV 3R4I GLY F 0 UNP Q13S43 EXPRESSION TAG
SEQRES 1 A 339 GLY MSE ARG ALA LEU THR PRO ALA GLU VAL LEU PHE ASP
SEQRES 2 A 339 GLY GLU VAL PRO PRO ALA VAL LEU PRO ALA CYS ASP HIS
SEQRES 3 A 339 TYR ALA GLY SER GLU LYS LEU MSE LEU LYS SER LEU ALA
SEQRES 4 A 339 LEU GLN GLN GLN LEU GLY PRO VAL PHE ASP ILE THR LEU
SEQRES 5 A 339 ASP CYS GLU ASP GLY ALA GLN VAL GLY ARG GLU ALA GLN
SEQRES 6 A 339 HIS ALA GLU LEU VAL ALA SER LEU LEU GLY SER GLU HIS
SEQRES 7 A 339 ASP ARG PHE GLY ARG VAL GLY VAL ARG ILE HIS ASP PHE
SEQRES 8 A 339 ASP HIS ALA HIS TRP ARG ASP ASP VAL ARG LEU ILE LEU
SEQRES 9 A 339 ARG ALA ALA LYS ARG ALA PRO ALA TYR ILE THR LEU PRO
SEQRES 10 A 339 LYS ILE ARG HIS VAL HIS ASP ALA ALA GLU MSE VAL ALA
SEQRES 11 A 339 PHE ILE GLU ALA THR ARG ARG GLU LEU GLY ILE ALA GLN
SEQRES 12 A 339 PRO VAL PRO VAL GLN LEU LEU VAL GLU THR HIS GLY ALA
SEQRES 13 A 339 LEU THR ARG VAL PHE ASP LEU ALA ALA LEU PRO GLY VAL
SEQRES 14 A 339 GLU ALA LEU SER PHE GLY LEU MSE ASP PHE VAL SER ALA
SEQRES 15 A 339 HIS ASP GLY ALA ILE PRO ASP THR ALA MSE ARG SER PRO
SEQRES 16 A 339 GLY GLN PHE ASP HIS PRO LEU VAL ARG ARG ALA LYS LEU
SEQRES 17 A 339 GLU ILE SER ALA ALA CYS HIS ALA TYR GLY LYS VAL PRO
SEQRES 18 A 339 SER HIS ASN VAL SER THR GLU VAL ARG ASP MSE SER VAL
SEQRES 19 A 339 VAL ALA ASN ASP ALA ALA ARG ALA ARG ASN GLU PHE GLY
SEQRES 20 A 339 TYR THR ARG MSE TRP SER ILE HIS PRO ALA GLN ILE GLU
SEQRES 21 A 339 ALA ILE VAL ALA ALA PHE ALA PRO ARG ASP GLU GLU ILE
SEQRES 22 A 339 THR THR ALA THR GLU ILE LEU LEU ALA ALA GLN SER ALA
SEQRES 23 A 339 GLN TRP GLY PRO THR ARG TYR HIS ASP THR LEU HIS ASP
SEQRES 24 A 339 ARG ALA SER TYR ARG TYR TYR TRP SER VAL LEU ARG ARG
SEQRES 25 A 339 ALA GLN ALA THR GLY ARG ALA VAL PRO GLN ASP ALA ALA
SEQRES 26 A 339 PRO LEU PHE THR LYS VAL GLY THR ASN VAL GLN ALA ALA
SEQRES 27 A 339 SER
SEQRES 1 B 339 GLY MSE ARG ALA LEU THR PRO ALA GLU VAL LEU PHE ASP
SEQRES 2 B 339 GLY GLU VAL PRO PRO ALA VAL LEU PRO ALA CYS ASP HIS
SEQRES 3 B 339 TYR ALA GLY SER GLU LYS LEU MSE LEU LYS SER LEU ALA
SEQRES 4 B 339 LEU GLN GLN GLN LEU GLY PRO VAL PHE ASP ILE THR LEU
SEQRES 5 B 339 ASP CYS GLU ASP GLY ALA GLN VAL GLY ARG GLU ALA GLN
SEQRES 6 B 339 HIS ALA GLU LEU VAL ALA SER LEU LEU GLY SER GLU HIS
SEQRES 7 B 339 ASP ARG PHE GLY ARG VAL GLY VAL ARG ILE HIS ASP PHE
SEQRES 8 B 339 ASP HIS ALA HIS TRP ARG ASP ASP VAL ARG LEU ILE LEU
SEQRES 9 B 339 ARG ALA ALA LYS ARG ALA PRO ALA TYR ILE THR LEU PRO
SEQRES 10 B 339 LYS ILE ARG HIS VAL HIS ASP ALA ALA GLU MSE VAL ALA
SEQRES 11 B 339 PHE ILE GLU ALA THR ARG ARG GLU LEU GLY ILE ALA GLN
SEQRES 12 B 339 PRO VAL PRO VAL GLN LEU LEU VAL GLU THR HIS GLY ALA
SEQRES 13 B 339 LEU THR ARG VAL PHE ASP LEU ALA ALA LEU PRO GLY VAL
SEQRES 14 B 339 GLU ALA LEU SER PHE GLY LEU MSE ASP PHE VAL SER ALA
SEQRES 15 B 339 HIS ASP GLY ALA ILE PRO ASP THR ALA MSE ARG SER PRO
SEQRES 16 B 339 GLY GLN PHE ASP HIS PRO LEU VAL ARG ARG ALA LYS LEU
SEQRES 17 B 339 GLU ILE SER ALA ALA CYS HIS ALA TYR GLY LYS VAL PRO
SEQRES 18 B 339 SER HIS ASN VAL SER THR GLU VAL ARG ASP MSE SER VAL
SEQRES 19 B 339 VAL ALA ASN ASP ALA ALA ARG ALA ARG ASN GLU PHE GLY
SEQRES 20 B 339 TYR THR ARG MSE TRP SER ILE HIS PRO ALA GLN ILE GLU
SEQRES 21 B 339 ALA ILE VAL ALA ALA PHE ALA PRO ARG ASP GLU GLU ILE
SEQRES 22 B 339 THR THR ALA THR GLU ILE LEU LEU ALA ALA GLN SER ALA
SEQRES 23 B 339 GLN TRP GLY PRO THR ARG TYR HIS ASP THR LEU HIS ASP
SEQRES 24 B 339 ARG ALA SER TYR ARG TYR TYR TRP SER VAL LEU ARG ARG
SEQRES 25 B 339 ALA GLN ALA THR GLY ARG ALA VAL PRO GLN ASP ALA ALA
SEQRES 26 B 339 PRO LEU PHE THR LYS VAL GLY THR ASN VAL GLN ALA ALA
SEQRES 27 B 339 SER
SEQRES 1 C 339 GLY MSE ARG ALA LEU THR PRO ALA GLU VAL LEU PHE ASP
SEQRES 2 C 339 GLY GLU VAL PRO PRO ALA VAL LEU PRO ALA CYS ASP HIS
SEQRES 3 C 339 TYR ALA GLY SER GLU LYS LEU MSE LEU LYS SER LEU ALA
SEQRES 4 C 339 LEU GLN GLN GLN LEU GLY PRO VAL PHE ASP ILE THR LEU
SEQRES 5 C 339 ASP CYS GLU ASP GLY ALA GLN VAL GLY ARG GLU ALA GLN
SEQRES 6 C 339 HIS ALA GLU LEU VAL ALA SER LEU LEU GLY SER GLU HIS
SEQRES 7 C 339 ASP ARG PHE GLY ARG VAL GLY VAL ARG ILE HIS ASP PHE
SEQRES 8 C 339 ASP HIS ALA HIS TRP ARG ASP ASP VAL ARG LEU ILE LEU
SEQRES 9 C 339 ARG ALA ALA LYS ARG ALA PRO ALA TYR ILE THR LEU PRO
SEQRES 10 C 339 LYS ILE ARG HIS VAL HIS ASP ALA ALA GLU MSE VAL ALA
SEQRES 11 C 339 PHE ILE GLU ALA THR ARG ARG GLU LEU GLY ILE ALA GLN
SEQRES 12 C 339 PRO VAL PRO VAL GLN LEU LEU VAL GLU THR HIS GLY ALA
SEQRES 13 C 339 LEU THR ARG VAL PHE ASP LEU ALA ALA LEU PRO GLY VAL
SEQRES 14 C 339 GLU ALA LEU SER PHE GLY LEU MSE ASP PHE VAL SER ALA
SEQRES 15 C 339 HIS ASP GLY ALA ILE PRO ASP THR ALA MSE ARG SER PRO
SEQRES 16 C 339 GLY GLN PHE ASP HIS PRO LEU VAL ARG ARG ALA LYS LEU
SEQRES 17 C 339 GLU ILE SER ALA ALA CYS HIS ALA TYR GLY LYS VAL PRO
SEQRES 18 C 339 SER HIS ASN VAL SER THR GLU VAL ARG ASP MSE SER VAL
SEQRES 19 C 339 VAL ALA ASN ASP ALA ALA ARG ALA ARG ASN GLU PHE GLY
SEQRES 20 C 339 TYR THR ARG MSE TRP SER ILE HIS PRO ALA GLN ILE GLU
SEQRES 21 C 339 ALA ILE VAL ALA ALA PHE ALA PRO ARG ASP GLU GLU ILE
SEQRES 22 C 339 THR THR ALA THR GLU ILE LEU LEU ALA ALA GLN SER ALA
SEQRES 23 C 339 GLN TRP GLY PRO THR ARG TYR HIS ASP THR LEU HIS ASP
SEQRES 24 C 339 ARG ALA SER TYR ARG TYR TYR TRP SER VAL LEU ARG ARG
SEQRES 25 C 339 ALA GLN ALA THR GLY ARG ALA VAL PRO GLN ASP ALA ALA
SEQRES 26 C 339 PRO LEU PHE THR LYS VAL GLY THR ASN VAL GLN ALA ALA
SEQRES 27 C 339 SER
SEQRES 1 D 339 GLY MSE ARG ALA LEU THR PRO ALA GLU VAL LEU PHE ASP
SEQRES 2 D 339 GLY GLU VAL PRO PRO ALA VAL LEU PRO ALA CYS ASP HIS
SEQRES 3 D 339 TYR ALA GLY SER GLU LYS LEU MSE LEU LYS SER LEU ALA
SEQRES 4 D 339 LEU GLN GLN GLN LEU GLY PRO VAL PHE ASP ILE THR LEU
SEQRES 5 D 339 ASP CYS GLU ASP GLY ALA GLN VAL GLY ARG GLU ALA GLN
SEQRES 6 D 339 HIS ALA GLU LEU VAL ALA SER LEU LEU GLY SER GLU HIS
SEQRES 7 D 339 ASP ARG PHE GLY ARG VAL GLY VAL ARG ILE HIS ASP PHE
SEQRES 8 D 339 ASP HIS ALA HIS TRP ARG ASP ASP VAL ARG LEU ILE LEU
SEQRES 9 D 339 ARG ALA ALA LYS ARG ALA PRO ALA TYR ILE THR LEU PRO
SEQRES 10 D 339 LYS ILE ARG HIS VAL HIS ASP ALA ALA GLU MSE VAL ALA
SEQRES 11 D 339 PHE ILE GLU ALA THR ARG ARG GLU LEU GLY ILE ALA GLN
SEQRES 12 D 339 PRO VAL PRO VAL GLN LEU LEU VAL GLU THR HIS GLY ALA
SEQRES 13 D 339 LEU THR ARG VAL PHE ASP LEU ALA ALA LEU PRO GLY VAL
SEQRES 14 D 339 GLU ALA LEU SER PHE GLY LEU MSE ASP PHE VAL SER ALA
SEQRES 15 D 339 HIS ASP GLY ALA ILE PRO ASP THR ALA MSE ARG SER PRO
SEQRES 16 D 339 GLY GLN PHE ASP HIS PRO LEU VAL ARG ARG ALA LYS LEU
SEQRES 17 D 339 GLU ILE SER ALA ALA CYS HIS ALA TYR GLY LYS VAL PRO
SEQRES 18 D 339 SER HIS ASN VAL SER THR GLU VAL ARG ASP MSE SER VAL
SEQRES 19 D 339 VAL ALA ASN ASP ALA ALA ARG ALA ARG ASN GLU PHE GLY
SEQRES 20 D 339 TYR THR ARG MSE TRP SER ILE HIS PRO ALA GLN ILE GLU
SEQRES 21 D 339 ALA ILE VAL ALA ALA PHE ALA PRO ARG ASP GLU GLU ILE
SEQRES 22 D 339 THR THR ALA THR GLU ILE LEU LEU ALA ALA GLN SER ALA
SEQRES 23 D 339 GLN TRP GLY PRO THR ARG TYR HIS ASP THR LEU HIS ASP
SEQRES 24 D 339 ARG ALA SER TYR ARG TYR TYR TRP SER VAL LEU ARG ARG
SEQRES 25 D 339 ALA GLN ALA THR GLY ARG ALA VAL PRO GLN ASP ALA ALA
SEQRES 26 D 339 PRO LEU PHE THR LYS VAL GLY THR ASN VAL GLN ALA ALA
SEQRES 27 D 339 SER
SEQRES 1 E 339 GLY MSE ARG ALA LEU THR PRO ALA GLU VAL LEU PHE ASP
SEQRES 2 E 339 GLY GLU VAL PRO PRO ALA VAL LEU PRO ALA CYS ASP HIS
SEQRES 3 E 339 TYR ALA GLY SER GLU LYS LEU MSE LEU LYS SER LEU ALA
SEQRES 4 E 339 LEU GLN GLN GLN LEU GLY PRO VAL PHE ASP ILE THR LEU
SEQRES 5 E 339 ASP CYS GLU ASP GLY ALA GLN VAL GLY ARG GLU ALA GLN
SEQRES 6 E 339 HIS ALA GLU LEU VAL ALA SER LEU LEU GLY SER GLU HIS
SEQRES 7 E 339 ASP ARG PHE GLY ARG VAL GLY VAL ARG ILE HIS ASP PHE
SEQRES 8 E 339 ASP HIS ALA HIS TRP ARG ASP ASP VAL ARG LEU ILE LEU
SEQRES 9 E 339 ARG ALA ALA LYS ARG ALA PRO ALA TYR ILE THR LEU PRO
SEQRES 10 E 339 LYS ILE ARG HIS VAL HIS ASP ALA ALA GLU MSE VAL ALA
SEQRES 11 E 339 PHE ILE GLU ALA THR ARG ARG GLU LEU GLY ILE ALA GLN
SEQRES 12 E 339 PRO VAL PRO VAL GLN LEU LEU VAL GLU THR HIS GLY ALA
SEQRES 13 E 339 LEU THR ARG VAL PHE ASP LEU ALA ALA LEU PRO GLY VAL
SEQRES 14 E 339 GLU ALA LEU SER PHE GLY LEU MSE ASP PHE VAL SER ALA
SEQRES 15 E 339 HIS ASP GLY ALA ILE PRO ASP THR ALA MSE ARG SER PRO
SEQRES 16 E 339 GLY GLN PHE ASP HIS PRO LEU VAL ARG ARG ALA LYS LEU
SEQRES 17 E 339 GLU ILE SER ALA ALA CYS HIS ALA TYR GLY LYS VAL PRO
SEQRES 18 E 339 SER HIS ASN VAL SER THR GLU VAL ARG ASP MSE SER VAL
SEQRES 19 E 339 VAL ALA ASN ASP ALA ALA ARG ALA ARG ASN GLU PHE GLY
SEQRES 20 E 339 TYR THR ARG MSE TRP SER ILE HIS PRO ALA GLN ILE GLU
SEQRES 21 E 339 ALA ILE VAL ALA ALA PHE ALA PRO ARG ASP GLU GLU ILE
SEQRES 22 E 339 THR THR ALA THR GLU ILE LEU LEU ALA ALA GLN SER ALA
SEQRES 23 E 339 GLN TRP GLY PRO THR ARG TYR HIS ASP THR LEU HIS ASP
SEQRES 24 E 339 ARG ALA SER TYR ARG TYR TYR TRP SER VAL LEU ARG ARG
SEQRES 25 E 339 ALA GLN ALA THR GLY ARG ALA VAL PRO GLN ASP ALA ALA
SEQRES 26 E 339 PRO LEU PHE THR LYS VAL GLY THR ASN VAL GLN ALA ALA
SEQRES 27 E 339 SER
SEQRES 1 F 339 GLY MSE ARG ALA LEU THR PRO ALA GLU VAL LEU PHE ASP
SEQRES 2 F 339 GLY GLU VAL PRO PRO ALA VAL LEU PRO ALA CYS ASP HIS
SEQRES 3 F 339 TYR ALA GLY SER GLU LYS LEU MSE LEU LYS SER LEU ALA
SEQRES 4 F 339 LEU GLN GLN GLN LEU GLY PRO VAL PHE ASP ILE THR LEU
SEQRES 5 F 339 ASP CYS GLU ASP GLY ALA GLN VAL GLY ARG GLU ALA GLN
SEQRES 6 F 339 HIS ALA GLU LEU VAL ALA SER LEU LEU GLY SER GLU HIS
SEQRES 7 F 339 ASP ARG PHE GLY ARG VAL GLY VAL ARG ILE HIS ASP PHE
SEQRES 8 F 339 ASP HIS ALA HIS TRP ARG ASP ASP VAL ARG LEU ILE LEU
SEQRES 9 F 339 ARG ALA ALA LYS ARG ALA PRO ALA TYR ILE THR LEU PRO
SEQRES 10 F 339 LYS ILE ARG HIS VAL HIS ASP ALA ALA GLU MSE VAL ALA
SEQRES 11 F 339 PHE ILE GLU ALA THR ARG ARG GLU LEU GLY ILE ALA GLN
SEQRES 12 F 339 PRO VAL PRO VAL GLN LEU LEU VAL GLU THR HIS GLY ALA
SEQRES 13 F 339 LEU THR ARG VAL PHE ASP LEU ALA ALA LEU PRO GLY VAL
SEQRES 14 F 339 GLU ALA LEU SER PHE GLY LEU MSE ASP PHE VAL SER ALA
SEQRES 15 F 339 HIS ASP GLY ALA ILE PRO ASP THR ALA MSE ARG SER PRO
SEQRES 16 F 339 GLY GLN PHE ASP HIS PRO LEU VAL ARG ARG ALA LYS LEU
SEQRES 17 F 339 GLU ILE SER ALA ALA CYS HIS ALA TYR GLY LYS VAL PRO
SEQRES 18 F 339 SER HIS ASN VAL SER THR GLU VAL ARG ASP MSE SER VAL
SEQRES 19 F 339 VAL ALA ASN ASP ALA ALA ARG ALA ARG ASN GLU PHE GLY
SEQRES 20 F 339 TYR THR ARG MSE TRP SER ILE HIS PRO ALA GLN ILE GLU
SEQRES 21 F 339 ALA ILE VAL ALA ALA PHE ALA PRO ARG ASP GLU GLU ILE
SEQRES 22 F 339 THR THR ALA THR GLU ILE LEU LEU ALA ALA GLN SER ALA
SEQRES 23 F 339 GLN TRP GLY PRO THR ARG TYR HIS ASP THR LEU HIS ASP
SEQRES 24 F 339 ARG ALA SER TYR ARG TYR TYR TRP SER VAL LEU ARG ARG
SEQRES 25 F 339 ALA GLN ALA THR GLY ARG ALA VAL PRO GLN ASP ALA ALA
SEQRES 26 F 339 PRO LEU PHE THR LYS VAL GLY THR ASN VAL GLN ALA ALA
SEQRES 27 F 339 SER
MODRES 3R4I MSE A 33 MET SELENOMETHIONINE
MODRES 3R4I MSE A 127 MET SELENOMETHIONINE
MODRES 3R4I MSE A 176 MET SELENOMETHIONINE
MODRES 3R4I MSE A 191 MET SELENOMETHIONINE
MODRES 3R4I MSE A 231 MET SELENOMETHIONINE
MODRES 3R4I MSE A 250 MET SELENOMETHIONINE
MODRES 3R4I MSE B 33 MET SELENOMETHIONINE
MODRES 3R4I MSE B 127 MET SELENOMETHIONINE
MODRES 3R4I MSE B 176 MET SELENOMETHIONINE
MODRES 3R4I MSE B 191 MET SELENOMETHIONINE
MODRES 3R4I MSE B 231 MET SELENOMETHIONINE
MODRES 3R4I MSE B 250 MET SELENOMETHIONINE
MODRES 3R4I MSE C 33 MET SELENOMETHIONINE
MODRES 3R4I MSE C 127 MET SELENOMETHIONINE
MODRES 3R4I MSE C 176 MET SELENOMETHIONINE
MODRES 3R4I MSE C 191 MET SELENOMETHIONINE
MODRES 3R4I MSE C 231 MET SELENOMETHIONINE
MODRES 3R4I MSE C 250 MET SELENOMETHIONINE
MODRES 3R4I MSE D 33 MET SELENOMETHIONINE
MODRES 3R4I MSE D 127 MET SELENOMETHIONINE
MODRES 3R4I MSE D 176 MET SELENOMETHIONINE
MODRES 3R4I MSE D 191 MET SELENOMETHIONINE
MODRES 3R4I MSE D 231 MET SELENOMETHIONINE
MODRES 3R4I MSE D 250 MET SELENOMETHIONINE
MODRES 3R4I MSE E 33 MET SELENOMETHIONINE
MODRES 3R4I MSE E 127 MET SELENOMETHIONINE
MODRES 3R4I MSE E 176 MET SELENOMETHIONINE
MODRES 3R4I MSE E 191 MET SELENOMETHIONINE
MODRES 3R4I MSE E 231 MET SELENOMETHIONINE
MODRES 3R4I MSE E 250 MET SELENOMETHIONINE
MODRES 3R4I MSE F 33 MET SELENOMETHIONINE
MODRES 3R4I MSE F 127 MET SELENOMETHIONINE
MODRES 3R4I MSE F 176 MET SELENOMETHIONINE
MODRES 3R4I MSE F 191 MET SELENOMETHIONINE
MODRES 3R4I MSE F 231 MET SELENOMETHIONINE
MODRES 3R4I MSE F 250 MET SELENOMETHIONINE
HET MSE A 33 8
HET MSE A 127 8
HET MSE A 176 8
HET MSE A 191 8
HET MSE A 231 8
HET MSE A 250 8
HET MSE B 33 8
HET MSE B 127 8
HET MSE B 176 8
HET MSE B 191 8
HET MSE B 231 8
HET MSE B 250 8
HET MSE C 33 8
HET MSE C 127 8
HET MSE C 176 8
HET MSE C 191 8
HET MSE C 231 8
HET MSE C 250 8
HET MSE D 33 8
HET MSE D 127 8
HET MSE D 176 8
HET MSE D 191 8
HET MSE D 231 8
HET MSE D 250 8
HET MSE E 33 8
HET MSE E 127 8
HET MSE E 176 8
HET MSE E 191 8
HET MSE E 231 8
HET MSE E 250 8
HET MSE F 33 8
HET MSE F 127 8
HET MSE F 176 8
HET MSE F 191 8
HET MSE F 231 8
HET MSE F 250 8
HET CA A 341 1
HET CA A 346 1
HET CA B 339 1
HET CA B 340 1
HET CL B 354 1
HET CA C 343 1
HET CA C 344 1
HET CL C 353 1
HET ACT C 357 4
HET CA D 342 1
HET CA D 345 1
HET CA D 350 1
HET CL D 352 1
HET ACT D 358 4
HET CA E 347 1
HET CA E 348 1
HET CL E 355 1
HET CA F 349 1
HET CA F 351 1
HET CL F 356 1
HETNAM MSE SELENOMETHIONINE
HETNAM CA CALCIUM ION
HETNAM CL CHLORIDE ION
HETNAM ACT ACETATE ION
FORMUL 1 MSE 36(C5 H11 N O2 SE)
FORMUL 7 CA 13(CA 2+)
FORMUL 11 CL 5(CL 1-)
FORMUL 15 ACT 2(C2 H3 O2 1-)
FORMUL 27 HOH *286(H2 O)
HELIX 1 1 THR A 5 LEU A 10 1 6
HELIX 2 2 SER A 29 GLY A 44 1 16
HELIX 3 3 ARG A 61 LEU A 73 1 13
HELIX 4 4 HIS A 94 ALA A 106 1 13
HELIX 5 5 HIS A 120 LEU A 138 1 19
HELIX 6 6 THR A 152 ARG A 158 1 7
HELIX 7 7 ARG A 158 ALA A 164 1 7
HELIX 8 8 GLY A 174 ALA A 181 1 8
HELIX 9 9 PRO A 187 ARG A 192 5 6
HELIX 10 10 PRO A 194 HIS A 199 1 6
HELIX 11 11 HIS A 199 TYR A 216 1 18
HELIX 12 12 ASP A 230 GLU A 244 1 15
HELIX 13 13 HIS A 254 PHE A 265 1 12
HELIX 14 14 GLU A 270 ALA A 285 1 16
HELIX 15 15 ASP A 298 THR A 315 1 18
HELIX 16 16 PRO A 320 PHE A 327 5 8
HELIX 17 17 THR B 5 LEU B 10 1 6
HELIX 18 18 SER B 29 GLY B 44 1 16
HELIX 19 19 ARG B 61 LEU B 73 1 13
HELIX 20 20 HIS B 94 ALA B 106 1 13
HELIX 21 21 HIS B 120 LEU B 138 1 19
HELIX 22 22 THR B 152 ARG B 158 1 7
HELIX 23 23 ARG B 158 ALA B 164 1 7
HELIX 24 24 GLY B 174 ALA B 181 1 8
HELIX 25 25 PRO B 187 ARG B 192 5 6
HELIX 26 26 PRO B 194 HIS B 199 1 6
HELIX 27 27 HIS B 199 TYR B 216 1 18
HELIX 28 28 ASP B 230 GLU B 244 1 15
HELIX 29 29 HIS B 254 PHE B 265 1 12
HELIX 30 30 GLU B 270 ALA B 285 1 16
HELIX 31 31 ASP B 298 THR B 315 1 18
HELIX 32 32 PRO B 320 PHE B 327 5 8
HELIX 33 33 THR C 5 LEU C 10 1 6
HELIX 34 34 SER C 29 GLY C 44 1 16
HELIX 35 35 ARG C 61 LEU C 73 1 13
HELIX 36 36 HIS C 94 ALA C 106 1 13
HELIX 37 37 HIS C 120 LEU C 138 1 19
HELIX 38 38 THR C 152 ARG C 158 1 7
HELIX 39 39 ARG C 158 ALA C 164 1 7
HELIX 40 40 GLY C 174 ALA C 181 1 8
HELIX 41 41 PRO C 187 ARG C 192 5 6
HELIX 42 42 PRO C 194 HIS C 199 1 6
HELIX 43 43 HIS C 199 TYR C 216 1 18
HELIX 44 44 ASP C 230 GLU C 244 1 15
HELIX 45 45 HIS C 254 PHE C 265 1 12
HELIX 46 46 GLU C 270 ALA C 285 1 16
HELIX 47 47 ASP C 298 THR C 315 1 18
HELIX 48 48 PRO C 320 PHE C 327 5 8
HELIX 49 49 THR D 5 LEU D 10 1 6
HELIX 50 50 SER D 29 GLY D 44 1 16
HELIX 51 51 ARG D 61 LEU D 73 1 13
HELIX 52 52 HIS D 94 ALA D 106 1 13
HELIX 53 53 HIS D 120 LEU D 138 1 19
HELIX 54 54 THR D 152 ARG D 158 1 7
HELIX 55 55 ARG D 158 ALA D 164 1 7
HELIX 56 56 GLY D 174 ALA D 181 1 8
HELIX 57 57 PRO D 187 ARG D 192 5 6
HELIX 58 58 PRO D 194 HIS D 199 1 6
HELIX 59 59 HIS D 199 TYR D 216 1 18
HELIX 60 60 ASP D 230 GLU D 244 1 15
HELIX 61 61 HIS D 254 PHE D 265 1 12
HELIX 62 62 GLU D 270 ALA D 285 1 16
HELIX 63 63 ASP D 298 THR D 315 1 18
HELIX 64 64 PRO D 320 PHE D 327 5 8
HELIX 65 65 THR E 5 LEU E 10 1 6
HELIX 66 66 SER E 29 GLY E 44 1 16
HELIX 67 67 ARG E 61 LEU E 73 1 13
HELIX 68 68 HIS E 94 ALA E 106 1 13
HELIX 69 69 HIS E 120 LEU E 138 1 19
HELIX 70 70 THR E 152 ARG E 158 1 7
HELIX 71 71 ARG E 158 ALA E 164 1 7
HELIX 72 72 GLY E 174 ALA E 181 1 8
HELIX 73 73 PRO E 187 ARG E 192 5 6
HELIX 74 74 PRO E 194 HIS E 199 1 6
HELIX 75 75 HIS E 199 TYR E 216 1 18
HELIX 76 76 ASP E 230 GLU E 244 1 15
HELIX 77 77 HIS E 254 PHE E 265 1 12
HELIX 78 78 GLU E 270 ALA E 285 1 16
HELIX 79 79 ASP E 298 THR E 315 1 18
HELIX 80 80 PRO E 320 PHE E 327 5 8
HELIX 81 81 THR F 5 LEU F 10 1 6
HELIX 82 82 SER F 29 GLY F 44 1 16
HELIX 83 83 ARG F 61 LEU F 73 1 13
HELIX 84 84 HIS F 94 ALA F 106 1 13
HELIX 85 85 HIS F 120 LEU F 138 1 19
HELIX 86 86 THR F 152 ARG F 158 1 7
HELIX 87 87 ARG F 158 ALA F 164 1 7
HELIX 88 88 GLY F 174 ALA F 181 1 8
HELIX 89 89 PRO F 187 ARG F 192 5 6
HELIX 90 90 PRO F 194 HIS F 199 1 6
HELIX 91 91 HIS F 199 TYR F 216 1 18
HELIX 92 92 ASP F 230 GLU F 244 1 15
HELIX 93 93 HIS F 254 PHE F 265 1 12
HELIX 94 94 GLU F 270 ALA F 285 1 16
HELIX 95 95 ASP F 298 THR F 315 1 18
HELIX 96 96 PRO F 320 PHE F 327 5 8
SHEET 1 A 9 CYS A 23 ALA A 27 0
SHEET 2 A 9 PHE A 47 ASP A 52 1 O ASP A 48 N CYS A 23
SHEET 3 A 9 VAL A 83 ARG A 86 1 O GLY A 84 N ILE A 49
SHEET 4 A 9 ILE A 113 LEU A 115 1 O THR A 114 N VAL A 85
SHEET 5 A 9 VAL A 146 VAL A 150 1 O GLN A 147 N LEU A 115
SHEET 6 A 9 VAL A 168 PHE A 173 1 O SER A 172 N VAL A 150
SHEET 7 A 9 VAL A 219 HIS A 222 1 O SER A 221 N LEU A 171
SHEET 8 A 9 ARG A 249 SER A 252 1 O ARG A 249 N HIS A 222
SHEET 9 A 9 CYS A 23 ALA A 27 1 N TYR A 26 O SER A 252
SHEET 1 B 2 THR A 290 TYR A 292 0
SHEET 2 B 2 THR A 295 HIS A 297 -1 O HIS A 297 N THR A 290
SHEET 1 C 9 CYS B 23 ALA B 27 0
SHEET 2 C 9 PHE B 47 ASP B 52 1 O ASP B 48 N CYS B 23
SHEET 3 C 9 VAL B 83 ARG B 86 1 O GLY B 84 N ILE B 49
SHEET 4 C 9 ILE B 113 LEU B 115 1 O THR B 114 N VAL B 85
SHEET 5 C 9 VAL B 146 VAL B 150 1 O GLN B 147 N LEU B 115
SHEET 6 C 9 VAL B 168 PHE B 173 1 O SER B 172 N VAL B 150
SHEET 7 C 9 VAL B 219 HIS B 222 1 O SER B 221 N LEU B 171
SHEET 8 C 9 ARG B 249 SER B 252 1 O ARG B 249 N HIS B 222
SHEET 9 C 9 CYS B 23 ALA B 27 1 N TYR B 26 O SER B 252
SHEET 1 D 2 THR B 290 TYR B 292 0
SHEET 2 D 2 THR B 295 HIS B 297 -1 O HIS B 297 N THR B 290
SHEET 1 E 9 CYS C 23 ALA C 27 0
SHEET 2 E 9 PHE C 47 ASP C 52 1 O ASP C 48 N CYS C 23
SHEET 3 E 9 VAL C 83 ARG C 86 1 O GLY C 84 N ILE C 49
SHEET 4 E 9 ILE C 113 LEU C 115 1 O THR C 114 N VAL C 85
SHEET 5 E 9 VAL C 146 VAL C 150 1 O GLN C 147 N LEU C 115
SHEET 6 E 9 VAL C 168 PHE C 173 1 O SER C 172 N VAL C 150
SHEET 7 E 9 VAL C 219 HIS C 222 1 O SER C 221 N LEU C 171
SHEET 8 E 9 ARG C 249 SER C 252 1 O ARG C 249 N HIS C 222
SHEET 9 E 9 CYS C 23 ALA C 27 1 N TYR C 26 O SER C 252
SHEET 1 F 2 THR C 290 TYR C 292 0
SHEET 2 F 2 THR C 295 HIS C 297 -1 O HIS C 297 N THR C 290
SHEET 1 G 9 CYS D 23 ALA D 27 0
SHEET 2 G 9 PHE D 47 ASP D 52 1 O ASP D 48 N CYS D 23
SHEET 3 G 9 VAL D 83 ARG D 86 1 O GLY D 84 N ILE D 49
SHEET 4 G 9 ILE D 113 LEU D 115 1 O THR D 114 N VAL D 85
SHEET 5 G 9 VAL D 146 VAL D 150 1 O GLN D 147 N LEU D 115
SHEET 6 G 9 VAL D 168 PHE D 173 1 O SER D 172 N VAL D 150
SHEET 7 G 9 VAL D 219 HIS D 222 1 O SER D 221 N LEU D 171
SHEET 8 G 9 ARG D 249 SER D 252 1 O ARG D 249 N HIS D 222
SHEET 9 G 9 CYS D 23 ALA D 27 1 N TYR D 26 O SER D 252
SHEET 1 H 2 THR D 290 TYR D 292 0
SHEET 2 H 2 THR D 295 HIS D 297 -1 O HIS D 297 N THR D 290
SHEET 1 I 9 CYS E 23 ALA E 27 0
SHEET 2 I 9 PHE E 47 ASP E 52 1 O ASP E 48 N CYS E 23
SHEET 3 I 9 VAL E 83 ARG E 86 1 O GLY E 84 N ILE E 49
SHEET 4 I 9 ILE E 113 LEU E 115 1 O THR E 114 N VAL E 85
SHEET 5 I 9 VAL E 146 VAL E 150 1 O GLN E 147 N LEU E 115
SHEET 6 I 9 VAL E 168 PHE E 173 1 O SER E 172 N VAL E 150
SHEET 7 I 9 VAL E 219 HIS E 222 1 O SER E 221 N LEU E 171
SHEET 8 I 9 ARG E 249 SER E 252 1 O ARG E 249 N HIS E 222
SHEET 9 I 9 CYS E 23 ALA E 27 1 N TYR E 26 O SER E 252
SHEET 1 J 2 THR E 290 TYR E 292 0
SHEET 2 J 2 THR E 295 HIS E 297 -1 O HIS E 297 N THR E 290
SHEET 1 K 9 CYS F 23 ALA F 27 0
SHEET 2 K 9 PHE F 47 ASP F 52 1 O ASP F 48 N CYS F 23
SHEET 3 K 9 VAL F 83 ARG F 86 1 O GLY F 84 N ILE F 49
SHEET 4 K 9 ILE F 113 LEU F 115 1 O THR F 114 N VAL F 85
SHEET 5 K 9 VAL F 146 VAL F 150 1 O GLN F 147 N LEU F 115
SHEET 6 K 9 VAL F 168 PHE F 173 1 O SER F 172 N VAL F 150
SHEET 7 K 9 VAL F 219 HIS F 222 1 O SER F 221 N LEU F 171
SHEET 8 K 9 ARG F 249 SER F 252 1 O ARG F 249 N HIS F 222
SHEET 9 K 9 CYS F 23 ALA F 27 1 N TYR F 26 O SER F 252
SHEET 1 L 2 THR F 290 TYR F 292 0
SHEET 2 L 2 THR F 295 HIS F 297 -1 O HIS F 297 N THR F 290
LINK C LEU A 32 N MSE A 33 1555 1555 1.33
LINK C MSE A 33 N LEU A 34 1555 1555 1.33
LINK C GLU A 126 N MSE A 127 1555 1555 1.33
LINK C MSE A 127 N VAL A 128 1555 1555 1.32
LINK C LEU A 175 N MSE A 176 1555 1555 1.33
LINK C MSE A 176 N ASP A 177 1555 1555 1.33
LINK C ALA A 190 N MSE A 191 1555 1555 1.33
LINK C MSE A 191 N ARG A 192 1555 1555 1.33
LINK C ASP A 230 N MSE A 231 1555 1555 1.33
LINK C MSE A 231 N SER A 232 1555 1555 1.34
LINK C ARG A 249 N MSE A 250 1555 1555 1.33
LINK C MSE A 250 N TRP A 251 1555 1555 1.33
LINK C LEU B 32 N MSE B 33 1555 1555 1.33
LINK C MSE B 33 N LEU B 34 1555 1555 1.33
LINK C GLU B 126 N MSE B 127 1555 1555 1.33
LINK C MSE B 127 N VAL B 128 1555 1555 1.33
LINK C LEU B 175 N MSE B 176 1555 1555 1.33
LINK C MSE B 176 N ASP B 177 1555 1555 1.33
LINK C ALA B 190 N MSE B 191 1555 1555 1.33
LINK C MSE B 191 N ARG B 192 1555 1555 1.34
LINK C ASP B 230 N MSE B 231 1555 1555 1.33
LINK C MSE B 231 N SER B 232 1555 1555 1.33
LINK C ARG B 249 N MSE B 250 1555 1555 1.33
LINK C MSE B 250 N TRP B 251 1555 1555 1.33
LINK C LEU C 32 N MSE C 33 1555 1555 1.33
LINK C MSE C 33 N LEU C 34 1555 1555 1.33
LINK C GLU C 126 N MSE C 127 1555 1555 1.33
LINK C MSE C 127 N VAL C 128 1555 1555 1.33
LINK C LEU C 175 N MSE C 176 1555 1555 1.33
LINK C MSE C 176 N ASP C 177 1555 1555 1.33
LINK C ALA C 190 N MSE C 191 1555 1555 1.33
LINK C MSE C 191 N ARG C 192 1555 1555 1.33
LINK C ASP C 230 N MSE C 231 1555 1555 1.33
LINK C MSE C 231 N SER C 232 1555 1555 1.33
LINK C ARG C 249 N MSE C 250 1555 1555 1.32
LINK C MSE C 250 N TRP C 251 1555 1555 1.33
LINK C LEU D 32 N MSE D 33 1555 1555 1.33
LINK C MSE D 33 N LEU D 34 1555 1555 1.33
LINK C GLU D 126 N MSE D 127 1555 1555 1.33
LINK C MSE D 127 N VAL D 128 1555 1555 1.33
LINK C LEU D 175 N MSE D 176 1555 1555 1.33
LINK C MSE D 176 N ASP D 177 1555 1555 1.33
LINK C ALA D 190 N MSE D 191 1555 1555 1.33
LINK C MSE D 191 N ARG D 192 1555 1555 1.33
LINK C ASP D 230 N MSE D 231 1555 1555 1.33
LINK C MSE D 231 N SER D 232 1555 1555 1.33
LINK C ARG D 249 N MSE D 250 1555 1555 1.33
LINK C MSE D 250 N TRP D 251 1555 1555 1.33
LINK C LEU E 32 N MSE E 33 1555 1555 1.33
LINK C MSE E 33 N LEU E 34 1555 1555 1.33
LINK C GLU E 126 N MSE E 127 1555 1555 1.33
LINK C MSE E 127 N VAL E 128 1555 1555 1.33
LINK C LEU E 175 N MSE E 176 1555 1555 1.33
LINK C MSE E 176 N ASP E 177 1555 1555 1.34
LINK C ALA E 190 N MSE E 191 1555 1555 1.33
LINK C MSE E 191 N ARG E 192 1555 1555 1.33
LINK C ASP E 230 N MSE E 231 1555 1555 1.33
LINK C MSE E 231 N SER E 232 1555 1555 1.33
LINK C ARG E 249 N MSE E 250 1555 1555 1.33
LINK C MSE E 250 N TRP E 251 1555 1555 1.33
LINK C LEU F 32 N MSE F 33 1555 1555 1.33
LINK C MSE F 33 N LEU F 34 1555 1555 1.33
LINK C GLU F 126 N MSE F 127 1555 1555 1.33
LINK C MSE F 127 N VAL F 128 1555 1555 1.33
LINK C LEU F 175 N MSE F 176 1555 1555 1.33
LINK C MSE F 176 N ASP F 177 1555 1555 1.34
LINK C ALA F 190 N MSE F 191 1555 1555 1.33
LINK C MSE F 191 N ARG F 192 1555 1555 1.33
LINK C ASP F 230 N MSE F 231 1555 1555 1.33
LINK C MSE F 231 N SER F 232 1555 1555 1.33
LINK C ARG F 249 N MSE F 250 1555 1555 1.32
LINK C MSE F 250 N TRP F 251 1555 1555 1.34
LINK OE1 GLU A 151 CA CA A 341 1555 1555 2.50
LINK OD2 ASP A 177 CA CA A 341 1555 1555 2.61
LINK OD1 ASP A 230 CA CA A 346 1555 1555 2.49
LINK OD2 ASP A 230 CA CA A 346 1555 1555 2.71
LINK CA CA A 341 O HOH A 372 1555 1555 2.79
LINK CA CA A 341 O HOH A 381 1555 1555 2.72
LINK CA CA A 341 O HOH A 427 1555 1555 2.64
LINK CA CA A 346 O HOH A 390 1555 1555 2.52
LINK CA CA A 346 O HOH A 391 1555 1555 2.58
LINK CA CA A 346 O HOH A 550 1555 1555 2.88
LINK CA CA A 346 O HOH B 408 1555 1555 2.62
LINK O HOH A 385 CA CA B 340 1555 1555 2.43
LINK OE1 GLU B 151 CA CA B 339 1555 1555 2.42
LINK OD2 ASP B 177 CA CA B 339 1555 1555 2.46
LINK OD1 ASP B 230 CA CA B 340 1555 1555 2.60
LINK OD2 ASP B 230 CA CA B 340 1555 1555 2.69
LINK CA CA B 339 O HOH B 395 1555 1555 2.48
LINK CA CA B 339 O HOH B 397 1555 1555 2.60
LINK CA CA B 339 O HOH B 432 1555 1555 2.62
LINK OE1 GLU C 151 CA CA C 343 1555 1555 2.64
LINK OD2 ASP C 177 CA CA C 343 1555 1555 2.81
LINK OD1 ASP C 230 CA CA C 344 1555 1555 2.61
LINK OD2 ASP C 230 CA CA C 344 1555 1555 2.83
LINK CA CA C 343 O HOH C 407 1555 1555 2.67
LINK CA CA C 343 O HOH C 442 1555 1555 2.54
LINK CA CA C 344 O HOH C 402 1555 1555 2.67
LINK CA CA C 344 O HOH C 426 1555 1555 2.54
LINK OE1 GLU D 126 CA CA D 350 1555 1555 3.14
LINK OE1 GLU D 151 CA CA D 342 1555 1555 2.51
LINK OD2 ASP D 177 CA CA D 342 1555 1555 2.46
LINK OD1 ASP D 230 CA CA D 345 1555 1555 2.63
LINK OD2 ASP D 230 CA CA D 345 1555 1555 3.03
LINK CA CA D 342 O HOH D 364 1555 1555 2.52
LINK CA CA D 342 O HOH D 430 1555 1555 2.51
LINK CA CA D 345 O HOH D 549 1555 1555 2.51
LINK OE1 GLU E 151 CA CA E 348 1555 1555 2.57
LINK OD2 ASP E 177 CA CA E 348 1555 1555 2.55
LINK OD1 ASP E 230 CA CA E 347 1555 1555 2.75
LINK OD2 ASP E 230 CA CA E 347 1555 1555 3.04
LINK CA CA E 348 O HOH E 463 1555 1555 2.56
LINK OE1 GLU F 151 CA CA F 349 1555 1555 2.75
LINK OD2 ASP F 177 CA CA F 349 1555 1555 2.67
LINK OD1 ASP F 230 CA CA F 351 1555 1555 2.56
LINK OD2 ASP F 230 CA CA F 351 1555 1555 2.88
CISPEP 1 SER A 193 PRO A 194 0 4.53
CISPEP 2 SER B 193 PRO B 194 0 5.04
CISPEP 3 SER C 193 PRO C 194 0 4.77
CISPEP 4 SER D 193 PRO D 194 0 4.24
CISPEP 5 SER E 193 PRO E 194 0 3.91
CISPEP 6 SER F 193 PRO F 194 0 5.78
SITE 1 AC1 5 GLU A 151 ASP A 177 HOH A 372 HOH A 381
SITE 2 AC1 5 HOH A 427
SITE 1 AC2 5 ASP A 230 HOH A 390 HOH A 391 HOH A 550
SITE 2 AC2 5 HOH B 408
SITE 1 AC3 6 GLU B 151 ASP B 177 CL B 354 HOH B 395
SITE 2 AC3 6 HOH B 397 HOH B 432
SITE 1 AC4 3 HOH A 385 HOH A 561 ASP B 230
SITE 1 AC5 6 GLY B 174 LEU B 175 MSE B 176 ASP B 177
SITE 2 AC5 6 CA B 339 HOH B 483
SITE 1 AC6 6 ARG C 86 GLU C 151 ASP C 177 CL C 353
SITE 2 AC6 6 HOH C 407 HOH C 442
SITE 1 AC7 6 ASP C 230 HOH C 402 HOH C 426 HOH D 388
SITE 2 AC7 6 HOH D 409 HOH D 439
SITE 1 AC8 6 GLY C 174 LEU C 175 MSE C 176 ASP C 177
SITE 2 AC8 6 ALA C 300 CA C 343
SITE 1 AC9 5 ARG C 86 MSE C 176 TRP C 251 ILE C 253
SITE 2 AC9 5 ASP C 298
SITE 1 BC1 5 GLU D 151 ASP D 177 CL D 352 HOH D 364
SITE 2 BC1 5 HOH D 430
SITE 1 BC2 5 HOH C 382 HOH C 404 HOH C 446 ASP D 230
SITE 2 BC2 5 HOH D 549
SITE 1 BC3 3 ASP C 91 HIS C 120 GLU D 126
SITE 1 BC4 5 GLY D 174 MSE D 176 ASP D 177 ALA D 300
SITE 2 BC4 5 CA D 342
SITE 1 BC5 7 ARG D 86 MSE D 176 TRP D 251 ASP D 298
SITE 2 BC5 7 HOH D 364 HOH D 430 HOH D 433
SITE 1 BC6 1 ASP E 230
SITE 1 BC7 4 GLU E 151 ASP E 177 CL E 355 HOH E 463
SITE 1 BC8 5 GLY E 174 LEU E 175 MSE E 176 ASP E 177
SITE 2 BC8 5 CA E 348
SITE 1 BC9 4 ARG F 86 GLU F 151 ASP F 177 CL F 356
SITE 1 CC1 2 HOH E 558 ASP F 230
SITE 1 CC2 5 GLY F 174 MSE F 176 ASP F 177 ALA F 300
SITE 2 CC2 5 CA F 349
CRYST1 148.468 148.468 79.570 90.00 90.00 120.00 P 3 18
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 0.006735 0.003889 0.000000 0.00000
SCALE2 0.000000 0.007777 0.000000 0.00000
SCALE3 0.000000 0.000000 0.012568 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
