HEADER CHAPERONE/TRANSCRIPTION INHIBITOR 04-DEC-09 3KXY
TITLE CRYSTAL STRUCTURE OF THE EXSC-EXSE COMPLEX
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: EXOENZYME S SYNTHESIS PROTEIN C;
COMPND 3 CHAIN: A, B, C, D, E, F, G, H, I, J, K, L;
COMPND 4 FRAGMENT: SEQUENCE DATBASE RESIDUES 1-133;
COMPND 5 ENGINEERED: YES;
COMPND 6 MUTATION: YES;
COMPND 7 MOL_ID: 2;
COMPND 8 MOLECULE: EXSE;
COMPND 9 CHAIN: T, U, V, W, X, Y;
COMPND 10 FRAGMENT: SEQUENCE DATABASE RESIDUES 16-81;
COMPND 11 ENGINEERED: YES;
COMPND 12 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: PSEUDOMONAS AERUGINOSA;
SOURCE 3 ORGANISM_TAXID: 287;
SOURCE 4 GENE: EXSC, PA1710;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)CODONPLUS RIL;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: HISMBP GATEWAY DEST;
SOURCE 10 MOL_ID: 2;
SOURCE 11 ORGANISM_SCIENTIFIC: PSEUDOMONAS AERUGINOSA;
SOURCE 12 ORGANISM_TAXID: 287;
SOURCE 13 GENE: EXSE, PA1711;
SOURCE 14 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 15 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 16 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)CODONPLUS RIL;
SOURCE 17 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 18 EXPRESSION_SYSTEM_PLASMID: HISMBP GATEWAY DEST
KEYWDS TYPE-THREE SECRETION SYSTEM, TTSS, T3SS, CHAPERONE-EFFECTOR COMPLEX,
KEYWDS 2 CHAPERONE, EFFECTOR, CHAPERONE-TRANSCRIPTION INHIBITOR COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR N.J.VOGELAAR,H.H.ROBINSON,F.D.SCHUBOT
REVDAT 4 21-FEB-24 3KXY 1 SEQADV
REVDAT 3 01-NOV-17 3KXY 1 REMARK
REVDAT 2 11-AUG-10 3KXY 1 JRNL
REVDAT 1 30-JUN-10 3KXY 0
JRNL AUTH N.J.VOGELAAR,X.JING,H.H.ROBINSON,F.D.SCHUBOT
JRNL TITL ANALYSIS OF THE CRYSTAL STRUCTURE OF THE EXSC.EXSE COMPLEX
JRNL TITL 2 REVEALS DISTINCTIVE BINDING INTERACTIONS OF THE PSEUDOMONAS
JRNL TITL 3 AERUGINOSA TYPE III SECRETION CHAPERONE EXSC WITH EXSE AND
JRNL TITL 4 EXSD.
JRNL REF BIOCHEMISTRY V. 49 5870 2010
JRNL REFN ISSN 0006-2960
JRNL PMID 20536183
JRNL DOI 10.1021/BI100432E
REMARK 2
REMARK 2 RESOLUTION. 2.80 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.5_2
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 : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.80
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 30.00
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 0.110
REMARK 3 COMPLETENESS FOR RANGE (%) : 89.2
REMARK 3 NUMBER OF REFLECTIONS : 60940
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.219
REMARK 3 R VALUE (WORKING SET) : 0.217
REMARK 3 FREE R VALUE : 0.257
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 3.280
REMARK 3 FREE R VALUE TEST SET COUNT : 1999
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 30.0017 - 6.7332 0.99 4939 166 0.2112 0.2374
REMARK 3 2 6.7332 - 5.3542 0.97 4652 159 0.2269 0.2613
REMARK 3 3 5.3542 - 4.6803 0.97 4630 157 0.1774 0.2343
REMARK 3 4 4.6803 - 4.2537 0.98 4615 157 0.1703 0.1858
REMARK 3 5 4.2537 - 3.9495 0.96 4507 152 0.1841 0.2425
REMARK 3 6 3.9495 - 3.7171 0.94 4427 151 0.1976 0.2583
REMARK 3 7 3.7171 - 3.5313 0.93 4369 147 0.2182 0.2890
REMARK 3 8 3.5313 - 3.3778 0.91 4257 145 0.2215 0.2369
REMARK 3 9 3.3778 - 3.2479 0.91 4289 146 0.2340 0.2633
REMARK 3 10 3.2479 - 3.1359 0.89 4155 140 0.2381 0.2713
REMARK 3 11 3.1359 - 3.0380 0.85 3959 135 0.2591 0.3183
REMARK 3 12 3.0380 - 2.9512 0.79 3669 124 0.2706 0.3406
REMARK 3 13 2.9512 - 2.8736 0.73 3403 116 0.3078 0.3433
REMARK 3 14 2.8736 - 2.8035 0.66 3070 104 0.3175 0.3676
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.11
REMARK 3 SHRINKAGE RADIUS : 0.90
REMARK 3 K_SOL : 0.30
REMARK 3 B_SOL : 37.90
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.340
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 26.860
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -8.22310
REMARK 3 B22 (A**2) : 19.33460
REMARK 3 B33 (A**2) : -11.11160
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 TWINNING INFORMATION.
REMARK 3 FRACTION: NULL
REMARK 3 OPERATOR: NULL
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : 0.002 15171
REMARK 3 ANGLE : 0.477 20508
REMARK 3 CHIRALITY : 0.034 2348
REMARK 3 PLANARITY : 0.001 2679
REMARK 3 DIHEDRAL : 12.217 5493
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 18
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN A
REMARK 3 ORIGIN FOR THE GROUP (A): -39.3519 33.6498 -16.4294
REMARK 3 T TENSOR
REMARK 3 T11: 0.0549 T22: 0.3229
REMARK 3 T33: 0.2662 T12: 0.0286
REMARK 3 T13: 0.0182 T23: 0.0602
REMARK 3 L TENSOR
REMARK 3 L11: 0.8313 L22: 2.6008
REMARK 3 L33: 2.9768 L12: -0.0512
REMARK 3 L13: 0.9542 L23: 0.2055
REMARK 3 S TENSOR
REMARK 3 S11: 0.0902 S12: 0.0074 S13: -0.0609
REMARK 3 S21: -0.0034 S22: -0.2424 S23: -0.1731
REMARK 3 S31: 0.1221 S32: -0.0067 S33: 0.1472
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN B
REMARK 3 ORIGIN FOR THE GROUP (A): -24.3615 50.8421 -14.4998
REMARK 3 T TENSOR
REMARK 3 T11: 0.2599 T22: 0.4014
REMARK 3 T33: 0.5753 T12: 0.0070
REMARK 3 T13: -0.0811 T23: 0.1328
REMARK 3 L TENSOR
REMARK 3 L11: 4.9558 L22: 1.5407
REMARK 3 L33: 1.8272 L12: 2.0629
REMARK 3 L13: -0.2512 L23: -0.9628
REMARK 3 S TENSOR
REMARK 3 S11: -0.0270 S12: -0.0698 S13: 0.9009
REMARK 3 S21: -0.0272 S22: -0.1072 S23: 0.0779
REMARK 3 S31: -0.0632 S32: 0.3512 S33: 0.1811
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN C
REMARK 3 ORIGIN FOR THE GROUP (A): -36.0058 10.6043 -50.1647
REMARK 3 T TENSOR
REMARK 3 T11: 0.3450 T22: 0.3714
REMARK 3 T33: 0.2578 T12: 0.1466
REMARK 3 T13: -0.1340 T23: -0.1387
REMARK 3 L TENSOR
REMARK 3 L11: 2.1042 L22: 0.8755
REMARK 3 L33: 3.5372 L12: -0.1003
REMARK 3 L13: -0.3513 L23: -0.2184
REMARK 3 S TENSOR
REMARK 3 S11: 0.2416 S12: 0.5498 S13: 0.0783
REMARK 3 S21: -0.2789 S22: 0.0003 S23: 0.1601
REMARK 3 S31: -0.1447 S32: 0.0973 S33: -0.1469
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN D
REMARK 3 ORIGIN FOR THE GROUP (A): -26.2957 -4.5864 -65.3119
REMARK 3 T TENSOR
REMARK 3 T11: 0.4798 T22: 0.6478
REMARK 3 T33: 0.2897 T12: 0.1568
REMARK 3 T13: -0.0225 T23: -0.1607
REMARK 3 L TENSOR
REMARK 3 L11: 1.9248 L22: 5.3715
REMARK 3 L33: 1.3077 L12: -0.9546
REMARK 3 L13: 0.1438 L23: 1.9080
REMARK 3 S TENSOR
REMARK 3 S11: -0.2083 S12: 0.1047 S13: -0.1314
REMARK 3 S21: 0.1107 S22: 0.1307 S23: -0.1814
REMARK 3 S31: 0.1086 S32: -0.0667 S33: 0.0113
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: CHAIN E
REMARK 3 ORIGIN FOR THE GROUP (A): -53.5895 -4.7188 -16.6887
REMARK 3 T TENSOR
REMARK 3 T11: 0.2183 T22: 0.1579
REMARK 3 T33: 0.4856 T12: -0.0613
REMARK 3 T13: -0.1151 T23: 0.0631
REMARK 3 L TENSOR
REMARK 3 L11: 3.8913 L22: 2.6849
REMARK 3 L33: 2.2614 L12: -0.0926
REMARK 3 L13: -1.2607 L23: 1.0026
REMARK 3 S TENSOR
REMARK 3 S11: 0.0196 S12: -0.1014 S13: -0.4314
REMARK 3 S21: 0.1569 S22: 0.0717 S23: 0.3313
REMARK 3 S31: 0.1550 S32: -0.3419 S33: -0.0833
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: CHAIN F
REMARK 3 ORIGIN FOR THE GROUP (A): -54.3956 -15.5271 4.0140
REMARK 3 T TENSOR
REMARK 3 T11: 0.9269 T22: 0.6690
REMARK 3 T33: 1.1296 T12: -0.0927
REMARK 3 T13: 0.1337 T23: 0.2123
REMARK 3 L TENSOR
REMARK 3 L11: 1.7123 L22: 0.7884
REMARK 3 L33: 3.5104 L12: -0.1588
REMARK 3 L13: 0.4160 L23: 2.2866
REMARK 3 S TENSOR
REMARK 3 S11: -0.2189 S12: -0.2722 S13: 0.3177
REMARK 3 S21: 1.0165 S22: 0.3387 S23: 0.7339
REMARK 3 S31: 1.0428 S32: -0.1647 S33: -0.0877
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: CHAIN G
REMARK 3 ORIGIN FOR THE GROUP (A): -21.2216 15.9874 0.9621
REMARK 3 T TENSOR
REMARK 3 T11: 0.1345 T22: 0.2941
REMARK 3 T33: 0.2985 T12: 0.0235
REMARK 3 T13: -0.0447 T23: 0.0972
REMARK 3 L TENSOR
REMARK 3 L11: 1.0749 L22: 3.2188
REMARK 3 L33: 2.8153 L12: -0.5358
REMARK 3 L13: -0.0705 L23: 0.7239
REMARK 3 S TENSOR
REMARK 3 S11: -0.0086 S12: 0.2779 S13: -0.0348
REMARK 3 S21: 0.0614 S22: 0.1528 S23: 0.1307
REMARK 3 S31: 0.1559 S32: 0.0010 S33: -0.1571
REMARK 3 TLS GROUP : 8
REMARK 3 SELECTION: CHAIN H
REMARK 3 ORIGIN FOR THE GROUP (A): -34.8992 18.6699 19.1996
REMARK 3 T TENSOR
REMARK 3 T11: 0.1344 T22: 0.3739
REMARK 3 T33: 0.2417 T12: 0.0410
REMARK 3 T13: 0.0388 T23: 0.0823
REMARK 3 L TENSOR
REMARK 3 L11: 3.6331 L22: 1.5481
REMARK 3 L33: 1.7500 L12: 0.3128
REMARK 3 L13: -0.9569 L23: -0.6452
REMARK 3 S TENSOR
REMARK 3 S11: 0.0082 S12: -0.7200 S13: 0.0552
REMARK 3 S21: 0.0631 S22: 0.0624 S23: 0.1850
REMARK 3 S31: 0.1071 S32: -0.1105 S33: -0.0869
REMARK 3 TLS GROUP : 9
REMARK 3 SELECTION: CHAIN I
REMARK 3 ORIGIN FOR THE GROUP (A): -26.4363 -17.9853 -21.3981
REMARK 3 T TENSOR
REMARK 3 T11: 0.6954 T22: 0.3678
REMARK 3 T33: 0.6754 T12: 0.0721
REMARK 3 T13: -0.2209 T23: -0.1241
REMARK 3 L TENSOR
REMARK 3 L11: 2.5372 L22: 0.9045
REMARK 3 L33: 0.4088 L12: 0.8178
REMARK 3 L13: -0.5956 L23: -0.6322
REMARK 3 S TENSOR
REMARK 3 S11: 0.1925 S12: 0.0516 S13: -0.7327
REMARK 3 S21: 0.0905 S22: 0.0593 S23: 0.0151
REMARK 3 S31: 0.5419 S32: 0.1627 S33: -0.2355
REMARK 3 TLS GROUP : 10
REMARK 3 SELECTION: CHAIN J
REMARK 3 ORIGIN FOR THE GROUP (A): -37.2866 -33.0570 -36.2393
REMARK 3 T TENSOR
REMARK 3 T11: 1.0018 T22: 0.5289
REMARK 3 T33: 1.0205 T12: -0.0859
REMARK 3 T13: -0.3452 T23: -0.0334
REMARK 3 L TENSOR
REMARK 3 L11: 0.7701 L22: 2.0450
REMARK 3 L33: 4.7919 L12: -0.1748
REMARK 3 L13: 1.1803 L23: 1.5014
REMARK 3 S TENSOR
REMARK 3 S11: -0.0872 S12: 0.3984 S13: -0.6450
REMARK 3 S21: -0.0192 S22: 0.3028 S23: -0.4732
REMARK 3 S31: 0.0820 S32: -0.4222 S33: -0.1802
REMARK 3 TLS GROUP : 11
REMARK 3 SELECTION: CHAIN K
REMARK 3 ORIGIN FOR THE GROUP (A): -8.1995 14.5616 -37.9348
REMARK 3 T TENSOR
REMARK 3 T11: 0.3509 T22: 0.8372
REMARK 3 T33: 0.2518 T12: 0.0459
REMARK 3 T13: -0.0166 T23: -0.1420
REMARK 3 L TENSOR
REMARK 3 L11: 2.1353 L22: 1.8285
REMARK 3 L33: 1.4874 L12: 1.3960
REMARK 3 L13: -0.3525 L23: 0.3430
REMARK 3 S TENSOR
REMARK 3 S11: -0.0030 S12: 0.5375 S13: -0.0419
REMARK 3 S21: -0.3412 S22: 0.1629 S23: -0.1357
REMARK 3 S31: -0.3100 S32: 1.0367 S33: -0.1592
REMARK 3 TLS GROUP : 12
REMARK 3 SELECTION: CHAIN L
REMARK 3 ORIGIN FOR THE GROUP (A): -5.7945 34.4395 -48.5339
REMARK 3 T TENSOR
REMARK 3 T11: 0.7195 T22: 1.2149
REMARK 3 T33: 0.5446 T12: -0.1337
REMARK 3 T13: 0.1661 T23: 0.0364
REMARK 3 L TENSOR
REMARK 3 L11: 1.1693 L22: 4.5292
REMARK 3 L33: -0.0732 L12: -0.8266
REMARK 3 L13: 0.1647 L23: 0.1983
REMARK 3 S TENSOR
REMARK 3 S11: 0.0010 S12: 0.3548 S13: 0.3238
REMARK 3 S21: -0.9611 S22: -0.2665 S23: -0.1333
REMARK 3 S31: -0.3943 S32: 0.4644 S33: 0.2106
REMARK 3 TLS GROUP : 13
REMARK 3 SELECTION: CHAIN T
REMARK 3 ORIGIN FOR THE GROUP (A): -40.9578 47.1642 -18.5237
REMARK 3 T TENSOR
REMARK 3 T11: 0.1695 T22: 0.3319
REMARK 3 T33: 0.4740 T12: 0.1365
REMARK 3 T13: -0.0583 T23: 0.2911
REMARK 3 L TENSOR
REMARK 3 L11: 2.4165 L22: 3.2980
REMARK 3 L33: 0.1882 L12: 1.6253
REMARK 3 L13: -1.0484 L23: 0.7587
REMARK 3 S TENSOR
REMARK 3 S11: 0.3243 S12: 0.2861 S13: 0.8771
REMARK 3 S21: 0.0216 S22: -0.2041 S23: 0.9622
REMARK 3 S31: -0.0258 S32: -0.0984 S33: -0.1651
REMARK 3 TLS GROUP : 14
REMARK 3 SELECTION: CHAIN U
REMARK 3 ORIGIN FOR THE GROUP (A): -39.2570 5.9230 -65.1769
REMARK 3 T TENSOR
REMARK 3 T11: 0.3305 T22: 0.5869
REMARK 3 T33: 0.3024 T12: 0.1854
REMARK 3 T13: -0.3805 T23: -0.1555
REMARK 3 L TENSOR
REMARK 3 L11: 0.9172 L22: 0.5671
REMARK 3 L33: 2.6988 L12: 0.6028
REMARK 3 L13: -1.4739 L23: -0.4649
REMARK 3 S TENSOR
REMARK 3 S11: -0.1691 S12: 0.4500 S13: -0.0958
REMARK 3 S21: -0.3328 S22: -0.0070 S23: 0.4981
REMARK 3 S31: -0.6644 S32: -0.3028 S33: 0.1563
REMARK 3 TLS GROUP : 15
REMARK 3 SELECTION: CHAIN V
REMARK 3 ORIGIN FOR THE GROUP (A): -58.5755 -5.8600 -11.0171
REMARK 3 T TENSOR
REMARK 3 T11: 0.1823 T22: 0.2388
REMARK 3 T33: 0.8980 T12: 0.2358
REMARK 3 T13: 0.1365 T23: -0.0555
REMARK 3 L TENSOR
REMARK 3 L11: 0.6459 L22: 2.1201
REMARK 3 L33: 3.2274 L12: 1.6162
REMARK 3 L13: -0.1392 L23: 0.0130
REMARK 3 S TENSOR
REMARK 3 S11: -0.3970 S12: 0.3234 S13: -0.0653
REMARK 3 S21: -0.2102 S22: 0.0948 S23: 0.6421
REMARK 3 S31: 0.4116 S32: -0.5632 S33: 0.2494
REMARK 3 TLS GROUP : 16
REMARK 3 SELECTION: CHAIN W
REMARK 3 ORIGIN FOR THE GROUP (A): -18.4198 14.6750 15.9971
REMARK 3 T TENSOR
REMARK 3 T11: 0.1349 T22: 0.3823
REMARK 3 T33: 0.3338 T12: 0.0076
REMARK 3 T13: -0.0525 T23: 0.1361
REMARK 3 L TENSOR
REMARK 3 L11: 0.3231 L22: 1.2012
REMARK 3 L33: 4.4789 L12: 0.2696
REMARK 3 L13: 0.7685 L23: 0.9342
REMARK 3 S TENSOR
REMARK 3 S11: 0.0470 S12: -0.0839 S13: -0.1732
REMARK 3 S21: 0.1249 S22: -0.0420 S23: 0.1406
REMARK 3 S31: 0.0857 S32: 0.4471 S33: 0.0034
REMARK 3 TLS GROUP : 17
REMARK 3 SELECTION: CHAIN X
REMARK 3 ORIGIN FOR THE GROUP (A): -24.8778 -25.6564 -26.3548
REMARK 3 T TENSOR
REMARK 3 T11: 0.4783 T22: 0.4511
REMARK 3 T33: 0.7744 T12: 0.3261
REMARK 3 T13: -0.1762 T23: -0.2059
REMARK 3 L TENSOR
REMARK 3 L11: 0.8157 L22: 3.2856
REMARK 3 L33: 1.8788 L12: 0.7865
REMARK 3 L13: -1.0491 L23: -0.1664
REMARK 3 S TENSOR
REMARK 3 S11: -0.3907 S12: 0.0243 S13: -0.2873
REMARK 3 S21: -0.2140 S22: 0.3778 S23: -0.2557
REMARK 3 S31: -0.0171 S32: 0.5181 S33: -0.0381
REMARK 3 TLS GROUP : 18
REMARK 3 SELECTION: CHAIN Y
REMARK 3 ORIGIN FOR THE GROUP (A): 0.5478 23.8416 -40.7665
REMARK 3 T TENSOR
REMARK 3 T11: 0.2513 T22: 0.9973
REMARK 3 T33: 0.5607 T12: -0.0730
REMARK 3 T13: -0.1951 T23: 0.0203
REMARK 3 L TENSOR
REMARK 3 L11: 1.7180 L22: 3.4529
REMARK 3 L33: 2.5954 L12: 1.3519
REMARK 3 L13: -1.1235 L23: 0.4187
REMARK 3 S TENSOR
REMARK 3 S11: -0.4153 S12: 0.9657 S13: -0.2602
REMARK 3 S21: -0.2495 S22: 0.4213 S23: -0.8613
REMARK 3 S31: -0.2149 S32: 0.3605 S33: 0.0052
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 3KXY COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 08-JAN-10.
REMARK 100 THE DEPOSITION ID IS D_1000056586.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 03-OCT-07
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 9.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : NSLS
REMARK 200 BEAMLINE : X29A
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0809
REMARK 200 MONOCHROMATOR : SI(1 1 1)
REMARK 200 OPTICS : VERTICALLY-FOCUSING MIRROR AND
REMARK 200 HORIZONTALLY-FOCUSING
REMARK 200 MONOCHROMATOR
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315R
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO, HKL-2000
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK, HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 66241
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.800
REMARK 200 RESOLUTION RANGE LOW (A) : 30.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 97.0
REMARK 200 DATA REDUNDANCY : 10.40
REMARK 200 R MERGE (I) : 0.10700
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 7.8000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.80
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.90
REMARK 200 COMPLETENESS FOR SHELL (%) : 83.6
REMARK 200 DATA REDUNDANCY IN SHELL : 5.30
REMARK 200 R MERGE FOR SHELL (I) : 0.59500
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.600
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHENIX (PHASER)
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 60.20
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.09
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.0M SODIUM POTASSIUM TARTRATE, 0.2M
REMARK 280 LITHIUM SULFATE, 0.1M CHES, PH 9.0, VAPOR DIFFUSION, HANGING
REMARK 280 DROP, TEMPERATURE 288K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
REMARK 290 4555 X+1/2,-Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 48.15650
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 114.06300
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 62.48650
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 114.06300
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 48.15650
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 62.48650
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: TRIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 7480 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 15920 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -16.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: G, H, W
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: TRIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 7400 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 15560 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -12.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, T
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: TRIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 6980 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 16490 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -22.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D, U
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: TRIMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: E, F, V
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: TRIMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: I, J, X
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 6
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TRIMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: K, L, Y
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 B 133
REMARK 465 GLY T 16
REMARK 465 CYS D 131
REMARK 465 ALA D 132
REMARK 465 SER D 133
REMARK 465 ALA U 53
REMARK 465 GLY U 54
REMARK 465 ASP U 55
REMARK 465 PRO U 56
REMARK 465 ARG U 57
REMARK 465 SER U 58
REMARK 465 MET F 1
REMARK 465 GLY V 16
REMARK 465 MET H 1
REMARK 465 ALA H 132
REMARK 465 SER H 133
REMARK 465 GLY W 16
REMARK 465 SER W 40
REMARK 465 VAL W 41
REMARK 465 ALA W 42
REMARK 465 GLY W 43
REMARK 465 LEU W 44
REMARK 465 ALA W 45
REMARK 465 ARG W 46
REMARK 465 TRP W 47
REMARK 465 LEU W 48
REMARK 465 ALA W 49
REMARK 465 ARG W 50
REMARK 465 ASN W 51
REMARK 465 VAL W 52
REMARK 465 ALA W 53
REMARK 465 GLY W 54
REMARK 465 ASP W 55
REMARK 465 PRO W 56
REMARK 465 ARG W 57
REMARK 465 SER W 58
REMARK 465 GLU W 59
REMARK 465 GLN W 60
REMARK 465 ALA W 61
REMARK 465 LEU W 62
REMARK 465 GLN W 63
REMARK 465 ARG W 64
REMARK 465 LEU W 65
REMARK 465 ALA W 66
REMARK 465 ASP W 67
REMARK 465 MET J 1
REMARK 465 CYS J 131
REMARK 465 ALA J 132
REMARK 465 SER J 133
REMARK 465 GLY X 16
REMARK 465 SER X 40
REMARK 465 VAL X 41
REMARK 465 ALA X 42
REMARK 465 GLY X 43
REMARK 465 LEU X 44
REMARK 465 ALA X 45
REMARK 465 ARG X 46
REMARK 465 TRP X 47
REMARK 465 LEU X 48
REMARK 465 ALA X 49
REMARK 465 ARG X 50
REMARK 465 ASN X 51
REMARK 465 VAL X 52
REMARK 465 ALA X 53
REMARK 465 GLY X 54
REMARK 465 ASP X 55
REMARK 465 PRO X 56
REMARK 465 ARG X 57
REMARK 465 SER X 58
REMARK 465 GLU X 59
REMARK 465 GLN X 60
REMARK 465 ALA X 61
REMARK 465 LEU X 62
REMARK 465 GLN X 63
REMARK 465 ARG X 64
REMARK 465 LEU X 65
REMARK 465 MET L 1
REMARK 465 ALA L 132
REMARK 465 SER L 133
REMARK 465 GLY Y 35
REMARK 465 GLU Y 36
REMARK 465 ASP Y 37
REMARK 465 ARG Y 38
REMARK 465 SER Y 39
REMARK 465 SER Y 40
REMARK 465 VAL Y 41
REMARK 465 ALA Y 42
REMARK 465 GLY Y 43
REMARK 465 LEU Y 44
REMARK 465 ALA Y 45
REMARK 465 ARG Y 46
REMARK 465 TRP Y 47
REMARK 465 LEU Y 48
REMARK 465 ALA Y 49
REMARK 465 ARG Y 50
REMARK 465 ASN Y 51
REMARK 465 VAL Y 52
REMARK 465 ALA Y 53
REMARK 465 GLY Y 54
REMARK 465 ASP Y 55
REMARK 465 PRO Y 56
REMARK 465 ARG Y 57
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 ASP A 36 15.68 56.31
REMARK 500 GLN A 38 -43.55 -139.35
REMARK 500 VAL A 58 -62.39 -105.06
REMARK 500 GLN B 38 -54.48 -126.50
REMARK 500 VAL T 52 -76.57 -107.35
REMARK 500 ASP T 55 117.67 -161.26
REMARK 500 GLU C 37 16.71 57.84
REMARK 500 GLN C 38 -61.34 -128.58
REMARK 500 GLN D 38 -58.69 -130.88
REMARK 500 VAL D 58 -65.77 -97.35
REMARK 500 GLN E 38 -41.79 -136.56
REMARK 500 LEU E 106 98.71 -68.89
REMARK 500 PRO E 130 159.19 -45.99
REMARK 500 ASP F 26 -173.73 -67.38
REMARK 500 GLU F 37 16.22 56.56
REMARK 500 GLN F 38 -6.80 -147.51
REMARK 500 VAL F 58 -76.49 -98.68
REMARK 500 ASP V 55 100.04 -161.94
REMARK 500 VAL G 58 -73.77 -96.94
REMARK 500 VAL H 58 -80.04 -106.79
REMARK 500 ASP I 26 -163.65 -74.50
REMARK 500 GLN I 38 -58.43 -135.30
REMARK 500 VAL I 58 -73.71 -75.77
REMARK 500 LEU I 106 89.38 -69.59
REMARK 500 GLN J 38 -54.78 -142.14
REMARK 500 VAL J 58 -79.43 -101.05
REMARK 500 ASP X 69 55.37 -91.55
REMARK 500 LEU K 23 106.58 -162.78
REMARK 500 ASP K 36 19.83 54.39
REMARK 500 GLN K 38 -66.95 -121.31
REMARK 500 VAL K 58 -68.57 -98.77
REMARK 500 ASP L 26 -167.74 -79.50
REMARK 500 GLU L 37 18.37 56.65
REMARK 500 LEU L 44 104.00 -165.97
REMARK 500 VAL L 58 -72.77 -102.83
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1TTW RELATED DB: PDB
REMARK 900 SYCH-YSCM2 TTSS CHAPERONE-EFFECTOR COMPLEX
REMARK 900 RELATED ID: 1XKP RELATED DB: PDB
REMARK 900 SYCN-YSCB-YOPN TTSS CHAPERONE-EFFECTOR COMPLEX
REMARK 900 RELATED ID: 1L2W RELATED DB: PDB
REMARK 900 SYCE-YOPE TTSS CHAPERONE-EFFECTOR COMPLEX
REMARK 900 RELATED ID: 1JYO RELATED DB: PDB
REMARK 900 SICP-SPTP TTSS CHAPERONE-EFFECTOR COMPLEX
REMARK 900 RELATED ID: 2FM8 RELATED DB: PDB
REMARK 900 INVB-SIPA TTSS CHAPERONE-EFFECTOR COMPLEX
DBREF 3KXY A 1 133 UNP P26995 EXSC_PSEAE 1 133
DBREF 3KXY B 1 133 UNP P26995 EXSC_PSEAE 1 133
DBREF 3KXY T 16 81 UNP Q9I322 Q9I322_PSEAE 16 81
DBREF 3KXY C 1 133 UNP P26995 EXSC_PSEAE 1 133
DBREF 3KXY D 1 133 UNP P26995 EXSC_PSEAE 1 133
DBREF 3KXY U 16 81 UNP Q9I322 Q9I322_PSEAE 16 81
DBREF 3KXY E 1 133 UNP P26995 EXSC_PSEAE 1 133
DBREF 3KXY F 1 133 UNP P26995 EXSC_PSEAE 1 133
DBREF 3KXY V 16 81 UNP Q9I322 Q9I322_PSEAE 16 81
DBREF 3KXY G 1 133 UNP P26995 EXSC_PSEAE 1 133
DBREF 3KXY H 1 133 UNP P26995 EXSC_PSEAE 1 133
DBREF 3KXY W 16 81 UNP Q9I322 Q9I322_PSEAE 16 81
DBREF 3KXY I 1 133 UNP P26995 EXSC_PSEAE 1 133
DBREF 3KXY J 1 133 UNP P26995 EXSC_PSEAE 1 133
DBREF 3KXY X 16 81 UNP Q9I322 Q9I322_PSEAE 16 81
DBREF 3KXY K 1 133 UNP P26995 EXSC_PSEAE 1 133
DBREF 3KXY L 1 133 UNP P26995 EXSC_PSEAE 1 133
DBREF 3KXY Y 16 81 UNP Q9I322 Q9I322_PSEAE 16 81
SEQADV 3KXY VAL A 59 UNP P26995 ALA 59 ENGINEERED MUTATION
SEQADV 3KXY ALA A 132 UNP P26995 ASP 132 ENGINEERED MUTATION
SEQADV 3KXY VAL B 59 UNP P26995 ALA 59 ENGINEERED MUTATION
SEQADV 3KXY ALA B 132 UNP P26995 ASP 132 ENGINEERED MUTATION
SEQADV 3KXY THR T 17 UNP Q9I322 ALA 17 ENGINEERED MUTATION
SEQADV 3KXY VAL C 59 UNP P26995 ALA 59 ENGINEERED MUTATION
SEQADV 3KXY ALA C 132 UNP P26995 ASP 132 ENGINEERED MUTATION
SEQADV 3KXY VAL D 59 UNP P26995 ALA 59 ENGINEERED MUTATION
SEQADV 3KXY ALA D 132 UNP P26995 ASP 132 ENGINEERED MUTATION
SEQADV 3KXY THR U 17 UNP Q9I322 ALA 17 ENGINEERED MUTATION
SEQADV 3KXY VAL E 59 UNP P26995 ALA 59 ENGINEERED MUTATION
SEQADV 3KXY ALA E 132 UNP P26995 ASP 132 ENGINEERED MUTATION
SEQADV 3KXY VAL F 59 UNP P26995 ALA 59 ENGINEERED MUTATION
SEQADV 3KXY ALA F 132 UNP P26995 ASP 132 ENGINEERED MUTATION
SEQADV 3KXY THR V 17 UNP Q9I322 ALA 17 ENGINEERED MUTATION
SEQADV 3KXY VAL G 59 UNP P26995 ALA 59 ENGINEERED MUTATION
SEQADV 3KXY ALA G 132 UNP P26995 ASP 132 ENGINEERED MUTATION
SEQADV 3KXY VAL H 59 UNP P26995 ALA 59 ENGINEERED MUTATION
SEQADV 3KXY ALA H 132 UNP P26995 ASP 132 ENGINEERED MUTATION
SEQADV 3KXY THR W 17 UNP Q9I322 ALA 17 ENGINEERED MUTATION
SEQADV 3KXY VAL I 59 UNP P26995 ALA 59 ENGINEERED MUTATION
SEQADV 3KXY ALA I 132 UNP P26995 ASP 132 ENGINEERED MUTATION
SEQADV 3KXY VAL J 59 UNP P26995 ALA 59 ENGINEERED MUTATION
SEQADV 3KXY ALA J 132 UNP P26995 ASP 132 ENGINEERED MUTATION
SEQADV 3KXY THR X 17 UNP Q9I322 ALA 17 ENGINEERED MUTATION
SEQADV 3KXY VAL K 59 UNP P26995 ALA 59 ENGINEERED MUTATION
SEQADV 3KXY ALA K 132 UNP P26995 ASP 132 ENGINEERED MUTATION
SEQADV 3KXY VAL L 59 UNP P26995 ALA 59 ENGINEERED MUTATION
SEQADV 3KXY ALA L 132 UNP P26995 ASP 132 ENGINEERED MUTATION
SEQADV 3KXY THR Y 17 UNP Q9I322 ALA 17 ENGINEERED MUTATION
SEQRES 1 A 133 MET ASP LEU THR SER LYS VAL ASN ARG LEU LEU ALA GLU
SEQRES 2 A 133 PHE ALA GLY ARG ILE GLY LEU PRO SER LEU SER LEU ASP
SEQRES 3 A 133 GLU GLU GLY MET ALA SER LEU LEU PHE ASP GLU GLN VAL
SEQRES 4 A 133 GLY VAL THR LEU LEU LEU LEU ALA GLU ARG GLU ARG LEU
SEQRES 5 A 133 LEU LEU GLU ALA ASP VAL VAL GLY ILE ASP VAL LEU GLY
SEQRES 6 A 133 GLU GLY ILE PHE ARG GLN LEU ALA SER PHE ASN ARG HIS
SEQRES 7 A 133 TRP HIS ARG PHE ASP LEU HIS PHE GLY PHE ASP GLU LEU
SEQRES 8 A 133 THR GLY LYS VAL GLN LEU TYR ALA GLN ILE LEU ALA ALA
SEQRES 9 A 133 GLN LEU THR LEU GLU CYS PHE GLU ALA THR LEU ALA ASN
SEQRES 10 A 133 LEU LEU ASP HIS ALA GLU PHE TRP GLN ARG LEU LEU PRO
SEQRES 11 A 133 CYS ALA SER
SEQRES 1 B 133 MET ASP LEU THR SER LYS VAL ASN ARG LEU LEU ALA GLU
SEQRES 2 B 133 PHE ALA GLY ARG ILE GLY LEU PRO SER LEU SER LEU ASP
SEQRES 3 B 133 GLU GLU GLY MET ALA SER LEU LEU PHE ASP GLU GLN VAL
SEQRES 4 B 133 GLY VAL THR LEU LEU LEU LEU ALA GLU ARG GLU ARG LEU
SEQRES 5 B 133 LEU LEU GLU ALA ASP VAL VAL GLY ILE ASP VAL LEU GLY
SEQRES 6 B 133 GLU GLY ILE PHE ARG GLN LEU ALA SER PHE ASN ARG HIS
SEQRES 7 B 133 TRP HIS ARG PHE ASP LEU HIS PHE GLY PHE ASP GLU LEU
SEQRES 8 B 133 THR GLY LYS VAL GLN LEU TYR ALA GLN ILE LEU ALA ALA
SEQRES 9 B 133 GLN LEU THR LEU GLU CYS PHE GLU ALA THR LEU ALA ASN
SEQRES 10 B 133 LEU LEU ASP HIS ALA GLU PHE TRP GLN ARG LEU LEU PRO
SEQRES 11 B 133 CYS ALA SER
SEQRES 1 T 66 GLY THR GLU ALA VAL GLY HIS PHE GLU GLY ARG SER VAL
SEQRES 2 T 66 THR ARG ALA ALA VAL ARG GLY GLU ASP ARG SER SER VAL
SEQRES 3 T 66 ALA GLY LEU ALA ARG TRP LEU ALA ARG ASN VAL ALA GLY
SEQRES 4 T 66 ASP PRO ARG SER GLU GLN ALA LEU GLN ARG LEU ALA ASP
SEQRES 5 T 66 GLY ASP GLY THR PRO LEU GLU ALA ARG THR VAL ARG ARG
SEQRES 6 T 66 ARG
SEQRES 1 C 133 MET ASP LEU THR SER LYS VAL ASN ARG LEU LEU ALA GLU
SEQRES 2 C 133 PHE ALA GLY ARG ILE GLY LEU PRO SER LEU SER LEU ASP
SEQRES 3 C 133 GLU GLU GLY MET ALA SER LEU LEU PHE ASP GLU GLN VAL
SEQRES 4 C 133 GLY VAL THR LEU LEU LEU LEU ALA GLU ARG GLU ARG LEU
SEQRES 5 C 133 LEU LEU GLU ALA ASP VAL VAL GLY ILE ASP VAL LEU GLY
SEQRES 6 C 133 GLU GLY ILE PHE ARG GLN LEU ALA SER PHE ASN ARG HIS
SEQRES 7 C 133 TRP HIS ARG PHE ASP LEU HIS PHE GLY PHE ASP GLU LEU
SEQRES 8 C 133 THR GLY LYS VAL GLN LEU TYR ALA GLN ILE LEU ALA ALA
SEQRES 9 C 133 GLN LEU THR LEU GLU CYS PHE GLU ALA THR LEU ALA ASN
SEQRES 10 C 133 LEU LEU ASP HIS ALA GLU PHE TRP GLN ARG LEU LEU PRO
SEQRES 11 C 133 CYS ALA SER
SEQRES 1 D 133 MET ASP LEU THR SER LYS VAL ASN ARG LEU LEU ALA GLU
SEQRES 2 D 133 PHE ALA GLY ARG ILE GLY LEU PRO SER LEU SER LEU ASP
SEQRES 3 D 133 GLU GLU GLY MET ALA SER LEU LEU PHE ASP GLU GLN VAL
SEQRES 4 D 133 GLY VAL THR LEU LEU LEU LEU ALA GLU ARG GLU ARG LEU
SEQRES 5 D 133 LEU LEU GLU ALA ASP VAL VAL GLY ILE ASP VAL LEU GLY
SEQRES 6 D 133 GLU GLY ILE PHE ARG GLN LEU ALA SER PHE ASN ARG HIS
SEQRES 7 D 133 TRP HIS ARG PHE ASP LEU HIS PHE GLY PHE ASP GLU LEU
SEQRES 8 D 133 THR GLY LYS VAL GLN LEU TYR ALA GLN ILE LEU ALA ALA
SEQRES 9 D 133 GLN LEU THR LEU GLU CYS PHE GLU ALA THR LEU ALA ASN
SEQRES 10 D 133 LEU LEU ASP HIS ALA GLU PHE TRP GLN ARG LEU LEU PRO
SEQRES 11 D 133 CYS ALA SER
SEQRES 1 U 66 GLY THR GLU ALA VAL GLY HIS PHE GLU GLY ARG SER VAL
SEQRES 2 U 66 THR ARG ALA ALA VAL ARG GLY GLU ASP ARG SER SER VAL
SEQRES 3 U 66 ALA GLY LEU ALA ARG TRP LEU ALA ARG ASN VAL ALA GLY
SEQRES 4 U 66 ASP PRO ARG SER GLU GLN ALA LEU GLN ARG LEU ALA ASP
SEQRES 5 U 66 GLY ASP GLY THR PRO LEU GLU ALA ARG THR VAL ARG ARG
SEQRES 6 U 66 ARG
SEQRES 1 E 133 MET ASP LEU THR SER LYS VAL ASN ARG LEU LEU ALA GLU
SEQRES 2 E 133 PHE ALA GLY ARG ILE GLY LEU PRO SER LEU SER LEU ASP
SEQRES 3 E 133 GLU GLU GLY MET ALA SER LEU LEU PHE ASP GLU GLN VAL
SEQRES 4 E 133 GLY VAL THR LEU LEU LEU LEU ALA GLU ARG GLU ARG LEU
SEQRES 5 E 133 LEU LEU GLU ALA ASP VAL VAL GLY ILE ASP VAL LEU GLY
SEQRES 6 E 133 GLU GLY ILE PHE ARG GLN LEU ALA SER PHE ASN ARG HIS
SEQRES 7 E 133 TRP HIS ARG PHE ASP LEU HIS PHE GLY PHE ASP GLU LEU
SEQRES 8 E 133 THR GLY LYS VAL GLN LEU TYR ALA GLN ILE LEU ALA ALA
SEQRES 9 E 133 GLN LEU THR LEU GLU CYS PHE GLU ALA THR LEU ALA ASN
SEQRES 10 E 133 LEU LEU ASP HIS ALA GLU PHE TRP GLN ARG LEU LEU PRO
SEQRES 11 E 133 CYS ALA SER
SEQRES 1 F 133 MET ASP LEU THR SER LYS VAL ASN ARG LEU LEU ALA GLU
SEQRES 2 F 133 PHE ALA GLY ARG ILE GLY LEU PRO SER LEU SER LEU ASP
SEQRES 3 F 133 GLU GLU GLY MET ALA SER LEU LEU PHE ASP GLU GLN VAL
SEQRES 4 F 133 GLY VAL THR LEU LEU LEU LEU ALA GLU ARG GLU ARG LEU
SEQRES 5 F 133 LEU LEU GLU ALA ASP VAL VAL GLY ILE ASP VAL LEU GLY
SEQRES 6 F 133 GLU GLY ILE PHE ARG GLN LEU ALA SER PHE ASN ARG HIS
SEQRES 7 F 133 TRP HIS ARG PHE ASP LEU HIS PHE GLY PHE ASP GLU LEU
SEQRES 8 F 133 THR GLY LYS VAL GLN LEU TYR ALA GLN ILE LEU ALA ALA
SEQRES 9 F 133 GLN LEU THR LEU GLU CYS PHE GLU ALA THR LEU ALA ASN
SEQRES 10 F 133 LEU LEU ASP HIS ALA GLU PHE TRP GLN ARG LEU LEU PRO
SEQRES 11 F 133 CYS ALA SER
SEQRES 1 V 66 GLY THR GLU ALA VAL GLY HIS PHE GLU GLY ARG SER VAL
SEQRES 2 V 66 THR ARG ALA ALA VAL ARG GLY GLU ASP ARG SER SER VAL
SEQRES 3 V 66 ALA GLY LEU ALA ARG TRP LEU ALA ARG ASN VAL ALA GLY
SEQRES 4 V 66 ASP PRO ARG SER GLU GLN ALA LEU GLN ARG LEU ALA ASP
SEQRES 5 V 66 GLY ASP GLY THR PRO LEU GLU ALA ARG THR VAL ARG ARG
SEQRES 6 V 66 ARG
SEQRES 1 G 133 MET ASP LEU THR SER LYS VAL ASN ARG LEU LEU ALA GLU
SEQRES 2 G 133 PHE ALA GLY ARG ILE GLY LEU PRO SER LEU SER LEU ASP
SEQRES 3 G 133 GLU GLU GLY MET ALA SER LEU LEU PHE ASP GLU GLN VAL
SEQRES 4 G 133 GLY VAL THR LEU LEU LEU LEU ALA GLU ARG GLU ARG LEU
SEQRES 5 G 133 LEU LEU GLU ALA ASP VAL VAL GLY ILE ASP VAL LEU GLY
SEQRES 6 G 133 GLU GLY ILE PHE ARG GLN LEU ALA SER PHE ASN ARG HIS
SEQRES 7 G 133 TRP HIS ARG PHE ASP LEU HIS PHE GLY PHE ASP GLU LEU
SEQRES 8 G 133 THR GLY LYS VAL GLN LEU TYR ALA GLN ILE LEU ALA ALA
SEQRES 9 G 133 GLN LEU THR LEU GLU CYS PHE GLU ALA THR LEU ALA ASN
SEQRES 10 G 133 LEU LEU ASP HIS ALA GLU PHE TRP GLN ARG LEU LEU PRO
SEQRES 11 G 133 CYS ALA SER
SEQRES 1 H 133 MET ASP LEU THR SER LYS VAL ASN ARG LEU LEU ALA GLU
SEQRES 2 H 133 PHE ALA GLY ARG ILE GLY LEU PRO SER LEU SER LEU ASP
SEQRES 3 H 133 GLU GLU GLY MET ALA SER LEU LEU PHE ASP GLU GLN VAL
SEQRES 4 H 133 GLY VAL THR LEU LEU LEU LEU ALA GLU ARG GLU ARG LEU
SEQRES 5 H 133 LEU LEU GLU ALA ASP VAL VAL GLY ILE ASP VAL LEU GLY
SEQRES 6 H 133 GLU GLY ILE PHE ARG GLN LEU ALA SER PHE ASN ARG HIS
SEQRES 7 H 133 TRP HIS ARG PHE ASP LEU HIS PHE GLY PHE ASP GLU LEU
SEQRES 8 H 133 THR GLY LYS VAL GLN LEU TYR ALA GLN ILE LEU ALA ALA
SEQRES 9 H 133 GLN LEU THR LEU GLU CYS PHE GLU ALA THR LEU ALA ASN
SEQRES 10 H 133 LEU LEU ASP HIS ALA GLU PHE TRP GLN ARG LEU LEU PRO
SEQRES 11 H 133 CYS ALA SER
SEQRES 1 W 66 GLY THR GLU ALA VAL GLY HIS PHE GLU GLY ARG SER VAL
SEQRES 2 W 66 THR ARG ALA ALA VAL ARG GLY GLU ASP ARG SER SER VAL
SEQRES 3 W 66 ALA GLY LEU ALA ARG TRP LEU ALA ARG ASN VAL ALA GLY
SEQRES 4 W 66 ASP PRO ARG SER GLU GLN ALA LEU GLN ARG LEU ALA ASP
SEQRES 5 W 66 GLY ASP GLY THR PRO LEU GLU ALA ARG THR VAL ARG ARG
SEQRES 6 W 66 ARG
SEQRES 1 I 133 MET ASP LEU THR SER LYS VAL ASN ARG LEU LEU ALA GLU
SEQRES 2 I 133 PHE ALA GLY ARG ILE GLY LEU PRO SER LEU SER LEU ASP
SEQRES 3 I 133 GLU GLU GLY MET ALA SER LEU LEU PHE ASP GLU GLN VAL
SEQRES 4 I 133 GLY VAL THR LEU LEU LEU LEU ALA GLU ARG GLU ARG LEU
SEQRES 5 I 133 LEU LEU GLU ALA ASP VAL VAL GLY ILE ASP VAL LEU GLY
SEQRES 6 I 133 GLU GLY ILE PHE ARG GLN LEU ALA SER PHE ASN ARG HIS
SEQRES 7 I 133 TRP HIS ARG PHE ASP LEU HIS PHE GLY PHE ASP GLU LEU
SEQRES 8 I 133 THR GLY LYS VAL GLN LEU TYR ALA GLN ILE LEU ALA ALA
SEQRES 9 I 133 GLN LEU THR LEU GLU CYS PHE GLU ALA THR LEU ALA ASN
SEQRES 10 I 133 LEU LEU ASP HIS ALA GLU PHE TRP GLN ARG LEU LEU PRO
SEQRES 11 I 133 CYS ALA SER
SEQRES 1 J 133 MET ASP LEU THR SER LYS VAL ASN ARG LEU LEU ALA GLU
SEQRES 2 J 133 PHE ALA GLY ARG ILE GLY LEU PRO SER LEU SER LEU ASP
SEQRES 3 J 133 GLU GLU GLY MET ALA SER LEU LEU PHE ASP GLU GLN VAL
SEQRES 4 J 133 GLY VAL THR LEU LEU LEU LEU ALA GLU ARG GLU ARG LEU
SEQRES 5 J 133 LEU LEU GLU ALA ASP VAL VAL GLY ILE ASP VAL LEU GLY
SEQRES 6 J 133 GLU GLY ILE PHE ARG GLN LEU ALA SER PHE ASN ARG HIS
SEQRES 7 J 133 TRP HIS ARG PHE ASP LEU HIS PHE GLY PHE ASP GLU LEU
SEQRES 8 J 133 THR GLY LYS VAL GLN LEU TYR ALA GLN ILE LEU ALA ALA
SEQRES 9 J 133 GLN LEU THR LEU GLU CYS PHE GLU ALA THR LEU ALA ASN
SEQRES 10 J 133 LEU LEU ASP HIS ALA GLU PHE TRP GLN ARG LEU LEU PRO
SEQRES 11 J 133 CYS ALA SER
SEQRES 1 X 66 GLY THR GLU ALA VAL GLY HIS PHE GLU GLY ARG SER VAL
SEQRES 2 X 66 THR ARG ALA ALA VAL ARG GLY GLU ASP ARG SER SER VAL
SEQRES 3 X 66 ALA GLY LEU ALA ARG TRP LEU ALA ARG ASN VAL ALA GLY
SEQRES 4 X 66 ASP PRO ARG SER GLU GLN ALA LEU GLN ARG LEU ALA ASP
SEQRES 5 X 66 GLY ASP GLY THR PRO LEU GLU ALA ARG THR VAL ARG ARG
SEQRES 6 X 66 ARG
SEQRES 1 K 133 MET ASP LEU THR SER LYS VAL ASN ARG LEU LEU ALA GLU
SEQRES 2 K 133 PHE ALA GLY ARG ILE GLY LEU PRO SER LEU SER LEU ASP
SEQRES 3 K 133 GLU GLU GLY MET ALA SER LEU LEU PHE ASP GLU GLN VAL
SEQRES 4 K 133 GLY VAL THR LEU LEU LEU LEU ALA GLU ARG GLU ARG LEU
SEQRES 5 K 133 LEU LEU GLU ALA ASP VAL VAL GLY ILE ASP VAL LEU GLY
SEQRES 6 K 133 GLU GLY ILE PHE ARG GLN LEU ALA SER PHE ASN ARG HIS
SEQRES 7 K 133 TRP HIS ARG PHE ASP LEU HIS PHE GLY PHE ASP GLU LEU
SEQRES 8 K 133 THR GLY LYS VAL GLN LEU TYR ALA GLN ILE LEU ALA ALA
SEQRES 9 K 133 GLN LEU THR LEU GLU CYS PHE GLU ALA THR LEU ALA ASN
SEQRES 10 K 133 LEU LEU ASP HIS ALA GLU PHE TRP GLN ARG LEU LEU PRO
SEQRES 11 K 133 CYS ALA SER
SEQRES 1 L 133 MET ASP LEU THR SER LYS VAL ASN ARG LEU LEU ALA GLU
SEQRES 2 L 133 PHE ALA GLY ARG ILE GLY LEU PRO SER LEU SER LEU ASP
SEQRES 3 L 133 GLU GLU GLY MET ALA SER LEU LEU PHE ASP GLU GLN VAL
SEQRES 4 L 133 GLY VAL THR LEU LEU LEU LEU ALA GLU ARG GLU ARG LEU
SEQRES 5 L 133 LEU LEU GLU ALA ASP VAL VAL GLY ILE ASP VAL LEU GLY
SEQRES 6 L 133 GLU GLY ILE PHE ARG GLN LEU ALA SER PHE ASN ARG HIS
SEQRES 7 L 133 TRP HIS ARG PHE ASP LEU HIS PHE GLY PHE ASP GLU LEU
SEQRES 8 L 133 THR GLY LYS VAL GLN LEU TYR ALA GLN ILE LEU ALA ALA
SEQRES 9 L 133 GLN LEU THR LEU GLU CYS PHE GLU ALA THR LEU ALA ASN
SEQRES 10 L 133 LEU LEU ASP HIS ALA GLU PHE TRP GLN ARG LEU LEU PRO
SEQRES 11 L 133 CYS ALA SER
SEQRES 1 Y 66 GLY THR GLU ALA VAL GLY HIS PHE GLU GLY ARG SER VAL
SEQRES 2 Y 66 THR ARG ALA ALA VAL ARG GLY GLU ASP ARG SER SER VAL
SEQRES 3 Y 66 ALA GLY LEU ALA ARG TRP LEU ALA ARG ASN VAL ALA GLY
SEQRES 4 Y 66 ASP PRO ARG SER GLU GLN ALA LEU GLN ARG LEU ALA ASP
SEQRES 5 Y 66 GLY ASP GLY THR PRO LEU GLU ALA ARG THR VAL ARG ARG
SEQRES 6 Y 66 ARG
FORMUL 19 HOH *90(H2 O)
HELIX 1 1 ASP A 2 GLY A 19 1 18
HELIX 2 2 ASP A 62 LEU A 64 5 3
HELIX 3 3 GLY A 67 HIS A 78 1 12
HELIX 4 4 TRP A 79 PHE A 82 5 4
HELIX 5 5 THR A 107 LEU A 129 1 23
HELIX 6 6 MET B 1 GLY B 19 1 19
HELIX 7 7 GLY B 67 HIS B 80 1 14
HELIX 8 8 ARG B 81 ASP B 83 5 3
HELIX 9 9 ALA B 104 LEU B 106 5 3
HELIX 10 10 THR B 107 LEU B 129 1 23
HELIX 11 11 SER T 40 VAL T 52 1 13
HELIX 12 12 ARG T 57 GLY T 68 1 12
HELIX 13 13 PRO T 72 ARG T 76 5 5
HELIX 14 14 ASP C 2 GLY C 19 1 18
HELIX 15 15 ASP C 62 LEU C 64 5 3
HELIX 16 16 ILE C 68 HIS C 78 1 11
HELIX 17 17 TRP C 79 PHE C 82 5 4
HELIX 18 18 ALA C 104 LEU C 106 5 3
HELIX 19 19 THR C 107 LEU C 129 1 23
HELIX 20 20 ASP D 2 GLY D 19 1 18
HELIX 21 21 GLY D 67 HIS D 80 1 14
HELIX 22 22 THR D 107 GLN D 126 1 20
HELIX 23 23 SER U 40 VAL U 52 1 13
HELIX 24 24 GLU U 59 GLY U 68 1 10
HELIX 25 25 PRO U 72 ARG U 76 5 5
HELIX 26 26 ASP E 2 GLY E 19 1 18
HELIX 27 27 ASP E 62 LEU E 64 5 3
HELIX 28 28 GLY E 67 HIS E 78 1 12
HELIX 29 29 TRP E 79 PHE E 82 5 4
HELIX 30 30 THR E 107 LEU E 129 1 23
HELIX 31 31 ASP F 2 GLY F 19 1 18
HELIX 32 32 GLY F 67 HIS F 80 1 14
HELIX 33 33 ARG F 81 ASP F 83 5 3
HELIX 34 34 THR F 107 LEU F 129 1 23
HELIX 35 35 PRO F 130 ALA F 132 5 3
HELIX 36 36 ARG V 34 ARG V 38 5 5
HELIX 37 37 SER V 40 ALA V 53 1 14
HELIX 38 38 ARG V 57 GLY V 68 1 12
HELIX 39 39 PRO V 72 ARG V 76 5 5
HELIX 40 40 ASP G 2 GLY G 19 1 18
HELIX 41 41 ASP G 62 LEU G 64 5 3
HELIX 42 42 GLY G 67 ARG G 77 1 11
HELIX 43 43 HIS G 78 PHE G 82 5 5
HELIX 44 44 THR G 107 LEU G 129 1 23
HELIX 45 45 ASP H 2 GLY H 19 1 18
HELIX 46 46 ASP H 62 LEU H 64 5 3
HELIX 47 47 GLY H 67 TRP H 79 1 13
HELIX 48 48 THR H 107 LEU H 129 1 23
HELIX 49 49 ASP I 2 GLY I 19 1 18
HELIX 50 50 GLY I 67 HIS I 78 1 12
HELIX 51 51 TRP I 79 PHE I 82 5 4
HELIX 52 52 THR I 107 ARG I 127 1 21
HELIX 53 53 ASP J 2 GLY J 19 1 18
HELIX 54 54 ASP J 62 LEU J 64 5 3
HELIX 55 55 GLY J 67 HIS J 80 1 14
HELIX 56 56 ARG J 81 ASP J 83 5 3
HELIX 57 57 THR J 107 LEU J 128 1 22
HELIX 58 58 ASP K 2 GLY K 19 1 18
HELIX 59 59 ASP K 62 LEU K 64 5 3
HELIX 60 60 ILE K 68 ARG K 77 1 10
HELIX 61 61 HIS K 78 PHE K 82 5 5
HELIX 62 62 ALA K 104 LEU K 106 5 3
HELIX 63 63 THR K 107 LEU K 129 1 23
HELIX 64 64 ASP L 2 GLY L 19 1 18
HELIX 65 65 ASP L 62 LEU L 64 5 3
HELIX 66 66 GLY L 67 TRP L 79 1 13
HELIX 67 67 THR L 107 LEU L 129 1 23
HELIX 68 68 SER Y 58 ASP Y 67 1 10
SHEET 1 A 7 HIS A 85 PHE A 88 0
SHEET 2 A 7 LYS A 94 LEU A 102 -1 O GLN A 96 N GLY A 87
SHEET 3 A 7 ARG A 51 GLY A 60 -1 N VAL A 58 O VAL A 95
SHEET 4 A 7 VAL A 39 LEU A 46 -1 N LEU A 44 O LEU A 53
SHEET 5 A 7 MET A 30 PHE A 35 -1 N ALA A 31 O LEU A 43
SHEET 6 A 7 ARG T 26 ALA T 31 -1 O ALA T 31 N SER A 32
SHEET 7 A 7 GLY T 21 PHE T 23 -1 N PHE T 23 O ARG T 26
SHEET 1 B 6 HIS B 85 PHE B 88 0
SHEET 2 B 6 LYS B 94 LEU B 102 -1 O TYR B 98 N HIS B 85
SHEET 3 B 6 ARG B 51 GLY B 60 -1 N LEU B 52 O ILE B 101
SHEET 4 B 6 VAL B 39 LEU B 46 -1 N LEU B 44 O LEU B 53
SHEET 5 B 6 MET B 30 PHE B 35 -1 N ALA B 31 O LEU B 43
SHEET 6 B 6 VAL T 78 ARG T 80 -1 O ARG T 79 N LEU B 34
SHEET 1 C 7 HIS C 85 ASP C 89 0
SHEET 2 C 7 LYS C 94 LEU C 102 -1 O GLN C 96 N GLY C 87
SHEET 3 C 7 ARG C 51 GLY C 60 -1 N LEU C 54 O ALA C 99
SHEET 4 C 7 VAL C 39 LEU C 46 -1 N LEU C 46 O ARG C 51
SHEET 5 C 7 MET C 30 PHE C 35 -1 N PHE C 35 O VAL C 39
SHEET 6 C 7 ARG U 26 ALA U 31 -1 O ALA U 31 N SER C 32
SHEET 7 C 7 GLY U 21 PHE U 23 -1 N PHE U 23 O ARG U 26
SHEET 1 D 6 HIS D 85 ASP D 89 0
SHEET 2 D 6 LYS D 94 LEU D 102 -1 O TYR D 98 N HIS D 85
SHEET 3 D 6 ARG D 51 GLY D 60 -1 N LEU D 54 O ALA D 99
SHEET 4 D 6 VAL D 39 LEU D 46 -1 N LEU D 44 O LEU D 53
SHEET 5 D 6 MET D 30 PHE D 35 -1 N ALA D 31 O LEU D 43
SHEET 6 D 6 VAL U 78 ARG U 81 -1 O ARG U 81 N SER D 32
SHEET 1 E 7 HIS E 85 ASP E 89 0
SHEET 2 E 7 LYS E 94 LEU E 102 -1 O GLN E 96 N GLY E 87
SHEET 3 E 7 ARG E 51 GLY E 60 -1 N LEU E 52 O ILE E 101
SHEET 4 E 7 VAL E 39 LEU E 46 -1 N LEU E 44 O LEU E 53
SHEET 5 E 7 MET E 30 PHE E 35 -1 N ALA E 31 O LEU E 43
SHEET 6 E 7 ARG V 26 ALA V 31 -1 O THR V 29 N LEU E 34
SHEET 7 E 7 GLY V 21 PHE V 23 -1 N GLY V 21 O VAL V 28
SHEET 1 F 6 HIS F 85 ASP F 89 0
SHEET 2 F 6 LYS F 94 LEU F 102 -1 O TYR F 98 N HIS F 85
SHEET 3 F 6 ARG F 51 GLY F 60 -1 N LEU F 54 O ALA F 99
SHEET 4 F 6 VAL F 39 LEU F 46 -1 N LEU F 44 O LEU F 53
SHEET 5 F 6 MET F 30 PHE F 35 -1 N LEU F 33 O VAL F 41
SHEET 6 F 6 VAL V 78 ARG V 80 -1 O ARG V 79 N LEU F 34
SHEET 1 G 7 HIS G 85 PHE G 88 0
SHEET 2 G 7 LYS G 94 LEU G 102 -1 O GLN G 96 N GLY G 87
SHEET 3 G 7 ARG G 51 GLY G 60 -1 N VAL G 58 O VAL G 95
SHEET 4 G 7 VAL G 39 LEU G 46 -1 N LEU G 44 O LEU G 53
SHEET 5 G 7 MET G 30 PHE G 35 -1 N ALA G 31 O LEU G 43
SHEET 6 G 7 SER W 27 ALA W 31 -1 O ALA W 31 N SER G 32
SHEET 7 G 7 GLY W 21 HIS W 22 -1 N GLY W 21 O VAL W 28
SHEET 1 H 6 HIS H 85 ASP H 89 0
SHEET 2 H 6 LYS H 94 LEU H 102 -1 O GLN H 96 N GLY H 87
SHEET 3 H 6 ARG H 51 GLY H 60 -1 N LEU H 54 O ALA H 99
SHEET 4 H 6 VAL H 39 LEU H 46 -1 N LEU H 44 O LEU H 53
SHEET 5 H 6 MET H 30 PHE H 35 -1 N PHE H 35 O VAL H 39
SHEET 6 H 6 VAL W 78 ARG W 80 -1 O ARG W 79 N LEU H 34
SHEET 1 I 7 HIS I 85 GLY I 87 0
SHEET 2 I 7 LYS I 94 LEU I 102 -1 O GLN I 96 N GLY I 87
SHEET 3 I 7 ARG I 51 GLY I 60 -1 N LEU I 54 O ALA I 99
SHEET 4 I 7 VAL I 39 LEU I 46 -1 N LEU I 44 O LEU I 53
SHEET 5 I 7 MET I 30 PHE I 35 -1 N PHE I 35 O VAL I 39
SHEET 6 I 7 ARG X 26 ARG X 30 -1 O THR X 29 N LEU I 34
SHEET 7 I 7 GLY X 21 PHE X 23 -1 N GLY X 21 O VAL X 28
SHEET 1 J 5 MET J 30 PHE J 35 0
SHEET 2 J 5 VAL J 39 LEU J 46 -1 O VAL J 41 N LEU J 33
SHEET 3 J 5 ARG J 51 GLY J 60 -1 O GLU J 55 N THR J 42
SHEET 4 J 5 LYS J 94 LEU J 102 -1 O ALA J 99 N LEU J 54
SHEET 5 J 5 HIS J 85 ASP J 89 -1 N GLY J 87 O GLN J 96
SHEET 1 K 7 HIS K 85 ASP K 89 0
SHEET 2 K 7 LYS K 94 LEU K 102 -1 O LYS K 94 N ASP K 89
SHEET 3 K 7 ARG K 51 GLY K 60 -1 N VAL K 58 O VAL K 95
SHEET 4 K 7 VAL K 39 LEU K 46 -1 N LEU K 44 O LEU K 53
SHEET 5 K 7 MET K 30 PHE K 35 -1 N LEU K 33 O VAL K 41
SHEET 6 K 7 ARG Y 26 ALA Y 31 -1 O THR Y 29 N LEU K 34
SHEET 7 K 7 VAL Y 20 PHE Y 23 -1 N PHE Y 23 O ARG Y 26
SHEET 1 L 6 HIS L 85 ASP L 89 0
SHEET 2 L 6 LYS L 94 LEU L 102 -1 O GLN L 96 N GLY L 87
SHEET 3 L 6 ARG L 51 GLY L 60 -1 N LEU L 54 O ALA L 99
SHEET 4 L 6 VAL L 39 LEU L 46 -1 N LEU L 44 O LEU L 53
SHEET 5 L 6 MET L 30 PHE L 35 -1 N ALA L 31 O LEU L 43
SHEET 6 L 6 VAL Y 78 ARG Y 80 -1 O ARG Y 79 N LEU L 34
CISPEP 1 GLU B 66 GLY B 67 0 0.62
CISPEP 2 GLU C 28 GLY C 29 0 -2.31
CISPEP 3 LEU D 129 PRO D 130 0 -1.86
CISPEP 4 PRO V 56 ARG V 57 0 -0.88
CISPEP 5 GLY X 35 GLU X 36 0 -1.21
CISPEP 6 GLY L 65 GLU L 66 0 -0.17
CISPEP 7 LEU L 129 PRO L 130 0 0.75
CISPEP 8 THR Y 17 GLU Y 18 0 0.73
CRYST1 96.313 124.973 228.126 90.00 90.00 90.00 P 21 21 21 48
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 0.010383 0.000000 0.000000 0.00000
SCALE2 0.000000 0.008002 0.000000 0.00000
SCALE3 0.000000 0.000000 0.004384 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
