HEADER SOLUTE-BINDING PROTEIN 26-SEP-13 4MX8
TITLE CRYSTAL STRUCTURE OF TROA-LIKE PERIPLASMIC BINDING PROTEIN
TITLE 2 PERIPLA_BP_2 FROM XYLANIMONAS CELLULOSILYTICA
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PERIPLASMIC BINDING PROTEIN;
COMPND 3 CHAIN: A, B, C, D, E, F;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: XYLANIMONAS CELLULOSILYTICA;
SOURCE 3 ORGANISM_TAXID: 446471;
SOURCE 4 STRAIN: DSM 15894;
SOURCE 5 GENE: XCEL_1393;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 511693;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21 MAGIC;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PMCSG68
KEYWDS STRUCTURAL GENOMICS, PSI-BIOLOGY, MIDWEST CENTER FOR STRUCTURAL
KEYWDS 2 GENOMICS, MCSG, ALPHA-BETA-FOLD, SOLUTE-BINDING PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR Y.KIM,R.WU,M.ENDRES,A.JOACHIMIAK,MIDWEST CENTER FOR STRUCTURAL
AUTHOR 2 GENOMICS (MCSG)
REVDAT 1 11-DEC-13 4MX8 0
JRNL AUTH Y.KIM,R.WU,M.ENDRES,A.JOACHIMIAK,
JRNL AUTH 2 MIDWEST CENTER FOR STRUCTURAL GENOMICS (MCSG)
JRNL TITL CRYSTAL STRUCTURE OF TROA-LIKE PERIPLASMIC BINDING PROTEIN
JRNL TITL 2 PERIPLA_BP_2 FROM XYLANIMONAS CELLULOSILYTICA
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.91 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE: DEV_1367)
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 : MLHL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.91
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 49.37
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 96.6
REMARK 3 NUMBER OF REFLECTIONS : 80493
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.161
REMARK 3 R VALUE (WORKING SET) : 0.159
REMARK 3 FREE R VALUE : 0.196
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.990
REMARK 3 FREE R VALUE TEST SET COUNT : 4013
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS).
REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE
REMARK 3 1 49.3774 - 8.9271 0.97 2743 130 0.1722 0.1824
REMARK 3 2 8.9271 - 7.0924 1.00 2761 163 0.1424 0.1741
REMARK 3 3 7.0924 - 6.1978 1.00 2739 151 0.1553 0.1990
REMARK 3 4 6.1978 - 5.6320 1.00 2737 156 0.1460 0.2022
REMARK 3 5 5.6320 - 5.2288 1.00 2736 141 0.1260 0.1381
REMARK 3 6 5.2288 - 4.9208 1.00 2736 150 0.1167 0.1453
REMARK 3 7 4.9208 - 4.6746 1.00 2739 134 0.1028 0.1307
REMARK 3 8 4.6746 - 4.4712 1.00 2721 150 0.1053 0.1507
REMARK 3 9 4.4712 - 4.2992 1.00 2700 151 0.1074 0.1487
REMARK 3 10 4.2992 - 4.1509 0.99 2734 126 0.1165 0.1745
REMARK 3 11 4.1509 - 4.0212 0.99 2683 154 0.1164 0.1349
REMARK 3 12 4.0212 - 3.9063 0.99 2704 138 0.1288 0.1513
REMARK 3 13 3.9063 - 3.8035 0.98 2656 162 0.1345 0.1922
REMARK 3 14 3.8035 - 3.7108 0.97 2674 145 0.1405 0.1896
REMARK 3 15 3.7108 - 3.6264 0.98 2633 155 0.1562 0.1973
REMARK 3 16 3.6264 - 3.5493 0.98 2673 130 0.1641 0.2162
REMARK 3 17 3.5493 - 3.4783 0.97 2651 138 0.1685 0.2285
REMARK 3 18 3.4783 - 3.4127 0.97 2598 131 0.1899 0.2452
REMARK 3 19 3.4127 - 3.3517 0.97 2676 141 0.1883 0.2334
REMARK 3 20 3.3517 - 3.2949 0.97 2645 147 0.2059 0.2374
REMARK 3 21 3.2949 - 3.2418 0.97 2620 123 0.2167 0.2585
REMARK 3 22 3.2418 - 3.1919 0.97 2671 143 0.2192 0.2970
REMARK 3 23 3.1919 - 3.1450 0.97 2571 133 0.2379 0.2691
REMARK 3 24 3.1450 - 3.1007 0.97 2715 123 0.2367 0.3082
REMARK 3 25 3.1007 - 3.0588 0.96 2556 107 0.2496 0.2821
REMARK 3 26 3.0588 - 3.0191 0.95 2609 143 0.2610 0.3216
REMARK 3 27 3.0191 - 2.9813 0.93 2495 143 0.2887 0.3678
REMARK 3 28 2.9813 - 2.9454 0.90 2474 114 0.2885 0.3489
REMARK 3 29 2.9454 - 2.9112 0.68 1830 91 0.3174 0.3261
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 : NULL
REMARK 3 B_SOL : NULL
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.320
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 21.060
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 54.12
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 59.40
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
REMARK 3
REMARK 3 TWINNING INFORMATION.
REMARK 3 FRACTION: NULL
REMARK 3 OPERATOR: NULL
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : 0.008 13823
REMARK 3 ANGLE : 1.137 18933
REMARK 3 CHIRALITY : 0.075 2224
REMARK 3 PLANARITY : 0.004 2520
REMARK 3 DIHEDRAL : 16.124 4840
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 13
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: chain 'A' and (resid 12 through 152 )
REMARK 3 ORIGIN FOR THE GROUP (A): -17.2707 38.6912 185.3635
REMARK 3 T TENSOR
REMARK 3 T11: 0.2463 T22: 0.2236
REMARK 3 T33: 0.2709 T12: -0.0074
REMARK 3 T13: -0.0622 T23: -0.0640
REMARK 3 L TENSOR
REMARK 3 L11: 3.4693 L22: 3.7474
REMARK 3 L33: 2.4127 L12: 0.6582
REMARK 3 L13: -0.6659 L23: -0.3317
REMARK 3 S TENSOR
REMARK 3 S11: 0.0093 S12: -0.3376 S13: 0.0152
REMARK 3 S21: 0.3392 S22: 0.0048 S23: -0.2044
REMARK 3 S31: -0.1717 S32: 0.1256 S33: -0.0121
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: chain 'A' and (resid 153 through 313 )
REMARK 3 ORIGIN FOR THE GROUP (A): -11.6484 32.2199 160.2270
REMARK 3 T TENSOR
REMARK 3 T11: 0.3466 T22: 0.2070
REMARK 3 T33: 0.5115 T12: -0.0376
REMARK 3 T13: 0.0648 T23: -0.0701
REMARK 3 L TENSOR
REMARK 3 L11: 1.0567 L22: 3.4876
REMARK 3 L33: 4.2420 L12: 0.6560
REMARK 3 L13: -0.0000 L23: 0.4288
REMARK 3 S TENSOR
REMARK 3 S11: -0.1365 S12: 0.0855 S13: -0.0410
REMARK 3 S21: -0.4541 S22: -0.0452 S23: -0.1114
REMARK 3 S31: 0.5169 S32: -0.3014 S33: 0.1497
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: chain 'B' and (resid 12 through 152 )
REMARK 3 ORIGIN FOR THE GROUP (A): -32.8799 10.2562 185.2278
REMARK 3 T TENSOR
REMARK 3 T11: 0.2376 T22: 0.2150
REMARK 3 T33: 0.2773 T12: 0.0044
REMARK 3 T13: -0.0038 T23: 0.0781
REMARK 3 L TENSOR
REMARK 3 L11: 3.0876 L22: 4.0531
REMARK 3 L33: 2.7502 L12: -0.5725
REMARK 3 L13: -0.0966 L23: 0.8155
REMARK 3 S TENSOR
REMARK 3 S11: -0.0258 S12: -0.3126 S13: -0.1739
REMARK 3 S21: 0.4087 S22: 0.0706 S23: -0.0023
REMARK 3 S31: 0.1660 S32: 0.0407 S33: -0.0391
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: chain 'B' and (resid 153 through 313 )
REMARK 3 ORIGIN FOR THE GROUP (A): -41.3458 8.6600 160.0255
REMARK 3 T TENSOR
REMARK 3 T11: 0.2474 T22: 0.2879
REMARK 3 T33: 0.4854 T12: 0.0727
REMARK 3 T13: -0.0683 T23: -0.0151
REMARK 3 L TENSOR
REMARK 3 L11: 2.0915 L22: 2.3522
REMARK 3 L33: 4.6308 L12: -1.3677
REMARK 3 L13: 0.5479 L23: -0.3090
REMARK 3 S TENSOR
REMARK 3 S11: 0.1147 S12: 0.2773 S13: -0.1493
REMARK 3 S21: -0.2365 S22: -0.2901 S23: 0.1505
REMARK 3 S31: -0.5405 S32: -0.2427 S33: 0.1336
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: chain 'C' and (resid 13 through 134 )
REMARK 3 ORIGIN FOR THE GROUP (A): -26.1160 13.3022 96.6522
REMARK 3 T TENSOR
REMARK 3 T11: 0.7489 T22: 0.6321
REMARK 3 T33: 0.2807 T12: 0.0468
REMARK 3 T13: -0.0148 T23: -0.1115
REMARK 3 L TENSOR
REMARK 3 L11: 3.4622 L22: 2.3099
REMARK 3 L33: 1.1854 L12: 0.0437
REMARK 3 L13: 0.4157 L23: -0.8340
REMARK 3 S TENSOR
REMARK 3 S11: 0.2158 S12: 0.4010 S13: -0.2614
REMARK 3 S21: -0.4165 S22: -0.0604 S23: -0.0580
REMARK 3 S31: 0.3017 S32: 0.1469 S33: -0.1448
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: chain 'C' and (resid 135 through 313 )
REMARK 3 ORIGIN FOR THE GROUP (A): -19.1977 12.6773 120.8402
REMARK 3 T TENSOR
REMARK 3 T11: 0.8271 T22: 0.4390
REMARK 3 T33: 0.3961 T12: -0.1264
REMARK 3 T13: -0.1265 T23: -0.0161
REMARK 3 L TENSOR
REMARK 3 L11: 2.3792 L22: 3.1427
REMARK 3 L33: 6.1935 L12: 0.7490
REMARK 3 L13: 0.7776 L23: 1.0639
REMARK 3 S TENSOR
REMARK 3 S11: 0.3913 S12: -0.1110 S13: -0.1127
REMARK 3 S21: 0.4851 S22: -0.4436 S23: -0.0072
REMARK 3 S31: -0.2374 S32: -0.1234 S33: 0.0446
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: chain 'D' and (resid 12 through 152 )
REMARK 3 ORIGIN FOR THE GROUP (A): -49.6151 37.9596 185.3745
REMARK 3 T TENSOR
REMARK 3 T11: 0.2169 T22: 0.2483
REMARK 3 T33: 0.2976 T12: -0.0009
REMARK 3 T13: 0.0874 T23: -0.0380
REMARK 3 L TENSOR
REMARK 3 L11: 4.0826 L22: 3.0348
REMARK 3 L33: 2.6612 L12: 0.0256
REMARK 3 L13: 0.8747 L23: -0.3911
REMARK 3 S TENSOR
REMARK 3 S11: -0.0361 S12: -0.3493 S13: 0.1974
REMARK 3 S21: 0.2932 S22: 0.0757 S23: 0.0748
REMARK 3 S31: 0.0031 S32: -0.2127 S33: -0.0399
REMARK 3 TLS GROUP : 8
REMARK 3 SELECTION: chain 'D' and (resid 153 through 313 )
REMARK 3 ORIGIN FOR THE GROUP (A): -46.8509 46.0700 160.1192
REMARK 3 T TENSOR
REMARK 3 T11: 0.1991 T22: 0.3606
REMARK 3 T33: 0.4937 T12: -0.0554
REMARK 3 T13: 0.0199 T23: 0.0893
REMARK 3 L TENSOR
REMARK 3 L11: 3.6692 L22: 1.2518
REMARK 3 L33: 3.9118 L12: 0.7164
REMARK 3 L13: -0.4072 L23: -0.1775
REMARK 3 S TENSOR
REMARK 3 S11: -0.2428 S12: 0.3690 S13: 0.1582
REMARK 3 S21: -0.1285 S22: 0.0529 S23: 0.0546
REMARK 3 S31: -0.0264 S32: 0.6345 S33: 0.1540
REMARK 3 TLS GROUP : 9
REMARK 3 SELECTION: chain 'E' and (resid 13 through 152 )
REMARK 3 ORIGIN FOR THE GROUP (A): -51.8821 31.3557 97.6645
REMARK 3 T TENSOR
REMARK 3 T11: 0.6851 T22: 0.7555
REMARK 3 T33: 0.2771 T12: 0.0115
REMARK 3 T13: -0.0933 T23: 0.0825
REMARK 3 L TENSOR
REMARK 3 L11: 2.5681 L22: 2.6331
REMARK 3 L33: 0.8512 L12: -0.0211
REMARK 3 L13: -1.1469 L23: -0.5496
REMARK 3 S TENSOR
REMARK 3 S11: 0.0447 S12: 0.4578 S13: 0.0496
REMARK 3 S21: -0.1810 S22: 0.1268 S23: 0.2798
REMARK 3 S31: -0.0805 S32: -0.3060 S33: -0.1737
REMARK 3 TLS GROUP : 10
REMARK 3 SELECTION: chain 'E' and (resid 153 through 313 )
REMARK 3 ORIGIN FOR THE GROUP (A): -53.8033 23.4543 122.8052
REMARK 3 T TENSOR
REMARK 3 T11: 0.7496 T22: 0.6102
REMARK 3 T33: 0.4434 T12: 0.2805
REMARK 3 T13: 0.0587 T23: 0.1282
REMARK 3 L TENSOR
REMARK 3 L11: 2.3958 L22: 2.8412
REMARK 3 L33: 5.8485 L12: -0.8482
REMARK 3 L13: 0.7800 L23: -0.9313
REMARK 3 S TENSOR
REMARK 3 S11: -0.4241 S12: -0.1384 S13: 0.0601
REMARK 3 S21: 0.7180 S22: 0.4100 S23: 0.1335
REMARK 3 S31: 0.0812 S32: 0.2676 S33: 0.0156
REMARK 3 TLS GROUP : 11
REMARK 3 SELECTION: chain 'F' and (resid 13 through 68 )
REMARK 3 ORIGIN FOR THE GROUP (A): -19.2334 41.8810 98.0621
REMARK 3 T TENSOR
REMARK 3 T11: 0.7381 T22: 0.6974
REMARK 3 T33: 0.2607 T12: -0.0499
REMARK 3 T13: 0.1238 T23: -0.0143
REMARK 3 L TENSOR
REMARK 3 L11: 2.7815 L22: 6.3612
REMARK 3 L33: 0.8093 L12: -0.9644
REMARK 3 L13: 1.2465 L23: 0.2397
REMARK 3 S TENSOR
REMARK 3 S11: 0.1307 S12: 0.2828 S13: 0.1699
REMARK 3 S21: 0.1205 S22: 0.0139 S23: -0.2675
REMARK 3 S31: -0.2308 S32: 0.4750 S33: -0.1703
REMARK 3 TLS GROUP : 12
REMARK 3 SELECTION: chain 'F' and (resid 69 through 152 )
REMARK 3 ORIGIN FOR THE GROUP (A): -23.9159 45.2339 97.2441
REMARK 3 T TENSOR
REMARK 3 T11: 0.7353 T22: 0.6197
REMARK 3 T33: 0.2668 T12: -0.0662
REMARK 3 T13: 0.1126 T23: 0.0396
REMARK 3 L TENSOR
REMARK 3 L11: 3.0921 L22: 2.5490
REMARK 3 L33: 2.1172 L12: 0.4455
REMARK 3 L13: -0.1777 L23: 1.4725
REMARK 3 S TENSOR
REMARK 3 S11: -0.0241 S12: 0.3064 S13: 0.1095
REMARK 3 S21: -0.5033 S22: 0.2653 S23: -0.0990
REMARK 3 S31: -0.3349 S32: 0.0340 S33: -0.2230
REMARK 3 TLS GROUP : 13
REMARK 3 SELECTION: chain 'F' and (resid 153 through 313 )
REMARK 3 ORIGIN FOR THE GROUP (A): -27.9128 49.4828 122.8977
REMARK 3 T TENSOR
REMARK 3 T11: 0.4012 T22: 0.8634
REMARK 3 T33: 0.4107 T12: -0.0782
REMARK 3 T13: 0.0578 T23: -0.1150
REMARK 3 L TENSOR
REMARK 3 L11: 3.5394 L22: 1.9671
REMARK 3 L33: 5.9275 L12: 0.1197
REMARK 3 L13: -1.0658 L23: -0.0639
REMARK 3 S TENSOR
REMARK 3 S11: -0.0284 S12: -0.9194 S13: 0.1613
REMARK 3 S21: 0.0230 S22: 0.0587 S23: -0.0177
REMARK 3 S31: 0.1420 S32: -0.1901 S33: -0.0383
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 4MX8 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 30-SEP-13.
REMARK 100 THE RCSB ID CODE IS RCSB082479.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 23-APR-13
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 19-ID
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97897
REMARK 200 MONOCHROMATOR : DOUBLE CRYSTAL MONOCHROMATOR
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315R
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-3000
REMARK 200 DATA SCALING SOFTWARE : HKL-3000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 81145
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.900
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.2
REMARK 200 DATA REDUNDANCY : 4.100
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.05800
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 11.7000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.90
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.95
REMARK 200 COMPLETENESS FOR SHELL (%) : 96.4
REMARK 200 DATA REDUNDANCY IN SHELL : 4.10
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.60100
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.200
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD
REMARK 200 SOFTWARE USED: HKL3000, SHELXS,MLPHARE,RESOLVE,SOLVE,BUCCANEER
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 74.48
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.82
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 2.4 M SODIUM MALONATE PH 7.0, VAPOR
REMARK 280 DIFFUSION, SITTING DROP, TEMPERATURE 289K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1
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 X+1/2,Y+1/2,Z
REMARK 290 4555 -X+1/2,Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 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 1.000000 0.000000 0.000000 100.83150
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 58.27350
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 100.83150
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 58.27350
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 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 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 3
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: 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
REMARK 350 BIOMOLECULE: 4
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: 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
REMARK 350 BIOMOLECULE: 5
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: 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
REMARK 350 BIOMOLECULE: 6
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: 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 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 SER A -1
REMARK 465 ASN A 0
REMARK 465 ALA A 1
REMARK 465 GLY A 2
REMARK 465 THR A 3
REMARK 465 ALA A 4
REMARK 465 ASP A 5
REMARK 465 ASP A 6
REMARK 465 SER A 7
REMARK 465 ALA A 8
REMARK 465 GLU A 9
REMARK 465 THR A 10
REMARK 465 THR A 11
REMARK 465 SER B -1
REMARK 465 ASN B 0
REMARK 465 ALA B 1
REMARK 465 GLY B 2
REMARK 465 THR B 3
REMARK 465 ALA B 4
REMARK 465 ASP B 5
REMARK 465 ASP B 6
REMARK 465 SER B 7
REMARK 465 ALA B 8
REMARK 465 GLU B 9
REMARK 465 THR B 10
REMARK 465 THR B 11
REMARK 465 SER C -1
REMARK 465 ASN C 0
REMARK 465 ALA C 1
REMARK 465 GLY C 2
REMARK 465 THR C 3
REMARK 465 ALA C 4
REMARK 465 ASP C 5
REMARK 465 ASP C 6
REMARK 465 SER C 7
REMARK 465 ALA C 8
REMARK 465 GLU C 9
REMARK 465 THR C 10
REMARK 465 THR C 11
REMARK 465 PRO C 12
REMARK 465 SER D -1
REMARK 465 ASN D 0
REMARK 465 ALA D 1
REMARK 465 GLY D 2
REMARK 465 THR D 3
REMARK 465 ALA D 4
REMARK 465 ASP D 5
REMARK 465 ASP D 6
REMARK 465 SER D 7
REMARK 465 ALA D 8
REMARK 465 GLU D 9
REMARK 465 THR D 10
REMARK 465 THR D 11
REMARK 465 SER E -1
REMARK 465 ASN E 0
REMARK 465 ALA E 1
REMARK 465 GLY E 2
REMARK 465 THR E 3
REMARK 465 ALA E 4
REMARK 465 ASP E 5
REMARK 465 ASP E 6
REMARK 465 SER E 7
REMARK 465 ALA E 8
REMARK 465 GLU E 9
REMARK 465 THR E 10
REMARK 465 THR E 11
REMARK 465 PRO E 12
REMARK 465 SER F -1
REMARK 465 ASN F 0
REMARK 465 ALA F 1
REMARK 465 GLY F 2
REMARK 465 THR F 3
REMARK 465 ALA F 4
REMARK 465 ASP F 5
REMARK 465 ASP F 6
REMARK 465 SER F 7
REMARK 465 ALA F 8
REMARK 465 GLU F 9
REMARK 465 THR F 10
REMARK 465 THR F 11
REMARK 465 PRO F 12
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 PRO A 69 86.56 -67.63
REMARK 500 SER A 178 -147.31 45.36
REMARK 500 HIS A 228 -5.42 72.96
REMARK 500 ASP A 241 77.20 35.19
REMARK 500 GLU A 269 -34.10 -38.96
REMARK 500 PRO B 69 84.63 -67.47
REMARK 500 LEU B 129 37.90 -98.65
REMARK 500 SER B 178 -147.34 41.34
REMARK 500 PRO B 231 175.20 -57.86
REMARK 500 ASP B 241 76.08 42.12
REMARK 500 PRO C 69 95.15 -69.20
REMARK 500 GLN C 103 68.04 32.49
REMARK 500 LEU C 129 46.73 -107.47
REMARK 500 SER C 178 -150.38 52.13
REMARK 500 ASN C 197 92.63 -68.45
REMARK 500 PHE C 294 65.40 36.37
REMARK 500 ARG D 46 80.43 -161.10
REMARK 500 PRO D 69 87.84 -69.30
REMARK 500 LEU D 129 35.91 -98.93
REMARK 500 SER D 178 -151.52 52.45
REMARK 500 ASP D 241 77.78 34.47
REMARK 500 PHE D 294 64.91 60.89
REMARK 500 GLN E 103 68.34 35.07
REMARK 500 SER E 178 -160.17 57.27
REMARK 500 ASN E 197 95.68 -65.34
REMARK 500 ASP E 241 70.86 28.32
REMARK 500 ASP E 280 30.12 71.47
REMARK 500 HIS E 281 32.12 -99.06
REMARK 500 PHE E 294 72.43 33.00
REMARK 500 LEU E 308 -9.57 -59.53
REMARK 500 PRO F 69 87.21 -66.66
REMARK 500 GLN F 103 69.68 33.57
REMARK 500 SER F 178 -150.30 40.79
REMARK 500 ASP F 241 71.90 57.66
REMARK 500 ASN F 286 106.19 -58.55
REMARK 500 PHE F 294 71.23 31.85
REMARK 500 ALA F 312 51.70 -99.70
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: MCSG-APC111338 RELATED DB: TARGETTRACK
DBREF 4MX8 A 2 313 UNP D1BRG9 D1BRG9_XYLCX 29 340
DBREF 4MX8 B 2 313 UNP D1BRG9 D1BRG9_XYLCX 29 340
DBREF 4MX8 C 2 313 UNP D1BRG9 D1BRG9_XYLCX 29 340
DBREF 4MX8 D 2 313 UNP D1BRG9 D1BRG9_XYLCX 29 340
DBREF 4MX8 E 2 313 UNP D1BRG9 D1BRG9_XYLCX 29 340
DBREF 4MX8 F 2 313 UNP D1BRG9 D1BRG9_XYLCX 29 340
SEQADV 4MX8 SER A -1 UNP D1BRG9 EXPRESSION TAG
SEQADV 4MX8 ASN A 0 UNP D1BRG9 EXPRESSION TAG
SEQADV 4MX8 ALA A 1 UNP D1BRG9 EXPRESSION TAG
SEQADV 4MX8 SER B -1 UNP D1BRG9 EXPRESSION TAG
SEQADV 4MX8 ASN B 0 UNP D1BRG9 EXPRESSION TAG
SEQADV 4MX8 ALA B 1 UNP D1BRG9 EXPRESSION TAG
SEQADV 4MX8 SER C -1 UNP D1BRG9 EXPRESSION TAG
SEQADV 4MX8 ASN C 0 UNP D1BRG9 EXPRESSION TAG
SEQADV 4MX8 ALA C 1 UNP D1BRG9 EXPRESSION TAG
SEQADV 4MX8 SER D -1 UNP D1BRG9 EXPRESSION TAG
SEQADV 4MX8 ASN D 0 UNP D1BRG9 EXPRESSION TAG
SEQADV 4MX8 ALA D 1 UNP D1BRG9 EXPRESSION TAG
SEQADV 4MX8 SER E -1 UNP D1BRG9 EXPRESSION TAG
SEQADV 4MX8 ASN E 0 UNP D1BRG9 EXPRESSION TAG
SEQADV 4MX8 ALA E 1 UNP D1BRG9 EXPRESSION TAG
SEQADV 4MX8 SER F -1 UNP D1BRG9 EXPRESSION TAG
SEQADV 4MX8 ASN F 0 UNP D1BRG9 EXPRESSION TAG
SEQADV 4MX8 ALA F 1 UNP D1BRG9 EXPRESSION TAG
SEQRES 1 A 315 SER ASN ALA GLY THR ALA ASP ASP SER ALA GLU THR THR
SEQRES 2 A 315 PRO ALA THR ALA SER TYR THR TRP ASP ARG ASN THR ALA
SEQRES 3 A 315 THR GLU GLU GLY ALA ASP PRO VAL TYR GLU GLU THR THR
SEQRES 4 A 315 VAL GLU VAL PRO VAL ASP PRO GLN ARG ILE VAL VAL PHE
SEQRES 5 A 315 ASP MSE ALA ALA LEU ASP THR ILE GLY ALA LEU GLY GLY
SEQRES 6 A 315 GLU ILE ALA GLY ALA PRO LEU ASP SER VAL PRO ASP TYR
SEQRES 7 A 315 LEU GLU GLU TYR LEU ALA ASP ASP ALA PHE ASN ALA GLY
SEQRES 8 A 315 THR LEU PHE GLU ALA ASP LEU ILE ALA ILE GLU ALA GLN
SEQRES 9 A 315 GLN PRO ASP LEU ILE VAL VAL GLY GLY ARG SER SER GLY
SEQRES 10 A 315 LEU TRP ALA ASP LEU ASN GLU ILE ALA PRO THR ILE ASP
SEQRES 11 A 315 LEU SER LEU ARG GLY SER TYR LEU ASP THR LEU GLU GLN
SEQRES 12 A 315 ASN THR THR PHE LEU GLY LYS VAL LEU GLY ALA GLU ALA
SEQRES 13 A 315 GLU ALA GLU SER VAL LEU ALA GLU LEU GLU ALA GLY ILE
SEQRES 14 A 315 ALA GLU ALA LYS ALA ALA VAL THR GLU ALA SER GLY THR
SEQRES 15 A 315 GLY LEU GLY ILE MSE VAL SER GLY GLY GLN LEU SER ALA
SEQRES 16 A 315 LEU SER PRO ASN THR GLY ASN ASP PRO ARG GLY ALA ARG
SEQRES 17 A 315 GLY GLY LEU ILE TYR ASP VAL PHE GLY VAL GLN PRO VAL
SEQRES 18 A 315 LEU GLU ASP ILE LYS ALA ALA THR HIS GLY GLU PRO ILE
SEQRES 19 A 315 SER PHE GLU PHE LEU LEU GLU HIS ASP PRO GLN TRP LEU
SEQRES 20 A 315 TRP VAL VAL ASP ARG ASP ALA ALA THR GLY ALA GLU GLY
SEQRES 21 A 315 ALA GLN ALA ALA LYS VAL VAL LEU ASP ASN GLU ILE VAL
SEQRES 22 A 315 ASN ARG THR THR ALA ALA THR GLU ASP HIS VAL LEU TYR
SEQRES 23 A 315 LEU ASN PRO THR ALA TRP TYR ILE VAL PHE GLY GLY VAL
SEQRES 24 A 315 GLU THR THR ARG ILE MSE ILE ASP ASP VAL LEU GLN VAL
SEQRES 25 A 315 ALA ALA ARG
SEQRES 1 B 315 SER ASN ALA GLY THR ALA ASP ASP SER ALA GLU THR THR
SEQRES 2 B 315 PRO ALA THR ALA SER TYR THR TRP ASP ARG ASN THR ALA
SEQRES 3 B 315 THR GLU GLU GLY ALA ASP PRO VAL TYR GLU GLU THR THR
SEQRES 4 B 315 VAL GLU VAL PRO VAL ASP PRO GLN ARG ILE VAL VAL PHE
SEQRES 5 B 315 ASP MSE ALA ALA LEU ASP THR ILE GLY ALA LEU GLY GLY
SEQRES 6 B 315 GLU ILE ALA GLY ALA PRO LEU ASP SER VAL PRO ASP TYR
SEQRES 7 B 315 LEU GLU GLU TYR LEU ALA ASP ASP ALA PHE ASN ALA GLY
SEQRES 8 B 315 THR LEU PHE GLU ALA ASP LEU ILE ALA ILE GLU ALA GLN
SEQRES 9 B 315 GLN PRO ASP LEU ILE VAL VAL GLY GLY ARG SER SER GLY
SEQRES 10 B 315 LEU TRP ALA ASP LEU ASN GLU ILE ALA PRO THR ILE ASP
SEQRES 11 B 315 LEU SER LEU ARG GLY SER TYR LEU ASP THR LEU GLU GLN
SEQRES 12 B 315 ASN THR THR PHE LEU GLY LYS VAL LEU GLY ALA GLU ALA
SEQRES 13 B 315 GLU ALA GLU SER VAL LEU ALA GLU LEU GLU ALA GLY ILE
SEQRES 14 B 315 ALA GLU ALA LYS ALA ALA VAL THR GLU ALA SER GLY THR
SEQRES 15 B 315 GLY LEU GLY ILE MSE VAL SER GLY GLY GLN LEU SER ALA
SEQRES 16 B 315 LEU SER PRO ASN THR GLY ASN ASP PRO ARG GLY ALA ARG
SEQRES 17 B 315 GLY GLY LEU ILE TYR ASP VAL PHE GLY VAL GLN PRO VAL
SEQRES 18 B 315 LEU GLU ASP ILE LYS ALA ALA THR HIS GLY GLU PRO ILE
SEQRES 19 B 315 SER PHE GLU PHE LEU LEU GLU HIS ASP PRO GLN TRP LEU
SEQRES 20 B 315 TRP VAL VAL ASP ARG ASP ALA ALA THR GLY ALA GLU GLY
SEQRES 21 B 315 ALA GLN ALA ALA LYS VAL VAL LEU ASP ASN GLU ILE VAL
SEQRES 22 B 315 ASN ARG THR THR ALA ALA THR GLU ASP HIS VAL LEU TYR
SEQRES 23 B 315 LEU ASN PRO THR ALA TRP TYR ILE VAL PHE GLY GLY VAL
SEQRES 24 B 315 GLU THR THR ARG ILE MSE ILE ASP ASP VAL LEU GLN VAL
SEQRES 25 B 315 ALA ALA ARG
SEQRES 1 C 315 SER ASN ALA GLY THR ALA ASP ASP SER ALA GLU THR THR
SEQRES 2 C 315 PRO ALA THR ALA SER TYR THR TRP ASP ARG ASN THR ALA
SEQRES 3 C 315 THR GLU GLU GLY ALA ASP PRO VAL TYR GLU GLU THR THR
SEQRES 4 C 315 VAL GLU VAL PRO VAL ASP PRO GLN ARG ILE VAL VAL PHE
SEQRES 5 C 315 ASP MSE ALA ALA LEU ASP THR ILE GLY ALA LEU GLY GLY
SEQRES 6 C 315 GLU ILE ALA GLY ALA PRO LEU ASP SER VAL PRO ASP TYR
SEQRES 7 C 315 LEU GLU GLU TYR LEU ALA ASP ASP ALA PHE ASN ALA GLY
SEQRES 8 C 315 THR LEU PHE GLU ALA ASP LEU ILE ALA ILE GLU ALA GLN
SEQRES 9 C 315 GLN PRO ASP LEU ILE VAL VAL GLY GLY ARG SER SER GLY
SEQRES 10 C 315 LEU TRP ALA ASP LEU ASN GLU ILE ALA PRO THR ILE ASP
SEQRES 11 C 315 LEU SER LEU ARG GLY SER TYR LEU ASP THR LEU GLU GLN
SEQRES 12 C 315 ASN THR THR PHE LEU GLY LYS VAL LEU GLY ALA GLU ALA
SEQRES 13 C 315 GLU ALA GLU SER VAL LEU ALA GLU LEU GLU ALA GLY ILE
SEQRES 14 C 315 ALA GLU ALA LYS ALA ALA VAL THR GLU ALA SER GLY THR
SEQRES 15 C 315 GLY LEU GLY ILE MSE VAL SER GLY GLY GLN LEU SER ALA
SEQRES 16 C 315 LEU SER PRO ASN THR GLY ASN ASP PRO ARG GLY ALA ARG
SEQRES 17 C 315 GLY GLY LEU ILE TYR ASP VAL PHE GLY VAL GLN PRO VAL
SEQRES 18 C 315 LEU GLU ASP ILE LYS ALA ALA THR HIS GLY GLU PRO ILE
SEQRES 19 C 315 SER PHE GLU PHE LEU LEU GLU HIS ASP PRO GLN TRP LEU
SEQRES 20 C 315 TRP VAL VAL ASP ARG ASP ALA ALA THR GLY ALA GLU GLY
SEQRES 21 C 315 ALA GLN ALA ALA LYS VAL VAL LEU ASP ASN GLU ILE VAL
SEQRES 22 C 315 ASN ARG THR THR ALA ALA THR GLU ASP HIS VAL LEU TYR
SEQRES 23 C 315 LEU ASN PRO THR ALA TRP TYR ILE VAL PHE GLY GLY VAL
SEQRES 24 C 315 GLU THR THR ARG ILE MSE ILE ASP ASP VAL LEU GLN VAL
SEQRES 25 C 315 ALA ALA ARG
SEQRES 1 D 315 SER ASN ALA GLY THR ALA ASP ASP SER ALA GLU THR THR
SEQRES 2 D 315 PRO ALA THR ALA SER TYR THR TRP ASP ARG ASN THR ALA
SEQRES 3 D 315 THR GLU GLU GLY ALA ASP PRO VAL TYR GLU GLU THR THR
SEQRES 4 D 315 VAL GLU VAL PRO VAL ASP PRO GLN ARG ILE VAL VAL PHE
SEQRES 5 D 315 ASP MSE ALA ALA LEU ASP THR ILE GLY ALA LEU GLY GLY
SEQRES 6 D 315 GLU ILE ALA GLY ALA PRO LEU ASP SER VAL PRO ASP TYR
SEQRES 7 D 315 LEU GLU GLU TYR LEU ALA ASP ASP ALA PHE ASN ALA GLY
SEQRES 8 D 315 THR LEU PHE GLU ALA ASP LEU ILE ALA ILE GLU ALA GLN
SEQRES 9 D 315 GLN PRO ASP LEU ILE VAL VAL GLY GLY ARG SER SER GLY
SEQRES 10 D 315 LEU TRP ALA ASP LEU ASN GLU ILE ALA PRO THR ILE ASP
SEQRES 11 D 315 LEU SER LEU ARG GLY SER TYR LEU ASP THR LEU GLU GLN
SEQRES 12 D 315 ASN THR THR PHE LEU GLY LYS VAL LEU GLY ALA GLU ALA
SEQRES 13 D 315 GLU ALA GLU SER VAL LEU ALA GLU LEU GLU ALA GLY ILE
SEQRES 14 D 315 ALA GLU ALA LYS ALA ALA VAL THR GLU ALA SER GLY THR
SEQRES 15 D 315 GLY LEU GLY ILE MSE VAL SER GLY GLY GLN LEU SER ALA
SEQRES 16 D 315 LEU SER PRO ASN THR GLY ASN ASP PRO ARG GLY ALA ARG
SEQRES 17 D 315 GLY GLY LEU ILE TYR ASP VAL PHE GLY VAL GLN PRO VAL
SEQRES 18 D 315 LEU GLU ASP ILE LYS ALA ALA THR HIS GLY GLU PRO ILE
SEQRES 19 D 315 SER PHE GLU PHE LEU LEU GLU HIS ASP PRO GLN TRP LEU
SEQRES 20 D 315 TRP VAL VAL ASP ARG ASP ALA ALA THR GLY ALA GLU GLY
SEQRES 21 D 315 ALA GLN ALA ALA LYS VAL VAL LEU ASP ASN GLU ILE VAL
SEQRES 22 D 315 ASN ARG THR THR ALA ALA THR GLU ASP HIS VAL LEU TYR
SEQRES 23 D 315 LEU ASN PRO THR ALA TRP TYR ILE VAL PHE GLY GLY VAL
SEQRES 24 D 315 GLU THR THR ARG ILE MSE ILE ASP ASP VAL LEU GLN VAL
SEQRES 25 D 315 ALA ALA ARG
SEQRES 1 E 315 SER ASN ALA GLY THR ALA ASP ASP SER ALA GLU THR THR
SEQRES 2 E 315 PRO ALA THR ALA SER TYR THR TRP ASP ARG ASN THR ALA
SEQRES 3 E 315 THR GLU GLU GLY ALA ASP PRO VAL TYR GLU GLU THR THR
SEQRES 4 E 315 VAL GLU VAL PRO VAL ASP PRO GLN ARG ILE VAL VAL PHE
SEQRES 5 E 315 ASP MSE ALA ALA LEU ASP THR ILE GLY ALA LEU GLY GLY
SEQRES 6 E 315 GLU ILE ALA GLY ALA PRO LEU ASP SER VAL PRO ASP TYR
SEQRES 7 E 315 LEU GLU GLU TYR LEU ALA ASP ASP ALA PHE ASN ALA GLY
SEQRES 8 E 315 THR LEU PHE GLU ALA ASP LEU ILE ALA ILE GLU ALA GLN
SEQRES 9 E 315 GLN PRO ASP LEU ILE VAL VAL GLY GLY ARG SER SER GLY
SEQRES 10 E 315 LEU TRP ALA ASP LEU ASN GLU ILE ALA PRO THR ILE ASP
SEQRES 11 E 315 LEU SER LEU ARG GLY SER TYR LEU ASP THR LEU GLU GLN
SEQRES 12 E 315 ASN THR THR PHE LEU GLY LYS VAL LEU GLY ALA GLU ALA
SEQRES 13 E 315 GLU ALA GLU SER VAL LEU ALA GLU LEU GLU ALA GLY ILE
SEQRES 14 E 315 ALA GLU ALA LYS ALA ALA VAL THR GLU ALA SER GLY THR
SEQRES 15 E 315 GLY LEU GLY ILE MSE VAL SER GLY GLY GLN LEU SER ALA
SEQRES 16 E 315 LEU SER PRO ASN THR GLY ASN ASP PRO ARG GLY ALA ARG
SEQRES 17 E 315 GLY GLY LEU ILE TYR ASP VAL PHE GLY VAL GLN PRO VAL
SEQRES 18 E 315 LEU GLU ASP ILE LYS ALA ALA THR HIS GLY GLU PRO ILE
SEQRES 19 E 315 SER PHE GLU PHE LEU LEU GLU HIS ASP PRO GLN TRP LEU
SEQRES 20 E 315 TRP VAL VAL ASP ARG ASP ALA ALA THR GLY ALA GLU GLY
SEQRES 21 E 315 ALA GLN ALA ALA LYS VAL VAL LEU ASP ASN GLU ILE VAL
SEQRES 22 E 315 ASN ARG THR THR ALA ALA THR GLU ASP HIS VAL LEU TYR
SEQRES 23 E 315 LEU ASN PRO THR ALA TRP TYR ILE VAL PHE GLY GLY VAL
SEQRES 24 E 315 GLU THR THR ARG ILE MSE ILE ASP ASP VAL LEU GLN VAL
SEQRES 25 E 315 ALA ALA ARG
SEQRES 1 F 315 SER ASN ALA GLY THR ALA ASP ASP SER ALA GLU THR THR
SEQRES 2 F 315 PRO ALA THR ALA SER TYR THR TRP ASP ARG ASN THR ALA
SEQRES 3 F 315 THR GLU GLU GLY ALA ASP PRO VAL TYR GLU GLU THR THR
SEQRES 4 F 315 VAL GLU VAL PRO VAL ASP PRO GLN ARG ILE VAL VAL PHE
SEQRES 5 F 315 ASP MSE ALA ALA LEU ASP THR ILE GLY ALA LEU GLY GLY
SEQRES 6 F 315 GLU ILE ALA GLY ALA PRO LEU ASP SER VAL PRO ASP TYR
SEQRES 7 F 315 LEU GLU GLU TYR LEU ALA ASP ASP ALA PHE ASN ALA GLY
SEQRES 8 F 315 THR LEU PHE GLU ALA ASP LEU ILE ALA ILE GLU ALA GLN
SEQRES 9 F 315 GLN PRO ASP LEU ILE VAL VAL GLY GLY ARG SER SER GLY
SEQRES 10 F 315 LEU TRP ALA ASP LEU ASN GLU ILE ALA PRO THR ILE ASP
SEQRES 11 F 315 LEU SER LEU ARG GLY SER TYR LEU ASP THR LEU GLU GLN
SEQRES 12 F 315 ASN THR THR PHE LEU GLY LYS VAL LEU GLY ALA GLU ALA
SEQRES 13 F 315 GLU ALA GLU SER VAL LEU ALA GLU LEU GLU ALA GLY ILE
SEQRES 14 F 315 ALA GLU ALA LYS ALA ALA VAL THR GLU ALA SER GLY THR
SEQRES 15 F 315 GLY LEU GLY ILE MSE VAL SER GLY GLY GLN LEU SER ALA
SEQRES 16 F 315 LEU SER PRO ASN THR GLY ASN ASP PRO ARG GLY ALA ARG
SEQRES 17 F 315 GLY GLY LEU ILE TYR ASP VAL PHE GLY VAL GLN PRO VAL
SEQRES 18 F 315 LEU GLU ASP ILE LYS ALA ALA THR HIS GLY GLU PRO ILE
SEQRES 19 F 315 SER PHE GLU PHE LEU LEU GLU HIS ASP PRO GLN TRP LEU
SEQRES 20 F 315 TRP VAL VAL ASP ARG ASP ALA ALA THR GLY ALA GLU GLY
SEQRES 21 F 315 ALA GLN ALA ALA LYS VAL VAL LEU ASP ASN GLU ILE VAL
SEQRES 22 F 315 ASN ARG THR THR ALA ALA THR GLU ASP HIS VAL LEU TYR
SEQRES 23 F 315 LEU ASN PRO THR ALA TRP TYR ILE VAL PHE GLY GLY VAL
SEQRES 24 F 315 GLU THR THR ARG ILE MSE ILE ASP ASP VAL LEU GLN VAL
SEQRES 25 F 315 ALA ALA ARG
MODRES 4MX8 MSE A 52 MET SELENOMETHIONINE
MODRES 4MX8 MSE A 185 MET SELENOMETHIONINE
MODRES 4MX8 MSE A 303 MET SELENOMETHIONINE
MODRES 4MX8 MSE B 52 MET SELENOMETHIONINE
MODRES 4MX8 MSE B 185 MET SELENOMETHIONINE
MODRES 4MX8 MSE B 303 MET SELENOMETHIONINE
MODRES 4MX8 MSE C 52 MET SELENOMETHIONINE
MODRES 4MX8 MSE C 185 MET SELENOMETHIONINE
MODRES 4MX8 MSE C 303 MET SELENOMETHIONINE
MODRES 4MX8 MSE D 52 MET SELENOMETHIONINE
MODRES 4MX8 MSE D 185 MET SELENOMETHIONINE
MODRES 4MX8 MSE D 303 MET SELENOMETHIONINE
MODRES 4MX8 MSE E 52 MET SELENOMETHIONINE
MODRES 4MX8 MSE E 185 MET SELENOMETHIONINE
MODRES 4MX8 MSE E 303 MET SELENOMETHIONINE
MODRES 4MX8 MSE F 52 MET SELENOMETHIONINE
MODRES 4MX8 MSE F 185 MET SELENOMETHIONINE
MODRES 4MX8 MSE F 303 MET SELENOMETHIONINE
HET MSE A 52 8
HET MSE A 185 8
HET MSE A 303 8
HET MSE B 52 8
HET MSE B 185 8
HET MSE B 303 8
HET MSE C 52 8
HET MSE C 185 8
HET MSE C 303 8
HET MSE D 52 8
HET MSE D 185 8
HET MSE D 303 8
HET MSE E 52 8
HET MSE E 185 8
HET MSE E 303 8
HET MSE F 52 8
HET MSE F 185 8
HET MSE F 303 8
HETNAM MSE SELENOMETHIONINE
FORMUL 1 MSE 18(C5 H11 N O2 SE)
FORMUL 7 HOH *234(H2 O)
HELIX 1 1 ASP A 51 LEU A 61 1 11
HELIX 2 2 PRO A 69 VAL A 73 5 5
HELIX 3 3 PRO A 74 GLU A 79 1 6
HELIX 4 4 ASP A 95 GLN A 103 1 9
HELIX 5 5 GLY A 110 GLY A 115 5 6
HELIX 6 6 LEU A 116 GLU A 122 1 7
HELIX 7 7 SER A 134 GLY A 151 1 18
HELIX 8 8 ALA A 152 SER A 178 1 27
HELIX 9 9 GLY A 204 VAL A 213 1 10
HELIX 10 10 ASP A 222 HIS A 228 1 7
HELIX 11 11 SER A 233 ASP A 241 1 9
HELIX 12 12 ARG A 250 GLY A 255 1 6
HELIX 13 13 ALA A 261 LEU A 266 1 6
HELIX 14 14 ILE A 270 ARG A 273 5 4
HELIX 15 15 THR A 274 GLU A 279 1 6
HELIX 16 16 ASN A 286 ILE A 292 1 7
HELIX 17 17 GLY A 296 LEU A 308 1 13
HELIX 18 18 GLN A 309 ARG A 313 5 5
HELIX 19 19 ASP B 51 LEU B 61 1 11
HELIX 20 20 PRO B 69 VAL B 73 5 5
HELIX 21 21 PRO B 74 GLU B 79 5 6
HELIX 22 22 ASP B 95 GLN B 103 1 9
HELIX 23 23 GLY B 110 GLY B 115 5 6
HELIX 24 24 LEU B 116 GLU B 122 1 7
HELIX 25 25 SER B 134 GLY B 151 1 18
HELIX 26 26 ALA B 152 SER B 178 1 27
HELIX 27 27 ASP B 201 ARG B 203 5 3
HELIX 28 28 GLY B 204 VAL B 213 1 10
HELIX 29 29 ASP B 222 HIS B 228 1 7
HELIX 30 30 SER B 233 ASP B 241 1 9
HELIX 31 31 ARG B 250 GLY B 255 1 6
HELIX 32 32 ALA B 261 LEU B 266 1 6
HELIX 33 33 ILE B 270 ARG B 273 5 4
HELIX 34 34 THR B 274 GLU B 279 1 6
HELIX 35 35 ASN B 286 ILE B 292 1 7
HELIX 36 36 GLY B 296 GLN B 309 1 14
HELIX 37 37 VAL B 310 ARG B 313 5 4
HELIX 38 38 ASP C 51 LEU C 61 1 11
HELIX 39 39 PRO C 69 VAL C 73 5 5
HELIX 40 40 PRO C 74 GLU C 79 5 6
HELIX 41 41 ASP C 95 GLN C 103 1 9
HELIX 42 42 GLY C 110 GLY C 115 5 6
HELIX 43 43 LEU C 116 GLU C 122 1 7
HELIX 44 44 SER C 134 GLY C 151 1 18
HELIX 45 45 ALA C 152 SER C 178 1 27
HELIX 46 46 ASP C 201 GLY C 207 5 7
HELIX 47 47 GLY C 208 VAL C 213 1 6
HELIX 48 48 ASP C 222 HIS C 228 1 7
HELIX 49 49 SER C 233 ASP C 241 1 9
HELIX 50 50 ARG C 250 THR C 254 1 5
HELIX 51 51 ALA C 261 LEU C 266 1 6
HELIX 52 52 ILE C 270 ARG C 273 5 4
HELIX 53 53 THR C 274 GLU C 279 1 6
HELIX 54 54 ASN C 286 ILE C 292 1 7
HELIX 55 55 GLY C 296 LEU C 308 1 13
HELIX 56 56 GLN C 309 ARG C 313 5 5
HELIX 57 57 ASP D 51 LEU D 61 1 11
HELIX 58 58 PRO D 69 VAL D 73 5 5
HELIX 59 59 PRO D 74 GLU D 79 5 6
HELIX 60 60 ASP D 95 GLN D 103 1 9
HELIX 61 61 GLY D 110 GLY D 115 5 6
HELIX 62 62 LEU D 116 GLU D 122 1 7
HELIX 63 63 SER D 134 GLY D 151 1 18
HELIX 64 64 ALA D 152 SER D 178 1 27
HELIX 65 65 ASP D 201 ARG D 203 5 3
HELIX 66 66 GLY D 204 VAL D 213 1 10
HELIX 67 67 ASP D 222 HIS D 228 1 7
HELIX 68 68 SER D 233 ASP D 241 1 9
HELIX 69 69 ARG D 250 GLY D 255 1 6
HELIX 70 70 ALA D 261 LEU D 266 1 6
HELIX 71 71 ILE D 270 ARG D 273 5 4
HELIX 72 72 THR D 274 GLU D 279 1 6
HELIX 73 73 ASN D 286 ILE D 292 1 7
HELIX 74 74 GLY D 296 GLN D 309 1 14
HELIX 75 75 VAL D 310 ARG D 313 5 4
HELIX 76 76 ASP E 51 LEU E 61 1 11
HELIX 77 77 PRO E 69 VAL E 73 5 5
HELIX 78 78 LEU E 77 GLU E 79 5 3
HELIX 79 79 ASP E 95 GLN E 103 1 9
HELIX 80 80 GLY E 110 GLY E 115 5 6
HELIX 81 81 LEU E 116 GLU E 122 1 7
HELIX 82 82 SER E 134 GLY E 151 1 18
HELIX 83 83 ALA E 152 SER E 178 1 27
HELIX 84 84 ASP E 201 ALA E 205 5 5
HELIX 85 85 ARG E 206 GLY E 207 5 2
HELIX 86 86 GLY E 208 VAL E 213 1 6
HELIX 87 87 ASP E 222 THR E 227 1 6
HELIX 88 88 SER E 233 ASP E 241 1 9
HELIX 89 89 ARG E 250 THR E 254 1 5
HELIX 90 90 ALA E 261 LEU E 266 1 6
HELIX 91 91 ILE E 270 ARG E 273 5 4
HELIX 92 92 THR E 274 GLU E 279 1 6
HELIX 93 93 ASN E 286 ILE E 292 1 7
HELIX 94 94 GLY E 296 LEU E 308 1 13
HELIX 95 95 GLN E 309 ARG E 313 5 5
HELIX 96 96 ASP F 51 LEU F 61 1 11
HELIX 97 97 PRO F 69 VAL F 73 5 5
HELIX 98 98 LEU F 77 GLU F 79 5 3
HELIX 99 99 ASP F 95 GLN F 103 1 9
HELIX 100 100 SER F 113 GLY F 115 5 3
HELIX 101 101 LEU F 116 GLU F 122 1 7
HELIX 102 102 SER F 134 GLY F 151 1 18
HELIX 103 103 ALA F 152 SER F 178 1 27
HELIX 104 104 ASP F 201 ALA F 205 5 5
HELIX 105 105 ARG F 206 GLY F 207 5 2
HELIX 106 106 GLY F 208 VAL F 213 1 6
HELIX 107 107 ASP F 222 THR F 227 1 6
HELIX 108 108 SER F 233 ASP F 241 1 9
HELIX 109 109 ARG F 250 GLY F 255 1 6
HELIX 110 110 ALA F 261 LEU F 266 1 6
HELIX 111 111 ILE F 270 ARG F 273 5 4
HELIX 112 112 THR F 274 GLU F 279 1 6
HELIX 113 113 ASN F 286 ILE F 292 1 7
HELIX 114 114 GLY F 296 LEU F 308 1 13
HELIX 115 115 GLN F 309 ARG F 313 5 5
SHEET 1 A 2 THR A 14 ASN A 22 0
SHEET 2 A 2 TYR A 33 PRO A 41 -1 O VAL A 40 N ALA A 15
SHEET 1 B 3 ILE A 47 VAL A 49 0
SHEET 2 B 3 LEU A 106 VAL A 109 1 O VAL A 108 N VAL A 48
SHEET 3 B 3 THR A 126 ASP A 128 1 O ILE A 127 N VAL A 109
SHEET 1 C 2 ILE A 65 ALA A 68 0
SHEET 2 C 2 LEU A 81 ASN A 87 1 O ALA A 82 N ILE A 65
SHEET 1 D 4 GLN A 190 ALA A 193 0
SHEET 2 D 4 GLY A 181 SER A 187 -1 N MSE A 185 O SER A 192
SHEET 3 D 4 TRP A 244 ASP A 249 1 O TRP A 246 N ILE A 184
SHEET 4 D 4 VAL A 282 LEU A 285 1 O LEU A 285 N VAL A 247
SHEET 1 E 2 THR B 14 ASN B 22 0
SHEET 2 E 2 TYR B 33 PRO B 41 -1 O VAL B 40 N ALA B 15
SHEET 1 F 3 ILE B 47 VAL B 49 0
SHEET 2 F 3 LEU B 106 VAL B 109 1 O VAL B 108 N VAL B 48
SHEET 3 F 3 THR B 126 ASP B 128 1 O ILE B 127 N VAL B 109
SHEET 1 G 2 ILE B 65 ALA B 68 0
SHEET 2 G 2 LEU B 81 ASN B 87 1 O ALA B 82 N ILE B 65
SHEET 1 H 4 GLN B 190 ALA B 193 0
SHEET 2 H 4 GLY B 181 SER B 187 -1 N SER B 187 O GLN B 190
SHEET 3 H 4 TRP B 244 ASP B 249 1 O TRP B 246 N ILE B 184
SHEET 4 H 4 VAL B 282 LEU B 285 1 O LEU B 285 N VAL B 247
SHEET 1 I 2 THR C 14 ASN C 22 0
SHEET 2 I 2 TYR C 33 PRO C 41 -1 O VAL C 40 N ALA C 15
SHEET 1 J 5 LEU C 81 ASN C 87 0
SHEET 2 J 5 ILE C 65 ALA C 68 1 N ILE C 65 O ALA C 82
SHEET 3 J 5 ILE C 47 VAL C 49 1 N ILE C 47 O ALA C 66
SHEET 4 J 5 LEU C 106 VAL C 109 1 O LEU C 106 N VAL C 48
SHEET 5 J 5 THR C 126 ASP C 128 1 O ILE C 127 N VAL C 109
SHEET 1 K 4 GLN C 190 ALA C 193 0
SHEET 2 K 4 GLY C 181 SER C 187 -1 N SER C 187 O GLN C 190
SHEET 3 K 4 TRP C 244 ASP C 249 1 O TRP C 246 N ILE C 184
SHEET 4 K 4 VAL C 282 LEU C 285 1 O LEU C 285 N VAL C 247
SHEET 1 L 2 THR D 14 ASN D 22 0
SHEET 2 L 2 TYR D 33 PRO D 41 -1 O VAL D 40 N ALA D 15
SHEET 1 M 3 ILE D 47 VAL D 49 0
SHEET 2 M 3 LEU D 106 VAL D 109 1 O VAL D 108 N VAL D 48
SHEET 3 M 3 THR D 126 ASP D 128 1 O ILE D 127 N VAL D 109
SHEET 1 N 2 ILE D 65 ALA D 68 0
SHEET 2 N 2 LEU D 81 ASN D 87 1 O ALA D 82 N ILE D 65
SHEET 1 O 4 GLN D 190 ALA D 193 0
SHEET 2 O 4 GLY D 181 SER D 187 -1 N SER D 187 O GLN D 190
SHEET 3 O 4 TRP D 244 ASP D 249 1 O TRP D 246 N ILE D 184
SHEET 4 O 4 VAL D 282 LEU D 285 1 O LEU D 285 N VAL D 247
SHEET 1 P 2 THR E 14 ASN E 22 0
SHEET 2 P 2 TYR E 33 PRO E 41 -1 O VAL E 40 N ALA E 15
SHEET 1 Q 3 ILE E 47 VAL E 49 0
SHEET 2 Q 3 LEU E 106 VAL E 109 1 O VAL E 108 N VAL E 48
SHEET 3 Q 3 THR E 126 ASP E 128 1 O ILE E 127 N VAL E 109
SHEET 1 R 2 ILE E 65 ALA E 68 0
SHEET 2 R 2 LEU E 81 ASN E 87 1 O ALA E 82 N ILE E 65
SHEET 1 S 3 GLN E 190 LEU E 194 0
SHEET 2 S 3 THR E 180 SER E 187 -1 N GLY E 183 O LEU E 194
SHEET 3 S 3 GLN E 217 PRO E 218 1 O GLN E 217 N GLY E 181
SHEET 1 T 4 GLN E 190 LEU E 194 0
SHEET 2 T 4 THR E 180 SER E 187 -1 N GLY E 183 O LEU E 194
SHEET 3 T 4 TRP E 244 ASP E 249 1 O TRP E 246 N ILE E 184
SHEET 4 T 4 VAL E 282 LEU E 285 1 O LEU E 283 N VAL E 247
SHEET 1 U 2 THR F 14 ASN F 22 0
SHEET 2 U 2 TYR F 33 PRO F 41 -1 O VAL F 40 N ALA F 15
SHEET 1 V 5 LEU F 81 ASN F 87 0
SHEET 2 V 5 ILE F 65 ALA F 68 1 N ALA F 66 O PHE F 86
SHEET 3 V 5 ILE F 47 VAL F 49 1 N ILE F 47 O ALA F 66
SHEET 4 V 5 LEU F 106 VAL F 109 1 O VAL F 108 N VAL F 48
SHEET 5 V 5 THR F 126 ASP F 128 1 O ILE F 127 N VAL F 109
SHEET 1 W 5 PRO F 231 ILE F 232 0
SHEET 2 W 5 GLN F 190 ALA F 193 -1 N LEU F 191 O ILE F 232
SHEET 3 W 5 GLY F 181 SER F 187 -1 N SER F 187 O GLN F 190
SHEET 4 W 5 TRP F 244 ASP F 249 1 O TRP F 246 N LEU F 182
SHEET 5 W 5 VAL F 282 LEU F 285 1 O LEU F 285 N VAL F 247
LINK C ASP A 51 N MSE A 52 1555 1555 1.33
LINK C MSE A 52 N ALA A 53 1555 1555 1.33
LINK C ILE A 184 N MSE A 185 1555 1555 1.33
LINK C MSE A 185 N VAL A 186 1555 1555 1.33
LINK C ILE A 302 N MSE A 303 1555 1555 1.33
LINK C MSE A 303 N ILE A 304 1555 1555 1.33
LINK C ASP B 51 N MSE B 52 1555 1555 1.33
LINK C MSE B 52 N ALA B 53 1555 1555 1.33
LINK C ILE B 184 N MSE B 185 1555 1555 1.32
LINK C MSE B 185 N VAL B 186 1555 1555 1.33
LINK C ILE B 302 N MSE B 303 1555 1555 1.33
LINK C MSE B 303 N ILE B 304 1555 1555 1.33
LINK C ASP C 51 N MSE C 52 1555 1555 1.33
LINK C MSE C 52 N ALA C 53 1555 1555 1.33
LINK C ILE C 184 N MSE C 185 1555 1555 1.32
LINK C MSE C 185 N VAL C 186 1555 1555 1.33
LINK C ILE C 302 N MSE C 303 1555 1555 1.33
LINK C MSE C 303 N ILE C 304 1555 1555 1.33
LINK C ASP D 51 N MSE D 52 1555 1555 1.33
LINK C MSE D 52 N ALA D 53 1555 1555 1.33
LINK C ILE D 184 N MSE D 185 1555 1555 1.32
LINK C MSE D 185 N VAL D 186 1555 1555 1.33
LINK C ILE D 302 N MSE D 303 1555 1555 1.33
LINK C MSE D 303 N ILE D 304 1555 1555 1.33
LINK C ASP E 51 N MSE E 52 1555 1555 1.32
LINK C MSE E 52 N ALA E 53 1555 1555 1.33
LINK C ILE E 184 N MSE E 185 1555 1555 1.32
LINK C MSE E 185 N VAL E 186 1555 1555 1.33
LINK C ILE E 302 N MSE E 303 1555 1555 1.33
LINK C MSE E 303 N ILE E 304 1555 1555 1.33
LINK C ASP F 51 N MSE F 52 1555 1555 1.32
LINK C MSE F 52 N ALA F 53 1555 1555 1.33
LINK C ILE F 184 N MSE F 185 1555 1555 1.33
LINK C MSE F 185 N VAL F 186 1555 1555 1.33
LINK C ILE F 302 N MSE F 303 1555 1555 1.33
LINK C MSE F 303 N ILE F 304 1555 1555 1.34
CRYST1 201.663 116.547 177.158 90.00 112.19 90.00 C 1 2 1 24
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 0.004959 0.000000 0.002022 0.00000
SCALE2 0.000000 0.008580 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006096 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
